data_8ZUS
# 
_entry.id   8ZUS 
# 
_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   8ZUS         pdb_00008zus 10.2210/pdb8zus/pdb 
WWPDB D_1300048422 ?            ?                   
# 
_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                        8ZUS 
_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' 25841.984 1   ? F99S,M153T,V163A,T203V ? 
'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    519 ? ?                      ? ? 
# 
_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
GIKANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSVQSALSKDPNEKRDHMVLLEFVTAAGITH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKRH
DFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGI
KANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSVQSALSKDPNEKRDHMVLLEFVTAAGITH
;
_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 VAL 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 GLU 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 VAL 200 203 203 VAL VAL 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 GLU 219 222 222 GLU GLU 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 176 576 576 HOH HOH A . 
D 3 HOH 177 577 577 HOH HOH A . 
D 3 HOH 178 578 578 HOH HOH A . 
D 3 HOH 179 579 579 HOH HOH A . 
D 3 HOH 180 580 580 HOH HOH A . 
D 3 HOH 181 581 581 HOH HOH A . 
D 3 HOH 182 582 582 HOH HOH A . 
D 3 HOH 183 583 583 HOH HOH A . 
D 3 HOH 184 584 584 HOH HOH A . 
D 3 HOH 185 585 585 HOH HOH A . 
D 3 HOH 186 586 586 HOH HOH A . 
D 3 HOH 187 587 587 HOH HOH A . 
D 3 HOH 188 588 588 HOH HOH A . 
D 3 HOH 189 589 589 HOH HOH A . 
D 3 HOH 190 590 590 HOH HOH A . 
D 3 HOH 191 591 591 HOH HOH A . 
D 3 HOH 192 592 592 HOH HOH A . 
D 3 HOH 193 593 593 HOH HOH A . 
D 3 HOH 194 594 594 HOH HOH A . 
D 3 HOH 195 595 595 HOH HOH A . 
D 3 HOH 196 596 596 HOH HOH A . 
D 3 HOH 197 597 597 HOH HOH A . 
D 3 HOH 198 598 598 HOH HOH A . 
D 3 HOH 199 599 599 HOH HOH A . 
D 3 HOH 200 600 600 HOH HOH A . 
D 3 HOH 201 601 601 HOH HOH A . 
D 3 HOH 202 602 602 HOH HOH A . 
D 3 HOH 203 603 603 HOH HOH A . 
D 3 HOH 204 604 604 HOH HOH A . 
D 3 HOH 205 605 605 HOH HOH A . 
D 3 HOH 206 606 606 HOH HOH A . 
D 3 HOH 207 607 607 HOH HOH A . 
D 3 HOH 208 608 608 HOH HOH A . 
D 3 HOH 209 609 609 HOH HOH A . 
D 3 HOH 210 610 610 HOH HOH A . 
D 3 HOH 211 611 611 HOH HOH A . 
D 3 HOH 212 612 612 HOH HOH A . 
D 3 HOH 213 613 613 HOH HOH A . 
D 3 HOH 214 614 614 HOH HOH A . 
D 3 HOH 215 615 615 HOH HOH A . 
D 3 HOH 216 616 616 HOH HOH A . 
D 3 HOH 217 617 617 HOH HOH A . 
D 3 HOH 218 618 618 HOH HOH A . 
D 3 HOH 219 619 619 HOH HOH A . 
D 3 HOH 220 620 620 HOH HOH A . 
D 3 HOH 221 621 621 HOH HOH A . 
D 3 HOH 222 622 622 HOH HOH A . 
D 3 HOH 223 623 623 HOH HOH A . 
D 3 HOH 224 624 624 HOH HOH A . 
D 3 HOH 225 625 625 HOH HOH A . 
D 3 HOH 226 626 626 HOH HOH A . 
D 3 HOH 227 627 627 HOH HOH A . 
D 3 HOH 228 628 628 HOH HOH A . 
D 3 HOH 229 629 629 HOH HOH A . 
D 3 HOH 230 630 630 HOH HOH A . 
D 3 HOH 231 631 631 HOH HOH A . 
D 3 HOH 232 632 632 HOH HOH A . 
D 3 HOH 233 633 633 HOH HOH A . 
D 3 HOH 234 634 634 HOH HOH A . 
D 3 HOH 235 635 635 HOH HOH A . 
D 3 HOH 236 636 636 HOH HOH A . 
D 3 HOH 237 637 637 HOH HOH A . 
D 3 HOH 238 638 638 HOH HOH A . 
D 3 HOH 239 639 639 HOH HOH A . 
D 3 HOH 240 640 640 HOH HOH A . 
D 3 HOH 241 641 641 HOH HOH A . 
D 3 HOH 242 642 642 HOH HOH A . 
D 3 HOH 243 643 643 HOH HOH A . 
D 3 HOH 244 644 644 HOH HOH A . 
D 3 HOH 245 645 645 HOH HOH A . 
D 3 HOH 246 646 646 HOH HOH A . 
D 3 HOH 247 647 647 HOH HOH A . 
D 3 HOH 248 648 648 HOH HOH A . 
D 3 HOH 249 649 649 HOH HOH A . 
D 3 HOH 250 650 650 HOH HOH A . 
D 3 HOH 251 651 651 HOH HOH A . 
D 3 HOH 252 652 652 HOH HOH A . 
D 3 HOH 253 653 653 HOH HOH A . 
D 3 HOH 254 654 654 HOH HOH A . 
D 3 HOH 255 655 655 HOH HOH A . 
D 3 HOH 256 656 656 HOH HOH A . 
D 3 HOH 257 657 657 HOH HOH A . 
D 3 HOH 258 658 658 HOH HOH A . 
D 3 HOH 259 659 659 HOH HOH A . 
D 3 HOH 260 660 660 HOH HOH A . 
D 3 HOH 261 661 661 HOH HOH A . 
D 3 HOH 262 662 662 HOH HOH A . 
D 3 HOH 263 663 663 HOH HOH A . 
D 3 HOH 264 664 664 HOH HOH A . 
D 3 HOH 265 665 665 HOH HOH A . 
D 3 HOH 266 666 666 HOH HOH A . 
D 3 HOH 267 667 667 HOH HOH A . 
D 3 HOH 268 668 668 HOH HOH A . 
D 3 HOH 269 669 669 HOH HOH A . 
D 3 HOH 270 670 670 HOH HOH A . 
D 3 HOH 271 671 671 HOH HOH A . 
D 3 HOH 272 672 672 HOH HOH A . 
D 3 HOH 273 673 673 HOH HOH A . 
D 3 HOH 274 674 674 HOH HOH A . 
D 3 HOH 275 675 675 HOH HOH A . 
D 3 HOH 276 676 676 HOH HOH A . 
D 3 HOH 277 677 677 HOH HOH A . 
D 3 HOH 278 678 678 HOH HOH A . 
D 3 HOH 279 679 679 HOH HOH A . 
D 3 HOH 280 680 680 HOH HOH A . 
D 3 HOH 281 681 681 HOH HOH A . 
D 3 HOH 282 682 682 HOH HOH A . 
D 3 HOH 283 683 683 HOH HOH A . 
D 3 HOH 284 684 684 HOH HOH A . 
D 3 HOH 285 685 685 HOH HOH A . 
D 3 HOH 286 686 686 HOH HOH A . 
D 3 HOH 287 687 687 HOH HOH A . 
D 3 HOH 288 688 688 HOH HOH A . 
D 3 HOH 289 689 689 HOH HOH A . 
D 3 HOH 290 690 690 HOH HOH A . 
D 3 HOH 291 691 691 HOH HOH A . 
D 3 HOH 292 692 692 HOH HOH A . 
D 3 HOH 293 693 693 HOH HOH A . 
D 3 HOH 294 694 694 HOH HOH A . 
D 3 HOH 295 695 695 HOH HOH A . 
D 3 HOH 296 696 696 HOH HOH A . 
D 3 HOH 297 697 697 HOH HOH A . 
D 3 HOH 298 698 698 HOH HOH A . 
D 3 HOH 299 699 699 HOH HOH A . 
D 3 HOH 300 700 700 HOH HOH A . 
D 3 HOH 301 701 701 HOH HOH A . 
D 3 HOH 302 702 702 HOH HOH A . 
D 3 HOH 303 703 703 HOH HOH A . 
D 3 HOH 304 704 704 HOH HOH A . 
D 3 HOH 305 705 705 HOH HOH A . 
D 3 HOH 306 706 706 HOH HOH A . 
D 3 HOH 307 707 707 HOH HOH A . 
D 3 HOH 308 708 708 HOH HOH A . 
D 3 HOH 309 709 709 HOH HOH A . 
D 3 HOH 310 710 710 HOH HOH A . 
D 3 HOH 311 711 711 HOH HOH A . 
D 3 HOH 312 712 712 HOH HOH A . 
D 3 HOH 313 713 713 HOH HOH A . 
D 3 HOH 314 714 714 HOH HOH A . 
D 3 HOH 315 715 715 HOH HOH A . 
D 3 HOH 316 716 716 HOH HOH A . 
D 3 HOH 317 717 717 HOH HOH A . 
D 3 HOH 318 718 718 HOH HOH A . 
D 3 HOH 319 719 719 HOH HOH A . 
D 3 HOH 320 720 720 HOH HOH A . 
D 3 HOH 321 721 721 HOH HOH A . 
D 3 HOH 322 722 722 HOH HOH A . 
D 3 HOH 323 723 723 HOH HOH A . 
D 3 HOH 324 724 724 HOH HOH A . 
D 3 HOH 325 725 725 HOH HOH A . 
D 3 HOH 326 726 726 HOH HOH A . 
D 3 HOH 327 727 727 HOH HOH A . 
D 3 HOH 328 728 728 HOH HOH A . 
D 3 HOH 329 729 729 HOH HOH A . 
D 3 HOH 330 730 730 HOH HOH A . 
D 3 HOH 331 731 731 HOH HOH A . 
D 3 HOH 332 732 732 HOH HOH A . 
D 3 HOH 333 733 733 HOH HOH A . 
D 3 HOH 334 734 734 HOH HOH A . 
D 3 HOH 335 735 735 HOH HOH A . 
D 3 HOH 336 736 736 HOH HOH A . 
D 3 HOH 337 737 737 HOH HOH A . 
D 3 HOH 338 738 738 HOH HOH A . 
D 3 HOH 339 739 739 HOH HOH A . 
D 3 HOH 340 740 740 HOH HOH A . 
D 3 HOH 341 741 741 HOH HOH A . 
D 3 HOH 342 742 742 HOH HOH A . 
D 3 HOH 343 743 743 HOH HOH A . 
D 3 HOH 344 744 744 HOH HOH A . 
D 3 HOH 345 745 745 HOH HOH A . 
D 3 HOH 346 746 746 HOH HOH A . 
D 3 HOH 347 747 747 HOH HOH A . 
D 3 HOH 348 748 748 HOH HOH A . 
D 3 HOH 349 749 749 HOH HOH A . 
D 3 HOH 350 750 750 HOH HOH A . 
D 3 HOH 351 751 751 HOH HOH A . 
D 3 HOH 352 752 752 HOH HOH A . 
D 3 HOH 353 753 753 HOH HOH A . 
D 3 HOH 354 754 754 HOH HOH A . 
D 3 HOH 355 755 755 HOH HOH A . 
D 3 HOH 356 756 756 HOH HOH A . 
D 3 HOH 357 757 757 HOH HOH A . 
D 3 HOH 358 758 758 HOH HOH A . 
D 3 HOH 359 759 759 HOH HOH A . 
D 3 HOH 360 760 760 HOH HOH A . 
D 3 HOH 361 761 761 HOH HOH A . 
D 3 HOH 362 762 762 HOH HOH A . 
D 3 HOH 363 763 763 HOH HOH A . 
D 3 HOH 364 764 764 HOH HOH A . 
D 3 HOH 365 765 765 HOH HOH A . 
D 3 HOH 366 766 766 HOH HOH A . 
D 3 HOH 367 767 767 HOH HOH A . 
D 3 HOH 368 768 768 HOH HOH A . 
D 3 HOH 369 769 769 HOH HOH A . 
D 3 HOH 370 770 770 HOH HOH A . 
D 3 HOH 371 771 771 HOH HOH A . 
D 3 HOH 372 772 772 HOH HOH A . 
D 3 HOH 373 773 773 HOH HOH A . 
D 3 HOH 374 774 774 HOH HOH A . 
D 3 HOH 375 775 775 HOH HOH A . 
D 3 HOH 376 776 776 HOH HOH A . 
D 3 HOH 377 777 777 HOH HOH A . 
D 3 HOH 378 778 778 HOH HOH A . 
D 3 HOH 379 779 779 HOH HOH A . 
D 3 HOH 380 780 780 HOH HOH A . 
D 3 HOH 381 781 781 HOH HOH A . 
D 3 HOH 382 782 782 HOH HOH A . 
D 3 HOH 383 783 783 HOH HOH A . 
D 3 HOH 384 784 784 HOH HOH A . 
D 3 HOH 385 785 785 HOH HOH A . 
D 3 HOH 386 786 786 HOH HOH A . 
D 3 HOH 387 787 787 HOH HOH A . 
D 3 HOH 388 788 788 HOH HOH A . 
D 3 HOH 389 789 789 HOH HOH A . 
D 3 HOH 390 790 790 HOH HOH A . 
D 3 HOH 391 791 791 HOH HOH A . 
D 3 HOH 392 792 792 HOH HOH A . 
D 3 HOH 393 793 793 HOH HOH A . 
D 3 HOH 394 794 794 HOH HOH A . 
D 3 HOH 395 795 795 HOH HOH A . 
D 3 HOH 396 796 796 HOH HOH A . 
D 3 HOH 397 797 797 HOH HOH A . 
D 3 HOH 398 798 798 HOH HOH A . 
D 3 HOH 399 799 799 HOH HOH A . 
D 3 HOH 400 800 800 HOH HOH A . 
D 3 HOH 401 801 801 HOH HOH A . 
D 3 HOH 402 802 802 HOH HOH A . 
D 3 HOH 403 803 803 HOH HOH A . 
D 3 HOH 404 804 804 HOH HOH A . 
D 3 HOH 405 805 805 HOH HOH A . 
D 3 HOH 406 806 806 HOH HOH A . 
D 3 HOH 407 807 807 HOH HOH A . 
D 3 HOH 408 808 808 HOH HOH A . 
D 3 HOH 409 809 809 HOH HOH A . 
D 3 HOH 410 810 810 HOH HOH A . 
D 3 HOH 411 812 812 HOH HOH A . 
D 3 HOH 412 813 813 HOH HOH A . 
D 3 HOH 413 814 814 HOH HOH A . 
D 3 HOH 414 815 815 HOH HOH A . 
D 3 HOH 415 816 816 HOH HOH A . 
D 3 HOH 416 817 817 HOH HOH A . 
D 3 HOH 417 818 818 HOH HOH A . 
D 3 HOH 418 819 819 HOH HOH A . 
D 3 HOH 419 820 820 HOH HOH A . 
D 3 HOH 420 821 821 HOH HOH A . 
D 3 HOH 421 822 822 HOH HOH A . 
D 3 HOH 422 823 823 HOH HOH A . 
D 3 HOH 423 824 824 HOH HOH A . 
D 3 HOH 424 825 825 HOH HOH A . 
D 3 HOH 425 826 826 HOH HOH A . 
D 3 HOH 426 827 827 HOH HOH A . 
D 3 HOH 427 828 828 HOH HOH A . 
D 3 HOH 428 829 829 HOH HOH A . 
D 3 HOH 429 830 830 HOH HOH A . 
D 3 HOH 430 831 831 HOH HOH A . 
D 3 HOH 431 832 832 HOH HOH A . 
D 3 HOH 432 833 833 HOH HOH A . 
D 3 HOH 433 834 834 HOH HOH A . 
D 3 HOH 434 835 835 HOH HOH A . 
D 3 HOH 435 836 836 HOH HOH A . 
D 3 HOH 436 837 837 HOH HOH A . 
D 3 HOH 437 838 838 HOH HOH A . 
D 3 HOH 438 839 839 HOH HOH A . 
D 3 HOH 439 840 840 HOH HOH A . 
D 3 HOH 440 841 841 HOH HOH A . 
D 3 HOH 441 842 842 HOH HOH A . 
D 3 HOH 442 843 843 HOH HOH A . 
D 3 HOH 443 844 844 HOH HOH A . 
D 3 HOH 444 845 845 HOH HOH A . 
D 3 HOH 445 846 846 HOH HOH A . 
D 3 HOH 446 847 847 HOH HOH A . 
D 3 HOH 447 848 848 HOH HOH A . 
D 3 HOH 448 849 849 HOH HOH A . 
D 3 HOH 449 850 850 HOH HOH A . 
D 3 HOH 450 851 851 HOH HOH A . 
D 3 HOH 451 852 852 HOH HOH A . 
D 3 HOH 452 853 853 HOH HOH A . 
D 3 HOH 453 854 854 HOH HOH A . 
D 3 HOH 454 855 855 HOH HOH A . 
D 3 HOH 455 856 856 HOH HOH A . 
D 3 HOH 456 857 857 HOH HOH A . 
D 3 HOH 457 858 858 HOH HOH A . 
D 3 HOH 458 859 859 HOH HOH A . 
D 3 HOH 459 860 860 HOH HOH A . 
D 3 HOH 460 861 861 HOH HOH A . 
D 3 HOH 461 862 862 HOH HOH A . 
D 3 HOH 462 863 863 HOH HOH A . 
D 3 HOH 463 864 864 HOH HOH A . 
D 3 HOH 464 865 865 HOH HOH A . 
D 3 HOH 465 866 866 HOH HOH A . 
D 3 HOH 466 867 867 HOH HOH A . 
D 3 HOH 467 868 868 HOH HOH A . 
D 3 HOH 468 869 869 HOH HOH A . 
D 3 HOH 469 870 870 HOH HOH A . 
D 3 HOH 470 871 871 HOH HOH A . 
D 3 HOH 471 872 872 HOH HOH A . 
D 3 HOH 472 873 873 HOH HOH A . 
D 3 HOH 473 874 874 HOH HOH A . 
D 3 HOH 474 875 875 HOH HOH A . 
D 3 HOH 475 876 876 HOH HOH A . 
D 3 HOH 476 877 877 HOH HOH A . 
D 3 HOH 477 878 878 HOH HOH A . 
D 3 HOH 478 879 879 HOH HOH A . 
D 3 HOH 479 880 880 HOH HOH A . 
D 3 HOH 480 881 881 HOH HOH A . 
D 3 HOH 481 882 882 HOH HOH A . 
D 3 HOH 482 883 883 HOH HOH A . 
D 3 HOH 483 884 884 HOH HOH A . 
D 3 HOH 484 885 885 HOH HOH A . 
D 3 HOH 485 886 886 HOH HOH A . 
D 3 HOH 486 887 887 HOH HOH A . 
D 3 HOH 487 888 888 HOH HOH A . 
D 3 HOH 488 889 889 HOH HOH A . 
D 3 HOH 489 890 890 HOH HOH A . 
D 3 HOH 490 891 891 HOH HOH A . 
D 3 HOH 491 892 892 HOH HOH A . 
D 3 HOH 492 893 893 HOH HOH A . 
D 3 HOH 493 894 894 HOH HOH A . 
D 3 HOH 494 895 895 HOH HOH A . 
D 3 HOH 495 896 896 HOH HOH A . 
D 3 HOH 496 897 897 HOH HOH A . 
D 3 HOH 497 898 898 HOH HOH A . 
D 3 HOH 498 899 899 HOH HOH A . 
D 3 HOH 499 900 900 HOH HOH A . 
D 3 HOH 500 901 901 HOH HOH A . 
D 3 HOH 501 902 902 HOH HOH A . 
D 3 HOH 502 903 903 HOH HOH A . 
D 3 HOH 503 904 904 HOH HOH A . 
D 3 HOH 504 905 905 HOH HOH A . 
D 3 HOH 505 906 906 HOH HOH A . 
D 3 HOH 506 907 907 HOH HOH A . 
D 3 HOH 507 908 908 HOH HOH A . 
D 3 HOH 508 909 909 HOH HOH A . 
D 3 HOH 509 910 910 HOH HOH A . 
D 3 HOH 510 911 911 HOH HOH A . 
D 3 HOH 511 912 912 HOH HOH A . 
D 3 HOH 512 913 913 HOH HOH A . 
D 3 HOH 513 914 914 HOH HOH A . 
D 3 HOH 514 915 915 HOH HOH A . 
D 3 HOH 515 916 916 HOH HOH A . 
D 3 HOH 516 917 917 HOH HOH A . 
D 3 HOH 517 918 918 HOH HOH A . 
D 3 HOH 518 919 919 HOH HOH A . 
D 3 HOH 519 920 920 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19.2_4158 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
# 
_cell.volume             215732.192 
_cell.length_a           50.720 
_cell.length_b           62.236 
_cell.length_c           68.343 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           8ZUS 
_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                         8ZUS 
_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                   8ZUS 
_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             2.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.06 
_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         2024-02-17 
_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                          9.22 
_reflns.entry_id                                       8ZUS 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.2 
_reflns.d_resolution_low                               46.02 
_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                                     68343 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.73 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.00 
_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                                0.118 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.109 
_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                                    1.20 
_reflns_shell.d_res_low                                     1.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.12 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10858 
_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                               6.34 
_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                               0.668 
_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                                  0.841 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.613 
_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                 15.6978 
_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                          0.1343 
_refine.B_iso_mean                               14.94 
_refine.ls_number_reflns_R_free                  3419 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_R_factor_R_work                       0.1327 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.20 
_refine.ls_number_reflns_obs                     68327 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.ls_number_reflns_R_work                  64908 
_refine.ls_d_res_low                             46.02 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1653 
_refine.overall_SU_ML                            0.1197 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.entry_id                                 8ZUS 
_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        1823 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             519 
_refine_hist.number_atoms_total               2344 
_refine_hist.d_res_high                       1.20 
_refine_hist.d_res_low                        46.02 
# 
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           2138 0.0066  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2939 0.9844  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     316  0.0930  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      392  0.0076  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 864  13.2876 ? ? ? 
# 
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' 1.20 1.22  2598 0.2198 98.14  0.2473 150 . . . . . . . 
'X-RAY DIFFRACTION' 1.22 1.23  2685 0.2062 99.93  0.2456 131 . . . . . . . 
'X-RAY DIFFRACTION' 1.23 1.25  2643 0.1887 99.96  0.2403 150 . . . . . . . 
'X-RAY DIFFRACTION' 1.25 1.27  2673 0.1825 99.93  0.2340 145 . . . . . . . 
'X-RAY DIFFRACTION' 1.27 1.30  2698 0.1757 100.00 0.2050 127 . . . . . . . 
'X-RAY DIFFRACTION' 1.30 1.32  2665 0.1578 100.00 0.1968 137 . . . . . . . 
'X-RAY DIFFRACTION' 1.32 1.35  2692 0.1587 99.96  0.2058 138 . . . . . . . 
'X-RAY DIFFRACTION' 1.35 1.37  2672 0.1497 99.96  0.1785 149 . . . . . . . 
'X-RAY DIFFRACTION' 1.37 1.40  2688 0.1471 99.96  0.1979 134 . . . . . . . 
'X-RAY DIFFRACTION' 1.40 1.44  2665 0.1484 99.93  0.1846 147 . . . . . . . 
'X-RAY DIFFRACTION' 1.44 1.47  2677 0.1452 100.00 0.1939 139 . . . . . . . 
'X-RAY DIFFRACTION' 1.47 1.51  2686 0.1398 100.00 0.1816 156 . . . . . . . 
'X-RAY DIFFRACTION' 1.51 1.56  2675 0.1389 99.96  0.1831 152 . . . . . . . 
'X-RAY DIFFRACTION' 1.56 1.61  2705 0.1272 100.00 0.1781 134 . . . . . . . 
'X-RAY DIFFRACTION' 1.61 1.66  2687 0.1214 100.00 0.1500 149 . . . . . . . 
'X-RAY DIFFRACTION' 1.66 1.73  2711 0.1190 100.00 0.1744 152 . . . . . . . 
'X-RAY DIFFRACTION' 1.73 1.81  2709 0.1166 100.00 0.1432 139 . . . . . . . 
'X-RAY DIFFRACTION' 1.81 1.90  2677 0.1180 100.00 0.1433 158 . . . . . . . 
'X-RAY DIFFRACTION' 1.90 2.02  2755 0.1126 100.00 0.1434 127 . . . . . . . 
'X-RAY DIFFRACTION' 2.02 2.18  2743 0.1153 100.00 0.1342 121 . . . . . . . 
'X-RAY DIFFRACTION' 2.18 2.40  2738 0.1224 100.00 0.1377 153 . . . . . . . 
'X-RAY DIFFRACTION' 2.40 2.75  2779 0.1309 100.00 0.1544 121 . . . . . . . 
'X-RAY DIFFRACTION' 2.75 3.46  2773 0.1228 100.00 0.1396 157 . . . . . . . 
'X-RAY DIFFRACTION' 3.46 46.02 2914 0.1283 99.64  0.1773 153 . . . . . . . 
# 
_struct.entry_id                     8ZUS 
_struct.title                        'Crystal structure of the F99S/M153T/V163A/T203V variant of GFP at pH 7.5' 
_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        8ZUS 
_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              8ZUS 
_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 8ZUS GYS A 64  ? UNP P42212 SER 65  chromophore           66  1 
1 8ZUS GYS A 64  ? UNP P42212 TYR 66  chromophore           66  2 
1 8ZUS GYS A 64  ? UNP P42212 GLY 67  chromophore           66  3 
1 8ZUS ARG A 77  ? UNP P42212 GLN 80  conflict              80  4 
1 8ZUS SER A 96  ? UNP P42212 PHE 99  'engineered mutation' 99  5 
1 8ZUS THR A 150 ? UNP P42212 MET 153 'engineered mutation' 153 6 
1 8ZUS ALA A 160 ? UNP P42212 VAL 163 'engineered mutation' 163 7 
1 8ZUS VAL A 200 ? UNP P42212 THR 203 'engineered mutation' 203 8 
# 
_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)'  10320 ? 
# 
_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 LYS A 2   ? THR A 8   ? LYS A 3   THR A 9   5 ? 7 
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 ? ? ? ? ? ? ? 1.332 ? ? 
covale2  covale both ? A GYS 64 C3 ? ? ? 1_555 A VAL 65 N  ? ? A GYS 66  A VAL 68  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
metalc1  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  A ? A MG  301 A HOH 800 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc2  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  301 A HOH 800 1_555 ? ? ? ? ? ? ? 2.220 ? ? 
metalc3  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  ? ? A MG  301 A HOH 816 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc4  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  301 A HOH 831 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc5  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  ? ? A MG  301 A HOH 860 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc6  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  A ? A MG  301 A HOH 894 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc7  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  301 A HOH 894 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc8  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  A ? A MG  301 A HOH 899 1_555 ? ? ? ? ? ? ? 2.500 ? ? 
metalc9  metalc ?    ? B MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  301 A HOH 899 1_555 ? ? ? ? ? ? ? 2.126 ? ? 
metalc10 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  A ? A MG  302 A HOH 589 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc11 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  302 A HOH 589 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc12 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 649 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc13 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  A ? A MG  302 A HOH 650 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc14 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  302 A HOH 650 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc15 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 667 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc16 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  ? ? A MG  302 A HOH 673 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc17 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  A ? A MG  302 A HOH 747 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc18 metalc ?    ? C MG  .  MG ? ? ? 1_555 D HOH .  O  B ? A MG  302 A HOH 747 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
# 
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  O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 800 ? 1_555 50.9  ? 
2  O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 816 ? 1_555 97.3  ? 
3  O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 816 ? 1_555 57.6  ? 
4  O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 831 ? 1_555 84.5  ? 
5  O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 831 ? 1_555 113.3 ? 
6  O ? D HOH . ? A HOH 816 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 831 ? 1_555 89.9  ? 
7  O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 860 ? 1_555 83.6  ? 
8  O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 860 ? 1_555 56.7  ? 
9  O ? D HOH . ? A HOH 816 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 860 ? 1_555 89.4  ? 
10 O B D HOH . ? A HOH 831 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O ? D HOH . ? A HOH 860 ? 1_555 167.9 ? 
11 O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 894 ? 1_555 178.3 ? 
12 O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 894 ? 1_555 127.7 ? 
13 O ? D HOH . ? A HOH 816 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 894 ? 1_555 81.0  ? 
14 O B D HOH . ? A HOH 831 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 894 ? 1_555 95.5  ? 
15 O ? D HOH . ? A HOH 860 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 894 ? 1_555 96.4  ? 
16 O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 894 ? 1_555 149.8 ? 
17 O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 894 ? 1_555 148.5 ? 
18 O ? D HOH . ? A HOH 816 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 894 ? 1_555 112.9 ? 
19 O B D HOH . ? A HOH 831 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 894 ? 1_555 95.7  ? 
20 O ? D HOH . ? A HOH 860 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 894 ? 1_555 95.7  ? 
21 O A D HOH . ? A HOH 894 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 894 ? 1_555 31.9  ? 
22 O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 99.5  ? 
23 O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 130.5 ? 
24 O ? D HOH . ? A HOH 816 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 161.6 ? 
25 O B D HOH . ? A HOH 831 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 99.1  ? 
26 O ? D HOH . ? A HOH 860 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 85.0  ? 
27 O A D HOH . ? A HOH 894 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 82.2  ? 
28 O B D HOH . ? A HOH 894 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O A D HOH . ? A HOH 899 ? 1_555 50.6  ? 
29 O A D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 52.7  ? 
30 O B D HOH . ? A HOH 800 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 84.1  ? 
31 O ? D HOH . ? A HOH 816 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 141.7 ? 
32 O B D HOH . ? A HOH 831 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 107.5 ? 
33 O ? D HOH . ? A HOH 860 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 66.5  ? 
34 O A D HOH . ? A HOH 894 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 128.8 ? 
35 O B D HOH . ? A HOH 894 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 99.3  ? 
36 O A D HOH . ? A HOH 899 ? 1_555 MG ? B MG . ? A MG 301 ? 1_555 O B D HOH . ? A HOH 899 ? 1_555 49.9  ? 
37 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 589 ? 1_555 27.9  ? 
38 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 649 ? 1_555 90.3  ? 
39 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 649 ? 1_555 85.8  ? 
40 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 650 ? 1_555 89.2  ? 
41 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 650 ? 1_555 61.5  ? 
42 O ? D HOH . ? A HOH 649 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 650 ? 1_555 86.5  ? 
43 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 650 ? 1_555 123.5 ? 
44 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 650 ? 1_555 95.7  ? 
45 O ? D HOH . ? A HOH 649 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 650 ? 1_555 85.5  ? 
46 O A D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 650 ? 1_555 34.4  ? 
47 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 667 ? 1_555 87.2  ? 
48 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 667 ? 1_555 115.0 ? 
49 O ? D HOH . ? A HOH 649 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 667 ? 1_555 94.5  ? 
50 O A D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 667 ? 1_555 176.3 ? 
51 O B D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 667 ? 1_555 149.3 ? 
52 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 673 ? 1_555 93.1  ? 
53 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 673 ? 1_555 94.7  ? 
54 O ? D HOH . ? A HOH 649 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 673 ? 1_555 173.5 ? 
55 O A D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 673 ? 1_555 88.1  ? 
56 O B D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 673 ? 1_555 88.0  ? 
57 O ? D HOH . ? A HOH 667 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O ? D HOH . ? A HOH 673 ? 1_555 91.2  ? 
58 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 171.4 ? 
59 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 145.2 ? 
60 O ? D HOH . ? A HOH 649 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 94.0  ? 
61 O A D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 83.7  ? 
62 O B D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 49.6  ? 
63 O ? D HOH . ? A HOH 667 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 99.8  ? 
64 O ? D HOH . ? A HOH 673 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O A D HOH . ? A HOH 747 ? 1_555 82.0  ? 
65 O A D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 148.2 ? 
66 O B D HOH . ? A HOH 589 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 173.4 ? 
67 O ? D HOH . ? A HOH 649 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 89.2  ? 
68 O A D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 122.5 ? 
69 O B D HOH . ? A HOH 650 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 88.1  ? 
70 O ? D HOH . ? A HOH 667 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 61.1  ? 
71 O ? D HOH . ? A HOH 673 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 90.8  ? 
72 O A D HOH . ? A HOH 747 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O B D HOH . ? A HOH 747 ? 1_555 39.5  ? 
# 
_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       7.75 
# 
_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 THR A 222 ? O THR A 225 N SER A 199 ? N SER A 202 
AA1 5  6  O VAL A 200 ? O VAL A 203 N HIS A 145 ? N HIS A 148 
AA1 6  7  N ASP A 152 ? N ASP A 155 O GLY A 157 ? O GLY A 160 
AA1 7  8  N PHE A 162 ? N PHE A 165 O HIS A 178 ? O HIS A 181 
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                   8ZUS 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     103 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -152.88 
_pdbx_validate_torsion.psi             -158.04 
# 
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 502 ? 6.02 . 
2 1 O ? A HOH 598 ? 6.73 . 
3 1 O ? A HOH 730 ? 5.91 . 
4 1 O A A HOH 899 ? 6.10 . 
5 1 O ? A HOH 903 ? 6.22 . 
6 1 O ? A HOH 908 ? 6.86 . 
# 
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                    8ZUS 
_atom_sites.fract_transf_matrix[1][1]   0.019716 
_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]   0.016068 
_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]   0.014632 
_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   ? -3.79200  20.57700  84.70500 0.430 15.26378 ? 2   SER A N   1 
ATOM   2    N  N   B SER A 1 1   ? -3.26300  23.49400  83.99900 0.570 23.24378 ? 2   SER A N   1 
ATOM   3    C  CA  A SER A 1 1   ? -2.35300  20.51000  84.94600 0.430 16.33378 ? 2   SER A CA  1 
ATOM   4    C  CA  B SER A 1 1   ? -1.97800  23.09300  84.55800 0.570 22.11170 ? 2   SER A CA  1 
ATOM   5    C  C   A SER A 1 1   ? -1.62300  21.54200  84.10000 0.430 15.52378 ? 2   SER A C   1 
ATOM   6    C  C   B SER A 1 1   ? -0.88100  23.17700  83.50900 0.570 23.21378 ? 2   SER A C   1 
ATOM   7    O  O   A SER A 1 1   ? -2.11800  21.96600  83.05700 0.430 12.65378 ? 2   SER A O   1 
ATOM   8    O  O   B SER A 1 1   ? -1.14900  23.27500  82.31500 0.570 23.56450 ? 2   SER A O   1 
ATOM   9    C  CB  A SER A 1 1   ? -1.81800  19.11600  84.61100 0.430 12.82378 ? 2   SER A CB  1 
ATOM   10   C  CB  B SER A 1 1   ? -2.05000  21.66400  85.09500 0.570 26.77378 ? 2   SER A CB  1 
ATOM   11   O  OG  A SER A 1 1   ? -1.69000  18.95800  83.21200 0.430 9.96378  ? 2   SER A OG  1 
ATOM   12   O  OG  B SER A 1 1   ? -2.24200  20.74000  84.03800 0.570 28.01378 ? 2   SER A OG  1 
ATOM   13   N  N   A LYS A 1 2   ? -0.43500  21.94400  84.55100 0.430 9.74378  ? 3   LYS A N   1 
ATOM   14   N  N   B LYS A 1 2   ? 0.36200   23.10800  83.98200 0.570 22.15381 ? 3   LYS A N   1 
ATOM   15   C  CA  A LYS A 1 2   ? 0.41400   22.77700  83.70800 0.430 11.83378 ? 3   LYS A CA  1 
ATOM   16   C  CA  B LYS A 1 2   ? 1.51600   23.23000  83.10200 0.570 21.20106 ? 3   LYS A CA  1 
ATOM   17   C  C   A LYS A 1 2   ? 0.71100   22.07800  82.38800 0.430 11.98378 ? 3   LYS A C   1 
ATOM   18   C  C   B LYS A 1 2   ? 1.45700   22.21000  81.97000 0.570 17.86382 ? 3   LYS A C   1 
ATOM   19   O  O   A LYS A 1 2   ? 0.65100   22.69400  81.31600 0.430 10.50378 ? 3   LYS A O   1 
ATOM   20   O  O   B LYS A 1 2   ? 1.58100   22.56400  80.79200 0.570 16.97687 ? 3   LYS A O   1 
ATOM   21   C  CB  A LYS A 1 2   ? 1.70600   23.09800  84.45800 0.430 11.72378 ? 3   LYS A CB  1 
ATOM   22   C  CB  B LYS A 1 2   ? 2.78100   23.05200  83.93900 0.570 20.38378 ? 3   LYS A CB  1 
ATOM   23   C  CG  A LYS A 1 2   ? 2.66900   23.98900  83.71600 0.430 17.10378 ? 3   LYS A CG  1 
ATOM   24   C  CG  B LYS A 1 2   ? 4.09500   23.11200  83.18500 0.570 27.11378 ? 3   LYS A CG  1 
ATOM   25   C  CD  A LYS A 1 2   ? 3.88700   24.27900  84.57500 0.430 20.05378 ? 3   LYS A CD  1 
ATOM   26   C  CD  B LYS A 1 2   ? 5.25300   22.81600  84.13800 0.570 30.67378 ? 3   LYS A CD  1 
ATOM   27   C  CE  A LYS A 1 2   ? 4.92900   25.07300  83.81000 0.430 24.57378 ? 3   LYS A CE  1 
ATOM   28   C  CE  B LYS A 1 2   ? 6.60000   22.84700  83.43800 0.570 46.19378 ? 3   LYS A CE  1 
ATOM   29   N  NZ  A LYS A 1 2   ? 6.17300   25.24700  84.60900 0.430 29.89378 ? 3   LYS A NZ  1 
ATOM   30   N  NZ  B LYS A 1 2   ? 7.70000   22.36800  84.31900 0.570 53.26378 ? 3   LYS A NZ  1 
ATOM   31   N  N   A GLY A 1 3   ? 1.00700   20.77800  82.44700 0.430 9.20378  ? 4   GLY A N   1 
ATOM   32   N  N   B GLY A 1 3   ? 1.23400   20.93800  82.30700 0.570 16.05044 ? 4   GLY A N   1 
ATOM   33   C  CA  A GLY A 1 3   ? 1.36200   20.04800  81.24100 0.430 7.52378  ? 4   GLY A CA  1 
ATOM   34   C  CA  B GLY A 1 3   ? 1.33200   19.89200  81.30000 0.570 14.32129 ? 4   GLY A CA  1 
ATOM   35   C  C   A GLY A 1 3   ? 0.24500   19.99500  80.22000 0.430 8.01378  ? 4   GLY A C   1 
ATOM   36   C  C   B GLY A 1 3   ? 0.25000   19.98500  80.24100 0.570 12.70531 ? 4   GLY A C   1 
ATOM   37   O  O   A GLY A 1 3   ? 0.49900   19.84900  79.02200 0.430 8.86378  ? 4   GLY A O   1 
ATOM   38   O  O   B GLY A 1 3   ? 0.53100   19.94000  79.04000 0.570 12.86322 ? 4   GLY A O   1 
ATOM   39   N  N   . GLU A 1 4   ? -1.00300  20.12300  80.66800 1.000 11.68940 ? 5   GLU A N   1 
ATOM   40   C  CA  A GLU A 1 4   ? -2.11900  20.13100  79.72900 0.340 11.27378 ? 5   GLU A CA  1 
ATOM   41   C  CA  B GLU A 1 4   ? -2.10900  20.12300  79.71700 0.320 12.28378 ? 5   GLU A CA  1 
ATOM   42   C  CA  C GLU A 1 4   ? -2.13600  20.14800  79.74800 0.340 14.85378 ? 5   GLU A CA  1 
ATOM   43   C  C   . GLU A 1 4   ? -1.98600  21.25900  78.70700 1.000 11.50516 ? 5   GLU A C   1 
ATOM   44   O  O   . GLU A 1 4   ? -2.36100  21.09600  77.53700 1.000 11.00510 ? 5   GLU A O   1 
ATOM   45   C  CB  A GLU A 1 4   ? -3.41700  20.23600  80.52800 0.340 26.38378 ? 5   GLU A CB  1 
ATOM   46   C  CB  B GLU A 1 4   ? -3.43100  20.19500  80.48100 0.320 12.70378 ? 5   GLU A CB  1 
ATOM   47   C  CB  C GLU A 1 4   ? -3.45200  20.32000  80.52000 0.340 28.69378 ? 5   GLU A CB  1 
ATOM   48   C  CG  A GLU A 1 4   ? -4.63300  20.71100  79.78000 0.340 31.01378 ? 5   GLU A CG  1 
ATOM   49   C  CG  B GLU A 1 4   ? -4.66200  19.91100  79.65800 0.320 5.59378  ? 5   GLU A CG  1 
ATOM   50   C  CG  C GLU A 1 4   ? -3.61600  21.68600  81.17800 0.340 24.49378 ? 5   GLU A CG  1 
ATOM   51   C  CD  A GLU A 1 4   ? -5.77700  21.00100  80.72800 0.340 27.66378 ? 5   GLU A CD  1 
ATOM   52   C  CD  B GLU A 1 4   ? -5.23200  21.14900  78.97700 0.320 8.65378  ? 5   GLU A CD  1 
ATOM   53   C  CD  C GLU A 1 4   ? -4.92600  21.84100  81.92800 0.340 39.90378 ? 5   GLU A CD  1 
ATOM   54   O  OE1 A GLU A 1 4   ? -5.68800  20.58100  81.90300 0.340 20.16378 ? 5   GLU A OE1 1 
ATOM   55   O  OE1 B GLU A 1 4   ? -4.85900  22.28200  79.35300 0.320 9.52378  ? 5   GLU A OE1 1 
ATOM   56   O  OE1 C GLU A 1 4   ? -5.16200  21.07200  82.88200 0.340 42.08378 ? 5   GLU A OE1 1 
ATOM   57   O  OE2 A GLU A 1 4   ? -6.75200  21.65500  80.31000 0.340 18.25378 ? 5   GLU A OE2 1 
ATOM   58   O  OE2 B GLU A 1 4   ? -6.06000  20.98400  78.05600 0.320 9.56378  ? 5   GLU A OE2 1 
ATOM   59   O  OE2 C GLU A 1 4   ? -5.71800  22.73500  81.56100 0.340 23.19378 ? 5   GLU A OE2 1 
ATOM   60   N  N   . GLU A 1 5   ? -1.43800  22.40200  79.11700 1.000 11.16302 ? 6   GLU A N   1 
ATOM   61   C  CA  . GLU A 1 5   ? -1.33000  23.53900  78.21500 1.000 12.55792 ? 6   GLU A CA  1 
ATOM   62   C  C   . GLU A 1 5   ? -0.37800  23.28900  77.06100 1.000 10.70770 ? 6   GLU A C   1 
ATOM   63   O  O   . GLU A 1 5   ? -0.44900  23.99800  76.05000 1.000 11.08669 ? 6   GLU A O   1 
ATOM   64   C  CB  . GLU A 1 5   ? -0.90900  24.76700  79.01300 1.000 20.84839 ? 6   GLU A CB  1 
ATOM   65   C  CG  . GLU A 1 5   ? -1.94500  25.13500  80.06800 1.000 28.16378 ? 6   GLU A CG  1 
ATOM   66   C  CD  . GLU A 1 5   ? -1.47600  26.20600  81.02100 1.000 46.67378 ? 6   GLU A CD  1 
ATOM   67   O  OE1 . GLU A 1 5   ? -0.70000  27.08500  80.59200 1.000 41.69378 ? 6   GLU A OE1 1 
ATOM   68   O  OE2 . GLU A 1 5   ? -1.88600  26.16100  82.20200 1.000 25.17378 ? 6   GLU A OE2 1 
ATOM   69   N  N   . LEU A 1 6   ? 0.50600   22.30100  77.18800 1.000 9.54440  ? 7   LEU A N   1 
ATOM   70   C  CA  . LEU A 1 6   ? 1.41400   21.96200  76.10200 1.000 9.05487  ? 7   LEU A CA  1 
ATOM   71   C  C   . LEU A 1 6   ? 0.71700   21.27600  74.94400 1.000 8.56270  ? 7   LEU A C   1 
ATOM   72   O  O   . LEU A 1 6   ? 1.34600   21.07200  73.90800 1.000 9.57335  ? 7   LEU A O   1 
ATOM   73   C  CB  . LEU A 1 6   ? 2.53500   21.05000  76.60700 1.000 9.44439  ? 7   LEU A CB  1 
ATOM   74   C  CG  . LEU A 1 6   ? 3.37700   21.68400  77.71700 1.000 10.44188 ? 7   LEU A CG  1 
ATOM   75   C  CD1 . LEU A 1 6   ? 4.35400   20.65900  78.26100 1.000 11.35778 ? 7   LEU A CD1 1 
ATOM   76   C  CD2 . LEU A 1 6   ? 4.09700   22.92700  77.21000 1.000 12.60003 ? 7   LEU A CD2 1 
ATOM   77   N  N   . PHE A 1 7   ? -0.55800  20.91900  75.08900 1.000 7.83367  ? 8   PHE A N   1 
ATOM   78   C  CA  . PHE A 1 7   ? -1.25400  20.08100  74.11700 1.000 8.63113  ? 8   PHE A CA  1 
ATOM   79   C  C   . PHE A 1 7   ? -2.45100  20.76900  73.47600 1.000 8.86011  ? 8   PHE A C   1 
ATOM   80   O  O   . PHE A 1 7   ? -3.24200  20.10000  72.79700 1.000 9.60493  ? 8   PHE A O   1 
ATOM   81   C  CB  . PHE A 1 7   ? -1.68300  18.76100  74.77800 1.000 8.35215  ? 8   PHE A CB  1 
ATOM   82   C  CG  . PHE A 1 7   ? -0.52800  17.87000  75.10400 1.000 7.88894  ? 8   PHE A CG  1 
ATOM   83   C  CD1 . PHE A 1 7   ? -0.04000  16.98100  74.15200 1.000 7.81261  ? 8   PHE A CD1 1 
ATOM   84   C  CD2 . PHE A 1 7   ? 0.13400   17.97700  76.33200 1.000 8.62587  ? 8   PHE A CD2 1 
ATOM   85   C  CE1 . PHE A 1 7   ? 1.05700   16.18000  74.43000 1.000 8.19424  ? 8   PHE A CE1 1 
ATOM   86   C  CE2 . PHE A 1 7   ? 1.24500   17.17100  76.61600 1.000 8.02317  ? 8   PHE A CE2 1 
ATOM   87   C  CZ  . PHE A 1 7   ? 1.69100   16.26100  75.64900 1.000 8.61008  ? 8   PHE A CZ  1 
ATOM   88   N  N   . THR A 1 8   ? -2.61300  22.07600  73.66400 1.000 8.97328  ? 9   THR A N   1 
ATOM   89   C  CA  . THR A 1 8   ? -3.78700  22.75500  73.12000 1.000 10.50504 ? 9   THR A CA  1 
ATOM   90   C  C   . THR A 1 8   ? -3.70700  22.95900  71.61500 1.000 10.66559 ? 9   THR A C   1 
ATOM   91   O  O   . THR A 1 8   ? -4.73000  23.26800  70.99700 1.000 12.17103 ? 9   THR A O   1 
ATOM   92   C  CB  . THR A 1 8   ? -4.00000  24.08400  73.84300 1.000 12.29736 ? 9   THR A CB  1 
ATOM   93   O  OG1 . THR A 1 8   ? -2.78900  24.82300  73.77400 1.000 13.22116 ? 9   THR A OG1 1 
ATOM   94   C  CG2 . THR A 1 8   ? -4.34500  23.85300  75.31200 1.000 13.75543 ? 9   THR A CG2 1 
ATOM   95   N  N   . GLY A 1 9   ? -2.52900  22.79500  71.02100 1.000 9.95498  ? 10  GLY A N   1 
ATOM   96   C  CA  . GLY A 1 9   ? -2.36800  22.91000  69.58800 1.000 11.22092 ? 10  GLY A CA  1 
ATOM   97   C  C   . GLY A 1 9   ? -1.80800  21.63300  68.99500 1.000 9.78127  ? 10  GLY A C   1 
ATOM   98   O  O   . GLY A 1 9   ? -1.77500  20.58300  69.65400 1.000 10.69191 ? 10  GLY A O   1 
ATOM   99   N  N   . VAL A 1 10  ? -1.38300  21.70800  67.73900 1.000 9.68916  ? 11  VAL A N   1 
ATOM   100  C  CA  . VAL A 1 10  ? -0.80400  20.55800  67.05200 1.000 9.33648  ? 11  VAL A CA  1 
ATOM   101  C  C   . VAL A 1 10  ? 0.63900   20.41400  67.50700 1.000 9.12067  ? 11  VAL A C   1 
ATOM   102  O  O   . VAL A 1 10  ? 1.39800   21.38800  67.49300 1.000 11.40515 ? 11  VAL A O   1 
ATOM   103  C  CB  . VAL A 1 10  ? -0.86500  20.76700  65.53300 1.000 9.99446  ? 11  VAL A CB  1 
ATOM   104  C  CG1 . VAL A 1 10  ? -0.19100  19.63100  64.81100 1.000 12.15524 ? 11  VAL A CG1 1 
ATOM   105  C  CG2 . VAL A 1 10  ? -2.30700  20.90600  65.08500 1.000 11.32356 ? 11  VAL A CG2 1 
ATOM   106  N  N   . VAL A 1 11  ? 1.03000   19.20700  67.89800 1.000 8.51533  ? 12  VAL A N   1 
ATOM   107  C  CA  . VAL A 1 11  ? 2.34500   18.95400  68.47200 1.000 8.33373  ? 12  VAL A CA  1 
ATOM   108  C  C   . VAL A 1 11  ? 3.05700   17.94200  67.58200 1.000 7.77840  ? 12  VAL A C   1 
ATOM   109  O  O   . VAL A 1 11  ? 2.50100   16.87100  67.31900 1.000 7.98106  ? 12  VAL A O   1 
ATOM   110  C  CB  . VAL A 1 11  ? 2.24400   18.42500  69.91400 1.000 8.02580  ? 12  VAL A CB  1 
ATOM   111  C  CG1 . VAL A 1 11  ? 3.60800   18.06900  70.44500 1.000 8.96275  ? 12  VAL A CG1 1 
ATOM   112  C  CG2 . VAL A 1 11  ? 1.56200   19.42600  70.81100 1.000 8.65745  ? 12  VAL A CG2 1 
ATOM   113  N  N   . PRO A 1 12  ? 4.28500   18.22500  67.12300 1.000 7.55469  ? 13  PRO A N   1 
ATOM   114  C  CA  . PRO A 1 12  ? 5.02300   17.22900  66.33200 1.000 7.65207  ? 13  PRO A CA  1 
ATOM   115  C  C   . PRO A 1 12  ? 5.40100   16.06100  67.22000 1.000 7.41257  ? 13  PRO A C   1 
ATOM   116  O  O   . PRO A 1 12  ? 5.66200   16.22600  68.41200 1.000 7.55732  ? 13  PRO A O   1 
ATOM   117  C  CB  . PRO A 1 12  ? 6.28700   17.97800  65.87900 1.000 9.82075  ? 13  PRO A CB  1 
ATOM   118  C  CG  . PRO A 1 12  ? 6.14800   19.34600  66.36000 1.000 11.99469 ? 13  PRO A CG  1 
ATOM   119  C  CD  . PRO A 1 12  ? 5.07100   19.45400  67.35400 1.000 8.75483  ? 13  PRO A CD  1 
ATOM   120  N  N   . ILE A 1 13  ? 5.42200   14.86900  66.61400 1.000 6.80986  ? 14  ILE A N   1 
ATOM   121  C  CA  . ILE A 1 13  ? 5.73200   13.62300  67.31100 1.000 6.94146  ? 14  ILE A CA  1 
ATOM   122  C  C   . ILE A 1 13  ? 6.85900   12.89900  66.59300 1.000 6.88882  ? 14  ILE A C   1 
ATOM   123  O  O   . ILE A 1 13  ? 6.88100   12.81000  65.35900 1.000 7.08095  ? 14  ILE A O   1 
ATOM   124  C  CB  . ILE A 1 13  ? 4.51300   12.68200  67.35600 1.000 6.43087  ? 14  ILE A CB  1 
ATOM   125  C  CG1 . ILE A 1 13  ? 3.33200   13.37100  68.04400 1.000 7.41520  ? 14  ILE A CG1 1 
ATOM   126  C  CG2 . ILE A 1 13  ? 4.86600   11.38500  68.05300 1.000 7.34151  ? 14  ILE A CG2 1 
ATOM   127  C  CD1 . ILE A 1 13  ? 2.03900   12.60400  67.88600 1.000 7.92842  ? 14  ILE A CD1 1 
ATOM   128  N  N   . LEU A 1 14  ? 7.78000   12.35100  67.37800 1.000 7.12043  ? 15  LEU A N   1 
ATOM   129  C  CA  . LEU A 1 14  ? 8.78600   11.42200  66.88200 1.000 6.54931  ? 15  LEU A CA  1 
ATOM   130  C  C   . LEU A 1 14  ? 8.69200   10.12000  67.66100 1.000 6.42297  ? 15  LEU A C   1 
ATOM   131  O  O   . LEU A 1 14  ? 8.51900   10.13200  68.88100 1.000 6.82302  ? 15  LEU A O   1 
ATOM   132  C  CB  . LEU A 1 14  ? 10.19500  11.98000  67.09400 1.000 7.06516  ? 15  LEU A CB  1 
ATOM   133  C  CG  . LEU A 1 14  ? 10.41100  13.31000  66.37700 1.000 7.72313  ? 15  LEU A CG  1 
ATOM   134  C  CD1 . LEU A 1 14  ? 11.76300  13.90300  66.79000 1.000 8.48112  ? 15  LEU A CD1 1 
ATOM   135  C  CD2 . LEU A 1 14  ? 10.33000  13.11200  64.86400 1.000 8.39426  ? 15  LEU A CD2 1 
ATOM   136  N  N   . VAL A 1 15  ? 8.83900   8.99700   66.96200 1.000 6.72564  ? 16  VAL A N   1 
ATOM   137  C  CA  . VAL A 1 15  ? 8.85500   7.68800   67.60100 1.000 6.34665  ? 16  VAL A CA  1 
ATOM   138  C  C   . VAL A 1 15  ? 10.11900  6.97400   67.15400 1.000 6.44929  ? 16  VAL A C   1 
ATOM   139  O  O   . VAL A 1 15  ? 10.44800  6.98600   65.96800 1.000 6.84934  ? 16  VAL A O   1 
ATOM   140  C  CB  . VAL A 1 15  ? 7.60400   6.86200   67.22600 1.000 7.12306  ? 16  VAL A CB  1 
ATOM   141  C  CG1 . VAL A 1 15  ? 7.66300   5.46700   67.87800 1.000 7.04147  ? 16  VAL A CG1 1 
ATOM   142  C  CG2 . VAL A 1 15  ? 6.32600   7.62000   67.62000 1.000 7.23097  ? 16  VAL A CG2 1 
ATOM   143  N  N   . GLU A 1 16  ? 10.84500  6.38600   68.10000 1.000 6.32559  ? 17  GLU A N   1 
ATOM   144  C  CA  A GLU A 1 16  ? 12.05200  5.63000   67.78000 0.650 6.73354  ? 17  GLU A CA  1 
ATOM   145  C  CA  B GLU A 1 16  ? 12.06500  5.64000   67.79800 0.350 6.55378  ? 17  GLU A CA  1 
ATOM   146  C  C   . GLU A 1 16  ? 12.02800  4.33900   68.58100 1.000 6.77302  ? 17  GLU A C   1 
ATOM   147  O  O   . GLU A 1 16  ? 11.92700  4.37100   69.80800 1.000 8.22319  ? 17  GLU A O   1 
ATOM   148  C  CB  A GLU A 1 16  ? 13.31200  6.45000   68.08900 0.650 7.50205  ? 17  GLU A CB  1 
ATOM   149  C  CB  B GLU A 1 16  ? 13.30200  6.44700   68.20200 0.350 9.28378  ? 17  GLU A CB  1 
ATOM   150  C  CG  A GLU A 1 16  ? 13.47600  7.70400   67.20500 0.650 8.39690  ? 17  GLU A CG  1 
ATOM   151  C  CG  B GLU A 1 16  ? 13.58400  7.65100   67.31300 0.350 10.27378 ? 17  GLU A CG  1 
ATOM   152  C  CD  A GLU A 1 16  ? 13.73400  7.38300   65.72700 0.650 8.40742  ? 17  GLU A CD  1 
ATOM   153  C  CD  B GLU A 1 16  ? 14.15700  7.26100   65.96200 0.350 6.57378  ? 17  GLU A CD  1 
ATOM   154  O  OE1 A GLU A 1 16  ? 14.24300  6.28600   65.42200 0.650 9.29174  ? 17  GLU A OE1 1 
ATOM   155  O  OE1 B GLU A 1 16  ? 15.17300  6.53200   65.92600 0.350 8.09378  ? 17  GLU A OE1 1 
ATOM   156  O  OE2 A GLU A 1 16  ? 13.44100  8.24200   64.86500 0.650 9.94971  ? 17  GLU A OE2 1 
ATOM   157  O  OE2 B GLU A 1 16  ? 13.59800  7.68900   64.93800 0.350 8.07378  ? 17  GLU A OE2 1 
ATOM   158  N  N   . LEU A 1 17  ? 12.11600  3.20400   67.88300 1.000 7.03357  ? 18  LEU A N   1 
ATOM   159  C  CA  . LEU A 1 17  ? 12.05300  1.90600   68.53400 1.000 6.74143  ? 18  LEU A CA  1 
ATOM   160  C  C   . LEU A 1 17  ? 13.23500  1.06900   68.08300 1.000 7.05989  ? 18  LEU A C   1 
ATOM   161  O  O   . LEU A 1 17  ? 13.55800  1.02800   66.89200 1.000 7.80998  ? 18  LEU A O   1 
ATOM   162  C  CB  . LEU A 1 17  ? 10.73600  1.19300   68.18300 1.000 6.99936  ? 18  LEU A CB  1 
ATOM   163  C  CG  . LEU A 1 17  ? 10.59800  -0.24400  68.72400 1.000 7.52047  ? 18  LEU A CG  1 
ATOM   164  C  CD1 . LEU A 1 17  ? 9.15100   -0.52100  69.13500 1.000 8.77062  ? 18  LEU A CD1 1 
ATOM   165  C  CD2 . LEU A 1 17  ? 11.07900  -1.31300  67.74200 1.000 8.84958  ? 18  LEU A CD2 1 
ATOM   166  N  N   . ASP A 1 18  ? 13.87300  0.40300   69.04500 1.000 7.10727  ? 19  ASP A N   1 
ATOM   167  C  CA  . ASP A 1 18  ? 14.77700  -0.70100  68.76500 1.000 8.28109  ? 19  ASP A CA  1 
ATOM   168  C  C   . ASP A 1 18  ? 14.15300  -1.97100  69.30500 1.000 7.82577  ? 19  ASP A C   1 
ATOM   169  O  O   . ASP A 1 18  ? 13.63800  -1.98000  70.42900 1.000 8.41532  ? 19  ASP A O   1 
ATOM   170  C  CB  . ASP A 1 18  ? 16.11800  -0.47200  69.44500 1.000 10.37082 ? 19  ASP A CB  1 
ATOM   171  C  CG  . ASP A 1 18  ? 16.88000  0.66300   68.82200 1.000 13.77649 ? 19  ASP A CG  1 
ATOM   172  O  OD1 . ASP A 1 18  ? 16.87800  0.79400   67.58000 1.000 13.80281 ? 19  ASP A OD1 1 
ATOM   173  O  OD2 . ASP A 1 18  ? 17.47900  1.43100   69.59200 1.000 17.96646 ? 19  ASP A OD2 1 
ATOM   174  N  N   . GLY A 1 19  ? 14.18600  -3.02900  68.50900 1.000 7.71523  ? 20  GLY A N   1 
ATOM   175  C  CA  . GLY A 1 19  ? 13.53600  -4.27400  68.87300 1.000 8.11265  ? 20  GLY A CA  1 
ATOM   176  C  C   . GLY A 1 19  ? 14.40800  -5.49000  68.64200 1.000 7.93895  ? 20  GLY A C   1 
ATOM   177  O  O   . GLY A 1 19  ? 15.28800  -5.50600  67.77600 1.000 7.73103  ? 20  GLY A O   1 
ATOM   178  N  N   . ASP A 1 20  ? 14.12300  -6.53000  69.42000 1.000 7.27834  ? 21  ASP A N   1 
ATOM   179  C  CA  . ASP A 1 20  ? 14.72500  -7.84600  69.22800 1.000 7.58364  ? 21  ASP A CA  1 
ATOM   180  C  C   . ASP A 1 20  ? 13.60500  -8.82800  69.52800 1.000 7.01778  ? 21  ASP A C   1 
ATOM   181  O  O   . ASP A 1 20  ? 13.18300  -8.93400  70.68600 1.000 7.68892  ? 21  ASP A O   1 
ATOM   182  C  CB  . ASP A 1 20  ? 15.89100  -8.04800  70.19700 1.000 8.30741  ? 21  ASP A CB  1 
ATOM   183  C  CG  . ASP A 1 20  ? 16.45700  -9.46500  70.17400 1.000 9.23910  ? 21  ASP A CG  1 
ATOM   184  O  OD1 . ASP A 1 20  ? 15.74600  -10.42400 69.80300 1.000 8.76799  ? 21  ASP A OD1 1 
ATOM   185  O  OD2 . ASP A 1 20  ? 17.63700  -9.62100  70.57100 1.000 12.34210 ? 21  ASP A OD2 1 
ATOM   186  N  N   . VAL A 1 21  ? 13.11700  -9.52800  68.50000 1.000 6.68353  ? 22  VAL A N   1 
ATOM   187  C  CA  . VAL A 1 21  ? 12.04800  -10.51800 68.65900 1.000 7.35730  ? 22  VAL A CA  1 
ATOM   188  C  C   . VAL A 1 21  ? 12.63100  -11.84600 68.20500 1.000 7.53890  ? 22  VAL A C   1 
ATOM   189  O  O   . VAL A 1 21  ? 12.97200  -12.01100 67.02500 1.000 8.10475  ? 22  VAL A O   1 
ATOM   190  C  CB  . VAL A 1 21  ? 10.79100  -10.15300 67.85400 1.000 7.79682  ? 22  VAL A CB  1 
ATOM   191  C  CG1 . VAL A 1 21  ? 9.76000   -11.28800 67.90400 1.000 8.68904  ? 22  VAL A CG1 1 
ATOM   192  C  CG2 . VAL A 1 21  ? 10.16400  -8.86600  68.36500 1.000 7.75998  ? 22  VAL A CG2 1 
ATOM   193  N  N   . ASN A 1 22  ? 12.80400  -12.77300 69.14300 1.000 7.66523  ? 23  ASN A N   1 
ATOM   194  C  CA  . ASN A 1 22  ? 13.40600  -14.08100 68.84400 1.000 8.29162  ? 23  ASN A CA  1 
ATOM   195  C  C   . ASN A 1 22  ? 14.75000  -13.94200 68.11500 1.000 8.34952  ? 23  ASN A C   1 
ATOM   196  O  O   . ASN A 1 22  ? 15.07600  -14.72500 67.22100 1.000 8.94170  ? 23  ASN A O   1 
ATOM   197  C  CB  . ASN A 1 22  ? 12.44200  -14.95400 68.03100 1.000 8.91275  ? 23  ASN A CB  1 
ATOM   198  C  CG  . ASN A 1 22  ? 11.41800  -15.67800 68.87900 1.000 8.89432  ? 23  ASN A CG  1 
ATOM   199  O  OD1 . ASN A 1 22  ? 10.86100  -15.14400 69.84600 1.000 9.45755  ? 23  ASN A OD1 1 
ATOM   200  N  ND2 . ASN A 1 22  ? 11.16400  -16.92200 68.50700 1.000 9.59441  ? 23  ASN A ND2 1 
ATOM   201  N  N   . GLY A 1 23  ? 15.53800  -12.92000 68.48200 1.000 8.35215  ? 24  GLY A N   1 
ATOM   202  C  CA  . GLY A 1 23  ? 16.83100  -12.70400 67.86200 1.000 9.13646  ? 24  GLY A CA  1 
ATOM   203  C  C   . GLY A 1 23  ? 16.79900  -11.93400 66.56300 1.000 9.29700  ? 24  GLY A C   1 
ATOM   204  O  O   . GLY A 1 23  ? 17.86900  -11.62900 66.02800 1.000 11.00773 ? 24  GLY A O   1 
ATOM   205  N  N   . HIS A 1 24  ? 15.61300  -11.61100 66.03900 1.000 8.84958  ? 25  HIS A N   1 
ATOM   206  C  CA  . HIS A 1 24  ? 15.49600  -10.70300 64.90000 1.000 10.09973 ? 25  HIS A CA  1 
ATOM   207  C  C   . HIS A 1 24  ? 15.59200  -9.28300  65.42700 1.000 9.58914  ? 25  HIS A C   1 
ATOM   208  O  O   . HIS A 1 24  ? 14.68900  -8.80900  66.12500 1.000 9.34701  ? 25  HIS A O   1 
ATOM   209  C  CB  . HIS A 1 24  ? 14.15600  -10.86600 64.19800 1.000 12.51581 ? 25  HIS A CB  1 
ATOM   210  C  CG  . HIS A 1 24  ? 13.93900  -12.21600 63.60300 1.000 14.25549 ? 25  HIS A CG  1 
ATOM   211  N  ND1 . HIS A 1 24  ? 14.28900  -12.52000 62.30400 1.000 16.70579 ? 25  HIS A ND1 1 
ATOM   212  C  CD2 . HIS A 1 24  ? 13.38700  -13.33600 64.12000 1.000 14.64764 ? 25  HIS A CD2 1 
ATOM   213  C  CE1 . HIS A 1 24  ? 13.97600  -13.77900 62.05300 1.000 16.86370 ? 25  HIS A CE1 1 
ATOM   214  N  NE2 . HIS A 1 24  ? 13.42200  -14.29500 63.13500 1.000 15.72935 ? 25  HIS A NE2 1 
ATOM   215  N  N   . LYS A 1 25  ? 16.68200  -8.60500  65.10000 1.000 9.55230  ? 26  LYS A N   1 
ATOM   216  C  CA  . LYS A 1 25  ? 16.91600  -7.24200  65.55600 1.000 10.20501 ? 26  LYS A CA  1 
ATOM   217  C  C   . LYS A 1 25  ? 16.48000  -6.24500  64.49100 1.000 9.98393  ? 26  LYS A C   1 
ATOM   218  O  O   . LYS A 1 25  ? 16.77100  -6.41600  63.30600 1.000 12.45528 ? 26  LYS A O   1 
ATOM   219  C  CB  . LYS A 1 25  ? 18.38900  -7.05700  65.91500 1.000 11.85520 ? 26  LYS A CB  1 
ATOM   220  C  CG  . LYS A 1 25  ? 18.79800  -7.96300  67.07300 1.000 14.27128 ? 26  LYS A CG  1 
ATOM   221  C  CD  . LYS A 1 25  ? 20.26000  -7.83300  67.42200 1.000 18.61917 ? 26  LYS A CD  1 
ATOM   222  C  CE  . LYS A 1 25  ? 20.57400  -8.62700  68.68700 1.000 22.28378 ? 26  LYS A CE  1 
ATOM   223  N  NZ  . LYS A 1 25  ? 20.29700  -10.08000 68.52600 1.000 79.17378 ? 26  LYS A NZ  1 
ATOM   224  N  N   . PHE A 1 26  ? 15.78700  -5.19600  64.92100 1.000 8.58902  ? 27  PHE A N   1 
ATOM   225  C  CA  . PHE A 1 26  ? 15.22700  -4.24900  63.97000 1.000 8.98381  ? 27  PHE A CA  1 
ATOM   226  C  C   . PHE A 1 26  ? 15.04800  -2.89400  64.62800 1.000 8.42058  ? 27  PHE A C   1 
ATOM   227  O  O   . PHE A 1 26  ? 15.04100  -2.77800  65.85400 1.000 8.72588  ? 27  PHE A O   1 
ATOM   228  C  CB  . PHE A 1 26  ? 13.88200  -4.72300  63.41400 1.000 8.87327  ? 27  PHE A CB  1 
ATOM   229  C  CG  . PHE A 1 26  ? 12.81900  -4.95100  64.46700 1.000 8.78115  ? 27  PHE A CG  1 
ATOM   230  C  CD1 . PHE A 1 26  ? 12.77900  -6.14000  65.18900 1.000 9.04697  ? 27  PHE A CD1 1 
ATOM   231  C  CD2 . PHE A 1 26  ? 11.84400  -3.99400  64.71600 1.000 9.03381  ? 27  PHE A CD2 1 
ATOM   232  C  CE1 . PHE A 1 26  ? 11.78200  -6.36600  66.14100 1.000 8.89432  ? 27  PHE A CE1 1 
ATOM   233  C  CE2 . PHE A 1 26  ? 10.84300  -4.22400  65.67700 1.000 8.48901  ? 27  PHE A CE2 1 
ATOM   234  C  CZ  . PHE A 1 26  ? 10.82000  -5.41000  66.37900 1.000 9.16804  ? 27  PHE A CZ  1 
ATOM   235  N  N   . SER A 1 27  ? 14.88600  -1.87200  63.79200 1.000 8.37584  ? 28  SER A N   1 
ATOM   236  C  CA  . SER A 1 27  ? 14.62700  -0.53100  64.29500 1.000 8.51533  ? 28  SER A CA  1 
ATOM   237  C  C   . SER A 1 27  ? 13.55000  0.11600   63.44600 1.000 7.28097  ? 28  SER A C   1 
ATOM   238  O  O   . SER A 1 27  ? 13.44600  -0.15600  62.24600 1.000 7.94421  ? 28  SER A O   1 
ATOM   239  C  CB  . SER A 1 27  ? 15.88900  0.33200   64.26400 1.000 10.22869 ? 28  SER A CB  1 
ATOM   240  O  OG  . SER A 1 27  ? 16.89600  -0.22800  65.10100 1.000 11.89468 ? 28  SER A OG  1 
ATOM   241  N  N   . VAL A 1 28  ? 12.77700  1.00600   64.07500 1.000 7.26255  ? 29  VAL A N   1 
ATOM   242  C  CA  . VAL A 1 28  ? 11.72000  1.74600   63.39700 1.000 7.90999  ? 29  VAL A CA  1 
ATOM   243  C  C   . VAL A 1 28  ? 11.80600  3.20400   63.81800 1.000 7.88894  ? 29  VAL A C   1 
ATOM   244  O  O   . VAL A 1 28  ? 11.99900  3.51300   64.99900 1.000 8.11528  ? 29  VAL A O   1 
ATOM   245  C  CB  . VAL A 1 28  ? 10.32400  1.17800   63.73600 1.000 7.63891  ? 29  VAL A CB  1 
ATOM   246  C  CG1 . VAL A 1 28  ? 9.22100   2.07100   63.12800 1.000 8.28636  ? 29  VAL A CG1 1 
ATOM   247  C  CG2 . VAL A 1 28  ? 10.19600  -0.24200  63.25100 1.000 7.44941  ? 29  VAL A CG2 1 
ATOM   248  N  N   . SER A 1 29  ? 11.66700  4.09900   62.84300 1.000 7.34940  ? 30  SER A N   1 
ATOM   249  C  CA  . SER A 1 29  ? 11.55200  5.53200   63.09400 1.000 7.44415  ? 30  SER A CA  1 
ATOM   250  C  C   . SER A 1 29  ? 10.18700  6.00800   62.61500 1.000 7.35993  ? 30  SER A C   1 
ATOM   251  O  O   . SER A 1 29  ? 9.74500   5.64800   61.52400 1.000 9.20225  ? 30  SER A O   1 
ATOM   252  C  CB  . SER A 1 29  ? 12.63700  6.29800   62.33500 1.000 8.44953  ? 30  SER A CB  1 
ATOM   253  O  OG  . SER A 1 29  ? 13.92000  5.95000   62.82500 1.000 9.93129  ? 30  SER A OG  1 
ATOM   254  N  N   . GLY A 1 30  ? 9.52800   6.83200   63.41800 1.000 7.10990  ? 31  GLY A N   1 
ATOM   255  C  CA  . GLY A 1 30  ? 8.24300   7.38400   63.03900 1.000 7.60996  ? 31  GLY A CA  1 
ATOM   256  C  C   . GLY A 1 30  ? 8.19500   8.88200   63.24000 1.000 7.11253  ? 31  GLY A C   1 
ATOM   257  O  O   . GLY A 1 30  ? 8.88800   9.43700   64.09000 1.000 7.48100  ? 31  GLY A O   1 
ATOM   258  N  N   . GLU A 1 31  ? 7.33000   9.52300   62.45800 1.000 6.97304  ? 32  GLU A N   1 
ATOM   259  C  CA  . GLU A 1 31  ? 7.10500   10.96000  62.54100 1.000 7.26781  ? 32  GLU A CA  1 
ATOM   260  C  C   . GLU A 1 31  ? 5.63200   11.23700  62.32200 1.000 7.13359  ? 32  GLU A C   1 
ATOM   261  O  O   . GLU A 1 31  ? 4.96000   10.54100  61.56100 1.000 7.85736  ? 32  GLU A O   1 
ATOM   262  C  CB  . GLU A 1 31  ? 7.83200   11.72600  61.43100 1.000 8.86011  ? 32  GLU A CB  1 
ATOM   263  C  CG  . GLU A 1 31  ? 9.31300   11.52800  61.40800 1.000 9.37333  ? 32  GLU A CG  1 
ATOM   264  C  CD  . GLU A 1 31  ? 9.99300   12.29900  60.30500 1.000 9.88918  ? 32  GLU A CD  1 
ATOM   265  O  OE1 . GLU A 1 31  ? 9.41400   13.26500  59.77400 1.000 11.29987 ? 32  GLU A OE1 1 
ATOM   266  O  OE2 . GLU A 1 31  ? 11.13500  11.95300  59.99000 1.000 10.20501 ? 32  GLU A OE2 1 
ATOM   267  N  N   . GLY A 1 32  ? 5.15400   12.30400  62.93300 1.000 7.39941  ? 33  GLY A N   1 
ATOM   268  C  CA  . GLY A 1 32  ? 3.81200   12.76800  62.62400 1.000 7.70997  ? 33  GLY A CA  1 
ATOM   269  C  C   . GLY A 1 32  ? 3.44500   13.85600  63.59400 1.000 6.77565  ? 33  GLY A C   1 
ATOM   270  O  O   . GLY A 1 32  ? 4.30000   14.64700  64.01300 1.000 7.39151  ? 33  GLY A O   1 
ATOM   271  N  N   . GLU A 1 33  ? 2.15800   13.91900  63.92500 1.000 7.17833  ? 34  GLU A N   1 
ATOM   272  C  CA  . GLU A 1 33  ? 1.72600   15.00100  64.79900 1.000 7.97579  ? 34  GLU A CA  1 
ATOM   273  C  C   . GLU A 1 33  ? 0.45500   14.59300  65.51300 1.000 7.22570  ? 34  GLU A C   1 
ATOM   274  O  O   . GLU A 1 33  ? -0.30000  13.73600  65.04000 1.000 8.34689  ? 34  GLU A O   1 
ATOM   275  C  CB  . GLU A 1 33  ? 1.49600   16.30400  64.04000 1.000 10.75770 ? 34  GLU A CB  1 
ATOM   276  C  CG  . GLU A 1 33  ? 0.40600   16.19900  63.02300 1.000 11.96574 ? 34  GLU A CG  1 
ATOM   277  C  CD  . GLU A 1 33  ? 0.29700   17.44100  62.14500 1.000 14.63712 ? 34  GLU A CD  1 
ATOM   278  O  OE1 . GLU A 1 33  ? 1.32600   18.10900  61.88400 1.000 15.34246 ? 34  GLU A OE1 1 
ATOM   279  O  OE2 . GLU A 1 33  ? -0.83000  17.77200  61.73900 1.000 15.08191 ? 34  GLU A OE2 1 
ATOM   280  N  N   . GLY A 1 34  ? 0.22800   15.23200  66.65100 1.000 7.51784  ? 35  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 34  ? -0.95300  14.97000  67.45200 1.000 8.25477  ? 35  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 34  ? -1.69000  16.25000  67.77400 1.000 7.92315  ? 35  GLY A C   1 
ATOM   283  O  O   . GLY A 1 34  ? -1.09400  17.31600  67.94700 1.000 8.51270  ? 35  GLY A O   1 
ATOM   284  N  N   . ASP A 1 35  ? -3.00700  16.12800  67.88700 1.000 7.40467  ? 36  ASP A N   1 
ATOM   285  C  CA  A ASP A 1 35  ? -3.84100  17.27400  68.24800 0.320 8.72378  ? 36  ASP A CA  1 
ATOM   286  C  CA  B ASP A 1 35  ? -3.89100  17.25600  68.18200 0.680 8.80221  ? 36  ASP A CA  1 
ATOM   287  C  C   . ASP A 1 35  ? -4.84300  16.75700  69.26900 1.000 7.68102  ? 36  ASP A C   1 
ATOM   288  O  O   . ASP A 1 35  ? -5.93400  16.28600  68.92800 1.000 8.63640  ? 36  ASP A O   1 
ATOM   289  C  CB  A ASP A 1 35  ? -4.51300  17.94600  67.06000 0.320 10.34378 ? 36  ASP A CB  1 
ATOM   290  C  CB  B ASP A 1 35  ? -4.64500  17.60900  66.87500 0.680 11.09196 ? 36  ASP A CB  1 
ATOM   291  C  CG  A ASP A 1 35  ? -5.15100  19.26900  67.43700 0.320 28.88378 ? 36  ASP A CG  1 
ATOM   292  C  CG  B ASP A 1 35  ? -5.13200  19.06200  66.80500 0.680 11.98417 ? 36  ASP A CG  1 
ATOM   293  O  OD1 A ASP A 1 35  ? -5.18300  19.57900  68.64900 0.320 12.70378 ? 36  ASP A OD1 1 
ATOM   294  O  OD1 B ASP A 1 35  ? -5.08400  19.79500  67.80800 0.680 11.55517 ? 36  ASP A OD1 1 
ATOM   295  O  OD2 A ASP A 1 35  ? -5.60900  19.99600  66.53100 0.320 31.05378 ? 36  ASP A OD2 1 
ATOM   296  O  OD2 B ASP A 1 35  ? -5.57400  19.46400  65.70700 0.680 13.33696 ? 36  ASP A OD2 1 
ATOM   297  N  N   . ALA A 1 36  ? -4.43400  16.83700  70.53700 1.000 7.95210  ? 37  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 36  ? -5.21600  16.25700  71.62100 1.000 8.07844  ? 37  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 36  ? -6.57500  16.92000  71.77200 1.000 7.51258  ? 37  ALA A C   1 
ATOM   300  O  O   . ALA A 1 36  ? -7.49800  16.30600  72.31900 1.000 8.33636  ? 37  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 36  ? -4.46600  16.37700  72.94400 1.000 8.74167  ? 37  ALA A CB  1 
ATOM   302  N  N   . THR A 1 37  ? -6.72800  18.15200  71.29300 1.000 7.69155  ? 38  THR A N   1 
