data_7HGK
# 
_entry.id   7HGK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HGK         pdb_00007hgk 10.2210/pdb7hgk/pdb 
WWPDB D_1001407446 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HGK 
_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   2024-08-29 
_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           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
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 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '3-cyclohexyl-1-(morpholin-4-yl)propan-1-one'      225.327   1   ? ?    ? ? 
5 water       nat water                                              18.015    233 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                 SO4 
3 1,2-ETHANEDIOL                                EDO 
4 '3-cyclohexyl-1-(morpholin-4-yl)propan-1-one' NW4 
5 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                      ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                    ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                               ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                      ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
NW4 non-polymer         . '3-cyclohexyl-1-(morpholin-4-yl)propan-1-one' ?                 'C13 H23 N O2'   225.327 
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  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 ?  ?   ?   B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  ?  ?   ?   C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NW4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NW4 
_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 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 NW4 1   103 101 NW4 LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 259 HOH HOH A . 
M 5 HOH 3   203 66  HOH HOH A . 
M 5 HOH 4   204 202 HOH HOH A . 
M 5 HOH 5   205 84  HOH HOH A . 
M 5 HOH 6   206 208 HOH HOH A . 
M 5 HOH 7   207 91  HOH HOH A . 
M 5 HOH 8   208 293 HOH HOH A . 
M 5 HOH 9   209 55  HOH HOH A . 
M 5 HOH 10  210 34  HOH HOH A . 
M 5 HOH 11  211 86  HOH HOH A . 
M 5 HOH 12  212 97  HOH HOH A . 
M 5 HOH 13  213 85  HOH HOH A . 
M 5 HOH 14  214 260 HOH HOH A . 
M 5 HOH 15  215 304 HOH HOH A . 
M 5 HOH 16  216 199 HOH HOH A . 
M 5 HOH 17  217 139 HOH HOH A . 
M 5 HOH 18  218 26  HOH HOH A . 
M 5 HOH 19  219 301 HOH HOH A . 
M 5 HOH 20  220 167 HOH HOH A . 
M 5 HOH 21  221 71  HOH HOH A . 
M 5 HOH 22  222 292 HOH HOH A . 
M 5 HOH 23  223 289 HOH HOH A . 
M 5 HOH 24  224 87  HOH HOH A . 
M 5 HOH 25  225 23  HOH HOH A . 
M 5 HOH 26  226 7   HOH HOH A . 
M 5 HOH 27  227 8   HOH HOH A . 
M 5 HOH 28  228 95  HOH HOH A . 
M 5 HOH 29  229 28  HOH HOH A . 
M 5 HOH 30  230 190 HOH HOH A . 
M 5 HOH 31  231 188 HOH HOH A . 
M 5 HOH 32  232 93  HOH HOH A . 
M 5 HOH 33  233 32  HOH HOH A . 
M 5 HOH 34  234 2   HOH HOH A . 
M 5 HOH 35  235 37  HOH HOH A . 
M 5 HOH 36  236 290 HOH HOH A . 
M 5 HOH 37  237 179 HOH HOH A . 
M 5 HOH 38  238 218 HOH HOH A . 
M 5 HOH 39  239 78  HOH HOH A . 
M 5 HOH 40  240 38  HOH HOH A . 
M 5 HOH 41  241 288 HOH HOH A . 
M 5 HOH 42  242 42  HOH HOH A . 
M 5 HOH 43  243 278 HOH HOH A . 
M 5 HOH 44  244 115 HOH HOH A . 
M 5 HOH 45  245 27  HOH HOH A . 
M 5 HOH 46  246 77  HOH HOH A . 
M 5 HOH 47  247 111 HOH HOH A . 
M 5 HOH 48  248 267 HOH HOH A . 
M 5 HOH 49  249 41  HOH HOH A . 
M 5 HOH 50  250 12  HOH HOH A . 
M 5 HOH 51  251 145 HOH HOH A . 
M 5 HOH 52  252 73  HOH HOH A . 
M 5 HOH 53  253 58  HOH HOH A . 
M 5 HOH 54  254 274 HOH HOH A . 
M 5 HOH 55  255 1   HOH HOH A . 
M 5 HOH 56  256 60  HOH HOH A . 
M 5 HOH 57  257 203 HOH HOH A . 
M 5 HOH 58  258 109 HOH HOH A . 
M 5 HOH 59  259 211 HOH HOH A . 
M 5 HOH 60  260 297 HOH HOH A . 
M 5 HOH 61  261 94  HOH HOH A . 
M 5 HOH 62  262 20  HOH HOH A . 
M 5 HOH 63  263 18  HOH HOH A . 
M 5 HOH 64  264 143 HOH HOH A . 
M 5 HOH 65  265 99  HOH HOH A . 
M 5 HOH 66  266 318 HOH HOH A . 
M 5 HOH 67  267 222 HOH HOH A . 
M 5 HOH 68  268 300 HOH HOH A . 
M 5 HOH 69  269 14  HOH HOH A . 
M 5 HOH 70  270 116 HOH HOH A . 
M 5 HOH 71  271 21  HOH HOH A . 
M 5 HOH 72  272 164 HOH HOH A . 
M 5 HOH 73  273 299 HOH HOH A . 
M 5 HOH 74  274 9   HOH HOH A . 
M 5 HOH 75  275 165 HOH HOH A . 
M 5 HOH 76  276 281 HOH HOH A . 
M 5 HOH 77  277 131 HOH HOH A . 
M 5 HOH 78  278 152 HOH HOH A . 
M 5 HOH 79  279 16  HOH HOH A . 
M 5 HOH 80  280 19  HOH HOH A . 
M 5 HOH 81  281 47  HOH HOH A . 
M 5 HOH 82  282 64  HOH HOH A . 
M 5 HOH 83  283 31  HOH HOH A . 
M 5 HOH 84  284 22  HOH HOH A . 
M 5 HOH 85  285 146 HOH HOH A . 
M 5 HOH 86  286 113 HOH HOH A . 
M 5 HOH 87  287 327 HOH HOH A . 
M 5 HOH 88  288 83  HOH HOH A . 
M 5 HOH 89  289 185 HOH HOH A . 
M 5 HOH 90  290 210 HOH HOH A . 
M 5 HOH 91  291 108 HOH HOH A . 
M 5 HOH 92  292 63  HOH HOH A . 
M 5 HOH 93  293 219 HOH HOH A . 
M 5 HOH 94  294 283 HOH HOH A . 
M 5 HOH 95  295 57  HOH HOH A . 
M 5 HOH 96  296 35  HOH HOH A . 
M 5 HOH 97  297 205 HOH HOH A . 
M 5 HOH 98  298 75  HOH HOH A . 
M 5 HOH 99  299 332 HOH HOH A . 
M 5 HOH 100 300 156 HOH HOH A . 
M 5 HOH 101 301 313 HOH HOH A . 
M 5 HOH 102 302 125 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 279 HOH HOH B . 
N 5 HOH 3   203 68  HOH HOH B . 
N 5 HOH 4   204 258 HOH HOH B . 
N 5 HOH 5   205 89  HOH HOH B . 
N 5 HOH 6   206 184 HOH HOH B . 
N 5 HOH 7   207 272 HOH HOH B . 
N 5 HOH 8   208 79  HOH HOH B . 
N 5 HOH 9   209 215 HOH HOH B . 
N 5 HOH 10  210 98  HOH HOH B . 
N 5 HOH 11  211 242 HOH HOH B . 
N 5 HOH 12  212 69  HOH HOH B . 
N 5 HOH 13  213 172 HOH HOH B . 
N 5 HOH 14  214 331 HOH HOH B . 
N 5 HOH 15  215 117 HOH HOH B . 
N 5 HOH 16  216 123 HOH HOH B . 
N 5 HOH 17  217 54  HOH HOH B . 
N 5 HOH 18  218 329 HOH HOH B . 
N 5 HOH 19  219 249 HOH HOH B . 
N 5 HOH 20  220 96  HOH HOH B . 
N 5 HOH 21  221 153 HOH HOH B . 
N 5 HOH 22  222 150 HOH HOH B . 
N 5 HOH 23  223 59  HOH HOH B . 
N 5 HOH 24  224 137 HOH HOH B . 
N 5 HOH 25  225 10  HOH HOH B . 
N 5 HOH 26  226 168 HOH HOH B . 
N 5 HOH 27  227 261 HOH HOH B . 
N 5 HOH 28  228 280 HOH HOH B . 
N 5 HOH 29  229 17  HOH HOH B . 
N 5 HOH 30  230 320 HOH HOH B . 
N 5 HOH 31  231 6   HOH HOH B . 
N 5 HOH 32  232 5   HOH HOH B . 
N 5 HOH 33  233 101 HOH HOH B . 
N 5 HOH 34  234 169 HOH HOH B . 
N 5 HOH 35  235 197 HOH HOH B . 
N 5 HOH 36  236 61  HOH HOH B . 
N 5 HOH 37  237 24  HOH HOH B . 
N 5 HOH 38  238 170 HOH HOH B . 
N 5 HOH 39  239 214 HOH HOH B . 
N 5 HOH 40  240 74  HOH HOH B . 
N 5 HOH 41  241 36  HOH HOH B . 
N 5 HOH 42  242 25  HOH HOH B . 
N 5 HOH 43  243 319 HOH HOH B . 
N 5 HOH 44  244 72  HOH HOH B . 
N 5 HOH 45  245 315 HOH HOH B . 
N 5 HOH 46  246 120 HOH HOH B . 
N 5 HOH 47  247 224 HOH HOH B . 
N 5 HOH 48  248 157 HOH HOH B . 
N 5 HOH 49  249 223 HOH HOH B . 
N 5 HOH 50  250 76  HOH HOH B . 
N 5 HOH 51  251 217 HOH HOH B . 
N 5 HOH 52  252 119 HOH HOH B . 
N 5 HOH 53  253 175 HOH HOH B . 
N 5 HOH 54  254 13  HOH HOH B . 
N 5 HOH 55  255 44  HOH HOH B . 
N 5 HOH 56  256 201 HOH HOH B . 
N 5 HOH 57  257 160 HOH HOH B . 
N 5 HOH 58  258 303 HOH HOH B . 
N 5 HOH 59  259 182 HOH HOH B . 
N 5 HOH 60  260 104 HOH HOH B . 
N 5 HOH 61  261 46  HOH HOH B . 
N 5 HOH 62  262 163 HOH HOH B . 
N 5 HOH 63  263 291 HOH HOH B . 
N 5 HOH 64  264 177 HOH HOH B . 
N 5 HOH 65  265 322 HOH HOH B . 
N 5 HOH 66  266 316 HOH HOH B . 
N 5 HOH 67  267 103 HOH HOH B . 
N 5 HOH 68  268 314 HOH HOH B . 
N 5 HOH 69  269 107 HOH HOH B . 
N 5 HOH 70  270 309 HOH HOH B . 
N 5 HOH 71  271 312 HOH HOH B . 
N 5 HOH 72  272 310 HOH HOH B . 
O 5 HOH 1   201 254 HOH HOH C . 
O 5 HOH 2   202 317 HOH HOH C . 
O 5 HOH 3   203 161 HOH HOH C . 
O 5 HOH 4   204 323 HOH HOH C . 
O 5 HOH 5   205 226 HOH HOH C . 
O 5 HOH 6   206 173 HOH HOH C . 
O 5 HOH 7   207 134 HOH HOH C . 
O 5 HOH 8   208 151 HOH HOH C . 
O 5 HOH 9   209 269 HOH HOH C . 
O 5 HOH 10  210 284 HOH HOH C . 
O 5 HOH 11  211 15  HOH HOH C . 
O 5 HOH 12  212 296 HOH HOH C . 
O 5 HOH 13  213 271 HOH HOH C . 
O 5 HOH 14  214 118 HOH HOH C . 
O 5 HOH 15  215 142 HOH HOH C . 
O 5 HOH 16  216 189 HOH HOH C . 
O 5 HOH 17  217 302 HOH HOH C . 
O 5 HOH 18  218 45  HOH HOH C . 
O 5 HOH 19  219 90  HOH HOH C . 
O 5 HOH 20  220 4   HOH HOH C . 
O 5 HOH 21  221 102 HOH HOH C . 
O 5 HOH 22  222 49  HOH HOH C . 
O 5 HOH 23  223 132 HOH HOH C . 
O 5 HOH 24  224 122 HOH HOH C . 
O 5 HOH 25  225 275 HOH HOH C . 
O 5 HOH 26  226 326 HOH HOH C . 
O 5 HOH 27  227 82  HOH HOH C . 
O 5 HOH 28  228 43  HOH HOH C . 
O 5 HOH 29  229 294 HOH HOH C . 
O 5 HOH 30  230 40  HOH HOH C . 
O 5 HOH 31  231 298 HOH HOH C . 
O 5 HOH 32  232 48  HOH HOH C . 
O 5 HOH 33  233 126 HOH HOH C . 
O 5 HOH 34  234 62  HOH HOH C . 
O 5 HOH 35  235 56  HOH HOH C . 
O 5 HOH 36  236 149 HOH HOH C . 
O 5 HOH 37  237 209 HOH HOH C . 
O 5 HOH 38  238 53  HOH HOH C . 
O 5 HOH 39  239 198 HOH HOH C . 
O 5 HOH 40  240 287 HOH HOH C . 
O 5 HOH 41  241 135 HOH HOH C . 
O 5 HOH 42  242 325 HOH HOH C . 
O 5 HOH 43  243 246 HOH HOH C . 
O 5 HOH 44  244 130 HOH HOH C . 
O 5 HOH 45  245 148 HOH HOH C . 
O 5 HOH 46  246 171 HOH HOH C . 
O 5 HOH 47  247 321 HOH HOH C . 
O 5 HOH 48  248 328 HOH HOH C . 
O 5 HOH 49  249 305 HOH HOH C . 
O 5 HOH 50  250 65  HOH HOH C . 
O 5 HOH 51  251 67  HOH HOH C . 
O 5 HOH 52  252 330 HOH HOH C . 
O 5 HOH 53  253 295 HOH HOH C . 
O 5 HOH 54  254 241 HOH HOH C . 
O 5 HOH 55  255 70  HOH HOH C . 
O 5 HOH 56  256 270 HOH HOH C . 
O 5 HOH 57  257 324 HOH HOH C . 
O 5 HOH 58  258 92  HOH HOH C . 
O 5 HOH 59  259 206 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
19 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
20 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
21 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
22 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
23 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
24 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
25 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
26 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
27 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
28 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
29 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
30 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
31 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
32 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
33 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
34 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
35 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
36 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
37 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
38 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
39 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
40 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
41 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
42 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
43 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
44 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
45 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
46 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
47 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
48 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
49 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
50 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
51 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
52 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
53 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
54 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGK 
_cell.length_a           41.583 
_cell.length_b           42.028 
_cell.length_c           158.253 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HGK 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.entry_id          7HGK 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.76 
_exptl_crystal.density_percent_sol   55.0 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              4.6 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    '28% PEG MME 2000; 0.15 M ammonium sulfate; 0.1 M sodium acetate pH 4.6' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2021-05-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.918076 
_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        0.918076 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HGK 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.13 
_reflns.d_resolution_high            1.59 
_reflns.number_obs                   38526 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.057 
_reflns.pdbx_netI_over_sigmaI        13.7 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.062 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     242606 
_reflns.pdbx_chi_squared             0.88 
_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                  1.59 
_reflns_shell.d_res_low                   1.67 
_reflns_shell.number_measured_all         30571 
_reflns_shell.number_unique_obs           5545 
_reflns_shell.Rmerge_I_obs                1.867 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             5.5 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.064 
_reflns_shell.pdbx_Rpim_I_all             0.869 
_reflns_shell.pdbx_CC_half                0.427 
_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                                 7HGK 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     36168 
_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                             79.13 
_refine.ls_d_res_high                            1.59 
_refine.ls_percent_reflns_obs                    99.17 
_refine.ls_R_factor_obs                          0.21212 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20983 
_refine.ls_R_factor_R_free                       0.25332 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1992 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               37.922 
_refine.aniso_B[1][1]                            0.33 
_refine.aniso_B[2][2]                            0.89 
_refine.aniso_B[3][3]                            -1.22 
_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                    'BABINET MODEL WITH 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                                  ? 
_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                       0.103 
_refine.pdbx_overall_ESU_R_Free                  0.106 
_refine.overall_SU_ML                            0.095 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.882 
_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        2107 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             233 
_refine_hist.number_atoms_total               2394 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        79.13 
# 
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             0.009  0.012  ? 2263 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.731  1.834  ? 3077 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.272  5.000  ? 261  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.665  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.982 10.000 ? 296  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 283  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1850 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    '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                  3.455  3.523  ? 1058 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.719  6.284  ? 1314 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.402  3.894  ? 1205 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.399  50.85  ? 3434 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    '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                       1.588 
_refine_ls_shell.d_res_low                        1.629 
_refine_ls_shell.number_reflns_R_work             2403 
_refine_ls_shell.R_factor_R_work                  0.371 
_refine_ls_shell.percent_reflns_obs               90.55 
_refine_ls_shell.R_factor_R_free                  0.359 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             117 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGK 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z31721798' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGK 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
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 7HGK A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGK B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGK C 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
# 
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 7HGK GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGK SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGK GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGK SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGK GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGK SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? 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 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 GLU B 50 ? LEU B 54 ? GLU B 49 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
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 ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGK 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  B HOH 228 ? ? O B HOH 265 ? ? 1.63 
2 1 O2 A SO4 104 ? ? O A HOH 201 ? ? 1.80 
3 1 O  B HOH 258 ? ? O B HOH 265 ? ? 2.05 
4 1 O  B HOH 213 ? ? O B HOH 237 ? ? 2.06 
5 1 O  B ASP 27  ? B O B HOH 201 ? ? 2.15 
6 1 O4 C SO4 102 ? ? O C HOH 201 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 228 ? ? 1_555 O A HOH 279 ? ? 4_545 1.98 
2 1 O A HOH 285 ? ? 1_555 O C HOH 257 ? ? 4_445 2.16 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              24 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              24 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              24 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.28 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -3.02 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 16 ? ? -37.58  122.06 
2 1 ASN A 87 ? ? -153.54 67.39  
3 1 ASN B 38 ? ? 82.07   -2.58  
4 1 HIS B 48 ? ? -103.04 40.46  
5 1 ASN B 87 ? ? -162.37 60.57  
6 1 ASN C 87 ? ? -150.95 55.71  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.089 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C HIS 3  ? C HIS 4  
12 1 Y 1 C ASP 27 ? C ASP 28 
13 1 Y 1 C ILE 28 ? C ILE 29 
14 1 Y 1 C ALA 29 ? C ALA 30 
15 1 Y 1 C ASP 30 ? C ASP 31 
16 1 Y 1 C GLY 31 ? C GLY 32 
17 1 Y 1 C ALA 32 ? C ALA 33 
18 1 Y 1 C VAL 33 ? C VAL 34 
19 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
NW4 N1   N N N 260 
NW4 C4   C N N 261 
NW4 C5   C N N 262 
NW4 C6   C N N 263 
NW4 C7   C N N 264 
NW4 C8   C N N 265 
NW4 C10  C N N 266 
NW4 C13  C N N 267 
NW4 C1   C N N 268 
NW4 C11  C N N 269 
NW4 C12  C N N 270 
NW4 C2   C N N 271 
NW4 C3   C N N 272 
NW4 C9   C N N 273 
NW4 O1   O N N 274 
NW4 O2   O N N 275 
NW4 H1   H N N 276 
NW4 H2   H N N 277 
NW4 H3   H N N 278 
NW4 H4   H N N 279 
NW4 H5   H N N 280 
NW4 H6   H N N 281 
NW4 H7   H N N 282 
NW4 H8   H N N 283 
NW4 H9   H N N 284 
NW4 H10  H N N 285 
NW4 H11  H N N 286 
NW4 H12  H N N 287 
NW4 H13  H N N 288 
NW4 H14  H N N 289 
NW4 H15  H N N 290 
NW4 H16  H N N 291 
NW4 H17  H N N 292 
NW4 H18  H N N 293 
NW4 H19  H N N 294 
NW4 H20  H N N 295 
NW4 H21  H N N 296 
NW4 H22  H N N 297 
NW4 H23  H N N 298 
PHE N    N N N 299 
PHE CA   C N S 300 
PHE C    C N N 301 
PHE O    O N N 302 
PHE CB   C N N 303 
PHE CG   C Y N 304 
PHE CD1  C Y N 305 
PHE CD2  C Y N 306 
PHE CE1  C Y N 307 
PHE CE2  C Y N 308 
PHE CZ   C Y N 309 
PHE OXT  O N N 310 
PHE H    H N N 311 
PHE H2   H N N 312 
PHE HA   H N N 313 
PHE HB2  H N N 314 
PHE HB3  H N N 315 
PHE HD1  H N N 316 
PHE HD2  H N N 317 
PHE HE1  H N N 318 
PHE HE2  H N N 319 
PHE HZ   H N N 320 
PHE HXT  H N N 321 
PRO N    N N N 322 
PRO CA   C N S 323 
PRO C    C N N 324 
PRO O    O N N 325 
PRO CB   C N N 326 
PRO CG   C N N 327 
PRO CD   C N N 328 
PRO OXT  O N N 329 
PRO H    H N N 330 
PRO HA   H N N 331 
PRO HB2  H N N 332 
PRO HB3  H N N 333 
PRO HG2  H N N 334 
PRO HG3  H N N 335 
PRO HD2  H N N 336 
PRO HD3  H N N 337 
PRO HXT  H N N 338 
SER N    N N N 339 
SER CA   C N S 340 
SER C    C N N 341 
SER O    O N N 342 
SER CB   C N N 343 
SER OG   O N N 344 
SER OXT  O N N 345 
SER H    H N N 346 
SER H2   H N N 347 
SER HA   H N N 348 
SER HB2  H N N 349 
SER HB3  H N N 350 
SER HG   H N N 351 
SER HXT  H N N 352 
SO4 S    S N N 353 
SO4 O1   O N N 354 
SO4 O2   O N N 355 
SO4 O3   O N N 356 
SO4 O4   O N N 357 
THR N    N N N 358 
THR CA   C N S 359 
THR C    C N N 360 
THR O    O N N 361 
THR CB   C N R 362 
THR OG1  O N N 363 
THR CG2  C N N 364 
THR OXT  O N N 365 
THR H    H N N 366 
THR H2   H N N 367 
THR HA   H N N 368 
THR HB   H N N 369 
THR HG1  H N N 370 
THR HG21 H N N 371 
THR HG22 H N N 372 
THR HG23 H N N 373 
THR HXT  H N N 374 
TRP N    N N N 375 
TRP CA   C N S 376 
TRP C    C N N 377 
TRP O    O N N 378 
TRP CB   C N N 379 
TRP CG   C Y N 380 
TRP CD1  C Y N 381 
TRP CD2  C Y N 382 
TRP NE1  N Y N 383 
TRP CE2  C Y N 384 
TRP CE3  C Y N 385 
TRP CZ2  C Y N 386 
TRP CZ3  C Y N 387 
TRP CH2  C Y N 388 
TRP OXT  O N N 389 
TRP H    H N N 390 
TRP H2   H N N 391 
TRP HA   H N N 392 
TRP HB2  H N N 393 
TRP HB3  H N N 394 
TRP HD1  H N N 395 
TRP HE1  H N N 396 
TRP HE3  H N N 397 
TRP HZ2  H N N 398 
TRP HZ3  H N N 399 
TRP HH2  H N N 400 
TRP HXT  H N N 401 
TYR N    N N N 402 
TYR CA   C N S 403 
TYR C    C N N 404 
TYR O    O N N 405 
TYR CB   C N N 406 
TYR CG   C Y N 407 
TYR CD1  C Y N 408 
TYR CD2  C Y N 409 
TYR CE1  C Y N 410 
TYR CE2  C Y N 411 
TYR CZ   C Y N 412 
TYR OH   O N N 413 
TYR OXT  O N N 414 
TYR H    H N N 415 
TYR H2   H N N 416 
TYR HA   H N N 417 
TYR HB2  H N N 418 
TYR HB3  H N N 419 
TYR HD1  H N N 420 
TYR HD2  H N N 421 
TYR HE1  H N N 422 
TYR HE2  H N N 423 
TYR HH   H N N 424 
TYR HXT  H N N 425 
VAL N    N N N 426 
VAL CA   C N S 427 
VAL C    C N N 428 
VAL O    O N N 429 
VAL CB   C N N 430 
VAL CG1  C N N 431 
VAL CG2  C N N 432 
VAL OXT  O N N 433 
VAL H    H N N 434 
VAL H2   H N N 435 
VAL HA   H N N 436 
VAL HB   H N N 437 
VAL HG11 H N N 438 
VAL HG12 H N N 439 
VAL HG13 H N N 440 
VAL HG21 H N N 441 
VAL HG22 H N N 442 
VAL HG23 H N N 443 
VAL HXT  H N N 444 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
NW4 C2  C1   sing N N 246 
NW4 C2  C3   sing N N 247 
NW4 C4  C9   sing N N 248 
NW4 C4  C3   sing N N 249 
NW4 C4  C5   sing N N 250 
NW4 C9  C8   sing N N 251 
NW4 C13 N1   sing N N 252 
NW4 C13 C12  sing N N 253 
NW4 C1  O1   doub N N 254 
NW4 C1  N1   sing N N 255 
NW4 C5  C6   sing N N 256 
NW4 N1  C10  sing N N 257 
NW4 C6  C7   sing N N 258 
NW4 C12 O2   sing N N 259 
NW4 C8  C7   sing N N 260 
NW4 C10 C11  sing N N 261 
NW4 O2  C11  sing N N 262 
NW4 C4  H1   sing N N 263 
NW4 C5  H2   sing N N 264 
NW4 C5  H3   sing N N 265 
NW4 C6  H4   sing N N 266 
NW4 C6  H5   sing N N 267 
NW4 C7  H6   sing N N 268 
NW4 C7  H7   sing N N 269 
NW4 C8  H8   sing N N 270 
NW4 C8  H9   sing N N 271 
NW4 C10 H10  sing N N 272 
NW4 C10 H11  sing N N 273 
NW4 C13 H12  sing N N 274 
NW4 C13 H13  sing N N 275 
NW4 C11 H14  sing N N 276 
NW4 C11 H15  sing N N 277 
NW4 C12 H16  sing N N 278 
NW4 C12 H17  sing N N 279 
NW4 C2  H18  sing N N 280 
NW4 C2  H19  sing N N 281 
NW4 C3  H20  sing N N 282 
NW4 C3  H21  sing N N 283 
NW4 C9  H22  sing N N 284 
NW4 C9  H23  sing N N 285 
PHE N   CA   sing N N 286 
PHE N   H    sing N N 287 
PHE N   H2   sing N N 288 
PHE CA  C    sing N N 289 
PHE CA  CB   sing N N 290 
PHE CA  HA   sing N N 291 
PHE C   O    doub N N 292 
PHE C   OXT  sing N N 293 
PHE CB  CG   sing N N 294 
PHE CB  HB2  sing N N 295 
PHE CB  HB3  sing N N 296 
PHE CG  CD1  doub Y N 297 
PHE CG  CD2  sing Y N 298 
PHE CD1 CE1  sing Y N 299 
PHE CD1 HD1  sing N N 300 
PHE CD2 CE2  doub Y N 301 
PHE CD2 HD2  sing N N 302 
PHE CE1 CZ   doub Y N 303 
PHE CE1 HE1  sing N N 304 
PHE CE2 CZ   sing Y N 305 
PHE CE2 HE2  sing N N 306 
PHE CZ  HZ   sing N N 307 
PHE OXT HXT  sing N N 308 
PRO N   CA   sing N N 309 
PRO N   CD   sing N N 310 
PRO N   H    sing N N 311 
