data_8R3N
# 
_entry.id   8R3N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   8R3N         pdb_00008r3n 10.2210/pdb8r3n/pdb 
WWPDB D_1292134464 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8R3N 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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              mw240@cam.ac.uk 
_pdbx_contact_author.name_first         Martin 
_pdbx_contact_author.name_last          Welch 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3646-1733 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Grimm, L.'    1 0000-0003-3372-9618 
'Wijaya, A.J.' 2 0009-0006-0378-376X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108374 
_citation.page_last                 108374 
_citation.title                     'Pseudomonas aeruginosa PfpI is a methylglyoxalase.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108374 
_citation.pdbx_database_id_PubMed   40043953 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Grimm, L.'    1 ? 
primary 'Wijaya, A.'   2 ? 
primary 'Askenasy, I.' 3 ? 
primary 'Nazeer, R.R.' 4 ? 
primary 'Seki, H.'     5 ? 
primary 'Brear, P.D.'  6 ? 
primary 'Figueroa, W.' 7 ? 
primary 'Spring, D.R.' 8 ? 
primary 'Welch, M.'    9 ? 
# 
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 'Protease PfpI' 19268.674 2   ? ? ? ? 
2 water   nat water           18.015    348 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTQSLHGKVVAALVTDGFEQVELTGPKKALEDAGATVRILSDKAGEVRGWNHHQPAEAFRVDGTFEDASLDDYDALLLPG
GVINSDQIRSLAKAQELAIRAEQASKPVAVICHGAWLLISAGLVQGRTLTSWPSLKDDINNAGGHWVDQEVAVDGKLVSS
RKPEDIPAFNRRFIEILAG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTQSLHGKVVAALVTDGFEQVELTGPKKALEDAGATVRILSDKAGEVRGWNHHQPAEAFRVDGTFEDASLDDYDALLLPG
GVINSDQIRSLAKAQELAIRAEQASKPVAVICHGAWLLISAGLVQGRTLTSWPSLKDDINNAGGHWVDQEVAVDGKLVSS
RKPEDIPAFNRRFIEILAG
;
_entity_poly.pdbx_strand_id                 B,X 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   GLN n 
1 4   SER n 
1 5   LEU n 
1 6   HIS n 
1 7   GLY n 
1 8   LYS n 
1 9   VAL n 
1 10  VAL n 
1 11  ALA n 
1 12  ALA n 
1 13  LEU n 
1 14  VAL n 
1 15  THR n 
1 16  ASP n 
1 17  GLY n 
1 18  PHE n 
1 19  GLU n 
1 20  GLN n 
1 21  VAL n 
1 22  GLU n 
1 23  LEU n 
1 24  THR n 
1 25  GLY n 
1 26  PRO n 
1 27  LYS n 
1 28  LYS n 
1 29  ALA n 
1 30  LEU n 
1 31  GLU n 
1 32  ASP n 
1 33  ALA n 
1 34  GLY n 
1 35  ALA n 
1 36  THR n 
1 37  VAL n 
1 38  ARG n 
1 39  ILE n 
1 40  LEU n 
1 41  SER n 
1 42  ASP n 
1 43  LYS n 
1 44  ALA n 
1 45  GLY n 
1 46  GLU n 
1 47  VAL n 
1 48  ARG n 
1 49  GLY n 
1 50  TRP n 
1 51  ASN n 
1 52  HIS n 
1 53  HIS n 
1 54  GLN n 
1 55  PRO n 
1 56  ALA n 
1 57  GLU n 
1 58  ALA n 
1 59  PHE n 
1 60  ARG n 
1 61  VAL n 
1 62  ASP n 
1 63  GLY n 
1 64  THR n 
1 65  PHE n 
1 66  GLU n 
1 67  ASP n 
1 68  ALA n 
1 69  SER n 
1 70  LEU n 
1 71  ASP n 
1 72  ASP n 
1 73  TYR n 
1 74  ASP n 
1 75  ALA n 
1 76  LEU n 
1 77  LEU n 
1 78  LEU n 
1 79  PRO n 
1 80  GLY n 
1 81  GLY n 
1 82  VAL n 
1 83  ILE n 
1 84  ASN n 
1 85  SER n 
1 86  ASP n 
1 87  GLN n 
1 88  ILE n 
1 89  ARG n 
1 90  SER n 
1 91  LEU n 
1 92  ALA n 
1 93  LYS n 
1 94  ALA n 
1 95  GLN n 
1 96  GLU n 
1 97  LEU n 
1 98  ALA n 
1 99  ILE n 
1 100 ARG n 
1 101 ALA n 
1 102 GLU n 
1 103 GLN n 
1 104 ALA n 
1 105 SER n 
1 106 LYS n 
1 107 PRO n 
1 108 VAL n 
1 109 ALA n 
1 110 VAL n 
1 111 ILE n 
1 112 CYS n 
1 113 HIS n 
1 114 GLY n 
1 115 ALA n 
1 116 TRP n 
1 117 LEU n 
1 118 LEU n 
1 119 ILE n 
1 120 SER n 
1 121 ALA n 
1 122 GLY n 
1 123 LEU n 
1 124 VAL n 
1 125 GLN n 
1 126 GLY n 
1 127 ARG n 
1 128 THR n 
1 129 LEU n 
1 130 THR n 
1 131 SER n 
1 132 TRP n 
1 133 PRO n 
1 134 SER n 
1 135 LEU n 
1 136 LYS n 
1 137 ASP n 
1 138 ASP n 
1 139 ILE n 
1 140 ASN n 
1 141 ASN n 
1 142 ALA n 
1 143 GLY n 
1 144 GLY n 
1 145 HIS n 
1 146 TRP n 
1 147 VAL n 
1 148 ASP n 
1 149 GLN n 
1 150 GLU n 
1 151 VAL n 
1 152 ALA n 
1 153 VAL n 
1 154 ASP n 
1 155 GLY n 
1 156 LYS n 
1 157 LEU n 
1 158 VAL n 
1 159 SER n 
1 160 SER n 
1 161 ARG n 
1 162 LYS n 
1 163 PRO n 
1 164 GLU n 
1 165 ASP n 
1 166 ILE n 
1 167 PRO n 
1 168 ALA n 
1 169 PHE n 
1 170 ASN n 
1 171 ARG n 
1 172 ARG n 
1 173 PHE n 
1 174 ILE n 
1 175 GLU n 
1 176 ILE n 
1 177 LEU n 
1 178 ALA n 
1 179 GLY 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                   179 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 pfpI 
_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      'Pseudomonas aeruginosa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     287 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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   MET 1   1   ?   ?   ?   B . n 
A 1 2   THR 2   2   2   THR THR B . n 
A 1 3   GLN 3   3   3   GLN GLN B . n 
A 1 4   SER 4   4   4   SER SER B . n 
A 1 5   LEU 5   5   5   LEU LEU B . n 
A 1 6   HIS 6   6   6   HIS HIS B . n 
A 1 7   GLY 7   7   7   GLY GLY B . n 
A 1 8   LYS 8   8   8   LYS LYS B . n 
A 1 9   VAL 9   9   9   VAL VAL B . n 
A 1 10  VAL 10  10  10  VAL VAL B . n 
A 1 11  ALA 11  11  11  ALA ALA B . n 
A 1 12  ALA 12  12  12  ALA ALA B . n 
A 1 13  LEU 13  13  13  LEU LEU B . n 
A 1 14  VAL 14  14  14  VAL VAL B . n 
A 1 15  THR 15  15  15  THR THR B . n 
A 1 16  ASP 16  16  16  ASP ASP B . n 
A 1 17  GLY 17  17  17  GLY GLY B . n 
A 1 18  PHE 18  18  18  PHE PHE B . n 
A 1 19  GLU 19  19  19  GLU GLU B . n 
A 1 20  GLN 20  20  20  GLN GLN B . n 
A 1 21  VAL 21  21  21  VAL VAL B . n 
A 1 22  GLU 22  22  22  GLU GLU B . n 
A 1 23  LEU 23  23  23  LEU LEU B . n 
A 1 24  THR 24  24  24  THR THR B . n 
A 1 25  GLY 25  25  25  GLY GLY B . n 
A 1 26  PRO 26  26  26  PRO PRO B . n 
A 1 27  LYS 27  27  27  LYS LYS B . n 
A 1 28  LYS 28  28  28  LYS LYS B . n 
A 1 29  ALA 29  29  29  ALA ALA B . n 
A 1 30  LEU 30  30  30  LEU LEU B . n 
A 1 31  GLU 31  31  31  GLU GLU B . n 
A 1 32  ASP 32  32  32  ASP ASP B . n 
A 1 33  ALA 33  33  33  ALA ALA B . n 
A 1 34  GLY 34  34  34  GLY GLY B . n 
A 1 35  ALA 35  35  35  ALA ALA B . n 
A 1 36  THR 36  36  36  THR THR B . n 
A 1 37  VAL 37  37  37  VAL VAL B . n 
A 1 38  ARG 38  38  38  ARG ARG B . n 
A 1 39  ILE 39  39  39  ILE ILE B . n 
A 1 40  LEU 40  40  40  LEU LEU B . n 
A 1 41  SER 41  41  41  SER SER B . n 
A 1 42  ASP 42  42  42  ASP ASP B . n 
A 1 43  LYS 43  43  43  LYS LYS B . n 
A 1 44  ALA 44  44  44  ALA ALA B . n 
A 1 45  GLY 45  45  45  GLY GLY B . n 
A 1 46  GLU 46  46  46  GLU GLU B . n 
A 1 47  VAL 47  47  47  VAL VAL B . n 
A 1 48  ARG 48  48  48  ARG ARG B . n 
A 1 49  GLY 49  49  49  GLY GLY B . n 
A 1 50  TRP 50  50  50  TRP TRP B . n 
A 1 51  ASN 51  51  51  ASN ASN B . n 
A 1 52  HIS 52  52  52  HIS HIS B . n 
A 1 53  HIS 53  53  53  HIS HIS B . n 
A 1 54  GLN 54  54  54  GLN GLN B . n 
A 1 55  PRO 55  55  55  PRO PRO B . n 
A 1 56  ALA 56  56  56  ALA ALA B . n 
A 1 57  GLU 57  57  57  GLU GLU B . n 
A 1 58  ALA 58  58  58  ALA ALA B . n 
A 1 59  PHE 59  59  59  PHE PHE B . n 
A 1 60  ARG 60  60  60  ARG ARG B . n 
A 1 61  VAL 61  61  61  VAL VAL B . n 
A 1 62  ASP 62  62  62  ASP ASP B . n 
A 1 63  GLY 63  63  63  GLY GLY B . n 
A 1 64  THR 64  64  64  THR THR B . n 
A 1 65  PHE 65  65  65  PHE PHE B . n 
A 1 66  GLU 66  66  66  GLU GLU B . n 
A 1 67  ASP 67  67  67  ASP ASP B . n 
A 1 68  ALA 68  68  68  ALA ALA B . n 
A 1 69  SER 69  69  69  SER SER B . n 
A 1 70  LEU 70  70  70  LEU LEU B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  ASP 72  72  72  ASP ASP B . n 
A 1 73  TYR 73  73  73  TYR TYR B . n 
A 1 74  ASP 74  74  74  ASP ASP B . n 
A 1 75  ALA 75  75  75  ALA ALA B . n 
A 1 76  LEU 76  76  76  LEU LEU B . n 
A 1 77  LEU 77  77  77  LEU LEU B . n 
A 1 78  LEU 78  78  78  LEU LEU B . n 
A 1 79  PRO 79  79  79  PRO PRO B . n 
A 1 80  GLY 80  80  80  GLY GLY B . n 
A 1 81  GLY 81  81  81  GLY GLY B . n 
A 1 82  VAL 82  82  82  VAL VAL B . n 
A 1 83  ILE 83  83  83  ILE ILE B . n 
A 1 84  ASN 84  84  84  ASN ASN B . n 
A 1 85  SER 85  85  85  SER SER B . n 
A 1 86  ASP 86  86  86  ASP ASP B . n 
A 1 87  GLN 87  87  87  GLN GLN B . n 
A 1 88  ILE 88  88  88  ILE ILE B . n 
A 1 89  ARG 89  89  89  ARG ARG B . n 
A 1 90  SER 90  90  90  SER SER B . n 
A 1 91  LEU 91  91  91  LEU LEU B . n 
A 1 92  ALA 92  92  92  ALA ALA B . n 
A 1 93  LYS 93  93  93  LYS LYS B . n 
A 1 94  ALA 94  94  94  ALA ALA B . n 
A 1 95  GLN 95  95  95  GLN GLN B . n 
A 1 96  GLU 96  96  96  GLU GLU B . n 
A 1 97  LEU 97  97  97  LEU LEU B . n 
A 1 98  ALA 98  98  98  ALA ALA B . n 
A 1 99  ILE 99  99  99  ILE ILE B . n 
A 1 100 ARG 100 100 100 ARG ARG B . n 
A 1 101 ALA 101 101 101 ALA ALA B . n 
A 1 102 GLU 102 102 102 GLU GLU B . n 
A 1 103 GLN 103 103 103 GLN GLN B . n 
A 1 104 ALA 104 104 104 ALA ALA B . n 
A 1 105 SER 105 105 105 SER SER B . n 
A 1 106 LYS 106 106 106 LYS LYS B . n 
A 1 107 PRO 107 107 107 PRO PRO B . n 
A 1 108 VAL 108 108 108 VAL VAL B . n 
A 1 109 ALA 109 109 109 ALA ALA B . n 
A 1 110 VAL 110 110 110 VAL VAL B . n 
A 1 111 ILE 111 111 111 ILE ILE B . n 
A 1 112 CYS 112 112 112 CYS CYS B . n 
A 1 113 HIS 113 113 113 HIS HIS B . n 
A 1 114 GLY 114 114 114 GLY GLY B . n 
A 1 115 ALA 115 115 115 ALA ALA B . n 
A 1 116 TRP 116 116 116 TRP TRP B . n 
A 1 117 LEU 117 117 117 LEU LEU B . n 
A 1 118 LEU 118 118 118 LEU LEU B . n 
A 1 119 ILE 119 119 119 ILE ILE B . n 
A 1 120 SER 120 120 120 SER SER B . n 
A 1 121 ALA 121 121 121 ALA ALA B . n 
A 1 122 GLY 122 122 122 GLY GLY B . n 
A 1 123 LEU 123 123 123 LEU LEU B . n 
A 1 124 VAL 124 124 124 VAL VAL B . n 
A 1 125 GLN 125 125 125 GLN GLN B . n 
A 1 126 GLY 126 126 126 GLY GLY B . n 
A 1 127 ARG 127 127 127 ARG ARG B . n 
A 1 128 THR 128 128 128 THR THR B . n 
A 1 129 LEU 129 129 129 LEU LEU B . n 
A 1 130 THR 130 130 130 THR THR B . n 
A 1 131 SER 131 131 131 SER SER B . n 
A 1 132 TRP 132 132 132 TRP TRP B . n 
A 1 133 PRO 133 133 133 PRO PRO B . n 
A 1 134 SER 134 134 134 SER SER B . n 
A 1 135 LEU 135 135 135 LEU LEU B . n 
A 1 136 LYS 136 136 136 LYS LYS B . n 
A 1 137 ASP 137 137 137 ASP ASP B . n 
A 1 138 ASP 138 138 138 ASP ASP B . n 
A 1 139 ILE 139 139 139 ILE ILE B . n 
A 1 140 ASN 140 140 140 ASN ASN B . n 
A 1 141 ASN 141 141 141 ASN ASN B . n 
A 1 142 ALA 142 142 142 ALA ALA B . n 
A 1 143 GLY 143 143 143 GLY GLY B . n 
A 1 144 GLY 144 144 144 GLY GLY B . n 
A 1 145 HIS 145 145 145 HIS HIS B . n 
A 1 146 TRP 146 146 146 TRP TRP B . n 
A 1 147 VAL 147 147 147 VAL VAL B . n 
A 1 148 ASP 148 148 148 ASP ASP B . n 
A 1 149 GLN 149 149 149 GLN GLN B . n 
A 1 150 GLU 150 150 150 GLU GLU B . n 
A 1 151 VAL 151 151 151 VAL VAL B . n 
A 1 152 ALA 152 152 152 ALA ALA B . n 
A 1 153 VAL 153 153 153 VAL VAL B . n 
A 1 154 ASP 154 154 154 ASP ASP B . n 
A 1 155 GLY 155 155 155 GLY GLY B . n 
A 1 156 LYS 156 156 156 LYS LYS B . n 
A 1 157 LEU 157 157 157 LEU LEU B . n 
A 1 158 VAL 158 158 158 VAL VAL B . n 
A 1 159 SER 159 159 159 SER SER B . n 
A 1 160 SER 160 160 160 SER SER B . n 
A 1 161 ARG 161 161 161 ARG ARG B . n 
A 1 162 LYS 162 162 162 LYS LYS B . n 
A 1 163 PRO 163 163 163 PRO PRO B . n 
A 1 164 GLU 164 164 164 GLU GLU B . n 
A 1 165 ASP 165 165 165 ASP ASP B . n 
A 1 166 ILE 166 166 166 ILE ILE B . n 
A 1 167 PRO 167 167 167 PRO PRO B . n 
A 1 168 ALA 168 168 168 ALA ALA B . n 
A 1 169 PHE 169 169 169 PHE PHE B . n 
A 1 170 ASN 170 170 170 ASN ASN B . n 
A 1 171 ARG 171 171 171 ARG ARG B . n 
A 1 172 ARG 172 172 172 ARG ARG B . n 
A 1 173 PHE 173 173 173 PHE PHE B . n 
A 1 174 ILE 174 174 174 ILE ILE B . n 
A 1 175 GLU 175 175 175 GLU GLU B . n 
A 1 176 ILE 176 176 176 ILE ILE B . n 
A 1 177 LEU 177 177 177 LEU LEU B . n 
A 1 178 ALA 178 178 178 ALA ALA B . n 
A 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 1   MET 1   1   ?   ?   ?   X . n 
B 1 2   THR 2   2   2   THR THR X . n 
B 1 3   GLN 3   3   3   GLN GLN X . n 
B 1 4   SER 4   4   4   SER SER X . n 
B 1 5   LEU 5   5   5   LEU LEU X . n 
B 1 6   HIS 6   6   6   HIS HIS X . n 
B 1 7   GLY 7   7   7   GLY GLY X . n 
B 1 8   LYS 8   8   8   LYS LYS X . n 
B 1 9   VAL 9   9   9   VAL VAL X . n 
B 1 10  VAL 10  10  10  VAL VAL X . n 
B 1 11  ALA 11  11  11  ALA ALA X . n 
B 1 12  ALA 12  12  12  ALA ALA X . n 
B 1 13  LEU 13  13  13  LEU LEU X . n 
B 1 14  VAL 14  14  14  VAL VAL X . n 
B 1 15  THR 15  15  15  THR THR X . n 
B 1 16  ASP 16  16  16  ASP ASP X . n 
B 1 17  GLY 17  17  17  GLY GLY X . n 
B 1 18  PHE 18  18  18  PHE PHE X . n 
B 1 19  GLU 19  19  19  GLU GLU X . n 
B 1 20  GLN 20  20  20  GLN GLN X . n 
B 1 21  VAL 21  21  21  VAL VAL X . n 
B 1 22  GLU 22  22  22  GLU GLU X . n 
B 1 23  LEU 23  23  23  LEU LEU X . n 
B 1 24  THR 24  24  24  THR THR X . n 
B 1 25  GLY 25  25  25  GLY GLY X . n 
B 1 26  PRO 26  26  26  PRO PRO X . n 
B 1 27  LYS 27  27  27  LYS LYS X . n 
B 1 28  LYS 28  28  28  LYS LYS X . n 
B 1 29  ALA 29  29  29  ALA ALA X . n 
B 1 30  LEU 30  30  30  LEU LEU X . n 
B 1 31  GLU 31  31  31  GLU GLU X . n 
B 1 32  ASP 32  32  32  ASP ASP X . n 
B 1 33  ALA 33  33  33  ALA ALA X . n 
B 1 34  GLY 34  34  34  GLY GLY X . n 
B 1 35  ALA 35  35  35  ALA ALA X . n 
B 1 36  THR 36  36  36  THR THR X . n 
B 1 37  VAL 37  37  37  VAL VAL X . n 
B 1 38  ARG 38  38  38  ARG ARG X . n 
B 1 39  ILE 39  39  39  ILE ILE X . n 
B 1 40  LEU 40  40  40  LEU LEU X . n 
B 1 41  SER 41  41  41  SER SER X . n 
B 1 42  ASP 42  42  42  ASP ASP X . n 
B 1 43  LYS 43  43  43  LYS LYS X . n 
B 1 44  ALA 44  44  44  ALA ALA X . n 
B 1 45  GLY 45  45  45  GLY GLY X . n 
B 1 46  GLU 46  46  46  GLU GLU X . n 
B 1 47  VAL 47  47  47  VAL VAL X . n 
B 1 48  ARG 48  48  48  ARG ARG X . n 
B 1 49  GLY 49  49  49  GLY GLY X . n 
B 1 50  TRP 50  50  50  TRP TRP X . n 
B 1 51  ASN 51  51  51  ASN ASN X . n 
B 1 52  HIS 52  52  52  HIS HIS X . n 
B 1 53  HIS 53  53  53  HIS HIS X . n 
B 1 54  GLN 54  54  54  GLN GLN X . n 
B 1 55  PRO 55  55  55  PRO PRO X . n 
B 1 56  ALA 56  56  56  ALA ALA X . n 
B 1 57  GLU 57  57  57  GLU GLU X . n 
B 1 58  ALA 58  58  58  ALA ALA X . n 
B 1 59  PHE 59  59  59  PHE PHE X . n 
B 1 60  ARG 60  60  60  ARG ARG X . n 
B 1 61  VAL 61  61  61  VAL VAL X . n 
B 1 62  ASP 62  62  62  ASP ASP X . n 
B 1 63  GLY 63  63  63  GLY GLY X . n 
B 1 64  THR 64  64  64  THR THR X . n 
B 1 65  PHE 65  65  65  PHE PHE X . n 
B 1 66  GLU 66  66  66  GLU GLU X . n 
B 1 67  ASP 67  67  67  ASP ASP X . n 
B 1 68  ALA 68  68  68  ALA ALA X . n 
B 1 69  SER 69  69  69  SER SER X . n 
B 1 70  LEU 70  70  70  LEU LEU X . n 
B 1 71  ASP 71  71  71  ASP ASP X . n 
B 1 72  ASP 72  72  72  ASP ASP X . n 
B 1 73  TYR 73  73  73  TYR TYR X . n 
B 1 74  ASP 74  74  74  ASP ASP X . n 
B 1 75  ALA 75  75  75  ALA ALA X . n 
B 1 76  LEU 76  76  76  LEU LEU X . n 
B 1 77  LEU 77  77  77  LEU LEU X . n 
B 1 78  LEU 78  78  78  LEU LEU X . n 
B 1 79  PRO 79  79  79  PRO PRO X . n 
B 1 80  GLY 80  80  80  GLY GLY X . n 
B 1 81  GLY 81  81  81  GLY GLY X . n 
B 1 82  VAL 82  82  82  VAL VAL X . n 
B 1 83  ILE 83  83  83  ILE ILE X . n 
B 1 84  ASN 84  84  84  ASN ASN X . n 
B 1 85  SER 85  85  85  SER SER X . n 
B 1 86  ASP 86  86  86  ASP ASP X . n 
B 1 87  GLN 87  87  87  GLN GLN X . n 
B 1 88  ILE 88  88  88  ILE ILE X . n 
B 1 89  ARG 89  89  89  ARG ARG X . n 
B 1 90  SER 90  90  90  SER SER X . n 
B 1 91  LEU 91  91  91  LEU LEU X . n 
B 1 92  ALA 92  92  92  ALA ALA X . n 
B 1 93  LYS 93  93  93  LYS LYS X . n 
B 1 94  ALA 94  94  94  ALA ALA X . n 
B 1 95  GLN 95  95  95  GLN GLN X . n 
B 1 96  GLU 96  96  96  GLU GLU X . n 
B 1 97  LEU 97  97  97  LEU LEU X . n 
B 1 98  ALA 98  98  98  ALA ALA X . n 
B 1 99  ILE 99  99  99  ILE ILE X . n 
B 1 100 ARG 100 100 100 ARG ARG X . n 
B 1 101 ALA 101 101 101 ALA ALA X . n 
B 1 102 GLU 102 102 102 GLU GLU X . n 
B 1 103 GLN 103 103 103 GLN GLN X . n 
B 1 104 ALA 104 104 104 ALA ALA X . n 
B 1 105 SER 105 105 105 SER SER X . n 
B 1 106 LYS 106 106 106 LYS LYS X . n 
B 1 107 PRO 107 107 107 PRO PRO X . n 
B 1 108 VAL 108 108 108 VAL VAL X . n 
B 1 109 ALA 109 109 109 ALA ALA X . n 
B 1 110 VAL 110 110 110 VAL VAL X . n 
B 1 111 ILE 111 111 111 ILE ILE X . n 
B 1 112 CYS 112 112 112 CYS CYS X . n 
B 1 113 HIS 113 113 113 HIS HIS X . n 
B 1 114 GLY 114 114 114 GLY GLY X . n 
B 1 115 ALA 115 115 115 ALA ALA X . n 
B 1 116 TRP 116 116 116 TRP TRP X . n 
B 1 117 LEU 117 117 117 LEU LEU X . n 
B 1 118 LEU 118 118 118 LEU LEU X . n 
B 1 119 ILE 119 119 119 ILE ILE X . n 
B 1 120 SER 120 120 120 SER SER X . n 
B 1 121 ALA 121 121 121 ALA ALA X . n 
B 1 122 GLY 122 122 122 GLY GLY X . n 
B 1 123 LEU 123 123 123 LEU LEU X . n 
B 1 124 VAL 124 124 124 VAL VAL X . n 
B 1 125 GLN 125 125 125 GLN GLN X . n 
B 1 126 GLY 126 126 126 GLY GLY X . n 
B 1 127 ARG 127 127 127 ARG ARG X . n 
B 1 128 THR 128 128 128 THR THR X . n 
B 1 129 LEU 129 129 129 LEU LEU X . n 
B 1 130 THR 130 130 130 THR THR X . n 
B 1 131 SER 131 131 131 SER SER X . n 
B 1 132 TRP 132 132 132 TRP TRP X . n 
B 1 133 PRO 133 133 133 PRO PRO X . n 
B 1 134 SER 134 134 134 SER SER X . n 
B 1 135 LEU 135 135 135 LEU LEU X . n 
B 1 136 LYS 136 136 136 LYS LYS X . n 
B 1 137 ASP 137 137 137 ASP ASP X . n 
B 1 138 ASP 138 138 138 ASP ASP X . n 
B 1 139 ILE 139 139 139 ILE ILE X . n 
B 1 140 ASN 140 140 140 ASN ASN X . n 
B 1 141 ASN 141 141 141 ASN ASN X . n 
B 1 142 ALA 142 142 142 ALA ALA X . n 
B 1 143 GLY 143 143 143 GLY GLY X . n 
B 1 144 GLY 144 144 144 GLY GLY X . n 
B 1 145 HIS 145 145 145 HIS HIS X . n 
B 1 146 TRP 146 146 146 TRP TRP X . n 
B 1 147 VAL 147 147 147 VAL VAL X . n 
B 1 148 ASP 148 148 148 ASP ASP X . n 
B 1 149 GLN 149 149 149 GLN GLN X . n 
B 1 150 GLU 150 150 150 GLU GLU X . n 
B 1 151 VAL 151 151 151 VAL VAL X . n 
B 1 152 ALA 152 152 152 ALA ALA X . n 
B 1 153 VAL 153 153 153 VAL VAL X . n 
B 1 154 ASP 154 154 154 ASP ASP X . n 
B 1 155 GLY 155 155 155 GLY GLY X . n 
B 1 156 LYS 156 156 156 LYS LYS X . n 
B 1 157 LEU 157 157 157 LEU LEU X . n 
B 1 158 VAL 158 158 158 VAL VAL X . n 
B 1 159 SER 159 159 159 SER SER X . n 
B 1 160 SER 160 160 160 SER SER X . n 
B 1 161 ARG 161 161 161 ARG ARG X . n 
B 1 162 LYS 162 162 162 LYS LYS X . n 
B 1 163 PRO 163 163 163 PRO PRO X . n 
B 1 164 GLU 164 164 164 GLU GLU X . n 
B 1 165 ASP 165 165 165 ASP ASP X . n 
B 1 166 ILE 166 166 166 ILE ILE X . n 
B 1 167 PRO 167 167 167 PRO PRO X . n 
B 1 168 ALA 168 168 168 ALA ALA X . n 
B 1 169 PHE 169 169 169 PHE PHE X . n 
B 1 170 ASN 170 170 170 ASN ASN X . n 
B 1 171 ARG 171 171 171 ARG ARG X . n 
B 1 172 ARG 172 172 172 ARG ARG X . n 
B 1 173 PHE 173 173 173 PHE PHE X . n 
B 1 174 ILE 174 174 174 ILE ILE X . n 
B 1 175 GLU 175 175 175 GLU GLU X . n 
B 1 176 ILE 176 176 176 ILE ILE X . n 
B 1 177 LEU 177 177 177 LEU LEU X . n 
B 1 178 ALA 178 178 178 ALA ALA X . n 
B 1 179 GLY 179 179 179 GLY GLY X . 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 
C 2 HOH 1   201 170 HOH HOH B . 
C 2 HOH 2   202 331 HOH HOH B . 
C 2 HOH 3   203 227 HOH HOH B . 
C 2 HOH 4   204 125 HOH HOH B . 
C 2 HOH 5   205 239 HOH HOH B . 
C 2 HOH 6   206 185 HOH HOH B . 
C 2 HOH 7   207 55  HOH HOH B . 
C 2 HOH 8   208 299 HOH HOH B . 
C 2 HOH 9   209 279 HOH HOH B . 
C 2 HOH 10  210 60  HOH HOH B . 
C 2 HOH 11  211 195 HOH HOH B . 
C 2 HOH 12  212 206 HOH HOH B . 
C 2 HOH 13  213 147 HOH HOH B . 
C 2 HOH 14  214 272 HOH HOH B . 
C 2 HOH 15  215 329 HOH HOH B . 
C 2 HOH 16  216 106 HOH HOH B . 
C 2 HOH 17  217 75  HOH HOH B . 
C 2 HOH 18  218 67  HOH HOH B . 
C 2 HOH 19  219 197 HOH HOH B . 
C 2 HOH 20  220 70  HOH HOH B . 
C 2 HOH 21  221 186 HOH HOH B . 
C 2 HOH 22  222 213 HOH HOH B . 
C 2 HOH 23  223 81  HOH HOH B . 
C 2 HOH 24  224 257 HOH HOH B . 
C 2 HOH 25  225 56  HOH HOH B . 
C 2 HOH 26  226 145 HOH HOH B . 
C 2 HOH 27  227 92  HOH HOH B . 
C 2 HOH 28  228 360 HOH HOH B . 
C 2 HOH 29  229 201 HOH HOH B . 
C 2 HOH 30  230 8   HOH HOH B . 
C 2 HOH 31  231 240 HOH HOH B . 
C 2 HOH 32  232 160 HOH HOH B . 
C 2 HOH 33  233 46  HOH HOH B . 
C 2 HOH 34  234 133 HOH HOH B . 
C 2 HOH 35  235 276 HOH HOH B . 
C 2 HOH 36  236 273 HOH HOH B . 
C 2 HOH 37  237 307 HOH HOH B . 
C 2 HOH 38  238 218 HOH HOH B . 
C 2 HOH 39  239 83  HOH HOH B . 
C 2 HOH 40  240 14  HOH HOH B . 
C 2 HOH 41  241 15  HOH HOH B . 
C 2 HOH 42  242 153 HOH HOH B . 
C 2 HOH 43  243 243 HOH HOH B . 
C 2 HOH 44  244 100 HOH HOH B . 
C 2 HOH 45  245 89  HOH HOH B . 
C 2 HOH 46  246 12  HOH HOH B . 
C 2 HOH 47  247 135 HOH HOH B . 
C 2 HOH 48  248 50  HOH HOH B . 
C 2 HOH 49  249 117 HOH HOH B . 
C 2 HOH 50  250 262 HOH HOH B . 
C 2 HOH 51  251 164 HOH HOH B . 
C 2 HOH 52  252 301 HOH HOH B . 
C 2 HOH 53  253 253 HOH HOH B . 
C 2 HOH 54  254 16  HOH HOH B . 
C 2 HOH 55  255 132 HOH HOH B . 
C 2 HOH 56  256 263 HOH HOH B . 
C 2 HOH 57  257 110 HOH HOH B . 
C 2 HOH 58  258 342 HOH HOH B . 
C 2 HOH 59  259 293 HOH HOH B . 
C 2 HOH 60  260 246 HOH HOH B . 
C 2 HOH 61  261 286 HOH HOH B . 
C 2 HOH 62  262 193 HOH HOH B . 
C 2 HOH 63  263 178 HOH HOH B . 
C 2 HOH 64  264 34  HOH HOH B . 
C 2 HOH 65  265 5   HOH HOH B . 
C 2 HOH 66  266 173 HOH HOH B . 
C 2 HOH 67  267 118 HOH HOH B . 
C 2 HOH 68  268 53  HOH HOH B . 
C 2 HOH 69  269 107 HOH HOH B . 
C 2 HOH 70  270 24  HOH HOH B . 
C 2 HOH 71  271 217 HOH HOH B . 
C 2 HOH 72  272 10  HOH HOH B . 
C 2 HOH 73  273 113 HOH HOH B . 
C 2 HOH 74  274 166 HOH HOH B . 
C 2 HOH 75  275 292 HOH HOH B . 
C 2 HOH 76  276 319 HOH HOH B . 
C 2 HOH 77  277 345 HOH HOH B . 
C 2 HOH 78  278 248 HOH HOH B . 
C 2 HOH 79  279 174 HOH HOH B . 
C 2 HOH 80  280 290 HOH HOH B . 
C 2 HOH 81  281 137 HOH HOH B . 
C 2 HOH 82  282 325 HOH HOH B . 
C 2 HOH 83  283 2   HOH HOH B . 
C 2 HOH 84  284 58  HOH HOH B . 
C 2 HOH 85  285 126 HOH HOH B . 
C 2 HOH 86  286 3   HOH HOH B . 
C 2 HOH 87  287 346 HOH HOH B . 
C 2 HOH 88  288 198 HOH HOH B . 
C 2 HOH 89  289 22  HOH HOH B . 
C 2 HOH 90  290 155 HOH HOH B . 
C 2 HOH 91  291 33  HOH HOH B . 
C 2 HOH 92  292 189 HOH HOH B . 
C 2 HOH 93  293 93  HOH HOH B . 
C 2 HOH 94  294 368 HOH HOH B . 
C 2 HOH 95  295 32  HOH HOH B . 
C 2 HOH 96  296 25  HOH HOH B . 
C 2 HOH 97  297 356 HOH HOH B . 
C 2 HOH 98  298 150 HOH HOH B . 
C 2 HOH 99  299 306 HOH HOH B . 
C 2 HOH 100 300 27  HOH HOH B . 
C 2 HOH 101 301 28  HOH HOH B . 
C 2 HOH 102 302 13  HOH HOH B . 
C 2 HOH 103 303 68  HOH HOH B . 
C 2 HOH 104 304 140 HOH HOH B . 
C 2 HOH 105 305 9   HOH HOH B . 
C 2 HOH 106 306 131 HOH HOH B . 
C 2 HOH 107 307 80  HOH HOH B . 
C 2 HOH 108 308 215 HOH HOH B . 
C 2 HOH 109 309 242 HOH HOH B . 
C 2 HOH 110 310 303 HOH HOH B . 
C 2 HOH 111 311 268 HOH HOH B . 
C 2 HOH 112 312 291 HOH HOH B . 
C 2 HOH 113 313 171 HOH HOH B . 
C 2 HOH 114 314 162 HOH HOH B . 
C 2 HOH 115 315 57  HOH HOH B . 
C 2 HOH 116 316 274 HOH HOH B . 
C 2 HOH 117 317 258 HOH HOH B . 
C 2 HOH 118 318 247 HOH HOH B . 
C 2 HOH 119 319 211 HOH HOH B . 
C 2 HOH 120 320 339 HOH HOH B . 
C 2 HOH 121 321 97  HOH HOH B . 
C 2 HOH 122 322 19  HOH HOH B . 
C 2 HOH 123 323 82  HOH HOH B . 
C 2 HOH 124 324 119 HOH HOH B . 
C 2 HOH 125 325 148 HOH HOH B . 
C 2 HOH 126 326 267 HOH HOH B . 
C 2 HOH 127 327 311 HOH HOH B . 
C 2 HOH 128 328 158 HOH HOH B . 
C 2 HOH 129 329 281 HOH HOH B . 
C 2 HOH 130 330 36  HOH HOH B . 
C 2 HOH 131 331 351 HOH HOH B . 
C 2 HOH 132 332 236 HOH HOH B . 
C 2 HOH 133 333 31  HOH HOH B . 
C 2 HOH 134 334 169 HOH HOH B . 
C 2 HOH 135 335 309 HOH HOH B . 
C 2 HOH 136 336 111 HOH HOH B . 
C 2 HOH 137 337 179 HOH HOH B . 
C 2 HOH 138 338 144 HOH HOH B . 
C 2 HOH 139 339 312 HOH HOH B . 
C 2 HOH 140 340 264 HOH HOH B . 
C 2 HOH 141 341 199 HOH HOH B . 
C 2 HOH 142 342 271 HOH HOH B . 
C 2 HOH 143 343 40  HOH HOH B . 
C 2 HOH 144 344 130 HOH HOH B . 
C 2 HOH 145 345 302 HOH HOH B . 
C 2 HOH 146 346 208 HOH HOH B . 
C 2 HOH 147 347 225 HOH HOH B . 
C 2 HOH 148 348 295 HOH HOH B . 
C 2 HOH 149 349 328 HOH HOH B . 
C 2 HOH 150 350 296 HOH HOH B . 
C 2 HOH 151 351 114 HOH HOH B . 
C 2 HOH 152 352 265 HOH HOH B . 
C 2 HOH 153 353 154 HOH HOH B . 
C 2 HOH 154 354 156 HOH HOH B . 
C 2 HOH 155 355 298 HOH HOH B . 
C 2 HOH 156 356 308 HOH HOH B . 
C 2 HOH 157 357 244 HOH HOH B . 
C 2 HOH 158 358 332 HOH HOH B . 
C 2 HOH 159 359 94  HOH HOH B . 
C 2 HOH 160 360 254 HOH HOH B . 
C 2 HOH 161 361 283 HOH HOH B . 
C 2 HOH 162 362 112 HOH HOH B . 
C 2 HOH 163 363 287 HOH HOH B . 
C 2 HOH 164 364 226 HOH HOH B . 
C 2 HOH 165 365 101 HOH HOH B . 
C 2 HOH 166 366 152 HOH HOH B . 
C 2 HOH 167 367 207 HOH HOH B . 
C 2 HOH 168 368 192 HOH HOH B . 
C 2 HOH 169 369 289 HOH HOH B . 
C 2 HOH 170 370 182 HOH HOH B . 
C 2 HOH 171 371 86  HOH HOH B . 
C 2 HOH 172 372 205 HOH HOH B . 
C 2 HOH 173 373 95  HOH HOH B . 
C 2 HOH 174 374 128 HOH HOH B . 
C 2 HOH 175 375 116 HOH HOH B . 
C 2 HOH 176 376 96  HOH HOH B . 
C 2 HOH 177 377 115 HOH HOH B . 
C 2 HOH 178 378 249 HOH HOH B . 
C 2 HOH 179 379 241 HOH HOH B . 
C 2 HOH 180 380 255 HOH HOH B . 
C 2 HOH 181 381 277 HOH HOH B . 
D 2 HOH 1   201 29  HOH HOH X . 
D 2 HOH 2   202 54  HOH HOH X . 
D 2 HOH 3   203 159 HOH HOH X . 
D 2 HOH 4   204 69  HOH HOH X . 
D 2 HOH 5   205 79  HOH HOH X . 
D 2 HOH 6   206 143 HOH HOH X . 
D 2 HOH 7   207 23  HOH HOH X . 
D 2 HOH 8   208 71  HOH HOH X . 
D 2 HOH 9   209 142 HOH HOH X . 
D 2 HOH 10  210 260 HOH HOH X . 
D 2 HOH 11  211 61  HOH HOH X . 
D 2 HOH 12  212 314 HOH HOH X . 
D 2 HOH 13  213 90  HOH HOH X . 
D 2 HOH 14  214 47  HOH HOH X . 
D 2 HOH 15  215 129 HOH HOH X . 
D 2 HOH 16  216 352 HOH HOH X . 
D 2 HOH 17  217 183 HOH HOH X . 
D 2 HOH 18  218 190 HOH HOH X . 
D 2 HOH 19  219 26  HOH HOH X . 
D 2 HOH 20  220 202 HOH HOH X . 
D 2 HOH 21  221 136 HOH HOH X . 
D 2 HOH 22  222 316 HOH HOH X . 
D 2 HOH 23  223 270 HOH HOH X . 
D 2 HOH 24  224 6   HOH HOH X . 
D 2 HOH 25  225 49  HOH HOH X . 
D 2 HOH 26  226 165 HOH HOH X . 
D 2 HOH 27  227 64  HOH HOH X . 
D 2 HOH 28  228 188 HOH HOH X . 
D 2 HOH 29  229 297 HOH HOH X . 
D 2 HOH 30  230 35  HOH HOH X . 
D 2 HOH 31  231 20  HOH HOH X . 
D 2 HOH 32  232 7   HOH HOH X . 
D 2 HOH 33  233 11  HOH HOH X . 
D 2 HOH 34  234 124 HOH HOH X . 
D 2 HOH 35  235 59  HOH HOH X . 
D 2 HOH 36  236 87  HOH HOH X . 
D 2 HOH 37  237 175 HOH HOH X . 
D 2 HOH 38  238 39  HOH HOH X . 
D 2 HOH 39  239 78  HOH HOH X . 
D 2 HOH 40  240 337 HOH HOH X . 
D 2 HOH 41  241 138 HOH HOH X . 
D 2 HOH 42  242 66  HOH HOH X . 
D 2 HOH 43  243 52  HOH HOH X . 
D 2 HOH 44  244 347 HOH HOH X . 
D 2 HOH 45  245 76  HOH HOH X . 
D 2 HOH 46  246 51  HOH HOH X . 
D 2 HOH 47  247 184 HOH HOH X . 
D 2 HOH 48  248 98  HOH HOH X . 
D 2 HOH 49  249 44  HOH HOH X . 
D 2 HOH 50  250 99  HOH HOH X . 
D 2 HOH 51  251 259 HOH HOH X . 
D 2 HOH 52  252 280 HOH HOH X . 
D 2 HOH 53  253 355 HOH HOH X . 
D 2 HOH 54  254 187 HOH HOH X . 
D 2 HOH 55  255 43  HOH HOH X . 
D 2 HOH 56  256 88  HOH HOH X . 
D 2 HOH 57  257 335 HOH HOH X . 
D 2 HOH 58  258 1   HOH HOH X . 
D 2 HOH 59  259 42  HOH HOH X . 
D 2 HOH 60  260 45  HOH HOH X . 
D 2 HOH 61  261 72  HOH HOH X . 
D 2 HOH 62  262 200 HOH HOH X . 
D 2 HOH 63  263 122 HOH HOH X . 
D 2 HOH 64  264 85  HOH HOH X . 
D 2 HOH 65  265 62  HOH HOH X . 
D 2 HOH 66  266 4   HOH HOH X . 
D 2 HOH 67  267 209 HOH HOH X . 
D 2 HOH 68  268 326 HOH HOH X . 
D 2 HOH 69  269 91  HOH HOH X . 
D 2 HOH 70  270 30  HOH HOH X . 
D 2 HOH 71  271 233 HOH HOH X . 
D 2 HOH 72  272 181 HOH HOH X . 
D 2 HOH 73  273 134 HOH HOH X . 
D 2 HOH 74  274 220 HOH HOH X . 
D 2 HOH 75  275 151 HOH HOH X . 
D 2 HOH 76  276 176 HOH HOH X . 
D 2 HOH 77  277 141 HOH HOH X . 
D 2 HOH 78  278 21  HOH HOH X . 
D 2 HOH 79  279 18  HOH HOH X . 
D 2 HOH 80  280 65  HOH HOH X . 
D 2 HOH 81  281 37  HOH HOH X . 
D 2 HOH 82  282 108 HOH HOH X . 
D 2 HOH 83  283 38  HOH HOH X . 
D 2 HOH 84  284 121 HOH HOH X . 
D 2 HOH 85  285 103 HOH HOH X . 
D 2 HOH 86  286 256 HOH HOH X . 
D 2 HOH 87  287 191 HOH HOH X . 
D 2 HOH 88  288 177 HOH HOH X . 
D 2 HOH 89  289 63  HOH HOH X . 
D 2 HOH 90  290 74  HOH HOH X . 
D 2 HOH 91  291 245 HOH HOH X . 
D 2 HOH 92  292 17  HOH HOH X . 
D 2 HOH 93  293 330 HOH HOH X . 
D 2 HOH 94  294 77  HOH HOH X . 
D 2 HOH 95  295 204 HOH HOH X . 
D 2 HOH 96  296 105 HOH HOH X . 
D 2 HOH 97  297 84  HOH HOH X . 
D 2 HOH 98  298 210 HOH HOH X . 
D 2 HOH 99  299 109 HOH HOH X . 
D 2 HOH 100 300 120 HOH HOH X . 
D 2 HOH 101 301 172 HOH HOH X . 
D 2 HOH 102 302 203 HOH HOH X . 
D 2 HOH 103 303 238 HOH HOH X . 
D 2 HOH 104 304 224 HOH HOH X . 
D 2 HOH 105 305 149 HOH HOH X . 
D 2 HOH 106 306 321 HOH HOH X . 
D 2 HOH 107 307 41  HOH HOH X . 
D 2 HOH 108 308 284 HOH HOH X . 
D 2 HOH 109 309 285 HOH HOH X . 
D 2 HOH 110 310 282 HOH HOH X . 
D 2 HOH 111 311 324 HOH HOH X . 
D 2 HOH 112 312 196 HOH HOH X . 
D 2 HOH 113 313 102 HOH HOH X . 
D 2 HOH 114 314 157 HOH HOH X . 
D 2 HOH 115 315 104 HOH HOH X . 
D 2 HOH 116 316 237 HOH HOH X . 
D 2 HOH 117 317 146 HOH HOH X . 
D 2 HOH 118 318 139 HOH HOH X . 
D 2 HOH 119 319 366 HOH HOH X . 
D 2 HOH 120 320 167 HOH HOH X . 
D 2 HOH 121 321 353 HOH HOH X . 
D 2 HOH 122 322 234 HOH HOH X . 
D 2 HOH 123 323 222 HOH HOH X . 
D 2 HOH 124 324 315 HOH HOH X . 
D 2 HOH 125 325 251 HOH HOH X . 
D 2 HOH 126 326 48  HOH HOH X . 
D 2 HOH 127 327 323 HOH HOH X . 
D 2 HOH 128 328 288 HOH HOH X . 
D 2 HOH 129 329 194 HOH HOH X . 
D 2 HOH 130 330 362 HOH HOH X . 
D 2 HOH 131 331 322 HOH HOH X . 
D 2 HOH 132 332 334 HOH HOH X . 
D 2 HOH 133 333 229 HOH HOH X . 
D 2 HOH 134 334 364 HOH HOH X . 
D 2 HOH 135 335 336 HOH HOH X . 
D 2 HOH 136 336 228 HOH HOH X . 
D 2 HOH 137 337 333 HOH HOH X . 
D 2 HOH 138 338 266 HOH HOH X . 
D 2 HOH 139 339 168 HOH HOH X . 
D 2 HOH 140 340 219 HOH HOH X . 
D 2 HOH 141 341 216 HOH HOH X . 
D 2 HOH 142 342 320 HOH HOH X . 
D 2 HOH 143 343 300 HOH HOH X . 
D 2 HOH 144 344 327 HOH HOH X . 
D 2 HOH 145 345 275 HOH HOH X . 
D 2 HOH 146 346 358 HOH HOH X . 
D 2 HOH 147 347 161 HOH HOH X . 
D 2 HOH 148 348 349 HOH HOH X . 
D 2 HOH 149 349 163 HOH HOH X . 
D 2 HOH 150 350 235 HOH HOH X . 
D 2 HOH 151 351 250 HOH HOH X . 
D 2 HOH 152 352 223 HOH HOH X . 
D 2 HOH 153 353 361 HOH HOH X . 
D 2 HOH 154 354 348 HOH HOH X . 
D 2 HOH 155 355 317 HOH HOH X . 
D 2 HOH 156 356 318 HOH HOH X . 
D 2 HOH 157 357 261 HOH HOH X . 
D 2 HOH 158 358 350 HOH HOH X . 
D 2 HOH 159 359 73  HOH HOH X . 
D 2 HOH 160 360 344 HOH HOH X . 
D 2 HOH 161 361 221 HOH HOH X . 
D 2 HOH 162 362 269 HOH HOH X . 
D 2 HOH 163 363 212 HOH HOH X . 
D 2 HOH 164 364 363 HOH HOH X . 
D 2 HOH 165 365 341 HOH HOH X . 
D 2 HOH 166 366 214 HOH HOH X . 
D 2 HOH 167 367 123 HOH HOH X . 
# 
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 B ARG 100 ? CG  ? A ARG 100 CG  
2  1 Y 1 B ARG 100 ? CD  ? A ARG 100 CD  
3  1 Y 1 B ARG 100 ? NE  ? A ARG 100 NE  
4  1 Y 1 B ARG 100 ? CZ  ? A ARG 100 CZ  
5  1 Y 1 B ARG 100 ? NH1 ? A ARG 100 NH1 
6  1 Y 1 B ARG 100 ? NH2 ? A ARG 100 NH2 
7  1 Y 1 X LYS 43  ? CG  ? B LYS 43  CG  
8  1 Y 1 X LYS 43  ? CD  ? B LYS 43  CD  
9  1 Y 1 X LYS 43  ? CE  ? B LYS 43  CE  
10 1 Y 1 X LYS 43  ? NZ  ? B LYS 43  NZ  
# 
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 reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R3N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.990 
_cell.length_a_esd                 ? 
_cell.length_b                     78.710 
_cell.length_b_esd                 ? 
_cell.length_c                     103.090 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8R3N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8R3N 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.35 
_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' 
_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    '0.2 M calcium chloride, 0.1 M Tris buffer (pH 8.5), PEG 3350, 20% (w/v)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     70 
_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 EIGER2 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         2017-12-04 
_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   0.9795 
_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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R3N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.45 
_reflns.d_resolution_low                               43.12 
_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                                     59398 
_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                           96.47 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9 
_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                                0.081 
_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                                   1 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.45 
_reflns_shell.d_res_low                                     1.502 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2343 
_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                               2.7 
_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                               ? 
_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                                  0.6 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          81.07 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8R3N 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.45 
_refine.ls_d_res_low                             43.12 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     59225 
_refine.ls_number_reflns_R_free                  2965 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.46 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2576 
_refine.ls_R_factor_R_free                       0.2818 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2563 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.68 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        43.12 
_refine_hist.number_atoms_solvent             348 
_refine_hist.number_atoms_total               3036 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2688 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? 2769 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.895 ? 3765 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 8.583 ? 383  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.079 ? 428  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 497  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.45 1.47  . . 105 2107 78.00  . . . . 0.4239 . . . . . . . . . . . 0.4239 
'X-RAY DIFFRACTION' 1.47 1.50  . . 141 2299 84.00  . . . . 0.3889 . . . . . . . . . . . 0.4901 
'X-RAY DIFFRACTION' 1.50 1.53  . . 130 2404 88.00  . . . . 0.3707 . . . . . . . . . . . 0.3816 
'X-RAY DIFFRACTION' 1.53 1.56  . . 124 2572 93.00  . . . . 0.3400 . . . . . . . . . . . 0.4182 
'X-RAY DIFFRACTION' 1.56 1.59  . . 133 2617 96.00  . . . . 0.3129 . . . . . . . . . . . 0.3845 
'X-RAY DIFFRACTION' 1.59 1.62  . . 171 2699 98.00  . . . . 0.2894 . . . . . . . . . . . 0.3305 
'X-RAY DIFFRACTION' 1.62 1.66  . . 144 2704 99.00  . . . . 0.2682 . . . . . . . . . . . 0.2848 
'X-RAY DIFFRACTION' 1.66 1.70  . . 140 2713 99.00  . . . . 0.2636 . . . . . . . . . . . 0.2985 
'X-RAY DIFFRACTION' 1.70 1.75  . . 149 2756 99.00  . . . . 0.2738 . . . . . . . . . . . 0.3199 
'X-RAY DIFFRACTION' 1.75 1.80  . . 154 2694 99.00  . . . . 0.2777 . . . . . . . . . . . 0.3667 
'X-RAY DIFFRACTION' 1.80 1.86  . . 138 2768 100.00 . . . . 0.2609 . . . . . . . . . . . 0.3279 
'X-RAY DIFFRACTION' 1.86 1.92  . . 145 2746 100.00 . . . . 0.2576 . . . . . . . . . . . 0.2935 
'X-RAY DIFFRACTION' 1.92 2.00  . . 151 2730 99.00  . . . . 0.2555 . . . . . . . . . . . 0.2753 
'X-RAY DIFFRACTION' 2.00 2.09  . . 136 2746 99.00  . . . . 0.2495 . . . . . . . . . . . 0.2652 
'X-RAY DIFFRACTION' 2.09 2.20  . . 148 2762 99.00  . . . . 0.2574 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 2.20 2.34  . . 134 2782 99.00  . . . . 0.2633 . . . . . . . . . . . 0.2734 
'X-RAY DIFFRACTION' 2.34 2.52  . . 127 2762 99.00  . . . . 0.2777 . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 2.52 2.77  . . 146 2795 99.00  . . . . 0.2788 . . . . . . . . . . . 0.3280 
'X-RAY DIFFRACTION' 2.77 3.17  . . 125 2822 99.00  . . . . 0.2646 . . . . . . . . . . . 0.2579 
'X-RAY DIFFRACTION' 3.18 4.00  . . 177 2809 99.00  . . . . 0.2098 . . . . . . . . . . . 0.2366 
'X-RAY DIFFRACTION' 4.00 43.12 . . 147 2973 99.00  . . . . 0.2118 . . . . . . . . . . . 0.2270 
# 
_struct.entry_id                     8R3N 
_struct.title                        'Crystal structure of PfpI, Pseudomonas aeruginosa PAO1' 
_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        8R3N 
_struct_keywords.text            'Glyoxalase, ThiJ/DJ-1/PfpI superfamily member, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0A8R9N9_PSEAI 
_struct_ref.pdbx_db_accession          A0A0A8R9N9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTQSLHGKVVAALVTDGFEQVELTGPKKALEDAGATVRILSDKAGEVRGWNHHQPAEAFRVDGTFEDASLDDYDALLLPG
GVINSDQIRSLAKAQELAIRAEQASKPVAVICHGAWLLISAGLVQGRTLTSWPSLKDDINNAGGHWVDQEVAVDGKLVSS
RKPEDIPAFNRRFIEILAG
;
_struct_ref.pdbx_align_begin           37 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8R3N B 1 ? 179 ? A0A0A8R9N9 37 ? 215 ? 1 179 
2 1 8R3N X 1 ? 179 ? A0A0A8R9N9 37 ? 215 ? 1 179 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 1460  ? 
1 MORE         -5    ? 
1 'SSA (A^2)'  14380 ? 