ATOM   303  C  CA  . THR A 1 37  ? -8.03800  18.80100  71.29100 1.000 8.26004  ? 38  THR A CA  1 
ATOM   304  C  C   . THR A 1 37  ? -9.08400  17.93000  70.62100 1.000 8.16266  ? 38  THR A C   1 
ATOM   305  O  O   . THR A 1 37  ? -10.25700 17.94100  71.02500 1.000 9.03118  ? 38  THR A O   1 
ATOM   306  C  CB  . THR A 1 37  ? -7.92000  20.14200  70.56600 1.000 9.73390  ? 38  THR A CB  1 
ATOM   307  O  OG1 . THR A 1 37  ? -7.00200  20.96300  71.28800 1.000 11.38936 ? 38  THR A OG1 1 
ATOM   308  C  CG2 . THR A 1 37  ? -9.26000  20.88300  70.49200 1.000 10.14710 ? 38  THR A CG2 1 
ATOM   309  N  N   . TYR A 1 38  ? -8.67600  17.15500  69.61400 1.000 7.83367  ? 39  TYR A N   1 
ATOM   310  C  CA  . TYR A 1 38  ? -9.56100  16.26200  68.88100 1.000 9.07066  ? 39  TYR A CA  1 
ATOM   311  C  C   . TYR A 1 38  ? -9.19200  14.80200  69.08900 1.000 8.78378  ? 39  TYR A C   1 
ATOM   312  O  O   . TYR A 1 38  ? -9.68200  13.94000  68.35600 1.000 9.77864  ? 39  TYR A O   1 
ATOM   313  C  CB  . TYR A 1 38  ? -9.54500  16.63700  67.39400 1.000 9.85233  ? 39  TYR A CB  1 
ATOM   314  C  CG  . TYR A 1 38  ? -9.72100  18.13500  67.21100 1.000 10.55242 ? 39  TYR A CG  1 
ATOM   315  C  CD1 . TYR A 1 38  ? -10.96700 18.73500  67.36000 1.000 11.85257 ? 39  TYR A CD1 1 
ATOM   316  C  CD2 . TYR A 1 38  ? -8.62200  18.96200  66.99000 1.000 11.59465 ? 39  TYR A CD2 1 
ATOM   317  C  CE1 . TYR A 1 38  ? -11.11700 20.10700  67.24400 1.000 12.24209 ? 39  TYR A CE1 1 
ATOM   318  C  CE2 . TYR A 1 38  ? -8.77200  20.34300  66.87400 1.000 12.77900 ? 39  TYR A CE2 1 
ATOM   319  C  CZ  . TYR A 1 38  ? -10.02300 20.90500  66.99900 1.000 13.23695 ? 39  TYR A CZ  1 
ATOM   320  O  OH  . TYR A 1 38  ? -10.18800 22.26600  66.90300 1.000 15.29246 ? 39  TYR A OH  1 
ATOM   321  N  N   . GLY A 1 39  ? -8.32100  14.50800  70.05600 1.000 7.97053  ? 40  GLY A N   1 
ATOM   322  C  CA  . GLY A 1 39  ? -7.90800  13.13800  70.30300 1.000 7.77577  ? 40  GLY A CA  1 
ATOM   323  C  C   . GLY A 1 39  ? -7.19200  12.50100  69.13800 1.000 8.18898  ? 40  GLY A C   1 
ATOM   324  O  O   . GLY A 1 39  ? -7.21900  11.27400  68.99400 1.000 8.80221  ? 40  GLY A O   1 
ATOM   325  N  N   . LYS A 1 40  ? -6.54500  13.30000  68.30200 1.000 7.84946  ? 41  LYS A N   1 
ATOM   326  C  CA  . LYS A 1 40  ? -6.16600  12.87000  66.96200 1.000 7.88894  ? 41  LYS A CA  1 
ATOM   327  C  C   . LYS A 1 40  ? -4.66500  12.70100  66.82000 1.000 7.73892  ? 41  LYS A C   1 
ATOM   328  O  O   . LYS A 1 40  ? -3.89500  13.57800  67.22300 1.000 9.21278  ? 41  LYS A O   1 
ATOM   329  C  CB  . LYS A 1 40  ? -6.63800  13.92700  65.96000 1.000 8.98644  ? 41  LYS A CB  1 
ATOM   330  C  CG  . LYS A 1 40  ? -6.34700  13.61100  64.52300 1.000 10.66822 ? 41  LYS A CG  1 
ATOM   331  C  CD  . LYS A 1 40  ? -6.83900  14.72900  63.62000 1.000 12.63951 ? 41  LYS A CD  1 
ATOM   332  C  CE  . LYS A 1 40  ? -6.73400  14.36200  62.14500 1.000 15.50301 ? 41  LYS A CE  1 
ATOM   333  N  NZ  . LYS A 1 40  ? -7.46400  15.34800  61.29600 1.000 16.80580 ? 41  LYS A NZ  1 
ATOM   334  N  N   A LEU A 1 41  ? -4.27400  11.58400  66.18700 0.530 7.08095  ? 42  LEU A N   1 
ATOM   335  N  N   B LEU A 1 41  ? -4.23800  11.60100  66.22800 0.470 6.81378  ? 42  LEU A N   1 
ATOM   336  C  CA  A LEU A 1 41  ? -2.89200  11.22700  65.89300 0.530 6.06240  ? 42  LEU A CA  1 
ATOM   337  C  CA  B LEU A 1 41  ? -2.84200  11.55800  65.84600 0.470 7.43378  ? 42  LEU A CA  1 
ATOM   338  C  C   A LEU A 1 41  ? -2.74100  10.86200  64.42200 0.530 7.02041  ? 42  LEU A C   1 
ATOM   339  C  C   B LEU A 1 41  ? -2.68300  10.88500  64.49700 0.470 7.23378  ? 42  LEU A C   1 
ATOM   340  O  O   A LEU A 1 41  ? -3.56700  10.12700  63.87000 0.530 7.92579  ? 42  LEU A O   1 
ATOM   341  O  O   B LEU A 1 41  ? -3.44600  9.99400   64.11400 0.470 8.09378  ? 42  LEU A O   1 
ATOM   342  C  CB  A LEU A 1 41  ? -2.47100  9.99500   66.71800 0.530 6.04661  ? 42  LEU A CB  1 
ATOM   343  C  CB  B LEU A 1 41  ? -1.90900  10.99900  66.93000 0.470 10.50378 ? 42  LEU A CB  1 
ATOM   344  C  CG  A LEU A 1 41  ? -2.25900  10.32200  68.18900 0.530 6.57562  ? 42  LEU A CG  1 
ATOM   345  C  CG  B LEU A 1 41  ? -2.12000  9.55400   67.35400 0.470 9.58378  ? 42  LEU A CG  1 
ATOM   346  C  CD1 A LEU A 1 41  ? -2.29300  9.03600   69.01500 0.530 6.55983  ? 42  LEU A CD1 1 
ATOM   347  C  CD1 B LEU A 1 41  ? -1.40800  8.61600   66.40200 0.470 9.95378  ? 42  LEU A CD1 1 
ATOM   348  C  CD2 A LEU A 1 41  ? -0.95500  11.07300  68.37500 0.530 6.27032  ? 42  LEU A CD2 1 
ATOM   349  C  CD2 B LEU A 1 41  ? -1.60800  9.36000   68.76800 0.470 14.98378 ? 42  LEU A CD2 1 
ATOM   350  N  N   . THR A 1 42  ? -1.65200  11.32800  63.80100 1.000 7.43099  ? 43  THR A N   1 
ATOM   351  C  CA  A THR A 1 42  ? -1.26200  10.86400  62.47800 0.530 8.28109  ? 43  THR A CA  1 
ATOM   352  C  CA  B THR A 1 42  ? -1.26600  10.83400  62.49000 0.470 8.00378  ? 43  THR A CA  1 
ATOM   353  C  C   . THR A 1 42  ? 0.22700   10.55300  62.54100 1.000 7.88368  ? 43  THR A C   1 
ATOM   354  O  O   . THR A 1 42  ? 1.02100   11.43100  62.88900 1.000 8.99170  ? 43  THR A O   1 
ATOM   355  C  CB  A THR A 1 42  ? -1.55100  11.94600  61.42900 0.530 10.24185 ? 43  THR A CB  1 
ATOM   356  C  CB  B THR A 1 42  ? -1.55700  11.87200  61.39000 0.470 11.81378 ? 43  THR A CB  1 
ATOM   357  O  OG1 A THR A 1 42  ? -2.87500  12.47100  61.62500 0.530 10.07604 ? 43  THR A OG1 1 
ATOM   358  O  OG1 B THR A 1 42  ? -0.96400  13.12700  61.73500 0.470 13.91378 ? 43  THR A OG1 1 
ATOM   359  C  CG2 A THR A 1 42  ? -1.47500  11.35800  60.05000 0.530 12.75794 ? 43  THR A CG2 1 
ATOM   360  C  CG2 B THR A 1 42  ? -3.04800  12.07400  61.21000 0.470 13.57378 ? 43  THR A CG2 1 
ATOM   361  N  N   . LEU A 1 43  ? 0.60900   9.32200   62.20100 1.000 7.89157  ? 44  LEU A N   1 
ATOM   362  C  CA  . LEU A 1 43  ? 1.99800   8.89500   62.29100 1.000 8.03896  ? 44  LEU A CA  1 
ATOM   363  C  C   . LEU A 1 43  ? 2.36000   8.02500   61.09900 1.000 8.24425  ? 44  LEU A C   1 
ATOM   364  O  O   . LEU A 1 43  ? 1.55300   7.21600   60.63600 1.000 9.11014  ? 44  LEU A O   1 
ATOM   365  C  CB  . LEU A 1 43  ? 2.24200   8.09100   63.58500 1.000 9.61546  ? 44  LEU A CB  1 
ATOM   366  C  CG  . LEU A 1 43  ? 2.13700   8.92100   64.87400 1.000 10.49715 ? 44  LEU A CG  1 
ATOM   367  C  CD1 . LEU A 1 43  ? 2.04300   7.98900   66.08200 1.000 12.83427 ? 44  LEU A CD1 1 
ATOM   368  C  CD2 . LEU A 1 43  ? 3.30700   9.87900   65.04700 1.000 11.14722 ? 44  LEU A CD2 1 
ATOM   369  N  N   . LYS A 1 44  ? 3.59400   8.16800   60.62200 1.000 7.64417  ? 45  LYS A N   1 
ATOM   370  C  CA  . LYS A 1 44  ? 4.14300   7.27800   59.60600 1.000 7.63628  ? 45  LYS A CA  1 
ATOM   371  C  C   . LYS A 1 44  ? 5.42800   6.68000   60.13800 1.000 7.17043  ? 45  LYS A C   1 
ATOM   372  O  O   . LYS A 1 44  ? 6.30900   7.41600   60.60400 1.000 7.59943  ? 45  LYS A O   1 
ATOM   373  C  CB  . LYS A 1 44  ? 4.39900   8.01800   58.28700 1.000 8.71535  ? 45  LYS A CB  1 
ATOM   374  C  CG  . LYS A 1 44  ? 5.09800   7.12500   57.25000 1.000 9.03908  ? 45  LYS A CG  1 
ATOM   375  C  CD  . LYS A 1 44  ? 5.35400   7.84700   55.92100 1.000 9.90760  ? 45  LYS A CD  1 
ATOM   376  C  CE  . LYS A 1 44  ? 6.18800   6.99900   54.99400 1.000 10.73665 ? 45  LYS A CE  1 
ATOM   377  N  NZ  . LYS A 1 44  ? 6.53600   7.73200   53.74600 1.000 11.37883 ? 45  LYS A NZ  1 
ATOM   378  N  N   . PHE A 1 45  ? 5.51700   5.35000   60.08200 1.000 7.45204  ? 46  PHE A N   1 
ATOM   379  C  CA  . PHE A 1 45  ? 6.63800   4.58700   60.61400 1.000 7.62838  ? 46  PHE A CA  1 
ATOM   380  C  C   . PHE A 1 45  ? 7.38000   3.92600   59.46900 1.000 7.46784  ? 46  PHE A C   1 
ATOM   381  O  O   . PHE A 1 45  ? 6.76100   3.41400   58.53100 1.000 8.58639  ? 46  PHE A O   1 
ATOM   382  C  CB  . PHE A 1 45  ? 6.14200   3.48500   61.55800 1.000 8.16002  ? 46  PHE A CB  1 
ATOM   383  C  CG  . PHE A 1 45  ? 5.28400   4.01300   62.64500 1.000 7.33098  ? 46  PHE A CG  1 
ATOM   384  C  CD1 . PHE A 1 45  ? 5.86700   4.56800   63.76800 1.000 7.96526  ? 46  PHE A CD1 1 
ATOM   385  C  CD2 . PHE A 1 45  ? 3.90900   4.01400   62.52900 1.000 8.39953  ? 46  PHE A CD2 1 
ATOM   386  C  CE1 . PHE A 1 45  ? 5.11800   5.09800   64.78300 1.000 7.76787  ? 46  PHE A CE1 1 
ATOM   387  C  CE2 . PHE A 1 45  ? 3.12500   4.53600   63.55900 1.000 8.20477  ? 46  PHE A CE2 1 
ATOM   388  C  CZ  . PHE A 1 45  ? 3.72800   5.08600   64.68000 1.000 8.15476  ? 46  PHE A CZ  1 
ATOM   389  N  N   . ILE A 1 46  ? 8.71000   3.90200   59.57000 1.000 7.81788  ? 47  ILE A N   1 
ATOM   390  C  CA  A ILE A 1 46  ? 9.56300   3.25900   58.58300 0.540 8.02053  ? 47  ILE A CA  1 
ATOM   391  C  CA  B ILE A 1 46  ? 9.59900   3.28900   58.58300 0.460 6.72378  ? 47  ILE A CA  1 
ATOM   392  C  C   . ILE A 1 46  ? 10.48800  2.28900   59.30600 1.000 7.32308  ? 47  ILE A C   1 
ATOM   393  O  O   . ILE A 1 46  ? 11.11900  2.64800   60.30700 1.000 8.34689  ? 47  ILE A O   1 
ATOM   394  C  CB  A ILE A 1 46  ? 10.36700  4.30700   57.78800 0.540 9.49176  ? 47  ILE A CB  1 
ATOM   395  C  CB  B ILE A 1 46  ? 10.51400  4.35000   57.93800 0.460 9.34378  ? 47  ILE A CB  1 
ATOM   396  C  CG1 A ILE A 1 46  ? 9.40500   5.31000   57.14600 0.540 10.85772 ? 47  ILE A CG1 1 
ATOM   397  C  CG1 B ILE A 1 46  ? 9.71300   5.36000   57.12000 0.460 16.96378 ? 47  ILE A CG1 1 
ATOM   398  C  CG2 A ILE A 1 46  ? 11.24100  3.64400   56.75100 0.540 10.09447 ? 47  ILE A CG2 1 
ATOM   399  C  CG2 B ILE A 1 46  ? 11.63500  3.68500   57.12900 0.460 10.39378 ? 47  ILE A CG2 1 
ATOM   400  C  CD1 A ILE A 1 46  ? 10.06500  6.54400   56.60900 0.540 10.77350 ? 47  ILE A CD1 1 
ATOM   401  C  CD1 B ILE A 1 46  ? 9.14700   4.79000   55.86600 0.460 9.71378  ? 47  ILE A CD1 1 
ATOM   402  N  N   . CYS A 1 47  ? 10.55800  1.04200   58.80600 1.000 7.37572  ? 48  CYS A N   1 
ATOM   403  C  CA  . CYS A 1 47  ? 11.54900  0.11300   59.33500 1.000 8.18371  ? 48  CYS A CA  1 
ATOM   404  C  C   . CYS A 1 47  ? 12.89300  0.44900   58.69500 1.000 9.50492  ? 48  CYS A C   1 
ATOM   405  O  O   . CYS A 1 47  ? 13.06100  0.30500   57.48100 1.000 11.17091 ? 48  CYS A O   1 
ATOM   406  C  CB  . CYS A 1 47  ? 11.16900  -1.34500  59.05200 1.000 9.33911  ? 48  CYS A CB  1 
ATOM   407  S  SG  . CYS A 1 47  ? 12.44200  -2.47500  59.69800 1.000 9.29437  ? 48  CYS A SG  1 
ATOM   408  N  N   . THR A 1 48  ? 13.85500  0.89900   59.49400 1.000 9.07592  ? 49  THR A N   1 
ATOM   409  C  CA  . THR A 1 48  ? 15.11100  1.39400   58.93900 1.000 10.61295 ? 49  THR A CA  1 
ATOM   410  C  C   . THR A 1 48  ? 16.15300  0.30200   58.79200 1.000 11.51569 ? 49  THR A C   1 
ATOM   411  O  O   . THR A 1 48  ? 17.22700  0.54700   58.24500 1.000 13.12904 ? 49  THR A O   1 
ATOM   412  C  CB  . THR A 1 48  ? 15.66900  2.50300   59.83000 1.000 10.58663 ? 49  THR A CB  1 
ATOM   413  O  OG1 . THR A 1 48  ? 15.89300  1.96700   61.13700 1.000 10.97089 ? 49  THR A OG1 1 
ATOM   414  C  CG2 . THR A 1 48  ? 14.69700  3.68500   59.90700 1.000 11.11301 ? 49  THR A CG2 1 
ATOM   415  N  N   . THR A 1 49  ? 15.85000  -0.90300  59.23900 1.000 9.92603  ? 50  THR A N   1 
ATOM   416  C  CA  . THR A 1 49  ? 16.77500  -2.01000  59.14500 1.000 10.26028 ? 50  THR A CA  1 
ATOM   417  C  C   . THR A 1 49  ? 16.44800  -2.97200  58.01400 1.000 10.69980 ? 50  THR A C   1 
ATOM   418  O  O   . THR A 1 49  ? 17.19200  -3.93500  57.82800 1.000 13.10009 ? 50  THR A O   1 
ATOM   419  C  CB  . THR A 1 49  ? 16.85400  -2.74100  60.49000 1.000 10.24185 ? 50  THR A CB  1 
ATOM   420  O  OG1 . THR A 1 49  ? 15.52900  -2.96600  60.98900 1.000 9.71547  ? 50  THR A OG1 1 
ATOM   421  C  CG2 . THR A 1 49  ? 17.61900  -1.91000  61.50200 1.000 10.09973 ? 50  THR A CG2 1 
ATOM   422  N  N   . GLY A 1 50  ? 15.40900  -2.69700  57.22700 1.000 10.56558 ? 51  GLY A N   1 
ATOM   423  C  CA  . GLY A 1 50  ? 14.99300  -3.57100  56.14900 1.000 11.19723 ? 51  GLY A CA  1 
ATOM   424  C  C   . GLY A 1 50  ? 13.53900  -3.94500  56.32800 1.000 11.03142 ? 51  GLY A C   1 
ATOM   425  O  O   . GLY A 1 50  ? 12.69200  -3.08800  56.60300 1.000 12.34737 ? 51  GLY A O   1 
ATOM   426  N  N   . LYS A 1 51  ? 13.23600  -5.22600  56.18500 1.000 10.59716 ? 52  LYS A N   1 
ATOM   427  C  CA  . LYS A 1 51  ? 11.88400  -5.71400  56.39200 1.000 11.17091 ? 52  LYS A CA  1 
ATOM   428  C  C   . LYS A 1 51  ? 11.60300  -5.86500  57.87900 1.000 9.66810  ? 52  LYS A C   1 
ATOM   429  O  O   . LYS A 1 51  ? 12.42600  -6.41000  58.62200 1.000 10.66559 ? 52  LYS A O   1 
ATOM   430  C  CB  . LYS A 1 51  ? 11.72900  -7.08200  55.72600 1.000 14.68712 ? 52  LYS A CB  1 
ATOM   431  C  CG  . LYS A 1 51  ? 10.37000  -7.72400  55.97400 1.000 22.76378 ? 52  LYS A CG  1 
ATOM   432  C  CD  . LYS A 1 51  ? 10.21400  -9.05200  55.25400 1.000 39.09378 ? 52  LYS A CD  1 
ATOM   433  C  CE  . LYS A 1 51  ? 8.87700   -9.70400  55.58500 1.000 73.03378 ? 52  LYS A CE  1 
ATOM   434  N  NZ  . LYS A 1 51  ? 7.71800   -8.81900  55.27900 1.000 67.67378 ? 52  LYS A NZ  1 
ATOM   435  N  N   . LEU A 1 52  ? 10.41900  -5.41700  58.31100 1.000 9.46018  ? 53  LEU A N   1 
ATOM   436  C  CA  . LEU A 1 52  ? 10.03800  -5.60700  59.70700 1.000 9.51808  ? 53  LEU A CA  1 
ATOM   437  C  C   . LEU A 1 52  ? 9.79100   -7.09800  59.94700 1.000 8.82326  ? 53  LEU A C   1 
ATOM   438  O  O   . LEU A 1 52  ? 9.03100   -7.71800  59.20000 1.000 10.17342 ? 53  LEU A O   1 
ATOM   439  C  CB  . LEU A 1 52  ? 8.78100   -4.77800  60.00200 1.000 9.43913  ? 53  LEU A CB  1 
ATOM   440  C  CG  . LEU A 1 52  ? 8.41300   -4.65200  61.47300 1.000 9.22857  ? 53  LEU A CG  1 
ATOM   441  C  CD1 . LEU A 1 52  ? 9.41200   -3.74200  62.17400 1.000 8.93643  ? 53  LEU A CD1 1 
ATOM   442  C  CD2 . LEU A 1 52  ? 6.99300   -4.13500  61.62300 1.000 9.24437  ? 53  LEU A CD2 1 
ATOM   443  N  N   . PRO A 1 53  ? 10.41100  -7.70800  60.96200 1.000 9.02065  ? 54  PRO A N   1 
ATOM   444  C  CA  . PRO A 1 53  ? 10.29400  -9.16400  61.14900 1.000 9.03645  ? 54  PRO A CA  1 
ATOM   445  C  C   . PRO A 1 53  ? 9.04800   -9.59900  61.91000 1.000 8.59692  ? 54  PRO A C   1 
ATOM   446  O  O   . PRO A 1 53  ? 8.89700   -10.79500 62.19300 1.000 9.29700  ? 54  PRO A O   1 
ATOM   447  C  CB  . PRO A 1 53  ? 11.56700  -9.50400  61.94200 1.000 10.73139 ? 54  PRO A CB  1 
ATOM   448  C  CG  . PRO A 1 53  ? 11.78200  -8.28300  62.77400 1.000 10.58926 ? 54  PRO A CG  1 
ATOM   449  C  CD  . PRO A 1 53  ? 11.40600  -7.11000  61.87400 1.000 9.72600  ? 54  PRO A CD  1 
ATOM   450  N  N   . VAL A 1 54  ? 8.17400   -8.66400  62.26600 1.000 7.78893  ? 55  VAL A N   1 
ATOM   451  C  CA  . VAL A 1 54  ? 6.88400   -8.96500  62.88300 1.000 7.60206  ? 55  VAL A CA  1 
ATOM   452  C  C   . VAL A 1 54  ? 5.84100   -8.16600  62.11600 1.000 7.52311  ? 55  VAL A C   1 
ATOM   453  O  O   . VAL A 1 54  ? 6.19100   -7.19700  61.42800 1.000 7.96263  ? 55  VAL A O   1 
ATOM   454  C  CB  . VAL A 1 54  ? 6.85700   -8.59900  64.38100 1.000 8.05475  ? 55  VAL A CB  1 
ATOM   455  C  CG1 . VAL A 1 54  ? 7.89300   -9.37300  65.16700 1.000 9.14699  ? 55  VAL A CG1 1 
ATOM   456  C  CG2 . VAL A 1 54  ? 7.03700   -7.07800  64.60400 1.000 7.77577  ? 55  VAL A CG2 1 
ATOM   457  N  N   . PRO A 1 55  ? 4.55500   -8.47400  62.24900 1.000 7.54943  ? 56  PRO A N   1 
ATOM   458  C  CA  . PRO A 1 55  ? 3.55400   -7.69500  61.51000 1.000 7.32045  ? 56  PRO A CA  1 
ATOM   459  C  C   . PRO A 1 55  ? 3.40400   -6.30500  62.11000 1.000 7.08095  ? 56  PRO A C   1 
ATOM   460  O  O   . PRO A 1 55  ? 3.36000   -6.13800  63.33300 1.000 7.24939  ? 56  PRO A O   1 
ATOM   461  C  CB  . PRO A 1 55  ? 2.27000   -8.52300  61.67000 1.000 8.36794  ? 56  PRO A CB  1 
ATOM   462  C  CG  . PRO A 1 55  ? 2.77000   -9.92800  61.94800 1.000 8.51270  ? 56  PRO A CG  1 
ATOM   463  C  CD  . PRO A 1 55  ? 3.98800   -9.70700  62.81500 1.000 7.84420  ? 56  PRO A CD  1 
ATOM   464  N  N   . TRP A 1 56  ? 3.33000   -5.31000  61.23300 1.000 7.01252  ? 57  TRP A N   1 
ATOM   465  C  CA  . TRP A 1 56  ? 3.12700   -3.92700  61.67100 1.000 6.82829  ? 57  TRP A CA  1 
ATOM   466  C  C   . TRP A 1 56  ? 2.01900   -3.77800  62.70200 1.000 6.86250  ? 57  TRP A C   1 
ATOM   467  O  O   . TRP A 1 56  ? 2.21700   -3.04200  63.68300 1.000 6.58615  ? 57  TRP A O   1 
ATOM   468  C  CB  . TRP A 1 56  ? 2.83700   -3.00200  60.47500 1.000 7.10463  ? 57  TRP A CB  1 
ATOM   469  C  CG  . TRP A 1 56  ? 4.04300   -2.65700  59.70100 1.000 7.05463  ? 57  TRP A CG  1 
ATOM   470  C  CD1 . TRP A 1 56  ? 4.41100   -3.15200  58.48500 1.000 7.76787  ? 57  TRP A CD1 1 
ATOM   471  C  CD2 . TRP A 1 56  ? 5.06800   -1.74800  60.09800 1.000 7.14675  ? 57  TRP A CD2 1 
ATOM   472  N  NE1 . TRP A 1 56  ? 5.61300   -2.59400  58.10400 1.000 7.78366  ? 57  TRP A NE1 1 
ATOM   473  C  CE2 . TRP A 1 56  ? 6.02900   -1.72300  59.07100 1.000 7.44152  ? 57  TRP A CE2 1 
ATOM   474  C  CE3 . TRP A 1 56  ? 5.26200   -0.94400  61.22300 1.000 7.07832  ? 57  TRP A CE3 1 
ATOM   475  C  CZ2 . TRP A 1 56  ? 7.18500   -0.93800  59.14400 1.000 7.79946  ? 57  TRP A CZ2 1 
ATOM   476  C  CZ3 . TRP A 1 56  ? 6.41000   -0.15200  61.29500 1.000 7.28887  ? 57  TRP A CZ3 1 
ATOM   477  C  CH2 . TRP A 1 56  ? 7.35500   -0.15400  60.26000 1.000 8.16266  ? 57  TRP A CH2 1 
ATOM   478  N  N   . PRO A 1 57  ? 0.84800   -4.40400  62.55700 1.000 6.79670  ? 58  PRO A N   1 
ATOM   479  C  CA  . PRO A 1 57  ? -0.20400  -4.16700  63.55300 1.000 6.52562  ? 58  PRO A CA  1 
ATOM   480  C  C   . PRO A 1 57  ? 0.21400   -4.52100  64.95900 1.000 7.41520  ? 58  PRO A C   1 
ATOM   481  O  O   . PRO A 1 57  ? -0.30000  -3.92100  65.90600 1.000 7.16517  ? 58  PRO A O   1 
ATOM   482  C  CB  . PRO A 1 57  ? -1.35300  -5.05600  63.06300 1.000 7.03357  ? 58  PRO A CB  1 
ATOM   483  C  CG  . PRO A 1 57  ? -1.16000  -5.09700  61.57000 1.000 7.97579  ? 58  PRO A CG  1 
ATOM   484  C  CD  . PRO A 1 57  ? 0.34800   -5.21900  61.43200 1.000 7.70207  ? 58  PRO A CD  1 
ATOM   485  N  N   . THR A 1 58  ? 1.12800   -5.48700  65.13400 1.000 6.79934  ? 59  THR A N   1 
ATOM   486  C  CA  . THR A 1 58  ? 1.50000   -5.88000  66.48700 1.000 6.93356  ? 59  THR A CA  1 
ATOM   487  C  C   . THR A 1 58  ? 2.26600   -4.80000  67.24100 1.000 6.60194  ? 59  THR A C   1 
ATOM   488  O  O   . THR A 1 58  ? 2.41200   -4.92800  68.46000 1.000 6.40718  ? 59  THR A O   1 
ATOM   489  C  CB  . THR A 1 58  ? 2.32500   -7.17800  66.51500 1.000 7.16254  ? 59  THR A CB  1 
ATOM   490  O  OG1 . THR A 1 58  ? 3.63200   -6.94900  65.96000 1.000 6.78091  ? 59  THR A OG1 1 
ATOM   491  C  CG2 . THR A 1 58  ? 1.64400   -8.30300  65.77100 1.000 7.62575  ? 59  THR A CG2 1 
ATOM   492  N  N   . LEU A 1 59  ? 2.74000   -3.75500  66.55600 1.000 6.93093  ? 60  LEU A N   1 
ATOM   493  C  CA  . LEU A 1 59  ? 3.52500   -2.67900  67.15200 1.000 6.98883  ? 60  LEU A CA  1 
ATOM   494  C  C   . LEU A 1 59  ? 2.73300   -1.39800  67.34400 1.000 6.63879  ? 60  LEU A C   1 
ATOM   495  O  O   . LEU A 1 59  ? 3.25800   -0.45300  67.92200 1.000 6.31770  ? 60  LEU A O   1 
ATOM   496  C  CB  . LEU A 1 59  ? 4.75800   -2.37900  66.29200 1.000 6.74143  ? 60  LEU A CB  1 
ATOM   497  C  CG  . LEU A 1 59  ? 5.71500   -3.57400  66.14000 1.000 6.88619  ? 60  LEU A CG  1 
ATOM   498  C  CD1 . LEU A 1 59  ? 6.92200   -3.18600  65.29700 1.000 7.65733  ? 60  LEU A CD1 1 
ATOM   499  C  CD2 . LEU A 1 59  ? 6.18300   -4.11200  67.51200 1.000 7.39414  ? 60  LEU A CD2 1 
ATOM   500  N  N   . VAL A 1 60  ? 1.48100   -1.34000  66.88400 1.000 6.12031  ? 61  VAL A N   1 
ATOM   501  C  CA  . VAL A 1 60  ? 0.68800   -0.11200  66.97700 1.000 6.02293  ? 61  VAL A CA  1 
ATOM   502  C  C   . VAL A 1 60  ? 0.61700   0.40600   68.40700 1.000 5.92291  ? 61  VAL A C   1 
ATOM   503  O  O   . VAL A 1 60  ? 0.85900   1.58900   68.65600 1.000 6.28348  ? 61  VAL A O   1 
ATOM   504  C  CB  . VAL A 1 60  ? -0.71200  -0.35600  66.39600 1.000 6.49404  ? 61  VAL A CB  1 
ATOM   505  C  CG1 . VAL A 1 60  ? -1.68800  0.76800   66.78700 1.000 6.50983  ? 61  VAL A CG1 1 
ATOM   506  C  CG2 . VAL A 1 60  ? -0.61800  -0.51300  64.89400 1.000 7.19149  ? 61  VAL A CG2 1 
ATOM   507  N  N   . THR A 1 61  ? 0.25100   -0.45100  69.36700 1.000 6.29664  ? 62  THR A N   1 
ATOM   508  C  CA  . THR A 1 61  ? 0.10000   0.07800   70.72100 1.000 6.03345  ? 62  THR A CA  1 
ATOM   509  C  C   . THR A 1 61  ? 1.42700   0.54900   71.30000 1.000 5.74131  ? 62  THR A C   1 
ATOM   510  O  O   . THR A 1 61  ? 1.44500   1.41700   72.17500 1.000 6.11241  ? 62  THR A O   1 
ATOM   511  C  CB  . THR A 1 61  ? -0.51200  -0.94700  71.66800 1.000 6.55983  ? 62  THR A CB  1 
ATOM   512  O  OG1 . THR A 1 61  ? 0.29100   -2.12900  71.64400 1.000 6.42297  ? 62  THR A OG1 1 
ATOM   513  C  CG2 . THR A 1 61  ? -1.96400  -1.25600  71.28200 1.000 7.79946  ? 62  THR A CG2 1 
ATOM   514  N  N   . THR A 1 62  ? 2.53700   -0.06200  70.88600 1.000 5.65446  ? 63  THR A N   1 
ATOM   515  C  CA  . THR A 1 62  ? 3.84400   0.31300   71.41600 1.000 5.33074  ? 63  THR A CA  1 
ATOM   516  C  C   . THR A 1 62  ? 4.27300   1.66900   70.86500 1.000 5.34653  ? 63  THR A C   1 
ATOM   517  O  O   . THR A 1 62  ? 4.73100   2.53900   71.62100 1.000 6.37560  ? 63  THR A O   1 
ATOM   518  C  CB  . THR A 1 62  ? 4.85800   -0.77500  71.06600 1.000 6.08872  ? 63  THR A CB  1 
ATOM   519  O  OG1 . THR A 1 62  ? 4.48600   -1.99600  71.71400 1.000 6.17294  ? 63  THR A OG1 1 
ATOM   520  C  CG2 . THR A 1 62  ? 6.25300   -0.41000  71.54600 1.000 7.39941  ? 63  THR A CG2 1 
ATOM   521  N  N   . PHE A 1 63  ? 4.13700   1.86100   69.54800 1.000 6.09925  ? 64  PHE A N   1 
ATOM   522  C  CA  . PHE A 1 63  ? 4.42300   3.15700   68.91300 1.000 6.12294  ? 64  PHE A CA  1 
ATOM   523  C  C   . PHE A 1 63  ? 3.47900   4.25000   69.39500 1.000 5.87028  ? 64  PHE A C   1 
ATOM   524  O  O   . PHE A 1 63  ? 3.87900   5.39700   69.60800 1.000 6.54141  ? 64  PHE A O   1 
ATOM   525  C  CB  . PHE A 1 63  ? 4.22400   3.08900   67.40000 1.000 6.82829  ? 64  PHE A CB  1 
ATOM   526  C  CG  . PHE A 1 63  ? 5.13300   2.13900   66.65200 1.000 6.12820  ? 64  PHE A CG  1 
ATOM   527  C  CD1 . PHE A 1 63  ? 6.46500   1.93600   67.00500 1.000 6.89408  ? 64  PHE A CD1 1 
ATOM   528  C  CD2 . PHE A 1 63  ? 4.64200   1.49100   65.51500 1.000 6.38613  ? 64  PHE A CD2 1 
ATOM   529  C  CE1 . PHE A 1 63  ? 7.26800   1.08100   66.24900 1.000 6.93356  ? 64  PHE A CE1 1 
ATOM   530  C  CE2 . PHE A 1 63  ? 5.43800   0.65600   64.76600 1.000 6.75196  ? 64  PHE A CE2 1 
ATOM   531  C  CZ  . PHE A 1 63  ? 6.75100   0.44100   65.14200 1.000 7.57311  ? 64  PHE A CZ  1 
HETATM 532  N  N1  . GYS A 1 64  ? 2.20400   3.88400   69.51700 1.000 5.83343  ? 66  GYS A N1  1 
HETATM 533  O  OG1 A GYS A 1 64  ? -0.73400  5.98800   68.75200 1.000 7.18622  ? 66  GYS A OG1 1 
HETATM 534  C  CB1 . GYS A 1 64  ? 0.19400   4.93700   68.57400 1.000 6.27822  ? 66  GYS A CB1 1 
HETATM 535  C  CA1 . GYS A 1 64  ? 1.10500   4.80600   69.77700 1.000 6.10451  ? 66  GYS A CA1 1 
HETATM 536  C  C1  . GYS A 1 64  ? 0.40200   4.26600   70.96900 1.000 6.10715  ? 66  GYS A C1  1 
HETATM 537  N  N2  . GYS A 1 64  ? -0.77000  3.69400   70.96400 1.000 6.30454  ? 66  GYS A N2  1 
HETATM 538  N  N3  . GYS A 1 64  ? 0.93900   4.37200   72.24100 1.000 6.08609  ? 66  GYS A N3  1 
HETATM 539  C  C2  . GYS A 1 64  ? 0.07500   3.78200   73.10700 1.000 5.81237  ? 66  GYS A C2  1 
HETATM 540  O  O2  . GYS A 1 64  ? 0.27300   3.67800   74.33600 1.000 6.63353  ? 66  GYS A O2  1 
HETATM 541  C  CA2 . GYS A 1 64  ? -1.02100  3.35200   72.28500 1.000 6.14926  ? 66  GYS A CA2 1 
HETATM 542  C  CA3 . GYS A 1 64  ? 2.25100   4.83500   72.60600 1.000 7.32835  ? 66  GYS A CA3 1 
HETATM 543  C  CB2 . GYS A 1 64  ? -2.12800  2.68100   72.74600 1.000 6.18874  ? 66  GYS A CB2 1 
HETATM 544  C  CG2 . GYS A 1 64  ? -3.22700  2.04500   72.05600 1.000 6.73617  ? 66  GYS A CG2 1 
HETATM 545  C  CD1 . GYS A 1 64  ? -3.45500  2.12300   70.66100 1.000 6.67564  ? 66  GYS A CD1 1 
HETATM 546  C  CD2 . GYS A 1 64  ? -4.11800  1.30300   72.82700 1.000 6.77038  ? 66  GYS A CD2 1 
HETATM 547  C  CE1 . GYS A 1 64  ? -4.55000  1.49000   70.11100 1.000 7.28097  ? 66  GYS A CE1 1 
HETATM 548  C  CE2 . GYS A 1 64  ? -5.22000  0.66300   72.25000 1.000 7.57048  ? 66  GYS A CE2 1 
HETATM 549  C  CZ  . GYS A 1 64  ? -5.43600  0.76100   70.90000 1.000 6.78091  ? 66  GYS A CZ  1 
HETATM 550  O  OH  . GYS A 1 64  ? -6.54000  0.14400   70.37900 1.000 7.61259  ? 66  GYS A OH  1 
HETATM 551  C  C3  . GYS A 1 64  ? 2.39000   6.21000   73.15300 1.000 6.40718  ? 66  GYS A C3  1 
HETATM 552  O  O3  . GYS A 1 64  ? 3.32300   6.45900   73.94400 1.000 6.32559  ? 66  GYS A O3  1 
ATOM   553  N  N   . VAL A 1 65  ? 1.50200   7.11700   72.74100 1.000 6.17558  ? 68  VAL A N   1 
ATOM   554  C  CA  . VAL A 1 65  ? 1.60700   8.54100   73.08300 1.000 6.24927  ? 68  VAL A CA  1 
ATOM   555  C  C   . VAL A 1 65  ? 0.24000   9.01300   73.56000 1.000 6.43613  ? 68  VAL A C   1 
ATOM   556  O  O   . VAL A 1 65  ? -0.39100  9.89900   72.97900 1.000 6.97041  ? 68  VAL A O   1 
ATOM   557  C  CB  . VAL A 1 65  ? 2.22000   9.38200   71.93000 1.000 6.64142  ? 68  VAL A CB  1 
ATOM   558  C  CG1 . VAL A 1 65  ? 3.69200   9.02800   71.78600 1.000 7.74419  ? 68  VAL A CG1 1 
ATOM   559  C  CG2 . VAL A 1 65  ? 1.48300   9.16400   70.60300 1.000 7.04937  ? 68  VAL A CG2 1 
ATOM   560  N  N   . GLN A 1 66  ? -0.19400  8.39700   74.66000 1.000 6.80197  ? 69  GLN A N   1 
ATOM   561  C  CA  . GLN A 1 66  ? -1.54800  8.57000   75.17700 1.000 6.90987  ? 69  GLN A CA  1 
ATOM   562  C  C   . GLN A 1 66  ? -1.78500  9.94400   75.77600 1.000 6.67037  ? 69  GLN A C   1 
ATOM   563  O  O   . GLN A 1 66  ? -2.93800  10.25800  76.11300 1.000 6.78618  ? 69  GLN A O   1 
ATOM   564  C  CB  . GLN A 1 66  ? -1.85200  7.43400   76.15800 1.000 7.30729  ? 69  GLN A CB  1 
ATOM   565  C  CG  . GLN A 1 66  ? -1.91900  6.09200   75.43400 1.000 7.56522  ? 69  GLN A CG  1 
ATOM   566  C  CD  . GLN A 1 66  ? -2.01300  4.91700   76.39100 1.000 7.39414  ? 69  GLN A CD  1 
ATOM   567  O  OE1 . GLN A 1 66  ? -1.28700  4.85700   77.39000 1.000 7.65470  ? 69  GLN A OE1 1 
ATOM   568  N  NE2 . GLN A 1 66  ? -2.89900  3.95100   76.08500 1.000 7.86262  ? 69  GLN A NE2 1 
ATOM   569  N  N   . CYS A 1 67  ? -0.74400  10.77300  75.86600 1.000 6.58352  ? 70  CYS A N   1 
ATOM   570  C  CA  . CYS A 1 67  ? -0.92400  12.19300  76.10700 1.000 7.03621  ? 70  CYS A CA  1 
ATOM   571  C  C   . CYS A 1 67  ? -1.73200  12.88500  75.02100 1.000 6.86250  ? 70  CYS A C   1 
ATOM   572  O  O   . CYS A 1 67  ? -2.19800  13.99700  75.25600 1.000 7.38362  ? 70  CYS A O   1 
ATOM   573  C  CB  . CYS A 1 67  ? 0.43700   12.86800  76.26600 1.000 7.33624  ? 70  CYS A CB  1 
ATOM   574  S  SG  . CYS A 1 67  ? 1.67900   12.43100  75.01000 1.000 7.45994  ? 70  CYS A SG  1 
ATOM   575  N  N   . PHE A 1 68  ? -1.92600  12.25800  73.85700 1.000 6.84145  ? 71  PHE A N   1 
ATOM   576  C  CA  . PHE A 1 68  ? -2.76200  12.83900  72.81200 1.000 7.69681  ? 71  PHE A CA  1 
ATOM   577  C  C   . PHE A 1 68  ? -4.22200  12.43200  72.89600 1.000 7.34677  ? 71  PHE A C   1 
ATOM   578  O  O   . PHE A 1 68  ? -5.02500  12.85200  72.05400 1.000 8.75220  ? 71  PHE A O   1 
ATOM   579  C  CB  . PHE A 1 68  ? -2.16500  12.59400  71.43400 1.000 7.32571  ? 71  PHE A CB  1 
ATOM   580  C  CG  . PHE A 1 68  ? -0.90100  13.36000  71.23600 1.000 6.84671  ? 71  PHE A CG  1 
ATOM   581  C  CD1 . PHE A 1 68  ? -0.95700  14.73500  71.05600 1.000 7.43099  ? 71  PHE A CD1 1 
ATOM   582  C  CD2 . PHE A 1 68  ? 0.34600   12.74300  71.31200 1.000 7.30203  ? 71  PHE A CD2 1 
ATOM   583  C  CE1 . PHE A 1 68  ? 0.18400   15.46700  70.90200 1.000 7.86788  ? 71  PHE A CE1 1 
ATOM   584  C  CE2 . PHE A 1 68  ? 1.50600   13.47800  71.17100 1.000 7.34151  ? 71  PHE A CE2 1 
ATOM   585  C  CZ  . PHE A 1 68  ? 1.43300   14.84200  70.95900 1.000 7.49679  ? 71  PHE A CZ  1 
ATOM   586  N  N   . SER A 1 69  ? -4.59900  11.66300  73.91000 1.000 7.13885  ? 72  SER A N   1 
ATOM   587  C  CA  . SER A 1 69  ? -6.00800  11.36900  74.12800 1.000 7.70734  ? 72  SER A CA  1 
ATOM   588  C  C   . SER A 1 69  ? -6.78600  12.65300  74.37400 1.000 7.45204  ? 72  SER A C   1 
ATOM   589  O  O   . SER A 1 69  ? -6.29500  13.58800  75.00800 1.000 7.52574  ? 72  SER A O   1 
ATOM   590  C  CB  . SER A 1 69  ? -6.14400  10.53700  75.39500 1.000 8.64166  ? 72  SER A CB  1 
ATOM   591  O  OG  . SER A 1 69  ? -5.41900  9.32500   75.29400 1.000 8.77589  ? 72  SER A OG  1 
ATOM   592  N  N   . ARG A 1 70  ? -8.03000  12.68900  73.89700 1.000 7.33887  ? 73  ARG A N   1 
ATOM   593  C  CA  . ARG A 1 70  ? -8.91500  13.79600  74.26900 1.000 7.44678  ? 73  ARG A CA  1 
ATOM   594  C  C   . ARG A 1 70  ? -9.55700  13.48100  75.61300 1.000 7.42309  ? 73  ARG A C   1 
ATOM   595  O  O   . ARG A 1 70  ? -10.42700 12.60300  75.70800 1.000 8.01001  ? 73  ARG A O   1 
ATOM   596  C  CB  . ARG A 1 70  ? -9.99100  14.05800  73.22600 1.000 8.51796  ? 73  ARG A CB  1 
ATOM   597  C  CG  . ARG A 1 70  ? -10.79000 15.29300  73.58600 1.000 9.03908  ? 73  ARG A CG  1 
ATOM   598  C  CD  . ARG A 1 70  ? -11.88000 15.63100  72.58900 1.000 9.50229  ? 73  ARG A CD  1 
ATOM   599  N  NE  . ARG A 1 70  ? -13.00000 14.69300  72.59800 1.000 9.83128  ? 73  ARG A NE  1 
ATOM   600  C  CZ  . ARG A 1 70  ? -14.03000 14.76200  73.43600 1.000 11.01563 ? 73  ARG A CZ  1 
ATOM   601  N  NH1 . ARG A 1 70  ? -14.04400 15.61300  74.45100 1.000 11.53411 ? 73  ARG A NH1 1 
ATOM   602  N  NH2 . ARG A 1 70  ? -15.06700 13.93800  73.26600 1.000 12.66056 ? 73  ARG A NH2 1 
ATOM   603  N  N   . TYR A 1 71  ? -9.14800  14.20400  76.65200 1.000 8.01790  ? 74  TYR A N   1 
ATOM   604  C  CA  . TYR A 1 71  ? -9.86100  14.15500  77.91800 1.000 8.41005  ? 74  TYR A CA  1 
ATOM   605  C  C   . TYR A 1 71  ? -10.93400 15.22700  77.91900 1.000 8.80484  ? 74  TYR A C   1 
ATOM   606  O  O   . TYR A 1 71  ? -10.59900 16.41400  77.81000 1.000 10.05499 ? 74  TYR A O   1 
ATOM   607  C  CB  . TYR A 1 71  ? -8.90300  14.34500  79.09100 1.000 8.81273  ? 74  TYR A CB  1 
ATOM   608  C  CG  . TYR A 1 71  ? -8.27600  13.02600  79.51000 1.000 8.44427  ? 74  TYR A CG  1 
ATOM   609  C  CD1 . TYR A 1 71  ? -7.24800  12.44600  78.75400 1.000 8.33636  ? 74  TYR A CD1 1 
ATOM   610  C  CD2 . TYR A 1 71  ? -8.71200  12.35400  80.66100 1.000 8.84695  ? 74  TYR A CD2 1 
ATOM   611  C  CE1 . TYR A 1 71  ? -6.69400  11.22900  79.11200 1.000 7.86788  ? 74  TYR A CE1 1 
ATOM   612  C  CE2 . TYR A 1 71  ? -8.15100  11.14300  81.04300 1.000 8.50743  ? 74  TYR A CE2 1 
ATOM   613  C  CZ  . TYR A 1 71  ? -7.15700  10.59000  80.25200 1.000 7.39414  ? 74  TYR A CZ  1 
ATOM   614  O  OH  . TYR A 1 71  ? -6.58700  9.38900   80.59600 1.000 8.01001  ? 74  TYR A OH  1 
ATOM   615  N  N   . PRO A 1 72  ? -12.21600 14.86300  77.99700 1.000 8.53375  ? 75  PRO A N   1 
ATOM   616  C  CA  . PRO A 1 72  ? -13.26200 15.88000  78.13800 1.000 8.84432  ? 75  PRO A CA  1 
ATOM   617  C  C   . PRO A 1 72  ? -12.92100 16.81900  79.28000 1.000 9.42597  ? 75  PRO A C   1 
ATOM   618  O  O   . PRO A 1 72  ? -12.29900 16.42900  80.26900 1.000 9.93392  ? 75  PRO A O   1 
ATOM   619  C  CB  . PRO A 1 72  ? -14.50500 15.05500  78.46700 1.000 8.82853  ? 75  PRO A CB  1 
ATOM   620  C  CG  . PRO A 1 72  ? -14.23800 13.72200  77.83800 1.000 9.02329  ? 75  PRO A CG  1 
ATOM   621  C  CD  . PRO A 1 72  ? -12.76800 13.49400  77.99600 1.000 8.77852  ? 75  PRO A CD  1 
ATOM   622  N  N   . ASP A 1 73  ? -13.36300 18.06600  79.13900 1.000 9.92339  ? 76  ASP A N   1 
ATOM   623  C  CA  . ASP A 1 73  ? -13.06700 19.06800  80.15300 1.000 10.32871 ? 76  ASP A CA  1 
ATOM   624  C  C   . ASP A 1 73  ? -13.41900 18.57100  81.55300 1.000 11.36567 ? 76  ASP A C   1 
ATOM   625  O  O   . ASP A 1 73  ? -12.65000 18.77000  82.50200 1.000 12.45791 ? 76  ASP A O   1 
ATOM   626  C  CB  . ASP A 1 73  ? -13.81300 20.36500  79.84900 1.000 11.95258 ? 76  ASP A CB  1 
ATOM   627  C  CG  . ASP A 1 73  ? -13.56100 21.41300  80.90200 1.000 13.03429 ? 76  ASP A CG  1 
ATOM   628  O  OD1 . ASP A 1 73  ? -12.49100 22.05200  80.86600 1.000 14.07652 ? 76  ASP A OD1 1 
ATOM   629  O  OD2 . ASP A 1 73  ? -14.42300 21.58300  81.79400 1.000 15.58460 ? 76  ASP A OD2 1 
ATOM   630  N  N   . HIS A 1 74  ? -14.56400 17.89900  81.70100 1.000 11.65255 ? 77  HIS A N   1 
ATOM   631  C  CA  . HIS A 1 74  ? -14.97000 17.45400  83.03100 1.000 12.73426 ? 77  HIS A CA  1 
ATOM   632  C  C   . HIS A 1 74  ? -14.10000 16.32500  83.56200 1.000 12.70794 ? 77  HIS A C   1 
ATOM   633  O  O   . HIS A 1 74  ? -14.20300 16.00000  84.74800 1.000 15.06348 ? 77  HIS A O   1 
ATOM   634  C  CB  . HIS A 1 74  ? -16.45400 17.06100  83.05900 1.000 13.66858 ? 77  HIS A CB  1 
ATOM   635  C  CG  . HIS A 1 74  ? -16.74900 15.74100  82.41600 1.000 13.23432 ? 77  HIS A CG  1 
ATOM   636  N  ND1 . HIS A 1 74  ? -16.92100 15.59300  81.05500 1.000 13.62647 ? 77  HIS A ND1 1 
ATOM   637  C  CD2 . HIS A 1 74  ? -16.91400 14.50600  82.95400 1.000 14.68712 ? 77  HIS A CD2 1 
ATOM   638  C  CE1 . HIS A 1 74  ? -17.16800 14.32200  80.78400 1.000 14.23444 ? 77  HIS A CE1 1 
ATOM   639  N  NE2 . HIS A 1 74  ? -17.17900 13.64500  81.91700 1.000 14.28708 ? 77  HIS A NE2 1 
ATOM   640  N  N   . MET A 1 75  ? -13.26500 15.71900  82.71600 1.000 11.62097 ? 78  MET A N   1 
ATOM   641  C  CA  . MET A 1 75  ? -12.33600 14.67000  83.12200 1.000 10.70243 ? 78  MET A CA  1 
ATOM   642  C  C   . MET A 1 75  ? -10.88900 15.14500  83.18800 1.000 10.52347 ? 78  MET A C   1 
ATOM   643  O  O   . MET A 1 75  ? -9.99200  14.30900  83.33300 1.000 11.38146 ? 78  MET A O   1 
ATOM   644  C  CB  . MET A 1 75  ? -12.42100 13.48700  82.15400 1.000 11.03142 ? 78  MET A CB  1 
ATOM   645  C  CG  . MET A 1 75  ? -13.74700 12.75000  82.21400 1.000 11.58938 ? 78  MET A CG  1 
ATOM   646  S  SD  . MET A 1 75  ? -13.85300 11.33800  81.10400 1.000 11.43410 ? 78  MET A SD  1 
ATOM   647  C  CE  . MET A 1 75  ? -12.54900 10.29800  81.76300 1.000 11.45252 ? 78  MET A CE  1 
ATOM   648  N  N   . LYS A 1 76  ? -10.64100 16.45500  83.09400 1.000 12.32105 ? 79  LYS A N   1 
ATOM   649  C  CA  A LYS A 1 76  ? -9.27000  16.96500  83.04000 0.400 12.95378 ? 79  LYS A CA  1 
ATOM   650  C  CA  B LYS A 1 76  ? -9.26000  16.91400  83.01400 0.320 16.40378 ? 79  LYS A CA  1 
ATOM   651  C  CA  C LYS A 1 76  ? -9.27100  16.97000  83.04200 0.280 9.06378  ? 79  LYS A CA  1 
ATOM   652  C  C   . LYS A 1 76  ? -8.44400  16.50000  84.23100 1.000 11.98154 ? 79  LYS A C   1 
ATOM   653  O  O   . LYS A 1 76  ? -7.23800  16.25800  84.10400 1.000 11.07090 ? 79  LYS A O   1 
ATOM   654  C  CB  A LYS A 1 76  ? -9.29300  18.49200  83.01000 0.400 17.91378 ? 79  LYS A CB  1 
ATOM   655  C  CB  B LYS A 1 76  ? -9.20200  18.42200  82.78000 0.320 16.63378 ? 79  LYS A CB  1 
ATOM   656  C  CB  C LYS A 1 76  ? -9.29000  18.50000  83.03100 0.280 12.38378 ? 79  LYS A CB  1 
ATOM   657  C  CG  A LYS A 1 76  ? -8.70100  19.09500  81.76400 0.400 50.30378 ? 79  LYS A CG  1 
ATOM   658  C  CG  B LYS A 1 76  ? -9.47000  18.79300  81.33900 0.320 28.60378 ? 79  LYS A CG  1 
ATOM   659  C  CG  C LYS A 1 76  ? -9.28300  19.15800  81.66400 0.280 22.60378 ? 79  LYS A CG  1 
ATOM   660  C  CD  A LYS A 1 76  ? -9.36700  18.53300  80.53000 0.400 23.98378 ? 79  LYS A CD  1 
ATOM   661  C  CD  B LYS A 1 76  ? -9.51400  20.29000  81.13100 0.320 15.53378 ? 79  LYS A CD  1 
ATOM   662  C  CD  C LYS A 1 76  ? -9.19100  20.67100  81.82700 0.280 10.84378 ? 79  LYS A CD  1 
ATOM   663  C  CE  A LYS A 1 76  ? -9.44900  19.59200  79.45400 0.400 24.77378 ? 79  LYS A CE  1 
ATOM   664  C  CE  B LYS A 1 76  ? -9.75600  20.60500  79.66800 0.320 27.74378 ? 79  LYS A CE  1 
ATOM   665  C  CE  C LYS A 1 76  ? -8.97900  21.38100  80.50300 0.280 19.40378 ? 79  LYS A CE  1 
ATOM   666  N  NZ  A LYS A 1 76  ? -9.73900  18.99800  78.13300 0.400 10.76378 ? 79  LYS A NZ  1 
ATOM   667  N  NZ  B LYS A 1 76  ? -10.15100 22.01600  79.46100 0.320 14.77378 ? 79  LYS A NZ  1 
ATOM   668  N  NZ  C LYS A 1 76  ? -8.86300  22.85300  80.69500 0.280 23.86378 ? 79  LYS A NZ  1 
ATOM   669  N  N   . ARG A 1 77  ? -9.06700  16.39600  85.39800 1.000 10.90246 ? 80  ARG A N   1 
ATOM   670  C  CA  . ARG A 1 77  ? -8.29800  16.03900  86.58600 1.000 11.25250 ? 80  ARG A CA  1 
ATOM   671  C  C   . ARG A 1 77  ? -7.85300  14.58200  86.58100 1.000 9.94708  ? 80  ARG A C   1 
ATOM   672  O  O   . ARG A 1 77  ? -7.12900  14.17100  87.49100 1.000 10.64190 ? 80  ARG A O   1 
ATOM   673  C  CB  . ARG A 1 77  ? -9.08000  16.36700  87.86000 1.000 13.38170 ? 80  ARG A CB  1 
ATOM   674  C  CG  . ARG A 1 77  ? -10.23000 15.41500  88.15100 1.000 15.37668 ? 80  ARG A CG  1 
ATOM   675  C  CD  . ARG A 1 77  ? -11.10700 15.98300  89.26900 1.000 18.88499 ? 80  ARG A CD  1 
ATOM   676  N  NE  . ARG A 1 77  ? -12.34600 15.24100  89.47900 1.000 21.04052 ? 80  ARG A NE  1 
ATOM   677  C  CZ  . ARG A 1 77  ? -12.50700 14.29200  90.39300 1.000 20.16410 ? 80  ARG A CZ  1 
ATOM   678  N  NH1 . ARG A 1 77  ? -11.50800 13.90200  91.16600 1.000 20.45378 ? 80  ARG A NH1 1 
ATOM   679  N  NH2 . ARG A 1 77  ? -13.69700 13.71000  90.52400 1.000 22.04378 ? 80  ARG A NH2 1 
ATOM   680  N  N   . HIS A 1 78  ? -8.22900  13.80700  85.56700 1.000 9.06803  ? 81  HIS A N   1 
ATOM   681  C  CA  . HIS A 1 78  ? -7.84500  12.40600  85.47000 1.000 8.31004  ? 81  HIS A CA  1 
ATOM   682  C  C   . HIS A 1 78  ? -6.79400  12.14700  84.40500 1.000 8.11002  ? 81  HIS A C   1 
ATOM   683  O  O   . HIS A 1 78  ? -6.48900  10.98400  84.14600 1.000 9.48387  ? 81  HIS A O   1 
ATOM   684  C  CB  . HIS A 1 78  ? -9.08000  11.54000  85.20300 1.000 9.25752  ? 81  HIS A CB  1 
ATOM   685  C  CG  . HIS A 1 78  ? -10.15900 11.74900  86.20000 1.000 9.44176  ? 81  HIS A CG  1 
ATOM   686  N  ND1 . HIS A 1 78  ? -10.04600 11.34100  87.51400 1.000 10.93667 ? 81  HIS A ND1 1 
ATOM   687  C  CD2 . HIS A 1 78  ? -11.35300 12.36900  86.08600 1.000 10.92878 ? 81  HIS A CD2 1 
ATOM   688  C  CE1 . HIS A 1 78  ? -11.14200 11.69200  88.16300 1.000 11.18144 ? 81  HIS A CE1 1 
ATOM   689  N  NE2 . HIS A 1 78  ? -11.95300 12.30200  87.31500 1.000 11.61570 ? 81  HIS A NE2 1 
ATOM   690  N  N   . ASP A 1 79  ? -6.21700  13.18700  83.80400 1.000 8.16002  ? 82  ASP A N   1 
ATOM   691  C  CA  . ASP A 1 79  ? -5.29700  13.01000  82.68300 1.000 7.52047  ? 82  ASP A CA  1 
ATOM   692  C  C   . ASP A 1 79  ? -3.87200  12.95300  83.22700 1.000 7.93368  ? 82  ASP A C   1 
ATOM   693  O  O   . ASP A 1 79  ? -3.15000  13.95100  83.28400 1.000 8.03633  ? 82  ASP A O   1 
ATOM   694  C  CB  . ASP A 1 79  ? -5.50900  14.13600  81.68400 1.000 8.40479  ? 82  ASP A CB  1 
ATOM   695  C  CG  . ASP A 1 79  ? -4.68700  13.98200  80.42100 1.000 8.16266  ? 82  ASP A CG  1 
ATOM   696  O  OD1 . ASP A 1 79  ? -3.80300  13.08200  80.36200 1.000 7.66523  ? 82  ASP A OD1 1 
ATOM   697  O  OD2 . ASP A 1 79  ? -4.92900  14.79300  79.49100 1.000 8.10475  ? 82  ASP A OD2 1 
ATOM   698  N  N   . PHE A 1 80  ? -3.45300  11.74600  83.61600 1.000 8.20740  ? 83  PHE A N   1 
ATOM   699  C  CA  . PHE A 1 80  ? -2.08700  11.55400  84.08800 1.000 8.32320  ? 83  PHE A CA  1 
ATOM   700  C  C   . PHE A 1 80  ? -1.08000  11.92100  83.00800 1.000 7.44152  ? 83  PHE A C   1 
ATOM   701  O  O   . PHE A 1 80  ? -0.02900  12.52100  83.28400 1.000 8.13897  ? 83  PHE A O   1 
ATOM   702  C  CB  . PHE A 1 80  ? -1.87600  10.08900  84.48800 1.000 8.91801  ? 83  PHE A CB  1 
ATOM   703  C  CG  . PHE A 1 80  ? -0.41800  9.72100   84.61500 1.000 9.39175  ? 83  PHE A CG  1 
ATOM   704  C  CD1 . PHE A 1 80  ? 0.27400   9.98800   85.78400 1.000 10.17079 ? 83  PHE A CD1 1 
ATOM   705  C  CD2 . PHE A 1 80  ? 0.26900   9.14000   83.55100 1.000 8.52323  ? 83  PHE A CD2 1 
ATOM   706  C  CE1 . PHE A 1 80  ? 1.61400   9.67700   85.89500 1.000 10.79192 ? 83  PHE A CE1 1 
ATOM   707  C  CE2 . PHE A 1 80  ? 1.62100   8.84900   83.65800 1.000 9.44439  ? 83  PHE A CE2 1 
ATOM   708  C  CZ  . PHE A 1 80  ? 2.28800   9.12000   84.83900 1.000 10.48399 ? 83  PHE A CZ  1 
ATOM   709  N  N   . PHE A 1 81  ? -1.36400  11.50200  81.77200 1.000 7.73892  ? 84  PHE A N   1 
ATOM   710  C  CA  . PHE A 1 81  ? -0.36200  11.54200  80.71600 1.000 7.08621  ? 84  PHE A CA  1 
ATOM   711  C  C   . PHE A 1 81  ? 0.13400   12.95700  80.45400 1.000 7.27571  ? 84  PHE A C   1 
ATOM   712  O  O   . PHE A 1 81  ? 1.34300   13.20300  80.37000 1.000 8.23372  ? 84  PHE A O   1 
ATOM   713  C  CB  . PHE A 1 81  ? -0.96200  10.97000  79.44000 1.000 7.06779  ? 84  PHE A CB  1 
ATOM   714  C  CG  . PHE A 1 81  ? -1.52800  9.58400   79.58700 1.000 7.06779  ? 84  PHE A CG  1 
ATOM   715  C  CD1 . PHE A 1 81  ? -0.68600  8.48600   79.61400 1.000 7.25202  ? 84  PHE A CD1 1 
ATOM   716  C  CD2 . PHE A 1 81  ? -2.89900  9.38300   79.66000 1.000 7.61259  ? 84  PHE A CD2 1 
ATOM   717  C  CE1 . PHE A 1 81  ? -1.19100  7.20700   79.72200 1.000 7.79682  ? 84  PHE A CE1 1 
ATOM   718  C  CE2 . PHE A 1 81  ? -3.42300  8.10000   79.79200 1.000 7.87315  ? 84  PHE A CE2 1 
ATOM   719  C  CZ  . PHE A 1 81  ? -2.56200  7.01700   79.80900 1.000 7.91789  ? 84  PHE A CZ  1 
ATOM   720  N  N   . LYS A 1 82  ? -0.78700  13.90700  80.28400 1.000 7.28097  ? 85  LYS A N   1 
ATOM   721  C  CA  . LYS A 1 82  ? -0.33100  15.27600  80.07100 1.000 8.07054  ? 85  LYS A CA  1 
ATOM   722  C  C   . LYS A 1 82  ? 0.26500   15.87100  81.33300 1.000 8.20213  ? 85  LYS A C   1 
ATOM   723  O  O   . LYS A 1 82  ? 1.17600   16.70600  81.25900 1.000 8.71535  ? 85  LYS A O   1 
ATOM   724  C  CB  . LYS A 1 82  ? -1.46600  16.16700  79.57000 1.000 7.96526  ? 85  LYS A CB  1 
ATOM   725  C  CG  . LYS A 1 82  ? -2.03600  15.76300  78.22200 1.000 7.33624  ? 85  LYS A CG  1 
ATOM   726  C  CD  . LYS A 1 82  ? -3.11100  16.76800  77.78100 1.000 7.39678  ? 85  LYS A CD  1 
ATOM   727  C  CE  . LYS A 1 82  ? -3.82500  16.34500  76.52000 1.000 7.46784  ? 85  LYS A CE  1 
ATOM   728  N  NZ  . LYS A 1 82  ? -4.51300  15.01400  76.73800 1.000 7.52047  ? 85  LYS A NZ  1 
ATOM   729  N  N   . SER A 1 83  ? -0.22300  15.45300  82.50000 1.000 8.76010  ? 86  SER A N   1 
ATOM   730  C  CA  . SER A 1 83  ? 0.24500   16.07900  83.72700 1.000 9.58914  ? 86  SER A CA  1 
ATOM   731  C  C   . SER A 1 83  ? 1.71500   15.80300  83.97900 1.000 9.20225  ? 86  SER A C   1 
ATOM   732  O  O   . SER A 1 83  ? 2.36600   16.60200  84.65400 1.000 10.91825 ? 86  SER A O   1 
ATOM   733  C  CB  . SER A 1 83  ? -0.58900  15.59900  84.91000 1.000 10.14710 ? 86  SER A CB  1 
ATOM   734  O  OG  . SER A 1 83  ? -0.16800  14.32300  85.35700 1.000 9.95761  ? 86  SER A OG  1 
ATOM   735  N  N   . ALA A 1 84  ? 2.24800   14.70700  83.43600 1.000 8.59955  ? 87  ALA A N   1 
ATOM   736  C  CA  . ALA A 1 84  ? 3.65800   14.35100  83.58600 1.000 8.14160  ? 87  ALA A CA  1 
ATOM   737  C  C   . ALA A 1 84  ? 4.56900   15.14900  82.66600 1.000 8.50217  ? 87  ALA A C   1 
ATOM   738  O  O   . ALA A 1 84  ? 5.78600   15.04400  82.79200 1.000 9.16014  ? 87  ALA A O   1 
ATOM   739  C  CB  . ALA A 1 84  ? 3.83800   12.84600  83.33600 1.000 8.97591  ? 87  ALA A CB  1 
ATOM   740  N  N   . MET A 1 85  ? 4.02000   15.94800  81.76500 1.000 8.73641  ? 88  MET A N   1 
ATOM   741  C  CA  . MET A 1 85  ? 4.80900   16.66500  80.77600 1.000 9.27332  ? 88  MET A CA  1 
ATOM   742  C  C   . MET A 1 85  ? 5.23200   18.02800  81.32000 1.000 9.57335  ? 88  MET A C   1 
ATOM   743  O  O   . MET A 1 85  ? 4.52100   18.62800  82.13800 1.000 10.43135 ? 88  MET A O   1 
ATOM   744  C  CB  . MET A 1 85  ? 3.99500   16.84000  79.50500 1.000 8.96802  ? 88  MET A CB  1 
ATOM   745  C  CG  . MET A 1 85  ? 3.66500   15.51200  78.87700 1.000 8.52586  ? 88  MET A CG  1 
ATOM   746  S  SD  . MET A 1 85  ? 5.15900   14.64700  78.32600 1.000 8.67324  ? 88  MET A SD  1 
ATOM   747  C  CE  . MET A 1 85  ? 4.46900   12.98500  78.17400 1.000 9.10751  ? 88  MET A CE  1 
ATOM   748  N  N   . PRO A 1 86  ? 6.37100   18.57600  80.86900 1.000 9.67600  ? 89  PRO A N   1 
ATOM   749  C  CA  . PRO A 1 86  ? 7.19800   18.06700  79.76700 1.000 9.79969  ? 89  PRO A CA  1 
ATOM   750  C  C   . PRO A 1 86  ? 8.21900   17.00200  80.14100 1.000 9.66284  ? 89  PRO A C   1 
ATOM   751  O  O   . PRO A 1 86  ? 8.81000   16.41400  79.23400 1.000 9.61809  ? 89  PRO A O   1 
ATOM   752  C  CB  . PRO A 1 86  ? 7.93500   19.32600  79.30500 1.000 10.89193 ? 89  PRO A CB  1 
ATOM   753  C  CG  . PRO A 1 86  ? 8.08100   20.12800  80.55200 1.000 12.26578 ? 89  PRO A CG  1 
ATOM   754  C  CD  . PRO A 1 86  ? 6.81400   19.91000  81.33000 1.000 11.24197 ? 89  PRO A CD  1 
ATOM   755  N  N   . GLU A 1 87  ? 8.45500   16.77600  81.43400 1.000 9.46281  ? 90  GLU A N   1 
ATOM   756  C  CA  A GLU A 1 87  ? 9.51600   15.84900  81.82800 0.680 10.26028 ? 90  GLU A CA  1 
ATOM   757  C  CA  B GLU A 1 87  ? 9.50900   15.85000  81.84500 0.320 9.30378  ? 90  GLU A CA  1 
ATOM   758  C  C   . GLU A 1 87  ? 9.22600   14.42400  81.38400 1.000 9.33122  ? 90  GLU A C   1 
ATOM   759  O  O   . GLU A 1 87  ? 10.16300  13.66500  81.08200 1.000 9.75495  ? 90  GLU A O   1 
ATOM   760  C  CB  A GLU A 1 87  ? 9.72800   15.89200  83.34000 0.680 12.97902 ? 90  GLU A CB  1 
ATOM   761  C  CB  B GLU A 1 87  ? 9.67400   15.90600  83.36300 0.320 8.49378  ? 90  GLU A CB  1 
ATOM   762  C  CG  A GLU A 1 87  ? 10.26100  17.23200  83.86100 0.680 16.28731 ? 90  GLU A CG  1 
ATOM   763  C  CG  B GLU A 1 87  ? 9.88100   17.32300  83.92700 0.320 14.97378 ? 90  GLU A CG  1 
ATOM   764  C  CD  A GLU A 1 87  ? 9.17900   18.29200  84.05000 0.680 18.62444 ? 90  GLU A CD  1 
ATOM   765  C  CD  B GLU A 1 87  ? 8.58200   18.00300  84.36800 0.320 15.05378 ? 90  GLU A CD  1 
ATOM   766  O  OE1 A GLU A 1 87  ? 7.96900   17.96500  83.98300 0.680 18.95079 ? 90  GLU A OE1 1 
ATOM   767  O  OE1 B GLU A 1 87  ? 7.51600   17.74900  83.76700 0.320 11.77378 ? 90  GLU A OE1 1 
ATOM   768  O  OE2 A GLU A 1 87  ? 9.54900   19.46500  84.27900 0.680 23.92378 ? 90  GLU A OE2 1 
ATOM   769  O  OE2 B GLU A 1 87  ? 8.62900   18.79700  85.33300 0.320 15.30378 ? 90  GLU A OE2 1 
ATOM   770  N  N   . GLY A 1 88  ? 7.95800   14.04400  81.34600 1.000 8.18898  ? 91  GLY A N   1 
ATOM   771  C  CA  . GLY A 1 88  ? 7.54600   12.81200  80.69800 1.000 8.44690  ? 91  GLY A CA  1 
ATOM   772  C  C   . GLY A 1 88  ? 7.25100   11.67100  81.64700 1.000 7.83893  ? 91  GLY A C   1 
ATOM   773  O  O   . GLY A 1 88  ? 7.21600   11.81400  82.87200 1.000 7.74155  ? 91  GLY A O   1 
ATOM   774  N  N   . TYR A 1 89  ? 7.04600   10.50100  81.04600 1.000 7.80472  ? 92  TYR A N   1 
ATOM   775  C  CA  . TYR A 1 89  ? 6.81100   9.29300   81.81800 1.000 7.77840  ? 92  TYR A CA  1 
ATOM   776  C  C   . TYR A 1 89  ? 7.48200   8.09200   81.16600 1.000 7.57311  ? 92  TYR A C   1 
ATOM   777  O  O   . TYR A 1 89  ? 7.71400   8.05500   79.95700 1.000 7.32835  ? 92  TYR A O   1 
ATOM   778  C  CB  . TYR A 1 89  ? 5.30700   9.01900   82.01500 1.000 8.47059  ? 92  TYR A CB  1 
ATOM   779  C  CG  . TYR A 1 89  ? 4.45800   9.05500   80.75500 1.000 7.65470  ? 92  TYR A CG  1 
ATOM   780  C  CD1 . TYR A 1 89  ? 4.41900   7.97000   79.87500 1.000 7.80998  ? 92  TYR A CD1 1 
ATOM   781  C  CD2 . TYR A 1 89  ? 3.66400   10.15400  80.46700 1.000 8.02317  ? 92  TYR A CD2 1 
ATOM   782  C  CE1 . TYR A 1 89  ? 3.63400   8.00500   78.72400 1.000 7.55469  ? 92  TYR A CE1 1 
ATOM   783  C  CE2 . TYR A 1 89  ? 2.87600   10.19700  79.32700 1.000 7.42046  ? 92  TYR A CE2 1 
ATOM   784  C  CZ  . TYR A 1 89  ? 2.84900   9.11400   78.47300 1.000 7.01515  ? 92  TYR A CZ  1 
ATOM   785  O  OH  . TYR A 1 89  ? 2.04200   9.17700   77.36400 1.000 7.13095  ? 92  TYR A OH  1 
ATOM   786  N  N   . VAL A 1 90  ? 7.76100   7.10100   81.99200 1.000 7.61522  ? 93  VAL A N   1 
ATOM   787  C  CA  . VAL A 1 90  ? 8.12200   5.76300   81.55100 1.000 7.39151  ? 93  VAL A CA  1 
ATOM   788  C  C   . VAL A 1 90  ? 6.82300   5.01000   81.31000 1.000 8.11002  ? 93  VAL A C   1 
ATOM   789  O  O   . VAL A 1 90  ? 5.88800   5.11600   82.10400 1.000 9.34175  ? 93  VAL A O   1 
ATOM   790  C  CB  . VAL A 1 90  ? 8.95900   5.05400   82.63700 1.000 8.90485  ? 93  VAL A CB  1 
ATOM   791  C  CG1 . VAL A 1 90  ? 9.31300   3.65900   82.18100 1.000 9.37333  ? 93  VAL A CG1 1 
ATOM   792  C  CG2 . VAL A 1 90  ? 10.23900  5.85200   82.95000 1.000 9.83917  ? 93  VAL A CG2 1 
ATOM   793  N  N   . GLN A 1 91  ? 6.75600   4.26600   80.21000 1.000 6.97567  ? 94  GLN A N   1 
ATOM   794  C  CA  . GLN A 1 91  ? 5.61200   3.42000   79.91700 1.000 7.67839  ? 94  GLN A CA  1 
ATOM   795  C  C   . GLN A 1 91  ? 6.15300   2.03500   79.64500 1.000 7.56522  ? 94  GLN A C   1 
ATOM   796  O  O   . GLN A 1 91  ? 6.95300   1.85200   78.72300 1.000 6.88882  ? 94  GLN A O   1 
ATOM   797  C  CB  . GLN A 1 91  ? 4.85200   3.93000   78.69700 1.000 7.44941  ? 94  GLN A CB  1 
ATOM   798  C  CG  . GLN A 1 91  ? 3.66700   3.03200   78.33200 1.000 7.50205  ? 94  GLN A CG  1 
ATOM   799  C  CD  . GLN A 1 91  ? 2.67800   3.74000   77.42500 1.000 7.14148  ? 94  GLN A CD  1 
ATOM   800  O  OE1 . GLN A 1 91  ? 2.08600   4.75700   77.81500 1.000 6.87566  ? 94  GLN A OE1 1 
ATOM   801  N  NE2 . GLN A 1 91  ? 2.46500   3.19400   76.22400 1.000 7.44678  ? 94  GLN A NE2 1 
ATOM   802  N  N   . GLU A 1 92  ? 5.73800   1.07300   80.45400 1.000 7.59680  ? 95  GLU A N   1 
ATOM   803  C  CA  . GLU A 1 92  ? 6.19800   -0.30400  80.32400 1.000 7.89420  ? 95  GLU A CA  1 
ATOM   804  C  C   . GLU A 1 92  ? 5.00200   -1.19600  80.03900 1.000 7.27571  ? 95  GLU A C   1 
ATOM   805  O  O   . GLU A 1 92  ? 3.91700   -0.97900  80.59400 1.000 8.34163  ? 95  GLU A O   1 
ATOM   806  C  CB  . GLU A 1 92  ? 6.83400   -0.77300  81.62800 1.000 12.88954 ? 95  GLU A CB  1 
ATOM   807  C  CG  . GLU A 1 92  ? 8.15300   -0.09600  81.92200 1.000 21.73007 ? 95  GLU A CG  1 
ATOM   808  C  CD  . GLU A 1 92  ? 8.62400   -0.34300  83.33900 1.000 33.17378 ? 95  GLU A CD  1 
ATOM   809  O  OE1 . GLU A 1 92  ? 8.16300   0.36000   84.27000 1.000 24.89378 ? 95  GLU A OE1 1 
ATOM   810  O  OE2 . GLU A 1 92  ? 9.45500   -1.25300  83.51400 1.000 30.87378 ? 95  GLU A OE2 1 
ATOM   811  N  N   . ARG A 1 93  ? 5.19300   -2.20500  79.18900 1.000 6.83618  ? 96  ARG A N   1 
ATOM   812  C  CA  . ARG A 1 93  ? 4.12700   -3.17500  78.97700 1.000 7.04147  ? 96  ARG A CA  1 
ATOM   813  C  C   . ARG A 1 93  ? 4.67600   -4.57900  78.86700 1.000 6.53878  ? 96  ARG A C   1 
ATOM   814  O  O   . ARG A 1 93  ? 5.82500   -4.79300  78.46700 1.000 7.14938  ? 96  ARG A O   1 
ATOM   815  C  CB  . ARG A 1 93  ? 3.35100   -2.94200  77.68000 1.000 6.63879  ? 96  ARG A CB  1 
ATOM   816  C  CG  . ARG A 1 93  ? 2.58600   -1.64100  77.63800 1.000 6.94409  ? 96  ARG A CG  1 
ATOM   817  C  CD  . ARG A 1 93  ? 1.38300   -1.81200  76.72200 1.000 6.90198  ? 96  ARG A CD  1 
ATOM   818  N  NE  . ARG A 1 93  ? 0.53200   -0.62400  76.61200 1.000 6.64142  ? 96  ARG A NE  1 
ATOM   819  C  CZ  . ARG A 1 93  ? 0.61500   0.29900   75.65500 1.000 6.04398  ? 96  ARG A CZ  1 
ATOM   820  N  NH1 . ARG A 1 93  ? 1.54000   0.23800   74.71400 1.000 6.32033  ? 96  ARG A NH1 1 
ATOM   821  N  NH2 . ARG A 1 93  ? -0.27400  1.29600   75.62700 1.000 6.53088  ? 96  ARG A NH2 1 
ATOM   822  N  N   . THR A 1 94  ? 3.79900   -5.53700  79.16900 1.000 6.97567  ? 97  THR A N   1 
ATOM   823  C  CA  . THR A 1 94  ? 3.90800   -6.90500  78.68200 1.000 6.91777  ? 97  THR A CA  1 
ATOM   824  C  C   . THR A 1 94  ? 2.72000   -7.12500  77.76200 1.000 6.80986  ? 97  THR A C   1 
ATOM   825  O  O   . THR A 1 94  ? 1.56800   -6.92400  78.16500 1.000 7.32571  ? 97  THR A O   1 
ATOM   826  C  CB  . THR A 1 94  ? 3.87900   -7.91100  79.83100 1.000 8.51796  ? 97  THR A CB  1 
ATOM   827  O  OG1 . THR A 1 94  ? 4.99300   -7.65200  80.68600 1.000 9.48913  ? 97  THR A OG1 1 
ATOM   828  C  CG2 . THR A 1 94  ? 3.98600   -9.35500  79.28800 1.000 9.30227  ? 97  THR A CG2 1 
ATOM   829  N  N   . ILE A 1 95  ? 3.00400   -7.50200  76.52900 1.000 6.59142  ? 98  ILE A N   1 
ATOM   830  C  CA  . ILE A 1 95  ? 1.98300   -7.85400  75.54600 1.000 6.53351  ? 98  ILE A CA  1 
ATOM   831  C  C   . ILE A 1 95  ? 2.09000   -9.35700  75.33100 1.000 7.07042  ? 98  ILE A C   1 
ATOM   832  O  O   . ILE A 1 95  ? 3.11400   -9.85800  74.83900 1.000 6.97567  ? 98  ILE A O   1 
ATOM   833  C  CB  . ILE A 1 95  ? 2.17400   -7.10000  74.22900 1.000 6.82039  ? 98  ILE A CB  1 
ATOM   834  C  CG1 . ILE A 1 95  ? 2.10300   -5.59500  74.47700 1.000 7.48363  ? 98  ILE A CG1 1 
ATOM   835  C  CG2 . ILE A 1 95  ? 1.11300   -7.55000  73.23800 1.000 7.47310  ? 98  ILE A CG2 1 
ATOM   836  C  CD1 . ILE A 1 95  ? 2.50200   -4.75700  73.26900 1.000 7.60996  ? 98  ILE A CD1 1 
ATOM   837  N  N   . SER A 1 96  ? 1.04700   -10.09600 75.72300 1.000 7.11253  ? 99  SER A N   1 
ATOM   838  C  CA  A SER A 1 96  ? 1.05300   -11.55600 75.66800 0.750 7.17043  ? 99  SER A CA  1 
ATOM   839  C  CA  B SER A 1 96  ? 1.05200   -11.55400 75.67200 0.250 8.13378  ? 99  SER A CA  1 
ATOM   840  C  C   . SER A 1 96  ? 0.19000   -11.99500 74.49600 1.000 6.86250  ? 99  SER A C   1 
ATOM   841  O  O   . SER A 1 96  ? -1.03400  -11.82900 74.52100 1.000 7.40993  ? 99  SER A O   1 
ATOM   842  C  CB  A SER A 1 96  ? 0.50700   -12.10800 76.97700 0.750 7.97053  ? 99  SER A CB  1 
ATOM   843  C  CB  B SER A 1 96  ? 0.50700   -12.12200 76.98100 0.250 7.67378  ? 99  SER A CB  1 
ATOM   844  O  OG  A SER A 1 96  ? 1.23300   -11.53900 78.04100 0.750 8.94170  ? 99  SER A OG  1 
ATOM   845  O  OG  B SER A 1 96  ? 0.35300   -13.52700 76.90100 0.250 8.67378  ? 99  SER A OG  1 
ATOM   846  N  N   . PHE A 1 97  ? 0.82400   -12.55300 73.46600 1.000 7.08621  ? 100 PHE A N   1 
ATOM   847  C  CA  . PHE A 1 97  ? 0.07800   -13.05900 72.31800 1.000 7.10990  ? 100 PHE A CA  1 
ATOM   848  C  C   . PHE A 1 97  ? -0.39700  -14.45900 72.65500 1.000 7.67312  ? 100 PHE A C   1 
ATOM   849  O  O   . PHE A 1 97  ? 0.41500   -15.36000 72.88900 1.000 7.63365  ? 100 PHE A O   1 
ATOM   850  C  CB  . PHE A 1 97  ? 0.96100   -13.04000 71.07500 1.000 7.58890  ? 100 PHE A CB  1 
ATOM   851  C  CG  . PHE A 1 97  ? 1.32900   -11.64500 70.65500 1.000 6.55983  ? 100 PHE A CG  1 
ATOM   852  C  CD1 . PHE A 1 97  ? 0.49200   -10.93000 69.81200 1.000 7.14148  ? 100 PHE A CD1 1 
ATOM   853  C  CD2 . PHE A 1 97  ? 2.48400   -11.03600 71.12300 1.000 6.86513  ? 100 PHE A CD2 1 
ATOM   854  C  CE1 . PHE A 1 97  ? 0.80400   -9.63000  69.42900 1.000 7.60206  ? 100 PHE A CE1 1 
ATOM   855  C  CE2 . PHE A 1 97  ? 2.80300   -9.73200  70.76100 1.000 7.05726  ? 100 PHE A CE2 1 
ATOM   856  C  CZ  . PHE A 1 97  ? 1.96400   -9.02800  69.90000 1.000 6.51772  ? 100 PHE A CZ  1 
ATOM   857  N  N   . LYS A 1 98  ? -1.71500  -14.64800 72.70100 1.000 7.71523  ? 101 LYS A N   1 
ATOM   858  C  CA  A LYS A 1 98  ? -2.27200  -15.92700 73.11200 0.440 11.43378 ? 101 LYS A CA  1 
ATOM   859  C  CA  B LYS A 1 98  ? -2.28200  -15.92900 73.10700 0.560 8.84958  ? 101 LYS A CA  1 
ATOM   860  C  C   . LYS A 1 98  ? -1.71800  -17.05000 72.24800 1.000 10.09710 ? 101 LYS A C   1 
ATOM   861  O  O   . LYS A 1 98  ? -1.69100  -16.95100 71.01500 1.000 9.87076  ? 101 LYS A O   1 
ATOM   862  C  CB  A LYS A 1 98  ? -3.79200  -15.87600 72.99800 0.440 11.82378 ? 101 LYS A CB  1 
ATOM   863  C  CB  B LYS A 1 98  ? -3.80500  -15.87600 72.96100 0.560 9.60757  ? 101 LYS A CB  1 
ATOM   864  C  CG  A LYS A 1 98  ? -4.48200  -17.08100 73.60500 0.440 16.79378 ? 101 LYS A CG  1 
ATOM   865  C  CG  B LYS A 1 98  ? -4.50500  -17.19500 73.30200 0.560 10.94457 ? 101 LYS A CG  1 
ATOM   866  C  CD  A LYS A 1 98  ? -5.85100  -16.68800 74.11400 0.440 23.61378 ? 101 LYS A CD  1 
ATOM   867  C  CD  B LYS A 1 98  ? -6.00300  -16.97000 73.49200 0.560 13.16062 ? 101 LYS A CD  1 
ATOM   868  C  CE  A LYS A 1 98  ? -6.93800  -17.52900 73.48500 0.440 52.28378 ? 101 LYS A CE  1 
ATOM   869  C  CE  B LYS A 1 98  ? -6.68100  -18.21300 74.06600 0.560 14.88188 ? 101 LYS A CE  1 
ATOM   870  N  NZ  A LYS A 1 98  ? -8.26700  -16.95300 73.79600 0.440 12.68378 ? 101 LYS A NZ  1 
ATOM   871  N  NZ  B LYS A 1 98  ? -6.22500  -18.50800 75.46100 0.560 16.28205 ? 101 LYS A NZ  1 
ATOM   872  N  N   . ASP A 1 99  ? -1.27800  -18.12300 72.91800 1.000 10.02341 ? 102 ASP A N   1 
ATOM   873  C  CA  A ASP A 1 99  ? -0.69000  -19.30700 72.30400 0.590 10.68401 ? 102 ASP A CA  1 
ATOM   874  C  CA  B ASP A 1 99  ? -0.72600  -19.30200 72.24800 0.410 10.57378 ? 102 ASP A CA  1 
ATOM   875  C  C   . ASP A 1 99  ? 0.55900   -18.98800 71.48200 1.000 10.10763 ? 102 ASP A C   1 
ATOM   876  O  O   . ASP A 1 99  ? 0.93800   -19.73100 70.57000 1.000 11.31567 ? 102 ASP A O   1 
ATOM   877  C  CB  A ASP A 1 99  ? -1.74200  -20.14600 71.57400 0.590 13.12115 ? 102 ASP A CB  1 
ATOM   878  C  CB  B ASP A 1 99  ? -1.76600  -20.00100 71.34900 0.410 16.35378 ? 102 ASP A CB  1 
ATOM   879  C  CG  A ASP A 1 99  ? -2.81700  -20.65500 72.53000 0.590 15.11086 ? 102 ASP A CG  1 
ATOM   880  C  CG  B ASP A 1 99  ? -1.30900  -21.37600 70.86500 0.410 16.35378 ? 102 ASP A CG  1 
ATOM   881  O  OD1 A ASP A 1 99  ? -2.46500  -21.00500 73.68100 0.590 16.70315 ? 102 ASP A OD1 1 
ATOM   882  O  OD1 B ASP A 1 99  ? -0.75600  -22.14600 71.67800 0.410 18.67378 ? 102 ASP A OD1 1 
ATOM   883  O  OD2 A ASP A 1 99  ? -4.00200  -20.66300 72.15700 0.590 17.15058 ? 102 ASP A OD2 1 
ATOM   884  O  OD2 B ASP A 1 99  ? -1.50300  -21.68200 69.67000 0.410 24.58378 ? 102 ASP A OD2 1 
ATOM   885  N  N   . ASP A 1 100 ? 1.24500   -17.90800 71.83700 1.000 9.04434  ? 103 ASP A N   1 
ATOM   886  C  CA  . ASP A 1 100 ? 2.46300   -17.50700 71.13600 1.000 8.09423  ? 103 ASP A CA  1 
ATOM   887  C  C   . ASP A 1 100 ? 3.33100   -16.72700 72.12500 1.000 7.90473  ? 103 ASP A C   1 
ATOM   888  O  O   . ASP A 1 100 ? 3.17300   -16.85400 73.34500 1.000 8.16792  ? 103 ASP A O   1 
ATOM   889  C  CB  . ASP A 1 100 ? 2.08000   -16.78200 69.82500 1.000 8.42848  ? 103 ASP A CB  1 
ATOM   890  C  CG  . ASP A 1 100 ? 3.14200   -16.89000 68.73600 1.000 8.99697  ? 103 ASP A CG  1 
ATOM   891  O  OD1 . ASP A 1 100 ? 4.32200   -17.10300 69.05500 1.000 9.54966  ? 103 ASP A OD1 1 
ATOM   892  O  OD2 . ASP A 1 100 ? 2.79800   -16.75900 67.54000 1.000 10.08394 ? 103 ASP A OD2 1 
ATOM   893  N  N   . GLY A 1 101 ? 4.24000   -15.90400 71.60700 1.000 7.76261  ? 104 GLY A N   1 
ATOM   894  C  CA  . GLY A 1 101 ? 5.22200   -15.24100 72.43700 1.000 7.87841  ? 104 GLY A CA  1 
ATOM   895  C  C   . GLY A 1 101 ? 4.70600   -13.96500 73.08800 1.000 7.87315  ? 104 GLY A C   1 
ATOM   896  O  O   . GLY A 1 101 ? 3.51400   -13.64700 73.08500 1.000 7.67049  ? 104 GLY A O   1 
ATOM   897  N  N   . ASN A 1 102 ? 5.64100   -13.22500 73.67500 1.000 7.50468  ? 105 ASN A N   1 
ATOM   898  C  CA  . ASN A 1 102 ? 5.30100   -11.98300 74.35100 1.000 7.23623  ? 105 ASN A CA  1 
ATOM   899  C  C   . ASN A 1 102 ? 6.30200   -10.89700 73.99000 1.000 6.88356  ? 105 ASN A C   1 