PRO CA  C    sing N N 312 
PRO CA  CB   sing N N 313 
PRO CA  HA   sing N N 314 
PRO C   O    doub N N 315 
PRO C   OXT  sing N N 316 
PRO CB  CG   sing N N 317 
PRO CB  HB2  sing N N 318 
PRO CB  HB3  sing N N 319 
PRO CG  CD   sing N N 320 
PRO CG  HG2  sing N N 321 
PRO CG  HG3  sing N N 322 
PRO CD  HD2  sing N N 323 
PRO CD  HD3  sing N N 324 
PRO OXT HXT  sing N N 325 
SER N   CA   sing N N 326 
SER N   H    sing N N 327 
SER N   H2   sing N N 328 
SER CA  C    sing N N 329 
SER CA  CB   sing N N 330 
SER CA  HA   sing N N 331 
SER C   O    doub N N 332 
SER C   OXT  sing N N 333 
SER CB  OG   sing N N 334 
SER CB  HB2  sing N N 335 
SER CB  HB3  sing N N 336 
SER OG  HG   sing N N 337 
SER OXT HXT  sing N N 338 
SO4 S   O1   doub N N 339 
SO4 S   O2   doub N N 340 
SO4 S   O3   sing N N 341 
SO4 S   O4   sing N N 342 
THR N   CA   sing N N 343 
THR N   H    sing N N 344 
THR N   H2   sing N N 345 
THR CA  C    sing N N 346 
THR CA  CB   sing N N 347 
THR CA  HA   sing N N 348 
THR C   O    doub N N 349 
THR C   OXT  sing N N 350 
THR CB  OG1  sing N N 351 
THR CB  CG2  sing N N 352 
THR CB  HB   sing N N 353 
THR OG1 HG1  sing N N 354 
THR CG2 HG21 sing N N 355 
THR CG2 HG22 sing N N 356 
THR CG2 HG23 sing N N 357 
THR OXT HXT  sing N N 358 
TRP N   CA   sing N N 359 
TRP N   H    sing N N 360 
TRP N   H2   sing N N 361 
TRP CA  C    sing N N 362 
TRP CA  CB   sing N N 363 
TRP CA  HA   sing N N 364 
TRP C   O    doub N N 365 
TRP C   OXT  sing N N 366 
TRP CB  CG   sing N N 367 
TRP CB  HB2  sing N N 368 
TRP CB  HB3  sing N N 369 
TRP CG  CD1  doub Y N 370 
TRP CG  CD2  sing Y N 371 
TRP CD1 NE1  sing Y N 372 
TRP CD1 HD1  sing N N 373 
TRP CD2 CE2  doub Y N 374 
TRP CD2 CE3  sing Y N 375 
TRP NE1 CE2  sing Y N 376 
TRP NE1 HE1  sing N N 377 
TRP CE2 CZ2  sing Y N 378 
TRP CE3 CZ3  doub Y N 379 
TRP CE3 HE3  sing N N 380 
TRP CZ2 CH2  doub Y N 381 
TRP CZ2 HZ2  sing N N 382 
TRP CZ3 CH2  sing Y N 383 
TRP CZ3 HZ3  sing N N 384 
TRP CH2 HH2  sing N N 385 
TRP OXT HXT  sing N N 386 
TYR N   CA   sing N N 387 
TYR N   H    sing N N 388 
TYR N   H2   sing N N 389 
TYR CA  C    sing N N 390 
TYR CA  CB   sing N N 391 
TYR CA  HA   sing N N 392 
TYR C   O    doub N N 393 
TYR C   OXT  sing N N 394 
TYR CB  CG   sing N N 395 
TYR CB  HB2  sing N N 396 
TYR CB  HB3  sing N N 397 
TYR CG  CD1  doub Y N 398 
TYR CG  CD2  sing Y N 399 
TYR CD1 CE1  sing Y N 400 
TYR CD1 HD1  sing N N 401 
TYR CD2 CE2  doub Y N 402 
TYR CD2 HD2  sing N N 403 
TYR CE1 CZ   doub Y N 404 
TYR CE1 HE1  sing N N 405 
TYR CE2 CZ   sing Y N 406 
TYR CE2 HE2  sing N N 407 
TYR CZ  OH   sing N N 408 
TYR OH  HH   sing N N 409 
TYR OXT HXT  sing N N 410 
VAL N   CA   sing N N 411 
VAL N   H    sing N N 412 
VAL N   H2   sing N N 413 
VAL CA  C    sing N N 414 
VAL CA  CB   sing N N 415 
VAL CA  HA   sing N N 416 
VAL C   O    doub N N 417 
VAL C   OXT  sing N N 418 
VAL CB  CG1  sing N N 419 
VAL CB  CG2  sing N N 420 
VAL CB  HB   sing N N 421 
VAL CG1 HG11 sing N N 422 
VAL CG1 HG12 sing N N 423 
VAL CG1 HG13 sing N N 424 
VAL CG2 HG21 sing N N 425 
VAL CG2 HG22 sing N N 426 
VAL CG2 HG23 sing N N 427 
VAL OXT HXT  sing N N 428 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HGK 
_atom_sites.fract_transf_matrix[1][1]   0.024048 
_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]   0.023794 
_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]   0.006319 
_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   . MET A 1 2  ? 0.665   4.203   2.612   1.00 48.53  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.387  3.484   1.849   1.00 55.41  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.233   2.438   0.915   1.00 49.33  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.347   2.608   0.418   1.00 48.02  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.299  4.447   1.076   1.00 58.09  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.373  5.143   1.908   1.00 69.92  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.452  4.182   2.999   1.00 65.95  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -2.455  4.343   4.490   1.00 74.44  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.463  1.289   0.724   1.00 40.56  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.034  0.208   -0.174  1.00 38.94  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.167   0.622   -1.637  1.00 38.15  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.598  1.425   -2.170  1.00 39.39  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.276  -0.753  -0.050  1.00 39.29  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.770  -0.554  1.374   1.00 41.11  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.699  0.952   1.459   1.00 41.69  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.168   0.018   -2.289  1.00 36.07  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.329   0.127   -3.721  1.00 38.28  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.745   -1.149  -4.312  1.00 36.60  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.244   -1.999  -3.565  1.00 34.45  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.822   0.239   -4.086  1.00 42.20  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.512   1.474   -3.585  1.00 54.53  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.450   1.936   -2.286  1.00 62.00  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.302   2.340   -4.242  1.00 58.48  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.161   3.052   -2.175  1.00 62.28  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.693   3.312   -3.351  1.00 59.08  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.800   -1.274  -5.639  1.00 29.60  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.530   -2.544  -6.287  1.00 28.88  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.641   -3.510  -5.894  1.00 28.11  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.723   -3.089  -5.467  1.00 28.12  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.499   -2.341  -7.796  1.00 32.39  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.384   -4.802  -6.080  1.00 28.59  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.406   -5.813  -5.851  1.00 26.96  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.558   -5.638  -6.846  1.00 28.25  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.354   -5.292  -8.024  1.00 27.18  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.840   -7.229  -6.000  1.00 26.25  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.060   -7.633  -4.749  1.00 27.57  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.738   -7.884  -3.558  1.00 26.86  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.333  -7.820  -4.765  1.00 24.93  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.077   -8.212  -2.367  1.00 23.42  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.970  -8.254  -3.593  1.00 24.42  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.301  -8.398  -2.401  1.00 24.48  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.776   -5.924  -6.356  1.00 24.46  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.920   -5.860  -7.232  1.00 26.34  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.826   -7.058  -6.949  1.00 25.14  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.816   -7.654  -5.867  1.00 23.60  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.656   -4.535  -6.982  1.00 30.44  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.323   -4.481  -5.621  1.00 30.94  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.894   -3.091  -5.320  1.00 38.44  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.514   -2.935  -3.955  1.00 39.00  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.575   -3.232  -2.878  1.00 38.40  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.699   -7.426  -7.905  1.00 26.14  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.643   -8.518  -7.668  1.00 25.06  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.458   -8.250  -6.394  1.00 24.18  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.908   -7.133  -6.134  1.00 26.48  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.517   -8.537  -8.967  1.00 26.75  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.571   -7.936  -10.002 1.00 30.87  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.791   -6.851  -9.266  1.00 29.59  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.655   -9.315  -5.609  1.00 22.02  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.351  -9.237  -4.339  1.00 20.81  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.405   -9.129  -3.141  1.00 23.31  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.780   -9.406  -1.983  1.00 23.11  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.152   -8.714  -3.380  1.00 20.80  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.238   -8.680  -2.246  1.00 21.25  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.015   -10.077 -1.646  1.00 20.44  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.867   -11.051 -2.363  1.00 22.29  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.884   -8.108  -2.662  1.00 21.81  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.871   -6.598  -2.838  1.00 26.39  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.861   -5.927  -2.429  1.00 27.31  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.896   -6.088  -3.421  1.00 25.68  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.901   -10.138 -0.304  1.00 20.59  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.707   -11.401 0.420   1.00 19.53  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.234   -11.506 0.821   1.00 19.03  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.640   -10.520 1.302   1.00 22.73  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.642   -11.480 1.631   1.00 20.72  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.125   -11.252 1.289   1.00 20.18  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.919   -11.399 2.584   1.00 24.16  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.558   -12.243 0.201   1.00 21.95  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.671   -12.715 0.682   1.00 18.83  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.233   -12.881 0.910   1.00 20.91  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.988   -14.247 1.532   1.00 22.17  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.856   -15.124 1.543   1.00 21.40  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.450   -12.800 -0.423  1.00 20.31  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.584   -11.426 -1.053  1.00 23.04  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.851   -13.921 -1.410  1.00 21.72  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.750   -14.459 2.020   1.00 22.36  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.194   -15.811 2.032   1.00 23.24  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.229   -15.890 0.859   1.00 26.01  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.578  -14.975 0.675   1.00 23.27  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.396   -16.167 3.308   1.00 22.74  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.345   -16.256 4.499   1.00 23.13  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.670   -15.110 5.223   1.00 25.45  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.882   -17.487 4.868   1.00 26.60  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.575   -15.197 6.274   1.00 29.26  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.799   -17.565 5.920   1.00 30.62  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.139   -16.420 6.607   1.00 29.86  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.330   -16.975 0.064   1.00 23.25  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.440  -17.101 -1.177  1.00 23.72  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.425  -18.252 -0.950  1.00 27.15  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.072  -19.283 -0.380  1.00 27.16  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.443   -17.361 -2.391  1.00 22.03  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.674  -18.054 -1.371  1.00 25.19  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.684  -19.054 -1.073  1.00 24.92  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.067  -19.752 -2.377  1.00 27.97  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.399  -19.116 -3.378  1.00 29.52  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.916  -18.422 -0.407  1.00 27.61  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.976  -19.514 -0.062  1.00 34.15  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.551  -20.469 1.068   1.00 34.22  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.706  -21.214 1.707   1.00 39.84  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.194  -22.210 0.745   1.00 37.52  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.001  -21.084 -2.325  1.00 28.15  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.685  -21.852 -3.336  1.00 34.11  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.676  -22.832 -2.736  1.00 37.53  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.470  -23.316 -1.629  1.00 31.47  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.695  -22.656 -4.139  1.00 36.92  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.675  -22.036 -5.503  1.00 50.16  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.976  -21.830 -6.019  1.00 39.91  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.376  -23.481 -6.337  1.00 38.88  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.703  -23.114 -3.551  1.00 41.66  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.712  -24.127 -3.283  1.00 42.67  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.063  -25.330 -2.620  1.00 37.54  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.114  -25.914 -3.153  1.00 38.72  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.335  -24.526 -4.629  1.00 49.09  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.695  -25.223 -4.529  1.00 59.87  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.780 -24.336 -3.919  1.00 65.20  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.552  -25.676 -1.417  1.00 38.49  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.182  -26.952 -0.833  1.00 39.50  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.812  -26.945 -0.170  1.00 45.39  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.391  -27.970 0.342   1.00 43.93  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.103  -25.805 -0.190  1.00 35.75  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.857  -25.731 0.548   1.00 33.90  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.937  -24.618 1.570   1.00 33.48  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.658  -23.648 1.362   1.00 32.50  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.690  -25.369 -0.375  1.00 36.19  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.410  -26.330 -1.519  1.00 42.10  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.405  -27.290 -1.443  1.00 53.46  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.107  -26.210 -2.713  1.00 45.67  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.132  -28.125 -2.521  1.00 56.94  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.844  -27.031 -3.796  1.00 50.37  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.851  -27.988 -3.701  1.00 58.42  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -1.651  -28.783 -4.799  1.00 71.67  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.177  -24.700 2.685   1.00 32.89  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.134  -23.606 3.662   1.00 34.75  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.451  -22.383 3.022   1.00 30.42  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.744  -22.542 2.034   1.00 29.70  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.304  -24.192 4.810   1.00 34.45  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.415  -25.230 4.144   1.00 37.30  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.272  -25.819 3.026   1.00 36.32  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.748  -21.191 3.538   1.00 28.71  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -2.022  -19.977 3.168   1.00 26.57  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.522  -20.291 3.230   1.00 28.00  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.046  -20.764 4.261   1.00 28.92  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.489  -18.807 4.035   1.00 25.21  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.925  -18.412 3.801   1.00 28.57  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.985  -19.072 4.423   1.00 31.59  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.465  -17.392 3.113   1.00 28.51  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.134  -18.477 4.091   1.00 30.65  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.857  -17.474 3.265   1.00 30.47  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.214   -19.995 2.133   1.00 26.51  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.525   -20.627 1.964   1.00 24.44  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.590   -19.545 1.802   1.00 25.92  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.375   -18.604 1.044   1.00 25.41  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.538   -21.536 0.723   1.00 26.00  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.644   -22.565 0.756   1.00 25.23  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 3.984   -22.388 0.535   1.00 27.91  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.476   -23.968 1.071   1.00 30.30  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.655   -23.584 0.647   1.00 28.03  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.760   -24.566 0.997   1.00 31.12  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.378   -24.774 1.404   1.00 34.29  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.973   -25.924 1.241   1.00 32.22  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.593   -26.127 1.627   1.00 34.11  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.873   -26.690 1.577   1.00 31.69  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.729   -19.610 2.535   1.00 23.20  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.771   -18.564 2.389   1.00 21.18  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.286   -18.526 0.952   1.00 21.25  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.578   -19.582 0.346   1.00 24.04  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.859   -19.025 3.397   1.00 21.97  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.627   -20.534 3.578   1.00 22.37  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.077   -20.636 3.527   1.00 23.67  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.375   -17.317 0.380   1.00 19.62  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.699   -17.197 -1.038  1.00 18.71  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.240   -15.797 -1.343  1.00 19.61  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.242   -14.910 -0.470  1.00 20.26  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.430   -17.533 -1.880  1.00 22.28  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.749   -15.621 -2.569  1.00 19.50  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.179   -14.306 -2.999  1.00 18.95  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.646   -14.043 -4.395  1.00 19.88  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.361   -14.992 -5.141  1.00 21.70  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.705   -14.122 -2.903  1.00 20.39  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.414   -15.020 -3.904  1.00 21.43  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.954  -14.848 -3.788  1.00 21.50  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.630  -15.634 -4.844  1.00 23.95  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.878  -16.099 -4.744  1.00 24.53  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.588  -15.929 -3.635  1.00 23.06  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.379  -16.727 -5.799  1.00 24.92  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.496   -12.764 -4.708  1.00 18.66  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.301   -12.370 -6.112  1.00 19.84  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.640   -12.474 -6.827  1.00 23.79  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.593   -11.801 -6.448  1.00 24.01  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.820   -10.915 -6.255  1.00 24.20  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.643   -10.547 -5.297  1.00 32.01  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.453   -10.642 -7.732  1.00 23.40  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.333   -11.226 -5.605  1.00 31.29  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.682   -13.279 -7.882  1.00 24.30  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.930   -13.425 -8.615  1.00 28.36  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.024   -12.405 -9.746  1.00 29.88  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.036   -11.797 -10.168 1.00 27.61  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.085   -14.778 -9.277  1.00 28.09  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.993   -15.774 -8.582  1.00 28.76  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.561  -15.451 -7.526  1.00 30.38  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.069  -16.894 -9.064  1.00 30.13  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.272  -12.207 -10.203 1.00 31.94  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.524  -11.503 -11.444 1.00 34.55  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.255  -12.477 -12.593 1.00 31.26  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.117  -13.677 -12.393 1.00 33.64  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 11.972  -11.035 -11.539 1.00 41.58  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.327  -9.728  -10.840 1.00 49.33  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 11.952  -8.647  -11.363 1.00 53.52  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.009  -9.801  -9.798  1.00 55.52  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.116  -11.931 -13.788 1.00 40.74  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.067  -12.784 -14.967 1.00 38.94  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.376  -12.494 -15.694 1.00 35.38  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.612  -11.343 -16.003 1.00 35.78  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.877   -12.353 -15.834 1.00 41.27  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.534   -12.381 -15.067 1.00 38.78  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.821   -13.188 -17.119 1.00 35.11  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.621   -11.212 -15.405 1.00 39.21  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.200  -13.524 -15.871 1.00 38.91  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.487  -13.407 -16.542 1.00 37.06  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.205  -13.203 -18.035 1.00 36.13  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.137  -13.565 -18.553 1.00 32.12  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.282  -14.671 -16.319 1.00 35.81  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.136  -12.514 -18.696 1.00 34.65  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.115  -12.489 -20.149 1.00 31.06  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 13.970  -13.924 -20.633 1.00 26.98  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.667  -14.803 -20.154 1.00 30.65  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.430  -11.878 -20.633 1.00 34.62  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.536  -10.362 -20.526 1.00 36.93  