# 
_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   'assay for oligomerization' 
_pdbx_struct_assembly_auth_evidence.details                'Sedimentation Velocity Analytical Ultracentrifugation' 
# 
_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 GLN A 20  ? ALA A 33  ? GLN B 20  ALA B 33  1 ? 14 
HELX_P HELX_P2  AA2 SER A 69  ? TYR A 73  ? SER B 69  TYR B 73  5 ? 5  
HELX_P HELX_P3  AA3 GLY A 81  ? ARG A 89  ? GLY B 81  ARG B 89  1 ? 9  
HELX_P HELX_P4  AA4 LEU A 91  ? ALA A 104 ? LEU B 91  ALA B 104 1 ? 14 
HELX_P HELX_P5  AA5 ALA A 115 ? ALA A 121 ? ALA B 115 ALA B 121 1 ? 7  
HELX_P HELX_P6  AA6 TRP A 132 ? SER A 134 ? TRP B 132 SER B 134 5 ? 3  
HELX_P HELX_P7  AA7 LEU A 135 ? ALA A 142 ? LEU B 135 ALA B 142 1 ? 8  
HELX_P HELX_P8  AA8 LYS A 162 ? GLU A 164 ? LYS B 162 GLU B 164 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 165 ? GLY A 179 ? ASP B 165 GLY B 179 1 ? 15 
HELX_P HELX_P10 AB1 GLN B 20  ? ALA B 33  ? GLN X 20  ALA X 33  1 ? 14 
HELX_P HELX_P11 AB2 SER B 69  ? TYR B 73  ? SER X 69  TYR X 73  5 ? 5  
HELX_P HELX_P12 AB3 GLY B 81  ? ARG B 89  ? GLY X 81  ARG X 89  1 ? 9  
HELX_P HELX_P13 AB4 LEU B 91  ? ALA B 104 ? LEU X 91  ALA X 104 1 ? 14 
HELX_P HELX_P14 AB5 ALA B 115 ? ALA B 121 ? ALA X 115 ALA X 121 1 ? 7  
HELX_P HELX_P15 AB6 TRP B 132 ? SER B 134 ? TRP X 132 SER X 134 5 ? 3  
HELX_P HELX_P16 AB7 LEU B 135 ? ALA B 142 ? LEU X 135 ALA X 142 1 ? 8  
HELX_P HELX_P17 AB8 LYS B 162 ? GLU B 164 ? LYS X 162 GLU X 164 5 ? 3  
HELX_P HELX_P18 AB9 ASP B 165 ? GLY B 179 ? ASP X 165 GLY X 179 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
AA4 ? 7 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA6 1 2 ? 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 GLY A 63  ? THR A 64  ? GLY B 63  THR B 64  
AA1 2 THR A 36  ? SER A 41  ? THR B 36  SER B 41  
AA1 3 VAL A 9   ? LEU A 13  ? VAL B 9   LEU B 13  
AA1 4 ALA A 75  ? LEU A 78  ? ALA B 75  LEU B 78  
AA1 5 VAL A 108 ? ILE A 111 ? VAL B 108 ILE B 111 
AA1 6 LEU A 157 ? SER A 160 ? LEU B 157 SER B 160 
AA1 7 VAL A 151 ? ASP A 154 ? VAL B 151 ASP B 154 
AA2 1 PHE A 18  ? GLU A 19  ? PHE B 18  GLU B 19  
AA2 2 GLU A 46  ? ASN A 51  ? GLU B 46  ASN B 51  
AA2 3 GLN A 54  ? ARG A 60  ? GLN B 54  ARG B 60  
AA3 1 THR A 128 ? LEU A 129 ? THR B 128 LEU B 129 
AA3 2 HIS A 145 ? TRP A 146 ? HIS B 145 TRP B 146 
AA4 1 GLY B 63  ? THR B 64  ? GLY X 63  THR X 64  
AA4 2 THR B 36  ? SER B 41  ? THR X 36  SER X 41  
AA4 3 VAL B 9   ? LEU B 13  ? VAL X 9   LEU X 13  
AA4 4 ALA B 75  ? LEU B 78  ? ALA X 75  LEU X 78  
AA4 5 VAL B 108 ? ILE B 111 ? VAL X 108 ILE X 111 
AA4 6 LEU B 157 ? SER B 160 ? LEU X 157 SER X 160 
AA4 7 ALA B 152 ? ASP B 154 ? ALA X 152 ASP X 154 
AA5 1 PHE B 18  ? GLU B 19  ? PHE X 18  GLU X 19  
AA5 2 GLU B 46  ? ASN B 51  ? GLU X 46  ASN X 51  
AA5 3 GLN B 54  ? ARG B 60  ? GLN X 54  ARG X 60  
AA6 1 THR B 128 ? LEU B 129 ? THR X 128 LEU X 129 
AA6 2 HIS B 145 ? TRP B 146 ? HIS X 145 TRP X 146 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLY A 63  ? O GLY B 63  N SER A 41  ? N SER B 41  
AA1 2 3 O THR A 36  ? O THR B 36  N VAL A 10  ? N VAL B 10  
AA1 3 4 N ALA A 11  ? N ALA B 11  O LEU A 77  ? O LEU B 77  
AA1 4 5 N LEU A 78  ? N LEU B 78  O ALA A 109 ? O ALA B 109 
AA1 5 6 N VAL A 108 ? N VAL B 108 O VAL A 158 ? O VAL B 158 
AA1 6 7 O SER A 159 ? O SER B 159 N ALA A 152 ? N ALA B 152 
AA2 1 2 N PHE A 18  ? N PHE B 18  O TRP A 50  ? O TRP B 50  
AA2 2 3 N GLY A 49  ? N GLY B 49  O ALA A 56  ? O ALA B 56  
AA3 1 2 N LEU A 129 ? N LEU B 129 O HIS A 145 ? O HIS B 145 
AA4 1 2 O GLY B 63  ? O GLY X 63  N SER B 41  ? N SER X 41  
AA4 2 3 O ARG B 38  ? O ARG X 38  N ALA B 12  ? N ALA X 12  
AA4 3 4 N ALA B 11  ? N ALA X 11  O LEU B 77  ? O LEU X 77  
AA4 4 5 N LEU B 78  ? N LEU X 78  O ALA B 109 ? O ALA X 109 
AA4 5 6 N VAL B 108 ? N VAL X 108 O VAL B 158 ? O VAL X 158 
AA4 6 7 O SER B 159 ? O SER X 159 N ALA B 152 ? N ALA X 152 
AA5 1 2 N PHE B 18  ? N PHE X 18  O TRP B 50  ? O TRP X 50  
AA5 2 3 N GLY B 49  ? N GLY X 49  O ALA B 56  ? O ALA X 56  
AA6 1 2 N LEU B 129 ? N LEU X 129 O HIS B 145 ? O HIS X 145 
# 
_pdbx_entry_details.entry_id                   8R3N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    229 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    243 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     318 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    X 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     205 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.15 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             X 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              112 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             X 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              112 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             X 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              112 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                120.34 
_pdbx_validate_rmsd_angle.angle_target_value         111.50 
_pdbx_validate_rmsd_angle.angle_deviation            8.84 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS B 52  ? ? 52.44   -110.49 
2 1 ALA B 56  ? ? -127.34 -124.16 
3 1 CYS B 112 ? ? 62.77   -108.28 
4 1 SER B 131 ? ? 179.45  174.73  
5 1 HIS X 52  ? ? 59.97   -111.57 
6 1 ALA X 56  ? ? -119.31 -134.51 
7 1 CYS X 112 ? ? 73.27   -110.68 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B MET 1 ? A MET 1 
2 1 Y 1 X MET 1 ? B MET 1 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Biotechnology and Biological Sciences Research Council (BBSRC)' 'United Kingdom' ? 1 
'Jardine Foundation'                                             'Hong Kong'      ? 2 
'Rosetrees Trust'                                                'United Kingdom' ? 3 
# 
_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   2VRN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R3N 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.023815 
_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]   0.012705 
_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]   0.009700 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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   . THR A 1 2   ? 26.687 9.282   64.604  1.00 31.49 ? 2   THR B N   1 
ATOM   2    C CA  . THR A 1 2   ? 26.541 8.669   63.287  1.00 36.59 ? 2   THR B CA  1 
ATOM   3    C C   . THR A 1 2   ? 27.857 8.105   62.751  1.00 25.38 ? 2   THR B C   1 
ATOM   4    O O   . THR A 1 2   ? 28.891 8.151   63.414  1.00 35.15 ? 2   THR B O   1 
ATOM   5    C CB  . THR A 1 2   ? 25.956 9.655   62.250  1.00 37.58 ? 2   THR B CB  1 
ATOM   6    O OG1 . THR A 1 2   ? 26.916 10.683  61.967  1.00 35.56 ? 2   THR B OG1 1 
ATOM   7    C CG2 . THR A 1 2   ? 24.673 10.285  62.775  1.00 42.24 ? 2   THR B CG2 1 
ATOM   8    N N   . GLN A 1 3   ? 27.805 7.602   61.523  1.00 27.94 ? 3   GLN B N   1 
ATOM   9    C CA  . GLN A 1 3   ? 28.912 6.853   60.951  1.00 22.72 ? 3   GLN B CA  1 
ATOM   10   C C   . GLN A 1 3   ? 29.993 7.791   60.431  1.00 19.15 ? 3   GLN B C   1 
ATOM   11   O O   . GLN A 1 3   ? 29.717 8.689   59.627  1.00 20.34 ? 3   GLN B O   1 
ATOM   12   C CB  . GLN A 1 3   ? 28.387 6.002   59.800  1.00 16.08 ? 3   GLN B CB  1 
ATOM   13   C CG  . GLN A 1 3   ? 29.468 5.256   59.069  1.00 18.01 ? 3   GLN B CG  1 
ATOM   14   C CD  . GLN A 1 3   ? 30.024 4.134   59.908  1.00 15.01 ? 3   GLN B CD  1 
ATOM   15   O OE1 . GLN A 1 3   ? 29.305 3.199   60.267  1.00 17.16 ? 3   GLN B OE1 1 
ATOM   16   N NE2 . GLN A 1 3   ? 31.316 4.197   60.194  1.00 15.84 ? 3   GLN B NE2 1 
ATOM   17   N N   . SER A 1 4   ? 31.232 7.568   60.865  1.00 19.59 ? 4   SER B N   1 
ATOM   18   C CA  . SER A 1 4   ? 32.360 8.303   60.316  1.00 18.17 ? 4   SER B CA  1 
ATOM   19   C C   . SER A 1 4   ? 32.960 7.503   59.174  1.00 16.31 ? 4   SER B C   1 
ATOM   20   O O   . SER A 1 4   ? 33.163 6.291   59.295  1.00 18.83 ? 4   SER B O   1 
ATOM   21   C CB  . SER A 1 4   ? 33.446 8.557   61.362  1.00 19.61 ? 4   SER B CB  1 
ATOM   22   O OG  . SER A 1 4   ? 34.629 8.979   60.701  1.00 18.62 ? 4   SER B OG  1 
ATOM   23   N N   . LEU A 1 5   ? 33.211 8.188   58.057  1.00 18.41 ? 5   LEU B N   1 
ATOM   24   C CA  . LEU A 1 5   ? 33.966 7.653   56.932  1.00 14.26 ? 5   LEU B CA  1 
ATOM   25   C C   . LEU A 1 5   ? 35.365 8.255   56.843  1.00 17.37 ? 5   LEU B C   1 
ATOM   26   O O   . LEU A 1 5   ? 35.986 8.217   55.776  1.00 17.93 ? 5   LEU B O   1 
ATOM   27   C CB  . LEU A 1 5   ? 33.218 7.901   55.628  1.00 17.78 ? 5   LEU B CB  1 
ATOM   28   C CG  . LEU A 1 5   ? 31.893 7.168   55.474  1.00 14.95 ? 5   LEU B CG  1 
ATOM   29   C CD1 . LEU A 1 5   ? 31.311 7.506   54.122  1.00 17.71 ? 5   LEU B CD1 1 
ATOM   30   C CD2 . LEU A 1 5   ? 32.066 5.664   55.624  1.00 16.62 ? 5   LEU B CD2 1 
ATOM   31   N N   . HIS A 1 6   ? 35.863 8.831   57.937  1.00 16.48 ? 6   HIS B N   1 
ATOM   32   C CA  . HIS A 1 6   ? 37.176 9.458   57.916  1.00 18.75 ? 6   HIS B CA  1 
ATOM   33   C C   . HIS A 1 6   ? 38.222 8.464   57.428  1.00 18.66 ? 6   HIS B C   1 
ATOM   34   O O   . HIS A 1 6   ? 38.236 7.306   57.855  1.00 19.48 ? 6   HIS B O   1 
ATOM   35   C CB  . HIS A 1 6   ? 37.526 9.935   59.323  1.00 20.65 ? 6   HIS B CB  1 
ATOM   36   C CG  . HIS A 1 6   ? 38.725 10.826  59.361  1.00 28.03 ? 6   HIS B CG  1 
ATOM   37   N ND1 . HIS A 1 6   ? 38.663 12.171  59.072  1.00 34.15 ? 6   HIS B ND1 1 
ATOM   38   C CD2 . HIS A 1 6   ? 40.028 10.554  59.608  1.00 34.22 ? 6   HIS B CD2 1 
ATOM   39   C CE1 . HIS A 1 6   ? 39.873 12.694  59.160  1.00 36.16 ? 6   HIS B CE1 1 
ATOM   40   N NE2 . HIS A 1 6   ? 40.718 11.734  59.487  1.00 32.71 ? 6   HIS B NE2 1 
ATOM   41   N N   . GLY A 1 7   ? 39.089 8.921   56.513  1.00 18.18 ? 7   GLY B N   1 
ATOM   42   C CA  . GLY A 1 7   ? 40.103 8.086   55.889  1.00 16.70 ? 7   GLY B CA  1 
ATOM   43   C C   . GLY A 1 7   ? 39.682 7.443   54.577  1.00 15.24 ? 7   GLY B C   1 
ATOM   44   O O   . GLY A 1 7   ? 40.541 6.947   53.831  1.00 17.10 ? 7   GLY B O   1 
ATOM   45   N N   . LYS A 1 8   ? 38.387 7.414   54.281  1.00 19.54 ? 8   LYS B N   1 
ATOM   46   C CA  . LYS A 1 8   ? 37.939 6.837   53.032  1.00 11.93 ? 8   LYS B CA  1 
ATOM   47   C C   . LYS A 1 8   ? 38.008 7.879   51.928  1.00 16.01 ? 8   LYS B C   1 
ATOM   48   O O   . LYS A 1 8   ? 37.840 9.080   52.169  1.00 18.93 ? 8   LYS B O   1 
ATOM   49   C CB  . LYS A 1 8   ? 36.479 6.385   53.162  1.00 13.23 ? 8   LYS B CB  1 
ATOM   50   C CG  . LYS A 1 8   ? 36.224 5.238   54.145  1.00 13.57 ? 8   LYS B CG  1 
ATOM   51   C CD  . LYS A 1 8   ? 36.774 3.925   53.602  1.00 17.02 ? 8   LYS B CD  1 
ATOM   52   C CE  . LYS A 1 8   ? 36.527 2.773   54.569  1.00 18.64 ? 8   LYS B CE  1 
ATOM   53   N NZ  . LYS A 1 8   ? 37.235 1.537   54.111  1.00 21.99 ? 8   LYS B NZ  1 
ATOM   54   N N   . VAL A 1 9   ? 38.191 7.397   50.700  1.00 14.77 ? 9   VAL B N   1 
ATOM   55   C CA  . VAL A 1 9   ? 38.295 8.233   49.512  1.00 15.16 ? 9   VAL B CA  1 
ATOM   56   C C   . VAL A 1 9   ? 37.452 7.623   48.403  1.00 17.13 ? 9   VAL B C   1 
ATOM   57   O O   . VAL A 1 9   ? 37.560 6.425   48.118  1.00 15.33 ? 9   VAL B O   1 
ATOM   58   C CB  . VAL A 1 9   ? 39.744 8.407   49.027  1.00 20.23 ? 9   VAL B CB  1 
ATOM   59   C CG1 . VAL A 1 9   ? 39.793 9.457   47.935  1.00 17.89 ? 9   VAL B CG1 1 
ATOM   60   C CG2 . VAL A 1 9   ? 40.652 8.814   50.176  1.00 17.00 ? 9   VAL B CG2 1 
ATOM   61   N N   . VAL A 1 10  ? 36.606 8.438   47.798  1.00 16.86 ? 10  VAL B N   1 
ATOM   62   C CA  . VAL A 1 10  ? 35.698 7.972   46.765  1.00 13.92 ? 10  VAL B CA  1 
ATOM   63   C C   . VAL A 1 10  ? 36.031 8.684   45.464  1.00 15.33 ? 10  VAL B C   1 
ATOM   64   O O   . VAL A 1 10  ? 36.190 9.912   45.445  1.00 17.77 ? 10  VAL B O   1 
ATOM   65   C CB  . VAL A 1 10  ? 34.227 8.216   47.145  1.00 13.65 ? 10  VAL B CB  1 
ATOM   66   C CG1 . VAL A 1 10  ? 33.321 7.822   45.964  1.00 16.02 ? 10  VAL B CG1 1 
ATOM   67   C CG2 . VAL A 1 10  ? 33.868 7.430   48.389  1.00 16.53 ? 10  VAL B CG2 1 
ATOM   68   N N   . ALA A 1 11  ? 36.117 7.915   44.375  1.00 12.63 ? 11  ALA B N   1 
ATOM   69   C CA  . ALA A 1 11  ? 36.285 8.474   43.042  1.00 17.28 ? 11  ALA B CA  1 
ATOM   70   C C   . ALA A 1 11  ? 34.909 8.519   42.388  1.00 15.19 ? 11  ALA B C   1 
ATOM   71   O O   . ALA A 1 11  ? 34.242 7.489   42.284  1.00 17.24 ? 11  ALA B O   1 
ATOM   72   C CB  . ALA A 1 11  ? 37.253 7.637   42.201  1.00 16.79 ? 11  ALA B CB  1 
ATOM   73   N N   . ALA A 1 12  ? 34.479 9.714   41.996  1.00 15.36 ? 12  ALA B N   1 
ATOM   74   C CA  . ALA A 1 12  ? 33.317 9.877   41.130  1.00 15.57 ? 12  ALA B CA  1 
ATOM   75   C C   . ALA A 1 12  ? 33.805 9.905   39.688  1.00 15.47 ? 12  ALA B C   1 
ATOM   76   O O   . ALA A 1 12  ? 34.687 10.699  39.348  1.00 19.28 ? 12  ALA B O   1 
ATOM   77   C CB  . ALA A 1 12  ? 32.625 11.204  41.424  1.00 17.83 ? 12  ALA B CB  1 
ATOM   78   N N   . LEU A 1 13  ? 33.245 9.042   38.844  1.00 12.05 ? 13  LEU B N   1 
ATOM   79   C CA  . LEU A 1 13  ? 33.648 8.984   37.434  1.00 17.22 ? 13  LEU B CA  1 
ATOM   80   C C   . LEU A 1 13  ? 32.570 9.667   36.598  1.00 15.21 ? 13  LEU B C   1 
ATOM   81   O O   . LEU A 1 13  ? 31.447 9.165   36.509  1.00 15.82 ? 13  LEU B O   1 
ATOM   82   C CB  . LEU A 1 13  ? 33.788 7.534   36.983  1.00 18.30 ? 13  LEU B CB  1 
ATOM   83   C CG  . LEU A 1 13  ? 34.578 6.568   37.858  1.00 31.96 ? 13  LEU B CG  1 
ATOM   84   C CD1 . LEU A 1 13  ? 34.740 5.271   37.108  1.00 21.13 ? 13  LEU B CD1 1 
ATOM   85   C CD2 . LEU A 1 13  ? 35.938 7.160   38.245  1.00 22.39 ? 13  LEU B CD2 1 
ATOM   86   N N   . VAL A 1 14  ? 32.906 10.784  35.954  1.00 17.05 ? 14  VAL B N   1 
ATOM   87   C CA  . VAL A 1 14  ? 31.913 11.540  35.196  1.00 14.44 ? 14  VAL B CA  1 
ATOM   88   C C   . VAL A 1 14  ? 32.544 12.055  33.912  1.00 16.41 ? 14  VAL B C   1 
ATOM   89   O O   . VAL A 1 14  ? 33.754 12.294  33.841  1.00 19.07 ? 14  VAL B O   1 
ATOM   90   C CB  . VAL A 1 14  ? 31.384 12.752  35.989  1.00 15.00 ? 14  VAL B CB  1 
ATOM   91   C CG1 . VAL A 1 14  ? 30.447 12.329  37.110  1.00 18.17 ? 14  VAL B CG1 1 
ATOM   92   C CG2 . VAL A 1 14  ? 32.547 13.553  36.554  1.00 20.53 ? 14  VAL B CG2 1 
ATOM   93   N N   . THR A 1 15  ? 31.701 12.265  32.905  1.00 17.41 ? 15  THR B N   1 
ATOM   94   C CA  . THR A 1 15  ? 32.066 12.977  31.683  1.00 15.92 ? 15  THR B CA  1 
ATOM   95   C C   . THR A 1 15  ? 31.096 14.140  31.524  1.00 17.10 ? 15  THR B C   1 
ATOM   96   O O   . THR A 1 15  ? 30.149 14.277  32.294  1.00 17.09 ? 15  THR B O   1 
ATOM   97   C CB  . THR A 1 15  ? 32.045 12.050  30.452  1.00 15.77 ? 15  THR B CB  1 
ATOM   98   O OG1 . THR A 1 15  ? 30.703 11.644  30.140  1.00 16.82 ? 15  THR B OG1 1 
ATOM   99   C CG2 . THR A 1 15  ? 32.890 10.810  30.693  1.00 22.30 ? 15  THR B CG2 1 
ATOM   100  N N   . ASP A 1 16  ? 31.326 14.998  30.528  1.00 16.15 ? 16  ASP B N   1 
ATOM   101  C CA  . ASP A 1 16  ? 30.412 16.118  30.320  1.00 17.04 ? 16  ASP B CA  1 
ATOM   102  C C   . ASP A 1 16  ? 28.989 15.600  30.138  1.00 18.39 ? 16  ASP B C   1 
ATOM   103  O O   . ASP A 1 16  ? 28.745 14.627  29.416  1.00 18.38 ? 16  ASP B O   1 
ATOM   104  C CB  . ASP A 1 16  ? 30.807 16.905  29.064  1.00 16.80 ? 16  ASP B CB  1 
ATOM   105  C CG  . ASP A 1 16  ? 32.064 17.742  29.240  1.00 22.95 ? 16  ASP B CG  1 
ATOM   106  O OD1 . ASP A 1 16  ? 32.404 18.140  30.371  1.00 21.17 ? 16  ASP B OD1 1 
ATOM   107  O OD2 . ASP A 1 16  ? 32.724 18.002  28.215  1.00 30.70 ? 16  ASP B OD2 1 
ATOM   108  N N   . GLY A 1 17  ? 28.043 16.262  30.786  1.00 17.40 ? 17  GLY B N   1 
ATOM   109  C CA  . GLY A 1 17  ? 26.653 15.880  30.681  1.00 20.14 ? 17  GLY B CA  1 
ATOM   110  C C   . GLY A 1 17  ? 26.156 14.989  31.790  1.00 18.45 ? 17  GLY B C   1 
ATOM   111  O O   . GLY A 1 17  ? 25.116 14.335  31.615  1.00 18.18 ? 17  GLY B O   1 
ATOM   112  N N   . PHE A 1 18  ? 26.881 14.913  32.905  1.00 18.21 ? 18  PHE B N   1 
ATOM   113  C CA  . PHE A 1 18  ? 26.411 14.165  34.056  1.00 18.19 ? 18  PHE B CA  1 
ATOM   114  C C   . PHE A 1 18  ? 25.354 14.965  34.799  1.00 15.80 ? 18  PHE B C   1 
ATOM   115  O O   . PHE A 1 18  ? 25.319 16.198  34.745  1.00 17.11 ? 18  PHE B O   1 
ATOM   116  C CB  . PHE A 1 18  ? 27.580 13.749  34.965  1.00 19.54 ? 18  PHE B CB  1 
ATOM   117  C CG  . PHE A 1 18  ? 28.241 14.889  35.706  1.00 15.53 ? 18  PHE B CG  1 
ATOM   118  C CD1 . PHE A 1 18  ? 29.312 15.576  35.144  1.00 17.44 ? 18  PHE B CD1 1 
ATOM   119  C CD2 . PHE A 1 18  ? 27.795 15.258  36.963  1.00 17.58 ? 18  PHE B CD2 1 
ATOM   120  C CE1 . PHE A 1 18  ? 29.917 16.610  35.820  1.00 16.64 ? 18  PHE B CE1 1 
ATOM   121  C CE2 . PHE A 1 18  ? 28.396 16.300  37.640  1.00 18.24 ? 18  PHE B CE2 1 
ATOM   122  C CZ  . PHE A 1 18  ? 29.456 16.970  37.071  1.00 17.20 ? 18  PHE B CZ  1 
ATOM   123  N N   . GLU A 1 19  ? 24.473 14.243  35.480  1.00 16.61 ? 19  GLU B N   1 
ATOM   124  C CA  . GLU A 1 19  ? 23.438 14.874  36.292  1.00 15.22 ? 19  GLU B CA  1 
ATOM   125  C C   . GLU A 1 19  ? 24.099 15.493  37.514  1.00 19.76 ? 19  GLU B C   1 
ATOM   126  O O   . GLU A 1 19  ? 24.618 14.777  38.378  1.00 17.73 ? 19  GLU B O   1 
ATOM   127  C CB  . GLU A 1 19  ? 22.406 13.834  36.702  1.00 17.24 ? 19  GLU B CB  1 
ATOM   128  C CG  . GLU A 1 19  ? 21.174 14.462  37.328  1.00 20.25 ? 19  GLU B CG  1 
ATOM   129  C CD  . GLU A 1 19  ? 20.414 15.301  36.326  1.00 24.47 ? 19  GLU B CD  1 
ATOM   130  O OE1 . GLU A 1 19  ? 20.067 14.753  35.255  1.00 22.07 ? 19  GLU B OE1 1 
ATOM   131  O OE2 . GLU A 1 19  ? 20.202 16.506  36.588  1.00 21.66 ? 19  GLU B OE2 1 
ATOM   132  N N   . GLN A 1 20  ? 24.076 16.824  37.594  1.00 18.76 ? 20  GLN B N   1 
ATOM   133  C CA  . GLN A 1 20  ? 24.883 17.515  38.599  1.00 18.50 ? 20  GLN B CA  1 
ATOM   134  C C   . GLN A 1 20  ? 24.564 17.063  40.031  1.00 19.04 ? 20  GLN B C   1 
ATOM   135  O O   . GLN A 1 20  ? 25.478 16.782  40.816  1.00 16.57 ? 20  GLN B O   1 
ATOM   136  C CB  . GLN A 1 20  ? 24.748 19.028  38.440  1.00 19.01 ? 20  GLN B CB  1 
ATOM   137  C CG  . GLN A 1 20  ? 25.652 19.806  39.391  1.00 19.30 ? 20  GLN B CG  1 
ATOM   138  C CD  . GLN A 1 20  ? 25.739 21.258  39.008  1.00 23.80 ? 20  GLN B CD  1 
ATOM   139  O OE1 . GLN A 1 20  ? 26.002 21.593  37.850  1.00 22.44 ? 20  GLN B OE1 1 
ATOM   140  N NE2 . GLN A 1 20  ? 25.521 22.135  39.978  1.00 22.67 ? 20  GLN B NE2 1 
ATOM   141  N N   . VAL A 1 21  ? 23.282 16.992  40.395  1.00 20.81 ? 21  VAL B N   1 
ATOM   142  C CA  . VAL A 1 21  ? 22.910 16.645  41.771  1.00 17.20 ? 21  VAL B CA  1 
ATOM   143  C C   . VAL A 1 21  ? 23.306 15.212  42.120  1.00 18.97 ? 21  VAL B C   1 
ATOM   144  O O   . VAL A 1 21  ? 23.559 14.898  43.292  1.00 18.03 ? 21  VAL B O   1 
ATOM   145  C CB  . VAL A 1 21  ? 21.410 16.906  41.996  1.00 18.74 ? 21  VAL B CB  1 
ATOM   146  C CG1 . VAL A 1 21  ? 20.579 15.962  41.140  1.00 19.97 ? 21  VAL B CG1 1 
ATOM   147  C CG2 . VAL A 1 21  ? 21.056 16.736  43.447  1.00 24.61 ? 21  VAL B CG2 1 
ATOM   148  N N   . GLU A 1 22  ? 23.380 14.322  41.128  1.00 20.97 ? 22  GLU B N   1 
ATOM   149  C CA  . GLU A 1 22  ? 23.826 12.956  41.367  1.00 18.66 ? 22  GLU B CA  1 
ATOM   150  C C   . GLU A 1 22  ? 25.316 12.883  41.656  1.00 16.65 ? 22  GLU B C   1 
ATOM   151  O O   . GLU A 1 22  ? 25.791 11.845  42.131  1.00 16.44 ? 22  GLU B O   1 
ATOM   152  C CB  . GLU A 1 22  ? 23.415 12.046  40.202  1.00 12.49 ? 22  GLU B CB  1 
ATOM   153  C CG  . GLU A 1 22  ? 21.895 11.805  40.179  1.00 17.01 ? 22  GLU B CG  1 
ATOM   154  C CD  . GLU A 1 22  ? 21.373 11.242  38.856  1.00 16.80 ? 22  GLU B CD  1 
ATOM   155  O OE1 . GLU A 1 22  ? 22.157 10.623  38.114  1.00 17.02 ? 22  GLU B OE1 1 
ATOM   156  O OE2 . GLU A 1 22  ? 20.162 11.426  38.561  1.00 22.01 ? 22  GLU B OE2 1 
ATOM   157  N N   . LEU A 1 23  ? 26.059 13.957  41.385  1.00 15.76 ? 23  LEU B N   1 
ATOM   158  C CA  . LEU A 1 23  ? 27.406 14.098  41.932  1.00 15.72 ? 23  LEU B CA  1 
ATOM   159  C C   . LEU A 1 23  ? 27.367 14.882  43.241  1.00 20.26 ? 23  LEU B C   1 
ATOM   160  O O   . LEU A 1 23  ? 27.832 14.399  44.277  1.00 15.86 ? 23  LEU B O   1 
ATOM   161  C CB  . LEU A 1 23  ? 28.328 14.810  40.936  1.00 17.39 ? 23  LEU B CB  1 
ATOM   162  C CG  . LEU A 1 23  ? 29.627 15.304  41.595  1.00 17.44 ? 23  LEU B CG  1 
ATOM   163  C CD1 . LEU A 1 23  ? 30.429 14.097  41.979  1.00 15.30 ? 23  LEU B CD1 1 
ATOM   164  C CD2 . LEU A 1 23  ? 30.431 16.214  40.658  1.00 21.76 ? 23  LEU B CD2 1 
ATOM   165  N N   . THR A 1 24  ? 26.789 16.086  43.220  1.00 20.21 ? 24  THR B N   1 
ATOM   166  C CA  . THR A 1 24  ? 26.941 16.984  44.372  1.00 22.25 ? 24  THR B CA  1 
ATOM   167  C C   . THR A 1 24  ? 26.225 16.477  45.620  1.00 22.03 ? 24  THR B C   1 
ATOM   168  O O   . THR A 1 24  ? 26.712 16.693  46.737  1.00 20.08 ? 24  THR B O   1 
ATOM   169  C CB  . THR A 1 24  ? 26.472 18.396  44.041  1.00 21.99 ? 24  THR B CB  1 
ATOM   170  O OG1 . THR A 1 24  ? 25.064 18.374  43.748  1.00 20.63 ? 24  THR B OG1 1 
ATOM   171  C CG2 . THR A 1 24  ? 27.262 18.966  42.882  1.00 22.27 ? 24  THR B CG2 1 
ATOM   172  N N   . GLY A 1 25  ? 25.055 15.855  45.468  1.00 18.24 ? 25  GLY B N   1 
ATOM   173  C CA  . GLY A 1 25  ? 24.313 15.350  46.603  1.00 18.84 ? 25  GLY B CA  1 
ATOM   174  C C   . GLY A 1 25  ? 25.089 14.288  47.360  1.00 18.72 ? 25  GLY B C   1 
ATOM   175  O O   . GLY A 1 25  ? 25.343 14.411  48.562  1.00 17.02 ? 25  GLY B O   1 
ATOM   176  N N   . PRO A 1 26  ? 25.457 13.204  46.675  1.00 18.66 ? 26  PRO B N   1 
ATOM   177  C CA  . PRO A 1 26  ? 26.309 12.195  47.326  1.00 13.81 ? 26  PRO B CA  1 
ATOM   178  C C   . PRO A 1 26  ? 27.647 12.735  47.800  1.00 18.17 ? 26  PRO B C   1 
ATOM   179  O O   . PRO A 1 26  ? 28.099 12.361  48.883  1.00 14.09 ? 26  PRO B O   1 
ATOM   180  C CB  . PRO A 1 26  ? 26.452 11.110  46.251  1.00 20.06 ? 26  PRO B CB  1 
ATOM   181  C CG  . PRO A 1 26  ? 25.227 11.281  45.393  1.00 16.19 ? 26  PRO B CG  1 
ATOM   182  C CD  . PRO A 1 26  ? 24.955 12.747  45.363  1.00 15.83 ? 26  PRO B CD  1 
ATOM   183  N N   . LYS A 1 27  ? 28.285 13.616  47.028  1.00 18.63 ? 27  LYS B N   1 
ATOM   184  C CA  . LYS A 1 27  ? 29.582 14.160  47.426  1.00 16.67 ? 27  LYS B CA  1 
ATOM   185  C C   . LYS A 1 27  ? 29.492 14.889  48.761  1.00 22.06 ? 27  LYS B C   1 
ATOM   186  O O   . LYS A 1 27  ? 30.322 14.678  49.657  1.00 19.11 ? 27  LYS B O   1 
ATOM   187  C CB  . LYS A 1 27  ? 30.101 15.092  46.327  1.00 23.42 ? 27  LYS B CB  1 
ATOM   188  C CG  . LYS A 1 27  ? 31.462 15.708  46.590  1.00 17.90 ? 27  LYS B CG  1 
ATOM   189  C CD  . LYS A 1 27  ? 32.005 16.331  45.319  1.00 18.04 ? 27  LYS B CD  1 
ATOM   190  C CE  . LYS A 1 27  ? 33.393 16.893  45.504  1.00 24.97 ? 27  LYS B CE  1 
ATOM   191  N NZ  . LYS A 1 27  ? 33.319 18.178  46.244  1.00 26.37 ? 27  LYS B NZ  1 
ATOM   192  N N   . LYS A 1 28  ? 28.472 15.739  48.923  1.00 21.48 ? 28  LYS B N   1 
ATOM   193  C CA  . LYS A 1 28  ? 28.306 16.431  50.196  1.00 19.64 ? 28  LYS B CA  1 
ATOM   194  C C   . LYS A 1 28  ? 28.089 15.440  51.328  1.00 21.75 ? 28  LYS B C   1 
ATOM   195  O O   . LYS A 1 28  ? 28.697 15.565  52.398  1.00 19.67 ? 28  LYS B O   1 
ATOM   196  C CB  . LYS A 1 28  ? 27.150 17.422  50.124  1.00 21.60 ? 28  LYS B CB  1 
ATOM   197  C CG  . LYS A 1 28  ? 27.072 18.350  51.324  1.00 32.86 ? 28  LYS B CG  1 
ATOM   198  C CD  . LYS A 1 28  ? 25.655 18.845  51.567  1.00 40.36 ? 28  LYS B CD  1 
ATOM   199  C CE  . LYS A 1 28  ? 25.572 19.608  52.885  1.00 37.24 ? 28  LYS B CE  1 
ATOM   200  N NZ  . LYS A 1 28  ? 26.935 19.923  53.414  1.00 36.62 ? 28  LYS B NZ  1 
ATOM   201  N N   . ALA A 1 29  ? 27.254 14.424  51.102  1.00 20.58 ? 29  ALA B N   1 
ATOM   202  C CA  . ALA A 1 29  ? 26.948 13.470  52.163  1.00 19.26 ? 29  ALA B CA  1 
ATOM   203  C C   . ALA A 1 29  ? 28.197 12.705  52.598  1.00 19.31 ? 29  ALA B C   1 
ATOM   204  O O   . ALA A 1 29  ? 28.455 12.539  53.799  1.00 16.07 ? 29  ALA B O   1 
ATOM   205  C CB  . ALA A 1 29  ? 25.855 12.510  51.695  1.00 19.14 ? 29  ALA B CB  1 
ATOM   206  N N   . LEU A 1 30  ? 28.978 12.222  51.632  1.00 17.66 ? 30  LEU B N   1 
ATOM   207  C CA  . LEU A 1 30  ? 30.222 11.532  51.948  1.00 14.05 ? 30  LEU B CA  1 
ATOM   208  C C   . LEU A 1 30  ? 31.184 12.454  52.679  1.00 16.45 ? 30  LEU B C   1 
ATOM   209  O O   . LEU A 1 30  ? 31.851 12.034  53.634  1.00 17.29 ? 30  LEU B O   1 
ATOM   210  C CB  . LEU A 1 30  ? 30.858 11.003  50.660  1.00 17.27 ? 30  LEU B CB  1 
ATOM   211  C CG  . LEU A 1 30  ? 30.054 9.914   49.944  1.00 15.77 ? 30  LEU B CG  1 
ATOM   212  C CD1 . LEU A 1 30  ? 30.507 9.813   48.498  1.00 18.83 ? 30  LEU B CD1 1 
ATOM   213  C CD2 . LEU A 1 30  ? 30.238 8.588   50.632  1.00 18.45 ? 30  LEU B CD2 1 
ATOM   214  N N   . GLU A 1 31  ? 31.249 13.723  52.262  1.00 17.90 ? 31  GLU B N   1 
ATOM   215  C CA  . GLU A 1 31  ? 32.175 14.668  52.876  1.00 18.78 ? 31  GLU B CA  1 
ATOM   216  C C   . GLU A 1 31  ? 31.747 15.021  54.294  1.00 21.28 ? 31  GLU B C   1 
ATOM   217  O O   . GLU A 1 31  ? 32.584 15.106  55.201  1.00 20.92 ? 31  GLU B O   1 
ATOM   218  C CB  . GLU A 1 31  ? 32.305 15.921  52.013  1.00 20.05 ? 31  GLU B CB  1 
ATOM   219  C CG  . GLU A 1 31  ? 33.089 15.667  50.732  1.00 17.28 ? 31  GLU B CG  1 
ATOM   220  C CD  . GLU A 1 31  ? 33.013 16.820  49.747  1.00 22.43 ? 31  GLU B CD  1 
ATOM   221  O OE1 . GLU A 1 31  ? 32.224 17.761  49.996  1.00 28.35 ? 31  GLU B OE1 1 
ATOM   222  O OE2 . GLU A 1 31  ? 33.748 16.785  48.731  1.00 24.45 ? 31  GLU B OE2 1 
ATOM   223  N N   . ASP A 1 32  ? 30.447 15.238  54.497  1.00 21.82 ? 32  ASP B N   1 
ATOM   224  C CA  . ASP A 1 32  ? 29.925 15.409  55.847  1.00 15.24 ? 32  ASP B CA  1 
ATOM   225  C C   . ASP A 1 32  ? 30.279 14.224  56.727  1.00 17.15 ? 32  ASP B C   1 
ATOM   226  O O   . ASP A 1 32  ? 30.519 14.398  57.930  1.00 21.70 ? 32  ASP B O   1 
ATOM   227  C CB  . ASP A 1 32  ? 28.411 15.561  55.794  1.00 17.27 ? 32  ASP B CB  1 
ATOM   228  C CG  . ASP A 1 32  ? 27.962 16.920  55.275  1.00 22.72 ? 32  ASP B CG  1 
ATOM   229  O OD1 . ASP A 1 32  ? 28.807 17.818  55.088  1.00 27.05 ? 32  ASP B OD1 1 
ATOM   230  O OD2 . ASP A 1 32  ? 26.740 17.078  55.052  1.00 27.08 ? 32  ASP B OD2 1 
ATOM   231  N N   . ALA A 1 33  ? 30.341 13.020  56.156  1.00 15.85 ? 33  ALA B N   1 
ATOM   232  C CA  . ALA A 1 33  ? 30.694 11.828  56.921  1.00 18.33 ? 33  ALA B CA  1 
ATOM   233  C C   . ALA A 1 33  ? 32.190 11.691  57.166  1.00 18.52 ? 33  ALA B C   1 
ATOM   234  O O   . ALA A 1 33  ? 32.602 10.754  57.865  1.00 19.14 ? 33  ALA B O   1 
ATOM   235  C CB  . ALA A 1 33  ? 30.154 10.561  56.254  1.00 19.81 ? 33  ALA B CB  1 
ATOM   236  N N   . GLY A 1 34  ? 33.003 12.595  56.623  1.00 17.12 ? 34  GLY B N   1 
ATOM   237  C CA  . GLY A 1 34  ? 34.441 12.570  56.809  1.00 16.35 ? 34  GLY B CA  1 
ATOM   238  C C   . GLY A 1 34  ? 35.240 12.026  55.644  1.00 17.73 ? 34  GLY B C   1 
ATOM   239  O O   . GLY A 1 34  ? 36.480 12.039  55.698  1.00 20.14 ? 34  GLY B O   1 
ATOM   240  N N   . ALA A 1 35  ? 34.576 11.549  54.595  1.00 21.21 ? 35  ALA B N   1 
ATOM   241  C CA  . ALA A 1 35  ? 35.255 10.989  53.438  1.00 19.61 ? 35  ALA B CA  1 
ATOM   242  C C   . ALA A 1 35  ? 35.724 12.090  52.488  1.00 17.85 ? 35  ALA B C   1 
ATOM   243  O O   . ALA A 1 35  ? 35.301 13.249  52.565  1.00 18.46 ? 35  ALA B O   1 
ATOM   244  C CB  . ALA A 1 35  ? 34.321 10.041  52.685  1.00 16.67 ? 35  ALA B CB  1 
ATOM   245  N N   . THR A 1 36  ? 36.588 11.694  51.557  1.00 16.78 ? 36  THR B N   1 
ATOM   246  C CA  . THR A 1 36  ? 37.135 12.565  50.526  1.00 16.61 ? 36  THR B CA  1 
ATOM   247  C C   . THR A 1 36  ? 36.586 12.101  49.180  1.00 22.07 ? 36  THR B C   1 
ATOM   248  O O   . THR A 1 36  ? 36.543 10.900  48.904  1.00 21.75 ? 36  THR B O   1 
ATOM   249  C CB  . THR A 1 36  ? 38.670 12.490  50.495  1.00 21.74 ? 36  THR B CB  1 
ATOM   250  O OG1 . THR A 1 36  ? 39.224 13.023  51.706  1.00 26.75 ? 36  THR B OG1 1 
ATOM   251  C CG2 . THR A 1 36  ? 39.214 13.289  49.329  1.00 27.36 ? 36  THR B CG2 1 
ATOM   252  N N   . VAL A 1 37  ? 36.163 13.045  48.340  1.00 15.24 ? 37  VAL B N   1 
ATOM   253  C CA  . VAL A 1 37  ? 35.566 12.713  47.050  1.00 19.69 ? 37  VAL B CA  1 
ATOM   254  C C   . VAL A 1 37  ? 36.386 13.361  45.946  1.00 21.29 ? 37  VAL B C   1 
ATOM   255  O O   . VAL A 1 37  ? 36.542 14.589  45.916  1.00 22.22 ? 37  VAL B O   1 
ATOM   256  C CB  . VAL A 1 37  ? 34.093 13.130  46.967  1.00 18.87 ? 37  VAL B CB  1 
ATOM   257  C CG1 . VAL A 1 37  ? 33.551 12.766  45.609  1.00 22.34 ? 37  VAL B CG1 1 
ATOM   258  C CG2 . VAL A 1 37  ? 33.315 12.426  48.042  1.00 18.92 ? 37  VAL B CG2 1 
ATOM   259  N N   . ARG A 1 38  ? 36.903 12.537  45.041  1.00 15.40 ? 38  ARG B N   1 
ATOM   260  C CA  . ARG A 1 38  ? 37.677 13.001  43.901  1.00 15.04 ? 38  ARG B CA  1 
ATOM   261  C C   . ARG A 1 38  ? 36.843 12.879  42.638  1.00 19.21 ? 38  ARG B C   1 
ATOM   262  O O   . ARG A 1 38  ? 36.150 11.880  42.437  1.00 15.17 ? 38  ARG B O   1 
ATOM   263  C CB  . ARG A 1 38  ? 38.944 12.172  43.722  1.00 17.82 ? 38  ARG B CB  1 
ATOM   264  C CG  . ARG A 1 38  ? 39.817 12.120  44.960  1.00 20.14 ? 38  ARG B CG  1 
ATOM   265  C CD  . ARG A 1 38  ? 40.308 13.490  45.299  1.00 22.37 ? 38  ARG B CD  1 
ATOM   266  N NE  . ARG A 1 38  ? 41.339 13.423  46.326  1.00 30.47 ? 38  ARG B NE  1 
ATOM   267  C CZ  . ARG A 1 38  ? 41.952 14.478  46.841  1.00 38.81 ? 38  ARG B CZ  1 
ATOM   268  N NH1 . ARG A 1 38  ? 41.657 15.706  46.451  1.00 37.82 ? 38  ARG B NH1 1 
ATOM   269  N NH2 . ARG A 1 38  ? 42.879 14.295  47.780  1.00 46.71 ? 38  ARG B NH2 1 
ATOM   270  N N   . ILE A 1 39  ? 36.890 13.910  41.815  1.00 15.39 ? 39  ILE B N   1 
ATOM   271  C CA  . ILE A 1 39  ? 36.150 13.945  40.564  1.00 20.56 ? 39  ILE B CA  1 
ATOM   272  C C   . ILE A 1 39  ? 37.121 13.546  39.458  1.00 19.96 ? 39  ILE B C   1 
ATOM   273  O O   . ILE A 1 39  ? 38.113 14.242  39.197  1.00 22.34 ? 39  ILE B O   1 
ATOM   274  C CB  . ILE A 1 39  ? 35.528 15.328  40.337  1.00 17.55 ? 39  ILE B CB  1 
ATOM   275  C CG1 . ILE A 1 39  ? 34.510 15.627  41.446  1.00 19.84 ? 39  ILE B CG1 1 
ATOM   276  C CG2 . ILE A 1 39  ? 34.875 15.404  38.958  1.00 18.93 ? 39  ILE B CG2 1 
ATOM   277  C CD1 . ILE A 1 39  ? 34.105 17.085  41.534  1.00 26.23 ? 39  ILE B CD1 1 
ATOM   278  N N   . LEU A 1 40  ? 36.863 12.403  38.831  1.00 16.06 ? 40  LEU B N   1 
ATOM   279  C CA  . LEU A 1 40  ? 37.692 11.882  37.755  1.00 15.14 ? 40  LEU B CA  1 
ATOM   280  C C   . LEU A 1 40  ? 36.926 11.943  36.449  1.00 17.90 ? 40  LEU B C   1 
ATOM   281  O O   . LEU A 1 40  ? 35.754 11.578  36.399  1.00 14.63 ? 40  LEU B O   1 
ATOM   282  C CB  . LEU A 1 40  ? 38.060 10.425  38.007  1.00 18.54 ? 40  LEU B CB  1 
ATOM   283  C CG  . LEU A 1 40  ? 38.800 10.119  39.301  1.00 16.63 ? 40  LEU B CG  1 
ATOM   284  C CD1 . LEU A 1 40  ? 39.269 8.670   39.266  1.00 17.66 ? 40  LEU B CD1 1 
ATOM   285  C CD2 . LEU A 1 40  ? 39.976 11.082  39.476  1.00 20.07 ? 40  LEU B CD2 1 
ATOM   286  N N   A SER A 1 41  ? 37.603 12.373  35.387  0.76 17.19 ? 41  SER B N   1 
ATOM   287  N N   B SER A 1 41  ? 37.600 12.379  35.390  0.24 17.25 ? 41  SER B N   1 
ATOM   288  C CA  A SER A 1 41  ? 36.960 12.494  34.091  0.76 18.04 ? 41  SER B CA  1 
ATOM   289  C CA  B SER A 1 41  ? 36.978 12.520  34.084  0.24 18.09 ? 41  SER B CA  1 
ATOM   290  C C   A SER A 1 41  ? 37.881 11.919  33.023  0.76 19.05 ? 41  SER B C   1 
ATOM   291  C C   B SER A 1 41  ? 37.876 11.899  33.024  0.24 19.04 ? 41  SER B C   1 
ATOM   292  O O   A SER A 1 41  ? 38.989 11.460  33.307  0.76 19.76 ? 41  SER B O   1 
ATOM   293  O O   B SER A 1 41  ? 38.956 11.380  33.317  0.24 19.76 ? 41  SER B O   1 
ATOM   294  C CB  A SER A 1 41  ? 36.540 13.943  33.806  0.76 22.57 ? 41  SER B CB  1 
ATOM   295  C CB  B SER A 1 41  ? 36.678 13.991  33.773  0.24 22.43 ? 41  SER B CB  1 
ATOM   296  O OG  A SER A 1 41  ? 35.556 13.992  32.780  0.76 15.80 ? 41  SER B OG  1 
ATOM   297  O OG  B SER A 1 41  ? 35.791 14.532  34.733  0.24 21.35 ? 41  SER B OG  1 
ATOM   298  N N   . ASP A 1 42  ? 37.419 11.947  31.773  1.00 18.88 ? 42  ASP B N   1 
ATOM   299  C CA  . ASP A 1 42  ? 38.232 11.447  30.677  1.00 20.93 ? 42  ASP B CA  1 
ATOM   300  C C   . ASP A 1 42  ? 39.277 12.464  30.232  1.00 22.04 ? 42  ASP B C   1 
ATOM   301  O O   . ASP A 1 42  ? 40.274 12.080  29.608  1.00 23.49 ? 42  ASP B O   1 
ATOM   302  C CB  . ASP A 1 42  ? 37.323 11.050  29.509  1.00 21.36 ? 42  ASP B CB  1 
ATOM   303  C CG  . ASP A 1 42  ? 36.563 12.217  28.940  1.00 23.34 ? 42  ASP B CG  1 
ATOM   304  O OD1 . ASP A 1 42  ? 36.062 13.053  29.703  1.00 20.08 ? 42  ASP B OD1 1 
ATOM   305  O OD2 . ASP A 1 42  ? 36.449 12.290  27.698  1.00 30.58 ? 42  ASP B OD2 1 
ATOM   306  N N   . LYS A 1 43  ? 39.042 13.713  30.601  1.00 23.65 ? 43  LYS B N   1 
ATOM   307  C CA  . LYS A 1 43  ? 39.933 14.804  30.177  1.00 27.26 ? 43  LYS B CA  1 
ATOM   308  C C   . LYS A 1 43  ? 40.202 15.718  31.362  1.00 24.13 ? 43  LYS B C   1 
ATOM   309  O O   . LYS A 1 43  ? 39.330 15.900  32.183  1.00 25.38 ? 43  LYS B O   1 
ATOM   310  C CB  . LYS A 1 43  ? 39.296 15.667  29.083  1.00 32.28 ? 43  LYS B CB  1 
ATOM   311  C CG  . LYS A 1 43  ? 38.895 14.977  27.791  1.00 32.59 ? 43  LYS B CG  1 
ATOM   312  C CD  . LYS A 1 43  ? 38.258 15.940  26.814  1.00 39.59 ? 43  LYS B CD  1 
ATOM   313  C CE  . LYS A 1 43  ? 37.264 15.287  25.876  1.00 48.46 ? 43  LYS B CE  1 
ATOM   314  N NZ  . LYS A 1 43  ? 36.000 14.941  26.568  1.00 45.70 ? 43  LYS B NZ  1 
ATOM   315  N N   . ALA A 1 44  ? 41.412 16.255  31.397  1.00 28.42 ? 44  ALA B N   1 
ATOM   316  C CA  . ALA A 1 44  ? 41.777 17.197  32.462  1.00 25.51 ? 44  ALA B CA  1 
ATOM   317  C C   . ALA A 1 44  ? 41.047 18.529  32.331  1.00 22.48 ? 44  ALA B C   1 
ATOM   318  O O   . ALA A 1 44  ? 40.470 18.817  31.288  1.00 24.94 ? 44  ALA B O   1 
ATOM   319  C CB  . ALA A 1 44  ? 43.268 17.433  32.449  1.00 23.93 ? 44  ALA B CB  1 
ATOM   320  N N   . GLY A 1 45  ? 41.102 19.300  33.405  1.00 24.43 ? 45  GLY B N   1 
ATOM   321  C CA  . GLY A 1 45  ? 40.502 20.636  33.403  1.00 28.09 ? 45  GLY B CA  1 
ATOM   322  C C   . GLY A 1 45  ? 39.197 20.665  34.151  1.00 28.06 ? 45  GLY B C   1 
ATOM   323  O O   . GLY A 1 45  ? 39.208 20.557  35.377  1.00 23.34 ? 45  GLY B O   1 
ATOM   324  N N   . GLU A 1 46  ? 38.125 20.830  33.393  1.00 20.21 ? 46  GLU B N   1 
ATOM   325  C CA  . GLU A 1 46  ? 36.801 20.930  34.005  1.00 23.37 ? 46  GLU B CA  1 
ATOM   326  C C   . GLU A 1 46  ? 35.830 19.958  33.348  1.00 24.19 ? 46  GLU B C   1 
ATOM   327  O O   . GLU A 1 46  ? 35.998 19.655  32.189  1.00 23.97 ? 46  GLU B O   1 
ATOM   328  C CB  . GLU A 1 46  ? 36.289 22.351  33.876  1.00 30.35 ? 46  GLU B CB  1 
ATOM   329  C CG  . GLU A 1 46  ? 36.769 23.276  34.972  1.00 35.25 ? 46  GLU B CG  1 
ATOM   330  C CD  . GLU A 1 46  ? 36.415 24.713  34.644  1.00 45.47 ? 46  GLU B CD  1 
ATOM   331  O OE1 . GLU A 1 46  ? 36.315 25.019  33.442  1.00 48.31 ? 46  GLU B OE1 1 
ATOM   332  O OE2 . GLU A 1 46  ? 36.207 25.502  35.582  1.00 37.44 ? 46  GLU B OE2 1 
ATOM   333  N N   . VAL A 1 47  ? 34.851 19.526  34.124  1.00 26.52 ? 47  VAL B N   1 
ATOM   334  C CA  . VAL A 1 47  ? 33.801 18.607  33.616  1.00 21.72 ? 47  VAL B CA  1 
ATOM   335  C C   . VAL A 1 47  ? 32.475 19.321  33.838  1.00 24.83 ? 47  VAL B C   1 
ATOM   336  O O   . VAL A 1 47  ? 32.284 19.922  34.893  1.00 24.94 ? 47  VAL B O   1 
ATOM   337  C CB  . VAL A 1 47  ? 33.906 17.218  34.264  1.00 31.51 ? 47  VAL B CB  1 
ATOM   338  C CG1 . VAL A 1 47  ? 33.744 17.239  35.773  1.00 23.66 ? 47  VAL B CG1 1 
ATOM   339  C CG2 . VAL A 1 47  ? 32.981 16.213  33.606  1.00 26.36 ? 47  VAL B CG2 1 
ATOM   340  N N   . ARG A 1 48  ? 31.605 19.275  32.841  1.00 22.16 ? 48  ARG B N   1 
ATOM   341  C CA  . ARG A 1 48  ? 30.387 20.072  32.870  1.00 22.86 ? 48  ARG B CA  1 
ATOM   342  C C   . ARG A 1 48  ? 29.233 19.247  33.418  1.00 19.16 ? 48  ARG B C   1 
ATOM   343  O O   . ARG A 1 48  ? 28.819 18.254  32.809  1.00 18.89 ? 48  ARG B O   1 
ATOM   344  C CB  . ARG A 1 48  ? 30.051 20.569  31.466  1.00 21.56 ? 48  ARG B CB  1 
ATOM   345  C CG  . ARG A 1 48  ? 28.798 21.403  31.392  1.00 21.96 ? 48  ARG B CG  1 
ATOM   346  C CD  . ARG A 1 48  ? 28.939 22.764  32.065  1.00 24.80 ? 48  ARG B CD  1 
ATOM   347  N NE  . ARG A 1 48  ? 29.993 23.568  31.465  1.00 30.38 ? 48  ARG B NE  1 
ATOM   348  C CZ  . ARG A 1 48  ? 30.336 24.783  31.868  1.00 24.13 ? 48  ARG B CZ  1 
ATOM   349  N NH1 . ARG A 1 48  ? 29.677 25.404  32.829  1.00 24.93 ? 48  ARG B NH1 1 
ATOM   350  N NH2 . ARG A 1 48  ? 31.357 25.397  31.275  1.00 28.31 ? 48  ARG B NH2 1 
ATOM   351  N N   . GLY A 1 49  ? 28.719 19.652  34.566  1.00 14.04 ? 49  GLY B N   1 
ATOM   352  C CA  . GLY A 1 49  ? 27.488 19.080  35.036  1.00 19.32 ? 49  GLY B CA  1 
ATOM   353  C C   . GLY A 1 49  ? 26.295 19.660  34.309  1.00 18.01 ? 49  GLY B C   1 
ATOM   354  O O   . GLY A 1 49  ? 26.355 20.755  33.750  1.00 19.93 ? 49  GLY B O   1 
ATOM   355  N N   . TRP A 1 50  ? 25.203 18.901  34.321  1.00 15.37 ? 50  TRP B N   1 
ATOM   356  C CA  . TRP A 1 50  ? 23.974 19.304  33.665  1.00 18.40 ? 50  TRP B CA  1 
ATOM   357  C C   . TRP A 1 50  ? 22.842 19.185  34.662  1.00 14.06 ? 50  TRP B C   1 
ATOM   358  O O   . TRP A 1 50  ? 22.853 18.303  35.523  1.00 19.11 ? 50  TRP B O   1 
ATOM   359  C CB  . TRP A 1 50  ? 23.637 18.378  32.481  1.00 14.69 ? 50  TRP B CB  1 
ATOM   360  C CG  . TRP A 1 50  ? 24.351 18.704  31.192  1.00 17.31 ? 50  TRP B CG  1 
ATOM   361  C CD1 . TRP A 1 50  ? 25.667 18.982  31.035  1.00 22.32 ? 50  TRP B CD1 1 
ATOM   362  C CD2 . TRP A 1 50  ? 23.769 18.766  29.883  1.00 16.39 ? 50  TRP B CD2 1 
ATOM   363  N NE1 . TRP A 1 50  ? 25.950 19.224  29.716  1.00 17.66 ? 50  TRP B NE1 1 
ATOM   364  C CE2 . TRP A 1 50  ? 24.797 19.093  28.986  1.00 23.45 ? 50  TRP B CE2 1 
ATOM   365  C CE3 . TRP A 1 50  ? 22.473 18.582  29.391  1.00 25.29 ? 50  TRP B CE3 1 
ATOM   366  C CZ2 . TRP A 1 50  ? 24.574 19.242  27.617  1.00 18.69 ? 50  TRP B CZ2 1 
ATOM   367  C CZ3 . TRP A 1 50  ? 22.251 18.730  28.033  1.00 18.42 ? 50  TRP B CZ3 1 
ATOM   368  C CH2 . TRP A 1 50  ? 23.297 19.058  27.161  1.00 22.91 ? 50  TRP B CH2 1 
ATOM   369  N N   . ASN A 1 51  ? 21.845 20.052  34.510  1.00 16.20 ? 51  ASN B N   1 
ATOM   370  C CA  . ASN A 1 51  ? 20.622 19.971  35.299  1.00 16.03 ? 51  ASN B CA  1 
ATOM   371  C C   . ASN A 1 51  ? 19.526 19.529  34.344  1.00 21.56 ? 51  ASN B C   1 
ATOM   372  O O   . ASN A 1 51  ? 19.040 20.324  33.538  1.00 19.89 ? 51  ASN B O   1 
ATOM   373  C CB  . ASN A 1 51  ? 20.309 21.299  35.978  1.00 20.92 ? 51  ASN B CB  1 
ATOM   374  C CG  . ASN A 1 51  ? 21.259 21.600  37.093  1.00 23.66 ? 51  ASN B CG  1 
ATOM   375  O OD1 . ASN A 1 51  ? 21.721 20.693  37.782  1.00 26.21 ? 51  ASN B OD1 1 
ATOM   376  N ND2 . ASN A 1 51  ? 21.566 22.877  37.282  1.00 21.98 ? 51  ASN B ND2 1 
