data_7HOZ
# 
_entry.id   7HOZ 
# 
_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   7HOZ         pdb_00007hoz 10.2210/pdb7hoz/pdb 
WWPDB D_1001407749 ?            ?                   
# 
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 2025-02-26 ? 
2 'Structure model' 1 1 2025-05-28 ? 
# 
_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               'Structure summary' 
# 
_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            pdbx_deposit_group 
# 
_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                '_pdbx_deposit_group.group_description' 
# 
_pdbx_database_status.entry_id                        7HOZ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-07 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frankfurt.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ni, X.'              1  
'Marples, P.G.'       2  
'Godoy, A.S.'         3  
'Koekemoer, L.'       4  
'Aschenbrenner, J.C.' 5  
'Balcomb, B.H.'       6  
'Fairhead, M.'        7  
'Lithgo, R.M.'        8  
'Lee, A.'             9  
'Kenton, N.'          10 
'Thompson, W.'        11 
'Tomlinson, C.W.E.'   12 
'Wild, C.'            13 
'Winokan, M.'         14 
'Williams, E.P.'      15 
'Chandran, A.V.'      16 
'Walsh, M.A.'         17 
'Fearon, D.'          18 
'von Delft, F.'       19 
# 
_citation.id                        primary 
_citation.title                     'PanDDA analysis group deposition' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Ni, X.'              ? 1  
primary 'Marples, P.G.'       ? 2  
primary 'Godoy, A.S.'         ? 3  
primary 'Koekemoer, L.'       ? 4  
primary 'Aschenbrenner, J.C.' ? 5  
primary 'Balcomb, B.H.'       ? 6  
primary 'Fairhead, M.'        ? 7  
primary 'Lithgo, R.M.'        ? 8  
primary 'Lee, A.'             ? 9  
primary 'Kenton, N.'          ? 10 
primary 'Thompson, W.'        ? 11 
primary 'Tomlinson, C.W.E.'   ? 12 
primary 'Wild, C.'            ? 13 
primary 'Winokan, M.'         ? 14 
primary 'Williams, E.P.'      ? 15 
primary 'Chandran, A.V.'      ? 16 
primary 'Walsh, M.A.'         ? 17 
primary 'Fearon, D.'          ? 18 
primary 'von Delft, F.'       ? 19 
# 
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 'Serine protease subunit NS2B'                        5067.486  1   ?                           ?    ? ? 
2 polymer     man 'Serine protease NS3'                                 18117.629 1   3.4.21.91,3.6.1.15,3.6.4.13 None ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                  78.133    3   ?                           ?    ? ? 
4 non-polymer syn 'N-(1-methyl-1H-pyrazol-4-yl)quinoline-5-carboxamide' 252.271   1   ?                           ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                         96.063    2   ?                           ?    ? ? 
6 water       nat water                                                 18.015    100 ?                           ?    ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Flavivirin protease NS2B regulatory subunit,Non-structural protein 2B' 
2 'Flavivirin protease NS3 catalytic subunit,Non-structural protein 3'    
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE SMGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE A ? 
2 'polypeptide(L)' no no 
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
;MKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAW
DGLSEVQLLAVPPGERAKNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGK
REEETPVE
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'DIMETHYL SULFOXIDE'                                  DMS   
4 'N-(1-methyl-1H-pyrazol-4-yl)quinoline-5-carboxamide' A1BGI 
5 'SULFATE ION'                                         SO4   
6 water                                                 HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   GLY n 
1 4   LYS n 
1 5   SER n 
1 6   VAL n 
1 7   ASP n 
1 8   MET n 
1 9   TYR n 
1 10  ILE n 
1 11  GLU n 
1 12  ARG n 
1 13  ALA n 
1 14  GLY n 
1 15  ASP n 
1 16  ILE n 
1 17  THR n 
1 18  TRP n 
1 19  GLU n 
1 20  LYS n 
1 21  ASP n 
1 22  ALA n 
1 23  GLU n 
1 24  VAL n 
1 25  THR n 
1 26  GLY n 
1 27  ASN n 
1 28  SER n 
1 29  PRO n 
1 30  ARG n 
1 31  LEU n 
1 32  ASP n 
1 33  VAL n 
1 34  ALA n 
1 35  LEU n 
1 36  ASP n 
1 37  GLU n 
1 38  SER n 
1 39  GLY n 
1 40  ASP n 
1 41  PHE n 
1 42  SER n 
1 43  LEU n 
1 44  VAL n 
1 45  GLU n 
1 46  GLU n 
2 1   MET n 
2 2   LYS n 
2 3   GLU n 
2 4   VAL n 
2 5   LYS n 
2 6   LYS n 
2 7   GLY n 
2 8   GLU n 
2 9   THR n 
2 10  THR n 
2 11  ASP n 
2 12  GLY n 
2 13  VAL n 
2 14  TYR n 
2 15  ARG n 
2 16  VAL n 
2 17  MET n 
2 18  THR n 
2 19  ARG n 
2 20  ARG n 
2 21  LEU n 
2 22  LEU n 
2 23  GLY n 
2 24  SER n 
2 25  THR n 
2 26  GLN n 
2 27  VAL n 
2 28  GLY n 
2 29  VAL n 
2 30  GLY n 
2 31  VAL n 
2 32  MET n 
2 33  GLN n 
2 34  GLU n 
2 35  GLY n 
2 36  VAL n 
2 37  PHE n 
2 38  HIS n 
2 39  THR n 
2 40  MET n 
2 41  TRP n 
2 42  HIS n 
2 43  VAL n 
2 44  THR n 
2 45  LYS n 
2 46  GLY n 
2 47  ALA n 
2 48  ALA n 
2 49  LEU n 
2 50  ARG n 
2 51  SER n 
2 52  GLY n 
2 53  GLU n 
2 54  GLY n 
2 55  ARG n 
2 56  LEU n 
2 57  ASP n 
2 58  PRO n 
2 59  TYR n 
2 60  TRP n 
2 61  GLY n 
2 62  ASP n 
2 63  VAL n 
2 64  LYS n 
2 65  GLN n 
2 66  ASP n 
2 67  LEU n 
2 68  VAL n 
2 69  SER n 
2 70  TYR n 
2 71  CYS n 
2 72  GLY n 
2 73  PRO n 
2 74  TRP n 
2 75  LYS n 
2 76  LEU n 
2 77  ASP n 
2 78  ALA n 
2 79  ALA n 
2 80  TRP n 
2 81  ASP n 
2 82  GLY n 
2 83  LEU n 
2 84  SER n 
2 85  GLU n 
2 86  VAL n 
2 87  GLN n 
2 88  LEU n 
2 89  LEU n 
2 90  ALA n 
2 91  VAL n 
2 92  PRO n 
2 93  PRO n 
2 94  GLY n 
2 95  GLU n 
2 96  ARG n 
2 97  ALA n 
2 98  LYS n 
2 99  ASN n 
2 100 ILE n 
2 101 GLN n 
2 102 THR n 
2 103 LEU n 
2 104 PRO n 
2 105 GLY n 
2 106 ILE n 
2 107 PHE n 
2 108 LYS n 
2 109 THR n 
2 110 LYS n 
2 111 ASP n 
2 112 GLY n 
2 113 ASP n 
2 114 ILE n 
2 115 GLY n 
2 116 ALA n 
2 117 VAL n 
2 118 ALA n 
2 119 LEU n 
2 120 ASP n 
2 121 TYR n 
2 122 PRO n 
2 123 ALA n 
2 124 GLY n 
2 125 THR n 
2 126 SER n 
2 127 GLY n 
2 128 SER n 
2 129 PRO n 
2 130 ILE n 
2 131 LEU n 
2 132 ASP n 
2 133 LYS n 
2 134 CYS n 
2 135 GLY n 
2 136 ARG n 
2 137 VAL n 
2 138 ILE n 
2 139 GLY n 
2 140 LEU n 
2 141 TYR n 
2 142 GLY n 
2 143 ASN n 
2 144 GLY n 
2 145 VAL n 
2 146 VAL n 
2 147 ILE n 
2 148 LYS n 
2 149 ASN n 
2 150 GLY n 
2 151 SER n 
2 152 TYR n 
2 153 VAL n 
2 154 SER n 
2 155 ALA n 
2 156 ILE n 
2 157 THR n 
2 158 GLN n 
2 159 GLY n 
2 160 LYS n 
2 161 ARG n 
2 162 GLU n 
2 163 GLU n 
2 164 GLU n 
2 165 THR n 
2 166 PRO n 
2 167 VAL n 
2 168 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 46  ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 168 ? ? ? ? ? ? ? ? ? 'Zika virus' 64320 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? 
? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1BGI non-polymer         . 'N-(1-methyl-1H-pyrazol-4-yl)quinoline-5-carboxamide' ? 'C14 H12 N4 O'   252.271 
ALA   'L-peptide linking' y ALANINE                                               ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                              ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                            ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                       ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                              ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                  ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                             ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                       ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                               ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                             ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                 ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                            ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                               ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                            ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                         ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                               ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                         ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                             ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                            ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                              ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   44  ?   ?   ?   A . n 
A 1 2   MET 2   45  ?   ?   ?   A . n 
A 1 3   GLY 3   46  ?   ?   ?   A . n 
A 1 4   LYS 4   47  ?   ?   ?   A . n 
A 1 5   SER 5   48  ?   ?   ?   A . n 
A 1 6   VAL 6   49  ?   ?   ?   A . n 
A 1 7   ASP 7   50  50  ASP ASP A . n 
A 1 8   MET 8   51  51  MET MET A . n 
A 1 9   TYR 9   52  52  TYR TYR A . n 
A 1 10  ILE 10  53  53  ILE ILE A . n 
A 1 11  GLU 11  54  54  GLU GLU A . n 
A 1 12  ARG 12  55  55  ARG ARG A . n 
A 1 13  ALA 13  56  56  ALA ALA A . n 
A 1 14  GLY 14  57  57  GLY GLY A . n 
A 1 15  ASP 15  58  58  ASP ASP A . n 
A 1 16  ILE 16  59  59  ILE ILE A . n 
A 1 17  THR 17  60  60  THR THR A . n 
A 1 18  TRP 18  61  61  TRP TRP A . n 
A 1 19  GLU 19  62  62  GLU GLU A . n 
A 1 20  LYS 20  63  63  LYS LYS A . n 
A 1 21  ASP 21  64  64  ASP ASP A . n 
A 1 22  ALA 22  65  65  ALA ALA A . n 
A 1 23  GLU 23  66  66  GLU GLU A . n 
A 1 24  VAL 24  67  67  VAL VAL A . n 
A 1 25  THR 25  68  68  THR THR A . n 
A 1 26  GLY 26  69  69  GLY GLY A . n 
A 1 27  ASN 27  70  70  ASN ASN A . n 
A 1 28  SER 28  71  71  SER SER A . n 
A 1 29  PRO 29  72  72  PRO PRO A . n 
A 1 30  ARG 30  73  73  ARG ARG A . n 
A 1 31  LEU 31  74  74  LEU LEU A . n 
A 1 32  ASP 32  75  75  ASP ASP A . n 
A 1 33  VAL 33  76  76  VAL VAL A . n 
A 1 34  ALA 34  77  77  ALA ALA A . n 
A 1 35  LEU 35  78  78  LEU LEU A . n 
A 1 36  ASP 36  79  79  ASP ASP A . n 
A 1 37  GLU 37  80  80  GLU GLU A . n 
A 1 38  SER 38  81  81  SER SER A . n 
A 1 39  GLY 39  82  82  GLY GLY A . n 
A 1 40  ASP 40  83  83  ASP ASP A . n 
A 1 41  PHE 41  84  84  PHE PHE A . n 
A 1 42  SER 42  85  85  SER SER A . n 
A 1 43  LEU 43  86  86  LEU LEU A . n 
A 1 44  VAL 44  87  87  VAL VAL A . n 
A 1 45  GLU 45  88  88  GLU GLU A . n 
A 1 46  GLU 46  89  ?   ?   ?   A . n 
B 2 1   MET 1   10  ?   ?   ?   B . n 
B 2 2   LYS 2   11  ?   ?   ?   B . n 
B 2 3   GLU 3   12  ?   ?   ?   B . n 
B 2 4   VAL 4   13  ?   ?   ?   B . n 
B 2 5   LYS 5   14  ?   ?   ?   B . n 
B 2 6   LYS 6   15  ?   ?   ?   B . n 
B 2 7   GLY 7   16  16  GLY GLY B . n 
B 2 8   GLU 8   17  17  GLU GLU B . n 
B 2 9   THR 9   18  18  THR THR B . n 
B 2 10  THR 10  19  19  THR THR B . n 
B 2 11  ASP 11  20  20  ASP ASP B . n 
B 2 12  GLY 12  21  21  GLY GLY B . n 
B 2 13  VAL 13  22  22  VAL VAL B . n 
B 2 14  TYR 14  23  23  TYR TYR B . n 
B 2 15  ARG 15  24  24  ARG ARG B . n 
B 2 16  VAL 16  25  25  VAL VAL B . n 
B 2 17  MET 17  26  26  MET MET B . n 
B 2 18  THR 18  27  27  THR THR B . n 
B 2 19  ARG 19  28  28  ARG ARG B . n 
B 2 20  ARG 20  29  29  ARG ARG B . n 
B 2 21  LEU 21  30  30  LEU LEU B . n 
B 2 22  LEU 22  31  31  LEU LEU B . n 
B 2 23  GLY 23  32  32  GLY GLY B . n 
B 2 24  SER 24  33  33  SER SER B . n 
B 2 25  THR 25  34  34  THR THR B . n 
B 2 26  GLN 26  35  35  GLN GLN B . n 
B 2 27  VAL 27  36  36  VAL VAL B . n 
B 2 28  GLY 28  37  37  GLY GLY B . n 
B 2 29  VAL 29  38  38  VAL VAL B . n 
B 2 30  GLY 30  39  39  GLY GLY B . n 
B 2 31  VAL 31  40  40  VAL VAL B . n 
B 2 32  MET 32  41  41  MET MET B . n 
B 2 33  GLN 33  42  42  GLN GLN B . n 
B 2 34  GLU 34  43  43  GLU GLU B . n 
B 2 35  GLY 35  44  44  GLY GLY B . n 
B 2 36  VAL 36  45  45  VAL VAL B . n 
B 2 37  PHE 37  46  46  PHE PHE B . n 
B 2 38  HIS 38  47  47  HIS HIS B . n 
B 2 39  THR 39  48  48  THR THR B . n 
B 2 40  MET 40  49  49  MET MET B . n 
B 2 41  TRP 41  50  50  TRP TRP B . n 
B 2 42  HIS 42  51  51  HIS HIS B . n 
B 2 43  VAL 43  52  52  VAL VAL B . n 
B 2 44  THR 44  53  53  THR THR B . n 
B 2 45  LYS 45  54  54  LYS LYS B . n 
B 2 46  GLY 46  55  55  GLY GLY B . n 
B 2 47  ALA 47  56  56  ALA ALA B . n 
B 2 48  ALA 48  57  57  ALA ALA B . n 
B 2 49  LEU 49  58  58  LEU LEU B . n 
B 2 50  ARG 50  59  59  ARG ARG B . n 
B 2 51  SER 51  60  60  SER SER B . n 
B 2 52  GLY 52  61  61  GLY GLY B . n 
B 2 53  GLU 53  62  62  GLU GLU B . n 
B 2 54  GLY 54  63  63  GLY GLY B . n 
B 2 55  ARG 55  64  64  ARG ARG B . n 
B 2 56  LEU 56  65  65  LEU LEU B . n 
B 2 57  ASP 57  66  66  ASP ASP B . n 
B 2 58  PRO 58  67  67  PRO PRO B . n 
B 2 59  TYR 59  68  68  TYR TYR B . n 
B 2 60  TRP 60  69  69  TRP TRP B . n 
B 2 61  GLY 61  70  70  GLY GLY B . n 
B 2 62  ASP 62  71  71  ASP ASP B . n 
B 2 63  VAL 63  72  72  VAL VAL B . n 
B 2 64  LYS 64  73  73  LYS LYS B . n 
B 2 65  GLN 65  74  74  GLN GLN B . n 
B 2 66  ASP 66  75  75  ASP ASP B . n 
B 2 67  LEU 67  76  76  LEU LEU B . n 
B 2 68  VAL 68  77  77  VAL VAL B . n 
B 2 69  SER 69  78  78  SER SER B . n 
B 2 70  TYR 70  79  79  TYR TYR B . n 
B 2 71  CYS 71  80  80  CYS CYS B . n 
B 2 72  GLY 72  81  81  GLY GLY B . n 
B 2 73  PRO 73  82  82  PRO PRO B . n 
B 2 74  TRP 74  83  83  TRP TRP B . n 
B 2 75  LYS 75  84  84  LYS LYS B . n 
B 2 76  LEU 76  85  85  LEU LEU B . n 
B 2 77  ASP 77  86  86  ASP ASP B . n 
B 2 78  ALA 78  87  87  ALA ALA B . n 
B 2 79  ALA 79  88  88  ALA ALA B . n 
B 2 80  TRP 80  89  89  TRP TRP B . n 
B 2 81  ASP 81  90  90  ASP ASP B . n 
B 2 82  GLY 82  91  91  GLY GLY B . n 
B 2 83  LEU 83  92  92  LEU LEU B . n 
B 2 84  SER 84  93  93  SER SER B . n 
B 2 85  GLU 85  94  94  GLU GLU B . n 
B 2 86  VAL 86  95  95  VAL VAL B . n 
B 2 87  GLN 87  96  96  GLN GLN B . n 
B 2 88  LEU 88  97  97  LEU LEU B . n 
B 2 89  LEU 89  98  98  LEU LEU B . n 
B 2 90  ALA 90  99  99  ALA ALA B . n 
B 2 91  VAL 91  100 100 VAL VAL B . n 
B 2 92  PRO 92  101 101 PRO PRO B . n 
B 2 93  PRO 93  102 102 PRO PRO B . n 
B 2 94  GLY 94  103 103 GLY GLY B . n 
B 2 95  GLU 95  104 104 GLU GLU B . n 
B 2 96  ARG 96  105 105 ARG ARG B . n 
B 2 97  ALA 97  106 106 ALA ALA B . n 
B 2 98  LYS 98  107 107 LYS LYS B . n 
B 2 99  ASN 99  108 108 ASN ASN B . n 
B 2 100 ILE 100 109 109 ILE ILE B . n 
B 2 101 GLN 101 110 110 GLN GLN B . n 
B 2 102 THR 102 111 111 THR THR B . n 
B 2 103 LEU 103 112 112 LEU LEU B . n 
B 2 104 PRO 104 113 113 PRO PRO B . n 
B 2 105 GLY 105 114 114 GLY GLY B . n 
B 2 106 ILE 106 115 115 ILE ILE B . n 
B 2 107 PHE 107 116 116 PHE PHE B . n 
B 2 108 LYS 108 117 117 LYS LYS B . n 
B 2 109 THR 109 118 118 THR THR B . n 
B 2 110 LYS 110 119 119 LYS LYS B . n 
B 2 111 ASP 111 120 120 ASP ASP B . n 
B 2 112 GLY 112 121 121 GLY GLY B . n 
B 2 113 ASP 113 122 122 ASP ASP B . n 
B 2 114 ILE 114 123 123 ILE ILE B . n 
B 2 115 GLY 115 124 124 GLY GLY B . n 
B 2 116 ALA 116 125 125 ALA ALA B . n 
B 2 117 VAL 117 126 126 VAL VAL B . n 
B 2 118 ALA 118 127 127 ALA ALA B . n 
B 2 119 LEU 119 128 128 LEU LEU B . n 
B 2 120 ASP 120 129 129 ASP ASP B . n 
B 2 121 TYR 121 130 130 TYR TYR B . n 
B 2 122 PRO 122 131 131 PRO PRO B . n 
B 2 123 ALA 123 132 132 ALA ALA B . n 
B 2 124 GLY 124 133 133 GLY GLY B . n 
B 2 125 THR 125 134 134 THR THR B . n 
B 2 126 SER 126 135 135 SER SER B . n 
B 2 127 GLY 127 136 136 GLY GLY B . n 
B 2 128 SER 128 137 137 SER SER B . n 
B 2 129 PRO 129 138 138 PRO PRO B . n 
B 2 130 ILE 130 139 139 ILE ILE B . n 
B 2 131 LEU 131 140 140 LEU LEU B . n 
B 2 132 ASP 132 141 141 ASP ASP B . n 
B 2 133 LYS 133 142 142 LYS LYS B . n 
B 2 134 CYS 134 143 143 CYS CYS B . n 
B 2 135 GLY 135 144 144 GLY GLY B . n 
B 2 136 ARG 136 145 145 ARG ARG B . n 
B 2 137 VAL 137 146 146 VAL VAL B . n 
B 2 138 ILE 138 147 147 ILE ILE B . n 
B 2 139 GLY 139 148 148 GLY GLY B . n 
B 2 140 LEU 140 149 149 LEU LEU B . n 
B 2 141 TYR 141 150 150 TYR TYR B . n 
B 2 142 GLY 142 151 151 GLY GLY B . n 
B 2 143 ASN 143 152 152 ASN ASN B . n 
B 2 144 GLY 144 153 153 GLY GLY B . n 
B 2 145 VAL 145 154 154 VAL VAL B . n 
B 2 146 VAL 146 155 155 VAL VAL B . n 
B 2 147 ILE 147 156 156 ILE ILE B . n 
B 2 148 LYS 148 157 157 LYS LYS B . n 
B 2 149 ASN 149 158 158 ASN ASN B . n 
B 2 150 GLY 150 159 159 GLY GLY B . n 
B 2 151 SER 151 160 160 SER SER B . n 
B 2 152 TYR 152 161 161 TYR TYR B . n 
B 2 153 VAL 153 162 162 VAL VAL B . n 
B 2 154 SER 154 163 163 SER SER B . n 
B 2 155 ALA 155 164 164 ALA ALA B . n 
B 2 156 ILE 156 165 165 ILE ILE B . n 
B 2 157 THR 157 166 166 THR THR B . n 
B 2 158 GLN 158 167 167 GLN GLN B . n 
B 2 159 GLY 159 168 168 GLY GLY B . n 
B 2 160 LYS 160 169 169 LYS LYS B . n 
B 2 161 ARG 161 170 170 ARG ARG B . n 
B 2 162 GLU 162 171 171 GLU GLU B . n 
B 2 163 GLU 163 172 ?   ?   ?   B . n 
B 2 164 GLU 164 173 ?   ?   ?   B . n 
B 2 165 THR 165 174 ?   ?   ?   B . n 
B 2 166 PRO 166 175 ?   ?   ?   B . n 
B 2 167 VAL 167 176 ?   ?   ?   B . n 
B 2 168 GLU 168 177 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BGI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BGI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 DMS   1  201 201 DMS   DMS B . 
D 3 DMS   1  202 202 DMS   DMS B . 
E 3 DMS   1  203 203 DMS   DMS B . 
F 4 A1BGI 1  204 301 A1BGI LIG B . 
G 5 SO4   1  205 302 SO4   SO4 B . 
H 5 SO4   1  206 303 SO4   SO4 B . 
I 6 HOH   1  101 65  HOH   HOH A . 
I 6 HOH   2  102 34  HOH   HOH A . 
I 6 HOH   3  103 20  HOH   HOH A . 
I 6 HOH   4  104 54  HOH   HOH A . 
I 6 HOH   5  105 129 HOH   HOH A . 
I 6 HOH   6  106 121 HOH   HOH A . 
I 6 HOH   7  107 27  HOH   HOH A . 
I 6 HOH   8  108 60  HOH   HOH A . 
I 6 HOH   9  109 16  HOH   HOH A . 
I 6 HOH   10 110 118 HOH   HOH A . 
I 6 HOH   11 111 105 HOH   HOH A . 
I 6 HOH   12 112 70  HOH   HOH A . 
I 6 HOH   13 113 98  HOH   HOH A . 
I 6 HOH   14 114 110 HOH   HOH A . 
I 6 HOH   15 115 123 HOH   HOH A . 
I 6 HOH   16 116 128 HOH   HOH A . 
I 6 HOH   17 117 119 HOH   HOH A . 
I 6 HOH   18 118 120 HOH   HOH A . 
I 6 HOH   19 119 85  HOH   HOH A . 
I 6 HOH   20 120 87  HOH   HOH A . 
I 6 HOH   21 121 50  HOH   HOH A . 
J 6 HOH   1  301 131 HOH   HOH B . 
J 6 HOH   2  302 1   HOH   HOH B . 
J 6 HOH   3  303 11  HOH   HOH B . 
J 6 HOH   4  304 103 HOH   HOH B . 
J 6 HOH   5  305 40  HOH   HOH B . 
J 6 HOH   6  306 127 HOH   HOH B . 
J 6 HOH   7  307 115 HOH   HOH B . 
J 6 HOH   8  308 51  HOH   HOH B . 
J 6 HOH   9  309 29  HOH   HOH B . 
J 6 HOH   10 310 48  HOH   HOH B . 
J 6 HOH   11 311 116 HOH   HOH B . 
J 6 HOH   12 312 130 HOH   HOH B . 
J 6 HOH   13 313 133 HOH   HOH B . 
J 6 HOH   14 314 108 HOH   HOH B . 
J 6 HOH   15 315 90  HOH   HOH B . 
J 6 HOH   16 316 32  HOH   HOH B . 
J 6 HOH   17 317 92  HOH   HOH B . 
J 6 HOH   18 318 81  HOH   HOH B . 
J 6 HOH   19 319 14  HOH   HOH B . 
J 6 HOH   20 320 4   HOH   HOH B . 
J 6 HOH   21 321 117 HOH   HOH B . 
J 6 HOH   22 322 57  HOH   HOH B . 
J 6 HOH   23 323 23  HOH   HOH B . 
J 6 HOH   24 324 59  HOH   HOH B . 
J 6 HOH   25 325 68  HOH   HOH B . 
J 6 HOH   26 326 9   HOH   HOH B . 
J 6 HOH   27 327 63  HOH   HOH B . 
J 6 HOH   28 328 10  HOH   HOH B . 
J 6 HOH   29 329 73  HOH   HOH B . 
J 6 HOH   30 330 122 HOH   HOH B . 
J 6 HOH   31 331 35  HOH   HOH B . 
J 6 HOH   32 332 17  HOH   HOH B . 
J 6 HOH   33 333 46  HOH   HOH B . 
J 6 HOH   34 334 132 HOH   HOH B . 
J 6 HOH   35 335 100 HOH   HOH B . 
J 6 HOH   36 336 58  HOH   HOH B . 
J 6 HOH   37 337 67  HOH   HOH B . 
J 6 HOH   38 338 79  HOH   HOH B . 
J 6 HOH   39 339 75  HOH   HOH B . 
J 6 HOH   40 340 2   HOH   HOH B . 
J 6 HOH   41 341 28  HOH   HOH B . 
J 6 HOH   42 342 77  HOH   HOH B . 
J 6 HOH   43 343 106 HOH   HOH B . 
J 6 HOH   44 344 66  HOH   HOH B . 
J 6 HOH   45 345 82  HOH   HOH B . 
J 6 HOH   46 346 13  HOH   HOH B . 
J 6 HOH   47 347 21  HOH   HOH B . 
J 6 HOH   48 348 61  HOH   HOH B . 
J 6 HOH   49 349 31  HOH   HOH B . 
J 6 HOH   50 350 36  HOH   HOH B . 
J 6 HOH   51 351 43  HOH   HOH B . 
J 6 HOH   52 352 56  HOH   HOH B . 
J 6 HOH   53 353 3   HOH   HOH B . 
J 6 HOH   54 354 125 HOH   HOH B . 
J 6 HOH   55 355 124 HOH   HOH B . 
J 6 HOH   56 356 18  HOH   HOH B . 
J 6 HOH   57 357 126 HOH   HOH B . 
J 6 HOH   58 358 49  HOH   HOH B . 
J 6 HOH   59 359 44  HOH   HOH B . 
J 6 HOH   60 360 109 HOH   HOH B . 
J 6 HOH   61 361 80  HOH   HOH B . 
J 6 HOH   62 362 69  HOH   HOH B . 
J 6 HOH   63 363 64  HOH   HOH B . 
J 6 HOH   64 364 30  HOH   HOH B . 
J 6 HOH   65 365 5   HOH   HOH B . 
J 6 HOH   66 366 112 HOH   HOH B . 
J 6 HOH   67 367 42  HOH   HOH B . 
J 6 HOH   68 368 24  HOH   HOH B . 
J 6 HOH   69 369 102 HOH   HOH B . 
J 6 HOH   70 370 94  HOH   HOH B . 
J 6 HOH   71 371 26  HOH   HOH B . 
J 6 HOH   72 372 107 HOH   HOH B . 
J 6 HOH   73 373 72  HOH   HOH B . 
J 6 HOH   74 374 89  HOH   HOH B . 
J 6 HOH   75 375 45  HOH   HOH B . 
J 6 HOH   76 376 83  HOH   HOH B . 
J 6 HOH   77 377 39  HOH   HOH B . 
J 6 HOH   78 378 62  HOH   HOH B . 
J 6 HOH   79 379 12  HOH   HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       BUSTER  .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
'data reduction' XDS     .        ? 6 
'data reduction' XDS     .        ? 7 
'data reduction' XDS     .        ? 8 
'data reduction' XDS     .        ? 9 
# 
_cell.entry_id           7HOZ 
_cell.length_a           42.549 
_cell.length_b           42.549 
_cell.length_c           216.320 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HOZ 
_symmetry.space_group_name_H-M             'P 43 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                95 
# 
_exptl.entry_id          7HOZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.11 
_exptl_crystal.density_percent_sol   41.75 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              4.8 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.pdbx_details    '30% w/v PEG 2000, 0.2M Ammonium sulfate, 0.1M acetate (pH 4.8)' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2023-09-27 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92124 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92124 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HOZ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             216.28 
_reflns.d_resolution_high            1.58 
_reflns.number_obs                   28658 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.094 
_reflns.pdbx_netI_over_sigmaI        14.4 
_reflns.pdbx_redundancy              25.5 
_reflns.pdbx_Rrim_I_all              0.096 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_number_measured_all     730956 
_reflns.pdbx_chi_squared             0.34 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.58 
_reflns_shell.d_res_low                   1.61 
_reflns_shell.number_measured_all         32203 
_reflns_shell.number_unique_obs           1394 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_chi_squared            0.12 
_reflns_shell.pdbx_redundancy             23.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             10.502 
_reflns_shell.pdbx_Rpim_I_all             2.162 
_reflns_shell.pdbx_CC_half                0.440 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HOZ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24206 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             54.08 
_refine.ls_d_res_high                            1.58 
_refine.ls_percent_reflns_obs                    89.36 
_refine.ls_R_factor_obs                          0.25489 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.25193 
_refine.ls_R_factor_R_free                       0.31093 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1306 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.933 
_refine.B_iso_mean                               44.504 
_refine.aniso_B[1][1]                            1.51 
_refine.aniso_B[2][2]                            1.51 
_refine.aniso_B[3][3]                            -3.02 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.284 
_refine.pdbx_overall_ESU_R_Free                  0.209 
_refine.overall_SU_ML                            0.331 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             11.039 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1476 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         41 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               1617 
_refine_hist.d_res_high                       1.58 
_refine_hist.d_res_low                        54.08 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.015  ? 5288 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 3360 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.471  1.642  ? 5237 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.169  1.597  ? 7830 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.161  5.000  ? 541  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.354 23.147 ? 197  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.358 15.000 ? 577  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       14.039 15.000 ? 25   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.054  0.200  ? 456  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 4772 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.004  0.020  ? 866  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.331  4.365  ? 2783 'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.378  4.379  ? 2643 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.204  6.532  ? 2553 'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.205  6.534  ? 2554 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.561  4.769  ? 2505 'X-RAY DIFFRACTION' ? 
r_scbond_other               2.560  4.755  ? 2479 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              4.548  6.931  ? 2661 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.957  50.657 ? 4411 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.841  50.565 ? 4367 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.580 
_refine_ls_shell.d_res_low                        1.621 
_refine_ls_shell.number_reflns_R_work             141 
_refine_ls_shell.R_factor_R_work                  0.906 
_refine_ls_shell.percent_reflns_obs               7.26 
_refine_ls_shell.R_factor_R_free                  0.721 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             7 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HOZ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal Structure of ZIKV NS2B-NS3 protease in complex with ASAP-0014795-001' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HOZ 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SGC - Diamond I04-1, PanDDA, XChemExplorer, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP POLG_ZIKV Q32ZE1 ? 1 GKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEE 1414 
2 UNP POLG_ZIKV Q32ZE1 ? 2 
;KEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWD
GLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKR
EEETPVE
;
1509 
# 
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 7HOZ A 3 ? 46  ? Q32ZE1 1414 ? 1457 ? 46 89  
2 2 7HOZ B 2 ? 168 ? Q32ZE1 1509 ? 1675 ? 11 177 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HOZ SER A 1  ? UNP Q32ZE1 ?   ?    'expression tag'        44  1 
1 7HOZ MET A 2  ? UNP Q32ZE1 ?   ?    'expression tag'        45  2 
2 7HOZ MET B 1  ? UNP Q32ZE1 ?   ?    'initiating methionine' 10  3 
2 7HOZ LYS B 98 ? UNP Q32ZE1 ARG 1605 conflict                107 4 
# 
_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 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_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 MET B 40  ? LYS B 45  ? MET B 49  LYS B 54  1 ? 6 
HELX_P HELX_P2 AA2 PRO B 122 ? SER B 126 ? PRO B 131 SER B 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            134 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            134 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            B 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             143 
_struct_conn.ptnr2_auth_asym_id            B 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             143 
_struct_conn.ptnr2_symmetry                8_444 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               2.779 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       134 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     B 
_pdbx_modification_feature.modified_residue_label_seq_id      134 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       B 
_pdbx_modification_feature.auth_seq_id                        143 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      B 
_pdbx_modification_feature.modified_residue_auth_seq_id       143 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          8_444 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 5 ? 
AA3 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLY B 54  ? LEU B 56  ? GLY B 63  LEU B 65  
AA1 2 LEU B 49  ? SER B 51  ? LEU B 58  SER B 60  
AA1 3 MET A 8   ? GLY A 14  ? MET A 51  GLY A 57  
AA1 4 GLY B 12  ? THR B 18  ? GLY B 21  THR B 27  
AA1 5 THR B 25  ? GLN B 33  ? THR B 34  GLN B 42  
AA1 6 VAL B 36  ? THR B 39  ? VAL B 45  THR B 48  
AA1 7 LEU B 67  ? TYR B 70  ? LEU B 76  TYR B 79  
AA1 8 PRO B 58  ? ASP B 62  ? PRO B 67  ASP B 71  
AA2 1 GLU A 23  ? VAL A 24  ? GLU A 66  VAL A 67  
AA2 2 LYS B 98  ? THR B 102 ? LYS B 107 THR B 111 
AA2 3 VAL B 86  ? ALA B 90  ? VAL B 95  ALA B 99  
AA2 4 PRO B 129 ? LEU B 131 ? PRO B 138 LEU B 140 
AA2 5 VAL B 137 ? LEU B 140 ? VAL B 146 LEU B 149 
AA3 1 PHE A 41  ? LEU A 43  ? PHE A 84  LEU A 86  
AA3 2 ARG A 30  ? LEU A 35  ? ARG A 73  LEU A 78  
AA3 3 GLY B 105 ? LYS B 108 ? GLY B 114 LYS B 117 
AA3 4 ASP B 113 ? VAL B 117 ? ASP B 122 VAL B 126 
AA3 5 TYR B 152 ? ALA B 155 ? TYR B 161 ALA B 164 
AA3 6 GLY B 144 ? VAL B 146 ? GLY B 153 VAL B 155 
# 
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 LEU B 56  ? O LEU B 65  N LEU B 49  ? N LEU B 58  
AA1 2 3 O ARG B 50  ? O ARG B 59  N MET A 8   ? N MET A 51  
AA1 3 4 N GLU A 11  ? N GLU A 54  O ARG B 15  ? O ARG B 24  
AA1 4 5 N THR B 18  ? N THR B 27  O THR B 25  ? O THR B 34  
AA1 5 6 N VAL B 31  ? N VAL B 40  O HIS B 38  ? O HIS B 47  
AA1 6 7 N THR B 39  ? N THR B 48  O VAL B 68  ? O VAL B 77  
AA1 7 8 O SER B 69  ? O SER B 78  N TYR B 59  ? N TYR B 68  
AA2 1 2 N GLU A 23  ? N GLU A 66  O GLN B 101 ? O GLN B 110 
AA2 2 3 O THR B 102 ? O THR B 111 N VAL B 86  ? N VAL B 95  
AA2 3 4 N GLN B 87  ? N GLN B 96  O LEU B 131 ? O LEU B 140 
AA2 4 5 N ILE B 130 ? N ILE B 139 O GLY B 139 ? O GLY B 148 
AA3 1 2 O SER A 42  ? O SER A 85  N ALA A 34  ? N ALA A 77  
AA3 2 3 N LEU A 31  ? N LEU A 74  O ILE B 106 ? O ILE B 115 
AA3 3 4 N GLY B 105 ? N GLY B 114 O ALA B 116 ? O ALA B 125 
AA3 4 5 N VAL B 117 ? N VAL B 126 O SER B 154 ? O SER B 163 
AA3 5 6 O VAL B 153 ? O VAL B 162 N VAL B 145 ? N VAL B 154 
# 
_pdbx_entry_details.entry_id                   7HOZ 
_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     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    90 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    93 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.94 
# 
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 ALA A 56  ? C -146.43 -15.77  
2  1 ALA A 56  ? D -146.38 -15.81  
3  1 ASP A 64  ? C 73.24   54.83   
4  1 ASP A 64  ? D 73.25   54.89   
5  1 THR A 68  ? C -123.03 -168.92 
6  1 THR A 68  ? D -123.10 -168.92 
7  1 CYS B 80  ? ? 83.52   -9.29   
8  1 LEU B 92  ? ? -127.61 -51.42  
9  1 LEU B 98  ? A -110.81 78.59   
10 1 LEU B 98  ? B -110.84 78.54   
11 1 LEU B 98  ? C -61.12  78.19   
12 1 LEU B 98  ? D -61.12  78.19   
13 1 LYS B 157 ? A -37.34  -27.88  
14 1 LYS B 157 ? B -37.36  -27.73  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 359 ? J HOH . 
2 1 B HOH 375 ? J HOH . 
3 1 B HOH 377 ? J HOH . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER 44  ? A SER 1   
2  1 Y 1 A MET 45  ? A MET 2   
3  1 Y 1 A GLY 46  ? A GLY 3   
4  1 Y 1 A LYS 47  ? A LYS 4   
5  1 Y 1 A SER 48  ? A SER 5   
6  1 Y 1 A VAL 49  ? A VAL 6   
7  1 Y 1 A GLU 89  ? A GLU 46  
8  1 Y 1 B MET 10  ? B MET 1   
9  1 Y 1 B LYS 11  ? B LYS 2   
10 1 Y 1 B GLU 12  ? B GLU 3   
11 1 Y 1 B VAL 13  ? B VAL 4   
12 1 Y 1 B LYS 14  ? B LYS 5   
13 1 Y 1 B LYS 15  ? B LYS 6   
14 1 Y 1 B GLU 172 ? B GLU 163 
15 1 Y 1 B GLU 173 ? B GLU 164 
16 1 Y 1 B THR 174 ? B THR 165 
17 1 Y 1 B PRO 175 ? B PRO 166 
18 1 Y 1 B VAL 176 ? B VAL 167 
19 1 Y 1 B GLU 177 ? B GLU 168 
# 
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 
A1BGI N1   N Y N 1   
A1BGI N3   N Y N 2   
A1BGI C4   C N N 3   
A1BGI C5   C Y N 4   
A1BGI C6   C Y N 5   
A1BGI C7   C Y N 6   
A1BGI C8   C Y N 7   
A1BGI C10  C Y N 8   
A1BGI C13  C Y N 9   
A1BGI C1   C N N 10  
A1BGI C2   C Y N 11  
A1BGI C3   C Y N 12  
A1BGI N2   N N N 13  
A1BGI O1   O N N 14  
A1BGI C9   C Y N 15  
A1BGI C11  C Y N 16  
A1BGI C12  C Y N 17  
A1BGI C14  C Y N 18  
A1BGI N4   N Y N 19  
A1BGI H6   H N N 20  
A1BGI H7   H N N 21  
A1BGI H8   H N N 22  
A1BGI H9   H N N 23  
A1BGI H3   H N N 24  
A1BGI H1   H N N 25  
A1BGI H2   H N N 26  
A1BGI H4   H N N 27  
A1BGI H5   H N N 28  
A1BGI H10  H N N 29  
A1BGI H11  H N N 30  
A1BGI H12  H N N 31  
ALA   N    N N N 32  
ALA   CA   C N S 33  
ALA   C    C N N 34  
ALA   O    O N N 35  
ALA   CB   C N N 36  
ALA   OXT  O N N 37  
ALA   H    H N N 38  
ALA   H2   H N N 39  
ALA   HA   H N N 40  
ALA   HB1  H N N 41  
ALA   HB2  H N N 42  
ALA   HB3  H N N 43  
ALA   HXT  H N N 44  
ARG   N    N N N 45  
ARG   CA   C N S 46  
ARG   C    C N N 47  
ARG   O    O N N 48  
ARG   CB   C N N 49  
ARG   CG   C N N 50  
ARG   CD   C N N 51  
ARG   NE   N N N 52  
ARG   CZ   C N N 53  
ARG   NH1  N N N 54  
ARG   NH2  N N N 55  
ARG   OXT  O N N 56  
ARG   H    H N N 57  
ARG   H2   H N N 58  
ARG   HA   H N N 59  
ARG   HB2  H N N 60  
ARG   HB3  H N N 61  
ARG   HG2  H N N 62  
ARG   HG3  H N N 63  
ARG   HD2  H N N 64  
ARG   HD3  H N N 65  
ARG   HE   H N N 66  
ARG   HH11 H N N 67  
ARG   HH12 H N N 68  
ARG   HH21 H N N 69  
ARG   HH22 H N N 70  
ARG   HXT  H N N 71  
ASN   N    N N N 72  
ASN   CA   C N S 73  
ASN   C    C N N 74  
ASN   O    O N N 75  
ASN   CB   C N N 76  
ASN   CG   C N N 77  
ASN   OD1  O N N 78  
ASN   ND2  N N N 79  
ASN   OXT  O N N 80  
ASN   H    H N N 81  
ASN   H2   H N N 82  
ASN   HA   H N N 83  
ASN   HB2  H N N 84  
ASN   HB3  H N N 85  
ASN   HD21 H N N 86  
ASN   HD22 H N N 87  
ASN   HXT  H N N 88  
ASP   N    N N N 89  
ASP   CA   C N S 90  
ASP   C    C N N 91  
ASP   O    O N N 92  
ASP   CB   C N N 93  
ASP   CG   C N N 94  
ASP   OD1  O N N 95  
ASP   OD2  O N N 96  
ASP   OXT  O N N 97  
ASP   H    H N N 98  
ASP   H2   H N N 99  
ASP   HA   H N N 100 
ASP   HB2  H N N 101 
ASP   HB3  H N N 102 
ASP   HD2  H N N 103 
ASP   HXT  H N N 104 
CYS   N    N N N 105 
CYS   CA   C N R 106 
CYS   C    C N N 107 
CYS   O    O N N 108 
CYS   CB   C N N 109 
CYS   SG   S N N 110 
CYS   OXT  O N N 111 
CYS   H    H N N 112 
CYS   H2   H N N 113 
CYS   HA   H N N 114 
CYS   HB2  H N N 115 
CYS   HB3  H N N 116 
CYS   HG   H N N 117 
CYS   HXT  H N N 118 
DMS   S    S N N 119 
DMS   O    O N N 120 
DMS   C1   C N N 121 
DMS   C2   C N N 122 
DMS   H11  H N N 123 
DMS   H12  H N N 124 
DMS   H13  H N N 125 
DMS   H21  H N N 126 
DMS   H22  H N N 127 
DMS   H23  H N N 128 
GLN   N    N N N 129 
GLN   CA   C N S 130 
GLN   C    C N N 131 
GLN   O    O N N 132 
GLN   CB   C N N 133 
GLN   CG   C N N 134 
GLN   CD   C N N 135 
GLN   OE1  O N N 136 
GLN   NE2  N N N 137 
GLN   OXT  O N N 138 
GLN   H    H N N 139 
GLN   H2   H N N 140 
GLN   HA   H N N 141 
GLN   HB2  H N N 142 
GLN   HB3  H N N 143 
GLN   HG2  H N N 144 
GLN   HG3  H N N 145 
GLN   HE21 H N N 146 
GLN   HE22 H N N 147 
GLN   HXT  H N N 148 
GLU   N    N N N 149 
GLU   CA   C N S 150 
GLU   C    C N N 151 
GLU   O    O N N 152 
GLU   CB   C N N 153 
GLU   CG   C N N 154 
GLU   CD   C N N 155 
GLU   OE1  O N N 156 
GLU   OE2  O N N 157 
GLU   OXT  O N N 158 
GLU   H    H N N 159 
GLU   H2   H N N 160 
GLU   HA   H N N 161 
GLU   HB2  H N N 162 
GLU   HB3  H N N 163 
GLU   HG2  H N N 164 
GLU   HG3  H N N 165 
GLU   HE2  H N N 166 
GLU   HXT  H N N 167 
GLY   N    N N N 168 
GLY   CA   C N N 169 
GLY   C    C N N 170 
GLY   O    O N N 171 
GLY   OXT  O N N 172 
GLY   H    H N N 173 
GLY   H2   H N N 174 
GLY   HA2  H N N 175 
GLY   HA3  H N N 176 
GLY   HXT  H N N 177 
HIS   N    N N N 178 
HIS   CA   C N S 179 
HIS   C    C N N 180 
HIS   O    O N N 181 
HIS   CB   C N N 182 
HIS   CG   C Y N 183 
HIS   ND1  N Y N 184 
HIS   CD2  C Y N 185 
HIS   CE1  C Y N 186 
HIS   NE2  N Y N 187 
HIS   OXT  O N N 188 
HIS   H    H N N 189 
HIS   H2   H N N 190 
HIS   HA   H N N 191 
HIS   HB2  H N N 192 
HIS   HB3  H N N 193 
HIS   HD1  H N N 194 
HIS   HD2  H N N 195 
HIS   HE1  H N N 196 
HIS   HE2  H N N 197 
HIS   HXT  H N N 198 
HOH   O    O N N 199 
HOH   H1   H N N 200 
HOH   H2   H N N 201 
ILE   N    N N N 202 
ILE   CA   C N S 203 
ILE   C    C N N 204 
ILE   O    O N N 205 
ILE   CB   C N S 206 
ILE   CG1  C N N 207 
ILE   CG2  C N N 208 
ILE   CD1  C N N 209 
ILE   OXT  O N N 210 
ILE   H    H N N 211 
ILE   H2   H N N 212 
ILE   HA   H N N 213 
ILE   HB   H N N 214 
ILE   HG12 H N N 215 
ILE   HG13 H N N 216 
ILE   HG21 H N N 217 
ILE   HG22 H N N 218 
ILE   HG23 H N N 219 
ILE   HD11 H N N 220 
ILE   HD12 H N N 221 
ILE   HD13 H N N 222 
ILE   HXT  H N N 223 
LEU   N    N N N 224 
LEU   CA   C N S 225 
LEU   C    C N N 226 
LEU   O    O N N 227 
LEU   CB   C N N 228 
LEU   CG   C N N 229 
LEU   CD1  C N N 230 
LEU   CD2  C N N 231 
LEU   OXT  O N N 232 
LEU   H    H N N 233 
LEU   H2   H N N 234 
LEU   HA   H N N 235 
LEU   HB2  H N N 236 
LEU   HB3  H N N 237 
LEU   HG   H N N 238 
LEU   HD11 H N N 239 
LEU   HD12 H N N 240 
LEU   HD13 H N N 241 
LEU   HD21 H N N 242 
LEU   HD22 H N N 243 
LEU   HD23 H N N 244 
LEU   HXT  H N N 245 
LYS   N    N N N 246 
LYS   CA   C N S 247 
LYS   C    C N N 248 
LYS   O    O N N 249 
LYS   CB   C N N 250 
LYS   CG   C N N 251 
LYS   CD   C N N 252 
LYS   CE   C N N 253 
LYS   NZ   N N N 254 
LYS   OXT  O N N 255 
LYS   H    H N N 256 
LYS   H2   H N N 257 
LYS   HA   H N N 258 
LYS   HB2  H N N 259 
LYS   HB3  H N N 260 
LYS   HG2  H N N 261 
LYS   HG3  H N N 262 
LYS   HD2  H N N 263 
LYS   HD3  H N N 264 
LYS   HE2  H N N 265 
LYS   HE3  H N N 266 
LYS   HZ1  H N N 267 
LYS   HZ2  H N N 268 
LYS   HZ3  H N N 269 
LYS   HXT  H N N 270 
MET   N    N N N 271 
MET   CA   C N S 272 
MET   C    C N N 273 
MET   O    O N N 274 
MET   CB   C N N 275 
MET   CG   C N N 276 
MET   SD   S N N 277 
MET   CE   C N N 278 
MET   OXT  O N N 279 
MET   H    H N N 280 
MET   H2   H N N 281 
MET   HA   H N N 282 
MET   HB2  H N N 283 
MET   HB3  H N N 284 
MET   HG2  H N N 285 
MET   HG3  H N N 286 
MET   HE1  H N N 287 
MET   HE2  H N N 288 
MET   HE3  H N N 289 
MET   HXT  H N N 290 
PHE   N    N N N 291 
PHE   CA   C N S 292 
PHE   C    C N N 293 
PHE   O    O N N 294 
PHE   CB   C N N 295 
PHE   CG   C Y N 296 
PHE   CD1  C Y N 297 
PHE   CD2  C Y N 298 
PHE   CE1  C Y N 299 
PHE   CE2  C Y N 300 
PHE   CZ   C Y N 301 
PHE   OXT  O N N 302 
PHE   H    H N N 303 
PHE   H2   H N N 304 
PHE   HA   H N N 305 
PHE   HB2  H N N 306 
PHE   HB3  H N N 307 
PHE   HD1  H N N 308 
PHE   HD2  H N N 309 
PHE   HE1  H N N 310 
PHE   HE2  H N N 311 
PHE   HZ   H N N 312 
PHE   HXT  H N N 313 
PRO   N    N N N 314 
PRO   CA   C N S 315 
PRO   C    C N N 316 
PRO   O    O N N 317 
PRO   CB   C N N 318 
PRO   CG   C N N 319 
PRO   CD   C N N 320 
PRO   OXT  O N N 321 
PRO   H    H N N 322 
PRO   HA   H N N 323 
PRO   HB2  H N N 324 
PRO   HB3  H N N 325 
PRO   HG2  H N N 326 
PRO   HG3  H N N 327 
PRO   HD2  H N N 328 
PRO   HD3  H N N 329 
PRO   HXT  H N N 330 
SER   N    N N N 331 
SER   CA   C N S 332 
SER   C    C N N 333 
SER   O    O N N 334 
SER   CB   C N N 335 
SER   OG   O N N 336 
SER   OXT  O N N 337 
SER   H    H N N 338 
SER   H2   H N N 339 
SER   HA   H N N 340 
SER   HB2  H N N 341 
SER   HB3  H N N 342 
SER   HG   H N N 343 
SER   HXT  H N N 344 
SO4   S    S N N 345 
SO4   O1   O N N 346 
SO4   O2   O N N 347 
SO4   O3   O N N 348 
SO4   O4   O N N 349 
THR   N    N N N 350 
THR   CA   C N S 351 
THR   C    C N N 352 
THR   O    O N N 353 
THR   CB   C N R 354 
THR   OG1  O N N 355 
THR   CG2  C N N 356 
THR   OXT  O N N 357 
THR   H    H N N 358 
THR   H2   H N N 359 
THR   HA   H N N 360 
THR   HB   H N N 361 
THR   HG1  H N N 362 
THR   HG21 H N N 363 
THR   HG22 H N N 364 
THR   HG23 H N N 365 
THR   HXT  H N N 366 
TRP   N    N N N 367 
TRP   CA   C N S 368 
TRP   C    C N N 369 
TRP   O    O N N 370 
TRP   CB   C N N 371 
TRP   CG   C Y N 372 
TRP   CD1  C Y N 373 
TRP   CD2  C Y N 374 
TRP   NE1  N Y N 375 
TRP   CE2  C Y N 376 
TRP   CE3  C Y N 377 
TRP   CZ2  C Y N 378 
TRP   CZ3  C Y N 379 
TRP   CH2  C Y N 380 
TRP   OXT  O N N 381 
TRP   H    H N N 382 
TRP   H2   H N N 383 
TRP   HA   H N N 384 
TRP   HB2  H N N 385 
TRP   HB3  H N N 386 
TRP   HD1  H N N 387 
TRP   HE1  H N N 388 
TRP   HE3  H N N 389 
TRP   HZ2  H N N 390 
TRP   HZ3  H N N 391 
TRP   HH2  H N N 392 
TRP   HXT  H N N 393 
TYR   N    N N N 394 
TYR   CA   C N S 395 
TYR   C    C N N 396 
TYR   O    O N N 397 
TYR   CB   C N N 398 
TYR   CG   C Y N 399 
TYR   CD1  C Y N 400 
TYR   CD2  C Y N 401 
TYR   CE1  C Y N 402 
TYR   CE2  C Y N 403 
TYR   CZ   C Y N 404 
TYR   OH   O N N 405 
TYR   OXT  O N N 406 
TYR   H    H N N 407 
TYR   H2   H N N 408 
TYR   HA   H N N 409 
TYR   HB2  H N N 410 
TYR   HB3  H N N 411 
TYR   HD1  H N N 412 
TYR   HD2  H N N 413 
TYR   HE1  H N N 414 
TYR   HE2  H N N 415 
TYR   HH   H N N 416 
TYR   HXT  H N N 417 
VAL   N    N N N 418 
VAL   CA   C N S 419 
VAL   C    C N N 420 
VAL   O    O N N 421 
VAL   CB   C N N 422 
VAL   CG1  C N N 423 
VAL   CG2  C N N 424 
VAL   OXT  O N N 425 
VAL   H    H N N 426 
VAL   H2   H N N 427 
VAL   HA   H N N 428 
VAL   HB   H N N 429 
VAL   HG11 H N N 430 
VAL   HG12 H N N 431 
VAL   HG13 H N N 432 
VAL   HG21 H N N 433 
VAL   HG22 H N N 434 
VAL   HG23 H N N 435 
VAL   HXT  H N N 436 
# 
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 
A1BGI C1  N1   sing N N 1   
A1BGI N1  C2   sing Y N 2   
A1BGI C2  C3   doub Y N 3   
A1BGI C3  N2   sing N N 4   
A1BGI N2  C4   sing N N 5   
A1BGI C4  O1   doub N N 6   
A1BGI C4  C5   sing N N 7   
A1BGI C5  C6   doub Y N 8   
A1BGI C6  C7   sing Y N 9   
A1BGI C7  C8   doub Y N 10  
A1BGI C8  C9   sing Y N 11  
A1BGI C9  N3   doub Y N 12  
A1BGI N3  C10  sing Y N 13  
A1BGI C10 C11  doub Y N 14  
A1BGI C11 C12  sing Y N 15  
A1BGI C12 C13  doub Y N 16  
A1BGI C3  C14  sing Y N 17  
A1BGI C14 N4   doub Y N 18  
A1BGI N1  N4   sing Y N 19  
A1BGI C5  C13  sing Y N 20  
A1BGI C9  C13  sing Y N 21  
A1BGI C6  H6   sing N N 22  
A1BGI C7  H7   sing N N 23  
A1BGI C8  H8   sing N N 24  
A1BGI C10 H9   sing N N 25  
A1BGI C1  H3   sing N N 26  
A1BGI C1  H1   sing N N 27  
A1BGI C1  H2   sing N N 28  
A1BGI C2  H4   sing N N 29  
A1BGI N2  H5   sing N N 30  
A1BGI C11 H10  sing N N 31  
A1BGI C12 H11  sing N N 32  
A1BGI C14 H12  sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
DMS   S   O    doub N N 116 
DMS   S   C1   sing N N 117 
DMS   S   C2   sing N N 118 
DMS   C1  H11  sing N N 119 
DMS   C1  H12  sing N N 120 
DMS   C1  H13  sing N N 121 
DMS   C2  H21  sing N N 122 
DMS   C2  H22  sing N N 123 
DMS   C2  H23  sing N N 124 
GLN   N   CA   sing N N 125 
GLN   N   H    sing N N 126 
GLN   N   H2   sing N N 127 
GLN   CA  C    sing N N 128 
GLN   CA  CB   sing N N 129 
GLN   CA  HA   sing N N 130 
GLN   C   O    doub N N 131 
GLN   C   OXT  sing N N 132 
GLN   CB  CG   sing N N 133 
GLN   CB  HB2  sing N N 134 
GLN   CB  HB3  sing N N 135 
GLN   CG  CD   sing N N 136 
GLN   CG  HG2  sing N N 137 
GLN   CG  HG3  sing N N 138 
GLN   CD  OE1  doub N N 139 
GLN   CD  NE2  sing N N 140 
GLN   NE2 HE21 sing N N 141 
GLN   NE2 HE22 sing N N 142 
GLN   OXT HXT  sing N N 143 
GLU   N   CA   sing N N 144 
GLU   N   H    sing N N 145 
GLU   N   H2   sing N N 146 
GLU   CA  C    sing N N 147 
GLU   CA  CB   sing N N 148 
GLU   CA  HA   sing N N 149 
GLU   C   O    doub N N 150 
GLU   C   OXT  sing N N 151 
GLU   CB  CG   sing N N 152 
GLU   CB  HB2  sing N N 153 
GLU   CB  HB3  sing N N 154 
GLU   CG  CD   sing N N 155 
GLU   CG  HG2  sing N N 156 
GLU   CG  HG3  sing N N 157 
GLU   CD  OE1  doub N N 158 
GLU   CD  OE2  sing N N 159 
GLU   OE2 HE2  sing N N 160 
GLU   OXT HXT  sing N N 161 
GLY   N   CA   sing N N 162 
GLY   N   H    sing N N 163 
GLY   N   H2   sing N N 164 
GLY   CA  C    sing N N 165 
GLY   CA  HA2  sing N N 166 
GLY   CA  HA3  sing N N 167 
GLY   C   O    doub N N 168 
GLY   C   OXT  sing N N 169 
GLY   OXT HXT  sing N N 170 
HIS   N   CA   sing N N 171 
HIS   N   H    sing N N 172 
HIS   N   H2   sing N N 173 
HIS   CA  C    sing N N 174 
HIS   CA  CB   sing N N 175 
HIS   CA  HA   sing N N 176 
HIS   C   O    doub N N 177 
HIS   C   OXT  sing N N 178 
HIS   CB  CG   sing N N 179 
HIS   CB  HB2  sing N N 180 
HIS   CB  HB3  sing N N 181 
HIS   CG  ND1  sing Y N 182 
HIS   CG  CD2  doub Y N 183 
HIS   ND1 CE1  doub Y N 184 
HIS   ND1 HD1  sing N N 185 
HIS   CD2 NE2  sing Y N 186 
HIS   CD2 HD2  sing N N 187 
HIS   CE1 NE2  sing Y N 188 
HIS   CE1 HE1  sing N N 189 
HIS   NE2 HE2  sing N N 190 
HIS   OXT HXT  sing N N 191 
HOH   O   H1   sing N N 192 
HOH   O   H2   sing N N 193 
ILE   N   CA   sing N N 194 
ILE   N   H    sing N N 195 
ILE   N   H2   sing N N 196 
ILE   CA  C    sing N N 197 
ILE   CA  CB   sing N N 198 
ILE   CA  HA   sing N N 199 
ILE   C   O    doub N N 200 
ILE   C   OXT  sing N N 201 
ILE   CB  CG1  sing N N 202 
ILE   CB  CG2  sing N N 203 
ILE   CB  HB   sing N N 204 
ILE   CG1 CD1  sing N N 205 
ILE   CG1 HG12 sing N N 206 
ILE   CG1 HG13 sing N N 207 
ILE   CG2 HG21 sing N N 208 
ILE   CG2 HG22 sing N N 209 
ILE   CG2 HG23 sing N N 210 
ILE   CD1 HD11 sing N N 211 
ILE   CD1 HD12 sing N N 212 
ILE   CD1 HD13 sing N N 213 
ILE   OXT HXT  sing N N 214 
LEU   N   CA   sing N N 215 
LEU   N   H    sing N N 216 
LEU   N   H2   sing N N 217 
LEU   CA  C    sing N N 218 
LEU   CA  CB   sing N N 219 
LEU   CA  HA   sing N N 220 
LEU   C   O    doub N N 221 
LEU   C   OXT  sing N N 222 
LEU   CB  CG   sing N N 223 
LEU   CB  HB2  sing N N 224 
LEU   CB  HB3  sing N N 225 
LEU   CG  CD1  sing N N 226 
LEU   CG  CD2  sing N N 227 
LEU   CG  HG   sing N N 228 
LEU   CD1 HD11 sing N N 229 
LEU   CD1 HD12 sing N N 230 
LEU   CD1 HD13 sing N N 231 
LEU   CD2 HD21 sing N N 232 
LEU   CD2 HD22 sing N N 233 
LEU   CD2 HD23 sing N N 234 
LEU   OXT HXT  sing N N 235 
LYS   N   CA   sing N N 236 
LYS   N   H    sing N N 237 
LYS   N   H2   sing N N 238 
LYS   CA  C    sing N N 239 
LYS   CA  CB   sing N N 240 
LYS   CA  HA   sing N N 241 
LYS   C   O    doub N N 242 
LYS   C   OXT  sing N N 243 
LYS   CB  CG   sing N N 244 
LYS   CB  HB2  sing N N 245 
LYS   CB  HB3  sing N N 246 
LYS   CG  CD   sing N N 247 
LYS   CG  HG2  sing N N 248 
LYS   CG  HG3  sing N N 249 
LYS   CD  CE   sing N N 250 
LYS   CD  HD2  sing N N 251 
LYS   CD  HD3  sing N N 252 
LYS   CE  NZ   sing N N 253 
LYS   CE  HE2  sing N N 254 
LYS   CE  HE3  sing N N 255 
LYS   NZ  HZ1  sing N N 256 
LYS   NZ  HZ2  sing N N 257 
LYS   NZ  HZ3  sing N N 258 
LYS   OXT HXT  sing N N 259 
MET   N   CA   sing N N 260 
MET   N   H    sing N N 261 
MET   N   H2   sing N N 262 
MET   CA  C    sing N N 263 
MET   CA  CB   sing N N 264 
MET   CA  HA   sing N N 265 
MET   C   O    doub N N 266 
MET   C   OXT  sing N N 267 
MET   CB  CG   sing N N 268 
MET   CB  HB2  sing N N 269 
MET   CB  HB3  sing N N 270 
MET   CG  SD   sing N N 271 
MET   CG  HG2  sing N N 272 
MET   CG  HG3  sing N N 273 
MET   SD  CE   sing N N 274 
MET   CE  HE1  sing N N 275 
MET   CE  HE2  sing N N 276 
MET   CE  HE3  sing N N 277 
MET   OXT HXT  sing N N 278 
PHE   N   CA   sing N N 279 
PHE   N   H    sing N N 280 
PHE   N   H2   sing N N 281 
PHE   CA  C    sing N N 282 
PHE   CA  CB   sing N N 283 
PHE   CA  HA   sing N N 284 
PHE   C   O    doub N N 285 
PHE   C   OXT  sing N N 286 
PHE   CB  CG   sing N N 287 
PHE   CB  HB2  sing N N 288 
PHE   CB  HB3  sing N N 289 
PHE   CG  CD1  doub Y N 290 
PHE   CG  CD2  sing Y N 291 
PHE   CD1 CE1  sing Y N 292 
PHE   CD1 HD1  sing N N 293 
PHE   CD2 CE2  doub Y N 294 
PHE   CD2 HD2  sing N N 295 
PHE   CE1 CZ   doub Y N 296 
PHE   CE1 HE1  sing N N 297 
PHE   CE2 CZ   sing Y N 298 
PHE   CE2 HE2  sing N N 299 
PHE   CZ  HZ   sing N N 300 
PHE   OXT HXT  sing N N 301 
PRO   N   CA   sing N N 302 
PRO   N   CD   sing N N 303 
PRO   N   H    sing N N 304 
PRO   CA  C    sing N N 305 
PRO   CA  CB   sing N N 306 
PRO   CA  HA   sing N N 307 
PRO   C   O    doub N N 308 
PRO   C   OXT  sing N N 309 
PRO   CB  CG   sing N N 310 
PRO   CB  HB2  sing N N 311 
PRO   CB  HB3  sing N N 312 
PRO   CG  CD   sing N N 313 
PRO   CG  HG2  sing N N 314 
PRO   CG  HG3  sing N N 315 
PRO   CD  HD2  sing N N 316 
PRO   CD  HD3  sing N N 317 
PRO   OXT HXT  sing N N 318 
SER   N   CA   sing N N 319 
SER   N   H    sing N N 320 
SER   N   H2   sing N N 321 
SER   CA  C    sing N N 322 
SER   CA  CB   sing N N 323 
SER   CA  HA   sing N N 324 
SER   C   O    doub N N 325 
SER   C   OXT  sing N N 326 
SER   CB  OG   sing N N 327 
SER   CB  HB2  sing N N 328 
SER   CB  HB3  sing N N 329 
SER   OG  HG   sing N N 330 
SER   OXT HXT  sing N N 331 
SO4   S   O1   doub N N 332 
SO4   S   O2   doub N N 333 
SO4   S   O3   sing N N 334 
SO4   S   O4   sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TRP   N   CA   sing N N 352 
TRP   N   H    sing N N 353 
TRP   N   H2   sing N N 354 
TRP   CA  C    sing N N 355 
TRP   CA  CB   sing N N 356 
TRP   CA  HA   sing N N 357 
TRP   C   O    doub N N 358 
TRP   C   OXT  sing N N 359 
TRP   CB  CG   sing N N 360 
TRP   CB  HB2  sing N N 361 
TRP   CB  HB3  sing N N 362 
TRP   CG  CD1  doub Y N 363 
TRP   CG  CD2  sing Y N 364 
TRP   CD1 NE1  sing Y N 365 
TRP   CD1 HD1  sing N N 366 
TRP   CD2 CE2  doub Y N 367 
TRP   CD2 CE3  sing Y N 368 
TRP   NE1 CE2  sing Y N 369 
TRP   NE1 HE1  sing N N 370 
TRP   CE2 CZ2  sing Y N 371 
TRP   CE3 CZ3  doub Y N 372 
TRP   CE3 HE3  sing N N 373 
TRP   CZ2 CH2  doub Y N 374 
TRP   CZ2 HZ2  sing N N 375 
TRP   CZ3 CH2  sing Y N 376 
TRP   CZ3 HZ3  sing N N 377 
TRP   CH2 HH2  sing N N 378 
TRP   OXT HXT  sing N N 379 
TYR   N   CA   sing N N 380 
TYR   N   H    sing N N 381 
TYR   N   H2   sing N N 382 
TYR   CA  C    sing N N 383 
TYR   CA  CB   sing N N 384 
TYR   CA  HA   sing N N 385 
TYR   C   O    doub N N 386 
TYR   C   OXT  sing N N 387 
TYR   CB  CG   sing N N 388 
TYR   CB  HB2  sing N N 389 
TYR   CB  HB3  sing N N 390 
TYR   CG  CD1  doub Y N 391 
TYR   CG  CD2  sing Y N 392 
TYR   CD1 CE1  sing Y N 393 
TYR   CD1 HD1  sing N N 394 
TYR   CD2 CE2  doub Y N 395 
TYR   CD2 HD2  sing N N 396 
TYR   CE1 CZ   doub Y N 397 
TYR   CE1 HE1  sing N N 398 
TYR   CE2 CZ   sing Y N 399 
TYR   CE2 HE2  sing N N 400 
TYR   CZ  OH   sing N N 401 
TYR   OH  HH   sing N N 402 
TYR   OXT HXT  sing N N 403 
VAL   N   CA   sing N N 404 
VAL   N   H    sing N N 405 
VAL   N   H2   sing N N 406 
VAL   CA  C    sing N N 407 
VAL   CA  CB   sing N N 408 
VAL   CA  HA   sing N N 409 
VAL   C   O    doub N N 410 
VAL   C   OXT  sing N N 411 
VAL   CB  CG1  sing N N 412 
VAL   CB  CG2  sing N N 413 
VAL   CB  HB   sing N N 414 
VAL   CG1 HG11 sing N N 415 
VAL   CG1 HG12 sing N N 416 
VAL   CG1 HG13 sing N N 417 
VAL   CG2 HG21 sing N N 418 
VAL   CG2 HG22 sing N N 419 
VAL   CG2 HG23 sing N N 420 
VAL   OXT HXT  sing N N 421 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002322 
_pdbx_deposit_group.group_description   
'Crystallographic fragment screen of ZIKV NS2B-NS3 protease at the XChem facility of Diamond Light Source beamline I04-1' 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HOZ 
_atom_sites.fract_transf_matrix[1][1]   0.023502 
_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]   0.023502 