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.484  -9.694  -20.467 1.00 39.58  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.678  -9.842  -20.600 1.00 38.96  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.100  -14.137 -21.635 1.00 30.13  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.990  -15.445 -22.250 1.00 29.11  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 11.944  -16.320 -21.573 1.00 33.37  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.564  -17.341 -22.116 1.00 33.00  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.565  -15.959 -20.342 1.00 34.10  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.678  -16.813 -19.553 1.00 34.24  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.210   -16.610 -19.920 1.00 29.03  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.781   -15.542 -20.369 1.00 31.13  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 10.919  -16.556 -18.057 1.00 35.79  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.403   -17.645 -19.619 1.00 35.67  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.953   -17.619 -19.790 1.00 34.64  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.344   -16.558 -18.881 1.00 34.95  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.583   -16.570 -17.672 1.00 38.05  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.401   -19.025 -19.470 1.00 37.48  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.879   -19.065 -19.577 1.00 42.10  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.025   -20.068 -20.397 1.00 39.84  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.592   -15.633 -19.483 1.00 34.07  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.896   -14.544 -18.803 1.00 34.41  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.588   -15.063 -18.197 1.00 38.57  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 2.982   -15.998 -18.716 1.00 36.55  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.556   -13.366 -19.725 1.00 39.84  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.767   -12.604 -20.285 1.00 33.34  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.393   -11.463 -21.224 1.00 46.49  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.243   -11.878 -22.654 1.00 44.25  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.978   -10.701 -23.485 1.00 44.37  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.104   -14.457 -17.085 1.00 39.38  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.793   -14.824 -16.535 1.00 35.44  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.644   -14.332 -17.410 1.00 34.72  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.783   -13.372 -18.167 1.00 38.00  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.697   -14.125 -15.156 1.00 35.75  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.026   -13.379 -14.972 1.00 36.01  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.758   -13.373 -16.338 1.00 38.13  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.582  -14.871 -17.225 1.00 38.93  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.776  -14.274 -17.832 1.00 38.08  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.966  -12.841 -17.360 1.00 42.96  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.449  -12.462 -16.308 1.00 33.60  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.922  -15.154 -17.318 1.00 40.26  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.270  -16.459 -16.955 1.00 36.48  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.861  -16.110 -16.481 1.00 39.79  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.744  -12.001 -18.078 1.00 39.94  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -3.089  -10.666 -17.576 1.00 40.47  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.702  -10.674 -16.173 1.00 35.92  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.423  -11.603 -15.817 1.00 39.40  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -4.068  -10.094 -18.635 1.00 44.22  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.456  -11.297 -19.466 1.00 37.69  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.295  -12.273 -19.425 1.00 45.64  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.337  -9.659  -15.383 1.00 39.83  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.777  -9.449  -14.013 1.00 44.38  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.283  -10.541 -13.064 1.00 37.87  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.739  -10.542 -11.914 1.00 37.65  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.278  -9.207  -13.916 1.00 47.61  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.675  -8.031  -14.772 1.00 48.03  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.476  -6.873  -14.383 1.00 46.72  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.204  -8.316  -15.947 1.00 53.31  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.358  -11.414 -13.524 1.00 33.67  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.780  -12.481 -12.698 1.00 29.19  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.279  -12.227 -12.467 1.00 25.13  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.351   -11.446 -13.193 1.00 30.71  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.955  -13.938 -13.138 1.00 30.95  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.380  -14.475 -13.426 1.00 36.37  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.380  -13.964 -12.404 1.00 38.65  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.826  -14.259 -12.751 1.00 46.65  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.094  -15.694 -12.603 1.00 47.76  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.194   -12.686 -11.304 1.00 21.73  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.586   -12.490 -10.891 1.00 23.29  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.255   -13.844 -10.849 1.00 23.42  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.626   -14.853 -10.525 1.00 24.74  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.620   -11.930 -9.439  1.00 22.88  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.153   -10.491 -9.425  1.00 24.47  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.211  -10.198 -9.337  1.00 26.93  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.029   -9.430  -9.621  1.00 27.60  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.673  -8.891  -9.409  1.00 30.71  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.582   -8.110  -9.644  1.00 29.09  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.223   -7.852  -9.551  1.00 33.24  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.249  -6.582  -9.636  1.00 34.65  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.581   -13.960 -11.099 1.00 22.42  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.239   -15.247 -10.899 1.00 21.87  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.584   -15.440 -9.421  1.00 22.74  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.280   -14.595 -8.862  1.00 26.41  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.508   -15.111 -11.749 1.00 25.20  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.758   -13.654 -11.820 1.00 25.72  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.471   -12.884 -11.575 1.00 26.47  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.013   -16.472 -8.801  1.00 23.44  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.214   -16.666 -7.365  1.00 21.78  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.161   -17.842 -7.155  1.00 24.65  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.874   -18.989 -7.564  1.00 26.52  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.870   -16.930 -6.665  1.00 22.00  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.838   -15.789 -6.964  1.00 20.76  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.117   -17.087 -5.156  1.00 20.20  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.377   -14.398 -6.621  1.00 21.93  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.258   -17.576 -6.428  1.00 21.62  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.175   -18.651 -6.076  1.00 22.70  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.882   -19.089 -4.648  1.00 22.29  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.918   -18.286 -3.716  1.00 23.42  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.616   -18.122 -6.203  1.00 21.26  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.663   -19.137 -5.753  1.00 25.63  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.047  -20.178 -6.597  1.00 28.39  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.201  -19.099 -4.460  1.00 27.53  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.016  -21.099 -6.203  1.00 29.93  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.145  -20.051 -4.063  1.00 31.67  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.569  -21.029 -4.937  1.00 29.65  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.549   -20.372 -4.480  1.00 22.51  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.150   -20.880 -3.167  1.00 22.37  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.415   -21.373 -2.480  1.00 24.77  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.136   -22.229 -3.045  1.00 25.98  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.194   -22.073 -3.398  1.00 24.61  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.801   -21.596 -3.807  1.00 25.62  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.459   -21.414 -5.149  1.00 27.75  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.858   -21.286 -2.835  1.00 28.85  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.187   -20.934 -5.493  1.00 29.76  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.592   -20.823 -3.177  1.00 27.91  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.280   -20.626 -4.508  1.00 28.04  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.667   -20.850 -1.267  1.00 22.61  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.838   -21.318 -0.522  1.00 24.97  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.615   -22.761 -0.070  1.00 26.06  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.477   -23.237 0.069   1.00 27.32  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.161   -20.437 0.703   1.00 25.81  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.602   -19.037 0.322   1.00 25.22  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.835  -18.823 -0.262  1.00 22.60  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.837   -17.905 0.615   1.00 23.15  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.231  -17.534 -0.624  1.00 22.37  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.239   -16.615 0.236   1.00 24.67  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.464  -16.416 -0.369  1.00 24.01  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.723   -23.465 0.134   1.00 25.91  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.669   -24.844 0.587   1.00 28.55  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.466   -25.835 -0.566  1.00 36.40  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.345  -26.659 -0.835  1.00 31.76  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.315   -25.755 -1.261  1.00 34.04  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.059   -26.619 -2.416  1.00 34.44  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.884   -26.182 -3.622  1.00 34.29  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.208   -27.000 -4.502  1.00 31.44  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.563   -26.677 -2.745  1.00 34.41  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.220   -25.386 -3.259  1.00 32.94  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.698   -27.029 -1.557  1.00 34.40  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.167   -24.863 -3.704  1.00 27.96  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.846   -24.228 -4.826  1.00 29.13  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.063   -24.347 -6.135  1.00 28.41  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.671   -24.312 -7.202  1.00 32.04  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.322  -24.692 -4.948  1.00 29.11  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.026  -24.740 -3.638  1.00 34.31  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.823  -25.801 -3.268  1.00 32.53  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.075  -23.855 -2.613  1.00 31.44  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.333  -25.566 -2.063  1.00 38.87  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.917  -24.375 -1.656  1.00 33.18  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.725   -24.443 -6.065  1.00 30.76  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.861   -24.491 -7.238  1.00 34.54  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.348   -23.089 -7.541  1.00 28.93  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.405   -22.215 -6.664  1.00 29.13  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.676   -25.409 -6.934  1.00 38.50  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.142   -26.855 -6.775  1.00 44.05  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.137   -27.793 -6.148  1.00 53.82  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.941   -27.440 -6.007  1.00 54.24  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.603   -28.883 -5.750  1.00 56.74  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.960   -22.867 -8.804  1.00 25.77  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.479   -21.565 -9.249  1.00 27.88  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.024   -21.719 -9.681  1.00 30.57  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.681   -22.724 -10.311 1.00 34.12  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.301   -20.967 -10.393 1.00 30.66  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.599   -20.616 -9.917  1.00 31.99  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.637   -19.751 -11.025 1.00 32.29  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.176   -20.754 -9.306  1.00 27.40  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.852   -20.670 -9.918  1.00 27.08  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.500   -19.217 -10.198 1.00 27.87  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.152   -18.296 -9.705  1.00 29.11  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.802   -21.340 -9.060  1.00 26.99  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.444   -19.008 -10.989 1.00 24.65  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.078   -17.655 -11.351 1.00 26.48  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.178  -17.295 -10.586 1.00 29.79  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.184  -18.005 -10.732 1.00 31.52  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.164  -17.628 -12.864 1.00 29.73  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.079   -17.926 -13.687 1.00 32.09  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.196   -17.099 -13.620 1.00 33.65  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.078   -18.980 -14.601 1.00 41.83  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.322   -17.373 -14.408 1.00 46.48  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.195   -19.243 -15.383 1.00 37.94  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.318   -18.461 -15.277 1.00 36.23  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.118  -16.185 -9.821  1.00 25.33  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.245  -15.836 -8.957  1.00 24.35  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.543  -14.353 -9.041  1.00 24.86  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.670  -13.530 -9.328  1.00 23.86  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.931  -16.194 -7.498  1.00 27.05  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.852  -17.678 -7.177  1.00 25.88  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.485  -17.752 -5.699  1.00 28.05  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.251  -18.281 -7.388  1.00 34.40  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.820  -13.999 -8.798  1.00 22.19  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.121  -12.577 -8.697  1.00 24.20  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.172  -12.124 -7.226  1.00 22.33  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.116  -12.936 -6.304  1.00 22.22  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.239  -10.803 -6.998  1.00 22.72  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.177  -10.206 -5.660  1.00 22.23  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.169  -10.756 -4.646  1.00 22.89  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.867  -10.741 -3.468  1.00 22.89  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.393  -8.717  -5.932  1.00 24.52  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.847  -8.550  -7.350  1.00 23.83  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.310  -9.793  -8.071  1.00 24.62  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.332  -11.256 -5.132  1.00 23.16  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.306  -11.755 -4.155  1.00 24.49  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.737  -12.910 -3.316  1.00 23.96  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.197  -13.173 -2.219  1.00 24.60  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.586  -12.259 -4.850  1.00 27.41  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.391  -13.572 -5.620  1.00 29.83  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.694  -13.982 -6.323  1.00 40.96  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.673  -15.336 -6.980  1.00 38.01  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.617  -16.438 -6.012  1.00 45.09  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.704  -13.596 -3.826  1.00 23.52  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.142  -14.734 -3.161  1.00 22.62  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.778  -14.397 -2.524  1.00 22.99  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.106  -15.330 -2.106  1.00 23.88  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.040  -15.898 -4.151  1.00 24.46  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.424  -16.478 -4.456  1.00 27.72  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.236  -16.514 -3.509  1.00 29.56  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.681  -16.856 -5.614  1.00 30.40  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.399  -13.109 -2.458  1.00 21.29  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.050  -12.715 -1.994  1.00 19.40  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.191  -11.870 -0.718  1.00 18.31  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.808  -10.798 -0.733  1.00 21.80  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.354  -11.915 -3.101  1.00 18.45  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.194  -12.658 -4.424  1.00 20.62  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.484  -11.793 -5.470  1.00 22.23  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.438  -13.946 -4.233  1.00 21.11  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.665  -12.364 0.399   1.00 20.98  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.755  -11.654 1.691   1.00 21.60  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.367  -11.160 2.094   1.00 22.39  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.558   -11.983 2.265   1.00 25.00  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.198  -12.682 2.719   1.00 24.32  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.634  -13.115 2.433   1.00 23.63  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.931  -14.027 1.406   1.00 23.67  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.665  -12.576 3.191   1.00 26.33  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.264  -14.398 1.147   1.00 27.79  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.972  -12.973 2.931   1.00 25.30  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.271  -13.866 1.936   1.00 24.16  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.143  -9.840  2.191   1.00 24.18  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.209   -9.362  2.547   1.00 23.08  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.734   -9.995  3.834   1.00 24.25  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.031   -10.146 4.819   1.00 24.69  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.025   -7.823  2.586   1.00 25.82  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.093  -7.546  1.542   1.00 27.83  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.047  -8.737  1.794   1.00 26.91  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.026   -10.408 3.811   1.00 24.49  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.628   -11.264 4.829   1.00 23.64  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.657   -10.599 6.208   1.00 24.95  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.230   -11.239 7.167   1.00 29.18  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.044   -11.652 4.340   1.00 24.46  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.825   -12.463 5.383   1.00 22.94  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.507   -13.789 5.657   1.00 24.66  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.875   -11.876 6.080   1.00 28.23  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.213   -14.531 6.605   1.00 26.75  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.589   -12.604 7.024   1.00 30.13  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.249   -13.913 7.288   1.00 28.77  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.982   -14.598 8.226   1.00 31.57  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.078   -9.321  6.260   1.00 23.54  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.216   -8.619  7.542   1.00 30.54  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.875   -8.601  8.283   1.00 30.31  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.807   -9.006  9.455   1.00 34.17  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.830   -7.242  7.356   1.00 30.62  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 1.816   -8.152  7.580   1.00 32.71  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.472   -8.095  8.145   1.00 32.12  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? -0.034  -9.474  8.576   1.00 31.90  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.781  -9.560  9.572   1.00 32.00  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.496  -7.381  7.184   1.00 31.04  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.967  -7.256  7.673   1.00 35.61  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.790  -6.527  6.617   1.00 35.31  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.989  -5.811  7.172   1.00 41.47  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.943  -6.672  7.862   1.00 44.64  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.320   -10.561 7.853   1.00 28.54  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.382  -11.837 7.983   1.00 27.88  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.394   -12.915 8.738   1.00 29.06  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? -0.138  -14.004 8.926   1.00 29.43  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.753  -12.414 6.626   1.00 30.46  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.587  -11.469 5.998   1.00 39.52  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.643   -12.653 9.128   1.00 27.34  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.469   -13.768 9.595   1.00 31.50  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.041   -14.291 10.976  1.00 30.57  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.200   -15.483 11.263  1.00 31.97  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 