ATOM   377  N N   . HIS A 1 52  ? 19.156 18.253  34.436  1.00 23.43 ? 52  HIS B N   1 
ATOM   378  C CA  . HIS A 1 52  ? 18.268 17.622  33.470  1.00 20.67 ? 52  HIS B CA  1 
ATOM   379  C C   . HIS A 1 52  ? 18.805 17.849  32.065  1.00 27.81 ? 52  HIS B C   1 
ATOM   380  O O   . HIS A 1 52  ? 19.863 17.321  31.708  1.00 23.27 ? 52  HIS B O   1 
ATOM   381  C CB  . HIS A 1 52  ? 16.830 18.137  33.601  1.00 26.08 ? 52  HIS B CB  1 
ATOM   382  C CG  . HIS A 1 52  ? 15.834 17.332  32.826  1.00 25.73 ? 52  HIS B CG  1 
ATOM   383  N ND1 . HIS A 1 52  ? 15.741 15.960  32.938  1.00 31.07 ? 52  HIS B ND1 1 
ATOM   384  C CD2 . HIS A 1 52  ? 14.885 17.704  31.935  1.00 23.49 ? 52  HIS B CD2 1 
ATOM   385  C CE1 . HIS A 1 52  ? 14.780 15.523  32.143  1.00 29.17 ? 52  HIS B CE1 1 
ATOM   386  N NE2 . HIS A 1 52  ? 14.244 16.560  31.525  1.00 30.94 ? 52  HIS B NE2 1 
ATOM   387  N N   . HIS A 1 53  ? 18.114 18.665  31.273  1.00 24.63 ? 53  HIS B N   1 
ATOM   388  C CA  . HIS A 1 53  ? 18.468 18.859  29.873  1.00 22.34 ? 53  HIS B CA  1 
ATOM   389  C C   . HIS A 1 53  ? 19.152 20.196  29.587  1.00 23.80 ? 53  HIS B C   1 
ATOM   390  O O   . HIS A 1 53  ? 19.087 20.698  28.462  1.00 26.34 ? 53  HIS B O   1 
ATOM   391  C CB  . HIS A 1 53  ? 17.251 18.657  28.968  1.00 23.00 ? 53  HIS B CB  1 
ATOM   392  C CG  . HIS A 1 53  ? 16.712 17.263  28.984  1.00 26.41 ? 53  HIS B CG  1 
ATOM   393  N ND1 . HIS A 1 53  ? 15.512 16.923  28.399  1.00 20.34 ? 53  HIS B ND1 1 
ATOM   394  C CD2 . HIS A 1 53  ? 17.230 16.112  29.474  1.00 19.31 ? 53  HIS B CD2 1 
ATOM   395  C CE1 . HIS A 1 53  ? 15.301 15.629  28.551  1.00 24.15 ? 53  HIS B CE1 1 
ATOM   396  N NE2 . HIS A 1 53  ? 16.330 15.112  29.197  1.00 20.09 ? 53  HIS B NE2 1 
ATOM   397  N N   . GLN A 1 54  ? 19.847 20.769  30.573  1.00 26.65 ? 54  GLN B N   1 
ATOM   398  C CA  . GLN A 1 54  ? 20.577 22.017  30.367  1.00 27.20 ? 54  GLN B CA  1 
ATOM   399  C C   . GLN A 1 54  ? 21.949 21.856  31.005  1.00 17.87 ? 54  GLN B C   1 
ATOM   400  O O   . GLN A 1 54  ? 22.043 21.396  32.155  1.00 22.31 ? 54  GLN B O   1 
ATOM   401  C CB  . GLN A 1 54  ? 19.887 23.227  30.982  1.00 30.96 ? 54  GLN B CB  1 
ATOM   402  C CG  . GLN A 1 54  ? 19.209 24.135  29.993  1.00 32.57 ? 54  GLN B CG  1 
ATOM   403  C CD  . GLN A 1 54  ? 18.151 24.991  30.646  1.00 42.13 ? 54  GLN B CD  1 
ATOM   404  O OE1 . GLN A 1 54  ? 17.130 24.493  31.123  1.00 44.41 ? 54  GLN B OE1 1 
ATOM   405  N NE2 . GLN A 1 54  ? 18.404 26.295  30.696  1.00 40.34 ? 54  GLN B NE2 1 
ATOM   406  N N   . PRO A 1 55  ? 23.016 22.249  30.326  1.00 23.35 ? 55  PRO B N   1 
ATOM   407  C CA  . PRO A 1 55  ? 24.325 22.225  30.975  1.00 22.12 ? 55  PRO B CA  1 
ATOM   408  C C   . PRO A 1 55  ? 24.312 23.233  32.109  1.00 23.17 ? 55  PRO B C   1 
ATOM   409  O O   . PRO A 1 55  ? 23.610 24.250  32.058  1.00 27.65 ? 55  PRO B O   1 
ATOM   410  C CB  . PRO A 1 55  ? 25.283 22.649  29.861  1.00 26.48 ? 55  PRO B CB  1 
ATOM   411  C CG  . PRO A 1 55  ? 24.532 22.463  28.597  1.00 28.20 ? 55  PRO B CG  1 
ATOM   412  C CD  . PRO A 1 55  ? 23.099 22.701  28.928  1.00 25.93 ? 55  PRO B CD  1 
ATOM   413  N N   . ALA A 1 56  ? 25.047 22.910  33.170  1.00 21.50 ? 56  ALA B N   1 
ATOM   414  C CA  . ALA A 1 56  ? 25.031 23.738  34.365  1.00 24.55 ? 56  ALA B CA  1 
ATOM   415  C C   . ALA A 1 56  ? 26.454 24.112  34.767  1.00 24.07 ? 56  ALA B C   1 
ATOM   416  O O   . ALA A 1 56  ? 27.198 24.672  33.952  1.00 24.47 ? 56  ALA B O   1 
ATOM   417  C CB  . ALA A 1 56  ? 24.271 23.027  35.486  1.00 24.15 ? 56  ALA B CB  1 
ATOM   418  N N   . GLU A 1 57  ? 26.852 23.807  35.999  1.00 20.31 ? 57  GLU B N   1 
ATOM   419  C CA  . GLU A 1 57  ? 28.130 24.289  36.498  1.00 18.89 ? 57  GLU B CA  1 
ATOM   420  C C   . GLU A 1 57  ? 29.278 23.365  36.110  1.00 23.66 ? 57  GLU B C   1 
ATOM   421  O O   . GLU A 1 57  ? 29.096 22.175  35.849  1.00 23.78 ? 57  GLU B O   1 
ATOM   422  C CB  . GLU A 1 57  ? 28.075 24.456  38.012  1.00 26.52 ? 57  GLU B CB  1 
ATOM   423  C CG  . GLU A 1 57  ? 27.032 25.474  38.413  1.00 27.36 ? 57  GLU B CG  1 
ATOM   424  C CD  . GLU A 1 57  ? 26.839 25.527  39.885  1.00 26.18 ? 57  GLU B CD  1 
ATOM   425  O OE1 . GLU A 1 57  ? 27.783 25.971  40.567  1.00 28.61 ? 57  GLU B OE1 1 
ATOM   426  O OE2 . GLU A 1 57  ? 25.753 25.119  40.356  1.00 31.94 ? 57  GLU B OE2 1 
ATOM   427  N N   . ALA A 1 58  ? 30.478 23.942  36.088  1.00 22.75 ? 58  ALA B N   1 
ATOM   428  C CA  . ALA A 1 58  ? 31.717 23.245  35.778  1.00 20.48 ? 58  ALA B CA  1 
ATOM   429  C C   . ALA A 1 58  ? 32.405 22.814  37.067  1.00 22.60 ? 58  ALA B C   1 
ATOM   430  O O   . ALA A 1 58  ? 32.349 23.508  38.087  1.00 26.07 ? 58  ALA B O   1 
ATOM   431  C CB  . ALA A 1 58  ? 32.660 24.158  34.997  1.00 26.66 ? 58  ALA B CB  1 
ATOM   432  N N   . PHE A 1 59  ? 33.063 21.660  37.012  1.00 24.79 ? 59  PHE B N   1 
ATOM   433  C CA  . PHE A 1 59  ? 33.698 21.077  38.186  1.00 23.08 ? 59  PHE B CA  1 
ATOM   434  C C   . PHE A 1 59  ? 35.145 20.733  37.886  1.00 20.08 ? 59  PHE B C   1 
ATOM   435  O O   . PHE A 1 59  ? 35.460 20.217  36.810  1.00 23.76 ? 59  PHE B O   1 
ATOM   436  C CB  . PHE A 1 59  ? 32.956 19.820  38.623  1.00 25.22 ? 59  PHE B CB  1 
ATOM   437  C CG  . PHE A 1 59  ? 31.599 20.098  39.165  1.00 19.51 ? 59  PHE B CG  1 
ATOM   438  C CD1 . PHE A 1 59  ? 30.533 20.365  38.323  1.00 23.83 ? 59  PHE B CD1 1 
ATOM   439  C CD2 . PHE A 1 59  ? 31.393 20.129  40.531  1.00 20.44 ? 59  PHE B CD2 1 
ATOM   440  C CE1 . PHE A 1 59  ? 29.292 20.644  38.844  1.00 20.17 ? 59  PHE B CE1 1 
ATOM   441  C CE2 . PHE A 1 59  ? 30.156 20.402  41.050  1.00 18.96 ? 59  PHE B CE2 1 
ATOM   442  C CZ  . PHE A 1 59  ? 29.102 20.654  40.212  1.00 17.22 ? 59  PHE B CZ  1 
ATOM   443  N N   . ARG A 1 60  ? 36.028 20.995  38.844  1.00 21.78 ? 60  ARG B N   1 
ATOM   444  C CA  . ARG A 1 60  ? 37.434 20.709  38.611  1.00 22.47 ? 60  ARG B CA  1 
ATOM   445  C C   . ARG A 1 60  ? 37.656 19.202  38.544  1.00 24.38 ? 60  ARG B C   1 
ATOM   446  O O   . ARG A 1 60  ? 37.130 18.443  39.362  1.00 23.88 ? 60  ARG B O   1 
ATOM   447  C CB  . ARG A 1 60  ? 38.320 21.327  39.693  1.00 31.81 ? 60  ARG B CB  1 
ATOM   448  C CG  . ARG A 1 60  ? 39.808 21.170  39.373  1.00 34.95 ? 60  ARG B CG  1 
ATOM   449  C CD  . ARG A 1 60  ? 40.665 20.903  40.591  1.00 42.16 ? 60  ARG B CD  1 
ATOM   450  N NE  . ARG A 1 60  ? 40.304 21.752  41.720  1.00 55.65 ? 60  ARG B NE  1 
ATOM   451  C CZ  . ARG A 1 60  ? 40.084 21.308  42.949  1.00 51.60 ? 60  ARG B CZ  1 
ATOM   452  N NH1 . ARG A 1 60  ? 40.200 20.025  43.251  1.00 46.21 ? 60  ARG B NH1 1 
ATOM   453  N NH2 . ARG A 1 60  ? 39.741 22.173  43.899  1.00 50.01 ? 60  ARG B NH2 1 
ATOM   454  N N   . VAL A 1 61  ? 38.411 18.771  37.543  1.00 20.75 ? 61  VAL B N   1 
ATOM   455  C CA  . VAL A 1 61  ? 38.794 17.374  37.389  1.00 21.04 ? 61  VAL B CA  1 
ATOM   456  C C   . VAL A 1 61  ? 40.045 17.144  38.227  1.00 23.32 ? 61  VAL B C   1 
ATOM   457  O O   . VAL A 1 61  ? 41.056 17.830  38.053  1.00 24.32 ? 61  VAL B O   1 
ATOM   458  C CB  . VAL A 1 61  ? 39.044 17.041  35.909  1.00 14.69 ? 61  VAL B CB  1 
ATOM   459  C CG1 . VAL A 1 61  ? 39.489 15.601  35.751  1.00 19.30 ? 61  VAL B CG1 1 
ATOM   460  C CG2 . VAL A 1 61  ? 37.779 17.308  35.100  1.00 20.98 ? 61  VAL B CG2 1 
ATOM   461  N N   . ASP A 1 62  ? 39.969 16.194  39.159  1.00 23.15 ? 62  ASP B N   1 
ATOM   462  C CA  . ASP A 1 62  ? 41.115 15.875  40.005  1.00 19.96 ? 62  ASP B CA  1 
ATOM   463  C C   . ASP A 1 62  ? 42.112 14.951  39.320  1.00 23.12 ? 62  ASP B C   1 
ATOM   464  O O   . ASP A 1 62  ? 43.285 14.913  39.716  1.00 23.34 ? 62  ASP B O   1 
ATOM   465  C CB  . ASP A 1 62  ? 40.620 15.255  41.311  1.00 21.83 ? 62  ASP B CB  1 
ATOM   466  C CG  . ASP A 1 62  ? 39.826 16.231  42.146  1.00 29.63 ? 62  ASP B CG  1 
ATOM   467  O OD1 . ASP A 1 62  ? 40.374 17.313  42.451  1.00 32.71 ? 62  ASP B OD1 1 
ATOM   468  O OD2 . ASP A 1 62  ? 38.664 15.929  42.503  1.00 19.20 ? 62  ASP B OD2 1 
ATOM   469  N N   . GLY A 1 63  ? 41.682 14.233  38.296  1.00 25.29 ? 63  GLY B N   1 
ATOM   470  C CA  . GLY A 1 63  ? 42.524 13.264  37.638  1.00 19.67 ? 63  GLY B CA  1 
ATOM   471  C C   . GLY A 1 63  ? 41.751 12.638  36.499  1.00 17.84 ? 63  GLY B C   1 
ATOM   472  O O   . GLY A 1 63  ? 40.517 12.675  36.468  1.00 20.16 ? 63  GLY B O   1 
ATOM   473  N N   . THR A 1 64  ? 42.497 12.060  35.560  1.00 19.60 ? 64  THR B N   1 
ATOM   474  C CA  . THR A 1 64  ? 41.875 11.415  34.413  1.00 19.52 ? 64  THR B CA  1 
ATOM   475  C C   . THR A 1 64  ? 41.797 9.910   34.614  1.00 20.24 ? 64  THR B C   1 
ATOM   476  O O   . THR A 1 64  ? 42.558 9.326   35.390  1.00 19.80 ? 64  THR B O   1 
ATOM   477  C CB  . THR A 1 64  ? 42.619 11.685  33.107  1.00 24.21 ? 64  THR B CB  1 
ATOM   478  O OG1 . THR A 1 64  ? 43.946 11.156  33.211  1.00 18.71 ? 64  THR B OG1 1 
ATOM   479  C CG2 . THR A 1 64  ? 42.656 13.178  32.810  1.00 31.37 ? 64  THR B CG2 1 
ATOM   480  N N   . PHE A 1 65  ? 40.837 9.289   33.918  1.00 18.71 ? 65  PHE B N   1 
ATOM   481  C CA  . PHE A 1 65  ? 40.738 7.833   33.933  1.00 18.80 ? 65  PHE B CA  1 
ATOM   482  C C   . PHE A 1 65  ? 42.057 7.201   33.516  1.00 20.43 ? 65  PHE B C   1 
ATOM   483  O O   . PHE A 1 65  ? 42.447 6.153   34.036  1.00 20.09 ? 65  PHE B O   1 
ATOM   484  C CB  . PHE A 1 65  ? 39.637 7.368   32.974  1.00 18.90 ? 65  PHE B CB  1 
ATOM   485  C CG  . PHE A 1 65  ? 38.285 7.985   33.236  1.00 17.16 ? 65  PHE B CG  1 
ATOM   486  C CD1 . PHE A 1 65  ? 37.841 8.227   34.521  1.00 18.56 ? 65  PHE B CD1 1 
ATOM   487  C CD2 . PHE A 1 65  ? 37.450 8.304   32.181  1.00 16.53 ? 65  PHE B CD2 1 
ATOM   488  C CE1 . PHE A 1 65  ? 36.589 8.794   34.748  1.00 19.26 ? 65  PHE B CE1 1 
ATOM   489  C CE2 . PHE A 1 65  ? 36.203 8.871   32.402  1.00 17.45 ? 65  PHE B CE2 1 
ATOM   490  C CZ  . PHE A 1 65  ? 35.769 9.107   33.689  1.00 20.08 ? 65  PHE B CZ  1 
ATOM   491  N N   . GLU A 1 66  ? 42.737 7.818   32.547  1.00 20.91 ? 66  GLU B N   1 
ATOM   492  C CA  . GLU A 1 66  ? 43.991 7.281   32.036  1.00 22.70 ? 66  GLU B CA  1 
ATOM   493  C C   . GLU A 1 66  ? 45.038 7.178   33.137  1.00 22.36 ? 66  GLU B C   1 
ATOM   494  O O   . GLU A 1 66  ? 45.784 6.195   33.203  1.00 27.90 ? 66  GLU B O   1 
ATOM   495  C CB  . GLU A 1 66  ? 44.484 8.192   30.910  1.00 26.27 ? 66  GLU B CB  1 
ATOM   496  C CG  . GLU A 1 66  ? 45.736 7.720   30.159  1.00 30.41 ? 66  GLU B CG  1 
ATOM   497  C CD  . GLU A 1 66  ? 45.481 6.493   29.299  1.00 33.61 ? 66  GLU B CD  1 
ATOM   498  O OE1 . GLU A 1 66  ? 44.496 6.498   28.529  1.00 42.65 ? 66  GLU B OE1 1 
ATOM   499  O OE2 . GLU A 1 66  ? 46.273 5.533   29.370  1.00 41.95 ? 66  GLU B OE2 1 
ATOM   500  N N   . ASP A 1 67  ? 45.088 8.170   34.031  1.00 26.00 ? 67  ASP B N   1 
ATOM   501  C CA  . ASP A 1 67  ? 46.104 8.241   35.075  1.00 26.42 ? 67  ASP B CA  1 
ATOM   502  C C   . ASP A 1 67  ? 45.692 7.582   36.383  1.00 18.20 ? 67  ASP B C   1 
ATOM   503  O O   . ASP A 1 67  ? 46.543 7.427   37.267  1.00 25.57 ? 67  ASP B O   1 
ATOM   504  C CB  . ASP A 1 67  ? 46.475 9.702   35.360  1.00 24.77 ? 67  ASP B CB  1 
ATOM   505  C CG  . ASP A 1 67  ? 47.087 10.391  34.152  1.00 23.81 ? 67  ASP B CG  1 
ATOM   506  O OD1 . ASP A 1 67  ? 47.589 9.669   33.267  1.00 27.54 ? 67  ASP B OD1 1 
ATOM   507  O OD2 . ASP A 1 67  ? 47.057 11.642  34.089  1.00 27.64 ? 67  ASP B OD2 1 
ATOM   508  N N   . ALA A 1 68  ? 44.431 7.191   36.539  1.00 20.53 ? 68  ALA B N   1 
ATOM   509  C CA  . ALA A 1 68  ? 43.912 6.819   37.849  1.00 15.94 ? 68  ALA B CA  1 
ATOM   510  C C   . ALA A 1 68  ? 44.264 5.388   38.222  1.00 17.03 ? 68  ALA B C   1 
ATOM   511  O O   . ALA A 1 68  ? 44.247 4.480   37.389  1.00 23.66 ? 68  ALA B O   1 
ATOM   512  C CB  . ALA A 1 68  ? 42.387 6.965   37.856  1.00 22.76 ? 68  ALA B CB  1 
ATOM   513  N N   . SER A 1 69  ? 44.544 5.181   39.501  1.00 19.61 ? 69  SER B N   1 
ATOM   514  C CA  . SER A 1 69  ? 44.690 3.846   40.056  1.00 19.82 ? 69  SER B CA  1 
ATOM   515  C C   . SER A 1 69  ? 43.636 3.622   41.123  1.00 19.56 ? 69  SER B C   1 
ATOM   516  O O   . SER A 1 69  ? 43.391 4.497   41.958  1.00 23.05 ? 69  SER B O   1 
ATOM   517  C CB  . SER A 1 69  ? 46.065 3.660   40.683  1.00 23.10 ? 69  SER B CB  1 
ATOM   518  O OG  . SER A 1 69  ? 46.164 2.363   41.255  1.00 27.77 ? 69  SER B OG  1 
ATOM   519  N N   . LEU A 1 70  ? 43.004 2.449   41.088  1.00 21.54 ? 70  LEU B N   1 
ATOM   520  C CA  . LEU A 1 70  ? 42.050 2.130   42.140  1.00 16.68 ? 70  LEU B CA  1 
ATOM   521  C C   . LEU A 1 70  ? 42.716 1.897   43.479  1.00 23.58 ? 70  LEU B C   1 
ATOM   522  O O   . LEU A 1 70  ? 42.031 1.914   44.506  1.00 19.48 ? 70  LEU B O   1 
ATOM   523  C CB  . LEU A 1 70  ? 41.191 0.932   41.775  1.00 21.97 ? 70  LEU B CB  1 
ATOM   524  C CG  . LEU A 1 70  ? 39.825 1.091   42.421  1.00 23.55 ? 70  LEU B CG  1 
ATOM   525  C CD1 . LEU A 1 70  ? 39.146 2.362   41.960  1.00 20.58 ? 70  LEU B CD1 1 
ATOM   526  C CD2 . LEU A 1 70  ? 39.017 -0.097  42.065  1.00 24.36 ? 70  LEU B CD2 1 
ATOM   527  N N   . ASP A 1 71  ? 44.029 1.689   43.497  1.00 20.58 ? 71  ASP B N   1 
ATOM   528  C CA  . ASP A 1 71  ? 44.712 1.567   44.773  1.00 19.78 ? 71  ASP B CA  1 
ATOM   529  C C   . ASP A 1 71  ? 44.375 2.725   45.691  1.00 19.91 ? 71  ASP B C   1 
ATOM   530  O O   . ASP A 1 71  ? 44.340 2.556   46.913  1.00 22.65 ? 71  ASP B O   1 
ATOM   531  C CB  . ASP A 1 71  ? 46.210 1.618   44.543  1.00 17.06 ? 71  ASP B CB  1 
ATOM   532  C CG  . ASP A 1 71  ? 46.756 0.362   43.919  1.00 27.58 ? 71  ASP B CG  1 
ATOM   533  O OD1 . ASP A 1 71  ? 46.020 -0.634  43.738  1.00 27.24 ? 71  ASP B OD1 1 
ATOM   534  O OD2 . ASP A 1 71  ? 47.956 0.394   43.596  1.00 19.16 ? 71  ASP B OD2 1 
ATOM   535  N N   . ASP A 1 72  ? 44.129 3.908   45.126  1.00 17.28 ? 72  ASP B N   1 
ATOM   536  C CA  . ASP A 1 72  ? 43.921 5.118   45.908  1.00 17.72 ? 72  ASP B CA  1 
ATOM   537  C C   . ASP A 1 72  ? 42.463 5.420   46.217  1.00 16.60 ? 72  ASP B C   1 
ATOM   538  O O   . ASP A 1 72  ? 42.178 6.494   46.761  1.00 24.02 ? 72  ASP B O   1 
ATOM   539  C CB  . ASP A 1 72  ? 44.562 6.320   45.228  1.00 20.73 ? 72  ASP B CB  1 
ATOM   540  C CG  . ASP A 1 72  ? 46.039 6.441   45.560  1.00 32.61 ? 72  ASP B CG  1 
ATOM   541  O OD1 . ASP A 1 72  ? 46.673 5.393   45.821  1.00 47.03 ? 72  ASP B OD1 1 
ATOM   542  O OD2 . ASP A 1 72  ? 46.567 7.575   45.549  1.00 29.78 ? 72  ASP B OD2 1 
ATOM   543  N N   . TYR A 1 73  ? 41.542 4.512   45.899  1.00 15.48 ? 73  TYR B N   1 
ATOM   544  C CA  . TYR A 1 73  ? 40.125 4.743   46.137  1.00 15.76 ? 73  TYR B CA  1 
ATOM   545  C C   . TYR A 1 73  ? 39.463 3.528   46.765  1.00 13.79 ? 73  TYR B C   1 
ATOM   546  O O   . TYR A 1 73  ? 39.674 2.390   46.339  1.00 16.71 ? 73  TYR B O   1 
ATOM   547  C CB  . TYR A 1 73  ? 39.418 5.096   44.824  1.00 11.79 ? 73  TYR B CB  1 
ATOM   548  C CG  . TYR A 1 73  ? 39.978 6.339   44.216  1.00 18.07 ? 73  TYR B CG  1 
ATOM   549  C CD1 . TYR A 1 73  ? 39.667 7.576   44.740  1.00 13.27 ? 73  TYR B CD1 1 
ATOM   550  C CD2 . TYR A 1 73  ? 40.865 6.275   43.148  1.00 21.68 ? 73  TYR B CD2 1 
ATOM   551  C CE1 . TYR A 1 73  ? 40.197 8.723   44.210  1.00 17.80 ? 73  TYR B CE1 1 
ATOM   552  C CE2 . TYR A 1 73  ? 41.406 7.420   42.603  1.00 19.39 ? 73  TYR B CE2 1 
ATOM   553  C CZ  . TYR A 1 73  ? 41.067 8.642   43.139  1.00 15.79 ? 73  TYR B CZ  1 
ATOM   554  O OH  . TYR A 1 73  ? 41.588 9.791   42.611  1.00 24.53 ? 73  TYR B OH  1 
ATOM   555  N N   . ASP A 1 74  ? 38.631 3.787   47.766  1.00 13.55 ? 74  ASP B N   1 
ATOM   556  C CA  . ASP A 1 74  ? 37.870 2.723   48.414  1.00 14.49 ? 74  ASP B CA  1 
ATOM   557  C C   . ASP A 1 74  ? 36.590 2.375   47.672  1.00 15.19 ? 74  ASP B C   1 
ATOM   558  O O   . ASP A 1 74  ? 36.018 1.303   47.911  1.00 16.57 ? 74  ASP B O   1 
ATOM   559  C CB  . ASP A 1 74  ? 37.534 3.123   49.848  1.00 14.16 ? 74  ASP B CB  1 
ATOM   560  C CG  . ASP A 1 74  ? 38.788 3.440   50.645  1.00 13.11 ? 74  ASP B CG  1 
ATOM   561  O OD1 . ASP A 1 74  ? 39.503 2.477   50.964  1.00 24.29 ? 74  ASP B OD1 1 
ATOM   562  O OD2 . ASP A 1 74  ? 39.061 4.633   50.911  1.00 17.72 ? 74  ASP B OD2 1 
ATOM   563  N N   . ALA A 1 75  ? 36.120 3.252   46.796  1.00 15.23 ? 75  ALA B N   1 
ATOM   564  C CA  . ALA A 1 75  ? 34.849 3.010   46.127  1.00 14.47 ? 75  ALA B CA  1 
ATOM   565  C C   . ALA A 1 75  ? 34.736 3.929   44.928  1.00 15.83 ? 75  ALA B C   1 
ATOM   566  O O   . ALA A 1 75  ? 35.465 4.916   44.794  1.00 14.71 ? 75  ALA B O   1 
ATOM   567  C CB  . ALA A 1 75  ? 33.655 3.222   47.067  1.00 13.82 ? 75  ALA B CB  1 
ATOM   568  N N   . LEU A 1 76  ? 33.794 3.586   44.059  1.00 14.86 ? 76  LEU B N   1 
ATOM   569  C CA  . LEU A 1 76  ? 33.442 4.393   42.907  1.00 15.63 ? 76  LEU B CA  1 
ATOM   570  C C   . LEU A 1 76  ? 32.037 4.932   43.091  1.00 14.37 ? 76  LEU B C   1 
ATOM   571  O O   . LEU A 1 76  ? 31.164 4.245   43.636  1.00 17.26 ? 76  LEU B O   1 
ATOM   572  C CB  . LEU A 1 76  ? 33.467 3.555   41.627  1.00 15.40 ? 76  LEU B CB  1 
ATOM   573  C CG  . LEU A 1 76  ? 34.863 3.061   41.242  1.00 15.27 ? 76  LEU B CG  1 
ATOM   574  C CD1 . LEU A 1 76  ? 34.764 2.197   39.986  1.00 15.72 ? 76  LEU B CD1 1 
ATOM   575  C CD2 . LEU A 1 76  ? 35.775 4.242   40.989  1.00 18.33 ? 76  LEU B CD2 1 
ATOM   576  N N   . LEU A 1 77  ? 31.833 6.170   42.653  1.00 14.29 ? 77  LEU B N   1 
ATOM   577  C CA  . LEU A 1 77  ? 30.506 6.758   42.550  1.00 18.85 ? 77  LEU B CA  1 
ATOM   578  C C   . LEU A 1 77  ? 30.265 7.044   41.075  1.00 16.88 ? 77  LEU B C   1 
ATOM   579  O O   . LEU A 1 77  ? 31.103 7.674   40.416  1.00 15.82 ? 77  LEU B O   1 
ATOM   580  C CB  . LEU A 1 77  ? 30.428 8.055   43.379  1.00 13.17 ? 77  LEU B CB  1 
ATOM   581  C CG  . LEU A 1 77  ? 29.274 8.986   43.028  1.00 13.37 ? 77  LEU B CG  1 
ATOM   582  C CD1 . LEU A 1 77  ? 27.947 8.364   43.454  1.00 14.24 ? 77  LEU B CD1 1 
ATOM   583  C CD2 . LEU A 1 77  ? 29.474 10.348  43.660  1.00 18.16 ? 77  LEU B CD2 1 
ATOM   584  N N   . LEU A 1 78  ? 29.135 6.559   40.544  1.00 14.98 ? 78  LEU B N   1 
ATOM   585  C CA  . LEU A 1 78  ? 28.812 6.688   39.121  1.00 18.05 ? 78  LEU B CA  1 
ATOM   586  C C   . LEU A 1 78  ? 27.531 7.500   38.996  1.00 11.32 ? 78  LEU B C   1 
ATOM   587  O O   . LEU A 1 78  ? 26.428 6.931   38.868  1.00 15.31 ? 78  LEU B O   1 
ATOM   588  C CB  . LEU A 1 78  ? 28.645 5.329   38.446  1.00 16.65 ? 78  LEU B CB  1 
ATOM   589  C CG  . LEU A 1 78  ? 29.801 4.345   38.559  1.00 16.50 ? 78  LEU B CG  1 
ATOM   590  C CD1 . LEU A 1 78  ? 29.488 3.044   37.834  1.00 20.24 ? 78  LEU B CD1 1 
ATOM   591  C CD2 . LEU A 1 78  ? 31.068 5.001   38.011  1.00 17.19 ? 78  LEU B CD2 1 
ATOM   592  N N   . PRO A 1 79  ? 27.631 8.828   39.014  1.00 12.30 ? 79  PRO B N   1 
ATOM   593  C CA  . PRO A 1 79  ? 26.441 9.654   38.771  1.00 15.77 ? 79  PRO B CA  1 
ATOM   594  C C   . PRO A 1 79  ? 25.890 9.374   37.384  1.00 17.05 ? 79  PRO B C   1 
ATOM   595  O O   . PRO A 1 79  ? 26.577 8.856   36.501  1.00 15.44 ? 79  PRO B O   1 
ATOM   596  C CB  . PRO A 1 79  ? 26.979 11.091  38.855  1.00 15.99 ? 79  PRO B CB  1 
ATOM   597  C CG  . PRO A 1 79  ? 28.338 10.971  39.491  1.00 13.83 ? 79  PRO B CG  1 
ATOM   598  C CD  . PRO A 1 79  ? 28.857 9.636   39.087  1.00 13.67 ? 79  PRO B CD  1 
ATOM   599  N N   . GLY A 1 80  ? 24.623 9.714   37.201  1.00 14.93 ? 80  GLY B N   1 
ATOM   600  C CA  . GLY A 1 80  ? 23.997 9.485   35.916  1.00 17.45 ? 80  GLY B CA  1 
ATOM   601  C C   . GLY A 1 80  ? 24.049 10.673  34.984  1.00 19.94 ? 80  GLY B C   1 
ATOM   602  O O   . GLY A 1 80  ? 25.069 11.359  34.869  1.00 17.74 ? 80  GLY B O   1 
ATOM   603  N N   . GLY A 1 81  ? 22.927 10.918  34.325  1.00 14.61 ? 81  GLY B N   1 
ATOM   604  C CA  . GLY A 1 81  ? 22.840 11.832  33.201  1.00 19.83 ? 81  GLY B CA  1 
ATOM   605  C C   . GLY A 1 81  ? 22.875 11.054  31.896  1.00 16.35 ? 81  GLY B C   1 
ATOM   606  O O   . GLY A 1 81  ? 23.846 10.345  31.619  1.00 18.46 ? 81  GLY B O   1 
ATOM   607  N N   . VAL A 1 82  ? 21.824 11.154  31.083  1.00 18.26 ? 82  VAL B N   1 
ATOM   608  C CA  . VAL A 1 82  ? 21.774 10.335  29.871  1.00 15.76 ? 82  VAL B CA  1 
ATOM   609  C C   . VAL A 1 82  ? 22.956 10.624  28.939  1.00 18.54 ? 82  VAL B C   1 
ATOM   610  O O   . VAL A 1 82  ? 23.535 9.702   28.348  1.00 17.77 ? 82  VAL B O   1 
ATOM   611  C CB  . VAL A 1 82  ? 20.402 10.453  29.170  1.00 17.91 ? 82  VAL B CB  1 
ATOM   612  C CG1 . VAL A 1 82  ? 20.268 11.759  28.393  1.00 18.26 ? 82  VAL B CG1 1 
ATOM   613  C CG2 . VAL A 1 82  ? 20.171 9.256   28.260  1.00 14.77 ? 82  VAL B CG2 1 
ATOM   614  N N   . ILE A 1 83  ? 23.364 11.891  28.820  1.00 15.58 ? 83  ILE B N   1 
ATOM   615  C CA  . ILE A 1 83  ? 24.491 12.219  27.948  1.00 21.33 ? 83  ILE B CA  1 
ATOM   616  C C   . ILE A 1 83  ? 25.794 11.641  28.498  1.00 16.65 ? 83  ILE B C   1 
ATOM   617  O O   . ILE A 1 83  ? 26.532 10.960  27.785  1.00 17.58 ? 83  ILE B O   1 
ATOM   618  C CB  . ILE A 1 83  ? 24.577 13.736  27.709  1.00 21.94 ? 83  ILE B CB  1 
ATOM   619  C CG1 . ILE A 1 83  ? 23.453 14.192  26.777  1.00 26.89 ? 83  ILE B CG1 1 
ATOM   620  C CG2 . ILE A 1 83  ? 25.922 14.117  27.137  1.00 22.13 ? 83  ILE B CG2 1 
ATOM   621  C CD1 . ILE A 1 83  ? 23.412 15.681  26.569  1.00 26.55 ? 83  ILE B CD1 1 
ATOM   622  N N   . ASN A 1 84  ? 26.082 11.882  29.782  1.00 16.58 ? 84  ASN B N   1 
ATOM   623  C CA  . ASN A 1 84  ? 27.305 11.346  30.376  1.00 16.47 ? 84  ASN B CA  1 
ATOM   624  C C   . ASN A 1 84  ? 27.313 9.824   30.348  1.00 14.62 ? 84  ASN B C   1 
ATOM   625  O O   . ASN A 1 84  ? 28.301 9.200   29.940  1.00 12.97 ? 84  ASN B O   1 
ATOM   626  C CB  . ASN A 1 84  ? 27.443 11.836  31.823  1.00 18.92 ? 84  ASN B CB  1 
ATOM   627  C CG  . ASN A 1 84  ? 28.286 10.899  32.687  1.00 15.31 ? 84  ASN B CG  1 
ATOM   628  O OD1 . ASN A 1 84  ? 29.458 10.699  32.415  1.00 17.71 ? 84  ASN B OD1 1 
ATOM   629  N ND2 . ASN A 1 84  ? 27.681 10.324  33.732  1.00 15.89 ? 84  ASN B ND2 1 
ATOM   630  N N   . SER A 1 85  ? 26.232 9.206   30.824  1.00 15.72 ? 85  SER B N   1 
ATOM   631  C CA  . SER A 1 85  ? 26.217 7.751   30.978  1.00 13.77 ? 85  SER B CA  1 
ATOM   632  C C   . SER A 1 85  ? 26.420 7.050   29.645  1.00 16.68 ? 85  SER B C   1 
ATOM   633  O O   . SER A 1 85  ? 27.077 6.005   29.575  1.00 18.04 ? 85  SER B O   1 
ATOM   634  C CB  . SER A 1 85  ? 24.901 7.312   31.626  1.00 15.73 ? 85  SER B CB  1 
ATOM   635  O OG  . SER A 1 85  ? 24.727 7.937   32.901  1.00 13.78 ? 85  SER B OG  1 
ATOM   636  N N   . ASP A 1 86  ? 25.885 7.633   28.569  1.00 17.94 ? 86  ASP B N   1 
ATOM   637  C CA  . ASP A 1 86  ? 26.037 7.075   27.230  1.00 15.57 ? 86  ASP B CA  1 
ATOM   638  C C   . ASP A 1 86  ? 27.471 7.215   26.721  1.00 16.30 ? 86  ASP B C   1 
ATOM   639  O O   . ASP A 1 86  ? 27.994 6.305   26.066  1.00 17.86 ? 86  ASP B O   1 
ATOM   640  C CB  . ASP A 1 86  ? 25.026 7.772   26.319  1.00 12.88 ? 86  ASP B CB  1 
ATOM   641  C CG  . ASP A 1 86  ? 25.150 7.359   24.857  1.00 19.41 ? 86  ASP B CG  1 
ATOM   642  O OD1 . ASP A 1 86  ? 24.756 6.227   24.506  1.00 17.91 ? 86  ASP B OD1 1 
ATOM   643  O OD2 . ASP A 1 86  ? 25.624 8.203   24.064  1.00 17.75 ? 86  ASP B OD2 1 
ATOM   644  N N   . GLN A 1 87  ? 28.116 8.343   27.018  1.00 17.07 ? 87  GLN B N   1 
ATOM   645  C CA  . GLN A 1 87  ? 29.499 8.576   26.609  1.00 16.01 ? 87  GLN B CA  1 
ATOM   646  C C   . GLN A 1 87  ? 30.458 7.683   27.395  1.00 14.52 ? 87  GLN B C   1 
ATOM   647  O O   . GLN A 1 87  ? 31.334 7.029   26.812  1.00 17.10 ? 87  GLN B O   1 
ATOM   648  C CB  . GLN A 1 87  ? 29.855 10.040  26.905  1.00 19.64 ? 87  GLN B CB  1 
ATOM   649  C CG  . GLN A 1 87  ? 29.419 11.039  25.851  1.00 20.57 ? 87  GLN B CG  1 
ATOM   650  C CD  . GLN A 1 87  ? 29.387 12.498  26.350  1.00 17.01 ? 87  GLN B CD  1 
ATOM   651  O OE1 . GLN A 1 87  ? 29.034 13.409  25.580  1.00 23.06 ? 87  GLN B OE1 1 
ATOM   652  N NE2 . GLN A 1 87  ? 29.822 12.738  27.609  1.00 13.93 ? 87  GLN B NE2 1 
ATOM   653  N N   . ILE A 1 88  ? 30.317 7.666   28.729  1.00 16.81 ? 88  ILE B N   1 
ATOM   654  C CA  . ILE A 1 88  ? 31.327 7.057   29.596  1.00 16.07 ? 88  ILE B CA  1 
ATOM   655  C C   . ILE A 1 88  ? 31.376 5.541   29.437  1.00 13.95 ? 88  ILE B C   1 
ATOM   656  O O   . ILE A 1 88  ? 32.411 4.917   29.702  1.00 16.70 ? 88  ILE B O   1 
ATOM   657  C CB  . ILE A 1 88  ? 31.117 7.469   31.076  1.00 18.72 ? 88  ILE B CB  1 
ATOM   658  C CG1 . ILE A 1 88  ? 32.414 7.239   31.871  1.00 17.79 ? 88  ILE B CG1 1 
ATOM   659  C CG2 . ILE A 1 88  ? 29.959 6.676   31.707  1.00 18.00 ? 88  ILE B CG2 1 
ATOM   660  C CD1 . ILE A 1 88  ? 32.353 7.683   33.347  1.00 19.60 ? 88  ILE B CD1 1 
ATOM   661  N N   . ARG A 1 89  ? 30.274 4.919   29.005  1.00 16.51 ? 89  ARG B N   1 
ATOM   662  C CA  . ARG A 1 89  ? 30.201 3.460   28.997  1.00 14.39 ? 89  ARG B CA  1 
ATOM   663  C C   . ARG A 1 89  ? 31.216 2.828   28.042  1.00 14.07 ? 89  ARG B C   1 
ATOM   664  O O   . ARG A 1 89  ? 31.604 1.673   28.235  1.00 16.37 ? 89  ARG B O   1 
ATOM   665  C CB  . ARG A 1 89  ? 28.777 2.997   28.669  1.00 13.64 ? 89  ARG B CB  1 
ATOM   666  C CG  . ARG A 1 89  ? 28.416 3.135   27.189  1.00 14.19 ? 89  ARG B CG  1 
ATOM   667  C CD  . ARG A 1 89  ? 26.988 2.732   26.948  1.00 14.96 ? 89  ARG B CD  1 
ATOM   668  N NE  . ARG A 1 89  ? 26.753 1.309   27.163  1.00 12.60 ? 89  ARG B NE  1 
ATOM   669  C CZ  . ARG A 1 89  ? 25.576 0.744   26.930  1.00 12.54 ? 89  ARG B CZ  1 
ATOM   670  N NH1 . ARG A 1 89  ? 24.568 1.447   26.458  1.00 16.20 ? 89  ARG B NH1 1 
ATOM   671  N NH2 . ARG A 1 89  ? 25.419 -0.558  27.156  1.00 19.75 ? 89  ARG B NH2 1 
ATOM   672  N N   . SER A 1 90  ? 31.639 3.550   27.012  1.00 18.41 ? 90  SER B N   1 
ATOM   673  C CA  . SER A 1 90  ? 32.534 3.006   25.997  1.00 17.00 ? 90  SER B CA  1 
ATOM   674  C C   . SER A 1 90  ? 34.008 3.195   26.322  1.00 21.67 ? 90  SER B C   1 
ATOM   675  O O   . SER A 1 90  ? 34.858 2.628   25.625  1.00 20.26 ? 90  SER B O   1 
ATOM   676  C CB  . SER A 1 90  ? 32.255 3.672   24.654  1.00 15.48 ? 90  SER B CB  1 
ATOM   677  O OG  . SER A 1 90  ? 32.479 5.068   24.753  1.00 25.96 ? 90  SER B OG  1 
ATOM   678  N N   . LEU A 1 91  ? 34.333 3.984   27.342  1.00 17.63 ? 91  LEU B N   1 
ATOM   679  C CA  . LEU A 1 91  ? 35.721 4.306   27.652  1.00 16.96 ? 91  LEU B CA  1 
ATOM   680  C C   . LEU A 1 91  ? 36.349 3.145   28.411  1.00 17.67 ? 91  LEU B C   1 
ATOM   681  O O   . LEU A 1 91  ? 35.964 2.856   29.549  1.00 19.08 ? 91  LEU B O   1 
ATOM   682  C CB  . LEU A 1 91  ? 35.777 5.590   28.475  1.00 19.19 ? 91  LEU B CB  1 
ATOM   683  C CG  . LEU A 1 91  ? 35.118 6.807   27.818  1.00 21.58 ? 91  LEU B CG  1 
ATOM   684  C CD1 . LEU A 1 91  ? 35.235 8.058   28.697  1.00 20.73 ? 91  LEU B CD1 1 
ATOM   685  C CD2 . LEU A 1 91  ? 35.699 7.061   26.426  1.00 25.88 ? 91  LEU B CD2 1 
ATOM   686  N N   . ALA A 1 92  ? 37.337 2.495   27.789  1.00 20.14 ? 92  ALA B N   1 
ATOM   687  C CA  . ALA A 1 92  ? 37.930 1.305   28.387  1.00 20.93 ? 92  ALA B CA  1 
ATOM   688  C C   . ALA A 1 92  ? 38.537 1.610   29.749  1.00 19.86 ? 92  ALA B C   1 
ATOM   689  O O   . ALA A 1 92  ? 38.481 0.772   30.656  1.00 19.67 ? 92  ALA B O   1 
ATOM   690  C CB  . ALA A 1 92  ? 38.993 0.716   27.464  1.00 24.40 ? 92  ALA B CB  1 
ATOM   691  N N   . LYS A 1 93  ? 39.131 2.798   29.905  1.00 21.06 ? 93  LYS B N   1 
ATOM   692  C CA  . LYS A 1 93  ? 39.763 3.130   31.179  1.00 18.34 ? 93  LYS B CA  1 
ATOM   693  C C   . LYS A 1 93  ? 38.742 3.291   32.291  1.00 16.24 ? 93  LYS B C   1 
ATOM   694  O O   . LYS A 1 93  ? 39.036 2.960   33.441  1.00 22.66 ? 93  LYS B O   1 
ATOM   695  C CB  . LYS A 1 93  ? 40.641 4.371   31.049  1.00 23.94 ? 93  LYS B CB  1 
ATOM   696  C CG  . LYS A 1 93  ? 41.844 4.178   30.120  1.00 26.93 ? 93  LYS B CG  1 
ATOM   697  C CD  . LYS A 1 93  ? 42.818 3.159   30.690  1.00 32.83 ? 93  LYS B CD  1 
ATOM   698  C CE  . LYS A 1 93  ? 43.309 2.188   29.630  1.00 37.07 ? 93  LYS B CE  1 
ATOM   699  N NZ  . LYS A 1 93  ? 44.744 1.832   29.827  1.00 39.57 ? 93  LYS B NZ  1 
ATOM   700  N N   . ALA A 1 94  ? 37.539 3.780   31.967  1.00 18.05 ? 94  ALA B N   1 
ATOM   701  C CA  . ALA A 1 94  ? 36.467 3.813   32.960  1.00 16.37 ? 94  ALA B CA  1 
ATOM   702  C C   . ALA A 1 94  ? 35.967 2.407   33.271  1.00 15.91 ? 94  ALA B C   1 
ATOM   703  O O   . ALA A 1 94  ? 35.710 2.077   34.437  1.00 16.37 ? 94  ALA B O   1 
ATOM   704  C CB  . ALA A 1 94  ? 35.324 4.705   32.470  1.00 17.81 ? 94  ALA B CB  1 
ATOM   705  N N   . GLN A 1 95  ? 35.834 1.564   32.244  1.00 17.42 ? 95  GLN B N   1 
ATOM   706  C CA  . GLN A 1 95  ? 35.463 0.172   32.461  1.00 15.94 ? 95  GLN B CA  1 
ATOM   707  C C   . GLN A 1 95  ? 36.488 -0.534  33.331  1.00 20.76 ? 95  GLN B C   1 
ATOM   708  O O   . GLN A 1 95  ? 36.129 -1.275  34.258  1.00 19.48 ? 95  GLN B O   1 
ATOM   709  C CB  . GLN A 1 95  ? 35.354 -0.538  31.116  1.00 22.10 ? 95  GLN B CB  1 
ATOM   710  C CG  . GLN A 1 95  ? 34.283 0.005   30.207  1.00 17.30 ? 95  GLN B CG  1 
ATOM   711  C CD  . GLN A 1 95  ? 34.187 -0.788  28.917  1.00 18.31 ? 95  GLN B CD  1 
ATOM   712  O OE1 . GLN A 1 95  ? 34.937 -1.745  28.719  1.00 24.73 ? 95  GLN B OE1 1 
ATOM   713  N NE2 . GLN A 1 95  ? 33.303 -0.368  28.015  1.00 18.87 ? 95  GLN B NE2 1 
ATOM   714  N N   . GLU A 1 96  ? 37.771 -0.313  33.045  1.00 20.51 ? 96  GLU B N   1 
ATOM   715  C CA  . GLU A 1 96  ? 38.832 -0.924  33.835  1.00 20.71 ? 96  GLU B CA  1 
ATOM   716  C C   . GLU A 1 96  ? 38.706 -0.561  35.307  1.00 17.26 ? 96  GLU B C   1 
ATOM   717  O O   . GLU A 1 96  ? 38.839 -1.425  36.179  1.00 21.91 ? 96  GLU B O   1 
ATOM   718  C CB  . GLU A 1 96  ? 40.183 -0.473  33.289  1.00 25.83 ? 96  GLU B CB  1 
ATOM   719  C CG  . GLU A 1 96  ? 41.378 -1.011  34.052  1.00 31.47 ? 96  GLU B CG  1 
ATOM   720  C CD  . GLU A 1 96  ? 42.681 -0.670  33.360  1.00 35.80 ? 96  GLU B CD  1 
ATOM   721  O OE1 . GLU A 1 96  ? 42.691 -0.697  32.125  1.00 27.97 ? 96  GLU B OE1 1 
ATOM   722  O OE2 . GLU A 1 96  ? 43.680 -0.369  34.044  1.00 38.98 ? 96  GLU B OE2 1 
ATOM   723  N N   . LEU A 1 97  ? 38.460 0.716   35.601  1.00 16.70 ? 97  LEU B N   1 
ATOM   724  C CA  . LEU A 1 97  ? 38.362 1.138   36.991  1.00 17.72 ? 97  LEU B CA  1 
ATOM   725  C C   . LEU A 1 97  ? 37.225 0.410   37.687  1.00 17.66 ? 97  LEU B C   1 
ATOM   726  O O   . LEU A 1 97  ? 37.353 -0.023  38.838  1.00 17.83 ? 97  LEU B O   1 
ATOM   727  C CB  . LEU A 1 97  ? 38.138 2.645   37.038  1.00 20.36 ? 97  LEU B CB  1 
ATOM   728  C CG  . LEU A 1 97  ? 39.395 3.484   36.802  1.00 19.20 ? 97  LEU B CG  1 
ATOM   729  C CD1 . LEU A 1 97  ? 39.033 4.948   36.669  1.00 19.76 ? 97  LEU B CD1 1 
ATOM   730  C CD2 . LEU A 1 97  ? 40.401 3.259   37.930  1.00 22.30 ? 97  LEU B CD2 1 
ATOM   731  N N   . ALA A 1 98  ? 36.116 0.224   36.981  1.00 17.56 ? 98  ALA B N   1 
ATOM   732  C CA  . ALA A 1 98  ? 34.988 -0.484  37.566  1.00 14.43 ? 98  ALA B CA  1 
ATOM   733  C C   . ALA A 1 98  ? 35.280 -1.974  37.715  1.00 15.17 ? 98  ALA B C   1 
ATOM   734  O O   . ALA A 1 98  ? 34.871 -2.591  38.705  1.00 15.99 ? 98  ALA B O   1 
ATOM   735  C CB  . ALA A 1 98  ? 33.745 -0.253  36.709  1.00 16.92 ? 98  ALA B CB  1 
ATOM   736  N N   . ILE A 1 99  ? 35.978 -2.577  36.746  1.00 15.71 ? 99  ILE B N   1 
ATOM   737  C CA  . ILE A 1 99  ? 36.310 -3.993  36.874  1.00 17.47 ? 99  ILE B CA  1 
ATOM   738  C C   . ILE A 1 99  ? 37.275 -4.213  38.033  1.00 21.33 ? 99  ILE B C   1 
ATOM   739  O O   . ILE A 1 99  ? 37.113 -5.147  38.834  1.00 18.77 ? 99  ILE B O   1 
ATOM   740  C CB  . ILE A 1 99  ? 36.857 -4.576  35.559  1.00 27.99 ? 99  ILE B CB  1 
ATOM   741  C CG1 . ILE A 1 99  ? 35.790 -4.576  34.458  1.00 23.19 ? 99  ILE B CG1 1 
ATOM   742  C CG2 . ILE A 1 99  ? 37.406 -5.979  35.795  1.00 30.57 ? 99  ILE B CG2 1 
ATOM   743  C CD1 . ILE A 1 99  ? 36.334 -4.263  33.054  1.00 22.51 ? 99  ILE B CD1 1 
ATOM   744  N N   . ARG A 1 100 ? 38.294 -3.359  38.141  1.00 20.00 ? 100 ARG B N   1 
ATOM   745  C CA  . ARG A 1 100 ? 39.191 -3.441  39.289  1.00 20.47 ? 100 ARG B CA  1 
ATOM   746  C C   . ARG A 1 100 ? 38.411 -3.333  40.598  1.00 20.40 ? 100 ARG B C   1 
ATOM   747  O O   . ARG A 1 100 ? 38.722 -4.025  41.572  1.00 22.54 ? 100 ARG B O   1 
ATOM   748  C CB  . ARG A 1 100 ? 40.267 -2.359  39.196  1.00 20.31 ? 100 ARG B CB  1 
ATOM   749  N N   . ALA A 1 101 ? 37.364 -2.503  40.628  1.00 21.92 ? 101 ALA B N   1 
ATOM   750  C CA  . ALA A 1 101 ? 36.555 -2.386  41.840  1.00 21.85 ? 101 ALA B CA  1 
ATOM   751  C C   . ALA A 1 101 ? 35.885 -3.708  42.178  1.00 18.00 ? 101 ALA B C   1 
ATOM   752  O O   . ALA A 1 101 ? 35.894 -4.150  43.332  1.00 20.27 ? 101 ALA B O   1 
ATOM   753  C CB  . ALA A 1 101 ? 35.509 -1.281  41.676  1.00 18.96 ? 101 ALA B CB  1 
ATOM   754  N N   . GLU A 1 102 ? 35.285 -4.344  41.177  1.00 16.57 ? 102 GLU B N   1 
ATOM   755  C CA  . GLU A 1 102 ? 34.695 -5.660  41.367  1.00 19.55 ? 102 GLU B CA  1 
ATOM   756  C C   . GLU A 1 102 ? 35.731 -6.664  41.846  1.00 21.65 ? 102 GLU B C   1 
ATOM   757  O O   . GLU A 1 102 ? 35.465 -7.453  42.760  1.00 22.11 ? 102 GLU B O   1 
ATOM   758  C CB  . GLU A 1 102 ? 34.096 -6.112  40.034  1.00 20.61 ? 102 GLU B CB  1 
ATOM   759  C CG  . GLU A 1 102 ? 33.117 -7.251  40.110  1.00 25.57 ? 102 GLU B CG  1 
ATOM   760  C CD  . GLU A 1 102 ? 33.727 -8.578  39.745  1.00 30.39 ? 102 GLU B CD  1 
ATOM   761  O OE1 . GLU A 1 102 ? 34.953 -8.625  39.489  1.00 34.81 ? 102 GLU B OE1 1 
ATOM   762  O OE2 . GLU A 1 102 ? 32.966 -9.569  39.673  1.00 42.98 ? 102 GLU B OE2 1 
ATOM   763  N N   . GLN A 1 103 ? 36.920 -6.656  41.237  1.00 20.98 ? 103 GLN B N   1 
ATOM   764  C CA  . GLN A 1 103 ? 37.921 -7.656  41.585  1.00 20.19 ? 103 GLN B CA  1 
ATOM   765  C C   . GLN A 1 103 ? 38.430 -7.452  43.006  1.00 20.90 ? 103 GLN B C   1 
ATOM   766  O O   . GLN A 1 103 ? 38.734 -8.424  43.704  1.00 21.76 ? 103 GLN B O   1 
ATOM   767  C CB  . GLN A 1 103 ? 39.089 -7.628  40.592  1.00 22.80 ? 103 GLN B CB  1 
ATOM   768  C CG  . GLN A 1 103 ? 38.794 -8.314  39.262  1.00 29.63 ? 103 GLN B CG  1 
ATOM   769  C CD  . GLN A 1 103 ? 39.847 -8.019  38.211  1.00 40.58 ? 103 GLN B CD  1 
ATOM   770  O OE1 . GLN A 1 103 ? 40.614 -7.062  38.336  1.00 41.67 ? 103 GLN B OE1 1 
ATOM   771  N NE2 . GLN A 1 103 ? 39.887 -8.840  37.164  1.00 44.79 ? 103 GLN B NE2 1 
ATOM   772  N N   . ALA A 1 104 ? 38.542 -6.198  43.442  1.00 20.80 ? 104 ALA B N   1 
ATOM   773  C CA  . ALA A 1 104 ? 39.041 -5.862  44.768  1.00 19.71 ? 104 ALA B CA  1 
ATOM   774  C C   . ALA A 1 104 ? 37.938 -5.759  45.815  1.00 23.85 ? 104 ALA B C   1 
ATOM   775  O O   . ALA A 1 104 ? 38.209 -5.312  46.937  1.00 19.65 ? 104 ALA B O   1 
ATOM   776  C CB  . ALA A 1 104 ? 39.837 -4.556  44.720  1.00 22.69 ? 104 ALA B CB  1 
ATOM   777  N N   A SER A 1 105 ? 36.707 -6.153  45.484  0.28 20.18 ? 105 SER B N   1 
ATOM   778  N N   B SER A 1 105 ? 36.708 -6.148  45.474  0.72 20.15 ? 105 SER B N   1 
ATOM   779  C CA  A SER A 1 105 ? 35.591 -6.136  46.434  0.28 19.35 ? 105 SER B CA  1 
ATOM   780  C CA  B SER A 1 105 ? 35.593 -6.144  46.422  0.72 19.29 ? 105 SER B CA  1 
ATOM   781  C C   A SER A 1 105 ? 35.377 -4.746  47.039  0.28 20.16 ? 105 SER B C   1 
ATOM   782  C C   B SER A 1 105 ? 35.359 -4.759  47.024  0.72 20.12 ? 105 SER B C   1 
ATOM   783  O O   A SER A 1 105 ? 35.201 -4.591  48.248  0.28 26.87 ? 105 SER B O   1 
ATOM   784  O O   B SER A 1 105 ? 35.147 -4.618  48.226  0.72 27.01 ? 105 SER B O   1 
ATOM   785  C CB  A SER A 1 105 ? 35.759 -7.200  47.528  0.28 20.22 ? 105 SER B CB  1 
ATOM   786  C CB  B SER A 1 105 ? 35.776 -7.207  47.512  0.72 20.24 ? 105 SER B CB  1 
ATOM   787  O OG  A SER A 1 105 ? 35.814 -8.505  46.985  0.28 21.16 ? 105 SER B OG  1 
ATOM   788  O OG  B SER A 1 105 ? 34.705 -7.181  48.432  0.72 19.45 ? 105 SER B OG  1 
ATOM   789  N N   . LYS A 1 106 ? 35.398 -3.727  46.182  1.00 20.84 ? 106 LYS B N   1 
ATOM   790  C CA  . LYS A 1 106 ? 35.175 -2.348  46.594  1.00 15.84 ? 106 LYS B CA  1 
ATOM   791  C C   . LYS A 1 106 ? 33.789 -1.878  46.168  1.00 15.80 ? 106 LYS B C   1 
ATOM   792  O O   . LYS A 1 106 ? 33.331 -2.227  45.077  1.00 17.08 ? 106 LYS B O   1 
ATOM   793  C CB  . LYS A 1 106 ? 36.222 -1.417  45.974  1.00 15.63 ? 106 LYS B CB  1 
ATOM   794  C CG  . LYS A 1 106 ? 37.613 -1.652  46.509  1.00 12.87 ? 106 LYS B CG  1 
ATOM   795  C CD  . LYS A 1 106 ? 38.597 -0.709  45.880  1.00 15.61 ? 106 LYS B CD  1 
ATOM   796  C CE  . LYS A 1 106 ? 40.023 -1.172  46.112  1.00 23.52 ? 106 LYS B CE  1 
ATOM   797  N NZ  . LYS A 1 106 ? 40.937 -0.033  45.959  1.00 20.00 ? 106 LYS B NZ  1 
ATOM   798  N N   . PRO A 1 107 ? 33.118 -1.076  47.005  1.00 16.00 ? 107 PRO B N   1 
ATOM   799  C CA  . PRO A 1 107 ? 31.774 -0.596  46.668  1.00 12.68 ? 107 PRO B CA  1 
ATOM   800  C C   . PRO A 1 107 ? 31.729 0.200   45.368  1.00 18.61 ? 107 PRO B C   1 
ATOM   801  O O   . PRO A 1 107 ? 32.674 0.905   44.994  1.00 14.21 ? 107 PRO B O   1 
ATOM   802  C CB  . PRO A 1 107 ? 31.405 0.288   47.865  1.00 17.29 ? 107 PRO B CB  1 
ATOM   803  C CG  . PRO A 1 107 ? 32.233 -0.231  48.990  1.00 19.27 ? 107 PRO B CG  1 
ATOM   804  C CD  . PRO A 1 107 ? 33.520 -0.679  48.366  1.00 14.27 ? 107 PRO B CD  1 
ATOM   805  N N   . VAL A 1 108 ? 30.605 0.077   44.672  1.00 15.07 ? 108 VAL B N   1 
ATOM   806  C CA  . VAL A 1 108 ? 30.301 0.912   43.523  1.00 15.88 ? 108 VAL B CA  1 
ATOM   807  C C   . VAL A 1 108 ? 28.886 1.402   43.732  1.00 15.78 ? 108 VAL B C   1 
ATOM   808  O O   . VAL A 1 108 ? 27.966 0.585   43.856  1.00 15.92 ? 108 VAL B O   1 
ATOM   809  C CB  . VAL A 1 108 ? 30.383 0.129   42.203  1.00 14.86 ? 108 VAL B CB  1 
ATOM   810  C CG1 . VAL A 1 108 ? 29.934 1.010   41.043  1.00 15.49 ? 108 VAL B CG1 1 
ATOM   811  C CG2 . VAL A 1 108 ? 31.800 -0.399  41.948  1.00 20.93 ? 108 VAL B CG2 1 
ATOM   812  N N   . ALA A 1 109 ? 28.706 2.719   43.771  1.00 13.94 ? 109 ALA B N   1 
ATOM   813  C CA  . ALA A 1 109 ? 27.382 3.313   43.902  1.00 13.52 ? 109 ALA B CA  1 
ATOM   814  C C   . ALA A 1 109 ? 27.012 3.981   42.587  1.00 17.57 ? 109 ALA B C   1 
ATOM   815  O O   . ALA A 1 109 ? 27.739 4.855   42.108  1.00 16.87 ? 109 ALA B O   1 
ATOM   816  C CB  . ALA A 1 109 ? 27.363 4.335   45.034  1.00 15.28 ? 109 ALA B CB  1 
ATOM   817  N N   . VAL A 1 110 ? 25.858 3.599   42.034  1.00 18.52 ? 110 VAL B N   1 
ATOM   818  C CA  . VAL A 1 110 ? 25.456 4.005   40.693  1.00 13.03 ? 110 VAL B CA  1 
ATOM   819  C C   . VAL A 1 110 ? 24.008 4.493   40.750  1.00 13.40 ? 110 VAL B C   1 
ATOM   820  O O   . VAL A 1 110 ? 23.204 4.001   41.545  1.00 14.11 ? 110 VAL B O   1 
ATOM   821  C CB  . VAL A 1 110 ? 25.631 2.819   39.718  1.00 21.12 ? 110 VAL B CB  1 
ATOM   822  C CG1 . VAL A 1 110 ? 24.717 1.654   40.052  1.00 28.09 ? 110 VAL B CG1 1 
ATOM   823  C CG2 . VAL A 1 110 ? 25.450 3.261   38.284  1.00 25.18 ? 110 VAL B CG2 1 
ATOM   824  N N   . ILE A 1 111 ? 23.661 5.463   39.905  1.00 13.88 ? 111 ILE B N   1 