ATOM   900  O  O   . ASN A 1 102 ? 7.47700   -11.17400 73.73500 1.000 6.90987  ? 105 ASN A O   1 
ATOM   901  C  CB  . ASN A 1 102 ? 5.23400   -12.13600 75.88000 1.000 7.89684  ? 105 ASN A CB  1 
ATOM   902  C  CG  . ASN A 1 102 ? 6.55000   -12.61200 76.47100 1.000 9.44702  ? 105 ASN A CG  1 
ATOM   903  O  OD1 . ASN A 1 102 ? 7.40500   -11.80500 76.84500 1.000 10.96036 ? 105 ASN A OD1 1 
ATOM   904  N  ND2 . ASN A 1 102 ? 6.71500   -13.91800 76.56700 1.000 10.40766 ? 105 ASN A ND2 1 
ATOM   905  N  N   . TYR A 1 103 ? 5.81400   -9.65900  73.97100 1.000 6.83618  ? 106 TYR A N   1 
ATOM   906  C  CA  . TYR A 1 103 ? 6.68500   -8.49200  73.94800 1.000 7.15464  ? 106 TYR A CA  1 
ATOM   907  C  C   . TYR A 1 103 ? 6.76100   -7.88100  75.33800 1.000 7.00989  ? 106 TYR A C   1 
ATOM   908  O  O   . TYR A 1 103 ? 5.75100   -7.78200  76.03600 1.000 7.33098  ? 106 TYR A O   1 
ATOM   909  C  CB  . TYR A 1 103 ? 6.14700   -7.38800  73.03000 1.000 7.06252  ? 106 TYR A CB  1 
ATOM   910  C  CG  . TYR A 1 103 ? 5.99000   -7.67800  71.55700 1.000 6.55720  ? 106 TYR A CG  1 
ATOM   911  C  CD1 . TYR A 1 103 ? 6.70200   -8.69100  70.91100 1.000 7.14675  ? 106 TYR A CD1 1 
ATOM   912  C  CD2 . TYR A 1 103 ? 5.12100   -6.89500  70.79300 1.000 6.80723  ? 106 TYR A CD2 1 
ATOM   913  C  CE1 . TYR A 1 103 ? 6.53800   -8.90700  69.53700 1.000 7.39151  ? 106 TYR A CE1 1 
ATOM   914  C  CE2 . TYR A 1 103 ? 4.96800   -7.10400  69.43000 1.000 7.21781  ? 106 TYR A CE2 1 
ATOM   915  C  CZ  . TYR A 1 103 ? 5.67300   -8.11500  68.80900 1.000 7.32045  ? 106 TYR A CZ  1 
ATOM   916  O  OH  . TYR A 1 103 ? 5.55100   -8.35600  67.47100 1.000 7.54153  ? 106 TYR A OH  1 
ATOM   917  N  N   . LYS A 1 104 ? 7.96000   -7.45500  75.72200 1.000 6.62300  ? 107 LYS A N   1 
ATOM   918  C  CA  A LYS A 1 104 ? 8.11800   -6.57000  76.85900 0.590 7.32045  ? 107 LYS A CA  1 
ATOM   919  C  CA  B LYS A 1 104 ? 8.17700   -6.59200  76.88100 0.410 6.50378  ? 107 LYS A CA  1 
ATOM   920  C  C   . LYS A 1 104 ? 8.70200   -5.28200  76.32400 1.000 6.93883  ? 107 LYS A C   1 
ATOM   921  O  O   . LYS A 1 104 ? 9.68900   -5.29300  75.57500 1.000 7.34414  ? 107 LYS A O   1 
ATOM   922  C  CB  A LYS A 1 104 ? 8.95800   -7.19600  77.97200 0.590 8.99697  ? 107 LYS A CB  1 
ATOM   923  C  CB  B LYS A 1 104 ? 9.24700   -7.18100  77.80700 0.410 7.90378  ? 107 LYS A CB  1 
ATOM   924  C  CG  A LYS A 1 104 ? 8.15600   -8.27500  78.68500 0.590 9.92076  ? 107 LYS A CG  1 
ATOM   925  C  CG  B LYS A 1 104 ? 8.87400   -8.48100  78.51200 0.410 9.40378  ? 107 LYS A CG  1 
ATOM   926  C  CD  A LYS A 1 104 ? 8.93700   -8.97300  79.77200 0.590 10.80771 ? 107 LYS A CD  1 
ATOM   927  C  CD  B LYS A 1 104 ? 8.01300   -8.22200  79.74200 0.410 9.15378  ? 107 LYS A CD  1 
ATOM   928  C  CE  A LYS A 1 104 ? 8.08700   -10.02400 80.47600 0.590 11.95522 ? 107 LYS A CE  1 
ATOM   929  C  CE  B LYS A 1 104 ? 7.63100   -9.53400  80.41800 0.410 9.18378  ? 107 LYS A CE  1 
ATOM   930  N  NZ  A LYS A 1 104 ? 7.09100   -9.43000  81.42200 0.590 12.36316 ? 107 LYS A NZ  1 
ATOM   931  N  NZ  B LYS A 1 104 ? 6.78400   -9.30700  81.62100 0.410 33.61378 ? 107 LYS A NZ  1 
ATOM   932  N  N   . THR A 1 105 ? 8.03900   -4.17700  76.64100 1.000 6.88356  ? 108 THR A N   1 
ATOM   933  C  CA  . THR A 1 105 ? 8.42700   -2.88600  76.10700 1.000 6.57826  ? 108 THR A CA  1 
ATOM   934  C  C   . THR A 1 105 ? 8.69500   -1.92500  77.24500 1.000 6.33612  ? 108 THR A C   1 
ATOM   935  O  O   . THR A 1 105 ? 8.00500   -1.94400  78.26900 1.000 7.54153  ? 108 THR A O   1 
ATOM   936  C  CB  . THR A 1 105 ? 7.34000   -2.31600  75.17100 1.000 6.79407  ? 108 THR A CB  1 
ATOM   937  O  OG1 . THR A 1 105 ? 6.12000   -2.09200  75.89000 1.000 7.39414  ? 108 THR A OG1 1 
ATOM   938  C  CG2 . THR A 1 105 ? 7.05500   -3.28300  74.02800 1.000 7.69418  ? 108 THR A CG2 1 
ATOM   939  N  N   . ARG A 1 106 ? 9.73600   -1.11600  77.08000 1.000 6.87829  ? 109 ARG A N   1 
ATOM   940  C  CA  A ARG A 1 106 ? 10.01800  -0.02400  77.99400 0.650 6.93883  ? 109 ARG A CA  1 
ATOM   941  C  CA  B ARG A 1 106 ? 10.01600  -0.02300  77.99500 0.350 7.86378  ? 109 ARG A CA  1 
ATOM   942  C  C   . ARG A 1 106 ? 10.22700  1.21600   77.14700 1.000 6.80723  ? 109 ARG A C   1 
ATOM   943  O  O   . ARG A 1 106 ? 11.11400  1.24300   76.29500 1.000 8.07844  ? 109 ARG A O   1 
ATOM   944  C  CB  A ARG A 1 106 ? 11.25300  -0.30400  78.85000 0.650 7.96000  ? 109 ARG A CB  1 
ATOM   945  C  CB  B ARG A 1 106 ? 11.24200  -0.31100  78.86500 0.350 8.33378  ? 109 ARG A CB  1 
ATOM   946  C  CG  A ARG A 1 106 ? 11.46500  0.77200   79.91000 0.650 9.22331  ? 109 ARG A CG  1 
ATOM   947  C  CG  B ARG A 1 106 ? 11.46700  0.74200   79.94800 0.350 13.70378 ? 109 ARG A CG  1 
ATOM   948  C  CD  A ARG A 1 106 ? 12.78600  0.61200   80.63100 0.650 10.04446 ? 109 ARG A CD  1 
ATOM   949  C  CD  B ARG A 1 106 ? 12.63900  0.38300   80.84400 0.350 16.60378 ? 109 ARG A CD  1 
ATOM   950  N  NE  A ARG A 1 106 ? 12.86500  1.48500   81.79700 0.650 10.99457 ? 109 ARG A NE  1 
ATOM   951  N  NE  B ARG A 1 106 ? 12.88300  1.39900   81.86300 0.350 17.65378 ? 109 ARG A NE  1 
ATOM   952  C  CZ  A ARG A 1 106 ? 13.12100  2.78400   81.73700 0.650 12.61319 ? 109 ARG A CZ  1 
ATOM   953  C  CZ  B ARG A 1 106 ? 12.47200  1.31800   83.12100 0.350 24.26378 ? 109 ARG A CZ  1 
ATOM   954  N  NH1 A ARG A 1 106 ? 13.35100  3.39000   80.58300 0.650 13.17115 ? 109 ARG A NH1 1 
ATOM   955  N  NH1 B ARG A 1 106 ? 11.80600  0.26400   83.56500 0.350 30.31378 ? 109 ARG A NH1 1 
ATOM   956  N  NH2 A ARG A 1 106 ? 13.16800  3.48600   82.86600 0.650 13.61331 ? 109 ARG A NH2 1 
ATOM   957  N  NH2 B ARG A 1 106 ? 12.74100  2.31700   83.95600 0.350 23.75378 ? 109 ARG A NH2 1 
ATOM   958  N  N   . ALA A 1 107 ? 9.41900   2.22900   77.38100 1.000 6.65195  ? 110 ALA A N   1 
ATOM   959  C  CA  . ALA A 1 107 ? 9.45500   3.44700   76.60100 1.000 7.23623  ? 110 ALA A CA  1 
ATOM   960  C  C   . ALA A 1 107 ? 9.54900   4.64000   77.53100 1.000 7.53363  ? 110 ALA A C   1 
ATOM   961  O  O   . ALA A 1 107 ? 9.11400   4.58800   78.67900 1.000 7.45468  ? 110 ALA A O   1 
ATOM   962  C  CB  . ALA A 1 107 ? 8.19600   3.60200   75.72900 1.000 7.70734  ? 110 ALA A CB  1 
ATOM   963  N  N   . GLU A 1 108 ? 10.12400  5.71200   77.01500 1.000 7.75208  ? 111 GLU A N   1 
ATOM   964  C  CA  . GLU A 1 108 ? 10.06700  7.01300   77.66600 1.000 8.17055  ? 111 GLU A CA  1 
ATOM   965  C  C   . GLU A 1 108 ? 9.42400   8.00200   76.71000 1.000 7.01515  ? 111 GLU A C   1 
ATOM   966  O  O   . GLU A 1 108 ? 9.82700   8.10300   75.54200 1.000 7.87841  ? 111 GLU A O   1 
ATOM   967  C  CB  . GLU A 1 108 ? 11.45700  7.46800   78.09500 1.000 10.41819 ? 111 GLU A CB  1 
ATOM   968  C  CG  . GLU A 1 108 ? 12.00200  6.53300   79.15400 1.000 13.17905 ? 111 GLU A CG  1 
ATOM   969  C  CD  . GLU A 1 108 ? 13.22100  7.05400   79.87500 1.000 16.44260 ? 111 GLU A CD  1 
ATOM   970  O  OE1 . GLU A 1 108 ? 13.64900  8.21000   79.63900 1.000 17.00056 ? 111 GLU A OE1 1 
ATOM   971  O  OE2 . GLU A 1 108 ? 13.75100  6.27500   80.69000 1.000 18.84288 ? 111 GLU A OE2 1 
ATOM   972  N  N   . VAL A 1 109 ? 8.38800   8.68300   77.20100 1.000 7.39414  ? 112 VAL A N   1 
ATOM   973  C  CA  . VAL A 1 109 ? 7.63200   9.65300   76.42500 1.000 7.54153  ? 112 VAL A CA  1 
ATOM   974  C  C   . VAL A 1 109 ? 7.86600   10.99900  77.08100 1.000 7.21517  ? 112 VAL A C   1 
ATOM   975  O  O   . VAL A 1 109 ? 7.52400   11.18600  78.25500 1.000 7.33361  ? 112 VAL A O   1 
ATOM   976  C  CB  . VAL A 1 109 ? 6.13600   9.30600   76.41900 1.000 8.34952  ? 112 VAL A CB  1 
ATOM   977  C  CG1 . VAL A 1 109 ? 5.38100   10.29100  75.54700 1.000 8.13107  ? 112 VAL A CG1 1 
ATOM   978  C  CG2 . VAL A 1 109 ? 5.92900   7.86100   75.95300 1.000 8.64429  ? 112 VAL A CG2 1 
ATOM   979  N  N   . LYS A 1 110 ? 8.43000   11.94500  76.33800 1.000 7.12832  ? 113 LYS A N   1 
ATOM   980  C  CA  A LYS A 1 110 ? 8.73600   13.24700  76.92300 0.500 7.22378  ? 113 LYS A CA  1 
ATOM   981  C  CA  B LYS A 1 110 ? 8.75500   13.24300  76.92300 0.500 7.07378  ? 113 LYS A CA  1 
ATOM   982  C  C   . LYS A 1 110 ? 8.95100   14.24400  75.79600 1.000 6.90987  ? 113 LYS A C   1 
ATOM   983  O  O   . LYS A 1 110 ? 9.09400   13.86900  74.63900 1.000 7.96000  ? 113 LYS A O   1 
ATOM   984  C  CB  A LYS A 1 110 ? 9.97500   13.17700  77.81700 0.500 9.02378  ? 113 LYS A CB  1 
ATOM   985  C  CB  B LYS A 1 110 ? 10.02600  13.16100  77.76900 0.500 8.30378  ? 113 LYS A CB  1 
ATOM   986  C  CG  A LYS A 1 110 ? 11.27900  12.98900  77.05000 0.500 10.64378 ? 113 LYS A CG  1 
ATOM   987  C  CG  B LYS A 1 110 ? 11.28500  12.95900  76.93100 0.500 8.35378  ? 113 LYS A CG  1 
ATOM   988  C  CD  A LYS A 1 110 ? 12.46200  12.98600  78.01300 0.500 11.11378 ? 113 LYS A CD  1 
ATOM   989  C  CD  B LYS A 1 110 ? 12.52200  12.77800  77.80000 0.500 12.27378 ? 113 LYS A CD  1 
ATOM   990  C  CE  A LYS A 1 110 ? 13.77600  12.77800  77.29200 0.500 25.84378 ? 113 LYS A CE  1 
ATOM   991  C  CE  B LYS A 1 110 ? 12.81400  14.02400  78.60600 0.500 30.20378 ? 113 LYS A CE  1 
ATOM   992  N  NZ  A LYS A 1 110 ? 14.90900  13.41900  78.01800 0.500 52.71378 ? 113 LYS A NZ  1 
ATOM   993  N  NZ  B LYS A 1 110 ? 13.09000  15.20400  77.74800 0.500 54.98378 ? 113 LYS A NZ  1 
ATOM   994  N  N   . PHE A 1 111 ? 8.98200   15.53100  76.15200 1.000 8.18108  ? 114 PHE A N   1 
ATOM   995  C  CA  . PHE A 1 111 ? 9.30600   16.54600  75.15400 1.000 8.36531  ? 114 PHE A CA  1 
ATOM   996  C  C   . PHE A 1 111 ? 10.81300  16.68300  74.96100 1.000 8.87590  ? 114 PHE A C   1 
ATOM   997  O  O   . PHE A 1 111 ? 11.58800  16.63600  75.92500 1.000 9.73916  ? 114 PHE A O   1 
ATOM   998  C  CB  . PHE A 1 111 ? 8.73300   17.91200  75.54300 1.000 8.72062  ? 114 PHE A CB  1 
ATOM   999  C  CG  . PHE A 1 111 ? 7.28700   18.06400  75.19000 1.000 8.48901  ? 114 PHE A CG  1 
ATOM   1000 C  CD1 . PHE A 1 111 ? 6.28600   17.62500  76.04700 1.000 8.85221  ? 114 PHE A CD1 1 
ATOM   1001 C  CD2 . PHE A 1 111 ? 6.93100   18.62200  73.98200 1.000 8.95222  ? 114 PHE A CD2 1 
ATOM   1002 C  CE1 . PHE A 1 111 ? 4.94100   17.74400  75.69100 1.000 8.19424  ? 114 PHE A CE1 1 
ATOM   1003 C  CE2 . PHE A 1 111 ? 5.60000   18.75400  73.62600 1.000 9.45228  ? 114 PHE A CE2 1 
ATOM   1004 C  CZ  . PHE A 1 111 ? 4.60400   18.32000  74.47800 1.000 8.89959  ? 114 PHE A CZ  1 
ATOM   1005 N  N   . GLU A 1 112 ? 11.21300  16.86200  73.70700 1.000 8.85221  ? 115 GLU A N   1 
ATOM   1006 C  CA  . GLU A 1 112 ? 12.54500  17.34700  73.35000 1.000 8.72062  ? 115 GLU A CA  1 
ATOM   1007 C  C   . GLU A 1 112 ? 12.28800  18.65000  72.61000 1.000 9.19699  ? 115 GLU A C   1 
ATOM   1008 O  O   . GLU A 1 112 ? 11.84800  18.64300  71.45900 1.000 9.44176  ? 115 GLU A O   1 
ATOM   1009 C  CB  . GLU A 1 112 ? 13.29100  16.34500  72.47300 1.000 9.57335  ? 115 GLU A CB  1 
ATOM   1010 C  CG  . GLU A 1 112 ? 13.58000  15.02500  73.15600 1.000 10.70243 ? 115 GLU A CG  1 
ATOM   1011 C  CD  . GLU A 1 112 ? 14.69300  15.10200  74.18400 1.000 12.70531 ? 115 GLU A CD  1 
ATOM   1012 O  OE1 . GLU A 1 112 ? 15.29500  16.17300  74.39600 1.000 11.27882 ? 115 GLU A OE1 1 
ATOM   1013 O  OE2 . GLU A 1 112 ? 14.98600  14.05000  74.78000 1.000 16.63209 ? 115 GLU A OE2 1 
ATOM   1014 N  N   . GLY A 1 113 ? 12.51700  19.76600  73.28700 1.000 9.75232  ? 116 GLY A N   1 
ATOM   1015 C  CA  . GLY A 1 113 ? 12.06800  21.03500  72.74000 1.000 10.69191 ? 116 GLY A CA  1 
ATOM   1016 C  C   . GLY A 1 113 ? 10.55100  21.01400  72.68100 1.000 10.40766 ? 116 GLY A C   1 
ATOM   1017 O  O   . GLY A 1 113 ? 9.87500   20.67100  73.65600 1.000 11.33935 ? 116 GLY A O   1 
ATOM   1018 N  N   . ASP A 1 114 ? 10.00600  21.35800  71.52300 1.000 9.74179  ? 117 ASP A N   1 
ATOM   1019 C  CA  A ASP A 1 114 ? 8.55700   21.35200  71.35500 0.640 9.93129  ? 117 ASP A CA  1 
ATOM   1020 C  CA  B ASP A 1 114 ? 8.57400   21.38800  71.26400 0.360 8.65378  ? 117 ASP A CA  1 
ATOM   1021 C  C   . ASP A 1 114 ? 8.04400   20.06500  70.73100 1.000 9.02329  ? 117 ASP A C   1 
ATOM   1022 O  O   . ASP A 1 114 ? 6.87000   19.99400  70.35500 1.000 10.13395 ? 117 ASP A O   1 
ATOM   1023 C  CB  A ASP A 1 114 ? 8.10500   22.55700  70.53600 0.640 11.96311 ? 117 ASP A CB  1 
ATOM   1024 C  CB  B ASP A 1 114 ? 8.27900   22.47300  70.22100 0.360 14.72378 ? 117 ASP A CB  1 
ATOM   1025 C  CG  A ASP A 1 114 ? 8.39400   23.84700  71.23000 0.640 13.55541 ? 117 ASP A CG  1 
ATOM   1026 C  CG  B ASP A 1 114 ? 8.84400   22.13500  68.84500 0.360 13.65378 ? 117 ASP A CG  1 
ATOM   1027 O  OD1 A ASP A 1 114 ? 8.15600   23.93400  72.45300 0.640 13.73438 ? 117 ASP A OD1 1 
ATOM   1028 O  OD1 B ASP A 1 114 ? 9.79300   21.32300  68.75200 0.360 21.32378 ? 117 ASP A OD1 1 
ATOM   1029 O  OD2 A ASP A 1 114 ? 8.89500   24.75500  70.55200 0.640 15.46880 ? 117 ASP A OD2 1 
ATOM   1030 O  OD2 B ASP A 1 114 ? 8.33600   22.68400  67.84500 0.360 45.17378 ? 117 ASP A OD2 1 
ATOM   1031 N  N   . THR A 1 115 ? 8.87700   19.04400  70.63600 1.000 8.33110  ? 118 THR A N   1 
ATOM   1032 C  CA  . THR A 1 115 ? 8.49600   17.80400  69.98000 1.000 8.61271  ? 118 THR A CA  1 
ATOM   1033 C  C   . THR A 1 115 ? 8.28000   16.71100  71.01100 1.000 7.65207  ? 118 THR A C   1 
ATOM   1034 O  O   . THR A 1 115 ? 9.10800   16.52200  71.90600 1.000 8.31004  ? 118 THR A O   1 
ATOM   1035 C  CB  . THR A 1 115 ? 9.60300   17.42600  68.99700 1.000 9.20489  ? 118 THR A CB  1 
ATOM   1036 O  OG1 . THR A 1 115 ? 9.71600   18.47700  68.02100 1.000 11.69729 ? 118 THR A OG1 1 
ATOM   1037 C  CG2 . THR A 1 115 ? 9.29500   16.13900  68.29600 1.000 9.16804  ? 118 THR A CG2 1 
ATOM   1038 N  N   . LEU A 1 116 ? 7.15200   16.01800  70.89900 1.000 7.15464  ? 119 LEU A N   1 
ATOM   1039 C  CA  . LEU A 1 116 ? 6.83400   14.92400  71.80000 1.000 7.63628  ? 119 LEU A CA  1 
ATOM   1040 C  C   . LEU A 1 116 ? 7.47900   13.65400  71.25600 1.000 7.34677  ? 119 LEU A C   1 
ATOM   1041 O  O   . LEU A 1 116 ? 7.20600   13.24800  70.11900 1.000 7.33098  ? 119 LEU A O   1 
ATOM   1042 C  CB  . LEU A 1 116 ? 5.30800   14.81300  71.91200 1.000 7.59417  ? 119 LEU A CB  1 
ATOM   1043 C  CG  . LEU A 1 116 ? 4.72800   13.86500  72.96600 1.000 6.99936  ? 119 LEU A CG  1 
ATOM   1044 C  CD1 . LEU A 1 116 ? 4.86300   12.38900  72.56600 1.000 7.32835  ? 119 LEU A CD1 1 
ATOM   1045 C  CD2 . LEU A 1 116 ? 5.33700   14.13200  74.34000 1.000 7.48889  ? 119 LEU A CD2 1 
ATOM   1046 N  N   . VAL A 1 117 ? 8.32800   13.03000  72.06300 1.000 7.08884  ? 120 VAL A N   1 
ATOM   1047 C  CA  . VAL A 1 117 ? 9.13800   11.90000  71.62500 1.000 7.50205  ? 120 VAL A CA  1 
ATOM   1048 C  C   . VAL A 1 117 ? 8.75200   10.65400  72.40700 1.000 6.90724  ? 120 VAL A C   1 
ATOM   1049 O  O   . VAL A 1 117 ? 8.59500   10.69700  73.63300 1.000 7.95210  ? 120 VAL A O   1 
ATOM   1050 C  CB  . VAL A 1 117 ? 10.63300  12.21000  71.81700 1.000 8.98381  ? 120 VAL A CB  1 
ATOM   1051 C  CG1 . VAL A 1 117 ? 11.49400  11.01200  71.47200 1.000 10.72086 ? 120 VAL A CG1 1 
ATOM   1052 C  CG2 . VAL A 1 117 ? 10.98600  13.43400  70.99600 1.000 8.89696  ? 120 VAL A CG2 1 
ATOM   1053 N  N   . ASN A 1 118 ? 8.65200   9.53000   71.69400 1.000 6.27032  ? 121 ASN A N   1 
ATOM   1054 C  CA  . ASN A 1 118 ? 8.43200   8.21500   72.29300 1.000 6.71248  ? 121 ASN A CA  1 
ATOM   1055 C  C   . ASN A 1 118 ? 9.60500   7.32100   71.89500 1.000 6.24401  ? 121 ASN A C   1 
ATOM   1056 O  O   . ASN A 1 118 ? 9.71400   6.93500   70.72500 1.000 6.44403  ? 121 ASN A O   1 
ATOM   1057 C  CB  . ASN A 1 118 ? 7.11000   7.65000   71.77100 1.000 6.88092  ? 121 ASN A CB  1 
ATOM   1058 C  CG  . ASN A 1 118 ? 6.78900   6.29100   72.34600 1.000 6.22821  ? 121 ASN A CG  1 
ATOM   1059 O  OD1 . ASN A 1 118 ? 7.35200   5.89500   73.36700 1.000 6.57562  ? 121 ASN A OD1 1 
ATOM   1060 N  ND2 . ASN A 1 118 ? 5.87100   5.55900   71.69100 1.000 6.16768  ? 121 ASN A ND2 1 
ATOM   1061 N  N   . ARG A 1 119 ? 10.51400  7.05400   72.83900 1.000 6.95725  ? 122 ARG A N   1 
ATOM   1062 C  CA  A ARG A 1 119 ? 11.67500  6.19000   72.62300 0.600 7.22044  ? 122 ARG A CA  1 
ATOM   1063 C  CA  B ARG A 1 119 ? 11.64900  6.17700   72.59800 0.400 6.97378  ? 122 ARG A CA  1 
ATOM   1064 C  C   . ARG A 1 119 ? 11.38200  4.83900   73.26500 1.000 7.27571  ? 122 ARG A C   1 
ATOM   1065 O  O   . ARG A 1 119 ? 11.09100  4.78600   74.46200 1.000 8.03896  ? 122 ARG A O   1 
ATOM   1066 C  CB  A ARG A 1 119 ? 12.92200  6.75900   73.30600 0.600 7.96790  ? 122 ARG A CB  1 
ATOM   1067 C  CB  B ARG A 1 119 ? 12.93700  6.78700   73.14500 0.400 10.80378 ? 122 ARG A CB  1 
ATOM   1068 C  CG  A ARG A 1 119 ? 13.58200  8.00000   72.68600 0.600 9.37070  ? 122 ARG A CG  1 
ATOM   1069 C  CG  B ARG A 1 119 ? 13.61900  7.68800   72.14400 0.400 12.99378 ? 122 ARG A CG  1 
ATOM   1070 C  CD  A ARG A 1 119 ? 14.80700  8.37300   73.54900 0.600 10.30765 ? 122 ARG A CD  1 
ATOM   1071 C  CD  B ARG A 1 119 ? 14.62200  8.61700   72.80300 0.400 14.23378 ? 122 ARG A CD  1 
ATOM   1072 N  NE  A ARG A 1 119 ? 15.63700  9.46800   73.04800 0.600 11.01300 ? 122 ARG A NE  1 
ATOM   1073 N  NE  B ARG A 1 119 ? 13.95800  9.70800   73.50500 0.400 17.76378 ? 122 ARG A NE  1 
ATOM   1074 C  CZ  A ARG A 1 119 ? 15.45800  10.74500  73.35800 0.600 12.35000 ? 122 ARG A CZ  1 
ATOM   1075 C  CZ  B ARG A 1 119 ? 14.52400  10.87100  73.80000 0.400 30.63378 ? 122 ARG A CZ  1 
ATOM   1076 N  NH1 A ARG A 1 119 ? 14.41900  11.14600  74.07200 0.600 11.69466 ? 122 ARG A NH1 1 
ATOM   1077 N  NH1 B ARG A 1 119 ? 15.77800  11.13500  73.46600 0.400 26.64378 ? 122 ARG A NH1 1 
ATOM   1078 N  NH2 A ARG A 1 119 ? 16.33600  11.64400  72.93200 0.600 12.77900 ? 122 ARG A NH2 1 
ATOM   1079 N  NH2 B ARG A 1 119 ? 13.81200  11.79500  74.43900 0.400 11.32378 ? 122 ARG A NH2 1 
ATOM   1080 N  N   . ILE A 1 120 ? 11.48500  3.75200   72.49200 1.000 7.15201  ? 123 ILE A N   1 
ATOM   1081 C  CA  . ILE A 1 120 ? 11.09000  2.43600   72.98600 1.000 7.49416  ? 123 ILE A CA  1 
ATOM   1082 C  C   . ILE A 1 120 ? 12.18700  1.40200   72.77900 1.000 7.53100  ? 123 ILE A C   1 
ATOM   1083 O  O   . ILE A 1 120 ? 12.79800  1.33300   71.70700 1.000 7.40204  ? 123 ILE A O   1 
ATOM   1084 C  CB  . ILE A 1 120 ? 9.84400   1.90700   72.24600 1.000 8.95222  ? 123 ILE A CB  1 
ATOM   1085 C  CG1 . ILE A 1 120 ? 8.74300   2.97000   72.13000 1.000 8.56534  ? 123 ILE A CG1 1 
ATOM   1086 C  CG2 . ILE A 1 120 ? 9.34400   0.63000   72.92600 1.000 10.64980 ? 123 ILE A CG2 1 
ATOM   1087 C  CD1 . ILE A 1 120 ? 8.34500   3.23100   70.70700 1.000 9.39438  ? 123 ILE A CD1 1 
ATOM   1088 N  N   . GLU A 1 121 ? 12.36700  0.55100   73.78600 1.000 7.46520  ? 124 GLU A N   1 
ATOM   1089 C  CA  A GLU A 1 121 ? 13.10000  -0.70000  73.65100 0.330 8.57378  ? 124 GLU A CA  1 
ATOM   1090 C  CA  B GLU A 1 121 ? 13.09600  -0.70000  73.64500 0.310 7.48378  ? 124 GLU A CA  1 
ATOM   1091 C  CA  C GLU A 1 121 ? 13.10100  -0.70200  73.66000 0.360 5.35378  ? 124 GLU A CA  1 
ATOM   1092 C  C   . GLU A 1 121 ? 12.09500  -1.84000  73.75300 1.000 7.09411  ? 124 GLU A C   1 
ATOM   1093 O  O   . GLU A 1 121 ? 11.29800  -1.88600  74.69700 1.000 8.41532  ? 124 GLU A O   1 
ATOM   1094 C  CB  A GLU A 1 121 ? 14.16800  -0.83800  74.74300 0.330 11.93378 ? 124 GLU A CB  1 
ATOM   1095 C  CB  B GLU A 1 121 ? 14.18500  -0.83100  74.71400 0.310 9.93378  ? 124 GLU A CB  1 
ATOM   1096 C  CB  C GLU A 1 121 ? 14.15400  -0.83700  74.77100 0.360 8.29378  ? 124 GLU A CB  1 
ATOM   1097 C  CG  A GLU A 1 121 ? 15.19500  -1.94200  74.48500 0.330 15.27378 ? 124 GLU A CG  1 
ATOM   1098 C  CG  B GLU A 1 121 ? 15.28200  0.21700   74.59200 0.310 10.45378 ? 124 GLU A CG  1 
ATOM   1099 C  CG  C GLU A 1 121 ? 14.99800  -2.11300  74.70700 0.360 10.61378 ? 124 GLU A CG  1 
ATOM   1100 C  CD  A GLU A 1 121 ? 16.18800  -1.58000  73.39200 0.330 20.74378 ? 124 GLU A CD  1 
ATOM   1101 C  CD  B GLU A 1 121 ? 16.49500  -0.10200  75.44400 0.310 21.55378 ? 124 GLU A CD  1 
ATOM   1102 C  CD  C GLU A 1 121 ? 16.17800  -2.08500  75.66500 0.360 33.68378 ? 124 GLU A CD  1 
ATOM   1103 O  OE1 A GLU A 1 121 ? 16.68800  -0.43400  73.38800 0.330 16.62378 ? 124 GLU A OE1 1 
ATOM   1104 O  OE1 B GLU A 1 121 ? 16.65000  -1.27400  75.84600 0.310 31.06378 ? 124 GLU A OE1 1 
ATOM   1105 O  OE1 C GLU A 1 121 ? 16.54800  -0.98300  76.12300 0.360 40.12378 ? 124 GLU A OE1 1 
ATOM   1106 O  OE2 A GLU A 1 121 ? 16.46600  -2.44100  72.53300 0.330 17.76378 ? 124 GLU A OE2 1 
ATOM   1107 O  OE2 B GLU A 1 121 ? 17.28600  0.82200   75.72900 0.310 19.51378 ? 124 GLU A OE2 1 
ATOM   1108 O  OE2 C GLU A 1 121 ? 16.73900  -3.16400  75.95800 0.360 27.07378 ? 124 GLU A OE2 1 
ATOM   1109 N  N   . LEU A 1 122 ? 12.11500  -2.73500  72.77400 1.000 6.75722  ? 125 LEU A N   1 
ATOM   1110 C  CA  . LEU A 1 122 ? 11.16800  -3.84800  72.73600 1.000 6.65195  ? 125 LEU A CA  1 
ATOM   1111 C  C   . LEU A 1 122 ? 11.93100  -5.16600  72.68500 1.000 7.61259  ? 125 LEU A C   1 
ATOM   1112 O  O   . LEU A 1 122 ? 12.86000  -5.32200  71.88100 1.000 7.92315  ? 125 LEU A O   1 
ATOM   1113 C  CB  . LEU A 1 122 ? 10.25200  -3.73300  71.50600 1.000 7.81788  ? 125 LEU A CB  1 
ATOM   1114 C  CG  . LEU A 1 122 ? 9.23600   -4.86500  71.27600 1.000 7.18886  ? 125 LEU A CG  1 
ATOM   1115 C  CD1 . LEU A 1 122 ? 8.02400   -4.32200  70.51700 1.000 6.72564  ? 125 LEU A CD1 1 
ATOM   1116 C  CD2 . LEU A 1 122 ? 9.83300   -6.04600  70.51600 1.000 8.08370  ? 125 LEU A CD2 1 
ATOM   1117 N  N   . LYS A 1 123 ? 11.49900  -6.12700  73.50400 1.000 6.97567  ? 126 LYS A N   1 
ATOM   1118 C  CA  . LYS A 1 123 ? 12.09700  -7.45800  73.53700 1.000 7.20465  ? 126 LYS A CA  1 
ATOM   1119 C  C   . LYS A 1 123 ? 10.97500  -8.46700  73.37900 1.000 7.13622  ? 126 LYS A C   1 
ATOM   1120 O  O   . LYS A 1 123 ? 10.01400  -8.45100  74.15400 1.000 7.87578  ? 126 LYS A O   1 
ATOM   1121 C  CB  . LYS A 1 123 ? 12.80400  -7.67900  74.87400 1.000 8.21266  ? 126 LYS A CB  1 
ATOM   1122 C  CG  . LYS A 1 123 ? 13.58900  -8.96600  75.01000 1.000 9.64441  ? 126 LYS A CG  1 
ATOM   1123 C  CD  . LYS A 1 123 ? 14.76500  -9.04000  74.02500 1.000 10.38398 ? 126 LYS A CD  1 
ATOM   1124 C  CE  . LYS A 1 123 ? 15.72000  -10.20800 74.38200 1.000 11.07090 ? 126 LYS A CE  1 
ATOM   1125 N  NZ  . LYS A 1 123 ? 16.40200  -9.94700  75.69000 1.000 13.44224 ? 126 LYS A NZ  1 
ATOM   1126 N  N   . GLY A 1 124 ? 11.08400  -9.33000  72.37900 1.000 7.09148  ? 127 GLY A N   1 
ATOM   1127 C  CA  . GLY A 1 124 ? 10.08200  -10.36500 72.19500 1.000 6.93883  ? 127 GLY A CA  1 
ATOM   1128 C  C   . GLY A 1 124 ? 10.71700  -11.73200 72.29600 1.000 6.82039  ? 127 GLY A C   1 
ATOM   1129 O  O   . GLY A 1 124 ? 11.77600  -11.97300 71.71100 1.000 7.48889  ? 127 GLY A O   1 
ATOM   1130 N  N   . ILE A 1 125 ? 10.09200  -12.63400 73.04400 1.000 6.94935  ? 128 ILE A N   1 
ATOM   1131 C  CA  . ILE A 1 125 ? 10.60700  -13.98700 73.20800 1.000 7.32835  ? 128 ILE A CA  1 
ATOM   1132 C  C   . ILE A 1 125 ? 9.45600   -14.97300 73.10600 1.000 7.66786  ? 128 ILE A C   1 
ATOM   1133 O  O   . ILE A 1 125 ? 8.27800   -14.61100 73.18700 1.000 7.97053  ? 128 ILE A O   1 
ATOM   1134 C  CB  . ILE A 1 125 ? 11.36800  -14.20100 74.53300 1.000 7.55469  ? 128 ILE A CB  1 
ATOM   1135 C  CG1 . ILE A 1 125 ? 10.43500  -14.06500 75.74400 1.000 8.24161  ? 128 ILE A CG1 1 
ATOM   1136 C  CG2 . ILE A 1 125 ? 12.55000  -13.25600 74.62900 1.000 7.86262  ? 128 ILE A CG2 1 
ATOM   1137 C  CD1 . ILE A 1 125 ? 11.10800  -14.45900 77.06600 1.000 10.65506 ? 128 ILE A CD1 1 
ATOM   1138 N  N   . ASP A 1 126 ? 9.82600   -16.24200 72.93700 1.000 8.47848  ? 129 ASP A N   1 
ATOM   1139 C  CA  A ASP A 1 126 ? 8.90600   -17.37200 72.93800 0.780 10.39450 ? 129 ASP A CA  1 
ATOM   1140 C  CA  B ASP A 1 126 ? 8.88200   -17.35400 72.96100 0.220 9.19378  ? 129 ASP A CA  1 
ATOM   1141 C  C   . ASP A 1 126 ? 7.95600   -17.37000 71.75300 1.000 9.01013  ? 129 ASP A C   1 
ATOM   1142 O  O   . ASP A 1 126 ? 6.90500   -18.00600 71.80200 1.000 9.51545  ? 129 ASP A O   1 
ATOM   1143 C  CB  A ASP A 1 126 ? 8.14900   -17.49000 74.26400 0.780 14.51342 ? 129 ASP A CB  1 
ATOM   1144 C  CB  B ASP A 1 126 ? 8.04000   -17.40300 74.25100 0.220 7.50378  ? 129 ASP A CB  1 
ATOM   1145 C  CG  A ASP A 1 126 ? 9.01900   -18.02200 75.38100 0.780 20.12988 ? 129 ASP A CG  1 
ATOM   1146 C  CG  B ASP A 1 126 ? 8.86900   -17.35100 75.52300 0.220 39.85378 ? 129 ASP A CG  1 
ATOM   1147 O  OD1 A ASP A 1 126 ? 9.97400   -18.75600 75.06800 0.780 21.80377 ? 129 ASP A OD1 1 
ATOM   1148 O  OD1 B ASP A 1 126 ? 9.99500   -17.87500 75.52900 0.220 8.70378  ? 129 ASP A OD1 1 
ATOM   1149 O  OD2 A ASP A 1 126 ? 8.73700   -17.72100 76.55700 0.780 28.63378 ? 129 ASP A OD2 1 
ATOM   1150 O  OD2 B ASP A 1 126 ? 8.37300   -16.80300 76.53500 0.220 7.63378  ? 129 ASP A OD2 1 
ATOM   1151 N  N   . PHE A 1 127 ? 8.30100   -16.69200 70.66700 1.000 9.03381  ? 130 PHE A N   1 
ATOM   1152 C  CA  . PHE A 1 127 ? 7.44200   -16.75600 69.49200 1.000 8.35215  ? 130 PHE A CA  1 
ATOM   1153 C  C   . PHE A 1 127 ? 7.63900   -18.05000 68.71200 1.000 8.87064  ? 130 PHE A C   1 
ATOM   1154 O  O   . PHE A 1 127 ? 8.74400   -18.60400 68.61600 1.000 10.11815 ? 130 PHE A O   1 
ATOM   1155 C  CB  . PHE A 1 127 ? 7.64600   -15.53900 68.59400 1.000 8.59955  ? 130 PHE A CB  1 
ATOM   1156 C  CG  . PHE A 1 127 ? 7.05000   -14.31500 69.17700 1.000 7.34677  ? 130 PHE A CG  1 
ATOM   1157 C  CD1 . PHE A 1 127 ? 5.71000   -14.03800 68.95900 1.000 7.38098  ? 130 PHE A CD1 1 
ATOM   1158 C  CD2 . PHE A 1 127 ? 7.78600   -13.48600 70.02700 1.000 7.53627  ? 130 PHE A CD2 1 
ATOM   1159 C  CE1 . PHE A 1 127 ? 5.11000   -12.94400 69.56000 1.000 7.00989  ? 130 PHE A CE1 1 
ATOM   1160 C  CE2 . PHE A 1 127 ? 7.18400   -12.38700 70.62800 1.000 7.31782  ? 130 PHE A CE2 1 
ATOM   1161 C  CZ  . PHE A 1 127 ? 5.84700   -12.11000 70.39300 1.000 6.91251  ? 130 PHE A CZ  1 
ATOM   1162 N  N   . LYS A 1 128 ? 6.54000   -18.52500 68.13900 1.000 9.00486  ? 131 LYS A N   1 
ATOM   1163 C  CA  A LYS A 1 128 ? 6.57200   -19.69900 67.28100 0.720 10.28133 ? 131 LYS A CA  1 
ATOM   1164 C  CA  B LYS A 1 128 ? 6.58200   -19.70200 67.28600 0.280 10.07378 ? 131 LYS A CA  1 
ATOM   1165 C  C   . LYS A 1 128 ? 7.01800   -19.30200 65.88300 1.000 11.14459 ? 131 LYS A C   1 
ATOM   1166 O  O   . LYS A 1 128 ? 6.55900   -18.29600 65.33300 1.000 12.13682 ? 131 LYS A O   1 
ATOM   1167 C  CB  A LYS A 1 128 ? 5.17600   -20.30300 67.19500 0.720 10.90246 ? 131 LYS A CB  1 
ATOM   1168 C  CB  B LYS A 1 128 ? 5.20800   -20.37000 67.23500 0.280 17.69378 ? 131 LYS A CB  1 
ATOM   1169 C  CG  A LYS A 1 128 ? 4.70400   -20.87800 68.50700 0.720 12.59740 ? 131 LYS A CG  1 
ATOM   1170 C  CG  B LYS A 1 128 ? 4.77000   -20.95700 68.56500 0.280 14.57378 ? 131 LYS A CG  1 
ATOM   1171 C  CD  A LYS A 1 128 ? 3.29700   -21.45900 68.40000 0.720 14.63185 ? 131 LYS A CD  1 
ATOM   1172 C  CD  B LYS A 1 128 ? 3.43200   -21.67300 68.45000 0.280 32.45378 ? 131 LYS A CD  1 
ATOM   1173 C  CE  A LYS A 1 128 ? 2.88400   -22.07100 69.73300 0.720 19.04028 ? 131 LYS A CE  1 
ATOM   1174 C  CE  B LYS A 1 128 ? 2.36700   -20.75400 67.88500 0.280 14.69378 ? 131 LYS A CE  1 
ATOM   1175 N  NZ  A LYS A 1 128 ? 1.44100   -22.42300 69.76800 0.720 22.95378 ? 131 LYS A NZ  1 
ATOM   1176 N  NZ  B LYS A 1 128 ? 0.98500   -21.24400 68.16400 0.280 15.34378 ? 131 LYS A NZ  1 
ATOM   1177 N  N   . GLU A 1 129 ? 7.90800   -20.11000 65.30100 1.000 13.02113 ? 132 GLU A N   1 
ATOM   1178 C  CA  . GLU A 1 129 ? 8.49900   -19.74900 64.01500 1.000 16.50839 ? 132 GLU A CA  1 
ATOM   1179 C  C   . GLU A 1 129 ? 7.45800   -19.56100 62.92800 1.000 17.22427 ? 132 GLU A C   1 
ATOM   1180 O  O   . GLU A 1 129 ? 7.62900   -18.70400 62.05100 1.000 19.29557 ? 132 GLU A O   1 
ATOM   1181 C  CB  . GLU A 1 129 ? 9.51300   -20.81000 63.58300 1.000 19.50349 ? 132 GLU A CB  1 
ATOM   1182 C  CG  . GLU A 1 129 ? 10.84700  -20.68400 64.29100 1.000 22.95378 ? 132 GLU A CG  1 
ATOM   1183 C  CD  A GLU A 1 129 ? 10.75500  -21.00400 65.77100 0.640 23.58299 ? 132 GLU A CD  1 
ATOM   1184 O  OE1 A GLU A 1 129 ? 9.92900   -21.86900 66.14300 0.640 23.15107 ? 132 GLU A OE1 1 
ATOM   1185 O  OE2 A GLU A 1 129 ? 11.49900  -20.38600 66.56100 0.640 25.73378 ? 132 GLU A OE2 1 
ATOM   1186 N  N   . ASP A 1 130 ? 6.38600   -20.34700 62.94800 1.000 16.08203 ? 133 ASP A N   1 
ATOM   1187 C  CA  . ASP A 1 130 ? 5.30500   -20.15900 61.99300 1.000 17.81118 ? 133 ASP A CA  1 
ATOM   1188 C  C   . ASP A 1 130 ? 3.97500   -19.89100 62.68700 1.000 15.19771 ? 133 ASP A C   1 
ATOM   1189 O  O   . ASP A 1 130 ? 2.90900   -20.28700 62.20000 1.000 16.47155 ? 133 ASP A O   1 
ATOM   1190 C  CB  . ASP A 1 130 ? 5.20900   -21.29000 60.97100 1.000 23.60378 ? 133 ASP A CB  1 
ATOM   1191 C  CG  . ASP A 1 130 ? 4.38200   -20.89400 59.75100 1.000 24.58378 ? 133 ASP A CG  1 
ATOM   1192 O  OD1 . ASP A 1 130 ? 4.69000   -19.84900 59.13400 1.000 29.07378 ? 133 ASP A OD1 1 
ATOM   1193 O  OD2 . ASP A 1 130 ? 3.41800   -21.61500 59.42700 1.000 27.36378 ? 133 ASP A OD2 1 
ATOM   1194 N  N   . GLY A 1 131 ? 4.02700   -19.19700 63.81800 1.000 12.55266 ? 134 GLY A N   1 
ATOM   1195 C  CA  . GLY A 1 131 ? 2.84000   -18.64500 64.41600 1.000 11.09985 ? 134 GLY A CA  1 
ATOM   1196 C  C   . GLY A 1 131 ? 2.36600   -17.44400 63.62500 1.000 9.47334  ? 134 GLY A C   1 
ATOM   1197 O  O   . GLY A 1 131 ? 2.90200   -17.08700 62.57600 1.000 9.89707  ? 134 GLY A O   1 
ATOM   1198 N  N   . ASN A 1 132 ? 1.36400   -16.77000 64.18300 1.000 8.76010  ? 135 ASN A N   1 
ATOM   1199 C  CA  . ASN A 1 132 ? 0.75900   -15.65700 63.45800 1.000 8.42058  ? 135 ASN A CA  1 
ATOM   1200 C  C   . ASN A 1 132 ? 1.67900   -14.45500 63.36000 1.000 7.93368  ? 135 ASN A C   1 
ATOM   1201 O  O   . ASN A 1 132 ? 1.48400   -13.61200 62.47900 1.000 8.07844  ? 135 ASN A O   1 
ATOM   1202 C  CB  . ASN A 1 132 ? -0.54600  -15.24500 64.13300 1.000 10.19185 ? 135 ASN A CB  1 
ATOM   1203 C  CG  . ASN A 1 132 ? -1.60200  -16.28900 63.99100 1.000 10.01025 ? 135 ASN A CG  1 
ATOM   1204 O  OD1 . ASN A 1 132 ? -1.74700  -16.88600 62.92700 1.000 11.98943 ? 135 ASN A OD1 1 
ATOM   1205 N  ND2 . ASN A 1 132 ? -2.34400  -16.53500 65.06400 1.000 9.46808  ? 135 ASN A ND2 1 
ATOM   1206 N  N   . ILE A 1 133 ? 2.62200   -14.32800 64.29400 1.000 7.75734  ? 136 ILE A N   1 
ATOM   1207 C  CA  . ILE A 1 133 ? 3.51700   -13.18100 64.35100 1.000 7.54416  ? 136 ILE A CA  1 
ATOM   1208 C  C   . ILE A 1 133 ? 4.69900   -13.42700 63.41500 1.000 7.83893  ? 136 ILE A C   1 
ATOM   1209 O  O   . ILE A 1 133 ? 4.83700   -12.73700 62.39900 1.000 8.61797  ? 136 ILE A O   1 
ATOM   1210 C  CB  . ILE A 1 133 ? 3.94100   -12.85700 65.80300 1.000 8.22056  ? 136 ILE A CB  1 
ATOM   1211 C  CG1 . ILE A 1 133 ? 2.75000   -12.31700 66.61700 1.000 9.47334  ? 136 ILE A CG1 1 
ATOM   1212 C  CG2 . ILE A 1 133 ? 5.03700   -11.80100 65.83300 1.000 8.34426  ? 136 ILE A CG2 1 
ATOM   1213 C  CD1 . ILE A 1 133 ? 1.84000   -13.37900 67.19900 1.000 11.16038 ? 136 ILE A CD1 1 
ATOM   1214 N  N   . LEU A 1 134 ? 5.55400   -14.41000 63.73100 1.000 8.30741  ? 137 LEU A N   1 
ATOM   1215 C  CA  . LEU A 1 134 ? 6.72000   -14.61900 62.88400 1.000 9.23647  ? 137 LEU A CA  1 
ATOM   1216 C  C   . LEU A 1 134 ? 6.33800   -15.18400 61.52700 1.000 10.07341 ? 137 LEU A C   1 
ATOM   1217 O  O   . LEU A 1 134 ? 7.10100   -15.02100 60.57100 1.000 12.32631 ? 137 LEU A O   1 
ATOM   1218 C  CB  . LEU A 1 134 ? 7.75300   -15.51000 63.57600 1.000 10.32344 ? 137 LEU A CB  1 
ATOM   1219 C  CG  . LEU A 1 134 ? 8.45300   -14.87500 64.78100 1.000 11.19197 ? 137 LEU A CG  1 
ATOM   1220 C  CD1 . LEU A 1 134 ? 9.38900   -15.89700 65.41700 1.000 10.90772 ? 137 LEU A CD1 1 
ATOM   1221 C  CD2 . LEU A 1 134 ? 9.23200   -13.60600 64.40900 1.000 11.67360 ? 137 LEU A CD2 1 
ATOM   1222 N  N   . GLY A 1 135 ? 5.16900   -15.81400 61.41900 1.000 9.83391  ? 138 GLY A N   1 
ATOM   1223 C  CA  . GLY A 1 135 ? 4.67700   -16.26000 60.13800 1.000 10.63664 ? 138 GLY A CA  1 
ATOM   1224 C  C   . GLY A 1 135 ? 3.94300   -15.21400 59.33500 1.000 9.49703  ? 138 GLY A C   1 
ATOM   1225 O  O   . GLY A 1 135 ? 3.49300   -15.52200 58.22600 1.000 10.79192 ? 138 GLY A O   1 
ATOM   1226 N  N   . HIS A 1 136 ? 3.79800   -13.98900 59.85400 1.000 9.25226  ? 139 HIS A N   1 
ATOM   1227 C  CA  . HIS A 1 136 ? 3.13700   -12.89600 59.13500 1.000 9.36806  ? 139 HIS A CA  1 
ATOM   1228 C  C   . HIS A 1 136 ? 1.75500   -13.30700 58.62400 1.000 9.20489  ? 139 HIS A C   1 
ATOM   1229 O  O   . HIS A 1 136 ? 1.44800   -13.23400 57.43300 1.000 10.07604 ? 139 HIS A O   1 
ATOM   1230 C  CB  . HIS A 1 136 ? 4.01700   -12.35000 58.00500 1.000 9.90760  ? 139 HIS A CB  1 
ATOM   1231 C  CG  . HIS A 1 136 ? 5.27400   -11.69700 58.48100 1.000 10.73402 ? 139 HIS A CG  1 
ATOM   1232 N  ND1 . HIS A 1 136 ? 5.31700   -10.38200 58.89200 1.000 11.60254 ? 139 HIS A ND1 1 
ATOM   1233 C  CD2 . HIS A 1 136 ? 6.53500   -12.17500 58.60200 1.000 13.32907 ? 139 HIS A CD2 1 
ATOM   1234 C  CE1 . HIS A 1 136 ? 6.55300   -10.07900 59.24700 1.000 13.63700 ? 139 HIS A CE1 1 
ATOM   1235 N  NE2 . HIS A 1 136 ? 7.30900   -11.15000 59.08700 1.000 15.17139 ? 139 HIS A NE2 1 
ATOM   1236 N  N   . LYS A 1 137 ? 0.90600   -13.72000 59.55600 1.000 8.25740  ? 140 LYS A N   1 
ATOM   1237 C  CA  . LYS A 1 137 ? -0.43000  -14.17500 59.20700 1.000 8.57850  ? 140 LYS A CA  1 
ATOM   1238 C  C   . LYS A 1 137 ? -1.50200  -13.19400 59.63700 1.000 8.26793  ? 140 LYS A C   1 
ATOM   1239 O  O   . LYS A 1 137 ? -2.69700  -13.53200 59.59900 1.000 9.28911  ? 140 LYS A O   1 
ATOM   1240 C  CB  . LYS A 1 137 ? -0.72500  -15.54700 59.80200 1.000 9.01013  ? 140 LYS A CB  1 
ATOM   1241 C  CG  . LYS A 1 137 ? 0.34200   -16.55500 59.46500 1.000 9.96287  ? 140 LYS A CG  1 
ATOM   1242 C  CD  . LYS A 1 137 ? -0.00800  -17.93900 60.00000 1.000 11.07880 ? 140 LYS A CD  1 
ATOM   1243 C  CE  . LYS A 1 137 ? 1.17100   -18.88300 59.84400 1.000 12.23683 ? 140 LYS A CE  1 
ATOM   1244 N  NZ  . LYS A 1 137 ? 0.86400   -20.28300 60.26900 1.000 13.82386 ? 140 LYS A NZ  1 
ATOM   1245 N  N   . LEU A 1 138 ? -1.11000  -11.98700 60.05800 1.000 8.25740  ? 141 LEU A N   1 
ATOM   1246 C  CA  . LEU A 1 138 ? -2.06800  -10.99200 60.52900 1.000 8.30741  ? 141 LEU A CA  1 
ATOM   1247 C  C   . LEU A 1 138 ? -2.46300  -10.03000 59.41800 1.000 8.86537  ? 141 LEU A C   1 
ATOM   1248 O  O   . LEU A 1 138 ? -1.62200  -9.56500  58.65000 1.000 10.49188 ? 141 LEU A O   1 
ATOM   1249 C  CB  . LEU A 1 138 ? -1.50700  -10.22700 61.72600 1.000 8.44690  ? 141 LEU A CB  1 
ATOM   1250 C  CG  . LEU A 1 138 ? -1.15500  -11.13200 62.90800 1.000 9.21541  ? 141 LEU A CG  1 
ATOM   1251 C  CD1 . LEU A 1 138 ? -0.60400  -10.27900 64.06600 1.000 10.90772 ? 141 LEU A CD1 1 
ATOM   1252 C  CD2 . LEU A 1 138 ? -2.38000  -11.91200 63.33100 1.000 9.51019  ? 141 LEU A CD2 1 
ATOM   1253 N  N   . GLU A 1 139 ? -3.75400  -9.72800  59.34400 1.000 8.75746  ? 142 GLU A N   1 
ATOM   1254 C  CA  . GLU A 1 139 ? -4.23400  -8.76000  58.37200 1.000 9.37333  ? 142 GLU A CA  1 
ATOM   1255 C  C   . GLU A 1 139 ? -3.69600  -7.37400  58.68500 1.000 8.82326  ? 142 GLU A C   1 
ATOM   1256 O  O   . GLU A 1 139 ? -3.46300  -7.02100  59.84200 1.000 8.75220  ? 142 GLU A O   1 
ATOM   1257 C  CB  . GLU A 1 139 ? -5.75800  -8.70500  58.40300 1.000 10.15763 ? 142 GLU A CB  1 
ATOM   1258 C  CG  . GLU A 1 139 ? -6.42200  -9.97800  57.91300 1.000 11.16565 ? 142 GLU A CG  1 
ATOM   1259 C  CD  . GLU A 1 139 ? -7.93200  -9.90600  57.89100 1.000 12.17893 ? 142 GLU A CD  1 
ATOM   1260 O  OE1 . GLU A 1 139 ? -8.51600  -8.94800  58.44300 1.000 11.85784 ? 142 GLU A OE1 1 
ATOM   1261 O  OE2 . GLU A 1 139 ? -8.53400  -10.82400 57.30700 1.000 14.58974 ? 142 GLU A OE2 1 
ATOM   1262 N  N   . TYR A 1 140 ? -3.52300  -6.57500  57.63400 1.000 9.04434  ? 143 TYR A N   1 
ATOM   1263 C  CA  . TYR A 1 140 ? -3.05600  -5.19900  57.79800 1.000 8.54428  ? 143 TYR A CA  1 
ATOM   1264 C  C   . TYR A 1 140 ? -4.26000  -4.29700  58.05800 1.000 8.65482  ? 143 TYR A C   1 
ATOM   1265 O  O   . TYR A 1 140 ? -4.75300  -3.58800  57.17500 1.000 9.66284  ? 143 TYR A O   1 
ATOM   1266 C  CB  . TYR A 1 140 ? -2.28000  -4.75800  56.55900 1.000 9.39175  ? 143 TYR A CB  1 
ATOM   1267 C  CG  . TYR A 1 140 ? -1.60100  -3.41700  56.73900 1.000 9.02592  ? 143 TYR A CG  1 
ATOM   1268 C  CD1 . TYR A 1 140 ? -0.49100  -3.29100  57.57600 1.000 8.92327  ? 143 TYR A CD1 1 
ATOM   1269 C  CD2 . TYR A 1 140 ? -2.06600  -2.27900  56.08700 1.000 8.55744  ? 143 TYR A CD2 1 
ATOM   1270 C  CE1 . TYR A 1 140 ? 0.12800   -2.08200  57.75800 1.000 9.26805  ? 143 TYR A CE1 1 
ATOM   1271 C  CE2 . TYR A 1 140 ? -1.44400  -1.05600  56.25300 1.000 9.13383  ? 143 TYR A CE2 1 
ATOM   1272 C  CZ  . TYR A 1 140 ? -0.34200  -0.97100  57.08300 1.000 8.64429  ? 143 TYR A CZ  1 
ATOM   1273 O  OH  . TYR A 1 140 ? 0.30300   0.23400   57.27500 1.000 9.40754  ? 143 TYR A OH  1 
ATOM   1274 N  N   . ASN A 1 141 ? -4.74000  -4.33100  59.29800 1.000 9.04171  ? 144 ASN A N   1 
ATOM   1275 C  CA  . ASN A 1 141 ? -5.86800  -3.50600  59.70800 1.000 8.95749  ? 144 ASN A CA  1 
ATOM   1276 C  C   . ASN A 1 141 ? -5.87400  -3.47900  61.22900 1.000 8.27846  ? 144 ASN A C   1 
ATOM   1277 O  O   . ASN A 1 141 ? -4.97700  -4.02900  61.87300 1.000 8.41269  ? 144 ASN A O   1 
ATOM   1278 C  CB  . ASN A 1 141 ? -7.18900  -3.98200  59.09500 1.000 9.67073  ? 144 ASN A CB  1 
ATOM   1279 C  CG  . ASN A 1 141 ? -7.48400  -5.43200  59.39200 1.000 10.77613 ? 144 ASN A CG  1 
ATOM   1280 O  OD1 . ASN A 1 141 ? -7.27500  -5.90600  60.49800 1.000 12.61319 ? 144 ASN A OD1 1 
ATOM   1281 N  ND2 . ASN A 1 141 ? -8.00000  -6.14400  58.39900 1.000 11.16302 ? 144 ASN A ND2 1 
ATOM   1282 N  N   . TYR A 1 142 ? -6.87700  -2.81900  61.80700 1.000 8.07580  ? 145 TYR A N   1 
ATOM   1283 C  CA  . TYR A 1 142 ? -6.85900  -2.61200  63.25200 1.000 8.04159  ? 145 TYR A CA  1 
ATOM   1284 C  C   . TYR A 1 142 ? -8.26300  -2.37600  63.77400 1.000 9.14172  ? 145 TYR A C   1 
ATOM   1285 O  O   . TYR A 1 142 ? -8.99700  -1.56100  63.22300 1.000 11.34199 ? 145 TYR A O   1 
ATOM   1286 C  CB  . TYR A 1 142 ? -5.95100  -1.42700  63.63900 1.000 8.88643  ? 145 TYR A CB  1 
ATOM   1287 C  CG  . TYR A 1 142 ? -5.24600  -1.68200  64.94600 1.000 7.64154  ? 145 TYR A CG  1 
ATOM   1288 C  CD1 . TYR A 1 142 ? -4.04200  -2.38100  64.96500 1.000 7.25728  ? 145 TYR A CD1 1 
ATOM   1289 C  CD2 . TYR A 1 142 ? -5.77400  -1.25800  66.15600 1.000 7.94947  ? 145 TYR A CD2 1 
ATOM   1290 C  CE1 . TYR A 1 142 ? -3.38900  -2.66200  66.17000 1.000 7.61259  ? 145 TYR A CE1 1 
ATOM   1291 C  CE2 . TYR A 1 142 ? -5.13100  -1.52900  67.36200 1.000 8.02580  ? 145 TYR A CE2 1 
ATOM   1292 C  CZ  . TYR A 1 142 ? -3.93600  -2.22700  67.36100 1.000 7.10727  ? 145 TYR A CZ  1 
ATOM   1293 O  OH  . TYR A 1 142 ? -3.32600  -2.45300  68.55600 1.000 7.62312  ? 145 TYR A OH  1 
ATOM   1294 N  N   . ASN A 1 143 ? -8.60300  -3.05400  64.85600 1.000 8.82063  ? 146 ASN A N   1 
ATOM   1295 C  CA  . ASN A 1 143 ? -9.89500  -2.91700  65.50500 1.000 9.63915  ? 146 ASN A CA  1 
ATOM   1296 C  C   . ASN A 1 143 ? -9.87000  -1.80000  66.54000 1.000 8.92591  ? 146 ASN A C   1 
ATOM   1297 O  O   . ASN A 1 143 ? -8.81200  -1.30900  66.93300 1.000 10.18132 ? 146 ASN A O   1 
ATOM   1298 C  CB  . ASN A 1 143 ? -10.27400 -4.25300  66.14100 1.000 10.56294 ? 146 ASN A CB  1 
ATOM   1299 C  CG  . ASN A 1 143 ? -10.45200 -5.33600  65.09200 1.000 11.72098 ? 146 ASN A CG  1 
ATOM   1300 O  OD1 . ASN A 1 143 ? -11.12200 -5.11200  64.08400 1.000 14.68186 ? 146 ASN A OD1 1 
ATOM   1301 N  ND2 . ASN A 1 143 ? -9.82800  -6.49000  65.29200 1.000 12.06576 ? 146 ASN A ND2 1 
ATOM   1302 N  N   . SER A 1 144 ? -11.07200 -1.39500  66.97000 1.000 9.67863  ? 147 SER A N   1 
ATOM   1303 C  CA  . SER A 1 144 ? -11.24700 -0.38700  68.00200 1.000 9.42860  ? 147 SER A CA  1 
ATOM   1304 C  C   . SER A 1 144 ? -11.28300 -1.06900  69.35800 1.000 8.53639  ? 147 SER A C   1 
ATOM   1305 O  O   . SER A 1 144 ? -11.83000 -2.16600  69.49500 1.000 9.51019  ? 147 SER A O   1 
ATOM   1306 C  CB  . SER A 1 144 ? -12.54600 0.37100   67.74900 1.000 11.21829 ? 147 SER A CB  1 
ATOM   1307 O  OG  . SER A 1 144 ? -12.45300 0.98500   66.47400 1.000 12.14471 ? 147 SER A OG  1 
ATOM   1308 N  N   . HIS A 1 145 ? -10.68600 -0.42500  70.36500 1.000 7.92315  ? 148 HIS A N   1 
ATOM   1309 C  CA  . HIS A 1 145 ? -10.56200 -1.06000  71.67500 1.000 7.35466  ? 148 HIS A CA  1 
ATOM   1310 C  C   . HIS A 1 145 ? -10.65700 -0.00700  72.76900 1.000 7.34414  ? 148 HIS A C   1 
ATOM   1311 O  O   . HIS A 1 145 ? -10.41200 1.17400   72.54200 1.000 9.18120  ? 148 HIS A O   1 
ATOM   1312 C  CB  . HIS A 1 145 ? -9.20000  -1.72900  71.84400 1.000 7.98369  ? 148 HIS A CB  1 
ATOM   1313 C  CG  . HIS A 1 145 ? -8.89400  -2.76400  70.80700 1.000 8.23898  ? 148 HIS A CG  1 
ATOM   1314 N  ND1 . HIS A 1 145 ? -8.23000  -2.46100  69.63400 1.000 9.51019  ? 148 HIS A ND1 1 
ATOM   1315 C  CD2 . HIS A 1 145 ? -9.11200  -4.10400  70.78700 1.000 8.90748  ? 148 HIS A CD2 1 
ATOM   1316 C  CE1 . HIS A 1 145 ? -8.08700  -3.56900  68.92300 1.000 9.34438  ? 148 HIS A CE1 1 
ATOM   1317 N  NE2 . HIS A 1 145 ? -8.60600  -4.58100  69.60100 1.000 9.95498  ? 148 HIS A NE2 1 
ATOM   1318 N  N   . ASN A 1 146 ? -11.00700 -0.47200  73.97300 1.000 7.92842  ? 149 ASN A N   1 
ATOM   1319 C  CA  . ASN A 1 146 ? -10.97100 0.33600   75.18500 1.000 9.02592  ? 149 ASN A CA  1 
ATOM   1320 C  C   . ASN A 1 146 ? -9.75100  -0.01400  76.02800 1.000 8.82589  ? 149 ASN A C   1 
ATOM   1321 O  O   . ASN A 1 146 ? -9.43100  -1.19000  76.22400 1.000 9.67336  ? 149 ASN A O   1 
ATOM   1322 C  CB  . ASN A 1 146 ? -12.21100 0.10200   76.04200 1.000 10.17606 ? 149 ASN A CB  1 
ATOM   1323 C  CG  . ASN A 1 146 ? -13.48400 0.53800   75.36800 1.000 11.56306 ? 149 ASN A CG  1 
ATOM   1324 O  OD1 . ASN A 1 146 ? -13.51400 1.48600   74.59600 1.000 12.06576 ? 149 ASN A OD1 1 
ATOM   1325 N  ND2 . ASN A 1 146 ? -14.55900 -0.15300  75.68000 1.000 13.60278 ? 149 ASN A ND2 1 
ATOM   1326 N  N   . VAL A 1 147 ? -9.09600  1.02100   76.55700 1.000 8.77589  ? 150 VAL A N   1 
ATOM   1327 C  CA  . VAL A 1 147 ? -7.92300  0.90200   77.41900 1.000 8.21266  ? 150 VAL A CA  1 
ATOM   1328 C  C   . VAL A 1 147 ? -8.37700  1.25800   78.82600 1.000 7.37309  ? 150 VAL A C   1 
ATOM   1329 O  O   . VAL A 1 147 ? -8.72400  2.41500   79.08800 1.000 8.48901  ? 150 VAL A O   1 
ATOM   1330 C  CB  . VAL A 1 147 ? -6.82300  1.87300   76.96600 1.000 8.56534  ? 150 VAL A CB  1 
ATOM   1331 C  CG1 . VAL A 1 147 ? -5.68700  1.92300   77.99800 1.000 8.50743  ? 150 VAL A CG1 1 
ATOM   1332 C  CG2 . VAL A 1 147 ? -6.32400  1.49500   75.58200 1.000 9.48650  ? 150 VAL A CG2 1 
ATOM   1333 N  N   . TYR A 1 148 ? -8.35700  0.29200   79.75200 1.000 8.60481  ? 151 TYR A N   1 
ATOM   1334 C  CA  . TYR A 1 148 ? -8.87700  0.51800   81.10100 1.000 8.31267  ? 151 TYR A CA  1 
ATOM   1335 C  C   . TYR A 1 148 ? -7.76100  0.98000   82.02500 1.000 8.81010  ? 151 TYR A C   1 
ATOM   1336 O  O   . TYR A 1 148 ? -6.81200  0.23100   82.26500 1.000 10.14710 ? 151 TYR A O   1 
ATOM   1337 C  CB  . TYR A 1 148 ? -9.56100  -0.74300  81.63800 1.000 9.40754  ? 151 TYR A CB  1 
ATOM   1338 C  CG  . TYR A 1 148 ? -10.71900 -1.11400  80.74800 1.000 9.82075  ? 151 TYR A CG  1 
ATOM   1339 C  CD1 . TYR A 1 148 ? -11.92500 -0.42600  80.84400 1.000 11.20513 ? 151 TYR A CD1 1 
ATOM   1340 C  CD2 . TYR A 1 148 ? -10.60200 -2.10700  79.76900 1.000 11.32356 ? 151 TYR A CD2 1 
ATOM   1341 C  CE1 . TYR A 1 148 ? -12.99200 -0.73300  80.00900 1.000 12.13682 ? 151 TYR A CE1 1 
ATOM   1342 C  CE2 . TYR A 1 148 ? -11.66300 -2.42000  78.93300 1.000 12.13155 ? 151 TYR A CE2 1 
ATOM   1343 C  CZ  . TYR A 1 148 ? -12.85500 -1.72900  79.05400 1.000 12.01575 ? 151 TYR A CZ  1 
ATOM   1344 O  OH  . TYR A 1 148 ? -13.91000 -2.01700  78.22800 1.000 13.41855 ? 151 TYR A OH  1 
ATOM   1345 N  N   . ILE A 1 149 ? -7.89400  2.20000   82.55400 1.000 8.79431  ? 152 ILE A N   1 
ATOM   1346 C  CA  . ILE A 1 149 ? -6.85900  2.85600   83.35200 1.000 8.98907  ? 152 ILE A CA  1 
ATOM   1347 C  C   . ILE A 1 149 ? -7.26000  2.89100   84.81600 1.000 8.73641  ? 152 ILE A C   1 
ATOM   1348 O  O   . ILE A 1 149 ? -8.41000  3.20400   85.15800 1.000 9.70495  ? 152 ILE A O   1 
ATOM   1349 C  CB  . ILE A 1 149 ? -6.62500  4.28400   82.83200 1.000 8.98381  ? 152 ILE A CB  1 
ATOM   1350 C  CG1 . ILE A 1 149 ? -6.04900  4.20000   81.42300 1.000 9.79706  ? 152 ILE A CG1 1 
ATOM   1351 C  CG2 . ILE A 1 149 ? -5.66700  5.07200   83.74100 1.000 9.79180  ? 152 ILE A CG2 1 
ATOM   1352 C  CD1 . ILE A 1 149 ? -5.88900  5.54300   80.79300 1.000 9.28911  ? 152 ILE A CD1 1 
ATOM   1353 N  N   . THR A 1 150 ? -6.28100  2.63200   85.68300 1.000 9.44176  ? 153 THR A N   1 
ATOM   1354 C  CA  A THR A 1 150 ? -6.44600  2.77000   87.12200 0.560 10.07078 ? 153 THR A CA  1 
ATOM   1355 C  CA  B THR A 1 150 ? -6.45000  2.78300   87.12000 0.440 9.54378  ? 153 THR A CA  1 
ATOM   1356 C  C   . THR A 1 150 ? -5.19900  3.42800   87.70500 1.000 9.33122  ? 153 THR A C   1 
ATOM   1357 O  O   . THR A 1 150 ? -4.10900  3.36500   87.13100 1.000 9.41017  ? 153 THR A O   1 
ATOM   1358 C  CB  A THR A 1 150 ? -6.69600  1.40800   87.79500 0.560 11.59991 ? 153 THR A CB  1 
ATOM   1359 C  CB  B THR A 1 150 ? -6.73400  1.43000   87.79700 0.440 12.57378 ? 153 THR A CB  1 
ATOM   1360 O  OG1 A THR A 1 150 ? -5.62700  0.50700   87.47400 0.560 12.95797 ? 153 THR A OG1 1 
ATOM   1361 O  OG1 B THR A 1 150 ? -7.28100  1.63900   89.10100 0.440 11.12378 ? 153 THR A OG1 1 
ATOM   1362 C  CG2 A THR A 1 150 ? -7.99600  0.78200   87.31400 0.560 11.96838 ? 153 THR A CG2 1 
ATOM   1363 C  CG2 B THR A 1 150 ? -5.45700  0.62200   87.93800 0.440 14.27378 ? 153 THR A CG2 1 
ATOM   1364 N  N   . ALA A 1 151 ? -5.36100  4.05900   88.86400 1.000 9.98393  ? 154 ALA A N   1 
ATOM   1365 C  CA  . ALA A 1 151 ? -4.21700  4.70200   89.50000 1.000 10.55768 ? 154 ALA A CA  1 
ATOM   1366 C  C   . ALA A 1 151 ? -3.24100  3.66800   90.05400 1.000 11.46832 ? 154 ALA A C   1 
ATOM   1367 O  O   . ALA A 1 151 ? -3.62900  2.56400   90.44300 1.000 12.40001 ? 154 ALA A O   1 
ATOM   1368 C  CB  . ALA A 1 151 ? -4.68600  5.60200   90.63500 1.000 12.12629 ? 154 ALA A CB  1 
ATOM   1369 N  N   . ASP A 1 152 ? -1.95100  4.05200   90.10300 1.000 11.95785 ? 155 ASP A N   1 
ATOM   1370 C  CA  A ASP A 1 152 ? -0.86900  3.25700   90.70000 0.470 12.55378 ? 155 ASP A CA  1 
ATOM   1371 C  CA  B ASP A 1 152 ? -0.88500  3.25200   90.72900 0.530 15.61618 ? 155 ASP A CA  1 
ATOM   1372 C  C   . ASP A 1 152 ? -0.13400  4.18400   91.68000 1.000 14.77398 ? 155 ASP A C   1 
ATOM   1373 O  O   . ASP A 1 152 ? 0.94400   4.70400   91.36200 1.000 15.60039 ? 155 ASP A O   1 
ATOM   1374 C  CB  A ASP A 1 152 ? 0.05600   2.75000   89.58200 0.470 16.04378 ? 155 ASP A CB  1 
ATOM   1375 C  CB  B ASP A 1 152 ? 0.04600   2.63200   89.69100 0.530 20.25358 ? 155 ASP A CB  1 
ATOM   1376 C  CG  A ASP A 1 152 ? 0.81500   1.48900   89.96000 0.470 33.01378 ? 155 ASP A CG  1 
ATOM   1377 C  CG  B ASP A 1 152 ? 1.05800   1.67700   90.31500 0.530 26.84378 ? 155 ASP A CG  1 
ATOM   1378 O  OD1 A ASP A 1 152 ? 0.67200   1.01700   91.11100 0.470 17.46378 ? 155 ASP A OD1 1 
ATOM   1379 O  OD1 B ASP A 1 152 ? 1.13300   1.60600   91.56600 0.530 21.44378 ? 155 ASP A OD1 1 
ATOM   1380 O  OD2 A ASP A 1 152 ? 1.55600   0.97100   89.09200 0.470 18.93378 ? 155 ASP A OD2 1 
ATOM   1381 O  OD2 B ASP A 1 152 ? 1.77700   0.99700   89.55300 0.530 33.91378 ? 155 ASP A OD2 1 
ATOM   1382 N  N   . LYS A 1 153 ? -0.70600  4.37600   92.87900 1.000 16.62157 ? 156 LYS A N   1 
ATOM   1383 C  CA  . LYS A 1 153 ? -0.24900  5.46000   93.75100 1.000 18.49811 ? 156 LYS A CA  1 
ATOM   1384 C  C   . LYS A 1 153 ? 1.18200   5.27300   94.25000 1.000 17.34534 ? 156 LYS A C   1 
ATOM   1385 O  O   . LYS A 1 153 ? 1.91800   6.25500   94.39400 1.000 17.85856 ? 156 LYS A O   1 
ATOM   1386 C  CB  . LYS A 1 153 ? -1.24400  5.70100   94.88600 1.000 23.82769 ? 156 LYS A CB  1 
ATOM   1387 C  CG  . LYS A 1 153 ? -2.57200  6.27700   94.39000 1.000 31.63378 ? 156 LYS A CG  1 
ATOM   1388 C  CD  . LYS A 1 153 ? -3.53200  6.61000   95.53000 1.000 37.20378 ? 156 LYS A CD  1 
ATOM   1389 C  CE  . LYS A 1 153 ? -4.76800  7.36500   95.02300 1.000 42.04378 ? 156 LYS A CE  1 
ATOM   1390 N  NZ  . LYS A 1 153 ? -4.45300  8.74000   94.53000 1.000 44.47378 ? 156 LYS A NZ  1 
ATOM   1391 N  N   . GLN A 1 154 ? 1.60200   4.03800   94.53100 1.000 16.58735 ? 157 GLN A N   1 
ATOM   1392 C  CA  . GLN A 1 154 ? 2.95800   3.86200   95.05200 1.000 18.43231 ? 157 GLN A CA  1 
ATOM   1393 C  C   . GLN A 1 154 ? 4.01100   4.23900   94.02300 1.000 17.50062 ? 157 GLN A C   1 
ATOM   1394 O  O   . GLN A 1 154 ? 5.13700   4.61000   94.38500 1.000 19.47191 ? 157 GLN A O   1 
ATOM   1395 C  CB  . GLN A 1 154 ? 3.18900   2.41900   95.47100 1.000 21.11378 ? 157 GLN A CB  1 
ATOM   1396 C  CG  . GLN A 1 154 ? 2.60900   2.04400   96.80800 1.000 54.76378 ? 157 GLN A CG  1 
ATOM   1397 C  CD  . GLN A 1 154 ? 3.24500   0.78500   97.34800 1.000 74.58378 ? 157 GLN A CD  1 
ATOM   1398 O  OE1 . GLN A 1 154 ? 4.09900   0.84000   98.23200 1.000 51.01378 ? 157 GLN A OE1 1 
ATOM   1399 N  NE2 . GLN A 1 154 ? 2.84800   -0.36000  96.80300 1.000 67.14378 ? 157 GLN A NE2 1 
ATOM   1400 N  N   . LYS A 1 155 ? 3.68100   4.09900   92.74500 1.000 16.68999 ? 158 LYS A N   1 
ATOM   1401 C  CA  A LYS A 1 155 ? 4.56300   4.49000   91.65900 0.440 10.64378 ? 158 LYS A CA  1 
ATOM   1402 C  CA  B LYS A 1 155 ? 4.55900   4.48700   91.65800 0.560 22.77378 ? 158 LYS A CA  1 
ATOM   1403 C  C   . LYS A 1 155 ? 4.34500   5.93200   91.23400 1.000 14.85030 ? 158 LYS A C   1 
ATOM   1404 O  O   . LYS A 1 155 ? 5.02200   6.39700   90.30900 1.000 13.65016 ? 158 LYS A O   1 
ATOM   1405 C  CB  A LYS A 1 155 ? 4.34000   3.58300   90.44400 0.440 12.51378 ? 158 LYS A CB  1 
ATOM   1406 C  CB  B LYS A 1 155 ? 4.32000   3.56100   90.46300 0.560 32.67378 ? 158 LYS A CB  1 
ATOM   1407 C  CG  A LYS A 1 155 ? 4.56800   2.09300   90.69000 0.440 29.62378 ? 158 LYS A CG  1 
ATOM   1408 C  CG  B LYS A 1 155 ? 4.60600   2.08700   90.73000 0.560 29.48378 ? 158 LYS A CG  1 
ATOM   1409 C  CD  A LYS A 1 155 ? 6.04700   1.74300   90.73400 0.440 25.02378 ? 158 LYS A CD  1 
ATOM   1410 C  CD  B LYS A 1 155 ? 6.08100   1.77700   90.57200 0.560 33.85378 ? 158 LYS A CD  1 
ATOM   1411 C  CE  A LYS A 1 155 ? 6.77500   2.12600   89.44500 0.440 11.73378 ? 158 LYS A CE  1 
ATOM   1412 C  CE  B LYS A 1 155 ? 6.29600   0.41600   89.93000 0.560 53.25378 ? 158 LYS A CE  1 
ATOM   1413 N  NZ  A LYS A 1 155 ? 6.26800   1.37900   88.25300 0.440 26.34378 ? 158 LYS A NZ  1 
ATOM   1414 N  NZ  B LYS A 1 155 ? 5.77800   -0.69500  90.77300 0.560 38.47378 ? 158 LYS A NZ  1 
ATOM   1415 N  N   . ASN A 1 156 ? 3.40500   6.63900   91.87500 1.000 14.18443 ? 159 ASN A N   1 
ATOM   1416 C  CA  . ASN A 1 156 ? 3.03400   7.99700   91.47500 1.000 13.26853 ? 159 ASN A CA  1 
ATOM   1417 C  C   . ASN A 1 156 ? 2.53800   8.02700   90.02500 1.000 11.69992 ? 159 ASN A C   1 
ATOM   1418 O  O   . ASN A 1 156 ? 2.79300   8.97900   89.28500 1.000 11.70255 ? 159 ASN A O   1 
ATOM   1419 C  CB  . ASN A 1 156 ? 4.19700   8.97100   91.69400 1.000 13.61857 ? 159 ASN A CB  1 
ATOM   1420 C  CG  . ASN A 1 156 ? 3.74300   10.42600  91.73000 1.000 15.28456 ? 159 ASN A CG  1 
ATOM   1421 O  OD1 . ASN A 1 156 ? 2.60000   10.73500  92.09800 1.000 16.80843 ? 159 ASN A OD1 1 
ATOM   1422 N  ND2 . ASN A 1 156 ? 4.63200   11.32800  91.32500 1.000 17.28743 ? 159 ASN A ND2 1 
ATOM   1423 N  N   . GLY A 1 157 ? 1.82500   6.98300   89.60700 1.000 10.91299 ? 160 GLY A N   1 
ATOM   1424 C  CA  . GLY A 1 157 ? 1.49200   6.79400   88.20200 1.000 10.68138 ? 160 GLY A CA  1 
ATOM   1425 C  C   . GLY A 1 157 ? 0.18200   6.07000   87.97400 1.000 9.82865  ? 160 GLY A C   1 
ATOM   1426 O  O   . GLY A 1 157 ? -0.76700  6.21700   88.75300 1.000 10.57610 ? 160 GLY A O   1 
ATOM   1427 N  N   . ILE A 1 158 ? 0.12100   5.31400   86.87300 1.000 9.58914  ? 161 ILE A N   1 
ATOM   1428 C  CA  A ILE A 1 158 ? -1.08500  4.60300   86.48000 0.720 9.31806  ? 161 ILE A CA  1 
ATOM   1429 C  CA  B ILE A 1 158 ? -1.08500  4.61300   86.45600 0.280 8.91378  ? 161 ILE A CA  1 
ATOM   1430 C  C   . ILE A 1 158 ? -0.71400  3.22000   85.97000 1.000 9.29174  ? 161 ILE A C   1 
ATOM   1431 O  O   . ILE A 1 158 ? 0.44000   2.93200   85.64200 1.000 9.35227  ? 161 ILE A O   1 
ATOM   1432 C  CB  A ILE A 1 158 ? -1.89000  5.34200   85.38500 0.720 9.60230  ? 161 ILE A CB  1 
ATOM   1433 C  CB  B ILE A 1 158 ? -1.86400  5.36000   85.34200 0.280 8.67378  ? 161 ILE A CB  1 
ATOM   1434 C  CG1 A ILE A 1 158 ? -1.04000  5.52300   84.12500 0.720 10.06288 ? 161 ILE A CG1 1 
ATOM   1435 C  CG1 B ILE A 1 158 ? -1.00300  5.53900   84.08500 0.280 14.21378 ? 161 ILE A CG1 1 
ATOM   1436 C  CG2 A ILE A 1 158 ? -2.38900  6.67200   85.89700 0.720 9.62073  ? 161 ILE A CG2 1 
ATOM   1437 C  CG2 B ILE A 1 158 ? -2.35400  6.70300   85.83600 0.280 15.05378 ? 161 ILE A CG2 1 
ATOM   1438 C  CD1 A ILE A 1 158 ? -1.81600  5.98200   82.96200 0.720 10.58400 ? 161 ILE A CD1 1 
ATOM   1439 C  CD1 B ILE A 1 158 ? -1.29300  4.53600   82.96800 0.280 10.60378 ? 161 ILE A CD1 1 
ATOM   1440 N  N   . LYS A 1 159 ? -1.72200  2.36200   85.91500 1.000 9.67863  ? 162 LYS A N   1 
ATOM   1441 C  CA  A LYS A 1 159 ? -1.60400  1.10300   85.21200 0.610 11.26040 ? 162 LYS A CA  1 
ATOM   1442 C  CA  B LYS A 1 159 ? -1.64200  1.06400   85.27000 0.390 10.04378 ? 162 LYS A CA  1 
ATOM   1443 C  C   . LYS A 1 159 ? -2.81200  0.94300   84.30600 1.000 9.14962  ? 162 LYS A C   1 
ATOM   1444 O  O   . LYS A 1 159 ? -3.81700  1.65600   84.43200 1.000 9.81022  ? 162 LYS A O   1 
ATOM   1445 C  CB  A LYS A 1 159 ? -1.46500  -0.07000  86.18300 0.610 14.97400 ? 162 LYS A CB  1 
ATOM   1446 C  CB  B LYS A 1 159 ? -1.73800  -0.07100  86.29500 0.390 15.98378 ? 162 LYS A CB  1 
ATOM   1447 C  CG  A LYS A 1 159 ? -2.54400  -0.13900  87.22800 0.610 16.63209 ? 162 LYS A CG  1 
ATOM   1448 C  CG  B LYS A 1 159 ? -0.56700  -0.15300  87.25300 0.390 12.07378 ? 162 LYS A CG  1 
ATOM   1449 C  CD  A LYS A 1 159 ? -2.19400  -1.16300  88.30000 0.610 20.29378 ? 162 LYS A CD  1 
ATOM   1450 C  CD  B LYS A 1 159 ? -0.78000  -1.25600  88.27900 0.390 33.49378 ? 162 LYS A CD  1 
ATOM   1451 C  CE  A LYS A 1 159 ? -3.39700  -1.46600  89.17800 0.610 29.76378 ? 162 LYS A CE  1 
ATOM   1452 N  NZ  A LYS A 1 159 ? -3.92100  -0.25400  89.85700 0.610 23.44378 ? 162 LYS A NZ  1 
ATOM   1453 N  N   . ALA A 1 160 ? -2.68600  0.03200   83.35000 1.000 9.24700  ? 163 ALA A N   1 
ATOM   1454 C  CA  . ALA A 1 160 ? -3.77400  -0.20200  82.42700 1.000 9.77864  ? 163 ALA A CA  1 
ATOM   1455 C  C   . ALA A 1 160 ? -3.77200  -1.65100  82.00700 1.000 8.91538  ? 163 ALA A C   1 
ATOM   1456 O  O   . ALA A 1 160 ? -2.73800  -2.32500  82.01500 1.000 9.37859  ? 163 ALA A O   1 
ATOM   1457 C  CB  . ALA A 1 160 ? -3.72900  0.71000   81.19400 1.000 10.72349 ? 163 ALA A CB  1 
ATOM   1458 N  N   A ASN A 1 161 ? -4.96200  -2.12700  81.65900 0.670 10.66822 ? 164 ASN A N   1 
ATOM   1459 N  N   B ASN A 1 161 ? -4.94300  -2.13200  81.62800 0.330 8.17378  ? 164 ASN A N   1 
ATOM   1460 C  CA  A ASN A 1 161 ? -5.17100  -3.46400  81.13000 0.670 13.00008 ? 164 ASN A CA  1 
ATOM   1461 C  CA  B ASN A 1 161 ? -5.01800  -3.45900  81.04900 0.330 6.99378  ? 164 ASN A CA  1 
ATOM   1462 C  C   A ASN A 1 161 ? -6.09300  -3.34800  79.93000 0.670 10.65243 ? 164 ASN A C   1 
ATOM   1463 C  C   B ASN A 1 161 ? -6.09600  -3.44000  79.98700 0.330 15.99378 ? 164 ASN A C   1 
ATOM   1464 O  O   A ASN A 1 161 ? -7.03100  -2.53700  79.93500 0.670 9.99446  ? 164 ASN A O   1 
ATOM   1465 O  O   B ASN A 1 161 ? -7.12600  -2.77700  80.14300 0.330 21.09378 ? 164 ASN A O   1 
ATOM   1466 C  CB  A ASN A 1 161 ? -5.85300  -4.36900  82.16600 0.670 17.49799 ? 164 ASN A CB  1 
ATOM   1467 C  CB  B ASN A 1 161 ? -5.32700  -4.52900  82.09600 0.330 13.58378 ? 164 ASN A CB  1 
ATOM   1468 C  CG  A ASN A 1 161 ? -4.94200  -4.72700  83.32400 0.670 22.22378 ? 164 ASN A CG  1 
ATOM   1469 C  CG  B ASN A 1 161 ? -6.75400  -4.47300  82.57200 0.330 17.00378 ? 164 ASN A CG  1 
ATOM   1470 O  OD1 A ASN A 1 161 ? -4.24200  -5.73600  83.28300 0.670 35.16378 ? 164 ASN A OD1 1 
ATOM   1471 O  OD1 B ASN A 1 161 ? -7.64600  -5.04000  81.94500 0.330 14.47378 ? 164 ASN A OD1 1 
ATOM   1472 N  ND2 A ASN A 1 161 ? -4.95100  -3.90600  84.36500 0.670 25.56378 ? 164 ASN A ND2 1 
ATOM   1473 N  ND2 B ASN A 1 161 ? -6.98400  -3.78400  83.68200 0.330 24.27378 ? 164 ASN A ND2 1 
ATOM   1474 N  N   . PHE A 1 162 ? -5.84600  -4.16800  78.91200 1.000 10.38134 ? 165 PHE A N   1 
ATOM   1475 C  CA  . PHE A 1 162 ? -6.76900  -4.19600  77.79300 1.000 9.51808  ? 165 PHE A CA  1 
ATOM   1476 C  C   . PHE A 1 162 ? -6.40400  -5.36600  76.91100 1.000 8.76273  ? 165 PHE A C   1 
ATOM   1477 O  O   . PHE A 1 162 ? -5.32200  -5.94300  77.02800 1.000 8.94959  ? 165 PHE A O   1 
ATOM   1478 C  CB  . PHE A 1 162 ? -6.82700  -2.88400  77.00200 1.000 10.18132 ? 165 PHE A CB  1 
ATOM   1479 C  CG  . PHE A 1 162 ? -5.49400  -2.32500  76.56700 1.000 8.23898  ? 165 PHE A CG  1 
ATOM   1480 C  CD1 . PHE A 1 162 ? -4.66200  -1.64000  77.46100 1.000 8.79168  ? 165 PHE A CD1 1 
ATOM   1481 C  CD2 . PHE A 1 162 ? -5.10900  -2.42000  75.23900 1.000 8.84958  ? 165 PHE A CD2 1 
ATOM   1482 C  CE1 . PHE A 1 162 ? -3.45500  -1.05200  77.01800 1.000 8.64166  ? 165 PHE A CE1 1 
ATOM   1483 C  CE2 . PHE A 1 162 ? -3.90700  -1.86000  74.78900 1.000 8.84432  ? 165 PHE A CE2 1 
ATOM   1484 C  CZ  . PHE A 1 162 ? -3.08300  -1.17200  75.68000 1.000 8.36794  ? 165 PHE A CZ  1 
ATOM   1485 N  N   . LYS A 1 163 ? -7.33000  -5.70300  76.02700 1.000 10.02341 ? 166 LYS A N   1 
ATOM   1486 C  CA  . LYS A 1 163 ? -7.18800  -6.83800  75.12700 1.000 9.57335  ? 166 LYS A CA  1 
ATOM   1487 C  C   . LYS A 1 163 ? -7.23000  -6.32200  73.69900 1.000 10.28923 ? 166 LYS A C   1 
ATOM   1488 O  O   . LYS A 1 163 ? -8.25400  -5.79300  73.26000 1.000 14.39235 ? 166 LYS A O   1 
ATOM   1489 C  CB  . LYS A 1 163 ? -8.31700  -7.85200  75.35000 1.000 9.46281  ? 166 LYS A CB  1 
ATOM   1490 C  CG  . LYS A 1 163 ? -8.20200  -8.62100  76.65700 1.000 10.71296 ? 166 LYS A CG  1 
ATOM   1491 C  CD  . LYS A 1 163 ? -9.39100  -9.56300  76.84900 1.000 12.44738 ? 166 LYS A CD  1 
ATOM   1492 C  CE  . LYS A 1 163 ? -9.23200  -10.39200 78.10300 1.000 12.82111 ? 166 LYS A CE  1 
ATOM   1493 N  NZ  . LYS A 1 163 ? -8.26400  -11.53200 77.90400 1.000 12.97639 ? 166 LYS A NZ  1 
ATOM   1494 N  N   . ILE A 1 164 ? -6.14400  -6.46600  72.98400 1.000 7.93368  ? 167 ILE A N   1 
ATOM   1495 C  CA  . ILE A 1 164 ? -6.12400  -6.13400  71.56800 1.000 7.36782  ? 167 ILE A CA  1 
ATOM   1496 C  C   . ILE A 1 164 ? -6.42700  -7.40300  70.79800 1.000 7.16254  ? 167 ILE A C   1 