3.959   -13.423 9.541   1.00 33.09  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.388   -12.237 10.370  1.00 37.53  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 5.910   -12.264 10.347  1.00 47.09  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.530   -11.296 11.308  1.00 54.00  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.122   -9.923  10.988  1.00 63.13  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.439   -13.426 11.799  0.50 32.18  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.465   -13.410 11.801  0.50 31.51  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 0.955   -13.876 13.101  0.50 36.58  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 0.922   -13.844 13.082  0.50 35.56  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? -0.178  -14.894 12.925  0.50 36.33  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? -0.088  -14.965 12.842  0.50 35.32  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.328  -15.811 13.729  0.50 38.05  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? -0.059  -16.000 13.509  0.50 36.20  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.671   -12.702 14.028  0.50 38.46  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.261   -12.692 13.819  0.50 35.97  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 1.897   -11.993 14.592  0.50 42.95  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? -0.094  -12.977 15.269  0.50 40.17  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.014   -12.543 14.464  0.50 48.57  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.822   -12.910 16.118  0.50 44.47  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.733   -10.890 15.154  0.50 48.57  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.276  -13.283 15.529  0.50 44.63  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.965  -14.766 11.847  1.00 31.61  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -2.065  -15.689 11.625  1.00 31.77  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.608  -16.957 10.910  1.00 34.17  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -2.089  -18.049 11.195  1.00 31.90  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -3.133  -14.947 10.822  1.00 33.42  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.417  -15.688 10.709  1.00 38.96  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.431  -14.752 10.043  1.00 41.75  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.734  -15.446 9.775   1.00 51.89  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.669  -14.496 9.162   1.00 46.22  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.750  -16.808 9.897   1.00 29.87  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.551  -17.891 8.948   1.00 30.78  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 0.838   -18.514 9.102   1.00 28.81  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.075   -19.592 8.558   1.00 30.85  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.685  -17.338 7.515   1.00 27.52  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -2.088  -16.923 7.120   1.00 29.95  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.200  -17.702 7.451   1.00 30.62  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.292  -15.739 6.406   1.00 28.83  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.482  -17.298 7.090   1.00 33.15  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.564  -15.338 6.028   1.00 31.58  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.653  -16.120 6.375   1.00 30.43  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.875  -15.669 5.981   1.00 32.33  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.710   -17.870 9.885   1.00 29.49  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.114   -18.264 9.951   1.00 29.76  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.346   -19.266 11.093  1.00 31.34  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.051   -18.981 12.037  1.00 39.37  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.664   -20.402 11.023  1.00 36.37  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.780   -21.415 12.061  1.00 38.47  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.031   -22.754 11.379  1.00 36.51  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.622   -22.978 10.238  1.00 35.02  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.509   -21.413 12.925  1.00 40.14  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.320   -20.168 13.780  1.00 42.93  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? -0.063  -20.063 14.416  1.00 54.63  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.721   -23.716 12.035  1.00 35.49  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 3.970   -25.003 11.389  1.00 32.29  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.729   -25.722 10.893  1.00 36.27  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.655   -25.580 11.473  1.00 39.41  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 4.702   -25.791 12.497  1.00 40.32  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.394   -24.695 13.285  1.00 39.90  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.324   -23.593 13.371  1.00 38.39  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 2.923   -26.474 9.812   1.00 35.22  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 1.902   -27.211 9.103   1.00 40.39  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.517   -28.542 8.708   1.00 45.27  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.713   -28.620 8.441   1.00 45.11  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.492   -26.471 7.831   1.00 41.31  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? 0.095   -26.830 7.392   1.00 47.26  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? -0.083  -27.696 6.534   1.00 46.50  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -0.906  -26.201 7.986   1.00 52.31  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.670   -29.569 8.630   1.00 50.89  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 2.084   -30.920 8.309   1.00 49.72  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.453   -31.027 6.833   1.00 47.58  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.190   -31.932 6.443   1.00 44.65  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 0.935   -31.873 8.681   1.00 52.66  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.292  -31.833 7.760   1.00 53.30  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 1.952   -30.098 6.000   1.00 42.75  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 2.048   -30.278 4.558   1.00 42.31  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.507   -30.271 4.098   1.00 41.35  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.323   -29.522 4.641   1.00 39.06  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 1.129   -29.307 3.801   1.00 44.92  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.338  -29.537 4.129   1.00 47.24  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -0.992  -30.592 3.254   1.00 43.76  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.913  -30.000 2.279   1.00 63.88  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -3.093  -29.435 2.589   1.00 59.67  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.864  -28.977 1.623   1.00 62.45  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.520  -29.353 3.846   1.00 60.68  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.799   -31.094 3.077   1.00 39.01  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 5.145   -31.265 2.544   1.00 40.06  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.705   -29.903 2.144   1.00 37.68  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 5.125   -29.217 1.304   1.00 35.73  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 5.132   -32.146 1.287   1.00 40.97  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.477   -32.461 0.661   1.00 42.39  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.487   -33.621 -0.328  1.00 52.79  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.885   -34.014 -0.725  1.00 54.51  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.833   -29.533 2.753   1.00 39.13  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.564   -28.369 2.295   1.00 35.14  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.166   -27.106 3.049   1.00 32.96  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 7.870   -26.108 2.968   1.00 30.06  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.074   -27.157 3.804   1.00 30.06  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.595   -25.960 4.479   1.00 32.29  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.621   -25.374 5.453   1.00 33.99  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 6.839   -24.162 5.490   1.00 30.80  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.240   -26.248 5.127   1.00 30.46  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.506   -24.970 5.491   1.00 30.32  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.757   -24.323 6.695   1.00 29.11  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.539   -24.439 4.625   1.00 30.76  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.124   -23.125 7.020   1.00 33.10  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 1.870   -23.270 4.965   1.00 24.73  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.162   -22.618 6.160   1.00 28.69  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.181   -26.210 6.339   1.00 28.61  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 8.010   -25.690 7.416   1.00 29.74  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.359   -25.240 6.854   1.00 28.04  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 9.947   -24.264 7.349   1.00 27.33  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.190   -26.750 8.507   1.00 29.56  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 6.851   -27.037 9.150   1.00 37.80  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 5.938   -26.197 9.109   1.00 31.73  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.716   -28.198 9.777   1.00 35.44  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 9.843   -25.950 5.824   1.00 27.59  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 11.005  -25.452 5.098   1.00 29.64  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.674  -24.073 4.534   1.00 27.19  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.481  -23.142 4.599   1.00 25.79  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.452  -26.369 3.962   1.00 29.83  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.675  -25.852 3.202   1.00 30.80  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.186  -26.843 2.148   1.00 39.71  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.469  -27.790 1.771   1.00 44.08  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.325  -26.687 1.694   1.00 41.73  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.459   -23.936 4.008   1.00 26.18  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 9.091   -22.634 3.443   1.00 25.82  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 9.048   -21.524 4.500   1.00 24.58  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.347   -20.358 4.200   1.00 22.99  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.623   -21.834 5.735   1.00 24.25  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.613   -20.818 6.778   1.00 25.31  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 10.036  -20.329 7.074   1.00 24.71  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.276  -19.141 7.324   1.00 24.15  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 7.992   -21.396 8.045   1.00 24.69  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.484   -21.675 7.982   1.00 28.33  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.077   -22.203 9.337   1.00 29.30  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.648   -20.422 7.692   1.00 27.45  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 10.995  -21.270 7.029   1.00 25.00  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.378  -20.899 7.282   1.00 26.55  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 12.854  -19.956 6.178   1.00 25.44  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.483  -18.935 6.429   1.00 24.77  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.286  -22.145 7.392   1.00 24.23  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.735  -21.780 7.655   1.00 25.84  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.347  -21.628 8.873   1.00 28.86  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.720  -21.430 6.657   1.00 24.81  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.659  -21.278 8.700   1.00 27.99  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 16.899  -21.098 7.351   1.00 26.46  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.685  -21.377 5.251   1.00 25.58  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.059  -20.711 6.680   1.00 24.74  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 16.816  -20.951 4.583   1.00 26.49  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 17.982  -20.627 5.302   1.00 27.30  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.532  -20.306 4.935   1.00 24.45  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 13.066  -19.547 3.810   1.00 22.54  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.536  -18.115 3.829   1.00 24.20  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.275  -17.168 3.613   1.00 23.06  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.702  -20.194 2.481   1.00 24.05  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.347  -21.572 2.342   1.00 23.94  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 12.972  -22.308 1.039   1.00 28.57  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 12.045  -21.863 0.321   1.00 29.40  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.556  -23.393 0.741   1.00 29.28  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.234  -17.963 4.044   1.00 21.46  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.633  -16.633 3.984   1.00 21.60  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.208  -15.733 5.082   1.00 24.66  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.354  -14.511 4.880   1.00 22.27  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.078   -16.683 3.980   1.00 21.49  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.505   -15.307 3.495   1.00 22.80  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.522   -17.062 5.376   1.00 20.92  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.031   -15.355 3.045   1.00 21.95  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.487  -16.320 6.266   1.00 23.60  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 12.012  -15.537 7.387   1.00 24.24  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.507  -15.256 7.238   1.00 24.48  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 13.933  -14.175 7.647   1.00 28.14  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.639  -16.275 8.682   1.00 26.78  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.165  -15.626 9.965   1.00 37.13  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.435  -16.120 11.206  1.00 43.21  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.034  -17.292 11.303  1.00 42.24  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.214  -15.214 12.152  1.00 42.85  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.280  -16.229 6.703   1.00 23.29  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 15.739  -16.242 6.806   1.00 22.11  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.464  -15.931 5.499   1.00 24.46  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.576  -15.377 5.538   1.00 25.29  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.244  -17.546 7.421   1.00 24.07  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 15.714  -17.630 8.838   1.00 29.46  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 16.058  -16.770 9.665   1.00 30.93  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 14.785  -18.542 9.108   1.00 26.03  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 15.912  -16.296 4.325   1.00 22.56  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.569  -15.884 3.088   1.00 21.64  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.540  -15.790 1.947   1.00 20.85  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.575  -16.540 0.968   1.00 23.73  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 17.736  -16.829 2.752   1.00 25.16  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 18.813  -16.194 1.892   1.00 26.82  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.564  -15.208 1.199   1.00 26.27  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 20.014  -16.778 1.846   1.00 28.59  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.597  -14.820 2.021   1.00 21.54  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.456  -14.837 1.124   1.00 22.92  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 13.822  -14.387 -0.279  1.00 26.73  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 13.041  -14.628 -1.166  1.00 23.76  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.478  -13.886 1.827   1.00 21.37  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.416  -12.873 2.527   1.00 20.08  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.501  -13.801 3.067   1.00 22.10  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 15.020  -13.784 -0.465  1.00 20.57  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.352  -13.259 -1.804  1.00 21.21  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.487  -14.051 -2.484  1.00 20.71  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 16.994  -13.640 -3.559  1.00 23.39  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.728  -11.771 -1.658  1.00 20.76  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.661  -10.912 -1.095  1.00 21.03  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.384  -10.858 -1.666  1.00 21.00  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.608  -10.190 0.040   1.00 22.53  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.632  -10.049 -0.946  1.00 22.16  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.339  -9.617  0.097   1.00 23.10  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.770  -15.258 -1.942  1.00 22.63  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.822  -16.119 -2.491  1.00 23.03  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.361  -16.818 -3.769  1.00 26.10  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.182  -16.965 -4.040  1.00 23.53  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.295  -17.177 -1.507  1.00 24.61  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.356  -17.331 -4.512  1.00 26.00  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 18.092  -18.229 -5.623  1.00 29.39  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.837  -19.639 -5.093  1.00 31.55  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.671  -20.212 -4.385  1.00 35.95  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.284  -18.202 -6.550  1.00 33.95  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 19.193  -19.314 -7.416  1.00 39.31  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.669  -20.198 -5.408  1.00 28.80  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.346  -21.537 -4.964  1.00 28.56  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.252  -22.469 -6.174  1.00 35.69  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.725  -23.576 -6.057  1.00 40.58  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 14.998  -21.521 -4.229  1.00 31.55  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 15.127  -20.916 -2.843  1.00 27.87  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.542  -21.689 -1.764  1.00 29.77  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.849  -19.563 -2.631  1.00 27.04  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.745  -21.116 -0.514  1.00 31.34  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 14.979  -19.007 -1.375  1.00 28.28  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.409  -19.784 -0.311  1.00 28.00  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.626  -19.266 0.938   1.00 28.36  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.749  -21.993 -7.312  1.00 41.17  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.885  -22.755 -8.547  1.00 61.87  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 17.970  -23.838 -8.399  1.00 73.41  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 18.789  -23.723 -7.451  1.00 82.21  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.218  -21.828 -9.691  1.00 64.02  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 16.329  -20.719 -9.714  1.00 72.98  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 17.977  -24.761 -9.250  1.00 82.21  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.756  -10.787 -42.103 1.00 81.36  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.580  -11.950 -43.013 1.00 83.24  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 37.100  -12.338 -43.021 1.00 77.83  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.580  -12.822 -42.013 1.00 75.18  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.474  -13.121 -42.580 1.00 92.31  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.810  -14.109 -43.687 1.00 102.65 ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.928  -13.488 -44.964 1.00 106.93 ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 42.467  -13.189 -44.081 1.00 111.64 ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.372  -12.129 -44.149 1.00 64.33  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.922  -12.337 -44.177 1.00 57.56  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.580  -13.780 -43.816 1.00 58.91  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.368  -14.689 -44.066 1.00 52.45  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.517  -11.953 -45.610 1.00 60.45  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.666  -11.078 -46.078 1.00 56.91  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.905  -11.696 -45.453 1.00 56.60  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.425  -13.963 -43.164 1.00 60.79  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.976  -15.287 -42.755 1.00 63.57  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.577  -15.548 -43.315 1.00 58.05  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.939  -14.629 -43.841 1.00 58.82  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 33.145  -15.472 -41.243 1.00 69.01  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.549  -15.795 -40.841 1.00 76.72  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.328  -16.709 -41.521 1.00 74.19  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 35.299  -15.355 -39.814 1.00 73.67  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.507  -16.806 -40.923 1.00 68.06  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.511  -15.992 -39.888 1.00 74.73  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 31.126  -16.813 -43.238 1.00 46.34  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.815  -17.178 -43.744 1.00 47.12  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.801  -16.158 -43.239 1.00 47.42  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 28.084  -15.551 -44.032 1.00 47.61  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.440  -18.565 -43.284 1.00 49.40  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.790  -15.973 -41.915 1.00 44.44  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 28.024  -14.914 -41.267 1.00 47.88  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.902  -13.693 -40.982 1.00 47.59  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 30.060  -13.807 -40.571 1.00 46.88  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.377  -15.379 -39.959 1.00 45.68  