_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]   0.004623 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   A ASP   A 1 7   ? -20.690 19.084  -7.796  0.22 36.24  ? 50  ASP   A N   1 
ATOM   2    N N   B ASP   A 1 7   ? -20.690 19.084  -7.796  0.22 36.24  ? 50  ASP   A N   1 
ATOM   3    N N   C ASP   A 1 7   ? -22.819 18.999  -6.621  0.28 51.17  ? 50  ASP   A N   1 
ATOM   4    N N   D ASP   A 1 7   ? -22.819 19.000  -6.621  0.28 51.16  ? 50  ASP   A N   1 
ATOM   5    C CA  A ASP   A 1 7   ? -22.015 18.410  -7.799  0.22 35.66  ? 50  ASP   A CA  1 
ATOM   6    C CA  B ASP   A 1 7   ? -22.015 18.411  -7.799  0.22 35.66  ? 50  ASP   A CA  1 
ATOM   7    C CA  C ASP   A 1 7   ? -23.633 17.759  -6.767  0.28 51.00  ? 50  ASP   A CA  1 
ATOM   8    C CA  D ASP   A 1 7   ? -23.633 17.760  -6.767  0.28 50.99  ? 50  ASP   A CA  1 
ATOM   9    C C   A ASP   A 1 7   ? -22.218 17.692  -9.137  0.22 36.15  ? 50  ASP   A C   1 
ATOM   10   C C   B ASP   A 1 7   ? -22.218 17.692  -9.137  0.22 36.14  ? 50  ASP   A C   1 
ATOM   11   C C   C ASP   A 1 7   ? -23.473 17.246  -8.207  0.28 50.92  ? 50  ASP   A C   1 
ATOM   12   C C   D ASP   A 1 7   ? -23.473 17.246  -8.207  0.28 50.90  ? 50  ASP   A C   1 
ATOM   13   O O   A ASP   A 1 7   ? -22.057 18.345  -10.191 0.22 39.00  ? 50  ASP   A O   1 
ATOM   14   O O   B ASP   A 1 7   ? -22.057 18.344  -10.191 0.22 38.98  ? 50  ASP   A O   1 
ATOM   15   O O   C ASP   A 1 7   ? -24.134 17.791  -9.116  0.28 54.83  ? 50  ASP   A O   1 
ATOM   16   O O   D ASP   A 1 7   ? -24.134 17.792  -9.116  0.28 54.80  ? 50  ASP   A O   1 
ATOM   17   C CB  A ASP   A 1 7   ? -23.152 19.404  -7.552  0.22 35.23  ? 50  ASP   A CB  1 
ATOM   18   C CB  B ASP   A 1 7   ? -23.152 19.404  -7.552  0.22 35.23  ? 50  ASP   A CB  1 
ATOM   19   C CB  C ASP   A 1 7   ? -25.092 18.005  -6.355  0.28 50.82  ? 50  ASP   A CB  1 
ATOM   20   C CB  D ASP   A 1 7   ? -25.092 18.005  -6.355  0.28 50.80  ? 50  ASP   A CB  1 
ATOM   21   C CG  A ASP   A 1 7   ? -24.428 18.754  -7.043  0.22 33.57  ? 50  ASP   A CG  1 
ATOM   22   C CG  B ASP   A 1 7   ? -24.428 18.754  -7.043  0.22 33.57  ? 50  ASP   A CG  1 
ATOM   23   C CG  C ASP   A 1 7   ? -25.819 16.771  -5.840  0.28 48.52  ? 50  ASP   A CG  1 
ATOM   24   C CG  D ASP   A 1 7   ? -25.819 16.772  -5.841  0.28 48.53  ? 50  ASP   A CG  1 
ATOM   25   O OD1 A ASP   A 1 7   ? -24.448 18.355  -5.850  0.22 34.39  ? 50  ASP   A OD1 1 
ATOM   26   O OD1 B ASP   A 1 7   ? -24.448 18.355  -5.850  0.22 34.39  ? 50  ASP   A OD1 1 
ATOM   27   O OD1 C ASP   A 1 7   ? -26.392 16.847  -4.738  0.28 49.55  ? 50  ASP   A OD1 1 
ATOM   28   O OD1 D ASP   A 1 7   ? -26.392 16.847  -4.738  0.28 49.55  ? 50  ASP   A OD1 1 
ATOM   29   O OD2 A ASP   A 1 7   ? -25.394 18.655  -7.838  0.22 31.33  ? 50  ASP   A OD2 1 
ATOM   30   O OD2 B ASP   A 1 7   ? -25.394 18.655  -7.838  0.22 31.35  ? 50  ASP   A OD2 1 
ATOM   31   O OD2 C ASP   A 1 7   ? -25.822 15.750  -6.548  0.28 46.84  ? 50  ASP   A OD2 1 
ATOM   32   O OD2 D ASP   A 1 7   ? -25.821 15.750  -6.548  0.28 46.86  ? 50  ASP   A OD2 1 
ATOM   33   N N   A MET   A 1 8   ? -22.615 16.416  -9.086  0.22 33.95  ? 51  MET   A N   1 
ATOM   34   N N   B MET   A 1 8   ? -22.615 16.416  -9.086  0.22 33.95  ? 51  MET   A N   1 
ATOM   35   N N   C MET   A 1 8   ? -22.589 16.263  -8.406  0.28 47.60  ? 51  MET   A N   1 
ATOM   36   N N   D MET   A 1 8   ? -22.589 16.263  -8.406  0.28 47.59  ? 51  MET   A N   1 
ATOM   37   C CA  A MET   A 1 8   ? -22.654 15.499  -10.255 0.22 35.04  ? 51  MET   A CA  1 
ATOM   38   C CA  B MET   A 1 8   ? -22.654 15.499  -10.254 0.22 35.03  ? 51  MET   A CA  1 
ATOM   39   C CA  C MET   A 1 8   ? -22.323 15.623  -9.720  0.28 44.04  ? 51  MET   A CA  1 
ATOM   40   C CA  D MET   A 1 8   ? -22.323 15.623  -9.720  0.28 44.04  ? 51  MET   A CA  1 
ATOM   41   C C   A MET   A 1 8   ? -24.093 15.317  -10.741 0.22 31.86  ? 51  MET   A C   1 
ATOM   42   C C   B MET   A 1 8   ? -24.093 15.317  -10.741 0.22 31.86  ? 51  MET   A C   1 
ATOM   43   C C   C MET   A 1 8   ? -23.663 15.190  -10.325 0.28 41.25  ? 51  MET   A C   1 
ATOM   44   C C   D MET   A 1 8   ? -23.663 15.189  -10.325 0.28 41.25  ? 51  MET   A C   1 
ATOM   45   O O   A MET   A 1 8   ? -25.017 15.456  -9.919  0.22 31.34  ? 51  MET   A O   1 
ATOM   46   O O   B MET   A 1 8   ? -25.017 15.457  -9.919  0.22 31.35  ? 51  MET   A O   1 
ATOM   47   O O   C MET   A 1 8   ? -24.509 14.697  -9.559  0.28 40.08  ? 51  MET   A O   1 
ATOM   48   O O   D MET   A 1 8   ? -24.510 14.697  -9.559  0.28 40.09  ? 51  MET   A O   1 
ATOM   49   C CB  A MET   A 1 8   ? -22.088 14.121  -9.897  0.22 36.65  ? 51  MET   A CB  1 
ATOM   50   C CB  B MET   A 1 8   ? -22.088 14.121  -9.897  0.22 36.64  ? 51  MET   A CB  1 
ATOM   51   C CB  C MET   A 1 8   ? -21.412 14.398  -9.566  0.28 43.03  ? 51  MET   A CB  1 
ATOM   52   C CB  D MET   A 1 8   ? -21.413 14.398  -9.566  0.28 43.04  ? 51  MET   A CB  1 
ATOM   53   C CG  A MET   A 1 8   ? -20.591 14.075  -9.883  0.22 36.36  ? 51  MET   A CG  1 
ATOM   54   C CG  B MET   A 1 8   ? -20.591 14.075  -9.883  0.22 36.36  ? 51  MET   A CG  1 
ATOM   55   C CG  C MET   A 1 8   ? -19.982 14.736  -9.206  0.28 43.04  ? 51  MET   A CG  1 
ATOM   56   C CG  D MET   A 1 8   ? -19.982 14.736  -9.206  0.28 43.05  ? 51  MET   A CG  1 
ATOM   57   S SD  A MET   A 1 8   ? -19.986 12.460  -9.339  0.22 36.93  ? 51  MET   A SD  1 
ATOM   58   S SD  B MET   A 1 8   ? -19.985 12.460  -9.339  0.22 36.93  ? 51  MET   A SD  1 
ATOM   59   S SD  C MET   A 1 8   ? -18.970 13.247  -8.948  0.28 44.74  ? 51  MET   A SD  1 
ATOM   60   S SD  D MET   A 1 8   ? -18.970 13.247  -8.948  0.28 44.73  ? 51  MET   A SD  1 
ATOM   61   C CE  A MET   A 1 8   ? -18.234 12.825  -9.242  0.22 38.04  ? 51  MET   A CE  1 
ATOM   62   C CE  B MET   A 1 8   ? -18.234 12.825  -9.242  0.22 38.03  ? 51  MET   A CE  1 
ATOM   63   C CE  C MET   A 1 8   ? -17.321 13.951  -8.956  0.28 46.23  ? 51  MET   A CE  1 
ATOM   64   C CE  D MET   A 1 8   ? -17.321 13.951  -8.956  0.28 46.21  ? 51  MET   A CE  1 
ATOM   65   N N   A TYR   A 1 9   ? -24.246 14.975  -12.023 0.22 28.75  ? 52  TYR   A N   1 
ATOM   66   N N   B TYR   A 1 9   ? -24.246 14.975  -12.023 0.22 28.76  ? 52  TYR   A N   1 
ATOM   67   N N   C TYR   A 1 9   ? -23.838 15.372  -11.637 0.28 35.90  ? 52  TYR   A N   1 
ATOM   68   N N   D TYR   A 1 9   ? -23.838 15.372  -11.638 0.28 35.93  ? 52  TYR   A N   1 
ATOM   69   C CA  A TYR   A 1 9   ? -25.542 14.692  -12.688 0.22 29.36  ? 52  TYR   A CA  1 
ATOM   70   C CA  B TYR   A 1 9   ? -25.542 14.692  -12.688 0.22 29.36  ? 52  TYR   A CA  1 
ATOM   71   C CA  C TYR   A 1 9   ? -25.085 15.061  -12.383 0.28 36.37  ? 52  TYR   A CA  1 
ATOM   72   C CA  D TYR   A 1 9   ? -25.085 15.061  -12.384 0.28 36.39  ? 52  TYR   A CA  1 
ATOM   73   C C   A TYR   A 1 9   ? -25.342 13.693  -13.837 0.22 29.68  ? 52  TYR   A C   1 
ATOM   74   C C   B TYR   A 1 9   ? -25.342 13.694  -13.837 0.22 29.68  ? 52  TYR   A C   1 
ATOM   75   C C   C TYR   A 1 9   ? -24.773 14.106  -13.540 0.28 36.07  ? 52  TYR   A C   1 
ATOM   76   C C   D TYR   A 1 9   ? -24.774 14.106  -13.540 0.28 36.08  ? 52  TYR   A C   1 
ATOM   77   O O   A TYR   A 1 9   ? -24.201 13.507  -14.307 0.22 27.49  ? 52  TYR   A O   1 
ATOM   78   O O   B TYR   A 1 9   ? -24.201 13.507  -14.306 0.22 27.50  ? 52  TYR   A O   1 
ATOM   79   O O   C TYR   A 1 9   ? -23.627 14.091  -14.017 0.28 38.74  ? 52  TYR   A O   1 
ATOM   80   O O   D TYR   A 1 9   ? -23.627 14.091  -14.017 0.28 38.73  ? 52  TYR   A O   1 
ATOM   81   C CB  A TYR   A 1 9   ? -26.185 16.000  -13.169 0.22 28.49  ? 52  TYR   A CB  1 
ATOM   82   C CB  B TYR   A 1 9   ? -26.185 16.000  -13.169 0.22 28.49  ? 52  TYR   A CB  1 
ATOM   83   C CB  C TYR   A 1 9   ? -25.758 16.352  -12.868 0.28 36.12  ? 52  TYR   A CB  1 
ATOM   84   C CB  D TYR   A 1 9   ? -25.759 16.352  -12.868 0.28 36.13  ? 52  TYR   A CB  1 
ATOM   85   C CG  A TYR   A 1 9   ? -25.267 16.880  -13.975 0.22 26.66  ? 52  TYR   A CG  1 
ATOM   86   C CG  B TYR   A 1 9   ? -25.267 16.880  -13.975 0.22 26.67  ? 52  TYR   A CG  1 
ATOM   87   C CG  C TYR   A 1 9   ? -25.153 16.995  -14.089 0.28 35.21  ? 52  TYR   A CG  1 
ATOM   88   C CG  D TYR   A 1 9   ? -25.153 16.995  -14.089 0.28 35.22  ? 52  TYR   A CG  1 
ATOM   89   C CD1 A TYR   A 1 9   ? -24.320 17.687  -13.367 0.22 26.96  ? 52  TYR   A CD1 1 
ATOM   90   C CD1 B TYR   A 1 9   ? -24.320 17.687  -13.367 0.22 26.97  ? 52  TYR   A CD1 1 
ATOM   91   C CD1 C TYR   A 1 9   ? -25.596 16.686  -15.367 0.28 36.64  ? 52  TYR   A CD1 1 
ATOM   92   C CD1 D TYR   A 1 9   ? -25.596 16.686  -15.367 0.28 36.64  ? 52  TYR   A CD1 1 
ATOM   93   C CD2 A TYR   A 1 9   ? -25.330 16.885  -15.356 0.22 26.97  ? 52  TYR   A CD2 1 
ATOM   94   C CD2 B TYR   A 1 9   ? -25.330 16.886  -15.356 0.22 26.97  ? 52  TYR   A CD2 1 
ATOM   95   C CD2 C TYR   A 1 9   ? -24.140 17.930  -13.968 0.28 36.33  ? 52  TYR   A CD2 1 
ATOM   96   C CD2 D TYR   A 1 9   ? -24.140 17.930  -13.968 0.28 36.33  ? 52  TYR   A CD2 1 
ATOM   97   C CE1 A TYR   A 1 9   ? -23.450 18.470  -14.113 0.22 26.46  ? 52  TYR   A CE1 1 
ATOM   98   C CE1 B TYR   A 1 9   ? -23.450 18.470  -14.113 0.22 26.46  ? 52  TYR   A CE1 1 
ATOM   99   C CE1 C TYR   A 1 9   ? -25.039 17.283  -16.491 0.28 37.82  ? 52  TYR   A CE1 1 
ATOM   100  C CE1 D TYR   A 1 9   ? -25.039 17.283  -16.491 0.28 37.81  ? 52  TYR   A CE1 1 
ATOM   101  C CE2 A TYR   A 1 9   ? -24.480 17.673  -16.116 0.22 26.59  ? 52  TYR   A CE2 1 
ATOM   102  C CE2 B TYR   A 1 9   ? -24.480 17.673  -16.116 0.22 26.59  ? 52  TYR   A CE2 1 
ATOM   103  C CE2 C TYR   A 1 9   ? -23.574 18.537  -15.076 0.28 36.38  ? 52  TYR   A CE2 1 
ATOM   104  C CE2 D TYR   A 1 9   ? -23.574 18.537  -15.076 0.28 36.39  ? 52  TYR   A CE2 1 
ATOM   105  C CZ  A TYR   A 1 9   ? -23.542 18.475  -15.495 0.22 26.16  ? 52  TYR   A CZ  1 
ATOM   106  C CZ  B TYR   A 1 9   ? -23.542 18.475  -15.496 0.22 26.16  ? 52  TYR   A CZ  1 
ATOM   107  C CZ  C TYR   A 1 9   ? -24.023 18.215  -16.344 0.28 36.57  ? 52  TYR   A CZ  1 
ATOM   108  C CZ  D TYR   A 1 9   ? -24.023 18.215  -16.344 0.28 36.57  ? 52  TYR   A CZ  1 
ATOM   109  O OH  A TYR   A 1 9   ? -22.717 19.233  -16.280 0.22 24.93  ? 52  TYR   A OH  1 
ATOM   110  O OH  B TYR   A 1 9   ? -22.717 19.234  -16.279 0.22 24.94  ? 52  TYR   A OH  1 
ATOM   111  O OH  C TYR   A 1 9   ? -23.459 18.819  -17.432 0.28 37.13  ? 52  TYR   A OH  1 
ATOM   112  O OH  D TYR   A 1 9   ? -23.459 18.819  -17.432 0.28 37.13  ? 52  TYR   A OH  1 
ATOM   113  N N   A ILE   A 1 10  ? -26.438 13.081  -14.297 0.22 31.67  ? 53  ILE   A N   1 
ATOM   114  N N   B ILE   A 1 10  ? -26.438 13.081  -14.297 0.22 31.66  ? 53  ILE   A N   1 
ATOM   115  N N   C ILE   A 1 10  ? -25.782 13.344  -13.975 0.28 37.72  ? 53  ILE   A N   1 
ATOM   116  N N   D ILE   A 1 10  ? -25.782 13.344  -13.975 0.28 37.72  ? 53  ILE   A N   1 
ATOM   117  C CA  A ILE   A 1 10  ? -26.428 12.049  -15.377 0.22 31.13  ? 53  ILE   A CA  1 
ATOM   118  C CA  B ILE   A 1 10  ? -26.428 12.049  -15.377 0.22 31.13  ? 53  ILE   A CA  1 
ATOM   119  C CA  C ILE   A 1 10  ? -25.697 12.368  -15.104 0.28 36.15  ? 53  ILE   A CA  1 
ATOM   120  C CA  D ILE   A 1 10  ? -25.697 12.368  -15.105 0.28 36.16  ? 53  ILE   A CA  1 
ATOM   121  C C   A ILE   A 1 10  ? -27.215 12.550  -16.596 0.22 32.51  ? 53  ILE   A C   1 
ATOM   122  C C   B ILE   A 1 10  ? -27.215 12.550  -16.596 0.22 32.51  ? 53  ILE   A C   1 
ATOM   123  C C   C ILE   A 1 10  ? -26.484 12.900  -16.314 0.28 37.16  ? 53  ILE   A C   1 
ATOM   124  C C   D ILE   A 1 10  ? -26.484 12.900  -16.314 0.28 37.16  ? 53  ILE   A C   1 
ATOM   125  O O   A ILE   A 1 10  ? -28.162 13.354  -16.442 0.22 30.30  ? 53  ILE   A O   1 
ATOM   126  O O   B ILE   A 1 10  ? -28.161 13.354  -16.441 0.22 30.31  ? 53  ILE   A O   1 
ATOM   127  O O   C ILE   A 1 10  ? -27.426 13.682  -16.093 0.28 35.21  ? 53  ILE   A O   1 
ATOM   128  O O   D ILE   A 1 10  ? -27.427 13.682  -16.093 0.28 35.22  ? 53  ILE   A O   1 
ATOM   129  C CB  A ILE   A 1 10  ? -26.947 10.684  -14.872 0.22 31.01  ? 53  ILE   A CB  1 
ATOM   130  C CB  B ILE   A 1 10  ? -26.947 10.684  -14.872 0.22 31.02  ? 53  ILE   A CB  1 
ATOM   131  C CB  C ILE   A 1 10  ? -26.186 10.970  -14.659 0.28 37.07  ? 53  ILE   A CB  1 
ATOM   132  C CB  D ILE   A 1 10  ? -26.186 10.970  -14.659 0.28 37.07  ? 53  ILE   A CB  1 
ATOM   133  C CG1 A ILE   A 1 10  ? -28.408 10.733  -14.425 0.22 32.15  ? 53  ILE   A CG1 1 
ATOM   134  C CG1 B ILE   A 1 10  ? -28.408 10.733  -14.425 0.22 32.15  ? 53  ILE   A CG1 1 
ATOM   135  C CG1 C ILE   A 1 10  ? -27.637 10.968  -14.177 0.28 36.97  ? 53  ILE   A CG1 1 
ATOM   136  C CG1 D ILE   A 1 10  ? -27.637 10.968  -14.177 0.28 36.98  ? 53  ILE   A CG1 1 
ATOM   137  C CG2 A ILE   A 1 10  ? -26.053 10.134  -13.771 0.22 31.23  ? 53  ILE   A CG2 1 
ATOM   138  C CG2 B ILE   A 1 10  ? -26.052 10.134  -13.771 0.22 31.23  ? 53  ILE   A CG2 1 
ATOM   139  C CG2 C ILE   A 1 10  ? -25.260 10.383  -13.601 0.28 37.54  ? 53  ILE   A CG2 1 
ATOM   140  C CG2 D ILE   A 1 10  ? -25.260 10.383  -13.601 0.28 37.53  ? 53  ILE   A CG2 1 
ATOM   141  C CD1 A ILE   A 1 10  ? -29.039 9.364   -14.266 0.22 33.03  ? 53  ILE   A CD1 1 
ATOM   142  C CD1 B ILE   A 1 10  ? -29.039 9.364   -14.266 0.22 33.03  ? 53  ILE   A CD1 1 
ATOM   143  C CD1 C ILE   A 1 10  ? -28.196 9.580   -13.954 0.28 38.70  ? 53  ILE   A CD1 1 
ATOM   144  C CD1 D ILE   A 1 10  ? -28.196 9.580   -13.954 0.28 38.69  ? 53  ILE   A CD1 1 
ATOM   145  N N   A GLU   A 1 11  ? -26.813 12.074  -17.772 0.22 32.33  ? 54  GLU   A N   1 
ATOM   146  N N   B GLU   A 1 11  ? -26.813 12.074  -17.772 0.22 32.34  ? 54  GLU   A N   1 
ATOM   147  N N   C GLU   A 1 11  ? -26.098 12.497  -17.536 0.28 35.97  ? 54  GLU   A N   1 
ATOM   148  N N   D GLU   A 1 11  ? -26.098 12.497  -17.536 0.28 35.99  ? 54  GLU   A N   1 
ATOM   149  C CA  A GLU   A 1 11  ? -27.443 12.365  -19.088 0.22 34.49  ? 54  GLU   A CA  1 
ATOM   150  C CA  B GLU   A 1 11  ? -27.443 12.365  -19.087 0.22 34.49  ? 54  GLU   A CA  1 
ATOM   151  C CA  C GLU   A 1 11  ? -26.848 12.723  -18.812 0.28 38.37  ? 54  GLU   A CA  1 
ATOM   152  C CA  D GLU   A 1 11  ? -26.848 12.723  -18.813 0.28 38.36  ? 54  GLU   A CA  1 
ATOM   153  C C   A GLU   A 1 11  ? -27.346 11.102  -19.946 0.22 33.74  ? 54  GLU   A C   1 
ATOM   154  C C   B GLU   A 1 11  ? -27.346 11.102  -19.946 0.22 33.74  ? 54  GLU   A C   1 
ATOM   155  C C   C GLU   A 1 11  ? -26.952 11.396  -19.584 0.28 37.33  ? 54  GLU   A C   1 
ATOM   156  C C   D GLU   A 1 11  ? -26.952 11.395  -19.584 0.28 37.34  ? 54  GLU   A C   1 
ATOM   157  O O   A GLU   A 1 11  ? -26.251 10.502  -19.993 0.22 32.58  ? 54  GLU   A O   1 
ATOM   158  O O   B GLU   A 1 11  ? -26.251 10.503  -19.993 0.22 32.59  ? 54  GLU   A O   1 
ATOM   159  O O   C GLU   A 1 11  ? -25.927 10.698  -19.677 0.28 36.19  ? 54  GLU   A O   1 
ATOM   160  O O   D GLU   A 1 11  ? -25.927 10.698  -19.676 0.28 36.20  ? 54  GLU   A O   1 
ATOM   161  C CB  A GLU   A 1 11  ? -26.738 13.546  -19.759 0.22 37.06  ? 54  GLU   A CB  1 
ATOM   162  C CB  B GLU   A 1 11  ? -26.738 13.546  -19.759 0.22 37.06  ? 54  GLU   A CB  1 
ATOM   163  C CB  C GLU   A 1 11  ? -26.149 13.718  -19.746 0.28 38.65  ? 54  GLU   A CB  1 
ATOM   164  C CB  D GLU   A 1 11  ? -26.148 13.718  -19.746 0.28 38.66  ? 54  GLU   A CB  1 
ATOM   165  C CG  A GLU   A 1 11  ? -27.227 14.895  -19.282 0.22 39.36  ? 54  GLU   A CG  1 
ATOM   166  C CG  B GLU   A 1 11  ? -27.227 14.895  -19.282 0.22 39.36  ? 54  GLU   A CG  1 
ATOM   167  C CG  C GLU   A 1 11  ? -25.713 15.029  -19.122 0.28 40.08  ? 54  GLU   A CG  1 
ATOM   168  C CG  D GLU   A 1 11  ? -25.713 15.028  -19.122 0.28 40.07  ? 54  GLU   A CG  1 
ATOM   169  C CD  A GLU   A 1 11  ? -26.322 16.044  -19.674 0.22 41.55  ? 54  GLU   A CD  1 
ATOM   170  C CD  B GLU   A 1 11  ? -26.322 16.044  -19.674 0.22 41.55  ? 54  GLU   A CD  1 
ATOM   171  C CD  C GLU   A 1 11  ? -24.911 15.915  -20.072 0.28 41.65  ? 54  GLU   A CD  1 
ATOM   172  C CD  D GLU   A 1 11  ? -24.911 15.915  -20.072 0.28 41.62  ? 54  GLU   A CD  1 
ATOM   173  O OE1 A GLU   A 1 11  ? -25.962 16.137  -20.868 0.22 43.21  ? 54  GLU   A OE1 1 
ATOM   174  O OE1 B GLU   A 1 11  ? -25.962 16.137  -20.868 0.22 43.20  ? 54  GLU   A OE1 1 
ATOM   175  O OE1 C GLU   A 1 11  ? -24.153 15.360  -20.909 0.28 39.14  ? 54  GLU   A OE1 1 
ATOM   176  O OE1 D GLU   A 1 11  ? -24.153 15.360  -20.909 0.28 39.14  ? 54  GLU   A OE1 1 
ATOM   177  O OE2 A GLU   A 1 11  ? -25.955 16.822  -18.775 0.22 47.28  ? 54  GLU   A OE2 1 
ATOM   178  O OE2 B GLU   A 1 11  ? -25.955 16.822  -18.775 0.22 47.25  ? 54  GLU   A OE2 1 
ATOM   179  O OE2 C GLU   A 1 11  ? -25.036 17.163  -19.980 0.28 38.78  ? 54  GLU   A OE2 1 
ATOM   180  O OE2 D GLU   A 1 11  ? -25.036 17.163  -19.979 0.28 38.79  ? 54  GLU   A OE2 1 
ATOM   181  N N   A ARG   A 1 12  ? -28.456 10.689  -20.562 0.22 34.48  ? 55  ARG   A N   1 
ATOM   182  N N   B ARG   A 1 12  ? -28.455 10.689  -20.562 0.22 34.48  ? 55  ARG   A N   1 
ATOM   183  N N   C ARG   A 1 12  ? -28.118 11.060  -20.150 0.28 38.66  ? 55  ARG   A N   1 
ATOM   184  N N   D ARG   A 1 12  ? -28.118 11.059  -20.150 0.28 38.66  ? 55  ARG   A N   1 
ATOM   185  C CA  A ARG   A 1 12  ? -28.495 9.494   -21.440 0.22 34.52  ? 55  ARG   A CA  1 
ATOM   186  C CA  B ARG   A 1 12  ? -28.494 9.494   -21.439 0.22 34.52  ? 55  ARG   A CA  1 
ATOM   187  C CA  C ARG   A 1 12  ? -28.322 9.776   -20.885 0.28 37.85  ? 55  ARG   A CA  1 
ATOM   188  C CA  D ARG   A 1 12  ? -28.322 9.775   -20.885 0.28 37.86  ? 55  ARG   A CA  1 
ATOM   189  C C   A ARG   A 1 12  ? -27.580 9.760   -22.644 0.22 34.66  ? 55  ARG   A C   1 
ATOM   190  C C   B ARG   A 1 12  ? -27.580 9.760   -22.644 0.22 34.66  ? 55  ARG   A C   1 
ATOM   191  C C   C ARG   A 1 12  ? -27.497 9.782   -22.182 0.28 37.46  ? 55  ARG   A C   1 
ATOM   192  C C   D ARG   A 1 12  ? -27.497 9.782   -22.182 0.28 37.46  ? 55  ARG   A C   1 
ATOM   193  O O   A ARG   A 1 12  ? -27.928 10.641  -23.446 0.22 35.00  ? 55  ARG   A O   1 
ATOM   194  O O   B ARG   A 1 12  ? -27.928 10.641  -23.446 0.22 35.00  ? 55  ARG   A O   1 
ATOM   195  O O   C ARG   A 1 12  ? -27.075 10.894  -22.594 0.28 36.11  ? 55  ARG   A O   1 
ATOM   196  O O   D ARG   A 1 12  ? -27.076 10.894  -22.594 0.28 36.12  ? 55  ARG   A O   1 
ATOM   197  C CB  A ARG   A 1 12  ? -29.945 9.187   -21.819 0.22 35.96  ? 55  ARG   A CB  1 
ATOM   198  C CB  B ARG   A 1 12  ? -29.945 9.187   -21.819 0.22 35.96  ? 55  ARG   A CB  1 
ATOM   199  C CB  C ARG   A 1 12  ? -29.806 9.519   -21.148 0.28 39.99  ? 55  ARG   A CB  1 
ATOM   200  C CB  D ARG   A 1 12  ? -29.805 9.519   -21.148 0.28 40.00  ? 55  ARG   A CB  1 
ATOM   201  C CG  A ARG   A 1 12  ? -30.188 7.745   -22.233 0.22 36.52  ? 55  ARG   A CG  1 
ATOM   202  C CG  B ARG   A 1 12  ? -30.188 7.745   -22.233 0.22 36.52  ? 55  ARG   A CG  1 
ATOM   203  C CG  C ARG   A 1 12  ? -30.082 8.146   -21.743 0.28 43.18  ? 55  ARG   A CG  1 
ATOM   204  C CG  D ARG   A 1 12  ? -30.082 8.146   -21.743 0.28 43.18  ? 55  ARG   A CG  1 
ATOM   205  C CD  A ARG   A 1 12  ? -31.660 7.464   -22.454 0.22 37.73  ? 55  ARG   A CD  1 
ATOM   206  C CD  B ARG   A 1 12  ? -31.660 7.465   -22.454 0.22 37.73  ? 55  ARG   A CD  1 
ATOM   207  C CD  C ARG   A 1 12  ? -31.493 7.646   -21.511 0.28 46.62  ? 55  ARG   A CD  1 
ATOM   208  C CD  D ARG   A 1 12  ? -31.493 7.646   -21.512 0.28 46.61  ? 55  ARG   A CD  1 
ATOM   209  N NE  A ARG   A 1 12  ? -31.970 6.046   -22.571 0.22 40.01  ? 55  ARG   A NE  1 
ATOM   210  N NE  B ARG   A 1 12  ? -31.970 6.046   -22.571 0.22 39.99  ? 55  ARG   A NE  1 
ATOM   211  N NE  C ARG   A 1 12  ? -31.623 6.264   -21.936 0.28 48.91  ? 55  ARG   A NE  1 
ATOM   212  N NE  D ARG   A 1 12  ? -31.623 6.264   -21.936 0.28 48.90  ? 55  ARG   A NE  1 
ATOM   213  C CZ  A ARG   A 1 12  ? -31.596 5.264   -23.584 0.22 39.16  ? 55  ARG   A CZ  1 
ATOM   214  C CZ  B ARG   A 1 12  ? -31.596 5.264   -23.584 0.22 39.16  ? 55  ARG   A CZ  1 
ATOM   215  C CZ  C ARG   A 1 12  ? -31.657 5.868   -23.207 0.28 52.76  ? 55  ARG   A CZ  1 
ATOM   216  C CZ  D ARG   A 1 12  ? -31.657 5.867   -23.207 0.28 52.73  ? 55  ARG   A CZ  1 
ATOM   217  N NH1 A ARG   A 1 12  ? -30.880 5.747   -24.585 0.22 39.74  ? 55  ARG   A NH1 1 
ATOM   218  N NH1 B ARG   A 1 12  ? -30.880 5.747   -24.585 0.22 39.73  ? 55  ARG   A NH1 1 
ATOM   219  N NH1 C ARG   A 1 12  ? -31.598 6.754   -24.189 0.28 54.41  ? 55  ARG   A NH1 1 
ATOM   220  N NH1 D ARG   A 1 12  ? -31.598 6.753   -24.189 0.28 54.38  ? 55  ARG   A NH1 1 
ATOM   221  N NH2 A ARG   A 1 12  ? -31.942 3.988   -23.598 0.22 39.51  ? 55  ARG   A NH2 1 
ATOM   222  N NH2 B ARG   A 1 12  ? -31.942 3.988   -23.598 0.22 39.51  ? 55  ARG   A NH2 1 
ATOM   223  N NH2 C ARG   A 1 12  ? -31.756 4.581   -23.497 0.28 54.11  ? 55  ARG   A NH2 1 
ATOM   224  N NH2 D ARG   A 1 12  ? -31.756 4.581   -23.496 0.28 54.08  ? 55  ARG   A NH2 1 
ATOM   225  N N   A ALA   A 1 13  ? -26.424 9.072   -22.722 0.22 33.34  ? 56  ALA   A N   1 
ATOM   226  N N   B ALA   A 1 13  ? -26.424 9.072   -22.722 0.22 33.33  ? 56  ALA   A N   1 
ATOM   227  N N   C ALA   A 1 13  ? -27.216 8.593   -22.762 0.28 35.32  ? 56  ALA   A N   1 
ATOM   228  N N   D ALA   A 1 13  ? -27.215 8.593   -22.762 0.28 35.31  ? 56  ALA   A N   1 
ATOM   229  C CA  A ALA   A 1 13  ? -25.433 9.154   -23.829 0.22 29.84  ? 56  ALA   A CA  1 
ATOM   230  C CA  B ALA   A 1 13  ? -25.433 9.155   -23.829 0.22 29.84  ? 56  ALA   A CA  1 
ATOM   231  C CA  C ALA   A 1 13  ? -26.239 8.416   -23.873 0.28 31.84  ? 56  ALA   A CA  1 
ATOM   232  C CA  D ALA   A 1 13  ? -26.239 8.416   -23.873 0.28 31.86  ? 56  ALA   A CA  1 
ATOM   233  C C   A ALA   A 1 13  ? -25.748 8.102   -24.896 0.22 27.92  ? 56  ALA   A C   1 
ATOM   234  C C   B ALA   A 1 13  ? -25.748 8.102   -24.896 0.22 27.93  ? 56  ALA   A C   1 
ATOM   235  C C   C ALA   A 1 13  ? -26.620 7.314   -24.871 0.28 30.06  ? 56  ALA   A C   1 
ATOM   236  C C   D ALA   A 1 13  ? -26.620 7.314   -24.871 0.28 30.07  ? 56  ALA   A C   1 
ATOM   237  O O   A ALA   A 1 13  ? -25.066 8.106   -25.957 0.22 28.40  ? 56  ALA   A O   1 
ATOM   238  O O   B ALA   A 1 13  ? -25.066 8.107   -25.957 0.22 28.41  ? 56  ALA   A O   1 
ATOM   239  O O   C ALA   A 1 13  ? -26.010 7.319   -25.954 0.28 31.33  ? 56  ALA   A O   1 
ATOM   240  O O   D ALA   A 1 13  ? -26.011 7.319   -25.954 0.28 31.33  ? 56  ALA   A O   1 
ATOM   241  C CB  A ALA   A 1 13  ? -24.021 8.979   -23.310 0.22 30.37  ? 56  ALA   A CB  1 
ATOM   242  C CB  B ALA   A 1 13  ? -24.022 8.979   -23.310 0.22 30.37  ? 56  ALA   A CB  1 
ATOM   243  C CB  C ALA   A 1 13  ? -24.855 8.161   -23.329 0.28 34.88  ? 56  ALA   A CB  1 
ATOM   244  C CB  D ALA   A 1 13  ? -24.855 8.161   -23.328 0.28 34.87  ? 56  ALA   A CB  1 
ATOM   245  N N   A GLY   A 1 14  ? -26.712 7.218   -24.622 0.22 25.68  ? 57  GLY   A N   1 
ATOM   246  N N   B GLY   A 1 14  ? -26.712 7.218   -24.622 0.22 25.70  ? 57  GLY   A N   1 
ATOM   247  N N   C GLY   A 1 14  ? -27.548 6.400   -24.571 0.28 27.81  ? 57  GLY   A N   1 
ATOM   248  N N   D GLY   A 1 14  ? -27.547 6.399   -24.571 0.28 27.83  ? 57  GLY   A N   1 
ATOM   249  C CA  A GLY   A 1 14  ? -27.236 6.258   -25.611 0.22 25.26  ? 57  GLY   A CA  1 
ATOM   250  C CA  B GLY   A 1 14  ? -27.236 6.259   -25.612 0.22 25.28  ? 57  GLY   A CA  1 
ATOM   251  C CA  C GLY   A 1 14  ? -27.947 5.385   -25.564 0.28 28.68  ? 57  GLY   A CA  1 
ATOM   252  C CA  D GLY   A 1 14  ? -27.948 5.384   -25.564 0.28 28.70  ? 57  GLY   A CA  1 
ATOM   253  C C   A GLY   A 1 14  ? -27.797 5.004   -24.975 0.22 24.87  ? 57  GLY   A C   1 
ATOM   254  C C   B GLY   A 1 14  ? -27.798 5.005   -24.976 0.22 24.90  ? 57  GLY   A C   1 
ATOM   255  C C   C GLY   A 1 14  ? -28.654 4.168   -24.993 0.28 31.74  ? 57  GLY   A C   1 
ATOM   256  C C   D GLY   A 1 14  ? -28.653 4.167   -24.994 0.28 31.74  ? 57  GLY   A C   1 
ATOM   257  O O   A GLY   A 1 14  ? -27.751 4.895   -23.717 0.22 24.25  ? 57  GLY   A O   1 
ATOM   258  O O   B GLY   A 1 14  ? -27.751 4.896   -23.719 0.22 24.27  ? 57  GLY   A O   1 
ATOM   259  O O   C GLY   A 1 14  ? -28.737 4.031   -23.748 0.28 31.52  ? 57  GLY   A O   1 
ATOM   260  O O   D GLY   A 1 14  ? -28.737 4.031   -23.748 0.28 31.51  ? 57  GLY   A O   1 
ATOM   261  N N   A ASP   A 1 15  ? -28.308 4.098   -25.822 0.22 27.06  ? 58  ASP   A N   1 
ATOM   262  N N   B ASP   A 1 15  ? -28.310 4.100   -25.823 0.22 27.10  ? 58  ASP   A N   1 
ATOM   263  N N   C ASP   A 1 15  ? -29.157 3.319   -25.901 0.28 33.13  ? 58  ASP   A N   1 
ATOM   264  N N   D ASP   A 1 15  ? -29.154 3.317   -25.901 0.28 33.14  ? 58  ASP   A N   1 
ATOM   265  C CA  A ASP   A 1 15  ? -28.792 2.739   -25.455 0.22 28.29  ? 58  ASP   A CA  1 
ATOM   266  C CA  B ASP   A 1 15  ? -28.794 2.741   -25.455 0.22 28.34  ? 58  ASP   A CA  1 
ATOM   267  C CA  C ASP   A 1 15  ? -29.678 1.957   -25.620 0.28 34.84  ? 58  ASP   A CA  1 
ATOM   268  C CA  D ASP   A 1 15  ? -29.674 1.953   -25.621 0.28 34.84  ? 58  ASP   A CA  1 
ATOM   269  C C   A ASP   A 1 15  ? -27.596 1.797   -25.283 0.22 29.52  ? 58  ASP   A C   1 
ATOM   270  C C   B ASP   A 1 15  ? -27.597 1.801   -25.286 0.22 29.64  ? 58  ASP   A C   1 
ATOM   271  C C   C ASP   A 1 15  ? -28.494 0.995   -25.491 0.28 35.11  ? 58  ASP   A C   1 
ATOM   272  C C   D ASP   A 1 15  ? -28.488 0.992   -25.496 0.28 35.13  ? 58  ASP   A C   1 
ATOM   273  O O   A ASP   A 1 15  ? -26.481 2.152   -25.727 0.22 29.49  ? 58  ASP   A O   1 
ATOM   274  O O   B ASP   A 1 15  ? -26.482 2.157   -25.729 0.22 29.56  ? 58  ASP   A O   1 
ATOM   275  O O   C ASP   A 1 15  ? -27.493 1.189   -26.211 0.28 35.67  ? 58  ASP   A O   1 
ATOM   276  O O   D ASP   A 1 15  ? -27.487 1.189   -26.213 0.28 35.68  ? 58  ASP   A O   1 
ATOM   277  C CB  A ASP   A 1 15  ? -29.669 2.092   -26.534 0.22 29.13  ? 58  ASP   A CB  1 
ATOM   278  C CB  B ASP   A 1 15  ? -29.675 2.094   -26.530 0.22 29.16  ? 58  ASP   A CB  1 
ATOM   279  C CB  C ASP   A 1 15  ? -30.585 1.436   -26.739 0.28 34.21  ? 58  ASP   A CB  1 
ATOM   280  C CB  D ASP   A 1 15  ? -30.582 1.435   -26.739 0.28 34.22  ? 58  ASP   A CB  1 
ATOM   281  C CG  A ASP   A 1 15  ? -30.912 2.854   -26.935 0.22 29.81  ? 58  ASP   A CG  1 
ATOM   282  C CG  B ASP   A 1 15  ? -30.916 2.858   -26.935 0.22 29.83  ? 58  ASP   A CG  1 
ATOM   283  C CG  C ASP   A 1 15  ? -31.976 2.034   -26.721 0.28 35.65  ? 58  ASP   A CG  1 
ATOM   284  C CG  D ASP   A 1 15  ? -31.974 2.033   -26.719 0.28 35.64  ? 58  ASP   A CG  1 
ATOM   285  O OD1 A ASP   A 1 15  ? -31.315 3.775   -26.190 0.22 29.29  ? 58  ASP   A OD1 1 
ATOM   286  O OD1 B ASP   A 1 15  ? -31.321 3.778   -26.190 0.22 29.30  ? 58  ASP   A OD1 1 
ATOM   287  O OD1 C ASP   A 1 15  ? -32.193 2.966   -25.922 0.28 36.57  ? 58  ASP   A OD1 1 
ATOM   288  O OD1 D ASP   A 1 15  ? -32.189 2.965   -25.920 0.28 36.56  ? 58  ASP   A OD1 1 
ATOM   289  O OD2 A ASP   A 1 15  ? -31.468 2.508   -27.995 0.22 29.92  ? 58  ASP   A OD2 1 
ATOM   290  O OD2 B ASP   A 1 15  ? -31.472 2.511   -27.996 0.22 29.93  ? 58  ASP   A OD2 1 
ATOM   291  O OD2 C ASP   A 1 15  ? -32.828 1.560   -27.504 0.28 32.80  ? 58  ASP   A OD2 1 
ATOM   292  O OD2 D ASP   A 1 15  ? -32.826 1.561   -27.502 0.28 32.81  ? 58  ASP   A OD2 1 
ATOM   293  N N   A ILE   A 1 16  ? -27.845 0.623   -24.702 0.22 30.11  ? 59  ILE   A N   1 
ATOM   294  N N   B ILE   A 1 16  ? -27.845 0.625   -24.708 0.22 30.42  ? 59  ILE   A N   1 
ATOM   295  N N   C ILE   A 1 16  ? -28.643 -0.025  -24.647 0.28 37.85  ? 59  ILE   A N   1 
ATOM   296  N N   D ILE   A 1 16  ? -28.633 -0.029  -24.652 0.28 37.89  ? 59  ILE   A N   1 
ATOM   297  C CA  A ILE   A 1 16  ? -26.877 -0.515  -24.625 0.22 30.47  ? 59  ILE   A CA  1 
ATOM   298  C CA  B ILE   A 1 16  ? -26.884 -0.520  -24.640 0.22 31.05  ? 59  ILE   A CA  1 
ATOM   299  C CA  C ILE   A 1 16  ? -27.604 -1.065  -24.390 0.28 37.80  ? 59  ILE   A CA  1 
ATOM   300  C CA  D ILE   A 1 16  ? -27.589 -1.064  -24.393 0.28 37.88  ? 59  ILE   A CA  1 
ATOM   301  C C   A ILE   A 1 16  ? -27.425 -1.682  -25.460 0.22 31.63  ? 59  ILE   A C   1 
ATOM   302  C C   B ILE   A 1 16  ? -27.461 -1.698  -25.452 0.22 32.96  ? 59  ILE   A C   1 
ATOM   303  C C   C ILE   A 1 16  ? -27.777 -2.141  -25.463 0.28 37.40  ? 59  ILE   A C   1 
ATOM   304  C C   D ILE   A 1 16  ? -27.742 -2.137  -25.467 0.28 37.53  ? 59  ILE   A C   1 
ATOM   305  O O   A ILE   A 1 16  ? -28.428 -2.311  -25.036 0.22 35.32  ? 59  ILE   A O   1 
ATOM   306  O O   B ILE   A 1 16  ? -28.410 -2.336  -24.988 0.22 36.41  ? 59  ILE   A O   1 
ATOM   307  O O   C ILE   A 1 16  ? -28.682 -3.006  -25.308 0.28 37.02  ? 59  ILE   A O   1 
ATOM   308  O O   D ILE   A 1 16  ? -28.646 -3.007  -25.310 0.28 37.19  ? 59  ILE   A O   1 
ATOM   309  C CB  A ILE   A 1 16  ? -26.610 -0.901  -23.163 0.22 28.15  ? 59  ILE   A CB  1 
ATOM   310  C CB  B ILE   A 1 16  ? -26.614 -0.899  -23.172 0.22 28.40  ? 59  ILE   A CB  1 
ATOM   311  C CB  C ILE   A 1 16  ? -27.726 -1.600  -22.951 0.28 38.37  ? 59  ILE   A CB  1 
ATOM   312  C CB  D ILE   A 1 16  ? -27.720 -1.602  -22.955 0.28 38.41  ? 59  ILE   A CB  1 
ATOM   313  C CG1 A ILE   A 1 16  ? -26.106 0.293   -22.350 0.22 26.84  ? 59  ILE   A CG1 1 
ATOM   314  C CG1 B ILE   A 1 16  ? -26.113 0.294   -22.356 0.22 27.00  ? 59  ILE   A CG1 1 
ATOM   315  C CG1 C ILE   A 1 16  ? -27.215 -0.560  -21.950 0.28 37.49  ? 59  ILE   A CG1 1 
ATOM   316  C CG1 D ILE   A 1 16  ? -27.213 -0.563  -21.952 0.28 37.52  ? 59  ILE   A CG1 1 
ATOM   317  C CG2 A ILE   A 1 16  ? -25.651 -2.073  -23.091 0.22 27.66  ? 59  ILE   A CG2 1 
ATOM   318  C CG2 B ILE   A 1 16  ? -25.654 -2.070  -23.096 0.22 27.84  ? 59  ILE   A CG2 1 
ATOM   319  C CG2 C ILE   A 1 16  ? -27.025 -2.939  -22.783 0.28 38.91  ? 59  ILE   A CG2 1 
ATOM   320  C CG2 D ILE   A 1 16  ? -27.022 -2.942  -22.784 0.28 38.93  ? 59  ILE   A CG2 1 
ATOM   321  C CD1 A ILE   A 1 16  ? -26.202 0.113   -20.857 0.22 27.54  ? 59  ILE   A CD1 1 
ATOM   322  C CD1 B ILE   A 1 16  ? -26.206 0.109   -20.861 0.22 27.64  ? 59  ILE   A CD1 1 
ATOM   323  C CD1 C ILE   A 1 16  ? -27.813 -0.694  -20.582 0.28 39.94  ? 59  ILE   A CD1 1 
ATOM   324  C CD1 D ILE   A 1 16  ? -27.814 -0.697  -20.585 0.28 39.95  ? 59  ILE   A CD1 1 
ATOM   325  N N   A THR   A 1 17  ? -26.755 -1.914  -26.604 0.22 33.21  ? 60  THR   A N   1 
ATOM   326  N N   B THR   A 1 17  ? -26.903 -1.987  -26.620 0.22 37.37  ? 60  THR   A N   1 
ATOM   327  N N   C THR   A 1 17  ? -26.981 -2.056  -26.532 0.28 39.20  ? 60  THR   A N   1 
ATOM   328  N N   D THR   A 1 17  ? -26.962 -2.055  -26.555 0.28 39.41  ? 60  THR   A N   1 
ATOM   329  C CA  A THR   A 1 17  ? -27.128 -2.864  -27.690 0.22 36.16  ? 60  THR   A CA  1 
ATOM   330  C CA  B THR   A 1 17  ? -27.279 -3.028  -27.614 0.22 41.42  ? 60  THR   A CA  1 
ATOM   331  C CA  C THR   A 1 17  ? -27.150 -2.869  -27.767 0.28 42.48  ? 60  THR   A CA  1 
ATOM   332  C CA  D THR   A 1 17  ? -27.220 -3.045  -27.630 0.28 43.12  ? 60  THR   A CA  1 
ATOM   333  C C   A THR   A 1 17  ? -25.877 -3.544  -28.273 0.22 36.87  ? 60  THR   A C   1 
ATOM   334  C C   B THR   A 1 17  ? -26.015 -3.460  -28.373 0.22 41.80  ? 60  THR   A C   1 
ATOM   335  C C   C THR   A 1 17  ? -25.793 -3.356  -28.274 0.28 42.62  ? 60  THR   A C   1 
ATOM   336  C C   D THR   A 1 17  ? -25.898 -3.436  -28.295 0.28 43.26  ? 60  THR   A C   1 
ATOM   337  O O   A THR   A 1 17  ? -24.810 -2.892  -28.343 0.22 37.14  ? 60  THR   A O   1 
ATOM   338  O O   B THR   A 1 17  ? -25.110 -2.596  -28.582 0.22 43.86  ? 60  THR   A O   1 
ATOM   339  O O   C THR   A 1 17  ? -24.846 -2.532  -28.343 0.28 43.46  ? 60  THR   A O   1 
ATOM   340  O O   D THR   A 1 17  ? -25.033 -2.569  -28.482 0.28 45.00  ? 60  THR   A O   1 
ATOM   341  C CB  A THR   A 1 17  ? -27.907 -2.146  -28.804 0.22 34.70  ? 60  THR   A CB  1 
ATOM   342  C CB  B THR   A 1 17  ? -28.393 -2.527  -28.548 0.22 41.73  ? 60  THR   A CB  1 
ATOM   343  C CB  C THR   A 1 17  ? -27.876 -2.074  -28.863 0.28 40.42  ? 60  THR   A CB  1 
ATOM   344  C CB  D THR   A 1 17  ? -28.347 -2.530  -28.546 0.28 42.54  ? 60  THR   A CB  1 
ATOM   345  O OG1 A THR   A 1 17  ? -27.016 -1.274  -29.498 0.22 33.88  ? 60  THR   A OG1 1 
ATOM   346  O OG1 B THR   A 1 17  ? -29.655 -2.857  -27.962 0.22 41.70  ? 60  THR   A OG1 1 
ATOM   347  O OG1 C THR   A 1 17  ? -26.956 -1.163  -29.463 0.28 39.26  ? 60  THR   A OG1 1 
ATOM   348  O OG1 D THR   A 1 17  ? -29.607 -2.858  -27.950 0.28 42.20  ? 60  THR   A OG1 1 
ATOM   349  C CG2 A THR   A 1 17  ? -29.080 -1.347  -28.277 0.22 35.07  ? 60  THR   A CG2 1 
ATOM   350  C CG2 B THR   A 1 17  ? -28.325 -3.114  -29.939 0.22 42.32  ? 60  THR   A CG2 1 
ATOM   351  C CG2 C THR   A 1 17  ? -29.066 -1.305  -28.331 0.28 41.41  ? 60  THR   A CG2 1 
ATOM   352  C CG2 D THR   A 1 17  ? -28.312 -3.105  -29.942 0.28 43.08  ? 60  THR   A CG2 1 
ATOM   353  N N   A TRP   A 1 18  ? -26.023 -4.801  -28.699 0.22 40.74  ? 61  TRP   A N   1 
ATOM   354  N N   B TRP   A 1 18  ? -26.020 -4.768  -28.718 0.22 42.78  ? 61  TRP   A N   1 
ATOM   355  N N   C TRP   A 1 18  ? -25.715 -4.632  -28.657 0.28 45.40  ? 61  TRP   A N   1 
ATOM   356  N N   D TRP   A 1 18  ? -25.705 -4.699  -28.616 0.28 45.71  ? 61  TRP   A N   1 
ATOM   357  C CA  A TRP   A 1 18  ? -25.037 -5.561  -29.518 0.22 43.96  ? 61  TRP   A CA  1 
ATOM   358  C CA  B TRP   A 1 18  ? -25.038 -5.547  -29.530 0.22 44.98  ? 61  TRP   A CA  1 
ATOM   359  C CA  C TRP   A 1 18  ? -24.642 -5.094  -29.570 0.28 48.54  ? 61  TRP   A CA  1 
ATOM   360  C CA  D TRP   A 1 18  ? -24.639 -5.114  -29.558 0.28 48.69  ? 61  TRP   A CA  1 
ATOM   361  C C   A TRP   A 1 18  ? -25.110 -5.092  -30.982 0.22 46.81  ? 61  TRP   A C   1 
ATOM   362  C C   B TRP   A 1 18  ? -25.111 -5.088  -30.994 0.22 47.30  ? 61  TRP   A C   1 
ATOM   363  C C   C TRP   A 1 18  ? -24.918 -4.467  -30.940 0.28 51.07  ? 61  TRP   A C   1 
ATOM   364  C C   D TRP   A 1 18  ? -24.921 -4.483  -30.928 0.28 51.15  ? 61  TRP   A C   1 
ATOM   365  O O   A TRP   A 1 18  ? -26.088 -5.476  -31.653 0.22 47.78  ? 61  TRP   A O   1 
ATOM   366  O O   B TRP   A 1 18  ? -26.091 -5.468  -31.663 0.22 48.03  ? 61  TRP   A O   1 
ATOM   367  O O   C TRP   A 1 18  ? -26.103 -4.440  -31.341 0.28 53.97  ? 61  TRP   A O   1 
ATOM   368  O O   D TRP   A 1 18  ? -26.102 -4.466  -31.328 0.28 54.10  ? 61  TRP   A O   1 
ATOM   369  C CB  A TRP   A 1 18  ? -25.321 -7.064  -29.391 0.22 43.69  ? 61  TRP   A CB  1 
ATOM   370  C CB  B TRP   A 1 18  ? -25.325 -7.055  -29.399 0.22 44.18  ? 61  TRP   A CB  1 
ATOM   371  C CB  C TRP   A 1 18  ? -24.588 -6.619  -29.641 0.28 45.29  ? 61  TRP   A CB  1 
ATOM   372  C CB  D TRP   A 1 18  ? -24.582 -6.636  -29.633 0.28 45.39  ? 61  TRP   A CB  1 
ATOM   373  C CG  A TRP   A 1 18  ? -24.401 -7.963  -30.163 0.22 45.93  ? 61  TRP   A CG  1 
ATOM   374  C CG  B TRP   A 1 18  ? -24.405 -7.960  -30.166 0.22 46.19  ? 61  TRP   A CG  1 
ATOM   375  C CG  C TRP   A 1 18  ? -23.399 -7.146  -30.382 0.28 45.95  ? 61  TRP   A CG  1 
ATOM   376  C CG  D TRP   A 1 18  ? -23.396 -7.159  -30.378 0.28 46.00  ? 61  TRP   A CG  1 
ATOM   377  C CD1 A TRP   A 1 18  ? -24.673 -8.628  -31.327 0.22 45.18  ? 61  TRP   A CD1 1 
ATOM   378  C CD1 B TRP   A 1 18  ? -24.676 -8.628  -31.328 0.22 45.34  ? 61  TRP   A CD1 1 
ATOM   379  C CD1 C TRP   A 1 18  ? -23.259 -7.282  -31.733 0.28 45.60  ? 61  TRP   A CD1 1 
ATOM   380  C CD1 D TRP   A 1 18  ? -23.259 -7.292  -31.730 0.28 45.62  ? 61  TRP   A CD1 1 
ATOM   381  C CD2 A TRP   A 1 18  ? -23.056 -8.330  -29.799 0.22 48.15  ? 61  TRP   A CD2 1 
ATOM   382  C CD2 B TRP   A 1 18  ? -23.060 -8.329  -29.802 0.22 48.25  ? 61  TRP   A CD2 1 
ATOM   383  C CD2 C TRP   A 1 18  ? -22.188 -7.664  -29.803 0.28 47.23  ? 61  TRP   A CD2 1 
ATOM   384  C CD2 D TRP   A 1 18  ? -22.185 -7.674  -29.801 0.28 47.24  ? 61  TRP   A CD2 1 
ATOM   385  N NE1 A TRP   A 1 18  ? -23.589 -9.369  -31.718 0.22 45.41  ? 61  TRP   A NE1 1 
ATOM   386  N NE1 B TRP   A 1 18  ? -23.593 -9.372  -31.717 0.22 45.52  ? 61  TRP   A NE1 1 
ATOM   387  N NE1 C TRP   A 1 18  ? -22.042 -7.831  -32.035 0.28 43.37  ? 61  TRP   A NE1 1 
ATOM   388  N NE1 D TRP   A 1 18  ? -22.042 -7.840  -32.033 0.28 43.41  ? 61  TRP   A NE1 1 
ATOM   389  C CE2 A TRP   A 1 18  ? -22.581 -9.205  -30.802 0.22 46.91  ? 61  TRP   A CE2 1 
ATOM   390  C CE2 B TRP   A 1 18  ? -22.584 -9.207  -30.801 0.22 47.00  ? 61  TRP   A CE2 1 
ATOM   391  C CE2 C TRP   A 1 18  ? -21.367 -8.085  -30.871 0.28 45.99  ? 61  TRP   A CE2 1 
ATOM   392  C CE2 D TRP   A 1 18  ? -21.365 -8.094  -30.870 0.28 46.01  ? 61  TRP   A CE2 1 
ATOM   393  C CE3 A TRP   A 1 18  ? -22.209 -8.001  -28.733 0.22 49.10  ? 61  TRP   A CE3 1 
ATOM   394  C CE3 B TRP   A 1 18  ? -22.212 -7.998  -28.736 0.22 49.16  ? 61  TRP   A CE3 1 
ATOM   395  C CE3 C TRP   A 1 18  ? -21.726 -7.824  -28.492 0.28 48.65  ? 61  TRP   A CE3 1 
ATOM   396  C CE3 D TRP   A 1 18  ? -21.723 -7.834  -28.490 0.28 48.65  ? 61  TRP   A CE3 1 
ATOM   397  C CZ2 A TRP   A 1 18  ? -21.294 -9.743  -30.766 0.22 48.37  ? 61  TRP   A CZ2 1 
ATOM   398  C CZ2 B TRP   A 1 18  ? -21.297 -9.745  -30.764 0.22 48.42  ? 61  TRP   A CZ2 1 
ATOM   399  C CZ2 C TRP   A 1 18  ? -20.104 -8.638  -30.662 0.28 47.91  ? 61  TRP   A CZ2 1 
ATOM   400  C CZ2 D TRP   A 1 18  ? -20.102 -8.645  -30.662 0.28 47.91  ? 61  TRP   A CZ2 1 
ATOM   401  C CZ3 A TRP   A 1 18  ? -20.941 -8.540  -28.695 0.22 49.79  ? 61  TRP   A CZ3 1 
ATOM   402  C CZ3 B TRP   A 1 18  ? -20.944 -8.538  -28.697 0.22 49.83  ? 61  TRP   A CZ3 1 
ATOM   403  C CZ3 C TRP   A 1 18  ? -20.478 -8.368  -28.287 0.28 49.26  ? 61  TRP   A CZ3 1 
ATOM   404  C CZ3 D TRP   A 1 18  ? -20.474 -8.377  -28.286 0.28 49.25  ? 61  TRP   A CZ3 1 
ATOM   405  C CH2 A TRP   A 1 18  ? -20.492 -9.400  -29.699 0.22 49.28  ? 61  TRP   A CH2 1 
ATOM   406  C CH2 B TRP   A 1 18  ? -20.495 -9.401  -29.698 0.22 49.31  ? 61  TRP   A CH2 1 
ATOM   407  C CH2 C TRP   A 1 18  ? -19.679 -8.771  -29.359 0.28 48.27  ? 61  TRP   A CH2 1 
ATOM   408  C CH2 D TRP   A 1 18  ? -19.676 -8.778  -29.359 0.28 48.27  ? 61  TRP   A CH2 1 
ATOM   409  N N   A GLU   A 1 19  ? -24.115 -4.318  -31.451 0.22 49.21  ? 62  GLU   A N   1 
ATOM   410  N N   B GLU   A 1 19  ? -24.113 -4.319  -31.459 0.22 49.43  ? 62  GLU   A N   1 
ATOM   411  N N   C GLU   A 1 19  ? -23.879 -3.950  -31.603 0.28 52.07  ? 62  GLU   A N   1 
ATOM   412  N N   D GLU   A 1 19  ? -23.886 -3.957  -31.593 0.28 52.12  ? 62  GLU   A N   1 
ATOM   413  C CA  A GLU   A 1 19  ? -24.089 -3.636  -32.782 0.22 51.34  ? 62  GLU   A CA  1 
ATOM   414  C CA  B GLU   A 1 19  ? -24.086 -3.634  -32.787 0.22 51.44  ? 62  GLU   A CA  1 
ATOM   415  C CA  C GLU   A 1 19  ? -23.944 -3.474  -33.010 0.28 53.73  ? 62  GLU   A CA  1 
ATOM   416  C CA  D GLU   A 1 19  ? -23.949 -3.478  -33.002 0.28 53.75  ? 62  GLU   A CA  1 
ATOM   417  C C   A GLU   A 1 19  ? -23.119 -4.337  -33.750 0.22 51.52  ? 62  GLU   A C   1 
ATOM   418  C C   B GLU   A 1 19  ? -23.116 -4.337  -33.753 0.22 51.56  ? 62  GLU   A C   1 
ATOM   419  C C   C GLU   A 1 19  ? -23.536 -4.625  -33.938 0.28 56.84  ? 62  GLU   A C   1 
ATOM   420  C C   D GLU   A 1 19  ? -23.539 -4.628  -33.932 0.28 56.85  ? 62  GLU   A C   1 
ATOM   421  O O   A GLU   A 1 19  ? -21.893 -4.102  -33.640 0.22 50.58  ? 62  GLU   A O   1 
ATOM   422  O O   B GLU   A 1 19  ? -21.889 -4.107  -33.639 0.22 50.60  ? 62  GLU   A O   1 
ATOM   423  O O   C GLU   A 1 19  ? -22.482 -5.235  -33.692 0.28 57.47  ? 62  GLU   A O   1 
ATOM   424  O O   D GLU   A 1 19  ? -22.485 -5.238  -33.686 0.28 57.48  ? 62  GLU   A O   1 
ATOM   425  C CB  A GLU   A 1 19  ? -23.677 -2.171  -32.613 0.22 52.84  ? 62  GLU   A CB  1 
ATOM   426  C CB  B GLU   A 1 19  ? -23.674 -2.169  -32.612 0.22 52.89  ? 62  GLU   A CB  1 
ATOM   427  C CB  C GLU   A 1 19  ? -23.045 -2.249  -33.210 0.28 51.58  ? 62  GLU   A CB  1 
ATOM   428  C CB  D GLU   A 1 19  ? -23.049 -2.254  -33.204 0.28 51.59  ? 62  GLU   A CB  1 
ATOM   429  C CG  A GLU   A 1 19  ? -24.726 -1.313  -31.923 0.22 53.46  ? 62  GLU   A CG  1 
ATOM   430  C CG  B GLU   A 1 19  ? -24.726 -1.314  -31.924 0.22 53.49  ? 62  GLU   A CG  1 
ATOM   431  C CG  C GLU   A 1 19  ? -22.929 -1.807  -34.663 0.28 50.81  ? 62  GLU   A CG  1 
ATOM   432  C CG  D GLU   A 1 19  ? -22.933 -1.812  -34.657 0.28 50.82  ? 62  GLU   A CG  1 
ATOM   433  C CD  A GLU   A 1 19  ? -25.983 -1.081  -32.742 0.22 53.99  ? 62  GLU   A CD  1 
ATOM   434  C CD  B GLU   A 1 19  ? -25.981 -1.084  -32.745 0.22 54.01  ? 62  GLU   A CD  1 
ATOM   435  C CD  C GLU   A 1 19  ? -22.105 -0.556  -34.912 0.28 49.33  ? 62  GLU   A CD  1 
ATOM   436  C CD  D GLU   A 1 19  ? -22.109 -0.560  -34.907 0.28 49.35  ? 62  GLU   A CD  1 
ATOM   437  O OE1 A GLU   A 1 19  ? -25.879 -0.450  -33.819 0.22 52.78  ? 62  GLU   A OE1 1 
ATOM   438  O OE1 B GLU   A 1 19  ? -25.877 -0.453  -33.822 0.22 52.74  ? 62  GLU   A OE1 1 
ATOM   439  O OE1 C GLU   A 1 19  ? -21.623 0.046   -33.934 0.28 51.98  ? 62  GLU   A OE1 1 
ATOM   440  O OE1 D GLU   A 1 19  ? -21.629 0.044   -33.930 0.28 51.97  ? 62  GLU   A OE1 1 
ATOM   441  O OE2 A GLU   A 1 19  ? -27.057 -1.555  -32.315 0.22 52.88  ? 62  GLU   A OE2 1 
ATOM   442  O OE2 B GLU   A 1 19  ? -27.053 -1.563  -32.322 0.22 52.93  ? 62  GLU   A OE2 1 
ATOM   443  O OE2 C GLU   A 1 19  ? -21.951 -0.182  -36.091 0.28 49.39  ? 62  GLU   A OE2 1 
ATOM   444  O OE2 D GLU   A 1 19  ? -21.953 -0.189  -36.087 0.28 49.39  ? 62  GLU   A OE2 1 
ATOM   445  N N   A LYS   A 1 20  ? -23.658 -5.100  -34.710 0.22 52.41  ? 63  LYS   A N   1 
ATOM   446  N N   B LYS   A 1 20  ? -23.657 -5.100  -34.712 0.22 52.42  ? 63  LYS   A N   1 
ATOM   447  N N   C LYS   A 1 20  ? -24.344 -4.916  -34.959 0.28 61.71  ? 63  LYS   A N   1 
ATOM   448  N N   D LYS   A 1 20  ? -24.345 -4.915  -34.957 0.28 61.71  ? 63  LYS   A N   1 
ATOM   449  C CA  A LYS   A 1 20  ? -22.900 -5.956  -35.670 0.22 51.33  ? 63  LYS   A CA  1 
ATOM   450  C CA  B LYS   A 1 20  ? -22.899 -5.957  -35.672 0.22 51.34  ? 63  LYS   A CA  1 
ATOM   451  C CA  C LYS   A 1 20  ? -23.909 -5.720  -36.132 0.28 64.37  ? 63  LYS   A CA  1 
ATOM   452  C CA  D LYS   A 1 20  ? -23.909 -5.718  -36.130 0.28 64.38  ? 63  LYS   A CA  1 
ATOM   453  C C   A LYS   A 1 20  ? -21.900 -5.125  -36.486 0.22 50.63  ? 63  LYS   A C   1 
ATOM   454  C C   B LYS   A 1 20  ? -21.899 -5.126  -36.488 0.22 50.64  ? 63  LYS   A C   1 
ATOM   455  C C   C LYS   A 1 20  ? -23.099 -4.784  -37.025 0.28 63.64  ? 63  LYS   A C   1 
ATOM   456  C C   D LYS   A 1 20  ? -23.100 -4.783  -37.024 0.28 63.65  ? 63  LYS   A C   1 
ATOM   457  O O   A LYS   A 1 20  ? -22.197 -3.953  -36.782 0.22 50.59  ? 63  LYS   A O   1 
ATOM   458  O O   B LYS   A 1 20  ? -22.197 -3.954  -36.785 0.22 50.59  ? 63  LYS   A O   1 
ATOM   459  O O   C LYS   A 1 20  ? -23.619 -3.695  -37.348 0.28 66.54  ? 63  LYS   A O   1 
ATOM   460  O O   D LYS   A 1 20  ? -23.620 -3.695  -37.349 0.28 66.53  ? 63  LYS   A O   1 
ATOM   461  C CB  A LYS   A 1 20  ? -23.859 -6.699  -36.604 0.22 51.59  ? 63  LYS   A CB  1 
ATOM   462  C CB  B LYS   A 1 20  ? -23.859 -6.699  -36.604 0.22 51.60  ? 63  LYS   A CB  1 
ATOM   463  C CB  C LYS   A 1 20  ? -25.091 -6.313  -36.907 0.28 68.85  ? 63  LYS   A CB  1 
ATOM   464  C CB  D LYS   A 1 20  ? -25.091 -6.313  -36.906 0.28 68.84  ? 63  LYS   A CB  1 
ATOM   465  C CG  A LYS   A 1 20  ? -24.607 -7.856  -35.958 0.22 52.65  ? 63  LYS   A CG  1 
ATOM   466  C CG  B LYS   A 1 20  ? -24.607 -7.856  -35.959 0.22 52.66  ? 63  LYS   A CG  1 
ATOM   467  C CG  C LYS   A 1 20  ? -25.301 -7.813  -36.737 0.28 71.51  ? 63  LYS   A CG  1 
ATOM   468  C CG  D LYS   A 1 20  ? -25.300 -7.812  -36.736 0.28 71.50  ? 63  LYS   A CG  1 
ATOM   469  C CD  A LYS   A 1 20  ? -25.864 -8.257  -36.702 0.22 55.08  ? 63  LYS   A CD  1 
ATOM   470  C CD  B LYS   A 1 20  ? -25.864 -8.257  -36.702 0.22 55.07  ? 63  LYS   A CD  1 
ATOM   471  C CD  C LYS   A 1 20  ? -26.321 -8.187  -35.676 0.28 75.47  ? 63  LYS   A CD  1 
ATOM   472  C CD  D LYS   A 1 20  ? -26.320 -8.187  -35.676 0.28 75.44  ? 63  LYS   A CD  1 
ATOM   473  C CE  A LYS   A 1 20  ? -26.647 -9.343  -35.992 0.22 56.51  ? 63  LYS   A CE  1 
ATOM   474  C CE  B LYS   A 1 20  ? -26.648 -9.343  -35.992 0.22 56.50  ? 63  LYS   A CE  1 
ATOM   475  C CE  C LYS   A 1 20  ? -25.902 -7.816  -34.268 0.28 77.65  ? 63  LYS   A CE  1 
ATOM   476  C CE  D LYS   A 1 20  ? -25.902 -7.816  -34.268 0.28 77.62  ? 63  LYS   A CE  1 
ATOM   477  N NZ  A LYS   A 1 20  ? -28.000 -9.512  -36.572 0.22 56.69  ? 63  LYS   A NZ  1 
ATOM   478  N NZ  B LYS   A 1 20  ? -28.000 -9.512  -36.572 0.22 56.68  ? 63  LYS   A NZ  1 
ATOM   479  N NZ  C LYS   A 1 20  ? -26.587 -6.594  -33.780 0.28 79.58  ? 63  LYS   A NZ  1 
ATOM   480  N NZ  D LYS   A 1 20  ? -26.587 -6.594  -33.780 0.28 79.54  ? 63  LYS   A NZ  1 
ATOM   481  N N   A ASP   A 1 21  ? -20.758 -5.735  -36.831 0.22 49.39  ? 64  ASP   A N   1 
ATOM   482  N N   B ASP   A 1 21  ? -20.757 -5.735  -36.831 0.22 49.40  ? 64  ASP   A N   1 
ATOM   483  N N   C ASP   A 1 21  ? -21.878 -5.182  -37.385 0.28 64.53  ? 64  ASP   A N   1 
ATOM   484  N N   D ASP   A 1 21  ? -21.879 -5.181  -37.384 0.28 64.53  ? 64  ASP   A N   1 
ATOM   485  C CA  A ASP   A 1 21  ? -19.622 -5.113  -37.567 0.22 50.72  ? 64  ASP   A CA  1 
ATOM   486  C CA  B ASP   A 1 21  ? -19.621 -5.113  -37.568 0.22 50.72  ? 64  ASP   A CA  1 
ATOM   487  C CA  C ASP   A 1 21  ? -20.956 -4.377  -38.229 0.28 67.28  ? 64  ASP   A CA  1 
ATOM   488  C CA  D ASP   A 1 21  ? -20.956 -4.377  -38.229 0.28 67.25  ? 64  ASP   A CA  1 
ATOM   489  C C   A ASP   A 1 21  ? -19.245 -3.771  -36.926 0.22 50.35  ? 64  ASP   A C   1 
ATOM   490  C C   B ASP   A 1 21  ? -19.245 -3.771  -36.927 0.22 50.34  ? 64  ASP   A C   1 
ATOM   491  C C   C ASP   A 1 21  ? -20.411 -3.216  -37.385 0.28 64.09  ? 64  ASP   A C   1 
ATOM   492  C C   D ASP   A 1 21  ? -20.411 -3.216  -37.385 0.28 64.08  ? 64  ASP   A C   1 
ATOM   493  O O   A ASP   A 1 21  ? -19.275 -2.740  -37.636 0.22 47.13  ? 64  ASP   A O   1 
ATOM   494  O O   B ASP   A 1 21  ? -19.274 -2.740  -37.636 0.22 47.14  ? 64  ASP   A O   1 
ATOM   495  O O   C ASP   A 1 21  ? -20.561 -2.049  -37.806 0.28 63.82  ? 64  ASP   A O   1 
ATOM   496  O O   D ASP   A 1 21  ? -20.559 -2.050  -37.807 0.28 63.81  ? 64  ASP   A O   1 
ATOM   497  C CB  A ASP   A 1 21  ? -19.932 -4.939  -39.059 0.22 55.50  ? 64  ASP   A CB  1 
ATOM   498  C CB  B ASP   A 1 21  ? -19.932 -4.939  -39.059 0.22 55.48  ? 64  ASP   A CB  1 
ATOM   499  C CB  C ASP   A 1 21  ? -21.642 -3.896  -39.517 0.28 67.56  ? 64  ASP   A CB  1 
ATOM   500  C CB  D ASP   A 1 21  ? -21.643 -3.896  -39.516 0.28 67.54  ? 64  ASP   A CB  1 
ATOM   501  C CG  A ASP   A 1 21  ? -19.743 -6.201  -39.879 0.22 58.22  ? 64  ASP   A CG  1 
ATOM   502  C CG  B ASP   A 1 21  ? -19.743 -6.201  -39.878 0.22 58.20  ? 64  ASP   A CG  1 
ATOM   503  C CG  C ASP   A 1 21  ? -22.538 -4.927  -40.192 0.28 66.39  ? 64  ASP   A CG  1 
ATOM   504  C CG  D ASP   A 1 21  ? -22.539 -4.928  -40.190 0.28 66.37  ? 64  ASP   A CG  1 
ATOM   505  O OD1 A ASP   A 1 21  ? -18.619 -6.404  -40.386 0.22 60.47  ? 64  ASP   A OD1 1 
ATOM   506  O OD1 B ASP   A 1 21  ? -18.618 -6.408  -40.381 0.22 60.45  ? 64  ASP   A OD1 1 
ATOM   507  O OD1 C ASP   A 1 21  ? -22.350 -6.137  -39.936 0.28 65.33  ? 64  ASP   A OD1 1 
ATOM   508  O OD1 D ASP   A 1 21  ? -22.352 -6.138  -39.934 0.28 65.32  ? 64  ASP   A OD1 1 
ATOM   509  O OD2 A ASP   A 1 21  ? -20.726 -6.954  -40.025 0.22 61.53  ? 64  ASP   A OD2 1 
ATOM   510  O OD2 B ASP   A 1 21  ? -20.728 -6.951  -40.028 0.22 61.51  ? 64  ASP   A OD2 1 
ATOM   511  O OD2 C ASP   A 1 21  ? -23.423 -4.510  -40.971 0.28 60.13  ? 64  ASP   A OD2 1 
ATOM   512  O OD2 D ASP   A 1 21  ? -23.426 -4.511  -40.968 0.28 60.16  ? 64  ASP   A OD2 1 
ATOM   513  N N   A ALA   A 1 22  ? -18.895 -3.782  -35.636 0.22 45.56  ? 65  ALA   A N   1 
ATOM   514  N N   B ALA   A 1 22  ? -18.895 -3.782  -35.636 0.22 45.57  ? 65  ALA   A N   1 
ATOM   515  N N   C ALA   A 1 22  ? -19.817 -3.541  -36.230 0.28 64.53  ? 65  ALA   A N   1 
ATOM   516  N N   D ALA   A 1 22  ? -19.817 -3.541  -36.231 0.28 64.50  ? 65  ALA   A N   1 
ATOM   517  C CA  A ALA   A 1 22  ? -18.262 -2.639  -34.937 0.22 42.67  ? 65  ALA   A CA  1 
ATOM   518  C CA  B ALA   A 1 22  ? -18.262 -2.639  -34.937 0.22 42.68  ? 65  ALA   A CA  1 
ATOM   519  C CA  C ALA   A 1 22  ? -19.029 -2.625  -35.372 0.28 59.02  ? 65  ALA   A CA  1 
ATOM   520  C CA  D ALA   A 1 22  ? -19.029 -2.624  -35.372 0.28 59.02  ? 65  ALA   A CA  1 
ATOM   521  C C   A ALA   A 1 22  ? -16.775 -2.598  -35.313 0.22 40.19  ? 65  ALA   A C   1 
ATOM   522  C C   B ALA   A 1 22  ? -16.775 -2.598  -35.313 0.22 40.21  ? 65  ALA   A C   1 
ATOM   523  C C   C ALA   A 1 22  ? -17.535 -2.938  -35.525 0.28 55.04  ? 65  ALA   A C   1 
ATOM   524  C C   D ALA   A 1 22  ? -17.535 -2.938  -35.527 0.28 55.07  ? 65  ALA   A C   1 
ATOM   525  O O   A ALA   A 1 22  ? -16.289 -3.584  -35.897 0.22 40.91  ? 65  ALA   A O   1 
ATOM   526  O O   B ALA   A 1 22  ? -16.289 -3.584  -35.897 0.22 40.92  ? 65  ALA   A O   1 
ATOM   527  O O   C ALA   A 1 22  ? -17.202 -4.099  -35.851 0.28 54.53  ? 65  ALA   A O   1 
ATOM   528  O O   D ALA   A 1 22  ? -17.202 -4.098  -35.855 0.28 54.54  ? 65  ALA   A O   1 
ATOM   529  C CB  A ALA   A 1 22  ? -18.463 -2.764  -33.445 0.22 43.09  ? 65  ALA   A CB  1 
ATOM   530  C CB  B ALA   A 1 22  ? -18.463 -2.764  -33.445 0.22 43.10  ? 65  ALA   A CB  1 
ATOM   531  C CB  C ALA   A 1 22  ? -19.467 -2.762  -33.940 0.28 60.50  ? 65  ALA   A CB  1 
ATOM   532  C CB  D ALA   A 1 22  ? -19.466 -2.762  -33.940 0.28 60.49  ? 65  ALA   A CB  1 
ATOM   533  N N   A GLU   A 1 23  ? -16.088 -1.493  -35.005 0.22 40.63  ? 66  GLU   A N   1 
ATOM   534  N N   B GLU   A 1 23  ? -16.088 -1.493  -35.005 0.22 40.64  ? 66  GLU   A N   1 
ATOM   535  N N   C GLU   A 1 23  ? -16.684 -1.932  -35.294 0.28 53.03  ? 66  GLU   A N   1 
ATOM   536  N N   D GLU   A 1 23  ? -16.684 -1.932  -35.294 0.28 53.05  ? 66  GLU   A N   1 
ATOM   537  C CA  A GLU   A 1 23  ? -14.622 -1.318  -35.210 0.22 40.27  ? 66  GLU   A CA  1 
ATOM   538  C CA  B GLU   A 1 23  ? -14.622 -1.318  -35.210 0.22 40.28  ? 66  GLU   A CA  1 
ATOM   539  C CA  C GLU   A 1 23  ? -15.197 -2.007  -35.348 0.28 52.15  ? 66  GLU   A CA  1 
ATOM   540  C CA  D GLU   A 1 23  ? -15.197 -2.007  -35.348 0.28 52.18  ? 66  GLU   A CA  1 
ATOM   541  C C   A GLU   A 1 23  ? -13.867 -2.281  -34.276 0.22 40.95  ? 66  GLU   A C   1 
ATOM   542  C C   B GLU   A 1 23  ? -13.867 -2.281  -34.276 0.22 40.95  ? 66  GLU   A C   1 
ATOM   543  C C   C GLU   A 1 23  ? -14.715 -3.129  -34.411 0.28 53.98  ? 66  GLU   A C   1 
ATOM   544  C C   D GLU   A 1 23  ? -14.715 -3.129  -34.411 0.28 53.98  ? 66  GLU   A C   1 
ATOM   545  O O   A GLU   A 1 23  ? -14.071 -2.214  -33.048 0.22 37.47  ? 66  GLU   A O   1 
ATOM   546  O O   B GLU   A 1 23  ? -14.071 -2.214  -33.048 0.22 37.49  ? 66  GLU   A O   1 
ATOM   547  O O   C GLU   A 1 23  ? -15.084 -3.102  -33.215 0.28 48.48  ? 66  GLU   A O   1 
ATOM   548  O O   D GLU   A 1 23  ? -15.083 -3.102  -33.215 0.28 48.52  ? 66  GLU   A O   1 
ATOM   549  C CB  A GLU   A 1 23  ? -14.242 0.145   -34.966 0.22 42.82  ? 66  GLU   A CB  1 
ATOM   550  C CB  B GLU   A 1 23  ? -14.242 0.145   -34.966 0.22 42.83  ? 66  GLU   A CB  1 
ATOM   551  C CB  C GLU   A 1 23  ? -14.626 -0.632  -34.980 0.28 53.92  ? 66  GLU   A CB  1 
ATOM   552  C CB  D GLU   A 1 23  ? -14.626 -0.632  -34.980 0.28 53.94  ? 66  GLU   A CB  1 
ATOM   553  C CG  A GLU   A 1 23  ? -12.913 0.553   -35.579 0.22 45.83  ? 66  GLU   A CG  1 
ATOM   554  C CG  B GLU   A 1 23  ? -12.913 0.553   -35.579 0.22 45.82  ? 66  GLU   A CG  1 
ATOM   555  C CG  C GLU   A 1 23  ? -13.134 -0.607  -34.690 0.28 55.91  ? 66  GLU   A CG  1 
ATOM   556  C CG  D GLU   A 1 23  ? -13.134 -0.607  -34.690 0.28 55.93  ? 66  GLU   A CG  1 
ATOM   557  C CD  A GLU   A 1 23  ? -12.903 1.958   -36.158 0.22 46.87  ? 66  GLU   A CD  1 
ATOM   558  C CD  B GLU   A 1 23  ? -12.902 1.958   -36.158 0.22 46.87  ? 66  GLU   A CD  1 