ATOM   1497 O  O   . ILE A 1 164 ? -5.89000  -8.47400  71.10100 1.000 8.28109  ? 167 ILE A O   1 
ATOM   1498 C  CB  . ILE A 1 164 ? -4.74600  -5.57300  71.16600 1.000 8.08896  ? 167 ILE A CB  1 
ATOM   1499 C  CG1 . ILE A 1 164 ? -4.47200  -4.22400  71.85100 1.000 7.97842  ? 167 ILE A CG1 1 
ATOM   1500 C  CG2 . ILE A 1 164 ? -4.60900  -5.47500  69.64100 1.000 9.04434  ? 167 ILE A CG2 1 
ATOM   1501 C  CD1 . ILE A 1 164 ? -5.39800  -3.10900  71.42700 1.000 7.79682  ? 167 ILE A CD1 1 
ATOM   1502 N  N   . ARG A 1 165 ? -7.26900  -7.29800  69.78100 1.000 8.30478  ? 168 ARG A N   1 
ATOM   1503 C  CA  A ARG A 1 165 ? -7.54200  -8.42200  68.90400 0.720 9.92339  ? 168 ARG A CA  1 
ATOM   1504 C  CA  B ARG A 1 165 ? -7.56600  -8.41800  68.90000 0.280 11.04378 ? 168 ARG A CA  1 
ATOM   1505 C  C   . ARG A 1 165 ? -7.05000  -8.09700  67.50500 1.000 9.01013  ? 168 ARG A C   1 
ATOM   1506 O  O   . ARG A 1 165 ? -7.51600  -7.14500  66.87200 1.000 10.36555 ? 168 ARG A O   1 
ATOM   1507 C  CB  A ARG A 1 165 ? -9.02700  -8.75900  68.93100 0.720 12.36053 ? 168 ARG A CB  1 
ATOM   1508 C  CB  B ARG A 1 165 ? -9.07000  -8.67800  68.86600 0.280 17.88378 ? 168 ARG A CB  1 
ATOM   1509 C  CG  A ARG A 1 165 ? -9.38700  -9.34100  70.28400 0.720 15.23982 ? 168 ARG A CG  1 
ATOM   1510 C  CG  B ARG A 1 165 ? -9.57400  -9.43200  70.08000 0.280 29.74378 ? 168 ARG A CG  1 
ATOM   1511 C  CD  A ARG A 1 165 ? -10.80500 -9.83500  70.39300 0.720 20.50378 ? 168 ARG A CD  1 
ATOM   1512 C  CD  B ARG A 1 165 ? -11.08200 -9.39400  70.16900 0.280 29.34378 ? 168 ARG A CD  1 
ATOM   1513 N  NE  A ARG A 1 165 ? -11.08100 -10.21700 71.77400 0.720 27.80378 ? 168 ARG A NE  1 
ATOM   1514 N  NE  B ARG A 1 165 ? -11.54200 -8.15600  70.78100 0.280 14.84378 ? 168 ARG A NE  1 
ATOM   1515 C  CZ  A ARG A 1 165 ? -11.34400 -9.35500  72.74900 0.720 23.62378 ? 168 ARG A CZ  1 
ATOM   1516 C  CZ  B ARG A 1 165 ? -12.05500 -7.12800  70.11900 0.280 24.70378 ? 168 ARG A CZ  1 
ATOM   1517 N  NH1 A ARG A 1 165 ? -11.41600 -8.05500  72.52200 0.720 24.14615 ? 168 ARG A NH1 1 
ATOM   1518 N  NH1 B ARG A 1 165 ? -12.22100 -7.16000  68.80800 0.280 23.96378 ? 168 ARG A NH1 1 
ATOM   1519 N  NH2 A ARG A 1 165 ? -11.55200 -9.81100  73.97900 0.720 23.17761 ? 168 ARG A NH2 1 
ATOM   1520 N  NH2 B ARG A 1 165 ? -12.42100 -6.04400  70.79300 0.280 32.37378 ? 168 ARG A NH2 1 
ATOM   1521 N  N   . HIS A 1 166 ? -6.09100  -8.88000  67.03100 1.000 7.69418  ? 169 HIS A N   1 
ATOM   1522 C  CA  . HIS A 1 166 ? -5.55800  -8.71800  65.68700 1.000 7.57838  ? 169 HIS A CA  1 
ATOM   1523 C  C   . HIS A 1 166 ? -6.22400  -9.72900  64.76500 1.000 7.88894  ? 169 HIS A C   1 
ATOM   1524 O  O   . HIS A 1 166 ? -6.14500  -10.93800 65.00100 1.000 9.73390  ? 169 HIS A O   1 
ATOM   1525 C  CB  . HIS A 1 166 ? -4.05900  -9.01500  65.67600 1.000 7.99422  ? 169 HIS A CB  1 
ATOM   1526 C  CG  . HIS A 1 166 ? -3.22900  -8.07400  66.50600 1.000 7.64154  ? 169 HIS A CG  1 
ATOM   1527 N  ND1 . HIS A 1 166 ? -3.12500  -6.72600  66.23900 1.000 7.36782  ? 169 HIS A ND1 1 
ATOM   1528 C  CD2 . HIS A 1 166 ? -2.41000  -8.31300  67.55900 1.000 7.98106  ? 169 HIS A CD2 1 
ATOM   1529 C  CE1 . HIS A 1 166 ? -2.29700  -6.17400  67.11400 1.000 7.19412  ? 169 HIS A CE1 1 
ATOM   1530 N  NE2 . HIS A 1 166 ? -1.85300  -7.11200  67.92900 1.000 7.10990  ? 169 HIS A NE2 1 
ATOM   1531 N  N   . ASN A 1 167 ? -6.82100  -9.25500  63.69200 1.000 7.91263  ? 170 ASN A N   1 
ATOM   1532 C  CA  A ASN A 1 167 ? -7.45900  -10.15500 62.73900 0.560 8.37847  ? 170 ASN A CA  1 
ATOM   1533 C  CA  B ASN A 1 167 ? -7.45800  -10.15800 62.74200 0.440 8.98378  ? 170 ASN A CA  1 
ATOM   1534 C  C   . ASN A 1 167 ? -6.39900  -11.00800 62.05200 1.000 8.63640  ? 170 ASN A C   1 
ATOM   1535 O  O   . ASN A 1 167 ? -5.37000  -10.49200 61.59800 1.000 8.91011  ? 170 ASN A O   1 
ATOM   1536 C  CB  A ASN A 1 167 ? -8.19000  -9.34000  61.67400 0.560 9.20752  ? 170 ASN A CB  1 
ATOM   1537 C  CB  B ASN A 1 167 ? -8.21100  -9.34900  61.69000 0.440 10.62378 ? 170 ASN A CB  1 
ATOM   1538 C  CG  A ASN A 1 167 ? -9.49400  -8.75000  62.16900 0.560 10.27607 ? 170 ASN A CG  1 
ATOM   1539 C  CG  B ASN A 1 167 ? -9.27200  -8.46100  62.29500 0.440 15.91378 ? 170 ASN A CG  1 
ATOM   1540 O  OD1 A ASN A 1 167 ? -9.77800  -8.72300  63.36100 0.560 9.75232  ? 170 ASN A OD1 1 
ATOM   1541 O  OD1 B ASN A 1 167 ? -9.39400  -7.28600  61.94200 0.440 30.12378 ? 170 ASN A OD1 1 
ATOM   1542 N  ND2 A ASN A 1 167 ? -10.29300 -8.25600  61.23700 0.560 12.21841 ? 170 ASN A ND2 1 
ATOM   1543 N  ND2 B ASN A 1 167 ? -10.04200 -9.01200  63.21800 0.440 14.77378 ? 170 ASN A ND2 1 
ATOM   1544 N  N   . ILE A 1 168 ? -6.64600  -12.31900 61.98000 1.000 8.11265  ? 171 ILE A N   1 
ATOM   1545 C  CA  . ILE A 1 168 ? -5.78700  -13.25100 61.25500 1.000 8.69430  ? 171 ILE A CA  1 
ATOM   1546 C  C   . ILE A 1 168 ? -6.34100  -13.40300 59.83800 1.000 8.85484  ? 171 ILE A C   1 
ATOM   1547 O  O   . ILE A 1 168 ? -7.55500  -13.29100 59.60800 1.000 8.72588  ? 171 ILE A O   1 
ATOM   1548 C  CB  . ILE A 1 168 ? -5.73500  -14.61100 61.99500 1.000 9.62862  ? 171 ILE A CB  1 
ATOM   1549 C  CG1 . ILE A 1 168 ? -5.33100  -14.43700 63.46700 1.000 8.80221  ? 171 ILE A CG1 1 
ATOM   1550 C  CG2 . ILE A 1 168 ? -4.81600  -15.59400 61.27500 1.000 9.74443  ? 171 ILE A CG2 1 
ATOM   1551 C  CD1 . ILE A 1 168 ? -5.50100  -15.69000 64.28900 1.000 8.82326  ? 171 ILE A CD1 1 
ATOM   1552 N  N   . GLU A 1 169 ? -5.44600  -13.68300 58.88400 1.000 9.48124  ? 172 GLU A N   1 
ATOM   1553 C  CA  A GLU A 1 169 ? -5.82300  -13.78500 57.47600 0.600 10.91035 ? 172 GLU A CA  1 
ATOM   1554 C  CA  B GLU A 1 169 ? -5.83200  -13.78000 57.47800 0.400 9.80378  ? 172 GLU A CA  1 
ATOM   1555 C  C   . GLU A 1 169 ? -6.86600  -14.86700 57.20300 1.000 10.95246 ? 172 GLU A C   1 
ATOM   1556 O  O   . GLU A 1 169 ? -7.53200  -14.82200 56.15800 1.000 12.65530 ? 172 GLU A O   1 
ATOM   1557 C  CB  A GLU A 1 169 ? -4.57200  -14.05000 56.64000 0.600 12.56845 ? 172 GLU A CB  1 
ATOM   1558 C  CB  B GLU A 1 169 ? -4.60000  -14.00500 56.60300 0.400 14.63378 ? 172 GLU A CB  1 
ATOM   1559 C  CG  A GLU A 1 169 ? -3.93500  -15.38900 56.95400 0.600 14.33971 ? 172 GLU A CG  1 
ATOM   1560 C  CG  B GLU A 1 169 ? -3.65800  -12.82200 56.55900 0.400 17.14378 ? 172 GLU A CG  1 
ATOM   1561 C  CD  A GLU A 1 169 ? -2.49600  -15.50900 56.47900 0.600 17.08215 ? 172 GLU A CD  1 
ATOM   1562 C  CD  B GLU A 1 169 ? -2.55200  -12.98900 55.53200 0.400 20.11378 ? 172 GLU A CD  1 
ATOM   1563 O  OE1 A GLU A 1 169 ? -1.91200  -14.49900 56.02100 0.600 17.60589 ? 172 GLU A OE1 1 
ATOM   1564 O  OE1 B GLU A 1 169 ? -2.19300  -14.14000 55.22200 0.400 26.24378 ? 172 GLU A OE1 1 
ATOM   1565 O  OE2 A GLU A 1 169 ? -1.94800  -16.62700 56.58600 0.600 18.32703 ? 172 GLU A OE2 1 
ATOM   1566 O  OE2 B GLU A 1 169 ? -2.04200  -11.96500 55.02800 0.400 15.13378 ? 172 GLU A OE2 1 
ATOM   1567 N  N   . ASP A 1 170 ? -7.01300  -15.84700 58.09000 1.000 10.19448 ? 173 ASP A N   1 
ATOM   1568 C  CA  . ASP A 1 170 ? -8.02400  -16.88700 57.92300 1.000 10.35502 ? 173 ASP A CA  1 
ATOM   1569 C  C   . ASP A 1 170 ? -9.37200  -16.48300 58.49400 1.000 10.42872 ? 173 ASP A C   1 
ATOM   1570 O  O   . ASP A 1 170 ? -10.29600 -17.30300 58.52200 1.000 11.74466 ? 173 ASP A O   1 
ATOM   1571 C  CB  . ASP A 1 170 ? -7.54900  -18.21100 58.52800 1.000 11.03405 ? 173 ASP A CB  1 
ATOM   1572 C  CG  . ASP A 1 170 ? -7.40700  -18.15400 60.03600 1.000 10.27080 ? 173 ASP A CG  1 
ATOM   1573 O  OD1 . ASP A 1 170 ? -7.58500  -17.06800 60.63800 1.000 10.02341 ? 173 ASP A OD1 1 
ATOM   1574 O  OD2 . ASP A 1 170 ? -7.11600  -19.21500 60.63200 1.000 11.22618 ? 173 ASP A OD2 1 
ATOM   1575 N  N   . GLY A 1 171 ? -9.51100  -15.23900 58.93600 1.000 10.11552 ? 174 GLY A N   1 
ATOM   1576 C  CA  . GLY A 1 171 ? -10.74100 -14.78500 59.54600 1.000 10.14974 ? 174 GLY A CA  1 
ATOM   1577 C  C   . GLY A 1 171 ? -10.78900 -14.91500 61.05000 1.000 9.26542  ? 174 GLY A C   1 
ATOM   1578 O  O   . GLY A 1 171 ? -11.72800 -14.39600 61.67200 1.000 9.75495  ? 174 GLY A O   1 
ATOM   1579 N  N   . SER A 1 172 ? -9.82500  -15.59900 61.65200 1.000 8.64693  ? 175 SER A N   1 
ATOM   1580 C  CA  . SER A 1 172 ? -9.79400  -15.75500 63.10200 1.000 8.23635  ? 175 SER A CA  1 
ATOM   1581 C  C   . SER A 1 172 ? -9.20700  -14.49700 63.74600 1.000 7.56258  ? 175 SER A C   1 
ATOM   1582 O  O   . SER A 1 172 ? -9.01500  -13.46900 63.09200 1.000 8.59955  ? 175 SER A O   1 
ATOM   1583 C  CB  . SER A 1 172 ? -9.05800  -17.04000 63.48400 1.000 8.59955  ? 175 SER A CB  1 
ATOM   1584 O  OG  . SER A 1 172 ? -9.18800  -17.32600 64.87100 1.000 8.95222  ? 175 SER A OG  1 
ATOM   1585 N  N   . VAL A 1 173 ? -8.91300  -14.56900 65.04100 1.000 7.73629  ? 176 VAL A N   1 
ATOM   1586 C  CA  A VAL A 1 173 ? -8.34000  -13.44900 65.77200 0.750 11.31040 ? 176 VAL A CA  1 
ATOM   1587 C  CA  B VAL A 1 173 ? -8.34500  -13.44800 65.77800 0.250 3.16378  ? 176 VAL A CA  1 
ATOM   1588 C  C   . VAL A 1 173 ? -7.19900  -13.93000 66.65700 1.000 8.19161  ? 176 VAL A C   1 
ATOM   1589 O  O   . VAL A 1 173 ? -7.27200  -15.00300 67.27500 1.000 9.10751  ? 176 VAL A O   1 
ATOM   1590 C  CB  A VAL A 1 173 ? -9.40700  -12.67500 66.57200 0.750 17.24269 ? 176 VAL A CB  1 
ATOM   1591 C  CB  B VAL A 1 173 ? -9.41300  -12.68700 66.59400 0.250 3.33378  ? 176 VAL A CB  1 
ATOM   1592 C  CG1 A VAL A 1 173 ? -10.23800 -13.61400 67.40100 0.750 13.69490 ? 176 VAL A CG1 1 
ATOM   1593 C  CG1 B VAL A 1 173 ? -8.79900  -12.01300 67.79500 0.250 10.71378 ? 176 VAL A CG1 1 
ATOM   1594 C  CG2 A VAL A 1 173 ? -8.75300  -11.67000 67.45400 0.750 26.42378 ? 176 VAL A CG2 1 
ATOM   1595 C  CG2 B VAL A 1 173 ? -10.13400 -11.64600 65.72100 0.250 4.15378  ? 176 VAL A CG2 1 
ATOM   1596 N  N   . GLN A 1 174 ? -6.13700  -13.13700 66.68300 1.000 7.72576  ? 177 GLN A N   1 
ATOM   1597 C  CA  . GLN A 1 174 ? -4.99000  -13.31800 67.55200 1.000 7.43362  ? 177 GLN A CA  1 
ATOM   1598 C  C   . GLN A 1 174 ? -5.11300  -12.31200 68.69100 1.000 6.93619  ? 177 GLN A C   1 
ATOM   1599 O  O   . GLN A 1 174 ? -4.94800  -11.09900 68.48400 1.000 7.24413  ? 177 GLN A O   1 
ATOM   1600 C  CB  . GLN A 1 174 ? -3.70800  -13.08100 66.75900 1.000 8.30478  ? 177 GLN A CB  1 
ATOM   1601 C  CG  . GLN A 1 174 ? -2.47900  -12.98600 67.64600 1.000 8.91011  ? 177 GLN A CG  1 
ATOM   1602 C  CD  . GLN A 1 174 ? -2.09200  -14.32200 68.24400 1.000 8.96012  ? 177 GLN A CD  1 
ATOM   1603 O  OE1 . GLN A 1 174 ? -1.69000  -15.25000 67.53000 1.000 10.52347 ? 177 GLN A OE1 1 
ATOM   1604 N  NE2 . GLN A 1 174 ? -2.21400  -14.43200 69.55200 1.000 8.10739  ? 177 GLN A NE2 1 
ATOM   1605 N  N   . LEU A 1 175 ? -5.39000  -12.81800 69.88900 1.000 6.44929  ? 178 LEU A N   1 
ATOM   1606 C  CA  . LEU A 1 175 ? -5.47000  -11.95900 71.06400 1.000 7.13095  ? 178 LEU A CA  1 
ATOM   1607 C  C   . LEU A 1 175 ? -4.07600  -11.53700 71.51300 1.000 6.78881  ? 178 LEU A C   1 
ATOM   1608 O  O   . LEU A 1 175 ? -3.14600  -12.35000 71.55200 1.000 7.49152  ? 178 LEU A O   1 
ATOM   1609 C  CB  . LEU A 1 175 ? -6.14300  -12.74300 72.18900 1.000 8.27846  ? 178 LEU A CB  1 
ATOM   1610 C  CG  . LEU A 1 175 ? -6.15500  -12.11500 73.57800 1.000 10.23396 ? 178 LEU A CG  1 
ATOM   1611 C  CD1 . LEU A 1 175 ? -6.98700  -10.84500 73.58200 1.000 11.08406 ? 178 LEU A CD1 1 
ATOM   1612 C  CD2 . LEU A 1 175 ? -6.69100  -13.12100 74.59200 1.000 10.72612 ? 178 LEU A CD2 1 
ATOM   1613 N  N   . ALA A 1 176 ? -3.95200  -10.26700 71.88900 1.000 6.98357  ? 179 ALA A N   1 
ATOM   1614 C  CA  . ALA A 1 176 ? -2.73200  -9.72300  72.48000 1.000 7.06779  ? 179 ALA A CA  1 
ATOM   1615 C  C   . ALA A 1 176 ? -3.15000  -9.04700  73.78500 1.000 6.75722  ? 179 ALA A C   1 
ATOM   1616 O  O   . ALA A 1 176 ? -3.63600  -7.90700  73.78100 1.000 6.58089  ? 179 ALA A O   1 
ATOM   1617 C  CB  . ALA A 1 176 ? -2.05200  -8.74700  71.52100 1.000 7.54416  ? 179 ALA A CB  1 
ATOM   1618 N  N   . ASP A 1 177 ? -3.00200  -9.75100  74.90000 1.000 7.17833  ? 180 ASP A N   1 
ATOM   1619 C  CA  . ASP A 1 177 ? -3.33100  -9.16000  76.19000 1.000 7.52311  ? 180 ASP A CA  1 
ATOM   1620 C  C   . ASP A 1 177 ? -2.27900  -8.12200  76.53400 1.000 7.35466  ? 180 ASP A C   1 
ATOM   1621 O  O   . ASP A 1 177 ? -1.08300  -8.37900  76.38700 1.000 7.94684  ? 180 ASP A O   1 
ATOM   1622 C  CB  . ASP A 1 177 ? -3.31500  -10.24800 77.26300 1.000 8.14160  ? 180 ASP A CB  1 
ATOM   1623 C  CG  . ASP A 1 177 ? -4.54900  -11.12900 77.22600 1.000 9.36017  ? 180 ASP A CG  1 
ATOM   1624 O  OD1 . ASP A 1 177 ? -5.66200  -10.59100 77.40500 1.000 9.99182  ? 180 ASP A OD1 1 
ATOM   1625 O  OD2 . ASP A 1 177 ? -4.41500  -12.36100 77.05900 1.000 10.29449 ? 180 ASP A OD2 1 
ATOM   1626 N  N   . HIS A 1 178 ? -2.72600  -6.95700  77.00000 1.000 7.01778  ? 181 HIS A N   1 
ATOM   1627 C  CA  . HIS A 1 178 ? -1.82300  -5.86900  77.36000 1.000 6.69406  ? 181 HIS A CA  1 
ATOM   1628 C  C   . HIS A 1 178 ? -1.90800  -5.56700  78.84700 1.000 7.02041  ? 181 HIS A C   1 
ATOM   1629 O  O   . HIS A 1 178 ? -3.00300  -5.31300  79.36900 1.000 8.24425  ? 181 HIS A O   1 
ATOM   1630 C  CB  . HIS A 1 178 ? -2.18400  -4.58600  76.61200 1.000 6.80197  ? 181 HIS A CB  1 
ATOM   1631 C  CG  . HIS A 1 178 ? -1.71500  -4.54200  75.19300 1.000 6.79144  ? 181 HIS A CG  1 
ATOM   1632 N  ND1 . HIS A 1 178 ? -2.04200  -5.49500  74.24800 1.000 6.09662  ? 181 HIS A ND1 1 
ATOM   1633 C  CD2 . HIS A 1 178 ? -0.95100  -3.62500  74.55200 1.000 6.46508  ? 181 HIS A CD2 1 
ATOM   1634 C  CE1 . HIS A 1 178 ? -1.51000  -5.14800  73.08500 1.000 6.25190  ? 181 HIS A CE1 1 
ATOM   1635 N  NE2 . HIS A 1 178 ? -0.82900  -4.02200  73.24600 1.000 6.56246  ? 181 HIS A NE2 1 
ATOM   1636 N  N   . TYR A 1 179 ? -0.75300  -5.54100  79.50800 1.000 6.77302  ? 182 TYR A N   1 
ATOM   1637 C  CA  A TYR A 1 179 ? -0.63800  -5.00200  80.85200 0.760 8.01790  ? 182 TYR A CA  1 
ATOM   1638 C  CA  B TYR A 1 179 ? -0.61500  -5.02000  80.86200 0.240 5.96378  ? 182 TYR A CA  1 
ATOM   1639 C  C   . TYR A 1 179 ? 0.37700   -3.87100  80.80700 1.000 7.37309  ? 182 TYR A C   1 
ATOM   1640 O  O   . TYR A 1 179 ? 1.44500   -4.00900  80.20900 1.000 8.15739  ? 182 TYR A O   1 
ATOM   1641 C  CB  A TYR A 1 179 ? -0.22900  -6.08100  81.85700 0.760 10.37082 ? 182 TYR A CB  1 
ATOM   1642 C  CB  B TYR A 1 179 ? -0.08500  -6.09100  81.81700 0.240 9.37378  ? 182 TYR A CB  1 
ATOM   1643 C  CG  A TYR A 1 179 ? -0.16900  -5.55900  83.28000 0.760 12.41053 ? 182 TYR A CG  1 
ATOM   1644 C  CG  B TYR A 1 179 ? 0.39100   -5.50800  83.13000 0.240 11.72378 ? 182 TYR A CG  1 
ATOM   1645 C  CD1 A TYR A 1 179 ? -1.28200  -4.97500  83.87500 0.760 13.90808 ? 182 TYR A CD1 1 
ATOM   1646 C  CD1 B TYR A 1 179 ? -0.50500  -5.20100  84.14000 0.240 11.05378 ? 182 TYR A CD1 1 
ATOM   1647 C  CD2 A TYR A 1 179 ? 1.00200   -5.62800  84.01100 0.760 16.88475 ? 182 TYR A CD2 1 
ATOM   1648 C  CD2 B TYR A 1 179 ? 1.73800   -5.23600  83.34500 0.240 12.74378 ? 182 TYR A CD2 1 
ATOM   1649 C  CE1 A TYR A 1 179 ? -1.22700  -4.48000  85.18100 0.760 15.72146 ? 182 TYR A CE1 1 
ATOM   1650 C  CE1 B TYR A 1 179 ? -0.07200  -4.65200  85.33800 0.240 10.61378 ? 182 TYR A CE1 1 
ATOM   1651 C  CE2 A TYR A 1 179 ? 1.06400   -5.13900  85.31100 0.760 21.38378 ? 182 TYR A CE2 1 
ATOM   1652 C  CE2 B TYR A 1 179 ? 2.17800   -4.68500  84.53000 0.240 13.91378 ? 182 TYR A CE2 1 
ATOM   1653 C  CZ  A TYR A 1 179 ? -0.04900  -4.56500  85.88500 0.760 17.76118 ? 182 TYR A CZ  1 
ATOM   1654 C  CZ  B TYR A 1 179 ? 1.26800   -4.39700  85.52200 0.240 11.22378 ? 182 TYR A CZ  1 
ATOM   1655 O  OH  A TYR A 1 179 ? 0.01500   -4.07800  87.17600 0.760 17.59010 ? 182 TYR A OH  1 
ATOM   1656 O  OH  B TYR A 1 179 ? 1.70400   -3.85400  86.71000 0.240 23.28378 ? 182 TYR A OH  1 
ATOM   1657 N  N   . GLN A 1 180 ? 0.04000   -2.75700  81.42700 1.000 7.29676  ? 183 GLN A N   1 
ATOM   1658 C  CA  . GLN A 1 180 ? 0.78000   -1.51800  81.23600 1.000 7.42046  ? 183 GLN A CA  1 
ATOM   1659 C  C   . GLN A 1 180 ? 0.97600   -0.80500  82.56600 1.000 6.85987  ? 183 GLN A C   1 
ATOM   1660 O  O   . GLN A 1 180 ? 0.07600   -0.80200  83.41200 1.000 7.90473  ? 183 GLN A O   1 
ATOM   1661 C  CB  . GLN A 1 180 ? -0.03400  -0.61700  80.30400 1.000 7.34677  ? 183 GLN A CB  1 
ATOM   1662 C  CG  . GLN A 1 180 ? 0.52400   0.77800   80.08500 1.000 7.48363  ? 183 GLN A CG  1 
ATOM   1663 C  CD  . GLN A 1 180 ? -0.33400  1.60500   79.14300 1.000 7.39151  ? 183 GLN A CD  1 
ATOM   1664 O  OE1 . GLN A 1 180 ? -1.07400  1.06500   78.33100 1.000 6.60194  ? 183 GLN A OE1 1 
ATOM   1665 N  NE2 . GLN A 1 180 ? -0.22100  2.93100   79.23800 1.000 6.90461  ? 183 GLN A NE2 1 
ATOM   1666 N  N   . GLN A 1 181 ? 2.16100   -0.19900  82.74300 1.000 7.17306  ? 184 GLN A N   1 
ATOM   1667 C  CA  A GLN A 1 181 ? 2.46700   0.61400   83.91800 0.720 9.47597  ? 184 GLN A CA  1 
ATOM   1668 C  CA  B GLN A 1 181 ? 2.42700   0.63300   83.90600 0.280 7.93378  ? 184 GLN A CA  1 
ATOM   1669 C  C   . GLN A 1 181 ? 3.18400   1.87500   83.46700 1.000 8.77589  ? 184 GLN A C   1 
ATOM   1670 O  O   . GLN A 1 181 ? 4.11400   1.79800   82.66200 1.000 9.68126  ? 184 GLN A O   1 
ATOM   1671 C  CB  A GLN A 1 181 ? 3.36600   -0.15600  84.89800 0.720 12.32631 ? 184 GLN A CB  1 
ATOM   1672 C  CB  B GLN A 1 181 ? 3.19600   -0.11800  85.00700 0.280 8.07378  ? 184 GLN A CB  1 
ATOM   1673 C  CG  A GLN A 1 181 ? 2.73000   -1.43600  85.43400 0.720 15.81094 ? 184 GLN A CG  1 
ATOM   1674 C  CG  B GLN A 1 181 ? 4.52900   -0.71600  84.59900 0.280 17.92378 ? 184 GLN A CG  1 
ATOM   1675 C  CD  A GLN A 1 181 ? 3.76100   -2.40700  85.99200 0.720 22.18378 ? 184 GLN A CD  1 
ATOM   1676 C  CD  B GLN A 1 181 ? 5.15300   -1.52600  85.72600 0.280 30.50378 ? 184 GLN A CD  1 
ATOM   1677 O  OE1 A GLN A 1 181 ? 3.88000   -2.57400  87.20500 0.720 30.04378 ? 184 GLN A OE1 1 
ATOM   1678 O  OE1 B GLN A 1 181 ? 4.44200   -2.11000  86.54600 0.280 14.86378 ? 184 GLN A OE1 1 
ATOM   1679 N  NE2 A GLN A 1 181 ? 4.50900   -3.05100  85.10200 0.720 24.89378 ? 184 GLN A NE2 1 
ATOM   1680 N  NE2 B GLN A 1 181 ? 6.48300   -1.55400  85.77800 0.280 15.79378 ? 184 GLN A NE2 1 
ATOM   1681 N  N   . ASN A 1 182 ? 2.76100   3.02000   83.98000 1.000 8.64166  ? 185 ASN A N   1 
ATOM   1682 C  CA  . ASN A 1 182 ? 3.37700   4.29800   83.66200 1.000 7.97316  ? 185 ASN A CA  1 
ATOM   1683 C  C   . ASN A 1 182 ? 3.83400   4.96900   84.94800 1.000 8.49954  ? 185 ASN A C   1 
ATOM   1684 O  O   . ASN A 1 182 ? 3.09400   4.99600   85.94600 1.000 9.30753  ? 185 ASN A O   1 
ATOM   1685 C  CB  . ASN A 1 182 ? 2.41100   5.25000   82.93600 1.000 7.97053  ? 185 ASN A CB  1 
ATOM   1686 C  CG  . ASN A 1 182 ? 2.05800   4.77500   81.54200 1.000 8.05475  ? 185 ASN A CG  1 
ATOM   1687 O  OD1 . ASN A 1 182 ? 1.63000   3.65200   81.35500 1.000 11.43410 ? 185 ASN A OD1 1 
ATOM   1688 N  ND2 . ASN A 1 182 ? 2.21100   5.64500   80.56300 1.000 7.74155  ? 185 ASN A ND2 1 
ATOM   1689 N  N   . THR A 1 183 ? 5.03300   5.56200   84.90200 1.000 8.91538  ? 186 THR A N   1 
ATOM   1690 C  CA  A THR A 1 183 ? 5.65200   6.22800   86.04900 0.710 9.96024  ? 186 THR A CA  1 
ATOM   1691 C  CA  B THR A 1 183 ? 5.58600   6.26400   86.05000 0.290 13.83378 ? 186 THR A CA  1 
ATOM   1692 C  C   . THR A 1 183 ? 6.19700   7.57200   85.57700 1.000 10.31555 ? 186 THR A C   1 
ATOM   1693 O  O   . THR A 1 183 ? 6.90000   7.61300   84.55600 1.000 11.09196 ? 186 THR A O   1 
ATOM   1694 C  CB  A THR A 1 183 ? 6.82000   5.35500   86.56300 0.710 10.48925 ? 186 THR A CB  1 
ATOM   1695 C  CB  B THR A 1 183 ? 6.65300   5.47200   86.82000 0.290 21.53378 ? 186 THR A CB  1 
ATOM   1696 O  OG1 A THR A 1 183 ? 6.39900   3.99200   86.66100 0.710 11.30251 ? 186 THR A OG1 1 
ATOM   1697 O  OG1 B THR A 1 183 ? 7.65800   5.00900   85.91800 0.290 13.45378 ? 186 THR A OG1 1 
ATOM   1698 C  CG2 A THR A 1 183 ? 7.26900   5.82700   87.93600 0.710 11.57359 ? 186 THR A CG2 1 
ATOM   1699 C  CG2 B THR A 1 183 ? 6.04000   4.30000   87.53300 0.290 23.74378 ? 186 THR A CG2 1 
ATOM   1700 N  N   . PRO A 1 184 ? 5.94400   8.66800   86.29400 1.000 9.43649  ? 187 PRO A N   1 
ATOM   1701 C  CA  . PRO A 1 184 ? 6.48400   9.95700   85.85400 1.000 9.56809  ? 187 PRO A CA  1 
ATOM   1702 C  C   . PRO A 1 184 ? 7.99400   10.01700  86.01300 1.000 9.81285  ? 187 PRO A C   1 
ATOM   1703 O  O   . PRO A 1 184 ? 8.56800   9.43300   86.92700 1.000 10.98405 ? 187 PRO A O   1 
ATOM   1704 C  CB  . PRO A 1 184 ? 5.80700   10.96400  86.78600 1.000 11.03669 ? 187 PRO A CB  1 
ATOM   1705 C  CG  . PRO A 1 184 ? 5.50500   10.20100  88.00800 1.000 12.26578 ? 187 PRO A CG  1 
ATOM   1706 C  CD  . PRO A 1 184 ? 5.18200   8.80500   87.54800 1.000 10.91035 ? 187 PRO A CD  1 
ATOM   1707 N  N   . ILE A 1 185 ? 8.63000   10.76500  85.11800 1.000 9.82865  ? 188 ILE A N   1 
ATOM   1708 C  CA  . ILE A 1 185 ? 10.07500  10.96400  85.16300 1.000 10.42609 ? 188 ILE A CA  1 
ATOM   1709 C  C   . ILE A 1 185 ? 10.45600  12.17400  86.00200 1.000 10.67612 ? 188 ILE A C   1 
ATOM   1710 O  O   . ILE A 1 185 ? 11.46700  12.13800  86.71300 1.000 12.43685 ? 188 ILE A O   1 
ATOM   1711 C  CB  . ILE A 1 185 ? 10.61800  11.07900  83.72500 1.000 10.24712 ? 188 ILE A CB  1 
ATOM   1712 C  CG1 . ILE A 1 185 ? 10.45900  9.75200   82.98500 1.000 10.31555 ? 188 ILE A CG1 1 
ATOM   1713 C  CG2 . ILE A 1 185 ? 12.09400  11.57200  83.71600 1.000 11.28672 ? 188 ILE A CG2 1 
ATOM   1714 C  CD1 . ILE A 1 185 ? 10.70700  9.87400   81.47700 1.000 10.03130 ? 188 ILE A CD1 1 
ATOM   1715 N  N   . GLY A 1 186 ? 9.67700   13.25400  85.91400 1.000 11.02879 ? 189 GLY A N   1 
ATOM   1716 C  CA  . GLY A 1 186 ? 10.00500  14.49700  86.57200 1.000 11.59991 ? 189 GLY A CA  1 
ATOM   1717 C  C   . GLY A 1 186 ? 9.43200   14.61900  87.96700 1.000 10.84719 ? 189 GLY A C   1 
ATOM   1718 O  O   . GLY A 1 186 ? 8.83600   13.68800  88.51800 1.000 11.53148 ? 189 GLY A O   1 
ATOM   1719 N  N   A ASP A 1 187 ? 9.60600   15.81400  88.53300 0.730 12.49739 ? 190 ASP A N   1 
ATOM   1720 N  N   B ASP A 1 187 ? 9.60700   15.82000  88.52900 0.270 8.87378  ? 190 ASP A N   1 
ATOM   1721 C  CA  A ASP A 1 187 ? 9.25200   16.09200  89.91800 0.730 14.57658 ? 190 ASP A CA  1 
ATOM   1722 C  CA  B ASP A 1 187 ? 9.28400   16.14000  89.91400 0.270 13.39378 ? 190 ASP A CA  1 
ATOM   1723 C  C   A ASP A 1 187 ? 8.03300   16.99000  90.06200 0.730 14.25549 ? 190 ASP A C   1 
ATOM   1724 C  C   B ASP A 1 187 ? 8.08500   17.06700  90.05000 0.270 6.55378  ? 190 ASP A C   1 
ATOM   1725 O  O   A ASP A 1 187 ? 7.73400   17.42400  91.17500 0.730 15.47932 ? 190 ASP A O   1 
ATOM   1726 O  O   B ASP A 1 187 ? 7.84700   17.59200  91.14100 0.270 10.86378 ? 190 ASP A O   1 
ATOM   1727 C  CB  A ASP A 1 187 ? 10.44500  16.69200  90.68100 0.730 17.43482 ? 190 ASP A CB  1 
ATOM   1728 C  CB  B ASP A 1 187 ? 10.48700  16.78800  90.60700 0.270 9.10378  ? 190 ASP A CB  1 
ATOM   1729 C  CG  A ASP A 1 187 ? 10.78600  18.12400  90.24200 0.730 20.00618 ? 190 ASP A CG  1 
ATOM   1730 C  CG  B ASP A 1 187 ? 11.73000  15.94200  90.52600 0.270 17.23378 ? 190 ASP A CG  1 
ATOM   1731 O  OD1 A ASP A 1 187 ? 10.17600  18.64700  89.28800 0.730 23.71378 ? 190 ASP A OD1 1 
ATOM   1732 O  OD1 B ASP A 1 187 ? 11.60200  14.70500  90.59100 0.270 13.47378 ? 190 ASP A OD1 1 
ATOM   1733 O  OD2 A ASP A 1 187 ? 11.68900  18.73400  90.85500 0.730 21.20378 ? 190 ASP A OD2 1 
ATOM   1734 O  OD2 B ASP A 1 187 ? 12.83600  16.50800  90.40000 0.270 42.56378 ? 190 ASP A OD2 1 
ATOM   1735 N  N   . GLY A 1 188 ? 7.34900   17.31000  88.97900 1.000 12.24472 ? 191 GLY A N   1 
ATOM   1736 C  CA  . GLY A 1 188 ? 6.14100   18.08700  89.08700 1.000 12.83953 ? 191 GLY A CA  1 
ATOM   1737 C  C   . GLY A 1 188 ? 5.00800   17.23100  89.59300 1.000 13.00797 ? 191 GLY A C   1 
ATOM   1738 O  O   . GLY A 1 188 ? 5.06300   15.99500  89.59300 1.000 13.83439 ? 191 GLY A O   1 
ATOM   1739 N  N   . PRO A 1 189 ? 3.94700   17.87800  90.04900 1.000 14.07916 ? 192 PRO A N   1 
ATOM   1740 C  CA  . PRO A 1 189 ? 2.77600   17.11600  90.48600 1.000 13.85281 ? 192 PRO A CA  1 
ATOM   1741 C  C   . PRO A 1 189 ? 2.15300   16.43100  89.28400 1.000 12.62898 ? 192 PRO A C   1 
ATOM   1742 O  O   . PRO A 1 189 ? 2.10600   16.99100  88.18400 1.000 14.24760 ? 192 PRO A O   1 
ATOM   1743 C  CB  . PRO A 1 189 ? 1.85300   18.19200  91.06600 1.000 15.97938 ? 192 PRO A CB  1 
ATOM   1744 C  CG  . PRO A 1 189 ? 2.22700   19.42100  90.32000 1.000 16.07676 ? 192 PRO A CG  1 
ATOM   1745 C  CD  . PRO A 1 189 ? 3.73000   19.33000  90.12500 1.000 15.25035 ? 192 PRO A CD  1 
ATOM   1746 N  N   . VAL A 1 190 ? 1.71500   15.19600  89.48400 1.000 12.01049 ? 193 VAL A N   1 
ATOM   1747 C  CA  . VAL A 1 190 ? 1.00400   14.47800  88.44000 1.000 11.65255 ? 193 VAL A CA  1 
ATOM   1748 C  C   . VAL A 1 190 ? -0.36100  14.07500  88.96300 1.000 11.17354 ? 193 VAL A C   1 
ATOM   1749 O  O   . VAL A 1 190 ? -0.59200  13.96200  90.16700 1.000 12.86322 ? 193 VAL A O   1 
ATOM   1750 C  CB  . VAL A 1 190 ? 1.76600   13.26300  87.86300 1.000 13.40276 ? 193 VAL A CB  1 
ATOM   1751 C  CG1 . VAL A 1 190 ? 3.11800   13.69600  87.31300 1.000 13.62647 ? 193 VAL A CG1 1 
ATOM   1752 C  CG2 . VAL A 1 190 ? 1.91400   12.15000  88.89300 1.000 14.90031 ? 193 VAL A CG2 1 
ATOM   1753 N  N   . LEU A 1 191 ? -1.27300  13.86400  88.02500 1.000 10.47083 ? 194 LEU A N   1 
ATOM   1754 C  CA  . LEU A 1 191 ? -2.65500  13.52800  88.33500 1.000 10.44451 ? 194 LEU A CA  1 
ATOM   1755 C  C   . LEU A 1 191 ? -2.81000  12.02600  88.47800 1.000 10.57610 ? 194 LEU A C   1 
ATOM   1756 O  O   . LEU A 1 191 ? -2.38300  11.26000  87.60800 1.000 12.00522 ? 194 LEU A O   1 
ATOM   1757 C  CB  . LEU A 1 191 ? -3.59400  14.05200  87.25200 1.000 10.28133 ? 194 LEU A CB  1 
ATOM   1758 C  CG  . LEU A 1 191 ? -3.56700  15.58100  87.13700 1.000 10.69191 ? 194 LEU A CG  1 
ATOM   1759 C  CD1 . LEU A 1 191 ? -4.38000  16.05200  85.94000 1.000 11.63149 ? 194 LEU A CD1 1 
ATOM   1760 C  CD2 . LEU A 1 191 ? -4.06400  16.23000  88.43900 1.000 11.94206 ? 194 LEU A CD2 1 
ATOM   1761 N  N   . LEU A 1 192 ? -3.41800  11.61700  89.57800 1.000 11.02353 ? 195 LEU A N   1 
ATOM   1762 C  CA  . LEU A 1 192 ? -3.68100  10.21300  89.84800 1.000 12.38685 ? 195 LEU A CA  1 
ATOM   1763 C  C   . LEU A 1 192 ? -5.17200  9.98800   89.62600 1.000 12.40527 ? 195 LEU A C   1 
ATOM   1764 O  O   . LEU A 1 192 ? -5.99900  10.48000  90.41300 1.000 14.58711 ? 195 LEU A O   1 
ATOM   1765 C  CB  . LEU A 1 192 ? -3.25400  9.85600   91.27600 1.000 14.77398 ? 195 LEU A CB  1 
ATOM   1766 C  CG  . LEU A 1 192 ? -1.76100  10.11100  91.55700 1.000 16.72421 ? 195 LEU A CG  1 
ATOM   1767 C  CD1 . LEU A 1 192 ? -1.40800  9.73600   93.00500 1.000 17.48746 ? 195 LEU A CD1 1 
ATOM   1768 C  CD2 . LEU A 1 192 ? -0.83500  9.39600   90.53500 1.000 16.97687 ? 195 LEU A CD2 1 
ATOM   1769 N  N   . PRO A 1 193 ? -5.56200  9.30300   88.55500 1.000 10.57874 ? 196 PRO A N   1 
ATOM   1770 C  CA  . PRO A 1 193 ? -6.95400  9.35100   88.09200 1.000 10.60242 ? 196 PRO A CA  1 
ATOM   1771 C  C   . PRO A 1 193 ? -7.86900  8.37400   88.80400 1.000 9.65231  ? 196 PRO A C   1 
ATOM   1772 O  O   . PRO A 1 193 ? -7.44100  7.33600   89.31200 1.000 10.89719 ? 196 PRO A O   1 
ATOM   1773 C  CB  . PRO A 1 193 ? -6.82800  8.93100   86.62200 1.000 10.40240 ? 196 PRO A CB  1 
ATOM   1774 C  CG  . PRO A 1 193 ? -5.67300  7.96300   86.63900 1.000 10.91035 ? 196 PRO A CG  1 
ATOM   1775 C  CD  . PRO A 1 193 ? -4.68800  8.58100   87.62300 1.000 10.59716 ? 196 PRO A CD  1 
ATOM   1776 N  N   . ASP A 1 194 ? -9.15500  8.71700   88.81700 1.000 10.05762 ? 197 ASP A N   1 
ATOM   1777 C  CA  . ASP A 1 194 ? -10.16700 7.69700   89.04900 1.000 10.81034 ? 197 ASP A CA  1 
ATOM   1778 C  C   . ASP A 1 194 ? -10.19600 6.73800   87.86000 1.000 9.98919  ? 197 ASP A C   1 
ATOM   1779 O  O   . ASP A 1 194 ? -9.73100  7.04700   86.76400 1.000 10.29975 ? 197 ASP A O   1 
ATOM   1780 C  CB  . ASP A 1 194 ? -11.56000 8.32400   89.19700 1.000 11.59728 ? 197 ASP A CB  1 
ATOM   1781 C  CG  . ASP A 1 194 ? -11.72800 9.09700   90.48400 1.000 15.42932 ? 197 ASP A CG  1 
ATOM   1782 O  OD1 . ASP A 1 194 ? -10.88000 8.96400   91.38100 1.000 18.12438 ? 197 ASP A OD1 1 
ATOM   1783 O  OD2 . ASP A 1 194 ? -12.72000 9.84600   90.59800 1.000 16.12940 ? 197 ASP A OD2 1 
ATOM   1784 N  N   . ASN A 1 195 ? -10.74000 5.54900   88.09400 1.000 9.63125  ? 198 ASN A N   1 
ATOM   1785 C  CA  . ASN A 1 195 ? -10.88000 4.56500   87.02500 1.000 10.26817 ? 198 ASN A CA  1 
ATOM   1786 C  C   . ASN A 1 195 ? -11.62700 5.16700   85.84500 1.000 9.84970  ? 198 ASN A C   1 
ATOM   1787 O  O   . ASN A 1 195 ? -12.65500 5.83200   86.00200 1.000 11.13670 ? 198 ASN A O   1 
ATOM   1788 C  CB  . ASN A 1 195 ? -11.68100 3.36600   87.53100 1.000 11.51306 ? 198 ASN A CB  1 
ATOM   1789 C  CG  . ASN A 1 195 ? -10.93300 2.54700   88.56300 1.000 13.26064 ? 198 ASN A CG  1 
ATOM   1790 O  OD1 . ASN A 1 195 ? -9.81700  2.87400   88.96200 1.000 13.49224 ? 198 ASN A OD1 1 
ATOM   1791 N  ND2 . ASN A 1 195 ? -11.56100 1.46800   89.01200 1.000 17.20848 ? 198 ASN A ND2 1 
ATOM   1792 N  N   . HIS A 1 196 ? -11.11100 4.91800   84.65400 1.000 9.44176  ? 199 HIS A N   1 
ATOM   1793 C  CA  . HIS A 1 196 ? -11.76400 5.37000   83.43900 1.000 8.78905  ? 199 HIS A CA  1 
ATOM   1794 C  C   . HIS A 1 196 ? -11.14600 4.58000   82.30200 1.000 8.37584  ? 199 HIS A C   1 
ATOM   1795 O  O   . HIS A 1 196 ? -10.28500 3.72700   82.52200 1.000 9.61283  ? 199 HIS A O   1 
ATOM   1796 C  CB  . HIS A 1 196 ? -11.59700 6.87400   83.25300 1.000 8.97591  ? 199 HIS A CB  1 
ATOM   1797 C  CG  . HIS A 1 196 ? -10.18400 7.29800   83.00100 1.000 8.88116  ? 199 HIS A CG  1 
ATOM   1798 N  ND1 . HIS A 1 196 ? -9.24000  7.40700   84.00300 1.000 8.58902  ? 199 HIS A ND1 1 
ATOM   1799 C  CD2 . HIS A 1 196 ? -9.56100  7.64900   81.85100 1.000 8.31531  ? 199 HIS A CD2 1 
ATOM   1800 C  CE1 . HIS A 1 196 ? -8.09300  7.81200   83.47200 1.000 7.92579  ? 199 HIS A CE1 1 
ATOM   1801 N  NE2 . HIS A 1 196 ? -8.26000  7.95900   82.16900 1.000 8.03369  ? 199 HIS A NE2 1 
ATOM   1802 N  N   . TYR A 1 197 ? -11.58000 4.85900   81.07900 1.000 9.22594  ? 200 TYR A N   1 
ATOM   1803 C  CA  . TYR A 1 197 ? -10.98500 4.17600   79.94700 1.000 9.66020  ? 200 TYR A CA  1 
ATOM   1804 C  C   . TYR A 1 197 ? -10.73500 5.15800   78.81400 1.000 8.85484  ? 200 TYR A C   1 
ATOM   1805 O  O   . TYR A 1 197 ? -11.27400 6.27300   78.77700 1.000 9.20752  ? 200 TYR A O   1 
ATOM   1806 C  CB  . TYR A 1 197 ? -11.79900 2.95000   79.49900 1.000 10.15237 ? 200 TYR A CB  1 
ATOM   1807 C  CG  . TYR A 1 197 ? -13.19200 3.26400   79.01400 1.000 10.78402 ? 200 TYR A CG  1 
ATOM   1808 C  CD1 . TYR A 1 197 ? -14.26700 3.36700   79.90200 1.000 11.97627 ? 200 TYR A CD1 1 
ATOM   1809 C  CD2 . TYR A 1 197 ? -13.44400 3.44300   77.66200 1.000 11.37620 ? 200 TYR A CD2 1 
ATOM   1810 C  CE1 . TYR A 1 197 ? -15.54200 3.66200   79.44100 1.000 13.37644 ? 200 TYR A CE1 1 
ATOM   1811 C  CE2 . TYR A 1 197 ? -14.70800 3.73700   77.19400 1.000 12.38158 ? 200 TYR A CE2 1 
ATOM   1812 C  CZ  . TYR A 1 197 ? -15.75600 3.84400   78.09000 1.000 13.68437 ? 200 TYR A CZ  1 
ATOM   1813 O  OH  . TYR A 1 197 ? -17.02500 4.13700   77.62000 1.000 15.88990 ? 200 TYR A OH  1 
ATOM   1814 N  N   . LEU A 1 198 ? -9.88900  4.72100   77.88700 1.000 8.16266  ? 201 LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 198 ? -9.68500  5.41700   76.62500 1.000 8.22582  ? 201 LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 198 ? -10.35700 4.61000   75.52300 1.000 8.31004  ? 201 LEU A C   1 
ATOM   1817 O  O   . LEU A 1 198 ? -10.12900 3.40500   75.40700 1.000 8.79168  ? 201 LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 198 ? -8.19300  5.55000   76.30200 1.000 8.58113  ? 201 LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 198 ? -7.34900  6.19700   77.40400 1.000 9.14435  ? 201 LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 198 ? -5.87600  6.24300   76.99400 1.000 8.69430  ? 201 LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 198 ? -7.85900  7.59600   77.75700 1.000 8.34163  ? 201 LEU A CD2 1 
ATOM   1822 N  N   . SER A 1 199 ? -11.17800 5.27300   74.72400 1.000 8.00211  ? 202 SER A N   1 
ATOM   1823 C  CA  . SER A 1 199 ? -11.87400 4.64000   73.61000 1.000 8.35215  ? 202 SER A CA  1 
ATOM   1824 C  C   . SER A 1 199 ? -11.07200 4.95500   72.35600 1.000 8.80221  ? 202 SER A C   1 
ATOM   1825 O  O   . SER A 1 199 ? -10.95800 6.12400   71.97900 1.000 9.19962  ? 202 SER A O   1 
ATOM   1826 C  CB  . SER A 1 199 ? -13.27300 5.23500   73.52600 1.000 9.99446  ? 202 SER A CB  1 
ATOM   1827 O  OG  . SER A 1 199 ? -13.98500 4.77100   72.41400 1.000 12.26578 ? 202 SER A OG  1 
ATOM   1828 N  N   . VAL A 1 200 ? -10.49300 3.92300   71.73300 1.000 7.86788  ? 203 VAL A N   1 
ATOM   1829 C  CA  . VAL A 1 200 ? -9.52500  4.10500   70.66100 1.000 7.74419  ? 203 VAL A CA  1 
ATOM   1830 C  C   . VAL A 1 200 ? -10.04200 3.50700   69.36900 1.000 8.09160  ? 203 VAL A C   1 
ATOM   1831 O  O   . VAL A 1 200 ? -10.53200 2.37200   69.34900 1.000 8.86537  ? 203 VAL A O   1 
ATOM   1832 C  CB  . VAL A 1 200 ? -8.18000  3.42700   71.00400 1.000 8.01001  ? 203 VAL A CB  1 
ATOM   1833 C  CG1 . VAL A 1 200 ? -7.13700  3.77700   69.94700 1.000 9.44702  ? 203 VAL A CG1 1 
ATOM   1834 C  CG2 . VAL A 1 200 ? -7.69600  3.78700   72.42400 1.000 7.74155  ? 203 VAL A CG2 1 
ATOM   1835 N  N   . GLN A 1 201 ? -9.87400  4.24900   68.28300 1.000 7.90999  ? 204 GLN A N   1 
ATOM   1836 C  CA  . GLN A 1 201 ? -10.02600 3.68200   66.94800 1.000 9.15751  ? 204 GLN A CA  1 
ATOM   1837 C  C   . GLN A 1 201 ? -8.77700  4.00100   66.14000 1.000 8.24688  ? 204 GLN A C   1 
ATOM   1838 O  O   . GLN A 1 201 ? -8.22300  5.10100   66.25100 1.000 8.75483  ? 204 GLN A O   1 
ATOM   1839 C  CB  . GLN A 1 201 ? -11.25900 4.16900   66.22500 1.000 11.06564 ? 204 GLN A CB  1 
ATOM   1840 C  CG  . GLN A 1 201 ? -11.26700 5.63400   65.95600 1.000 13.66332 ? 204 GLN A CG  1 
ATOM   1841 C  CD  . GLN A 1 201 ? -12.62400 6.09400   65.48600 1.000 17.93225 ? 204 GLN A CD  1 
ATOM   1842 O  OE1 . GLN A 1 201 ? -12.95100 5.98700   64.30400 1.000 20.51414 ? 204 GLN A OE1 1 
ATOM   1843 N  NE2 . GLN A 1 201 ? -13.44400 6.57700   66.42000 1.000 18.44020 ? 204 GLN A NE2 1 
ATOM   1844 N  N   . SER A 1 202 ? -8.33500  3.03400   65.33800 1.000 8.59955  ? 205 SER A N   1 
ATOM   1845 C  CA  . SER A 1 202 ? -7.07500  3.13900   64.62100 1.000 8.84169  ? 205 SER A CA  1 
ATOM   1846 C  C   . SER A 1 202 ? -7.27200  2.63000   63.20600 1.000 8.77326  ? 205 SER A C   1 
ATOM   1847 O  O   . SER A 1 202 ? -7.85700  1.56200   63.00000 1.000 11.03142 ? 205 SER A O   1 
ATOM   1848 C  CB  . SER A 1 202 ? -5.99800  2.27600   65.29600 1.000 8.61534  ? 205 SER A CB  1 
ATOM   1849 O  OG  . SER A 1 202 ? -5.94300  2.49200   66.70400 1.000 8.28109  ? 205 SER A OG  1 
ATOM   1850 N  N   . ALA A 1 203 ? -6.70900  3.35000   62.24400 1.000 8.21793  ? 206 ALA A N   1 
ATOM   1851 C  CA  . ALA A 1 203 ? -6.78000  2.96500   60.84300 1.000 8.85221  ? 206 ALA A CA  1 
ATOM   1852 C  C   . ALA A 1 203 ? -5.36900  2.89800   60.27800 1.000 7.90473  ? 206 ALA A C   1 
ATOM   1853 O  O   . ALA A 1 203 ? -4.59100  3.85500   60.42000 1.000 8.32847  ? 206 ALA A O   1 
ATOM   1854 C  CB  . ALA A 1 203 ? -7.61000  3.97500   60.04500 1.000 10.21027 ? 206 ALA A CB  1 
ATOM   1855 N  N   . LEU A 1 204 ? -5.04700  1.78200   59.62300 1.000 7.84946  ? 207 LEU A N   1 
ATOM   1856 C  CA  . LEU A 1 204 ? -3.72500  1.57100   59.05100 1.000 7.69944  ? 207 LEU A CA  1 
ATOM   1857 C  C   . LEU A 1 204 ? -3.81200  1.71900   57.54200 1.000 8.09949  ? 207 LEU A C   1 
ATOM   1858 O  O   . LEU A 1 204 ? -4.77800  1.27500   56.92100 1.000 9.72863  ? 207 LEU A O   1 
ATOM   1859 C  CB  . LEU A 1 204 ? -3.18800  0.17400   59.35900 1.000 7.61522  ? 207 LEU A CB  1 
ATOM   1860 C  CG  . LEU A 1 204 ? -3.35000  -0.29900  60.80100 1.000 8.58902  ? 207 LEU A CG  1 
ATOM   1861 C  CD1 . LEU A 1 204 ? -2.58100  -1.59100  60.97200 1.000 8.94696  ? 207 LEU A CD1 1 
ATOM   1862 C  CD2 . LEU A 1 204 ? -2.83800  0.72700   61.78200 1.000 8.06528  ? 207 LEU A CD2 1 
ATOM   1863 N  N   . SER A 1 205 ? -2.78800  2.32000   56.94900 1.000 8.28109  ? 208 SER A N   1 
ATOM   1864 C  CA  . SER A 1 205 ? -2.75700  2.49300   55.50900 1.000 8.91011  ? 208 SER A CA  1 
ATOM   1865 C  C   . SER A 1 205 ? -1.31100  2.45700   55.03500 1.000 8.88906  ? 208 SER A C   1 
ATOM   1866 O  O   . SER A 1 205 ? -0.36700  2.36800   55.82600 1.000 9.04960  ? 208 SER A O   1 
ATOM   1867 C  CB  . SER A 1 205 ? -3.46400  3.79200   55.12500 1.000 9.62862  ? 208 SER A CB  1 
ATOM   1868 O  OG  . SER A 1 205 ? -2.80800  4.90400   55.72500 1.000 9.81812  ? 208 SER A OG  1 
ATOM   1869 N  N   . LYS A 1 206 ? -1.14600  2.52000   53.71900 1.000 10.09184 ? 209 LYS A N   1 
ATOM   1870 C  CA  . LYS A 1 206 ? 0.15900   2.54800   53.08600 1.000 12.21314 ? 209 LYS A CA  1 
ATOM   1871 C  C   . LYS A 1 206 ? 0.27300   3.81800   52.26400 1.000 13.21326 ? 209 LYS A C   1 
ATOM   1872 O  O   . LYS A 1 206 ? -0.71500  4.30900   51.70500 1.000 15.38458 ? 209 LYS A O   1 
ATOM   1873 C  CB  . LYS A 1 206 ? 0.35900   1.34900   52.15400 1.000 13.16852 ? 209 LYS A CB  1 
ATOM   1874 C  CG  . LYS A 1 206 ? 0.31400   -0.01100  52.84000 1.000 12.68425 ? 209 LYS A CG  1 
ATOM   1875 C  CD  . LYS A 1 206 ? 1.51300   -0.21100  53.76200 1.000 11.60781 ? 209 LYS A CD  1 
ATOM   1876 C  CE  . LYS A 1 206 ? 1.57400   -1.66400  54.24100 1.000 11.05774 ? 209 LYS A CE  1 
ATOM   1877 N  NZ  . LYS A 1 206 ? 2.69400   -1.89200  55.20700 1.000 10.19974 ? 209 LYS A NZ  1 
ATOM   1878 N  N   . ASP A 1 207 ? 1.49000   4.34500   52.23200 1.000 13.97914 ? 210 ASP A N   1 
ATOM   1879 C  CA  . ASP A 1 207 ? 1.85400   5.47200   51.39500 1.000 16.41891 ? 210 ASP A CA  1 
ATOM   1880 C  C   . ASP A 1 207 ? 2.16900   4.87600   50.02800 1.000 17.44272 ? 210 ASP A C   1 
ATOM   1881 O  O   . ASP A 1 207 ? 3.13200   4.10400   49.90800 1.000 15.46880 ? 210 ASP A O   1 
ATOM   1882 C  CB  . ASP A 1 207 ? 3.08300   6.13100   52.00700 1.000 17.55852 ? 210 ASP A CB  1 
ATOM   1883 C  CG  . ASP A 1 207 ? 3.60100   7.30900   51.22500 1.000 18.86394 ? 210 ASP A CG  1 
ATOM   1884 O  OD1 . ASP A 1 207 ? 3.20400   7.52500   50.06300 1.000 18.33493 ? 210 ASP A OD1 1 
ATOM   1885 O  OD2 . ASP A 1 207 ? 4.45500   8.01400   51.80600 1.000 19.29820 ? 210 ASP A OD2 1 
ATOM   1886 N  N   . PRO A 1 208 ? 1.37300   5.15500   48.99600 1.000 22.72756 ? 211 PRO A N   1 
ATOM   1887 C  CA  . PRO A 1 208 ? 1.58600   4.47800   47.70700 1.000 20.75890 ? 211 PRO A CA  1 
ATOM   1888 C  C   . PRO A 1 208 ? 2.94600   4.75300   47.09800 1.000 22.12378 ? 211 PRO A C   1 
ATOM   1889 O  O   . PRO A 1 208 ? 3.41500   3.95700   46.27800 1.000 23.79378 ? 211 PRO A O   1 
ATOM   1890 C  CB  . PRO A 1 208 ? 0.44900   5.02200   46.82700 1.000 21.38378 ? 211 PRO A CB  1 
ATOM   1891 C  CG  . PRO A 1 208 ? 0.07800   6.33400   47.45700 1.000 30.05378 ? 211 PRO A CG  1 
ATOM   1892 C  CD  . PRO A 1 208 ? 0.28100   6.14500   48.94000 1.000 26.07378 ? 211 PRO A CD  1 
ATOM   1893 N  N   . ASN A 1 209 ? 3.60500   5.82800   47.50100 1.000 22.25378 ? 212 ASN A N   1 
ATOM   1894 C  CA  . ASN A 1 209 ? 4.90400   6.20000   46.96400 1.000 21.05378 ? 212 ASN A CA  1 
ATOM   1895 C  C   . ASN A 1 209 ? 6.06500   5.70300   47.81300 1.000 23.33378 ? 212 ASN A C   1 
ATOM   1896 O  O   . ASN A 1 209 ? 7.22600   5.96000   47.47200 1.000 21.72378 ? 212 ASN A O   1 
ATOM   1897 C  CB  . ASN A 1 209 ? 4.95800   7.71900   46.80400 1.000 22.02378 ? 212 ASN A CB  1 
ATOM   1898 C  CG  . ASN A 1 209 ? 3.91000   8.22400   45.83600 1.000 27.65378 ? 212 ASN A CG  1 
ATOM   1899 O  OD1 . ASN A 1 209 ? 3.63000   7.57600   44.82500 1.000 26.85378 ? 212 ASN A OD1 1 
ATOM   1900 N  ND2 . ASN A 1 209 ? 3.31000   9.36700   46.14600 1.000 36.79378 ? 212 ASN A ND2 1 
ATOM   1901 N  N   . GLU A 1 210 ? 5.78800   4.98700   48.89500 1.000 14.59237 ? 213 GLU A N   1 
ATOM   1902 C  CA  . GLU A 1 210 ? 6.81500   4.56000   49.83400 1.000 12.20525 ? 213 GLU A CA  1 
ATOM   1903 C  C   . GLU A 1 210 ? 7.16600   3.10200   49.55600 1.000 12.02891 ? 213 GLU A C   1 
ATOM   1904 O  O   . GLU A 1 210 ? 6.32100   2.21400   49.71100 1.000 13.00008 ? 213 GLU A O   1 
ATOM   1905 C  CB  . GLU A 1 210 ? 6.31400   4.70900   51.27100 1.000 11.08143 ? 213 GLU A CB  1 
ATOM   1906 C  CG  . GLU A 1 210 ? 7.33200   4.30400   52.31500 1.000 10.62874 ? 213 GLU A CG  1 
ATOM   1907 C  CD  . GLU A 1 210 ? 8.60700   5.09100   52.18000 1.000 10.28133 ? 213 GLU A CD  1 
ATOM   1908 O  OE1 . GLU A 1 210 ? 8.56700   6.29800   52.50600 1.000 11.33935 ? 213 GLU A OE1 1 
ATOM   1909 O  OE2 . GLU A 1 210 ? 9.63200   4.52100   51.72900 1.000 11.19197 ? 213 GLU A OE2 1 
ATOM   1910 N  N   . LYS A 1 211 ? 8.42300   2.85300   49.18900 1.000 13.07904 ? 214 LYS A N   1 
ATOM   1911 C  CA  A LYS A 1 211 ? 8.86700   1.49300   48.93100 0.650 13.81860 ? 214 LYS A CA  1 
ATOM   1912 C  CA  B LYS A 1 211 ? 8.90400   1.50700   48.91700 0.350 12.77378 ? 214 LYS A CA  1 
ATOM   1913 C  C   . LYS A 1 211 ? 9.57700   0.85300   50.11600 1.000 12.07628 ? 214 LYS A C   1 
ATOM   1914 O  O   . LYS A 1 211 ? 9.77200   -0.36300  50.10500 1.000 12.97902 ? 214 LYS A O   1 
ATOM   1915 C  CB  A LYS A 1 211 ? 9.76600   1.42800   47.68900 0.650 17.12689 ? 214 LYS A CB  1 
ATOM   1916 C  CB  B LYS A 1 211 ? 9.89000   1.53000   47.74300 0.350 24.66378 ? 214 LYS A CB  1 
ATOM   1917 C  CG  A LYS A 1 211 ? 9.10600   1.95700   46.42400 0.650 21.96168 ? 214 LYS A CG  1 
ATOM   1918 C  CG  B LYS A 1 211 ? 9.34300   2.19700   46.49100 0.350 35.84378 ? 214 LYS A CG  1 
ATOM   1919 C  CD  A LYS A 1 211 ? 7.78600   1.25900   46.15500 0.650 27.61378 ? 214 LYS A CD  1 
ATOM   1920 C  CD  B LYS A 1 211 ? 10.41000  2.31800   45.41600 0.350 13.96378 ? 214 LYS A CD  1 
ATOM   1921 C  CE  A LYS A 1 211 ? 7.01000   1.97100   45.05600 0.650 36.04378 ? 214 LYS A CE  1 
ATOM   1922 C  CE  B LYS A 1 211 ? 11.52400  3.26600   45.83300 0.350 23.92378 ? 214 LYS A CE  1 
ATOM   1923 N  NZ  A LYS A 1 211 ? 5.65100   1.39500   44.87400 0.650 46.25378 ? 214 LYS A NZ  1 
ATOM   1924 N  NZ  B LYS A 1 211 ? 11.03600  4.66500   45.98800 0.350 28.80378 ? 214 LYS A NZ  1 
ATOM   1925 N  N   . ARG A 1 212 ? 9.96600   1.62600   51.12900 1.000 10.20764 ? 215 ARG A N   1 
ATOM   1926 C  CA  . ARG A 1 212 ? 10.46200  1.01500   52.34900 1.000 9.98919  ? 215 ARG A CA  1 
ATOM   1927 C  C   . ARG A 1 212 ? 9.29800   0.35700   53.07400 1.000 9.42597  ? 215 ARG A C   1 
ATOM   1928 O  O   . ARG A 1 212 ? 8.13400   0.70600   52.87000 1.000 9.90760  ? 215 ARG A O   1 
ATOM   1929 C  CB  . ARG A 1 212 ? 11.12700  2.06800   53.23500 1.000 10.91825 ? 215 ARG A CB  1 
ATOM   1930 C  CG  . ARG A 1 212 ? 12.38100  2.65100   52.60100 1.000 11.73677 ? 215 ARG A CG  1 
ATOM   1931 C  CD  . ARG A 1 212 ? 12.88200  3.86000   53.36000 1.000 12.09734 ? 215 ARG A CD  1 
ATOM   1932 N  NE  . ARG A 1 212 ? 11.94400  4.96800   53.21900 1.000 11.57622 ? 215 ARG A NE  1 
ATOM   1933 C  CZ  . ARG A 1 212 ? 12.10400  6.16200   53.76900 1.000 11.89205 ? 215 ARG A CZ  1 
ATOM   1934 N  NH1 . ARG A 1 212 ? 13.13600  6.42900   54.55500 1.000 13.31064 ? 215 ARG A NH1 1 
ATOM   1935 N  NH2 . ARG A 1 212 ? 11.19800  7.10900   53.52900 1.000 13.12378 ? 215 ARG A NH2 1 
ATOM   1936 N  N   . ASP A 1 213 ? 9.62200   -0.59300  53.94000 1.000 8.82326  ? 216 ASP A N   1 
ATOM   1937 C  CA  . ASP A 1 213 ? 8.58400   -1.22000  54.75000 1.000 9.14699  ? 216 ASP A CA  1 
ATOM   1938 C  C   . ASP A 1 213 ? 8.09400   -0.20400  55.78100 1.000 7.81261  ? 216 ASP A C   1 
ATOM   1939 O  O   . ASP A 1 213 ? 8.90000   0.40200   56.48400 1.000 8.32847  ? 216 ASP A O   1 
ATOM   1940 C  CB  . ASP A 1 213 ? 9.17800   -2.47600  55.40400 1.000 9.58388  ? 216 ASP A CB  1 
ATOM   1941 C  CG  . ASP A 1 213 ? 8.12300   -3.44700  55.89300 1.000 9.46281  ? 216 ASP A CG  1 
ATOM   1942 O  OD1 . ASP A 1 213 ? 6.91800   -3.25500  55.63700 1.000 9.89181  ? 216 ASP A OD1 1 
ATOM   1943 O  OD2 . ASP A 1 213 ? 8.50100   -4.43300  56.53200 1.000 10.65506 ? 216 ASP A OD2 1 
ATOM   1944 N  N   . HIS A 1 214 ? 6.78000   0.02000   55.84500 1.000 8.37584  ? 217 HIS A N   1 
ATOM   1945 C  CA  . HIS A 1 214 ? 6.27800   1.17800   56.57200 1.000 7.96526  ? 217 HIS A CA  1 
ATOM   1946 C  C   . HIS A 1 214 ? 4.83000   0.95700   56.97500 1.000 7.75734  ? 217 HIS A C   1 
ATOM   1947 O  O   . HIS A 1 214 ? 4.15300   0.04800   56.48100 1.000 8.50743  ? 217 HIS A O   1 
ATOM   1948 C  CB  . HIS A 1 214 ? 6.39500   2.44500   55.71900 1.000 8.37321  ? 217 HIS A CB  1 
ATOM   1949 C  CG  . HIS A 1 214 ? 5.39000   2.51000   54.61000 1.000 8.73904  ? 217 HIS A CG  1 
ATOM   1950 N  ND1 . HIS A 1 214 ? 5.50100   1.76600   53.45400 1.000 8.97328  ? 217 HIS A ND1 1 
ATOM   1951 C  CD2 . HIS A 1 214 ? 4.22100   3.19300   54.50600 1.000 9.80759  ? 217 HIS A CD2 1 
ATOM   1952 C  CE1 . HIS A 1 214 ? 4.46100   2.01900   52.67200 1.000 10.37345 ? 217 HIS A CE1 1 
ATOM   1953 N  NE2 . HIS A 1 214 ? 3.66600   2.87300   53.29200 1.000 11.10775 ? 217 HIS A NE2 1 
ATOM   1954 N  N   . MET A 1 215 ? 4.34300   1.86100   57.82700 1.000 7.84946  ? 218 MET A N   1 
ATOM   1955 C  CA  . MET A 1 215 ? 2.95000   1.86700   58.25300 1.000 7.18622  ? 218 MET A CA  1 
ATOM   1956 C  C   . MET A 1 215 ? 2.51500   3.30900   58.46800 1.000 7.28624  ? 218 MET A C   1 
ATOM   1957 O  O   . MET A 1 215 ? 3.22300   4.08400   59.11700 1.000 7.73629  ? 218 MET A O   1 
ATOM   1958 C  CB  . MET A 1 215 ? 2.76800   1.07500   59.55700 1.000 7.20201  ? 218 MET A CB  1 
ATOM   1959 C  CG  . MET A 1 215 ? 1.40400   1.30000   60.21200 1.000 7.54416  ? 218 MET A CG  1 
ATOM   1960 S  SD  . MET A 1 215 ? 1.05600   0.17600   61.57800 1.000 7.52837  ? 218 MET A SD  1 
ATOM   1961 C  CE  . MET A 1 215 ? 2.20600   0.74200   62.83400 1.000 8.50743  ? 218 MET A CE  1 
ATOM   1962 N  N   . VAL A 1 216 ? 1.34800   3.66100   57.94200 1.000 7.03621  ? 219 VAL A N   1 
ATOM   1963 C  CA  . VAL A 1 216 ? 0.69300   4.93200   58.24300 1.000 7.32835  ? 219 VAL A CA  1 
ATOM   1964 C  C   . VAL A 1 216 ? -0.46700  4.63900   59.18200 1.000 6.85987  ? 219 VAL A C   1 
ATOM   1965 O  O   . VAL A 1 216 ? -1.26300  3.72000   58.92900 1.000 7.20728  ? 219 VAL A O   1 
ATOM   1966 C  CB  . VAL A 1 216 ? 0.21500   5.64400   56.96800 1.000 8.52849  ? 219 VAL A CB  1 
ATOM   1967 C  CG1 . VAL A 1 216 ? -0.52600  6.94000   57.34200 1.000 9.87339  ? 219 VAL A CG1 1 
ATOM   1968 C  CG2 . VAL A 1 216 ? 1.41100   5.96300   56.05000 1.000 9.98656  ? 219 VAL A CG2 1 
ATOM   1969 N  N   . LEU A 1 217 ? -0.53600  5.39200   60.27900 1.000 7.47836  ? 220 LEU A N   1 
ATOM   1970 C  CA  . LEU A 1 217 ? -1.54200  5.22100   61.31500 1.000 7.27571  ? 220 LEU A CA  1 
ATOM   1971 C  C   . LEU A 1 217 ? -2.29900  6.53000   61.50600 1.000 7.78366  ? 220 LEU A C   1 
ATOM   1972 O  O   . LEU A 1 217 ? -1.69400  7.59300   61.68000 1.000 8.45216  ? 220 LEU A O   1 
ATOM   1973 C  CB  . LEU A 1 217 ? -0.83300  4.86200   62.61200 1.000 7.99948  ? 220 LEU A CB  1 
ATOM   1974 C  CG  . LEU A 1 217 ? -1.67600  4.86800   63.89000 1.000 7.85999  ? 220 LEU A CG  1 
ATOM   1975 C  CD1 . LEU A 1 217 ? -2.73500  3.77700   63.89500 1.000 8.51007  ? 220 LEU A CD1 1 
ATOM   1976 C  CD2 . LEU A 1 217 ? -0.77200  4.68100   65.10200 1.000 9.51545  ? 220 LEU A CD2 1 
ATOM   1977 N  N   . LEU A 1 218 ? -3.62300  6.44300   61.51500 1.000 7.24676  ? 221 LEU A N   1 
ATOM   1978 C  CA  . LEU A 1 218 ? -4.50800  7.54000   61.90100 1.000 8.14423  ? 221 LEU A CA  1 
ATOM   1979 C  C   . LEU A 1 218 ? -5.34200  7.02700   63.06400 1.000 6.99146  ? 221 LEU A C   1 
ATOM   1980 O  O   . LEU A 1 218 ? -6.01000  5.99200   62.94000 1.000 8.89959  ? 221 LEU A O   1 
ATOM   1981 C  CB  . LEU A 1 218 ? -5.42300  7.92900   60.73000 1.000 9.63915  ? 221 LEU A CB  1 
ATOM   1982 C  CG  . LEU A 1 218 ? -6.53800  8.92600   61.05700 1.000 12.58424 ? 221 LEU A CG  1 
ATOM   1983 C  CD1 . LEU A 1 218 ? -5.97900  10.27200  61.50400 1.000 14.41867 ? 221 LEU A CD1 1 
ATOM   1984 C  CD2 . LEU A 1 218 ? -7.47900  9.13000   59.86400 1.000 13.92387 ? 221 LEU A CD2 1 
ATOM   1985 N  N   . GLU A 1 219 ? -5.28200  7.72400   64.19600 1.000 7.41257  ? 222 GLU A N   1 
ATOM   1986 C  CA  . GLU A 1 219 ? -5.89400  7.21500   65.41300 1.000 7.37046  ? 222 GLU A CA  1 
ATOM   1987 C  C   . GLU A 1 219 ? -6.65400  8.33300   66.10800 1.000 7.94158  ? 222 GLU A C   1 
ATOM   1988 O  O   . GLU A 1 219 ? -6.20800  9.48600   66.12300 1.000 9.44176  ? 222 GLU A O   1 
ATOM   1989 C  CB  . GLU A 1 219 ? -4.80800  6.62800   66.32600 1.000 9.63125  ? 222 GLU A CB  1 
ATOM   1990 C  CG  . GLU A 1 219 ? -5.24900  5.83000   67.52200 1.000 9.64441  ? 222 GLU A CG  1 
ATOM   1991 C  CD  . GLU A 1 219 ? -4.08600  4.96500   68.02500 1.000 9.52071  ? 222 GLU A CD  1 
ATOM   1992 O  OE1 . GLU A 1 219 ? -3.89900  3.81300   67.53700 1.000 8.67588  ? 222 GLU A OE1 1 
ATOM   1993 O  OE2 . GLU A 1 219 ? -3.31900  5.47400   68.87200 1.000 10.30502 ? 222 GLU A OE2 1 
ATOM   1994 N  N   . PHE A 1 220 ? -7.80100  7.97500   66.68400 1.000 7.88894  ? 223 PHE A N   1 
ATOM   1995 C  CA  . PHE A 1 220 ? -8.60300  8.90400   67.47200 1.000 7.91789  ? 223 PHE A CA  1 
ATOM   1996 C  C   . PHE A 1 220 ? -8.88300  8.27200   68.82000 1.000 8.11265  ? 223 PHE A C   1 
ATOM   1997 O  O   . PHE A 1 220 ? -9.27000  7.10000   68.88500 1.000 9.47860  ? 223 PHE A O   1 
ATOM   1998 C  CB  . PHE A 1 220 ? -9.94700  9.24300   66.80500 1.000 9.00749  ? 223 PHE A CB  1 
ATOM   1999 C  CG  . PHE A 1 220 ? -9.79800  9.96300   65.50400 1.000 9.20225  ? 223 PHE A CG  1 
ATOM   2000 C  CD1 . PHE A 1 220 ? -9.65500  11.34800  65.45700 1.000 10.32607 ? 223 PHE A CD1 1 
ATOM   2001 C  CD2 . PHE A 1 220 ? -9.73500  9.25000   64.31800 1.000 9.64441  ? 223 PHE A CD2 1 
ATOM   2002 C  CE1 . PHE A 1 220 ? -9.49400  11.98400  64.23700 1.000 11.24197 ? 223 PHE A CE1 1 
ATOM   2003 C  CE2 . PHE A 1 220 ? -9.58100  9.88200   63.11300 1.000 10.75507 ? 223 PHE A CE2 1 
ATOM   2004 C  CZ  . PHE A 1 220 ? -9.45400  11.25200  63.07500 1.000 11.82625 ? 223 PHE A CZ  1 
ATOM   2005 N  N   . VAL A 1 221 ? -8.69100  9.03900   69.89400 1.000 8.79168  ? 224 VAL A N   1 
ATOM   2006 C  CA  . VAL A 1 221 ? -8.84800  8.52000   71.24500 1.000 9.94971  ? 224 VAL A CA  1 
ATOM   2007 C  C   . VAL A 1 221 ? -9.60300  9.53500   72.07600 1.000 10.27080 ? 224 VAL A C   1 
ATOM   2008 O  O   . VAL A 1 221 ? -9.21400  10.70400  72.13500 1.000 10.37082 ? 224 VAL A O   1 
ATOM   2009 C  CB  . VAL A 1 221 ? -7.48000  8.28300   71.89100 1.000 11.28145 ? 224 VAL A CB  1 
ATOM   2010 C  CG1 . VAL A 1 221 ? -7.65200  7.74900   73.31300 1.000 12.05523 ? 224 VAL A CG1 1 
ATOM   2011 C  CG2 . VAL A 1 221 ? -6.67900  7.32900   71.03800 1.000 11.19460 ? 224 VAL A CG2 1 
ATOM   2012 N  N   . THR A 1 222 ? -10.64300 9.07100   72.76200 1.000 10.32081 ? 225 THR A N   1 
ATOM   2013 C  CA  . THR A 1 222 ? -11.40600 9.88200   73.69900 1.000 10.14974 ? 225 THR A CA  1 
ATOM   2014 C  C   . THR A 1 222 ? -11.42900 9.17500   75.04800 1.000 9.00486  ? 225 THR A C   1 
ATOM   2015 O  O   . THR A 1 222 ? -11.74600 7.97900   75.11900 1.000 9.47071  ? 225 THR A O   1 
ATOM   2016 C  CB  . THR A 1 222 ? -12.84700 10.09200  73.19300 1.000 12.51055 ? 225 THR A CB  1 
ATOM   2017 O  OG1 . THR A 1 222 ? -12.82900 10.75200  71.91700 1.000 14.77661 ? 225 THR A OG1 1 
ATOM   2018 C  CG2 . THR A 1 222 ? -13.61800 10.95700  74.17800 1.000 12.54476 ? 225 THR A CG2 1 
ATOM   2019 N  N   . ALA A 1 223 ? -11.11000 9.91300   76.11400 1.000 8.70483  ? 226 ALA A N   1 
ATOM   2020 C  CA  . ALA A 1 223 ? -11.30000 9.37600   77.45400 1.000 8.98907  ? 226 ALA A CA  1 
ATOM   2021 C  C   . ALA A 1 223 ? -12.78000 9.36400   77.79700 1.000 8.83642  ? 226 ALA A C   1 
ATOM   2022 O  O   . ALA A 1 223 ? -13.52900 10.26300  77.41900 1.000 9.63125  ? 226 ALA A O   1 
ATOM   2023 C  CB  . ALA A 1 223 ? -10.55600 10.21700  78.49300 1.000 9.15488  ? 226 ALA A CB  1 
ATOM   2024 N  N   . ALA A 1 224 ? -13.19100 8.35700   78.55900 1.000 9.57598  ? 227 ALA A N   1 
ATOM   2025 C  CA  . ALA A 1 224 ? -14.60600 8.13500   78.83700 1.000 10.83666 ? 227 ALA A CA  1 
ATOM   2026 C  C   . ALA A 1 224 ? -14.73600 7.31800   80.11600 1.000 10.65243 ? 227 ALA A C   1 
ATOM   2027 O  O   . ALA A 1 224 ? -13.74700 6.90100   80.72600 1.000 10.79455 ? 227 ALA A O   1 
ATOM   2028 C  CB  . ALA A 1 224 ? -15.30700 7.44600   77.65700 1.000 11.65781 ? 227 ALA A CB  1 
ATOM   2029 N  N   . GLY A 1 225 ? -15.98200 7.09300   80.51400 1.000 12.86059 ? 228 GLY A N   1 
ATOM   2030 C  CA  . GLY A 1 225 ? -16.28800 6.27800   81.66700 1.000 14.53974 ? 228 GLY A CA  1 
ATOM   2031 C  C   . GLY A 1 225 ? -16.51500 7.05200   82.94200 1.000 15.87148 ? 228 GLY A C   1 
ATOM   2032 O  O   . GLY A 1 225 ? -16.77200 6.43300   83.97800 1.000 17.47693 ? 228 GLY A O   1 
ATOM   2033 N  N   . ILE A 1 226 ? -16.40100 8.37700   82.90800 1.000 16.09782 ? 229 ILE A N   1 
ATOM   2034 C  CA  . ILE A 1 226 ? -16.72300 9.23400   84.04200 1.000 18.17175 ? 229 ILE A CA  1 
ATOM   2035 C  C   . ILE A 1 226 ? -17.72700 10.27200  83.56400 1.000 19.17713 ? 229 ILE A C   1 
ATOM   2036 O  O   . ILE A 1 226 ? -17.51000 10.92900  82.53800 1.000 18.26387 ? 229 ILE A O   1 
ATOM   2037 C  CB  . ILE A 1 226 ? -15.45900 9.89600   84.62400 1.000 19.72983 ? 229 ILE A CB  1 
ATOM   2038 C  CG1 . ILE A 1 226 ? -14.53500 8.83000   85.22600 1.000 19.30610 ? 229 ILE A CG1 1 
ATOM   2039 C  CG2 . ILE A 1 226 ? -15.82700 10.93600  85.67100 1.000 22.57378 ? 229 ILE A CG2 1 
ATOM   2040 C  CD1 . ILE A 1 226 ? -13.20200 9.36000   85.71600 1.000 19.16398 ? 229 ILE A CD1 1 
ATOM   2041 N  N   . THR A 1 227 ? -18.82800 10.41700  84.30100 1.000 20.70378 ? 230 THR A N   1 
ATOM   2042 C  CA  . THR A 1 227 ? -19.89700 11.31200  83.87300 1.000 24.16378 ? 230 THR A CA  1 
ATOM   2043 C  C   . THR A 1 227 ? -19.76400 12.73600  84.40400 1.000 23.31378 ? 230 THR A C   1 
ATOM   2044 O  O   . THR A 1 227 ? -20.29700 13.66100  83.77800 1.000 34.51378 ? 230 THR A O   1 
ATOM   2045 C  CB  . THR A 1 227 ? -21.26700 10.72900  84.23900 1.000 38.53378 ? 230 THR A CB  1 
ATOM   2046 O  OG1 . THR A 1 227 ? -21.30500 10.42800  85.63900 1.000 36.38378 ? 230 THR A OG1 1 
ATOM   2047 C  CG2 . THR A 1 227 ? -21.53300 9.46000   83.44000 1.000 38.41378 ? 230 THR A CG2 1 
ATOM   2048 N  N   . HIS A 1 228 ? -19.07800 12.94700  85.52400 1.000 23.93378 ? 231 HIS A N   1 
ATOM   2049 C  CA  . HIS A 1 228 ? -18.98100 14.29900  86.08600 1.000 43.02378 ? 231 HIS A CA  1 
ATOM   2050 C  C   . HIS A 1 228 ? -17.57400 14.69400  86.53000 1.000 65.89378 ? 231 HIS A C   1 
ATOM   2051 O  O   . HIS A 1 228 ? -16.71500 13.85300  86.79100 1.000 35.78378 ? 231 HIS A O   1 
ATOM   2052 C  CB  . HIS A 1 228 ? -19.96000 14.47400  87.25100 1.000 66.01378 ? 231 HIS A CB  1 
ATOM   2053 C  CG  . HIS A 1 228 ? -21.39100 14.24200  86.87800 1.000 78.42378 ? 231 HIS A CG  1 
ATOM   2054 N  ND1 . HIS A 1 228 ? -21.92100 12.98100  86.71100 1.000 73.43378 ? 231 HIS A ND1 1 
ATOM   2055 C  CD2 . HIS A 1 228 ? -22.40100 15.11100  86.63600 1.000 67.54378 ? 231 HIS A CD2 1 
ATOM   2056 C  CE1 . HIS A 1 228 ? -23.19600 13.08200  86.38400 1.000 58.86378 ? 231 HIS A CE1 1 
ATOM   2057 N  NE2 . HIS A 1 228 ? -23.51300 14.36300  86.33300 1.000 93.96378 ? 231 HIS A NE2 1 
ATOM   2058 O  OXT . HIS A 1 228 ? -17.27000 15.88300  86.64600 1.000 63.61378 ? 231 HIS A OXT 1 
HETATM 2059 MG MG  . MG  B 2 .   ? -13.56600 10.84300  94.24400 0.250 9.55378  ? 301 MG  A MG  1 
HETATM 2060 MG MG  . MG  C 2 .   ? -9.08300  22.08000  75.29400 0.520 9.21278  ? 302 MG  A MG  1 
HETATM 2061 O  O   . HOH D 3 .   ? -4.60400  4.65400   73.81100 1.000 8.41532  ? 401 HOH A O   1 
HETATM 2062 O  O   A HOH D 3 .   ? -3.38800  5.77800   71.53600 0.930 14.31603 ? 402 HOH A O   1 
HETATM 2063 O  O   B HOH D 3 .   ? -3.57700  7.79300   70.84100 0.070 5.93378  ? 402 HOH A O   1 
HETATM 2064 O  O   . HOH D 3 .   ? -7.62300  0.91400   68.13600 1.000 8.00211  ? 403 HOH A O   1 
HETATM 2065 O  O   A HOH D 3 .   ? -3.95500  8.66800   72.53700 0.720 15.06612 ? 404 HOH A O   1 
HETATM 2066 O  O   B HOH D 3 .   ? -4.34100  7.48200   73.67700 0.280 8.15378  ? 404 HOH A O   1 
HETATM 2067 O  O   . HOH D 3 .   ? -0.68700  -3.28400  68.59200 1.000 7.16254  ? 405 HOH A O   1 
HETATM 2068 O  O   . HOH D 3 .   ? -0.89900  6.96500   71.39500 1.000 6.99673  ? 406 HOH A O   1 
HETATM 2069 O  O   . HOH D 3 .   ? -6.56200  -4.65100  66.12800 1.000 11.21302 ? 407 HOH A O   1 
HETATM 2070 O  O   . HOH D 3 .   ? -0.26600  -5.74000  69.84600 1.000 7.17570  ? 408 HOH A O   1 
HETATM 2071 O  O   . HOH D 3 .   ? -9.73100  -3.97300  76.07300 1.000 15.01348 ? 409 HOH A O   1 
HETATM 2072 O  O   . HOH D 3 .   ? -12.08700 -3.35300  73.85700 1.000 12.92902 ? 410 HOH A O   1 
HETATM 2073 O  O   . HOH D 3 .   ? -4.82800  10.44700  70.36500 1.000 18.27966 ? 411 HOH A O   1 
HETATM 2074 O  O   A HOH D 3 .   ? -10.89600 -5.48600  73.79700 0.690 23.92378 ? 412 HOH A O   1 
HETATM 2075 O  O   B HOH D 3 .   ? -10.88500 -6.66000  73.23500 0.310 16.45378 ? 412 HOH A O   1 
HETATM 2076 O  O   . HOH D 3 .   ? 2.46000   -2.88600  70.24100 1.000 6.63879  ? 413 HOH A O   1 
HETATM 2077 O  O   . HOH D 3 .   ? 1.72600   6.79600   76.13200 1.000 8.42058  ? 414 HOH A O   1 
HETATM 2078 O  O   A HOH D 3 .   ? -12.19600 7.02100   69.12900 0.640 15.03190 ? 415 HOH A O   1 
HETATM 2079 O  O   B HOH D 3 .   ? -12.07000 7.92600   70.42700 0.360 19.05378 ? 415 HOH A O   1 
HETATM 2080 O  O   . HOH D 3 .   ? -10.15900 0.90200   64.66400 1.000 12.92902 ? 416 HOH A O   1 
HETATM 2081 O  O   A HOH D 3 .   ? -13.63600 1.55200   71.00900 0.370 12.36378 ? 417 HOH A O   1 
HETATM 2082 O  O   B HOH D 3 .   ? -13.95100 0.14400   71.44500 0.630 17.64800 ? 417 HOH A O   1 
HETATM 2083 O  O   A HOH D 3 .   ? -12.66000 -4.20500  71.26200 0.720 27.38813 ? 418 HOH A O   1 
HETATM 2084 O  O   . HOH D 3 .   ? -4.57300  -5.83500  63.98300 1.000 9.74443  ? 419 HOH A O   1 
HETATM 2085 O  O   . HOH D 3 .   ? 3.77500   -1.56200  74.38700 1.000 6.65195  ? 420 HOH A O   1 
HETATM 2086 O  O   . HOH D 3 .   ? -10.20100 -5.69900  78.03300 1.000 24.39378 ? 421 HOH A O   1 
HETATM 2087 O  O   . HOH D 3 .   ? -7.87400  -6.65500  79.78800 1.000 18.47179 ? 422 HOH A O   1 
HETATM 2088 O  O   A HOH D 3 .   ? -14.07500 3.15500   69.44600 0.560 21.45378 ? 423 HOH A O   1 
HETATM 2089 O  O   B HOH D 3 .   ? -14.54100 1.80800   69.78000 0.440 9.68378  ? 423 HOH A O   1 
HETATM 2090 O  O   A HOH D 3 .   ? -11.04600 -6.19000  69.13000 0.590 24.92378 ? 424 HOH A O   1 
HETATM 2091 O  O   A HOH D 3 .   ? -14.66400 2.70200   67.00700 0.330 8.70378  ? 425 HOH A O   1 
HETATM 2092 O  O   B HOH D 3 .   ? -15.05400 3.35500   68.12200 0.670 20.91378 ? 425 HOH A O   1 