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.198  -16.339 -40.098 1.00 40.49  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 24.909  -15.866 -40.336 1.00 37.59  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.384  -17.709 -39.935 1.00 40.51  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 23.837  -16.741 -40.427 1.00 38.81  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.310  -18.582 -40.025 1.00 33.57  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.036  -18.093 -40.243 1.00 36.76  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.317  -12.507 -41.155 1.00 44.30  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 29.071  -11.289 -40.912 1.00 52.03  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.273  -10.353 -40.003 1.00 47.83  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 27.035  -10.388 -40.017 1.00 42.11  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 29.369  -10.650 -42.265 1.00 47.29  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 28.128  -10.118 -42.962 1.00 41.29  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 28.413  -9.850  -44.432 1.00 53.23  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 27.238  -9.262  -45.150 1.00 52.07  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 26.144  -10.232 -45.295 1.00 58.20  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.951  -9.454  -39.240 1.00 51.31  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.267  -8.548  -38.314 1.00 43.03  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.168  -7.785  -39.035 1.00 41.02  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.340  -7.389  -40.191 1.00 48.01  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.408  -7.662  -37.830 1.00 51.27  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.615  -8.571  -37.883 1.00 50.45  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.408  -9.229  -39.239 1.00 54.58  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 26.006  -7.669  -38.370 1.00 36.18  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.810  -7.083  -38.936 1.00 33.36  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.869  -8.089  -39.600 1.00 33.32  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.755  -7.750  -39.964 1.00 35.15  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.325  -9.339  -39.812 1.00 35.42  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.421  -10.333 -40.370 1.00 33.11  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.304  -10.606 -39.356 1.00 28.74  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.577  -10.641 -38.161 1.00 33.02  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 24.185  -11.611 -40.677 1.00 38.53  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.856  -11.668 -42.048 1.00 45.64  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.483  -10.841 -42.915 1.00 45.31  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.734  -12.551 -42.228 1.00 41.31  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 21.081  -10.767 -39.846 1.00 31.03  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.958  -10.988 -38.950 1.00 31.18  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.620  -12.471 -38.964 1.00 30.29  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.673  -13.091 -40.026 1.00 33.68  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.799  -10.123 -39.425 1.00 30.76  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 19.144  -8.630  -39.589 1.00 29.01  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.861  -7.970  -39.951 1.00 32.68  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.748  -8.110  -38.275 1.00 30.51  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.269  -13.030 -37.791 1.00 27.92  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 19.031  -14.468 -37.755 1.00 27.62  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.920  -14.741 -36.748 1.00 31.24  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.509  -13.840 -36.008 1.00 28.08  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.320  -15.212 -37.322 1.00 26.45  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.472  -15.057 -38.331 1.00 31.00  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.770  -14.914 -35.877 1.00 26.44  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.451  -15.995 -36.733 1.00 28.28  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 16.914  -16.528 -35.493 1.00 28.27  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 18.009  -17.385 -34.880 1.00 29.52  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.614  -18.172 -35.620 1.00 29.91  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.678  -17.393 -35.755 1.00 26.03  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.470  -16.560 -36.147 1.00 30.25  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.222  -16.232 -37.482 1.00 30.23  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.600  -16.077 -35.175 1.00 30.40  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.119  -15.481 -37.821 1.00 34.67  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.496  -15.316 -35.520 1.00 30.80  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.248  -15.035 -36.853 1.00 37.68  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.181  -17.296 -33.537 1.00 25.23  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.235  -17.998 -32.833 1.00 26.09  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.612  -18.916 -31.778 1.00 27.31  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.645  -18.532 -31.120 1.00 27.64  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.192  -16.996 -32.221 1.00 29.85  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.082  -20.167 -31.742 1.00 25.79  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.462  -21.209 -30.929 1.00 29.15  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.290  -21.469 -29.684 1.00 28.45  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.478  -21.768 -29.776 1.00 31.52  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.306  -22.533 -31.695 1.00 33.09  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.552  -23.645 -30.926 1.00 30.07  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 16.107  -23.199 -30.644 1.00 35.73  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.220  -24.277 -29.997 1.00 38.20  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.660  -24.488 -28.617 1.00 32.87  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.650  -21.284 -28.522 1.00 30.14  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.251  -21.639 -27.240 1.00 32.15  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.415  -22.762 -26.622 1.00 29.86  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.195  -22.785 -26.767 1.00 30.31  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.301  -20.432 -26.291 1.00 33.12  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.140  -19.272 -26.811 1.00 33.23  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 21.917  -19.526 -26.617 1.00 43.28  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 21.960  -19.179 -24.851 1.00 38.98  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 19.087  -23.711 -25.960 1.00 31.88  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.365  -24.719 -25.193 1.00 33.83  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.401  -24.069 -24.189 1.00 29.86  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.760  -23.139 -23.464 1.00 37.30  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.385  -25.631 -24.501 1.00 46.63  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 18.805  -26.960 -23.995 1.00 48.06  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 19.628  -27.539 -22.846 1.00 48.13  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 16.148  -24.531 -24.185 1.00 33.53  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.148  -23.966 -23.284 1.00 33.58  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.279  -22.858 -23.891 1.00 36.33  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.337  -22.385 -23.240 1.00 35.87  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.622  -22.387 -25.104 1.00 31.17  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 13.926  -21.216 -25.629 1.00 28.99  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.581  -21.452 -27.089 1.00 28.33  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.287  -22.177 -27.779 1.00 32.91  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 14.854  -19.995 -25.634 1.00 27.68  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.263  -19.693 -24.197 1.00 33.75  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.490  -18.837 -23.414 1.00 31.78  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.341  -20.352 -23.611 1.00 33.99  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 14.815  -18.621 -22.079 1.00 37.26  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 16.681  -20.129 -22.281 1.00 41.64  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 15.916  -19.255 -21.527 1.00 40.45  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 16.250  -19.026 -20.221 1.00 45.19  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.544  -20.775 -27.604 1.00 29.52  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.234  -20.835 -29.039 1.00 27.13  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.296  -20.123 -29.867 1.00 29.68  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 13.951  -19.228 -29.369 1.00 26.53  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 10.905  -20.149 -29.147 1.00 28.09  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 10.855  -19.212 -27.935 1.00 32.46  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.622  -19.926 -26.832 1.00 29.42  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.441  -20.533 -31.140 1.00 26.34  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.281  -19.770 -32.073 1.00 30.51  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.022  -18.268 -31.917 1.00 25.11  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 12.880  -17.840 -31.989 1.00 27.54  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 13.946  -20.253 -33.495 1.00 27.44  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.268  -21.708 -33.680 1.00 28.65  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.377  -22.704 -33.303 1.00 29.24  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.332  -22.344 -34.213 1.00 30.28  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.918  -23.893 -33.572 1.00 32.26  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 15.085  -23.715 -34.145 1.00 30.27  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.075  -17.470 -31.726 1.00 25.59  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 14.849  -16.133 -31.164 1.00 26.32  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.390  -15.054 -32.105 1.00 25.27  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.527  -15.200 -32.540 1.00 24.82  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.571  -16.045 -29.814 1.00 26.12  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.068  -14.905 -28.963 1.00 27.17  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.342  -13.572 -29.110 1.00 27.43  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.124  -14.998 -27.857 1.00 30.08  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.649  -12.825 -28.174 1.00 28.65  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 13.888  -13.677 -27.400 1.00 29.48  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.461  -16.071 -27.226 1.00 27.07  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.043  -13.390 -26.315 1.00 29.93  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.621  -15.789 -26.154 1.00 27.54  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.366  -14.465 -25.761 1.00 27.76  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.646  -13.959 -32.429 1.00 27.62  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.178  -12.948 -33.362 1.00 25.75  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.476  -12.369 -32.805 1.00 27.44  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.549  -12.024 -31.623 1.00 26.48  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 14.021  -11.898 -33.429 1.00 26.50  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.190  -12.136 -32.156 1.00 28.67  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.272  -13.660 -31.973 1.00 26.81  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.543  -12.317 -33.616 1.00 27.04  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.843  -11.921 -33.103 1.00 25.16  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.684  -11.368 -34.254 1.00 25.41  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.226  -11.370 -35.398 1.00 29.73  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.540  -13.099 -32.456 1.00 28.13  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.880  -10.903 -33.906 1.00 29.11  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.846  -10.453 -34.901 1.00 32.60  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.250  -10.895 -34.519 1.00 28.96  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.545  -11.176 -33.354 1.00 29.22  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.837  -8.932  -35.085 1.00 32.17  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.405  -8.170  -33.900 1.00 32.94  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.161  -6.664  -34.051 1.00 31.72  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.745  -5.954  -32.909 1.00 30.84  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.498  -4.665  -32.609 1.00 32.17  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.600  -3.977  -33.299 1.00 27.86  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.164  -4.085  -31.620 1.00 30.92  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.117  -10.953 -35.551 1.00 29.90  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.546  -11.121 -35.377 1.00 33.98  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 26.091  -9.733  -35.034 1.00 31.50  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.758  -8.782  -35.730 1.00 35.47  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.186  -11.608 -36.694 1.00 36.07  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.425  -12.792 -37.303 1.00 37.01  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.679  -11.903 -36.509 1.00 38.49  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.440  -14.042 -36.447 1.00 36.97  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.832  -9.652  -33.939 1.00 34.99  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.495  -8.427  -33.509 1.00 41.42  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 28.977  -8.477  -33.888 1.00 45.76  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.527  -9.545  -34.126 1.00 46.80  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.395  -8.264  -32.005 1.00 37.99  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.117  -7.640  -31.459 1.00 41.32  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.293  -7.148  -32.264 1.00 42.34  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 25.955  -7.640  -30.217 1.00 40.35  ? 26  ASP B OD2 1 
ATOM   964  N N   A ASP B 1 28 ? 29.635  -7.315  -33.823 0.50 53.70  ? 27  ASP B N   1 
ATOM   965  N N   B ASP B 1 28 ? 29.614  -7.302  -33.955 0.50 54.00  ? 27  ASP B N   1 
ATOM   966  C CA  A ASP B 1 28 ? 31.073  -7.196  -34.020 0.50 52.50  ? 27  ASP B CA  1 
ATOM   967  C CA  B ASP B 1 28 ? 31.023  -7.220  -34.309 0.50 53.50  ? 27  ASP B CA  1 
ATOM   968  C C   A ASP B 1 28 ? 31.816  -7.938  -32.901 0.50 52.41  ? 27  ASP B C   1 
ATOM   969  C C   B ASP B 1 28 ? 31.875  -7.363  -33.041 0.50 51.09  ? 27  ASP B C   1 
ATOM   970  O O   A ASP B 1 28 ? 32.865  -7.423  -32.455 0.50 53.89  ? 27  ASP B O   1 
ATOM   971  O O   B ASP B 1 28 ? 31.331  -7.076  -31.946 0.50 51.39  ? 27  ASP B O   1 
ATOM   972  C CB  A ASP B 1 28 ? 31.454  -5.733  -34.176 0.50 51.05  ? 27  ASP B CB  1 
ATOM   973  C CB  B ASP B 1 28 ? 31.339  -5.942  -35.071 0.50 54.01  ? 27  ASP B CB  1 
ATOM   974  C CG  A ASP B 1 28 ? 30.771  -5.047  -35.349 0.50 48.06  ? 27  ASP B CG  1 
ATOM   975  C CG  B ASP B 1 28 ? 32.463  -6.059  -36.091 0.50 53.47  ? 27  ASP B CG  1 
ATOM   976  O OD1 A ASP B 1 28 ? 31.197  -5.290  -36.494 0.50 50.53  ? 27  ASP B OD1 1 
ATOM   977  O OD1 B ASP B 1 28 ? 33.472  -6.737  -35.791 0.50 56.54  ? 27  ASP B OD1 1 
ATOM   978  O OD2 A ASP B 1 28 ? 29.800  -4.306  -35.113 0.50 48.67  ? 27  ASP B OD2 1 
ATOM   979  O OD2 B ASP B 1 28 ? 32.325  -5.463  -37.176 0.50 50.62  ? 27  ASP B OD2 1 
ATOM   980  N N   . VAL B 1 34 ? 37.446  -10.141 -24.666 1.00 82.31  ? 33  VAL B N   1 
ATOM   981  C CA  . VAL B 1 34 ? 36.993  -11.509 -25.055 1.00 77.67  ? 33  VAL B CA  1 
ATOM   982  C C   . VAL B 1 34 ? 36.734  -11.505 -26.557 1.00 75.42  ? 33  VAL B C   1 
ATOM   983  O O   . VAL B 1 34 ? 36.298  -10.492 -27.095 1.00 83.23  ? 33  VAL B O   1 
ATOM   984  C CB  . VAL B 1 34 ? 35.716  -11.855 -24.263 1.00 72.84  ? 33  VAL B CB  1 
ATOM   985  C CG1 . VAL B 1 34 ? 34.667  -10.752 -24.380 1.00 66.27  ? 33  VAL B CG1 1 
ATOM   986  C CG2 . VAL B 1 34 ? 35.138  -13.215 -24.648 1.00 60.15  ? 33  VAL B CG2 1 
ATOM   987  N N   . LYS B 1 35 ? 37.052  -12.626 -27.218 1.00 74.42  ? 34  LYS B N   1 
ATOM   988  C CA  . LYS B 1 35 ? 36.595  -12.915 -28.574 1.00 68.46  ? 34  LYS B CA  1 
ATOM   989  C C   . LYS B 1 35 ? 35.754  -14.193 -28.539 1.00 62.32  ? 34  LYS B C   1 
ATOM   990  O O   . LYS B 1 35 ? 35.858  -14.967 -27.584 1.00 63.24  ? 34  LYS B O   1 
ATOM   991  C CB  . LYS B 1 35 ? 37.763  -13.042 -29.562 1.00 63.56  ? 34  LYS B CB  1 
ATOM   992  N N   . PRO B 1 36 ? 34.876  -14.467 -29.539 1.00 59.68  ? 35  PRO B N   1 
ATOM   993  C CA  . PRO B 1 36 ? 34.124  -15.725 -29.550 1.00 56.05  ? 35  PRO B CA  1 
ATOM   994  C C   . PRO B 1 36 ? 35.106  -16.890 -29.562 1.00 49.75  ? 35  PRO B C   1 
ATOM   995  O O   . PRO B 1 36 ? 36.190  -16.781 -30.132 1.00 54.88  ? 35  PRO B O   1 
ATOM   996  C CB  . PRO B 1 36 ? 33.274  -15.665 -30.837 1.00 50.60  ? 35  PRO B CB  1 
ATOM   997  C CG  . PRO B 1 36 ? 33.941  -14.583 -31.679 1.00 56.99  ? 35  PRO B CG  1 
ATOM   998  C CD  . PRO B 1 36 ? 34.548  -13.599 -30.685 1.00 55.21  ? 35  PRO B CD  1 
ATOM   999  N N   . PRO B 1 37 ? 34.777  -18.042 -28.936 1.00 53.87  ? 36  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 37 ? 35.584  -19.239 -29.135 1.00 50.11  ? 36  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 37 ? 35.577  -19.536 -30.640 1.00 58.43  ? 36  PRO B C   1 
ATOM   1002 O O   . PRO B 1 37 ? 34.782  -18.972 -31.408 1.00 46.63  ? 36  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 37 ? 34.859  -20.316 -28.311 1.00 52.29  ? 36  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 37 ? 34.020  -19.532 -27.328 1.00 55.31  ? 36  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 37 ? 33.622  -18.256 -28.049 1.00 48.82  ? 36  PRO B CD  1 
ATOM   1006 N N   . PRO B 1 38 ? 36.469  -20.436 -31.115 1.00 55.14  ? 37  PRO B N   1 
ATOM   1007 C CA  . PRO B 1 38 ? 36.518  -20.803 -32.538 1.00 58.53  ? 37  PRO B CA  1 
ATOM   1008 C C   . PRO B 1 38 ? 35.195  -21.337 -33.091 1.00 50.76  ? 37  PRO B C   1 
ATOM   1009 O O   . PRO B 1 38 ? 34.512  -22.121 -32.430 1.00 53.03  ? 37  PRO B O   1 
ATOM   1010 C CB  . PRO B 1 38 ? 37.638  -21.877 -32.598 1.00 61.84  ? 37  PRO B CB  1 
ATOM   1011 C CG  . PRO B 1 38 ? 38.459  -21.660 -31.334 1.00 55.46  ? 37  PRO B CG  1 
ATOM   1012 C CD  . PRO B 1 38 ? 37.479  -21.134 -30.299 1.00 65.07  ? 37  PRO B CD  1 
ATOM   1013 N N   . ASN B 1 39 ? 34.842  -20.905 -34.306 1.00 48.73  ? 38  ASN B N   1 
ATOM   1014 C CA  . ASN B 1 39 ? 33.666  -21.417 -35.002 1.00 52.51  ? 38  ASN B CA  1 
ATOM   1015 C C   . ASN B 1 39 ? 32.377  -20.732 -34.541 1.00 45.70  ? 38  ASN B C   1 
ATOM   1016 O O   . ASN B 1 39 ? 31.327  -21.010 -35.100 1.00 44.19  ? 38  ASN B O   1 
ATOM   1017 C CB  . ASN B 1 39 ? 33.452  -22.910 -34.766 1.00 52.52  ? 38  ASN B CB  1 
ATOM   1018 C CG  . ASN B 1 39 ? 34.605  -23.766 -35.239 1.00 62.84  ? 38  ASN B CG  1 
ATOM   1019 O OD1 . ASN B 1 39 ? 34.757  -24.897 -34.767 1.00 73.86  ? 38  ASN B OD1 1 
ATOM   1020 N ND2 . ASN B 1 39 ? 35.435  -23.255 -36.138 1.00 60.41  ? 38  ASN B ND2 1 
ATOM   1021 N N   . LYS B 1 40 ? 32.457  -19.821 -33.558 1.00 45.89  ? 39  LYS B N   1 
ATOM   1022 C CA  . LYS B 1 40 ? 31.261  -19.233 -32.970 1.00 45.37  ? 39  LYS B CA  1 
ATOM   1023 C C   . LYS B 1 40 ? 31.166  -17.736 -33.262 1.00 42.22  ? 39  LYS B C   1 
ATOM   1024 O O   . LYS B 1 40 ? 32.155  -17.087 -33.586 1.00 42.43  ? 39  LYS B O   1 
ATOM   1025 C CB  . LYS B 1 40 ? 31.271  -19.490 -31.463 1.00 45.77  ? 39  LYS B CB  1 
ATOM   1026 C CG  . LYS B 1 40 ? 30.977  -20.935 -31.093 1.00 49.97  ? 39  LYS B CG  1 
ATOM   1027 C CD  . LYS B 1 40 ? 30.708  -21.035 -29.596 1.00 61.13  ? 39  LYS B CD  1 
ATOM   1028 C CE  . LYS B 1 40 ? 29.676  -22.064 -29.247 1.00 67.53  ? 39  LYS B CE  1 
ATOM   1029 N NZ  . LYS B 1 40 ? 29.991  -23.365 -29.840 1.00 69.08  ? 39  LYS B NZ  1 
ATOM   1030 N N   . TYR B 1 41 ? 29.961  -17.187 -33.102 1.00 40.10  ? 40  TYR B N   1 
ATOM   1031 C CA  . TYR B 1 41 ? 29.769  -15.765 -33.327 1.00 38.83  ? 40  TYR B CA  1 
ATOM   1032 C C   . TYR B 1 41 ? 29.167  -15.105 -32.090 1.00 42.91  ? 40  TYR B C   1 
ATOM   1033 O O   . TYR B 1 41 ? 28.365  -15.720 -31.401 1.00 36.66  ? 40  TYR B O   1 
ATOM   1034 C CB  . TYR B 1 41 ? 28.757  -15.609 -34.458 1.00 38.48  ? 40  TYR B CB  1 
ATOM   1035 C CG  . TYR B 1 41 ? 29.267  -16.068 -35.815 1.00 39.56  ? 40  TYR B CG  1 
ATOM   1036 C CD1 . TYR B 1 41 ? 29.820  -15.152 -36.706 1.00 38.51  ? 40  TYR B CD1 1 
ATOM   1037 C CD2 . TYR B 1 41 ? 29.166  -17.398 -36.211 1.00 40.45  ? 40  TYR B CD2 1 
ATOM   1038 C CE1 . TYR B 1 41 ? 30.288  -15.567 -37.945 1.00 42.81  ? 40  TYR B CE1 1 
ATOM   1039 C CE2 . TYR B 1 41 ? 29.615  -17.814 -37.459 1.00 41.19  ? 40  TYR B CE2 1 
ATOM   1040 C CZ  . TYR B 1 41 ? 30.199  -16.894 -38.318 1.00 41.51  ? 40  TYR B CZ  1 
ATOM   1041 O OH  . TYR B 1 41 ? 30.654  -17.242 -39.574 1.00 42.31  ? 40  TYR B OH  1 
ATOM   1042 N N   . PRO B 1 42 ? 29.443  -13.798 -31.853 1.00 43.56  ? 41  PRO B N   1 
ATOM   1043 C CA  . PRO B 1 42 ? 28.745  -13.048 -30.812 1.00 38.28  ? 41  PRO B CA  1 
ATOM   1044 C C   . PRO B 1 42 ? 27.332  -12.752 -31.299 1.00 33.46  ? 41  PRO B C   1 
ATOM   1045 O O   . PRO B 1 42 ? 27.143  -12.124 -32.347 1.00 39.91  ? 41  PRO B O   1 
ATOM   1046 C CB  . PRO B 1 42 ? 29.585  -11.769 -30.658 1.00 40.67  ? 41  PRO B CB  1 
ATOM   1047 C CG  . PRO B 1 42 ? 30.214  -11.561 -32.026 1.00 41.36  ? 41  PRO B CG  1 
ATOM   1048 C CD  . PRO B 1 42 ? 30.382  -12.958 -32.618 1.00 39.64  ? 41  PRO B CD  1 
ATOM   1049 N N   . ILE B 1 43 ? 26.344  -13.209 -30.516 1.00 31.79  ? 42  ILE B N   1 
ATOM   1050 C CA  . ILE B 1 43 ? 24.936  -12.990 -30.817 1.00 29.69  ? 42  ILE B CA  1 
ATOM   1051 C C   . ILE B 1 43 ? 24.301  -12.003 -29.837 1.00 32.45  ? 42  ILE B C   1 
ATOM   1052 O O   . ILE B 1 43 ? 24.487  -12.151 -28.635 1.00 34.90  ? 42  ILE B O   1 
ATOM   1053 C CB  . ILE B 1 43 ? 24.185  -14.333 -30.751 1.00 30.68  ? 42  ILE B CB  1 
ATOM   1054 C CG1 . ILE B 1 43 ? 24.877  -15.469 -31.560 1.00 31.60  ? 42  ILE B CG1 1 
ATOM   1055 C CG2 . ILE B 1 43 ? 22.730  -14.143 -31.186 1.00 33.07  ? 42  ILE B CG2 1 
ATOM   1056 C CD1 . ILE B 1 43 ? 25.191  -15.155 -33.012 1.00 30.24  ? 42  ILE B CD1 1 
ATOM   1057 N N   . PHE B 1 44 ? 23.494  -11.074 -30.374 1.00 30.64  ? 43  PHE B N   1 
ATOM   1058 C CA  . PHE B 1 44 ? 22.610  -10.212 -29.592 1.00 32.70  ? 43  PHE B CA  1 
ATOM   1059 C C   . PHE B 1 44 ? 21.156  -10.659 -29.791 1.00 31.34  ? 43  PHE B C   1 
ATOM   1060 O O   . PHE B 1 44 ? 20.671  -10.729 -30.922 1.00 30.13  ? 43  PHE B O   1 
ATOM   1061 C CB  . PHE B 1 44 ? 22.851  -8.720  -29.888 1.00 34.01  ? 43  PHE B CB  1 
ATOM   1062 C CG  . PHE B 1 44 ? 21.788  -7.829  -29.244 1.00 35.86  ? 43  PHE B CG  1 
ATOM   1063 C CD1 . PHE B 1 44 ? 20.832  -7.159  -30.007 1.00 35.81  ? 43  PHE B CD1 1 