ATOM   559  C CD  C GLU   A 1 23  ? -12.638 0.713   -34.122 0.28 61.09  ? 66  GLU   A CD  1 
ATOM   560  C CD  D GLU   A 1 23  ? -12.638 0.713   -34.121 0.28 61.07  ? 66  GLU   A CD  1 
ATOM   561  O OE1 A GLU   A 1 23  ? -13.415 2.132   -37.282 0.22 50.27  ? 66  GLU   A OE1 1 
ATOM   562  O OE1 B GLU   A 1 23  ? -13.419 2.133   -37.280 0.22 50.25  ? 66  GLU   A OE1 1 
ATOM   563  O OE1 C GLU   A 1 23  ? -13.473 1.632   -33.929 0.28 61.17  ? 66  GLU   A OE1 1 
ATOM   564  O OE1 D GLU   A 1 23  ? -13.472 1.631   -33.926 0.28 61.16  ? 66  GLU   A OE1 1 
ATOM   565  O OE2 A GLU   A 1 23  ? -12.395 2.876   -35.482 0.22 49.09  ? 66  GLU   A OE2 1 
ATOM   566  O OE2 B GLU   A 1 23  ? -12.390 2.875   -35.484 0.22 49.07  ? 66  GLU   A OE2 1 
ATOM   567  O OE2 C GLU   A 1 23  ? -11.417 0.822   -33.871 0.28 64.83  ? 66  GLU   A OE2 1 
ATOM   568  O OE2 D GLU   A 1 23  ? -11.416 0.822   -33.872 0.28 64.79  ? 66  GLU   A OE2 1 
ATOM   569  N N   A VAL   A 1 24  ? -13.034 -3.165  -34.832 0.22 41.11  ? 67  VAL   A N   1 
ATOM   570  N N   B VAL   A 1 24  ? -13.034 -3.165  -34.832 0.22 41.11  ? 67  VAL   A N   1 
ATOM   571  N N   C VAL   A 1 24  ? -13.933 -4.081  -34.940 0.28 54.48  ? 67  VAL   A N   1 
ATOM   572  N N   D VAL   A 1 24  ? -13.933 -4.080  -34.941 0.28 54.48  ? 67  VAL   A N   1 
ATOM   573  C CA  A VAL   A 1 24  ? -12.409 -4.292  -34.077 0.22 41.03  ? 67  VAL   A CA  1 
ATOM   574  C CA  B VAL   A 1 24  ? -12.409 -4.293  -34.077 0.22 41.04  ? 67  VAL   A CA  1 
ATOM   575  C CA  C VAL   A 1 24  ? -13.343 -5.232  -34.188 0.28 54.86  ? 67  VAL   A CA  1 
ATOM   576  C CA  D VAL   A 1 24  ? -13.342 -5.231  -34.188 0.28 54.86  ? 67  VAL   A CA  1 
ATOM   577  C C   A VAL   A 1 24  ? -10.923 -3.988  -33.870 0.22 40.46  ? 67  VAL   A C   1 
ATOM   578  C C   B VAL   A 1 24  ? -10.923 -3.988  -33.870 0.22 40.46  ? 67  VAL   A C   1 
ATOM   579  C C   C VAL   A 1 24  ? -11.826 -5.018  -34.052 0.28 55.89  ? 67  VAL   A C   1 
ATOM   580  C C   D VAL   A 1 24  ? -11.826 -5.017  -34.053 0.28 55.88  ? 67  VAL   A C   1 
ATOM   581  O O   A VAL   A 1 24  ? -10.228 -3.726  -34.869 0.22 39.12  ? 67  VAL   A O   1 
ATOM   582  O O   B VAL   A 1 24  ? -10.229 -3.726  -34.869 0.22 39.13  ? 67  VAL   A O   1 
ATOM   583  O O   C VAL   A 1 24  ? -11.091 -5.428  -34.972 0.28 57.09  ? 67  VAL   A O   1 
ATOM   584  O O   D VAL   A 1 24  ? -11.091 -5.426  -34.973 0.28 57.08  ? 67  VAL   A O   1 
ATOM   585  C CB  A VAL   A 1 24  ? -12.633 -5.642  -34.786 0.22 41.61  ? 67  VAL   A CB  1 
ATOM   586  C CB  B VAL   A 1 24  ? -12.633 -5.642  -34.786 0.22 41.61  ? 67  VAL   A CB  1 
ATOM   587  C CB  C VAL   A 1 24  ? -13.660 -6.579  -34.873 0.28 56.16  ? 67  VAL   A CB  1 
ATOM   588  C CB  D VAL   A 1 24  ? -13.660 -6.578  -34.873 0.28 56.14  ? 67  VAL   A CB  1 
ATOM   589  C CG1 A VAL   A 1 24  ? -12.188 -6.805  -33.914 0.22 40.81  ? 67  VAL   A CG1 1 
ATOM   590  C CG1 B VAL   A 1 24  ? -12.188 -6.805  -33.914 0.22 40.81  ? 67  VAL   A CG1 1 
ATOM   591  C CG1 C VAL   A 1 24  ? -13.152 -7.756  -34.057 0.28 55.93  ? 67  VAL   A CG1 1 
ATOM   592  C CG1 D VAL   A 1 24  ? -13.151 -7.755  -34.057 0.28 55.92  ? 67  VAL   A CG1 1 
ATOM   593  C CG2 A VAL   A 1 24  ? -14.086 -5.815  -35.215 0.22 42.61  ? 67  VAL   A CG2 1 
ATOM   594  C CG2 B VAL   A 1 24  ? -14.086 -5.815  -35.215 0.22 42.60  ? 67  VAL   A CG2 1 
ATOM   595  C CG2 C VAL   A 1 24  ? -15.142 -6.744  -35.178 0.28 53.41  ? 67  VAL   A CG2 1 
ATOM   596  C CG2 D VAL   A 1 24  ? -15.142 -6.744  -35.178 0.28 53.43  ? 67  VAL   A CG2 1 
ATOM   597  N N   A THR   A 1 25  ? -10.463 -4.046  -32.614 0.22 41.60  ? 68  THR   A N   1 
ATOM   598  N N   B THR   A 1 25  ? -10.463 -4.046  -32.614 0.22 41.60  ? 68  THR   A N   1 
ATOM   599  N N   C THR   A 1 25  ? -11.380 -4.413  -32.942 0.28 55.38  ? 68  THR   A N   1 
ATOM   600  N N   D THR   A 1 25  ? -11.380 -4.413  -32.942 0.28 55.37  ? 68  THR   A N   1 
ATOM   601  C CA  A THR   A 1 25  ? -9.126  -3.560  -32.177 0.22 41.16  ? 68  THR   A CA  1 
ATOM   602  C CA  B THR   A 1 25  ? -9.126  -3.560  -32.177 0.22 41.16  ? 68  THR   A CA  1 
ATOM   603  C CA  C THR   A 1 25  ? -9.948  -4.215  -32.578 0.28 54.87  ? 68  THR   A CA  1 
ATOM   604  C CA  D THR   A 1 25  ? -9.948  -4.215  -32.578 0.28 54.86  ? 68  THR   A CA  1 
ATOM   605  C C   A THR   A 1 25  ? -8.778  -4.135  -30.794 0.22 39.53  ? 68  THR   A C   1 
ATOM   606  C C   B THR   A 1 25  ? -8.778  -4.135  -30.795 0.22 39.53  ? 68  THR   A C   1 
ATOM   607  C C   C THR   A 1 25  ? -9.698  -4.855  -31.208 0.28 55.03  ? 68  THR   A C   1 
ATOM   608  C C   D THR   A 1 25  ? -9.698  -4.855  -31.208 0.28 55.02  ? 68  THR   A C   1 
ATOM   609  O O   A THR   A 1 25  ? -9.627  -4.835  -30.204 0.22 38.97  ? 68  THR   A O   1 
ATOM   610  O O   B THR   A 1 25  ? -9.627  -4.835  -30.204 0.22 38.98  ? 68  THR   A O   1 
ATOM   611  O O   C THR   A 1 25  ? -10.586 -5.584  -30.730 0.28 51.25  ? 68  THR   A O   1 
ATOM   612  O O   D THR   A 1 25  ? -10.586 -5.585  -30.730 0.28 51.27  ? 68  THR   A O   1 
ATOM   613  C CB  A THR   A 1 25  ? -9.095  -2.026  -32.218 0.22 45.14  ? 68  THR   A CB  1 
ATOM   614  C CB  B THR   A 1 25  ? -9.095  -2.026  -32.218 0.22 45.12  ? 68  THR   A CB  1 
ATOM   615  C CB  C THR   A 1 25  ? -9.562  -2.729  -32.610 0.28 54.57  ? 68  THR   A CB  1 
ATOM   616  C CB  D THR   A 1 25  ? -9.562  -2.729  -32.611 0.28 54.57  ? 68  THR   A CB  1 
ATOM   617  O OG1 A THR   A 1 25  ? -7.845  -1.557  -31.709 0.22 47.37  ? 68  THR   A OG1 1 
ATOM   618  O OG1 B THR   A 1 25  ? -7.845  -1.557  -31.709 0.22 47.35  ? 68  THR   A OG1 1 
ATOM   619  O OG1 C THR   A 1 25  ? -8.139  -2.651  -32.524 0.28 52.69  ? 68  THR   A OG1 1 
ATOM   620  O OG1 D THR   A 1 25  ? -8.139  -2.651  -32.524 0.28 52.70  ? 68  THR   A OG1 1 
ATOM   621  C CG2 A THR   A 1 25  ? -10.231 -1.394  -31.440 0.22 47.36  ? 68  THR   A CG2 1 
ATOM   622  C CG2 B THR   A 1 25  ? -10.231 -1.394  -31.440 0.22 47.34  ? 68  THR   A CG2 1 
ATOM   623  C CG2 C THR   A 1 25  ? -10.188 -1.910  -31.502 0.28 56.95  ? 68  THR   A CG2 1 
ATOM   624  C CG2 D THR   A 1 25  ? -10.188 -1.910  -31.502 0.28 56.93  ? 68  THR   A CG2 1 
ATOM   625  N N   A GLY   A 1 26  ? -7.555  -3.876  -30.326 0.22 37.77  ? 69  GLY   A N   1 
ATOM   626  N N   B GLY   A 1 26  ? -7.555  -3.877  -30.326 0.22 37.78  ? 69  GLY   A N   1 
ATOM   627  N N   C GLY   A 1 26  ? -8.537  -4.591  -30.604 0.28 53.47  ? 69  GLY   A N   1 
ATOM   628  N N   D GLY   A 1 26  ? -8.537  -4.591  -30.604 0.28 53.48  ? 69  GLY   A N   1 
ATOM   629  C CA  A GLY   A 1 26  ? -7.014  -4.382  -29.051 0.22 37.32  ? 69  GLY   A CA  1 
ATOM   630  C CA  B GLY   A 1 26  ? -7.014  -4.382  -29.052 0.22 37.32  ? 69  GLY   A CA  1 
ATOM   631  C CA  C GLY   A 1 26  ? -8.184  -5.090  -29.265 0.28 52.91  ? 69  GLY   A CA  1 
ATOM   632  C CA  D GLY   A 1 26  ? -8.184  -5.090  -29.265 0.28 52.93  ? 69  GLY   A CA  1 
ATOM   633  C C   A GLY   A 1 26  ? -6.490  -5.802  -29.175 0.22 36.76  ? 69  GLY   A C   1 
ATOM   634  C C   B GLY   A 1 26  ? -6.490  -5.803  -29.175 0.22 36.76  ? 69  GLY   A C   1 
ATOM   635  C C   C GLY   A 1 26  ? -7.685  -6.526  -29.300 0.28 56.06  ? 69  GLY   A C   1 
ATOM   636  C C   D GLY   A 1 26  ? -7.685  -6.525  -29.300 0.28 56.06  ? 69  GLY   A C   1 
ATOM   637  O O   A GLY   A 1 26  ? -7.032  -6.568  -29.993 0.22 36.22  ? 69  GLY   A O   1 
ATOM   638  O O   B GLY   A 1 26  ? -7.032  -6.569  -29.993 0.22 36.22  ? 69  GLY   A O   1 
ATOM   639  O O   C GLY   A 1 26  ? -8.270  -7.362  -30.033 0.28 53.14  ? 69  GLY   A O   1 
ATOM   640  O O   D GLY   A 1 26  ? -8.270  -7.362  -30.032 0.28 53.16  ? 69  GLY   A O   1 
ATOM   641  N N   A ASN   A 1 27  ? -5.482  -6.150  -28.369 0.22 36.42  ? 70  ASN   A N   1 
ATOM   642  N N   B ASN   A 1 27  ? -5.482  -6.150  -28.369 0.22 36.43  ? 70  ASN   A N   1 
ATOM   643  N N   C ASN   A 1 27  ? -6.664  -6.794  -28.486 0.28 59.14  ? 70  ASN   A N   1 
ATOM   644  N N   D ASN   A 1 27  ? -6.664  -6.794  -28.486 0.28 59.13  ? 70  ASN   A N   1 
ATOM   645  C CA  A ASN   A 1 27  ? -4.971  -7.541  -28.219 0.22 37.05  ? 70  ASN   A CA  1 
ATOM   646  C CA  B ASN   A 1 27  ? -4.971  -7.541  -28.219 0.22 37.05  ? 70  ASN   A CA  1 
ATOM   647  C CA  C ASN   A 1 27  ? -5.957  -8.095  -28.356 0.28 61.18  ? 70  ASN   A CA  1 
ATOM   648  C CA  D ASN   A 1 27  ? -5.957  -8.094  -28.356 0.28 61.17  ? 70  ASN   A CA  1 
ATOM   649  C C   A ASN   A 1 27  ? -5.628  -8.182  -26.978 0.22 35.78  ? 70  ASN   A C   1 
ATOM   650  C C   B ASN   A 1 27  ? -5.628  -8.182  -26.978 0.22 35.78  ? 70  ASN   A C   1 
ATOM   651  C C   C ASN   A 1 27  ? -6.524  -8.853  -27.140 0.28 58.14  ? 70  ASN   A C   1 
ATOM   652  C C   D ASN   A 1 27  ? -6.523  -8.853  -27.140 0.28 58.14  ? 70  ASN   A C   1 
ATOM   653  O O   A ASN   A 1 27  ? -6.545  -7.552  -26.400 0.22 31.37  ? 70  ASN   A O   1 
ATOM   654  O O   B ASN   A 1 27  ? -6.545  -7.553  -26.400 0.22 31.39  ? 70  ASN   A O   1 
ATOM   655  O O   C ASN   A 1 27  ? -7.599  -8.442  -26.626 0.28 50.23  ? 70  ASN   A O   1 
ATOM   656  O O   D ASN   A 1 27  ? -7.598  -8.440  -26.625 0.28 50.28  ? 70  ASN   A O   1 
ATOM   657  C CB  A ASN   A 1 27  ? -3.440  -7.559  -28.239 0.22 38.60  ? 70  ASN   A CB  1 
ATOM   658  C CB  B ASN   A 1 27  ? -3.440  -7.560  -28.239 0.22 38.60  ? 70  ASN   A CB  1 
ATOM   659  C CB  C ASN   A 1 27  ? -4.442  -7.856  -28.309 0.28 64.34  ? 70  ASN   A CB  1 
ATOM   660  C CB  D ASN   A 1 27  ? -4.442  -7.856  -28.308 0.28 64.32  ? 70  ASN   A CB  1 
ATOM   661  C CG  A ASN   A 1 27  ? -2.816  -7.007  -26.975 0.22 40.34  ? 70  ASN   A CG  1 
ATOM   662  C CG  B ASN   A 1 27  ? -2.816  -7.007  -26.975 0.22 40.33  ? 70  ASN   A CG  1 
ATOM   663  C CG  C ASN   A 1 27  ? -4.029  -6.809  -27.296 0.28 67.23  ? 70  ASN   A CG  1 
ATOM   664  C CG  D ASN   A 1 27  ? -4.029  -6.809  -27.295 0.28 67.22  ? 70  ASN   A CG  1 
ATOM   665  O OD1 A ASN   A 1 27  ? -3.043  -5.851  -26.617 0.22 40.17  ? 70  ASN   A OD1 1 
ATOM   666  O OD1 B ASN   A 1 27  ? -3.043  -5.852  -26.617 0.22 40.17  ? 70  ASN   A OD1 1 
ATOM   667  O OD1 C ASN   A 1 27  ? -4.380  -5.637  -27.436 0.28 70.36  ? 70  ASN   A OD1 1 
ATOM   668  O OD1 D ASN   A 1 27  ? -4.382  -5.638  -27.434 0.28 70.34  ? 70  ASN   A OD1 1 
ATOM   669  N ND2 A ASN   A 1 27  ? -2.032  -7.825  -26.290 0.22 42.22  ? 70  ASN   A ND2 1 
ATOM   670  N ND2 B ASN   A 1 27  ? -2.032  -7.825  -26.290 0.22 42.21  ? 70  ASN   A ND2 1 
ATOM   671  N ND2 C ASN   A 1 27  ? -3.279  -7.216  -26.283 0.28 71.07  ? 70  ASN   A ND2 1 
ATOM   672  N ND2 D ASN   A 1 27  ? -3.278  -7.216  -26.283 0.28 71.03  ? 70  ASN   A ND2 1 
ATOM   673  N N   A SER   A 1 28  ? -5.223  -9.407  -26.616 0.22 34.37  ? 71  SER   A N   1 
ATOM   674  N N   B SER   A 1 28  ? -5.223  -9.407  -26.616 0.22 34.38  ? 71  SER   A N   1 
ATOM   675  N N   C SER   A 1 28  ? -5.844  -9.929  -26.714 0.28 55.07  ? 71  SER   A N   1 
ATOM   676  N N   D SER   A 1 28  ? -5.843  -9.928  -26.714 0.28 55.10  ? 71  SER   A N   1 
ATOM   677  C CA  A SER   A 1 28  ? -5.868  -10.265 -25.583 0.22 34.65  ? 71  SER   A CA  1 
ATOM   678  C CA  B SER   A 1 28  ? -5.868  -10.265 -25.583 0.22 34.66  ? 71  SER   A CA  1 
ATOM   679  C CA  C SER   A 1 28  ? -6.230  -10.812 -25.579 0.28 57.20  ? 71  SER   A CA  1 
ATOM   680  C CA  D SER   A 1 28  ? -6.230  -10.812 -25.579 0.28 57.22  ? 71  SER   A CA  1 
ATOM   681  C C   A SER   A 1 28  ? -4.841  -10.734 -24.554 0.22 34.81  ? 71  SER   A C   1 
ATOM   682  C C   B SER   A 1 28  ? -4.841  -10.734 -24.554 0.22 34.82  ? 71  SER   A C   1 
ATOM   683  C C   C SER   A 1 28  ? -4.986  -11.252 -24.810 0.28 60.33  ? 71  SER   A C   1 
ATOM   684  C C   D SER   A 1 28  ? -4.986  -11.252 -24.810 0.28 60.34  ? 71  SER   A C   1 
ATOM   685  O O   A SER   A 1 28  ? -4.700  -11.929 -24.326 0.22 35.67  ? 71  SER   A O   1 
ATOM   686  O O   B SER   A 1 28  ? -4.700  -11.929 -24.326 0.22 35.67  ? 71  SER   A O   1 
ATOM   687  O O   C SER   A 1 28  ? -4.529  -12.381 -24.970 0.28 65.72  ? 71  SER   A O   1 
ATOM   688  O O   D SER   A 1 28  ? -4.529  -12.381 -24.970 0.28 65.69  ? 71  SER   A O   1 
ATOM   689  C CB  A SER   A 1 28  ? -6.573  -11.440 -26.223 0.22 34.99  ? 71  SER   A CB  1 
ATOM   690  C CB  B SER   A 1 28  ? -6.573  -11.440 -26.223 0.22 35.00  ? 71  SER   A CB  1 
ATOM   691  C CB  C SER   A 1 28  ? -7.005  -12.013 -26.062 0.28 55.18  ? 71  SER   A CB  1 
ATOM   692  C CB  D SER   A 1 28  ? -7.005  -12.013 -26.062 0.28 55.21  ? 71  SER   A CB  1 
ATOM   693  O OG  A SER   A 1 28  ? -7.332  -11.027 -27.354 0.22 36.94  ? 71  SER   A OG  1 
ATOM   694  O OG  B SER   A 1 28  ? -7.332  -11.027 -27.354 0.22 36.94  ? 71  SER   A OG  1 
ATOM   695  O OG  C SER   A 1 28  ? -8.112  -11.641 -26.870 0.28 54.84  ? 71  SER   A OG  1 
ATOM   696  O OG  D SER   A 1 28  ? -8.112  -11.640 -26.870 0.28 54.86  ? 71  SER   A OG  1 
ATOM   697  N N   A PRO   A 1 29  ? -4.135  -9.815  -23.859 0.22 35.11  ? 72  PRO   A N   1 
ATOM   698  N N   B PRO   A 1 29  ? -4.135  -9.815  -23.858 0.22 35.12  ? 72  PRO   A N   1 
ATOM   699  N N   C PRO   A 1 29  ? -4.399  -10.385 -23.954 0.28 62.88  ? 72  PRO   A N   1 
ATOM   700  N N   D PRO   A 1 29  ? -4.399  -10.385 -23.954 0.28 62.91  ? 72  PRO   A N   1 
ATOM   701  C CA  A PRO   A 1 29  ? -3.002  -10.192 -23.013 0.22 36.63  ? 72  PRO   A CA  1 
ATOM   702  C CA  B PRO   A 1 29  ? -3.002  -10.192 -23.013 0.22 36.63  ? 72  PRO   A CA  1 
ATOM   703  C CA  C PRO   A 1 29  ? -3.200  -10.741 -23.196 0.28 67.02  ? 72  PRO   A CA  1 
ATOM   704  C CA  D PRO   A 1 29  ? -3.199  -10.741 -23.196 0.28 67.03  ? 72  PRO   A CA  1 
ATOM   705  C C   A PRO   A 1 29  ? -3.381  -10.954 -21.729 0.22 37.87  ? 72  PRO   A C   1 
ATOM   706  C C   B PRO   A 1 29  ? -3.381  -10.954 -21.729 0.22 37.87  ? 72  PRO   A C   1 
ATOM   707  C C   C PRO   A 1 29  ? -3.481  -11.597 -21.949 0.28 69.62  ? 72  PRO   A C   1 
ATOM   708  C C   D PRO   A 1 29  ? -3.481  -11.596 -21.948 0.28 69.64  ? 72  PRO   A C   1 
ATOM   709  O O   A PRO   A 1 29  ? -4.369  -10.599 -21.088 0.22 32.76  ? 72  PRO   A O   1 
ATOM   710  O O   B PRO   A 1 29  ? -4.369  -10.598 -21.087 0.22 32.79  ? 72  PRO   A O   1 
ATOM   711  O O   C PRO   A 1 29  ? -4.582  -11.539 -21.433 0.28 64.68  ? 72  PRO   A O   1 
ATOM   712  O O   D PRO   A 1 29  ? -4.581  -11.536 -21.432 0.28 64.72  ? 72  PRO   A O   1 
ATOM   713  C CB  A PRO   A 1 29  ? -2.358  -8.835  -22.680 0.22 36.84  ? 72  PRO   A CB  1 
ATOM   714  C CB  B PRO   A 1 29  ? -2.358  -8.835  -22.680 0.22 36.84  ? 72  PRO   A CB  1 
ATOM   715  C CB  C PRO   A 1 29  ? -2.634  -9.367  -22.802 0.28 67.32  ? 72  PRO   A CB  1 
ATOM   716  C CB  D PRO   A 1 29  ? -2.634  -9.367  -22.802 0.28 67.33  ? 72  PRO   A CB  1 
ATOM   717  C CG  A PRO   A 1 29  ? -3.516  -7.853  -22.709 0.22 36.87  ? 72  PRO   A CG  1 
ATOM   718  C CG  B PRO   A 1 29  ? -3.516  -7.853  -22.709 0.22 36.87  ? 72  PRO   A CG  1 
ATOM   719  C CG  C PRO   A 1 29  ? -3.861  -8.490  -22.653 0.28 68.82  ? 72  PRO   A CG  1 
ATOM   720  C CG  D PRO   A 1 29  ? -3.861  -8.490  -22.653 0.28 68.80  ? 72  PRO   A CG  1 
ATOM   721  C CD  A PRO   A 1 29  ? -4.419  -8.370  -23.814 0.22 36.75  ? 72  PRO   A CD  1 
ATOM   722  C CD  B PRO   A 1 29  ? -4.419  -8.370  -23.813 0.22 36.75  ? 72  PRO   A CD  1 
ATOM   723  C CD  C PRO   A 1 29  ? -4.849  -9.011  -23.680 0.28 67.26  ? 72  PRO   A CD  1 
ATOM   724  C CD  D PRO   A 1 29  ? -4.849  -9.011  -23.680 0.28 67.25  ? 72  PRO   A CD  1 
ATOM   725  N N   A ARG   A 1 30  ? -2.582  -11.973 -21.388 0.22 39.36  ? 73  ARG   A N   1 
ATOM   726  N N   B ARG   A 1 30  ? -2.582  -11.973 -21.388 0.22 39.36  ? 73  ARG   A N   1 
ATOM   727  N N   C ARG   A 1 30  ? -2.476  -12.362 -21.506 0.28 77.31  ? 73  ARG   A N   1 
ATOM   728  N N   D ARG   A 1 30  ? -2.476  -12.362 -21.506 0.28 77.32  ? 73  ARG   A N   1 
ATOM   729  C CA  A ARG   A 1 30  ? -2.683  -12.769 -20.131 0.22 43.13  ? 73  ARG   A CA  1 
ATOM   730  C CA  B ARG   A 1 30  ? -2.683  -12.769 -20.131 0.22 43.12  ? 73  ARG   A CA  1 
ATOM   731  C CA  C ARG   A 1 30  ? -2.487  -13.166 -20.251 0.28 83.36  ? 73  ARG   A CA  1 
ATOM   732  C CA  D ARG   A 1 30  ? -2.487  -13.166 -20.251 0.28 83.36  ? 73  ARG   A CA  1 
ATOM   733  C C   A ARG   A 1 30  ? -1.687  -12.192 -19.120 0.22 43.07  ? 73  ARG   A C   1 
ATOM   734  C C   B ARG   A 1 30  ? -1.687  -12.192 -19.120 0.22 43.06  ? 73  ARG   A C   1 
ATOM   735  C C   C ARG   A 1 30  ? -1.532  -12.517 -19.243 0.28 82.32  ? 73  ARG   A C   1 
ATOM   736  C C   D ARG   A 1 30  ? -1.531  -12.517 -19.243 0.28 82.33  ? 73  ARG   A C   1 
ATOM   737  O O   A ARG   A 1 30  ? -0.480  -12.258 -19.390 0.22 41.70  ? 73  ARG   A O   1 
ATOM   738  O O   B ARG   A 1 30  ? -0.480  -12.258 -19.390 0.22 41.71  ? 73  ARG   A O   1 
ATOM   739  O O   C ARG   A 1 30  ? -0.341  -12.875 -19.245 0.28 83.89  ? 73  ARG   A O   1 
ATOM   740  O O   D ARG   A 1 30  ? -0.341  -12.875 -19.245 0.28 83.89  ? 73  ARG   A O   1 
ATOM   741  C CB  A ARG   A 1 30  ? -2.414  -14.251 -20.408 0.22 46.01  ? 73  ARG   A CB  1 
ATOM   742  C CB  B ARG   A 1 30  ? -2.414  -14.250 -20.407 0.22 46.00  ? 73  ARG   A CB  1 
ATOM   743  C CB  C ARG   A 1 30  ? -2.100  -14.622 -20.539 0.28 91.63  ? 73  ARG   A CB  1 
ATOM   744  C CB  D ARG   A 1 30  ? -2.100  -14.621 -20.539 0.28 91.62  ? 73  ARG   A CB  1 
ATOM   745  C CG  A ARG   A 1 30  ? -3.332  -14.851 -21.464 0.22 49.08  ? 73  ARG   A CG  1 
ATOM   746  C CG  B ARG   A 1 30  ? -3.333  -14.852 -21.462 0.22 49.06  ? 73  ARG   A CG  1 
ATOM   747  C CG  C ARG   A 1 30  ? -3.280  -15.578 -20.635 0.28 99.62  ? 73  ARG   A CG  1 
ATOM   748  C CG  D ARG   A 1 30  ? -3.280  -15.577 -20.635 0.28 99.59  ? 73  ARG   A CG  1 
ATOM   749  C CD  A ARG   A 1 30  ? -2.894  -16.235 -21.914 0.22 52.41  ? 73  ARG   A CD  1 
ATOM   750  C CD  B ARG   A 1 30  ? -2.894  -16.234 -21.915 0.22 52.38  ? 73  ARG   A CD  1 
ATOM   751  C CD  C ARG   A 1 30  ? -4.322  -15.137 -21.650 0.28 107.21 ? 73  ARG   A CD  1 
ATOM   752  C CD  D ARG   A 1 30  ? -4.322  -15.137 -21.650 0.28 107.16 ? 73  ARG   A CD  1 
ATOM   753  N NE  A ARG   A 1 30  ? -3.891  -16.862 -22.779 0.22 53.83  ? 73  ARG   A NE  1 
ATOM   754  N NE  B ARG   A 1 30  ? -3.891  -16.862 -22.779 0.22 53.80  ? 73  ARG   A NE  1 
ATOM   755  N NE  C ARG   A 1 30  ? -5.181  -16.235 -22.084 0.28 114.50 ? 73  ARG   A NE  1 
ATOM   756  N NE  D ARG   A 1 30  ? -5.181  -16.235 -22.084 0.28 114.43 ? 73  ARG   A NE  1 
ATOM   757  C CZ  A ARG   A 1 30  ? -5.024  -17.423 -22.358 0.22 53.26  ? 73  ARG   A CZ  1 
ATOM   758  C CZ  B ARG   A 1 30  ? -5.024  -17.423 -22.358 0.22 53.25  ? 73  ARG   A CZ  1 
ATOM   759  C CZ  C ARG   A 1 30  ? -4.858  -17.160 -22.989 0.28 118.70 ? 73  ARG   A CZ  1 
ATOM   760  C CZ  D ARG   A 1 30  ? -4.858  -17.160 -22.989 0.28 118.64 ? 73  ARG   A CZ  1 
ATOM   761  N NH1 A ARG   A 1 30  ? -5.323  -17.439 -21.068 0.22 54.15  ? 73  ARG   A NH1 1 
ATOM   762  N NH1 B ARG   A 1 30  ? -5.322  -17.439 -21.067 0.22 54.13  ? 73  ARG   A NH1 1 
ATOM   763  N NH1 C ARG   A 1 30  ? -3.675  -17.141 -23.584 0.28 121.86 ? 73  ARG   A NH1 1 
ATOM   764  N NH1 D ARG   A 1 30  ? -3.675  -17.141 -23.584 0.28 121.79 ? 73  ARG   A NH1 1 
ATOM   765  N NH2 A ARG   A 1 30  ? -5.864  -17.960 -23.232 0.22 49.01  ? 73  ARG   A NH2 1 
ATOM   766  N NH2 B ARG   A 1 30  ? -5.863  -17.960 -23.232 0.22 49.03  ? 73  ARG   A NH2 1 
ATOM   767  N NH2 C ARG   A 1 30  ? -5.729  -18.107 -23.301 0.28 116.76 ? 73  ARG   A NH2 1 
ATOM   768  N NH2 D ARG   A 1 30  ? -5.729  -18.107 -23.300 0.28 116.73 ? 73  ARG   A NH2 1 
ATOM   769  N N   A LEU   A 1 31  ? -2.185  -11.615 -18.021 0.22 42.15  ? 74  LEU   A N   1 
ATOM   770  N N   B LEU   A 1 31  ? -2.185  -11.615 -18.021 0.22 42.15  ? 74  LEU   A N   1 
ATOM   771  N N   C LEU   A 1 31  ? -2.043  -11.590 -18.424 0.28 84.06  ? 74  LEU   A N   1 
ATOM   772  N N   D LEU   A 1 31  ? -2.042  -11.590 -18.424 0.28 84.05  ? 74  LEU   A N   1 
ATOM   773  C CA  A LEU   A 1 31  ? -1.384  -10.779 -17.089 0.22 42.48  ? 74  LEU   A CA  1 
ATOM   774  C CA  B LEU   A 1 31  ? -1.383  -10.779 -17.089 0.22 42.47  ? 74  LEU   A CA  1 
ATOM   775  C CA  C LEU   A 1 31  ? -1.254  -10.797 -17.442 0.28 82.78  ? 74  LEU   A CA  1 
ATOM   776  C CA  D LEU   A 1 31  ? -1.254  -10.797 -17.442 0.28 82.77  ? 74  LEU   A CA  1 
ATOM   777  C C   A LEU   A 1 31  ? -1.609  -11.238 -15.644 0.22 40.23  ? 74  LEU   A C   1 
ATOM   778  C C   B LEU   A 1 31  ? -1.609  -11.238 -15.644 0.22 40.23  ? 74  LEU   A C   1 
ATOM   779  C C   C LEU   A 1 31  ? -1.409  -11.410 -16.044 0.28 79.55  ? 74  LEU   A C   1 
ATOM   780  C C   D LEU   A 1 31  ? -1.409  -11.410 -16.044 0.28 79.54  ? 74  LEU   A C   1 
ATOM   781  O O   A LEU   A 1 31  ? -2.779  -11.271 -15.208 0.22 36.83  ? 74  LEU   A O   1 
ATOM   782  O O   B LEU   A 1 31  ? -2.778  -11.271 -15.208 0.22 36.85  ? 74  LEU   A O   1 
ATOM   783  O O   C LEU   A 1 31  ? -2.528  -11.850 -15.710 0.28 76.45  ? 74  LEU   A O   1 
ATOM   784  O O   D LEU   A 1 31  ? -2.528  -11.850 -15.710 0.28 76.46  ? 74  LEU   A O   1 
ATOM   785  C CB  A LEU   A 1 31  ? -1.783  -9.313  -17.273 0.22 44.30  ? 74  LEU   A CB  1 
ATOM   786  C CB  B LEU   A 1 31  ? -1.783  -9.313  -17.273 0.22 44.29  ? 74  LEU   A CB  1 
ATOM   787  C CB  C LEU   A 1 31  ? -1.734  -9.342  -17.467 0.28 84.81  ? 74  LEU   A CB  1 
ATOM   788  C CB  D LEU   A 1 31  ? -1.734  -9.342  -17.467 0.28 84.79  ? 74  LEU   A CB  1 
ATOM   789  C CG  A LEU   A 1 31  ? -1.500  -8.715  -18.652 0.22 45.35  ? 74  LEU   A CG  1 
ATOM   790  C CG  B LEU   A 1 31  ? -1.500  -8.715  -18.652 0.22 45.35  ? 74  LEU   A CG  1 
ATOM   791  C CG  C LEU   A 1 31  ? -1.488  -8.582  -18.772 0.28 86.78  ? 74  LEU   A CG  1 
ATOM   792  C CG  D LEU   A 1 31  ? -1.488  -8.582  -18.772 0.28 86.76  ? 74  LEU   A CG  1 
ATOM   793  C CD1 A LEU   A 1 31  ? -2.180  -7.362  -18.798 0.22 46.06  ? 74  LEU   A CD1 1 
ATOM   794  C CD1 B LEU   A 1 31  ? -2.180  -7.362  -18.798 0.22 46.05  ? 74  LEU   A CD1 1 
ATOM   795  C CD1 C LEU   A 1 31  ? -2.223  -7.249  -18.768 0.28 87.23  ? 74  LEU   A CD1 1 
ATOM   796  C CD1 D LEU   A 1 31  ? -2.223  -7.249  -18.768 0.28 87.21  ? 74  LEU   A CD1 1 
ATOM   797  C CD2 A LEU   A 1 31  ? -0.001  -8.589  -18.903 0.22 45.19  ? 74  LEU   A CD2 1 
ATOM   798  C CD2 B LEU   A 1 31  ? -0.001  -8.589  -18.903 0.22 45.19  ? 74  LEU   A CD2 1 
ATOM   799  C CD2 C LEU   A 1 31  ? 0.000   -8.366  -19.015 0.28 85.59  ? 74  LEU   A CD2 1 
ATOM   800  C CD2 D LEU   A 1 31  ? 0.000   -8.366  -19.015 0.28 85.58  ? 74  LEU   A CD2 1 
ATOM   801  N N   A ASP   A 1 32  ? -0.521  -11.591 -14.953 0.22 38.97  ? 75  ASP   A N   1 
ATOM   802  N N   B ASP   A 1 32  ? -0.521  -11.591 -14.953 0.22 38.97  ? 75  ASP   A N   1 
ATOM   803  N N   C ASP   A 1 32  ? -0.314  -11.444 -15.276 0.28 74.36  ? 75  ASP   A N   1 
ATOM   804  N N   D ASP   A 1 32  ? -0.314  -11.444 -15.276 0.28 74.37  ? 75  ASP   A N   1 
ATOM   805  C CA  A ASP   A 1 32  ? -0.487  -11.870 -13.492 0.22 38.65  ? 75  ASP   A CA  1 
ATOM   806  C CA  B ASP   A 1 32  ? -0.486  -11.870 -13.492 0.22 38.65  ? 75  ASP   A CA  1 
ATOM   807  C CA  C ASP   A 1 32  ? -0.268  -11.900 -13.860 0.28 72.94  ? 75  ASP   A CA  1 
ATOM   808  C CA  D ASP   A 1 32  ? -0.268  -11.901 -13.860 0.28 72.93  ? 75  ASP   A CA  1 
ATOM   809  C C   A ASP   A 1 32  ? -0.603  -10.540 -12.745 0.22 35.94  ? 75  ASP   A C   1 
ATOM   810  C C   B ASP   A 1 32  ? -0.603  -10.540 -12.745 0.22 35.94  ? 75  ASP   A C   1 
ATOM   811  C C   C ASP   A 1 32  ? -0.490  -10.683 -12.958 0.28 64.68  ? 75  ASP   A C   1 
ATOM   812  C C   D ASP   A 1 32  ? -0.490  -10.683 -12.958 0.28 64.69  ? 75  ASP   A C   1 
ATOM   813  O O   A ASP   A 1 32  ? 0.323   -9.707  -12.875 0.22 37.07  ? 75  ASP   A O   1 
ATOM   814  O O   B ASP   A 1 32  ? 0.323   -9.707  -12.875 0.22 37.07  ? 75  ASP   A O   1 
ATOM   815  O O   C ASP   A 1 32  ? 0.403   -9.806  -12.924 0.28 66.41  ? 75  ASP   A O   1 
ATOM   816  O O   D ASP   A 1 32  ? 0.403   -9.806  -12.924 0.28 66.41  ? 75  ASP   A O   1 
ATOM   817  C CB  A ASP   A 1 32  ? 0.803   -12.590 -13.077 0.22 40.21  ? 75  ASP   A CB  1 
ATOM   818  C CB  B ASP   A 1 32  ? 0.803   -12.590 -13.077 0.22 40.20  ? 75  ASP   A CB  1 
ATOM   819  C CB  C ASP   A 1 32  ? 1.065   -12.584 -13.546 0.28 76.09  ? 75  ASP   A CB  1 
ATOM   820  C CB  D ASP   A 1 32  ? 1.065   -12.584 -13.546 0.28 76.07  ? 75  ASP   A CB  1 
ATOM   821  C CG  A ASP   A 1 32  ? 0.794   -14.094 -13.286 0.22 40.52  ? 75  ASP   A CG  1 
ATOM   822  C CG  B ASP   A 1 32  ? 0.794   -14.094 -13.287 0.22 40.52  ? 75  ASP   A CG  1 
ATOM   823  C CG  C ASP   A 1 32  ? 1.327   -13.831 -14.370 0.28 77.66  ? 75  ASP   A CG  1 
ATOM   824  C CG  D ASP   A 1 32  ? 1.327   -13.831 -14.370 0.28 77.65  ? 75  ASP   A CG  1 
ATOM   825  O OD1 A ASP   A 1 32  ? -0.294  -14.654 -13.539 0.22 39.55  ? 75  ASP   A OD1 1 
ATOM   826  O OD1 B ASP   A 1 32  ? -0.293  -14.653 -13.543 0.22 39.56  ? 75  ASP   A OD1 1 
ATOM   827  O OD1 C ASP   A 1 32  ? 0.376   -14.614 -14.563 0.28 81.16  ? 75  ASP   A OD1 1 
ATOM   828  O OD1 D ASP   A 1 32  ? 0.377   -14.617 -14.558 0.28 81.13  ? 75  ASP   A OD1 1 
ATOM   829  O OD2 A ASP   A 1 32  ? 1.881   -14.703 -13.166 0.22 45.49  ? 75  ASP   A OD2 1 
ATOM   830  O OD2 B ASP   A 1 32  ? 1.881   -14.704 -13.163 0.22 45.47  ? 75  ASP   A OD2 1 
ATOM   831  O OD2 C ASP   A 1 32  ? 2.482   -14.006 -14.814 0.28 82.67  ? 75  ASP   A OD2 1 
ATOM   832  O OD2 D ASP   A 1 32  ? 2.480   -14.003 -14.819 0.28 82.64  ? 75  ASP   A OD2 1 
ATOM   833  N N   A VAL   A 1 33  ? -1.688  -10.348 -11.992 0.22 34.73  ? 76  VAL   A N   1 
ATOM   834  N N   B VAL   A 1 33  ? -1.688  -10.348 -11.992 0.22 34.74  ? 76  VAL   A N   1 
ATOM   835  N N   C VAL   A 1 33  ? -1.627  -10.633 -12.256 0.28 58.09  ? 76  VAL   A N   1 
ATOM   836  N N   D VAL   A 1 33  ? -1.627  -10.633 -12.256 0.28 58.11  ? 76  VAL   A N   1 
ATOM   837  C CA  A VAL   A 1 33  ? -1.964  -9.067  -11.277 0.22 35.22  ? 76  VAL   A CA  1 
ATOM   838  C CA  B VAL   A 1 33  ? -1.964  -9.067  -11.277 0.22 35.21  ? 76  VAL   A CA  1 
ATOM   839  C CA  C VAL   A 1 33  ? -2.145  -9.392  -11.607 0.28 56.71  ? 76  VAL   A CA  1 
ATOM   840  C CA  D VAL   A 1 33  ? -2.145  -9.392  -11.607 0.28 56.71  ? 76  VAL   A CA  1 
ATOM   841  C C   A VAL   A 1 33  ? -2.301  -9.364  -9.813  0.22 33.02  ? 76  VAL   A C   1 
ATOM   842  C C   B VAL   A 1 33  ? -2.301  -9.364  -9.813  0.22 33.02  ? 76  VAL   A C   1 
ATOM   843  C C   C VAL   A 1 33  ? -2.377  -9.638  -10.109 0.28 53.53  ? 76  VAL   A C   1 
ATOM   844  C C   D VAL   A 1 33  ? -2.377  -9.638  -10.109 0.28 53.54  ? 76  VAL   A C   1 
ATOM   845  O O   A VAL   A 1 33  ? -2.774  -10.483 -9.526  0.22 34.04  ? 76  VAL   A O   1 
ATOM   846  O O   B VAL   A 1 33  ? -2.774  -10.483 -9.526  0.22 34.04  ? 76  VAL   A O   1 
ATOM   847  O O   C VAL   A 1 33  ? -2.736  -10.774 -9.739  0.28 53.79  ? 76  VAL   A O   1 
ATOM   848  O O   D VAL   A 1 33  ? -2.736  -10.774 -9.739  0.28 53.79  ? 76  VAL   A O   1 
ATOM   849  C CB  A VAL   A 1 33  ? -3.094  -8.271  -11.959 0.22 34.07  ? 76  VAL   A CB  1 
ATOM   850  C CB  B VAL   A 1 33  ? -3.095  -8.271  -11.959 0.22 34.07  ? 76  VAL   A CB  1 
ATOM   851  C CB  C VAL   A 1 33  ? -3.430  -8.901  -12.304 0.28 54.90  ? 76  VAL   A CB  1 
ATOM   852  C CB  D VAL   A 1 33  ? -3.430  -8.901  -12.304 0.28 54.91  ? 76  VAL   A CB  1 
ATOM   853  C CG1 A VAL   A 1 33  ? -2.769  -7.978  -13.416 0.22 33.59  ? 76  VAL   A CG1 1 
ATOM   854  C CG1 B VAL   A 1 33  ? -2.769  -7.978  -13.416 0.22 33.60  ? 76  VAL   A CG1 1 
ATOM   855  C CG1 C VAL   A 1 33  ? -3.794  -7.488  -11.881 0.28 54.90  ? 76  VAL   A CG1 1 
ATOM   856  C CG1 D VAL   A 1 33  ? -3.794  -7.488  -11.881 0.28 54.90  ? 76  VAL   A CG1 1 
ATOM   857  C CG2 A VAL   A 1 33  ? -4.442  -8.971  -11.828 0.22 33.86  ? 76  VAL   A CG2 1 
ATOM   858  C CG2 B VAL   A 1 33  ? -4.442  -8.971  -11.829 0.22 33.86  ? 76  VAL   A CG2 1 
ATOM   859  C CG2 C VAL   A 1 33  ? -3.324  -8.984  -13.820 0.28 53.86  ? 76  VAL   A CG2 1 
ATOM   860  C CG2 D VAL   A 1 33  ? -3.324  -8.984  -13.820 0.28 53.88  ? 76  VAL   A CG2 1 
ATOM   861  N N   A ALA   A 1 34  ? -2.087  -8.373  -8.945  0.22 31.86  ? 77  ALA   A N   1 
ATOM   862  N N   B ALA   A 1 34  ? -2.087  -8.373  -8.945  0.22 31.86  ? 77  ALA   A N   1 
ATOM   863  N N   C ALA   A 1 34  ? -2.180  -8.595  -9.295  0.28 49.31  ? 77  ALA   A N   1 
ATOM   864  N N   D ALA   A 1 34  ? -2.180  -8.595  -9.295  0.28 49.33  ? 77  ALA   A N   1 
ATOM   865  C CA  A ALA   A 1 34  ? -2.501  -8.364  -7.521  0.22 31.25  ? 77  ALA   A CA  1 
ATOM   866  C CA  B ALA   A 1 34  ? -2.501  -8.364  -7.521  0.22 31.25  ? 77  ALA   A CA  1 
ATOM   867  C CA  C ALA   A 1 34  ? -2.567  -8.516  -7.864  0.28 50.12  ? 77  ALA   A CA  1 
ATOM   868  C CA  D ALA   A 1 34  ? -2.567  -8.516  -7.865  0.28 50.13  ? 77  ALA   A CA  1 
ATOM   869  C C   A ALA   A 1 34  ? -3.565  -7.279  -7.314  0.22 30.73  ? 77  ALA   A C   1 
ATOM   870  C C   B ALA   A 1 34  ? -3.565  -7.279  -7.314  0.22 30.73  ? 77  ALA   A C   1 
ATOM   871  C C   C ALA   A 1 34  ? -3.554  -7.356  -7.676  0.28 49.25  ? 77  ALA   A C   1 
ATOM   872  C C   D ALA   A 1 34  ? -3.554  -7.356  -7.676  0.28 49.26  ? 77  ALA   A C   1 
ATOM   873  O O   A ALA   A 1 34  ? -3.360  -6.146  -7.807  0.22 28.18  ? 77  ALA   A O   1 
ATOM   874  O O   B ALA   A 1 34  ? -3.360  -6.147  -7.807  0.22 28.19  ? 77  ALA   A O   1 
ATOM   875  O O   C ALA   A 1 34  ? -3.744  -6.591  -8.637  0.28 45.07  ? 77  ALA   A O   1 
ATOM   876  O O   D ALA   A 1 34  ? -3.744  -6.590  -8.637  0.28 45.10  ? 77  ALA   A O   1 
ATOM   877  C CB  A ALA   A 1 34  ? -1.301  -8.125  -6.640  0.22 31.83  ? 77  ALA   A CB  1 
ATOM   878  C CB  B ALA   A 1 34  ? -1.301  -8.126  -6.640  0.22 31.83  ? 77  ALA   A CB  1 
ATOM   879  C CB  C ALA   A 1 34  ? -1.338  -8.334  -7.008  0.28 49.75  ? 77  ALA   A CB  1 
ATOM   880  C CB  D ALA   A 1 34  ? -1.338  -8.335  -7.008  0.28 49.76  ? 77  ALA   A CB  1 
ATOM   881  N N   A LEU   A 1 35  ? -4.648  -7.616  -6.606  0.22 28.99  ? 78  LEU   A N   1 
ATOM   882  N N   B LEU   A 1 35  ? -4.648  -7.616  -6.606  0.22 28.99  ? 78  LEU   A N   1 
ATOM   883  N N   C LEU   A 1 35  ? -4.137  -7.222  -6.480  0.28 48.35  ? 78  LEU   A N   1 
ATOM   884  N N   D LEU   A 1 35  ? -4.137  -7.222  -6.480  0.28 48.36  ? 78  LEU   A N   1 
ATOM   885  C CA  A LEU   A 1 35  ? -5.726  -6.675  -6.203  0.22 28.80  ? 78  LEU   A CA  1 
ATOM   886  C CA  B LEU   A 1 35  ? -5.726  -6.675  -6.203  0.22 28.80  ? 78  LEU   A CA  1 
ATOM   887  C CA  C LEU   A 1 35  ? -5.132  -6.168  -6.140  0.28 48.90  ? 78  LEU   A CA  1 
ATOM   888  C CA  D LEU   A 1 35  ? -5.132  -6.168  -6.140  0.28 48.91  ? 78  LEU   A CA  1 
ATOM   889  C C   A LEU   A 1 35  ? -5.565  -6.378  -4.703  0.22 28.89  ? 78  LEU   A C   1 
ATOM   890  C C   B LEU   A 1 35  ? -5.565  -6.377  -4.703  0.22 28.89  ? 78  LEU   A C   1 
ATOM   891  C C   C LEU   A 1 35  ? -4.908  -5.713  -4.689  0.28 48.81  ? 78  LEU   A C   1 
ATOM   892  C C   D LEU   A 1 35  ? -4.908  -5.713  -4.689  0.28 48.82  ? 78  LEU   A C   1 
ATOM   893  O O   A LEU   A 1 35  ? -5.668  -7.335  -3.892  0.22 27.26  ? 78  LEU   A O   1 
ATOM   894  O O   B LEU   A 1 35  ? -5.668  -7.335  -3.892  0.22 27.27  ? 78  LEU   A O   1 
ATOM   895  O O   C LEU   A 1 35  ? -4.890  -6.576  -3.790  0.28 48.85  ? 78  LEU   A O   1 
ATOM   896  O O   D LEU   A 1 35  ? -4.890  -6.577  -3.790  0.28 48.86  ? 78  LEU   A O   1 
ATOM   897  C CB  A LEU   A 1 35  ? -7.082  -7.309  -6.548  0.22 27.31  ? 78  LEU   A CB  1 
ATOM   898  C CB  B LEU   A 1 35  ? -7.082  -7.309  -6.548  0.22 27.32  ? 78  LEU   A CB  1 
ATOM   899  C CB  C LEU   A 1 35  ? -6.537  -6.745  -6.363  0.28 49.78  ? 78  LEU   A CB  1 
ATOM   900  C CB  D LEU   A 1 35  ? -6.537  -6.745  -6.363  0.28 49.78  ? 78  LEU   A CB  1 
ATOM   901  C CG  A LEU   A 1 35  ? -8.335  -6.523  -6.147  0.22 27.59  ? 78  LEU   A CG  1 
ATOM   902  C CG  B LEU   A 1 35  ? -8.335  -6.523  -6.147  0.22 27.59  ? 78  LEU   A CG  1 
ATOM   903  C CG  C LEU   A 1 35  ? -7.718  -5.798  -6.125  0.28 51.14  ? 78  LEU   A CG  1 
ATOM   904  C CG  D LEU   A 1 35  ? -7.718  -5.799  -6.125  0.28 51.14  ? 78  LEU   A CG  1 
ATOM   905  C CD1 A LEU   A 1 35  ? -8.330  -5.118  -6.724  0.22 26.87  ? 78  LEU   A CD1 1 
ATOM   906  C CD1 B LEU   A 1 35  ? -8.330  -5.118  -6.724  0.22 26.88  ? 78  LEU   A CD1 1 
ATOM   907  C CD1 C LEU   A 1 35  ? -7.672  -4.607  -7.069  0.28 52.07  ? 78  LEU   A CD1 1 
ATOM   908  C CD1 D LEU   A 1 35  ? -7.672  -4.607  -7.069  0.28 52.05  ? 78  LEU   A CD1 1 
ATOM   909  C CD2 A LEU   A 1 35  ? -9.598  -7.265  -6.567  0.22 25.99  ? 78  LEU   A CD2 1 
ATOM   910  C CD2 B LEU   A 1 35  ? -9.598  -7.265  -6.566  0.22 26.00  ? 78  LEU   A CD2 1 
ATOM   911  C CD2 C LEU   A 1 35  ? -9.041  -6.537  -6.278  0.28 50.58  ? 78  LEU   A CD2 1 
ATOM   912  C CD2 D LEU   A 1 35  ? -9.041  -6.537  -6.277  0.28 50.58  ? 78  LEU   A CD2 1 
ATOM   913  N N   A ASP   A 1 36  ? -5.267  -5.114  -4.367  0.22 28.66  ? 79  ASP   A N   1 
ATOM   914  N N   B ASP   A 1 36  ? -5.268  -5.114  -4.367  0.22 28.67  ? 79  ASP   A N   1 
ATOM   915  N N   C ASP   A 1 36  ? -4.722  -4.407  -4.473  0.28 49.50  ? 79  ASP   A N   1 
ATOM   916  N N   D ASP   A 1 36  ? -4.722  -4.408  -4.473  0.28 49.51  ? 79  ASP   A N   1 
ATOM   917  C CA  A ASP   A 1 36  ? -5.007  -4.622  -2.985  0.22 30.36  ? 79  ASP   A CA  1 
ATOM   918  C CA  B ASP   A 1 36  ? -5.007  -4.621  -2.985  0.22 30.36  ? 79  ASP   A CA  1 
ATOM   919  C CA  C ASP   A 1 36  ? -4.484  -3.816  -3.128  0.28 51.61  ? 79  ASP   A CA  1 
ATOM   920  C CA  D ASP   A 1 36  ? -4.483  -3.817  -3.128  0.28 51.62  ? 79  ASP   A CA  1 
ATOM   921  C C   A ASP   A 1 36  ? -6.311  -4.079  -2.371  0.22 29.56  ? 79  ASP   A C   1 
ATOM   922  C C   B ASP   A 1 36  ? -6.311  -4.079  -2.371  0.22 29.57  ? 79  ASP   A C   1 
ATOM   923  C C   C ASP   A 1 36  ? -5.838  -3.561  -2.450  0.28 51.93  ? 79  ASP   A C   1 
ATOM   924  C C   D ASP   A 1 36  ? -5.838  -3.562  -2.450  0.28 51.92  ? 79  ASP   A C   1 
ATOM   925  O O   A ASP   A 1 36  ? -7.329  -4.024  -3.081  0.22 26.71  ? 79  ASP   A O   1 
ATOM   926  O O   B ASP   A 1 36  ? -7.329  -4.025  -3.081  0.22 26.73  ? 79  ASP   A O   1 
ATOM   927  O O   C ASP   A 1 36  ? -6.880  -3.571  -3.140  0.28 48.99  ? 79  ASP   A O   1 
ATOM   928  O O   D ASP   A 1 36  ? -6.879  -3.572  -3.141  0.28 49.01  ? 79  ASP   A O   1 
ATOM   929  C CB  A ASP   A 1 36  ? -3.849  -3.610  -2.978  0.22 31.42  ? 79  ASP   A CB  1 
ATOM   930  C CB  B ASP   A 1 36  ? -3.849  -3.610  -2.978  0.22 31.43  ? 79  ASP   A CB  1 
ATOM   931  C CB  C ASP   A 1 36  ? -3.577  -2.580  -3.203  0.28 54.12  ? 79  ASP   A CB  1 
ATOM   932  C CB  D ASP   A 1 36  ? -3.577  -2.580  -3.203  0.28 54.12  ? 79  ASP   A CB  1 
ATOM   933  C CG  A ASP   A 1 36  ? -4.137  -2.244  -3.590  0.22 34.29  ? 79  ASP   A CG  1 
ATOM   934  C CG  B ASP   A 1 36  ? -4.137  -2.244  -3.590  0.22 34.29  ? 79  ASP   A CG  1 
ATOM   935  C CG  C ASP   A 1 36  ? -4.271  -1.239  -3.398  0.28 55.01  ? 79  ASP   A CG  1 
ATOM   936  C CG  D ASP   A 1 36  ? -4.272  -1.240  -3.400  0.28 55.02  ? 79  ASP   A CG  1 
ATOM   937  O OD1 A ASP   A 1 36  ? -5.283  -2.013  -4.027  0.22 36.62  ? 79  ASP   A OD1 1 
ATOM   938  O OD1 B ASP   A 1 36  ? -5.283  -2.014  -4.027  0.22 36.60  ? 79  ASP   A OD1 1 
ATOM   939  O OD1 C ASP   A 1 36  ? -5.273  -1.186  -4.120  0.28 55.97  ? 79  ASP   A OD1 1 
ATOM   940  O OD1 D ASP   A 1 36  ? -5.272  -1.188  -4.125  0.28 55.97  ? 79  ASP   A OD1 1 
ATOM   941  O OD2 A ASP   A 1 36  ? -3.201  -1.415  -3.631  0.22 35.80  ? 79  ASP   A OD2 1 
ATOM   942  O OD2 B ASP   A 1 36  ? -3.201  -1.415  -3.632  0.22 35.79  ? 79  ASP   A OD2 1 
ATOM   943  O OD2 C ASP   A 1 36  ? -3.789  -0.249  -2.825  0.28 63.06  ? 79  ASP   A OD2 1 
ATOM   944  O OD2 D ASP   A 1 36  ? -3.792  -0.249  -2.825  0.28 63.01  ? 79  ASP   A OD2 1 
ATOM   945  N N   A GLU   A 1 37  ? -6.270  -3.691  -1.090  0.22 29.44  ? 80  GLU   A N   1 
ATOM   946  N N   B GLU   A 1 37  ? -6.270  -3.691  -1.090  0.22 29.45  ? 80  GLU   A N   1 
ATOM   947  N N   C GLU   A 1 37  ? -5.812  -3.347  -1.133  0.28 51.66  ? 80  GLU   A N   1 
ATOM   948  N N   D GLU   A 1 37  ? -5.812  -3.347  -1.134  0.28 51.66  ? 80  GLU   A N   1 
ATOM   949  C CA  A GLU   A 1 37  ? -7.445  -3.247  -0.292  0.22 31.10  ? 80  GLU   A CA  1 
ATOM   950  C CA  B GLU   A 1 37  ? -7.445  -3.247  -0.292  0.22 31.11  ? 80  GLU   A CA  1 
ATOM   951  C CA  C GLU   A 1 37  ? -7.015  -3.167  -0.282  0.28 51.68  ? 80  GLU   A CA  1 
ATOM   952  C CA  D GLU   A 1 37  ? -7.015  -3.167  -0.283  0.28 51.68  ? 80  GLU   A CA  1 
ATOM   953  C C   A GLU   A 1 37  ? -8.044  -1.964  -0.900  0.22 30.58  ? 80  GLU   A C   1 
ATOM   954  C C   B GLU   A 1 37  ? -8.044  -1.964  -0.900  0.22 30.59  ? 80  GLU   A C   1 
ATOM   955  C C   C GLU   A 1 37  ? -7.781  -1.914  -0.738  0.28 49.93  ? 80  GLU   A C   1 
ATOM   956  C C   D GLU   A 1 37  ? -7.781  -1.914  -0.738  0.28 49.93  ? 80  GLU   A C   1 
ATOM   957  O O   A GLU   A 1 37  ? -9.265  -1.795  -0.764  0.22 30.55  ? 80  GLU   A O   1 
ATOM   958  O O   B GLU   A 1 37  ? -9.265  -1.795  -0.764  0.22 30.56  ? 80  GLU   A O   1 
ATOM   959  O O   C GLU   A 1 37  ? -8.990  -1.840  -0.457  0.28 47.86  ? 80  GLU   A O   1 
ATOM   960  O O   D GLU   A 1 37  ? -8.990  -1.840  -0.458  0.28 47.87  ? 80  GLU   A O   1 
ATOM   961  C CB  A GLU   A 1 37  ? -7.029  -3.093  1.177   0.22 31.64  ? 80  GLU   A CB  1 
ATOM   962  C CB  B GLU   A 1 37  ? -7.029  -3.093  1.177   0.22 31.65  ? 80  GLU   A CB  1 
ATOM   963  C CB  C GLU   A 1 37  ? -6.579  -3.092  1.183   0.28 53.20  ? 80  GLU   A CB  1 
ATOM   964  C CB  D GLU   A 1 37  ? -6.579  -3.092  1.183   0.28 53.20  ? 80  GLU   A CB  1 
ATOM   965  C CG  A GLU   A 1 37  ? -8.128  -2.609  2.114   0.22 33.96  ? 80  GLU   A CG  1 
ATOM   966  C CG  B GLU   A 1 37  ? -8.128  -2.609  2.113   0.22 33.96  ? 80  GLU   A CG  1 
ATOM   967  C CG  C GLU   A 1 37  ? -7.633  -3.546  2.170   0.28 54.68  ? 80  GLU   A CG  1 
ATOM   968  C CG  D GLU   A 1 37  ? -7.633  -3.545  2.170   0.28 54.68  ? 80  GLU   A CG  1 
ATOM   969  C CD  A GLU   A 1 37  ? -7.755  -2.572  3.593   0.22 35.37  ? 80  GLU   A CD  1 
ATOM   970  C CD  B GLU   A 1 37  ? -7.755  -2.572  3.593   0.22 35.37  ? 80  GLU   A CD  1 
ATOM   971  C CD  C GLU   A 1 37  ? -7.113  -3.684  3.593   0.28 56.79  ? 80  GLU   A CD  1 
ATOM   972  C CD  D GLU   A 1 37  ? -7.113  -3.684  3.593   0.28 56.77  ? 80  GLU   A CD  1 
ATOM   973  O OE1 A GLU   A 1 37  ? -7.422  -1.484  4.098   0.22 34.10  ? 80  GLU   A OE1 1 
ATOM   974  O OE1 B GLU   A 1 37  ? -7.422  -1.484  4.098   0.22 34.10  ? 80  GLU   A OE1 1 
ATOM   975  O OE1 C GLU   A 1 37  ? -6.590  -2.682  4.139   0.28 54.62  ? 80  GLU   A OE1 1 
ATOM   976  O OE1 D GLU   A 1 37  ? -6.593  -2.681  4.140   0.28 54.63  ? 80  GLU   A OE1 1 
ATOM   977  O OE2 A GLU   A 1 37  ? -7.816  -3.634  4.247   0.22 38.07  ? 80  GLU   A OE2 1 
ATOM   978  O OE2 B GLU   A 1 37  ? -7.815  -3.635  4.247   0.22 38.05  ? 80  GLU   A OE2 1 
ATOM   979  O OE2 C GLU   A 1 37  ? -7.220  -4.798  4.151   0.28 60.09  ? 80  GLU   A OE2 1 
ATOM   980  O OE2 D GLU   A 1 37  ? -7.215  -4.799  4.149   0.28 60.06  ? 80  GLU   A OE2 1 
ATOM   981  N N   A SER   A 1 38  ? -7.242  -1.111  -1.562  0.22 32.72  ? 81  SER   A N   1 
ATOM   982  N N   B SER   A 1 38  ? -7.242  -1.111  -1.562  0.22 32.72  ? 81  SER   A N   1 
ATOM   983  N N   C SER   A 1 38  ? -7.107  -0.975  -1.420  0.28 48.56  ? 81  SER   A N   1 
ATOM   984  N N   D SER   A 1 38  ? -7.107  -0.975  -1.420  0.28 48.57  ? 81  SER   A N   1 
ATOM   985  C CA  A SER   A 1 38  ? -7.690  0.160   -2.201  0.22 33.84  ? 81  SER   A CA  1 
ATOM   986  C CA  B SER   A 1 38  ? -7.689  0.160   -2.201  0.22 33.85  ? 81  SER   A CA  1 
ATOM   987  C CA  C SER   A 1 38  ? -7.682  0.299   -1.930  0.28 47.67  ? 81  SER   A CA  1 
ATOM   988  C CA  D SER   A 1 38  ? -7.682  0.299   -1.930  0.28 47.68  ? 81  SER   A CA  1 
ATOM   989  C C   A SER   A 1 38  ? -8.333  -0.095  -3.573  0.22 32.94  ? 81  SER   A C   1 
ATOM   990  C C   B SER   A 1 38  ? -8.333  -0.095  -3.573  0.22 32.95  ? 81  SER   A C   1 
ATOM   991  C C   C SER   A 1 38  ? -8.171  0.154   -3.377  0.28 45.22  ? 81  SER   A C   1 
ATOM   992  C C   D SER   A 1 38  ? -8.171  0.154   -3.377  0.28 45.24  ? 81  SER   A C   1 
ATOM   993  O O   A SER   A 1 38  ? -8.726  0.893   -4.220  0.22 34.40  ? 81  SER   A O   1 
ATOM   994  O O   B SER   A 1 38  ? -8.727  0.893   -4.220  0.22 34.40  ? 81  SER   A O   1 
ATOM   995  O O   C SER   A 1 38  ? -8.357  1.200   -4.021  0.28 47.31  ? 81  SER   A O   1 
ATOM   996  O O   D SER   A 1 38  ? -8.358  1.199   -4.021  0.28 47.31  ? 81  SER   A O   1 
ATOM   997  C CB  A SER   A 1 38  ? -6.554  1.152   -2.320  0.22 37.17  ? 81  SER   A CB  1 
ATOM   998  C CB  B SER   A 1 38  ? -6.554  1.152   -2.320  0.22 37.16  ? 81  SER   A CB  1 
ATOM   999  C CB  C SER   A 1 38  ? -6.681  1.419   -1.818  0.28 51.22  ? 81  SER   A CB  1 
ATOM   1000 C CB  D SER   A 1 38  ? -6.681  1.419   -1.818  0.28 51.21  ? 81  SER   A CB  1 
ATOM   1001 O OG  A SER   A 1 38  ? -6.149  1.611   -1.039  0.22 40.49  ? 81  SER   A OG  1 
ATOM   1002 O OG  B SER   A 1 38  ? -6.149  1.611   -1.038  0.22 40.46  ? 81  SER   A OG  1 
ATOM   1003 O OG  C SER   A 1 38  ? -6.189  1.522   -0.488  0.28 53.86  ? 81  SER   A OG  1 
ATOM   1004 O OG  D SER   A 1 38  ? -6.189  1.522   -0.488  0.28 53.83  ? 81  SER   A OG  1 
ATOM   1005 N N   A GLY   A 1 39  ? -8.425  -1.356  -4.018  0.22 33.05  ? 82  GLY   A N   1 
ATOM   1006 N N   B GLY   A 1 39  ? -8.425  -1.355  -4.018  0.22 33.06  ? 82  GLY   A N   1 
ATOM   1007 N N   C GLY   A 1 39  ? -8.359  -1.078  -3.869  0.28 44.75  ? 82  GLY   A N   1 
ATOM   1008 N N   D GLY   A 1 39  ? -8.359  -1.078  -3.869  0.28 44.76  ? 82  GLY   A N   1 
ATOM   1009 C CA  A GLY   A 1 39  ? -9.067  -1.741  -5.295  0.22 32.75  ? 82  GLY   A CA  1 
ATOM   1010 C CA  B GLY   A 1 39  ? -9.066  -1.741  -5.294  0.22 32.76  ? 82  GLY   A CA  1 
ATOM   1011 C CA  C GLY   A 1 39  ? -8.952  -1.376  -5.191  0.28 44.61  ? 82  GLY   A CA  1 
ATOM   1012 C CA  D GLY   A 1 39  ? -8.952  -1.376  -5.191  0.28 44.62  ? 82  GLY   A CA  1 
ATOM   1013 C C   A GLY   A 1 39  ? -8.214  -1.412  -6.516  0.22 33.35  ? 82  GLY   A C   1 
ATOM   1014 C C   B GLY   A 1 39  ? -8.214  -1.412  -6.516  0.22 33.36  ? 82  GLY   A C   1 
ATOM   1015 C C   C GLY   A 1 39  ? -8.087  -0.918  -6.361  0.28 43.56  ? 82  GLY   A C   1 
ATOM   1016 C C   D GLY   A 1 39  ? -8.088  -0.918  -6.361  0.28 43.58  ? 82  GLY   A C   1 
ATOM   1017 O O   A GLY   A 1 39  ? -8.754  -1.492  -7.647  0.22 29.46  ? 82  GLY   A O   1 
ATOM   1018 O O   B GLY   A 1 39  ? -8.754  -1.491  -7.647  0.22 29.49  ? 82  GLY   A O   1 
ATOM   1019 O O   C GLY   A 1 39  ? -8.657  -0.472  -7.375  0.28 43.07  ? 82  GLY   A O   1 
ATOM   1020 O O   D GLY   A 1 39  ? -8.657  -0.472  -7.374  0.28 43.09  ? 82  GLY   A O   1 
ATOM   1021 N N   A ASP   A 1 40  ? -6.934  -1.080  -6.311  0.22 35.69  ? 83  ASP   A N   1 
ATOM   1022 N N   B ASP   A 1 40  ? -6.934  -1.080  -6.311  0.22 35.70  ? 83  ASP   A N   1 
ATOM   1023 N N   C ASP   A 1 40  ? -6.764  -1.042  -6.247  0.28 46.10  ? 83  ASP   A N   1 
ATOM   1024 N N   D ASP   A 1 40  ? -6.764  -1.042  -6.247  0.28 46.11  ? 83  ASP   A N   1 
ATOM   1025 C CA  A ASP   A 1 40  ? -5.943  -0.775  -7.382  0.22 39.43  ? 83  ASP   A CA  1 
ATOM   1026 C CA  B ASP   A 1 40  ? -5.943  -0.776  -7.382  0.22 39.43  ? 83  ASP   A CA  1 
ATOM   1027 C CA  C ASP   A 1 40  ? -5.791  -0.747  -7.335  0.28 48.29  ? 83  ASP   A CA  1 
ATOM   1028 C CA  D ASP   A 1 40  ? -5.791  -0.747  -7.335  0.28 48.29  ? 83  ASP   A CA  1 
ATOM   1029 C C   A ASP   A 1 40  ? -5.225  -2.071  -7.781  0.22 41.94  ? 83  ASP   A C   1 
ATOM   1030 C C   B ASP   A 1 40  ? -5.225  -2.071  -7.781  0.22 41.93  ? 83  ASP   A C   1 
ATOM   1031 C C   C ASP   A 1 40  ? -5.157  -2.068  -7.786  0.28 47.21  ? 83  ASP   A C   1 
ATOM   1032 C C   D ASP   A 1 40  ? -5.157  -2.068  -7.786  0.28 47.21  ? 83  ASP   A C   1 
ATOM   1033 O O   A ASP   A 1 40  ? -4.641  -2.723  -6.894  0.22 40.14  ? 83  ASP   A O   1 
ATOM   1034 O O   B ASP   A 1 40  ? -4.640  -2.723  -6.894  0.22 40.15  ? 83  ASP   A O   1 
ATOM   1035 O O   C ASP   A 1 40  ? -4.563  -2.749  -6.928  0.28 44.53  ? 83  ASP   A O   1 
ATOM   1036 O O   D ASP   A 1 40  ? -4.562  -2.749  -6.928  0.28 44.55  ? 83  ASP   A O   1 
ATOM   1037 C CB  A ASP   A 1 40  ? -4.952  0.306   -6.934  0.22 40.29  ? 83  ASP   A CB  1 
ATOM   1038 C CB  B ASP   A 1 40  ? -4.952  0.306   -6.934  0.22 40.29  ? 83  ASP   A CB  1 
ATOM   1039 C CB  C ASP   A 1 40  ? -4.719  0.250   -6.879  0.28 51.79  ? 83  ASP   A CB  1 
ATOM   1040 C CB  D ASP   A 1 40  ? -4.719  0.250   -6.879  0.28 51.78  ? 83  ASP   A CB  1 
ATOM   1041 C CG  A ASP   A 1 40  ? -5.521  1.716   -6.931  0.22 40.80  ? 83  ASP   A CG  1 
ATOM   1042 C CG  B ASP   A 1 40  ? -5.521  1.716   -6.931  0.22 40.79  ? 83  ASP   A CG  1 
ATOM   1043 C CG  C ASP   A 1 40  ? -5.238  1.416   -6.053  0.28 55.05  ? 83  ASP   A CG  1 
ATOM   1044 C CG  D ASP   A 1 40  ? -5.238  1.416   -6.054  0.28 55.03  ? 83  ASP   A CG  1 
ATOM   1045 O OD1 A ASP   A 1 40  ? -6.571  1.927   -7.571  0.22 42.64  ? 83  ASP   A OD1 1 
ATOM   1046 O OD1 B ASP   A 1 40  ? -6.571  1.927   -7.571  0.22 42.63  ? 83  ASP   A OD1 1 
ATOM   1047 O OD1 C ASP   A 1 40  ? -6.190  2.085   -6.503  0.28 57.26  ? 83  ASP   A OD1 1 
ATOM   1048 O OD1 D ASP   A 1 40  ? -6.191  2.084   -6.503  0.28 57.24  ? 83  ASP   A OD1 1 
ATOM   1049 O OD2 A ASP   A 1 40  ? -4.907  2.597   -6.292  0.22 39.74  ? 83  ASP   A OD2 1 
ATOM   1050 O OD2 B ASP   A 1 40  ? -4.907  2.597   -6.292  0.22 39.75  ? 83  ASP   A OD2 1 
ATOM   1051 O OD2 C ASP   A 1 40  ? -4.679  1.648   -4.965  0.28 58.79  ? 83  ASP   A OD2 1 
ATOM   1052 O OD2 D ASP   A 1 40  ? -4.679  1.648   -4.966  0.28 58.76  ? 83  ASP   A OD2 1 
ATOM   1053 N N   . PHE   A 1 41  ? -5.299  -2.432  -9.065  1.00 45.22  ? 84  PHE   A N   1 
ATOM   1054 C CA  . PHE   A 1 41  ? -4.616  -3.621  -9.645  1.00 44.49  ? 84  PHE   A CA  1 
ATOM   1055 C C   . PHE   A 1 41  ? -3.144  -3.278  -9.895  1.00 47.19  ? 84  PHE   A C   1 
ATOM   1056 O O   . PHE   A 1 41  ? -2.834  -2.116  -10.120 1.00 53.24  ? 84  PHE   A O   1 
ATOM   1057 C CB  . PHE   A 1 41  ? -5.256  -4.039  -10.965 1.00 39.32  ? 84  PHE   A CB  1 
ATOM   1058 C CG  . PHE   A 1 41  ? -6.560  -4.791  -10.880 1.00 41.25  ? 84  PHE   A CG  1 
ATOM   1059 C CD1 . PHE   A 1 41  ? -6.581  -6.099  -10.450 1.00 36.66  ? 84  PHE   A CD1 1 
ATOM   1060 C CD2 . PHE   A 1 41  ? -7.767  -4.205  -11.262 1.00 40.07  ? 84  PHE   A CD2 1 
ATOM   1061 C CE1 . PHE   A 1 41  ? -7.769  -6.807  -10.395 1.00 40.09  ? 84  PHE   A CE1 1 
ATOM   1062 C CE2 . PHE   A 1 41  ? -8.954  -4.918  -11.212 1.00 38.43  ? 84  PHE   A CE2 1 
ATOM   1063 C CZ  . PHE   A 1 41  ? -8.954  -6.220  -10.783 1.00 37.97  ? 84  PHE   A CZ  1 
ATOM   1064 N N   A SER   A 1 42  ? -2.249  -4.270  -9.836  0.22 46.35  ? 85  SER   A N   1 
ATOM   1065 N N   B SER   A 1 42  ? -2.249  -4.270  -9.836  0.22 46.35  ? 85  SER   A N   1 
ATOM   1066 N N   C SER   A 1 42  ? -2.287  -4.308  -9.902  0.28 50.17  ? 85  SER   A N   1 
ATOM   1067 N N   D SER   A 1 42  ? -2.287  -4.308  -9.902  0.28 50.17  ? 85  SER   A N   1 
ATOM   1068 C CA  A SER   A 1 42  ? -0.790  -4.083  -10.060 0.22 45.62  ? 85  SER   A CA  1 
ATOM   1069 C CA  B SER   A 1 42  ? -0.790  -4.083  -10.060 0.22 45.63  ? 85  SER   A CA  1 
ATOM   1070 C CA  C SER   A 1 42  ? -0.822  -4.224  -10.147 0.28 52.35  ? 85  SER   A CA  1 
ATOM   1071 C CA  D SER   A 1 42  ? -0.822  -4.224  -10.147 0.28 52.36  ? 85  SER   A CA  1 
ATOM   1072 C C   A SER   A 1 42  ? -0.190  -5.323  -10.730 0.22 45.22  ? 85  SER   A C   1 
ATOM   1073 C C   B SER   A 1 42  ? -0.191  -5.323  -10.730 0.22 45.23  ? 85  SER   A C   1 
ATOM   1074 C C   C SER   A 1 42  ? -0.332  -5.493  -10.860 0.28 55.18  ? 85  SER   A C   1 
ATOM   1075 C C   D SER   A 1 42  ? -0.332  -5.493  -10.860 0.28 55.18  ? 85  SER   A C   1 
ATOM   1076 O O   A SER   A 1 42  ? -0.681  -6.434  -10.469 0.22 42.01  ? 85  SER   A O   1 
ATOM   1077 O O   B SER   A 1 42  ? -0.682  -6.434  -10.469 0.22 42.04  ? 85  SER   A O   1 
ATOM   1078 O O   C SER   A 1 42  ? -0.920  -6.569  -10.631 0.28 51.60  ? 85  SER   A O   1 
ATOM   1079 O O   D SER   A 1 42  ? -0.920  -6.568  -10.631 0.28 51.63  ? 85  SER   A O   1 
ATOM   1080 C CB  A SER   A 1 42  ? -0.082  -3.772  -8.769  0.22 47.59  ? 85  SER   A CB  1 
ATOM   1081 C CB  B SER   A 1 42  ? -0.082  -3.772  -8.769  0.22 47.59  ? 85  SER   A CB  1 
ATOM   1082 C CB  C SER   A 1 42  ? -0.090  -4.022  -8.852  0.28 54.74  ? 85  SER   A CB  1 
ATOM   1083 C CB  D SER   A 1 42  ? -0.090  -4.022  -8.852  0.28 54.73  ? 85  SER   A CB  1 
ATOM   1084 O OG  A SER   A 1 42  ? -0.202  -4.859  -7.862  0.22 48.59  ? 85  SER   A OG  1 
ATOM   1085 O OG  B SER   A 1 42  ? -0.201  -4.859  -7.862  0.22 48.59  ? 85  SER   A OG  1 
ATOM   1086 O OG  C SER   A 1 42  ? -0.437  -5.046  -7.928  0.28 55.13  ? 85  SER   A OG  1 
ATOM   1087 O OG  D SER   A 1 42  ? -0.437  -5.045  -7.928  0.28 55.13  ? 85  SER   A OG  1 
ATOM   1088 N N   A LEU   A 1 43  ? 0.842   -5.131  -11.554 0.22 46.60  ? 86  LEU   A N   1 
ATOM   1089 N N   B LEU   A 1 43  ? 0.842   -5.131  -11.554 0.22 46.61  ? 86  LEU   A N   1 
ATOM   1090 N N   C LEU   A 1 43  ? 0.714   -5.379  -11.684 0.28 61.18  ? 86  LEU   A N   1 
ATOM   1091 N N   D LEU   A 1 43  ? 0.714   -5.379  -11.684 0.28 61.18  ? 86  LEU   A N   1 
ATOM   1092 C CA  A LEU   A 1 43  ? 1.546   -6.237  -12.259 0.22 48.98  ? 86  LEU   A CA  1 
ATOM   1093 C CA  B LEU   A 1 43  ? 1.545   -6.237  -12.259 0.22 48.98  ? 86  LEU   A CA  1 
ATOM   1094 C CA  C LEU   A 1 43  ? 1.324   -6.537  -12.399 0.28 65.00  ? 86  LEU   A CA  1 
ATOM   1095 C CA  D LEU   A 1 43  ? 1.324   -6.537  -12.399 0.28 65.00  ? 86  LEU   A CA  1 
ATOM   1096 C C   A LEU   A 1 43  ? 2.391   -7.019  -11.248 0.22 46.41  ? 86  LEU   A C   1 
ATOM   1097 C C   B LEU   A 1 43  ? 2.391   -7.020  -11.248 0.22 46.42  ? 86  LEU   A C   1 
ATOM   1098 C C   C LEU   A 1 43  ? 2.274   -7.281  -11.453 0.28 64.91  ? 86  LEU   A C   1 
ATOM   1099 C C   D LEU   A 1 43  ? 2.274   -7.281  -11.453 0.28 64.93  ? 86  LEU   A C   1 
ATOM   1100 O O   A LEU   A 1 43  ? 3.319   -6.422  -10.670 0.22 45.41  ? 86  LEU   A O   1 
ATOM   1101 O O   B LEU   A 1 43  ? 3.319   -6.422  -10.671 0.22 45.43  ? 86  LEU   A O   1 
ATOM   1102 O O   C LEU   A 1 43  ? 2.960   -6.614  -10.654 0.28 60.40  ? 86  LEU   A O   1 
ATOM   1103 O O   D LEU   A 1 43  ? 2.960   -6.614  -10.654 0.28 60.44  ? 86  LEU   A O   1 
ATOM   1104 C CB  A LEU   A 1 43  ? 2.407   -5.656  -13.383 0.22 49.92  ? 86  LEU   A CB  1 
ATOM   1105 C CB  B LEU   A 1 43  ? 2.407   -5.656  -13.383 0.22 49.92  ? 86  LEU   A CB  1 
ATOM   1106 C CB  C LEU   A 1 43  ? 2.056   -6.044  -13.650 0.28 66.03  ? 86  LEU   A CB  1 
ATOM   1107 C CB  D LEU   A 1 43  ? 2.056   -6.044  -13.650 0.28 66.03  ? 86  LEU   A CB  1 
ATOM   1108 C CG  A LEU   A 1 43  ? 1.625   -5.037  -14.540 0.22 51.59  ? 86  LEU   A CG  1 
ATOM   1109 C CG  B LEU   A 1 43  ? 1.625   -5.037  -14.540 0.22 51.59  ? 86  LEU   A CG  1 
ATOM   1110 C CG  C LEU   A 1 43  ? 1.150   -5.609  -14.800 0.28 67.64  ? 86  LEU   A CG  1 
ATOM   1111 C CG  D LEU   A 1 43  ? 1.151   -5.609  -14.800 0.28 67.64  ? 86  LEU   A CG  1 
ATOM   1112 C CD1 A LEU   A 1 43  ? 2.512   -4.120  -15.367 0.22 54.61  ? 86  LEU   A CD1 1 
ATOM   1113 C CD1 B LEU   A 1 43  ? 2.512   -4.120  -15.367 0.22 54.59  ? 86  LEU   A CD1 1 
ATOM   1114 C CD1 C LEU   A 1 43  ? 1.933   -4.824  -15.839 0.28 71.19  ? 86  LEU   A CD1 1 
ATOM   1115 C CD1 D LEU   A 1 43  ? 1.934   -4.824  -15.838 0.28 71.16  ? 86  LEU   A CD1 1 
ATOM   1116 C CD2 A LEU   A 1 43  ? 1.008   -6.118  -15.414 0.22 52.00  ? 86  LEU   A CD2 1 
ATOM   1117 C CD2 B LEU   A 1 43  ? 1.008   -6.118  -15.414 0.22 52.00  ? 86  LEU   A CD2 1 