HETATM 2093 O  O   . HOH D 3 .   ? -8.93100  6.08200   62.81700 1.000 20.92998 ? 426 HOH A O   1 
HETATM 2094 O  O   A HOH D 3 .   ? -15.46400 0.17100   71.81800 0.530 12.35526 ? 427 HOH A O   1 
HETATM 2095 O  O   B HOH D 3 .   ? -15.77900 -1.04900  72.13600 0.470 19.23378 ? 427 HOH A O   1 
HETATM 2096 O  O   . HOH D 3 .   ? -13.43700 -2.67700  65.86000 1.000 21.63378 ? 428 HOH A O   1 
HETATM 2097 O  O   B HOH D 3 .   ? -14.65100 -3.72200  74.70300 0.410 18.71378 ? 429 HOH A O   1 
HETATM 2098 O  O   . HOH D 3 .   ? 5.86600   0.49400   76.47500 1.000 8.57323  ? 430 HOH A O   1 
HETATM 2099 O  O   A HOH D 3 .   ? -10.30100 3.40900   62.63900 0.530 19.85880 ? 431 HOH A O   1 
HETATM 2100 O  O   B HOH D 3 .   ? -11.04400 4.73500   62.67300 0.470 19.95378 ? 431 HOH A O   1 
HETATM 2101 O  O   . HOH D 3 .   ? -7.31900  -6.44700  63.22300 1.000 11.98417 ? 432 HOH A O   1 
HETATM 2102 O  O   . HOH D 3 .   ? 7.06900   13.71000  85.11500 1.000 11.86310 ? 433 HOH A O   1 
HETATM 2103 O  O   . HOH D 3 .   ? 10.92100  24.43400  66.00500 1.000 30.93378 ? 434 HOH A O   1 
HETATM 2104 O  O   . HOH D 3 .   ? 4.77800   2.17700   74.54700 1.000 7.05463  ? 435 HOH A O   1 
HETATM 2105 O  O   . HOH D 3 .   ? -3.85500  12.47000  77.62600 1.000 7.57574  ? 436 HOH A O   1 
HETATM 2106 O  O   . HOH D 3 .   ? -15.66900 2.93200   73.53200 1.000 15.61092 ? 437 HOH A O   1 
HETATM 2107 O  O   . HOH D 3 .   ? -9.31000  0.41800   60.94400 1.000 16.15572 ? 438 HOH A O   1 
HETATM 2108 O  O   A HOH D 3 .   ? -13.73500 -3.80000  76.37800 0.580 20.41149 ? 439 HOH A O   1 
HETATM 2109 O  O   B HOH D 3 .   ? -14.08200 -4.68000  77.45300 0.420 20.28378 ? 439 HOH A O   1 
HETATM 2110 O  O   . HOH D 3 .   ? -12.43800 9.86600   69.45900 1.000 23.55378 ? 440 HOH A O   1 
HETATM 2111 O  O   . HOH D 3 .   ? -16.26200 -0.00300  68.46200 1.000 27.16378 ? 441 HOH A O   1 
HETATM 2112 O  O   . HOH D 3 .   ? -15.39900 -0.69900  65.74900 1.000 34.43378 ? 442 HOH A O   1 
HETATM 2113 O  O   . HOH D 3 .   ? 5.29700   4.76000   74.97600 1.000 6.68616  ? 443 HOH A O   1 
HETATM 2114 O  O   . HOH D 3 .   ? -6.99300  -0.36800  59.41500 1.000 11.71308 ? 444 HOH A O   1 
HETATM 2115 O  O   A HOH D 3 .   ? -14.45500 2.09400   64.50600 0.680 28.95378 ? 445 HOH A O   1 
HETATM 2116 O  O   B HOH D 3 .   ? -15.44400 2.67000   65.69200 0.320 23.82378 ? 445 HOH A O   1 
HETATM 2117 O  O   . HOH D 3 .   ? -9.78400  -2.22700  60.44000 1.000 21.95378 ? 446 HOH A O   1 
HETATM 2118 O  O   A HOH D 3 .   ? -12.43600 -7.47800  75.34700 0.710 23.33378 ? 447 HOH A O   1 
HETATM 2119 O  O   B HOH D 3 .   ? -13.16800 -8.88300  75.93800 0.290 17.44378 ? 447 HOH A O   1 
HETATM 2120 O  O   . HOH D 3 .   ? -10.04200 -4.72100  61.53700 1.000 24.32378 ? 448 HOH A O   1 
HETATM 2121 O  O   A HOH D 3 .   ? -12.36100 -8.15400  67.21600 0.720 26.71602 ? 449 HOH A O   1 
HETATM 2122 O  O   . HOH D 3 .   ? -17.36300 2.27500   71.44400 1.000 23.54378 ? 450 HOH A O   1 
HETATM 2123 O  O   A HOH D 3 .   ? -3.66800  -7.94700  80.43600 0.650 16.43207 ? 451 HOH A O   1 
HETATM 2124 O  O   B HOH D 3 .   ? -2.52700  -8.62100  80.03000 0.350 12.53378 ? 451 HOH A O   1 
HETATM 2125 O  O   . HOH D 3 .   ? -12.21500 -7.01400  77.57900 1.000 50.47378 ? 452 HOH A O   1 
HETATM 2126 O  O   A HOH D 3 .   ? -6.11700  -8.77300  79.47800 0.560 14.72660 ? 453 HOH A O   1 
HETATM 2127 O  O   B HOH D 3 .   ? -5.27200  -8.16900  78.95300 0.440 12.91378 ? 453 HOH A O   1 
HETATM 2128 O  O   A HOH D 3 .   ? -17.34600 -0.83700  72.87000 0.440 19.28378 ? 454 HOH A O   1 
HETATM 2129 O  O   B HOH D 3 .   ? -17.09500 -0.16900  74.22200 0.560 16.50839 ? 454 HOH A O   1 
HETATM 2130 O  O   . HOH D 3 .   ? -15.53900 7.80900   73.07800 1.000 34.93378 ? 455 HOH A O   1 
HETATM 2131 O  O   . HOH D 3 .   ? -4.14800  -8.00100  62.31600 1.000 9.72337  ? 456 HOH A O   1 
HETATM 2132 O  O   B HOH D 3 .   ? -9.74000  -4.35800  82.33500 1.000 40.14378 ? 457 HOH A O   1 
HETATM 2133 O  O   . HOH D 3 .   ? -9.97600  6.57100   60.42700 1.000 25.11378 ? 458 HOH A O   1 
HETATM 2134 O  O   . HOH D 3 .   ? -15.00100 -6.81100  74.25000 1.000 47.85378 ? 459 HOH A O   1 
HETATM 2135 O  O   A HOH D 3 .   ? -6.35500  -0.89500  84.83300 0.550 17.59537 ? 460 HOH A O   1 
HETATM 2136 O  O   B HOH D 3 .   ? -7.33200  -1.65000  84.44500 0.450 16.44378 ? 460 HOH A O   1 
HETATM 2137 O  O   . HOH D 3 .   ? -10.89000 1.96000   59.38700 1.000 31.14378 ? 461 HOH A O   1 
HETATM 2138 O  O   . HOH D 3 .   ? -4.84500  9.17500   82.95900 1.000 8.68640  ? 462 HOH A O   1 
HETATM 2139 O  O   . HOH D 3 .   ? -17.41400 4.43800   75.05200 1.000 24.76378 ? 463 HOH A O   1 
HETATM 2140 O  O   . HOH D 3 .   ? -17.90600 4.32100   70.29800 1.000 37.00378 ? 464 HOH A O   1 
HETATM 2141 O  O   . HOH D 3 .   ? 0.19600   -9.23700  79.17300 1.000 12.45264 ? 465 HOH A O   1 
HETATM 2142 O  O   . HOH D 3 .   ? -17.11900 6.73300   74.26100 1.000 38.19378 ? 466 HOH A O   1 
HETATM 2143 O  O   . HOH D 3 .   ? -4.17000  5.37600   58.03100 1.000 12.74478 ? 467 HOH A O   1 
HETATM 2144 O  O   B HOH D 3 .   ? -4.54500  -2.64300  85.11100 0.610 20.78378 ? 468 HOH A O   1 
HETATM 2145 O  O   . HOH D 3 .   ? -17.13200 -2.80900  76.30400 1.000 41.70378 ? 469 HOH A O   1 
HETATM 2146 O  O   A HOH D 3 .   ? -12.16500 12.62000  67.80700 0.740 14.24233 ? 470 HOH A O   1 
HETATM 2147 O  O   B HOH D 3 .   ? -12.29600 13.82200  67.48500 0.260 10.72378 ? 470 HOH A O   1 
HETATM 2148 O  O   . HOH D 3 .   ? -12.34600 13.07500  70.50800 1.000 22.73378 ? 471 HOH A O   1 
HETATM 2149 O  O   . HOH D 3 .   ? -11.62400 4.74700   59.70900 1.000 44.75378 ? 472 HOH A O   1 
HETATM 2150 O  O   A HOH D 3 .   ? -18.34500 0.17200   74.78100 0.360 19.32378 ? 473 HOH A O   1 
HETATM 2151 O  O   B HOH D 3 .   ? -17.96500 0.99100   76.22000 0.640 25.55378 ? 473 HOH A O   1 
HETATM 2152 O  O   A HOH D 3 .   ? -17.58600 -0.04500  77.01600 0.570 17.84013 ? 474 HOH A O   1 
HETATM 2153 O  O   B HOH D 3 .   ? -17.10600 0.61700   78.18200 0.430 21.18378 ? 474 HOH A O   1 
HETATM 2154 O  O   . HOH D 3 .   ? -10.61900 1.35300   84.67300 1.000 16.28731 ? 475 HOH A O   1 
HETATM 2155 O  O   A HOH D 3 .   ? 4.06500   -3.55800  82.56000 0.880 23.92378 ? 476 HOH A O   1 
HETATM 2156 O  O   . HOH D 3 .   ? -12.86600 -6.95000  62.73700 1.000 32.46378 ? 477 HOH A O   1 
HETATM 2157 O  O   . HOH D 3 .   ? -12.21600 -8.98800  64.42000 1.000 36.19378 ? 478 HOH A O   1 
HETATM 2158 O  O   . HOH D 3 .   ? -15.16900 6.36700   62.78900 1.000 30.79378 ? 479 HOH A O   1 
HETATM 2159 O  O   B HOH D 3 .   ? -1.65500  9.36300   59.39300 0.290 18.63378 ? 480 HOH A O   1 
HETATM 2160 O  O   A HOH D 3 .   ? -3.49100  -8.07600  82.95200 0.600 20.34378 ? 481 HOH A O   1 
HETATM 2161 O  O   B HOH D 3 .   ? -2.51200  -8.91200  82.65000 0.400 19.93378 ? 481 HOH A O   1 
HETATM 2162 O  O   . HOH D 3 .   ? -13.20000 2.13800   83.45900 1.000 22.25378 ? 482 HOH A O   1 
HETATM 2163 O  O   A HOH D 3 .   ? -17.11700 -0.73800  79.20800 1.000 47.23378 ? 483 HOH A O   1 
HETATM 2164 O  O   . HOH D 3 .   ? -6.20000  -1.30300  56.79900 1.000 20.08514 ? 484 HOH A O   1 
HETATM 2165 O  O   . HOH D 3 .   ? -2.87900  14.33200  63.71200 1.000 13.20010 ? 485 HOH A O   1 
HETATM 2166 O  O   . HOH D 3 .   ? -10.71000 -12.32200 73.78300 1.000 20.64836 ? 486 HOH A O   1 
HETATM 2167 O  O   . HOH D 3 .   ? -9.42900  1.67000   57.10100 1.000 37.05378 ? 487 HOH A O   1 
HETATM 2168 O  O   . HOH D 3 .   ? -9.02600  6.32100   57.86600 1.000 25.83378 ? 488 HOH A O   1 
HETATM 2169 O  O   . HOH D 3 .   ? -10.74800 -2.29100  58.05300 1.000 39.80378 ? 489 HOH A O   1 
HETATM 2170 O  O   . HOH D 3 .   ? -15.39200 12.05600  71.28500 1.000 17.87961 ? 490 HOH A O   1 
HETATM 2171 O  O   . HOH D 3 .   ? -7.20000  2.56700   56.45900 1.000 24.38378 ? 491 HOH A O   1 
HETATM 2172 O  O   . HOH D 3 .   ? -9.86000  -13.04900 71.24500 1.000 15.82937 ? 492 HOH A O   1 
HETATM 2173 O  O   . HOH D 3 .   ? -10.29400 -1.04400  85.51900 1.000 39.24378 ? 493 HOH A O   1 
HETATM 2174 O  O   . HOH D 3 .   ? -6.70100  5.25400   56.81100 1.000 20.70627 ? 494 HOH A O   1 
HETATM 2175 O  O   . HOH D 3 .   ? -15.52500 0.33000   82.10800 1.000 43.92378 ? 495 HOH A O   1 
HETATM 2176 O  O   . HOH D 3 .   ? -12.21000 -2.48200  84.24700 1.000 39.65378 ? 496 HOH A O   1 
HETATM 2177 O  O   . HOH D 3 .   ? -17.19400 9.32700   75.45000 1.000 27.11378 ? 497 HOH A O   1 
HETATM 2178 O  O   . HOH D 3 .   ? -11.75600 -6.10600  59.84500 1.000 27.33378 ? 498 HOH A O   1 
HETATM 2179 O  O   A HOH D 3 .   ? 5.98800   -5.23000  81.69600 0.550 21.66378 ? 499 HOH A O   1 
HETATM 2180 O  O   B HOH D 3 .   ? 4.59800   -5.91500  82.66300 0.450 18.93378 ? 499 HOH A O   1 
HETATM 2181 O  O   . HOH D 3 .   ? -7.17600  16.37400  76.20500 1.000 17.07162 ? 500 HOH A O   1 
HETATM 2182 O  O   . HOH D 3 .   ? 1.03100   -9.45600  81.85300 1.000 17.04530 ? 501 HOH A O   1 
HETATM 2183 O  O   . HOH D 3 .   ? -16.82700 -7.66100  75.91500 1.000 37.28378 ? 502 HOH A O   1 
HETATM 2184 O  O   . HOH D 3 .   ? -2.65100  -13.92800 75.76400 1.000 18.18754 ? 503 HOH A O   1 
HETATM 2185 O  O   A HOH D 3 .   ? -17.43300 10.55000  72.89600 0.710 22.76378 ? 504 HOH A O   1 
HETATM 2186 O  O   B HOH D 3 .   ? -16.55000 9.74200   71.73500 0.290 16.20378 ? 504 HOH A O   1 
HETATM 2187 O  O   . HOH D 3 .   ? -12.10700 -9.70400  80.15200 1.000 48.24378 ? 505 HOH A O   1 
HETATM 2188 O  O   A HOH D 3 .   ? -0.30600  -6.98400  58.43800 0.750 13.52646 ? 506 HOH A O   1 
HETATM 2189 O  O   B HOH D 3 .   ? -0.24400  -7.53300  57.33800 0.250 11.62378 ? 506 HOH A O   1 
HETATM 2190 O  O   . HOH D 3 .   ? -4.26600  8.65300   57.10200 1.000 48.20378 ? 507 HOH A O   1 
HETATM 2191 O  O   . HOH D 3 .   ? -16.20700 10.88600  77.11500 1.000 16.28468 ? 508 HOH A O   1 
HETATM 2192 O  O   . HOH D 3 .   ? 8.24500   -4.18700  80.36600 1.000 22.18378 ? 509 HOH A O   1 
HETATM 2193 O  O   . HOH D 3 .   ? -9.80600  -13.28100 76.26300 1.000 16.99003 ? 510 HOH A O   1 
HETATM 2194 O  O   . HOH D 3 .   ? -20.27800 3.78100   74.57400 1.000 51.25378 ? 511 HOH A O   1 
HETATM 2195 O  O   . HOH D 3 .   ? 6.47800   2.59300   84.20400 1.000 14.80556 ? 512 HOH A O   1 
HETATM 2196 O  O   A HOH D 3 .   ? 2.35500   -6.07500  58.43500 0.780 8.33899  ? 513 HOH A O   1 
HETATM 2197 O  O   B HOH D 3 .   ? 1.71000   -5.74200  58.22600 0.220 10.50378 ? 513 HOH A O   1 
HETATM 2198 O  O   . HOH D 3 .   ? 1.11100   9.97100   58.49800 1.000 31.08378 ? 514 HOH A O   1 
HETATM 2199 O  O   B HOH D 3 .   ? -4.13300  -3.81100  87.40500 0.880 31.01378 ? 515 HOH A O   1 
HETATM 2200 O  O   . HOH D 3 .   ? -17.28600 2.23800   82.31200 1.000 52.65378 ? 516 HOH A O   1 
HETATM 2201 O  O   . HOH D 3 .   ? -1.98900  18.20100  71.11900 1.000 9.21278  ? 517 HOH A O   1 
HETATM 2202 O  O   A HOH D 3 .   ? -19.22500 4.21100   79.12200 0.440 19.38378 ? 518 HOH A O   1 
HETATM 2203 O  O   B HOH D 3 .   ? -18.93800 3.41600   80.89900 0.560 24.19378 ? 518 HOH A O   1 
HETATM 2204 O  O   . HOH D 3 .   ? -15.14000 3.86700   84.34400 1.000 33.71378 ? 519 HOH A O   1 
HETATM 2205 O  O   . HOH D 3 .   ? 3.31200   -8.49200  83.02600 1.000 32.28378 ? 520 HOH A O   1 
HETATM 2206 O  O   A HOH D 3 .   ? -4.36000  13.30400  59.38400 0.570 21.19378 ? 521 HOH A O   1 
HETATM 2207 O  O   . HOH D 3 .   ? -6.09400  -14.39900 77.71500 1.000 13.48172 ? 522 HOH A O   1 
HETATM 2208 O  O   . HOH D 3 .   ? -7.80100  17.92900  74.66900 1.000 21.88378 ? 523 HOH A O   1 
HETATM 2209 O  O   . HOH D 3 .   ? -6.14000  -15.61500 69.79500 1.000 9.87076  ? 524 HOH A O   1 
HETATM 2210 O  O   . HOH D 3 .   ? -19.19700 8.69500   76.61200 1.000 41.48378 ? 525 HOH A O   1 
HETATM 2211 O  O   . HOH D 3 .   ? -8.17900  -4.93500  55.84700 1.000 36.81378 ? 526 HOH A O   1 
HETATM 2212 O  O   . HOH D 3 .   ? -9.95600  13.15800  60.14800 1.000 19.64824 ? 527 HOH A O   1 
HETATM 2213 O  O   . HOH D 3 .   ? 3.08300   11.49200  59.51800 1.000 17.98489 ? 528 HOH A O   1 
HETATM 2214 O  O   . HOH D 3 .   ? -8.47600  -15.52900 71.25600 1.000 13.46856 ? 529 HOH A O   1 
HETATM 2215 O  O   . HOH D 3 .   ? -18.52400 7.93200   79.30400 1.000 27.08378 ? 530 HOH A O   1 
HETATM 2216 O  O   A HOH D 3 .   ? -7.25200  13.30700  59.00600 0.430 37.72378 ? 531 HOH A O   1 
HETATM 2217 O  O   B HOH D 3 .   ? -6.66200  14.78300  58.72100 0.570 42.88378 ? 531 HOH A O   1 
HETATM 2218 O  O   A HOH D 3 .   ? 3.41300   2.44500   87.41100 0.600 15.39510 ? 532 HOH A O   1 
HETATM 2219 O  O   B HOH D 3 .   ? 2.47300   1.89100   87.51600 0.400 17.01378 ? 532 HOH A O   1 
HETATM 2220 O  O   . HOH D 3 .   ? -5.76300  -0.63700  54.09900 1.000 46.07378 ? 533 HOH A O   1 
HETATM 2221 O  O   . HOH D 3 .   ? -11.00500 -7.94200  57.96700 1.000 24.33378 ? 534 HOH A O   1 
HETATM 2222 O  O   . HOH D 3 .   ? 1.48900   13.70200  60.20700 1.000 21.94378 ? 535 HOH A O   1 
HETATM 2223 O  O   . HOH D 3 .   ? -11.09600 -5.30400  56.40200 1.000 43.68378 ? 536 HOH A O   1 
HETATM 2224 O  O   . HOH D 3 .   ? -6.42900  16.97700  80.03100 1.000 11.13933 ? 537 HOH A O   1 
HETATM 2225 O  O   . HOH D 3 .   ? -3.09600  16.88100  62.81400 1.000 24.48830 ? 538 HOH A O   1 
HETATM 2226 O  O   B HOH D 3 .   ? 5.30200   -6.47000  58.79900 0.640 14.44236 ? 539 HOH A O   1 
HETATM 2227 O  O   C HOH D 3 .   ? 4.16000   -6.39400  58.55100 0.360 10.28378 ? 539 HOH A O   1 
HETATM 2228 O  O   . HOH D 3 .   ? -17.34000 10.55800  79.69400 1.000 32.17378 ? 540 HOH A O   1 
HETATM 2229 O  O   B HOH D 3 .   ? 5.07400   1.46100   86.93400 0.450 28.34378 ? 541 HOH A O   1 
HETATM 2230 O  O   . HOH D 3 .   ? -5.88300  -4.36200  54.59700 1.000 33.16378 ? 542 HOH A O   1 
HETATM 2231 O  O   . HOH D 3 .   ? 1.87700   -14.97600 75.45700 1.000 18.45336 ? 543 HOH A O   1 
HETATM 2232 O  O   . HOH D 3 .   ? 1.02700   -10.32500 59.03500 1.000 10.39187 ? 544 HOH A O   1 
HETATM 2233 O  O   A HOH D 3 .   ? 2.09800   -13.23100 79.80100 0.840 19.62193 ? 545 HOH A O   1 
HETATM 2234 O  O   B HOH D 3 .   ? 1.67500   -14.04400 79.62900 0.160 16.62378 ? 545 HOH A O   1 
HETATM 2235 O  O   . HOH D 3 .   ? -7.03400  1.87400   53.72200 1.000 51.76378 ? 546 HOH A O   1 
HETATM 2236 O  O   . HOH D 3 .   ? -5.75500  7.38700   54.60600 1.000 51.40378 ? 547 HOH A O   1 
HETATM 2237 O  O   . HOH D 3 .   ? -8.25400  -15.62700 76.31300 1.000 17.63484 ? 548 HOH A O   1 
HETATM 2238 O  O   . HOH D 3 .   ? 2.44000   -4.64100  55.91700 1.000 13.89229 ? 549 HOH A O   1 
HETATM 2239 O  O   . HOH D 3 .   ? -9.85700  18.06200  76.04200 1.000 33.23378 ? 550 HOH A O   1 
HETATM 2240 O  O   . HOH D 3 .   ? 1.92400   -12.01700 82.08800 1.000 23.49378 ? 551 HOH A O   1 
HETATM 2241 O  O   . HOH D 3 .   ? -3.49100  -0.41200  53.46500 1.000 24.81378 ? 552 HOH A O   1 
HETATM 2242 O  O   . HOH D 3 .   ? 12.36200  -4.01900  76.71100 1.000 23.94378 ? 553 HOH A O   1 
HETATM 2243 O  O   . HOH D 3 .   ? -6.95000  18.47100  77.89600 1.000 18.20597 ? 554 HOH A O   1 
HETATM 2244 O  O   . HOH D 3 .   ? 4.82500   -7.23400  85.05500 1.000 38.43378 ? 555 HOH A O   1 
HETATM 2245 O  O   A HOH D 3 .   ? -5.78100  19.60700  74.41100 0.710 19.57981 ? 556 HOH A O   1 
HETATM 2246 O  O   B HOH D 3 .   ? -6.50500  20.27000  74.36200 0.290 11.56378 ? 556 HOH A O   1 
HETATM 2247 O  O   A HOH D 3 .   ? 4.45600   -13.02200 78.99200 0.680 18.56917 ? 557 HOH A O   1 
HETATM 2248 O  O   B HOH D 3 .   ? 3.51000   -12.80700 79.55700 0.320 14.59378 ? 557 HOH A O   1 
HETATM 2249 O  O   A HOH D 3 .   ? 13.49700  4.53600   76.16900 0.530 19.31926 ? 558 HOH A O   1 
HETATM 2250 O  O   . HOH D 3 .   ? 3.24400   -8.84500  58.14300 1.000 13.38434 ? 559 HOH A O   1 
HETATM 2251 O  O   . HOH D 3 .   ? -4.46200  16.09100  60.21400 1.000 30.76378 ? 560 HOH A O   1 
HETATM 2252 O  O   . HOH D 3 .   ? -1.95600  -4.34800  89.09400 1.000 24.56378 ? 561 HOH A O   1 
HETATM 2253 O  O   A HOH D 3 .   ? -4.53500  -7.35400  55.09400 0.710 16.53734 ? 562 HOH A O   1 
HETATM 2254 O  O   B HOH D 3 .   ? -3.35100  -7.99200  55.13200 0.290 12.97378 ? 562 HOH A O   1 
HETATM 2255 O  O   . HOH D 3 .   ? -12.30900 17.82000  75.19000 1.000 14.26865 ? 563 HOH A O   1 
HETATM 2256 O  O   . HOH D 3 .   ? 12.02300  9.89300   75.28600 1.000 15.32404 ? 564 HOH A O   1 
HETATM 2257 O  O   B HOH D 3 .   ? -4.78500  19.99600  70.25800 1.000 14.58185 ? 565 HOH A O   1 
HETATM 2258 O  O   A HOH D 3 .   ? -0.27300  -7.84700  55.90000 0.750 22.16378 ? 566 HOH A O   1 
HETATM 2259 O  O   B HOH D 3 .   ? -0.76100  -7.39800  54.16900 0.250 21.17378 ? 566 HOH A O   1 
HETATM 2260 O  O   A HOH D 3 .   ? -1.88600  6.56100   53.80700 0.620 19.34821 ? 567 HOH A O   1 
HETATM 2261 O  O   B HOH D 3 .   ? -3.09800  7.26100   54.38800 0.380 18.76378 ? 567 HOH A O   1 
HETATM 2262 O  O   . HOH D 3 .   ? 13.45800  2.39600   77.74300 1.000 20.21673 ? 568 HOH A O   1 
HETATM 2263 O  O   . HOH D 3 .   ? -17.45500 13.35800  77.44900 1.000 22.41378 ? 569 HOH A O   1 
HETATM 2264 O  O   . HOH D 3 .   ? 10.93900  -2.51200  81.84000 1.000 30.93378 ? 570 HOH A O   1 
HETATM 2265 O  O   . HOH D 3 .   ? -3.11400  16.75300  82.66000 1.000 11.03932 ? 571 HOH A O   1 
HETATM 2266 O  O   A HOH D 3 .   ? 1.00300   -15.19200 78.89500 0.750 20.28378 ? 572 HOH A O   1 
HETATM 2267 O  O   B HOH D 3 .   ? 0.89500   -16.24200 78.58500 0.250 14.84378 ? 572 HOH A O   1 
HETATM 2268 O  O   . HOH D 3 .   ? -7.99100  4.72600   89.88200 1.000 11.53938 ? 573 HOH A O   1 
HETATM 2269 O  O   A HOH D 3 .   ? -4.15700  -17.44700 69.13400 0.800 12.25262 ? 574 HOH A O   1 
HETATM 2270 O  O   B HOH D 3 .   ? -3.31700  -18.32300 68.46700 0.200 18.02378 ? 574 HOH A O   1 
HETATM 2271 O  O   . HOH D 3 .   ? 9.78500   -10.56500 76.00600 1.000 8.33110  ? 575 HOH A O   1 
HETATM 2272 O  O   . HOH D 3 .   ? -5.05200  18.56600  63.30900 1.000 23.19378 ? 576 HOH A O   1 
HETATM 2273 O  O   B HOH D 3 .   ? 2.09900   9.77000   55.63200 1.000 43.32378 ? 577 HOH A O   1 
HETATM 2274 O  O   . HOH D 3 .   ? -15.65900 3.19700   86.85200 1.000 34.33378 ? 578 HOH A O   1 
HETATM 2275 O  O   A HOH D 3 .   ? 12.09500  -5.37600  78.86600 0.530 25.89378 ? 579 HOH A O   1 
HETATM 2276 O  O   B HOH D 3 .   ? 10.70000  -4.24800  79.80500 0.470 32.02378 ? 579 HOH A O   1 
HETATM 2277 O  O   . HOH D 3 .   ? 2.28600   -1.54000  89.37800 1.000 36.15378 ? 580 HOH A O   1 
HETATM 2278 O  O   . HOH D 3 .   ? -4.57200  20.04600  76.35800 1.000 20.45097 ? 581 HOH A O   1 
HETATM 2279 O  O   . HOH D 3 .   ? 8.41300   -7.52400  83.01700 1.000 31.51378 ? 582 HOH A O   1 
HETATM 2280 O  O   B HOH D 3 .   ? 8.25800   8.74700   58.88400 1.000 20.64047 ? 583 HOH A O   1 
HETATM 2281 O  O   . HOH D 3 .   ? -16.78300 15.64700  75.58400 1.000 12.92375 ? 584 HOH A O   1 
HETATM 2282 O  O   . HOH D 3 .   ? -7.11400  18.09100  62.18600 1.000 23.24378 ? 585 HOH A O   1 
HETATM 2283 O  O   . HOH D 3 .   ? -4.87200  -16.88000 77.90400 1.000 24.04378 ? 586 HOH A O   1 
HETATM 2284 O  O   . HOH D 3 .   ? 0.48600   -5.43600  54.08500 1.000 24.36378 ? 587 HOH A O   1 
HETATM 2285 O  O   A HOH D 3 .   ? 15.13600  3.33000   71.14000 0.600 19.58508 ? 588 HOH A O   1 
HETATM 2286 O  O   B HOH D 3 .   ? 15.18900  3.83500   72.31900 0.400 14.01378 ? 588 HOH A O   1 
HETATM 2287 O  O   A HOH D 3 .   ? -8.29300  20.17200  75.01200 0.650 16.58472 ? 589 HOH A O   1 
HETATM 2288 O  O   B HOH D 3 .   ? -9.12900  20.03600  75.54000 0.350 19.24378 ? 589 HOH A O   1 
HETATM 2289 O  O   . HOH D 3 .   ? -3.44300  2.00700   52.10700 1.000 19.46138 ? 590 HOH A O   1 
HETATM 2290 O  O   . HOH D 3 .   ? -5.78900  3.43600   52.22500 1.000 41.64378 ? 591 HOH A O   1 
HETATM 2291 O  O   A HOH D 3 .   ? -11.60100 19.43300  72.92400 0.650 8.74167  ? 592 HOH A O   1 
HETATM 2292 O  O   B HOH D 3 .   ? -10.74000 19.01800  73.52200 0.350 11.93378 ? 592 HOH A O   1 
HETATM 2293 O  O   . HOH D 3 .   ? 11.72600  9.83700   64.07800 1.000 15.15823 ? 593 HOH A O   1 
HETATM 2294 O  O   A HOH D 3 .   ? 5.99100   15.85700  62.09100 0.630 20.60099 ? 594 HOH A O   1 
HETATM 2295 O  O   B HOH D 3 .   ? 7.25200   15.02300  63.44900 0.370 8.44378  ? 594 HOH A O   1 
HETATM 2296 O  O   . HOH D 3 .   ? -2.73300  -2.51800  52.41200 1.000 36.76378 ? 595 HOH A O   1 
HETATM 2297 O  O   A HOH D 3 .   ? 15.22500  3.10600   73.47500 0.350 18.70378 ? 596 HOH A O   1 
HETATM 2298 O  O   B HOH D 3 .   ? 14.80000  3.42700   74.75600 0.650 28.40378 ? 596 HOH A O   1 
HETATM 2299 O  O   . HOH D 3 .   ? 3.20600   15.93600  60.73600 1.000 30.76378 ? 597 HOH A O   1 
HETATM 2300 O  O   . HOH D 3 .   ? -20.70100 11.06800  76.60900 1.000 39.83378 ? 598 HOH A O   1 
HETATM 2301 O  O   A HOH D 3 .   ? 3.41600   -15.33200 78.32000 0.740 21.54378 ? 599 HOH A O   1 
HETATM 2302 O  O   B HOH D 3 .   ? 4.43500   -14.71200 78.93600 0.260 8.20378  ? 599 HOH A O   1 
HETATM 2303 O  O   . HOH D 3 .   ? -1.22800  -4.34900  52.98500 1.000 39.18378 ? 600 HOH A O   1 
HETATM 2304 O  O   B HOH D 3 .   ? -14.60700 1.53500   88.36400 0.590 21.63532 ? 601 HOH A O   1 
HETATM 2305 O  O   C HOH D 3 .   ? -14.01100 0.98200   87.09900 0.410 20.62378 ? 601 HOH A O   1 
HETATM 2306 O  O   A HOH D 3 .   ? 0.29600   -17.16700 66.83900 0.690 9.76022  ? 602 HOH A O   1 
HETATM 2307 O  O   B HOH D 3 .   ? 0.65500   -18.09800 66.53600 0.310 10.19378 ? 602 HOH A O   1 
HETATM 2308 O  O   . HOH D 3 .   ? -5.62400  17.81600  82.53700 1.000 11.63413 ? 603 HOH A O   1 
HETATM 2309 O  O   A HOH D 3 .   ? -5.82300  1.41300   91.28600 0.690 20.13778 ? 604 HOH A O   1 
HETATM 2310 O  O   B HOH D 3 .   ? -6.02600  2.47300   91.92000 0.310 19.44378 ? 604 HOH A O   1 
HETATM 2311 O  O   . HOH D 3 .   ? 4.51700   -15.70800 75.96100 1.000 19.86669 ? 605 HOH A O   1 
HETATM 2312 O  O   . HOH D 3 .   ? -14.51800 6.03800   87.92700 1.000 22.33378 ? 606 HOH A O   1 
HETATM 2313 O  O   . HOH D 3 .   ? 4.68400   11.87100  57.20400 1.000 29.04378 ? 607 HOH A O   1 
HETATM 2314 O  O   A HOH D 3 .   ? -1.38900  -18.09600 68.69200 0.530 15.25561 ? 608 HOH A O   1 
HETATM 2315 O  O   B HOH D 3 .   ? -0.54400  -19.74900 67.04700 0.470 19.42378 ? 608 HOH A O   1 
HETATM 2316 O  O   . HOH D 3 .   ? 8.94600   1.93200   86.65200 1.000 31.60378 ? 609 HOH A O   1 
HETATM 2317 O  O   A HOH D 3 .   ? 0.16600   8.27500   53.33800 0.630 24.30378 ? 610 HOH A O   1 
HETATM 2318 O  O   B HOH D 3 .   ? -0.72700  8.95900   54.01300 0.370 20.53378 ? 610 HOH A O   1 
HETATM 2319 O  O   A HOH D 3 .   ? 5.10000   -5.27200  55.24300 0.690 19.44822 ? 611 HOH A O   1 
HETATM 2320 O  O   B HOH D 3 .   ? 4.52400   -5.86900  55.05100 0.310 21.39378 ? 611 HOH A O   1 
HETATM 2321 O  O   . HOH D 3 .   ? -4.08600  -10.15900 55.12600 1.000 33.48378 ? 612 HOH A O   1 
HETATM 2322 O  O   . HOH D 3 .   ? 10.64200  -6.78200  82.31700 1.000 44.53378 ? 613 HOH A O   1 
HETATM 2323 O  O   . HOH D 3 .   ? -2.53700  -17.31200 78.84700 1.000 29.23378 ? 614 HOH A O   1 
HETATM 2324 O  O   . HOH D 3 .   ? 10.69200  7.88700   59.69600 1.000 22.53806 ? 615 HOH A O   1 
HETATM 2325 O  O   A HOH D 3 .   ? 15.73400  3.65100   68.88000 0.330 16.55378 ? 616 HOH A O   1 
HETATM 2326 O  O   B HOH D 3 .   ? 15.90300  4.78300   70.35400 0.670 38.26378 ? 616 HOH A O   1 
HETATM 2327 O  O   . HOH D 3 .   ? 7.30700   -6.84600  57.18500 1.000 20.19305 ? 617 HOH A O   1 
HETATM 2328 O  O   . HOH D 3 .   ? 15.10700  3.66500   65.95600 1.000 19.89564 ? 618 HOH A O   1 
HETATM 2329 O  O   . HOH D 3 .   ? 5.18800   -1.80300  53.95700 1.000 10.64980 ? 619 HOH A O   1 
HETATM 2330 O  O   A HOH D 3 .   ? -0.36700  -18.11100 75.59700 0.640 17.46114 ? 620 HOH A O   1 
HETATM 2331 O  O   B HOH D 3 .   ? -1.54400  -18.24900 75.62200 0.360 16.41378 ? 620 HOH A O   1 
HETATM 2332 O  O   . HOH D 3 .   ? -4.37800  -18.33300 66.29800 1.000 16.92950 ? 621 HOH A O   1 
HETATM 2333 O  O   . HOH D 3 .   ? 6.40100   -11.93200 82.68900 1.000 22.61378 ? 622 HOH A O   1 
HETATM 2334 O  O   . HOH D 3 .   ? -1.50900  -0.39700  91.74400 1.000 47.00378 ? 623 HOH A O   1 
HETATM 2335 O  O   . HOH D 3 .   ? 6.52300   -13.47100 80.51100 1.000 18.67971 ? 624 HOH A O   1 
HETATM 2336 O  O   A HOH D 3 .   ? -1.67000  -11.81000 56.09900 0.560 25.11378 ? 625 HOH A O   1 
HETATM 2337 O  O   B HOH D 3 .   ? -1.91300  -16.14800 55.99600 0.440 35.47378 ? 625 HOH A O   1 
HETATM 2338 O  O   . HOH D 3 .   ? 15.29200  0.51700   77.93200 1.000 26.13378 ? 626 HOH A O   1 
HETATM 2339 O  O   . HOH D 3 .   ? -17.38300 6.46400   86.56700 1.000 43.52378 ? 627 HOH A O   1 
HETATM 2340 O  O   . HOH D 3 .   ? 13.97900  9.32800   77.19400 1.000 21.55378 ? 628 HOH A O   1 
HETATM 2341 O  O   A HOH D 3 .   ? 5.27900   14.61600  59.03800 0.580 34.04378 ? 629 HOH A O   1 
HETATM 2342 O  O   B HOH D 3 .   ? 5.21500   14.71000  57.40400 0.420 23.43378 ? 629 HOH A O   1 
HETATM 2343 O  O   A HOH D 3 .   ? 12.10800  -0.27500  84.03400 0.380 16.18378 ? 630 HOH A O   1 
HETATM 2344 O  O   B HOH D 3 .   ? 12.63600  -4.04800  83.63400 0.620 32.12378 ? 630 HOH A O   1 
HETATM 2345 O  O   . HOH D 3 .   ? -2.29600  6.01400   51.58800 1.000 48.22378 ? 631 HOH A O   1 
HETATM 2346 O  O   . HOH D 3 .   ? -8.60300  -17.64400 78.28500 1.000 27.55378 ? 632 HOH A O   1 
HETATM 2347 O  O   . HOH D 3 .   ? 12.79600  -7.93800  78.54200 1.000 17.61905 ? 633 HOH A O   1 
HETATM 2348 O  O   A HOH D 3 .   ? 15.23500  6.46300   76.69800 0.650 27.11378 ? 634 HOH A O   1 
HETATM 2349 O  O   B HOH D 3 .   ? 15.18600  5.21100   75.89300 0.350 23.10378 ? 634 HOH A O   1 
HETATM 2350 O  O   . HOH D 3 .   ? 4.72300   -16.27700 65.78600 1.000 9.16278  ? 635 HOH A O   1 
HETATM 2351 O  O   . HOH D 3 .   ? 0.55700   -11.17400 55.80200 1.000 26.69378 ? 636 HOH A O   1 
HETATM 2352 O  O   . HOH D 3 .   ? -8.89300  1.69700   91.78800 1.000 43.18378 ? 637 HOH A O   1 
HETATM 2353 O  O   . HOH D 3 .   ? 8.69400   -12.92200 79.12500 1.000 13.52909 ? 638 HOH A O   1 
HETATM 2354 O  O   A HOH D 3 .   ? 3.68900   -9.04100  55.48200 0.710 33.06378 ? 639 HOH A O   1 
HETATM 2355 O  O   B HOH D 3 .   ? 1.90500   -9.20900  55.70000 0.290 18.38378 ? 639 HOH A O   1 
HETATM 2356 O  O   A HOH D 3 .   ? 15.50500  -5.01400  72.83100 0.750 21.59321 ? 640 HOH A O   1 
HETATM 2357 O  O   B HOH D 3 .   ? 17.04900  -4.05200  71.06100 0.250 21.28378 ? 640 HOH A O   1 
HETATM 2358 O  O   . HOH D 3 .   ? -11.67000 5.01400   90.71800 1.000 19.57718 ? 641 HOH A O   1 
HETATM 2359 O  O   . HOH D 3 .   ? 3.45400   19.11300  63.63600 1.000 18.95079 ? 642 HOH A O   1 
HETATM 2360 O  O   . HOH D 3 .   ? 8.18400   9.02600   56.69100 1.000 37.08378 ? 643 HOH A O   1 
HETATM 2361 O  O   A HOH D 3 .   ? -5.08600  -18.96100 76.22700 0.640 22.77378 ? 644 HOH A O   1 
HETATM 2362 O  O   B HOH D 3 .   ? -3.81100  -19.94600 75.66500 0.360 25.25378 ? 644 HOH A O   1 
HETATM 2363 O  O   A HOH D 3 .   ? 7.22900   10.98700  56.99400 1.000 16.85317 ? 645 HOH A O   1 
HETATM 2364 O  O   . HOH D 3 .   ? 11.87500  -10.42800 77.73900 1.000 9.93392  ? 646 HOH A O   1 
HETATM 2365 O  O   . HOH D 3 .   ? -5.73500  18.34900  58.90500 1.000 41.45378 ? 647 HOH A O   1 
HETATM 2366 O  O   . HOH D 3 .   ? 12.20700  9.74300   60.99000 1.000 13.35275 ? 648 HOH A O   1 
HETATM 2367 O  O   . HOH D 3 .   ? -10.40000 21.77300  73.76300 1.000 15.87148 ? 649 HOH A O   1 
HETATM 2368 O  O   A HOH D 3 .   ? -10.60100 21.22500  76.59200 0.590 12.37106 ? 650 HOH A O   1 
HETATM 2369 O  O   B HOH D 3 .   ? -10.79000 22.47100  76.46300 0.410 17.43378 ? 650 HOH A O   1 
HETATM 2370 O  O   . HOH D 3 .   ? 15.25800  3.59500   63.15700 1.000 19.09291 ? 651 HOH A O   1 
HETATM 2371 O  O   . HOH D 3 .   ? -6.96500  -18.98200 65.42400 1.000 10.69191 ? 652 HOH A O   1 
HETATM 2372 O  O   . HOH D 3 .   ? -5.66800  22.54000  68.27900 1.000 19.89301 ? 653 HOH A O   1 
HETATM 2373 O  O   . HOH D 3 .   ? -0.72200  -18.57800 78.43400 1.000 27.96378 ? 654 HOH A O   1 
HETATM 2374 O  O   . HOH D 3 .   ? -0.52000  -3.14000  92.23700 1.000 55.69378 ? 655 HOH A O   1 
HETATM 2375 O  O   . HOH D 3 .   ? 4.02100   -2.20700  91.12800 1.000 48.55378 ? 656 HOH A O   1 
HETATM 2376 O  O   A HOH D 3 .   ? 12.46000  -8.16500  81.33400 0.710 37.79378 ? 657 HOH A O   1 
HETATM 2377 O  O   B HOH D 3 .   ? 11.93000  -6.36700  80.46700 0.290 19.05378 ? 657 HOH A O   1 
HETATM 2378 O  O   . HOH D 3 .   ? -8.24900  -12.17500 55.09400 1.000 28.65378 ? 658 HOH A O   1 
HETATM 2379 O  O   . HOH D 3 .   ? -16.33800 7.86100   88.33400 1.000 24.39378 ? 659 HOH A O   1 
HETATM 2380 O  O   A HOH D 3 .   ? 15.87300  -5.44200  75.50100 0.480 18.72378 ? 660 HOH A O   1 
HETATM 2381 O  O   B HOH D 3 .   ? 14.65800  -4.73400  75.70400 0.520 18.77972 ? 660 HOH A O   1 
HETATM 2382 O  O   . HOH D 3 .   ? 10.18000  7.11200   86.77400 1.000 17.90330 ? 661 HOH A O   1 
HETATM 2383 O  O   A HOH D 3 .   ? -6.81800  21.79700  64.64100 0.380 15.87378 ? 662 HOH A O   1 
HETATM 2384 O  O   B HOH D 3 .   ? -5.59900  22.46000  65.30000 0.620 23.16378 ? 662 HOH A O   1 
HETATM 2385 O  O   A HOH D 3 .   ? -4.17300  19.82800  87.29000 0.560 20.45378 ? 663 HOH A O   1 
HETATM 2386 O  O   B HOH D 3 .   ? -2.17300  18.48900  84.86000 0.440 15.74378 ? 663 HOH A O   1 
HETATM 2387 O  O   . HOH D 3 .   ? 0.23100   22.66400  71.85100 1.000 12.37895 ? 664 HOH A O   1 
HETATM 2388 O  O   . HOH D 3 .   ? 7.35000   -9.70000  86.11800 1.000 33.22378 ? 665 HOH A O   1 
HETATM 2389 O  O   A HOH D 3 .   ? -7.86100  4.83600   92.73700 0.550 27.60378 ? 666 HOH A O   1 
HETATM 2390 O  O   B HOH D 3 .   ? -7.95500  6.27000   92.58500 0.450 33.85378 ? 666 HOH A O   1 
HETATM 2391 O  O   . HOH D 3 .   ? -7.58200  22.77200  74.07800 1.000 30.57378 ? 667 HOH A O   1 
HETATM 2392 O  O   A HOH D 3 .   ? -8.57300  11.83500  90.19800 0.670 24.51378 ? 668 HOH A O   1 
HETATM 2393 O  O   B HOH D 3 .   ? -8.56400  11.00800  91.27300 0.330 14.70378 ? 668 HOH A O   1 
HETATM 2394 O  O   . HOH D 3 .   ? -1.50500  20.24000  60.92800 1.000 26.00378 ? 669 HOH A O   1 
HETATM 2395 O  O   A HOH D 3 .   ? 5.72200   18.59200  62.28500 0.770 19.70878 ? 670 HOH A O   1 
HETATM 2396 O  O   B HOH D 3 .   ? 5.68700   17.09000  62.51100 0.230 15.26378 ? 670 HOH A O   1 
HETATM 2397 O  O   . HOH D 3 .   ? 4.59200   21.53900  70.60100 1.000 13.98178 ? 671 HOH A O   1 
HETATM 2398 O  O   A HOH D 3 .   ? -7.44300  7.63200   92.42900 0.380 29.15378 ? 672 HOH A O   1 
HETATM 2399 O  O   B HOH D 3 .   ? -7.74800  9.18700   92.24300 0.620 28.89378 ? 672 HOH A O   1 
HETATM 2400 O  O   . HOH D 3 .   ? -7.94700  22.42400  76.96500 1.000 21.95378 ? 673 HOH A O   1 
HETATM 2401 O  O   . HOH D 3 .   ? 11.10100  -11.89400 79.92000 1.000 13.59752 ? 674 HOH A O   1 
HETATM 2402 O  O   . HOH D 3 .   ? 8.61700   -11.18900 84.17800 1.000 38.21378 ? 675 HOH A O   1 
HETATM 2403 O  O   A HOH D 3 .   ? 13.80000  6.40200   83.36200 0.500 24.67378 ? 676 HOH A O   1 
HETATM 2404 O  O   B HOH D 3 .   ? 14.04000  8.00300   83.74300 0.500 25.35378 ? 676 HOH A O   1 
HETATM 2405 O  O   . HOH D 3 .   ? -18.69500 8.68100   86.65300 1.000 27.09378 ? 677 HOH A O   1 
HETATM 2406 O  O   A HOH D 3 .   ? -14.12300 14.11500  86.73900 0.640 18.89026 ? 678 HOH A O   1 
HETATM 2407 O  O   B HOH D 3 .   ? -14.69500 12.80400  88.14000 0.360 17.42378 ? 678 HOH A O   1 
HETATM 2408 O  O   A HOH D 3 .   ? 16.79300  5.98400   66.61900 0.420 13.30378 ? 679 HOH A O   1 
HETATM 2409 O  O   B HOH D 3 .   ? 17.12300  5.99000   68.02500 0.580 23.17378 ? 679 HOH A O   1 
HETATM 2410 O  O   . HOH D 3 .   ? 17.37900  6.09300   72.99500 1.000 37.21378 ? 680 HOH A O   1 
HETATM 2411 O  O   . HOH D 3 .   ? 3.21100   -1.03800  50.90000 1.000 47.47378 ? 681 HOH A O   1 
HETATM 2412 O  O   B HOH D 3 .   ? -5.83300  20.34700  83.02800 0.920 24.66378 ? 682 HOH A O   1 
HETATM 2413 O  O   . HOH D 3 .   ? -14.86900 9.85600   89.16400 1.000 24.64378 ? 683 HOH A O   1 
HETATM 2414 O  O   . HOH D 3 .   ? -2.90200  2.85300   93.69600 1.000 27.10378 ? 684 HOH A O   1 
HETATM 2415 O  O   . HOH D 3 .   ? 11.12600  -10.49700 82.25900 1.000 28.98378 ? 685 HOH A O   1 
HETATM 2416 O  O   A HOH D 3 .   ? -2.39300  -20.20400 76.36000 0.540 27.09378 ? 686 HOH A O   1 
HETATM 2417 O  O   . HOH D 3 .   ? 15.27300  -7.49600  77.42000 1.000 26.82378 ? 687 HOH A O   1 
HETATM 2418 O  O   . HOH D 3 .   ? 3.88200   22.13300  73.18100 1.000 13.38434 ? 688 HOH A O   1 
HETATM 2419 O  O   . HOH D 3 .   ? -1.91100  -8.57200  51.77200 1.000 40.08378 ? 689 HOH A O   1 
HETATM 2420 O  O   . HOH D 3 .   ? 16.57400  1.93800   79.72400 1.000 38.20378 ? 690 HOH A O   1 
HETATM 2421 O  O   A HOH D 3 .   ? 13.57000  1.93000   85.17200 0.450 24.29378 ? 691 HOH A O   1 
HETATM 2422 O  O   B HOH D 3 .   ? 15.71300  2.78800   85.55700 0.550 29.45378 ? 691 HOH A O   1 
HETATM 2423 O  O   . HOH D 3 .   ? 2.46800   -0.44800  92.85100 1.000 49.12378 ? 692 HOH A O   1 
HETATM 2424 O  O   . HOH D 3 .   ? 4.61700   -17.49000 79.50700 1.000 14.72134 ? 693 HOH A O   1 
HETATM 2425 O  O   A HOH D 3 .   ? -3.17800  -18.94500 62.07000 1.000 14.41341 ? 694 HOH A O   1 
HETATM 2426 O  O   A HOH D 3 .   ? 3.13200   21.59400  64.95700 0.590 20.84378 ? 695 HOH A O   1 
HETATM 2427 O  O   B HOH D 3 .   ? 2.80800   22.95500  66.03200 0.410 18.13378 ? 695 HOH A O   1 
HETATM 2428 O  O   B HOH D 3 .   ? -7.57500  22.04600  63.29600 0.670 30.02378 ? 696 HOH A O   1 
HETATM 2429 O  O   . HOH D 3 .   ? -1.77500  3.09100   49.29200 1.000 33.24378 ? 697 HOH A O   1 
HETATM 2430 O  O   . HOH D 3 .   ? -7.57000  23.71800  71.96900 1.000 30.59378 ? 698 HOH A O   1 
HETATM 2431 O  O   . HOH D 3 .   ? 5.68000   -18.05600 76.99300 1.000 24.70378 ? 699 HOH A O   1 
HETATM 2432 O  O   . HOH D 3 .   ? 18.33600  0.99700   71.98300 1.000 45.48378 ? 700 HOH A O   1 
HETATM 2433 O  O   . HOH D 3 .   ? -2.97700  -20.49500 65.86200 1.000 23.88378 ? 701 HOH A O   1 
HETATM 2434 O  O   . HOH D 3 .   ? -21.30400 12.86000  81.24000 1.000 53.87378 ? 702 HOH A O   1 
HETATM 2435 O  O   A HOH D 3 .   ? -0.39300  -20.04600 65.42000 0.550 24.92378 ? 703 HOH A O   1 
HETATM 2436 O  O   B HOH D 3 .   ? 0.47500   -21.10900 65.08400 0.450 22.41378 ? 703 HOH A O   1 
HETATM 2437 O  O   . HOH D 3 .   ? -10.53600 6.38200   92.84000 1.000 36.34378 ? 704 HOH A O   1 
HETATM 2438 O  O   . HOH D 3 .   ? 1.96200   20.15000  60.31900 1.000 38.80378 ? 705 HOH A O   1 
HETATM 2439 O  O   A HOH D 3 .   ? 8.23800   9.94600   54.64800 0.670 14.28444 ? 706 HOH A O   1 
HETATM 2440 O  O   B HOH D 3 .   ? 6.91500   10.49300  53.93600 0.330 15.74378 ? 706 HOH A O   1 
HETATM 2441 O  O   . HOH D 3 .   ? 1.36500   23.39900  69.41300 1.000 17.01635 ? 707 HOH A O   1 
HETATM 2442 O  O   . HOH D 3 .   ? 9.54000   -12.96700 60.67100 1.000 19.82195 ? 708 HOH A O   1 
HETATM 2443 O  O   A HOH D 3 .   ? 8.57100   -15.93800 78.73300 0.430 16.56378 ? 709 HOH A O   1 
HETATM 2444 O  O   B HOH D 3 .   ? 8.99400   -17.32200 79.25800 0.260 13.78378 ? 709 HOH A O   1 
HETATM 2445 O  O   C HOH D 3 .   ? 7.90000   -16.50400 77.18300 0.310 15.79378 ? 709 HOH A O   1 
HETATM 2446 O  O   . HOH D 3 .   ? 8.77500   13.20400  57.10100 1.000 12.59740 ? 710 HOH A O   1 
HETATM 2447 O  O   A HOH D 3 .   ? 17.69000  -4.07900  68.40500 0.550 19.16661 ? 711 HOH A O   1 
HETATM 2448 O  O   B HOH D 3 .   ? 17.56200  -3.76100  67.61600 0.450 13.58378 ? 711 HOH A O   1 
HETATM 2449 O  O   A HOH D 3 .   ? 17.90400  3.03800   66.45300 0.610 18.89815 ? 712 HOH A O   1 
HETATM 2450 O  O   B HOH D 3 .   ? 19.76900  3.62000   66.76700 0.390 15.94378 ? 712 HOH A O   1 
HETATM 2451 O  O   . HOH D 3 .   ? -2.75900  8.14000   49.83400 1.000 42.35378 ? 713 HOH A O   1 
HETATM 2452 O  O   . HOH D 3 .   ? 14.80100  9.90500   81.31700 1.000 26.75378 ? 714 HOH A O   1 
HETATM 2453 O  O   A HOH D 3 .   ? -7.95300  23.76200  67.68800 0.420 12.74378 ? 715 HOH A O   1 
HETATM 2454 O  O   B HOH D 3 .   ? -8.16500  23.49900  66.45100 0.580 21.24378 ? 715 HOH A O   1 
HETATM 2455 O  O   . HOH D 3 .   ? 14.51700  -11.74200 71.83900 1.000 9.02065  ? 716 HOH A O   1 
HETATM 2456 O  O   . HOH D 3 .   ? 5.74700   -11.03200 55.09000 1.000 44.89378 ? 717 HOH A O   1 
HETATM 2457 O  O   A HOH D 3 .   ? -6.85800  14.85100  90.10100 0.590 12.70531 ? 718 HOH A O   1 
HETATM 2458 O  O   B HOH D 3 .   ? -7.22200  13.29400  90.00200 0.410 15.46378 ? 718 HOH A O   1 
HETATM 2459 O  O   . HOH D 3 .   ? 11.33200  17.02500  78.53100 1.000 16.23731 ? 719 HOH A O   1 
HETATM 2460 O  O   A HOH D 3 .   ? -11.48300 18.08100  85.80200 0.630 20.43378 ? 720 HOH A O   1 
HETATM 2461 O  O   B HOH D 3 .   ? -12.00000 16.89500  86.14700 0.370 12.41378 ? 720 HOH A O   1 
HETATM 2462 O  O   . HOH D 3 .   ? 16.39400  10.44700  76.88800 1.000 34.75378 ? 721 HOH A O   1 
HETATM 2463 O  O   A HOH D 3 .   ? 17.44900  -6.16800  73.54800 0.660 39.49378 ? 722 HOH A O   1 
HETATM 2464 O  O   . HOH D 3 .   ? -0.13000  18.20700  87.04200 1.000 19.52981 ? 723 HOH A O   1 
HETATM 2465 O  O   A HOH D 3 .   ? -6.72600  -21.56900 73.44400 1.000 17.25585 ? 724 HOH A O   1 
HETATM 2466 O  O   A HOH D 3 .   ? 4.34500   17.18500  86.32400 0.470 12.25378 ? 725 HOH A O   1 
HETATM 2467 O  O   B HOH D 3 .   ? 5.05600   17.53100  85.11400 0.530 12.97639 ? 725 HOH A O   1 
HETATM 2468 O  O   B HOH D 3 .   ? -3.96400  -17.45300 58.02500 0.480 23.33378 ? 726 HOH A O   1 
HETATM 2469 O  O   A HOH D 3 .   ? 6.17200   -0.47200  50.98300 0.570 24.19378 ? 727 HOH A O   1 
HETATM 2470 O  O   B HOH D 3 .   ? 6.04900   -1.92700  51.47000 0.430 25.41378 ? 727 HOH A O   1 
HETATM 2471 O  O   . HOH D 3 .   ? 0.16800   1.71600   94.37900 1.000 42.61378 ? 728 HOH A O   1 
HETATM 2472 O  O   . HOH D 3 .   ? 14.67000  -5.37900  60.00100 1.000 13.30011 ? 729 HOH A O   1 
HETATM 2473 O  O   . HOH D 3 .   ? 8.20700   18.64600  62.08200 1.000 31.52378 ? 730 HOH A O   1 
HETATM 2474 O  O   . HOH D 3 .   ? 7.63900   7.44900   90.79300 1.000 17.19532 ? 731 HOH A O   1 
HETATM 2475 O  O   . HOH D 3 .   ? -4.07100  23.21100  63.18500 1.000 45.57378 ? 732 HOH A O   1 
HETATM 2476 O  O   A HOH D 3 .   ? 18.22900  -2.43600  66.54800 0.430 15.38378 ? 733 HOH A O   1 
HETATM 2477 O  O   B HOH D 3 .   ? 18.14000  -2.71200  65.09100 0.570 19.00606 ? 733 HOH A O   1 
HETATM 2478 O  O   A HOH D 3 .   ? -0.32800  -20.01200 63.02700 0.670 20.67378 ? 734 HOH A O   1 
HETATM 2479 O  O   B HOH D 3 .   ? -0.88800  -20.67000 62.47800 0.330 10.50378 ? 734 HOH A O   1 
HETATM 2480 O  O   . HOH D 3 .   ? 14.48900  -11.29800 77.27600 1.000 13.74490 ? 735 HOH A O   1 
HETATM 2481 O  O   . HOH D 3 .   ? 0.24200   1.16800   48.62300 1.000 50.45378 ? 736 HOH A O   1 
HETATM 2482 O  O   . HOH D 3 .   ? 3.00700   1.46700   49.35500 1.000 29.51378 ? 737 HOH A O   1 
HETATM 2483 O  O   . HOH D 3 .   ? 18.94600  3.64400   69.12400 1.000 44.92378 ? 738 HOH A O   1 
HETATM 2484 O  O   . HOH D 3 .   ? 10.17900  -11.60200 58.54700 1.000 22.05378 ? 739 HOH A O   1 
HETATM 2485 O  O   A HOH D 3 .   ? 5.20300   -19.98300 72.56700 0.610 22.92378 ? 740 HOH A O   1 
HETATM 2486 O  O   B HOH D 3 .   ? 3.41800   -21.24400 72.00400 0.390 21.17378 ? 740 HOH A O   1 
HETATM 2487 O  O   . HOH D 3 .   ? 12.72100  14.32100  81.65600 1.000 16.16888 ? 741 HOH A O   1 
HETATM 2488 O  O   A HOH D 3 .   ? 1.29900   19.89000  85.16600 0.560 23.11378 ? 742 HOH A O   1 
HETATM 2489 O  O   B HOH D 3 .   ? 1.89200   19.36600  84.72700 0.440 11.59378 ? 742 HOH A O   1 
HETATM 2490 O  O   . HOH D 3 .   ? -4.45000  24.48900  66.78700 1.000 25.79378 ? 743 HOH A O   1 
HETATM 2491 O  O   . HOH D 3 .   ? -1.70300  24.27900  66.41800 1.000 20.02724 ? 744 HOH A O   1 
HETATM 2492 O  O   A HOH D 3 .   ? 0.69700   -15.29500 55.65300 0.230 11.76378 ? 745 HOH A O   1 
HETATM 2493 O  O   B HOH D 3 .   ? 0.14700   -15.13600 54.08800 0.770 40.38378 ? 745 HOH A O   1 
HETATM 2494 O  O   A HOH D 3 .   ? 7.03300   16.32900  86.10100 0.660 12.69741 ? 746 HOH A O   1 
HETATM 2495 O  O   B HOH D 3 .   ? 6.39900   15.77500  86.89700 0.340 12.07378 ? 746 HOH A O   1 
HETATM 2496 O  O   A HOH D 3 .   ? -9.96200  23.93100  75.87600 0.480 13.74378 ? 747 HOH A O   1 
HETATM 2497 O  O   B HOH D 3 .   ? -9.03500  24.10800  74.80800 0.520 17.31112 ? 747 HOH A O   1 
HETATM 2498 O  O   . HOH D 3 .   ? 14.61100  12.37500  80.97400 1.000 28.31378 ? 748 HOH A O   1 
HETATM 2499 O  O   A HOH D 3 .   ? 15.15100  -7.87000  61.75300 0.750 19.34821 ? 749 HOH A O   1 
HETATM 2500 O  O   B HOH D 3 .   ? 16.05100  -7.26300  60.85800 0.250 14.01378 ? 749 HOH A O   1 
HETATM 2501 O  O   . HOH D 3 .   ? 1.61600   22.75100  62.93600 1.000 48.70378 ? 750 HOH A O   1 
HETATM 2502 O  O   . HOH D 3 .   ? 12.34300  -0.99000  54.78700 1.000 17.31112 ? 751 HOH A O   1 
HETATM 2503 O  O   . HOH D 3 .   ? 19.36900  4.76100   71.35100 1.000 36.81378 ? 752 HOH A O   1 
HETATM 2504 O  O   . HOH D 3 .   ? 5.21100   -20.18500 75.48300 1.000 40.18378 ? 753 HOH A O   1 
HETATM 2505 O  O   . HOH D 3 .   ? 4.44100   23.63200  69.13900 1.000 29.33378 ? 754 HOH A O   1 
HETATM 2506 O  O   A HOH D 3 .   ? 6.38800   22.78100  74.22900 0.720 17.49535 ? 755 HOH A O   1 
HETATM 2507 O  O   B HOH D 3 .   ? 6.41400   21.73200  74.37700 0.280 13.69378 ? 755 HOH A O   1 
HETATM 2508 O  O   . HOH D 3 .   ? 0.66500   24.81600  73.61000 1.000 19.39295 ? 756 HOH A O   1 
HETATM 2509 O  O   . HOH D 3 .   ? -7.36900  -20.95400 79.80000 1.000 15.54249 ? 757 HOH A O   1 
HETATM 2510 O  O   . HOH D 3 .   ? 2.78300   -14.89100 55.38400 1.000 39.79378 ? 758 HOH A O   1 
HETATM 2511 O  O   . HOH D 3 .   ? 9.21700   11.09200  89.12700 1.000 14.47657 ? 759 HOH A O   1 
HETATM 2512 O  O   . HOH D 3 .   ? 17.83000  -7.51700  75.48200 1.000 24.89378 ? 760 HOH A O   1 
HETATM 2513 O  O   . HOH D 3 .   ? -9.90100  -15.55500 55.13000 1.000 29.11378 ? 761 HOH A O   1 
HETATM 2514 O  O   . HOH D 3 .   ? 7.49500   21.97000  76.87300 1.000 25.40378 ? 762 HOH A O   1 
HETATM 2515 O  O   A HOH D 3 .   ? 4.28900   20.78200  83.47600 0.450 16.83378 ? 763 HOH A O   1 
HETATM 2516 O  O   B HOH D 3 .   ? 4.37300   19.77900  84.88100 0.550 30.25378 ? 763 HOH A O   1 
HETATM 2517 O  O   . HOH D 3 .   ? -10.05300 11.64500  92.76700 1.000 27.97378 ? 764 HOH A O   1 
HETATM 2518 O  O   . HOH D 3 .   ? -1.15300  24.21900  63.97800 1.000 36.39378 ? 765 HOH A O   1 
HETATM 2519 O  O   . HOH D 3 .   ? 5.91200   22.39500  64.86600 1.000 37.55378 ? 766 HOH A O   1 
HETATM 2520 O  O   . HOH D 3 .   ? -19.06000 11.15400  88.16400 1.000 27.17378 ? 767 HOH A O   1 
HETATM 2521 O  O   . HOH D 3 .   ? -3.36600  -19.62400 59.44500 1.000 24.33378 ? 768 HOH A O   1 
HETATM 2522 O  O   A HOH D 3 .   ? -5.63800  25.57100  69.50800 0.390 20.22378 ? 769 HOH A O   1 
HETATM 2523 O  O   B HOH D 3 .   ? -6.26500  25.56000  70.84400 0.610 32.42378 ? 769 HOH A O   1 
HETATM 2524 O  O   . HOH D 3 .   ? 13.49800  -8.91000  58.73000 1.000 25.70378 ? 770 HOH A O   1 
HETATM 2525 O  O   A HOH D 3 .   ? -20.46900 16.24300  82.02400 1.000 50.89378 ? 771 HOH A O   1 
HETATM 2526 O  O   B HOH D 3 .   ? 16.14100  13.51000  77.24800 0.960 26.98378 ? 772 HOH A O   1 
HETATM 2527 O  O   . HOH D 3 .   ? -5.31500  24.61600  78.86000 1.000 33.25378 ? 773 HOH A O   1 
HETATM 2528 O  O   . HOH D 3 .   ? -0.35000  -22.39000 74.50000 1.000 42.08378 ? 774 HOH A O   1 
HETATM 2529 O  O   A HOH D 3 .   ? 9.96000   20.99900  68.18000 0.310 13.23378 ? 775 HOH A O   1 
HETATM 2530 O  O   B HOH D 3 .   ? 11.86400  20.49100  69.07200 0.690 24.36378 ? 775 HOH A O   1 
HETATM 2531 O  O   . HOH D 3 .   ? 19.98300  -1.18800  70.46700 1.000 46.05378 ? 776 HOH A O   1 
HETATM 2532 O  O   A HOH D 3 .   ? 7.03500   22.61500  66.96200 0.360 43.18378 ? 777 HOH A O   1 
HETATM 2533 O  O   B HOH D 3 .   ? 5.61700   23.26300  67.07600 0.640 42.00378 ? 777 HOH A O   1 
HETATM 2534 O  O   A HOH D 3 .   ? -4.47900  -21.74400 63.54000 0.520 18.93763 ? 778 HOH A O   1 
HETATM 2535 O  O   B HOH D 3 .   ? -5.02500  -22.23700 62.34500 0.480 29.75378 ? 778 HOH A O   1 
HETATM 2536 O  O   . HOH D 3 .   ? 15.18700  -10.53000 80.46800 1.000 42.40378 ? 779 HOH A O   1 
HETATM 2537 O  O   A HOH D 3 .   ? 17.80900  5.16900   61.55600 0.300 14.79378 ? 780 HOH A O   1 
HETATM 2538 O  O   B HOH D 3 .   ? 17.96400  5.05500   63.00800 0.700 34.75378 ? 780 HOH A O   1 
HETATM 2539 O  O   A HOH D 3 .   ? -1.93800  -22.97000 69.66100 0.620 42.28378 ? 781 HOH A O   1 
HETATM 2540 O  O   B HOH D 3 .   ? -4.48300  -21.12100 72.85000 0.380 16.81378 ? 781 HOH A O   1 
HETATM 2541 O  O   . HOH D 3 .   ? 3.41700   24.71500  73.49900 1.000 23.97378 ? 782 HOH A O   1 
HETATM 2542 O  O   . HOH D 3 .   ? -11.97000 21.02500  84.28100 1.000 30.48378 ? 783 HOH A O   1 
HETATM 2543 O  O   . HOH D 3 .   ? -7.78200  25.10700  77.46400 1.000 34.67378 ? 784 HOH A O   1 
HETATM 2544 O  O   . HOH D 3 .   ? 19.25200  0.85900   64.24300 1.000 27.71378 ? 785 HOH A O   1 
HETATM 2545 O  O   . HOH D 3 .   ? 6.47300   13.74700  90.12500 1.000 20.77996 ? 786 HOH A O   1 
HETATM 2546 O  O   . HOH D 3 .   ? 19.41700  -5.33800  70.31500 1.000 55.37378 ? 787 HOH A O   1 
HETATM 2547 O  O   . HOH D 3 .   ? 11.44700  19.48700  77.93400 1.000 17.80855 ? 788 HOH A O   1 
HETATM 2548 O  O   . HOH D 3 .   ? 2.02600   9.83300   49.23800 1.000 44.67378 ? 789 HOH A O   1 
HETATM 2549 O  O   A HOH D 3 .   ? -14.14500 18.29600  86.70000 0.470 32.56378 ? 790 HOH A O   1 
HETATM 2550 O  O   B HOH D 3 .   ? -13.67000 17.02100  87.80200 0.530 34.41378 ? 790 HOH A O   1 
HETATM 2551 O  O   . HOH D 3 .   ? 14.39200  1.65700   55.39700 1.000 63.08378 ? 791 HOH A O   1 
HETATM 2552 O  O   . HOH D 3 .   ? 10.02100  21.13600  76.34300 1.000 16.07676 ? 792 HOH A O   1 
HETATM 2553 O  O   A HOH D 3 .   ? 13.41700  16.56400  80.28100 0.680 20.76680 ? 793 HOH A O   1 
HETATM 2554 O  O   B HOH D 3 .   ? 14.60100  17.00900  79.31300 0.320 25.96378 ? 793 HOH A O   1 
HETATM 2555 O  O   . HOH D 3 .   ? -0.01800  25.66000  68.54000 1.000 42.23378 ? 794 HOH A O   1 
HETATM 2556 O  O   . HOH D 3 .   ? -1.99400  26.14100  71.46100 1.000 28.49378 ? 795 HOH A O   1 
HETATM 2557 O  O   . HOH D 3 .   ? 12.81900  9.97400   87.52500 1.000 22.72378 ? 796 HOH A O   1 
HETATM 2558 O  O   . HOH D 3 .   ? 3.70100   19.23300  87.00800 1.000 39.92378 ? 797 HOH A O   1 
HETATM 2559 O  O   . HOH D 3 .   ? -11.77200 24.18100  78.09400 1.000 25.88378 ? 798 HOH A O   1 
HETATM 2560 O  O   A HOH D 3 .   ? 4.64500   22.64300  81.06900 0.500 24.57378 ? 799 HOH A O   1 
HETATM 2561 O  O   B HOH D 3 .   ? 5.73000   23.53300  80.57400 0.500 29.48378 ? 799 HOH A O   1 
HETATM 2562 O  O   A HOH D 3 .   ? -11.91100 9.91700   93.64800 0.710 16.83738 ? 800 HOH A O   1 
HETATM 2563 O  O   B HOH D 3 .   ? -12.18600 11.37100  92.58700 0.290 12.37378 ? 800 HOH A O   1 
HETATM 2564 O  O   . HOH D 3 .   ? -6.24900  -22.99800 75.93900 1.000 22.48378 ? 801 HOH A O   1 
HETATM 2565 O  O   . HOH D 3 .   ? 20.27000  -0.87200  67.91700 1.000 34.10378 ? 802 HOH A O   1 
HETATM 2566 O  O   . HOH D 3 .   ? 10.83500  -5.41300  53.02300 1.000 42.32378 ? 803 HOH A O   1 
HETATM 2567 O  O   . HOH D 3 .   ? 11.56800  18.58800  80.50000 1.000 44.10378 ? 804 HOH A O   1 
HETATM 2568 O  O   A HOH D 3 .   ? 19.84800  2.84000   65.43200 0.520 28.95378 ? 805 HOH A O   1 
HETATM 2569 O  O   B HOH D 3 .   ? 20.11300  4.10600   64.44600 0.480 30.31378 ? 805 HOH A O   1 
HETATM 2570 O  O   . HOH D 3 .   ? 12.56400  -16.93000 72.44200 1.000 12.45264 ? 806 HOH A O   1 
HETATM 2571 O  O   . HOH D 3 .   ? 5.89700   9.65900   50.32800 1.000 29.89378 ? 807 HOH A O   1 
HETATM 2572 O  O   . HOH D 3 .   ? -11.42400 6.59700   94.97700 1.000 35.87378 ? 808 HOH A O   1 
HETATM 2573 O  O   A HOH D 3 .   ? 11.14300  -15.21800 61.09800 0.650 22.36378 ? 809 HOH A O   1 
HETATM 2574 O  O   B HOH D 3 .   ? 9.94800   -15.14900 60.46400 0.350 13.88378 ? 809 HOH A O   1 
HETATM 2575 O  O   A HOH D 3 .   ? 19.00400  -7.75500  71.78800 0.560 15.23719 ? 810 HOH A O   1 
HETATM 2576 O  O   B HOH D 3 .   ? 18.54900  -7.83500  72.86000 0.440 22.13378 ? 810 HOH A O   1 
HETATM 2577 O  O   A HOH D 3 .   ? 15.22700  4.75500   56.24200 0.680 16.32604 ? 812 HOH A O   1 
HETATM 2578 O  O   B HOH D 3 .   ? 15.64400  6.44700   57.60700 0.320 13.93978 ? 812 HOH A O   1 
HETATM 2579 O  O   . HOH D 3 .   ? 7.74800   -15.85500 58.02500 1.000 38.22378 ? 813 HOH A O   1 
HETATM 2580 O  O   . HOH D 3 .   ? 18.64800  1.52500   61.45900 1.000 20.41378 ? 814 HOH A O   1 
HETATM 2581 O  O   B HOH D 3 .   ? 2.76200   -17.52000 56.65600 0.650 21.33378 ? 815 HOH A O   1 
HETATM 2582 O  O   C HOH D 3 .   ? 3.76900   -18.13200 57.25100 0.350 12.02378 ? 815 HOH A O   1 
HETATM 2583 O  O   . HOH D 3 .   ? -14.24700 11.39700  92.36700 1.000 19.46664 ? 816 HOH A O   1 
HETATM 2584 O  O   . HOH D 3 .   ? -3.63300  26.48800  69.71300 1.000 47.29378 ? 817 HOH A O   1 
HETATM 2585 O  O   A HOH D 3 .   ? 15.10100  -10.12000 60.43000 0.560 15.39773 ? 818 HOH A O   1 
HETATM 2586 O  O   B HOH D 3 .   ? 16.31600  -11.15700 61.28300 0.440 17.91378 ? 818 HOH A O   1 
HETATM 2587 O  O   . HOH D 3 .   ? 12.32000  -3.37800  53.16000 1.000 29.66378 ? 819 HOH A O   1 
HETATM 2588 O  O   A HOH D 3 .   ? 15.22500  16.15300  78.85800 0.220 20.48378 ? 820 HOH A O   1 
HETATM 2589 O  O   B HOH D 3 .   ? 16.41300  15.78300  79.92200 0.780 44.40378 ? 820 HOH A O   1 
HETATM 2590 O  O   A HOH D 3 .   ? -9.69500  22.99500  83.93400 0.630 36.76378 ? 821 HOH A O   1 
HETATM 2591 O  O   B HOH D 3 .   ? -8.13800  23.28800  81.27800 0.370 22.96378 ? 821 HOH A O   1 
HETATM 2592 O  O   A HOH D 3 .   ? 0.19300   -18.33900 56.14400 0.630 28.99378 ? 822 HOH A O   1 
HETATM 2593 O  O   B HOH D 3 .   ? 1.48800   -16.79800 54.69000 0.370 29.43378 ? 822 HOH A O   1 
HETATM 2594 O  O   A HOH D 3 .   ? -15.62500 20.76300  83.62200 0.520 20.60378 ? 823 HOH A O   1 
HETATM 2595 O  O   B HOH D 3 .   ? -17.61100 19.98500  84.64200 0.480 24.19378 ? 823 HOH A O   1 
HETATM 2596 O  O   A HOH D 3 .   ? -5.33600  -18.27000 55.36900 0.620 29.01378 ? 824 HOH A O   1 
HETATM 2597 O  O   B HOH D 3 .   ? -7.44900  -18.19000 54.90600 0.380 24.10378 ? 824 HOH A O   1 
HETATM 2598 O  O   . HOH D 3 .   ? -5.54900  -20.98600 59.39800 1.000 22.16378 ? 825 HOH A O   1 
HETATM 2599 O  O   . HOH D 3 .   ? 10.11300  -12.57400 55.95000 1.000 56.42378 ? 826 HOH A O   1 
HETATM 2600 O  O   . HOH D 3 .   ? 13.10300  15.11300  84.54200 1.000 30.05378 ? 827 HOH A O   1 
HETATM 2601 O  O   . HOH D 3 .   ? -1.99700  26.57700  75.86800 1.000 21.58378 ? 828 HOH A O   1 
HETATM 2602 O  O   . HOH D 3 .   ? 2.64800   24.56700  80.23300 1.000 18.35072 ? 829 HOH A O   1 
HETATM 2603 O  O   A HOH D 3 .   ? -3.71400  24.27200  83.31900 0.700 23.43378 ? 830 HOH A O   1 
HETATM 2604 O  O   B HOH D 3 .   ? -14.44100 9.00200   94.01600 0.420 15.36378 ? 831 HOH A O   1 
HETATM 2605 O  O   . HOH D 3 .   ? 19.99400  -3.49300  64.43500 1.000 28.63378 ? 832 HOH A O   1 
HETATM 2606 O  O   . HOH D 3 .   ? 2.48600   25.57000  65.50600 1.000 41.60378 ? 833 HOH A O   1 
HETATM 2607 O  O   . HOH D 3 .   ? 4.44300   25.76400  71.19300 1.000 41.28378 ? 834 HOH A O   1 
HETATM 2608 O  O   . HOH D 3 .   ? 6.71000   20.26400  85.63400 1.000 39.26378 ? 835 HOH A O   1 
HETATM 2609 O  O   A HOH D 3 .   ? -15.52300 19.84200  85.92300 0.710 32.75378 ? 836 HOH A O   1 
HETATM 2610 O  O   B HOH D 3 .   ? -15.58800 17.86700  86.62400 0.290 18.66378 ? 836 HOH A O   1 
HETATM 2611 O  O   . HOH D 3 .   ? -3.76500  26.59700  77.79200 1.000 29.42378 ? 837 HOH A O   1 
HETATM 2612 O  O   . HOH D 3 .   ? 13.45900  19.87500  76.09600 1.000 12.64477 ? 838 HOH A O   1 
HETATM 2613 O  O   . HOH D 3 .   ? 3.70100   8.09400   95.36700 1.000 26.41378 ? 839 HOH A O   1 
HETATM 2614 O  O   . HOH D 3 .   ? 10.37000  -17.56100 61.75900 1.000 22.25378 ? 840 HOH A O   1 
HETATM 2615 O  O   A HOH D 3 .   ? 7.01600   23.13300  79.85500 0.370 14.28378 ? 841 HOH A O   1 
HETATM 2616 O  O   B HOH D 3 .   ? 7.40700   23.56500  78.73800 0.630 20.27378 ? 841 HOH A O   1 
HETATM 2617 O  O   . HOH D 3 .   ? 0.20300   27.12600  72.15000 1.000 43.28378 ? 842 HOH A O   1 
HETATM 2618 O  O   . HOH D 3 .   ? 3.01600   -22.72000 64.76500 1.000 35.90378 ? 843 HOH A O   1 
HETATM 2619 O  O   . HOH D 3 .   ? 14.81300  0.04000   53.79600 1.000 35.10378 ? 844 HOH A O   1 
HETATM 2620 O  O   . HOH D 3 .   ? 12.41200  -16.97800 63.48500 1.000 21.97484 ? 845 HOH A O   1 
HETATM 2621 O  O   . HOH D 3 .   ? 17.36400  -6.42500  59.19400 1.000 20.88378 ? 846 HOH A O   1 
HETATM 2622 O  O   A HOH D 3 .   ? -5.40700  27.36300  74.96500 0.440 18.57378 ? 847 HOH A O   1 
HETATM 2623 O  O   B HOH D 3 .   ? -5.91300  27.06900  76.69900 0.560 37.80378 ? 847 HOH A O   1 
HETATM 2624 O  O   . HOH D 3 .   ? -1.11700  -20.95100 58.28700 1.000 32.26378 ? 848 HOH A O   1 
HETATM 2625 O  O   . HOH D 3 .   ? 9.74500   -20.61600 70.24200 1.000 47.67378 ? 849 HOH A O   1 
HETATM 2626 O  O   . HOH D 3 .   ? 2.34900   25.99700  77.99700 1.000 31.84378 ? 850 HOH A O   1 
HETATM 2627 O  O   A HOH D 3 .   ? 9.81700   7.44500   50.30900 0.650 17.41377 ? 851 HOH A O   1 
HETATM 2628 O  O   B HOH D 3 .   ? 8.80300   8.25700   50.27500 0.350 20.08378 ? 851 HOH A O   1 
HETATM 2629 O  O   . HOH D 3 .   ? 4.17700   26.01100  75.73700 1.000 43.04378 ? 852 HOH A O   1 
HETATM 2630 O  O   . HOH D 3 .   ? 6.24400   25.33300  75.35500 1.000 38.01378 ? 853 HOH A O   1 
HETATM 2631 O  O   A HOH D 3 .   ? 0.57800   21.17100  87.13900 0.680 17.49535 ? 854 HOH A O   1 
HETATM 2632 O  O   B HOH D 3 .   ? 1.03000   22.42600  86.72300 0.320 12.62378 ? 854 HOH A O   1 
HETATM 2633 O  O   . HOH D 3 .   ? 7.31000   -18.76500 59.02700 1.000 30.92378 ? 855 HOH A O   1 
HETATM 2634 O  O   . HOH D 3 .   ? 12.74300  -18.07200 66.19000 1.000 14.64238 ? 856 HOH A O   1 
HETATM 2635 O  O   . HOH D 3 .   ? 15.24400  10.96000  86.86100 1.000 46.24378 ? 857 HOH A O   1 
HETATM 2636 O  O   . HOH D 3 .   ? 11.99000  -19.46300 71.35600 1.000 22.98378 ? 858 HOH A O   1 
HETATM 2637 O  O   . HOH D 3 .   ? 7.31200   10.42200  93.74500 1.000 21.28378 ? 859 HOH A O   1 
HETATM 2638 O  O   . HOH D 3 .   ? -12.21200 12.69600  94.27200 1.000 16.66894 ? 860 HOH A O   1 
HETATM 2639 O  O   . HOH D 3 .   ? 13.98200  -9.73600  55.84100 1.000 19.51665 ? 861 HOH A O   1 
HETATM 2640 O  O   . HOH D 3 .   ? -0.61100  -23.07600 61.77400 1.000 42.46378 ? 862 HOH A O   1 
HETATM 2641 O  O   . HOH D 3 .   ? -1.81200  9.65600   96.80900 1.000 33.39378 ? 863 HOH A O   1 
HETATM 2642 O  O   . HOH D 3 .   ? 8.83100   -4.74000  49.21800 1.000 32.40378 ? 864 HOH A O   1 
HETATM 2643 O  O   . HOH D 3 .   ? 14.57800  13.78700  86.03200 1.000 51.42378 ? 865 HOH A O   1 
HETATM 2644 O  O   . HOH D 3 .   ? -2.20800  12.20800  95.97600 1.000 21.00367 ? 866 HOH A O   1 
HETATM 2645 O  O   . HOH D 3 .   ? -13.49600 17.92300  90.53400 1.000 25.08378 ? 867 HOH A O   1 
HETATM 2646 O  O   . HOH D 3 .   ? 15.26000  -7.13100  55.42400 1.000 15.06875 ? 868 HOH A O   1 
HETATM 2647 O  O   A HOH D 3 .   ? 18.07900  2.80500   56.88100 0.580 23.85378 ? 869 HOH A O   1 
HETATM 2648 O  O   B HOH D 3 .   ? 16.56100  2.37100   55.76000 0.420 22.52378 ? 869 HOH A O   1 
HETATM 2649 O  O   A HOH D 3 .   ? -8.05100  -19.54600 55.08700 0.680 34.17378 ? 870 HOH A O   1 
HETATM 2650 O  O   B HOH D 3 .   ? -7.68100  -20.57600 55.90500 0.320 24.17378 ? 870 HOH A O   1 
HETATM 2651 O  O   . HOH D 3 .   ? 11.72600  21.36500  80.02300 1.000 37.05378 ? 871 HOH A O   1 
HETATM 2652 O  O   A HOH D 3 .   ? 7.90100   9.15900   48.92200 0.550 30.02378 ? 872 HOH A O   1 
HETATM 2653 O  O   A HOH D 3 .   ? 12.31000  13.35300  89.17000 0.730 20.40575 ? 873 HOH A O   1 
HETATM 2654 O  O   . HOH D 3 .   ? 5.71100   -22.61000 64.42600 1.000 20.45624 ? 874 HOH A O   1 
HETATM 2655 O  O   A HOH D 3 .   ? -10.93100 10.37000  96.21300 0.670 56.67378 ? 875 HOH A O   1 
HETATM 2656 O  O   B HOH D 3 .   ? -10.42700 10.53600  97.37500 0.330 24.90378 ? 875 HOH A O   1 
HETATM 2657 O  O   . HOH D 3 .   ? 8.76600   -2.01000  48.15100 1.000 28.76378 ? 876 HOH A O   1 
HETATM 2658 O  O   . HOH D 3 .   ? 8.67900   24.91300  67.73500 1.000 26.96378 ? 877 HOH A O   1 
HETATM 2659 O  O   . HOH D 3 .   ? 19.96800  0.02300   59.61400 1.000 28.44378 ? 878 HOH A O   1 
HETATM 2660 O  O   . HOH D 3 .   ? 5.36800   25.45600  79.89300 1.000 27.04378 ? 879 HOH A O   1 
HETATM 2661 O  O   A HOH D 3 .   ? 11.50600  17.29400  87.09900 0.620 24.43378 ? 880 HOH A O   1 
HETATM 2662 O  O   B HOH D 3 .   ? 10.34900  18.24100  87.38500 0.380 20.17378 ? 880 HOH A O   1 
HETATM 2663 O  O   . HOH D 3 .   ? 0.57900   15.53500  94.39700 1.000 23.13378 ? 881 HOH A O   1 
HETATM 2664 O  O   . HOH D 3 .   ? 21.33500  10.37600  75.12500 1.000 28.25378 ? 882 HOH A O   1 
HETATM 2665 O  O   . HOH D 3 .   ? 19.60200  -11.73000 73.75400 1.000 12.88954 ? 883 HOH A O   1 
HETATM 2666 O  O   A HOH D 3 .   ? 11.24500  23.57700  76.24000 0.720 19.28767 ? 884 HOH A O   1 
HETATM 2667 O  O   B HOH D 3 .   ? 11.45500  23.31600  77.27600 0.280 16.10378 ? 884 HOH A O   1 
HETATM 2668 O  O   A HOH D 3 .   ? 10.33700  4.90800   48.58300 0.730 21.42378 ? 885 HOH A O   1 
HETATM 2669 O  O   B HOH D 3 .   ? 10.78500  6.21500   49.77800 0.270 22.83378 ? 885 HOH A O   1 
HETATM 2670 O  O   . HOH D 3 .   ? 5.95900   5.08600   96.90700 1.000 22.16378 ? 886 HOH A O   1 
HETATM 2671 O  O   B HOH D 3 .   ? 8.82600   -22.37200 66.96000 0.610 29.63378 ? 887 HOH A O   1 
HETATM 2672 O  O   . HOH D 3 .   ? 5.77500   21.60600  87.60300 1.000 41.72378 ? 888 HOH A O   1 
HETATM 2673 O  O   . HOH D 3 .   ? 2.77800   -20.82100 56.77300 1.000 49.41378 ? 889 HOH A O   1 
HETATM 2674 O  O   B HOH D 3 .   ? 12.20700  -20.48900 68.38800 0.360 23.61460 ? 890 HOH A O   1 
HETATM 2675 O  O   . HOH D 3 .   ? 12.83500  -7.70900  51.77100 1.000 23.81378 ? 891 HOH A O   1 
HETATM 2676 O  O   . HOH D 3 .   ? 14.95000  -4.24900  52.38100 1.000 25.00378 ? 892 HOH A O   1 
HETATM 2677 O  O   . HOH D 3 .   ? 6.45600   -23.75600 66.50400 1.000 41.36378 ? 893 HOH A O   1 
HETATM 2678 O  O   A HOH D 3 .   ? -15.45300 11.90300  94.85400 0.560 10.70770 ? 894 HOH A O   1 
HETATM 2679 O  O   B HOH D 3 .   ? -14.87500 11.50700  95.85100 0.440 19.47378 ? 894 HOH A O   1 
HETATM 2680 O  O   A HOH D 3 .   ? 2.67600   -23.36800 60.65000 0.410 31.51378 ? 895 HOH A O   1 
HETATM 2681 O  O   B HOH D 3 .   ? 1.78500   -23.49800 62.15500 0.590 31.86378 ? 895 HOH A O   1 
HETATM 2682 O  O   A HOH D 3 .   ? 11.18100  13.26600  92.04600 0.730 21.11220 ? 896 HOH A O   1 
HETATM 2683 O  O   A HOH D 3 .   ? 13.85100  22.50700  76.71800 0.670 20.88523 ? 897 HOH A O   1 
HETATM 2684 O  O   B HOH D 3 .   ? 13.13300  22.90400  75.42700 0.330 26.12378 ? 897 HOH A O   1 
HETATM 2685 O  O   A HOH D 3 .   ? 15.82900  2.19000   51.80600 0.510 23.44378 ? 898 HOH A O   1 
HETATM 2686 O  O   B HOH D 3 .   ? 15.07900  4.10600   50.61000 0.490 32.66378 ? 898 HOH A O   1 
HETATM 2687 O  O   A HOH D 3 .   ? -13.19300 10.80200  96.71600 0.720 34.87378 ? 899 HOH A O   1 
HETATM 2688 O  O   B HOH D 3 .   ? -11.77400 10.56700  95.35400 0.280 25.51378 ? 899 HOH A O   1 
HETATM 2689 O  O   A HOH D 3 .   ? 3.71900   6.87100   98.18100 0.600 23.69378 ? 900 HOH A O   1 
HETATM 2690 O  O   B HOH D 3 .   ? 2.33600   6.52400   99.61000 0.400 24.62378 ? 900 HOH A O   1 