ATOM   825  C CA  . ILE A 1 111 ? 22.322 6.054   40.017  1.00 11.47 ? 111 ILE B CA  1 
ATOM   826  C C   . ILE A 1 111 ? 21.801 6.452   38.644  1.00 15.96 ? 111 ILE B C   1 
ATOM   827  O O   . ILE A 1 111 ? 22.552 6.933   37.789  1.00 17.30 ? 111 ILE B O   1 
ATOM   828  C CB  . ILE A 1 111 ? 22.347 7.250   41.001  1.00 14.27 ? 111 ILE B CB  1 
ATOM   829  C CG1 . ILE A 1 111 ? 20.949 7.858   41.200  1.00 13.91 ? 111 ILE B CG1 1 
ATOM   830  C CG2 . ILE A 1 111 ? 23.370 8.292   40.554  1.00 18.81 ? 111 ILE B CG2 1 
ATOM   831  C CD1 . ILE A 1 111 ? 20.746 8.462   42.540  1.00 17.00 ? 111 ILE B CD1 1 
ATOM   832  N N   . CYS A 1 112 ? 20.481 6.282   38.466  1.00 13.37 ? 112 CYS B N   1 
ATOM   833  C CA  . CYS A 1 112 ? 19.766 6.720   37.266  1.00 19.80 ? 112 CYS B CA  1 
ATOM   834  C C   . CYS A 1 112 ? 20.234 6.018   35.995  1.00 12.91 ? 112 CYS B C   1 
ATOM   835  O O   . CYS A 1 112 ? 19.958 4.830   35.853  1.00 14.00 ? 112 CYS B O   1 
ATOM   836  C CB  . CYS A 1 112 ? 19.809 8.239   37.121  1.00 30.00 ? 112 CYS B CB  1 
ATOM   837  S SG  . CYS A 1 112 ? 18.330 8.901   36.298  1.00 30.00 ? 112 CYS B SG  1 
ATOM   838  N N   . HIS A 1 113 ? 20.943 6.728   35.117  1.00 17.22 ? 113 HIS B N   1 
ATOM   839  C CA  . HIS A 1 113 ? 21.417 6.142   33.870  1.00 12.23 ? 113 HIS B CA  1 
ATOM   840  C C   . HIS A 1 113 ? 22.825 5.560   34.007  1.00 15.01 ? 113 HIS B C   1 
ATOM   841  O O   . HIS A 1 113 ? 23.355 4.997   33.045  1.00 15.95 ? 113 HIS B O   1 
ATOM   842  C CB  . HIS A 1 113 ? 21.435 7.201   32.759  1.00 15.31 ? 113 HIS B CB  1 
ATOM   843  C CG  . HIS A 1 113 ? 20.078 7.580   32.248  1.00 12.08 ? 113 HIS B CG  1 
ATOM   844  N ND1 . HIS A 1 113 ? 19.345 8.600   32.811  1.00 15.39 ? 113 HIS B ND1 1 
ATOM   845  C CD2 . HIS A 1 113 ? 19.330 7.101   31.226  1.00 16.62 ? 113 HIS B CD2 1 
ATOM   846  C CE1 . HIS A 1 113 ? 18.190 8.720   32.179  1.00 12.40 ? 113 HIS B CE1 1 
ATOM   847  N NE2 . HIS A 1 113 ? 18.166 7.832   31.203  1.00 16.52 ? 113 HIS B NE2 1 
ATOM   848  N N   . GLY A 1 114 ? 23.451 5.683   35.176  1.00 13.55 ? 114 GLY B N   1 
ATOM   849  C CA  . GLY A 1 114 ? 24.872 5.423   35.285  1.00 16.18 ? 114 GLY B CA  1 
ATOM   850  C C   . GLY A 1 114 ? 25.285 3.973   35.132  1.00 16.96 ? 114 GLY B C   1 
ATOM   851  O O   . GLY A 1 114 ? 26.492 3.713   35.054  1.00 14.29 ? 114 GLY B O   1 
ATOM   852  N N   . ALA A 1 115 ? 24.340 3.023   35.112  1.00 15.47 ? 115 ALA B N   1 
ATOM   853  C CA  . ALA A 1 115 ? 24.755 1.623   35.066  1.00 15.20 ? 115 ALA B CA  1 
ATOM   854  C C   . ALA A 1 115 ? 25.148 1.162   33.673  1.00 15.04 ? 115 ALA B C   1 
ATOM   855  O O   . ALA A 1 115 ? 25.541 0.001   33.507  1.00 16.49 ? 115 ALA B O   1 
ATOM   856  C CB  . ALA A 1 115 ? 23.663 0.702   35.608  1.00 18.74 ? 115 ALA B CB  1 
ATOM   857  N N   . TRP A 1 116 ? 25.005 2.015   32.665  1.00 15.14 ? 116 TRP B N   1 
ATOM   858  C CA  . TRP A 1 116 ? 25.409 1.600   31.329  1.00 13.55 ? 116 TRP B CA  1 
ATOM   859  C C   . TRP A 1 116 ? 26.877 1.201   31.308  1.00 12.36 ? 116 TRP B C   1 
ATOM   860  O O   . TRP A 1 116 ? 27.261 0.259   30.608  1.00 13.47 ? 116 TRP B O   1 
ATOM   861  C CB  . TRP A 1 116 ? 25.135 2.713   30.314  1.00 13.36 ? 116 TRP B CB  1 
ATOM   862  C CG  . TRP A 1 116 ? 23.791 2.623   29.651  1.00 16.87 ? 116 TRP B CG  1 
ATOM   863  C CD1 . TRP A 1 116 ? 23.098 1.487   29.310  1.00 14.32 ? 116 TRP B CD1 1 
ATOM   864  C CD2 . TRP A 1 116 ? 22.979 3.726   29.231  1.00 14.30 ? 116 TRP B CD2 1 
ATOM   865  N NE1 . TRP A 1 116 ? 21.897 1.826   28.709  1.00 16.13 ? 116 TRP B NE1 1 
ATOM   866  C CE2 . TRP A 1 116 ? 21.805 3.192   28.653  1.00 16.36 ? 116 TRP B CE2 1 
ATOM   867  C CE3 . TRP A 1 116 ? 23.127 5.117   29.297  1.00 15.40 ? 116 TRP B CE3 1 
ATOM   868  C CZ2 . TRP A 1 116 ? 20.792 4.001   28.151  1.00 14.60 ? 116 TRP B CZ2 1 
ATOM   869  C CZ3 . TRP A 1 116 ? 22.121 5.918   28.787  1.00 14.23 ? 116 TRP B CZ3 1 
ATOM   870  C CH2 . TRP A 1 116 ? 20.974 5.357   28.212  1.00 15.80 ? 116 TRP B CH2 1 
ATOM   871  N N   . LEU A 1 117 ? 27.708 1.901   32.086  1.00 12.40 ? 117 LEU B N   1 
ATOM   872  C CA  . LEU A 1 117 ? 29.129 1.578   32.143  1.00 14.71 ? 117 LEU B CA  1 
ATOM   873  C C   . LEU A 1 117 ? 29.354 0.191   32.736  1.00 17.83 ? 117 LEU B C   1 
ATOM   874  O O   . LEU A 1 117 ? 30.217 -0.564  32.273  1.00 17.36 ? 117 LEU B O   1 
ATOM   875  C CB  . LEU A 1 117 ? 29.850 2.618   32.998  1.00 16.73 ? 117 LEU B CB  1 
ATOM   876  C CG  . LEU A 1 117 ? 31.314 2.304   33.355  1.00 12.35 ? 117 LEU B CG  1 
ATOM   877  C CD1 . LEU A 1 117 ? 32.199 2.402   32.122  1.00 16.22 ? 117 LEU B CD1 1 
ATOM   878  C CD2 . LEU A 1 117 ? 31.803 3.211   34.472  1.00 16.62 ? 117 LEU B CD2 1 
ATOM   879  N N   . LEU A 1 118 ? 28.606 -0.157  33.779  1.00 16.66 ? 118 LEU B N   1 
ATOM   880  C CA  . LEU A 1 118 ? 28.731 -1.501  34.332  1.00 18.49 ? 118 LEU B CA  1 
ATOM   881  C C   . LEU A 1 118 ? 28.294 -2.558  33.319  1.00 14.86 ? 118 LEU B C   1 
ATOM   882  O O   . LEU A 1 118 ? 28.864 -3.653  33.273  1.00 15.16 ? 118 LEU B O   1 
ATOM   883  C CB  . LEU A 1 118 ? 27.924 -1.609  35.624  1.00 14.03 ? 118 LEU B CB  1 
ATOM   884  C CG  . LEU A 1 118 ? 28.258 -0.583  36.699  1.00 16.88 ? 118 LEU B CG  1 
ATOM   885  C CD1 . LEU A 1 118 ? 27.320 -0.710  37.888  1.00 15.58 ? 118 LEU B CD1 1 
ATOM   886  C CD2 . LEU A 1 118 ? 29.705 -0.749  37.165  1.00 16.76 ? 118 LEU B CD2 1 
ATOM   887  N N   . ILE A 1 119 ? 27.270 -2.262  32.513  1.00 17.84 ? 119 ILE B N   1 
ATOM   888  C CA  . ILE A 1 119 ? 26.861 -3.206  31.475  1.00 17.13 ? 119 ILE B CA  1 
ATOM   889  C C   . ILE A 1 119 ? 27.994 -3.440  30.494  1.00 16.49 ? 119 ILE B C   1 
ATOM   890  O O   . ILE A 1 119 ? 28.365 -4.584  30.205  1.00 16.30 ? 119 ILE B O   1 
ATOM   891  C CB  . ILE A 1 119 ? 25.598 -2.714  30.748  1.00 15.30 ? 119 ILE B CB  1 
ATOM   892  C CG1 . ILE A 1 119 ? 24.374 -2.792  31.662  1.00 17.67 ? 119 ILE B CG1 1 
ATOM   893  C CG2 . ILE A 1 119 ? 25.420 -3.513  29.468  1.00 15.70 ? 119 ILE B CG2 1 
ATOM   894  C CD1 . ILE A 1 119 ? 23.247 -1.938  31.186  1.00 18.56 ? 119 ILE B CD1 1 
ATOM   895  N N   . SER A 1 120 ? 28.555 -2.354  29.968  1.00 14.06 ? 120 SER B N   1 
ATOM   896  C CA  . SER A 1 120 ? 29.619 -2.462  28.979  1.00 12.28 ? 120 SER B CA  1 
ATOM   897  C C   . SER A 1 120 ? 30.895 -3.053  29.558  1.00 14.76 ? 120 SER B C   1 
ATOM   898  O O   . SER A 1 120 ? 31.686 -3.638  28.811  1.00 17.54 ? 120 SER B O   1 
ATOM   899  C CB  . SER A 1 120 ? 29.854 -1.100  28.326  1.00 11.70 ? 120 SER B CB  1 
ATOM   900  O OG  . SER A 1 120 ? 28.716 -0.759  27.544  1.00 14.69 ? 120 SER B OG  1 
ATOM   901  N N   . ALA A 1 121 ? 31.109 -2.935  30.868  1.00 18.16 ? 121 ALA B N   1 
ATOM   902  C CA  . ALA A 1 121 ? 32.270 -3.548  31.501  1.00 13.27 ? 121 ALA B CA  1 
ATOM   903  C C   . ALA A 1 121 ? 32.038 -5.011  31.850  1.00 15.47 ? 121 ALA B C   1 
ATOM   904  O O   . ALA A 1 121 ? 32.929 -5.643  32.433  1.00 22.90 ? 121 ALA B O   1 
ATOM   905  C CB  . ALA A 1 121 ? 32.677 -2.769  32.764  1.00 16.66 ? 121 ALA B CB  1 
ATOM   906  N N   . GLY A 1 122 ? 30.854 -5.544  31.554  1.00 17.13 ? 122 GLY B N   1 
ATOM   907  C CA  . GLY A 1 122 ? 30.541 -6.923  31.867  1.00 21.33 ? 122 GLY B CA  1 
ATOM   908  C C   . GLY A 1 122 ? 30.247 -7.177  33.326  1.00 22.33 ? 122 GLY B C   1 
ATOM   909  O O   . GLY A 1 122 ? 30.336 -8.319  33.784  1.00 27.62 ? 122 GLY B O   1 
ATOM   910  N N   . LEU A 1 123 ? 29.856 -6.147  34.067  1.00 18.22 ? 123 LEU B N   1 
ATOM   911  C CA  . LEU A 1 123 ? 29.805 -6.242  35.508  1.00 16.04 ? 123 LEU B CA  1 
ATOM   912  C C   . LEU A 1 123 ? 28.399 -6.406  36.057  1.00 18.09 ? 123 LEU B C   1 
ATOM   913  O O   . LEU A 1 123 ? 28.251 -6.599  37.266  1.00 24.72 ? 123 LEU B O   1 
ATOM   914  C CB  . LEU A 1 123 ? 30.460 -5.012  36.144  1.00 18.78 ? 123 LEU B CB  1 
ATOM   915  C CG  . LEU A 1 123 ? 31.921 -4.849  35.729  1.00 17.63 ? 123 LEU B CG  1 
ATOM   916  C CD1 . LEU A 1 123 ? 32.455 -3.552  36.310  1.00 19.15 ? 123 LEU B CD1 1 
ATOM   917  C CD2 . LEU A 1 123 ? 32.760 -6.050  36.137  1.00 24.28 ? 123 LEU B CD2 1 
ATOM   918  N N   . VAL A 1 124 ? 27.355 -6.348  35.224  1.00 18.49 ? 124 VAL B N   1 
ATOM   919  C CA  . VAL A 1 124 ? 26.003 -6.522  35.757  1.00 22.80 ? 124 VAL B CA  1 
ATOM   920  C C   . VAL A 1 124 ? 25.535 -7.966  35.701  1.00 24.19 ? 124 VAL B C   1 
ATOM   921  O O   . VAL A 1 124 ? 24.452 -8.279  36.216  1.00 24.09 ? 124 VAL B O   1 
ATOM   922  C CB  . VAL A 1 124 ? 24.962 -5.573  35.131  1.00 22.52 ? 124 VAL B CB  1 
ATOM   923  C CG1 . VAL A 1 124 ? 25.462 -4.153  35.152  1.00 25.12 ? 124 VAL B CG1 1 
ATOM   924  C CG2 . VAL A 1 124 ? 24.631 -6.021  33.741  1.00 20.45 ? 124 VAL B CG2 1 
ATOM   925  N N   . GLN A 1 125 ? 26.328 -8.858  35.124  1.00 22.03 ? 125 GLN B N   1 
ATOM   926  C CA  . GLN A 1 125 ? 25.944 -10.251 34.997  1.00 25.88 ? 125 GLN B CA  1 
ATOM   927  C C   . GLN A 1 125 ? 25.729 -10.871 36.377  1.00 26.06 ? 125 GLN B C   1 
ATOM   928  O O   . GLN A 1 125 ? 26.605 -10.796 37.245  1.00 27.68 ? 125 GLN B O   1 
ATOM   929  C CB  . GLN A 1 125 ? 27.068 -10.969 34.266  1.00 27.55 ? 125 GLN B CB  1 
ATOM   930  C CG  . GLN A 1 125 ? 26.755 -12.392 33.998  1.00 33.70 ? 125 GLN B CG  1 
ATOM   931  C CD  . GLN A 1 125 ? 25.832 -12.535 32.804  1.00 39.02 ? 125 GLN B CD  1 
ATOM   932  O OE1 . GLN A 1 125 ? 24.647 -12.842 32.954  1.00 41.58 ? 125 GLN B OE1 1 
ATOM   933  N NE2 . GLN A 1 125 ? 26.374 -12.328 31.607  1.00 37.55 ? 125 GLN B NE2 1 
ATOM   934  N N   . GLY A 1 126 ? 24.563 -11.484 36.579  1.00 21.91 ? 126 GLY B N   1 
ATOM   935  C CA  . GLY A 1 126 ? 24.206 -12.075 37.850  1.00 19.76 ? 126 GLY B CA  1 
ATOM   936  C C   . GLY A 1 126 ? 24.016 -11.101 38.984  1.00 25.84 ? 126 GLY B C   1 
ATOM   937  O O   . GLY A 1 126 ? 23.923 -11.535 40.137  1.00 34.64 ? 126 GLY B O   1 
ATOM   938  N N   . ARG A 1 127 ? 23.987 -9.800  38.715  1.00 19.00 ? 127 ARG B N   1 
ATOM   939  C CA  . ARG A 1 127 ? 23.848 -8.823  39.781  1.00 23.91 ? 127 ARG B CA  1 
ATOM   940  C C   . ARG A 1 127 ? 22.412 -8.314  39.850  1.00 17.71 ? 127 ARG B C   1 
ATOM   941  O O   . ARG A 1 127 ? 21.686 -8.304  38.855  1.00 21.28 ? 127 ARG B O   1 
ATOM   942  C CB  . ARG A 1 127 ? 24.821 -7.653  39.605  1.00 24.75 ? 127 ARG B CB  1 
ATOM   943  C CG  . ARG A 1 127 ? 26.276 -8.063  39.317  1.00 22.91 ? 127 ARG B CG  1 
ATOM   944  C CD  . ARG A 1 127 ? 26.830 -9.036  40.363  1.00 20.28 ? 127 ARG B CD  1 
ATOM   945  N NE  . ARG A 1 127 ? 26.788 -8.488  41.710  1.00 27.68 ? 127 ARG B NE  1 
ATOM   946  C CZ  . ARG A 1 127 ? 27.780 -7.819  42.286  1.00 26.05 ? 127 ARG B CZ  1 
ATOM   947  N NH1 . ARG A 1 127 ? 28.901 -7.542  41.637  1.00 28.35 ? 127 ARG B NH1 1 
ATOM   948  N NH2 . ARG A 1 127 ? 27.647 -7.422  43.549  1.00 23.63 ? 127 ARG B NH2 1 
ATOM   949  N N   . THR A 1 128 ? 21.994 -7.929  41.048  1.00 20.12 ? 128 THR B N   1 
ATOM   950  C CA  . THR A 1 128 ? 20.717 -7.270  41.248  1.00 18.53 ? 128 THR B CA  1 
ATOM   951  C C   . THR A 1 128 ? 20.970 -5.780  41.411  1.00 20.27 ? 128 THR B C   1 
ATOM   952  O O   . THR A 1 128 ? 21.829 -5.377  42.210  1.00 19.28 ? 128 THR B O   1 
ATOM   953  C CB  . THR A 1 128 ? 20.024 -7.838  42.489  1.00 27.42 ? 128 THR B CB  1 
ATOM   954  O OG1 . THR A 1 128 ? 19.509 -9.136  42.173  1.00 33.06 ? 128 THR B OG1 1 
ATOM   955  C CG2 . THR A 1 128 ? 18.881 -6.938  42.958  1.00 19.51 ? 128 THR B CG2 1 
ATOM   956  N N   . LEU A 1 129 ? 20.249 -4.972  40.632  1.00 20.11 ? 129 LEU B N   1 
ATOM   957  C CA  . LEU A 1 129 ? 20.390 -3.526  40.722  1.00 18.71 ? 129 LEU B CA  1 
ATOM   958  C C   . LEU A 1 129 ? 19.151 -2.857  40.155  1.00 11.79 ? 129 LEU B C   1 
ATOM   959  O O   . LEU A 1 129 ? 18.360 -3.470  39.436  1.00 15.34 ? 129 LEU B O   1 
ATOM   960  C CB  . LEU A 1 129 ? 21.635 -3.017  39.992  1.00 16.34 ? 129 LEU B CB  1 
ATOM   961  C CG  . LEU A 1 129 ? 21.629 -3.158  38.465  1.00 18.50 ? 129 LEU B CG  1 
ATOM   962  C CD1 . LEU A 1 129 ? 22.461 -2.065  37.843  1.00 18.74 ? 129 LEU B CD1 1 
ATOM   963  C CD2 . LEU A 1 129 ? 22.076 -4.534  38.012  1.00 15.87 ? 129 LEU B CD2 1 
ATOM   964  N N   . THR A 1 130 ? 18.977 -1.603  40.533  1.00 14.19 ? 130 THR B N   1 
ATOM   965  C CA  . THR A 1 130 ? 17.962 -0.733  39.994  1.00 18.82 ? 130 THR B CA  1 
ATOM   966  C C   . THR A 1 130 ? 18.656 0.352   39.183  1.00 13.05 ? 130 THR B C   1 
ATOM   967  O O   . THR A 1 130 ? 19.889 0.387   39.067  1.00 14.92 ? 130 THR B O   1 
ATOM   968  C CB  . THR A 1 130 ? 17.115 -0.164  41.132  1.00 17.51 ? 130 THR B CB  1 
ATOM   969  O OG1 . THR A 1 130 ? 15.939 0.457   40.594  1.00 17.82 ? 130 THR B OG1 1 
ATOM   970  C CG2 . THR A 1 130 ? 17.905 0.838   41.968  1.00 15.77 ? 130 THR B CG2 1 
ATOM   971  N N   . SER A 1 131 ? 17.848 1.246   38.631  1.00 19.73 ? 131 SER B N   1 
ATOM   972  C CA  . SER A 1 131 ? 18.293 2.269   37.696  1.00 16.31 ? 131 SER B CA  1 
ATOM   973  C C   . SER A 1 131 ? 17.066 3.073   37.292  1.00 14.72 ? 131 SER B C   1 
ATOM   974  O O   . SER A 1 131 ? 15.926 2.736   37.636  1.00 16.51 ? 131 SER B O   1 
ATOM   975  C CB  . SER A 1 131 ? 18.927 1.638   36.452  1.00 21.01 ? 131 SER B CB  1 
ATOM   976  O OG  . SER A 1 131 ? 17.930 1.092   35.612  1.00 19.87 ? 131 SER B OG  1 
ATOM   977  N N   . TRP A 1 132 ? 17.310 4.125   36.520  1.00 15.78 ? 132 TRP B N   1 
ATOM   978  C CA  . TRP A 1 132 ? 16.204 4.766   35.832  1.00 16.26 ? 132 TRP B CA  1 
ATOM   979  C C   . TRP A 1 132 ? 15.520 3.708   34.967  1.00 19.52 ? 132 TRP B C   1 
ATOM   980  O O   . TRP A 1 132 ? 16.202 2.886   34.344  1.00 19.17 ? 132 TRP B O   1 
ATOM   981  C CB  . TRP A 1 132 ? 16.733 5.923   34.982  1.00 16.69 ? 132 TRP B CB  1 
ATOM   982  C CG  . TRP A 1 132 ? 15.665 6.736   34.324  1.00 15.35 ? 132 TRP B CG  1 
ATOM   983  C CD1 . TRP A 1 132 ? 15.391 6.807   32.981  1.00 15.22 ? 132 TRP B CD1 1 
ATOM   984  C CD2 . TRP A 1 132 ? 14.727 7.609   34.967  1.00 17.27 ? 132 TRP B CD2 1 
ATOM   985  N NE1 . TRP A 1 132 ? 14.338 7.663   32.758  1.00 16.87 ? 132 TRP B NE1 1 
ATOM   986  C CE2 . TRP A 1 132 ? 13.911 8.163   33.959  1.00 20.50 ? 132 TRP B CE2 1 
ATOM   987  C CE3 . TRP A 1 132 ? 14.491 7.970   36.298  1.00 19.52 ? 132 TRP B CE3 1 
ATOM   988  C CZ2 . TRP A 1 132 ? 12.872 9.052   34.245  1.00 19.83 ? 132 TRP B CZ2 1 
ATOM   989  C CZ3 . TRP A 1 132 ? 13.457 8.850   36.574  1.00 22.82 ? 132 TRP B CZ3 1 
ATOM   990  C CH2 . TRP A 1 132 ? 12.679 9.392   35.557  1.00 18.04 ? 132 TRP B CH2 1 
ATOM   991  N N   . PRO A 1 133 ? 14.186 3.651   34.948  1.00 16.84 ? 133 PRO B N   1 
ATOM   992  C CA  . PRO A 1 133 ? 13.509 2.527   34.271  1.00 17.30 ? 133 PRO B CA  1 
ATOM   993  C C   . PRO A 1 133 ? 13.884 2.327   32.814  1.00 19.18 ? 133 PRO B C   1 
ATOM   994  O O   . PRO A 1 133 ? 13.706 1.215   32.298  1.00 18.32 ? 133 PRO B O   1 
ATOM   995  C CB  . PRO A 1 133 ? 12.018 2.855   34.439  1.00 17.62 ? 133 PRO B CB  1 
ATOM   996  C CG  . PRO A 1 133 ? 11.969 3.713   35.659  1.00 26.73 ? 133 PRO B CG  1 
ATOM   997  C CD  . PRO A 1 133 ? 13.231 4.546   35.618  1.00 19.68 ? 133 PRO B CD  1 
ATOM   998  N N   . SER A 1 134 ? 14.401 3.354   32.134  1.00 16.25 ? 134 SER B N   1 
ATOM   999  C CA  . SER A 1 134 ? 14.722 3.212   30.721  1.00 22.33 ? 134 SER B CA  1 
ATOM   1000 C C   . SER A 1 134 ? 15.825 2.190   30.479  1.00 18.70 ? 134 SER B C   1 
ATOM   1001 O O   . SER A 1 134 ? 15.920 1.657   29.370  1.00 20.89 ? 134 SER B O   1 
ATOM   1002 C CB  . SER A 1 134 ? 15.143 4.561   30.144  1.00 18.24 ? 134 SER B CB  1 
ATOM   1003 O OG  . SER A 1 134 ? 16.455 4.893   30.588  1.00 20.02 ? 134 SER B OG  1 
ATOM   1004 N N   . LEU A 1 135 ? 16.654 1.901   31.483  1.00 18.78 ? 135 LEU B N   1 
ATOM   1005 C CA  . LEU A 1 135 ? 17.729 0.930   31.352  1.00 15.06 ? 135 LEU B CA  1 
ATOM   1006 C C   . LEU A 1 135 ? 17.297 -0.482  31.722  1.00 14.28 ? 135 LEU B C   1 
ATOM   1007 O O   . LEU A 1 135 ? 18.106 -1.409  31.594  1.00 17.47 ? 135 LEU B O   1 
ATOM   1008 C CB  . LEU A 1 135 ? 18.895 1.347   32.251  1.00 14.04 ? 135 LEU B CB  1 
ATOM   1009 C CG  . LEU A 1 135 ? 19.951 2.264   31.623  1.00 21.20 ? 135 LEU B CG  1 
ATOM   1010 C CD1 . LEU A 1 135 ? 19.455 3.696   31.662  1.00 21.45 ? 135 LEU B CD1 1 
ATOM   1011 C CD2 . LEU A 1 135 ? 21.317 2.150   32.337  1.00 19.80 ? 135 LEU B CD2 1 
ATOM   1012 N N   . LYS A 1 136 ? 16.057 -0.661  32.197  1.00 13.36 ? 136 LYS B N   1 
ATOM   1013 C CA  . LYS A 1 136 ? 15.584 -1.970  32.640  1.00 15.82 ? 136 LYS B CA  1 
ATOM   1014 C C   . LYS A 1 136 ? 15.922 -3.074  31.655  1.00 14.31 ? 136 LYS B C   1 
ATOM   1015 O O   . LYS A 1 136 ? 16.432 -4.132  32.040  1.00 17.44 ? 136 LYS B O   1 
ATOM   1016 C CB  . LYS A 1 136 ? 14.067 -1.942  32.819  1.00 18.25 ? 136 LYS B CB  1 
ATOM   1017 C CG  . LYS A 1 136 ? 13.545 -3.262  33.333  1.00 17.44 ? 136 LYS B CG  1 
ATOM   1018 C CD  . LYS A 1 136 ? 12.028 -3.288  33.357  1.00 18.03 ? 136 LYS B CD  1 
ATOM   1019 C CE  . LYS A 1 136 ? 11.500 -4.679  33.683  1.00 28.42 ? 136 LYS B CE  1 
ATOM   1020 N NZ  . LYS A 1 136 ? 10.052 -4.813  33.336  1.00 24.61 ? 136 LYS B NZ  1 
ATOM   1021 N N   . ASP A 1 137 ? 15.598 -2.860  30.378  1.00 15.92 ? 137 ASP B N   1 
ATOM   1022 C CA  . ASP A 1 137 ? 15.794 -3.904  29.382  1.00 18.08 ? 137 ASP B CA  1 
ATOM   1023 C C   . ASP A 1 137 ? 17.276 -4.158  29.126  1.00 17.60 ? 137 ASP B C   1 
ATOM   1024 O O   . ASP A 1 137 ? 17.689 -5.306  28.940  1.00 19.58 ? 137 ASP B O   1 
ATOM   1025 C CB  . ASP A 1 137 ? 15.077 -3.523  28.089  1.00 15.73 ? 137 ASP B CB  1 
ATOM   1026 C CG  . ASP A 1 137 ? 13.565 -3.453  28.256  1.00 21.48 ? 137 ASP B CG  1 
ATOM   1027 O OD1 . ASP A 1 137 ? 13.025 -4.211  29.077  1.00 20.86 ? 137 ASP B OD1 1 
ATOM   1028 O OD2 . ASP A 1 137 ? 12.919 -2.649  27.551  1.00 22.95 ? 137 ASP B OD2 1 
ATOM   1029 N N   . ASP A 1 138 ? 18.092 -3.101  29.119  1.00 17.85 ? 138 ASP B N   1 
ATOM   1030 C CA  . ASP A 1 138 ? 19.528 -3.278  28.930  1.00 17.07 ? 138 ASP B CA  1 
ATOM   1031 C C   . ASP A 1 138 ? 20.150 -4.057  30.090  1.00 17.51 ? 138 ASP B C   1 
ATOM   1032 O O   . ASP A 1 138 ? 21.007 -4.921  29.880  1.00 16.10 ? 138 ASP B O   1 
ATOM   1033 C CB  . ASP A 1 138 ? 20.205 -1.914  28.755  1.00 19.08 ? 138 ASP B CB  1 
ATOM   1034 C CG  . ASP A 1 138 ? 19.722 -1.175  27.497  1.00 17.54 ? 138 ASP B CG  1 
ATOM   1035 O OD1 . ASP A 1 138 ? 19.290 -1.852  26.544  1.00 18.26 ? 138 ASP B OD1 1 
ATOM   1036 O OD2 . ASP A 1 138 ? 19.789 0.076   27.456  1.00 17.05 ? 138 ASP B OD2 1 
ATOM   1037 N N   . ILE A 1 139 ? 19.725 -3.772  31.321  1.00 15.04 ? 139 ILE B N   1 
ATOM   1038 C CA  . ILE A 1 139 ? 20.257 -4.480  32.487  1.00 16.73 ? 139 ILE B CA  1 
ATOM   1039 C C   . ILE A 1 139 ? 19.840 -5.948  32.456  1.00 14.98 ? 139 ILE B C   1 
ATOM   1040 O O   . ILE A 1 139 ? 20.673 -6.853  32.616  1.00 18.48 ? 139 ILE B O   1 
ATOM   1041 C CB  . ILE A 1 139 ? 19.840 -3.757  33.784  1.00 15.87 ? 139 ILE B CB  1 
ATOM   1042 C CG1 . ILE A 1 139 ? 20.641 -2.453  33.897  1.00 18.41 ? 139 ILE B CG1 1 
ATOM   1043 C CG2 . ILE A 1 139 ? 20.068 -4.637  35.001  1.00 16.59 ? 139 ILE B CG2 1 
ATOM   1044 C CD1 . ILE A 1 139 ? 20.130 -1.459  34.909  1.00 15.43 ? 139 ILE B CD1 1 
ATOM   1045 N N   . ASN A 1 140 ? 18.553 -6.209  32.181  1.00 14.99 ? 140 ASN B N   1 
ATOM   1046 C CA  . ASN A 1 140 ? 18.105 -7.596  32.101  1.00 17.75 ? 140 ASN B CA  1 
ATOM   1047 C C   . ASN A 1 140 ? 18.754 -8.327  30.928  1.00 18.49 ? 140 ASN B C   1 
ATOM   1048 O O   . ASN A 1 140 ? 19.164 -9.486  31.064  1.00 19.90 ? 140 ASN B O   1 
ATOM   1049 C CB  . ASN A 1 140 ? 16.580 -7.665  32.038  1.00 16.82 ? 140 ASN B CB  1 
ATOM   1050 C CG  . ASN A 1 140 ? 15.923 -7.364  33.378  1.00 20.35 ? 140 ASN B CG  1 
ATOM   1051 O OD1 . ASN A 1 140 ? 16.489 -7.632  34.436  1.00 19.37 ? 140 ASN B OD1 1 
ATOM   1052 N ND2 . ASN A 1 140 ? 14.710 -6.821  33.340  1.00 17.34 ? 140 ASN B ND2 1 
ATOM   1053 N N   . ASN A 1 141 ? 18.884 -7.664  29.775  1.00 19.19 ? 141 ASN B N   1 
ATOM   1054 C CA  . ASN A 1 141 ? 19.446 -8.348  28.614  1.00 18.18 ? 141 ASN B CA  1 
ATOM   1055 C C   . ASN A 1 141 ? 20.906 -8.700  28.837  1.00 17.79 ? 141 ASN B C   1 
ATOM   1056 O O   . ASN A 1 141 ? 21.414 -9.666  28.254  1.00 19.31 ? 141 ASN B O   1 
ATOM   1057 C CB  . ASN A 1 141 ? 19.304 -7.482  27.361  1.00 19.19 ? 141 ASN B CB  1 
ATOM   1058 C CG  . ASN A 1 141 ? 17.875 -7.454  26.852  1.00 18.28 ? 141 ASN B CG  1 
ATOM   1059 O OD1 . ASN A 1 141 ? 17.054 -8.294  27.227  1.00 23.02 ? 141 ASN B OD1 1 
ATOM   1060 N ND2 . ASN A 1 141 ? 17.570 -6.490  26.006  1.00 24.93 ? 141 ASN B ND2 1 
ATOM   1061 N N   . ALA A 1 142 ? 21.581 -7.943  29.691  1.00 17.34 ? 142 ALA B N   1 
ATOM   1062 C CA  . ALA A 1 142 ? 22.977 -8.177  30.006  1.00 19.63 ? 142 ALA B CA  1 
ATOM   1063 C C   . ALA A 1 142 ? 23.153 -9.184  31.135  1.00 17.37 ? 142 ALA B C   1 
ATOM   1064 O O   . ALA A 1 142 ? 24.254 -9.290  31.687  1.00 19.61 ? 142 ALA B O   1 
ATOM   1065 C CB  . ALA A 1 142 ? 23.656 -6.846  30.347  1.00 22.37 ? 142 ALA B CB  1 
ATOM   1066 N N   . GLY A 1 143 ? 22.095 -9.911  31.498  1.00 21.42 ? 143 GLY B N   1 
ATOM   1067 C CA  . GLY A 1 143 ? 22.178 -10.919 32.526  1.00 25.57 ? 143 GLY B CA  1 
ATOM   1068 C C   . GLY A 1 143 ? 21.969 -10.412 33.933  1.00 19.13 ? 143 GLY B C   1 
ATOM   1069 O O   . GLY A 1 143 ? 22.119 -11.193 34.882  1.00 24.93 ? 143 GLY B O   1 
ATOM   1070 N N   . GLY A 1 144 ? 21.670 -9.128  34.108  1.00 17.65 ? 144 GLY B N   1 
ATOM   1071 C CA  . GLY A 1 144 ? 21.318 -8.622  35.412  1.00 23.41 ? 144 GLY B CA  1 
ATOM   1072 C C   . GLY A 1 144 ? 19.894 -8.967  35.783  1.00 21.40 ? 144 GLY B C   1 
ATOM   1073 O O   . GLY A 1 144 ? 19.109 -9.456  34.964  1.00 21.58 ? 144 GLY B O   1 
ATOM   1074 N N   . HIS A 1 145 ? 19.575 -8.715  37.049  1.00 18.86 ? 145 HIS B N   1 
ATOM   1075 C CA  . HIS A 1 145 ? 18.222 -8.842  37.574  1.00 20.42 ? 145 HIS B CA  1 
ATOM   1076 C C   . HIS A 1 145 ? 17.806 -7.421  37.936  1.00 18.37 ? 145 HIS B C   1 
ATOM   1077 O O   . HIS A 1 145 ? 18.228 -6.888  38.963  1.00 20.36 ? 145 HIS B O   1 
ATOM   1078 C CB  . HIS A 1 145 ? 18.217 -9.771  38.786  1.00 28.44 ? 145 HIS B CB  1 
ATOM   1079 C CG  . HIS A 1 145 ? 16.927 -9.777  39.547  1.00 25.71 ? 145 HIS B CG  1 
ATOM   1080 N ND1 . HIS A 1 145 ? 16.869 -9.760  40.926  1.00 33.13 ? 145 HIS B ND1 1 
ATOM   1081 C CD2 . HIS A 1 145 ? 15.643 -9.805  39.115  1.00 23.24 ? 145 HIS B CD2 1 
ATOM   1082 C CE1 . HIS A 1 145 ? 15.603 -9.776  41.309  1.00 23.16 ? 145 HIS B CE1 1 
ATOM   1083 N NE2 . HIS A 1 145 ? 14.840 -9.797  40.229  1.00 29.64 ? 145 HIS B NE2 1 
ATOM   1084 N N   . TRP A 1 146 ? 16.998 -6.788  37.094  1.00 15.97 ? 146 TRP B N   1 
ATOM   1085 C CA  . TRP A 1 146 ? 16.562 -5.428  37.379  1.00 16.93 ? 146 TRP B CA  1 
ATOM   1086 C C   . TRP A 1 146 ? 15.442 -5.431  38.410  1.00 18.68 ? 146 TRP B C   1 
ATOM   1087 O O   . TRP A 1 146 ? 14.481 -6.197  38.292  1.00 17.45 ? 146 TRP B O   1 
ATOM   1088 C CB  . TRP A 1 146 ? 16.085 -4.741  36.104  1.00 14.77 ? 146 TRP B CB  1 
ATOM   1089 C CG  . TRP A 1 146 ? 15.841 -3.280  36.306  1.00 17.47 ? 146 TRP B CG  1 
ATOM   1090 C CD1 . TRP A 1 146 ? 16.755 -2.275  36.169  1.00 16.47 ? 146 TRP B CD1 1 
ATOM   1091 C CD2 . TRP A 1 146 ? 14.601 -2.652  36.672  1.00 14.56 ? 146 TRP B CD2 1 
ATOM   1092 N NE1 . TRP A 1 146 ? 16.163 -1.062  36.429  1.00 18.97 ? 146 TRP B NE1 1 
ATOM   1093 C CE2 . TRP A 1 146 ? 14.843 -1.264  36.742  1.00 17.30 ? 146 TRP B CE2 1 
ATOM   1094 C CE3 . TRP A 1 146 ? 13.316 -3.130  36.964  1.00 13.84 ? 146 TRP B CE3 1 
ATOM   1095 C CZ2 . TRP A 1 146 ? 13.846 -0.345  37.078  1.00 18.73 ? 146 TRP B CZ2 1 
ATOM   1096 C CZ3 . TRP A 1 146 ? 12.325 -2.216  37.303  1.00 14.64 ? 146 TRP B CZ3 1 
ATOM   1097 C CH2 . TRP A 1 146 ? 12.591 -0.841  37.355  1.00 14.90 ? 146 TRP B CH2 1 
ATOM   1098 N N   . VAL A 1 147 ? 15.568 -4.572  39.426  1.00 15.24 ? 147 VAL B N   1 
ATOM   1099 C CA  . VAL A 1 147 ? 14.539 -4.412  40.440  1.00 15.98 ? 147 VAL B CA  1 
ATOM   1100 C C   . VAL A 1 147 ? 14.161 -2.939  40.532  1.00 13.90 ? 147 VAL B C   1 
ATOM   1101 O O   . VAL A 1 147 ? 14.929 -2.051  40.159  1.00 13.82 ? 147 VAL B O   1 
ATOM   1102 C CB  . VAL A 1 147 ? 14.993 -4.952  41.811  1.00 12.33 ? 147 VAL B CB  1 
ATOM   1103 C CG1 . VAL A 1 147 ? 15.333 -6.431  41.707  1.00 15.97 ? 147 VAL B CG1 1 
ATOM   1104 C CG2 . VAL A 1 147 ? 16.187 -4.153  42.383  1.00 12.57 ? 147 VAL B CG2 1 
ATOM   1105 N N   . ASP A 1 148 ? 12.970 -2.687  41.065  1.00 13.86 ? 148 ASP B N   1 
ATOM   1106 C CA  . ASP A 1 148 ? 12.450 -1.332  41.268  1.00 14.93 ? 148 ASP B CA  1 
ATOM   1107 C C   . ASP A 1 148 ? 12.523 -1.032  42.768  1.00 12.19 ? 148 ASP B C   1 
ATOM   1108 O O   . ASP A 1 148 ? 11.588 -1.320  43.513  1.00 16.58 ? 148 ASP B O   1 
ATOM   1109 C CB  . ASP A 1 148 ? 11.003 -1.259  40.797  1.00 12.46 ? 148 ASP B CB  1 
ATOM   1110 C CG  . ASP A 1 148 ? 10.437 0.137   40.859  1.00 19.68 ? 148 ASP B CG  1 
ATOM   1111 O OD1 . ASP A 1 148 ? 11.194 1.099   41.093  1.00 19.82 ? 148 ASP B OD1 1 
ATOM   1112 O OD2 . ASP A 1 148 ? 9.214  0.277   40.635  1.00 24.06 ? 148 ASP B OD2 1 
ATOM   1113 N N   . GLN A 1 149 ? 13.660 -0.470  43.205  1.00 11.91 ? 149 GLN B N   1 
ATOM   1114 C CA  . GLN A 1 149 ? 13.834 -0.095  44.600  1.00 16.40 ? 149 GLN B CA  1 
ATOM   1115 C C   . GLN A 1 149 ? 14.419 1.305   44.700  1.00 16.21 ? 149 GLN B C   1 
ATOM   1116 O O   . GLN A 1 149 ? 15.145 1.760   43.811  1.00 15.79 ? 149 GLN B O   1 
ATOM   1117 C CB  . GLN A 1 149 ? 14.766 -1.085  45.316  1.00 17.23 ? 149 GLN B CB  1 
ATOM   1118 C CG  . GLN A 1 149 ? 14.230 -2.506  45.359  1.00 15.18 ? 149 GLN B CG  1 
ATOM   1119 C CD  . GLN A 1 149 ? 15.203 -3.488  45.953  1.00 15.84 ? 149 GLN B CD  1 
ATOM   1120 O OE1 . GLN A 1 149 ? 16.280 -3.102  46.402  1.00 18.53 ? 149 GLN B OE1 1 
ATOM   1121 N NE2 . GLN A 1 149 ? 14.834 -4.766  45.971  1.00 17.76 ? 149 GLN B NE2 1 
ATOM   1122 N N   . GLU A 1 150 ? 14.124 1.978   45.821  1.00 16.46 ? 150 GLU B N   1 
ATOM   1123 C CA  . GLU A 1 150 ? 14.745 3.273   46.076  1.00 14.93 ? 150 GLU B CA  1 
ATOM   1124 C C   . GLU A 1 150 ? 16.264 3.139   46.162  1.00 17.86 ? 150 GLU B C   1 
ATOM   1125 O O   . GLU A 1 150 ? 17.010 3.946   45.592  1.00 16.73 ? 150 GLU B O   1 
ATOM   1126 C CB  . GLU A 1 150 ? 14.176 3.895   47.346  1.00 13.71 ? 150 GLU B CB  1 
ATOM   1127 C CG  . GLU A 1 150 ? 14.716 5.265   47.647  1.00 17.10 ? 150 GLU B CG  1 
ATOM   1128 C CD  . GLU A 1 150 ? 14.070 5.859   48.878  1.00 22.66 ? 150 GLU B CD  1 
ATOM   1129 O OE1 . GLU A 1 150 ? 13.958 5.135   49.893  1.00 21.80 ? 150 GLU B OE1 1 
ATOM   1130 O OE2 . GLU A 1 150 ? 13.686 7.041   48.824  1.00 24.19 ? 150 GLU B OE2 1 
ATOM   1131 N N   . VAL A 1 151 ? 16.735 2.122   46.881  1.00 13.98 ? 151 VAL B N   1 
ATOM   1132 C CA  . VAL A 1 151 ? 18.146 1.748   46.919  1.00 12.60 ? 151 VAL B CA  1 
ATOM   1133 C C   . VAL A 1 151 ? 18.225 0.230   46.921  1.00 18.67 ? 151 VAL B C   1 
ATOM   1134 O O   . VAL A 1 151 ? 17.790 -0.415  47.878  1.00 16.57 ? 151 VAL B O   1 
ATOM   1135 C CB  . VAL A 1 151 ? 18.906 2.308   48.136  1.00 16.27 ? 151 VAL B CB  1 
ATOM   1136 C CG1 . VAL A 1 151 ? 20.423 2.144   47.943  1.00 17.10 ? 151 VAL B CG1 1 
ATOM   1137 C CG2 . VAL A 1 151 ? 18.563 3.744   48.398  1.00 19.47 ? 151 VAL B CG2 1 
ATOM   1138 N N   . ALA A 1 152 ? 18.805 -0.343  45.875  1.00 13.60 ? 152 ALA B N   1 
ATOM   1139 C CA  . ALA A 1 152 ? 19.081 -1.767  45.840  1.00 9.58  ? 152 ALA B CA  1 
ATOM   1140 C C   . ALA A 1 152 ? 20.535 -1.987  46.208  1.00 16.76 ? 152 ALA B C   1 
ATOM   1141 O O   . ALA A 1 152 ? 21.384 -1.134  45.957  1.00 14.52 ? 152 ALA B O   1 
ATOM   1142 C CB  . ALA A 1 152 ? 18.847 -2.334  44.440  1.00 18.52 ? 152 ALA B CB  1 
ATOM   1143 N N   . VAL A 1 153 ? 20.806 -3.137  46.810  1.00 14.74 ? 153 VAL B N   1 
ATOM   1144 C CA  . VAL A 1 153 ? 22.150 -3.526  47.221  1.00 14.80 ? 153 VAL B CA  1 
ATOM   1145 C C   . VAL A 1 153 ? 22.367 -4.978  46.838  1.00 15.54 ? 153 VAL B C   1 
ATOM   1146 O O   . VAL A 1 153 ? 21.519 -5.837  47.118  1.00 19.92 ? 153 VAL B O   1 
ATOM   1147 C CB  . VAL A 1 153 ? 22.375 -3.340  48.732  1.00 13.18 ? 153 VAL B CB  1 
ATOM   1148 C CG1 . VAL A 1 153 ? 23.669 -4.015  49.133  1.00 16.94 ? 153 VAL B CG1 1 
ATOM   1149 C CG2 . VAL A 1 153 ? 22.481 -1.866  49.072  1.00 17.47 ? 153 VAL B CG2 1 
ATOM   1150 N N   . ASP A 1 154 ? 23.499 -5.250  46.189  1.00 13.18 ? 154 ASP B N   1 
ATOM   1151 C CA  . ASP A 1 154 ? 23.915 -6.613  45.880  1.00 14.27 ? 154 ASP B CA  1 
ATOM   1152 C C   . ASP A 1 154 ? 25.390 -6.676  46.242  1.00 17.42 ? 154 ASP B C   1 
ATOM   1153 O O   . ASP A 1 154 ? 26.248 -6.243  45.470  1.00 17.28 ? 154 ASP B O   1 
ATOM   1154 C CB  . ASP A 1 154 ? 23.648 -6.978  44.420  1.00 17.30 ? 154 ASP B CB  1 
ATOM   1155 C CG  . ASP A 1 154 ? 23.915 -8.444  44.133  1.00 23.53 ? 154 ASP B CG  1 
ATOM   1156 O OD1 . ASP A 1 154 ? 24.545 -9.116  44.980  1.00 31.84 ? 154 ASP B OD1 1 
ATOM   1157 O OD2 . ASP A 1 154 ? 23.528 -8.931  43.050  1.00 28.22 ? 154 ASP B OD2 1 
ATOM   1158 N N   . GLY A 1 155 ? 25.668 -7.190  47.432  1.00 15.65 ? 155 GLY B N   1 
ATOM   1159 C CA  . GLY A 1 155 ? 27.019 -7.135  47.940  1.00 16.84 ? 155 GLY B CA  1 
ATOM   1160 C C   . GLY A 1 155 ? 27.429 -5.703  48.208  1.00 22.91 ? 155 GLY B C   1 
ATOM   1161 O O   . GLY A 1 155 ? 26.877 -5.043  49.089  1.00 17.77 ? 155 GLY B O   1 
ATOM   1162 N N   . LYS A 1 156 ? 28.410 -5.202  47.464  1.00 17.58 ? 156 LYS B N   1 
ATOM   1163 C CA  . LYS A 1 156 ? 28.824 -3.810  47.591  1.00 15.33 ? 156 LYS B CA  1 
ATOM   1164 C C   . LYS A 1 156 ? 28.375 -2.945  46.415  1.00 16.97 ? 156 LYS B C   1 
ATOM   1165 O O   . LYS A 1 156 ? 28.817 -1.798  46.289  1.00 15.51 ? 156 LYS B O   1 
ATOM   1166 C CB  . LYS A 1 156 ? 30.331 -3.722  47.846  1.00 16.72 ? 156 LYS B CB  1 
ATOM   1167 C CG  . LYS A 1 156 ? 30.739 -4.501  49.087  1.00 22.43 ? 156 LYS B CG  1 
ATOM   1168 C CD  . LYS A 1 156 ? 32.243 -4.470  49.336  1.00 25.43 ? 156 LYS B CD  1 
ATOM   1169 C CE  . LYS A 1 156 ? 32.592 -5.305  50.575  1.00 24.46 ? 156 LYS B CE  1 
ATOM   1170 N NZ  . LYS A 1 156 ? 34.071 -5.519  50.848  1.00 28.47 ? 156 LYS B NZ  1 
ATOM   1171 N N   . LEU A 1 157 ? 27.497 -3.464  45.564  1.00 15.40 ? 157 LEU B N   1 
ATOM   1172 C CA  . LEU A 1 157 ? 26.914 -2.689  44.472  1.00 17.82 ? 157 LEU B CA  1 
ATOM   1173 C C   . LEU A 1 157 ? 25.644 -2.019  44.989  1.00 10.06 ? 157 LEU B C   1 
ATOM   1174 O O   . LEU A 1 157 ? 24.674 -2.697  45.322  1.00 16.10 ? 157 LEU B O   1 
ATOM   1175 C CB  . LEU A 1 157 ? 26.614 -3.592  43.276  1.00 16.56 ? 157 LEU B CB  1 
ATOM   1176 C CG  . LEU A 1 157 ? 25.940 -2.905  42.082  1.00 16.02 ? 157 LEU B CG  1 
ATOM   1177 C CD1 . LEU A 1 157 ? 26.784 -1.745  41.560  1.00 18.72 ? 157 LEU B CD1 1 
ATOM   1178 C CD2 . LEU A 1 157 ? 25.606 -3.882  40.945  1.00 18.24 ? 157 LEU B CD2 1 
ATOM   1179 N N   . VAL A 1 158 ? 25.655 -0.689  45.057  1.00 13.49 ? 158 VAL B N   1 
ATOM   1180 C CA  . VAL A 1 158 ? 24.553 0.095   45.607  1.00 16.87 ? 158 VAL B CA  1 
ATOM   1181 C C   . VAL A 1 158 ? 23.967 0.911   44.465  1.00 16.70 ? 158 VAL B C   1 
ATOM   1182 O O   . VAL A 1 158 ? 24.698 1.658   43.805  1.00 16.03 ? 158 VAL B O   1 
ATOM   1183 C CB  . VAL A 1 158 ? 25.061 1.026   46.728  1.00 16.02 ? 158 VAL B CB  1 
ATOM   1184 C CG1 . VAL A 1 158 ? 23.932 1.849   47.300  1.00 21.65 ? 158 VAL B CG1 1 
ATOM   1185 C CG2 . VAL A 1 158 ? 25.767 0.234   47.825  1.00 16.18 ? 158 VAL B CG2 1 
ATOM   1186 N N   . SER A 1 159 ? 22.652 0.783   44.232  1.00 13.83 ? 159 SER B N   1 
ATOM   1187 C CA  . SER A 1 159 ? 22.056 1.403   43.053  1.00 15.74 ? 159 SER B CA  1 
ATOM   1188 C C   . SER A 1 159 ? 20.732 2.089   43.380  1.00 14.87 ? 159 SER B C   1 
ATOM   1189 O O   . SER A 1 159 ? 19.946 1.597   44.196  1.00 17.32 ? 159 SER B O   1 
ATOM   1190 C CB  . SER A 1 159 ? 21.885 0.393   41.889  1.00 14.38 ? 159 SER B CB  1 
ATOM   1191 O OG  . SER A 1 159 ? 21.114 -0.727  42.285  1.00 16.84 ? 159 SER B OG  1 
ATOM   1192 N N   . SER A 1 160 ? 20.501 3.232   42.738  1.00 14.18 ? 160 SER B N   1 
ATOM   1193 C CA  . SER A 1 160 ? 19.274 3.998   42.922  1.00 16.97 ? 160 SER B CA  1 
ATOM   1194 C C   . SER A 1 160 ? 18.762 4.394   41.543  1.00 13.78 ? 160 SER B C   1 
ATOM   1195 O O   . SER A 1 160 ? 19.422 4.170   40.526  1.00 13.15 ? 160 SER B O   1 
ATOM   1196 C CB  . SER A 1 160 ? 19.531 5.242   43.775  1.00 15.40 ? 160 SER B CB  1 
ATOM   1197 O OG  . SER A 1 160 ? 19.571 4.896   45.151  1.00 16.42 ? 160 SER B OG  1 
ATOM   1198 N N   . ARG A 1 161 ? 17.570 4.983   41.502  1.00 17.08 ? 161 ARG B N   1 
ATOM   1199 C CA  . ARG A 1 161 ? 16.877 5.190   40.237  1.00 16.14 ? 161 ARG B CA  1 
ATOM   1200 C C   . ARG A 1 161 ? 16.871 6.623   39.744  1.00 14.46 ? 161 ARG B C   1 
ATOM   1201 O O   . ARG A 1 161 ? 16.733 6.828   38.537  1.00 16.75 ? 161 ARG B O   1 
ATOM   1202 C CB  . ARG A 1 161 ? 15.407 4.756   40.344  1.00 15.18 ? 161 ARG B CB  1 
ATOM   1203 C CG  . ARG A 1 161 ? 15.174 3.426   41.006  1.00 14.24 ? 161 ARG B CG  1 
ATOM   1204 C CD  . ARG A 1 161 ? 13.727 3.300   41.380  1.00 14.96 ? 161 ARG B CD  1 
ATOM   1205 N NE  . ARG A 1 161 ? 13.470 4.167   42.519  1.00 16.06 ? 161 ARG B NE  1 
ATOM   1206 C CZ  . ARG A 1 161 ? 12.443 4.030   43.347  1.00 16.64 ? 161 ARG B CZ  1 
ATOM   1207 N NH1 . ARG A 1 161 ? 11.545 3.074   43.175  1.00 17.89 ? 161 ARG B NH1 1 
ATOM   1208 N NH2 . ARG A 1 161 ? 12.305 4.883   44.358  1.00 16.89 ? 161 ARG B NH2 1 
ATOM   1209 N N   . LYS A 1 162 ? 16.897 7.612   40.628  1.00 18.51 ? 162 LYS B N   1 
ATOM   1210 C CA  . LYS A 1 162 ? 16.543 8.975   40.245  1.00 17.66 ? 162 LYS B CA  1 
ATOM   1211 C C   . LYS A 1 162 ? 16.983 9.922   41.354  1.00 21.57 ? 162 LYS B C   1 
ATOM   1212 O O   . LYS A 1 162 ? 17.241 9.483   42.480  1.00 15.99 ? 162 LYS B O   1 
ATOM   1213 C CB  . LYS A 1 162 ? 15.026 9.110   40.000  1.00 22.39 ? 162 LYS B CB  1 
ATOM   1214 C CG  . LYS A 1 162 ? 14.173 8.782   41.207  1.00 22.90 ? 162 LYS B CG  1 
ATOM   1215 C CD  . LYS A 1 162 ? 12.786 8.323   40.821  1.00 20.91 ? 162 LYS B CD  1 
ATOM   1216 C CE  . LYS A 1 162 ? 12.042 7.794   42.028  1.00 24.78 ? 162 LYS B CE  1 
ATOM   1217 N NZ  . LYS A 1 162 ? 10.567 7.684   41.786  1.00 23.85 ? 162 LYS B NZ  1 
ATOM   1218 N N   . PRO A 1 163 ? 17.039 11.227  41.068  1.00 21.98 ? 163 PRO B N   1 
ATOM   1219 C CA  . PRO A 1 163 ? 17.494 12.183  42.093  1.00 22.66 ? 163 PRO B CA  1 
ATOM   1220 C C   . PRO A 1 163 ? 16.700 12.153  43.391  1.00 19.28 ? 163 PRO B C   1 
ATOM   1221 O O   . PRO A 1 163 ? 17.276 12.409  44.454  1.00 19.42 ? 163 PRO B O   1 
ATOM   1222 C CB  . PRO A 1 163 ? 17.361 13.535  41.380  1.00 18.46 ? 163 PRO B CB  1 
ATOM   1223 C CG  . PRO A 1 163 ? 17.578 13.200  39.945  1.00 16.03 ? 163 PRO B CG  1 
ATOM   1224 C CD  . PRO A 1 163 ? 16.879 11.876  39.755  1.00 16.03 ? 163 PRO B CD  1 
ATOM   1225 N N   . GLU A 1 164 ? 15.392 11.866  43.360  1.00 19.37 ? 164 GLU B N   1 
ATOM   1226 C CA  . GLU A 1 164 ? 14.649 11.798  44.622  1.00 19.10 ? 164 GLU B CA  1 
ATOM   1227 C C   . GLU A 1 164 ? 15.133 10.671  45.528  1.00 19.05 ? 164 GLU B C   1 
ATOM   1228 O O   . GLU A 1 164 ? 14.909 10.727  46.745  1.00 17.95 ? 164 GLU B O   1 
ATOM   1229 C CB  . GLU A 1 164 ? 13.121 11.725  44.423  1.00 22.45 ? 164 GLU B CB  1 
ATOM   1230 C CG  . GLU A 1 164 ? 12.445 12.815  43.557  1.00 27.36 ? 164 GLU B CG  1 
ATOM   1231 C CD  . GLU A 1 164 ? 13.135 13.114  42.239  1.00 50.46 ? 164 GLU B CD  1 
ATOM   1232 O OE1 . GLU A 1 164 ? 13.472 14.294  42.008  1.00 59.85 ? 164 GLU B OE1 1 
ATOM   1233 O OE2 . GLU A 1 164 ? 13.345 12.175  41.439  1.00 52.33 ? 164 GLU B OE2 1 
ATOM   1234 N N   . ASP A 1 165 ? 15.775 9.646   44.966  1.00 15.43 ? 165 ASP B N   1 
ATOM   1235 C CA  . ASP A 1 165 ? 16.347 8.568   45.768  1.00 15.97 ? 165 ASP B CA  1 
ATOM   1236 C C   . ASP A 1 165 ? 17.646 8.954   46.480  1.00 16.58 ? 165 ASP B C   1 
ATOM   1237 O O   . ASP A 1 165 ? 18.123 8.157   47.294  1.00 17.65 ? 165 ASP B O   1 
ATOM   1238 C CB  . ASP A 1 165 ? 16.664 7.361   44.875  1.00 15.59 ? 165 ASP B CB  1 
ATOM   1239 C CG  . ASP A 1 165 ? 15.422 6.721   44.260  1.00 17.57 ? 165 ASP B CG  1 
ATOM   1240 O OD1 . ASP A 1 165 ? 14.278 6.931   44.738  1.00 17.73 ? 165 ASP B OD1 1 
ATOM   1241 O OD2 . ASP A 1 165 ? 15.585 5.957   43.293  1.00 18.54 ? 165 ASP B OD2 1 
ATOM   1242 N N   . ILE A 1 166 ? 18.226 10.128  46.186  1.00 16.02 ? 166 ILE B N   1 
ATOM   1243 C CA  . ILE A 1 166 ? 19.575 10.448  46.676  1.00 15.22 ? 166 ILE B CA  1 
ATOM   1244 C C   . ILE A 1 166 ? 19.724 10.361  48.194  1.00 13.69 ? 166 ILE B C   1 
ATOM   1245 O O   . ILE A 1 166 ? 20.702 9.755   48.660  1.00 15.06 ? 166 ILE B O   1 
ATOM   1246 C CB  . ILE A 1 166 ? 20.073 11.768  46.068  1.00 16.93 ? 166 ILE B CB  1 
ATOM   1247 C CG1 . ILE A 1 166 ? 20.464 11.550  44.607  1.00 16.19 ? 166 ILE B CG1 1 
ATOM   1248 C CG2 . ILE A 1 166 ? 21.242 12.323  46.873  1.00 16.49 ? 166 ILE B CG2 1 
ATOM   1249 C CD1 . ILE A 1 166 ? 20.825 12.821  43.848  1.00 17.34 ? 166 ILE B CD1 1 
ATOM   1250 N N   . PRO A 1 167 ? 18.847 10.956  49.008  1.00 13.49 ? 167 PRO B N   1 
ATOM   1251 C CA  . PRO A 1 167 ? 19.036 10.817  50.461  1.00 14.03 ? 167 PRO B CA  1 
ATOM   1252 C C   . PRO A 1 167 ? 19.204 9.372   50.907  1.00 16.81 ? 167 PRO B C   1 
ATOM   1253 O O   . PRO A 1 167 ? 20.129 9.054   51.671  1.00 15.00 ? 167 PRO B O   1 
ATOM   1254 C CB  . PRO A 1 167 ? 17.791 11.507  51.037  1.00 17.32 ? 167 PRO B CB  1 
ATOM   1255 C CG  . PRO A 1 167 ? 17.392 12.483  50.000  1.00 19.80 ? 167 PRO B CG  1 
ATOM   1256 C CD  . PRO A 1 167 ? 17.696 11.817  48.688  1.00 13.68 ? 167 PRO B CD  1 
ATOM   1257 N N   . ALA A 1 168 ? 18.346 8.476   50.415  1.00 15.55 ? 168 ALA B N   1 
ATOM   1258 C CA  . ALA A 1 168 ? 18.443 7.069   50.785  1.00 15.70 ? 168 ALA B CA  1 
ATOM   1259 C C   . ALA A 1 168 ? 19.666 6.420   50.164  1.00 17.80 ? 168 ALA B C   1 
ATOM   1260 O O   . ALA A 1 168 ? 20.298 5.557   50.780  1.00 15.01 ? 168 ALA B O   1 
ATOM   1261 C CB  . ALA A 1 168 ? 17.178 6.327   50.359  1.00 20.77 ? 168 ALA B CB  1 
ATOM   1262 N N   . PHE A 1 169 ? 19.978 6.797   48.921  1.00 15.71 ? 169 PHE B N   1 
ATOM   1263 C CA  . PHE A 1 169 ? 21.204 6.365   48.254  1.00 15.18 ? 169 PHE B CA  1 
ATOM   1264 C C   . PHE A 1 169 ? 22.434 6.742   49.066  1.00 15.24 ? 169 PHE B C   1 
ATOM   1265 O O   . PHE A 1 169 ? 23.321 5.906   49.300  1.00 17.09 ? 169 PHE B O   1 
ATOM   1266 C CB  . PHE A 1 169 ? 21.226 7.058   46.893  1.00 11.19 ? 169 PHE B CB  1 
ATOM   1267 C CG  . PHE A 1 169 ? 22.420 6.739   46.011  1.00 15.82 ? 169 PHE B CG  1 
ATOM   1268 C CD1 . PHE A 1 169 ? 22.540 5.516   45.363  1.00 12.94 ? 169 PHE B CD1 1 
ATOM   1269 C CD2 . PHE A 1 169 ? 23.405 7.698   45.814  1.00 14.59 ? 169 PHE B CD2 1 
ATOM   1270 C CE1 . PHE A 1 169 ? 23.603 5.258   44.522  1.00 14.52 ? 169 PHE B CE1 1 
ATOM   1271 C CE2 . PHE A 1 169 ? 24.479 7.447   44.952  1.00 16.74 ? 169 PHE B CE2 1 
ATOM   1272 C CZ  . PHE A 1 169 ? 24.576 6.219   44.322  1.00 18.54 ? 169 PHE B CZ  1 