ATOM   1118 C CD2 C LEU   A 1 43  ? 0.467   -6.809  -15.442 0.28 69.00  ? 86  LEU   A CD2 1 
ATOM   1119 C CD2 D LEU   A 1 43  ? 0.467   -6.809  -15.442 0.28 68.98  ? 86  LEU   A CD2 1 
ATOM   1120 N N   A VAL   A 1 44  ? 2.042   -8.289  -11.021 0.22 48.45  ? 87  VAL   A N   1 
ATOM   1121 N N   B VAL   A 1 44  ? 2.042   -8.289  -11.021 0.22 48.46  ? 87  VAL   A N   1 
ATOM   1122 N N   C VAL   A 1 44  ? 2.298   -8.613  -11.551 0.28 72.08  ? 87  VAL   A N   1 
ATOM   1123 N N   D VAL   A 1 44  ? 2.298   -8.613  -11.551 0.28 72.08  ? 87  VAL   A N   1 
ATOM   1124 C CA  A VAL   A 1 44  ? 2.854   -9.274  -10.242 0.22 50.88  ? 87  VAL   A CA  1 
ATOM   1125 C CA  B VAL   A 1 44  ? 2.854   -9.274  -10.242 0.22 50.88  ? 87  VAL   A CA  1 
ATOM   1126 C CA  C VAL   A 1 44  ? 3.162   -9.526  -10.741 0.28 78.84  ? 87  VAL   A CA  1 
ATOM   1127 C CA  D VAL   A 1 44  ? 3.162   -9.526  -10.741 0.28 78.82  ? 87  VAL   A CA  1 
ATOM   1128 C C   A VAL   A 1 44  ? 3.939   -9.817  -11.176 0.22 52.42  ? 87  VAL   A C   1 
ATOM   1129 C C   B VAL   A 1 44  ? 3.939   -9.817  -11.177 0.22 52.41  ? 87  VAL   A C   1 
ATOM   1130 C C   C VAL   A 1 44  ? 4.068   -10.310 -11.701 0.28 81.65  ? 87  VAL   A C   1 
ATOM   1131 C C   D VAL   A 1 44  ? 4.068   -10.310 -11.700 0.28 81.62  ? 87  VAL   A C   1 
ATOM   1132 O O   A VAL   A 1 44  ? 3.605   -10.649 -12.044 0.22 54.63  ? 87  VAL   A O   1 
ATOM   1133 O O   B VAL   A 1 44  ? 3.604   -10.649 -12.044 0.22 54.62  ? 87  VAL   A O   1 
ATOM   1134 O O   C VAL   A 1 44  ? 3.619   -11.353 -12.215 0.28 87.03  ? 87  VAL   A O   1 
ATOM   1135 O O   D VAL   A 1 44  ? 3.619   -11.353 -12.215 0.28 86.99  ? 87  VAL   A O   1 
ATOM   1136 C CB  A VAL   A 1 44  ? 1.984   -10.417 -9.677  0.22 50.03  ? 87  VAL   A CB  1 
ATOM   1137 C CB  B VAL   A 1 44  ? 1.984   -10.417 -9.677  0.22 50.03  ? 87  VAL   A CB  1 
ATOM   1138 C CB  C VAL   A 1 44  ? 2.308   -10.471 -9.870  0.28 78.92  ? 87  VAL   A CB  1 
ATOM   1139 C CB  D VAL   A 1 44  ? 2.308   -10.471 -9.870  0.28 78.90  ? 87  VAL   A CB  1 
ATOM   1140 C CG1 A VAL   A 1 44  ? 2.829   -11.570 -9.143  0.22 49.51  ? 87  VAL   A CG1 1 
ATOM   1141 C CG1 B VAL   A 1 44  ? 2.829   -11.570 -9.143  0.22 49.51  ? 87  VAL   A CG1 1 
ATOM   1142 C CG1 C VAL   A 1 44  ? 3.155   -11.513 -9.149  0.28 78.17  ? 87  VAL   A CG1 1 
ATOM   1143 C CG1 D VAL   A 1 44  ? 3.155   -11.513 -9.149  0.28 78.16  ? 87  VAL   A CG1 1 
ATOM   1144 C CG2 A VAL   A 1 44  ? 1.021   -9.916  -8.612  0.22 48.94  ? 87  VAL   A CG2 1 
ATOM   1145 C CG2 B VAL   A 1 44  ? 1.021   -9.916  -8.612  0.22 48.95  ? 87  VAL   A CG2 1 
ATOM   1146 C CG2 C VAL   A 1 44  ? 1.447   -9.701  -8.878  0.28 78.04  ? 87  VAL   A CG2 1 
ATOM   1147 C CG2 D VAL   A 1 44  ? 1.447   -9.700  -8.878  0.28 78.04  ? 87  VAL   A CG2 1 
ATOM   1148 N N   A GLU   A 1 45  ? 5.178   -9.349  -11.021 0.22 52.64  ? 88  GLU   A N   1 
ATOM   1149 N N   B GLU   A 1 45  ? 5.178   -9.349  -11.022 0.22 52.65  ? 88  GLU   A N   1 
ATOM   1150 N N   C GLU   A 1 45  ? 5.291   -9.825  -11.940 0.28 82.71  ? 88  GLU   A N   1 
ATOM   1151 N N   D GLU   A 1 45  ? 5.290   -9.826  -11.940 0.28 82.69  ? 88  GLU   A N   1 
ATOM   1152 C CA  A GLU   A 1 45  ? 6.317   -9.742  -11.893 0.22 56.87  ? 88  GLU   A CA  1 
ATOM   1153 C CA  B GLU   A 1 45  ? 6.317   -9.742  -11.893 0.22 56.85  ? 88  GLU   A CA  1 
ATOM   1154 C CA  C GLU   A 1 45  ? 6.290   -10.504 -12.814 0.28 82.81  ? 88  GLU   A CA  1 
ATOM   1155 C CA  D GLU   A 1 45  ? 6.290   -10.504 -12.813 0.28 82.79  ? 88  GLU   A CA  1 
ATOM   1156 C C   A GLU   A 1 45  ? 7.334   -10.540 -11.063 0.22 54.69  ? 88  GLU   A C   1 
ATOM   1157 C C   B GLU   A 1 45  ? 7.334   -10.540 -11.064 0.22 54.68  ? 88  GLU   A C   1 
ATOM   1158 C C   C GLU   A 1 45  ? 7.032   -11.575 -12.005 0.28 81.20  ? 88  GLU   A C   1 
ATOM   1159 C C   D GLU   A 1 45  ? 7.032   -11.574 -12.004 0.28 81.19  ? 88  GLU   A C   1 
ATOM   1160 O O   A GLU   A 1 45  ? 7.036   -11.612 -10.519 0.22 50.13  ? 88  GLU   A O   1 
ATOM   1161 O O   B GLU   A 1 45  ? 7.039   -11.615 -10.525 0.22 50.15  ? 88  GLU   A O   1 
ATOM   1162 O O   C GLU   A 1 45  ? 6.449   -12.590 -11.626 0.28 77.37  ? 88  GLU   A O   1 
ATOM   1163 O O   D GLU   A 1 45  ? 6.449   -12.589 -11.624 0.28 77.38  ? 88  GLU   A O   1 
ATOM   1164 C CB  A GLU   A 1 45  ? 6.918   -8.492  -12.535 0.22 56.66  ? 88  GLU   A CB  1 
ATOM   1165 C CB  B GLU   A 1 45  ? 6.918   -8.492  -12.535 0.22 56.65  ? 88  GLU   A CB  1 
ATOM   1166 C CB  C GLU   A 1 45  ? 7.266   -9.490  -13.415 0.28 82.11  ? 88  GLU   A CB  1 
ATOM   1167 C CB  D GLU   A 1 45  ? 7.266   -9.490  -13.415 0.28 82.09  ? 88  GLU   A CB  1 
ATOM   1168 C CG  A GLU   A 1 45  ? 5.933   -7.716  -13.393 0.22 57.78  ? 88  GLU   A CG  1 
ATOM   1169 C CG  B GLU   A 1 45  ? 5.933   -7.716  -13.393 0.22 57.77  ? 88  GLU   A CG  1 
ATOM   1170 C CG  C GLU   A 1 45  ? 6.659   -8.663  -14.533 0.28 81.75  ? 88  GLU   A CG  1 
ATOM   1171 C CG  D GLU   A 1 45  ? 6.658   -8.663  -14.533 0.28 81.73  ? 88  GLU   A CG  1 
ATOM   1172 C CD  A GLU   A 1 45  ? 5.735   -8.256  -14.799 0.22 56.75  ? 88  GLU   A CD  1 
ATOM   1173 C CD  B GLU   A 1 45  ? 5.736   -8.255  -14.799 0.22 56.74  ? 88  GLU   A CD  1 
ATOM   1174 C CD  C GLU   A 1 45  ? 6.517   -9.389  -15.859 0.28 79.52  ? 88  GLU   A CD  1 
ATOM   1175 C CD  D GLU   A 1 45  ? 6.517   -9.389  -15.859 0.28 79.53  ? 88  GLU   A CD  1 
ATOM   1176 O OE1 A GLU   A 1 45  ? 5.008   -9.265  -14.954 0.22 51.19  ? 88  GLU   A OE1 1 
ATOM   1177 O OE1 B GLU   A 1 45  ? 5.004   -9.261  -14.955 0.22 51.21  ? 88  GLU   A OE1 1 
ATOM   1178 O OE1 C GLU   A 1 45  ? 6.400   -8.703  -16.896 0.28 78.68  ? 88  GLU   A OE1 1 
ATOM   1179 O OE1 D GLU   A 1 45  ? 6.407   -8.703  -16.897 0.28 78.69  ? 88  GLU   A OE1 1 
ATOM   1180 O OE2 A GLU   A 1 45  ? 6.311   -7.658  -15.737 0.22 55.45  ? 88  GLU   A OE2 1 
ATOM   1181 O OE2 B GLU   A 1 45  ? 6.317   -7.662  -15.737 0.22 55.45  ? 88  GLU   A OE2 1 
ATOM   1182 O OE2 C GLU   A 1 45  ? 6.526   -10.634 -15.855 0.28 76.07  ? 88  GLU   A OE2 1 
ATOM   1183 O OE2 D GLU   A 1 45  ? 6.519   -10.634 -15.854 0.28 76.09  ? 88  GLU   A OE2 1 
ATOM   1184 N N   . GLY   B 2 7   ? -35.915 12.179  -11.839 1.00 72.36  ? 16  GLY   B N   1 
ATOM   1185 C CA  . GLY   B 2 7   ? -35.447 12.467  -13.232 1.00 70.41  ? 16  GLY   B CA  1 
ATOM   1186 C C   . GLY   B 2 7   ? -35.586 11.260  -14.156 1.00 68.26  ? 16  GLY   B C   1 
ATOM   1187 O O   . GLY   B 2 7   ? -36.547 10.472  -13.995 1.00 72.98  ? 16  GLY   B O   1 
ATOM   1188 N N   A GLU   B 2 8   ? -34.680 11.123  -15.132 0.22 64.00  ? 17  GLU   B N   1 
ATOM   1189 N N   B GLU   B 2 8   ? -34.678 11.127  -15.131 0.22 63.94  ? 17  GLU   B N   1 
ATOM   1190 N N   C GLU   B 2 8   ? -34.605 11.086  -15.047 0.28 63.98  ? 17  GLU   B N   1 
ATOM   1191 N N   D GLU   B 2 8   ? -34.601 11.084  -15.042 0.28 63.91  ? 17  GLU   B N   1 
ATOM   1192 C CA  A GLU   B 2 8   ? -34.737 10.035  -16.148 0.22 59.27  ? 17  GLU   B CA  1 
ATOM   1193 C CA  B GLU   B 2 8   ? -34.732 10.039  -16.146 0.22 59.15  ? 17  GLU   B CA  1 
ATOM   1194 C CA  C GLU   B 2 8   ? -34.562 10.047  -16.113 0.28 59.20  ? 17  GLU   B CA  1 
ATOM   1195 C CA  D GLU   B 2 8   ? -34.557 10.050  -16.113 0.28 59.06  ? 17  GLU   B CA  1 
ATOM   1196 C C   A GLU   B 2 8   ? -34.306 8.716   -15.498 0.22 56.16  ? 17  GLU   B C   1 
ATOM   1197 C C   B GLU   B 2 8   ? -34.318 8.719   -15.489 0.22 55.91  ? 17  GLU   B C   1 
ATOM   1198 C C   C GLU   B 2 8   ? -34.243 8.683   -15.483 0.28 55.57  ? 17  GLU   B C   1 
ATOM   1199 C C   D GLU   B 2 8   ? -34.245 8.679   -15.496 0.28 55.34  ? 17  GLU   B C   1 
ATOM   1200 O O   A GLU   B 2 8   ? -33.206 8.662   -14.924 0.22 54.94  ? 17  GLU   B O   1 
ATOM   1201 O O   B GLU   B 2 8   ? -33.232 8.652   -14.885 0.22 54.73  ? 17  GLU   B O   1 
ATOM   1202 O O   C GLU   B 2 8   ? -33.165 8.556   -14.879 0.28 54.51  ? 17  GLU   B O   1 
ATOM   1203 O O   D GLU   B 2 8   ? -33.154 8.526   -14.919 0.28 54.33  ? 17  GLU   B O   1 
ATOM   1204 C CB  A GLU   B 2 8   ? -33.875 10.318  -17.382 0.22 56.66  ? 17  GLU   B CB  1 
ATOM   1205 C CB  B GLU   B 2 8   ? -33.871 10.318  -17.381 0.22 56.60  ? 17  GLU   B CB  1 
ATOM   1206 C CB  C GLU   B 2 8   ? -33.514 10.459  -17.153 0.28 55.93  ? 17  GLU   B CB  1 
ATOM   1207 C CB  D GLU   B 2 8   ? -33.511 10.461  -17.153 0.28 55.87  ? 17  GLU   B CB  1 
ATOM   1208 C CG  A GLU   B 2 8   ? -34.066 9.271   -18.474 0.22 54.31  ? 17  GLU   B CG  1 
ATOM   1209 C CG  B GLU   B 2 8   ? -34.067 9.271   -18.472 0.22 54.29  ? 17  GLU   B CG  1 
ATOM   1210 C CG  C GLU   B 2 8   ? -33.718 9.850   -18.529 0.28 54.22  ? 17  GLU   B CG  1 
ATOM   1211 C CG  D GLU   B 2 8   ? -33.716 9.852   -18.528 0.28 54.19  ? 17  GLU   B CG  1 
ATOM   1212 C CD  A GLU   B 2 8   ? -33.674 9.689   -19.881 0.22 53.09  ? 17  GLU   B CD  1 
ATOM   1213 C CD  B GLU   B 2 8   ? -33.676 9.688   -19.880 0.22 53.08  ? 17  GLU   B CD  1 
ATOM   1214 C CD  C GLU   B 2 8   ? -32.880 10.523  -19.606 0.28 52.34  ? 17  GLU   B CD  1 
ATOM   1215 C CD  D GLU   B 2 8   ? -32.878 10.524  -19.605 0.28 52.33  ? 17  GLU   B CD  1 
ATOM   1216 O OE1 A GLU   B 2 8   ? -32.763 10.541  -20.009 0.22 51.59  ? 17  GLU   B OE1 1 
ATOM   1217 O OE1 B GLU   B 2 8   ? -32.765 10.538  -20.010 0.22 51.59  ? 17  GLU   B OE1 1 
ATOM   1218 O OE1 C GLU   B 2 8   ? -31.948 11.266  -19.238 0.28 45.01  ? 17  GLU   B OE1 1 
ATOM   1219 O OE1 D GLU   B 2 8   ? -31.947 11.268  -19.236 0.28 45.05  ? 17  GLU   B OE1 1 
ATOM   1220 O OE2 A GLU   B 2 8   ? -34.298 9.177   -20.852 0.22 49.60  ? 17  GLU   B OE2 1 
ATOM   1221 O OE2 B GLU   B 2 8   ? -34.302 9.176   -20.850 0.22 49.62  ? 17  GLU   B OE2 1 
ATOM   1222 O OE2 C GLU   B 2 8   ? -33.178 10.329  -20.810 0.28 57.97  ? 17  GLU   B OE2 1 
ATOM   1223 O OE2 D GLU   B 2 8   ? -33.174 10.328  -20.809 0.28 57.93  ? 17  GLU   B OE2 1 
ATOM   1224 N N   A THR   B 2 9   ? -35.163 7.701   -15.598 0.22 53.95  ? 18  THR   B N   1 
ATOM   1225 N N   B THR   B 2 9   ? -35.192 7.723   -15.622 0.22 53.35  ? 18  THR   B N   1 
ATOM   1226 N N   C THR   B 2 9   ? -35.147 7.705   -15.604 0.28 53.63  ? 18  THR   B N   1 
ATOM   1227 N N   D THR   B 2 9   ? -35.181 7.731   -15.617 0.28 53.02  ? 18  THR   B N   1 
ATOM   1228 C CA  A THR   B 2 9   ? -34.976 6.341   -15.034 0.22 53.78  ? 18  THR   B CA  1 
ATOM   1229 C CA  B THR   B 2 9   ? -35.094 6.361   -15.044 0.22 52.72  ? 18  THR   B CA  1 
ATOM   1230 C CA  C THR   B 2 9   ? -34.979 6.340   -15.039 0.28 53.76  ? 18  THR   B CA  1 
ATOM   1231 C CA  D THR   B 2 9   ? -35.100 6.362   -15.045 0.28 52.66  ? 18  THR   B CA  1 
ATOM   1232 C C   A THR   B 2 9   ? -34.982 5.305   -16.165 0.22 51.85  ? 18  THR   B C   1 
ATOM   1233 C C   B THR   B 2 9   ? -34.878 5.333   -16.162 0.22 51.58  ? 18  THR   B C   1 
ATOM   1234 C C   C THR   B 2 9   ? -34.982 5.304   -16.167 0.28 51.76  ? 18  THR   B C   1 
ATOM   1235 C C   D THR   B 2 9   ? -34.883 5.333   -16.162 0.28 51.51  ? 18  THR   B C   1 
ATOM   1236 O O   A THR   B 2 9   ? -34.974 4.103   -15.843 0.22 54.17  ? 18  THR   B O   1 
ATOM   1237 O O   B THR   B 2 9   ? -34.578 4.174   -15.826 0.22 55.10  ? 18  THR   B O   1 
ATOM   1238 O O   C THR   B 2 9   ? -34.970 4.104   -15.844 0.28 54.46  ? 18  THR   B O   1 
ATOM   1239 O O   D THR   B 2 9   ? -34.582 4.175   -15.825 0.28 55.56  ? 18  THR   B O   1 
ATOM   1240 C CB  A THR   B 2 9   ? -36.069 6.030   -14.005 0.22 54.31  ? 18  THR   B CB  1 
ATOM   1241 C CB  B THR   B 2 9   ? -36.365 6.042   -14.249 0.22 51.97  ? 18  THR   B CB  1 
ATOM   1242 C CB  C THR   B 2 9   ? -36.071 6.032   -14.007 0.28 54.41  ? 18  THR   B CB  1 
ATOM   1243 C CB  D THR   B 2 9   ? -36.370 6.044   -14.248 0.28 51.86  ? 18  THR   B CB  1 
ATOM   1244 O OG1 A THR   B 2 9   ? -36.574 7.273   -13.518 0.22 52.23  ? 18  THR   B OG1 1 
ATOM   1245 O OG1 B THR   B 2 9   ? -37.479 6.247   -15.116 0.22 49.90  ? 18  THR   B OG1 1 
ATOM   1246 O OG1 C THR   B 2 9   ? -36.568 7.277   -13.521 0.28 51.99  ? 18  THR   B OG1 1 
ATOM   1247 O OG1 D THR   B 2 9   ? -37.484 6.250   -15.115 0.28 49.56  ? 18  THR   B OG1 1 
ATOM   1248 C CG2 A THR   B 2 9   ? -35.572 5.170   -12.862 0.22 54.80  ? 18  THR   B CG2 1 
ATOM   1249 C CG2 B THR   B 2 9   ? -36.520 6.900   -13.014 0.22 52.44  ? 18  THR   B CG2 1 
ATOM   1250 C CG2 C THR   B 2 9   ? -35.572 5.172   -12.864 0.28 54.96  ? 18  THR   B CG2 1 
ATOM   1251 C CG2 D THR   B 2 9   ? -36.521 6.901   -13.013 0.28 52.45  ? 18  THR   B CG2 1 
ATOM   1252 N N   . THR   B 2 10  ? -35.011 5.749   -17.429 1.00 49.36  ? 19  THR   B N   1 
ATOM   1253 C CA  . THR   B 2 10  ? -34.980 4.852   -18.608 1.00 49.98  ? 19  THR   B CA  1 
ATOM   1254 C C   . THR   B 2 10  ? -33.678 4.020   -18.592 1.00 42.80  ? 19  THR   B C   1 
ATOM   1255 O O   . THR   B 2 10  ? -32.598 4.623   -18.437 1.00 44.12  ? 19  THR   B O   1 
ATOM   1256 C CB  . THR   B 2 10  ? -35.089 5.667   -19.911 1.00 55.21  ? 19  THR   B CB  1 
ATOM   1257 O OG1 . THR   B 2 10  ? -36.093 6.679   -19.804 1.00 72.14  ? 19  THR   B OG1 1 
ATOM   1258 C CG2 . THR   B 2 10  ? -35.422 4.804   -21.105 1.00 52.88  ? 19  THR   B CG2 1 
ATOM   1259 N N   . ASP   B 2 11  ? -33.767 2.720   -18.852 1.00 40.32  ? 20  ASP   B N   1 
ATOM   1260 C CA  . ASP   B 2 11  ? -32.561 1.871   -19.042 1.00 43.24  ? 20  ASP   B CA  1 
ATOM   1261 C C   . ASP   B 2 11  ? -31.637 2.502   -20.078 1.00 51.58  ? 20  ASP   B C   1 
ATOM   1262 O O   . ASP   B 2 11  ? -32.135 3.263   -20.945 1.00 52.95  ? 20  ASP   B O   1 
ATOM   1263 C CB  . ASP   B 2 11  ? -32.913 0.464   -19.469 1.00 47.56  ? 20  ASP   B CB  1 
ATOM   1264 C CG  . ASP   B 2 11  ? -33.499 -0.399  -18.372 1.00 54.10  ? 20  ASP   B CG  1 
ATOM   1265 O OD1 . ASP   B 2 11  ? -33.782 0.145   -17.274 1.00 46.94  ? 20  ASP   B OD1 1 
ATOM   1266 O OD2 . ASP   B 2 11  ? -33.686 -1.605  -18.657 1.00 55.91  ? 20  ASP   B OD2 1 
ATOM   1267 N N   . GLY   B 2 12  ? -30.339 2.220   -19.971 1.00 44.17  ? 21  GLY   B N   1 
ATOM   1268 C CA  . GLY   B 2 12  ? -29.333 2.641   -20.947 1.00 40.01  ? 21  GLY   B CA  1 
ATOM   1269 C C   . GLY   B 2 12  ? -28.108 3.160   -20.266 1.00 37.27  ? 21  GLY   B C   1 
ATOM   1270 O O   . GLY   B 2 12  ? -27.987 3.016   -19.020 1.00 34.95  ? 21  GLY   B O   1 
ATOM   1271 N N   . VAL   B 2 13  ? -27.231 3.746   -21.062 1.00 36.28  ? 22  VAL   B N   1 
ATOM   1272 C CA  . VAL   B 2 13  ? -25.904 4.234   -20.628 1.00 34.44  ? 22  VAL   B CA  1 
ATOM   1273 C C   . VAL   B 2 13  ? -25.988 5.736   -20.467 1.00 36.32  ? 22  VAL   B C   1 
ATOM   1274 O O   . VAL   B 2 13  ? -26.679 6.418   -21.256 1.00 40.00  ? 22  VAL   B O   1 
ATOM   1275 C CB  . VAL   B 2 13  ? -24.783 3.764   -21.570 1.00 34.54  ? 22  VAL   B CB  1 
ATOM   1276 C CG1 . VAL   B 2 13  ? -24.932 4.305   -23.002 1.00 34.30  ? 22  VAL   B CG1 1 
ATOM   1277 C CG2 . VAL   B 2 13  ? -23.402 4.096   -21.001 1.00 37.54  ? 22  VAL   B CG2 1 
ATOM   1278 N N   A TYR   B 2 14  ? -25.308 6.261   -19.448 0.22 33.27  ? 23  TYR   B N   1 
ATOM   1279 N N   B TYR   B 2 14  ? -25.308 6.261   -19.448 0.22 33.27  ? 23  TYR   B N   1 
ATOM   1280 N N   C TYR   B 2 14  ? -25.323 6.248   -19.430 0.28 33.97  ? 23  TYR   B N   1 
ATOM   1281 N N   D TYR   B 2 14  ? -25.323 6.248   -19.430 0.28 33.98  ? 23  TYR   B N   1 
ATOM   1282 C CA  A TYR   B 2 14  ? -25.400 7.686   -19.040 0.22 32.99  ? 23  TYR   B CA  1 
ATOM   1283 C CA  B TYR   B 2 14  ? -25.400 7.686   -19.040 0.22 32.98  ? 23  TYR   B CA  1 
ATOM   1284 C CA  C TYR   B 2 14  ? -25.332 7.684   -19.060 0.28 34.34  ? 23  TYR   B CA  1 
ATOM   1285 C CA  D TYR   B 2 14  ? -25.332 7.684   -19.060 0.28 34.34  ? 23  TYR   B CA  1 
ATOM   1286 C C   A TYR   B 2 14  ? -23.993 8.203   -18.748 0.22 32.46  ? 23  TYR   B C   1 
ATOM   1287 C C   B TYR   B 2 14  ? -23.993 8.203   -18.748 0.22 32.46  ? 23  TYR   B C   1 
ATOM   1288 C C   C TYR   B 2 14  ? -23.902 8.163   -18.916 0.28 34.01  ? 23  TYR   B C   1 
ATOM   1289 C C   D TYR   B 2 14  ? -23.902 8.163   -18.916 0.28 34.01  ? 23  TYR   B C   1 
ATOM   1290 O O   A TYR   B 2 14  ? -23.187 7.446   -18.172 0.22 33.42  ? 23  TYR   B O   1 
ATOM   1291 O O   B TYR   B 2 14  ? -23.187 7.447   -18.172 0.22 33.42  ? 23  TYR   B O   1 
ATOM   1292 O O   C TYR   B 2 14  ? -23.022 7.331   -18.661 0.28 36.61  ? 23  TYR   B O   1 
ATOM   1293 O O   D TYR   B 2 14  ? -23.021 7.332   -18.661 0.28 36.59  ? 23  TYR   B O   1 
ATOM   1294 C CB  A TYR   B 2 14  ? -26.330 7.846   -17.831 0.22 30.11  ? 23  TYR   B CB  1 
ATOM   1295 C CB  B TYR   B 2 14  ? -26.330 7.846   -17.830 0.22 30.12  ? 23  TYR   B CB  1 
ATOM   1296 C CB  C TYR   B 2 14  ? -26.036 7.945   -17.726 0.28 31.82  ? 23  TYR   B CB  1 
ATOM   1297 C CB  D TYR   B 2 14  ? -26.036 7.944   -17.726 0.28 31.83  ? 23  TYR   B CB  1 
ATOM   1298 C CG  A TYR   B 2 14  ? -27.787 7.574   -18.100 0.22 29.63  ? 23  TYR   B CG  1 
ATOM   1299 C CG  B TYR   B 2 14  ? -27.787 7.574   -18.099 0.22 29.64  ? 23  TYR   B CG  1 
ATOM   1300 C CG  C TYR   B 2 14  ? -27.526 7.792   -17.762 0.28 30.87  ? 23  TYR   B CG  1 
ATOM   1301 C CG  D TYR   B 2 14  ? -27.526 7.792   -17.762 0.28 30.88  ? 23  TYR   B CG  1 
ATOM   1302 C CD1 A TYR   B 2 14  ? -28.250 6.291   -18.335 0.22 28.08  ? 23  TYR   B CD1 1 
ATOM   1303 C CD1 B TYR   B 2 14  ? -28.250 6.291   -18.335 0.22 28.09  ? 23  TYR   B CD1 1 
ATOM   1304 C CD1 C TYR   B 2 14  ? -28.099 6.559   -18.009 0.28 28.64  ? 23  TYR   B CD1 1 
ATOM   1305 C CD1 D TYR   B 2 14  ? -28.100 6.558   -18.009 0.28 28.66  ? 23  TYR   B CD1 1 
ATOM   1306 C CD2 A TYR   B 2 14  ? -28.715 8.607   -18.092 0.22 30.30  ? 23  TYR   B CD2 1 
ATOM   1307 C CD2 B TYR   B 2 14  ? -28.715 8.607   -18.092 0.22 30.29  ? 23  TYR   B CD2 1 
ATOM   1308 C CD2 C TYR   B 2 14  ? -28.360 8.884   -17.557 0.28 30.72  ? 23  TYR   B CD2 1 
ATOM   1309 C CD2 D TYR   B 2 14  ? -28.360 8.883   -17.557 0.28 30.73  ? 23  TYR   B CD2 1 
ATOM   1310 C CE1 A TYR   B 2 14  ? -29.586 6.037   -18.587 0.22 28.58  ? 23  TYR   B CE1 1 
ATOM   1311 C CE1 B TYR   B 2 14  ? -29.586 6.037   -18.587 0.22 28.59  ? 23  TYR   B CE1 1 
ATOM   1312 C CE1 C TYR   B 2 14  ? -29.469 6.399   -18.046 0.28 30.79  ? 23  TYR   B CE1 1 
ATOM   1313 C CE1 D TYR   B 2 14  ? -29.469 6.399   -18.046 0.28 30.79  ? 23  TYR   B CE1 1 
ATOM   1314 C CE2 A TYR   B 2 14  ? -30.061 8.372   -18.330 0.22 29.25  ? 23  TYR   B CE2 1 
ATOM   1315 C CE2 B TYR   B 2 14  ? -30.060 8.372   -18.330 0.22 29.25  ? 23  TYR   B CE2 1 
ATOM   1316 C CE2 C TYR   B 2 14  ? -29.739 8.741   -17.588 0.28 30.90  ? 23  TYR   B CE2 1 
ATOM   1317 C CE2 D TYR   B 2 14  ? -29.739 8.740   -17.588 0.28 30.90  ? 23  TYR   B CE2 1 
ATOM   1318 C CZ  A TYR   B 2 14  ? -30.496 7.084   -18.579 0.22 29.79  ? 23  TYR   B CZ  1 
ATOM   1319 C CZ  B TYR   B 2 14  ? -30.496 7.084   -18.579 0.22 29.79  ? 23  TYR   B CZ  1 
ATOM   1320 C CZ  C TYR   B 2 14  ? -30.291 7.494   -17.826 0.28 29.84  ? 23  TYR   B CZ  1 
ATOM   1321 C CZ  D TYR   B 2 14  ? -30.291 7.494   -17.826 0.28 29.85  ? 23  TYR   B CZ  1 
ATOM   1322 O OH  A TYR   B 2 14  ? -31.813 6.856   -18.816 0.22 29.25  ? 23  TYR   B OH  1 
ATOM   1323 O OH  B TYR   B 2 14  ? -31.813 6.856   -18.816 0.22 29.25  ? 23  TYR   B OH  1 
ATOM   1324 O OH  C TYR   B 2 14  ? -31.638 7.334   -17.880 0.28 31.90  ? 23  TYR   B OH  1 
ATOM   1325 O OH  D TYR   B 2 14  ? -31.638 7.334   -17.880 0.28 31.90  ? 23  TYR   B OH  1 
ATOM   1326 N N   A ARG   B 2 15  ? -23.716 9.448   -19.143 0.22 32.34  ? 24  ARG   B N   1 
ATOM   1327 N N   B ARG   B 2 15  ? -23.716 9.448   -19.143 0.22 32.34  ? 24  ARG   B N   1 
ATOM   1328 N N   C ARG   B 2 15  ? -23.730 9.476   -19.029 0.28 33.68  ? 24  ARG   B N   1 
ATOM   1329 N N   D ARG   B 2 15  ? -23.729 9.476   -19.029 0.28 33.69  ? 24  ARG   B N   1 
ATOM   1330 C CA  A ARG   B 2 15  ? -22.501 10.195  -18.732 0.22 32.44  ? 24  ARG   B CA  1 
ATOM   1331 C CA  B ARG   B 2 15  ? -22.501 10.195  -18.732 0.22 32.45  ? 24  ARG   B CA  1 
ATOM   1332 C CA  C ARG   B 2 15  ? -22.478 10.202  -18.731 0.28 33.67  ? 24  ARG   B CA  1 
ATOM   1333 C CA  D ARG   B 2 15  ? -22.478 10.203  -18.731 0.28 33.68  ? 24  ARG   B CA  1 
ATOM   1334 C C   A ARG   B 2 15  ? -22.645 10.545  -17.249 0.22 35.40  ? 24  ARG   B C   1 
ATOM   1335 C C   B ARG   B 2 15  ? -22.645 10.545  -17.249 0.22 35.40  ? 24  ARG   B C   1 
ATOM   1336 C C   C ARG   B 2 15  ? -22.599 10.782  -17.321 0.28 36.68  ? 24  ARG   B C   1 
ATOM   1337 C C   D ARG   B 2 15  ? -22.599 10.782  -17.321 0.28 36.67  ? 24  ARG   B C   1 
ATOM   1338 O O   A ARG   B 2 15  ? -23.800 10.632  -16.790 0.22 35.07  ? 24  ARG   B O   1 
ATOM   1339 O O   B ARG   B 2 15  ? -23.800 10.632  -16.790 0.22 35.07  ? 24  ARG   B O   1 
ATOM   1340 O O   C ARG   B 2 15  ? -23.671 11.316  -16.993 0.28 35.03  ? 24  ARG   B O   1 
ATOM   1341 O O   D ARG   B 2 15  ? -23.671 11.315  -16.993 0.28 35.04  ? 24  ARG   B O   1 
ATOM   1342 C CB  A ARG   B 2 15  ? -22.324 11.481  -19.542 0.22 30.96  ? 24  ARG   B CB  1 
ATOM   1343 C CB  B ARG   B 2 15  ? -22.324 11.481  -19.542 0.22 30.97  ? 24  ARG   B CB  1 
ATOM   1344 C CB  C ARG   B 2 15  ? -22.260 11.297  -19.774 0.28 32.58  ? 24  ARG   B CB  1 
ATOM   1345 C CB  D ARG   B 2 15  ? -22.259 11.297  -19.774 0.28 32.59  ? 24  ARG   B CB  1 
ATOM   1346 C CG  A ARG   B 2 15  ? -22.159 11.285  -21.042 0.22 30.11  ? 24  ARG   B CG  1 
ATOM   1347 C CG  B ARG   B 2 15  ? -22.159 11.285  -21.042 0.22 30.11  ? 24  ARG   B CG  1 
ATOM   1348 C CG  C ARG   B 2 15  ? -22.352 10.812  -21.214 0.28 32.21  ? 24  ARG   B CG  1 
ATOM   1349 C CG  D ARG   B 2 15  ? -22.351 10.812  -21.214 0.28 32.22  ? 24  ARG   B CG  1 
ATOM   1350 C CD  A ARG   B 2 15  ? -21.930 12.603  -21.766 0.22 29.94  ? 24  ARG   B CD  1 
ATOM   1351 C CD  B ARG   B 2 15  ? -21.930 12.603  -21.766 0.22 29.95  ? 24  ARG   B CD  1 
ATOM   1352 C CD  C ARG   B 2 15  ? -22.392 11.964  -22.196 0.28 32.63  ? 24  ARG   B CD  1 
ATOM   1353 C CD  D ARG   B 2 15  ? -22.392 11.965  -22.196 0.28 32.62  ? 24  ARG   B CD  1 
ATOM   1354 N NE  A ARG   B 2 15  ? -21.959 12.438  -23.217 0.22 28.36  ? 24  ARG   B NE  1 
ATOM   1355 N NE  B ARG   B 2 15  ? -21.959 12.438  -23.217 0.22 28.38  ? 24  ARG   B NE  1 
ATOM   1356 N NE  C ARG   B 2 15  ? -22.630 11.496  -23.554 0.28 31.82  ? 24  ARG   B NE  1 
ATOM   1357 N NE  D ARG   B 2 15  ? -22.630 11.497  -23.555 0.28 31.82  ? 24  ARG   B NE  1 
ATOM   1358 C CZ  A ARG   B 2 15  ? -20.906 12.219  -24.000 0.22 29.77  ? 24  ARG   B CZ  1 
ATOM   1359 C CZ  B ARG   B 2 15  ? -20.907 12.218  -24.000 0.22 29.78  ? 24  ARG   B CZ  1 
ATOM   1360 C CZ  C ARG   B 2 15  ? -21.688 11.268  -24.467 0.28 31.26  ? 24  ARG   B CZ  1 
ATOM   1361 C CZ  D ARG   B 2 15  ? -21.688 11.268  -24.467 0.28 31.26  ? 24  ARG   B CZ  1 
ATOM   1362 N NH1 A ARG   B 2 15  ? -19.683 12.161  -23.502 0.22 30.06  ? 24  ARG   B NH1 1 
ATOM   1363 N NH1 B ARG   B 2 15  ? -19.684 12.160  -23.502 0.22 30.07  ? 24  ARG   B NH1 1 
ATOM   1364 N NH1 C ARG   B 2 15  ? -20.412 11.479  -24.188 0.28 28.97  ? 24  ARG   B NH1 1 
ATOM   1365 N NH1 D ARG   B 2 15  ? -20.412 11.479  -24.188 0.28 28.98  ? 24  ARG   B NH1 1 
ATOM   1366 N NH2 A ARG   B 2 15  ? -21.082 12.073  -25.302 0.22 30.36  ? 24  ARG   B NH2 1 
ATOM   1367 N NH2 B ARG   B 2 15  ? -21.082 12.073  -25.302 0.22 30.36  ? 24  ARG   B NH2 1 
ATOM   1368 N NH2 C ARG   B 2 15  ? -22.029 10.835  -25.668 0.28 31.19  ? 24  ARG   B NH2 1 
ATOM   1369 N NH2 D ARG   B 2 15  ? -22.029 10.835  -25.668 0.28 31.19  ? 24  ARG   B NH2 1 
ATOM   1370 N N   . VAL   B 2 16  ? -21.518 10.712  -16.546 1.00 38.38  ? 25  VAL   B N   1 
ATOM   1371 C CA  . VAL   B 2 16  ? -21.476 11.232  -15.162 1.00 39.93  ? 25  VAL   B CA  1 
ATOM   1372 C C   . VAL   B 2 16  ? -20.613 12.494  -15.246 1.00 39.80  ? 25  VAL   B C   1 
ATOM   1373 O O   . VAL   B 2 16  ? -19.444 12.380  -15.546 1.00 38.48  ? 25  VAL   B O   1 
ATOM   1374 C CB  . VAL   B 2 16  ? -20.956 10.147  -14.177 1.00 42.41  ? 25  VAL   B CB  1 
ATOM   1375 C CG1 . VAL   B 2 16  ? -20.883 10.670  -12.750 1.00 46.39  ? 25  VAL   B CG1 1 
ATOM   1376 C CG2 . VAL   B 2 16  ? -21.818 8.887   -14.230 1.00 41.13  ? 25  VAL   B CG2 1 
ATOM   1377 N N   . MET   B 2 17  ? -21.223 13.660  -15.012 1.00 40.77  ? 26  MET   B N   1 
ATOM   1378 C CA  . MET   B 2 17  ? -20.658 15.012  -15.245 1.00 38.93  ? 26  MET   B CA  1 
ATOM   1379 C C   . MET   B 2 17  ? -20.552 15.758  -13.913 1.00 41.69  ? 26  MET   B C   1 
ATOM   1380 O O   . MET   B 2 17  ? -21.315 15.420  -12.953 1.00 39.75  ? 26  MET   B O   1 
ATOM   1381 C CB  . MET   B 2 17  ? -21.598 15.813  -16.150 1.00 41.31  ? 26  MET   B CB  1 
ATOM   1382 C CG  . MET   B 2 17  ? -22.034 15.104  -17.415 1.00 48.06  ? 26  MET   B CG  1 
ATOM   1383 S SD  . MET   B 2 17  ? -20.696 14.907  -18.640 1.00 46.91  ? 26  MET   B SD  1 
ATOM   1384 C CE  . MET   B 2 17  ? -20.146 16.600  -18.815 1.00 51.96  ? 26  MET   B CE  1 
ATOM   1385 N N   . THR   B 2 18  ? -19.672 16.750  -13.870 1.00 39.85  ? 27  THR   B N   1 
ATOM   1386 C CA  . THR   B 2 18  ? -19.512 17.719  -12.764 1.00 53.80  ? 27  THR   B CA  1 
ATOM   1387 C C   . THR   B 2 18  ? -19.239 19.133  -13.319 1.00 58.11  ? 27  THR   B C   1 
ATOM   1388 O O   . THR   B 2 18  ? -18.651 19.263  -14.445 1.00 44.03  ? 27  THR   B O   1 
ATOM   1389 C CB  . THR   B 2 18  ? -18.362 17.313  -11.835 1.00 52.46  ? 27  THR   B CB  1 
ATOM   1390 O OG1 . THR   B 2 18  ? -18.348 18.278  -10.774 1.00 51.99  ? 27  THR   B OG1 1 
ATOM   1391 C CG2 . THR   B 2 18  ? -17.013 17.264  -12.522 1.00 51.76  ? 27  THR   B CG2 1 
ATOM   1392 N N   A ARG   B 2 19  ? -19.696 20.156  -12.585 0.22 57.95  ? 28  ARG   B N   1 
ATOM   1393 N N   B ARG   B 2 19  ? -19.696 20.156  -12.585 0.22 57.96  ? 28  ARG   B N   1 
ATOM   1394 N N   C ARG   B 2 19  ? -19.597 20.155  -12.532 0.28 56.82  ? 28  ARG   B N   1 
ATOM   1395 N N   D ARG   B 2 19  ? -19.597 20.155  -12.532 0.28 56.83  ? 28  ARG   B N   1 
ATOM   1396 C CA  A ARG   B 2 19  ? -19.509 21.599  -12.909 0.22 62.33  ? 28  ARG   B CA  1 
ATOM   1397 C CA  B ARG   B 2 19  ? -19.509 21.599  -12.909 0.22 62.33  ? 28  ARG   B CA  1 
ATOM   1398 C CA  C ARG   B 2 19  ? -19.267 21.583  -12.794 0.28 60.61  ? 28  ARG   B CA  1 
ATOM   1399 C CA  D ARG   B 2 19  ? -19.267 21.583  -12.794 0.28 60.61  ? 28  ARG   B CA  1 
ATOM   1400 C C   A ARG   B 2 19  ? -18.607 22.258  -11.855 0.22 63.21  ? 28  ARG   B C   1 
ATOM   1401 C C   B ARG   B 2 19  ? -18.607 22.258  -11.855 0.22 63.21  ? 28  ARG   B C   1 
ATOM   1402 C C   C ARG   B 2 19  ? -18.328 22.118  -11.701 0.28 61.10  ? 28  ARG   B C   1 
ATOM   1403 C C   D ARG   B 2 19  ? -18.329 22.118  -11.700 0.28 61.11  ? 28  ARG   B C   1 
ATOM   1404 O O   A ARG   B 2 19  ? -18.507 23.505  -11.859 0.22 62.14  ? 28  ARG   B O   1 
ATOM   1405 O O   B ARG   B 2 19  ? -18.508 23.505  -11.858 0.22 62.15  ? 28  ARG   B O   1 
ATOM   1406 O O   C ARG   B 2 19  ? -18.103 23.346  -11.671 0.28 58.02  ? 28  ARG   B O   1 
ATOM   1407 O O   D ARG   B 2 19  ? -18.104 23.347  -11.669 0.28 58.04  ? 28  ARG   B O   1 
ATOM   1408 C CB  A ARG   B 2 19  ? -20.863 22.312  -12.983 0.22 63.58  ? 28  ARG   B CB  1 
ATOM   1409 C CB  B ARG   B 2 19  ? -20.863 22.312  -12.984 0.22 63.58  ? 28  ARG   B CB  1 
ATOM   1410 C CB  C ARG   B 2 19  ? -20.552 22.411  -12.893 0.28 60.63  ? 28  ARG   B CB  1 
ATOM   1411 C CB  D ARG   B 2 19  ? -20.552 22.411  -12.893 0.28 60.63  ? 28  ARG   B CB  1 
ATOM   1412 C CG  A ARG   B 2 19  ? -21.796 21.772  -14.058 0.22 66.45  ? 28  ARG   B CG  1 
ATOM   1413 C CG  B ARG   B 2 19  ? -21.796 21.772  -14.058 0.22 66.45  ? 28  ARG   B CG  1 
ATOM   1414 C CG  C ARG   B 2 19  ? -21.529 21.897  -13.940 0.28 62.26  ? 28  ARG   B CG  1 
ATOM   1415 C CG  D ARG   B 2 19  ? -21.529 21.897  -13.940 0.28 62.25  ? 28  ARG   B CG  1 
ATOM   1416 C CD  A ARG   B 2 19  ? -22.778 22.817  -14.555 0.22 67.82  ? 28  ARG   B CD  1 
ATOM   1417 C CD  B ARG   B 2 19  ? -22.778 22.817  -14.555 0.22 67.81  ? 28  ARG   B CD  1 
ATOM   1418 C CD  C ARG   B 2 19  ? -21.893 22.943  -14.974 0.28 61.90  ? 28  ARG   B CD  1 
ATOM   1419 C CD  D ARG   B 2 19  ? -21.893 22.943  -14.974 0.28 61.90  ? 28  ARG   B CD  1 
ATOM   1420 N NE  A ARG   B 2 19  ? -23.765 22.289  -15.491 0.22 68.50  ? 28  ARG   B NE  1 
ATOM   1421 N NE  B ARG   B 2 19  ? -23.765 22.289  -15.491 0.22 68.50  ? 28  ARG   B NE  1 
ATOM   1422 N NE  C ARG   B 2 19  ? -23.025 22.520  -15.789 0.28 62.10  ? 28  ARG   B NE  1 
ATOM   1423 N NE  D ARG   B 2 19  ? -23.025 22.520  -15.789 0.28 62.10  ? 28  ARG   B NE  1 
ATOM   1424 C CZ  A ARG   B 2 19  ? -24.870 21.622  -15.153 0.22 71.63  ? 28  ARG   B CZ  1 
ATOM   1425 C CZ  B ARG   B 2 19  ? -24.870 21.622  -15.153 0.22 71.62  ? 28  ARG   B CZ  1 
ATOM   1426 C CZ  C ARG   B 2 19  ? -24.305 22.606  -15.431 0.28 61.75  ? 28  ARG   B CZ  1 
ATOM   1427 C CZ  D ARG   B 2 19  ? -24.305 22.606  -15.431 0.28 61.75  ? 28  ARG   B CZ  1 
ATOM   1428 N NH1 A ARG   B 2 19  ? -25.147 21.371  -13.882 0.22 74.61  ? 28  ARG   B NH1 1 
ATOM   1429 N NH1 B ARG   B 2 19  ? -25.147 21.371  -13.882 0.22 74.58  ? 28  ARG   B NH1 1 
ATOM   1430 N NH1 C ARG   B 2 19  ? -24.646 23.100  -14.250 0.28 64.38  ? 28  ARG   B NH1 1 
ATOM   1431 N NH1 D ARG   B 2 19  ? -24.646 23.100  -14.250 0.28 64.36  ? 28  ARG   B NH1 1 
ATOM   1432 N NH2 A ARG   B 2 19  ? -25.697 21.199  -16.094 0.22 71.26  ? 28  ARG   B NH2 1 
ATOM   1433 N NH2 B ARG   B 2 19  ? -25.697 21.199  -16.094 0.22 71.25  ? 28  ARG   B NH2 1 
ATOM   1434 N NH2 C ARG   B 2 19  ? -25.247 22.186  -16.258 0.28 62.37  ? 28  ARG   B NH2 1 
ATOM   1435 N NH2 D ARG   B 2 19  ? -25.247 22.186  -16.258 0.28 62.37  ? 28  ARG   B NH2 1 
ATOM   1436 N N   A ARG   B 2 20  ? -17.963 21.454  -11.003 0.22 63.73  ? 29  ARG   B N   1 
ATOM   1437 N N   B ARG   B 2 20  ? -17.963 21.454  -11.003 0.22 63.75  ? 29  ARG   B N   1 
ATOM   1438 N N   C ARG   B 2 20  ? -17.762 21.231  -10.874 0.28 63.53  ? 29  ARG   B N   1 
ATOM   1439 N N   D ARG   B 2 20  ? -17.762 21.231  -10.874 0.28 63.56  ? 29  ARG   B N   1 
ATOM   1440 C CA  A ARG   B 2 20  ? -17.090 21.927  -9.894  0.22 68.01  ? 29  ARG   B CA  1 
ATOM   1441 C CA  B ARG   B 2 20  ? -17.090 21.927  -9.894  0.22 68.02  ? 29  ARG   B CA  1 
ATOM   1442 C CA  C ARG   B 2 20  ? -16.849 21.585  -9.751  0.28 70.15  ? 29  ARG   B CA  1 
ATOM   1443 C CA  D ARG   B 2 20  ? -16.849 21.585  -9.750  0.28 70.16  ? 29  ARG   B CA  1 
ATOM   1444 C C   A ARG   B 2 20  ? -15.813 22.534  -10.491 0.22 66.59  ? 29  ARG   B C   1 
ATOM   1445 C C   B ARG   B 2 20  ? -15.813 22.534  -10.491 0.22 66.60  ? 29  ARG   B C   1 
ATOM   1446 C C   C ARG   B 2 20  ? -15.430 21.825  -10.294 0.28 68.29  ? 29  ARG   B C   1 
ATOM   1447 C C   D ARG   B 2 20  ? -15.430 21.825  -10.294 0.28 68.29  ? 29  ARG   B C   1 
ATOM   1448 O O   A ARG   B 2 20  ? -15.365 23.581  -9.984  0.22 64.25  ? 29  ARG   B O   1 
ATOM   1449 O O   B ARG   B 2 20  ? -15.364 23.581  -9.984  0.22 64.27  ? 29  ARG   B O   1 
ATOM   1450 O O   C ARG   B 2 20  ? -14.501 22.011  -9.479  0.28 62.95  ? 29  ARG   B O   1 
ATOM   1451 O O   D ARG   B 2 20  ? -14.501 22.012  -9.479  0.28 62.98  ? 29  ARG   B O   1 
ATOM   1452 C CB  A ARG   B 2 20  ? -16.775 20.769  -8.940  0.22 72.53  ? 29  ARG   B CB  1 
ATOM   1453 C CB  B ARG   B 2 20  ? -16.775 20.769  -8.940  0.22 72.54  ? 29  ARG   B CB  1 
ATOM   1454 C CB  C ARG   B 2 20  ? -16.871 20.487  -8.681  0.28 75.91  ? 29  ARG   B CB  1 
ATOM   1455 C CB  D ARG   B 2 20  ? -16.872 20.487  -8.681  0.28 75.92  ? 29  ARG   B CB  1 
ATOM   1456 C CG  A ARG   B 2 20  ? -16.477 21.200  -7.512  0.22 77.68  ? 29  ARG   B CG  1 
ATOM   1457 C CG  B ARG   B 2 20  ? -16.477 21.200  -7.512  0.22 77.68  ? 29  ARG   B CG  1 
ATOM   1458 C CG  C ARG   B 2 20  ? -16.599 20.989  -7.270  0.28 84.07  ? 29  ARG   B CG  1 
ATOM   1459 C CG  D ARG   B 2 20  ? -16.599 20.989  -7.270  0.28 84.06  ? 29  ARG   B CG  1 
ATOM   1460 C CD  A ARG   B 2 20  ? -16.298 20.005  -6.594  0.22 85.11  ? 29  ARG   B CD  1 
ATOM   1461 C CD  B ARG   B 2 20  ? -16.298 20.005  -6.594  0.22 85.09  ? 29  ARG   B CD  1 
ATOM   1462 C CD  C ARG   B 2 20  ? -16.411 19.859  -6.274  0.28 95.34  ? 29  ARG   B CD  1 
ATOM   1463 C CD  D ARG   B 2 20  ? -16.411 19.859  -6.274  0.28 95.29  ? 29  ARG   B CD  1 
ATOM   1464 N NE  A ARG   B 2 20  ? -15.220 19.126  -7.039  0.22 90.24  ? 29  ARG   B NE  1 
ATOM   1465 N NE  B ARG   B 2 20  ? -15.220 19.126  -7.039  0.22 90.21  ? 29  ARG   B NE  1 
ATOM   1466 N NE  C ARG   B 2 20  ? -15.289 18.989  -6.618  0.28 103.96 ? 29  ARG   B NE  1 
ATOM   1467 N NE  D ARG   B 2 20  ? -15.289 18.989  -6.618  0.28 103.89 ? 29  ARG   B NE  1 
ATOM   1468 C CZ  A ARG   B 2 20  ? -13.919 19.333  -6.829  0.22 94.24  ? 29  ARG   B CZ  1 
ATOM   1469 C CZ  B ARG   B 2 20  ? -13.919 19.333  -6.828  0.22 94.21  ? 29  ARG   B CZ  1 
ATOM   1470 C CZ  C ARG   B 2 20  ? -14.005 19.232  -6.343  0.28 110.43 ? 29  ARG   B CZ  1 
ATOM   1471 C CZ  D ARG   B 2 20  ? -14.005 19.232  -6.343  0.28 110.36 ? 29  ARG   B CZ  1 
ATOM   1472 N NH1 A ARG   B 2 20  ? -13.502 20.404  -6.171  0.22 96.96  ? 29  ARG   B NH1 1 
ATOM   1473 N NH1 B ARG   B 2 20  ? -13.502 20.404  -6.171  0.22 96.92  ? 29  ARG   B NH1 1 
ATOM   1474 N NH1 C ARG   B 2 20  ? -13.644 20.337  -5.710  0.28 113.03 ? 29  ARG   B NH1 1 
ATOM   1475 N NH1 D ARG   B 2 20  ? -13.644 20.338  -5.710  0.28 112.95 ? 29  ARG   B NH1 1 
ATOM   1476 N NH2 A ARG   B 2 20  ? -13.033 18.462  -7.283  0.22 93.18  ? 29  ARG   B NH2 1 
ATOM   1477 N NH2 B ARG   B 2 20  ? -13.033 18.462  -7.283  0.22 93.16  ? 29  ARG   B NH2 1 
ATOM   1478 N NH2 C ARG   B 2 20  ? -13.079 18.362  -6.712  0.28 111.18 ? 29  ARG   B NH2 1 
ATOM   1479 N NH2 D ARG   B 2 20  ? -13.079 18.362  -6.712  0.28 111.12 ? 29  ARG   B NH2 1 
ATOM   1480 N N   A LEU   B 2 21  ? -15.268 21.893  -11.531 0.22 66.11  ? 30  LEU   B N   1 
ATOM   1481 N N   B LEU   B 2 21  ? -15.268 21.893  -11.531 0.22 66.10  ? 30  LEU   B N   1 
ATOM   1482 N N   C LEU   B 2 21  ? -15.267 21.799  -11.621 0.28 66.53  ? 30  LEU   B N   1 
ATOM   1483 N N   D LEU   B 2 21  ? -15.267 21.799  -11.621 0.28 66.52  ? 30  LEU   B N   1 
ATOM   1484 C CA  A LEU   B 2 21  ? -14.053 22.325  -12.276 0.22 64.36  ? 30  LEU   B CA  1 
ATOM   1485 C CA  B LEU   B 2 21  ? -14.053 22.325  -12.276 0.22 64.37  ? 30  LEU   B CA  1 
ATOM   1486 C CA  C LEU   B 2 21  ? -14.042 22.243  -12.337 0.28 63.77  ? 30  LEU   B CA  1 
ATOM   1487 C CA  D LEU   B 2 21  ? -14.042 22.243  -12.337 0.28 63.77  ? 30  LEU   B CA  1 
ATOM   1488 C C   A LEU   B 2 21  ? -14.473 23.170  -13.488 0.22 62.47  ? 30  LEU   B C   1 
ATOM   1489 C C   B LEU   B 2 21  ? -14.473 23.170  -13.488 0.22 62.48  ? 30  LEU   B C   1 
ATOM   1490 C C   C LEU   B 2 21  ? -14.455 23.199  -13.464 0.28 61.68  ? 30  LEU   B C   1 
ATOM   1491 C C   D LEU   B 2 21  ? -14.455 23.199  -13.464 0.28 61.69  ? 30  LEU   B C   1 
ATOM   1492 O O   A LEU   B 2 21  ? -15.676 23.491  -13.592 0.22 61.75  ? 30  LEU   B O   1 
ATOM   1493 O O   B LEU   B 2 21  ? -15.676 23.490  -13.592 0.22 61.76  ? 30  LEU   B O   1 
ATOM   1494 O O   C LEU   B 2 21  ? -15.626 23.636  -13.472 0.28 59.88  ? 30  LEU   B O   1 
ATOM   1495 O O   D LEU   B 2 21  ? -15.626 23.636  -13.472 0.28 59.90  ? 30  LEU   B O   1 
ATOM   1496 C CB  A LEU   B 2 21  ? -13.260 21.078  -12.684 0.22 63.50  ? 30  LEU   B CB  1 
ATOM   1497 C CB  B LEU   B 2 21  ? -13.260 21.078  -12.684 0.22 63.51  ? 30  LEU   B CB  1 
ATOM   1498 C CB  C LEU   B 2 21  ? -13.302 21.013  -12.873 0.28 62.56  ? 30  LEU   B CB  1 
ATOM   1499 C CB  D LEU   B 2 21  ? -13.302 21.013  -12.873 0.28 62.57  ? 30  LEU   B CB  1 
ATOM   1500 C CG  A LEU   B 2 21  ? -12.168 20.641  -11.709 0.22 65.10  ? 30  LEU   B CG  1 
ATOM   1501 C CG  B LEU   B 2 21  ? -12.168 20.641  -11.709 0.22 65.10  ? 30  LEU   B CG  1 
ATOM   1502 C CG  C LEU   B 2 21  ? -13.036 19.906  -11.856 0.28 62.87  ? 30  LEU   B CG  1 
ATOM   1503 C CG  D LEU   B 2 21  ? -13.036 19.906  -11.856 0.28 62.88  ? 30  LEU   B CG  1 
ATOM   1504 C CD1 A LEU   B 2 21  ? -12.674 20.636  -10.273 0.22 65.60  ? 30  LEU   B CD1 1 
ATOM   1505 C CD1 B LEU   B 2 21  ? -12.674 20.635  -10.273 0.22 65.59  ? 30  LEU   B CD1 1 
ATOM   1506 C CD1 C LEU   B 2 21  ? -12.653 18.611  -12.553 0.28 62.88  ? 30  LEU   B CD1 1 
ATOM   1507 C CD1 D LEU   B 2 21  ? -12.653 18.611  -12.553 0.28 62.89  ? 30  LEU   B CD1 1 
ATOM   1508 C CD2 A LEU   B 2 21  ? -11.626 19.271  -12.089 0.22 65.32  ? 30  LEU   B CD2 1 
ATOM   1509 C CD2 B LEU   B 2 21  ? -11.626 19.271  -12.089 0.22 65.32  ? 30  LEU   B CD2 1 
ATOM   1510 C CD2 C LEU   B 2 21  ? -11.957 20.325  -10.868 0.28 64.28  ? 30  LEU   B CD2 1 
ATOM   1511 C CD2 D LEU   B 2 21  ? -11.957 20.325  -10.868 0.28 64.27  ? 30  LEU   B CD2 1 
ATOM   1512 N N   . LEU   B 2 22  ? -13.519 23.529  -14.358 1.00 63.53  ? 31  LEU   B N   1 
ATOM   1513 C CA  . LEU   B 2 22  ? -13.768 24.413  -15.534 1.00 61.95  ? 31  LEU   B CA  1 
ATOM   1514 C C   . LEU   B 2 22  ? -14.878 23.816  -16.396 1.00 63.86  ? 31  LEU   B C   1 
ATOM   1515 O O   . LEU   B 2 22  ? -14.838 22.585  -16.589 1.00 67.17  ? 31  LEU   B O   1 
ATOM   1516 C CB  . LEU   B 2 22  ? -12.468 24.521  -16.338 1.00 59.02  ? 31  LEU   B CB  1 
ATOM   1517 C CG  . LEU   B 2 22  ? -12.443 25.624  -17.388 1.00 56.24  ? 31  LEU   B CG  1 
ATOM   1518 C CD1 . LEU   B 2 22  ? -12.242 26.994  -16.746 1.00 51.04  ? 31  LEU   B CD1 1 
ATOM   1519 C CD2 . LEU   B 2 22  ? -11.365 25.349  -18.425 1.00 54.30  ? 31  LEU   B CD2 1 
ATOM   1520 N N   . GLY   B 2 23  ? -15.829 24.629  -16.882 1.00 57.41  ? 32  GLY   B N   1 
ATOM   1521 C CA  . GLY   B 2 23  ? -16.944 24.125  -17.716 1.00 50.96  ? 32  GLY   B CA  1 
ATOM   1522 C C   . GLY   B 2 23  ? -17.632 22.921  -17.063 1.00 48.87  ? 32  GLY   B C   1 
ATOM   1523 O O   . GLY   B 2 23  ? -17.614 22.816  -15.818 1.00 50.10  ? 32  GLY   B O   1 
ATOM   1524 N N   . SER   B 2 24  ? -18.282 22.088  -17.873 1.00 49.04  ? 33  SER   B N   1 
ATOM   1525 C CA  . SER   B 2 24  ? -18.871 20.777  -17.496 1.00 47.73  ? 33  SER   B CA  1 
ATOM   1526 C C   . SER   B 2 24  ? -17.901 19.656  -17.888 1.00 48.18  ? 33  SER   B C   1 
ATOM   1527 O O   . SER   B 2 24  ? -17.603 19.570  -19.066 1.00 44.83  ? 33  SER   B O   1 
ATOM   1528 C CB  . SER   B 2 24  ? -20.199 20.620  -18.151 1.00 50.94  ? 33  SER   B CB  1 
ATOM   1529 O OG  . SER   B 2 24  ? -21.029 21.728  -17.784 1.00 59.76  ? 33  SER   B OG  1 
ATOM   1530 N N   . THR   B 2 25  ? -17.432 18.845  -16.933 1.00 41.79  ? 34  THR   B N   1 
ATOM   1531 C CA  . THR   B 2 25  ? -16.380 17.806  -17.126 1.00 46.44  ? 34  THR   B CA  1 
ATOM   1532 C C   . THR   B 2 25  ? -16.976 16.416  -16.920 1.00 47.56  ? 34  THR   B C   1 
ATOM   1533 O O   . THR   B 2 25  ? -17.633 16.246  -15.890 1.00 43.22  ? 34  THR   B O   1 
ATOM   1534 C CB  . THR   B 2 25  ? -15.214 18.002  -16.155 1.00 52.44  ? 34  THR   B CB  1 
ATOM   1535 O OG1 . THR   B 2 25  ? -14.722 19.337  -16.304 1.00 46.22  ? 34  THR   B OG1 1 
ATOM   1536 C CG2 . THR   B 2 25  ? -14.102 16.999  -16.380 1.00 52.38  ? 34  THR   B CG2 1 
ATOM   1537 N N   . GLN   B 2 26  ? -16.764 15.472  -17.850 1.00 42.53  ? 35  GLN   B N   1 
ATOM   1538 C CA  . GLN   B 2 26  ? -17.269 14.083  -17.698 1.00 42.33  ? 35  GLN   B CA  1 
ATOM   1539 C C   . GLN   B 2 26  ? -16.274 13.292  -16.839 1.00 47.76  ? 35  GLN   B C   1 
ATOM   1540 O O   . GLN   B 2 26  ? -15.140 13.052  -17.304 1.00 48.99  ? 35  GLN   B O   1 
ATOM   1541 C CB  . GLN   B 2 26  ? -17.427 13.359  -19.020 1.00 40.08  ? 35  GLN   B CB  1 
ATOM   1542 C CG  . GLN   B 2 26  ? -18.053 11.973  -18.906 1.00 40.02  ? 35  GLN   B CG  1 
ATOM   1543 C CD  . GLN   B 2 26  ? -18.297 11.397  -20.274 1.00 39.30  ? 35  GLN   B CD  1 
ATOM   1544 O OE1 . GLN   B 2 26  ? -18.859 12.051  -21.132 1.00 38.21  ? 35  GLN   B OE1 1 
ATOM   1545 N NE2 . GLN   B 2 26  ? -17.923 10.150  -20.502 1.00 36.61  ? 35  GLN   B NE2 1 
ATOM   1546 N N   . VAL   B 2 27  ? -16.653 12.940  -15.617 1.00 45.40  ? 36  VAL   B N   1 
ATOM   1547 C CA  . VAL   B 2 27  ? -15.745 12.188  -14.693 1.00 41.48  ? 36  VAL   B CA  1 
ATOM   1548 C C   . VAL   B 2 27  ? -15.899 10.686  -14.956 1.00 36.95  ? 36  VAL   B C   1 
ATOM   1549 O O   . VAL   B 2 27  ? -15.015 9.909   -14.561 1.00 41.89  ? 36  VAL   B O   1 
ATOM   1550 C CB  . VAL   B 2 27  ? -16.018 12.588  -13.231 1.00 47.22  ? 36  VAL   B CB  1 
ATOM   1551 C CG1 . VAL   B 2 27  ? -15.462 13.973  -12.946 1.00 52.15  ? 36  VAL   B CG1 1 
ATOM   1552 C CG2 . VAL   B 2 27  ? -17.497 12.520  -12.874 1.00 47.21  ? 36  VAL   B CG2 1 
ATOM   1553 N N   . GLY   B 2 28  ? -16.990 10.259  -15.579 1.00 37.11  ? 37  GLY   B N   1 
ATOM   1554 C CA  . GLY   B 2 28  ? -17.200 8.834   -15.883 1.00 33.08  ? 37  GLY   B CA  1 
ATOM   1555 C C   . GLY   B 2 28  ? -18.523 8.569   -16.559 1.00 32.91  ? 37  GLY   B C   1 
ATOM   1556 O O   . GLY   B 2 28  ? -19.137 9.525   -17.113 1.00 37.43  ? 37  GLY   B O   1 
ATOM   1557 N N   . VAL   B 2 29  ? -18.955 7.305   -16.489 1.00 30.46  ? 38  VAL   B N   1 
ATOM   1558 C CA  . VAL   B 2 29  ? -20.114 6.698   -17.211 1.00 28.29  ? 38  VAL   B CA  1 
ATOM   1559 C C   . VAL   B 2 29  ? -20.810 5.733   -16.264 1.00 28.71  ? 38  VAL   B C   1 
ATOM   1560 O O   . VAL   B 2 29  ? -20.115 5.233   -15.332 1.00 30.25  ? 38  VAL   B O   1 
ATOM   1561 C CB  . VAL   B 2 29  ? -19.655 5.920   -18.462 1.00 32.05  ? 38  VAL   B CB  1 
ATOM   1562 C CG1 . VAL   B 2 29  ? -20.774 5.154   -19.149 1.00 32.90  ? 38  VAL   B CG1 1 
ATOM   1563 C CG2 . VAL   B 2 29  ? -18.922 6.784   -19.447 1.00 31.62  ? 38  VAL   B CG2 1 
ATOM   1564 N N   . GLY   B 2 30  ? -22.058 5.359   -16.582 1.00 30.51  ? 39  GLY   B N   1 
ATOM   1565 C CA  . GLY   B 2 30  ? -22.814 4.365   -15.816 1.00 27.68  ? 39  GLY   B CA  1 
ATOM   1566 C C   . GLY   B 2 30  ? -23.901 3.765   -16.602 1.00 30.11  ? 39  GLY   B C   1 
ATOM   1567 O O   . GLY   B 2 30  ? -24.130 4.241   -17.719 1.00 32.73  ? 39  GLY   B O   1 
ATOM   1568 N N   . VAL   B 2 31  ? -24.536 2.763   -16.017 1.00 26.84  ? 40  VAL   B N   1 
ATOM   1569 C CA  . VAL   B 2 31  ? -25.626 1.906   -16.560 1.00 30.47  ? 40  VAL   B CA  1 
ATOM   1570 C C   . VAL   B 2 31  ? -26.819 2.009   -15.630 1.00 33.94  ? 40  VAL   B C   1 
ATOM   1571 O O   . VAL   B 2 31  ? -26.660 1.704   -14.401 1.00 31.25  ? 40  VAL   B O   1 
ATOM   1572 C CB  . VAL   B 2 31  ? -25.229 0.425   -16.670 1.00 32.95  ? 40  VAL   B CB  1 
ATOM   1573 C CG1 . VAL   B 2 31  ? -26.375 -0.481  -17.085 1.00 32.96  ? 40  VAL   B CG1 1 
ATOM   1574 C CG2 . VAL   B 2 31  ? -24.075 0.266   -17.614 1.00 38.93  ? 40  VAL   B CG2 1 
ATOM   1575 N N   . MET   B 2 32  ? -27.935 2.476   -16.198 1.00 28.29  ? 41  MET   B N   1 
ATOM   1576 C CA  . MET   B 2 32  ? -29.270 2.450   -15.601 1.00 34.55  ? 41  MET   B CA  1 
ATOM   1577 C C   . MET   B 2 32  ? -29.939 1.147   -16.050 1.00 32.49  ? 41  MET   B C   1 
ATOM   1578 O O   . MET   B 2 32  ? -30.160 0.893   -17.261 1.00 33.67  ? 41  MET   B O   1 
ATOM   1579 C CB  . MET   B 2 32  ? -30.069 3.689   -16.046 1.00 35.14  ? 41  MET   B CB  1 
ATOM   1580 C CG  . MET   B 2 32  ? -31.366 3.906   -15.260 1.00 36.26  ? 41  MET   B CG  1 
ATOM   1581 S SD  . MET   B 2 32  ? -31.058 4.468   -13.545 1.00 39.22  ? 41  MET   B SD  1 
ATOM   1582 C CE  . MET   B 2 32  ? -30.200 5.988   -13.895 1.00 41.65  ? 41  MET   B CE  1 
ATOM   1583 N N   . GLN   B 2 33  ? -30.312 0.321   -15.097 1.00 32.38  ? 42  GLN   B N   1 
ATOM   1584 C CA  . GLN   B 2 33  ? -31.079 -0.910  -15.378 1.00 36.39  ? 42  GLN   B CA  1 
ATOM   1585 C C   . GLN   B 2 33  ? -31.958 -1.164  -14.183 1.00 38.35  ? 42  GLN   B C   1 
ATOM   1586 O O   . GLN   B 2 33  ? -31.487 -0.975  -13.051 1.00 36.92  ? 42  GLN   B O   1 
ATOM   1587 C CB  . GLN   B 2 33  ? -30.149 -2.131  -15.582 1.00 37.63  ? 42  GLN   B CB  1 
ATOM   1588 C CG  . GLN   B 2 33  ? -30.918 -3.391  -15.961 1.00 42.94  ? 42  GLN   B CG  1 
ATOM   1589 C CD  . GLN   B 2 33  ? -30.056 -4.437  -16.638 1.00 52.48  ? 42  GLN   B CD  1 
ATOM   1590 O OE1 . GLN   B 2 33  ? -30.154 -5.634  -16.359 1.00 54.76  ? 42  GLN   B OE1 1 
ATOM   1591 N NE2 . GLN   B 2 33  ? -29.150 -3.986  -17.492 1.00 52.02  ? 42  GLN   B NE2 1 
ATOM   1592 N N   A GLU   B 2 34  ? -33.212 -1.547  -14.424 0.22 40.63  ? 43  GLU   B N   1 
ATOM   1593 N N   B GLU   B 2 34  ? -33.212 -1.547  -14.424 0.22 40.63  ? 43  GLU   B N   1 
ATOM   1594 N N   C GLU   B 2 34  ? -33.179 -1.646  -14.428 0.28 41.19  ? 43  GLU   B N   1 
ATOM   1595 N N   D GLU   B 2 34  ? -33.179 -1.645  -14.428 0.28 41.19  ? 43  GLU   B N   1 
ATOM   1596 C CA  A GLU   B 2 34  ? -34.203 -1.904  -13.375 0.22 41.63  ? 43  GLU   B CA  1 
ATOM   1597 C CA  B GLU   B 2 34  ? -34.203 -1.904  -13.375 0.22 41.62  ? 43  GLU   B CA  1 
ATOM   1598 C CA  C GLU   B 2 34  ? -34.208 -1.961  -13.400 0.28 42.65  ? 43  GLU   B CA  1 
ATOM   1599 C CA  D GLU   B 2 34  ? -34.208 -1.960  -13.400 0.28 42.65  ? 43  GLU   B CA  1 
ATOM   1600 C C   A GLU   B 2 34  ? -34.291 -0.781  -12.325 0.22 42.75  ? 43  GLU   B C   1 
ATOM   1601 C C   B GLU   B 2 34  ? -34.291 -0.781  -12.325 0.22 42.73  ? 43  GLU   B C   1 
ATOM   1602 C C   C GLU   B 2 34  ? -34.204 -0.879  -12.308 0.28 43.85  ? 43  GLU   B C   1 
ATOM   1603 C C   D GLU   B 2 34  ? -34.204 -0.879  -12.308 0.28 43.83  ? 43  GLU   B C   1 
ATOM   1604 O O   A GLU   B 2 34  ? -34.488 -1.103  -11.140 0.22 42.01  ? 43  GLU   B O   1 
ATOM   1605 O O   B GLU   B 2 34  ? -34.485 -1.102  -11.140 0.22 42.00  ? 43  GLU   B O   1 
ATOM   1606 O O   C GLU   B 2 34  ? -34.194 -1.245  -11.118 0.28 41.85  ? 43  GLU   B O   1 
ATOM   1607 O O   D GLU   B 2 34  ? -34.192 -1.244  -11.118 0.28 41.86  ? 43  GLU   B O   1 
ATOM   1608 C CB  A GLU   B 2 34  ? -33.813 -3.253  -12.764 0.22 43.67  ? 43  GLU   B CB  1 
ATOM   1609 C CB  B GLU   B 2 34  ? -33.813 -3.253  -12.764 0.22 43.66  ? 43  GLU   B CB  1 
ATOM   1610 C CB  C GLU   B 2 34  ? -33.970 -3.362  -12.828 0.28 45.93  ? 43  GLU   B CB  1 
ATOM   1611 C CB  D GLU   B 2 34  ? -33.970 -3.361  -12.827 0.28 45.91  ? 43  GLU   B CB  1 
ATOM   1612 C CG  A GLU   B 2 34  ? -33.821 -4.396  -13.774 0.22 44.59  ? 43  GLU   B CG  1 
ATOM   1613 C CG  B GLU   B 2 34  ? -33.821 -4.396  -13.774 0.22 44.58  ? 43  GLU   B CG  1 
ATOM   1614 C CG  C GLU   B 2 34  ? -34.225 -4.480  -13.830 0.28 47.30  ? 43  GLU   B CG  1 
ATOM   1615 C CG  D GLU   B 2 34  ? -34.225 -4.479  -13.830 0.28 47.28  ? 43  GLU   B CG  1 
ATOM   1616 C CD  A GLU   B 2 34  ? -32.927 -5.580  -13.440 0.22 44.11  ? 43  GLU   B CD  1 
ATOM   1617 C CD  B GLU   B 2 34  ? -32.928 -5.580  -13.439 0.22 44.11  ? 43  GLU   B CD  1 
ATOM   1618 C CD  C GLU   B 2 34  ? -34.022 -5.896  -13.312 0.28 46.14  ? 43  GLU   B CD  1 
ATOM   1619 C CD  D GLU   B 2 34  ? -34.020 -5.895  -13.312 0.28 46.15  ? 43  GLU   B CD  1 
ATOM   1620 O OE1 A GLU   B 2 34  ? -33.082 -6.143  -12.340 0.22 42.03  ? 43  GLU   B OE1 1 
ATOM   1621 O OE1 B GLU   B 2 34  ? -33.085 -6.144  -12.340 0.22 42.03  ? 43  GLU   B OE1 1 
ATOM   1622 O OE1 C GLU   B 2 34  ? -34.721 -6.290  -12.360 0.28 48.53  ? 43  GLU   B OE1 1 
ATOM   1623 O OE1 D GLU   B 2 34  ? -34.716 -6.289  -12.358 0.28 48.52  ? 43  GLU   B OE1 1 
ATOM   1624 O OE2 A GLU   B 2 34  ? -32.075 -5.940  -14.285 0.22 43.44  ? 43  GLU   B OE2 1 
ATOM   1625 O OE2 B GLU   B 2 34  ? -32.075 -5.940  -14.284 0.22 43.43  ? 43  GLU   B OE2 1 
ATOM   1626 O OE2 C GLU   B 2 34  ? -33.163 -6.604  -13.864 0.28 48.03  ? 43  GLU   B OE2 1 
ATOM   1627 O OE2 D GLU   B 2 34  ? -33.162 -6.604  -13.867 0.28 48.02  ? 43  GLU   B OE2 1 
ATOM   1628 N N   A GLY   B 2 35  ? -34.145 0.484   -12.742 0.22 41.31  ? 44  GLY   B N   1 
ATOM   1629 N N   B GLY   B 2 35  ? -34.146 0.485   -12.743 0.22 41.29  ? 44  GLY   B N   1 
ATOM   1630 N N   C GLY   B 2 35  ? -34.194 0.399   -12.707 0.28 42.08  ? 44  GLY   B N   1 
ATOM   1631 N N   D GLY   B 2 35  ? -34.195 0.400   -12.707 0.28 42.07  ? 44  GLY   B N   1 
ATOM   1632 C CA  A GLY   B 2 35  ? -34.287 1.676   -11.878 0.22 40.22  ? 44  GLY   B CA  1 
ATOM   1633 C CA  B GLY   B 2 35  ? -34.287 1.677   -11.880 0.22 40.18  ? 44  GLY   B CA  1 
ATOM   1634 C CA  C GLY   B 2 35  ? -34.332 1.569   -11.814 0.28 40.56  ? 44  GLY   B CA  1 
ATOM   1635 C CA  D GLY   B 2 35  ? -34.332 1.570   -11.814 0.28 40.54  ? 44  GLY   B CA  1 
ATOM   1636 C C   A GLY   B 2 35  ? -33.041 1.968   -11.058 0.22 39.28  ? 44  GLY   B C   1 
ATOM   1637 C C   B GLY   B 2 35  ? -33.039 1.970   -11.061 0.22 39.24  ? 44  GLY   B C   1 
ATOM   1638 C C   C GLY   B 2 35  ? -33.161 1.735   -10.862 0.28 39.00  ? 44  GLY   B C   1 
ATOM   1639 C C   D GLY   B 2 35  ? -33.161 1.736   -10.862 0.28 38.99  ? 44  GLY   B C   1 
ATOM   1640 O O   A GLY   B 2 35  ? -33.017 3.010   -10.357 0.22 37.63  ? 44  GLY   B O   1 
ATOM   1641 O O   B GLY   B 2 35  ? -33.012 3.015   -10.366 0.22 37.63  ? 44  GLY   B O   1 
ATOM   1642 O O   C GLY   B 2 35  ? -33.334 2.430   -9.835  0.28 35.61  ? 44  GLY   B O   1 
ATOM   1643 O O   D GLY   B 2 35  ? -33.334 2.430   -9.836  0.28 35.62  ? 44  GLY   B O   1 
ATOM   1644 N N   . VAL   B 2 36  ? -32.017 1.119   -11.177 1.00 36.39  ? 45  VAL   B N   1 
ATOM   1645 C CA  . VAL   B 2 36  ? -30.774 1.210   -10.386 1.00 34.06  ? 45  VAL   B CA  1 
ATOM   1646 C C   . VAL   B 2 36  ? -29.707 1.750   -11.324 1.00 32.86  ? 45  VAL   B C   1 
ATOM   1647 O O   . VAL   B 2 36  ? -29.603 1.221   -12.483 1.00 34.30  ? 45  VAL   B O   1 
ATOM   1648 C CB  . VAL   B 2 36  ? -30.417 -0.168  -9.779  1.00 35.64  ? 45  VAL   B CB  1 
ATOM   1649 C CG1 . VAL   B 2 36  ? -28.976 -0.219  -9.280  1.00 39.17  ? 45  VAL   B CG1 1 
ATOM   1650 C CG2 . VAL   B 2 36  ? -31.347 -0.522  -8.638  1.00 38.44  ? 45  VAL   B CG2 1 
ATOM   1651 N N   . PHE   B 2 37  ? -28.947 2.736   -10.847 1.00 30.21  ? 46  PHE   B N   1 
ATOM   1652 C CA  . PHE   B 2 37  ? -27.757 3.287   -11.526 1.00 32.46  ? 46  PHE   B CA  1 
ATOM   1653 C C   . PHE   B 2 37  ? -26.497 2.597   -10.986 1.00 30.55  ? 46  PHE   B C   1 
ATOM   1654 O O   . PHE   B 2 37  ? -26.195 2.598   -9.779  1.00 32.15  ? 46  PHE   B O   1 
ATOM   1655 C CB  . PHE   B 2 37  ? -27.593 4.792   -11.376 1.00 31.12  ? 46  PHE   B CB  1 
ATOM   1656 C CG  . PHE   B 2 37  ? -26.632 5.401   -12.366 1.00 29.97  ? 46  PHE   B CG  1 
ATOM   1657 C CD1 . PHE   B 2 37  ? -26.858 5.290   -13.722 1.00 31.67  ? 46  PHE   B CD1 1 
ATOM   1658 C CD2 . PHE   B 2 37  ? -25.496 6.037   -11.940 1.00 29.22  ? 46  PHE   B CD2 1 
ATOM   1659 C CE1 . PHE   B 2 37  ? -25.984 5.837   -14.634 1.00 33.23  ? 46  PHE   B CE1 1 
ATOM   1660 C CE2 . PHE   B 2 37  ? -24.597 6.568   -12.852 1.00 33.42  ? 46  PHE   B CE2 1 
ATOM   1661 C CZ  . PHE   B 2 37  ? -24.872 6.506   -14.201 1.00 29.41  ? 46  PHE   B CZ  1 
ATOM   1662 N N   . HIS   B 2 38  ? -25.717 2.093   -11.920 1.00 28.29  ? 47  HIS   B N   1 
ATOM   1663 C CA  . HIS   B 2 38  ? -24.491 1.272   -11.646 1.00 29.90  ? 47  HIS   B CA  1 
ATOM   1664 C C   . HIS   B 2 38  ? -23.266 1.986   -12.196 1.00 31.15  ? 47  HIS   B C   1 
ATOM   1665 O O   . HIS   B 2 38  ? -23.259 2.287   -13.421 1.00 33.95  ? 47  HIS   B O   1 
ATOM   1666 C CB  . HIS   B 2 38  ? -24.634 -0.046  -12.353 1.00 29.09  ? 47  HIS   B CB  1 
ATOM   1667 C CG  . HIS   B 2 38  ? -25.839 -0.851  -12.041 1.00 25.74  ? 47  HIS   B CG  1 
ATOM   1668 N ND1 . HIS   B 2 38  ? -27.044 -0.612  -12.630 1.00 30.60  ? 47  HIS   B ND1 1 
ATOM   1669 C CD2 . HIS   B 2 38  ? -26.016 -1.923  -11.227 1.00 27.03  ? 47  HIS   B CD2 1 
ATOM   1670 C CE1 . HIS   B 2 38  ? -27.932 -1.495  -12.191 1.00 27.57  ? 47  HIS   B CE1 1 
ATOM   1671 N NE2 . HIS   B 2 38  ? -27.319 -2.320  -11.334 1.00 30.67  ? 47  HIS   B NE2 1 
ATOM   1672 N N   . THR   B 2 39  ? -22.292 2.316   -11.362 1.00 32.91  ? 48  THR   B N   1 
ATOM   1673 C CA  . THR   B 2 39  ? -21.022 2.901   -11.842 1.00 32.78  ? 48  THR   B CA  1 
ATOM   1674 C C   . THR   B 2 39  ? -19.833 2.305   -11.069 1.00 36.10  ? 48  THR   B C   1 
ATOM   1675 O O   . THR   B 2 39  ? -20.052 1.361   -10.229 1.00 29.90  ? 48  THR   B O   1 
ATOM   1676 C CB  . THR   B 2 39  ? -21.089 4.427   -11.886 1.00 35.45  ? 48  THR   B CB  1 