HETATM 2691 O  O   A HOH D 3 .   ? 20.41500  -11.32500 66.45000 0.790 12.61319 ? 901 HOH A O   1 
HETATM 2692 O  O   B HOH D 3 .   ? 20.51900  -12.82900 66.64600 0.210 13.67378 ? 901 HOH A O   1 
HETATM 2693 O  O   A HOH D 3 .   ? 14.33800  6.11400   50.74400 0.440 28.50378 ? 902 HOH A O   1 
HETATM 2694 O  O   B HOH D 3 .   ? 12.91500  7.71700   50.74000 0.560 33.18378 ? 902 HOH A O   1 
HETATM 2695 O  O   . HOH D 3 .   ? 15.75300  20.41900  79.85600 1.000 52.72378 ? 903 HOH A O   1 
HETATM 2696 O  O   . HOH D 3 .   ? 11.73900  -19.67400 60.45100 1.000 34.73378 ? 904 HOH A O   1 
HETATM 2697 O  O   . HOH D 3 .   ? 12.79000  11.00700  92.73200 1.000 33.68378 ? 905 HOH A O   1 
HETATM 2698 O  O   A HOH D 3 .   ? 7.31200   21.20800  89.51000 0.520 24.24378 ? 906 HOH A O   1 
HETATM 2699 O  O   B HOH D 3 .   ? 9.75600   20.54900  89.19300 0.480 29.22378 ? 906 HOH A O   1 
HETATM 2700 O  O   . HOH D 3 .   ? 1.06600   7.08700   43.51900 1.000 49.62378 ? 907 HOH A O   1 
HETATM 2701 O  O   . HOH D 3 .   ? 14.63100  22.36200  79.27600 1.000 44.27378 ? 908 HOH A O   1 
HETATM 2702 O  O   . HOH D 3 .   ? 6.75000   -24.37200 62.28200 0.580 33.83378 ? 909 HOH A O   1 
HETATM 2703 O  O   A HOH D 3 .   ? 8.09600   6.46300   45.01600 0.340 20.74378 ? 910 HOH A O   1 
HETATM 2704 O  O   B HOH D 3 .   ? 7.45400   4.21800   44.65000 0.660 37.30378 ? 910 HOH A O   1 
HETATM 2705 O  O   . HOH D 3 .   ? 6.13000   27.46000  81.88100 1.000 50.62378 ? 911 HOH A O   1 
HETATM 2706 O  O   . HOH D 3 .   ? 10.40500  -23.82400 64.73000 1.000 38.68378 ? 912 HOH A O   1 
HETATM 2707 O  O   . HOH D 3 .   ? 7.94500   24.02100  87.31900 1.000 52.23378 ? 913 HOH A O   1 
HETATM 2708 O  O   . HOH D 3 .   ? 7.52000   9.32700   44.78300 1.000 35.43378 ? 914 HOH A O   1 
HETATM 2709 O  O   . HOH D 3 .   ? 6.29100   6.39600   43.54400 1.000 54.92378 ? 915 HOH A O   1 
HETATM 2710 O  O   . HOH D 3 .   ? 8.30000   26.25100  84.24000 1.000 47.55378 ? 916 HOH A O   1 
HETATM 2711 O  O   . HOH D 3 .   ? 12.60000  15.32600  93.35100 1.000 36.33378 ? 917 HOH A O   1 
HETATM 2712 O  O   . HOH D 3 .   ? 15.22400  15.12400  91.47300 1.000 36.06378 ? 918 HOH A O   1 
HETATM 2713 O  O   B HOH D 3 .   ? 14.64000  17.95400  90.21900 1.000 49.22378 ? 919 HOH A O   1 
HETATM 2714 O  O   . HOH D 3 .   ? 12.14700  17.91500  93.36600 1.000 27.11378 ? 920 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
4    C  CA  B SER A 1   ? 0.30485 0.27035 0.26495 0.02090  -0.03180 0.01110  2   SER A CA  
8    O  O   B SER A 1   ? 0.31725 0.28105 0.29705 0.14790  0.02370  -0.06210 2   SER A O   
14   N  N   B LYS A 2   ? 0.27985 0.27185 0.29005 0.05170  -0.08940 -0.07740 3   LYS A N   
16   C  CA  B LYS A 2   ? 0.26435 0.25505 0.28615 0.04680  -0.09730 -0.07580 3   LYS A CA  
18   C  C   B LYS A 2   ? 0.23565 0.19345 0.24965 0.03430  -0.07250 -0.06540 3   LYS A C   
20   O  O   B LYS A 2   ? 0.22265 0.18125 0.24115 0.01210  -0.07990 -0.05980 3   LYS A O   
32   N  N   B GLY A 3   ? 0.22405 0.16385 0.22195 0.03090  -0.05320 -0.05460 4   GLY A N   
34   C  CA  B GLY A 3   ? 0.20055 0.15265 0.19095 0.01670  -0.04120 -0.04930 4   GLY A CA  
36   C  C   B GLY A 3   ? 0.16935 0.14075 0.17265 0.01290  -0.02370 -0.03300 4   GLY A C   
38   O  O   B GLY A 3   ? 0.18445 0.14125 0.16305 0.02820  -0.02740 -0.03570 4   GLY A O   
39   N  N   . GLU A 4   ? 0.14735 0.14455 0.15225 -0.00260 -0.02380 -0.00690 5   GLU A N   
43   C  C   . GLU A 4   ? 0.13965 0.14785 0.14965 0.03830  -0.01260 -0.02050 5   GLU A C   
44   O  O   . GLU A 4   ? 0.12005 0.15955 0.13855 0.01400  0.00060  -0.01600 5   GLU A O   
60   N  N   . GLU A 5   ? 0.14605 0.12665 0.15145 0.04540  0.00540  -0.02610 6   GLU A N   
61   C  CA  . GLU A 5   ? 0.15025 0.12905 0.19785 0.02610  0.00470  -0.04230 6   GLU A CA  
62   C  C   . GLU A 5   ? 0.12505 0.10785 0.17395 0.00380  -0.01380 -0.01370 6   GLU A C   
63   O  O   . GLU A 5   ? 0.15015 0.10785 0.16325 0.02480  -0.01180 -0.01250 6   GLU A O   
64   C  CB  . GLU A 5   ? 0.25515 0.23725 0.29975 0.02390  0.00930  -0.08270 6   GLU A CB  
69   N  N   . LEU A 6   ? 0.10525 0.10075 0.15665 0.00340  0.01600  -0.02710 7   LEU A N   
70   C  CA  . LEU A 6   ? 0.10015 0.11165 0.13225 0.00770  0.00460  -0.00760 7   LEU A CA  
71   C  C   . LEU A 6   ? 0.10055 0.10365 0.12115 -0.00540 0.00510  0.00790  7   LEU A C   
72   O  O   . LEU A 6   ? 0.10625 0.12705 0.13045 -0.00760 0.00330  0.01240  7   LEU A O   
73   C  CB  . LEU A 6   ? 0.10135 0.11095 0.14655 0.01380  -0.02030 -0.03760 7   LEU A CB  
74   C  CG  . LEU A 6   ? 0.12225 0.12705 0.14745 -0.00750 -0.01070 -0.02760 7   LEU A CG  
75   C  CD1 . LEU A 6   ? 0.12275 0.14215 0.16665 0.02570  -0.01880 -0.03760 7   LEU A CD1 
76   C  CD2 . LEU A 6   ? 0.16205 0.14965 0.16705 -0.03970 -0.02110 -0.01890 7   LEU A CD2 
77   N  N   . PHE A 7   ? 0.09835 0.08915 0.11015 -0.01100 -0.00290 -0.00840 8   PHE A N   
78   C  CA  . PHE A 7   ? 0.11465 0.09175 0.12155 -0.00660 -0.00590 -0.00420 8   PHE A CA  
79   C  C   . PHE A 7   ? 0.09705 0.09725 0.14235 0.00440  -0.00140 0.01160  8   PHE A C   
80   O  O   . PHE A 7   ? 0.11565 0.10165 0.14765 -0.00240 -0.01760 0.00230  8   PHE A O   
81   C  CB  . PHE A 7   ? 0.10515 0.07965 0.13255 -0.00430 0.01900  0.00990  8   PHE A CB  
82   C  CG  . PHE A 7   ? 0.09435 0.08055 0.12485 -0.00500 0.01010  0.01390  8   PHE A CG  
83   C  CD1 . PHE A 7   ? 0.09595 0.07675 0.12415 -0.00270 0.02090  0.00990  8   PHE A CD1 
84   C  CD2 . PHE A 7   ? 0.11275 0.08405 0.13095 -0.00490 -0.00260 0.01520  8   PHE A CD2 
85   C  CE1 . PHE A 7   ? 0.11175 0.07825 0.12135 -0.01000 0.00050  0.00760  8   PHE A CE1 
86   C  CE2 . PHE A 7   ? 0.10485 0.07675 0.12325 0.00050  -0.00250 -0.00190 8   PHE A CE2 
87   C  CZ  . PHE A 7   ? 0.11075 0.09565 0.12075 -0.00670 0.00520  -0.00450 8   PHE A CZ  
88   N  N   . THR A 8   ? 0.09135 0.11055 0.13905 0.02600  0.00940  0.00410  9   THR A N   
89   C  CA  . THR A 8   ? 0.12425 0.11735 0.15755 0.03040  -0.00160 0.00320  9   THR A CA  
90   C  C   . THR A 8   ? 0.13475 0.11235 0.15815 0.02460  -0.00320 0.00250  9   THR A C   
91   O  O   . THR A 8   ? 0.15045 0.14105 0.17095 0.03580  -0.00260 0.01880  9   THR A O   
92   C  CB  . THR A 8   ? 0.15565 0.12535 0.18625 0.03360  -0.01720 -0.00080 9   THR A CB  
93   O  OG1 . THR A 8   ? 0.18255 0.11445 0.20535 0.02870  -0.01820 -0.01210 9   THR A OG1 
94   C  CG2 . THR A 8   ? 0.18035 0.15105 0.19125 0.05040  -0.02340 -0.00350 9   THR A CG2 
95   N  N   . GLY A 9   ? 0.15745 0.09165 0.12915 0.02390  0.00190  0.00090  10  GLY A N   
96   C  CA  . GLY A 9   ? 0.17955 0.11385 0.13295 0.04120  0.01500  -0.00120 10  GLY A CA  
97   C  C   . GLY A 9   ? 0.14535 0.09505 0.13125 0.03430  0.00740  0.01340  10  GLY A C   
98   O  O   . GLY A 9   ? 0.14945 0.10185 0.15495 0.02480  0.02560  0.01790  10  GLY A O   
99   N  N   . VAL A 10  ? 0.14225 0.09815 0.12775 0.01900  0.02210  -0.00200 11  VAL A N   
100  C  CA  . VAL A 10  ? 0.10625 0.11375 0.13475 0.01570  0.00280  0.00160  11  VAL A CA  
101  C  C   . VAL A 10  ? 0.09595 0.09095 0.15965 0.00270  -0.01410 0.02050  11  VAL A C   
102  O  O   . VAL A 10  ? 0.12375 0.10885 0.20075 -0.01930 -0.02300 0.04750  11  VAL A O   
103  C  CB  . VAL A 10  ? 0.12785 0.12415 0.12775 0.02750  -0.00720 0.01170  11  VAL A CB  
104  C  CG1 . VAL A 10  ? 0.17935 0.14305 0.13945 0.03330  0.00280  0.01570  11  VAL A CG1 
105  C  CG2 . VAL A 10  ? 0.13135 0.14805 0.15085 0.02980  -0.01840 0.00510  11  VAL A CG2 
106  N  N   . VAL A 11  ? 0.09905 0.09535 0.12915 0.01380  -0.01300 0.00590  12  VAL A N   
107  C  CA  . VAL A 11  ? 0.09995 0.09435 0.12235 0.00710  -0.01140 -0.00750 12  VAL A CA  
108  C  C   . VAL A 11  ? 0.07785 0.09315 0.12455 -0.00990 0.00050  0.00620  12  VAL A C   
109  O  O   . VAL A 11  ? 0.07735 0.10145 0.12445 -0.00180 -0.00180 0.00340  12  VAL A O   
110  C  CB  . VAL A 11  ? 0.10125 0.08345 0.12025 0.01480  -0.00970 0.00150  12  VAL A CB  
111  C  CG1 . VAL A 11  ? 0.10265 0.11075 0.12715 0.03210  -0.02130 -0.00650 12  VAL A CG1 
112  C  CG2 . VAL A 11  ? 0.11165 0.09125 0.12605 0.00100  0.01160  -0.03180 12  VAL A CG2 
113  N  N   . PRO A 12  ? 0.07755 0.08055 0.12895 -0.00190 -0.00250 0.00130  13  PRO A N   
114  C  CA  . PRO A 12  ? 0.07965 0.08435 0.12675 0.01260  0.00920  0.00920  13  PRO A CA  
115  C  C   . PRO A 12  ? 0.08705 0.08485 0.10975 0.00310  0.00660  0.00920  13  PRO A C   
116  O  O   . PRO A 12  ? 0.10745 0.07025 0.10945 0.00130  -0.00410 0.00690  13  PRO A O   
117  C  CB  . PRO A 12  ? 0.11315 0.10655 0.15345 -0.00720 0.00800  0.01150  13  PRO A CB  
118  C  CG  . PRO A 12  ? 0.11635 0.14165 0.19775 -0.02580 0.03760  -0.01630 13  PRO A CG  
119  C  CD  . PRO A 12  ? 0.08595 0.09155 0.15515 -0.01540 0.00650  -0.00030 13  PRO A CD  
120  N  N   . ILE A 13  ? 0.08455 0.07535 0.09885 -0.00150 0.00490  0.01150  14  ILE A N   
121  C  CA  . ILE A 13  ? 0.09605 0.08485 0.08285 0.00790  0.01240  0.00460  14  ILE A CA  
122  C  C   . ILE A 13  ? 0.08455 0.08925 0.08795 -0.00210 -0.00340 -0.01240 14  ILE A C   
123  O  O   . ILE A 13  ? 0.07985 0.09485 0.09435 0.00800  -0.00230 -0.00610 14  ILE A O   
124  C  CB  . ILE A 13  ? 0.07635 0.07965 0.08835 -0.00130 -0.00040 0.00380  14  ILE A CB  
125  C  CG1 . ILE A 13  ? 0.08235 0.09365 0.10575 0.01760  0.02000  -0.00220 14  ILE A CG1 
126  C  CG2 . ILE A 13  ? 0.10325 0.07065 0.10505 -0.00300 -0.00090 0.01090  14  ILE A CG2 
127  C  CD1 . ILE A 13  ? 0.06875 0.10785 0.12465 0.02100  0.01160  0.01120  14  ILE A CD1 
128  N  N   . LEU A 14  ? 0.08565 0.07645 0.10845 -0.00030 -0.00640 0.00690  15  LEU A N   
129  C  CA  . LEU A 14  ? 0.07375 0.07215 0.10295 0.01400  0.02070  0.00800  15  LEU A CA  
130  C  C   . LEU A 14  ? 0.07565 0.08725 0.08115 0.00620  0.01490  0.00720  15  LEU A C   
131  O  O   . LEU A 14  ? 0.08235 0.09285 0.08405 -0.00220 0.01360  0.00860  15  LEU A O   
132  C  CB  . LEU A 14  ? 0.07705 0.08375 0.10765 -0.00040 0.00660  0.00170  15  LEU A CB  
133  C  CG  . LEU A 14  ? 0.08635 0.10105 0.10605 -0.00890 -0.00980 0.00070  15  LEU A CG  
134  C  CD1 . LEU A 14  ? 0.07655 0.13015 0.11555 -0.02420 -0.01030 -0.00120 15  LEU A CD1 
135  C  CD2 . LEU A 14  ? 0.10145 0.11265 0.10485 -0.00940 -0.00510 0.02900  15  LEU A CD2 
136  N  N   . VAL A 15  ? 0.07845 0.08295 0.09415 -0.00440 0.00560  0.00800  16  VAL A N   
137  C  CA  . VAL A 15  ? 0.06675 0.07825 0.09615 0.00360  0.01020  0.00640  16  VAL A CA  
138  C  C   . VAL A 15  ? 0.07755 0.07355 0.09395 -0.00140 0.01350  -0.00080 16  VAL A C   
139  O  O   . VAL A 15  ? 0.07935 0.08935 0.09155 0.00770  0.01560  -0.00000 16  VAL A O   
140  C  CB  . VAL A 15  ? 0.07655 0.08635 0.10775 -0.01030 -0.00330 -0.00160 16  VAL A CB  
141  C  CG1 . VAL A 15  ? 0.08425 0.08275 0.10055 -0.00580 -0.00870 0.00930  16  VAL A CG1 
142  C  CG2 . VAL A 15  ? 0.07195 0.09065 0.11215 0.00580  -0.00280 0.00550  16  VAL A CG2 
143  N  N   . GLU A 16  ? 0.07635 0.06595 0.09805 -0.00400 0.00020  -0.00670 17  GLU A N   
144  C  CA  A GLU A 16  ? 0.06565 0.07665 0.11355 -0.00720 -0.00030 0.01080  17  GLU A CA  
146  C  C   . GLU A 16  ? 0.07685 0.07875 0.10175 0.00600  0.01370  0.01210  17  GLU A C   
147  O  O   . GLU A 16  ? 0.12565 0.09235 0.09445 0.00930  0.01050  0.00560  17  GLU A O   
148  C  CB  A GLU A 16  ? 0.06925 0.08405 0.13175 -0.01840 -0.00290 -0.00060 17  GLU A CB  
150  C  CG  A GLU A 16  ? 0.10215 0.09845 0.11845 -0.02080 -0.00280 -0.00280 17  GLU A CG  
152  C  CD  A GLU A 16  ? 0.09965 0.09715 0.12265 -0.02090 -0.00080 0.01050  17  GLU A CD  
154  O  OE1 A GLU A 16  ? 0.11075 0.11045 0.13185 -0.01220 0.01320  -0.00220 17  GLU A OE1 
156  O  OE2 A GLU A 16  ? 0.13075 0.10855 0.13875 -0.02360 -0.00900 0.02180  17  GLU A OE2 
158  N  N   . LEU A 17  ? 0.07655 0.07435 0.11635 0.01420  0.00400  0.01280  18  LEU A N   
159  C  CA  . LEU A 17  ? 0.06925 0.07275 0.11415 0.00760  0.00540  0.01360  18  LEU A CA  
160  C  C   . LEU A 17  ? 0.08925 0.07175 0.10725 -0.00960 0.01830  0.01100  18  LEU A C   
161  O  O   . LEU A 17  ? 0.10155 0.08795 0.10725 0.01030  0.02640  -0.00010 18  LEU A O   
162  C  CB  . LEU A 17  ? 0.07215 0.08605 0.10775 0.00770  -0.00580 0.00780  18  LEU A CB  
163  C  CG  . LEU A 17  ? 0.08725 0.08485 0.11365 -0.01290 0.01630  0.00110  18  LEU A CG  
164  C  CD1 . LEU A 17  ? 0.08565 0.10835 0.13925 -0.00750 0.01400  0.01470  18  LEU A CD1 
165  C  CD2 . LEU A 17  ? 0.12545 0.09445 0.11635 0.00490  0.00920  -0.00680 18  LEU A CD2 
166  N  N   . ASP A 18  ? 0.06935 0.07495 0.12575 0.00600  0.00660  0.00950  19  ASP A N   
167  C  CA  . ASP A 18  ? 0.07895 0.08595 0.14975 -0.00520 0.00770  0.01060  19  ASP A CA  
168  C  C   . ASP A 18  ? 0.09985 0.07775 0.11975 0.00940  0.01050  0.01230  19  ASP A C   
169  O  O   . ASP A 18  ? 0.11855 0.08545 0.11575 0.00930  0.02220  0.00260  19  ASP A O   
170  C  CB  . ASP A 18  ? 0.09485 0.11375 0.18545 0.00830  -0.00370 0.00850  19  ASP A CB  
171  C  CG  . ASP A 18  ? 0.14845 0.17105 0.20395 -0.02680 -0.01820 0.00210  19  ASP A CG  
172  O  OD1 . ASP A 18  ? 0.15795 0.16285 0.20365 -0.02850 -0.01080 0.00920  19  ASP A OD1 
173  O  OD2 . ASP A 18  ? 0.23565 0.21025 0.23675 -0.07040 -0.03850 -0.00200 19  ASP A OD2 
174  N  N   . GLY A 19  ? 0.10135 0.07425 0.11755 0.00710  0.01930  0.00530  20  GLY A N   
175  C  CA  . GLY A 19  ? 0.10755 0.06475 0.13595 -0.00280 0.01520  -0.01090 20  GLY A CA  
176  C  C   . GLY A 19  ? 0.10515 0.08495 0.11155 -0.00690 0.01800  -0.01340 20  GLY A C   
177  O  O   . GLY A 19  ? 0.08595 0.08885 0.11895 0.00600  0.01690  0.00630  20  GLY A O   
178  N  N   . ASP A 20  ? 0.08865 0.07595 0.11195 0.00440  0.00400  -0.00210 21  ASP A N   
179  C  CA  . ASP A 20  ? 0.08875 0.07145 0.12795 0.02020  0.00040  -0.00190 21  ASP A CA  
180  C  C   . ASP A 20  ? 0.08775 0.06695 0.11195 0.00230  0.00690  -0.00600 21  ASP A C   
181  O  O   . ASP A 20  ? 0.09515 0.08245 0.11455 0.00210  0.01070  -0.00140 21  ASP A O   
182  C  CB  . ASP A 20  ? 0.07755 0.09015 0.14795 0.01690  -0.01280 0.00450  21  ASP A CB  
183  C  CG  . ASP A 20  ? 0.08035 0.11075 0.15995 0.02180  -0.00700 0.01080  21  ASP A CG  
184  O  OD1 . ASP A 20  ? 0.10075 0.09945 0.13295 0.02270  0.00780  -0.01060 21  ASP A OD1 
185  O  OD2 . ASP A 20  ? 0.12355 0.13055 0.21485 0.02860  -0.02310 0.03340  21  ASP A OD2 
186  N  N   . VAL A 21  ? 0.06495 0.07675 0.11225 0.01170  0.00640  -0.00060 22  VAL A N   
187  C  CA  . VAL A 21  ? 0.07965 0.08555 0.11435 0.01420  0.00590  -0.00930 22  VAL A CA  
188  C  C   . VAL A 21  ? 0.07595 0.09395 0.11655 0.01270  0.00870  -0.00650 22  VAL A C   
189  O  O   . VAL A 21  ? 0.09465 0.09745 0.11585 0.01560  0.00570  -0.00350 22  VAL A O   
190  C  CB  . VAL A 21  ? 0.08915 0.08965 0.11745 0.00340  0.00090  -0.00170 22  VAL A CB  
191  C  CG1 . VAL A 21  ? 0.11285 0.09565 0.12165 -0.00160 0.00350  0.00250  22  VAL A CG1 
192  C  CG2 . VAL A 21  ? 0.10175 0.08275 0.11035 0.00800  0.00990  0.00140  22  VAL A CG2 
193  N  N   . ASN A 22  ? 0.09275 0.07505 0.12345 0.00460  -0.00910 -0.00690 23  ASN A N   
194  C  CA  . ASN A 22  ? 0.10185 0.08585 0.12735 0.00460  0.01160  0.00120  23  ASN A CA  
195  C  C   . ASN A 22  ? 0.08985 0.09215 0.13525 0.01180  0.01910  -0.01180 23  ASN A C   
196  O  O   . ASN A 22  ? 0.08505 0.10545 0.14925 0.01270  0.02120  -0.02020 23  ASN A O   
197  C  CB  . ASN A 22  ? 0.10195 0.11065 0.12605 -0.01040 0.01570  -0.00230 23  ASN A CB  
198  C  CG  . ASN A 22  ? 0.10235 0.09915 0.13645 0.00210  0.00740  0.00610  23  ASN A CG  
199  O  OD1 . ASN A 22  ? 0.10645 0.11455 0.13835 -0.00840 0.00890  0.00590  23  ASN A OD1 
200  N  ND2 . ASN A 22  ? 0.10565 0.09285 0.16605 -0.01310 -0.00410 0.02550  23  ASN A ND2 
201  N  N   . GLY A 23  ? 0.07655 0.10565 0.13515 0.00960  0.00780  -0.00360 24  GLY A N   
202  C  CA  . GLY A 23  ? 0.10475 0.10455 0.13785 0.01010  0.01960  0.01580  24  GLY A CA  
203  C  C   . GLY A 23  ? 0.08795 0.11975 0.14555 0.01180  0.02930  0.01620  24  GLY A C   
204  O  O   . GLY A 23  ? 0.10325 0.13635 0.17865 0.01790  0.02920  0.03160  24  GLY A O   
205  N  N   . HIS A 24  ? 0.11175 0.10435 0.12015 0.02630  0.00160  0.00580  25  HIS A N   
206  C  CA  . HIS A 24  ? 0.13575 0.12185 0.12615 0.01720  0.01370  0.00040  25  HIS A CA  
207  C  C   . HIS A 24  ? 0.13805 0.10195 0.12435 0.03400  0.04180  0.00370  25  HIS A C   
208  O  O   . HIS A 24  ? 0.14415 0.09455 0.11645 0.03240  0.04780  0.00390  25  HIS A O   
209  C  CB  . HIS A 24  ? 0.14885 0.16345 0.16325 0.01600  0.02520  -0.04580 25  HIS A CB  
210  C  CG  . HIS A 24  ? 0.14785 0.20065 0.19315 0.02700  0.01650  -0.07560 25  HIS A CG  
211  N  ND1 . HIS A 24  ? 0.18455 0.24035 0.20985 -0.00050 0.02390  -0.08000 25  HIS A ND1 
212  C  CD2 . HIS A 24  ? 0.15115 0.19295 0.21245 0.02500  -0.00240 -0.08200 25  HIS A CD2 
213  C  CE1 . HIS A 24  ? 0.18845 0.23105 0.22125 -0.00020 0.00920  -0.09370 25  HIS A CE1 
214  N  NE2 . HIS A 24  ? 0.16705 0.20845 0.22215 0.00040  0.01380  -0.09580 25  HIS A NE2 
215  N  N   . LYS A 25  ? 0.15245 0.08805 0.12245 0.02730  0.03350  0.01030  26  LYS A N   
216  C  CA  . LYS A 25  ? 0.15485 0.10305 0.12985 0.03480  0.02010  0.00130  26  LYS A CA  
217  C  C   . LYS A 25  ? 0.15625 0.10555 0.11755 0.03890  0.02440  0.00070  26  LYS A C   
218  O  O   . LYS A 25  ? 0.21805 0.13805 0.11715 0.07020  0.05070  0.01090  26  LYS A O   
219  C  CB  . LYS A 25  ? 0.15485 0.15085 0.14475 0.03670  0.01370  0.00390  26  LYS A CB  
220  C  CG  . LYS A 25  ? 0.16585 0.17835 0.19805 0.04360  0.00750  0.01870  26  LYS A CG  
221  C  CD  . LYS A 25  ? 0.22645 0.23505 0.24595 0.02960  0.00170  0.01900  26  LYS A CD  
224  N  N   . PHE A 26  ? 0.11095 0.08375 0.13165 0.00970  0.03170  0.00580  27  PHE A N   
225  C  CA  . PHE A 26  ? 0.12385 0.09505 0.12245 0.01090  0.02170  0.01010  27  PHE A CA  
226  C  C   . PHE A 26  ? 0.09295 0.10045 0.12655 0.00610  0.02410  0.01960  27  PHE A C   
227  O  O   . PHE A 26  ? 0.10515 0.10715 0.11925 0.00560  0.02450  0.01480  27  PHE A O   
228  C  CB  . PHE A 26  ? 0.11735 0.10935 0.11045 0.00690  0.02420  0.00260  27  PHE A CB  
229  C  CG  . PHE A 26  ? 0.11575 0.10905 0.10885 0.01780  -0.00100 0.00230  27  PHE A CG  
230  C  CD1 . PHE A 26  ? 0.11985 0.11155 0.11235 0.00910  0.01090  0.00800  27  PHE A CD1 
231  C  CD2 . PHE A 26  ? 0.10405 0.12255 0.11665 0.00990  -0.00510 -0.01500 27  PHE A CD2 
232  C  CE1 . PHE A 26  ? 0.09095 0.12265 0.12435 0.00530  0.01020  0.00020  27  PHE A CE1 
233  C  CE2 . PHE A 26  ? 0.10455 0.10935 0.10865 0.00290  -0.00760 -0.01570 27  PHE A CE2 
234  C  CZ  . PHE A 26  ? 0.11235 0.12015 0.11585 -0.00210 -0.00970 -0.02400 27  PHE A CZ  
235  N  N   . SER A 27  ? 0.08255 0.10165 0.13405 0.01970  0.01810  0.01500  28  SER A N   
236  C  CA  . SER A 27  ? 0.09485 0.09575 0.13295 0.01400  0.00870  0.00520  28  SER A CA  
237  C  C   . SER A 27  ? 0.08335 0.08865 0.10465 0.00060  0.01340  0.01400  28  SER A C   
238  O  O   . SER A 27  ? 0.10395 0.10175 0.09615 0.00830  0.01060  0.00220  28  SER A O   
239  C  CB  . SER A 27  ? 0.08835 0.12805 0.17225 -0.00850 -0.00750 0.02150  28  SER A CB  
240  O  OG  . SER A 27  ? 0.10245 0.13515 0.21435 -0.00870 -0.01750 0.02890  28  SER A OG  
241  N  N   . VAL A 28  ? 0.06695 0.08355 0.12545 0.00520  0.00800  -0.00110 29  VAL A N   
242  C  CA  . VAL A 28  ? 0.08425 0.09775 0.11855 -0.00310 0.00970  0.00750  29  VAL A CA  
243  C  C   . VAL A 28  ? 0.08715 0.10835 0.10425 0.00150  -0.01110 -0.00500 29  VAL A C   
244  O  O   . VAL A 28  ? 0.10365 0.09935 0.10535 0.00370  -0.00330 -0.00560 29  VAL A O   
245  C  CB  . VAL A 28  ? 0.07795 0.09195 0.12035 -0.00050 0.01400  0.00590  29  VAL A CB  
246  C  CG1 . VAL A 28  ? 0.09085 0.09525 0.12875 -0.00060 0.01430  0.01050  29  VAL A CG1 
247  C  CG2 . VAL A 28  ? 0.08855 0.08175 0.11275 0.00690  0.01530  -0.00450 29  VAL A CG2 
248  N  N   . SER A 29  ? 0.08245 0.09015 0.10665 0.00300  0.00310  0.00520  30  SER A N   
249  C  CA  . SER A 29  ? 0.08695 0.08785 0.10805 0.01090  -0.00710 0.00700  30  SER A CA  
250  C  C   . SER A 29  ? 0.10845 0.07785 0.09335 0.00600  -0.00450 -0.00480 30  SER A C   
251  O  O   . SER A 29  ? 0.13445 0.11965 0.09555 0.02250  -0.02490 -0.02970 30  SER A O   
252  C  CB  . SER A 29  ? 0.08755 0.10885 0.12465 -0.00880 0.00010  0.01300  30  SER A CB  
253  O  OG  . SER A 29  ? 0.10185 0.11395 0.16155 -0.01030 0.01890  0.01790  30  SER A OG  
254  N  N   . GLY A 30  ? 0.08775 0.08005 0.10235 0.01080  0.00490  -0.00050 31  GLY A N   
255  C  CA  . GLY A 30  ? 0.10335 0.07025 0.11555 0.00890  -0.00490 -0.00570 31  GLY A CA  
256  C  C   . GLY A 30  ? 0.08755 0.08275 0.09995 -0.00130 0.00440  0.00040  31  GLY A C   
257  O  O   . GLY A 30  ? 0.09815 0.09355 0.09255 -0.00260 0.00150  -0.00280 31  GLY A O   
258  N  N   . GLU A 31  ? 0.07915 0.07975 0.10605 0.00630  0.01670  0.01260  32  GLU A N   
259  C  CA  . GLU A 31  ? 0.08245 0.07605 0.11765 0.00830  0.02260  0.00540  32  GLU A CA  
260  C  C   . GLU A 31  ? 0.08855 0.07225 0.11025 -0.00280 0.01530  0.01980  32  GLU A C   
261  O  O   . GLU A 31  ? 0.08335 0.09215 0.12305 0.00090  0.00380  -0.00320 32  GLU A O   
262  C  CB  . GLU A 31  ? 0.09485 0.09445 0.14735 -0.01260 0.02980  0.01080  32  GLU A CB  
263  C  CG  . GLU A 31  ? 0.11475 0.10305 0.13835 -0.00140 0.03070  0.00940  32  GLU A CG  
264  C  CD  . GLU A 31  ? 0.12105 0.10995 0.14475 -0.01200 0.01990  0.02080  32  GLU A CD  
265  O  OE1 . GLU A 31  ? 0.12805 0.13855 0.16275 -0.00460 0.04150  0.03130  32  GLU A OE1 
266  O  OE2 . GLU A 31  ? 0.13225 0.10775 0.14775 -0.01200 0.02060  0.02030  32  GLU A OE2 
267  N  N   . GLY A 32  ? 0.08465 0.09125 0.10525 0.01270  0.01260  0.00500  33  GLY A N   
268  C  CA  . GLY A 32  ? 0.08735 0.09585 0.10975 0.02830  -0.00330 -0.01840 33  GLY A CA  
269  C  C   . GLY A 32  ? 0.07825 0.07835 0.10085 0.01450  0.00350  0.00910  33  GLY A C   
270  O  O   . GLY A 32  ? 0.09685 0.08515 0.09885 -0.00850 -0.00710 0.01040  33  GLY A O   
271  N  N   . GLU A 33  ? 0.08675 0.07215 0.11385 0.01310  0.01520  0.00660  34  GLU A N   
272  C  CA  . GLU A 33  ? 0.09375 0.07885 0.13045 0.01850  0.02600  0.01400  34  GLU A CA  
273  C  C   . GLU A 33  ? 0.06875 0.07595 0.12985 0.01590  0.02010  0.01010  34  GLU A C   
274  O  O   . GLU A 33  ? 0.08615 0.09455 0.13645 -0.00840 0.01170  -0.00340 34  GLU A O   
275  C  CB  . GLU A 33  ? 0.15085 0.12025 0.13765 0.03620  0.01330  0.02940  34  GLU A CB  
276  C  CG  . GLU A 33  ? 0.14585 0.15105 0.15775 0.01760  -0.00510 0.04080  34  GLU A CG  
277  C  CD  . GLU A 33  ? 0.17235 0.20015 0.18365 0.02810  -0.00440 0.04630  34  GLU A CD  
278  O  OE1 . GLU A 33  ? 0.18755 0.21495 0.18045 0.03250  0.01840  0.07870  34  GLU A OE1 
279  O  OE2 . GLU A 33  ? 0.16575 0.21365 0.19365 0.02030  -0.02180 0.06280  34  GLU A OE2 
280  N  N   . GLY A 34  ? 0.08395 0.08675 0.11495 0.01760  0.03420  0.00840  35  GLY A N   
281  C  CA  . GLY A 34  ? 0.08195 0.09385 0.13785 0.01960  0.02140  -0.00290 35  GLY A CA  
282  C  C   . GLY A 34  ? 0.07885 0.09655 0.12565 0.01090  0.00730  -0.00220 35  GLY A C   
283  O  O   . GLY A 34  ? 0.08035 0.10225 0.14085 0.00230  0.01120  -0.00930 35  GLY A O   
284  N  N   . ASP A 35  ? 0.07275 0.09275 0.11585 0.01650  0.01340  -0.00140 36  ASP A N   
286  C  CA  B ASP A 35  ? 0.09955 0.11305 0.12185 0.01370  0.01890  0.00290  36  ASP A CA  
287  C  C   . ASP A 35  ? 0.08175 0.09565 0.11445 0.00130  0.00510  -0.00890 36  ASP A C   
288  O  O   . ASP A 35  ? 0.09025 0.10655 0.13135 -0.00660 0.01800  -0.01100 36  ASP A O   
290  C  CB  B ASP A 35  ? 0.12975 0.15255 0.13915 0.03890  0.02660  0.03510  36  ASP A CB  
292  C  CG  B ASP A 35  ? 0.14825 0.15935 0.14775 0.04230  0.03470  0.03810  36  ASP A CG  
294  O  OD1 B ASP A 35  ? 0.14285 0.14625 0.14995 0.02390  0.05180  0.01110  36  ASP A OD1 
296  O  OD2 B ASP A 35  ? 0.18395 0.16155 0.16125 0.04850  0.02020  0.05170  36  ASP A OD2 
297  N  N   . ALA A 36  ? 0.09295 0.09535 0.11385 0.00920  0.00330  -0.01290 37  ALA A N   
298  C  CA  . ALA A 36  ? 0.08025 0.11355 0.11315 0.00490  -0.00050 -0.00550 37  ALA A CA  
299  C  C   . ALA A 36  ? 0.08665 0.09355 0.10525 0.01460  -0.00110 -0.01050 37  ALA A C   
300  O  O   . ALA A 36  ? 0.08005 0.11875 0.11795 0.01290  0.01300  0.00690  37  ALA A O   
301  C  CB  . ALA A 36  ? 0.09305 0.12055 0.11855 0.02090  -0.01810 -0.00760 37  ALA A CB  
302  N  N   . THR A 37  ? 0.09625 0.09245 0.10355 0.02020  -0.00730 -0.02160 38  THR A N   
303  C  CA  . THR A 37  ? 0.08595 0.10165 0.12625 0.02870  -0.03100 -0.01390 38  THR A CA  
304  C  C   . THR A 37  ? 0.09115 0.10025 0.11875 0.02060  0.00320  -0.00330 38  THR A C   
305  O  O   . THR A 37  ? 0.08915 0.11915 0.13485 0.01320  0.00860  -0.00010 38  THR A O   
306  C  CB  . THR A 37  ? 0.09935 0.10055 0.16995 0.01550  -0.01570 0.00310  38  THR A CB  
307  O  OG1 . THR A 37  ? 0.12145 0.11735 0.19395 -0.00190 -0.02960 -0.01030 38  THR A OG1 
308  C  CG2 . THR A 37  ? 0.09175 0.11035 0.18345 0.03890  0.00810  0.02030  38  THR A CG2 
309  N  N   . TYR A 38  ? 0.09075 0.09845 0.10845 0.01460  0.00410  0.00260  39  TYR A N   
310  C  CA  . TYR A 38  ? 0.09905 0.12475 0.12085 0.00400  -0.00600 -0.01950 39  TYR A CA  
311  C  C   . TYR A 38  ? 0.08525 0.11985 0.12865 0.00040  -0.00990 -0.01030 39  TYR A C   
312  O  O   . TYR A 38  ? 0.08735 0.13195 0.15225 -0.00250 -0.00760 -0.02760 39  TYR A O   
313  C  CB  . TYR A 38  ? 0.11475 0.13295 0.12665 0.00440  -0.00680 -0.00270 39  TYR A CB  
314  C  CG  . TYR A 38  ? 0.12875 0.13025 0.14195 0.03930  -0.00010 0.00310  39  TYR A CG  
315  C  CD1 . TYR A 38  ? 0.14905 0.15835 0.14295 0.04400  -0.00710 0.00520  39  TYR A CD1 
316  C  CD2 . TYR A 38  ? 0.15275 0.14005 0.14775 0.04140  -0.01590 0.01850  39  TYR A CD2 
317  C  CE1 . TYR A 38  ? 0.15295 0.16545 0.14675 0.05810  -0.01050 0.00540  39  TYR A CE1 
318  C  CE2 . TYR A 38  ? 0.17795 0.15305 0.15455 0.05980  -0.01570 0.02670  39  TYR A CE2 
319  C  CZ  . TYR A 38  ? 0.18685 0.15765 0.15845 0.07880  -0.01060 0.00950  39  TYR A CZ  
320  O  OH  . TYR A 38  ? 0.23135 0.17595 0.17375 0.11120  0.01810  0.00560  39  TYR A OH  
321  N  N   . GLY A 39  ? 0.08545 0.10715 0.11025 0.01820  -0.00280 0.01080  40  GLY A N   
322  C  CA  . GLY A 39  ? 0.09325 0.10125 0.10095 0.00890  0.00350  -0.00130 40  GLY A CA  
323  C  C   . GLY A 39  ? 0.08285 0.10655 0.12175 -0.00490 -0.00550 -0.00590 40  GLY A C   
324  O  O   . GLY A 39  ? 0.11505 0.08845 0.13095 0.00270  0.00080  0.00210  40  GLY A O   
325  N  N   . LYS A 40  ? 0.07155 0.11425 0.11245 0.01120  0.00340  0.00700  41  LYS A N   
326  C  CA  . LYS A 40  ? 0.07095 0.11405 0.11475 0.00810  0.01140  0.00130  41  LYS A CA  
327  C  C   . LYS A 40  ? 0.08585 0.08505 0.12315 0.00230  0.00810  -0.00100 41  LYS A C   
328  O  O   . LYS A 40  ? 0.09315 0.09315 0.16375 0.00240  0.00550  -0.02550 41  LYS A O   
329  C  CB  . LYS A 40  ? 0.09795 0.12845 0.11505 0.00720  0.01000  0.01410  41  LYS A CB  
330  C  CG  . LYS A 40  ? 0.10785 0.16315 0.13435 0.02080  0.01210  0.02560  41  LYS A CG  
331  C  CD  . LYS A 40  ? 0.11015 0.20765 0.16245 0.05430  0.00890  0.04390  41  LYS A CD  
332  C  CE  . LYS A 40  ? 0.15115 0.24785 0.19005 0.05550  0.03580  0.05280  41  LYS A CE  
333  N  NZ  . LYS A 40  ? 0.16455 0.27105 0.20295 0.05380  0.03950  0.06260  41  LYS A NZ  
334  N  N   A LEU A 41  ? 0.08395 0.09315 0.09195 0.00030  0.02450  -0.01100 42  LEU A N   
336  C  CA  A LEU A 41  ? 0.06635 0.07045 0.09355 0.00910  0.01250  -0.00210 42  LEU A CA  
338  C  C   A LEU A 41  ? 0.07295 0.08785 0.10595 0.02370  0.00720  0.00570  42  LEU A C   
340  O  O   A LEU A 41  ? 0.09095 0.08915 0.12105 0.00030  0.01720  0.01350  42  LEU A O   
342  C  CB  A LEU A 41  ? 0.06675 0.05885 0.10415 -0.00220 0.00690  -0.00410 42  LEU A CB  
344  C  CG  A LEU A 41  ? 0.07595 0.06285 0.11105 -0.01320 -0.00280 0.00430  42  LEU A CG  
346  C  CD1 A LEU A 41  ? 0.05985 0.05735 0.13205 -0.01960 0.01550  0.01160  42  LEU A CD1 
348  C  CD2 A LEU A 41  ? 0.06695 0.07025 0.10105 -0.00620 -0.00350 0.00090  42  LEU A CD2 
350  N  N   . THR A 42  ? 0.07875 0.09705 0.10655 0.00660  0.01260  0.00420  43  THR A N   
351  C  CA  A THR A 42  ? 0.08275 0.12355 0.10835 0.00970  0.01830  -0.01050 43  THR A CA  
353  C  C   . THR A 42  ? 0.08715 0.11095 0.10145 -0.00370 0.02250  -0.02580 43  THR A C   
354  O  O   . THR A 42  ? 0.10565 0.11075 0.12525 -0.01930 0.01450  -0.02060 43  THR A O   
355  C  CB  A THR A 42  ? 0.11635 0.16415 0.10865 0.02080  0.00270  -0.01600 43  THR A CB  
357  O  OG1 A THR A 42  ? 0.11205 0.15845 0.11235 0.00890  -0.00190 0.01240  43  THR A OG1 
359  C  CG2 A THR A 42  ? 0.16465 0.20175 0.11835 0.02150  0.02550  -0.02680 43  THR A CG2 
361  N  N   . LEU A 43  ? 0.09515 0.10395 0.10075 0.00500  0.02030  -0.00860 44  LEU A N   
362  C  CA  . LEU A 43  ? 0.09525 0.11805 0.09215 -0.01270 0.01560  -0.00210 44  LEU A CA  
363  C  C   . LEU A 43  ? 0.09625 0.11615 0.10085 -0.01550 -0.00130 -0.00140 44  LEU A C   
364  O  O   . LEU A 43  ? 0.09145 0.12715 0.12755 -0.02550 0.01860  -0.03000 44  LEU A O   
365  C  CB  . LEU A 43  ? 0.15715 0.11945 0.08875 -0.03040 0.01770  -0.00110 44  LEU A CB  
366  C  CG  . LEU A 43  ? 0.20325 0.09965 0.09595 -0.04680 0.02740  -0.02330 44  LEU A CG  
367  C  CD1 . LEU A 43  ? 0.25845 0.13115 0.09805 -0.04730 0.03990  -0.03010 44  LEU A CD1 
368  C  CD2 . LEU A 43  ? 0.18705 0.12525 0.11125 -0.03500 -0.00690 -0.02450 44  LEU A CD2 
369  N  N   . LYS A 44  ? 0.08455 0.11395 0.09195 0.00440  0.01010  0.00210  45  LYS A N   
370  C  CA  . LYS A 44  ? 0.09395 0.11375 0.08245 0.00590  0.01250  -0.00450 45  LYS A CA  
371  C  C   . LYS A 44  ? 0.09715 0.09085 0.08445 -0.01170 0.00970  -0.00590 45  LYS A C   
372  O  O   . LYS A 44  ? 0.10495 0.09135 0.09245 -0.00890 -0.00510 0.00580  45  LYS A O   
373  C  CB  . LYS A 44  ? 0.12485 0.12515 0.08115 0.00800  0.01810  -0.00640 45  LYS A CB  
374  C  CG  . LYS A 44  ? 0.12175 0.12375 0.09795 -0.01380 0.02790  -0.00490 45  LYS A CG  
375  C  CD  . LYS A 44  ? 0.14995 0.11715 0.10935 0.00350  0.03280  0.00400  45  LYS A CD  
376  C  CE  . LYS A 44  ? 0.17975 0.13135 0.09685 -0.00880 0.02320  -0.00320 45  LYS A CE  
377  N  NZ  . LYS A 44  ? 0.20905 0.13025 0.09305 -0.00050 0.04460  0.00740  45  LYS A NZ  
378  N  N   . PHE A 45  ? 0.10515 0.08275 0.09525 -0.00550 -0.00120 -0.00880 46  PHE A N   
379  C  CA  . PHE A 45  ? 0.10235 0.09305 0.09445 0.00740  0.00110  0.00170  46  PHE A CA  
380  C  C   . PHE A 45  ? 0.09475 0.08945 0.09955 0.01000  0.00760  -0.00610 46  PHE A C   
381  O  O   . PHE A 45  ? 0.12255 0.09485 0.10885 0.00310  0.00190  -0.01540 46  PHE A O   
382  C  CB  . PHE A 45  ? 0.10735 0.08785 0.11485 -0.00060 -0.00300 0.00080  46  PHE A CB  
383  C  CG  . PHE A 45  ? 0.10265 0.08005 0.09585 -0.00640 0.00330  0.01180  46  PHE A CG  
384  C  CD1 . PHE A 45  ? 0.11575 0.09335 0.09355 -0.01240 -0.00790 0.01580  46  PHE A CD1 
385  C  CD2 . PHE A 45  ? 0.10395 0.10835 0.10685 -0.00740 0.00050  0.01080  46  PHE A CD2 
386  C  CE1 . PHE A 45  ? 0.10965 0.08185 0.10365 -0.01070 0.00870  0.01960  46  PHE A CE1 
387  C  CE2 . PHE A 45  ? 0.10615 0.11255 0.09305 0.00000  -0.00300 -0.00090 46  PHE A CE2 
388  C  CZ  . PHE A 45  ? 0.10045 0.10565 0.10375 0.00920  -0.00200 0.01910  46  PHE A CZ  
389  N  N   . ILE A 46  ? 0.09465 0.09025 0.11215 0.01950  0.01120  -0.00620 47  ILE A N   
390  C  CA  A ILE A 46  ? 0.10695 0.09295 0.10485 0.00220  0.03800  0.00420  47  ILE A CA  
392  C  C   . ILE A 46  ? 0.08665 0.08985 0.10175 0.01100  0.01900  -0.01430 47  ILE A C   
393  O  O   . ILE A 46  ? 0.09665 0.11105 0.10945 0.00820  0.02140  -0.01660 47  ILE A O   
394  C  CB  A ILE A 46  ? 0.14535 0.10715 0.10815 -0.01310 0.04260  0.00060  47  ILE A CB  
396  C  CG1 A ILE A 46  ? 0.16355 0.12935 0.11965 -0.02770 0.02560  0.01510  47  ILE A CG1 
398  C  CG2 A ILE A 46  ? 0.17055 0.10785 0.10515 -0.01470 0.06570  -0.00320 47  ILE A CG2 
400  C  CD1 A ILE A 46  ? 0.15425 0.13245 0.12265 -0.03950 0.02300  0.01040  47  ILE A CD1 
402  N  N   . CYS A 47  ? 0.09825 0.08365 0.09835 0.01170  0.02540  -0.00170 48  CYS A N   
403  C  CA  . CYS A 47  ? 0.10185 0.09175 0.11735 0.00960  0.01190  -0.01700 48  CYS A CA  
404  C  C   . CYS A 47  ? 0.11435 0.12205 0.12475 0.00860  0.01300  -0.01500 48  CYS A C   
405  O  O   . CYS A 47  ? 0.11755 0.19725 0.10965 -0.00930 0.02040  -0.00940 48  CYS A O   
406  C  CB  . CYS A 47  ? 0.11795 0.10435 0.13255 0.00950  0.00670  -0.00830 48  CYS A CB  
407  S  SG  . CYS A 47  ? 0.11215 0.10125 0.13975 0.00360  0.01260  -0.01670 48  CYS A SG  
408  N  N   . THR A 48  ? 0.09105 0.11305 0.14075 -0.00730 0.01930  0.00370  49  THR A N   
409  C  CA  . THR A 48  ? 0.11565 0.12595 0.16165 0.00150  0.02610  -0.01900 49  THR A CA  
410  C  C   . THR A 48  ? 0.11985 0.13615 0.18155 -0.01080 0.03300  -0.00570 49  THR A C   
411  O  O   . THR A 48  ? 0.14665 0.13575 0.21645 -0.02630 0.06670  -0.00150 49  THR A O   
412  C  CB  . THR A 48  ? 0.11915 0.12115 0.16195 0.00350  0.02130  -0.00830 49  THR A CB  
413  O  OG1 . THR A 48  ? 0.11105 0.13515 0.17065 -0.01400 0.01480  -0.01170 49  THR A OG1 
414  C  CG2 . THR A 48  ? 0.12565 0.13475 0.16185 -0.00940 0.02780  -0.00010 49  THR A CG2 
415  N  N   . THR A 49  ? 0.11385 0.11805 0.14525 -0.00350 0.03020  -0.00900 50  THR A N   
416  C  CA  . THR A 49  ? 0.12375 0.12835 0.13775 0.01110  0.03860  -0.00270 50  THR A CA  
417  C  C   . THR A 49  ? 0.11665 0.14455 0.14535 0.01520  0.03090  -0.00460 50  THR A C   
418  O  O   . THR A 49  ? 0.16195 0.16795 0.16785 0.04570  0.02900  -0.02990 50  THR A O   
419  C  CB  . THR A 49  ? 0.10895 0.14565 0.13455 -0.00260 0.03110  -0.00250 50  THR A CB  
420  O  OG1 . THR A 49  ? 0.08775 0.14815 0.13325 0.01610  0.02970  0.00440  50  THR A OG1 
421  C  CG2 . THR A 49  ? 0.10035 0.15075 0.13265 -0.00470 0.01620  -0.02310 50  THR A CG2 
422  N  N   . GLY A 50  ? 0.13135 0.14135 0.12875 -0.01080 0.03410  -0.02550 51  GLY A N   
423  C  CA  . GLY A 50  ? 0.12935 0.15865 0.13745 -0.01660 0.02390  -0.02790 51  GLY A CA  
424  C  C   . GLY A 50  ? 0.13205 0.14415 0.14295 -0.01010 0.02750  -0.03100 51  GLY A C   
425  O  O   . GLY A 50  ? 0.15515 0.14345 0.17055 -0.00590 0.00540  -0.03030 51  GLY A O   
426  N  N   . LYS A 51  ? 0.12825 0.13145 0.14295 0.00190  0.02990  -0.01640 52  LYS A N   
427  C  CA  . LYS A 51  ? 0.13235 0.13635 0.15575 -0.00770 0.03280  -0.02400 52  LYS A CA  
428  C  C   . LYS A 51  ? 0.10675 0.11735 0.14325 0.00140  0.01530  -0.01310 52  LYS A C   
429  O  O   . LYS A 51  ? 0.11455 0.12625 0.16445 0.00160  0.01420  -0.00850 52  LYS A O   
430  C  CB  . LYS A 51  ? 0.17745 0.18475 0.19585 -0.03650 0.03890  -0.02580 52  LYS A CB  
435  N  N   . LEU A 52  ? 0.11575 0.11805 0.12565 -0.01760 0.02460  -0.00830 53  LEU A N   
436  C  CA  . LEU A 52  ? 0.12025 0.11345 0.12795 0.00500  0.02340  -0.00540 53  LEU A CA  
437  C  C   . LEU A 52  ? 0.10315 0.10445 0.12765 0.00470  0.00940  -0.01050 53  LEU A C   
438  O  O   . LEU A 52  ? 0.13785 0.12875 0.11995 -0.01400 0.00680  -0.00010 53  LEU A O   
439  C  CB  . LEU A 52  ? 0.11845 0.10865 0.13155 0.00510  0.00070  -0.01540 53  LEU A CB  
440  C  CG  . LEU A 52  ? 0.09345 0.11825 0.13895 0.00320  -0.00270 -0.01050 53  LEU A CG  
441  C  CD1 . LEU A 52  ? 0.09915 0.09965 0.14075 0.00110  -0.00030 0.00250  53  LEU A CD1 
442  C  CD2 . LEU A 52  ? 0.08885 0.12265 0.13975 0.01490  -0.00960 -0.01600 53  LEU A CD2 
443  N  N   . PRO A 53  ? 0.11355 0.11245 0.11675 0.00680  0.00790  -0.01390 54  PRO A N   
444  C  CA  . PRO A 53  ? 0.09635 0.11735 0.12965 0.00480  0.01340  -0.00040 54  PRO A CA  
445  C  C   . PRO A 53  ? 0.10995 0.09655 0.12015 0.00970  0.01330  -0.00070 54  PRO A C   
446  O  O   . PRO A 53  ? 0.12225 0.10335 0.12765 0.00900  0.01710  -0.00340 54  PRO A O   
447  C  CB  . PRO A 53  ? 0.11455 0.13685 0.15635 0.02220  0.01710  -0.00950 54  PRO A CB  
448  C  CG  . PRO A 53  ? 0.12885 0.13035 0.14315 0.01940  0.01720  -0.00880 54  PRO A CG  
449  C  CD  . PRO A 53  ? 0.12565 0.12085 0.12305 0.00340  -0.00820 -0.00420 54  PRO A CD  
450  N  N   . VAL A 54  ? 0.09325 0.10045 0.10225 0.01560  -0.00310 -0.00930 55  VAL A N   
451  C  CA  . VAL A 54  ? 0.09375 0.10935 0.08575 0.00080  0.00230  -0.01270 55  VAL A CA  
452  C  C   . VAL A 54  ? 0.10255 0.08615 0.09715 -0.00330 0.00400  -0.00670 55  VAL A C   
453  O  O   . VAL A 54  ? 0.09945 0.08845 0.11465 -0.00020 0.01830  0.00550  55  VAL A O   
454  C  CB  . VAL A 54  ? 0.10055 0.11215 0.09335 -0.00460 0.01130  -0.00610 55  VAL A CB  
455  C  CG1 . VAL A 54  ? 0.12395 0.10875 0.11485 0.00720  -0.01770 0.00080  55  VAL A CG1 
456  C  CG2 . VAL A 54  ? 0.11435 0.07785 0.10325 -0.01440 0.00380  -0.01500 55  VAL A CG2 
457  N  N   . PRO A 55  ? 0.09645 0.08475 0.10565 -0.00670 0.01280  0.00040  56  PRO A N   
458  C  CA  . PRO A 55  ? 0.09995 0.08935 0.08885 -0.01520 -0.01350 0.00030  56  PRO A CA  
459  C  C   . PRO A 55  ? 0.08125 0.09815 0.08965 -0.01220 -0.00120 -0.00710 56  PRO A C   
460  O  O   . PRO A 55  ? 0.08695 0.10515 0.08335 0.00010  -0.00370 -0.00080 56  PRO A O   
461  C  CB  . PRO A 55  ? 0.12305 0.08835 0.10655 -0.01610 -0.00700 -0.00390 56  PRO A CB  
462  C  CG  . PRO A 55  ? 0.10905 0.09535 0.11905 -0.01210 -0.01380 -0.00560 56  PRO A CG  
463  C  CD  . PRO A 55  ? 0.09495 0.08705 0.11605 -0.02520 0.00440  0.00250  56  PRO A CD  
464  N  N   . TRP A 56  ? 0.09465 0.08835 0.08345 -0.00300 0.00730  -0.00400 57  TRP A N   
465  C  CA  . TRP A 56  ? 0.10045 0.07595 0.08305 -0.00850 0.00160  0.02320  57  TRP A CA  
466  C  C   . TRP A 56  ? 0.09315 0.08875 0.07885 -0.00860 -0.00830 0.00330  57  TRP A C   
467  O  O   . TRP A 56  ? 0.09205 0.08895 0.06925 -0.00500 0.00830  -0.00360 57  TRP A O   
468  C  CB  . TRP A 56  ? 0.08315 0.10035 0.08645 -0.00590 -0.00430 0.01120  57  TRP A CB  
469  C  CG  . TRP A 56  ? 0.10205 0.09385 0.07215 -0.01560 -0.00190 0.00390  57  TRP A CG  
470  C  CD1 . TRP A 56  ? 0.10745 0.10935 0.07835 -0.00480 0.00650  0.00620  57  TRP A CD1 
471  C  CD2 . TRP A 56  ? 0.09455 0.08715 0.08985 -0.01850 -0.00030 0.00300  57  TRP A CD2 
472  N  NE1 . TRP A 56  ? 0.10665 0.10885 0.08025 -0.02000 0.00910  0.00640  57  TRP A NE1 
473  C  CE2 . TRP A 56  ? 0.09635 0.10155 0.08485 -0.00410 0.00030  0.00460  57  TRP A CE2 
474  C  CE3 . TRP A 56  ? 0.09865 0.08345 0.08685 -0.00100 -0.01430 -0.00830 57  TRP A CE3 
475  C  CZ2 . TRP A 56  ? 0.10545 0.08585 0.10505 0.00910  0.00300  0.00220  57  TRP A CZ2 
476  C  CZ3 . TRP A 56  ? 0.10045 0.08505 0.09145 -0.00140 -0.00350 0.00050  57  TRP A CZ3 
477  C  CH2 . TRP A 56  ? 0.10245 0.10065 0.10705 0.00920  0.01520  0.00690  57  TRP A CH2 
478  N  N   . PRO A 57  ? 0.08505 0.08315 0.09005 -0.01330 0.00140  0.00250  58  PRO A N   
479  C  CA  . PRO A 57  ? 0.07195 0.09115 0.08485 -0.00900 0.00270  -0.00260 58  PRO A CA  
480  C  C   . PRO A 57  ? 0.09665 0.09025 0.09485 -0.00710 -0.00300 0.01150  58  PRO A C   
481  O  O   . PRO A 57  ? 0.08725 0.09305 0.09195 -0.01490 -0.00820 0.00110  58  PRO A O   
482  C  CB  . PRO A 57  ? 0.09145 0.07965 0.09615 -0.01330 -0.00730 0.00100  58  PRO A CB  
483  C  CG  . PRO A 57  ? 0.09925 0.11085 0.09295 -0.01270 -0.01090 -0.01970 58  PRO A CG  
484  C  CD  . PRO A 57  ? 0.10505 0.09755 0.09005 -0.01040 -0.00510 -0.01660 58  PRO A CD  
485  N  N   . THR A 58  ? 0.07715 0.07845 0.10275 -0.00110 -0.01590 0.01100  59  THR A N   
486  C  CA  . THR A 58  ? 0.09365 0.07965 0.09015 -0.00300 -0.02060 0.00350  59  THR A CA  
487  C  C   . THR A 58  ? 0.07305 0.08725 0.09055 -0.00530 -0.00360 -0.00720 59  THR A C   
488  O  O   . THR A 58  ? 0.07365 0.08765 0.08215 -0.00080 0.00560  -0.01290 59  THR A O   
489  C  CB  . THR A 58  ? 0.08095 0.08425 0.10695 -0.01420 0.00940  0.00390  59  THR A CB  
490  O  OG1 . THR A 58  ? 0.08295 0.07295 0.10175 -0.01280 -0.00500 -0.00040 59  THR A OG1 
491  C  CG2 . THR A 58  ? 0.10295 0.10165 0.08515 -0.01990 0.00580  -0.00700 59  THR A CG2 
492  N  N   . LEU A 59  ? 0.08535 0.08495 0.09305 -0.00550 0.00290  -0.00950 60  LEU A N   
493  C  CA  . LEU A 59  ? 0.08605 0.07505 0.10445 -0.01510 0.01070  -0.00430 60  LEU A CA  
494  C  C   . LEU A 59  ? 0.09105 0.07615 0.08505 -0.00940 0.01180  0.00370  60  LEU A C   
495  O  O   . LEU A 59  ? 0.08025 0.07435 0.08545 -0.00920 0.00660  -0.00490 60  LEU A O   
496  C  CB  . LEU A 59  ? 0.08315 0.07535 0.09765 -0.00350 0.01030  0.00020  60  LEU A CB  
497  C  CG  . LEU A 59  ? 0.07345 0.08895 0.09925 -0.00530 0.00540  -0.00160 60  LEU A CG  
498  C  CD1 . LEU A 59  ? 0.08495 0.09155 0.11445 0.00630  0.01510  -0.00320 60  LEU A CD1 
499  C  CD2 . LEU A 59  ? 0.07425 0.11525 0.09145 0.01660  -0.00840 0.00790  60  LEU A CD2 
500  N  N   . VAL A 60  ? 0.07845 0.07995 0.07415 -0.00240 0.00000  0.01000  61  VAL A N   
501  C  CA  . VAL A 60  ? 0.06905 0.09735 0.06245 0.00010  -0.00840 -0.00220 61  VAL A CA  
502  C  C   . VAL A 60  ? 0.06075 0.09225 0.07205 -0.01300 -0.00810 0.00540  61  VAL A C   
503  O  O   . VAL A 60  ? 0.08295 0.08015 0.07565 -0.01380 -0.00590 -0.01000 61  VAL A O   
504  C  CB  . VAL A 60  ? 0.08405 0.09295 0.06975 0.00740  -0.02050 -0.01330 61  VAL A CB  
505  C  CG1 . VAL A 60  ? 0.06955 0.09285 0.08495 0.00600  -0.01450 -0.01160 61  VAL A CG1 
506  C  CG2 . VAL A 60  ? 0.11725 0.09835 0.05765 -0.00550 -0.01720 0.00370  61  VAL A CG2 
507  N  N   . THR A 61  ? 0.06545 0.09925 0.07455 0.00700  0.00220  0.01750  62  THR A N   
508  C  CA  . THR A 61  ? 0.06405 0.08945 0.07575 -0.00310 0.01260  0.01380  62  THR A CA  
509  C  C   . THR A 61  ? 0.07365 0.07015 0.07435 0.00620  0.00060  0.01060  62  THR A C   
510  O  O   . THR A 61  ? 0.09005 0.07255 0.06965 0.00870  0.00220  0.00300  62  THR A O   
511  C  CB  . THR A 61  ? 0.06845 0.09225 0.08855 0.00370  -0.00080 0.00980  62  THR A CB  
512  O  OG1 . THR A 61  ? 0.07345 0.08655 0.08405 0.01710  -0.00270 -0.00260 62  THR A OG1 
513  C  CG2 . THR A 61  ? 0.08455 0.12175 0.09005 -0.01250 -0.00100 0.00790  62  THR A CG2 
514  N  N   . THR A 62  ? 0.05505 0.08245 0.07735 0.00330  0.00090  -0.00400 63  THR A N   
515  C  CA  . THR A 62  ? 0.05445 0.06625 0.08185 0.00160  0.00190  0.00050  63  THR A CA  
516  C  C   . THR A 62  ? 0.05925 0.07605 0.06785 0.00570  0.00200  -0.00590 63  THR A C   
517  O  O   . THR A 62  ? 0.07625 0.08815 0.07785 -0.00140 -0.00180 0.00420  63  THR A O   
518  C  CB  . THR A 62  ? 0.06925 0.07435 0.08775 -0.00530 -0.00150 0.00020  63  THR A CB  
519  O  OG1 . THR A 62  ? 0.06905 0.07685 0.08865 0.00750  0.00190  -0.00350 63  THR A OG1 
520  C  CG2 . THR A 62  ? 0.07875 0.09085 0.11155 -0.00250 0.00500  -0.00190 63  THR A CG2 
521  N  N   . PHE A 63  ? 0.06895 0.07995 0.08285 0.00600  -0.00240 0.00490  64  PHE A N   
522  C  CA  . PHE A 63  ? 0.07565 0.07385 0.08315 0.00030  -0.00030 0.00910  64  PHE A CA  
523  C  C   . PHE A 63  ? 0.07645 0.06345 0.08315 -0.00210 -0.01140 -0.00110 64  PHE A C   
524  O  O   . PHE A 63  ? 0.07715 0.08255 0.08885 0.00640  -0.00480 0.00080  64  PHE A O   
525  C  CB  . PHE A 63  ? 0.08635 0.09565 0.07745 0.00090  0.00020  0.00070  64  PHE A CB  
526  C  CG  . PHE A 63  ? 0.07755 0.07745 0.07785 -0.01180 -0.00610 0.00470  64  PHE A CG  
527  C  CD1 . PHE A 63  ? 0.08705 0.07845 0.09645 -0.01370 0.00790  0.00500  64  PHE A CD1 
528  C  CD2 . PHE A 63  ? 0.07935 0.07825 0.08505 -0.00630 0.00820  0.00580  64  PHE A CD2 
529  C  CE1 . PHE A 63  ? 0.09215 0.07495 0.09635 -0.01040 0.00200  -0.00380 64  PHE A CE1 
530  C  CE2 . PHE A 63  ? 0.08545 0.08025 0.09085 -0.00700 0.03680  0.00510  64  PHE A CE2 
531  C  CZ  . PHE A 63  ? 0.08515 0.10525 0.09735 -0.00530 0.01400  -0.00560 64  PHE A CZ  
532  N  N1  . GYS A 64  ? 0.06175 0.07975 0.08015 0.00870  -0.00390 -0.00300 66  GYS A N1  
533  O  OG1 A GYS A 64  ? 0.08705 0.08905 0.09695 0.00880  -0.00570 -0.00090 66  GYS A OG1 
534  C  CB1 . GYS A 64  ? 0.06625 0.09295 0.07935 0.01380  -0.01050 0.00380  66  GYS A CB1 
535  C  CA1 . GYS A 64  ? 0.06995 0.08765 0.07435 -0.00450 -0.00540 0.00600  66  GYS A CA1 
536  C  C1  . GYS A 64  ? 0.05935 0.08235 0.09035 0.00140  0.00050  0.01050  66  GYS A C1  
537  N  N2  . GYS A 64  ? 0.07395 0.08065 0.08495 -0.00070 -0.00040 0.00640  66  GYS A N2  
538  N  N3  . GYS A 64  ? 0.07095 0.06775 0.09255 0.00050  -0.00350 0.00590  66  GYS A N3  
539  C  C2  . GYS A 64  ? 0.07715 0.06345 0.08025 -0.00710 0.01180  -0.00110 66  GYS A C2  
540  O  O2  . GYS A 64  ? 0.08685 0.07955 0.08565 0.00300  0.00020  0.00320  66  GYS A O2  
541  C  CA2 . GYS A 64  ? 0.07155 0.08075 0.08135 -0.00730 0.00020  0.00180  66  GYS A CA2 
542  C  CA3 . GYS A 64  ? 0.09355 0.08365 0.10125 -0.00540 -0.01900 0.00030  66  GYS A CA3 
543  C  CB2 . GYS A 64  ? 0.06795 0.07485 0.09235 0.01020  0.01950  -0.00200 66  GYS A CB2 
544  C  CG2 . GYS A 64  ? 0.08345 0.07605 0.09645 0.00950  0.00420  0.00470  66  GYS A CG2 
545  C  CD1 . GYS A 64  ? 0.07275 0.08835 0.09255 0.00610  -0.00720 -0.00340 66  GYS A CD1 
546  C  CD2 . GYS A 64  ? 0.07855 0.07025 0.10845 -0.00350 0.00940  -0.00000 66  GYS A CD2 
547  C  CE1 . GYS A 64  ? 0.07975 0.09545 0.10145 -0.00300 0.00440  -0.01340 66  GYS A CE1 
548  C  CE2 . GYS A 64  ? 0.09035 0.07955 0.11775 0.00900  -0.00210 -0.01470 66  GYS A CE2 
549  C  CZ  . GYS A 64  ? 0.06135 0.09105 0.10525 0.01420  0.00470  -0.01600 66  GYS A CZ  
550  O  OH  . GYS A 64  ? 0.07995 0.08685 0.12245 -0.00240 0.00300  -0.00540 66  GYS A OH  
551  C  C3  . GYS A 64  ? 0.08985 0.07775 0.07585 -0.00320 0.00550  0.00290  66  GYS A C3  
552  O  O3  . GYS A 64  ? 0.07625 0.07685 0.08725 0.00270  -0.00270 -0.00900 66  GYS A O3  
553  N  N   . VAL A 65  ? 0.09065 0.05785 0.08615 0.00820  -0.00470 0.00420  68  VAL A N   
554  C  CA  . VAL A 65  ? 0.07895 0.06665 0.09185 0.00230  0.01190  0.00500  68  VAL A CA  
555  C  C   . VAL A 65  ? 0.07595 0.07545 0.09315 -0.00150 -0.00430 -0.00660 68  VAL A C   
556  O  O   . VAL A 65  ? 0.08595 0.08255 0.09635 0.01180  -0.00280 -0.00640 68  VAL A O   
557  C  CB  . VAL A 65  ? 0.07685 0.08775 0.08775 0.00380  -0.00200 0.02300  68  VAL A CB  
558  C  CG1 . VAL A 65  ? 0.07925 0.10655 0.10845 0.01230  0.01400  -0.00590 68  VAL A CG1 
559  C  CG2 . VAL A 65  ? 0.09325 0.09875 0.07585 0.00800  0.00250  0.01880  68  VAL A CG2 
560  N  N   . GLN A 66  ? 0.07985 0.09055 0.08805 -0.00650 -0.00200 0.00130  69  GLN A N   
561  C  CA  . GLN A 66  ? 0.08625 0.09095 0.08535 0.00510  0.01850  -0.00640 69  GLN A CA  
562  C  C   . GLN A 66  ? 0.08655 0.08055 0.08635 0.00240  0.00630  0.00360  69  GLN A C   
563  O  O   . GLN A 66  ? 0.07905 0.08725 0.09155 0.01130  0.01660  0.00860  69  GLN A O   
564  C  CB  . GLN A 66  ? 0.10345 0.08745 0.08675 0.00130  0.01750  0.01360  69  GLN A CB  
565  C  CG  . GLN A 66  ? 0.10655 0.07515 0.10575 0.01150  0.01160  -0.00350 69  GLN A CG  
566  C  CD  . GLN A 66  ? 0.08225 0.09235 0.10635 0.01510  0.01350  0.00160  69  GLN A CD  
567  O  OE1 . GLN A 66  ? 0.11265 0.08985 0.08835 0.01120  0.00320  0.00810  69  GLN A OE1 
568  N  NE2 . GLN A 66  ? 0.07595 0.09015 0.13265 -0.00110 0.01920  -0.00260 69  GLN A NE2 
569  N  N   . CYS A 67  ? 0.09485 0.06505 0.09025 0.00310  0.00810  0.00200  70  CYS A N   
570  C  CA  . CYS A 67  ? 0.09605 0.07725 0.09405 0.01780  0.00210  0.00480  70  CYS A CA  
571  C  C   . CYS A 67  ? 0.08465 0.08195 0.09415 0.01260  0.00130  0.01040  70  CYS A C   
572  O  O   . CYS A 67  ? 0.09135 0.08865 0.10055 0.01770  0.00780  0.00360  70  CYS A O   
573  C  CB  . CYS A 67  ? 0.09115 0.08965 0.09795 -0.00170 0.01750  -0.00750 70  CYS A CB  
574  S  SG  . CYS A 67  ? 0.08775 0.09245 0.10325 0.00350  0.00230  -0.00220 70  CYS A SG  
575  N  N   . PHE A 68  ? 0.07975 0.10205 0.07815 0.01050  -0.01010 0.01870  71  PHE A N   
576  C  CA  . PHE A 68  ? 0.08895 0.10705 0.09645 0.00620  0.00590  0.00980  71  PHE A CA  
577  C  C   . PHE A 68  ? 0.08045 0.09695 0.10175 0.00680  -0.00570 0.01880  71  PHE A C   
578  O  O   . PHE A 68  ? 0.10265 0.13095 0.09895 0.00870  0.00750  0.03140  71  PHE A O   
579  C  CB  . PHE A 68  ? 0.07615 0.11665 0.08555 0.00220  0.01480  0.01050  71  PHE A CB  
580  C  CG  . PHE A 68  ? 0.08705 0.09645 0.07665 0.00770  0.01830  0.01170  71  PHE A CG  
581  C  CD1 . PHE A 68  ? 0.10045 0.08525 0.09665 0.00130  0.02300  0.00400  71  PHE A CD1 
582  C  CD2 . PHE A 68  ? 0.09355 0.10425 0.07965 0.02010  0.01240  -0.00990 71  PHE A CD2 
583  C  CE1 . PHE A 68  ? 0.10955 0.08505 0.10435 0.01430  0.02990  0.00560  71  PHE A CE1 
584  C  CE2 . PHE A 68  ? 0.10105 0.08655 0.09135 0.01380  0.01320  -0.00570 71  PHE A CE2 
585  C  CZ  . PHE A 68  ? 0.10305 0.09155 0.09025 0.01740  0.01210  -0.00130 71  PHE A CZ  
586  N  N   . SER A 69  ? 0.07905 0.09225 0.09995 0.01040  0.01740  0.01720  72  SER A N   
587  C  CA  . SER A 69  ? 0.08245 0.10205 0.10835 0.01220  0.01780  0.01610  72  SER A CA  
588  C  C   . SER A 69  ? 0.08165 0.10545 0.09605 0.00420  0.00940  0.02230  72  SER A C   
589  O  O   . SER A 69  ? 0.08445 0.10155 0.09995 0.01190  0.00740  0.00830  72  SER A O   
590  C  CB  . SER A 69  ? 0.09895 0.10295 0.12645 0.02310  0.01010  0.03470  72  SER A CB  
591  O  OG  . SER A 69  ? 0.09035 0.08655 0.15655 0.00160  -0.00500 0.02760  72  SER A OG  
592  N  N   . ARG A 70  ? 0.07325 0.10945 0.09615 0.02080  0.00210  0.00210  73  ARG A N   
593  C  CA  . ARG A 70  ? 0.09475 0.10565 0.08255 0.03510  -0.02130 -0.00210 73  ARG A CA  
594  C  C   . ARG A 70  ? 0.09985 0.09175 0.09045 0.02890  -0.00870 -0.00010 73  ARG A C   
595  O  O   . ARG A 70  ? 0.10695 0.08615 0.11125 0.02070  0.00540  0.00400  73  ARG A O   
596  C  CB  . ARG A 70  ? 0.09415 0.11355 0.11595 0.02350  0.00380  0.01200  73  ARG A CB  
597  C  CG  . ARG A 70  ? 0.10155 0.10665 0.13525 0.00990  -0.01380 0.02490  73  ARG A CG  
598  C  CD  . ARG A 70  ? 0.09525 0.11525 0.15055 0.01270  -0.02040 0.02370  73  ARG A CD  
599  N  NE  . ARG A 70  ? 0.09585 0.12025 0.15745 0.00250  -0.00720 0.04340  73  ARG A NE  
600  C  CZ  . ARG A 70  ? 0.10965 0.13545 0.17345 -0.01510 -0.00260 0.05200  73  ARG A CZ  
601  N  NH1 . ARG A 70  ? 0.11865 0.15205 0.16755 0.01100  -0.01870 0.04940  73  ARG A NH1 
602  N  NH2 . ARG A 70  ? 0.11455 0.16655 0.19995 -0.02400 -0.02250 0.07110  73  ARG A NH2 
603  N  N   . TYR A 71  ? 0.10895 0.09775 0.09795 0.03030  0.01110  -0.00020 74  TYR A N   
604  C  CA  . TYR A 71  ? 0.12995 0.08845 0.10115 0.03590  0.00840  0.00130  74  TYR A CA  
605  C  C   . TYR A 71  ? 0.11915 0.10005 0.11535 0.02040  0.02050  0.01240  74  TYR A C   
606  O  O   . TYR A 71  ? 0.13615 0.09745 0.14845 0.02950  0.03030  0.00100  74  TYR A O   
607  C  CB  . TYR A 71  ? 0.13115 0.10355 0.10015 0.03330  -0.00120 -0.00380 74  TYR A CB  
608  C  CG  . TYR A 71  ? 0.10315 0.11605 0.10165 0.02160  -0.01380 0.00010  74  TYR A CG  
609  C  CD1 . TYR A 71  ? 0.09025 0.11895 0.10755 0.02720  -0.00100 -0.00160 74  TYR A CD1 
610  C  CD2 . TYR A 71  ? 0.10445 0.12125 0.11045 0.02040  -0.00290 0.00370  74  TYR A CD2 
611  C  CE1 . TYR A 71  ? 0.09475 0.11635 0.08785 0.01460  -0.00180 -0.00220 74  TYR A CE1 
612  C  CE2 . TYR A 71  ? 0.08495 0.13175 0.10655 0.01800  -0.01200 -0.00010 74  TYR A CE2 
613  C  CZ  . TYR A 71  ? 0.07565 0.12345 0.08185 0.01460  0.00030  -0.00150 74  TYR A CZ  
614  O  OH  . TYR A 71  ? 0.08975 0.11975 0.09485 0.02610  0.00310  -0.00370 74  TYR A OH  
615  N  N   . PRO A 72  ? 0.10315 0.10865 0.11245 0.02840  0.02580  0.00090  75  PRO A N   
616  C  CA  . PRO A 72  ? 0.10735 0.11635 0.11235 0.04130  0.02650  -0.01300 75  PRO A CA  
617  C  C   . PRO A 72  ? 0.10925 0.12715 0.12175 0.04950  0.00320  -0.01220 75  PRO A C   
618  O  O   . PRO A 72  ? 0.12195 0.13505 0.12045 0.06350  -0.01100 -0.00680 75  PRO A O   
619  C  CB  . PRO A 72  ? 0.09435 0.12375 0.11735 0.04460  0.02650  0.00680  75  PRO A CB  
620  C  CG  . PRO A 72  ? 0.09265 0.12825 0.12195 0.02600  0.02820  -0.00700 75  PRO A CG  
621  C  CD  . PRO A 72  ? 0.10035 0.11885 0.11435 0.00300  0.02350  -0.00330 75  PRO A CD  
622  N  N   . ASP A 73  ? 0.12705 0.11155 0.13845 0.04820  0.00960  -0.01960 76  ASP A N   
623  C  CA  . ASP A 73  ? 0.14185 0.11195 0.13865 0.04910  -0.00750 -0.01980 76  ASP A CA  
624  C  C   . ASP A 73  ? 0.16545 0.14235 0.12405 0.05370  -0.00070 -0.01480 76  ASP A C   
625  O  O   . ASP A 73  ? 0.17235 0.17025 0.13075 0.05160  -0.01420 -0.02300 76  ASP A O   
626  C  CB  . ASP A 73  ? 0.16625 0.10995 0.17795 0.03810  -0.02720 -0.03190 76  ASP A CB  
627  C  CG  . ASP A 73  ? 0.15925 0.12585 0.21015 0.04440  -0.00420 -0.04030 76  ASP A CG  
628  O  OD1 . ASP A 73  ? 0.16575 0.15855 0.21055 0.03790  -0.02100 -0.03040 76  ASP A OD1 
629  O  OD2 . ASP A 73  ? 0.21035 0.15515 0.22665 0.01810  0.01450  -0.05690 76  ASP A OD2 
630  N  N   . HIS A 74  ? 0.15835 0.14875 0.13565 0.07930  0.00890  -0.01320 77  HIS A N   
631  C  CA  . HIS A 74  ? 0.15275 0.18605 0.14505 0.06250  0.01290  -0.01240 77  HIS A CA  
632  C  C   . HIS A 74  ? 0.16845 0.18835 0.12605 0.06160  0.01430  -0.00820 77  HIS A C   
633  O  O   . HIS A 74  ? 0.20765 0.22705 0.13765 0.06890  0.02370  -0.01350 77  HIS A O   
634  C  CB  . HIS A 74  ? 0.15655 0.20245 0.16035 0.04670  0.03250  0.01710  77  HIS A CB  
635  C  CG  . HIS A 74  ? 0.14505 0.19485 0.16295 0.04480  0.03660  0.02860  77  HIS A CG  
636  N  ND1 . HIS A 74  ? 0.14625 0.19185 0.17965 0.03320  0.03540  0.02630  77  HIS A ND1 
637  C  CD2 . HIS A 74  ? 0.16585 0.20515 0.18705 0.03080  0.02750  0.03870  77  HIS A CD2 
638  C  CE1 . HIS A 74  ? 0.14915 0.19885 0.19285 0.02050  0.03850  0.03200  77  HIS A CE1 
639  N  NE2 . HIS A 74  ? 0.14815 0.19565 0.19905 0.02670  0.03300  0.03130  77  HIS A NE2 
640  N  N   . MET A 75  ? 0.14695 0.16585 0.12875 0.05930  -0.00310 -0.01850 78  MET A N   
641  C  CA  . MET A 75  ? 0.14505 0.14205 0.11955 0.05210  -0.02460 -0.00760 78  MET A CA  
642  C  C   . MET A 75  ? 0.13575 0.15075 0.11335 0.04810  -0.00770 -0.02340 78  MET A C   
643  O  O   . MET A 75  ? 0.15645 0.16245 0.11355 0.06000  -0.01840 -0.03370 78  MET A O   
644  C  CB  . MET A 75  ? 0.13945 0.14655 0.13315 0.03280  -0.02120 0.00130  78  MET A CB  
645  C  CG  . MET A 75  ? 0.14075 0.16565 0.13395 0.03940  -0.01000 0.00320  78  MET A CG  
646  S  SD  . MET A 75  ? 0.15015 0.16045 0.12385 0.01340  0.00410  0.00650  78  MET A SD  
647  C  CE  . MET A 75  ? 0.14745 0.15585 0.13185 0.02390  0.00710  0.00600  78  MET A CE  
648  N  N   . LYS A 76  ? 0.15195 0.16015 0.15605 0.03470  -0.02080 0.00030  79  LYS A N   
652  C  C   . LYS A 76  ? 0.15235 0.14495 0.15795 0.04960  -0.00120 -0.00680 79  LYS A C   
653  O  O   . LYS A 76  ? 0.13645 0.13035 0.15385 0.01250  0.01810  0.00520  79  LYS A O   
669  N  N   . ARG A 77  ? 0.12205 0.14665 0.14555 0.04740  -0.00250 -0.02300 80  ARG A N   
670  C  CA  . ARG A 77  ? 0.12825 0.15815 0.14115 0.04130  0.00310  -0.02820 80  ARG A CA  
671  C  C   . ARG A 77  ? 0.10795 0.14885 0.12115 0.03130  0.00880  -0.00840 80  ARG A C   
672  O  O   . ARG A 77  ? 0.13005 0.15145 0.12285 0.02830  0.00030  0.00040  80  ARG A O   
673  C  CB  . ARG A 77  ? 0.16015 0.18835 0.15995 0.00310  0.02680  -0.05060 80  ARG A CB  
674  C  CG  . ARG A 77  ? 0.17215 0.23385 0.17825 0.00670  0.05530  -0.05910 80  ARG A CG  
675  C  CD  . ARG A 77  ? 0.21495 0.27095 0.23165 0.00290  0.06530  -0.07790 80  ARG A CD  
676  N  NE  . ARG A 77  ? 0.24675 0.28835 0.26435 0.00080  0.08900  -0.08640 80  ARG A NE  
677  C  CZ  . ARG A 77  ? 0.25535 0.26105 0.24975 0.01920  0.09030  -0.06330 80  ARG A CZ  
680  N  N   . HIS A 78  ? 0.11395 0.13015 0.10045 0.03230  0.00940  0.00190  81  HIS A N   
681  C  CA  . HIS A 78  ? 0.10915 0.12135 0.08525 0.02250  0.01290  0.00890  81  HIS A CA  
682  C  C   . HIS A 78  ? 0.11215 0.12035 0.07565 0.02510  0.02370  0.02000  81  HIS A C   
683  O  O   . HIS A 78  ? 0.13565 0.12975 0.09495 0.04580  0.02900  0.01270  81  HIS A O   
684  C  CB  . HIS A 78  ? 0.11255 0.14035 0.09885 0.02380  0.02410  -0.00790 81  HIS A CB  
685  C  CG  . HIS A 78  ? 0.11175 0.13955 0.10745 0.01590  0.01560  -0.00510 81  HIS A CG  
686  N  ND1 . HIS A 78  ? 0.13425 0.15515 0.12615 0.02270  0.01990  -0.00490 81  HIS A ND1 
687  C  CD2 . HIS A 78  ? 0.10875 0.16695 0.13955 0.01130  0.01940  -0.00110 81  HIS A CD2 
688  C  CE1 . HIS A 78  ? 0.11985 0.16435 0.14065 0.03120  0.02770  -0.00250 81  HIS A CE1 
689  N  NE2 . HIS A 78  ? 0.12465 0.17635 0.14035 0.02110  0.04580  0.01080  81  HIS A NE2 
690  N  N   . ASP A 79  ? 0.09755 0.13245 0.08005 0.03340  0.01460  0.02740  82  ASP A N   
691  C  CA  . ASP A 79  ? 0.09035 0.11995 0.07545 0.02170  0.01350  0.01020  82  ASP A CA  
692  C  C   . ASP A 79  ? 0.09445 0.12145 0.08555 0.01190  0.01880  0.00230  82  ASP A C   
693  O  O   . ASP A 79  ? 0.10595 0.11035 0.08905 0.00810  0.00280  -0.00240 82  ASP A O   
694  C  CB  . ASP A 79  ? 0.10945 0.11835 0.09155 -0.00110 0.00990  0.00390  82  ASP A CB  
695  C  CG  . ASP A 79  ? 0.10765 0.10735 0.09515 0.00850  -0.00600 -0.00970 82  ASP A CG  
696  O  OD1 . ASP A 79  ? 0.10185 0.10095 0.08845 0.00880  0.00850  -0.00100 82  ASP A OD1 
697  O  OD2 . ASP A 79  ? 0.10255 0.11115 0.09425 -0.00520 0.00230  -0.01380 82  ASP A OD2 
698  N  N   . PHE A 80  ? 0.11625 0.10225 0.09335 0.03520  0.00360  -0.00020 83  PHE A N   
699  C  CA  . PHE A 80  ? 0.10365 0.11035 0.10225 0.02660  0.01040  0.01670  83  PHE A CA  
700  C  C   . PHE A 80  ? 0.08725 0.09515 0.10035 0.02130  -0.00420 -0.01400 83  PHE A C   
701  O  O   . PHE A 80  ? 0.10515 0.10635 0.09775 0.02900  0.01280  -0.01520 83  PHE A O   
702  C  CB  . PHE A 80  ? 0.12025 0.10295 0.11565 0.03100  -0.01150 0.01110  83  PHE A CB  
703  C  CG  . PHE A 80  ? 0.12925 0.11975 0.10785 0.02990  -0.01130 0.00580  83  PHE A CG  
704  C  CD1 . PHE A 80  ? 0.13285 0.13565 0.11795 0.01360  -0.01480 0.00950  83  PHE A CD1 
705  C  CD2 . PHE A 80  ? 0.11605 0.08925 0.11855 0.01570  -0.00320 0.00220  83  PHE A CD2 
706  C  CE1 . PHE A 80  ? 0.14405 0.14445 0.12155 0.03080  -0.01180 0.01500  83  PHE A CE1 
707  C  CE2 . PHE A 80  ? 0.12915 0.11145 0.11825 0.02240  -0.01510 -0.00140 83  PHE A CE2 
708  C  CZ  . PHE A 80  ? 0.15395 0.13065 0.11375 0.02220  -0.01090 0.00690  83  PHE A CZ  
709  N  N   . PHE A 81  ? 0.11715 0.09345 0.08345 0.01260  -0.00540 0.00650  84  PHE A N   
710  C  CA  . PHE A 81  ? 0.09515 0.09135 0.08275 -0.01030 0.00730  -0.00190 84  PHE A CA  
711  C  C   . PHE A 81  ? 0.09025 0.10095 0.08525 0.00580  -0.00760 -0.01220 84  PHE A C   
712  O  O   . PHE A 81  ? 0.09465 0.12175 0.09645 0.01610  -0.00090 0.00110  84  PHE A O   
713  C  CB  . PHE A 81  ? 0.09965 0.08895 0.07995 -0.00080 -0.00550 -0.00330 84  PHE A CB  
714  C  CG  . PHE A 81  ? 0.09975 0.09775 0.07105 0.01820  -0.00560 0.00150  84  PHE A CG  