ATOM   1273 N N   . ASN A 1 170 ? 22.495 7.999   49.517  1.00 15.25 ? 170 ASN B N   1 
ATOM   1274 C CA  . ASN A 1 170 ? 23.615 8.438   50.355  1.00 14.85 ? 170 ASN B CA  1 
ATOM   1275 C C   . ASN A 1 170 ? 23.698 7.613   51.636  1.00 17.27 ? 170 ASN B C   1 
ATOM   1276 O O   . ASN A 1 170 ? 24.767 7.120   52.003  1.00 17.78 ? 170 ASN B O   1 
ATOM   1277 C CB  . ASN A 1 170 ? 23.474 9.918   50.705  1.00 17.27 ? 170 ASN B CB  1 
ATOM   1278 C CG  . ASN A 1 170 ? 23.602 10.825  49.512  1.00 15.71 ? 170 ASN B CG  1 
ATOM   1279 O OD1 . ASN A 1 170 ? 24.055 10.414  48.444  1.00 19.51 ? 170 ASN B OD1 1 
ATOM   1280 N ND2 . ASN A 1 170 ? 23.171 12.071  49.679  1.00 21.40 ? 170 ASN B ND2 1 
ATOM   1281 N N   . ARG A 1 171 ? 22.570 7.435   52.321  1.00 15.76 ? 171 ARG B N   1 
ATOM   1282 C CA  . ARG A 1 171 ? 22.613 6.732   53.601  1.00 15.15 ? 171 ARG B CA  1 
ATOM   1283 C C   . ARG A 1 171 ? 23.078 5.293   53.430  1.00 18.12 ? 171 ARG B C   1 
ATOM   1284 O O   . ARG A 1 171 ? 23.872 4.789   54.237  1.00 18.85 ? 171 ARG B O   1 
ATOM   1285 C CB  . ARG A 1 171 ? 21.242 6.769   54.268  1.00 15.59 ? 171 ARG B CB  1 
ATOM   1286 C CG  . ARG A 1 171 ? 20.788 8.138   54.764  1.00 15.58 ? 171 ARG B CG  1 
ATOM   1287 C CD  . ARG A 1 171 ? 19.528 8.001   55.602  1.00 23.40 ? 171 ARG B CD  1 
ATOM   1288 N NE  . ARG A 1 171 ? 18.368 7.533   54.841  1.00 22.01 ? 171 ARG B NE  1 
ATOM   1289 C CZ  . ARG A 1 171 ? 17.516 8.325   54.199  1.00 19.49 ? 171 ARG B CZ  1 
ATOM   1290 N NH1 . ARG A 1 171 ? 17.728 9.626   54.095  1.00 20.15 ? 171 ARG B NH1 1 
ATOM   1291 N NH2 . ARG A 1 171 ? 16.422 7.800   53.654  1.00 23.02 ? 171 ARG B NH2 1 
ATOM   1292 N N   . ARG A 1 172 ? 22.635 4.634   52.353  1.00 16.10 ? 172 ARG B N   1 
ATOM   1293 C CA  . ARG A 1 172 ? 23.030 3.252   52.118  1.00 14.98 ? 172 ARG B CA  1 
ATOM   1294 C C   . ARG A 1 172 ? 24.494 3.159   51.733  1.00 15.42 ? 172 ARG B C   1 
ATOM   1295 O O   . ARG A 1 172 ? 25.200 2.265   52.203  1.00 16.62 ? 172 ARG B O   1 
ATOM   1296 C CB  . ARG A 1 172 ? 22.162 2.627   51.034  1.00 15.87 ? 172 ARG B CB  1 
ATOM   1297 C CG  . ARG A 1 172 ? 22.205 1.114   50.978  1.00 13.93 ? 172 ARG B CG  1 
ATOM   1298 C CD  . ARG A 1 172 ? 21.326 0.518   52.081  1.00 15.29 ? 172 ARG B CD  1 
ATOM   1299 N NE  . ARG A 1 172 ? 21.411 -0.935  52.129  1.00 16.38 ? 172 ARG B NE  1 
ATOM   1300 C CZ  . ARG A 1 172 ? 22.345 -1.606  52.796  1.00 15.71 ? 172 ARG B CZ  1 
ATOM   1301 N NH1 . ARG A 1 172 ? 23.254 -0.982  53.520  1.00 19.83 ? 172 ARG B NH1 1 
ATOM   1302 N NH2 . ARG A 1 172 ? 22.391 -2.932  52.695  1.00 19.31 ? 172 ARG B NH2 1 
ATOM   1303 N N   . PHE A 1 173 ? 24.944 4.045   50.842  1.00 17.38 ? 173 PHE B N   1 
ATOM   1304 C CA  . PHE A 1 173 ? 26.347 4.080   50.449  1.00 12.83 ? 173 PHE B CA  1 
ATOM   1305 C C   . PHE A 1 173 ? 27.252 4.221   51.663  1.00 18.16 ? 173 PHE B C   1 
ATOM   1306 O O   . PHE A 1 173 ? 28.258 3.511   51.786  1.00 16.98 ? 173 PHE B O   1 
ATOM   1307 C CB  . PHE A 1 173 ? 26.551 5.252   49.488  1.00 19.96 ? 173 PHE B CB  1 
ATOM   1308 C CG  . PHE A 1 173 ? 27.838 5.204   48.693  1.00 15.43 ? 173 PHE B CG  1 
ATOM   1309 C CD1 . PHE A 1 173 ? 28.646 4.075   48.658  1.00 17.65 ? 173 PHE B CD1 1 
ATOM   1310 C CD2 . PHE A 1 173 ? 28.210 6.304   47.950  1.00 14.53 ? 173 PHE B CD2 1 
ATOM   1311 C CE1 . PHE A 1 173 ? 29.822 4.061   47.893  1.00 21.82 ? 173 PHE B CE1 1 
ATOM   1312 C CE2 . PHE A 1 173 ? 29.375 6.309   47.197  1.00 16.74 ? 173 PHE B CE2 1 
ATOM   1313 C CZ  . PHE A 1 173 ? 30.186 5.185   47.166  1.00 17.68 ? 173 PHE B CZ  1 
ATOM   1314 N N   . ILE A 1 174 ? 26.912 5.135   52.571  1.00 16.14 ? 174 ILE B N   1 
ATOM   1315 C CA  . ILE A 1 174 ? 27.737 5.326   53.763  1.00 14.40 ? 174 ILE B CA  1 
ATOM   1316 C C   . ILE A 1 174 ? 27.845 4.028   54.553  1.00 17.37 ? 174 ILE B C   1 
ATOM   1317 O O   . ILE A 1 174 ? 28.939 3.621   54.956  1.00 15.86 ? 174 ILE B O   1 
ATOM   1318 C CB  . ILE A 1 174 ? 27.202 6.509   54.589  1.00 15.64 ? 174 ILE B CB  1 
ATOM   1319 C CG1 . ILE A 1 174 ? 27.539 7.816   53.855  1.00 18.61 ? 174 ILE B CG1 1 
ATOM   1320 C CG2 . ILE A 1 174 ? 27.758 6.480   56.030  1.00 14.92 ? 174 ILE B CG2 1 
ATOM   1321 C CD1 . ILE A 1 174 ? 26.719 9.008   54.266  1.00 14.97 ? 174 ILE B CD1 1 
ATOM   1322 N N   . GLU A 1 175 ? 26.725 3.319   54.712  1.00 15.98 ? 175 GLU B N   1 
ATOM   1323 C CA  . GLU A 1 175 ? 26.719 2.047   55.439  1.00 14.37 ? 175 GLU B CA  1 
ATOM   1324 C C   . GLU A 1 175 ? 27.609 1.018   54.770  1.00 11.34 ? 175 GLU B C   1 
ATOM   1325 O O   . GLU A 1 175 ? 28.404 0.333   55.434  1.00 16.00 ? 175 GLU B O   1 
ATOM   1326 C CB  . GLU A 1 175 ? 25.295 1.492   55.496  1.00 14.80 ? 175 GLU B CB  1 
ATOM   1327 C CG  . GLU A 1 175 ? 24.358 2.190   56.476  1.00 15.54 ? 175 GLU B CG  1 
ATOM   1328 C CD  . GLU A 1 175 ? 22.949 1.622   56.451  1.00 19.99 ? 175 GLU B CD  1 
ATOM   1329 O OE1 . GLU A 1 175 ? 22.453 1.211   55.365  1.00 22.45 ? 175 GLU B OE1 1 
ATOM   1330 O OE2 . GLU A 1 175 ? 22.335 1.595   57.524  1.00 21.09 ? 175 GLU B OE2 1 
ATOM   1331 N N   . ILE A 1 176 ? 27.470 0.873   53.448  1.00 13.46 ? 176 ILE B N   1 
ATOM   1332 C CA  . ILE A 1 176 ? 28.240 -0.120  52.713  1.00 16.24 ? 176 ILE B CA  1 
ATOM   1333 C C   . ILE A 1 176 ? 29.722 0.237   52.727  1.00 16.17 ? 176 ILE B C   1 
ATOM   1334 O O   . ILE A 1 176 ? 30.582 -0.643  52.838  1.00 18.75 ? 176 ILE B O   1 
ATOM   1335 C CB  . ILE A 1 176 ? 27.682 -0.249  51.280  1.00 14.80 ? 176 ILE B CB  1 
ATOM   1336 C CG1 . ILE A 1 176 ? 26.280 -0.887  51.297  1.00 19.06 ? 176 ILE B CG1 1 
ATOM   1337 C CG2 . ILE A 1 176 ? 28.639 -1.002  50.390  1.00 15.40 ? 176 ILE B CG2 1 
ATOM   1338 C CD1 . ILE A 1 176 ? 26.286 -2.339  51.762  1.00 22.99 ? 176 ILE B CD1 1 
ATOM   1339 N N   . LEU A 1 177 ? 30.041 1.530   52.625  1.00 12.40 ? 177 LEU B N   1 
ATOM   1340 C CA  . LEU A 1 177 ? 31.437 1.962   52.617  1.00 16.39 ? 177 LEU B CA  1 
ATOM   1341 C C   . LEU A 1 177 ? 32.113 1.648   53.940  1.00 14.41 ? 177 LEU B C   1 
ATOM   1342 O O   . LEU A 1 177 ? 33.270 1.214   53.966  1.00 16.66 ? 177 LEU B O   1 
ATOM   1343 C CB  . LEU A 1 177 ? 31.499 3.463   52.385  1.00 18.69 ? 177 LEU B CB  1 
ATOM   1344 C CG  . LEU A 1 177 ? 31.626 3.834   50.916  1.00 24.45 ? 177 LEU B CG  1 
ATOM   1345 C CD1 . LEU A 1 177 ? 31.477 5.332   50.763  1.00 25.23 ? 177 LEU B CD1 1 
ATOM   1346 C CD2 . LEU A 1 177 ? 32.955 3.358   50.381  1.00 28.12 ? 177 LEU B CD2 1 
ATOM   1347 N N   . ALA A 1 178 ? 31.407 1.876   55.052  1.00 15.10 ? 178 ALA B N   1 
ATOM   1348 C CA  . ALA A 1 178 ? 31.976 1.601   56.367  1.00 16.59 ? 178 ALA B CA  1 
ATOM   1349 C C   . ALA A 1 178 ? 32.211 0.111   56.573  1.00 16.11 ? 178 ALA B C   1 
ATOM   1350 O O   . ALA A 1 178 ? 33.253 -0.288  57.098  1.00 15.86 ? 178 ALA B O   1 
ATOM   1351 C CB  . ALA A 1 178 ? 31.041 2.150   57.446  1.00 17.00 ? 178 ALA B CB  1 
ATOM   1352 N N   A GLY A 1 179 ? 31.261 -0.729  56.166  0.50 18.98 ? 179 GLY B N   1 
ATOM   1353 N N   B GLY A 1 179 ? 31.253 -0.726  56.180  0.50 19.01 ? 179 GLY B N   1 
ATOM   1354 C CA  A GLY A 1 179 ? 31.380 -2.168  56.342  0.50 16.73 ? 179 GLY B CA  1 
ATOM   1355 C CA  B GLY A 1 179 ? 31.349 -2.160  56.390  0.50 16.72 ? 179 GLY B CA  1 
ATOM   1356 C C   A GLY A 1 179 ? 31.239 -2.644  57.779  0.50 17.92 ? 179 GLY B C   1 
ATOM   1357 C C   B GLY A 1 179 ? 31.227 -2.585  57.846  0.50 17.93 ? 179 GLY B C   1 
ATOM   1358 O O   A GLY A 1 179 ? 31.389 -3.832  58.070  0.50 14.16 ? 179 GLY B O   1 
ATOM   1359 O O   B GLY A 1 179 ? 30.762 -1.821  58.697  0.50 12.04 ? 179 GLY B O   1 
ATOM   1360 N N   . THR B 1 2   ? 15.157 8.373   -11.738 1.00 41.20 ? 2   THR X N   1 
ATOM   1361 C CA  . THR B 1 2   ? 15.165 8.583   -10.295 1.00 31.60 ? 2   THR X CA  1 
ATOM   1362 C C   . THR B 1 2   ? 13.919 7.954   -9.670  1.00 26.94 ? 2   THR X C   1 
ATOM   1363 O O   . THR B 1 2   ? 12.803 8.178   -10.138 1.00 27.29 ? 2   THR X O   1 
ATOM   1364 C CB  . THR B 1 2   ? 15.248 10.083  -9.944  1.00 38.55 ? 2   THR X CB  1 
ATOM   1365 O OG1 . THR B 1 2   ? 16.600 10.527  -10.100 1.00 48.91 ? 2   THR X OG1 1 
ATOM   1366 C CG2 . THR B 1 2   ? 14.830 10.329  -8.503  1.00 38.36 ? 2   THR X CG2 1 
ATOM   1367 N N   . GLN B 1 3   ? 14.128 7.166   -8.617  1.00 20.11 ? 3   GLN X N   1 
ATOM   1368 C CA  . GLN B 1 3   ? 13.049 6.404   -8.005  1.00 24.57 ? 3   GLN X CA  1 
ATOM   1369 C C   . GLN B 1 3   ? 11.978 7.341   -7.469  1.00 21.43 ? 3   GLN X C   1 
ATOM   1370 O O   . GLN B 1 3   ? 12.274 8.272   -6.712  1.00 22.92 ? 3   GLN X O   1 
ATOM   1371 C CB  . GLN B 1 3   ? 13.618 5.588   -6.848  1.00 22.68 ? 3   GLN X CB  1 
ATOM   1372 C CG  . GLN B 1 3   ? 12.582 4.786   -6.060  1.00 21.76 ? 3   GLN X CG  1 
ATOM   1373 C CD  . GLN B 1 3   ? 11.948 3.687   -6.882  1.00 20.31 ? 3   GLN X CD  1 
ATOM   1374 O OE1 . GLN B 1 3   ? 12.614 2.713   -7.230  1.00 20.86 ? 3   GLN X OE1 1 
ATOM   1375 N NE2 . GLN B 1 3   ? 10.638 3.805   -7.153  1.00 17.05 ? 3   GLN X NE2 1 
ATOM   1376 N N   . SER B 1 4   ? 10.728 7.084   -7.837  1.00 18.36 ? 4   SER X N   1 
ATOM   1377 C CA  . SER B 1 4   ? 9.605  7.834   -7.287  1.00 18.63 ? 4   SER X CA  1 
ATOM   1378 C C   . SER B 1 4   ? 9.022  7.089   -6.094  1.00 16.94 ? 4   SER X C   1 
ATOM   1379 O O   . SER B 1 4   ? 8.820  5.872   -6.152  1.00 17.27 ? 4   SER X O   1 
ATOM   1380 C CB  . SER B 1 4   ? 8.509  8.037   -8.335  1.00 16.68 ? 4   SER X CB  1 
ATOM   1381 O OG  . SER B 1 4   ? 7.367  8.636   -7.750  1.00 21.19 ? 4   SER X OG  1 
ATOM   1382 N N   . LEU B 1 5   ? 8.760  7.821   -5.009  1.00 15.75 ? 5   LEU X N   1 
ATOM   1383 C CA  . LEU B 1 5   ? 7.995  7.291   -3.894  1.00 18.12 ? 5   LEU X CA  1 
ATOM   1384 C C   . LEU B 1 5   ? 6.610  7.918   -3.817  1.00 17.69 ? 5   LEU X C   1 
ATOM   1385 O O   . LEU B 1 5   ? 6.021  7.958   -2.736  1.00 17.85 ? 5   LEU X O   1 
ATOM   1386 C CB  . LEU B 1 5   ? 8.728  7.523   -2.574  1.00 15.74 ? 5   LEU X CB  1 
ATOM   1387 C CG  . LEU B 1 5   ? 10.069 6.796   -2.515  1.00 19.58 ? 5   LEU X CG  1 
ATOM   1388 C CD1 . LEU B 1 5   ? 10.720 7.132   -1.199  1.00 20.38 ? 5   LEU X CD1 1 
ATOM   1389 C CD2 . LEU B 1 5   ? 9.936  5.293   -2.714  1.00 20.18 ? 5   LEU X CD2 1 
ATOM   1390 N N   . HIS B 1 6   ? 6.081  8.434   -4.932  1.00 15.01 ? 6   HIS X N   1 
ATOM   1391 C CA  . HIS B 1 6   ? 4.768  9.055   -4.860  1.00 15.59 ? 6   HIS X CA  1 
ATOM   1392 C C   . HIS B 1 6   ? 3.769  8.056   -4.303  1.00 16.89 ? 6   HIS X C   1 
ATOM   1393 O O   . HIS B 1 6   ? 3.788  6.871   -4.647  1.00 17.75 ? 6   HIS X O   1 
ATOM   1394 C CB  . HIS B 1 6   ? 4.323  9.558   -6.234  1.00 20.25 ? 6   HIS X CB  1 
ATOM   1395 C CG  . HIS B 1 6   ? 3.100  10.422  -6.181  1.00 31.14 ? 6   HIS X CG  1 
ATOM   1396 N ND1 . HIS B 1 6   ? 2.871  11.322  -5.161  1.00 40.81 ? 6   HIS X ND1 1 
ATOM   1397 C CD2 . HIS B 1 6   ? 2.027  10.509  -7.003  1.00 34.51 ? 6   HIS X CD2 1 
ATOM   1398 C CE1 . HIS B 1 6   ? 1.716  11.931  -5.365  1.00 40.85 ? 6   HIS X CE1 1 
ATOM   1399 N NE2 . HIS B 1 6   ? 1.184  11.456  -6.476  1.00 37.34 ? 6   HIS X NE2 1 
ATOM   1400 N N   . GLY B 1 7   ? 2.915  8.541   -3.405  1.00 17.45 ? 7   GLY X N   1 
ATOM   1401 C CA  . GLY B 1 7   ? 1.898  7.726   -2.789  1.00 15.42 ? 7   GLY X CA  1 
ATOM   1402 C C   . GLY B 1 7   ? 2.330  7.058   -1.510  1.00 20.08 ? 7   GLY X C   1 
ATOM   1403 O O   . GLY B 1 7   ? 1.469  6.554   -0.783  1.00 19.99 ? 7   GLY X O   1 
ATOM   1404 N N   . LYS B 1 8   ? 3.636  7.110   -1.227  1.00 15.02 ? 8   LYS X N   1 
ATOM   1405 C CA  . LYS B 1 8   ? 4.168  6.496   0.025   1.00 14.75 ? 8   LYS X CA  1 
ATOM   1406 C C   . LYS B 1 8   ? 4.080  7.487   1.186   1.00 14.49 ? 8   LYS X C   1 
ATOM   1407 O O   . LYS B 1 8   ? 4.273  8.654   0.965   1.00 16.54 ? 8   LYS X O   1 
ATOM   1408 C CB  . LYS B 1 8   ? 5.580  5.929   -0.139  1.00 19.31 ? 8   LYS X CB  1 
ATOM   1409 C CG  . LYS B 1 8   ? 5.740  4.893   -1.242  1.00 23.10 ? 8   LYS X CG  1 
ATOM   1410 C CD  . LYS B 1 8   ? 5.083  3.583   -0.909  1.00 16.99 ? 8   LYS X CD  1 
ATOM   1411 C CE  . LYS B 1 8   ? 5.387  2.495   -1.909  1.00 18.65 ? 8   LYS X CE  1 
ATOM   1412 N NZ  . LYS B 1 8   ? 4.775  1.213   -1.497  1.00 21.61 ? 8   LYS X NZ  1 
ATOM   1413 N N   . VAL B 1 9   ? 3.724  6.975   2.355   1.00 15.01 ? 9   VAL X N   1 
ATOM   1414 C CA  . VAL B 1 9   ? 3.656  7.786   3.588   1.00 19.22 ? 9   VAL X CA  1 
ATOM   1415 C C   . VAL B 1 9   ? 4.556  7.118   4.623   1.00 17.58 ? 9   VAL X C   1 
ATOM   1416 O O   . VAL B 1 9   ? 4.419  5.939   4.840   1.00 19.40 ? 9   VAL X O   1 
ATOM   1417 C CB  . VAL B 1 9   ? 2.207  7.933   4.096   1.00 13.29 ? 9   VAL X CB  1 
ATOM   1418 C CG1 . VAL B 1 9   ? 2.098  9.027   5.141   1.00 23.69 ? 9   VAL X CG1 1 
ATOM   1419 C CG2 . VAL B 1 9   ? 1.230  8.193   2.961   1.00 21.82 ? 9   VAL X CG2 1 
ATOM   1420 N N   . VAL B 1 10  ? 5.463  7.897   5.189   1.00 16.69 ? 10  VAL X N   1 
ATOM   1421 C CA  . VAL B 1 10  ? 6.356  7.399   6.267   1.00 16.63 ? 10  VAL X CA  1 
ATOM   1422 C C   . VAL B 1 10  ? 6.000  8.112   7.569   1.00 15.39 ? 10  VAL X C   1 
ATOM   1423 O O   . VAL B 1 10  ? 5.795  9.303   7.533   1.00 16.98 ? 10  VAL X O   1 
ATOM   1424 C CB  . VAL B 1 10  ? 7.813  7.693   5.895   1.00 14.56 ? 10  VAL X CB  1 
ATOM   1425 C CG1 . VAL B 1 10  ? 8.792  7.216   6.956   1.00 14.57 ? 10  VAL X CG1 1 
ATOM   1426 C CG2 . VAL B 1 10  ? 8.166  7.109   4.538   1.00 17.72 ? 10  VAL X CG2 1 
ATOM   1427 N N   . ALA B 1 11  ? 5.985  7.362   8.665   1.00 30.00 ? 11  ALA X N   1 
ATOM   1428 C CA  . ALA B 1 11  ? 5.773  7.964   9.997   1.00 30.00 ? 11  ALA X CA  1 
ATOM   1429 C C   . ALA B 1 11  ? 7.107  8.109   10.736  1.00 30.00 ? 11  ALA X C   1 
ATOM   1430 O O   . ALA B 1 11  ? 7.772  7.108   10.917  1.00 30.00 ? 11  ALA X O   1 
ATOM   1431 C CB  . ALA B 1 11  ? 4.801  7.136   10.780  1.00 30.00 ? 11  ALA X CB  1 
ATOM   1432 N N   . ALA B 1 12  ? 7.450  9.340   11.114  1.00 30.00 ? 12  ALA X N   1 
ATOM   1433 C CA  . ALA B 1 12  ? 8.653  9.561   11.937  1.00 30.00 ? 12  ALA X CA  1 
ATOM   1434 C C   . ALA B 1 12  ? 8.234  9.599   13.400  1.00 30.00 ? 12  ALA X C   1 
ATOM   1435 O O   . ALA B 1 12  ? 7.382  10.364  13.742  1.00 30.00 ? 12  ALA X O   1 
ATOM   1436 C CB  . ALA B 1 12  ? 9.375  10.812  11.559  1.00 30.00 ? 12  ALA X CB  1 
ATOM   1437 N N   . LEU B 1 13  ? 8.859  8.746   14.196  1.00 21.58 ? 13  LEU X N   1 
ATOM   1438 C CA  . LEU B 1 13  ? 8.487  8.635   15.604  1.00 11.69 ? 13  LEU X CA  1 
ATOM   1439 C C   . LEU B 1 13  ? 9.528  9.365   16.432  1.00 17.51 ? 13  LEU X C   1 
ATOM   1440 O O   . LEU B 1 13  ? 10.692 8.954   16.463  1.00 16.17 ? 13  LEU X O   1 
ATOM   1441 C CB  . LEU B 1 13  ? 8.419  7.162   15.997  1.00 20.19 ? 13  LEU X CB  1 
ATOM   1442 C CG  . LEU B 1 13  ? 7.086  6.420   15.851  1.00 31.50 ? 13  LEU X CG  1 
ATOM   1443 C CD1 . LEU B 1 13  ? 6.348  6.754   14.571  1.00 26.89 ? 13  LEU X CD1 1 
ATOM   1444 C CD2 . LEU B 1 13  ? 7.321  4.923   15.929  1.00 21.35 ? 13  LEU X CD2 1 
ATOM   1445 N N   . VAL B 1 14  ? 9.119  10.448  17.099  1.00 19.33 ? 14  VAL X N   1 
ATOM   1446 C CA  . VAL B 1 14  ? 10.055 11.283  17.836  1.00 18.81 ? 14  VAL X CA  1 
ATOM   1447 C C   . VAL B 1 14  ? 9.401  11.800  19.106  1.00 21.19 ? 14  VAL X C   1 
ATOM   1448 O O   . VAL B 1 14  ? 8.187  12.017  19.164  1.00 17.96 ? 14  VAL X O   1 
ATOM   1449 C CB  . VAL B 1 14  ? 10.628 12.468  17.014  1.00 25.29 ? 14  VAL X CB  1 
ATOM   1450 C CG1 . VAL B 1 14  ? 11.653 11.983  16.002  1.00 21.08 ? 14  VAL X CG1 1 
ATOM   1451 C CG2 . VAL B 1 14  ? 9.528  13.268  16.338  1.00 21.55 ? 14  VAL X CG2 1 
ATOM   1452 N N   . THR B 1 15  ? 10.229 11.972  20.127  1.00 19.61 ? 15  THR X N   1 
ATOM   1453 C CA  . THR B 1 15  ? 9.931  12.746  21.323  1.00 17.83 ? 15  THR X CA  1 
ATOM   1454 C C   . THR B 1 15  ? 10.979 13.846  21.448  1.00 18.04 ? 15  THR X C   1 
ATOM   1455 O O   . THR B 1 15  ? 11.978 13.865  20.717  1.00 18.19 ? 15  THR X O   1 
ATOM   1456 C CB  . THR B 1 15  ? 9.917  11.862  22.582  1.00 17.93 ? 15  THR X CB  1 
ATOM   1457 O OG1 . THR B 1 15  ? 11.228 11.312  22.814  1.00 21.01 ? 15  THR X OG1 1 
ATOM   1458 C CG2 . THR B 1 15  ? 8.883  10.737  22.458  1.00 14.06 ? 15  THR X CG2 1 
ATOM   1459 N N   . ASP B 1 16  ? 10.734 14.790  22.365  1.00 18.72 ? 16  ASP X N   1 
ATOM   1460 C CA  . ASP B 1 16  ? 11.664 15.898  22.542  1.00 18.74 ? 16  ASP X CA  1 
ATOM   1461 C C   . ASP B 1 16  ? 13.073 15.367  22.743  1.00 17.88 ? 16  ASP X C   1 
ATOM   1462 O O   . ASP B 1 16  ? 13.274 14.337  23.388  1.00 17.36 ? 16  ASP X O   1 
ATOM   1463 C CB  . ASP B 1 16  ? 11.293 16.788  23.735  1.00 18.63 ? 16  ASP X CB  1 
ATOM   1464 C CG  . ASP B 1 16  ? 9.993  17.544  23.540  1.00 26.11 ? 16  ASP X CG  1 
ATOM   1465 O OD1 . ASP B 1 16  ? 9.614  17.832  22.379  1.00 27.34 ? 16  ASP X OD1 1 
ATOM   1466 O OD2 . ASP B 1 16  ? 9.374  17.887  24.564  1.00 25.89 ? 16  ASP X OD2 1 
ATOM   1467 N N   . GLY B 1 17  ? 14.040 16.070  22.164  1.00 17.97 ? 17  GLY X N   1 
ATOM   1468 C CA  . GLY B 1 17  ? 15.425 15.642  22.200  1.00 18.47 ? 17  GLY X CA  1 
ATOM   1469 C C   . GLY B 1 17  ? 15.862 14.768  21.050  1.00 17.98 ? 17  GLY X C   1 
ATOM   1470 O O   . GLY B 1 17  ? 16.890 14.088  21.157  1.00 19.72 ? 17  GLY X O   1 
ATOM   1471 N N   . PHE B 1 18  ? 15.116 14.752  19.949  1.00 17.98 ? 18  PHE X N   1 
ATOM   1472 C CA  . PHE B 1 18  ? 15.543 13.984  18.788  1.00 18.14 ? 18  PHE X CA  1 
ATOM   1473 C C   . PHE B 1 18  ? 16.600 14.743  17.994  1.00 17.10 ? 18  PHE X C   1 
ATOM   1474 O O   . PHE B 1 18  ? 16.612 15.975  17.949  1.00 24.53 ? 18  PHE X O   1 
ATOM   1475 C CB  . PHE B 1 18  ? 14.348 13.611  17.907  1.00 17.93 ? 18  PHE X CB  1 
ATOM   1476 C CG  . PHE B 1 18  ? 13.728 14.766  17.179  1.00 19.77 ? 18  PHE X CG  1 
ATOM   1477 C CD1 . PHE B 1 18  ? 14.175 15.137  15.910  1.00 20.73 ? 18  PHE X CD1 1 
ATOM   1478 C CD2 . PHE B 1 18  ? 12.660 15.448  17.736  1.00 19.91 ? 18  PHE X CD2 1 
ATOM   1479 C CE1 . PHE B 1 18  ? 13.590 16.188  15.239  1.00 18.03 ? 18  PHE X CE1 1 
ATOM   1480 C CE2 . PHE B 1 18  ? 12.065 16.498  17.059  1.00 23.88 ? 18  PHE X CE2 1 
ATOM   1481 C CZ  . PHE B 1 18  ? 12.521 16.865  15.810  1.00 18.97 ? 18  PHE X CZ  1 
ATOM   1482 N N   . GLU B 1 19  ? 17.493 13.987  17.363  1.00 18.98 ? 19  GLU X N   1 
ATOM   1483 C CA  . GLU B 1 19  ? 18.565 14.614  16.555  1.00 23.37 ? 19  GLU X CA  1 
ATOM   1484 C C   . GLU B 1 19  ? 17.884 15.220  15.347  1.00 18.13 ? 19  GLU X C   1 
ATOM   1485 O O   . GLU B 1 19  ? 17.371 14.457  14.531  1.00 20.61 ? 19  GLU X O   1 
ATOM   1486 C CB  . GLU B 1 19  ? 19.657 13.629  16.167  1.00 20.41 ? 19  GLU X CB  1 
ATOM   1487 C CG  . GLU B 1 19  ? 20.838 14.304  15.510  1.00 17.45 ? 19  GLU X CG  1 
ATOM   1488 C CD  . GLU B 1 19  ? 21.652 15.125  16.487  1.00 20.27 ? 19  GLU X CD  1 
ATOM   1489 O OE1 . GLU B 1 19  ? 22.000 14.584  17.541  1.00 24.87 ? 19  GLU X OE1 1 
ATOM   1490 O OE2 . GLU B 1 19  ? 21.932 16.287  16.190  1.00 22.27 ? 19  GLU X OE2 1 
ATOM   1491 N N   . GLN B 1 20  ? 17.961 16.529  15.224  1.00 16.11 ? 20  GLN X N   1 
ATOM   1492 C CA  . GLN B 1 20  ? 17.137 17.212  14.235  1.00 17.31 ? 20  GLN X CA  1 
ATOM   1493 C C   . GLN B 1 20  ? 17.441 16.741  12.824  1.00 20.72 ? 20  GLN X C   1 
ATOM   1494 O O   . GLN B 1 20  ? 16.525 16.427  12.057  1.00 21.20 ? 20  GLN X O   1 
ATOM   1495 C CB  . GLN B 1 20  ? 17.299 18.723  14.342  1.00 18.52 ? 20  GLN X CB  1 
ATOM   1496 C CG  . GLN B 1 20  ? 16.381 19.433  13.360  1.00 23.09 ? 20  GLN X CG  1 
ATOM   1497 C CD  . GLN B 1 20  ? 16.168 20.880  13.706  1.00 22.94 ? 20  GLN X CD  1 
ATOM   1498 O OE1 . GLN B 1 20  ? 15.803 21.205  14.832  1.00 22.58 ? 20  GLN X OE1 1 
ATOM   1499 N NE2 . GLN B 1 20  ? 16.357 21.758  12.730  1.00 26.72 ? 20  GLN X NE2 1 
ATOM   1500 N N   . VAL B 1 21  ? 18.712 16.658  12.462  1.00 16.57 ? 21  VAL X N   1 
ATOM   1501 C CA  . VAL B 1 21  ? 19.085 16.283  11.067  1.00 21.14 ? 21  VAL X CA  1 
ATOM   1502 C C   . VAL B 1 21  ? 18.678 14.840  10.787  1.00 20.04 ? 21  VAL X C   1 
ATOM   1503 O O   . VAL B 1 21  ? 18.485 14.508  9.629   1.00 19.61 ? 21  VAL X O   1 
ATOM   1504 C CB  . VAL B 1 21  ? 20.576 16.553  10.793  1.00 18.51 ? 21  VAL X CB  1 
ATOM   1505 C CG1 . VAL B 1 21  ? 21.510 15.581  11.499  1.00 14.90 ? 21  VAL X CG1 1 
ATOM   1506 C CG2 . VAL B 1 21  ? 20.905 16.668  9.316   1.00 22.11 ? 21  VAL X CG2 1 
ATOM   1507 N N   . GLU B 1 22  ? 18.570 14.026  11.832  1.00 16.26 ? 22  GLU X N   1 
ATOM   1508 C CA  . GLU B 1 22  ? 18.180 12.591  11.674  1.00 16.02 ? 22  GLU X CA  1 
ATOM   1509 C C   . GLU B 1 22  ? 16.704 12.511  11.295  1.00 19.36 ? 22  GLU X C   1 
ATOM   1510 O O   . GLU B 1 22  ? 16.277 11.436  10.862  1.00 17.43 ? 22  GLU X O   1 
ATOM   1511 C CB  . GLU B 1 22  ? 18.648 11.735  12.850  1.00 19.57 ? 22  GLU X CB  1 
ATOM   1512 C CG  . GLU B 1 22  ? 20.144 11.531  12.818  1.00 15.59 ? 22  GLU X CG  1 
ATOM   1513 C CD  . GLU B 1 22  ? 20.660 10.877  14.076  1.00 21.07 ? 22  GLU X CD  1 
ATOM   1514 O OE1 . GLU B 1 22  ? 19.852 10.291  14.775  1.00 16.66 ? 22  GLU X OE1 1 
ATOM   1515 O OE2 . GLU B 1 22  ? 21.853 10.971  14.342  1.00 21.46 ? 22  GLU X OE2 1 
ATOM   1516 N N   . LEU B 1 23  ? 15.967 13.609  11.469  1.00 15.08 ? 23  LEU X N   1 
ATOM   1517 C CA  . LEU B 1 23  ? 14.593 13.699  10.932  1.00 18.29 ? 23  LEU X CA  1 
ATOM   1518 C C   . LEU B 1 23  ? 14.600 14.512  9.636   1.00 19.02 ? 23  LEU X C   1 
ATOM   1519 O O   . LEU B 1 23  ? 14.086 14.001  8.657   1.00 22.32 ? 23  LEU X O   1 
ATOM   1520 C CB  . LEU B 1 23  ? 13.704 14.411  11.952  1.00 14.70 ? 23  LEU X CB  1 
ATOM   1521 C CG  . LEU B 1 23  ? 12.345 14.853  11.415  1.00 17.31 ? 23  LEU X CG  1 
ATOM   1522 C CD1 . LEU B 1 23  ? 11.390 13.681  11.335  1.00 21.92 ? 23  LEU X CD1 1 
ATOM   1523 C CD2 . LEU B 1 23  ? 11.754 15.972  12.249  1.00 21.56 ? 23  LEU X CD2 1 
ATOM   1524 N N   . THR B 1 24  ? 15.240 15.685  9.609   1.00 19.86 ? 24  THR X N   1 
ATOM   1525 C CA  . THR B 1 24  ? 15.060 16.574  8.458   1.00 16.93 ? 24  THR X CA  1 
ATOM   1526 C C   . THR B 1 24  ? 15.807 16.088  7.219   1.00 19.95 ? 24  THR X C   1 
ATOM   1527 O O   . THR B 1 24  ? 15.340 16.299  6.092   1.00 19.54 ? 24  THR X O   1 
ATOM   1528 C CB  . THR B 1 24  ? 15.497 17.998  8.799   1.00 21.01 ? 24  THR X CB  1 
ATOM   1529 O OG1 . THR B 1 24  ? 16.910 18.019  9.064   1.00 26.24 ? 24  THR X OG1 1 
ATOM   1530 C CG2 . THR B 1 24  ? 14.728 18.521  9.997   1.00 20.27 ? 24  THR X CG2 1 
ATOM   1531 N N   . GLY B 1 25  ? 16.958 15.452  7.386   1.00 20.10 ? 25  GLY X N   1 
ATOM   1532 C CA  . GLY B 1 25  ? 17.654 14.907  6.246   1.00 17.85 ? 25  GLY X CA  1 
ATOM   1533 C C   . GLY B 1 25  ? 16.843 13.841  5.543   1.00 19.00 ? 25  GLY X C   1 
ATOM   1534 O O   . GLY B 1 25  ? 16.529 13.953  4.346   1.00 19.18 ? 25  GLY X O   1 
ATOM   1535 N N   . PRO B 1 26  ? 16.496 12.770  6.260   1.00 17.20 ? 26  PRO X N   1 
ATOM   1536 C CA  . PRO B 1 26  ? 15.642 11.742  5.638   1.00 18.86 ? 26  PRO X CA  1 
ATOM   1537 C C   . PRO B 1 26  ? 14.300 12.270  5.177   1.00 19.98 ? 26  PRO X C   1 
ATOM   1538 O O   . PRO B 1 26  ? 13.789 11.836  4.137   1.00 19.47 ? 26  PRO X O   1 
ATOM   1539 C CB  . PRO B 1 26  ? 15.490 10.690  6.740   1.00 15.75 ? 26  PRO X CB  1 
ATOM   1540 C CG  . PRO B 1 26  ? 16.740 10.838  7.545   1.00 16.97 ? 26  PRO X CG  1 
ATOM   1541 C CD  . PRO B 1 26  ? 17.057 12.315  7.541   1.00 19.22 ? 26  PRO X CD  1 
ATOM   1542 N N   . LYS B 1 27  ? 13.717 13.203  5.925   1.00 16.58 ? 27  LYS X N   1 
ATOM   1543 C CA  . LYS B 1 27  ? 12.429 13.767  5.533   1.00 18.40 ? 27  LYS X CA  1 
ATOM   1544 C C   . LYS B 1 27  ? 12.523 14.464  4.188   1.00 19.31 ? 27  LYS X C   1 
ATOM   1545 O O   . LYS B 1 27  ? 11.657 14.272  3.326   1.00 20.09 ? 27  LYS X O   1 
ATOM   1546 C CB  . LYS B 1 27  ? 11.922 14.745  6.590   1.00 17.01 ? 27  LYS X CB  1 
ATOM   1547 C CG  . LYS B 1 27  ? 10.506 15.243  6.326   1.00 22.40 ? 27  LYS X CG  1 
ATOM   1548 C CD  . LYS B 1 27  ? 9.840  15.761  7.600   1.00 26.60 ? 27  LYS X CD  1 
ATOM   1549 C CE  . LYS B 1 27  ? 8.397  16.208  7.330   1.00 28.74 ? 27  LYS X CE  1 
ATOM   1550 N NZ  . LYS B 1 27  ? 8.294  17.484  6.550   1.00 22.80 ? 27  LYS X NZ  1 
ATOM   1551 N N   . LYS B 1 28  ? 13.568 15.275  3.986   1.00 19.07 ? 28  LYS X N   1 
ATOM   1552 C CA  . LYS B 1 28  ? 13.709 15.983  2.718   1.00 21.43 ? 28  LYS X CA  1 
ATOM   1553 C C   . LYS B 1 28  ? 13.993 15.025  1.566   1.00 25.04 ? 28  LYS X C   1 
ATOM   1554 O O   . LYS B 1 28  ? 13.432 15.177  0.473   1.00 21.07 ? 28  LYS X O   1 
ATOM   1555 C CB  . LYS B 1 28  ? 14.803 17.045  2.808   1.00 21.94 ? 28  LYS X CB  1 
ATOM   1556 C CG  . LYS B 1 28  ? 15.055 17.743  1.470   1.00 21.47 ? 28  LYS X CG  1 
ATOM   1557 C CD  . LYS B 1 28  ? 16.300 18.604  1.497   1.00 30.55 ? 28  LYS X CD  1 
ATOM   1558 C CE  . LYS B 1 28  ? 16.519 19.306  0.160   1.00 36.16 ? 28  LYS X CE  1 
ATOM   1559 N NZ  . LYS B 1 28  ? 17.487 18.555  -0.691  1.00 40.31 ? 28  LYS X NZ  1 
ATOM   1560 N N   . ALA B 1 29  ? 14.873 14.044  1.776   1.00 30.00 ? 29  ALA X N   1 
ATOM   1561 C CA  . ALA B 1 29  ? 15.142 13.073  0.717   1.00 30.00 ? 29  ALA X CA  1 
ATOM   1562 C C   . ALA B 1 29  ? 13.878 12.317  0.329   1.00 30.00 ? 29  ALA X C   1 
ATOM   1563 O O   . ALA B 1 29  ? 13.615 12.094  -0.857  1.00 30.00 ? 29  ALA X O   1 
ATOM   1564 C CB  . ALA B 1 29  ? 16.229 12.097  1.159   1.00 30.00 ? 29  ALA X CB  1 
ATOM   1565 N N   . LEU B 1 30  ? 13.084 11.920  1.324   1.00 17.49 ? 30  LEU X N   1 
ATOM   1566 C CA  . LEU B 1 30  ? 11.846 11.188  1.075   1.00 18.35 ? 30  LEU X CA  1 
ATOM   1567 C C   . LEU B 1 30  ? 10.816 12.066  0.377   1.00 18.19 ? 30  LEU X C   1 
ATOM   1568 O O   . LEU B 1 30  ? 10.169 11.632  -0.589  1.00 20.15 ? 30  LEU X O   1 
ATOM   1569 C CB  . LEU B 1 30  ? 11.281 10.679  2.406   1.00 15.65 ? 30  LEU X CB  1 
ATOM   1570 C CG  . LEU B 1 30  ? 12.022 9.493   3.031   1.00 19.42 ? 30  LEU X CG  1 
ATOM   1571 C CD1 . LEU B 1 30  ? 11.627 9.303   4.502   1.00 13.99 ? 30  LEU X CD1 1 
ATOM   1572 C CD2 . LEU B 1 30  ? 11.807 8.208   2.226   1.00 20.25 ? 30  LEU X CD2 1 
ATOM   1573 N N   . GLU B 1 31  ? 10.669 13.313  0.830   1.00 19.30 ? 31  GLU X N   1 
ATOM   1574 C CA  . GLU B 1 31  ? 9.762  14.243  0.164   1.00 19.63 ? 31  GLU X CA  1 
ATOM   1575 C C   . GLU B 1 31  ? 10.225 14.558  -1.251  1.00 18.18 ? 31  GLU X C   1 
ATOM   1576 O O   . GLU B 1 31  ? 9.394  14.667  -2.167  1.00 22.09 ? 31  GLU X O   1 
ATOM   1577 C CB  . GLU B 1 31  ? 9.643  15.523  0.981   1.00 26.11 ? 31  GLU X CB  1 
ATOM   1578 C CG  . GLU B 1 31  ? 8.883  15.329  2.260   1.00 24.06 ? 31  GLU X CG  1 
ATOM   1579 C CD  . GLU B 1 31  ? 8.924  16.552  3.135   1.00 28.00 ? 31  GLU X CD  1 
ATOM   1580 O OE1 . GLU B 1 31  ? 9.815  17.403  2.928   1.00 28.22 ? 31  GLU X OE1 1 
ATOM   1581 O OE2 . GLU B 1 31  ? 8.073  16.653  4.034   1.00 30.67 ? 31  GLU X OE2 1 
ATOM   1582 N N   . ASP B 1 32  ? 11.540 14.724  -1.454  1.00 16.07 ? 32  ASP X N   1 
ATOM   1583 C CA  . ASP B 1 32  ? 12.039 14.963  -2.813  1.00 22.95 ? 32  ASP X CA  1 
ATOM   1584 C C   . ASP B 1 32  ? 11.650 13.842  -3.767  1.00 23.44 ? 32  ASP X C   1 
ATOM   1585 O O   . ASP B 1 32  ? 11.418 14.089  -4.953  1.00 24.15 ? 32  ASP X O   1 
ATOM   1586 C CB  . ASP B 1 32  ? 13.559 15.168  -2.859  1.00 25.18 ? 32  ASP X CB  1 
ATOM   1587 C CG  . ASP B 1 32  ? 13.998 16.457  -2.223  1.00 25.25 ? 32  ASP X CG  1 
ATOM   1588 O OD1 . ASP B 1 32  ? 13.130 17.322  -1.984  1.00 26.60 ? 32  ASP X OD1 1 
ATOM   1589 O OD2 . ASP B 1 32  ? 15.219 16.619  -1.992  1.00 25.24 ? 32  ASP X OD2 1 
ATOM   1590 N N   . ALA B 1 33  ? 11.619 12.604  -3.284  1.00 30.00 ? 33  ALA X N   1 
ATOM   1591 C CA  . ALA B 1 33  ? 11.278 11.474  -4.133  1.00 30.00 ? 33  ALA X CA  1 
ATOM   1592 C C   . ALA B 1 33  ? 9.780  11.315  -4.315  1.00 30.00 ? 33  ALA X C   1 
ATOM   1593 O O   . ALA B 1 33  ? 9.347  10.383  -4.999  1.00 30.00 ? 33  ALA X O   1 
ATOM   1594 C CB  . ALA B 1 33  ? 11.875 10.183  -3.575  1.00 30.00 ? 33  ALA X CB  1 
ATOM   1595 N N   . GLY B 1 34  ? 8.989  12.184  -3.700  1.00 20.45 ? 34  GLY X N   1 
ATOM   1596 C CA  . GLY B 1 34  ? 7.553  12.177  -3.868  1.00 21.26 ? 34  GLY X CA  1 
ATOM   1597 C C   . GLY B 1 34  ? 6.744  11.622  -2.715  1.00 25.19 ? 34  GLY X C   1 
ATOM   1598 O O   . GLY B 1 34  ? 5.518  11.532  -2.837  1.00 19.24 ? 34  GLY X O   1 
ATOM   1599 N N   . ALA B 1 35  ? 7.371  11.254  -1.604  1.00 30.00 ? 35  ALA X N   1 
ATOM   1600 C CA  . ALA B 1 35  ? 6.627  10.676  -0.498  1.00 30.00 ? 35  ALA X CA  1 
ATOM   1601 C C   . ALA B 1 35  ? 6.063  11.770  0.403   1.00 30.00 ? 35  ALA X C   1 
ATOM   1602 O O   . ALA B 1 35  ? 6.404  12.948  0.294   1.00 30.00 ? 35  ALA X O   1 
ATOM   1603 C CB  . ALA B 1 35  ? 7.504  9.709   0.298   1.00 30.00 ? 35  ALA X CB  1 
ATOM   1604 N N   . THR B 1 36  ? 5.156  11.364  1.283   1.00 20.89 ? 36  THR X N   1 
ATOM   1605 C CA  . THR B 1 36  ? 4.703  12.204  2.380   1.00 21.00 ? 36  THR X CA  1 
ATOM   1606 C C   . THR B 1 36  ? 5.347  11.674  3.651   1.00 18.54 ? 36  THR X C   1 
ATOM   1607 O O   . THR B 1 36  ? 5.524  10.463  3.803   1.00 17.26 ? 36  THR X O   1 
ATOM   1608 C CB  . THR B 1 36  ? 3.175  12.140  2.503   1.00 18.33 ? 36  THR X CB  1 
ATOM   1609 O OG1 . THR B 1 36  ? 2.577  12.724  1.335   1.00 27.98 ? 36  THR X OG1 1 
ATOM   1610 C CG2 . THR B 1 36  ? 2.682  12.899  3.735   1.00 22.79 ? 36  THR X CG2 1 
ATOM   1611 N N   . VAL B 1 37  ? 5.736  12.582  4.541   1.00 25.75 ? 37  VAL X N   1 
ATOM   1612 C CA  . VAL B 1 37  ? 6.259  12.233  5.857   1.00 15.33 ? 37  VAL X CA  1 
ATOM   1613 C C   . VAL B 1 37  ? 5.428  12.965  6.889   1.00 18.37 ? 37  VAL X C   1 
ATOM   1614 O O   . VAL B 1 37  ? 5.280  14.190  6.806   1.00 19.85 ? 37  VAL X O   1 
ATOM   1615 C CB  . VAL B 1 37  ? 7.739  12.646  5.991   1.00 16.33 ? 37  VAL X CB  1 
ATOM   1616 C CG1 . VAL B 1 37  ? 8.296  12.255  7.377   1.00 20.04 ? 37  VAL X CG1 1 
ATOM   1617 C CG2 . VAL B 1 37  ? 8.562  12.028  4.881   1.00 19.10 ? 37  VAL X CG2 1 
ATOM   1618 N N   . ARG B 1 38  ? 4.881  12.218  7.852   1.00 20.74 ? 38  ARG X N   1 
ATOM   1619 C CA  . ARG B 1 38  ? 4.195  12.780  9.006   1.00 19.74 ? 38  ARG X CA  1 
ATOM   1620 C C   . ARG B 1 38  ? 5.048  12.571  10.244  1.00 18.75 ? 38  ARG X C   1 
ATOM   1621 O O   . ARG B 1 38  ? 5.795  11.591  10.342  1.00 19.54 ? 38  ARG X O   1 
ATOM   1622 C CB  . ARG B 1 38  ? 2.854  12.083  9.259   1.00 21.64 ? 38  ARG X CB  1 
ATOM   1623 C CG  . ARG B 1 38  ? 1.922  12.071  8.066   1.00 20.48 ? 38  ARG X CG  1 
ATOM   1624 C CD  . ARG B 1 38  ? 1.702  13.485  7.554   1.00 27.77 ? 38  ARG X CD  1 
ATOM   1625 N NE  . ARG B 1 38  ? 0.782  13.528  6.426   1.00 40.81 ? 38  ARG X NE  1 
ATOM   1626 C CZ  . ARG B 1 38  ? 0.435  14.637  5.790   1.00 35.63 ? 38  ARG X CZ  1 
ATOM   1627 N NH1 . ARG B 1 38  ? 0.960  15.808  6.111   1.00 34.74 ? 38  ARG X NH1 1 
ATOM   1628 N NH2 . ARG B 1 38  ? -0.460 14.569  4.806   1.00 32.13 ? 38  ARG X NH2 1 
ATOM   1629 N N   . ILE B 1 39  ? 4.901  13.481  11.206  1.00 21.02 ? 39  ILE X N   1 
ATOM   1630 C CA  . ILE B 1 39  ? 5.632  13.441  12.470  1.00 18.52 ? 39  ILE X CA  1 
ATOM   1631 C C   . ILE B 1 39  ? 4.670  13.013  13.563  1.00 17.87 ? 39  ILE X C   1 
ATOM   1632 O O   . ILE B 1 39  ? 3.693  13.718  13.854  1.00 20.21 ? 39  ILE X O   1 
ATOM   1633 C CB  . ILE B 1 39  ? 6.261  14.800  12.812  1.00 23.05 ? 39  ILE X CB  1 
ATOM   1634 C CG1 . ILE B 1 39  ? 7.371  15.144  11.822  1.00 21.03 ? 39  ILE X CG1 1 
ATOM   1635 C CG2 . ILE B 1 39  ? 6.803  14.800  14.248  1.00 20.48 ? 39  ILE X CG2 1 
ATOM   1636 C CD1 . ILE B 1 39  ? 7.895  16.563  11.951  1.00 25.49 ? 39  ILE X CD1 1 
ATOM   1637 N N   . LEU B 1 40  ? 4.951  11.873  14.182  1.00 19.11 ? 40  LEU X N   1 
ATOM   1638 C CA  . LEU B 1 40  ? 4.173  11.380  15.305  1.00 19.21 ? 40  LEU X CA  1 
ATOM   1639 C C   . LEU B 1 40  ? 4.996  11.526  16.576  1.00 17.09 ? 40  LEU X C   1 
ATOM   1640 O O   . LEU B 1 40  ? 6.211  11.285  16.575  1.00 20.12 ? 40  LEU X O   1 
ATOM   1641 C CB  . LEU B 1 40  ? 3.795  9.913   15.098  1.00 17.66 ? 40  LEU X CB  1 
ATOM   1642 C CG  . LEU B 1 40  ? 3.082  9.575   13.780  1.00 16.15 ? 40  LEU X CG  1 
ATOM   1643 C CD1 . LEU B 1 40  ? 2.651  8.124   13.773  1.00 23.24 ? 40  LEU X CD1 1 
ATOM   1644 C CD2 . LEU B 1 40  ? 1.877  10.484  13.524  1.00 21.32 ? 40  LEU X CD2 1 
ATOM   1645 N N   . SER B 1 41  ? 4.349  11.941  17.655  1.00 19.57 ? 41  SER X N   1 
ATOM   1646 C CA  . SER B 1 41  ? 5.048  12.115  18.925  1.00 16.86 ? 41  SER X CA  1 
ATOM   1647 C C   . SER B 1 41  ? 4.168  11.607  20.055  1.00 25.05 ? 41  SER X C   1 
ATOM   1648 O O   . SER B 1 41  ? 3.042  11.142  19.837  1.00 23.76 ? 41  SER X O   1 
ATOM   1649 C CB  . SER B 1 41  ? 5.513  13.564  19.107  1.00 19.87 ? 41  SER X CB  1 
ATOM   1650 O OG  . SER B 1 41  ? 6.476  13.660  20.140  1.00 24.25 ? 41  SER X OG  1 
ATOM   1651 N N   . ASP B 1 42  ? 4.690  11.670  21.281  1.00 22.72 ? 42  ASP X N   1 
ATOM   1652 C CA  . ASP B 1 42  ? 3.909  11.168  22.402  1.00 21.27 ? 42  ASP X CA  1 
ATOM   1653 C C   . ASP B 1 42  ? 2.774  12.126  22.751  1.00 25.93 ? 42  ASP X C   1 
ATOM   1654 O O   . ASP B 1 42  ? 1.666  11.687  23.081  1.00 25.45 ? 42  ASP X O   1 
ATOM   1655 C CB  . ASP B 1 42  ? 4.808  10.875  23.607  1.00 20.46 ? 42  ASP X CB  1 
ATOM   1656 C CG  . ASP B 1 42  ? 5.641  12.066  24.031  1.00 25.62 ? 42  ASP X CG  1 
ATOM   1657 O OD1 . ASP B 1 42  ? 6.173  12.793  23.169  1.00 28.36 ? 42  ASP X OD1 1 
ATOM   1658 O OD2 . ASP B 1 42  ? 5.780  12.257  25.260  1.00 24.21 ? 42  ASP X OD2 1 
ATOM   1659 N N   . LYS B 1 43  ? 3.020  13.432  22.632  1.00 24.19 ? 43  LYS X N   1 
ATOM   1660 C CA  . LYS B 1 43  ? 2.045  14.470  22.929  1.00 28.68 ? 43  LYS X CA  1 
ATOM   1661 C C   . LYS B 1 43  ? 1.774  15.309  21.686  1.00 25.44 ? 43  LYS X C   1 
ATOM   1662 O O   . LYS B 1 43  ? 2.616  15.421  20.787  1.00 24.62 ? 43  LYS X O   1 
ATOM   1663 C CB  . LYS B 1 43  ? 2.556  15.380  24.057  1.00 27.88 ? 43  LYS X CB  1 
ATOM   1664 N N   . ALA B 1 44  ? 0.587  15.907  21.646  1.00 30.00 ? 44  ALA X N   1 
ATOM   1665 C CA  . ALA B 1 44  ? 0.226  16.782  20.546  1.00 30.00 ? 44  ALA X CA  1 
ATOM   1666 C C   . ALA B 1 44  ? 0.856  18.157  20.727  1.00 30.00 ? 44  ALA X C   1 
ATOM   1667 O O   . ALA B 1 44  ? 1.283  18.543  21.822  1.00 30.00 ? 44  ALA X O   1 
ATOM   1668 C CB  . ALA B 1 44  ? -1.295 16.920  20.436  1.00 30.00 ? 44  ALA X CB  1 
ATOM   1669 N N   . GLY B 1 45  ? 0.892  18.905  19.632  1.00 26.81 ? 45  GLY X N   1 
ATOM   1670 C CA  . GLY B 1 45  ? 1.462  20.232  19.639  1.00 22.86 ? 45  GLY X CA  1 
ATOM   1671 C C   . GLY B 1 45  ? 2.723  20.297  18.810  1.00 20.91 ? 45  GLY X C   1 
ATOM   1672 O O   . GLY B 1 45  ? 2.678  20.161  17.581  1.00 30.87 ? 45  GLY X O   1 
ATOM   1673 N N   . GLU B 1 46  ? 3.852  20.507  19.472  1.00 28.06 ? 46  GLU X N   1 
ATOM   1674 C CA  . GLU B 1 46  ? 5.142  20.587  18.816  1.00 23.07 ? 46  GLU X CA  1 
ATOM   1675 C C   . GLU B 1 46  ? 6.122  19.680  19.543  1.00 22.23 ? 46  GLU X C   1 
ATOM   1676 O O   . GLU B 1 46  ? 5.989  19.427  20.746  1.00 26.89 ? 46  GLU X O   1 
ATOM   1677 C CB  . GLU B 1 46  ? 5.663  22.031  18.786  1.00 24.36 ? 46  GLU X CB  1 
ATOM   1678 C CG  . GLU B 1 46  ? 4.834  22.947  17.891  1.00 31.71 ? 46  GLU X CG  1 
ATOM   1679 C CD  . GLU B 1 46  ? 5.281  24.399  17.941  1.00 39.17 ? 46  GLU X CD  1 
ATOM   1680 O OE1 . GLU B 1 46  ? 5.874  24.815  18.960  1.00 39.29 ? 46  GLU X OE1 1 
ATOM   1681 O OE2 . GLU B 1 46  ? 5.029  25.128  16.957  1.00 49.66 ? 46  GLU X OE2 1 
ATOM   1682 N N   . VAL B 1 47  ? 7.098  19.172  18.798  1.00 20.87 ? 47  VAL X N   1 
ATOM   1683 C CA  . VAL B 1 47  ? 8.145  18.323  19.349  1.00 20.80 ? 47  VAL X CA  1 
ATOM   1684 C C   . VAL B 1 47  ? 9.490  18.964  19.024  1.00 21.60 ? 47  VAL X C   1 
ATOM   1685 O O   . VAL B 1 47  ? 9.679  19.504  17.930  1.00 23.13 ? 47  VAL X O   1 
ATOM   1686 C CB  . VAL B 1 47  ? 8.027  16.877  18.809  1.00 23.49 ? 47  VAL X CB  1 
ATOM   1687 C CG1 . VAL B 1 47  ? 8.221  16.843  17.295  1.00 19.57 ? 47  VAL X CG1 1 
ATOM   1688 C CG2 . VAL B 1 47  ? 9.030  15.942  19.502  1.00 21.38 ? 47  VAL X CG2 1 
ATOM   1689 N N   . ARG B 1 48  ? 10.412 18.951  19.987  1.00 22.01 ? 48  ARG X N   1 
ATOM   1690 C CA  . ARG B 1 48  ? 11.644 19.727  19.877  1.00 18.61 ? 48  ARG X CA  1 
ATOM   1691 C C   . ARG B 1 48  ? 12.813 18.881  19.385  1.00 23.24 ? 48  ARG X C   1 
ATOM   1692 O O   . ARG B 1 48  ? 13.236 17.943  20.064  1.00 23.76 ? 48  ARG X O   1 
ATOM   1693 C CB  . ARG B 1 48  ? 12.003 20.401  21.200  1.00 22.23 ? 48  ARG X CB  1 
ATOM   1694 C CG  . ARG B 1 48  ? 13.214 21.326  21.084  1.00 23.16 ? 48  ARG X CG  1 
ATOM   1695 C CD  . ARG B 1 48  ? 12.920 22.615  20.339  1.00 27.12 ? 48  ARG X CD  1 
ATOM   1696 N NE  . ARG B 1 48  ? 11.814 23.379  20.897  1.00 35.22 ? 48  ARG X NE  1 
ATOM   1697 C CZ  . ARG B 1 48  ? 11.500 24.613  20.524  1.00 39.61 ? 48  ARG X CZ  1 
ATOM   1698 N NH1 . ARG B 1 48  ? 12.232 25.275  19.641  1.00 31.16 ? 48  ARG X NH1 1 
ATOM   1699 N NH2 . ARG B 1 48  ? 10.423 25.196  21.045  1.00 45.81 ? 48  ARG X NH2 1 
ATOM   1700 N N   . GLY B 1 49  ? 13.355 19.239  18.227  1.00 21.65 ? 49  GLY X N   1 
ATOM   1701 C CA  . GLY B 1 49  ? 14.595 18.642  17.786  1.00 18.24 ? 49  GLY X CA  1 
ATOM   1702 C C   . GLY B 1 49  ? 15.811 19.339  18.363  1.00 24.32 ? 49  GLY X C   1 
ATOM   1703 O O   . GLY B 1 49  ? 15.723 20.450  18.882  1.00 26.00 ? 49  GLY X O   1 
ATOM   1704 N N   . TRP B 1 50  ? 16.956 18.659  18.262  1.00 23.39 ? 50  TRP X N   1 
ATOM   1705 C CA  . TRP B 1 50  ? 18.214 19.126  18.826  1.00 18.02 ? 50  TRP X CA  1 
ATOM   1706 C C   . TRP B 1 50  ? 19.315 18.957  17.794  1.00 25.66 ? 50  TRP X C   1 
ATOM   1707 O O   . TRP B 1 50  ? 19.281 18.032  16.977  1.00 20.38 ? 50  TRP X O   1 
ATOM   1708 C CB  . TRP B 1 50  ? 18.615 18.292  20.060  1.00 22.87 ? 50  TRP X CB  1 
ATOM   1709 C CG  . TRP B 1 50  ? 17.881 18.630  21.354  1.00 17.88 ? 50  TRP X CG  1 
ATOM   1710 C CD1 . TRP B 1 50  ? 16.528 18.786  21.515  1.00 23.35 ? 50  TRP X CD1 1 
ATOM   1711 C CD2 . TRP B 1 50  ? 18.458 18.807  22.657  1.00 21.76 ? 50  TRP X CD2 1 
ATOM   1712 N NE1 . TRP B 1 50  ? 16.234 19.064  22.823  1.00 22.10 ? 50  TRP X NE1 1 
ATOM   1713 C CE2 . TRP B 1 50  ? 17.396 19.080  23.549  1.00 16.80 ? 50  TRP X CE2 1 
ATOM   1714 C CE3 . TRP B 1 50  ? 19.766 18.770  23.159  1.00 17.75 ? 50  TRP X CE3 1 
ATOM   1715 C CZ2 . TRP B 1 50  ? 17.598 19.318  24.906  1.00 22.40 ? 50  TRP X CZ2 1 
ATOM   1716 C CZ3 . TRP B 1 50  ? 19.959 19.003  24.512  1.00 20.26 ? 50  TRP X CZ3 1 
ATOM   1717 C CH2 . TRP B 1 50  ? 18.874 19.277  25.368  1.00 18.03 ? 50  TRP X CH2 1 
ATOM   1718 N N   . ASN B 1 51  ? 20.306 19.838  17.884  1.00 19.35 ? 51  ASN X N   1 
ATOM   1719 C CA  . ASN B 1 51  ? 21.544 19.706  17.103  1.00 22.57 ? 51  ASN X CA  1 
ATOM   1720 C C   . ASN B 1 51  ? 22.613 19.309  18.130  1.00 23.60 ? 51  ASN X C   1 