ATOM   1677 O OG1 . THR   B 2 39  ? -20.003 4.950   -12.651 1.00 30.87  ? 48  THR   B OG1 1 
ATOM   1678 C CG2 . THR   B 2 39  ? -21.041 5.068   -10.518 1.00 37.11  ? 48  THR   B CG2 1 
ATOM   1679 N N   . MET   B 2 40  ? -18.633 2.845   -11.337 1.00 33.22  ? 49  MET   B N   1 
ATOM   1680 C CA  . MET   B 2 40  ? -17.394 2.488   -10.619 1.00 37.01  ? 49  MET   B CA  1 
ATOM   1681 C C   . MET   B 2 40  ? -17.220 3.485   -9.483  1.00 35.65  ? 49  MET   B C   1 
ATOM   1682 O O   . MET   B 2 40  ? -17.511 4.679   -9.644  1.00 35.29  ? 49  MET   B O   1 
ATOM   1683 C CB  . MET   B 2 40  ? -16.154 2.460   -11.530 1.00 33.33  ? 49  MET   B CB  1 
ATOM   1684 C CG  . MET   B 2 40  ? -16.407 1.709   -12.830 1.00 36.37  ? 49  MET   B CG  1 
ATOM   1685 S SD  . MET   B 2 40  ? -14.954 0.796   -13.407 1.00 43.34  ? 49  MET   B SD  1 
ATOM   1686 C CE  . MET   B 2 40  ? -14.861 -0.555  -12.238 1.00 40.86  ? 49  MET   B CE  1 
ATOM   1687 N N   A TRP   B 2 41  ? -16.760 2.984   -8.338  0.22 34.27  ? 50  TRP   B N   1 
ATOM   1688 N N   B TRP   B 2 41  ? -16.775 2.998   -8.323  0.22 34.20  ? 50  TRP   B N   1 
ATOM   1689 N N   C TRP   B 2 41  ? -16.759 2.984   -8.339  0.28 33.99  ? 50  TRP   B N   1 
ATOM   1690 N N   D TRP   B 2 41  ? -16.775 2.999   -8.323  0.28 33.92  ? 50  TRP   B N   1 
ATOM   1691 C CA  A TRP   B 2 41  ? -16.612 3.757   -7.082  0.22 35.12  ? 50  TRP   B CA  1 
ATOM   1692 C CA  B TRP   B 2 41  ? -16.654 3.811   -7.086  0.22 34.95  ? 50  TRP   B CA  1 
ATOM   1693 C CA  C TRP   B 2 41  ? -16.612 3.757   -7.082  0.28 35.01  ? 50  TRP   B CA  1 
ATOM   1694 C CA  D TRP   B 2 41  ? -16.654 3.810   -7.086  0.28 34.83  ? 50  TRP   B CA  1 
ATOM   1695 C C   A TRP   B 2 41  ? -15.702 4.967   -7.330  0.22 35.94  ? 50  TRP   B C   1 
ATOM   1696 C C   B TRP   B 2 41  ? -15.706 4.991   -7.339  0.22 35.85  ? 50  TRP   B C   1 
ATOM   1697 C C   C TRP   B 2 41  ? -15.701 4.965   -7.329  0.28 36.08  ? 50  TRP   B C   1 
ATOM   1698 C C   D TRP   B 2 41  ? -15.706 4.990   -7.339  0.28 35.98  ? 50  TRP   B C   1 
ATOM   1699 O O   A TRP   B 2 41  ? -16.032 6.070   -6.842  0.22 35.59  ? 50  TRP   B O   1 
ATOM   1700 O O   B TRP   B 2 41  ? -16.014 6.105   -6.860  0.22 35.20  ? 50  TRP   B O   1 
ATOM   1701 O O   C TRP   B 2 41  ? -16.029 6.070   -6.841  0.28 35.61  ? 50  TRP   B O   1 
ATOM   1702 O O   D TRP   B 2 41  ? -16.013 6.106   -6.863  0.28 35.18  ? 50  TRP   B O   1 
ATOM   1703 C CB  A TRP   B 2 41  ? -16.084 2.864   -5.949  0.22 35.27  ? 50  TRP   B CB  1 
ATOM   1704 C CB  B TRP   B 2 41  ? -16.200 2.964   -5.886  0.22 35.24  ? 50  TRP   B CB  1 
ATOM   1705 C CB  C TRP   B 2 41  ? -16.085 2.862   -5.949  0.28 35.09  ? 50  TRP   B CB  1 
ATOM   1706 C CB  D TRP   B 2 41  ? -16.201 2.962   -5.886  0.28 35.08  ? 50  TRP   B CB  1 
ATOM   1707 C CG  A TRP   B 2 41  ? -16.192 3.528   -4.615  0.22 36.01  ? 50  TRP   B CG  1 
ATOM   1708 C CG  B TRP   B 2 41  ? -16.026 3.791   -4.650  0.22 35.71  ? 50  TRP   B CG  1 
ATOM   1709 C CG  C TRP   B 2 41  ? -16.191 3.526   -4.616  0.28 35.84  ? 50  TRP   B CG  1 
ATOM   1710 C CG  D TRP   B 2 41  ? -16.027 3.788   -4.650  0.28 35.51  ? 50  TRP   B CG  1 
ATOM   1711 C CD1 A TRP   B 2 41  ? -17.202 3.383   -3.709  0.22 37.17  ? 50  TRP   B CD1 1 
ATOM   1712 C CD1 B TRP   B 2 41  ? -14.931 4.530   -4.311  0.22 36.13  ? 50  TRP   B CD1 1 
ATOM   1713 C CD1 C TRP   B 2 41  ? -17.201 3.381   -3.710  0.28 37.16  ? 50  TRP   B CD1 1 
ATOM   1714 C CD1 D TRP   B 2 41  ? -14.933 4.528   -4.310  0.28 36.00  ? 50  TRP   B CD1 1 
ATOM   1715 C CD2 A TRP   B 2 41  ? -15.285 4.496   -4.058  0.22 36.88  ? 50  TRP   B CD2 1 
ATOM   1716 C CD2 B TRP   B 2 41  ? -17.000 4.021   -3.615  0.22 38.28  ? 50  TRP   B CD2 1 
ATOM   1717 C CD2 C TRP   B 2 41  ? -15.285 4.495   -4.060  0.28 36.76  ? 50  TRP   B CD2 1 
ATOM   1718 C CD2 D TRP   B 2 41  ? -17.001 4.017   -3.615  0.28 38.44  ? 50  TRP   B CD2 1 
ATOM   1719 N NE1 A TRP   B 2 41  ? -16.973 4.177   -2.618  0.22 38.17  ? 50  TRP   B NE1 1 
ATOM   1720 N NE1 B TRP   B 2 41  ? -15.148 5.189   -3.132  0.22 36.14  ? 50  TRP   B NE1 1 
ATOM   1721 N NE1 C TRP   B 2 41  ? -16.973 4.177   -2.620  0.28 38.29  ? 50  TRP   B NE1 1 
ATOM   1722 N NE1 D TRP   B 2 41  ? -15.150 5.186   -3.131  0.28 35.96  ? 50  TRP   B NE1 1 
ATOM   1723 C CE2 A TRP   B 2 41  ? -15.808 4.873   -2.804  0.22 37.11  ? 50  TRP   B CE2 1 
ATOM   1724 C CE2 B TRP   B 2 41  ? -16.406 4.895   -2.680  0.22 37.07  ? 50  TRP   B CE2 1 
ATOM   1725 C CE2 C TRP   B 2 41  ? -15.808 4.873   -2.807  0.28 36.96  ? 50  TRP   B CE2 1 
ATOM   1726 C CE2 D TRP   B 2 41  ? -16.408 4.892   -2.679  0.28 36.98  ? 50  TRP   B CE2 1 
ATOM   1727 C CE3 A TRP   B 2 41  ? -14.082 5.071   -4.486  0.22 37.91  ? 50  TRP   B CE3 1 
ATOM   1728 C CE3 B TRP   B 2 41  ? -18.306 3.572   -3.380  0.22 39.95  ? 50  TRP   B CE3 1 
ATOM   1729 C CE3 C TRP   B 2 41  ? -14.082 5.070   -4.487  0.28 37.95  ? 50  TRP   B CE3 1 
ATOM   1730 C CE3 D TRP   B 2 41  ? -18.307 3.568   -3.381  0.28 40.29  ? 50  TRP   B CE3 1 
ATOM   1731 C CZ2 A TRP   B 2 41  ? -15.162 5.793   -1.978  0.22 40.46  ? 50  TRP   B CZ2 1 
ATOM   1732 C CZ2 B TRP   B 2 41  ? -17.069 5.317   -1.527  0.22 38.14  ? 50  TRP   B CZ2 1 
ATOM   1733 C CZ2 C TRP   B 2 41  ? -15.162 5.794   -1.980  0.28 40.91  ? 50  TRP   B CZ2 1 
ATOM   1734 C CZ2 D TRP   B 2 41  ? -17.073 5.312   -1.525  0.28 38.18  ? 50  TRP   B CZ2 1 
ATOM   1735 C CZ3 A TRP   B 2 41  ? -13.447 5.981   -3.669  0.22 38.55  ? 50  TRP   B CZ3 1 
ATOM   1736 C CZ3 B TRP   B 2 41  ? -18.961 3.990   -2.239  0.22 40.01  ? 50  TRP   B CZ3 1 
ATOM   1737 C CZ3 C TRP   B 2 41  ? -13.447 5.980   -3.670  0.28 38.65  ? 50  TRP   B CZ3 1 
ATOM   1738 C CZ3 D TRP   B 2 41  ? -18.963 3.984   -2.239  0.28 40.32  ? 50  TRP   B CZ3 1 
ATOM   1739 C CH2 A TRP   B 2 41  ? -13.981 6.335   -2.430  0.22 38.50  ? 50  TRP   B CH2 1 
ATOM   1740 C CH2 B TRP   B 2 41  ? -18.349 4.851   -1.327  0.22 38.27  ? 50  TRP   B CH2 1 
ATOM   1741 C CH2 C TRP   B 2 41  ? -13.981 6.336   -2.431  0.28 38.55  ? 50  TRP   B CH2 1 
ATOM   1742 C CH2 D TRP   B 2 41  ? -18.354 4.845   -1.326  0.28 38.24  ? 50  TRP   B CH2 1 
ATOM   1743 N N   . HIS   B 2 42  ? -14.607 4.780   -8.072  1.00 34.91  ? 51  HIS   B N   1 
ATOM   1744 C CA  . HIS   B 2 42  ? -13.598 5.867   -8.287  1.00 33.39  ? 51  HIS   B CA  1 
ATOM   1745 C C   . HIS   B 2 42  ? -14.154 7.087   -9.076  1.00 33.12  ? 51  HIS   B C   1 
ATOM   1746 O O   . HIS   B 2 42  ? -13.564 8.157   -8.994  1.00 37.26  ? 51  HIS   B O   1 
ATOM   1747 C CB  . HIS   B 2 42  ? -12.282 5.328   -8.864  1.00 35.34  ? 51  HIS   B CB  1 
ATOM   1748 C CG  . HIS   B 2 42  ? -12.307 5.121   -10.325 1.00 33.59  ? 51  HIS   B CG  1 
ATOM   1749 N ND1 . HIS   B 2 42  ? -12.633 3.913   -10.890 1.00 37.41  ? 51  HIS   B ND1 1 
ATOM   1750 C CD2 . HIS   B 2 42  ? -12.037 5.975   -11.343 1.00 36.32  ? 51  HIS   B CD2 1 
ATOM   1751 C CE1 . HIS   B 2 42  ? -12.564 4.028   -12.203 1.00 36.03  ? 51  HIS   B CE1 1 
ATOM   1752 N NE2 . HIS   B 2 42  ? -12.208 5.297   -12.500 1.00 33.72  ? 51  HIS   B NE2 1 
ATOM   1753 N N   A VAL   B 2 43  ? -15.236 6.904   -9.832  0.22 33.51  ? 52  VAL   B N   1 
ATOM   1754 N N   B VAL   B 2 43  ? -15.236 6.904   -9.832  0.22 33.51  ? 52  VAL   B N   1 
ATOM   1755 N N   C VAL   B 2 43  ? -15.297 6.922   -9.750  0.28 32.88  ? 52  VAL   B N   1 
ATOM   1756 N N   D VAL   B 2 43  ? -15.297 6.922   -9.750  0.28 32.89  ? 52  VAL   B N   1 
ATOM   1757 C CA  A VAL   B 2 43  ? -15.940 8.010   -10.542 0.22 34.69  ? 52  VAL   B CA  1 
ATOM   1758 C CA  B VAL   B 2 43  ? -15.940 8.010   -10.543 0.22 34.69  ? 52  VAL   B CA  1 
ATOM   1759 C CA  C VAL   B 2 43  ? -15.968 7.961   -10.591 0.28 33.80  ? 52  VAL   B CA  1 
ATOM   1760 C CA  D VAL   B 2 43  ? -15.968 7.961   -10.591 0.28 33.80  ? 52  VAL   B CA  1 
ATOM   1761 C C   A VAL   B 2 43  ? -16.563 8.934   -9.484  0.22 35.29  ? 52  VAL   B C   1 
ATOM   1762 C C   B VAL   B 2 43  ? -16.563 8.934   -9.484  0.22 35.29  ? 52  VAL   B C   1 
ATOM   1763 C C   C VAL   B 2 43  ? -16.798 8.922   -9.714  0.28 34.58  ? 52  VAL   B C   1 
ATOM   1764 C C   D VAL   B 2 43  ? -16.797 8.922   -9.714  0.28 34.57  ? 52  VAL   B C   1 
ATOM   1765 O O   A VAL   B 2 43  ? -16.083 10.077  -9.345  0.22 33.00  ? 52  VAL   B O   1 
ATOM   1766 O O   B VAL   B 2 43  ? -16.083 10.077  -9.345  0.22 33.01  ? 52  VAL   B O   1 
ATOM   1767 O O   C VAL   B 2 43  ? -16.784 10.129  -10.017 0.28 32.74  ? 52  VAL   B O   1 
ATOM   1768 O O   D VAL   B 2 43  ? -16.783 10.129  -10.017 0.28 32.75  ? 52  VAL   B O   1 
ATOM   1769 C CB  A VAL   B 2 43  ? -16.981 7.451   -11.530 0.22 36.02  ? 52  VAL   B CB  1 
ATOM   1770 C CB  B VAL   B 2 43  ? -16.981 7.451   -11.530 0.22 36.02  ? 52  VAL   B CB  1 
ATOM   1771 C CB  C VAL   B 2 43  ? -16.821 7.280   -11.679 0.28 34.68  ? 52  VAL   B CB  1 
ATOM   1772 C CB  D VAL   B 2 43  ? -16.822 7.281   -11.679 0.28 34.67  ? 52  VAL   B CB  1 
ATOM   1773 C CG1 A VAL   B 2 43  ? -17.889 8.535   -12.096 0.22 36.70  ? 52  VAL   B CG1 1 
ATOM   1774 C CG1 B VAL   B 2 43  ? -17.889 8.535   -12.096 0.22 36.69  ? 52  VAL   B CG1 1 
ATOM   1775 C CG1 C VAL   B 2 43  ? -17.820 8.225   -12.340 0.28 35.05  ? 52  VAL   B CG1 1 
ATOM   1776 C CG1 D VAL   B 2 43  ? -17.820 8.226   -12.340 0.28 35.04  ? 52  VAL   B CG1 1 
ATOM   1777 C CG2 A VAL   B 2 43  ? -16.309 6.675   -12.654 0.22 36.02  ? 52  VAL   B CG2 1 
ATOM   1778 C CG2 B VAL   B 2 43  ? -16.309 6.675   -12.654 0.22 36.02  ? 52  VAL   B CG2 1 
ATOM   1779 C CG2 C VAL   B 2 43  ? -15.937 6.621   -12.723 0.28 34.19  ? 52  VAL   B CG2 1 
ATOM   1780 C CG2 D VAL   B 2 43  ? -15.937 6.621   -12.724 0.28 34.19  ? 52  VAL   B CG2 1 
ATOM   1781 N N   . THR   B 2 44  ? -17.513 8.419   -8.695  1.00 33.24  ? 53  THR   B N   1 
ATOM   1782 C CA  . THR   B 2 44  ? -18.395 9.263   -7.802  1.00 35.35  ? 53  THR   B CA  1 
ATOM   1783 C C   . THR   B 2 44  ? -17.822 9.448   -6.390  1.00 39.35  ? 53  THR   B C   1 
ATOM   1784 O O   . THR   B 2 44  ? -18.229 10.408  -5.699  1.00 39.28  ? 53  THR   B O   1 
ATOM   1785 C CB  . THR   B 2 44  ? -19.824 8.704   -7.786  1.00 32.51  ? 53  THR   B CB  1 
ATOM   1786 O OG1 . THR   B 2 44  ? -19.840 7.480   -7.068  1.00 35.02  ? 53  THR   B OG1 1 
ATOM   1787 C CG2 . THR   B 2 44  ? -20.426 8.504   -9.163  1.00 31.40  ? 53  THR   B CG2 1 
ATOM   1788 N N   . LYS   B 2 45  ? -16.924 8.551   -5.956  1.00 34.79  ? 54  LYS   B N   1 
ATOM   1789 C CA  . LYS   B 2 45  ? -16.429 8.399   -4.562  1.00 39.90  ? 54  LYS   B CA  1 
ATOM   1790 C C   . LYS   B 2 45  ? -17.596 8.249   -3.562  1.00 38.54  ? 54  LYS   B C   1 
ATOM   1791 O O   . LYS   B 2 45  ? -17.450 8.654   -2.398  1.00 43.90  ? 54  LYS   B O   1 
ATOM   1792 C CB  . LYS   B 2 45  ? -15.560 9.589   -4.141  1.00 47.35  ? 54  LYS   B CB  1 
ATOM   1793 C CG  . LYS   B 2 45  ? -14.511 10.024  -5.144  1.00 59.52  ? 54  LYS   B CG  1 
ATOM   1794 C CD  . LYS   B 2 45  ? -13.338 9.090   -5.285  1.00 66.33  ? 54  LYS   B CD  1 
ATOM   1795 C CE  . LYS   B 2 45  ? -12.210 9.735   -6.072  1.00 71.71  ? 54  LYS   B CE  1 
ATOM   1796 N NZ  . LYS   B 2 45  ? -11.673 8.828   -7.117  1.00 75.37  ? 54  LYS   B NZ  1 
ATOM   1797 N N   A GLY   B 2 46  ? -18.709 7.658   -4.007  0.22 39.73  ? 55  GLY   B N   1 
ATOM   1798 N N   B GLY   B 2 46  ? -18.709 7.659   -4.007  0.22 39.73  ? 55  GLY   B N   1 
ATOM   1799 N N   C GLY   B 2 46  ? -18.725 7.692   -4.011  0.28 39.16  ? 55  GLY   B N   1 
ATOM   1800 N N   D GLY   B 2 46  ? -18.725 7.693   -4.011  0.28 39.17  ? 55  GLY   B N   1 
ATOM   1801 C CA  A GLY   B 2 46  ? -19.903 7.410   -3.176  0.22 40.41  ? 55  GLY   B CA  1 
ATOM   1802 C CA  B GLY   B 2 46  ? -19.904 7.410   -3.176  0.22 40.41  ? 55  GLY   B CA  1 
ATOM   1803 C CA  C GLY   B 2 46  ? -19.898 7.405   -3.161  0.28 39.76  ? 55  GLY   B CA  1 
ATOM   1804 C CA  D GLY   B 2 46  ? -19.898 7.406   -3.160  0.28 39.77  ? 55  GLY   B CA  1 
ATOM   1805 C C   A GLY   B 2 46  ? -20.677 8.685   -2.883  0.22 41.26  ? 55  GLY   B C   1 
ATOM   1806 C C   B GLY   B 2 46  ? -20.679 8.685   -2.883  0.22 41.26  ? 55  GLY   B C   1 
ATOM   1807 C C   C GLY   B 2 46  ? -20.856 8.584   -3.055  0.28 41.00  ? 55  GLY   B C   1 
ATOM   1808 C C   D GLY   B 2 46  ? -20.856 8.584   -3.055  0.28 40.99  ? 55  GLY   B C   1 
ATOM   1809 O O   A GLY   B 2 46  ? -21.336 8.737   -1.835  0.22 43.08  ? 55  GLY   B O   1 
ATOM   1810 O O   B GLY   B 2 46  ? -21.338 8.737   -1.836  0.22 43.07  ? 55  GLY   B O   1 
ATOM   1811 O O   C GLY   B 2 46  ? -21.871 8.433   -2.365  0.28 39.98  ? 55  GLY   B O   1 
ATOM   1812 O O   D GLY   B 2 46  ? -21.871 8.434   -2.365  0.28 39.98  ? 55  GLY   B O   1 
ATOM   1813 N N   . ALA   B 2 47  ? -20.591 9.684   -3.765  1.00 40.91  ? 56  ALA   B N   1 
ATOM   1814 C CA  . ALA   B 2 47  ? -21.386 10.935  -3.673  1.00 42.68  ? 56  ALA   B CA  1 
ATOM   1815 C C   . ALA   B 2 47  ? -22.752 10.750  -4.339  1.00 42.95  ? 56  ALA   B C   1 
ATOM   1816 O O   . ALA   B 2 47  ? -22.885 9.982   -5.287  1.00 40.89  ? 56  ALA   B O   1 
ATOM   1817 C CB  . ALA   B 2 47  ? -20.620 12.084  -4.306  1.00 41.51  ? 56  ALA   B CB  1 
ATOM   1818 N N   . ALA   B 2 48  ? -23.742 11.501  -3.880  1.00 38.86  ? 57  ALA   B N   1 
ATOM   1819 C CA  . ALA   B 2 48  ? -25.073 11.607  -4.490  1.00 40.97  ? 57  ALA   B CA  1 
ATOM   1820 C C   . ALA   B 2 48  ? -24.953 12.224  -5.879  1.00 37.23  ? 57  ALA   B C   1 
ATOM   1821 O O   . ALA   B 2 48  ? -23.982 12.961  -6.151  1.00 40.68  ? 57  ALA   B O   1 
ATOM   1822 C CB  . ALA   B 2 48  ? -25.981 12.441  -3.614  1.00 48.45  ? 57  ALA   B CB  1 
ATOM   1823 N N   . LEU   B 2 49  ? -25.922 11.901  -6.715  1.00 37.11  ? 58  LEU   B N   1 
ATOM   1824 C CA  . LEU   B 2 49  ? -26.007 12.343  -8.126  1.00 40.16  ? 58  LEU   B CA  1 
ATOM   1825 C C   . LEU   B 2 49  ? -27.349 13.053  -8.372  1.00 44.47  ? 58  LEU   B C   1 
ATOM   1826 O O   . LEU   B 2 49  ? -28.373 12.660  -7.772  1.00 47.55  ? 58  LEU   B O   1 
ATOM   1827 C CB  . LEU   B 2 49  ? -25.907 11.124  -9.052  1.00 38.16  ? 58  LEU   B CB  1 
ATOM   1828 C CG  . LEU   B 2 49  ? -24.697 10.201  -8.874  1.00 36.41  ? 58  LEU   B CG  1 
ATOM   1829 C CD1 . LEU   B 2 49  ? -24.870 8.946   -9.710  1.00 35.85  ? 58  LEU   B CD1 1 
ATOM   1830 C CD2 . LEU   B 2 49  ? -23.393 10.901  -9.250  1.00 37.73  ? 58  LEU   B CD2 1 
ATOM   1831 N N   . ARG   B 2 50  ? -27.361 13.998  -9.303  1.00 42.59  ? 59  ARG   B N   1 
ATOM   1832 C CA  . ARG   B 2 50  ? -28.592 14.672  -9.783  1.00 50.01  ? 59  ARG   B CA  1 
ATOM   1833 C C   . ARG   B 2 50  ? -29.005 14.045  -11.122 1.00 50.86  ? 59  ARG   B C   1 
ATOM   1834 O O   . ARG   B 2 50  ? -28.132 13.729  -11.935 1.00 52.01  ? 59  ARG   B O   1 
ATOM   1835 C CB  . ARG   B 2 50  ? -28.298 16.172  -9.840  1.00 57.33  ? 59  ARG   B CB  1 
ATOM   1836 C CG  . ARG   B 2 50  ? -29.477 17.037  -10.262 1.00 70.79  ? 59  ARG   B CG  1 
ATOM   1837 C CD  . ARG   B 2 50  ? -29.269 18.478  -9.845  1.00 73.85  ? 59  ARG   B CD  1 
ATOM   1838 N NE  . ARG   B 2 50  ? -27.858 18.840  -9.947  1.00 77.70  ? 59  ARG   B NE  1 
ATOM   1839 C CZ  . ARG   B 2 50  ? -27.223 19.126  -11.081 1.00 72.69  ? 59  ARG   B CZ  1 
ATOM   1840 N NH1 . ARG   B 2 50  ? -27.864 19.087  -12.243 1.00 70.50  ? 59  ARG   B NH1 1 
ATOM   1841 N NH2 . ARG   B 2 50  ? -25.936 19.431  -11.044 1.00 75.57  ? 59  ARG   B NH2 1 
ATOM   1842 N N   . SER   B 2 51  ? -30.287 13.755  -11.299 1.00 47.23  ? 60  SER   B N   1 
ATOM   1843 C CA  . SER   B 2 51  ? -30.923 13.475  -12.610 1.00 52.45  ? 60  SER   B CA  1 
ATOM   1844 C C   . SER   B 2 51  ? -32.190 14.333  -12.735 1.00 56.17  ? 60  SER   B C   1 
ATOM   1845 O O   . SER   B 2 51  ? -33.133 14.106  -11.942 1.00 65.00  ? 60  SER   B O   1 
ATOM   1846 C CB  . SER   B 2 51  ? -31.272 12.030  -12.742 1.00 50.34  ? 60  SER   B CB  1 
ATOM   1847 O OG  . SER   B 2 51  ? -31.823 11.779  -14.016 1.00 53.91  ? 60  SER   B OG  1 
ATOM   1848 N N   . GLY   B 2 52  ? -32.234 15.266  -13.681 1.00 59.85  ? 61  GLY   B N   1 
ATOM   1849 C CA  . GLY   B 2 52  ? -33.279 16.312  -13.690 1.00 69.66  ? 61  GLY   B CA  1 
ATOM   1850 C C   . GLY   B 2 52  ? -33.186 17.137  -12.416 1.00 71.22  ? 61  GLY   B C   1 
ATOM   1851 O O   . GLY   B 2 52  ? -32.064 17.569  -12.059 1.00 76.17  ? 61  GLY   B O   1 
ATOM   1852 N N   . GLU   B 2 53  ? -34.300 17.291  -11.708 1.00 73.06  ? 62  GLU   B N   1 
ATOM   1853 C CA  . GLU   B 2 53  ? -34.315 17.863  -10.337 1.00 78.94  ? 62  GLU   B CA  1 
ATOM   1854 C C   . GLU   B 2 53  ? -34.364 16.734  -9.301  1.00 72.53  ? 62  GLU   B C   1 
ATOM   1855 O O   . GLU   B 2 53  ? -34.312 17.070  -8.107  1.00 64.48  ? 62  GLU   B O   1 
ATOM   1856 C CB  . GLU   B 2 53  ? -35.479 18.839  -10.194 1.00 84.66  ? 62  GLU   B CB  1 
ATOM   1857 C CG  . GLU   B 2 53  ? -35.193 20.154  -10.885 1.00 100.20 ? 62  GLU   B CG  1 
ATOM   1858 C CD  . GLU   B 2 53  ? -36.408 21.021  -11.144 1.00 113.49 ? 62  GLU   B CD  1 
ATOM   1859 O OE1 . GLU   B 2 53  ? -37.463 20.465  -11.521 1.00 124.19 ? 62  GLU   B OE1 1 
ATOM   1860 O OE2 . GLU   B 2 53  ? -36.291 22.253  -10.981 1.00 127.36 ? 62  GLU   B OE2 1 
ATOM   1861 N N   . GLY   B 2 54  ? -34.432 15.469  -9.750  1.00 65.63  ? 63  GLY   B N   1 
ATOM   1862 C CA  . GLY   B 2 54  ? -34.417 14.256  -8.905  1.00 67.03  ? 63  GLY   B CA  1 
ATOM   1863 C C   . GLY   B 2 54  ? -33.008 13.933  -8.429  1.00 65.70  ? 63  GLY   B C   1 
ATOM   1864 O O   . GLY   B 2 54  ? -32.061 14.291  -9.146  1.00 58.93  ? 63  GLY   B O   1 
ATOM   1865 N N   . ARG   B 2 55  ? -32.880 13.315  -7.249  1.00 58.67  ? 64  ARG   B N   1 
ATOM   1866 C CA  . ARG   B 2 55  ? -31.590 12.964  -6.585  1.00 51.28  ? 64  ARG   B CA  1 
ATOM   1867 C C   . ARG   B 2 55  ? -31.414 11.437  -6.610  1.00 53.61  ? 64  ARG   B C   1 
ATOM   1868 O O   . ARG   B 2 55  ? -32.384 10.689  -6.402  1.00 47.68  ? 64  ARG   B O   1 
ATOM   1869 C CB  . ARG   B 2 55  ? -31.566 13.504  -5.152  1.00 54.76  ? 64  ARG   B CB  1 
ATOM   1870 C CG  . ARG   B 2 55  ? -30.243 13.358  -4.413  1.00 57.66  ? 64  ARG   B CG  1 
ATOM   1871 C CD  . ARG   B 2 55  ? -30.439 13.730  -2.948  1.00 59.66  ? 64  ARG   B CD  1 
ATOM   1872 N NE  . ARG   B 2 55  ? -29.319 13.383  -2.086  1.00 64.55  ? 64  ARG   B NE  1 
ATOM   1873 C CZ  . ARG   B 2 55  ? -28.540 14.239  -1.416  1.00 65.53  ? 64  ARG   B CZ  1 
ATOM   1874 N NH1 . ARG   B 2 55  ? -28.756 15.541  -1.481  1.00 67.13  ? 64  ARG   B NH1 1 
ATOM   1875 N NH2 . ARG   B 2 55  ? -27.554 13.781  -0.653  1.00 63.78  ? 64  ARG   B NH2 1 
ATOM   1876 N N   . LEU   B 2 56  ? -30.195 10.972  -6.863  1.00 46.10  ? 65  LEU   B N   1 
ATOM   1877 C CA  . LEU   B 2 56  ? -29.874 9.534   -6.756  1.00 43.74  ? 65  LEU   B CA  1 
ATOM   1878 C C   . LEU   B 2 56  ? -28.961 9.399   -5.546  1.00 38.22  ? 65  LEU   B C   1 
ATOM   1879 O O   . LEU   B 2 56  ? -27.875 10.021  -5.537  1.00 39.19  ? 65  LEU   B O   1 
ATOM   1880 C CB  . LEU   B 2 56  ? -29.167 9.072   -8.037  1.00 39.73  ? 65  LEU   B CB  1 
ATOM   1881 C CG  . LEU   B 2 56  ? -29.954 9.073   -9.340  1.00 45.56  ? 65  LEU   B CG  1 
ATOM   1882 C CD1 . LEU   B 2 56  ? -29.251 8.173   -10.357 1.00 47.30  ? 65  LEU   B CD1 1 
ATOM   1883 C CD2 . LEU   B 2 56  ? -31.383 8.576   -9.150  1.00 53.30  ? 65  LEU   B CD2 1 
ATOM   1884 N N   A ASP   B 2 57  ? -29.383 8.612   -4.550  0.23 37.39  ? 66  ASP   B N   1 
ATOM   1885 N N   B ASP   B 2 57  ? -29.383 8.612   -4.550  0.23 37.39  ? 66  ASP   B N   1 
ATOM   1886 N N   C ASP   B 2 57  ? -29.380 8.609   -4.552  0.27 37.46  ? 66  ASP   B N   1 
ATOM   1887 N N   D ASP   B 2 57  ? -29.380 8.609   -4.552  0.27 37.46  ? 66  ASP   B N   1 
ATOM   1888 C CA  A ASP   B 2 57  ? -28.592 8.339   -3.322  0.23 36.87  ? 66  ASP   B CA  1 
ATOM   1889 C CA  B ASP   B 2 57  ? -28.592 8.339   -3.322  0.23 36.87  ? 66  ASP   B CA  1 
ATOM   1890 C CA  C ASP   B 2 57  ? -28.585 8.342   -3.326  0.27 37.14  ? 66  ASP   B CA  1 
ATOM   1891 C CA  D ASP   B 2 57  ? -28.585 8.342   -3.326  0.27 37.14  ? 66  ASP   B CA  1 
ATOM   1892 C C   A ASP   B 2 57  ? -27.875 6.996   -3.455  0.23 34.17  ? 66  ASP   B C   1 
ATOM   1893 C C   B ASP   B 2 57  ? -27.875 6.996   -3.455  0.23 34.17  ? 66  ASP   B C   1 
ATOM   1894 C C   C ASP   B 2 57  ? -27.875 6.994   -3.450  0.27 34.12  ? 66  ASP   B C   1 
ATOM   1895 C C   D ASP   B 2 57  ? -27.875 6.994   -3.450  0.27 34.12  ? 66  ASP   B C   1 
ATOM   1896 O O   A ASP   B 2 57  ? -28.455 6.020   -3.934  0.23 35.16  ? 66  ASP   B O   1 
ATOM   1897 O O   B ASP   B 2 57  ? -28.455 6.020   -3.934  0.23 35.16  ? 66  ASP   B O   1 
ATOM   1898 O O   C ASP   B 2 57  ? -28.462 6.014   -3.911  0.27 35.30  ? 66  ASP   B O   1 
ATOM   1899 O O   D ASP   B 2 57  ? -28.462 6.014   -3.911  0.27 35.30  ? 66  ASP   B O   1 
ATOM   1900 C CB  A ASP   B 2 57  ? -29.481 8.369   -2.077  0.23 40.24  ? 66  ASP   B CB  1 
ATOM   1901 C CB  B ASP   B 2 57  ? -29.481 8.369   -2.077  0.23 40.24  ? 66  ASP   B CB  1 
ATOM   1902 C CB  C ASP   B 2 57  ? -29.471 8.395   -2.082  0.27 41.26  ? 66  ASP   B CB  1 
ATOM   1903 C CB  D ASP   B 2 57  ? -29.471 8.395   -2.082  0.27 41.26  ? 66  ASP   B CB  1 
ATOM   1904 C CG  A ASP   B 2 57  ? -29.795 9.780   -1.605  0.23 41.51  ? 66  ASP   B CG  1 
ATOM   1905 C CG  B ASP   B 2 57  ? -29.795 9.780   -1.605  0.23 41.51  ? 66  ASP   B CG  1 
ATOM   1906 C CG  C ASP   B 2 57  ? -29.959 9.800   -1.766  0.27 42.70  ? 66  ASP   B CG  1 
ATOM   1907 C CG  D ASP   B 2 57  ? -29.959 9.800   -1.766  0.27 42.70  ? 66  ASP   B CG  1 
ATOM   1908 O OD1 A ASP   B 2 57  ? -29.908 9.975   -0.378  0.23 40.55  ? 66  ASP   B OD1 1 
ATOM   1909 O OD1 B ASP   B 2 57  ? -29.908 9.975   -0.378  0.23 40.55  ? 66  ASP   B OD1 1 
ATOM   1910 O OD1 C ASP   B 2 57  ? -29.098 10.684  -1.540  0.27 44.29  ? 66  ASP   B OD1 1 
ATOM   1911 O OD1 D ASP   B 2 57  ? -29.098 10.684  -1.540  0.27 44.29  ? 66  ASP   B OD1 1 
ATOM   1912 O OD2 A ASP   B 2 57  ? -29.903 10.675  -2.472  0.23 41.00  ? 66  ASP   B OD2 1 
ATOM   1913 O OD2 B ASP   B 2 57  ? -29.903 10.675  -2.472  0.23 41.00  ? 66  ASP   B OD2 1 
ATOM   1914 O OD2 C ASP   B 2 57  ? -31.187 10.003  -1.779  0.27 40.17  ? 66  ASP   B OD2 1 
ATOM   1915 O OD2 D ASP   B 2 57  ? -31.187 10.003  -1.779  0.27 40.17  ? 66  ASP   B OD2 1 
ATOM   1916 N N   . PRO   B 2 58  ? -26.607 6.887   -2.996  1.00 33.44  ? 67  PRO   B N   1 
ATOM   1917 C CA  . PRO   B 2 58  ? -25.890 5.598   -3.011  1.00 33.48  ? 67  PRO   B CA  1 
ATOM   1918 C C   . PRO   B 2 58  ? -26.644 4.549   -2.179  1.00 36.17  ? 67  PRO   B C   1 
ATOM   1919 O O   . PRO   B 2 58  ? -27.287 4.921   -1.175  1.00 36.92  ? 67  PRO   B O   1 
ATOM   1920 C CB  . PRO   B 2 58  ? -24.543 5.994   -2.420  1.00 31.83  ? 67  PRO   B CB  1 
ATOM   1921 C CG  . PRO   B 2 58  ? -24.838 7.185   -1.585  1.00 33.52  ? 67  PRO   B CG  1 
ATOM   1922 C CD  . PRO   B 2 58  ? -25.815 7.976   -2.405  1.00 32.36  ? 67  PRO   B CD  1 
ATOM   1923 N N   . TYR   B 2 59  ? -26.686 3.301   -2.629  1.00 29.79  ? 68  TYR   B N   1 
ATOM   1924 C CA  . TYR   B 2 59  ? -27.357 2.186   -1.932  1.00 30.32  ? 68  TYR   B CA  1 
ATOM   1925 C C   . TYR   B 2 59  ? -26.333 1.150   -1.452  1.00 33.26  ? 68  TYR   B C   1 
ATOM   1926 O O   . TYR   B 2 59  ? -26.451 0.647   -0.363  1.00 30.85  ? 68  TYR   B O   1 
ATOM   1927 C CB  . TYR   B 2 59  ? -28.437 1.594   -2.839  1.00 32.64  ? 68  TYR   B CB  1 
ATOM   1928 C CG  . TYR   B 2 59  ? -29.256 0.484   -2.220  1.00 32.70  ? 68  TYR   B CG  1 
ATOM   1929 C CD1 . TYR   B 2 59  ? -28.731 -0.801  -2.117  1.00 32.97  ? 68  TYR   B CD1 1 
ATOM   1930 C CD2 . TYR   B 2 59  ? -30.558 0.690   -1.781  1.00 32.96  ? 68  TYR   B CD2 1 
ATOM   1931 C CE1 . TYR   B 2 59  ? -29.499 -1.856  -1.639  1.00 34.24  ? 68  TYR   B CE1 1 
ATOM   1932 C CE2 . TYR   B 2 59  ? -31.329 -0.356  -1.269  1.00 33.70  ? 68  TYR   B CE2 1 
ATOM   1933 C CZ  . TYR   B 2 59  ? -30.782 -1.633  -1.171  1.00 35.21  ? 68  TYR   B CZ  1 
ATOM   1934 O OH  . TYR   B 2 59  ? -31.481 -2.718  -0.695  1.00 36.66  ? 68  TYR   B OH  1 
ATOM   1935 N N   . TRP   B 2 60  ? -25.390 0.790   -2.302  1.00 30.63  ? 69  TRP   B N   1 
ATOM   1936 C CA  . TRP   B 2 60  ? -24.356 -0.257  -2.077  1.00 30.06  ? 69  TRP   B CA  1 
ATOM   1937 C C   . TRP   B 2 60  ? -23.047 0.239   -2.674  1.00 29.52  ? 69  TRP   B C   1 
ATOM   1938 O O   . TRP   B 2 60  ? -23.058 0.789   -3.808  1.00 30.18  ? 69  TRP   B O   1 
ATOM   1939 C CB  . TRP   B 2 60  ? -24.741 -1.618  -2.647  1.00 28.44  ? 69  TRP   B CB  1 
ATOM   1940 C CG  . TRP   B 2 60  ? -23.601 -2.582  -2.548  1.00 29.59  ? 69  TRP   B CG  1 
ATOM   1941 C CD1 . TRP   B 2 60  ? -23.150 -3.265  -1.456  1.00 31.11  ? 69  TRP   B CD1 1 
ATOM   1942 C CD2 . TRP   B 2 60  ? -22.725 -2.929  -3.623  1.00 25.28  ? 69  TRP   B CD2 1 
ATOM   1943 N NE1 . TRP   B 2 60  ? -22.045 -4.011  -1.792  1.00 29.28  ? 69  TRP   B NE1 1 
ATOM   1944 C CE2 . TRP   B 2 60  ? -21.757 -3.814  -3.111  1.00 29.33  ? 69  TRP   B CE2 1 
ATOM   1945 C CE3 . TRP   B 2 60  ? -22.640 -2.505  -4.951  1.00 30.66  ? 69  TRP   B CE3 1 
ATOM   1946 C CZ2 . TRP   B 2 60  ? -20.723 -4.307  -3.899  1.00 28.61  ? 69  TRP   B CZ2 1 
ATOM   1947 C CZ3 . TRP   B 2 60  ? -21.636 -3.022  -5.741  1.00 25.82  ? 69  TRP   B CZ3 1 
ATOM   1948 C CH2 . TRP   B 2 60  ? -20.702 -3.916  -5.229  1.00 29.43  ? 69  TRP   B CH2 1 
ATOM   1949 N N   . GLY   B 2 61  ? -21.939 -0.009  -2.002  1.00 32.05  ? 70  GLY   B N   1 
ATOM   1950 C CA  . GLY   B 2 61  ? -20.631 0.282   -2.606  1.00 34.57  ? 70  GLY   B CA  1 
ATOM   1951 C C   . GLY   B 2 61  ? -19.544 -0.518  -1.962  1.00 31.41  ? 70  GLY   B C   1 
ATOM   1952 O O   . GLY   B 2 61  ? -19.712 -0.963  -0.800  1.00 32.21  ? 70  GLY   B O   1 
ATOM   1953 N N   A ASP   B 2 62  ? -18.440 -0.711  -2.679  0.22 31.58  ? 71  ASP   B N   1 
ATOM   1954 N N   B ASP   B 2 62  ? -18.440 -0.711  -2.679  0.22 31.58  ? 71  ASP   B N   1 
ATOM   1955 N N   C ASP   B 2 62  ? -18.441 -0.695  -2.687  0.28 31.18  ? 71  ASP   B N   1 
ATOM   1956 N N   D ASP   B 2 62  ? -18.441 -0.695  -2.687  0.28 31.18  ? 71  ASP   B N   1 
ATOM   1957 C CA  A ASP   B 2 62  ? -17.222 -1.389  -2.156  0.22 30.61  ? 71  ASP   B CA  1 
ATOM   1958 C CA  B ASP   B 2 62  ? -17.222 -1.389  -2.156  0.22 30.62  ? 71  ASP   B CA  1 
ATOM   1959 C CA  C ASP   B 2 62  ? -17.222 -1.421  -2.232  0.28 29.84  ? 71  ASP   B CA  1 
ATOM   1960 C CA  D ASP   B 2 62  ? -17.222 -1.421  -2.232  0.28 29.84  ? 71  ASP   B CA  1 
ATOM   1961 C C   A ASP   B 2 62  ? -16.010 -0.871  -2.932  0.22 30.51  ? 71  ASP   B C   1 
ATOM   1962 C C   B ASP   B 2 62  ? -16.010 -0.871  -2.932  0.22 30.51  ? 71  ASP   B C   1 
ATOM   1963 C C   C ASP   B 2 62  ? -16.011 -0.837  -2.961  0.28 30.11  ? 71  ASP   B C   1 
ATOM   1964 C C   D ASP   B 2 62  ? -16.011 -0.837  -2.961  0.28 30.12  ? 71  ASP   B C   1 
ATOM   1965 O O   A ASP   B 2 62  ? -15.961 -1.076  -4.162  0.22 30.57  ? 71  ASP   B O   1 
ATOM   1966 O O   B ASP   B 2 62  ? -15.961 -1.076  -4.162  0.22 30.57  ? 71  ASP   B O   1 
ATOM   1967 O O   C ASP   B 2 62  ? -15.956 -0.969  -4.202  0.28 30.40  ? 71  ASP   B O   1 
ATOM   1968 O O   D ASP   B 2 62  ? -15.956 -0.969  -4.202  0.28 30.40  ? 71  ASP   B O   1 
ATOM   1969 C CB  A ASP   B 2 62  ? -17.366 -2.905  -2.219  0.22 30.54  ? 71  ASP   B CB  1 
ATOM   1970 C CB  B ASP   B 2 62  ? -17.366 -2.905  -2.220  0.22 30.54  ? 71  ASP   B CB  1 
ATOM   1971 C CB  C ASP   B 2 62  ? -17.351 -2.918  -2.489  0.28 29.49  ? 71  ASP   B CB  1 
ATOM   1972 C CB  D ASP   B 2 62  ? -17.351 -2.918  -2.489  0.28 29.50  ? 71  ASP   B CB  1 
ATOM   1973 C CG  A ASP   B 2 62  ? -16.126 -3.664  -1.773  0.22 31.97  ? 71  ASP   B CG  1 
ATOM   1974 C CG  B ASP   B 2 62  ? -16.126 -3.664  -1.773  0.22 31.97  ? 71  ASP   B CG  1 
ATOM   1975 C CG  C ASP   B 2 62  ? -16.246 -3.750  -1.859  0.28 30.15  ? 71  ASP   B CG  1 
ATOM   1976 C CG  D ASP   B 2 62  ? -16.246 -3.751  -1.859  0.28 30.15  ? 71  ASP   B CG  1 
ATOM   1977 O OD1 A ASP   B 2 62  ? -15.783 -4.641  -2.448  0.22 30.93  ? 71  ASP   B OD1 1 
ATOM   1978 O OD1 B ASP   B 2 62  ? -15.783 -4.641  -2.448  0.22 30.93  ? 71  ASP   B OD1 1 
ATOM   1979 O OD1 C ASP   B 2 62  ? -15.050 -3.461  -2.108  0.28 28.55  ? 71  ASP   B OD1 1 
ATOM   1980 O OD1 D ASP   B 2 62  ? -15.050 -3.461  -2.108  0.28 28.55  ? 71  ASP   B OD1 1 
ATOM   1981 O OD2 A ASP   B 2 62  ? -15.517 -3.275  -0.747  0.22 31.40  ? 71  ASP   B OD2 1 
ATOM   1982 O OD2 B ASP   B 2 62  ? -15.518 -3.275  -0.747  0.22 31.40  ? 71  ASP   B OD2 1 
ATOM   1983 O OD2 C ASP   B 2 62  ? -16.592 -4.656  -1.090  0.28 28.04  ? 71  ASP   B OD2 1 
ATOM   1984 O OD2 D ASP   B 2 62  ? -16.592 -4.657  -1.090  0.28 28.05  ? 71  ASP   B OD2 1 
ATOM   1985 N N   . VAL   B 2 63  ? -15.083 -0.224  -2.218  1.00 30.12  ? 72  VAL   B N   1 
ATOM   1986 C CA  . VAL   B 2 63  ? -13.869 0.390   -2.791  1.00 31.09  ? 72  VAL   B CA  1 
ATOM   1987 C C   . VAL   B 2 63  ? -12.979 -0.714  -3.382  1.00 36.46  ? 72  VAL   B C   1 
ATOM   1988 O O   . VAL   B 2 63  ? -12.287 -0.420  -4.385  1.00 32.56  ? 72  VAL   B O   1 
ATOM   1989 C CB  . VAL   B 2 63  ? -13.088 1.219   -1.760  1.00 33.96  ? 72  VAL   B CB  1 
ATOM   1990 C CG1 . VAL   B 2 63  ? -11.664 1.464   -2.189  1.00 36.25  ? 72  VAL   B CG1 1 
ATOM   1991 C CG2 . VAL   B 2 63  ? -13.749 2.536   -1.448  1.00 32.24  ? 72  VAL   B CG2 1 
ATOM   1992 N N   . LYS   B 2 64  ? -13.028 -1.947  -2.877  1.00 34.70  ? 73  LYS   B N   1 
ATOM   1993 C CA  . LYS   B 2 64  ? -12.067 -2.976  -3.372  1.00 35.73  ? 73  LYS   B CA  1 
ATOM   1994 C C   . LYS   B 2 64  ? -12.555 -3.526  -4.723  1.00 33.39  ? 73  LYS   B C   1 
ATOM   1995 O O   . LYS   B 2 64  ? -11.705 -3.735  -5.637  1.00 38.13  ? 73  LYS   B O   1 
ATOM   1996 C CB  . LYS   B 2 64  ? -11.860 -4.117  -2.379  1.00 34.99  ? 73  LYS   B CB  1 
ATOM   1997 C CG  . LYS   B 2 64  ? -10.842 -5.133  -2.895  1.00 38.30  ? 73  LYS   B CG  1 
ATOM   1998 C CD  . LYS   B 2 64  ? -10.388 -6.087  -1.866  1.00 37.93  ? 73  LYS   B CD  1 
ATOM   1999 C CE  . LYS   B 2 64  ? -9.254  -6.965  -2.364  1.00 43.79  ? 73  LYS   B CE  1 
ATOM   2000 N NZ  . LYS   B 2 64  ? -8.897  -7.970  -1.338  1.00 44.59  ? 73  LYS   B NZ  1 
ATOM   2001 N N   . GLN   B 2 65  ? -13.859 -3.798  -4.837  1.00 36.48  ? 74  GLN   B N   1 
ATOM   2002 C CA  . GLN   B 2 65  ? -14.522 -4.132  -6.120  1.00 34.88  ? 74  GLN   B CA  1 
ATOM   2003 C C   . GLN   B 2 65  ? -14.519 -2.930  -7.085  1.00 33.25  ? 74  GLN   B C   1 
ATOM   2004 O O   . GLN   B 2 65  ? -14.654 -3.173  -8.319  1.00 32.91  ? 74  GLN   B O   1 
ATOM   2005 C CB  . GLN   B 2 65  ? -15.958 -4.607  -5.920  1.00 34.38  ? 74  GLN   B CB  1 
ATOM   2006 C CG  . GLN   B 2 65  ? -16.063 -5.933  -5.186  1.00 39.17  ? 74  GLN   B CG  1 
ATOM   2007 C CD  . GLN   B 2 65  ? -17.488 -6.402  -5.057  1.00 42.86  ? 74  GLN   B CD  1 
ATOM   2008 O OE1 . GLN   B 2 65  ? -18.212 -6.592  -6.045  1.00 49.47  ? 74  GLN   B OE1 1 
ATOM   2009 N NE2 . GLN   B 2 65  ? -17.931 -6.536  -3.818  1.00 49.35  ? 74  GLN   B NE2 1 
ATOM   2010 N N   A ASP   B 2 66  ? -14.359 -1.715  -6.550  0.22 33.30  ? 75  ASP   B N   1 
ATOM   2011 N N   B ASP   B 2 66  ? -14.359 -1.715  -6.550  0.22 33.31  ? 75  ASP   B N   1 
ATOM   2012 N N   C ASP   B 2 66  ? -14.356 -1.717  -6.532  0.28 33.38  ? 75  ASP   B N   1 
ATOM   2013 N N   D ASP   B 2 66  ? -14.356 -1.717  -6.531  0.28 33.39  ? 75  ASP   B N   1 
ATOM   2014 C CA  A ASP   B 2 66  ? -14.444 -0.418  -7.276  0.22 34.57  ? 75  ASP   B CA  1 
ATOM   2015 C CA  B ASP   B 2 66  ? -14.445 -0.418  -7.276  0.22 34.56  ? 75  ASP   B CA  1 
ATOM   2016 C CA  C ASP   B 2 66  ? -14.441 -0.375  -7.183  0.28 35.08  ? 75  ASP   B CA  1 
ATOM   2017 C CA  D ASP   B 2 66  ? -14.441 -0.376  -7.184  0.28 35.06  ? 75  ASP   B CA  1 
ATOM   2018 C C   A ASP   B 2 66  ? -15.813 -0.313  -7.952  0.22 33.91  ? 75  ASP   B C   1 
ATOM   2019 C C   B ASP   B 2 66  ? -15.813 -0.313  -7.952  0.22 33.90  ? 75  ASP   B C   1 
ATOM   2020 C C   C ASP   B 2 66  ? -15.793 -0.231  -7.888  0.28 33.93  ? 75  ASP   B C   1 
ATOM   2021 C C   D ASP   B 2 66  ? -15.793 -0.231  -7.888  0.28 33.91  ? 75  ASP   B C   1 
ATOM   2022 O O   A ASP   B 2 66  ? -15.849 0.092   -9.138  0.22 32.11  ? 75  ASP   B O   1 
ATOM   2023 O O   B ASP   B 2 66  ? -15.849 0.092   -9.138  0.22 32.11  ? 75  ASP   B O   1 
ATOM   2024 O O   C ASP   B 2 66  ? -15.784 0.316   -9.019  0.28 31.07  ? 75  ASP   B O   1 
ATOM   2025 O O   D ASP   B 2 66  ? -15.785 0.316   -9.019  0.28 31.08  ? 75  ASP   B O   1 
ATOM   2026 C CB  A ASP   B 2 66  ? -13.317 -0.261  -8.300  0.22 36.02  ? 75  ASP   B CB  1 
ATOM   2027 C CB  B ASP   B 2 66  ? -13.317 -0.261  -8.300  0.22 36.00  ? 75  ASP   B CB  1 
ATOM   2028 C CB  C ASP   B 2 66  ? -13.272 -0.124  -8.143  0.28 37.46  ? 75  ASP   B CB  1 
ATOM   2029 C CB  D ASP   B 2 66  ? -13.272 -0.124  -8.143  0.28 37.43  ? 75  ASP   B CB  1 
ATOM   2030 C CG  A ASP   B 2 66  ? -13.275 1.121   -8.930  0.22 35.57  ? 75  ASP   B CG  1 
ATOM   2031 C CG  B ASP   B 2 66  ? -13.275 1.121   -8.930  0.22 35.56  ? 75  ASP   B CG  1 
ATOM   2032 C CG  C ASP   B 2 66  ? -13.204 1.290   -8.707  0.28 36.71  ? 75  ASP   B CG  1 
ATOM   2033 C CG  D ASP   B 2 66  ? -13.204 1.290   -8.707  0.28 36.69  ? 75  ASP   B CG  1 
ATOM   2034 O OD1 A ASP   B 2 66  ? -13.887 2.040   -8.352  0.22 31.73  ? 75  ASP   B OD1 1 
ATOM   2035 O OD1 B ASP   B 2 66  ? -13.885 2.040   -8.350  0.22 31.74  ? 75  ASP   B OD1 1 
ATOM   2036 O OD1 C ASP   B 2 66  ? -13.211 2.262   -7.905  0.28 31.47  ? 75  ASP   B OD1 1 
ATOM   2037 O OD1 D ASP   B 2 66  ? -13.211 2.262   -7.904  0.28 31.49  ? 75  ASP   B OD1 1 
ATOM   2038 O OD2 A ASP   B 2 66  ? -12.637 1.262   -9.996  0.22 34.48  ? 75  ASP   B OD2 1 
ATOM   2039 O OD2 B ASP   B 2 66  ? -12.639 1.262   -9.997  0.22 34.48  ? 75  ASP   B OD2 1 
ATOM   2040 O OD2 C ASP   B 2 66  ? -13.123 1.407   -9.954  0.28 37.14  ? 75  ASP   B OD2 1 
ATOM   2041 O OD2 D ASP   B 2 66  ? -13.124 1.408   -9.953  0.28 37.13  ? 75  ASP   B OD2 1 
ATOM   2042 N N   . LEU   B 2 67  ? -16.882 -0.684  -7.235  1.00 30.43  ? 76  LEU   B N   1 
ATOM   2043 C CA  . LEU   B 2 67  ? -18.289 -0.621  -7.743  1.00 29.29  ? 76  LEU   B CA  1 
ATOM   2044 C C   . LEU   B 2 67  ? -19.225 0.116   -6.749  1.00 33.79  ? 76  LEU   B C   1 
ATOM   2045 O O   . LEU   B 2 67  ? -18.933 0.123   -5.531  1.00 31.43  ? 76  LEU   B O   1 
ATOM   2046 C CB  . LEU   B 2 67  ? -18.816 -2.021  -8.018  1.00 30.10  ? 76  LEU   B CB  1 
ATOM   2047 C CG  . LEU   B 2 67  ? -18.166 -2.833  -9.166  1.00 27.85  ? 76  LEU   B CG  1 
ATOM   2048 C CD1 . LEU   B 2 67  ? -18.890 -4.171  -9.265  1.00 27.29  ? 76  LEU   B CD1 1 
ATOM   2049 C CD2 . LEU   B 2 67  ? -18.300 -2.093  -10.511 1.00 27.56  ? 76  LEU   B CD2 1 
ATOM   2050 N N   . VAL   B 2 68  ? -20.323 0.676   -7.268  1.00 32.87  ? 77  VAL   B N   1 
ATOM   2051 C CA  . VAL   B 2 68  ? -21.357 1.442   -6.490  1.00 31.28  ? 77  VAL   B CA  1 
ATOM   2052 C C   . VAL   B 2 68  ? -22.678 1.418   -7.242  1.00 29.84  ? 77  VAL   B C   1 
ATOM   2053 O O   . VAL   B 2 68  ? -22.652 1.561   -8.512  1.00 28.59  ? 77  VAL   B O   1 
ATOM   2054 C CB  . VAL   B 2 68  ? -20.903 2.877   -6.192  1.00 31.26  ? 77  VAL   B CB  1 
ATOM   2055 C CG1 . VAL   B 2 68  ? -20.695 3.700   -7.464  1.00 31.43  ? 77  VAL   B CG1 1 
ATOM   2056 C CG2 . VAL   B 2 68  ? -21.906 3.593   -5.275  1.00 30.78  ? 77  VAL   B CG2 1 
ATOM   2057 N N   . SER   B 2 69  ? -23.791 1.113   -6.550  1.00 26.68  ? 78  SER   B N   1 
ATOM   2058 C CA  . SER   B 2 69  ? -25.167 1.195   -7.076  1.00 25.59  ? 78  SER   B CA  1 
ATOM   2059 C C   . SER   B 2 69  ? -25.922 2.346   -6.370  1.00 31.17  ? 78  SER   B C   1 
ATOM   2060 O O   . SER   B 2 69  ? -25.659 2.628   -5.165  1.00 27.92  ? 78  SER   B O   1 
ATOM   2061 C CB  . SER   B 2 69  ? -25.929 -0.127  -6.998  1.00 29.65  ? 78  SER   B CB  1 
ATOM   2062 O OG  . SER   B 2 69  ? -26.122 -0.544  -5.650  1.00 30.34  ? 78  SER   B OG  1 
ATOM   2063 N N   . TYR   B 2 70  ? -26.806 2.983   -7.118  1.00 28.75  ? 79  TYR   B N   1 
ATOM   2064 C CA  . TYR   B 2 70  ? -27.741 4.083   -6.695  1.00 30.01  ? 79  TYR   B CA  1 
ATOM   2065 C C   . TYR   B 2 70  ? -29.191 3.591   -6.818  1.00 33.56  ? 79  TYR   B C   1 
ATOM   2066 O O   . TYR   B 2 70  ? -29.578 3.015   -7.864  1.00 30.40  ? 79  TYR   B O   1 
ATOM   2067 C CB  . TYR   B 2 70  ? -27.475 5.358   -7.506  1.00 31.98  ? 79  TYR   B CB  1 
ATOM   2068 C CG  . TYR   B 2 70  ? -26.133 5.983   -7.219  1.00 28.24  ? 79  TYR   B CG  1 
ATOM   2069 C CD1 . TYR   B 2 70  ? -24.964 5.483   -7.783  1.00 32.22  ? 79  TYR   B CD1 1 
ATOM   2070 C CD2 . TYR   B 2 70  ? -26.006 7.043   -6.341  1.00 33.87  ? 79  TYR   B CD2 1 
ATOM   2071 C CE1 . TYR   B 2 70  ? -23.722 6.016   -7.467  1.00 29.24  ? 79  TYR   B CE1 1 
ATOM   2072 C CE2 . TYR   B 2 70  ? -24.784 7.626   -6.061  1.00 33.31  ? 79  TYR   B CE2 1 
ATOM   2073 C CZ  . TYR   B 2 70  ? -23.626 7.096   -6.612  1.00 27.98  ? 79  TYR   B CZ  1 
ATOM   2074 O OH  . TYR   B 2 70  ? -22.410 7.666   -6.284  1.00 33.10  ? 79  TYR   B OH  1 
ATOM   2075 N N   . CYS   B 2 71  ? -29.996 3.849   -5.763  1.00 32.35  ? 80  CYS   B N   1 
ATOM   2076 C CA  . CYS   B 2 71  ? -31.469 3.689   -5.722  1.00 32.88  ? 80  CYS   B CA  1 
ATOM   2077 C C   . CYS   B 2 71  ? -31.862 2.249   -5.414  1.00 36.25  ? 80  CYS   B C   1 
ATOM   2078 O O   . CYS   B 2 71  ? -33.062 2.009   -5.205  1.00 37.39  ? 80  CYS   B O   1 
ATOM   2079 C CB  . CYS   B 2 71  ? -32.138 4.102   -7.027  1.00 40.02  ? 80  CYS   B CB  1 
ATOM   2080 S SG  . CYS   B 2 71  ? -31.691 5.788   -7.507  1.00 42.93  ? 80  CYS   B SG  1 
ATOM   2081 N N   . GLY   B 2 72  ? -30.916 1.301   -5.410  1.00 32.79  ? 81  GLY   B N   1 
ATOM   2082 C CA  . GLY   B 2 72  ? -31.301 -0.113  -5.304  1.00 32.18  ? 81  GLY   B CA  1 
ATOM   2083 C C   . GLY   B 2 72  ? -30.058 -0.991  -5.318  1.00 27.60  ? 81  GLY   B C   1 
ATOM   2084 O O   . GLY   B 2 72  ? -28.954 -0.504  -5.511  1.00 29.83  ? 81  GLY   B O   1 
ATOM   2085 N N   . PRO   B 2 73  ? -30.196 -2.284  -5.020  1.00 29.21  ? 82  PRO   B N   1 
ATOM   2086 C CA  . PRO   B 2 73  ? -29.046 -3.187  -5.045  1.00 33.62  ? 82  PRO   B CA  1 
ATOM   2087 C C   . PRO   B 2 73  ? -28.475 -3.406  -6.462  1.00 33.57  ? 82  PRO   B C   1 
ATOM   2088 O O   . PRO   B 2 73  ? -29.181 -3.167  -7.385  1.00 32.34  ? 82  PRO   B O   1 
ATOM   2089 C CB  . PRO   B 2 73  ? -29.663 -4.452  -4.458  1.00 31.31  ? 82  PRO   B CB  1 
ATOM   2090 C CG  . PRO   B 2 73  ? -31.099 -4.377  -4.840  1.00 32.50  ? 82  PRO   B CG  1 
ATOM   2091 C CD  . PRO   B 2 73  ? -31.451 -2.938  -4.617  1.00 33.94  ? 82  PRO   B CD  1 
ATOM   2092 N N   . TRP   B 2 74  ? -27.223 -3.852  -6.570  1.00 34.83  ? 83  TRP   B N   1 
ATOM   2093 C CA  . TRP   B 2 74  ? -26.572 -4.207  -7.853  1.00 34.59  ? 83  TRP   B CA  1 
ATOM   2094 C C   . TRP   B 2 74  ? -27.469 -5.171  -8.631  1.00 33.21  ? 83  TRP   B C   1 
ATOM   2095 O O   . TRP   B 2 74  ? -27.868 -6.158  -8.072  1.00 36.07  ? 83  TRP   B O   1 
ATOM   2096 C CB  . TRP   B 2 74  ? -25.171 -4.783  -7.605  1.00 36.76  ? 83  TRP   B CB  1 
ATOM   2097 C CG  . TRP   B 2 74  ? -24.388 -4.951  -8.871  1.00 31.55  ? 83  TRP   B CG  1 
ATOM   2098 C CD1 . TRP   B 2 74  ? -24.351 -6.059  -9.666  1.00 31.18  ? 83  TRP   B CD1 1 
ATOM   2099 C CD2 . TRP   B 2 74  ? -23.511 -3.989  -9.475  1.00 30.45  ? 83  TRP   B CD2 1 
ATOM   2100 N NE1 . TRP   B 2 74  ? -23.511 -5.848  -10.725 1.00 31.34  ? 83  TRP   B NE1 1 
ATOM   2101 C CE2 . TRP   B 2 74  ? -22.999 -4.587  -10.653 1.00 27.67  ? 83  TRP   B CE2 1 
ATOM   2102 C CE3 . TRP   B 2 74  ? -23.163 -2.663  -9.183  1.00 27.37  ? 83  TRP   B CE3 1 
ATOM   2103 C CZ2 . TRP   B 2 74  ? -22.182 -3.901  -11.547 1.00 28.86  ? 83  TRP   B CZ2 1 
ATOM   2104 C CZ3 . TRP   B 2 74  ? -22.327 -2.002  -10.053 1.00 31.36  ? 83  TRP   B CZ3 1 
ATOM   2105 C CH2 . TRP   B 2 74  ? -21.812 -2.634  -11.199 1.00 27.55  ? 83  TRP   B CH2 1 
ATOM   2106 N N   . LYS   B 2 75  ? -27.753 -4.891  -9.910  1.00 33.07  ? 84  LYS   B N   1 
ATOM   2107 C CA  . LYS   B 2 75  ? -28.740 -5.666  -10.712 1.00 32.13  ? 84  LYS   B CA  1 
ATOM   2108 C C   . LYS   B 2 75  ? -28.081 -6.525  -11.816 1.00 33.63  ? 84  LYS   B C   1 
ATOM   2109 O O   . LYS   B 2 75  ? -28.766 -7.428  -12.319 1.00 37.86  ? 84  LYS   B O   1 
ATOM   2110 C CB  . LYS   B 2 75  ? -29.691 -4.690  -11.415 1.00 34.01  ? 84  LYS   B CB  1 
ATOM   2111 C CG  . LYS   B 2 75  ? -30.578 -3.864  -10.493 1.00 37.68  ? 84  LYS   B CG  1 
ATOM   2112 C CD  . LYS   B 2 75  ? -31.653 -4.677  -9.844  1.00 39.79  ? 84  LYS   B CD  1 
ATOM   2113 C CE  . LYS   B 2 75  ? -32.329 -3.926  -8.725  1.00 42.80  ? 84  LYS   B CE  1 
ATOM   2114 N NZ  . LYS   B 2 75  ? -33.688 -4.463  -8.490  1.00 50.12  ? 84  LYS   B NZ  1 
ATOM   2115 N N   . LEU   B 2 76  ? -26.846 -6.249  -12.204 1.00 33.11  ? 85  LEU   B N   1 
ATOM   2116 C CA  . LEU   B 2 76  ? -26.186 -6.857  -13.400 1.00 37.93  ? 85  LEU   B CA  1 
ATOM   2117 C C   . LEU   B 2 76  ? -25.443 -8.146  -13.002 1.00 37.39  ? 85  LEU   B C   1 
ATOM   2118 O O   . LEU   B 2 76  ? -24.490 -8.055  -12.190 1.00 37.99  ? 85  LEU   B O   1 
ATOM   2119 C CB  . LEU   B 2 76  ? -25.219 -5.810  -13.955 1.00 38.94  ? 85  LEU   B CB  1 
ATOM   2120 C CG  . LEU   B 2 76  ? -25.829 -4.410  -14.139 1.00 38.42  ? 85  LEU   B CG  1 
ATOM   2121 C CD1 . LEU   B 2 76  ? -24.821 -3.448  -14.721 1.00 35.31  ? 85  LEU   B CD1 1 
ATOM   2122 C CD2 . LEU   B 2 76  ? -27.077 -4.465  -14.999 1.00 42.15  ? 85  LEU   B CD2 1 
ATOM   2123 N N   . ASP   B 2 77  ? -25.846 -9.296  -13.552 1.00 41.04  ? 86  ASP   B N   1 
ATOM   2124 C CA  . ASP   B 2 77  ? -25.356 -10.631 -13.098 1.00 54.19  ? 86  ASP   B CA  1 
ATOM   2125 C C   . ASP   B 2 77  ? -24.700 -11.410 -14.256 1.00 52.48  ? 86  ASP   B C   1 
ATOM   2126 O O   . ASP   B 2 77  ? -24.226 -12.520 -14.020 1.00 52.34  ? 86  ASP   B O   1 
ATOM   2127 C CB  . ASP   B 2 77  ? -26.471 -11.452 -12.441 1.00 56.63  ? 86  ASP   B CB  1 
ATOM   2128 C CG  . ASP   B 2 77  ? -27.762 -11.402 -13.227 1.00 68.74  ? 86  ASP   B CG  1 
ATOM   2129 O OD1 . ASP   B 2 77  ? -27.753 -10.760 -14.306 1.00 68.30  ? 86  ASP   B OD1 1 
ATOM   2130 O OD2 . ASP   B 2 77  ? -28.769 -11.999 -12.757 1.00 74.36  ? 86  ASP   B OD2 1 
ATOM   2131 N N   . ALA   B 2 78  ? -24.613 -10.849 -15.456 1.00 44.44  ? 87  ALA   B N   1 
ATOM   2132 C CA  . ALA   B 2 78  ? -24.119 -11.597 -16.617 1.00 38.94  ? 87  ALA   B CA  1 
ATOM   2133 C C   . ALA   B 2 78  ? -22.597 -11.650 -16.510 1.00 38.07  ? 87  ALA   B C   1 
ATOM   2134 O O   . ALA   B 2 78  ? -21.975 -10.705 -15.899 1.00 34.35  ? 87  ALA   B O   1 
ATOM   2135 C CB  . ALA   B 2 78  ? -24.616 -10.994 -17.920 1.00 41.93  ? 87  ALA   B CB  1 
ATOM   2136 N N   . ALA   B 2 79  ? -22.018 -12.688 -17.126 1.00 36.76  ? 88  ALA   B N   1 
ATOM   2137 C CA  . ALA   B 2 79  ? -20.596 -13.062 -17.021 1.00 37.24  ? 88  ALA   B CA  1 
ATOM   2138 C C   . ALA   B 2 79  ? -20.028 -13.344 -18.411 1.00 34.22  ? 88  ALA   B C   1 
ATOM   2139 O O   . ALA   B 2 79  ? -20.757 -13.981 -19.203 1.00 36.50  ? 88  ALA   B O   1 
ATOM   2140 C CB  . ALA   B 2 79  ? -20.474 -14.274 -16.119 1.00 41.16  ? 88  ALA   B CB  1 
ATOM   2141 N N   . TRP   B 2 80  ? -18.832 -12.815 -18.719 1.00 33.17  ? 89  TRP   B N   1 
ATOM   2142 C CA  . TRP   B 2 80  ? -17.995 -13.237 -19.879 1.00 41.72  ? 89  TRP   B CA  1 
ATOM   2143 C C   . TRP   B 2 80  ? -17.890 -14.747 -19.851 1.00 46.56  ? 89  TRP   B C   1 
ATOM   2144 O O   . TRP   B 2 80  ? -17.625 -15.249 -18.722 1.00 38.70  ? 89  TRP   B O   1 
ATOM   2145 C CB  . TRP   B 2 80  ? -16.596 -12.640 -19.877 1.00 43.24  ? 89  TRP   B CB  1 
ATOM   2146 C CG  . TRP   B 2 80  ? -15.790 -13.048 -21.072 1.00 50.19  ? 89  TRP   B CG  1 
ATOM   2147 C CD1 . TRP   B 2 80  ? -16.214 -13.134 -22.373 1.00 52.08  ? 89  TRP   B CD1 1 
ATOM   2148 C CD2 . TRP   B 2 80  ? -14.387 -13.379 -21.087 1.00 53.04  ? 89  TRP   B CD2 1 
ATOM   2149 N NE1 . TRP   B 2 80  ? -15.178 -13.501 -23.190 1.00 48.97  ? 89  TRP   B NE1 1 
ATOM   2150 C CE2 . TRP   B 2 80  ? -14.058 -13.708 -22.423 1.00 45.92  ? 89  TRP   B CE2 1 
ATOM   2151 C CE3 . TRP   B 2 80  ? -13.406 -13.519 -20.094 1.00 48.77  ? 89  TRP   B CE3 1 
ATOM   2152 C CZ2 . TRP   B 2 80  ? -12.778 -14.103 -22.790 1.00 43.36  ? 89  TRP   B CZ2 1 
ATOM   2153 C CZ3 . TRP   B 2 80  ? -12.139 -13.926 -20.465 1.00 46.47  ? 89  TRP   B CZ3 1 
ATOM   2154 C CH2 . TRP   B 2 80  ? -11.832 -14.196 -21.799 1.00 46.03  ? 89  TRP   B CH2 1 
ATOM   2155 N N   . ASP   B 2 81  ? -18.189 -15.392 -20.995 1.00 47.52  ? 90  ASP   B N   1 
ATOM   2156 C CA  . ASP   B 2 81  ? -18.319 -16.869 -21.149 1.00 47.59  ? 90  ASP   B CA  1 
ATOM   2157 C C   . ASP   B 2 81  ? -16.921 -17.499 -21.121 1.00 44.83  ? 90  ASP   B C   1 
ATOM   2158 O O   . ASP   B 2 81  ? -16.868 -18.712 -20.914 1.00 50.33  ? 90  ASP   B O   1 
ATOM   2159 C CB  . ASP   B 2 81  ? -19.063 -17.297 -22.431 1.00 43.03  ? 90  ASP   B CB  1 
ATOM   2160 C CG  . ASP   B 2 81  ? -18.393 -16.878 -23.717 1.00 41.43  ? 90  ASP   B CG  1 
ATOM   2161 O OD1 . ASP   B 2 81  ? -17.294 -16.223 -23.674 1.00 50.38  ? 90  ASP   B OD1 1 
ATOM   2162 O OD2 . ASP   B 2 81  ? -18.979 -17.156 -24.771 1.00 51.05  ? 90  ASP   B OD2 1 
ATOM   2163 N N   . GLY   B 2 82  ? -15.869 -16.712 -21.347 1.00 48.89  ? 91  GLY   B N   1 
ATOM   2164 C CA  . GLY   B 2 82  ? -14.454 -17.139 -21.307 1.00 48.45  ? 91  GLY   B CA  1 
ATOM   2165 C C   . GLY   B 2 82  ? -13.876 -17.386 -22.701 1.00 51.29  ? 91  GLY   B C   1 
ATOM   2166 O O   . GLY   B 2 82  ? -12.649 -17.627 -22.797 1.00 48.37  ? 91  GLY   B O   1 
ATOM   2167 N N   . LEU   B 2 83  ? -14.719 -17.308 -23.741 1.00 48.30  ? 92  LEU   B N   1 
ATOM   2168 C CA  . LEU   B 2 83  ? -14.428 -17.712 -25.145 1.00 47.79  ? 92  LEU   B CA  1 
ATOM   2169 C C   . LEU   B 2 83  ? -14.748 -16.591 -26.135 1.00 53.54  ? 92  LEU   B C   1 
ATOM   2170 O O   . LEU   B 2 83  ? -13.897 -16.287 -27.004 1.00 50.66  ? 92  LEU   B O   1 
ATOM   2171 C CB  . LEU   B 2 83  ? -15.308 -18.913 -25.466 1.00 53.99  ? 92  LEU   B CB  1 
ATOM   2172 C CG  . LEU   B 2 83  ? -14.801 -20.249 -24.938 1.00 60.78  ? 92  LEU   B CG  1 
ATOM   2173 C CD1 . LEU   B 2 83  ? -15.824 -21.338 -25.211 1.00 62.46  ? 92  LEU   B CD1 1 
ATOM   2174 C CD2 . LEU   B 2 83  ? -13.450 -20.603 -25.545 1.00 54.62  ? 92  LEU   B CD2 1 
ATOM   2175 N N   . SER   B 2 84  ? -15.960 -16.035 -26.055 1.00 56.89  ? 93  SER   B N   1 
ATOM   2176 C CA  . SER   B 2 84  ? -16.568 -15.216 -27.134 1.00 49.82  ? 93  SER   B CA  1 
ATOM   2177 C C   . SER   B 2 84  ? -16.016 -13.792 -27.098 1.00 50.39  ? 93  SER   B C   1 
ATOM   2178 O O   . SER   B 2 84  ? -15.508 -13.334 -26.036 1.00 51.77  ? 93  SER   B O   1 
ATOM   2179 C CB  . SER   B 2 84  ? -18.041 -15.220 -27.023 1.00 48.23  ? 93  SER   B CB  1 
ATOM   2180 O OG  . SER   B 2 84  ? -18.487 -16.459 -26.508 1.00 49.23  ? 93  SER   B OG  1 
ATOM   2181 N N   A GLU   B 2 85  ? -16.119 -13.095 -28.228 0.22 48.50  ? 94  GLU   B N   1 
ATOM   2182 N N   B GLU   B 2 85  ? -16.119 -13.095 -28.228 0.22 48.50  ? 94  GLU   B N   1 
ATOM   2183 N N   C GLU   B 2 85  ? -16.076 -13.090 -28.236 0.28 46.43  ? 94  GLU   B N   1 
ATOM   2184 N N   D GLU   B 2 85  ? -16.076 -13.090 -28.236 0.28 46.43  ? 94  GLU   B N   1 
ATOM   2185 C CA  A GLU   B 2 85  ? -15.745 -11.662 -28.349 0.22 48.35  ? 94  GLU   B CA  1 
ATOM   2186 C CA  B GLU   B 2 85  ? -15.745 -11.662 -28.349 0.22 48.34  ? 94  GLU   B CA  1 
ATOM   2187 C CA  C GLU   B 2 85  ? -15.689 -11.652 -28.310 0.28 45.30  ? 94  GLU   B CA  1 
ATOM   2188 C CA  D GLU   B 2 85  ? -15.690 -11.652 -28.310 0.28 45.29  ? 94  GLU   B CA  1 
ATOM   2189 C C   A GLU   B 2 85  ? -16.769 -10.838 -27.553 0.22 41.74  ? 94  GLU   B C   1 
ATOM   2190 C C   B GLU   B 2 85  ? -16.769 -10.838 -27.554 0.22 41.75  ? 94  GLU   B C   1 
ATOM   2191 C C   C GLU   B 2 85  ? -16.746 -10.848 -27.533 0.28 39.32  ? 94  GLU   B C   1 
ATOM   2192 C C   D GLU   B 2 85  ? -16.746 -10.848 -27.533 0.28 39.35  ? 94  GLU   B C   1 
ATOM   2193 O O   A GLU   B 2 85  ? -17.875 -11.355 -27.288 0.22 36.73  ? 94  GLU   B O   1 
ATOM   2194 O O   B GLU   B 2 85  ? -17.875 -11.355 -27.288 0.22 36.76  ? 94  GLU   B O   1 
ATOM   2195 O O   C GLU   B 2 85  ? -17.837 -11.385 -27.253 0.28 33.04  ? 94  GLU   B O   1 
ATOM   2196 O O   D GLU   B 2 85  ? -17.837 -11.386 -27.253 0.28 33.09  ? 94  GLU   B O   1 
ATOM   2197 C CB  A GLU   B 2 85  ? -15.651 -11.290 -29.832 0.22 53.01  ? 94  GLU   B CB  1 
ATOM   2198 C CB  B GLU   B 2 85  ? -15.651 -11.290 -29.832 0.22 52.99  ? 94  GLU   B CB  1 
ATOM   2199 C CB  C GLU   B 2 85  ? -15.495 -11.158 -29.755 0.28 48.33  ? 94  GLU   B CB  1 
ATOM   2200 C CB  D GLU   B 2 85  ? -15.496 -11.158 -29.755 0.28 48.31  ? 94  GLU   B CB  1 
ATOM   2201 C CG  A GLU   B 2 85  ? -14.492 -11.982 -30.544 0.22 55.79  ? 94  GLU   B CG  1 
ATOM   2202 C CG  B GLU   B 2 85  ? -14.492 -11.982 -30.544 0.22 55.76  ? 94  GLU   B CG  1 
ATOM   2203 C CG  C GLU   B 2 85  ? -14.075 -11.364 -30.294 0.28 48.67  ? 94  GLU   B CG  1 
ATOM   2204 C CG  D GLU   B 2 85  ? -14.075 -11.364 -30.295 0.28 48.65  ? 94  GLU   B CG  1 
ATOM   2205 C CD  A GLU   B 2 85  ? -14.857 -12.839 -31.747 0.22 56.08  ? 94  GLU   B CD  1 
ATOM   2206 C CD  B GLU   B 2 85  ? -14.858 -12.839 -31.747 0.22 56.07  ? 94  GLU   B CD  1 
ATOM   2207 C CD  C GLU   B 2 85  ? -13.702 -10.670 -31.602 0.28 49.09  ? 94  GLU   B CD  1 
ATOM   2208 C CD  D GLU   B 2 85  ? -13.702 -10.670 -31.601 0.28 49.06  ? 94  GLU   B CD  1 
ATOM   2209 O OE1 A GLU   B 2 85  ? -15.845 -12.512 -32.441 0.22 54.98  ? 94  GLU   B OE1 1 
ATOM   2210 O OE1 B GLU   B 2 85  ? -15.845 -12.511 -32.441 0.22 54.98  ? 94  GLU   B OE1 1 
ATOM   2211 O OE1 C GLU   B 2 85  ? -14.596 -10.096 -32.249 0.28 40.76  ? 94  GLU   B OE1 1 
ATOM   2212 O OE1 D GLU   B 2 85  ? -14.597 -10.096 -32.249 0.28 40.80  ? 94  GLU   B OE1 1 
ATOM   2213 O OE2 A GLU   B 2 85  ? -14.152 -13.840 -31.982 0.22 57.69  ? 94  GLU   B OE2 1 
ATOM   2214 O OE2 B GLU   B 2 85  ? -14.153 -13.840 -31.982 0.22 57.68  ? 94  GLU   B OE2 1 
ATOM   2215 O OE2 C GLU   B 2 85  ? -12.502 -10.703 -31.969 0.28 49.23  ? 94  GLU   B OE2 1 
ATOM   2216 O OE2 D GLU   B 2 85  ? -12.503 -10.702 -31.968 0.28 49.21  ? 94  GLU   B OE2 1 
ATOM   2217 N N   . VAL   B 2 86  ? -16.385 -9.632  -27.130 1.00 39.33  ? 95  VAL   B N   1 
ATOM   2218 C CA  . VAL   B 2 86  ? -17.307 -8.719  -26.396 1.00 39.65  ? 95  VAL   B CA  1 
ATOM   2219 C C   . VAL   B 2 86  ? -17.230 -7.347  -27.060 1.00 38.38  ? 95  VAL   B C   1 
ATOM   2220 O O   . VAL   B 2 86  ? -16.287 -7.111  -27.858 1.00 42.68  ? 95  VAL   B O   1 
ATOM   2221 C CB  . VAL   B 2 86  ? -16.924 -8.628  -24.905 1.00 31.91  ? 95  VAL   B CB  1 
ATOM   2222 C CG1 . VAL   B 2 86  ? -16.729 -9.983  -24.308 1.00 36.55  ? 95  VAL   B CG1 1 
ATOM   2223 C CG2 . VAL   B 2 86  ? -15.668 -7.780  -24.737 1.00 32.18  ? 95  VAL   B CG2 1 
ATOM   2224 N N   A GLN   B 2 87  ? -18.326 -6.608  -26.886 0.22 37.04  ? 96  GLN   B N   1 
ATOM   2225 N N   B GLN   B 2 87  ? -18.326 -6.608  -26.886 0.22 37.03  ? 96  GLN   B N   1 
ATOM   2226 N N   C GLN   B 2 87  ? -18.039 -6.362  -26.617 0.28 36.53  ? 96  GLN   B N   1 
ATOM   2227 N N   D GLN   B 2 87  ? -18.039 -6.362  -26.617 0.28 36.53  ? 96  GLN   B N   1 
ATOM   2228 C CA  A GLN   B 2 87  ? -18.481 -5.205  -27.319 0.22 35.70  ? 96  GLN   B CA  1 
ATOM   2229 C CA  B GLN   B 2 87  ? -18.481 -5.205  -27.319 0.22 35.69  ? 96  GLN   B CA  1 
ATOM   2230 C CA  C GLN   B 2 87  ? -17.926 -4.934  -27.066 0.28 34.49  ? 96  GLN   B CA  1 
ATOM   2231 C CA  D GLN   B 2 87  ? -17.926 -4.934  -27.067 0.28 34.48  ? 96  GLN   B CA  1 
ATOM   2232 C C   A GLN   B 2 87  ? -18.428 -4.360  -26.052 0.22 31.26  ? 96  GLN   B C   1 
ATOM   2233 C C   B GLN   B 2 87  ? -18.428 -4.359  -26.052 0.22 31.27  ? 96  GLN   B C   1 
ATOM   2234 C C   C GLN   B 2 87  ? -17.811 -3.975  -25.867 0.28 30.63  ? 96  GLN   B C   1 
ATOM   2235 C C   D GLN   B 2 87  ? -17.812 -3.975  -25.867 0.28 30.64  ? 96  GLN   B C   1 
