data_8ZUR
# 
_entry.id   8ZUR 
# 
_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   8ZUR         pdb_00008zur 10.2210/pdb8zur/pdb 
WWPDB D_1300048420 ?            ?                   
# 
_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                        8ZUR 
_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' 25841.000 1   ? F99S,M153T,V163A,T203V,E222Q ? 
'Q80R was caused by a PCR error in the early study (Chalfie, M. et al., Science, 1994)' 
2 non-polymer syn 'CHLORIDE ION'              35.453    2   ? ?                            ? ? 
3 water       nat water                       18.015    406 ? ?                            ? ? 
# 
_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
GIKANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSVQSALSKDPNEKRDHMVLLQFVTAAGITH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKRH
DFFKSAMPEGYVQERTISFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYITADKQKNGI
KANFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSVQSALSKDPNEKRDHMVLLQFVTAAGITH
;
_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 'CHLORIDE ION' CL  
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 GLN n 
1 220 PHE n 
1 221 VAL n 
1 222 THR n 
1 223 ALA n 
1 224 ALA n 
1 225 GLY n 
1 226 ILE n 
1 227 THR n 
1 228 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   228 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GFP 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aequorea victoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6100 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                           'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ?                           'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                           'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                           'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION' ?                           'Cl -1'          35.453  
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 
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 GLN 219 222 222 GLN GLN A . n 
A 1 220 PHE 220 223 223 PHE PHE A . n 
A 1 221 VAL 221 224 224 VAL VAL A . n 
A 1 222 THR 222 225 225 THR THR A . n 
A 1 223 ALA 223 226 226 ALA ALA A . n 
A 1 224 ALA 224 227 227 ALA ALA A . n 
A 1 225 GLY 225 228 228 GLY GLY A . n 
A 1 226 ILE 226 229 229 ILE ILE A . n 
A 1 227 THR 227 230 230 THR THR A . n 
A 1 228 HIS 228 231 231 HIS HIS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CL  1   301 301 CL  CL  A . 
C 2 CL  1   302 302 CL  CL  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 279 680 680 HOH HOH A . 
D 3 HOH 280 681 681 HOH HOH A . 
D 3 HOH 281 682 682 HOH HOH A . 
D 3 HOH 282 683 683 HOH HOH A . 
D 3 HOH 283 684 684 HOH HOH A . 
D 3 HOH 284 685 685 HOH HOH A . 
D 3 HOH 285 686 686 HOH HOH A . 
D 3 HOH 286 687 687 HOH HOH A . 
D 3 HOH 287 688 688 HOH HOH A . 
D 3 HOH 288 689 689 HOH HOH A . 
D 3 HOH 289 690 690 HOH HOH A . 
D 3 HOH 290 691 691 HOH HOH A . 
D 3 HOH 291 692 692 HOH HOH A . 
D 3 HOH 292 693 693 HOH HOH A . 
D 3 HOH 293 694 694 HOH HOH A . 
D 3 HOH 294 695 695 HOH HOH A . 
D 3 HOH 295 696 696 HOH HOH A . 
D 3 HOH 296 697 697 HOH HOH A . 
D 3 HOH 297 698 698 HOH HOH A . 
D 3 HOH 298 699 699 HOH HOH A . 
D 3 HOH 299 700 700 HOH HOH A . 
D 3 HOH 300 701 701 HOH HOH A . 
D 3 HOH 301 702 702 HOH HOH A . 
D 3 HOH 302 703 703 HOH HOH A . 
D 3 HOH 303 704 704 HOH HOH A . 
D 3 HOH 304 705 705 HOH HOH A . 
D 3 HOH 305 706 706 HOH HOH A . 
D 3 HOH 306 707 707 HOH HOH A . 
D 3 HOH 307 708 708 HOH HOH A . 
D 3 HOH 308 709 709 HOH HOH A . 
D 3 HOH 309 710 710 HOH HOH A . 
D 3 HOH 310 711 711 HOH HOH A . 
D 3 HOH 311 712 712 HOH HOH A . 
D 3 HOH 312 713 713 HOH HOH A . 
D 3 HOH 313 714 714 HOH HOH A . 
D 3 HOH 314 715 715 HOH HOH A . 
D 3 HOH 315 716 716 HOH HOH A . 
D 3 HOH 316 717 717 HOH HOH A . 
D 3 HOH 317 718 718 HOH HOH A . 
D 3 HOH 318 719 719 HOH HOH A . 
D 3 HOH 319 720 720 HOH HOH A . 
D 3 HOH 320 721 721 HOH HOH A . 
D 3 HOH 321 722 722 HOH HOH A . 
D 3 HOH 322 723 723 HOH HOH A . 
D 3 HOH 323 724 724 HOH HOH A . 
D 3 HOH 324 725 725 HOH HOH A . 
D 3 HOH 325 726 726 HOH HOH A . 
D 3 HOH 326 727 727 HOH HOH A . 
D 3 HOH 327 728 728 HOH HOH A . 
D 3 HOH 328 729 729 HOH HOH A . 
D 3 HOH 329 730 730 HOH HOH A . 
D 3 HOH 330 731 731 HOH HOH A . 
D 3 HOH 331 732 732 HOH HOH A . 
D 3 HOH 332 733 733 HOH HOH A . 
D 3 HOH 333 734 734 HOH HOH A . 
D 3 HOH 334 735 735 HOH HOH A . 
D 3 HOH 335 736 736 HOH HOH A . 
D 3 HOH 336 737 737 HOH HOH A . 
D 3 HOH 337 738 738 HOH HOH A . 
D 3 HOH 338 739 739 HOH HOH A . 
D 3 HOH 339 740 740 HOH HOH A . 
D 3 HOH 340 741 741 HOH HOH A . 
D 3 HOH 341 742 742 HOH HOH A . 
D 3 HOH 342 743 743 HOH HOH A . 
D 3 HOH 343 744 744 HOH HOH A . 
D 3 HOH 344 745 745 HOH HOH A . 
D 3 HOH 345 746 746 HOH HOH A . 
D 3 HOH 346 747 747 HOH HOH A . 
D 3 HOH 347 748 748 HOH HOH A . 
D 3 HOH 348 749 749 HOH HOH A . 
D 3 HOH 349 750 750 HOH HOH A . 
D 3 HOH 350 751 751 HOH HOH A . 
D 3 HOH 351 752 752 HOH HOH A . 
D 3 HOH 352 753 753 HOH HOH A . 
D 3 HOH 353 754 754 HOH HOH A . 
D 3 HOH 354 755 755 HOH HOH A . 
D 3 HOH 355 756 756 HOH HOH A . 
D 3 HOH 356 757 757 HOH HOH A . 
D 3 HOH 357 758 758 HOH HOH A . 
D 3 HOH 358 759 759 HOH HOH A . 
D 3 HOH 359 760 760 HOH HOH A . 
D 3 HOH 360 761 761 HOH HOH A . 
D 3 HOH 361 762 762 HOH HOH A . 
D 3 HOH 362 763 763 HOH HOH A . 
D 3 HOH 363 764 764 HOH HOH A . 
D 3 HOH 364 765 765 HOH HOH A . 
D 3 HOH 365 766 766 HOH HOH A . 
D 3 HOH 366 767 767 HOH HOH A . 
D 3 HOH 367 768 768 HOH HOH A . 
D 3 HOH 368 769 769 HOH HOH A . 
D 3 HOH 369 770 770 HOH HOH A . 
D 3 HOH 370 771 771 HOH HOH A . 
D 3 HOH 371 772 772 HOH HOH A . 
D 3 HOH 372 773 773 HOH HOH A . 
D 3 HOH 373 774 774 HOH HOH A . 
D 3 HOH 374 775 775 HOH HOH A . 
D 3 HOH 375 776 776 HOH HOH A . 
D 3 HOH 376 777 777 HOH HOH A . 
D 3 HOH 377 778 778 HOH HOH A . 
D 3 HOH 378 779 779 HOH HOH A . 
D 3 HOH 379 780 780 HOH HOH A . 
D 3 HOH 380 781 781 HOH HOH A . 
D 3 HOH 381 782 782 HOH HOH A . 
D 3 HOH 382 783 783 HOH HOH A . 
D 3 HOH 383 784 784 HOH HOH A . 
D 3 HOH 384 785 785 HOH HOH A . 
D 3 HOH 385 786 786 HOH HOH A . 
D 3 HOH 386 787 787 HOH HOH A . 
D 3 HOH 387 788 788 HOH HOH A . 
D 3 HOH 388 789 789 HOH HOH A . 
D 3 HOH 389 790 790 HOH HOH A . 
D 3 HOH 390 791 791 HOH HOH A . 
D 3 HOH 391 792 792 HOH HOH A . 
D 3 HOH 392 793 793 HOH HOH A . 
D 3 HOH 393 794 794 HOH HOH A . 
D 3 HOH 394 795 795 HOH HOH A . 
D 3 HOH 395 796 796 HOH HOH A . 
D 3 HOH 396 797 797 HOH HOH A . 
D 3 HOH 397 798 798 HOH HOH A . 
D 3 HOH 398 799 799 HOH HOH A . 
D 3 HOH 399 800 800 HOH HOH A . 
D 3 HOH 400 801 801 HOH HOH A . 
D 3 HOH 401 802 802 HOH HOH A . 
D 3 HOH 402 803 803 HOH HOH A . 
D 3 HOH 403 804 804 HOH HOH A . 
D 3 HOH 404 805 805 HOH HOH A . 
D 3 HOH 405 806 806 HOH HOH A . 
D 3 HOH 406 807 807 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 156 ? CE  ? A LYS 153 CE  
2 1 Y 1 A LYS 156 ? NZ  ? A LYS 153 NZ  
3 1 Y 1 A HIS 231 ? CG  ? A HIS 228 CG  
4 1 Y 1 A HIS 231 ? ND1 ? A HIS 228 ND1 
5 1 Y 1 A HIS 231 ? CD2 ? A HIS 228 CD2 
6 1 Y 1 A HIS 231 ? CE1 ? A HIS 228 CE1 
7 1 Y 1 A HIS 231 ? NE2 ? A HIS 228 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.19.2_4158 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
# 
_cell.volume             204374.624 
_cell.length_a           51.500 
_cell.length_b           57.790 
_cell.length_c           68.670 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.angle_alpha        90.000 
_cell.entry_id           8ZUR 
_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                         8ZUR 
_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                   8ZUR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.79 
_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         2023-05-15 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.70 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SPRING-8 BEAMLINE BL41XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.70 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL41XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          11.34 
_reflns.entry_id                                       8ZUR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.2 
_reflns.d_resolution_low                               44.22 
_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                                     64730 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.71 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.78 
_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                                0.094 
_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                              0.087 
_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                           1.99 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9968 
_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                               6.42 
_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                               0.869 
_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                                  0.770 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.798 
_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                 4.98 
_refine.pdbx_overall_phase_error                 15.2979 
_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                          0.1305 
_refine.B_iso_mean                               16.18 
_refine.ls_number_reflns_R_free                  3226 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_R_factor_R_work                       0.1287 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_d_res_high                            1.20 
_refine.ls_number_reflns_obs                     64720 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.ls_number_reflns_R_work                  61494 
_refine.ls_d_res_low                             41.20 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.ls_R_factor_R_free                       0.1662 
_refine.overall_SU_ML                            0.1057 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.entry_id                                 8ZUR 
_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        1816 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.number_atoms_solvent             406 
_refine_hist.number_atoms_total               2224 
_refine_hist.d_res_high                       1.20 
_refine_hist.d_res_low                        41.20 
# 
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           2106 0.0141  ? ? ? 
'X-RAY DIFFRACTION' f_angle_d          2895 1.3430  ? ? ? 
'X-RAY DIFFRACTION' f_chiral_restr     317  0.1139  ? ? ? 
'X-RAY DIFFRACTION' f_plane_restr      386  0.0121  ? ? ? 
'X-RAY DIFFRACTION' f_dihedral_angle_d 829  13.3337 ? ? ? 
# 
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  2614 0.2041 99.96  0.2571 137 . . . . . . . 
'X-RAY DIFFRACTION' 1.22 1.24  2621 0.1975 99.96  0.2221 135 . . . . . . . 
'X-RAY DIFFRACTION' 1.24 1.26  2663 0.1808 99.96  0.1927 138 . . . . . . . 
'X-RAY DIFFRACTION' 1.26 1.28  2642 0.1701 99.93  0.2198 136 . . . . . . . 
'X-RAY DIFFRACTION' 1.28 1.30  2642 0.1659 100.00 0.2233 130 . . . . . . . 
'X-RAY DIFFRACTION' 1.30 1.33  2650 0.1639 100.00 0.2255 137 . . . . . . . 
'X-RAY DIFFRACTION' 1.33 1.35  2649 0.1565 99.96  0.1904 142 . . . . . . . 
'X-RAY DIFFRACTION' 1.35 1.38  2658 0.1595 100.00 0.1935 153 . . . . . . . 
'X-RAY DIFFRACTION' 1.38 1.42  2608 0.1414 100.00 0.2031 138 . . . . . . . 
'X-RAY DIFFRACTION' 1.42 1.45  2655 0.1314 100.00 0.1906 139 . . . . . . . 
'X-RAY DIFFRACTION' 1.45 1.49  2656 0.1183 100.00 0.1757 146 . . . . . . . 
'X-RAY DIFFRACTION' 1.49 1.53  2652 0.1115 100.00 0.1604 140 . . . . . . . 
'X-RAY DIFFRACTION' 1.53 1.58  2651 0.1143 99.96  0.1513 145 . . . . . . . 
'X-RAY DIFFRACTION' 1.58 1.64  2669 0.1096 100.00 0.1704 152 . . . . . . . 
'X-RAY DIFFRACTION' 1.64 1.71  2672 0.1131 100.00 0.1391 131 . . . . . . . 
'X-RAY DIFFRACTION' 1.71 1.78  2651 0.1174 100.00 0.1529 157 . . . . . . . 
'X-RAY DIFFRACTION' 1.78 1.88  2672 0.1126 99.96  0.1540 145 . . . . . . . 
'X-RAY DIFFRACTION' 1.88 2.00  2709 0.1060 100.00 0.1186 123 . . . . . . . 
'X-RAY DIFFRACTION' 2.00 2.15  2734 0.1098 100.00 0.1516 111 . . . . . . . 
'X-RAY DIFFRACTION' 2.15 2.37  2670 0.1231 100.00 0.1594 165 . . . . . . . 
'X-RAY DIFFRACTION' 2.37 2.71  2732 0.1284 100.00 0.1897 122 . . . . . . . 
'X-RAY DIFFRACTION' 2.71 3.41  2754 0.1278 100.00 0.1480 152 . . . . . . . 
'X-RAY DIFFRACTION' 3.41 41.20 2870 0.1344 99.83  0.1644 152 . . . . . . . 
# 
_struct.entry_id                     8ZUR 
_struct.title                        'Crystal structure of the F99S/M153T/V163A/T203V/E222Q variant of GFP at pH 5.0' 
_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        8ZUR 
_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              8ZUR 
_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 8ZUR GYS A 64  ? UNP P42212 SER 65  chromophore           66  1 
1 8ZUR GYS A 64  ? UNP P42212 TYR 66  chromophore           66  2 
1 8ZUR GYS A 64  ? UNP P42212 GLY 67  chromophore           66  3 
1 8ZUR ARG A 77  ? UNP P42212 GLN 80  conflict              80  4 
1 8ZUR SER A 96  ? UNP P42212 PHE 99  'engineered mutation' 99  5 
1 8ZUR THR A 150 ? UNP P42212 MET 153 'engineered mutation' 153 6 
1 8ZUR ALA A 160 ? UNP P42212 VAL 163 'engineered mutation' 163 7 
1 8ZUR VAL A 200 ? UNP P42212 THR 203 'engineered mutation' 203 8 
1 8ZUR GLN A 219 ? UNP P42212 GLU 222 'engineered mutation' 222 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 140   ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  10200 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 3  ? THR A 8  ? GLY A 4  THR A 9  5 ? 6 
HELX_P HELX_P2 AA2 ALA A 36 ? TYR A 38 ? ALA A 37 TYR A 39 5 ? 3 
HELX_P HELX_P3 AA3 PRO A 55 ? VAL A 60 ? PRO A 56 VAL A 61 5 ? 6 
HELX_P HELX_P4 AA4 VAL A 65 ? SER A 69 ? VAL A 68 SER A 72 5 ? 5 
HELX_P HELX_P5 AA5 PRO A 72 ? HIS A 78 ? PRO A 75 HIS A 81 5 ? 7 
HELX_P HELX_P6 AA6 ASP A 79 ? ALA A 84 ? ASP A 82 ALA A 87 1 ? 6 
# 
_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 ? ? ? ? ? ? ? 1.342 ? ? 
covale2 covale both ? A GYS 64 C3 ? ? ? 1_555 A VAL 65 N  ? ? A GYS 66 A VAL 68 1_555 ? ? ? ? ? ? ? 1.319 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_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       9.37 
# 
_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 GLY A 19  ? N GLY A 20  O PHE A 26  ? O PHE A 27  
AA1 2  3  N SER A 29  ? N SER A 30  O ILE A 46  ? O ILE A 47  
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 HIS A 196 ? O HIS A 199 N ILE A 149 ? N ILE A 152 
AA1 6  7  N ASP A 152 ? N ASP A 155 O GLY A 157 ? O GLY A 160 
AA1 7  8  N HIS A 166 ? N HIS A 169 O GLN A 174 ? O GLN A 177 
AA1 8  9  O THR A 183 ? O THR A 186 N VAL A 90  ? N VAL A 93  
AA1 9  10 N ILE A 95  ? N ILE A 98  O TYR A 103 ? O TYR A 106 
AA1 10 11 N LYS A 110 ? N LYS A 113 O VAL A 117 ? O VAL A 120 
AA1 11 12 O GLY A 124 ? O GLY A 127 N ASP A 20  ? N ASP A 21  
# 
_pdbx_entry_details.entry_id                   8ZUR 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 THR A 230 ? A -149.94 -35.44  
2 1 THR A 230 ? B 83.38   -108.66 
# 
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 466 ? 5.88 . 
2 1 O ? A HOH 579 ? 6.85 . 
3 1 O ? A HOH 781 ? 6.19 . 
# 
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  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
GYS N1   N  N N 138 
GYS OG1  O  N N 139 
GYS CB1  C  N N 140 
GYS CA1  C  N R 141 
GYS C1   C  N N 142 
GYS N2   N  N N 143 
GYS N3   N  N N 144 
GYS C2   C  N N 145 
GYS O2   O  N N 146 
GYS CA2  C  N N 147 
GYS CA3  C  N N 148 
GYS CB2  C  N N 149 
GYS CG2  C  Y N 150 
GYS CD1  C  Y N 151 
GYS CD2  C  Y N 152 
GYS CE1  C  Y N 153 
GYS CE2  C  Y N 154 
GYS CZ   C  Y N 155 
GYS OH   O  N N 156 
GYS C3   C  N N 157 
GYS O3   O  N N 158 
GYS OXT  O  N N 159 
GYS H    H  N N 160 
GYS H2   H  N N 161 
GYS HA1  H  N N 162 
GYS HB11 H  N N 163 
GYS HB12 H  N N 164 
GYS HG1  H  N N 165 
GYS HB2  H  N N 166 
GYS HD2  H  N N 167 
GYS HE2  H  N N 168 
GYS HOH  H  N N 169 
GYS HE1  H  N N 170 
GYS HD1  H  N N 171 
GYS HA31 H  N N 172 
GYS HA32 H  N N 173 
GYS HXT  H  N N 174 
HIS N    N  N N 175 
HIS CA   C  N S 176 
HIS C    C  N N 177 
HIS O    O  N N 178 
HIS CB   C  N N 179 
HIS CG   C  Y N 180 
HIS ND1  N  Y N 181 
HIS CD2  C  Y N 182 
HIS CE1  C  Y N 183 
HIS NE2  N  Y N 184 
HIS OXT  O  N N 185 
HIS H    H  N N 186 
HIS H2   H  N N 187 
HIS HA   H  N N 188 
HIS HB2  H  N N 189 
HIS HB3  H  N N 190 
HIS HD1  H  N N 191 
HIS HD2  H  N N 192 
HIS HE1  H  N N 193 
HIS HE2  H  N N 194 
HIS HXT  H  N N 195 
HOH O    O  N N 196 
HOH H1   H  N N 197 
HOH H2   H  N N 198 
ILE N    N  N N 199 
ILE CA   C  N S 200 
ILE C    C  N N 201 
ILE O    O  N N 202 
ILE CB   C  N S 203 
ILE CG1  C  N N 204 
ILE CG2  C  N N 205 
ILE CD1  C  N N 206 
ILE OXT  O  N N 207 
ILE H    H  N N 208 
ILE H2   H  N N 209 
ILE HA   H  N N 210 
ILE HB   H  N N 211 
ILE HG12 H  N N 212 
ILE HG13 H  N N 213 
ILE HG21 H  N N 214 
ILE HG22 H  N N 215 
ILE HG23 H  N N 216 
ILE HD11 H  N N 217 
ILE HD12 H  N N 218 
ILE HD13 H  N N 219 
ILE HXT  H  N N 220 
LEU N    N  N N 221 
LEU CA   C  N S 222 
LEU C    C  N N 223 
LEU O    O  N N 224 
LEU CB   C  N N 225 
LEU CG   C  N N 226 
LEU CD1  C  N N 227 
LEU CD2  C  N N 228 
LEU OXT  O  N N 229 
LEU H    H  N N 230 
LEU H2   H  N N 231 
LEU HA   H  N N 232 
LEU HB2  H  N N 233 
LEU HB3  H  N N 234 
LEU HG   H  N N 235 
LEU HD11 H  N N 236 
LEU HD12 H  N N 237 
LEU HD13 H  N N 238 
LEU HD21 H  N N 239 
LEU HD22 H  N N 240 
LEU HD23 H  N N 241 
LEU HXT  H  N N 242 
LYS N    N  N N 243 
LYS CA   C  N S 244 
LYS C    C  N N 245 
LYS O    O  N N 246 
LYS CB   C  N N 247 
LYS CG   C  N N 248 
LYS CD   C  N N 249 
LYS CE   C  N N 250 
LYS NZ   N  N N 251 
LYS OXT  O  N N 252 
LYS H    H  N N 253 
LYS H2   H  N N 254 
LYS HA   H  N N 255 
LYS HB2  H  N N 256 
LYS HB3  H  N N 257 
LYS HG2  H  N N 258 
LYS HG3  H  N N 259 
LYS HD2  H  N N 260 
LYS HD3  H  N N 261 
LYS HE2  H  N N 262 
LYS HE3  H  N N 263 
LYS HZ1  H  N N 264 
LYS HZ2  H  N N 265 
LYS HZ3  H  N N 266 
LYS HXT  H  N N 267 
MET N    N  N N 268 
MET CA   C  N S 269 
MET C    C  N N 270 
MET O    O  N N 271 
MET CB   C  N N 272 
MET CG   C  N N 273 
MET SD   S  N N 274 
MET CE   C  N N 275 
MET OXT  O  N N 276 
MET H    H  N N 277 
MET H2   H  N N 278 
MET HA   H  N N 279 
MET HB2  H  N N 280 
MET HB3  H  N N 281 
MET HG2  H  N N 282 
MET HG3  H  N N 283 
MET HE1  H  N N 284 
MET HE2  H  N N 285 
MET HE3  H  N N 286 
MET HXT  H  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                    8ZUR 
_atom_sites.fract_transf_matrix[1][1]   0.019417 
_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]   0.017304 
_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]   0.014562 
_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  
CL 
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   . SER A 1 1   ? -6.33700  22.65800  83.32300 1.000 16.21980 ? 2   SER A N   1 
ATOM   2    C  CA  A SER A 1 1   ? -5.52400  22.03000  84.36300 0.670 15.40128 ? 2   SER A CA  1 
ATOM   3    C  CA  B SER A 1 1   ? -5.54300  21.98800  84.35600 0.330 16.05996 ? 2   SER A CA  1 
ATOM   4    C  C   . SER A 1 1   ? -4.22800  21.46400  83.77800 1.000 14.84858 ? 2   SER A C   1 
ATOM   5    O  O   . SER A 1 1   ? -4.03100  21.44800  82.54100 1.000 14.73278 ? 2   SER A O   1 
ATOM   6    C  CB  A SER A 1 1   ? -6.34100  20.95300  85.08900 0.670 15.10388 ? 2   SER A CB  1 
ATOM   7    C  CB  B SER A 1 1   ? -6.32700  20.82900  84.99100 0.330 17.82996 ? 2   SER A CB  1 
ATOM   8    O  OG  A SER A 1 1   ? -6.71800  19.92400  84.18200 0.670 15.06966 ? 2   SER A OG  1 
ATOM   9    O  OG  B SER A 1 1   ? -7.67000  21.17600  85.26900 0.330 16.64996 ? 2   SER A OG  1 
ATOM   10   N  N   . LYS A 1 2   ? -3.33300  21.02300  84.65200 1.000 14.42748 ? 3   LYS A N   1 
ATOM   11   C  CA  . LYS A 1 2   ? -2.02700  20.51700  84.20300 1.000 13.28524 ? 3   LYS A CA  1 
ATOM   12   C  C   . LYS A 1 2   ? -2.19300  19.42900  83.16500 1.000 11.92981 ? 3   LYS A C   1 
ATOM   13   O  O   . LYS A 1 2   ? -2.99600  18.49800  83.34400 1.000 13.15101 ? 3   LYS A O   1 
ATOM   14   C  CB  . LYS A 1 2   ? -1.23400  19.96200  85.39100 1.000 13.39578 ? 3   LYS A CB  1 
ATOM   15   C  CG  . LYS A 1 2   ? 0.13500   19.43600  84.99900 1.000 12.97731 ? 3   LYS A CG  1 
ATOM   16   C  CD  . LYS A 1 2   ? 0.96500   18.95200  86.20000 1.000 14.08797 ? 3   LYS A CD  1 
ATOM   17   C  CE  . LYS A 1 2   ? 2.37700   18.56200  85.78800 1.000 13.34051 ? 3   LYS A CE  1 
ATOM   18   N  NZ  . LYS A 1 2   ? 2.38500   17.21700  85.00500 1.000 13.33788 ? 3   LYS A NZ  1 
ATOM   19   N  N   . GLY A 1 3   ? -1.41300  19.52600  82.10300 1.000 12.49830 ? 4   GLY A N   1 
ATOM   20   C  CA  . GLY A 1 3   ? -1.38700  18.46300  81.11100 1.000 12.43777 ? 4   GLY A CA  1 
ATOM   21   C  C   . GLY A 1 3   ? -2.56100  18.56800  80.15500 1.000 12.47988 ? 4   GLY A C   1 
ATOM   22   O  O   . GLY A 1 3   ? -2.34800  18.66900  78.94300 1.000 13.34577 ? 4   GLY A O   1 
ATOM   23   N  N   . GLU A 1 4   ? -3.80700  18.51600  80.66200 1.000 13.03521 ? 5   GLU A N   1 
ATOM   24   C  CA  A GLU A 1 4   ? -4.91800  18.55900  79.72600 0.590 13.32208 ? 5   GLU A CA  1 
ATOM   25   C  CA  B GLU A 1 4   ? -5.01200  18.63100  79.84600 0.410 13.17996 ? 5   GLU A CA  1 
ATOM   26   C  C   . GLU A 1 4   ? -4.93900  19.84700  78.91800 1.000 12.63253 ? 5   GLU A C   1 
ATOM   27   O  O   . GLU A 1 4   ? -5.36800  19.82600  77.76200 1.000 13.08521 ? 5   GLU A O   1 
ATOM   28   C  CB  A GLU A 1 4   ? -6.24400  18.32400  80.41900 0.590 14.65645 ? 5   GLU A CB  1 
ATOM   29   C  CB  B GLU A 1 4   ? -6.16200  18.75400  80.85300 0.410 16.10996 ? 5   GLU A CB  1 
ATOM   30   C  CG  A GLU A 1 4   ? -6.70800  19.40700  81.32200 0.590 15.03282 ? 5   GLU A CG  1 
ATOM   31   C  CG  B GLU A 1 4   ? -7.51500  19.08300  80.29700 0.410 11.60996 ? 5   GLU A CG  1 
ATOM   32   C  CD  A GLU A 1 4   ? -7.38400  20.54400  80.58000 0.590 16.16453 ? 5   GLU A CD  1 
ATOM   33   C  CD  B GLU A 1 4   ? -7.70700  20.58500  80.07200 0.410 22.85996 ? 5   GLU A CD  1 
ATOM   34   O  OE1 A GLU A 1 4   ? -8.02800  20.27600  79.53800 0.590 17.19886 ? 5   GLU A OE1 1 
ATOM   35   O  OE1 B GLU A 1 4   ? -6.91200  21.37600  80.62900 0.410 26.27996 ? 5   GLU A OE1 1 
ATOM   36   O  OE2 A GLU A 1 4   ? -7.24600  21.70200  81.01600 0.590 16.03820 ? 5   GLU A OE2 1 
ATOM   37   O  OE2 B GLU A 1 4   ? -8.63200  20.97300  79.31300 0.410 24.56996 ? 5   GLU A OE2 1 
ATOM   38   N  N   . GLU A 1 5   ? -4.40900  20.94200  79.43600 1.000 12.65358 ? 6   GLU A N   1 
ATOM   39   C  CA  . GLU A 1 5   ? -4.36700  22.19000  78.68200 1.000 13.53000 ? 6   GLU A CA  1 
ATOM   40   C  C   . GLU A 1 5   ? -3.48500  22.08300  77.42400 1.000 12.67201 ? 6   GLU A C   1 
ATOM   41   O  O   . GLU A 1 5   ? -3.62000  22.90600  76.52300 1.000 14.54591 ? 6   GLU A O   1 
ATOM   42   C  CB  . GLU A 1 5   ? -3.83900  23.31800  79.59800 1.000 14.87227 ? 6   GLU A CB  1 
ATOM   43   C  CG  . GLU A 1 5   ? -2.38500  23.04700  80.02000 1.000 16.29349 ? 6   GLU A CG  1 
ATOM   44   C  CD  . GLU A 1 5   ? -1.83800  24.08600  80.97700 1.000 19.60178 ? 6   GLU A CD  1 
ATOM   45   O  OE1 . GLU A 1 5   ? -2.58000  25.02800  81.34400 1.000 22.39686 ? 6   GLU A OE1 1 
ATOM   46   O  OE2 . GLU A 1 5   ? -0.64900  24.00400  81.32800 1.000 20.82298 ? 6   GLU A OE2 1 
ATOM   47   N  N   . LEU A 1 6   ? -2.61200  21.08700  77.34900 1.000 12.31933 ? 7   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 6   ? -1.71500  20.90400  76.21300 1.000 12.82992 ? 7   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 6   ? -2.41500  20.20800  75.06000 1.000 12.40618 ? 7   LEU A C   1 
ATOM   50   O  O   . LEU A 1 6   ? -1.80400  20.05900  73.99000 1.000 13.43262 ? 7   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 6   ? -0.49100  20.07400  76.63400 1.000 12.95362 ? 7   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 6   ? 0.31700   20.69700  77.79900 1.000 13.61686 ? 7   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 6   ? 1.44800   19.78500  78.25300 1.000 15.26179 ? 7   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 6   ? 0.81900   22.13500  77.51500 1.000 15.33812 ? 7   LEU A CD2 1 
ATOM   55   N  N   . PHE A 1 7   ? -3.65500  19.75700  75.25900 1.000 12.94046 ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 7   ? -4.33300  18.90900  74.27700 1.000 12.05351 ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 7   ? -5.57100  19.56100  73.71300 1.000 12.83255 ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 7   ? -6.30700  18.90000  72.97900 1.000 14.06691 ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 7   ? -4.68500  17.55900  74.91300 1.000 12.20353 ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 7   ? -3.49600  16.72500  75.21800 1.000 10.66387 ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 7   ? -2.95200  15.87100  74.26100 1.000 11.41922 ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 7   ? -2.88100  16.80400  76.45400 1.000 11.40606 ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 7   ? -1.82900  15.11300  74.50900 1.000 11.41396 ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 7   ? -1.76000  15.99500  76.71900 1.000 11.25341 ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 7   ? -1.22800  15.16100  75.74000 1.000 11.57187 ? 8   PHE A CZ  1 
ATOM   66   N  N   . THR A 1 8   ? -5.77800  20.85800  73.95500 1.000 13.88268 ? 9   THR A N   1 
ATOM   67   C  CA  . THR A 1 8   ? -6.98600  21.49800  73.45300 1.000 15.54603 ? 9   THR A CA  1 
ATOM   68   C  C   . THR A 1 8   ? -6.97200  21.67900  71.93400 1.000 15.78027 ? 9   THR A C   1 
ATOM   69   O  O   . THR A 1 8   ? -8.03900  21.88400  71.33600 1.000 16.55931 ? 9   THR A O   1 
ATOM   70   C  CB  . THR A 1 8   ? -7.19100  22.80900  74.18500 1.000 19.52283 ? 9   THR A CB  1 
ATOM   71   O  OG1 . THR A 1 8   ? -6.03700  23.57600  73.95300 1.000 22.29421 ? 9   THR A OG1 1 
ATOM   72   C  CG2 . THR A 1 8   ? -7.28100  22.57700  75.64100 1.000 20.53874 ? 9   THR A CG2 1 
ATOM   73   N  N   . GLY A 1 9   ? -5.80200  21.64900  71.30800 1.000 15.34864 ? 10  GLY A N   1 
ATOM   74   C  CA  . GLY A 1 9   ? -5.67500  21.79400  69.87600 1.000 15.45392 ? 10  GLY A CA  1 
ATOM   75   C  C   . GLY A 1 9   ? -5.16400  20.50500  69.24600 1.000 14.22746 ? 10  GLY A C   1 
ATOM   76   O  O   . GLY A 1 9   ? -5.14600  19.44300  69.86100 1.000 13.86425 ? 10  GLY A O   1 
ATOM   77   N  N   . VAL A 1 10  ? -4.73100  20.60800  67.99500 1.000 14.30641 ? 11  VAL A N   1 
ATOM   78   C  CA  . VAL A 1 10  ? -4.11600  19.47800  67.29300 1.000 14.21693 ? 11  VAL A CA  1 
ATOM   79   C  C   . VAL A 1 10  ? -2.65500  19.41300  67.69300 1.000 13.86952 ? 11  VAL A C   1 
ATOM   80   O  O   . VAL A 1 10  ? -1.92700  20.40900  67.59600 1.000 16.28297 ? 11  VAL A O   1 
ATOM   81   C  CB  . VAL A 1 10  ? -4.26100  19.65800  65.76700 1.000 15.53288 ? 11  VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 10  ? -3.55200  18.53600  65.03200 1.000 16.09610 ? 11  VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 10  ? -5.71100  19.65600  65.41500 1.000 15.96187 ? 11  VAL A CG2 1 
ATOM   84   N  N   . VAL A 1 11  ? -2.20300  18.23000  68.10800 1.000 11.82717 ? 12  VAL A N   1 
ATOM   85   C  CA  . VAL A 1 11  ? -0.85800  18.02900  68.64100 1.000 11.40343 ? 12  VAL A CA  1 
ATOM   86   C  C   . VAL A 1 11  ? -0.09200  17.07900  67.72500 1.000 11.16656 ? 12  VAL A C   1 
ATOM   87   O  O   . VAL A 1 11  ? -0.58600  15.98900  67.43300 1.000 11.34553 ? 12  VAL A O   1 
ATOM   88   C  CB  . VAL A 1 11  ? -0.89900  17.45000  70.07100 1.000 11.55082 ? 12  VAL A CB  1 
ATOM   89   C  CG1 . VAL A 1 11  ? 0.51100   17.14900  70.55200 1.000 12.13247 ? 12  VAL A CG1 1 
ATOM   90   C  CG2 . VAL A 1 11  ? -1.65500  18.43400  70.98900 1.000 12.24827 ? 12  VAL A CG2 1 
ATOM   91   N  N   . PRO A 1 12  ? 1.11600   17.43500  67.24600 1.000 11.14288 ? 13  PRO A N   1 
ATOM   92   C  CA  . PRO A 1 12  ? 1.91000   16.46500  66.45500 1.000 11.30342 ? 13  PRO A CA  1 
ATOM   93   C  C   . PRO A 1 12  ? 2.38300   15.31700  67.31900 1.000 10.21382 ? 13  PRO A C   1 
ATOM   94   O  O   . PRO A 1 12  ? 2.67900   15.47000  68.51100 1.000 11.30605 ? 13  PRO A O   1 
ATOM   95   C  CB  . PRO A 1 12  ? 3.11100   17.26900  65.96200 1.000 13.25629 ? 13  PRO A CB  1 
ATOM   96   C  CG  . PRO A 1 12  ? 3.16400   18.44700  66.79000 1.000 15.68816 ? 13  PRO A CG  1 
ATOM   97   C  CD  . PRO A 1 12  ? 1.85000   18.68100  67.50100 1.000 12.75886 ? 13  PRO A CD  1 
ATOM   98   N  N   . ILE A 1 13  ? 2.45000   14.14200  66.70000 1.000 10.16381 ? 14  ILE A N   1 
ATOM   99   C  CA  . ILE A 1 13  ? 2.83200   12.90400  67.37800 1.000 10.01379 ? 14  ILE A CA  1 
ATOM   100  C  C   . ILE A 1 13  ? 3.99000   12.24800  66.64900 1.000 9.80850  ? 14  ILE A C   1 
ATOM   101  O  O   . ILE A 1 13  ? 4.02900   12.22900  65.40800 1.000 10.50596 ? 14  ILE A O   1 
ATOM   102  C  CB  . ILE A 1 13  ? 1.64600   11.91800  67.40800 1.000 9.79008  ? 14  ILE A CB  1 
ATOM   103  C  CG1 . ILE A 1 13  ? 0.44500   12.49100  68.17800 1.000 10.72704 ? 14  ILE A CG1 1 
ATOM   104  C  CG2 . ILE A 1 13  ? 2.07300   10.57900  68.04200 1.000 10.11117 ? 14  ILE A CG2 1 
ATOM   105  C  CD1 . ILE A 1 13  ? -0.86300  11.71400  67.97800 1.000 10.44016 ? 14  ILE A CD1 1 
ATOM   106  N  N   . LEU A 1 14  ? 4.90900   11.67700  67.42800 1.000 9.72955  ? 15  LEU A N   1 
ATOM   107  C  CA  A LEU A 1 14  ? 5.98000   10.83200  66.89700 0.680 9.51110  ? 15  LEU A CA  1 
ATOM   108  C  CA  B LEU A 1 14  ? 5.97500   10.84400  66.89800 0.320 8.09996  ? 15  LEU A CA  1 
ATOM   109  C  C   . LEU A 1 14  ? 5.95300   9.52800   67.65700 1.000 9.00578  ? 15  LEU A C   1 
ATOM   110  O  O   . LEU A 1 14  ? 5.86900   9.52200   68.88600 1.000 10.15591 ? 15  LEU A O   1 
ATOM   111  C  CB  A LEU A 1 14  ? 7.36800   11.42500  67.09800 0.680 10.16907 ? 15  LEU A CB  1 
ATOM   112  C  CB  B LEU A 1 14  ? 7.31100   11.55500  67.07800 0.320 12.97996 ? 15  LEU A CB  1 
ATOM   113  C  CG  A LEU A 1 14  ? 7.61200   12.64900  66.28100 0.680 11.12972 ? 15  LEU A CG  1 
ATOM   114  C  CG  B LEU A 1 14  ? 8.49200   11.00900  66.31300 0.320 12.73996 ? 15  LEU A CG  1 
ATOM   115  C  CD1 A LEU A 1 14  ? 8.93200   13.29100  66.79600 0.680 12.16405 ? 15  LEU A CD1 1 
ATOM   116  C  CD1 B LEU A 1 14  ? 8.30800   11.14800  64.80600 0.320 11.74996 ? 15  LEU A CD1 1 
ATOM   117  C  CD2 A LEU A 1 14  ? 7.67500   12.32000  64.78100 0.680 12.31670 ? 15  LEU A CD2 1 
ATOM   118  C  CD2 B LEU A 1 14  ? 9.69600   11.77300  66.75100 0.320 10.39996 ? 15  LEU A CD2 1 
ATOM   119  N  N   . VAL A 1 15  ? 6.01400   8.42000   66.92800 1.000 9.17422  ? 16  VAL A N   1 
ATOM   120  C  CA  . VAL A 1 15  ? 6.07500   7.08600   67.51900 1.000 9.89009  ? 16  VAL A CA  1 
ATOM   121  C  C   . VAL A 1 15  ? 7.37000   6.43100   67.05500 1.000 9.95589  ? 16  VAL A C   1 
ATOM   122  O  O   . VAL A 1 15  ? 7.69700   6.47900   65.87200 1.000 10.12433 ? 16  VAL A O   1 
ATOM   123  C  CB  . VAL A 1 15  ? 4.83800   6.23200   67.12600 1.000 10.04538 ? 16  VAL A CB  1 
ATOM   124  C  CG1 . VAL A 1 15  ? 4.92900   4.82600   67.77400 1.000 10.55333 ? 16  VAL A CG1 1 
ATOM   125  C  CG2 . VAL A 1 15  ? 3.52700   6.97900   67.53800 1.000 10.33225 ? 16  VAL A CG2 1 
ATOM   126  N  N   . GLU A 1 16  ? 8.08500   5.76800   67.95100 1.000 9.48741  ? 17  GLU A N   1 
ATOM   127  C  CA  . GLU A 1 16  ? 9.31500   5.08600   67.56200 1.000 9.55584  ? 17  GLU A CA  1 
ATOM   128  C  C   . GLU A 1 16  ? 9.35300   3.77200   68.31400 1.000 9.04262  ? 17  GLU A C   1 
ATOM   129  O  O   . GLU A 1 16  ? 9.29600   3.76100   69.54900 1.000 11.74032 ? 17  GLU A O   1 
ATOM   130  C  CB  . GLU A 1 16  ? 10.54000  5.92600   67.91500 1.000 11.60609 ? 17  GLU A CB  1 
ATOM   131  C  CG  . GLU A 1 16  ? 10.47900  7.33600   67.30300 1.000 13.79319 ? 17  GLU A CG  1 
ATOM   132  C  CD  . GLU A 1 16  ? 10.55300  7.40800   65.79600 1.000 16.21454 ? 17  GLU A CD  1 
ATOM   133  O  OE1 . GLU A 1 16  ? 11.01000  6.50400   65.12300 1.000 15.81712 ? 17  GLU A OE1 1 
ATOM   134  O  OE2 . GLU A 1 16  ? 10.20600  8.51100   65.28600 1.000 17.87789 ? 17  GLU A OE2 1 
ATOM   135  N  N   . LEU A 1 17  ? 9.43200   2.66200   67.59600 1.000 9.50057  ? 18  LEU A N   1 
ATOM   136  C  CA  . LEU A 1 17  ? 9.44700   1.33900   68.19900 1.000 9.27949  ? 18  LEU A CA  1 
ATOM   137  C  C   . LEU A 1 17  ? 10.64200  0.52600   67.70800 1.000 9.58743  ? 18  LEU A C   1 
ATOM   138  O  O   . LEU A 1 17  ? 10.91100  0.46000   66.49600 1.000 10.25593 ? 18  LEU A O   1 
ATOM   139  C  CB  . LEU A 1 17  ? 8.14100   0.60100   67.84000 1.000 9.94010  ? 18  LEU A CB  1 
ATOM   140  C  CG  . LEU A 1 17  ? 8.03600   -0.84000  68.40500 1.000 9.80850  ? 18  LEU A CG  1 
ATOM   141  C  CD1 . LEU A 1 17  ? 6.58600   -1.15400  68.85800 1.000 10.99286 ? 18  LEU A CD1 1 
ATOM   142  C  CD2 . LEU A 1 17  ? 8.53900   -1.86800  67.39900 1.000 11.29553 ? 18  LEU A CD2 1 
ATOM   143  N  N   . ASP A 1 18  ? 11.33200  -0.09700  68.67000 1.000 9.40583  ? 19  ASP A N   1 
ATOM   144  C  CA  A ASP A 1 18  ? 12.34800  -1.11500  68.42800 0.550 10.72967 ? 19  ASP A CA  1 
ATOM   145  C  CA  B ASP A 1 18  ? 12.30700  -1.13500  68.35500 0.450 10.02996 ? 19  ASP A CA  1 
ATOM   146  C  C   . ASP A 1 18  ? 11.75400  -2.44700  68.85500 1.000 10.08749 ? 19  ASP A C   1 
ATOM   147  O  O   . ASP A 1 18  ? 11.29900  -2.55600  69.99900 1.000 11.09813 ? 19  ASP A O   1 
ATOM   148  C  CB  A ASP A 1 18  ? 13.56000  -0.81600  69.32000 0.550 13.81951 ? 19  ASP A CB  1 
ATOM   149  C  CB  B ASP A 1 18  ? 13.68800  -0.89700  68.96800 0.450 12.02996 ? 19  ASP A CB  1 
ATOM   150  C  CG  A ASP A 1 18  ? 14.62000  -1.81500  69.14500 0.550 17.38310 ? 19  ASP A CG  1 
ATOM   151  C  CG  B ASP A 1 18  ? 14.41100  0.25500   68.32700 0.450 20.35996 ? 19  ASP A CG  1 
ATOM   152  O  OD1 A ASP A 1 18  ? 15.28400  -1.74700  68.10800 0.550 18.82274 ? 19  ASP A OD1 1 
ATOM   153  O  OD1 B ASP A 1 18  ? 14.21700  0.51100   67.11500 0.450 14.71996 ? 19  ASP A OD1 1 
ATOM   154  O  OD2 A ASP A 1 18  ? 14.74400  -2.67600  70.00000 0.550 19.44913 ? 19  ASP A OD2 1 
ATOM   155  O  OD2 B ASP A 1 18  ? 15.15900  0.93900   69.05900 0.450 28.21996 ? 19  ASP A OD2 1 
ATOM   156  N  N   . GLY A 1 19  ? 11.72300  -3.41000  67.95000 1.000 10.43753 ? 20  GLY A N   1 
ATOM   157  C  CA  . GLY A 1 19  ? 11.05300  -4.66900  68.21400 1.000 11.19025 ? 20  GLY A CA  1 
ATOM   158  C  C   . GLY A 1 19  ? 11.95300  -5.85700  67.94900 1.000 10.23224 ? 20  GLY A C   1 
ATOM   159  O  O   . GLY A 1 19  ? 12.83300  -5.83100  67.08200 1.000 10.91127 ? 20  GLY A O   1 
ATOM   160  N  N   . ASP A 1 20  ? 11.67600  -6.93200  68.68300 1.000 10.10591 ? 21  ASP A N   1 
ATOM   161  C  CA  A ASP A 1 20  ? 12.40800  -8.19000  68.45000 0.640 9.56900  ? 21  ASP A CA  1 
ATOM   162  C  CA  B ASP A 1 20  ? 12.43000  -8.15800  68.52100 0.360 11.41996 ? 21  ASP A CA  1 
ATOM   163  C  C   . ASP A 1 20  ? 11.44500  -9.26900  68.86800 1.000 9.47162  ? 21  ASP A C   1 
ATOM   164  O  O   . ASP A 1 20  ? 11.14100  -9.40200  70.05100 1.000 10.24014 ? 21  ASP A O   1 
ATOM   165  C  CB  A ASP A 1 20  ? 13.70600  -8.33100  69.27400 0.640 10.22698 ? 21  ASP A CB  1 
ATOM   166  C  CB  B ASP A 1 20  ? 13.56100  -8.05300  69.54200 0.360 15.81996 ? 21  ASP A CB  1 
ATOM   167  C  CG  A ASP A 1 20  ? 14.28400  -9.80500  69.28300 0.640 10.43753 ? 21  ASP A CG  1 
ATOM   168  C  CG  B ASP A 1 20  ? 14.70100  -8.94100  69.23400 0.360 10.47996 ? 21  ASP A CG  1 
ATOM   169  O  OD1 A ASP A 1 20  ? 13.81300  -10.67900 68.55900 0.640 11.38764 ? 21  ASP A OD1 1 
ATOM   170  O  OD1 B ASP A 1 20  ? 14.38500  -10.02200 68.74300 0.360 8.38996  ? 21  ASP A OD1 1 
ATOM   171  O  OD2 A ASP A 1 20  ? 15.24600  -10.09100 70.04100 0.640 12.26406 ? 21  ASP A OD2 1 
ATOM   172  O  OD2 B ASP A 1 20  ? 15.89800  -8.61100  69.50100 0.360 10.16996 ? 21  ASP A OD2 1 
ATOM   173  N  N   . VAL A 1 21  ? 10.93700  -10.00000 67.86600 1.000 9.59006  ? 22  VAL A N   1 
ATOM   174  C  CA  . VAL A 1 21  ? 9.93300   -11.04800 68.12600 1.000 9.73481  ? 22  VAL A CA  1 
ATOM   175  C  C   . VAL A 1 21  ? 10.49900  -12.36000 67.63900 1.000 9.34266  ? 22  VAL A C   1 
ATOM   176  O  O   . VAL A 1 21  ? 10.77500  -12.50600 66.44100 1.000 9.35582  ? 22  VAL A O   1 
ATOM   177  C  CB  . VAL A 1 21  ? 8.60500   -10.75600 67.42600 1.000 10.12170 ? 22  VAL A CB  1 
ATOM   178  C  CG1 . VAL A 1 21  ? 7.63600   -11.92900 67.58100 1.000 11.39291 ? 22  VAL A CG1 1 
ATOM   179  C  CG2 . VAL A 1 21  ? 8.01500   -9.45600  67.97200 1.000 10.77967 ? 22  VAL A CG2 1 
ATOM   180  N  N   . ASN A 1 22  ? 10.72600  -13.30600 68.55800 1.000 9.54532  ? 23  ASN A N   1 
ATOM   181  C  CA  . ASN A 1 22  ? 11.33400  -14.59700 68.16000 1.000 10.00853 ? 23  ASN A CA  1 
ATOM   182  C  C   . ASN A 1 22  ? 12.68000  -14.40900 67.45300 1.000 10.31383 ? 23  ASN A C   1 
ATOM   183  O  O   . ASN A 1 22  ? 13.09800  -15.26500 66.65100 1.000 11.27710 ? 23  ASN A O   1 
ATOM   184  C  CB  . ASN A 1 22  ? 10.37800  -15.46900 67.30400 1.000 10.84284 ? 23  ASN A CB  1 
ATOM   185  C  CG  . ASN A 1 22  ? 9.64200   -16.50000 68.08000 1.000 10.51385 ? 23  ASN A CG  1 
ATOM   186  O  OD1 . ASN A 1 22  ? 9.42000   -16.37400 69.29600 1.000 10.80862 ? 23  ASN A OD1 1 
ATOM   187  N  ND2 . ASN A 1 22  ? 9.28000   -17.58700 67.39800 1.000 11.38764 ? 23  ASN A ND2 1 
ATOM   188  N  N   . GLY A 1 23  ? 13.42000  -13.32200 67.77400 1.000 10.24014 ? 24  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 23  ? 14.71300  -13.06300 67.17000 1.000 10.99549 ? 24  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 23  ? 14.63800  -12.25900 65.92400 1.000 9.67165  ? 24  GLY A C   1 
ATOM   191  O  O   . GLY A 1 23  ? 15.67900  -11.85600 65.43000 1.000 9.45320  ? 24  GLY A O   1 
ATOM   192  N  N   . HIS A 1 24  ? 13.43700  -12.04200 65.41500 1.000 10.01906 ? 25  HIS A N   1 
ATOM   193  C  CA  . HIS A 1 24  ? 13.20100  -11.27000 64.20300 1.000 10.51122 ? 25  HIS A CA  1 
ATOM   194  C  C   . HIS A 1 24  ? 13.10900  -9.80900  64.63100 1.000 10.87705 ? 25  HIS A C   1 
ATOM   195  O  O   . HIS A 1 24  ? 12.13000  -9.39500  65.26800 1.000 11.06129 ? 25  HIS A O   1 
ATOM   196  C  CB  . HIS A 1 24  ? 11.91400  -11.72600 63.49800 1.000 11.26921 ? 25  HIS A CB  1 
ATOM   197  C  CG  . HIS A 1 24  ? 11.83600  -13.22900 63.30400 1.000 11.52450 ? 25  HIS A CG  1 
ATOM   198  N  ND1 . HIS A 1 24  ? 12.71600  -13.91400 62.49800 1.000 13.48789 ? 25  HIS A ND1 1 
ATOM   199  C  CD2 . HIS A 1 24  ? 11.06400  -14.17000 63.89600 1.000 13.20365 ? 25  HIS A CD2 1 
ATOM   200  C  CE1 . HIS A 1 24  ? 12.44500  -15.21400 62.56700 1.000 14.15113 ? 25  HIS A CE1 1 
ATOM   201  N  NE2 . HIS A 1 24  ? 11.45200  -15.39600 63.41900 1.000 14.00111 ? 25  HIS A NE2 1 
ATOM   202  N  N   . LYS A 1 25  ? 14.11900  -9.01400  64.27100 1.000 11.49555 ? 26  LYS A N   1 
ATOM   203  C  CA  . LYS A 1 25  ? 14.21300  -7.64400  64.73800 1.000 11.71926 ? 26  LYS A CA  1 
ATOM   204  C  C   . LYS A 1 25  ? 13.59700  -6.71800  63.69800 1.000 12.51672 ? 26  LYS A C   1 
ATOM   205  O  O   . LYS A 1 25  ? 13.61900  -6.97600  62.49000 1.000 15.22494 ? 26  LYS A O   1 
ATOM   206  C  CB  . LYS A 1 25  ? 15.66300  -7.23600  64.99500 1.000 12.37987 ? 26  LYS A CB  1 
ATOM   207  C  CG  . LYS A 1 25  ? 16.31800  -8.03200  66.07000 1.000 14.62750 ? 26  LYS A CG  1 
ATOM   208  C  CD  . LYS A 1 25  ? 17.72500  -7.47700  66.26000 1.000 19.09646 ? 26  LYS A CD  1 
ATOM   209  C  CE  . LYS A 1 25  ? 18.39700  -7.75800  67.52400 1.000 20.90194 ? 26  LYS A CE  1 
ATOM   210  N  NZ  . LYS A 1 25  ? 19.52600  -6.72200  67.66900 1.000 19.55704 ? 26  LYS A NZ  1 
ATOM   211  N  N   . PHE A 1 26  ? 13.04500  -5.60300  64.17100 1.000 11.54819 ? 27  PHE A N   1 
ATOM   212  C  CA  . PHE A 1 26  ? 12.47100  -4.60100  63.28300 1.000 10.75599 ? 27  PHE A CA  1 
ATOM   213  C  C   . PHE A 1 26  ? 12.40100  -3.27800  64.01300 1.000 10.38489 ? 27  PHE A C   1 
ATOM   214  O  O   . PHE A 1 26  ? 12.32900  -3.21800  65.24500 1.000 11.34816 ? 27  PHE A O   1 
ATOM   215  C  CB  . PHE A 1 26  ? 11.07000  -5.02600  62.81100 1.000 11.52976 ? 27  PHE A CB  1 
ATOM   216  C  CG  . PHE A 1 26  ? 10.13700  -5.40600  63.92800 1.000 11.16656 ? 27  PHE A CG  1 
ATOM   217  C  CD1 . PHE A 1 26  ? 10.16500  -6.68700  64.48100 1.000 11.12182 ? 27  PHE A CD1 1 
ATOM   218  C  CD2 . PHE A 1 26  ? 9.17200   -4.48700  64.38000 1.000 11.02707 ? 27  PHE A CD2 1 
ATOM   219  C  CE1 . PHE A 1 26  ? 9.25400   -7.05800  65.51700 1.000 10.51648 ? 27  PHE A CE1 1 
ATOM   220  C  CE2 . PHE A 1 26  ? 8.26300   -4.84300  65.41000 1.000 11.40870 ? 27  PHE A CE2 1 
ATOM   221  C  CZ  . PHE A 1 26  ? 8.31700   -6.13400  65.95700 1.000 11.70347 ? 27  PHE A CZ  1 
ATOM   222  N  N   . SER A 1 27  ? 12.33300  -2.20600  63.23200 1.000 10.27961 ? 28  SER A N   1 
ATOM   223  C  CA  . SER A 1 27  ? 12.07500  -0.87700  63.77800 1.000 10.90074 ? 28  SER A CA  1 
ATOM   224  C  C   . SER A 1 27  ? 10.95100  -0.22200  63.00500 1.000 10.62176 ? 28  SER A C   1 
ATOM   225  O  O   . SER A 1 27  ? 10.78700  -0.46100  61.79600 1.000 11.86665 ? 28  SER A O   1 
ATOM   226  C  CB  . SER A 1 27  ? 13.32000  0.00000   63.65900 1.000 13.00889 ? 28  SER A CB  1 
ATOM   227  O  OG  . SER A 1 27  ? 14.38400  -0.55600  64.41900 1.000 14.99334 ? 28  SER A OG  1 
ATOM   228  N  N   . VAL A 1 28  ? 10.15400  0.56600   63.69800 1.000 9.42425  ? 29  VAL A N   1 
ATOM   229  C  CA  . VAL A 1 28  ? 9.04600   1.28500   63.08000 1.000 9.75060  ? 29  VAL A CA  1 
ATOM   230  C  C   . VAL A 1 28  ? 9.06800   2.74100   63.54600 1.000 9.90588  ? 29  VAL A C   1 
ATOM   231  O  O   . VAL A 1 28  ? 9.22900   3.00400   64.75000 1.000 10.85074 ? 29  VAL A O   1 
ATOM   232  C  CB  . VAL A 1 28  ? 7.68500   0.64800   63.43600 1.000 10.07959 ? 29  VAL A CB  1 
ATOM   233  C  CG1 . VAL A 1 28  ? 6.53500   1.47200   62.91200 1.000 10.42437 ? 29  VAL A CG1 1 
ATOM   234  C  CG2 . VAL A 1 28  ? 7.63000   -0.79100  62.93500 1.000 10.87442 ? 29  VAL A CG2 1 
ATOM   235  N  N   . SER A 1 29  ? 8.89800   3.65800   62.60700 1.000 10.29804 ? 30  SER A N   1 
ATOM   236  C  CA  A SER A 1 29  ? 8.69600   5.07100   62.92100 0.590 10.37173 ? 30  SER A CA  1 
ATOM   237  C  CA  B SER A 1 29  ? 8.68100   5.06100   62.94300 0.410 10.82996 ? 30  SER A CA  1 
ATOM   238  C  C   . SER A 1 29  ? 7.25200   5.43500   62.59400 1.000 10.93759 ? 30  SER A C   1 
ATOM   239  O  O   . SER A 1 29  ? 6.66500   4.88600   61.66900 1.000 14.83542 ? 30  SER A O   1 
ATOM   240  C  CB  A SER A 1 29  ? 9.65100   5.91200   62.06000 0.590 10.37963 ? 30  SER A CB  1 
ATOM   241  C  CB  B SER A 1 29  ? 9.64800   5.96400   62.17200 0.410 11.37996 ? 30  SER A CB  1 
ATOM   242  O  OG  A SER A 1 29  ? 9.34100   5.65300   60.70100 0.590 10.51385 ? 30  SER A OG  1 
ATOM   243  O  OG  B SER A 1 29  ? 10.96300  5.71200   62.59100 0.410 15.27996 ? 30  SER A OG  1 
ATOM   244  N  N   . GLY A 1 30  ? 6.66500   6.35200   63.33000 1.000 10.07169 ? 31  GLY A N   1 
ATOM   245  C  CA  . GLY A 1 30  ? 5.34100   6.83200   62.98600 1.000 10.44279 ? 31  GLY A CA  1 
ATOM   246  C  C   . GLY A 1 30  ? 5.24200   8.33400   63.19300 1.000 9.95852  ? 31  GLY A C   1 
ATOM   247  O  O   . GLY A 1 30  ? 5.91600   8.91500   64.06000 1.000 9.92957  ? 31  GLY A O   1 
ATOM   248  N  N   . GLU A 1 31  ? 4.37900   8.94600   62.38200 1.000 9.62954  ? 32  GLU A N   1 
ATOM   249  C  CA  A GLU A 1 31  ? 4.09000   10.37200  62.47300 0.680 9.75587  ? 32  GLU A CA  1 
ATOM   250  C  CA  B GLU A 1 31  ? 4.09900   10.37400  62.44600 0.320 9.59996  ? 32  GLU A CA  1 
ATOM   251  C  C   . GLU A 1 31  ? 2.60900   10.58200  62.30100 1.000 10.16381 ? 32  GLU A C   1 
ATOM   252  O  O   . GLU A 1 31  ? 1.93900   9.81900   61.61100 1.000 11.42449 ? 32  GLU A O   1 
ATOM   253  C  CB  A GLU A 1 31  ? 4.82400   11.13600  61.33900 0.680 10.48753 ? 32  GLU A CB  1 
ATOM   254  C  CB  B GLU A 1 31  ? 4.74300   11.10700  61.25700 0.320 8.11996  ? 32  GLU A CB  1 
ATOM   255  C  CG  A GLU A 1 31  ? 6.32700   11.06000  61.47500 0.680 11.37711 ? 32  GLU A CG  1 
ATOM   256  C  CG  B GLU A 1 31  ? 6.23600   11.05400  61.21800 0.320 9.53996  ? 32  GLU A CG  1 
ATOM   257  C  CD  A GLU A 1 31  ? 7.09000   11.92000  60.46500 0.680 12.51409 ? 32  GLU A CD  1 
ATOM   258  C  CD  B GLU A 1 31  ? 6.79300   11.65400  59.93700 0.320 9.77996  ? 32  GLU A CD  1 
ATOM   259  O  OE1 A GLU A 1 31  ? 6.49400   12.86000  59.85900 0.680 13.21154 ? 32  GLU A OE1 1 
ATOM   260  O  OE1 B GLU A 1 31  ? 5.99400   11.97400  59.04700 0.320 11.13996 ? 32  GLU A OE1 1 
ATOM   261  O  OE2 A GLU A 1 31  ? 8.29000   11.69000  60.28200 0.680 12.70885 ? 32  GLU A OE2 1 
ATOM   262  O  OE2 B GLU A 1 31  ? 8.02600   11.81700  59.85600 0.320 9.27996  ? 32  GLU A OE2 1 
ATOM   263  N  N   . GLY A 1 32  ? 2.11800   11.65500  62.91100 1.000 10.92180 ? 33  GLY A N   1 
ATOM   264  C  CA  . GLY A 1 32  ? 0.73000   12.01500  62.69100 1.000 11.69294 ? 33  GLY A CA  1 
ATOM   265  C  C   . GLY A 1 32  ? 0.31300   13.06000  63.70900 1.000 10.70072 ? 33  GLY A C   1 
ATOM   266  O  O   . GLY A 1 32  ? 1.13800   13.87000  64.16300 1.000 10.82178 ? 33  GLY A O   1 
ATOM   267  N  N   . GLU A 1 33  ? -0.95800  13.05300  64.05700 1.000 10.67177 ? 34  GLU A N   1 
ATOM   268  C  CA  . GLU A 1 33  ? -1.43000  14.11100  64.92300 1.000 12.05088 ? 34  GLU A CA  1 
ATOM   269  C  C   . GLU A 1 33  ? -2.63900  13.62200  65.67800 1.000 10.39015 ? 34  GLU A C   1 
ATOM   270  O  O   . GLU A 1 33  ? -3.36300  12.71800  65.21900 1.000 11.31395 ? 34  GLU A O   1 
ATOM   271  C  CB  . GLU A 1 33  ? -1.69100  15.40000  64.17800 1.000 15.70395 ? 34  GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 33  ? -2.83400  15.25200  63.25700 1.000 17.36731 ? 34  GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 33  ? -3.03500  16.47000  62.33300 1.000 20.54137 ? 34  GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 33  ? -2.03700  17.10600  61.96700 1.000 22.38106 ? 34  GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 33  ? -4.17500  16.79100  61.97100 1.000 21.70730 ? 34  GLU A OE2 1 
ATOM   276  N  N   . GLY A 1 34  ? -2.86500  14.24000  66.83500 1.000 9.93220  ? 35  GLY A N   1 
ATOM   277  C  CA  . GLY A 1 34  ? -3.99400  13.88700  67.66500 1.000 10.78757 ? 35  GLY A CA  1 
ATOM   278  C  C   . GLY A 1 34  ? -4.80700  15.10600  68.02600 1.000 11.08761 ? 35  GLY A C   1 
ATOM   279  O  O   . GLY A 1 34  ? -4.26600  16.19800  68.19800 1.000 11.44818 ? 35  GLY A O   1 
ATOM   280  N  N   . ASP A 1 35  ? -6.12400  14.92900  68.11400 1.000 11.69557 ? 36  ASP A N   1 
ATOM   281  C  CA  . ASP A 1 35  ? -7.08800  16.00800  68.42900 1.000 12.77991 ? 36  ASP A CA  1 
ATOM   282  C  C   . ASP A 1 35  ? -7.97800  15.43500  69.52300 1.000 12.08246 ? 36  ASP A C   1 
ATOM   283  O  O   . ASP A 1 35  ? -9.05800  14.88100  69.27300 1.000 12.76939 ? 36  ASP A O   1 
ATOM   284  C  CB  . ASP A 1 35  ? -7.86700  16.36900  67.11600 1.000 15.20389 ? 36  ASP A CB  1 
ATOM   285  C  CG  . ASP A 1 35  ? -8.48100  17.77700  67.08700 1.000 16.84093 ? 36  ASP A CG  1 
ATOM   286  O  OD1 . ASP A 1 35  ? -8.44000  18.53800  68.04000 1.000 17.71472 ? 36  ASP A OD1 1 
ATOM   287  O  OD2 . ASP A 1 35  ? -9.01100  18.08500  66.00000 1.000 18.37269 ? 36  ASP A OD2 1 
ATOM   288  N  N   . ALA A 1 36  ? -7.46600  15.51600  70.76000 1.000 10.94548 ? 37  ALA A N   1 
ATOM   289  C  CA  . ALA A 1 36  ? -8.12800  14.87900  71.89000 1.000 11.32448 ? 37  ALA A CA  1 
ATOM   290  C  C   . ALA A 1 36  ? -9.51100  15.42400  72.14300 1.000 11.85875 ? 37  ALA A C   1 
ATOM   291  O  O   . ALA A 1 36  ? -10.32800 14.72000  72.76300 1.000 12.40355 ? 37  ALA A O   1 
ATOM   292  C  CB  . ALA A 1 36  ? -7.30200  15.08600  73.15400 1.000 12.53252 ? 37  ALA A CB  1 
ATOM   293  N  N   . THR A 1 37  ? -9.79300  16.65400  71.69700 1.000 11.19551 ? 38  THR A N   1 
ATOM   294  C  CA  . THR A 1 37  ? -11.13500 17.21200  71.83300 1.000 12.42461 ? 38  THR A CA  1 
ATOM   295  C  C   . THR A 1 37  ? -12.16800 16.30000  71.19600 1.000 13.32735 ? 38  THR A C   1 
ATOM   296  O  O   . THR A 1 37  ? -13.30900 16.21400  71.66300 1.000 13.49579 ? 38  THR A O   1 
ATOM   297  C  CB  . THR A 1 37  ? -11.15500 18.60600  71.19000 1.000 14.16692 ? 38  THR A CB  1 
ATOM   298  O  OG1 . THR A 1 37  ? -10.20300 19.43000  71.91900 1.000 14.60382 ? 38  THR A OG1 1 
ATOM   299  C  CG2 . THR A 1 37  ? -12.54400 19.26200  71.33500 1.000 14.81700 ? 38  THR A CG2 1 
ATOM   300  N  N   . TYR A 1 38  ? -11.78000 15.59400  70.13100 1.000 13.13785 ? 39  TYR A N   1 
ATOM   301  C  CA  . TYR A 1 38  ? -12.65600 14.67400  69.41300 1.000 13.77740 ? 39  TYR A CA  1 
ATOM   302  C  C   . TYR A 1 38  ? -12.25100 13.23000  69.63400 1.000 13.19575 ? 39  TYR A C   1 
ATOM   303  O  O   . TYR A 1 38  ? -12.81900 12.33500  68.97800 1.000 14.76963 ? 39  TYR A O   1 
ATOM   304  C  CB  . TYR A 1 38  ? -12.64900 15.02300  67.90000 1.000 15.55393 ? 39  TYR A CB  1 
ATOM   305  C  CG  . TYR A 1 38  ? -12.88300 16.51800  67.75500 1.000 16.20664 ? 39  TYR A CG  1 
ATOM   306  C  CD1 . TYR A 1 38  ? -14.15100 17.04700  67.91200 1.000 17.26466 ? 39  TYR A CD1 1 
ATOM   307  C  CD2 . TYR A 1 38  ? -11.83200 17.39600  67.53800 1.000 16.76197 ? 39  TYR A CD2 1 
ATOM   308  C  CE1 . TYR A 1 38  ? -14.37000 18.40700  67.82300 1.000 18.09108 ? 39  TYR A CE1 1 
ATOM   309  C  CE2 . TYR A 1 38  ? -12.04000 18.78900  67.47200 1.000 17.69629 ? 39  TYR A CE2 1 
ATOM   310  C  CZ  . TYR A 1 38  ? -13.31900 19.28200  67.60600 1.000 18.60166 ? 39  TYR A CZ  1 
ATOM   311  O  OH  . TYR A 1 38  ? -13.58500 20.64500  67.54500 1.000 20.32556 ? 39  TYR A OH  1 
ATOM   312  N  N   . GLY A 1 39  ? -11.25000 12.97700  70.48200 1.000 12.88519 ? 40  GLY A N   1 
ATOM   313  C  CA  . GLY A 1 39  ? -10.76000 11.61400  70.65400 1.000 12.29565 ? 40  GLY A CA  1 
ATOM   314  C  C   . GLY A 1 39  ? -10.09800 11.04900  69.40700 1.000 11.39291 ? 40  GLY A C   1 
ATOM   315  O  O   . GLY A 1 39  ? -10.09100 9.83500   69.21500 1.000 11.63504 ? 40  GLY A O   1 
ATOM   316  N  N   . LYS A 1 40  ? -9.54900  11.91100  68.54900 1.000 11.13761 ? 41  LYS A N   1 
ATOM   317  C  CA  A LYS A 1 40  ? -9.19000  11.54900  67.19100 0.580 11.67978 ? 41  LYS A CA  1 
ATOM   318  C  CA  B LYS A 1 40  ? -9.19100  11.50300  67.20300 0.420 11.76996 ? 41  LYS A CA  1 
ATOM   319  C  C   . LYS A 1 40  ? -7.67900  11.41900  67.03500 1.000 11.18762 ? 41  LYS A C   1 
ATOM   320  O  O   . LYS A 1 40  ? -6.93700  12.32500  67.42700 1.000 13.12206 ? 41  LYS A O   1 
ATOM   321  C  CB  A LYS A 1 40  ? -9.69300  12.64700  66.26400 0.580 12.80623 ? 41  LYS A CB  1 
ATOM   322  C  CB  B LYS A 1 40  ? -9.79800  12.46700  66.18300 0.420 12.57996 ? 41  LYS A CB  1 
ATOM   323  C  CG  A LYS A 1 40  ? -9.27800  12.49500  64.81200 0.580 13.84846 ? 41  LYS A CG  1 
ATOM   324  C  CG  B LYS A 1 40  ? -9.52500  12.11800  64.72000 0.420 12.63996 ? 41  LYS A CG  1 
ATOM   325  C  CD  A LYS A 1 40  ? -9.95400  13.53000  63.92100 0.580 15.67763 ? 41  LYS A CD  1 
ATOM   326  C  CD  B LYS A 1 40  ? -10.38100 12.95800  63.75300 0.420 15.97996 ? 41  LYS A CD  1 
ATOM   327  C  CE  A LYS A 1 40  ? -10.03800 12.99300  62.45000 0.580 16.86725 ? 41  LYS A CE  1 
ATOM   328  C  CE  B LYS A 1 40  ? -9.58200  14.09600  63.11000 0.420 22.30996 ? 41  LYS A CE  1 
ATOM   329  N  NZ  A LYS A 1 40  ? -10.86800 13.77500  61.51400 0.580 17.73577 ? 41  LYS A NZ  1 
ATOM   330  N  NZ  B LYS A 1 40  ? -10.44500 14.99100  62.24400 0.420 13.56996 ? 41  LYS A NZ  1 
ATOM   331  N  N   A LEU A 1 41  ? -7.24400  10.32300  66.39400 0.790 11.27973 ? 42  LEU A N   1 
ATOM   332  N  N   B LEU A 1 41  ? -7.20500  10.36200  66.41600 0.210 10.98996 ? 42  LEU A N   1 
ATOM   333  C  CA  A LEU A 1 41  ? -5.83800  10.10400  66.05300 0.790 11.53240 ? 42  LEU A CA  1 
ATOM   334  C  CA  B LEU A 1 41  ? -5.82800  10.46600  65.98500 0.210 11.73996 ? 42  LEU A CA  1 
ATOM   335  C  C   A LEU A 1 41  ? -5.72300  9.78900   64.56200 0.790 10.39805 ? 42  LEU A C   1 
ATOM   336  C  C   B LEU A 1 41  ? -5.65600  9.80300   64.63800 0.210 9.44996  ? 42  LEU A C   1 
ATOM   337  O  O   A LEU A 1 41  ? -6.48700  8.96700   64.05500 0.790 10.85863 ? 42  LEU A O   1 
ATOM   338  O  O   B LEU A 1 41  ? -6.33800  8.83300   64.29100 0.210 10.39996 ? 42  LEU A O   1 
ATOM   339  C  CB  A LEU A 1 41  ? -5.27600  8.91700   66.85900 0.790 11.76400 ? 42  LEU A CB  1 
ATOM   340  C  CB  B LEU A 1 41  ? -4.80100  10.00800  67.01500 0.210 13.92996 ? 42  LEU A CB  1 
ATOM   341  C  CG  A LEU A 1 41  ? -5.09200  9.24100   68.31300 0.790 12.89572 ? 42  LEU A CG  1 
ATOM   342  C  CG  B LEU A 1 41  ? -4.94100  8.58200   67.49900 0.210 10.85996 ? 42  LEU A CG  1 
ATOM   343  C  CD1 A LEU A 1 41  ? -5.04800  7.95300   69.09200 0.790 14.53802 ? 42  LEU A CD1 1 
ATOM   344  C  CD1 B LEU A 1 41  ? -4.36700  7.57700   66.49700 0.210 15.31996 ? 42  LEU A CD1 1 
ATOM   345  C  CD2 A LEU A 1 41  ? -3.85700  10.02800  68.44700 0.790 12.84308 ? 42  LEU A CD2 1 
ATOM   346  C  CD2 B LEU A 1 41  ? -4.21300  8.48300   68.80700 0.210 15.58996 ? 42  LEU A CD2 1 
ATOM   347  N  N   . THR A 1 42  ? -4.71100  10.35000  63.90900 1.000 10.29277 ? 43  THR A N   1 
ATOM   348  C  CA  A THR A 1 42  ? -4.35300  9.98200   62.53900 0.680 11.42186 ? 43  THR A CA  1 
ATOM   349  C  CA  B THR A 1 42  ? -4.35200  9.91000   62.57000 0.320 9.28996  ? 43  THR A CA  1 
ATOM   350  C  C   . THR A 1 42  ? -2.84700  9.71000   62.53800 1.000 10.76388 ? 43  THR A C   1 
ATOM   351  O  O   . THR A 1 42  ? -2.07500  10.61500  62.86100 1.000 12.07983 ? 43  THR A O   1 
ATOM   352  C  CB  A THR A 1 42  ? -4.69900  11.13600  61.59300 0.680 13.60106 ? 43  THR A CB  1 
ATOM   353  C  CB  B THR A 1 42  ? -4.79500  10.92700  61.53500 0.320 14.06996 ? 43  THR A CB  1 
ATOM   354  O  OG1 A THR A 1 42  ? -6.09100  11.50200  61.78700 0.680 14.98544 ? 43  THR A OG1 1 
ATOM   355  O  OG1 B THR A 1 42  ? -4.24100  12.20500  61.83500 0.320 13.57996 ? 43  THR A OG1 1 
ATOM   356  C  CG2 A THR A 1 42  ? -4.49100  10.69300  60.16900 0.680 15.34338 ? 43  THR A CG2 1 
ATOM   357  C  CG2 B THR A 1 42  ? -6.25600  11.01800  61.64700 0.320 16.16996 ? 43  THR A CG2 1 
ATOM   358  N  N   . LEU A 1 43  ? -2.43500  8.49100   62.17200 1.000 10.69809 ? 44  LEU A N   1 
ATOM   359  C  CA  . LEU A 1 43  ? -1.02600  8.11300   62.27100 1.000 10.69545 ? 44  LEU A CA  1 
ATOM   360  C  C   . LEU A 1 43  ? -0.63400  7.28500   61.06400 1.000 10.34278 ? 44  LEU A C   1 
ATOM   361  O  O   . LEU A 1 43  ? -1.42100  6.47600   60.58500 1.000 12.56936 ? 44  LEU A O   1 
ATOM   362  C  CB  . LEU A 1 43  ? -0.77800  7.27800   63.54700 1.000 11.34816 ? 44  LEU A CB  1 
ATOM   363  C  CG  . LEU A 1 43  ? -0.85600  8.14800   64.84400 1.000 13.00889 ? 44  LEU A CG  1 
ATOM   364  C  CD1 . LEU A 1 43  ? -1.02000  7.23300   66.07100 1.000 15.88555 ? 44  LEU A CD1 1 
ATOM   365  C  CD2 . LEU A 1 43  ? 0.37300   9.01900   65.04100 1.000 14.30904 ? 44  LEU A CD2 1 
ATOM   366  N  N   . LYS A 1 44  ? 0.63000   7.45300   60.62500 1.000 10.03748 ? 45  LYS A N   1 
ATOM   367  C  CA  . LYS A 1 44  ? 1.18200   6.58500   59.58500 1.000 10.42700 ? 45  LYS A CA  1 
ATOM   368  C  C   . LYS A 1 44  ? 2.47600   6.01100   60.12100 1.000 10.31646 ? 45  LYS A C   1 
ATOM   369  O  O   . LYS A 1 44  ? 3.35300   6.78300   60.56900 1.000 10.32962 ? 45  LYS A O   1 
ATOM   370  C  CB  . LYS A 1 44  ? 1.48600   7.40200   58.30900 1.000 11.08761 ? 45  LYS A CB  1 
ATOM   371  C  CG  . LYS A 1 44  ? 2.20200   6.53100   57.26600 1.000 11.22973 ? 45  LYS A CG  1 
ATOM   372  C  CD  . LYS A 1 44  ? 2.48000   7.35500   56.00400 1.000 13.65107 ? 45  LYS A CD  1 
ATOM   373  C  CE  . LYS A 1 44  ? 3.32100   6.52400   55.03700 1.000 14.54328 ? 45  LYS A CE  1 
ATOM   374  N  NZ  . LYS A 1 44  ? 3.74100   7.33800   53.82900 1.000 15.84344 ? 45  LYS A NZ  1 
ATOM   375  N  N   . PHE A 1 45  ? 2.61600   4.68700   60.06500 1.000 9.84272  ? 46  PHE A N   1 
ATOM   376  C  CA  . PHE A 1 45  ? 3.78100   3.95800   60.58100 1.000 9.88220  ? 46  PHE A CA  1 
ATOM   377  C  C   . PHE A 1 45  ? 4.53600   3.36300   59.41400 1.000 9.63743  ? 46  PHE A C   1 
ATOM   378  O  O   . PHE A 1 45  ? 3.91100   2.84200   58.46900 1.000 10.87442 ? 46  PHE A O   1 
ATOM   379  C  CB  . PHE A 1 45  ? 3.32500   2.83700   61.48500 1.000 9.63217  ? 46  PHE A CB  1 
ATOM   380  C  CG  . PHE A 1 45  ? 2.48200   3.34600   62.61400 1.000 9.46373  ? 46  PHE A CG  1 
ATOM   381  C  CD1 . PHE A 1 45  ? 3.07600   3.92500   63.73200 1.000 9.53742  ? 46  PHE A CD1 1 