ATOM   1721 O O   . ASN B 1 51  ? 23.087 20.180  18.839  1.00 22.58 ? 51  ASN X O   1 
ATOM   1722 C CB  . ASN B 1 51  ? 21.871 20.987  16.359  1.00 23.88 ? 51  ASN X CB  1 
ATOM   1723 C CG  . ASN B 1 51  ? 20.925 21.302  15.215  1.00 24.95 ? 51  ASN X CG  1 
ATOM   1724 O OD1 . ASN B 1 51  ? 20.436 20.413  14.527  1.00 20.70 ? 51  ASN X OD1 1 
ATOM   1725 N ND2 . ASN B 1 51  ? 20.666 22.580  14.995  1.00 26.57 ? 51  ASN X ND2 1 
ATOM   1726 N N   . HIS B 1 52  ? 22.915 18.019  18.207  1.00 19.35 ? 52  HIS X N   1 
ATOM   1727 C CA  . HIS B 1 52  ? 23.842 17.451  19.230  1.00 16.60 ? 52  HIS X CA  1 
ATOM   1728 C C   . HIS B 1 52  ? 23.324 17.719  20.647  1.00 19.22 ? 52  HIS X C   1 
ATOM   1729 O O   . HIS B 1 52  ? 22.302 17.171  21.008  1.00 25.32 ? 52  HIS X O   1 
ATOM   1730 C CB  . HIS B 1 52  ? 25.305 17.845  18.956  1.00 21.80 ? 52  HIS X CB  1 
ATOM   1731 C CG  . HIS B 1 52  ? 26.280 17.010  19.699  1.00 23.11 ? 52  HIS X CG  1 
ATOM   1732 N ND1 . HIS B 1 52  ? 26.224 15.640  19.689  1.00 24.90 ? 52  HIS X ND1 1 
ATOM   1733 C CD2 . HIS B 1 52  ? 27.318 17.348  20.483  1.00 20.01 ? 52  HIS X CD2 1 
ATOM   1734 C CE1 . HIS B 1 52  ? 27.199 15.163  20.423  1.00 22.76 ? 52  HIS X CE1 1 
ATOM   1735 N NE2 . HIS B 1 52  ? 27.875 16.188  20.916  1.00 24.34 ? 52  HIS X NE2 1 
ATOM   1736 N N   . HIS B 1 53  ? 24.013 18.563  21.397  1.00 22.46 ? 53  HIS X N   1 
ATOM   1737 C CA  . HIS B 1 53  ? 23.653 18.789  22.813  1.00 21.09 ? 53  HIS X CA  1 
ATOM   1738 C C   . HIS B 1 53  ? 22.971 20.146  23.018  1.00 19.11 ? 53  HIS X C   1 
ATOM   1739 O O   . HIS B 1 53  ? 22.913 20.593  24.157  1.00 29.66 ? 53  HIS X O   1 
ATOM   1740 C CB  . HIS B 1 53  ? 24.911 18.594  23.643  1.00 22.18 ? 53  HIS X CB  1 
ATOM   1741 C CG  . HIS B 1 53  ? 25.452 17.210  23.637  1.00 27.10 ? 53  HIS X CG  1 
ATOM   1742 N ND1 . HIS B 1 53  ? 26.714 16.924  24.100  1.00 27.01 ? 53  HIS X ND1 1 
ATOM   1743 C CD2 . HIS B 1 53  ? 24.916 16.040  23.238  1.00 25.18 ? 53  HIS X CD2 1 
ATOM   1744 C CE1 . HIS B 1 53  ? 26.936 15.634  23.984  1.00 28.22 ? 53  HIS X CE1 1 
ATOM   1745 N NE2 . HIS B 1 53  ? 25.853 15.073  23.454  1.00 24.28 ? 53  HIS X NE2 1 
ATOM   1746 N N   . GLN B 1 54  ? 22.474 20.781  21.952  1.00 25.26 ? 54  GLN X N   1 
ATOM   1747 C CA  . GLN B 1 54  ? 21.752 22.032  22.079  1.00 26.21 ? 54  GLN X CA  1 
ATOM   1748 C C   . GLN B 1 54  ? 20.352 21.890  21.498  1.00 28.84 ? 54  GLN X C   1 
ATOM   1749 O O   . GLN B 1 54  ? 20.184 21.288  20.428  1.00 22.83 ? 54  GLN X O   1 
ATOM   1750 C CB  . GLN B 1 54  ? 22.513 23.197  21.403  1.00 28.70 ? 54  GLN X CB  1 
ATOM   1751 C CG  . GLN B 1 54  ? 22.531 23.171  19.874  1.00 37.64 ? 54  GLN X CG  1 
ATOM   1752 C CD  . GLN B 1 54  ? 22.309 24.537  19.237  1.00 48.11 ? 54  GLN X CD  1 
ATOM   1753 O OE1 . GLN B 1 54  ? 23.078 25.473  19.463  1.00 64.08 ? 54  GLN X OE1 1 
ATOM   1754 N NE2 . GLN B 1 54  ? 21.257 24.649  18.417  1.00 45.23 ? 54  GLN X NE2 1 
ATOM   1755 N N   . PRO B 1 55  ? 19.325 22.369  22.197  1.00 21.52 ? 55  PRO X N   1 
ATOM   1756 C CA  . PRO B 1 55  ? 17.969 22.347  21.631  1.00 25.51 ? 55  PRO X CA  1 
ATOM   1757 C C   . PRO B 1 55  ? 17.920 23.141  20.335  1.00 25.07 ? 55  PRO X C   1 
ATOM   1758 O O   . PRO B 1 55  ? 18.562 24.184  20.194  1.00 25.96 ? 55  PRO X O   1 
ATOM   1759 C CB  . PRO B 1 55  ? 17.103 22.999  22.717  1.00 23.10 ? 55  PRO X CB  1 
ATOM   1760 C CG  . PRO B 1 55  ? 17.964 23.107  23.939  1.00 26.46 ? 55  PRO X CG  1 
ATOM   1761 C CD  . PRO B 1 55  ? 19.375 22.760  23.620  1.00 24.14 ? 55  PRO X CD  1 
ATOM   1762 N N   . ALA B 1 56  ? 17.167 22.621  19.369  1.00 30.00 ? 56  ALA X N   1 
ATOM   1763 C CA  . ALA B 1 56  ? 17.049 23.288  18.077  1.00 30.00 ? 56  ALA X CA  1 
ATOM   1764 C C   . ALA B 1 56  ? 15.597 23.661  17.811  1.00 30.00 ? 56  ALA X C   1 
ATOM   1765 O O   . ALA B 1 56  ? 14.925 24.185  18.697  1.00 30.00 ? 56  ALA X O   1 
ATOM   1766 C CB  . ALA B 1 56  ? 17.657 22.435  16.961  1.00 30.00 ? 56  ALA X CB  1 
ATOM   1767 N N   . GLU B 1 57  ? 15.097 23.401  16.610  1.00 29.22 ? 57  GLU X N   1 
ATOM   1768 C CA  . GLU B 1 57  ? 13.791 23.920  16.228  1.00 29.07 ? 57  GLU X CA  1 
ATOM   1769 C C   . GLU B 1 57  ? 12.664 23.008  16.699  1.00 22.64 ? 57  GLU X C   1 
ATOM   1770 O O   . GLU B 1 57  ? 12.857 21.820  16.976  1.00 26.67 ? 57  GLU X O   1 
ATOM   1771 C CB  . GLU B 1 57  ? 13.722 24.104  14.717  1.00 27.53 ? 57  GLU X CB  1 
ATOM   1772 C CG  . GLU B 1 57  ? 14.818 24.987  14.179  1.00 26.83 ? 57  GLU X CG  1 
ATOM   1773 C CD  . GLU B 1 57  ? 15.025 24.828  12.679  1.00 28.71 ? 57  GLU X CD  1 
ATOM   1774 O OE1 . GLU B 1 57  ? 14.071 25.057  11.918  1.00 30.10 ? 57  GLU X OE1 1 
ATOM   1775 O OE2 . GLU B 1 57  ? 16.142 24.450  12.277  1.00 36.00 ? 57  GLU X OE2 1 
ATOM   1776 N N   . ALA B 1 58  ? 11.473 23.594  16.811  1.00 30.00 ? 58  ALA X N   1 
ATOM   1777 C CA  . ALA B 1 58  ? 10.263 22.862  17.160  1.00 30.00 ? 58  ALA X CA  1 
ATOM   1778 C C   . ALA B 1 58  ? 9.493  22.519  15.893  1.00 30.00 ? 58  ALA X C   1 
ATOM   1779 O O   . ALA B 1 58  ? 9.383  23.342  14.982  1.00 30.00 ? 58  ALA X O   1 
ATOM   1780 C CB  . ALA B 1 58  ? 9.370  23.678  18.097  1.00 30.00 ? 58  ALA X CB  1 
ATOM   1781 N N   . PHE B 1 59  ? 8.951  21.305  15.854  1.00 23.28 ? 59  PHE X N   1 
ATOM   1782 C CA  . PHE B 1 59  ? 8.251  20.770  14.694  1.00 21.94 ? 59  PHE X CA  1 
ATOM   1783 C C   . PHE B 1 59  ? 6.810  20.449  15.053  1.00 27.54 ? 59  PHE X C   1 
ATOM   1784 O O   . PHE B 1 59  ? 6.526  19.948  16.143  1.00 23.85 ? 59  PHE X O   1 
ATOM   1785 C CB  . PHE B 1 59  ? 8.956  19.511  14.202  1.00 20.58 ? 59  PHE X CB  1 
ATOM   1786 C CG  . PHE B 1 59  ? 10.303 19.779  13.603  1.00 22.22 ? 59  PHE X CG  1 
ATOM   1787 C CD1 . PHE B 1 59  ? 11.412 19.977  14.407  1.00 21.86 ? 59  PHE X CD1 1 
ATOM   1788 C CD2 . PHE B 1 59  ? 10.462 19.821  12.220  1.00 20.57 ? 59  PHE X CD2 1 
ATOM   1789 C CE1 . PHE B 1 59  ? 12.657 20.230  13.854  1.00 22.73 ? 59  PHE X CE1 1 
ATOM   1790 C CE2 . PHE B 1 59  ? 11.701 20.076  11.657  1.00 23.73 ? 59  PHE X CE2 1 
ATOM   1791 C CZ  . PHE B 1 59  ? 12.802 20.274  12.467  1.00 19.81 ? 59  PHE X CZ  1 
ATOM   1792 N N   . ARG B 1 60  ? 5.895  20.743  14.132  1.00 23.97 ? 60  ARG X N   1 
ATOM   1793 C CA  . ARG B 1 60  ? 4.492  20.473  14.392  1.00 26.04 ? 60  ARG X CA  1 
ATOM   1794 C C   . ARG B 1 60  ? 4.237  18.969  14.407  1.00 25.58 ? 60  ARG X C   1 
ATOM   1795 O O   . ARG B 1 60  ? 4.656  18.241  13.498  1.00 28.20 ? 60  ARG X O   1 
ATOM   1796 C CB  . ARG B 1 60  ? 3.621  21.184  13.354  1.00 27.36 ? 60  ARG X CB  1 
ATOM   1797 C CG  . ARG B 1 60  ? 2.300  20.508  13.050  1.00 35.90 ? 60  ARG X CG  1 
ATOM   1798 C CD  . ARG B 1 60  ? 1.762  20.964  11.698  1.00 40.69 ? 60  ARG X CD  1 
ATOM   1799 N NE  . ARG B 1 60  ? 2.010  19.992  10.640  1.00 56.88 ? 60  ARG X NE  1 
ATOM   1800 C CZ  . ARG B 1 60  ? 1.827  20.227  9.347   1.00 61.38 ? 60  ARG X CZ  1 
ATOM   1801 N NH1 . ARG B 1 60  ? 1.404  21.402  8.908   1.00 56.45 ? 60  ARG X NH1 1 
ATOM   1802 N NH2 . ARG B 1 60  ? 2.073  19.256  8.471   1.00 63.45 ? 60  ARG X NH2 1 
ATOM   1803 N N   . VAL B 1 61  ? 3.558  18.510  15.455  1.00 26.22 ? 61  VAL X N   1 
ATOM   1804 C CA  . VAL B 1 61  ? 3.194  17.105  15.604  1.00 22.95 ? 61  VAL X CA  1 
ATOM   1805 C C   . VAL B 1 61  ? 1.924  16.833  14.811  1.00 25.97 ? 61  VAL X C   1 
ATOM   1806 O O   . VAL B 1 61  ? 0.868  17.406  15.094  1.00 26.16 ? 61  VAL X O   1 
ATOM   1807 C CB  . VAL B 1 61  ? 3.036  16.736  17.086  1.00 23.93 ? 61  VAL X CB  1 
ATOM   1808 C CG1 . VAL B 1 61  ? 2.448  15.345  17.245  1.00 22.80 ? 61  VAL X CG1 1 
ATOM   1809 C CG2 . VAL B 1 61  ? 4.389  16.817  17.782  1.00 23.85 ? 61  VAL X CG2 1 
ATOM   1810 N N   . ASP B 1 62  ? 2.028  15.961  13.806  1.00 26.41 ? 62  ASP X N   1 
ATOM   1811 C CA  . ASP B 1 62  ? 0.879  15.614  12.985  1.00 24.14 ? 62  ASP X CA  1 
ATOM   1812 C C   . ASP B 1 62  ? -0.070 14.649  13.687  1.00 28.38 ? 62  ASP X C   1 
ATOM   1813 O O   . ASP B 1 62  ? -1.261 14.633  13.366  1.00 27.97 ? 62  ASP X O   1 
ATOM   1814 C CB  . ASP B 1 62  ? 1.352  14.995  11.669  1.00 21.68 ? 62  ASP X CB  1 
ATOM   1815 C CG  . ASP B 1 62  ? 2.090  15.995  10.775  1.00 25.90 ? 62  ASP X CG  1 
ATOM   1816 O OD1 . ASP B 1 62  ? 1.535  17.073  10.469  1.00 27.78 ? 62  ASP X OD1 1 
ATOM   1817 O OD2 . ASP B 1 62  ? 3.228  15.688  10.366  1.00 28.73 ? 62  ASP X OD2 1 
ATOM   1818 N N   . GLY B 1 63  ? 0.421  13.852  14.633  1.00 20.06 ? 63  GLY X N   1 
ATOM   1819 C CA  . GLY B 1 63  ? -0.422 12.897  15.334  1.00 19.35 ? 63  GLY X CA  1 
ATOM   1820 C C   . GLY B 1 63  ? 0.327  12.302  16.507  1.00 23.68 ? 63  GLY X C   1 
ATOM   1821 O O   . GLY B 1 63  ? 1.546  12.431  16.621  1.00 18.52 ? 63  GLY X O   1 
ATOM   1822 N N   . THR B 1 64  ? -0.413 11.626  17.373  1.00 21.06 ? 64  THR X N   1 
ATOM   1823 C CA  . THR B 1 64  ? 0.188  10.980  18.532  1.00 21.31 ? 64  THR X CA  1 
ATOM   1824 C C   . THR B 1 64  ? 0.333  9.484   18.297  1.00 26.47 ? 64  THR X C   1 
ATOM   1825 O O   . THR B 1 64  ? -0.352 8.894   17.461  1.00 23.46 ? 64  THR X O   1 
ATOM   1826 C CB  . THR B 1 64  ? -0.648 11.206  19.793  1.00 22.75 ? 64  THR X CB  1 
ATOM   1827 O OG1 . THR B 1 64  ? -1.896 10.517  19.662  1.00 28.27 ? 64  THR X OG1 1 
ATOM   1828 C CG2 . THR B 1 64  ? -0.888 12.694  20.019  1.00 23.11 ? 64  THR X CG2 1 
ATOM   1829 N N   . PHE B 1 65  ? 1.254  8.871   19.049  1.00 23.85 ? 65  PHE X N   1 
ATOM   1830 C CA  . PHE B 1 65  ? 1.369  7.417   19.012  1.00 21.57 ? 65  PHE X CA  1 
ATOM   1831 C C   . PHE B 1 65  ? 0.048  6.774   19.410  1.00 25.46 ? 65  PHE X C   1 
ATOM   1832 O O   . PHE B 1 65  ? -0.407 5.822   18.763  1.00 22.85 ? 65  PHE X O   1 
ATOM   1833 C CB  . PHE B 1 65  ? 2.467  6.939   19.958  1.00 19.08 ? 65  PHE X CB  1 
ATOM   1834 C CG  . PHE B 1 65  ? 3.798  7.611   19.762  1.00 20.80 ? 65  PHE X CG  1 
ATOM   1835 C CD1 . PHE B 1 65  ? 4.274  7.949   18.500  1.00 21.48 ? 65  PHE X CD1 1 
ATOM   1836 C CD2 . PHE B 1 65  ? 4.604  7.861   20.862  1.00 18.90 ? 65  PHE X CD2 1 
ATOM   1837 C CE1 . PHE B 1 65  ? 5.516  8.557   18.357  1.00 17.31 ? 65  PHE X CE1 1 
ATOM   1838 C CE2 . PHE B 1 65  ? 5.846  8.463   20.717  1.00 17.55 ? 65  PHE X CE2 1 
ATOM   1839 C CZ  . PHE B 1 65  ? 6.307  8.807   19.473  1.00 21.46 ? 65  PHE X CZ  1 
ATOM   1840 N N   . GLU B 1 66  ? -0.578 7.296   20.478  1.00 19.78 ? 66  GLU X N   1 
ATOM   1841 C CA  . GLU B 1 66  ? -1.868 6.801   20.965  1.00 26.38 ? 66  GLU X CA  1 
ATOM   1842 C C   . GLU B 1 66  ? -2.912 6.700   19.855  1.00 25.30 ? 66  GLU X C   1 
ATOM   1843 O O   . GLU B 1 66  ? -3.663 5.718   19.786  1.00 29.36 ? 66  GLU X O   1 
ATOM   1844 C CB  . GLU B 1 66  ? -2.374 7.732   22.072  1.00 25.11 ? 66  GLU X CB  1 
ATOM   1845 C CG  . GLU B 1 66  ? -3.723 7.366   22.640  1.00 34.79 ? 66  GLU X CG  1 
ATOM   1846 C CD  . GLU B 1 66  ? -3.694 6.108   23.478  1.00 37.74 ? 66  GLU X CD  1 
ATOM   1847 O OE1 . GLU B 1 66  ? -4.549 5.222   23.241  1.00 38.71 ? 66  GLU X OE1 1 
ATOM   1848 O OE2 . GLU B 1 66  ? -2.834 6.015   24.385  1.00 43.52 ? 66  GLU X OE2 1 
ATOM   1849 N N   . ASP B 1 67  ? -2.980 7.710   18.984  1.00 24.71 ? 67  ASP X N   1 
ATOM   1850 C CA  . ASP B 1 67  ? -3.995 7.805   17.944  1.00 19.42 ? 67  ASP X CA  1 
ATOM   1851 C C   . ASP B 1 67  ? -3.582 7.164   16.625  1.00 31.30 ? 67  ASP X C   1 
ATOM   1852 O O   . ASP B 1 67  ? -4.427 7.021   15.733  1.00 27.74 ? 67  ASP X O   1 
ATOM   1853 C CB  . ASP B 1 67  ? -4.318 9.275   17.675  1.00 20.50 ? 67  ASP X CB  1 
ATOM   1854 C CG  . ASP B 1 67  ? -5.081 9.926   18.805  1.00 26.90 ? 67  ASP X CG  1 
ATOM   1855 O OD1 . ASP B 1 67  ? -5.533 9.211   19.728  1.00 33.43 ? 67  ASP X OD1 1 
ATOM   1856 O OD2 . ASP B 1 67  ? -5.213 11.164  18.773  1.00 34.36 ? 67  ASP X OD2 1 
ATOM   1857 N N   . ALA B 1 68  ? -2.317 6.789   16.463  1.00 30.00 ? 68  ALA X N   1 
ATOM   1858 C CA  . ALA B 1 68  ? -1.848 6.380   15.150  1.00 30.00 ? 68  ALA X CA  1 
ATOM   1859 C C   . ALA B 1 68  ? -2.294 4.965   14.810  1.00 30.00 ? 68  ALA X C   1 
ATOM   1860 O O   . ALA B 1 68  ? -2.405 4.093   15.675  1.00 30.00 ? 68  ALA X O   1 
ATOM   1861 C CB  . ALA B 1 68  ? -0.321 6.462   15.082  1.00 30.00 ? 68  ALA X CB  1 
ATOM   1862 N N   . SER B 1 69  ? -2.558 4.751   13.524  1.00 20.00 ? 69  SER X N   1 
ATOM   1863 C CA  . SER B 1 69  ? -2.774 3.429   12.956  1.00 25.20 ? 69  SER X CA  1 
ATOM   1864 C C   . SER B 1 69  ? -1.724 3.182   11.890  1.00 27.11 ? 69  SER X C   1 
ATOM   1865 O O   . SER B 1 69  ? -1.575 3.986   10.963  1.00 20.10 ? 69  SER X O   1 
ATOM   1866 C CB  . SER B 1 69  ? -4.141 3.311   12.283  1.00 28.12 ? 69  SER X CB  1 
ATOM   1867 O OG  . SER B 1 69  ? -4.252 2.048   11.643  1.00 24.06 ? 69  SER X OG  1 
ATOM   1868 N N   . LEU B 1 70  ? -1.020 2.062   12.006  1.00 19.81 ? 70  LEU X N   1 
ATOM   1869 C CA  . LEU B 1 70  ? -0.067 1.754   10.955  1.00 25.62 ? 70  LEU X CA  1 
ATOM   1870 C C   . LEU B 1 70  ? -0.715 1.372   9.627   1.00 23.20 ? 70  LEU X C   1 
ATOM   1871 O O   . LEU B 1 70  ? 0.024  1.181   8.662   1.00 23.25 ? 70  LEU X O   1 
ATOM   1872 C CB  . LEU B 1 70  ? 0.920  0.690   11.420  1.00 28.68 ? 70  LEU X CB  1 
ATOM   1873 C CG  . LEU B 1 70  ? 2.315  0.808   10.814  1.00 29.31 ? 70  LEU X CG  1 
ATOM   1874 C CD1 . LEU B 1 70  ? 2.975  2.119   11.190  1.00 25.34 ? 70  LEU X CD1 1 
ATOM   1875 C CD2 . LEU B 1 70  ? 3.106  -0.329  11.353  1.00 28.72 ? 70  LEU X CD2 1 
ATOM   1876 N N   . ASP B 1 71  ? -2.051 1.271   9.528   1.00 19.91 ? 71  ASP X N   1 
ATOM   1877 C CA  . ASP B 1 71  ? -2.680 1.148   8.210   1.00 21.79 ? 71  ASP X CA  1 
ATOM   1878 C C   . ASP B 1 71  ? -2.346 2.342   7.330   1.00 20.26 ? 71  ASP X C   1 
ATOM   1879 O O   . ASP B 1 71  ? -2.421 2.252   6.098   1.00 18.32 ? 71  ASP X O   1 
ATOM   1880 C CB  . ASP B 1 71  ? -4.219 1.112   8.319   1.00 18.51 ? 71  ASP X CB  1 
ATOM   1881 C CG  . ASP B 1 71  ? -4.751 -0.017  9.186   1.00 22.87 ? 71  ASP X CG  1 
ATOM   1882 O OD1 . ASP B 1 71  ? -3.981 -0.904  9.615   1.00 27.21 ? 71  ASP X OD1 1 
ATOM   1883 O OD2 . ASP B 1 71  ? -5.978 0.004   9.456   1.00 21.53 ? 71  ASP X OD2 1 
ATOM   1884 N N   . ASP B 1 72  ? -2.078 3.468   7.964   1.00 16.74 ? 72  ASP X N   1 
ATOM   1885 C CA  . ASP B 1 72  ? -1.907 4.733   7.221   1.00 19.47 ? 72  ASP X CA  1 
ATOM   1886 C C   . ASP B 1 72  ? -0.466 4.970   6.766   1.00 17.49 ? 72  ASP X C   1 
ATOM   1887 O O   . ASP B 1 72  ? -0.221 5.980   6.127   1.00 17.26 ? 72  ASP X O   1 
ATOM   1888 C CB  . ASP B 1 72  ? -2.291 5.844   8.187   1.00 22.08 ? 72  ASP X CB  1 
ATOM   1889 C CG  . ASP B 1 72  ? -3.771 5.850   8.538   1.00 28.94 ? 72  ASP X CG  1 
ATOM   1890 O OD1 . ASP B 1 72  ? -4.438 4.839   8.281   1.00 27.17 ? 72  ASP X OD1 1 
ATOM   1891 O OD2 . ASP B 1 72  ? -4.240 6.869   9.067   1.00 39.30 ? 72  ASP X OD2 1 
ATOM   1892 N N   . TYR B 1 73  ? 0.432  4.052   7.099   1.00 16.17 ? 73  TYR X N   1 
ATOM   1893 C CA  . TYR B 1 73  ? 1.864  4.310   6.803   1.00 18.19 ? 73  TYR X CA  1 
ATOM   1894 C C   . TYR B 1 73  ? 2.526  3.105   6.154   1.00 17.04 ? 73  TYR X C   1 
ATOM   1895 O O   . TYR B 1 73  ? 2.285  1.993   6.531   1.00 17.04 ? 73  TYR X O   1 
ATOM   1896 C CB  . TYR B 1 73  ? 2.604  4.729   8.073   1.00 18.70 ? 73  TYR X CB  1 
ATOM   1897 C CG  . TYR B 1 73  ? 2.018  5.938   8.749   1.00 17.11 ? 73  TYR X CG  1 
ATOM   1898 C CD1 . TYR B 1 73  ? 2.239  7.199   8.231   1.00 18.38 ? 73  TYR X CD1 1 
ATOM   1899 C CD2 . TYR B 1 73  ? 1.219  5.823   9.873   1.00 19.90 ? 73  TYR X CD2 1 
ATOM   1900 C CE1 . TYR B 1 73  ? 1.695  8.324   8.819   1.00 26.29 ? 73  TYR X CE1 1 
ATOM   1901 C CE2 . TYR B 1 73  ? 0.670  6.939   10.478  1.00 20.37 ? 73  TYR X CE2 1 
ATOM   1902 C CZ  . TYR B 1 73  ? 0.910  8.193   9.946   1.00 25.67 ? 73  TYR X CZ  1 
ATOM   1903 O OH  . TYR B 1 73  ? 0.388  9.317   10.508  1.00 26.01 ? 73  TYR X OH  1 
ATOM   1904 N N   . ASP B 1 74  ? 3.387  3.388   5.190   1.00 19.68 ? 74  ASP X N   1 
ATOM   1905 C CA  . ASP B 1 74  ? 4.117  2.306   4.505   1.00 19.67 ? 74  ASP X CA  1 
ATOM   1906 C C   . ASP B 1 74  ? 5.414  1.983   5.256   1.00 14.88 ? 74  ASP X C   1 
ATOM   1907 O O   . ASP B 1 74  ? 5.935  0.914   5.035   1.00 15.97 ? 74  ASP X O   1 
ATOM   1908 C CB  . ASP B 1 74  ? 4.425  2.715   3.074   1.00 17.60 ? 74  ASP X CB  1 
ATOM   1909 C CG  . ASP B 1 74  ? 3.192  2.994   2.233   1.00 25.15 ? 74  ASP X CG  1 
ATOM   1910 O OD1 . ASP B 1 74  ? 2.574  2.039   1.783   1.00 20.26 ? 74  ASP X OD1 1 
ATOM   1911 O OD2 . ASP B 1 74  ? 2.873  4.160   2.034   1.00 21.55 ? 74  ASP X OD2 1 
ATOM   1912 N N   . ALA B 1 75  ? 5.817  2.848   6.180   1.00 30.00 ? 75  ALA X N   1 
ATOM   1913 C CA  . ALA B 1 75  ? 7.092  2.645   6.894   1.00 30.00 ? 75  ALA X CA  1 
ATOM   1914 C C   . ALA B 1 75  ? 7.224  3.560   8.090   1.00 30.00 ? 75  ALA X C   1 
ATOM   1915 O O   . ALA B 1 75  ? 6.493  4.495   8.172   1.00 30.00 ? 75  ALA X O   1 
ATOM   1916 C CB  . ALA B 1 75  ? 8.270  2.876   5.984   1.00 30.00 ? 75  ALA X CB  1 
ATOM   1917 N N   . LEU B 1 76  ? 8.175  3.221   8.963   1.00 16.15 ? 76  LEU X N   1 
ATOM   1918 C CA  . LEU B 1 76  ? 8.515  4.060   10.134  1.00 15.02 ? 76  LEU X CA  1 
ATOM   1919 C C   . LEU B 1 76  ? 9.946  4.588   9.998   1.00 18.50 ? 76  LEU X C   1 
ATOM   1920 O O   . LEU B 1 76  ? 10.791 3.866   9.480   1.00 18.13 ? 76  LEU X O   1 
ATOM   1921 C CB  . LEU B 1 76  ? 8.436  3.215   11.406  1.00 15.64 ? 76  LEU X CB  1 
ATOM   1922 C CG  . LEU B 1 76  ? 7.060  2.690   11.790  1.00 18.42 ? 76  LEU X CG  1 
ATOM   1923 C CD1 . LEU B 1 76  ? 7.156  1.923   13.091  1.00 19.34 ? 76  LEU X CD1 1 
ATOM   1924 C CD2 . LEU B 1 76  ? 6.080  3.838   11.931  1.00 17.81 ? 76  LEU X CD2 1 
ATOM   1925 N N   . LEU B 1 77  ? 10.155 5.814   10.455  1.00 15.76 ? 77  LEU X N   1 
ATOM   1926 C CA  . LEU B 1 77  ? 11.514 6.404   10.530  1.00 13.67 ? 77  LEU X CA  1 
ATOM   1927 C C   . LEU B 1 77  ? 11.762 6.642   12.023  1.00 14.08 ? 77  LEU X C   1 
ATOM   1928 O O   . LEU B 1 77  ? 10.886 7.177   12.676  1.00 17.62 ? 77  LEU X O   1 
ATOM   1929 C CB  . LEU B 1 77  ? 11.603 7.716   9.748   1.00 18.84 ? 77  LEU X CB  1 
ATOM   1930 C CG  . LEU B 1 77  ? 12.875 8.543   9.941   1.00 15.80 ? 77  LEU X CG  1 
ATOM   1931 C CD1 . LEU B 1 77  ? 14.096 7.797   9.428   1.00 13.51 ? 77  LEU X CD1 1 
ATOM   1932 C CD2 . LEU B 1 77  ? 12.766 9.899   9.261   1.00 17.65 ? 77  LEU X CD2 1 
ATOM   1933 N N   . LEU B 1 78  ? 12.898 6.183   12.508  1.00 13.21 ? 78  LEU X N   1 
ATOM   1934 C CA  . LEU B 1 78  ? 13.232 6.293   13.946  1.00 14.46 ? 78  LEU X CA  1 
ATOM   1935 C C   . LEU B 1 78  ? 14.494 7.157   14.047  1.00 16.26 ? 78  LEU X C   1 
ATOM   1936 O O   . LEU B 1 78  ? 15.587 6.588   14.042  1.00 15.92 ? 78  LEU X O   1 
ATOM   1937 C CB  . LEU B 1 78  ? 13.452 4.902   14.502  1.00 14.09 ? 78  LEU X CB  1 
ATOM   1938 C CG  . LEU B 1 78  ? 12.207 4.039   14.647  1.00 17.83 ? 78  LEU X CG  1 
ATOM   1939 C CD1 . LEU B 1 78  ? 12.537 2.767   15.401  1.00 13.30 ? 78  LEU X CD1 1 
ATOM   1940 C CD2 . LEU B 1 78  ? 11.121 4.814   15.364  1.00 17.35 ? 78  LEU X CD2 1 
ATOM   1941 N N   . PRO B 1 79  ? 14.389 8.509   14.079  1.00 17.05 ? 79  PRO X N   1 
ATOM   1942 C CA  . PRO B 1 79  ? 15.579 9.335   14.313  1.00 13.63 ? 79  PRO X CA  1 
ATOM   1943 C C   . PRO B 1 79  ? 16.183 9.084   15.690  1.00 14.58 ? 79  PRO X C   1 
ATOM   1944 O O   . PRO B 1 79  ? 15.519 8.650   16.636  1.00 18.65 ? 79  PRO X O   1 
ATOM   1945 C CB  . PRO B 1 79  ? 15.029 10.764  14.184  1.00 20.02 ? 79  PRO X CB  1 
ATOM   1946 C CG  . PRO B 1 79  ? 13.825 10.586  13.240  1.00 18.71 ? 79  PRO X CG  1 
ATOM   1947 C CD  . PRO B 1 79  ? 13.204 9.333   13.767  1.00 19.31 ? 79  PRO X CD  1 
ATOM   1948 N N   . GLY B 1 80  ? 17.477 9.337   15.784  1.00 13.97 ? 80  GLY X N   1 
ATOM   1949 C CA  . GLY B 1 80  ? 18.156 9.217   17.054  1.00 16.00 ? 80  GLY X CA  1 
ATOM   1950 C C   . GLY B 1 80  ? 18.069 10.457  17.914  1.00 14.19 ? 80  GLY X C   1 
ATOM   1951 O O   . GLY B 1 80  ? 16.996 11.040  18.083  1.00 16.17 ? 80  GLY X O   1 
ATOM   1952 N N   . GLY B 1 81  ? 19.201 10.871  18.471  1.00 23.08 ? 81  GLY X N   1 
ATOM   1953 C CA  . GLY B 1 81  ? 19.154 11.774  19.597  1.00 11.58 ? 81  GLY X CA  1 
ATOM   1954 C C   . GLY B 1 81  ? 19.112 10.903  20.824  1.00 12.64 ? 81  GLY X C   1 
ATOM   1955 O O   . GLY B 1 81  ? 18.135 10.172  21.020  1.00 16.26 ? 81  GLY X O   1 
ATOM   1956 N N   . VAL B 1 82  ? 20.178 10.936  21.633  1.00 15.38 ? 82  VAL X N   1 
ATOM   1957 C CA  . VAL B 1 82  ? 20.214 10.114  22.841  1.00 18.16 ? 82  VAL X CA  1 
ATOM   1958 C C   . VAL B 1 82  ? 19.016 10.409  23.753  1.00 16.96 ? 82  VAL X C   1 
ATOM   1959 O O   . VAL B 1 82  ? 18.435 9.495   24.353  1.00 15.76 ? 82  VAL X O   1 
ATOM   1960 C CB  . VAL B 1 82  ? 21.589 10.220  23.540  1.00 12.50 ? 82  VAL X CB  1 
ATOM   1961 C CG1 . VAL B 1 82  ? 21.835 11.637  24.029  1.00 20.74 ? 82  VAL X CG1 1 
ATOM   1962 C CG2 . VAL B 1 82  ? 21.635 9.243   24.709  1.00 22.95 ? 82  VAL X CG2 1 
ATOM   1963 N N   . ILE B 1 83  ? 18.605 11.679  23.850  1.00 15.30 ? 83  ILE X N   1 
ATOM   1964 C CA  . ILE B 1 83  ? 17.522 12.048  24.759  1.00 15.27 ? 83  ILE X CA  1 
ATOM   1965 C C   . ILE B 1 83  ? 16.197 11.477  24.272  1.00 17.23 ? 83  ILE X C   1 
ATOM   1966 O O   . ILE B 1 83  ? 15.469 10.828  25.032  1.00 19.09 ? 83  ILE X O   1 
ATOM   1967 C CB  . ILE B 1 83  ? 17.456 13.574  24.957  1.00 14.96 ? 83  ILE X CB  1 
ATOM   1968 C CG1 . ILE B 1 83  ? 18.675 14.073  25.748  1.00 17.34 ? 83  ILE X CG1 1 
ATOM   1969 C CG2 . ILE B 1 83  ? 16.146 13.971  25.663  1.00 15.59 ? 83  ILE X CG2 1 
ATOM   1970 C CD1 . ILE B 1 83  ? 18.790 15.592  25.770  1.00 15.80 ? 83  ILE X CD1 1 
ATOM   1971 N N   . ASN B 1 84  ? 15.872 11.703  22.997  1.00 15.36 ? 84  ASN X N   1 
ATOM   1972 C CA  . ASN B 1 84  ? 14.653 11.139  22.422  1.00 17.21 ? 84  ASN X CA  1 
ATOM   1973 C C   . ASN B 1 84  ? 14.674 9.624   22.510  1.00 16.49 ? 84  ASN X C   1 
ATOM   1974 O O   . ASN B 1 84  ? 13.680 8.997   22.892  1.00 16.30 ? 84  ASN X O   1 
ATOM   1975 C CB  . ASN B 1 84  ? 14.549 11.550  20.955  1.00 16.50 ? 84  ASN X CB  1 
ATOM   1976 C CG  . ASN B 1 84  ? 13.639 10.624  20.145  1.00 19.27 ? 84  ASN X CG  1 
ATOM   1977 O OD1 . ASN B 1 84  ? 12.468 10.465  20.473  1.00 16.74 ? 84  ASN X OD1 1 
ATOM   1978 N ND2 . ASN B 1 84  ? 14.182 10.021  19.061  1.00 16.40 ? 84  ASN X ND2 1 
ATOM   1979 N N   . SER B 1 85  ? 15.815 9.021   22.165  1.00 13.69 ? 85  SER X N   1 
ATOM   1980 C CA  . SER B 1 85  ? 15.881 7.571   22.062  1.00 16.37 ? 85  SER X CA  1 
ATOM   1981 C C   . SER B 1 85  ? 15.691 6.924   23.425  1.00 12.30 ? 85  SER X C   1 
ATOM   1982 O O   . SER B 1 85  ? 15.061 5.867   23.539  1.00 15.67 ? 85  SER X O   1 
ATOM   1983 C CB  . SER B 1 85  ? 17.206 7.147   21.417  1.00 12.30 ? 85  SER X CB  1 
ATOM   1984 O OG  . SER B 1 85  ? 17.372 7.795   20.152  1.00 16.61 ? 85  SER X OG  1 
ATOM   1985 N N   . ASP B 1 86  ? 16.270 7.529   24.463  1.00 14.34 ? 86  ASP X N   1 
ATOM   1986 C CA  . ASP B 1 86  ? 16.088 7.016   25.808  1.00 19.01 ? 86  ASP X CA  1 
ATOM   1987 C C   . ASP B 1 86  ? 14.647 7.158   26.285  1.00 19.94 ? 86  ASP X C   1 
ATOM   1988 O O   . ASP B 1 86  ? 14.164 6.293   27.023  1.00 15.32 ? 86  ASP X O   1 
ATOM   1989 C CB  . ASP B 1 86  ? 17.090 7.702   26.736  1.00 16.87 ? 86  ASP X CB  1 
ATOM   1990 C CG  . ASP B 1 86  ? 16.933 7.269   28.166  1.00 14.55 ? 86  ASP X CG  1 
ATOM   1991 O OD1 . ASP B 1 86  ? 17.429 6.176   28.511  1.00 18.17 ? 86  ASP X OD1 1 
ATOM   1992 O OD2 . ASP B 1 86  ? 16.303 8.031   28.927  1.00 16.93 ? 86  ASP X OD2 1 
ATOM   1993 N N   . GLN B 1 87  ? 13.954 8.223   25.869  1.00 16.80 ? 87  GLN X N   1 
ATOM   1994 C CA  . GLN B 1 87  ? 12.572 8.483   26.277  1.00 21.57 ? 87  GLN X CA  1 
ATOM   1995 C C   . GLN B 1 87  ? 11.595 7.569   25.549  1.00 20.75 ? 87  GLN X C   1 
ATOM   1996 O O   . GLN B 1 87  ? 10.703 6.970   26.161  1.00 18.51 ? 87  GLN X O   1 
ATOM   1997 C CB  . GLN B 1 87  ? 12.228 9.915   25.885  1.00 14.56 ? 87  GLN X CB  1 
ATOM   1998 C CG  . GLN B 1 87  ? 12.559 10.923  26.952  1.00 25.00 ? 87  GLN X CG  1 
ATOM   1999 C CD  . GLN B 1 87  ? 12.639 12.328  26.409  1.00 25.77 ? 87  GLN X CD  1 
ATOM   2000 O OE1 . GLN B 1 87  ? 12.288 12.587  25.256  1.00 19.52 ? 87  GLN X OE1 1 
ATOM   2001 N NE2 . GLN B 1 87  ? 13.129 13.249  27.232  1.00 31.75 ? 87  GLN X NE2 1 
ATOM   2002 N N   . ILE B 1 88  ? 11.742 7.464   24.231  1.00 17.25 ? 88  ILE X N   1 
ATOM   2003 C CA  . ILE B 1 88  ? 10.713 6.833   23.411  1.00 18.85 ? 88  ILE X CA  1 
ATOM   2004 C C   . ILE B 1 88  ? 10.685 5.326   23.614  1.00 17.75 ? 88  ILE X C   1 
ATOM   2005 O O   . ILE B 1 88  ? 9.632  4.687   23.458  1.00 16.10 ? 88  ILE X O   1 
ATOM   2006 C CB  . ILE B 1 88  ? 10.913 7.242   21.939  1.00 12.03 ? 88  ILE X CB  1 
ATOM   2007 C CG1 . ILE B 1 88  ? 9.654  7.019   21.114  1.00 14.22 ? 88  ILE X CG1 1 
ATOM   2008 C CG2 . ILE B 1 88  ? 12.129 6.513   21.330  1.00 16.11 ? 88  ILE X CG2 1 
ATOM   2009 C CD1 . ILE B 1 88  ? 9.823  7.443   19.663  1.00 16.18 ? 88  ILE X CD1 1 
ATOM   2010 N N   . ARG B 1 89  ? 11.818 4.742   24.003  1.00 14.50 ? 89  ARG X N   1 
ATOM   2011 C CA  . ARG B 1 89  ? 11.962 3.294   23.973  1.00 19.43 ? 89  ARG X CA  1 
ATOM   2012 C C   . ARG B 1 89  ? 10.999 2.610   24.927  1.00 20.87 ? 89  ARG X C   1 
ATOM   2013 O O   . ARG B 1 89  ? 10.650 1.446   24.715  1.00 23.63 ? 89  ARG X O   1 
ATOM   2014 C CB  . ARG B 1 89  ? 13.399 2.906   24.334  1.00 14.21 ? 89  ARG X CB  1 
ATOM   2015 C CG  . ARG B 1 89  ? 13.681 3.036   25.830  1.00 14.30 ? 89  ARG X CG  1 
ATOM   2016 C CD  . ARG B 1 89  ? 15.110 2.664   26.143  1.00 17.53 ? 89  ARG X CD  1 
ATOM   2017 N NE  . ARG B 1 89  ? 15.438 1.305   25.727  1.00 17.40 ? 89  ARG X NE  1 
ATOM   2018 C CZ  . ARG B 1 89  ? 16.585 0.689   25.990  1.00 13.12 ? 89  ARG X CZ  1 
ATOM   2019 N NH1 . ARG B 1 89  ? 17.579 1.303   26.617  1.00 13.32 ? 89  ARG X NH1 1 
ATOM   2020 N NH2 . ARG B 1 89  ? 16.741 -0.577  25.621  1.00 17.08 ? 89  ARG X NH2 1 
ATOM   2021 N N   . SER B 1 90  ? 10.585 3.304   25.990  1.00 17.21 ? 90  SER X N   1 
ATOM   2022 C CA  . SER B 1 90  ? 9.701  2.769   27.010  1.00 17.42 ? 90  SER X CA  1 
ATOM   2023 C C   . SER B 1 90  ? 8.225  3.029   26.734  1.00 20.85 ? 90  SER X C   1 
ATOM   2024 O O   . SER B 1 90  ? 7.382  2.560   27.505  1.00 21.26 ? 90  SER X O   1 
ATOM   2025 C CB  . SER B 1 90  ? 10.095 3.338   28.374  1.00 25.54 ? 90  SER X CB  1 
ATOM   2026 O OG  . SER B 1 90  ? 9.409  4.547   28.634  1.00 35.18 ? 90  SER X OG  1 
ATOM   2027 N N   . LEU B 1 91  ? 7.885  3.735   25.650  1.00 19.68 ? 91  LEU X N   1 
ATOM   2028 C CA  . LEU B 1 91  ? 6.494  4.082   25.375  1.00 14.71 ? 91  LEU X CA  1 
ATOM   2029 C C   . LEU B 1 91  ? 5.787  2.929   24.673  1.00 16.96 ? 91  LEU X C   1 
ATOM   2030 O O   . LEU B 1 91  ? 6.174  2.531   23.567  1.00 18.63 ? 91  LEU X O   1 
ATOM   2031 C CB  . LEU B 1 91  ? 6.408  5.371   24.559  1.00 18.34 ? 91  LEU X CB  1 
ATOM   2032 C CG  . LEU B 1 91  ? 6.934  6.638   25.238  1.00 19.54 ? 91  LEU X CG  1 
ATOM   2033 C CD1 . LEU B 1 91  ? 6.814  7.832   24.319  1.00 22.69 ? 91  LEU X CD1 1 
ATOM   2034 C CD2 . LEU B 1 91  ? 6.153  6.903   26.513  1.00 22.67 ? 91  LEU X CD2 1 
ATOM   2035 N N   . ALA B 1 92  ? 4.725  2.418   25.299  1.00 30.00 ? 92  ALA X N   1 
ATOM   2036 C CA  . ALA B 1 92  ? 4.089  1.202   24.807  1.00 30.00 ? 92  ALA X CA  1 
ATOM   2037 C C   . ALA B 1 92  ? 3.517  1.373   23.407  1.00 30.00 ? 92  ALA X C   1 
ATOM   2038 O O   . ALA B 1 92  ? 3.533  0.424   22.619  1.00 30.00 ? 92  ALA X O   1 
ATOM   2039 C CB  . ALA B 1 92  ? 3.001  0.740   25.779  1.00 30.00 ? 92  ALA X CB  1 
ATOM   2040 N N   . LYS B 1 93  ? 3.005  2.564   23.081  1.00 20.76 ? 93  LYS X N   1 
ATOM   2041 C CA  . LYS B 1 93  ? 2.385  2.775   21.776  1.00 22.42 ? 93  LYS X CA  1 
ATOM   2042 C C   . LYS B 1 93  ? 3.418  2.943   20.675  1.00 23.70 ? 93  LYS X C   1 
ATOM   2043 O O   . LYS B 1 93  ? 3.139  2.601   19.515  1.00 19.08 ? 93  LYS X O   1 
ATOM   2044 C CB  . LYS B 1 93  ? 1.457  3.993   21.810  1.00 19.48 ? 93  LYS X CB  1 
ATOM   2045 C CG  . LYS B 1 93  ? 0.094  3.735   22.450  1.00 30.91 ? 93  LYS X CG  1 
ATOM   2046 C CD  . LYS B 1 93  ? -0.720 2.759   21.631  1.00 27.37 ? 93  LYS X CD  1 
ATOM   2047 C CE  . LYS B 1 93  ? -1.878 2.170   22.420  1.00 39.01 ? 93  LYS X CE  1 
ATOM   2048 N NZ  . LYS B 1 93  ? -2.635 1.155   21.628  1.00 37.06 ? 93  LYS X NZ  1 
ATOM   2049 N N   . ALA B 1 94  ? 4.585  3.501   21.007  1.00 30.00 ? 94  ALA X N   1 
ATOM   2050 C CA  . ALA B 1 94  ? 5.697  3.509   20.064  1.00 30.00 ? 94  ALA X CA  1 
ATOM   2051 C C   . ALA B 1 94  ? 6.176  2.092   19.792  1.00 30.00 ? 94  ALA X C   1 
ATOM   2052 O O   . ALA B 1 94  ? 6.380  1.714   18.635  1.00 30.00 ? 94  ALA X O   1 
ATOM   2053 C CB  . ALA B 1 94  ? 6.826  4.383   20.609  1.00 30.00 ? 94  ALA X CB  1 
ATOM   2054 N N   . GLN B 1 95  ? 6.340  1.292   20.850  1.00 20.98 ? 95  GLN X N   1 
ATOM   2055 C CA  . GLN B 1 95  ? 6.673  -0.121  20.688  1.00 19.24 ? 95  GLN X CA  1 
ATOM   2056 C C   . GLN B 1 95  ? 5.636  -0.842  19.834  1.00 17.92 ? 95  GLN X C   1 
ATOM   2057 O O   . GLN B 1 95  ? 5.988  -1.656  18.973  1.00 19.24 ? 95  GLN X O   1 
ATOM   2058 C CB  . GLN B 1 95  ? 6.777  -0.793  22.061  1.00 17.67 ? 95  GLN X CB  1 
ATOM   2059 C CG  . GLN B 1 95  ? 7.909  -0.282  22.914  1.00 17.36 ? 95  GLN X CG  1 
ATOM   2060 C CD  . GLN B 1 95  ? 8.015  -1.044  24.213  1.00 23.40 ? 95  GLN X CD  1 
ATOM   2061 O OE1 . GLN B 1 95  ? 7.379  -2.086  24.388  1.00 24.19 ? 95  GLN X OE1 1 
ATOM   2062 N NE2 . GLN B 1 95  ? 8.816  -0.533  25.132  1.00 22.60 ? 95  GLN X NE2 1 
ATOM   2063 N N   . GLU B 1 96  ? 4.350  -0.571  20.076  1.00 20.64 ? 96  GLU X N   1 
ATOM   2064 C CA  . GLU B 1 96  ? 3.297  -1.236  19.316  1.00 19.94 ? 96  GLU X CA  1 
ATOM   2065 C C   . GLU B 1 96  ? 3.379  -0.892  17.836  1.00 19.50 ? 96  GLU X C   1 
ATOM   2066 O O   . GLU B 1 96  ? 3.180  -1.758  16.977  1.00 16.85 ? 96  GLU X O   1 
ATOM   2067 C CB  . GLU B 1 96  ? 1.931  -0.847  19.875  1.00 19.22 ? 96  GLU X CB  1 
ATOM   2068 C CG  . GLU B 1 96  ? 0.754  -1.609  19.298  1.00 26.52 ? 96  GLU X CG  1 
ATOM   2069 C CD  . GLU B 1 96  ? -0.567 -0.963  19.684  1.00 32.64 ? 96  GLU X CD  1 
ATOM   2070 O OE1 . GLU B 1 96  ? -0.792 -0.783  20.901  1.00 33.93 ? 96  GLU X OE1 1 
ATOM   2071 O OE2 . GLU B 1 96  ? -1.368 -0.637  18.782  1.00 34.02 ? 96  GLU X OE2 1 
ATOM   2072 N N   . LEU B 1 97  ? 3.653  0.373   17.521  1.00 16.41 ? 97  LEU X N   1 
ATOM   2073 C CA  . LEU B 1 97  ? 3.832  0.758   16.125  1.00 17.80 ? 97  LEU X CA  1 
ATOM   2074 C C   . LEU B 1 97  ? 4.992  0.005   15.484  1.00 17.26 ? 97  LEU X C   1 
ATOM   2075 O O   . LEU B 1 97  ? 4.896  -0.437  14.334  1.00 19.10 ? 97  LEU X O   1 
ATOM   2076 C CB  . LEU B 1 97  ? 4.043  2.268   16.025  1.00 22.02 ? 97  LEU X CB  1 
ATOM   2077 C CG  . LEU B 1 97  ? 2.780  3.123   16.126  1.00 18.91 ? 97  LEU X CG  1 
ATOM   2078 C CD1 . LEU B 1 97  ? 3.126  4.587   16.202  1.00 18.72 ? 97  LEU X CD1 1 
ATOM   2079 C CD2 . LEU B 1 97  ? 1.855  2.861   14.951  1.00 26.21 ? 97  LEU X CD2 1 
ATOM   2080 N N   . ALA B 1 98  ? 6.111  -0.129  16.201  1.00 30.00 ? 98  ALA X N   1 
ATOM   2081 C CA  . ALA B 1 98  ? 7.249  -0.851  15.643  1.00 30.00 ? 98  ALA X CA  1 
ATOM   2082 C C   . ALA B 1 98  ? 6.944  -2.336  15.508  1.00 30.00 ? 98  ALA X C   1 
ATOM   2083 O O   . ALA B 1 98  ? 7.353  -2.980  14.533  1.00 30.00 ? 98  ALA X O   1 
ATOM   2084 C CB  . ALA B 1 98  ? 8.484  -0.629  16.518  1.00 30.00 ? 98  ALA X CB  1 
ATOM   2085 N N   . ILE B 1 99  ? 6.209  -2.895  16.473  1.00 18.46 ? 99  ILE X N   1 
ATOM   2086 C CA  . ILE B 1 99  ? 5.848  -4.306  16.409  1.00 20.37 ? 99  ILE X CA  1 
ATOM   2087 C C   . ILE B 1 99  ? 4.912  -4.554  15.237  1.00 17.56 ? 99  ILE X C   1 
ATOM   2088 O O   . ILE B 1 99  ? 5.101  -5.496  14.464  1.00 19.54 ? 99  ILE X O   1 
ATOM   2089 C CB  . ILE B 1 99  ? 5.237  -4.766  17.746  1.00 19.48 ? 99  ILE X CB  1 
ATOM   2090 C CG1 . ILE B 1 99  ? 6.314  -4.822  18.826  1.00 21.24 ? 99  ILE X CG1 1 
ATOM   2091 C CG2 . ILE B 1 99  ? 4.570  -6.125  17.600  1.00 21.59 ? 99  ILE X CG2 1 
ATOM   2092 C CD1 . ILE B 1 99  ? 5.740  -4.780  20.227  1.00 20.56 ? 99  ILE X CD1 1 
ATOM   2093 N N   . ARG B 1 100 ? 3.899  -3.696  15.084  1.00 30.00 ? 100 ARG X N   1 
ATOM   2094 C CA  . ARG B 1 100 ? 2.981  -3.807  13.953  1.00 30.00 ? 100 ARG X CA  1 
ATOM   2095 C C   . ARG B 1 100 ? 3.702  -3.677  12.618  1.00 30.00 ? 100 ARG X C   1 
ATOM   2096 O O   . ARG B 1 100 ? 3.333  -4.357  11.653  1.00 30.00 ? 100 ARG X O   1 
ATOM   2097 C CB  . ARG B 1 100 ? 1.834  -2.797  14.099  1.00 30.00 ? 100 ARG X CB  1 
ATOM   2098 C CG  . ARG B 1 100 ? 0.983  -3.044  15.349  1.00 30.00 ? 100 ARG X CG  1 
ATOM   2099 C CD  . ARG B 1 100 ? -0.422 -2.433  15.309  1.00 30.00 ? 100 ARG X CD  1 
ATOM   2100 N NE  . ARG B 1 100 ? -0.485 -1.148  16.004  1.00 30.00 ? 100 ARG X NE  1 
ATOM   2101 C CZ  . ARG B 1 100 ? -1.019 -0.039  15.505  1.00 30.00 ? 100 ARG X CZ  1 
ATOM   2102 N NH1 . ARG B 1 100 ? -1.616 -0.028  14.322  1.00 30.00 ? 100 ARG X NH1 1 
ATOM   2103 N NH2 . ARG B 1 100 ? -0.942 1.089   16.207  1.00 30.00 ? 100 ARG X NH2 1 
ATOM   2104 N N   . ALA B 1 101 ? 4.745  -2.847  12.542  1.00 30.00 ? 101 ALA X N   1 
ATOM   2105 C CA  . ALA B 1 101 ? 5.491  -2.751  11.289  1.00 30.00 ? 101 ALA X CA  1 
ATOM   2106 C C   . ALA B 1 101 ? 6.173  -4.064  10.954  1.00 30.00 ? 101 ALA X C   1 
ATOM   2107 O O   . ALA B 1 101 ? 6.201  -4.473  9.789   1.00 30.00 ? 101 ALA X O   1 
ATOM   2108 C CB  . ALA B 1 101 ? 6.496  -1.599  11.320  1.00 30.00 ? 101 ALA X CB  1 
ATOM   2109 N N   . GLU B 1 102 ? 6.723  -4.744  11.961  1.00 21.54 ? 102 GLU X N   1 
ATOM   2110 C CA  . GLU B 1 102 ? 7.367  -6.027  11.711  1.00 22.07 ? 102 GLU X CA  1 
ATOM   2111 C C   . GLU B 1 102 ? 6.351  -7.059  11.231  1.00 23.41 ? 102 GLU X C   1 
ATOM   2112 O O   . GLU B 1 102 ? 6.575  -7.743  10.221  1.00 25.12 ? 102 GLU X O   1 
ATOM   2113 C CB  . GLU B 1 102 ? 8.088  -6.501  12.975  1.00 23.09 ? 102 GLU X CB  1 
ATOM   2114 C CG  . GLU B 1 102 ? 9.120  -7.598  12.735  1.00 29.88 ? 102 GLU X CG  1 
ATOM   2115 C CD  . GLU B 1 102 ? 8.512  -8.975  12.566  1.00 32.77 ? 102 GLU X CD  1 
ATOM   2116 O OE1 . GLU B 1 102 ? 7.346  -9.174  12.980  1.00 32.92 ? 102 GLU X OE1 1 
ATOM   2117 O OE2 . GLU B 1 102 ? 9.212  -9.866  12.036  1.00 40.83 ? 102 GLU X OE2 1 
ATOM   2118 N N   . GLN B 1 103 ? 5.219  -7.175  11.940  1.00 23.84 ? 103 GLN X N   1 
ATOM   2119 C CA  . GLN B 1 103 ? 4.175  -8.124  11.549  1.00 24.76 ? 103 GLN X CA  1 
ATOM   2120 C C   . GLN B 1 103 ? 3.677  -7.853  10.134  1.00 26.52 ? 103 GLN X C   1 
ATOM   2121 O O   . GLN B 1 103 ? 3.350  -8.786  9.392   1.00 28.84 ? 103 GLN X O   1 
ATOM   2122 C CB  . GLN B 1 103 ? 3.010  -8.075  12.542  1.00 24.75 ? 103 GLN X CB  1 
ATOM   2123 C CG  . GLN B 1 103 ? 3.411  -7.752  13.959  1.00 37.20 ? 103 GLN X CG  1 
ATOM   2124 C CD  . GLN B 1 103 ? 2.253  -7.774  14.939  1.00 45.98 ? 103 GLN X CD  1 
ATOM   2125 O OE1 . GLN B 1 103 ? 1.460  -6.830  15.005  1.00 43.51 ? 103 GLN X OE1 1 
ATOM   2126 N NE2 . GLN B 1 103 ? 2.183  -8.825  15.747  1.00 47.44 ? 103 GLN X NE2 1 
ATOM   2127 N N   . ALA B 1 104 ? 3.635  -6.587  9.732   1.00 30.00 ? 104 ALA X N   1 
ATOM   2128 C CA  . ALA B 1 104 ? 3.097  -6.208  8.434   1.00 30.00 ? 104 ALA X CA  1 
ATOM   2129 C C   . ALA B 1 104 ? 4.157  -6.133  7.340   1.00 30.00 ? 104 ALA X C   1 
ATOM   2130 O O   . ALA B 1 104 ? 3.840  -5.717  6.217   1.00 30.00 ? 104 ALA X O   1 
ATOM   2131 C CB  . ALA B 1 104 ? 2.351  -4.878  8.545   1.00 30.00 ? 104 ALA X CB  1 
ATOM   2132 N N   . SER B 1 105 ? 5.379  -6.573  7.635   1.00 22.46 ? 105 SER X N   1 
ATOM   2133 C CA  . SER B 1 105 ? 6.506  -6.462  6.663   1.00 23.64 ? 105 SER X CA  1 
ATOM   2134 C C   . SER B 1 105 ? 6.585  -5.036  6.104   1.00 26.41 ? 105 SER X C   1 
ATOM   2135 O O   . SER B 1 105 ? 6.607  -4.870  4.902   1.00 24.33 ? 105 SER X O   1 
ATOM   2136 C CB  . SER B 1 105 ? 6.412  -7.490  5.592   1.00 22.62 ? 105 SER X CB  1 
ATOM   2137 O OG  . SER B 1 105 ? 6.466  -8.791  6.140   1.00 30.97 ? 105 SER X OG  1 
ATOM   2138 N N   . LYS B 1 106 ? 6.639  -4.049  6.983   1.00 16.46 ? 106 LYS X N   1 
ATOM   2139 C CA  . LYS B 1 106 ? 6.793  -2.656  6.545   1.00 16.50 ? 106 LYS X CA  1 
ATOM   2140 C C   . LYS B 1 106 ? 8.180  -2.194  6.978   1.00 21.06 ? 106 LYS X C   1 
ATOM   2141 O O   . LYS B 1 106 ? 8.636  -2.632  8.033   1.00 19.46 ? 106 LYS X O   1 
ATOM   2142 C CB  . LYS B 1 106 ? 5.672  -1.785  7.095   1.00 23.46 ? 106 LYS X CB  1 
ATOM   2143 C CG  . LYS B 1 106 ? 4.343  -1.988  6.393   1.00 18.40 ? 106 LYS X CG  1 
ATOM   2144 C CD  . LYS B 1 106 ? 3.277  -1.061  6.875   1.00 22.89 ? 106 LYS X CD  1 
ATOM   2145 C CE  . LYS B 1 106 ? 1.915  -1.461  6.353   1.00 22.11 ? 106 LYS X CE  1 
ATOM   2146 N NZ  . LYS B 1 106 ? 0.972  -0.325  6.314   1.00 24.25 ? 106 LYS X NZ  1 
ATOM   2147 N N   . PRO B 1 107 ? 8.879  -1.415  6.143   1.00 14.02 ? 107 PRO X N   1 
ATOM   2148 C CA  . PRO B 1 107 ? 10.190 -0.933  6.487   1.00 15.95 ? 107 PRO X CA  1 
ATOM   2149 C C   . PRO B 1 107 ? 10.305 -0.092  7.758   1.00 13.36 ? 107 PRO X C   1 
ATOM   2150 O O   . PRO B 1 107 ? 9.416  0.622   8.084   1.00 16.10 ? 107 PRO X O   1 
ATOM   2151 C CB  . PRO B 1 107 ? 10.565 -0.020  5.323   1.00 16.71 ? 107 PRO X CB  1 
ATOM   2152 C CG  . PRO B 1 107 ? 9.818  -0.618  4.160   1.00 18.02 ? 107 PRO X CG  1 
ATOM   2153 C CD  . PRO B 1 107 ? 8.513  -1.076  4.773   1.00 15.57 ? 107 PRO X CD  1 
ATOM   2154 N N   . VAL B 1 108 ? 11.389 -0.320  8.477   1.00 16.33 ? 108 VAL X N   1 
ATOM   2155 C CA  . VAL B 1 108 ? 11.716 0.518   9.660   1.00 13.21 ? 108 VAL X CA  1 
ATOM   2156 C C   . VAL B 1 108 ? 13.138 1.020   9.384   1.00 13.96 ? 108 VAL X C   1 
ATOM   2157 O O   . VAL B 1 108 ? 14.023 0.183   9.191   1.00 15.98 ? 108 VAL X O   1 
ATOM   2158 C CB  . VAL B 1 108 ? 11.655 -0.278  10.977  1.00 14.09 ? 108 VAL X CB  1 
ATOM   2159 C CG1 . VAL B 1 108 ? 12.079 0.576   12.160  1.00 16.65 ? 108 VAL X CG1 1 
ATOM   2160 C CG2 . VAL B 1 108 ? 10.267 -0.850  11.222  1.00 16.42 ? 108 VAL X CG2 1 
ATOM   2161 N N   . ALA B 1 109 ? 13.302 2.329   9.333   1.00 30.00 ? 109 ALA X N   1 
ATOM   2162 C CA  . ALA B 1 109 ? 14.628 2.947   9.130   1.00 30.00 ? 109 ALA X CA  1 
ATOM   2163 C C   . ALA B 1 109 ? 15.031 3.590   10.443  1.00 30.00 ? 109 ALA X C   1 
ATOM   2164 O O   . ALA B 1 109 ? 14.276 4.407   10.920  1.00 30.00 ? 109 ALA X O   1 
ATOM   2165 C CB  . ALA B 1 109 ? 14.524 3.940   8.019   1.00 30.00 ? 109 ALA X CB  1 
ATOM   2166 N N   . VAL B 1 110 ? 16.201 3.199   10.944  1.00 12.10 ? 110 VAL X N   1 
ATOM   2167 C CA  . VAL B 1 110 ? 16.621 3.657   12.294  1.00 15.41 ? 110 VAL X CA  1 
ATOM   2168 C C   . VAL B 1 110 ? 18.055 4.169   12.237  1.00 14.49 ? 110 VAL X C   1 