ATOM   1064 C CD2 . PHE B 1 44 ? 21.663  -7.772  -27.854 1.00 49.39  ? 43  PHE B CD2 1 
ATOM   1065 C CE1 . PHE B 1 44 ? 19.837  -6.396  -29.402 1.00 38.50  ? 43  PHE B CE1 1 
ATOM   1066 C CE2 . PHE B 1 44 ? 20.656  -7.028  -27.253 1.00 45.75  ? 43  PHE B CE2 1 
ATOM   1067 C CZ  . PHE B 1 44 ? 19.751  -6.336  -28.024 1.00 46.67  ? 43  PHE B CZ  1 
ATOM   1068 N N   . PHE B 1 45 ? 20.433  -10.900 -28.678 1.00 31.19  ? 44  PHE B N   1 
ATOM   1069 C CA  . PHE B 1 45 ? 19.040  -11.309 -28.776 1.00 28.92  ? 44  PHE B CA  1 
ATOM   1070 C C   . PHE B 1 45 ? 18.157  -10.081 -28.647 1.00 29.68  ? 44  PHE B C   1 
ATOM   1071 O O   . PHE B 1 45 ? 18.122  -9.430  -27.589 1.00 32.70  ? 44  PHE B O   1 
ATOM   1072 C CB  . PHE B 1 45 ? 18.690  -12.346 -27.698 1.00 31.67  ? 44  PHE B CB  1 
ATOM   1073 C CG  . PHE B 1 45 ? 19.502  -13.630 -27.833 1.00 26.76  ? 44  PHE B CG  1 
ATOM   1074 C CD1 . PHE B 1 45 ? 20.769  -13.738 -27.274 1.00 30.74  ? 44  PHE B CD1 1 
ATOM   1075 C CD2 . PHE B 1 45 ? 18.977  -14.729 -28.519 1.00 27.14  ? 44  PHE B CD2 1 
ATOM   1076 C CE1 . PHE B 1 45 ? 21.517  -14.901 -27.434 1.00 34.82  ? 44  PHE B CE1 1 
ATOM   1077 C CE2 . PHE B 1 45 ? 19.716  -15.908 -28.647 1.00 31.03  ? 44  PHE B CE2 1 
ATOM   1078 C CZ  . PHE B 1 45 ? 20.994  -15.974 -28.140 1.00 31.66  ? 44  PHE B CZ  1 
ATOM   1079 N N   . PHE B 1 46 ? 17.385  -9.812  -29.709 1.00 26.93  ? 45  PHE B N   1 
ATOM   1080 C CA  . PHE B 1 46 ? 16.524  -8.647  -29.697 1.00 27.06  ? 45  PHE B CA  1 
ATOM   1081 C C   . PHE B 1 46 ? 15.467  -8.806  -28.591 1.00 28.88  ? 45  PHE B C   1 
ATOM   1082 O O   . PHE B 1 46 ? 15.040  -9.912  -28.280 1.00 29.52  ? 45  PHE B O   1 
ATOM   1083 C CB  . PHE B 1 46 ? 15.823  -8.420  -31.026 1.00 26.39  ? 45  PHE B CB  1 
ATOM   1084 C CG  . PHE B 1 46 ? 16.780  -7.991  -32.129 1.00 29.68  ? 45  PHE B CG  1 
ATOM   1085 C CD1 . PHE B 1 46 ? 17.292  -6.692  -32.168 1.00 33.08  ? 45  PHE B CD1 1 
ATOM   1086 C CD2 . PHE B 1 46 ? 17.092  -8.864  -33.170 1.00 29.83  ? 45  PHE B CD2 1 
ATOM   1087 C CE1 . PHE B 1 46 ? 18.169  -6.286  -33.191 1.00 33.56  ? 45  PHE B CE1 1 
ATOM   1088 C CE2 . PHE B 1 46 ? 17.947  -8.448  -34.200 1.00 32.28  ? 45  PHE B CE2 1 
ATOM   1089 C CZ  . PHE B 1 46 ? 18.476  -7.161  -34.214 1.00 31.18  ? 45  PHE B CZ  1 
ATOM   1090 N N   . GLY B 1 47 ? 15.039  -7.675  -28.024 1.00 29.52  ? 46  GLY B N   1 
ATOM   1091 C CA  . GLY B 1 47 ? 13.951  -7.706  -27.043 1.00 30.87  ? 46  GLY B CA  1 
ATOM   1092 C C   . GLY B 1 47 ? 14.442  -7.932  -25.613 1.00 34.89  ? 46  GLY B C   1 
ATOM   1093 O O   . GLY B 1 47 ? 13.647  -7.786  -24.692 1.00 38.76  ? 46  GLY B O   1 
ATOM   1094 N N   . THR B 1 48 ? 15.691  -8.358  -25.431 1.00 32.81  ? 47  THR B N   1 
ATOM   1095 C CA  . THR B 1 48 ? 16.247  -8.793  -24.161 1.00 34.10  ? 47  THR B CA  1 
ATOM   1096 C C   . THR B 1 48 ? 17.537  -8.025  -23.921 1.00 38.99  ? 47  THR B C   1 
ATOM   1097 O O   . THR B 1 48 ? 18.015  -7.315  -24.808 1.00 40.30  ? 47  THR B O   1 
ATOM   1098 C CB  . THR B 1 48 ? 16.534  -10.304 -24.100 1.00 38.57  ? 47  THR B CB  1 
ATOM   1099 O OG1 . THR B 1 48 ? 17.642  -10.638 -24.933 1.00 36.65  ? 47  THR B OG1 1 
ATOM   1100 C CG2 . THR B 1 48 ? 15.360  -11.175 -24.491 1.00 39.32  ? 47  THR B CG2 1 
ATOM   1101 N N   . HIS B 1 49 ? 18.121  -8.240  -22.737 1.00 32.61  ? 48  HIS B N   1 
ATOM   1102 C CA  . HIS B 1 49 ? 19.469  -7.764  -22.456 1.00 42.71  ? 48  HIS B CA  1 
ATOM   1103 C C   . HIS B 1 49 ? 20.467  -8.918  -22.533 1.00 46.94  ? 48  HIS B C   1 
ATOM   1104 O O   . HIS B 1 49 ? 21.394  -8.956  -21.727 1.00 54.19  ? 48  HIS B O   1 
ATOM   1105 C CB  . HIS B 1 49 ? 19.534  -6.978  -21.128 1.00 48.53  ? 48  HIS B CB  1 
ATOM   1106 C CG  . HIS B 1 49 ? 19.017  -5.572  -21.265 1.00 61.55  ? 48  HIS B CG  1 
ATOM   1107 N ND1 . HIS B 1 49 ? 17.775  -5.157  -20.821 1.00 67.18  ? 48  HIS B ND1 1 
ATOM   1108 C CD2 . HIS B 1 49 ? 19.576  -4.486  -21.845 1.00 68.60  ? 48  HIS B CD2 1 
ATOM   1109 C CE1 . HIS B 1 49 ? 17.600  -3.872  -21.123 1.00 62.86  ? 48  HIS B CE1 1 
ATOM   1110 N NE2 . HIS B 1 49 ? 18.680  -3.446  -21.749 1.00 63.06  ? 48  HIS B NE2 1 
ATOM   1111 N N   . GLU B 1 50 ? 20.318  -9.826  -23.517 1.00 44.03  ? 49  GLU B N   1 
ATOM   1112 C CA  . GLU B 1 50 ? 21.163  -11.015 -23.522 1.00 44.36  ? 49  GLU B CA  1 
ATOM   1113 C C   . GLU B 1 50 ? 22.056  -11.086 -24.761 1.00 38.91  ? 49  GLU B C   1 
ATOM   1114 O O   . GLU B 1 50 ? 21.668  -10.713 -25.867 1.00 38.17  ? 49  GLU B O   1 
ATOM   1115 C CB  . GLU B 1 50 ? 20.277  -12.261 -23.483 1.00 47.67  ? 49  GLU B CB  1 
ATOM   1116 C CG  . GLU B 1 50 ? 19.302  -12.308 -22.307 1.00 47.54  ? 49  GLU B CG  1 
ATOM   1117 C CD  . GLU B 1 50 ? 19.986  -12.525 -20.971 1.00 61.79  ? 49  GLU B CD  1 
ATOM   1118 O OE1 . GLU B 1 50 ? 19.754  -11.709 -20.053 1.00 71.29  ? 49  GLU B OE1 1 
ATOM   1119 O OE2 . GLU B 1 50 ? 20.778  -13.484 -20.850 1.00 61.69  ? 49  GLU B OE2 1 
ATOM   1120 N N   . THR B 1 51 ? 23.285  -11.556 -24.550 1.00 37.25  ? 50  THR B N   1 
ATOM   1121 C CA  . THR B 1 51 ? 24.193  -11.973 -25.615 1.00 35.58  ? 50  THR B CA  1 
ATOM   1122 C C   . THR B 1 51 ? 24.681  -13.379 -25.274 1.00 38.41  ? 50  THR B C   1 
ATOM   1123 O O   . THR B 1 51 ? 24.572  -13.846 -24.143 1.00 34.85  ? 50  THR B O   1 
ATOM   1124 C CB  . THR B 1 51 ? 25.354  -10.979 -25.741 1.00 39.98  ? 50  THR B CB  1 
ATOM   1125 O OG1 . THR B 1 51 ? 25.964  -11.023 -24.456 1.00 43.14  ? 50  THR B OG1 1 
ATOM   1126 C CG2 . THR B 1 51 ? 24.932  -9.538  -25.975 1.00 38.49  ? 50  THR B CG2 1 
ATOM   1127 N N   . ALA B 1 52 ? 25.206  -14.087 -26.274 1.00 37.71  ? 51  ALA B N   1 
ATOM   1128 C CA  . ALA B 1 52 ? 25.837  -15.379 -26.069 1.00 33.98  ? 51  ALA B CA  1 
ATOM   1129 C C   . ALA B 1 52 ? 26.691  -15.659 -27.303 1.00 36.78  ? 51  ALA B C   1 
ATOM   1130 O O   . ALA B 1 52 ? 26.610  -14.932 -28.298 1.00 40.95  ? 51  ALA B O   1 
ATOM   1131 C CB  . ALA B 1 52 ? 24.794  -16.439 -25.881 1.00 33.74  ? 51  ALA B CB  1 
ATOM   1132 N N   . PHE B 1 53 ? 27.523  -16.695 -27.217 1.00 35.36  ? 52  PHE B N   1 
ATOM   1133 C CA  . PHE B 1 53 ? 28.266  -17.159 -28.376 1.00 39.95  ? 52  PHE B CA  1 
ATOM   1134 C C   . PHE B 1 53 ? 27.587  -18.425 -28.898 1.00 37.78  ? 52  PHE B C   1 
ATOM   1135 O O   . PHE B 1 53 ? 27.307  -19.330 -28.120 1.00 38.18  ? 52  PHE B O   1 
ATOM   1136 C CB  . PHE B 1 53 ? 29.710  -17.440 -27.940 1.00 44.45  ? 52  PHE B CB  1 
ATOM   1137 C CG  . PHE B 1 53 ? 30.517  -16.226 -27.504 1.00 45.31  ? 52  PHE B CG  1 
ATOM   1138 C CD1 . PHE B 1 53 ? 30.633  -15.117 -28.329 1.00 45.50  ? 52  PHE B CD1 1 
ATOM   1139 C CD2 . PHE B 1 53 ? 31.119  -16.185 -26.248 1.00 50.40  ? 52  PHE B CD2 1 
ATOM   1140 C CE1 . PHE B 1 53 ? 31.360  -14.005 -27.934 1.00 46.98  ? 52  PHE B CE1 1 
ATOM   1141 C CE2 . PHE B 1 53 ? 31.840  -15.068 -25.846 1.00 44.77  ? 52  PHE B CE2 1 
ATOM   1142 C CZ  . PHE B 1 53 ? 31.954  -13.977 -26.681 1.00 44.82  ? 52  PHE B CZ  1 
ATOM   1143 N N   . LEU B 1 54 ? 27.308  -18.467 -30.216 1.00 36.45  ? 53  LEU B N   1 
ATOM   1144 C CA  . LEU B 1 54 ? 26.656  -19.613 -30.828 1.00 34.16  ? 53  LEU B CA  1 
ATOM   1145 C C   . LEU B 1 54 ? 27.395  -20.000 -32.106 1.00 34.13  ? 53  LEU B C   1 
ATOM   1146 O O   . LEU B 1 54 ? 27.903  -19.128 -32.817 1.00 35.51  ? 53  LEU B O   1 
ATOM   1147 C CB  . LEU B 1 54 ? 25.199  -19.323 -31.192 1.00 32.50  ? 53  LEU B CB  1 
ATOM   1148 C CG  . LEU B 1 54 ? 24.196  -19.265 -30.038 1.00 32.81  ? 53  LEU B CG  1 
ATOM   1149 C CD1 . LEU B 1 54 ? 22.811  -18.913 -30.557 1.00 31.84  ? 53  LEU B CD1 1 
ATOM   1150 C CD2 . LEU B 1 54 ? 24.171  -20.629 -29.348 1.00 32.09  ? 53  LEU B CD2 1 
ATOM   1151 N N   . GLY B 1 55 ? 27.313  -21.285 -32.447 1.00 35.59  ? 54  GLY B N   1 
ATOM   1152 C CA  . GLY B 1 55 ? 27.817  -21.760 -33.727 1.00 36.36  ? 54  GLY B CA  1 
ATOM   1153 C C   . GLY B 1 55 ? 26.712  -21.765 -34.784 1.00 34.09  ? 54  GLY B C   1 
ATOM   1154 O O   . GLY B 1 55 ? 25.523  -21.676 -34.473 1.00 32.44  ? 54  GLY B O   1 
ATOM   1155 N N   . PRO B 1 56 ? 27.066  -21.903 -36.085 1.00 33.09  ? 55  PRO B N   1 
ATOM   1156 C CA  . PRO B 1 56 ? 26.082  -21.939 -37.162 1.00 30.67  ? 55  PRO B CA  1 
ATOM   1157 C C   . PRO B 1 56 ? 24.891  -22.890 -37.074 1.00 27.58  ? 55  PRO B C   1 
ATOM   1158 O O   . PRO B 1 56 ? 23.849  -22.598 -37.624 1.00 28.30  ? 55  PRO B O   1 
ATOM   1159 C CB  . PRO B 1 56 ? 26.951  -22.289 -38.380 1.00 34.07  ? 55  PRO B CB  1 
ATOM   1160 C CG  . PRO B 1 56 ? 28.341  -21.846 -38.028 1.00 35.78  ? 55  PRO B CG  1 
ATOM   1161 C CD  . PRO B 1 56 ? 28.455  -22.046 -36.542 1.00 36.18  ? 55  PRO B CD  1 
ATOM   1162 N N   . LYS B 1 57 ? 25.063  -24.052 -36.415 1.00 30.47  ? 56  LYS B N   1 
ATOM   1163 C CA  . LYS B 1 57 ? 24.003  -25.048 -36.323 1.00 33.14  ? 56  LYS B CA  1 
ATOM   1164 C C   . LYS B 1 57 ? 22.784  -24.425 -35.647 1.00 31.94  ? 56  LYS B C   1 
ATOM   1165 O O   . LYS B 1 57 ? 21.642  -24.839 -35.889 1.00 30.92  ? 56  LYS B O   1 
ATOM   1166 C CB  . LYS B 1 57 ? 24.487  -26.314 -35.593 1.00 34.52  ? 56  LYS B CB  1 
ATOM   1167 C CG  . LYS B 1 57 ? 24.738  -26.196 -34.107 1.00 37.08  ? 56  LYS B CG  1 
ATOM   1168 C CD  . LYS B 1 57 ? 24.822  -27.565 -33.435 1.00 41.35  ? 56  LYS B CD  1 
ATOM   1169 C CE  . LYS B 1 57 ? 25.185  -27.514 -31.951 1.00 44.01  ? 56  LYS B CE  1 
ATOM   1170 N NZ  . LYS B 1 57 ? 24.107  -26.994 -31.102 1.00 48.60  ? 56  LYS B NZ  1 
ATOM   1171 N N   . ASP B 1 58 ? 23.054  -23.383 -34.842 1.00 31.30  ? 57  ASP B N   1 
ATOM   1172 C CA  . ASP B 1 58 ? 22.006  -22.747 -34.060 1.00 32.59  ? 57  ASP B CA  1 
ATOM   1173 C C   . ASP B 1 58 ? 21.600  -21.389 -34.632 1.00 31.51  ? 57  ASP B C   1 
ATOM   1174 O O   . ASP B 1 58 ? 20.837  -20.660 -33.961 1.00 28.43  ? 57  ASP B O   1 
ATOM   1175 C CB  . ASP B 1 58 ? 22.411  -22.650 -32.591 1.00 34.79  ? 57  ASP B CB  1 
ATOM   1176 C CG  . ASP B 1 58 ? 22.410  -24.000 -31.877 1.00 38.96  ? 57  ASP B CG  1 
ATOM   1177 O OD1 . ASP B 1 58 ? 21.468  -24.767 -32.104 1.00 35.82  ? 57  ASP B OD1 1 
ATOM   1178 O OD2 . ASP B 1 58 ? 23.353  -24.272 -31.122 1.00 39.14  ? 57  ASP B OD2 1 
ATOM   1179 N N   . LEU B 1 59 ? 22.059  -21.082 -35.867 1.00 29.93  ? 58  LEU B N   1 
ATOM   1180 C CA  . LEU B 1 59 ? 21.864  -19.770 -36.491 1.00 28.65  ? 58  LEU B CA  1 
ATOM   1181 C C   . LEU B 1 59 ? 21.126  -19.916 -37.816 1.00 29.53  ? 58  LEU B C   1 
ATOM   1182 O O   . LEU B 1 59 ? 21.616  -20.571 -38.750 1.00 29.78  ? 58  LEU B O   1 
ATOM   1183 C CB  . LEU B 1 59 ? 23.164  -18.985 -36.684 1.00 30.28  ? 58  LEU B CB  1 
ATOM   1184 C CG  . LEU B 1 59 ? 23.985  -18.728 -35.417 1.00 28.45  ? 58  LEU B CG  1 
ATOM   1185 C CD1 . LEU B 1 59 ? 25.382  -18.142 -35.631 1.00 31.06  ? 58  LEU B CD1 1 
ATOM   1186 C CD2 . LEU B 1 59 ? 23.184  -17.901 -34.391 1.00 29.74  ? 58  LEU B CD2 1 
ATOM   1187 N N   . PHE B 1 60 ? 19.925  -19.341 -37.871 1.00 26.55  ? 59  PHE B N   1 
ATOM   1188 C CA  . PHE B 1 60 ? 19.018  -19.524 -38.995 1.00 27.44  ? 59  PHE B CA  1 
ATOM   1189 C C   . PHE B 1 60 ? 18.856  -18.172 -39.691 1.00 30.13  ? 59  PHE B C   1 
ATOM   1190 O O   . PHE B 1 60 ? 18.274  -17.246 -39.128 1.00 28.54  ? 59  PHE B O   1 
ATOM   1191 C CB  . PHE B 1 60 ? 17.657  -20.036 -38.480 1.00 26.38  ? 59  PHE B CB  1 
ATOM   1192 C CG  . PHE B 1 60 ? 17.757  -21.440 -37.880 1.00 28.35  ? 59  PHE B CG  1 
ATOM   1193 C CD1 . PHE B 1 60 ? 18.299  -21.629 -36.603 1.00 31.37  ? 59  PHE B CD1 1 
ATOM   1194 C CD2 . PHE B 1 60 ? 17.336  -22.559 -38.605 1.00 30.07  ? 59  PHE B CD2 1 
ATOM   1195 C CE1 . PHE B 1 60 ? 18.467  -22.909 -36.068 1.00 31.67  ? 59  PHE B CE1 1 
ATOM   1196 C CE2 . PHE B 1 60 ? 17.472  -23.842 -38.059 1.00 32.95  ? 59  PHE B CE2 1 
ATOM   1197 C CZ  . PHE B 1 60 ? 18.048  -24.015 -36.806 1.00 34.03  ? 59  PHE B CZ  1 
ATOM   1198 N N   . PRO B 1 61 ? 19.336  -17.980 -40.944 1.00 33.70  ? 60  PRO B N   1 
ATOM   1199 C CA  . PRO B 1 61 ? 19.129  -16.688 -41.608 1.00 34.28  ? 60  PRO B CA  1 
ATOM   1200 C C   . PRO B 1 61 ? 17.692  -16.165 -41.549 1.00 30.04  ? 60  PRO B C   1 
ATOM   1201 O O   . PRO B 1 61 ? 16.721  -16.869 -41.838 1.00 28.24  ? 60  PRO B O   1 
ATOM   1202 C CB  . PRO B 1 61 ? 19.676  -16.935 -43.050 1.00 31.07  ? 60  PRO B CB  1 
ATOM   1203 C CG  . PRO B 1 61 ? 20.692  -18.043 -42.870 1.00 37.48  ? 60  PRO B CG  1 
ATOM   1204 C CD  . PRO B 1 61 ? 20.094  -18.945 -41.772 1.00 33.25  ? 60  PRO B CD  1 
ATOM   1205 N N   . TYR B 1 62 ? 17.531  -14.869 -41.219 1.00 29.60  ? 61  TYR B N   1 
ATOM   1206 C CA  . TYR B 1 62 ? 16.230  -14.331 -40.861 1.00 32.19  ? 61  TYR B CA  1 
ATOM   1207 C C   . TYR B 1 62 ? 15.253  -14.311 -42.029 1.00 32.90  ? 61  TYR B C   1 
ATOM   1208 O O   . TYR B 1 62 ? 14.103  -14.708 -41.871 1.00 32.88  ? 61  TYR B O   1 
ATOM   1209 C CB  . TYR B 1 62 ? 16.407  -12.895 -40.349 1.00 33.36  ? 61  TYR B CB  1 
ATOM   1210 C CG  . TYR B 1 62 ? 15.086  -12.177 -40.123 1.00 35.30  ? 61  TYR B CG  1 
ATOM   1211 C CD1 . TYR B 1 62 ? 14.318  -12.433 -38.993 1.00 34.11  ? 61  TYR B CD1 1 
ATOM   1212 C CD2 . TYR B 1 62 ? 14.643  -11.209 -41.018 1.00 37.46  ? 61  TYR B CD2 1 
ATOM   1213 C CE1 . TYR B 1 62 ? 13.123  -11.773 -38.785 1.00 37.08  ? 61  TYR B CE1 1 
ATOM   1214 C CE2 . TYR B 1 62 ? 13.448  -10.536 -40.819 1.00 43.70  ? 61  TYR B CE2 1 
ATOM   1215 C CZ  . TYR B 1 62 ? 12.695  -10.819 -39.695 1.00 36.41  ? 61  TYR B CZ  1 
ATOM   1216 O OH  . TYR B 1 62 ? 11.529  -10.170 -39.479 1.00 39.81  ? 61  TYR B OH  1 
ATOM   1217 N N   . ASP B 1 63 ? 15.720  -13.873 -43.216 1.00 37.80  ? 62  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 63 ? 14.836  -13.824 -44.382 1.00 41.84  ? 62  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 63 ? 14.309  -15.215 -44.740 1.00 37.64  ? 62  ASP B C   1 
ATOM   1220 O O   . ASP B 1 63 ? 13.108  -15.391 -44.931 1.00 40.60  ? 62  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 63 ? 15.464  -13.078 -45.549 1.00 48.34  ? 62  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 63 ? 15.204  -11.577 -45.582 1.00 63.41  ? 62  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 63 ? 14.439  -11.080 -44.719 1.00 64.80  ? 62  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 63 ? 15.763  -10.907 -46.478 1.00 77.32  ? 62  ASP B OD2 1 
ATOM   1225 N N   . LYS B 1 64 ? 15.206  -16.203 -44.775 1.00 40.24  ? 63  LYS B N   1 
ATOM   1226 C CA  . LYS B 1 64 ? 14.827  -17.571 -45.095 1.00 38.26  ? 63  LYS B CA  1 
ATOM   1227 C C   . LYS B 1 64 ? 13.798  -18.132 -44.104 1.00 38.32  ? 63  LYS B C   1 
ATOM   1228 O O   . LYS B 1 64 ? 12.888  -18.873 -44.498 1.00 40.26  ? 63  LYS B O   1 
ATOM   1229 C CB  . LYS B 1 64 ? 16.059  -18.480 -45.074 1.00 42.52  ? 63  LYS B CB  1 
ATOM   1230 C CG  . LYS B 1 64 ? 15.748  -19.878 -45.586 1.00 39.98  ? 63  LYS B CG  1 
ATOM   1231 C CD  . LYS B 1 64 ? 17.001  -20.724 -45.713 1.00 47.71  ? 63  LYS B CD  1 
ATOM   1232 C CE  . LYS B 1 64 ? 16.770  -21.996 -46.490 1.00 51.47  ? 63  LYS B CE  1 
ATOM   1233 N NZ  . LYS B 1 64 ? 15.658  -22.837 -46.049 1.00 48.04  ? 63  LYS B NZ  1 
ATOM   1234 N N   . SER B 1 65 ? 13.948  -17.789 -42.820 1.00 35.43  ? 64  SER B N   1 
ATOM   1235 C CA  . SER B 1 65 ? 13.300  -18.571 -41.766 1.00 35.97  ? 64  SER B CA  1 
ATOM   1236 C C   . SER B 1 65 ? 12.184  -17.805 -41.042 1.00 37.15  ? 64  SER B C   1 
ATOM   1237 O O   . SER B 1 65 ? 11.515  -18.360 -40.181 1.00 33.55  ? 64  SER B O   1 
ATOM   1238 C CB  . SER B 1 65 ? 14.327  -19.131 -40.818 1.00 38.72  ? 64  SER B CB  1 
ATOM   1239 O OG  . SER B 1 65 ? 15.108  -18.085 -40.263 1.00 50.16  ? 64  SER B OG  1 
ATOM   1240 N N   . LYS B 1 66 ? 11.913  -16.560 -41.454 1.00 36.32  ? 65  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 66 ? 10.961  -15.710 -40.740 1.00 38.87  ? 65  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 66 ? 9.513   -16.201 -40.776 1.00 40.53  ? 65  LYS B C   1 
ATOM   1243 O O   . LYS B 1 66 ? 8.765   -15.897 -39.858 1.00 41.24  ? 65  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 66 ? 11.034  -14.212 -41.072 1.00 39.25  ? 65  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 66 ? 10.779  -13.868 -42.549 1.00 37.02  ? 65  LYS B CG  1 
ATOM   1246 N N   . ASP B 1 67 ? 9.043   -16.912 -41.812 1.00 37.13  ? 66  ASP B N   1 
ATOM   1247 C CA  . ASP B 1 67 ? 7.650   -17.317 -41.661 1.00 43.82  ? 66  ASP B CA  1 
ATOM   1248 C C   . ASP B 1 67 ? 7.531   -18.584 -40.810 1.00 43.66  ? 66  ASP B C   1 
ATOM   1249 O O   . ASP B 1 67 ? 6.453   -18.900 -40.300 1.00 47.17  ? 66  ASP B O   1 
ATOM   1250 C CB  . ASP B 1 67 ? 6.811   -17.190 -42.926 1.00 60.53  ? 66  ASP B CB  1 
ATOM   1251 C CG  . ASP B 1 67 ? 7.399   -17.822 -44.177 1.00 73.43  ? 66  ASP B CG  1 
ATOM   1252 O OD1 . ASP B 1 67 ? 6.697   -17.842 -45.217 1.00 71.60  ? 66  ASP B OD1 1 
ATOM   1253 O OD2 . ASP B 1 67 ? 8.559   -18.275 -44.102 1.00 84.22  ? 66  ASP B OD2 1 
ATOM   1254 N N   . LYS B 1 68 ? 8.649   -19.283 -40.612 1.00 39.62  ? 67  LYS B N   1 
ATOM   1255 C CA  . LYS B 1 68 ? 8.629   -20.451 -39.742 1.00 35.77  ? 67  LYS B CA  1 
ATOM   1256 C C   . LYS B 1 68 ? 8.756   -20.028 -38.279 1.00 36.27  ? 67  LYS B C   1 
ATOM   1257 O O   . LYS B 1 68 ? 8.001   -20.509 -37.429 1.00 34.95  ? 67  LYS B O   1 
ATOM   1258 C CB  . LYS B 1 68 ? 9.699   -21.426 -40.233 1.00 42.91  ? 67  LYS B CB  1 
ATOM   1259 C CG  . LYS B 1 68 ? 9.805   -22.747 -39.480 1.00 46.97  ? 67  LYS B CG  1 
ATOM   1260 C CD  . LYS B 1 68 ? 10.762  -23.652 -40.248 1.00 56.25  ? 67  LYS B CD  1 
ATOM   1261 C CE  . LYS B 1 68 ? 11.062  -24.950 -39.563 1.00 61.66  ? 67  LYS B CE  1 
ATOM   1262 N NZ  . LYS B 1 68 ? 9.870   -25.787 -39.423 1.00 62.65  ? 67  LYS B NZ  1 
ATOM   1263 N N   . TYR B 1 69 ? 9.702   -19.124 -37.983 1.00 32.13  ? 68  TYR B N   1 
ATOM   1264 C CA  . TYR B 1 69 ? 10.033  -18.869 -36.576 1.00 28.09  ? 68  TYR B CA  1 
ATOM   1265 C C   . TYR B 1 69 ? 9.517   -17.518 -36.091 1.00 37.93  ? 68  TYR B C   1 
ATOM   1266 O O   . TYR B 1 69 ? 9.565   -17.256 -34.883 1.00 34.55  ? 68  TYR B O   1 
ATOM   1267 C CB  . TYR B 1 69 ? 11.539  -18.916 -36.335 1.00 30.32  ? 68  TYR B CB  1 
ATOM   1268 C CG  . TYR B 1 69 ? 12.144  -20.282 -36.649 1.00 29.77  ? 68  TYR B CG  1 
ATOM   1269 C CD1 . TYR B 1 69 ? 11.639  -21.451 -36.084 1.00 34.18  ? 68  TYR B CD1 1 
ATOM   1270 C CD2 . TYR B 1 69 ? 13.218  -20.392 -37.518 1.00 31.99  ? 68  TYR B CD2 1 
ATOM   1271 C CE1 . TYR B 1 69 ? 12.202  -22.694 -36.348 1.00 35.27  ? 68  TYR B CE1 1 
ATOM   1272 C CE2 . TYR B 1 69 ? 13.777  -21.628 -37.813 1.00 37.55  ? 68  TYR B CE2 1 
ATOM   1273 C CZ  . TYR B 1 69 ? 13.253  -22.781 -37.243 1.00 36.89  ? 68  TYR B CZ  1 
ATOM   1274 O OH  . TYR B 1 69 ? 13.809  -23.988 -37.541 1.00 38.28  ? 68  TYR B OH  1 
ATOM   1275 N N   . GLY B 1 70 ? 8.993   -16.685 -37.009 1.00 36.19  ? 69  GLY B N   1 
ATOM   1276 C CA  . GLY B 1 70 ? 8.790   -15.281 -36.669 1.00 40.83  ? 69  GLY B CA  1 
ATOM   1277 C C   . GLY B 1 70 ? 7.397   -14.981 -36.112 1.00 45.57  ? 69  GLY B C   1 
ATOM   1278 O O   . GLY B 1 70 ? 6.819   -13.948 -36.445 1.00 44.96  ? 69  GLY B O   1 
ATOM   1279 N N   . LYS B 1 71 ? 6.869   -15.881 -35.271 1.00 45.28  ? 70  LYS B N   1 
ATOM   1280 C CA  . LYS B 1 71 ? 5.494   -15.772 -34.816 1.00 45.42  ? 70  LYS B CA  1 
ATOM   1281 C C   . LYS B 1 71 ? 5.494   -15.433 -33.333 1.00 49.70  ? 70  LYS B C   1 
ATOM   1282 O O   . LYS B 1 71 ? 6.327   -15.960 -32.598 1.00 42.35  ? 70  LYS B O   1 
ATOM   1283 C CB  . LYS B 1 71 ? 4.804   -17.125 -35.018 1.00 50.00  ? 70  LYS B CB  1 
ATOM   1284 C CG  . LYS B 1 71 ? 4.525   -17.353 -36.508 1.00 57.11  ? 70  LYS B CG  1 
ATOM   1285 C CD  . LYS B 1 71 ? 4.140   -18.762 -36.946 1.00 55.87  ? 70  LYS B CD  1 
ATOM   1286 C CE  . LYS B 1 71 ? 3.592   -18.769 -38.354 1.00 57.88  ? 70  LYS B CE  1 
ATOM   1287 N NZ  . LYS B 1 71 ? 4.362   -17.973 -39.321 1.00 62.62  ? 70  LYS B NZ  1 
ATOM   1288 N N   . PRO B 1 72 ? 4.572   -14.563 -32.853 1.00 47.34  ? 71  PRO B N   1 
ATOM   1289 C CA  . PRO B 1 72 ? 4.582   -14.138 -31.445 1.00 47.42  ? 71  PRO B CA  1 
ATOM   1290 C C   . PRO B 1 72 ? 4.342   -15.305 -30.484 1.00 46.60  ? 71  PRO B C   1 
ATOM   1291 O O   . PRO B 1 72 ? 3.726   -16.292 -30.876 1.00 40.79  ? 71  PRO B O   1 
ATOM   1292 C CB  . PRO B 1 72 ? 3.482   -13.051 -31.363 1.00 48.73  ? 71  PRO B CB  1 
ATOM   1293 C CG  . PRO B 1 72 ? 3.246   -12.655 -32.805 1.00 51.17  ? 71  PRO B CG  1 
ATOM   1294 C CD  . PRO B 1 72 ? 3.511   -13.912 -33.645 1.00 49.44  ? 71  PRO B CD  1 
ATOM   1295 N N   . ASN B 1 73 ? 4.824   -15.191 -29.227 1.00 40.24  ? 72  ASN B N   1 
ATOM   1296 C CA  . ASN B 1 73 ? 4.572   -16.236 -28.237 1.00 39.94  ? 72  ASN B CA  1 
ATOM   1297 C C   . ASN B 1 73 ? 4.544   -15.615 -26.828 1.00 42.69  ? 72  ASN B C   1 
ATOM   1298 O O   . ASN B 1 73 ? 4.504   -14.391 -26.701 1.00 47.06  ? 72  ASN B O   1 
ATOM   1299 C CB  . ASN B 1 73 ? 5.588   -17.371 -28.304 1.00 41.55  ? 72  ASN B CB  1 
ATOM   1300 C CG  . ASN B 1 73 ? 7.002   -16.887 -28.088 1.00 38.15  ? 72  ASN B CG  1 
ATOM   1301 O OD1 . ASN B 1 73 ? 7.269   -16.152 -27.124 1.00 34.14  ? 72  ASN B OD1 1 
ATOM   1302 N ND2 . ASN B 1 73 ? 7.911   -17.262 -28.982 1.00 33.28  ? 72  ASN B ND2 1 
ATOM   1303 N N   . LYS B 1 74 ? 4.667   -16.462 -25.799 1.00 45.81  ? 73  LYS B N   1 
ATOM   1304 C CA  . LYS B 1 74 ? 4.426   -16.080 -24.407 1.00 50.63  ? 73  LYS B CA  1 
ATOM   1305 C C   . LYS B 1 74 ? 5.706   -15.678 -23.661 1.00 47.68  ? 73  LYS B C   1 
ATOM   1306 O O   . LYS B 1 74 ? 5.637   -15.286 -22.490 1.00 42.03  ? 73  LYS B O   1 
ATOM   1307 C CB  . LYS B 1 74 ? 3.847   -17.296 -23.669 1.00 46.69  ? 73  LYS B CB  1 
ATOM   1308 N N   . ARG B 1 75 ? 6.867   -15.799 -24.323 1.00 32.05  ? 74  ARG B N   1 
ATOM   1309 C CA  . ARG B 1 75 ? 8.169   -15.584 -23.704 1.00 30.38  ? 74  ARG B CA  1 
ATOM   1310 C C   . ARG B 1 75 ? 8.477   -14.091 -23.642 1.00 30.19  ? 74  ARG B C   1 
ATOM   1311 O O   . ARG B 1 75 ? 8.241   -13.343 -24.608 1.00 36.54  ? 74  ARG B O   1 
ATOM   1312 C CB  . ARG B 1 75 ? 9.308   -16.364 -24.381 1.00 35.68  ? 74  ARG B CB  1 
ATOM   1313 C CG  . ARG B 1 75 ? 9.125   -17.855 -24.627 1.00 30.04  ? 74  ARG B CG  1 
ATOM   1314 C CD  . ARG B 1 75 ? 8.984   -18.619 -23.297 1.00 33.64  ? 74  ARG B CD  1 
ATOM   1315 N NE  . ARG B 1 75 ? 9.184   -20.048 -23.522 1.00 36.90  ? 74  ARG B NE  1 
ATOM   1316 C CZ  . ARG B 1 75 ? 10.316  -20.684 -23.324 1.00 33.80  ? 74  ARG B CZ  1 
ATOM   1317 N NH1 . ARG B 1 75 ? 11.402  -20.034 -22.906 1.00 40.26  ? 74  ARG B NH1 1 
ATOM   1318 N NH2 . ARG B 1 75 ? 10.393  -21.967 -23.627 1.00 38.56  ? 74  ARG B NH2 1 
ATOM   1319 N N   . LYS B 1 76 ? 8.962   -13.658 -22.461 1.00 30.00  ? 75  LYS B N   1 
ATOM   1320 C CA  . LYS B 1 76 ? 9.239   -12.264 -22.174 1.00 26.22  ? 75  LYS B CA  1 
ATOM   1321 C C   . LYS B 1 76 ? 10.321  -11.743 -23.130 1.00 28.63  ? 75  LYS B C   1 
ATOM   1322 O O   . LYS B 1 76 ? 11.412  -12.297 -23.160 1.00 28.71  ? 75  LYS B O   1 
ATOM   1323 C CB  . LYS B 1 76 ? 9.808   -12.167 -20.747 1.00 33.12  ? 75  LYS B CB  1 
ATOM   1324 C CG  . LYS B 1 76 ? 10.125  -10.723 -20.352 1.00 33.30  ? 75  LYS B CG  1 
ATOM   1325 C CD  . LYS B 1 76 ? 10.695  -10.560 -18.957 1.00 37.98  ? 75  LYS B CD  1 
ATOM   1326 C CE  . LYS B 1 76 ? 10.903  -9.104  -18.566 1.00 47.03  ? 75  LYS B CE  1 
ATOM   1327 N NZ  . LYS B 1 76 ? 11.177  -8.969  -17.125 1.00 51.12  ? 75  LYS B NZ  1 
ATOM   1328 N N   . GLY B 1 77 ? 10.006  -10.657 -23.837 1.00 29.31  ? 76  GLY B N   1 
ATOM   1329 C CA  . GLY B 1 77 ? 10.965  -9.986  -24.714 1.00 32.03  ? 76  GLY B CA  1 
ATOM   1330 C C   . GLY B 1 77 ? 10.812  -10.432 -26.170 1.00 30.18  ? 76  GLY B C   1 
ATOM   1331 O O   . GLY B 1 77 ? 11.407  -9.841  -27.071 1.00 30.28  ? 76  GLY B O   1 
ATOM   1332 N N   . PHE B 1 78 ? 10.045  -11.498 -26.420 1.00 28.65  ? 77  PHE B N   1 
ATOM   1333 C CA  . PHE B 1 78 ? 9.978   -12.049 -27.785 1.00 28.42  ? 77  PHE B CA  1 
ATOM   1334 C C   . PHE B 1 78 ? 9.254   -11.117 -28.755 1.00 32.42  ? 77  PHE B C   1 
ATOM   1335 O O   . PHE B 1 78 ? 9.758   -10.860 -29.857 1.00 29.14  ? 77  PHE B O   1 
ATOM   1336 C CB  . PHE B 1 78 ? 9.315   -13.425 -27.783 1.00 32.26  ? 77  PHE B CB  1 