ATOM   382  C  CD2 . PHE A 1 45  ? 1.08500   3.27500   62.53800 1.000 10.36647 ? 46  PHE A CD2 1 
ATOM   383  C  CE1 . PHE A 1 45  ? 2.29900   4.45400   64.74000 1.000 10.28488 ? 46  PHE A CE1 1 
ATOM   384  C  CE2 . PHE A 1 45  ? 0.30600   3.78200   63.53000 1.000 11.21394 ? 46  PHE A CE2 1 
ATOM   385  C  CZ  . PHE A 1 45  ? 0.92000   4.35500   64.65800 1.000 10.94285 ? 46  PHE A CZ  1 
ATOM   386  N  N   . ILE A 1 46  ? 5.87100   3.40600   59.47200 1.000 10.07696 ? 47  ILE A N   1 
ATOM   387  C  CA  . ILE A 1 46  ? 6.72100   2.85600   58.41800 1.000 10.24014 ? 47  ILE A CA  1 
ATOM   388  C  C   . ILE A 1 46  ? 7.69300   1.88100   59.05200 1.000 9.91115  ? 47  ILE A C   1 
ATOM   389  O  O   . ILE A 1 46  ? 8.35800   2.23200   60.03800 1.000 10.61913 ? 47  ILE A O   1 
ATOM   390  C  CB  . ILE A 1 46  ? 7.52400   3.99000   57.72900 1.000 11.14551 ? 47  ILE A CB  1 
ATOM   391  C  CG1 . ILE A 1 46  ? 6.58100   4.99400   57.09000 1.000 12.58515 ? 47  ILE A CG1 1 
ATOM   392  C  CG2 . ILE A 1 46  ? 8.57600   3.41200   56.75800 1.000 12.39566 ? 47  ILE A CG2 1 
ATOM   393  C  CD1 . ILE A 1 46  ? 7.21600   6.33700   56.71700 1.000 14.34326 ? 47  ILE A CD1 1 
ATOM   394  N  N   . CYS A 1 47  ? 7.82000   0.67600   58.49300 1.000 10.44542 ? 48  CYS A N   1 
ATOM   395  C  CA  . CYS A 1 47  ? 8.85500   -0.24100  58.95900 1.000 10.86916 ? 48  CYS A CA  1 
ATOM   396  C  C   . CYS A 1 47  ? 10.16000  0.17900   58.28300 1.000 12.08509 ? 48  CYS A C   1 
ATOM   397  O  O   . CYS A 1 47  ? 10.26600  0.15300   57.05100 1.000 13.20365 ? 48  CYS A O   1 
ATOM   398  C  CB  . CYS A 1 47  ? 8.51900   -1.69900  58.61400 1.000 11.74295 ? 48  CYS A CB  1 
ATOM   399  S  SG  . CYS A 1 47  ? 9.81300   -2.81000  59.18300 1.000 12.18511 ? 48  CYS A SG  1 
ATOM   400  N  N   . THR A 1 48  ? 11.13600  0.61200   59.07000 1.000 12.50620 ? 49  THR A N   1 
ATOM   401  C  CA  . THR A 1 48  ? 12.35700  1.17800   58.51300 1.000 13.59843 ? 49  THR A CA  1 
ATOM   402  C  C   . THR A 1 48  ? 13.42300  0.13200   58.26800 1.000 13.92216 ? 49  THR A C   1 
ATOM   403  O  O   . THR A 1 48  ? 14.47900  0.46600   57.71100 1.000 17.22255 ? 49  THR A O   1 
ATOM   404  C  CB  . THR A 1 48  ? 12.89400  2.24900   59.43100 1.000 14.60118 ? 49  THR A CB  1 
ATOM   405  O  OG1 . THR A 1 48  ? 13.21100  1.64300   60.67300 1.000 15.66447 ? 49  THR A OG1 1 
ATOM   406  C  CG2 . THR A 1 48  ? 11.87100  3.40600   59.59900 1.000 15.29864 ? 49  THR A CG2 1 
ATOM   407  N  N   . THR A 1 49  ? 13.15000  -1.10900  58.65600 1.000 14.03006 ? 50  THR A N   1 
ATOM   408  C  CA  . THR A 1 49  ? 14.10000  -2.19900  58.52700 1.000 14.71699 ? 50  THR A CA  1 
ATOM   409  C  C   . THR A 1 49  ? 13.76900  -3.14600  57.39100 1.000 16.38561 ? 50  THR A C   1 
ATOM   410  O  O   . THR A 1 49  ? 14.48600  -4.12000  57.19900 1.000 19.99920 ? 50  THR A O   1 
ATOM   411  C  CB  . THR A 1 49  ? 14.24400  -2.94800  59.85400 1.000 14.75120 ? 50  THR A CB  1 
ATOM   412  O  OG1 . THR A 1 49  ? 12.93800  -3.22800  60.37400 1.000 14.31168 ? 50  THR A OG1 1 
ATOM   413  C  CG2 . THR A 1 49  ? 15.03900  -2.11400  60.81200 1.000 15.69079 ? 50  THR A CG2 1 
ATOM   414  N  N   . GLY A 1 50  ? 12.72000  -2.87900  56.61200 1.000 15.73027 ? 51  GLY A N   1 
ATOM   415  C  CA  . GLY A 1 50  ? 12.30200  -3.77000  55.54400 1.000 15.66710 ? 51  GLY A CA  1 
ATOM   416  C  C   . GLY A 1 50  ? 10.87900  -4.20800  55.75100 1.000 15.58025 ? 51  GLY A C   1 
ATOM   417  O  O   . GLY A 1 50  ? 10.01200  -3.39100  56.06500 1.000 16.67249 ? 51  GLY A O   1 
ATOM   418  N  N   . LYS A 1 51  ? 10.62900  -5.49300  55.57100 1.000 15.61446 ? 52  LYS A N   1 
ATOM   419  C  CA  . LYS A 1 51  ? 9.27800   -5.98800  55.79700 1.000 17.18044 ? 52  LYS A CA  1 
ATOM   420  C  C   . LYS A 1 51  ? 9.05600   -6.21500  57.28200 1.000 14.33010 ? 52  LYS A C   1 
ATOM   421  O  O   . LYS A 1 51  ? 9.92200   -6.75800  57.96400 1.000 14.64066 ? 52  LYS A O   1 
ATOM   422  C  CB  . LYS A 1 51  ? 9.07400   -7.30000  55.01500 1.000 22.69952 ? 52  LYS A CB  1 
ATOM   423  C  CG  . LYS A 1 51  ? 7.66900   -7.90400  55.14200 1.000 30.68206 ? 52  LYS A CG  1 
ATOM   424  C  CD  . LYS A 1 51  ? 7.58100   -9.27600  54.47700 1.000 39.79996 ? 52  LYS A CD  1 
ATOM   425  C  CE  . LYS A 1 51  ? 6.32400   -10.02200 54.90400 1.000 47.83996 ? 52  LYS A CE  1 
ATOM   426  N  NZ  . LYS A 1 51  ? 5.08300   -9.32900  54.46700 1.000 37.09996 ? 52  LYS A NZ  1 
ATOM   427  N  N   . LEU A 1 52  ? 7.88400   -5.83500  57.76400 1.000 13.36683 ? 53  LEU A N   1 
ATOM   428  C  CA  . LEU A 1 52  ? 7.54200   -6.10100  59.15700 1.000 11.59293 ? 53  LEU A CA  1 
ATOM   429  C  C   . LEU A 1 52  ? 7.33100   -7.60600  59.33700 1.000 11.23499 ? 53  LEU A C   1 
ATOM   430  O  O   . LEU A 1 52  ? 6.54000   -8.21000  58.60800 1.000 12.77728 ? 53  LEU A O   1 
ATOM   431  C  CB  . LEU A 1 52  ? 6.27200   -5.33500  59.48400 1.000 10.99023 ? 53  LEU A CB  1 
ATOM   432  C  CG  . LEU A 1 52  ? 5.97600   -5.28400  60.98000 1.000 10.17434 ? 53  LEU A CG  1 
ATOM   433  C  CD1 . LEU A 1 52  ? 6.93000   -4.34100  61.72300 1.000 10.91653 ? 53  LEU A CD1 1 
ATOM   434  C  CD2 . LEU A 1 52  ? 4.53100   -4.81000  61.19200 1.000 10.80599 ? 53  LEU A CD2 1 
ATOM   435  N  N   . PRO A 1 53  ? 7.99100   -8.25100  60.30100 1.000 11.90349 ? 54  PRO A N   1 
ATOM   436  C  CA  . PRO A 1 53  ? 7.89900   -9.71800  60.43200 1.000 12.30880 ? 54  PRO A CA  1 
ATOM   437  C  C   . PRO A 1 53  ? 6.72600   -10.18100 61.27100 1.000 12.18511 ? 54  PRO A C   1 
ATOM   438  O  O   . PRO A 1 53  ? 6.59500   -11.38200 61.47700 1.000 13.77477 ? 54  PRO A O   1 
ATOM   439  C  CB  . PRO A 1 53  ? 9.24100   -10.08100 61.12400 1.000 14.65382 ? 54  PRO A CB  1 
ATOM   440  C  CG  . PRO A 1 53  ? 9.50800   -8.90500  61.96600 1.000 13.73792 ? 54  PRO A CG  1 
ATOM   441  C  CD  . PRO A 1 53  ? 9.07200   -7.69100  61.14600 1.000 12.57199 ? 54  PRO A CD  1 
ATOM   442  N  N   . VAL A 1 54  ? 5.87300   -9.27100  61.71400 1.000 10.15855 ? 55  VAL A N   1 
ATOM   443  C  CA  . VAL A 1 54  ? 4.61200   -9.59500  62.37600 1.000 10.60334 ? 55  VAL A CA  1 
ATOM   444  C  C   . VAL A 1 54  ? 3.49800   -8.84800  61.65100 1.000 11.02181 ? 55  VAL A C   1 
ATOM   445  O  O   . VAL A 1 54  ? 3.75700   -7.89700  60.89900 1.000 10.81126 ? 55  VAL A O   1 
ATOM   446  C  CB  . VAL A 1 54  ? 4.64500   -9.25100  63.88600 1.000 11.24289 ? 55  VAL A CB  1 
ATOM   447  C  CG1 . VAL A 1 54  ? 5.73000   -9.98500  64.63000 1.000 12.43514 ? 55  VAL A CG1 1 
ATOM   448  C  CG2 . VAL A 1 54  ? 4.82500   -7.74900  64.06900 1.000 11.84033 ? 55  VAL A CG2 1 
ATOM   449  N  N   . PRO A 1 55  ? 2.23600   -9.22900  61.87300 1.000 10.43226 ? 56  PRO A N   1 
ATOM   450  C  CA  . PRO A 1 55  ? 1.14600   -8.48600  61.20200 1.000 10.12696 ? 56  PRO A CA  1 
ATOM   451  C  C   . PRO A 1 55  ? 1.03000   -7.09800  61.83500 1.000 9.47689  ? 56  PRO A C   1 
ATOM   452  O  O   . PRO A 1 55  ? 1.03100   -6.94800  63.06200 1.000 10.04801 ? 56  PRO A O   1 
ATOM   453  C  CB  . PRO A 1 55  ? -0.09400  -9.34200  61.48600 1.000 10.80073 ? 56  PRO A CB  1 
ATOM   454  C  CG  . PRO A 1 55  ? 0.48800   -10.74200 61.79100 1.000 11.73242 ? 56  PRO A CG  1 
ATOM   455  C  CD  . PRO A 1 55  ? 1.73800   -10.41800 62.57300 1.000 11.60872 ? 56  PRO A CD  1 
ATOM   456  N  N   . TRP A 1 56  ? 0.85000   -6.09300  60.98000 1.000 9.39793  ? 57  TRP A N   1 
ATOM   457  C  CA  . TRP A 1 56  ? 0.62900   -4.71500  61.43800 1.000 9.38740  ? 57  TRP A CA  1 
ATOM   458  C  C   . TRP A 1 56  ? -0.44400  -4.62600  62.51300 1.000 8.66889  ? 57  TRP A C   1 
ATOM   459  O  O   . TRP A 1 56  ? -0.25500  -3.88000  63.50200 1.000 9.01894  ? 57  TRP A O   1 
ATOM   460  C  CB  . TRP A 1 56  ? 0.26600   -3.80000  60.24000 1.000 10.01379 ? 57  TRP A CB  1 
ATOM   461  C  CG  . TRP A 1 56  ? 1.46100   -3.39100  59.43200 1.000 9.41635  ? 57  TRP A CG  1 
ATOM   462  C  CD1 . TRP A 1 56  ? 1.84600   -3.84900  58.20000 1.000 9.94536  ? 57  TRP A CD1 1 
ATOM   463  C  CD2 . TRP A 1 56  ? 2.48300   -2.46400  59.83400 1.000 9.47952  ? 57  TRP A CD2 1 
ATOM   464  N  NE1 . TRP A 1 56  ? 3.01100   -3.26300  57.80600 1.000 9.90062  ? 57  TRP A NE1 1 
ATOM   465  C  CE2 . TRP A 1 56  ? 3.43300   -2.41600  58.79300 1.000 10.12696 ? 57  TRP A CE2 1 
ATOM   466  C  CE3 . TRP A 1 56  ? 2.69100   -1.68400  60.98300 1.000 10.07169 ? 57  TRP A CE3 1 
ATOM   467  C  CZ2 . TRP A 1 56  ? 4.54900   -1.57200  58.83600 1.000 10.00327 ? 57  TRP A CZ2 1 
ATOM   468  C  CZ3 . TRP A 1 56  ? 3.77300   -0.88100  61.02600 1.000 9.45846  ? 57  TRP A CZ3 1 
ATOM   469  C  CH2 . TRP A 1 56  ? 4.70900   -0.80700  59.96300 1.000 9.38740  ? 57  TRP A CH2 1 
ATOM   470  N  N   . PRO A 1 57  ? -1.60400  -5.29200  62.38000 1.000 8.78996  ? 58  PRO A N   1 
ATOM   471  C  CA  . PRO A 1 57  ? -2.64800  -5.10900  63.40000 1.000 9.09000  ? 58  PRO A CA  1 
ATOM   472  C  C   . PRO A 1 57  ? -2.15300  -5.43900  64.80500 1.000 8.44255  ? 58  PRO A C   1 
ATOM   473  O  O   . PRO A 1 57  ? -2.65400  -4.90300  65.78900 1.000 9.07421  ? 58  PRO A O   1 
ATOM   474  C  CB  . PRO A 1 57  ? -3.76600  -6.06200  62.93300 1.000 10.02695 ? 58  PRO A CB  1 
ATOM   475  C  CG  . PRO A 1 57  ? -3.63000  -6.02700  61.45200 1.000 9.85851  ? 58  PRO A CG  1 
ATOM   476  C  CD  . PRO A 1 57  ? -2.12900  -6.10200  61.25300 1.000 9.09526  ? 58  PRO A CD  1 
ATOM   477  N  N   . THR A 1 58  ? -1.20300  -6.38300  64.92700 1.000 9.03210  ? 59  THR A N   1 
ATOM   478  C  CA  . THR A 1 58  ? -0.75000  -6.81100  66.26100 1.000 8.79523  ? 59  THR A CA  1 
ATOM   479  C  C   . THR A 1 58  ? -0.03000  -5.70500  67.02200 1.000 8.48993  ? 59  THR A C   1 
ATOM   480  O  O   . THR A 1 58  ? 0.15100   -5.85800  68.24000 1.000 8.66626  ? 59  THR A O   1 
ATOM   481  C  CB  . THR A 1 58  ? 0.14100   -8.07300  66.25200 1.000 8.92682  ? 59  THR A CB  1 
ATOM   482  O  OG1 . THR A 1 58  ? 1.42100   -7.76700  65.68100 1.000 9.31897  ? 59  THR A OG1 1 
ATOM   483  C  CG2 . THR A 1 58  ? -0.55800  -9.22200  65.57300 1.000 9.77692  ? 59  THR A CG2 1 
ATOM   484  N  N   . LEU A 1 59  ? 0.40000   -4.62900  66.33000 1.000 8.40044  ? 60  LEU A N   1 
ATOM   485  C  CA  . LEU A 1 59  ? 1.15200   -3.52700  66.91800 1.000 7.88459  ? 60  LEU A CA  1 
ATOM   486  C  C   . LEU A 1 59  ? 0.29100   -2.29700  67.17900 1.000 8.07935  ? 60  LEU A C   1 
ATOM   487  O  O   . LEU A 1 59  ? 0.80900   -1.32600  67.77000 1.000 8.53467  ? 60  LEU A O   1 
ATOM   488  C  CB  . LEU A 1 59  ? 2.35000   -3.15300  66.02700 1.000 8.87681  ? 60  LEU A CB  1 
ATOM   489  C  CG  . LEU A 1 59  ? 3.33100   -4.29200  65.83400 1.000 9.44530  ? 60  LEU A CG  1 
ATOM   490  C  CD1 . LEU A 1 59  ? 4.49200   -3.82400  64.92600 1.000 10.46911 ? 60  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A 1 59  ? 3.91500   -4.83200  67.16400 1.000 10.05064 ? 60  LEU A CD2 1 
ATOM   492  N  N   . VAL A 1 60  ? -0.97500  -2.28300  66.74000 1.000 8.12146  ? 61  VAL A N   1 
ATOM   493  C  CA  . VAL A 1 60  ? -1.81600  -1.09700  66.87100 1.000 8.86629  ? 61  VAL A CA  1 
ATOM   494  C  C   . VAL A 1 60  ? -1.86200  -0.59400  68.30700 1.000 8.70311  ? 61  VAL A C   1 
ATOM   495  O  O   . VAL A 1 60  ? -1.71400  0.60900   68.55000 1.000 9.51900  ? 61  VAL A O   1 
ATOM   496  C  CB  . VAL A 1 60  ? -3.22000  -1.38000  66.31200 1.000 9.01894  ? 61  VAL A CB  1 
ATOM   497  C  CG1 . VAL A 1 60  ? -4.21500  -0.31200  66.70400 1.000 9.43741  ? 61  VAL A CG1 1 
ATOM   498  C  CG2 . VAL A 1 60  ? -3.14300  -1.46800  64.77400 1.000 9.09789  ? 61  VAL A CG2 1 
ATOM   499  N  N   . THR A 1 61  ? -2.17200  -1.47300  69.27100 1.000 8.91103  ? 62  THR A N   1 
ATOM   500  C  CA  . THR A 1 61  ? -2.32400  -0.99400  70.64300 1.000 8.22410  ? 62  THR A CA  1 
ATOM   501  C  C   . THR A 1 61  ? -1.01400  -0.46100  71.20300 1.000 8.09514  ? 62  THR A C   1 
ATOM   502  O  O   . THR A 1 61  ? -1.03700  0.41100   72.06700 1.000 8.52151  ? 62  THR A O   1 
ATOM   503  C  CB  . THR A 1 61  ? -2.85300  -2.10100  71.55800 1.000 8.29253  ? 62  THR A CB  1 
ATOM   504  O  OG1 . THR A 1 61  ? -1.96700  -3.22200  71.47000 1.000 8.55046  ? 62  THR A OG1 1 
ATOM   505  C  CG2 . THR A 1 61  ? -4.27000  -2.47400  71.22500 1.000 9.25844  ? 62  THR A CG2 1 
ATOM   506  N  N   . THR A 1 62  ? 0.11300   -0.99700  70.74000 1.000 7.87933  ? 63  THR A N   1 
ATOM   507  C  CA  . THR A 1 62  ? 1.41300   -0.55600  71.25100 1.000 8.47940  ? 63  THR A CA  1 
ATOM   508  C  C   . THR A 1 62  ? 1.76100   0.82000   70.71500 1.000 8.72153  ? 63  THR A C   1 
ATOM   509  O  O   . THR A 1 62  ? 2.17900   1.71000   71.48100 1.000 8.67679  ? 63  THR A O   1 
ATOM   510  C  CB  . THR A 1 62  ? 2.49100   -1.59100  70.88900 1.000 8.03461  ? 63  THR A CB  1 
ATOM   511  O  OG1 . THR A 1 62  ? 2.16800   -2.82400  71.54200 1.000 8.50572  ? 63  THR A OG1 1 
ATOM   512  C  CG2 . THR A 1 62  ? 3.85700   -1.17800  71.36600 1.000 9.44267  ? 63  THR A CG2 1 
ATOM   513  N  N   . PHE A 1 63  ? 1.57300   1.02200   69.40400 1.000 8.47677  ? 64  PHE A N   1 
ATOM   514  C  CA  . PHE A 1 63  ? 1.81700   2.31800   68.80400 1.000 8.88997  ? 64  PHE A CA  1 
ATOM   515  C  C   . PHE A 1 63  ? 0.84000   3.36300   69.31200 1.000 9.30055  ? 64  PHE A C   1 
ATOM   516  O  O   . PHE A 1 63  ? 1.22000   4.54100   69.53300 1.000 9.62690  ? 64  PHE A O   1 
ATOM   517  C  CB  . PHE A 1 63  ? 1.55700   2.25000   67.30400 1.000 9.29792  ? 64  PHE A CB  1 
ATOM   518  C  CG  . PHE A 1 63  ? 2.48400   1.36200   66.49700 1.000 9.10316  ? 64  PHE A CG  1 
ATOM   519  C  CD1 . PHE A 1 63  ? 3.86200   1.20600   66.80300 1.000 8.88734  ? 64  PHE A CD1 1 
ATOM   520  C  CD2 . PHE A 1 63  ? 1.97200   0.75100   65.33200 1.000 9.08737  ? 64  PHE A CD2 1 
ATOM   521  C  CE1 . PHE A 1 63  ? 4.67000   0.43000   65.96800 1.000 9.25581  ? 64  PHE A CE1 1 
ATOM   522  C  CE2 . PHE A 1 63  ? 2.80100   -0.02300  64.54200 1.000 9.44267  ? 64  PHE A CE2 1 
ATOM   523  C  CZ  . PHE A 1 63  ? 4.14600   -0.19400  64.86300 1.000 9.08473  ? 64  PHE A CZ  1 
HETATM 524  N  N1  . GYS A 1 64  ? -0.42900  2.94600   69.43600 1.000 8.66100  ? 66  GYS A N1  1 
HETATM 525  O  OG1 A GYS A 1 64  ? -3.24700  5.20300   68.79800 1.000 11.30079 ? 66  GYS A OG1 1 
HETATM 526  C  CB1 . GYS A 1 64  ? -2.41500  4.07400   68.54900 1.000 9.85062  ? 66  GYS A CB1 1 
HETATM 527  C  CA1 . GYS A 1 64  ? -1.54200  3.83700   69.76400 1.000 9.29792  ? 66  GYS A CA1 1 
HETATM 528  C  C1  . GYS A 1 64  ? -2.25100  3.25700   70.91600 1.000 9.09263  ? 66  GYS A C1  1 
HETATM 529  N  N2  . GYS A 1 64  ? -3.37700  2.62500   70.88200 1.000 9.65586  ? 66  GYS A N2  1 
HETATM 530  N  N3  . GYS A 1 64  ? -1.69600  3.35500   72.21100 1.000 8.70574  ? 66  GYS A N3  1 
HETATM 531  C  C2  . GYS A 1 64  ? -2.55800  2.70000   73.02800 1.000 9.27686  ? 66  GYS A C2  1 
HETATM 532  O  O2  . GYS A 1 64  ? -2.33800  2.56700   74.27000 1.000 9.42162  ? 66  GYS A O2  1 
HETATM 533  C  CA2 . GYS A 1 64  ? -3.62300  2.23400   72.19500 1.000 9.39530  ? 66  GYS A CA2 1 
HETATM 534  C  CA3 . GYS A 1 64  ? -0.37200  3.78500   72.59700 1.000 9.57427  ? 66  GYS A CA3 1 
HETATM 535  C  CB2 . GYS A 1 64  ? -4.61400  1.43800   72.64100 1.000 10.59544 ? 66  GYS A CB2 1 
HETATM 536  C  CG2 . GYS A 1 64  ? -5.65900  0.71000   71.99600 1.000 10.13749 ? 66  GYS A CG2 1 
HETATM 537  C  CD1 . GYS A 1 64  ? -5.87300  0.72800   70.59500 1.000 10.61123 ? 66  GYS A CD1 1 
HETATM 538  C  CD2 . GYS A 1 64  ? -6.57200  -0.01500  72.80200 1.000 10.81915 ? 66  GYS A CD2 1 
HETATM 539  C  CE1 . GYS A 1 64  ? -6.92200  0.03500   70.01500 1.000 10.95075 ? 66  GYS A CE1 1 
HETATM 540  C  CE2 . GYS A 1 64  ? -7.62800  -0.72700  72.23600 1.000 10.12170 ? 66  GYS A CE2 1 
HETATM 541  C  CZ  . GYS A 1 64  ? -7.81300  -0.64000  70.85200 1.000 10.41384 ? 66  GYS A CZ  1 
HETATM 542  O  OH  . GYS A 1 64  ? -8.87300  -1.30600  70.34700 1.000 11.14551 ? 66  GYS A OH  1 
HETATM 543  C  C3  . GYS A 1 64  ? -0.30400  5.15700   73.18700 1.000 10.01116 ? 66  GYS A C3  1 
HETATM 544  O  O3  . GYS A 1 64  ? 0.67500   5.44500   73.92100 1.000 10.19803 ? 66  GYS A O3  1 
ATOM   545  N  N   . VAL A 1 65  ? -1.20500  6.04500   72.81500 1.000 9.39530  ? 68  VAL A N   1 
ATOM   546  C  CA  . VAL A 1 65  ? -1.11800  7.47000   73.21600 1.000 9.72165  ? 68  VAL A CA  1 
ATOM   547  C  C   . VAL A 1 65  ? -2.49900  7.86500   73.74100 1.000 8.78996  ? 68  VAL A C   1 
ATOM   548  O  O   . VAL A 1 65  ? -3.19500  8.74100   73.20300 1.000 10.04011 ? 68  VAL A O   1 
ATOM   549  C  CB  . VAL A 1 65  ? -0.58500  8.37800   72.03800 1.000 10.32436 ? 68  VAL A CB  1 
ATOM   550  C  CG1 . VAL A 1 65  ? 0.90900   8.09200   71.82200 1.000 11.41133 ? 68  VAL A CG1 1 
ATOM   551  C  CG2 . VAL A 1 65  ? -1.37100  8.18100   70.70500 1.000 11.47976 ? 68  VAL A CG2 1 
ATOM   552  N  N   . GLN A 1 66  ? -2.85300  7.28200   74.87700 1.000 9.17422  ? 69  GLN A N   1 
ATOM   553  C  CA  . GLN A 1 66  ? -4.19700  7.36900   75.42500 1.000 9.51110  ? 69  GLN A CA  1 
ATOM   554  C  C   . GLN A 1 66  ? -4.48300  8.73400   76.03400 1.000 8.96893  ? 69  GLN A C   1 
ATOM   555  O  O   . GLN A 1 66  ? -5.63300  9.01700   76.36200 1.000 9.71902  ? 69  GLN A O   1 
ATOM   556  C  CB  . GLN A 1 66  ? -4.41700  6.20200   76.39400 1.000 10.29014 ? 69  GLN A CB  1 
ATOM   557  C  CG  . GLN A 1 66  ? -4.45500  4.87500   75.62700 1.000 11.01128 ? 69  GLN A CG  1 
ATOM   558  C  CD  . GLN A 1 66  ? -4.50500  3.70600   76.52700 1.000 11.27710 ? 69  GLN A CD  1 
ATOM   559  O  OE1 . GLN A 1 66  ? -3.73300  3.60300   77.49500 1.000 11.72452 ? 69  GLN A OE1 1 
ATOM   560  N  NE2 . GLN A 1 66  ? -5.30800  2.71500   76.14700 1.000 13.13785 ? 69  GLN A NE2 1 
ATOM   561  N  N   . CYS A 1 67  ? -3.45900  9.60100   76.12200 1.000 9.10053  ? 70  CYS A N   1 
ATOM   562  C  CA  . CYS A 1 67  ? -3.71600  11.01800  76.36500 1.000 9.81640  ? 70  CYS A CA  1 
ATOM   563  C  C   . CYS A 1 67  ? -4.56200  11.67300  75.28400 1.000 8.82154  ? 70  CYS A C   1 
ATOM   564  O  O   . CYS A 1 67  ? -5.07900  12.75900  75.54400 1.000 9.97431  ? 70  CYS A O   1 
ATOM   565  C  CB  . CYS A 1 67  ? -2.38800  11.77000  76.55000 1.000 9.83219  ? 70  CYS A CB  1 
ATOM   566  S  SG  . CYS A 1 67  ? -1.13700  11.37900  75.21000 1.000 9.94010  ? 70  CYS A SG  1 
ATOM   567  N  N   . PHE A 1 68  ? -4.75600  11.06100  74.10500 1.000 8.94524  ? 71  PHE A N   1 
ATOM   568  C  CA  . PHE A 1 68  ? -5.61500  11.62000  73.07500 1.000 9.65059  ? 71  PHE A CA  1 
ATOM   569  C  C   . PHE A 1 68  ? -7.05500  11.13900  73.17900 1.000 9.59532  ? 71  PHE A C   1 
ATOM   570  O  O   . PHE A 1 68  ? -7.86600  11.48000  72.31600 1.000 11.09024 ? 71  PHE A O   1 
ATOM   571  C  CB  . PHE A 1 68  ? -5.02000  11.39200  71.68400 1.000 9.74534  ? 71  PHE A CB  1 
ATOM   572  C  CG  . PHE A 1 68  ? -3.79600  12.22600  71.44800 1.000 9.67428  ? 71  PHE A CG  1 
ATOM   573  C  CD1 . PHE A 1 68  ? -3.92000  13.60400  71.21000 1.000 9.87167  ? 71  PHE A CD1 1 
ATOM   574  C  CD2 . PHE A 1 68  ? -2.53100  11.67200  71.51100 1.000 9.34529  ? 71  PHE A CD2 1 
ATOM   575  C  CE1 . PHE A 1 68  ? -2.76200  14.40800  71.03000 1.000 10.54280 ? 71  PHE A CE1 1 
ATOM   576  C  CE2 . PHE A 1 68  ? -1.39300  12.45300  71.34500 1.000 9.14264  ? 71  PHE A CE2 1 
ATOM   577  C  CZ  . PHE A 1 68  ? -1.52100  13.84600  71.09500 1.000 9.91115  ? 71  PHE A CZ  1 
ATOM   578  N  N   . SER A 1 69  ? -7.39600  10.34200  74.19300 1.000 9.20843  ? 72  SER A N   1 
ATOM   579  C  CA  . SER A 1 69  ? -8.78800  9.97300   74.37300 1.000 9.71902  ? 72  SER A CA  1 
ATOM   580  C  C   . SER A 1 69  ? -9.63700  11.19800  74.64000 1.000 9.60059  ? 72  SER A C   1 
ATOM   581  O  O   . SER A 1 69  ? -9.19400  12.13500  75.29900 1.000 10.46385 ? 72  SER A O   1 
ATOM   582  C  CB  . SER A 1 69  ? -8.87000  9.08400   75.61200 1.000 11.44554 ? 72  SER A CB  1 
ATOM   583  O  OG  . SER A 1 69  ? -8.00900  7.95300   75.46500 1.000 13.01942 ? 72  SER A OG  1 
ATOM   584  N  N   . ARG A 1 70  ? -10.89300 11.14700  74.21100 1.000 10.26645 ? 73  ARG A N   1 
ATOM   585  C  CA  . ARG A 1 70  ? -11.84400 12.18400  74.59300 1.000 10.29277 ? 73  ARG A CA  1 
ATOM   586  C  C   . ARG A 1 70  ? -12.45400 11.81900  75.92800 1.000 10.64545 ? 73  ARG A C   1 
ATOM   587  O  O   . ARG A 1 70  ? -13.21000 10.85200  76.02900 1.000 11.31921 ? 73  ARG A O   1 
ATOM   588  C  CB  . ARG A 1 70  ? -12.94700 12.35300  73.55600 1.000 12.26933 ? 73  ARG A CB  1 
ATOM   589  C  CG  . ARG A 1 70  ? -13.83700 13.53700  73.95300 1.000 12.58252 ? 73  ARG A CG  1 
ATOM   590  C  CD  . ARG A 1 70  ? -14.91400 13.82600  72.90000 1.000 13.81951 ? 73  ARG A CD  1 
ATOM   591  N  NE  . ARG A 1 70  ? -15.96900 12.82100  72.86600 1.000 15.52235 ? 73  ARG A NE  1 
ATOM   592  C  CZ  . ARG A 1 70  ? -17.04300 12.83200  73.66500 1.000 17.51732 ? 73  ARG A CZ  1 
ATOM   593  N  NH1 . ARG A 1 70  ? -17.16200 13.70900  74.66200 1.000 18.42270 ? 73  ARG A NH1 1 
ATOM   594  N  NH2 . ARG A 1 70  ? -18.03900 11.97500  73.43200 1.000 19.08067 ? 73  ARG A NH2 1 
ATOM   595  N  N   . TYR A 1 71  ? -12.13800 12.61300  76.95500 1.000 10.34804 ? 74  TYR A N   1 
ATOM   596  C  CA  . TYR A 1 71  ? -12.81800 12.49600  78.24200 1.000 10.65334 ? 74  TYR A CA  1 
ATOM   597  C  C   . TYR A 1 71  ? -13.94600 13.51900  78.26800 1.000 10.84547 ? 74  TYR A C   1 
ATOM   598  O  O   . TYR A 1 71  ? -13.65500 14.73000  78.18400 1.000 12.37723 ? 74  TYR A O   1 
ATOM   599  C  CB  . TYR A 1 71  ? -11.86300 12.74200  79.42500 1.000 11.33764 ? 74  TYR A CB  1 
ATOM   600  C  CG  . TYR A 1 71  ? -11.13400 11.45500  79.82800 1.000 11.45870 ? 74  TYR A CG  1 
ATOM   601  C  CD1 . TYR A 1 71  ? -10.14700 10.90800  79.01900 1.000 9.79798  ? 74  TYR A CD1 1 
ATOM   602  C  CD2 . TYR A 1 71  ? -11.49100 10.76600  80.99000 1.000 12.24827 ? 74  TYR A CD2 1 
ATOM   603  C  CE1 . TYR A 1 71  ? -9.49900  9.73700   79.34200 1.000 10.63229 ? 74  TYR A CE1 1 
ATOM   604  C  CE2 . TYR A 1 71  ? -10.87900 9.56400   81.31500 1.000 10.68493 ? 74  TYR A CE2 1 
ATOM   605  C  CZ  . TYR A 1 71  ? -9.89700  9.05400   80.48500 1.000 10.74546 ? 74  TYR A CZ  1 
ATOM   606  O  OH  . TYR A 1 71  ? -9.27100  7.83200   80.78900 1.000 11.15867 ? 74  TYR A OH  1 
ATOM   607  N  N   . PRO A 1 72  ? -15.20700 13.09500  78.37800 1.000 10.95338 ? 75  PRO A N   1 
ATOM   608  C  CA  . PRO A 1 72  ? -16.29600 14.06700  78.54100 1.000 10.86916 ? 75  PRO A CA  1 
ATOM   609  C  C   . PRO A 1 72  ? -16.01900 14.95500  79.73300 1.000 11.37975 ? 75  PRO A C   1 
ATOM   610  O  O   . PRO A 1 72  ? -15.35500 14.56500  80.71100 1.000 10.96654 ? 75  PRO A O   1 
ATOM   611  C  CB  . PRO A 1 72  ? -17.53600 13.19300  78.76300 1.000 13.01942 ? 75  PRO A CB  1 
ATOM   612  C  CG  . PRO A 1 72  ? -17.16200 11.84300  78.12800 1.000 13.42473 ? 75  PRO A CG  1 
ATOM   613  C  CD  . PRO A 1 72  ? -15.68500 11.69000  78.37100 1.000 11.81401 ? 75  PRO A CD  1 
ATOM   614  N  N   . ASP A 1 73  ? -16.55000 16.18200  79.66600 1.000 11.16656 ? 76  ASP A N   1 
ATOM   615  C  CA  . ASP A 1 73  ? -16.29800 17.13600  80.73300 1.000 11.36395 ? 76  ASP A CA  1 
ATOM   616  C  C   . ASP A 1 73  ? -16.59700 16.55900  82.11600 1.000 11.42449 ? 76  ASP A C   1 
ATOM   617  O  O   . ASP A 1 73  ? -15.82500 16.76500  83.06700 1.000 11.39027 ? 76  ASP A O   1 
ATOM   618  C  CB  . ASP A 1 73  ? -17.13600 18.37000  80.46700 1.000 12.56936 ? 76  ASP A CB  1 
ATOM   619  C  CG  . ASP A 1 73  ? -16.84000 19.42700  81.50000 1.000 14.16955 ? 76  ASP A CG  1 
ATOM   620  O  OD1 . ASP A 1 73  ? -15.79500 20.09000  81.34100 1.000 16.02767 ? 76  ASP A OD1 1 
ATOM   621  O  OD2 . ASP A 1 73  ? -17.60800 19.57300  82.49800 1.000 15.85660 ? 76  ASP A OD2 1 
ATOM   622  N  N   . HIS A 1 74  ? -17.69300 15.80300  82.23700 1.000 12.32723 ? 77  HIS A N   1 
ATOM   623  C  CA  . HIS A 1 74  ? -18.02100 15.30000  83.56400 1.000 14.24062 ? 77  HIS A CA  1 
ATOM   624  C  C   . HIS A 1 74  ? -17.02300 14.26900  84.07400 1.000 13.60106 ? 77  HIS A C   1 
ATOM   625  O  O   . HIS A 1 74  ? -17.09200 13.92400  85.25500 1.000 15.51708 ? 77  HIS A O   1 
ATOM   626  C  CB  . HIS A 1 74  ? -19.43000 14.68800  83.60800 1.000 18.17003 ? 77  HIS A CB  1 
ATOM   627  C  CG  . HIS A 1 74  ? -19.58300 13.38200  82.88800 1.000 26.41576 ? 77  HIS A CG  1 
ATOM   628  N  ND1 . HIS A 1 74  ? -19.87900 13.30300  81.53900 1.000 30.51996 ? 77  HIS A ND1 1 
ATOM   629  C  CD2 . HIS A 1 74  ? -19.56700 12.10900  83.34500 1.000 31.74996 ? 77  HIS A CD2 1 
ATOM   630  C  CE1 . HIS A 1 74  ? -19.98600 12.02900  81.19000 1.000 29.76616 ? 77  HIS A CE1 1 
ATOM   631  N  NE2 . HIS A 1 74  ? -19.79100 11.28600  82.26400 1.000 29.67404 ? 77  HIS A NE2 1 
ATOM   632  N  N   . MET A 1 75  ? -16.15000 13.74600  83.21100 1.000 12.13773 ? 78  MET A N   1 
ATOM   633  C  CA  . MET A 1 75  ? -15.14300 12.77300  83.57000 1.000 12.84308 ? 78  MET A CA  1 
ATOM   634  C  C   . MET A 1 75  ? -13.75100 13.36400  83.66900 1.000 12.51409 ? 78  MET A C   1 
ATOM   635  O  O   . MET A 1 75  ? -12.78700 12.62500  83.87400 1.000 12.87466 ? 78  MET A O   1 
ATOM   636  C  CB  . MET A 1 75  ? -15.10600 11.60800  82.53400 1.000 14.10112 ? 78  MET A CB  1 
ATOM   637  C  CG  . MET A 1 75  ? -16.34600 10.79400  82.53500 1.000 14.68541 ? 78  MET A CG  1 
ATOM   638  S  SD  . MET A 1 75  ? -16.29100 9.39000   81.45700 1.000 13.88268 ? 78  MET A SD  1 
ATOM   639  C  CE  . MET A 1 75  ? -14.93000 8.42800   82.14300 1.000 14.11955 ? 78  MET A CE  1 
ATOM   640  N  N   A LYS A 1 76  ? -13.63200 14.69800  83.55200 0.490 12.88996 ? 79  LYS A N   1 
ATOM   641  N  N   B LYS A 1 76  ? -13.58900 14.67600  83.50200 0.510 12.47725 ? 79  LYS A N   1 
ATOM   642  C  CA  A LYS A 1 76  ? -12.31800 15.34000  83.44300 0.490 13.32996 ? 79  LYS A CA  1 
ATOM   643  C  CA  B LYS A 1 76  ? -12.21400 15.16500  83.36700 0.510 12.97467 ? 79  LYS A CA  1 
ATOM   644  C  C   A LYS A 1 76  ? -11.42600 15.00900  84.63000 0.490 11.06996 ? 79  LYS A C   1 
ATOM   645  C  C   B LYS A 1 76  ? -11.40000 15.13200  84.66400 0.510 13.72476 ? 79  LYS A C   1 
ATOM   646  O  O   A LYS A 1 76  ? -10.20600 14.83800  84.47700 0.490 11.05996 ? 79  LYS A O   1 
ATOM   647  O  O   B LYS A 1 76  ? -10.16700 15.27300  84.61200 0.510 14.69856 ? 79  LYS A O   1 
ATOM   648  C  CB  A LYS A 1 76  ? -12.47900 16.85500  83.29300 0.490 16.26996 ? 79  LYS A CB  1 
ATOM   649  C  CB  B LYS A 1 76  ? -12.20100 16.51200  82.67300 0.510 13.49842 ? 79  LYS A CB  1 
ATOM   650  C  CG  A LYS A 1 76  ? -13.16500 17.59000  84.40900 0.490 16.05996 ? 79  LYS A CG  1 
ATOM   651  C  CG  B LYS A 1 76  ? -12.65700 16.43000  81.22400 0.510 13.99585 ? 79  LYS A CG  1 
ATOM   652  C  CD  A LYS A 1 76  ? -13.43700 19.02100  83.93100 0.490 20.64996 ? 79  LYS A CD  1 
ATOM   653  C  CD  B LYS A 1 76  ? -12.44800 17.72000  80.50600 0.510 14.55381 ? 79  LYS A CD  1 
ATOM   654  C  CE  A LYS A 1 76  ? -14.28800 19.80900  84.87500 0.490 21.11996 ? 79  LYS A CE  1 
ATOM   655  C  CE  B LYS A 1 76  ? -12.52100 17.51600  79.06100 0.510 14.88806 ? 79  LYS A CE  1 
ATOM   656  N  NZ  A LYS A 1 76  ? -15.66000 19.26100  84.97200 0.490 20.30996 ? 79  LYS A NZ  1 
ATOM   657  N  NZ  B LYS A 1 76  ? -12.18800 18.74900  78.32300 0.510 14.84858 ? 79  LYS A NZ  1 
ATOM   658  N  N   . ARG A 1 77  ? -12.02000 14.90400  85.81500 1.000 13.33261 ? 80  ARG A N   1 
ATOM   659  C  CA  A ARG A 1 77  ? -11.21900 14.69700  87.02400 0.530 14.62224 ? 80  ARG A CA  1 
ATOM   660  C  CA  B ARG A 1 77  ? -11.14900 14.73700  86.97300 0.470 14.08996 ? 80  ARG A CA  1 
ATOM   661  C  C   . ARG A 1 77  ? -10.57900 13.32800  87.04500 1.000 15.10651 ? 80  ARG A C   1 
ATOM   662  O  O   . ARG A 1 77  ? -9.83200  13.02200  87.96900 1.000 18.77274 ? 80  ARG A O   1 
ATOM   663  C  CB  A ARG A 1 77  ? -12.11400 14.85000  88.27400 0.530 15.62499 ? 80  ARG A CB  1 
ATOM   664  C  CB  B ARG A 1 77  ? -11.89700 15.12800  88.25600 0.470 18.34996 ? 80  ARG A CB  1 
ATOM   665  C  CG  A ARG A 1 77  ? -11.33000 15.04700  89.57400 0.530 17.21729 ? 80  ARG A CG  1 
ATOM   666  C  CG  B ARG A 1 77  ? -13.04700 14.21800  88.54500 0.470 23.94996 ? 80  ARG A CG  1 
ATOM   667  C  CD  A ARG A 1 77  ? -12.25500 15.30600  90.77100 0.530 18.71220 ? 80  ARG A CD  1 
ATOM   668  C  CD  B ARG A 1 77  ? -13.81700 14.58200  89.81100 0.470 26.60996 ? 80  ARG A CD  1 
ATOM   669  N  NE  A ARG A 1 77  ? -12.71700 14.04300  91.34100 0.530 19.62021 ? 80  ARG A NE  1 
ATOM   670  N  NE  B ARG A 1 77  ? -12.94100 14.68200  90.97100 0.470 21.97996 ? 80  ARG A NE  1 
ATOM   671  C  CZ  A ARG A 1 77  ? -11.99200 13.30700  92.18000 0.530 21.59676 ? 80  ARG A CZ  1 
ATOM   672  C  CZ  B ARG A 1 77  ? -12.77300 13.73400  91.88100 0.470 19.33996 ? 80  ARG A CZ  1 
ATOM   673  N  NH1 A ARG A 1 77  ? -10.75400 13.64500  92.49000 0.530 22.35211 ? 80  ARG A NH1 1 
ATOM   674  N  NH1 B ARG A 1 77  ? -13.39500 12.56800  91.78900 0.470 32.92996 ? 80  ARG A NH1 1 
ATOM   675  N  NH2 A ARG A 1 77  ? -12.52700 12.20900  92.72900 0.530 22.09156 ? 80  ARG A NH2 1 
ATOM   676  N  NH2 B ARG A 1 77  ? -11.95400 13.95900  92.90400 0.470 34.60996 ? 80  ARG A NH2 1 
ATOM   677  N  N   . HIS A 1 78  ? -10.90000 12.49400  86.06600 1.000 13.37999 ? 81  HIS A N   1 
ATOM   678  C  CA  A HIS A 1 78  ? -10.51600 11.09100  85.97200 0.440 15.16996 ? 81  HIS A CA  1 
ATOM   679  C  CA  B HIS A 1 78  ? -10.36300 11.15300  86.10200 0.560 13.01152 ? 81  HIS A CA  1 
ATOM   680  C  C   . HIS A 1 78  ? -9.53500  10.84200  84.85400 1.000 12.46145 ? 81  HIS A C   1 
ATOM   681  O  O   . HIS A 1 78  ? -9.30300  9.68500   84.52200 1.000 13.23260 ? 81  HIS A O   1 
ATOM   682  C  CB  A HIS A 1 78  ? -11.74300 10.18200  85.75100 0.440 14.18996 ? 81  HIS A CB  1 
ATOM   683  C  CB  B HIS A 1 78  ? -11.48900 10.18500  86.42700 0.560 14.04849 ? 81  HIS A CB  1 
ATOM   684  C  CG  A HIS A 1 78  ? -12.71500 10.26700  86.86600 0.440 11.66996 ? 81  HIS A CG  1 
ATOM   685  C  CG  B HIS A 1 78  ? -12.15100 10.45800  87.75700 0.560 13.68529 ? 81  HIS A CG  1 
ATOM   686  N  ND1 A HIS A 1 78  ? -12.64900 9.45000   87.98400 0.440 12.82996 ? 81  HIS A ND1 1 
ATOM   687  N  ND1 B HIS A 1 78  ? -11.53800 10.19500  88.97000 0.560 15.69079 ? 81  HIS A ND1 1 
ATOM   688  C  CD2 A HIS A 1 78  ? -13.69200 11.16700  87.10000 0.440 20.08996 ? 81  HIS A CD2 1 
ATOM   689  C  CD2 B HIS A 1 78  ? -13.40200 10.89900  88.05500 0.560 13.92216 ? 81  HIS A CD2 1 
ATOM   690  C  CE1 A HIS A 1 78  ? -13.58600 9.83400   88.83500 0.440 21.39996 ? 81  HIS A CE1 1 
ATOM   691  C  CE1 B HIS A 1 78  ? -12.37700 10.48000  89.95200 0.560 15.66184 ? 81  HIS A CE1 1 
ATOM   692  N  NE2 A HIS A 1 78  ? -14.23000 10.86800  88.31800 0.440 13.13996 ? 81  HIS A NE2 1 
ATOM   693  N  NE2 B HIS A 1 78  ? -13.50900 10.91600  89.42600 0.560 15.28285 ? 81  HIS A NE2 1 
ATOM   694  N  N   . ASP A 1 79  ? -9.01300  11.88400  84.19900 1.000 10.01642 ? 82  ASP A N   1 
ATOM   695  C  CA  . ASP A 1 79  ? -8.14000  11.69800  83.02400 1.000 10.35331 ? 82  ASP A CA  1 
ATOM   696  C  C   . ASP A 1 79  ? -6.68700  11.66800  83.44000 1.000 10.11380 ? 82  ASP A C   1 
ATOM   697  O  O   . ASP A 1 79  ? -6.00400  12.69200  83.51300 1.000 9.96905  ? 82  ASP A O   1 
ATOM   698  C  CB  . ASP A 1 79  ? -8.41400  12.79800  82.01800 1.000 10.72704 ? 82  ASP A CB  1 
ATOM   699  C  CG  . ASP A 1 79  ? -7.63400  12.64600  80.73100 1.000 10.19276 ? 82  ASP A CG  1 
ATOM   700  O  OD1 . ASP A 1 79  ? -6.74100  11.78500  80.62800 1.000 10.47964 ? 82  ASP A OD1 1 
ATOM   701  O  OD2 . ASP A 1 79  ? -7.99100  13.44100  79.79500 1.000 10.62439 ? 82  ASP A OD2 1 
ATOM   702  N  N   . PHE A 1 80  ? -6.23600  10.46300  83.79200 1.000 9.74797  ? 83  PHE A N   1 
ATOM   703  C  CA  . PHE A 1 80  ? -4.87100  10.28300  84.26200 1.000 9.16369  ? 83  PHE A CA  1 
ATOM   704  C  C   . PHE A 1 80  ? -3.88300  10.64400  83.16700 1.000 9.41898  ? 83  PHE A C   1 
ATOM   705  O  O   . PHE A 1 80  ? -2.85100  11.26200  83.43300 1.000 8.90577  ? 83  PHE A O   1 
ATOM   706  C  CB  . PHE A 1 80  ? -4.65100  8.79600   84.65900 1.000 9.57163  ? 83  PHE A CB  1 
ATOM   707  C  CG  . PHE A 1 80  ? -3.19900  8.46000   84.84700 1.000 9.44267  ? 83  PHE A CG  1 
ATOM   708  C  CD1 . PHE A 1 80  ? -2.55300  8.73500   86.08600 1.000 10.97707 ? 83  PHE A CD1 1 
ATOM   709  C  CD2 . PHE A 1 80  ? -2.45100  7.87300   83.81700 1.000 10.12960 ? 83  PHE A CD2 1 
ATOM   710  C  CE1 . PHE A 1 80  ? -1.21500  8.47400   86.23200 1.000 11.44554 ? 83  PHE A CE1 1 
ATOM   711  C  CE2 . PHE A 1 80  ? -1.06900  7.60300   83.96900 1.000 10.68756 ? 83  PHE A CE2 1 
ATOM   712  C  CZ  . PHE A 1 80  ? -0.45900  7.90800   85.17600 1.000 11.08234 ? 83  PHE A CZ  1 
ATOM   713  N  N   . PHE A 1 81  ? -4.15000  10.18700  81.93200 1.000 9.67428  ? 84  PHE A N   1 
ATOM   714  C  CA  . PHE A 1 81  ? -3.14800  10.23300  80.88600 1.000 9.16632  ? 84  PHE A CA  1 
ATOM   715  C  C   . PHE A 1 81  ? -2.73500  11.66000  80.58300 1.000 9.72955  ? 84  PHE A C   1 
ATOM   716  O  O   . PHE A 1 81  ? -1.53800  11.94000  80.44100 1.000 10.15855 ? 84  PHE A O   1 
ATOM   717  C  CB  . PHE A 1 81  ? -3.69600  9.59800   79.61200 1.000 8.47677  ? 84  PHE A CB  1 
ATOM   718  C  CG  . PHE A 1 81  ? -4.18900  8.19900   79.81400 1.000 9.32687  ? 84  PHE A CG  1 
ATOM   719  C  CD1 . PHE A 1 81  ? -3.30300  7.15100   79.85900 1.000 10.29014 ? 84  PHE A CD1 1 
ATOM   720  C  CD2 . PHE A 1 81  ? -5.56500  7.94800   79.91800 1.000 10.87705 ? 84  PHE A CD2 1 
ATOM   721  C  CE1 . PHE A 1 81  ? -3.76000  5.84200   80.00100 1.000 11.27710 ? 84  PHE A CE1 1 
ATOM   722  C  CE2 . PHE A 1 81  ? -6.06300  6.63800   80.05900 1.000 11.26394 ? 84  PHE A CE2 1 
ATOM   723  C  CZ  . PHE A 1 81  ? -5.13400  5.58200   80.11500 1.000 11.53240 ? 84  PHE A CZ  1 
ATOM   724  N  N   . LYS A 1 82  ? -3.71000  12.58800  80.46100 1.000 9.29792  ? 85  LYS A N   1 
ATOM   725  C  CA  . LYS A 1 82  ? -3.31600  13.97400  80.23200 1.000 9.66901  ? 85  LYS A CA  1 
ATOM   726  C  C   . LYS A 1 82  ? -2.69300  14.56700  81.47800 1.000 9.56637  ? 85  LYS A C   1 
ATOM   727  O  O   . LYS A 1 82  ? -1.79200  15.40400  81.37600 1.000 10.26909 ? 85  LYS A O   1 
ATOM   728  C  CB  . LYS A 1 82  ? -4.49700  14.83400  79.81800 1.000 10.44806 ? 85  LYS A CB  1 
ATOM   729  C  CG  . LYS A 1 82  ? -5.03200  14.46000  78.42600 1.000 10.72704 ? 85  LYS A CG  1 
ATOM   730  C  CD  . LYS A 1 82  ? -6.12500  15.44600  78.00100 1.000 10.50069 ? 85  LYS A CD  1 
ATOM   731  C  CE  . LYS A 1 82  ? -6.90100  14.97400  76.76700 1.000 10.75599 ? 85  LYS A CE  1 
ATOM   732  N  NZ  . LYS A 1 82  ? -7.53500  13.60500  77.02700 1.000 10.63492 ? 85  LYS A NZ  1 
ATOM   733  N  N   . SER A 1 83  ? -3.16800  14.17600  82.66900 1.000 9.66375  ? 86  SER A N   1 
ATOM   734  C  CA  . SER A 1 83  ? -2.69600  14.86000  83.87100 1.000 10.04801 ? 86  SER A CA  1 
ATOM   735  C  C   . SER A 1 83  ? -1.20000  14.69100  84.07100 1.000 10.63755 ? 86  SER A C   1 
ATOM   736  O  O   . SER A 1 83  ? -0.55100  15.57400  84.67500 1.000 11.49292 ? 86  SER A O   1 
ATOM   737  C  CB  . SER A 1 83  ? -3.48800  14.31300  85.09300 1.000 10.19803 ? 86  SER A CB  1 
ATOM   738  O  OG  . SER A 1 83  ? -3.00200  13.02200  85.55800 1.000 10.47437 ? 86  SER A OG  1 
ATOM   739  N  N   . ALA A 1 84  ? -0.61500  13.58700  83.60900 1.000 9.96379  ? 87  ALA A N   1 
ATOM   740  C  CA  . ALA A 1 84  ? 0.81200   13.34700  83.79900 1.000 9.84798  ? 87  ALA A CA  1 
ATOM   741  C  C   . ALA A 1 84  ? 1.69000   14.19500  82.89500 1.000 9.53216  ? 87  ALA A C   1 
ATOM   742  O  O   . ALA A 1 84  ? 2.92900   14.22900  83.07300 1.000 10.58491 ? 87  ALA A O   1 
ATOM   743  C  CB  . ALA A 1 84  ? 1.09800   11.85500  83.55200 1.000 11.05076 ? 87  ALA A CB  1 
ATOM   744  N  N   . MET A 1 85  ? 1.10600   14.82600  81.86100 1.000 9.91641  ? 88  MET A N   1 
ATOM   745  C  CA  . MET A 1 85  ? 1.87400   15.59100  80.87500 1.000 10.15855 ? 88  MET A CA  1 
ATOM   746  C  C   . MET A 1 85  ? 2.21700   16.96100  81.45600 1.000 10.95864 ? 88  MET A C   1 
ATOM   747  O  O   . MET A 1 85  ? 1.49700   17.49100  82.31800 1.000 10.76915 ? 88  MET A O   1 
ATOM   748  C  CB  . MET A 1 85  ? 1.02800   15.73400  79.60800 1.000 10.36120 ? 88  MET A CB  1 
ATOM   749  C  CG  . MET A 1 85  ? 0.73400   14.38700  78.99700 1.000 10.87442 ? 88  MET A CG  1 
ATOM   750  S  SD  . MET A 1 85  ? 2.26900   13.59200  78.41600 1.000 10.33488 ? 88  MET A SD  1 
ATOM   751  C  CE  . MET A 1 85  ? 1.71600   11.93200  78.27500 1.000 11.54556 ? 88  MET A CE  1 
ATOM   752  N  N   . PRO A 1 86  ? 3.35100   17.57200  81.01700 1.000 11.11392 ? 89  PRO A N   1 
ATOM   753  C  CA  . PRO A 1 86  ? 4.17800   17.11300  79.88300 1.000 11.60609 ? 89  PRO A CA  1 
ATOM   754  C  C   . PRO A 1 86  ? 5.25600   16.10600  80.23000 1.000 11.05865 ? 89  PRO A C   1 
ATOM   755  O  O   . PRO A 1 86  ? 5.86000   15.52500  79.31100 1.000 11.24815 ? 89  PRO A O   1 
ATOM   756  C  CB  . PRO A 1 86  ? 4.82300   18.43200  79.39700 1.000 12.74833 ? 89  PRO A CB  1 
ATOM   757  C  CG  . PRO A 1 86  ? 4.97700   19.24700  80.69900 1.000 12.81676 ? 89  PRO A CG  1 
ATOM   758  C  CD  . PRO A 1 86  ? 3.66500   18.96300  81.40800 1.000 12.19037 ? 89  PRO A CD  1 
ATOM   759  N  N   . GLU A 1 87  ? 5.51500   15.88100  81.52700 1.000 11.62714 ? 90  GLU A N   1 
ATOM   760  C  CA  . GLU A 1 87  ? 6.57900   14.96100  81.94800 1.000 11.91139 ? 90  GLU A CA  1 
ATOM   761  C  C   . GLU A 1 87  ? 6.29300   13.54500  81.49600 1.000 11.32974 ? 90  GLU A C   1 
ATOM   762  O  O   . GLU A 1 87  ? 7.23000   12.80400  81.12000 1.000 12.73780 ? 90  GLU A O   1 
ATOM   763  C  CB  . GLU A 1 87  ? 6.75700   14.97900  83.47400 1.000 13.56422 ? 90  GLU A CB  1 
ATOM   764  C  CG  . GLU A 1 87  ? 7.22400   16.34900  84.01700 1.000 15.56183 ? 90  GLU A CG  1 
ATOM   765  C  CD  . GLU A 1 87  ? 6.08700   17.30400  84.29500 1.000 16.83830 ? 90  GLU A CD  1 
ATOM   766  O  OE1 . GLU A 1 87  ? 4.93000   17.10600  83.89900 1.000 14.62224 ? 90  GLU A OE1 1 
ATOM   767  O  OE2 . GLU A 1 87  ? 6.36200   18.29900  85.01300 1.000 20.98090 ? 90  GLU A OE2 1 
ATOM   768  N  N   . GLY A 1 88  ? 5.01600   13.15900  81.49000 1.000 10.71124 ? 91  GLY A N   1 
ATOM   769  C  CA  . GLY A 1 88  ? 4.58200   11.92800  80.86700 1.000 10.88495 ? 91  GLY A CA  1 
ATOM   770  C  C   . GLY A 1 88  ? 4.44900   10.77300  81.82800 1.000 10.02958 ? 91  GLY A C   1 
ATOM   771  O  O   . GLY A 1 88  ? 4.39600   10.91300  83.05300 1.000 10.50859 ? 91  GLY A O   1 
ATOM   772  N  N   . TYR A 1 89  ? 4.37300   9.59000   81.21600 1.000 9.92694  ? 92  TYR A N   1 
ATOM   773  C  CA  . TYR A 1 89  ? 4.19300   8.35200   81.93800 1.000 10.14012 ? 92  TYR A CA  1 
ATOM   774  C  C   . TYR A 1 89  ? 4.92000   7.23200   81.19800 1.000 9.46636  ? 92  TYR A C   1 
ATOM   775  O  O   . TYR A 1 89  ? 5.16700   7.28600   79.98100 1.000 9.52689  ? 92  TYR A O   1 
ATOM   776  C  CB  . TYR A 1 89  ? 2.71700   7.98000   82.14400 1.000 10.20592 ? 92  TYR A CB  1 
ATOM   777  C  CG  . TYR A 1 89  ? 1.84500   7.98700   80.92300 1.000 9.12948  ? 92  TYR A CG  1 
ATOM   778  C  CD1 . TYR A 1 89  ? 1.86100   6.91800   80.03600 1.000 10.19276 ? 92  TYR A CD1 1 
ATOM   779  C  CD2 . TYR A 1 89  ? 0.98300   9.06900   80.64700 1.000 10.58755 ? 92  TYR A CD2 1 
ATOM   780  C  CE1 . TYR A 1 89  ? 1.04200   6.93500   78.88300 1.000 9.56111  ? 92  TYR A CE1 1 
ATOM   781  C  CE2 . TYR A 1 89  ? 0.19000   9.09900   79.50200 1.000 10.91390 ? 92  TYR A CE2 1 
ATOM   782  C  CZ  . TYR A 1 89  ? 0.20400   8.02100   78.62900 1.000 9.90588  ? 92  TYR A CZ  1 
ATOM   783  O  OH  . TYR A 1 89  ? -0.61300  8.04000   77.53300 1.000 10.01642 ? 92  TYR A OH  1 
ATOM   784  N  N   . VAL A 1 90  ? 5.20400   6.19000   81.96800 1.000 9.20580  ? 93  VAL A N   1 
ATOM   785  C  CA  . VAL A 1 90  ? 5.68400   4.93100   81.42400 1.000 10.05590 ? 93  VAL A CA  1 
ATOM   786  C  C   . VAL A 1 90  ? 4.48300   4.02100   81.27600 1.000 10.12170 ? 93  VAL A C   1 
ATOM   787  O  O   . VAL A 1 90  ? 3.65000   3.91500   82.18100 1.000 12.72201 ? 93  VAL A O   1 
ATOM   788  C  CB  . VAL A 1 90  ? 6.76900   4.31900   82.32800 1.000 11.25605 ? 93  VAL A CB  1 
ATOM   789  C  CG1 . VAL A 1 90  ? 7.18900   2.90500   81.87500 1.000 12.14300 ? 93  VAL A CG1 1 
ATOM   790  C  CG2 . VAL A 1 90  ? 8.01100   5.26900   82.34600 1.000 13.87741 ? 93  VAL A CG2 1 
ATOM   791  N  N   . GLN A 1 91  ? 4.38500   3.35400   80.13200 1.000 9.29792  ? 94  GLN A N   1 
ATOM   792  C  CA  . GLN A 1 91  ? 3.29500   2.43200   79.85100 1.000 9.17685  ? 94  GLN A CA  1 
ATOM   793  C  C   . GLN A 1 91  ? 3.92800   1.08400   79.54800 1.000 9.18738  ? 94  GLN A C   1 
ATOM   794  O  O   . GLN A 1 91  ? 4.72300   0.97600   78.60500 1.000 9.62164  ? 94  GLN A O   1 
ATOM   795  C  CB  . GLN A 1 91  ? 2.45000   2.90300   78.66400 1.000 9.33740  ? 94  GLN A CB  1 
ATOM   796  C  CG  . GLN A 1 91  ? 1.34700   1.95400   78.28600 1.000 9.76903  ? 94  GLN A CG  1 
ATOM   797  C  CD  . GLN A 1 91  ? 0.29000   2.64700   77.44900 1.000 9.23212  ? 94  GLN A CD  1 
ATOM   798  O  OE1 . GLN A 1 91  ? -0.31100  3.63900   77.86500 1.000 10.74546 ? 94  GLN A OE1 1 
ATOM   799  N  NE2 . GLN A 1 91  ? 0.03000   2.13700   76.24200 1.000 10.02958 ? 94  GLN A NE2 1 
ATOM   800  N  N   . GLU A 1 92  ? 3.57700   0.08300   80.34900 1.000 9.01104  ? 95  GLU A N   1 
ATOM   801  C  CA  A GLU A 1 92  ? 4.08600   -1.26000  80.13800 0.610 10.42174 ? 95  GLU A CA  1 
ATOM   802  C  CA  B GLU A 1 92  ? 4.08900   -1.27600  80.19600 0.390 8.98996  ? 95  GLU A CA  1 
ATOM   803  C  C   . GLU A 1 92  ? 2.92800   -2.20400  79.89300 1.000 9.55321  ? 95  GLU A C   1 
ATOM   804  O  O   . GLU A 1 92  ? 1.88600   -2.09500  80.54100 1.000 10.81652 ? 95  GLU A O   1 
ATOM   805  C  CB  A GLU A 1 92  ? 4.84000   -1.70600  81.35300 0.610 12.94309 ? 95  GLU A CB  1 
ATOM   806  C  CB  B GLU A 1 92  ? 4.72100   -1.75700  81.49900 0.390 8.81996  ? 95  GLU A CB  1 
ATOM   807  C  CG  A GLU A 1 92  ? 6.11400   -0.90000  81.55700 0.610 15.87239 ? 95  GLU A CG  1 
ATOM   808  C  CG  B GLU A 1 92  ? 5.95500   -0.97600  81.94200 0.390 11.59996 ? 95  GLU A CG  1 
ATOM   809  C  CD  A GLU A 1 92  ? 6.73900   -1.16600  82.90400 0.610 18.43322 ? 95  GLU A CD  1 
ATOM   810  C  CD  B GLU A 1 92  ? 6.37200   -1.28700  83.37100 0.390 30.38996 ? 95  GLU A CD  1 
ATOM   811  O  OE1 A GLU A 1 92  ? 6.02300   -0.95400  83.92400 0.610 19.74127 ? 95  GLU A OE1 1 
ATOM   812  O  OE1 B GLU A 1 92  ? 6.62300   -2.47600  83.69000 0.390 18.44996 ? 95  GLU A OE1 1 
ATOM   813  O  OE2 A GLU A 1 92  ? 7.90800   -1.62300  82.93300 0.610 18.38322 ? 95  GLU A OE2 1 
ATOM   814  O  OE2 B GLU A 1 92  ? 6.44300   -0.32600  84.17600 0.390 29.21996 ? 95  GLU A OE2 1 
ATOM   815  N  N   . ARG A 1 93  ? 3.11800   -3.14400  78.97300 1.000 8.91629  ? 96  ARG A N   1 
ATOM   816  C  CA  . ARG A 1 93  ? 2.08900   -4.12200  78.73300 1.000 8.63994  ? 96  ARG A CA  1 
ATOM   817  C  C   . ARG A 1 93  ? 2.70400   -5.49600  78.53800 1.000 8.65047  ? 96  ARG A C   1 
ATOM   818  O  O   . ARG A 1 93  ? 3.85900   -5.64100  78.08300 1.000 9.33213  ? 96  ARG A O   1 
ATOM   819  C  CB  . ARG A 1 93  ? 1.27500   -3.87100  77.44900 1.000 9.13737  ? 96  ARG A CB  1 
ATOM   820  C  CG  . ARG A 1 93  ? 0.40800   -2.61200  77.45400 1.000 8.61626  ? 96  ARG A CG  1 
ATOM   821  C  CD  . ARG A 1 93  ? -0.80800  -2.84800  76.64800 1.000 9.17685  ? 96  ARG A CD  1 
ATOM   822  N  NE  . ARG A 1 93  ? -1.72400  -1.70100  76.55900 1.000 8.78733  ? 96  ARG A NE  1 
ATOM   823  C  CZ  . ARG A 1 93  ? -1.71600  -0.79300  75.59100 1.000 8.35307  ? 96  ARG A CZ  1 
ATOM   824  N  NH1 . ARG A 1 93  ? -0.79800  -0.81300  74.62400 1.000 9.74008  ? 96  ARG A NH1 1 
ATOM   825  N  NH2 . ARG A 1 93  ? -2.66100  0.15500   75.58800 1.000 9.09263  ? 96  ARG A NH2 1 
ATOM   826  N  N   . THR A 1 94  ? 1.88500   -6.51500  78.83500 1.000 8.35570  ? 97  THR A N   1 
ATOM   827  C  CA  . THR A 1 94  ? 2.07600   -7.83100  78.25100 1.000 8.88471  ? 97  THR A CA  1 
ATOM   828  C  C   . THR A 1 94  ? 0.85800   -8.12700  77.39000 1.000 8.54256  ? 97  THR A C   1 
ATOM   829  O  O   . THR A 1 94  ? -0.29500  -7.96200  77.84100 1.000 8.60573  ? 97  THR A O   1 
ATOM   830  C  CB  . THR A 1 94  ? 2.22700   -8.93400  79.32100 1.000 9.33740  ? 97  THR A CB  1 
ATOM   831  O  OG1 . THR A 1 94  ? 3.28500   -8.55900  80.20100 1.000 10.06380 ? 97  THR A OG1 1 
ATOM   832  C  CG2 . THR A 1 94  ? 2.50400   -10.29000 78.64100 1.000 10.24803 ? 97  THR A CG2 1 
ATOM   833  N  N   . ILE A 1 95  ? 1.12400   -8.54400  76.14600 1.000 8.12409  ? 98  ILE A N   1 
ATOM   834  C  CA  . ILE A 1 95  ? 0.06700   -8.90200  75.19700 1.000 8.55046  ? 98  ILE A CA  1 
ATOM   835  C  C   . ILE A 1 95  ? 0.25000   -10.40300 74.96900 1.000 8.43202  ? 98  ILE A C   1 
ATOM   836  O  O   . ILE A 1 95  ? 1.28200   -10.83900 74.42800 1.000 9.13474  ? 98  ILE A O   1 
ATOM   837  C  CB  . ILE A 1 95  ? 0.20300   -8.13300  73.86700 1.000 9.14000  ? 98  ILE A CB  1 
ATOM   838  C  CG1 . ILE A 1 95  ? 0.06800   -6.61900  74.11700 1.000 9.10842  ? 98  ILE A CG1 1 
ATOM   839  C  CG2 . ILE A 1 95  ? -0.87600  -8.66100  72.89000 1.000 9.05315  ? 98  ILE A CG2 1 
ATOM   840  C  CD1 . ILE A 1 95  ? 0.37900   -5.73500  72.92600 1.000 9.74271  ? 98  ILE A CD1 1 
ATOM   841  N  N   . SER A 1 96  ? -0.72200  -11.19400 75.44000 1.000 8.58731  ? 99  SER A N   1 
ATOM   842  C  CA  . SER A 1 96  ? -0.59800  -12.67300 75.42400 1.000 8.72943  ? 99  SER A CA  1 
ATOM   843  C  C   . SER A 1 96  ? -1.50300  -13.17700 74.31500 1.000 8.41886  ? 99  SER A C   1 
ATOM   844  O  O   . SER A 1 96  ? -2.72900  -13.05300 74.39400 1.000 8.81891  ? 99  SER A O   1 
ATOM   845  C  CB  . SER A 1 96  ? -1.07300  -13.20900 76.77300 1.000 9.68481  ? 99  SER A CB  1 
ATOM   846  O  OG  . SER A 1 96  ? -0.29500  -12.62700 77.82000 1.000 10.37436 ? 99  SER A OG  1 
ATOM   847  N  N   . PHE A 1 97  ? -0.89100  -13.68100 73.23800 1.000 8.66100  ? 100 PHE A N   1 
ATOM   848  C  CA  . PHE A 1 97  ? -1.68700  -14.23000 72.14500 1.000 8.88997  ? 100 PHE A CA  1 
ATOM   849  C  C   . PHE A 1 97  ? -2.07800  -15.66200 72.51300 1.000 8.85839  ? 100 PHE A C   1 
ATOM   850  O  O   . PHE A 1 97  ? -1.20400  -16.50000 72.72900 1.000 9.35582  ? 100 PHE A O   1 
ATOM   851  C  CB  . PHE A 1 97  ? -0.88300  -14.21500 70.84900 1.000 9.00315  ? 100 PHE A CB  1 
ATOM   852  C  CG  . PHE A 1 97  ? -0.58700  -12.80600 70.39400 1.000 8.58731  ? 100 PHE A CG  1 
ATOM   853  C  CD1 . PHE A 1 97  ? -1.52000  -12.09700 69.63000 1.000 8.90050  ? 100 PHE A CD1 1 
ATOM   854  C  CD2 . PHE A 1 97  ? 0.59800   -12.17000 70.78200 1.000 8.96893  ? 100 PHE A CD2 1 
ATOM   855  C  CE1 . PHE A 1 97  ? -1.26100  -10.79600 69.20800 1.000 8.97156  ? 100 PHE A CE1 1 
ATOM   856  C  CE2 . PHE A 1 97  ? 0.87400   -10.85100 70.39200 1.000 8.23990  ? 100 PHE A CE2 1 
ATOM   857  C  CZ  . PHE A 1 97  ? -0.04800  -10.16800 69.58500 1.000 8.86892  ? 100 PHE A CZ  1 
ATOM   858  N  N   . LYS A 1 98  ? -3.37900  -15.93000 72.60600 1.000 8.90577  ? 101 LYS A N   1 
ATOM   859  C  CA  . LYS A 1 98  ? -3.86400  -17.24200 73.05200 1.000 9.27686  ? 101 LYS A CA  1 
ATOM   860  C  C   . LYS A 1 98  ? -3.21900  -18.33100 72.22000 1.000 10.32962 ? 101 LYS A C   1 
ATOM   861  O  O   . LYS A 1 98  ? -3.23600  -18.28000 70.99300 1.000 10.54544 ? 101 LYS A O   1 
ATOM   862  C  CB  . LYS A 1 98  ? -5.36500  -17.29900 72.87500 1.000 10.09801 ? 101 LYS A CB  1 
ATOM   863  C  CG  . LYS A 1 98  ? -5.99100  -18.69100 73.20000 1.000 11.55871 ? 101 LYS A CG  1 
ATOM   864  C  CD  . LYS A 1 98  ? -5.94500  -19.03100 74.67700 1.000 12.87993 ? 101 LYS A CD  1 
ATOM   865  C  CE  . LYS A 1 98  ? -6.61100  -20.39300 74.92300 1.000 14.07217 ? 101 LYS A CE  1 
ATOM   866  N  NZ  . LYS A 1 98  ? -6.55900  -20.70200 76.39800 1.000 16.24086 ? 101 LYS A NZ  1 
ATOM   867  N  N   . ASP A 1 99  ? -2.66000  -19.33000 72.90600 1.000 10.58491 ? 102 ASP A N   1 
ATOM   868  C  CA  . ASP A 1 99  ? -2.02200  -20.49800 72.26600 1.000 11.80085 ? 102 ASP A CA  1 
ATOM   869  C  C   . ASP A 1 99  ? -0.87300  -20.09700 71.37100 1.000 11.50081 ? 102 ASP A C   1 
ATOM   870  O  O   . ASP A 1 99  ? -0.53500  -20.82700 70.45000 1.000 12.40618 ? 102 ASP A O   1 
ATOM   871  C  CB  . ASP A 1 99  ? -3.05500  -21.38700 71.55200 1.000 12.81676 ? 102 ASP A CB  1 
ATOM   872  C  CG  . ASP A 1 99  ? -3.96700  -22.10500 72.54800 1.000 13.27734 ? 102 ASP A CG  1 
ATOM   873  O  OD1 . ASP A 1 99  ? -3.55400  -22.32700 73.70900 1.000 15.08282 ? 102 ASP A OD1 1 
ATOM   874  O  OD2 . ASP A 1 99  ? -5.07800  -22.44300 72.17100 1.000 14.74068 ? 102 ASP A OD2 1 
ATOM   875  N  N   . ASP A 1 100 ? -0.20500  -19.00200 71.69900 1.000 10.63492 ? 103 ASP A N   1 
ATOM   876  C  CA  . ASP A 1 100 ? 0.96600   -18.54500 70.97300 1.000 10.25593 ? 103 ASP A CA  1 
ATOM   877  C  C   . ASP A 1 100 ? 1.80900   -17.72100 71.94300 1.000 10.82178 ? 103 ASP A C   1 
ATOM   878  O  O   . ASP A 1 100 ? 1.65600   -17.85000 73.15600 1.000 11.39817 ? 103 ASP A O   1 
ATOM   879  C  CB  . ASP A 1 100 ? 0.52600   -17.80600 69.68900 1.000 10.64282 ? 103 ASP A CB  1 
ATOM   880  C  CG  . ASP A 1 100 ? 1.53300   -17.83600 68.56600 1.000 11.14814 ? 103 ASP A CG  1 
ATOM   881  O  OD1 . ASP A 1 100 ? 2.75900   -17.99100 68.81000 1.000 10.77441 ? 103 ASP A OD1 1 
ATOM   882  O  OD2 . ASP A 1 100 ? 1.09000   -17.72000 67.39300 1.000 12.87203 ? 103 ASP A OD2 1 
ATOM   883  N  N   . GLY A 1 101 ? 2.72800   -16.93600 71.40100 1.000 9.54268  ? 104 GLY A N   1 
ATOM   884  C  CA  . GLY A 1 101 ? 3.67800   -16.21300 72.22200 1.000 9.57690  ? 104 GLY A CA  1 
ATOM   885  C  C   . GLY A 1 101 ? 3.07600   -14.94900 72.82000 1.000 9.53216  ? 104 GLY A C   1 
ATOM   886  O  O   . GLY A 1 101 ? 1.87800   -14.65600 72.72400 1.000 9.59795  ? 104 GLY A O   1 
ATOM   887  N  N   . ASN A 1 102 ? 3.98500   -14.14800 73.40900 1.000 9.85062  ? 105 ASN A N   1 
ATOM   888  C  CA  . ASN A 1 102 ? 3.56200   -12.88200 74.01300 1.000 9.67691  ? 105 ASN A CA  1 
ATOM   889  C  C   . ASN A 1 102 ? 4.53000   -11.76600 73.65600 1.000 9.00841  ? 105 ASN A C   1 
ATOM   890  O  O   . ASN A 1 102 ? 5.73700   -12.00700 73.47700 1.000 9.23738  ? 105 ASN A O   1 
ATOM   891  C  CB  . ASN A 1 102 ? 3.37600   -13.00700 75.53400 1.000 10.83231 ? 105 ASN A CB  1 
ATOM   892  C  CG  . ASN A 1 102 ? 4.63800   -13.35600 76.24000 1.000 11.79559 ? 105 ASN A CG  1 
ATOM   893  O  OD1 . ASN A 1 102 ? 5.44900   -12.48200 76.59900 1.000 13.33788 ? 105 ASN A OD1 1 
ATOM   894  N  ND2 . ASN A 1 102 ? 4.82900   -14.66100 76.46200 1.000 13.07995 ? 105 ASN A ND2 1 
ATOM   895  N  N   . TYR A 1 103 ? 3.97600   -10.55300 73.55800 1.000 8.80049  ? 106 TYR A N   1 
ATOM   896  C  CA  . TYR A 1 103 ? 4.77700   -9.34300  73.51100 1.000 9.14000  ? 106 TYR A CA  1 
ATOM   897  C  C   . TYR A 1 103 ? 4.85700   -8.74400  74.90600 1.000 8.52677  ? 106 TYR A C   1 
ATOM   898  O  O   . TYR A 1 103 ? 3.85200   -8.67800  75.61300 1.000 9.25054  ? 106 TYR A O   1 
ATOM   899  C  CB  . TYR A 1 103 ? 4.14200   -8.25500  72.62600 1.000 9.10053  ? 106 TYR A CB  1 
ATOM   900  C  CG  . TYR A 1 103 ? 3.91300   -8.55700  71.14600 1.000 8.73469  ? 106 TYR A CG  1 
ATOM   901  C  CD1 . TYR A 1 103 ? 4.64400   -9.54000  70.46000 1.000 9.19001  ? 106 TYR A CD1 1 
ATOM   902  C  CD2 . TYR A 1 103 ? 3.00300   -7.80800  70.43300 1.000 8.69258  ? 106 TYR A CD2 1 
ATOM   903  C  CE1 . TYR A 1 103 ? 4.46300   -9.75700  69.09200 1.000 8.78733  ? 106 TYR A CE1 1 
ATOM   904  C  CE2 . TYR A 1 103 ? 2.80800   -7.97700  69.08500 1.000 8.48466  ? 106 TYR A CE2 1 
ATOM   905  C  CZ  . TYR A 1 103 ? 3.54600   -8.96600  68.39100 1.000 8.79259  ? 106 TYR A CZ  1 
ATOM   906  O  OH  . TYR A 1 103 ? 3.41300   -9.19300  67.05800 1.000 9.67165  ? 106 TYR A OH  1 
ATOM   907  N  N   . LYS A 1 104 ? 6.02400   -8.19700  75.25900 1.000 8.61099  ? 107 LYS A N   1 
ATOM   908  C  CA  . LYS A 1 104 ? 6.13400   -7.31200  76.42600 1.000 9.24265  ? 107 LYS A CA  1 
ATOM   909  C  C   . LYS A 1 104 ? 6.67200   -5.98800  75.90900 1.000 8.61626  ? 107 LYS A C   1 
ATOM   910  O  O   . LYS A 1 104 ? 7.65200   -5.95600  75.14400 1.000 8.98735  ? 107 LYS A O   1 
ATOM   911  C  CB  . LYS A 1 104 ? 7.02500   -7.90700  77.50600 1.000 11.13235 ? 107 LYS A CB  1 
ATOM   912  C  CG  . LYS A 1 104 ? 6.25600   -9.02000  78.21700 1.000 12.41934 ? 107 LYS A CG  1 
ATOM   913  C  CD  . LYS A 1 104 ? 6.98400   -9.59600  79.40600 1.000 14.76699 ? 107 LYS A CD  1 
ATOM   914  C  CE  . LYS A 1 104 ? 6.18700   -10.65100 80.10400 1.000 15.76711 ? 107 LYS A CE  1 
ATOM   915  N  NZ  . LYS A 1 104 ? 6.18200   -11.97700 79.37900 1.000 16.18559 ? 107 LYS A NZ  1 
ATOM   916  N  N   . THR A 1 105 ? 5.97100   -4.92600  76.25300 1.000 8.41886  ? 108 THR A N   1 
ATOM   917  C  CA  . THR A 1 105 ? 6.27900   -3.60300  75.74000 1.000 8.87418  ? 108 THR A CA  1 
ATOM   918  C  C   . THR A 1 105 ? 6.55800   -2.66100  76.90300 1.000 8.88734  ? 108 THR A C   1 
ATOM   919  O  O   . THR A 1 105 ? 5.91400   -2.73400  77.95600 1.000 9.59269  ? 108 THR A O   1 
ATOM   920  C  CB  . THR A 1 105 ? 5.14000   -3.06100  74.84900 1.000 9.27949  ? 108 THR A CB  1 
ATOM   921  O  OG1 . THR A 1 105 ? 3.94200   -2.87900  75.61900 1.000 9.01104  ? 108 THR A OG1 1 
ATOM   922  C  CG2 . THR A 1 105 ? 4.84700   -3.97400  73.69600 1.000 9.45846  ? 108 THR A CG2 1 
ATOM   923  N  N   . ARG A 1 106 ? 7.55900   -1.80800  76.73100 1.000 9.37951  ? 109 ARG A N   1 
ATOM   924  C  CA  A ARG A 1 106 ? 7.85700   -0.72500  77.66700 0.650 9.76113  ? 109 ARG A CA  1 
ATOM   925  C  CA  B ARG A 1 106 ? 7.84000   -0.73000  77.66200 0.350 8.41996  ? 109 ARG A CA  1 
ATOM   926  C  C   . ARG A 1 106 ? 7.93600   0.54500   76.84400 1.000 9.15053  ? 109 ARG A C   1 
ATOM   927  O  O   . ARG A 1 106 ? 8.73200   0.62200   75.90100 1.000 9.24002  ? 109 ARG A O   1 
ATOM   928  C  CB  A ARG A 1 106 ? 9.19900   -0.95300  78.39100 0.650 11.38501 ? 109 ARG A CB  1 
ATOM   929  C  CB  B ARG A 1 106 ? 9.14500   -0.98700  78.41500 0.350 10.97996 ? 109 ARG A CB  1 
ATOM   930  C  CG  A ARG A 1 106 ? 9.22700   -2.25600  79.11800 0.650 13.16680 ? 109 ARG A CG  1 
ATOM   931  C  CG  B ARG A 1 106 ? 9.44600   0.08400   79.39900 0.350 11.99996 ? 109 ARG A CG  1 
ATOM   932  C  CD  A ARG A 1 106 ? 10.41900  -2.39200  80.04900 0.650 16.55405 ? 109 ARG A CD  1 
ATOM   933  C  CD  B ARG A 1 106 ? 10.63100  -0.32400  80.25300 0.350 19.34996 ? 109 ARG A CD  1 
ATOM   934  N  NE  A ARG A 1 106 ? 10.28600  -1.48700  81.19000 0.650 21.39937 ? 109 ARG A NE  1 
ATOM   935  N  NE  B ARG A 1 106 ? 11.03500  0.69100   81.22200 0.350 29.81996 ? 109 ARG A NE  1 
ATOM   936  C  CZ  A ARG A 1 106 ? 11.09300  -0.47400  81.47000 0.650 24.87084 ? 109 ARG A CZ  1 
ATOM   937  C  CZ  B ARG A 1 106 ? 10.80900  0.61000   82.52600 0.350 30.34996 ? 109 ARG A CZ  1 
ATOM   938  N  NH1 A ARG A 1 106 ? 12.06500  -0.11000  80.64100 0.650 25.76042 ? 109 ARG A NH1 1 
ATOM   939  N  NH1 B ARG A 1 106 ? 10.13100  -0.39800  83.04900 0.350 30.67996 ? 109 ARG A NH1 1 
ATOM   940  N  NH2 A ARG A 1 106 ? 10.93600  0.17800   82.62300 0.650 26.21310 ? 109 ARG A NH2 1 
ATOM   941  N  NH2 B ARG A 1 106 ? 11.28800  1.55600   83.32800 0.350 30.28996 ? 109 ARG A NH2 1 
ATOM   942  N  N   . ALA A 1 107 ? 7.13400   1.53200   77.20700 1.000 9.36371  ? 110 ALA A N   1 
ATOM   943  C  CA  . ALA A 1 107 ? 7.04000   2.76400   76.44300 1.000 10.53754 ? 110 ALA A CA  1 
ATOM   944  C  C   . ALA A 1 107 ? 7.11400   3.94400   77.37700 1.000 10.00590 ? 110 ALA A C   1 
ATOM   945  O  O   . ALA A 1 107 ? 6.65300   3.89600   78.52300 1.000 10.65071 ? 110 ALA A O   1 
ATOM   946  C  CB  . ALA A 1 107 ? 5.72200   2.81600   75.67000 1.000 10.22698 ? 110 ALA A CB  1 
ATOM   947  N  N   . GLU A 1 108 ? 7.69100   5.02400   76.85800 1.000 9.80850  ? 111 GLU A N   1 
ATOM   948  C  CA  . GLU A 1 108 ? 7.62600   6.29600   77.53100 1.000 10.27172 ? 111 GLU A CA  1 
ATOM   949  C  C   . GLU A 1 108 ? 6.84300   7.26800   76.65600 1.000 10.12960 ? 111 GLU A C   1 
ATOM   950  O  O   . GLU A 1 108 ? 7.17200   7.42200   75.46600 1.000 10.65597 ? 111 GLU A O   1 
ATOM   951  C  CB  . GLU A 1 108 ? 9.04200   6.82200   77.75800 1.000 13.67739 ? 111 GLU A CB  1 
ATOM   952  C  CG  . GLU A 1 108 ? 9.16300   8.11000   78.48100 1.000 17.61734 ? 111 GLU A CG  1 
ATOM   953  C  CD  . GLU A 1 108 ? 10.61100  8.56400   78.54000 1.000 21.77836 ? 111 GLU A CD  1 
ATOM   954  O  OE1 . GLU A 1 108 ? 11.20000  8.82400   77.48800 1.000 23.03641 ? 111 GLU A OE1 1 
ATOM   955  O  OE2 . GLU A 1 108 ? 11.15300  8.68200   79.63700 1.000 24.70240 ? 111 GLU A OE2 1 
ATOM   956  N  N   . VAL A 1 109 ? 5.80500   7.88000   77.22800 1.000 9.43214  ? 112 VAL A N   1 
ATOM   957  C  CA  . VAL A 1 109 ? 4.93500   8.79200   76.48200 1.000 9.64006  ? 112 VAL A CA  1 
ATOM   958  C  C   . VAL A 1 109 ? 5.09100   10.14800  77.14500 1.000 9.91904  ? 112 VAL A C   1 