ATOM   2236 O O   A GLN   B 2 87  ? -19.262 -4.594  -25.158 0.22 32.03  ? 96  GLN   B O   1 
ATOM   2237 O O   B GLN   B 2 87  ? -19.263 -4.593  -25.158 0.22 32.03  ? 96  GLN   B O   1 
ATOM   2238 O O   C GLN   B 2 87  ? -18.596 -4.114  -24.933 0.28 29.70  ? 96  GLN   B O   1 
ATOM   2239 O O   D GLN   B 2 87  ? -18.597 -4.114  -24.933 0.28 29.71  ? 96  GLN   B O   1 
ATOM   2240 C CB  A GLN   B 2 87  ? -19.765 -5.046  -28.139 0.22 34.26  ? 96  GLN   B CB  1 
ATOM   2241 C CB  B GLN   B 2 87  ? -19.764 -5.045  -28.139 0.22 34.26  ? 96  GLN   B CB  1 
ATOM   2242 C CB  C GLN   B 2 87  ? -19.112 -4.539  -27.968 0.28 34.77  ? 96  GLN   B CB  1 
ATOM   2243 C CB  D GLN   B 2 87  ? -19.113 -4.539  -27.968 0.28 34.76  ? 96  GLN   B CB  1 
ATOM   2244 C CG  A GLN   B 2 87  ? -19.628 -5.657  -29.530 0.22 34.51  ? 96  GLN   B CG  1 
ATOM   2245 C CG  B GLN   B 2 87  ? -19.628 -5.657  -29.530 0.22 34.50  ? 96  GLN   B CG  1 
ATOM   2246 C CG  C GLN   B 2 87  ? -19.017 -5.104  -29.385 0.28 35.15  ? 96  GLN   B CG  1 
ATOM   2247 C CG  D GLN   B 2 87  ? -19.017 -5.104  -29.385 0.28 35.13  ? 96  GLN   B CG  1 
ATOM   2248 C CD  A GLN   B 2 87  ? -20.869 -5.563  -30.383 0.22 32.70  ? 96  GLN   B CD  1 
ATOM   2249 C CD  B GLN   B 2 87  ? -20.869 -5.562  -30.383 0.22 32.70  ? 96  GLN   B CD  1 
ATOM   2250 C CD  C GLN   B 2 87  ? -20.017 -4.566  -30.389 0.28 32.75  ? 96  GLN   B CD  1 
ATOM   2251 C CD  D GLN   B 2 87  ? -20.018 -4.567  -30.389 0.28 32.75  ? 96  GLN   B CD  1 
ATOM   2252 O OE1 A GLN   B 2 87  ? -21.821 -4.858  -30.060 0.22 30.05  ? 96  GLN   B OE1 1 
ATOM   2253 O OE1 B GLN   B 2 87  ? -21.821 -4.858  -30.060 0.22 30.07  ? 96  GLN   B OE1 1 
ATOM   2254 O OE1 C GLN   B 2 87  ? -20.904 -3.775  -30.075 0.28 29.58  ? 96  GLN   B OE1 1 
ATOM   2255 O OE1 D GLN   B 2 87  ? -20.904 -3.776  -30.074 0.28 29.59  ? 96  GLN   B OE1 1 
ATOM   2256 N NE2 A GLN   B 2 87  ? -20.856 -6.270  -31.502 0.22 30.87  ? 96  GLN   B NE2 1 
ATOM   2257 N NE2 B GLN   B 2 87  ? -20.856 -6.270  -31.502 0.22 30.88  ? 96  GLN   B NE2 1 
ATOM   2258 N NE2 C GLN   B 2 87  ? -19.881 -5.006  -31.633 0.28 30.11  ? 96  GLN   B NE2 1 
ATOM   2259 N NE2 D GLN   B 2 87  ? -19.881 -5.007  -31.632 0.28 30.13  ? 96  GLN   B NE2 1 
ATOM   2260 N N   A LEU   B 2 88  ? -17.405 -3.511  -25.970 0.22 28.56  ? 97  LEU   B N   1 
ATOM   2261 N N   B LEU   B 2 88  ? -17.405 -3.510  -25.970 0.22 28.57  ? 97  LEU   B N   1 
ATOM   2262 N N   C LEU   B 2 88  ? -16.858 -3.033  -25.904 0.28 28.79  ? 97  LEU   B N   1 
ATOM   2263 N N   D LEU   B 2 88  ? -16.859 -3.034  -25.904 0.28 28.81  ? 97  LEU   B N   1 
ATOM   2264 C CA  A LEU   B 2 88  ? -17.340 -2.337  -25.076 0.22 27.66  ? 97  LEU   B CA  1 
ATOM   2265 C CA  B LEU   B 2 88  ? -17.340 -2.337  -25.076 0.22 27.67  ? 97  LEU   B CA  1 
ATOM   2266 C CA  C LEU   B 2 88  ? -16.806 -1.844  -25.007 0.28 30.45  ? 97  LEU   B CA  1 
ATOM   2267 C CA  D LEU   B 2 88  ? -16.807 -1.845  -25.007 0.28 30.45  ? 97  LEU   B CA  1 
ATOM   2268 C C   A LEU   B 2 88  ? -18.225 -1.238  -25.675 0.22 27.26  ? 97  LEU   B C   1 
ATOM   2269 C C   B LEU   B 2 88  ? -18.225 -1.238  -25.674 0.22 27.26  ? 97  LEU   B C   1 
ATOM   2270 C C   C LEU   B 2 88  ? -17.718 -0.778  -25.633 0.28 32.13  ? 97  LEU   B C   1 
ATOM   2271 C C   D LEU   B 2 88  ? -17.718 -0.778  -25.633 0.28 32.12  ? 97  LEU   B C   1 
ATOM   2272 O O   A LEU   B 2 88  ? -18.264 -1.135  -26.921 0.22 22.03  ? 97  LEU   B O   1 
ATOM   2273 O O   B LEU   B 2 88  ? -18.264 -1.135  -26.921 0.22 22.05  ? 97  LEU   B O   1 
ATOM   2274 O O   C LEU   B 2 88  ? -17.221 -0.020  -26.507 0.28 27.91  ? 97  LEU   B O   1 
ATOM   2275 O O   D LEU   B 2 88  ? -17.221 -0.020  -26.507 0.28 27.93  ? 97  LEU   B O   1 
ATOM   2276 C CB  A LEU   B 2 88  ? -15.892 -1.843  -24.981 0.22 28.27  ? 97  LEU   B CB  1 
ATOM   2277 C CB  B LEU   B 2 88  ? -15.892 -1.843  -24.981 0.22 28.27  ? 97  LEU   B CB  1 
ATOM   2278 C CB  C LEU   B 2 88  ? -15.362 -1.341  -24.850 0.28 29.19  ? 97  LEU   B CB  1 
ATOM   2279 C CB  D LEU   B 2 88  ? -15.362 -1.342  -24.851 0.28 29.21  ? 97  LEU   B CB  1 
ATOM   2280 C CG  A LEU   B 2 88  ? -15.687 -0.598  -24.124 0.22 29.17  ? 97  LEU   B CG  1 
ATOM   2281 C CG  B LEU   B 2 88  ? -15.687 -0.598  -24.123 0.22 29.18  ? 97  LEU   B CG  1 
ATOM   2282 C CG  C LEU   B 2 88  ? -15.161 -0.040  -24.066 0.28 30.44  ? 97  LEU   B CG  1 
ATOM   2283 C CG  D LEU   B 2 88  ? -15.161 -0.040  -24.066 0.28 30.44  ? 97  LEU   B CG  1 
ATOM   2284 C CD1 A LEU   B 2 88  ? -15.984 -0.889  -22.657 0.22 31.17  ? 97  LEU   B CD1 1 
ATOM   2285 C CD1 B LEU   B 2 88  ? -15.984 -0.889  -22.657 0.22 31.17  ? 97  LEU   B CD1 1 
ATOM   2286 C CD1 C LEU   B 2 88  ? -15.437 -0.226  -22.581 0.28 32.43  ? 97  LEU   B CD1 1 
ATOM   2287 C CD1 D LEU   B 2 88  ? -15.438 -0.227  -22.581 0.28 32.42  ? 97  LEU   B CD1 1 
ATOM   2288 C CD2 A LEU   B 2 88  ? -14.289 -0.033  -24.290 0.22 29.76  ? 97  LEU   B CD2 1 
ATOM   2289 C CD2 B LEU   B 2 88  ? -14.289 -0.032  -24.289 0.22 29.76  ? 97  LEU   B CD2 1 
ATOM   2290 C CD2 C LEU   B 2 88  ? -13.758 0.521   -24.252 0.28 30.83  ? 97  LEU   B CD2 1 
ATOM   2291 C CD2 D LEU   B 2 88  ? -13.758 0.520   -24.253 0.28 30.84  ? 97  LEU   B CD2 1 
ATOM   2292 N N   A LEU   B 2 89  ? -18.846 -0.431  -24.807 0.22 26.10  ? 98  LEU   B N   1 
ATOM   2293 N N   B LEU   B 2 89  ? -18.846 -0.431  -24.807 0.22 26.10  ? 98  LEU   B N   1 
ATOM   2294 N N   C LEU   B 2 89  ? -19.017 -0.800  -25.290 0.28 33.21  ? 98  LEU   B N   1 
ATOM   2295 N N   D LEU   B 2 89  ? -19.017 -0.800  -25.290 0.28 33.19  ? 98  LEU   B N   1 
ATOM   2296 C CA  A LEU   B 2 89  ? -19.602 0.800   -25.166 0.22 24.80  ? 98  LEU   B CA  1 
ATOM   2297 C CA  B LEU   B 2 89  ? -19.602 0.799   -25.166 0.22 24.81  ? 98  LEU   B CA  1 
ATOM   2298 C CA  C LEU   B 2 89  ? -19.945 0.324   -25.595 0.28 30.61  ? 98  LEU   B CA  1 
ATOM   2299 C CA  D LEU   B 2 89  ? -19.945 0.324   -25.595 0.28 30.62  ? 98  LEU   B CA  1 
ATOM   2300 C C   A LEU   B 2 89  ? -18.809 2.006   -24.649 0.22 26.69  ? 98  LEU   B C   1 
ATOM   2301 C C   B LEU   B 2 89  ? -18.810 2.006   -24.649 0.22 26.69  ? 98  LEU   B C   1 
ATOM   2302 C C   C LEU   B 2 89  ? -19.370 1.522   -24.854 0.28 30.66  ? 98  LEU   B C   1 
ATOM   2303 C C   D LEU   B 2 89  ? -19.370 1.522   -24.854 0.28 30.67  ? 98  LEU   B C   1 
ATOM   2304 O O   A LEU   B 2 89  ? -19.183 2.572   -23.571 0.22 25.57  ? 98  LEU   B O   1 
ATOM   2305 O O   B LEU   B 2 89  ? -19.183 2.572   -23.572 0.22 25.58  ? 98  LEU   B O   1 
ATOM   2306 O O   C LEU   B 2 89  ? -19.847 1.809   -23.724 0.28 33.90  ? 98  LEU   B O   1 
ATOM   2307 O O   D LEU   B 2 89  ? -19.847 1.810   -23.725 0.28 33.88  ? 98  LEU   B O   1 
ATOM   2308 C CB  A LEU   B 2 89  ? -20.986 0.706   -24.519 0.22 25.28  ? 98  LEU   B CB  1 
ATOM   2309 C CB  B LEU   B 2 89  ? -20.987 0.706   -24.519 0.22 25.29  ? 98  LEU   B CB  1 
ATOM   2310 C CB  C LEU   B 2 89  ? -21.373 -0.035  -25.164 0.28 31.31  ? 98  LEU   B CB  1 
ATOM   2311 C CB  D LEU   B 2 89  ? -21.373 -0.035  -25.164 0.28 31.31  ? 98  LEU   B CB  1 
ATOM   2312 C CG  A LEU   B 2 89  ? -22.077 1.682   -24.993 0.22 25.64  ? 98  LEU   B CG  1 
ATOM   2313 C CG  B LEU   B 2 89  ? -22.078 1.682   -24.993 0.22 25.64  ? 98  LEU   B CG  1 
ATOM   2314 C CG  C LEU   B 2 89  ? -22.445 1.068   -25.263 0.28 31.98  ? 98  LEU   B CG  1 
ATOM   2315 C CG  D LEU   B 2 89  ? -22.444 1.068   -25.263 0.28 31.98  ? 98  LEU   B CG  1 
ATOM   2316 C CD1 A LEU   B 2 89  ? -21.507 2.838   -25.786 0.22 26.00  ? 98  LEU   B CD1 1 
ATOM   2317 C CD1 B LEU   B 2 89  ? -21.507 2.838   -25.786 0.22 26.00  ? 98  LEU   B CD1 1 
ATOM   2318 C CD1 C LEU   B 2 89  ? -22.280 1.921   -26.511 0.28 32.71  ? 98  LEU   B CD1 1 
ATOM   2319 C CD1 D LEU   B 2 89  ? -22.280 1.920   -26.512 0.28 32.71  ? 98  LEU   B CD1 1 
ATOM   2320 C CD2 A LEU   B 2 89  ? -23.148 0.972   -25.801 0.22 26.49  ? 98  LEU   B CD2 1 
ATOM   2321 C CD2 B LEU   B 2 89  ? -23.148 0.972   -25.801 0.22 26.49  ? 98  LEU   B CD2 1 
ATOM   2322 C CD2 C LEU   B 2 89  ? -23.846 0.460   -25.216 0.28 32.59  ? 98  LEU   B CD2 1 
ATOM   2323 C CD2 D LEU   B 2 89  ? -23.845 0.460   -25.216 0.28 32.59  ? 98  LEU   B CD2 1 
ATOM   2324 N N   A ALA   B 2 90  ? -17.756 2.398   -25.370 0.22 27.16  ? 99  ALA   B N   1 
ATOM   2325 N N   B ALA   B 2 90  ? -17.756 2.398   -25.370 0.22 27.17  ? 99  ALA   B N   1 
ATOM   2326 N N   C ALA   B 2 90  ? -18.319 2.124   -25.425 0.28 30.52  ? 99  ALA   B N   1 
ATOM   2327 N N   D ALA   B 2 90  ? -18.319 2.124   -25.425 0.28 30.54  ? 99  ALA   B N   1 
ATOM   2328 C CA  A ALA   B 2 90  ? -16.963 3.605   -25.055 0.22 29.47  ? 99  ALA   B CA  1 
ATOM   2329 C CA  B ALA   B 2 90  ? -16.964 3.604   -25.055 0.22 29.48  ? 99  ALA   B CA  1 
ATOM   2330 C CA  C ALA   B 2 90  ? -17.552 3.238   -24.820 0.28 31.06  ? 99  ALA   B CA  1 
ATOM   2331 C CA  D ALA   B 2 90  ? -17.552 3.238   -24.820 0.28 31.08  ? 99  ALA   B CA  1 
ATOM   2332 C C   A ALA   B 2 90  ? -17.888 4.820   -25.149 0.22 33.03  ? 99  ALA   B C   1 
ATOM   2333 C C   B ALA   B 2 90  ? -17.888 4.819   -25.149 0.22 33.03  ? 99  ALA   B C   1 
ATOM   2334 C C   C ALA   B 2 90  ? -18.355 4.534   -24.957 0.28 34.63  ? 99  ALA   B C   1 
ATOM   2335 C C   D ALA   B 2 90  ? -18.355 4.534   -24.957 0.28 34.62  ? 99  ALA   B C   1 
ATOM   2336 O O   A ALA   B 2 90  ? -18.333 5.150   -26.279 0.22 30.39  ? 99  ALA   B O   1 
ATOM   2337 O O   B ALA   B 2 90  ? -18.333 5.150   -26.279 0.22 30.40  ? 99  ALA   B O   1 
ATOM   2338 O O   C ALA   B 2 90  ? -19.172 4.608   -25.925 0.28 32.19  ? 99  ALA   B O   1 
ATOM   2339 O O   D ALA   B 2 90  ? -19.172 4.609   -25.925 0.28 32.20  ? 99  ALA   B O   1 
ATOM   2340 C CB  A ALA   B 2 90  ? -15.787 3.755   -25.984 0.22 31.56  ? 99  ALA   B CB  1 
ATOM   2341 C CB  B ALA   B 2 90  ? -15.787 3.754   -25.984 0.22 31.55  ? 99  ALA   B CB  1 
ATOM   2342 C CB  C ALA   B 2 90  ? -16.208 3.388   -25.472 0.28 32.16  ? 99  ALA   B CB  1 
ATOM   2343 C CB  D ALA   B 2 90  ? -16.207 3.388   -25.473 0.28 32.16  ? 99  ALA   B CB  1 
ATOM   2344 N N   . VAL   B 2 91  ? -18.145 5.468   -24.011 1.00 37.33  ? 100 VAL   B N   1 
ATOM   2345 C CA  . VAL   B 2 91  ? -18.784 6.811   -24.002 1.00 34.08  ? 100 VAL   B CA  1 
ATOM   2346 C C   . VAL   B 2 91  ? -17.698 7.797   -23.613 1.00 36.34  ? 100 VAL   B C   1 
ATOM   2347 O O   . VAL   B 2 91  ? -17.533 8.147   -22.448 1.00 37.14  ? 100 VAL   B O   1 
ATOM   2348 C CB  . VAL   B 2 91  ? -19.999 6.850   -23.081 1.00 38.27  ? 100 VAL   B CB  1 
ATOM   2349 C CG1 . VAL   B 2 91  ? -20.620 8.247   -23.070 1.00 40.61  ? 100 VAL   B CG1 1 
ATOM   2350 C CG2 . VAL   B 2 91  ? -21.029 5.797   -23.468 1.00 35.69  ? 100 VAL   B CG2 1 
ATOM   2351 N N   . PRO   B 2 92  ? -16.869 8.265   -24.570 1.00 35.62  ? 101 PRO   B N   1 
ATOM   2352 C CA  . PRO   B 2 92  ? -15.773 9.157   -24.224 1.00 35.75  ? 101 PRO   B CA  1 
ATOM   2353 C C   . PRO   B 2 92  ? -16.253 10.583  -24.010 1.00 37.81  ? 101 PRO   B C   1 
ATOM   2354 O O   . PRO   B 2 92  ? -17.308 10.948  -24.526 1.00 41.39  ? 101 PRO   B O   1 
ATOM   2355 C CB  . PRO   B 2 92  ? -14.817 9.071   -25.427 1.00 37.18  ? 101 PRO   B CB  1 
ATOM   2356 C CG  . PRO   B 2 92  ? -15.369 7.979   -26.303 1.00 35.68  ? 101 PRO   B CG  1 
ATOM   2357 C CD  . PRO   B 2 92  ? -16.840 7.886   -25.986 1.00 39.76  ? 101 PRO   B CD  1 
ATOM   2358 N N   A PRO   B 2 93  ? -15.519 11.419  -23.245 0.22 37.54  ? 102 PRO   B N   1 
ATOM   2359 N N   B PRO   B 2 93  ? -15.519 11.419  -23.245 0.22 37.55  ? 102 PRO   B N   1 
ATOM   2360 N N   C PRO   B 2 93  ? -15.475 11.427  -23.288 0.28 39.25  ? 102 PRO   B N   1 
ATOM   2361 N N   D PRO   B 2 93  ? -15.475 11.427  -23.288 0.28 39.26  ? 102 PRO   B N   1 
ATOM   2362 C CA  A PRO   B 2 93  ? -15.894 12.820  -23.087 0.22 38.11  ? 102 PRO   B CA  1 
ATOM   2363 C CA  B PRO   B 2 93  ? -15.894 12.820  -23.087 0.22 38.11  ? 102 PRO   B CA  1 
ATOM   2364 C CA  C PRO   B 2 93  ? -15.880 12.796  -22.962 0.28 41.70  ? 102 PRO   B CA  1 
ATOM   2365 C CA  D PRO   B 2 93  ? -15.880 12.796  -22.962 0.28 41.71  ? 102 PRO   B CA  1 
ATOM   2366 C C   A PRO   B 2 93  ? -16.152 13.469  -24.458 0.22 38.01  ? 102 PRO   B C   1 
ATOM   2367 C C   B PRO   B 2 93  ? -16.152 13.469  -24.458 0.22 38.01  ? 102 PRO   B C   1 
ATOM   2368 C C   C PRO   B 2 93  ? -15.896 13.767  -24.158 0.28 44.87  ? 102 PRO   B C   1 
ATOM   2369 C C   D PRO   B 2 93  ? -15.896 13.767  -24.158 0.28 44.86  ? 102 PRO   B C   1 
ATOM   2370 O O   A PRO   B 2 93  ? -15.488 13.102  -25.420 0.22 35.01  ? 102 PRO   B O   1 
ATOM   2371 O O   B PRO   B 2 93  ? -15.488 13.103  -25.420 0.22 35.03  ? 102 PRO   B O   1 
ATOM   2372 O O   C PRO   B 2 93  ? -14.832 14.145  -24.660 0.28 46.15  ? 102 PRO   B O   1 
ATOM   2373 O O   D PRO   B 2 93  ? -14.832 14.145  -24.660 0.28 46.14  ? 102 PRO   B O   1 
ATOM   2374 C CB  A PRO   B 2 93  ? -14.692 13.421  -22.346 0.22 38.12  ? 102 PRO   B CB  1 
ATOM   2375 C CB  B PRO   B 2 93  ? -14.692 13.421  -22.346 0.22 38.13  ? 102 PRO   B CB  1 
ATOM   2376 C CB  C PRO   B 2 93  ? -14.843 13.247  -21.917 0.28 41.20  ? 102 PRO   B CB  1 
ATOM   2377 C CB  D PRO   B 2 93  ? -14.843 13.248  -21.917 0.28 41.20  ? 102 PRO   B CB  1 
ATOM   2378 C CG  A PRO   B 2 93  ? -14.142 12.254  -21.547 0.22 39.98  ? 102 PRO   B CG  1 
ATOM   2379 C CG  B PRO   B 2 93  ? -14.142 12.254  -21.547 0.22 39.97  ? 102 PRO   B CG  1 
ATOM   2380 C CG  C PRO   B 2 93  ? -14.201 11.960  -21.433 0.28 42.25  ? 102 PRO   B CG  1 
ATOM   2381 C CG  D PRO   B 2 93  ? -14.201 11.961  -21.433 0.28 42.24  ? 102 PRO   B CG  1 
ATOM   2382 C CD  A PRO   B 2 93  ? -14.333 11.056  -22.454 0.22 38.53  ? 102 PRO   B CD  1 
ATOM   2383 C CD  B PRO   B 2 93  ? -14.333 11.056  -22.454 0.22 38.53  ? 102 PRO   B CD  1 
ATOM   2384 C CD  C PRO   B 2 93  ? -14.192 11.078  -22.660 0.28 40.80  ? 102 PRO   B CD  1 
ATOM   2385 C CD  D PRO   B 2 93  ? -14.192 11.078  -22.660 0.28 40.80  ? 102 PRO   B CD  1 
ATOM   2386 N N   A GLY   B 2 94  ? -17.157 14.347  -24.520 0.22 39.13  ? 103 GLY   B N   1 
ATOM   2387 N N   B GLY   B 2 94  ? -17.158 14.347  -24.520 0.22 39.13  ? 103 GLY   B N   1 
ATOM   2388 N N   C GLY   B 2 94  ? -17.103 14.165  -24.571 0.28 46.59  ? 103 GLY   B N   1 
ATOM   2389 N N   D GLY   B 2 94  ? -17.103 14.165  -24.571 0.28 46.58  ? 103 GLY   B N   1 
ATOM   2390 C CA  A GLY   B 2 94  ? -17.507 15.184  -25.686 0.22 39.82  ? 103 GLY   B CA  1 
ATOM   2391 C CA  B GLY   B 2 94  ? -17.507 15.184  -25.686 0.22 39.81  ? 103 GLY   B CA  1 
ATOM   2392 C CA  C GLY   B 2 94  ? -17.352 15.088  -25.695 0.28 47.40  ? 103 GLY   B CA  1 
ATOM   2393 C CA  D GLY   B 2 94  ? -17.353 15.088  -25.695 0.28 47.39  ? 103 GLY   B CA  1 
ATOM   2394 C C   A GLY   B 2 94  ? -17.669 14.409  -26.988 0.22 39.79  ? 103 GLY   B C   1 
ATOM   2395 C C   B GLY   B 2 94  ? -17.669 14.409  -26.988 0.22 39.79  ? 103 GLY   B C   1 
ATOM   2396 C C   C GLY   B 2 94  ? -17.727 14.354  -26.973 0.28 47.34  ? 103 GLY   B C   1 
ATOM   2397 C C   D GLY   B 2 94  ? -17.729 14.354  -26.972 0.28 47.34  ? 103 GLY   B C   1 
ATOM   2398 O O   A GLY   B 2 94  ? -17.624 15.063  -28.049 0.22 45.66  ? 103 GLY   B O   1 
ATOM   2399 O O   B GLY   B 2 94  ? -17.623 15.063  -28.049 0.22 45.63  ? 103 GLY   B O   1 
ATOM   2400 O O   C GLY   B 2 94  ? -18.043 15.039  -27.965 0.28 55.06  ? 103 GLY   B O   1 
ATOM   2401 O O   D GLY   B 2 94  ? -18.048 15.039  -27.964 0.28 55.01  ? 103 GLY   B O   1 
ATOM   2402 N N   A GLU   B 2 95  ? -17.886 13.090  -26.936 0.22 37.50  ? 104 GLU   B N   1 
ATOM   2403 N N   B GLU   B 2 95  ? -17.885 13.090  -26.937 0.22 37.51  ? 104 GLU   B N   1 
ATOM   2404 N N   C GLU   B 2 95  ? -17.724 13.017  -26.953 0.28 45.04  ? 104 GLU   B N   1 
ATOM   2405 N N   D GLU   B 2 95  ? -17.723 13.017  -26.953 0.28 45.05  ? 104 GLU   B N   1 
ATOM   2406 C CA  A GLU   B 2 95  ? -17.887 12.198  -28.130 0.22 37.24  ? 104 GLU   B CA  1 
ATOM   2407 C CA  B GLU   B 2 95  ? -17.887 12.198  -28.130 0.22 37.25  ? 104 GLU   B CA  1 
ATOM   2408 C CA  C GLU   B 2 95  ? -17.894 12.160  -28.156 0.28 44.90  ? 104 GLU   B CA  1 
ATOM   2409 C CA  D GLU   B 2 95  ? -17.894 12.160  -28.157 0.28 44.91  ? 104 GLU   B CA  1 
ATOM   2410 C C   A GLU   B 2 95  ? -19.065 11.218  -28.004 0.22 39.05  ? 104 GLU   B C   1 
ATOM   2411 C C   B GLU   B 2 95  ? -19.065 11.218  -28.004 0.22 39.06  ? 104 GLU   B C   1 
ATOM   2412 C C   C GLU   B 2 95  ? -19.140 11.292  -28.004 0.28 43.66  ? 104 GLU   B C   1 
ATOM   2413 C C   D GLU   B 2 95  ? -19.140 11.292  -28.004 0.28 43.67  ? 104 GLU   B C   1 
ATOM   2414 O O   A GLU   B 2 95  ? -19.423 10.869  -26.862 0.22 41.46  ? 104 GLU   B O   1 
ATOM   2415 O O   B GLU   B 2 95  ? -19.423 10.869  -26.862 0.22 41.45  ? 104 GLU   B O   1 
ATOM   2416 O O   C GLU   B 2 95  ? -19.589 11.075  -26.860 0.28 47.12  ? 104 GLU   B O   1 
ATOM   2417 O O   D GLU   B 2 95  ? -19.589 11.075  -26.860 0.28 47.10  ? 104 GLU   B O   1 
ATOM   2418 C CB  A GLU   B 2 95  ? -16.526 11.490  -28.266 0.22 36.82  ? 104 GLU   B CB  1 
ATOM   2419 C CB  B GLU   B 2 95  ? -16.526 11.490  -28.266 0.22 36.82  ? 104 GLU   B CB  1 
ATOM   2420 C CB  C GLU   B 2 95  ? -16.685 11.243  -28.368 0.28 47.86  ? 104 GLU   B CB  1 
ATOM   2421 C CB  D GLU   B 2 95  ? -16.685 11.243  -28.368 0.28 47.86  ? 104 GLU   B CB  1 
ATOM   2422 C CG  A GLU   B 2 95  ? -15.319 12.428  -28.428 0.22 35.25  ? 104 GLU   B CG  1 
ATOM   2423 C CG  B GLU   B 2 95  ? -15.319 12.428  -28.428 0.22 35.26  ? 104 GLU   B CG  1 
ATOM   2424 C CG  C GLU   B 2 95  ? -15.507 11.923  -29.039 0.28 50.56  ? 104 GLU   B CG  1 
ATOM   2425 C CG  D GLU   B 2 95  ? -15.507 11.923  -29.039 0.28 50.54  ? 104 GLU   B CG  1 
ATOM   2426 C CD  A GLU   B 2 95  ? -13.938 11.768  -28.403 0.22 35.65  ? 104 GLU   B CD  1 
ATOM   2427 C CD  B GLU   B 2 95  ? -13.938 11.768  -28.404 0.22 35.65  ? 104 GLU   B CD  1 
ATOM   2428 C CD  C GLU   B 2 95  ? -14.391 10.983  -29.471 0.28 52.36  ? 104 GLU   B CD  1 
ATOM   2429 C CD  D GLU   B 2 95  ? -14.391 10.983  -29.471 0.28 52.34  ? 104 GLU   B CD  1 
ATOM   2430 O OE1 A GLU   B 2 95  ? -13.882 10.539  -28.213 0.22 34.36  ? 104 GLU   B OE1 1 
ATOM   2431 O OE1 B GLU   B 2 95  ? -13.882 10.539  -28.213 0.22 34.37  ? 104 GLU   B OE1 1 
ATOM   2432 O OE1 C GLU   B 2 95  ? -14.701 9.836   -29.890 0.28 54.91  ? 104 GLU   B OE1 1 
ATOM   2433 O OE1 D GLU   B 2 95  ? -14.701 9.835   -29.886 0.28 54.88  ? 104 GLU   B OE1 1 
ATOM   2434 O OE2 A GLU   B 2 95  ? -12.906 12.484  -28.578 0.22 31.34  ? 104 GLU   B OE2 1 
ATOM   2435 O OE2 B GLU   B 2 95  ? -12.906 12.484  -28.578 0.22 31.36  ? 104 GLU   B OE2 1 
ATOM   2436 O OE2 C GLU   B 2 95  ? -13.210 11.398  -29.385 0.28 51.29  ? 104 GLU   B OE2 1 
ATOM   2437 O OE2 D GLU   B 2 95  ? -13.210 11.399  -29.388 0.28 51.29  ? 104 GLU   B OE2 1 
ATOM   2438 N N   . ARG   B 2 96  ? -19.664 10.799  -29.123 1.00 40.01  ? 105 ARG   B N   1 
ATOM   2439 C CA  . ARG   B 2 96  ? -20.875 9.939   -29.105 1.00 42.67  ? 105 ARG   B CA  1 
ATOM   2440 C C   . ARG   B 2 96  ? -20.496 8.554   -28.600 1.00 49.04  ? 105 ARG   B C   1 
ATOM   2441 O O   . ARG   B 2 96  ? -19.305 8.155   -28.773 1.00 48.32  ? 105 ARG   B O   1 
ATOM   2442 C CB  . ARG   B 2 96  ? -21.503 9.864   -30.497 1.00 52.93  ? 105 ARG   B CB  1 
ATOM   2443 C CG  . ARG   B 2 96  ? -22.824 9.117   -30.515 1.00 57.79  ? 105 ARG   B CG  1 
ATOM   2444 C CD  . ARG   B 2 96  ? -23.767 9.559   -31.612 1.00 68.68  ? 105 ARG   B CD  1 
ATOM   2445 N NE  . ARG   B 2 96  ? -23.173 9.418   -32.927 1.00 68.56  ? 105 ARG   B NE  1 
ATOM   2446 C CZ  . ARG   B 2 96  ? -22.555 10.381  -33.595 1.00 79.83  ? 105 ARG   B CZ  1 
ATOM   2447 N NH1 . ARG   B 2 96  ? -22.454 11.602  -33.098 1.00 81.38  ? 105 ARG   B NH1 1 
ATOM   2448 N NH2 . ARG   B 2 96  ? -22.037 10.112  -34.782 1.00 96.16  ? 105 ARG   B NH2 1 
ATOM   2449 N N   . ALA   B 2 97  ? -21.468 7.851   -28.015 1.00 52.92  ? 106 ALA   B N   1 
ATOM   2450 C CA  . ALA   B 2 97  ? -21.361 6.414   -27.685 1.00 47.80  ? 106 ALA   B CA  1 
ATOM   2451 C C   . ALA   B 2 97  ? -20.841 5.691   -28.932 1.00 53.19  ? 106 ALA   B C   1 
ATOM   2452 O O   . ALA   B 2 97  ? -21.285 6.039   -30.020 1.00 49.67  ? 106 ALA   B O   1 
ATOM   2453 C CB  . ALA   B 2 97  ? -22.684 5.870   -27.242 1.00 43.40  ? 106 ALA   B CB  1 
ATOM   2454 N N   . LYS   B 2 98  ? -19.936 4.726   -28.766 1.00 47.97  ? 107 LYS   B N   1 
ATOM   2455 C CA  . LYS   B 2 98  ? -19.280 3.975   -29.869 1.00 51.05  ? 107 LYS   B CA  1 
ATOM   2456 C C   . LYS   B 2 98  ? -18.944 2.568   -29.370 1.00 51.88  ? 107 LYS   B C   1 
ATOM   2457 O O   . LYS   B 2 98  ? -18.211 2.495   -28.367 1.00 47.65  ? 107 LYS   B O   1 
ATOM   2458 C CB  . LYS   B 2 98  ? -18.006 4.733   -30.256 1.00 59.83  ? 107 LYS   B CB  1 
ATOM   2459 C CG  . LYS   B 2 98  ? -16.999 3.964   -31.103 1.00 73.13  ? 107 LYS   B CG  1 
ATOM   2460 C CD  . LYS   B 2 98  ? -15.726 4.743   -31.411 1.00 78.56  ? 107 LYS   B CD  1 
ATOM   2461 C CE  . LYS   B 2 98  ? -15.069 5.314   -30.172 1.00 80.26  ? 107 LYS   B CE  1 
ATOM   2462 N NZ  . LYS   B 2 98  ? -13.655 5.679   -30.421 1.00 94.16  ? 107 LYS   B NZ  1 
ATOM   2463 N N   . ASN   B 2 99  ? -19.477 1.524   -30.011 1.00 45.87  ? 108 ASN   B N   1 
ATOM   2464 C CA  . ASN   B 2 99  ? -19.108 0.110   -29.754 1.00 50.63  ? 108 ASN   B CA  1 
ATOM   2465 C C   . ASN   B 2 99  ? -17.704 -0.169  -30.318 1.00 55.58  ? 108 ASN   B C   1 
ATOM   2466 O O   . ASN   B 2 99  ? -17.414 0.217   -31.489 1.00 51.92  ? 108 ASN   B O   1 
ATOM   2467 C CB  . ASN   B 2 99  ? -20.158 -0.891  -30.257 1.00 43.99  ? 108 ASN   B CB  1 
ATOM   2468 C CG  . ASN   B 2 99  ? -21.547 -0.580  -29.748 1.00 50.03  ? 108 ASN   B CG  1 
ATOM   2469 O OD1 . ASN   B 2 99  ? -21.932 0.580   -29.764 1.00 59.50  ? 108 ASN   B OD1 1 
ATOM   2470 N ND2 . ASN   B 2 99  ? -22.320 -1.569  -29.316 1.00 48.14  ? 108 ASN   B ND2 1 
ATOM   2471 N N   . ILE   B 2 100 ? -16.858 -0.834  -29.522 1.00 46.84  ? 109 ILE   B N   1 
ATOM   2472 C CA  . ILE   B 2 100 ? -15.505 -1.295  -29.925 1.00 44.83  ? 109 ILE   B CA  1 
ATOM   2473 C C   . ILE   B 2 100 ? -15.432 -2.774  -29.600 1.00 48.13  ? 109 ILE   B C   1 
ATOM   2474 O O   . ILE   B 2 100 ? -15.457 -3.123  -28.384 1.00 46.31  ? 109 ILE   B O   1 
ATOM   2475 C CB  . ILE   B 2 100 ? -14.416 -0.495  -29.202 1.00 54.12  ? 109 ILE   B CB  1 
ATOM   2476 C CG1 . ILE   B 2 100 ? -14.678 1.007   -29.257 1.00 57.20  ? 109 ILE   B CG1 1 
ATOM   2477 C CG2 . ILE   B 2 100 ? -13.035 -0.855  -29.736 1.00 55.45  ? 109 ILE   B CG2 1 
ATOM   2478 C CD1 . ILE   B 2 100 ? -14.451 1.618   -30.612 1.00 61.06  ? 109 ILE   B CD1 1 
ATOM   2479 N N   . GLN   B 2 101 ? -15.423 -3.639  -30.607 1.00 50.92  ? 110 GLN   B N   1 
ATOM   2480 C CA  . GLN   B 2 101 ? -15.488 -5.114  -30.393 1.00 47.99  ? 110 GLN   B CA  1 
ATOM   2481 C C   . GLN   B 2 101 ? -14.070 -5.641  -30.164 1.00 47.28  ? 110 GLN   B C   1 
ATOM   2482 O O   . GLN   B 2 101 ? -13.138 -5.121  -30.798 1.00 47.65  ? 110 GLN   B O   1 
ATOM   2483 C CB  . GLN   B 2 101 ? -16.135 -5.821  -31.567 1.00 54.06  ? 110 GLN   B CB  1 
ATOM   2484 C CG  . GLN   B 2 101 ? -16.119 -7.329  -31.428 1.00 52.24  ? 110 GLN   B CG  1 
ATOM   2485 C CD  . GLN   B 2 101 ? -17.205 -7.924  -32.286 1.00 55.94  ? 110 GLN   B CD  1 
ATOM   2486 O OE1 . GLN   B 2 101 ? -18.232 -7.301  -32.524 1.00 53.58  ? 110 GLN   B OE1 1 
ATOM   2487 N NE2 . GLN   B 2 101 ? -16.975 -9.114  -32.800 1.00 51.61  ? 110 GLN   B NE2 1 
ATOM   2488 N N   A THR   B 2 102 ? -13.856 -6.548  -29.208 0.22 43.46  ? 111 THR   B N   1 
ATOM   2489 N N   B THR   B 2 102 ? -13.857 -6.549  -29.209 0.22 43.45  ? 111 THR   B N   1 
ATOM   2490 N N   C THR   B 2 102 ? -13.960 -6.684  -29.315 0.28 46.25  ? 111 THR   B N   1 
ATOM   2491 N N   D THR   B 2 102 ? -13.959 -6.684  -29.315 0.28 46.24  ? 111 THR   B N   1 
ATOM   2492 C CA  A THR   B 2 102 ? -12.482 -6.955  -28.806 0.22 39.55  ? 111 THR   B CA  1 
ATOM   2493 C CA  B THR   B 2 102 ? -12.482 -6.957  -28.808 0.22 39.56  ? 111 THR   B CA  1 
ATOM   2494 C CA  C THR   B 2 102 ? -12.703 -7.408  -28.968 0.28 43.61  ? 111 THR   B CA  1 
ATOM   2495 C CA  D THR   B 2 102 ? -12.702 -7.408  -28.968 0.28 43.62  ? 111 THR   B CA  1 
ATOM   2496 C C   A THR   B 2 102 ? -12.538 -8.283  -28.061 0.22 37.79  ? 111 THR   B C   1 
ATOM   2497 C C   B THR   B 2 102 ? -12.538 -8.284  -28.062 0.22 37.80  ? 111 THR   B C   1 
ATOM   2498 C C   C THR   B 2 102 ? -13.003 -8.795  -28.372 0.28 42.65  ? 111 THR   B C   1 
ATOM   2499 C C   D THR   B 2 102 ? -13.003 -8.795  -28.372 0.28 42.65  ? 111 THR   B C   1 
ATOM   2500 O O   A THR   B 2 102 ? -13.554 -8.516  -27.386 0.22 41.18  ? 111 THR   B O   1 
ATOM   2501 O O   B THR   B 2 102 ? -13.554 -8.516  -27.385 0.22 41.17  ? 111 THR   B O   1 
ATOM   2502 O O   C THR   B 2 102 ? -14.171 -9.045  -28.020 0.28 45.62  ? 111 THR   B O   1 
ATOM   2503 O O   D THR   B 2 102 ? -14.171 -9.045  -28.020 0.28 45.59  ? 111 THR   B O   1 
ATOM   2504 C CB  A THR   B 2 102 ? -11.804 -5.854  -27.978 0.22 39.10  ? 111 THR   B CB  1 
ATOM   2505 C CB  B THR   B 2 102 ? -11.804 -5.856  -27.981 0.22 39.10  ? 111 THR   B CB  1 
ATOM   2506 C CB  C THR   B 2 102 ? -11.845 -6.577  -28.009 0.28 42.66  ? 111 THR   B CB  1 
ATOM   2507 C CB  D THR   B 2 102 ? -11.846 -6.578  -28.008 0.28 42.67  ? 111 THR   B CB  1 
ATOM   2508 O OG1 A THR   B 2 102 ? -10.403 -6.121  -27.909 0.22 37.05  ? 111 THR   B OG1 1 
ATOM   2509 O OG1 B THR   B 2 102 ? -10.403 -6.122  -27.910 0.22 37.06  ? 111 THR   B OG1 1 
ATOM   2510 O OG1 C THR   B 2 102 ? -10.661 -7.342  -27.795 0.28 43.35  ? 111 THR   B OG1 1 
ATOM   2511 O OG1 D THR   B 2 102 ? -10.660 -7.342  -27.795 0.28 43.36  ? 111 THR   B OG1 1 
ATOM   2512 C CG2 A THR   B 2 102 ? -12.381 -5.711  -26.585 0.22 39.76  ? 111 THR   B CG2 1 
ATOM   2513 C CG2 B THR   B 2 102 ? -12.383 -5.714  -26.588 0.22 39.75  ? 111 THR   B CG2 1 
ATOM   2514 C CG2 C THR   B 2 102 ? -12.538 -6.258  -26.700 0.28 45.42  ? 111 THR   B CG2 1 
ATOM   2515 C CG2 D THR   B 2 102 ? -12.539 -6.261  -26.700 0.28 45.41  ? 111 THR   B CG2 1 
ATOM   2516 N N   A LEU   B 2 103 ? -11.495 -9.112  -28.209 0.22 36.30  ? 112 LEU   B N   1 
ATOM   2517 N N   B LEU   B 2 103 ? -11.496 -9.112  -28.209 0.22 36.31  ? 112 LEU   B N   1 
ATOM   2518 N N   C LEU   B 2 103 ? -11.989 -9.675  -28.304 0.28 40.38  ? 112 LEU   B N   1 
ATOM   2519 N N   D LEU   B 2 103 ? -11.988 -9.675  -28.305 0.28 40.38  ? 112 LEU   B N   1 
ATOM   2520 C CA  A LEU   B 2 103 ? -11.301 -10.346 -27.401 0.22 36.71  ? 112 LEU   B CA  1 
ATOM   2521 C CA  B LEU   B 2 103 ? -11.301 -10.346 -27.400 0.22 36.71  ? 112 LEU   B CA  1 
ATOM   2522 C CA  C LEU   B 2 103 ? -11.989 -10.944 -27.509 0.28 36.25  ? 112 LEU   B CA  1 
ATOM   2523 C CA  D LEU   B 2 103 ? -11.988 -10.944 -27.509 0.28 36.27  ? 112 LEU   B CA  1 
ATOM   2524 C C   A LEU   B 2 103 ? -10.510 -9.957  -26.155 0.22 35.17  ? 112 LEU   B C   1 
ATOM   2525 C C   B LEU   B 2 103 ? -10.510 -9.957  -26.154 0.22 35.17  ? 112 LEU   B C   1 
ATOM   2526 C C   C LEU   B 2 103 ? -11.200 -10.687 -26.227 0.28 34.29  ? 112 LEU   B C   1 
ATOM   2527 C C   D LEU   B 2 103 ? -11.200 -10.687 -26.227 0.28 34.32  ? 112 LEU   B C   1 
ATOM   2528 O O   A LEU   B 2 103 ? -9.348  -9.545  -26.254 0.22 34.18  ? 112 LEU   B O   1 
ATOM   2529 O O   B LEU   B 2 103 ? -9.348  -9.546  -26.253 0.22 34.18  ? 112 LEU   B O   1 
ATOM   2530 O O   C LEU   B 2 103 ? -10.057 -10.246 -26.292 0.28 36.43  ? 112 LEU   B O   1 
ATOM   2531 O O   D LEU   B 2 103 ? -10.057 -10.246 -26.292 0.28 36.43  ? 112 LEU   B O   1 
ATOM   2532 C CB  A LEU   B 2 103 ? -10.576 -11.427 -28.213 0.22 36.75  ? 112 LEU   B CB  1 
ATOM   2533 C CB  B LEU   B 2 103 ? -10.577 -11.427 -28.212 0.22 36.75  ? 112 LEU   B CB  1 
ATOM   2534 C CB  C LEU   B 2 103 ? -11.337 -12.095 -28.293 0.28 34.82  ? 112 LEU   B CB  1 
ATOM   2535 C CB  D LEU   B 2 103 ? -11.336 -12.094 -28.293 0.28 34.84  ? 112 LEU   B CB  1 
ATOM   2536 C CG  A LEU   B 2 103 ? -10.584 -12.813 -27.567 0.22 36.72  ? 112 LEU   B CG  1 
ATOM   2537 C CG  B LEU   B 2 103 ? -10.584 -12.813 -27.567 0.22 36.73  ? 112 LEU   B CG  1 
ATOM   2538 C CG  C LEU   B 2 103 ? -10.999 -13.335 -27.461 0.28 35.13  ? 112 LEU   B CG  1 
ATOM   2539 C CG  D LEU   B 2 103 ? -10.998 -13.335 -27.462 0.28 35.14  ? 112 LEU   B CG  1 
ATOM   2540 C CD1 A LEU   B 2 103 ? -11.885 -13.546 -27.867 0.22 36.16  ? 112 LEU   B CD1 1 
ATOM   2541 C CD1 B LEU   B 2 103 ? -11.885 -13.546 -27.867 0.22 36.17  ? 112 LEU   B CD1 1 
ATOM   2542 C CD1 C LEU   B 2 103 ? -12.246 -14.136 -27.155 0.28 34.57  ? 112 LEU   B CD1 1 
ATOM   2543 C CD1 D LEU   B 2 103 ? -12.246 -14.135 -27.156 0.28 34.58  ? 112 LEU   B CD1 1 
ATOM   2544 C CD2 A LEU   B 2 103 ? -9.372  -13.631 -28.001 0.22 38.93  ? 112 LEU   B CD2 1 
ATOM   2545 C CD2 B LEU   B 2 103 ? -9.372  -13.631 -28.001 0.22 38.91  ? 112 LEU   B CD2 1 
ATOM   2546 C CD2 C LEU   B 2 103 ? -9.972  -14.223 -28.153 0.28 37.02  ? 112 LEU   B CD2 1 
ATOM   2547 C CD2 D LEU   B 2 103 ? -9.972  -14.223 -28.153 0.28 37.01  ? 112 LEU   B CD2 1 
ATOM   2548 N N   A PRO   B 2 104 ? -11.121 -10.019 -24.950 0.22 32.81  ? 113 PRO   B N   1 
ATOM   2549 N N   B PRO   B 2 104 ? -11.121 -10.017 -24.949 0.22 32.83  ? 113 PRO   B N   1 
ATOM   2550 N N   C PRO   B 2 104 ? -11.768 -10.910 -25.025 0.28 33.80  ? 113 PRO   B N   1 
ATOM   2551 N N   D PRO   B 2 104 ? -11.767 -10.910 -25.025 0.28 33.82  ? 113 PRO   B N   1 
ATOM   2552 C CA  A PRO   B 2 104 ? -10.419 -9.632  -23.734 0.22 34.44  ? 113 PRO   B CA  1 
ATOM   2553 C CA  B PRO   B 2 104 ? -10.420 -9.630  -23.733 0.22 34.44  ? 113 PRO   B CA  1 
ATOM   2554 C CA  C PRO   B 2 104 ? -11.048 -10.600 -23.790 0.28 36.65  ? 113 PRO   B CA  1 
ATOM   2555 C CA  D PRO   B 2 104 ? -11.047 -10.600 -23.790 0.28 36.65  ? 113 PRO   B CA  1 
ATOM   2556 C C   A PRO   B 2 104 ? -9.260  -10.601 -23.481 0.22 36.27  ? 113 PRO   B C   1 
ATOM   2557 C C   B PRO   B 2 104 ? -9.260  -10.599 -23.481 0.22 36.27  ? 113 PRO   B C   1 
ATOM   2558 C C   C PRO   B 2 104 ? -9.833  -11.509 -23.528 0.28 38.64  ? 113 PRO   B C   1 
ATOM   2559 C C   D PRO   B 2 104 ? -9.832  -11.509 -23.528 0.28 38.64  ? 113 PRO   B C   1 
ATOM   2560 O O   A PRO   B 2 104 ? -9.334  -11.760 -23.860 0.22 35.08  ? 113 PRO   B O   1 
ATOM   2561 O O   B PRO   B 2 104 ? -9.335  -11.758 -23.860 0.22 35.09  ? 113 PRO   B O   1 
ATOM   2562 O O   C PRO   B 2 104 ? -9.929  -12.686 -23.834 0.28 38.72  ? 113 PRO   B O   1 
ATOM   2563 O O   D PRO   B 2 104 ? -9.928  -12.686 -23.834 0.28 38.72  ? 113 PRO   B O   1 
ATOM   2564 C CB  A PRO   B 2 104 ? -11.461 -9.742  -22.607 0.22 33.79  ? 113 PRO   B CB  1 
ATOM   2565 C CB  B PRO   B 2 104 ? -11.461 -9.743  -22.606 0.22 33.79  ? 113 PRO   B CB  1 
ATOM   2566 C CB  C PRO   B 2 104 ? -12.102 -10.785 -22.689 0.28 34.23  ? 113 PRO   B CB  1 
ATOM   2567 C CB  D PRO   B 2 104 ? -12.101 -10.785 -22.689 0.28 34.25  ? 113 PRO   B CB  1 
ATOM   2568 C CG  A PRO   B 2 104 ? -12.794 -9.863  -23.320 0.22 33.24  ? 113 PRO   B CG  1 
ATOM   2569 C CG  B PRO   B 2 104 ? -12.794 -9.858  -23.321 0.22 33.24  ? 113 PRO   B CG  1 
ATOM   2570 C CG  C PRO   B 2 104 ? -13.426 -10.767 -23.423 0.28 35.77  ? 113 PRO   B CG  1 
ATOM   2571 C CG  D PRO   B 2 104 ? -13.426 -10.766 -23.423 0.28 35.78  ? 113 PRO   B CG  1 
ATOM   2572 C CD  A PRO   B 2 104 ? -12.486 -10.481 -24.672 0.22 33.48  ? 113 PRO   B CD  1 
ATOM   2573 C CD  B PRO   B 2 104 ? -12.486 -10.480 -24.671 0.22 33.48  ? 113 PRO   B CD  1 
ATOM   2574 C CD  C PRO   B 2 104 ? -13.137 -11.384 -24.781 0.28 35.39  ? 113 PRO   B CD  1 
ATOM   2575 C CD  D PRO   B 2 104 ? -13.137 -11.383 -24.781 0.28 35.40  ? 113 PRO   B CD  1 
ATOM   2576 N N   A GLY   B 2 105 ? -8.216  -10.094 -22.840 0.22 39.01  ? 114 GLY   B N   1 
ATOM   2577 N N   B GLY   B 2 105 ? -8.216  -10.093 -22.840 0.22 39.01  ? 114 GLY   B N   1 
ATOM   2578 N N   C GLY   B 2 105 ? -8.731  -10.910 -23.050 0.28 40.22  ? 114 GLY   B N   1 
ATOM   2579 N N   D GLY   B 2 105 ? -8.731  -10.909 -23.050 0.28 40.22  ? 114 GLY   B N   1 
ATOM   2580 C CA  A GLY   B 2 105 ? -7.220  -10.942 -22.178 0.22 41.24  ? 114 GLY   B CA  1 
ATOM   2581 C CA  B GLY   B 2 105 ? -7.220  -10.942 -22.178 0.22 41.24  ? 114 GLY   B CA  1 
ATOM   2582 C CA  C GLY   B 2 105 ? -7.583  -11.561 -22.381 0.28 42.77  ? 114 GLY   B CA  1 
ATOM   2583 C CA  D GLY   B 2 105 ? -7.583  -11.561 -22.380 0.28 42.77  ? 114 GLY   B CA  1 
ATOM   2584 C C   A GLY   B 2 105 ? -7.771  -11.531 -20.891 0.22 43.84  ? 114 GLY   B C   1 
ATOM   2585 C C   B GLY   B 2 105 ? -7.771  -11.531 -20.891 0.22 43.83  ? 114 GLY   B C   1 
ATOM   2586 C C   C GLY   B 2 105 ? -7.871  -11.811 -20.904 0.28 44.96  ? 114 GLY   B C   1 
ATOM   2587 C C   D GLY   B 2 105 ? -7.871  -11.811 -20.904 0.28 44.95  ? 114 GLY   B C   1 
ATOM   2588 O O   A GLY   B 2 105 ? -9.004  -11.584 -20.702 0.22 42.22  ? 114 GLY   B O   1 
ATOM   2589 O O   B GLY   B 2 105 ? -9.004  -11.584 -20.703 0.22 42.23  ? 114 GLY   B O   1 
ATOM   2590 O O   C GLY   B 2 105 ? -9.072  -11.912 -20.569 0.28 40.71  ? 114 GLY   B O   1 
ATOM   2591 O O   D GLY   B 2 105 ? -9.071  -11.912 -20.569 0.28 40.73  ? 114 GLY   B O   1 
ATOM   2592 N N   . ILE   B 2 106 ? -6.842  -11.962 -20.050 1.00 46.17  ? 115 ILE   B N   1 
ATOM   2593 C CA  . ILE   B 2 106 ? -7.065  -12.521 -18.690 1.00 48.09  ? 115 ILE   B CA  1 
ATOM   2594 C C   . ILE   B 2 106 ? -6.215  -11.764 -17.670 1.00 44.54  ? 115 ILE   B C   1 
ATOM   2595 O O   . ILE   B 2 106 ? -5.055  -11.497 -17.906 1.00 48.30  ? 115 ILE   B O   1 
ATOM   2596 C CB  . ILE   B 2 106 ? -6.685  -14.013 -18.702 1.00 53.41  ? 115 ILE   B CB  1 
ATOM   2597 C CG1 . ILE   B 2 106 ? -7.537  -14.837 -19.665 1.00 60.22  ? 115 ILE   B CG1 1 
ATOM   2598 C CG2 . ILE   B 2 106 ? -6.733  -14.608 -17.309 1.00 59.87  ? 115 ILE   B CG2 1 
ATOM   2599 C CD1 . ILE   B 2 106 ? -8.900  -15.135 -19.152 1.00 57.76  ? 115 ILE   B CD1 1 
ATOM   2600 N N   A PHE   B 2 107 ? -6.834  -11.429 -16.537 0.22 45.30  ? 116 PHE   B N   1 
ATOM   2601 N N   B PHE   B 2 107 ? -6.834  -11.429 -16.537 0.22 45.30  ? 116 PHE   B N   1 
ATOM   2602 N N   C PHE   B 2 107 ? -6.845  -11.367 -16.566 0.28 45.13  ? 116 PHE   B N   1 
ATOM   2603 N N   D PHE   B 2 107 ? -6.845  -11.367 -16.566 0.28 45.12  ? 116 PHE   B N   1 
ATOM   2604 C CA  A PHE   B 2 107 ? -6.172  -11.000 -15.279 0.22 44.36  ? 116 PHE   B CA  1 
ATOM   2605 C CA  B PHE   B 2 107 ? -6.172  -11.000 -15.279 0.22 44.37  ? 116 PHE   B CA  1 
ATOM   2606 C CA  C PHE   B 2 107 ? -6.182  -11.020 -15.284 0.28 43.94  ? 116 PHE   B CA  1 
ATOM   2607 C CA  D PHE   B 2 107 ? -6.182  -11.020 -15.284 0.28 43.94  ? 116 PHE   B CA  1 
ATOM   2608 C C   A PHE   B 2 107 ? -6.101  -12.221 -14.355 0.22 44.90  ? 116 PHE   B C   1 
ATOM   2609 C C   B PHE   B 2 107 ? -6.101  -12.221 -14.355 0.22 44.90  ? 116 PHE   B C   1 
ATOM   2610 C C   C PHE   B 2 107 ? -6.116  -12.308 -14.463 0.28 43.92  ? 116 PHE   B C   1 
ATOM   2611 C C   D PHE   B 2 107 ? -6.116  -12.307 -14.462 0.28 43.93  ? 116 PHE   B C   1 
ATOM   2612 O O   A PHE   B 2 107 ? -7.164  -12.617 -13.842 0.22 45.61  ? 116 PHE   B O   1 
ATOM   2613 O O   B PHE   B 2 107 ? -7.163  -12.617 -13.842 0.22 45.61  ? 116 PHE   B O   1 
ATOM   2614 O O   C PHE   B 2 107 ? -7.191  -12.859 -14.173 0.28 42.82  ? 116 PHE   B O   1 
ATOM   2615 O O   D PHE   B 2 107 ? -7.191  -12.858 -14.171 0.28 42.83  ? 116 PHE   B O   1 
ATOM   2616 C CB  A PHE   B 2 107 ? -6.952  -9.851  -14.630 0.22 43.77  ? 116 PHE   B CB  1 
ATOM   2617 C CB  B PHE   B 2 107 ? -6.952  -9.852  -14.630 0.22 43.77  ? 116 PHE   B CB  1 
ATOM   2618 C CB  C PHE   B 2 107 ? -6.966  -9.941  -14.534 0.28 43.64  ? 116 PHE   B CB  1 
ATOM   2619 C CB  D PHE   B 2 107 ? -6.966  -9.941  -14.534 0.28 43.63  ? 116 PHE   B CB  1 
ATOM   2620 C CG  A PHE   B 2 107 ? -6.478  -8.452  -14.942 0.22 42.65  ? 116 PHE   B CG  1 
ATOM   2621 C CG  B PHE   B 2 107 ? -6.478  -8.452  -14.942 0.22 42.65  ? 116 PHE   B CG  1 
ATOM   2622 C CG  C PHE   B 2 107 ? -6.785  -8.521  -15.012 0.28 42.94  ? 116 PHE   B CG  1 
ATOM   2623 C CG  D PHE   B 2 107 ? -6.785  -8.521  -15.012 0.28 42.93  ? 116 PHE   B CG  1 
ATOM   2624 C CD1 A PHE   B 2 107 ? -5.684  -8.176  -16.046 0.22 41.94  ? 116 PHE   B CD1 1 
ATOM   2625 C CD1 B PHE   B 2 107 ? -5.685  -8.176  -16.046 0.22 41.94  ? 116 PHE   B CD1 1 
ATOM   2626 C CD1 C PHE   B 2 107 ? -6.168  -8.229  -16.220 0.28 41.06  ? 116 PHE   B CD1 1 
ATOM   2627 C CD1 D PHE   B 2 107 ? -6.168  -8.229  -16.220 0.28 41.07  ? 116 PHE   B CD1 1 
ATOM   2628 C CD2 A PHE   B 2 107 ? -6.878  -7.392  -14.141 0.22 41.86  ? 116 PHE   B CD2 1 
ATOM   2629 C CD2 B PHE   B 2 107 ? -6.878  -7.392  -14.141 0.22 41.87  ? 116 PHE   B CD2 1 
ATOM   2630 C CD2 C PHE   B 2 107 ? -7.294  -7.469  -14.264 0.28 40.48  ? 116 PHE   B CD2 1 
ATOM   2631 C CD2 D PHE   B 2 107 ? -7.294  -7.469  -14.264 0.28 40.49  ? 116 PHE   B CD2 1 
ATOM   2632 C CE1 A PHE   B 2 107 ? -5.265  -6.881  -16.312 0.22 41.84  ? 116 PHE   B CE1 1 
ATOM   2633 C CE1 B PHE   B 2 107 ? -5.265  -6.881  -16.313 0.22 41.84  ? 116 PHE   B CE1 1 
ATOM   2634 C CE1 C PHE   B 2 107 ? -6.027  -6.917  -16.645 0.28 42.05  ? 116 PHE   B CE1 1 
ATOM   2635 C CE1 D PHE   B 2 107 ? -6.027  -6.917  -16.645 0.28 42.05  ? 116 PHE   B CE1 1 
ATOM   2636 C CE2 A PHE   B 2 107 ? -6.462  -6.098  -14.411 0.22 41.66  ? 116 PHE   B CE2 1 
ATOM   2637 C CE2 B PHE   B 2 107 ? -6.462  -6.098  -14.411 0.22 41.67  ? 116 PHE   B CE2 1 
ATOM   2638 C CE2 C PHE   B 2 107 ? -7.149  -6.158  -14.689 0.28 40.69  ? 116 PHE   B CE2 1 
ATOM   2639 C CE2 D PHE   B 2 107 ? -7.149  -6.158  -14.689 0.28 40.70  ? 116 PHE   B CE2 1 
ATOM   2640 C CZ  A PHE   B 2 107 ? -5.660  -5.843  -15.498 0.22 42.62  ? 116 PHE   B CZ  1 
ATOM   2641 C CZ  B PHE   B 2 107 ? -5.660  -5.843  -15.499 0.22 42.62  ? 116 PHE   B CZ  1 
ATOM   2642 C CZ  C PHE   B 2 107 ? -6.523  -5.883  -15.882 0.28 41.14  ? 116 PHE   B CZ  1 
ATOM   2643 C CZ  D PHE   B 2 107 ? -6.523  -5.883  -15.882 0.28 41.14  ? 116 PHE   B CZ  1 
ATOM   2644 N N   . LYS   B 2 108 ? -4.906  -12.800 -14.179 1.00 45.09  ? 117 LYS   B N   1 
ATOM   2645 C CA  . LYS   B 2 108 ? -4.677  -13.987 -13.299 1.00 45.70  ? 117 LYS   B CA  1 
ATOM   2646 C C   . LYS   B 2 108 ? -4.325  -13.448 -11.904 1.00 39.19  ? 117 LYS   B C   1 
ATOM   2647 O O   . LYS   B 2 108 ? -3.405  -12.645 -11.805 1.00 37.01  ? 117 LYS   B O   1 
ATOM   2648 C CB  . LYS   B 2 108 ? -3.524  -14.844 -13.848 1.00 55.57  ? 117 LYS   B CB  1 
ATOM   2649 C CG  . LYS   B 2 108 ? -3.908  -15.983 -14.789 1.00 67.04  ? 117 LYS   B CG  1 
ATOM   2650 C CD  . LYS   B 2 108 ? -2.822  -16.371 -15.794 1.00 74.95  ? 117 LYS   B CD  1 
ATOM   2651 C CE  . LYS   B 2 108 ? -3.341  -17.209 -16.952 1.00 90.13  ? 117 LYS   B CE  1 
ATOM   2652 N NZ  . LYS   B 2 108 ? -2.288  -17.550 -17.947 1.00 95.95  ? 117 LYS   B NZ  1 
ATOM   2653 N N   A THR   B 2 109 ? -5.074  -13.867 -10.879 0.22 42.60  ? 118 THR   B N   1 
ATOM   2654 N N   B THR   B 2 109 ? -5.074  -13.867 -10.879 0.22 42.60  ? 118 THR   B N   1 
ATOM   2655 N N   C THR   B 2 109 ? -5.063  -13.865 -10.869 0.28 42.94  ? 118 THR   B N   1 
ATOM   2656 N N   D THR   B 2 109 ? -5.063  -13.865 -10.869 0.28 42.93  ? 118 THR   B N   1 
ATOM   2657 C CA  A THR   B 2 109 ? -4.916  -13.437 -9.461  0.22 44.16  ? 118 THR   B CA  1 
ATOM   2658 C CA  B THR   B 2 109 ? -4.916  -13.437 -9.461  0.22 44.15  ? 118 THR   B CA  1 
ATOM   2659 C CA  C THR   B 2 109 ? -4.874  -13.420 -9.457  0.28 44.63  ? 118 THR   B CA  1 
ATOM   2660 C CA  D THR   B 2 109 ? -4.874  -13.420 -9.457  0.28 44.62  ? 118 THR   B CA  1 
ATOM   2661 C C   A THR   B 2 109 ? -4.810  -14.675 -8.564  0.22 44.59  ? 118 THR   B C   1 
ATOM   2662 C C   B THR   B 2 109 ? -4.810  -14.675 -8.564  0.22 44.59  ? 118 THR   B C   1 
ATOM   2663 C C   C THR   B 2 109 ? -5.005  -14.616 -8.504  0.28 45.38  ? 118 THR   B C   1 
ATOM   2664 C C   D THR   B 2 109 ? -5.005  -14.616 -8.504  0.28 45.38  ? 118 THR   B C   1 
ATOM   2665 O O   A THR   B 2 109 ? -5.032  -15.790 -9.062  0.22 40.83  ? 118 THR   B O   1 
ATOM   2666 O O   B THR   B 2 109 ? -5.032  -15.790 -9.062  0.22 40.85  ? 118 THR   B O   1 
ATOM   2667 O O   C THR   B 2 109 ? -5.651  -15.620 -8.869  0.28 42.12  ? 118 THR   B O   1 
ATOM   2668 O O   D THR   B 2 109 ? -5.650  -15.621 -8.870  0.28 42.15  ? 118 THR   B O   1 
ATOM   2669 C CB  A THR   B 2 109 ? -6.083  -12.550 -8.998  0.22 43.18  ? 118 THR   B CB  1 
ATOM   2670 C CB  B THR   B 2 109 ? -6.083  -12.550 -8.999  0.22 43.18  ? 118 THR   B CB  1 
ATOM   2671 C CB  C THR   B 2 109 ? -5.864  -12.309 -9.061  0.28 43.28  ? 118 THR   B CB  1 
ATOM   2672 C CB  D THR   B 2 109 ? -5.864  -12.309 -9.061  0.28 43.29  ? 118 THR   B CB  1 
ATOM   2673 O OG1 A THR   B 2 109 ? -7.187  -13.375 -8.615  0.22 42.68  ? 118 THR   B OG1 1 
ATOM   2674 O OG1 B THR   B 2 109 ? -7.187  -13.375 -8.615  0.22 42.69  ? 118 THR   B OG1 1 
ATOM   2675 O OG1 C THR   B 2 109 ? -7.112  -12.876 -8.657  0.28 43.69  ? 118 THR   B OG1 1 
ATOM   2676 O OG1 D THR   B 2 109 ? -7.112  -12.876 -8.657  0.28 43.69  ? 118 THR   B OG1 1 
ATOM   2677 C CG2 A THR   B 2 109 ? -6.527  -11.564 -10.057 0.22 43.15  ? 118 THR   B CG2 1 
ATOM   2678 C CG2 B THR   B 2 109 ? -6.527  -11.564 -10.057 0.22 43.15  ? 118 THR   B CG2 1 
ATOM   2679 C CG2 C THR   B 2 109 ? -6.113  -11.310 -10.170 0.28 42.56  ? 118 THR   B CG2 1 
ATOM   2680 C CG2 D THR   B 2 109 ? -6.113  -11.310 -10.170 0.28 42.57  ? 118 THR   B CG2 1 
ATOM   2681 N N   . LYS   B 2 110 ? -4.472  -14.468 -7.289  1.00 49.47  ? 119 LYS   B N   1 
ATOM   2682 C CA  . LYS   B 2 110 ? -4.510  -15.530 -6.255  1.00 50.21  ? 119 LYS   B CA  1 
ATOM   2683 C C   . LYS   B 2 110 ? -5.952  -16.014 -6.001  1.00 55.26  ? 119 LYS   B C   1 
ATOM   2684 O O   . LYS   B 2 110 ? -6.120  -17.187 -5.618  1.00 61.15  ? 119 LYS   B O   1 
ATOM   2685 C CB  . LYS   B 2 110 ? -3.830  -15.027 -4.974  1.00 54.69  ? 119 LYS   B CB  1 
ATOM   2686 C CG  . LYS   B 2 110 ? -4.202  -13.628 -4.505  1.00 60.21  ? 119 LYS   B CG  1 
ATOM   2687 C CD  . LYS   B 2 110 ? -3.581  -13.206 -3.186  1.00 61.91  ? 119 LYS   B CD  1 
ATOM   2688 C CE  . LYS   B 2 110 ? -4.496  -13.380 -1.995  1.00 67.64  ? 119 LYS   B CE  1 
ATOM   2689 N NZ  . LYS   B 2 110 ? -5.494  -12.291 -1.902  1.00 67.02  ? 119 LYS   B NZ  1 
ATOM   2690 N N   A ASP   B 2 111 ? -6.950  -15.152 -6.236  0.22 53.51  ? 120 ASP   B N   1 
ATOM   2691 N N   B ASP   B 2 111 ? -6.949  -15.152 -6.236  0.22 53.51  ? 120 ASP   B N   1 
ATOM   2692 N N   C ASP   B 2 111 ? -6.949  -15.139 -6.206  0.28 54.13  ? 120 ASP   B N   1 
ATOM   2693 N N   D ASP   B 2 111 ? -6.949  -15.139 -6.206  0.28 54.13  ? 120 ASP   B N   1 
ATOM   2694 C CA  A ASP   B 2 111 ? -8.376  -15.400 -5.890  0.22 52.49  ? 120 ASP   B CA  1 
ATOM   2695 C CA  B ASP   B 2 111 ? -8.376  -15.401 -5.890  0.22 52.49  ? 120 ASP   B CA  1 
ATOM   2696 C CA  C ASP   B 2 111 ? -8.383  -15.392 -5.888  0.28 53.45  ? 120 ASP   B CA  1 
ATOM   2697 C CA  D ASP   B 2 111 ? -8.383  -15.392 -5.888  0.28 53.46  ? 120 ASP   B CA  1 
ATOM   2698 C C   A ASP   B 2 111 ? -9.169  -15.851 -7.123  0.22 52.51  ? 120 ASP   B C   1 
ATOM   2699 C C   B ASP   B 2 111 ? -9.169  -15.851 -7.123  0.22 52.51  ? 120 ASP   B C   1 
ATOM   2700 C C   C ASP   B 2 111 ? -9.125  -15.968 -7.101  0.28 52.79  ? 120 ASP   B C   1 
ATOM   2701 C C   D ASP   B 2 111 ? -9.125  -15.968 -7.101  0.28 52.80  ? 120 ASP   B C   1 
ATOM   2702 O O   A ASP   B 2 111 ? -10.373 -16.143 -6.965  0.22 54.72  ? 120 ASP   B O   1 
ATOM   2703 O O   B ASP   B 2 111 ? -10.373 -16.143 -6.965  0.22 54.71  ? 120 ASP   B O   1 
ATOM   2704 O O   C ASP   B 2 111 ? -10.251 -16.474 -6.907  0.28 55.19  ? 120 ASP   B O   1 
ATOM   2705 O O   D ASP   B 2 111 ? -10.251 -16.474 -6.907  0.28 55.18  ? 120 ASP   B O   1 
ATOM   2706 C CB  A ASP   B 2 111 ? -8.980  -14.154 -5.243  0.22 51.72  ? 120 ASP   B CB  1 
ATOM   2707 C CB  B ASP   B 2 111 ? -8.980  -14.154 -5.243  0.22 51.72  ? 120 ASP   B CB  1 
ATOM   2708 C CB  C ASP   B 2 111 ? -9.069  -14.116 -5.391  0.28 53.45  ? 120 ASP   B CB  1 
ATOM   2709 C CB  D ASP   B 2 111 ? -9.069  -14.116 -5.391  0.28 53.46  ? 120 ASP   B CB  1 
ATOM   2710 C CG  A ASP   B 2 111 ? -8.282  -13.791 -3.945  0.22 52.62  ? 120 ASP   B CG  1 
ATOM   2711 C CG  B ASP   B 2 111 ? -8.282  -13.792 -3.945  0.22 52.61  ? 120 ASP   B CG  1 
ATOM   2712 C CG  C ASP   B 2 111 ? -8.696  -13.746 -3.966  0.28 56.16  ? 120 ASP   B CG  1 
ATOM   2713 C CG  D ASP   B 2 111 ? -8.696  -13.746 -3.965  0.28 56.15  ? 120 ASP   B CG  1 
ATOM   2714 O OD1 A ASP   B 2 111 ? -8.008  -14.719 -3.158  0.22 49.71  ? 120 ASP   B OD1 1 
ATOM   2715 O OD1 B ASP   B 2 111 ? -8.013  -14.719 -3.155  0.22 49.72  ? 120 ASP   B OD1 1 
ATOM   2716 O OD1 C ASP   B 2 111 ? -7.570  -14.091 -3.549  0.28 53.78  ? 120 ASP   B OD1 1 
ATOM   2717 O OD1 D ASP   B 2 111 ? -7.570  -14.091 -3.548  0.28 53.79  ? 120 ASP   B OD1 1 
ATOM   2718 O OD2 A ASP   B 2 111 ? -7.995  -12.594 -3.745  0.22 52.80  ? 120 ASP   B OD2 1 
ATOM   2719 O OD2 B ASP   B 2 111 ? -7.990  -12.596 -3.746  0.22 52.80  ? 120 ASP   B OD2 1 
ATOM   2720 O OD2 C ASP   B 2 111 ? -9.540  -13.125 -3.280  0.28 57.25  ? 120 ASP   B OD2 1 
ATOM   2721 O OD2 D ASP   B 2 111 ? -9.540  -13.125 -3.280  0.28 57.23  ? 120 ASP   B OD2 1 
ATOM   2722 N N   . GLY   B 2 112 ? -8.528  -15.901 -8.294  1.00 52.97  ? 121 GLY   B N   1 
ATOM   2723 C CA  . GLY   B 2 112 ? -9.175  -16.357 -9.535  1.00 50.66  ? 121 GLY   B CA  1 
ATOM   2724 C C   . GLY   B 2 112 ? -8.794  -15.512 -10.734 1.00 48.56  ? 121 GLY   B C   1 
ATOM   2725 O O   . GLY   B 2 112 ? -8.085  -14.519 -10.587 1.00 48.15  ? 121 GLY   B O   1 
ATOM   2726 N N   A ASP   B 2 113 ? -9.242  -15.960 -11.913 0.22 49.44  ? 122 ASP   B N   1 
ATOM   2727 N N   B ASP   B 2 113 ? -9.242  -15.960 -11.913 0.22 49.43  ? 122 ASP   B N   1 
ATOM   2728 N N   C ASP   B 2 113 ? -9.273  -15.912 -11.910 0.28 50.19  ? 122 ASP   B N   1 
ATOM   2729 N N   D ASP   B 2 113 ? -9.273  -15.912 -11.910 0.28 50.19  ? 122 ASP   B N   1 
ATOM   2730 C CA  A ASP   B 2 113 ? -9.037  -15.320 -13.242 0.22 50.25  ? 122 ASP   B CA  1 
ATOM   2731 C CA  B ASP   B 2 113 ? -9.037  -15.320 -13.242 0.22 50.24  ? 122 ASP   B CA  1 
ATOM   2732 C CA  C ASP   B 2 113 ? -8.962  -15.256 -13.206 0.28 51.97  ? 122 ASP   B CA  1 
ATOM   2733 C CA  D ASP   B 2 113 ? -8.962  -15.256 -13.206 0.28 51.96  ? 122 ASP   B CA  1 
ATOM   2734 C C   A ASP   B 2 113 ? -10.163 -14.308 -13.485 0.22 47.07  ? 122 ASP   B C   1 
ATOM   2735 C C   B ASP   B 2 113 ? -10.163 -14.308 -13.485 0.22 47.07  ? 122 ASP   B C   1 
ATOM   2736 C C   C ASP   B 2 113 ? -10.154 -14.376 -13.604 0.28 47.61  ? 122 ASP   B C   1 
ATOM   2737 C C   D ASP   B 2 113 ? -10.154 -14.376 -13.604 0.28 47.62  ? 122 ASP   B C   1 
ATOM   2738 O O   A ASP   B 2 113 ? -11.292 -14.572 -13.024 0.22 43.18  ? 122 ASP   B O   1 
ATOM   2739 O O   B ASP   B 2 113 ? -11.292 -14.572 -13.024 0.22 43.20  ? 122 ASP   B O   1 
ATOM   2740 O O   C ASP   B 2 113 ? -11.308 -14.788 -13.355 0.28 42.36  ? 122 ASP   B O   1 
ATOM   2741 O O   D ASP   B 2 113 ? -11.308 -14.788 -13.355 0.28 42.39  ? 122 ASP   B O   1 
ATOM   2742 C CB  A ASP   B 2 113 ? -9.065  -16.351 -14.376 0.22 51.50  ? 122 ASP   B CB  1 
ATOM   2743 C CB  B ASP   B 2 113 ? -9.065  -16.351 -14.376 0.22 51.50  ? 122 ASP   B CB  1 
ATOM   2744 C CB  C ASP   B 2 113 ? -8.572  -16.301 -14.254 0.28 54.65  ? 122 ASP   B CB  1 
ATOM   2745 C CB  D ASP   B 2 113 ? -8.572  -16.301 -14.255 0.28 54.64  ? 122 ASP   B CB  1 
ATOM   2746 C CG  A ASP   B 2 113 ? -7.860  -17.271 -14.472 0.22 54.03  ? 122 ASP   B CG  1 
ATOM   2747 C CG  B ASP   B 2 113 ? -7.859  -17.270 -14.473 0.22 54.03  ? 122 ASP   B CG  1 
ATOM   2748 C CG  C ASP   B 2 113 ? -7.254  -16.996 -13.942 0.28 59.85  ? 122 ASP   B CG  1 
ATOM   2749 C CG  D ASP   B 2 113 ? -7.255  -16.996 -13.942 0.28 59.81  ? 122 ASP   B CG  1 
ATOM   2750 O OD1 A ASP   B 2 113 ? -6.796  -16.927 -13.908 0.22 58.21  ? 122 ASP   B OD1 1 
ATOM   2751 O OD1 B ASP   B 2 113 ? -6.796  -16.927 -13.907 0.22 58.19  ? 122 ASP   B OD1 1 
ATOM   2752 O OD1 C ASP   B 2 113 ? -6.833  -16.960 -12.761 0.28 63.41  ? 122 ASP   B OD1 1 
ATOM   2753 O OD1 D ASP   B 2 113 ? -6.834  -16.961 -12.761 0.28 63.37  ? 122 ASP   B OD1 1 
ATOM   2754 O OD2 A ASP   B 2 113 ? -7.993  -18.321 -15.138 0.22 55.86  ? 122 ASP   B OD2 1 
ATOM   2755 O OD2 B ASP   B 2 113 ? -7.991  -18.318 -15.142 0.22 55.85  ? 122 ASP   B OD2 1 
ATOM   2756 O OD2 C ASP   B 2 113 ? -6.648  -17.555 -14.880 0.28 60.66  ? 122 ASP   B OD2 1 
ATOM   2757 O OD2 D ASP   B 2 113 ? -6.648  -17.554 -14.880 0.28 60.64  ? 122 ASP   B OD2 1 
ATOM   2758 N N   . ILE   B 2 114 ? -9.869  -13.204 -14.182 1.00 46.21  ? 123 ILE   B N   1 
ATOM   2759 C CA  . ILE   B 2 114 ? -10.903 -12.195 -14.566 1.00 48.49  ? 123 ILE   B CA  1 
ATOM   2760 C C   . ILE   B 2 114 ? -10.649 -11.826 -16.034 1.00 45.12  ? 123 ILE   B C   1 
ATOM   2761 O O   . ILE   B 2 114 ? -9.513  -11.526 -16.333 1.00 42.33  ? 123 ILE   B O   1 
ATOM   2762 C CB  . ILE   B 2 114 ? -10.818 -10.951 -13.647 1.00 48.35  ? 123 ILE   B CB  1 
ATOM   2763 C CG1 . ILE   B 2 114 ? -10.575 -11.293 -12.178 1.00 57.46  ? 123 ILE   B CG1 1 
ATOM   2764 C CG2 . ILE   B 2 114 ? -12.035 -10.061 -13.793 1.00 51.72  ? 123 ILE   B CG2 1 
ATOM   2765 C CD1 . ILE   B 2 114 ? -10.231 -10.085 -11.329 1.00 66.23  ? 123 ILE   B CD1 1 
ATOM   2766 N N   . GLY   B 2 115 ? -11.685 -11.733 -16.879 1.00 47.91  ? 124 GLY   B N   1 
ATOM   2767 C CA  . GLY   B 2 115 ? -11.574 -11.100 -18.211 1.00 39.27  ? 124 GLY   B CA  1 
ATOM   2768 C C   . GLY   B 2 115 ? -10.922 -9.737  -18.110 1.00 39.84  ? 124 GLY   B C   1 
ATOM   2769 O O   . GLY   B 2 115 ? -11.021 -9.036  -17.050 1.00 36.87  ? 124 GLY   B O   1 
ATOM   2770 N N   A ALA   B 2 116 ? -10.223 -9.318  -19.162 0.22 36.15  ? 125 ALA   B N   1 
ATOM   2771 N N   B ALA   B 2 116 ? -10.225 -9.320  -19.166 0.22 36.11  ? 125 ALA   B N   1 
ATOM   2772 N N   C ALA   B 2 116 ? -10.259 -9.338  -19.195 0.28 38.53  ? 125 ALA   B N   1 
ATOM   2773 N N   D ALA   B 2 116 ? -10.258 -9.342  -19.194 0.28 38.62  ? 125 ALA   B N   1 
ATOM   2774 C CA  A ALA   B 2 116 ? -9.555  -7.996  -19.218 0.22 36.93  ? 125 ALA   B CA  1 
ATOM   2775 C CA  B ALA   B 2 116 ? -9.552  -8.001  -19.222 0.22 36.82  ? 125 ALA   B CA  1 
ATOM   2776 C CA  C ALA   B 2 116 ? -9.597  -8.023  -19.350 0.28 41.72  ? 125 ALA   B CA  1 
ATOM   2777 C CA  D ALA   B 2 116 ? -9.597  -8.028  -19.348 0.28 41.90  ? 125 ALA   B CA  1 
ATOM   2778 C C   A ALA   B 2 116 ? -9.505  -7.508  -20.669 0.22 35.71  ? 125 ALA   B C   1 
ATOM   2779 C C   B ALA   B 2 116 ? -9.494  -7.502  -20.669 0.22 35.48  ? 125 ALA   B C   1 
ATOM   2780 C C   C ALA   B 2 116 ? -9.823  -7.508  -20.777 0.28 42.05  ? 125 ALA   B C   1 
ATOM   2781 C C   D ALA   B 2 116 ? -9.807  -7.509  -20.775 0.28 42.41  ? 125 ALA   B C   1 
ATOM   2782 O O   A ALA   B 2 116 ? -8.766  -8.119  -21.460 0.22 33.44  ? 125 ALA   B O   1 
ATOM   2783 O O   B ALA   B 2 116 ? -8.769  -8.111  -21.476 0.22 33.36  ? 125 ALA   B O   1 
ATOM   2784 O O   C ALA   B 2 116 ? -10.182 -8.345  -21.648 0.28 40.69  ? 125 ALA   B O   1 
ATOM   2785 O O   D ALA   B 2 116 ? -10.175 -8.331  -21.657 0.28 41.30  ? 125 ALA   B O   1 
ATOM   2786 C CB  A ALA   B 2 116 ? -8.183  -8.081  -18.597 0.22 38.69  ? 125 ALA   B CB  1 
ATOM   2787 C CB  B ALA   B 2 116 ? -8.183  -8.087  -18.600 0.22 38.61  ? 125 ALA   B CB  1 
ATOM   2788 C CB  C ALA   B 2 116 ? -8.133  -8.146  -19.021 0.28 44.21  ? 125 ALA   B CB  1 
ATOM   2789 C CB  D ALA   B 2 116 ? -8.134  -8.147  -19.011 0.28 44.31  ? 125 ALA   B CB  1 
ATOM   2790 N N   A VAL   B 2 117 ? -10.322 -6.504  -21.017 0.22 34.55  ? 126 VAL   B N   1 
ATOM   2791 N N   B VAL   B 2 117 ? -10.224 -6.416  -20.950 0.22 34.03  ? 126 VAL   B N   1 
ATOM   2792 N N   C VAL   B 2 117 ? -9.683  -6.191  -20.986 0.28 40.27  ? 126 VAL   B N   1 
ATOM   2793 N N   D VAL   B 2 117 ? -9.530  -6.208  -20.965 0.28 41.20  ? 126 VAL   B N   1 