ATOM   1337 C CG  . PHE B 1 78 ? 9.555   -14.198 -29.076 1.00 31.48  ? 77  PHE B CG  1 
ATOM   1338 C CD1 . PHE B 1 78 ? 10.671  -15.013 -29.194 1.00 30.44  ? 77  PHE B CD1 1 
ATOM   1339 C CD2 . PHE B 1 78 ? 8.639   -14.118 -30.121 1.00 35.99  ? 77  PHE B CD2 1 
ATOM   1340 C CE1 . PHE B 1 78 ? 10.889  -15.717 -30.375 1.00 31.88  ? 77  PHE B CE1 1 
ATOM   1341 C CE2 . PHE B 1 78 ? 8.865   -14.827 -31.299 1.00 33.12  ? 77  PHE B CE2 1 
ATOM   1342 C CZ  . PHE B 1 78 ? 9.990   -15.626 -31.397 1.00 31.23  ? 77  PHE B CZ  1 
ATOM   1343 N N   . ASN B 1 79 ? 8.070   -10.606 -28.388 1.00 28.16  ? 78  ASN B N   1 
ATOM   1344 C CA  . ASN B 1 79 ? 7.346   -9.755  -29.318 1.00 32.14  ? 78  ASN B CA  1 
ATOM   1345 C C   . ASN B 1 79 ? 8.088   -8.430  -29.510 1.00 33.22  ? 78  ASN B C   1 
ATOM   1346 O O   . ASN B 1 79 ? 8.042   -7.840  -30.594 1.00 34.53  ? 78  ASN B O   1 
ATOM   1347 C CB  . ASN B 1 79 ? 5.882   -9.576  -28.935 1.00 35.65  ? 78  ASN B CB  1 
ATOM   1348 C CG  . ASN B 1 79 ? 5.140   -10.898 -28.960 1.00 44.04  ? 78  ASN B CG  1 
ATOM   1349 O OD1 . ASN B 1 79 ? 5.635   -11.890 -29.506 1.00 45.65  ? 78  ASN B OD1 1 
ATOM   1350 N ND2 . ASN B 1 79 ? 3.983   -10.957 -28.322 1.00 45.55  ? 78  ASN B ND2 1 
ATOM   1351 N N   . GLU B 1 80 ? 8.765   -7.975  -28.466 1.00 30.82  ? 79  GLU B N   1 
ATOM   1352 C CA  . GLU B 1 80 ? 9.546   -6.755  -28.594 1.00 33.37  ? 79  GLU B CA  1 
ATOM   1353 C C   . GLU B 1 80 ? 10.704  -7.024  -29.551 1.00 27.24  ? 79  GLU B C   1 
ATOM   1354 O O   . GLU B 1 80 ? 11.014  -6.155  -30.363 1.00 30.11  ? 79  GLU B O   1 
ATOM   1355 C CB  . GLU B 1 80 ? 10.141  -6.170  -27.320 1.00 33.53  ? 79  GLU B CB  1 
ATOM   1356 C CG  . GLU B 1 80 ? 9.234   -5.136  -26.673 1.00 45.41  ? 79  GLU B CG  1 
ATOM   1357 N N   . GLY B 1 81 ? 11.316  -8.216  -29.415 1.00 26.94  ? 80  GLY B N   1 
ATOM   1358 C CA  . GLY B 1 81 ? 12.429  -8.656  -30.259 1.00 27.34  ? 80  GLY B CA  1 
ATOM   1359 C C   . GLY B 1 81 ? 12.001  -8.728  -31.720 1.00 29.29  ? 80  GLY B C   1 
ATOM   1360 O O   . GLY B 1 81 ? 12.757  -8.348  -32.611 1.00 28.01  ? 80  GLY B O   1 
ATOM   1361 N N   . LEU B 1 82 ? 10.766  -9.166  -31.953 1.00 25.37  ? 81  LEU B N   1 
ATOM   1362 C CA  . LEU B 1 82 ? 10.256  -9.238  -33.319 1.00 29.44  ? 81  LEU B CA  1 
ATOM   1363 C C   . LEU B 1 82 ? 10.088  -7.823  -33.872 1.00 33.43  ? 81  LEU B C   1 
ATOM   1364 O O   . LEU B 1 82 ? 10.315  -7.594  -35.054 1.00 31.21  ? 81  LEU B O   1 
ATOM   1365 C CB  . LEU B 1 82 ? 8.926   -10.019 -33.355 1.00 28.68  ? 81  LEU B CB  1 
ATOM   1366 C CG  . LEU B 1 82 ? 8.987   -11.542 -33.147 1.00 29.15  ? 81  LEU B CG  1 
ATOM   1367 C CD1 . LEU B 1 82 ? 7.579   -12.133 -33.191 1.00 30.72  ? 81  LEU B CD1 1 
ATOM   1368 C CD2 . LEU B 1 82 ? 9.925   -12.248 -34.146 1.00 28.36  ? 81  LEU B CD2 1 
ATOM   1369 N N   . TRP B 1 83 ? 9.672   -6.870  -33.031 1.00 31.44  ? 82  TRP B N   1 
ATOM   1370 C CA  . TRP B 1 83 ? 9.530   -5.495  -33.479 1.00 31.73  ? 82  TRP B CA  1 
ATOM   1371 C C   . TRP B 1 83 ? 10.896  -4.933  -33.885 1.00 31.53  ? 82  TRP B C   1 
ATOM   1372 O O   . TRP B 1 83 ? 10.983  -4.275  -34.917 1.00 31.63  ? 82  TRP B O   1 
ATOM   1373 C CB  . TRP B 1 83 ? 8.899   -4.604  -32.401 1.00 32.64  ? 82  TRP B CB  1 
ATOM   1374 C CG  . TRP B 1 83 ? 8.600   -3.217  -32.912 1.00 33.86  ? 82  TRP B CG  1 
ATOM   1375 C CD1 . TRP B 1 83 ? 7.449   -2.792  -33.508 1.00 35.64  ? 82  TRP B CD1 1 
ATOM   1376 C CD2 . TRP B 1 83 ? 9.519   -2.103  -32.952 1.00 33.35  ? 82  TRP B CD2 1 
ATOM   1377 N NE1 . TRP B 1 83 ? 7.571   -1.476  -33.869 1.00 36.44  ? 82  TRP B NE1 1 
ATOM   1378 C CE2 . TRP B 1 83 ? 8.830   -1.030  -33.557 1.00 36.71  ? 82  TRP B CE2 1 
ATOM   1379 C CE3 . TRP B 1 83 ? 10.843  -1.905  -32.519 1.00 37.09  ? 82  TRP B CE3 1 
ATOM   1380 C CZ2 . TRP B 1 83 ? 9.431   0.219   -33.741 1.00 40.97  ? 82  TRP B CZ2 1 
ATOM   1381 C CZ3 . TRP B 1 83 ? 11.435  -0.668  -32.688 1.00 40.13  ? 82  TRP B CZ3 1 
ATOM   1382 C CH2 . TRP B 1 83 ? 10.737  0.366   -33.311 1.00 39.77  ? 82  TRP B CH2 1 
ATOM   1383 N N   . GLU B 1 84 ? 11.929  -5.254  -33.098 1.00 26.55  ? 83  GLU B N   1 
ATOM   1384 C CA  . GLU B 1 84 ? 13.268  -4.692  -33.268 1.00 29.08  ? 83  GLU B CA  1 
ATOM   1385 C C   . GLU B 1 84 ? 13.902  -5.201  -34.560 1.00 32.00  ? 83  GLU B C   1 
ATOM   1386 O O   . GLU B 1 84 ? 14.561  -4.434  -35.287 1.00 31.14  ? 83  GLU B O   1 
ATOM   1387 C CB  . GLU B 1 84 ? 14.184  -5.015  -32.098 1.00 27.75  ? 83  GLU B CB  1 
ATOM   1388 C CG  . GLU B 1 84 ? 13.726  -4.230  -30.868 1.00 34.25  ? 83  GLU B CG  1 
ATOM   1389 C CD  . GLU B 1 84 ? 14.481  -4.573  -29.634 1.00 32.42  ? 83  GLU B CD  1 
ATOM   1390 O OE1 . GLU B 1 84 ? 15.441  -5.393  -29.674 1.00 31.07  ? 83  GLU B OE1 1 
ATOM   1391 O OE2 . GLU B 1 84 ? 14.107  -3.960  -28.582 1.00 34.03  ? 83  GLU B OE2 1 
ATOM   1392 N N   . ILE B 1 85 ? 13.754  -6.512  -34.813 1.00 30.95  ? 84  ILE B N   1 
ATOM   1393 C CA  . ILE B 1 85 ? 14.464  -7.106  -35.945 1.00 28.32  ? 84  ILE B CA  1 
ATOM   1394 C C   . ILE B 1 85 ? 13.850  -6.584  -37.252 1.00 29.89  ? 84  ILE B C   1 
ATOM   1395 O O   . ILE B 1 85 ? 14.540  -6.473  -38.279 1.00 28.64  ? 84  ILE B O   1 
ATOM   1396 C CB  . ILE B 1 85 ? 14.536  -8.649  -35.851 1.00 28.57  ? 84  ILE B CB  1 
ATOM   1397 C CG1 . ILE B 1 85 ? 15.580  -9.231  -36.836 1.00 29.12  ? 84  ILE B CG1 1 
ATOM   1398 C CG2 . ILE B 1 85 ? 13.161  -9.276  -36.062 1.00 28.34  ? 84  ILE B CG2 1 
ATOM   1399 C CD1 . ILE B 1 85 ? 16.095  -10.617 -36.469 1.00 28.40  ? 84  ILE B CD1 1 
ATOM   1400 N N   . GLN B 1 86 ? 12.563  -6.211  -37.194 1.00 30.41  ? 85  GLN B N   1 
ATOM   1401 C CA  . GLN B 1 86 ? 11.808  -5.733  -38.347 1.00 32.67  ? 85  GLN B CA  1 
ATOM   1402 C C   . GLN B 1 86 ? 12.007  -4.219  -38.539 1.00 36.67  ? 85  GLN B C   1 
ATOM   1403 O O   . GLN B 1 86 ? 12.179  -3.760  -39.670 1.00 37.00  ? 85  GLN B O   1 
ATOM   1404 C CB  . GLN B 1 86 ? 10.334  -6.140  -38.265 1.00 36.12  ? 85  GLN B CB  1 
ATOM   1405 N N   . ASN B 1 87 ? 12.050  -3.444  -37.445 1.00 33.65  ? 86  ASN B N   1 
ATOM   1406 C CA  . ASN B 1 87 ? 11.912  -1.988  -37.549 1.00 33.62  ? 86  ASN B CA  1 
ATOM   1407 C C   . ASN B 1 87 ? 13.224  -1.243  -37.308 1.00 33.19  ? 86  ASN B C   1 
ATOM   1408 O O   . ASN B 1 87 ? 13.350  -0.086  -37.727 1.00 35.19  ? 86  ASN B O   1 
ATOM   1409 C CB  . ASN B 1 87 ? 10.768  -1.502  -36.656 1.00 41.20  ? 86  ASN B CB  1 
ATOM   1410 C CG  . ASN B 1 87 ? 9.453   -2.036  -37.167 1.00 41.61  ? 86  ASN B CG  1 
ATOM   1411 O OD1 . ASN B 1 87 ? 8.923   -1.495  -38.136 1.00 45.09  ? 86  ASN B OD1 1 
ATOM   1412 N ND2 . ASN B 1 87 ? 8.925   -3.104  -36.583 1.00 37.33  ? 86  ASN B ND2 1 
ATOM   1413 N N   . ASN B 1 88 ? 14.184  -1.836  -36.587 1.00 31.23  ? 87  ASN B N   1 
ATOM   1414 C CA  . ASN B 1 88 ? 15.436  -1.148  -36.325 1.00 30.34  ? 87  ASN B CA  1 
ATOM   1415 C C   . ASN B 1 88 ? 16.492  -2.148  -35.888 1.00 29.80  ? 87  ASN B C   1 
ATOM   1416 O O   . ASN B 1 88 ? 17.050  -2.048  -34.791 1.00 28.55  ? 87  ASN B O   1 
ATOM   1417 C CB  . ASN B 1 88 ? 15.276  0.014   -35.335 1.00 33.88  ? 87  ASN B CB  1 
ATOM   1418 C CG  . ASN B 1 88 ? 16.333  1.092   -35.480 1.00 37.03  ? 87  ASN B CG  1 
ATOM   1419 O OD1 . ASN B 1 88 ? 17.413  0.901   -36.066 1.00 32.45  ? 87  ASN B OD1 1 
ATOM   1420 N ND2 . ASN B 1 88 ? 16.047  2.253   -34.904 1.00 32.64  ? 87  ASN B ND2 1 
ATOM   1421 N N   . PRO B 1 89 ? 16.811  -3.129  -36.763 1.00 28.86  ? 88  PRO B N   1 
ATOM   1422 C CA  . PRO B 1 89 ? 17.746  -4.195  -36.407 1.00 27.53  ? 88  PRO B CA  1 
ATOM   1423 C C   . PRO B 1 89 ? 19.182  -3.777  -36.122 1.00 25.87  ? 88  PRO B C   1 
ATOM   1424 O O   . PRO B 1 89 ? 19.932  -4.502  -35.467 1.00 29.72  ? 88  PRO B O   1 
ATOM   1425 C CB  . PRO B 1 89 ? 17.674  -5.114  -37.661 1.00 26.00  ? 88  PRO B CB  1 
ATOM   1426 C CG  . PRO B 1 89 ? 17.343  -4.170  -38.802 1.00 28.25  ? 88  PRO B CG  1 
ATOM   1427 C CD  . PRO B 1 89 ? 16.326  -3.219  -38.160 1.00 27.07  ? 88  PRO B CD  1 
ATOM   1428 N N   . HIS B 1 90 ? 19.576  -2.574  -36.612 1.00 27.53  ? 89  HIS B N   1 
ATOM   1429 C CA  . HIS B 1 90 ? 20.966  -2.184  -36.504 1.00 25.97  ? 89  HIS B CA  1 
ATOM   1430 C C   . HIS B 1 90 ? 21.208  -1.089  -35.460 1.00 30.35  ? 89  HIS B C   1 
ATOM   1431 O O   . HIS B 1 90 ? 22.348  -0.622  -35.334 1.00 31.44  ? 89  HIS B O   1 
ATOM   1432 C CB  . HIS B 1 90 ? 21.500  -1.801  -37.901 1.00 26.70  ? 89  HIS B CB  1 
ATOM   1433 C CG  . HIS B 1 90 ? 21.300  -2.871  -38.924 1.00 30.89  ? 89  HIS B CG  1 
ATOM   1434 N ND1 . HIS B 1 90 ? 21.913  -4.096  -38.766 1.00 30.04  ? 89  HIS B ND1 1 
ATOM   1435 C CD2 . HIS B 1 90 ? 20.674  -2.914  -40.127 1.00 28.28  ? 89  HIS B CD2 1 
ATOM   1436 C CE1 . HIS B 1 90 ? 21.594  -4.871  -39.805 1.00 28.04  ? 89  HIS B CE1 1 
ATOM   1437 N NE2 . HIS B 1 90 ? 20.873  -4.169  -40.632 1.00 29.22  ? 89  HIS B NE2 1 
ATOM   1438 N N   . ALA B 1 91 ? 20.197  -0.804  -34.628 1.00 28.94  ? 90  ALA B N   1 
ATOM   1439 C CA  . ALA B 1 91 ? 20.283  0.234   -33.601 1.00 31.04  ? 90  ALA B CA  1 
ATOM   1440 C C   . ALA B 1 91 ? 21.168  -0.188  -32.433 1.00 36.78  ? 90  ALA B C   1 
ATOM   1441 O O   . ALA B 1 91 ? 21.448  -1.367  -32.230 1.00 31.25  ? 90  ALA B O   1 
ATOM   1442 C CB  . ALA B 1 91 ? 18.884  0.612   -33.133 1.00 29.91  ? 90  ALA B CB  1 
ATOM   1443 N N   . SER B 1 92 ? 21.584  0.806   -31.631 1.00 35.49  ? 91  SER B N   1 
ATOM   1444 C CA  . SER B 1 92 ? 22.243  0.569   -30.361 1.00 38.03  ? 91  SER B CA  1 
ATOM   1445 C C   . SER B 1 92 ? 21.166  0.259   -29.313 1.00 41.56  ? 91  SER B C   1 
ATOM   1446 O O   . SER B 1 92 ? 20.184  0.990   -29.197 1.00 46.10  ? 91  SER B O   1 
ATOM   1447 C CB  . SER B 1 92 ? 23.107  1.784   -30.001 1.00 39.54  ? 91  SER B CB  1 
ATOM   1448 O OG  . SER B 1 92 ? 23.734  1.571   -28.744 1.00 54.49  ? 91  SER B OG  1 
ATOM   1449 N N   . TYR B 1 93 ? 21.305  -0.896  -28.652 1.00 38.23  ? 92  TYR B N   1 
ATOM   1450 C CA  . TYR B 1 93 ? 20.416  -1.387  -27.613 1.00 41.40  ? 92  TYR B CA  1 
ATOM   1451 C C   . TYR B 1 93 ? 21.211  -1.549  -26.318 1.00 47.83  ? 92  TYR B C   1 
ATOM   1452 O O   . TYR B 1 93 ? 20.817  -2.316  -25.448 1.00 53.90  ? 92  TYR B O   1 
ATOM   1453 C CB  . TYR B 1 93 ? 19.759  -2.703  -28.045 1.00 35.60  ? 92  TYR B CB  1 
ATOM   1454 C CG  . TYR B 1 93 ? 18.773  -2.514  -29.185 1.00 36.69  ? 92  TYR B CG  1 
ATOM   1455 C CD1 . TYR B 1 93 ? 17.494  -2.015  -28.949 1.00 32.23  ? 92  TYR B CD1 1 
ATOM   1456 C CD2 . TYR B 1 93 ? 19.098  -2.853  -30.501 1.00 32.27  ? 92  TYR B CD2 1 
ATOM   1457 C CE1 . TYR B 1 93 ? 16.591  -1.803  -29.973 1.00 33.41  ? 92  TYR B CE1 1 
ATOM   1458 C CE2 . TYR B 1 93 ? 18.171  -2.692  -31.526 1.00 32.01  ? 92  TYR B CE2 1 
ATOM   1459 C CZ  . TYR B 1 93 ? 16.927  -2.154  -31.274 1.00 33.65  ? 92  TYR B CZ  1 
ATOM   1460 O OH  . TYR B 1 93 ? 15.988  -1.964  -32.245 1.00 29.94  ? 92  TYR B OH  1 
ATOM   1461 N N   . SER B 1 94 ? 22.317  -0.800  -26.216 1.00 59.43  ? 93  SER B N   1 
ATOM   1462 C CA  . SER B 1 94 ? 23.267  -0.878  -25.114 1.00 67.17  ? 93  SER B CA  1 
ATOM   1463 C C   . SER B 1 94 ? 22.660  -0.260  -23.845 1.00 78.33  ? 93  SER B C   1 
ATOM   1464 O O   . SER B 1 94 ? 21.528  0.294   -23.942 1.00 78.25  ? 93  SER B O   1 
ATOM   1465 C CB  . SER B 1 94 ? 24.563  -0.172  -25.448 1.00 72.64  ? 93  SER B CB  1 
ATOM   1466 O OG  . SER B 1 94 ? 24.986  -0.389  -26.786 1.00 76.81  ? 93  SER B OG  1 
ATOM   1467 O OXT . SER B 1 94 ? 23.357  -0.326  -22.805 1.00 79.09  ? 93  SER B OXT 1 
ATOM   1468 N N   . ALA C 1 5  ? 29.372  -22.583 29.280  1.00 70.87  ? 4   ALA C N   1 
ATOM   1469 C CA  . ALA C 1 5  ? 28.431  -23.191 30.253  1.00 66.58  ? 4   ALA C CA  1 
ATOM   1470 C C   . ALA C 1 5  ? 26.987  -22.830 29.918  1.00 66.21  ? 4   ALA C C   1 
ATOM   1471 O O   . ALA C 1 5  ? 26.707  -21.784 29.329  1.00 65.42  ? 4   ALA C O   1 
ATOM   1472 C CB  . ALA C 1 5  ? 28.763  -22.727 31.639  1.00 69.69  ? 4   ALA C CB  1 
ATOM   1473 N N   . PHE C 1 6  ? 26.071  -23.684 30.384  1.00 48.48  ? 5   PHE C N   1 
ATOM   1474 C CA  . PHE C 1 6  ? 24.703  -23.666 29.907  1.00 49.98  ? 5   PHE C CA  1 
ATOM   1475 C C   . PHE C 1 6  ? 23.763  -23.732 31.107  1.00 54.68  ? 5   PHE C C   1 
ATOM   1476 O O   . PHE C 1 6  ? 24.073  -24.388 32.095  1.00 64.84  ? 5   PHE C O   1 
ATOM   1477 C CB  . PHE C 1 6  ? 24.645  -24.913 29.006  1.00 48.02  ? 5   PHE C CB  1 
ATOM   1478 C CG  . PHE C 1 6  ? 25.550  -24.928 27.773  1.00 47.51  ? 5   PHE C CG  1 
ATOM   1479 C CD1 . PHE C 1 6  ? 26.644  -25.783 27.686  1.00 46.94  ? 5   PHE C CD1 1 
ATOM   1480 C CD2 . PHE C 1 6  ? 25.300  -24.081 26.690  1.00 52.69  ? 5   PHE C CD2 1 
ATOM   1481 C CE1 . PHE C 1 6  ? 27.462  -25.779 26.565  1.00 48.64  ? 5   PHE C CE1 1 
ATOM   1482 C CE2 . PHE C 1 6  ? 26.123  -24.086 25.566  1.00 49.53  ? 5   PHE C CE2 1 
ATOM   1483 C CZ  . PHE C 1 6  ? 27.187  -24.948 25.497  1.00 49.87  ? 5   PHE C CZ  1 
ATOM   1484 N N   . LYS C 1 7  ? 22.607  -23.069 31.025  1.00 50.43  ? 6   LYS C N   1 
ATOM   1485 C CA  . LYS C 1 7  ? 21.610  -23.218 32.073  1.00 50.37  ? 6   LYS C CA  1 
ATOM   1486 C C   . LYS C 1 7  ? 20.292  -23.624 31.425  1.00 51.12  ? 6   LYS C C   1 
ATOM   1487 O O   . LYS C 1 7  ? 20.092  -23.392 30.223  1.00 49.52  ? 6   LYS C O   1 
ATOM   1488 C CB  . LYS C 1 7  ? 21.496  -21.934 32.909  1.00 58.49  ? 6   LYS C CB  1 
ATOM   1489 N N   . PRO C 1 8  ? 19.339  -24.234 32.169  1.00 47.14  ? 7   PRO C N   1 
ATOM   1490 C CA  . PRO C 1 8  ? 18.076  -24.641 31.550  1.00 47.94  ? 7   PRO C CA  1 
ATOM   1491 C C   . PRO C 1 8  ? 17.504  -23.454 30.775  1.00 53.72  ? 7   PRO C C   1 
ATOM   1492 O O   . PRO C 1 8  ? 17.525  -22.322 31.264  1.00 58.99  ? 7   PRO C O   1 
ATOM   1493 C CB  . PRO C 1 8  ? 17.204  -25.085 32.755  1.00 52.31  ? 7   PRO C CB  1 
ATOM   1494 C CG  . PRO C 1 8  ? 18.231  -25.514 33.790  1.00 50.03  ? 7   PRO C CG  1 
ATOM   1495 C CD  . PRO C 1 8  ? 19.406  -24.549 33.613  1.00 45.48  ? 7   PRO C CD  1 
ATOM   1496 N N   . GLY C 1 9  ? 17.030  -23.716 29.549  1.00 57.48  ? 8   GLY C N   1 
ATOM   1497 C CA  . GLY C 1 9  ? 16.413  -22.688 28.728  1.00 51.89  ? 8   GLY C CA  1 
ATOM   1498 C C   . GLY C 1 9  ? 17.354  -22.096 27.671  1.00 53.80  ? 8   GLY C C   1 
ATOM   1499 O O   . GLY C 1 9  ? 16.869  -21.502 26.713  1.00 52.64  ? 8   GLY C O   1 
ATOM   1500 N N   . ASP C 1 10 ? 18.679  -22.238 27.842  1.00 46.44  ? 9   ASP C N   1 
ATOM   1501 C CA  . ASP C 1 10 ? 19.670  -21.790 26.870  1.00 42.49  ? 9   ASP C CA  1 
ATOM   1502 C C   . ASP C 1 10 ? 19.528  -22.538 25.537  1.00 44.47  ? 9   ASP C C   1 
ATOM   1503 O O   . ASP C 1 10 ? 19.295  -23.738 25.513  1.00 41.30  ? 9   ASP C O   1 
ATOM   1504 C CB  . ASP C 1 10 ? 21.091  -22.044 27.333  1.00 45.61  ? 9   ASP C CB  1 
ATOM   1505 C CG  . ASP C 1 10 ? 21.666  -21.043 28.331  1.00 59.29  ? 9   ASP C CG  1 
ATOM   1506 O OD1 . ASP C 1 10 ? 20.904  -20.143 28.779  1.00 62.35  ? 9   ASP C OD1 1 
ATOM   1507 O OD2 . ASP C 1 10 ? 22.873  -21.166 28.648  1.00 56.59  ? 9   ASP C OD2 1 
ATOM   1508 N N   . LEU C 1 11 ? 19.680  -21.810 24.418  1.00 41.64  ? 10  LEU C N   1 
ATOM   1509 C CA  . LEU C 1 11 ? 19.368  -22.338 23.093  1.00 39.90  ? 10  LEU C CA  1 
ATOM   1510 C C   . LEU C 1 11 ? 20.657  -22.783 22.405  1.00 34.78  ? 10  LEU C C   1 
ATOM   1511 O O   . LEU C 1 11 ? 21.657  -22.075 22.430  1.00 33.87  ? 10  LEU C O   1 
ATOM   1512 C CB  . LEU C 1 11 ? 18.587  -21.295 22.280  1.00 35.80  ? 10  LEU C CB  1 
ATOM   1513 C CG  . LEU C 1 11 ? 17.262  -20.822 22.886  1.00 34.85  ? 10  LEU C CG  1 
ATOM   1514 C CD1 . LEU C 1 11 ? 16.576  -19.794 21.971  1.00 36.79  ? 10  LEU C CD1 1 
ATOM   1515 C CD2 . LEU C 1 11 ? 16.262  -21.961 23.208  1.00 36.64  ? 10  LEU C CD2 1 
ATOM   1516 N N   . VAL C 1 12 ? 20.620  -23.966 21.759  1.00 32.24  ? 11  VAL C N   1 
ATOM   1517 C CA  . VAL C 1 12 ? 21.798  -24.599 21.208  1.00 30.58  ? 11  VAL C CA  1 
ATOM   1518 C C   . VAL C 1 12 ? 21.423  -25.366 19.923  1.00 28.57  ? 11  VAL C C   1 
ATOM   1519 O O   . VAL C 1 12 ? 20.235  -25.620 19.673  1.00 27.38  ? 11  VAL C O   1 
ATOM   1520 C CB  . VAL C 1 12 ? 22.461  -25.566 22.223  1.00 34.44  ? 11  VAL C CB  1 
ATOM   1521 C CG1 . VAL C 1 12 ? 22.833  -24.877 23.546  1.00 34.87  ? 11  VAL C CG1 1 
ATOM   1522 C CG2 . VAL C 1 12 ? 21.607  -26.806 22.503  1.00 33.50  ? 11  VAL C CG2 1 
ATOM   1523 N N   . PHE C 1 13 ? 22.465  -25.754 19.172  1.00 31.86  ? 12  PHE C N   1 
ATOM   1524 C CA  . PHE C 1 13 ? 22.466  -26.911 18.278  1.00 27.49  ? 12  PHE C CA  1 
ATOM   1525 C C   . PHE C 1 13 ? 23.156  -28.073 18.994  1.00 29.46  ? 12  PHE C C   1 
ATOM   1526 O O   . PHE C 1 13 ? 24.253  -27.921 19.549  1.00 34.37  ? 12  PHE C O   1 
ATOM   1527 C CB  . PHE C 1 13 ? 23.102  -26.710 16.890  1.00 33.47  ? 12  PHE C CB  1 
ATOM   1528 C CG  . PHE C 1 13 ? 22.318  -25.703 16.067  1.00 33.02  ? 12  PHE C CG  1 
ATOM   1529 C CD1 . PHE C 1 13 ? 21.263  -26.114 15.251  1.00 34.24  ? 12  PHE C CD1 1 
ATOM   1530 C CD2 . PHE C 1 13 ? 22.600  -24.337 16.158  1.00 36.17  ? 12  PHE C CD2 1 
ATOM   1531 C CE1 . PHE C 1 13 ? 20.518  -25.185 14.532  1.00 33.99  ? 12  PHE C CE1 1 
ATOM   1532 C CE2 . PHE C 1 13 ? 21.849  -23.414 15.438  1.00 36.83  ? 12  PHE C CE2 1 
ATOM   1533 C CZ  . PHE C 1 13 ? 20.814  -23.844 14.631  1.00 36.27  ? 12  PHE C CZ  1 
ATOM   1534 N N   . ALA C 1 14 ? 22.471  -29.229 19.006  1.00 30.69  ? 13  ALA C N   1 
ATOM   1535 C CA  . ALA C 1 14 ? 22.959  -30.402 19.709  1.00 29.17  ? 13  ALA C CA  1 
ATOM   1536 C C   . ALA C 1 14 ? 23.255  -31.515 18.711  1.00 31.60  ? 13  ALA C C   1 
ATOM   1537 O O   . ALA C 1 14 ? 22.397  -31.868 17.897  1.00 28.75  ? 13  ALA C O   1 
ATOM   1538 C CB  . ALA C 1 14 ? 21.941  -30.835 20.735  1.00 29.88  ? 13  ALA C CB  1 
ATOM   1539 N N   . LYS C 1 15 ? 24.457  -32.104 18.825  1.00 29.68  ? 14  LYS C N   1 
ATOM   1540 C CA  . LYS C 1 15 ? 24.891  -33.120 17.870  1.00 30.79  ? 14  LYS C CA  1 
ATOM   1541 C C   . LYS C 1 15 ? 24.885  -34.492 18.532  1.00 30.81  ? 14  LYS C C   1 
ATOM   1542 O O   . LYS C 1 15 ? 25.622  -34.721 19.492  1.00 33.36  ? 14  LYS C O   1 
ATOM   1543 C CB  . LYS C 1 15 ? 26.339  -32.921 17.396  1.00 31.35  ? 14  LYS C CB  1 
ATOM   1544 C CG  . LYS C 1 15 ? 26.714  -33.898 16.265  1.00 31.61  ? 14  LYS C CG  1 
ATOM   1545 C CD  . LYS C 1 15 ? 25.897  -33.790 14.970  1.00 29.55  ? 14  LYS C CD  1 
ATOM   1546 C CE  . LYS C 1 15 ? 26.459  -34.674 13.820  1.00 30.32  ? 14  LYS C CE  1 
ATOM   1547 N NZ  . LYS C 1 15 ? 26.181  -36.096 14.104  1.00 29.98  ? 14  LYS C NZ  1 
ATOM   1548 N N   . MET C 1 16 ? 24.098  -35.410 17.969  1.00 28.49  ? 15  MET C N   1 
ATOM   1549 C CA  . MET C 1 16 ? 24.096  -36.834 18.303  1.00 29.98  ? 15  MET C CA  1 
ATOM   1550 C C   . MET C 1 16 ? 24.594  -37.650 17.110  1.00 34.76  ? 15  MET C C   1 
ATOM   1551 O O   . MET C 1 16 ? 24.358  -37.293 15.959  1.00 28.71  ? 15  MET C O   1 
ATOM   1552 C CB  . MET C 1 16 ? 22.679  -37.326 18.637  1.00 29.71  ? 15  MET C CB  1 
ATOM   1553 C CG  . MET C 1 16 ? 22.071  -36.755 19.926  1.00 34.29  ? 15  MET C CG  1 
ATOM   1554 S SD  . MET C 1 16 ? 20.468  -37.511 20.257  1.00 40.87  ? 15  MET C SD  1 
ATOM   1555 C CE  . MET C 1 16 ? 19.512  -36.843 18.880  1.00 37.86  ? 15  MET C CE  1 
ATOM   1556 N N   . LYS C 1 17 ? 25.244  -38.785 17.389  1.00 33.50  ? 16  LYS C N   1 
ATOM   1557 C CA  . LYS C 1 17 ? 25.659  -39.666 16.300  1.00 35.25  ? 16  LYS C CA  1 
ATOM   1558 C C   . LYS C 1 17 ? 24.412  -40.094 15.534  1.00 28.03  ? 16  LYS C C   1 
ATOM   1559 O O   . LYS C 1 17 ? 23.423  -40.544 16.125  1.00 32.42  ? 16  LYS C O   1 
ATOM   1560 C CB  . LYS C 1 17 ? 26.358  -40.920 16.860  1.00 36.66  ? 16  LYS C CB  1 
ATOM   1561 C CG  . LYS C 1 17 ? 27.053  -41.818 15.837  1.00 40.19  ? 16  LYS C CG  1 
ATOM   1562 C CD  . LYS C 1 17 ? 28.310  -41.151 15.297  1.00 43.71  ? 16  LYS C CD  1 
ATOM   1563 C CE  . LYS C 1 17 ? 28.916  -41.998 14.226  1.00 51.49  ? 16  LYS C CE  1 
ATOM   1564 N NZ  . LYS C 1 17 ? 30.173  -41.386 13.797  1.00 47.42  ? 16  LYS C NZ  1 
ATOM   1565 N N   . GLY C 1 18 ? 24.485  -39.970 14.207  1.00 33.65  ? 17  GLY C N   1 
ATOM   1566 C CA  . GLY C 1 18 ? 23.390  -40.445 13.373  1.00 30.75  ? 17  GLY C CA  1 
ATOM   1567 C C   . GLY C 1 18 ? 22.413  -39.328 12.992  1.00 35.63  ? 17  GLY C C   1 
ATOM   1568 O O   . GLY C 1 18 ? 21.415  -39.609 12.327  1.00 33.28  ? 17  GLY C O   1 
ATOM   1569 N N   . TYR C 1 19 ? 22.677  -38.088 13.433  1.00 33.05  ? 18  TYR C N   1 
ATOM   1570 C CA  . TYR C 1 19 ? 21.718  -36.995 13.229  1.00 32.09  ? 18  TYR C CA  1 
ATOM   1571 C C   . TYR C 1 19 ? 22.477  -35.722 12.910  1.00 32.65  ? 18  TYR C C   1 
ATOM   1572 O O   . TYR C 1 19 ? 23.591  -35.533 13.394  1.00 33.02  ? 18  TYR C O   1 
ATOM   1573 C CB  . TYR C 1 19 ? 20.927  -36.722 14.519  1.00 29.63  ? 18  TYR C CB  1 
ATOM   1574 C CG  . TYR C 1 19 ? 20.086  -37.912 14.933  1.00 30.16  ? 18  TYR C CG  1 
ATOM   1575 C CD1 . TYR C 1 19 ? 20.612  -38.921 15.745  1.00 32.19  ? 18  TYR C CD1 1 
ATOM   1576 C CD2 . TYR C 1 19 ? 18.792  -38.060 14.439  1.00 33.94  ? 18  TYR C CD2 1 
ATOM   1577 C CE1 . TYR C 1 19 ? 19.847  -40.024 16.080  1.00 34.80  ? 18  TYR C CE1 1 
ATOM   1578 C CE2 . TYR C 1 19 ? 18.019  -39.151 14.792  1.00 40.60  ? 18  TYR C CE2 1 
ATOM   1579 C CZ  . TYR C 1 19 ? 18.557  -40.137 15.600  1.00 38.22  ? 18  TYR C CZ  1 
ATOM   1580 O OH  . TYR C 1 19 ? 17.765  -41.208 15.913  1.00 45.58  ? 18  TYR C OH  1 
ATOM   1581 N N   . PRO C 1 20 ? 21.904  -34.809 12.090  1.00 29.26  ? 19  PRO C N   1 
ATOM   1582 C CA  . PRO C 1 20 ? 22.510  -33.499 11.880  1.00 29.70  ? 19  PRO C CA  1 
ATOM   1583 C C   . PRO C 1 20 ? 22.464  -32.695 13.183  1.00 26.40  ? 19  PRO C C   1 
ATOM   1584 O O   . PRO C 1 20 ? 21.703  -33.016 14.097  1.00 27.58  ? 19  PRO C O   1 
ATOM   1585 C CB  . PRO C 1 20 ? 21.595  -32.886 10.792  1.00 31.46  ? 19  PRO C CB  1 
ATOM   1586 C CG  . PRO C 1 20 ? 20.246  -33.540 11.036  1.00 30.76  ? 19  PRO C CG  1 
ATOM   1587 C CD  . PRO C 1 20 ? 20.598  -34.972 11.416  1.00 31.20  ? 19  PRO C CD  1 
ATOM   1588 N N   . HIS C 1 21 ? 23.292  -31.652 13.239  1.00 27.42  ? 20  HIS C N   1 
ATOM   1589 C CA  . HIS C 1 21 ? 23.254  -30.727 14.361  1.00 27.49  ? 20  HIS C CA  1 
ATOM   1590 C C   . HIS C 1 21 ? 21.833  -30.175 14.498  1.00 28.39  ? 20  HIS C C   1 
ATOM   1591 O O   . HIS C 1 21 ? 21.260  -29.684 13.523  1.00 30.79  ? 20  HIS C O   1 
ATOM   1592 C CB  . HIS C 1 21 ? 24.243  -29.581 14.159  1.00 28.03  ? 20  HIS C CB  1 
ATOM   1593 C CG  . HIS C 1 21 ? 25.666  -30.042 14.208  1.00 31.07  ? 20  HIS C CG  1 
ATOM   1594 N ND1 . HIS C 1 21 ? 26.315  -30.670 13.168  1.00 35.32  ? 20  HIS C ND1 1 
ATOM   1595 C CD2 . HIS C 1 21 ? 26.581  -29.900 15.192  1.00 33.90  ? 20  HIS C CD2 1 
ATOM   1596 C CE1 . HIS C 1 21 ? 27.579  -30.909 13.521  1.00 35.99  ? 20  HIS C CE1 1 
ATOM   1597 N NE2 . HIS C 1 21 ? 27.767  -30.438 14.735  1.00 35.57  ? 20  HIS C NE2 1 
ATOM   1598 N N   . TRP C 1 22 ? 21.257  -30.329 15.693  1.00 26.24  ? 21  TRP C N   1 
ATOM   1599 C CA  . TRP C 1 22 ? 19.807  -30.212 15.806  1.00 24.68  ? 21  TRP C CA  1 
ATOM   1600 C C   . TRP C 1 22 ? 19.425  -29.050 16.713  1.00 26.27  ? 21  TRP C C   1 
ATOM   1601 O O   . TRP C 1 22 ? 19.944  -28.945 17.830  1.00 27.42  ? 21  TRP C O   1 
ATOM   1602 C CB  . TRP C 1 22 ? 19.235  -31.525 16.372  1.00 27.27  ? 21  TRP C CB  1 
ATOM   1603 C CG  . TRP C 1 22 ? 17.787  -31.753 16.009  1.00 29.44  ? 21  TRP C CG  1 
ATOM   1604 C CD1 . TRP C 1 22 ? 16.683  -31.180 16.578  1.00 28.59  ? 21  TRP C CD1 1 
ATOM   1605 C CD2 . TRP C 1 22 ? 17.295  -32.675 15.000  1.00 30.29  ? 21  TRP C CD2 1 
ATOM   1606 N NE1 . TRP C 1 22 ? 15.544  -31.661 15.977  1.00 31.79  ? 21  TRP C NE1 1 
ATOM   1607 C CE2 . TRP C 1 22 ? 15.885  -32.576 15.013  1.00 28.42  ? 21  TRP C CE2 1 
ATOM   1608 C CE3 . TRP C 1 22 ? 17.896  -33.566 14.100  1.00 29.28  ? 21  TRP C CE3 1 
ATOM   1609 C CZ2 . TRP C 1 22 ? 15.096  -33.329 14.131  1.00 28.07  ? 21  TRP C CZ2 1 
ATOM   1610 C CZ3 . TRP C 1 22 ? 17.120  -34.312 13.227  1.00 29.68  ? 21  TRP C CZ3 1 
ATOM   1611 C CH2 . TRP C 1 22 ? 15.726  -34.199 13.269  1.00 26.91  ? 21  TRP C CH2 1 
ATOM   1612 N N   . PRO C 1 23 ? 18.408  -28.219 16.356  1.00 28.93  ? 22  PRO C N   1 