715  C  CD1 . PHE A 81  ? 0.10535 0.10755 0.06265 0.00650  -0.00410 0.00490  84  PHE A CD1 
716  C  CD2 . PHE A 81  ? 0.10455 0.11385 0.07085 0.01060  0.00990  -0.00590 84  PHE A CD2 
717  C  CE1 . PHE A 81  ? 0.09525 0.11455 0.08645 -0.00730 0.00550  0.00070  84  PHE A CE1 
718  C  CE2 . PHE A 81  ? 0.10185 0.11085 0.08645 0.02910  -0.00400 -0.01200 84  PHE A CE2 
719  C  CZ  . PHE A 81  ? 0.10805 0.10885 0.08395 0.00900  -0.00180 -0.00550 84  PHE A CZ  
720  N  N   . LYS A 82  ? 0.09945 0.08265 0.09455 0.01350  -0.01400 -0.00390 85  LYS A N   
721  C  CA  . LYS A 82  ? 0.11735 0.07815 0.11115 0.01760  -0.01430 -0.00390 85  LYS A CA  
722  C  C   . LYS A 82  ? 0.11195 0.09125 0.10845 0.00770  -0.01320 -0.01590 85  LYS A C   
723  O  O   . LYS A 82  ? 0.12225 0.09435 0.11455 0.00270  -0.02990 -0.00060 85  LYS A O   
724  C  CB  . LYS A 82  ? 0.10475 0.09615 0.10175 0.01630  -0.00410 -0.00210 85  LYS A CB  
725  C  CG  . LYS A 82  ? 0.09815 0.09715 0.08345 0.01430  -0.00260 0.01320  85  LYS A CG  
726  C  CD  . LYS A 82  ? 0.10245 0.08075 0.09785 0.01140  -0.00030 -0.01460 85  LYS A CD  
727  C  CE  . LYS A 82  ? 0.09915 0.07465 0.10995 0.01680  -0.01500 0.00200  85  LYS A CE  
728  N  NZ  . LYS A 82  ? 0.10165 0.08305 0.10105 0.00370  0.01010  0.00520  85  LYS A NZ  
729  N  N   . SER A 83  ? 0.13245 0.10875 0.09165 0.01820  0.00190  -0.02640 86  SER A N   
730  C  CA  . SER A 83  ? 0.12695 0.13675 0.10065 0.02200  -0.01310 -0.02800 86  SER A CA  
731  C  C   . SER A 83  ? 0.12315 0.11825 0.10825 0.02790  -0.01980 -0.02250 86  SER A C   
732  O  O   . SER A 83  ? 0.14125 0.13305 0.14055 0.02120  -0.02400 -0.04730 86  SER A O   
733  C  CB  . SER A 83  ? 0.13605 0.14285 0.10665 0.04520  0.01350  -0.03830 86  SER A CB  
734  O  OG  . SER A 83  ? 0.11905 0.15495 0.10435 0.02210  0.01340  -0.05020 86  SER A OG  
735  N  N   . ALA A 84  ? 0.10505 0.10735 0.11435 0.02230  0.00040  -0.02060 87  ALA A N   
736  C  CA  . ALA A 84  ? 0.09595 0.10285 0.11055 0.00790  -0.01020 -0.00850 87  ALA A CA  
737  C  C   . ALA A 84  ? 0.11565 0.09715 0.11025 0.00240  -0.00870 -0.00830 87  ALA A C   
738  O  O   . ALA A 84  ? 0.10935 0.12405 0.11465 -0.00150 -0.00280 -0.01950 87  ALA A O   
739  C  CB  . ALA A 84  ? 0.11965 0.09305 0.12835 0.01300  -0.01750 -0.01390 87  ALA A CB  
740  N  N   . MET A 85  ? 0.12345 0.09285 0.11565 0.00610  -0.01250 0.00820  88  MET A N   
741  C  CA  . MET A 85  ? 0.13235 0.10045 0.11955 -0.01130 -0.03230 0.00630  88  MET A CA  
742  C  C   . MET A 85  ? 0.13085 0.10385 0.12905 0.01530  -0.02730 -0.00670 88  MET A C   
743  O  O   . MET A 85  ? 0.14565 0.11975 0.13095 0.01380  -0.02630 -0.02300 88  MET A O   
744  C  CB  . MET A 85  ? 0.12655 0.09955 0.11465 0.00520  -0.02330 -0.00590 88  MET A CB  
745  C  CG  . MET A 85  ? 0.10755 0.09695 0.11945 0.01810  -0.01090 -0.00680 88  MET A CG  
746  S  SD  . MET A 85  ? 0.09685 0.10955 0.12315 0.00260  -0.01660 -0.00020 88  MET A SD  
747  C  CE  . MET A 85  ? 0.10645 0.12115 0.11845 -0.01100 -0.02660 -0.00780 88  MET A CE  
748  N  N   . PRO A 86  ? 0.13405 0.09445 0.13915 -0.00140 -0.02040 -0.01690 89  PRO A N   
749  C  CA  . PRO A 86  ? 0.11545 0.10695 0.14995 -0.00030 -0.01300 -0.00150 89  PRO A CA  
750  C  C   . PRO A 86  ? 0.11815 0.11335 0.13565 -0.01600 -0.02780 -0.00780 89  PRO A C   
751  O  O   . PRO A 86  ? 0.12685 0.11075 0.12785 0.00550  -0.02310 -0.00480 89  PRO A O   
752  C  CB  . PRO A 86  ? 0.13525 0.10335 0.17525 -0.02530 -0.02550 -0.01010 89  PRO A CB  
753  C  CG  . PRO A 86  ? 0.15665 0.12965 0.17975 -0.02650 -0.00990 -0.01360 89  PRO A CG  
754  C  CD  . PRO A 86  ? 0.15565 0.11075 0.16075 -0.01350 0.00280  -0.03060 89  PRO A CD  
755  N  N   . GLU A 87  ? 0.12545 0.10915 0.12495 0.00010  -0.03030 -0.01370 90  GLU A N   
756  C  CA  A GLU A 87  ? 0.13975 0.11765 0.13245 0.00050  -0.04020 -0.02480 90  GLU A CA  
758  C  C   . GLU A 87  ? 0.12375 0.11015 0.12065 0.00870  -0.02250 -0.01040 90  GLU A C   
759  O  O   . GLU A 87  ? 0.13305 0.12495 0.11265 0.01160  -0.02350 -0.02200 90  GLU A O   
760  C  CB  A GLU A 87  ? 0.19845 0.13935 0.15535 -0.01840 -0.05070 -0.05770 90  GLU A CB  
762  C  CG  A GLU A 87  ? 0.24865 0.17495 0.19525 -0.05050 -0.05910 -0.07770 90  GLU A CG  
764  C  CD  A GLU A 87  ? 0.29495 0.18835 0.22435 -0.04530 -0.02150 -0.06330 90  GLU A CD  
766  O  OE1 A GLU A 87  ? 0.33805 0.16505 0.21695 -0.02560 -0.01810 -0.06330 90  GLU A OE1 
770  N  N   . GLY A 88  ? 0.10885 0.09675 0.10555 -0.01620 -0.01730 -0.01040 91  GLY A N   
771  C  CA  . GLY A 88  ? 0.13725 0.08185 0.10185 -0.00970 -0.02990 -0.00050 91  GLY A CA  
772  C  C   . GLY A 88  ? 0.10005 0.09835 0.09945 0.00680  -0.01460 -0.01230 91  GLY A C   
773  O  O   . GLY A 88  ? 0.10505 0.10605 0.08305 0.02300  -0.01260 -0.01390 91  GLY A O   
774  N  N   . TYR A 89  ? 0.11355 0.08965 0.09335 0.00190  -0.01040 -0.01330 92  TYR A N   
775  C  CA  . TYR A 89  ? 0.10775 0.10335 0.08445 0.00060  -0.02110 -0.00670 92  TYR A CA  
776  C  C   . TYR A 89  ? 0.10035 0.10435 0.08305 0.00800  -0.01220 -0.00660 92  TYR A C   
777  O  O   . TYR A 89  ? 0.10225 0.10395 0.07225 0.00160  -0.01120 -0.00750 92  TYR A O   
778  C  CB  . TYR A 89  ? 0.10875 0.11275 0.10035 -0.01120 -0.00570 -0.00540 92  TYR A CB  
779  C  CG  . TYR A 89  ? 0.09415 0.09315 0.10355 -0.00140 0.00480  -0.02500 92  TYR A CG  
780  C  CD1 . TYR A 89  ? 0.10495 0.09735 0.09445 -0.00490 -0.00390 -0.01300 92  TYR A CD1 
781  C  CD2 . TYR A 89  ? 0.10475 0.09095 0.10915 0.00020  -0.01430 -0.01880 92  TYR A CD2 
782  C  CE1 . TYR A 89  ? 0.09315 0.10305 0.09085 0.00510  0.00360  -0.00630 92  TYR A CE1 
783  C  CE2 . TYR A 89  ? 0.08875 0.08775 0.10545 -0.02500 0.00520  -0.01850 92  TYR A CE2 
784  C  CZ  . TYR A 89  ? 0.08425 0.09595 0.08635 -0.00400 0.00480  -0.01680 92  TYR A CZ  
785  O  OH  . TYR A 89  ? 0.08455 0.10165 0.08475 0.00800  -0.00150 -0.00390 92  TYR A OH  
786  N  N   . VAL A 90  ? 0.10355 0.08575 0.10005 0.00580  -0.00780 -0.00110 93  VAL A N   
787  C  CA  . VAL A 90  ? 0.11035 0.07595 0.09455 0.00140  -0.01760 0.00130  93  VAL A CA  
788  C  C   . VAL A 90  ? 0.10545 0.10745 0.09525 0.00080  -0.00050 -0.00630 93  VAL A C   
789  O  O   . VAL A 90  ? 0.12785 0.12285 0.10425 -0.03040 0.00850  -0.01860 93  VAL A O   
790  C  CB  . VAL A 90  ? 0.13535 0.09475 0.10825 0.00870  -0.02010 0.00480  93  VAL A CB  
791  C  CG1 . VAL A 90  ? 0.12545 0.11035 0.12035 0.02310  -0.02890 0.01000  93  VAL A CG1 
792  C  CG2 . VAL A 90  ? 0.13395 0.11795 0.12195 -0.02870 -0.02920 0.00910  93  VAL A CG2 
793  N  N   . GLN A 91  ? 0.09785 0.08095 0.08625 0.00340  -0.01210 -0.00230 94  GLN A N   
794  C  CA  . GLN A 91  ? 0.09905 0.09745 0.09525 -0.00170 -0.00690 -0.00900 94  GLN A CA  
795  C  C   . GLN A 91  ? 0.09895 0.09525 0.09325 0.01370  -0.01080 -0.00540 94  GLN A C   
796  O  O   . GLN A 91  ? 0.08815 0.08915 0.08445 0.00370  0.00040  -0.01060 94  GLN A O   
797  C  CB  . GLN A 91  ? 0.08135 0.10295 0.09875 0.00040  -0.02280 0.00090  94  GLN A CB  
798  C  CG  . GLN A 91  ? 0.08805 0.09935 0.09765 0.00490  -0.01630 -0.00230 94  GLN A CG  
799  C  CD  . GLN A 91  ? 0.09815 0.08705 0.08615 0.00180  -0.00630 0.00080  94  GLN A CD  
800  O  OE1 . GLN A 91  ? 0.09725 0.07855 0.08545 0.01160  -0.00050 0.00910  94  GLN A OE1 
801  N  NE2 . GLN A 91  ? 0.09495 0.10515 0.08285 -0.00510 -0.00230 -0.00990 94  GLN A NE2 
802  N  N   . GLU A 92  ? 0.09835 0.08755 0.10275 0.01330  -0.02540 -0.00340 95  GLU A N   
803  C  CA  . GLU A 92  ? 0.09815 0.08095 0.12085 0.01780  -0.02770 -0.00720 95  GLU A CA  
804  C  C   . GLU A 92  ? 0.09025 0.08315 0.10305 0.01860  0.00480  -0.00900 95  GLU A C   
805  O  O   . GLU A 92  ? 0.11105 0.09655 0.10935 -0.00230 0.02180  -0.01880 95  GLU A O   
806  C  CB  . GLU A 92  ? 0.13915 0.14335 0.20725 0.00810  -0.07890 0.01110  95  GLU A CB  
807  C  CG  . GLU A 92  ? 0.26825 0.26925 0.28815 -0.01370 -0.06330 0.00500  95  GLU A CG  
811  N  N   . ARG A 93  ? 0.08585 0.07715 0.09675 0.00990  -0.00630 0.00030  96  ARG A N   
812  C  CA  . ARG A 93  ? 0.08825 0.08675 0.09255 0.00110  -0.01270 0.00660  96  ARG A CA  
813  C  C   . ARG A 93  ? 0.07975 0.08725 0.08145 -0.00450 0.00290  -0.00410 96  ARG A C   
814  O  O   . ARG A 93  ? 0.08385 0.08825 0.09955 0.01230  0.00810  0.00530  96  ARG A O   
815  C  CB  . ARG A 93  ? 0.09165 0.08395 0.07665 0.01890  0.00970  0.00370  96  ARG A CB  
816  C  CG  . ARG A 93  ? 0.09875 0.08295 0.08215 0.02140  -0.01700 0.00290  96  ARG A CG  
817  C  CD  . ARG A 93  ? 0.08945 0.07895 0.09385 0.00110  -0.00900 0.00160  96  ARG A CD  
818  N  NE  . ARG A 93  ? 0.08455 0.08295 0.08485 0.00680  0.00100  0.01040  96  ARG A NE  
819  C  CZ  . ARG A 93  ? 0.08385 0.07135 0.07445 0.00970  0.00750  0.00240  96  ARG A CZ  
820  N  NH1 . ARG A 93  ? 0.08135 0.08235 0.07645 0.00080  0.00460  0.00460  96  ARG A NH1 
821  N  NH2 . ARG A 93  ? 0.07935 0.07595 0.09285 0.00840  -0.01160 0.00470  96  ARG A NH2 
822  N  N   . THR A 94  ? 0.09615 0.07775 0.09115 -0.01080 -0.00620 0.00420  97  THR A N   
823  C  CA  . THR A 94  ? 0.09695 0.07655 0.08935 -0.00510 -0.00720 0.00430  97  THR A CA  
824  C  C   . THR A 94  ? 0.08095 0.07685 0.10095 0.00020  0.00020  0.00320  97  THR A C   
825  O  O   . THR A 94  ? 0.08715 0.09235 0.09885 0.00250  0.00960  0.00540  97  THR A O   
826  C  CB  . THR A 94  ? 0.13015 0.08835 0.10515 -0.00490 -0.01550 0.00650  97  THR A CB  
827  O  OG1 . THR A 94  ? 0.14795 0.10825 0.10435 0.00020  -0.02910 0.01480  97  THR A OG1 
828  C  CG2 . THR A 94  ? 0.11975 0.09355 0.14015 -0.01670 0.00120  0.02880  97  THR A CG2 
829  N  N   . ILE A 95  ? 0.09225 0.06865 0.08955 0.00690  -0.00480 -0.00210 98  ILE A N   
830  C  CA  . ILE A 95  ? 0.08725 0.06745 0.09355 0.00450  -0.00180 -0.00450 98  ILE A CA  
831  C  C   . ILE A 95  ? 0.09065 0.07555 0.10245 0.00780  0.00770  0.01190  98  ILE A C   
832  O  O   . ILE A 95  ? 0.08025 0.08025 0.10455 0.00500  0.00210  0.00360  98  ILE A O   
833  C  CB  . ILE A 95  ? 0.07565 0.08105 0.10245 0.00380  0.00920  0.00850  98  ILE A CB  
834  C  CG1 . ILE A 95  ? 0.09585 0.07795 0.11055 0.01610  0.00680  0.01010  98  ILE A CG1 
835  C  CG2 . ILE A 95  ? 0.07675 0.10835 0.09885 -0.00270 -0.01740 -0.00070 98  ILE A CG2 
836  C  CD1 . ILE A 95  ? 0.11805 0.07435 0.09675 0.00690  0.01860  0.02950  98  ILE A CD1 
837  N  N   . SER A 96  ? 0.09035 0.07685 0.10305 -0.00850 0.00650  0.00970  99  SER A N   
838  C  CA  A SER A 96  ? 0.09605 0.07515 0.10125 -0.01590 0.00790  0.01450  99  SER A CA  
840  C  C   . SER A 96  ? 0.08565 0.07885 0.09625 -0.02230 0.01000  0.00450  99  SER A C   
841  O  O   . SER A 96  ? 0.07795 0.08635 0.11725 -0.00120 0.01350  0.01920  99  SER A O   
842  C  CB  A SER A 96  ? 0.12065 0.08975 0.09245 -0.01720 -0.00090 0.02240  99  SER A CB  
844  O  OG  A SER A 96  ? 0.13235 0.10735 0.10005 -0.00350 -0.01780 0.01210  99  SER A OG  
846  N  N   . PHE A 97  ? 0.08765 0.08935 0.09225 -0.01030 0.00300  0.00140  100 PHE A N   
847  C  CA  . PHE A 97  ? 0.08985 0.08705 0.09325 -0.02130 -0.00840 -0.00450 100 PHE A CA  
848  C  C   . PHE A 97  ? 0.08635 0.09165 0.11355 -0.01640 -0.00730 -0.00050 100 PHE A C   
849  O  O   . PHE A 97  ? 0.08645 0.09245 0.11115 0.00160  0.00010  0.00440  100 PHE A O   
850  C  CB  . PHE A 97  ? 0.09345 0.09435 0.10055 -0.01000 0.00400  0.00700  100 PHE A CB  
851  C  CG  . PHE A 97  ? 0.06855 0.09085 0.08985 -0.00490 0.00630  -0.00490 100 PHE A CG  
852  C  CD1 . PHE A 97  ? 0.08595 0.08565 0.09975 -0.00190 0.01140  0.00490  100 PHE A CD1 
853  C  CD2 . PHE A 97  ? 0.08705 0.07955 0.09425 -0.00410 0.02550  -0.01750 100 PHE A CD2 
854  C  CE1 . PHE A 97  ? 0.08355 0.10265 0.10265 -0.00460 0.01890  -0.00290 100 PHE A CE1 
855  C  CE2 . PHE A 97  ? 0.08085 0.07965 0.10765 0.00470  0.01700  -0.00650 100 PHE A CE2 
856  C  CZ  . PHE A 97  ? 0.06855 0.08675 0.09235 0.01240  0.01810  -0.00070 100 PHE A CZ  
857  N  N   . LYS A 98  ? 0.07785 0.08465 0.13065 -0.01430 0.01420  0.00580  101 LYS A N   
859  C  CA  B LYS A 98  ? 0.07995 0.08345 0.17285 -0.02170 0.03230  0.00430  101 LYS A CA  
860  C  C   . LYS A 98  ? 0.11395 0.10935 0.16035 -0.02090 0.01860  0.01830  101 LYS A C   
861  O  O   . LYS A 98  ? 0.09445 0.10445 0.17615 -0.02630 0.00290  0.00580  101 LYS A O   
863  C  CB  B LYS A 98  ? 0.07435 0.08865 0.20205 -0.01580 0.03820  0.01000  101 LYS A CB  
865  C  CG  B LYS A 98  ? 0.08115 0.10315 0.23155 -0.01600 0.04190  0.01190  101 LYS A CG  
867  C  CD  B LYS A 98  ? 0.10355 0.12905 0.26745 -0.01530 0.02160  -0.00610 101 LYS A CD  
869  C  CE  B LYS A 98  ? 0.13315 0.14705 0.28525 -0.02320 0.01530  -0.00740 101 LYS A CE  
871  N  NZ  B LYS A 98  ? 0.17535 0.14205 0.30125 -0.02110 0.01800  -0.00150 101 LYS A NZ  
872  N  N   . ASP A 99  ? 0.11125 0.09795 0.17165 -0.01470 0.02540  0.02230  102 ASP A N   
873  C  CA  A ASP A 99  ? 0.09265 0.11115 0.20215 0.00260  0.00190  0.01110  102 ASP A CA  
875  C  C   . ASP A 99  ? 0.10045 0.10185 0.18175 -0.01080 -0.00580 -0.00240 102 ASP A C   
876  O  O   . ASP A 99  ? 0.10285 0.11195 0.21515 -0.00820 -0.00230 -0.02350 102 ASP A O   
877  C  CB  A ASP A 99  ? 0.11555 0.14095 0.24205 -0.01830 0.00190  0.00830  102 ASP A CB  
879  C  CG  A ASP A 99  ? 0.14295 0.17635 0.25485 -0.02540 0.00500  0.01200  102 ASP A CG  
881  O  OD1 A ASP A 99  ? 0.16255 0.20235 0.26975 -0.03840 0.03620  0.03010  102 ASP A OD1 
883  O  OD2 A ASP A 99  ? 0.17495 0.21135 0.26535 -0.03730 -0.00080 -0.00690 102 ASP A OD2 
885  N  N   . ASP A 100 ? 0.08395 0.09415 0.16555 -0.01390 -0.00780 0.01140  103 ASP A N   
886  C  CA  . ASP A 100 ? 0.08115 0.09005 0.13635 -0.00530 -0.00110 0.00160  103 ASP A CA  
887  C  C   . ASP A 100 ? 0.08715 0.09525 0.11795 0.00570  -0.01050 0.00240  103 ASP A C   
888  O  O   . ASP A 100 ? 0.09335 0.09065 0.12635 -0.01240 0.01030  -0.00370 103 ASP A O   
889  C  CB  . ASP A 100 ? 0.09335 0.09835 0.12855 0.00410  0.00820  0.01110  103 ASP A CB  
890  C  CG  . ASP A 100 ? 0.09695 0.11185 0.13305 0.01000  -0.00630 -0.00000 103 ASP A CG  
891  O  OD1 . ASP A 100 ? 0.09975 0.13685 0.12625 0.00260  -0.00760 -0.01890 103 ASP A OD1 
892  O  OD2 . ASP A 100 ? 0.09605 0.14375 0.14335 0.00010  -0.00240 -0.00820 103 ASP A OD2 
893  N  N   . GLY A 101 ? 0.08315 0.09125 0.12055 -0.01310 -0.00100 0.00180  104 GLY A N   
894  C  CA  . GLY A 101 ? 0.09615 0.08695 0.11625 0.00270  -0.00510 -0.00320 104 GLY A CA  
895  C  C   . GLY A 101 ? 0.09475 0.08485 0.11955 -0.00040 -0.00560 0.00330  104 GLY A C   
896  O  O   . GLY A 101 ? 0.08595 0.09385 0.11165 0.01360  -0.00800 0.00810  104 GLY A O   
897  N  N   . ASN A 102 ? 0.10565 0.07805 0.10145 -0.00630 -0.00070 -0.00260 105 ASN A N   
898  C  CA  . ASN A 102 ? 0.10495 0.07625 0.09375 -0.00840 0.01430  -0.00200 105 ASN A CA  
899  C  C   . ASN A 102 ? 0.07545 0.08785 0.09825 0.01360  0.00800  -0.00790 105 ASN A C   
900  O  O   . ASN A 102 ? 0.07725 0.08845 0.09685 0.00290  0.00280  0.00000  105 ASN A O   
901  C  CB  . ASN A 102 ? 0.10785 0.10485 0.08735 0.00610  0.00340  0.00630  105 ASN A CB  
902  C  CG  . ASN A 102 ? 0.11225 0.15035 0.09635 -0.00370 0.01420  0.00960  105 ASN A CG  
903  O  OD1 . ASN A 102 ? 0.12425 0.18115 0.11105 -0.03000 -0.00550 0.00080  105 ASN A OD1 
904  N  ND2 . ASN A 102 ? 0.13195 0.16655 0.09695 0.04250  0.01670  0.03870  105 ASN A ND2 
905  N  N   . TYR A 103 ? 0.07665 0.07835 0.10475 0.00460  -0.00010 -0.00310 106 TYR A N   
906  C  CA  . TYR A 103 ? 0.09565 0.07175 0.10445 -0.01160 -0.00170 -0.00800 106 TYR A CA  
907  C  C   . TYR A 103 ? 0.06965 0.08375 0.11295 0.00930  -0.00370 -0.00210 106 TYR A C   
908  O  O   . TYR A 103 ? 0.07855 0.09445 0.10555 -0.00390 0.01360  -0.00050 106 TYR A O   
909  C  CB  . TYR A 103 ? 0.07475 0.08525 0.10835 0.00510  -0.01320 0.00830  106 TYR A CB  
910  C  CG  . TYR A 103 ? 0.06515 0.07775 0.10625 -0.00160 -0.00410 -0.00020 106 TYR A CG  
911  C  CD1 . TYR A 103 ? 0.07755 0.08295 0.11105 -0.01550 0.00790  0.01230  106 TYR A CD1 
912  C  CD2 . TYR A 103 ? 0.07645 0.07845 0.10375 -0.01270 -0.00510 0.00790  106 TYR A CD2 
913  C  CE1 . TYR A 103 ? 0.08295 0.08495 0.11295 -0.00570 0.01240  0.01650  106 TYR A CE1 
914  C  CE2 . TYR A 103 ? 0.09045 0.08885 0.09495 -0.00350 -0.00330 0.00490  106 TYR A CE2 
915  C  CZ  . TYR A 103 ? 0.08455 0.09415 0.09945 -0.00480 0.00670  -0.00530 106 TYR A CZ  
916  O  OH  . TYR A 103 ? 0.09215 0.08865 0.10575 -0.01330 0.00190  0.00290  106 TYR A OH  
917  N  N   . LYS A 104 ? 0.07765 0.07735 0.09665 -0.00160 -0.00300 -0.00430 107 LYS A N   
918  C  CA  A LYS A 104 ? 0.09405 0.08175 0.10235 -0.00270 -0.00920 0.00530  107 LYS A CA  
920  C  C   . LYS A 104 ? 0.08505 0.08565 0.09295 -0.00230 0.00080  0.00390  107 LYS A C   
921  O  O   . LYS A 104 ? 0.08855 0.08725 0.10325 -0.00600 0.01770  0.00260  107 LYS A O   
922  C  CB  A LYS A 104 ? 0.12585 0.10105 0.11495 0.01140  0.00850  -0.00320 107 LYS A CB  
924  C  CG  A LYS A 104 ? 0.14165 0.11845 0.11685 0.01620  0.01050  0.01700  107 LYS A CG  
926  C  CD  A LYS A 104 ? 0.14245 0.14385 0.12435 0.03050  -0.00140 0.01920  107 LYS A CD  
928  C  CE  A LYS A 104 ? 0.15845 0.15845 0.13735 0.03420  0.01260  0.03500  107 LYS A CE  
930  N  NZ  A LYS A 104 ? 0.16195 0.17385 0.13395 0.04160  0.00550  0.05110  107 LYS A NZ  
932  N  N   . THR A 105 ? 0.08705 0.07635 0.09815 0.00450  -0.01890 0.00610  108 THR A N   
933  C  CA  . THR A 105 ? 0.08975 0.07385 0.08635 0.01100  0.00410  0.00360  108 THR A CA  
934  C  C   . THR A 105 ? 0.07055 0.07885 0.09135 0.00380  0.01410  0.00250  108 THR A C   
935  O  O   . THR A 105 ? 0.08825 0.10105 0.09725 -0.01010 0.00510  0.00440  108 THR A O   
936  C  CB  . THR A 105 ? 0.07055 0.09055 0.09705 0.01830  -0.00080 -0.00010 108 THR A CB  
937  O  OG1 . THR A 105 ? 0.08135 0.09605 0.10355 0.00700  0.00320  0.00410  108 THR A OG1 
938  C  CG2 . THR A 105 ? 0.09305 0.10795 0.09135 0.01290  0.00350  -0.00290 108 THR A CG2 
939  N  N   . ARG A 106 ? 0.08355 0.07945 0.09835 0.00620  0.01210  -0.00360 109 ARG A N   
940  C  CA  A ARG A 106 ? 0.07555 0.08375 0.10435 0.01980  -0.02240 -0.00290 109 ARG A CA  
942  C  C   . ARG A 106 ? 0.07775 0.09065 0.09025 0.01260  -0.00520 -0.00140 109 ARG A C   
943  O  O   . ARG A 106 ? 0.10095 0.10045 0.10555 0.01000  0.01150  0.00290  109 ARG A O   
944  C  CB  A ARG A 106 ? 0.09405 0.10765 0.10075 0.01990  -0.04050 0.00220  109 ARG A CB  
946  C  CG  A ARG A 106 ? 0.11065 0.13205 0.10775 0.00580  -0.05280 -0.00110 109 ARG A CG  
948  C  CD  A ARG A 106 ? 0.12595 0.13795 0.11775 0.01400  -0.07020 0.00430  109 ARG A CD  
950  N  NE  A ARG A 106 ? 0.12925 0.14805 0.14045 0.02940  -0.07520 -0.00580 109 ARG A NE  
952  C  CZ  A ARG A 106 ? 0.14045 0.16065 0.17815 0.03360  -0.08020 -0.01010 109 ARG A CZ  
954  N  NH1 A ARG A 106 ? 0.13395 0.16565 0.20085 0.03580  -0.08640 -0.00780 109 ARG A NH1 
956  N  NH2 A ARG A 106 ? 0.16485 0.16725 0.18515 0.03680  -0.07850 -0.01490 109 ARG A NH2 
958  N  N   . ALA A 107 ? 0.07935 0.08575 0.08765 0.00930  -0.00710 -0.00780 110 ALA A N   
959  C  CA  . ALA A 107 ? 0.08965 0.08885 0.09645 0.01580  -0.00940 -0.00500 110 ALA A CA  
960  C  C   . ALA A 107 ? 0.09185 0.09565 0.09875 0.00950  -0.00590 -0.01410 110 ALA A C   
961  O  O   . ALA A 107 ? 0.09265 0.09865 0.09195 -0.00000 -0.00600 -0.00800 110 ALA A O   
962  C  CB  . ALA A 107 ? 0.10035 0.09385 0.09865 0.00770  -0.01950 -0.01970 110 ALA A CB  
963  N  N   . GLU A 108 ? 0.10865 0.08215 0.10375 0.00460  -0.01170 -0.01840 111 GLU A N   
964  C  CA  . GLU A 108 ? 0.12105 0.09335 0.09605 0.00850  -0.01550 -0.00980 111 GLU A CA  
965  C  C   . GLU A 108 ? 0.10615 0.08705 0.07335 -0.00170 -0.00000 -0.00970 111 GLU A C   
966  O  O   . GLU A 108 ? 0.11835 0.09195 0.08905 0.01290  0.01300  -0.00290 111 GLU A O   
967  C  CB  . GLU A 108 ? 0.15025 0.11255 0.13305 -0.00140 -0.04390 0.01020  111 GLU A CB  
968  C  CG  . GLU A 108 ? 0.17385 0.15035 0.17655 -0.00930 -0.06840 0.01810  111 GLU A CG  
969  C  CD  . GLU A 108 ? 0.20085 0.19365 0.23025 -0.02590 -0.08160 0.03510  111 GLU A CD  
970  O  OE1 . GLU A 108 ? 0.20715 0.19895 0.23985 -0.01150 -0.07040 0.01510  111 GLU A OE1 
971  O  OE2 . GLU A 108 ? 0.22255 0.23435 0.25905 -0.04950 -0.12270 0.05840  111 GLU A OE2 
972  N  N   . VAL A 109 ? 0.10395 0.07885 0.09815 0.00560  -0.01070 -0.00800 112 VAL A N   
973  C  CA  . VAL A 109 ? 0.09615 0.08695 0.10345 0.00610  -0.00660 -0.00430 112 VAL A CA  
974  C  C   . VAL A 109 ? 0.08245 0.09515 0.09655 -0.00010 -0.00150 -0.00640 112 VAL A C   
975  O  O   . VAL A 109 ? 0.09915 0.09295 0.08655 0.00900  -0.00370 -0.01200 112 VAL A O   
976  C  CB  . VAL A 109 ? 0.11475 0.08415 0.11835 -0.00150 -0.00550 -0.01110 112 VAL A CB  
977  C  CG1 . VAL A 109 ? 0.10215 0.09345 0.11335 0.00340  -0.01780 -0.00160 112 VAL A CG1 
978  C  CG2 . VAL A 109 ? 0.10645 0.09805 0.12395 -0.00370 -0.00590 -0.02390 112 VAL A CG2 
979  N  N   . LYS A 110 ? 0.08075 0.08625 0.10385 0.00590  0.00330  -0.01450 113 LYS A N   
982  C  C   . LYS A 110 ? 0.07905 0.08845 0.09505 0.00790  -0.01380 -0.00030 113 LYS A C   
983  O  O   . LYS A 110 ? 0.10695 0.09995 0.09555 -0.00270 -0.00720 -0.00610 113 LYS A O   
994  N  N   . PHE A 111 ? 0.10165 0.08985 0.11935 -0.00810 -0.00600 -0.00520 114 PHE A N   
995  C  CA  . PHE A 111 ? 0.09625 0.08845 0.13315 -0.00150 -0.01680 -0.00440 114 PHE A CA  
996  C  C   . PHE A 111 ? 0.08595 0.10885 0.14245 -0.01150 -0.01900 -0.00010 114 PHE A C   
997  O  O   . PHE A 111 ? 0.10075 0.11515 0.15415 -0.02040 -0.02570 -0.00110 114 PHE A O   
998  C  CB  . PHE A 111 ? 0.09245 0.10055 0.13835 0.00380  -0.01550 -0.01030 114 PHE A CB  
999  C  CG  . PHE A 111 ? 0.08745 0.09315 0.14195 -0.00420 -0.00840 -0.00470 114 PHE A CG  
1000 C  CD1 . PHE A 111 ? 0.09525 0.10205 0.13905 0.00370  -0.00670 -0.01640 114 PHE A CD1 
1001 C  CD2 . PHE A 111 ? 0.10895 0.08795 0.14325 -0.00570 -0.01440 0.00270  114 PHE A CD2 
1002 C  CE1 . PHE A 111 ? 0.10385 0.08305 0.12445 0.02040  -0.01730 -0.02580 114 PHE A CE1 
1003 C  CE2 . PHE A 111 ? 0.10255 0.11705 0.13955 -0.00750 -0.00730 -0.00060 114 PHE A CE2 
1004 C  CZ  . PHE A 111 ? 0.10975 0.08855 0.13985 0.01280  -0.01070 -0.00260 114 PHE A CZ  
1005 N  N   . GLU A 112 ? 0.08165 0.09725 0.15745 -0.01300 0.00590  0.00190  115 GLU A N   
1006 C  CA  . GLU A 112 ? 0.07465 0.10375 0.15295 -0.00100 0.00800  0.00430  115 GLU A CA  
1007 C  C   . GLU A 112 ? 0.08105 0.11585 0.15255 -0.01180 0.00800  -0.00390 115 GLU A C   
1008 O  O   . GLU A 112 ? 0.09785 0.12245 0.13845 -0.00600 -0.00010 0.00500  115 GLU A O   
1009 C  CB  . GLU A 112 ? 0.09785 0.09735 0.16855 -0.01030 0.00680  -0.00390 115 GLU A CB  
1010 C  CG  . GLU A 112 ? 0.09915 0.10415 0.20335 -0.01770 -0.01470 0.02060  115 GLU A CG  
1011 C  CD  . GLU A 112 ? 0.13435 0.11655 0.23185 -0.02440 -0.03650 0.03280  115 GLU A CD  
1012 O  OE1 . GLU A 112 ? 0.10885 0.11175 0.20795 -0.00310 -0.01900 0.02460  115 GLU A OE1 
1013 O  OE2 . GLU A 112 ? 0.19875 0.14835 0.28485 -0.03710 -0.08850 0.05700  115 GLU A OE2 
1014 N  N   . GLY A 113 ? 0.08515 0.10035 0.18505 -0.00930 -0.01540 -0.01600 116 GLY A N   
1015 C  CA  . GLY A 113 ? 0.10815 0.11205 0.18605 -0.00060 -0.01590 0.01170  116 GLY A CA  
1016 C  C   . GLY A 113 ? 0.11105 0.10765 0.17675 -0.00600 -0.00510 0.00960  116 GLY A C   
1017 O  O   . GLY A 113 ? 0.11605 0.12585 0.18895 -0.00990 -0.01130 0.00010  116 GLY A O   
1018 N  N   . ASP A 114 ? 0.09115 0.11235 0.16665 -0.00810 -0.00200 0.01230  117 ASP A N   
1019 C  CA  A ASP A 114 ? 0.10245 0.09205 0.18285 -0.00010 -0.01130 0.01940  117 ASP A CA  
1021 C  C   . ASP A 114 ? 0.10645 0.08735 0.14905 0.00340  -0.00130 0.01340  117 ASP A C   
1022 O  O   . ASP A 114 ? 0.09175 0.11965 0.17365 0.01240  -0.00730 0.00400  117 ASP A O   
1023 C  CB  A ASP A 114 ? 0.13115 0.10265 0.22075 -0.00770 -0.02080 0.02710  117 ASP A CB  
1025 C  CG  A ASP A 114 ? 0.15185 0.10655 0.25665 -0.02700 0.00900  0.01580  117 ASP A CG  
1027 O  OD1 A ASP A 114 ? 0.15795 0.08955 0.27435 -0.03120 0.01820  -0.01050 117 ASP A OD1 
1029 O  OD2 A ASP A 114 ? 0.18385 0.12385 0.28005 -0.03880 0.01560  0.02100  117 ASP A OD2 
1031 N  N   . THR A 115 ? 0.10405 0.07175 0.14075 -0.00550 -0.00010 0.00650  118 THR A N   
1032 C  CA  . THR A 115 ? 0.10775 0.09785 0.12165 -0.01050 0.00180  0.01430  118 THR A CA  
1033 C  C   . THR A 115 ? 0.08025 0.09445 0.11605 -0.00660 -0.01150 0.00800  118 THR A C   
1034 O  O   . THR A 115 ? 0.09945 0.09815 0.11815 0.00180  -0.01100 -0.00090 118 THR A O   
1035 C  CB  . THR A 115 ? 0.12275 0.10115 0.12585 -0.01140 0.02030  0.01950  118 THR A CB  
1036 O  OG1 . THR A 115 ? 0.18395 0.11325 0.14725 -0.00440 0.02620  0.03870  118 THR A OG1 
1037 C  CG2 . THR A 115 ? 0.09075 0.10735 0.15025 -0.01310 0.01560  -0.02070 118 THR A CG2 
1038 N  N   . LEU A 116 ? 0.06975 0.09125 0.11085 -0.00210 0.00140  0.00310  119 LEU A N   
1039 C  CA  . LEU A 116 ? 0.08705 0.10845 0.09465 0.01070  -0.00300 0.00340  119 LEU A CA  
1040 C  C   . LEU A 116 ? 0.08085 0.09625 0.10205 -0.00070 -0.00520 -0.00010 119 LEU A C   
1041 O  O   . LEU A 116 ? 0.08635 0.08485 0.10735 0.00480  -0.00140 -0.00550 119 LEU A O   
1042 C  CB  . LEU A 116 ? 0.08035 0.11075 0.09745 -0.00500 -0.00870 0.01260  119 LEU A CB  
1043 C  CG  . LEU A 116 ? 0.08965 0.09125 0.08505 0.00990  -0.00160 0.00180  119 LEU A CG  
1044 C  CD1 . LEU A 116 ? 0.09635 0.07445 0.10765 -0.00030 -0.00580 0.00540  119 LEU A CD1 
1045 C  CD2 . LEU A 116 ? 0.09605 0.09765 0.09085 0.00820  -0.00280 0.00100  119 LEU A CD2 
1046 N  N   . VAL A 117 ? 0.08355 0.07735 0.10845 0.00270  0.00490  -0.00140 120 VAL A N   
1047 C  CA  . VAL A 117 ? 0.09405 0.07465 0.11635 0.00950  0.01370  -0.00120 120 VAL A CA  
1048 C  C   . VAL A 117 ? 0.09055 0.07645 0.09545 0.00190  0.00790  0.00130  120 VAL A C   
1049 O  O   . VAL A 117 ? 0.12305 0.08815 0.09095 -0.00370 0.00710  -0.00600 120 VAL A O   
1050 C  CB  . VAL A 117 ? 0.08775 0.09495 0.15865 -0.00540 0.01790  -0.00150 120 VAL A CB  
1051 C  CG1 . VAL A 117 ? 0.11925 0.10235 0.18575 0.00660  0.01440  -0.00430 120 VAL A CG1 
1052 C  CG2 . VAL A 117 ? 0.10055 0.08065 0.15685 -0.01630 0.01230  0.00440  120 VAL A CG2 
1053 N  N   . ASN A 118 ? 0.07995 0.06025 0.09805 0.00140  0.00190  -0.00340 121 ASN A N   
1054 C  CA  . ASN A 118 ? 0.09035 0.06395 0.10075 -0.00760 0.00730  0.00250  121 ASN A CA  
1055 C  C   . ASN A 118 ? 0.09495 0.06405 0.07825 0.00450  0.00490  0.01250  121 ASN A C   
1056 O  O   . ASN A 118 ? 0.09505 0.07495 0.07485 0.00160  0.01190  -0.00250 121 ASN A O   
1057 C  CB  . ASN A 118 ? 0.08945 0.07885 0.09315 -0.01460 -0.01740 0.00250  121 ASN A CB  
1058 C  CG  . ASN A 118 ? 0.08065 0.08025 0.07575 0.00380  0.00470  -0.00030 121 ASN A CG  
1059 O  OD1 . ASN A 118 ? 0.09215 0.07285 0.08485 0.00540  -0.00540 0.00090  121 ASN A OD1 
1060 N  ND2 . ASN A 118 ? 0.07245 0.07795 0.08395 -0.00100 0.00500  -0.01810 121 ASN A ND2 
1061 N  N   . ARG A 119 ? 0.09165 0.07255 0.10015 0.00750  -0.01360 0.00990  122 ARG A N   
1062 C  CA  A ARG A 119 ? 0.09005 0.07825 0.10605 0.01150  -0.00120 0.00560  122 ARG A CA  
1064 C  C   . ARG A 119 ? 0.08745 0.09335 0.09565 0.00310  0.00570  0.00110  122 ARG A C   
1065 O  O   . ARG A 119 ? 0.13405 0.09055 0.08085 0.01230  0.00060  0.00000  122 ARG A O   
1066 C  CB  A ARG A 119 ? 0.10295 0.07965 0.12015 0.01550  -0.00340 0.02170  122 ARG A CB  
1068 C  CG  A ARG A 119 ? 0.12355 0.09415 0.13835 0.00500  -0.00170 0.01150  122 ARG A CG  
1070 C  CD  A ARG A 119 ? 0.13015 0.10225 0.15925 -0.00330 -0.02410 0.00280  122 ARG A CD  
1072 N  NE  A ARG A 119 ? 0.14735 0.09965 0.17145 -0.00160 -0.02660 -0.00560 122 ARG A NE  
1074 C  CZ  A ARG A 119 ? 0.18485 0.11855 0.16585 -0.02140 -0.01870 0.00180  122 ARG A CZ  
1076 N  NH1 A ARG A 119 ? 0.15745 0.12215 0.16475 -0.04250 -0.01720 0.01660  122 ARG A NH1 
1078 N  NH2 A ARG A 119 ? 0.21095 0.11935 0.15525 -0.03960 -0.02370 -0.00110 122 ARG A NH2 
1080 N  N   . ILE A 120 ? 0.08395 0.08705 0.10075 -0.00610 -0.00360 -0.00150 123 ILE A N   
1081 C  CA  . ILE A 120 ? 0.08105 0.08195 0.12175 0.00650  -0.00170 -0.00680 123 ILE A CA  
1082 C  C   . ILE A 120 ? 0.09215 0.09065 0.10335 -0.00690 0.00170  -0.00400 123 ILE A C   
1083 O  O   . ILE A 120 ? 0.09245 0.10135 0.08745 0.00670  0.00810  0.00150  123 ILE A O   
1084 C  CB  . ILE A 120 ? 0.08625 0.10125 0.15265 0.02310  -0.02890 -0.00590 123 ILE A CB  
1085 C  CG1 . ILE A 120 ? 0.08465 0.12345 0.11735 0.03130  -0.02170 0.00560  123 ILE A CG1 
1086 C  CG2 . ILE A 120 ? 0.10755 0.09915 0.19795 0.02070  -0.04450 -0.00070 123 ILE A CG2 
1087 C  CD1 . ILE A 120 ? 0.12005 0.12655 0.11035 0.03350  0.01860  0.02330  123 ILE A CD1 
1088 N  N   . GLU A 121 ? 0.09345 0.07505 0.11515 0.01230  -0.01530 -0.00260 124 GLU A N   
1092 C  C   . GLU A 121 ? 0.09285 0.08665 0.09005 0.00750  0.00960  0.00980  124 GLU A C   
1093 O  O   . GLU A 121 ? 0.11455 0.08895 0.11625 -0.00540 0.02110  -0.00720 124 GLU A O   
1109 N  N   . LEU A 122 ? 0.08275 0.07215 0.10185 0.00920  0.01950  -0.00150 125 LEU A N   
1110 C  CA  . LEU A 122 ? 0.08815 0.06575 0.09885 0.00860  -0.00240 -0.00330 125 LEU A CA  
1111 C  C   . LEU A 122 ? 0.10585 0.08225 0.10115 -0.00030 0.00910  -0.00150 125 LEU A C   
1112 O  O   . LEU A 122 ? 0.09965 0.09505 0.10635 0.00620  0.00990  -0.00370 125 LEU A O   
1113 C  CB  . LEU A 122 ? 0.10205 0.09925 0.09575 -0.00390 -0.01530 -0.00750 125 LEU A CB  
1114 C  CG  . LEU A 122 ? 0.08175 0.08995 0.10145 0.00280  -0.00150 -0.01460 125 LEU A CG  
1115 C  CD1 . LEU A 122 ? 0.07745 0.09525 0.08285 0.00370  -0.00180 -0.00820 125 LEU A CD1 
1116 C  CD2 . LEU A 122 ? 0.10165 0.09545 0.11005 0.00680  0.02200  -0.01770 125 LEU A CD2 
1117 N  N   . LYS A 123 ? 0.08355 0.07025 0.11125 -0.00070 0.00300  0.00700  126 LYS A N   
1118 C  CA  . LYS A 123 ? 0.09505 0.06295 0.11575 0.01770  0.00520  -0.00130 126 LYS A CA  
1119 C  C   . LYS A 123 ? 0.08635 0.06885 0.11595 0.01410  0.00770  -0.00420 126 LYS A C   
1120 O  O   . LYS A 123 ? 0.09875 0.08515 0.11535 0.01180  0.01980  -0.00870 126 LYS A O   
1121 C  CB  . LYS A 123 ? 0.10645 0.08805 0.11755 0.00610  -0.01420 0.01320  126 LYS A CB  
1122 C  CG  . LYS A 123 ? 0.12155 0.09685 0.14805 0.00410  -0.00660 0.01260  126 LYS A CG  
1123 C  CD  . LYS A 123 ? 0.11785 0.12435 0.15235 0.02700  -0.00410 0.00190  126 LYS A CD  
1124 C  CE  . LYS A 123 ? 0.12405 0.13985 0.15675 0.03920  -0.01570 -0.01920 126 LYS A CE  
1125 N  NZ  . LYS A 123 ? 0.14925 0.16495 0.19655 0.02730  -0.03510 -0.02230 126 LYS A NZ  
1126 N  N   . GLY A 124 ? 0.08485 0.07385 0.11075 -0.00540 0.00610  0.00550  127 GLY A N   
1127 C  CA  . GLY A 124 ? 0.08125 0.07775 0.10465 0.01050  -0.00100 0.00470  127 GLY A CA  
1128 C  C   . GLY A 124 ? 0.07035 0.07365 0.11515 -0.00190 -0.00610 0.00610  127 GLY A C   
1129 O  O   . GLY A 124 ? 0.06735 0.09725 0.11995 -0.00490 0.01120  -0.00050 127 GLY A O   
1130 N  N   . ILE A 125 ? 0.09525 0.05755 0.11125 0.00660  -0.00780 0.00960  128 ILE A N   
1131 C  CA  . ILE A 125 ? 0.08965 0.07705 0.11175 -0.00640 -0.01270 0.00160  128 ILE A CA  
1132 C  C   . ILE A 125 ? 0.09545 0.07225 0.12365 0.00930  0.01010  0.00480  128 ILE A C   
1133 O  O   . ILE A 125 ? 0.09155 0.09055 0.12075 0.00520  0.00870  0.01220  128 ILE A O   
1134 C  CB  . ILE A 125 ? 0.08545 0.09145 0.11015 0.00830  -0.00660 0.00290  128 ILE A CB  
1135 C  CG1 . ILE A 125 ? 0.10175 0.10685 0.10455 0.01630  -0.00730 -0.00260 128 ILE A CG1 
1136 C  CG2 . ILE A 125 ? 0.10085 0.08975 0.10815 0.00010  -0.02200 0.01200  128 ILE A CG2 
1137 C  CD1 . ILE A 125 ? 0.15185 0.13545 0.11755 0.01210  -0.01750 -0.01550 128 ILE A CD1 
1138 N  N   . ASP A 126 ? 0.10785 0.07125 0.14305 0.00190  -0.01900 -0.00180 129 ASP A N   
1139 C  CA  A ASP A 126 ? 0.11255 0.10305 0.17935 -0.03060 -0.04610 0.01840  129 ASP A CA  
1141 C  C   . ASP A 126 ? 0.10095 0.09385 0.14755 0.01870  -0.00990 -0.00580 129 ASP A C   
1142 O  O   . ASP A 126 ? 0.10765 0.10185 0.15205 -0.01440 -0.02150 0.00340  129 ASP A O   
1143 C  CB  A ASP A 126 ? 0.15365 0.17145 0.22635 -0.07380 -0.07430 0.06350  129 ASP A CB  
1145 C  CG  A ASP A 126 ? 0.22165 0.25535 0.28785 -0.06330 -0.06330 0.08420  129 ASP A CG  
1147 O  OD1 A ASP A 126 ? 0.21835 0.29705 0.31305 -0.06330 -0.06330 0.11390  129 ASP A OD1 
1151 N  N   . PHE A 127 ? 0.09105 0.10695 0.14525 0.01270  -0.00990 -0.02070 130 PHE A N   
1152 C  CA  . PHE A 127 ? 0.09365 0.08935 0.13435 0.01950  -0.00430 -0.00960 130 PHE A CA  
1153 C  C   . PHE A 127 ? 0.09725 0.09895 0.14085 0.01350  0.00590  -0.01470 130 PHE A C   
1154 O  O   . PHE A 127 ? 0.12045 0.10285 0.16115 0.00930  -0.00910 -0.03240 130 PHE A O   
1155 C  CB  . PHE A 127 ? 0.10455 0.08905 0.13315 -0.00020 -0.00250 0.00060  130 PHE A CB  
1156 C  CG  . PHE A 127 ? 0.08935 0.07955 0.11025 -0.00840 -0.00570 0.00140  130 PHE A CG  
1157 C  CD1 . PHE A 127 ? 0.09295 0.09605 0.09145 0.00620  0.00150  0.00830  130 PHE A CD1 
1158 C  CD2 . PHE A 127 ? 0.09875 0.07475 0.11285 -0.00870 0.01860  0.01350  130 PHE A CD2 
1159 C  CE1 . PHE A 127 ? 0.10715 0.06945 0.08975 0.00710  -0.00110 0.00920  130 PHE A CE1 
1160 C  CE2 . PHE A 127 ? 0.08545 0.09145 0.10115 0.00990  0.02790  0.02240  130 PHE A CE2 
1161 C  CZ  . PHE A 127 ? 0.08905 0.07345 0.10015 -0.01180 0.01320  0.02370  130 PHE A CZ  
1162 N  N   . LYS A 128 ? 0.10855 0.10945 0.12415 -0.01200 -0.01200 -0.00980 131 LYS A N   
1163 C  CA  A LYS A 128 ? 0.11575 0.11885 0.15605 -0.02190 -0.00360 -0.02850 131 LYS A CA  
1165 C  C   . LYS A 128 ? 0.13105 0.13025 0.16215 0.00650  -0.00030 -0.03340 131 LYS A C   
1166 O  O   . LYS A 128 ? 0.15795 0.13695 0.16625 0.02700  0.00420  -0.02320 131 LYS A O   
1167 C  CB  A LYS A 128 ? 0.10865 0.11815 0.18745 -0.03820 0.00630  -0.01900 131 LYS A CB  
1169 C  CG  A LYS A 128 ? 0.12565 0.14185 0.21115 -0.02840 0.01810  -0.00130 131 LYS A CG  
1171 C  CD  A LYS A 128 ? 0.14745 0.17205 0.23645 -0.02450 0.05730  0.01740  131 LYS A CD  
1173 C  CE  A LYS A 128 ? 0.22935 0.22715 0.26695 -0.00300 0.03560  0.03510  131 LYS A CE  
1177 N  N   . GLU A 129 ? 0.13735 0.16455 0.19285 0.03950  0.00500  -0.06010 132 GLU A N   
1178 C  CA  . GLU A 129 ? 0.19955 0.21165 0.21605 0.07940  0.01280  -0.04820 132 GLU A CA  
1179 C  C   . GLU A 129 ? 0.24395 0.19855 0.21195 0.08840  0.01220  -0.03930 132 GLU A C   
1180 O  O   . GLU A 129 ? 0.31625 0.20515 0.21175 0.06770  0.01190  -0.01910 132 GLU A O   
1181 C  CB  . GLU A 129 ? 0.23825 0.25715 0.24565 0.09170  0.02700  -0.04910 132 GLU A CB  
1186 N  N   . ASP A 130 ? 0.20255 0.19415 0.21435 0.09000  -0.00110 -0.07880 133 ASP A N   
1187 C  CA  . ASP A 130 ? 0.24095 0.21775 0.21805 0.10020  -0.02330 -0.07440 133 ASP A CA  
1188 C  C   . ASP A 130 ? 0.22095 0.17525 0.18125 0.08240  -0.04860 -0.04560 133 ASP A C   
1189 O  O   . ASP A 130 ? 0.26295 0.19035 0.17255 0.05700  -0.07050 -0.04550 133 ASP A O   
1194 N  N   . GLY A 131 ? 0.18425 0.14545 0.14725 0.04900  -0.03090 -0.04230 134 GLY A N   
1195 C  CA  . GLY A 131 ? 0.14965 0.12075 0.15135 0.02520  -0.01250 -0.02380 134 GLY A CA  
1196 C  C   . GLY A 131 ? 0.11815 0.12185 0.11995 -0.00780 -0.00220 -0.02240 134 GLY A C   
1197 O  O   . GLY A 131 ? 0.10915 0.14815 0.11875 0.01710  0.00030  -0.02920 134 GLY A O   
1198 N  N   . ASN A 132 ? 0.09585 0.11705 0.11995 -0.00170 -0.01510 -0.02350 135 ASN A N   
1199 C  CA  . ASN A 132 ? 0.08615 0.11195 0.12185 -0.00690 -0.00860 -0.00550 135 ASN A CA  
1200 C  C   . ASN A 132 ? 0.08105 0.11925 0.10115 -0.00080 0.00040  -0.00040 135 ASN A C   
1201 O  O   . ASN A 132 ? 0.09535 0.11595 0.09565 0.00240  -0.00390 -0.01430 135 ASN A O   
1202 C  CB  . ASN A 132 ? 0.11085 0.14495 0.13145 -0.02280 -0.00390 -0.02940 135 ASN A CB  
1203 C  CG  . ASN A 132 ? 0.10805 0.15055 0.12175 -0.01270 -0.00480 -0.03530 135 ASN A CG  
1204 O  OD1 . ASN A 132 ? 0.13145 0.18185 0.14225 -0.05030 0.00850  -0.05010 135 ASN A OD1 
1205 N  ND2 . ASN A 132 ? 0.08115 0.14825 0.13035 0.00510  0.01070  -0.02190 135 ASN A ND2 
1206 N  N   . ILE A 133 ? 0.08645 0.10555 0.10275 -0.00510 -0.00170 -0.01450 136 ILE A N   
1207 C  CA  . ILE A 133 ? 0.09735 0.09085 0.09845 -0.00590 0.00630  -0.00670 136 ILE A CA  
1208 C  C   . ILE A 133 ? 0.09375 0.09975 0.10435 -0.00110 -0.00350 -0.00030 136 ILE A C   
1209 O  O   . ILE A 133 ? 0.11625 0.10675 0.10445 -0.01390 -0.00970 -0.01870 136 ILE A O   
1210 C  CB  . ILE A 133 ? 0.09745 0.10175 0.11315 -0.00500 -0.00720 -0.01120 136 ILE A CB  
1211 C  CG1 . ILE A 133 ? 0.11055 0.12365 0.12575 0.01310  -0.01090 -0.02330 136 ILE A CG1 
1212 C  CG2 . ILE A 133 ? 0.11155 0.09225 0.11325 -0.02670 -0.02090 0.00780  136 ILE A CG2 
1213 C  CD1 . ILE A 133 ? 0.13995 0.14175 0.14235 -0.01040 -0.00240 -0.04740 136 ILE A CD1 
1214 N  N   . LEU A 134 ? 0.08585 0.11715 0.11265 -0.00670 0.00130  -0.00300 137 LEU A N   
1215 C  CA  . LEU A 134 ? 0.10015 0.14315 0.10765 0.00870  0.00210  -0.00510 137 LEU A CA  
1216 C  C   . LEU A 134 ? 0.11485 0.15995 0.10795 0.01910  0.01040  -0.01510 137 LEU A C   
1217 O  O   . LEU A 134 ? 0.13245 0.21865 0.11725 0.00480  0.00190  -0.01950 137 LEU A O   
1218 C  CB  . LEU A 134 ? 0.11385 0.16655 0.11185 0.00800  -0.00510 -0.00440 137 LEU A CB  
1219 C  CG  . LEU A 134 ? 0.12925 0.17855 0.11745 0.01040  -0.00780 0.00810  137 LEU A CG  
1220 C  CD1 . LEU A 134 ? 0.11215 0.17995 0.12235 0.02840  -0.00040 0.00790  137 LEU A CD1 
1221 C  CD2 . LEU A 134 ? 0.12985 0.19155 0.12215 -0.00650 0.00640  0.00820  137 LEU A CD2 
1222 N  N   . GLY A 135 ? 0.12775 0.13735 0.10855 0.01720  -0.00530 -0.01080 138 GLY A N   
1223 C  CA  . GLY A 135 ? 0.16075 0.13265 0.11075 0.01550  -0.00020 -0.00440 138 GLY A CA  
1224 C  C   . GLY A 135 ? 0.13905 0.12295 0.09885 -0.00950 0.00440  -0.00480 138 GLY A C   
1225 O  O   . GLY A 135 ? 0.14635 0.15555 0.10815 -0.00130 0.00400  -0.02240 138 GLY A O   
1226 N  N   . HIS A 136 ? 0.10065 0.12825 0.12265 -0.00050 0.01260  -0.00580 139 HIS A N   
1227 C  CA  . HIS A 136 ? 0.10185 0.13695 0.11715 -0.00830 0.01370  -0.00190 139 HIS A CA  
1228 C  C   . HIS A 136 ? 0.11885 0.12785 0.10305 -0.00980 0.01760  -0.01780 139 HIS A C   
1229 O  O   . HIS A 136 ? 0.13535 0.15065 0.09685 -0.01710 0.00770  -0.01130 139 HIS A O   
1230 C  CB  . HIS A 136 ? 0.10995 0.15135 0.11515 -0.01980 0.00580  -0.02200 139 HIS A CB  
1231 C  CG  . HIS A 136 ? 0.10455 0.18435 0.11895 -0.02190 0.00040  -0.03090 139 HIS A CG  
1232 N  ND1 . HIS A 136 ? 0.12505 0.20195 0.11385 -0.04290 0.00640  -0.01910 139 HIS A ND1 
1233 C  CD2 . HIS A 136 ? 0.11835 0.23045 0.15765 -0.02540 0.00300  -0.05190 139 HIS A CD2 
1234 C  CE1 . HIS A 136 ? 0.12605 0.23505 0.15705 -0.02950 0.02900  -0.03270 139 HIS A CE1 
1235 N  NE2 . HIS A 136 ? 0.14535 0.24675 0.18435 -0.03690 0.00290  -0.05360 139 HIS A NE2 
1236 N  N   . LYS A 137 ? 0.08545 0.10575 0.12255 -0.00070 0.00390  -0.01140 140 LYS A N   
1237 C  CA  . LYS A 137 ? 0.08915 0.11015 0.12665 0.01030  -0.01330 -0.00890 140 LYS A CA  
1238 C  C   . LYS A 137 ? 0.09085 0.10815 0.11515 0.00280  -0.01390 0.00190  140 LYS A C   
1239 O  O   . LYS A 137 ? 0.10895 0.10835 0.13565 -0.00930 -0.01250 -0.01760 140 LYS A O   
1240 C  CB  . LYS A 137 ? 0.10825 0.09525 0.13885 -0.01070 -0.01430 0.00590  140 LYS A CB  
1241 C  CG  . LYS A 137 ? 0.11555 0.10165 0.16135 0.00450  -0.01310 -0.00210 140 LYS A CG  
1242 C  CD  . LYS A 137 ? 0.13805 0.10315 0.17975 0.00180  -0.00680 0.00040  140 LYS A CD  
1243 C  CE  . LYS A 137 ? 0.16055 0.09835 0.20605 0.01910  -0.01980 -0.01950 140 LYS A CE  
1244 N  NZ  . LYS A 137 ? 0.18475 0.10855 0.23195 0.01160  -0.01520 -0.02910 140 LYS A NZ  
1245 N  N   . LEU A 138 ? 0.10555 0.08985 0.11835 -0.00660 -0.00740 0.00150  141 LEU A N   
1246 C  CA  . LEU A 138 ? 0.11375 0.09785 0.10405 0.00190  -0.01370 0.00470  141 LEU A CA  
1247 C  C   . LEU A 138 ? 0.10775 0.11635 0.11275 -0.01960 -0.01440 0.00990  141 LEU A C   
1248 O  O   . LEU A 138 ? 0.12915 0.13535 0.13415 -0.01590 -0.00450 0.02820  141 LEU A O   
1249 C  CB  . LEU A 138 ? 0.11305 0.11285 0.09505 -0.00540 -0.02600 -0.00670 141 LEU A CB  
1250 C  CG  . LEU A 138 ? 0.10865 0.13415 0.10735 -0.03950 -0.01750 -0.00890 141 LEU A CG  
1251 C  CD1 . LEU A 138 ? 0.13415 0.15495 0.12535 -0.04470 0.00150  -0.00930 141 LEU A CD1 
1252 C  CD2 . LEU A 138 ? 0.11075 0.13095 0.11965 -0.03260 0.00150  0.00110  141 LEU A CD2 
1253 N  N   . GLU A 139 ? 0.11425 0.11135 0.10715 -0.01060 -0.01250 -0.01300 142 GLU A N   
1254 C  CA  . GLU A 139 ? 0.10935 0.12155 0.12525 -0.00790 -0.01340 -0.00450 142 GLU A CA  
1255 C  C   . GLU A 139 ? 0.11085 0.11575 0.10865 -0.01590 -0.00210 0.00900  142 GLU A C   
1256 O  O   . GLU A 139 ? 0.13025 0.10565 0.09665 -0.01560 -0.00020 0.00680  142 GLU A O   
1257 C  CB  . GLU A 139 ? 0.10405 0.11765 0.16425 -0.00090 -0.02730 0.00650  142 GLU A CB  
1258 C  CG  . GLU A 139 ? 0.12655 0.11785 0.17985 -0.02820 -0.03200 0.00690  142 GLU A CG  
1259 C  CD  . GLU A 139 ? 0.15425 0.12035 0.18815 -0.01640 -0.05010 -0.00460 142 GLU A CD  
1260 O  OE1 . GLU A 139 ? 0.13315 0.15445 0.16295 -0.01390 -0.03120 0.00350  142 GLU A OE1 
1261 O  OE2 . GLU A 139 ? 0.17495 0.15125 0.22815 -0.01530 -0.07300 -0.03060 142 GLU A OE2 
1262 N  N   . TYR A 140 ? 0.12175 0.10965 0.11225 -0.01160 -0.00010 -0.00220 143 TYR A N   
1263 C  CA  . TYR A 140 ? 0.13195 0.09565 0.09705 -0.02420 0.00220  0.00000  143 TYR A CA  
1264 C  C   . TYR A 140 ? 0.12485 0.10165 0.10235 -0.02390 -0.00310 0.00650  143 TYR A C   
1265 O  O   . TYR A 140 ? 0.13095 0.12415 0.11205 -0.00810 -0.00910 0.00980  143 TYR A O   
1266 C  CB  . TYR A 140 ? 0.14545 0.12735 0.08405 -0.03300 -0.01200 0.00490  143 TYR A CB  
1267 C  CG  . TYR A 140 ? 0.12165 0.13785 0.08345 -0.03130 -0.00950 -0.00050 143 TYR A CG  
1268 C  CD1 . TYR A 140 ? 0.09475 0.13885 0.10545 -0.02510 -0.00480 0.00620  143 TYR A CD1 
1269 C  CD2 . TYR A 140 ? 0.12015 0.11675 0.08825 -0.02340 0.00370  -0.01080 143 TYR A CD2 
1270 C  CE1 . TYR A 140 ? 0.10835 0.13855 0.10525 -0.01770 -0.00120 0.01290  143 TYR A CE1 
1271 C  CE2 . TYR A 140 ? 0.12465 0.12375 0.09865 -0.02340 -0.00990 -0.01590 143 TYR A CE2 
1272 C  CZ  . TYR A 140 ? 0.11095 0.11615 0.10135 -0.02400 -0.02510 0.00370  143 TYR A CZ  
1273 O  OH  . TYR A 140 ? 0.11235 0.12335 0.12175 -0.03460 -0.02510 0.00230  143 TYR A OH  
1274 N  N   . ASN A 141 ? 0.12265 0.10915 0.11175 -0.00410 -0.00530 -0.00030 144 ASN A N   
1275 C  CA  . ASN A 141 ? 0.12245 0.10855 0.10935 -0.00410 -0.01420 -0.00480 144 ASN A CA  
1276 C  C   . ASN A 141 ? 0.11245 0.10475 0.09735 -0.00200 -0.01710 -0.00350 144 ASN A C   
1277 O  O   . ASN A 141 ? 0.10725 0.09695 0.11545 -0.00540 -0.01210 0.01360  144 ASN A O   
1278 C  CB  . ASN A 141 ? 0.11545 0.11365 0.13835 -0.01550 -0.01550 -0.00500 144 ASN A CB  
1279 C  CG  . ASN A 141 ? 0.13055 0.13175 0.14715 -0.02260 -0.04390 0.01040  144 ASN A CG  
1280 O  OD1 . ASN A 141 ? 0.18255 0.14825 0.14845 -0.02950 -0.04610 0.01150  144 ASN A OD1 
1281 N  ND2 . ASN A 141 ? 0.12325 0.14635 0.15455 -0.01400 -0.04570 -0.00620 144 ASN A ND2 
1282 N  N   . TYR A 142 ? 0.11585 0.09895 0.09205 0.00620  -0.01940 -0.00020 145 TYR A N   
1283 C  CA  . TYR A 142 ? 0.10385 0.10495 0.09675 -0.01120 0.00690  0.01000  145 TYR A CA  
1284 C  C   . TYR A 142 ? 0.09605 0.11735 0.13395 -0.01010 -0.00530 0.01220  145 TYR A C   
1285 O  O   . TYR A 142 ? 0.10885 0.13955 0.18255 0.00820  -0.00850 0.04150  145 TYR A O   
1286 C  CB  . TYR A 142 ? 0.12895 0.10775 0.10095 -0.01900 -0.00170 0.01450  145 TYR A CB  
1287 C  CG  . TYR A 142 ? 0.10185 0.08525 0.10325 -0.01840 -0.00520 0.00500  145 TYR A CG  
1288 C  CD1 . TYR A 142 ? 0.08205 0.08285 0.11085 -0.00940 -0.00200 0.00610  145 TYR A CD1 
1289 C  CD2 . TYR A 142 ? 0.11155 0.08375 0.10675 -0.00820 -0.01970 0.00830  145 TYR A CD2 
1290 C  CE1 . TYR A 142 ? 0.09995 0.08845 0.10085 -0.02810 -0.00310 -0.00090 145 TYR A CE1 
1291 C  CE2 . TYR A 142 ? 0.09285 0.09795 0.11415 0.00430  -0.00590 0.00060  145 TYR A CE2 
1292 C  CZ  . TYR A 142 ? 0.09045 0.08815 0.09145 -0.01700 -0.00410 -0.00080 145 TYR A CZ  
1293 O  OH  . TYR A 142 ? 0.09085 0.10955 0.08925 -0.00140 0.00730  -0.00020 145 TYR A OH  
1294 N  N   . ASN A 143 ? 0.08725 0.12875 0.11915 -0.00580 0.00310  0.00060  146 ASN A N   
1295 C  CA  . ASN A 143 ? 0.11265 0.12325 0.13035 -0.01240 0.01150  -0.01110 146 ASN A CA  
1296 C  C   . ASN A 143 ? 0.09625 0.12425 0.11865 -0.01610 0.00810  0.00890  146 ASN A C   
1297 O  O   . ASN A 143 ? 0.11945 0.12635 0.14105 -0.02080 -0.00040 -0.00430 146 ASN A O   
1298 C  CB  . ASN A 143 ? 0.14685 0.12835 0.12615 -0.01790 -0.01710 0.00170  146 ASN A CB  
1299 C  CG  . ASN A 143 ? 0.16475 0.13115 0.14945 -0.01340 -0.04510 0.00030  146 ASN A CG  
1300 O  OD1 . ASN A 143 ? 0.20395 0.16605 0.18785 -0.00500 -0.07780 0.00250  146 ASN A OD1 
1301 N  ND2 . ASN A 143 ? 0.15965 0.14355 0.15525 0.02200  -0.04040 0.00100  146 ASN A ND2 
1302 N  N   . SER A 144 ? 0.11065 0.14305 0.11405 -0.03050 0.01080  -0.00220 147 SER A N   
1303 C  CA  . SER A 144 ? 0.10625 0.13285 0.11915 -0.01880 0.00410  -0.00540 147 SER A CA  
1304 C  C   . SER A 144 ? 0.08785 0.11185 0.12465 -0.02220 -0.00110 -0.00780 147 SER A C   
1305 O  O   . SER A 144 ? 0.09485 0.11815 0.14835 -0.02230 -0.01090 -0.01050 147 SER A O   
1306 C  CB  . SER A 144 ? 0.13515 0.16075 0.13035 -0.01950 0.00520  0.02920  147 SER A CB  
1307 O  OG  . SER A 144 ? 0.15475 0.17035 0.13635 -0.02730 -0.01750 0.02650  147 SER A OG  
1308 N  N   . HIS A 145 ? 0.07715 0.11385 0.11005 -0.01360 -0.01680 -0.01000 148 HIS A N   
1309 C  CA  . HIS A 145 ? 0.06915 0.10235 0.10795 0.00430  -0.00070 0.01220  148 HIS A CA  
1310 C  C   . HIS A 145 ? 0.08185 0.09275 0.10445 0.00610  0.01500  0.00020  148 HIS A C   
1311 O  O   . HIS A 145 ? 0.11575 0.10855 0.12455 0.00350  0.00280  0.00460  148 HIS A O   
1312 C  CB  . HIS A 145 ? 0.07395 0.10715 0.12225 0.01430  0.00850  0.00060  148 HIS A CB  
1313 C  CG  . HIS A 145 ? 0.07905 0.10925 0.12475 0.01320  0.01300  -0.01010 148 HIS A CG  
1314 N  ND1 . HIS A 145 ? 0.10485 0.13425 0.12225 0.02120  0.02080  -0.00150 148 HIS A ND1 
1315 C  CD2 . HIS A 145 ? 0.11145 0.10255 0.12445 0.00230  0.00200  -0.01820 148 HIS A CD2 
1316 C  CE1 . HIS A 145 ? 0.10735 0.12455 0.12315 0.01490  -0.00430 -0.00190 148 HIS A CE1 
1317 N  NE2 . HIS A 145 ? 0.11635 0.12595 0.13595 0.02780  -0.00860 -0.00390 148 HIS A NE2 
1318 N  N   . ASN A 146 ? 0.09035 0.11495 0.09595 0.00750  0.02010  0.00680  149 ASN A N   
1319 C  CA  . ASN A 146 ? 0.10785 0.11925 0.11585 0.00740  0.01140  -0.00160 149 ASN A CA  
1320 C  C   . ASN A 146 ? 0.11885 0.09945 0.11705 0.01690  0.00980  0.01790  149 ASN A C   
1321 O  O   . ASN A 146 ? 0.13455 0.08805 0.14495 0.00470  -0.00690 -0.00030 149 ASN A O   
1322 C  CB  . ASN A 146 ? 0.11885 0.13035 0.13745 0.01070  0.03130  -0.00980 149 ASN A CB  
1323 C  CG  . ASN A 146 ? 0.11715 0.15365 0.16855 -0.00350 0.03600  -0.00600 149 ASN A CG  
1324 O  OD1 . ASN A 146 ? 0.12465 0.17395 0.15985 0.00340  0.01470  -0.00280 149 ASN A OD1 
1325 N  ND2 . ASN A 146 ? 0.11155 0.19475 0.21055 -0.01650 0.03060  0.03410  149 ASN A ND2 
1326 N  N   . VAL A 147 ? 0.11835 0.10035 0.11475 0.01070  0.01300  -0.00200 150 VAL A N   
1327 C  CA  . VAL A 147 ? 0.11265 0.10375 0.09565 0.01000  0.01530  -0.00590 150 VAL A CA  
1328 C  C   . VAL A 147 ? 0.08765 0.10425 0.08825 0.00160  0.01190  -0.00430 150 VAL A C   
1329 O  O   . VAL A 147 ? 0.11865 0.11275 0.09115 0.01240  0.02970  0.00210  150 VAL A O   
1330 C  CB  . VAL A 147 ? 0.11355 0.12075 0.09115 0.00660  0.01330  0.00860  150 VAL A CB  
1331 C  CG1 . VAL A 147 ? 0.11645 0.11935 0.08745 0.01150  -0.00060 0.01420  150 VAL A CG1 
1332 C  CG2 . VAL A 147 ? 0.13185 0.13715 0.09145 -0.00050 0.02480  0.01770  150 VAL A CG2 
1333 N  N   . TYR A 148 ? 0.10725 0.11705 0.10265 -0.00290 0.01730  0.01440  151 TYR A N   
1334 C  CA  . TYR A 148 ? 0.10485 0.11265 0.09835 -0.01490 0.02290  0.01030  151 TYR A CA  
1335 C  C   . TYR A 148 ? 0.11155 0.11455 0.10865 -0.00360 0.02590  0.00410  151 TYR A C   
1336 O  O   . TYR A 148 ? 0.11595 0.13505 0.13455 0.01250  0.01780  -0.00930 151 TYR A O   
1337 C  CB  . TYR A 148 ? 0.12285 0.12965 0.10495 -0.00790 0.01720  0.00720  151 TYR A CB  
1338 C  CG  . TYR A 148 ? 0.12445 0.11705 0.13165 -0.01280 0.00610  0.00330  151 TYR A CG  
1339 C  CD1 . TYR A 148 ? 0.12675 0.13155 0.16745 -0.00750 0.00500  0.02390  151 TYR A CD1 
1340 C  CD2 . TYR A 148 ? 0.15025 0.12935 0.15065 -0.02380 -0.00850 0.01340  151 TYR A CD2 
1341 C  CE1 . TYR A 148 ? 0.15255 0.14915 0.15945 -0.02360 0.01260  0.01300  151 TYR A CE1 
1342 C  CE2 . TYR A 148 ? 0.14585 0.16305 0.15205 -0.02470 -0.00350 0.00860  151 TYR A CE2 
1343 C  CZ  . TYR A 148 ? 0.13595 0.15845 0.16215 -0.03550 -0.00870 0.01840  151 TYR A CZ  
1344 O  OH  . TYR A 148 ? 0.13375 0.19035 0.18575 -0.03390 -0.00320 0.02690  151 TYR A OH  
1345 N  N   . ILE A 149 ? 0.10755 0.11355 0.11305 -0.01700 0.02630  -0.00450 152 ILE A N   
1346 C  CA  . ILE A 149 ? 0.12545 0.11785 0.09825 0.01610  0.01950  -0.00720 152 ILE A CA  
1347 C  C   . ILE A 149 ? 0.11795 0.12575 0.08825 0.02130  0.02620  0.00440  152 ILE A C   
1348 O  O   . ILE A 149 ? 0.13075 0.13995 0.09805 0.01850  0.02160  -0.00430 152 ILE A O   
1349 C  CB  . ILE A 149 ? 0.12805 0.11845 0.09485 0.00130  0.01720  -0.01140 152 ILE A CB  
1350 C  CG1 . ILE A 149 ? 0.13925 0.13195 0.10105 0.00680  0.03180  0.00550  152 ILE A CG1 
1351 C  CG2 . ILE A 149 ? 0.13815 0.11845 0.11545 -0.00650 0.01290  -0.01150 152 ILE A CG2 
1352 C  CD1 . ILE A 149 ? 0.14755 0.10985 0.09555 0.02700  0.00630  0.02070  152 ILE A CD1 
1353 N  N   . THR A 150 ? 0.14855 0.12135 0.08885 0.00130  0.00930  -0.00600 153 THR A N   
1354 C  CA  A THR A 150 ? 0.15905 0.12725 0.09635 -0.00140 0.03140  -0.01010 153 THR A CA  
1356 C  C   . THR A 150 ? 0.13335 0.12325 0.09795 0.01230  0.02750  -0.00600 153 THR A C   
1357 O  O   . THR A 150 ? 0.12565 0.13455 0.09735 0.01450  0.02560  -0.01200 153 THR A O   
1358 C  CB  A THR A 150 ? 0.18125 0.14035 0.11915 -0.00530 0.02350  0.01140  153 THR A CB  
1360 O  OG1 A THR A 150 ? 0.18055 0.15735 0.15445 0.01200  -0.00990 0.03680  153 THR A OG1 
1362 C  CG2 A THR A 150 ? 0.19485 0.13355 0.12635 -0.00520 0.01110  -0.00760 153 THR A CG2 
1364 N  N   . ALA A 151 ? 0.14185 0.14535 0.09215 0.00520  0.00900  -0.00600 154 ALA A N   
1365 C  CA  . ALA A 151 ? 0.14035 0.14855 0.11225 0.01170  -0.00220 -0.01050 154 ALA A CA  
1366 C  C   . ALA A 151 ? 0.16805 0.14565 0.12205 0.02090  -0.01640 0.01380  154 ALA A C   
1367 O  O   . ALA A 151 ? 0.17525 0.14985 0.14605 0.01740  0.00270  0.02600  154 ALA A O   
1368 C  CB  . ALA A 151 ? 0.17865 0.16495 0.11715 0.01990  0.02780  -0.03480 154 ALA A CB  
1369 N  N   . ASP A 152 ? 0.15555 0.15265 0.14615 0.03580  -0.01680 0.00840  155 ASP A N   
1371 C  CA  B ASP A 152 ? 0.20285 0.19945 0.19105 0.05500  -0.02570 0.00940  155 ASP A CA  
1372 C  C   . ASP A 152 ? 0.18095 0.20815 0.17225 0.02440  -0.02780 0.01270  155 ASP A C   
1373 O  O   . ASP A 152 ? 0.20375 0.22025 0.16875 0.00490  -0.04310 0.03190  155 ASP A O   
1375 C  CB  B ASP A 152 ? 0.25605 0.25325 0.26025 0.09010  -0.02770 0.01830  155 ASP A CB  
1382 N  N   . LYS A 153 ? 0.21275 0.23355 0.18525 0.02990  0.00110  -0.00050 156 LYS A N   
1383 C  CA  . LYS A 153 ? 0.22535 0.26585 0.21165 0.02630  -0.00010 -0.01650 156 LYS A CA  
1384 C  C   . LYS A 153 ? 0.22165 0.25385 0.18355 0.00070  -0.01820 0.01100  156 LYS A C   
1385 O  O   . LYS A 153 ? 0.21725 0.26755 0.19375 -0.01630 -0.01080 0.02410  156 LYS A O   
1386 C  CB  . LYS A 153 ? 0.29245 0.32175 0.29115 0.01870  0.00260  -0.04050 156 LYS A CB  
1391 N  N   . GLN A 154 ? 0.21815 0.24055 0.17155 0.01220  -0.02980 0.01900  157 GLN A N   
1392 C  CA  . GLN A 154 ? 0.22575 0.26395 0.21065 0.02040  -0.05730 0.02270  157 GLN A CA  
1393 C  C   . GLN A 154 ? 0.19145 0.27155 0.20195 0.00950  -0.06530 0.00830  157 GLN A C   
1394 O  O   . GLN A 154 ? 0.21735 0.31475 0.20775 0.03670  -0.06980 0.01180  157 GLN A O   
1400 N  N   . LYS A 155 ? 0.19605 0.23475 0.20335 0.03120  -0.07840 0.01950  158 LYS A N   
1403 C  C   . LYS A 155 ? 0.18125 0.19105 0.19195 0.02860  -0.03390 0.00640  158 LYS A C   
1404 O  O   . LYS A 155 ? 0.15955 0.16965 0.18945 0.03490  -0.04000 0.01270  158 LYS A O   
1415 N  N   . ASN A 156 ? 0.18125 0.18965 0.16805 0.02080  -0.02370 -0.01040 159 ASN A N   
1416 C  CA  . ASN A 156 ? 0.19185 0.17725 0.13505 0.02320  -0.02510 -0.03260 159 ASN A CA  
1417 C  C   . ASN A 156 ? 0.15725 0.18175 0.10555 0.02130  -0.00920 -0.02000 159 ASN A C   
1418 O  O   . ASN A 156 ? 0.15995 0.16875 0.11595 0.02050  -0.00190 -0.02250 159 ASN A O   
1419 C  CB  . ASN A 156 ? 0.19095 0.17335 0.15315 0.05520  -0.06170 -0.04610 159 ASN A CB  
1420 C  CG  . ASN A 156 ? 0.20705 0.20845 0.16525 0.07280  -0.04720 -0.03860 159 ASN A CG  
1421 O  OD1 . ASN A 156 ? 0.23385 0.23685 0.16795 0.09310  -0.03860 -0.02520 159 ASN A OD1 
1422 N  ND2 . ASN A 156 ? 0.25605 0.23345 0.16735 0.05390  -0.03920 -0.01620 159 ASN A ND2 
1423 N  N   . GLY A 157 ? 0.15875 0.16655 0.08935 0.01210  -0.00170 -0.01200 160 GLY A N   
1424 C  CA  . GLY A 157 ? 0.14465 0.16945 0.09175 0.00570  -0.00640 -0.02080 160 GLY A CA  
1425 C  C   . GLY A 157 ? 0.13165 0.14175 0.10005 0.03240  0.01870  -0.02600 160 GLY A C   
1426 O  O   . GLY A 157 ? 0.13085 0.15725 0.11375 0.01470  0.01530  -0.01850 160 GLY A O   
1427 N  N   . ILE A 158 ? 0.13395 0.12095 0.10945 0.00390  0.01630  0.00010  161 ILE A N   
1428 C  CA  A ILE A 158 ? 0.13045 0.12105 0.10255 0.02230  0.01930  0.00230  161 ILE A CA  
1430 C  C   . ILE A 158 ? 0.12465 0.12555 0.10285 0.02720  0.02180  -0.00030 161 ILE A C   
1431 O  O   . ILE A 158 ? 0.12635 0.13695 0.09205 0.01440  0.01440  -0.00500 161 ILE A O   
1432 C  CB  A ILE A 158 ? 0.14215 0.13455 0.08815 0.02630  0.01950  0.00580  161 ILE A CB  
1434 C  CG1 A ILE A 158 ? 0.15775 0.13545 0.08915 0.01200  0.01240  -0.00220 161 ILE A CG1 
1436 C  CG2 A ILE A 158 ? 0.11945 0.13885 0.10725 0.02380  0.01520  0.00890  161 ILE A CG2 
1438 C  CD1 A ILE A 158 ? 0.15365 0.15045 0.09805 -0.00750 -0.00820 -0.00750 161 ILE A CD1 
1440 N  N   . LYS A 159 ? 0.12895 0.12975 0.10905 0.03160  0.02730  -0.00250 162 LYS A N   
1441 C  CA  A LYS A 159 ? 0.15085 0.13895 0.13805 0.04270  0.00230  -0.00440 162 LYS A CA  
1443 C  C   . LYS A 159 ? 0.10665 0.12055 0.12045 0.02560  0.00840  -0.01880 162 LYS A C   
1444 O  O   . LYS A 159 ? 0.10965 0.12605 0.13705 0.02760  0.01690  -0.02040 162 LYS A O   
1445 C  CB  A LYS A 159 ? 0.20875 0.17135 0.18885 0.06370  0.00850  0.00120  162 LYS A CB  
1447 C  CG  A LYS A 159 ? 0.23535 0.18885 0.20775 0.06030  0.00570  0.01620  162 LYS A CG  
1453 N  N   . ALA A 160 ? 0.11295 0.11095 0.12745 0.01620  -0.01370 -0.01570 163 ALA A N   
1454 C  CA  . ALA A 160 ? 0.11735 0.12405 0.13015 0.00900  -0.00700 -0.01120 163 ALA A CA  
1455 C  C   . ALA A 160 ? 0.10505 0.11115 0.12255 0.01740  0.01360  -0.01820 163 ALA A C   
1456 O  O   . ALA A 160 ? 0.11525 0.11685 0.12425 0.01360  0.01520  -0.00120 163 ALA A O   
1457 C  CB  . ALA A 160 ? 0.12485 0.14255 0.14005 0.01220  -0.01760 0.00020  163 ALA A CB  
1458 N  N   A ASN A 161 ? 0.11135 0.14355 0.15045 -0.01200 0.01820  -0.04900 164 ASN A N   
1460 C  CA  A ASN A 161 ? 0.13585 0.17835 0.17975 -0.02360 -0.00030 -0.04980 164 ASN A CA  
1462 C  C   A ASN A 161 ? 0.09675 0.14845 0.15955 0.00750  0.00890  -0.06250 164 ASN A C   
1464 O  O   A ASN A 161 ? 0.07745 0.14045 0.16185 0.01860  0.00260  -0.05690 164 ASN A O   
1466 C  CB  A ASN A 161 ? 0.20635 0.23075 0.22775 -0.01900 -0.02360 -0.02740 164 ASN A CB  
1474 N  N   . PHE A 162 ? 0.10725 0.13415 0.15305 0.00460  0.02480  -0.03960 165 PHE A N   
1475 C  CA  . PHE A 162 ? 0.10925 0.11005 0.14235 0.00930  0.00390  -0.01420 165 PHE A CA  
1476 C  C   . PHE A 162 ? 0.09925 0.09945 0.13425 0.00450  0.02490  -0.01300 165 PHE A C   
1477 O  O   . PHE A 162 ? 0.09905 0.11175 0.12925 0.01330  0.00520  -0.01820 165 PHE A O   
1478 C  CB  . PHE A 162 ? 0.12165 0.09435 0.17085 0.00810  -0.00060 -0.02080 165 PHE A CB  
1479 C  CG  . PHE A 162 ? 0.08435 0.08615 0.14255 0.00720  0.01120  -0.00370 165 PHE A CG  
1480 C  CD1 . PHE A 162 ? 0.09125 0.09865 0.14415 0.00010  -0.00750 -0.01260 165 PHE A CD1 
1481 C  CD2 . PHE A 162 ? 0.09795 0.10055 0.13775 0.03310  0.01610  0.00550  165 PHE A CD2 
1482 C  CE1 . PHE A 162 ? 0.09705 0.10425 0.12705 0.02350  -0.00040 -0.00880 165 PHE A CE1 
1483 C  CE2 . PHE A 162 ? 0.10075 0.10025 0.13505 0.02470  -0.00370 0.00180  165 PHE A CE2 
1484 C  CZ  . PHE A 162 ? 0.10165 0.09715 0.11915 0.02690  -0.01040 -0.01730 165 PHE A CZ  
1485 N  N   . LYS A 163 ? 0.11405 0.11375 0.15305 -0.00350 0.01080  -0.02640 166 LYS A N   
1486 C  CA  . LYS A 163 ? 0.10995 0.12205 0.13175 0.00760  0.00750  -0.00430 166 LYS A CA  
1487 C  C   . LYS A 163 ? 0.09875 0.14835 0.14385 0.04730  0.02270  0.03470  166 LYS A C   
1488 O  O   . LYS A 163 ? 0.11645 0.25245 0.17795 0.06730  0.04900  0.06780  166 LYS A O   
1489 C  CB  . LYS A 163 ? 0.11395 0.12395 0.12165 -0.01290 0.01220  0.00140  166 LYS A CB  
1490 C  CG  . LYS A 163 ? 0.10805 0.15695 0.14205 -0.00330 0.02070  0.03530  166 LYS A CG  
1491 C  CD  . LYS A 163 ? 0.12885 0.17365 0.17045 -0.00760 0.01960  0.04220  166 LYS A CD  
1492 C  CE  . LYS A 163 ? 0.12055 0.19435 0.17225 -0.02230 0.03260  0.03960  166 LYS A CE  
1493 N  NZ  . LYS A 163 ? 0.13595 0.19335 0.16375 -0.01950 0.03570  0.03780  166 LYS A NZ  
1494 N  N   . ILE A 164 ? 0.08455 0.10335 0.11355 -0.00240 0.00530  0.00320  167 ILE A N   
1495 C  CA  . ILE A 164 ? 0.08085 0.09735 0.10175 -0.01880 -0.00120 0.00180  167 ILE A CA  
1496 C  C   . ILE A 164 ? 0.06605 0.10335 0.10275 -0.00640 -0.00180 0.00490  167 ILE A C   
1497 O  O   . ILE A 164 ? 0.08935 0.09315 0.13215 0.00080  -0.00310 0.00250  167 ILE A O   
1498 C  CB  . ILE A 164 ? 0.08505 0.10665 0.11565 -0.00740 0.00290  -0.00620 167 ILE A CB  
1499 C  CG1 . ILE A 164 ? 0.09375 0.07895 0.13045 0.00170  -0.02240 -0.01010 167 ILE A CG1 
1500 C  CG2 . ILE A 164 ? 0.11755 0.11615 0.10995 -0.00280 0.01860  -0.01080 167 ILE A CG2 
1501 C  CD1 . ILE A 164 ? 0.09085 0.07805 0.12735 0.01170  -0.00750 0.00470  167 ILE A CD1 
1502 N  N   . ARG A 165 ? 0.08325 0.11855 0.11375 -0.01450 -0.00350 -0.01680 168 ARG A N   
1503 C  CA  A ARG A 165 ? 0.10775 0.14685 0.12245 -0.03360 -0.00570 -0.02880 168 ARG A CA  
1505 C  C   . ARG A 165 ? 0.10705 0.11695 0.11835 -0.01440 -0.00470 -0.01070 168 ARG A C   
1506 O  O   . ARG A 165 ? 0.14485 0.12605 0.12295 0.02670  0.01000  0.00830  168 ARG A O   
1507 C  CB  A ARG A 165 ? 0.13045 0.20215 0.13705 -0.08560 -0.00090 -0.01170 168 ARG A CB  
1509 C  CG  A ARG A 165 ? 0.17445 0.22345 0.18115 -0.11530 -0.00870 -0.00210 168 ARG A CG  
1517 N  NH1 A ARG A 165 ? 0.28615 0.31205 0.31925 -0.01070 0.05900  -0.06330 168 ARG A NH1 