ATOM   959  O  O   . VAL A 1 109 ? 4.76600   10.31700  78.32900 1.000 10.58491 ? 112 VAL A O   1 
ATOM   960  C  CB  . VAL A 1 109 ? 3.46500   8.35600   76.53200 1.000 10.24540 ? 112 VAL A CB  1 
ATOM   961  C  CG1 . VAL A 1 109 ? 2.60500   9.24600   75.67400 1.000 10.55333 ? 112 VAL A CG1 1 
ATOM   962  C  CG2 . VAL A 1 109 ? 3.30900   6.89700   76.07800 1.000 11.10077 ? 112 VAL A CG2 1 
ATOM   963  N  N   . LYS A 1 110 ? 5.61600   11.12000  76.40600 1.000 9.69797  ? 113 LYS A N   1 
ATOM   964  C  CA  . LYS A 1 110 ? 5.88000   12.42300  77.01100 1.000 10.35857 ? 113 LYS A CA  1 
ATOM   965  C  C   . LYS A 1 110 ? 6.04700   13.43900  75.90600 1.000 10.16118 ? 113 LYS A C   1 
ATOM   966  O  O   . LYS A 1 110 ? 6.20600   13.07100  74.74500 1.000 10.75862 ? 113 LYS A O   1 
ATOM   967  C  CB  . LYS A 1 110 ? 7.14800   12.38200  77.87900 1.000 11.41922 ? 113 LYS A CB  1 
ATOM   968  C  CG  . LYS A 1 110 ? 8.42800   12.21600  77.03900 1.000 13.22207 ? 113 LYS A CG  1 
ATOM   969  C  CD  . LYS A 1 110 ? 9.66500   12.27400  77.90600 1.000 18.63325 ? 113 LYS A CD  1 
ATOM   970  C  CE  . LYS A 1 110 ? 10.95800  12.03100  77.10000 1.000 26.40523 ? 113 LYS A CE  1 
ATOM   971  N  NZ  . LYS A 1 110 ? 12.17500  12.28300  77.95700 1.000 36.48996 ? 113 LYS A NZ  1 
ATOM   972  N  N   . PHE A 1 111 ? 6.04900   14.74200  76.26900 1.000 10.79810 ? 114 PHE A N   1 
ATOM   973  C  CA  . PHE A 1 111 ? 6.35900   15.74000  75.24000 1.000 11.35080 ? 114 PHE A CA  1 
ATOM   974  C  C   . PHE A 1 111 ? 7.86300   15.87500  75.07900 1.000 11.12445 ? 114 PHE A C   1 
ATOM   975  O  O   . PHE A 1 111 ? 8.61200   15.89300  76.06400 1.000 12.14036 ? 114 PHE A O   1 
ATOM   976  C  CB  . PHE A 1 111 ? 5.77900   17.11500  75.59800 1.000 11.55608 ? 114 PHE A CB  1 
ATOM   977  C  CG  . PHE A 1 111 ? 4.34300   17.23000  75.23700 1.000 11.60872 ? 114 PHE A CG  1 
ATOM   978  C  CD1 . PHE A 1 111 ? 3.34300   16.77200  76.10100 1.000 12.32723 ? 114 PHE A CD1 1 
ATOM   979  C  CD2 . PHE A 1 111 ? 3.97600   17.74900  74.01700 1.000 12.63253 ? 114 PHE A CD2 1 
ATOM   980  C  CE1 . PHE A 1 111 ? 1.99700   16.88700  75.75400 1.000 12.09825 ? 114 PHE A CE1 1 
ATOM   981  C  CE2 . PHE A 1 111 ? 2.64600   17.88900  73.68200 1.000 12.37723 ? 114 PHE A CE2 1 
ATOM   982  C  CZ  . PHE A 1 111 ? 1.64400   17.43500  74.54100 1.000 12.17984 ? 114 PHE A CZ  1 
ATOM   983  N  N   . GLU A 1 112 ? 8.29600   16.00400  73.81900 1.000 10.83231 ? 115 GLU A N   1 
ATOM   984  C  CA  . GLU A 1 112 ? 9.64100   16.47900  73.48400 1.000 12.22458 ? 115 GLU A CA  1 
ATOM   985  C  C   . GLU A 1 112 ? 9.39100   17.79000  72.75100 1.000 13.34840 ? 115 GLU A C   1 
ATOM   986  O  O   . GLU A 1 112 ? 8.94500   17.79600  71.60000 1.000 14.16955 ? 115 GLU A O   1 
ATOM   987  C  CB  . GLU A 1 112 ? 10.39300  15.50000  72.57900 1.000 13.15891 ? 115 GLU A CB  1 
ATOM   988  C  CG  . GLU A 1 112 ? 10.76900  14.23100  73.25600 1.000 14.67488 ? 115 GLU A CG  1 
ATOM   989  C  CD  . GLU A 1 112 ? 11.95700  14.30500  74.18100 1.000 16.85672 ? 115 GLU A CD  1 
ATOM   990  O  OE1 . GLU A 1 112 ? 12.35900  15.43900  74.52800 1.000 17.10148 ? 115 GLU A OE1 1 
ATOM   991  O  OE2 . GLU A 1 112 ? 12.46900  13.22400  74.54600 1.000 18.87012 ? 115 GLU A OE2 1 
ATOM   992  N  N   . GLY A 1 113 ? 9.62800   18.92300  73.42500 1.000 13.00099 ? 116 GLY A N   1 
ATOM   993  C  CA  . GLY A 1 113 ? 9.18700   20.20400  72.85700 1.000 14.62224 ? 116 GLY A CA  1 
ATOM   994  C  C   . GLY A 1 113 ? 7.68500   20.19700  72.72900 1.000 14.92491 ? 116 GLY A C   1 
ATOM   995  O  O   . GLY A 1 113 ? 6.97200   19.83500  73.66700 1.000 17.65681 ? 116 GLY A O   1 
ATOM   996  N  N   . ASP A 1 114 ? 7.18700   20.53900  71.53600 1.000 16.06189 ? 117 ASP A N   1 
ATOM   997  C  CA  . ASP A 1 114 ? 5.74800   20.59100  71.31000 1.000 16.97779 ? 117 ASP A CA  1 
ATOM   998  C  C   . ASP A 1 114 ? 5.16300   19.28500  70.78500 1.000 15.48550 ? 117 ASP A C   1 
ATOM   999  O  O   . ASP A 1 114 ? 3.96500   19.25000  70.49400 1.000 15.59604 ? 117 ASP A O   1 
ATOM   1000 C  CB  . ASP A 1 114 ? 5.40300   21.68300  70.30200 1.000 23.33118 ? 117 ASP A CB  1 
ATOM   1001 C  CG  . ASP A 1 114 ? 5.84900   21.32800  68.90200 1.000 31.55848 ? 117 ASP A CG  1 
ATOM   1002 O  OD1 . ASP A 1 114 ? 6.72500   20.43200  68.74600 1.000 29.58193 ? 117 ASP A OD1 1 
ATOM   1003 O  OD2 . ASP A 1 114 ? 5.33100   21.94800  67.94100 1.000 42.29996 ? 117 ASP A OD2 1 
ATOM   1004 N  N   . THR A 1 115 ? 5.96900   18.22100  70.68700 1.000 14.32484 ? 118 THR A N   1 
ATOM   1005 C  CA  . THR A 1 115 ? 5.53100   16.98200  70.06600 1.000 13.45105 ? 118 THR A CA  1 
ATOM   1006 C  C   . THR A 1 115 ? 5.31100   15.90900  71.10700 1.000 11.46923 ? 118 THR A C   1 
ATOM   1007 O  O   . THR A 1 115 ? 6.15000   15.72700  72.00900 1.000 11.24552 ? 118 THR A O   1 
ATOM   1008 C  CB  . THR A 1 115 ? 6.56800   16.56000  69.03000 1.000 14.50907 ? 118 THR A CB  1 
ATOM   1009 O  OG1 . THR A 1 115 ? 6.67300   17.62600  68.06700 1.000 17.13044 ? 118 THR A OG1 1 
ATOM   1010 C  CG2 . THR A 1 115 ? 6.20100   15.25000  68.33100 1.000 14.81437 ? 118 THR A CG2 1 
ATOM   1011 N  N   . LEU A 1 116 ? 4.17500   15.22000  71.00100 1.000 10.25330 ? 119 LEU A N   1 
ATOM   1012 C  CA  . LEU A 1 116 ? 3.89000   14.11100  71.90700 1.000 9.95326  ? 119 LEU A CA  1 
ATOM   1013 C  C   . LEU A 1 116 ? 4.56700   12.86300  71.33900 1.000 9.69270  ? 119 LEU A C   1 
ATOM   1014 O  O   . LEU A 1 116 ? 4.30000   12.47500  70.20500 1.000 10.10065 ? 119 LEU A O   1 
ATOM   1015 C  CB  . LEU A 1 116 ? 2.36200   13.97300  72.01400 1.000 10.73230 ? 119 LEU A CB  1 
ATOM   1016 C  CG  . LEU A 1 116 ? 1.86800   12.96300  73.07300 1.000 10.78231 ? 119 LEU A CG  1 
ATOM   1017 C  CD1 . LEU A 1 116 ? 2.05300   11.48200  72.65400 1.000 10.34804 ? 119 LEU A CD1 1 
ATOM   1018 C  CD2 . LEU A 1 116 ? 2.44500   13.22100  74.46000 1.000 11.61135 ? 119 LEU A CD2 1 
ATOM   1019 N  N   . VAL A 1 117 ? 5.47200   12.27800  72.11500 1.000 9.95589  ? 120 VAL A N   1 
ATOM   1020 C  CA  . VAL A 1 117 ? 6.29600   11.16700  71.64000 1.000 10.20592 ? 120 VAL A CA  1 
ATOM   1021 C  C   . VAL A 1 117 ? 5.88700   9.91000   72.38400 1.000 9.56374  ? 120 VAL A C   1 
ATOM   1022 O  O   . VAL A 1 117 ? 5.69900   9.91800   73.60500 1.000 10.61913 ? 120 VAL A O   1 
ATOM   1023 C  CB  . VAL A 1 117 ? 7.79800   11.49200  71.84400 1.000 11.76663 ? 120 VAL A CB  1 
ATOM   1024 C  CG1 . VAL A 1 117 ? 8.70200   10.31500  71.58000 1.000 14.30641 ? 120 VAL A CG1 1 
ATOM   1025 C  CG2 . VAL A 1 117 ? 8.19000   12.74300  71.03300 1.000 12.05614 ? 120 VAL A CG2 1 
ATOM   1026 N  N   . ASN A 1 118 ? 5.89300   8.79500   71.65800 1.000 10.00853 ? 121 ASN A N   1 
ATOM   1027 C  CA  . ASN A 1 118 ? 5.71200   7.47000   72.22900 1.000 9.58743  ? 121 ASN A CA  1 
ATOM   1028 C  C   . ASN A 1 118 ? 6.91700   6.63000   71.79700 1.000 9.70586  ? 121 ASN A C   1 
ATOM   1029 O  O   . ASN A 1 118 ? 6.99100   6.22200   70.63400 1.000 10.40331 ? 121 ASN A O   1 
ATOM   1030 C  CB  . ASN A 1 118 ? 4.40400   6.87500   71.73800 1.000 9.87430  ? 121 ASN A CB  1 
ATOM   1031 C  CG  . ASN A 1 118 ? 4.12800   5.51200   72.27600 1.000 9.16632  ? 121 ASN A CG  1 
ATOM   1032 O  OD1 . ASN A 1 118 ? 4.70100   5.10300   73.29800 1.000 9.65059  ? 121 ASN A OD1 1 
ATOM   1033 N  ND2 . ASN A 1 118 ? 3.18600   4.78700   71.61700 1.000 9.73218  ? 121 ASN A ND2 1 
ATOM   1034 N  N   . ARG A 1 119 ? 7.86000   6.40400   72.71400 1.000 9.23738  ? 122 ARG A N   1 
ATOM   1035 C  CA  A ARG A 1 119 ? 9.09600   5.64800   72.46800 0.580 9.30844  ? 122 ARG A CA  1 
ATOM   1036 C  CA  B ARG A 1 119 ? 9.06400   5.64100   72.43700 0.420 10.93996 ? 122 ARG A CA  1 
ATOM   1037 C  C   . ARG A 1 119 ? 8.89500   4.27400   73.08400 1.000 9.60848  ? 122 ARG A C   1 
ATOM   1038 O  O   . ARG A 1 119 ? 8.64400   4.17900   74.28200 1.000 11.15603 ? 122 ARG A O   1 
ATOM   1039 C  CB  A ARG A 1 119 ? 10.26800  6.26900   73.22000 0.580 10.59018 ? 122 ARG A CB  1 
ATOM   1040 C  CB  B ARG A 1 119 ? 10.24100  6.39400   73.03100 0.420 14.62996 ? 122 ARG A CB  1 
ATOM   1041 C  CG  A ARG A 1 119 ? 11.00400  7.46800   72.60600 0.580 10.76388 ? 122 ARG A CG  1 
ATOM   1042 C  CG  B ARG A 1 119 ? 11.56800  5.86000   72.64200 0.420 15.53996 ? 122 ARG A CG  1 
ATOM   1043 C  CD  A ARG A 1 119 ? 12.21500  7.79900   73.43900 0.580 11.40080 ? 122 ARG A CD  1 
ATOM   1044 C  CD  B ARG A 1 119 ? 12.66300  6.80200   73.15000 0.420 16.08996 ? 122 ARG A CD  1 
ATOM   1045 N  NE  A ARG A 1 119 ? 13.00300  8.91200   72.95400 0.580 12.28775 ? 122 ARG A NE  1 
ATOM   1046 N  NE  B ARG A 1 119 ? 12.63000  6.88400   74.60100 0.420 21.46996 ? 122 ARG A NE  1 
ATOM   1047 C  CZ  A ARG A 1 119 ? 12.84100  10.16900  73.31200 0.580 13.01678 ? 122 ARG A CZ  1 
ATOM   1048 C  CZ  B ARG A 1 119 ? 13.35100  6.11300   75.40500 0.420 28.08996 ? 122 ARG A CZ  1 
ATOM   1049 N  NH1 A ARG A 1 119 ? 11.79500  10.56000  74.03300 0.580 12.99310 ? 122 ARG A NH1 1 
ATOM   1050 N  NH1 B ARG A 1 119 ? 14.15700  5.18100   74.92600 0.420 36.97996 ? 122 ARG A NH1 1 
ATOM   1051 N  NH2 A ARG A 1 119 ? 13.74100  11.06200  72.92500 0.580 14.17745 ? 122 ARG A NH2 1 
ATOM   1052 N  NH2 B ARG A 1 119 ? 13.25600  6.27900   76.72100 0.420 27.03996 ? 122 ARG A NH2 1 
ATOM   1053 N  N   . ILE A 1 120 ? 9.04400   3.21600   72.28500 1.000 10.00327 ? 123 ILE A N   1 
ATOM   1054 C  CA  . ILE A 1 120 ? 8.68400   1.86700   72.72200 1.000 9.46109  ? 123 ILE A CA  1 
ATOM   1055 C  C   . ILE A 1 120 ? 9.79700   0.87100   72.45400 1.000 9.35582  ? 123 ILE A C   1 
ATOM   1056 O  O   . ILE A 1 120 ? 10.39000  0.86500   71.35500 1.000 9.82693  ? 123 ILE A O   1 
ATOM   1057 C  CB  . ILE A 1 120 ? 7.44400   1.34200   71.94400 1.000 10.70598 ? 123 ILE A CB  1 
ATOM   1058 C  CG1 . ILE A 1 120 ? 6.29500   2.33900   71.93700 1.000 11.15603 ? 123 ILE A CG1 1 
ATOM   1059 C  CG2 . ILE A 1 120 ? 7.00300   0.00600   72.53400 1.000 12.56147 ? 123 ILE A CG2 1 
ATOM   1060 C  CD1 . ILE A 1 120 ? 5.74200   2.53500   70.58100 1.000 12.07193 ? 123 ILE A CD1 1 
ATOM   1061 N  N   . GLU A 1 121 ? 10.02600  -0.03100  73.41800 1.000 9.57163  ? 124 GLU A N   1 
ATOM   1062 C  CA  A GLU A 1 121 ? 10.76200  -1.27900  73.19900 0.600 13.51684 ? 124 GLU A CA  1 
ATOM   1063 C  CA  B GLU A 1 121 ? 10.75400  -1.28000  73.17600 0.400 7.92996  ? 124 GLU A CA  1 
ATOM   1064 C  C   . GLU A 1 121 ? 9.79900   -2.45700  73.30100 1.000 9.30581  ? 124 GLU A C   1 
ATOM   1065 O  O   . GLU A 1 121 ? 9.00100   -2.52600  74.24900 1.000 10.52964 ? 124 GLU A O   1 
ATOM   1066 C  CB  A GLU A 1 121 ? 11.84000  -1.40600  74.27500 0.600 24.51553 ? 124 GLU A CB  1 
ATOM   1067 C  CB  B GLU A 1 121 ? 11.89200  -1.43700  74.17600 0.400 9.11996  ? 124 GLU A CB  1 
ATOM   1068 C  CG  A GLU A 1 121 ? 12.55200  -2.72600  74.28600 0.600 38.91199 ? 124 GLU A CG  1 
ATOM   1069 C  CG  B GLU A 1 121 ? 12.85900  -0.29200  74.24000 0.400 23.02996 ? 124 GLU A CG  1 
ATOM   1070 C  CD  A GLU A 1 121 ? 13.23100  -2.97400  75.61300 0.600 56.00996 ? 124 GLU A CD  1 
ATOM   1071 C  CD  B GLU A 1 121 ? 14.04400  -0.62600  75.12400 0.400 56.07996 ? 124 GLU A CD  1 
ATOM   1072 O  OE1 A GLU A 1 121 ? 12.52600  -3.12000  76.64100 0.600 36.24996 ? 124 GLU A OE1 1 
ATOM   1073 O  OE1 B GLU A 1 121 ? 14.30600  -1.83600  75.31500 0.400 36.05996 ? 124 GLU A OE1 1 
ATOM   1074 O  OE2 A GLU A 1 121 ? 14.47400  -3.00000  75.62800 0.600 48.78996 ? 124 GLU A OE2 1 
ATOM   1075 O  OE2 B GLU A 1 121 ? 14.69700  0.30800   75.63600 0.400 49.14996 ? 124 GLU A OE2 1 
ATOM   1076 N  N   . LEU A 1 122 ? 9.85100   -3.35700  72.33400 1.000 8.75048  ? 125 LEU A N   1 
ATOM   1077 C  CA  . LEU A 1 122 ? 8.94700   -4.51200  72.34300 1.000 9.47689  ? 125 LEU A CA  1 
ATOM   1078 C  C   . LEU A 1 122 ? 9.78700   -5.78100  72.22700 1.000 8.71890  ? 125 LEU A C   1 
ATOM   1079 O  O   . LEU A 1 122 ? 10.63100  -5.90500  71.30700 1.000 9.90062  ? 125 LEU A O   1 
ATOM   1080 C  CB  . LEU A 1 122 ? 7.97900   -4.41200  71.17300 1.000 10.02695 ? 125 LEU A CB  1 
ATOM   1081 C  CG  . LEU A 1 122 ? 6.97300   -5.54600  70.95800 1.000 9.82430  ? 125 LEU A CG  1 
ATOM   1082 C  CD1 . LEU A 1 122 ? 5.75500   -5.02300  70.20100 1.000 10.37436 ? 125 LEU A CD1 1 
ATOM   1083 C  CD2 . LEU A 1 122 ? 7.57200   -6.75300  70.15800 1.000 10.00063 ? 125 LEU A CD2 1 
ATOM   1084 N  N   . LYS A 1 123 ? 9.49500   -6.76100  73.08100 1.000 9.05315  ? 126 LYS A N   1 
ATOM   1085 C  CA  . LYS A 1 123 ? 10.14500  -8.06600  73.03200 1.000 9.40056  ? 126 LYS A CA  1 
ATOM   1086 C  C   . LYS A 1 123 ? 9.06400   -9.13100  72.90700 1.000 9.04526  ? 126 LYS A C   1 
ATOM   1087 O  O   . LYS A 1 123 ? 8.11000   -9.15400  73.70300 1.000 9.93220  ? 126 LYS A O   1 
ATOM   1088 C  CB  . LYS A 1 123 ? 10.92400  -8.31600  74.32900 1.000 11.40606 ? 126 LYS A CB  1 
ATOM   1089 C  CG  . LYS A 1 123 ? 12.08000  -7.36100  74.53700 1.000 16.21717 ? 126 LYS A CG  1 
ATOM   1090 C  CD  . LYS A 1 123 ? 12.64900  -7.52500  75.94700 1.000 23.45225 ? 126 LYS A CD  1 
ATOM   1091 C  CE  . LYS A 1 123 ? 13.78700  -6.53300  76.20700 1.000 34.22996 ? 126 LYS A CE  1 
ATOM   1092 N  NZ  . LYS A 1 123 ? 14.08200  -6.45400  77.67100 1.000 42.21996 ? 126 LYS A NZ  1 
ATOM   1093 N  N   . GLY A 1 124 ? 9.21000   -10.01200 71.91800 1.000 8.90840  ? 127 GLY A N   1 
ATOM   1094 C  CA  . GLY A 1 124 ? 8.26400   -11.10200 71.74700 1.000 9.03210  ? 127 GLY A CA  1 
ATOM   1095 C  C   . GLY A 1 124 ? 8.97000   -12.44800 71.89100 1.000 8.94524  ? 127 GLY A C   1 
ATOM   1096 O  O   . GLY A 1 124 ? 10.05500  -12.66000 71.31900 1.000 10.39015 ? 127 GLY A O   1 
ATOM   1097 N  N   A ILE A 1 125 ? 8.39700   -13.33800 72.73200 0.730 8.97419  ? 128 ILE A N   1 
ATOM   1098 N  N   B ILE A 1 125 ? 8.39300   -13.33500 72.70400 0.270 8.89996  ? 128 ILE A N   1 
ATOM   1099 C  CA  A ILE A 1 125 ? 9.01700   -14.62000 73.05000 0.730 10.03222 ? 128 ILE A CA  1 
ATOM   1100 C  CA  B ILE A 1 125 ? 8.99700   -14.63100 72.95800 0.270 8.98996  ? 128 ILE A CA  1 
ATOM   1101 C  C   A ILE A 1 125 ? 7.97100   -15.71300 72.87600 0.730 9.97168  ? 128 ILE A C   1 
ATOM   1102 C  C   B ILE A 1 125 ? 7.95700   -15.72300 72.82500 0.270 8.35996  ? 128 ILE A C   1 
ATOM   1103 O  O   A ILE A 1 125 ? 6.75800   -15.46500 72.97900 0.730 10.24277 ? 128 ILE A O   1 
ATOM   1104 O  O   B ILE A 1 125 ? 6.74800   -15.48500 72.91200 0.270 11.14996 ? 128 ILE A O   1 
ATOM   1105 C  CB  A ILE A 1 125 ? 9.59000   -14.58400 74.47800 0.730 12.03246 ? 128 ILE A CB  1 
ATOM   1106 C  CB  B ILE A 1 125 ? 9.68500   -14.70300 74.32300 0.270 11.06996 ? 128 ILE A CB  1 
ATOM   1107 C  CG1 A ILE A 1 125 ? 10.63900  -15.70800 74.66800 0.730 12.39039 ? 128 ILE A CG1 1 
ATOM   1108 C  CG1 B ILE A 1 125 ? 8.73900   -14.28400 75.43600 0.270 10.15996 ? 128 ILE A CG1 1 
ATOM   1109 C  CG2 A ILE A 1 125 ? 8.43800   -14.62500 75.50800 0.730 13.47737 ? 128 ILE A CG2 1 
ATOM   1110 C  CG2 B ILE A 1 125 ? 10.76500  -13.75700 74.34100 0.270 14.32996 ? 128 ILE A CG2 1 
ATOM   1111 C  CD1 A ILE A 1 125 ? 11.64800  -15.48000 75.79000 0.730 14.23798 ? 128 ILE A CD1 1 
ATOM   1112 C  CD1 B ILE A 1 125 ? 9.16300   -14.78600 76.79800 0.270 14.47996 ? 128 ILE A CD1 1 
ATOM   1113 N  N   . ASP A 1 126 ? 8.45900   -16.93900 72.60900 1.000 9.83482  ? 129 ASP A N   1 
ATOM   1114 C  CA  . ASP A 1 126 ? 7.63000   -18.14000 72.64600 1.000 10.76651 ? 129 ASP A CA  1 
ATOM   1115 C  C   . ASP A 1 126 ? 6.56000   -18.16000 71.55500 1.000 10.27172 ? 129 ASP A C   1 
ATOM   1116 O  O   . ASP A 1 126 ? 5.52100   -18.77600 71.74400 1.000 11.43502 ? 129 ASP A O   1 
ATOM   1117 C  CB  . ASP A 1 126 ? 7.05700   -18.44900 74.02000 1.000 12.16405 ? 129 ASP A CB  1 
ATOM   1118 C  CG  . ASP A 1 126 ? 8.15300   -18.81200 75.01100 1.000 16.79882 ? 129 ASP A CG  1 
ATOM   1119 O  OD1 . ASP A 1 126 ? 9.21500   -19.31200 74.58300 1.000 18.80432 ? 129 ASP A OD1 1 
ATOM   1120 O  OD2 . ASP A 1 126 ? 7.93600   -18.64900 76.20200 1.000 20.61243 ? 129 ASP A OD2 1 
ATOM   1121 N  N   . PHE A 1 127 ? 6.83500   -17.54800 70.38900 1.000 10.23487 ? 130 PHE A N   1 
ATOM   1122 C  CA  . PHE A 1 127 ? 5.89500   -17.63800 69.29000 1.000 10.45595 ? 130 PHE A CA  1 
ATOM   1123 C  C   . PHE A 1 127 ? 6.10500   -18.89700 68.47800 1.000 10.50069 ? 130 PHE A C   1 
ATOM   1124 O  O   . PHE A 1 127 ? 7.21700   -19.43000 68.36500 1.000 11.30868 ? 130 PHE A O   1 
ATOM   1125 C  CB  . PHE A 1 127 ? 5.99900   -16.42600 68.35900 1.000 10.65071 ? 130 PHE A CB  1 
ATOM   1126 C  CG  . PHE A 1 127 ? 5.36100   -15.21000 68.94100 1.000 9.96642  ? 130 PHE A CG  1 
ATOM   1127 C  CD1 . PHE A 1 127 ? 6.08500   -14.37100 69.83400 1.000 9.52689  ? 130 PHE A CD1 1 
ATOM   1128 C  CD2 . PHE A 1 127 ? 4.02700   -14.94100 68.65400 1.000 10.21645 ? 130 PHE A CD2 1 
ATOM   1129 C  CE1 . PHE A 1 127 ? 5.44500   -13.28200 70.42800 1.000 9.82956  ? 130 PHE A CE1 1 
ATOM   1130 C  CE2 . PHE A 1 127 ? 3.35700   -13.83100 69.23000 1.000 9.56900  ? 130 PHE A CE2 1 
ATOM   1131 C  CZ  . PHE A 1 127 ? 4.05700   -13.02800 70.13700 1.000 9.02683  ? 130 PHE A CZ  1 
ATOM   1132 N  N   . LYS A 1 128 ? 5.00400   -19.37400 67.92600 1.000 11.41659 ? 131 LYS A N   1 
ATOM   1133 C  CA  . LYS A 1 128 ? 5.03100   -20.46300 66.96900 1.000 11.87454 ? 131 LYS A CA  1 
ATOM   1134 C  C   . LYS A 1 128 ? 5.44600   -19.86600 65.62300 1.000 12.09299 ? 131 LYS A C   1 
ATOM   1135 O  O   . LYS A 1 128 ? 4.80400   -18.92800 65.12300 1.000 13.61159 ? 131 LYS A O   1 
ATOM   1136 C  CB  . LYS A 1 128 ? 3.64500   -21.09800 66.88200 1.000 13.08785 ? 131 LYS A CB  1 
ATOM   1137 C  CG  . LYS A 1 128 ? 3.28500   -21.83700 68.15500 1.000 15.60657 ? 131 LYS A CG  1 
ATOM   1138 C  CD  . LYS A 1 128 ? 1.81200   -22.25400 68.23100 1.000 18.02265 ? 131 LYS A CD  1 
ATOM   1139 C  CE  . LYS A 1 128 ? 1.52900   -22.98500 69.55000 1.000 20.68349 ? 131 LYS A CE  1 
ATOM   1140 N  NZ  . LYS A 1 128 ? 0.13000   -23.50900 69.66700 1.000 22.91271 ? 131 LYS A NZ  1 
ATOM   1141 N  N   . GLU A 1 129 ? 6.48800   -20.42000 64.99200 1.000 12.79834 ? 132 GLU A N   1 
ATOM   1142 C  CA  . GLU A 1 129 ? 6.90100   -19.87800 63.69800 1.000 13.62738 ? 132 GLU A CA  1 
ATOM   1143 C  C   . GLU A 1 129 ? 5.84300   -20.05100 62.61800 1.000 15.54603 ? 132 GLU A C   1 
ATOM   1144 O  O   . GLU A 1 129 ? 5.84400   -19.29800 61.63100 1.000 17.21466 ? 132 GLU A O   1 
ATOM   1145 C  CB  . GLU A 1 129 ? 8.23500   -20.48600 63.27100 1.000 14.39327 ? 132 GLU A CB  1 
ATOM   1146 C  CG  . GLU A 1 129 ? 9.39900   -19.95300 64.10400 1.000 13.87215 ? 132 GLU A CG  1 
ATOM   1147 C  CD  . GLU A 1 129 ? 9.83900   -18.55100 63.71900 1.000 14.55118 ? 132 GLU A CD  1 
ATOM   1148 O  OE1 . GLU A 1 129 ? 9.84000   -18.28100 62.50800 1.000 17.34099 ? 132 GLU A OE1 1 
ATOM   1149 O  OE2 . GLU A 1 129 ? 10.22000  -17.73800 64.58000 1.000 13.24576 ? 132 GLU A OE2 1 
ATOM   1150 N  N   . ASP A 1 130 ? 4.89900   -20.97300 62.80900 1.000 15.90660 ? 133 ASP A N   1 
ATOM   1151 C  CA  . ASP A 1 130 ? 3.80600   -21.21300 61.86800 1.000 17.79630 ? 133 ASP A CA  1 
ATOM   1152 C  C   . ASP A 1 130 ? 2.46000   -20.83800 62.44900 1.000 15.56183 ? 133 ASP A C   1 
ATOM   1153 O  O   . ASP A 1 130 ? 1.42300   -21.30100 61.95700 1.000 16.47773 ? 133 ASP A O   1 
ATOM   1154 C  CB  . ASP A 1 130 ? 3.81300   -22.67800 61.44000 1.000 21.30199 ? 133 ASP A CB  1 
ATOM   1155 C  CG  . ASP A 1 130 ? 3.56400   -23.63900 62.60500 1.000 25.93412 ? 133 ASP A CG  1 
ATOM   1156 O  OD1 . ASP A 1 130 ? 3.72000   -23.27800 63.81200 1.000 25.82621 ? 133 ASP A OD1 1 
ATOM   1157 O  OD2 . ASP A 1 130 ? 3.25300   -24.82800 62.29000 1.000 30.35996 ? 133 ASP A OD2 1 
ATOM   1158 N  N   . GLY A 1 131 ? 2.46300   -20.03900 63.50200 1.000 14.09849 ? 134 GLY A N   1 
ATOM   1159 C  CA  . GLY A 1 131 ? 1.24200   -19.59800 64.12900 1.000 14.01164 ? 134 GLY A CA  1 
ATOM   1160 C  C   . GLY A 1 131 ? 0.61600   -18.41600 63.40000 1.000 12.44566 ? 134 GLY A C   1 
ATOM   1161 O  O   . GLY A 1 131 ? 1.07400   -17.96700 62.34400 1.000 13.45105 ? 134 GLY A O   1 
ATOM   1162 N  N   . ASN A 1 132 ? -0.45100  -17.89400 63.99900 1.000 12.47988 ? 135 ASN A N   1 
ATOM   1163 C  CA  . ASN A 1 132 ? -1.19000  -16.82400 63.31600 1.000 12.11404 ? 135 ASN A CA  1 
ATOM   1164 C  C   . ASN A 1 132 ? -0.37000  -15.54900 63.18600 1.000 11.86665 ? 135 ASN A C   1 
ATOM   1165 O  O   . ASN A 1 132 ? -0.66600  -14.71600 62.31800 1.000 12.93783 ? 135 ASN A O   1 
ATOM   1166 C  CB  . ASN A 1 132 ? -2.48200  -16.55200 64.08500 1.000 12.55883 ? 135 ASN A CB  1 
ATOM   1167 C  CG  . ASN A 1 132 ? -3.46000  -17.68300 63.96900 1.000 13.36946 ? 135 ASN A CG  1 
ATOM   1168 O  OD1 . ASN A 1 132 ? -3.53300  -18.36200 62.92800 1.000 15.64868 ? 135 ASN A OD1 1 
ATOM   1169 N  ND2 . ASN A 1 132 ? -4.22200  -17.89400 65.02900 1.000 14.09849 ? 135 ASN A ND2 1 
ATOM   1170 N  N   . ILE A 1 133 ? 0.58100   -15.33600 64.10800 1.000 10.85600 ? 136 ILE A N   1 
ATOM   1171 C  CA  A ILE A 1 133 ? 1.35700   -14.09100 64.11700 0.750 11.17709 ? 136 ILE A CA  1 
ATOM   1172 C  CA  B ILE A 1 133 ? 1.35400   -14.10100 64.12900 0.250 9.90996  ? 136 ILE A CA  1 
ATOM   1173 C  C   . ILE A 1 133 ? 2.51400   -14.18600 63.14000 1.000 11.29816 ? 136 ILE A C   1 
ATOM   1174 O  O   . ILE A 1 133 ? 2.57000   -13.45200 62.14100 1.000 13.30103 ? 136 ILE A O   1 
ATOM   1175 C  CB  A ILE A 1 133 ? 1.80800   -13.71600 65.55300 0.750 11.10866 ? 136 ILE A CB  1 
ATOM   1176 C  CB  B ILE A 1 133 ? 1.80600   -13.79800 65.57700 0.250 10.05996 ? 136 ILE A CB  1 
ATOM   1177 C  CG1 A ILE A 1 133 ? 0.61700   -13.25500 66.38400 0.750 9.90325  ? 136 ILE A CG1 1 
ATOM   1178 C  CG1 B ILE A 1 133 ? 0.65700   -14.04500 66.57900 0.250 6.88996  ? 136 ILE A CG1 1 
ATOM   1179 C  CG2 A ILE A 1 133 ? 2.86800   -12.59700 65.49400 0.750 11.85086 ? 136 ILE A CG2 1 
ATOM   1180 C  CG2 B ILE A 1 133 ? 2.35500   -12.38900 65.69500 0.250 7.60996  ? 136 ILE A CG2 1 
ATOM   1181 C  CD1 A ILE A 1 133 ? -0.20300  -14.42400 66.95100 0.750 11.84822 ? 136 ILE A CD1 1 
ATOM   1182 C  CD1 B ILE A 1 133 ? -0.69000  -13.36400 66.25100 0.250 12.19996 ? 136 ILE A CD1 1 
ATOM   1183 N  N   . LEU A 1 134 ? 3.44700   -15.10500 63.38700 1.000 12.80623 ? 137 LEU A N   1 
ATOM   1184 C  CA  . LEU A 1 134 ? 4.60000   -15.17900 62.48700 1.000 13.63265 ? 137 LEU A CA  1 
ATOM   1185 C  C   . LEU A 1 134 ? 4.27600   -15.85300 61.16900 1.000 15.40128 ? 137 LEU A C   1 
ATOM   1186 O  O   . LEU A 1 134 ? 5.04100   -15.67100 60.19200 1.000 16.73039 ? 137 LEU A O   1 
ATOM   1187 C  CB  . LEU A 1 134 ? 5.73700   -15.92300 63.18000 1.000 13.44052 ? 137 LEU A CB  1 
ATOM   1188 C  CG  . LEU A 1 134 ? 6.31200   -15.15100 64.36800 1.000 14.07744 ? 137 LEU A CG  1 
ATOM   1189 C  CD1 . LEU A 1 134 ? 7.30600   -15.99100 65.08500 1.000 12.60621 ? 137 LEU A CD1 1 
ATOM   1190 C  CD2 . LEU A 1 134 ? 6.95000   -13.80600 63.92700 1.000 15.42497 ? 137 LEU A CD2 1 
ATOM   1191 N  N   . GLY A 1 135 ? 3.15600   -16.59600 61.08400 1.000 14.99597 ? 138 GLY A N   1 
ATOM   1192 C  CA  . GLY A 1 135 ? 2.66300   -17.07500 59.79700 1.000 16.31455 ? 138 GLY A CA  1 
ATOM   1193 C  C   . GLY A 1 135 ? 1.92100   -16.03100 58.99600 1.000 17.74367 ? 138 GLY A C   1 
ATOM   1194 O  O   . GLY A 1 135 ? 1.46500   -16.34900 57.92200 1.000 18.93592 ? 138 GLY A O   1 
ATOM   1195 N  N   . HIS A 1 136 ? 1.75000   -14.81000 59.50100 1.000 17.62260 ? 139 HIS A N   1 
ATOM   1196 C  CA  . HIS A 1 136 ? 1.00400   -13.75100 58.80800 1.000 16.38824 ? 139 HIS A CA  1 
ATOM   1197 C  C   . HIS A 1 136 ? -0.37600  -14.23700 58.36400 1.000 16.44351 ? 139 HIS A C   1 
ATOM   1198 O  O   . HIS A 1 136 ? -0.74600  -14.11000 57.18900 1.000 18.59903 ? 139 HIS A O   1 
ATOM   1199 C  CB  . HIS A 1 136 ? 1.79700   -13.18700 57.60400 1.000 16.80934 ? 139 HIS A CB  1 
ATOM   1200 C  CG  . HIS A 1 136 ? 3.07700   -12.47000 57.96700 1.000 18.32005 ? 139 HIS A CG  1 
ATOM   1201 N  ND1 . HIS A 1 136 ? 3.14100   -11.10700 58.19400 1.000 19.23858 ? 139 HIS A ND1 1 
ATOM   1202 C  CD2 . HIS A 1 136 ? 4.35300   -12.92100 58.04400 1.000 19.31228 ? 139 HIS A CD2 1 
ATOM   1203 C  CE1 . HIS A 1 136 ? 4.40000   -10.75400 58.42400 1.000 19.85445 ? 139 HIS A CE1 1 
ATOM   1204 N  NE2 . HIS A 1 136 ? 5.15500   -11.83700 58.32700 1.000 20.12553 ? 139 HIS A NE2 1 
ATOM   1205 N  N   . LYS A 1 137 ? -1.16600  -14.73300 59.32300 1.000 15.04334 ? 140 LYS A N   1 
ATOM   1206 C  CA  . LYS A 1 137 ? -2.49900  -15.25700 59.08000 1.000 13.78793 ? 140 LYS A CA  1 
ATOM   1207 C  C   . LYS A 1 137 ? -3.56100  -14.27800 59.49900 1.000 12.37987 ? 140 LYS A C   1 
ATOM   1208 O  O   . LYS A 1 137 ? -4.74800  -14.58900 59.38600 1.000 13.31156 ? 140 LYS A O   1 
ATOM   1209 C  CB  . LYS A 1 137 ? -2.72300  -16.62900 59.72400 1.000 14.71172 ? 140 LYS A CB  1 
ATOM   1210 C  CG  . LYS A 1 137 ? -1.56700  -17.52900 59.52700 1.000 17.46469 ? 140 LYS A CG  1 
ATOM   1211 C  CD  . LYS A 1 137 ? -1.91600  -18.93000 59.96800 1.000 19.04382 ? 140 LYS A CD  1 
ATOM   1212 C  CE  . LYS A 1 137 ? -0.65000  -19.78800 59.89600 1.000 21.36779 ? 140 LYS A CE  1 
ATOM   1213 N  NZ  . LYS A 1 137 ? -0.83000  -21.16900 60.40300 1.000 22.94166 ? 140 LYS A NZ  1 
ATOM   1214 N  N   A LEU A 1 138 ? -3.17100  -13.11700 60.00500 0.720 11.82454 ? 141 LEU A N   1 
ATOM   1215 N  N   B LEU A 1 138 ? -3.15800  -13.11700 60.03300 0.280 12.12996 ? 141 LEU A N   1 
ATOM   1216 C  CA  A LEU A 1 138 ? -4.15300  -12.18700 60.54200 0.720 11.74032 ? 141 LEU A CA  1 
ATOM   1217 C  CA  B LEU A 1 138 ? -4.10100  -12.10100 60.49300 0.280 7.64996  ? 141 LEU A CA  1 
ATOM   1218 C  C   A LEU A 1 138 ? -4.56000  -11.20700 59.45000 0.720 11.17183 ? 141 LEU A C   1 
ATOM   1219 C  C   B LEU A 1 138 ? -4.57600  -11.26500 59.32300 0.280 9.12996  ? 141 LEU A C   1 
ATOM   1220 O  O   A LEU A 1 138 ? -3.71000  -10.66300 58.73600 0.720 12.21406 ? 141 LEU A O   1 
ATOM   1221 O  O   B LEU A 1 138 ? -3.79100  -10.85100 58.47000 0.280 13.57996 ? 141 LEU A O   1 
ATOM   1222 C  CB  A LEU A 1 138 ? -3.59900  -11.45500 61.76300 0.720 12.71412 ? 141 LEU A CB  1 
ATOM   1223 C  CB  B LEU A 1 138 ? -3.45300  -11.13300 61.48600 0.280 18.57996 ? 141 LEU A CB  1 
ATOM   1224 C  CG  A LEU A 1 138 ? -3.23200  -12.36000 62.95100 0.720 11.72452 ? 141 LEU A CG  1 
ATOM   1225 C  CG  B LEU A 1 138 ? -3.73200  -11.35900 62.96200 0.280 10.40996 ? 141 LEU A CG  1 
ATOM   1226 C  CD1 A LEU A 1 138 ? -2.80700  -11.46800 64.10100 0.720 11.01918 ? 141 LEU A CD1 1 
ATOM   1227 C  CD1 B LEU A 1 138 ? -2.88800  -12.54700 63.35900 0.280 17.96996 ? 141 LEU A CD1 1 
ATOM   1228 C  CD2 A LEU A 1 138 ? -4.37900  -13.23500 63.42100 0.720 10.88495 ? 141 LEU A CD2 1 
ATOM   1229 C  CD2 B LEU A 1 138 ? -3.35000  -10.14400 63.80800 0.280 11.71996 ? 141 LEU A CD2 1 
ATOM   1230 N  N   . GLU A 1 139 ? -5.87100  -10.98200 59.31200 1.000 10.71914 ? 142 GLU A N   1 
ATOM   1231 C  CA  A GLU A 1 139 ? -6.38100  -10.02700 58.34500 0.710 11.46133 ? 142 GLU A CA  1 
ATOM   1232 C  CA  B GLU A 1 139 ? -6.44900  -10.01300 58.38600 0.290 12.00996 ? 142 GLU A CA  1 
ATOM   1233 C  C   . GLU A 1 139 ? -5.97100  -8.59500  58.70700 1.000 10.87179 ? 142 GLU A C   1 
ATOM   1234 O  O   . GLU A 1 139 ? -5.78200  -8.22400  59.87400 1.000 10.72440 ? 142 GLU A O   1 
ATOM   1235 C  CB  A GLU A 1 139 ? -7.88900  -10.12300 58.30500 0.710 13.15627 ? 142 GLU A CB  1 
ATOM   1236 C  CB  B GLU A 1 139 ? -7.97300  -10.03300 58.51400 0.290 13.72996 ? 142 GLU A CB  1 
ATOM   1237 C  CG  A GLU A 1 139 ? -8.32600  -11.50500 57.75300 0.710 14.41958 ? 142 GLU A CG  1 
ATOM   1238 C  CG  B GLU A 1 139 ? -8.61400  -11.34300 58.06900 0.290 17.22996 ? 142 GLU A CG  1 
ATOM   1239 C  CD  A GLU A 1 139 ? -9.82800  -11.63800 57.63700 0.710 16.02767 ? 142 GLU A CD  1 
ATOM   1240 C  CD  B GLU A 1 139 ? -8.87700  -11.37300 56.58000 0.290 14.15996 ? 142 GLU A CD  1 
ATOM   1241 O  OE1 A GLU A 1 139 ? -10.55400 -10.94600 58.38800 0.710 16.64617 ? 142 GLU A OE1 1 
ATOM   1242 O  OE1 B GLU A 1 139 ? -8.19800  -10.63300 55.83900 0.290 19.38996 ? 142 GLU A OE1 1 
ATOM   1243 O  OE2 A GLU A 1 139 ? -10.28900 -12.42600 56.78300 0.710 17.49890 ? 142 GLU A OE2 1 
ATOM   1244 O  OE2 B GLU A 1 139 ? -9.78400  -12.11800 56.13500 0.290 15.31996 ? 142 GLU A OE2 1 
ATOM   1245 N  N   . TYR A 1 140 ? -5.80800  -7.78600  57.67400 1.000 10.49017 ? 143 TYR A N   1 
ATOM   1246 C  CA  . TYR A 1 140 ? -5.47100  -6.37700  57.82700 1.000 10.21118 ? 143 TYR A CA  1 
ATOM   1247 C  C   . TYR A 1 140 ? -6.76700  -5.60400  58.10600 1.000 10.43490 ? 143 TYR A C   1 
ATOM   1248 O  O   . TYR A 1 140 ? -7.32700  -4.92600  57.23800 1.000 11.62188 ? 143 TYR A O   1 
ATOM   1249 C  CB  . TYR A 1 140 ? -4.77400  -5.86200  56.58000 1.000 11.56924 ? 143 TYR A CB  1 
ATOM   1250 C  CG  . TYR A 1 140 ? -4.15300  -4.48900  56.74800 1.000 10.50859 ? 143 TYR A CG  1 
ATOM   1251 C  CD1 . TYR A 1 140 ? -2.98100  -4.32600  57.49000 1.000 10.58228 ? 143 TYR A CD1 1 
ATOM   1252 C  CD2 . TYR A 1 140 ? -4.72500  -3.35100  56.16300 1.000 11.21920 ? 143 TYR A CD2 1 
ATOM   1253 C  CE1 . TYR A 1 140 ? -2.38600  -3.08200  57.61600 1.000 10.64282 ? 143 TYR A CE1 1 
ATOM   1254 C  CE2 . TYR A 1 140 ? -4.12800  -2.08500  56.29400 1.000 10.36383 ? 143 TYR A CE2 1 
ATOM   1255 C  CZ  . TYR A 1 140 ? -2.97300  -1.97400  57.01400 1.000 10.05327 ? 143 TYR A CZ  1 
ATOM   1256 O  OH  . TYR A 1 140 ? -2.32800  -0.75600  57.14200 1.000 11.09287 ? 143 TYR A OH  1 
ATOM   1257 N  N   . ASN A 1 141 ? -7.24900  -5.68800  59.35000 1.000 10.82968 ? 144 ASN A N   1 
ATOM   1258 C  CA  A ASN A 1 141 ? -8.48500  -5.04100  59.76500 0.610 11.62451 ? 144 ASN A CA  1 
ATOM   1259 C  CA  B ASN A 1 141 ? -8.45900  -4.99100  59.76300 0.390 10.10996 ? 144 ASN A CA  1 
ATOM   1260 C  C   . ASN A 1 141 ? -8.43400  -4.90200  61.27800 1.000 11.15340 ? 144 ASN A C   1 
ATOM   1261 O  O   . ASN A 1 141 ? -7.44000  -5.27200  61.91600 1.000 11.74032 ? 144 ASN A O   1 
ATOM   1262 C  CB  A ASN A 1 141 ? -9.74900  -5.76500  59.24400 0.610 12.84308 ? 144 ASN A CB  1 
ATOM   1263 C  CB  B ASN A 1 141 ? -9.72300  -5.69000  59.25400 0.390 10.79996 ? 144 ASN A CB  1 
ATOM   1264 C  CG  A ASN A 1 141 ? -9.78100  -7.26800  59.58300 0.610 13.86689 ? 144 ASN A CG  1 
ATOM   1265 C  CG  B ASN A 1 141 ? -10.05600 -6.95200  60.02800 0.390 18.54996 ? 144 ASN A CG  1 
ATOM   1266 O  OD1 A ASN A 1 141 ? -9.33400  -7.67500  60.65500 0.610 14.98018 ? 144 ASN A OD1 1 
ATOM   1267 O  OD1 B ASN A 1 141 ? -9.20400  -7.56000  60.69200 0.390 17.12996 ? 144 ASN A OD1 1 
ATOM   1268 N  ND2 A ASN A 1 141 ? -10.31400 -8.08200  58.66100 0.610 16.02767 ? 144 ASN A ND2 1 
ATOM   1269 N  ND2 B ASN A 1 141 ? -11.30700 -7.35800  59.93100 0.390 19.33996 ? 144 ASN A ND2 1 
ATOM   1270 N  N   . TYR A 1 142 ? -9.50500  -4.36000  61.86900 1.000 11.66925 ? 145 TYR A N   1 
ATOM   1271 C  CA  . TYR A 1 142 ? -9.44000  -4.10000  63.30200 1.000 10.91127 ? 145 TYR A CA  1 
ATOM   1272 C  C   . TYR A 1 142 ? -10.83300 -3.91100  63.88500 1.000 11.94297 ? 145 TYR A C   1 
ATOM   1273 O  O   . TYR A 1 142 ? -11.61100 -3.08800  63.40800 1.000 14.90122 ? 145 TYR A O   1 
ATOM   1274 C  CB  . TYR A 1 142 ? -8.57100  -2.86100  63.62000 1.000 11.05602 ? 145 TYR A CB  1 
ATOM   1275 C  CG  . TYR A 1 142 ? -7.79000  -3.02500  64.89500 1.000 10.84284 ? 145 TYR A CG  1 
ATOM   1276 C  CD1 . TYR A 1 142 ? -6.51000  -3.60100  64.87600 1.000 10.43490 ? 145 TYR A CD1 1 
ATOM   1277 C  CD2 . TYR A 1 142 ? -8.32400  -2.65900  66.13100 1.000 10.02432 ? 145 TYR A CD2 1 
ATOM   1278 C  CE1 . TYR A 1 142 ? -5.78600  -3.82400  66.05100 1.000 9.71902  ? 145 TYR A CE1 1 
ATOM   1279 C  CE2 . TYR A 1 142 ? -7.60700  -2.84800  67.31000 1.000 9.80850  ? 145 TYR A CE2 1 
ATOM   1280 C  CZ  . TYR A 1 142 ? -6.34900  -3.43000  67.25700 1.000 9.55058  ? 145 TYR A CZ  1 
ATOM   1281 O  OH  . TYR A 1 142 ? -5.68400  -3.58400  68.43600 1.000 10.50596 ? 145 TYR A OH  1 
ATOM   1282 N  N   . ASN A 1 143 ? -11.10800 -4.61000  64.97600 1.000 11.79295 ? 146 ASN A N   1 
ATOM   1283 C  CA  . ASN A 1 143 ? -12.38700 -4.53700  65.65900 1.000 11.44818 ? 146 ASN A CA  1 
ATOM   1284 C  C   . ASN A 1 143 ? -12.42800 -3.39600  66.67900 1.000 10.77967 ? 146 ASN A C   1 
ATOM   1285 O  O   . ASN A 1 143 ? -11.41300 -2.85200  67.08100 1.000 12.22985 ? 146 ASN A O   1 
ATOM   1286 C  CB  . ASN A 1 143 ? -12.65200 -5.87700  66.35100 1.000 12.61937 ? 146 ASN A CB  1 
ATOM   1287 C  CG  . ASN A 1 143 ? -12.95000 -6.96000  65.35800 1.000 14.26167 ? 146 ASN A CG  1 
ATOM   1288 O  OD1 . ASN A 1 143 ? -13.81500 -6.77800  64.48700 1.000 17.66997 ? 146 ASN A OD1 1 
ATOM   1289 N  ND2 . ASN A 1 143 ? -12.24300 -8.06500  65.43100 1.000 13.70897 ? 146 ASN A ND2 1 
ATOM   1290 N  N   . SER A 1 144 ? -13.64400 -3.02300  67.05900 1.000 12.33776 ? 147 SER A N   1 
ATOM   1291 C  CA  A SER A 1 144 ? -13.84400 -2.08300  68.15200 0.550 12.84308 ? 147 SER A CA  1 
ATOM   1292 C  CA  B SER A 1 144 ? -13.90900 -2.09200  68.15900 0.450 10.64996 ? 147 SER A CA  1 
ATOM   1293 C  C   . SER A 1 144 ? -13.75500 -2.80500  69.49900 1.000 11.66662 ? 147 SER A C   1 
ATOM   1294 O  O   . SER A 1 144 ? -14.19500 -3.96800  69.65800 1.000 13.30103 ? 147 SER A O   1 
ATOM   1295 C  CB  A SER A 1 144 ? -15.16000 -1.32500  67.94500 0.550 14.66172 ? 147 SER A CB  1 
ATOM   1296 C  CB  B SER A 1 144 ? -15.34600 -1.57300  68.04000 0.450 15.52996 ? 147 SER A CB  1 
ATOM   1297 O  OG  A SER A 1 144 ? -15.08900 -0.63500  66.70000 0.550 16.21980 ? 147 SER A OG  1 
ATOM   1298 O  OG  B SER A 1 144 ? -15.68600 -0.73200  69.13400 0.450 12.68996 ? 147 SER A OG  1 
ATOM   1299 N  N   . HIS A 1 145 ? -13.12300 -2.13400  70.48300 1.000 11.81664 ? 148 HIS A N   1 
ATOM   1300 C  CA  . HIS A 1 145 ? -12.88600 -2.75600  71.78900 1.000 12.01930 ? 148 HIS A CA  1 
ATOM   1301 C  C   . HIS A 1 145 ? -13.09700 -1.73700  72.89200 1.000 11.16656 ? 148 HIS A C   1 
ATOM   1302 O  O   . HIS A 1 145 ? -12.96400 -0.53800  72.67300 1.000 12.47198 ? 148 HIS A O   1 
ATOM   1303 C  CB  . HIS A 1 145 ? -11.48700 -3.30100  71.95600 1.000 11.91665 ? 148 HIS A CB  1 
ATOM   1304 C  CG  . HIS A 1 145 ? -11.11000 -4.29600  70.90900 1.000 10.78494 ? 148 HIS A CG  1 
ATOM   1305 N  ND1 . HIS A 1 145 ? -10.63200 -3.94300  69.66700 1.000 11.94560 ? 148 HIS A ND1 1 
ATOM   1306 C  CD2 . HIS A 1 145 ? -11.10800 -5.65900  70.93700 1.000 11.15867 ? 148 HIS A CD2 1 
ATOM   1307 C  CE1 . HIS A 1 145 ? -10.34900 -5.04500  68.99000 1.000 11.64820 ? 148 HIS A CE1 1 
ATOM   1308 N  NE2 . HIS A 1 145 ? -10.61900 -6.10700  69.72900 1.000 10.63492 ? 148 HIS A NE2 1 
ATOM   1309 N  N   . ASN A 1 146 ? -13.35200 -2.24000  74.10700 1.000 11.43238 ? 149 ASN A N   1 
ATOM   1310 C  CA  . ASN A 1 146 ? -13.30400 -1.43000  75.32600 1.000 12.00877 ? 149 ASN A CA  1 
ATOM   1311 C  C   . ASN A 1 146 ? -12.02800 -1.69200  76.11000 1.000 12.02982 ? 149 ASN A C   1 
ATOM   1312 O  O   . ASN A 1 146 ? -11.62200 -2.84900  76.28100 1.000 12.77991 ? 149 ASN A O   1 
ATOM   1313 C  CB  . ASN A 1 146 ? -14.45200 -1.77300  76.23400 1.000 13.25102 ? 149 ASN A CB  1 
ATOM   1314 C  CG  . ASN A 1 146 ? -15.77300 -1.32800  75.67300 1.000 14.51170 ? 149 ASN A CG  1 
ATOM   1315 O  OD1 . ASN A 1 146 ? -15.83900 -0.40000  74.86000 1.000 15.10124 ? 149 ASN A OD1 1 
ATOM   1316 N  ND2 . ASN A 1 146 ? -16.85600 -1.95400  76.14700 1.000 15.88555 ? 149 ASN A ND2 1 
ATOM   1317 N  N   . VAL A 1 147 ? -11.41300 -0.61500  76.59900 1.000 11.12182 ? 150 VAL A N   1 
ATOM   1318 C  CA  . VAL A 1 147 ? -10.21800 -0.67500  77.44500 1.000 10.81652 ? 150 VAL A CA  1 
ATOM   1319 C  C   . VAL A 1 147 ? -10.65200 -0.37400  78.87600 1.000 10.71651 ? 150 VAL A C   1 
ATOM   1320 O  O   . VAL A 1 147 ? -11.15700 0.72600   79.13800 1.000 11.47713 ? 150 VAL A O   1 
ATOM   1321 C  CB  . VAL A 1 147 ? -9.18100  0.36400   76.98000 1.000 11.15340 ? 150 VAL A CB  1 
ATOM   1322 C  CG1 . VAL A 1 147 ? -8.00500  0.46100   77.94300 1.000 11.51924 ? 150 VAL A CG1 1 
ATOM   1323 C  CG2 . VAL A 1 147 ? -8.71300  0.02300   75.58300 1.000 13.27997 ? 150 VAL A CG2 1 
ATOM   1324 N  N   . TYR A 1 148 ? -10.55600 -1.34900  79.77900 1.000 11.20604 ? 151 TYR A N   1 
ATOM   1325 C  CA  . TYR A 1 148 ? -11.07400 -1.18700  81.14100 1.000 10.84547 ? 151 TYR A CA  1 
ATOM   1326 C  C   . TYR A 1 148 ? -9.96100  -0.65400  82.03200 1.000 11.89033 ? 151 TYR A C   1 
ATOM   1327 O  O   . TYR A 1 148 ? -8.88300  -1.26600  82.10200 1.000 13.36156 ? 151 TYR A O   1 
ATOM   1328 C  CB  . TYR A 1 148 ? -11.64200 -2.50800  81.67300 1.000 11.12445 ? 151 TYR A CB  1 
ATOM   1329 C  CG  . TYR A 1 148 ? -12.79700 -2.94200  80.83900 1.000 11.85086 ? 151 TYR A CG  1 
ATOM   1330 C  CD1 . TYR A 1 148 ? -14.04600 -2.30800  80.94200 1.000 13.32998 ? 151 TYR A CD1 1 
ATOM   1331 C  CD2 . TYR A 1 148 ? -12.63100 -3.90500  79.84900 1.000 12.74570 ? 151 TYR A CD2 1 
ATOM   1332 C  CE1 . TYR A 1 148 ? -15.13600 -2.66700  80.13300 1.000 14.49065 ? 151 TYR A CE1 1 
ATOM   1333 C  CE2 . TYR A 1 148 ? -13.71300 -4.31100  79.04100 1.000 13.77740 ? 151 TYR A CE2 1 
ATOM   1334 C  CZ  . TYR A 1 148 ? -14.93800 -3.66600  79.17500 1.000 14.44590 ? 151 TYR A CZ  1 
ATOM   1335 O  OH  . TYR A 1 148 ? -15.99400 -4.04100  78.36000 1.000 15.63289 ? 151 TYR A OH  1 
ATOM   1336 N  N   . ILE A 1 149 ? -10.17700 0.52000   82.63300 1.000 11.61135 ? 152 ILE A N   1 
ATOM   1337 C  CA  . ILE A 1 149 ? -9.15400  1.22000   83.41400 1.000 11.75874 ? 152 ILE A CA  1 
ATOM   1338 C  C   . ILE A 1 149 ? -9.50100  1.18900   84.89000 1.000 11.06655 ? 152 ILE A C   1 
ATOM   1339 O  O   . ILE A 1 149 ? -10.65800 1.40800   85.27000 1.000 12.39829 ? 152 ILE A O   1 
ATOM   1340 C  CB  . ILE A 1 149 ? -9.01100  2.67600   82.94400 1.000 12.32460 ? 152 ILE A CB  1 
ATOM   1341 C  CG1 . ILE A 1 149 ? -8.51600  2.65100   81.49100 1.000 13.89584 ? 152 ILE A CG1 1 
ATOM   1342 C  CG2 . ILE A 1 149 ? -8.07000  3.44300   83.86200 1.000 12.78518 ? 152 ILE A CG2 1 
ATOM   1343 C  CD1 . ILE A 1 149 ? -8.50000  4.00800   80.89700 1.000 14.88806 ? 152 ILE A CD1 1 
ATOM   1344 N  N   . THR A 1 150 ? -8.49400  0.94500   85.73200 1.000 11.97982 ? 153 THR A N   1 
ATOM   1345 C  CA  A THR A 1 150 ? -8.62000  1.02800   87.17600 0.690 13.55106 ? 153 THR A CA  1 
ATOM   1346 C  CA  B THR A 1 150 ? -8.64300  1.06900   87.17800 0.310 13.86996 ? 153 THR A CA  1 
ATOM   1347 C  C   . THR A 1 150 ? -7.43300  1.80200   87.73900 1.000 12.57199 ? 153 THR A C   1 
ATOM   1348 O  O   . THR A 1 150 ? -6.34400  1.83300   87.14400 1.000 12.20090 ? 153 THR A O   1 
ATOM   1349 C  CB  A THR A 1 150 ? -8.64000  -0.39000  87.77500 0.690 15.80659 ? 153 THR A CB  1 
ATOM   1350 C  CB  B THR A 1 150 ? -8.82600  -0.29300  87.89100 0.310 11.58996 ? 153 THR A CB  1 
ATOM   1351 O  OG1 A THR A 1 150 ? -7.45200  -1.11400  87.39700 0.690 16.97252 ? 153 THR A OG1 1 
ATOM   1352 O  OG1 B THR A 1 150 ? -9.24400  -0.11100  89.25100 0.310 10.84996 ? 153 THR A OG1 1 
ATOM   1353 C  CG2 A THR A 1 150 ? -9.85100  -1.17000  87.26400 0.690 16.69091 ? 153 THR A CG2 1 
ATOM   1354 C  CG2 B THR A 1 150 ? -7.53400  -1.07600  87.93500 0.310 12.01996 ? 153 THR A CG2 1 
ATOM   1355 N  N   . ALA A 1 151 ? -7.61700  2.40800   88.90000 1.000 12.89045 ? 154 ALA A N   1 
ATOM   1356 C  CA  . ALA A 1 151 ? -6.50300  3.08000   89.55100 1.000 13.12996 ? 154 ALA A CA  1 
ATOM   1357 C  C   . ALA A 1 151 ? -5.56000  2.05200   90.15100 1.000 14.77226 ? 154 ALA A C   1 
ATOM   1358 O  O   . ALA A 1 151 ? -5.96600  0.97100   90.60400 1.000 16.33297 ? 154 ALA A O   1 
ATOM   1359 C  CB  . ALA A 1 151 ? -7.02300  3.95900   90.69800 1.000 13.85899 ? 154 ALA A CB  1 
ATOM   1360 N  N   . ASP A 1 152 ? -4.28600  2.41600   90.16000 1.000 15.14599 ? 155 ASP A N   1 
ATOM   1361 C  CA  . ASP A 1 152 ? -3.21900  1.69000   90.84100 1.000 19.20963 ? 155 ASP A CA  1 
ATOM   1362 C  C   . ASP A 1 152 ? -2.71200  2.64700   91.91300 1.000 21.49938 ? 155 ASP A C   1 
ATOM   1363 O  O   . ASP A 1 152 ? -1.77100  3.41700   91.70400 1.000 21.32831 ? 155 ASP A O   1 
ATOM   1364 C  CB  . ASP A 1 152 ? -2.13800  1.29800   89.86300 1.000 20.95984 ? 155 ASP A CB  1 
ATOM   1365 C  CG  . ASP A 1 152 ? -0.99200  0.54400   90.52200 1.000 23.74702 ? 155 ASP A CG  1 
ATOM   1366 O  OD1 . ASP A 1 152 ? -0.97100  0.44000   91.77200 1.000 25.69725 ? 155 ASP A OD1 1 
ATOM   1367 O  OD2 . ASP A 1 152 ? -0.11800  0.03700   89.77100 1.000 25.34195 ? 155 ASP A OD2 1 
ATOM   1368 N  N   . LYS A 1 153 ? -3.37200  2.60800   93.06700 1.000 23.32328 ? 156 LYS A N   1 
ATOM   1369 C  CA  . LYS A 1 153 ? -3.03400  3.55300   94.11900 1.000 27.95015 ? 156 LYS A CA  1 
ATOM   1370 C  C   . LYS A 1 153 ? -1.60400  3.36400   94.60600 1.000 28.37652 ? 156 LYS A C   1 
ATOM   1371 O  O   . LYS A 1 153 ? -0.91900  4.34500   94.92000 1.000 27.93173 ? 156 LYS A O   1 
ATOM   1372 C  CB  . LYS A 1 153 ? -4.03900  3.44100   95.25600 1.000 32.51649 ? 156 LYS A CB  1 
ATOM   1373 C  CG  . LYS A 1 153 ? -5.44700  3.85400   94.82100 1.000 38.80996 ? 156 LYS A CG  1 
ATOM   1374 C  CD  . LYS A 1 153 ? -6.48500  3.50600   95.88900 1.000 47.99996 ? 156 LYS A CD  1 
ATOM   1375 N  N   . GLN A 1 154 ? -1.12900  2.11400   94.66800 1.000 29.52139 ? 157 GLN A N   1 
ATOM   1376 C  CA  . GLN A 1 154 ? 0.19400   1.84400   95.23800 1.000 31.83996 ? 157 GLN A CA  1 
ATOM   1377 C  C   . GLN A 1 154 ? 1.30100   2.50000   94.42400 1.000 34.59996 ? 157 GLN A C   1 
ATOM   1378 O  O   . GLN A 1 154 ? 2.26200   3.03800   94.98500 1.000 33.60996 ? 157 GLN A O   1 
ATOM   1379 C  CB  . GLN A 1 154 ? 0.43900   0.33800   95.28800 1.000 42.00996 ? 157 GLN A CB  1 
ATOM   1380 C  CG  . GLN A 1 154 ? -0.33600  -0.38100  96.38000 1.000 71.32996 ? 157 GLN A CG  1 
ATOM   1381 C  CD  . GLN A 1 154 ? 0.10200   0.02800   97.77600 1.000 81.30996 ? 157 GLN A CD  1 
ATOM   1382 O  OE1 . GLN A 1 154 ? 1.26000   0.39500   97.99800 1.000 76.07996 ? 157 GLN A OE1 1 
ATOM   1383 N  NE2 . GLN A 1 154 ? -0.82700  -0.02900  98.72600 1.000 82.65996 ? 157 GLN A NE2 1 
ATOM   1384 N  N   . LYS A 1 155 ? 1.17800   2.47500   93.10200 1.000 29.43454 ? 158 LYS A N   1 
ATOM   1385 C  CA  A LYS A 1 155 ? 2.15700   3.06100   92.19800 0.450 27.54996 ? 158 LYS A CA  1 
ATOM   1386 C  CA  B LYS A 1 155 ? 2.15100   3.06000   92.19200 0.550 28.43179 ? 158 LYS A CA  1 
ATOM   1387 C  C   . LYS A 1 155 ? 1.74400   4.43600   91.70700 1.000 24.51553 ? 158 LYS A C   1 
ATOM   1388 O  O   . LYS A 1 155 ? 2.41200   4.99400   90.82200 1.000 24.03126 ? 158 LYS A O   1 
ATOM   1389 C  CB  A LYS A 1 155 ? 2.39300   2.13900   90.99700 0.450 28.09996 ? 158 LYS A CB  1 
ATOM   1390 C  CB  B LYS A 1 155 ? 2.33700   2.15600   90.97900 0.550 31.61901 ? 158 LYS A CB  1 
ATOM   1391 C  CG  A LYS A 1 155 ? 3.48900   1.09500   91.19500 0.450 35.22996 ? 158 LYS A CG  1 
ATOM   1392 C  CG  B LYS A 1 155 ? 3.14700   0.91600   91.24000 0.550 35.36996 ? 158 LYS A CG  1 
ATOM   1393 C  CD  A LYS A 1 155 ? 3.01800   -0.05900  92.05100 0.450 40.27996 ? 158 LYS A CD  1 
ATOM   1394 C  CD  B LYS A 1 155 ? 3.55700   0.32500   89.92000 0.550 33.54996 ? 158 LYS A CD  1 
ATOM   1395 C  CE  A LYS A 1 155 ? 4.05500   -1.16700  92.09600 0.450 31.50996 ? 158 LYS A CE  1 
ATOM   1396 C  CE  B LYS A 1 155 ? 3.39000   -1.15300  89.93500 0.550 35.44996 ? 158 LYS A CE  1 
ATOM   1397 N  NZ  A LYS A 1 155 ? 3.55900   -2.30200  92.90200 0.450 44.31996 ? 158 LYS A NZ  1 
ATOM   1398 N  NZ  B LYS A 1 155 ? 1.97800   -1.54900  90.25600 0.550 34.82466 ? 158 LYS A NZ  1 
ATOM   1399 N  N   . ASN A 1 156 ? 0.64500   4.96800   92.22300 1.000 19.12278 ? 159 ASN A N   1 
ATOM   1400 C  CA  . ASN A 1 156 ? 0.17400   6.30300   91.85800 1.000 16.65143 ? 159 ASN A CA  1 
ATOM   1401 C  C   . ASN A 1 156 ? -0.07200  6.39300   90.35200 1.000 15.12230 ? 159 ASN A C   1 
ATOM   1402 O  O   . ASN A 1 156 ? 0.23600   7.40800   89.70400 1.000 15.77501 ? 159 ASN A O   1 
ATOM   1403 C  CB  . ASN A 1 156 ? 1.12800   7.39200   92.34800 1.000 17.59628 ? 159 ASN A CB  1 
ATOM   1404 C  CG  . ASN A 1 156 ? 0.46000   8.71800   92.42600 1.000 17.44626 ? 159 ASN A CG  1 
ATOM   1405 O  OD1 . ASN A 1 156 ? -0.74400  8.82500   92.73900 1.000 17.88842 ? 159 ASN A OD1 1 
ATOM   1406 N  ND2 . ASN A 1 156 ? 1.21300   9.76800   92.10100 1.000 17.98054 ? 159 ASN A ND2 1 
ATOM   1407 N  N   . GLY A 1 157 ? -0.64500  5.34700   89.78300 1.000 14.27483 ? 160 GLY A N   1 
ATOM   1408 C  CA  . GLY A 1 157 ? -0.88200  5.29700   88.35000 1.000 13.06153 ? 160 GLY A CA  1 
ATOM   1409 C  C   . GLY A 1 157 ? -2.15100  4.54700   88.06100 1.000 11.76400 ? 160 GLY A C   1 
ATOM   1410 O  O   . GLY A 1 157 ? -3.10900  4.58500   88.84400 1.000 12.73517 ? 160 GLY A O   1 
ATOM   1411 N  N   . ILE A 1 158 ? -2.17900  3.85400   86.90700 1.000 11.67189 ? 161 ILE A N   1 
ATOM   1412 C  CA  A ILE A 1 158 ? -3.36400  3.13100   86.46200 0.480 10.07996 ? 161 ILE A CA  1 
ATOM   1413 C  CA  B ILE A 1 158 ? -3.35600  3.10200   86.52200 0.520 10.80996 ? 161 ILE A CA  1 
ATOM   1414 C  C   . ILE A 1 158 ? -2.95200  1.74100   85.98600 1.000 10.93232 ? 161 ILE A C   1 
ATOM   1415 O  O   . ILE A 1 158 ? -1.79500  1.48800   85.62100 1.000 11.41133 ? 161 ILE A O   1 
ATOM   1416 C  CB  A ILE A 1 158 ? -4.18000  3.84500   85.35000 0.480 13.58996 ? 161 ILE A CB  1 
ATOM   1417 C  CB  B ILE A 1 158 ? -4.21000  3.84300   85.49400 0.520 10.60996 ? 161 ILE A CB  1 
ATOM   1418 C  CG1 A ILE A 1 158 ? -3.35100  4.00800   84.06800 0.480 13.58996 ? 161 ILE A CG1 1 
ATOM   1419 C  CG1 B ILE A 1 158 ? -3.40200  4.13000   84.23400 0.520 13.76996 ? 161 ILE A CG1 1 
ATOM   1420 C  CG2 A ILE A 1 158 ? -4.71500  5.21200   85.80800 0.480 12.56996 ? 161 ILE A CG2 1 
ATOM   1421 C  CG2 B ILE A 1 158 ? -4.66600  5.17600   86.09000 0.520 15.71996 ? 161 ILE A CG2 1 
ATOM   1422 C  CD1 A ILE A 1 158 ? -3.65500  2.97300   82.96100 0.480 14.36996 ? 161 ILE A CD1 1 
ATOM   1423 C  CD1 B ILE A 1 158 ? -4.25800  4.55600   83.14600 0.520 12.81996 ? 161 ILE A CD1 1 
ATOM   1424 N  N   . LYS A 1 159 ? -3.92600  0.86200   85.97900 1.000 11.56924 ? 162 LYS A N   1 
ATOM   1425 C  CA  A LYS A 1 159 ? -3.81700  -0.38100  85.24900 0.340 13.15101 ? 162 LYS A CA  1 
ATOM   1426 C  CA  B LYS A 1 159 ? -3.82400  -0.39100  85.26000 0.660 12.22722 ? 162 LYS A CA  1 
ATOM   1427 C  C   . LYS A 1 159 ? -4.95300  -0.42600  84.24300 1.000 12.02719 ? 162 LYS A C   1 
ATOM   1428 O  O   . LYS A 1 159 ? -5.98500  0.24200   84.40000 1.000 13.40894 ? 162 LYS A O   1 
ATOM   1429 C  CB  A LYS A 1 159 ? -3.87900  -1.58300  86.19100 0.340 15.96714 ? 162 LYS A CB  1 
ATOM   1430 C  CB  B LYS A 1 159 ? -3.94900  -1.57900  86.21100 0.660 13.44315 ? 162 LYS A CB  1 
ATOM   1431 C  CG  A LYS A 1 159 ? -2.59000  -1.83000  86.96700 0.340 19.55178 ? 162 LYS A CG  1 
ATOM   1432 C  CG  B LYS A 1 159 ? -2.81600  -1.72800  87.21600 0.660 17.06201 ? 162 LYS A CG  1 
ATOM   1433 C  CD  A LYS A 1 159 ? -2.77700  -2.94100  88.00000 0.340 23.34996 ? 162 LYS A CD  1 
ATOM   1434 C  CD  B LYS A 1 159 ? -3.06400  -2.94800  88.12800 0.660 22.47318 ? 162 LYS A CD  1 
ATOM   1435 C  CE  A LYS A 1 159 ? -1.50000  -3.14200  88.80600 0.340 26.87996 ? 162 LYS A CE  1 
ATOM   1436 C  CE  B LYS A 1 159 ? -1.86000  -3.20300  89.04400 0.660 28.58970 ? 162 LYS A CE  1 
ATOM   1437 N  NZ  A LYS A 1 159 ? -1.74100  -3.92800  90.05000 0.340 32.96996 ? 162 LYS A NZ  1 
ATOM   1438 N  NZ  B LYS A 1 159 ? -0.65400  -3.56100  88.27400 0.660 34.14996 ? 162 LYS A NZ  1 
ATOM   1439 N  N   . ALA A 1 160 ? -4.77000  -1.26200  83.24000 1.000 12.20090 ? 163 ALA A N   1 
ATOM   1440 C  CA  . ALA A 1 160 ? -5.86400  -1.49300  82.32200 1.000 12.20353 ? 163 ALA A CA  1 
ATOM   1441 C  C   . ALA A 1 160 ? -5.84200  -2.95900  81.91400 1.000 11.63767 ? 163 ALA A C   1 
ATOM   1442 O  O   . ALA A 1 160 ? -4.79100  -3.64900  81.94200 1.000 11.94034 ? 163 ALA A O   1 
ATOM   1443 C  CB  . ALA A 1 160 ? -5.78800  -0.58300  81.06500 1.000 13.86689 ? 163 ALA A CB  1 
ATOM   1444 N  N   . ASN A 1 161 ? -7.00200  -3.40900  81.48000 1.000 11.75084 ? 164 ASN A N   1 
ATOM   1445 C  CA  . ASN A 1 161 ? -7.16100  -4.77000  81.00200 1.000 13.40894 ? 164 ASN A CA  1 
ATOM   1446 C  C   . ASN A 1 161 ? -8.14600  -4.74300  79.84800 1.000 11.70610 ? 164 ASN A C   1 
ATOM   1447 O  O   . ASN A 1 161 ? -9.14300  -4.00600  79.86200 1.000 12.72991 ? 164 ASN A O   1 
ATOM   1448 C  CB  . ASN A 1 161 ? -7.67600  -5.68900  82.11000 1.000 17.03569 ? 164 ASN A CB  1 
ATOM   1449 C  CG  . ASN A 1 161 ? -8.98700  -5.20900  82.67400 1.000 21.23356 ? 164 ASN A CG  1 
ATOM   1450 O  OD1 . ASN A 1 161 ? -9.02500  -4.23100  83.47900 1.000 23.92072 ? 164 ASN A OD1 1 
ATOM   1451 N  ND2 . ASN A 1 161 ? -10.07100 -5.87000  82.28700 1.000 21.77836 ? 164 ASN A ND2 1 
ATOM   1452 N  N   . PHE A 1 162 ? -7.85600  -5.56300  78.84500 1.000 11.44554 ? 165 PHE A N   1 
ATOM   1453 C  CA  . PHE A 1 162 ? -8.75900  -5.66200  77.70600 1.000 10.68493 ? 165 PHE A CA  1 
ATOM   1454 C  C   . PHE A 1 162 ? -8.26600  -6.82300  76.88400 1.000 10.29014 ? 165 PHE A C   1 
ATOM   1455 O  O   . PHE A 1 162 ? -7.17100  -7.33200  77.10200 1.000 10.89021 ? 165 PHE A O   1 
ATOM   1456 C  CB  . PHE A 1 162 ? -8.89300  -4.37300  76.88300 1.000 11.04023 ? 165 PHE A CB  1 
ATOM   1457 C  CG  . PHE A 1 162 ? -7.58800  -3.75000  76.44300 1.000 10.30593 ? 165 PHE A CG  1 
ATOM   1458 C  CD1 . PHE A 1 162 ? -6.81100  -2.97700  77.33400 1.000 10.58228 ? 165 PHE A CD1 1 
ATOM   1459 C  CD2 . PHE A 1 162 ? -7.18900  -3.84500  75.12000 1.000 10.73493 ? 165 PHE A CD2 1 
ATOM   1460 C  CE1 . PHE A 1 162 ? -5.67600  -2.33600  76.89200 1.000 10.93759 ? 165 PHE A CE1 1 
ATOM   1461 C  CE2 . PHE A 1 162 ? -6.04500  -3.15500  74.63300 1.000 10.15065 ? 165 PHE A CE2 1 
ATOM   1462 C  CZ  . PHE A 1 162 ? -5.28000  -2.41000  75.53000 1.000 10.68493 ? 165 PHE A CZ  1 
ATOM   1463 N  N   . LYS A 1 163 ? -9.08200  -7.25700  75.96000 1.000 10.56649 ? 166 LYS A N   1 
ATOM   1464 C  CA  . LYS A 1 163 ? -8.72300  -8.38800  75.10900 1.000 10.32436 ? 166 LYS A CA  1 
ATOM   1465 C  C   . LYS A 1 163 ? -8.95700  -7.99000  73.66600 1.000 10.31120 ? 166 LYS A C   1 
ATOM   1466 O  O   . LYS A 1 163 ? -10.10900 -7.77400  73.27000 1.000 11.56398 ? 166 LYS A O   1 
ATOM   1467 C  CB  . LYS A 1 163 ? -9.52300  -9.65900  75.48000 1.000 11.78506 ? 166 LYS A CB  1 
ATOM   1468 C  CG  . LYS A 1 163 ? -9.30700  -10.03700 76.96400 1.000 12.01140 ? 166 LYS A CG  1 
ATOM   1469 C  CD  . LYS A 1 163 ? -10.01900 -11.34000 77.34200 1.000 13.69055 ? 166 LYS A CD  1 
ATOM   1470 C  CE  . LYS A 1 163 ? -9.97300  -11.49900 78.85100 1.000 14.46433 ? 166 LYS A CE  1 
ATOM   1471 N  NZ  . LYS A 1 163 ? -10.69100 -12.75600 79.28200 1.000 16.21717 ? 166 LYS A NZ  1 
ATOM   1472 N  N   . ILE A 1 164 ? -7.89400  -7.92600  72.88500 1.000 9.78219  ? 167 ILE A N   1 
ATOM   1473 C  CA  . ILE A 1 164 ? -8.04200  -7.58500  71.47000 1.000 9.74271  ? 167 ILE A CA  1 
ATOM   1474 C  C   . ILE A 1 164 ? -8.41700  -8.84200  70.71700 1.000 9.03473  ? 167 ILE A C   1 
ATOM   1475 O  O   . ILE A 1 164 ? -7.92300  -9.96400  71.01100 1.000 9.74271  ? 167 ILE A O   1 
ATOM   1476 C  CB  . ILE A 1 164 ? -6.75800  -6.94600  70.93100 1.000 9.82693  ? 167 ILE A CB  1 
ATOM   1477 C  CG1 . ILE A 1 164 ? -6.45400  -5.57700  71.60100 1.000 9.85325  ? 167 ILE A CG1 1 
ATOM   1478 C  CG2 . ILE A 1 164 ? -6.78900  -6.80600  69.38800 1.000 10.75336 ? 167 ILE A CG2 1 
ATOM   1479 C  CD1 . ILE A 1 164 ? -7.50800  -4.50400  71.32000 1.000 9.96115  ? 167 ILE A CD1 1 
ATOM   1480 N  N   . ARG A 1 165 ? -9.27600  -8.66900  69.71700 1.000 9.04262  ? 168 ARG A N   1 
ATOM   1481 C  CA  . ARG A 1 165 ? -9.74400  -9.78000  68.88400 1.000 9.24528  ? 168 ARG A CA  1 
ATOM   1482 C  C   . ARG A 1 165 ? -9.26800  -9.52800  67.46700 1.000 9.36635  ? 168 ARG A C   1 
ATOM   1483 O  O   . ARG A 1 165 ? -9.75900  -8.58400  66.81800 1.000 10.61386 ? 168 ARG A O   1 
ATOM   1484 C  CB  . ARG A 1 165 ? -11.26600 -9.82300  68.95500 1.000 10.00063 ? 168 ARG A CB  1 
ATOM   1485 C  CG  . ARG A 1 165 ? -11.71400 -10.38500 70.29700 1.000 10.95601 ? 168 ARG A CG  1 
ATOM   1486 C  CD  . ARG A 1 165 ? -13.20000 -10.21900 70.52200 1.000 11.34816 ? 168 ARG A CD  1 
ATOM   1487 N  NE  . ARG A 1 165 ? -13.50600 -8.85800  70.97200 1.000 12.49567 ? 168 ARG A NE  1 
ATOM   1488 C  CZ  . ARG A 1 165 ? -14.07100 -7.88800  70.24800 1.000 12.36934 ? 168 ARG A CZ  1 
ATOM   1489 N  NH1 . ARG A 1 165 ? -14.44400 -8.07700  68.99500 1.000 13.19312 ? 168 ARG A NH1 1 
ATOM   1490 N  NH2 . ARG A 1 165 ? -14.32300 -6.71600  70.82300 1.000 13.11416 ? 168 ARG A NH2 1 
ATOM   1491 N  N   . HIS A 1 166 ? -8.30600  -10.33800 66.98700 1.000 8.75312  ? 169 HIS A N   1 
ATOM   1492 C  CA  . HIS A 1 166 ? -7.76500  -10.13800 65.65000 1.000 9.60848  ? 169 HIS A CA  1 
ATOM   1493 C  C   . HIS A 1 166 ? -8.37600  -11.18500 64.70500 1.000 9.60585  ? 169 HIS A C   1 
ATOM   1494 O  O   . HIS A 1 166 ? -8.17700  -12.39500 64.89300 1.000 10.17434 ? 169 HIS A O   1 
ATOM   1495 C  CB  . HIS A 1 166 ? -6.25400  -10.36700 65.65400 1.000 9.44794  ? 169 HIS A CB  1 
ATOM   1496 C  CG  . HIS A 1 166 ? -5.44300  -9.36600  66.42200 1.000 9.51636  ? 169 HIS A CG  1 
ATOM   1497 N  ND1 . HIS A 1 166 ? -5.35700  -8.03000  66.06000 1.000 8.72153  ? 169 HIS A ND1 1 
ATOM   1498 C  CD2 . HIS A 1 166 ? -4.57900  -9.51600  67.45700 1.000 9.61374  ? 169 HIS A CD2 1 
ATOM   1499 C  CE1 . HIS A 1 166 ? -4.49500  -7.40500  66.86500 1.000 8.74785  ? 169 HIS A CE1 1 
ATOM   1500 N  NE2 . HIS A 1 166 ? -4.02800  -8.28000  67.74900 1.000 9.71112  ? 169 HIS A NE2 1 
ATOM   1501 N  N   . ASN A 1 167 ? -9.06900  -10.73200 63.67200 1.000 10.03748 ? 170 ASN A N   1 
ATOM   1502 C  CA  . ASN A 1 167 ? -9.64400  -11.68900 62.72000 1.000 9.98747  ? 170 ASN A CA  1 
ATOM   1503 C  C   . ASN A 1 167 ? -8.50300  -12.42700 62.01000 1.000 9.57427  ? 170 ASN A C   1 
ATOM   1504 O  O   . ASN A 1 167 ? -7.51000  -11.82400 61.59200 1.000 10.50859 ? 170 ASN A O   1 
ATOM   1505 C  CB  . ASN A 1 167 ? -10.47500 -10.98300 61.68900 1.000 10.92706 ? 170 ASN A CB  1 
ATOM   1506 C  CG  . ASN A 1 167 ? -11.78000 -10.43300 62.21600 1.000 13.07205 ? 170 ASN A CG  1 
ATOM   1507 O  OD1 . ASN A 1 167 ? -12.44600 -9.70800  61.44300 1.000 18.44638 ? 170 ASN A OD1 1 
ATOM   1508 N  ND2 . ASN A 1 167 ? -12.13500 -10.62800 63.45800 1.000 12.19827 ? 170 ASN A ND2 1 
ATOM   1509 N  N   . ILE A 1 168 ? -8.68200  -13.75000 61.87800 1.000 10.26382 ? 171 ILE A N   1 
ATOM   1510 C  CA  A ILE A 1 168 ? -7.74100  -14.60700 61.15600 0.780 10.95864 ? 171 ILE A CA  1 
ATOM   1511 C  CA  B ILE A 1 168 ? -7.75200  -14.60800 61.14600 0.220 10.91996 ? 171 ILE A CA  1 
ATOM   1512 C  C   . ILE A 1 168 ? -8.33400  -14.89600 59.76700 1.000 11.47713 ? 171 ILE A C   1 
ATOM   1513 O  O   . ILE A 1 168 ? -9.55400  -14.91900 59.57700 1.000 11.11656 ? 171 ILE A O   1 
ATOM   1514 C  CB  A ILE A 1 168 ? -7.53900  -15.93100 61.94200 0.780 11.65609 ? 171 ILE A CB  1 
ATOM   1515 C  CB  B ILE A 1 168 ? -7.49200  -15.91100 61.93400 0.220 8.08996  ? 171 ILE A CB  1 
ATOM   1516 C  CG1 A ILE A 1 168 ? -7.18100  -15.67300 63.42100 0.780 12.06667 ? 171 ILE A CG1 1 
ATOM   1517 C  CG1 B ILE A 1 168 ? -6.87800  -15.57200 63.28300 0.220 12.03996 ? 171 ILE A CG1 1 
ATOM   1518 C  CG2 A ILE A 1 168 ? -6.47400  -16.81900 61.26400 0.780 12.58779 ? 171 ILE A CG2 1 
ATOM   1519 C  CG2 B ILE A 1 168 ? -6.55700  -16.84200 61.16800 0.220 15.74996 ? 171 ILE A CG2 1 
ATOM   1520 C  CD1 A ILE A 1 168 ? -7.32600  -16.96100 64.35700 0.780 12.62990 ? 171 ILE A CD1 1 
ATOM   1521 C  CD1 B ILE A 1 168 ? -5.64000  -14.76800 63.14400 0.220 11.08996 ? 171 ILE A CD1 1 
ATOM   1522 N  N   . GLU A 1 169 ? -7.45200  -15.14700 58.79300 1.000 11.35080 ? 172 GLU A N   1 
ATOM   1523 C  CA  . GLU A 1 169 ? -7.87000  -15.31200 57.38800 1.000 12.17984 ? 172 GLU A CA  1 
ATOM   1524 C  C   . GLU A 1 169 ? -8.80900  -16.48600 57.15700 1.000 13.04310 ? 172 GLU A C   1 
ATOM   1525 O  O   . GLU A 1 169 ? -9.50000  -16.53900 56.12600 1.000 14.45117 ? 172 GLU A O   1 
ATOM   1526 C  CB  . GLU A 1 169 ? -6.66100  -15.41900 56.47100 1.000 16.29612 ? 172 GLU A CB  1 
ATOM   1527 C  CG  . GLU A 1 169 ? -5.83200  -16.60600 56.81200 1.000 19.54125 ? 172 GLU A CG  1 
ATOM   1528 C  CD  . GLU A 1 169 ? -4.51300  -16.66700 56.02400 1.000 25.69725 ? 172 GLU A CD  1 
ATOM   1529 O  OE1 . GLU A 1 169 ? -4.06000  -15.59500 55.53600 1.000 24.86557 ? 172 GLU A OE1 1 
ATOM   1530 O  OE2 . GLU A 1 169 ? -3.95800  -17.78600 55.95300 1.000 33.45996 ? 172 GLU A OE2 1 
ATOM   1531 N  N   . ASP A 1 170 ? -8.85200  -17.43400 58.09400 1.000 14.35115 ? 173 ASP A N   1 
ATOM   1532 C  CA  A ASP A 1 170 ? -9.73300  -18.58200 57.95200 0.590 15.21178 ? 173 ASP A CA  1 
ATOM   1533 C  CA  B ASP A 1 170 ? -9.72400  -18.59300 57.98100 0.410 18.37996 ? 173 ASP A CA  1 
ATOM   1534 C  C   . ASP A 1 170 ? -11.11300 -18.34900 58.56000 1.000 15.91713 ? 173 ASP A C   1 
ATOM   1535 O  O   . ASP A 1 170 ? -11.90900 -19.27700 58.64800 1.000 18.65430 ? 173 ASP A O   1 