ATOM   2169 O O   . VAL B 1 110 ? 18.826 3.659   11.460  1.00 15.67 ? 110 VAL X O   1 
ATOM   2170 C CB  . VAL B 1 110 ? 16.428 2.509   13.295  1.00 15.55 ? 110 VAL X CB  1 
ATOM   2171 C CG1 . VAL B 1 110 ? 17.193 1.252   12.915  1.00 12.02 ? 110 VAL X CG1 1 
ATOM   2172 C CG2 . VAL B 1 110 ? 16.734 2.915   14.711  1.00 10.69 ? 110 VAL X CG2 1 
ATOM   2173 N N   . ILE B 1 111 ? 18.361 5.144   13.085  1.00 12.43 ? 111 ILE X N   1 
ATOM   2174 C CA  . ILE B 1 111 ? 19.695 5.766   12.977  1.00 15.48 ? 111 ILE X CA  1 
ATOM   2175 C C   . ILE B 1 111 ? 20.216 6.196   14.352  1.00 13.84 ? 111 ILE X C   1 
ATOM   2176 O O   . ILE B 1 111 ? 19.421 6.654   15.156  1.00 18.07 ? 111 ILE X O   1 
ATOM   2177 C CB  . ILE B 1 111 ? 19.700 6.893   11.908  1.00 19.18 ? 111 ILE X CB  1 
ATOM   2178 C CG1 . ILE B 1 111 ? 21.080 7.546   11.786  1.00 15.75 ? 111 ILE X CG1 1 
ATOM   2179 C CG2 . ILE B 1 111 ? 18.604 7.915   12.160  1.00 18.42 ? 111 ILE X CG2 1 
ATOM   2180 C CD1 . ILE B 1 111 ? 21.334 8.214   10.460  1.00 16.70 ? 111 ILE X CD1 1 
ATOM   2181 N N   . CYS B 1 112 ? 21.487 5.899   14.611  1.00 16.93 ? 112 CYS X N   1 
ATOM   2182 C CA  . CYS B 1 112 ? 22.211 6.413   15.805  1.00 13.95 ? 112 CYS X CA  1 
ATOM   2183 C C   . CYS B 1 112 ? 21.782 5.744   17.130  1.00 16.63 ? 112 CYS X C   1 
ATOM   2184 O O   . CYS B 1 112 ? 22.056 4.541   17.186  1.00 19.43 ? 112 CYS X O   1 
ATOM   2185 C CB  . CYS B 1 112 ? 22.317 7.925   15.708  1.00 30.00 ? 112 CYS X CB  1 
ATOM   2186 S SG  . CYS B 1 112 ? 23.767 8.656   16.509  1.00 30.00 ? 112 CYS X SG  1 
ATOM   2187 N N   . HIS B 1 113 ? 21.095 6.491   18.026  1.00 14.00 ? 113 HIS X N   1 
ATOM   2188 C CA  . HIS B 1 113 ? 20.606 5.872   19.290  1.00 16.93 ? 113 HIS X CA  1 
ATOM   2189 C C   . HIS B 1 113 ? 19.188 5.312   19.134  1.00 17.51 ? 113 HIS X C   1 
ATOM   2190 O O   . HIS B 1 113 ? 18.720 4.678   20.032  1.00 15.70 ? 113 HIS X O   1 
ATOM   2191 C CB  . HIS B 1 113 ? 20.632 6.900   20.426  1.00 16.36 ? 113 HIS X CB  1 
ATOM   2192 C CG  . HIS B 1 113 ? 21.975 7.372   20.859  1.00 21.97 ? 113 HIS X CG  1 
ATOM   2193 N ND1 . HIS B 1 113 ? 22.633 8.400   20.231  1.00 17.43 ? 113 HIS X ND1 1 
ATOM   2194 C CD2 . HIS B 1 113 ? 22.749 7.016   21.900  1.00 18.48 ? 113 HIS X CD2 1 
ATOM   2195 C CE1 . HIS B 1 113 ? 23.768 8.635   20.840  1.00 24.56 ? 113 HIS X CE1 1 
ATOM   2196 N NE2 . HIS B 1 113 ? 23.863 7.796   21.862  1.00 15.91 ? 113 HIS X NE2 1 
ATOM   2197 N N   . GLY B 1 114 ? 18.597 5.467   17.963  1.00 14.63 ? 114 GLY X N   1 
ATOM   2198 C CA  . GLY B 1 114 ? 17.175 5.127   17.777  1.00 12.75 ? 114 GLY X CA  1 
ATOM   2199 C C   . GLY B 1 114 ? 16.784 3.670   17.920  1.00 12.16 ? 114 GLY X C   1 
ATOM   2200 O O   . GLY B 1 114 ? 15.598 3.421   18.025  1.00 18.95 ? 114 GLY X O   1 
ATOM   2201 N N   . ALA B 1 115 ? 17.730 2.760   17.978  1.00 30.00 ? 115 ALA X N   1 
ATOM   2202 C CA  . ALA B 1 115 ? 17.353 1.333   17.978  1.00 30.00 ? 115 ALA X CA  1 
ATOM   2203 C C   . ALA B 1 115 ? 16.962 0.873   19.371  1.00 30.00 ? 115 ALA X C   1 
ATOM   2204 O O   . ALA B 1 115 ? 16.524 -0.247  19.502  1.00 30.00 ? 115 ALA X O   1 
ATOM   2205 C CB  . ALA B 1 115 ? 18.484 0.484   17.436  1.00 30.00 ? 115 ALA X CB  1 
ATOM   2206 N N   . TRP B 1 116 ? 17.114 1.745   20.360  1.00 17.58 ? 116 TRP X N   1 
ATOM   2207 C CA  . TRP B 1 116 ? 16.652 1.330   21.680  1.00 13.01 ? 116 TRP X CA  1 
ATOM   2208 C C   . TRP B 1 116 ? 15.162 1.003   21.682  1.00 16.05 ? 116 TRP X C   1 
ATOM   2209 O O   . TRP B 1 116 ? 14.718 0.104   22.410  1.00 16.87 ? 116 TRP X O   1 
ATOM   2210 C CB  . TRP B 1 116 ? 16.930 2.432   22.688  1.00 13.19 ? 116 TRP X CB  1 
ATOM   2211 C CG  . TRP B 1 116 ? 18.311 2.379   23.303  1.00 13.88 ? 116 TRP X CG  1 
ATOM   2212 C CD1 . TRP B 1 116 ? 19.013 1.260   23.677  1.00 13.10 ? 116 TRP X CD1 1 
ATOM   2213 C CD2 . TRP B 1 116 ? 19.112 3.499   23.664  1.00 14.95 ? 116 TRP X CD2 1 
ATOM   2214 N NE1 . TRP B 1 116 ? 20.213 1.629   24.239  1.00 15.73 ? 116 TRP X NE1 1 
ATOM   2215 C CE2 . TRP B 1 116 ? 20.300 2.998   24.235  1.00 13.07 ? 116 TRP X CE2 1 
ATOM   2216 C CE3 . TRP B 1 116 ? 18.951 4.881   23.544  1.00 15.54 ? 116 TRP X CE3 1 
ATOM   2217 C CZ2 . TRP B 1 116 ? 21.317 3.835   24.693  1.00 16.48 ? 116 TRP X CZ2 1 
ATOM   2218 C CZ3 . TRP B 1 116 ? 19.964 5.710   24.005  1.00 17.81 ? 116 TRP X CZ3 1 
ATOM   2219 C CH2 . TRP B 1 116 ? 21.131 5.186   24.561  1.00 10.76 ? 116 TRP X CH2 1 
ATOM   2220 N N   . LEU B 1 117 ? 14.367 1.756   20.922  1.00 15.19 ? 117 LEU X N   1 
ATOM   2221 C CA  . LEU B 1 117 ? 12.958 1.404   20.769  1.00 10.92 ? 117 LEU X CA  1 
ATOM   2222 C C   . LEU B 1 117 ? 12.813 -0.020  20.244  1.00 15.70 ? 117 LEU X C   1 
ATOM   2223 O O   . LEU B 1 117 ? 11.967 -0.783  20.718  1.00 16.22 ? 117 LEU X O   1 
ATOM   2224 C CB  . LEU B 1 117 ? 12.271 2.403   19.835  1.00 11.91 ? 117 LEU X CB  1 
ATOM   2225 C CG  . LEU B 1 117 ? 10.778 2.179   19.575  1.00 15.58 ? 117 LEU X CG  1 
ATOM   2226 C CD1 . LEU B 1 117 ? 10.026 2.123   20.889  1.00 13.69 ? 117 LEU X CD1 1 
ATOM   2227 C CD2 . LEU B 1 117 ? 10.202 3.285   18.706  1.00 15.76 ? 117 LEU X CD2 1 
ATOM   2228 N N   . LEU B 1 118 ? 13.646 -0.401  19.265  1.00 11.63 ? 118 LEU X N   1 
ATOM   2229 C CA  . LEU B 1 118 ? 13.556 -1.745  18.698  1.00 13.97 ? 118 LEU X CA  1 
ATOM   2230 C C   . LEU B 1 118 ? 13.938 -2.818  19.715  1.00 19.10 ? 118 LEU X C   1 
ATOM   2231 O O   . LEU B 1 118 ? 13.282 -3.866  19.786  1.00 21.34 ? 118 LEU X O   1 
ATOM   2232 C CB  . LEU B 1 118 ? 14.401 -1.834  17.425  1.00 15.64 ? 118 LEU X CB  1 
ATOM   2233 C CG  . LEU B 1 118 ? 13.994 -0.867  16.303  1.00 14.80 ? 118 LEU X CG  1 
ATOM   2234 C CD1 . LEU B 1 118 ? 14.858 -1.062  15.053  1.00 18.34 ? 118 LEU X CD1 1 
ATOM   2235 C CD2 . LEU B 1 118 ? 12.478 -0.942  15.980  1.00 16.76 ? 118 LEU X CD2 1 
ATOM   2236 N N   A ILE B 1 119 ? 14.994 -2.566  20.506  0.99 14.70 ? 119 ILE X N   1 
ATOM   2237 N N   B ILE B 1 119 ? 14.959 -2.578  20.536  0.01 14.78 ? 119 ILE X N   1 
ATOM   2238 C CA  A ILE B 1 119 ? 15.388 -3.479  21.589  0.99 16.85 ? 119 ILE X CA  1 
ATOM   2239 C CA  B ILE B 1 119 ? 15.317 -3.595  21.521  0.01 16.87 ? 119 ILE X CA  1 
ATOM   2240 C C   A ILE B 1 119 ? 14.236 -3.684  22.563  0.99 17.79 ? 119 ILE X C   1 
ATOM   2241 C C   B ILE B 1 119 ? 14.257 -3.705  22.619  0.01 17.76 ? 119 ILE X C   1 
ATOM   2242 O O   A ILE B 1 119 ? 13.886 -4.816  22.924  0.99 17.28 ? 119 ILE X O   1 
ATOM   2243 O O   B ILE B 1 119 ? 13.965 -4.806  23.102  0.01 17.51 ? 119 ILE X O   1 
ATOM   2244 C CB  A ILE B 1 119 ? 16.608 -2.916  22.341  0.99 15.93 ? 119 ILE X CB  1 
ATOM   2245 C CB  B ILE B 1 119 ? 16.757 -3.407  22.045  0.01 17.14 ? 119 ILE X CB  1 
ATOM   2246 C CG1 A ILE B 1 119 ? 17.882 -2.978  21.507  0.99 16.44 ? 119 ILE X CG1 1 
ATOM   2247 C CG1 B ILE B 1 119 ? 16.784 -2.729  23.416  0.01 17.80 ? 119 ILE X CG1 1 
ATOM   2248 C CG2 A ILE B 1 119 ? 16.824 -3.653  23.667  0.99 18.76 ? 119 ILE X CG2 1 
ATOM   2249 C CG2 B ILE B 1 119 ? 17.601 -2.642  21.040  0.01 16.60 ? 119 ILE X CG2 1 
ATOM   2250 C CD1 A ILE B 1 119 ? 19.040 -2.209  22.145  0.99 12.12 ? 119 ILE X CD1 1 
ATOM   2251 C CD1 B ILE B 1 119 ? 16.792 -3.679  24.596  0.01 16.97 ? 119 ILE X CD1 1 
ATOM   2252 N N   . SER B 1 120 ? 13.650 -2.582  23.021  1.00 18.85 ? 120 SER X N   1 
ATOM   2253 C CA  . SER B 1 120 ? 12.628 -2.652  24.060  1.00 21.57 ? 120 SER X CA  1 
ATOM   2254 C C   . SER B 1 120 ? 11.307 -3.198  23.540  1.00 20.05 ? 120 SER X C   1 
ATOM   2255 O O   . SER B 1 120 ? 10.551 -3.804  24.304  1.00 20.13 ? 120 SER X O   1 
ATOM   2256 C CB  . SER B 1 120 ? 12.472 -1.301  24.769  1.00 20.15 ? 120 SER X CB  1 
ATOM   2257 O OG  . SER B 1 120 ? 13.607 -1.019  25.588  1.00 17.56 ? 120 SER X OG  1 
ATOM   2258 N N   . ALA B 1 121 ? 11.023 -3.018  22.248  1.00 30.00 ? 121 ALA X N   1 
ATOM   2259 C CA  . ALA B 1 121 ? 9.863  -3.647  21.627  1.00 30.00 ? 121 ALA X CA  1 
ATOM   2260 C C   . ALA B 1 121 ? 10.053 -5.142  21.401  1.00 30.00 ? 121 ALA X C   1 
ATOM   2261 O O   . ALA B 1 121 ? 9.119  -5.809  20.942  1.00 30.00 ? 121 ALA X O   1 
ATOM   2262 C CB  . ALA B 1 121 ? 9.553  -2.969  20.291  1.00 30.00 ? 121 ALA X CB  1 
ATOM   2263 N N   . GLY B 1 122 ? 11.236 -5.677  21.695  1.00 19.64 ? 122 GLY X N   1 
ATOM   2264 C CA  . GLY B 1 122 ? 11.513 -7.081  21.475  1.00 22.90 ? 122 GLY X CA  1 
ATOM   2265 C C   . GLY B 1 122 ? 11.800 -7.459  20.042  1.00 22.15 ? 122 GLY X C   1 
ATOM   2266 O O   . GLY B 1 122 ? 11.563 -8.609  19.659  1.00 24.38 ? 122 GLY X O   1 
ATOM   2267 N N   . LEU B 1 123 ? 12.329 -6.532  19.241  1.00 16.46 ? 123 LEU X N   1 
ATOM   2268 C CA  . LEU B 1 123 ? 12.418 -6.706  17.797  1.00 18.66 ? 123 LEU X CA  1 
ATOM   2269 C C   . LEU B 1 123 ? 13.830 -6.896  17.253  1.00 23.06 ? 123 LEU X C   1 
ATOM   2270 O O   . LEU B 1 123 ? 13.976 -7.073  16.037  1.00 18.98 ? 123 LEU X O   1 
ATOM   2271 C CB  . LEU B 1 123 ? 11.793 -5.510  17.074  1.00 14.16 ? 123 LEU X CB  1 
ATOM   2272 C CG  . LEU B 1 123 ? 10.277 -5.286  17.173  1.00 16.49 ? 123 LEU X CG  1 
ATOM   2273 C CD1 . LEU B 1 123 ? 9.943  -3.959  16.563  1.00 14.04 ? 123 LEU X CD1 1 
ATOM   2274 C CD2 . LEU B 1 123 ? 9.477  -6.360  16.462  1.00 21.80 ? 123 LEU X CD2 1 
ATOM   2275 N N   . VAL B 1 124 ? 14.884 -6.839  18.071  1.00 22.28 ? 124 VAL X N   1 
ATOM   2276 C CA  . VAL B 1 124 ? 16.220 -6.973  17.484  1.00 17.61 ? 124 VAL X CA  1 
ATOM   2277 C C   . VAL B 1 124 ? 16.766 -8.384  17.548  1.00 21.65 ? 124 VAL X C   1 
ATOM   2278 O O   . VAL B 1 124 ? 17.783 -8.675  16.895  1.00 15.63 ? 124 VAL X O   1 
ATOM   2279 C CB  . VAL B 1 124 ? 17.242 -5.944  18.009  1.00 22.14 ? 124 VAL X CB  1 
ATOM   2280 C CG1 . VAL B 1 124 ? 16.656 -4.551  17.985  1.00 22.90 ? 124 VAL X CG1 1 
ATOM   2281 C CG2 . VAL B 1 124 ? 17.741 -6.333  19.393  1.00 24.60 ? 124 VAL X CG2 1 
ATOM   2282 N N   . GLN B 1 125 ? 16.120 -9.268  18.292  1.00 19.15 ? 125 GLN X N   1 
ATOM   2283 C CA  . GLN B 1 125 ? 16.596 -10.627 18.463  1.00 16.80 ? 125 GLN X CA  1 
ATOM   2284 C C   . GLN B 1 125 ? 16.686 -11.320 17.106  1.00 24.22 ? 125 GLN X C   1 
ATOM   2285 O O   . GLN B 1 125 ? 15.703 -11.376 16.362  1.00 24.25 ? 125 GLN X O   1 
ATOM   2286 C CB  . GLN B 1 125 ? 15.578 -11.309 19.364  1.00 27.47 ? 125 GLN X CB  1 
ATOM   2287 C CG  . GLN B 1 125 ? 16.142 -12.190 20.432  1.00 31.75 ? 125 GLN X CG  1 
ATOM   2288 C CD  . GLN B 1 125 ? 15.043 -12.930 21.153  1.00 33.96 ? 125 GLN X CD  1 
ATOM   2289 O OE1 . GLN B 1 125 ? 13.967 -12.384 21.384  1.00 34.39 ? 125 GLN X OE1 1 
ATOM   2290 N NE2 . GLN B 1 125 ? 15.299 -14.162 21.513  1.00 45.35 ? 125 GLN X NE2 1 
ATOM   2291 N N   . GLY B 1 126 ? 17.880 -11.802 16.760  1.00 19.64 ? 126 GLY X N   1 
ATOM   2292 C CA  . GLY B 1 126 ? 18.099 -12.459 15.486  1.00 20.24 ? 126 GLY X CA  1 
ATOM   2293 C C   . GLY B 1 126 ? 18.257 -11.544 14.290  1.00 26.59 ? 126 GLY X C   1 
ATOM   2294 O O   . GLY B 1 126 ? 18.460 -12.047 13.175  1.00 25.01 ? 126 GLY X O   1 
ATOM   2295 N N   . ARG B 1 127 ? 18.180 -10.230 14.470  1.00 30.00 ? 127 ARG X N   1 
ATOM   2296 C CA  . ARG B 1 127 ? 18.293 -9.300  13.358  1.00 30.00 ? 127 ARG X CA  1 
ATOM   2297 C C   . ARG B 1 127 ? 19.664 -8.640  13.313  1.00 30.00 ? 127 ARG X C   1 
ATOM   2298 O O   . ARG B 1 127 ? 20.310 -8.421  14.339  1.00 30.00 ? 127 ARG X O   1 
ATOM   2299 C CB  . ARG B 1 127 ? 17.200 -8.230  13.398  1.00 30.00 ? 127 ARG X CB  1 
ATOM   2300 C CG  . ARG B 1 127 ? 15.827 -8.775  13.717  1.00 30.00 ? 127 ARG X CG  1 
ATOM   2301 C CD  . ARG B 1 127 ? 15.333 -9.646  12.572  1.00 30.00 ? 127 ARG X CD  1 
ATOM   2302 N NE  . ARG B 1 127 ? 15.265 -8.931  11.304  1.00 30.00 ? 127 ARG X NE  1 
ATOM   2303 C CZ  . ARG B 1 127 ? 14.262 -8.150  10.926  1.00 30.00 ? 127 ARG X CZ  1 
ATOM   2304 N NH1 . ARG B 1 127 ? 13.245 -7.885  11.734  1.00 30.00 ? 127 ARG X NH1 1 
ATOM   2305 N NH2 . ARG B 1 127 ? 14.265 -7.638  9.696   1.00 30.00 ? 127 ARG X NH2 1 
ATOM   2306 N N   . THR B 1 128 ? 20.092 -8.321  12.096  1.00 17.11 ? 128 THR X N   1 
ATOM   2307 C CA  . THR B 1 128 ? 21.335 -7.606  11.854  1.00 15.92 ? 128 THR X CA  1 
ATOM   2308 C C   . THR B 1 128 ? 21.038 -6.122  11.722  1.00 17.40 ? 128 THR X C   1 
ATOM   2309 O O   . THR B 1 128 ? 20.153 -5.726  10.965  1.00 16.60 ? 128 THR X O   1 
ATOM   2310 C CB  . THR B 1 128 ? 21.980 -8.110  10.562  1.00 19.08 ? 128 THR X CB  1 
ATOM   2311 O OG1 . THR B 1 128 ? 22.359 -9.484  10.710  1.00 24.15 ? 128 THR X OG1 1 
ATOM   2312 C CG2 . THR B 1 128 ? 23.195 -7.265  10.170  1.00 23.22 ? 128 THR X CG2 1 
ATOM   2313 N N   . LEU B 1 129 ? 21.773 -5.303  12.460  1.00 15.80 ? 129 LEU X N   1 
ATOM   2314 C CA  . LEU B 1 129 ? 21.609 -3.864  12.340  1.00 12.26 ? 129 LEU X CA  1 
ATOM   2315 C C   . LEU B 1 129 ? 22.903 -3.222  12.801  1.00 14.97 ? 129 LEU X C   1 
ATOM   2316 O O   . LEU B 1 129 ? 23.752 -3.872  13.416  1.00 15.93 ? 129 LEU X O   1 
ATOM   2317 C CB  . LEU B 1 129 ? 20.399 -3.350  13.131  1.00 14.82 ? 129 LEU X CB  1 
ATOM   2318 C CG  . LEU B 1 129 ? 20.529 -3.461  14.645  1.00 15.89 ? 129 LEU X CG  1 
ATOM   2319 C CD1 . LEU B 1 129 ? 19.668 -2.402  15.325  1.00 19.43 ? 129 LEU X CD1 1 
ATOM   2320 C CD2 . LEU B 1 129 ? 20.146 -4.858  15.085  1.00 20.50 ? 129 LEU X CD2 1 
ATOM   2321 N N   . THR B 1 130 ? 23.017 -1.942  12.481  1.00 14.65 ? 130 THR X N   1 
ATOM   2322 C CA  . THR B 1 130 ? 24.118 -1.121  12.995  1.00 15.06 ? 130 THR X CA  1 
ATOM   2323 C C   . THR B 1 130 ? 23.507 -0.026  13.879  1.00 16.87 ? 130 THR X C   1 
ATOM   2324 O O   . THR B 1 130 ? 22.276 0.017   13.984  1.00 16.67 ? 130 THR X O   1 
ATOM   2325 C CB  . THR B 1 130 ? 24.972 -0.567  11.854  1.00 13.65 ? 130 THR X CB  1 
ATOM   2326 O OG1 . THR B 1 130 ? 26.168 -0.055  12.439  1.00 12.91 ? 130 THR X OG1 1 
ATOM   2327 C CG2 . THR B 1 130 ? 24.285 0.506   11.048  1.00 14.69 ? 130 THR X CG2 1 
ATOM   2328 N N   . SER B 1 131 ? 24.357 0.804   14.473  1.00 14.98 ? 131 SER X N   1 
ATOM   2329 C CA  . SER B 1 131 ? 23.903 1.899   15.357  1.00 15.00 ? 131 SER X CA  1 
ATOM   2330 C C   . SER B 1 131 ? 25.097 2.725   15.771  1.00 16.49 ? 131 SER X C   1 
ATOM   2331 O O   . SER B 1 131 ? 26.200 2.403   15.377  1.00 16.15 ? 131 SER X O   1 
ATOM   2332 C CB  . SER B 1 131 ? 23.301 1.336   16.617  1.00 11.39 ? 131 SER X CB  1 
ATOM   2333 O OG  . SER B 1 131 ? 24.300 0.786   17.460  1.00 12.08 ? 131 SER X OG  1 
ATOM   2334 N N   . TRP B 1 132 ? 24.835 3.763   16.534  1.00 17.42 ? 132 TRP X N   1 
ATOM   2335 C CA  . TRP B 1 132 ? 25.941 4.478   17.179  1.00 15.64 ? 132 TRP X CA  1 
ATOM   2336 C C   . TRP B 1 132 ? 26.618 3.439   18.058  1.00 14.04 ? 132 TRP X C   1 
ATOM   2337 O O   . TRP B 1 132 ? 25.948 2.639   18.662  1.00 15.73 ? 132 TRP X O   1 
ATOM   2338 C CB  . TRP B 1 132 ? 25.369 5.631   18.016  1.00 17.60 ? 132 TRP X CB  1 
ATOM   2339 C CG  . TRP B 1 132 ? 26.378 6.536   18.633  1.00 17.57 ? 132 TRP X CG  1 
ATOM   2340 C CD1 . TRP B 1 132 ? 26.600 6.711   19.964  1.00 16.69 ? 132 TRP X CD1 1 
ATOM   2341 C CD2 . TRP B 1 132 ? 27.285 7.413   17.947  1.00 22.56 ? 132 TRP X CD2 1 
ATOM   2342 N NE1 . TRP B 1 132 ? 27.599 7.619   20.152  1.00 18.17 ? 132 TRP X NE1 1 
ATOM   2343 C CE2 . TRP B 1 132 ? 28.036 8.072   18.939  1.00 14.82 ? 132 TRP X CE2 1 
ATOM   2344 C CE3 . TRP B 1 132 ? 27.550 7.692   16.602  1.00 22.19 ? 132 TRP X CE3 1 
ATOM   2345 C CZ2 . TRP B 1 132 ? 29.027 8.997   18.628  1.00 22.56 ? 132 TRP X CZ2 1 
ATOM   2346 C CZ3 . TRP B 1 132 ? 28.528 8.607   16.294  1.00 20.58 ? 132 TRP X CZ3 1 
ATOM   2347 C CH2 . TRP B 1 132 ? 29.256 9.246   17.296  1.00 19.46 ? 132 TRP X CH2 1 
ATOM   2348 N N   . PRO B 1 133 ? 27.947 3.416   18.142  1.00 20.12 ? 133 PRO X N   1 
ATOM   2349 C CA  . PRO B 1 133 ? 28.607 2.343   18.881  1.00 14.68 ? 133 PRO X CA  1 
ATOM   2350 C C   . PRO B 1 133 ? 28.280 2.200   20.376  1.00 16.77 ? 133 PRO X C   1 
ATOM   2351 O O   . PRO B 1 133 ? 28.488 1.183   20.905  1.00 18.34 ? 133 PRO X O   1 
ATOM   2352 C CB  . PRO B 1 133 ? 30.094 2.574   18.572  1.00 17.88 ? 133 PRO X CB  1 
ATOM   2353 C CG  . PRO B 1 133 ? 30.098 3.422   17.319  1.00 24.65 ? 133 PRO X CG  1 
ATOM   2354 C CD  . PRO B 1 133 ? 28.875 4.301   17.446  1.00 19.06 ? 133 PRO X CD  1 
ATOM   2355 N N   . SER B 1 134 ? 27.761 3.255   20.979  1.00 19.24 ? 134 SER X N   1 
ATOM   2356 C CA  . SER B 1 134 ? 27.349 3.162   22.393  1.00 15.97 ? 134 SER X CA  1 
ATOM   2357 C C   . SER B 1 134 ? 26.259 2.099   22.562  1.00 20.12 ? 134 SER X C   1 
ATOM   2358 O O   . SER B 1 134 ? 26.154 1.561   23.650  1.00 23.34 ? 134 SER X O   1 
ATOM   2359 C CB  . SER B 1 134 ? 26.907 4.499   22.918  1.00 17.82 ? 134 SER X CB  1 
ATOM   2360 O OG  . SER B 1 134 ? 25.645 4.880   22.404  1.00 17.90 ? 134 SER X OG  1 
ATOM   2361 N N   . LEU B 1 135 ? 25.475 1.818   21.520  1.00 17.60 ? 135 LEU X N   1 
ATOM   2362 C CA  . LEU B 1 135 ? 24.320 0.889   21.639  1.00 17.53 ? 135 LEU X CA  1 
ATOM   2363 C C   . LEU B 1 135 ? 24.744 -0.529  21.284  1.00 17.04 ? 135 LEU X C   1 
ATOM   2364 O O   . LEU B 1 135 ? 23.937 -1.414  21.389  1.00 16.26 ? 135 LEU X O   1 
ATOM   2365 C CB  . LEU B 1 135 ? 23.275 1.359   20.617  1.00 19.58 ? 135 LEU X CB  1 
ATOM   2366 C CG  . LEU B 1 135 ? 22.083 2.126   21.158  1.00 17.40 ? 135 LEU X CG  1 
ATOM   2367 C CD1 . LEU B 1 135 ? 22.475 3.571   21.366  1.00 21.02 ? 135 LEU X CD1 1 
ATOM   2368 C CD2 . LEU B 1 135 ? 20.921 2.026   20.187  1.00 16.31 ? 135 LEU X CD2 1 
ATOM   2369 N N   . LYS B 1 136 ? 26.002 -0.702  20.888  1.00 14.50 ? 136 LYS X N   1 
ATOM   2370 C CA  . LYS B 1 136 ? 26.445 -2.021  20.397  1.00 17.18 ? 136 LYS X CA  1 
ATOM   2371 C C   . LYS B 1 136 ? 26.199 -3.102  21.460  1.00 17.15 ? 136 LYS X C   1 
ATOM   2372 O O   . LYS B 1 136 ? 25.685 -4.163  21.120  1.00 16.14 ? 136 LYS X O   1 
ATOM   2373 C CB  . LYS B 1 136 ? 27.904 -1.931  19.930  1.00 17.27 ? 136 LYS X CB  1 
ATOM   2374 C CG  . LYS B 1 136 ? 28.616 -3.275  19.812  1.00 16.98 ? 136 LYS X CG  1 
ATOM   2375 C CD  . LYS B 1 136 ? 30.043 -3.204  19.315  1.00 21.03 ? 136 LYS X CD  1 
ATOM   2376 C CE  . LYS B 1 136 ? 30.552 -4.577  18.931  1.00 26.35 ? 136 LYS X CE  1 
ATOM   2377 N NZ  . LYS B 1 136 ? 31.938 -4.547  18.414  1.00 29.36 ? 136 LYS X NZ  1 
ATOM   2378 N N   . ASP B 1 137 ? 26.586 -2.816  22.700  1.00 16.09 ? 137 ASP X N   1 
ATOM   2379 C CA  . ASP B 1 137 ? 26.430 -3.836  23.732  1.00 17.12 ? 137 ASP X CA  1 
ATOM   2380 C C   . ASP B 1 137 ? 24.969 -4.142  23.979  1.00 14.36 ? 137 ASP X C   1 
ATOM   2381 O O   . ASP B 1 137 ? 24.594 -5.310  24.117  1.00 14.46 ? 137 ASP X O   1 
ATOM   2382 C CB  . ASP B 1 137 ? 27.085 -3.405  25.046  1.00 19.68 ? 137 ASP X CB  1 
ATOM   2383 C CG  . ASP B 1 137 ? 28.580 -3.354  24.953  1.00 22.89 ? 137 ASP X CG  1 
ATOM   2384 O OD1 . ASP B 1 137 ? 29.151 -3.877  23.975  1.00 21.98 ? 137 ASP X OD1 1 
ATOM   2385 O OD2 . ASP B 1 137 ? 29.189 -2.769  25.850  1.00 20.02 ? 137 ASP X OD2 1 
ATOM   2386 N N   . ASP B 1 138 ? 24.129 -3.107  23.989  1.00 14.64 ? 138 ASP X N   1 
ATOM   2387 C CA  . ASP B 1 138 ? 22.709 -3.315  24.247  1.00 15.87 ? 138 ASP X CA  1 
ATOM   2388 C C   . ASP B 1 138 ? 22.071 -4.137  23.145  1.00 13.63 ? 138 ASP X C   1 
ATOM   2389 O O   . ASP B 1 138 ? 21.249 -5.022  23.415  1.00 16.43 ? 138 ASP X O   1 
ATOM   2390 C CB  . ASP B 1 138 ? 22.002 -1.968  24.387  1.00 15.17 ? 138 ASP X CB  1 
ATOM   2391 C CG  . ASP B 1 138 ? 22.503 -1.175  25.564  1.00 14.56 ? 138 ASP X CG  1 
ATOM   2392 O OD1 . ASP B 1 138 ? 22.966 -1.790  26.560  1.00 14.44 ? 138 ASP X OD1 1 
ATOM   2393 O OD2 . ASP B 1 138 ? 22.488 0.067   25.469  1.00 18.26 ? 138 ASP X OD2 1 
ATOM   2394 N N   . ILE B 1 139 ? 22.442 -3.859  21.897  1.00 17.04 ? 139 ILE X N   1 
ATOM   2395 C CA  . ILE B 1 139 ? 21.898 -4.626  20.781  1.00 14.88 ? 139 ILE X CA  1 
ATOM   2396 C C   . ILE B 1 139 ? 22.381 -6.070  20.826  1.00 15.11 ? 139 ILE X C   1 
ATOM   2397 O O   . ILE B 1 139 ? 21.600 -7.008  20.647  1.00 15.03 ? 139 ILE X O   1 
ATOM   2398 C CB  . ILE B 1 139 ? 22.209 -3.943  19.437  1.00 17.94 ? 139 ILE X CB  1 
ATOM   2399 C CG1 . ILE B 1 139 ? 21.453 -2.616  19.313  1.00 14.43 ? 139 ILE X CG1 1 
ATOM   2400 C CG2 . ILE B 1 139 ? 21.920 -4.882  18.301  1.00 16.35 ? 139 ILE X CG2 1 
ATOM   2401 C CD1 . ILE B 1 139 ? 21.948 -1.690  18.218  1.00 19.62 ? 139 ILE X CD1 1 
ATOM   2402 N N   . ASN B 1 140 ? 23.673 -6.275  21.080  1.00 19.08 ? 140 ASN X N   1 
ATOM   2403 C CA  . ASN B 1 140 ? 24.184 -7.638  21.154  1.00 18.14 ? 140 ASN X CA  1 
ATOM   2404 C C   . ASN B 1 140 ? 23.590 -8.383  22.337  1.00 17.27 ? 140 ASN X C   1 
ATOM   2405 O O   . ASN B 1 140 ? 23.246 -9.567  22.228  1.00 21.51 ? 140 ASN X O   1 
ATOM   2406 C CB  . ASN B 1 140 ? 25.702 -7.617  21.232  1.00 18.22 ? 140 ASN X CB  1 
ATOM   2407 C CG  . ASN B 1 140 ? 26.353 -7.514  19.865  1.00 18.09 ? 140 ASN X CG  1 
ATOM   2408 O OD1 . ASN B 1 140 ? 25.742 -7.834  18.838  1.00 20.94 ? 140 ASN X OD1 1 
ATOM   2409 N ND2 . ASN B 1 140 ? 27.611 -7.080  19.848  1.00 18.16 ? 140 ASN X ND2 1 
ATOM   2410 N N   . ASN B 1 141 ? 23.433 -7.702  23.470  1.00 16.68 ? 141 ASN X N   1 
ATOM   2411 C CA  . ASN B 1 141 ? 22.841 -8.348  24.637  1.00 15.64 ? 141 ASN X CA  1 
ATOM   2412 C C   . ASN B 1 141 ? 21.369 -8.676  24.403  1.00 19.08 ? 141 ASN X C   1 
ATOM   2413 O O   . ASN B 1 141 ? 20.848 -9.643  24.975  1.00 20.38 ? 141 ASN X O   1 
ATOM   2414 C CB  . ASN B 1 141 ? 23.005 -7.457  25.867  1.00 15.05 ? 141 ASN X CB  1 
ATOM   2415 C CG  . ASN B 1 141 ? 24.442 -7.399  26.364  1.00 18.59 ? 141 ASN X CG  1 
ATOM   2416 O OD1 . ASN B 1 141 ? 25.254 -8.290  26.091  1.00 20.78 ? 141 ASN X OD1 1 
ATOM   2417 N ND2 . ASN B 1 141 ? 24.772 -6.322  27.065  1.00 15.49 ? 141 ASN X ND2 1 
ATOM   2418 N N   . ALA B 1 142 ? 20.677 -7.871  23.605  1.00 30.00 ? 142 ALA X N   1 
ATOM   2419 C CA  . ALA B 1 142 ? 19.276 -8.130  23.300  1.00 30.00 ? 142 ALA X CA  1 
ATOM   2420 C C   . ALA B 1 142 ? 19.086 -9.261  22.299  1.00 30.00 ? 142 ALA X C   1 
ATOM   2421 O O   . ALA B 1 142 ? 17.943 -9.614  22.003  1.00 30.00 ? 142 ALA X O   1 
ATOM   2422 C CB  . ALA B 1 142 ? 18.604 -6.863  22.775  1.00 30.00 ? 142 ALA X CB  1 
ATOM   2423 N N   . GLY B 1 143 ? 20.165 -9.836  21.781  1.00 23.53 ? 143 GLY X N   1 
ATOM   2424 C CA  . GLY B 1 143 ? 20.085 -10.862 20.766  1.00 21.73 ? 143 GLY X CA  1 
ATOM   2425 C C   . GLY B 1 143 ? 20.296 -10.381 19.353  1.00 24.99 ? 143 GLY X C   1 
ATOM   2426 O O   . GLY B 1 143 ? 20.199 -11.193 18.421  1.00 23.52 ? 143 GLY X O   1 
ATOM   2427 N N   . GLY B 1 144 ? 20.590 -9.092  19.155  1.00 19.08 ? 144 GLY X N   1 
ATOM   2428 C CA  . GLY B 1 144 ? 20.841 -8.590  17.819  1.00 15.24 ? 144 GLY X CA  1 
ATOM   2429 C C   . GLY B 1 144 ? 22.212 -8.984  17.294  1.00 18.79 ? 144 GLY X C   1 
ATOM   2430 O O   . GLY B 1 144 ? 23.093 -9.438  18.005  1.00 19.22 ? 144 GLY X O   1 
ATOM   2431 N N   . HIS B 1 145 ? 22.373 -8.839  15.996  1.00 19.54 ? 145 HIS X N   1 
ATOM   2432 C CA  . HIS B 1 145 ? 23.664 -9.052  15.344  1.00 20.82 ? 145 HIS X CA  1 
ATOM   2433 C C   . HIS B 1 145 ? 24.205 -7.689  14.939  1.00 22.46 ? 145 HIS X C   1 
ATOM   2434 O O   . HIS B 1 145 ? 23.935 -7.208  13.839  1.00 17.35 ? 145 HIS X O   1 
ATOM   2435 C CB  . HIS B 1 145 ? 23.505 -9.927  14.118  1.00 19.06 ? 145 HIS X CB  1 
ATOM   2436 C CG  . HIS B 1 145 ? 24.783 -10.112 13.361  1.00 21.01 ? 145 HIS X CG  1 
ATOM   2437 N ND1 . HIS B 1 145 ? 24.837 -10.110 11.985  1.00 25.14 ? 145 HIS X ND1 1 
ATOM   2438 C CD2 . HIS B 1 145 ? 26.059 -10.270 13.788  1.00 19.71 ? 145 HIS X CD2 1 
ATOM   2439 C CE1 . HIS B 1 145 ? 26.090 -10.270 11.595  1.00 22.81 ? 145 HIS X CE1 1 
ATOM   2440 N NE2 . HIS B 1 145 ? 26.853 -10.365 12.667  1.00 22.73 ? 145 HIS X NE2 1 
ATOM   2441 N N   . TRP B 1 146 ? 24.976 -7.071  15.827  1.00 19.53 ? 146 TRP X N   1 
ATOM   2442 C CA  . TRP B 1 146 ? 25.491 -5.736  15.564  1.00 17.49 ? 146 TRP X CA  1 
ATOM   2443 C C   . TRP B 1 146 ? 26.645 -5.802  14.574  1.00 18.37 ? 146 TRP X C   1 
ATOM   2444 O O   . TRP B 1 146 ? 27.585 -6.590  14.740  1.00 17.73 ? 146 TRP X O   1 
ATOM   2445 C CB  . TRP B 1 146 ? 25.944 -5.054  16.855  1.00 16.16 ? 146 TRP X CB  1 
ATOM   2446 C CG  . TRP B 1 146 ? 26.221 -3.592  16.641  1.00 14.67 ? 146 TRP X CG  1 
ATOM   2447 C CD1 . TRP B 1 146 ? 25.337 -2.571  16.789  1.00 18.57 ? 146 TRP X CD1 1 
ATOM   2448 C CD2 . TRP B 1 146 ? 27.460 -2.993  16.200  1.00 16.32 ? 146 TRP X CD2 1 
ATOM   2449 N NE1 . TRP B 1 146 ? 25.942 -1.377  16.481  1.00 13.84 ? 146 TRP X NE1 1 
ATOM   2450 C CE2 . TRP B 1 146 ? 27.243 -1.601  16.133  1.00 14.40 ? 146 TRP X CE2 1 
ATOM   2451 C CE3 . TRP B 1 146 ? 28.728 -3.495  15.879  1.00 18.31 ? 146 TRP X CE3 1 
ATOM   2452 C CZ2 . TRP B 1 146 ? 28.235 -0.704  15.749  1.00 14.29 ? 146 TRP X CZ2 1 
ATOM   2453 C CZ3 . TRP B 1 146 ? 29.718 -2.603  15.494  1.00 18.77 ? 146 TRP X CZ3 1 
ATOM   2454 C CH2 . TRP B 1 146 ? 29.460 -1.221  15.421  1.00 16.11 ? 146 TRP X CH2 1 
ATOM   2455 N N   . VAL B 1 147 ? 26.555 -4.975  13.531  1.00 18.19 ? 147 VAL X N   1 
ATOM   2456 C CA  . VAL B 1 147 ? 27.579 -4.842  12.510  1.00 15.70 ? 147 VAL X CA  1 
ATOM   2457 C C   . VAL B 1 147 ? 27.901 -3.363  12.387  1.00 15.08 ? 147 VAL X C   1 
ATOM   2458 O O   . VAL B 1 147 ? 27.078 -2.501  12.695  1.00 15.24 ? 147 VAL X O   1 
ATOM   2459 C CB  . VAL B 1 147 ? 27.106 -5.386  11.143  1.00 19.66 ? 147 VAL X CB  1 
ATOM   2460 C CG1 . VAL B 1 147 ? 26.865 -6.884  11.234  1.00 18.78 ? 147 VAL X CG1 1 
ATOM   2461 C CG2 . VAL B 1 147 ? 25.848 -4.661  10.694  1.00 14.37 ? 147 VAL X CG2 1 
ATOM   2462 N N   . ASP B 1 148 ? 29.099 -3.082  11.876  1.00 13.45 ? 148 ASP X N   1 
ATOM   2463 C CA  . ASP B 1 148 ? 29.602 -1.721  11.700  1.00 10.87 ? 148 ASP X CA  1 
ATOM   2464 C C   . ASP B 1 148 ? 29.503 -1.429  10.212  1.00 15.04 ? 148 ASP X C   1 
ATOM   2465 O O   . ASP B 1 148 ? 30.386 -1.799  9.440   1.00 18.78 ? 148 ASP X O   1 
ATOM   2466 C CB  . ASP B 1 148 ? 31.056 -1.671  12.161  1.00 15.21 ? 148 ASP X CB  1 
ATOM   2467 C CG  . ASP B 1 148 ? 31.614 -0.271  12.202  1.00 19.44 ? 148 ASP X CG  1 
ATOM   2468 O OD1 . ASP B 1 148 ? 30.889 0.693   11.882  1.00 17.96 ? 148 ASP X OD1 1 
ATOM   2469 O OD2 . ASP B 1 148 ? 32.814 -0.124  12.518  1.00 19.56 ? 148 ASP X OD2 1 
ATOM   2470 N N   . GLN B 1 149 ? 28.423 -0.778  9.800   1.00 13.57 ? 149 GLN X N   1 
ATOM   2471 C CA  . GLN B 1 149 ? 28.215 -0.492  8.388   1.00 12.37 ? 149 GLN X CA  1 
ATOM   2472 C C   . GLN B 1 149 ? 27.585 0.882   8.278   1.00 14.71 ? 149 GLN X C   1 
ATOM   2473 O O   . GLN B 1 149 ? 26.782 1.269   9.127   1.00 18.24 ? 149 GLN X O   1 
ATOM   2474 C CB  . GLN B 1 149 ? 27.277 -1.542  7.789   1.00 17.86 ? 149 GLN X CB  1 
ATOM   2475 C CG  . GLN B 1 149 ? 27.885 -2.939  7.660   1.00 15.89 ? 149 GLN X CG  1 
ATOM   2476 C CD  . GLN B 1 149 ? 26.869 -3.925  7.160   1.00 14.41 ? 149 GLN X CD  1 
ATOM   2477 O OE1 . GLN B 1 149 ? 25.812 -3.516  6.702   1.00 17.20 ? 149 GLN X OE1 1 
ATOM   2478 N NE2 . GLN B 1 149 ? 27.177 -5.214  7.221   1.00 14.00 ? 149 GLN X NE2 1 
ATOM   2479 N N   . GLU B 1 150 ? 27.941 1.613   7.221   1.00 16.46 ? 150 GLU X N   1 
ATOM   2480 C CA  . GLU B 1 150 ? 27.303 2.900   6.968   1.00 16.73 ? 150 GLU X CA  1 
ATOM   2481 C C   . GLU B 1 150 ? 25.786 2.740   6.866   1.00 16.25 ? 150 GLU X C   1 
ATOM   2482 O O   . GLU B 1 150 ? 25.027 3.551   7.411   1.00 13.94 ? 150 GLU X O   1 
ATOM   2483 C CB  . GLU B 1 150 ? 27.856 3.498   5.667   1.00 17.97 ? 150 GLU X CB  1 
ATOM   2484 C CG  . GLU B 1 150 ? 27.234 4.841   5.275   1.00 17.17 ? 150 GLU X CG  1 
ATOM   2485 C CD  . GLU B 1 150 ? 27.771 5.388   3.966   1.00 15.28 ? 150 GLU X CD  1 
ATOM   2486 O OE1 . GLU B 1 150 ? 28.163 4.587   3.101   1.00 22.06 ? 150 GLU X OE1 1 
ATOM   2487 O OE2 . GLU B 1 150 ? 27.883 6.621   3.845   1.00 19.01 ? 150 GLU X OE2 1 
ATOM   2488 N N   . VAL B 1 151 ? 25.322 1.708   6.156   1.00 16.26 ? 151 VAL X N   1 
ATOM   2489 C CA  . VAL B 1 151 ? 23.901 1.350   6.126   1.00 14.42 ? 151 VAL X CA  1 
ATOM   2490 C C   . VAL B 1 151 ? 23.774 -0.163  6.158   1.00 15.83 ? 151 VAL X C   1 
ATOM   2491 O O   . VAL B 1 151 ? 24.197 -0.845  5.217   1.00 19.69 ? 151 VAL X O   1 
ATOM   2492 C CB  . VAL B 1 151 ? 23.146 1.895   4.902   1.00 16.28 ? 151 VAL X CB  1 
ATOM   2493 C CG1 . VAL B 1 151 ? 21.639 1.924   5.193   1.00 16.09 ? 151 VAL X CG1 1 
ATOM   2494 C CG2 . VAL B 1 151 ? 23.634 3.261   4.506   1.00 22.07 ? 151 VAL X CG2 1 
ATOM   2495 N N   . ALA B 1 152 ? 23.154 -0.686  7.204   1.00 30.00 ? 152 ALA X N   1 
ATOM   2496 C CA  . ALA B 1 152 ? 22.887 -2.108  7.287   1.00 30.00 ? 152 ALA X CA  1 
ATOM   2497 C C   . ALA B 1 152 ? 21.460 -2.371  6.834   1.00 30.00 ? 152 ALA X C   1 
ATOM   2498 O O   . ALA B 1 152 ? 20.576 -1.528  6.993   1.00 30.00 ? 152 ALA X O   1 
ATOM   2499 C CB  . ALA B 1 152 ? 23.075 -2.608  8.718   1.00 30.00 ? 152 ALA X CB  1 
ATOM   2500 N N   . VAL B 1 153 ? 21.249 -3.539  6.243   1.00 16.91 ? 153 VAL X N   1 
ATOM   2501 C CA  . VAL B 1 153 ? 19.916 -3.979  5.868   1.00 14.23 ? 153 VAL X CA  1 
ATOM   2502 C C   . VAL B 1 153 ? 19.724 -5.423  6.307   1.00 16.20 ? 153 VAL X C   1 
ATOM   2503 O O   . VAL B 1 153 ? 20.546 -6.292  5.994   1.00 15.58 ? 153 VAL X O   1 
ATOM   2504 C CB  . VAL B 1 153 ? 19.674 -3.844  4.353   1.00 12.74 ? 153 VAL X CB  1 
ATOM   2505 C CG1 . VAL B 1 153 ? 18.342 -4.463  3.963   1.00 20.99 ? 153 VAL X CG1 1 
ATOM   2506 C CG2 . VAL B 1 153 ? 19.721 -2.378  3.916   1.00 13.49 ? 153 VAL X CG2 1 
ATOM   2507 N N   . ASP B 1 154 ? 18.603 -5.681  6.984   1.00 14.52 ? 154 ASP X N   1 
ATOM   2508 C CA  . ASP B 1 154 ? 18.117 -7.029  7.265   1.00 14.08 ? 154 ASP X CA  1 
ATOM   2509 C C   . ASP B 1 154 ? 16.659 -7.039  6.824   1.00 17.12 ? 154 ASP X C   1 
ATOM   2510 O O   . ASP B 1 154 ? 15.792 -6.531  7.536   1.00 18.12 ? 154 ASP X O   1 
ATOM   2511 C CB  . ASP B 1 154 ? 18.232 -7.346  8.754   1.00 16.26 ? 154 ASP X CB  1 
ATOM   2512 C CG  . ASP B 1 154 ? 17.797 -8.764  9.083   1.00 18.78 ? 154 ASP X CG  1 
ATOM   2513 O OD1 . ASP B 1 154 ? 16.953 -9.333  8.360   1.00 24.21 ? 154 ASP X OD1 1 
ATOM   2514 O OD2 . ASP B 1 154 ? 18.263 -9.314  10.085  1.00 17.29 ? 154 ASP X OD2 1 
ATOM   2515 N N   . GLY B 1 155 ? 16.364 -7.650  5.688   1.00 16.80 ? 155 GLY X N   1 
ATOM   2516 C CA  . GLY B 1 155 ? 14.984 -7.578  5.175   1.00 16.13 ? 155 GLY X CA  1 
ATOM   2517 C C   . GLY B 1 155 ? 14.607 -6.138  4.903   1.00 13.68 ? 155 GLY X C   1 
ATOM   2518 O O   . GLY B 1 155 ? 15.179 -5.533  3.982   1.00 18.23 ? 155 GLY X O   1 
ATOM   2519 N N   . LYS B 1 156 ? 13.662 -5.617  5.685   1.00 15.74 ? 156 LYS X N   1 
ATOM   2520 C CA  . LYS B 1 156 ? 13.228 -4.209  5.528   1.00 16.02 ? 156 LYS X CA  1 
ATOM   2521 C C   . LYS B 1 156 ? 13.683 -3.383  6.735   1.00 16.71 ? 156 LYS X C   1 
ATOM   2522 O O   . LYS B 1 156 ? 13.192 -2.274  6.911   1.00 18.17 ? 156 LYS X O   1 
ATOM   2523 C CB  . LYS B 1 156 ? 11.731 -4.134  5.241   1.00 18.24 ? 156 LYS X CB  1 
ATOM   2524 C CG  . LYS B 1 156 ? 11.281 -4.966  4.049   1.00 21.48 ? 156 LYS X CG  1 
ATOM   2525 C CD  . LYS B 1 156 ? 10.012 -4.481  3.416   1.00 28.69 ? 156 LYS X CD  1 
ATOM   2526 C CE  . LYS B 1 156 ? 9.437  -5.506  2.467   1.00 20.49 ? 156 LYS X CE  1 
ATOM   2527 N NZ  . LYS B 1 156 ? 8.066  -5.909  2.847   1.00 24.78 ? 156 LYS X NZ  1 
ATOM   2528 N N   . LEU B 1 157 ? 14.567 -3.956  7.536   1.00 15.63 ? 157 LEU X N   1 
ATOM   2529 C CA  . LEU B 1 157 ? 15.154 -3.168  8.643   1.00 14.62 ? 157 LEU X CA  1 
ATOM   2530 C C   . LEU B 1 157 ? 16.389 -2.450  8.094   1.00 14.94 ? 157 LEU X C   1 
ATOM   2531 O O   . LEU B 1 157 ? 17.325 -3.121  7.703   1.00 18.35 ? 157 LEU X O   1 
ATOM   2532 C CB  . LEU B 1 157 ? 15.441 -4.077  9.842   1.00 17.33 ? 157 LEU X CB  1 
ATOM   2533 C CG  . LEU B 1 157 ? 16.139 -3.393  11.014  1.00 15.96 ? 157 LEU X CG  1 
ATOM   2534 C CD1 . LEU B 1 157 ? 15.261 -2.301  11.601  1.00 18.19 ? 157 LEU X CD1 1 
ATOM   2535 C CD2 . LEU B 1 157 ? 16.527 -4.410  12.070  1.00 20.06 ? 157 LEU X CD2 1 
ATOM   2536 N N   . VAL B 1 158 ? 16.326 -1.132  8.054   1.00 16.50 ? 158 VAL X N   1 
ATOM   2537 C CA  . VAL B 1 158 ? 17.417 -0.287  7.508   1.00 14.97 ? 158 VAL X CA  1 
ATOM   2538 C C   . VAL B 1 158 ? 18.027 0.512   8.663   1.00 13.72 ? 158 VAL X C   1 
ATOM   2539 O O   . VAL B 1 158 ? 17.316 1.225   9.318   1.00 15.14 ? 158 VAL X O   1 
ATOM   2540 C CB  . VAL B 1 158 ? 16.844 0.669   6.458   1.00 16.38 ? 158 VAL X CB  1 
ATOM   2541 C CG1 . VAL B 1 158 ? 17.931 1.519   5.825   1.00 17.80 ? 158 VAL X CG1 1 
ATOM   2542 C CG2 . VAL B 1 158 ? 16.058 -0.066  5.386   1.00 24.68 ? 158 VAL X CG2 1 
ATOM   2543 N N   . SER B 1 159 ? 19.331 0.360   8.842   1.00 16.06 ? 159 SER X N   1 
ATOM   2544 C CA  . SER B 1 159 ? 19.974 0.997   10.004  1.00 14.27 ? 159 SER X CA  1 
ATOM   2545 C C   . SER B 1 159 ? 21.241 1.762   9.633   1.00 16.02 ? 159 SER X C   1 
ATOM   2546 O O   . SER B 1 159 ? 21.984 1.287   8.802   1.00 14.46 ? 159 SER X O   1 
ATOM   2547 C CB  . SER B 1 159 ? 20.232 -0.007  11.073  1.00 16.90 ? 159 SER X CB  1 
ATOM   2548 O OG  . SER B 1 159 ? 21.069 -1.026  10.594  1.00 13.52 ? 159 SER X OG  1 
ATOM   2549 N N   . SER B 1 160 ? 21.485 2.859   10.350  1.00 15.03 ? 160 SER X N   1 
ATOM   2550 C CA  . SER B 1 160 ? 22.700 3.687   10.149  1.00 15.78 ? 160 SER X CA  1 
ATOM   2551 C C   . SER B 1 160 ? 23.243 4.122   11.521  1.00 15.06 ? 160 SER X C   1 
ATOM   2552 O O   . SER B 1 160 ? 22.521 3.970   12.500  1.00 16.49 ? 160 SER X O   1 
ATOM   2553 C CB  . SER B 1 160 ? 22.449 4.839   9.205   1.00 16.11 ? 160 SER X CB  1 
ATOM   2554 O OG  . SER B 1 160 ? 22.519 4.391   7.860   1.00 14.30 ? 160 SER X OG  1 
ATOM   2555 N N   . ARG B 1 161 ? 24.466 4.637   11.574  1.00 30.00 ? 161 ARG X N   1 
ATOM   2556 C CA  . ARG B 1 161 ? 25.117 4.874   12.894  1.00 30.00 ? 161 ARG X CA  1 
ATOM   2557 C C   . ARG B 1 161 ? 25.216 6.332   13.325  1.00 30.00 ? 161 ARG X C   1 
ATOM   2558 O O   . ARG B 1 161 ? 25.271 6.565   14.500  1.00 30.00 ? 161 ARG X O   1 
ATOM   2559 C CB  . ARG B 1 161 ? 26.566 4.382   12.809  1.00 30.00 ? 161 ARG X CB  1 
ATOM   2560 C CG  . ARG B 1 161 ? 26.781 3.132   11.975  1.00 30.00 ? 161 ARG X CG  1 
ATOM   2561 C CD  . ARG B 1 161 ? 28.234 2.954   11.582  1.00 30.00 ? 161 ARG X CD  1 
ATOM   2562 N NE  . ARG B 1 161 ? 28.534 3.839   10.471  1.00 30.00 ? 161 ARG X NE  1 
ATOM   2563 C CZ  . ARG B 1 161 ? 29.600 3.744   9.690   1.00 30.00 ? 161 ARG X CZ  1 
ATOM   2564 N NH1 . ARG B 1 161 ? 30.483 2.782   9.885   1.00 30.00 ? 161 ARG X NH1 1 
ATOM   2565 N NH2 . ARG B 1 161 ? 29.771 4.599   8.703   1.00 30.00 ? 161 ARG X NH2 1 
ATOM   2566 N N   . LYS B 1 162 ? 25.194 7.251   12.384  1.00 17.11 ? 162 LYS X N   1 
ATOM   2567 C CA  . LYS B 1 162 ? 25.492 8.650   12.729  1.00 22.25 ? 162 LYS X CA  1 
ATOM   2568 C C   . LYS B 1 162 ? 25.069 9.584   11.596  1.00 16.70 ? 162 LYS X C   1 
ATOM   2569 O O   . LYS B 1 162 ? 24.831 9.123   10.492  1.00 16.61 ? 162 LYS X O   1 
ATOM   2570 C CB  . LYS B 1 162 ? 27.017 8.736   12.890  1.00 16.06 ? 162 LYS X CB  1 
ATOM   2571 C CG  . LYS B 1 162 ? 27.832 8.331   11.674  1.00 16.24 ? 162 LYS X CG  1 
ATOM   2572 C CD  . LYS B 1 162 ? 29.302 8.187   11.950  1.00 20.26 ? 162 LYS X CD  1 
ATOM   2573 C CE  . LYS B 1 162 ? 30.068 7.780   10.712  1.00 20.31 ? 162 LYS X CE  1 
ATOM   2574 N NZ  . LYS B 1 162 ? 31.451 7.362   11.035  1.00 29.03 ? 162 LYS X NZ  1 
ATOM   2575 N N   . PRO B 1 163 ? 24.999 10.896  11.849  1.00 14.16 ? 163 PRO X N   1 
ATOM   2576 C CA  . PRO B 1 163 ? 24.580 11.854  10.837  1.00 16.24 ? 163 PRO X CA  1 
ATOM   2577 C C   . PRO B 1 163 ? 25.355 11.817  9.510   1.00 16.58 ? 163 PRO X C   1 
ATOM   2578 O O   . PRO B 1 163 ? 24.796 12.087  8.516   1.00 18.11 ? 163 PRO X O   1 
ATOM   2579 C CB  . PRO B 1 163 ? 24.765 13.197  11.556  1.00 18.77 ? 163 PRO X CB  1 
ATOM   2580 C CG  . PRO B 1 163 ? 24.492 12.876  12.994  1.00 23.98 ? 163 PRO X CG  1 
ATOM   2581 C CD  . PRO B 1 163 ? 25.143 11.526  13.169  1.00 26.98 ? 163 PRO X CD  1 
ATOM   2582 N N   . GLU B 1 164 ? 26.639 11.484  9.570   1.00 18.19 ? 164 GLU X N   1 
ATOM   2583 C CA  . GLU B 1 164 ? 27.379 11.411  8.316   1.00 17.56 ? 164 GLU X CA  1 
ATOM   2584 C C   . GLU B 1 164 ? 26.864 10.309  7.394   1.00 20.05 ? 164 GLU X C   1 
ATOM   2585 O O   . GLU B 1 164 ? 27.043 10.404  6.169   1.00 20.81 ? 164 GLU X O   1 
ATOM   2586 C CB  . GLU B 1 164 ? 28.884 11.316  8.601   1.00 25.39 ? 164 GLU X CB  1 
ATOM   2587 C CG  . GLU B 1 164 ? 29.389 12.478  9.473   1.00 26.04 ? 164 GLU X CG  1 
ATOM   2588 C CD  . GLU B 1 164 ? 29.437 12.169  10.977  1.00 32.96 ? 164 GLU X CD  1 
ATOM   2589 O OE1 . GLU B 1 164 ? 28.387 11.878  11.602  1.00 26.28 ? 164 GLU X OE1 1 
ATOM   2590 O OE2 . GLU B 1 164 ? 30.540 12.260  11.557  1.00 37.18 ? 164 GLU X OE2 1 
ATOM   2591 N N   . ASP B 1 165 ? 26.196 9.295   7.942   1.00 15.46 ? 165 ASP X N   1 
ATOM   2592 C CA  . ASP B 1 165 ? 25.673 8.205   7.139   1.00 15.87 ? 165 ASP X CA  1 
ATOM   2593 C C   . ASP B 1 165 ? 24.386 8.591   6.439   1.00 16.89 ? 165 ASP X C   1 
ATOM   2594 O O   . ASP B 1 165 ? 23.850 7.769   5.698   1.00 18.03 ? 165 ASP X O   1 
ATOM   2595 C CB  . ASP B 1 165 ? 25.332 6.985   8.010   1.00 15.37 ? 165 ASP X CB  1 
ATOM   2596 C CG  . ASP B 1 165 ? 26.537 6.410   8.749   1.00 19.53 ? 165 ASP X CG  1 
ATOM   2597 O OD1 . ASP B 1 165 ? 27.673 6.538   8.252   1.00 15.71 ? 165 ASP X OD1 1 
ATOM   2598 O OD2 . ASP B 1 165 ? 26.347 5.849   9.848   1.00 18.92 ? 165 ASP X OD2 1 
ATOM   2599 N N   . ILE B 1 166 ? 23.826 9.773   6.738   1.00 16.25 ? 166 ILE X N   1 
ATOM   2600 C CA  . ILE B 1 166 ? 22.454 10.076  6.294   1.00 15.66 ? 166 ILE X CA  1 
ATOM   2601 C C   . ILE B 1 166 ? 22.282 9.975   4.784   1.00 18.76 ? 166 ILE X C   1 
ATOM   2602 O O   . ILE B 1 166 ? 21.261 9.430   4.339   1.00 17.88 ? 166 ILE X O   1 
ATOM   2603 C CB  . ILE B 1 166 ? 21.969 11.403  6.894   1.00 18.50 ? 166 ILE X CB  1 
ATOM   2604 C CG1 . ILE B 1 166 ? 21.662 11.235  8.388   1.00 18.02 ? 166 ILE X CG1 1 
ATOM   2605 C CG2 . ILE B 1 166 ? 20.710 11.905  6.158   1.00 22.31 ? 166 ILE X CG2 1 
ATOM   2606 C CD1 . ILE B 1 166 ? 21.381 12.542  9.122   1.00 17.06 ? 166 ILE X CD1 1 
ATOM   2607 N N   . PRO B 1 167 ? 23.189 10.488  3.950   1.00 16.59 ? 167 PRO X N   1 
ATOM   2608 C CA  . PRO B 1 167 ? 22.977 10.372  2.491   1.00 17.15 ? 167 PRO X CA  1 
ATOM   2609 C C   . PRO B 1 167 ? 22.835 8.944   1.991   1.00 19.92 ? 167 PRO X C   1 
ATOM   2610 O O   . PRO B 1 167 ? 21.933 8.661   1.196   1.00 20.17 ? 167 PRO X O   1 
ATOM   2611 C CB  . PRO B 1 167 ? 24.199 11.088  1.917   1.00 23.06 ? 167 PRO X CB  1 
ATOM   2612 C CG  . PRO B 1 167 ? 24.511 12.121  2.942   1.00 22.93 ? 167 PRO X CG  1 
ATOM   2613 C CD  . PRO B 1 167 ? 24.338 11.369  4.245   1.00 21.26 ? 167 PRO X CD  1 
ATOM   2614 N N   . ALA B 1 168 ? 23.703 8.030   2.427   1.00 30.00 ? 168 ALA X N   1 
ATOM   2615 C CA  . ALA B 1 168 ? 23.564 6.626   2.042   1.00 30.00 ? 168 ALA X CA  1 
ATOM   2616 C C   . ALA B 1 168 ? 22.326 5.998   2.672   1.00 30.00 ? 168 ALA X C   1 