ATOM   2794 C CA  A VAL   B 2 117 ? -10.398 -5.915  -22.393 0.22 34.94  ? 126 VAL   B CA  1 
ATOM   2795 C CA  B VAL   B 2 117 ? -10.402 -5.794  -22.298 0.22 34.12  ? 126 VAL   B CA  1 
ATOM   2796 C CA  C VAL   B 2 117 ? -9.678  -5.536  -22.332 0.28 39.60  ? 126 VAL   B CA  1 
ATOM   2797 C CA  D VAL   B 2 117 ? -9.723  -5.412  -22.218 0.28 40.69  ? 126 VAL   B CA  1 
ATOM   2798 C C   A VAL   B 2 117 ? -9.222  -4.951  -22.585 0.22 34.43  ? 126 VAL   B C   1 
ATOM   2799 C C   B VAL   B 2 117 ? -9.223  -4.858  -22.586 0.22 33.85  ? 126 VAL   B C   1 
ATOM   2800 C C   C VAL   B 2 117 ? -8.540  -4.503  -22.377 0.28 42.24  ? 126 VAL   B C   1 
ATOM   2801 C C   D VAL   B 2 117 ? -8.553  -4.419  -22.363 0.28 42.71  ? 126 VAL   B C   1 
ATOM   2802 O O   A VAL   B 2 117 ? -9.072  -4.040  -21.753 0.22 33.52  ? 126 VAL   B O   1 
ATOM   2803 O O   B VAL   B 2 117 ? -9.087  -3.860  -21.854 0.22 32.15  ? 126 VAL   B O   1 
ATOM   2804 O O   C VAL   B 2 117 ? -8.325  -3.807  -21.364 0.28 42.29  ? 126 VAL   B O   1 
ATOM   2805 O O   D VAL   B 2 117 ? -8.338  -3.633  -21.420 0.28 42.08  ? 126 VAL   B O   1 
ATOM   2806 C CB  A VAL   B 2 117 ? -11.754 -5.226  -22.668 0.22 35.39  ? 126 VAL   B CB  1 
ATOM   2807 C CB  B VAL   B 2 117 ? -11.738 -5.025  -22.340 0.22 34.14  ? 126 VAL   B CB  1 
ATOM   2808 C CB  C VAL   B 2 117 ? -11.045 -4.906  -22.678 0.28 38.13  ? 126 VAL   B CB  1 
ATOM   2809 C CB  D VAL   B 2 117 ? -11.087 -4.692  -22.162 0.28 40.06  ? 126 VAL   B CB  1 
ATOM   2810 C CG1 A VAL   B 2 117 ? -12.890 -6.236  -22.667 0.22 36.08  ? 126 VAL   B CG1 1 
ATOM   2811 C CG1 B VAL   B 2 117 ? -11.843 -4.113  -23.544 0.22 34.40  ? 126 VAL   B CG1 1 
ATOM   2812 C CG1 C VAL   B 2 117 ? -12.152 -5.951  -22.690 0.28 39.36  ? 126 VAL   B CG1 1 
ATOM   2813 C CG1 D VAL   B 2 117 ? -11.146 -3.454  -23.036 0.28 40.80  ? 126 VAL   B CG1 1 
ATOM   2814 C CG2 A VAL   B 2 117 ? -12.067 -4.077  -21.715 0.22 35.76  ? 126 VAL   B CG2 1 
ATOM   2815 C CG2 B VAL   B 2 117 ? -12.929 -5.964  -22.267 0.22 33.74  ? 126 VAL   B CG2 1 
ATOM   2816 C CG2 C VAL   B 2 117 ? -11.416 -3.751  -21.760 0.28 38.99  ? 126 VAL   B CG2 1 
ATOM   2817 C CG2 D VAL   B 2 117 ? -12.237 -5.636  -22.480 0.28 40.95  ? 126 VAL   B CG2 1 
ATOM   2818 N N   A ALA   B 2 118 ? -8.434  -5.136  -23.652 0.22 32.85  ? 127 ALA   B N   1 
ATOM   2819 N N   B ALA   B 2 118 ? -8.441  -5.118  -23.643 0.22 32.61  ? 127 ALA   B N   1 
ATOM   2820 N N   C ALA   B 2 118 ? -7.835  -4.413  -23.511 0.28 41.77  ? 127 ALA   B N   1 
ATOM   2821 N N   D ALA   B 2 118 ? -7.829  -4.427  -23.494 0.28 42.00  ? 127 ALA   B N   1 
ATOM   2822 C CA  A ALA   B 2 118 ? -7.192  -4.373  -23.932 0.22 35.38  ? 127 ALA   B CA  1 
ATOM   2823 C CA  B ALA   B 2 118 ? -7.193  -4.370  -23.937 0.22 35.26  ? 127 ALA   B CA  1 
ATOM   2824 C CA  C ALA   B 2 118 ? -6.604  -3.599  -23.695 0.28 45.42  ? 127 ALA   B CA  1 
ATOM   2825 C CA  D ALA   B 2 118 ? -6.601  -3.609  -23.696 0.28 45.54  ? 127 ALA   B CA  1 
ATOM   2826 C C   A ALA   B 2 118 ? -7.495  -3.154  -24.814 0.22 37.07  ? 127 ALA   B C   1 
ATOM   2827 C C   B ALA   B 2 118 ? -7.492  -3.151  -24.820 0.22 37.02  ? 127 ALA   B C   1 
ATOM   2828 C C   C ALA   B 2 118 ? -6.896  -2.344  -24.526 0.28 47.45  ? 127 ALA   B C   1 
ATOM   2829 C C   D ALA   B 2 118 ? -6.896  -2.351  -24.523 0.28 47.50  ? 127 ALA   B C   1 
ATOM   2830 O O   A ALA   B 2 118 ? -7.354  -3.258  -26.055 0.22 33.28  ? 127 ALA   B O   1 
ATOM   2831 O O   B ALA   B 2 118 ? -7.352  -3.257  -26.061 0.22 33.28  ? 127 ALA   B O   1 
ATOM   2832 O O   C ALA   B 2 118 ? -5.953  -1.832  -25.154 0.28 47.15  ? 127 ALA   B O   1 
ATOM   2833 O O   D ALA   B 2 118 ? -5.953  -1.836  -25.148 0.28 47.15  ? 127 ALA   B O   1 
ATOM   2834 C CB  A ALA   B 2 118 ? -6.162  -5.275  -24.574 0.22 35.45  ? 127 ALA   B CB  1 
ATOM   2835 C CB  B ALA   B 2 118 ? -6.168  -5.279  -24.575 0.22 35.36  ? 127 ALA   B CB  1 
ATOM   2836 C CB  C ALA   B 2 118 ? -5.524  -4.435  -24.347 0.28 44.44  ? 127 ALA   B CB  1 
ATOM   2837 C CB  D ALA   B 2 118 ? -5.520  -4.439  -24.351 0.28 44.54  ? 127 ALA   B CB  1 
ATOM   2838 N N   A LEU   B 2 119 ? -7.898  -2.038  -24.192 0.22 40.12  ? 128 LEU   B N   1 
ATOM   2839 N N   B LEU   B 2 119 ? -7.895  -2.036  -24.197 0.22 40.08  ? 128 LEU   B N   1 
ATOM   2840 N N   C LEU   B 2 119 ? -8.146  -1.863  -24.506 0.28 52.58  ? 128 LEU   B N   1 
ATOM   2841 N N   D LEU   B 2 119 ? -8.146  -1.868  -24.503 0.28 52.56  ? 128 LEU   B N   1 
ATOM   2842 C CA  A LEU   B 2 119 ? -8.311  -0.789  -24.890 0.22 39.08  ? 128 LEU   B CA  1 
ATOM   2843 C CA  B LEU   B 2 119 ? -8.310  -0.787  -24.894 0.22 39.07  ? 128 LEU   B CA  1 
ATOM   2844 C CA  C LEU   B 2 119 ? -8.628  -0.703  -25.302 0.28 50.60  ? 128 LEU   B CA  1 
ATOM   2845 C CA  D LEU   B 2 119 ? -8.625  -0.707  -25.299 0.28 50.61  ? 128 LEU   B CA  1 
ATOM   2846 C C   A LEU   B 2 119 ? -7.904  0.428   -24.056 0.22 41.17  ? 128 LEU   B C   1 
ATOM   2847 C C   B LEU   B 2 119 ? -7.904  0.428   -24.058 0.22 41.17  ? 128 LEU   B C   1 
ATOM   2848 C C   C LEU   B 2 119 ? -8.423  0.567   -24.471 0.28 53.37  ? 128 LEU   B C   1 
ATOM   2849 C C   D LEU   B 2 119 ? -8.421  0.564   -24.469 0.28 53.37  ? 128 LEU   B C   1 
ATOM   2850 O O   A LEU   B 2 119 ? -7.873  0.320   -22.804 0.22 38.27  ? 128 LEU   B O   1 
ATOM   2851 O O   B LEU   B 2 119 ? -7.873  0.320   -22.806 0.22 38.28  ? 128 LEU   B O   1 
ATOM   2852 O O   C LEU   B 2 119 ? -9.211  0.777   -23.537 0.28 57.36  ? 128 LEU   B O   1 
ATOM   2853 O O   D LEU   B 2 119 ? -9.209  0.773   -23.535 0.28 57.33  ? 128 LEU   B O   1 
ATOM   2854 C CB  A LEU   B 2 119 ? -9.822  -0.823  -25.138 0.22 38.14  ? 128 LEU   B CB  1 
ATOM   2855 C CB  B LEU   B 2 119 ? -9.821  -0.824  -25.139 0.22 38.15  ? 128 LEU   B CB  1 
ATOM   2856 C CB  C LEU   B 2 119 ? -10.108 -0.916  -25.642 0.28 50.24  ? 128 LEU   B CB  1 
ATOM   2857 C CB  D LEU   B 2 119 ? -10.105 -0.918  -25.642 0.28 50.24  ? 128 LEU   B CB  1 
ATOM   2858 C CG  A LEU   B 2 119 ? -10.313 -1.923  -26.081 0.22 39.78  ? 128 LEU   B CG  1 
ATOM   2859 C CG  B LEU   B 2 119 ? -10.310 -1.923  -26.083 0.22 39.77  ? 128 LEU   B CG  1 
ATOM   2860 C CG  C LEU   B 2 119 ? -10.467 -2.249  -26.305 0.28 50.59  ? 128 LEU   B CG  1 
ATOM   2861 C CG  D LEU   B 2 119 ? -10.464 -2.250  -26.308 0.28 50.56  ? 128 LEU   B CG  1 
ATOM   2862 C CD1 A LEU   B 2 119 ? -11.825 -2.062  -26.024 0.22 37.96  ? 128 LEU   B CD1 1 
ATOM   2863 C CD1 B LEU   B 2 119 ? -11.823 -2.059  -26.033 0.22 37.97  ? 128 LEU   B CD1 1 
ATOM   2864 C CD1 C LEU   B 2 119 ? -11.951 -2.553  -26.166 0.28 47.40  ? 128 LEU   B CD1 1 
ATOM   2865 C CD1 D LEU   B 2 119 ? -11.949 -2.554  -26.174 0.28 47.39  ? 128 LEU   B CD1 1 
ATOM   2866 C CD2 A LEU   B 2 119 ? -9.852  -1.658  -27.508 0.22 39.70  ? 128 LEU   B CD2 1 
ATOM   2867 C CD2 B LEU   B 2 119 ? -9.847  -1.659  -27.510 0.22 39.69  ? 128 LEU   B CD2 1 
ATOM   2868 C CD2 C LEU   B 2 119 ? -10.062 -2.259  -27.772 0.28 50.88  ? 128 LEU   B CD2 1 
ATOM   2869 C CD2 D LEU   B 2 119 ? -10.058 -2.258  -27.774 0.28 50.86  ? 128 LEU   B CD2 1 
ATOM   2870 N N   A ASP   B 2 120 ? -7.634  1.543   -24.740 0.22 42.62  ? 129 ASP   B N   1 
ATOM   2871 N N   B ASP   B 2 120 ? -7.634  1.544   -24.742 0.22 42.63  ? 129 ASP   B N   1 
ATOM   2872 N N   C ASP   B 2 120 ? -7.392  1.367   -24.765 0.28 55.25  ? 129 ASP   B N   1 
ATOM   2873 N N   D ASP   B 2 120 ? -7.393  1.365   -24.764 0.28 55.25  ? 129 ASP   B N   1 
ATOM   2874 C CA  A ASP   B 2 120 ? -6.955  2.746   -24.197 0.22 45.78  ? 129 ASP   B CA  1 
ATOM   2875 C CA  B ASP   B 2 120 ? -6.954  2.747   -24.197 0.22 45.78  ? 129 ASP   B CA  1 
ATOM   2876 C CA  C ASP   B 2 120 ? -7.089  2.600   -23.990 0.28 57.53  ? 129 ASP   B CA  1 
ATOM   2877 C CA  D ASP   B 2 120 ? -7.090  2.599   -23.990 0.28 57.52  ? 129 ASP   B CA  1 
ATOM   2878 C C   A ASP   B 2 120 ? -7.839  3.971   -24.479 0.22 47.48  ? 129 ASP   B C   1 
ATOM   2879 C C   B ASP   B 2 120 ? -7.839  3.972   -24.479 0.22 47.48  ? 129 ASP   B C   1 
ATOM   2880 C C   C ASP   B 2 120 ? -8.097  3.687   -24.391 0.28 55.43  ? 129 ASP   B C   1 
ATOM   2881 C C   D ASP   B 2 120 ? -8.098  3.686   -24.391 0.28 55.42  ? 129 ASP   B C   1 
ATOM   2882 O O   A ASP   B 2 120 ? -7.934  4.372   -25.649 0.22 44.39  ? 129 ASP   B O   1 
ATOM   2883 O O   B ASP   B 2 120 ? -7.936  4.372   -25.649 0.22 44.40  ? 129 ASP   B O   1 
ATOM   2884 O O   C ASP   B 2 120 ? -8.587  3.645   -25.530 0.28 54.55  ? 129 ASP   B O   1 
ATOM   2885 O O   D ASP   B 2 120 ? -8.589  3.644   -25.530 0.28 54.55  ? 129 ASP   B O   1 
ATOM   2886 C CB  A ASP   B 2 120 ? -5.551  2.845   -24.807 0.22 47.50  ? 129 ASP   B CB  1 
ATOM   2887 C CB  B ASP   B 2 120 ? -5.551  2.846   -24.807 0.22 47.49  ? 129 ASP   B CB  1 
ATOM   2888 C CB  C ASP   B 2 120 ? -5.631  3.040   -24.153 0.28 62.68  ? 129 ASP   B CB  1 
ATOM   2889 C CB  D ASP   B 2 120 ? -5.632  3.040   -24.153 0.28 62.65  ? 129 ASP   B CB  1 
ATOM   2890 C CG  A ASP   B 2 120 ? -4.520  3.602   -23.984 0.22 48.67  ? 129 ASP   B CG  1 
ATOM   2891 C CG  B ASP   B 2 120 ? -4.520  3.603   -23.983 0.22 48.66  ? 129 ASP   B CG  1 
ATOM   2892 C CG  C ASP   B 2 120 ? -5.169  4.036   -23.094 0.28 66.48  ? 129 ASP   B CG  1 
ATOM   2893 C CG  D ASP   B 2 120 ? -5.169  4.036   -23.095 0.28 66.45  ? 129 ASP   B CG  1 
ATOM   2894 O OD1 A ASP   B 2 120 ? -4.806  3.928   -22.810 0.22 49.42  ? 129 ASP   B OD1 1 
ATOM   2895 O OD1 B ASP   B 2 120 ? -4.808  3.931   -22.810 0.22 49.41  ? 129 ASP   B OD1 1 
ATOM   2896 O OD1 C ASP   B 2 120 ? -5.914  4.249   -22.108 0.28 70.09  ? 129 ASP   B OD1 1 
ATOM   2897 O OD1 D ASP   B 2 120 ? -5.912  4.247   -22.106 0.28 70.05  ? 129 ASP   B OD1 1 
ATOM   2898 O OD2 A ASP   B 2 120 ? -3.426  3.858   -24.527 0.22 50.23  ? 129 ASP   B OD2 1 
ATOM   2899 O OD2 B ASP   B 2 120 ? -3.424  3.855   -24.524 0.22 50.22  ? 129 ASP   B OD2 1 
ATOM   2900 O OD2 C ASP   B 2 120 ? -4.066  4.596   -23.259 0.28 68.42  ? 129 ASP   B OD2 1 
ATOM   2901 O OD2 D ASP   B 2 120 ? -4.068  4.598   -23.261 0.28 68.39  ? 129 ASP   B OD2 1 
ATOM   2902 N N   . TYR   B 2 121 ? -8.443  4.566   -23.444 1.00 51.32  ? 130 TYR   B N   1 
ATOM   2903 C CA  . TYR   B 2 121 ? -9.459  5.643   -23.610 1.00 47.43  ? 130 TYR   B CA  1 
ATOM   2904 C C   . TYR   B 2 121 ? -9.302  6.590   -22.440 1.00 42.98  ? 130 TYR   B C   1 
ATOM   2905 O O   . TYR   B 2 121 ? -8.763  6.184   -21.405 1.00 46.41  ? 130 TYR   B O   1 
ATOM   2906 C CB  . TYR   B 2 121 ? -10.881 5.090   -23.574 1.00 48.58  ? 130 TYR   B CB  1 
ATOM   2907 C CG  . TYR   B 2 121 ? -11.431 4.641   -24.897 1.00 55.16  ? 130 TYR   B CG  1 
ATOM   2908 C CD1 . TYR   B 2 121 ? -11.558 5.530   -25.954 1.00 58.34  ? 130 TYR   B CD1 1 
ATOM   2909 C CD2 . TYR   B 2 121 ? -11.825 3.327   -25.106 1.00 57.14  ? 130 TYR   B CD2 1 
ATOM   2910 C CE1 . TYR   B 2 121 ? -12.072 5.122   -27.176 1.00 59.38  ? 130 TYR   B CE1 1 
ATOM   2911 C CE2 . TYR   B 2 121 ? -12.330 2.904   -26.326 1.00 57.63  ? 130 TYR   B CE2 1 
ATOM   2912 C CZ  . TYR   B 2 121 ? -12.455 3.806   -27.365 1.00 55.43  ? 130 TYR   B CZ  1 
ATOM   2913 O OH  . TYR   B 2 121 ? -12.940 3.398   -28.572 1.00 68.26  ? 130 TYR   B OH  1 
ATOM   2914 N N   A PRO   B 2 122 ? -9.710  7.880   -22.501 0.22 41.79  ? 131 PRO   B N   1 
ATOM   2915 N N   B PRO   B 2 122 ? -9.710  7.880   -22.501 0.22 41.80  ? 131 PRO   B N   1 
ATOM   2916 N N   C PRO   B 2 122 ? -9.830  7.827   -22.567 0.28 44.42  ? 131 PRO   B N   1 
ATOM   2917 N N   D PRO   B 2 122 ? -9.829  7.827   -22.567 0.28 44.43  ? 131 PRO   B N   1 
ATOM   2918 C CA  A PRO   B 2 122 ? -9.348  8.835   -21.445 0.22 40.21  ? 131 PRO   B CA  1 
ATOM   2919 C CA  B PRO   B 2 122 ? -9.349  8.835   -21.445 0.22 40.21  ? 131 PRO   B CA  1 
ATOM   2920 C CA  C PRO   B 2 122 ? -9.858  8.760   -21.453 0.28 43.99  ? 131 PRO   B CA  1 
ATOM   2921 C CA  D PRO   B 2 122 ? -9.857  8.760   -21.453 0.28 43.98  ? 131 PRO   B CA  1 
ATOM   2922 C C   A PRO   B 2 122 ? -9.963  8.490   -20.074 0.22 36.86  ? 131 PRO   B C   1 
ATOM   2923 C C   B PRO   B 2 122 ? -9.963  8.490   -20.074 0.22 36.87  ? 131 PRO   B C   1 
ATOM   2924 C C   C PRO   B 2 122 ? -10.478 8.021   -20.260 0.28 39.11  ? 131 PRO   B C   1 
ATOM   2925 C C   D PRO   B 2 122 ? -10.478 8.022   -20.260 0.28 39.11  ? 131 PRO   B C   1 
ATOM   2926 O O   A PRO   B 2 122 ? -10.876 7.691   -20.032 0.22 34.11  ? 131 PRO   B O   1 
ATOM   2927 O O   B PRO   B 2 122 ? -10.876 7.691   -20.032 0.22 34.12  ? 131 PRO   B O   1 
ATOM   2928 O O   C PRO   B 2 122 ? -11.373 7.200   -20.475 0.28 34.82  ? 131 PRO   B O   1 
ATOM   2929 O O   D PRO   B 2 122 ? -11.373 7.201   -20.474 0.28 34.85  ? 131 PRO   B O   1 
ATOM   2930 C CB  A PRO   B 2 122 ? -9.860  10.188  -21.968 0.22 42.94  ? 131 PRO   B CB  1 
ATOM   2931 C CB  B PRO   B 2 122 ? -9.861  10.188  -21.968 0.22 42.93  ? 131 PRO   B CB  1 
ATOM   2932 C CB  C PRO   B 2 122 ? -10.731 9.923   -21.948 0.28 48.32  ? 131 PRO   B CB  1 
ATOM   2933 C CB  D PRO   B 2 122 ? -10.731 9.923   -21.948 0.28 48.28  ? 131 PRO   B CB  1 
ATOM   2934 C CG  A PRO   B 2 122 ? -10.101 9.965   -23.452 0.22 44.09  ? 131 PRO   B CG  1 
ATOM   2935 C CG  B PRO   B 2 122 ? -10.102 9.965   -23.452 0.22 44.08  ? 131 PRO   B CG  1 
ATOM   2936 C CG  C PRO   B 2 122 ? -10.635 9.849   -23.457 0.28 48.68  ? 131 PRO   B CG  1 
ATOM   2937 C CG  D PRO   B 2 122 ? -10.635 9.849   -23.457 0.28 48.65  ? 131 PRO   B CG  1 
ATOM   2938 C CD  A PRO   B 2 122 ? -10.494 8.507   -23.576 0.22 44.16  ? 131 PRO   B CD  1 
ATOM   2939 C CD  B PRO   B 2 122 ? -10.494 8.506   -23.576 0.22 44.15  ? 131 PRO   B CD  1 
ATOM   2940 C CD  C PRO   B 2 122 ? -10.470 8.377   -23.773 0.28 48.31  ? 131 PRO   B CD  1 
ATOM   2941 C CD  D PRO   B 2 122 ? -10.469 8.378   -23.773 0.28 48.28  ? 131 PRO   B CD  1 
ATOM   2942 N N   A ALA   B 2 123 ? -9.443  9.088   -18.995 0.22 35.76  ? 132 ALA   B N   1 
ATOM   2943 N N   B ALA   B 2 123 ? -9.443  9.088   -18.995 0.22 35.75  ? 132 ALA   B N   1 
ATOM   2944 N N   C ALA   B 2 123 ? -9.947  8.295   -19.070 0.28 36.18  ? 132 ALA   B N   1 
ATOM   2945 N N   D ALA   B 2 123 ? -9.947  8.296   -19.069 0.28 36.19  ? 132 ALA   B N   1 
ATOM   2946 C CA  A ALA   B 2 123 ? -9.777  8.756   -17.585 0.22 32.31  ? 132 ALA   B CA  1 
ATOM   2947 C CA  B ALA   B 2 123 ? -9.777  8.756   -17.585 0.22 32.32  ? 132 ALA   B CA  1 
ATOM   2948 C CA  C ALA   B 2 123 ? -10.465 7.829   -17.765 0.28 36.36  ? 132 ALA   B CA  1 
ATOM   2949 C CA  D ALA   B 2 123 ? -10.465 7.830   -17.765 0.28 36.36  ? 132 ALA   B CA  1 
ATOM   2950 C C   A ALA   B 2 123 ? -11.278 8.948   -17.317 0.22 31.47  ? 132 ALA   B C   1 
ATOM   2951 C C   B ALA   B 2 123 ? -11.278 8.948   -17.317 0.22 31.47  ? 132 ALA   B C   1 
ATOM   2952 C C   C ALA   B 2 123 ? -11.952 8.194   -17.657 0.28 35.09  ? 132 ALA   B C   1 
ATOM   2953 C C   D ALA   B 2 123 ? -11.952 8.195   -17.656 0.28 35.09  ? 132 ALA   B C   1 
ATOM   2954 O O   A ALA   B 2 123 ? -11.880 8.119   -16.577 0.22 30.84  ? 132 ALA   B O   1 
ATOM   2955 O O   B ALA   B 2 123 ? -11.880 8.119   -16.577 0.22 30.84  ? 132 ALA   B O   1 
ATOM   2956 O O   C ALA   B 2 123 ? -12.697 7.437   -17.003 0.28 31.12  ? 132 ALA   B O   1 
ATOM   2957 O O   D ALA   B 2 123 ? -12.697 7.437   -17.002 0.28 31.14  ? 132 ALA   B O   1 
ATOM   2958 C CB  A ALA   B 2 123 ? -8.925  9.572   -16.640 0.22 34.57  ? 132 ALA   B CB  1 
ATOM   2959 C CB  B ALA   B 2 123 ? -8.925  9.572   -16.640 0.22 34.56  ? 132 ALA   B CB  1 
ATOM   2960 C CB  C ALA   B 2 123 ? -9.646  8.431   -16.653 0.28 34.65  ? 132 ALA   B CB  1 
ATOM   2961 C CB  D ALA   B 2 123 ? -9.646  8.431   -16.652 0.28 34.66  ? 132 ALA   B CB  1 
ATOM   2962 N N   A GLY   B 2 124 ? -11.882 9.986   -17.897 0.22 29.50  ? 133 GLY   B N   1 
ATOM   2963 N N   B GLY   B 2 124 ? -11.882 9.986   -17.897 0.22 29.50  ? 133 GLY   B N   1 
ATOM   2964 N N   C GLY   B 2 124 ? -12.369 9.276   -18.330 0.28 34.70  ? 133 GLY   B N   1 
ATOM   2965 N N   D GLY   B 2 124 ? -12.369 9.276   -18.329 0.28 34.70  ? 133 GLY   B N   1 
ATOM   2966 C CA  A GLY   B 2 124 ? -13.320 10.273  -17.731 0.22 27.37  ? 133 GLY   B CA  1 
ATOM   2967 C CA  B GLY   B 2 124 ? -13.320 10.273  -17.732 0.22 27.38  ? 133 GLY   B CA  1 
ATOM   2968 C CA  C GLY   B 2 124 ? -13.771 9.736   -18.391 0.28 34.64  ? 133 GLY   B CA  1 
ATOM   2969 C CA  D GLY   B 2 124 ? -13.771 9.736   -18.391 0.28 34.63  ? 133 GLY   B CA  1 
ATOM   2970 C C   A GLY   B 2 124 ? -14.213 9.236   -18.405 0.22 27.09  ? 133 GLY   B C   1 
ATOM   2971 C C   B GLY   B 2 124 ? -14.213 9.236   -18.405 0.22 27.09  ? 133 GLY   B C   1 
ATOM   2972 C C   C GLY   B 2 124 ? -14.693 8.696   -19.009 0.28 33.43  ? 133 GLY   B C   1 
ATOM   2973 C C   D GLY   B 2 124 ? -14.693 8.696   -19.009 0.28 33.43  ? 133 GLY   B C   1 
ATOM   2974 O O   A GLY   B 2 124 ? -15.442 9.387   -18.282 0.22 24.47  ? 133 GLY   B O   1 
ATOM   2975 O O   B GLY   B 2 124 ? -15.442 9.387   -18.282 0.22 24.48  ? 133 GLY   B O   1 
ATOM   2976 O O   C GLY   B 2 124 ? -15.929 8.842   -18.875 0.28 33.35  ? 133 GLY   B O   1 
ATOM   2977 O O   D GLY   B 2 124 ? -15.929 8.843   -18.875 0.28 33.35  ? 133 GLY   B O   1 
ATOM   2978 N N   A THR   B 2 125 ? -13.647 8.209   -19.065 0.22 24.82  ? 134 THR   B N   1 
ATOM   2979 N N   B THR   B 2 125 ? -13.647 8.209   -19.065 0.22 24.84  ? 134 THR   B N   1 
ATOM   2980 N N   C THR   B 2 125 ? -14.129 7.664   -19.638 0.28 30.45  ? 134 THR   B N   1 
ATOM   2981 N N   D THR   B 2 125 ? -14.129 7.664   -19.638 0.28 30.47  ? 134 THR   B N   1 
ATOM   2982 C CA  A THR   B 2 125 ? -14.404 7.137   -19.778 0.22 27.75  ? 134 THR   B CA  1 
ATOM   2983 C CA  B THR   B 2 125 ? -14.404 7.137   -19.778 0.22 27.76  ? 134 THR   B CA  1 
ATOM   2984 C CA  C THR   B 2 125 ? -14.887 6.507   -20.190 0.28 30.96  ? 134 THR   B CA  1 
ATOM   2985 C CA  D THR   B 2 125 ? -14.886 6.507   -20.190 0.28 30.97  ? 134 THR   B CA  1 
ATOM   2986 C C   A THR   B 2 125 ? -14.788 5.969   -18.837 0.22 30.22  ? 134 THR   B C   1 
ATOM   2987 C C   B THR   B 2 125 ? -14.789 5.969   -18.838 0.22 30.22  ? 134 THR   B C   1 
ATOM   2988 C C   C THR   B 2 125 ? -15.149 5.478   -19.075 0.28 32.47  ? 134 THR   B C   1 
ATOM   2989 C C   D THR   B 2 125 ? -15.148 5.478   -19.075 0.28 32.48  ? 134 THR   B C   1 
ATOM   2990 O O   A THR   B 2 125 ? -15.591 5.128   -19.283 0.22 31.54  ? 134 THR   B O   1 
ATOM   2991 O O   B THR   B 2 125 ? -15.591 5.128   -19.283 0.22 31.54  ? 134 THR   B O   1 
ATOM   2992 O O   C THR   B 2 125 ? -16.015 4.588   -19.286 0.28 32.83  ? 134 THR   B O   1 
ATOM   2993 O O   D THR   B 2 125 ? -16.014 4.588   -19.286 0.28 32.83  ? 134 THR   B O   1 
ATOM   2994 C CB  A THR   B 2 125 ? -13.609 6.674   -21.010 0.22 27.76  ? 134 THR   B CB  1 
ATOM   2995 C CB  B THR   B 2 125 ? -13.609 6.674   -21.010 0.22 27.76  ? 134 THR   B CB  1 
ATOM   2996 C CB  C THR   B 2 125 ? -14.165 5.942   -21.423 0.28 31.83  ? 134 THR   B CB  1 
ATOM   2997 C CB  D THR   B 2 125 ? -14.165 5.942   -21.422 0.28 31.83  ? 134 THR   B CB  1 
ATOM   2998 O OG1 A THR   B 2 125 ? -13.078 7.842   -21.637 0.22 29.49  ? 134 THR   B OG1 1 
ATOM   2999 O OG1 B THR   B 2 125 ? -13.078 7.842   -21.637 0.22 29.48  ? 134 THR   B OG1 1 
ATOM   3000 O OG1 C THR   B 2 125 ? -13.744 7.021   -22.256 0.28 30.08  ? 134 THR   B OG1 1 
ATOM   3001 O OG1 D THR   B 2 125 ? -13.743 7.021   -22.256 0.28 30.10  ? 134 THR   B OG1 1 
ATOM   3002 C CG2 A THR   B 2 125 ? -14.430 5.921   -22.036 0.22 27.17  ? 134 THR   B CG2 1 
ATOM   3003 C CG2 B THR   B 2 125 ? -14.430 5.921   -22.036 0.22 27.17  ? 134 THR   B CG2 1 
ATOM   3004 C CG2 C THR   B 2 125 ? -15.043 5.042   -22.256 0.28 31.80  ? 134 THR   B CG2 1 
ATOM   3005 C CG2 D THR   B 2 125 ? -15.042 5.042   -22.256 0.28 31.80  ? 134 THR   B CG2 1 
ATOM   3006 N N   A SER   B 2 126 ? -14.278 5.910   -17.594 0.22 32.42  ? 135 SER   B N   1 
ATOM   3007 N N   B SER   B 2 126 ? -14.279 5.910   -17.594 0.22 32.42  ? 135 SER   B N   1 
ATOM   3008 N N   C SER   B 2 126 ? -14.450 5.604   -17.935 0.28 34.65  ? 135 SER   B N   1 
ATOM   3009 N N   D SER   B 2 126 ? -14.450 5.604   -17.935 0.28 34.65  ? 135 SER   B N   1 
ATOM   3010 C CA  A SER   B 2 126 ? -14.577 4.838   -16.591 0.22 34.77  ? 135 SER   B CA  1 
ATOM   3011 C CA  B SER   B 2 126 ? -14.578 4.838   -16.591 0.22 34.76  ? 135 SER   B CA  1 
ATOM   3012 C CA  C SER   B 2 126 ? -14.613 4.760   -16.719 0.28 36.89  ? 135 SER   B CA  1 
ATOM   3013 C CA  D SER   B 2 126 ? -14.613 4.760   -16.719 0.28 36.87  ? 135 SER   B CA  1 
ATOM   3014 C C   A SER   B 2 126 ? -16.092 4.621   -16.406 0.22 35.08  ? 135 SER   B C   1 
ATOM   3015 C C   B SER   B 2 126 ? -16.093 4.621   -16.406 0.22 35.07  ? 135 SER   B C   1 
ATOM   3016 C C   C SER   B 2 126 ? -16.092 4.605   -16.378 0.28 36.14  ? 135 SER   B C   1 
ATOM   3017 C C   D SER   B 2 126 ? -16.092 4.605   -16.378 0.28 36.13  ? 135 SER   B C   1 
ATOM   3018 O O   A SER   B 2 126 ? -16.813 5.632   -16.280 0.22 33.67  ? 135 SER   B O   1 
ATOM   3019 O O   B SER   B 2 126 ? -16.813 5.632   -16.281 0.22 33.67  ? 135 SER   B O   1 
ATOM   3020 O O   C SER   B 2 126 ? -16.760 5.629   -16.125 0.28 34.00  ? 135 SER   B O   1 
ATOM   3021 O O   D SER   B 2 126 ? -16.760 5.629   -16.125 0.28 34.01  ? 135 SER   B O   1 
ATOM   3022 C CB  A SER   B 2 126 ? -13.942 5.154   -15.262 0.22 35.86  ? 135 SER   B CB  1 
ATOM   3023 C CB  B SER   B 2 126 ? -13.942 5.154   -15.262 0.22 35.85  ? 135 SER   B CB  1 
ATOM   3024 C CB  C SER   B 2 126 ? -13.879 5.313   -15.537 0.28 37.61  ? 135 SER   B CB  1 
ATOM   3025 C CB  D SER   B 2 126 ? -13.879 5.313   -15.537 0.28 37.60  ? 135 SER   B CB  1 
ATOM   3026 O OG  A SER   B 2 126 ? -12.559 5.438   -15.393 0.22 35.59  ? 135 SER   B OG  1 
ATOM   3027 O OG  B SER   B 2 126 ? -12.559 5.438   -15.393 0.22 35.59  ? 135 SER   B OG  1 
ATOM   3028 O OG  C SER   B 2 126 ? -12.497 5.055   -15.638 0.28 39.43  ? 135 SER   B OG  1 
ATOM   3029 O OG  D SER   B 2 126 ? -12.496 5.055   -15.639 0.28 39.41  ? 135 SER   B OG  1 
ATOM   3030 N N   . GLY   B 2 127 ? -16.558 3.361   -16.353 1.00 34.29  ? 136 GLY   B N   1 
ATOM   3031 C CA  . GLY   B 2 127 ? -17.977 3.015   -16.117 1.00 33.88  ? 136 GLY   B CA  1 
ATOM   3032 C C   . GLY   B 2 127 ? -18.676 2.573   -17.368 1.00 32.70  ? 136 GLY   B C   1 
ATOM   3033 O O   . GLY   B 2 127 ? -19.756 1.955   -17.291 1.00 30.87  ? 136 GLY   B O   1 
ATOM   3034 N N   . SER   B 2 128 ? -18.053 2.762   -18.533 1.00 33.25  ? 137 SER   B N   1 
ATOM   3035 C CA  . SER   B 2 128 ? -18.652 2.270   -19.790 1.00 33.49  ? 137 SER   B CA  1 
ATOM   3036 C C   . SER   B 2 128 ? -18.903 0.781   -19.685 1.00 28.71  ? 137 SER   B C   1 
ATOM   3037 O O   . SER   B 2 128 ? -18.017 0.050   -19.256 1.00 34.34  ? 137 SER   B O   1 
ATOM   3038 C CB  . SER   B 2 128 ? -17.764 2.559   -20.965 1.00 34.35  ? 137 SER   B CB  1 
ATOM   3039 O OG  . SER   B 2 128 ? -17.545 3.941   -21.091 1.00 33.81  ? 137 SER   B OG  1 
ATOM   3040 N N   A PRO   B 2 129 ? -20.084 0.285   -20.103 0.22 31.26  ? 138 PRO   B N   1 
ATOM   3041 N N   B PRO   B 2 129 ? -20.084 0.285   -20.103 0.22 31.26  ? 138 PRO   B N   1 
ATOM   3042 N N   C PRO   B 2 129 ? -20.075 0.282   -20.133 0.28 30.87  ? 138 PRO   B N   1 
ATOM   3043 N N   D PRO   B 2 129 ? -20.075 0.282   -20.133 0.28 30.88  ? 138 PRO   B N   1 
ATOM   3044 C CA  A PRO   B 2 129 ? -20.378 -1.140  -20.041 0.22 31.30  ? 138 PRO   B CA  1 
ATOM   3045 C CA  B PRO   B 2 129 ? -20.378 -1.140  -20.041 0.22 31.31  ? 138 PRO   B CA  1 
ATOM   3046 C CA  C PRO   B 2 129 ? -20.403 -1.138  -20.059 0.28 30.60  ? 138 PRO   B CA  1 
ATOM   3047 C CA  D PRO   B 2 129 ? -20.403 -1.138  -20.058 0.28 30.62  ? 138 PRO   B CA  1 
ATOM   3048 C C   A PRO   B 2 129 ? -19.628 -1.970  -21.096 0.22 34.82  ? 138 PRO   B C   1 
ATOM   3049 C C   B PRO   B 2 129 ? -19.628 -1.970  -21.096 0.22 34.81  ? 138 PRO   B C   1 
ATOM   3050 C C   C PRO   B 2 129 ? -19.828 -2.046  -21.161 0.28 34.61  ? 138 PRO   B C   1 
ATOM   3051 C C   D PRO   B 2 129 ? -19.828 -2.046  -21.161 0.28 34.59  ? 138 PRO   B C   1 
ATOM   3052 O O   A PRO   B 2 129 ? -19.275 -1.440  -22.157 0.22 33.86  ? 138 PRO   B O   1 
ATOM   3053 O O   B PRO   B 2 129 ? -19.276 -1.441  -22.157 0.22 33.85  ? 138 PRO   B O   1 
ATOM   3054 O O   C PRO   B 2 129 ? -19.853 -1.682  -22.343 0.28 31.82  ? 138 PRO   B O   1 
ATOM   3055 O O   D PRO   B 2 129 ? -19.853 -1.681  -22.343 0.28 31.83  ? 138 PRO   B O   1 
ATOM   3056 C CB  A PRO   B 2 129 ? -21.891 -1.212  -20.286 0.22 32.27  ? 138 PRO   B CB  1 
ATOM   3057 C CB  B PRO   B 2 129 ? -21.891 -1.212  -20.286 0.22 32.27  ? 138 PRO   B CB  1 
ATOM   3058 C CB  C PRO   B 2 129 ? -21.928 -1.136  -20.206 0.28 32.10  ? 138 PRO   B CB  1 
ATOM   3059 C CB  D PRO   B 2 129 ? -21.928 -1.136  -20.206 0.28 32.09  ? 138 PRO   B CB  1 
ATOM   3060 C CG  A PRO   B 2 129 ? -22.215 0.029   -21.097 0.22 30.91  ? 138 PRO   B CG  1 
ATOM   3061 C CG  B PRO   B 2 129 ? -22.215 0.029   -21.097 0.22 30.92  ? 138 PRO   B CG  1 
ATOM   3062 C CG  C PRO   B 2 129 ? -22.222 0.053   -21.099 0.28 30.28  ? 138 PRO   B CG  1 
ATOM   3063 C CG  D PRO   B 2 129 ? -22.222 0.053   -21.099 0.28 30.29  ? 138 PRO   B CG  1 
ATOM   3064 C CD  A PRO   B 2 129 ? -21.203 1.068   -20.661 0.22 31.23  ? 138 PRO   B CD  1 
ATOM   3065 C CD  B PRO   B 2 129 ? -21.203 1.068   -20.661 0.22 31.24  ? 138 PRO   B CD  1 
ATOM   3066 C CD  C PRO   B 2 129 ? -21.172 1.076   -20.722 0.28 30.68  ? 138 PRO   B CD  1 
ATOM   3067 C CD  D PRO   B 2 129 ? -21.172 1.076   -20.722 0.28 30.68  ? 138 PRO   B CD  1 
ATOM   3068 N N   . ILE   B 2 130 ? -19.388 -3.239  -20.754 1.00 33.59  ? 139 ILE   B N   1 
ATOM   3069 C CA  . ILE   B 2 130 ? -18.876 -4.288  -21.673 1.00 35.74  ? 139 ILE   B CA  1 
ATOM   3070 C C   . ILE   B 2 130 ? -20.064 -5.210  -21.853 1.00 30.18  ? 139 ILE   B C   1 
ATOM   3071 O O   . ILE   B 2 130 ? -20.665 -5.533  -20.828 1.00 33.67  ? 139 ILE   B O   1 
ATOM   3072 C CB  . ILE   B 2 130 ? -17.677 -5.017  -21.063 1.00 35.26  ? 139 ILE   B CB  1 
ATOM   3073 C CG1 . ILE   B 2 130 ? -16.508 -4.074  -20.794 1.00 37.12  ? 139 ILE   B CG1 1 
ATOM   3074 C CG2 . ILE   B 2 130 ? -17.274 -6.206  -21.930 1.00 41.70  ? 139 ILE   B CG2 1 
ATOM   3075 C CD1 . ILE   B 2 130 ? -15.717 -4.518  -19.610 1.00 41.21  ? 139 ILE   B CD1 1 
ATOM   3076 N N   . LEU   B 2 131 ? -20.386 -5.604  -23.091 1.00 36.45  ? 140 LEU   B N   1 
ATOM   3077 C CA  . LEU   B 2 131 ? -21.552 -6.464  -23.398 1.00 36.75  ? 140 LEU   B CA  1 
ATOM   3078 C C   . LEU   B 2 131 ? -21.156 -7.776  -24.069 1.00 37.66  ? 140 LEU   B C   1 
ATOM   3079 O O   . LEU   B 2 131 ? -20.163 -7.793  -24.805 1.00 46.97  ? 140 LEU   B O   1 
ATOM   3080 C CB  . LEU   B 2 131 ? -22.450 -5.748  -24.411 1.00 47.55  ? 140 LEU   B CB  1 
ATOM   3081 C CG  . LEU   B 2 131 ? -22.701 -4.270  -24.178 1.00 49.16  ? 140 LEU   B CG  1 
ATOM   3082 C CD1 . LEU   B 2 131 ? -23.573 -3.713  -25.306 1.00 55.27  ? 140 LEU   B CD1 1 
ATOM   3083 C CD2 . LEU   B 2 131 ? -23.343 -4.084  -22.807 1.00 48.08  ? 140 LEU   B CD2 1 
ATOM   3084 N N   . ASP   B 2 132 ? -22.035 -8.747  -23.923 1.00 39.41  ? 141 ASP   B N   1 
ATOM   3085 C CA  . ASP   B 2 132 ? -22.047 -10.030 -24.665 1.00 51.13  ? 141 ASP   B CA  1 
ATOM   3086 C C   . ASP   B 2 132 ? -23.008 -9.925  -25.852 1.00 56.10  ? 141 ASP   B C   1 
ATOM   3087 O O   . ASP   B 2 132 ? -23.649 -8.850  -26.020 1.00 58.48  ? 141 ASP   B O   1 
ATOM   3088 C CB  . ASP   B 2 132 ? -22.437 -11.189 -23.745 1.00 44.26  ? 141 ASP   B CB  1 
ATOM   3089 C CG  . ASP   B 2 132 ? -23.870 -11.208 -23.269 1.00 48.50  ? 141 ASP   B CG  1 
ATOM   3090 O OD1 . ASP   B 2 132 ? -24.684 -10.398 -23.751 1.00 45.92  ? 141 ASP   B OD1 1 
ATOM   3091 O OD2 . ASP   B 2 132 ? -24.162 -12.049 -22.400 1.00 52.52  ? 141 ASP   B OD2 1 
ATOM   3092 N N   . LYS   B 2 133 ? -23.166 -11.040 -26.574 1.00 60.61  ? 142 LYS   B N   1 
ATOM   3093 C CA  . LYS   B 2 133 ? -23.771 -11.106 -27.932 1.00 64.43  ? 142 LYS   B CA  1 
ATOM   3094 C C   . LYS   B 2 133 ? -25.261 -10.796 -27.827 1.00 59.48  ? 142 LYS   B C   1 
ATOM   3095 O O   . LYS   B 2 133 ? -25.849 -10.495 -28.845 1.00 51.89  ? 142 LYS   B O   1 
ATOM   3096 C CB  . LYS   B 2 133 ? -23.486 -12.462 -28.601 1.00 67.25  ? 142 LYS   B CB  1 
ATOM   3097 C CG  . LYS   B 2 133 ? -22.131 -12.531 -29.308 1.00 74.83  ? 142 LYS   B CG  1 
ATOM   3098 C CD  . LYS   B 2 133 ? -21.435 -13.886 -29.344 1.00 79.69  ? 142 LYS   B CD  1 
ATOM   3099 C CE  . LYS   B 2 133 ? -20.007 -13.766 -29.846 1.00 85.61  ? 142 LYS   B CE  1 
ATOM   3100 N NZ  . LYS   B 2 133 ? -19.416 -15.066 -30.258 1.00 85.82  ? 142 LYS   B NZ  1 
ATOM   3101 N N   . CYS   B 2 134 ? -25.822 -10.869 -26.620 1.00 55.90  ? 143 CYS   B N   1 
ATOM   3102 C CA  . CYS   B 2 134 ? -27.264 -10.682 -26.349 1.00 55.44  ? 143 CYS   B CA  1 
ATOM   3103 C C   . CYS   B 2 134 ? -27.566 -9.291  -25.766 1.00 47.27  ? 143 CYS   B C   1 
ATOM   3104 O O   . CYS   B 2 134 ? -28.704 -9.046  -25.400 1.00 46.99  ? 143 CYS   B O   1 
ATOM   3105 C CB  . CYS   B 2 134 ? -27.723 -11.775 -25.402 1.00 66.75  ? 143 CYS   B CB  1 
ATOM   3106 S SG  . CYS   B 2 134 ? -27.609 -13.404 -26.173 1.00 69.44  ? 143 CYS   B SG  1 
ATOM   3107 N N   A GLY   B 2 135 ? -26.550 -8.426  -25.679 0.22 47.23  ? 144 GLY   B N   1 
ATOM   3108 N N   B GLY   B 2 135 ? -26.550 -8.426  -25.679 0.22 47.23  ? 144 GLY   B N   1 
ATOM   3109 N N   C GLY   B 2 135 ? -26.563 -8.409  -25.741 0.28 47.35  ? 144 GLY   B N   1 
ATOM   3110 N N   D GLY   B 2 135 ? -26.562 -8.409  -25.741 0.28 47.35  ? 144 GLY   B N   1 
ATOM   3111 C CA  A GLY   B 2 135 ? -26.663 -7.045  -25.172 0.22 47.01  ? 144 GLY   B CA  1 
ATOM   3112 C CA  B GLY   B 2 135 ? -26.663 -7.045  -25.172 0.22 47.00  ? 144 GLY   B CA  1 
ATOM   3113 C CA  C GLY   B 2 135 ? -26.651 -7.054  -25.166 0.28 47.56  ? 144 GLY   B CA  1 
ATOM   3114 C CA  D GLY   B 2 135 ? -26.651 -7.054  -25.166 0.28 47.55  ? 144 GLY   B CA  1 
ATOM   3115 C C   A GLY   B 2 135 ? -26.528 -6.951  -23.657 0.22 43.86  ? 144 GLY   B C   1 
ATOM   3116 C C   B GLY   B 2 135 ? -26.528 -6.951  -23.656 0.22 43.87  ? 144 GLY   B C   1 
ATOM   3117 C C   C GLY   B 2 135 ? -26.863 -7.086  -23.659 0.28 43.91  ? 144 GLY   B C   1 
ATOM   3118 C C   D GLY   B 2 135 ? -26.864 -7.087  -23.659 0.28 43.93  ? 144 GLY   B C   1 
ATOM   3119 O O   A GLY   B 2 135 ? -26.575 -5.814  -23.145 0.22 43.12  ? 144 GLY   B O   1 
ATOM   3120 O O   B GLY   B 2 135 ? -26.577 -5.814  -23.145 0.22 43.14  ? 144 GLY   B O   1 
ATOM   3121 O O   C GLY   B 2 135 ? -27.603 -6.227  -23.157 0.28 44.91  ? 144 GLY   B O   1 
ATOM   3122 O O   D GLY   B 2 135 ? -27.605 -6.228  -23.157 0.28 44.92  ? 144 GLY   B O   1 
ATOM   3123 N N   . ARG   B 2 136 ? -26.286 -8.076  -22.969 1.00 46.85  ? 145 ARG   B N   1 
ATOM   3124 C CA  . ARG   B 2 136 ? -26.304 -8.141  -21.471 1.00 42.86  ? 145 ARG   B CA  1 
ATOM   3125 C C   . ARG   B 2 136 ? -25.003 -7.531  -20.963 1.00 44.33  ? 145 ARG   B C   1 
ATOM   3126 O O   . ARG   B 2 136 ? -23.952 -7.729  -21.656 1.00 40.47  ? 145 ARG   B O   1 
ATOM   3127 C CB  . ARG   B 2 136 ? -26.580 -9.566  -21.013 1.00 46.41  ? 145 ARG   B CB  1 
ATOM   3128 C CG  . ARG   B 2 136 ? -27.983 -10.026 -21.353 1.00 52.30  ? 145 ARG   B CG  1 
ATOM   3129 C CD  . ARG   B 2 136 ? -28.297 -11.393 -20.801 1.00 58.97  ? 145 ARG   B CD  1 
ATOM   3130 N NE  . ARG   B 2 136 ? -27.368 -12.318 -21.435 1.00 74.42  ? 145 ARG   B NE  1 
ATOM   3131 C CZ  . ARG   B 2 136 ? -26.883 -13.443 -20.912 1.00 73.09  ? 145 ARG   B CZ  1 
ATOM   3132 N NH1 . ARG   B 2 136 ? -27.205 -13.853 -19.692 1.00 68.57  ? 145 ARG   B NH1 1 
ATOM   3133 N NH2 . ARG   B 2 136 ? -26.044 -14.153 -21.641 1.00 81.76  ? 145 ARG   B NH2 1 
ATOM   3134 N N   . VAL   B 2 137 ? -25.049 -6.746  -19.867 1.00 35.22  ? 146 VAL   B N   1 
ATOM   3135 C CA  . VAL   B 2 137 ? -23.815 -6.093  -19.333 1.00 35.52  ? 146 VAL   B CA  1 
ATOM   3136 C C   . VAL   B 2 137 ? -23.121 -7.169  -18.484 1.00 38.40  ? 146 VAL   B C   1 
ATOM   3137 O O   . VAL   B 2 137 ? -23.727 -7.661  -17.495 1.00 36.36  ? 146 VAL   B O   1 
ATOM   3138 C CB  . VAL   B 2 137 ? -24.049 -4.794  -18.542 1.00 31.96  ? 146 VAL   B CB  1 
ATOM   3139 C CG1 . VAL   B 2 137 ? -22.754 -4.151  -18.065 1.00 32.15  ? 146 VAL   B CG1 1 
ATOM   3140 C CG2 . VAL   B 2 137 ? -24.817 -3.769  -19.366 1.00 41.32  ? 146 VAL   B CG2 1 
ATOM   3141 N N   . ILE   B 2 138 ? -21.937 -7.559  -18.913 1.00 38.61  ? 147 ILE   B N   1 
ATOM   3142 C CA  . ILE   B 2 138 ? -21.071 -8.566  -18.226 1.00 39.98  ? 147 ILE   B CA  1 
ATOM   3143 C C   . ILE   B 2 138 ? -20.051 -7.846  -17.317 1.00 35.85  ? 147 ILE   B C   1 
ATOM   3144 O O   . ILE   B 2 138 ? -19.268 -8.562  -16.612 1.00 34.13  ? 147 ILE   B O   1 
ATOM   3145 C CB  . ILE   B 2 138 ? -20.367 -9.454  -19.281 1.00 35.49  ? 147 ILE   B CB  1 
ATOM   3146 C CG1 . ILE   B 2 138 ? -19.536 -8.627  -20.267 1.00 38.11  ? 147 ILE   B CG1 1 
ATOM   3147 C CG2 . ILE   B 2 138 ? -21.363 -10.339 -19.967 1.00 33.13  ? 147 ILE   B CG2 1 
ATOM   3148 C CD1 . ILE   B 2 138 ? -18.546 -9.433  -21.073 1.00 43.39  ? 147 ILE   B CD1 1 
ATOM   3149 N N   . GLY   B 2 139 ? -20.025 -6.515  -17.302 1.00 32.80  ? 148 GLY   B N   1 
ATOM   3150 C CA  . GLY   B 2 139 ? -19.130 -5.740  -16.414 1.00 33.73  ? 148 GLY   B CA  1 
ATOM   3151 C C   . GLY   B 2 139 ? -18.906 -4.330  -16.874 1.00 35.40  ? 148 GLY   B C   1 
ATOM   3152 O O   . GLY   B 2 139 ? -19.414 -3.997  -17.953 1.00 37.77  ? 148 GLY   B O   1 
ATOM   3153 N N   . LEU   B 2 140 ? -18.100 -3.574  -16.132 1.00 34.69  ? 149 LEU   B N   1 
ATOM   3154 C CA  . LEU   B 2 140 ? -17.723 -2.177  -16.420 1.00 31.62  ? 149 LEU   B CA  1 
ATOM   3155 C C   . LEU   B 2 140 ? -16.224 -2.036  -16.662 1.00 36.36  ? 149 LEU   B C   1 
ATOM   3156 O O   . LEU   B 2 140 ? -15.388 -2.700  -15.981 1.00 34.20  ? 149 LEU   B O   1 
ATOM   3157 C CB  . LEU   B 2 140 ? -18.148 -1.236  -15.277 1.00 32.37  ? 149 LEU   B CB  1 
ATOM   3158 C CG  . LEU   B 2 140 ? -19.619 -1.292  -14.854 1.00 32.93  ? 149 LEU   B CG  1 
ATOM   3159 C CD1 . LEU   B 2 140 ? -19.939 -0.181  -13.854 1.00 35.85  ? 149 LEU   B CD1 1 
ATOM   3160 C CD2 . LEU   B 2 140 ? -20.582 -1.281  -16.028 1.00 36.05  ? 149 LEU   B CD2 1 
ATOM   3161 N N   . TYR   B 2 141 ? -15.909 -1.086  -17.535 1.00 32.04  ? 150 TYR   B N   1 
ATOM   3162 C CA  . TYR   B 2 141 ? -14.547 -0.713  -17.987 1.00 30.46  ? 150 TYR   B CA  1 
ATOM   3163 C C   . TYR   B 2 141 ? -14.052 0.408   -17.119 1.00 32.21  ? 150 TYR   B C   1 
ATOM   3164 O O   . TYR   B 2 141 ? -14.828 1.306   -16.862 1.00 38.20  ? 150 TYR   B O   1 
ATOM   3165 C CB  . TYR   B 2 141 ? -14.613 -0.246  -19.467 1.00 35.12  ? 150 TYR   B CB  1 
ATOM   3166 C CG  . TYR   B 2 141 ? -13.359 0.414   -20.021 1.00 37.31  ? 150 TYR   B CG  1 
ATOM   3167 C CD1 . TYR   B 2 141 ? -13.160 1.783   -19.958 1.00 37.84  ? 150 TYR   B CD1 1 
ATOM   3168 C CD2 . TYR   B 2 141 ? -12.333 -0.351  -20.583 1.00 43.45  ? 150 TYR   B CD2 1 
ATOM   3169 C CE1 . TYR   B 2 141 ? -11.989 2.375   -20.418 1.00 42.32  ? 150 TYR   B CE1 1 
ATOM   3170 C CE2 . TYR   B 2 141 ? -11.180 0.226   -21.101 1.00 36.93  ? 150 TYR   B CE2 1 
ATOM   3171 C CZ  . TYR   B 2 141 ? -10.999 1.595   -21.028 1.00 46.61  ? 150 TYR   B CZ  1 
ATOM   3172 O OH  . TYR   B 2 141 ? -9.825  2.157   -21.494 1.00 50.19  ? 150 TYR   B OH  1 
ATOM   3173 N N   A GLY   B 2 142 ? -12.803 0.368   -16.636 0.22 32.08  ? 151 GLY   B N   1 
ATOM   3174 N N   B GLY   B 2 142 ? -12.803 0.369   -16.637 0.22 32.09  ? 151 GLY   B N   1 
ATOM   3175 N N   C GLY   B 2 142 ? -12.781 0.358   -16.707 0.28 31.61  ? 151 GLY   B N   1 
ATOM   3176 N N   D GLY   B 2 142 ? -12.781 0.358   -16.707 0.28 31.63  ? 151 GLY   B N   1 
ATOM   3177 C CA  A GLY   B 2 142 ? -12.206 1.544   -15.961 0.22 33.97  ? 151 GLY   B CA  1 
ATOM   3178 C CA  B GLY   B 2 142 ? -12.206 1.545   -15.961 0.22 33.96  ? 151 GLY   B CA  1 
ATOM   3179 C CA  C GLY   B 2 142 ? -12.073 1.521   -16.129 0.28 33.83  ? 151 GLY   B CA  1 
ATOM   3180 C CA  D GLY   B 2 142 ? -12.073 1.521   -16.129 0.28 33.82  ? 151 GLY   B CA  1 
ATOM   3181 C C   A GLY   B 2 142 ? -11.234 1.242   -14.828 0.22 33.96  ? 151 GLY   B C   1 
ATOM   3182 C C   B GLY   B 2 142 ? -11.234 1.242   -14.828 0.22 33.96  ? 151 GLY   B C   1 
ATOM   3183 C C   C GLY   B 2 142 ? -11.292 1.226   -14.858 0.28 34.36  ? 151 GLY   B C   1 
ATOM   3184 C C   D GLY   B 2 142 ? -11.292 1.226   -14.858 0.28 34.36  ? 151 GLY   B C   1 
ATOM   3185 O O   A GLY   B 2 142 ? -10.508 2.183   -14.442 0.22 35.10  ? 151 GLY   B O   1 
ATOM   3186 O O   B GLY   B 2 142 ? -10.508 2.183   -14.442 0.22 35.09  ? 151 GLY   B O   1 
ATOM   3187 O O   C GLY   B 2 142 ? -10.779 2.191   -14.274 0.28 36.64  ? 151 GLY   B O   1 
ATOM   3188 O O   D GLY   B 2 142 ? -10.779 2.191   -14.274 0.28 36.63  ? 151 GLY   B O   1 
ATOM   3189 N N   A ASN   B 2 143 ? -11.193 0.014   -14.298 0.22 33.45  ? 152 ASN   B N   1 
ATOM   3190 N N   B ASN   B 2 143 ? -11.193 0.014   -14.298 0.22 33.45  ? 152 ASN   B N   1 
ATOM   3191 N N   C ASN   B 2 143 ? -11.166 -0.042  -14.453 0.28 33.80  ? 152 ASN   B N   1 
ATOM   3192 N N   D ASN   B 2 143 ? -11.166 -0.042  -14.453 0.28 33.80  ? 152 ASN   B N   1 
ATOM   3193 C CA  A ASN   B 2 143 ? -10.185 -0.392  -13.276 0.22 34.10  ? 152 ASN   B CA  1 
ATOM   3194 C CA  B ASN   B 2 143 ? -10.186 -0.392  -13.277 0.22 34.09  ? 152 ASN   B CA  1 
ATOM   3195 C CA  C ASN   B 2 143 ? -10.254 -0.468  -13.356 0.28 34.47  ? 152 ASN   B CA  1 
ATOM   3196 C CA  D ASN   B 2 143 ? -10.254 -0.468  -13.356 0.28 34.46  ? 152 ASN   B CA  1 
ATOM   3197 C C   A ASN   B 2 143 ? -9.320  -1.535  -13.825 0.22 31.71  ? 152 ASN   B C   1 
ATOM   3198 C C   B ASN   B 2 143 ? -9.320  -1.535  -13.825 0.22 31.72  ? 152 ASN   B C   1 
ATOM   3199 C C   C ASN   B 2 143 ? -9.315  -1.571  -13.856 0.28 31.25  ? 152 ASN   B C   1 
ATOM   3200 C C   D ASN   B 2 143 ? -9.315  -1.571  -13.856 0.28 31.28  ? 152 ASN   B C   1 
ATOM   3201 O O   A ASN   B 2 143 ? -9.865  -2.619  -14.096 0.22 31.90  ? 152 ASN   B O   1 
ATOM   3202 O O   B ASN   B 2 143 ? -9.865  -2.619  -14.096 0.22 31.91  ? 152 ASN   B O   1 
ATOM   3203 O O   C ASN   B 2 143 ? -9.805  -2.681  -14.110 0.28 32.31  ? 152 ASN   B O   1 
ATOM   3204 O O   D ASN   B 2 143 ? -9.805  -2.681  -14.110 0.28 32.32  ? 152 ASN   B O   1 
ATOM   3205 C CB  A ASN   B 2 143 ? -10.823 -0.801  -11.947 0.22 32.99  ? 152 ASN   B CB  1 
ATOM   3206 C CB  B ASN   B 2 143 ? -10.824 -0.800  -11.948 0.22 32.99  ? 152 ASN   B CB  1 
ATOM   3207 C CB  C ASN   B 2 143 ? -11.013 -0.985  -12.136 0.28 32.80  ? 152 ASN   B CB  1 
ATOM   3208 C CB  D ASN   B 2 143 ? -11.013 -0.985  -12.136 0.28 32.81  ? 152 ASN   B CB  1 
ATOM   3209 C CG  A ASN   B 2 143 ? -9.892  -0.633  -10.762 0.22 33.35  ? 152 ASN   B CG  1 
ATOM   3210 C CG  B ASN   B 2 143 ? -9.893  -0.633  -10.762 0.22 33.35  ? 152 ASN   B CG  1 
ATOM   3211 C CG  C ASN   B 2 143 ? -10.122 -1.097  -10.919 0.28 32.75  ? 152 ASN   B CG  1 
ATOM   3212 C CG  D ASN   B 2 143 ? -10.122 -1.097  -10.919 0.28 32.75  ? 152 ASN   B CG  1 
ATOM   3213 O OD1 A ASN   B 2 143 ? -9.007  0.225   -10.762 0.22 32.50  ? 152 ASN   B OD1 1 
ATOM   3214 O OD1 B ASN   B 2 143 ? -9.007  0.226   -10.762 0.22 32.50  ? 152 ASN   B OD1 1 
ATOM   3215 O OD1 C ASN   B 2 143 ? -9.134  -0.367  -10.790 0.28 35.48  ? 152 ASN   B OD1 1 
ATOM   3216 O OD1 D ASN   B 2 143 ? -9.135  -0.367  -10.789 0.28 35.46  ? 152 ASN   B OD1 1 
ATOM   3217 N ND2 A ASN   B 2 143 ? -10.089 -1.444  -9.734  0.22 31.51  ? 152 ASN   B ND2 1 
ATOM   3218 N ND2 B ASN   B 2 143 ? -10.089 -1.444  -9.734  0.22 31.52  ? 152 ASN   B ND2 1 
ATOM   3219 N ND2 C ASN   B 2 143 ? -10.469 -1.995  -10.013 0.28 30.63  ? 152 ASN   B ND2 1 
ATOM   3220 N ND2 D ASN   B 2 143 ? -10.469 -1.995  -10.013 0.28 30.65  ? 152 ASN   B ND2 1 
ATOM   3221 N N   . GLY   B 2 144 ? -8.026  -1.267  -13.978 1.00 33.41  ? 153 GLY   B N   1 
ATOM   3222 C CA  . GLY   B 2 144 ? -7.011  -2.264  -14.382 1.00 37.67  ? 153 GLY   B CA  1 
ATOM   3223 C C   . GLY   B 2 144 ? -5.629  -1.675  -14.245 1.00 42.85  ? 153 GLY   B C   1 
ATOM   3224 O O   . GLY   B 2 144 ? -5.354  -0.975  -13.220 1.00 42.77  ? 153 GLY   B O   1 
ATOM   3225 N N   . VAL   B 2 145 ? -4.799  -1.855  -15.276 1.00 42.97  ? 154 VAL   B N   1 
ATOM   3226 C CA  . VAL   B 2 145 ? -3.327  -1.735  -15.121 1.00 44.02  ? 154 VAL   B CA  1 
ATOM   3227 C C   . VAL   B 2 145 ? -2.676  -1.152  -16.402 1.00 48.26  ? 154 VAL   B C   1 
ATOM   3228 O O   . VAL   B 2 145 ? -3.150  -1.438  -17.534 1.00 44.07  ? 154 VAL   B O   1 
ATOM   3229 C CB  . VAL   B 2 145 ? -2.847  -3.150  -14.722 1.00 47.74  ? 154 VAL   B CB  1 
ATOM   3230 C CG1 . VAL   B 2 145 ? -2.632  -4.068  -15.908 1.00 42.48  ? 154 VAL   B CG1 1 
ATOM   3231 C CG2 . VAL   B 2 145 ? -1.636  -3.108  -13.817 1.00 53.64  ? 154 VAL   B CG2 1 
ATOM   3232 N N   A VAL   B 2 146 ? -1.627  -0.341  -16.221 0.22 48.85  ? 155 VAL   B N   1 
ATOM   3233 N N   B VAL   B 2 146 ? -1.627  -0.341  -16.221 0.22 48.86  ? 155 VAL   B N   1 
ATOM   3234 N N   C VAL   B 2 146 ? -1.623  -0.352  -16.217 0.28 51.02  ? 155 VAL   B N   1 
ATOM   3235 N N   D VAL   B 2 146 ? -1.623  -0.352  -16.217 0.28 51.02  ? 155 VAL   B N   1 
ATOM   3236 C CA  A VAL   B 2 146 ? -0.778  0.230   -17.313 0.22 51.15  ? 155 VAL   B CA  1 
ATOM   3237 C CA  B VAL   B 2 146 ? -0.778  0.230   -17.311 0.22 51.16  ? 155 VAL   B CA  1 
ATOM   3238 C CA  C VAL   B 2 146 ? -0.704  0.115   -17.299 0.28 54.93  ? 155 VAL   B CA  1 
ATOM   3239 C CA  D VAL   B 2 146 ? -0.704  0.115   -17.298 0.28 54.93  ? 155 VAL   B CA  1 
ATOM   3240 C C   A VAL   B 2 146 ? 0.375   -0.750  -17.583 0.22 53.24  ? 155 VAL   B C   1 
ATOM   3241 C C   B VAL   B 2 146 ? 0.375   -0.749  -17.583 0.22 53.24  ? 155 VAL   B C   1 
ATOM   3242 C C   C VAL   B 2 146 ? 0.370   -0.965  -17.507 0.28 57.68  ? 155 VAL   B C   1 
ATOM   3243 C C   D VAL   B 2 146 ? 0.369   -0.965  -17.506 0.28 57.67  ? 155 VAL   B C   1 
ATOM   3244 O O   A VAL   B 2 146 ? 1.157   -0.997  -16.646 0.22 53.70  ? 155 VAL   B O   1 
ATOM   3245 O O   B VAL   B 2 146 ? 1.157   -0.997  -16.645 0.22 53.70  ? 155 VAL   B O   1 
ATOM   3246 O O   C VAL   B 2 146 ? 0.957   -1.402  -16.497 0.28 58.73  ? 155 VAL   B O   1 
ATOM   3247 O O   D VAL   B 2 146 ? 0.956   -1.403  -16.496 0.28 58.73  ? 155 VAL   B O   1 
ATOM   3248 C CB  A VAL   B 2 146 ? -0.284  1.638   -16.925 0.22 51.27  ? 155 VAL   B CB  1 
ATOM   3249 C CB  B VAL   B 2 146 ? -0.283  1.639   -16.924 0.22 51.27  ? 155 VAL   B CB  1 
ATOM   3250 C CB  C VAL   B 2 146 ? -0.108  1.490   -16.938 0.28 56.23  ? 155 VAL   B CB  1 
ATOM   3251 C CB  D VAL   B 2 146 ? -0.108  1.490   -16.937 0.28 56.22  ? 155 VAL   B CB  1 
ATOM   3252 C CG1 A VAL   B 2 146 ? 0.710   2.200   -17.927 0.22 52.50  ? 155 VAL   B CG1 1 
ATOM   3253 C CG1 B VAL   B 2 146 ? 0.710   2.200   -17.927 0.22 52.49  ? 155 VAL   B CG1 1 
ATOM   3254 C CG1 C VAL   B 2 146 ? 0.902   1.967   -17.967 0.28 59.26  ? 155 VAL   B CG1 1 
ATOM   3255 C CG1 D VAL   B 2 146 ? 0.902   1.966   -17.966 0.28 59.23  ? 155 VAL   B CG1 1 
ATOM   3256 C CG2 A VAL   B 2 146 ? -1.449  2.600   -16.738 0.22 51.88  ? 155 VAL   B CG2 1 
ATOM   3257 C CG2 B VAL   B 2 146 ? -1.448  2.601   -16.738 0.22 51.87  ? 155 VAL   B CG2 1 
ATOM   3258 C CG2 C VAL   B 2 146 ? -1.199  2.533   -16.744 0.28 57.30  ? 155 VAL   B CG2 1 
ATOM   3259 C CG2 D VAL   B 2 146 ? -1.198  2.533   -16.743 0.28 57.29  ? 155 VAL   B CG2 1 
ATOM   3260 N N   A ILE   B 2 147 ? 0.478   -1.280  -18.812 0.22 55.66  ? 156 ILE   B N   1 
ATOM   3261 N N   B ILE   B 2 147 ? 0.479   -1.279  -18.812 0.22 55.66  ? 156 ILE   B N   1 
ATOM   3262 N N   C ILE   B 2 147 ? 0.600   -1.396  -18.755 0.28 60.90  ? 156 ILE   B N   1 
ATOM   3263 N N   D ILE   B 2 147 ? 0.600   -1.395  -18.755 0.28 60.90  ? 156 ILE   B N   1 
ATOM   3264 C CA  A ILE   B 2 147 ? 1.264   -2.518  -19.125 0.22 57.11  ? 156 ILE   B CA  1 
ATOM   3265 C CA  B ILE   B 2 147 ? 1.264   -2.516  -19.125 0.22 57.12  ? 156 ILE   B CA  1 
ATOM   3266 C CA  C ILE   B 2 147 ? 1.532   -2.520  -19.096 0.28 62.33  ? 156 ILE   B CA  1 
ATOM   3267 C CA  D ILE   B 2 147 ? 1.532   -2.519  -19.096 0.28 62.34  ? 156 ILE   B CA  1 
ATOM   3268 C C   A ILE   B 2 147 ? 2.643   -2.172  -19.702 0.22 58.72  ? 156 ILE   B C   1 
ATOM   3269 C C   B ILE   B 2 147 ? 2.643   -2.171  -19.703 0.22 58.72  ? 156 ILE   B C   1 
ATOM   3270 C C   C ILE   B 2 147 ? 2.843   -1.942  -19.640 0.28 64.89  ? 156 ILE   B C   1 
ATOM   3271 C C   D ILE   B 2 147 ? 2.843   -1.942  -19.640 0.28 64.89  ? 156 ILE   B C   1 
ATOM   3272 O O   A ILE   B 2 147 ? 2.898   -0.990  -20.004 0.22 54.88  ? 156 ILE   B O   1 
ATOM   3273 O O   B ILE   B 2 147 ? 2.897   -0.990  -20.008 0.22 54.91  ? 156 ILE   B O   1 
ATOM   3274 O O   C ILE   B 2 147 ? 2.884   -0.728  -19.910 0.28 61.67  ? 156 ILE   B O   1 
ATOM   3275 O O   D ILE   B 2 147 ? 2.884   -0.728  -19.912 0.28 61.70  ? 156 ILE   B O   1 
ATOM   3276 C CB  A ILE   B 2 147 ? 0.487   -3.473  -20.059 0.22 58.35  ? 156 ILE   B CB  1 
ATOM   3277 C CB  B ILE   B 2 147 ? 0.486   -3.471  -20.059 0.22 58.34  ? 156 ILE   B CB  1 
ATOM   3278 C CB  C ILE   B 2 147 ? 0.901   -3.532  -20.079 0.28 63.90  ? 156 ILE   B CB  1 
ATOM   3279 C CB  D ILE   B 2 147 ? 0.900   -3.530  -20.079 0.28 63.90  ? 156 ILE   B CB  1 
ATOM   3280 C CG1 A ILE   B 2 147 ? -0.039  -2.783  -21.322 0.22 58.89  ? 156 ILE   B CG1 1 
ATOM   3281 C CG1 B ILE   B 2 147 ? -0.039  -2.781  -21.322 0.22 58.88  ? 156 ILE   B CG1 1 
ATOM   3282 C CG1 C ILE   B 2 147 ? 0.234   -2.858  -21.283 0.28 64.64  ? 156 ILE   B CG1 1 
ATOM   3283 C CG1 D ILE   B 2 147 ? 0.235   -2.856  -21.284 0.28 64.63  ? 156 ILE   B CG1 1 
ATOM   3284 C CG2 A ILE   B 2 147 ? -0.627  -4.171  -19.297 0.22 58.40  ? 156 ILE   B CG2 1 
ATOM   3285 C CG2 B ILE   B 2 147 ? -0.628  -4.169  -19.296 0.22 58.40  ? 156 ILE   B CG2 1 
ATOM   3286 C CG2 C ILE   B 2 147 ? -0.063  -4.454  -19.349 0.28 62.54  ? 156 ILE   B CG2 1 
ATOM   3287 C CG2 D ILE   B 2 147 ? -0.064  -4.452  -19.350 0.28 62.54  ? 156 ILE   B CG2 1 
ATOM   3288 C CD1 A ILE   B 2 147 ? -0.300  -3.729  -22.472 0.22 58.17  ? 156 ILE   B CD1 1 
ATOM   3289 C CD1 B ILE   B 2 147 ? -0.299  -3.731  -22.470 0.22 58.18  ? 156 ILE   B CD1 1 
ATOM   3290 C CD1 C ILE   B 2 147 ? -0.053  -3.799  -22.432 0.28 63.83  ? 156 ILE   B CD1 1 
ATOM   3291 C CD1 D ILE   B 2 147 ? -0.055  -3.801  -22.430 0.28 63.83  ? 156 ILE   B CD1 1 
ATOM   3292 N N   A LYS   B 2 148 ? 3.488   -3.204  -19.831 0.22 62.67  ? 157 LYS   B N   1 
ATOM   3293 N N   B LYS   B 2 148 ? 3.488   -3.203  -19.831 0.22 62.66  ? 157 LYS   B N   1 
ATOM   3294 N N   C LYS   B 2 148 ? 3.875   -2.787  -19.770 0.28 69.73  ? 157 LYS   B N   1 
ATOM   3295 N N   D LYS   B 2 148 ? 3.875   -2.786  -19.770 0.28 69.72  ? 157 LYS   B N   1 
ATOM   3296 C CA  A LYS   B 2 148 ? 4.885   -3.174  -20.351 0.22 64.94  ? 157 LYS   B CA  1 
ATOM   3297 C CA  B LYS   B 2 148 ? 4.885   -3.173  -20.351 0.22 64.93  ? 157 LYS   B CA  1 
ATOM   3298 C CA  C LYS   B 2 148 ? 5.215   -2.405  -20.299 0.28 73.16  ? 157 LYS   B CA  1 
ATOM   3299 C CA  D LYS   B 2 148 ? 5.215   -2.405  -20.299 0.28 73.14  ? 157 LYS   B CA  1 
ATOM   3300 C C   A LYS   B 2 148 ? 5.047   -2.187  -21.518 0.22 66.57  ? 157 LYS   B C   1 
ATOM   3301 C C   B LYS   B 2 148 ? 5.048   -2.188  -21.519 0.22 66.57  ? 157 LYS   B C   1 
ATOM   3302 C C   C LYS   B 2 148 ? 5.016   -1.398  -21.433 0.28 75.21  ? 157 LYS   B C   1 
ATOM   3303 C C   D LYS   B 2 148 ? 5.017   -1.397  -21.432 0.28 75.19  ? 157 LYS   B C   1 
ATOM   3304 O O   A LYS   B 2 148 ? 6.177   -1.696  -21.696 0.22 69.84  ? 157 LYS   B O   1 
ATOM   3305 O O   B LYS   B 2 148 ? 6.178   -1.699  -21.699 0.22 69.83  ? 157 LYS   B O   1 
ATOM   3306 O O   C LYS   B 2 148 ? 5.592   -0.293  -21.352 0.28 77.89  ? 157 LYS   B O   1 
ATOM   3307 O O   D LYS   B 2 148 ? 5.593   -0.293  -21.352 0.28 77.87  ? 157 LYS   B O   1 
ATOM   3308 C CB  A LYS   B 2 148 ? 5.322   -4.581  -20.778 0.22 64.63  ? 157 LYS   B CB  1 
ATOM   3309 C CB  B LYS   B 2 148 ? 5.322   -4.581  -20.778 0.22 64.63  ? 157 LYS   B CB  1 
ATOM   3310 C CB  C LYS   B 2 148 ? 5.989   -3.633  -20.793 0.28 72.92  ? 157 LYS   B CB  1 
ATOM   3311 C CB  D LYS   B 2 148 ? 5.989   -3.633  -20.793 0.28 72.91  ? 157 LYS   B CB  1 
ATOM   3312 C CG  A LYS   B 2 148 ? 4.428   -5.278  -21.802 0.22 64.74  ? 157 LYS   B CG  1 
ATOM   3313 C CG  B LYS   B 2 148 ? 4.428   -5.278  -21.801 0.22 64.74  ? 157 LYS   B CG  1 
ATOM   3314 C CG  C LYS   B 2 148 ? 7.119   -3.337  -21.773 0.28 71.50  ? 157 LYS   B CG  1 
ATOM   3315 C CG  D LYS   B 2 148 ? 7.119   -3.337  -21.773 0.28 71.49  ? 157 LYS   B CG  1 
ATOM   3316 C CD  A LYS   B 2 148 ? 3.333   -6.155  -21.222 0.22 61.82  ? 157 LYS   B CD  1 
ATOM   3317 C CD  B LYS   B 2 148 ? 3.333   -6.155  -21.222 0.22 61.83  ? 157 LYS   B CD  1 
ATOM   3318 C CD  C LYS   B 2 148 ? 8.164   -4.429  -21.859 0.28 70.69  ? 157 LYS   B CD  1 
ATOM   3319 C CD  D LYS   B 2 148 ? 8.164   -4.429  -21.859 0.28 70.69  ? 157 LYS   B CD  1 
ATOM   3320 C CE  A LYS   B 2 148 ? 3.841   -7.261  -20.319 0.22 62.78  ? 157 LYS   B CE  1 
ATOM   3321 C CE  B LYS   B 2 148 ? 3.841   -7.261  -20.319 0.22 62.78  ? 157 LYS   B CE  1 
ATOM   3322 C CE  C LYS   B 2 148 ? 9.239   -4.304  -20.799 0.28 70.00  ? 157 LYS   B CE  1 
ATOM   3323 C CE  D LYS   B 2 148 ? 9.238   -4.305  -20.798 0.28 70.00  ? 157 LYS   B CE  1 
ATOM   3324 N NZ  A LYS   B 2 148 ? 3.610   -6.959  -18.886 0.22 60.52  ? 157 LYS   B NZ  1 
ATOM   3325 N NZ  B LYS   B 2 148 ? 3.610   -6.959  -18.886 0.22 60.53  ? 157 LYS   B NZ  1 
ATOM   3326 N NZ  C LYS   B 2 148 ? 10.006  -5.564  -20.649 0.28 67.63  ? 157 LYS   B NZ  1 
ATOM   3327 N NZ  D LYS   B 2 148 ? 10.006  -5.564  -20.649 0.28 67.64  ? 157 LYS   B NZ  1 
ATOM   3328 N N   A ASN   B 2 149 ? 3.984   -1.928  -22.289 0.22 69.51  ? 158 ASN   B N   1 
ATOM   3329 N N   B ASN   B 2 149 ? 3.984   -1.928  -22.289 0.22 69.50  ? 158 ASN   B N   1 
ATOM   3330 N N   C ASN   B 2 149 ? 4.209   -1.782  -22.426 0.28 77.14  ? 158 ASN   B N   1 
ATOM   3331 N N   D ASN   B 2 149 ? 4.210   -1.782  -22.426 0.28 77.12  ? 158 ASN   B N   1 
ATOM   3332 C CA  A ASN   B 2 149 ? 3.978   -0.984  -23.442 0.22 71.02  ? 158 ASN   B CA  1 
ATOM   3333 C CA  B ASN   B 2 149 ? 3.978   -0.984  -23.443 0.22 71.02  ? 158 ASN   B CA  1 
ATOM   3334 C CA  C ASN   B 2 149 ? 3.827   -0.957  -23.604 0.28 77.71  ? 158 ASN   B CA  1 
ATOM   3335 C CA  D ASN   B 2 149 ? 3.828   -0.957  -23.604 0.28 77.69  ? 158 ASN   B CA  1 
ATOM   3336 C C   A ASN   B 2 149 ? 3.838   0.456   -22.933 0.22 73.36  ? 158 ASN   B C   1 
ATOM   3337 C C   B ASN   B 2 149 ? 3.838   0.456   -22.933 0.22 73.36  ? 158 ASN   B C   1 
ATOM   3338 C C   C ASN   B 2 149 ? 3.627   0.496   -23.162 0.28 78.39  ? 158 ASN   B C   1 
ATOM   3339 C C   D ASN   B 2 149 ? 3.628   0.496   -23.162 0.28 78.37  ? 158 ASN   B C   1 
ATOM   3340 O O   A ASN   B 2 149 ? 4.712   1.285   -23.252 0.22 72.43  ? 158 ASN   B O   1 
ATOM   3341 O O   B ASN   B 2 149 ? 4.712   1.286   -23.253 0.22 72.44  ? 158 ASN   B O   1 
ATOM   3342 O O   C ASN   B 2 149 ? 4.232   1.388   -23.791 0.28 79.52  ? 158 ASN   B O   1 
ATOM   3343 O O   D ASN   B 2 149 ? 4.234   1.388   -23.789 0.28 79.50  ? 158 ASN   B O   1 
ATOM   3344 C CB  A ASN   B 2 149 ? 2.853   -1.298  -24.434 0.22 70.80  ? 158 ASN   B CB  1 
ATOM   3345 C CB  B ASN   B 2 149 ? 2.853   -1.298  -24.434 0.22 70.79  ? 158 ASN   B CB  1 
ATOM   3346 C CB  C ASN   B 2 149 ? 2.549   -1.462  -24.283 0.28 77.94  ? 158 ASN   B CB  1 
ATOM   3347 C CB  D ASN   B 2 149 ? 2.550   -1.462  -24.283 0.28 77.92  ? 158 ASN   B CB  1 
ATOM   3348 C CG  A ASN   B 2 149 ? 2.792   -2.757  -24.829 0.22 69.57  ? 158 ASN   B CG  1 
ATOM   3349 C CG  B ASN   B 2 149 ? 2.792   -2.758  -24.828 0.22 69.58  ? 158 ASN   B CG  1 
ATOM   3350 C CG  C ASN   B 2 149 ? 2.527   -2.956  -24.527 0.28 76.91  ? 158 ASN   B CG  1 
ATOM   3351 C CG  D ASN   B 2 149 ? 2.529   -2.956  -24.527 0.28 76.90  ? 158 ASN   B CG  1 
ATOM   3352 O OD1 A ASN   B 2 149 ? 3.793   -3.467  -24.762 0.22 71.19  ? 158 ASN   B OD1 1 