ATOM   1536 C  CB  A ASP A 1 170 ? -9.07500  -19.79700 58.57400 0.590 15.50392 ? 173 ASP A CB  1 
ATOM   1537 C  CB  B ASP A 1 170 ? -9.06200  -19.83200 58.60400 0.410 19.64996 ? 173 ASP A CB  1 
ATOM   1538 C  CG  A ASP A 1 170 ? -9.18100  -19.80400 60.08000 0.590 14.98544 ? 173 ASP A CG  1 
ATOM   1539 C  CG  B ASP A 1 170 ? -8.65900  -19.62200 60.06200 0.410 17.63996 ? 173 ASP A CG  1 
ATOM   1540 O  OD1 A ASP A 1 170 ? -9.36600  -18.72300 60.71700 0.590 15.00913 ? 173 ASP A OD1 1 
ATOM   1541 O  OD1 B ASP A 1 170 ? -9.13400  -18.62000 60.64500 0.410 14.00996 ? 173 ASP A OD1 1 
ATOM   1542 O  OD2 A ASP A 1 170 ? -9.05400  -20.90100 60.65400 0.590 14.52749 ? 173 ASP A OD2 1 
ATOM   1543 O  OD2 B ASP A 1 170 ? -7.89700  -20.45300 60.64100 0.410 17.40996 ? 173 ASP A OD2 1 
ATOM   1544 N  N   . GLY A 1 171 ? -11.42300 -17.14000 58.97500 1.000 14.70909 ? 174 GLY A N   1 
ATOM   1545 C  CA  . GLY A 1 171 ? -12.71700 -16.85600 59.55000 1.000 14.53276 ? 174 GLY A CA  1 
ATOM   1546 C  C   . GLY A 1 171 ? -12.79100 -17.15300 61.02200 1.000 13.90636 ? 174 GLY A C   1 
ATOM   1547 O  O   . GLY A 1 171 ? -13.87000 -17.13900 61.59200 1.000 15.93819 ? 174 GLY A O   1 
ATOM   1548 N  N   . SER A 1 172 ? -11.67100 -17.41900 61.67400 1.000 12.97994 ? 175 SER A N   1 
ATOM   1549 C  CA  . SER A 1 172 ? -11.66700 -17.46900 63.13500 1.000 12.64832 ? 175 SER A CA  1 
ATOM   1550 C  C   . SER A 1 172 ? -11.06900 -16.17000 63.67400 1.000 11.16656 ? 175 SER A C   1 
ATOM   1551 O  O   . SER A 1 172 ? -10.72200 -15.28000 62.90700 1.000 12.39829 ? 175 SER A O   1 
ATOM   1552 C  CB  . SER A 1 172 ? -10.93600 -18.67500 63.67600 1.000 15.60394 ? 175 SER A CB  1 
ATOM   1553 O  OG  . SER A 1 172 ? -9.60000  -18.67100 63.35000 1.000 18.04897 ? 175 SER A OG  1 
ATOM   1554 N  N   . VAL A 1 173 ? -10.96300 -16.06800 64.98100 1.000 10.07169 ? 176 VAL A N   1 
ATOM   1555 C  CA  . VAL A 1 173 ? -10.42700 -14.87300 65.64300 1.000 9.93747  ? 176 VAL A CA  1 
ATOM   1556 C  C   . VAL A 1 173 ? -9.32000  -15.30500 66.60600 1.000 9.43478  ? 176 VAL A C   1 
ATOM   1557 O  O   . VAL A 1 173 ? -9.48200  -16.28300 67.33600 1.000 10.30067 ? 176 VAL A O   1 
ATOM   1558 C  CB  . VAL A 1 173 ? -11.56600 -14.16200 66.40400 1.000 11.07971 ? 176 VAL A CB  1 
ATOM   1559 C  CG1 . VAL A 1 173 ? -11.05400 -13.02200 67.30100 1.000 11.35606 ? 176 VAL A CG1 1 
ATOM   1560 C  CG2 . VAL A 1 173 ? -12.64700 -13.65400 65.40100 1.000 12.37197 ? 176 VAL A CG2 1 
ATOM   1561 N  N   . GLN A 1 174 ? -8.24600  -14.52300 66.62900 1.000 9.38214  ? 177 GLN A N   1 
ATOM   1562 C  CA  . GLN A 1 174 ? -7.13500  -14.71400 67.55100 1.000 9.41898  ? 177 GLN A CA  1 
ATOM   1563 C  C   . GLN A 1 174 ? -7.30200  -13.73200 68.72100 1.000 8.93472  ? 177 GLN A C   1 
ATOM   1564 O  O   . GLN A 1 174 ? -7.29500  -12.51600 68.51700 1.000 9.41109  ? 177 GLN A O   1 
ATOM   1565 C  CB  . GLN A 1 174 ? -5.83200  -14.39900 66.79900 1.000 9.72428  ? 177 GLN A CB  1 
ATOM   1566 C  CG  . GLN A 1 174 ? -4.58900  -14.27600 67.69200 1.000 9.73218  ? 177 GLN A CG  1 
ATOM   1567 C  CD  . GLN A 1 174 ? -4.11900  -15.61600 68.24600 1.000 10.16644 ? 177 GLN A CD  1 
ATOM   1568 O  OE1 . GLN A 1 174 ? -3.71900  -16.50800 67.48200 1.000 12.00614 ? 177 GLN A OE1 1 
ATOM   1569 N  NE2 . GLN A 1 174 ? -4.18800  -15.78800 69.56900 1.000 10.33225 ? 177 GLN A NE2 1 
ATOM   1570 N  N   . LEU A 1 175 ? -7.34800  -14.26000 69.94500 1.000 8.90313  ? 178 LEU A N   1 
ATOM   1571 C  CA  . LEU A 1 175 ? -7.42500  -13.43400 71.14400 1.000 9.14527  ? 178 LEU A CA  1 
ATOM   1572 C  C   . LEU A 1 175 ? -6.04300  -12.92900 71.49600 1.000 8.42413  ? 178 LEU A C   1 
ATOM   1573 O  O   . LEU A 1 175 ? -5.06800  -13.69100 71.46900 1.000 9.29002  ? 178 LEU A O   1 
ATOM   1574 C  CB  . LEU A 1 175 ? -7.98400  -14.26300 72.29000 1.000 10.15065 ? 178 LEU A CB  1 
ATOM   1575 C  CG  . LEU A 1 175 ? -8.56200  -13.48200 73.49100 1.000 10.67966 ? 178 LEU A CG  1 
ATOM   1576 C  CD1 . LEU A 1 175 ? -9.76100  -12.66500 73.04800 1.000 12.08246 ? 178 LEU A CD1 1 
ATOM   1577 C  CD2 . LEU A 1 175 ? -8.92700  -14.46200 74.56800 1.000 11.98245 ? 178 LEU A CD2 1 
ATOM   1578 N  N   . ALA A 1 176 ? -5.98400  -11.68100 71.94900 1.000 9.20843  ? 179 ALA A N   1 
ATOM   1579 C  CA  . ALA A 1 176 ? -4.73400  -11.06600 72.42600 1.000 9.17948  ? 179 ALA A CA  1 
ATOM   1580 C  C   . ALA A 1 176 ? -5.05200  -10.35800 73.74400 1.000 9.16369  ? 179 ALA A C   1 
ATOM   1581 O  O   . ALA A 1 176 ? -5.43900  -9.18600  73.76000 1.000 9.23475  ? 179 ALA A O   1 
ATOM   1582 C  CB  . ALA A 1 176 ? -4.16900  -10.12500 71.38400 1.000 10.68493 ? 179 ALA A CB  1 
ATOM   1583 N  N   . ASP A 1 177 ? -4.93000  -11.06000 74.85700 1.000 9.85851  ? 180 ASP A N   1 
ATOM   1584 C  CA  . ASP A 1 177 ? -5.14400  -10.47400 76.16200 1.000 9.35319  ? 180 ASP A CA  1 
ATOM   1585 C  C   . ASP A 1 177 ? -4.11000  -9.37900  76.39000 1.000 9.16632  ? 180 ASP A C   1 
ATOM   1586 O  O   . ASP A 1 177 ? -2.92100  -9.56400  76.14100 1.000 9.81114  ? 180 ASP A O   1 
ATOM   1587 C  CB  . ASP A 1 177 ? -5.02200  -11.57600 77.22300 1.000 9.76113  ? 180 ASP A CB  1 
ATOM   1588 C  CG  . ASP A 1 177 ? -5.26600  -11.01100 78.61800 1.000 11.39554 ? 180 ASP A CG  1 
ATOM   1589 O  OD1 . ASP A 1 177 ? -4.29900  -10.51100 79.22100 1.000 10.93232 ? 180 ASP A OD1 1 
ATOM   1590 O  OD2 . ASP A 1 177 ? -6.43300  -10.99300 79.05600 1.000 12.87729 ? 180 ASP A OD2 1 
ATOM   1591 N  N   . HIS A 1 178 ? -4.56500  -8.22400  76.88500 1.000 8.93998  ? 181 HIS A N   1 
ATOM   1592 C  CA  . HIS A 1 178 ? -3.68400  -7.10100  77.21300 1.000 9.32160  ? 181 HIS A CA  1 
ATOM   1593 C  C   . HIS A 1 178 ? -3.75600  -6.83700  78.71900 1.000 9.65059  ? 181 HIS A C   1 
ATOM   1594 O  O   . HIS A 1 178 ? -4.83800  -6.60900  79.29300 1.000 10.18750 ? 181 HIS A O   1 
ATOM   1595 C  CB  . HIS A 1 178 ? -4.14700  -5.83300  76.49400 1.000 9.00315  ? 181 HIS A CB  1 
ATOM   1596 C  CG  . HIS A 1 178 ? -3.71900  -5.73100  75.05800 1.000 8.50045  ? 181 HIS A CG  1 
ATOM   1597 N  ND1 . HIS A 1 178 ? -3.97800  -6.72200  74.11800 1.000 8.22147  ? 181 HIS A ND1 1 
ATOM   1598 C  CD2 . HIS A 1 178 ? -3.05600  -4.74400  74.38400 1.000 8.60573  ? 181 HIS A CD2 1 
ATOM   1599 C  CE1 . HIS A 1 178 ? -3.50400  -6.32700  72.93400 1.000 8.60047  ? 181 HIS A CE1 1 
ATOM   1600 N  NE2 . HIS A 1 178 ? -2.93400  -5.13600  73.06500 1.000 7.85301  ? 181 HIS A NE2 1 
ATOM   1601 N  N   . TYR A 1 179 ? -2.57200  -6.82500  79.33500 1.000 8.84523  ? 182 TYR A N   1 
ATOM   1602 C  CA  . TYR A 1 179 ? -2.37300  -6.36500  80.70500 1.000 8.85050  ? 182 TYR A CA  1 
ATOM   1603 C  C   . TYR A 1 179 ? -1.51100  -5.11000  80.65000 1.000 8.32675  ? 182 TYR A C   1 
ATOM   1604 O  O   . TYR A 1 179 ? -0.50300  -5.10200  79.94800 1.000 9.13474  ? 182 TYR A O   1 
ATOM   1605 C  CB  . TYR A 1 179 ? -1.66000  -7.44500  81.51100 1.000 10.37173 ? 182 TYR A CB  1 
ATOM   1606 C  CG  . TYR A 1 179 ? -1.43100  -6.98400  82.90700 1.000 12.34828 ? 182 TYR A CG  1 
ATOM   1607 C  CD1 . TYR A 1 179 ? -2.48600  -6.98500  83.83200 1.000 14.70120 ? 182 TYR A CD1 1 
ATOM   1608 C  CD2 . TYR A 1 179 ? -0.21300  -6.46000  83.29400 1.000 14.90122 ? 182 TYR A CD2 1 
ATOM   1609 C  CE1 . TYR A 1 179 ? -2.30900  -6.52700  85.12000 1.000 17.58839 ? 182 TYR A CE1 1 
ATOM   1610 C  CE2 . TYR A 1 179 ? -0.01800  -5.98200  84.60900 1.000 16.44614 ? 182 TYR A CE2 1 
ATOM   1611 C  CZ  . TYR A 1 179 ? -1.07800  -6.01800  85.49500 1.000 17.33836 ? 182 TYR A CZ  1 
ATOM   1612 O  OH  . TYR A 1 179 ? -0.90200  -5.61400  86.78400 1.000 20.86246 ? 182 TYR A OH  1 
ATOM   1613 N  N   . GLN A 1 180 ? -1.94900  -4.04700  81.30200 1.000 8.59257  ? 183 GLN A N   1 
ATOM   1614 C  CA  . GLN A 1 180 ? -1.28400  -2.76300  81.15300 1.000 8.34780  ? 183 GLN A CA  1 
ATOM   1615 C  C   . GLN A 1 180 ? -1.08400  -2.11800  82.51700 1.000 8.56888  ? 183 GLN A C   1 
ATOM   1616 O  O   . GLN A 1 180 ? -1.97800  -2.13200  83.37300 1.000 8.92682  ? 183 GLN A O   1 
ATOM   1617 C  CB  . GLN A 1 180 ? -2.21800  -1.87300  80.27600 1.000 9.37951  ? 183 GLN A CB  1 
ATOM   1618 C  CG  . GLN A 1 180 ? -1.71700  -0.44500  80.09600 1.000 9.31634  ? 183 GLN A CG  1 
ATOM   1619 C  CD  . GLN A 1 180 ? -2.61600  0.36600   79.19200 1.000 9.26107  ? 183 GLN A CD  1 
ATOM   1620 O  OE1 . GLN A 1 180 ? -3.35800  -0.18500  78.36200 1.000 9.64533  ? 183 GLN A OE1 1 
ATOM   1621 N  NE2 . GLN A 1 180 ? -2.51800  1.70800   79.30900 1.000 11.49292 ? 183 GLN A NE2 1 
ATOM   1622 N  N   . GLN A 1 181 ? 0.06800   -1.45600  82.66000 1.000 9.52426  ? 184 GLN A N   1 
ATOM   1623 C  CA  A GLN A 1 181 ? 0.37000   -0.67500  83.86400 0.690 11.18762 ? 184 GLN A CA  1 
ATOM   1624 C  CA  B GLN A 1 181 ? 0.34600   -0.67000  83.86000 0.310 8.26996  ? 184 GLN A CA  1 
ATOM   1625 C  C   . GLN A 1 181 ? 0.98400   0.62300   83.41700 1.000 10.11907 ? 184 GLN A C   1 
ATOM   1626 O  O   . GLN A 1 181 ? 1.92200   0.61500   82.60200 1.000 11.64820 ? 184 GLN A O   1 
ATOM   1627 C  CB  A GLN A 1 181 ? 1.39600   -1.42500  84.69000 0.690 14.02217 ? 184 GLN A CB  1 
ATOM   1628 C  CB  B GLN A 1 181 ? 1.29600   -1.38200  84.82600 0.310 13.73996 ? 184 GLN A CB  1 
ATOM   1629 C  CG  A GLN A 1 181 ? 2.04200   -0.62300  85.77300 0.690 17.10938 ? 184 GLN A CG  1 
ATOM   1630 C  CG  B GLN A 1 181 ? 0.87900   -2.75700  85.26000 0.310 18.24996 ? 184 GLN A CG  1 
ATOM   1631 C  CD  A GLN A 1 181 ? 1.22100   -0.62500  86.92300 0.690 20.06763 ? 184 GLN A CD  1 
ATOM   1632 C  CD  B GLN A 1 181 ? 1.77600   -3.34800  86.37600 0.310 25.22996 ? 184 GLN A CD  1 
ATOM   1633 O  OE1 A GLN A 1 181 ? 0.96700   -1.69300  87.49500 0.690 22.93903 ? 184 GLN A OE1 1 
ATOM   1634 O  OE1 B GLN A 1 181 ? 2.63300   -2.66700  86.94400 0.310 17.16996 ? 184 GLN A OE1 1 
ATOM   1635 N  NE2 A GLN A 1 181 ? 0.83600   0.58600   87.39200 0.690 20.51505 ? 184 GLN A NE2 1 
ATOM   1636 N  NE2 B GLN A 1 181 ? 1.55400   -4.61500  86.69700 0.310 33.63996 ? 184 GLN A NE2 1 
ATOM   1637 N  N   . ASN A 1 182 ? 0.49200   1.74000   83.97800 1.000 9.34529  ? 185 ASN A N   1 
ATOM   1638 C  CA  . ASN A 1 182 ? 1.06600   3.04300   83.66600 1.000 10.04538 ? 185 ASN A CA  1 
ATOM   1639 C  C   . ASN A 1 182 ? 1.51100   3.70800   84.95500 1.000 10.44016 ? 185 ASN A C   1 
ATOM   1640 O  O   . ASN A 1 182 ? 0.77900   3.69200   85.95800 1.000 11.61662 ? 185 ASN A O   1 
ATOM   1641 C  CB  . ASN A 1 182 ? 0.06300   4.00800   82.99600 1.000 10.89548 ? 185 ASN A CB  1 
ATOM   1642 C  CG  . ASN A 1 182 ? -0.30100  3.56300   81.57000 1.000 11.46660 ? 185 ASN A CG  1 
ATOM   1643 O  OD1 . ASN A 1 182 ? -0.70100  2.44200   81.34800 1.000 15.46971 ? 185 ASN A OD1 1 
ATOM   1644 N  ND2 . ASN A 1 182 ? -0.24000  4.46400   80.63200 1.000 10.19013 ? 185 ASN A ND2 1 
ATOM   1645 N  N   . THR A 1 183 ? 2.69700   4.31600   84.91300 1.000 10.50596 ? 186 THR A N   1 
ATOM   1646 C  CA  A THR A 1 183 ? 3.30500   4.97500   86.07600 0.600 10.61650 ? 186 THR A CA  1 
ATOM   1647 C  CA  B THR A 1 183 ? 3.17300   5.02800   86.07900 0.400 13.11996 ? 186 THR A CA  1 
ATOM   1648 C  C   . THR A 1 183 ? 3.68900   6.39500   85.66400 1.000 10.21645 ? 186 THR A C   1 
ATOM   1649 O  O   . THR A 1 183 ? 4.37100   6.54800   84.62700 1.000 11.11129 ? 186 THR A O   1 
ATOM   1650 C  CB  A THR A 1 183 ? 4.60000   4.15200   86.47700 0.600 10.49017 ? 186 THR A CB  1 
ATOM   1651 C  CB  B THR A 1 183 ? 4.27400   4.29800   86.82300 0.400 17.72996 ? 186 THR A CB  1 
ATOM   1652 O  OG1 A THR A 1 183 ? 4.30900   2.73200   86.62900 0.600 10.84810 ? 186 THR A OG1 1 
ATOM   1653 O  OG1 B THR A 1 183 ? 5.35000   4.10700   85.91800 0.400 13.52996 ? 186 THR A OG1 1 
ATOM   1654 C  CG2 A THR A 1 183 ? 5.21100   4.70500   87.76600 0.600 12.03509 ? 186 THR A CG2 1 
ATOM   1655 C  CG2 B THR A 1 183 ? 3.75700   2.97500   87.37200 0.400 14.01996 ? 186 THR A CG2 1 
ATOM   1656 N  N   . PRO A 1 184 ? 3.31400   7.43500   86.41300 1.000 10.40858 ? 187 PRO A N   1 
ATOM   1657 C  CA  . PRO A 1 184 ? 3.72100   8.78900   86.03400 1.000 10.42700 ? 187 PRO A CA  1 
ATOM   1658 C  C   . PRO A 1 184 ? 5.21900   8.95900   86.20000 1.000 10.43753 ? 187 PRO A C   1 
ATOM   1659 O  O   . PRO A 1 184 ? 5.85400   8.32900   87.03400 1.000 11.73242 ? 187 PRO A O   1 
ATOM   1660 C  CB  . PRO A 1 184 ? 2.93500   9.69400   87.00900 1.000 12.02456 ? 187 PRO A CB  1 
ATOM   1661 C  CG  . PRO A 1 184 ? 2.74600   8.85800   88.21600 1.000 12.22195 ? 187 PRO A CG  1 
ATOM   1662 C  CD  . PRO A 1 184 ? 2.59000   7.39400   87.68100 1.000 11.72716 ? 187 PRO A CD  1 
ATOM   1663 N  N   . ILE A 1 185 ? 5.76500   9.88700   85.42200 1.000 10.84547 ? 188 ILE A N   1 
ATOM   1664 C  CA  . ILE A 1 185 ? 7.15600   10.30600  85.53000 1.000 11.43765 ? 188 ILE A CA  1 
ATOM   1665 C  C   . ILE A 1 185 ? 7.24200   11.50700  86.45300 1.000 10.91916 ? 188 ILE A C   1 
ATOM   1666 O  O   . ILE A 1 185 ? 6.46400   12.47800  86.31700 1.000 10.76388 ? 188 ILE A O   1 
ATOM   1667 C  CB  . ILE A 1 185 ? 7.70200   10.62900  84.12400 1.000 11.86401 ? 188 ILE A CB  1 
ATOM   1668 C  CG1 . ILE A 1 185 ? 7.72200   9.31500   83.31900 1.000 12.74833 ? 188 ILE A CG1 1 
ATOM   1669 C  CG2 . ILE A 1 185 ? 9.10700   11.26400  84.24300 1.000 13.80898 ? 188 ILE A CG2 1 
ATOM   1670 C  CD1 . ILE A 1 185 ? 8.08900   9.45600   81.84100 1.000 12.90888 ? 188 ILE A CD1 1 
ATOM   1671 N  N   . GLY A 1 186 ? 8.14300   11.44000  87.41300 1.000 12.02982 ? 189 GLY A N   1 
ATOM   1672 C  CA  . GLY A 1 186 ? 8.33200   12.55700  88.32500 1.000 12.81939 ? 189 GLY A CA  1 
ATOM   1673 C  C   . GLY A 1 186 ? 7.34000   12.52200  89.47200 1.000 12.38250 ? 189 GLY A C   1 
ATOM   1674 O  O   . GLY A 1 186 ? 6.53300   11.60500  89.62500 1.000 12.53515 ? 189 GLY A O   1 
ATOM   1675 N  N   . ASP A 1 187 ? 7.48100   13.49900  90.37000 1.000 12.26669 ? 190 ASP A N   1 
ATOM   1676 C  CA  . ASP A 1 187 ? 6.69700   13.61700  91.59400 1.000 12.48251 ? 190 ASP A CA  1 
ATOM   1677 C  C   . ASP A 1 187 ? 5.47100   14.49400  91.45800 1.000 12.41934 ? 190 ASP A C   1 
ATOM   1678 O  O   . ASP A 1 187 ? 4.79500   14.77800  92.45500 1.000 12.46672 ? 190 ASP A O   1 
ATOM   1679 C  CB  . ASP A 1 187 ? 7.55200   14.16800  92.73600 1.000 13.49842 ? 190 ASP A CB  1 
ATOM   1680 C  CG  . ASP A 1 187 ? 8.65500   13.25700  93.12400 1.000 15.13020 ? 190 ASP A CG  1 
ATOM   1681 O  OD1 . ASP A 1 187 ? 8.46100   12.02900  93.06500 1.000 14.85648 ? 190 ASP A OD1 1 
ATOM   1682 O  OD2 . ASP A 1 187 ? 9.72900   13.76100  93.52600 1.000 16.26717 ? 190 ASP A OD2 1 
ATOM   1683 N  N   . GLY A 1 188 ? 5.15300   14.91300  90.24300 1.000 11.83506 ? 191 GLY A N   1 
ATOM   1684 C  CA  . GLY A 1 188 ? 4.06900   15.83900  90.04900 1.000 11.40870 ? 191 GLY A CA  1 
ATOM   1685 C  C   . GLY A 1 188 ? 2.70200   15.24700  90.29900 1.000 11.13761 ? 191 GLY A C   1 
ATOM   1686 O  O   . GLY A 1 188 ? 2.53600   14.04000  90.54600 1.000 11.60872 ? 191 GLY A O   1 
ATOM   1687 N  N   . PRO A 1 189 ? 1.68300   16.10900  90.24700 1.000 10.87442 ? 192 PRO A N   1 
ATOM   1688 C  CA  . PRO A 1 189 ? 0.31200   15.66000  90.51900 1.000 10.88758 ? 192 PRO A CA  1 
ATOM   1689 C  C   . PRO A 1 189 ? -0.21900  14.80000  89.38300 1.000 11.16130 ? 192 PRO A C   1 
ATOM   1690 O  O   . PRO A 1 189 ? 0.11200   15.00000  88.20400 1.000 11.83506 ? 192 PRO A O   1 
ATOM   1691 C  CB  . PRO A 1 189 ? -0.46600  16.98600  90.58100 1.000 12.04562 ? 192 PRO A CB  1 
ATOM   1692 C  CG  . PRO A 1 189 ? 0.28600   17.91000  89.62500 1.000 12.17458 ? 192 PRO A CG  1 
ATOM   1693 C  CD  . PRO A 1 189 ? 1.74700   17.51100  89.76700 1.000 11.84033 ? 192 PRO A CD  1 
ATOM   1694 N  N   . VAL A 1 190 ? -1.11000  13.86400  89.72400 1.000 10.64545 ? 193 VAL A N   1 
ATOM   1695 C  CA  . VAL A 1 190 ? -1.82400  13.09000  88.70800 1.000 11.00075 ? 193 VAL A CA  1 
ATOM   1696 C  C   . VAL A 1 190 ? -3.27300  12.97900  89.14700 1.000 10.39279 ? 193 VAL A C   1 
ATOM   1697 O  O   . VAL A 1 190 ? -3.60800  13.14500  90.31500 1.000 12.09036 ? 193 VAL A O   1 
ATOM   1698 C  CB  . VAL A 1 190 ? -1.21900  11.70100  88.45800 1.000 12.96415 ? 193 VAL A CB  1 
ATOM   1699 C  CG1 . VAL A 1 190 ? 0.19500   11.83800  87.89100 1.000 15.61183 ? 193 VAL A CG1 1 
ATOM   1700 C  CG2 . VAL A 1 190 ? -1.30600  10.86100  89.74600 1.000 14.21693 ? 193 VAL A CG2 1 
ATOM   1701 N  N   . LEU A 1 191 ? -4.13500  12.62900  88.20000 1.000 11.29553 ? 194 LEU A N   1 
ATOM   1702 C  CA  . LEU A 1 191 ? -5.53700  12.36600  88.48900 1.000 11.36659 ? 194 LEU A CA  1 
ATOM   1703 C  C   . LEU A 1 191 ? -5.75600  10.86100  88.43300 1.000 12.46145 ? 194 LEU A C   1 
ATOM   1704 O  O   . LEU A 1 191 ? -5.71700  10.26600  87.35600 1.000 15.66710 ? 194 LEU A O   1 
ATOM   1705 C  CB  . LEU A 1 191 ? -6.40700  13.10800  87.45800 1.000 11.68505 ? 194 LEU A CB  1 
ATOM   1706 C  CG  . LEU A 1 191 ? -6.36500  14.62500  87.53500 1.000 11.19815 ? 194 LEU A CG  1 
ATOM   1707 C  CD1 . LEU A 1 191 ? -7.19600  15.20400  86.41100 1.000 12.42198 ? 194 LEU A CD1 1 
ATOM   1708 C  CD2 . LEU A 1 191 ? -6.95000  15.10600  88.87700 1.000 13.26945 ? 194 LEU A CD2 1 
ATOM   1709 N  N   . LEU A 1 192 ? -5.92300  10.23800  89.55500 1.000 14.00901 ? 195 LEU A N   1 
ATOM   1710 C  CA  . LEU A 1 192 ? -6.19600  8.81400   89.57100 1.000 14.76436 ? 195 LEU A CA  1 
ATOM   1711 C  C   . LEU A 1 192 ? -7.67400  8.60500   89.32300 1.000 14.44853 ? 195 LEU A C   1 
ATOM   1712 O  O   . LEU A 1 192 ? -8.50500  9.26300   89.95700 1.000 17.31993 ? 195 LEU A O   1 
ATOM   1713 C  CB  . LEU A 1 192 ? -5.82400  8.17600   90.90100 1.000 16.32508 ? 195 LEU A CB  1 
ATOM   1714 C  CG  . LEU A 1 192 ? -4.29700  8.09800   91.19500 1.000 17.25677 ? 195 LEU A CG  1 
ATOM   1715 C  CD1 . LEU A 1 192 ? -3.95400  7.05000   92.29700 1.000 20.09132 ? 195 LEU A CD1 1 
ATOM   1716 C  CD2 . LEU A 1 192 ? -3.40100  7.85000   89.93400 1.000 16.98305 ? 195 LEU A CD2 1 
ATOM   1717 N  N   . PRO A 1 193 ? -8.06200  7.70400   88.43300 1.000 13.19049 ? 196 PRO A N   1 
ATOM   1718 C  CA  . PRO A 1 193 ? -9.47500  7.60800   88.05300 1.000 14.35905 ? 196 PRO A CA  1 
ATOM   1719 C  C   . PRO A 1 193 ? -10.25900 6.59200   88.86400 1.000 13.46684 ? 196 PRO A C   1 
ATOM   1720 O  O   . PRO A 1 193 ? -9.71400  5.63900   89.39400 1.000 15.49603 ? 196 PRO A O   1 
ATOM   1721 C  CB  . PRO A 1 193 ? -9.37000  7.06100   86.63400 1.000 14.71436 ? 196 PRO A CB  1 
ATOM   1722 C  CG  . PRO A 1 193 ? -8.18000  6.14700   86.69400 1.000 14.15376 ? 196 PRO A CG  1 
ATOM   1723 C  CD  . PRO A 1 193 ? -7.19300  6.89900   87.56700 1.000 13.54316 ? 196 PRO A CD  1 
ATOM   1724 N  N   . ASP A 1 194 ? -11.57300 6.78100   88.89300 1.000 14.75647 ? 197 ASP A N   1 
ATOM   1725 C  CA  A ASP A 1 194 ? -12.47300 5.68400   89.22800 0.570 14.30378 ? 197 ASP A CA  1 
ATOM   1726 C  CA  B ASP A 1 194 ? -12.31700 5.59500   89.28100 0.430 16.36996 ? 197 ASP A CA  1 
ATOM   1727 C  C   . ASP A 1 194 ? -12.51200 4.69400   88.06200 1.000 14.11165 ? 197 ASP A C   1 
ATOM   1728 O  O   . ASP A 1 194 ? -12.07700 5.00200   86.93400 1.000 14.61171 ? 197 ASP A O   1 
ATOM   1729 C  CB  A ASP A 1 194 ? -13.86900 6.22800   89.55500 0.570 14.75120 ? 197 ASP A CB  1 
ATOM   1730 C  CB  B ASP A 1 194 ? -13.60300 5.94300   90.01700 0.430 23.33996 ? 197 ASP A CB  1 
ATOM   1731 C  CG  A ASP A 1 194 ? -13.90000 6.99800   90.87200 0.570 15.40128 ? 197 ASP A CG  1 
ATOM   1732 C  CG  B ASP A 1 194 ? -14.39600 6.97200   89.31400 0.430 18.04996 ? 197 ASP A CG  1 
ATOM   1733 O  OD1 A ASP A 1 194 ? -13.09100 6.69600   91.78700 0.570 17.27519 ? 197 ASP A OD1 1 
ATOM   1734 O  OD1 B ASP A 1 194 ? -14.05100 7.30200   88.15800 0.430 24.51996 ? 197 ASP A OD1 1 
ATOM   1735 O  OD2 A ASP A 1 194 ? -14.74500 7.90100   91.02800 0.570 16.76197 ? 197 ASP A OD2 1 
ATOM   1736 O  OD2 B ASP A 1 194 ? -15.37100 7.44500   89.93900 0.430 18.65996 ? 197 ASP A OD2 1 
ATOM   1737 N  N   . ASN A 1 195 ? -13.04700 3.49800   88.30300 1.000 13.59054 ? 198 ASN A N   1 
ATOM   1738 C  CA  . ASN A 1 195 ? -13.13900 2.50600   87.23200 1.000 14.04586 ? 198 ASN A CA  1 
ATOM   1739 C  C   . ASN A 1 195 ? -13.96500 3.06300   86.09100 1.000 14.06428 ? 198 ASN A C   1 
ATOM   1740 O  O   . ASN A 1 195 ? -15.06700 3.58500   86.30200 1.000 16.13032 ? 198 ASN A O   1 
ATOM   1741 C  CB  . ASN A 1 195 ? -13.80300 1.25200   87.76600 1.000 16.00662 ? 198 ASN A CB  1 
ATOM   1742 C  CG  . ASN A 1 195 ? -12.85900 0.41900   88.62300 1.000 17.44100 ? 198 ASN A CG  1 
ATOM   1743 O  OD1 . ASN A 1 195 ? -11.81100 0.88100   89.06600 1.000 16.74092 ? 198 ASN A OD1 1 
ATOM   1744 N  ND2 . ASN A 1 195 ? -13.19200 -0.86900  88.77700 1.000 19.99130 ? 198 ASN A ND2 1 
ATOM   1745 N  N   . HIS A 1 196 ? -13.46000 2.92000   84.87100 1.000 13.46947 ? 199 HIS A N   1 
ATOM   1746 C  CA  . HIS A 1 196 ? -14.18900 3.37200   83.69600 1.000 12.20353 ? 199 HIS A CA  1 
ATOM   1747 C  C   . HIS A 1 196 ? -13.57000 2.68800   82.48800 1.000 12.26406 ? 199 HIS A C   1 
ATOM   1748 O  O   . HIS A 1 196 ? -12.66700 1.86700   82.62400 1.000 12.98257 ? 199 HIS A O   1 
ATOM   1749 C  CB  . HIS A 1 196 ? -14.11900 4.90500   83.50400 1.000 12.75359 ? 199 HIS A CB  1 
ATOM   1750 C  CG  . HIS A 1 196 ? -12.73900 5.42800   83.19300 1.000 12.27196 ? 199 HIS A CG  1 
ATOM   1751 N  ND1 . HIS A 1 196 ? -11.73900 5.54300   84.13600 1.000 12.12720 ? 199 HIS A ND1 1 
ATOM   1752 C  CD2 . HIS A 1 196 ? -12.21900 5.89200   82.03300 1.000 11.47976 ? 199 HIS A CD2 1 
ATOM   1753 C  CE1 . HIS A 1 196 ? -10.68000 6.09200   83.55900 1.000 12.27196 ? 199 HIS A CE1 1 
ATOM   1754 N  NE2 . HIS A 1 196 ? -10.93100 6.27800   82.28100 1.000 11.72979 ? 199 HIS A NE2 1 
ATOM   1755 N  N   . TYR A 1 197 ? -14.05800 3.01500   81.30400 1.000 12.52199 ? 200 TYR A N   1 
ATOM   1756 C  CA  . TYR A 1 197 ? -13.46300 2.36600   80.13300 1.000 12.19300 ? 200 TYR A CA  1 
ATOM   1757 C  C   . TYR A 1 197 ? -13.28100 3.38800   78.99800 1.000 11.29816 ? 200 TYR A C   1 
ATOM   1758 O  O   . TYR A 1 197 ? -13.89300 4.47600   78.97400 1.000 12.54304 ? 200 TYR A O   1 
ATOM   1759 C  CB  . TYR A 1 197 ? -14.22700 1.10900   79.67800 1.000 13.77740 ? 200 TYR A CB  1 
ATOM   1760 C  CG  . TYR A 1 197 ? -15.61600 1.42400   79.16200 1.000 14.59592 ? 200 TYR A CG  1 
ATOM   1761 C  CD1 . TYR A 1 197 ? -16.68200 1.57900   80.02400 1.000 16.38561 ? 200 TYR A CD1 1 
ATOM   1762 C  CD2 . TYR A 1 197 ? -15.84800 1.51400   77.77800 1.000 15.31180 ? 200 TYR A CD2 1 
ATOM   1763 C  CE1 . TYR A 1 197 ? -17.96300 1.87900   79.54400 1.000 18.06213 ? 200 TYR A CE1 1 
ATOM   1764 C  CE2 . TYR A 1 197 ? -17.11100 1.75000   77.28900 1.000 16.75144 ? 200 TYR A CE2 1 
ATOM   1765 C  CZ  . TYR A 1 197 ? -18.16200 1.97000   78.17500 1.000 18.54639 ? 200 TYR A CZ  1 
ATOM   1766 O  OH  . TYR A 1 197 ? -19.43300 2.21900   77.65200 1.000 21.48885 ? 200 TYR A OH  1 
ATOM   1767 N  N   . LEU A 1 198 ? -12.45900 2.98100   78.02000 1.000 11.19025 ? 201 LEU A N   1 
ATOM   1768 C  CA  . LEU A 1 198 ? -12.30100 3.71800   76.77000 1.000 11.89297 ? 201 LEU A CA  1 
ATOM   1769 C  C   . LEU A 1 198 ? -12.91500 2.87900   75.65300 1.000 11.32184 ? 201 LEU A C   1 
ATOM   1770 O  O   . LEU A 1 198 ? -12.56200 1.70700   75.48300 1.000 12.41408 ? 201 LEU A O   1 
ATOM   1771 C  CB  . LEU A 1 198 ? -10.82500 3.97700   76.41700 1.000 11.39291 ? 201 LEU A CB  1 
ATOM   1772 C  CG  . LEU A 1 198 ? -9.97200  4.62700   77.52300 1.000 11.77716 ? 201 LEU A CG  1 
ATOM   1773 C  CD1 . LEU A 1 198 ? -8.54600  4.81100   77.05000 1.000 12.11668 ? 201 LEU A CD1 1 
ATOM   1774 C  CD2 . LEU A 1 198 ? -10.58000 5.98500   77.98400 1.000 12.25617 ? 201 LEU A CD2 1 
ATOM   1775 N  N   . SER A 1 199 ? -13.80300 3.47500   74.86200 1.000 11.95087 ? 202 SER A N   1 
ATOM   1776 C  CA  . SER A 1 199 ? -14.37200 2.80700   73.69000 1.000 12.34302 ? 202 SER A CA  1 
ATOM   1777 C  C   . SER A 1 199 ? -13.54100 3.19000   72.48000 1.000 11.62451 ? 202 SER A C   1 
ATOM   1778 O  O   . SER A 1 199 ? -13.35000 4.38300   72.20800 1.000 12.09036 ? 202 SER A O   1 
ATOM   1779 C  CB  . SER A 1 199 ? -15.79000 3.31800   73.51100 1.000 14.27483 ? 202 SER A CB  1 
ATOM   1780 O  OG  . SER A 1 199 ? -16.36500 2.76200   72.34000 1.000 16.06452 ? 202 SER A OG  1 
ATOM   1781 N  N   . VAL A 1 200 ? -12.94300 2.19100   71.82700 1.000 10.56912 ? 203 VAL A N   1 
ATOM   1782 C  CA  . VAL A 1 200 ? -11.93000 2.44500   70.80800 1.000 10.97707 ? 203 VAL A CA  1 
ATOM   1783 C  C   . VAL A 1 200 ? -12.36500 1.84700   69.47900 1.000 11.65346 ? 203 VAL A C   1 
ATOM   1784 O  O   . VAL A 1 200 ? -12.62700 0.63500   69.37100 1.000 14.29852 ? 203 VAL A O   1 
ATOM   1785 C  CB  . VAL A 1 200 ? -10.57300 1.84700   71.20900 1.000 11.47186 ? 203 VAL A CB  1 
ATOM   1786 C  CG1 . VAL A 1 200 ? -9.50100  2.25400   70.18000 1.000 12.05877 ? 203 VAL A CG1 1 
ATOM   1787 C  CG2 . VAL A 1 200 ? -10.15400 2.27900   72.58800 1.000 11.88507 ? 203 VAL A CG2 1 
ATOM   1788 N  N   . GLN A 1 201 ? -12.37000 2.67800   68.44300 1.000 11.21920 ? 204 GLN A N   1 
ATOM   1789 C  CA  A GLN A 1 201 ? -12.57000 2.22000   67.07400 0.590 12.17458 ? 204 GLN A CA  1 
ATOM   1790 C  CA  B GLN A 1 201 ? -12.57700 2.22400   67.06900 0.410 12.84996 ? 204 GLN A CA  1 
ATOM   1791 C  C   . GLN A 1 201 ? -11.33200 2.55900   66.25900 1.000 11.96929 ? 204 GLN A C   1 
ATOM   1792 O  O   . GLN A 1 201 ? -10.74700 3.65100   66.42400 1.000 12.68253 ? 204 GLN A O   1 
ATOM   1793 C  CB  A GLN A 1 201 ? -13.78200 2.88000   66.45000 0.590 13.50368 ? 204 GLN A CB  1 
ATOM   1794 C  CB  B GLN A 1 201 ? -13.84900 2.82400   66.40700 0.410 18.72996 ? 204 GLN A CB  1 
ATOM   1795 C  CG  A GLN A 1 201 ? -15.08000 2.41800   67.11500 0.590 13.51684 ? 204 GLN A CG  1 
ATOM   1796 C  CG  B GLN A 1 201 ? -13.95600 4.35300   66.39700 0.410 22.67996 ? 204 GLN A CG  1 
ATOM   1797 C  CD  A GLN A 1 201 ? -15.32300 2.97100   68.48700 0.590 14.43274 ? 204 GLN A CD  1 
ATOM   1798 C  CD  B GLN A 1 201 ? -15.36900 4.90500   66.02700 0.410 31.97996 ? 204 GLN A CD  1 
ATOM   1799 O  OE1 A GLN A 1 201 ? -15.56000 2.21700   69.45800 0.590 15.88555 ? 204 GLN A OE1 1 
ATOM   1800 O  OE1 B GLN A 1 201 ? -15.87000 5.90100   66.60700 0.410 15.82996 ? 204 GLN A OE1 1 
ATOM   1801 N  NE2 A GLN A 1 201 ? -15.24300 4.28300   68.61200 0.590 14.71436 ? 204 GLN A NE2 1 
ATOM   1802 N  NE2 B GLN A 1 201 ? -15.99200 4.27100   65.04600 0.410 30.91996 ? 204 GLN A NE2 1 
ATOM   1803 N  N   . SER A 1 202 ? -10.90500 1.62100   65.41300 1.000 11.64294 ? 205 SER A N   1 
ATOM   1804 C  CA  . SER A 1 202 ? -9.67900  1.77100   64.64900 1.000 11.95087 ? 205 SER A CA  1 
ATOM   1805 C  C   . SER A 1 202 ? -9.90600  1.30500   63.22800 1.000 12.40355 ? 205 SER A C   1 
ATOM   1806 O  O   . SER A 1 202 ? -10.47600 0.23800   62.99700 1.000 14.45643 ? 205 SER A O   1 
ATOM   1807 C  CB  . SER A 1 202 ? -8.60400  0.84700   65.24100 1.000 11.68768 ? 205 SER A CB  1 
ATOM   1808 O  OG  . SER A 1 202 ? -8.42400  1.08500   66.64900 1.000 11.75611 ? 205 SER A OG  1 
ATOM   1809 N  N   . ALA A 1 203 ? -9.40900  2.09200   62.28100 1.000 11.79295 ? 206 ALA A N   1 
ATOM   1810 C  CA  . ALA A 1 203 ? -9.51900  1.75000   60.86700 1.000 11.74032 ? 206 ALA A CA  1 
ATOM   1811 C  C   . ALA A 1 203 ? -8.10900  1.74000   60.28700 1.000 11.07971 ? 206 ALA A C   1 
ATOM   1812 O  O   . ALA A 1 203 ? -7.37300  2.73100   60.40900 1.000 11.46923 ? 206 ALA A O   1 
ATOM   1813 C  CB  . ALA A 1 203 ? -10.39200 2.75400   60.10000 1.000 14.20114 ? 206 ALA A CB  1 
ATOM   1814 N  N   . LEU A 1 204 ? -7.74400  0.65000   59.60900 1.000 11.04023 ? 207 LEU A N   1 
ATOM   1815 C  CA  . LEU A 1 204 ? -6.42300  0.49600   59.03000 1.000 10.23487 ? 207 LEU A CA  1 
ATOM   1816 C  C   . LEU A 1 204 ? -6.50000  0.64500   57.51500 1.000 10.80862 ? 207 LEU A C   1 
ATOM   1817 O  O   . LEU A 1 204 ? -7.43100  0.14600   56.87700 1.000 12.26669 ? 207 LEU A O   1 
ATOM   1818 C  CB  . LEU A 1 204 ? -5.84400  -0.87300  59.34600 1.000 10.77967 ? 207 LEU A CB  1 
ATOM   1819 C  CG  . LEU A 1 204 ? -5.98200  -1.38400  60.77200 1.000 11.52187 ? 207 LEU A CG  1 
ATOM   1820 C  CD1 . LEU A 1 204 ? -5.17900  -2.66100  60.96700 1.000 11.56661 ? 207 LEU A CD1 1 
ATOM   1821 C  CD2 . LEU A 1 204 ? -5.53900  -0.36500  61.78800 1.000 11.39817 ? 207 LEU A CD2 1 
ATOM   1822 N  N   . SER A 1 205 ? -5.51900  1.31700   56.92900 1.000 11.34553 ? 208 SER A N   1 
ATOM   1823 C  CA  . SER A 1 205 ? -5.50000  1.53000   55.48900 1.000 12.19300 ? 208 SER A CA  1 
ATOM   1824 C  C   . SER A 1 205 ? -4.04900  1.61300   55.02900 1.000 11.71926 ? 208 SER A C   1 
ATOM   1825 O  O   . SER A 1 205 ? -3.10000  1.45600   55.81500 1.000 11.06918 ? 208 SER A O   1 
ATOM   1826 C  CB  . SER A 1 205 ? -6.32200  2.78500   55.15400 1.000 12.69306 ? 208 SER A CB  1 
ATOM   1827 O  OG  . SER A 1 205 ? -5.74900  3.91900   55.77000 1.000 12.80623 ? 208 SER A OG  1 
ATOM   1828 N  N   . LYS A 1 206 ? -3.86300  1.87700   53.73400 1.000 13.76687 ? 209 LYS A N   1 
ATOM   1829 C  CA  . LYS A 1 206 ? -2.53600  2.05500   53.15400 1.000 15.05124 ? 209 LYS A CA  1 
ATOM   1830 C  C   . LYS A 1 206 ? -2.46400  3.42200   52.48400 1.000 14.63277 ? 209 LYS A C   1 
ATOM   1831 O  O   . LYS A 1 206 ? -3.48400  3.97300   52.07700 1.000 16.29612 ? 209 LYS A O   1 
ATOM   1832 C  CB  . LYS A 1 206 ? -2.28000  0.94800   52.11500 1.000 15.04597 ? 209 LYS A CB  1 
ATOM   1833 C  CG  . LYS A 1 206 ? -2.25700  -0.44700  52.71000 1.000 13.45631 ? 209 LYS A CG  1 
ATOM   1834 C  CD  . LYS A 1 206 ? -1.05400  -0.74900  53.60700 1.000 11.99035 ? 209 LYS A CD  1 
ATOM   1835 C  CE  . LYS A 1 206 ? -1.08900  -2.19800  54.05400 1.000 12.13773 ? 209 LYS A CE  1 
ATOM   1836 N  NZ  . LYS A 1 206 ? 0.05500   -2.50500  54.96700 1.000 11.38764 ? 209 LYS A NZ  1 
ATOM   1837 N  N   . ASP A 1 207 ? -1.26000  3.99000   52.43700 1.000 15.08809 ? 210 ASP A N   1 
ATOM   1838 C  CA  . ASP A 1 207 ? -0.96400  5.21700   51.68300 1.000 16.68038 ? 210 ASP A CA  1 
ATOM   1839 C  C   . ASP A 1 207 ? -0.67600  4.78300   50.26000 1.000 17.58839 ? 210 ASP A C   1 
ATOM   1840 O  O   . ASP A 1 207 ? 0.27900   4.02500   50.03500 1.000 17.64629 ? 210 ASP A O   1 
ATOM   1841 C  CB  . ASP A 1 207 ? 0.26500   5.87600   52.33500 1.000 18.03581 ? 210 ASP A CB  1 
ATOM   1842 C  CG  . ASP A 1 207 ? 0.80600   7.08900   51.57100 1.000 19.08330 ? 210 ASP A CG  1 
ATOM   1843 O  OD1 . ASP A 1 207 ? 0.39300   7.31900   50.43500 1.000 20.27818 ? 210 ASP A OD1 1 
ATOM   1844 O  OD2 . ASP A 1 207 ? 1.67500   7.76400   52.15600 1.000 20.69402 ? 210 ASP A OD2 1 
ATOM   1845 N  N   . PRO A 1 208 ? -1.47300  5.21500   49.28300 1.000 20.61243 ? 211 PRO A N   1 
ATOM   1846 C  CA  . PRO A 1 208 ? -1.31100  4.70100   47.91500 1.000 22.09419 ? 211 PRO A CA  1 
ATOM   1847 C  C   . PRO A 1 208 ? 0.02100   5.07700   47.31200 1.000 22.76532 ? 211 PRO A C   1 
ATOM   1848 O  O   . PRO A 1 208 ? 0.41000   4.48600   46.29800 1.000 24.23129 ? 211 PRO A O   1 
ATOM   1849 C  CB  . PRO A 1 208 ? -2.48100  5.34600   47.15800 1.000 23.46541 ? 211 PRO A CB  1 
ATOM   1850 C  CG  . PRO A 1 208 ? -2.78700  6.59600   47.90600 1.000 22.96535 ? 211 PRO A CG  1 
ATOM   1851 C  CD  . PRO A 1 208 ? -2.52600  6.23900   49.36400 1.000 21.99418 ? 211 PRO A CD  1 
ATOM   1852 N  N   . ASN A 1 209 ? 0.73400   6.03900   47.88800 1.000 22.38633 ? 212 ASN A N   1 
ATOM   1853 C  CA  . ASN A 1 209 ? 2.00100   6.49100   47.34400 1.000 24.38657 ? 212 ASN A CA  1 
ATOM   1854 C  C   . ASN A 1 209 ? 3.19200   5.88700   48.06300 1.000 22.98114 ? 212 ASN A C   1 
ATOM   1855 O  O   . ASN A 1 209 ? 4.34000   6.20800   47.74000 1.000 24.81557 ? 212 ASN A O   1 
ATOM   1856 C  CB  . ASN A 1 209 ? 2.04800   8.01900   47.36900 1.000 28.12912 ? 212 ASN A CB  1 
ATOM   1857 C  CG  . ASN A 1 209 ? 0.87300   8.63400   46.61300 1.000 33.15078 ? 212 ASN A CG  1 
ATOM   1858 O  OD1 . ASN A 1 209 ? 0.29200   7.96400   45.76700 1.000 42.25996 ? 212 ASN A OD1 1 
ATOM   1859 N  ND2 . ASN A 1 209 ? 0.50000   9.85900   46.92900 1.000 30.47996 ? 212 ASN A ND2 1 
ATOM   1860 N  N   . GLU A 1 210 ? 2.96400   5.00500   49.01800 1.000 19.85181 ? 213 GLU A N   1 
ATOM   1861 C  CA  . GLU A 1 210 ? 4.04100   4.54400   49.87000 1.000 18.73589 ? 213 GLU A CA  1 
ATOM   1862 C  C   . GLU A 1 210 ? 4.47100   3.14200   49.45800 1.000 18.60693 ? 213 GLU A C   1 
ATOM   1863 O  O   . GLU A 1 210 ? 3.66500   2.21600   49.49600 1.000 19.94656 ? 213 GLU A O   1 
ATOM   1864 C  CB  . GLU A 1 210 ? 3.54700   4.51700   51.31200 1.000 17.87000 ? 213 GLU A CB  1 
ATOM   1865 C  CG  . GLU A 1 210 ? 4.59500   4.02500   52.28700 1.000 16.82514 ? 213 GLU A CG  1 
ATOM   1866 C  CD  . GLU A 1 210 ? 5.86600   4.87000   52.22200 1.000 16.16979 ? 213 GLU A CD  1 
ATOM   1867 O  OE1 . GLU A 1 210 ? 5.79500   6.06500   52.62000 1.000 16.40930 ? 213 GLU A OE1 1 
ATOM   1868 O  OE2 . GLU A 1 210 ? 6.90700   4.34100   51.74100 1.000 16.59353 ? 213 GLU A OE2 1 
ATOM   1869 N  N   . LYS A 1 211 ? 5.74100   2.98900   49.09100 1.000 19.49388 ? 214 LYS A N   1 
ATOM   1870 C  CA  . LYS A 1 211 ? 6.27100   1.69000   48.70900 1.000 19.56494 ? 214 LYS A CA  1 
ATOM   1871 C  C   . LYS A 1 211 ? 6.94200   0.92700   49.84200 1.000 17.86737 ? 214 LYS A C   1 
ATOM   1872 O  O   . LYS A 1 211 ? 7.14000   -0.29100  49.69900 1.000 18.64904 ? 214 LYS A O   1 
ATOM   1873 C  CB  . LYS A 1 211 ? 7.21000   1.85100   47.51400 1.000 22.33632 ? 214 LYS A CB  1 
ATOM   1874 C  CG  . LYS A 1 211 ? 6.42800   2.32300   46.24300 1.000 25.16824 ? 214 LYS A CG  1 
ATOM   1875 C  CD  . LYS A 1 211 ? 7.28500   2.57200   45.04400 1.000 27.77645 ? 214 LYS A CD  1 
ATOM   1876 C  CE  . LYS A 1 211 ? 6.42500   2.96600   43.85400 1.000 30.51996 ? 214 LYS A CE  1 
ATOM   1877 N  NZ  . LYS A 1 211 ? 7.29800   3.56600   42.78900 1.000 32.60996 ? 214 LYS A NZ  1 
ATOM   1878 N  N   . ARG A 1 212 ? 7.22300   1.57500   50.97000 1.000 16.58827 ? 215 ARG A N   1 
ATOM   1879 C  CA  . ARG A 1 212 ? 7.74700   0.83900   52.09200 1.000 15.05124 ? 215 ARG A CA  1 
ATOM   1880 C  C   . ARG A 1 212 ? 6.59500   0.13100   52.79300 1.000 14.01164 ? 215 ARG A C   1 
ATOM   1881 O  O   . ARG A 1 212 ? 5.42700   0.44200   52.61000 1.000 13.79846 ? 215 ARG A O   1 
ATOM   1882 C  CB  . ARG A 1 212 ? 8.43500   1.80900   53.07600 1.000 15.11177 ? 215 ARG A CB  1 
ATOM   1883 C  CG  . ARG A 1 212 ? 9.74400   2.42000   52.52500 1.000 16.76197 ? 215 ARG A CG  1 
ATOM   1884 C  CD  . ARG A 1 212 ? 10.19000  3.61100   53.35900 1.000 17.03306 ? 215 ARG A CD  1 
ATOM   1885 N  NE  . ARG A 1 212 ? 9.25100   4.70800   53.20000 1.000 16.68828 ? 215 ARG A NE  1 
ATOM   1886 C  CZ  . ARG A 1 212 ? 9.38200   5.91100   53.76700 1.000 16.93304 ? 215 ARG A CZ  1 
ATOM   1887 N  NH1 . ARG A 1 212 ? 10.40200  6.19900   54.56900 1.000 17.56470 ? 215 ARG A NH1 1 
ATOM   1888 N  NH2 . ARG A 1 212 ? 8.44300   6.83400   53.55800 1.000 17.40942 ? 215 ARG A NH2 1 
ATOM   1889 N  N   . ASP A 1 213 ? 6.93100   -0.87700  53.57600 1.000 12.75886 ? 216 ASP A N   1 
ATOM   1890 C  CA  . ASP A 1 213 ? 5.90100   -1.56400  54.36000 1.000 11.79822 ? 216 ASP A CA  1 
ATOM   1891 C  C   . ASP A 1 213 ? 5.43000   -0.58200  55.45300 1.000 10.88758 ? 216 ASP A C   1 
ATOM   1892 O  O   . ASP A 1 213 ? 6.25600   0.02900   56.14300 1.000 11.36132 ? 216 ASP A O   1 
ATOM   1893 C  CB  . ASP A 1 213 ? 6.51600   -2.83100  54.95100 1.000 10.81389 ? 216 ASP A CB  1 
ATOM   1894 C  CG  . ASP A 1 213 ? 5.47500   -3.79300  55.49800 1.000 11.12445 ? 216 ASP A CG  1 
ATOM   1895 O  OD1 . ASP A 1 213 ? 4.26500   -3.61500  55.28700 1.000 11.44818 ? 216 ASP A OD1 1 
ATOM   1896 O  OD2 . ASP A 1 213 ? 5.90600   -4.79000  56.11100 1.000 12.92467 ? 216 ASP A OD2 1 
ATOM   1897 N  N   . HIS A 1 214 ? 4.10400   -0.43800  55.58800 1.000 10.86916 ? 217 HIS A N   1 
ATOM   1898 C  CA  . HIS A 1 214 ? 3.57500   0.65700   56.39200 1.000 10.16644 ? 217 HIS A CA  1 
ATOM   1899 C  C   . HIS A 1 214 ? 2.13600   0.38300   56.78100 1.000 9.91115  ? 217 HIS A C   1 
ATOM   1900 O  O   . HIS A 1 214 ? 1.51300   -0.55300  56.28900 1.000 10.53228 ? 217 HIS A O   1 
ATOM   1901 C  CB  . HIS A 1 214 ? 3.67800   1.99400   55.58800 1.000 11.14814 ? 217 HIS A CB  1 
ATOM   1902 C  CG  . HIS A 1 214 ? 2.67000   2.08100   54.48200 1.000 11.73768 ? 217 HIS A CG  1 
ATOM   1903 N  ND1 . HIS A 1 214 ? 2.80900   1.38500   53.28600 1.000 12.77991 ? 217 HIS A ND1 1 
ATOM   1904 C  CD2 . HIS A 1 214 ? 1.47000   2.69300   54.41500 1.000 12.25617 ? 217 HIS A CD2 1 
ATOM   1905 C  CE1 . HIS A 1 214 ? 1.74000   1.59700   52.54000 1.000 13.39315 ? 217 HIS A CE1 1 
ATOM   1906 N  NE2 . HIS A 1 214 ? 0.90900   2.38300   53.19600 1.000 12.66674 ? 217 HIS A NE2 1 
ATOM   1907 N  N   . MET A 1 215 ? 1.62700   1.21100   57.69400 1.000 9.30844  ? 218 MET A N   1 
ATOM   1908 C  CA  . MET A 1 215 ? 0.22700   1.15100   58.09800 1.000 10.02169 ? 218 MET A CA  1 
ATOM   1909 C  C   . MET A 1 215 ? -0.28200  2.56500   58.35200 1.000 10.19803 ? 218 MET A C   1 
ATOM   1910 O  O   . MET A 1 215 ? 0.37500   3.32700   59.08300 1.000 9.76113  ? 218 MET A O   1 
ATOM   1911 C  CB  . MET A 1 215 ? 0.08200   0.33100   59.41100 1.000 9.86641  ? 218 MET A CB  1 
ATOM   1912 C  CG  . MET A 1 215 ? -1.27400  0.45100   60.04800 1.000 10.19276 ? 218 MET A CG  1 
ATOM   1913 S  SD  . MET A 1 215 ? -1.56800  -0.69700  61.40600 1.000 9.80061  ? 218 MET A SD  1 
ATOM   1914 C  CE  . MET A 1 215 ? -0.44600  -0.01600  62.67200 1.000 10.16644 ? 218 MET A CE  1 
ATOM   1915 N  N   . VAL A 1 216 ? -1.46300  2.89200   57.81100 1.000 10.15855 ? 219 VAL A N   1 
ATOM   1916 C  CA  . VAL A 1 216 ? -2.18300  4.12200   58.18000 1.000 10.09275 ? 219 VAL A CA  1 
ATOM   1917 C  C   . VAL A 1 216 ? -3.29100  3.74600   59.13600 1.000 10.11644 ? 219 VAL A C   1 
ATOM   1918 O  O   . VAL A 1 216 ? -4.02700  2.76700   58.89800 1.000 10.49806 ? 219 VAL A O   1 
ATOM   1919 C  CB  . VAL A 1 216 ? -2.71700  4.83500   56.91800 1.000 11.50608 ? 219 VAL A CB  1 
ATOM   1920 C  CG1 . VAL A 1 216 ? -3.52900  6.07000   57.31700 1.000 12.16405 ? 219 VAL A CG1 1 
ATOM   1921 C  CG2 . VAL A 1 216 ? -1.55800  5.18700   55.97400 1.000 12.28249 ? 219 VAL A CG2 1 
ATOM   1922 N  N   . LEU A 1 217 ? -3.36800  4.48200   60.24200 1.000 10.03485 ? 220 LEU A N   1 
ATOM   1923 C  CA  . LEU A 1 217 ? -4.33000  4.23500   61.30800 1.000 10.53228 ? 220 LEU A CA  1 
ATOM   1924 C  C   . LEU A 1 217 ? -5.16500  5.48100   61.55200 1.000 10.47964 ? 220 LEU A C   1 
ATOM   1925 O  O   . LEU A 1 217 ? -4.61000  6.57600   61.74500 1.000 12.23511 ? 220 LEU A O   1 
ATOM   1926 C  CB  . LEU A 1 217 ? -3.58800  3.89200   62.59600 1.000 11.54029 ? 220 LEU A CB  1 
ATOM   1927 C  CG  . LEU A 1 217 ? -4.39100  3.82400   63.89500 1.000 11.69821 ? 220 LEU A CG  1 
ATOM   1928 C  CD1 . LEU A 1 217 ? -5.42300  2.62800   63.84800 1.000 11.50081 ? 220 LEU A CD1 1 
ATOM   1929 C  CD2 . LEU A 1 217 ? -3.45400  3.63100   65.07000 1.000 12.81413 ? 220 LEU A CD2 1 
ATOM   1930 N  N   . LEU A 1 218 ? -6.49300  5.31500   61.56200 1.000 10.42963 ? 221 LEU A N   1 
ATOM   1931 C  CA  . LEU A 1 218 ? -7.42300  6.34500   62.01500 1.000 11.15077 ? 221 LEU A CA  1 
ATOM   1932 C  C   . LEU A 1 218 ? -8.16800  5.77400   63.20200 1.000 11.23236 ? 221 LEU A C   1 
ATOM   1933 O  O   . LEU A 1 218 ? -8.74500  4.69700   63.10400 1.000 12.31670 ? 221 LEU A O   1 
ATOM   1934 C  CB  . LEU A 1 218 ? -8.44200  6.69300   60.92600 1.000 12.84834 ? 221 LEU A CB  1 
ATOM   1935 C  CG  . LEU A 1 218 ? -9.60900  7.62200   61.32000 1.000 17.55943 ? 221 LEU A CG  1 
ATOM   1936 C  CD1 . LEU A 1 218 ? -9.16000  9.05300   61.74000 1.000 19.27806 ? 221 LEU A CD1 1 
ATOM   1937 C  CD2 . LEU A 1 218 ? -10.65500 7.70300   60.19300 1.000 19.47282 ? 221 LEU A CD2 1 
ATOM   1938 N  N   . GLN A 1 219 ? -8.10500  6.46000   64.33200 1.000 11.10340 ? 222 GLN A N   1 
ATOM   1939 C  CA  . GLN A 1 219 ? -8.66100  5.88200   65.54200 1.000 11.74558 ? 222 GLN A CA  1 
ATOM   1940 C  C   . GLN A 1 219 ? -9.44500  6.94700   66.30300 1.000 12.61937 ? 222 GLN A C   1 
ATOM   1941 O  O   . GLN A 1 219 ? -9.05100  8.12700   66.33700 1.000 13.78267 ? 222 GLN A O   1 
ATOM   1942 C  CB  . GLN A 1 219 ? -7.51400  5.31400   66.40800 1.000 13.00626 ? 222 GLN A CB  1 
ATOM   1943 C  CG  . GLN A 1 219 ? -7.87900  4.62500   67.71400 1.000 13.32472 ? 222 GLN A CG  1 
ATOM   1944 C  CD  . GLN A 1 219 ? -6.71500  3.81500   68.24900 1.000 14.10112 ? 222 GLN A CD  1 
ATOM   1945 O  OE1 . GLN A 1 219 ? -6.42000  2.70300   67.75800 1.000 14.10639 ? 222 GLN A OE1 1 
ATOM   1946 N  NE2 . GLN A 1 219 ? -6.02300  4.35600   69.24700 1.000 16.23296 ? 222 GLN A NE2 1 
ATOM   1947 N  N   . PHE A 1 220 ? -10.57800 6.53100   66.88600 1.000 11.69557 ? 223 PHE A N   1 
ATOM   1948 C  CA  . PHE A 1 220 ? -11.40800 7.35800   67.77600 1.000 12.53515 ? 223 PHE A CA  1 
ATOM   1949 C  C   . PHE A 1 220 ? -11.48800 6.64700   69.11300 1.000 14.59329 ? 223 PHE A C   1 
ATOM   1950 O  O   . PHE A 1 220 ? -11.72600 5.43000   69.17100 1.000 16.41982 ? 223 PHE A O   1 
ATOM   1951 C  CB  . PHE A 1 220 ? -12.83200 7.57600   67.22800 1.000 14.27220 ? 223 PHE A CB  1 
ATOM   1952 C  CG  . PHE A 1 220 ? -12.83700 8.43100   66.01500 1.000 15.16967 ? 223 PHE A CG  1 
ATOM   1953 C  CD1 . PHE A 1 220 ? -12.74400 9.82400   66.15100 1.000 15.91713 ? 223 PHE A CD1 1 
ATOM   1954 C  CD2 . PHE A 1 220 ? -12.79600 7.88500   64.75200 1.000 16.53826 ? 223 PHE A CD2 1 
ATOM   1955 C  CE1 . PHE A 1 220 ? -12.68300 10.64700  65.07200 1.000 16.89356 ? 223 PHE A CE1 1 
ATOM   1956 C  CE2 . PHE A 1 220 ? -12.73800 8.70800   63.61600 1.000 16.98305 ? 223 PHE A CE2 1 
ATOM   1957 C  CZ  . PHE A 1 220 ? -12.67700 10.11100  63.80000 1.000 17.31467 ? 223 PHE A CZ  1 
ATOM   1958 N  N   . VAL A 1 221 ? -11.26900 7.39900   70.18300 1.000 13.85899 ? 224 VAL A N   1 
ATOM   1959 C  CA  . VAL A 1 221 ? -11.26500 6.85300   71.53500 1.000 15.07229 ? 224 VAL A CA  1 
ATOM   1960 C  C   . VAL A 1 221 ? -12.06200 7.79500   72.41400 1.000 14.98018 ? 224 VAL A C   1 
ATOM   1961 O  O   . VAL A 1 221 ? -11.75800 8.99400   72.47000 1.000 14.21430 ? 224 VAL A O   1 
ATOM   1962 C  CB  . VAL A 1 221 ? -9.84300  6.77400   72.07900 1.000 16.07241 ? 224 VAL A CB  1 
ATOM   1963 C  CG1 . VAL A 1 221 ? -9.87800  6.15400   73.47000 1.000 17.07253 ? 224 VAL A CG1 1 
ATOM   1964 C  CG2 . VAL A 1 221 ? -8.97900  5.97900   71.14000 1.000 17.05411 ? 224 VAL A CG2 1 
ATOM   1965 N  N   . THR A 1 222 ? -13.08300 7.25400   73.09000 1.000 14.13534 ? 225 THR A N   1 
ATOM   1966 C  CA  . THR A 1 222 ? -13.96000 8.04100   73.93300 1.000 13.80372 ? 225 THR A CA  1 
ATOM   1967 C  C   . THR A 1 222 ? -14.06900 7.37400   75.29700 1.000 11.67189 ? 225 THR A C   1 
ATOM   1968 O  O   . THR A 1 222 ? -14.38500 6.18100   75.39400 1.000 13.10100 ? 225 THR A O   1 
ATOM   1969 C  CB  . THR A 1 222 ? -15.32200 8.04900   73.28700 1.000 16.94094 ? 225 THR A CB  1 
ATOM   1970 O  OG1 . THR A 1 222 ? -15.17600 8.44200   71.92300 1.000 18.68852 ? 225 THR A OG1 1 
ATOM   1971 C  CG2 . THR A 1 222 ? -16.20300 8.98500   74.03700 1.000 17.37783 ? 225 THR A CG2 1 
ATOM   1972 N  N   . ALA A 1 223 ? -13.79600 8.13900   76.36300 1.000 11.15603 ? 226 ALA A N   1 
ATOM   1973 C  CA  . ALA A 1 223 ? -13.97000 7.59700   77.71500 1.000 10.66913 ? 226 ALA A CA  1 
ATOM   1974 C  C   . ALA A 1 223 ? -15.45000 7.57800   78.06000 1.000 11.16919 ? 226 ALA A C   1 
ATOM   1975 O  O   . ALA A 1 223 ? -16.20600 8.45000   77.64000 1.000 11.43238 ? 226 ALA A O   1 
ATOM   1976 C  CB  . ALA A 1 223 ? -13.24400 8.47900   78.72800 1.000 11.05865 ? 226 ALA A CB  1 
ATOM   1977 N  N   A ALA A 1 224 ? -15.83300 6.58400   78.84900 0.660 12.54304 ? 227 ALA A N   1 
ATOM   1978 N  N   B ALA A 1 224 ? -15.86400 6.59100   78.88200 0.340 11.12996 ? 227 ALA A N   1 
ATOM   1979 C  CA  A ALA A 1 224 ? -17.21500 6.39400   79.21600 0.660 13.40367 ? 227 ALA A CA  1 
ATOM   1980 C  CA  B ALA A 1 224 ? -17.23900 6.45600   79.37700 0.340 11.99996 ? 227 ALA A CA  1 
ATOM   1981 C  C   A ALA A 1 224 ? -17.25000 5.61500   80.51100 0.660 12.85624 ? 227 ALA A C   1 
ATOM   1982 C  C   B ALA A 1 224 ? -17.24300 6.07300   80.85100 0.340 11.65996 ? 227 ALA A C   1 
ATOM   1983 O  O   A ALA A 1 224 ? -16.23200 5.11800   81.00500 0.660 12.74044 ? 227 ALA A O   1 
ATOM   1984 O  O   B ALA A 1 224 ? -16.59200 5.09800   81.23500 0.340 15.62996 ? 227 ALA A O   1 
ATOM   1985 C  CB  A ALA A 1 224 ? -17.96400 5.68100   78.09600 0.660 14.73015 ? 227 ALA A CB  1 
ATOM   1986 C  CB  B ALA A 1 224 ? -18.02400 5.40000   78.58300 0.340 19.12996 ? 227 ALA A CB  1 
ATOM   1987 N  N   A GLY A 1 225 ? -18.43700 5.56000   81.07700 0.660 15.45918 ? 228 GLY A N   1 
ATOM   1988 N  N   B GLY A 1 225 ? -18.00400 6.81200   81.66200 0.340 9.69996  ? 228 GLY A N   1 
ATOM   1989 C  CA  A GLY A 1 225 ? -18.64300 4.71400   82.22500 0.660 17.38573 ? 228 GLY A CA  1 
ATOM   1990 C  CA  B GLY A 1 225 ? -18.07500 6.54200   83.09100 0.340 17.96996 ? 228 GLY A CA  1 
ATOM   1991 C  C   A GLY A 1 225 ? -18.73100 5.42600   83.53600 0.660 19.41755 ? 228 GLY A C   1 
ATOM   1992 C  C   B GLY A 1 225 ? -19.46900 6.27100   83.62200 0.340 23.60996 ? 228 GLY A C   1 
ATOM   1993 O  O   A GLY A 1 225 ? -18.99100 4.76800   84.55000 0.660 20.48084 ? 228 GLY A O   1 
ATOM   1994 O  O   B GLY A 1 225 ? -20.42600 6.15700   82.85400 0.340 25.30996 ? 228 GLY A O   1 
ATOM   1995 N  N   A ILE A 1 226 ? -18.55800 6.74000   83.55500 0.660 19.00171 ? 229 ILE A N   1 
ATOM   1996 N  N   B ILE A 1 226 ? -19.58200 6.13200   84.94100 0.340 10.28996 ? 229 ILE A N   1 
ATOM   1997 C  CA  A ILE A 1 226 ? -18.74600 7.52100   84.76800 0.660 19.68337 ? 229 ILE A CA  1 
ATOM   1998 C  CA  B ILE A 1 226 ? -20.86300 6.01500   85.63500 0.340 10.45996 ? 229 ILE A CA  1 
ATOM   1999 C  C   A ILE A 1 226 ? -19.74000 8.61900   84.43300 0.660 24.11548 ? 229 ILE A C   1 
ATOM   2000 C  C   B ILE A 1 226 ? -21.15800 7.28700   86.43000 0.340 12.54996 ? 229 ILE A C   1 
ATOM   2001 O  O   A ILE A 1 226 ? -19.50900 9.38600   83.49700 0.660 25.36037 ? 229 ILE A O   1 
ATOM   2002 O  O   B ILE A 1 226 ? -20.26700 7.88000   87.05600 0.340 12.02996 ? 229 ILE A O   1 
ATOM   2003 C  CB  A ILE A 1 226 ? -17.42100 8.14700   85.20600 0.660 17.44363 ? 229 ILE A CB  1 
ATOM   2004 C  CB  B ILE A 1 226 ? -20.85000 4.78300   86.56000 0.340 19.55996 ? 229 ILE A CB  1 
ATOM   2005 C  CG1 A ILE A 1 226 ? -16.48300 7.07600   85.76800 0.660 17.29361 ? 229 ILE A CG1 1 
ATOM   2006 C  CG2 A ILE A 1 226 ? -17.71500 9.28000   86.12300 0.660 16.98305 ? 229 ILE A CG2 1 
ATOM   2007 C  CD1 A ILE A 1 226 ? -15.19900 7.63100   85.98300 0.660 15.90397 ? 229 ILE A CD1 1 
ATOM   2008 N  N   A THR A 1 227 ? -20.84000 8.70500   85.19300 0.660 28.06069 ? 230 THR A N   1 
ATOM   2009 N  N   B THR A 1 227 ? -22.43700 7.69100   86.39400 0.340 18.19996 ? 230 THR A N   1 
ATOM   2010 C  CA  A THR A 1 227 ? -21.90000 9.66700   84.87700 0.660 32.13996 ? 230 THR A CA  1 
ATOM   2011 C  CA  B THR A 1 227 ? -23.03400 8.81700   87.11100 0.340 35.31996 ? 230 THR A CA  1 
ATOM   2012 C  C   A THR A 1 227 ? -22.64700 10.14800  86.12100 0.660 38.77996 ? 230 THR A C   1 
ATOM   2013 C  C   B THR A 1 227 ? -22.81000 10.12100  86.35600 0.340 34.68996 ? 230 THR A C   1 
ATOM   2014 O  O   A THR A 1 227 ? -23.05900 11.31100  86.19700 0.660 48.22996 ? 230 THR A O   1 
ATOM   2015 O  O   B THR A 1 227 ? -23.39500 10.31400  85.28300 0.340 40.65996 ? 230 THR A O   1 
ATOM   2016 C  CB  A THR A 1 227 ? -22.94400 9.03500   83.94200 0.660 33.09996 ? 230 THR A CB  1 
ATOM   2017 C  CB  B THR A 1 227 ? -22.63800 8.86700   88.59400 0.340 34.48996 ? 230 THR A CB  1 
ATOM   2018 O  OG1 A THR A 1 227 ? -23.37600 7.78300   84.48800 0.660 37.52996 ? 230 THR A OG1 1 
ATOM   2019 C  CG2 A THR A 1 227 ? -22.39800 8.80200   82.53800 0.660 32.07696 ? 230 THR A CG2 1 
ATOM   2020 N  N   A HIS A 1 228 ? -22.82400 9.25200   87.08900 0.660 33.43502 ? 231 HIS A N   1 
ATOM   2021 N  N   B HIS A 1 228 ? -21.95100 10.99900  86.86200 0.340 41.21996 ? 231 HIS A N   1 
ATOM   2022 C  CA  A HIS A 1 228 ? -23.89000 9.35100   88.08500 0.660 30.44782 ? 231 HIS A CA  1 
ATOM   2023 C  CA  B HIS A 1 228 ? -21.73900 12.28300  86.19500 0.340 33.97996 ? 231 HIS A CA  1 
ATOM   2024 C  C   A HIS A 1 228 ? -23.36700 9.65900   89.46300 0.660 31.36898 ? 231 HIS A C   1 
ATOM   2025 C  C   B HIS A 1 228 ? -20.47900 12.98000  86.67200 0.340 23.77996 ? 231 HIS A C   1 
ATOM   2026 O  O   A HIS A 1 228 ? -23.06300 10.80600  89.86600 0.660 32.47996 ? 231 HIS A O   1 
ATOM   2027 O  O   B HIS A 1 228 ? -20.55500 14.14800  87.05600 0.340 23.17996 ? 231 HIS A O   1 
ATOM   2028 C  CB  A HIS A 1 228 ? -24.66300 8.02700   88.12200 0.660 27.63696 ? 231 HIS A CB  1 
ATOM   2029 C  CB  B HIS A 1 228 ? -22.94100 13.20200  86.42900 0.340 30.84996 ? 231 HIS A CB  1 
ATOM   2030 O  OXT A HIS A 1 228 ? -23.22200 8.71500   90.21400 0.660 32.42996 ? 231 HIS A OXT 1 
ATOM   2031 O  OXT B HIS A 1 228 ? -19.39300 12.41600  86.69700 0.340 22.15996 ? 231 HIS A OXT 1 
HETATM 2032 CL CL  . CL  B 2 .   ? -14.07900 -5.51400  74.01700 1.000 14.19587 ? 301 CL  A CL  1 
HETATM 2033 CL CL  . CL  C 2 .   ? -0.09500  -6.85500  58.16900 1.000 16.64353 ? 302 CL  A CL  1 
HETATM 2034 O  O   A HOH D 3 .   ? -7.07700  3.18100   74.17400 0.640 16.15663 ? 401 HOH A O   1 
HETATM 2035 O  O   B HOH D 3 .   ? -6.58900  3.64400   73.26400 0.360 11.94996 ? 401 HOH A O   1 
HETATM 2036 O  O   A HOH D 3 .   ? -6.09000  4.64100   72.22000 0.570 22.94429 ? 402 HOH A O   1 
HETATM 2037 O  O   B HOH D 3 .   ? -6.85500  6.36200   73.51500 0.430 26.52996 ? 402 HOH A O   1 
HETATM 2038 O  O   . HOH D 3 .   ? -10.19400 -0.51100  68.09000 1.000 11.63767 ? 403 HOH A O   1 
HETATM 2039 O  O   A HOH D 3 .   ? -6.40500  7.53300   72.72700 0.680 18.87538 ? 404 HOH A O   1 
HETATM 2040 O  O   B HOH D 3 .   ? -6.10200  7.06600   70.87600 0.320 12.15996 ? 404 HOH A O   1 
HETATM 2041 O  O   . HOH D 3 .   ? -3.04500  -4.35500  68.43800 1.000 9.38740  ? 405 HOH A O   1 
HETATM 2042 O  O   A HOH D 3 .   ? -3.63000  5.84400   71.53700 0.320 6.96996  ? 406 HOH A O   1 
HETATM 2043 O  O   B HOH D 3 .   ? -4.24800  5.67300   71.82400 0.680 6.60812  ? 406 HOH A O   1 
HETATM 2044 O  O   . HOH D 3 .   ? -8.94000  -6.10100  66.06100 1.000 13.06942 ? 407 HOH A O   1 
HETATM 2045 O  O   . HOH D 3 .   ? -2.48200  -6.79500  69.65600 1.000 9.30055  ? 408 HOH A O   1 
HETATM 2046 O  O   . HOH D 3 .   ? -11.69500 -5.66600  76.09200 1.000 12.75886 ? 409 HOH A O   1 
HETATM 2047 O  O   . HOH D 3 .   ? -12.72800 -0.57300  64.95700 1.000 16.46193 ? 410 HOH A O   1 
HETATM 2048 O  O   . HOH D 3 .   ? 0.18600   -3.79600  70.02100 1.000 9.11632  ? 411 HOH A O   1 
HETATM 2049 O  O   . HOH D 3 .   ? 1.47200   -2.47100  74.22300 1.000 10.25330 ? 412 HOH A O   1 
HETATM 2050 O  O   . HOH D 3 .   ? -0.77200  5.70400   76.21100 1.000 10.95075 ? 413 HOH A O   1 
HETATM 2051 O  O   . HOH D 3 .   ? -7.63200  9.20100   70.41700 1.000 21.06512 ? 414 HOH A O   1 
HETATM 2052 O  O   . HOH D 3 .   ? 2.35200   1.24400   74.45700 1.000 10.99812 ? 415 HOH A O   1 
HETATM 2053 O  O   . HOH D 3 .   ? -16.64200 -1.93700  71.36700 1.000 29.62667 ? 416 HOH A O   1 
HETATM 2054 O  O   . HOH D 3 .   ? -14.89200 5.99900   70.53500 1.000 25.70778 ? 417 HOH A O   1 
HETATM 2055 O  O   . HOH D 3 .   ? -6.95800  -7.12300  63.89400 1.000 10.15328 ? 418 HOH A O   1 
HETATM 2056 O  O   . HOH D 3 .   ? 2.75100   3.83900   74.90000 1.000 10.35068 ? 419 HOH A O   1 
HETATM 2057 O  O   A HOH D 3 .   ? -13.05900 1.85800   62.91400 0.500 18.94381 ? 420 HOH A O   1 
HETATM 2058 O  O   B HOH D 3 .   ? -13.52300 3.26500   62.48000 0.500 25.50996 ? 420 HOH A O   1 
HETATM 2059 O  O   . HOH D 3 .   ? -17.62100 0.51200   73.17100 1.000 31.17996 ? 421 HOH A O   1 
HETATM 2060 O  O   . HOH D 3 .   ? -11.78100 4.72400   62.98200 1.000 28.41337 ? 422 HOH A O   1 
HETATM 2061 O  O   . HOH D 3 .   ? -16.08500 -5.78100  68.24600 1.000 26.01045 ? 423 HOH A O   1 
HETATM 2062 O  O   . HOH D 3 .   ? -11.80300 -7.39500  78.35800 1.000 16.34087 ? 424 HOH A O   1 
HETATM 2063 O  O   . HOH D 3 .   ? -15.84300 -4.32200  65.76400 1.000 26.30785 ? 425 HOH A O   1 
HETATM 2064 O  O   A HOH D 3 .   ? 3.72600   -0.33000  76.32100 0.800 9.22422  ? 426 HOH A O   1 
HETATM 2065 O  O   B HOH D 3 .   ? 2.89100   -0.06600  75.80400 0.200 7.30996  ? 426 HOH A O   1 
HETATM 2066 O  O   . HOH D 3 .   ? -11.98200 -1.06500  61.08700 1.000 24.54185 ? 427 HOH A O   1 
HETATM 2067 O  O   . HOH D 3 .   ? -9.80200  -8.03000  63.26600 1.000 11.91139 ? 428 HOH A O   1 
HETATM 2068 O  O   . HOH D 3 .   ? -15.78900 -6.08300  76.64100 1.000 18.92012 ? 429 HOH A O   1 
HETATM 2069 O  O   . HOH D 3 .   ? -7.17500  -8.32600  80.12800 1.000 29.27136 ? 430 HOH A O   1 
HETATM 2070 O  O   . HOH D 3 .   ? -9.90200  -7.80700  80.20400 1.000 21.32304 ? 431 HOH A O   1 
HETATM 2071 O  O   . HOH D 3 .   ? -17.68100 5.78100   71.74600 1.000 37.82996 ? 432 HOH A O   1 
HETATM 2072 O  O   A HOH D 3 .   ? -11.47100 -2.94500  60.34500 0.490 14.69996 ? 433 HOH A O   1 
HETATM 2073 O  O   B HOH D 3 .   ? -12.21600 -4.06400  60.73300 0.510 16.73565 ? 433 HOH A O   1 
HETATM 2074 O  O   . HOH D 3 .   ? -9.44100  -1.61000  59.35600 1.000 15.74080 ? 434 HOH A O   1 
HETATM 2075 O  O   . HOH D 3 .   ? -18.14800 -2.53000  66.11600 1.000 38.20996 ? 435 HOH A O   1 
HETATM 2076 O  O   . HOH D 3 .   ? -6.68400  11.11100  77.91700 1.000 9.77955  ? 436 HOH A O   1 
HETATM 2077 O  O   A HOH D 3 .   ? -15.91400 5.15400   64.17800 0.670 27.17638 ? 437 HOH A O   1 
HETATM 2078 O  O   . HOH D 3 .   ? -6.44900  -9.29600  62.31100 1.000 11.40080 ? 438 HOH A O   1 
HETATM 2079 O  O   A HOH D 3 .   ? -15.79100 -4.44200  62.70200 0.470 31.28996 ? 439 HOH A O   1 
HETATM 2080 O  O   B HOH D 3 .   ? -14.82200 -2.98600  62.71600 0.530 31.30996 ? 439 HOH A O   1 
HETATM 2081 O  O   . HOH D 3 .   ? -19.00300 -4.34800  74.24100 1.000 28.91080 ? 440 HOH A O   1 
HETATM 2082 O  O   . HOH D 3 .   ? -18.49100 5.54600   74.59400 1.000 44.03996 ? 441 HOH A O   1 
HETATM 2083 O  O   A HOH D 3 .   ? -5.00000  -8.79000  81.28300 0.690 19.19910 ? 442 HOH A O   1 
HETATM 2084 O  O   B HOH D 3 .   ? -4.59700  -9.46600  81.91400 0.310 10.96996 ? 442 HOH A O   1 
HETATM 2085 O  O   . HOH D 3 .   ? -19.59000 2.81800   74.96400 1.000 36.98996 ? 443 HOH A O   1 
HETATM 2086 O  O   . HOH D 3 .   ? -19.84900 -1.47600  75.29700 1.000 36.00996 ? 444 HOH A O   1 
HETATM 2087 O  O   A HOH D 3 .   ? -14.93200 10.94700  70.74400 0.470 16.30996 ? 445 HOH A O   1 
HETATM 2088 O  O   B HOH D 3 .   ? -16.12200 10.87200  70.96000 0.530 22.43897 ? 445 HOH A O   1 
HETATM 2089 O  O   . HOH D 3 .   ? -18.51600 -5.40800  76.35700 1.000 33.07996 ? 446 HOH A O   1 
HETATM 2090 O  O   . HOH D 3 .   ? -1.57500  -10.42500 78.70900 1.000 10.56649 ? 447 HOH A O   1 
HETATM 2091 O  O   . HOH D 3 .   ? -7.67900  7.92200   83.18600 1.000 12.32723 ? 448 HOH A O   1 
HETATM 2092 O  O   . HOH D 3 .   ? -16.99400 -7.13900  64.53900 1.000 39.37996 ? 449 HOH A O   1 
HETATM 2093 O  O   . HOH D 3 .   ? -7.13400  4.29000   58.05400 1.000 17.34099 ? 450 HOH A O   1 
HETATM 2094 O  O   . HOH D 3 .   ? -5.24100  -4.57100  84.86400 1.000 26.87108 ? 451 HOH A O   1 
HETATM 2095 O  O   . HOH D 3 .   ? -18.75400 -1.47700  79.30600 1.000 46.18996 ? 452 HOH A O   1 
HETATM 2096 O  O   . HOH D 3 .   ? -14.71600 -7.19000  81.12600 1.000 39.60996 ? 453 HOH A O   1 
HETATM 2097 O  O   . HOH D 3 .   ? -11.97600 -0.01700  57.91800 1.000 34.65996 ? 454 HOH A O   1 
HETATM 2098 O  O   A HOH D 3 .   ? -7.18200  -3.33600  85.56600 0.600 29.83996 ? 455 HOH A O   1 
HETATM 2099 O  O   B HOH D 3 .   ? -8.65800  -2.91100  85.00900 0.400 33.46996 ? 455 HOH A O   1 
HETATM 2100 O  O   . HOH D 3 .   ? -9.47400  -9.60200  82.06000 1.000 28.73709 ? 456 HOH A O   1 
HETATM 2101 O  O   . HOH D 3 .   ? -12.72200 -0.60700  84.81400 1.000 19.91235 ? 457 HOH A O   1 
HETATM 2102 O  O   . HOH D 3 .   ? -5.27400  -14.19000 74.73900 1.000 13.27471 ? 458 HOH A O   1 
HETATM 2103 O  O   . HOH D 3 .   ? -12.58600 -5.68900  83.68500 1.000 48.07996 ? 459 HOH A O   1 
HETATM 2104 O  O   A HOH D 3 .   ? -15.26200 0.12200   83.50200 0.450 18.23320 ? 460 HOH A O   1 
HETATM 2105 O  O   B HOH D 3 .   ? -15.03500 -0.76600  84.73600 0.550 32.28996 ? 460 HOH A O   1 
HETATM 2106 O  O   . HOH D 3 .   ? 2.50300   -4.58900  82.24500 1.000 19.39650 ? 461 HOH A O   1 
HETATM 2107 O  O   . HOH D 3 .   ? -9.08000  -2.75400  56.94800 1.000 19.62810 ? 462 HOH A O   1 
HETATM 2108 O  O   . HOH D 3 .   ? -9.92600  1.31200   56.68100 1.000 27.28955 ? 463 HOH A O   1 
HETATM 2109 O  O   . HOH D 3 .   ? -11.71000 -3.30200  85.39300 1.000 37.95996 ? 464 HOH A O   1 
HETATM 2110 O  O   . HOH D 3 .   ? -6.09600  13.25100  64.00500 1.000 17.20150 ? 465 HOH A O   1 
HETATM 2111 O  O   . HOH D 3 .   ? -12.37500 4.44800   57.78800 1.000 36.28996 ? 466 HOH A O   1 
HETATM 2112 O  O   A HOH D 3 .   ? -18.37800 10.17600  71.52400 0.550 24.88136 ? 467 HOH A O   1 