ATOM   2617 O O   . ALA B 1 168 ? 21.669 5.151   2.058   1.00 30.00 ? 168 ALA X O   1 
ATOM   2618 C CB  . ALA B 1 168 ? 24.815 5.856   2.460   1.00 30.00 ? 168 ALA X CB  1 
ATOM   2619 N N   . PHE B 1 169 ? 22.026 6.381   3.914   1.00 15.71 ? 169 PHE X N   1 
ATOM   2620 C CA  . PHE B 1 169 ? 20.814 5.929   4.591   1.00 13.70 ? 169 PHE X CA  1 
ATOM   2621 C C   . PHE B 1 169 ? 19.577 6.278   3.778   1.00 14.83 ? 169 PHE X C   1 
ATOM   2622 O O   . PHE B 1 169 ? 18.683 5.446   3.602   1.00 14.28 ? 169 PHE X O   1 
ATOM   2623 C CB  . PHE B 1 169 ? 20.773 6.624   5.951   1.00 15.50 ? 169 PHE X CB  1 
ATOM   2624 C CG  . PHE B 1 169 ? 19.584 6.299   6.813   1.00 14.45 ? 169 PHE X CG  1 
ATOM   2625 C CD1 . PHE B 1 169 ? 19.343 5.007   7.266   1.00 18.59 ? 169 PHE X CD1 1 
ATOM   2626 C CD2 . PHE B 1 169 ? 18.771 7.318   7.255   1.00 19.88 ? 169 PHE X CD2 1 
ATOM   2627 C CE1 . PHE B 1 169 ? 18.267 4.743   8.115   1.00 18.15 ? 169 PHE X CE1 1 
ATOM   2628 C CE2 . PHE B 1 169 ? 17.715 7.066   8.105   1.00 16.84 ? 169 PHE X CE2 1 
ATOM   2629 C CZ  . PHE B 1 169 ? 17.468 5.777   8.540   1.00 19.62 ? 169 PHE X CZ  1 
ATOM   2630 N N   . ASN B 1 170 ? 19.491 7.532   3.334   1.00 14.19 ? 170 ASN X N   1 
ATOM   2631 C CA  . ASN B 1 170 ? 18.360 8.003   2.551   1.00 13.62 ? 170 ASN X CA  1 
ATOM   2632 C C   . ASN B 1 170 ? 18.212 7.187   1.277   1.00 18.07 ? 170 ASN X C   1 
ATOM   2633 O O   . ASN B 1 170 ? 17.113 6.728   0.935   1.00 14.99 ? 170 ASN X O   1 
ATOM   2634 C CB  . ASN B 1 170 ? 18.602 9.466   2.182   1.00 18.05 ? 170 ASN X CB  1 
ATOM   2635 C CG  . ASN B 1 170 ? 18.519 10.401  3.370   1.00 19.07 ? 170 ASN X CG  1 
ATOM   2636 O OD1 . ASN B 1 170 ? 18.096 10.020  4.456   1.00 16.53 ? 170 ASN X OD1 1 
ATOM   2637 N ND2 . ASN B 1 170 ? 18.930 11.644  3.159   1.00 25.03 ? 170 ASN X ND2 1 
ATOM   2638 N N   . ARG B 1 171 ? 19.325 7.014   0.550   1.00 16.22 ? 171 ARG X N   1 
ATOM   2639 C CA  . ARG B 1 171 ? 19.298 6.259   -0.696  1.00 12.99 ? 171 ARG X CA  1 
ATOM   2640 C C   . ARG B 1 171 ? 18.833 4.825   -0.463  1.00 15.47 ? 171 ARG X C   1 
ATOM   2641 O O   . ARG B 1 171 ? 17.981 4.311   -1.196  1.00 14.97 ? 171 ARG X O   1 
ATOM   2642 C CB  . ARG B 1 171 ? 20.687 6.297   -1.326  1.00 17.24 ? 171 ARG X CB  1 
ATOM   2643 C CG  . ARG B 1 171 ? 20.984 7.615   -2.021  1.00 15.43 ? 171 ARG X CG  1 
ATOM   2644 C CD  . ARG B 1 171 ? 22.300 7.577   -2.801  1.00 20.46 ? 171 ARG X CD  1 
ATOM   2645 N NE  . ARG B 1 171 ? 23.450 7.241   -1.958  1.00 18.46 ? 171 ARG X NE  1 
ATOM   2646 C CZ  . ARG B 1 171 ? 24.264 8.127   -1.402  1.00 18.30 ? 171 ARG X CZ  1 
ATOM   2647 N NH1 . ARG B 1 171 ? 24.063 9.428   -1.535  1.00 26.71 ? 171 ARG X NH1 1 
ATOM   2648 N NH2 . ARG B 1 171 ? 25.316 7.696   -0.709  1.00 20.17 ? 171 ARG X NH2 1 
ATOM   2649 N N   . ARG B 1 172 ? 19.329 4.171   0.568   1.00 14.87 ? 172 ARG X N   1 
ATOM   2650 C CA  . ARG B 1 172 ? 18.934 2.768   0.826   1.00 15.65 ? 172 ARG X CA  1 
ATOM   2651 C C   . ARG B 1 172 ? 17.471 2.671   1.289   1.00 15.16 ? 172 ARG X C   1 
ATOM   2652 O O   . ARG B 1 172 ? 16.798 1.752   0.867   1.00 15.15 ? 172 ARG X O   1 
ATOM   2653 C CB  . ARG B 1 172 ? 19.865 2.181   1.878   1.00 11.53 ? 172 ARG X CB  1 
ATOM   2654 C CG  . ARG B 1 172 ? 19.893 0.662   1.918   1.00 14.83 ? 172 ARG X CG  1 
ATOM   2655 C CD  . ARG B 1 172 ? 20.676 0.085   0.753   1.00 13.63 ? 172 ARG X CD  1 
ATOM   2656 N NE  . ARG B 1 172 ? 20.610 -1.366  0.740   1.00 15.25 ? 172 ARG X NE  1 
ATOM   2657 C CZ  . ARG B 1 172 ? 19.675 -2.064  0.112   1.00 19.27 ? 172 ARG X CZ  1 
ATOM   2658 N NH1 . ARG B 1 172 ? 18.739 -1.437  -0.572  1.00 18.46 ? 172 ARG X NH1 1 
ATOM   2659 N NH2 . ARG B 1 172 ? 19.672 -3.382  0.177   1.00 19.89 ? 172 ARG X NH2 1 
ATOM   2660 N N   . PHE B 1 173 ? 17.038 3.587   2.145   1.00 14.16 ? 173 PHE X N   1 
ATOM   2661 C CA  . PHE B 1 173 ? 15.630 3.603   2.630   1.00 13.73 ? 173 PHE X CA  1 
ATOM   2662 C C   . PHE B 1 173 ? 14.693 3.769   1.429   1.00 16.21 ? 173 PHE X C   1 
ATOM   2663 O O   . PHE B 1 173 ? 13.720 3.062   1.331   1.00 16.21 ? 173 PHE X O   1 
ATOM   2664 C CB  . PHE B 1 173 ? 15.445 4.692   3.695   1.00 12.57 ? 173 PHE X CB  1 
ATOM   2665 C CG  . PHE B 1 173 ? 14.114 4.715   4.401   1.00 14.67 ? 173 PHE X CG  1 
ATOM   2666 C CD1 . PHE B 1 173 ? 13.321 3.585   4.483   1.00 12.80 ? 173 PHE X CD1 1 
ATOM   2667 C CD2 . PHE B 1 173 ? 13.666 5.875   5.009   1.00 17.27 ? 173 PHE X CD2 1 
ATOM   2668 C CE1 . PHE B 1 173 ? 12.099 3.619   5.132   1.00 17.87 ? 173 PHE X CE1 1 
ATOM   2669 C CE2 . PHE B 1 173 ? 12.447 5.905   5.666   1.00 18.35 ? 173 PHE X CE2 1 
ATOM   2670 C CZ  . PHE B 1 173 ? 11.666 4.780   5.722   1.00 19.05 ? 173 PHE X CZ  1 
ATOM   2671 N N   . ILE B 1 174 ? 15.041 4.678   0.541   1.00 13.77 ? 174 ILE X N   1 
ATOM   2672 C CA  . ILE B 1 174 ? 14.224 4.858   -0.689  1.00 12.79 ? 174 ILE X CA  1 
ATOM   2673 C C   . ILE B 1 174 ? 14.185 3.568   -1.522  1.00 17.95 ? 174 ILE X C   1 
ATOM   2674 O O   . ILE B 1 174 ? 13.101 3.191   -1.949  1.00 15.58 ? 174 ILE X O   1 
ATOM   2675 C CB  . ILE B 1 174 ? 14.760 6.074   -1.469  1.00 13.65 ? 174 ILE X CB  1 
ATOM   2676 C CG1 . ILE B 1 174 ? 14.418 7.387   -0.765  1.00 15.36 ? 174 ILE X CG1 1 
ATOM   2677 C CG2 . ILE B 1 174 ? 14.266 6.072   -2.903  1.00 15.40 ? 174 ILE X CG2 1 
ATOM   2678 C CD1 . ILE B 1 174 ? 15.210 8.571   -1.260  1.00 19.86 ? 174 ILE X CD1 1 
ATOM   2679 N N   . GLU B 1 175 ? 15.330 2.909   -1.729  1.00 15.53 ? 175 GLU X N   1 
ATOM   2680 C CA  . GLU B 1 175 ? 15.288 1.630   -2.441  1.00 15.35 ? 175 GLU X CA  1 
ATOM   2681 C C   . GLU B 1 175 ? 14.384 0.629   -1.742  1.00 15.79 ? 175 GLU X C   1 
ATOM   2682 O O   . GLU B 1 175 ? 13.576 -0.044  -2.387  1.00 17.72 ? 175 GLU X O   1 
ATOM   2683 C CB  . GLU B 1 175 ? 16.680 1.042   -2.645  1.00 18.86 ? 175 GLU X CB  1 
ATOM   2684 C CG  . GLU B 1 175 ? 17.650 1.952   -3.362  1.00 19.17 ? 175 GLU X CG  1 
ATOM   2685 C CD  . GLU B 1 175 ? 19.053 1.367   -3.358  1.00 20.06 ? 175 GLU X CD  1 
ATOM   2686 O OE1 . GLU B 1 175 ? 19.529 1.019   -2.254  1.00 19.23 ? 175 GLU X OE1 1 
ATOM   2687 O OE2 . GLU B 1 175 ? 19.670 1.246   -4.439  1.00 17.46 ? 175 GLU X OE2 1 
ATOM   2688 N N   . ILE B 1 176 ? 14.431 0.542   -0.413  1.00 13.10 ? 176 ILE X N   1 
ATOM   2689 C CA  . ILE B 1 176 ? 13.660 -0.503  0.334   1.00 14.81 ? 176 ILE X CA  1 
ATOM   2690 C C   . ILE B 1 176 ? 12.158 -0.178  0.349   1.00 14.86 ? 176 ILE X C   1 
ATOM   2691 O O   . ILE B 1 176 ? 11.360 -1.074  0.236   1.00 15.56 ? 176 ILE X O   1 
ATOM   2692 C CB  . ILE B 1 176 ? 14.266 -0.684  1.741   1.00 14.15 ? 176 ILE X CB  1 
ATOM   2693 C CG1 . ILE B 1 176 ? 15.700 -1.210  1.653   1.00 13.92 ? 176 ILE X CG1 1 
ATOM   2694 C CG2 . ILE B 1 176 ? 13.410 -1.581  2.613   1.00 16.54 ? 176 ILE X CG2 1 
ATOM   2695 C CD1 . ILE B 1 176 ? 15.787 -2.688  1.409   1.00 16.20 ? 176 ILE X CD1 1 
ATOM   2696 N N   . LEU B 1 177 ? 11.838 1.105   0.440   1.00 14.36 ? 177 LEU X N   1 
ATOM   2697 C CA  . LEU B 1 177 ? 10.417 1.524   0.468   1.00 14.19 ? 177 LEU X CA  1 
ATOM   2698 C C   . LEU B 1 177 ? 9.765  1.187   -0.871  1.00 19.94 ? 177 LEU X C   1 
ATOM   2699 O O   . LEU B 1 177 ? 8.624  0.775   -0.889  1.00 17.73 ? 177 LEU X O   1 
ATOM   2700 C CB  . LEU B 1 177 ? 10.382 3.020   0.795   1.00 19.53 ? 177 LEU X CB  1 
ATOM   2701 C CG  . LEU B 1 177 ? 9.028  3.622   1.156   1.00 25.64 ? 177 LEU X CG  1 
ATOM   2702 C CD1 . LEU B 1 177 ? 8.324  2.791   2.208   1.00 23.21 ? 177 LEU X CD1 1 
ATOM   2703 C CD2 . LEU B 1 177 ? 9.199  5.046   1.641   1.00 37.26 ? 177 LEU X CD2 1 
ATOM   2704 N N   . ALA B 1 178 ? 10.512 1.384   -1.948  1.00 30.00 ? 178 ALA X N   1 
ATOM   2705 C CA  . ALA B 1 178 ? 9.963  1.148   -3.295  1.00 30.00 ? 178 ALA X CA  1 
ATOM   2706 C C   . ALA B 1 178 ? 9.813  -0.346  -3.576  1.00 30.00 ? 178 ALA X C   1 
ATOM   2707 O O   . ALA B 1 178 ? 8.739  -0.693  -4.080  1.00 30.00 ? 178 ALA X O   1 
ATOM   2708 C CB  . ALA B 1 178 ? 10.861 1.821   -4.286  1.00 30.00 ? 178 ALA X CB  1 
ATOM   2709 N N   A GLY B 1 179 ? 10.705 -1.067  -3.177  0.53 30.00 ? 179 GLY X N   1 
ATOM   2710 N N   B GLY B 1 179 ? 10.698 -1.071  -3.167  0.47 30.00 ? 179 GLY X N   1 
ATOM   2711 C CA  A GLY B 1 179 ? 10.602 -2.500  -3.361  0.53 30.00 ? 179 GLY X CA  1 
ATOM   2712 C CA  B GLY B 1 179 ? 10.587 -2.506  -3.349  0.47 30.00 ? 179 GLY X CA  1 
ATOM   2713 C C   A GLY B 1 179 ? 10.890 -2.948  -4.781  0.53 30.00 ? 179 GLY X C   1 
ATOM   2714 C C   B GLY B 1 179 ? 10.871 -2.947  -4.773  0.47 30.00 ? 179 GLY X C   1 
ATOM   2715 O O   A GLY B 1 179 ? 10.753 -4.127  -5.094  0.53 30.00 ? 179 GLY X O   1 
ATOM   2716 O O   B GLY B 1 179 ? 11.334 -2.153  -5.588  0.47 30.00 ? 179 GLY X O   1 
HETATM 2717 O O   . HOH C 2 .   ? 18.130 28.385  31.569  1.00 25.52 ? 201 HOH B O   1 
HETATM 2718 O O   . HOH C 2 .   ? 27.057 -14.164 30.341  1.00 33.22 ? 202 HOH B O   1 
HETATM 2719 O O   . HOH C 2 .   ? 25.240 25.349  42.630  1.00 30.19 ? 203 HOH B O   1 
HETATM 2720 O O   . HOH C 2 .   ? 43.492 3.862   35.182  1.00 37.63 ? 204 HOH B O   1 
HETATM 2721 O O   . HOH C 2 .   ? 24.580 27.188  40.801  1.00 25.45 ? 205 HOH B O   1 
HETATM 2722 O O   . HOH C 2 .   ? 31.028 -5.844  56.770  1.00 30.03 ? 206 HOH B O   1 
HETATM 2723 O O   . HOH C 2 .   ? 28.710 -1.351  59.915  1.00 5.76  ? 207 HOH B O   1 
HETATM 2724 O O   . HOH C 2 .   ? 31.784 -3.549  26.382  1.00 33.61 ? 208 HOH B O   1 
HETATM 2725 O O   . HOH C 2 .   ? 31.845 19.281  51.863  1.00 32.27 ? 209 HOH B O   1 
HETATM 2726 O O   . HOH C 2 .   ? 25.122 15.205  54.955  1.00 27.98 ? 210 HOH B O   1 
HETATM 2727 O O   . HOH C 2 .   ? 18.747 -11.193 33.188  1.00 30.23 ? 211 HOH B O   1 
HETATM 2728 O O   . HOH C 2 .   ? 11.394 0.460   31.638  1.00 39.08 ? 212 HOH B O   1 
HETATM 2729 O O   . HOH C 2 .   ? 16.652 5.298   53.870  1.00 29.56 ? 213 HOH B O   1 
HETATM 2730 O O   . HOH C 2 .   ? 27.405 9.540   59.054  1.00 32.49 ? 214 HOH B O   1 
HETATM 2731 O O   . HOH C 2 .   ? 39.183 -0.005  50.460  1.00 23.09 ? 215 HOH B O   1 
HETATM 2732 O O   . HOH C 2 .   ? 36.472 20.147  29.716  1.00 24.26 ? 216 HOH B O   1 
HETATM 2733 O O   . HOH C 2 .   ? 20.618 9.873   34.746  1.00 22.07 ? 217 HOH B O   1 
HETATM 2734 O O   . HOH C 2 .   ? 22.690 14.161  30.778  1.00 25.08 ? 218 HOH B O   1 
HETATM 2735 O O   . HOH C 2 .   ? 14.849 9.276   52.246  1.00 33.17 ? 219 HOH B O   1 
HETATM 2736 O O   . HOH C 2 .   ? 30.130 0.782   60.613  1.00 18.72 ? 220 HOH B O   1 
HETATM 2737 O O   . HOH C 2 .   ? 23.621 18.860  45.829  1.00 27.89 ? 221 HOH B O   1 
HETATM 2738 O O   . HOH C 2 .   ? 40.328 -4.330  48.034  1.00 24.45 ? 222 HOH B O   1 
HETATM 2739 O O   . HOH C 2 .   ? 30.098 15.763  25.551  1.00 32.08 ? 223 HOH B O   1 
HETATM 2740 O O   . HOH C 2 .   ? 34.485 -3.621  26.995  1.00 33.96 ? 224 HOH B O   1 
HETATM 2741 O O   . HOH C 2 .   ? 19.030 4.131   52.537  1.00 17.90 ? 225 HOH B O   1 
HETATM 2742 O O   . HOH C 2 .   ? 29.871 -7.319  39.172  1.00 23.73 ? 226 HOH B O   1 
HETATM 2743 O O   . HOH C 2 .   ? 27.931 8.416   22.874  1.00 24.38 ? 227 HOH B O   1 
HETATM 2744 O O   . HOH C 2 .   ? 30.196 9.309   65.349  1.00 43.32 ? 228 HOH B O   1 
HETATM 2745 O O   . HOH C 2 .   ? 45.277 -1.642  41.426  1.00 37.39 ? 229 HOH B O   1 
HETATM 2746 O O   . HOH C 2 .   ? 14.479 2.647   50.594  1.00 22.75 ? 230 HOH B O   1 
HETATM 2747 O O   . HOH C 2 .   ? 43.016 7.855   53.736  1.00 25.36 ? 231 HOH B O   1 
HETATM 2748 O O   . HOH C 2 .   ? 20.077 22.576  26.896  1.00 25.45 ? 232 HOH B O   1 
HETATM 2749 O O   . HOH C 2 .   ? 21.968 3.256   36.519  1.00 15.38 ? 233 HOH B O   1 
HETATM 2750 O O   . HOH C 2 .   ? 39.745 10.820  53.073  1.00 24.06 ? 234 HOH B O   1 
HETATM 2751 O O   . HOH C 2 .   ? 45.614 11.889  31.293  1.00 28.52 ? 235 HOH B O   1 
HETATM 2752 O O   . HOH C 2 .   ? 17.604 14.272  34.413  1.00 30.28 ? 236 HOH B O   1 
HETATM 2753 O O   . HOH C 2 .   ? 25.480 -10.828 43.181  1.00 30.07 ? 237 HOH B O   1 
HETATM 2754 O O   . HOH C 2 .   ? 37.222 18.597  42.020  1.00 29.01 ? 238 HOH B O   1 
HETATM 2755 O O   . HOH C 2 .   ? 38.350 -9.042  46.344  1.00 28.11 ? 239 HOH B O   1 
HETATM 2756 O O   . HOH C 2 .   ? 14.423 -0.529  29.036  1.00 19.40 ? 240 HOH B O   1 
HETATM 2757 O O   . HOH C 2 .   ? 20.857 14.911  32.707  1.00 20.41 ? 241 HOH B O   1 
HETATM 2758 O O   . HOH C 2 .   ? 38.012 16.713  45.230  1.00 28.64 ? 242 HOH B O   1 
HETATM 2759 O O   . HOH C 2 .   ? 43.799 -1.940  43.020  1.00 31.77 ? 243 HOH B O   1 
HETATM 2760 O O   . HOH C 2 .   ? 23.791 15.885  50.167  1.00 20.77 ? 244 HOH B O   1 
HETATM 2761 O O   . HOH C 2 .   ? 12.624 8.431   46.212  1.00 26.44 ? 245 HOH B O   1 
HETATM 2762 O O   . HOH C 2 .   ? 21.108 18.003  38.613  1.00 20.40 ? 246 HOH B O   1 
HETATM 2763 O O   . HOH C 2 .   ? 30.073 -3.192  53.484  1.00 27.29 ? 247 HOH B O   1 
HETATM 2764 O O   . HOH C 2 .   ? 24.141 4.326   26.293  1.00 14.51 ? 248 HOH B O   1 
HETATM 2765 O O   . HOH C 2 .   ? 45.149 12.918  35.489  1.00 23.17 ? 249 HOH B O   1 
HETATM 2766 O O   . HOH C 2 .   ? 20.942 -8.344  46.306  1.00 29.58 ? 250 HOH B O   1 
HETATM 2767 O O   . HOH C 2 .   ? 39.133 11.541  55.711  1.00 26.52 ? 251 HOH B O   1 
HETATM 2768 O O   . HOH C 2 .   ? 42.794 1.250   36.014  1.00 34.57 ? 252 HOH B O   1 
HETATM 2769 O O   . HOH C 2 .   ? 37.535 10.741  25.767  1.00 36.41 ? 253 HOH B O   1 
HETATM 2770 O O   . HOH C 2 .   ? 36.216 15.751  49.128  1.00 21.86 ? 254 HOH B O   1 
HETATM 2771 O O   . HOH C 2 .   ? 19.407 11.836  35.992  1.00 23.80 ? 255 HOH B O   1 
HETATM 2772 O O   . HOH C 2 .   ? 36.327 16.125  31.292  1.00 28.56 ? 256 HOH B O   1 
HETATM 2773 O O   . HOH C 2 .   ? 42.313 18.424  35.674  1.00 25.28 ? 257 HOH B O   1 
HETATM 2774 O O   . HOH C 2 .   ? 21.345 -11.069 41.645  1.00 36.13 ? 258 HOH B O   1 
HETATM 2775 O O   . HOH C 2 .   ? 12.740 11.793  38.817  1.00 29.64 ? 259 HOH B O   1 
HETATM 2776 O O   . HOH C 2 .   ? 11.346 5.151   50.674  1.00 34.26 ? 260 HOH B O   1 
HETATM 2777 O O   . HOH C 2 .   ? 34.030 -7.957  33.369  1.00 29.43 ? 261 HOH B O   1 
HETATM 2778 O O   . HOH C 2 .   ? 43.431 9.431   40.631  1.00 24.02 ? 262 HOH B O   1 
HETATM 2779 O O   . HOH C 2 .   ? 35.081 17.920  29.879  1.00 30.31 ? 263 HOH B O   1 
HETATM 2780 O O   . HOH C 2 .   ? 29.101 8.228   35.471  1.00 14.37 ? 264 HOH B O   1 
HETATM 2781 O O   . HOH C 2 .   ? 36.499 -0.257  50.114  1.00 20.53 ? 265 HOH B O   1 
HETATM 2782 O O   . HOH C 2 .   ? 31.217 19.255  47.929  1.00 30.18 ? 266 HOH B O   1 
HETATM 2783 O O   . HOH C 2 .   ? 26.637 -8.579  30.524  1.00 26.57 ? 267 HOH B O   1 
HETATM 2784 O O   . HOH C 2 .   ? 21.521 2.595   39.121  1.00 16.35 ? 268 HOH B O   1 
HETATM 2785 O O   . HOH C 2 .   ? 13.398 -6.289  30.984  1.00 26.25 ? 269 HOH B O   1 
HETATM 2786 O O   . HOH C 2 .   ? 29.911 5.878   24.143  1.00 23.50 ? 270 HOH B O   1 
HETATM 2787 O O   . HOH C 2 .   ? 31.364 18.564  54.405  1.00 31.29 ? 271 HOH B O   1 
HETATM 2788 O O   . HOH C 2 .   ? 26.170 -5.798  51.637  1.00 24.63 ? 272 HOH B O   1 
HETATM 2789 O O   . HOH C 2 .   ? 6.950  -1.064  41.434  1.00 23.19 ? 273 HOH B O   1 
HETATM 2790 O O   . HOH C 2 .   ? 27.517 -6.227  28.167  1.00 25.49 ? 274 HOH B O   1 
HETATM 2791 O O   . HOH C 2 .   ? 24.650 -12.749 42.498  1.00 34.50 ? 275 HOH B O   1 
HETATM 2792 O O   . HOH C 2 .   ? 36.324 13.516  59.655  1.00 38.12 ? 276 HOH B O   1 
HETATM 2793 O O   . HOH C 2 .   ? 48.736 7.319   32.378  1.00 37.08 ? 277 HOH B O   1 
HETATM 2794 O O   . HOH C 2 .   ? 46.779 0.208   39.636  1.00 39.59 ? 278 HOH B O   1 
HETATM 2795 O O   . HOH C 2 .   ? 35.380 1.141   52.097  1.00 22.34 ? 279 HOH B O   1 
HETATM 2796 O O   . HOH C 2 .   ? 29.970 -6.368  45.491  1.00 24.09 ? 280 HOH B O   1 
HETATM 2797 O O   . HOH C 2 .   ? 32.530 7.874   24.456  1.00 21.99 ? 281 HOH B O   1 
HETATM 2798 O O   . HOH C 2 .   ? 29.895 27.514  39.635  1.00 39.50 ? 282 HOH B O   1 
HETATM 2799 O O   . HOH C 2 .   ? 22.508 -2.944  43.371  1.00 16.76 ? 283 HOH B O   1 
HETATM 2800 O O   . HOH C 2 .   ? 8.518  2.352   42.355  1.00 19.96 ? 284 HOH B O   1 
HETATM 2801 O O   . HOH C 2 .   ? 21.897 20.801  40.562  1.00 27.40 ? 285 HOH B O   1 
HETATM 2802 O O   . HOH C 2 .   ? 19.582 -4.589  25.655  1.00 17.79 ? 286 HOH B O   1 
HETATM 2803 O O   . HOH C 2 .   ? 8.442  -1.872  39.031  1.00 35.32 ? 287 HOH B O   1 
HETATM 2804 O O   . HOH C 2 .   ? 10.389 -4.340  30.000  1.00 25.81 ? 288 HOH B O   1 
HETATM 2805 O O   . HOH C 2 .   ? 27.001 2.711   58.734  1.00 18.59 ? 289 HOH B O   1 
HETATM 2806 O O   . HOH C 2 .   ? 33.258 -1.442  52.504  1.00 27.69 ? 290 HOH B O   1 
HETATM 2807 O O   . HOH C 2 .   ? 28.513 5.553   34.379  1.00 13.46 ? 291 HOH B O   1 
HETATM 2808 O O   . HOH C 2 .   ? 10.295 -3.566  27.102  1.00 21.47 ? 292 HOH B O   1 
HETATM 2809 O O   . HOH C 2 .   ? 34.006 14.936  29.308  1.00 23.26 ? 293 HOH B O   1 
HETATM 2810 O O   . HOH C 2 .   ? 43.311 0.774   38.843  1.00 30.00 ? 294 HOH B O   1 
HETATM 2811 O O   . HOH C 2 .   ? 15.409 9.252   49.170  1.00 20.92 ? 295 HOH B O   1 
HETATM 2812 O O   . HOH C 2 .   ? 27.113 4.722   32.094  1.00 15.84 ? 296 HOH B O   1 
HETATM 2813 O O   . HOH C 2 .   ? 32.630 26.156  39.053  1.00 37.75 ? 297 HOH B O   1 
HETATM 2814 O O   . HOH C 2 .   ? 25.132 6.757   61.076  1.00 31.19 ? 298 HOH B O   1 
HETATM 2815 O O   . HOH C 2 .   ? 34.997 11.775  60.370  1.00 29.07 ? 299 HOH B O   1 
HETATM 2816 O O   . HOH C 2 .   ? 35.805 -0.407  55.845  1.00 16.49 ? 300 HOH B O   1 
HETATM 2817 O O   . HOH C 2 .   ? 25.750 10.909  24.944  1.00 21.82 ? 301 HOH B O   1 
HETATM 2818 O O   . HOH C 2 .   ? 24.108 20.740  42.478  1.00 20.38 ? 302 HOH B O   1 
HETATM 2819 O O   . HOH C 2 .   ? 13.291 -7.192  35.888  1.00 22.26 ? 303 HOH B O   1 
HETATM 2820 O O   . HOH C 2 .   ? 13.827 7.151   51.927  1.00 22.61 ? 304 HOH B O   1 
HETATM 2821 O O   . HOH C 2 .   ? 40.938 4.190   53.152  1.00 22.24 ? 305 HOH B O   1 
HETATM 2822 O O   . HOH C 2 .   ? 26.147 12.506  55.508  1.00 23.67 ? 306 HOH B O   1 
HETATM 2823 O O   . HOH C 2 .   ? 18.344 -4.378  47.942  1.00 22.59 ? 307 HOH B O   1 
HETATM 2824 O O   . HOH C 2 .   ? 35.042 22.046  41.339  1.00 24.73 ? 308 HOH B O   1 
HETATM 2825 O O   . HOH C 2 .   ? 19.799 11.523  54.766  1.00 33.76 ? 309 HOH B O   1 
HETATM 2826 O O   . HOH C 2 .   ? 29.055 13.210  22.695  1.00 29.78 ? 310 HOH B O   1 
HETATM 2827 O O   . HOH C 2 .   ? 38.535 2.930   25.191  1.00 37.85 ? 311 HOH B O   1 
HETATM 2828 O O   . HOH C 2 .   ? 31.328 -4.297  44.763  1.00 27.27 ? 312 HOH B O   1 
HETATM 2829 O O   . HOH C 2 .   ? 35.310 -2.548  50.301  1.00 31.10 ? 313 HOH B O   1 
HETATM 2830 O O   . HOH C 2 .   ? 23.262 24.481  39.018  1.00 27.64 ? 314 HOH B O   1 
HETATM 2831 O O   . HOH C 2 .   ? 27.965 0.413   58.300  1.00 16.17 ? 315 HOH B O   1 
HETATM 2832 O O   . HOH C 2 .   ? 34.553 0.461   23.717  1.00 35.67 ? 316 HOH B O   1 
HETATM 2833 O O   . HOH C 2 .   ? 45.240 7.409   41.243  1.00 30.84 ? 317 HOH B O   1 
HETATM 2834 O O   . HOH C 2 .   ? 19.800 0.319   54.557  1.00 27.16 ? 318 HOH B O   1 
HETATM 2835 O O   . HOH C 2 .   ? 14.491 -7.906  28.561  1.00 35.20 ? 319 HOH B O   1 
HETATM 2836 O O   . HOH C 2 .   ? 32.966 -7.220  44.244  1.00 29.27 ? 320 HOH B O   1 
HETATM 2837 O O   . HOH C 2 .   ? 24.107 6.036   56.866  1.00 20.78 ? 321 HOH B O   1 
HETATM 2838 O O   . HOH C 2 .   ? 19.967 2.513   54.549  1.00 23.24 ? 322 HOH B O   1 
HETATM 2839 O O   . HOH C 2 .   ? 23.626 -8.408  49.133  1.00 23.71 ? 323 HOH B O   1 
HETATM 2840 O O   . HOH C 2 .   ? 41.292 9.376   30.520  1.00 23.29 ? 324 HOH B O   1 
HETATM 2841 O O   . HOH C 2 .   ? 48.719 3.295   46.147  1.00 25.15 ? 325 HOH B O   1 
HETATM 2842 O O   . HOH C 2 .   ? 13.969 13.167  48.115  1.00 34.11 ? 326 HOH B O   1 
HETATM 2843 O O   . HOH C 2 .   ? 43.203 15.779  29.091  1.00 29.84 ? 327 HOH B O   1 
HETATM 2844 O O   . HOH C 2 .   ? 28.897 18.707  46.779  1.00 24.18 ? 328 HOH B O   1 
HETATM 2845 O O   . HOH C 2 .   ? 43.584 9.073   47.217  1.00 26.22 ? 329 HOH B O   1 
HETATM 2846 O O   . HOH C 2 .   ? 19.310 12.458  32.010  1.00 20.39 ? 330 HOH B O   1 
HETATM 2847 O O   . HOH C 2 .   ? 11.761 15.930  29.997  1.00 33.67 ? 331 HOH B O   1 
HETATM 2848 O O   . HOH C 2 .   ? 15.439 11.476  53.576  1.00 30.45 ? 332 HOH B O   1 
HETATM 2849 O O   . HOH C 2 .   ? 27.496 -6.641  32.250  1.00 20.26 ? 333 HOH B O   1 
HETATM 2850 O O   . HOH C 2 .   ? 28.390 19.920  28.127  1.00 21.94 ? 334 HOH B O   1 
HETATM 2851 O O   . HOH C 2 .   ? 10.653 3.342   39.176  1.00 31.45 ? 335 HOH B O   1 
HETATM 2852 O O   . HOH C 2 .   ? 16.130 20.913  31.530  1.00 26.73 ? 336 HOH B O   1 
HETATM 2853 O O   . HOH C 2 .   ? 24.417 -4.927  53.698  1.00 25.08 ? 337 HOH B O   1 
HETATM 2854 O O   . HOH C 2 .   ? 43.668 10.100  38.085  1.00 22.60 ? 338 HOH B O   1 
HETATM 2855 O O   . HOH C 2 .   ? 38.563 21.365  30.432  1.00 34.59 ? 339 HOH B O   1 
HETATM 2856 O O   . HOH C 2 .   ? 44.595 8.722   26.450  1.00 27.97 ? 340 HOH B O   1 
HETATM 2857 O O   . HOH C 2 .   ? 39.385 5.151   27.943  1.00 24.83 ? 341 HOH B O   1 
HETATM 2858 O O   . HOH C 2 .   ? 32.588 20.514  44.381  1.00 33.63 ? 342 HOH B O   1 
HETATM 2859 O O   . HOH C 2 .   ? 17.063 12.420  30.514  1.00 20.22 ? 343 HOH B O   1 
HETATM 2860 O O   . HOH C 2 .   ? 30.590 26.940  36.859  1.00 29.11 ? 344 HOH B O   1 
HETATM 2861 O O   . HOH C 2 .   ? 16.267 -10.672 35.244  1.00 32.23 ? 345 HOH B O   1 
HETATM 2862 O O   . HOH C 2 .   ? 22.598 3.743   59.779  1.00 25.73 ? 346 HOH B O   1 
HETATM 2863 O O   . HOH C 2 .   ? 31.964 5.587   63.211  1.00 10.97 ? 347 HOH B O   1 
HETATM 2864 O O   . HOH C 2 .   ? 48.664 3.621   42.772  1.00 31.45 ? 348 HOH B O   1 
HETATM 2865 O O   . HOH C 2 .   ? 45.795 3.015   33.452  1.00 38.82 ? 349 HOH B O   1 
HETATM 2866 O O   . HOH C 2 .   ? 27.816 -2.805  57.783  1.00 25.75 ? 350 HOH B O   1 
HETATM 2867 O O   . HOH C 2 .   ? 38.773 -1.150  53.108  1.00 23.54 ? 351 HOH B O   1 
HETATM 2868 O O   . HOH C 2 .   ? 29.269 4.201   63.371  1.00 30.58 ? 352 HOH B O   1 
HETATM 2869 O O   . HOH C 2 .   ? 15.537 27.787  31.176  1.00 38.53 ? 353 HOH B O   1 
HETATM 2870 O O   . HOH C 2 .   ? 21.507 14.866  49.353  1.00 27.81 ? 354 HOH B O   1 
HETATM 2871 O O   . HOH C 2 .   ? 31.048 -5.108  42.039  1.00 26.10 ? 355 HOH B O   1 
HETATM 2872 O O   . HOH C 2 .   ? 22.421 -10.286 47.264  1.00 38.23 ? 356 HOH B O   1 
HETATM 2873 O O   . HOH C 2 .   ? 10.984 5.591   39.226  1.00 33.36 ? 357 HOH B O   1 
HETATM 2874 O O   . HOH C 2 .   ? 32.598 4.545   21.227  1.00 35.76 ? 358 HOH B O   1 
HETATM 2875 O O   . HOH C 2 .   ? 21.987 12.281  53.108  1.00 36.56 ? 359 HOH B O   1 
HETATM 2876 O O   . HOH C 2 .   ? 11.790 0.459   29.090  1.00 37.07 ? 360 HOH B O   1 
HETATM 2877 O O   . HOH C 2 .   ? 35.111 19.788  43.485  1.00 40.99 ? 361 HOH B O   1 
HETATM 2878 O O   . HOH C 2 .   ? 42.355 10.264  53.374  1.00 31.00 ? 362 HOH B O   1 
HETATM 2879 O O   . HOH C 2 .   ? 30.186 -7.327  28.236  1.00 35.37 ? 363 HOH B O   1 
HETATM 2880 O O   . HOH C 2 .   ? 42.080 -7.926  45.521  1.00 26.37 ? 364 HOH B O   1 
HETATM 2881 O O   . HOH C 2 .   ? 26.959 12.127  57.887  1.00 32.35 ? 365 HOH B O   1 
HETATM 2882 O O   . HOH C 2 .   ? 46.155 -4.082  45.564  1.00 24.48 ? 366 HOH B O   1 
HETATM 2883 O O   . HOH C 2 .   ? 26.164 -8.289  51.386  1.00 32.81 ? 367 HOH B O   1 
HETATM 2884 O O   . HOH C 2 .   ? 45.643 11.929  38.203  1.00 27.37 ? 368 HOH B O   1 
HETATM 2885 O O   . HOH C 2 .   ? 17.260 11.811  34.277  1.00 32.27 ? 369 HOH B O   1 
HETATM 2886 O O   . HOH C 2 .   ? 18.652 18.866  40.003  1.00 33.26 ? 370 HOH B O   1 
HETATM 2887 O O   . HOH C 2 .   ? 23.492 15.120  52.887  1.00 22.85 ? 371 HOH B O   1 
HETATM 2888 O O   . HOH C 2 .   ? 44.507 15.819  35.570  1.00 32.77 ? 372 HOH B O   1 
HETATM 2889 O O   . HOH C 2 .   ? 21.525 5.773   57.842  1.00 21.64 ? 373 HOH B O   1 
HETATM 2890 O O   . HOH C 2 .   ? 24.853 8.309   58.346  1.00 37.36 ? 374 HOH B O   1 
HETATM 2891 O O   . HOH C 2 .   ? 39.396 7.772   29.017  1.00 26.80 ? 375 HOH B O   1 
HETATM 2892 O O   . HOH C 2 .   ? 25.253 4.900   58.908  1.00 20.76 ? 376 HOH B O   1 
HETATM 2893 O O   . HOH C 2 .   ? 44.786 7.185   23.954  1.00 23.41 ? 377 HOH B O   1 
HETATM 2894 O O   . HOH C 2 .   ? 33.883 -4.887  24.875  1.00 30.26 ? 378 HOH B O   1 
HETATM 2895 O O   . HOH C 2 .   ? 10.357 7.089   37.106  1.00 37.00 ? 379 HOH B O   1 
HETATM 2896 O O   . HOH C 2 .   ? 24.072 11.112  55.961  1.00 32.93 ? 380 HOH B O   1 
HETATM 2897 O O   . HOH C 2 .   ? 29.040 -9.417  51.009  1.00 38.50 ? 381 HOH B O   1 
HETATM 2898 O O   . HOH D 2 .   ? 5.821  19.633  22.940  1.00 19.99 ? 201 HOH X O   1 
HETATM 2899 O O   . HOH D 2 .   ? 13.215 -1.736  -6.863  1.00 4.80  ? 202 HOH X O   1 
HETATM 2900 O O   . HOH D 2 .   ? 13.531 13.060  29.592  1.00 33.86 ? 203 HOH X O   1 
HETATM 2901 O O   . HOH D 2 .   ? 14.750 2.126   -6.246  1.00 28.74 ? 204 HOH X O   1 
HETATM 2902 O O   . HOH D 2 .   ? 3.098  -0.382  2.022   1.00 26.85 ? 205 HOH X O   1 
HETATM 2903 O O   . HOH D 2 .   ? -7.192 -1.379  11.162  1.00 26.61 ? 206 HOH X O   1 
HETATM 2904 O O   . HOH D 2 .   ? 21.344 9.530   18.114  1.00 21.44 ? 207 HOH X O   1 
HETATM 2905 O O   . HOH D 2 .   ? 2.988  11.352  -2.525  1.00 26.22 ? 208 HOH X O   1 
HETATM 2906 O O   . HOH D 2 .   ? -0.587 18.046  17.109  1.00 28.83 ? 209 HOH X O   1 
HETATM 2907 O O   . HOH D 2 .   ? -3.343 13.133  13.185  1.00 33.47 ? 210 HOH X O   1 
HETATM 2908 O O   . HOH D 2 .   ? 16.745 14.576  -2.343  1.00 25.06 ? 211 HOH X O   1 
HETATM 2909 O O   . HOH D 2 .   ? 9.728  8.115   28.251  1.00 35.21 ? 212 HOH X O   1 
HETATM 2910 O O   . HOH D 2 .   ? -3.894 2.458   3.980   1.00 24.54 ? 213 HOH X O   1 
HETATM 2911 O O   . HOH D 2 .   ? 13.149 7.832   17.297  1.00 17.33 ? 214 HOH X O   1 
HETATM 2912 O O   . HOH D 2 .   ? 24.476 14.139  6.953   1.00 26.75 ? 215 HOH X O   1 
HETATM 2913 O O   . HOH D 2 .   ? 31.751 -3.888  23.877  1.00 35.78 ? 216 HOH X O   1 
HETATM 2914 O O   . HOH D 2 .   ? 21.528 14.858  20.096  1.00 24.83 ? 217 HOH X O   1 
HETATM 2915 O O   . HOH D 2 .   ? 31.274 2.619   13.594  1.00 32.29 ? 218 HOH X O   1 
HETATM 2916 O O   . HOH D 2 .   ? 11.918 0.219   -7.524  1.00 17.29 ? 219 HOH X O   1 
HETATM 2917 O O   . HOH D 2 .   ? 5.862  15.387  -0.466  1.00 34.55 ? 220 HOH X O   1 
HETATM 2918 O O   . HOH D 2 .   ? 8.897  -7.554  9.039   1.00 27.23 ? 221 HOH X O   1 
HETATM 2919 O O   . HOH D 2 .   ? 9.621  24.970  12.952  1.00 39.31 ? 222 HOH X O   1 
HETATM 2920 O O   . HOH D 2 .   ? 18.459 24.184  13.474  1.00 35.33 ? 223 HOH X O   1 
HETATM 2921 O O   . HOH D 2 .   ? 22.722 11.788  16.684  1.00 20.53 ? 224 HOH X O   1 
HETATM 2922 O O   . HOH D 2 .   ? 20.208 2.817   16.435  1.00 18.25 ? 225 HOH X O   1 
HETATM 2923 O O   . HOH D 2 .   ? 22.181 11.057  -2.422  1.00 36.21 ? 226 HOH X O   1 
HETATM 2924 O O   . HOH D 2 .   ? 15.612 -9.056  23.118  1.00 29.81 ? 227 HOH X O   1 
HETATM 2925 O O   . HOH D 2 .   ? 11.913 -3.653  -0.011  1.00 27.00 ? 228 HOH X O   1 
HETATM 2926 O O   . HOH D 2 .   ? 17.444 -11.874 7.714   1.00 27.73 ? 229 HOH X O   1 
HETATM 2927 O O   . HOH D 2 .   ? 27.335 2.173   2.314   1.00 17.85 ? 230 HOH X O   1 
HETATM 2928 O O   . HOH D 2 .   ? 16.372 10.607  28.225  1.00 21.48 ? 231 HOH X O   1 
HETATM 2929 O O   . HOH D 2 .   ? 2.350  10.218  -0.059  1.00 22.30 ? 232 HOH X O   1 
HETATM 2930 O O   . HOH D 2 .   ? 26.408 8.860   3.771   1.00 19.28 ? 233 HOH X O   1 
HETATM 2931 O O   . HOH D 2 .   ? 5.862  15.254  3.418   1.00 29.56 ? 234 HOH X O   1 
HETATM 2932 O O   . HOH D 2 .   ? 15.507 12.106  -2.790  1.00 24.74 ? 235 HOH X O   1 
HETATM 2933 O O   . HOH D 2 .   ? 17.714 5.617   -3.550  1.00 22.75 ? 236 HOH X O   1 
HETATM 2934 O O   . HOH D 2 .   ? 29.938 -7.350  13.624  1.00 21.69 ? 237 HOH X O   1 
HETATM 2935 O O   . HOH D 2 .   ? 20.838 17.695  14.144  1.00 21.85 ? 238 HOH X O   1 
HETATM 2936 O O   . HOH D 2 .   ? 1.144  3.719   -0.013  1.00 18.15 ? 239 HOH X O   1 
HETATM 2937 O O   . HOH D 2 .   ? 30.859 0.406   21.984  1.00 31.35 ? 240 HOH X O   1 
HETATM 2938 O O   . HOH D 2 .   ? 20.930 -8.699  7.198   1.00 25.12 ? 241 HOH X O   1 
HETATM 2939 O O   . HOH D 2 .   ? 17.797 20.191  10.443  1.00 26.96 ? 242 HOH X O   1 
HETATM 2940 O O   . HOH D 2 .   ? 17.871 4.161   26.733  1.00 15.68 ? 243 HOH X O   1 
HETATM 2941 O O   . HOH D 2 .   ? 10.183 -10.207 9.512   1.00 39.85 ? 244 HOH X O   1 
HETATM 2942 O O   . HOH D 2 .   ? 13.764 8.214   29.902  1.00 17.05 ? 245 HOH X O   1 
HETATM 2943 O O   . HOH D 2 .   ? 14.918 4.427   20.906  1.00 17.88 ? 246 HOH X O   1 
HETATM 2944 O O   . HOH D 2 .   ? 22.319 23.010  25.281  1.00 33.13 ? 247 HOH X O   1 
HETATM 2945 O O   . HOH D 2 .   ? 28.817 -7.387  17.046  1.00 24.45 ? 248 HOH X O   1 
HETATM 2946 O O   . HOH D 2 .   ? 22.739 -4.540  27.479  1.00 14.82 ? 249 HOH X O   1 
HETATM 2947 O O   . HOH D 2 .   ? 24.733 14.611  17.362  1.00 26.13 ? 250 HOH X O   1 
HETATM 2948 O O   . HOH D 2 .   ? 5.152  10.347  27.127  1.00 33.88 ? 251 HOH X O   1 
HETATM 2949 O O   . HOH D 2 .   ? 32.910 -2.136  17.527  1.00 36.63 ? 252 HOH X O   1 
HETATM 2950 O O   . HOH D 2 .   ? 30.253 15.698  22.201  1.00 38.56 ? 253 HOH X O   1 
HETATM 2951 O O   . HOH D 2 .   ? 10.580 -5.967  -3.058  1.00 32.71 ? 254 HOH X O   1 
HETATM 2952 O O   . HOH D 2 .   ? 13.612 5.221   18.640  1.00 18.93 ? 255 HOH X O   1 
HETATM 2953 O O   . HOH D 2 .   ? 8.223  14.452  23.950  1.00 25.42 ? 256 HOH X O   1 
HETATM 2954 O O   . HOH D 2 .   ? 2.092  1.832   -1.541  1.00 26.64 ? 257 HOH X O   1 
HETATM 2955 O O   . HOH D 2 .   ? 19.607 -3.286  9.810   1.00 14.89 ? 258 HOH X O   1 
HETATM 2956 O O   . HOH D 2 .   ? 14.151 -0.177  -5.080  1.00 20.68 ? 259 HOH X O   1 
HETATM 2957 O O   . HOH D 2 .   ? 20.613 2.212   13.843  1.00 16.67 ? 260 HOH X O   1 
HETATM 2958 O O   . HOH D 2 .   ? 27.974 -0.586  23.540  1.00 25.05 ? 261 HOH X O   1 
HETATM 2959 O O   . HOH D 2 .   ? 21.766 -0.520  -2.772  1.00 26.50 ? 262 HOH X O   1 
HETATM 2960 O O   . HOH D 2 .   ? 20.571 -13.933 18.250  1.00 24.26 ? 263 HOH X O   1 
HETATM 2961 O O   . HOH D 2 .   ? 11.600 26.291  16.172  1.00 30.88 ? 264 HOH X O   1 
HETATM 2962 O O   . HOH D 2 .   ? 23.728 -4.807  5.396   1.00 17.30 ? 265 HOH X O   1 
HETATM 2963 O O   . HOH D 2 .   ? 29.179 7.705   6.228   1.00 23.58 ? 266 HOH X O   1 
HETATM 2964 O O   . HOH D 2 .   ? 27.876 12.616  4.704   1.00 39.63 ? 267 HOH X O   1 
HETATM 2965 O O   . HOH D 2 .   ? 23.002 3.573   0.188   1.00 19.29 ? 268 HOH X O   1 
HETATM 2966 O O   . HOH D 2 .   ? -6.502 3.217   9.221   1.00 26.22 ? 269 HOH X O   1 
HETATM 2967 O O   . HOH D 2 .   ? 19.390 14.097  22.393  1.00 17.02 ? 270 HOH X O   1 
HETATM 2968 O O   . HOH D 2 .   ? -1.326 8.885   12.666  1.00 27.02 ? 271 HOH X O   1 
HETATM 2969 O O   . HOH D 2 .   ? 18.609 18.205  6.856   1.00 28.38 ? 272 HOH X O   1 
HETATM 2970 O O   . HOH D 2 .   ? -1.601 3.263   18.217  1.00 29.48 ? 273 HOH X O   1 
HETATM 2971 O O   . HOH D 2 .   ? 12.283 5.509   28.948  1.00 23.39 ? 274 HOH X O   1 
HETATM 2972 O O   . HOH D 2 .   ? 25.943 11.475  -1.164  1.00 34.39 ? 275 HOH X O   1 
HETATM 2973 O O   . HOH D 2 .   ? 22.007 2.308   -1.997  1.00 22.74 ? 276 HOH X O   1 
HETATM 2974 O O   . HOH D 2 .   ? 28.046 -8.013  26.233  1.00 27.28 ? 277 HOH X O   1 
HETATM 2975 O O   . HOH D 2 .   ? -3.163 6.900   11.664  1.00 24.60 ? 278 HOH X O   1 
HETATM 2976 O O   . HOH D 2 .   ? 6.376  0.589   0.791   1.00 17.20 ? 279 HOH X O   1 
HETATM 2977 O O   . HOH D 2 .   ? 18.242 -8.800  3.931   1.00 24.89 ? 280 HOH X O   1 
HETATM 2978 O O   . HOH D 2 .   ? 5.581  -1.091  3.074   1.00 19.82 ? 281 HOH X O   1 
HETATM 2979 O O   . HOH D 2 .   ? 14.550 -6.288  25.440  1.00 27.98 ? 282 HOH X O   1 
HETATM 2980 O O   . HOH D 2 .   ? 6.276  -0.899  -2.698  1.00 17.90 ? 283 HOH X O   1 
HETATM 2981 O O   . HOH D 2 .   ? -1.720 9.808   15.151  1.00 25.39 ? 284 HOH X O   1 
HETATM 2982 O O   . HOH D 2 .   ? 17.100 -3.138  -2.146  1.00 24.70 ? 285 HOH X O   1 
HETATM 2983 O O   . HOH D 2 .   ? 12.012 15.859  27.179  1.00 28.58 ? 286 HOH X O   1 
HETATM 2984 O O   . HOH D 2 .   ? 20.882 -11.836 11.705  1.00 30.76 ? 287 HOH X O   1 
HETATM 2985 O O   . HOH D 2 .   ? 0.468  4.855   3.392   1.00 20.31 ? 288 HOH X O   1 
HETATM 2986 O O   . HOH D 2 .   ? 22.900 -1.587  2.782   1.00 17.02 ? 289 HOH X O   1 
HETATM 2987 O O   . HOH D 2 .   ? 0.903  8.991   22.502  1.00 26.01 ? 290 HOH X O   1 
HETATM 2988 O O   . HOH D 2 .   ? 31.453 5.044   12.717  1.00 31.40 ? 291 HOH X O   1 
HETATM 2989 O O   . HOH D 2 .   ? -1.250 7.332   -0.318  1.00 25.49 ? 292 HOH X O   1 
HETATM 2990 O O   . HOH D 2 .   ? 8.744  -2.074  0.875   1.00 24.76 ? 293 HOH X O   1 
HETATM 2991 O O   . HOH D 2 .   ? 16.085 -6.520  1.436   1.00 28.47 ? 294 HOH X O   1 
HETATM 2992 O O   . HOH D 2 .   ? 25.166 4.872   -1.246  1.00 23.67 ? 295 HOH X O   1 
HETATM 2993 O O   . HOH D 2 .   ? 1.476  -4.565  5.041   1.00 23.94 ? 296 HOH X O   1 
HETATM 2994 O O   . HOH D 2 .   ? 28.774 -6.303  22.451  1.00 19.75 ? 297 HOH X O   1 
HETATM 2995 O O   . HOH D 2 .   ? 8.019  -7.867  19.235  1.00 33.63 ? 298 HOH X O   1 
HETATM 2996 O O   . HOH D 2 .   ? 25.100 12.320  22.944  1.00 30.88 ? 299 HOH X O   1 
HETATM 2997 O O   . HOH D 2 .   ? 12.131 -7.085  7.665   1.00 23.58 ? 300 HOH X O   1 
HETATM 2998 O O   . HOH D 2 .   ? -3.346 12.359  16.899  1.00 25.69 ? 301 HOH X O   1 
HETATM 2999 O O   . HOH D 2 .   ? 14.750 9.112   -5.442  1.00 30.61 ? 302 HOH X O   1 
HETATM 3000 O O   . HOH D 2 .   ? 10.618 19.033  0.657   1.00 33.49 ? 303 HOH X O   1 
HETATM 3001 O O   . HOH D 2 .   ? 19.538 3.885   -5.659  1.00 31.69 ? 304 HOH X O   1 
HETATM 3002 O O   . HOH D 2 .   ? 2.779  4.895   24.851  1.00 26.95 ? 305 HOH X O   1 
HETATM 3003 O O   . HOH D 2 .   ? 15.267 26.770  9.839   1.00 38.48 ? 306 HOH X O   1 
HETATM 3004 O O   . HOH D 2 .   ? 33.603 1.922   10.521  1.00 23.00 ? 307 HOH X O   1 
HETATM 3005 O O   . HOH D 2 .   ? 13.469 18.575  5.692   1.00 31.24 ? 308 HOH X O   1 
HETATM 3006 O O   . HOH D 2 .   ? -0.770 11.445  4.974   1.00 35.09 ? 309 HOH X O   1 
HETATM 3007 O O   . HOH D 2 .   ? 3.531  20.612  22.429  1.00 31.80 ? 310 HOH X O   1 
HETATM 3008 O O   . HOH D 2 .   ? 8.967  15.063  -6.342  1.00 46.56 ? 311 HOH X O   1 
HETATM 3009 O O   . HOH D 2 .   ? 20.026 20.585  11.577  1.00 29.33 ? 312 HOH X O   1 
HETATM 3010 O O   . HOH D 2 .   ? 14.933 -7.132  21.040  1.00 19.53 ? 313 HOH X O   1 
HETATM 3011 O O   . HOH D 2 .   ? 14.300 -2.941  -2.530  1.00 19.91 ? 314 HOH X O   1 
HETATM 3012 O O   . HOH D 2 .   ? 22.627 12.519  20.888  1.00 24.48 ? 315 HOH X O   1 
HETATM 3013 O O   . HOH D 2 .   ? 8.067  20.368  22.879  1.00 28.69 ? 316 HOH X O   1 
HETATM 3014 O O   . HOH D 2 .   ? 19.979 12.069  0.362   1.00 26.10 ? 317 HOH X O   1 
HETATM 3015 O O   . HOH D 2 .   ? 16.831 6.389   -7.502  1.00 27.50 ? 318 HOH X O   1 
HETATM 3016 O O   . HOH D 2 .   ? 18.085 15.300  2.091   1.00 30.00 ? 319 HOH X O   1 
HETATM 3017 O O   . HOH D 2 .   ? -0.087 2.460   4.125   1.00 25.80 ? 320 HOH X O   1 
HETATM 3018 O O   . HOH D 2 .   ? 16.348 24.497  9.212   1.00 43.68 ? 321 HOH X O   1 
HETATM 3019 O O   . HOH D 2 .   ? 13.715 19.769  24.473  1.00 26.12 ? 322 HOH X O   1 
HETATM 3020 O O   . HOH D 2 .   ? -1.602 8.452   4.874   1.00 29.17 ? 323 HOH X O   1 
HETATM 3021 O O   . HOH D 2 .   ? -7.002 7.030   22.631  1.00 37.44 ? 324 HOH X O   1 
HETATM 3022 O O   . HOH D 2 .   ? 14.270 10.334  29.402  1.00 36.95 ? 325 HOH X O   1 
HETATM 3023 O O   . HOH D 2 .   ? 9.969  5.174   -10.180 1.00 13.41 ? 326 HOH X O   1 
HETATM 3024 O O   . HOH D 2 .   ? 22.727 -11.860 26.139  1.00 42.80 ? 327 HOH X O   1 
HETATM 3025 O O   . HOH D 2 .   ? -1.418 15.299  23.987  1.00 32.88 ? 328 HOH X O   1 
HETATM 3026 O O   . HOH D 2 .   ? 9.554  -8.283  6.431   1.00 28.51 ? 329 HOH X O   1 
HETATM 3027 O O   . HOH D 2 .   ? 9.206  15.790  26.922  1.00 30.79 ? 330 HOH X O   1 
HETATM 3028 O O   . HOH D 2 .   ? 33.527 -1.956  15.035  1.00 32.98 ? 331 HOH X O   1 
HETATM 3029 O O   . HOH D 2 .   ? 31.543 -5.609  15.415  1.00 29.65 ? 332 HOH X O   1 
HETATM 3030 O O   . HOH D 2 .   ? 0.133  -2.004  9.205   1.00 27.34 ? 333 HOH X O   1 
HETATM 3031 O O   . HOH D 2 .   ? 26.411 20.697  20.994  1.00 30.00 ? 334 HOH X O   1 
HETATM 3032 O O   . HOH D 2 .   ? 27.008 9.444   1.430   1.00 29.42 ? 335 HOH X O   1 
HETATM 3033 O O   . HOH D 2 .   ? 6.978  -2.877  2.067   1.00 28.83 ? 336 HOH X O   1 
HETATM 3034 O O   . HOH D 2 .   ? 11.000 -4.336  9.734   1.00 33.10 ? 337 HOH X O   1 
HETATM 3035 O O   . HOH D 2 .   ? 11.447 6.010   30.949  1.00 30.95 ? 338 HOH X O   1 
HETATM 3036 O O   . HOH D 2 .   ? 23.336 18.495  13.855  1.00 42.73 ? 339 HOH X O   1 
HETATM 3037 O O   . HOH D 2 .   ? 33.532 4.547   9.917   1.00 32.66 ? 340 HOH X O   1 
HETATM 3038 O O   . HOH D 2 .   ? 14.574 12.178  -5.382  1.00 30.42 ? 341 HOH X O   1 
HETATM 3039 O O   . HOH D 2 .   ? -1.342 9.693   7.317   1.00 32.42 ? 342 HOH X O   1 
HETATM 3040 O O   . HOH D 2 .   ? 14.796 3.527   -10.055 1.00 31.88 ? 343 HOH X O   1 
HETATM 3041 O O   . HOH D 2 .   ? 11.238 -4.946  12.768  1.00 32.34 ? 344 HOH X O   1 
HETATM 3042 O O   . HOH D 2 .   ? 16.340 -10.126 2.914   1.00 39.73 ? 345 HOH X O   1 
HETATM 3043 O O   . HOH D 2 .   ? 31.949 6.609   14.791  1.00 37.86 ? 346 HOH X O   1 
HETATM 3044 O O   . HOH D 2 .   ? 24.951 12.102  17.892  1.00 27.36 ? 347 HOH X O   1 
HETATM 3045 O O   . HOH D 2 .   ? -7.169 2.944   21.457  1.00 43.85 ? 348 HOH X O   1 
HETATM 3046 O O   . HOH D 2 .   ? -0.344 9.885   0.313   1.00 32.43 ? 349 HOH X O   1 
HETATM 3047 O O   . HOH D 2 .   ? 27.642 11.155  21.933  1.00 30.89 ? 350 HOH X O   1 
HETATM 3048 O O   . HOH D 2 .   ? 13.283 -5.838  0.486   1.00 34.16 ? 351 HOH X O   1 
HETATM 3049 O O   . HOH D 2 .   ? 25.696 11.155  20.157  1.00 30.18 ? 352 HOH X O   1 
HETATM 3050 O O   . HOH D 2 .   ? 17.975 20.619  6.173   1.00 32.98 ? 353 HOH X O   1 
HETATM 3051 O O   . HOH D 2 .   ? 33.704 -4.562  14.778  1.00 45.34 ? 354 HOH X O   1 
HETATM 3052 O O   . HOH D 2 .   ? 3.792  -2.233  0.413   1.00 29.03 ? 355 HOH X O   1 
HETATM 3053 O O   . HOH D 2 .   ? 30.297 9.004   22.891  1.00 31.35 ? 356 HOH X O   1 
HETATM 3054 O O   . HOH D 2 .   ? 17.103 4.663   -9.987  1.00 31.19 ? 357 HOH X O   1 
HETATM 3055 O O   . HOH D 2 .   ? 4.022  16.486  2.983   1.00 39.21 ? 358 HOH X O   1 
HETATM 3056 O O   . HOH D 2 .   ? 12.543 4.063   -11.544 1.00 25.73 ? 359 HOH X O   1 
HETATM 3057 O O   . HOH D 2 .   ? 35.572 -3.520  12.953  1.00 32.40 ? 360 HOH X O   1 
HETATM 3058 O O   . HOH D 2 .   ? 18.172 10.704  -1.568  1.00 26.23 ? 361 HOH X O   1 
HETATM 3059 O O   . HOH D 2 .   ? 18.466 14.716  -4.364  1.00 31.55 ? 362 HOH X O   1 
HETATM 3060 O O   . HOH D 2 .   ? 27.254 12.623  15.887  1.00 34.23 ? 363 HOH X O   1 
HETATM 3061 O O   . HOH D 2 .   ? 32.977 1.411   21.211  1.00 37.46 ? 364 HOH X O   1 
HETATM 3062 O O   . HOH D 2 .   ? 23.791 24.967  25.416  1.00 35.98 ? 365 HOH X O   1 
HETATM 3063 O O   . HOH D 2 .   ? 4.346  19.345  25.265  1.00 37.97 ? 366 HOH X O   1 
HETATM 3064 O O   . HOH D 2 .   ? 17.408 8.161   -4.083  1.00 33.16 ? 367 HOH X O   1 
# 