ATOM   3353 O OD1 B ASN   B 2 149 ? 3.792   -3.468  -24.759 0.22 71.19  ? 158 ASN   B OD1 1 
ATOM   3354 O OD1 C ASN   B 2 149 ? 3.324   -3.701  -23.957 0.28 78.28  ? 158 ASN   B OD1 1 
ATOM   3355 O OD1 D ASN   B 2 149 ? 3.326   -3.702  -23.959 0.28 78.27  ? 158 ASN   B OD1 1 
ATOM   3356 N ND2 A ASN   B 2 149 ? 1.620   -3.215  -25.238 0.22 69.59  ? 158 ASN   B ND2 1 
ATOM   3357 N ND2 B ASN   B 2 149 ? 1.620   -3.215  -25.237 0.22 69.59  ? 158 ASN   B ND2 1 
ATOM   3358 N ND2 C ASN   B 2 149 ? 1.599   -3.407  -25.354 0.28 77.16  ? 158 ASN   B ND2 1 
ATOM   3359 N ND2 D ASN   B 2 149 ? 1.599   -3.407  -25.354 0.28 77.15  ? 158 ASN   B ND2 1 
ATOM   3360 N N   . GLY   B 2 150 ? 2.797   0.712   -22.134 1.00 77.82  ? 159 GLY   B N   1 
ATOM   3361 C CA  . GLY   B 2 150 ? 2.387   2.066   -21.692 1.00 71.15  ? 159 GLY   B CA  1 
ATOM   3362 C C   . GLY   B 2 150 ? 0.886   2.265   -21.883 1.00 68.30  ? 159 GLY   B C   1 
ATOM   3363 O O   . GLY   B 2 150 ? 0.327   3.260   -21.362 1.00 59.94  ? 159 GLY   B O   1 
ATOM   3364 N N   A SER   B 2 151 ? 0.250   1.343   -22.617 0.22 67.55  ? 160 SER   B N   1 
ATOM   3365 N N   B SER   B 2 151 ? 0.260   1.341   -22.620 0.22 65.55  ? 160 SER   B N   1 
ATOM   3366 N N   C SER   B 2 151 ? 0.246   1.350   -22.624 0.28 67.96  ? 160 SER   B N   1 
ATOM   3367 N N   D SER   B 2 151 ? 0.256   1.345   -22.624 0.28 65.89  ? 160 SER   B N   1 
ATOM   3368 C CA  A SER   B 2 151 ? -1.217  1.286   -22.846 0.22 66.38  ? 160 SER   B CA  1 
ATOM   3369 C CA  B SER   B 2 151 ? -1.203  1.242   -22.848 0.22 63.29  ? 160 SER   B CA  1 
ATOM   3370 C CA  C SER   B 2 151 ? -1.224  1.292   -22.848 0.28 66.94  ? 160 SER   B CA  1 
ATOM   3371 C CA  D SER   B 2 151 ? -1.211  1.247   -22.850 0.28 63.75  ? 160 SER   B CA  1 
ATOM   3372 C C   A SER   B 2 151 ? -1.923  0.703   -21.617 0.22 63.71  ? 160 SER   B C   1 
ATOM   3373 C C   B SER   B 2 151 ? -1.910  0.738   -21.586 0.22 61.65  ? 160 SER   B C   1 
ATOM   3374 C C   C SER   B 2 151 ? -1.920  0.718   -21.605 0.28 64.53  ? 160 SER   B C   1 
ATOM   3375 C C   D SER   B 2 151 ? -1.909  0.752   -21.574 0.28 62.42  ? 160 SER   B C   1 
ATOM   3376 O O   A SER   B 2 151 ? -1.261  0.045   -20.784 0.22 61.92  ? 160 SER   B O   1 
ATOM   3377 O O   B SER   B 2 151 ? -1.241  0.158   -20.701 0.22 60.13  ? 160 SER   B O   1 
ATOM   3378 O O   C SER   B 2 151 ? -1.240  0.045   -20.798 0.28 62.13  ? 160 SER   B O   1 
ATOM   3379 O O   D SER   B 2 151 ? -1.219  0.161   -20.712 0.28 60.41  ? 160 SER   B O   1 
ATOM   3380 C CB  A SER   B 2 151 ? -1.551  0.486   -24.079 0.22 67.79  ? 160 SER   B CB  1 
ATOM   3381 C CB  B SER   B 2 151 ? -1.488  0.329   -24.006 0.22 62.70  ? 160 SER   B CB  1 
ATOM   3382 C CB  C SER   B 2 151 ? -1.554  0.484   -24.078 0.28 68.26  ? 160 SER   B CB  1 
ATOM   3383 C CB  D SER   B 2 151 ? -1.492  0.327   -24.004 0.28 62.93  ? 160 SER   B CB  1 
ATOM   3384 O OG  A SER   B 2 151 ? -2.942  0.551   -24.360 0.22 68.83  ? 160 SER   B OG  1 
ATOM   3385 O OG  B SER   B 2 151 ? -0.827  -0.913  -23.820 0.22 60.01  ? 160 SER   B OG  1 
ATOM   3386 O OG  C SER   B 2 151 ? -2.945  0.545   -24.364 0.28 69.28  ? 160 SER   B OG  1 
ATOM   3387 O OG  D SER   B 2 151 ? -0.821  -0.910  -23.819 0.28 59.75  ? 160 SER   B OG  1 
ATOM   3388 N N   A TYR   B 2 152 ? -3.238  0.908   -21.567 0.22 57.58  ? 161 TYR   B N   1 
ATOM   3389 N N   B TYR   B 2 152 ? -3.233  0.905   -21.566 0.22 56.85  ? 161 TYR   B N   1 
ATOM   3390 N N   C TYR   B 2 152 ? -3.224  0.981   -21.458 0.28 59.09  ? 161 TYR   B N   1 
ATOM   3391 N N   D TYR   B 2 152 ? -3.223  0.979   -21.459 0.28 58.32  ? 161 TYR   B N   1 
ATOM   3392 C CA  A TYR   B 2 152 ? -4.132  0.565   -20.435 0.22 54.65  ? 161 TYR   B CA  1 
ATOM   3393 C CA  B TYR   B 2 152 ? -4.132  0.566   -20.436 0.22 54.33  ? 161 TYR   B CA  1 
ATOM   3394 C CA  C TYR   B 2 152 ? -4.061  0.562   -20.300 0.28 56.13  ? 161 TYR   B CA  1 
ATOM   3395 C CA  D TYR   B 2 152 ? -4.063  0.563   -20.301 0.28 55.78  ? 161 TYR   B CA  1 
ATOM   3396 C C   A TYR   B 2 152 ? -4.816  -0.774  -20.720 0.22 50.05  ? 161 TYR   B C   1 
ATOM   3397 C C   B TYR   B 2 152 ? -4.817  -0.774  -20.720 0.22 49.94  ? 161 TYR   B C   1 
ATOM   3398 C C   C TYR   B 2 152 ? -4.818  -0.721  -20.669 0.28 50.52  ? 161 TYR   B C   1 
ATOM   3399 C C   D TYR   B 2 152 ? -4.819  -0.720  -20.669 0.28 50.40  ? 161 TYR   B C   1 
ATOM   3400 O O   A TYR   B 2 152 ? -5.214  -1.003  -21.868 0.22 46.43  ? 161 TYR   B O   1 
ATOM   3401 O O   B TYR   B 2 152 ? -5.216  -1.002  -21.867 0.22 46.39  ? 161 TYR   B O   1 
ATOM   3402 O O   C TYR   B 2 152 ? -5.254  -0.862  -21.814 0.28 45.22  ? 161 TYR   B O   1 
ATOM   3403 O O   D TYR   B 2 152 ? -5.256  -0.861  -21.813 0.28 45.19  ? 161 TYR   B O   1 
ATOM   3404 C CB  A TYR   B 2 152 ? -5.155  1.687   -20.246 0.22 55.06  ? 161 TYR   B CB  1 
ATOM   3405 C CB  B TYR   B 2 152 ? -5.155  1.689   -20.248 0.22 54.89  ? 161 TYR   B CB  1 
ATOM   3406 C CB  C TYR   B 2 152 ? -5.016  1.691   -19.885 0.28 58.14  ? 161 TYR   B CB  1 
ATOM   3407 C CB  D TYR   B 2 152 ? -5.017  1.693   -19.886 0.28 57.94  ? 161 TYR   B CB  1 
ATOM   3408 C CG  A TYR   B 2 152 ? -6.093  1.482   -19.087 0.22 53.80  ? 161 TYR   B CG  1 
ATOM   3409 C CG  B TYR   B 2 152 ? -6.093  1.484   -19.088 0.22 53.71  ? 161 TYR   B CG  1 
ATOM   3410 C CG  C TYR   B 2 152 ? -5.594  1.593   -18.490 0.28 57.24  ? 161 TYR   B CG  1 
ATOM   3411 C CG  D TYR   B 2 152 ? -5.595  1.594   -18.491 0.28 57.13  ? 161 TYR   B CG  1 
ATOM   3412 C CD1 A TYR   B 2 152 ? -5.643  1.619   -17.783 0.22 52.72  ? 161 TYR   B CD1 1 
ATOM   3413 C CD1 B TYR   B 2 152 ? -5.643  1.622   -17.785 0.22 52.68  ? 161 TYR   B CD1 1 
ATOM   3414 C CD1 C TYR   B 2 152 ? -4.950  2.166   -17.404 0.28 56.74  ? 161 TYR   B CD1 1 
ATOM   3415 C CD1 D TYR   B 2 152 ? -4.951  2.167   -17.405 0.28 56.67  ? 161 TYR   B CD1 1 
ATOM   3416 C CD2 A TYR   B 2 152 ? -7.420  1.136   -19.290 0.22 51.09  ? 161 TYR   B CD2 1 
ATOM   3417 C CD2 B TYR   B 2 152 ? -7.420  1.138   -19.291 0.22 51.06  ? 161 TYR   B CD2 1 
ATOM   3418 C CD2 C TYR   B 2 152 ? -6.805  0.958   -18.251 0.28 58.21  ? 161 TYR   B CD2 1 
ATOM   3419 C CD2 D TYR   B 2 152 ? -6.805  0.959   -18.252 0.28 58.14  ? 161 TYR   B CD2 1 
ATOM   3420 C CE1 A TYR   B 2 152 ? -6.491  1.432   -16.706 0.22 51.80  ? 161 TYR   B CE1 1 
ATOM   3421 C CE1 B TYR   B 2 152 ? -6.491  1.435   -16.707 0.22 51.78  ? 161 TYR   B CE1 1 
ATOM   3422 C CE1 C TYR   B 2 152 ? -5.475  2.093   -16.121 0.28 53.73  ? 161 TYR   B CE1 1 
ATOM   3423 C CE1 D TYR   B 2 152 ? -5.475  2.092   -16.121 0.28 53.71  ? 161 TYR   B CE1 1 
ATOM   3424 C CE2 A TYR   B 2 152 ? -8.282  0.949   -18.223 0.22 50.42  ? 161 TYR   B CE2 1 
ATOM   3425 C CE2 B TYR   B 2 152 ? -8.281  0.951   -18.223 0.22 50.41  ? 161 TYR   B CE2 1 
ATOM   3426 C CE2 C TYR   B 2 152 ? -7.346  0.880   -16.975 0.28 55.23  ? 161 TYR   B CE2 1 
ATOM   3427 C CE2 D TYR   B 2 152 ? -7.346  0.880   -16.975 0.28 55.19  ? 161 TYR   B CE2 1 
ATOM   3428 C CZ  A TYR   B 2 152 ? -7.815  1.093   -16.927 0.22 51.43  ? 161 TYR   B CZ  1 
ATOM   3429 C CZ  B TYR   B 2 152 ? -7.814  1.096   -16.927 0.22 51.41  ? 161 TYR   B CZ  1 
ATOM   3430 C CZ  C TYR   B 2 152 ? -6.681  1.447   -15.900 0.28 53.03  ? 161 TYR   B CZ  1 
ATOM   3431 C CZ  D TYR   B 2 152 ? -6.680  1.447   -15.900 0.28 53.02  ? 161 TYR   B CZ  1 
ATOM   3432 O OH  A TYR   B 2 152 ? -8.654  0.902   -15.869 0.22 51.45  ? 161 TYR   B OH  1 
ATOM   3433 O OH  B TYR   B 2 152 ? -8.653  0.906   -15.870 0.22 51.44  ? 161 TYR   B OH  1 
ATOM   3434 O OH  C TYR   B 2 152 ? -7.204  1.374   -14.634 0.28 44.34  ? 161 TYR   B OH  1 
ATOM   3435 O OH  D TYR   B 2 152 ? -7.203  1.373   -14.634 0.28 44.39  ? 161 TYR   B OH  1 
ATOM   3436 N N   . VAL   B 2 153 ? -4.935  -1.634  -19.706 1.00 46.70  ? 162 VAL   B N   1 
ATOM   3437 C CA  . VAL   B 2 153 ? -5.752  -2.873  -19.805 1.00 45.55  ? 162 VAL   B CA  1 
ATOM   3438 C C   . VAL   B 2 153 ? -6.718  -2.830  -18.618 1.00 41.35  ? 162 VAL   B C   1 
ATOM   3439 O O   . VAL   B 2 153 ? -6.239  -2.614  -17.504 1.00 41.02  ? 162 VAL   B O   1 
ATOM   3440 C CB  . VAL   B 2 153 ? -4.881  -4.142  -19.751 1.00 44.54  ? 162 VAL   B CB  1 
ATOM   3441 C CG1 . VAL   B 2 153 ? -5.727  -5.398  -19.962 1.00 37.11  ? 162 VAL   B CG1 1 
ATOM   3442 C CG2 . VAL   B 2 153 ? -3.709  -4.047  -20.725 1.00 52.53  ? 162 VAL   B CG2 1 
ATOM   3443 N N   . SER   B 2 154 ? -7.995  -3.069  -18.860 1.00 41.61  ? 163 SER   B N   1 
ATOM   3444 C CA  . SER   B 2 154 ? -9.058  -2.890  -17.854 1.00 39.67  ? 163 SER   B CA  1 
ATOM   3445 C C   . SER   B 2 154 ? -9.596  -4.265  -17.537 1.00 34.16  ? 163 SER   B C   1 
ATOM   3446 O O   . SER   B 2 154 ? -9.851  -4.996  -18.462 1.00 35.54  ? 163 SER   B O   1 
ATOM   3447 C CB  . SER   B 2 154 ? -10.183 -1.994  -18.331 1.00 40.39  ? 163 SER   B CB  1 
ATOM   3448 O OG  . SER   B 2 154 ? -11.283 -2.083  -17.413 1.00 38.70  ? 163 SER   B OG  1 
ATOM   3449 N N   . ALA   B 2 155 ? -9.857  -4.549  -16.262 1.00 31.79  ? 164 ALA   B N   1 
ATOM   3450 C CA  . ALA   B 2 155 ? -10.680 -5.705  -15.914 1.00 24.95  ? 164 ALA   B CA  1 
ATOM   3451 C C   . ALA   B 2 155 ? -12.073 -5.471  -16.464 1.00 32.23  ? 164 ALA   B C   1 
ATOM   3452 O O   . ALA   B 2 155 ? -12.495 -4.280  -16.599 1.00 42.57  ? 164 ALA   B O   1 
ATOM   3453 C CB  . ALA   B 2 155 ? -10.705 -5.900  -14.410 1.00 31.02  ? 164 ALA   B CB  1 
ATOM   3454 N N   . ILE   B 2 156 ? -12.758 -6.577  -16.729 1.00 31.54  ? 165 ILE   B N   1 
ATOM   3455 C CA  . ILE   B 2 156 ? -14.225 -6.667  -16.813 1.00 36.11  ? 165 ILE   B CA  1 
ATOM   3456 C C   . ILE   B 2 156 ? -14.745 -6.788  -15.362 1.00 37.74  ? 165 ILE   B C   1 
ATOM   3457 O O   . ILE   B 2 156 ? -15.053 -7.958  -14.917 1.00 37.37  ? 165 ILE   B O   1 
ATOM   3458 C CB  . ILE   B 2 156 ? -14.630 -7.865  -17.683 1.00 36.88  ? 165 ILE   B CB  1 
ATOM   3459 C CG1 . ILE   B 2 156 ? -13.873 -7.869  -19.024 1.00 42.48  ? 165 ILE   B CG1 1 
ATOM   3460 C CG2 . ILE   B 2 156 ? -16.138 -7.880  -17.877 1.00 37.14  ? 165 ILE   B CG2 1 
ATOM   3461 C CD1 . ILE   B 2 156 ? -14.188 -9.046  -19.888 1.00 44.50  ? 165 ILE   B CD1 1 
ATOM   3462 N N   . THR   B 2 157 ? -14.890 -5.646  -14.665 1.00 41.01  ? 166 THR   B N   1 
ATOM   3463 C CA  . THR   B 2 157 ? -15.407 -5.583  -13.256 1.00 31.11  ? 166 THR   B CA  1 
ATOM   3464 C C   . THR   B 2 157 ? -16.917 -5.784  -13.238 1.00 33.91  ? 166 THR   B C   1 
ATOM   3465 O O   . THR   B 2 157 ? -17.654 -4.908  -13.767 1.00 30.90  ? 166 THR   B O   1 
ATOM   3466 C CB  . THR   B 2 157 ? -15.073 -4.269  -12.594 1.00 35.04  ? 166 THR   B CB  1 
ATOM   3467 O OG1 . THR   B 2 157 ? -13.662 -4.111  -12.741 1.00 32.51  ? 166 THR   B OG1 1 
ATOM   3468 C CG2 . THR   B 2 157 ? -15.569 -4.222  -11.157 1.00 33.27  ? 166 THR   B CG2 1 
ATOM   3469 N N   . GLN   B 2 158 ? -17.385 -6.865  -12.621 1.00 30.63  ? 167 GLN   B N   1 
ATOM   3470 C CA  . GLN   B 2 158 ? -18.815 -7.197  -12.442 1.00 30.75  ? 167 GLN   B CA  1 
ATOM   3471 C C   . GLN   B 2 158 ? -19.150 -7.331  -10.953 1.00 36.66  ? 167 GLN   B C   1 
ATOM   3472 O O   . GLN   B 2 158 ? -18.319 -7.824  -10.203 1.00 30.47  ? 167 GLN   B O   1 
ATOM   3473 C CB  . GLN   B 2 158 ? -19.130 -8.504  -13.123 1.00 29.38  ? 167 GLN   B CB  1 
ATOM   3474 C CG  . GLN   B 2 158 ? -20.572 -8.915  -13.126 1.00 29.59  ? 167 GLN   B CG  1 
ATOM   3475 C CD  . GLN   B 2 158 ? -21.511 -7.859  -13.680 1.00 39.16  ? 167 GLN   B CD  1 
ATOM   3476 O OE1 . GLN   B 2 158 ? -21.578 -6.747  -13.161 1.00 31.67  ? 167 GLN   B OE1 1 
ATOM   3477 N NE2 . GLN   B 2 158 ? -22.295 -8.220  -14.695 1.00 32.92  ? 167 GLN   B NE2 1 
ATOM   3478 N N   . GLY   B 2 159 ? -20.344 -6.934  -10.556 1.00 35.57  ? 168 GLY   B N   1 
ATOM   3479 C CA  . GLY   B 2 159 ? -20.794 -7.063  -9.162  1.00 40.97  ? 168 GLY   B CA  1 
ATOM   3480 C C   . GLY   B 2 159 ? -21.587 -8.330  -9.012  1.00 44.29  ? 168 GLY   B C   1 
ATOM   3481 O O   . GLY   B 2 159 ? -21.793 -9.046  -9.981  1.00 53.78  ? 168 GLY   B O   1 
ATOM   3482 N N   A LYS   B 2 160 ? -21.998 -8.623  -7.778  0.22 48.02  ? 169 LYS   B N   1 
ATOM   3483 N N   B LYS   B 2 160 ? -21.998 -8.623  -7.778  0.22 48.01  ? 169 LYS   B N   1 
ATOM   3484 N N   C LYS   B 2 160 ? -22.069 -8.582  -7.798  0.28 50.17  ? 169 LYS   B N   1 
ATOM   3485 N N   D LYS   B 2 160 ? -22.069 -8.582  -7.798  0.28 50.16  ? 169 LYS   B N   1 
ATOM   3486 C CA  A LYS   B 2 160 ? -22.889 -9.763  -7.450  0.22 48.40  ? 169 LYS   B CA  1 
ATOM   3487 C CA  B LYS   B 2 160 ? -22.889 -9.763  -7.450  0.22 48.41  ? 169 LYS   B CA  1 
ATOM   3488 C CA  C LYS   B 2 160 ? -22.878 -9.776  -7.455  0.28 51.70  ? 169 LYS   B CA  1 
ATOM   3489 C CA  D LYS   B 2 160 ? -22.878 -9.776  -7.455  0.28 51.71  ? 169 LYS   B CA  1 
ATOM   3490 C C   A LYS   B 2 160 ? -24.314 -9.232  -7.285  0.22 51.80  ? 169 LYS   B C   1 
ATOM   3491 C C   B LYS   B 2 160 ? -24.314 -9.232  -7.285  0.22 51.80  ? 169 LYS   B C   1 
ATOM   3492 C C   C LYS   B 2 160 ? -24.315 -9.319  -7.183  0.28 54.67  ? 169 LYS   B C   1 
ATOM   3493 C C   D LYS   B 2 160 ? -24.315 -9.319  -7.183  0.28 54.67  ? 169 LYS   B C   1 
ATOM   3494 O O   A LYS   B 2 160 ? -24.483 -8.163  -6.657  0.22 50.09  ? 169 LYS   B O   1 
ATOM   3495 O O   B LYS   B 2 160 ? -24.483 -8.164  -6.656  0.22 50.10  ? 169 LYS   B O   1 
ATOM   3496 O O   C LYS   B 2 160 ? -24.498 -8.378  -6.382  0.28 53.75  ? 169 LYS   B O   1 
ATOM   3497 O O   D LYS   B 2 160 ? -24.498 -8.378  -6.382  0.28 53.75  ? 169 LYS   B O   1 
ATOM   3498 C CB  A LYS   B 2 160 ? -22.423 -10.481 -6.181  0.22 49.07  ? 169 LYS   B CB  1 
ATOM   3499 C CB  B LYS   B 2 160 ? -22.423 -10.481 -6.181  0.22 49.06  ? 169 LYS   B CB  1 
ATOM   3500 C CB  C LYS   B 2 160 ? -22.204 -10.509 -6.289  0.28 54.85  ? 169 LYS   B CB  1 
ATOM   3501 C CB  D LYS   B 2 160 ? -22.204 -10.509 -6.289  0.28 54.84  ? 169 LYS   B CB  1 
ATOM   3502 C CG  A LYS   B 2 160 ? -23.036 -11.858 -5.963  0.22 47.91  ? 169 LYS   B CG  1 
ATOM   3503 C CG  B LYS   B 2 160 ? -23.036 -11.858 -5.963  0.22 47.91  ? 169 LYS   B CG  1 
ATOM   3504 C CG  C LYS   B 2 160 ? -20.873 -11.160 -6.653  0.28 55.34  ? 169 LYS   B CG  1 
ATOM   3505 C CG  D LYS   B 2 160 ? -20.873 -11.160 -6.653  0.28 55.33  ? 169 LYS   B CG  1 
ATOM   3506 C CD  A LYS   B 2 160 ? -22.638 -12.483 -4.648  0.22 47.85  ? 169 LYS   B CD  1 
ATOM   3507 C CD  B LYS   B 2 160 ? -22.638 -12.482 -4.647  0.22 47.85  ? 169 LYS   B CD  1 
ATOM   3508 C CD  C LYS   B 2 160 ? -19.797 -11.025 -5.598  0.28 57.43  ? 169 LYS   B CD  1 
ATOM   3509 C CD  D LYS   B 2 160 ? -19.798 -11.025 -5.598  0.28 57.42  ? 169 LYS   B CD  1 
ATOM   3510 C CE  A LYS   B 2 160 ? -23.586 -13.570 -4.197  0.22 45.75  ? 169 LYS   B CE  1 
ATOM   3511 C CE  B LYS   B 2 160 ? -23.586 -13.570 -4.197  0.22 45.77  ? 169 LYS   B CE  1 
ATOM   3512 C CE  C LYS   B 2 160 ? -18.446 -11.508 -6.083  0.28 58.11  ? 169 LYS   B CE  1 
ATOM   3513 C CE  D LYS   B 2 160 ? -18.446 -11.508 -6.083  0.28 58.10  ? 169 LYS   B CE  1 
ATOM   3514 N NZ  A LYS   B 2 160 ? -23.669 -13.615 -2.720  0.22 47.97  ? 169 LYS   B NZ  1 
ATOM   3515 N NZ  B LYS   B 2 160 ? -23.669 -13.615 -2.720  0.22 47.97  ? 169 LYS   B NZ  1 
ATOM   3516 N NZ  C LYS   B 2 160 ? -17.884 -10.636 -7.143  0.28 57.41  ? 169 LYS   B NZ  1 
ATOM   3517 N NZ  D LYS   B 2 160 ? -17.884 -10.636 -7.143  0.28 57.40  ? 169 LYS   B NZ  1 
ATOM   3518 N N   . ARG   B 2 161 ? -25.287 -9.951  -7.853  1.00 55.63  ? 170 ARG   B N   1 
ATOM   3519 C CA  . ARG   B 2 161 ? -26.735 -9.677  -7.660  1.00 59.99  ? 170 ARG   B CA  1 
ATOM   3520 C C   . ARG   B 2 161 ? -27.192 -10.546 -6.476  1.00 66.81  ? 170 ARG   B C   1 
ATOM   3521 O O   . ARG   B 2 161 ? -26.839 -11.742 -6.473  1.00 73.03  ? 170 ARG   B O   1 
ATOM   3522 C CB  . ARG   B 2 161 ? -27.443 -9.971  -8.990  1.00 61.68  ? 170 ARG   B CB  1 
ATOM   3523 C CG  . ARG   B 2 161 ? -28.898 -9.535  -9.042  1.00 60.69  ? 170 ARG   B CG  1 
ATOM   3524 C CD  . ARG   B 2 161 ? -29.672 -10.118 -10.209 1.00 60.62  ? 170 ARG   B CD  1 
ATOM   3525 N NE  . ARG   B 2 161 ? -31.077 -9.782  -10.021 1.00 67.28  ? 170 ARG   B NE  1 
ATOM   3526 C CZ  . ARG   B 2 161 ? -31.773 -8.895  -10.735 1.00 58.45  ? 170 ARG   B CZ  1 
ATOM   3527 N NH1 . ARG   B 2 161 ? -31.214 -8.227  -11.731 1.00 54.31  ? 170 ARG   B NH1 1 
ATOM   3528 N NH2 . ARG   B 2 161 ? -33.036 -8.675  -10.426 1.00 62.87  ? 170 ARG   B NH2 1 
ATOM   3529 N N   . GLU   B 2 162 ? -27.884 -9.973  -5.483  1.00 78.63  ? 171 GLU   B N   1 
ATOM   3530 C CA  . GLU   B 2 162 ? -28.493 -10.724 -4.344  1.00 79.88  ? 171 GLU   B CA  1 
ATOM   3531 C C   . GLU   B 2 162 ? -29.972 -10.976 -4.658  1.00 74.14  ? 171 GLU   B C   1 
ATOM   3532 O O   . GLU   B 2 162 ? -30.553 -12.002 -4.318  1.00 86.00  ? 171 GLU   B O   1 
ATOM   3533 C CB  . GLU   B 2 162 ? -28.338 -9.954  -3.028  1.00 88.30  ? 171 GLU   B CB  1 
ATOM   3534 C CG  . GLU   B 2 162 ? -26.909 -9.527  -2.692  1.00 93.98  ? 171 GLU   B CG  1 
ATOM   3535 C CD  . GLU   B 2 162 ? -25.896 -10.641 -2.445  1.00 104.99 ? 171 GLU   B CD  1 
ATOM   3536 O OE1 . GLU   B 2 162 ? -25.661 -10.987 -1.259  1.00 94.69  ? 171 GLU   B OE1 1 
ATOM   3537 O OE2 . GLU   B 2 162 ? -25.313 -11.144 -3.436  1.00 116.27 ? 171 GLU   B OE2 1 
HETATM 3538 S S   A DMS   C 3 .   ? -8.384  5.624   -18.044 0.22 74.69  ? 201 DMS   B S   1 
HETATM 3539 S S   B DMS   C 3 .   ? -8.382  5.623   -18.045 0.22 74.69  ? 201 DMS   B S   1 
HETATM 3540 O O   A DMS   C 3 .   ? -7.173  5.375   -18.903 0.22 75.26  ? 201 DMS   B O   1 
HETATM 3541 O O   B DMS   C 3 .   ? -7.171  5.370   -18.903 0.22 75.25  ? 201 DMS   B O   1 
HETATM 3542 C C1  A DMS   C 3 .   ? -8.018  4.932   -16.452 0.22 75.67  ? 201 DMS   B C1  1 
HETATM 3543 C C1  B DMS   C 3 .   ? -8.018  4.932   -16.452 0.22 75.66  ? 201 DMS   B C1  1 
HETATM 3544 C C2  A DMS   C 3 .   ? -9.603  4.439   -18.552 0.22 74.70  ? 201 DMS   B C2  1 
HETATM 3545 C C2  B DMS   C 3 .   ? -9.603  4.439   -18.552 0.22 74.70  ? 201 DMS   B C2  1 
HETATM 3546 S S   A DMS   D 3 .   ? -17.468 11.386  -0.022  0.22 101.35 ? 202 DMS   B S   1 
HETATM 3547 S S   B DMS   D 3 .   ? -17.468 11.386  -0.022  0.22 101.34 ? 202 DMS   B S   1 
HETATM 3548 O O   A DMS   D 3 .   ? -17.591 9.891   0.024   0.22 96.19  ? 202 DMS   B O   1 
HETATM 3549 O O   B DMS   D 3 .   ? -17.591 9.891   0.024   0.22 96.21  ? 202 DMS   B O   1 
HETATM 3550 C C1  A DMS   D 3 .   ? -19.081 11.998  -0.440  0.22 100.47 ? 202 DMS   B C1  1 
HETATM 3551 C C1  B DMS   D 3 .   ? -19.081 11.998  -0.440  0.22 100.46 ? 202 DMS   B C1  1 
HETATM 3552 C C2  A DMS   D 3 .   ? -16.661 11.772  -1.553  0.22 99.77  ? 202 DMS   B C2  1 
HETATM 3553 C C2  B DMS   D 3 .   ? -16.661 11.773  -1.553  0.22 99.77  ? 202 DMS   B C2  1 
HETATM 3554 S S   A DMS   E 3 .   ? -6.195  3.176   -13.469 0.22 68.62  ? 203 DMS   B S   1 
HETATM 3555 S S   B DMS   E 3 .   ? -6.194  3.175   -13.467 0.22 68.63  ? 203 DMS   B S   1 
HETATM 3556 O O   A DMS   E 3 .   ? -5.322  2.132   -12.845 0.22 67.27  ? 203 DMS   B O   1 
HETATM 3557 O O   B DMS   E 3 .   ? -5.321  2.133   -12.840 0.22 67.27  ? 203 DMS   B O   1 
HETATM 3558 C C1  A DMS   E 3 .   ? -7.723  3.167   -12.567 0.22 70.52  ? 203 DMS   B C1  1 
HETATM 3559 C C1  B DMS   E 3 .   ? -7.723  3.167   -12.567 0.22 70.50  ? 203 DMS   B C1  1 
HETATM 3560 C C2  A DMS   E 3 .   ? -5.576  4.742   -12.898 0.22 68.59  ? 203 DMS   B C2  1 
HETATM 3561 C C2  B DMS   E 3 .   ? -5.576  4.742   -12.897 0.22 68.59  ? 203 DMS   B C2  1 
HETATM 3562 N N1  C A1BGI F 4 .   ? -8.711  4.885   -10.056 0.28 37.91  ? 204 A1BGI B N1  1 
HETATM 3563 N N1  D A1BGI F 4 .   ? -8.711  4.885   -10.056 0.28 37.92  ? 204 A1BGI B N1  1 
HETATM 3564 N N3  C A1BGI F 4 .   ? -6.635  4.812   -19.115 0.28 47.99  ? 204 A1BGI B N3  1 
HETATM 3565 N N3  D A1BGI F 4 .   ? -6.635  4.812   -19.115 0.28 47.98  ? 204 A1BGI B N3  1 
HETATM 3566 C C4  C A1BGI F 4 .   ? -8.365  4.998   -14.388 0.28 42.46  ? 204 A1BGI B C4  1 
HETATM 3567 C C4  D A1BGI F 4 .   ? -8.365  4.999   -14.388 0.28 42.46  ? 204 A1BGI B C4  1 
HETATM 3568 C C5  C A1BGI F 4 .   ? -8.485  4.722   -15.863 0.28 44.14  ? 204 A1BGI B C5  1 
HETATM 3569 C C5  D A1BGI F 4 .   ? -8.485  4.722   -15.864 0.28 44.14  ? 204 A1BGI B C5  1 
HETATM 3570 C C6  C A1BGI F 4 .   ? -9.685  4.260   -16.340 0.28 44.16  ? 204 A1BGI B C6  1 
HETATM 3571 C C6  D A1BGI F 4 .   ? -9.685  4.260   -16.340 0.28 44.16  ? 204 A1BGI B C6  1 
HETATM 3572 C C7  C A1BGI F 4 .   ? -9.879  3.985   -17.705 0.28 45.46  ? 204 A1BGI B C7  1 
HETATM 3573 C C7  D A1BGI F 4 .   ? -9.879  3.985   -17.705 0.28 45.46  ? 204 A1BGI B C7  1 
HETATM 3574 C C8  C A1BGI F 4 .   ? -8.870  4.173   -18.597 0.28 46.68  ? 204 A1BGI B C8  1 
HETATM 3575 C C8  D A1BGI F 4 .   ? -8.870  4.173   -18.597 0.28 46.68  ? 204 A1BGI B C8  1 
HETATM 3576 C C10 C A1BGI F 4 .   ? -5.462  5.252   -18.699 0.28 47.10  ? 204 A1BGI B C10 1 
HETATM 3577 C C10 D A1BGI F 4 .   ? -5.462  5.252   -18.699 0.28 47.10  ? 204 A1BGI B C10 1 
HETATM 3578 C C13 C A1BGI F 4 .   ? -7.403  4.927   -16.781 0.28 45.90  ? 204 A1BGI B C13 1 
HETATM 3579 C C13 D A1BGI F 4 .   ? -7.403  4.927   -16.781 0.28 45.90  ? 204 A1BGI B C13 1 
HETATM 3580 C C1  C A1BGI F 4 .   ? -8.522  5.649   -8.832  0.28 39.50  ? 204 A1BGI B C1  1 
HETATM 3581 C C1  D A1BGI F 4 .   ? -8.522  5.649   -8.833  0.28 39.50  ? 204 A1BGI B C1  1 
HETATM 3582 C C2  C A1BGI F 4 .   ? -8.682  5.319   -11.327 0.28 38.97  ? 204 A1BGI B C2  1 
HETATM 3583 C C2  D A1BGI F 4 .   ? -8.682  5.319   -11.327 0.28 38.97  ? 204 A1BGI B C2  1 
HETATM 3584 C C3  C A1BGI F 4 .   ? -8.903  4.211   -12.130 0.28 39.47  ? 204 A1BGI B C3  1 
HETATM 3585 C C3  D A1BGI F 4 .   ? -8.903  4.211   -12.130 0.28 39.47  ? 204 A1BGI B C3  1 
HETATM 3586 N N2  C A1BGI F 4 .   ? -8.980  4.134   -13.530 0.28 39.13  ? 204 A1BGI B N2  1 
HETATM 3587 N N2  D A1BGI F 4 .   ? -8.980  4.134   -13.530 0.28 39.15  ? 204 A1BGI B N2  1 
HETATM 3588 O O1  C A1BGI F 4 .   ? -7.747  5.982   -13.991 0.28 41.98  ? 204 A1BGI B O1  1 
HETATM 3589 O O1  D A1BGI F 4 .   ? -7.747  5.982   -13.991 0.28 41.98  ? 204 A1BGI B O1  1 
HETATM 3590 C C9  C A1BGI F 4 .   ? -7.611  4.644   -18.164 0.28 47.31  ? 204 A1BGI B C9  1 
HETATM 3591 C C9  D A1BGI F 4 .   ? -7.612  4.644   -18.164 0.28 47.29  ? 204 A1BGI B C9  1 
HETATM 3592 C C11 C A1BGI F 4 .   ? -5.152  5.558   -17.361 0.28 46.22  ? 204 A1BGI B C11 1 
HETATM 3593 C C11 D A1BGI F 4 .   ? -5.153  5.558   -17.361 0.28 46.22  ? 204 A1BGI B C11 1 
HETATM 3594 C C12 C A1BGI F 4 .   ? -6.115  5.394   -16.406 0.28 46.24  ? 204 A1BGI B C12 1 
HETATM 3595 C C12 D A1BGI F 4 .   ? -6.115  5.394   -16.406 0.28 46.23  ? 204 A1BGI B C12 1 
HETATM 3596 C C14 C A1BGI F 4 .   ? -9.046  3.145   -11.256 0.28 39.00  ? 204 A1BGI B C14 1 
HETATM 3597 C C14 D A1BGI F 4 .   ? -9.046  3.145   -11.256 0.28 39.00  ? 204 A1BGI B C14 1 
HETATM 3598 N N4  C A1BGI F 4 .   ? -8.923  3.552   -10.002 0.28 38.96  ? 204 A1BGI B N4  1 
HETATM 3599 N N4  D A1BGI F 4 .   ? -8.923  3.552   -10.003 0.28 38.96  ? 204 A1BGI B N4  1 
HETATM 3600 S S   C SO4   G 5 .   ? -19.036 11.701  -0.396  0.28 57.82  ? 205 SO4   B S   1 
HETATM 3601 S S   D SO4   G 5 .   ? -19.035 11.701  -0.396  0.28 57.79  ? 205 SO4   B S   1 
HETATM 3602 O O1  C SO4   G 5 .   ? -17.733 11.890  -0.981  0.28 56.17  ? 205 SO4   B O1  1 
HETATM 3603 O O1  D SO4   G 5 .   ? -17.731 11.884  -0.981  0.28 56.16  ? 205 SO4   B O1  1 
HETATM 3604 O O2  C SO4   G 5 .   ? -19.050 12.229  0.941   0.28 53.00  ? 205 SO4   B O2  1 
HETATM 3605 O O2  D SO4   G 5 .   ? -19.048 12.232  0.940   0.28 53.02  ? 205 SO4   B O2  1 
HETATM 3606 O O3  C SO4   G 5 .   ? -20.004 12.404  -1.186  0.28 57.54  ? 205 SO4   B O3  1 
HETATM 3607 O O3  D SO4   G 5 .   ? -20.000 12.406  -1.188  0.28 57.53  ? 205 SO4   B O3  1 
HETATM 3608 O O4  C SO4   G 5 .   ? -19.360 10.290  -0.360  0.28 52.23  ? 205 SO4   B O4  1 
HETATM 3609 O O4  D SO4   G 5 .   ? -19.365 10.292  -0.358  0.28 52.26  ? 205 SO4   B O4  1 
HETATM 3610 S S   C SO4   H 5 .   ? -1.002  -14.651 -9.753  0.28 66.90  ? 206 SO4   B S   1 
HETATM 3611 S S   D SO4   H 5 .   ? -1.001  -14.651 -9.753  0.28 66.89  ? 206 SO4   B S   1 
HETATM 3612 O O1  C SO4   H 5 .   ? -1.238  -13.263 -9.458  0.28 64.18  ? 206 SO4   B O1  1 
HETATM 3613 O O1  D SO4   H 5 .   ? -1.238  -13.263 -9.458  0.28 64.19  ? 206 SO4   B O1  1 
HETATM 3614 O O2  C SO4   H 5 .   ? 0.193   -15.081 -9.080  0.28 70.49  ? 206 SO4   B O2  1 
HETATM 3615 O O2  D SO4   H 5 .   ? 0.194   -15.081 -9.080  0.28 70.46  ? 206 SO4   B O2  1 
HETATM 3616 O O3  C SO4   H 5 .   ? -2.119  -15.435 -9.301  0.28 63.55  ? 206 SO4   B O3  1 
HETATM 3617 O O3  D SO4   H 5 .   ? -2.119  -15.436 -9.301  0.28 63.57  ? 206 SO4   B O3  1 
HETATM 3618 O O4  C SO4   H 5 .   ? -0.834  -14.826 -11.171 0.28 66.28  ? 206 SO4   B O4  1 
HETATM 3619 O O4  D SO4   H 5 .   ? -0.834  -14.826 -11.171 0.28 66.28  ? 206 SO4   B O4  1 
HETATM 3620 O O   A HOH   I 6 .   ? -24.406 8.848   -27.842 0.22 21.25  ? 101 HOH   A O   1 
HETATM 3621 O O   B HOH   I 6 .   ? -24.406 8.848   -27.841 0.22 21.26  ? 101 HOH   A O   1 
HETATM 3622 O O   C HOH   I 6 .   ? -23.754 9.447   -27.168 0.28 31.80  ? 101 HOH   A O   1 
HETATM 3623 O O   D HOH   I 6 .   ? -23.754 9.447   -27.168 0.28 31.80  ? 101 HOH   A O   1 
HETATM 3624 O O   A HOH   I 6 .   ? -2.363  -4.444  -6.506  0.22 36.45  ? 102 HOH   A O   1 
HETATM 3625 O O   B HOH   I 6 .   ? -2.361  -4.444  -6.509  0.22 36.45  ? 102 HOH   A O   1 
HETATM 3626 O O   C HOH   I 6 .   ? -1.729  -3.432  -5.891  0.28 55.34  ? 102 HOH   A O   1 
HETATM 3627 O O   D HOH   I 6 .   ? -1.731  -3.432  -5.886  0.28 55.37  ? 102 HOH   A O   1 
HETATM 3628 O O   . HOH   I 6 .   ? -7.037  -9.085  -3.062  1.00 41.54  ? 103 HOH   A O   1 
HETATM 3629 O O   A HOH   I 6 .   ? 5.717   -5.573  -17.043 0.22 41.56  ? 104 HOH   A O   1 
HETATM 3630 O O   B HOH   I 6 .   ? 5.718   -5.571  -17.042 0.22 41.56  ? 104 HOH   A O   1 
HETATM 3631 O O   C HOH   I 6 .   ? -1.923  -16.086 -25.171 0.28 42.64  ? 105 HOH   A O   1 
HETATM 3632 O O   D HOH   I 6 .   ? -1.922  -16.086 -25.172 0.28 42.64  ? 105 HOH   A O   1 
HETATM 3633 O O   A HOH   I 6 .   ? -27.983 1.140   -29.621 0.22 33.29  ? 106 HOH   A O   1 
HETATM 3634 O O   B HOH   I 6 .   ? -27.302 0.560   -28.416 0.22 21.77  ? 106 HOH   A O   1 
HETATM 3635 O O   A HOH   I 6 .   ? -4.353  -9.797  -5.045  0.22 37.25  ? 107 HOH   A O   1 
HETATM 3636 O O   B HOH   I 6 .   ? -4.351  -9.793  -5.042  0.22 37.26  ? 107 HOH   A O   1 
HETATM 3637 O O   C HOH   I 6 .   ? -3.129  -9.168  -3.180  0.28 38.26  ? 107 HOH   A O   1 
HETATM 3638 O O   D HOH   I 6 .   ? -3.127  -9.168  -3.180  0.28 38.26  ? 107 HOH   A O   1 
HETATM 3639 O O   A HOH   I 6 .   ? -25.305 0.866   -29.748 0.22 67.92  ? 108 HOH   A O   1 
HETATM 3640 O O   B HOH   I 6 .   ? -25.312 0.896   -29.759 0.22 67.75  ? 108 HOH   A O   1 
HETATM 3641 O O   A HOH   I 6 .   ? -28.981 15.565  -15.013 0.22 28.00  ? 109 HOH   A O   1 
HETATM 3642 O O   B HOH   I 6 .   ? -28.981 15.565  -15.013 0.22 28.00  ? 109 HOH   A O   1 
HETATM 3643 O O   A HOH   I 6 .   ? -27.905 3.888   -28.585 0.22 7.85   ? 110 HOH   A O   1 
HETATM 3644 O O   B HOH   I 6 .   ? -28.550 3.005   -29.194 0.22 32.52  ? 110 HOH   A O   1 
HETATM 3645 O O   C HOH   I 6 .   ? -27.047 5.302   -28.735 0.28 36.71  ? 110 HOH   A O   1 
HETATM 3646 O O   D HOH   I 6 .   ? -27.047 5.303   -28.735 0.28 36.71  ? 110 HOH   A O   1 
HETATM 3647 O O   A HOH   I 6 .   ? -28.476 -6.043  -27.966 0.22 62.52  ? 111 HOH   A O   1 
HETATM 3648 O O   B HOH   I 6 .   ? -28.507 -6.058  -28.016 0.22 61.78  ? 111 HOH   A O   1 
HETATM 3649 O O   C HOH   I 6 .   ? -27.503 -5.984  -28.351 0.28 49.66  ? 111 HOH   A O   1 
HETATM 3650 O O   D HOH   I 6 .   ? -27.516 -5.985  -28.354 0.28 49.88  ? 111 HOH   A O   1 
HETATM 3651 O O   A HOH   I 6 .   ? -22.049 -1.128  -37.417 0.22 56.06  ? 112 HOH   A O   1 
HETATM 3652 O O   B HOH   I 6 .   ? -22.045 -1.131  -37.421 0.22 56.06  ? 112 HOH   A O   1 
HETATM 3653 O O   C HOH   I 6 .   ? -26.604 -3.634  -35.188 0.28 41.74  ? 112 HOH   A O   1 
HETATM 3654 O O   D HOH   I 6 .   ? -26.604 -3.634  -35.188 0.28 41.73  ? 112 HOH   A O   1 
HETATM 3655 O O   A HOH   I 6 .   ? -23.896 18.720  -19.584 0.22 35.46  ? 113 HOH   A O   1 
HETATM 3656 O O   B HOH   I 6 .   ? -23.895 18.718  -19.584 0.22 35.47  ? 113 HOH   A O   1 
HETATM 3657 O O   A HOH   I 6 .   ? -3.715  -4.487  0.073   0.22 32.15  ? 114 HOH   A O   1 
HETATM 3658 O O   B HOH   I 6 .   ? -3.714  -4.490  0.072   0.22 32.15  ? 114 HOH   A O   1 
HETATM 3659 O O   C HOH   I 6 .   ? -3.434  -3.429  0.555   0.28 56.59  ? 114 HOH   A O   1 
HETATM 3660 O O   D HOH   I 6 .   ? -3.434  -3.425  0.561   0.28 56.61  ? 114 HOH   A O   1 
HETATM 3661 O O   C HOH   I 6 .   ? -21.620 16.074  -22.511 0.28 30.24  ? 115 HOH   A O   1 
HETATM 3662 O O   D HOH   I 6 .   ? -21.619 16.074  -22.512 0.28 30.24  ? 115 HOH   A O   1 
HETATM 3663 O O   C HOH   I 6 .   ? -5.234  4.984   -7.500  0.28 39.83  ? 116 HOH   A O   1 
HETATM 3664 O O   D HOH   I 6 .   ? -5.236  4.980   -7.500  0.28 39.83  ? 116 HOH   A O   1 
HETATM 3665 O O   A HOH   I 6 .   ? -4.389  -0.928  -0.086  0.22 70.15  ? 117 HOH   A O   1 
HETATM 3666 O O   B HOH   I 6 .   ? -4.385  -0.933  -0.088  0.22 70.15  ? 117 HOH   A O   1 
HETATM 3667 O O   C HOH   I 6 .   ? -3.860  -0.588  -0.325  0.28 53.65  ? 117 HOH   A O   1 
HETATM 3668 O O   D HOH   I 6 .   ? -3.858  -0.590  -0.327  0.28 53.69  ? 117 HOH   A O   1 
HETATM 3669 O O   A HOH   I 6 .   ? -21.226 -8.566  -35.096 0.22 29.63  ? 118 HOH   A O   1 
HETATM 3670 O O   B HOH   I 6 .   ? -21.225 -8.566  -35.096 0.22 29.64  ? 118 HOH   A O   1 
HETATM 3671 O O   C HOH   I 6 .   ? -22.762 -9.575  -34.408 0.28 34.84  ? 118 HOH   A O   1 
HETATM 3672 O O   D HOH   I 6 .   ? -22.764 -9.576  -34.410 0.28 34.83  ? 118 HOH   A O   1 
HETATM 3673 O O   A HOH   I 6 .   ? -5.639  4.938   -9.117  0.22 26.98  ? 119 HOH   A O   1 
HETATM 3674 O O   B HOH   I 6 .   ? -7.965  6.683   -9.733  0.22 33.89  ? 119 HOH   A O   1 
HETATM 3675 O O   A HOH   I 6 .   ? 0.001   -12.915 -9.739  0.22 64.66  ? 120 HOH   A O   1 
HETATM 3676 O O   B HOH   I 6 .   ? -0.004  -12.911 -9.738  0.22 64.66  ? 120 HOH   A O   1 
HETATM 3677 O O   A HOH   I 6 .   ? -31.552 0.184   -23.416 0.22 29.68  ? 121 HOH   A O   1 
HETATM 3678 O O   B HOH   I 6 .   ? -31.553 0.184   -23.416 0.22 29.68  ? 121 HOH   A O   1 
HETATM 3679 O O   C HOH   I 6 .   ? -30.372 0.176   -22.625 0.28 38.77  ? 121 HOH   A O   1 
HETATM 3680 O O   D HOH   I 6 .   ? -30.369 0.173   -22.626 0.28 38.79  ? 121 HOH   A O   1 
HETATM 3681 O O   C HOH   J 6 .   ? -8.436  2.281   -8.507  0.28 41.40  ? 301 HOH   B O   1 
HETATM 3682 O O   D HOH   J 6 .   ? -8.441  2.280   -8.507  0.28 41.41  ? 301 HOH   B O   1 
HETATM 3683 O O   A HOH   J 6 .   ? -13.567 -2.860  -14.902 0.22 24.10  ? 302 HOH   B O   1 
HETATM 3684 O O   B HOH   J 6 .   ? -13.567 -2.859  -14.902 0.22 24.10  ? 302 HOH   B O   1 
HETATM 3685 O O   C HOH   J 6 .   ? -12.645 -1.818  -14.722 0.28 21.59  ? 302 HOH   B O   1 
HETATM 3686 O O   D HOH   J 6 .   ? -12.645 -1.818  -14.722 0.28 21.59  ? 302 HOH   B O   1 
HETATM 3687 O O   . HOH   J 6 .   ? -33.986 1.502   -15.504 1.00 47.82  ? 303 HOH   B O   1 
HETATM 3688 O O   A HOH   J 6 .   ? -1.242  -18.495 -19.735 0.22 56.74  ? 304 HOH   B O   1 
HETATM 3689 O O   B HOH   J 6 .   ? -1.238  -18.499 -19.735 0.22 56.69  ? 304 HOH   B O   1 
HETATM 3690 O O   A HOH   J 6 .   ? -5.413  2.548   -10.587 0.22 36.93  ? 305 HOH   B O   1 
HETATM 3691 O O   B HOH   J 6 .   ? -5.417  2.550   -10.583 0.22 36.93  ? 305 HOH   B O   1 
HETATM 3692 O O   C HOH   J 6 .   ? -20.648 13.740  1.666   0.28 39.36  ? 306 HOH   B O   1 
HETATM 3693 O O   D HOH   J 6 .   ? -20.650 13.738  1.670   0.28 39.36  ? 306 HOH   B O   1 
HETATM 3694 O O   A HOH   J 6 .   ? -15.461 9.146   -0.714  0.23 25.64  ? 307 HOH   B O   1 
HETATM 3695 O O   B HOH   J 6 .   ? -15.461 9.146   -0.714  0.23 25.64  ? 307 HOH   B O   1 
HETATM 3696 O O   A HOH   J 6 .   ? -31.318 12.291  -19.233 0.22 55.99  ? 308 HOH   B O   1 
HETATM 3697 O O   B HOH   J 6 .   ? -31.319 12.288  -19.231 0.22 56.04  ? 308 HOH   B O   1 
HETATM 3698 O O   C HOH   J 6 .   ? -30.404 12.738  -19.704 0.28 50.81  ? 308 HOH   B O   1 
HETATM 3699 O O   D HOH   J 6 .   ? -30.405 12.735  -19.704 0.28 50.84  ? 308 HOH   B O   1 
HETATM 3700 O O   A HOH   J 6 .   ? -7.123  -11.009 -5.360  0.22 30.24  ? 309 HOH   B O   1 
HETATM 3701 O O   B HOH   J 6 .   ? -7.122  -11.009 -5.360  0.22 30.24  ? 309 HOH   B O   1 
HETATM 3702 O O   C HOH   J 6 .   ? -5.077  -10.736 -5.716  0.28 40.14  ? 309 HOH   B O   1 
HETATM 3703 O O   D HOH   J 6 .   ? -5.081  -10.737 -5.719  0.28 40.16  ? 309 HOH   B O   1 
HETATM 3704 O O   A HOH   J 6 .   ? -34.526 1.049   -3.519  0.22 33.25  ? 310 HOH   B O   1 
HETATM 3705 O O   B HOH   J 6 .   ? -34.523 1.048   -3.518  0.22 33.25  ? 310 HOH   B O   1 
HETATM 3706 O O   C HOH   J 6 .   ? -34.632 0.151   -3.239  0.28 41.32  ? 310 HOH   B O   1 
HETATM 3707 O O   D HOH   J 6 .   ? -34.629 0.150   -3.244  0.28 41.31  ? 310 HOH   B O   1 
HETATM 3708 O O   A HOH   J 6 .   ? -14.060 -12.022 -16.440 0.22 32.29  ? 311 HOH   B O   1 
HETATM 3709 O O   B HOH   J 6 .   ? -14.060 -12.024 -16.441 0.22 32.29  ? 311 HOH   B O   1 
HETATM 3710 O O   C HOH   J 6 .   ? -14.864 -13.085 -16.260 0.28 32.37  ? 311 HOH   B O   1 
HETATM 3711 O O   D HOH   J 6 .   ? -14.864 -13.084 -16.259 0.28 32.36  ? 311 HOH   B O   1 
HETATM 3712 O O   C HOH   J 6 .   ? -20.370 -7.792  -5.968  0.28 40.61  ? 312 HOH   B O   1 
HETATM 3713 O O   D HOH   J 6 .   ? -20.370 -7.792  -5.972  0.28 40.62  ? 312 HOH   B O   1 
HETATM 3714 O O   C HOH   J 6 .   ? -3.123  2.317   -26.080 0.28 57.24  ? 313 HOH   B O   1 
HETATM 3715 O O   D HOH   J 6 .   ? -3.143  2.312   -26.074 0.28 57.36  ? 313 HOH   B O   1 
HETATM 3716 O O   A HOH   J 6 .   ? -22.245 -11.425 -10.533 0.22 32.63  ? 314 HOH   B O   1 
HETATM 3717 O O   B HOH   J 6 .   ? -22.245 -11.425 -10.533 0.22 32.64  ? 314 HOH   B O   1 
HETATM 3718 O O   . HOH   J 6 .   ? -19.484 -12.430 -25.684 1.00 54.02  ? 315 HOH   B O   1 
HETATM 3719 O O   A HOH   J 6 .   ? -11.914 -3.140  -10.109 0.22 22.16  ? 316 HOH   B O   1 
HETATM 3720 O O   B HOH   J 6 .   ? -11.914 -3.140  -10.109 0.22 22.17  ? 316 HOH   B O   1 
HETATM 3721 O O   C HOH   J 6 .   ? -12.767 -4.043  -10.016 0.28 26.37  ? 316 HOH   B O   1 
HETATM 3722 O O   D HOH   J 6 .   ? -12.767 -4.043  -10.016 0.28 26.37  ? 316 HOH   B O   1 
HETATM 3723 O O   A HOH   J 6 .   ? -15.697 -10.367 -15.326 0.22 38.28  ? 317 HOH   B O   1 
HETATM 3724 O O   B HOH   J 6 .   ? -15.695 -10.367 -15.329 0.22 38.28  ? 317 HOH   B O   1 
HETATM 3725 O O   C HOH   J 6 .   ? -16.386 -9.990  -15.565 0.28 50.16  ? 317 HOH   B O   1 
HETATM 3726 O O   D HOH   J 6 .   ? -16.384 -9.991  -15.562 0.28 50.26  ? 317 HOH   B O   1 
HETATM 3727 O O   A HOH   J 6 .   ? -34.474 -6.658  -9.904  0.22 51.51  ? 318 HOH   B O   1 
HETATM 3728 O O   B HOH   J 6 .   ? -34.469 -6.655  -9.907  0.22 51.52  ? 318 HOH   B O   1 
HETATM 3729 O O   C HOH   J 6 .   ? -35.456 -5.253  -10.269 0.28 28.88  ? 318 HOH   B O   1 
HETATM 3730 O O   D HOH   J 6 .   ? -35.456 -5.253  -10.269 0.28 28.89  ? 318 HOH   B O   1 
HETATM 3731 O O   A HOH   J 6 .   ? -6.883  -1.126  -11.059 0.22 31.56  ? 319 HOH   B O   1 
HETATM 3732 O O   B HOH   J 6 .   ? -6.885  -1.127  -11.060 0.22 31.57  ? 319 HOH   B O   1 
HETATM 3733 O O   C HOH   J 6 .   ? -6.088  -0.245  -10.614 0.28 41.95  ? 319 HOH   B O   1 
HETATM 3734 O O   D HOH   J 6 .   ? -6.083  -0.246  -10.612 0.28 41.96  ? 319 HOH   B O   1 
HETATM 3735 O O   A HOH   J 6 .   ? -17.527 -10.408 -16.571 0.22 23.88  ? 320 HOH   B O   1 
HETATM 3736 O O   B HOH   J 6 .   ? -17.527 -10.408 -16.572 0.22 23.88  ? 320 HOH   B O   1 
HETATM 3737 O O   C HOH   J 6 .   ? -18.559 -11.219 -16.354 0.28 25.32  ? 320 HOH   B O   1 
HETATM 3738 O O   D HOH   J 6 .   ? -18.559 -11.219 -16.355 0.28 25.31  ? 320 HOH   B O   1 
HETATM 3739 O O   A HOH   J 6 .   ? -9.822  -7.108  -25.629 0.22 23.17  ? 321 HOH   B O   1 
HETATM 3740 O O   B HOH   J 6 .   ? -9.821  -7.108  -25.628 0.22 23.15  ? 321 HOH   B O   1 
HETATM 3741 O O   C HOH   J 6 .   ? -8.644  -6.202  -25.240 0.28 36.01  ? 321 HOH   B O   1 
HETATM 3742 O O   D HOH   J 6 .   ? -8.649  -6.190  -25.232 0.28 35.96  ? 321 HOH   B O   1 
HETATM 3743 O O   A HOH   J 6 .   ? -16.689 25.539  -12.391 0.22 36.25  ? 322 HOH   B O   1 
HETATM 3744 O O   B HOH   J 6 .   ? -16.689 25.539  -12.390 0.22 36.25  ? 322 HOH   B O   1 
HETATM 3745 O O   A HOH   J 6 .   ? -31.456 7.094   -4.253  0.23 36.07  ? 323 HOH   B O   1 
HETATM 3746 O O   B HOH   J 6 .   ? -31.456 7.094   -4.253  0.23 36.07  ? 323 HOH   B O   1 
HETATM 3747 O O   A HOH   J 6 .   ? -16.124 -14.489 -16.746 0.22 39.28  ? 324 HOH   B O   1 
HETATM 3748 O O   B HOH   J 6 .   ? -16.125 -14.484 -16.744 0.22 39.24  ? 324 HOH   B O   1 
HETATM 3749 O O   C HOH   J 6 .   ? -19.066 -12.053 -13.720 0.28 36.76  ? 324 HOH   B O   1 
HETATM 3750 O O   D HOH   J 6 .   ? -19.066 -12.053 -13.720 0.28 36.76  ? 324 HOH   B O   1 
HETATM 3751 O O   A HOH   J 6 .   ? -21.923 -13.695 -21.504 0.22 34.62  ? 325 HOH   B O   1 
HETATM 3752 O O   B HOH   J 6 .   ? -21.921 -13.699 -21.504 0.22 34.62  ? 325 HOH   B O   1 
HETATM 3753 O O   . HOH   J 6 .   ? -15.195 -4.645  1.443   1.00 37.81  ? 326 HOH   B O   1 
HETATM 3754 O O   A HOH   J 6 .   ? -27.467 -6.919  -5.612  0.22 25.14  ? 327 HOH   B O   1 
HETATM 3755 O O   B HOH   J 6 .   ? -27.467 -6.919  -5.612  0.22 25.14  ? 327 HOH   B O   1 
HETATM 3756 O O   C HOH   J 6 .   ? -24.891 -6.436  -4.339  0.27 32.37  ? 327 HOH   B O   1 
HETATM 3757 O O   D HOH   J 6 .   ? -24.891 -6.436  -4.339  0.27 32.37  ? 327 HOH   B O   1 
HETATM 3758 O O   A HOH   J 6 .   ? -19.447 14.640  -22.658 0.22 48.97  ? 328 HOH   B O   1 
HETATM 3759 O O   B HOH   J 6 .   ? -19.449 14.638  -22.661 0.22 48.97  ? 328 HOH   B O   1 
HETATM 3760 O O   C HOH   J 6 .   ? -18.564 15.043  -22.040 0.28 25.96  ? 328 HOH   B O   1 
HETATM 3761 O O   D HOH   J 6 .   ? -18.564 15.043  -22.040 0.28 25.95  ? 328 HOH   B O   1 
HETATM 3762 O O   A HOH   J 6 .   ? -10.452 6.902   -14.718 0.22 47.40  ? 329 HOH   B O   1 
HETATM 3763 O O   B HOH   J 6 .   ? -10.447 6.899   -14.719 0.22 47.40  ? 329 HOH   B O   1 
HETATM 3764 O O   C HOH   J 6 .   ? -10.872 7.661   -13.696 0.28 32.69  ? 329 HOH   B O   1 
HETATM 3765 O O   D HOH   J 6 .   ? -10.873 7.661   -13.696 0.28 32.69  ? 329 HOH   B O   1 
HETATM 3766 O O   A HOH   J 6 .   ? -20.688 24.104  -16.620 0.22 31.49  ? 330 HOH   B O   1 
HETATM 3767 O O   B HOH   J 6 .   ? -20.688 24.104  -16.620 0.22 31.49  ? 330 HOH   B O   1 
HETATM 3768 O O   C HOH   J 6 .   ? -22.365 14.909  -6.118  0.28 27.25  ? 330 HOH   B O   1 
HETATM 3769 O O   D HOH   J 6 .   ? -22.364 14.908  -6.117  0.28 27.25  ? 330 HOH   B O   1 
HETATM 3770 O O   A HOH   J 6 .   ? -14.990 -15.921 -30.530 0.22 38.52  ? 331 HOH   B O   1 
HETATM 3771 O O   B HOH   J 6 .   ? -14.987 -15.923 -30.531 0.22 38.51  ? 331 HOH   B O   1 
HETATM 3772 O O   C HOH   J 6 .   ? -15.822 -14.046 -30.814 0.28 37.24  ? 331 HOH   B O   1 
HETATM 3773 O O   D HOH   J 6 .   ? -15.823 -14.047 -30.812 0.28 37.24  ? 331 HOH   B O   1 
HETATM 3774 O O   A HOH   J 6 .   ? 1.164   -1.270  -13.986 0.22 45.13  ? 332 HOH   B O   1 
HETATM 3775 O O   B HOH   J 6 .   ? 1.166   -1.270  -13.983 0.22 45.14  ? 332 HOH   B O   1 
HETATM 3776 O O   . HOH   J 6 .   ? -16.338 20.650  -14.077 1.00 55.54  ? 333 HOH   B O   1 
HETATM 3777 O O   C HOH   J 6 .   ? -18.156 0.444   -34.099 0.28 37.42  ? 334 HOH   B O   1 
HETATM 3778 O O   D HOH   J 6 .   ? -18.156 0.444   -34.099 0.28 37.42  ? 334 HOH   B O   1 
HETATM 3779 O O   A HOH   J 6 .   ? -35.232 3.848   -8.984  0.22 14.25  ? 335 HOH   B O   1 
HETATM 3780 O O   B HOH   J 6 .   ? -35.128 4.164   -10.121 0.22 17.86  ? 335 HOH   B O   1 
HETATM 3781 O O   A HOH   J 6 .   ? -17.091 12.846  -5.147  0.22 23.34  ? 336 HOH   B O   1 
HETATM 3782 O O   B HOH   J 6 .   ? -17.091 12.846  -5.147  0.22 23.34  ? 336 HOH   B O   1 
HETATM 3783 O O   C HOH   J 6 .   ? -17.624 12.643  -6.354  0.28 46.91  ? 336 HOH   B O   1 
HETATM 3784 O O   D HOH   J 6 .   ? -17.629 12.645  -6.353  0.28 46.91  ? 336 HOH   B O   1 
HETATM 3785 O O   A HOH   J 6 .   ? -23.710 -14.754 -17.769 0.22 41.04  ? 337 HOH   B O   1 
HETATM 3786 O O   B HOH   J 6 .   ? -23.710 -14.754 -17.763 0.22 41.03  ? 337 HOH   B O   1 
HETATM 3787 O O   C HOH   J 6 .   ? -24.783 -15.587 -17.256 0.27 40.07  ? 337 HOH   B O   1 
HETATM 3788 O O   D HOH   J 6 .   ? -24.783 -15.587 -17.256 0.27 40.07  ? 337 HOH   B O   1 
HETATM 3789 O O   A HOH   J 6 .   ? -23.154 -7.884  -4.202  0.22 60.48  ? 338 HOH   B O   1 
HETATM 3790 O O   B HOH   J 6 .   ? -23.154 -7.884  -4.199  0.22 60.46  ? 338 HOH   B O   1 
HETATM 3791 O O   C HOH   J 6 .   ? -23.463 -6.477  -5.481  0.28 44.55  ? 338 HOH   B O   1 
HETATM 3792 O O   D HOH   J 6 .   ? -23.463 -6.474  -5.486  0.28 44.60  ? 338 HOH   B O   1 
HETATM 3793 O O   A HOH   J 6 .   ? -11.134 11.364  -15.569 0.22 52.54  ? 339 HOH   B O   1 
HETATM 3794 O O   B HOH   J 6 .   ? -11.134 11.370  -15.573 0.22 52.54  ? 339 HOH   B O   1 
HETATM 3795 O O   A HOH   J 6 .   ? -28.629 -7.240  -18.086 0.22 26.93  ? 340 HOH   B O   1 
HETATM 3796 O O   B HOH   J 6 .   ? -28.629 -7.240  -18.086 0.22 26.94  ? 340 HOH   B O   1 
HETATM 3797 O O   C HOH   J 6 .   ? -27.797 -6.099  -18.772 0.28 32.32  ? 340 HOH   B O   1 
HETATM 3798 O O   D HOH   J 6 .   ? -27.797 -6.098  -18.772 0.28 32.32  ? 340 HOH   B O   1 
HETATM 3799 O O   . HOH   J 6 .   ? -3.067  -12.032 -7.009  1.00 36.97  ? 341 HOH   B O   1 
HETATM 3800 O O   A HOH   J 6 .   ? -9.885  1.873   -8.615  0.22 11.42  ? 342 HOH   B O   1 
HETATM 3801 O O   B HOH   J 6 .   ? -9.524  1.691   -7.614  0.22 11.66  ? 342 HOH   B O   1 
HETATM 3802 O O   A HOH   J 6 .   ? -18.539 18.913  -21.690 0.22 37.36  ? 343 HOH   B O   1 
HETATM 3803 O O   B HOH   J 6 .   ? -18.537 18.914  -21.691 0.22 37.36  ? 343 HOH   B O   1 
HETATM 3804 O O   A HOH   J 6 .   ? -10.537 -16.517 -24.427 0.22 27.33  ? 344 HOH   B O   1 
HETATM 3805 O O   B HOH   J 6 .   ? -10.537 -16.517 -24.427 0.22 27.34  ? 344 HOH   B O   1 
HETATM 3806 O O   A HOH   J 6 .   ? -10.849 -4.649  -8.263  0.22 34.94  ? 345 HOH   B O   1 
HETATM 3807 O O   B HOH   J 6 .   ? -10.849 -4.648  -8.264  0.22 34.94  ? 345 HOH   B O   1 
HETATM 3808 O O   C HOH   J 6 .   ? -11.811 -5.561  -8.231  0.28 30.39  ? 345 HOH   B O   1 
HETATM 3809 O O   D HOH   J 6 .   ? -11.812 -5.561  -8.230  0.28 30.39  ? 345 HOH   B O   1 
HETATM 3810 O O   A HOH   J 6 .   ? -29.649 -1.223  -19.228 0.22 28.41  ? 346 HOH   B O   1 
HETATM 3811 O O   B HOH   J 6 .   ? -29.649 -1.223  -19.228 0.22 28.41  ? 346 HOH   B O   1 
HETATM 3812 O O   A HOH   J 6 .   ? -14.958 16.561  -19.928 0.22 28.63  ? 347 HOH   B O   1 
HETATM 3813 O O   B HOH   J 6 .   ? -14.958 16.561  -19.928 0.22 28.63  ? 347 HOH   B O   1 
HETATM 3814 O O   C HOH   J 6 .   ? -15.833 16.097  -20.926 0.28 39.61  ? 347 HOH   B O   1 
HETATM 3815 O O   D HOH   J 6 .   ? -15.836 16.097  -20.925 0.28 39.61  ? 347 HOH   B O   1 
HETATM 3816 O O   A HOH   J 6 .   ? -29.953 -5.260  -1.057  0.22 33.53  ? 348 HOH   B O   1 
HETATM 3817 O O   B HOH   J 6 .   ? -29.953 -5.259  -1.056  0.22 33.53  ? 348 HOH   B O   1 
HETATM 3818 O O   C HOH   J 6 .   ? -28.997 -6.441  -1.066  0.28 31.96  ? 348 HOH   B O   1 
HETATM 3819 O O   D HOH   J 6 .   ? -28.997 -6.441  -1.066  0.28 31.96  ? 348 HOH   B O   1 
HETATM 3820 O O   A HOH   J 6 .   ? -11.770 2.004   -6.065  0.22 18.06  ? 349 HOH   B O   1 
HETATM 3821 O O   B HOH   J 6 .   ? -12.451 2.171   -5.593  0.22 24.12  ? 349 HOH   B O   1 
HETATM 3822 O O   A HOH   J 6 .   ? -31.328 12.965  -16.763 0.22 39.72  ? 350 HOH   B O   1 
HETATM 3823 O O   B HOH   J 6 .   ? -31.324 12.968  -16.760 0.22 39.72  ? 350 HOH   B O   1 
HETATM 3824 O O   C HOH   J 6 .   ? -30.123 12.249  -16.375 0.28 35.29  ? 350 HOH   B O   1 
HETATM 3825 O O   D HOH   J 6 .   ? -30.124 12.249  -16.376 0.28 35.29  ? 350 HOH   B O   1 
HETATM 3826 O O   A HOH   J 6 .   ? -19.311 25.252  -14.210 0.22 35.08  ? 351 HOH   B O   1 
HETATM 3827 O O   B HOH   J 6 .   ? -19.315 25.254  -14.208 0.22 35.08  ? 351 HOH   B O   1 
HETATM 3828 O O   C HOH   J 6 .   ? -19.390 25.097  -15.847 0.28 38.59  ? 351 HOH   B O   1 
HETATM 3829 O O   D HOH   J 6 .   ? -19.390 25.097  -15.847 0.28 38.59  ? 351 HOH   B O   1 
HETATM 3830 O O   A HOH   J 6 .   ? -17.068 26.383  -14.710 0.22 57.94  ? 352 HOH   B O   1 
HETATM 3831 O O   B HOH   J 6 .   ? -17.073 26.388  -14.709 0.22 57.94  ? 352 HOH   B O   1 
HETATM 3832 O O   C HOH   J 6 .   ? -16.505 27.460  -16.544 0.28 37.51  ? 352 HOH   B O   1 
HETATM 3833 O O   D HOH   J 6 .   ? -16.504 27.460  -16.547 0.28 37.52  ? 352 HOH   B O   1 
HETATM 3834 O O   A HOH   J 6 .   ? -25.974 -4.374  -3.798  0.22 26.05  ? 353 HOH   B O   1 
HETATM 3835 O O   B HOH   J 6 .   ? -25.974 -4.373  -3.798  0.22 26.06  ? 353 HOH   B O   1 
HETATM 3836 O O   C HOH   J 6 .   ? -26.278 -5.170  -4.413  0.28 29.05  ? 353 HOH   B O   1 
HETATM 3837 O O   D HOH   J 6 .   ? -26.278 -5.170  -4.413  0.28 29.05  ? 353 HOH   B O   1 
HETATM 3838 O O   C HOH   J 6 .   ? -22.037 -13.874 -25.960 0.28 36.34  ? 354 HOH   B O   1 
HETATM 3839 O O   D HOH   J 6 .   ? -22.037 -13.874 -25.960 0.28 36.34  ? 354 HOH   B O   1 
HETATM 3840 O O   C HOH   J 6 .   ? -9.224  -15.737 -23.877 0.28 30.52  ? 355 HOH   B O   1 
HETATM 3841 O O   D HOH   J 6 .   ? -9.223  -15.737 -23.878 0.28 30.52  ? 355 HOH   B O   1 
HETATM 3842 O O   A HOH   J 6 .   ? -19.446 -13.407 -23.078 0.22 29.14  ? 356 HOH   B O   1 
HETATM 3843 O O   B HOH   J 6 .   ? -19.447 -13.407 -23.078 0.22 29.15  ? 356 HOH   B O   1 
HETATM 3844 O O   C HOH   J 6 .   ? -7.859  10.654  -19.353 0.28 37.36  ? 357 HOH   B O   1 
HETATM 3845 O O   D HOH   J 6 .   ? -7.856  10.651  -19.354 0.28 37.36  ? 357 HOH   B O   1 
HETATM 3846 O O   A HOH   J 6 .   ? -33.931 -1.663  -7.033  0.22 35.02  ? 358 HOH   B O   1 
HETATM 3847 O O   B HOH   J 6 .   ? -33.931 -1.663  -7.033  0.22 35.01  ? 358 HOH   B O   1 
HETATM 3848 O O   C HOH   J 6 .   ? -34.979 -2.838  -6.631  0.28 40.43  ? 358 HOH   B O   1 
HETATM 3849 O O   D HOH   J 6 .   ? -34.981 -2.837  -6.632  0.28 40.42  ? 358 HOH   B O   1 
HETATM 3850 O O   A HOH   J 6 .   ? -21.274 2.372   -0.000  0.22 101.17 ? 359 HOH   B O   1 
HETATM 3851 O O   B HOH   J 6 .   ? -21.274 2.378   -0.000  0.22 101.11 ? 359 HOH   B O   1 
HETATM 3852 O O   A HOH   J 6 .   ? -11.686 -9.546  -1.083  0.22 33.89  ? 360 HOH   B O   1 
HETATM 3853 O O   B HOH   J 6 .   ? -11.688 -9.547  -1.088  0.22 33.90  ? 360 HOH   B O   1 
HETATM 3854 O O   C HOH   J 6 .   ? -12.025 -9.136  0.315   0.28 43.60  ? 360 HOH   B O   1 
HETATM 3855 O O   D HOH   J 6 .   ? -12.028 -9.133  0.318   0.28 43.62  ? 360 HOH   B O   1 
HETATM 3856 O O   A HOH   J 6 .   ? -31.952 -10.342 -6.970  0.21 34.10  ? 361 HOH   B O   1 
HETATM 3857 O O   B HOH   J 6 .   ? -31.952 -10.342 -6.970  0.21 34.10  ? 361 HOH   B O   1 
HETATM 3858 O O   A HOH   J 6 .   ? -8.730  -10.790 -7.444  0.22 37.91  ? 362 HOH   B O   1 
HETATM 3859 O O   B HOH   J 6 .   ? -8.730  -10.791 -7.444  0.22 37.91  ? 362 HOH   B O   1 
HETATM 3860 O O   A HOH   J 6 .   ? -23.290 -5.444  0.844   0.22 30.67  ? 363 HOH   B O   1 
HETATM 3861 O O   B HOH   J 6 .   ? -23.290 -5.444  0.844   0.22 30.67  ? 363 HOH   B O   1 
HETATM 3862 O O   C HOH   J 6 .   ? -22.244 -6.430  0.504   0.28 32.63  ? 363 HOH   B O   1 
HETATM 3863 O O   D HOH   J 6 .   ? -22.244 -6.430  0.504   0.28 32.63  ? 363 HOH   B O   1 
HETATM 3864 O O   A HOH   J 6 .   ? -8.730  12.291  -18.781 0.22 42.54  ? 364 HOH   B O   1 
HETATM 3865 O O   B HOH   J 6 .   ? -8.728  12.295  -18.777 0.22 42.55  ? 364 HOH   B O   1 
HETATM 3866 O O   C HOH   J 6 .   ? -10.713 11.997  -19.094 0.28 33.03  ? 364 HOH   B O   1 
HETATM 3867 O O   D HOH   J 6 .   ? -10.713 11.997  -19.093 0.28 33.03  ? 364 HOH   B O   1 
HETATM 3868 O O   A HOH   J 6 .   ? -26.956 -8.300  -16.621 0.22 31.08  ? 365 HOH   B O   1 
HETATM 3869 O O   B HOH   J 6 .   ? -26.957 -8.299  -16.619 0.22 31.08  ? 365 HOH   B O   1 
HETATM 3870 O O   C HOH   J 6 .   ? -25.509 -8.252  -16.694 0.28 32.16  ? 365 HOH   B O   1 
HETATM 3871 O O   D HOH   J 6 .   ? -25.508 -8.253  -16.692 0.28 32.16  ? 365 HOH   B O   1 
HETATM 3872 O O   A HOH   J 6 .   ? -30.457 -7.815  -4.856  0.22 35.98  ? 366 HOH   B O   1 
HETATM 3873 O O   B HOH   J 6 .   ? -30.460 -7.815  -4.855  0.22 35.98  ? 366 HOH   B O   1 
HETATM 3874 O O   A HOH   J 6 .   ? -20.567 -8.706  -4.610  0.22 46.83  ? 367 HOH   B O   1 
HETATM 3875 O O   B HOH   J 6 .   ? -20.569 -8.701  -4.612  0.22 46.83  ? 367 HOH   B O   1 
HETATM 3876 O O   A HOH   J 6 .   ? -18.576 -10.052 -5.688  0.22 44.21  ? 368 HOH   B O   1 
HETATM 3877 O O   B HOH   J 6 .   ? -18.579 -10.046 -5.686  0.22 44.22  ? 368 HOH   B O   1 
HETATM 3878 O O   C HOH   J 6 .   ? -16.418 -7.185  -8.357  0.28 39.00  ? 368 HOH   B O   1 
HETATM 3879 O O   D HOH   J 6 .   ? -16.418 -7.185  -8.359  0.28 39.00  ? 368 HOH   B O   1 
HETATM 3880 O O   A HOH   J 6 .   ? -31.422 4.663   -2.644  0.23 43.23  ? 369 HOH   B O   1 
HETATM 3881 O O   B HOH   J 6 .   ? -31.422 4.663   -2.644  0.23 43.23  ? 369 HOH   B O   1 
HETATM 3882 O O   C HOH   J 6 .   ? -30.577 4.575   -2.692  0.27 54.16  ? 369 HOH   B O   1 
HETATM 3883 O O   D HOH   J 6 .   ? -30.577 4.575   -2.692  0.27 54.16  ? 369 HOH   B O   1 
HETATM 3884 O O   A HOH   J 6 .   ? -10.439 21.785  -14.154 0.22 50.83  ? 370 HOH   B O   1 
HETATM 3885 O O   B HOH   J 6 .   ? -10.439 21.791  -14.152 0.22 50.83  ? 370 HOH   B O   1 
HETATM 3886 O O   A HOH   J 6 .   ? -17.289 16.800  -21.914 0.22 31.65  ? 371 HOH   B O   1 
HETATM 3887 O O   B HOH   J 6 .   ? -17.288 16.800  -21.915 0.22 31.65  ? 371 HOH   B O   1 
HETATM 3888 O O   A HOH   J 6 .   ? -10.948 -12.667 -8.967  0.22 43.49  ? 372 HOH   B O   1 
HETATM 3889 O O   B HOH   J 6 .   ? -10.946 -12.669 -8.962  0.22 43.49  ? 372 HOH   B O   1 
HETATM 3890 O O   C HOH   J 6 .   ? -10.767 -11.018 -8.258  0.28 55.85  ? 372 HOH   B O   1 
HETATM 3891 O O   D HOH   J 6 .   ? -10.764 -11.023 -8.260  0.28 55.85  ? 372 HOH   B O   1 
HETATM 3892 O O   A HOH   J 6 .   ? -17.372 14.565  -31.826 0.22 51.74  ? 373 HOH   B O   1 
HETATM 3893 O O   B HOH   J 6 .   ? -17.374 14.563  -31.825 0.22 51.76  ? 373 HOH   B O   1 
HETATM 3894 O O   C HOH   J 6 .   ? -17.321 14.960  -30.470 0.28 33.93  ? 373 HOH   B O   1 
HETATM 3895 O O   D HOH   J 6 .   ? -17.321 14.959  -30.467 0.28 33.93  ? 373 HOH   B O   1 
HETATM 3896 O O   A HOH   J 6 .   ? -31.104 -2.649  -21.407 0.22 37.98  ? 374 HOH   B O   1 
HETATM 3897 O O   B HOH   J 6 .   ? -31.108 -2.652  -21.405 0.22 37.99  ? 374 HOH   B O   1 
HETATM 3898 O O   A HOH   J 6 .   ? -30.182 -12.367 -27.040 0.25 87.79  ? 375 HOH   B O   1 
HETATM 3899 O O   B HOH   J 6 .   ? -30.182 -12.367 -27.040 0.25 87.79  ? 375 HOH   B O   1 
HETATM 3900 O O   A HOH   J 6 .   ? -9.115  5.494   -6.962  0.22 22.19  ? 376 HOH   B O   1 
HETATM 3901 O O   B HOH   J 6 .   ? -10.701 3.932   -6.009  0.22 26.19  ? 376 HOH   B O   1 
HETATM 3902 O O   A HOH   J 6 .   ? -21.274 4.930   -0.000  0.22 87.85  ? 377 HOH   B O   1 
HETATM 3903 O O   B HOH   J 6 .   ? -21.274 4.934   -0.000  0.22 87.85  ? 377 HOH   B O   1 
HETATM 3904 O O   C HOH   J 6 .   ? -21.274 6.930   -0.000  0.28 55.79  ? 377 HOH   B O   1 
HETATM 3905 O O   D HOH   J 6 .   ? -21.274 6.930   -0.000  0.28 55.83  ? 377 HOH   B O   1 
HETATM 3906 O O   A HOH   J 6 .   ? -13.690 -7.950  -0.330  0.22 48.62  ? 378 HOH   B O   1 
HETATM 3907 O O   B HOH   J 6 .   ? -13.690 -7.956  -0.333  0.22 48.62  ? 378 HOH   B O   1 
HETATM 3908 O O   C HOH   J 6 .   ? -14.613 -6.505  -1.567  0.28 36.75  ? 378 HOH   B O   1 
HETATM 3909 O O   D HOH   J 6 .   ? -14.613 -6.505  -1.565  0.28 36.75  ? 378 HOH   B O   1 
HETATM 3910 O O   A HOH   J 6 .   ? -11.643 -7.177  2.253   0.22 36.00  ? 379 HOH   B O   1 
HETATM 3911 O O   B HOH   J 6 .   ? -11.647 -7.175  2.252   0.22 36.00  ? 379 HOH   B O   1 
# 