HETATM 2113 O  O   B HOH D 3 .   ? -19.56500 8.01900   71.65700 0.450 24.10996 ? 467 HOH A O   1 
HETATM 2114 O  O   . HOH D 3 .   ? -9.75000  3.92300   56.82200 1.000 28.76867 ? 468 HOH A O   1 
HETATM 2115 O  O   . HOH D 3 .   ? -19.97000 7.24900   75.46300 1.000 26.24205 ? 469 HOH A O   1 
HETATM 2116 O  O   A HOH D 3 .   ? -2.71100  -7.97500  58.63300 0.700 18.72273 ? 470 HOH A O   1 
HETATM 2117 O  O   B HOH D 3 .   ? -2.29300  -8.47500  57.48400 0.300 11.87996 ? 470 HOH A O   1 
HETATM 2118 O  O   . HOH D 3 .   ? -18.44000 -1.70200  82.04100 1.000 49.03996 ? 471 HOH A O   1 
HETATM 2119 O  O   A HOH D 3 .   ? -10.28100 14.86300  76.05900 0.580 10.71651 ? 472 HOH A O   1 
HETATM 2120 O  O   B HOH D 3 .   ? -10.22700 14.75100  77.27200 0.420 16.06996 ? 472 HOH A O   1 
HETATM 2121 O  O   . HOH D 3 .   ? -16.34400 -2.93700  83.78300 1.000 41.94996 ? 473 HOH A O   1 
HETATM 2122 O  O   . HOH D 3 .   ? 4.52600   -6.16400  81.06900 1.000 20.37030 ? 474 HOH A O   1 
HETATM 2123 O  O   . HOH D 3 .   ? -18.86100 9.03000   77.34700 1.000 18.39638 ? 475 HOH A O   1 
HETATM 2124 O  O   . HOH D 3 .   ? 6.57600   -4.70800  79.88700 1.000 16.42509 ? 476 HOH A O   1 
HETATM 2125 O  O   . HOH D 3 .   ? -20.58200 9.14300   73.42100 1.000 36.40996 ? 477 HOH A O   1 
HETATM 2126 O  O   . HOH D 3 .   ? -21.28400 2.98300   79.37300 1.000 41.21996 ? 478 HOH A O   1 
HETATM 2127 O  O   . HOH D 3 .   ? -8.76300  -4.99700  87.45200 1.000 43.02996 ? 479 HOH A O   1 
HETATM 2128 O  O   . HOH D 3 .   ? 4.44100   1.46800   84.29900 1.000 17.01726 ? 480 HOH A O   1 
HETATM 2129 O  O   . HOH D 3 .   ? -7.79600  12.23700  59.79100 1.000 27.59222 ? 481 HOH A O   1 
HETATM 2130 O  O   . HOH D 3 .   ? -7.99100  -1.32600  54.61600 1.000 26.77896 ? 482 HOH A O   1 
HETATM 2131 O  O   . HOH D 3 .   ? -5.10200  16.99600  71.27400 1.000 13.34051 ? 483 HOH A O   1 
HETATM 2132 O  O   . HOH D 3 .   ? -1.98100  9.40100   58.11400 1.000 36.33996 ? 484 HOH A O   1 
HETATM 2133 O  O   . HOH D 3 .   ? 2.45800   -9.09100  82.63000 1.000 16.81461 ? 485 HOH A O   1 
HETATM 2134 O  O   . HOH D 3 .   ? -21.82500 6.14600   77.09700 1.000 44.05996 ? 486 HOH A O   1 
HETATM 2135 O  O   A HOH D 3 .   ? 3.62900   -4.26800  84.72700 0.660 21.51780 ? 487 HOH A O   1 
HETATM 2136 O  O   . HOH D 3 .   ? -0.04200  10.70400  59.51900 1.000 22.16262 ? 488 HOH A O   1 
HETATM 2137 O  O   . HOH D 3 .   ? -1.78600  12.81800  60.26500 1.000 27.33429 ? 489 HOH A O   1 
HETATM 2138 O  O   A HOH D 3 .   ? 2.28800   -13.55000 78.39100 0.570 10.16644 ? 490 HOH A O   1 
HETATM 2139 O  O   . HOH D 3 .   ? -6.29500  15.80000  63.12600 1.000 26.92898 ? 491 HOH A O   1 
HETATM 2140 O  O   . HOH D 3 .   ? 0.22400   -15.90400 75.23600 1.000 11.34816 ? 492 HOH A O   1 
HETATM 2141 O  O   . HOH D 3 .   ? -21.00200 6.63200   80.05300 1.000 37.91996 ? 493 HOH A O   1 
HETATM 2142 O  O   . HOH D 3 .   ? -1.13500  -11.35400 58.89700 1.000 17.70419 ? 494 HOH A O   1 
HETATM 2143 O  O   . HOH D 3 .   ? -0.08500  -5.24300  55.66300 1.000 12.82992 ? 495 HOH A O   1 
HETATM 2144 O  O   . HOH D 3 .   ? -9.38700  15.70800  80.18900 1.000 14.40379 ? 496 HOH A O   1 
HETATM 2145 O  O   . HOH D 3 .   ? -2.09600  -16.68100 76.57700 1.000 12.44303 ? 497 HOH A O   1 
HETATM 2146 O  O   A HOH D 3 .   ? -9.54600  16.86000  77.86800 0.380 15.87996 ? 498 HOH A O   1 
HETATM 2147 O  O   B HOH D 3 .   ? -9.38000  17.95100  78.48100 0.620 19.62810 ? 498 HOH A O   1 
HETATM 2148 O  O   A HOH D 3 .   ? -19.82600 9.01500   80.32400 0.600 21.56518 ? 499 HOH A O   1 
HETATM 2149 O  O   B HOH D 3 .   ? -20.39300 9.58900   79.29200 0.400 27.80996 ? 499 HOH A O   1 
HETATM 2150 O  O   A HOH D 3 .   ? 3.04900   -7.80400  58.37300 0.700 16.19348 ? 500 HOH A O   1 
HETATM 2151 O  O   B HOH D 3 .   ? 2.30800   -8.00000  56.76900 0.300 9.88996  ? 500 HOH A O   1 
HETATM 2152 O  O   A HOH D 3 .   ? 10.20800  -4.72700  76.35300 0.600 17.13307 ? 501 HOH A O   1 
HETATM 2153 O  O   B HOH D 3 .   ? 11.85200  -3.00600  77.21500 0.400 21.66996 ? 501 HOH A O   1 
HETATM 2154 O  O   . HOH D 3 .   ? 3.83300   -7.39500  84.35500 1.000 21.53359 ? 502 HOH A O   1 
HETATM 2155 O  O   B HOH D 3 .   ? -11.90200 -13.88200 60.75600 0.540 16.43825 ? 503 HOH A O   1 
HETATM 2156 O  O   . HOH D 3 .   ? -5.60600  -1.49100  53.36200 1.000 33.35996 ? 504 HOH A O   1 
HETATM 2157 O  O   . HOH D 3 .   ? -9.68500  4.17600   53.95300 1.000 38.16996 ? 505 HOH A O   1 
HETATM 2158 O  O   . HOH D 3 .   ? -3.69000  10.06000  56.50200 1.000 46.88996 ? 506 HOH A O   1 
HETATM 2159 O  O   A HOH D 3 .   ? -11.43600 17.43000  75.67800 0.640 18.90696 ? 507 HOH A O   1 
HETATM 2160 O  O   B HOH D 3 .   ? -12.88400 16.44400  76.30100 0.360 15.20996 ? 507 HOH A O   1 
HETATM 2161 O  O   A HOH D 3 .   ? 1.76600   -4.49500  87.30000 0.560 24.40762 ? 508 HOH A O   1 
HETATM 2162 O  O   . HOH D 3 .   ? -15.52100 15.86200  75.70600 1.000 17.40152 ? 509 HOH A O   1 
HETATM 2163 O  O   . HOH D 3 .   ? -7.60100  14.87500  60.35000 1.000 43.26996 ? 510 HOH A O   1 
HETATM 2164 O  O   . HOH D 3 .   ? -5.04200  5.65200   53.86100 1.000 25.63935 ? 511 HOH A O   1 
HETATM 2165 O  O   . HOH D 3 .   ? 0.91100   -9.93000  57.73800 1.000 19.49388 ? 512 HOH A O   1 
HETATM 2166 O  O   . HOH D 3 .   ? -8.04100  18.69100  70.60100 1.000 15.73290 ? 513 HOH A O   1 
HETATM 2167 O  O   . HOH D 3 .   ? 7.63800   -11.12300 75.76200 1.000 12.67201 ? 514 HOH A O   1 
HETATM 2168 O  O   . HOH D 3 .   ? -15.59700 -1.68600  87.87900 1.000 37.63996 ? 515 HOH A O   1 
HETATM 2169 O  O   . HOH D 3 .   ? -13.82200 17.24600  74.12500 1.000 16.86988 ? 516 HOH A O   1 
HETATM 2170 O  O   . HOH D 3 .   ? 9.42400   9.28400   75.13000 1.000 22.68636 ? 517 HOH A O   1 
HETATM 2171 O  O   B HOH D 3 .   ? -16.98500 5.46500   86.29000 0.590 22.79427 ? 518 HOH A O   1 
HETATM 2172 O  O   . HOH D 3 .   ? 8.79800   -5.63000  80.68500 1.000 38.38996 ? 519 HOH A O   1 
HETATM 2173 O  O   . HOH D 3 .   ? -8.35000  0.13000   52.60600 1.000 30.78996 ? 520 HOH A O   1 
HETATM 2174 O  O   . HOH D 3 .   ? -2.92500  -6.96100  88.69100 1.000 22.17315 ? 521 HOH A O   1 
HETATM 2175 O  O   A HOH D 3 .   ? 11.58600  3.06600   76.08800 0.550 22.89428 ? 522 HOH A O   1 
HETATM 2176 O  O   B HOH D 3 .   ? 12.76000  2.73200   76.18200 0.450 26.34996 ? 522 HOH A O   1 
HETATM 2177 O  O   . HOH D 3 .   ? -8.52000  17.21500  63.52700 1.000 24.39183 ? 523 HOH A O   1 
HETATM 2178 O  O   . HOH D 3 .   ? -0.90000  8.93800   55.72600 1.000 42.59996 ? 524 HOH A O   1 
HETATM 2179 O  O   . HOH D 3 .   ? -10.17300 2.92600   90.03400 1.000 16.46193 ? 525 HOH A O   1 
HETATM 2180 O  O   . HOH D 3 .   ? -7.56100  18.49700  76.48600 1.000 18.39374 ? 526 HOH A O   1 
HETATM 2181 O  O   A HOH D 3 .   ? -12.24800 16.17300  80.21600 0.610 16.94357 ? 527 HOH A O   1 
HETATM 2182 O  O   . HOH D 3 .   ? 5.12100   8.13500   58.81200 1.000 15.99083 ? 528 HOH A O   1 
HETATM 2183 O  O   . HOH D 3 .   ? 6.43900   -4.72200  84.69100 1.000 41.68996 ? 529 HOH A O   1 
HETATM 2184 O  O   . HOH D 3 .   ? -6.06700  15.59600  82.98800 1.000 12.40355 ? 530 HOH A O   1 
HETATM 2185 O  O   A HOH D 3 .   ? 3.59300   -11.65800 82.93300 0.570 12.64306 ? 531 HOH A O   1 
HETATM 2186 O  O   B HOH D 3 .   ? 3.97300   -11.15800 81.98500 0.430 29.42996 ? 531 HOH A O   1 
HETATM 2187 O  O   . HOH D 3 .   ? 12.51600  2.74200   70.43000 1.000 26.84739 ? 532 HOH A O   1 
HETATM 2188 O  O   A HOH D 3 .   ? 10.21100  -6.28200  78.61900 0.690 27.11848 ? 533 HOH A O   1 
HETATM 2189 O  O   B HOH D 3 .   ? 9.91300   -4.97700  77.15000 0.310 30.29996 ? 533 HOH A O   1 
HETATM 2190 O  O   A HOH D 3 .   ? -12.18600 17.38500  78.37200 0.370 23.94996 ? 534 HOH A O   1 
HETATM 2191 O  O   B HOH D 3 .   ? -13.67000 19.78100  83.46000 0.630 23.89440 ? 534 HOH A O   1 
HETATM 2192 O  O   . HOH D 3 .   ? -11.70300 -2.97500  90.01500 1.000 36.02996 ? 535 HOH A O   1 
HETATM 2193 O  O   . HOH D 3 .   ? -8.01600  5.61000   52.86800 1.000 40.29996 ? 536 HOH A O   1 
HETATM 2194 O  O   A HOH D 3 .   ? 11.35400  3.40400   78.34300 0.420 15.42996 ? 537 HOH A O   1 
HETATM 2195 O  O   B HOH D 3 .   ? 10.89100  2.78100   77.27300 0.580 24.08916 ? 537 HOH A O   1 
HETATM 2196 O  O   A HOH D 3 .   ? -9.63000  19.09000  74.68400 0.580 16.63038 ? 538 HOH A O   1 
HETATM 2197 O  O   B HOH D 3 .   ? -8.98900  17.98300  74.76900 0.420 20.43996 ? 538 HOH A O   1 
HETATM 2198 O  O   . HOH D 3 .   ? -0.06200  15.10100  61.01900 1.000 29.99777 ? 539 HOH A O   1 
HETATM 2199 O  O   . HOH D 3 .   ? 4.24000   14.23500  63.50000 1.000 19.68600 ? 540 HOH A O   1 
HETATM 2200 O  O   . HOH D 3 .   ? -6.08000  1.54300   51.95100 1.000 19.85445 ? 541 HOH A O   1 
HETATM 2201 O  O   . HOH D 3 .   ? 7.39700   7.61600   60.05700 1.000 14.19324 ? 542 HOH A O   1 
HETATM 2202 O  O   A HOH D 3 .   ? -3.03200  -19.08300 68.36700 0.650 12.67201 ? 543 HOH A O   1 
HETATM 2203 O  O   B HOH D 3 .   ? -4.18200  -19.76700 68.66100 0.350 19.47996 ? 543 HOH A O   1 
HETATM 2204 O  O   A HOH D 3 .   ? 2.79300   -16.78500 75.70300 0.730 15.99872 ? 544 HOH A O   1 
HETATM 2205 O  O   B HOH D 3 .   ? 2.31800   -15.97400 76.90500 0.270 10.70996 ? 544 HOH A O   1 
HETATM 2206 O  O   A HOH D 3 .   ? -8.27800  -19.93200 65.46500 0.580 24.36025 ? 545 HOH A O   1 
HETATM 2207 O  O   B HOH D 3 .   ? -7.37700  -18.81500 65.17100 0.420 17.04996 ? 545 HOH A O   1 
HETATM 2208 O  O   A HOH D 3 .   ? 2.25900   -7.64700  55.49600 0.460 17.80996 ? 546 HOH A O   1 
HETATM 2209 O  O   B HOH D 3 .   ? 1.22800   -8.06200  54.48000 0.540 23.07852 ? 546 HOH A O   1 
HETATM 2210 O  O   . HOH D 3 .   ? 1.88500   11.33900  57.49900 1.000 35.11996 ? 547 HOH A O   1 
HETATM 2211 O  O   . HOH D 3 .   ? 6.03400   -2.09300  86.79000 1.000 46.96996 ? 548 HOH A O   1 
HETATM 2212 O  O   . HOH D 3 .   ? -8.66300  16.47700  82.78100 1.000 12.88782 ? 549 HOH A O   1 
HETATM 2213 O  O   . HOH D 3 .   ? -16.64300 3.40800   88.50000 1.000 29.00028 ? 550 HOH A O   1 
HETATM 2214 O  O   . HOH D 3 .   ? -2.80800  7.97600   53.58400 1.000 36.75996 ? 551 HOH A O   1 
HETATM 2215 O  O   A HOH D 3 .   ? 11.94000  3.72600   65.04900 0.630 18.63325 ? 552 HOH A O   1 
HETATM 2216 O  O   B HOH D 3 .   ? 12.62200  3.09600   65.73300 0.370 17.25996 ? 552 HOH A O   1 
HETATM 2217 O  O   A HOH D 3 .   ? 4.16700   -6.81000  56.15300 0.740 20.55716 ? 553 HOH A O   1 
HETATM 2218 O  O   B HOH D 3 .   ? 2.39200   -6.21100  54.55900 0.260 24.10996 ? 553 HOH A O   1 
HETATM 2219 O  O   A HOH D 3 .   ? -20.74200 3.43300   85.52900 0.710 29.60298 ? 554 HOH A O   1 
HETATM 2220 O  O   . HOH D 3 .   ? 2.49900   -2.28000  53.67500 1.000 13.52474 ? 555 HOH A O   1 
HETATM 2221 O  O   A HOH D 3 .   ? 2.68400   15.33400  62.06000 0.570 23.67596 ? 556 HOH A O   1 
HETATM 2222 O  O   B HOH D 3 .   ? 2.19300   16.24100  62.84200 0.430 15.82996 ? 556 HOH A O   1 
HETATM 2223 O  O   . HOH D 3 .   ? -2.18900  -19.26000 75.71100 1.000 12.81413 ? 557 HOH A O   1 
HETATM 2224 O  O   A HOH D 3 .   ? 11.07600  3.59800   80.91500 0.470 20.68996 ? 558 HOH A O   1 
HETATM 2225 O  O   B HOH D 3 .   ? 10.75500  3.13500   79.46300 0.530 20.91247 ? 558 HOH A O   1 
HETATM 2226 O  O   . HOH D 3 .   ? 13.11800  2.80400   67.69000 1.000 28.39494 ? 559 HOH A O   1 
HETATM 2227 O  O   . HOH D 3 .   ? -4.02600  -1.87000  91.59800 1.000 41.65996 ? 560 HOH A O   1 
HETATM 2228 O  O   . HOH D 3 .   ? 9.63800   -4.16100  83.00100 1.000 38.86996 ? 561 HOH A O   1 
HETATM 2229 O  O   . HOH D 3 .   ? -8.18700  0.13800   91.83400 1.000 27.91331 ? 562 HOH A O   1 
HETATM 2230 O  O   B HOH D 3 .   ? 12.80400  -1.10700  77.81400 0.860 37.20996 ? 563 HOH A O   1 
HETATM 2231 O  O   . HOH D 3 .   ? 2.85800   -16.99900 65.50700 1.000 12.02982 ? 564 HOH A O   1 
HETATM 2232 O  O   A HOH D 3 .   ? -6.09000  -11.58300 54.46200 0.420 28.54996 ? 565 HOH A O   1 
HETATM 2233 O  O   B HOH D 3 .   ? -4.67200  -11.44500 55.11100 0.580 31.85996 ? 565 HOH A O   1 
HETATM 2234 O  O   . HOH D 3 .   ? 13.32300  -4.83100  71.34200 1.000 24.17339 ? 566 HOH A O   1 
HETATM 2235 O  O   A HOH D 3 .   ? -4.10100  -13.09700 55.69000 0.540 24.03916 ? 567 HOH A O   1 
HETATM 2236 O  O   B HOH D 3 .   ? -1.72700  -11.88100 55.85300 0.460 23.78996 ? 567 HOH A O   1 
HETATM 2237 O  O   A HOH D 3 .   ? -1.03200  -19.21400 66.45900 0.590 11.70347 ? 568 HOH A O   1 
HETATM 2238 O  O   B HOH D 3 .   ? -1.31300  -18.15900 66.75000 0.410 13.25996 ? 568 HOH A O   1 
HETATM 2239 O  O   . HOH D 3 .   ? 4.49300   10.38600  57.39400 1.000 18.14371 ? 569 HOH A O   1 
HETATM 2240 O  O   . HOH D 3 .   ? 9.75900   -11.22200 77.36100 1.000 14.63014 ? 570 HOH A O   1 
HETATM 2241 O  O   A HOH D 3 .   ? 5.93900   1.01800   88.15700 0.750 28.82131 ? 571 HOH A O   1 
HETATM 2242 O  O   . HOH D 3 .   ? -13.96900 2.79900   90.86000 1.000 22.83901 ? 572 HOH A O   1 
HETATM 2243 O  O   . HOH D 3 .   ? 10.72400  -8.99900  78.73700 1.000 31.62996 ? 573 HOH A O   1 
HETATM 2244 O  O   . HOH D 3 .   ? 0.17300   18.28000  63.65200 1.000 30.99996 ? 574 HOH A O   1 
HETATM 2245 O  O   . HOH D 3 .   ? 8.82000   2.70500   85.56500 1.000 46.05996 ? 575 HOH A O   1 
HETATM 2246 O  O   . HOH D 3 .   ? -8.63200  17.21800  59.51800 1.000 39.35996 ? 576 HOH A O   1 
HETATM 2247 O  O   A HOH D 3 .   ? -19.66200 5.19000   87.25200 0.450 20.39996 ? 577 HOH A O   1 
HETATM 2248 O  O   . HOH D 3 .   ? 7.49500   6.03100   86.00800 1.000 28.59497 ? 578 HOH A O   1 
HETATM 2249 O  O   . HOH D 3 .   ? -8.68300  -1.58000  50.31600 1.000 37.26996 ? 579 HOH A O   1 
HETATM 2250 O  O   . HOH D 3 .   ? 0.33900   -19.79500 74.72500 1.000 16.98568 ? 580 HOH A O   1 
HETATM 2251 O  O   . HOH D 3 .   ? 3.97000   14.23700  59.43500 1.000 32.02996 ? 581 HOH A O   1 
HETATM 2252 O  O   . HOH D 3 .   ? -8.91000  21.22000  68.57500 1.000 22.63636 ? 582 HOH A O   1 
HETATM 2253 O  O   . HOH D 3 .   ? -5.71600  -20.44800 65.01700 1.000 27.48431 ? 583 HOH A O   1 
HETATM 2254 O  O   . HOH D 3 .   ? -14.72400 19.83000  74.53500 1.000 18.28321 ? 584 HOH A O   1 
HETATM 2255 O  O   . HOH D 3 .   ? -17.73700 5.94000   89.06300 1.000 20.33608 ? 585 HOH A O   1 
HETATM 2256 O  O   . HOH D 3 .   ? -7.59300  19.32700  61.84600 1.000 38.77996 ? 586 HOH A O   1 
HETATM 2257 O  O   . HOH D 3 .   ? -10.52700 20.72100  76.48800 1.000 35.35996 ? 587 HOH A O   1 
HETATM 2258 O  O   . HOH D 3 .   ? 9.43400   9.43800   60.54700 1.000 15.15651 ? 588 HOH A O   1 
HETATM 2259 O  O   . HOH D 3 .   ? 14.93800  1.27200   72.11100 1.000 37.81996 ? 589 HOH A O   1 
HETATM 2260 O  O   . HOH D 3 .   ? 12.90900  3.44600   62.81300 1.000 35.28996 ? 590 HOH A O   1 
HETATM 2261 O  O   . HOH D 3 .   ? 3.77800   13.06700  85.57300 1.000 14.06954 ? 591 HOH A O   1 
HETATM 2262 O  O   . HOH D 3 .   ? -10.08900 3.27700   92.75200 1.000 28.89237 ? 592 HOH A O   1 
HETATM 2263 O  O   . HOH D 3 .   ? 9.03800   -12.61500 79.62800 1.000 16.86461 ? 593 HOH A O   1 
HETATM 2264 O  O   . HOH D 3 .   ? -3.01400  21.63400  72.02300 1.000 18.21478 ? 594 HOH A O   1 
HETATM 2265 O  O   . HOH D 3 .   ? 6.03100   14.83000  61.54400 1.000 16.31981 ? 595 HOH A O   1 
HETATM 2266 O  O   . HOH D 3 .   ? -4.79400  19.33800  61.20500 1.000 37.53996 ? 596 HOH A O   1 
HETATM 2267 O  O   A HOH D 3 .   ? -3.83800  -20.92500 77.29900 0.620 15.02229 ? 597 HOH A O   1 
HETATM 2268 O  O   B HOH D 3 .   ? -3.51700  -21.49400 76.32200 0.380 17.28996 ? 597 HOH A O   1 
HETATM 2269 O  O   . HOH D 3 .   ? -5.10900  17.65200  84.69600 1.000 15.01966 ? 598 HOH A O   1 
HETATM 2270 O  O   . HOH D 3 .   ? 9.60500   -10.78300 81.64700 1.000 24.44184 ? 599 HOH A O   1 
HETATM 2271 O  O   . HOH D 3 .   ? 1.58000   -5.17100  51.72600 1.000 44.49996 ? 600 HOH A O   1 
HETATM 2272 O  O   A HOH D 3 .   ? 14.91700  0.36300   66.63900 0.600 20.00710 ? 601 HOH A O   1 
HETATM 2273 O  O   A HOH D 3 .   ? -8.55400  11.91300  90.19900 0.550 14.16955 ? 602 HOH A O   1 
HETATM 2274 O  O   B HOH D 3 .   ? -7.95800  11.93800  91.66400 0.450 22.47996 ? 602 HOH A O   1 
HETATM 2275 O  O   . HOH D 3 .   ? 1.65500   20.69500  70.72300 1.000 21.84942 ? 603 HOH A O   1 
HETATM 2276 O  O   . HOH D 3 .   ? -5.07000  0.32600   93.74900 1.000 35.86996 ? 604 HOH A O   1 
HETATM 2277 O  O   . HOH D 3 .   ? -4.45500  3.08900   49.51200 1.000 32.47996 ? 605 HOH A O   1 
HETATM 2278 O  O   . HOH D 3 .   ? 2.99800   -11.20300 54.88200 1.000 31.35996 ? 606 HOH A O   1 
HETATM 2279 O  O   . HOH D 3 .   ? -10.39600 8.30100   91.96300 1.000 41.04996 ? 607 HOH A O   1 
HETATM 2280 O  O   . HOH D 3 .   ? 6.79400   -16.57900 77.75300 1.000 24.38920 ? 608 HOH A O   1 
HETATM 2281 O  O   A HOH D 3 .   ? -14.81200 14.39900  86.64700 0.740 16.98568 ? 609 HOH A O   1 
HETATM 2282 O  O   A HOH D 3 .   ? 12.45600  -11.42700 71.47900 0.580 13.24050 ? 610 HOH A O   1 
HETATM 2283 O  O   B HOH D 3 .   ? 13.10700  -11.71300 70.44300 0.420 10.41996 ? 610 HOH A O   1 
HETATM 2284 O  O   A HOH D 3 .   ? 10.53400  -1.39600  85.77900 0.650 30.74996 ? 611 HOH A O   1 
HETATM 2285 O  O   B HOH D 3 .   ? 9.28400   0.61900   85.81400 0.350 28.97996 ? 611 HOH A O   1 
HETATM 2286 O  O   . HOH D 3 .   ? 1.81300   -2.05900  50.94800 1.000 39.57996 ? 612 HOH A O   1 
HETATM 2287 O  O   . HOH D 3 .   ? 14.32000  3.40200   78.67700 1.000 48.61996 ? 613 HOH A O   1 
HETATM 2288 O  O   . HOH D 3 .   ? 11.36400  7.20000   82.83000 1.000 42.42996 ? 614 HOH A O   1 
HETATM 2289 O  O   . HOH D 3 .   ? -8.60200  6.29200   92.95100 1.000 41.02996 ? 615 HOH A O   1 
HETATM 2290 O  O   . HOH D 3 .   ? -12.65000 4.19700   92.70500 1.000 23.85229 ? 616 HOH A O   1 
HETATM 2291 O  O   . HOH D 3 .   ? 0.71700   21.23800  73.30500 1.000 21.36515 ? 617 HOH A O   1 
HETATM 2292 O  O   . HOH D 3 .   ? -0.34800  20.67200  65.06600 1.000 36.94996 ? 618 HOH A O   1 
HETATM 2293 O  O   A HOH D 3 .   ? -19.72400 16.26000  80.11000 0.380 11.21996 ? 619 HOH A O   1 
HETATM 2294 O  O   B HOH D 3 .   ? -19.75000 15.49900  80.36100 0.620 13.79319 ? 619 HOH A O   1 
HETATM 2295 O  O   . HOH D 3 .   ? -6.01100  7.13900   50.14900 1.000 43.40996 ? 620 HOH A O   1 
HETATM 2296 O  O   . HOH D 3 .   ? 3.05200   18.20800  62.34300 1.000 37.21996 ? 621 HOH A O   1 
HETATM 2297 O  O   A HOH D 3 .   ? -16.71600 9.74200   89.29300 0.550 23.94967 ? 622 HOH A O   1 
HETATM 2298 O  O   B HOH D 3 .   ? -17.00100 8.25900   89.47100 0.450 23.86996 ? 622 HOH A O   1 
HETATM 2299 O  O   . HOH D 3 .   ? -4.87600  -20.16900 61.53800 1.000 27.92120 ? 623 HOH A O   1 
HETATM 2300 O  O   . HOH D 3 .   ? -12.70400 21.54100  75.43000 1.000 28.82921 ? 624 HOH A O   1 
HETATM 2301 O  O   . HOH D 3 .   ? -10.68700 22.35100  72.36300 1.000 33.21996 ? 625 HOH A O   1 
HETATM 2302 O  O   . HOH D 3 .   ? 15.49600  2.56100   75.70600 1.000 40.15996 ? 626 HOH A O   1 
HETATM 2303 O  O   A HOH D 3 .   ? 13.03100  3.46100   82.30900 0.530 24.88400 ? 627 HOH A O   1 
HETATM 2304 O  O   B HOH D 3 .   ? 12.33300  2.92100   80.99400 0.470 18.26996 ? 627 HOH A O   1 
HETATM 2305 O  O   . HOH D 3 .   ? 14.91500  -6.69100  72.44200 1.000 36.53996 ? 628 HOH A O   1 
HETATM 2306 O  O   . HOH D 3 .   ? -9.24500  19.00700  83.75200 1.000 18.68589 ? 629 HOH A O   1 
HETATM 2307 O  O   . HOH D 3 .   ? -3.33000  -1.17200  49.10100 1.000 37.70996 ? 630 HOH A O   1 
HETATM 2308 O  O   . HOH D 3 .   ? 7.30900   -13.63700 60.14400 1.000 24.61291 ? 631 HOH A O   1 
HETATM 2309 O  O   . HOH D 3 .   ? -10.75900 20.80300  79.83700 1.000 25.64198 ? 632 HOH A O   1 
HETATM 2310 O  O   . HOH D 3 .   ? -14.64300 19.99600  78.93000 1.000 18.94118 ? 633 HOH A O   1 
HETATM 2311 O  O   . HOH D 3 .   ? 10.01400  7.02700   85.49700 1.000 37.54996 ? 634 HOH A O   1 
HETATM 2312 O  O   . HOH D 3 .   ? 15.22600  -4.20300  66.95700 1.000 16.08031 ? 635 HOH A O   1 
HETATM 2313 O  O   . HOH D 3 .   ? -11.49400 22.12000  67.87600 1.000 31.21996 ? 636 HOH A O   1 
HETATM 2314 O  O   . HOH D 3 .   ? -2.00100  22.39500  69.65600 1.000 23.73386 ? 637 HOH A O   1 
HETATM 2315 O  O   . HOH D 3 .   ? 13.90800  9.09900   76.40800 1.000 33.32975 ? 638 HOH A O   1 
HETATM 2316 O  O   . HOH D 3 .   ? -7.65500  -21.23900 62.91600 1.000 45.04996 ? 639 HOH A O   1 
HETATM 2317 O  O   . HOH D 3 .   ? -9.21200  -22.38600 76.12200 1.000 30.50046 ? 640 HOH A O   1 
HETATM 2318 O  O   . HOH D 3 .   ? 12.11800  -5.56400  59.46500 1.000 19.35702 ? 641 HOH A O   1 
HETATM 2319 O  O   B HOH D 3 .   ? -24.31500 6.69600   84.87800 0.410 28.47996 ? 642 HOH A O   1 
HETATM 2320 O  O   . HOH D 3 .   ? -1.65700  16.60100  86.93200 1.000 15.23284 ? 643 HOH A O   1 
HETATM 2321 O  O   . HOH D 3 .   ? -1.99200  -20.97000 63.05900 1.000 25.61303 ? 644 HOH A O   1 
HETATM 2322 O  O   . HOH D 3 .   ? 8.43000   16.25300  78.68200 1.000 22.37054 ? 645 HOH A O   1 
HETATM 2323 O  O   A HOH D 3 .   ? -0.15800  1.42600   49.25500 0.430 15.33996 ? 646 HOH A O   1 
HETATM 2324 O  O   B HOH D 3 .   ? 1.02500   1.50500   49.21600 0.570 26.17362 ? 646 HOH A O   1 
HETATM 2325 O  O   . HOH D 3 .   ? 7.75600   -12.26900 58.03000 1.000 27.34482 ? 647 HOH A O   1 
HETATM 2326 O  O   . HOH D 3 .   ? 9.86700   13.43700  81.38900 1.000 21.54675 ? 648 HOH A O   1 
HETATM 2327 O  O   A HOH D 3 .   ? 4.97900   5.27800   91.13500 0.660 28.35913 ? 649 HOH A O   1 
HETATM 2328 O  O   B HOH D 3 .   ? 4.89400   7.14600   91.25500 0.340 27.36831 ? 649 HOH A O   1 
HETATM 2329 O  O   . HOH D 3 .   ? -1.74700  -22.52500 68.21200 1.000 44.11996 ? 650 HOH A O   1 
HETATM 2330 O  O   . HOH D 3 .   ? -1.06200  -21.86900 65.72500 1.000 30.53996 ? 651 HOH A O   1 
HETATM 2331 O  O   . HOH D 3 .   ? -7.92200  22.94800  66.77900 1.000 33.11996 ? 652 HOH A O   1 
HETATM 2332 O  O   . HOH D 3 .   ? 2.54600   15.17300  86.93500 1.000 13.54580 ? 653 HOH A O   1 
HETATM 2333 O  O   . HOH D 3 .   ? 3.78500   -20.81100 72.11800 1.000 29.35295 ? 654 HOH A O   1 
HETATM 2334 O  O   . HOH D 3 .   ? 11.68300  11.32700  80.90400 1.000 27.55800 ? 655 HOH A O   1 
HETATM 2335 O  O   . HOH D 3 .   ? -2.56600  1.26100   48.42600 1.000 39.32996 ? 656 HOH A O   1 
HETATM 2336 O  O   A HOH D 3 .   ? -10.39900 18.00700  86.26300 0.400 23.07996 ? 657 HOH A O   1 
HETATM 2337 O  O   B HOH D 3 .   ? -10.07900 19.39400  86.34400 0.600 29.25821 ? 657 HOH A O   1 
HETATM 2338 O  O   . HOH D 3 .   ? 15.49600  -3.12300  64.43600 1.000 20.92563 ? 658 HOH A O   1 
HETATM 2339 O  O   . HOH D 3 .   ? -11.05600 20.48100  82.42100 1.000 26.68948 ? 659 HOH A O   1 
HETATM 2340 O  O   . HOH D 3 .   ? 3.69600   -0.67000  50.42200 1.000 38.76996 ? 660 HOH A O   1 
HETATM 2341 O  O   . HOH D 3 .   ? -5.05400  11.53100  92.05300 1.000 18.41217 ? 661 HOH A O   1 
HETATM 2342 O  O   A HOH D 3 .   ? 12.31600  -2.29200  85.29100 0.570 27.65538 ? 662 HOH A O   1 
HETATM 2343 O  O   B HOH D 3 .   ? 13.49500  -0.91900  84.68200 0.430 18.87996 ? 662 HOH A O   1 
HETATM 2344 O  O   A HOH D 3 .   ? 5.23800   -3.75000  51.48600 0.590 31.04996 ? 663 HOH A O   1 
HETATM 2345 O  O   B HOH D 3 .   ? 5.01500   -5.19100  52.13100 0.410 30.68996 ? 663 HOH A O   1 
HETATM 2346 O  O   . HOH D 3 .   ? 1.51400   -22.06400 72.91400 1.000 43.46996 ? 664 HOH A O   1 
HETATM 2347 O  O   . HOH D 3 .   ? -5.01700  23.22200  66.67600 1.000 27.72907 ? 665 HOH A O   1 
HETATM 2348 O  O   . HOH D 3 .   ? -19.57000 8.88500   89.36200 1.000 17.97001 ? 666 HOH A O   1 
HETATM 2349 O  O   A HOH D 3 .   ? 13.84300  1.36500   82.96100 0.540 21.75467 ? 667 HOH A O   1 
HETATM 2350 O  O   B HOH D 3 .   ? 14.18900  2.72200   82.62300 0.460 25.20996 ? 667 HOH A O   1 
HETATM 2351 O  O   . HOH D 3 .   ? 0.95800   22.50500  69.41900 1.000 48.17996 ? 668 HOH A O   1 
HETATM 2352 O  O   . HOH D 3 .   ? 0.29000   -15.44300 54.88800 1.000 30.39996 ? 669 HOH A O   1 
HETATM 2353 O  O   . HOH D 3 .   ? 9.68300   -1.17400  54.35600 1.000 19.74127 ? 670 HOH A O   1 
HETATM 2354 O  O   . HOH D 3 .   ? 16.54800  -1.44200  76.85800 1.000 41.85996 ? 671 HOH A O   1 
HETATM 2355 O  O   A HOH D 3 .   ? -5.78000  -15.20300 53.10900 0.780 38.00996 ? 672 HOH A O   1 
HETATM 2356 O  O   . HOH D 3 .   ? 5.84700   17.75500  61.39600 1.000 27.88436 ? 673 HOH A O   1 
HETATM 2357 O  O   . HOH D 3 .   ? 15.80800  8.32200   72.04400 1.000 23.61806 ? 674 HOH A O   1 
HETATM 2358 O  O   . HOH D 3 .   ? 3.46900   21.62300  74.38600 1.000 36.12996 ? 675 HOH A O   1 
HETATM 2359 O  O   . HOH D 3 .   ? 16.63700  -4.37100  74.73500 1.000 40.03996 ? 676 HOH A O   1 
HETATM 2360 O  O   . HOH D 3 .   ? 4.80100   -7.60500  51.91500 1.000 51.65996 ? 677 HOH A O   1 
HETATM 2361 O  O   . HOH D 3 .   ? 6.61200   8.77300   89.59300 1.000 25.87096 ? 678 HOH A O   1 
HETATM 2362 O  O   . HOH D 3 .   ? -11.65400 23.55300  69.98500 1.000 36.15996 ? 680 HOH A O   1 
HETATM 2363 O  O   . HOH D 3 .   ? -2.76700  23.75800  73.95500 1.000 25.20509 ? 681 HOH A O   1 
HETATM 2364 O  O   . HOH D 3 .   ? 3.82200   11.65700  89.93500 1.000 18.69904 ? 682 HOH A O   1 
HETATM 2365 O  O   . HOH D 3 .   ? 4.33600   -20.94700 75.58300 1.000 41.39996 ? 683 HOH A O   1 
HETATM 2366 O  O   . HOH D 3 .   ? 11.52100  -8.94500  58.58500 1.000 31.18996 ? 684 HOH A O   1 
HETATM 2367 O  O   A HOH D 3 .   ? -5.55200  18.41000  87.26400 0.690 15.34338 ? 685 HOH A O   1 
HETATM 2368 O  O   B HOH D 3 .   ? -4.02000  18.03100  87.40400 0.310 15.92996 ? 685 HOH A O   1 
HETATM 2369 O  O   . HOH D 3 .   ? -23.07200 13.42400  83.32200 1.000 38.69996 ? 686 HOH A O   1 
HETATM 2370 O  O   B HOH D 3 .   ? -23.56500 5.45700   88.04700 0.450 18.06996 ? 687 HOH A O   1 
HETATM 2371 O  O   A HOH D 3 .   ? 14.29400  -0.83400  83.78800 0.480 22.87996 ? 688 HOH A O   1 
HETATM 2372 O  O   B HOH D 3 .   ? 14.76800  0.43400   83.47600 0.520 25.32352 ? 688 HOH A O   1 
HETATM 2373 O  O   A HOH D 3 .   ? -15.68400 14.14800  89.15900 0.630 19.55178 ? 689 HOH A O   1 
HETATM 2374 O  O   B HOH D 3 .   ? -16.91400 12.70200  88.43100 0.370 24.50996 ? 689 HOH A O   1 
HETATM 2375 O  O   . HOH D 3 .   ? 16.67500  -6.48700  70.55800 1.000 35.00996 ? 690 HOH A O   1 
HETATM 2376 O  O   . HOH D 3 .   ? -14.13900 22.30900  77.90300 1.000 23.19958 ? 691 HOH A O   1 
HETATM 2377 O  O   A HOH D 3 .   ? 13.07000  -9.54800  61.17700 0.510 18.60693 ? 692 HOH A O   1 
HETATM 2378 O  O   B HOH D 3 .   ? 12.67400  -10.72500 59.67300 0.490 23.17996 ? 692 HOH A O   1 
HETATM 2379 O  O   . HOH D 3 .   ? 10.12800  -10.41700 57.45500 1.000 44.16996 ? 693 HOH A O   1 
HETATM 2380 O  O   . HOH D 3 .   ? -4.15100  23.24300  64.29500 1.000 39.70996 ? 694 HOH A O   1 
HETATM 2381 O  O   . HOH D 3 .   ? 4.50400   21.25500  76.95900 1.000 34.44996 ? 695 HOH A O   1 
HETATM 2382 O  O   . HOH D 3 .   ? 0.42000   21.47200  81.40900 1.000 16.67775 ? 696 HOH A O   1 
HETATM 2383 O  O   . HOH D 3 .   ? -6.11700  -24.43200 73.43700 1.000 33.49996 ? 697 HOH A O   1 
HETATM 2384 O  O   . HOH D 3 .   ? -0.03600  23.68900  73.55800 1.000 29.00028 ? 698 HOH A O   1 
HETATM 2385 O  O   . HOH D 3 .   ? -2.66800  10.70000  93.34700 1.000 25.00770 ? 699 HOH A O   1 
HETATM 2386 O  O   A HOH D 3 .   ? 10.32900  17.72500  69.11100 0.720 16.87514 ? 700 HOH A O   1 
HETATM 2387 O  O   B HOH D 3 .   ? 9.30100   18.80100  69.12000 0.280 13.78996 ? 700 HOH A O   1 
HETATM 2388 O  O   . HOH D 3 .   ? 10.43900  15.77800  80.12800 1.000 37.89996 ? 701 HOH A O   1 
HETATM 2389 O  O   A HOH D 3 .   ? -15.86100 17.23700  86.75600 0.700 27.86067 ? 702 HOH A O   1 
HETATM 2390 O  O   B HOH D 3 .   ? -14.73900 16.24700  85.79100 0.300 13.20996 ? 702 HOH A O   1 
HETATM 2391 O  O   . HOH D 3 .   ? 8.33200   18.70900  78.10900 1.000 27.29218 ? 703 HOH A O   1 
HETATM 2392 O  O   . HOH D 3 .   ? 4.09800   9.70100   91.67000 1.000 23.96547 ? 704 HOH A O   1 
HETATM 2393 O  O   . HOH D 3 .   ? 9.93600   9.19400   87.54800 1.000 22.57846 ? 705 HOH A O   1 
HETATM 2394 O  O   A HOH D 3 .   ? -8.56400  13.66500  92.18200 0.520 21.14407 ? 706 HOH A O   1 
HETATM 2395 O  O   B HOH D 3 .   ? -9.69700  13.79000  90.80500 0.480 16.83996 ? 706 HOH A O   1 
HETATM 2396 O  O   . HOH D 3 .   ? -10.22100 10.52600  93.82300 1.000 37.35996 ? 707 HOH A O   1 
HETATM 2397 O  O   . HOH D 3 .   ? 7.13500   20.32800  76.49000 1.000 27.19217 ? 708 HOH A O   1 
HETATM 2398 O  O   . HOH D 3 .   ? -7.56800  23.83200  79.17500 1.000 39.99996 ? 709 HOH A O   1 
HETATM 2399 O  O   . HOH D 3 .   ? -12.27500 23.07600  79.49200 1.000 26.36049 ? 710 HOH A O   1 
HETATM 2400 O  O   . HOH D 3 .   ? 3.16700   9.51100   50.59200 1.000 35.55996 ? 711 HOH A O   1 
HETATM 2401 O  O   . HOH D 3 .   ? -3.10300  24.62800  68.32000 1.000 42.92996 ? 712 HOH A O   1 
HETATM 2402 O  O   . HOH D 3 .   ? -8.42700  -24.70000 74.66000 1.000 26.82370 ? 713 HOH A O   1 
HETATM 2403 O  O   . HOH D 3 .   ? -1.55400  7.36000   94.98300 1.000 24.84715 ? 714 HOH A O   1 
HETATM 2404 O  O   . HOH D 3 .   ? 9.54200   -15.93600 61.06900 1.000 35.19996 ? 715 HOH A O   1 
HETATM 2405 O  O   . HOH D 3 .   ? -1.90500  -17.62000 54.26000 1.000 30.98996 ? 716 HOH A O   1 
HETATM 2406 O  O   . HOH D 3 .   ? -11.90400 -18.54400 55.26600 1.000 35.91996 ? 717 HOH A O   1 
HETATM 2407 O  O   A HOH D 3 .   ? -2.97300  -24.73600 69.59600 0.560 29.06608 ? 718 HOH A O   1 
HETATM 2408 O  O   B HOH D 3 .   ? -3.63600  -23.81200 68.33000 0.440 28.15996 ? 718 HOH A O   1 
HETATM 2409 O  O   A HOH D 3 .   ? -1.33600  12.96500  92.57000 0.600 12.52462 ? 719 HOH A O   1 
HETATM 2410 O  O   B HOH D 3 .   ? -1.64200  14.47200  92.67900 0.400 15.00996 ? 719 HOH A O   1 
HETATM 2411 O  O   . HOH D 3 .   ? -4.01400  15.73600  91.21300 1.000 14.49328 ? 720 HOH A O   1 
HETATM 2412 O  O   . HOH D 3 .   ? 1.75900   -18.77100 56.93600 1.000 31.42996 ? 721 HOH A O   1 
HETATM 2413 O  O   . HOH D 3 .   ? -9.93300  24.34000  77.93500 1.000 30.00303 ? 722 HOH A O   1 
HETATM 2414 O  O   . HOH D 3 .   ? 6.17200   14.97100  87.53800 1.000 18.18846 ? 723 HOH A O   1 
HETATM 2415 O  O   . HOH D 3 .   ? -8.13400  25.29800  69.84500 1.000 43.40996 ? 724 HOH A O   1 
HETATM 2416 O  O   . HOH D 3 .   ? -7.97400  19.18100  88.15000 1.000 27.75539 ? 725 HOH A O   1 
HETATM 2417 O  O   . HOH D 3 .   ? -11.83400 24.23900  65.78000 1.000 37.81996 ? 726 HOH A O   1 
HETATM 2418 O  O   A HOH D 3 .   ? -1.57900  -24.87500 71.49500 0.590 32.63996 ? 727 HOH A O   1 
HETATM 2419 O  O   B HOH D 3 .   ? -2.84700  -25.40600 71.10400 0.410 27.42996 ? 727 HOH A O   1 
HETATM 2420 O  O   A HOH D 3 .   ? 0.50600   -24.34500 72.64600 0.640 33.24996 ? 728 HOH A O   1 
HETATM 2421 O  O   B HOH D 3 .   ? -0.93100  -24.23400 73.08500 0.360 30.27996 ? 728 HOH A O   1 
HETATM 2422 O  O   A HOH D 3 .   ? 9.25700   -3.58700  51.94500 0.640 33.25996 ? 729 HOH A O   1 
HETATM 2423 O  O   B HOH D 3 .   ? 7.92900   -2.83500  50.72600 0.360 20.02996 ? 729 HOH A O   1 
HETATM 2424 O  O   . HOH D 3 .   ? -5.61800  25.09300  76.67200 1.000 34.18996 ? 730 HOH A O   1 
HETATM 2425 O  O   . HOH D 3 .   ? 12.77600  4.50000   55.50400 1.000 26.15520 ? 731 HOH A O   1 
HETATM 2426 O  O   . HOH D 3 .   ? 11.44900  -13.05500 59.16200 1.000 33.93996 ? 732 HOH A O   1 
HETATM 2427 O  O   . HOH D 3 .   ? 1.17000   12.58700  92.53600 1.000 14.10902 ? 733 HOH A O   1 
HETATM 2428 O  O   . HOH D 3 .   ? 10.68000  14.71800  83.60200 1.000 35.89996 ? 734 HOH A O   1 
HETATM 2429 O  O   . HOH D 3 .   ? 11.13100  -18.34800 72.83900 1.000 13.57738 ? 735 HOH A O   1 
HETATM 2430 O  O   A HOH D 3 .   ? 14.31000  -6.79700  58.34900 0.380 19.69996 ? 736 HOH A O   1 
HETATM 2431 O  O   B HOH D 3 .   ? 14.05000  -8.67500  57.25400 0.620 37.48996 ? 736 HOH A O   1 
HETATM 2432 O  O   . HOH D 3 .   ? 4.89100   23.11100  73.22900 1.000 42.16996 ? 737 HOH A O   1 
HETATM 2433 O  O   . HOH D 3 .   ? 11.18600  -18.46900 70.08200 1.000 16.73302 ? 738 HOH A O   1 
HETATM 2434 O  O   A HOH D 3 .   ? 8.62400   -20.72800 70.56000 0.550 19.32807 ? 739 HOH A O   1 
HETATM 2435 O  O   B HOH D 3 .   ? 7.53100   -21.62500 70.43700 0.450 28.76996 ? 739 HOH A O   1 
HETATM 2436 O  O   . HOH D 3 .   ? 10.44100  19.05400  76.16300 1.000 19.63074 ? 740 HOH A O   1 
HETATM 2437 O  O   . HOH D 3 .   ? 12.10300  10.32100  86.35000 1.000 34.52996 ? 741 HOH A O   1 
HETATM 2438 O  O   . HOH D 3 .   ? 5.68300   -22.72900 71.16100 1.000 35.95996 ? 742 HOH A O   1 
HETATM 2439 O  O   . HOH D 3 .   ? -18.47000 17.33300  86.96200 1.000 38.50996 ? 743 HOH A O   1 
HETATM 2440 O  O   . HOH D 3 .   ? -20.38400 19.31100  82.43300 1.000 19.87287 ? 744 HOH A O   1 
HETATM 2441 O  O   A HOH D 3 .   ? 9.49700   20.39800  69.25300 0.610 19.32544 ? 745 HOH A O   1 
HETATM 2442 O  O   B HOH D 3 .   ? 8.73300   21.17100  69.48700 0.390 23.61996 ? 745 HOH A O   1 
HETATM 2443 O  O   . HOH D 3 .   ? 6.84500   -21.49000 76.78500 1.000 45.52996 ? 746 HOH A O   1 
HETATM 2444 O  O   . HOH D 3 .   ? 6.62600   7.42100   50.38000 1.000 24.62081 ? 747 HOH A O   1 
HETATM 2445 O  O   . HOH D 3 .   ? 10.06800  14.39300  85.71400 1.000 33.69996 ? 748 HOH A O   1 
HETATM 2446 O  O   . HOH D 3 .   ? 13.75900  2.19600   55.36200 1.000 33.08996 ? 749 HOH A O   1 
HETATM 2447 O  O   . HOH D 3 .   ? 12.65100  17.14400  76.67200 1.000 27.76592 ? 750 HOH A O   1 
HETATM 2448 O  O   . HOH D 3 .   ? 19.04700  -4.16800  68.60300 1.000 36.78996 ? 751 HOH A O   1 
HETATM 2449 O  O   . HOH D 3 .   ? -8.52500  -23.06100 59.07800 1.000 34.06996 ? 752 HOH A O   1 
HETATM 2450 O  O   A HOH D 3 .   ? 3.26400   -20.38700 58.31700 0.540 23.42330 ? 753 HOH A O   1 
HETATM 2451 O  O   B HOH D 3 .   ? 2.34200   -20.84900 58.70700 0.460 17.45996 ? 753 HOH A O   1 
HETATM 2452 O  O   . HOH D 3 .   ? -11.55700 22.81200  83.88300 1.000 40.80996 ? 754 HOH A O   1 
HETATM 2453 O  O   . HOH D 3 .   ? 11.90600  -0.84100  52.71200 1.000 37.65996 ? 755 HOH A O   1 
HETATM 2454 O  O   A HOH D 3 .   ? 3.82000   22.86300  80.63700 0.530 33.15996 ? 756 HOH A O   1 
HETATM 2455 O  O   B HOH D 3 .   ? 4.64200   22.72100  79.05300 0.470 30.93996 ? 756 HOH A O   1 
HETATM 2456 O  O   . HOH D 3 .   ? 12.73900  -7.27500  54.86800 1.000 26.24995 ? 757 HOH A O   1 
HETATM 2457 O  O   . HOH D 3 .   ? -12.29400 -20.71700 55.60800 1.000 42.45996 ? 758 HOH A O   1 
HETATM 2458 O  O   . HOH D 3 .   ? 16.38700  -10.30200 63.17500 1.000 13.46157 ? 759 HOH A O   1 
HETATM 2459 O  O   . HOH D 3 .   ? 0.43700   -25.38400 67.42800 1.000 40.71996 ? 760 HOH A O   1 
HETATM 2460 O  O   . HOH D 3 .   ? 11.14500  -11.12400 55.01400 1.000 39.37996 ? 761 HOH A O   1 
HETATM 2461 O  O   A HOH D 3 .   ? 17.89600  -10.42100 69.36900 0.740 18.22267 ? 762 HOH A O   1 
HETATM 2462 O  O   B HOH D 3 .   ? 18.93300  -10.63500 69.47000 0.260 8.94996  ? 762 HOH A O   1 
HETATM 2463 O  O   . HOH D 3 .   ? 5.57900   17.68400  87.81100 1.000 25.85780 ? 763 HOH A O   1 
HETATM 2464 O  O   . HOH D 3 .   ? 5.16900   20.74900  84.26500 1.000 27.56327 ? 764 HOH A O   1 
HETATM 2465 O  O   . HOH D 3 .   ? -7.88900  -22.53300 56.67300 1.000 37.85996 ? 765 HOH A O   1 
HETATM 2466 O  O   . HOH D 3 .   ? 11.80300  12.83800  86.65800 1.000 38.89996 ? 766 HOH A O   1 
HETATM 2467 O  O   A HOH D 3 .   ? 1.46800   -22.42200 58.93200 0.530 24.54448 ? 767 HOH A O   1 
HETATM 2468 O  O   B HOH D 3 .   ? 0.76900   -23.28700 59.37100 0.470 21.97996 ? 767 HOH A O   1 
HETATM 2469 O  O   . HOH D 3 .   ? -8.79600  23.85500  84.26900 1.000 29.60562 ? 768 HOH A O   1 
HETATM 2470 O  O   . HOH D 3 .   ? 7.55600   -22.79300 74.42500 1.000 45.05996 ? 769 HOH A O   1 
HETATM 2471 O  O   . HOH D 3 .   ? 17.33800  0.96100   58.82400 1.000 39.23996 ? 770 HOH A O   1 
HETATM 2472 O  O   B HOH D 3 .   ? -25.29200 11.53200  87.79500 0.590 27.72381 ? 771 HOH A O   1 
HETATM 2473 O  O   . HOH D 3 .   ? 6.13600   -1.64500  47.42500 1.000 35.06996 ? 772 HOH A O   1 
HETATM 2474 O  O   . HOH D 3 .   ? 7.34200   23.49100  74.16200 1.000 46.77996 ? 773 HOH A O   1 
HETATM 2475 O  O   . HOH D 3 .   ? 7.42100   5.23500   48.65300 1.000 24.31551 ? 774 HOH A O   1 
HETATM 2476 O  O   . HOH D 3 .   ? -4.87700  24.96000  82.88000 1.000 29.62667 ? 775 HOH A O   1 
HETATM 2477 O  O   . HOH D 3 .   ? 8.97400   16.21700  87.32300 1.000 28.84763 ? 776 HOH A O   1 
HETATM 2478 O  O   . HOH D 3 .   ? 2.87500   -25.61900 72.64900 1.000 47.44996 ? 777 HOH A O   1 
HETATM 2479 O  O   . HOH D 3 .   ? 7.70600   -22.72300 66.30000 1.000 20.49400 ? 778 HOH A O   1 
HETATM 2480 O  O   A HOH D 3 .   ? 12.28600  -15.64700 59.39900 0.560 20.58611 ? 779 HOH A O   1 
HETATM 2481 O  O   B HOH D 3 .   ? 12.44300  -16.98100 58.13800 0.440 25.13996 ? 779 HOH A O   1 
HETATM 2482 O  O   . HOH D 3 .   ? 5.92000   10.72100  93.69800 1.000 18.82801 ? 780 HOH A O   1 
HETATM 2483 O  O   . HOH D 3 .   ? 6.93300   22.55500  80.18500 1.000 37.32996 ? 781 HOH A O   1 
HETATM 2484 O  O   . HOH D 3 .   ? 8.65500   22.58900  76.49100 1.000 43.31996 ? 782 HOH A O   1 
HETATM 2485 O  O   . HOH D 3 .   ? -6.14400  21.81400  88.62600 1.000 24.71292 ? 783 HOH A O   1 
HETATM 2486 O  O   . HOH D 3 .   ? 5.27300   -24.23700 66.00500 1.000 40.35996 ? 784 HOH A O   1 
HETATM 2487 O  O   . HOH D 3 .   ? 9.31600   8.00800   50.38800 1.000 32.46996 ? 785 HOH A O   1 
HETATM 2488 O  O   . HOH D 3 .   ? 11.72500  -9.24500  53.07300 1.000 49.07996 ? 786 HOH A O   1 
HETATM 2489 O  O   . HOH D 3 .   ? 11.04300  -20.86000 75.57200 1.000 27.52905 ? 787 HOH A O   1 
HETATM 2490 O  O   . HOH D 3 .   ? 16.76500  -9.95900  60.53600 1.000 22.50476 ? 788 HOH A O   1 
HETATM 2491 O  O   . HOH D 3 .   ? 10.21900  10.72100  91.05100 1.000 29.96618 ? 789 HOH A O   1 
HETATM 2492 O  O   . HOH D 3 .   ? 18.09400  -11.82800 67.00200 1.000 10.49806 ? 790 HOH A O   1 
HETATM 2493 O  O   . HOH D 3 .   ? 10.08600  4.30300   49.47500 1.000 33.11996 ? 791 HOH A O   1 
HETATM 2494 O  O   . HOH D 3 .   ? 8.76800   18.63600  86.20100 1.000 38.09996 ? 792 HOH A O   1 
HETATM 2495 O  O   A HOH D 3 .   ? 11.37100  5.89800   50.60700 0.550 34.81996 ? 793 HOH A O   1 
HETATM 2496 O  O   B HOH D 3 .   ? 12.77800  5.87000   51.33400 0.450 37.46996 ? 793 HOH A O   1 
HETATM 2497 O  O   . HOH D 3 .   ? 13.91400  -5.76900  52.95800 1.000 43.85996 ? 794 HOH A O   1 
HETATM 2498 O  O   . HOH D 3 .   ? 12.63400  -18.36400 61.86100 1.000 20.36767 ? 795 HOH A O   1 
HETATM 2499 O  O   A HOH D 3 .   ? 20.53600  -8.21100  69.50300 0.690 21.34936 ? 796 HOH A O   1 
HETATM 2500 O  O   . HOH D 3 .   ? 9.84600   -20.24700 60.09500 1.000 29.69773 ? 797 HOH A O   1 
HETATM 2501 O  O   . HOH D 3 .   ? 4.71400   13.17400  94.64900 1.000 13.63528 ? 798 HOH A O   1 
HETATM 2502 O  O   . HOH D 3 .   ? 11.74300  12.72600  89.90200 1.000 36.53996 ? 799 HOH A O   1 
HETATM 2503 O  O   A HOH D 3 .   ? 9.84800   15.27100  89.90600 0.570 15.86976 ? 800 HOH A O   1 
HETATM 2504 O  O   B HOH D 3 .   ? 9.18000   15.76900  89.86900 0.430 16.71996 ? 800 HOH A O   1 
HETATM 2505 O  O   . HOH D 3 .   ? 7.46300   17.50200  90.12100 1.000 22.98640 ? 801 HOH A O   1 
HETATM 2506 O  O   A HOH D 3 .   ? 6.06100   21.67900  86.65500 0.490 18.77011 ? 802 HOH A O   1 
HETATM 2507 O  O   B HOH D 3 .   ? 5.76300   21.64700  87.76400 0.510 31.19996 ? 802 HOH A O   1 
HETATM 2508 O  O   . HOH D 3 .   ? 13.07200  -20.57500 63.66700 1.000 13.52211 ? 803 HOH A O   1 
HETATM 2509 O  O   . HOH D 3 .   ? 12.31300  -19.27500 59.30600 1.000 24.13391 ? 804 HOH A O   1 
HETATM 2510 O  O   . HOH D 3 .   ? 8.99200   -24.37700 64.63700 1.000 19.12015 ? 805 HOH A O   1 
HETATM 2511 O  O   . HOH D 3 .   ? 7.75400   -1.34400  45.36900 1.000 36.73996 ? 806 HOH A O   1 
HETATM 2512 O  O   . HOH D 3 .   ? 11.31900  12.45300  95.28000 1.000 21.47833 ? 807 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 
1    N  N   . SER A 1   ? 0.22033 0.18523 0.21073 0.03640  -0.01410 -0.01880 2   SER A N   
2    C  CA  A SER A 1   ? 0.21353 0.16593 0.20573 0.02310  -0.01420 -0.02540 2   SER A CA  
4    C  C   . SER A 1   ? 0.20883 0.16283 0.19253 0.01250  -0.02100 -0.02720 2   SER A C   
5    O  O   . SER A 1   ? 0.22713 0.15433 0.17833 0.01320  -0.00750 -0.02560 2   SER A O   
6    C  CB  A SER A 1   ? 0.17903 0.18503 0.20983 0.00990  -0.01290 -0.03270 2   SER A CB  
8    O  OG  A SER A 1   ? 0.17683 0.19143 0.20433 -0.02260 -0.02650 -0.04070 2   SER A OG  
10   N  N   . LYS A 2   ? 0.19873 0.15363 0.19583 0.01450  -0.01920 -0.01920 3   LYS A N   
11   C  CA  . LYS A 2   ? 0.19783 0.13463 0.17233 0.02270  -0.00660 -0.02570 3   LYS A CA  
12   C  C   . LYS A 2   ? 0.17993 0.10993 0.16343 0.00780  0.00050  -0.01990 3   LYS A C   
13   O  O   . LYS A 2   ? 0.18143 0.14453 0.17373 -0.00950 0.00210  -0.01720 3   LYS A O   
14   C  CB  . LYS A 2   ? 0.19633 0.14403 0.16863 0.01040  -0.00880 -0.02300 3   LYS A CB  
15   C  CG  . LYS A 2   ? 0.19373 0.13013 0.16923 0.02230  -0.00940 -0.03590 3   LYS A CG  
16   C  CD  . LYS A 2   ? 0.21063 0.16103 0.16363 0.01480  -0.00630 -0.04210 3   LYS A CD  
17   C  CE  . LYS A 2   ? 0.20083 0.15383 0.15223 0.01110  -0.01300 -0.03750 3   LYS A CE  
18   N  NZ  . LYS A 2   ? 0.19933 0.15803 0.14943 0.00910  0.00370  -0.01370 3   LYS A NZ  
19   N  N   . GLY A 3   ? 0.18843 0.11793 0.16853 0.00410  -0.00780 -0.00430 4   GLY A N   
20   C  CA  . GLY A 3   ? 0.18493 0.12043 0.16723 -0.00230 -0.01720 -0.02410 4   GLY A CA  
21   C  C   . GLY A 3   ? 0.17923 0.13553 0.15943 0.01130  -0.01970 -0.00710 4   GLY A C   
22   O  O   . GLY A 3   ? 0.21483 0.13213 0.16013 0.01150  -0.02090 -0.00360 4   GLY A O   
23   N  N   . GLU A 4   ? 0.17653 0.15743 0.16133 -0.00330 -0.01490 -0.00440 5   GLU A N   
24   C  CA  A GLU A 4   ? 0.17463 0.15923 0.17233 -0.00580 -0.01790 0.00780  5   GLU A CA  
26   C  C   . GLU A 4   ? 0.16773 0.14183 0.17043 0.01360  -0.00570 -0.01360 5   GLU A C   
27   O  O   . GLU A 4   ? 0.17033 0.15763 0.16923 0.00380  -0.00600 -0.00110 5   GLU A O   
28   C  CB  A GLU A 4   ? 0.19263 0.17633 0.18793 -0.00160 0.00260  0.01190  5   GLU A CB  
30   C  CG  A GLU A 4   ? 0.20323 0.18413 0.18383 -0.00390 0.01070  0.00870  5   GLU A CG  
32   C  CD  A GLU A 4   ? 0.21183 0.19503 0.20733 0.00630  -0.00140 -0.01450 5   GLU A CD  
34   O  OE1 A GLU A 4   ? 0.22383 0.20663 0.22303 0.02450  -0.00390 -0.02880 5   GLU A OE1 
36   O  OE2 A GLU A 4   ? 0.19083 0.19413 0.22443 0.00140  -0.00270 -0.02470 5   GLU A OE2 
38   N  N   . GLU A 5   ? 0.19233 0.11633 0.17213 0.01050  0.01790  -0.02240 6   GLU A N   
39   C  CA  . GLU A 5   ? 0.20993 0.12853 0.17563 -0.01230 0.01470  -0.01210 6   GLU A CA  
40   C  C   . GLU A 5   ? 0.19903 0.11693 0.16553 0.01570  0.01750  -0.00590 6   GLU A C   
41   O  O   . GLU A 5   ? 0.24973 0.11873 0.18423 0.01840  0.00230  0.01370  6   GLU A O   
42   C  CB  . GLU A 5   ? 0.21293 0.14853 0.20363 0.00490  0.00210  -0.03400 6   GLU A CB  
43   C  CG  . GLU A 5   ? 0.22943 0.16373 0.22593 -0.03380 -0.02420 -0.04830 6   GLU A CG  
44   C  CD  . GLU A 5   ? 0.28613 0.19513 0.26353 -0.02460 -0.02240 -0.05190 6   GLU A CD  
45   O  OE1 . GLU A 5   ? 0.33693 0.22593 0.28813 -0.01520 -0.00430 -0.11220 6   GLU A OE1 
46   O  OE2 . GLU A 5   ? 0.32413 0.19173 0.27533 -0.05170 -0.07090 -0.03430 6   GLU A OE2 
47   N  N   . LEU A 6   ? 0.17683 0.12603 0.16523 0.01270  0.00760  -0.02020 7   LEU A N   
48   C  CA  . LEU A 6   ? 0.18313 0.13713 0.16723 0.02320  0.00210  -0.02040 7   LEU A CA  
49   C  C   . LEU A 6   ? 0.18763 0.11583 0.16793 0.01990  0.00240  -0.01530 7   LEU A C   
50   O  O   . LEU A 6   ? 0.19193 0.14473 0.17373 0.00490  -0.00050 -0.00090 7   LEU A O   
51   C  CB  . LEU A 6   ? 0.17963 0.14463 0.16793 0.01290  -0.00510 -0.02490 7   LEU A CB  
52   C  CG  . LEU A 6   ? 0.18933 0.14853 0.17953 -0.00250 -0.02380 -0.01470 7   LEU A CG  
53   C  CD1 . LEU A 6   ? 0.20383 0.18013 0.19593 0.01680  -0.02590 -0.00390 7   LEU A CD1 
54   C  CD2 . LEU A 6   ? 0.22633 0.15943 0.19703 -0.03270 -0.01410 -0.00920 7   LEU A CD2 
55   N  N   . PHE A 7   ? 0.19613 0.12693 0.16863 0.00770  0.00900  -0.02320 8   PHE A N   
56   C  CA  . PHE A 7   ? 0.17843 0.11923 0.16033 0.01430  -0.00430 -0.00810 8   PHE A CA  
57   C  C   . PHE A 7   ? 0.19393 0.12843 0.16523 0.03190  -0.01800 -0.01250 8   PHE A C   
58   O  O   . PHE A 7   ? 0.20933 0.14903 0.17613 0.01760  -0.03820 -0.00540 8   PHE A O   
59   C  CB  . PHE A 7   ? 0.16913 0.12483 0.16973 0.02010  -0.00440 0.00020  8   PHE A CB  
60   C  CG  . PHE A 7   ? 0.14583 0.10313 0.15623 0.01180  -0.00500 -0.00100 8   PHE A CG  
61   C  CD1 . PHE A 7   ? 0.16443 0.10893 0.16053 0.00270  0.00760  -0.00470 8   PHE A CD1 
62   C  CD2 . PHE A 7   ? 0.17123 0.10203 0.16013 0.01480  -0.01780 0.00800  8   PHE A CD2 
63   C  CE1 . PHE A 7   ? 0.17853 0.12123 0.13393 0.00440  -0.01070 0.00780  8   PHE A CE1 
64   C  CE2 . PHE A 7   ? 0.17153 0.10263 0.15343 0.01030  0.01000  0.01620  8   PHE A CE2 
65   C  CZ  . PHE A 7   ? 0.18833 0.10913 0.14223 0.00090  0.00560  0.00550  8   PHE A CZ  
66   N  N   . THR A 8   ? 0.21883 0.13693 0.17173 0.05440  -0.00410 -0.00600 9   THR A N   
67   C  CA  . THR A 8   ? 0.25803 0.14983 0.18283 0.09440  -0.00080 -0.01830 9   THR A CA  
68   C  C   . THR A 8   ? 0.27743 0.13933 0.18283 0.08450  -0.01470 0.00750  9   THR A C   
69   O  O   . THR A 8   ? 0.27843 0.16683 0.18393 0.07670  -0.01590 0.01290  9   THR A O   
70   C  CB  . THR A 8   ? 0.31923 0.20943 0.21313 0.09180  0.00000  -0.02880 9   THR A CB  
71   O  OG1 . THR A 8   ? 0.34633 0.23533 0.26543 0.08420  -0.00670 -0.03760 9   THR A OG1 
72   C  CG2 . THR A 8   ? 0.34673 0.23643 0.19723 0.10470  0.00180  -0.03400 9   THR A CG2 
73   N  N   . GLY A 9   ? 0.28333 0.13163 0.16823 0.07570  -0.00180 -0.00150 10  GLY A N   
74   C  CA  . GLY A 9   ? 0.27033 0.15093 0.16593 0.07950  0.00820  0.00010  10  GLY A CA  
75   C  C   . GLY A 9   ? 0.23693 0.13423 0.16943 0.04760  0.00410  0.00120  10  GLY A C   
76   O  O   . GLY A 9   ? 0.22483 0.12843 0.17353 0.05220  0.01890  0.01860  10  GLY A O   
77   N  N   . VAL A 10  ? 0.24893 0.12643 0.16823 0.04940  0.02340  -0.00150 11  VAL A N   
78   C  CA  . VAL A 10  ? 0.23033 0.13443 0.17543 0.04920  0.02090  -0.00130 11  VAL A CA  
79   C  C   . VAL A 10  ? 0.22453 0.11123 0.19123 0.01520  -0.00040 0.00010  11  VAL A C   
80   O  O   . VAL A 10  ? 0.25613 0.11643 0.24613 0.01110  -0.01200 0.02570  11  VAL A O   
81   C  CB  . VAL A 10  ? 0.24313 0.17143 0.17563 0.07450  0.02590  0.00750  11  VAL A CB  
82   C  CG1 . VAL A 10  ? 0.25523 0.18113 0.17523 0.07830  0.03350  0.00180  11  VAL A CG1 
83   C  CG2 . VAL A 10  ? 0.22973 0.19353 0.18323 0.09140  0.02840  0.00800  11  VAL A CG2 
84   N  N   . VAL A 11  ? 0.18463 0.10393 0.16083 0.02790  0.00590  0.01270  12  VAL A N   
85   C  CA  . VAL A 11  ? 0.18393 0.09803 0.15133 0.02790  0.00560  0.00400  12  VAL A CA  
86   C  C   . VAL A 11  ? 0.18163 0.09123 0.15143 0.00360  0.00720  0.01080  12  VAL A C   
87   O  O   . VAL A 11  ? 0.17783 0.09753 0.15573 0.00310  0.01240  0.01720  12  VAL A O   
88   C  CB  . VAL A 11  ? 0.19103 0.10843 0.13943 0.02250  0.00830  -0.00110 12  VAL A CB  
89   C  CG1 . VAL A 11  ? 0.19883 0.12503 0.13713 0.01180  0.01610  0.01650  12  VAL A CG1 
90   C  CG2 . VAL A 11  ? 0.19743 0.10413 0.16383 0.01180  -0.00310 -0.02290 12  VAL A CG2 
91   N  N   . PRO A 12  ? 0.17873 0.08233 0.16233 -0.00170 0.02340  0.01390  13  PRO A N   
92   C  CA  . PRO A 12  ? 0.17693 0.08393 0.16863 -0.00340 0.02560  0.02200  13  PRO A CA  
93   C  C   . PRO A 12  ? 0.17403 0.07893 0.13513 -0.01000 0.01950  0.02040  13  PRO A C   
94   O  O   . PRO A 12  ? 0.18673 0.09993 0.14293 0.00290  0.00700  0.00230  13  PRO A O   
95   C  CB  . PRO A 12  ? 0.20503 0.10023 0.19843 -0.01020 0.03630  0.01790  13  PRO A CB  
96   C  CG  . PRO A 12  ? 0.23103 0.14453 0.22053 -0.03520 0.05020  -0.00490 13  PRO A CG  
97   C  CD  . PRO A 12  ? 0.19603 0.10223 0.18653 -0.01290 0.03790  0.00940  13  PRO A CD  
98   N  N   . ILE A 13  ? 0.16783 0.08553 0.13283 0.00510  0.00610  0.01630  14  ILE A N   
99   C  CA  . ILE A 13  ? 0.14813 0.08773 0.14463 -0.00490 0.02430  0.01650  14  ILE A CA  
100  C  C   . ILE A 13  ? 0.14253 0.09673 0.13343 -0.01220 0.03780  0.01150  14  ILE A C   
101  O  O   . ILE A 13  ? 0.16853 0.09723 0.13343 -0.01350 0.02750  0.01650  14  ILE A O   
102  C  CB  . ILE A 13  ? 0.13533 0.08413 0.15253 0.00760  0.02140  0.01240  14  ILE A CB  
103  C  CG1 . ILE A 13  ? 0.14163 0.11063 0.15533 0.00100  0.01340  0.02320  14  ILE A CG1 
104  C  CG2 . ILE A 13  ? 0.13723 0.08633 0.16063 -0.00610 0.00100  0.02800  14  ILE A CG2 
105  C  CD1 . ILE A 13  ? 0.13683 0.12023 0.13963 0.00410  0.02740  0.01430  14  ILE A CD1 
106  N  N   . LEU A 14  ? 0.12443 0.09993 0.14533 -0.00460 0.01210  0.00120  15  LEU A N   
107  C  CA  A LEU A 14  ? 0.13143 0.08763 0.14233 -0.00930 0.00440  -0.00560 15  LEU A CA  
109  C  C   . LEU A 14  ? 0.13393 0.08523 0.12303 -0.01460 0.00160  -0.00980 15  LEU A C   
110  O  O   . LEU A 14  ? 0.15063 0.11183 0.12343 -0.00730 0.00570  -0.00100 15  LEU A O   
111  C  CB  A LEU A 14  ? 0.13643 0.09763 0.15233 -0.03250 0.01150  -0.00040 15  LEU A CB  
113  C  CG  A LEU A 14  ? 0.16763 0.11283 0.14243 -0.04870 0.00500  -0.00050 15  LEU A CG  
115  C  CD1 A LEU A 14  ? 0.18873 0.11943 0.15403 -0.05570 0.00720  0.01020  15  LEU A CD1 
117  C  CD2 A LEU A 14  ? 0.18473 0.13643 0.14683 -0.04790 -0.00410 -0.00350 15  LEU A CD2 
119  N  N   . VAL A 15  ? 0.13923 0.07683 0.13253 -0.00010 0.00570  -0.00940 16  VAL A N   
120  C  CA  . VAL A 15  ? 0.15293 0.08073 0.14213 -0.00330 -0.00660 -0.00220 16  VAL A CA  
121  C  C   . VAL A 15  ? 0.15723 0.08643 0.13463 -0.00050 0.00450  -0.00600 16  VAL A C   
122  O  O   . VAL A 15  ? 0.16243 0.10453 0.11773 -0.00270 0.01110  -0.00190 16  VAL A O   
123  C  CB  . VAL A 15  ? 0.14993 0.08723 0.14453 -0.00850 0.00750  -0.00030 16  VAL A CB  
124  C  CG1 . VAL A 15  ? 0.14303 0.09493 0.16303 -0.00530 0.01490  0.01920  16  VAL A CG1 
125  C  CG2 . VAL A 15  ? 0.14273 0.08733 0.16253 0.01140  0.01070  -0.00680 16  VAL A CG2 
126  N  N   . GLU A 16  ? 0.12383 0.09863 0.13803 0.00710  0.01230  -0.00020 17  GLU A N   
127  C  CA  . GLU A 16  ? 0.11713 0.10083 0.14513 -0.03270 0.01410  0.00960  17  GLU A CA  
128  C  C   . GLU A 16  ? 0.12593 0.08883 0.12883 -0.02080 0.02470  0.00030  17  GLU A C   
129  O  O   . GLU A 16  ? 0.21463 0.11103 0.12043 -0.00090 0.03280  0.01010  17  GLU A O   
130  C  CB  . GLU A 16  ? 0.16473 0.12163 0.15463 -0.03700 -0.00080 0.01760  17  GLU A CB  
131  C  CG  . GLU A 16  ? 0.20823 0.15633 0.15953 -0.05880 -0.02590 0.02020  17  GLU A CG  
132  C  CD  . GLU A 16  ? 0.21693 0.19963 0.19953 -0.06920 -0.01460 0.01490  17  GLU A CD  
133  O  OE1 . GLU A 16  ? 0.16433 0.23373 0.20293 -0.07330 0.03940  -0.01420 17  GLU A OE1 
134  O  OE2 . GLU A 16  ? 0.26923 0.19243 0.21763 -0.07270 -0.04270 0.06510  17  GLU A OE2 
135  N  N   . LEU A 17  ? 0.12763 0.09523 0.13813 -0.02120 0.02270  0.00020  18  LEU A N   
136  C  CA  . LEU A 17  ? 0.13023 0.07903 0.14333 -0.01030 0.01460  0.00210  18  LEU A CA  
137  C  C   . LEU A 17  ? 0.12563 0.10133 0.13733 -0.01180 0.01120  0.00090  18  LEU A C   
138  O  O   . LEU A 17  ? 0.14383 0.10883 0.13703 -0.00280 0.02390  0.00310  18  LEU A O   
139  C  CB  . LEU A 17  ? 0.12923 0.09973 0.14873 -0.01150 0.00110  0.00180  18  LEU A CB  
140  C  CG  . LEU A 17  ? 0.12473 0.09873 0.14923 -0.00030 0.02410  0.00360  18  LEU A CG  
141  C  CD1 . LEU A 17  ? 0.15033 0.10803 0.15933 -0.01450 0.01270  0.00580  18  LEU A CD1 
142  C  CD2 . LEU A 17  ? 0.14823 0.11483 0.16613 0.01400  0.02110  -0.02750 18  LEU A CD2 
143  N  N   . ASP A 18  ? 0.10753 0.09963 0.15023 -0.00030 0.00770  0.00280  19  ASP A N   
144  C  CA  A ASP A 18  ? 0.10443 0.11983 0.18343 0.00120  0.01520  0.00750  19  ASP A CA  
146  C  C   . ASP A 18  ? 0.13063 0.10093 0.15173 0.00220  0.03520  -0.00060 19  ASP A C   
147  O  O   . ASP A 18  ? 0.15443 0.11183 0.15543 -0.01200 0.03740  -0.00490 19  ASP A O   
148  C  CB  A ASP A 18  ? 0.12643 0.17183 0.22683 -0.00380 0.01980  0.01760  19  ASP A CB  
150  C  CG  A ASP A 18  ? 0.18033 0.22383 0.25633 -0.00150 0.02490  0.00770  19  ASP A CG  
152  O  OD1 A ASP A 18  ? 0.20503 0.24923 0.26093 0.02310  0.02750  -0.00860 19  ASP A OD1 
154  O  OD2 A ASP A 18  ? 0.20313 0.25173 0.28413 0.00380  0.03420  0.01740  19  ASP A OD2 
156  N  N   . GLY A 19  ? 0.14893 0.08913 0.15853 -0.00900 0.02270  -0.01920 20  GLY A N   
157  C  CA  . GLY A 19  ? 0.14793 0.10483 0.17243 -0.01000 0.01860  -0.02200 20  GLY A CA  
158  C  C   . GLY A 19  ? 0.12443 0.11183 0.15253 -0.00680 0.01630  -0.00240 20  GLY A C   
159  O  O   . GLY A 19  ? 0.12473 0.12733 0.16253 0.01210  0.02260  -0.00030 20  GLY A O   
160  N  N   . ASP A 20  ? 0.12633 0.10533 0.15233 0.00650  0.01100  -0.00340 21  ASP A N   
161  C  CA  A ASP A 20  ? 0.09733 0.11463 0.15163 0.02530  0.00780  -0.00140 21  ASP A CA  
163  C  C   . ASP A 20  ? 0.11753 0.09823 0.14413 0.03270  0.01880  -0.01180 21  ASP A C   
164  O  O   . ASP A 20  ? 0.13793 0.11233 0.13883 0.01240  0.02830  -0.00550 21  ASP A O   
165  C  CB  A ASP A 20  ? 0.10233 0.14223 0.14403 0.02950  -0.00670 -0.01310 21  ASP A CB  
167  C  CG  A ASP A 20  ? 0.09513 0.12993 0.17153 0.03130  0.00210  -0.02220 21  ASP A CG  
169  O  OD1 A ASP A 20  ? 0.10983 0.13123 0.19163 0.00770  0.00050  -0.00760 21  ASP A OD1 
171  O  OD2 A ASP A 20  ? 0.13603 0.12233 0.20763 0.01420  -0.00010 0.00040  21  ASP A OD2 
173  N  N   . VAL A 21  ? 0.12873 0.08453 0.15113 0.02630  0.00360  -0.01010 22  VAL A N   
174  C  CA  . VAL A 21  ? 0.11513 0.09363 0.16113 0.03800  0.01570  0.00420  22  VAL A CA  
175  C  C   . VAL A 21  ? 0.10503 0.10033 0.14963 0.02470  0.01800  0.01230  22  VAL A C   
176  O  O   . VAL A 21  ? 0.10053 0.10293 0.15203 0.02500  0.01120  0.00670  22  VAL A O   
177  C  CB  . VAL A 21  ? 0.11913 0.09463 0.17083 0.03990  0.00680  0.00890  22  VAL A CB  
178  C  CG1 . VAL A 21  ? 0.12923 0.11093 0.19273 0.01550  -0.00410 -0.00100 22  VAL A CG1 
179  C  CG2 . VAL A 21  ? 0.13073 0.10603 0.17283 0.04070  0.02670  0.00720  22  VAL A CG2 
180  N  N   . ASN A 22  ? 0.11893 0.08673 0.15703 0.01410  0.01930  -0.00880 23  ASN A N   
181  C  CA  . ASN A 22  ? 0.11053 0.09373 0.17603 0.01460  0.00720  -0.00520 23  ASN A CA  
182  C  C   . ASN A 22  ? 0.11533 0.11763 0.15893 0.02390  0.01800  -0.00020 23  ASN A C   
183  O  O   . ASN A 22  ? 0.13833 0.12703 0.16313 0.03590  0.01550  0.00130  23  ASN A O   
184  C  CB  . ASN A 22  ? 0.12513 0.09813 0.18873 -0.00590 0.00570  -0.00050 23  ASN A CB  
185  C  CG  . ASN A 22  ? 0.12413 0.10753 0.16783 0.00330  0.00380  -0.01160 23  ASN A CG  
186  O  OD1 . ASN A 22  ? 0.13483 0.11863 0.15723 0.00080  0.01790  -0.00470 23  ASN A OD1 
187  N  ND2 . ASN A 22  ? 0.13813 0.11883 0.17573 0.00240  -0.00070 -0.02170 23  ASN A ND2 
188  N  N   . GLY A 23  ? 0.09923 0.12073 0.16913 0.01560  0.01080  0.01090  24  GLY A N   
189  C  CA  . GLY A 23  ? 0.11603 0.13543 0.16633 0.02850  0.01670  0.00840  24  GLY A CA  
190  C  C   . GLY A 23  ? 0.10693 0.10873 0.15183 0.01760  0.00740  0.01010  24  GLY A C   
191  O  O   . GLY A 23  ? 0.10293 0.12423 0.13203 0.00900  0.00730  0.00150  24  GLY A O   
192  N  N   . HIS A 24  ? 0.12583 0.11743 0.13743 0.02380  0.01320  -0.00770 25  HIS A N   
193  C  CA  . HIS A 24  ? 0.15113 0.11463 0.13363 0.01770  0.00140  -0.00530 25  HIS A CA  
194  C  C   . HIS A 24  ? 0.15263 0.12433 0.13633 0.03440  0.00960  -0.00030 25  HIS A C   
195  O  O   . HIS A 24  ? 0.16023 0.13183 0.12823 0.03850  0.01860  0.00870  25  HIS A O   
196  C  CB  . HIS A 24  ? 0.13863 0.13503 0.15453 0.01750  0.00210  -0.00980 25  HIS A CB  
197  C  CG  . HIS A 24  ? 0.14763 0.14213 0.14813 0.03430  0.01980  -0.02550 25  HIS A CG  
198  N  ND1 . HIS A 24  ? 0.17423 0.17243 0.16583 0.03310  -0.00740 -0.03660 25  HIS A ND1 
199  C  CD2 . HIS A 24  ? 0.18873 0.15653 0.15643 0.01380  0.00030  -0.03190 25  HIS A CD2 
200  C  CE1 . HIS A 24  ? 0.18853 0.17223 0.17693 0.01400  0.00160  -0.04460 25  HIS A CE1 
201  N  NE2 . HIS A 24  ? 0.19543 0.17483 0.16173 0.01400  -0.00370 -0.05560 25  HIS A NE2 
202  N  N   . LYS A 25  ? 0.16163 0.12163 0.15353 0.00710  0.01980  -0.01340 26  LYS A N   
203  C  CA  . LYS A 25  ? 0.16413 0.12393 0.15723 -0.01260 0.02100  -0.00810 26  LYS A CA  
204  C  C   . LYS A 25  ? 0.18433 0.13533 0.15593 0.02100  0.05180  0.00450  26  LYS A C   
205  O  O   . LYS A 25  ? 0.25123 0.16003 0.16723 0.05380  0.05280  0.01710  26  LYS A O   
206  C  CB  . LYS A 25  ? 0.15893 0.13873 0.17273 -0.00670 0.00880  0.00580  26  LYS A CB  
207  C  CG  . LYS A 25  ? 0.14023 0.21143 0.20413 -0.00270 -0.00470 0.01040  26  LYS A CG  
208  C  CD  . LYS A 25  ? 0.18193 0.29873 0.24493 -0.03090 0.01320  -0.00130 26  LYS A CD  
209  C  CE  . LYS A 25  ? 0.20353 0.32253 0.26813 -0.05360 0.00430  0.00810  26  LYS A CE  
210  N  NZ  . LYS A 25  ? 0.17073 0.31583 0.25653 -0.08320 -0.02340 -0.02200 26  LYS A NZ  
211  N  N   . PHE A 26  ? 0.16263 0.12263 0.15353 0.00920  0.03430  0.00220  27  PHE A N   
212  C  CA  . PHE A 26  ? 0.15233 0.11993 0.13643 0.00260  0.00480  0.00120  27  PHE A CA  