1519 N  NH2 A ARG A 165 ? 0.29035 0.30075 0.28955 0.00360  -0.15710 -0.07340 168 ARG A NH2 
1521 N  N   . HIS A 166 ? 0.09045 0.08895 0.11295 -0.02540 -0.00880 -0.00400 169 HIS A N   
1522 C  CA  . HIS A 166 ? 0.08805 0.09105 0.10885 -0.01940 -0.01410 -0.00680 169 HIS A CA  
1523 C  C   . HIS A 166 ? 0.09625 0.09605 0.10745 -0.02060 -0.00980 0.01910  169 HIS A C   
1524 O  O   . HIS A 166 ? 0.14325 0.09965 0.12695 -0.02300 -0.02020 0.01460  169 HIS A O   
1525 C  CB  . HIS A 166 ? 0.08355 0.08835 0.13185 -0.00540 -0.02110 -0.00680 169 HIS A CB  
1526 C  CG  . HIS A 166 ? 0.07805 0.08945 0.12285 -0.01770 -0.00210 -0.00910 169 HIS A CG  
1527 N  ND1 . HIS A 166 ? 0.07985 0.07925 0.12085 -0.01460 -0.00840 -0.01000 169 HIS A ND1 
1528 C  CD2 . HIS A 166 ? 0.08825 0.10405 0.11095 -0.02460 0.00010  -0.01620 169 HIS A CD2 
1529 C  CE1 . HIS A 166 ? 0.07875 0.08365 0.11095 -0.00740 -0.00140 -0.00050 169 HIS A CE1 
1530 N  NE2 . HIS A 166 ? 0.07295 0.09535 0.10185 -0.02800 -0.00340 -0.00970 169 HIS A NE2 
1531 N  N   . ASN A 167 ? 0.09645 0.09365 0.11055 -0.02240 -0.02990 -0.00450 170 ASN A N   
1532 C  CA  A ASN A 167 ? 0.10055 0.09835 0.11945 -0.01960 -0.04030 0.01480  170 ASN A CA  
1534 C  C   . ASN A 167 ? 0.10325 0.10405 0.12085 -0.02170 -0.01340 0.01500  170 ASN A C   
1535 O  O   . ASN A 167 ? 0.11365 0.09975 0.12515 -0.02010 -0.00310 0.00430  170 ASN A O   
1536 C  CB  A ASN A 167 ? 0.10335 0.11965 0.12685 -0.00300 -0.03830 0.02030  170 ASN A CB  
1538 C  CG  A ASN A 167 ? 0.12035 0.11805 0.15205 0.00800  -0.02350 0.00940  170 ASN A CG  
1540 O  OD1 A ASN A 167 ? 0.06955 0.13425 0.16675 0.00680  -0.02020 0.00290  170 ASN A OD1 
1542 N  ND2 A ASN A 167 ? 0.16555 0.13415 0.16455 0.01340  -0.02260 0.03130  170 ASN A ND2 
1544 N  N   . ILE A 168 ? 0.10365 0.09465 0.10995 -0.01470 -0.01300 -0.00290 171 ILE A N   
1545 C  CA  . ILE A 168 ? 0.10375 0.11405 0.11255 -0.01260 -0.01810 0.00790  171 ILE A CA  
1546 C  C   . ILE A 168 ? 0.11425 0.11855 0.10365 -0.01420 -0.01510 -0.00020 171 ILE A C   
1547 O  O   . ILE A 168 ? 0.10935 0.11675 0.10545 -0.01520 -0.01960 -0.01190 171 ILE A O   
1548 C  CB  . ILE A 168 ? 0.12925 0.11425 0.12235 -0.00600 -0.02660 -0.00270 171 ILE A CB  
1549 C  CG1 . ILE A 168 ? 0.10555 0.10155 0.12735 -0.01180 -0.02320 -0.00070 171 ILE A CG1 
1550 C  CG2 . ILE A 168 ? 0.11245 0.11995 0.13785 0.00050  -0.02520 0.00830  171 ILE A CG2 
1551 C  CD1 . ILE A 168 ? 0.11425 0.09205 0.12895 -0.03070 -0.00180 0.00620  171 ILE A CD1 
1552 N  N   . GLU A 169 ? 0.13765 0.11805 0.10455 -0.03040 0.00450  -0.01040 172 GLU A N   
1553 C  CA  A GLU A 169 ? 0.15325 0.15035 0.11095 -0.04360 0.00920  -0.03370 172 GLU A CA  
1555 C  C   . GLU A 169 ? 0.14775 0.14845 0.11995 -0.02250 0.00200  -0.03350 172 GLU A C   
1556 O  O   . GLU A 169 ? 0.18215 0.15725 0.14145 -0.02030 -0.02480 -0.01650 172 GLU A O   
1557 C  CB  A GLU A 169 ? 0.15695 0.19755 0.12305 -0.04900 0.02960  -0.03380 172 GLU A CB  
1559 C  CG  A GLU A 169 ? 0.16185 0.23395 0.14905 -0.03650 0.02500  -0.04940 172 GLU A CG  
1561 C  CD  A GLU A 169 ? 0.18935 0.28375 0.17595 -0.01310 0.00830  -0.05760 172 GLU A CD  
1563 O  OE1 A GLU A 169 ? 0.17715 0.31955 0.17225 -0.00990 0.00870  -0.05310 172 GLU A OE1 
1565 O  OE2 A GLU A 169 ? 0.20415 0.29665 0.19555 0.01580  0.00170  -0.06900 172 GLU A OE2 
1567 N  N   . ASP A 170 ? 0.12645 0.13605 0.12485 -0.02230 -0.00480 -0.02240 173 ASP A N   
1568 C  CA  . ASP A 170 ? 0.12955 0.13795 0.12595 -0.02330 0.01520  -0.01260 173 ASP A CA  
1569 C  C   . ASP A 170 ? 0.10755 0.14435 0.14435 -0.01590 -0.00550 -0.00550 173 ASP A C   
1570 O  O   . ASP A 170 ? 0.12315 0.15775 0.16535 -0.03560 -0.00850 -0.00950 173 ASP A O   
1571 C  CB  . ASP A 170 ? 0.13905 0.13385 0.14635 -0.02840 0.00280  -0.00480 173 ASP A CB  
1572 C  CG  . ASP A 170 ? 0.11625 0.12515 0.14885 -0.02530 -0.00060 0.00410  173 ASP A CG  
1573 O  OD1 . ASP A 170 ? 0.11915 0.12295 0.13875 0.00240  -0.00180 -0.01310 173 ASP A OD1 
1574 O  OD2 . ASP A 170 ? 0.13165 0.13705 0.15785 -0.03410 0.01370  0.01280  173 ASP A OD2 
1575 N  N   . GLY A 171 ? 0.11725 0.13965 0.12745 -0.00550 -0.01550 -0.01030 174 GLY A N   
1576 C  CA  . GLY A 171 ? 0.11735 0.15795 0.11035 -0.00570 -0.00900 -0.01550 174 GLY A CA  
1577 C  C   . GLY A 171 ? 0.10775 0.13475 0.10955 -0.02310 -0.01380 0.00510  174 GLY A C   
1578 O  O   . GLY A 171 ? 0.09915 0.14635 0.12515 -0.02710 -0.00610 0.01100  174 GLY A O   
1579 N  N   . SER A 172 ? 0.11525 0.10195 0.11135 -0.03290 -0.02730 0.00360  175 SER A N   
1580 C  CA  . SER A 172 ? 0.11875 0.09045 0.10375 -0.01390 -0.02020 0.00080  175 SER A CA  
1581 C  C   . SER A 172 ? 0.08705 0.09495 0.10535 -0.00150 -0.01230 0.00250  175 SER A C   
1582 O  O   . SER A 172 ? 0.09765 0.10595 0.12315 -0.01720 -0.02090 0.00100  175 SER A O   
1583 C  CB  . SER A 172 ? 0.11485 0.09175 0.12015 -0.02420 -0.00390 0.02650  175 SER A CB  
1584 O  OG  . SER A 172 ? 0.10605 0.10985 0.12425 -0.03220 -0.00930 0.02390  175 SER A OG  
1585 N  N   . VAL A 173 ? 0.08805 0.10105 0.10485 -0.02030 -0.00560 -0.01750 176 VAL A N   
1586 C  CA  A VAL A 173 ? 0.13915 0.15325 0.13735 -0.02890 -0.02430 -0.02570 176 VAL A CA  
1588 C  C   . VAL A 173 ? 0.10205 0.10535 0.10385 -0.03400 -0.01120 -0.00060 176 VAL A C   
1589 O  O   . VAL A 173 ? 0.10615 0.12155 0.11835 -0.04410 0.00520  -0.01040 176 VAL A O   
1590 C  CB  A VAL A 173 ? 0.21665 0.22335 0.21515 -0.02300 -0.00330 -0.04030 176 VAL A CB  
1592 C  CG1 A VAL A 173 ? 0.16335 0.17695 0.18005 -0.00760 0.05940  -0.05740 176 VAL A CG1 
1596 N  N   . GLN A 174 ? 0.08305 0.10725 0.10325 -0.01800 -0.00190 0.00370  177 GLN A N   
1597 C  CA  . GLN A 174 ? 0.07435 0.10305 0.10505 0.00460  -0.01200 -0.01400 177 GLN A CA  
1598 C  C   . GLN A 174 ? 0.08445 0.08545 0.09365 -0.00270 -0.01320 0.00090  177 GLN A C   
1599 O  O   . GLN A 174 ? 0.09585 0.08385 0.09555 -0.01060 -0.00510 -0.00230 177 GLN A O   
1600 C  CB  . GLN A 174 ? 0.06685 0.12225 0.12645 -0.01030 0.00010  -0.01900 177 GLN A CB  
1601 C  CG  . GLN A 174 ? 0.09215 0.11085 0.13555 -0.00500 -0.02310 -0.01900 177 GLN A CG  
1602 C  CD  . GLN A 174 ? 0.09095 0.11215 0.13735 0.01460  -0.02400 -0.02380 177 GLN A CD  
1603 O  OE1 . GLN A 174 ? 0.12575 0.12835 0.14575 0.02020  -0.02730 -0.03870 177 GLN A OE1 
1604 N  NE2 . GLN A 174 ? 0.07295 0.10975 0.12535 -0.00600 -0.01710 -0.02380 177 GLN A NE2 
1605 N  N   . LEU A 175 ? 0.07145 0.08785 0.08575 -0.00460 -0.00830 -0.00830 178 LEU A N   
1606 C  CA  . LEU A 175 ? 0.08985 0.08855 0.09255 -0.01890 -0.00220 0.00740  178 LEU A CA  
1607 C  C   . LEU A 175 ? 0.07115 0.08735 0.09945 -0.01500 -0.00600 0.00170  178 LEU A C   
1608 O  O   . LEU A 175 ? 0.07785 0.10535 0.10145 -0.00800 0.00130  0.00760  178 LEU A O   
1609 C  CB  . LEU A 175 ? 0.12075 0.10375 0.09005 -0.01360 0.00710  0.02040  178 LEU A CB  
1610 C  CG  . LEU A 175 ? 0.14585 0.12515 0.11785 -0.00280 0.00910  0.01050  178 LEU A CG  
1611 C  CD1 . LEU A 175 ? 0.13835 0.13905 0.14375 0.01990  0.01790  0.00110  178 LEU A CD1 
1612 C  CD2 . LEU A 175 ? 0.14685 0.12805 0.13265 -0.03300 0.01090  0.01420  178 LEU A CD2 
1613 N  N   . ALA A 176 ? 0.06355 0.09135 0.11045 -0.00610 -0.00400 -0.00410 179 ALA A N   
1614 C  CA  . ALA A 176 ? 0.07935 0.09165 0.09755 -0.00930 -0.00090 -0.00900 179 ALA A CA  
1615 C  C   . ALA A 176 ? 0.06565 0.10025 0.09085 0.00150  0.00150  0.00070  179 ALA A C   
1616 O  O   . ALA A 176 ? 0.06955 0.08575 0.09475 0.00520  -0.00310 -0.00640 179 ALA A O   
1617 C  CB  . ALA A 176 ? 0.07905 0.11105 0.09655 -0.02690 -0.00280 -0.01160 179 ALA A CB  
1618 N  N   . ASP A 177 ? 0.07285 0.10605 0.09385 -0.00210 -0.00880 0.00590  180 ASP A N   
1619 C  CA  . ASP A 177 ? 0.09315 0.09385 0.09885 0.00710  0.00100  0.01080  180 ASP A CA  
1620 C  C   . ASP A 177 ? 0.08955 0.09005 0.09985 0.01610  0.00690  0.00260  180 ASP A C   
1621 O  O   . ASP A 177 ? 0.08415 0.09655 0.12125 0.00320  0.00100  -0.01220 180 ASP A O   
1622 C  CB  . ASP A 177 ? 0.10355 0.10055 0.10525 0.00410  0.01950  0.01450  180 ASP A CB  
1623 C  CG  . ASP A 177 ? 0.11415 0.12095 0.12055 0.00520  0.01420  0.00380  180 ASP A CG  
1624 O  OD1 . ASP A 177 ? 0.11145 0.12845 0.13975 -0.00830 0.01560  0.00840  180 ASP A OD1 
1625 O  OD2 . ASP A 177 ? 0.12615 0.13225 0.13275 -0.01230 0.02730  0.00200  180 ASP A OD2 
1626 N  N   . HIS A 178 ? 0.10335 0.07835 0.08495 -0.00220 0.00030  0.01320  181 HIS A N   
1627 C  CA  . HIS A 178 ? 0.09155 0.08035 0.08245 0.01000  0.00400  -0.00120 181 HIS A CA  
1628 C  C   . HIS A 178 ? 0.08365 0.09195 0.09115 0.00430  0.00590  -0.00240 181 HIS A C   
1629 O  O   . HIS A 178 ? 0.09155 0.12325 0.09845 0.01140  0.00730  -0.00550 181 HIS A O   
1630 C  CB  . HIS A 178 ? 0.09145 0.09405 0.07295 0.02480  0.00210  0.00640  181 HIS A CB  
1631 C  CG  . HIS A 178 ? 0.07865 0.09855 0.08085 0.01510  0.01060  -0.00630 181 HIS A CG  
1632 N  ND1 . HIS A 178 ? 0.06945 0.09325 0.06895 0.00710  0.00430  0.00190  181 HIS A ND1 
1633 C  CD2 . HIS A 178 ? 0.07745 0.09235 0.07585 0.01780  0.01100  0.01210  181 HIS A CD2 
1634 C  CE1 . HIS A 178 ? 0.07375 0.07655 0.08725 -0.01220 -0.00340 -0.00210 181 HIS A CE1 
1635 N  NE2 . HIS A 178 ? 0.07685 0.09165 0.08085 0.01060  0.00510  0.00960  181 HIS A NE2 
1636 N  N   . TYR A 179 ? 0.09755 0.08525 0.07455 0.00560  0.01010  -0.00020 182 TYR A N   
1637 C  CA  A TYR A 179 ? 0.13025 0.09955 0.07485 -0.00090 0.00480  0.01290  182 TYR A CA  
1639 C  C   . TYR A 179 ? 0.10935 0.09805 0.07275 0.00920  -0.00600 -0.00030 182 TYR A C   
1640 O  O   . TYR A 179 ? 0.09695 0.10185 0.11115 0.00380  0.01050  -0.02610 182 TYR A O   
1641 C  CB  A TYR A 179 ? 0.18435 0.11485 0.09485 0.00840  -0.01250 0.01730  182 TYR A CB  
1643 C  CG  A TYR A 179 ? 0.19345 0.14685 0.13125 0.00590  -0.01250 0.00070  182 TYR A CG  
1645 C  CD1 A TYR A 179 ? 0.22785 0.18605 0.11455 0.00670  -0.00020 -0.00530 182 TYR A CD1 
1647 C  CD2 A TYR A 179 ? 0.23305 0.21375 0.19475 0.00810  -0.03100 -0.01540 182 TYR A CD2 
1649 C  CE1 A TYR A 179 ? 0.24685 0.21505 0.13545 -0.01430 0.00450  -0.01770 182 TYR A CE1 
1653 C  CZ  A TYR A 179 ? 0.28065 0.22535 0.16885 -0.03540 -0.01540 -0.02430 182 TYR A CZ  
1655 O  OH  A TYR A 179 ? 0.32955 0.20795 0.13085 -0.05100 -0.02430 -0.01630 182 TYR A OH  
1657 N  N   . GLN A 180 ? 0.09465 0.09365 0.08895 0.00840  -0.00030 0.00340  183 GLN A N   
1658 C  CA  . GLN A 180 ? 0.10865 0.08755 0.08575 -0.00150 -0.00110 0.00910  183 GLN A CA  
1659 C  C   . GLN A 180 ? 0.09445 0.08215 0.08405 -0.00230 0.00400  0.00400  183 GLN A C   
1660 O  O   . GLN A 180 ? 0.11035 0.09665 0.09335 0.01530  -0.00460 0.00700  183 GLN A O   
1661 C  CB  . GLN A 180 ? 0.09535 0.09515 0.08865 0.01030  -0.00030 0.02930  183 GLN A CB  
1662 C  CG  . GLN A 180 ? 0.11305 0.09415 0.07715 0.02920  -0.00460 0.01690  183 GLN A CG  
1663 C  CD  . GLN A 180 ? 0.10795 0.08975 0.08315 0.02000  -0.00440 -0.00910 183 GLN A CD  
1664 O  OE1 . GLN A 180 ? 0.08555 0.09055 0.07475 -0.00450 0.01410  0.00240  183 GLN A OE1 
1665 N  NE2 . GLN A 180 ? 0.10505 0.07915 0.07815 0.01560  0.00490  0.00770  183 GLN A NE2 
1666 N  N   . GLN A 181 ? 0.10745 0.07945 0.08565 -0.00900 0.00300  -0.01050 184 GLN A N   
1667 C  CA  A GLN A 181 ? 0.13605 0.12085 0.10315 -0.00520 -0.02040 -0.00150 184 GLN A CA  
1669 C  C   . GLN A 181 ? 0.12345 0.11685 0.09315 -0.00260 -0.01010 -0.02720 184 GLN A C   
1670 O  O   . GLN A 181 ? 0.12335 0.13095 0.11355 -0.00310 0.03450  -0.01680 184 GLN A O   
1671 C  CB  A GLN A 181 ? 0.15945 0.17025 0.13865 -0.00030 -0.04270 0.04330  184 GLN A CB  
1673 C  CG  A GLN A 181 ? 0.19455 0.21115 0.19505 0.01480  -0.04970 0.08290  184 GLN A CG  
1681 N  N   . ASN A 182 ? 0.12675 0.11665 0.08495 0.00000  -0.00710 -0.01310 185 ASN A N   
1682 C  CA  . ASN A 182 ? 0.10955 0.11145 0.08195 -0.01050 -0.00410 -0.01770 185 ASN A CA  
1683 C  C   . ASN A 182 ? 0.12815 0.12205 0.07275 0.00280  -0.01460 -0.01420 185 ASN A C   
1684 O  O   . ASN A 182 ? 0.13725 0.13555 0.08085 0.01620  -0.01420 -0.01440 185 ASN A O   
1685 C  CB  . ASN A 182 ? 0.11455 0.10465 0.08365 -0.01020 -0.02230 0.00120  185 ASN A CB  
1686 C  CG  . ASN A 182 ? 0.11355 0.10325 0.08925 -0.00470 -0.01300 -0.00670 185 ASN A CG  
1687 O  OD1 . ASN A 182 ? 0.21585 0.12515 0.09345 -0.05300 -0.03650 0.01870  185 ASN A OD1 
1688 N  ND2 . ASN A 182 ? 0.11615 0.10105 0.07695 0.00930  0.02000  0.00050  185 ASN A ND2 
1689 N  N   . THR A 183 ? 0.11975 0.11895 0.10005 -0.00410 -0.03130 -0.01190 186 THR A N   
1690 C  CA  A THR A 183 ? 0.17385 0.12445 0.08015 -0.00520 -0.04290 -0.00680 186 THR A CA  
1692 C  C   . THR A 183 ? 0.16065 0.13635 0.09495 -0.00840 -0.02640 -0.01330 186 THR A C   
1693 O  O   . THR A 183 ? 0.17805 0.13855 0.10485 -0.01440 -0.01350 -0.02360 186 THR A O   
1694 C  CB  A THR A 183 ? 0.18545 0.11725 0.09585 -0.01080 -0.05350 0.00520  186 THR A CB  
1696 O  OG1 A THR A 183 ? 0.17405 0.12895 0.12645 -0.00050 -0.03480 -0.00360 186 THR A OG1 
1698 C  CG2 A THR A 183 ? 0.20705 0.13005 0.10265 -0.00990 -0.05280 -0.00930 186 THR A CG2 
1700 N  N   . PRO A 184 ? 0.13475 0.13885 0.08495 0.01030  -0.00660 -0.00850 187 PRO A N   
1701 C  CA  . PRO A 184 ? 0.13405 0.13615 0.09335 0.00370  0.00250  -0.00430 187 PRO A CA  
1702 C  C   . PRO A 184 ? 0.13425 0.13385 0.10475 -0.02120 -0.01830 -0.01610 187 PRO A C   
1703 O  O   . PRO A 184 ? 0.13675 0.16505 0.11555 -0.01380 -0.03830 0.00070  187 PRO A O   
1704 C  CB  . PRO A 184 ? 0.17005 0.14435 0.10495 0.02320  0.01450  -0.01210 187 PRO A CB  
1705 C  CG  . PRO A 184 ? 0.19375 0.15785 0.11445 0.01060  0.00910  -0.01730 187 PRO A CG  
1706 C  CD  . PRO A 184 ? 0.16145 0.15295 0.10015 0.00690  0.00580  -0.02360 187 PRO A CD  
1707 N  N   . ILE A 185 ? 0.11615 0.13905 0.11825 -0.01830 -0.00680 0.00260  188 ILE A N   
1708 C  CA  . ILE A 185 ? 0.12565 0.15145 0.11905 -0.00620 -0.00940 -0.00870 188 ILE A CA  
1709 C  C   . ILE A 185 ? 0.14505 0.14785 0.11275 -0.00770 -0.02920 -0.00920 188 ILE A C   
1710 O  O   . ILE A 185 ? 0.17385 0.17115 0.12755 -0.02820 -0.03260 -0.00890 188 ILE A O   
1711 C  CB  . ILE A 185 ? 0.12015 0.15395 0.11525 -0.00170 -0.00820 -0.02430 188 ILE A CB  
1712 C  CG1 . ILE A 185 ? 0.11825 0.15475 0.11895 0.00470  -0.01350 -0.03060 188 ILE A CG1 
1713 C  CG2 . ILE A 185 ? 0.13165 0.16345 0.13375 -0.00360 -0.03170 -0.00610 188 ILE A CG2 
1714 C  CD1 . ILE A 185 ? 0.10575 0.14575 0.12965 0.01410  -0.00300 -0.01990 188 ILE A CD1 
1715 N  N   . GLY A 186 ? 0.15025 0.14635 0.12245 -0.01410 -0.02310 -0.02600 189 GLY A N   
1716 C  CA  . GLY A 186 ? 0.16285 0.15705 0.12085 -0.02690 -0.00010 -0.04320 189 GLY A CA  
1717 C  C   . GLY A 186 ? 0.14485 0.14525 0.12205 -0.00220 -0.00750 -0.01530 189 GLY A C   
1718 O  O   . GLY A 186 ? 0.16565 0.15715 0.11535 0.02040  -0.01540 -0.00870 189 GLY A O   
1719 N  N   A ASP A 187 ? 0.18625 0.17805 0.11055 0.03010  -0.00580 -0.04540 190 ASP A N   
1721 C  CA  A ASP A 187 ? 0.19215 0.22235 0.13935 0.03950  -0.01580 -0.06250 190 ASP A CA  
1723 C  C   A ASP A 187 ? 0.19105 0.20855 0.14205 0.03380  -0.00130 -0.04670 190 ASP A C   
1725 O  O   A ASP A 187 ? 0.21915 0.23695 0.13205 0.02890  0.01500  -0.05010 190 ASP A O   
1727 C  CB  A ASP A 187 ? 0.22115 0.25355 0.18775 0.03370  -0.06360 -0.08940 190 ASP A CB  
1729 C  CG  A ASP A 187 ? 0.25165 0.26205 0.24645 0.02210  -0.06330 -0.06330 190 ASP A CG  
1735 N  N   . GLY A 188 ? 0.15185 0.16315 0.15025 0.02270  0.00190  -0.03290 191 GLY A N   
1736 C  CA  . GLY A 188 ? 0.13295 0.17605 0.17885 0.01420  -0.01320 -0.05110 191 GLY A CA  
1737 C  C   . GLY A 188 ? 0.12835 0.18315 0.18275 0.01480  -0.02230 -0.06610 191 GLY A C   
1738 O  O   . GLY A 188 ? 0.14525 0.16855 0.21185 -0.00070 -0.03730 -0.02400 191 GLY A O   
1739 N  N   . PRO A 189 ? 0.13525 0.20785 0.19185 -0.00620 -0.00600 -0.09750 192 PRO A N   
1740 C  CA  . PRO A 189 ? 0.14745 0.22275 0.15615 -0.01420 -0.00210 -0.09010 192 PRO A CA  
1741 C  C   . PRO A 189 ? 0.16635 0.19285 0.12065 -0.00050 -0.02100 -0.05470 192 PRO A C   
1742 O  O   . PRO A 189 ? 0.21535 0.19335 0.13265 0.00840  -0.03500 -0.01720 192 PRO A O   
1743 C  CB  . PRO A 189 ? 0.15465 0.25605 0.19645 0.00350  0.02150  -0.10160 192 PRO A CB  
1744 C  CG  . PRO A 189 ? 0.14955 0.23875 0.22255 0.01510  0.01080  -0.10810 192 PRO A CG  
1745 C  CD  . PRO A 189 ? 0.14415 0.21535 0.21995 0.00890  0.00220  -0.10540 192 PRO A CD  
1746 N  N   . VAL A 190 ? 0.15045 0.18785 0.11805 0.00170  -0.01820 -0.02070 193 VAL A N   
1747 C  CA  . VAL A 190 ? 0.15035 0.16395 0.12845 0.00100  0.00690  -0.01740 193 VAL A CA  
1748 C  C   . VAL A 190 ? 0.14695 0.15835 0.11925 -0.00760 0.01980  -0.00550 193 VAL A C   
1749 O  O   . VAL A 190 ? 0.18375 0.18305 0.12195 -0.03290 -0.01300 -0.00340 193 VAL A O   
1750 C  CB  . VAL A 190 ? 0.17915 0.16655 0.16355 0.01960  0.01040  -0.01190 193 VAL A CB  
1751 C  CG1 . VAL A 190 ? 0.17135 0.16805 0.17835 0.01020  0.00970  -0.02850 193 VAL A CG1 
1752 C  CG2 . VAL A 190 ? 0.18895 0.19535 0.18185 0.03980  0.01000  0.01660  193 VAL A CG2 
1753 N  N   . LEU A 191 ? 0.11505 0.15315 0.12965 0.00050  0.00880  -0.00580 194 LEU A N   
1754 C  CA  . LEU A 191 ? 0.12865 0.13395 0.13425 0.00580  0.01410  -0.00400 194 LEU A CA  
1755 C  C   . LEU A 191 ? 0.13535 0.13245 0.13405 0.00800  0.01870  -0.02830 194 LEU A C   
1756 O  O   . LEU A 191 ? 0.17595 0.13715 0.14305 0.01620  0.04360  -0.02700 194 LEU A O   
1757 C  CB  . LEU A 191 ? 0.12815 0.14115 0.12135 0.01270  0.00690  -0.03530 194 LEU A CB  
1758 C  CG  . LEU A 191 ? 0.14135 0.14205 0.12285 0.01060  -0.01010 -0.03180 194 LEU A CG  
1759 C  CD1 . LEU A 191 ? 0.15065 0.16295 0.12835 0.01810  -0.00120 -0.01790 194 LEU A CD1 
1760 C  CD2 . LEU A 191 ? 0.17875 0.14215 0.13285 0.00640  -0.00150 -0.04330 194 LEU A CD2 
1761 N  N   . LEU A 192 ? 0.15755 0.13985 0.12145 -0.01550 0.00410  0.00020  195 LEU A N   
1762 C  CA  . LEU A 192 ? 0.17845 0.15555 0.13665 -0.00910 0.00110  -0.00100 195 LEU A CA  
1763 C  C   . LEU A 192 ? 0.17445 0.15885 0.13805 -0.00920 0.01120  -0.00730 195 LEU A C   
1764 O  O   . LEU A 192 ? 0.19475 0.18975 0.16975 0.00450  0.02620  -0.03940 195 LEU A O   
1765 C  CB  . LEU A 192 ? 0.21445 0.18565 0.16125 -0.00890 0.00620  0.01020  195 LEU A CB  
1766 C  CG  . LEU A 192 ? 0.24355 0.21665 0.17525 0.02480  -0.00890 0.00320  195 LEU A CG  
1767 C  CD1 . LEU A 192 ? 0.24755 0.24245 0.17445 0.02120  -0.01210 0.00410  195 LEU A CD1 
1768 C  CD2 . LEU A 192 ? 0.22925 0.21335 0.20245 0.03860  -0.03280 -0.00430 195 LEU A CD2 
1769 N  N   . PRO A 193 ? 0.15175 0.13865 0.11155 0.00010  0.01120  0.00370  196 PRO A N   
1770 C  CA  . PRO A 193 ? 0.13975 0.14895 0.11415 0.01070  0.02060  -0.00100 196 PRO A CA  
1771 C  C   . PRO A 193 ? 0.12565 0.12295 0.11815 0.00610  0.03110  -0.00910 196 PRO A C   
1772 O  O   . PRO A 193 ? 0.16135 0.12415 0.12855 -0.00050 0.01800  -0.00370 196 PRO A O   
1773 C  CB  . PRO A 193 ? 0.12175 0.16095 0.11255 0.02920  0.02070  -0.00320 196 PRO A CB  
1774 C  CG  . PRO A 193 ? 0.13165 0.16265 0.12025 0.02660  -0.00350 0.00200  196 PRO A CG  
1775 C  CD  . PRO A 193 ? 0.13855 0.14955 0.11455 0.02970  0.00500  -0.00050 196 PRO A CD  
1776 N  N   . ASP A 194 ? 0.13815 0.13515 0.10885 0.01100  0.02050  -0.00720 197 ASP A N   
1777 C  CA  . ASP A 194 ? 0.15235 0.14295 0.11545 0.02210  0.02600  -0.01630 197 ASP A CA  
1778 C  C   . ASP A 194 ? 0.15525 0.13005 0.09425 0.02150  0.02730  -0.00450 197 ASP A C   
1779 O  O   . ASP A 194 ? 0.14285 0.14575 0.10275 0.00560  0.04170  -0.00340 197 ASP A O   
1780 C  CB  . ASP A 194 ? 0.14585 0.16185 0.13295 0.04450  0.04100  -0.01760 197 ASP A CB  
1781 C  CG  . ASP A 194 ? 0.20855 0.21885 0.15885 0.05610  0.05420  -0.02100 197 ASP A CG  
1782 O  OD1 . ASP A 194 ? 0.25185 0.28345 0.15335 0.07160  0.05690  -0.03530 197 ASP A OD1 
1783 O  OD2 . ASP A 194 ? 0.23635 0.21705 0.15945 0.07410  0.07340  -0.03000 197 ASP A OD2 
1784 N  N   . ASN A 195 ? 0.15725 0.10235 0.10635 0.02040  0.03790  -0.00240 198 ASN A N   
1785 C  CA  . ASN A 195 ? 0.15165 0.11675 0.12175 0.00900  0.03540  0.00590  198 ASN A CA  
1786 C  C   . ASN A 195 ? 0.13485 0.12435 0.11505 0.01990  0.04180  -0.00240 198 ASN A C   
1787 O  O   . ASN A 195 ? 0.15075 0.13825 0.13415 0.02940  0.03860  0.00340  198 ASN A O   
1788 C  CB  . ASN A 195 ? 0.16565 0.13285 0.13895 -0.00570 0.03580  0.01300  198 ASN A CB  
1789 C  CG  . ASN A 195 ? 0.19825 0.14335 0.16225 -0.00140 0.02820  0.00850  198 ASN A CG  
1790 O  OD1 . ASN A 195 ? 0.20745 0.13825 0.16695 0.01630  0.01340  0.01600  198 ASN A OD1 
1791 N  ND2 . ASN A 195 ? 0.24875 0.20185 0.20325 -0.03660 0.00130  0.04540  198 ASN A ND2 
1792 N  N   . HIS A 196 ? 0.12845 0.12855 0.10175 -0.00720 0.03560  0.00350  199 HIS A N   
1793 C  CA  . HIS A 196 ? 0.12445 0.11705 0.09245 -0.00460 0.03320  0.00840  199 HIS A CA  
1794 C  C   . HIS A 196 ? 0.10715 0.10805 0.10305 -0.00320 0.01560  0.00200  199 HIS A C   
1795 O  O   . HIS A 196 ? 0.13835 0.10835 0.11855 0.01340  0.02440  0.01580  199 HIS A O   
1796 C  CB  . HIS A 196 ? 0.12625 0.11625 0.09855 -0.00030 0.02590  0.00900  199 HIS A CB  
1797 C  CG  . HIS A 196 ? 0.11715 0.11015 0.11015 0.00130  0.02750  -0.00210 199 HIS A CG  
1798 N  ND1 . HIS A 196 ? 0.11235 0.10915 0.10485 0.00220  0.02530  -0.00610 199 HIS A ND1 
1799 C  CD2 . HIS A 196 ? 0.08715 0.10875 0.12005 0.00960  0.03960  0.01750  199 HIS A CD2 
1800 C  CE1 . HIS A 196 ? 0.09385 0.11345 0.09385 0.01100  0.02550  0.00230  199 HIS A CE1 
1801 N  NE2 . HIS A 196 ? 0.08695 0.11085 0.10745 0.01560  0.03120  0.00170  199 HIS A NE2 
1802 N  N   . TYR A 197 ? 0.11455 0.12515 0.11085 0.01140  0.02300  0.00730  200 TYR A N   
1803 C  CA  . TYR A 197 ? 0.12305 0.12675 0.11725 0.00020  0.02500  -0.00040 200 TYR A CA  
1804 C  C   . TYR A 197 ? 0.11565 0.10605 0.11475 0.00290  0.01900  -0.00210 200 TYR A C   
1805 O  O   . TYR A 197 ? 0.11025 0.11605 0.12355 0.00590  0.01590  0.00330  200 TYR A O   
1806 C  CB  . TYR A 197 ? 0.12055 0.13025 0.13495 -0.00930 0.03420  0.00070  200 TYR A CB  
1807 C  CG  . TYR A 197 ? 0.12165 0.14065 0.14745 -0.00180 0.03730  -0.00430 200 TYR A CG  
1808 C  CD1 . TYR A 197 ? 0.11125 0.16925 0.17455 -0.02900 0.04400  -0.02220 200 TYR A CD1 
1809 C  CD2 . TYR A 197 ? 0.13015 0.14575 0.15635 -0.00170 0.00520  0.01900  200 TYR A CD2 
1810 C  CE1 . TYR A 197 ? 0.11315 0.19375 0.20135 -0.01820 0.02520  -0.02270 200 TYR A CE1 
1811 C  CE2 . TYR A 197 ? 0.11415 0.16865 0.18765 -0.00880 0.01870  0.02130  200 TYR A CE2 
1812 C  CZ  . TYR A 197 ? 0.10455 0.20065 0.21475 0.00070  0.00730  -0.01050 200 TYR A CZ  
1813 O  OH  . TYR A 197 ? 0.12675 0.23185 0.24515 0.01020  -0.02430 -0.01740 200 TYR A OH  
1814 N  N   . LEU A 198 ? 0.08995 0.11385 0.10635 0.00180  0.02190  -0.00120 201 LEU A N   
1815 C  CA  . LEU A 198 ? 0.11035 0.10825 0.09395 -0.00170 0.01590  0.01250  201 LEU A CA  
1816 C  C   . LEU A 198 ? 0.12615 0.09625 0.09335 -0.00770 0.00570  0.01000  201 LEU A C   
1817 O  O   . LEU A 198 ? 0.12655 0.09355 0.11395 -0.00610 -0.01200 0.00130  201 LEU A O   
1818 C  CB  . LEU A 198 ? 0.10975 0.10925 0.10705 -0.00040 0.01800  0.01270  201 LEU A CB  
1819 C  CG  . LEU A 198 ? 0.11115 0.11885 0.11745 0.01950  0.01890  0.00300  201 LEU A CG  
1820 C  CD1 . LEU A 198 ? 0.09325 0.10835 0.12875 0.02110  0.01300  0.00220  201 LEU A CD1 
1821 C  CD2 . LEU A 198 ? 0.10305 0.11085 0.10305 0.01960  0.01170  -0.00920 201 LEU A CD2 
1822 N  N   . SER A 199 ? 0.10285 0.11255 0.08865 -0.00000 0.01210  0.00150  202 SER A N   
1823 C  CA  . SER A 199 ? 0.10235 0.11675 0.09825 0.00220  0.00090  0.01050  202 SER A CA  
1824 C  C   . SER A 199 ? 0.11555 0.11315 0.10575 0.00560  -0.00460 0.00820  202 SER A C   
1825 O  O   . SER A 199 ? 0.13125 0.10745 0.11085 0.00900  0.02390  0.00320  202 SER A O   
1826 C  CB  . SER A 199 ? 0.10705 0.15675 0.11595 0.01360  -0.00210 0.01020  202 SER A CB  
1827 O  OG  . SER A 199 ? 0.13605 0.18275 0.14725 0.01980  -0.01110 0.00350  202 SER A OG  
1828 N  N   . VAL A 200 ? 0.10355 0.10185 0.09355 -0.00370 -0.00690 0.00080  203 VAL A N   
1829 C  CA  . VAL A 200 ? 0.09085 0.11095 0.09245 -0.00130 -0.00250 0.00650  203 VAL A CA  
1830 C  C   . VAL A 200 ? 0.09885 0.10455 0.10405 -0.00690 -0.00070 0.01080  203 VAL A C   
1831 O  O   . VAL A 200 ? 0.12905 0.10615 0.10165 -0.00850 -0.00880 0.01670  203 VAL A O   
1832 C  CB  . VAL A 200 ? 0.09205 0.11365 0.09865 0.01590  -0.00380 0.00030  203 VAL A CB  
1833 C  CG1 . VAL A 200 ? 0.09205 0.13445 0.13245 0.01630  0.01200  0.00200  203 VAL A CG1 
1834 C  CG2 . VAL A 200 ? 0.09395 0.11425 0.08595 0.01800  -0.01000 0.00200  203 VAL A CG2 
1835 N  N   . GLN A 201 ? 0.08265 0.12085 0.09705 0.00770  -0.00700 0.00860  204 GLN A N   
1836 C  CA  . GLN A 201 ? 0.09135 0.15765 0.09895 0.00330  -0.00440 0.00850  204 GLN A CA  
1837 C  C   . GLN A 201 ? 0.08575 0.13185 0.09575 -0.00770 -0.00250 0.00320  204 GLN A C   
1838 O  O   . GLN A 201 ? 0.10065 0.11475 0.11725 -0.01690 0.00700  -0.00200 204 GLN A O   
1839 C  CB  . GLN A 201 ? 0.10665 0.17035 0.14345 0.00390  -0.00810 0.01100  204 GLN A CB  
1840 C  CG  . GLN A 201 ? 0.12205 0.21005 0.18705 0.01320  -0.01770 -0.00670 204 GLN A CG  
1841 C  CD  . GLN A 201 ? 0.18085 0.27265 0.22785 0.01930  -0.02940 -0.01780 204 GLN A CD  
1842 O  OE1 . GLN A 201 ? 0.20115 0.33295 0.24535 -0.00060 -0.05280 0.00370  204 GLN A OE1 
1843 N  NE2 . GLN A 201 ? 0.17525 0.28175 0.24365 0.05430  -0.02240 -0.02680 204 GLN A NE2 
1844 N  N   . SER A 202 ? 0.10745 0.12485 0.09445 -0.00490 0.00070  0.00560  205 SER A N   
1845 C  CA  . SER A 202 ? 0.12355 0.11655 0.09585 -0.00840 -0.00550 0.00770  205 SER A CA  
1846 C  C   . SER A 202 ? 0.11645 0.10935 0.10755 -0.01470 -0.00350 0.00760  205 SER A C   
1847 O  O   . SER A 202 ? 0.17075 0.11405 0.13435 -0.05070 -0.00720 -0.00250 205 SER A O   
1848 C  CB  . SER A 202 ? 0.12455 0.10375 0.09905 -0.00410 -0.01130 0.00640  205 SER A CB  
1849 O  OG  . SER A 202 ? 0.10145 0.10795 0.10525 0.00290  0.00590  -0.00980 205 SER A OG  
1850 N  N   . ALA A 203 ? 0.09955 0.11865 0.09405 -0.00470 0.00420  0.00350  206 ALA A N   
1851 C  CA  . ALA A 203 ? 0.10605 0.13335 0.09695 0.00170  0.00230  -0.00570 206 ALA A CA  
1852 C  C   . ALA A 203 ? 0.09135 0.11925 0.08975 -0.00770 -0.00910 -0.00110 206 ALA A C   
1853 O  O   . ALA A 203 ? 0.10405 0.12495 0.08745 0.00510  -0.01340 -0.01140 206 ALA A O   
1854 C  CB  . ALA A 203 ? 0.13155 0.13895 0.11745 0.02200  0.00450  -0.00070 206 ALA A CB  
1855 N  N   . LEU A 204 ? 0.08415 0.11245 0.10165 0.00660  -0.00200 -0.00550 207 LEU A N   
1856 C  CA  . LEU A 204 ? 0.09825 0.11085 0.08345 -0.00480 -0.01030 -0.01150 207 LEU A CA  
1857 C  C   . LEU A 204 ? 0.10825 0.11865 0.08085 -0.01730 -0.01800 -0.01260 207 LEU A C   
1858 O  O   . LEU A 204 ? 0.12195 0.15185 0.09585 -0.03340 -0.01820 -0.01110 207 LEU A O   
1859 C  CB  . LEU A 204 ? 0.09865 0.10865 0.08205 -0.00210 -0.00320 -0.01260 207 LEU A CB  
1860 C  CG  . LEU A 204 ? 0.10465 0.12665 0.09505 0.00520  0.00840  -0.01390 207 LEU A CG  
1861 C  CD1 . LEU A 204 ? 0.10535 0.11085 0.12375 -0.00600 -0.00480 0.00790  207 LEU A CD1 
1862 C  CD2 . LEU A 204 ? 0.10035 0.10875 0.09735 -0.01320 -0.01680 -0.02550 207 LEU A CD2 
1863 N  N   . SER A 205 ? 0.11715 0.11145 0.08605 -0.01060 -0.00430 0.00620  208 SER A N   
1864 C  CA  . SER A 205 ? 0.12065 0.12385 0.09405 -0.00530 0.00680  0.00590  208 SER A CA  
1865 C  C   . SER A 205 ? 0.11575 0.13805 0.08395 -0.02900 -0.00960 0.00700  208 SER A C   
1866 O  O   . SER A 205 ? 0.13975 0.11335 0.09075 -0.01740 -0.00320 0.00910  208 SER A O   
1867 C  CB  . SER A 205 ? 0.12275 0.12385 0.11925 -0.01000 -0.01180 0.01180  208 SER A CB  
1868 O  OG  . SER A 205 ? 0.11985 0.13575 0.11745 -0.00340 -0.01730 0.01100  208 SER A OG  
1869 N  N   . LYS A 206 ? 0.11695 0.18225 0.08425 -0.00430 0.01050  0.01010  209 LYS A N   
1870 C  CA  . LYS A 206 ? 0.14615 0.20885 0.10905 0.01310  0.02180  0.02180  209 LYS A CA  
1871 C  C   . LYS A 206 ? 0.14275 0.24725 0.11205 0.02530  0.00660  0.05940  209 LYS A C   
1872 O  O   . LYS A 206 ? 0.15505 0.28305 0.14645 0.03060  0.01160  0.09010  209 LYS A O   
1873 C  CB  . LYS A 206 ? 0.17695 0.19625 0.12715 0.02000  0.00770  -0.00990 209 LYS A CB  
1874 C  CG  . LYS A 206 ? 0.15355 0.18865 0.13975 0.00650  -0.02720 -0.00600 209 LYS A CG  
1875 C  CD  . LYS A 206 ? 0.13565 0.17325 0.13215 0.00870  -0.01480 -0.00720 209 LYS A CD  
1876 C  CE  . LYS A 206 ? 0.13225 0.15605 0.13185 0.00540  0.00380  -0.02570 209 LYS A CE  
1877 N  NZ  . LYS A 206 ? 0.11925 0.14255 0.12575 -0.00890 -0.00820 -0.02220 209 LYS A NZ  
1878 N  N   . ASP A 207 ? 0.16025 0.24785 0.12305 0.01470  0.00810  0.05900  210 ASP A N   
1879 C  CA  . ASP A 207 ? 0.18055 0.26845 0.17485 0.03540  0.00420  0.06110  210 ASP A CA  
1880 C  C   . ASP A 207 ? 0.18045 0.30115 0.18115 0.01940  -0.03190 0.08990  210 ASP A C   
1881 O  O   . ASP A 207 ? 0.18065 0.28135 0.12575 -0.02130 -0.00160 0.05880  210 ASP A O   
1882 C  CB  . ASP A 207 ? 0.21195 0.25945 0.19575 0.03250  0.02750  0.06060  210 ASP A CB  
1883 C  CG  . ASP A 207 ? 0.23055 0.27505 0.21115 0.04390  0.03210  0.07820  210 ASP A CG  
1884 O  OD1 . ASP A 207 ? 0.22375 0.28575 0.18715 0.07480  0.02880  0.09870  210 ASP A OD1 
1885 O  OD2 . ASP A 207 ? 0.22365 0.27925 0.23035 0.00480  0.02520  0.09820  210 ASP A OD2 
1886 N  N   . PRO A 208 ? 0.24885 0.35965 0.25505 0.02450  -0.05920 0.08790  211 PRO A N   
1887 C  CA  . PRO A 208 ? 0.24575 0.28905 0.25395 0.00300  -0.05880 0.02610  211 PRO A CA  
1901 N  N   . GLU A 210 ? 0.17765 0.19575 0.18105 -0.00170 0.01590  0.02040  213 GLU A N   
1902 C  CA  . GLU A 210 ? 0.15475 0.17105 0.13795 0.02330  0.01890  0.00050  213 GLU A CA  
1903 C  C   . GLU A 210 ? 0.15535 0.16905 0.13265 0.01600  0.04250  -0.00460 213 GLU A C   
1904 O  O   . GLU A 210 ? 0.17355 0.17675 0.14365 -0.00440 0.04190  -0.02390 213 GLU A O   
1905 C  CB  . GLU A 210 ? 0.16555 0.13235 0.12315 0.00940  0.02780  -0.00150 213 GLU A CB  
1906 C  CG  . GLU A 210 ? 0.15345 0.12425 0.12615 0.00630  0.03290  -0.01600 213 GLU A CG  
1907 C  CD  . GLU A 210 ? 0.15635 0.11565 0.11865 0.00290  0.03530  -0.00490 213 GLU A CD  
1908 O  OE1 . GLU A 210 ? 0.17075 0.13535 0.12475 -0.01060 0.03910  -0.00430 213 GLU A OE1 
1909 O  OE2 . GLU A 210 ? 0.17165 0.11395 0.13965 -0.00180 0.02820  0.00520  213 GLU A OE2 
1910 N  N   . LYS A 211 ? 0.16935 0.19515 0.13245 0.02860  0.04740  -0.00550 214 LYS A N   
1911 C  CA  A LYS A 211 ? 0.16745 0.20415 0.15345 0.05390  0.04860  -0.00470 214 LYS A CA  
1913 C  C   . LYS A 211 ? 0.15765 0.16985 0.13135 0.00910  0.03700  -0.00360 214 LYS A C   
1914 O  O   . LYS A 211 ? 0.18305 0.18345 0.12665 0.02230  0.01790  -0.02770 214 LYS A O   
1915 C  CB  A LYS A 211 ? 0.21005 0.23865 0.20205 0.09890  0.07080  -0.00950 214 LYS A CB  
1917 C  CG  A LYS A 211 ? 0.27185 0.29405 0.26855 0.12060  0.08080  -0.01320 214 LYS A CG  
1925 N  N   . ARG A 212 ? 0.13525 0.15145 0.10115 0.00140  0.02730  0.00170  215 ARG A N   
1926 C  CA  . ARG A 212 ? 0.13385 0.13595 0.10975 -0.00680 0.01760  -0.01540 215 ARG A CA  
1927 C  C   . ARG A 212 ? 0.11895 0.13095 0.10825 -0.00960 0.00840  -0.00170 215 ARG A C   
1928 O  O   . ARG A 212 ? 0.12145 0.15145 0.10355 0.00710  0.01680  0.00970  215 ARG A O   
1929 C  CB  . ARG A 212 ? 0.15725 0.12965 0.12795 -0.01640 0.02180  -0.01950 215 ARG A CB  
1930 C  CG  . ARG A 212 ? 0.15865 0.13855 0.14875 -0.02670 0.03170  -0.02070 215 ARG A CG  
1931 C  CD  . ARG A 212 ? 0.16465 0.14675 0.14825 -0.01390 0.02680  -0.02600 215 ARG A CD  
1932 N  NE  . ARG A 212 ? 0.15275 0.13985 0.14725 -0.03220 0.03370  -0.02180 215 ARG A NE  
1933 C  CZ  . ARG A 212 ? 0.15695 0.14085 0.15405 -0.04230 0.03520  -0.01000 215 ARG A CZ  
1934 N  NH1 . ARG A 212 ? 0.16685 0.16855 0.17035 -0.07160 0.03900  -0.01220 215 ARG A NH1 
1935 N  NH2 . ARG A 212 ? 0.18965 0.15095 0.15805 -0.01400 0.01420  -0.01660 215 ARG A NH2 
1936 N  N   . ASP A 213 ? 0.12635 0.11135 0.09755 -0.00700 0.02980  -0.00920 216 ASP A N   
1937 C  CA  . ASP A 213 ? 0.12495 0.11935 0.10325 -0.00130 0.03760  -0.00670 216 ASP A CA  
1938 C  C   . ASP A 213 ? 0.09645 0.11045 0.08995 -0.00290 0.02270  -0.00290 216 ASP A C   
1939 O  O   . ASP A 213 ? 0.09825 0.11685 0.10135 -0.01350 0.00560  -0.00780 216 ASP A O   
1940 C  CB  . ASP A 213 ? 0.13315 0.12345 0.10755 0.00420  0.01550  0.00100  216 ASP A CB  
1941 C  CG  . ASP A 213 ? 0.12785 0.11835 0.11335 0.00960  0.02540  -0.00770 216 ASP A CG  
1942 O  OD1 . ASP A 213 ? 0.12815 0.13905 0.10865 -0.01370 0.01460  -0.01440 216 ASP A OD1 
1943 O  OD2 . ASP A 213 ? 0.13035 0.14695 0.12755 -0.01090 0.00980  0.01780  216 ASP A OD2 
1944 N  N   . HIS A 214 ? 0.11175 0.11305 0.09345 0.00990  0.02560  -0.01060 217 HIS A N   
1945 C  CA  . HIS A 214 ? 0.10475 0.10025 0.09765 -0.00240 0.02840  -0.00160 217 HIS A CA  
1946 C  C   . HIS A 214 ? 0.11445 0.09285 0.08745 -0.00110 0.00780  -0.00760 217 HIS A C   
1947 O  O   . HIS A 214 ? 0.11725 0.09305 0.11295 -0.00390 0.00740  -0.01330 217 HIS A O   
1948 C  CB  . HIS A 214 ? 0.12665 0.09095 0.10055 -0.01070 0.00330  -0.00110 217 HIS A CB  
1949 C  CG  . HIS A 214 ? 0.12365 0.11975 0.08865 0.00360  -0.00090 0.01100  217 HIS A CG  
1950 N  ND1 . HIS A 214 ? 0.11775 0.12825 0.09495 -0.01230 -0.00370 0.00580  217 HIS A ND1 
1951 C  CD2 . HIS A 214 ? 0.13375 0.14475 0.09415 0.00220  -0.00480 0.03380  217 HIS A CD2 
1952 C  CE1 . HIS A 214 ? 0.14045 0.14305 0.11065 0.00610  -0.00540 0.01590  217 HIS A CE1 
1953 N  NE2 . HIS A 214 ? 0.13835 0.17355 0.11015 0.00170  -0.00740 0.01590  217 HIS A NE2 
1954 N  N   . MET A 215 ? 0.10025 0.10135 0.09665 -0.00660 0.02280  -0.01260 218 MET A N   
1955 C  CA  . MET A 215 ? 0.08835 0.09675 0.08795 -0.00040 0.01100  0.00060  218 MET A CA  
1956 C  C   . MET A 215 ? 0.08985 0.09355 0.09345 -0.01320 0.00740  0.00120  218 MET A C   
1957 O  O   . MET A 215 ? 0.09545 0.08755 0.11095 -0.01180 -0.00810 -0.00340 218 MET A O   
1958 C  CB  . MET A 215 ? 0.07695 0.11665 0.08005 0.00580  0.00770  -0.00560 218 MET A CB  
1959 C  CG  . MET A 215 ? 0.08355 0.10865 0.09445 -0.00200 0.00510  0.00390  218 MET A CG  
1960 S  SD  . MET A 215 ? 0.09285 0.09795 0.09525 -0.00480 0.00050  0.00330  218 MET A SD  
1961 C  CE  . MET A 215 ? 0.08605 0.12995 0.10725 -0.01320 -0.02660 -0.01250 218 MET A CE  
1962 N  N   . VAL A 216 ? 0.08975 0.08985 0.08775 0.00690  0.00400  0.00160  219 VAL A N   
1963 C  CA  . VAL A 216 ? 0.09265 0.09795 0.08785 0.00670  -0.00240 0.00770  219 VAL A CA  
1964 C  C   . VAL A 216 ? 0.07525 0.10275 0.08265 0.00310  -0.00130 -0.00240 219 VAL A C   
1965 O  O   . VAL A 216 ? 0.08695 0.09075 0.09615 -0.00380 -0.00800 -0.00270 219 VAL A O   
1966 C  CB  . VAL A 216 ? 0.11805 0.11055 0.09545 0.00890  0.01210  0.01270  219 VAL A CB  
1967 C  CG1 . VAL A 216 ? 0.14955 0.11735 0.10825 0.01880  0.00910  0.01510  219 VAL A CG1 
1968 C  CG2 . VAL A 216 ? 0.11325 0.15365 0.11255 0.00820  0.03830  0.01570  219 VAL A CG2 
1969 N  N   . LEU A 217 ? 0.08515 0.11355 0.08545 0.00540  0.00610  0.00910  220 LEU A N   
1970 C  CA  . LEU A 217 ? 0.08935 0.11435 0.07275 0.01150  -0.00250 -0.00220 220 LEU A CA  
1971 C  C   . LEU A 217 ? 0.09195 0.10895 0.09485 -0.00270 0.00490  -0.00060 220 LEU A C   
1972 O  O   . LEU A 217 ? 0.09585 0.10575 0.11955 -0.01420 0.01180  -0.02140 220 LEU A O   
1973 C  CB  . LEU A 217 ? 0.10195 0.12955 0.07245 0.00160  -0.00080 0.01220  220 LEU A CB  
1974 C  CG  . LEU A 217 ? 0.09955 0.13255 0.06655 -0.03090 0.00710  0.00120  220 LEU A CG  
1975 C  CD1 . LEU A 217 ? 0.10525 0.11515 0.10295 -0.02230 0.00590  0.02240  220 LEU A CD1 
1976 C  CD2 . LEU A 217 ? 0.12825 0.16235 0.07095 -0.03770 -0.00010 -0.00350 220 LEU A CD2 
1977 N  N   . LEU A 218 ? 0.07425 0.11095 0.09015 0.00250  0.00200  0.01230  221 LEU A N   
1978 C  CA  . LEU A 218 ? 0.09665 0.10535 0.10745 0.00020  -0.00230 0.00400  221 LEU A CA  
1979 C  C   . LEU A 218 ? 0.06895 0.10525 0.09145 0.00010  -0.02030 -0.00500 221 LEU A C   
1980 O  O   . LEU A 218 ? 0.09515 0.13125 0.11175 -0.02470 0.00200  -0.02430 221 LEU A O   
1981 C  CB  . LEU A 218 ? 0.10765 0.13035 0.12825 0.01580  -0.00630 0.01540  221 LEU A CB  
1982 C  CG  . LEU A 218 ? 0.16095 0.15105 0.16615 0.00400  -0.00990 0.02060  221 LEU A CG  
1983 C  CD1 . LEU A 218 ? 0.19845 0.15415 0.19525 0.00560  0.00200  0.02080  221 LEU A CD1 
1984 C  CD2 . LEU A 218 ? 0.17115 0.18945 0.16845 0.01880  -0.01870 0.01870  221 LEU A CD2 
1985 N  N   . GLU A 219 ? 0.09445 0.09735 0.08985 0.00300  -0.00320 0.00720  222 GLU A N   
1986 C  CA  . GLU A 219 ? 0.08705 0.09285 0.10015 0.01520  0.00960  0.01570  222 GLU A CA  
1987 C  C   . GLU A 219 ? 0.08575 0.09675 0.11925 -0.00660 0.00370  0.00570  222 GLU A C   
1988 O  O   . GLU A 219 ? 0.10055 0.11785 0.14035 -0.01510 0.01310  -0.00440 222 GLU A O   
1989 C  CB  . GLU A 219 ? 0.10885 0.13035 0.12675 -0.01270 -0.00700 0.03760  222 GLU A CB  
1990 C  CG  . GLU A 219 ? 0.09885 0.12235 0.14525 0.00150  -0.01110 0.02060  222 GLU A CG  
1991 C  CD  . GLU A 219 ? 0.10165 0.10595 0.15415 -0.00930 -0.01800 0.01420  222 GLU A CD  
1992 O  OE1 . GLU A 219 ? 0.08575 0.11765 0.12625 -0.00420 -0.01050 0.03110  222 GLU A OE1 
1993 O  OE2 . GLU A 219 ? 0.08065 0.11795 0.19295 0.01860  -0.02510 -0.02360 222 GLU A OE2 
1994 N  N   . PHE A 220 ? 0.07785 0.11135 0.11055 -0.00750 0.00600  0.00190  223 PHE A N   
1995 C  CA  . PHE A 220 ? 0.08865 0.11145 0.10075 0.01040  0.01260  -0.00070 223 PHE A CA  
1996 C  C   . PHE A 220 ? 0.09595 0.12205 0.09025 -0.00390 0.01350  -0.00590 223 PHE A C   
1997 O  O   . PHE A 220 ? 0.13235 0.11855 0.10925 -0.02220 0.02490  0.00040  223 PHE A O   
1998 C  CB  . PHE A 220 ? 0.09585 0.12355 0.12285 0.00360  -0.00220 0.00700  223 PHE A CB  
1999 C  CG  . PHE A 220 ? 0.08345 0.11765 0.14855 0.01450  -0.01100 0.02750  223 PHE A CG  
2000 C  CD1 . PHE A 220 ? 0.07845 0.12785 0.18605 0.02620  -0.00540 0.01890  223 PHE A CD1 
2001 C  CD2 . PHE A 220 ? 0.08135 0.14185 0.14325 0.00630  -0.00130 0.03340  223 PHE A CD2 
2002 C  CE1 . PHE A 220 ? 0.07885 0.14635 0.20195 0.01730  -0.01770 0.03090  223 PHE A CE1 
2003 C  CE2 . PHE A 220 ? 0.09475 0.15725 0.15665 0.02120  -0.01030 0.03960  223 PHE A CE2 
2004 C  CZ  . PHE A 220 ? 0.10175 0.15735 0.19025 0.01470  -0.01360 0.04890  223 PHE A CZ  
2005 N  N   . VAL A 221 ? 0.11675 0.13705 0.08025 0.00220  0.01110  0.00000  224 VAL A N   
2006 C  CA  . VAL A 221 ? 0.15865 0.12345 0.09595 0.00160  0.01910  0.01230  224 VAL A CA  
2007 C  C   . VAL A 221 ? 0.16725 0.11405 0.10895 -0.00270 0.03040  -0.01400 224 VAL A C   
2008 O  O   . VAL A 221 ? 0.17185 0.10285 0.11935 -0.01650 0.01430  -0.01100 224 VAL A O   
2009 C  CB  . VAL A 221 ? 0.18475 0.10835 0.13555 0.01340  -0.00490 0.02230  224 VAL A CB  
2010 C  CG1 . VAL A 221 ? 0.21655 0.11025 0.13125 -0.00990 -0.02360 0.01730  224 VAL A CG1 
2011 C  CG2 . VAL A 221 ? 0.16585 0.10425 0.15525 0.04370  -0.00760 -0.00850 224 VAL A CG2 
2012 N  N   . THR A 222 ? 0.15445 0.11585 0.12185 -0.00380 0.04120  0.00800  225 THR A N   
2013 C  CA  . THR A 222 ? 0.14085 0.13385 0.11095 0.00940  0.01640  0.01400  225 THR A CA  
2014 C  C   . THR A 222 ? 0.12585 0.10935 0.10695 0.01140  0.02320  -0.00550 225 THR A C   
2015 O  O   . THR A 222 ? 0.13415 0.10535 0.12035 0.00780  0.02420  0.00590  225 THR A O   
2016 C  CB  . THR A 222 ? 0.15365 0.20015 0.12155 0.00770  -0.00360 0.02530  225 THR A CB  
2017 O  OG1 . THR A 222 ? 0.17835 0.24625 0.13685 -0.01930 -0.01200 0.02890  225 THR A OG1 
2018 C  CG2 . THR A 222 ? 0.15795 0.18285 0.13585 0.02130  -0.00160 0.02790  225 THR A CG2 
2019 N  N   . ALA A 223 ? 0.11415 0.11175 0.10485 0.02840  0.01340  -0.00450 226 ALA A N   
2020 C  CA  . ALA A 223 ? 0.11445 0.12605 0.10105 0.01620  -0.00740 0.00050  226 ALA A CA  
2021 C  C   . ALA A 223 ? 0.09595 0.13145 0.10835 0.02620  -0.00460 -0.00370 226 ALA A C   
2022 O  O   . ALA A 223 ? 0.10065 0.13335 0.13195 0.03100  0.00760  0.00920  226 ALA A O   
2023 C  CB  . ALA A 223 ? 0.11105 0.12915 0.10765 0.00920  0.00100  -0.00160 226 ALA A CB  
2024 N  N   . ALA A 224 ? 0.09505 0.14825 0.12055 0.01110  0.01930  0.00350  227 ALA A N   
2025 C  CA  . ALA A 224 ? 0.10945 0.17055 0.13175 0.00640  0.01420  0.01450  227 ALA A CA  
2026 C  C   . ALA A 224 ? 0.09805 0.16535 0.14135 0.00790  0.02640  0.01150  227 ALA A C   
2027 O  O   . ALA A 224 ? 0.11755 0.15645 0.13615 0.01830  0.01190  0.01540  227 ALA A O   
2028 C  CB  . ALA A 224 ? 0.12925 0.17595 0.13775 -0.02170 -0.02460 0.01080  227 ALA A CB  
2029 N  N   . GLY A 225 ? 0.12265 0.20265 0.16335 0.01680  0.04530  0.00610  228 GLY A N   
2030 C  CA  . GLY A 225 ? 0.18605 0.19665 0.16975 0.00590  0.06700  0.00740  228 GLY A CA  
2031 C  C   . GLY A 225 ? 0.21125 0.20745 0.18435 0.01560  0.07240  0.01690  228 GLY A C   
2032 O  O   . GLY A 225 ? 0.25145 0.21575 0.19685 -0.01320 0.06350  0.01830  228 GLY A O   
2033 N  N   . ILE A 226 ? 0.20815 0.21005 0.19345 0.02170  0.09820  0.00970  229 ILE A N   
2034 C  CA  . ILE A 226 ? 0.23645 0.21965 0.23435 0.03860  0.09880  -0.00180 229 ILE A CA  
2035 C  C   . ILE A 226 ? 0.24605 0.22975 0.25285 0.04060  0.11010  0.01900  229 ILE A C   
2036 O  O   . ILE A 226 ? 0.24595 0.19775 0.25025 0.04690  0.10680  0.04200  229 ILE A O   
2037 C  CB  . ILE A 226 ? 0.26355 0.23635 0.24975 0.03770  0.09860  -0.00920 229 ILE A CB  
2038 C  CG1 . ILE A 226 ? 0.26355 0.22375 0.24625 0.02580  0.08810  0.00250  229 ILE A CG1 
2040 C  CD1 . ILE A 226 ? 0.26755 0.22645 0.23415 0.02470  0.08640  -0.00430 229 ILE A CD1 
2060 MG MG  . MG  C .   ? 0.08865 0.11045 0.15095 0.00570  -0.02540 0.04140  302 MG  A MG  
2061 O  O   . HOH D .   ? 0.08635 0.10625 0.12715 0.01130  -0.00050 -0.01950 401 HOH A O   
2062 O  O   A HOH D .   ? 0.08795 0.20915 0.24685 -0.00160 -0.00620 0.11550  402 HOH A O   
2064 O  O   . HOH D .   ? 0.07695 0.12205 0.10505 0.00940  -0.00370 -0.00770 403 HOH A O   
2065 O  O   A HOH D .   ? 0.16565 0.18235 0.22445 0.00920  -0.03460 -0.02190 404 HOH A O   
2067 O  O   . HOH D .   ? 0.07955 0.09525 0.09735 -0.00490 0.00770  -0.00290 405 HOH A O   
2068 O  O   . HOH D .   ? 0.10805 0.07345 0.08435 0.00630  -0.02430 0.00870  406 HOH A O   
2069 O  O   . HOH D .   ? 0.12845 0.15805 0.13955 0.01110  0.01420  0.03260  407 HOH A O   
2070 O  O   . HOH D .   ? 0.11635 0.08565 0.07065 -0.01240 0.00210  0.01310  408 HOH A O   
2071 O  O   . HOH D .   ? 0.11955 0.15245 0.29845 0.01280  0.00340  -0.05760 409 HOH A O   
2072 O  O   . HOH D .   ? 0.17935 0.15925 0.15265 -0.06910 0.00220  0.02500  410 HOH A O   
2073 O  O   . HOH D .   ? 0.15755 0.21275 0.32425 -0.00630 -0.03020 0.03650  411 HOH A O   
2076 O  O   . HOH D .   ? 0.08655 0.09725 0.06845 -0.01620 -0.01370 0.01080  413 HOH A O   
2077 O  O   . HOH D .   ? 0.11745 0.11355 0.08895 0.03120  -0.01580 -0.00660 414 HOH A O   
2078 O  O   A HOH D .   ? 0.10335 0.27465 0.19315 0.01910  0.01200  0.02940  415 HOH A O   
2080 O  O   . HOH D .   ? 0.17905 0.16525 0.14695 -0.05280 -0.00640 0.01820  416 HOH A O   
2082 O  O   B HOH D .   ? 0.16305 0.27175 0.23575 -0.01530 0.03310  -0.00580 417 HOH A O   
2084 O  O   . HOH D .   ? 0.09595 0.12345 0.15085 -0.02760 -0.00980 0.03310  419 HOH A O   
2085 O  O   . HOH D .   ? 0.09405 0.06965 0.08905 -0.00610 0.01770  -0.00420 420 HOH A O   
2087 O  O   . HOH D .   ? 0.23505 0.21885 0.24795 -0.03750 0.01540  0.01190  422 HOH A O   
2093 O  O   . HOH D .   ? 0.18055 0.34795 0.26675 0.05460  -0.02230 -0.06330 426 HOH A O   
2094 O  O   A HOH D .   ? 0.12515 0.18865 0.15565 0.05000  -0.03610 0.01010  427 HOH A O   
2098 O  O   . HOH D .   ? 0.13705 0.09575 0.09295 0.00200  -0.00790 0.00420  430 HOH A O   
2099 O  O   A HOH D .   ? 0.37345 0.20855 0.17255 0.06530  -0.03380 0.04150  431 HOH A O   
2101 O  O   . HOH D .   ? 0.13715 0.13285 0.18535 -0.00610 -0.00770 -0.00870 432 HOH A O   
2102 O  O   . HOH D .   ? 0.18375 0.16335 0.10365 0.01720  -0.02420 -0.02790 433 HOH A O   
2104 O  O   . HOH D .   ? 0.09155 0.08645 0.09005 0.01300  -0.00380 0.00500  435 HOH A O   
2105 O  O   . HOH D .   ? 0.10565 0.08665 0.09555 0.00940  0.01160  0.01630  436 HOH A O   
2106 O  O   . HOH D .   ? 0.18925 0.20405 0.19985 -0.02100 0.01920  -0.00820 437 HOH A O   
2107 O  O   . HOH D .   ? 0.18715 0.21425 0.21245 -0.07960 -0.00660 -0.01420 438 HOH A O   
2108 O  O   A HOH D .   ? 0.21315 0.28825 0.27415 -0.06460 0.05350  -0.08590 439 HOH A O   
2113 O  O   . HOH D .   ? 0.08595 0.07315 0.09495 -0.00140 -0.00160 -0.00710 443 HOH A O   
2114 O  O   . HOH D .   ? 0.13835 0.11525 0.19145 -0.00640 -0.02090 -0.01120 444 HOH A O   
2123 O  O   A HOH D .   ? 0.21215 0.26445 0.14775 -0.06500 -0.01500 0.03270  451 HOH A O   
2126 O  O   A HOH D .   ? 0.13165 0.21185 0.21605 -0.00310 0.03470  -0.02900 453 HOH A O   
2129 O  O   B HOH D .   ? 0.07555 0.28145 0.27025 -0.01960 0.00380  0.01140  454 HOH A O   
2131 O  O   . HOH D .   ? 0.13025 0.10645 0.13275 -0.01980 -0.00780 0.01030  456 HOH A O   
2135 O  O   A HOH D .   ? 0.28205 0.19745 0.18905 0.00540  0.01480  0.00310  460 HOH A O   
2138 O  O   . HOH D .   ? 0.11835 0.11305 0.09865 0.00740  0.01970  -0.00070 462 HOH A O   
2141 O  O   . HOH D .   ? 0.15735 0.14475 0.17105 -0.01650 0.01900  0.02190  465 HOH A O   
2143 O  O   . HOH D .   ? 0.17915 0.19005 0.11505 0.02450  0.01230  -0.00030 467 HOH A O   
2146 O  O   A HOH D .   ? 0.15355 0.22365 0.16395 -0.05900 0.03320  0.01900  470 HOH A O   
2152 O  O   A HOH D .   ? 0.09385 0.31635 0.26765 -0.03070 0.00230  0.05210  474 HOH A O   
2154 O  O   . HOH D .   ? 0.21705 0.20865 0.19315 -0.02640 0.04440  0.01460  475 HOH A O   
2164 O  O   . HOH D .   ? 0.28625 0.17775 0.29915 0.02090  -0.07960 0.00860  484 HOH A O   
2165 O  O   . HOH D .   ? 0.12015 0.16495 0.21645 0.01030  -0.01720 0.04800  485 HOH A O   
2166 O  O   . HOH D .   ? 0.17965 0.38965 0.21525 0.03220  -0.06330 -0.06330 486 HOH A O   
2170 O  O   . HOH D .   ? 0.20925 0.29125 0.17885 0.00600  -0.04350 0.03440  490 HOH A O   
2172 O  O   . HOH D .   ? 0.12595 0.22055 0.25495 0.01440  -0.03250 -0.09280 492 HOH A O   
2174 O  O   . HOH D .   ? 0.22925 0.38915 0.16835 0.00070  -0.02070 0.03640  494 HOH A O   
2181 O  O   . HOH D .   ? 0.11045 0.11135 0.42685 0.00220  -0.01140 -0.02310 500 HOH A O   
2182 O  O   . HOH D .   ? 0.21405 0.22265 0.21095 0.01210  0.00310  0.07920  501 HOH A O   
2184 O  O   . HOH D .   ? 0.18375 0.17825 0.32905 -0.05560 0.10640  -0.07230 503 HOH A O   
2188 O  O   A HOH D .   ? 0.13235 0.15115 0.23045 -0.01100 0.00950  0.00210  506 HOH A O   
2191 O  O   . HOH D .   ? 0.11615 0.16325 0.33935 0.02010  -0.00510 0.00660  508 HOH A O   
2193 O  O   . HOH D .   ? 0.17035 0.30205 0.17315 -0.04810 0.00210  -0.01690 510 HOH A O   
2195 O  O   . HOH D .   ? 0.16835 0.19995 0.19425 -0.00990 -0.05050 -0.00010 512 HOH A O   
2196 O  O   A HOH D .   ? 0.11755 0.10955 0.08975 -0.02850 -0.02780 0.00400  513 HOH A O   
2201 O  O   . HOH D .   ? 0.09085 0.10945 0.14975 -0.00010 -0.03830 0.01060  517 HOH A O   
2207 O  O   . HOH D .   ? 0.20655 0.14295 0.16275 -0.03390 0.03920  0.01300  522 HOH A O   
2209 O  O   . HOH D .   ? 0.11605 0.10455 0.15445 -0.01660 0.00750  0.00210  524 HOH A O   
2212 O  O   . HOH D .   ? 0.28325 0.28955 0.17375 -0.08460 0.05890  0.00810  527 HOH A O   
2213 O  O   . HOH D .   ? 0.25595 0.21115 0.21625 0.06480  -0.00850 -0.01810 528 HOH A O   
2214 O  O   . HOH D .   ? 0.15045 0.19525 0.16605 -0.02010 -0.01510 -0.04730 529 HOH A O   
2218 O  O   A HOH D .   ? 0.28485 0.18985 0.11025 -0.01050 -0.07790 0.01050  532 HOH A O   
2224 O  O   . HOH D .   ? 0.13465 0.11395 0.17465 0.02630  0.01020  0.01190  537 HOH A O   
2225 O  O   . HOH D .   ? 0.19155 0.25255 0.48635 0.05510  0.04930  0.16410  538 HOH A O   
2226 O  O   B HOH D .   ? 0.17355 0.20555 0.16965 -0.04290 -0.07670 0.02630  539 HOH A O   
2231 O  O   . HOH D .   ? 0.23965 0.28195 0.17955 0.12720  -0.04810 -0.03000 543 HOH A O   
2232 O  O   . HOH D .   ? 0.12795 0.11745 0.14945 -0.02330 0.01200  -0.00470 544 HOH A O   
2233 O  O   A HOH D .   ? 0.19905 0.24995 0.29655 0.01210  -0.07500 0.09740  545 HOH A O   
2237 O  O   . HOH D .   ? 0.32745 0.18445 0.15815 -0.08540 -0.00430 0.00350  548 HOH A O   
2238 O  O   . HOH D .   ? 0.20145 0.15775 0.16865 -0.05490 0.03860  -0.04430 549 HOH A O   
2243 O  O   . HOH D .   ? 0.26345 0.18875 0.23955 0.04160  -0.01050 0.02830  554 HOH A O   
2245 O  O   A HOH D .   ? 0.21855 0.15435 0.37105 0.05610  0.12330  0.03150  556 HOH A O   
2247 O  O   A HOH D .   ? 0.17675 0.34215 0.18665 0.01310  0.03230  0.10300  557 HOH A O   
2249 O  O   A HOH D .   ? 0.23245 0.24345 0.25815 0.02140  -0.00060 0.10570  558 HOH A O   
2250 O  O   . HOH D .   ? 0.20025 0.15965 0.14865 -0.06370 -0.00550 0.02270  559 HOH A O   
2253 O  O   A HOH D .   ? 0.27105 0.24545 0.11185 -0.01410 -0.06640 -0.04460 562 HOH A O   
2255 O  O   . HOH D .   ? 0.17575 0.14365 0.22275 0.00140  0.06700  -0.04420 563 HOH A O   
2256 O  O   . HOH D .   ? 0.28745 0.11145 0.18335 -0.03640 0.07560  -0.03130 564 HOH A O   
2257 O  O   B HOH D .   ? 0.09945 0.16085 0.29375 0.02040  0.02110  0.10830  565 HOH A O   
2260 O  O   A HOH D .   ? 0.31125 0.28805 0.13585 -0.08780 0.01280  0.06810  567 HOH A O   
2262 O  O   . HOH D .   ? 0.21305 0.27775 0.27735 -0.06330 -0.04710 0.06960  568 HOH A O   
2265 O  O   . HOH D .   ? 0.14135 0.14965 0.12845 0.01850  -0.00190 -0.02230 571 HOH A O   
2268 O  O   . HOH D .   ? 0.16275 0.15315 0.12255 0.01310  0.04600  0.00700  573 HOH A O   
2269 O  O   A HOH D .   ? 0.11825 0.12435 0.22295 -0.02700 -0.02130 0.02080  574 HOH A O   
2271 O  O   . HOH D .   ? 0.09135 0.11615 0.10905 0.00880  -0.01700 0.00690  575 HOH A O   
2278 O  O   . HOH D .   ? 0.20675 0.20905 0.36125 -0.01700 -0.05700 0.02360  581 HOH A O   
2280 O  O   B HOH D .   ? 0.28725 0.29765 0.19935 -0.14660 0.10320  -0.07630 583 HOH A O   
2281 O  O   . HOH D .   ? 0.12495 0.18665 0.17945 0.05130  -0.01100 0.00890  584 HOH A O   
2285 O  O   A HOH D .   ? 0.21585 0.27265 0.25565 -0.06270 0.02890  -0.06330 588 HOH A O   
2287 O  O   A HOH D .   ? 0.19335 0.25835 0.17845 0.02110  -0.02220 0.04780  589 HOH A O   
2289 O  O   . HOH D .   ? 0.20215 0.37575 0.16155 0.02270  -0.03890 -0.07360 590 HOH A O   
2291 O  O   A HOH D .   ? 0.07395 0.11505 0.14315 -0.00140 -0.01110 -0.01360 592 HOH A O   
2293 O  O   . HOH D .   ? 0.09915 0.14605 0.33075 -0.02690 0.02890  -0.02190 593 HOH A O   
2294 O  O   A HOH D .   ? 0.27215 0.20395 0.30665 -0.04580 0.10940  0.07940  594 HOH A O   
2304 O  O   B HOH D .   ? 0.22915 0.36485 0.22805 -0.06510 0.09060  0.03220  601 HOH A O   
2306 O  O   A HOH D .   ? 0.09815 0.14385 0.12885 0.01190  0.02440  -0.02370 602 HOH A O   
2308 O  O   . HOH D .   ? 0.14965 0.13755 0.15485 0.03410  0.01830  0.01030  603 HOH A O   
2309 O  O   A HOH D .   ? 0.35585 0.22855 0.18075 -0.04450 -0.00570 0.05690  604 HOH A O   
2311 O  O   . HOH D .   ? 0.20155 0.26655 0.28675 -0.05440 -0.01590 0.15460  605 HOH A O   
2314 O  O   A HOH D .   ? 0.20545 0.21155 0.16265 0.00380  -0.03090 -0.06030 608 HOH A O   
2319 O  O   A HOH D .   ? 0.17755 0.14495 0.41645 -0.03230 0.08900  -0.08530 611 HOH A O   
2324 O  O   . HOH D .   ? 0.48285 0.18675 0.18675 -0.06330 -0.06330 0.04540  615 HOH A O   
2327 O  O   . HOH D .   ? 0.24795 0.29225 0.22705 -0.09230 -0.03860 0.06430  617 HOH A O   
2328 O  O   . HOH D .   ? 0.23045 0.21795 0.30755 -0.00370 0.06340  0.00950  618 HOH A O   
2329 O  O   . HOH D .   ? 0.13325 0.13575 0.13565 -0.01890 0.00830  -0.04010 619 HOH A O   
2330 O  O   A HOH D .   ? 0.28315 0.19875 0.18155 0.04790  0.09090  0.05240  620 HOH A O   
2332 O  O   . HOH D .   ? 0.13505 0.22265 0.28555 -0.04960 -0.02040 0.11150  621 HOH A O   
2335 O  O   . HOH D .   ? 0.26405 0.28275 0.16295 -0.08180 0.01460  0.05210  624 HOH A O   
2347 O  O   . HOH D .   ? 0.22455 0.18525 0.25965 -0.03150 -0.04020 -0.03830 633 HOH A O   
2350 O  O   . HOH D .   ? 0.12705 0.10345 0.11765 0.00420  -0.00020 0.01170  635 HOH A O   
2353 O  O   . HOH D .   ? 0.14615 0.24855 0.11935 -0.01080 -0.00160 -0.00970 638 HOH A O   
2356 O  O   A HOH D .   ? 0.18415 0.32255 0.31375 0.06730  -0.06330 -0.01290 640 HOH A O   
2358 O  O   . HOH D .   ? 0.30225 0.25395 0.18765 0.05470  0.12740  0.00840  641 HOH A O   
2359 O  O   . HOH D .   ? 0.18645 0.23235 0.30125 -0.02820 -0.05980 0.06390  642 HOH A O   
2363 O  O   A HOH D .   ? 0.18845 0.19875 0.25315 -0.09320 0.06270  -0.06380 645 HOH A O   
2364 O  O   . HOH D .   ? 0.10055 0.15075 0.12615 0.00780  -0.00760 -0.00690 646 HOH A O   
2366 O  O   . HOH D .   ? 0.13205 0.14095 0.23435 -0.01790 -0.00680 0.01660  648 HOH A O   
2367 O  O   . HOH D .   ? 0.21515 0.18585 0.20205 0.00940  -0.03780 0.01150  649 HOH A O   
2368 O  O   A HOH D .   ? 0.16585 0.13175 0.17245 0.03400  -0.03420 0.02060  650 HOH A O   
2370 O  O   . HOH D .   ? 0.34805 0.20115 0.17625 0.11030  0.01200  0.02550  651 HOH A O   
2371 O  O   . HOH D .   ? 0.11085 0.11605 0.17935 -0.01230 0.00060  0.02360  652 HOH A O   
2372 O  O   . HOH D .   ? 0.28015 0.16825 0.30745 0.03440  -0.06700 0.00750  653 HOH A O   
2381 O  O   B HOH D .   ? 0.23785 0.23785 0.23785 -0.00000 -0.00000 0.00000  660 HOH A O   
2382 O  O   . HOH D .   ? 0.29515 0.20685 0.17825 -0.00370 -0.03130 0.04270  661 HOH A O   
2387 O  O   . HOH D .   ? 0.13225 0.15295 0.18515 0.00430  -0.00290 0.02030  664 HOH A O   
2395 O  O   A HOH D .   ? 0.20225 0.30865 0.23795 -0.00860 0.05970  0.08930  670 HOH A O   
2397 O  O   . HOH D .   ? 0.11995 0.16605 0.24525 -0.00870 0.00420  -0.03370 671 HOH A O   
2401 O  O   . HOH D .   ? 0.15875 0.21415 0.14375 -0.03400 -0.01140 0.03920  674 HOH A O   
2406 O  O   A HOH D .   ? 0.23035 0.23975 0.24765 0.06830  0.04430  0.03290  678 HOH A O   
2418 O  O   . HOH D .   ? 0.13175 0.16625 0.21055 -0.02940 0.00970  -0.01530 688 HOH A O   
2424 O  O   . HOH D .   ? 0.24455 0.17795 0.13685 -0.03490 -0.00290 0.02620  693 HOH A O   
2425 O  O   A HOH D .   ? 0.16155 0.13925 0.24685 -0.01730 0.01270  -0.06080 694 HOH A O   
2439 O  O   A HOH D .   ? 0.23735 0.13305 0.17235 -0.01820 0.01860  -0.02790 706 HOH A O   
2441 O  O   . HOH D .   ? 0.24505 0.20115 0.20035 -0.06820 0.00060  0.01400  707 HOH A O   
2442 O  O   . HOH D .   ? 0.27425 0.32475 0.15415 0.14490  -0.02650 -0.07140 708 HOH A O   
2446 O  O   . HOH D .   ? 0.14915 0.14055 0.18895 -0.03760 0.02120  -0.00030 710 HOH A O   
2447 O  O   A HOH D .   ? 0.13165 0.38095 0.21565 -0.03880 0.05210  -0.07730 711 HOH A O   
2449 O  O   A HOH D .   ? 0.29315 0.16295 0.26195 -0.09580 0.08370  0.00720  712 HOH A O   
2455 O  O   . HOH D .   ? 0.08715 0.10675 0.14885 0.01180  0.00250  0.01500  716 HOH A O   
2457 O  O   A HOH D .   ? 0.16705 0.18055 0.13515 0.00390  0.02460  -0.02730 718 HOH A O   
2459 O  O   . HOH D .   ? 0.17905 0.24405 0.19385 -0.01030 -0.00750 -0.01990 719 HOH A O   
2464 O  O   . HOH D .   ? 0.27935 0.19325 0.26945 0.02580  -0.01590 0.00430  723 HOH A O   
2465 O  O   A HOH D .   ? 0.24645 0.16695 0.24225 -0.03030 -0.12710 -0.02790 724 HOH A O   
2467 O  O   B HOH D .   ? 0.18455 0.17595 0.13255 0.01770  0.00760  -0.01620 725 HOH A O   
2472 O  O   . HOH D .   ? 0.18435 0.16755 0.15345 -0.04180 0.01020  -0.01780 729 HOH A O   
2474 O  O   . HOH D .   ? 0.18425 0.28145 0.18765 0.01060  -0.02060 -0.02310 731 HOH A O   
2477 O  O   B HOH D .   ? 0.21785 0.20905 0.29525 -0.01460 0.04200  0.12390  733 HOH A O   
2480 O  O   . HOH D .   ? 0.12155 0.17935 0.22135 0.02710  0.02450  0.04970  735 HOH A O   
2487 O  O   . HOH D .   ? 0.17815 0.20415 0.23205 -0.01870 -0.04600 0.04560  741 HOH A O   
2491 O  O   . HOH D .   ? 0.38055 0.15275 0.22765 0.07380  0.00540  0.06330  744 HOH A O   
2494 O  O   A HOH D .   ? 0.16075 0.17965 0.14205 -0.00230 -0.03010 -0.04680 746 HOH A O   
2497 O  O   B HOH D .   ? 0.19355 0.22985 0.23435 0.06090  -0.07500 -0.00120 747 HOH A O   
2499 O  O   A HOH D .   ? 0.13985 0.43015 0.16515 0.00860  -0.00660 -0.07190 749 HOH A O   
2502 O  O   . HOH D .   ? 0.14425 0.22355 0.28995 -0.00820 0.01400  0.11980  751 HOH A O   
2506 O  O   A HOH D .   ? 0.17395 0.24015 0.25065 -0.03830 0.02050  0.02370  755 HOH A O   
2508 O  O   . HOH D .   ? 0.26495 0.19075 0.28115 -0.02650 0.06440  -0.00650 756 HOH A O   
2509 O  O   . HOH D .   ? 0.20895 0.20745 0.17415 -0.04380 -0.03650 0.00080  757 HOH A O   
2511 O  O   . HOH D .   ? 0.16175 0.21195 0.17635 0.00580  0.01600  -0.00280 759 HOH A O   
2534 O  O   A HOH D .   ? 0.19085 0.20615 0.32255 0.07210  0.11260  0.03760  778 HOH A O   
2545 O  O   . HOH D .   ? 0.30445 0.22875 0.25635 0.03860  0.13480  0.03270  786 HOH A O   
2547 O  O   . HOH D .   ? 0.16085 0.29835 0.21745 -0.00500 0.02040  0.02890  788 HOH A O   
2552 O  O   . HOH D .   ? 0.18245 0.16865 0.25975 0.00160  -0.02410 -0.01790 792 HOH A O   
2553 O  O   A HOH D .   ? 0.24985 0.20785 0.33135 -0.09040 -0.10310 0.08400  793 HOH A O   
2562 O  O   A HOH D .   ? 0.30075 0.21185 0.12715 -0.07980 0.07120  -0.05160 800 HOH A O   
2570 O  O   . HOH D .   ? 0.12385 0.18725 0.16205 0.04860  -0.03010 -0.03840 806 HOH A O   
2575 O  O   A HOH D .   ? 0.11515 0.17505 0.28875 0.02540  -0.05070 -0.04830 810 HOH A O   
2583 O  O   . HOH D .   ? 0.23825 0.19585 0.30555 0.00400  -0.00210 -0.05270 816 HOH A O   
2585 O  O   A HOH D .   ? 0.24285 0.16895 0.17325 0.04470  0.05990  -0.05180 818 HOH A O   
2602 O  O   . HOH D .   ? 0.23535 0.22255 0.23935 0.01470  -0.04810 -0.09140 829 HOH A O   
2612 O  O   . HOH D .   ? 0.13985 0.17845 0.16215 -0.01800 -0.02630 -0.01740 838 HOH A O   
2620 O  O   . HOH D .   ? 0.24615 0.23215 0.35665 0.06120  0.00730  -0.06330 845 HOH A O   
2627 O  O   A HOH D .   ? 0.25585 0.20475 0.20105 -0.03150 0.03220  0.03990  851 HOH A O   
2631 O  O   A HOH D .   ? 0.27695 0.26315 0.12465 0.07160  -0.03730 -0.01990 854 HOH A O   
2634 O  O   . HOH D .   ? 0.12045 0.23515 0.20075 0.02150  0.01080  -0.09120 856 HOH A O   
2638 O  O   . HOH D .   ? 0.20775 0.21945 0.20615 0.01060  -0.02720 -0.03650 860 HOH A O   
2639 O  O   . HOH D .   ? 0.26065 0.24405 0.23685 0.06490  0.06570  0.02750  861 HOH A O   
2644 O  O   . HOH D .   ? 0.25155 0.31555 0.23095 0.10180  0.03060  -0.06330 866 HOH A O   
2646 O  O   . HOH D .   ? 0.19775 0.21765 0.15715 0.06730  0.00510  -0.04970 868 HOH A O   
2654 O  O   . HOH D .   ? 0.31625 0.23315 0.22785 -0.01430 -0.00550 -0.09120 874 HOH A O   
2665 O  O   . HOH D .   ? 0.11775 0.17225 0.19975 0.00260  -0.00070 0.02020  883 HOH A O   
2666 O  O   A HOH D .   ? 0.23405 0.19665 0.30215 -0.03290 -0.05620 -0.04350 884 HOH A O   
2678 O  O   A HOH D .   ? 0.12755 0.09285 0.18645 -0.03410 0.02230  0.01040  894 HOH A O   
2683 O  O   A HOH D .   ? 0.21785 0.22195 0.35375 -0.09480 0.09530  -0.11890 897 HOH A O   
2691 O  O   A HOH D .   ? 0.14305 0.12715 0.20905 0.02310  0.01060  0.00990  901 HOH A O   
# 