213  C  C   . PHE A 26  ? 0.14173 0.12033 0.13253 0.00470  0.01860  0.00480  27  PHE A C   
214  O  O   . PHE A 26  ? 0.17403 0.12023 0.13693 0.00270  0.01590  -0.00590 27  PHE A O   
215  C  CB  . PHE A 26  ? 0.17483 0.12583 0.13743 -0.00490 0.00910  -0.01370 27  PHE A CB  
216  C  CG  . PHE A 26  ? 0.15813 0.12833 0.13783 0.01040  0.00390  0.00030  27  PHE A CG  
217  C  CD1 . PHE A 26  ? 0.14333 0.14393 0.13533 0.00040  -0.01020 0.02240  27  PHE A CD1 
218  C  CD2 . PHE A 26  ? 0.13653 0.14333 0.13913 0.01700  -0.01720 -0.00650 27  PHE A CD2 
219  C  CE1 . PHE A 26  ? 0.10333 0.14083 0.15543 -0.00510 -0.00430 -0.00790 27  PHE A CE1 
220  C  CE2 . PHE A 26  ? 0.14393 0.13513 0.15443 0.01600  -0.03240 -0.02220 27  PHE A CE2 
221  C  CZ  . PHE A 26  ? 0.14293 0.13473 0.16703 0.02440  -0.01990 -0.01860 27  PHE A CZ  
222  N  N   . SER A 27  ? 0.13563 0.10153 0.15343 -0.00020 0.02180  -0.00100 28  SER A N   
223  C  CA  . SER A 27  ? 0.13403 0.09713 0.18303 0.01380  0.01880  0.00940  28  SER A CA  
224  C  C   . SER A 27  ? 0.14333 0.10283 0.15743 0.00740  0.01580  -0.00250 28  SER A C   
225  O  O   . SER A 27  ? 0.16843 0.13603 0.14643 0.00920  0.03030  -0.00380 28  SER A O   
226  C  CB  . SER A 27  ? 0.13233 0.13793 0.22403 0.00030  -0.00610 0.00930  28  SER A CB  
227  O  OG  . SER A 27  ? 0.16033 0.15563 0.25373 0.00050  -0.02700 -0.00020 28  SER A OG  
228  N  N   . VAL A 28  ? 0.12233 0.09033 0.14543 0.00570  0.00790  -0.00210 29  VAL A N   
229  C  CA  . VAL A 28  ? 0.12553 0.10133 0.14363 -0.00090 0.01350  -0.00010 29  VAL A CA  
230  C  C   . VAL A 28  ? 0.13213 0.11823 0.12603 0.00110  0.01040  0.00280  29  VAL A C   
231  O  O   . VAL A 28  ? 0.16123 0.12973 0.12133 -0.01290 0.00210  -0.00000 29  VAL A O   
232  C  CB  . VAL A 28  ? 0.12333 0.10463 0.15503 -0.00660 0.00900  0.00460  29  VAL A CB  
233  C  CG1 . VAL A 28  ? 0.12303 0.13193 0.14113 0.00780  0.01250  0.01440  29  VAL A CG1 
234  C  CG2 . VAL A 28  ? 0.15883 0.09203 0.16233 -0.03100 0.01250  -0.01270 29  VAL A CG2 
235  N  N   . SER A 29  ? 0.14703 0.10653 0.13773 -0.00560 0.01240  -0.00430 30  SER A N   
236  C  CA  A SER A 29  ? 0.14793 0.10293 0.14323 -0.00630 0.00540  -0.00470 30  SER A CA  
238  C  C   . SER A 29  ? 0.16003 0.11233 0.14323 0.02200  -0.00380 -0.01780 30  SER A C   
239  O  O   . SER A 29  ? 0.20323 0.18233 0.17813 0.05950  -0.02230 -0.06150 30  SER A O   
240  C  CB  A SER A 29  ? 0.14093 0.12273 0.13073 -0.02740 0.00790  0.01380  30  SER A CB  
242  O  OG  A SER A 29  ? 0.14083 0.12403 0.13463 -0.01730 0.02690  -0.00030 30  SER A OG  
244  N  N   . GLY A 30  ? 0.13873 0.10933 0.13463 0.00270  0.00210  -0.00060 31  GLY A N   
245  C  CA  . GLY A 30  ? 0.15243 0.10553 0.13883 0.00540  0.00220  -0.00020 31  GLY A CA  
246  C  C   . GLY A 30  ? 0.14653 0.10763 0.12423 -0.00120 0.01490  -0.00520 31  GLY A C   
247  O  O   . GLY A 30  ? 0.16353 0.10163 0.11213 -0.01490 0.01500  0.00350  31  GLY A O   
248  N  N   . GLU A 31  ? 0.13793 0.08973 0.13823 0.00210  0.02490  0.01190  32  GLU A N   
249  C  CA  A GLU A 31  ? 0.14033 0.09043 0.13993 0.02220  0.02500  0.02610  32  GLU A CA  
251  C  C   . GLU A 31  ? 0.14623 0.09323 0.14673 0.00470  0.02030  -0.01270 32  GLU A C   
252  O  O   . GLU A 31  ? 0.15923 0.10273 0.17213 -0.00160 0.00840  -0.01540 32  GLU A O   
253  C  CB  A GLU A 31  ? 0.14583 0.10993 0.14273 -0.00260 0.01830  0.03000  32  GLU A CB  
255  C  CG  A GLU A 31  ? 0.15643 0.13583 0.14003 -0.01110 0.04090  0.01100  32  GLU A CG  
257  C  CD  A GLU A 31  ? 0.18193 0.14243 0.15113 -0.02280 0.02930  -0.00560 32  GLU A CD  
259  O  OE1 A GLU A 31  ? 0.20163 0.14273 0.15763 -0.02000 0.01250  0.01330  32  GLU A OE1 
261  O  OE2 A GLU A 31  ? 0.18233 0.15633 0.14423 -0.04320 0.03380  -0.00580 32  GLU A OE2 
263  N  N   . GLY A 32  ? 0.16183 0.09623 0.15693 0.00660  0.01690  -0.02380 33  GLY A N   
264  C  CA  . GLY A 32  ? 0.16093 0.12413 0.15923 0.02410  0.01170  -0.02010 33  GLY A CA  
265  C  C   . GLY A 32  ? 0.15693 0.10733 0.14233 0.02500  0.02310  -0.00540 33  GLY A C   
266  O  O   . GLY A 32  ? 0.16973 0.10703 0.13443 0.00270  0.01370  0.01160  33  GLY A O   
267  N  N   . GLU A 33  ? 0.15913 0.11723 0.12913 0.03480  0.03040  -0.00320 34  GLU A N   
268  C  CA  . GLU A 33  ? 0.17903 0.13073 0.14813 0.02020  0.03440  0.00580  34  GLU A CA  
269  C  C   . GLU A 33  ? 0.15213 0.10663 0.13603 0.03480  0.02540  -0.01240 34  GLU A C   
270  O  O   . GLU A 33  ? 0.16253 0.13833 0.12903 0.00850  0.01610  -0.01690 34  GLU A O   
271  C  CB  . GLU A 33  ? 0.22293 0.18413 0.18963 0.04780  0.02700  0.03440  34  GLU A CB  
272  C  CG  . GLU A 33  ? 0.22673 0.20373 0.22943 0.07030  0.01230  0.04010  34  GLU A CG  
273  C  CD  . GLU A 33  ? 0.26633 0.24853 0.26563 0.06400  0.01260  0.04110  34  GLU A CD  
274  O  OE1 . GLU A 33  ? 0.30683 0.26963 0.27393 0.06050  0.04000  0.06600  34  GLU A OE1 
275  O  OE2 . GLU A 33  ? 0.27993 0.26053 0.28433 0.05270  -0.00880 0.05050  34  GLU A OE2 
276  N  N   . GLY A 34  ? 0.13933 0.10133 0.13673 0.02000  0.01670  -0.00590 35  GLY A N   
277  C  CA  . GLY A 34  ? 0.14853 0.11613 0.14523 0.02860  0.01130  -0.00060 35  GLY A CA  
278  C  C   . GLY A 34  ? 0.16253 0.11843 0.14033 0.02340  0.01570  0.01130  35  GLY A C   
279  O  O   . GLY A 34  ? 0.17053 0.11403 0.15043 0.01320  0.02040  0.00480  35  GLY A O   
280  N  N   . ASP A 35  ? 0.15203 0.13863 0.15373 0.04630  0.03020  0.00220  36  ASP A N   
281  C  CA  . ASP A 35  ? 0.16573 0.15123 0.16863 0.04750  0.03650  -0.00050 36  ASP A CA  
282  C  C   . ASP A 35  ? 0.16923 0.12403 0.16583 0.03260  0.01740  0.00380  36  ASP A C   
283  O  O   . ASP A 35  ? 0.17833 0.14543 0.16143 0.02270  0.02430  -0.00110 36  ASP A O   
284  C  CB  . ASP A 35  ? 0.22483 0.17573 0.17713 0.06710  0.01560  0.01430  36  ASP A CB  
285  C  CG  . ASP A 35  ? 0.25443 0.21113 0.17433 0.08340  0.01610  0.00300  36  ASP A CG  
286  O  OD1 . ASP A 35  ? 0.27103 0.21923 0.18283 0.07990  0.01550  -0.03100 36  ASP A OD1 
287  O  OD2 . ASP A 35  ? 0.26353 0.24263 0.19193 0.07700  -0.00150 0.01610  36  ASP A OD2 
288  N  N   . ALA A 36  ? 0.14303 0.11773 0.15513 0.04720  -0.00090 0.00270  37  ALA A N   
289  C  CA  . ALA A 36  ? 0.17403 0.10853 0.14773 0.04600  -0.01050 -0.00340 37  ALA A CA  
290  C  C   . ALA A 36  ? 0.17993 0.12283 0.14783 0.04250  -0.01750 0.00240  37  ALA A C   
291  O  O   . ALA A 36  ? 0.17203 0.14953 0.14973 0.03000  -0.00560 0.00600  37  ALA A O   
292  C  CB  . ALA A 36  ? 0.18813 0.14233 0.14573 0.04020  -0.02900 0.00590  37  ALA A CB  
293  N  N   . THR A 37  ? 0.17293 0.11593 0.13653 0.06290  -0.01420 -0.01200 38  THR A N   
294  C  CA  . THR A 37  ? 0.18793 0.12913 0.15503 0.05030  -0.00620 0.00400  38  THR A CA  
295  C  C   . THR A 37  ? 0.18843 0.15573 0.16223 0.03940  -0.00730 0.00630  38  THR A C   
296  O  O   . THR A 37  ? 0.18483 0.15283 0.17513 0.03840  0.01260  -0.00450 38  THR A O   
297  C  CB  . THR A 37  ? 0.20613 0.13613 0.19603 0.05700  -0.01030 0.00950  38  THR A CB  
298  O  OG1 . THR A 37  ? 0.21103 0.13423 0.20963 0.04680  -0.00470 0.00680  38  THR A OG1 
299  C  CG2 . THR A 37  ? 0.20553 0.15953 0.19793 0.08240  -0.00350 0.01310  38  THR A CG2 
300  N  N   . TYR A 38  ? 0.18953 0.16143 0.14823 0.04550  -0.02140 -0.02260 39  TYR A N   
301  C  CA  . TYR A 38  ? 0.18703 0.18013 0.15633 0.04470  -0.02230 -0.02380 39  TYR A CA  
302  C  C   . TYR A 38  ? 0.16663 0.17143 0.16333 0.02800  -0.00500 -0.03030 39  TYR A C   
303  O  O   . TYR A 38  ? 0.16713 0.19673 0.19733 0.02710  0.00040  -0.02880 39  TYR A O   
304  C  CB  . TYR A 38  ? 0.23083 0.20063 0.15953 0.06240  -0.01150 -0.02550 39  TYR A CB  
305  C  CG  . TYR A 38  ? 0.23263 0.21913 0.16403 0.07790  -0.02880 -0.00470 39  TYR A CG  
306  C  CD1 . TYR A 38  ? 0.24313 0.23673 0.17613 0.08230  -0.05160 -0.01190 39  TYR A CD1 
307  C  CD2 . TYR A 38  ? 0.24973 0.20543 0.18173 0.08750  -0.00760 0.01590  39  TYR A CD2 
308  C  CE1 . TYR A 38  ? 0.25313 0.24613 0.18813 0.10730  -0.03930 -0.00050 39  TYR A CE1 
309  C  CE2 . TYR A 38  ? 0.26473 0.21293 0.19473 0.09970  -0.00500 0.02240  39  TYR A CE2 
310  C  CZ  . TYR A 38  ? 0.27153 0.24033 0.19493 0.12400  -0.01260 0.01180  39  TYR A CZ  
311  O  OH  . TYR A 38  ? 0.30653 0.25963 0.20613 0.14670  0.02100  0.01100  39  TYR A OH  
312  N  N   . GLY A 39  ? 0.16713 0.16863 0.15383 0.04290  -0.00570 -0.00530 40  GLY A N   
313  C  CA  . GLY A 39  ? 0.16703 0.15203 0.14813 0.04030  -0.00030 -0.00260 40  GLY A CA  
314  C  C   . GLY A 39  ? 0.15533 0.13453 0.14303 0.02060  -0.00690 -0.00920 40  GLY A C   
315  O  O   . GLY A 39  ? 0.14933 0.14013 0.15263 0.01220  -0.00520 -0.00830 40  GLY A O   
316  N  N   . LYS A 40  ? 0.14273 0.14323 0.13723 0.02050  -0.00240 -0.00110 41  LYS A N   
317  C  CA  A LYS A 40  ? 0.14713 0.14913 0.14753 0.04080  -0.00020 0.01240  41  LYS A CA  
319  C  C   . LYS A 40  ? 0.14263 0.12793 0.15453 0.01970  -0.00800 0.01870  41  LYS A C   
320  O  O   . LYS A 40  ? 0.15563 0.14393 0.19903 0.02690  0.00620  -0.00910 41  LYS A O   
321  C  CB  A LYS A 40  ? 0.16293 0.17863 0.14503 0.05770  -0.00690 0.03670  41  LYS A CB  
323  C  CG  A LYS A 40  ? 0.18023 0.20683 0.13913 0.03680  -0.02320 0.05760  41  LYS A CG  
325  C  CD  A LYS A 40  ? 0.20603 0.24533 0.14433 0.01190  -0.01410 0.07290  41  LYS A CD  
327  C  CE  A LYS A 40  ? 0.21363 0.27373 0.15353 0.01100  -0.01580 0.06970  41  LYS A CE  
329  N  NZ  A LYS A 40  ? 0.21443 0.28803 0.17143 0.02230  -0.01040 0.05530  41  LYS A NZ  
331  N  N   A LEU A 41  ? 0.14143 0.14483 0.14233 0.02450  0.00860  0.00970  42  LEU A N   
333  C  CA  A LEU A 41  ? 0.15623 0.14833 0.13363 0.02000  -0.00610 0.00780  42  LEU A CA  
335  C  C   A LEU A 41  ? 0.14413 0.12713 0.12383 0.01610  -0.00190 0.00760  42  LEU A C   
337  O  O   A LEU A 41  ? 0.14953 0.14143 0.12163 -0.00600 0.00130  0.01320  42  LEU A O   
339  C  CB  A LEU A 41  ? 0.18573 0.12163 0.13963 -0.00940 -0.00500 0.00540  42  LEU A CB  
341  C  CG  A LEU A 41  ? 0.20123 0.13853 0.15023 -0.02180 -0.00550 0.00970  42  LEU A CG  
343  C  CD1 A LEU A 41  ? 0.23603 0.15633 0.16003 -0.04330 -0.02230 0.00670  42  LEU A CD1 
345  C  CD2 A LEU A 41  ? 0.18943 0.14793 0.15063 -0.02070 -0.01070 0.00700  42  LEU A CD2 
347  N  N   . THR A 42  ? 0.14453 0.12933 0.11723 0.02650  0.02080  0.01540  43  THR A N   
348  C  CA  A THR A 42  ? 0.16463 0.14153 0.12783 0.03310  0.02350  0.00910  43  THR A CA  
350  C  C   . THR A 42  ? 0.13923 0.12773 0.14203 0.00340  0.01940  -0.00580 43  THR A C   
351  O  O   . THR A 42  ? 0.16413 0.11323 0.18163 -0.00430 0.02800  -0.01710 43  THR A O   
352  C  CB  A THR A 42  ? 0.19903 0.16813 0.14963 0.04050  0.00350  0.01740  43  THR A CB  
354  O  OG1 A THR A 42  ? 0.21083 0.19253 0.16603 0.03410  -0.02800 0.04440  43  THR A OG1 
356  C  CG2 A THR A 42  ? 0.22913 0.19883 0.15503 0.04180  0.01860  0.01770  43  THR A CG2 
358  N  N   . LEU A 43  ? 0.13463 0.13183 0.14003 0.02950  0.02880  -0.01140 44  LEU A N   
359  C  CA  . LEU A 43  ? 0.16053 0.11793 0.12793 0.02180  0.02470  -0.00940 44  LEU A CA  
360  C  C   . LEU A 43  ? 0.15103 0.11323 0.12873 -0.00470 0.01080  0.00150  44  LEU A C   
361  O  O   . LEU A 43  ? 0.16203 0.14373 0.17183 -0.01490 0.02650  -0.02260 44  LEU A O   
362  C  CB  . LEU A 43  ? 0.19013 0.12883 0.11223 0.00960  0.02640  -0.01390 44  LEU A CB  
363  C  CG  . LEU A 43  ? 0.24403 0.12913 0.12113 -0.00580 0.03570  0.00180  44  LEU A CG  
364  C  CD1 . LEU A 43  ? 0.31613 0.15323 0.13423 0.01220  0.04700  0.01710  44  LEU A CD1 
365  C  CD2 . LEU A 43  ? 0.25333 0.15343 0.13693 -0.02080 -0.00250 -0.02730 44  LEU A CD2 
366  N  N   . LYS A 44  ? 0.14623 0.12333 0.11183 0.01280  0.01290  0.00450  45  LYS A N   
367  C  CA  . LYS A 44  ? 0.14823 0.11853 0.12943 0.00980  0.01730  -0.00210 45  LYS A CA  
368  C  C   . LYS A 44  ? 0.15183 0.11263 0.12753 -0.00090 0.01430  0.00020  45  LYS A C   
369  O  O   . LYS A 44  ? 0.15023 0.11153 0.13073 -0.01270 0.00800  -0.00310 45  LYS A O   
370  C  CB  . LYS A 44  ? 0.17363 0.11793 0.12973 0.00170  0.03980  -0.00090 45  LYS A CB  
371  C  CG  . LYS A 44  ? 0.19113 0.12223 0.11333 0.01340  0.04400  0.00470  45  LYS A CG  
372  C  CD  . LYS A 44  ? 0.25463 0.13843 0.12563 0.01630  0.04820  0.00390  45  LYS A CD  
373  C  CE  . LYS A 44  ? 0.27853 0.15233 0.12173 -0.01450 0.06560  0.00540  45  LYS A CE  
374  N  NZ  . LYS A 44  ? 0.28983 0.16013 0.15203 -0.01910 0.07170  0.00270  45  LYS A NZ  
375  N  N   . PHE A 45  ? 0.14613 0.11333 0.11453 0.00230  0.00790  0.01890  46  PHE A N   
376  C  CA  . PHE A 45  ? 0.14493 0.10243 0.12813 0.00580  0.02280  0.01180  46  PHE A CA  
377  C  C   . PHE A 45  ? 0.13433 0.10113 0.13073 0.00020  0.02710  -0.00600 46  PHE A C   
378  O  O   . PHE A 45  ? 0.14903 0.12933 0.13483 -0.01400 0.02050  -0.01240 46  PHE A O   
379  C  CB  . PHE A 45  ? 0.14663 0.09393 0.12543 -0.00440 0.02450  -0.00190 46  PHE A CB  
380  C  CG  . PHE A 45  ? 0.14463 0.09313 0.12183 0.00570  0.01930  0.00720  46  PHE A CG  
381  C  CD1 . PHE A 45  ? 0.15463 0.08953 0.11823 -0.00460 0.01410  0.01490  46  PHE A CD1 
382  C  CD2 . PHE A 45  ? 0.15113 0.09933 0.14343 0.01290  0.01700  0.00500  46  PHE A CD2 
383  C  CE1 . PHE A 45  ? 0.16733 0.10503 0.11843 0.01030  0.00450  0.01870  46  PHE A CE1 
384  C  CE2 . PHE A 45  ? 0.16463 0.12513 0.13633 0.01550  0.01820  0.02410  46  PHE A CE2 
385  C  CZ  . PHE A 45  ? 0.16223 0.12453 0.12903 0.01350  0.01930  0.02140  46  PHE A CZ  
386  N  N   . ILE A 46  ? 0.12823 0.11333 0.14133 0.00220  0.03240  -0.00940 47  ILE A N   
387  C  CA  . ILE A 46  ? 0.12823 0.11303 0.14783 -0.00230 0.01630  0.00880  47  ILE A CA  
388  C  C   . ILE A 46  ? 0.13263 0.10303 0.14093 -0.02560 0.01740  -0.00810 47  ILE A C   
389  O  O   . ILE A 46  ? 0.14123 0.12313 0.13913 -0.00500 0.01800  -0.00790 47  ILE A O   
390  C  CB  . ILE A 46  ? 0.14213 0.11823 0.16313 -0.00950 0.02470  0.01580  47  ILE A CB  
391  C  CG1 . ILE A 46  ? 0.17293 0.11733 0.18793 -0.01300 0.00050  0.03210  47  ILE A CG1 
392  C  CG2 . ILE A 46  ? 0.17553 0.13943 0.15603 -0.01410 0.02270  -0.00730 47  ILE A CG2 
393  C  CD1 . ILE A 46  ? 0.19863 0.15323 0.19313 -0.03050 0.01330  0.01840  47  ILE A CD1 
394  N  N   . CYS A 47  ? 0.14673 0.10323 0.14693 0.00160  0.03200  -0.00180 48  CYS A N   
395  C  CA  . CYS A 47  ? 0.14593 0.12033 0.14673 -0.00840 0.03240  -0.00910 48  CYS A CA  
396  C  C   . CYS A 47  ? 0.16173 0.15003 0.14743 -0.00890 0.03150  0.00150  48  CYS A C   
397  O  O   . CYS A 47  ? 0.16423 0.18943 0.14803 -0.01300 0.03120  -0.01970 48  CYS A O   
398  C  CB  . CYS A 47  ? 0.15543 0.12183 0.16893 -0.00180 0.01390  -0.00640 48  CYS A CB  
399  S  SG  . CYS A 47  ? 0.15423 0.12353 0.18523 0.01310  0.02010  -0.00450 48  CYS A SG  
400  N  N   . THR A 48  ? 0.15223 0.14703 0.17593 -0.02960 0.02930  0.00480  49  THR A N   
401  C  CA  . THR A 48  ? 0.16663 0.15943 0.19063 -0.02610 0.02890  -0.01490 49  THR A CA  
402  C  C   . THR A 48  ? 0.16013 0.17413 0.19473 -0.00580 0.04510  0.00800  49  THR A C   
403  O  O   . THR A 48  ? 0.20183 0.21423 0.23833 -0.00920 0.07720  0.02100  49  THR A O   
404  C  CB  . THR A 48  ? 0.19423 0.15843 0.20213 -0.02690 0.00960  -0.01270 49  THR A CB  
405  O  OG1 . THR A 48  ? 0.22043 0.18353 0.19123 -0.03440 0.01450  -0.01650 49  THR A OG1 
406  C  CG2 . THR A 48  ? 0.20483 0.14513 0.23133 -0.01530 0.02480  -0.01370 49  THR A CG2 
407  N  N   . THR A 49  ? 0.17343 0.17783 0.18183 0.01190  0.03460  -0.00560 50  THR A N   
408  C  CA  . THR A 49  ? 0.19353 0.17833 0.18733 0.03060  0.02970  -0.00000 50  THR A CA  
409  C  C   . THR A 49  ? 0.23183 0.20083 0.18993 0.02610  0.03870  -0.01750 50  THR A C   
410  O  O   . THR A 49  ? 0.30613 0.24183 0.21193 0.05970  0.03480  -0.03770 50  THR A O   
411  C  CB  . THR A 49  ? 0.18203 0.19923 0.17923 0.01710  0.03810  0.00140  50  THR A CB  
412  O  OG1 . THR A 49  ? 0.19013 0.18963 0.16403 0.02710  0.05350  0.01300  50  THR A OG1 
413  C  CG2 . THR A 49  ? 0.18823 0.20763 0.20033 0.01800  0.03180  0.00340  50  THR A CG2 
414  N  N   . GLY A 50  ? 0.20923 0.19393 0.19453 -0.01390 0.03850  -0.01490 51  GLY A N   
415  C  CA  . GLY A 50  ? 0.20003 0.19313 0.20213 -0.02600 0.05380  -0.02410 51  GLY A CA  
416  C  C   . GLY A 50  ? 0.20873 0.17903 0.20423 -0.00560 0.06770  -0.02770 51  GLY A C   
417  O  O   . GLY A 50  ? 0.22003 0.18743 0.22603 -0.00110 0.06510  -0.01840 51  GLY A O   
418  N  N   . LYS A 51  ? 0.21433 0.16893 0.21003 -0.00580 0.06410  -0.03400 52  LYS A N   
419  C  CA  . LYS A 51  ? 0.23923 0.19573 0.21783 -0.00640 0.08900  -0.03910 52  LYS A CA  
420  C  C   . LYS A 51  ? 0.20193 0.14783 0.19473 0.01980  0.04880  -0.01910 52  LYS A C   
421  O  O   . LYS A 51  ? 0.17933 0.17113 0.20583 0.03230  0.04520  0.01070  52  LYS A O   
422  C  CB  . LYS A 51  ? 0.30593 0.27623 0.28033 -0.02530 0.10870  -0.07290 52  LYS A CB  
423  C  CG  . LYS A 51  ? 0.40183 0.38133 0.38263 -0.04430 0.11090  -0.08810 52  LYS A CG  
427  N  N   . LEU A 52  ? 0.19743 0.14713 0.16333 0.01120  0.05060  -0.01490 53  LEU A N   
428  C  CA  . LEU A 52  ? 0.15573 0.12383 0.16093 0.01620  0.03460  -0.00430 53  LEU A CA  
429  C  C   . LEU A 52  ? 0.13063 0.12603 0.17023 0.01370  0.01980  -0.01440 53  LEU A C   
430  O  O   . LEU A 52  ? 0.16253 0.13923 0.18373 0.01490  0.00400  -0.02960 53  LEU A O   
431  C  CB  . LEU A 52  ? 0.14533 0.13143 0.14083 0.01630  0.01050  -0.00980 53  LEU A CB  
432  C  CG  . LEU A 52  ? 0.11983 0.12433 0.14243 0.00570  0.01150  -0.01870 53  LEU A CG  
433  C  CD1 . LEU A 52  ? 0.11623 0.12853 0.17003 -0.01410 -0.00150 -0.01030 53  LEU A CD1 
434  C  CD2 . LEU A 52  ? 0.13703 0.13493 0.13863 -0.01190 -0.00070 -0.01630 53  LEU A CD2 
435  N  N   . PRO A 53  ? 0.13423 0.13913 0.17893 0.01030  0.00930  -0.01600 54  PRO A N   
436  C  CA  . PRO A 53  ? 0.14513 0.13383 0.18873 0.02520  0.01420  -0.00940 54  PRO A CA  
437  C  C   . PRO A 53  ? 0.16413 0.12533 0.17353 0.01700  0.01250  -0.01770 54  PRO A C   
438  O  O   . PRO A 53  ? 0.20853 0.11953 0.19533 0.02180  0.02810  -0.01840 54  PRO A O   
439  C  CB  . PRO A 53  ? 0.18313 0.16583 0.20783 0.01680  -0.01810 -0.00370 54  PRO A CB  
440  C  CG  . PRO A 53  ? 0.16773 0.15913 0.19513 0.03230  -0.03620 -0.01620 54  PRO A CG  
441  C  CD  . PRO A 53  ? 0.14063 0.15523 0.18183 0.01640  -0.02760 -0.02140 54  PRO A CD  
442  N  N   . VAL A 54  ? 0.12883 0.11293 0.14423 0.00830  0.00450  -0.01810 55  VAL A N   
443  C  CA  . VAL A 54  ? 0.12873 0.11963 0.15453 0.00710  0.00390  -0.00210 55  VAL A CA  
444  C  C   . VAL A 54  ? 0.14003 0.11413 0.16463 -0.00160 0.00520  -0.00190 55  VAL A C   
445  O  O   . VAL A 54  ? 0.12993 0.10813 0.17273 -0.00190 -0.00060 0.01000  55  VAL A O   
446  C  CB  . VAL A 54  ? 0.14343 0.12563 0.15813 0.01950  -0.00750 -0.00850 55  VAL A CB  
447  C  CG1 . VAL A 54  ? 0.14363 0.15763 0.17123 -0.00300 -0.01760 0.00010  55  VAL A CG1 
448  C  CG2 . VAL A 54  ? 0.14213 0.12923 0.17853 0.00700  0.00330  -0.00380 55  VAL A CG2 
449  N  N   . PRO A 55  ? 0.12963 0.10673 0.16003 -0.00240 0.00090  0.00660  56  PRO A N   
450  C  CA  . PRO A 55  ? 0.11793 0.11213 0.15473 -0.00170 -0.00160 0.01110  56  PRO A CA  
451  C  C   . PRO A 55  ? 0.12843 0.11203 0.11963 -0.00520 0.01080  0.01710  56  PRO A C   
452  O  O   . PRO A 55  ? 0.11623 0.13733 0.12823 0.00580  0.00370  0.02240  56  PRO A O   
453  C  CB  . PRO A 55  ? 0.14913 0.11433 0.14693 -0.02560 -0.00620 0.01180  56  PRO A CB  
454  C  CG  . PRO A 55  ? 0.16493 0.11633 0.16453 -0.00880 -0.01210 0.03300  56  PRO A CG  
455  C  CD  . PRO A 55  ? 0.15403 0.11663 0.17043 -0.02630 -0.00480 0.02470  56  PRO A CD  
456  N  N   . TRP A 56  ? 0.13583 0.10513 0.11613 -0.00300 0.00140  0.00930  57  TRP A N   
457  C  CA  . TRP A 56  ? 0.14103 0.10943 0.10623 0.01120  0.00400  0.00570  57  TRP A CA  
458  C  C   . TRP A 56  ? 0.11503 0.11093 0.10343 -0.00580 -0.01370 0.00670  57  TRP A C   
459  O  O   . TRP A 56  ? 0.11943 0.12033 0.10293 -0.00710 -0.00680 0.00730  57  TRP A O   
460  C  CB  . TRP A 56  ? 0.12343 0.12553 0.13153 -0.00640 0.01430  0.01730  57  TRP A CB  
461  C  CG  . TRP A 56  ? 0.12583 0.11223 0.11973 -0.00710 -0.00050 0.00590  57  TRP A CG  
462  C  CD1 . TRP A 56  ? 0.11853 0.13563 0.12373 -0.02270 0.01170  0.00480  57  TRP A CD1 
463  C  CD2 . TRP A 56  ? 0.12883 0.10643 0.12493 0.01080  -0.00300 -0.00020 57  TRP A CD2 
464  N  NE1 . TRP A 56  ? 0.11843 0.12403 0.13373 -0.01400 0.00410  -0.00400 57  TRP A NE1 
465  C  CE2 . TRP A 56  ? 0.14483 0.11303 0.12693 -0.00850 0.01320  -0.00000 57  TRP A CE2 
466  C  CE3 . TRP A 56  ? 0.15123 0.10203 0.12943 0.00890  -0.01230 0.00290  57  TRP A CE3 
467  C  CZ2 . TRP A 56  ? 0.13893 0.11853 0.12263 -0.00640 0.00860  0.00060  57  TRP A CZ2 
468  C  CZ3 . TRP A 56  ? 0.12393 0.11643 0.11903 -0.00110 0.00790  0.01550  57  TRP A CZ3 
469  C  CH2 . TRP A 56  ? 0.12363 0.11843 0.11463 -0.01810 -0.00320 0.01750  57  TRP A CH2 
470  N  N   . PRO A 57  ? 0.11683 0.11163 0.10553 0.00100  -0.00160 -0.00440 58  PRO A N   
471  C  CA  . PRO A 57  ? 0.11913 0.11683 0.10943 -0.01170 0.01410  -0.00690 58  PRO A CA  
472  C  C   . PRO A 57  ? 0.11453 0.09853 0.10773 -0.02050 0.01830  -0.00020 58  PRO A C   
473  O  O   . PRO A 57  ? 0.11093 0.11693 0.11693 -0.01420 -0.00320 -0.00680 58  PRO A O   
474  C  CB  . PRO A 57  ? 0.12903 0.13663 0.11533 -0.01920 -0.01430 -0.01600 58  PRO A CB  
475  C  CG  . PRO A 57  ? 0.11993 0.13983 0.11483 -0.00310 0.00180  -0.00760 58  PRO A CG  
476  C  CD  . PRO A 57  ? 0.11813 0.12253 0.10493 -0.00480 -0.02410 -0.01880 58  PRO A CD  
477  N  N   . THR A 58  ? 0.11303 0.09943 0.13073 -0.00840 -0.00730 0.00820  59  THR A N   
478  C  CA  . THR A 58  ? 0.11223 0.09043 0.13153 -0.02130 -0.01170 0.00180  59  THR A CA  
479  C  C   . THR A 58  ? 0.11663 0.07543 0.13053 -0.00910 0.00040  -0.00120 59  THR A C   
480  O  O   . THR A 58  ? 0.12113 0.09733 0.11083 -0.00790 -0.00300 -0.00710 59  THR A O   
481  C  CB  . THR A 58  ? 0.11943 0.07673 0.14303 -0.02520 0.00570  -0.00150 59  THR A CB  
482  O  OG1 . THR A 58  ? 0.11813 0.09233 0.14363 -0.00870 -0.00980 0.01180  59  THR A OG1 
483  C  CG2 . THR A 58  ? 0.14143 0.08803 0.14203 -0.01530 -0.01880 -0.00290 59  THR A CG2 
484  N  N   . LEU A 59  ? 0.09833 0.09023 0.13063 -0.00660 0.00610  -0.00660 60  LEU A N   
485  C  CA  . LEU A 59  ? 0.10293 0.08013 0.11653 -0.01590 0.00200  0.00640  60  LEU A CA  
486  C  C   . LEU A 59  ? 0.10443 0.09023 0.11233 -0.01050 -0.00840 0.00550  60  LEU A C   
487  O  O   . LEU A 59  ? 0.10913 0.08393 0.13123 -0.00890 0.00090  -0.00510 60  LEU A O   
488  C  CB  . LEU A 59  ? 0.11033 0.10083 0.12613 -0.00590 0.00720  -0.00060 60  LEU A CB  
489  C  CG  . LEU A 59  ? 0.11093 0.11833 0.12963 0.00680  -0.00220 -0.00090 60  LEU A CG  
490  C  CD1 . LEU A 59  ? 0.13193 0.12983 0.13603 -0.01450 0.00030  -0.00250 60  LEU A CD1 
491  C  CD2 . LEU A 59  ? 0.13943 0.09823 0.14423 -0.00030 -0.01860 0.01810  60  LEU A CD2 
492  N  N   . VAL A 60  ? 0.10183 0.09723 0.10953 -0.00840 -0.00180 0.01020  61  VAL A N   
493  C  CA  . VAL A 60  ? 0.09983 0.11403 0.12303 0.00320  0.00910  -0.00160 61  VAL A CA  
494  C  C   . VAL A 60  ? 0.09933 0.10083 0.13053 -0.00010 0.01720  0.01550  61  VAL A C   
495  O  O   . VAL A 60  ? 0.11573 0.10393 0.14203 -0.01440 -0.00420 0.00670  61  VAL A O   
496  C  CB  . VAL A 60  ? 0.09133 0.12353 0.12783 -0.00350 0.00550  0.00470  61  VAL A CB  
497  C  CG1 . VAL A 60  ? 0.10543 0.13553 0.11763 0.00880  0.00200  0.00710  61  VAL A CG1 
498  C  CG2 . VAL A 60  ? 0.11263 0.12173 0.11133 -0.00790 -0.00190 0.00000  61  VAL A CG2 
499  N  N   . THR A 61  ? 0.10373 0.11253 0.12233 -0.00580 -0.00490 0.01020  62  THR A N   
500  C  CA  . THR A 61  ? 0.09773 0.09963 0.11513 -0.01900 0.00130  0.00910  62  THR A CA  
501  C  C   . THR A 61  ? 0.11553 0.06823 0.12383 -0.01030 -0.01190 0.01210  62  THR A C   
502  O  O   . THR A 61  ? 0.11713 0.08593 0.12073 -0.01280 -0.00130 0.00050  62  THR A O   
503  C  CB  . THR A 61  ? 0.10353 0.08223 0.12933 -0.01590 0.00520  0.00610  62  THR A CB  
504  O  OG1 . THR A 61  ? 0.11063 0.09073 0.12353 -0.00280 0.00810  0.00200  62  THR A OG1 
505  C  CG2 . THR A 61  ? 0.12023 0.09473 0.13683 -0.02540 0.00120  0.00840  62  THR A CG2 
506  N  N   . THR A 62  ? 0.08593 0.08833 0.12513 -0.00620 -0.01300 0.02020  63  THR A N   
507  C  CA  . THR A 62  ? 0.09503 0.10093 0.12623 -0.02400 -0.00460 0.00240  63  THR A CA  
508  C  C   . THR A 62  ? 0.11593 0.09443 0.12103 -0.01850 0.00140  -0.00960 63  THR A C   
509  O  O   . THR A 62  ? 0.10973 0.10483 0.11513 -0.01070 -0.00030 0.00140  63  THR A O   
510  C  CB  . THR A 62  ? 0.08613 0.09383 0.12533 -0.01080 0.00240  0.00270  63  THR A CB  
511  O  OG1 . THR A 62  ? 0.10743 0.09993 0.11583 0.00650  0.00510  0.00050  63  THR A OG1 
512  C  CG2 . THR A 62  ? 0.10143 0.10433 0.15303 -0.01410 0.01410  0.01510  63  THR A CG2 
513  N  N   . PHE A 63  ? 0.12043 0.08273 0.11893 -0.01070 0.01020  -0.00170 64  PHE A N   
514  C  CA  . PHE A 63  ? 0.13493 0.08413 0.11873 -0.00570 0.00670  0.00100  64  PHE A CA  
515  C  C   . PHE A 63  ? 0.12313 0.09483 0.13543 -0.00730 0.00870  0.00400  64  PHE A C   
516  O  O   . PHE A 63  ? 0.13123 0.09383 0.14073 -0.00710 0.01830  0.00330  64  PHE A O   
517  C  CB  . PHE A 63  ? 0.13953 0.09433 0.11943 -0.01050 0.00670  -0.00730 64  PHE A CB  
518  C  CG  . PHE A 63  ? 0.12643 0.09533 0.12413 -0.02610 0.00720  -0.00020 64  PHE A CG  
519  C  CD1 . PHE A 63  ? 0.12693 0.09553 0.11523 -0.01080 0.01440  0.00240  64  PHE A CD1 
520  C  CD2 . PHE A 63  ? 0.12753 0.09343 0.12433 -0.01940 0.00100  0.01250  64  PHE A CD2 
521  C  CE1 . PHE A 63  ? 0.13573 0.10803 0.10793 -0.00880 0.00990  -0.00400 64  PHE A CE1 
522  C  CE2 . PHE A 63  ? 0.11983 0.11003 0.12893 -0.00980 -0.00290 0.01780  64  PHE A CE2 
523  C  CZ  . PHE A 63  ? 0.12973 0.10993 0.10553 -0.00130 0.00550  -0.00060 64  PHE A CZ  
524  N  N1  . GYS A 64  ? 0.10193 0.10033 0.12683 -0.00150 0.00450  -0.00730 66  GYS A N1  
525  O  OG1 A GYS A 64  ? 0.13743 0.15593 0.13603 0.02650  -0.00070 0.00020  66  GYS A OG1 
526  C  CB1 . GYS A 64  ? 0.10383 0.13583 0.13463 0.01500  -0.01310 0.00100  66  GYS A CB1 
527  C  CA1 . GYS A 64  ? 0.10693 0.11423 0.13213 -0.01060 0.00920  0.00880  66  GYS A CA1 
528  C  C1  . GYS A 64  ? 0.12013 0.10003 0.12533 -0.00140 0.01870  0.01980  66  GYS A C1  
529  N  N2  . GYS A 64  ? 0.12613 0.10943 0.13133 -0.00080 0.01860  0.00050  66  GYS A N2  
530  N  N3  . GYS A 64  ? 0.12133 0.08693 0.12253 -0.01170 0.01040  0.00720  66  GYS A N3  
531  C  C2  . GYS A 64  ? 0.14593 0.08013 0.12643 -0.00410 0.00810  -0.00300 66  GYS A C2  
532  O  O2  . GYS A 64  ? 0.15073 0.08153 0.12573 -0.00120 0.01160  -0.00630 66  GYS A O2  
533  C  CA2 . GYS A 64  ? 0.13153 0.09003 0.13543 -0.00720 0.00410  0.00210  66  GYS A CA2 
534  C  CA3 . GYS A 64  ? 0.13223 0.09213 0.13943 -0.02310 -0.00530 -0.02130 66  GYS A CA3 
535  C  CB2 . GYS A 64  ? 0.14203 0.10153 0.15903 0.00340  0.00220  -0.00060 66  GYS A CB2 
536  C  CG2 . GYS A 64  ? 0.12563 0.10583 0.15373 0.00640  -0.00360 0.00340  66  GYS A CG2 
537  C  CD1 . GYS A 64  ? 0.13423 0.11823 0.15073 0.01350  -0.00690 0.00880  66  GYS A CD1 
538  C  CD2 . GYS A 64  ? 0.13813 0.11033 0.16263 0.00230  -0.00180 0.00990  66  GYS A CD2 
539  C  CE1 . GYS A 64  ? 0.13793 0.10253 0.17563 -0.00160 0.01560  0.00120  66  GYS A CE1 
540  C  CE2 . GYS A 64  ? 0.14283 0.09423 0.14753 0.01520  0.00980  -0.01600 66  GYS A CE2 
541  C  CZ  . GYS A 64  ? 0.13053 0.10933 0.15583 0.00260  0.00460  -0.01480 66  GYS A CZ  
542  O  OH  . GYS A 64  ? 0.13043 0.11803 0.17503 0.00170  0.00550  -0.00800 66  GYS A OH  
543  C  C3  . GYS A 64  ? 0.13333 0.09903 0.14803 -0.00580 0.01450  -0.01630 66  GYS A C3  
544  O  O3  . GYS A 64  ? 0.13583 0.10303 0.14863 -0.01190 0.00340  -0.01190 66  GYS A O3  
545  N  N   . VAL A 65  ? 0.14843 0.08223 0.12633 0.03060  0.01670  0.00380  68  VAL A N   
546  C  CA  . VAL A 65  ? 0.14043 0.09153 0.13743 0.01560  -0.00140 -0.00250 68  VAL A CA  
547  C  C   . VAL A 65  ? 0.12463 0.07463 0.13473 0.01420  0.00250  -0.00620 68  VAL A C   
548  O  O   . VAL A 65  ? 0.14513 0.09363 0.14273 0.01240  -0.00370 -0.00320 68  VAL A O   
549  C  CB  . VAL A 65  ? 0.13533 0.10693 0.15003 0.00370  0.00660  -0.00530 68  VAL A CB  
550  C  CG1 . VAL A 65  ? 0.13983 0.12893 0.16483 0.02350  0.03040  -0.01180 68  VAL A CG1 
551  C  CG2 . VAL A 65  ? 0.16873 0.11793 0.14953 0.00230  -0.01190 -0.00180 68  VAL A CG2 
552  N  N   . GLN A 66  ? 0.12303 0.09633 0.12923 0.01700  -0.01770 -0.00290 69  GLN A N   
553  C  CA  . GLN A 66  ? 0.12073 0.10493 0.13573 0.01410  -0.00600 -0.01220 69  GLN A CA  
554  C  C   . GLN A 66  ? 0.11493 0.10303 0.12283 0.02170  -0.00720 -0.00770 69  GLN A C   
555  O  O   . GLN A 66  ? 0.13073 0.10353 0.13503 0.00200  -0.00300 0.00370  69  GLN A O   
556  C  CB  . GLN A 66  ? 0.15273 0.08323 0.15503 0.00130  -0.00950 0.00140  69  GLN A CB  
557  C  CG  . GLN A 66  ? 0.17183 0.08583 0.16073 -0.02460 -0.01250 -0.00210 69  GLN A CG  
558  C  CD  . GLN A 66  ? 0.16243 0.09763 0.16843 -0.00880 0.01150  -0.00960 69  GLN A CD  
559  O  OE1 . GLN A 66  ? 0.19613 0.11183 0.13753 0.00450  0.01220  0.00800  69  GLN A OE1 
560  N  NE2 . GLN A 66  ? 0.17813 0.10493 0.21613 -0.01450 0.02810  -0.02220 69  GLN A NE2 
561  N  N   . CYS A 67  ? 0.13103 0.09223 0.12253 -0.00590 -0.01200 -0.02540 70  CYS A N   
562  C  CA  . CYS A 67  ? 0.12823 0.09403 0.15073 0.00590  -0.00750 -0.00940 70  CYS A CA  
563  C  C   . CYS A 67  ? 0.11613 0.08393 0.13513 0.02110  0.01400  0.00890  70  CYS A C   
564  O  O   . CYS A 67  ? 0.12583 0.09723 0.15593 0.01760  0.01950  0.00380  70  CYS A O   
565  C  CB  . CYS A 67  ? 0.11643 0.12003 0.13713 0.00220  -0.00240 -0.00460 70  CYS A CB  
566  S  SG  . CYS A 67  ? 0.12873 0.10683 0.14213 0.00820  0.00610  -0.00430 70  CYS A SG  
567  N  N   . PHE A 68  ? 0.12793 0.09493 0.11703 0.02490  0.00160  0.00790  71  PHE A N   
568  C  CA  . PHE A 68  ? 0.13933 0.09313 0.13423 0.01270  -0.00470 0.00130  71  PHE A CA  
569  C  C   . PHE A 68  ? 0.13993 0.08263 0.14203 0.02010  -0.00440 -0.00210 71  PHE A C   
570  O  O   . PHE A 68  ? 0.14303 0.13363 0.14473 0.02740  -0.00300 0.00900  71  PHE A O   
571  C  CB  . PHE A 68  ? 0.14083 0.09133 0.13813 0.00730  0.00870  -0.00470 71  PHE A CB  
572  C  CG  . PHE A 68  ? 0.14573 0.10283 0.11903 0.01400  -0.00620 0.00180  71  PHE A CG  
573  C  CD1 . PHE A 68  ? 0.15523 0.08473 0.13513 0.00770  0.00940  0.01300  71  PHE A CD1 
574  C  CD2 . PHE A 68  ? 0.12443 0.11003 0.12063 -0.00070 0.01030  0.00700  71  PHE A CD2 
575  C  CE1 . PHE A 68  ? 0.15953 0.08343 0.15763 0.01450  0.00890  0.00100  71  PHE A CE1 
576  C  CE2 . PHE A 68  ? 0.14473 0.08943 0.11323 -0.00450 0.00110  -0.00600 71  PHE A CE2 
577  C  CZ  . PHE A 68  ? 0.15993 0.09013 0.12653 0.00210  0.00930  0.00220  71  PHE A CZ  
578  N  N   . SER A 69  ? 0.11383 0.09623 0.13983 0.01050  -0.00510 0.00680  72  SER A N   
579  C  CA  . SER A 69  ? 0.10913 0.10283 0.15733 0.02000  -0.01080 0.01170  72  SER A CA  
580  C  C   . SER A 69  ? 0.11343 0.11193 0.13943 0.01700  -0.00030 0.00270  72  SER A C   
581  O  O   . SER A 69  ? 0.13593 0.12123 0.14043 0.02060  0.00090  -0.01640 72  SER A O   
582  C  CB  . SER A 69  ? 0.14183 0.10263 0.19043 0.03030  -0.00660 0.03960  72  SER A CB  
583  O  OG  . SER A 69  ? 0.15553 0.12073 0.21843 0.00100  -0.02500 0.02870  72  SER A OG  
584  N  N   . ARG A 70  ? 0.11133 0.13553 0.14323 0.01440  -0.00480 0.00750  73  ARG A N   
585  C  CA  . ARG A 70  ? 0.10353 0.13353 0.15403 0.03890  -0.01440 -0.00890 73  ARG A CA  
586  C  C   . ARG A 70  ? 0.13293 0.11853 0.15303 0.01600  0.01660  -0.01450 73  ARG A C   
587  O  O   . ARG A 70  ? 0.14423 0.11753 0.16833 0.01110  0.01180  -0.02270 73  ARG A O   
588  C  CB  . ARG A 70  ? 0.12763 0.16823 0.17033 0.04350  -0.01170 -0.01580 73  ARG A CB  
589  C  CG  . ARG A 70  ? 0.13273 0.16163 0.18373 0.04340  -0.03660 0.00490  73  ARG A CG  
590  C  CD  . ARG A 70  ? 0.14223 0.16853 0.21433 0.04040  -0.00610 0.00960  73  ARG A CD  
591  N  NE  . ARG A 70  ? 0.15473 0.18933 0.24573 0.01870  -0.01420 0.00650  73  ARG A NE  
592  C  CZ  . ARG A 70  ? 0.17783 0.20523 0.28253 0.01640  -0.01200 0.00900  73  ARG A CZ  
593  N  NH1 . ARG A 70  ? 0.19703 0.21623 0.28673 0.02870  0.01700  -0.00220 73  ARG A NH1 
594  N  NH2 . ARG A 70  ? 0.19893 0.21593 0.31013 -0.00380 -0.01400 0.03060  73  ARG A NH2 
595  N  N   . TYR A 71  ? 0.14533 0.11703 0.13083 0.02850  0.01710  -0.02690 74  TYR A N   
596  C  CA  . TYR A 71  ? 0.16033 0.11023 0.13423 0.03330  0.01450  -0.02260 74  TYR A CA  
597  C  C   . TYR A 71  ? 0.15883 0.11283 0.14043 0.01540  0.02860  -0.02010 74  TYR A C   
598  O  O   . TYR A 71  ? 0.19213 0.11303 0.16513 0.00630  0.03870  -0.01240 74  TYR A O   
599  C  CB  . TYR A 71  ? 0.16513 0.13583 0.12983 0.02100  -0.00390 -0.03340 74  TYR A CB  
600  C  CG  . TYR A 71  ? 0.17303 0.12673 0.13563 0.00300  -0.00860 -0.01520 74  TYR A CG  
601  C  CD1 . TYR A 71  ? 0.14603 0.10913 0.11713 -0.00200 -0.02290 -0.01320 74  TYR A CD1 
602  C  CD2 . TYR A 71  ? 0.17313 0.14323 0.14903 -0.00240 -0.00840 -0.00290 74  TYR A CD2 
603  C  CE1 . TYR A 71  ? 0.14223 0.13043 0.13133 -0.01500 -0.00440 0.01070  74  TYR A CE1 
604  C  CE2 . TYR A 71  ? 0.12103 0.13743 0.14753 0.00490  -0.00020 -0.00080 74  TYR A CE2 
605  C  CZ  . TYR A 71  ? 0.13833 0.13533 0.13463 0.00530  -0.00450 -0.00240 74  TYR A CZ  
606  O  OH  . TYR A 71  ? 0.13123 0.13553 0.15723 0.01040  -0.01210 -0.00650 74  TYR A OH  
607  N  N   . PRO A 72  ? 0.14893 0.12213 0.14513 0.02190  0.00780  -0.00340 75  PRO A N   
608  C  CA  . PRO A 72  ? 0.13853 0.12063 0.15383 0.03660  -0.00940 -0.01500 75  PRO A CA  
609  C  C   . PRO A 72  ? 0.14373 0.12383 0.16483 0.03940  -0.00770 -0.00630 75  PRO A C   
610  O  O   . PRO A 72  ? 0.13443 0.13873 0.14353 0.02530  -0.01270 -0.00050 75  PRO A O   
611  C  CB  . PRO A 72  ? 0.16523 0.15733 0.17213 0.01730  -0.01390 -0.00950 75  PRO A CB  
612  C  CG  . PRO A 72  ? 0.16093 0.17543 0.17373 0.03870  -0.01140 -0.01980 75  PRO A CG  
613  C  CD  . PRO A 72  ? 0.15063 0.12903 0.16923 0.02260  0.01460  0.01540  75  PRO A CD  
614  N  N   . ASP A 73  ? 0.14553 0.11023 0.16853 0.03080  -0.01180 -0.01610 76  ASP A N   
615  C  CA  . ASP A 73  ? 0.16323 0.10703 0.16153 0.05010  -0.00410 -0.02070 76  ASP A CA  
616  C  C   . ASP A 73  ? 0.14793 0.12653 0.15963 0.03560  -0.00500 -0.01790 76  ASP A C   
617  O  O   . ASP A 73  ? 0.14333 0.11973 0.16973 0.02930  -0.01710 -0.00320 76  ASP A O   
618  C  CB  . ASP A 73  ? 0.18453 0.10933 0.18373 0.04850  -0.01460 -0.03310 76  ASP A CB  
619  C  CG  . ASP A 73  ? 0.20873 0.12073 0.20893 0.06110  -0.02690 -0.03280 76  ASP A CG  
620  O  OD1 . ASP A 73  ? 0.21263 0.15023 0.24613 0.04260  -0.05360 -0.03140 76  ASP A OD1 
621  O  OD2 . ASP A 73  ? 0.26813 0.13793 0.19643 0.04700  -0.01040 -0.03970 76  ASP A OD2 
622  N  N   . HIS A 74  ? 0.13823 0.16363 0.16653 0.03660  0.00640  -0.02580 77  HIS A N   
623  C  CA  . HIS A 74  ? 0.15703 0.20663 0.17743 0.03060  0.01410  -0.01850 77  HIS A CA  
624  C  C   . HIS A 74  ? 0.17013 0.19153 0.15513 0.02320  0.01660  -0.00320 77  HIS A C   
625  O  O   . HIS A 74  ? 0.19783 0.23193 0.15983 0.03430  0.02030  0.01410  77  HIS A O   
626  C  CB  . HIS A 74  ? 0.19303 0.25313 0.24423 0.02550  0.01570  -0.03600 77  HIS A CB  
627  C  CG  . HIS A 74  ? 0.30973 0.35043 0.34353 0.02680  0.03990  -0.02220 77  HIS A CG  
630  C  CE1 . HIS A 74  ? 0.35473 0.38343 0.39283 -0.10050 0.03770  0.01050  77  HIS A CE1 
631  N  NE2 . HIS A 74  ? 0.34623 0.38173 0.39953 -0.09180 0.01770  0.00380  77  HIS A NE2 
632  N  N   . MET A 75  ? 0.15003 0.15503 0.15613 0.01050  0.00440  0.00030  78  MET A N   
633  C  CA  . MET A 75  ? 0.17723 0.14813 0.16263 0.02350  0.01410  0.00720  78  MET A CA  
634  C  C   . MET A 75  ? 0.16323 0.14913 0.16313 0.03000  0.00460  0.00190  78  MET A C   
635  O  O   . MET A 75  ? 0.17413 0.15653 0.15853 0.06070  -0.01610 0.00850  78  MET A O   
636  C  CB  . MET A 75  ? 0.21183 0.14733 0.17663 0.01390  0.02790  0.01000  78  MET A CB  
637  C  CG  . MET A 75  ? 0.23653 0.14093 0.18053 -0.00430 0.02240  -0.00320 78  MET A CG  
638  S  SD  . MET A 75  ? 0.21253 0.14333 0.17163 0.00150  0.02830  0.01650  78  MET A SD  
639  C  CE  . MET A 75  ? 0.18733 0.15463 0.19453 0.03890  0.02510  0.02250  78  MET A CE  
641  N  N   B LYS A 76  ? 0.16093 0.14933 0.16383 0.02830  -0.00760 0.03160  79  LYS A N   
643  C  CA  B LYS A 76  ? 0.16543 0.16563 0.16193 0.01350  -0.00160 0.04090  79  LYS A CA  
645  C  C   B LYS A 76  ? 0.16373 0.19693 0.16083 0.00880  -0.00350 0.03320  79  LYS A C   
647  O  O   B LYS A 76  ? 0.16523 0.22273 0.17053 0.01390  -0.02340 0.04610  79  LYS A O   
649  C  CB  B LYS A 76  ? 0.19233 0.15943 0.16113 -0.00260 0.00850  0.04150  79  LYS A CB  
651  C  CG  B LYS A 76  ? 0.20243 0.16313 0.16623 -0.00500 0.00540  0.03440  79  LYS A CG  
653  C  CD  B LYS A 76  ? 0.19553 0.18163 0.17583 -0.02210 0.01040  0.01140  79  LYS A CD  
655  C  CE  B LYS A 76  ? 0.18943 0.18363 0.19263 -0.01500 0.01060  0.00320  79  LYS A CE  
657  N  NZ  B LYS A 76  ? 0.17513 0.18973 0.19933 0.00520  0.01080  0.00590  79  LYS A NZ  
658  N  N   . ARG A 77  ? 0.15663 0.19553 0.15443 0.02530  -0.01230 0.02230  80  ARG A N   
659  C  CA  A ARG A 77  ? 0.16943 0.21763 0.16853 0.04650  -0.01840 0.01140  80  ARG A CA  
661  C  C   . ARG A 77  ? 0.16703 0.21833 0.18863 0.04780  -0.01380 0.04580  80  ARG A C   
662  O  O   . ARG A 77  ? 0.21833 0.27623 0.21873 0.04850  -0.03800 0.07570  80  ARG A O   
663  C  CB  A ARG A 77  ? 0.19773 0.22743 0.16853 0.03530  -0.03710 -0.00120 80  ARG A CB  
665  C  CG  A ARG A 77  ? 0.23513 0.23203 0.18703 0.00120  -0.03270 -0.00540 80  ARG A CG  
667  C  CD  A ARG A 77  ? 0.25633 0.23903 0.21563 -0.01890 -0.01280 -0.01370 80  ARG A CD  
669  N  NE  A ARG A 77  ? 0.26333 0.24263 0.23953 -0.01210 0.00070  -0.00980 80  ARG A NE  
671  C  CZ  A ARG A 77  ? 0.29183 0.27313 0.25563 -0.00750 0.00410  -0.00320 80  ARG A CZ  
673  N  NH1 A ARG A 77  ? 0.29903 0.29073 0.25953 -0.00390 0.00960  0.00200  80  ARG A NH1 
675  N  NH2 A ARG A 77  ? 0.29833 0.26823 0.27283 0.01140  -0.00810 -0.01000 80  ARG A NH2 
677  N  N   . HIS A 78  ? 0.14043 0.17973 0.18823 0.03160  0.03170  0.04200  81  HIS A N   
679  C  CA  B HIS A 78  ? 0.13183 0.17633 0.18623 0.06600  0.02800  0.04670  81  HIS A CA  
680  C  C   . HIS A 78  ? 0.14553 0.16143 0.16653 0.03720  0.01110  0.03710  81  HIS A C   
681  O  O   . HIS A 78  ? 0.17593 0.15603 0.17083 0.01240  -0.00280 0.03260  81  HIS A O   
683  C  CB  B HIS A 78  ? 0.14303 0.20183 0.18893 0.05870  0.03680  0.05000  81  HIS A CB  
685  C  CG  B HIS A 78  ? 0.13573 0.20423 0.18003 0.06040  0.04680  0.03790  81  HIS A CG  
687  N  ND1 B HIS A 78  ? 0.16903 0.23493 0.19223 0.06890  0.04670  0.02830  81  HIS A ND1 
689  C  CD2 B HIS A 78  ? 0.14573 0.20563 0.17763 0.05260  0.05990  0.03600  81  HIS A CD2 
691  C  CE1 B HIS A 78  ? 0.17733 0.23143 0.18633 0.06660  0.05370  0.02600  81  HIS A CE1 
693  N  NE2 B HIS A 78  ? 0.17163 0.22423 0.18483 0.05140  0.06160  0.02910  81  HIS A NE2 
694  N  N   . ASP A 79  ? 0.11413 0.14063 0.12583 0.01510  0.00770  0.02260  82  ASP A N   
695  C  CA  . ASP A 79  ? 0.13053 0.12883 0.13403 0.00240  0.01060  0.00110  82  ASP A CA  
696  C  C   . ASP A 79  ? 0.13413 0.12113 0.12903 -0.00320 -0.00180 -0.00210 82  ASP A C   
697  O  O   . ASP A 79  ? 0.13223 0.11073 0.13583 0.00620  -0.01160 -0.00340 82  ASP A O   
698  C  CB  . ASP A 79  ? 0.14243 0.14673 0.11843 0.00740  0.00740  0.00020  82  ASP A CB  
699  C  CG  . ASP A 79  ? 0.14293 0.11673 0.12763 0.00510  -0.00040 -0.00300 82  ASP A CG  
700  O  OD1 . ASP A 79  ? 0.16543 0.11893 0.11383 -0.00740 -0.00760 -0.00750 82  ASP A OD1 
701  O  OD2 . ASP A 79  ? 0.15893 0.11663 0.12813 -0.00050 -0.01460 -0.00150 82  ASP A OD2 
702  N  N   . PHE A 80  ? 0.13443 0.10693 0.12903 0.00670  -0.00680 -0.00260 83  PHE A N   
703  C  CA  . PHE A 80  ? 0.13513 0.10393 0.10913 0.02390  -0.00130 0.00550  83  PHE A CA  
704  C  C   . PHE A 80  ? 0.13883 0.10993 0.10913 0.01030  0.00540  -0.00190 83  PHE A C   
705  O  O   . PHE A 80  ? 0.14243 0.09103 0.10493 0.00450  0.00060  -0.01160 83  PHE A O   
706  C  CB  . PHE A 80  ? 0.13523 0.11043 0.11803 0.02040  0.00810  -0.00140 83  PHE A CB  
707  C  CG  . PHE A 80  ? 0.13583 0.09713 0.12583 0.02390  -0.01600 0.00630  83  PHE A CG  
708  C  CD1 . PHE A 80  ? 0.17103 0.10353 0.14253 0.00530  -0.02350 0.00420  83  PHE A CD1 
709  C  CD2 . PHE A 80  ? 0.15273 0.08513 0.14703 0.01310  -0.00510 -0.00130 83  PHE A CD2 
710  C  CE1 . PHE A 80  ? 0.17173 0.11003 0.15313 0.01530  -0.01630 -0.00710 83  PHE A CE1 
711  C  CE2 . PHE A 80  ? 0.16563 0.09213 0.14833 0.02180  -0.02120 -0.00550 83  PHE A CE2 
712  C  CZ  . PHE A 80  ? 0.16503 0.10453 0.15153 0.02150  -0.02050 -0.01900 83  PHE A CZ  
713  N  N   . PHE A 81  ? 0.14913 0.10593 0.11253 0.01420  0.00860  0.00160  84  PHE A N   
714  C  CA  . PHE A 81  ? 0.12873 0.10983 0.10973 -0.00060 0.01290  -0.00730 84  PHE A CA  
715  C  C   . PHE A 81  ? 0.14193 0.10563 0.12213 -0.00150 0.00960  -0.00750 84  PHE A C   
716  O  O   . PHE A 81  ? 0.14303 0.10363 0.13933 0.00560  0.00050  -0.00220 84  PHE A O   
717  C  CB  . PHE A 81  ? 0.12333 0.09253 0.10623 -0.00590 0.00120  -0.01520 84  PHE A CB  
718  C  CG  . PHE A 81  ? 0.11793 0.10233 0.13413 -0.00090 0.00690  -0.00750 84  PHE A CG  
719  C  CD1 . PHE A 81  ? 0.13453 0.10773 0.14873 0.00290  0.01600  -0.02150 84  PHE A CD1 
720  C  CD2 . PHE A 81  ? 0.14353 0.12943 0.14033 0.00510  0.00100  -0.00770 84  PHE A CD2 
721  C  CE1 . PHE A 81  ? 0.13813 0.11863 0.17173 0.00320  0.01470  -0.00080 84  PHE A CE1 
722  C  CE2 . PHE A 81  ? 0.15983 0.12163 0.14653 0.00120  0.00120  -0.01780 84  PHE A CE2 
723  C  CZ  . PHE A 81  ? 0.14723 0.12533 0.16563 0.01290  0.00030  -0.02010 84  PHE A CZ  
724  N  N   . LYS A 82  ? 0.12983 0.08903 0.13443 0.01250  0.00400  0.00100  85  LYS A N   
725  C  CA  . LYS A 82  ? 0.13323 0.09473 0.13943 0.00970  -0.01710 -0.01490 85  LYS A CA  
726  C  C   . LYS A 82  ? 0.12963 0.09333 0.14053 0.00100  -0.00790 -0.00940 85  LYS A C   
727  O  O   . LYS A 82  ? 0.13683 0.10623 0.14713 0.01730  -0.00870 -0.00450 85  LYS A O   
728  C  CB  . LYS A 82  ? 0.15683 0.10103 0.13913 0.01570  -0.02280 -0.01530 85  LYS A CB  
729  C  CG  . LYS A 82  ? 0.15113 0.11653 0.13993 0.01910  -0.03080 -0.00100 85  LYS A CG  
730  C  CD  . LYS A 82  ? 0.14193 0.11583 0.14123 0.02580  -0.01570 0.00180  85  LYS A CD  
731  C  CE  . LYS A 82  ? 0.14763 0.11303 0.14803 -0.00720 -0.01090 0.00300  85  LYS A CE  
732  N  NZ  . LYS A 82  ? 0.15163 0.11033 0.14213 -0.00010 -0.01000 0.00450  85  LYS A NZ  
733  N  N   . SER A 83  ? 0.14483 0.10443 0.11793 0.01310  -0.00310 -0.02050 86  SER A N   
734  C  CA  . SER A 83  ? 0.13263 0.10743 0.14173 0.02380  -0.01050 -0.01070 86  SER A CA  
735  C  C   . SER A 83  ? 0.13413 0.10553 0.16453 0.01190  -0.01400 -0.00110 86  SER A C   
736  O  O   . SER A 83  ? 0.14613 0.11603 0.17453 0.00300  -0.00810 -0.03370 86  SER A O   
737  C  CB  . SER A 83  ? 0.14353 0.10443 0.13953 0.01560  -0.00070 -0.00230 86  SER A CB  
738  O  OG  . SER A 83  ? 0.14443 0.12693 0.12663 0.00760  -0.00770 -0.00810 86  SER A OG  
739  N  N   . ALA A 84  ? 0.11913 0.11713 0.14233 0.03210  -0.01090 -0.00380 87  ALA A N   
740  C  CA  . ALA A 84  ? 0.10583 0.11873 0.14963 0.00320  -0.01220 -0.00400 87  ALA A CA  
741  C  C   . ALA A 84  ? 0.11703 0.11033 0.13483 -0.00140 -0.00130 -0.01010 87  ALA A C   
742  O  O   . ALA A 84  ? 0.13473 0.13903 0.12843 -0.00340 0.00130  -0.01570 87  ALA A O   
743  C  CB  . ALA A 84  ? 0.13143 0.11003 0.17843 0.00540  -0.00060 -0.01590 87  ALA A CB  
744  N  N   . MET A 85  ? 0.14283 0.10743 0.12653 -0.00180 -0.00350 -0.01820 88  MET A N   
745  C  CA  . MET A 85  ? 0.16363 0.10303 0.11933 -0.00460 -0.00290 -0.01020 88  MET A CA  
746  C  C   . MET A 85  ? 0.17073 0.11713 0.12853 -0.01520 0.00470  -0.01970 88  MET A C   
747  O  O   . MET A 85  ? 0.16343 0.12083 0.12493 0.00120  0.00700  -0.00940 88  MET A O   
748  C  CB  . MET A 85  ? 0.14943 0.11033 0.13393 0.00490  -0.01260 -0.01380 88  MET A CB  
749  C  CG  . MET A 85  ? 0.15933 0.10963 0.14423 0.01140  -0.00500 -0.02250 88  MET A CG  
750  S  SD  . MET A 85  ? 0.13493 0.11553 0.14223 0.00110  0.00330  -0.00860 88  MET A SD  
751  C  CE  . MET A 85  ? 0.14563 0.12073 0.17233 -0.00670 -0.00600 -0.01450 88  MET A CE  
752  N  N   . PRO A 86  ? 0.16513 0.09833 0.15883 -0.00910 0.01390  -0.01620 89  PRO A N   
753  C  CA  . PRO A 86  ? 0.18053 0.11393 0.14653 -0.01010 0.00350  -0.01420 89  PRO A CA  
754  C  C   . PRO A 86  ? 0.17453 0.09633 0.14933 -0.02130 -0.02020 -0.01370 89  PRO A C   
755  O  O   . PRO A 86  ? 0.16623 0.11043 0.15073 -0.01300 -0.01170 -0.02280 89  PRO A O   
756  C  CB  . PRO A 86  ? 0.19943 0.12023 0.16473 -0.02830 0.01330  -0.01860 89  PRO A CB  
757  C  CG  . PRO A 86  ? 0.18793 0.12203 0.17703 -0.02360 0.00730  -0.01950 89  PRO A CG  
758  C  CD  . PRO A 86  ? 0.17713 0.11163 0.17443 -0.01360 0.01090  -0.01570 89  PRO A CD  
759  N  N   . GLU A 87  ? 0.17313 0.11953 0.14913 -0.00020 -0.01410 -0.01880 90  GLU A N   
760  C  CA  . GLU A 87  ? 0.17663 0.13253 0.14343 -0.00310 -0.01770 -0.01980 90  GLU A CA  
761  C  C   . GLU A 87  ? 0.15643 0.12043 0.15363 -0.01070 -0.00180 -0.01830 90  GLU A C   
762  O  O   . GLU A 87  ? 0.15943 0.15863 0.16593 0.00310  0.00310  -0.01810 90  GLU A O   
763  C  CB  . GLU A 87  ? 0.18983 0.18693 0.13863 -0.02180 -0.02700 -0.03440 90  GLU A CB  
764  C  CG  . GLU A 87  ? 0.19213 0.21233 0.18683 -0.01270 -0.02480 -0.04590 90  GLU A CG  
765  C  CD  . GLU A 87  ? 0.22513 0.20953 0.20513 -0.01590 -0.04010 -0.06100 90  GLU A CD  
766  O  OE1 . GLU A 87  ? 0.18993 0.19323 0.17243 -0.02700 -0.01160 -0.04680 90  GLU A OE1 
767  O  OE2 . GLU A 87  ? 0.29213 0.23333 0.27173 -0.01970 -0.04190 -0.06170 90  GLU A OE2 
768  N  N   . GLY A 88  ? 0.16243 0.10663 0.13793 -0.02420 -0.00010 -0.01530 91  GLY A N   
769  C  CA  . GLY A 88  ? 0.16743 0.10193 0.14423 -0.01430 -0.00390 -0.01050 91  GLY A CA  
770  C  C   . GLY A 88  ? 0.12773 0.11533 0.13803 -0.00620 -0.01330 -0.00740 91  GLY A C   
771  O  O   . GLY A 88  ? 0.14923 0.12223 0.12783 0.00200  -0.01650 -0.01050 91  GLY A O   
772  N  N   . TYR A 89  ? 0.12603 0.10983 0.14133 -0.00620 0.00300  -0.01760 92  TYR A N   
773  C  CA  . TYR A 89  ? 0.13143 0.11283 0.14103 -0.02330 0.00800  -0.00580 92  TYR A CA  
774  C  C   . TYR A 89  ? 0.13503 0.10433 0.12033 -0.01370 -0.00890 -0.00590 92  TYR A C   
775  O  O   . TYR A 89  ? 0.12593 0.11603 0.12003 -0.00620 -0.00730 -0.00280 92  TYR A O   
776  C  CB  . TYR A 89  ? 0.12993 0.12743 0.13043 -0.01890 -0.01120 -0.00420 92  TYR A CB  
777  C  CG  . TYR A 89  ? 0.11493 0.10953 0.12243 -0.01020 0.01210  0.00140  92  TYR A CG  
778  C  CD1 . TYR A 89  ? 0.14083 0.11673 0.12973 -0.02400 0.01090  -0.02230 92  TYR A CD1 
779  C  CD2 . TYR A 89  ? 0.12893 0.11843 0.15493 0.00860  -0.00480 -0.02990 92  TYR A CD2 
780  C  CE1 . TYR A 89  ? 0.12113 0.10623 0.13593 -0.01060 -0.00090 0.00310  92  TYR A CE1 
781  C  CE2 . TYR A 89  ? 0.14003 0.11583 0.15883 -0.02420 0.00670  -0.00280 92  TYR A CE2 
782  C  CZ  . TYR A 89  ? 0.11233 0.11073 0.15333 -0.00920 -0.00250 -0.00240 92  TYR A CZ  
783  O  OH  . TYR A 89  ? 0.12453 0.11363 0.14243 0.00420  -0.00470 0.00780  92  TYR A OH  
784  N  N   . VAL A 90  ? 0.13213 0.09363 0.12403 -0.01960 -0.00940 -0.01060 93  VAL A N   
785  C  CA  . VAL A 90  ? 0.14183 0.10043 0.13983 -0.00990 -0.00660 -0.01180 93  VAL A CA  
786  C  C   . VAL A 90  ? 0.14483 0.11133 0.12843 -0.01840 0.01750  -0.00750 93  VAL A C   
787  O  O   . VAL A 90  ? 0.17223 0.16193 0.14923 -0.06210 0.02850  -0.02920 93  VAL A O   
788  C  CB  . VAL A 90  ? 0.14773 0.11783 0.16213 -0.00630 -0.04300 -0.01180 93  VAL A CB  
789  C  CG1 . VAL A 90  ? 0.16743 0.12693 0.16703 -0.00470 -0.04050 -0.01050 93  VAL A CG1 
790  C  CG2 . VAL A 90  ? 0.16503 0.15843 0.20383 -0.00020 -0.05020 -0.02330 93  VAL A CG2 
791  N  N   . GLN A 91  ? 0.12613 0.09753 0.12963 0.00220  0.00040  -0.02160 94  GLN A N   
792  C  CA  . GLN A 91  ? 0.11133 0.10043 0.13693 -0.00190 -0.00550 -0.01450 94  GLN A CA  
793  C  C   . GLN A 91  ? 0.11093 0.10333 0.13483 -0.01040 0.00220  -0.00280 94  GLN A C   
794  O  O   . GLN A 91  ? 0.11373 0.11393 0.13793 -0.01130 0.03390  -0.00880 94  GLN A O   
795  C  CB  . GLN A 91  ? 0.10313 0.11353 0.13813 -0.02590 0.00120  -0.00410 94  GLN A CB  
796  C  CG  . GLN A 91  ? 0.11453 0.11463 0.14203 -0.00430 -0.00910 -0.00620 94  GLN A CG  
797  C  CD  . GLN A 91  ? 0.11653 0.09693 0.13733 -0.00750 -0.00370 -0.01520 94  GLN A CD  
798  O  OE1 . GLN A 91  ? 0.15753 0.11083 0.13993 -0.00340 -0.00340 -0.00770 94  GLN A OE1 
799  N  NE2 . GLN A 91  ? 0.12243 0.13093 0.12773 -0.01810 -0.00980 -0.00530 94  GLN A NE2 
800  N  N   . GLU A 92  ? 0.11233 0.09143 0.13863 0.00600  -0.01210 -0.01460 95  GLU A N   
801  C  CA  A GLU A 92  ? 0.13243 0.10953 0.15403 -0.01640 -0.01610 -0.03210 95  GLU A CA  
803  C  C   . GLU A 92  ? 0.12273 0.10893 0.13133 -0.00360 0.01240  -0.02190 95  GLU A C   
804  O  O   . GLU A 92  ? 0.13653 0.12613 0.14833 -0.00280 0.02650  -0.03160 95  GLU A O   
805  C  CB  A GLU A 92  ? 0.15913 0.16693 0.16573 -0.02600 -0.03200 -0.04810 95  GLU A CB  
807  C  CG  A GLU A 92  ? 0.18023 0.22263 0.20023 -0.01080 -0.04220 -0.03700 95  GLU A CG  
809  C  CD  A GLU A 92  ? 0.20603 0.26913 0.22523 0.01570  -0.04770 -0.02030 95  GLU A CD  
811  O  OE1 A GLU A 92  ? 0.21803 0.30193 0.23013 0.01680  -0.07310 -0.01310 95  GLU A OE1 
813  O  OE2 A GLU A 92  ? 0.21293 0.25893 0.22663 0.03320  -0.05740 -0.00090 95  GLU A OE2 
815  N  N   . ARG A 93  ? 0.13133 0.08953 0.11793 -0.00320 0.00490  -0.00730 96  ARG A N   
816  C  CA  . ARG A 93  ? 0.10913 0.08943 0.12973 0.00810  -0.01580 -0.00770 96  ARG A CA  
817  C  C   . ARG A 93  ? 0.11643 0.09283 0.11943 0.00630  0.00770  -0.01860 96  ARG A C   
818  O  O   . ARG A 93  ? 0.12833 0.09283 0.13343 0.00600  0.00530  -0.00820 96  ARG A O   
819  C  CB  . ARG A 93  ? 0.12353 0.09653 0.12713 0.00260  0.00220  -0.00000 96  ARG A CB  
820  C  CG  . ARG A 93  ? 0.12113 0.09113 0.11513 0.00060  0.00650  0.00820  96  ARG A CG  
821  C  CD  . ARG A 93  ? 0.10943 0.10203 0.13723 0.00010  -0.01340 0.01250  96  ARG A CD  
822  N  NE  . ARG A 93  ? 0.12103 0.07943 0.13343 -0.00920 -0.01060 0.01030  96  ARG A NE  
823  C  CZ  . ARG A 93  ? 0.12993 0.07183 0.11563 -0.01540 -0.00190 0.00200  96  ARG A CZ  
824  N  NH1 . ARG A 93  ? 0.15213 0.11053 0.10743 -0.01690 0.01140  -0.00090 96  ARG A NH1 
825  N  NH2 . ARG A 93  ? 0.12253 0.09193 0.13103 -0.00980 -0.01060 0.00810  96  ARG A NH2 
826  N  N   . THR A 94  ? 0.11853 0.07683 0.12213 0.00130  0.00380  -0.00650 97  THR A N   
827  C  CA  . THR A 94  ? 0.13863 0.07883 0.12013 -0.00450 -0.00210 -0.00420 97  THR A CA  
828  C  C   . THR A 94  ? 0.13133 0.07923 0.11403 0.01050  0.00500  -0.00750 97  THR A C   
829  O  O   . THR A 94  ? 0.11983 0.08903 0.11813 0.00910  0.01490  -0.00800 97  THR A O   
830  C  CB  . THR A 94  ? 0.13173 0.09403 0.12903 0.00270  -0.00360 0.00510  97  THR A CB  
831  O  OG1 . THR A 94  ? 0.12743 0.11013 0.14483 -0.00620 -0.01450 0.01240  97  THR A OG1 
832  C  CG2 . THR A 94  ? 0.14993 0.09473 0.14473 0.00810  -0.00160 0.01680  97  THR A CG2 
833  N  N   . ILE A 95  ? 0.12903 0.06753 0.11213 0.01290  0.00490  -0.00070 98  ILE A N   
834  C  CA  . ILE A 95  ? 0.12333 0.08703 0.11453 0.00020  -0.01810 0.00430  98  ILE A CA  
835  C  C   . ILE A 95  ? 0.10823 0.09103 0.12113 0.01630  -0.00720 -0.00400 98  ILE A C   
836  O  O   . ILE A 95  ? 0.11183 0.10353 0.13173 0.00200  0.00270  0.00200  98  ILE A O   
837  C  CB  . ILE A 95  ? 0.12693 0.08693 0.13343 -0.00030 -0.00710 0.00550  98  ILE A CB  
838  C  CG1 . ILE A 95  ? 0.11883 0.08973 0.13753 0.00750  0.01250  0.00690  98  ILE A CG1 
839  C  CG2 . ILE A 95  ? 0.10943 0.10433 0.13023 -0.01020 -0.02080 -0.00390 98  ILE A CG2 
840  C  CD1 . ILE A 95  ? 0.13823 0.11203 0.11993 -0.00780 0.00470  0.00430  98  ILE A CD1 
841  N  N   . SER A 96  ? 0.12613 0.07923 0.12093 -0.01820 0.00980  -0.01520 99  SER A N   
842  C  CA  . SER A 96  ? 0.12343 0.09363 0.11463 -0.00590 0.00330  -0.01110 99  SER A CA  
843  C  C   . SER A 96  ? 0.10603 0.09083 0.12303 0.00710  -0.00470 0.00870  99  SER A C   
844  O  O   . SER A 96  ? 0.10283 0.10253 0.12973 0.00020  -0.00170 0.01350  99  SER A O   
845  C  CB  . SER A 96  ? 0.13393 0.10803 0.12603 -0.00610 -0.00910 -0.01880 99  SER A CB  
846  O  OG  . SER A 96  ? 0.13543 0.11633 0.14243 -0.00210 -0.00980 -0.00130 99  SER A OG  
847  N  N   . PHE A 97  ? 0.12333 0.07663 0.12913 0.00050  -0.00320 -0.00100 100 PHE A N   
848  C  CA  . PHE A 97  ? 0.12353 0.08783 0.12643 -0.00510 -0.00620 -0.01240 100 PHE A CA  
849  C  C   . PHE A 97  ? 0.12133 0.09413 0.12113 0.01100  -0.02010 -0.01030 100 PHE A C   
850  O  O   . PHE A 97  ? 0.12553 0.09203 0.13793 -0.00280 -0.01620 0.00290  100 PHE A O   
851  C  CB  . PHE A 97  ? 0.11543 0.09773 0.12893 0.01300  0.00870  -0.01680 100 PHE A CB  
852  C  CG  . PHE A 97  ? 0.10883 0.09123 0.12623 0.00320  0.00060  0.00410  100 PHE A CG  
853  C  CD1 . PHE A 97  ? 0.12113 0.09883 0.11823 0.00440  0.01300  0.00010  100 PHE A CD1 
854  C  CD2 . PHE A 97  ? 0.10343 0.11033 0.12703 0.00210  0.01350  -0.00840 100 PHE A CD2 
855  C  CE1 . PHE A 97  ? 0.11413 0.11683 0.10993 -0.01850 0.01380  -0.00380 100 PHE A CE1 
856  C  CE2 . PHE A 97  ? 0.10363 0.08813 0.12133 0.01260  0.01540  0.00500  100 PHE A CE2 
857  C  CZ  . PHE A 97  ? 0.10413 0.10263 0.13023 0.01460  0.00270  0.00150  100 PHE A CZ  
858  N  N   . LYS A 98  ? 0.11283 0.08413 0.14143 0.00080  -0.00850 -0.00520 101 LYS A N   
859  C  CA  . LYS A 98  ? 0.09873 0.08993 0.16383 -0.00220 -0.00530 -0.00590 101 LYS A CA  
860  C  C   . LYS A 98  ? 0.11463 0.10303 0.17483 -0.00710 -0.01570 -0.01250 101 LYS A C   
861  O  O   . LYS A 98  ? 0.12493 0.11153 0.16423 -0.01610 -0.02230 -0.01150 101 LYS A O   
862  C  CB  . LYS A 98  ? 0.11093 0.10453 0.16823 -0.02320 0.00160  0.00840  101 LYS A CB  
863  C  CG  . LYS A 98  ? 0.13993 0.11383 0.18543 -0.01370 -0.01590 0.00030  101 LYS A CG  
864  C  CD  . LYS A 98  ? 0.17433 0.12553 0.18953 -0.02700 -0.01530 0.00920  101 LYS A CD  
865  C  CE  . LYS A 98  ? 0.18553 0.15263 0.19653 -0.01860 0.00660  0.02990  101 LYS A CE  
866  N  NZ  . LYS A 98  ? 0.22303 0.18413 0.20993 -0.00980 0.01490  0.02710  101 LYS A NZ  
867  N  N   . ASP A 99  ? 0.13033 0.08143 0.19043 0.01080  -0.00380 -0.00720 102 ASP A N   
868  C  CA  . ASP A 99  ? 0.14043 0.09543 0.21253 -0.01040 -0.00010 -0.02010 102 ASP A CA  
869  C  C   . ASP A 99  ? 0.15313 0.08703 0.19683 -0.00380 0.00100  -0.01480 102 ASP A C   
870  O  O   . ASP A 99  ? 0.16853 0.10163 0.20123 -0.00230 -0.00070 -0.04970 102 ASP A O   
871  C  CB  . ASP A 99  ? 0.16143 0.10713 0.21843 -0.02930 -0.02100 -0.01190 102 ASP A CB  
872  C  CG  . ASP A 99  ? 0.16743 0.11173 0.22533 -0.02210 -0.03950 -0.00220 102 ASP A CG  
873  O  OD1 . ASP A 99  ? 0.18803 0.14663 0.23843 -0.03240 -0.03140 0.00390  102 ASP A OD1 
874  O  OD2 . ASP A 99  ? 0.17043 0.15243 0.23723 -0.00320 -0.01160 -0.00490 102 ASP A OD2 
875  N  N   . ASP A 100 ? 0.13753 0.08503 0.18153 -0.00660 -0.01040 -0.02450 103 ASP A N   
876  C  CA  . ASP A 100 ? 0.11033 0.10043 0.17893 -0.00720 -0.01710 -0.02450 103 ASP A CA  
877  C  C   . ASP A 100 ? 0.12163 0.10873 0.18083 0.00540  -0.00860 -0.02020 103 ASP A C   
878  O  O   . ASP A 100 ? 0.13303 0.12183 0.17823 -0.00110 -0.00590 0.00760  103 ASP A O   
879  C  CB  . ASP A 100 ? 0.11443 0.11763 0.17233 0.01010  -0.00250 -0.01020 103 ASP A CB  
880  C  CG  . ASP A 100 ? 0.12093 0.13033 0.17233 0.02850  -0.00490 -0.01010 103 ASP A CG  
881  O  OD1 . ASP A 100 ? 0.11563 0.12173 0.17203 0.02680  0.00580  -0.02930 103 ASP A OD1 
882  O  OD2 . ASP A 100 ? 0.12863 0.17663 0.18383 0.01930  -0.00840 -0.00330 103 ASP A OD2 
883  N  N   . GLY A 101 ? 0.10293 0.08753 0.17213 0.00890  -0.00820 -0.01680 104 GLY A N   
884  C  CA  . GLY A 101 ? 0.10973 0.09053 0.16363 0.01100  0.00390  -0.02140 104 GLY A CA  
885  C  C   . GLY A 101 ? 0.11953 0.08843 0.15423 0.02210  0.00310  -0.01430 104 GLY A C   
886  O  O   . GLY A 101 ? 0.12003 0.10633 0.13833 0.01570  0.00660  -0.01720 104 GLY A O   
887  N  N   . ASN A 102 ? 0.13463 0.09543 0.14423 0.00630  -0.00460 -0.01610 105 ASN A N   
888  C  CA  . ASN A 102 ? 0.13863 0.09933 0.12973 -0.00240 0.00320  -0.00420 105 ASN A CA  
889  C  C   . ASN A 102 ? 0.12253 0.09003 0.12973 0.01210  0.01070  -0.00960 105 ASN A C   
890  O  O   . ASN A 102 ? 0.12663 0.08683 0.13753 0.00940  -0.00000 -0.00590 105 ASN A O   
891  C  CB  . ASN A 102 ? 0.14293 0.12613 0.14253 -0.00850 -0.00360 0.01270  105 ASN A CB  
892  C  CG  . ASN A 102 ? 0.15383 0.14743 0.14693 -0.02390 -0.00890 0.02580  105 ASN A CG  
893  O  OD1 . ASN A 102 ? 0.14703 0.20613 0.15363 -0.03940 -0.01780 0.02810  105 ASN A OD1 
894  N  ND2 . ASN A 102 ? 0.14463 0.16553 0.18683 0.00040  -0.01300 0.05540  105 ASN A ND2 
895  N  N   . TYR A 103 ? 0.11253 0.09453 0.12733 0.00230  0.00560  0.00380  106 TYR A N   
896  C  CA  . TYR A 103 ? 0.12783 0.09443 0.12503 -0.01400 0.00350  0.00330  106 TYR A CA  
897  C  C   . TYR A 103 ? 0.10903 0.08953 0.12543 0.00490  0.01260  0.00180  106 TYR A C   
898  O  O   . TYR A 103 ? 0.11223 0.10603 0.13323 0.00260  0.01490  -0.01060 106 TYR A O   
899  C  CB  . TYR A 103 ? 0.10753 0.10853 0.12973 0.00690  -0.00210 0.01750  106 TYR A CB  
900  C  CG  . TYR A 103 ? 0.11303 0.09303 0.12583 0.00380  0.01170  0.00150  106 TYR A CG  
901  C  CD1 . TYR A 103 ? 0.12093 0.10943 0.11883 -0.00870 0.01320  -0.00280 106 TYR A CD1 
902  C  CD2 . TYR A 103 ? 0.11693 0.08663 0.12673 -0.00460 0.01090  0.00430  106 TYR A CD2 
903  C  CE1 . TYR A 103 ? 0.10633 0.12263 0.10493 0.00740  0.00170  0.00460  106 TYR A CE1 
904  C  CE2 . TYR A 103 ? 0.11033 0.09463 0.11743 -0.00140 0.01610  -0.00150 106 TYR A CE2 
905  C  CZ  . TYR A 103 ? 0.11183 0.10783 0.11443 -0.00980 0.00970  0.00580  106 TYR A CZ  
906  O  OH  . TYR A 103 ? 0.13683 0.11893 0.11173 -0.01130 0.00500  -0.00110 106 TYR A OH  
907  N  N   . LYS A 104 ? 0.12263 0.08403 0.12053 -0.00520 0.00300  0.00090  107 LYS A N   
908  C  CA  . LYS A 104 ? 0.14443 0.09153 0.11523 -0.00960 -0.00410 -0.00610 107 LYS A CA  
909  C  C   . LYS A 104 ? 0.09823 0.10213 0.12703 -0.00210 0.00710  -0.01580 107 LYS A C   
910  O  O   . LYS A 104 ? 0.09923 0.10003 0.14223 0.00270  0.00960  -0.00700 107 LYS A O   
911  C  CB  . LYS A 104 ? 0.17593 0.11563 0.13143 0.01320  -0.01740 0.00040  107 LYS A CB  
912  C  CG  . LYS A 104 ? 0.19763 0.14413 0.13013 0.00800  0.00620  0.03490  107 LYS A CG  
913  C  CD  . LYS A 104 ? 0.21733 0.18383 0.15993 -0.01530 -0.01170 0.03060  107 LYS A CD  
914  C  CE  . LYS A 104 ? 0.22753 0.19733 0.17423 -0.02460 -0.02170 0.03530  107 LYS A CE  
915  N  NZ  . LYS A 104 ? 0.21523 0.22463 0.17513 -0.04000 -0.02520 0.04120  107 LYS A NZ  
916  N  N   . THR A 105 ? 0.10103 0.08843 0.13043 0.00990  0.01250  -0.00470 108 THR A N   
917  C  CA  . THR A 105 ? 0.11753 0.09613 0.12353 0.00540  0.01170  0.01150  108 THR A CA  
918  C  C   . THR A 105 ? 0.11823 0.10053 0.11893 0.01370  0.00990  0.00470  108 THR A C   
919  O  O   . THR A 105 ? 0.12673 0.10403 0.13373 -0.00270 0.01440  -0.01200 108 THR A O   
920  C  CB  . THR A 105 ? 0.11073 0.11243 0.12943 0.01580  0.00730  -0.00230 108 THR A CB  
921  O  OG1 . THR A 105 ? 0.10433 0.10363 0.13443 0.00260  0.00570  -0.00230 108 THR A OG1 
922  C  CG2 . THR A 105 ? 0.14173 0.09283 0.12483 0.00390  0.00480  -0.01740 108 THR A CG2 
923  N  N   . ARG A 106 ? 0.12723 0.09733 0.13183 0.00080  -0.00000 0.00420  109 ARG A N   
924  C  CA  A ARG A 106 ? 0.12443 0.10003 0.14643 0.00360  -0.01190 -0.00080 109 ARG A CA  
926  C  C   . ARG A 106 ? 0.12123 0.10023 0.12623 -0.01300 0.00670  -0.00440 109 ARG A C   
927  O  O   . ARG A 106 ? 0.12813 0.09443 0.12853 -0.00140 0.02360  -0.00770 109 ARG A O   
928  C  CB  A ARG A 106 ? 0.12873 0.13343 0.17043 -0.01430 -0.01950 0.00710  109 ARG A CB  
930  C  CG  A ARG A 106 ? 0.15163 0.15553 0.19313 0.00500  -0.04420 0.02750  109 ARG A CG  
932  C  CD  A ARG A 106 ? 0.21153 0.18883 0.22863 0.02010  -0.05200 0.02390  109 ARG A CD  
934  N  NE  A ARG A 106 ? 0.28903 0.24983 0.27423 0.01900  -0.04340 0.02520  109 ARG A NE  
936  C  CZ  A ARG A 106 ? 0.33443 0.30083 0.30973 0.01540  -0.02940 0.02350  109 ARG A CZ  
938  N  NH1 A ARG A 106 ? 0.34043 0.31193 0.32643 0.01110  -0.03280 0.01740  109 ARG A NH1 
940  N  NH2 A ARG A 106 ? 0.35443 0.32313 0.31843 0.01080  -0.01180 0.03220  109 ARG A NH2 
942  N  N   . ALA A 107 ? 0.13513 0.08903 0.13163 0.00350  0.00080  -0.01850 110 ALA A N   
943  C  CA  . ALA A 107 ? 0.15553 0.10733 0.13753 -0.00060 0.00040  -0.01570 110 ALA A CA  
944  C  C   . ALA A 107 ? 0.13393 0.11693 0.12933 -0.01300 0.01230  -0.01220 110 ALA A C   
945  O  O   . ALA A 107 ? 0.13283 0.12513 0.14673 -0.01230 0.00330  -0.01480 110 ALA A O   
946  C  CB  . ALA A 107 ? 0.13003 0.11293 0.14563 0.01000  -0.00060 -0.00590 110 ALA A CB  
947  N  N   . GLU A 108 ? 0.14543 0.10083 0.12643 0.00790  -0.01290 -0.01130 111 GLU A N   
948  C  CA  . GLU A 108 ? 0.15053 0.10043 0.13933 -0.01310 -0.02830 -0.01790 111 GLU A CA  
949  C  C   . GLU A 108 ? 0.14963 0.09673 0.13853 -0.00720 0.00480  -0.01800 111 GLU A C   
950  O  O   . GLU A 108 ? 0.16043 0.11213 0.13233 0.00110  0.00360  -0.00860 111 GLU A O   
951  C  CB  . GLU A 108 ? 0.19773 0.14083 0.18113 -0.03290 -0.03920 -0.01530 111 GLU A CB  
952  C  CG  . GLU A 108 ? 0.23853 0.18993 0.24093 -0.04050 -0.03540 -0.03290 111 GLU A CG  
953  C  CD  . GLU A 108 ? 0.27893 0.26453 0.28403 -0.04970 -0.05010 -0.04910 111 GLU A CD  
954  O  OE1 . GLU A 108 ? 0.29003 0.27883 0.30643 -0.06610 -0.04290 -0.04810 111 GLU A OE1 
955  O  OE2 . GLU A 108 ? 0.30103 0.33103 0.30653 -0.00680 -0.06060 -0.04420 111 GLU A OE2 
956  N  N   . VAL A 109 ? 0.14173 0.08213 0.13453 -0.00370 -0.00050 -0.01480 112 VAL A N   
957  C  CA  . VAL A 109 ? 0.13003 0.09263 0.14363 -0.00510 -0.00460 -0.00470 112 VAL A CA  
958  C  C   . VAL A 109 ? 0.14213 0.09233 0.14243 -0.00850 -0.00120 -0.01180 112 VAL A C   
959  O  O   . VAL A 109 ? 0.16663 0.10873 0.12683 0.00000  -0.00110 -0.00910 112 VAL A O   
960  C  CB  . VAL A 109 ? 0.14173 0.09743 0.15013 -0.02620 0.01240  -0.00530 112 VAL A CB  
961  C  CG1 . VAL A 109 ? 0.15093 0.10933 0.14073 0.00510  0.00230  -0.00660 112 VAL A CG1 
962  C  CG2 . VAL A 109 ? 0.17263 0.10573 0.14343 -0.02880 0.01950  -0.00710 112 VAL A CG2 
963  N  N   . LYS A 110 ? 0.14413 0.07953 0.14483 -0.00090 0.00350  -0.00990 113 LYS A N   
964  C  CA  . LYS A 110 ? 0.15313 0.08773 0.15273 -0.02270 -0.00540 -0.00600 113 LYS A CA  
965  C  C   . LYS A 110 ? 0.14713 0.08883 0.15013 -0.03650 -0.00170 -0.01010 113 LYS A C   
966  O  O   . LYS A 110 ? 0.15433 0.11153 0.14293 -0.00890 -0.00830 -0.01140 113 LYS A O   
967  C  CB  . LYS A 110 ? 0.13893 0.12843 0.16653 -0.00350 -0.01680 -0.00760 113 LYS A CB  
968  C  CG  . LYS A 110 ? 0.13253 0.17063 0.19923 -0.00020 -0.03760 0.00670  113 LYS A CG  
969  C  CD  . LYS A 110 ? 0.19063 0.25223 0.26513 0.00330  -0.03290 0.02860  113 LYS A CD  
970  C  CE  . LYS A 110 ? 0.30783 0.34573 0.34973 -0.00740 -0.04230 0.04540  113 LYS A CE  
972  N  N   . PHE A 111 ? 0.15493 0.09273 0.16263 -0.03060 -0.00230 -0.00840 114 PHE A N   
973  C  CA  . PHE A 111 ? 0.15813 0.10233 0.17083 -0.01600 0.01170  0.00700  114 PHE A CA  
974  C  C   . PHE A 111 ? 0.15063 0.11203 0.16003 -0.01700 -0.01620 0.00740  114 PHE A C   
975  O  O   . PHE A 111 ? 0.17753 0.12373 0.16003 -0.02910 -0.01210 0.00400  114 PHE A O   
976  C  CB  . PHE A 111 ? 0.15393 0.10333 0.18183 0.00490  -0.00700 -0.01320 114 PHE A CB  
977  C  CG  . PHE A 111 ? 0.15953 0.10843 0.17313 0.00650  -0.01800 -0.00670 114 PHE A CG  
978  C  CD1 . PHE A 111 ? 0.17273 0.12133 0.17433 0.01170  -0.00760 -0.01610 114 PHE A CD1 
979  C  CD2 . PHE A 111 ? 0.18693 0.10773 0.18533 -0.00150 -0.03060 0.00290  114 PHE A CD2 
980  C  CE1 . PHE A 111 ? 0.17013 0.11493 0.17463 0.02610  0.01780  -0.01430 114 PHE A CE1 
981  C  CE2 . PHE A 111 ? 0.17153 0.10793 0.19083 0.01350  0.01080  0.00720  114 PHE A CE2 
982  C  CZ  . PHE A 111 ? 0.17613 0.10463 0.18203 0.02280  0.01260  -0.00270 114 PHE A CZ  
983  N  N   . GLU A 112 ? 0.14563 0.10483 0.16113 -0.02070 0.02680  -0.00190 115 GLU A N   
984  C  CA  . GLU A 112 ? 0.15543 0.11733 0.19173 -0.03380 0.02380  0.00870  115 GLU A CA  
985  C  C   . GLU A 112 ? 0.18543 0.12693 0.19483 -0.03290 -0.00170 0.00970  115 GLU A C   
986  O  O   . GLU A 112 ? 0.20093 0.14483 0.19263 -0.04580 -0.01090 0.01200  115 GLU A O   
987  C  CB  . GLU A 112 ? 0.15013 0.13513 0.21473 -0.01760 0.01520  0.00300  115 GLU A CB  
988  C  CG  . GLU A 112 ? 0.18403 0.14173 0.23183 -0.02240 -0.01350 0.02460  115 GLU A CG  
989  C  CD  . GLU A 112 ? 0.21873 0.15253 0.26923 -0.02260 -0.03280 0.04480  115 GLU A CD  
990  O  OE1 . GLU A 112 ? 0.18843 0.17503 0.28633 -0.03960 -0.03630 0.03780  115 GLU A OE1 
991  O  OE2 . GLU A 112 ? 0.24873 0.16683 0.30143 -0.01730 -0.05130 0.02040  115 GLU A OE2 
992  N  N   . GLY A 113 ? 0.19303 0.10693 0.19403 -0.03010 -0.01170 -0.00550 116 GLY A N   
993  C  CA  . GLY A 113 ? 0.21953 0.11703 0.21903 -0.01150 -0.03280 0.01480  116 GLY A CA  
994  C  C   . GLY A 113 ? 0.23173 0.09733 0.23803 -0.02910 -0.03540 0.01240  116 GLY A C   
995  O  O   . GLY A 113 ? 0.25823 0.15503 0.25763 -0.01470 -0.03780 0.01520  116 GLY A O   
996  N  N   . ASP A 114 ? 0.23943 0.10703 0.26383 -0.02420 -0.04440 0.01880  117 ASP A N   
997  C  CA  . ASP A 114 ? 0.24803 0.12643 0.27063 -0.01010 -0.05720 0.03110  117 ASP A CA  
998  C  C   . ASP A 114 ? 0.23363 0.12373 0.23103 -0.02150 -0.03750 0.00630  117 ASP A C   
999  O  O   . ASP A 114 ? 0.24013 0.13303 0.21943 -0.01240 -0.02580 0.00600  117 ASP A O   
1000 C  CB  . ASP A 114 ? 0.32623 0.20843 0.35183 -0.01210 -0.06590 0.04620  117 ASP A CB  
1001 C  CG  . ASP A 114 ? 0.40863 0.35253 0.43793 -0.03380 -0.04270 0.06940  117 ASP A CG  
1002 O  OD1 . ASP A 114 ? 0.37873 0.31733 0.42793 -0.06280 -0.03390 0.08660  117 ASP A OD1 
1004 N  N   . THR A 115 ? 0.23073 0.11223 0.20133 -0.02190 -0.02410 0.01550  118 THR A N   
1005 C  CA  . THR A 115 ? 0.20443 0.11103 0.19563 -0.02710 -0.01620 0.01450  118 THR A CA  
1006 C  C   . THR A 115 ? 0.16463 0.09753 0.17363 -0.01670 0.00270  -0.00400 118 THR A C   
1007 O  O   . THR A 115 ? 0.15583 0.10983 0.16163 -0.01400 -0.00690 0.00630  118 THR A O   
1008 C  CB  . THR A 115 ? 0.22243 0.13683 0.19203 -0.02730 -0.01240 0.03610  118 THR A CB  
1009 O  OG1 . THR A 115 ? 0.27263 0.16703 0.21123 -0.03420 0.00170  0.04820  118 THR A OG1 
1010 C  CG2 . THR A 115 ? 0.21353 0.13693 0.21243 -0.02060 -0.01250 0.01090  118 THR A CG2 
1011 N  N   . LEU A 116 ? 0.13603 0.09633 0.15723 -0.01600 0.01280  -0.00440 119 LEU A N   
1012 C  CA  . LEU A 116 ? 0.12733 0.09493 0.15593 -0.00310 0.01690  0.00280  119 LEU A CA  
1013 C  C   . LEU A 116 ? 0.12443 0.09763 0.14623 -0.00070 0.00990  -0.00250 119 LEU A C   
1014 O  O   . LEU A 116 ? 0.14403 0.09763 0.14213 0.00090  0.00630  0.00060  119 LEU A O   
1015 C  CB  . LEU A 116 ? 0.12993 0.12523 0.15263 -0.00920 0.01600  0.00040  119 LEU A CB  
1016 C  CG  . LEU A 116 ? 0.14333 0.11893 0.14743 0.00140  0.01770  -0.00890 119 LEU A CG  
1017 C  CD1 . LEU A 116 ? 0.14073 0.10303 0.14943 0.01530  0.00810  -0.01930 119 LEU A CD1 
1018 C  CD2 . LEU A 116 ? 0.15863 0.13413 0.14843 0.01010  0.01300  -0.01890 119 LEU A CD2 
1019 N  N   . VAL A 117 ? 0.12123 0.09583 0.16123 -0.00630 -0.00440 -0.00480 120 VAL A N   
1020 C  CA  . VAL A 117 ? 0.13323 0.10023 0.15433 -0.00010 0.01380  -0.01420 120 VAL A CA  
1021 C  C   . VAL A 117 ? 0.12133 0.10663 0.13543 -0.00540 0.00680  -0.00680 120 VAL A C   
1022 O  O   . VAL A 117 ? 0.16083 0.11913 0.12353 -0.00690 0.02130  -0.00950 120 VAL A O   
1023 C  CB  . VAL A 117 ? 0.13333 0.11833 0.19543 -0.00440 0.02230  -0.01610 120 VAL A CB  
1024 C  CG1 . VAL A 117 ? 0.16423 0.15693 0.22243 -0.00180 0.02510  -0.00660 120 VAL A CG1 
1025 C  CG2 . VAL A 117 ? 0.15393 0.11083 0.19333 -0.04100 0.01980  0.00290  120 VAL A CG2 
1026 N  N   . ASN A 118 ? 0.14273 0.08933 0.14823 -0.01580 0.00930  -0.01160 121 ASN A N   
1027 C  CA  . ASN A 118 ? 0.13323 0.08363 0.14743 -0.02260 0.00260  -0.00350 121 ASN A CA  
1028 C  C   . ASN A 118 ? 0.13703 0.09103 0.14073 -0.01560 0.00770  -0.00760 121 ASN A C   
1029 O  O   . ASN A 118 ? 0.14703 0.11103 0.13723 -0.01490 0.02000  -0.01140 121 ASN A O   
1030 C  CB  . ASN A 118 ? 0.13953 0.08993 0.14573 -0.02640 0.00810  0.00450  121 ASN A CB  
1031 C  CG  . ASN A 118 ? 0.13253 0.09393 0.12183 -0.01470 0.00270  -0.00320 121 ASN A CG  
1032 O  OD1 . ASN A 118 ? 0.14483 0.10283 0.11903 -0.01410 0.01220  0.00470  121 ASN A OD1 
1033 N  ND2 . ASN A 118 ? 0.13203 0.09653 0.14123 -0.00610 0.01170  -0.01470 121 ASN A ND2 
1034 N  N   . ARG A 119 ? 0.13143 0.09413 0.12543 0.01660  0.02290  -0.00270 122 ARG A N   
1035 C  CA  A ARG A 119 ? 0.11533 0.08743 0.15093 -0.01890 0.01510  0.00470  122 ARG A CA  
1037 C  C   . ARG A 119 ? 0.12713 0.10173 0.13623 -0.00050 0.00920  -0.00220 122 ARG A C   
1038 O  O   . ARG A 119 ? 0.18123 0.11353 0.12913 -0.00240 0.01110  -0.01200 122 ARG A O   
1039 C  CB  A ARG A 119 ? 0.13613 0.10543 0.16083 -0.02630 0.01340  -0.01740 122 ARG A CB  
1041 C  CG  A ARG A 119 ? 0.15213 0.09973 0.15713 -0.02070 -0.00450 -0.00050 122 ARG A CG  
1043 C  CD  A ARG A 119 ? 0.16063 0.10673 0.16583 -0.03800 -0.01420 0.02130  122 ARG A CD  
1045 N  NE  A ARG A 119 ? 0.17273 0.13333 0.16083 -0.02540 0.00240  0.02980  122 ARG A NE  
1047 C  CZ  A ARG A 119 ? 0.17833 0.13523 0.18103 -0.02120 -0.01040 0.02430  122 ARG A CZ  
1049 N  NH1 A ARG A 119 ? 0.17873 0.13263 0.18233 -0.02600 -0.02470 0.00520  122 ARG A NH1 
1051 N  NH2 A ARG A 119 ? 0.19943 0.13283 0.20643 -0.01700 -0.00350 0.02170  122 ARG A NH2 
1053 N  N   . ILE A 120 ? 0.13043 0.10263 0.14703 0.01120  0.01280  -0.00530 123 ILE A N   
1054 C  CA  . ILE A 120 ? 0.11683 0.08773 0.15493 -0.00380 0.00590  -0.01260 123 ILE A CA  
1055 C  C   . ILE A 120 ? 0.12713 0.09573 0.13263 -0.01740 0.00100  -0.01340 123 ILE A C   
1056 O  O   . ILE A 120 ? 0.13323 0.11603 0.12413 -0.00230 0.01530  -0.01190 123 ILE A O   
1057 C  CB  . ILE A 120 ? 0.10603 0.11653 0.18423 0.00180  -0.03620 -0.01260 123 ILE A CB  
1058 C  CG1 . ILE A 120 ? 0.11553 0.13683 0.17153 0.00780  -0.03180 -0.01460 123 ILE A CG1 
1059 C  CG2 . ILE A 120 ? 0.09473 0.14653 0.23603 -0.00600 -0.03390 -0.00880 123 ILE A CG2 
1060 C  CD1 . ILE A 120 ? 0.14813 0.14373 0.16683 0.02160  -0.00660 0.03100  123 ILE A CD1 
1061 N  N   . GLU A 121 ? 0.11783 0.09433 0.15153 -0.01560 0.00550  -0.02180 124 GLU A N   
1062 C  CA  A GLU A 121 ? 0.14783 0.13243 0.23333 -0.01170 -0.01510 -0.01430 124 GLU A CA  
1064 C  C   . GLU A 121 ? 0.11773 0.09123 0.14463 0.00590  0.00320  0.00210  124 GLU A C   
1065 O  O   . GLU A 121 ? 0.14253 0.11253 0.14503 0.00280  0.03840  -0.01240 124 GLU A O   
1066 C  CB  A GLU A 121 ? 0.27263 0.27323 0.38563 0.00040  -0.04190 -0.02540 124 GLU A CB  
1068 C  CG  A GLU A 121 ? 0.46613 0.47113 0.54123 0.00750  -0.04980 -0.03050 124 GLU A CG  
1076 N  N   . LEU A 122 ? 0.11283 0.07193 0.14773 0.00800  0.00530  -0.01040 125 LEU A N   
1077 C  CA  . LEU A 122 ? 0.12963 0.09513 0.13533 0.00460  -0.01210 -0.00530 125 LEU A CA  
1078 C  C   . LEU A 122 ? 0.10883 0.09053 0.13193 -0.00900 -0.00470 -0.00070 125 LEU A C   
1079 O  O   . LEU A 122 ? 0.12173 0.11463 0.13983 -0.00070 0.02330  -0.00450 125 LEU A O   
1080 C  CB  . LEU A 122 ? 0.12943 0.10713 0.14443 -0.00130 -0.01700 -0.00290 125 LEU A CB  
1081 C  CG  . LEU A 122 ? 0.12813 0.09863 0.14653 0.00160  0.00230  -0.00120 125 LEU A CG  
1082 C  CD1 . LEU A 122 ? 0.12993 0.12773 0.13653 0.00800  -0.00730 0.00620  125 LEU A CD1 
1083 C  CD2 . LEU A 122 ? 0.12213 0.10183 0.15603 -0.00060 0.02690  -0.01060 125 LEU A CD2 
1084 N  N   . LYS A 123 ? 0.11683 0.08933 0.13783 -0.00220 -0.00660 0.00200  126 LYS A N   
1085 C  CA  . LYS A 123 ? 0.10293 0.10003 0.15423 0.00990  -0.01270 -0.01790 126 LYS A CA  
1086 C  C   . LYS A 123 ? 0.10633 0.09543 0.14193 0.00040  -0.00730 -0.01490 126 LYS A C   
1087 O  O   . LYS A 123 ? 0.12393 0.11433 0.13913 0.00090  0.01720  -0.00810 126 LYS A O   
1088 C  CB  . LYS A 123 ? 0.12583 0.10613 0.20143 -0.00250 -0.03850 -0.00430 126 LYS A CB  
1089 C  CG  . LYS A 123 ? 0.19493 0.17983 0.24143 0.03230  -0.05940 -0.01820 126 LYS A CG  
1090 C  CD  . LYS A 123 ? 0.28213 0.28783 0.32113 0.05740  -0.10460 -0.03250 126 LYS A CD  
1093 N  N   . GLY A 124 ? 0.12093 0.07993 0.13763 -0.00270 -0.00220 0.00450  127 GLY A N   
1094 C  CA  . GLY A 124 ? 0.11213 0.08673 0.14433 0.01230  0.00320  -0.00310 127 GLY A CA  
1095 C  C   . GLY A 124 ? 0.10443 0.09213 0.14333 0.01780  -0.00120 -0.00580 127 GLY A C   
1096 O  O   . GLY A 124 ? 0.12683 0.11783 0.15013 0.03190  0.02050  0.00260  127 GLY A O   
1097 N  N   A ILE A 125 ? 0.12013 0.06023 0.16063 0.00100  -0.01120 0.00460  128 ILE A N   
1099 C  CA  A ILE A 125 ? 0.14393 0.07383 0.16343 0.01150  -0.00310 0.01310  128 ILE A CA  
1101 C  C   A ILE A 125 ? 0.13323 0.09053 0.15513 0.03180  0.00190  0.00240  128 ILE A C   
1103 O  O   A ILE A 125 ? 0.13293 0.10223 0.15403 0.02160  0.01480  0.00590  128 ILE A O   
1105 C  CB  A ILE A 125 ? 0.17243 0.11373 0.17103 0.03290  -0.01340 0.00460  128 ILE A CB  
1107 C  CG1 A ILE A 125 ? 0.16273 0.13373 0.17433 0.03670  -0.02290 0.00180  128 ILE A CG1 
1109 C  CG2 A ILE A 125 ? 0.21243 0.13583 0.16383 0.03080  -0.02140 -0.00850 128 ILE A CG2 
1111 C  CD1 A ILE A 125 ? 0.18393 0.16503 0.19203 0.00380  -0.02880 0.00380  128 ILE A CD1 
1113 N  N   . ASP A 126 ? 0.12983 0.09243 0.15143 0.00980  -0.00570 0.00530  129 ASP A N   
1114 C  CA  . ASP A 126 ? 0.14563 0.10063 0.16283 -0.00170 -0.00360 -0.01140 129 ASP A CA  
1115 C  C   . ASP A 126 ? 0.12203 0.10333 0.16493 0.00580  -0.01270 -0.01450 129 ASP A C   
1116 O  O   . ASP A 126 ? 0.13373 0.12493 0.17583 -0.00110 0.00800  -0.01410 129 ASP A O   
1117 C  CB  . ASP A 126 ? 0.16013 0.14503 0.15703 0.00040  0.00960  -0.00020 129 ASP A CB  
1118 C  CG  . ASP A 126 ? 0.23283 0.20753 0.19793 0.03680  0.00750  0.00310  129 ASP A CG  
1119 O  OD1 . ASP A 126 ? 0.24243 0.24663 0.22543 0.01770  -0.00730 0.01030  129 ASP A OD1 
1120 O  OD2 . ASP A 126 ? 0.29783 0.25063 0.23473 0.07210  0.00690  -0.00680 129 ASP A OD2 
1121 N  N   . PHE A 127 ? 0.12763 0.10813 0.15313 0.00880  -0.00780 -0.02660 130 PHE A N   
1122 C  CA  . PHE A 127 ? 0.15043 0.10123 0.14563 0.02420  -0.00850 -0.02290 130 PHE A CA  
1123 C  C   . PHE A 127 ? 0.13103 0.11293 0.15503 0.03040  0.00370  -0.02730 130 PHE A C   
1124 O  O   . PHE A 127 ? 0.13633 0.12453 0.16883 0.01750  -0.00350 -0.02020 130 PHE A O   
1125 C  CB  . PHE A 127 ? 0.14523 0.10983 0.14963 0.04120  0.00600  -0.00550 130 PHE A CB  
1126 C  CG  . PHE A 127 ? 0.12053 0.10333 0.15483 0.03230  -0.00240 -0.00340 130 PHE A CG  
1127 C  CD1 . PHE A 127 ? 0.10973 0.09963 0.15263 0.00930  0.00320  0.00880  130 PHE A CD1 
1128 C  CD2 . PHE A 127 ? 0.12683 0.10873 0.15263 0.03640  0.00290  0.00450  130 PHE A CD2 
1129 C  CE1 . PHE A 127 ? 0.10573 0.11903 0.14873 0.02110  0.00690  0.00020  130 PHE A CE1 
1130 C  CE2 . PHE A 127 ? 0.12363 0.10443 0.13553 0.00970  -0.00140 0.01090  130 PHE A CE2 
1131 C  CZ  . PHE A 127 ? 0.10473 0.09943 0.13883 -0.01110 0.00170  0.00300  130 PHE A CZ  
1132 N  N   . LYS A 128 ? 0.14683 0.12303 0.16393 -0.00080 -0.00330 -0.01750 131 LYS A N   
1133 C  CA  . LYS A 128 ? 0.15613 0.12373 0.17133 0.00020  -0.00250 -0.03450 131 LYS A CA  
1134 C  C   . LYS A 128 ? 0.15803 0.13363 0.16783 0.02330  0.01230  -0.04560 131 LYS A C   
1135 O  O   . LYS A 128 ? 0.18303 0.14843 0.18573 0.03350  0.01010  -0.04080 131 LYS A O   
1136 C  CB  . LYS A 128 ? 0.15523 0.15283 0.18923 -0.00980 -0.00240 -0.02300 131 LYS A CB  
1137 C  CG  . LYS A 128 ? 0.19933 0.18563 0.20803 -0.03790 0.00070  -0.02070 131 LYS A CG  
1138 C  CD  . LYS A 128 ? 0.24403 0.20293 0.23783 -0.03850 0.00420  -0.01280 131 LYS A CD  
1139 C  CE  . LYS A 128 ? 0.28963 0.22343 0.27283 -0.00390 0.01860  0.00520  131 LYS A CE  
1140 N  NZ  . LYS A 128 ? 0.32903 0.24363 0.29793 0.00340  0.02200  0.00840  131 LYS A NZ  
1141 N  N   . GLU A 129 ? 0.15183 0.15933 0.17513 -0.00740 0.02820  -0.05920 132 GLU A N   
1142 C  CA  . GLU A 129 ? 0.14713 0.19013 0.18053 0.03770  0.01980  -0.04520 132 GLU A CA  
1143 C  C   . GLU A 129 ? 0.18163 0.21913 0.18993 0.05680  0.00710  -0.05510 132 GLU A C   
1144 O  O   . GLU A 129 ? 0.21463 0.24173 0.19773 0.04480  0.00860  -0.02690 132 GLU A O   
1145 C  CB  . GLU A 129 ? 0.15753 0.20353 0.18583 0.04210  0.00800  -0.03570 132 GLU A CB  
1146 C  CG  . GLU A 129 ? 0.15163 0.19723 0.17823 0.02900  -0.00120 -0.00120 132 GLU A CG  
1147 C  CD  . GLU A 129 ? 0.17933 0.20093 0.17263 0.01870  0.01900  -0.00130 132 GLU A CD  
1148 O  OE1 . GLU A 129 ? 0.23863 0.24193 0.17833 -0.00030 0.01860  0.00210  132 GLU A OE1 
1149 O  OE2 . GLU A 129 ? 0.17213 0.15323 0.17793 0.02930  -0.01070 -0.02990 132 GLU A OE2 
1150 N  N   . ASP A 130 ? 0.17683 0.21633 0.21123 0.06280  -0.02300 -0.09180 133 ASP A N   
1151 C  CA  . ASP A 130 ? 0.20253 0.23213 0.24153 0.05640  -0.03720 -0.09760 133 ASP A CA  
1152 C  C   . ASP A 130 ? 0.18493 0.18453 0.22183 0.04060  -0.04300 -0.07400 133 ASP A C   
1153 O  O   . ASP A 130 ? 0.19393 0.19553 0.23663 0.02320  -0.03970 -0.07390 133 ASP A O   
1154 C  CB  . ASP A 130 ? 0.25133 0.26203 0.29603 0.06320  -0.05520 -0.10710 133 ASP A CB  
1155 C  CG  . ASP A 130 ? 0.33463 0.30673 0.34403 0.05150  -0.04790 -0.10810 133 ASP A CG  
1156 O  OD1 . ASP A 130 ? 0.34363 0.28773 0.34993 0.05470  -0.03190 -0.10610 133 ASP A OD1 
1158 N  N   . GLY A 131 ? 0.18393 0.15083 0.20093 0.05270  -0.01980 -0.05950 134 GLY A N   
1159 C  CA  . GLY A 131 ? 0.16993 0.16043 0.20203 0.06220  -0.02230 -0.04140 134 GLY A CA  
1160 C  C   . GLY A 131 ? 0.15893 0.14243 0.17153 0.04310  -0.02750 -0.05110 134 GLY A C   
1161 O  O   . GLY A 131 ? 0.18863 0.14753 0.17493 0.02400  -0.00530 -0.04940 134 GLY A O   
1162 N  N   . ASN A 132 ? 0.15813 0.14883 0.16723 0.03860  -0.02280 -0.05080 135 ASN A N   
1163 C  CA  . ASN A 132 ? 0.15273 0.15643 0.15113 0.03100  -0.01190 -0.03490 135 ASN A CA  
1164 C  C   . ASN A 132 ? 0.16093 0.16163 0.12833 0.03610  -0.02550 -0.02410 135 ASN A C   
1165 O  O   . ASN A 132 ? 0.15953 0.18853 0.14353 0.04090  -0.03020 -0.01520 135 ASN A O   
1166 C  CB  . ASN A 132 ? 0.14803 0.17093 0.15823 0.01660  -0.02180 -0.03730 135 ASN A CB  
1167 C  CG  . ASN A 132 ? 0.16463 0.18363 0.15973 0.00200  -0.02260 -0.03230 135 ASN A CG  
1168 O  OD1 . ASN A 132 ? 0.19503 0.23053 0.16903 -0.02730 -0.02890 -0.03680 135 ASN A OD1 
1169 N  ND2 . ASN A 132 ? 0.17923 0.18183 0.17463 0.00160  -0.04350 -0.00860 135 ASN A ND2 
1170 N  N   . ILE A 133 ? 0.14283 0.13603 0.13363 0.01630  -0.01690 -0.03010 136 ILE A N   
1171 C  CA  A ILE A 133 ? 0.14953 0.14013 0.13503 0.00710  -0.00560 -0.01340 136 ILE A CA  
1173 C  C   . ILE A 133 ? 0.13363 0.15603 0.13963 0.01730  0.00750  0.00540  136 ILE A C   
1174 O  O   . ILE A 133 ? 0.17253 0.17203 0.16083 0.02850  0.00770  0.02200  136 ILE A O   
1175 C  CB  A ILE A 133 ? 0.13943 0.13173 0.15093 0.01060  -0.00170 -0.02270 136 ILE A CB  
1177 C  CG1 A ILE A 133 ? 0.11023 0.10603 0.16003 0.01780  -0.00340 -0.02190 136 ILE A CG1 
1179 C  CG2 A ILE A 133 ? 0.15203 0.13413 0.16413 0.00830  -0.01420 -0.00380 136 ILE A CG2 
1181 C  CD1 A ILE A 133 ? 0.15163 0.11993 0.17863 -0.02400 0.02080  -0.03290 136 ILE A CD1 
1183 N  N   . LEU A 134 ? 0.15033 0.18973 0.14653 0.03670  0.01850  0.02210  137 LEU A N   
1184 C  CA  . LEU A 134 ? 0.16593 0.21793 0.13413 0.05940  0.01740  -0.01380 137 LEU A CA  
1185 C  C   . LEU A 134 ? 0.16673 0.27383 0.14463 0.07050  0.00610  -0.02200 137 LEU A C   
1186 O  O   . LEU A 134 ? 0.17443 0.32233 0.13893 0.06670  0.01040  -0.00560 137 LEU A O   
1187 C  CB  . LEU A 134 ? 0.17843 0.18893 0.14333 0.04990  0.00320  -0.01260 137 LEU A CB  
1188 C  CG  . LEU A 134 ? 0.20213 0.16293 0.16983 0.03990  0.00330  -0.00220 137 LEU A CG  
1189 C  CD1 . LEU A 134 ? 0.17293 0.14163 0.16443 0.03280  -0.00210 0.00920  137 LEU A CD1 
1190 C  CD2 . LEU A 134 ? 0.25083 0.15133 0.18393 0.03730  0.01470  0.00590  137 LEU A CD2 
1191 N  N   . GLY A 135 ? 0.18513 0.24153 0.14313 0.05550  -0.01030 -0.03810 138 GLY A N   
1192 C  CA  . GLY A 135 ? 0.17783 0.29983 0.14223 0.08320  -0.01810 -0.03750 138 GLY A CA  
1193 C  C   . GLY A 135 ? 0.17563 0.34283 0.15573 0.06330  0.00760  -0.01920 138 GLY A C   
1194 O  O   . GLY A 135 ? 0.18263 0.37733 0.15953 0.06000  -0.01160 -0.02520 138 GLY A O   
1195 N  N   . HIS A 136 ? 0.17143 0.33173 0.16643 0.04980  0.00590  -0.00220 139 HIS A N   
1196 C  CA  . HIS A 136 ? 0.14583 0.31903 0.15783 0.04860  0.00420  0.00020  139 HIS A CA  
1197 C  C   . HIS A 136 ? 0.17523 0.30393 0.14563 0.05530  0.00860  -0.02220 139 HIS A C   
1198 O  O   . HIS A 136 ? 0.20483 0.35843 0.14343 0.02120  -0.00920 -0.01200 139 HIS A O   
1199 C  CB  . HIS A 136 ? 0.13953 0.33133 0.16783 0.01860  0.00930  -0.00770 139 HIS A CB  
1200 C  CG  . HIS A 136 ? 0.17413 0.33603 0.18593 0.00560  -0.01680 -0.00860 139 HIS A CG  
1201 N  ND1 . HIS A 136 ? 0.19783 0.32903 0.20413 -0.00930 -0.03110 0.00710  139 HIS A ND1 
1202 C  CD2 . HIS A 136 ? 0.19283 0.33883 0.20213 0.01480  -0.03100 -0.01540 139 HIS A CD2 
1203 C  CE1 . HIS A 136 ? 0.21953 0.33013 0.20473 0.00080  -0.05300 -0.01510 139 HIS A CE1 
1204 N  NE2 . HIS A 136 ? 0.20793 0.33903 0.21773 0.00370  -0.03340 -0.01900 139 HIS A NE2 
1205 N  N   . LYS A 137 ? 0.16113 0.23623 0.17423 0.04750  0.00190  -0.02210 140 LYS A N   
1206 C  CA  . LYS A 137 ? 0.16413 0.18503 0.17473 0.04510  -0.00790 -0.01220 140 LYS A CA  
1207 C  C   . LYS A 137 ? 0.14863 0.16313 0.15863 0.01830  -0.02940 -0.01570 140 LYS A C   
1208 O  O   . LYS A 137 ? 0.14423 0.15733 0.20423 0.00080  -0.02020 -0.05010 140 LYS A O   
1209 C  CB  . LYS A 137 ? 0.18153 0.20063 0.17683 0.06510  -0.01980 -0.01660 140 LYS A CB  
1210 C  CG  . LYS A 137 ? 0.23653 0.21513 0.21193 0.07280  -0.01510 -0.02630 140 LYS A CG  
1211 C  CD  . LYS A 137 ? 0.27423 0.20953 0.23983 0.07150  -0.00660 -0.04020 140 LYS A CD  
1212 C  CE  . LYS A 137 ? 0.32003 0.22833 0.26353 0.05830  -0.03170 -0.02180 140 LYS A CE  
1213 N  NZ  . LYS A 137 ? 0.35693 0.24483 0.26993 0.03640  -0.04530 -0.02550 140 LYS A NZ  
1214 N  N   A LEU A 138 ? 0.14963 0.15443 0.14523 -0.03010 -0.02320 -0.00790 141 LEU A N   
1216 C  CA  A LEU A 138 ? 0.16923 0.14823 0.12863 -0.03560 -0.01190 -0.02240 141 LEU A CA  
1218 C  C   A LEU A 138 ? 0.17653 0.13303 0.11493 -0.03280 0.00460  -0.00600 141 LEU A C   
1220 O  O   A LEU A 138 ? 0.18823 0.14633 0.12953 -0.01330 0.01530  0.01580  141 LEU A O   
1222 C  CB  A LEU A 138 ? 0.16733 0.17123 0.14453 -0.04960 -0.00610 -0.01680 141 LEU A CB  
1224 C  CG  A LEU A 138 ? 0.15623 0.14773 0.14153 -0.02930 -0.00110 -0.01240 141 LEU A CG  
1226 C  CD1 A LEU A 138 ? 0.15013 0.14933 0.11923 -0.02320 -0.00370 -0.02270 141 LEU A CD1 
1228 C  CD2 A LEU A 138 ? 0.14403 0.11683 0.15273 -0.04240 -0.00550 -0.02990 141 LEU A CD2 
1230 N  N   . GLU A 139 ? 0.15293 0.13273 0.12163 -0.00590 -0.00780 -0.01440 142 GLU A N   
1231 C  CA  A GLU A 139 ? 0.16623 0.13123 0.13803 -0.02680 -0.02770 -0.00490 142 GLU A CA  
1233 C  C   . GLU A 139 ? 0.15653 0.12593 0.13063 -0.00570 -0.02880 -0.00430 142 GLU A C   
1234 O  O   . GLU A 139 ? 0.15633 0.13123 0.11993 -0.01450 -0.02350 -0.01520 142 GLU A O   
1235 C  CB  A GLU A 139 ? 0.18283 0.15653 0.16053 -0.05300 -0.04560 0.00270  142 GLU A CB  
1237 C  CG  A GLU A 139 ? 0.20753 0.15623 0.18413 -0.04620 -0.05020 0.01680  142 GLU A CG  
1239 C  CD  A GLU A 139 ? 0.23073 0.16963 0.20863 -0.05330 -0.04550 0.00520  142 GLU A CD  
1241 O  OE1 A GLU A 139 ? 0.21073 0.17923 0.24253 -0.04470 -0.03690 0.00990  142 GLU A OE1 
1243 O  OE2 A GLU A 139 ? 0.26003 0.19293 0.21193 -0.06180 -0.05170 -0.00910 142 GLU A OE2 
1245 N  N   . TYR A 140 ? 0.15523 0.12783 0.11553 -0.00060 -0.01270 0.00150  143 TYR A N   
1246 C  CA  . TYR A 140 ? 0.14613 0.12373 0.11813 0.00290  -0.00050 -0.01180 143 TYR A CA  
1247 C  C   . TYR A 140 ? 0.14533 0.12973 0.12143 -0.00230 -0.00690 -0.01450 143 TYR A C   
1248 O  O   . TYR A 140 ? 0.15363 0.14983 0.13813 0.00880  -0.01870 0.01300  143 TYR A O   
1249 C  CB  . TYR A 140 ? 0.16053 0.13633 0.14273 -0.02340 0.00360  -0.00810 143 TYR A CB  
1250 C  CG  . TYR A 140 ? 0.15613 0.13143 0.11173 -0.00760 0.01100  -0.01800 143 TYR A CG  
1251 C  CD1 . TYR A 140 ? 0.15703 0.12973 0.11533 -0.01900 -0.00680 -0.03100 143 TYR A CD1 
1252 C  CD2 . TYR A 140 ? 0.15663 0.14393 0.12573 0.01230  0.00810  -0.00190 143 TYR A CD2 
1253 C  CE1 . TYR A 140 ? 0.16053 0.12983 0.11403 -0.01050 -0.02020 -0.01590 143 TYR A CE1 
1254 C  CE2 . TYR A 140 ? 0.14443 0.14223 0.10713 -0.00820 -0.00330 -0.01190 143 TYR A CE2 
1255 C  CZ  . TYR A 140 ? 0.13823 0.13203 0.11173 0.00030  -0.01490 -0.00970 143 TYR A CZ  
1256 O  OH  . TYR A 140 ? 0.16533 0.13333 0.12283 -0.01320 -0.02400 0.00070  143 TYR A OH  
1257 N  N   . ASN A 141 ? 0.14353 0.13863 0.12933 0.00580  0.00130  -0.00600 144 ASN A N   
1258 C  CA  A ASN A 141 ? 0.14043 0.15983 0.14143 0.01680  -0.00600 0.00660  144 ASN A CA  
1260 C  C   . ASN A 141 ? 0.14293 0.14123 0.13963 0.02450  -0.00540 0.00270  144 ASN A C   
1261 O  O   . ASN A 141 ? 0.15953 0.14533 0.14123 0.01450  -0.00490 -0.00180 144 ASN A O   
1262 C  CB  A ASN A 141 ? 0.13553 0.17573 0.17673 0.00200  -0.01440 0.00790  144 ASN A CB  
1264 C  CG  A ASN A 141 ? 0.14423 0.18523 0.19743 0.00110  -0.01650 0.01010  144 ASN A CG  
1266 O  OD1 A ASN A 141 ? 0.17813 0.19603 0.19503 0.00100  0.02690  0.03570  144 ASN A OD1 
1268 N  ND2 A ASN A 141 ? 0.18623 0.19013 0.23263 0.00550  -0.01890 0.00900  144 ASN A ND2 
1270 N  N   . TYR A 142 ? 0.15633 0.14473 0.14233 0.01060  0.00840  -0.00780 145 TYR A N   
1271 C  CA  . TYR A 142 ? 0.12693 0.14693 0.14073 0.02300  0.00320  -0.01420 145 TYR A CA  
1272 C  C   . TYR A 142 ? 0.12253 0.17323 0.15803 0.03340  -0.00610 0.00610  145 TYR A C   
1273 O  O   . TYR A 142 ? 0.16133 0.23273 0.17213 0.05230  0.02350  0.03260  145 TYR A O   
1274 C  CB  . TYR A 142 ? 0.13623 0.14103 0.14283 0.01350  -0.00530 0.01040  145 TYR A CB  
1275 C  CG  . TYR A 142 ? 0.14633 0.12313 0.14253 0.01320  -0.00960 -0.00850 145 TYR A CG  
1276 C  CD1 . TYR A 142 ? 0.13593 0.11333 0.14723 -0.00190 0.00630  0.00800  145 TYR A CD1 
1277 C  CD2 . TYR A 142 ? 0.14143 0.10563 0.13383 -0.00440 0.00120  -0.00650 145 TYR A CD2 
1278 C  CE1 . TYR A 142 ? 0.13403 0.10243 0.13283 0.00560  0.02080  0.01690  145 TYR A CE1 
1279 C  CE2 . TYR A 142 ? 0.11663 0.11343 0.14263 -0.00550 -0.00890 -0.01030 145 TYR A CE2 
1280 C  CZ  . TYR A 142 ? 0.10813 0.12053 0.13423 -0.02020 0.00130  -0.00360 145 TYR A CZ  
1281 O  OH  . TYR A 142 ? 0.12543 0.12773 0.14603 -0.01730 -0.00750 -0.00160 145 TYR A OH  
1282 N  N   . ASN A 143 ? 0.14333 0.15593 0.14883 -0.01200 0.00720  -0.00990 146 ASN A N   
1283 C  CA  . ASN A 143 ? 0.13653 0.13953 0.15893 0.00090  0.01340  -0.00900 146 ASN A CA  
1284 C  C   . ASN A 143 ? 0.12193 0.13553 0.15213 0.01550  -0.00720 -0.01560 146 ASN A C   
1285 O  O   . ASN A 143 ? 0.14973 0.14403 0.17093 0.01630  -0.01920 -0.00840 146 ASN A O   
1286 C  CB  . ASN A 143 ? 0.15953 0.14013 0.17983 -0.00250 0.00010  -0.01520 146 ASN A CB  
1287 C  CG  . ASN A 143 ? 0.17533 0.15453 0.21203 -0.01070 -0.02620 -0.01230 146 ASN A CG  
1288 O  OD1 . ASN A 143 ? 0.22353 0.19233 0.25553 -0.00010 -0.06340 -0.01320 146 ASN A OD1 
1289 N  ND2 . ASN A 143 ? 0.18173 0.14083 0.19833 -0.00310 -0.00370 -0.02140 146 ASN A ND2 
1290 N  N   . SER A 144 ? 0.15403 0.15393 0.16083 0.00820  0.00010  -0.02110 147 SER A N   
1291 C  CA  A SER A 144 ? 0.15423 0.16423 0.16953 0.01710  0.00460  -0.03100 147 SER A CA  
1293 C  C   . SER A 144 ? 0.14553 0.14013 0.15763 -0.00250 0.00810  -0.02460 147 SER A C   
1294 O  O   . SER A 144 ? 0.15193 0.16173 0.19173 -0.00420 -0.00030 -0.00750 147 SER A O   
1295 C  CB  A SER A 144 ? 0.17423 0.19823 0.18463 0.04030  -0.00160 -0.02980 147 SER A CB  
1297 O  OG  A SER A 144 ? 0.20623 0.21263 0.19743 0.02400  -0.01250 -0.03380 147 SER A OG  
1299 N  N   . HIS A 145 ? 0.15383 0.13273 0.16243 0.02200  0.00230  -0.02660 148 HIS A N   
1300 C  CA  . HIS A 145 ? 0.15063 0.12903 0.17703 0.01160  0.00240  -0.01260 148 HIS A CA  
1301 C  C   . HIS A 145 ? 0.14393 0.12483 0.15553 0.01280  0.00400  -0.00040 148 HIS A C   
1302 O  O   . HIS A 145 ? 0.17783 0.12813 0.16793 -0.00210 0.01100  0.00110  148 HIS A O   
1303 C  CB  . HIS A 145 ? 0.13933 0.12173 0.19173 0.02980  0.02090  -0.02360 148 HIS A CB  
1304 C  CG  . HIS A 145 ? 0.12633 0.11833 0.16513 -0.00120 0.02310  -0.00780 148 HIS A CG  
1305 N  ND1 . HIS A 145 ? 0.16513 0.12833 0.16043 0.00080  0.01780  -0.00690 148 HIS A ND1 
1306 C  CD2 . HIS A 145 ? 0.13893 0.11303 0.17203 0.00660  0.00940  -0.01470 148 HIS A CD2 
1307 C  CE1 . HIS A 145 ? 0.15303 0.12453 0.16503 0.01840  -0.01090 -0.01200 148 HIS A CE1 
1308 N  NE2 . HIS A 145 ? 0.12293 0.11333 0.16783 0.01990  -0.00840 -0.00630 148 HIS A NE2 
1309 N  N   . ASN A 146 ? 0.15363 0.14273 0.13803 -0.00390 0.00790  -0.01180 149 ASN A N   
1310 C  CA  . ASN A 146 ? 0.14313 0.15083 0.16233 -0.00010 0.00260  -0.01180 149 ASN A CA  
1311 C  C   . ASN A 146 ? 0.15393 0.12963 0.17353 0.01590  0.00260  -0.00030 149 ASN A C   
1312 O  O   . ASN A 146 ? 0.14563 0.13783 0.20213 0.00130  -0.01120 0.00150  149 ASN A O   
1313 C  CB  . ASN A 146 ? 0.14283 0.16673 0.19393 0.00890  0.00550  -0.01440 149 ASN A CB  
1314 C  CG  . ASN A 146 ? 0.16043 0.17723 0.21373 0.00050  0.00450  -0.00980 149 ASN A CG  
1315 O  OD1 . ASN A 146 ? 0.14713 0.20103 0.22563 0.00740  -0.00010 -0.01440 149 ASN A OD1 
1316 N  ND2 . ASN A 146 ? 0.18013 0.17343 0.25003 0.00190  0.01480  -0.01580 149 ASN A ND2 
1317 N  N   . VAL A 147 ? 0.13713 0.13273 0.15273 -0.00240 -0.01290 -0.03070 150 VAL A N   
1318 C  CA  . VAL A 147 ? 0.13653 0.12133 0.15313 0.00690  -0.00390 -0.02020 150 VAL A CA  
1319 C  C   . VAL A 147 ? 0.13433 0.11453 0.15833 0.02220  0.00680  -0.00780 150 VAL A C   
1320 O  O   . VAL A 147 ? 0.14823 0.11983 0.16803 0.01760  0.01040  -0.01370 150 VAL A O   
1321 C  CB  . VAL A 147 ? 0.13093 0.13123 0.16163 0.01010  0.01210  -0.00460 150 VAL A CB  
1322 C  CG1 . VAL A 147 ? 0.14163 0.12723 0.16883 0.00520  -0.01610 0.01040  150 VAL A CG1 
1323 C  CG2 . VAL A 147 ? 0.17843 0.16313 0.16303 0.00450  0.03570  -0.01630 150 VAL A CG2 
1324 N  N   . TYR A 148 ? 0.14673 0.13663 0.14243 0.00300  0.01190  -0.00810 151 TYR A N   
1325 C  CA  . TYR A 148 ? 0.11763 0.15063 0.14383 -0.01160 0.00700  0.00980  151 TYR A CA  
1326 C  C   . TYR A 148 ? 0.14293 0.14593 0.16293 0.00090  0.00720  0.00040  151 TYR A C   
1327 O  O   . TYR A 148 ? 0.14213 0.16643 0.19913 0.01660  -0.00670 -0.02300 151 TYR A O   
1328 C  CB  . TYR A 148 ? 0.13383 0.12543 0.16343 -0.02940 0.01430  0.01420  151 TYR A CB  
1329 C  CG  . TYR A 148 ? 0.13873 0.13723 0.17433 -0.01200 0.01860  -0.00350 151 TYR A CG  
1330 C  CD1 . TYR A 148 ? 0.14373 0.15353 0.20923 0.00710  -0.00010 0.00920  151 TYR A CD1 
1331 C  CD2 . TYR A 148 ? 0.14703 0.16443 0.17283 -0.03830 0.00620  -0.02100 151 TYR A CD2 
1332 C  CE1 . TYR A 148 ? 0.15763 0.17063 0.22233 -0.00810 0.00510  -0.00660 151 TYR A CE1 
1333 C  CE2 . TYR A 148 ? 0.13883 0.18463 0.20003 -0.04310 0.01720  -0.00640 151 TYR A CE2 
1334 C  CZ  . TYR A 148 ? 0.14443 0.18383 0.22063 -0.03120 0.00860  -0.01050 151 TYR A CZ  
1335 O  OH  . TYR A 148 ? 0.14763 0.21023 0.23613 -0.02600 0.00980  -0.01660 151 TYR A OH  
1336 N  N   . ILE A 149 ? 0.15043 0.14003 0.15073 0.00510  0.01070  -0.01690 152 ILE A N   
1337 C  CA  . ILE A 149 ? 0.14763 0.13913 0.16003 -0.01100 0.01100  -0.01520 152 ILE A CA  
1338 C  C   . ILE A 149 ? 0.12803 0.13193 0.16053 0.02810  0.00480  0.00550  152 ILE A C   
1339 O  O   . ILE A 149 ? 0.13343 0.16623 0.17143 0.01840  0.00030  -0.01100 152 ILE A O   
1340 C  CB  . ILE A 149 ? 0.16423 0.14303 0.16103 -0.00730 0.01240  -0.01680 152 ILE A CB  
1341 C  CG1 . ILE A 149 ? 0.20793 0.15083 0.16923 -0.01200 0.01400  -0.01710 152 ILE A CG1 
1342 C  CG2 . ILE A 149 ? 0.17123 0.14713 0.16743 -0.01760 -0.00480 -0.01960 152 ILE A CG2 
1343 C  CD1 . ILE A 149 ? 0.21523 0.16333 0.18713 0.01300  -0.00660 -0.01800 152 ILE A CD1 
1344 N  N   . THR A 150 ? 0.15763 0.14053 0.15703 0.00020  0.00760  -0.00020 153 THR A N   
1345 C  CA  A THR A 150 ? 0.19213 0.15863 0.16413 -0.01600 0.02450  0.01400  153 THR A CA  
1347 C  C   . THR A 150 ? 0.16393 0.15203 0.16173 0.00250  0.01060  0.01040  153 THR A C   
1348 O  O   . THR A 150 ? 0.15353 0.15673 0.15333 0.00190  0.00380  -0.01870 153 THR A O   
1349 C  CB  A THR A 150 ? 0.22933 0.17243 0.19883 -0.03230 0.04610  0.00420  153 THR A CB  
1351 O  OG1 A THR A 150 ? 0.25953 0.16293 0.22243 -0.01750 0.02960  0.00150  153 THR A OG1 
1353 C  CG2 A THR A 150 ? 0.23833 0.19423 0.20163 -0.02900 0.04100  -0.01460 153 THR A CG2 
1355 N  N   . ALA A 151 ? 0.16633 0.16723 0.15623 -0.00490 -0.00220 0.00580  154 ALA A N   
1356 C  CA  . ALA A 151 ? 0.15963 0.17013 0.16913 0.01040  0.00820  -0.00850 154 ALA A CA  
1357 C  C   . ALA A 151 ? 0.17603 0.18393 0.20133 0.01650  0.00880  0.01650  154 ALA A C   
1358 O  O   . ALA A 151 ? 0.20153 0.18773 0.23133 -0.00210 0.00370  0.03960  154 ALA A O   
1359 C  CB  . ALA A 151 ? 0.16893 0.19213 0.16553 0.01750  0.02320  -0.03610 154 ALA A CB  
1360 N  N   . ASP A 152 ? 0.16023 0.21303 0.20223 0.02060  -0.01380 0.02070  155 ASP A N   
1361 C  CA  . ASP A 152 ? 0.22403 0.25973 0.24613 0.03030  -0.01510 0.03970  155 ASP A CA  
1362 C  C   . ASP A 152 ? 0.26333 0.29053 0.26303 0.01460  -0.02600 0.03560  155 ASP A C   
1363 O  O   . ASP A 152 ? 0.26763 0.28823 0.25453 -0.00040 -0.04100 0.03390  155 ASP A O   
1364 C  CB  . ASP A 152 ? 0.23833 0.27813 0.27993 0.05690  -0.00420 0.04820  155 ASP A CB  
1365 C  CG  . ASP A 152 ? 0.28353 0.31243 0.30633 0.07580  -0.01030 0.05110  155 ASP A CG  
1366 O  OD1 . ASP A 152 ? 0.30533 0.34613 0.32493 0.07910  -0.02840 0.05350  155 ASP A OD1 
1367 O  OD2 . ASP A 152 ? 0.31433 0.31623 0.33233 0.09540  -0.02250 0.04400  155 ASP A OD2 
1368 N  N   . LYS A 153 ? 0.29723 0.31263 0.27633 0.02140  -0.02710 0.05530  156 LYS A N   
1369 C  CA  . LYS A 153 ? 0.35853 0.36503 0.33843 0.00780  -0.03790 0.05060  156 LYS A CA  
1370 C  C   . LYS A 153 ? 0.36763 0.36913 0.34143 -0.00480 -0.05010 0.04450  156 LYS A C   
1371 O  O   . LYS A 153 ? 0.37293 0.35423 0.33413 -0.00860 -0.06030 0.05270  156 LYS A O   
1372 C  CB  . LYS A 153 ? 0.40603 0.41983 0.40963 0.00630  -0.02920 0.04960  156 LYS A CB  
1375 N  N   . GLN A 154 ? 0.37953 0.38073 0.36143 -0.00810 -0.06530 0.04790  157 GLN A N   
1384 N  N   . LYS A 155 ? 0.36763 0.36973 0.38103 0.04870  -0.04710 0.00180  158 LYS A N   
1386 C  CA  B LYS A 155 ? 0.35213 0.35233 0.37583 0.04890  -0.04960 0.00010  158 LYS A CA  
1387 C  C   . LYS A 155 ? 0.29863 0.29873 0.33413 0.05930  -0.05110 -0.01090 158 LYS A C   
1388 O  O   . LYS A 155 ? 0.26983 0.29833 0.34493 0.11340  -0.04640 -0.01010 158 LYS A O   
1390 C  CB  B LYS A 155 ? 0.39543 0.39563 0.41033 0.03990  -0.04430 0.00060  158 LYS A CB  
1398 N  NZ  B LYS A 155 ? 0.43973 0.43433 0.44913 -0.00470 -0.00250 0.01860  158 LYS A NZ  
1399 N  N   . ASN A 156 ? 0.24823 0.20723 0.27113 0.03180  -0.04560 -0.03030 159 ASN A N   
1400 C  CA  . ASN A 156 ? 0.22943 0.18213 0.22113 0.00210  -0.03990 -0.02120 159 ASN A CA  
1401 C  C   . ASN A 156 ? 0.20963 0.17203 0.19293 0.00800  -0.00140 -0.02690 159 ASN A C   
1402 O  O   . ASN A 156 ? 0.23993 0.17293 0.18653 -0.00100 0.03740  -0.02780 159 ASN A O   
1403 C  CB  . ASN A 156 ? 0.24173 0.19493 0.23193 -0.01140 -0.04170 -0.02550 159 ASN A CB  
1404 C  CG  . ASN A 156 ? 0.24083 0.20343 0.21863 -0.01120 -0.06440 -0.02120 159 ASN A CG  
1405 O  OD1 . ASN A 156 ? 0.25573 0.19443 0.22953 -0.00440 -0.04130 -0.02450 159 ASN A OD1 
1406 N  ND2 . ASN A 156 ? 0.25633 0.20853 0.21833 -0.02480 -0.08450 0.00160  159 ASN A ND2 
1407 N  N   . GLY A 157 ? 0.20183 0.16383 0.17673 0.01600  0.00640  -0.04340 160 GLY A N   
1408 C  CA  . GLY A 157 ? 0.16873 0.16133 0.16623 -0.02100 0.03320  -0.02950 160 GLY A CA  
1409 C  C   . GLY A 157 ? 0.15683 0.13903 0.15113 0.00010  0.01540  -0.01010 160 GLY A C   
1410 O  O   . GLY A 157 ? 0.16523 0.15223 0.16643 0.00050  0.02460  -0.00270 160 GLY A O   
1411 N  N   . ILE A 158 ? 0.15953 0.12873 0.15523 0.00140  0.02270  -0.02490 161 ILE A N   
1414 C  C   . ILE A 158 ? 0.14253 0.13123 0.14163 0.01890  0.03800  -0.03150 161 ILE A C   
1415 O  O   . ILE A 158 ? 0.15093 0.13553 0.14713 0.00850  0.02290  -0.02470 161 ILE A O   
1424 N  N   . LYS A 159 ? 0.15533 0.12803 0.15623 0.00140  -0.00130 -0.04310 162 LYS A N   
1425 C  CA  A LYS A 159 ? 0.16543 0.15313 0.18113 0.00690  0.00050  -0.03920 162 LYS A CA  
1426 C  CA  B LYS A 159 ? 0.15293 0.13663 0.17503 0.00470  0.00510  -0.03200 162 LYS A CA  
1427 C  C   . LYS A 159 ? 0.14313 0.14073 0.17313 0.00960  0.00640  -0.04280 162 LYS A C   
1428 O  O   . LYS A 159 ? 0.15333 0.17553 0.18063 0.02670  0.00720  -0.05390 162 LYS A O   
1429 C  CB  A LYS A 159 ? 0.20633 0.18423 0.21613 0.01300  -0.00750 -0.03590 162 LYS A CB  
1430 C  CB  B LYS A 159 ? 0.17823 0.12423 0.20833 0.00850  -0.00180 -0.01190 162 LYS A CB  
1431 C  CG  A LYS A 159 ? 0.25543 0.23343 0.25403 0.01220  -0.01400 -0.02730 162 LYS A CG  
1432 C  CG  B LYS A 159 ? 0.23003 0.16873 0.24953 -0.00320 -0.00510 0.03040  162 LYS A CG  
1434 C  CD  B LYS A 159 ? 0.29223 0.25443 0.30723 -0.00290 -0.00760 0.03400  162 LYS A CD  
1436 C  CE  B LYS A 159 ? 0.36313 0.34903 0.37413 0.00230  -0.01060 0.03030  162 LYS A CE  
1439 N  N   . ALA A 160 ? 0.14243 0.15283 0.16833 0.01100  -0.00360 -0.03860 163 ALA A N   
1440 C  CA  . ALA A 160 ? 0.15673 0.14513 0.16183 0.01110  -0.01370 -0.01720 163 ALA A CA  
1441 C  C   . ALA A 160 ? 0.13363 0.15033 0.15823 -0.00340 0.00720  -0.01750 163 ALA A C   
1442 O  O   . ALA A 160 ? 0.13693 0.15003 0.16673 0.00990  0.01010  -0.01710 163 ALA A O   
1443 C  CB  . ALA A 160 ? 0.19013 0.16413 0.17263 0.02640  -0.01540 0.01030  163 ALA A CB  
1444 N  N   . ASN A 161 ? 0.15053 0.15173 0.14423 -0.00120 0.00380  -0.02840 164 ASN A N   
1445 C  CA  . ASN A 161 ? 0.17483 0.15813 0.17653 0.00610  -0.01690 -0.02290 164 ASN A CA  
1446 C  C   . ASN A 161 ? 0.11253 0.14703 0.18523 -0.00060 -0.00420 -0.02690 164 ASN A C   
1447 O  O   . ASN A 161 ? 0.12743 0.17003 0.18623 0.01150  -0.00310 -0.02630 164 ASN A O   
1448 C  CB  . ASN A 161 ? 0.24073 0.19303 0.21353 -0.00290 -0.04720 -0.00150 164 ASN A CB  
1449 C  CG  . ASN A 161 ? 0.30263 0.24983 0.25433 -0.03250 -0.04570 -0.00910 164 ASN A CG  
1450 O  OD1 . ASN A 161 ? 0.34313 0.28933 0.27643 -0.03980 -0.03360 -0.00050 164 ASN A OD1 
1451 N  ND2 . ASN A 161 ? 0.30373 0.26323 0.26053 -0.02760 -0.06720 0.00120  164 ASN A ND2 
1452 N  N   . PHE A 162 ? 0.12743 0.13603 0.17143 -0.00900 0.00160  -0.02390 165 PHE A N   
1453 C  CA  . PHE A 162 ? 0.12473 0.12423 0.15703 0.00540  -0.00650 -0.01370 165 PHE A CA  
1454 C  C   . PHE A 162 ? 0.12263 0.11673 0.15163 0.01180  0.00840  -0.01310 165 PHE A C   
1455 O  O   . PHE A 162 ? 0.12433 0.12833 0.16113 0.02190  -0.00930 -0.02320 165 PHE A O   
1456 C  CB  . PHE A 162 ? 0.13943 0.10693 0.17313 0.00370  0.00350  -0.01940 165 PHE A CB  
1457 C  CG  . PHE A 162 ? 0.10953 0.10963 0.17243 -0.00460 0.00470  -0.00660 165 PHE A CG  
1458 C  CD1 . PHE A 162 ? 0.12133 0.08893 0.19183 -0.00600 0.00520  -0.00030 165 PHE A CD1 
1459 C  CD2 . PHE A 162 ? 0.14683 0.09323 0.16783 0.01660  -0.00050 -0.00220 165 PHE A CD2 
1460 C  CE1 . PHE A 162 ? 0.13803 0.09903 0.17853 -0.00300 -0.01070 -0.00020 165 PHE A CE1 
1461 C  CE2 . PHE A 162 ? 0.13273 0.09233 0.16063 0.00190  -0.02250 -0.01600 165 PHE A CE2 
1462 C  CZ  . PHE A 162 ? 0.13243 0.10683 0.16673 0.02270  -0.02540 -0.01130 165 PHE A CZ  
1463 N  N   . LYS A 163 ? 0.13233 0.13203 0.13713 -0.00190 -0.00300 -0.01940 166 LYS A N   
1464 C  CA  . LYS A 163 ? 0.13553 0.11693 0.13983 -0.00540 0.01100  -0.01300 166 LYS A CA  
1465 C  C   . LYS A 163 ? 0.11673 0.12553 0.14953 0.02200  -0.00050 0.00090  166 LYS A C   
1466 O  O   . LYS A 163 ? 0.11263 0.17043 0.15633 0.02410  0.00530  0.02230  166 LYS A O   
1467 C  CB  . LYS A 163 ? 0.15803 0.14253 0.14723 -0.02950 0.00020  -0.00370 166 LYS A CB  
1468 C  CG  . LYS A 163 ? 0.17603 0.13233 0.14803 -0.00860 0.01870  0.02830  166 LYS A CG  
1469 C  CD  . LYS A 163 ? 0.20233 0.14663 0.17123 -0.01700 0.01010  0.04090  166 LYS A CD  
1470 C  CE  . LYS A 163 ? 0.20223 0.16343 0.18393 -0.02590 0.00480  0.04030  166 LYS A CE  
1471 N  NZ  . LYS A 163 ? 0.21653 0.19183 0.20783 -0.03090 -0.00440 0.03870  166 LYS A NZ  
1472 N  N   . ILE A 164 ? 0.11733 0.10733 0.14703 -0.00530 0.00450  -0.01060 167 ILE A N   
1473 C  CA  . ILE A 164 ? 0.11983 0.10283 0.14753 -0.01820 -0.00020 -0.01460 167 ILE A CA  
1474 C  C   . ILE A 164 ? 0.10263 0.09663 0.14403 -0.00730 0.00500  -0.01720 167 ILE A C   
1475 O  O   . ILE A 164 ? 0.11173 0.10463 0.15383 0.00610  -0.00890 -0.00650 167 ILE A O   
1476 C  CB  . ILE A 164 ? 0.11933 0.10503 0.14903 -0.01890 0.00680  -0.00550 167 ILE A CB  
1477 C  CG1 . ILE A 164 ? 0.12113 0.09553 0.15773 -0.01830 0.01540  -0.00570 167 ILE A CG1 
1478 C  CG2 . ILE A 164 ? 0.13343 0.12983 0.14533 -0.01810 0.00970  -0.00280 167 ILE A CG2 
1479 C  CD1 . ILE A 164 ? 0.13203 0.09313 0.15333 -0.00560 0.01660  -0.00690 167 ILE A CD1 
1480 N  N   . ARG A 165 ? 0.10273 0.10943 0.13143 -0.02970 0.00330  -0.00740 168 ARG A N   
1481 C  CA  . ARG A 165 ? 0.10633 0.10403 0.14093 -0.01400 0.01290  -0.00730 168 ARG A CA  
1482 C  C   . ARG A 165 ? 0.12733 0.09163 0.13693 -0.00990 0.00050  -0.00720 168 ARG A C   
1483 O  O   . ARG A 165 ? 0.14293 0.11913 0.14123 0.01580  0.00760  0.01160  168 ARG A O   
1484 C  CB  . ARG A 165 ? 0.12583 0.10543 0.14873 -0.00290 0.03250  -0.02120 168 ARG A CB  
1485 C  CG  . ARG A 165 ? 0.13053 0.12613 0.15963 -0.01400 0.02150  -0.02620 168 ARG A CG  
1486 C  CD  . ARG A 165 ? 0.13283 0.11443 0.18393 -0.00240 0.02160  -0.02190 168 ARG A CD  
1487 N  NE  . ARG A 165 ? 0.15203 0.12793 0.19483 -0.00130 0.01800  0.00080  168 ARG A NE  
1488 C  CZ  . ARG A 165 ? 0.12543 0.14493 0.19963 -0.01700 0.00790  0.00590  168 ARG A CZ  
1489 N  NH1 . ARG A 165 ? 0.13173 0.17553 0.19403 -0.01660 0.00280  0.00420  168 ARG A NH1 
1490 N  NH2 . ARG A 165 ? 0.13883 0.15193 0.20753 -0.01110 0.00890  -0.02020 168 ARG A NH2 
1491 N  N   . HIS A 166 ? 0.10813 0.10143 0.12303 -0.01440 0.00880  -0.01120 169 HIS A N   
1492 C  CA  . HIS A 166 ? 0.10913 0.12153 0.13443 -0.00080 0.00410  -0.00390 169 HIS A CA  
1493 C  C   . HIS A 166 ? 0.12413 0.10753 0.13333 -0.01580 0.00260  0.00960  169 HIS A C   
1494 O  O   . HIS A 166 ? 0.14983 0.09783 0.13893 -0.03210 -0.00430 0.00170  169 HIS A O   
1495 C  CB  . HIS A 166 ? 0.11303 0.11523 0.13073 -0.00480 0.00550  -0.02520 169 HIS A CB  
1496 C  CG  . HIS A 166 ? 0.12083 0.10603 0.13473 -0.01190 0.01770  -0.01310 169 HIS A CG  
1497 N  ND1 . HIS A 166 ? 0.10973 0.10163 0.12003 -0.02370 0.00630  -0.00400 169 HIS A ND1 
1498 C  CD2 . HIS A 166 ? 0.11403 0.11733 0.13393 -0.02780 0.00070  -0.02340 169 HIS A CD2 
1499 C  CE1 . HIS A 166 ? 0.10463 0.11373 0.11403 0.00060  -0.00160 -0.00670 169 HIS A CE1 
1500 N  NE2 . HIS A 166 ? 0.12683 0.11503 0.12713 -0.00660 0.01120  -0.01750 169 HIS A NE2 
1501 N  N   . ASN A 167 ? 0.13553 0.11253 0.13333 -0.00770 -0.01200 -0.00460 170 ASN A N   
1502 C  CA  . ASN A 167 ? 0.12873 0.11433 0.13643 0.00550  -0.02360 -0.02460 170 ASN A CA  
1503 C  C   . ASN A 167 ? 0.11943 0.10783 0.13653 -0.02730 -0.02470 -0.00920 170 ASN A C   
1504 O  O   . ASN A 167 ? 0.13373 0.11733 0.14823 -0.02740 -0.01180 0.00040  170 ASN A O   
1505 C  CB  . ASN A 167 ? 0.13013 0.12203 0.16303 -0.00510 -0.03820 -0.00190 170 ASN A CB  
1506 C  CG  . ASN A 167 ? 0.14323 0.17313 0.18033 0.04050  -0.04090 0.00310  170 ASN A CG  
1507 O  OD1 . ASN A 167 ? 0.21803 0.26303 0.21983 0.06310  -0.03000 0.02730  170 ASN A OD1 
1508 N  ND2 . ASN A 167 ? 0.11473 0.14563 0.20313 0.00520  -0.00140 0.01400  170 ASN A ND2 
1509 N  N   . ILE A 168 ? 0.14023 0.11403 0.13573 -0.02120 -0.00770 -0.01800 171 ILE A N   
1510 C  CA  A ILE A 168 ? 0.15913 0.10583 0.15143 -0.00550 -0.01060 -0.02320 171 ILE A CA  
1512 C  C   . ILE A 168 ? 0.16253 0.12523 0.14833 -0.01510 -0.01090 -0.01620 171 ILE A C   
1513 O  O   . ILE A 168 ? 0.14873 0.12853 0.14513 -0.00960 -0.01070 -0.00820 171 ILE A O   
1514 C  CB  A ILE A 168 ? 0.19363 0.09653 0.15273 0.00920  -0.01750 -0.04490 171 ILE A CB  
1516 C  CG1 A ILE A 168 ? 0.18043 0.12173 0.15633 0.00150  -0.03650 -0.03460 171 ILE A CG1 
1518 C  CG2 A ILE A 168 ? 0.21333 0.11593 0.14903 0.02570  -0.02830 -0.06350 171 ILE A CG2 
1520 C  CD1 A ILE A 168 ? 0.16703 0.13433 0.17853 -0.00250 -0.02920 -0.03430 171 ILE A CD1 
1522 N  N   . GLU A 169 ? 0.17293 0.12003 0.13833 -0.00550 -0.02300 -0.00440 172 GLU A N   
1523 C  CA  . GLU A 169 ? 0.15503 0.15533 0.15243 -0.00310 0.00530  -0.00380 172 GLU A CA  
1524 C  C   . GLU A 169 ? 0.18013 0.16753 0.14793 -0.02410 -0.00760 -0.02680 172 GLU A C   
1525 O  O   . GLU A 169 ? 0.19723 0.18103 0.17083 -0.02660 -0.02100 -0.03470 172 GLU A O   
1526 C  CB  . GLU A 169 ? 0.18613 0.22693 0.20613 0.01030  0.02260  -0.02750 172 GLU A CB  
1527 C  CG  . GLU A 169 ? 0.21913 0.26903 0.25433 0.03260  0.03440  -0.05740 172 GLU A CG  
1528 C  CD  . GLU A 169 ? 0.30693 0.34583 0.32363 0.01450  0.02870  -0.06730 172 GLU A CD  
1529 O  OE1 . GLU A 169 ? 0.28123 0.36133 0.30223 0.01430  0.03550  -0.08080 172 GLU A OE1 
1531 N  N   . ASP A 170 ? 0.20783 0.17063 0.16683 -0.04530 0.00350  -0.03740 173 ASP A N   
1532 C  CA  A ASP A 170 ? 0.24013 0.17063 0.16723 -0.06280 0.00670  -0.05980 173 ASP A CA  
1534 C  C   . ASP A 170 ? 0.23773 0.19583 0.17123 -0.09820 0.00300  -0.05540 173 ASP A C   
1535 O  O   . ASP A 170 ? 0.28173 0.23233 0.19473 -0.13210 0.04560  -0.06290 173 ASP A O   
1536 C  CB  A ASP A 170 ? 0.25493 0.16043 0.17373 -0.04000 0.00720  -0.05450 173 ASP A CB  
1538 C  CG  A ASP A 170 ? 0.24103 0.14433 0.18403 -0.03280 0.01320  -0.02920 173 ASP A CG  
1540 O  OD1 A ASP A 170 ? 0.26283 0.12873 0.17873 -0.02670 0.01620  -0.01740 173 ASP A OD1 
1542 O  OD2 A ASP A 170 ? 0.21133 0.13283 0.20783 -0.02660 0.02920  -0.01270 173 ASP A OD2 
1544 N  N   . GLY A 171 ? 0.19923 0.20023 0.15943 -0.07080 -0.01120 -0.02020 174 GLY A N   
1545 C  CA  . GLY A 171 ? 0.17833 0.20923 0.16463 -0.07110 -0.00400 -0.01150 174 GLY A CA  
1546 C  C   . GLY A 171 ? 0.16343 0.19483 0.17013 -0.07170 -0.01410 -0.01430 174 GLY A C   
1547 O  O   . GLY A 171 ? 0.16983 0.23133 0.20443 -0.04420 -0.02470 0.01700  174 GLY A O   
1548 N  N   . SER A 172 ? 0.18003 0.15943 0.15373 -0.05450 -0.03890 -0.03060 175 SER A N   
1549 C  CA  . SER A 172 ? 0.18553 0.15273 0.14233 -0.04670 -0.04200 -0.03320 175 SER A CA  
1550 C  C   . SER A 172 ? 0.15613 0.13903 0.12913 -0.03730 -0.02170 -0.02190 175 SER A C   
1551 O  O   . SER A 172 ? 0.16253 0.15503 0.15353 -0.04380 -0.00670 -0.00160 175 SER A O   
1552 C  CB  . SER A 172 ? 0.25783 0.15493 0.18013 -0.03460 -0.02330 -0.03650 175 SER A CB  
1553 O  OG  . SER A 172 ? 0.30733 0.16513 0.21333 0.00820  -0.01900 -0.02330 175 SER A OG  
1554 N  N   . VAL A 173 ? 0.11243 0.14233 0.12793 -0.03020 -0.00560 -0.03120 176 VAL A N   
1555 C  CA  . VAL A 173 ? 0.11683 0.11773 0.14303 -0.00970 -0.01100 -0.00820 176 VAL A CA  
1556 C  C   . VAL A 173 ? 0.12213 0.10123 0.13513 -0.02910 -0.00300 -0.00030 176 VAL A C   
1557 O  O   . VAL A 173 ? 0.12903 0.11593 0.14643 -0.01600 0.00220  -0.02080 176 VAL A O   
1558 C  CB  . VAL A 173 ? 0.12893 0.13753 0.15453 0.00880  -0.01010 -0.01370 176 VAL A CB  
1559 C  CG1 . VAL A 173 ? 0.13833 0.11183 0.18133 0.00800  -0.00960 -0.01130 176 VAL A CG1 
1560 C  CG2 . VAL A 173 ? 0.14293 0.15453 0.17263 0.01580  -0.01140 -0.00380 176 VAL A CG2 
1561 N  N   . GLN A 174 ? 0.11473 0.11233 0.12943 -0.01330 -0.01270 -0.00620 177 GLN A N   
1562 C  CA  . GLN A 174 ? 0.11353 0.10373 0.14063 -0.01410 -0.00160 -0.01950 177 GLN A CA  
1563 C  C   . GLN A 174 ? 0.11803 0.08583 0.13563 -0.00640 -0.00110 0.00490  177 GLN A C   
1564 O  O   . GLN A 174 ? 0.12073 0.09983 0.13703 -0.00670 -0.00930 -0.00020 177 GLN A O   
1565 C  CB  . GLN A 174 ? 0.11013 0.13343 0.12593 -0.00670 -0.00280 -0.00550 177 GLN A CB  
1566 C  CG  . GLN A 174 ? 0.10133 0.12283 0.14563 -0.00770 -0.01770 -0.01230 177 GLN A CG  
1567 C  CD  . GLN A 174 ? 0.12753 0.12233 0.13643 0.00250  -0.01200 -0.00750 177 GLN A CD  
1568 O  OE1 . GLN A 174 ? 0.16323 0.14333 0.14963 0.02210  -0.00290 -0.03010 177 GLN A OE1 
1569 N  NE2 . GLN A 174 ? 0.13743 0.12123 0.13393 -0.01550 -0.01680 0.00090  177 GLN A NE2 
1570 N  N   . LEU A 175 ? 0.11013 0.10883 0.11933 0.01360  -0.00560 -0.01060 178 LEU A N   
1571 C  CA  . LEU A 175 ? 0.10113 0.10623 0.14013 -0.00950 0.00610  -0.00700 178 LEU A CA  
1572 C  C   . LEU A 175 ? 0.10113 0.09143 0.12753 0.01730  -0.00150 -0.00750 178 LEU A C   
1573 O  O   . LEU A 175 ? 0.11923 0.08773 0.14603 -0.01000 -0.00550 -0.00930 178 LEU A O   
1574 C  CB  . LEU A 175 ? 0.10733 0.12593 0.15243 -0.01280 0.00980  -0.00470 178 LEU A CB  
1575 C  CG  . LEU A 175 ? 0.14013 0.12323 0.14243 0.00470  0.00600  -0.00020 178 LEU A CG  
1576 C  CD1 . LEU A 175 ? 0.16213 0.13723 0.15973 0.00630  0.01210  -0.01010 178 LEU A CD1 
1577 C  CD2 . LEU A 175 ? 0.18093 0.12263 0.15173 -0.01700 0.01530  0.00010  178 LEU A CD2 
1578 N  N   . ALA A 176 ? 0.12463 0.10523 0.12003 -0.00030 0.00170  -0.01570 179 ALA A N   
1579 C  CA  . ALA A 176 ? 0.11863 0.11773 0.11243 -0.00940 0.00460  -0.02960 179 ALA A CA  
1580 C  C   . ALA A 176 ? 0.11623 0.10933 0.12263 -0.00860 0.00130  -0.01220 179 ALA A C   
1581 O  O   . ALA A 176 ? 0.11913 0.09643 0.13533 0.00000  -0.00060 -0.01770 179 ALA A O   
1582 C  CB  . ALA A 176 ? 0.13733 0.13663 0.13203 -0.02100 0.02320  -0.02290 179 ALA A CB  
1583 N  N   . ASP A 177 ? 0.14703 0.10243 0.12513 -0.00930 -0.00530 0.00620  180 ASP A N   
1584 C  CA  . ASP A 177 ? 0.12343 0.10093 0.13103 -0.01170 -0.00670 0.00510  180 ASP A CA  
1585 C  C   . ASP A 177 ? 0.11353 0.10073 0.13403 -0.00250 -0.00140 0.01110  180 ASP A C   
1586 O  O   . ASP A 177 ? 0.12093 0.10293 0.14893 -0.00110 0.00740  -0.01490 180 ASP A O   
1587 C  CB  . ASP A 177 ? 0.13563 0.09813 0.13713 0.00170  -0.00630 0.01630  180 ASP A CB  
1588 C  CG  . ASP A 177 ? 0.13903 0.13493 0.15903 -0.00780 0.00340  0.02130  180 ASP A CG  
1589 O  OD1 . ASP A 177 ? 0.14573 0.11743 0.15223 -0.01130 0.00630  0.00970  180 ASP A OD1 
1590 O  OD2 . ASP A 177 ? 0.13483 0.18803 0.16643 0.00960  0.01150  0.01760  180 ASP A OD2 
1591 N  N   . HIS A 178 ? 0.12363 0.08603 0.13003 0.00270  0.00420  -0.00210 181 HIS A N   
1592 C  CA  . HIS A 178 ? 0.12803 0.09843 0.12773 -0.00360 0.00960  -0.00250 181 HIS A CA  
1593 C  C   . HIS A 178 ? 0.12433 0.11673 0.12563 0.00130  0.02860  -0.01140 181 HIS A C   
1594 O  O   . HIS A 178 ? 0.12213 0.13183 0.13313 -0.01060 0.01020  -0.01860 181 HIS A O   
1595 C  CB  . HIS A 178 ? 0.12773 0.08293 0.13143 0.01480  0.01330  0.00230  181 HIS A CB  
1596 C  CG  . HIS A 178 ? 0.11403 0.08873 0.12023 0.00600  0.00900  0.00900  181 HIS A CG  
1597 N  ND1 . HIS A 178 ? 0.11613 0.08153 0.11473 0.00870  0.00560  -0.00370 181 HIS A ND1 
1598 C  CD2 . HIS A 178 ? 0.10773 0.10573 0.11353 -0.00040 0.00220  0.00850  181 HIS A CD2 
1599 C  CE1 . HIS A 178 ? 0.11913 0.08793 0.11973 -0.01170 0.00980  0.00090  181 HIS A CE1 
1600 N  NE2 . HIS A 178 ? 0.10653 0.09483 0.09703 -0.00870 0.00540  0.00880  181 HIS A NE2 
1601 N  N   . TYR A 179 ? 0.11843 0.09703 0.12063 -0.00570 0.01850  -0.00130 182 TYR A N   
1602 C  CA  . TYR A 179 ? 0.12733 0.08923 0.11973 -0.00690 0.00450  -0.00320 182 TYR A CA  
1603 C  C   . TYR A 179 ? 0.09893 0.09363 0.12383 -0.00110 0.01190  -0.00020 182 TYR A C   
1604 O  O   . TYR A 179 ? 0.11553 0.08953 0.14203 -0.00410 0.01510  0.00620  182 TYR A O   
1605 C  CB  . TYR A 179 ? 0.16903 0.09803 0.12703 0.02030  -0.00160 -0.00210 182 TYR A CB  
1606 C  CG  . TYR A 179 ? 0.22343 0.10843 0.13733 0.03090  -0.01050 0.01230  182 TYR A CG  
1607 C  CD1 . TYR A 179 ? 0.28243 0.14263 0.13353 0.04940  0.00950  0.01170  182 TYR A CD1 
1608 C  CD2 . TYR A 179 ? 0.25693 0.14923 0.16003 0.03950  -0.06780 0.00900  182 TYR A CD2 
1609 C  CE1 . TYR A 179 ? 0.33203 0.17933 0.15693 0.04010  -0.01190 -0.00860 182 TYR A CE1 
1610 C  CE2 . TYR A 179 ? 0.30083 0.15993 0.16413 0.04320  -0.04990 0.00340  182 TYR A CE2 
1611 C  CZ  . TYR A 179 ? 0.33463 0.18033 0.14383 0.01970  -0.04420 -0.03470 182 TYR A CZ  
1612 O  OH  . TYR A 179 ? 0.39773 0.23213 0.16283 0.01620  -0.04240 -0.03570 182 TYR A OH  
1613 N  N   . GLN A 180 ? 0.13173 0.08913 0.10563 0.00140  0.00700  -0.00390 183 GLN A N   
1614 C  CA  . GLN A 180 ? 0.12543 0.07963 0.11213 -0.00060 0.00350  -0.00130 183 GLN A CA  
1615 C  C   . GLN A 180 ? 0.12903 0.07723 0.11933 -0.00690 0.01190  0.01190  183 GLN A C   
1616 O  O   . GLN A 180 ? 0.13023 0.09903 0.10993 -0.00460 0.01260  -0.00830 183 GLN A O   
1617 C  CB  . GLN A 180 ? 0.12663 0.08913 0.14063 -0.00320 -0.00930 0.00640  183 GLN A CB  
1618 C  CG  . GLN A 180 ? 0.13813 0.08803 0.12783 0.00120  -0.01460 0.01530  183 GLN A CG  
1619 C  CD  . GLN A 180 ? 0.12703 0.09343 0.13143 -0.00470 0.01340  -0.00150 183 GLN A CD  
1620 O  OE1 . GLN A 180 ? 0.13193 0.09473 0.13983 0.00370  0.00970  -0.00270 183 GLN A OE1 
1621 N  NE2 . GLN A 180 ? 0.16873 0.10803 0.15993 -0.01060 0.00410  0.00570  183 GLN A NE2 
1622 N  N   . GLN A 181 ? 0.12973 0.09063 0.14153 -0.00940 0.01240  -0.01050 184 GLN A N   
1623 C  CA  A GLN A 181 ? 0.16483 0.11153 0.14873 -0.01340 -0.01170 -0.01050 184 GLN A CA  
1625 C  C   . GLN A 181 ? 0.14723 0.11003 0.12723 -0.01880 0.00370  -0.00790 184 GLN A C   
1626 O  O   . GLN A 181 ? 0.15873 0.12563 0.15823 -0.03370 0.03580  -0.03780 184 GLN A O   
1627 C  CB  A GLN A 181 ? 0.21403 0.14203 0.17673 -0.01150 -0.04270 -0.05710 184 GLN A CB  
1629 C  CG  A GLN A 181 ? 0.26443 0.16823 0.21743 0.00780  -0.03900 -0.04430 184 GLN A CG  
1631 C  CD  A GLN A 181 ? 0.30183 0.20503 0.25563 0.00820  -0.01420 0.00110  184 GLN A CD  
1633 O  OE1 A GLN A 181 ? 0.35753 0.23613 0.27793 -0.00670 0.00410  0.01080  184 GLN A OE1 
1635 N  NE2 A GLN A 181 ? 0.29653 0.22013 0.26283 0.03550  -0.01220 0.00050  184 GLN A NE2 
1637 N  N   . ASN A 182 ? 0.13383 0.09443 0.12683 -0.01090 -0.00540 -0.01170 185 ASN A N   
1638 C  CA  . ASN A 182 ? 0.14813 0.10283 0.13073 -0.01970 0.00290  -0.00720 185 ASN A CA  
1639 C  C   . ASN A 182 ? 0.15403 0.11203 0.13063 -0.01950 0.01090  -0.01610 185 ASN A C   
1640 O  O   . ASN A 182 ? 0.17093 0.12733 0.14313 -0.01980 0.00140  -0.03580 185 ASN A O   
1641 C  CB  . ASN A 182 ? 0.18163 0.09183 0.14053 -0.00080 -0.00810 -0.00690 185 ASN A CB  
1642 C  CG  . ASN A 182 ? 0.19383 0.09463 0.14723 -0.02200 -0.02440 -0.00450 185 ASN A CG  
1643 O  OD1 . ASN A 182 ? 0.31133 0.12503 0.15143 -0.07000 -0.06760 0.02550  185 ASN A OD1 
1644 N  ND2 . ASN A 182 ? 0.14193 0.09313 0.15213 0.00130  0.01390  0.00330  185 ASN A ND2 
1645 N  N   . THR A 183 ? 0.15763 0.11183 0.12973 -0.02190 -0.01300 -0.01690 186 THR A N   
1646 C  CA  A THR A 183 ? 0.16353 0.11203 0.12783 -0.02280 -0.01930 -0.00810 186 THR A CA  
1648 C  C   . THR A 183 ? 0.15123 0.11633 0.12063 -0.00720 -0.00940 -0.00740 186 THR A C   
1649 O  O   . THR A 183 ? 0.17233 0.12623 0.12363 -0.02240 -0.00870 -0.00640 186 THR A O   
1650 C  CB  A THR A 183 ? 0.16133 0.10143 0.13583 -0.01760 -0.02460 -0.00160 186 THR A CB  
1652 O  OG1 A THR A 183 ? 0.16523 0.10073 0.14623 -0.00020 -0.01790 -0.01130 186 THR A OG1 
1654 C  CG2 A THR A 183 ? 0.18203 0.13103 0.14423 -0.01110 -0.04990 -0.00280 186 THR A CG2 
1656 N  N   . PRO A 184 ? 0.15153 0.12173 0.12223 -0.00960 0.00120  -0.01570 187 PRO A N   
1657 C  CA  . PRO A 184 ? 0.13673 0.11993 0.13953 0.00970  -0.00640 -0.01860 187 PRO A CA  
1658 C  C   . PRO A 184 ? 0.14013 0.12803 0.12843 0.00260  -0.03200 -0.02480 187 PRO A C   
1659 O  O   . PRO A 184 ? 0.15933 0.14063 0.14583 0.00030  -0.04040 -0.02930 187 PRO A O   
1660 C  CB  . PRO A 184 ? 0.17443 0.12793 0.15453 0.01110  0.02370  -0.01660 187 PRO A CB  
1661 C  CG  . PRO A 184 ? 0.20143 0.12273 0.14023 0.00800  0.00910  -0.01320 187 PRO A CG  
1662 C  CD  . PRO A 184 ? 0.17993 0.14093 0.12473 0.00040  0.00940  -0.00960 187 PRO A CD  
1663 N  N   . ILE A 185 ? 0.13693 0.12723 0.14793 -0.02780 0.00010  -0.02080 188 ILE A N   
1664 C  CA  . ILE A 185 ? 0.14583 0.12893 0.15983 -0.00740 0.00390  -0.03100 188 ILE A CA  
1665 C  C   . ILE A 185 ? 0.12983 0.11393 0.17113 0.00870  -0.02770 -0.02540 188 ILE A C   
1666 O  O   . ILE A 185 ? 0.14513 0.10683 0.15703 -0.00330 -0.00960 -0.00880 188 ILE A O   
1667 C  CB  . ILE A 185 ? 0.14893 0.13713 0.16473 -0.01190 0.00790  -0.04110 188 ILE A CB  
1668 C  CG1 . ILE A 185 ? 0.14673 0.14813 0.18953 -0.00180 0.01500  -0.03770 188 ILE A CG1 
1669 C  CG2 . ILE A 185 ? 0.16243 0.16493 0.19733 -0.04140 0.00340  -0.01930 188 ILE A CG2 
1670 C  CD1 . ILE A 185 ? 0.14583 0.14853 0.19613 -0.02140 0.02120  -0.04090 188 ILE A CD1 
1671 N  N   . GLY A 186 ? 0.13113 0.13603 0.18993 0.00890  -0.02570 -0.03970 189 GLY A N   
1672 C  CA  . GLY A 186 ? 0.14853 0.15313 0.18543 -0.00330 -0.02540 -0.05400 189 GLY A CA  
1673 C  C   . GLY A 186 ? 0.14543 0.15073 0.17433 0.01010  -0.03510 -0.03780 189 GLY A C   
1674 O  O   . GLY A 186 ? 0.15623 0.13593 0.18413 -0.00140 -0.01280 -0.02550 189 GLY A O   
1675 N  N   . ASP A 187 ? 0.15733 0.15343 0.15533 0.03400  -0.03210 -0.04150 190 ASP A N   
1676 C  CA  . ASP A 187 ? 0.15513 0.16953 0.14963 0.02420  -0.03280 -0.02610 190 ASP A CA  
1677 C  C   . ASP A 187 ? 0.15333 0.16543 0.15313 0.01820  -0.02020 -0.01380 190 ASP A C   
1678 O  O   . ASP A 187 ? 0.15763 0.15393 0.16213 -0.00150 -0.00910 -0.01660 190 ASP A O   
1679 C  CB  . ASP A 187 ? 0.16703 0.18893 0.15693 0.01630  -0.05010 -0.02080 190 ASP A CB  
1680 C  CG  . ASP A 187 ? 0.18953 0.20083 0.18453 0.01080  -0.03880 0.00360  190 ASP A CG  
1681 O  OD1 . ASP A 187 ? 0.19963 0.18113 0.18373 0.01510  -0.02130 0.02290  190 ASP A OD1 
1682 O  OD2 . ASP A 187 ? 0.18933 0.22553 0.20323 0.03990  -0.05040 -0.00910 190 ASP A OD2 
1683 N  N   . GLY A 188 ? 0.13113 0.15993 0.15863 0.02220  -0.01550 -0.01190 191 GLY A N   
1684 C  CA  . GLY A 188 ? 0.12233 0.14123 0.16993 0.00710  -0.00810 -0.02900 191 GLY A CA  
1685 C  C   . GLY A 188 ? 0.13543 0.13223 0.15553 0.00870  -0.01160 -0.01900 191 GLY A C   
1686 O  O   . GLY A 188 ? 0.14573 0.13763 0.15773 0.01150  -0.01910 -0.02080 191 GLY A O   
1687 N  N   . PRO A 189 ? 0.13583 0.13053 0.14683 0.01520  0.00130  -0.01520 192 PRO A N   
1688 C  CA  . PRO A 189 ? 0.14013 0.13413 0.13943 0.02610  -0.00680 -0.02670 192 PRO A CA  
1689 C  C   . PRO A 189 ? 0.14943 0.13023 0.14443 0.01510  -0.00020 -0.02800 192 PRO A C   
1690 O  O   . PRO A 189 ? 0.15903 0.15593 0.13473 -0.00350 0.01200  -0.02820 192 PRO A O   
1691 C  CB  . PRO A 189 ? 0.15933 0.15253 0.14583 0.00820  -0.00340 -0.02140 192 PRO A CB  
1692 C  CG  . PRO A 189 ? 0.16083 0.14763 0.15413 0.01410  -0.00230 -0.01330 192 PRO A CG  
1693 C  CD  . PRO A 189 ? 0.15293 0.13573 0.16123 0.01870  0.00270  -0.00960 192 PRO A CD  
1694 N  N   . VAL A 190 ? 0.13953 0.11203 0.15293 0.02270  -0.01650 -0.01630 193 VAL A N   
1695 C  CA  . VAL A 190 ? 0.15783 0.10563 0.15453 0.01990  -0.00840 -0.03990 193 VAL A CA  
1696 C  C   . VAL A 190 ? 0.15793 0.10373 0.13323 0.00600  0.01380  -0.01790 193 VAL A C   
1697 O  O   . VAL A 190 ? 0.18243 0.14703 0.12993 -0.00710 -0.00440 -0.02410 193 VAL A O   
1698 C  CB  . VAL A 190 ? 0.17423 0.13233 0.18603 0.01990  0.01020  -0.02160 193 VAL A CB  
1699 C  CG1 . VAL A 190 ? 0.19963 0.16163 0.23193 0.01430  0.02980  -0.02440 193 VAL A CG1 
1700 C  CG2 . VAL A 190 ? 0.21153 0.13533 0.19333 0.01550  -0.03550 0.00870  193 VAL A CG2 
1701 N  N   . LEU A 191 ? 0.14843 0.13013 0.15063 0.01090  -0.00070 -0.01610 194 LEU A N   
1702 C  CA  . LEU A 191 ? 0.14813 0.14243 0.14133 0.01880  0.00160  -0.00760 194 LEU A CA  
1703 C  C   . LEU A 191 ? 0.19213 0.13663 0.14473 0.00630  0.03400  -0.00360 194 LEU A C   
1704 O  O   . LEU A 191 ? 0.27963 0.16013 0.15553 -0.00430 0.03120  -0.00350 194 LEU A O   
1705 C  CB  . LEU A 191 ? 0.17013 0.14583 0.12803 0.00020  -0.01160 -0.01240 194 LEU A CB  
1706 C  CG  . LEU A 191 ? 0.15913 0.14143 0.12493 0.02080  -0.01120 -0.01940 194 LEU A CG  
1707 C  CD1 . LEU A 191 ? 0.15603 0.16033 0.15563 0.02090  -0.03230 0.00460  194 LEU A CD1 
1708 C  CD2 . LEU A 191 ? 0.18823 0.16823 0.14773 0.02690  -0.00000 -0.01970 194 LEU A CD2 
1709 N  N   . LEU A 192 ? 0.21623 0.14833 0.16773 -0.00700 0.03430  -0.00320 195 LEU A N   
1710 C  CA  . LEU A 192 ? 0.20183 0.16493 0.19423 0.00100  0.00230  0.00160  195 LEU A CA  
1711 C  C   . LEU A 192 ? 0.16643 0.16743 0.21513 0.02500  0.00200  -0.02830 195 LEU A C   
1712 O  O   . LEU A 192 ? 0.18143 0.21673 0.25993 0.01700  0.03040  -0.06470 195 LEU A O   
1713 C  CB  . LEU A 192 ? 0.21613 0.20553 0.19863 -0.01010 -0.00610 0.03070  195 LEU A CB  
1714 C  CG  . LEU A 192 ? 0.21953 0.22003 0.21613 -0.02200 -0.00830 0.02670  195 LEU A CG  
1715 C  CD1 . LEU A 192 ? 0.26363 0.25783 0.24193 -0.00190 0.00600  0.04090  195 LEU A CD1 
1716 C  CD2 . LEU A 192 ? 0.20143 0.21563 0.22823 0.01100  -0.00480 -0.00840 195 LEU A CD2 
1717 N  N   . PRO A 193 ? 0.16193 0.15743 0.18183 0.01400  0.02000  -0.00610 196 PRO A N   
1718 C  CA  . PRO A 193 ? 0.17103 0.19543 0.17913 -0.00200 0.01190  0.01310  196 PRO A CA  
1719 C  C   . PRO A 193 ? 0.16043 0.18333 0.16793 0.01150  0.00380  0.00370  196 PRO A C   
1720 O  O   . PRO A 193 ? 0.18093 0.20593 0.20193 0.01300  0.03300  0.02500  196 PRO A O   
1721 C  CB  . PRO A 193 ? 0.19323 0.19143 0.17443 0.00440  0.02910  0.00550  196 PRO A CB  
1722 C  CG  . PRO A 193 ? 0.19363 0.17013 0.17403 -0.01110 0.03140  -0.01700 196 PRO A CG  
1723 C  CD  . PRO A 193 ? 0.18773 0.16103 0.16583 -0.00820 0.03370  -0.01480 196 PRO A CD  
1724 N  N   . ASP A 194 ? 0.18443 0.19223 0.18403 0.00310  0.00800  -0.00880 197 ASP A N   
1725 C  CA  A ASP A 194 ? 0.16803 0.18703 0.18843 0.00010  0.02220  -0.01570 197 ASP A CA  
1727 C  C   . ASP A 194 ? 0.16993 0.19123 0.17503 -0.01100 0.03160  -0.00060 197 ASP A C   
1728 O  O   . ASP A 194 ? 0.18963 0.20773 0.15783 -0.00580 0.02540  0.00720  197 ASP A O   
1729 C  CB  A ASP A 194 ? 0.17413 0.18163 0.20473 0.01980  0.01110  -0.01460 197 ASP A CB  
1731 C  CG  A ASP A 194 ? 0.19413 0.18743 0.20363 0.04330  0.03670  -0.02660 197 ASP A CG  
1733 O  OD1 A ASP A 194 ? 0.22693 0.21643 0.21303 0.02510  0.05900  -0.06670 197 ASP A OD1 
1735 O  OD2 A ASP A 194 ? 0.23033 0.19673 0.20983 0.04840  0.03490  -0.01200 197 ASP A OD2 
1737 N  N   . ASN A 195 ? 0.15543 0.18623 0.17473 -0.00200 0.02690  -0.01270 198 ASN A N   
1738 C  CA  . ASN A 195 ? 0.16583 0.19563 0.17223 -0.00260 0.01830  -0.00240 198 ASN A CA  
1739 C  C   . ASN A 195 ? 0.15363 0.21283 0.16793 0.01300  0.02400  -0.01330 198 ASN A C   
1740 O  O   . ASN A 195 ? 0.17023 0.24983 0.19283 0.02150  0.00950  -0.02510 198 ASN A O   
1741 C  CB  . ASN A 195 ? 0.19873 0.21053 0.19893 -0.02520 0.00190  0.02970  198 ASN A CB  
1742 C  CG  . ASN A 195 ? 0.22733 0.21833 0.21703 -0.03220 0.00410  0.04210  198 ASN A CG  
1743 O  OD1 . ASN A 195 ? 0.22383 0.21463 0.19763 -0.02090 -0.00100 0.01460  198 ASN A OD1 
1744 N  ND2 . ASN A 195 ? 0.26283 0.23563 0.26113 -0.03830 0.00470  0.04300  198 ASN A ND2 
1745 N  N   . HIS A 196 ? 0.15313 0.19073 0.16793 0.00680  0.00660  -0.00830 199 HIS A N   
1746 C  CA  . HIS A 196 ? 0.15063 0.16233 0.15073 0.01620  -0.00200 -0.01050 199 HIS A CA  
1747 C  C   . HIS A 196 ? 0.16153 0.15363 0.15083 0.01470  0.00380  -0.00270 199 HIS A C   
1748 O  O   . HIS A 196 ? 0.17343 0.16223 0.15763 0.03150  0.01520  0.00440  199 HIS A O   
1749 C  CB  . HIS A 196 ? 0.14703 0.16343 0.17413 -0.00420 0.00960  -0.01320 199 HIS A CB  
1750 C  CG  . HIS A 196 ? 0.14103 0.15703 0.16823 -0.00160 -0.00310 0.00770  199 HIS A CG  
1751 N  ND1 . HIS A 196 ? 0.12053 0.16783 0.17243 0.00310  -0.00280 -0.00120 199 HIS A ND1 
1752 C  CD2 . HIS A 196 ? 0.13613 0.14263 0.15743 0.01840  0.00610  -0.00400 199 HIS A CD2 
1753 C  CE1 . HIS A 196 ? 0.13633 0.18053 0.14943 0.01650  0.01430  0.01190  199 HIS A CE1 
1754 N  NE2 . HIS A 196 ? 0.13913 0.15563 0.15093 0.02110  0.00040  0.00360  199 HIS A NE2 
1755 N  N   . TYR A 197 ? 0.17133 0.16103 0.14343 -0.00160 0.00380  -0.01030 200 TYR A N   
1756 C  CA  . TYR A 197 ? 0.15303 0.16173 0.14853 0.00180  -0.00140 -0.00990 200 TYR A CA  
1757 C  C   . TYR A 197 ? 0.13763 0.14103 0.15063 0.01660  -0.01260 -0.01170 200 TYR A C   
1758 O  O   . TYR A 197 ? 0.15393 0.14983 0.17283 0.02100  0.00600  -0.00990 200 TYR A O   
1759 C  CB  . TYR A 197 ? 0.14873 0.19193 0.18283 -0.00970 0.00220  -0.01440 200 TYR A CB  
1760 C  CG  . TYR A 197 ? 0.15903 0.20213 0.19343 -0.00550 0.01060  -0.00940 200 TYR A CG  
1761 C  CD1 . TYR A 197 ? 0.15503 0.23803 0.22953 -0.01290 -0.00470 -0.01720 200 TYR A CD1 
1762 C  CD2 . TYR A 197 ? 0.16263 0.21173 0.20743 -0.01830 -0.01490 0.00100  200 TYR A CD2 
1763 C  CE1 . TYR A 197 ? 0.15903 0.26613 0.26113 0.00020  -0.00980 -0.01790 200 TYR A CE1 
1764 C  CE2 . TYR A 197 ? 0.15103 0.25173 0.23373 -0.01770 -0.00300 -0.00170 200 TYR A CE2 
1765 C  CZ  . TYR A 197 ? 0.16143 0.27633 0.26693 0.00410  -0.01190 -0.02590 200 TYR A CZ  
1766 O  OH  . TYR A 197 ? 0.18043 0.32983 0.30623 0.00500  -0.01330 -0.02650 200 TYR A OH  
1767 N  N   . LEU A 198 ? 0.15463 0.14063 0.12993 0.00360  -0.01880 -0.02760 201 LEU A N   
1768 C  CA  . LEU A 198 ? 0.17353 0.13693 0.14143 0.00520  -0.00330 -0.01460 201 LEU A CA  
1769 C  C   . LEU A 198 ? 0.16033 0.12283 0.14703 0.00850  -0.00240 -0.00990 201 LEU A C   
1770 O  O   . LEU A 198 ? 0.18713 0.11703 0.16753 0.01000  0.00350  -0.01760 201 LEU A O   
1771 C  CB  . LEU A 198 ? 0.15673 0.13043 0.14573 0.02190  -0.00960 -0.00090 201 LEU A CB  
1772 C  CG  . LEU A 198 ? 0.15993 0.12923 0.15833 0.02100  -0.00930 -0.00930 201 LEU A CG  
1773 C  CD1 . LEU A 198 ? 0.15243 0.12773 0.18023 0.01550  -0.01150 0.00190  201 LEU A CD1 
1774 C  CD2 . LEU A 198 ? 0.16673 0.13933 0.15963 0.02970  -0.00540 -0.02160 201 LEU A CD2 
1775 N  N   . SER A 199 ? 0.15453 0.15093 0.14863 0.02130  -0.01030 -0.01060 202 SER A N   
1776 C  CA  . SER A 199 ? 0.14733 0.16463 0.15703 -0.00420 -0.01040 0.00100  202 SER A CA  
1777 C  C   . SER A 199 ? 0.15383 0.14793 0.13993 -0.02150 -0.00890 -0.01430 202 SER A C   
1778 O  O   . SER A 199 ? 0.17333 0.13803 0.14803 -0.01220 0.01740  -0.01300 202 SER A O   
1779 C  CB  . SER A 199 ? 0.14993 0.21673 0.17573 -0.00660 -0.03380 0.00050  202 SER A CB  
1780 O  OG  . SER A 199 ? 0.15163 0.25823 0.20053 0.00300  -0.03800 0.00980  202 SER A OG  
1781 N  N   . VAL A 200 ? 0.13843 0.13353 0.12963 -0.01280 0.01070  -0.00360 203 VAL A N   
1782 C  CA  . VAL A 200 ? 0.15233 0.13893 0.12583 -0.00490 -0.00330 -0.01700 203 VAL A CA  
1783 C  C   . VAL A 200 ? 0.15943 0.14483 0.13853 -0.01540 -0.00210 -0.01220 203 VAL A C   
1784 O  O   . VAL A 200 ? 0.20953 0.16183 0.17193 -0.04410 -0.01910 -0.00650 203 VAL A O   
1785 C  CB  . VAL A 200 ? 0.15153 0.14643 0.13793 0.01810  0.00840  -0.00650 203 VAL A CB  
1786 C  CG1 . VAL A 200 ? 0.15583 0.15013 0.15223 -0.02280 0.01580  0.00730  203 VAL A CG1 
1787 C  CG2 . VAL A 200 ? 0.15673 0.16703 0.12783 0.02040  0.00960  -0.00560 203 VAL A CG2 
1788 N  N   . GLN A 201 ? 0.15913 0.13953 0.12763 -0.01260 -0.00830 -0.00760 204 GLN A N   
1789 C  CA  A GLN A 201 ? 0.15783 0.16953 0.13523 -0.03120 -0.01750 -0.01990 204 GLN A CA  
1791 C  C   . GLN A 201 ? 0.16823 0.14833 0.13823 -0.03560 -0.01070 -0.02300 204 GLN A C   
1792 O  O   . GLN A 201 ? 0.17763 0.15023 0.15403 -0.01590 0.00110  -0.02510 204 GLN A O   
1793 C  CB  A GLN A 201 ? 0.15823 0.20293 0.15193 -0.02630 -0.02730 -0.01630 204 GLN A CB  
1795 C  CG  A GLN A 201 ? 0.14863 0.21143 0.15353 -0.01030 -0.02390 0.02150  204 GLN A CG  
1797 C  CD  A GLN A 201 ? 0.16923 0.20963 0.16953 0.01860  -0.02110 0.02690  204 GLN A CD  
1799 O  OE1 A GLN A 201 ? 0.19773 0.22093 0.18493 0.03450  -0.03150 0.01600  204 GLN A OE1 
1801 N  NE2 A GLN A 201 ? 0.18353 0.21183 0.16373 0.02730  -0.00910 0.02840  204 GLN A NE2 
1803 N  N   . SER A 202 ? 0.16793 0.14043 0.13403 -0.02760 -0.01230 0.00590  205 SER A N   
1804 C  CA  . SER A 202 ? 0.18833 0.13813 0.12763 -0.02820 0.00210  0.00150  205 SER A CA  
1805 C  C   . SER A 202 ? 0.18653 0.14843 0.13633 -0.02630 0.00490  -0.00640 205 SER A C   
1806 O  O   . SER A 202 ? 0.23403 0.16023 0.15503 -0.03570 0.00360  -0.00850 205 SER A O   
1807 C  CB  . SER A 202 ? 0.18893 0.12993 0.12523 -0.00820 -0.00280 -0.00190 205 SER A CB  
1808 O  OG  . SER A 202 ? 0.16653 0.13563 0.14453 0.00360  -0.00850 -0.00220 205 SER A OG  
1809 N  N   . ALA A 203 ? 0.13983 0.16943 0.13883 0.00840  0.01350  -0.00710 206 ALA A N   
1810 C  CA  . ALA A 203 ? 0.12593 0.18963 0.13053 0.00970  -0.00730 -0.00290 206 ALA A CA  
1811 C  C   . ALA A 203 ? 0.13953 0.15953 0.12193 -0.00730 -0.01050 0.00900  206 ALA A C   
1812 O  O   . ALA A 203 ? 0.14933 0.14163 0.14483 -0.01040 -0.00110 -0.01270 206 ALA A O   
1813 C  CB  . ALA A 203 ? 0.14023 0.23883 0.16053 0.03080  -0.01240 0.00760  206 ALA A CB  
1814 N  N   . LEU A 204 ? 0.14733 0.15053 0.12163 0.00700  0.00210  -0.01100 207 LEU A N   
1815 C  CA  . LEU A 204 ? 0.14393 0.13743 0.10753 0.00540  0.00290  0.00330  207 LEU A CA  
1816 C  C   . LEU A 204 ? 0.15563 0.14303 0.11203 -0.00450 -0.01280 -0.01510 207 LEU A C   
1817 O  O   . LEU A 204 ? 0.16013 0.18443 0.12153 -0.01780 -0.01510 -0.00070 207 LEU A O   
1818 C  CB  . LEU A 204 ? 0.15803 0.12933 0.12223 -0.00250 -0.01520 -0.01890 207 LEU A CB  
1819 C  CG  . LEU A 204 ? 0.15923 0.14503 0.13353 0.01140  -0.01060 0.00050  207 LEU A CG  
1820 C  CD1 . LEU A 204 ? 0.17103 0.12623 0.14223 0.00660  -0.00280 -0.01150 207 LEU A CD1 
1821 C  CD2 . LEU A 204 ? 0.15693 0.14243 0.13373 0.02080  -0.01280 -0.00090 207 LEU A CD2 
1822 N  N   . SER A 205 ? 0.15963 0.15183 0.11963 -0.00550 -0.00750 0.00670  208 SER A N   
1823 C  CA  . SER A 205 ? 0.17313 0.16373 0.12643 -0.00130 -0.02100 0.00900  208 SER A CA  
1824 C  C   . SER A 205 ? 0.17013 0.16033 0.11483 0.00380  -0.01890 0.00390  208 SER A C   
1825 O  O   . SER A 205 ? 0.15543 0.14723 0.11793 -0.01040 0.00110  0.00430  208 SER A O   
1826 C  CB  . SER A 205 ? 0.17633 0.16213 0.14383 -0.00180 -0.02540 0.00630  208 SER A CB  
1827 O  OG  . SER A 205 ? 0.18513 0.15423 0.14723 0.01160  -0.02570 0.02910  208 SER A OG  
1828 N  N   . LYS A 206 ? 0.19523 0.19693 0.13093 0.02830  -0.01280 0.01120  209 LYS A N   
1829 C  CA  . LYS A 206 ? 0.23133 0.19553 0.14503 0.01790  -0.00010 0.02560  209 LYS A CA  
1830 C  C   . LYS A 206 ? 0.22203 0.19213 0.14183 0.02680  -0.01470 0.03410  209 LYS A C   
1831 O  O   . LYS A 206 ? 0.23733 0.21773 0.16413 0.03260  -0.00720 0.04070  209 LYS A O   
1832 C  CB  . LYS A 206 ? 0.22713 0.19853 0.14603 0.01040  -0.02350 0.00210  209 LYS A CB  
1833 C  CG  . LYS A 206 ? 0.19973 0.17323 0.13833 0.00490  -0.01420 0.00370  209 LYS A CG  
1834 C  CD  . LYS A 206 ? 0.17503 0.14643 0.13413 -0.00910 -0.02050 0.00540  209 LYS A CD  
1835 C  CE  . LYS A 206 ? 0.17423 0.14723 0.13973 -0.03040 -0.01190 -0.00570 209 LYS A CE  
1836 N  NZ  . LYS A 206 ? 0.17183 0.12703 0.13383 -0.01590 -0.00660 -0.01100 209 LYS A NZ  
1837 N  N   . ASP A 207 ? 0.23013 0.21843 0.12473 0.00690  0.01230  0.04210  210 ASP A N   
1838 C  CA  . ASP A 207 ? 0.27113 0.22333 0.13933 -0.00360 0.02600  0.05630  210 ASP A CA  
1839 C  C   . ASP A 207 ? 0.27403 0.24353 0.15073 -0.00260 0.02260  0.07700  210 ASP A C   
1840 O  O   . ASP A 207 ? 0.26673 0.24893 0.15483 -0.01580 0.03430  0.05710  210 ASP A O   
1841 C  CB  . ASP A 207 ? 0.30363 0.21773 0.16393 -0.03180 0.02710  0.05410  210 ASP A CB  
1842 C  CG  . ASP A 207 ? 0.33753 0.22043 0.16713 -0.05500 0.00270  0.05370  210 ASP A CG  
1843 O  OD1 . ASP A 207 ? 0.37283 0.23193 0.16573 -0.03420 0.02070  0.05890  210 ASP A OD1 
1844 O  OD2 . ASP A 207 ? 0.37523 0.21843 0.19263 -0.06310 -0.00680 0.05660  210 ASP A OD2 
1845 N  N   . PRO A 208 ? 0.31763 0.30293 0.16263 -0.01070 0.01230  0.07310  211 PRO A N   
1846 C  CA  . PRO A 208 ? 0.32913 0.33013 0.18023 -0.02210 0.00050  0.05850  211 PRO A CA  
1847 C  C   . PRO A 208 ? 0.33913 0.33553 0.19033 -0.05040 0.01470  0.05640  211 PRO A C   
1848 O  O   . PRO A 208 ? 0.36663 0.36973 0.18433 -0.06490 0.01350  0.01700  211 PRO A O   
1849 C  CB  . PRO A 208 ? 0.35053 0.34093 0.20013 -0.00280 0.00570  0.07550  211 PRO A CB  
1850 C  CG  . PRO A 208 ? 0.34903 0.34313 0.18043 -0.00400 0.00130  0.08330  211 PRO A CG  
1851 C  CD  . PRO A 208 ? 0.33063 0.32873 0.17633 -0.00080 0.00520  0.08090  211 PRO A CD  
1852 N  N   . ASN A 209 ? 0.33533 0.32083 0.19443 -0.05910 0.00280  0.08650  212 ASN A N   
1853 C  CA  . ASN A 209 ? 0.34453 0.33863 0.24343 -0.06930 0.02840  0.06710  212 ASN A CA  
1854 C  C   . ASN A 209 ? 0.33393 0.31973 0.21953 -0.07750 0.05310  0.06250  212 ASN A C   
1855 O  O   . ASN A 209 ? 0.33373 0.36003 0.24913 -0.09190 0.03850  0.08300  212 ASN A O   
1856 C  CB  . ASN A 209 ? 0.37763 0.37083 0.32033 -0.07590 0.02380  0.07170  212 ASN A CB  
1857 C  CG  . ASN A 209 ? 0.42733 0.42293 0.40933 -0.08780 0.02830  0.07500  212 ASN A CG  
1860 N  N   . GLU A 210 ? 0.33343 0.25063 0.17023 -0.05640 0.06960  0.03010  213 GLU A N   
1861 C  CA  . GLU A 210 ? 0.33253 0.21313 0.16623 -0.04550 0.07560  0.01280  213 GLU A CA  
1862 C  C   . GLU A 210 ? 0.33363 0.20753 0.16583 -0.05750 0.08810  -0.00930 213 GLU A C   
1863 O  O   . GLU A 210 ? 0.34683 0.23483 0.17623 -0.07910 0.09300  -0.02340 213 GLU A O   
1864 C  CB  . GLU A 210 ? 0.31553 0.20573 0.15773 -0.03390 0.08090  0.01240  213 GLU A CB  
1865 C  CG  . GLU A 210 ? 0.30193 0.17603 0.16133 -0.04150 0.08240  0.00390  213 GLU A CG  
1866 C  CD  . GLU A 210 ? 0.30693 0.13973 0.16773 -0.04100 0.08560  -0.01220 213 GLU A CD  
1867 O  OE1 . GLU A 210 ? 0.31033 0.14693 0.16623 -0.03670 0.08850  -0.01220 213 GLU A OE1 
1868 O  OE2 . GLU A 210 ? 0.32183 0.12673 0.18193 -0.04610 0.08600  -0.00690 213 GLU A OE2 
1869 N  N   . LYS A 211 ? 0.35323 0.21673 0.17073 -0.04290 0.08650  -0.01580 214 LYS A N   
1870 C  CA  . LYS A 211 ? 0.34013 0.22043 0.18283 -0.02710 0.11030  0.00050  214 LYS A CA  
1871 C  C   . LYS A 211 ? 0.33853 0.17023 0.17013 -0.03840 0.09550  -0.01830 214 LYS A C   
1872 O  O   . LYS A 211 ? 0.37113 0.16403 0.17343 -0.03280 0.06600  -0.02750 214 LYS A O   
1873 C  CB  . LYS A 211 ? 0.36523 0.26983 0.21363 -0.02770 0.10180  0.00630  214 LYS A CB  
1874 C  CG  . LYS A 211 ? 0.37793 0.30893 0.26943 -0.03630 0.09070  0.01450  214 LYS A CG  
1875 C  CD  . LYS A 211 ? 0.37893 0.34543 0.33103 -0.03890 0.08280  0.00140  214 LYS A CD  
1878 N  N   . ARG A 212 ? 0.29843 0.16203 0.16983 -0.05070 0.10770  -0.01110 215 ARG A N   
1879 C  CA  . ARG A 212 ? 0.25773 0.14273 0.17143 -0.04310 0.09900  -0.01590 215 ARG A CA  
1880 C  C   . ARG A 212 ? 0.23723 0.13143 0.16373 -0.02350 0.06470  -0.01090 215 ARG A C   
1881 O  O   . ARG A 212 ? 0.22073 0.12893 0.17463 -0.01370 0.06550  0.00080  215 ARG A O   
1882 C  CB  . ARG A 212 ? 0.25333 0.13103 0.18983 -0.06570 0.09520  -0.04090 215 ARG A CB  
1883 C  CG  . ARG A 212 ? 0.27263 0.15753 0.20673 -0.08260 0.08410  -0.04310 215 ARG A CG  
1884 C  CD  . ARG A 212 ? 0.26703 0.15783 0.22233 -0.07320 0.09220  -0.04180 215 ARG A CD  
1885 N  NE  . ARG A 212 ? 0.28293 0.15133 0.19983 -0.04470 0.09060  -0.02330 215 ARG A NE  
1886 C  CZ  . ARG A 212 ? 0.30003 0.15703 0.18633 -0.06100 0.06850  -0.01060 215 ARG A CZ  
1887 N  NH1 . ARG A 212 ? 0.28563 0.16513 0.21663 -0.07300 0.07890  -0.01160 215 ARG A NH1 
1888 N  NH2 . ARG A 212 ? 0.32433 0.16853 0.16863 -0.04960 0.04400  -0.01640 215 ARG A NH2 
1889 N  N   . ASP A 213 ? 0.22813 0.11793 0.13873 -0.01340 0.04950  -0.01390 216 ASP A N   
1890 C  CA  . ASP A 213 ? 0.19303 0.11373 0.14153 -0.00630 0.05670  -0.00900 216 ASP A CA  
1891 C  C   . ASP A 213 ? 0.16723 0.10793 0.13853 -0.00620 0.02290  -0.01120 216 ASP A C   
1892 O  O   . ASP A 213 ? 0.16893 0.12793 0.13483 -0.01270 0.03070  -0.00710 216 ASP A O   
1893 C  CB  . ASP A 213 ? 0.15933 0.11073 0.14083 0.00630  0.04090  0.00170  216 ASP A CB  
1894 C  CG  . ASP A 213 ? 0.15723 0.13193 0.13353 -0.01170 0.01620  -0.00620 216 ASP A CG  
1895 O  OD1 . ASP A 213 ? 0.16623 0.12793 0.14083 -0.00090 0.01020  -0.01250 216 ASP A OD1 
1896 O  OD2 . ASP A 213 ? 0.18143 0.15773 0.15193 -0.02740 0.02760  0.00920  216 ASP A OD2 
1897 N  N   . HIS A 214 ? 0.16073 0.12363 0.12863 -0.00860 0.03630  -0.00650 217 HIS A N   
1898 C  CA  . HIS A 214 ? 0.15093 0.11013 0.12523 -0.01020 0.03210  -0.00090 217 HIS A CA  
1899 C  C   . HIS A 214 ? 0.15703 0.10963 0.10993 -0.01070 0.02440  0.00320  217 HIS A C   
1900 O  O   . HIS A 214 ? 0.15273 0.12933 0.11813 -0.00760 0.00760  0.00000  217 HIS A O   
1901 C  CB  . HIS A 214 ? 0.18363 0.11303 0.12693 -0.01330 0.02400  0.01590  217 HIS A CB  
1902 C  CG  . HIS A 214 ? 0.19913 0.13123 0.11563 -0.01370 0.01760  0.01310  217 HIS A CG  
1903 N  ND1 . HIS A 214 ? 0.22443 0.15023 0.11093 -0.01620 0.01260  0.00920  217 HIS A ND1 
1904 C  CD2 . HIS A 214 ? 0.19943 0.15203 0.11423 0.00540  0.00710  0.01730  217 HIS A CD2 
1905 C  CE1 . HIS A 214 ? 0.22013 0.16953 0.11923 -0.01350 0.02600  0.00720  217 HIS A CE1 
1906 N  NE2 . HIS A 214 ? 0.19983 0.16183 0.11963 0.00610  0.00630  0.01000  217 HIS A NE2 
1907 N  N   . MET A 215 ? 0.13203 0.11543 0.10623 -0.00020 0.01800  0.00040  218 MET A N   
1908 C  CA  . MET A 215 ? 0.13843 0.12643 0.11593 -0.00420 0.01640  -0.01000 218 MET A CA  
1909 C  C   . MET A 215 ? 0.14793 0.11683 0.12273 0.01250  0.00390  -0.01520 218 MET A C   
1910 O  O   . MET A 215 ? 0.14613 0.10593 0.11883 -0.00120 0.00480  -0.00140 218 MET A O   
1911 C  CB  . MET A 215 ? 0.13493 0.11973 0.12023 -0.01740 0.01720  0.01540  218 MET A CB  
1912 C  CG  . MET A 215 ? 0.14793 0.11583 0.12353 -0.00470 0.02000  0.02300  218 MET A CG  
1913 S  SD  . MET A 215 ? 0.12413 0.12183 0.12643 -0.00490 -0.00020 0.00880  218 MET A SD  
1914 C  CE  . MET A 215 ? 0.12133 0.14153 0.12343 -0.01550 -0.01170 0.00830  218 MET A CE  
1915 N  N   . VAL A 216 ? 0.15033 0.11613 0.11953 0.00590  0.00420  0.00620  219 VAL A N   
1916 C  CA  . VAL A 216 ? 0.14393 0.12373 0.11583 0.00750  0.00190  0.01320  219 VAL A CA  
1917 C  C   . VAL A 216 ? 0.14893 0.12183 0.11363 -0.00180 -0.00360 -0.00110 219 VAL A C   
1918 O  O   . VAL A 216 ? 0.15843 0.12743 0.11303 -0.00500 0.00090  -0.00300 219 VAL A O   
1919 C  CB  . VAL A 216 ? 0.17553 0.13383 0.12783 0.00890  0.01260  0.01050  219 VAL A CB  
1920 C  CG1 . VAL A 216 ? 0.18303 0.13363 0.14553 0.03170  0.01860  0.01980  219 VAL A CG1 
1921 C  CG2 . VAL A 216 ? 0.17763 0.14733 0.14173 0.00290  0.02610  0.02580  219 VAL A CG2 
1922 N  N   . LEU A 217 ? 0.14373 0.13213 0.10543 0.00630  0.00380  0.00360  220 LEU A N   
1923 C  CA  . LEU A 217 ? 0.13883 0.14623 0.11513 0.01530  0.00910  0.00710  220 LEU A CA  
1924 C  C   . LEU A 217 ? 0.14183 0.13173 0.12463 -0.00500 0.01210  0.00030  220 LEU A C   
1925 O  O   . LEU A 217 ? 0.15163 0.15683 0.15643 -0.00790 0.01570  -0.01560 220 LEU A O   
1926 C  CB  . LEU A 217 ? 0.16053 0.15563 0.12233 -0.00800 -0.00010 -0.00840 220 LEU A CB  
1927 C  CG  . LEU A 217 ? 0.15233 0.16623 0.12593 -0.02150 0.01070  0.01790  220 LEU A CG  
1928 C  CD1 . LEU A 217 ? 0.15983 0.14093 0.13623 -0.02300 0.00950  0.00490  220 LEU A CD1 
1929 C  CD2 . LEU A 217 ? 0.17533 0.18213 0.12943 -0.01780 -0.02420 0.01030  220 LEU A CD2 
1930 N  N   . LEU A 218 ? 0.12353 0.15623 0.11653 0.01000  -0.00710 0.00810  221 LEU A N   
1931 C  CA  . LEU A 218 ? 0.13483 0.16033 0.12853 0.02480  -0.01620 0.01350  221 LEU A CA  
1932 C  C   . LEU A 218 ? 0.13713 0.15963 0.13003 0.01080  -0.00760 -0.00120 221 LEU A C   
1933 O  O   . LEU A 218 ? 0.15383 0.17213 0.14203 0.00160  0.00060  -0.01450 221 LEU A O   
1934 C  CB  . LEU A 218 ? 0.16983 0.16353 0.15483 0.04670  -0.00730 0.01330  221 LEU A CB  
1935 C  CG  . LEU A 218 ? 0.22873 0.22753 0.21093 0.06560  -0.02760 0.00210  221 LEU A CG  
1936 C  CD1 . LEU A 218 ? 0.25443 0.24173 0.23633 0.06240  -0.01000 0.00260  221 LEU A CD1 
1937 C  CD2 . LEU A 218 ? 0.25033 0.25593 0.23363 0.07580  -0.05110 -0.00230 221 LEU A CD2 
1938 N  N   . GLN A 219 ? 0.14533 0.15033 0.12623 0.01280  -0.00380 -0.00200 222 GLN A N   
1939 C  CA  . GLN A 219 ? 0.17113 0.14003 0.13513 -0.00070 0.00470  -0.00720 222 GLN A CA  
1940 C  C   . GLN A 219 ? 0.18293 0.13823 0.15833 -0.01030 0.02540  -0.01150 222 GLN A C   
1941 O  O   . GLN A 219 ? 0.21773 0.13053 0.17543 -0.02820 0.06010  -0.02220 222 GLN A O   
1942 C  CB  . GLN A 219 ? 0.18993 0.17383 0.13043 -0.01140 -0.04010 0.02950  222 GLN A CB  
1943 C  CG  . GLN A 219 ? 0.16893 0.17533 0.16203 0.01170  0.00090  0.00710  222 GLN A CG  
1944 C  CD  . GLN A 219 ? 0.14363 0.21583 0.17633 -0.00870 -0.00200 -0.00730 222 GLN A CD  
1945 O  OE1 . GLN A 219 ? 0.17373 0.17203 0.19023 -0.00140 0.00870  0.02800  222 GLN A OE1 
1946 N  NE2 . GLN A 219 ? 0.11853 0.29323 0.20503 -0.00950 0.00290  -0.05990 222 GLN A NE2 
1947 N  N   . PHE A 220 ? 0.16583 0.15473 0.12383 -0.01620 0.01670  -0.01750 223 PHE A N   
1948 C  CA  . PHE A 220 ? 0.17643 0.15843 0.14143 -0.03270 0.03060  -0.03730 223 PHE A CA  
1949 C  C   . PHE A 220 ? 0.23593 0.16503 0.15353 -0.05170 0.04040  -0.04600 223 PHE A C   
1950 O  O   . PHE A 220 ? 0.27823 0.17803 0.16763 -0.06890 0.04870  -0.05450 223 PHE A O   
1951 C  CB  . PHE A 220 ? 0.16843 0.18863 0.18523 -0.02520 0.02640  -0.04370 223 PHE A CB  
1952 C  CG  . PHE A 220 ? 0.16853 0.18793 0.21993 -0.00680 -0.00380 -0.02520 223 PHE A CG  
1953 C  CD1 . PHE A 220 ? 0.16253 0.19483 0.24743 0.00350  0.00240  -0.01620 223 PHE A CD1 
1954 C  CD2 . PHE A 220 ? 0.17493 0.21893 0.23453 0.02010  0.00260  0.00270  223 PHE A CD2 
1955 C  CE1 . PHE A 220 ? 0.14943 0.22753 0.26493 0.04640  -0.02110 0.00930  223 PHE A CE1 
1956 C  CE2 . PHE A 220 ? 0.15923 0.23753 0.24853 0.03100  -0.00600 0.01380  223 PHE A CE2 
1957 C  CZ  . PHE A 220 ? 0.16103 0.24023 0.25663 0.03630  -0.01670 0.02480  223 PHE A CZ  
1958 N  N   . VAL A 221 ? 0.23823 0.15423 0.13413 -0.04680 0.04460  -0.04370 224 VAL A N   
1959 C  CA  . VAL A 221 ? 0.27483 0.16103 0.13683 -0.02910 0.03060  -0.02530 224 VAL A CA  
1960 C  C   . VAL A 221 ? 0.25793 0.16143 0.14983 -0.03210 0.02150  -0.02410 224 VAL A C   
1961 O  O   . VAL A 221 ? 0.25393 0.14563 0.14053 -0.05620 0.02060  -0.03180 224 VAL A O   
1962 C  CB  . VAL A 221 ? 0.31463 0.15483 0.14123 0.01130  0.02790  -0.01670 224 VAL A CB  
1963 C  CG1 . VAL A 221 ? 0.35303 0.15453 0.14113 0.02350  0.02310  0.00890  224 VAL A CG1 
1964 C  CG2 . VAL A 221 ? 0.32873 0.15033 0.16893 0.04330  0.02780  -0.02570 224 VAL A CG2 
1965 N  N   . THR A 222 ? 0.21243 0.17533 0.14933 -0.03140 0.02450  -0.01260 225 THR A N   
1966 C  CA  . THR A 222 ? 0.19273 0.18453 0.14723 -0.00500 0.00740  0.01150  225 THR A CA  
1967 C  C   . THR A 222 ? 0.15823 0.13923 0.14603 0.00270  0.00620  0.00320  225 THR A C   
1968 O  O   . THR A 222 ? 0.19263 0.14913 0.15603 0.01450  0.01080  -0.00360 225 THR A O   
1969 C  CB  . THR A 222 ? 0.23213 0.25043 0.16113 0.00670  -0.02900 0.01580  225 THR A CB  
1970 O  OG1 . THR A 222 ? 0.26673 0.27533 0.16803 -0.01210 -0.04660 0.01510  225 THR A OG1 
1971 C  CG2 . THR A 222 ? 0.22023 0.25423 0.18583 0.03300  -0.03850 0.02590  225 THR A CG2 
1972 N  N   . ALA A 223 ? 0.15013 0.12843 0.14533 0.00840  -0.00920 -0.00720 226 ALA A N   
1973 C  CA  . ALA A 223 ? 0.12893 0.13553 0.14093 0.01450  0.00700  -0.00270 226 ALA A CA  
1974 C  C   . ALA A 223 ? 0.14143 0.13643 0.14653 0.02320  0.00700  -0.02360 226 ALA A C   
1975 O  O   . ALA A 223 ? 0.13993 0.13393 0.16053 0.02070  0.00400  -0.01840 226 ALA A O   
1976 C  CB  . ALA A 223 ? 0.12583 0.15123 0.14313 0.00420  -0.01750 -0.00810 226 ALA A CB  
1977 N  N   A ALA A 224 ? 0.16163 0.15563 0.15933 0.00180  0.00360  -0.01170 227 ALA A N   
1979 C  CA  A ALA A 224 ? 0.15873 0.17203 0.17853 -0.00320 -0.02600 -0.01270 227 ALA A CA  
1981 C  C   A ALA A 224 ? 0.13983 0.18293 0.16573 0.00580  -0.03380 -0.01190 227 ALA A C   
1983 O  O   A ALA A 224 ? 0.16833 0.16063 0.15513 0.02010  -0.02330 -0.00000 227 ALA A O   
1985 C  CB  A ALA A 224 ? 0.18383 0.18103 0.19483 -0.01070 -0.03790 -0.01050 227 ALA A CB  
1987 N  N   A GLY A 225 ? 0.18233 0.22233 0.18273 0.00870  -0.00830 -0.00410 228 GLY A N   
1989 C  CA  A GLY A 225 ? 0.22613 0.24133 0.19313 -0.00950 0.00350  -0.00710 228 GLY A CA  
1991 C  C   A GLY A 225 ? 0.27113 0.26473 0.20193 -0.01410 0.01240  -0.00080 228 GLY A C   
1993 O  O   A GLY A 225 ? 0.29903 0.27923 0.19993 -0.03540 0.02530  0.01800  228 GLY A O   
1995 N  N   A ILE A 226 ? 0.26363 0.25843 0.19993 -0.00150 -0.00320 0.00540  229 ILE A N   
1997 C  CA  A ILE A 226 ? 0.25833 0.26083 0.22873 0.01610  0.00540  -0.00310 229 ILE A CA  
1999 C  C   A ILE A 226 ? 0.29473 0.32853 0.29303 0.03170  0.01880  -0.01460 229 ILE A C   
2001 O  O   A ILE A 226 ? 0.29713 0.35983 0.30663 0.05820  0.01850  -0.01500 229 ILE A O   
2003 C  CB  A ILE A 226 ? 0.23803 0.21943 0.20533 0.03210  -0.00130 -0.00220 229 ILE A CB  
2005 C  CG1 A ILE A 226 ? 0.25143 0.21253 0.19313 0.02680  -0.01040 -0.00620 229 ILE A CG1 
2006 C  CG2 A ILE A 226 ? 0.22943 0.19393 0.22193 0.03920  0.03310  -0.00830 229 ILE A CG2 
2007 C  CD1 A ILE A 226 ? 0.23923 0.20113 0.16393 0.01350  -0.02390 -0.01600 229 ILE A CD1 
2008 N  N   A THR A 227 ? 0.34433 0.37203 0.34983 0.01060  0.01540  -0.02290 230 THR A N   
2019 C  CG2 A THR A 227 ? 0.40113 0.40623 0.41143 -0.01340 0.01440  -0.00780 230 THR A CG2 
2020 N  N   A HIS A 228 ? 0.40963 0.43113 0.42963 -0.04730 -0.01020 0.01090  231 HIS A N   
2022 C  CA  A HIS A 228 ? 0.37033 0.38733 0.39923 -0.03080 -0.00560 0.01310  231 HIS A CA  
2024 C  C   A HIS A 228 ? 0.38803 0.39953 0.40433 -0.02830 0.01070  0.01750  231 HIS A C   
2028 C  CB  A HIS A 228 ? 0.33243 0.34603 0.37163 -0.02080 -0.01440 0.01140  231 HIS A CB  
2032 CL CL  . CL  B .   ? 0.16583 0.15923 0.21433 -0.00130 -0.00140 -0.01860 301 CL  A CL  
2033 CL CL  . CL  C .   ? 0.23393 0.22703 0.17143 -0.02290 -0.01380 0.02230  302 CL  A CL  
2034 O  O   A HOH D .   ? 0.13353 0.19893 0.28143 0.02280  -0.00930 -0.10310 401 HOH A O   
2036 O  O   A HOH D .   ? 0.31993 0.29373 0.25813 0.10120  -0.04000 -0.09550 402 HOH A O   
2038 O  O   . HOH D .   ? 0.14713 0.14443 0.15063 -0.00240 0.01200  -0.00040 403 HOH A O   
2039 O  O   A HOH D .   ? 0.24033 0.25283 0.22403 0.07550  -0.00570 -0.02380 404 HOH A O   
2041 O  O   . HOH D .   ? 0.12383 0.10813 0.12473 -0.00320 -0.00340 0.00210  405 HOH A O   
2043 O  O   B HOH D .   ? 0.10663 0.06103 0.08343 0.00520  0.00430  0.00700  406 HOH A O   
2044 O  O   . HOH D .   ? 0.14013 0.15573 0.20073 0.02000  0.03020  0.03070  407 HOH A O   
2045 O  O   . HOH D .   ? 0.14683 0.09493 0.11163 0.00730  -0.00570 -0.00530 408 HOH A O   
2046 O  O   . HOH D .   ? 0.13423 0.15703 0.19353 0.01060  -0.00170 -0.03510 409 HOH A O   
2047 O  O   . HOH D .   ? 0.23723 0.17163 0.21663 -0.04890 -0.00140 -0.00190 410 HOH A O   
2048 O  O   . HOH D .   ? 0.12093 0.09973 0.12573 -0.00400 -0.00970 0.00380  411 HOH A O   
2049 O  O   . HOH D .   ? 0.14943 0.11233 0.12783 -0.00490 0.00670  -0.00450 412 HOH A O   
2050 O  O   . HOH D .   ? 0.15593 0.11103 0.14913 -0.00040 -0.01610 -0.01600 413 HOH A O   
2051 O  O   . HOH D .   ? 0.20823 0.20753 0.38463 0.03710  -0.08100 -0.05140 414 HOH A O   
2052 O  O   . HOH D .   ? 0.15933 0.10013 0.15843 0.00910  -0.00070 -0.01110 415 HOH A O   
2053 O  O   . HOH D .   ? 0.35943 0.36273 0.40353 0.04500  0.14270  0.03930  416 HOH A O   
2054 O  O   . HOH D .   ? 0.36033 0.29593 0.32053 0.07620  -0.09050 -0.07790 417 HOH A O   
2055 O  O   . HOH D .   ? 0.13143 0.13143 0.12293 -0.00340 -0.00270 0.01070  418 HOH A O   
2056 O  O   . HOH D .   ? 0.15093 0.09293 0.14943 -0.00300 -0.01130 -0.00100 419 HOH A O   
2057 O  O   A HOH D .   ? 0.31783 0.23073 0.17123 0.05190  -0.00080 -0.00530 420 HOH A O   
2060 O  O   . HOH D .   ? 0.34713 0.37793 0.35453 0.08480  0.06630  -0.10790 422 HOH A O   
2061 O  O   . HOH D .   ? 0.27913 0.27663 0.43253 0.05720  -0.09100 0.00830  423 HOH A O   
2062 O  O   . HOH D .   ? 0.18193 0.18913 0.24983 0.02270  0.01530  0.01390  424 HOH A O   
2063 O  O   . HOH D .   ? 0.26373 0.35703 0.37883 -0.09020 -0.05840 -0.09110 425 HOH A O   
2064 O  O   A HOH D .   ? 0.13993 0.08623 0.12433 0.01890  -0.02860 -0.00280 426 HOH A O   
2066 O  O   . HOH D .   ? 0.31683 0.33653 0.27913 -0.12660 -0.06220 0.00570  427 HOH A O   
2067 O  O   . HOH D .   ? 0.17753 0.11303 0.16203 0.00940  0.00620  0.00020  428 HOH A O   
2068 O  O   . HOH D .   ? 0.23763 0.24483 0.23643 -0.06710 0.05050  -0.06780 429 HOH A O   
2069 O  O   . HOH D .   ? 0.40493 0.33433 0.37293 -0.01760 -0.00600 0.09350  430 HOH A O   
2070 O  O   . HOH D .   ? 0.25833 0.28733 0.26453 -0.03570 0.02120  0.01450  431 HOH A O   
2073 O  O   B HOH D .   ? 0.17693 0.21733 0.24163 0.02000  -0.05050 -0.02190 433 HOH A O   
2074 O  O   . HOH D .   ? 0.17763 0.16773 0.25273 -0.01510 -0.00380 -0.04060 434 HOH A O   
2076 O  O   . HOH D .   ? 0.13883 0.09613 0.13663 0.00350  -0.00080 0.00990  436 HOH A O   
2077 O  O   A HOH D .   ? 0.35553 0.31333 0.36373 0.01070  -0.00370 0.04070  437 HOH A O   
2078 O  O   . HOH D .   ? 0.15813 0.14153 0.13353 -0.01810 -0.01650 -0.01920 438 HOH A O   
2081 O  O   . HOH D .   ? 0.28773 0.41123 0.39953 -0.04400 0.04170  -0.01800 440 HOH A O   
2083 O  O   A HOH D .   ? 0.26873 0.22943 0.23133 -0.02500 0.02540  0.05340  442 HOH A O   
2088 O  O   B HOH D .   ? 0.32683 0.26783 0.25793 0.00460  0.09210  -0.04150 445 HOH A O   
2090 O  O   . HOH D .   ? 0.16013 0.10603 0.13533 0.00880  -0.00960 0.00350  447 HOH A O   
2091 O  O   . HOH D .   ? 0.17463 0.13983 0.15393 -0.01140 -0.01370 0.02320  448 HOH A O   
2093 O  O   . HOH D .   ? 0.28513 0.20603 0.16773 0.03480  0.01600  0.01800  450 HOH A O   
2094 O  O   . HOH D .   ? 0.41193 0.25643 0.35263 -0.03740 -0.02060 0.06760  451 HOH A O   
2100 O  O   . HOH D .   ? 0.40403 0.33933 0.34853 0.06090  0.08530  -0.02710 456 HOH A O   
2101 O  O   . HOH D .   ? 0.26083 0.21873 0.27703 -0.03600 0.07760  -0.03290 457 HOH A O   
2102 O  O   . HOH D .   ? 0.16943 0.17293 0.16203 -0.01500 -0.00830 0.01130  458 HOH A O   
2104 O  O   A HOH D .   ? 0.24913 0.23923 0.20443 -0.04570 0.05670  -0.00850 460 HOH A O   
2106 O  O   . HOH D .   ? 0.29083 0.18403 0.26213 -0.04160 0.00740  -0.02060 461 HOH A O   
2107 O  O   . HOH D .   ? 0.28353 0.25183 0.21043 0.08760  0.01360  0.01280  462 HOH A O   
2108 O  O   . HOH D .   ? 0.27043 0.37673 0.38973 0.01640  -0.08920 -0.04200 463 HOH A O   
2110 O  O   . HOH D .   ? 0.18613 0.24873 0.21873 0.05980  -0.00870 -0.00840 465 HOH A O   
2112 O  O   A HOH D .   ? 0.37683 0.33003 0.23853 0.03880  -0.10190 0.04140  467 HOH A O   
2114 O  O   . HOH D .   ? 0.33113 0.40623 0.35573 0.00920  -0.00080 0.05810  468 HOH A O   
2115 O  O   . HOH D .   ? 0.31413 0.32403 0.35893 0.05620  -0.05820 -0.08280 469 HOH A O   
2116 O  O   A HOH D .   ? 0.19803 0.16403 0.34933 -0.01540 -0.06760 -0.03480 470 HOH A O   
2119 O  O   A HOH D .   ? 0.14323 0.09623 0.16773 -0.00230 0.01550  0.00410  472 HOH A O   
2122 O  O   . HOH D .   ? 0.35243 0.22263 0.19893 -0.11130 -0.09400 0.04540  474 HOH A O   
2123 O  O   . HOH D .   ? 0.16093 0.21213 0.32593 0.00870  -0.03730 0.03810  475 HOH A O   
2124 O  O   . HOH D .   ? 0.28003 0.15403 0.19003 -0.01790 -0.04110 0.02400  476 HOH A O   
2128 O  O   . HOH D .   ? 0.21343 0.18773 0.24543 0.01360  -0.01200 -0.01060 480 HOH A O   
2129 O  O   . HOH D .   ? 0.36513 0.38873 0.29453 0.07240  -0.05480 -0.00220 481 HOH A O   
2130 O  O   . HOH D .   ? 0.37563 0.38113 0.26073 -0.06200 -0.05410 -0.01790 482 HOH A O   
2131 O  O   . HOH D .   ? 0.18493 0.14283 0.17913 0.01190  -0.00350 0.01590  483 HOH A O   
2133 O  O   . HOH D .   ? 0.23123 0.23983 0.16783 -0.03110 0.01360  0.01730  485 HOH A O   
2135 O  O   A HOH D .   ? 0.31013 0.25543 0.25203 0.08840  -0.04880 -0.04190 487 HOH A O   
2136 O  O   . HOH D .   ? 0.35323 0.22853 0.26033 0.02830  0.02400  -0.00650 488 HOH A O   
2137 O  O   . HOH D .   ? 0.30873 0.39193 0.33793 0.09880  -0.04770 0.04810  489 HOH A O   
2138 O  O   A HOH D .   ? 0.13273 0.09613 0.15743 -0.00060 -0.00480 -0.00370 490 HOH A O   
2139 O  O   . HOH D .   ? 0.30023 0.24163 0.48133 0.09520  0.01180  0.03650  491 HOH A O   
2140 O  O   . HOH D .   ? 0.16653 0.11673 0.14793 0.00580  0.00270  -0.00220 492 HOH A O   
2142 O  O   . HOH D .   ? 0.19063 0.22903 0.25303 -0.02890 -0.03850 0.03200  494 HOH A O   
2143 O  O   . HOH D .   ? 0.17333 0.13873 0.17543 -0.02450 0.00020  0.01640  495 HOH A O   
2144 O  O   . HOH D .   ? 0.16543 0.14863 0.23323 0.02160  0.00200  -0.00140 496 HOH A O   
2145 O  O   . HOH D .   ? 0.15613 0.14603 0.17063 -0.00870 0.00060  -0.00940 497 HOH A O   
2147 O  O   B HOH D .   ? 0.27253 0.26043 0.21283 0.08110  0.02920  0.03760  498 HOH A O   
2148 O  O   A HOH D .   ? 0.25683 0.25713 0.30543 0.04280  0.04170  -0.00560 499 HOH A O   
2150 O  O   A HOH D .   ? 0.20423 0.23703 0.17403 -0.01970 -0.01520 0.00890  500 HOH A O   
2152 O  O   A HOH D .   ? 0.23183 0.20393 0.21523 0.05850  -0.08310 -0.04430 501 HOH A O   
2154 O  O   . HOH D .   ? 0.27883 0.34193 0.19743 -0.00840 -0.00400 0.03270  502 HOH A O   
2155 O  O   B HOH D .   ? 0.18423 0.22273 0.21763 -0.01330 -0.03480 0.00080  503 HOH A O   
2159 O  O   A HOH D .   ? 0.21063 0.25303 0.25473 0.03540  -0.02690 -0.02520 507 HOH A O   
2161 O  O   A HOH D .   ? 0.32573 0.37683 0.22483 0.06120  -0.11040 -0.07040 508 HOH A O   
2162 O  O   . HOH D .   ? 0.26223 0.16183 0.23713 0.02780  0.07070  0.00720  509 HOH A O   
2164 O  O   . HOH D .   ? 0.36133 0.32733 0.28553 -0.01750 -0.02470 0.07410  511 HOH A O   
2165 O  O   . HOH D .   ? 0.22953 0.25683 0.25433 -0.10220 0.05300  -0.01860 512 HOH A O   
2166 O  O   . HOH D .   ? 0.22473 0.14103 0.23203 0.04040  0.02780  0.04700  513 HOH A O   
2167 O  O   . HOH D .   ? 0.16463 0.15323 0.16363 -0.00080 -0.00790 0.01140  514 HOH A O   
2169 O  O   . HOH D .   ? 0.26443 0.15583 0.22073 0.05390  0.03760  -0.00750 516 HOH A O   
2170 O  O   . HOH D .   ? 0.38483 0.20673 0.27043 -0.05420 0.10270  -0.05350 517 HOH A O   
2171 O  O   B HOH D .   ? 0.28483 0.32843 0.25283 0.01740  0.03440  0.01020  518 HOH A O   
2174 O  O   . HOH D .   ? 0.27493 0.24763 0.31993 0.06170  0.01080  0.09050  521 HOH A O   
2175 O  O   A HOH D .   ? 0.27913 0.32513 0.26563 -0.00570 -0.04690 0.02430  522 HOH A O   
2177 O  O   . HOH D .   ? 0.35993 0.32843 0.23843 0.11260  0.02900  0.03790  523 HOH A O   
2179 O  O   . HOH D .   ? 0.18863 0.21703 0.21983 0.02540  -0.00350 0.01830  525 HOH A O   
2180 O  O   . HOH D .   ? 0.23183 0.23343 0.23363 0.01450  -0.02340 0.01600  526 HOH A O   
2181 O  O   A HOH D .   ? 0.21333 0.17023 0.26023 0.02990  -0.02370 0.01350  527 HOH A O   
2182 O  O   . HOH D .   ? 0.17693 0.27313 0.15753 -0.02670 0.01490  -0.00950 528 HOH A O   
2184 O  O   . HOH D .   ? 0.18143 0.13753 0.15233 0.00880  0.00850  -0.01160 530 HOH A O   
2185 O  O   A HOH D .   ? 0.19033 0.15063 0.13943 -0.03160 -0.00520 0.05240  531 HOH A O   
2187 O  O   . HOH D .   ? 0.28753 0.31083 0.42173 -0.05030 0.07850  -0.08440 532 HOH A O   
2188 O  O   A HOH D .   ? 0.38083 0.34733 0.30223 -0.07320 0.01470  -0.05170 533 HOH A O   
2191 O  O   B HOH D .   ? 0.30193 0.26973 0.33623 0.07730  -0.01460 -0.00450 534 HOH A O   
2195 O  O   B HOH D .   ? 0.27823 0.33853 0.29853 0.01700  -0.06740 -0.01500 537 HOH A O   
2196 O  O   A HOH D .   ? 0.21783 0.18753 0.22653 -0.03430 -0.03160 0.03260  538 HOH A O   
2198 O  O   . HOH D .   ? 0.39553 0.31573 0.42853 0.03500  0.03450  -0.00030 539 HOH A O   
2199 O  O   . HOH D .   ? 0.26993 0.24683 0.23123 -0.00240 0.04380  0.09800  540 HOH A O   
2200 O  O   . HOH D .   ? 0.27083 0.32143 0.16213 0.00980  -0.05440 -0.02290 541 HOH A O   
2201 O  O   . HOH D .   ? 0.18273 0.15733 0.19923 -0.02340 -0.03120 0.00680  542 HOH A O   
2202 O  O   A HOH D .   ? 0.13303 0.17153 0.17693 0.00860  -0.02220 -0.03020 543 HOH A O   
2204 O  O   A HOH D .   ? 0.16103 0.13053 0.31633 -0.00370 -0.03900 0.00050  544 HOH A O   
2206 O  O   A HOH D .   ? 0.31513 0.28313 0.32733 0.07500  -0.00070 0.09450  545 HOH A O   
2209 O  O   B HOH D .   ? 0.27683 0.30003 0.30003 0.02720  -0.02760 -0.05990 546 HOH A O   
2212 O  O   . HOH D .   ? 0.16503 0.15013 0.17453 0.01990  -0.00080 -0.00250 549 HOH A O   
2213 O  O   . HOH D .   ? 0.33513 0.45633 0.31043 -0.00180 0.10050  0.03460  550 HOH A O   
2215 O  O   A HOH D .   ? 0.26263 0.22883 0.21653 -0.04620 0.00550  0.06710  552 HOH A O   
2217 O  O   A HOH D .   ? 0.27073 0.25303 0.25733 -0.11800 0.05110  0.04360  553 HOH A O   
2219 O  O   A HOH D .   ? 0.37193 0.37833 0.37453 -0.00830 0.08270  0.02920  554 HOH A O   
2220 O  O   . HOH D .   ? 0.17893 0.15793 0.17703 -0.03510 0.01690  -0.01550 555 HOH A O   
2221 O  O   A HOH D .   ? 0.30203 0.27303 0.32453 -0.02320 0.15240  0.07180  556 HOH A O   
2223 O  O   . HOH D .   ? 0.18803 0.12533 0.17353 -0.00570 -0.02290 0.00310  557 HOH A O   
2225 O  O   B HOH D .   ? 0.20823 0.26583 0.32053 0.06070  -0.02100 0.00100  558 HOH A O   
2226 O  O   . HOH D .   ? 0.29543 0.35803 0.42543 -0.08000 -0.03460 -0.01620 559 HOH A O   
2229 O  O   . HOH D .   ? 0.28183 0.41583 0.36293 0.00120  0.07840  0.12980  562 HOH A O   
2231 O  O   . HOH D .   ? 0.17053 0.14173 0.14483 0.04000  -0.01100 -0.01490 564 HOH A O   
2234 O  O   . HOH D .   ? 0.20583 0.27073 0.44193 -0.07900 -0.05260 0.03190  566 HOH A O   
2235 O  O   A HOH D .   ? 0.26763 0.35353 0.29223 -0.06280 -0.03600 0.06230  567 HOH A O   
2237 O  O   A HOH D .   ? 0.12923 0.18993 0.12553 0.01350  -0.01430 -0.02160 568 HOH A O   
2239 O  O   . HOH D .   ? 0.20463 0.23633 0.24843 -0.06330 0.01890  -0.05960 569 HOH A O   
2240 O  O   . HOH D .   ? 0.15973 0.21393 0.18223 0.00920  0.01850  -0.01200 570 HOH A O   
2241 O  O   A HOH D .   ? 0.34843 0.38523 0.36143 0.03660  -0.07150 0.04370  571 HOH A O   
2242 O  O   . HOH D .   ? 0.27923 0.34563 0.24293 -0.01590 0.10140  0.02470  572 HOH A O   
2248 O  O   . HOH D .   ? 0.34693 0.35253 0.38703 0.08430  -0.07050 0.00750  578 HOH A O   
2250 O  O   . HOH D .   ? 0.24163 0.17373 0.23003 0.01620  -0.02720 0.02500  580 HOH A O   
2252 O  O   . HOH D .   ? 0.38873 0.19883 0.27253 0.11130  -0.07110 -0.00800 582 HOH A O   
2253 O  O   . HOH D .   ? 0.35043 0.31313 0.38073 -0.02980 -0.00290 -0.03180 583 HOH A O   
2254 O  O   . HOH D .   ? 0.29603 0.18943 0.20923 0.09160  0.01100  -0.02000 584 HOH A O   
2255 O  O   . HOH D .   ? 0.24843 0.31083 0.21343 0.06280  0.03550  -0.00840 585 HOH A O   
2258 O  O   . HOH D .   ? 0.18753 0.18603 0.20233 -0.04960 -0.00400 -0.00130 588 HOH A O   
2261 O  O   . HOH D .   ? 0.17973 0.18773 0.16713 0.03450  -0.00220 0.00320  591 HOH A O   
2262 O  O   . HOH D .   ? 0.33253 0.42943 0.33583 0.01740  0.10540  0.02250  592 HOH A O   
2263 O  O   . HOH D .   ? 0.24213 0.20313 0.19553 0.03860  -0.04210 0.01250  593 HOH A O   
2264 O  O   . HOH D .   ? 0.26873 0.20663 0.21673 0.03260  -0.00790 -0.00830 594 HOH A O   
2265 O  O   . HOH D .   ? 0.17393 0.24803 0.19813 -0.02730 0.02470  0.02240  595 HOH A O   
2267 O  O   A HOH D .   ? 0.20033 0.19043 0.18003 -0.01910 -0.03830 -0.00240 597 HOH A O   
2269 O  O   . HOH D .   ? 0.20843 0.17743 0.18483 -0.02240 0.02820  -0.04000 598 HOH A O   
2270 O  O   . HOH D .   ? 0.29203 0.33843 0.29823 0.02440  -0.08010 -0.03510 599 HOH A O   
2272 O  O   A HOH D .   ? 0.20583 0.29503 0.25933 -0.02220 -0.02530 -0.05910 601 HOH A O   
2273 O  O   A HOH D .   ? 0.21283 0.15403 0.17153 0.04790  -0.03480 -0.05100 602 HOH A O   
2275 O  O   . HOH D .   ? 0.32843 0.19783 0.30393 -0.00250 -0.01840 -0.01830 603 HOH A O   
2280 O  O   . HOH D .   ? 0.30123 0.33603 0.28943 0.06280  0.03090  0.08070  608 HOH A O   
2281 O  O   A HOH D .   ? 0.18693 0.29093 0.16753 0.04580  0.03440  0.02440  609 HOH A O   
2282 O  O   A HOH D .   ? 0.15043 0.11663 0.23603 0.01330  -0.04480 0.02840  610 HOH A O   
2290 O  O   . HOH D .   ? 0.27493 0.36703 0.26433 0.04480  0.04660  0.01940  616 HOH A O   
2291 O  O   . HOH D .   ? 0.28733 0.22263 0.30183 0.00850  0.04610  0.02260  617 HOH A O   
2294 O  O   B HOH D .   ? 0.12893 0.13593 0.25923 0.00700  0.00050  0.01240  619 HOH A O   
2297 O  O   A HOH D .   ? 0.33993 0.25943 0.31063 0.04410  -0.01310 0.00950  622 HOH A O   
2299 O  O   . HOH D .   ? 0.35513 0.29093 0.41483 0.07160  -0.02110 -0.12870 623 HOH A O   
2300 O  O   . HOH D .   ? 0.33993 0.40333 0.35213 -0.01280 -0.02550 -0.00840 624 HOH A O   
2303 O  O   A HOH D .   ? 0.33093 0.31883 0.29573 -0.04400 0.01160  -0.01240 627 HOH A O   
2306 O  O   . HOH D .   ? 0.22413 0.16543 0.32043 0.03870  -0.03510 -0.01770 629 HOH A O   
2308 O  O   . HOH D .   ? 0.33183 0.29083 0.31253 0.06680  0.08280  -0.11460 631 HOH A O   
2309 O  O   . HOH D .   ? 0.35043 0.31323 0.31063 -0.04500 0.02190  -0.05400 632 HOH A O   
2310 O  O   . HOH D .   ? 0.22813 0.20013 0.29143 0.05060  -0.02300 0.01440  633 HOH A O   
2312 O  O   . HOH D .   ? 0.18033 0.18773 0.24293 0.00180  0.00240  -0.01730 635 HOH A O   
2314 O  O   . HOH D .   ? 0.39903 0.24903 0.25373 -0.01630 -0.00650 0.01250  637 HOH A O   
2315 O  O   . HOH D .   ? 0.39923 0.42833 0.43883 -0.00410 -0.01380 0.02040  638 HOH A O   
2317 O  O   . HOH D .   ? 0.38253 0.38423 0.39213 -0.03550 0.00350  0.01430  640 HOH A O   
2318 O  O   . HOH D .   ? 0.20623 0.23263 0.29663 0.05950  0.05650  -0.03960 641 HOH A O   
2320 O  O   . HOH D .   ? 0.23503 0.17243 0.17133 -0.00290 -0.01810 -0.02130 643 HOH A O   
2321 O  O   . HOH D .   ? 0.31203 0.30773 0.35343 0.01700  -0.06930 -0.02270 644 HOH A O   
2322 O  O   . HOH D .   ? 0.29383 0.33083 0.22533 -0.09270 0.01070  -0.02570 645 HOH A O   
2324 O  O   B HOH D .   ? 0.32453 0.34153 0.32843 0.01150  -0.04360 -0.00440 646 HOH A O   
2325 O  O   . HOH D .   ? 0.27413 0.41113 0.35373 0.03860  0.03970  -0.13490 647 HOH A O   
2326 O  O   . HOH D .   ? 0.18613 0.38723 0.24533 -0.04560 -0.00850 0.03400  648 HOH A O   
2332 O  O   . HOH D .   ? 0.15913 0.19263 0.16293 -0.01430 -0.02490 -0.02270 653 HOH A O   
2333 O  O   . HOH D .   ? 0.30313 0.35153 0.46063 -0.06550 0.06440  0.04740  654 HOH A O   
2334 O  O   . HOH D .   ? 0.29783 0.41713 0.33213 -0.00630 -0.04990 -0.03270 655 HOH A O   
2337 O  O   B HOH D .   ? 0.37493 0.37533 0.36143 0.00100  0.06570  0.01620  657 HOH A O   
2338 O  O   . HOH D .   ? 0.22063 0.23573 0.33873 0.05650  0.05590  0.07370  658 HOH A O   
2339 O  O   . HOH D .   ? 0.30543 0.29363 0.41503 0.04950  -0.06480 0.01090  659 HOH A O   
2341 O  O   . HOH D .   ? 0.28943 0.22613 0.18403 0.01850  -0.01480 -0.01060 661 HOH A O   
2342 O  O   A HOH D .   ? 0.36573 0.29903 0.38603 -0.00980 -0.08540 0.00550  662 HOH A O   
2347 O  O   . HOH D .   ? 0.51013 0.22773 0.31573 0.06830  -0.00110 0.11690  665 HOH A O   
2348 O  O   . HOH D .   ? 0.32343 0.20213 0.15723 -0.01640 0.01600  0.01810  666 HOH A O   
2349 O  O   A HOH D .   ? 0.26323 0.26183 0.30153 -0.00810 -0.03140 -0.01900 667 HOH A O   
2353 O  O   . HOH D .   ? 0.20133 0.21713 0.33163 -0.02120 0.05050  0.04680  670 HOH A O   
2356 O  O   . HOH D .   ? 0.30743 0.35973 0.39233 -0.06230 0.08930  0.08260  673 HOH A O   
2357 O  O   . HOH D .   ? 0.29403 0.25873 0.34463 -0.03360 0.04690  0.05710  674 HOH A O   
2361 O  O   . HOH D .   ? 0.39653 0.34173 0.24473 0.04600  -0.11060 -0.02040 678 HOH A O   
2363 O  O   . HOH D .   ? 0.38763 0.25013 0.31993 0.01330  0.02020  0.02640  681 HOH A O   
2364 O  O   . HOH D .   ? 0.14993 0.14033 0.42023 -0.01400 0.00660  -0.04870 682 HOH A O   
2367 O  O   A HOH D .   ? 0.22643 0.17373 0.18283 -0.00810 -0.02310 0.02990  685 HOH A O   
2372 O  O   B HOH D .   ? 0.32463 0.32063 0.31693 0.03340  -0.08890 0.02520  688 HOH A O   
2373 O  O   A HOH D .   ? 0.37903 0.22493 0.13893 0.06000  0.04040  0.02960  689 HOH A O   
2376 O  O   . HOH D .   ? 0.26233 0.29583 0.32333 -0.00300 -0.09660 0.06240  691 HOH A O   
2377 O  O   A HOH D .   ? 0.28493 0.20903 0.21303 -0.02770 -0.03270 -0.00980 692 HOH A O   
2382 O  O   . HOH D .   ? 0.25863 0.16553 0.20953 -0.06960 -0.00190 0.00170  696 HOH A O   
2384 O  O   . HOH D .   ? 0.36473 0.31533 0.42183 0.00530  0.06980  0.05110  698 HOH A O   
2385 O  O   . HOH D .   ? 0.30163 0.32513 0.32343 0.05100  0.00210  -0.08980 699 HOH A O   
2386 O  O   A HOH D .   ? 0.25933 0.18473 0.19713 -0.01660 -0.01170 0.02560  700 HOH A O   
2389 O  O   A HOH D .   ? 0.43153 0.26093 0.36613 0.04690  0.00310  -0.03550 702 HOH A O   
2391 O  O   . HOH D .   ? 0.29263 0.40023 0.34413 -0.03290 0.00220  0.03710  703 HOH A O   
2392 O  O   . HOH D .   ? 0.31173 0.30123 0.29763 -0.03770 -0.00840 -0.02440 704 HOH A O   
2393 O  O   . HOH D .   ? 0.19283 0.26543 0.39963 0.09220  -0.04590 -0.01820 705 HOH A O   
2394 O  O   A HOH D .   ? 0.34753 0.27093 0.18493 0.00960  0.03800  -0.08110 706 HOH A O   
2397 O  O   . HOH D .   ? 0.42033 0.26123 0.35163 -0.07620 -0.02920 -0.03720 708 HOH A O   
2399 O  O   . HOH D .   ? 0.38723 0.27263 0.34173 0.06980  -0.04620 0.06880  710 HOH A O   
2402 O  O   . HOH D .   ? 0.32363 0.30153 0.39403 -0.08020 -0.04200 0.00020  713 HOH A O   
2403 O  O   . HOH D .   ? 0.27313 0.41453 0.25643 -0.03120 -0.01490 -0.05870 714 HOH A O   
2407 O  O   A HOH D .   ? 0.38653 0.38483 0.33303 0.00550  0.00780  -0.03010 718 HOH A O   
2409 O  O   A HOH D .   ? 0.16643 0.17153 0.13793 0.01330  -0.00700 0.00340  719 HOH A O   
2411 O  O   . HOH D .   ? 0.15093 0.18483 0.21493 0.01100  -0.03720 -0.05550 720 HOH A O   
2413 O  O   . HOH D .   ? 0.33283 0.41183 0.39533 0.06360  0.00640  0.03650  722 HOH A O   
2414 O  O   . HOH D .   ? 0.39933 0.13643 0.15533 0.05150  0.00950  -0.02270 723 HOH A O   
2416 O  O   . HOH D .   ? 0.36143 0.37553 0.31763 0.08020  0.05560  0.00670  725 HOH A O   
2425 O  O   . HOH D .   ? 0.32673 0.26713 0.39993 -0.01470 0.00840  -0.06660 731 HOH A O   
2427 O  O   . HOH D .   ? 0.18283 0.19823 0.15503 0.00140  0.01290  0.00090  733 HOH A O   
2429 O  O   . HOH D .   ? 0.17223 0.15553 0.18813 0.02690  0.00150  0.00070  735 HOH A O   
2433 O  O   . HOH D .   ? 0.22233 0.22603 0.18743 0.06600  -0.03740 -0.02970 738 HOH A O   
2434 O  O   A HOH D .   ? 0.31303 0.20413 0.21723 0.05640  0.01240  -0.00630 739 HOH A O   
2436 O  O   . HOH D .   ? 0.28863 0.28853 0.16873 -0.03650 0.02260  -0.03800 740 HOH A O   
2440 O  O   . HOH D .   ? 0.33373 0.17853 0.24283 0.01330  0.00410  -0.00540 744 HOH A O   
2441 O  O   A HOH D .   ? 0.23393 0.23863 0.26173 0.01390  0.03240  0.01090  745 HOH A O   
2444 O  O   . HOH D .   ? 0.35783 0.29803 0.27963 -0.04900 0.07120  0.05820  747 HOH A O   
2447 O  O   . HOH D .   ? 0.38933 0.37633 0.28933 -0.03990 -0.04010 0.00890  750 HOH A O   
2450 O  O   A HOH D .   ? 0.28733 0.26953 0.33313 -0.02770 -0.02370 0.01220  753 HOH A O   
2456 O  O   . HOH D .   ? 0.26303 0.26563 0.46873 0.09270  0.09280  -0.07800 757 HOH A O   
2458 O  O   . HOH D .   ? 0.17563 0.14283 0.19303 0.01910  0.02420  -0.01010 759 HOH A O   
2461 O  O   A HOH D .   ? 0.29263 0.17333 0.22643 0.04260  -0.02160 -0.02670 762 HOH A O   
2463 O  O   . HOH D .   ? 0.41263 0.28433 0.28553 -0.00690 -0.01200 0.02110  763 HOH A O   
2464 O  O   . HOH D .   ? 0.38083 0.32493 0.34153 -0.06230 -0.05590 -0.08690 764 HOH A O   
2467 O  O   A HOH D .   ? 0.30313 0.34503 0.28443 0.01280  0.01330  0.03320  767 HOH A O   
2469 O  O   . HOH D .   ? 0.33103 0.37833 0.41553 0.08380  -0.01110 -0.02230 768 HOH A O   
2472 O  O   B HOH D .   ? 0.32293 0.39563 0.33483 -0.01120 -0.04560 -0.03720 771 HOH A O   
2475 O  O   . HOH D .   ? 0.38703 0.20603 0.33083 -0.05880 0.13500  0.00770  774 HOH A O   
2476 O  O   . HOH D .   ? 0.40223 0.28193 0.44153 -0.07380 0.07140  -0.00460 775 HOH A O   
2477 O  O   . HOH D .   ? 0.35903 0.37053 0.36653 -0.00570 0.01150  -0.04010 776 HOH A O   
2479 O  O   . HOH D .   ? 0.26093 0.18823 0.32953 0.06150  0.04900  0.00540  778 HOH A O   
2480 O  O   A HOH D .   ? 0.25413 0.30783 0.22023 -0.00610 0.00480  0.02580  779 HOH A O   
2482 O  O   . HOH D .   ? 0.29843 0.19923 0.21773 0.01020  0.02040  -0.02060 780 HOH A O   
2485 O  O   . HOH D .   ? 0.33083 0.38943 0.21873 0.05760  -0.07760 -0.06150 783 HOH A O   
2489 O  O   . HOH D .   ? 0.30903 0.28273 0.45423 -0.08890 -0.09150 -0.02320 787 HOH A O   
2490 O  O   . HOH D .   ? 0.36853 0.21983 0.26673 0.02880  -0.01180 -0.00550 788 HOH A O   
2491 O  O   . HOH D .   ? 0.38503 0.37313 0.38043 0.06470  0.04610  0.02080  789 HOH A O   
2492 O  O   . HOH D .   ? 0.12683 0.09753 0.17453 0.00210  0.01170  0.01090  790 HOH A O   
2498 O  O   . HOH D .   ? 0.27233 0.20273 0.29883 -0.01610 0.04620  0.04440  795 HOH A O   
2499 O  O   A HOH D .   ? 0.27543 0.29573 0.24003 0.11290  0.08660  0.01410  796 HOH A O   
2500 O  O   . HOH D .   ? 0.37853 0.38033 0.36953 -0.03690 0.05040  0.04710  797 HOH A O   
2501 O  O   . HOH D .   ? 0.18253 0.17763 0.15793 -0.01500 -0.00860 -0.00540 798 HOH A O   
2503 O  O   A HOH D .   ? 0.19173 0.19173 0.21953 -0.04170 -0.06150 -0.07330 800 HOH A O   
2505 O  O   . HOH D .   ? 0.25723 0.34663 0.26953 -0.06080 0.04250  -0.04840 801 HOH A O   
2506 O  O   A HOH D .   ? 0.31293 0.21303 0.18723 0.02530  0.03380  -0.03460 802 HOH A O   
2508 O  O   . HOH D .   ? 0.15433 0.17463 0.18483 -0.00430 0.01000  -0.02080 803 HOH A O   
2509 O  O   . HOH D .   ? 0.31643 0.21853 0.38203 0.05000  0.02910  0.01120  804 HOH A O   
2510 O  O   . HOH D .   ? 0.21893 0.21093 0.29663 -0.01550 0.05410  -0.02660 805 HOH A O   
2512 O  O   . HOH D .   ? 0.22943 0.28743 0.29923 0.02840  -0.10220 -0.06840 807 HOH A O   
# 