ATOM   1613 C CA  . PRO C 1 23 ? 17.980  -27.141 17.248  1.00 28.30  ? 22  PRO C CA  1 
ATOM   1614 C C   . PRO C 1 23 ? 17.389  -27.715 18.532  1.00 25.07  ? 22  PRO C C   1 
ATOM   1615 O O   . PRO C 1 23 ? 16.553  -28.628 18.517  1.00 27.51  ? 22  PRO C O   1 
ATOM   1616 C CB  . PRO C 1 23 ? 16.934  -26.352 16.397  1.00 30.86  ? 22  PRO C CB  1 
ATOM   1617 C CG  . PRO C 1 23 ? 16.392  -27.404 15.443  1.00 28.29  ? 22  PRO C CG  1 
ATOM   1618 C CD  . PRO C 1 23 ? 17.642  -28.249 15.090  1.00 28.89  ? 22  PRO C CD  1 
ATOM   1619 N N   . ALA C 1 24 ? 17.855  -27.171 19.649  1.00 27.04  ? 23  ALA C N   1 
ATOM   1620 C CA  . ALA C 1 24 ? 17.557  -27.716 20.967  1.00 31.27  ? 23  ALA C CA  1 
ATOM   1621 C C   . ALA C 1 24 ? 17.693  -26.636 22.048  1.00 33.09  ? 23  ALA C C   1 
ATOM   1622 O O   . ALA C 1 24 ? 18.181  -25.526 21.816  1.00 30.70  ? 23  ALA C O   1 
ATOM   1623 C CB  . ALA C 1 24 ? 18.512  -28.884 21.241  1.00 29.49  ? 23  ALA C CB  1 
ATOM   1624 N N   . ARG C 1 25 ? 17.316  -27.010 23.273  1.00 32.44  ? 24  ARG C N   1 
ATOM   1625 C CA  . ARG C 1 25 ? 17.652  -26.194 24.432  1.00 34.84  ? 24  ARG C CA  1 
ATOM   1626 C C   . ARG C 1 25 ? 18.086  -27.101 25.586  1.00 39.28  ? 24  ARG C C   1 
ATOM   1627 O O   . ARG C 1 25 ? 17.702  -28.278 25.630  1.00 37.19  ? 24  ARG C O   1 
ATOM   1628 C CB  . ARG C 1 25 ? 16.409  -25.429 24.883  1.00 35.35  ? 24  ARG C CB  1 
ATOM   1629 C CG  . ARG C 1 25 ? 15.163  -26.230 25.215  1.00 42.67  ? 24  ARG C CG  1 
ATOM   1630 C CD  . ARG C 1 25 ? 14.144  -25.306 25.883  1.00 45.51  ? 24  ARG C CD  1 
ATOM   1631 N NE  . ARG C 1 25 ? 12.949  -26.120 26.124  1.00 44.42  ? 24  ARG C NE  1 
ATOM   1632 C CZ  . ARG C 1 25 ? 11.677  -25.870 25.866  1.00 54.39  ? 24  ARG C CZ  1 
ATOM   1633 N NH1 . ARG C 1 25 ? 11.318  -24.773 25.217  1.00 47.62  ? 24  ARG C NH1 1 
ATOM   1634 N NH2 . ARG C 1 25 ? 10.761  -26.747 26.258  1.00 55.88  ? 24  ARG C NH2 1 
ATOM   1635 N N   . ILE C 1 26 ? 18.862  -26.502 26.496  1.00 37.15  ? 25  ILE C N   1 
ATOM   1636 C CA  . ILE C 1 26 ? 19.180  -27.088 27.794  1.00 42.39  ? 25  ILE C CA  1 
ATOM   1637 C C   . ILE C 1 26 ? 17.902  -27.197 28.631  1.00 49.71  ? 25  ILE C C   1 
ATOM   1638 O O   . ILE C 1 26 ? 17.156  -26.232 28.814  1.00 49.04  ? 25  ILE C O   1 
ATOM   1639 C CB  . ILE C 1 26 ? 20.260  -26.267 28.517  1.00 45.10  ? 25  ILE C CB  1 
ATOM   1640 C CG1 . ILE C 1 26 ? 21.387  -25.831 27.619  1.00 41.35  ? 25  ILE C CG1 1 
ATOM   1641 C CG2 . ILE C 1 26 ? 20.788  -26.982 29.762  1.00 50.13  ? 25  ILE C CG2 1 
ATOM   1642 C CD1 . ILE C 1 26 ? 22.333  -26.924 27.136  1.00 39.97  ? 25  ILE C CD1 1 
ATOM   1643 N N   . ASP C 1 27 ? 17.667  -28.387 29.170  1.00 45.25  ? 26  ASP C N   1 
ATOM   1644 C CA  . ASP C 1 27 ? 16.552  -28.603 30.080  1.00 57.01  ? 26  ASP C CA  1 
ATOM   1645 C C   . ASP C 1 27 ? 16.923  -28.256 31.529  1.00 52.29  ? 26  ASP C C   1 
ATOM   1646 O O   . ASP C 1 27 ? 18.109  -28.413 31.877  1.00 53.52  ? 26  ASP C O   1 
ATOM   1647 C CB  . ASP C 1 27 ? 15.973  -29.996 29.928  1.00 57.59  ? 26  ASP C CB  1 
ATOM   1648 C CG  . ASP C 1 27 ? 14.599  -30.014 29.288  1.00 67.12  ? 26  ASP C CG  1 
ATOM   1649 O OD1 . ASP C 1 27 ? 14.260  -28.983 28.673  1.00 70.06  ? 26  ASP C OD1 1 
ATOM   1650 O OD2 . ASP C 1 27 ? 13.873  -31.023 29.477  1.00 58.57  ? 26  ASP C OD2 1 
ATOM   1651 N N   . LYS C 1 35 ? 19.127  -38.136 37.305  1.00 66.32  ? 34  LYS C N   1 
ATOM   1652 C CA  . LYS C 1 35 ? 20.376  -37.323 37.302  1.00 61.42  ? 34  LYS C CA  1 
ATOM   1653 C C   . LYS C 1 35 ? 21.244  -37.758 36.119  1.00 59.20  ? 34  LYS C C   1 
ATOM   1654 O O   . LYS C 1 35 ? 21.359  -38.951 35.836  1.00 62.37  ? 34  LYS C O   1 
ATOM   1655 C CB  . LYS C 1 35 ? 21.100  -37.409 38.654  1.00 63.02  ? 34  LYS C CB  1 
ATOM   1656 N N   . PRO C 1 36 ? 21.893  -36.811 35.399  1.00 54.67  ? 35  PRO C N   1 
ATOM   1657 C CA  . PRO C 1 36 ? 22.621  -37.146 34.173  1.00 57.87  ? 35  PRO C CA  1 
ATOM   1658 C C   . PRO C 1 36 ? 23.785  -38.089 34.480  1.00 56.46  ? 35  PRO C C   1 
ATOM   1659 O O   . PRO C 1 36 ? 24.229  -38.188 35.622  1.00 50.12  ? 35  PRO C O   1 
ATOM   1660 C CB  . PRO C 1 36 ? 23.117  -35.764 33.680  1.00 58.87  ? 35  PRO C CB  1 
ATOM   1661 C CG  . PRO C 1 36 ? 22.278  -34.745 34.420  1.00 59.24  ? 35  PRO C CG  1 
ATOM   1662 C CD  . PRO C 1 36 ? 22.013  -35.390 35.768  1.00 58.36  ? 35  PRO C CD  1 
ATOM   1663 N N   . PRO C 1 37 ? 24.344  -38.814 33.489  1.00 55.00  ? 36  PRO C N   1 
ATOM   1664 C CA  . PRO C 1 37 ? 25.695  -39.350 33.659  1.00 52.63  ? 36  PRO C CA  1 
ATOM   1665 C C   . PRO C 1 37 ? 26.617  -38.169 33.953  1.00 49.62  ? 36  PRO C C   1 
ATOM   1666 O O   . PRO C 1 37 ? 26.262  -37.027 33.658  1.00 41.99  ? 36  PRO C O   1 
ATOM   1667 C CB  . PRO C 1 37 ? 25.977  -40.000 32.286  1.00 47.73  ? 36  PRO C CB  1 
ATOM   1668 C CG  . PRO C 1 37 ? 24.599  -40.373 31.787  1.00 46.77  ? 36  PRO C CG  1 
ATOM   1669 C CD  . PRO C 1 37 ? 23.721  -39.198 32.207  1.00 49.51  ? 36  PRO C CD  1 
ATOM   1670 N N   . PRO C 1 38 ? 27.819  -38.407 34.537  1.00 47.31  ? 37  PRO C N   1 
ATOM   1671 C CA  . PRO C 1 38 ? 28.807  -37.349 34.766  1.00 47.69  ? 37  PRO C CA  1 
ATOM   1672 C C   . PRO C 1 38 ? 29.068  -36.464 33.554  1.00 45.54  ? 37  PRO C C   1 
ATOM   1673 O O   . PRO C 1 38 ? 29.351  -36.974 32.471  1.00 42.04  ? 37  PRO C O   1 
ATOM   1674 C CB  . PRO C 1 38 ? 30.085  -38.146 35.150  1.00 49.41  ? 37  PRO C CB  1 
ATOM   1675 C CG  . PRO C 1 38 ? 29.557  -39.422 35.753  1.00 50.00  ? 37  PRO C CG  1 
ATOM   1676 C CD  . PRO C 1 38 ? 28.276  -39.727 35.009  1.00 49.05  ? 37  PRO C CD  1 
ATOM   1677 N N   . ASN C 1 39 ? 28.994  -35.147 33.786  1.00 38.98  ? 38  ASN C N   1 
ATOM   1678 C CA  . ASN C 1 39 ? 29.369  -34.111 32.847  1.00 41.01  ? 38  ASN C CA  1 
ATOM   1679 C C   . ASN C 1 39 ? 28.455  -34.172 31.620  1.00 38.27  ? 38  ASN C C   1 
ATOM   1680 O O   . ASN C 1 39 ? 28.927  -33.932 30.507  1.00 45.95  ? 38  ASN C O   1 
ATOM   1681 C CB  . ASN C 1 39 ? 30.839  -34.220 32.456  1.00 44.31  ? 38  ASN C CB  1 
ATOM   1682 C CG  . ASN C 1 39 ? 31.382  -32.946 31.846  1.00 53.30  ? 38  ASN C CG  1 
ATOM   1683 O OD1 . ASN C 1 39 ? 30.863  -31.851 32.095  1.00 59.07  ? 38  ASN C OD1 1 
ATOM   1684 N ND2 . ASN C 1 39 ? 32.436  -33.063 31.050  1.00 52.17  ? 38  ASN C ND2 1 
ATOM   1685 N N   . LYS C 1 40 ? 27.169  -34.517 31.813  1.00 37.54  ? 39  LYS C N   1 
ATOM   1686 C CA  . LYS C 1 40 ? 26.208  -34.454 30.711  1.00 35.17  ? 39  LYS C CA  1 
ATOM   1687 C C   . LYS C 1 40 ? 25.065  -33.486 31.032  1.00 38.14  ? 39  LYS C C   1 
ATOM   1688 O O   . LYS C 1 40 ? 24.618  -33.389 32.164  1.00 40.80  ? 39  LYS C O   1 
ATOM   1689 C CB  . LYS C 1 40 ? 25.518  -35.791 30.423  1.00 35.90  ? 39  LYS C CB  1 
ATOM   1690 C CG  . LYS C 1 40 ? 26.463  -36.926 30.097  1.00 36.79  ? 39  LYS C CG  1 
ATOM   1691 C CD  . LYS C 1 40 ? 27.038  -36.939 28.694  1.00 43.85  ? 39  LYS C CD  1 
ATOM   1692 C CE  . LYS C 1 40 ? 27.972  -38.109 28.520  1.00 50.71  ? 39  LYS C CE  1 
ATOM   1693 N NZ  . LYS C 1 40 ? 28.940  -37.809 27.458  1.00 57.68  ? 39  LYS C NZ  1 
ATOM   1694 N N   . TYR C 1 41 ? 24.547  -32.793 30.005  1.00 32.68  ? 40  TYR C N   1 
ATOM   1695 C CA  . TYR C 1 41 ? 23.399  -31.914 30.199  1.00 33.17  ? 40  TYR C CA  1 
ATOM   1696 C C   . TYR C 1 41 ? 22.138  -32.588 29.671  1.00 36.13  ? 40  TYR C C   1 
ATOM   1697 O O   . TYR C 1 41 ? 22.195  -33.344 28.686  1.00 35.35  ? 40  TYR C O   1 
ATOM   1698 C CB  . TYR C 1 41 ? 23.561  -30.735 29.229  1.00 35.71  ? 40  TYR C CB  1 
ATOM   1699 C CG  . TYR C 1 41 ? 24.648  -29.774 29.670  1.00 37.06  ? 40  TYR C CG  1 
ATOM   1700 C CD1 . TYR C 1 41 ? 25.973  -29.935 29.267  1.00 39.06  ? 40  TYR C CD1 1 
ATOM   1701 C CD2 . TYR C 1 41 ? 24.335  -28.715 30.517  1.00 37.58  ? 40  TYR C CD2 1 
ATOM   1702 C CE1 . TYR C 1 41 ? 26.961  -29.051 29.673  1.00 46.35  ? 40  TYR C CE1 1 
ATOM   1703 C CE2 . TYR C 1 41 ? 25.317  -27.824 30.919  1.00 42.08  ? 40  TYR C CE2 1 
ATOM   1704 C CZ  . TYR C 1 41 ? 26.622  -27.995 30.504  1.00 45.26  ? 40  TYR C CZ  1 
ATOM   1705 O OH  . TYR C 1 41 ? 27.543  -27.079 30.919  1.00 55.51  ? 40  TYR C OH  1 
ATOM   1706 N N   . PRO C 1 42 ? 20.955  -32.275 30.257  1.00 38.62  ? 41  PRO C N   1 
ATOM   1707 C CA  . PRO C 1 42 ? 19.690  -32.757 29.714  1.00 35.47  ? 41  PRO C CA  1 
ATOM   1708 C C   . PRO C 1 42 ? 19.324  -31.805 28.583  1.00 34.65  ? 41  PRO C C   1 
ATOM   1709 O O   . PRO C 1 42 ? 19.314  -30.585 28.782  1.00 35.60  ? 41  PRO C O   1 
ATOM   1710 C CB  . PRO C 1 42 ? 18.713  -32.641 30.893  1.00 37.69  ? 41  PRO C CB  1 
ATOM   1711 C CG  . PRO C 1 42 ? 19.294  -31.560 31.756  1.00 40.17  ? 41  PRO C CG  1 
ATOM   1712 C CD  . PRO C 1 42 ? 20.780  -31.443 31.462  1.00 40.18  ? 41  PRO C CD  1 
ATOM   1713 N N   . ILE C 1 43 ? 19.045  -32.396 27.421  1.00 36.05  ? 42  ILE C N   1 
ATOM   1714 C CA  . ILE C 1 43 ? 18.723  -31.632 26.218  1.00 35.47  ? 42  ILE C CA  1 
ATOM   1715 C C   . ILE C 1 43 ? 17.296  -31.952 25.809  1.00 37.27  ? 42  ILE C C   1 
ATOM   1716 O O   . ILE C 1 43 ? 16.905  -33.117 25.774  1.00 38.09  ? 42  ILE C O   1 
ATOM   1717 C CB  . ILE C 1 43 ? 19.681  -32.031 25.083  1.00 32.41  ? 42  ILE C CB  1 
ATOM   1718 C CG1 . ILE C 1 43 ? 21.165  -31.798 25.483  1.00 33.07  ? 42  ILE C CG1 1 
ATOM   1719 C CG2 . ILE C 1 43 ? 19.288  -31.350 23.753  1.00 27.90  ? 42  ILE C CG2 1 
ATOM   1720 C CD1 . ILE C 1 43 ? 21.484  -30.378 25.914  1.00 33.57  ? 42  ILE C CD1 1 
ATOM   1721 N N   . PHE C 1 44 ? 16.558  -30.915 25.383  1.00 36.86  ? 43  PHE C N   1 
ATOM   1722 C CA  . PHE C 1 44 ? 15.277  -31.102 24.730  1.00 32.79  ? 43  PHE C CA  1 
ATOM   1723 C C   . PHE C 1 44 ? 15.437  -30.704 23.261  1.00 31.37  ? 43  PHE C C   1 
ATOM   1724 O O   . PHE C 1 44 ? 15.907  -29.606 22.991  1.00 33.25  ? 43  PHE C O   1 
ATOM   1725 C CB  . PHE C 1 44 ? 14.343  -30.075 25.381  1.00 35.70  ? 43  PHE C CB  1 
ATOM   1726 C CG  . PHE C 1 44 ? 12.959  -29.981 24.748  1.00 39.63  ? 43  PHE C CG  1 
ATOM   1727 C CD1 . PHE C 1 44 ? 11.965  -30.915 25.049  1.00 39.13  ? 43  PHE C CD1 1 
ATOM   1728 C CD2 . PHE C 1 44 ? 12.655  -28.951 23.851  1.00 39.57  ? 43  PHE C CD2 1 
ATOM   1729 C CE1 . PHE C 1 44 ? 10.694  -30.826 24.478  1.00 45.93  ? 43  PHE C CE1 1 
ATOM   1730 C CE2 . PHE C 1 44 ? 11.388  -28.868 23.284  1.00 39.85  ? 43  PHE C CE2 1 
ATOM   1731 C CZ  . PHE C 1 44 ? 10.411  -29.798 23.597  1.00 44.45  ? 43  PHE C CZ  1 
ATOM   1732 N N   . PHE C 1 45 ? 15.015  -31.591 22.353  1.00 29.44  ? 44  PHE C N   1 
ATOM   1733 C CA  . PHE C 1 45 ? 15.118  -31.381 20.916  1.00 32.84  ? 44  PHE C CA  1 
ATOM   1734 C C   . PHE C 1 45 ? 13.853  -30.689 20.401  1.00 34.78  ? 44  PHE C C   1 
ATOM   1735 O O   . PHE C 1 45 ? 12.744  -31.206 20.565  1.00 33.36  ? 44  PHE C O   1 
ATOM   1736 C CB  . PHE C 1 45 ? 15.467  -32.670 20.166  1.00 31.26  ? 44  PHE C CB  1 
ATOM   1737 C CG  . PHE C 1 45 ? 16.863  -33.174 20.492  1.00 30.78  ? 44  PHE C CG  1 
ATOM   1738 C CD1 . PHE C 1 45 ? 17.981  -32.707 19.812  1.00 27.46  ? 44  PHE C CD1 1 
ATOM   1739 C CD2 . PHE C 1 45 ? 17.049  -34.093 21.529  1.00 32.72  ? 44  PHE C CD2 1 
ATOM   1740 C CE1 . PHE C 1 45 ? 19.252  -33.185 20.128  1.00 35.09  ? 44  PHE C CE1 1 
ATOM   1741 C CE2 . PHE C 1 45 ? 18.322  -34.562 21.840  1.00 35.47  ? 44  PHE C CE2 1 
ATOM   1742 C CZ  . PHE C 1 45 ? 19.421  -34.094 21.168  1.00 36.18  ? 44  PHE C CZ  1 
ATOM   1743 N N   . PHE C 1 46 ? 14.036  -29.545 19.715  1.00 29.94  ? 45  PHE C N   1 
ATOM   1744 C CA  . PHE C 1 46 ? 12.895  -28.909 19.064  1.00 31.04  ? 45  PHE C CA  1 
ATOM   1745 C C   . PHE C 1 46 ? 12.394  -29.767 17.900  1.00 32.16  ? 45  PHE C C   1 
ATOM   1746 O O   . PHE C 1 46 ? 13.164  -30.481 17.257  1.00 32.12  ? 45  PHE C O   1 
ATOM   1747 C CB  . PHE C 1 46 ? 13.231  -27.467 18.642  1.00 30.10  ? 45  PHE C CB  1 
ATOM   1748 C CG  . PHE C 1 46 ? 13.462  -26.473 19.772  1.00 29.85  ? 45  PHE C CG  1 
ATOM   1749 C CD1 . PHE C 1 46 ? 12.406  -26.026 20.566  1.00 34.84  ? 45  PHE C CD1 1 
ATOM   1750 C CD2 . PHE C 1 46 ? 14.739  -25.975 20.042  1.00 28.90  ? 45  PHE C CD2 1 
ATOM   1751 C CE1 . PHE C 1 46 ? 12.655  -25.095 21.572  1.00 32.97  ? 45  PHE C CE1 1 
ATOM   1752 C CE2 . PHE C 1 46 ? 14.982  -25.073 21.070  1.00 32.76  ? 45  PHE C CE2 1 
ATOM   1753 C CZ  . PHE C 1 46 ? 13.938  -24.616 21.820  1.00 32.74  ? 45  PHE C CZ  1 
ATOM   1754 N N   . GLY C 1 47 ? 11.097  -29.641 17.575  1.00 29.71  ? 46  GLY C N   1 
ATOM   1755 C CA  . GLY C 1 47 ? 10.564  -30.373 16.429  1.00 32.66  ? 46  GLY C CA  1 
ATOM   1756 C C   . GLY C 1 47 ? 10.122  -31.780 16.815  1.00 39.75  ? 46  GLY C C   1 
ATOM   1757 O O   . GLY C 1 47 ? 8.923   -32.089 16.811  1.00 40.18  ? 46  GLY C O   1 
ATOM   1758 N N   . THR C 1 48 ? 11.089  -32.623 17.195  1.00 37.82  ? 47  THR C N   1 
ATOM   1759 C CA  . THR C 1 48 ? 10.745  -33.954 17.675  1.00 38.18  ? 47  THR C CA  1 
ATOM   1760 C C   . THR C 1 48 ? 10.247  -33.889 19.122  1.00 36.12  ? 47  THR C C   1 
ATOM   1761 O O   . THR C 1 48 ? 9.491   -34.769 19.543  1.00 39.45  ? 47  THR C O   1 
ATOM   1762 C CB  . THR C 1 48 ? 11.963  -34.871 17.587  1.00 35.63  ? 47  THR C CB  1 
ATOM   1763 O OG1 . THR C 1 48 ? 12.808  -34.366 18.616  1.00 36.48  ? 47  THR C OG1 1 
ATOM   1764 C CG2 . THR C 1 48 ? 12.578  -34.916 16.202  1.00 34.96  ? 47  THR C CG2 1 
ATOM   1765 N N   . HIS C 1 49 ? 10.689  -32.884 19.889  1.00 36.29  ? 48  HIS C N   1 
ATOM   1766 C CA  . HIS C 1 49 ? 10.396  -32.771 21.321  1.00 40.53  ? 48  HIS C CA  1 
ATOM   1767 C C   . HIS C 1 49 ? 10.841  -33.993 22.135  1.00 39.16  ? 48  HIS C C   1 
ATOM   1768 O O   . HIS C 1 49 ? 10.181  -34.342 23.115  1.00 43.20  ? 48  HIS C O   1 
ATOM   1769 C CB  . HIS C 1 49 ? 8.905   -32.531 21.585  1.00 43.84  ? 48  HIS C CB  1 
ATOM   1770 C CG  . HIS C 1 49 ? 8.342   -31.478 20.693  1.00 44.65  ? 48  HIS C CG  1 
ATOM   1771 N ND1 . HIS C 1 49 ? 7.204   -31.678 19.944  1.00 51.50  ? 48  HIS C ND1 1 
ATOM   1772 C CD2 . HIS C 1 49 ? 8.810   -30.273 20.353  1.00 41.64  ? 48  HIS C CD2 1 
ATOM   1773 C CE1 . HIS C 1 49 ? 6.971   -30.595 19.212  1.00 54.45  ? 48  HIS C CE1 1 
ATOM   1774 N NE2 . HIS C 1 49 ? 7.935   -29.729 19.450  1.00 49.45  ? 48  HIS C NE2 1 
ATOM   1775 N N   . GLU C 1 50 ? 11.957  -34.620 21.751  1.00 40.80  ? 49  GLU C N   1 
ATOM   1776 C CA  . GLU C 1 50 ? 12.543  -35.703 22.529  1.00 39.72  ? 49  GLU C CA  1 
ATOM   1777 C C   . GLU C 1 50 ? 13.666  -35.172 23.416  1.00 39.55  ? 49  GLU C C   1 
ATOM   1778 O O   . GLU C 1 50 ? 14.071  -34.019 23.286  1.00 37.53  ? 49  GLU C O   1 
ATOM   1779 C CB  . GLU C 1 50 ? 13.018  -36.773 21.561  1.00 38.60  ? 49  GLU C CB  1 
ATOM   1780 C CG  . GLU C 1 50 ? 11.855  -37.313 20.735  1.00 43.72  ? 49  GLU C CG  1 
ATOM   1781 C CD  . GLU C 1 50 ? 12.264  -38.316 19.682  1.00 49.60  ? 49  GLU C CD  1 
ATOM   1782 O OE1 . GLU C 1 50 ? 13.468  -38.635 19.545  1.00 56.04  ? 49  GLU C OE1 1 
ATOM   1783 O OE2 . GLU C 1 50 ? 11.340  -38.770 18.986  1.00 58.68  ? 49  GLU C OE2 1 
ATOM   1784 N N   . THR C 1 51 ? 14.120  -36.008 24.364  1.00 39.01  ? 50  THR C N   1 
ATOM   1785 C CA  . THR C 1 51 ? 15.203  -35.610 25.251  1.00 42.05  ? 50  THR C CA  1 
ATOM   1786 C C   . THR C 1 51 ? 16.356  -36.613 25.169  1.00 38.20  ? 50  THR C C   1 
ATOM   1787 O O   . THR C 1 51 ? 16.222  -37.744 24.687  1.00 37.35  ? 50  THR C O   1 
ATOM   1788 C CB  . THR C 1 51 ? 14.715  -35.373 26.684  1.00 43.45  ? 50  THR C CB  1 
ATOM   1789 O OG1 . THR C 1 51 ? 14.125  -36.622 27.044  1.00 42.94  ? 50  THR C OG1 1 
ATOM   1790 C CG2 . THR C 1 51 ? 13.742  -34.212 26.838  1.00 40.19  ? 50  THR C CG2 1 
ATOM   1791 N N   . ALA C 1 52 ? 17.526  -36.145 25.591  1.00 40.46  ? 51  ALA C N   1 
ATOM   1792 C CA  . ALA C 1 52 ? 18.692  -37.001 25.725  1.00 37.40  ? 51  ALA C CA  1 
ATOM   1793 C C   . ALA C 1 52 ? 19.711  -36.307 26.623  1.00 41.67  ? 51  ALA C C   1 
ATOM   1794 O O   . ALA C 1 52 ? 19.556  -35.139 26.967  1.00 43.08  ? 51  ALA C O   1 
ATOM   1795 C CB  . ALA C 1 52 ? 19.267  -37.326 24.364  1.00 36.04  ? 51  ALA C CB  1 
ATOM   1796 N N   . PHE C 1 53 ? 20.763  -37.044 26.997  1.00 41.35  ? 52  PHE C N   1 
ATOM   1797 C CA  . PHE C 1 53 ? 21.879  -36.465 27.729  1.00 40.12  ? 52  PHE C CA  1 
ATOM   1798 C C   . PHE C 1 53 ? 23.028  -36.316 26.753  1.00 40.00  ? 52  PHE C C   1 
ATOM   1799 O O   . PHE C 1 53 ? 23.370  -37.276 26.050  1.00 38.01  ? 52  PHE C O   1 
ATOM   1800 C CB  . PHE C 1 53 ? 22.311  -37.407 28.863  1.00 38.86  ? 52  PHE C CB  1 
ATOM   1801 C CG  . PHE C 1 53 ? 21.340  -37.359 30.025  1.00 40.26  ? 52  PHE C CG  1 
ATOM   1802 C CD1 . PHE C 1 53 ? 21.005  -36.149 30.622  1.00 43.12  ? 52  PHE C CD1 1 
ATOM   1803 C CD2 . PHE C 1 53 ? 20.694  -38.514 30.458  1.00 51.61  ? 52  PHE C CD2 1 
ATOM   1804 C CE1 . PHE C 1 53 ? 20.089  -36.095 31.668  1.00 50.59  ? 52  PHE C CE1 1 
ATOM   1805 C CE2 . PHE C 1 53 ? 19.778  -38.456 31.502  1.00 51.73  ? 52  PHE C CE2 1 
ATOM   1806 C CZ  . PHE C 1 53 ? 19.466  -37.250 32.096  1.00 48.29  ? 52  PHE C CZ  1 
ATOM   1807 N N   . LEU C 1 54 ? 23.633  -35.126 26.746  1.00 34.34  ? 53  LEU C N   1 
ATOM   1808 C CA  . LEU C 1 54 ? 24.799  -34.874 25.916  1.00 32.98  ? 53  LEU C CA  1 
ATOM   1809 C C   . LEU C 1 54 ? 25.873  -34.104 26.685  1.00 33.87  ? 53  LEU C C   1 
ATOM   1810 O O   . LEU C 1 54 ? 25.574  -33.314 27.574  1.00 36.35  ? 53  LEU C O   1 
ATOM   1811 C CB  . LEU C 1 54 ? 24.377  -34.106 24.658  1.00 34.22  ? 53  LEU C CB  1 
ATOM   1812 C CG  . LEU C 1 54 ? 23.633  -34.900 23.579  1.00 36.08  ? 53  LEU C CG  1 
ATOM   1813 C CD1 . LEU C 1 54 ? 23.286  -33.937 22.437  1.00 35.52  ? 53  LEU C CD1 1 
ATOM   1814 C CD2 . LEU C 1 54 ? 24.493  -36.059 23.068  1.00 42.96  ? 53  LEU C CD2 1 
ATOM   1815 N N   . GLY C 1 55 ? 27.121  -34.310 26.272  1.00 35.34  ? 54  GLY C N   1 
ATOM   1816 C CA  . GLY C 1 55 ? 28.272  -33.594 26.805  1.00 33.43  ? 54  GLY C CA  1 
ATOM   1817 C C   . GLY C 1 55 ? 28.460  -32.242 26.122  1.00 40.71  ? 54  GLY C C   1 
ATOM   1818 O O   . GLY C 1 55 ? 27.975  -32.011 24.997  1.00 33.87  ? 54  GLY C O   1 
ATOM   1819 N N   . PRO C 1 56 ? 29.192  -31.306 26.777  1.00 42.45  ? 55  PRO C N   1 
ATOM   1820 C CA  . PRO C 1 56 ? 29.255  -29.920 26.304  1.00 42.37  ? 55  PRO C CA  1 
ATOM   1821 C C   . PRO C 1 56 ? 29.917  -29.854 24.928  1.00 41.23  ? 55  PRO C C   1 
ATOM   1822 O O   . PRO C 1 56 ? 29.698  -28.908 24.171  1.00 47.30  ? 55  PRO C O   1 
ATOM   1823 C CB  . PRO C 1 56 ? 30.074  -29.185 27.417  1.00 44.78  ? 55  PRO C CB  1 
ATOM   1824 C CG  . PRO C 1 56 ? 30.891  -30.296 28.069  1.00 38.78  ? 55  PRO C CG  1 
ATOM   1825 C CD  . PRO C 1 56 ? 29.992  -31.529 28.001  1.00 43.42  ? 55  PRO C CD  1 
ATOM   1826 N N   . LYS C 1 57 ? 30.725  -30.873 24.620  1.00 35.93  ? 56  LYS C N   1 
ATOM   1827 C CA  . LYS C 1 57 ? 31.425  -31.012 23.357  1.00 40.87  ? 56  LYS C CA  1 
ATOM   1828 C C   . LYS C 1 57 ? 30.417  -31.049 22.210  1.00 43.02  ? 56  LYS C C   1 
ATOM   1829 O O   . LYS C 1 57 ? 30.753  -30.722 21.075  1.00 40.13  ? 56  LYS C O   1 
ATOM   1830 C CB  . LYS C 1 57 ? 32.093  -32.391 23.267  1.00 43.85  ? 56  LYS C CB  1 
ATOM   1831 N N   . ASP C 1 58 ? 29.191  -31.495 22.513  1.00 36.45  ? 57  ASP C N   1 
ATOM   1832 C CA  . ASP C 1 58 ? 28.231  -31.817 21.469  1.00 37.70  ? 57  ASP C CA  1 
ATOM   1833 C C   . ASP C 1 58 ? 27.213  -30.701 21.312  1.00 39.81  ? 57  ASP C C   1 
ATOM   1834 O O   . ASP C 1 58 ? 26.198  -30.882 20.637  1.00 34.35  ? 57  ASP C O   1 
ATOM   1835 C CB  . ASP C 1 58 ? 27.510  -33.109 21.785  1.00 39.95  ? 57  ASP C CB  1 
ATOM   1836 C CG  . ASP C 1 58 ? 28.405  -34.335 21.750  1.00 44.76  ? 57  ASP C CG  1 
ATOM   1837 O OD1 . ASP C 1 58 ? 29.297  -34.364 20.890  1.00 50.01  ? 57  ASP C OD1 1 
ATOM   1838 O OD2 . ASP C 1 58 ? 28.149  -35.266 22.531  1.00 49.47  ? 57  ASP C OD2 1 
ATOM   1839 N N   . LEU C 1 59 ? 27.493  -29.570 21.957  1.00 32.32  ? 58  LEU C N   1 
ATOM   1840 C CA  . LEU C 1 59 ? 26.549  -28.463 22.060  1.00 32.94  ? 58  LEU C CA  1 
ATOM   1841 C C   . LEU C 1 59 ? 27.196  -27.192 21.533  1.00 39.17  ? 58  LEU C C   1 
ATOM   1842 O O   . LEU C 1 59 ? 28.389  -26.978 21.787  1.00 39.35  ? 58  LEU C O   1 
ATOM   1843 C CB  . LEU C 1 59 ? 26.212  -28.296 23.533  1.00 33.87  ? 58  LEU C CB  1 
ATOM   1844 C CG  . LEU C 1 59 ? 25.649  -29.550 24.194  1.00 34.20  ? 58  LEU C CG  1 
ATOM   1845 C CD1 . LEU C 1 59 ? 25.478  -29.274 25.668  1.00 35.80  ? 58  LEU C CD1 1 
ATOM   1846 C CD2 . LEU C 1 59 ? 24.317  -29.984 23.550  1.00 30.82  ? 58  LEU C CD2 1 
ATOM   1847 N N   . PHE C 1 60 ? 26.389  -26.386 20.823  1.00 36.63  ? 59  PHE C N   1 
ATOM   1848 C CA  . PHE C 1 60 ? 26.819  -25.133 20.201  1.00 37.48  ? 59  PHE C CA  1 
ATOM   1849 C C   . PHE C 1 60 ? 25.780  -24.059 20.483  1.00 40.14  ? 59  PHE C C   1 
ATOM   1850 O O   . PHE C 1 60 ? 24.599  -24.285 20.252  1.00 39.14  ? 59  PHE C O   1 
ATOM   1851 C CB  . PHE C 1 60 ? 27.042  -25.308 18.695  1.00 38.74  ? 59  PHE C CB  1 
ATOM   1852 C CG  . PHE C 1 60 ? 27.945  -26.490 18.377  1.00 36.78  ? 59  PHE C CG  1 
ATOM   1853 C CD1 . PHE C 1 60 ? 27.451  -27.795 18.397  1.00 33.12  ? 59  PHE C CD1 1 
ATOM   1854 C CD2 . PHE C 1 60 ? 29.305  -26.301 18.120  1.00 42.30  ? 59  PHE C CD2 1 
ATOM   1855 C CE1 . PHE C 1 60 ? 28.283  -28.886 18.168  1.00 34.53  ? 59  PHE C CE1 1 
ATOM   1856 C CE2 . PHE C 1 60 ? 30.131  -27.393 17.857  1.00 41.14  ? 59  PHE C CE2 1 
ATOM   1857 C CZ  . PHE C 1 60 ? 29.618  -28.680 17.885  1.00 39.69  ? 59  PHE C CZ  1 
ATOM   1858 N N   . PRO C 1 61 ? 26.157  -22.863 21.009  1.00 38.21  ? 60  PRO C N   1 
ATOM   1859 C CA  . PRO C 1 61 ? 25.162  -21.829 21.317  1.00 36.03  ? 60  PRO C CA  1 
ATOM   1860 C C   . PRO C 1 61 ? 24.479  -21.386 20.025  1.00 34.44  ? 60  PRO C C   1 
ATOM   1861 O O   . PRO C 1 61 ? 25.146  -21.234 19.002  1.00 43.55  ? 60  PRO C O   1 
ATOM   1862 C CB  . PRO C 1 61 ? 25.929  -20.662 22.034  1.00 36.63  ? 60  PRO C CB  1 
ATOM   1863 C CG  . PRO C 1 61 ? 27.341  -21.212 22.231  1.00 38.35  ? 60  PRO C CG  1 
ATOM   1864 C CD  . PRO C 1 61 ? 27.536  -22.451 21.342  1.00 45.08  ? 60  PRO C CD  1 
ATOM   1865 N N   . TYR C 1 62 ? 23.148  -21.241 20.113  1.00 36.48  ? 61  TYR C N   1 
ATOM   1866 C CA  . TYR C 1 62 ? 22.259  -20.961 18.993  1.00 38.22  ? 61  TYR C CA  1 
ATOM   1867 C C   . TYR C 1 62 ? 22.787  -19.773 18.184  1.00 42.70  ? 61  TYR C C   1 
ATOM   1868 O O   . TYR C 1 62 ? 22.938  -19.870 16.958  1.00 42.09  ? 61  TYR C O   1 
ATOM   1869 C CB  . TYR C 1 62 ? 20.812  -20.795 19.472  1.00 42.42  ? 61  TYR C CB  1 
ATOM   1870 C CG  . TYR C 1 62 ? 19.865  -20.470 18.328  1.00 43.14  ? 61  TYR C CG  1 
ATOM   1871 C CD1 . TYR C 1 62 ? 19.695  -21.364 17.265  1.00 42.32  ? 61  TYR C CD1 1 
ATOM   1872 C CD2 . TYR C 1 62 ? 19.152  -19.272 18.305  1.00 45.25  ? 61  TYR C CD2 1 
ATOM   1873 C CE1 . TYR C 1 62 ? 18.853  -21.063 16.205  1.00 42.67  ? 61  TYR C CE1 1 
ATOM   1874 C CE2 . TYR C 1 62 ? 18.308  -18.964 17.253  1.00 44.24  ? 61  TYR C CE2 1 
ATOM   1875 C CZ  . TYR C 1 62 ? 18.162  -19.861 16.205  1.00 43.12  ? 61  TYR C CZ  1 
ATOM   1876 O OH  . TYR C 1 62 ? 17.321  -19.552 15.182  1.00 41.71  ? 61  TYR C OH  1 
ATOM   1877 N N   . ASP C 1 63 ? 23.144  -18.687 18.889  1.00 48.86  ? 62  ASP C N   1 
ATOM   1878 C CA  . ASP C 1 63 ? 23.479  -17.426 18.231  1.00 53.81  ? 62  ASP C CA  1 
ATOM   1879 C C   . ASP C 1 63 ? 24.792  -17.507 17.465  1.00 46.84  ? 62  ASP C C   1 
ATOM   1880 O O   . ASP C 1 63 ? 24.874  -17.028 16.334  1.00 52.29  ? 62  ASP C O   1 
ATOM   1881 C CB  . ASP C 1 63 ? 23.366  -16.232 19.163  1.00 58.13  ? 62  ASP C CB  1 
ATOM   1882 C CG  . ASP C 1 63 ? 22.039  -15.507 19.039  1.00 72.18  ? 62  ASP C CG  1 
ATOM   1883 O OD1 . ASP C 1 63 ? 21.188  -15.671 19.946  1.00 67.16  ? 62  ASP C OD1 1 
ATOM   1884 O OD2 . ASP C 1 63 ? 21.861  -14.805 18.015  1.00 82.48  ? 62  ASP C OD2 1 
ATOM   1885 N N   . LYS C 1 64 ? 25.795  -18.134 18.075  1.00 40.79  ? 63  LYS C N   1 
ATOM   1886 C CA  . LYS C 1 64 ? 27.125  -18.252 17.502  1.00 42.93  ? 63  LYS C CA  1 
ATOM   1887 C C   . LYS C 1 64 ? 27.117  -19.171 16.288  1.00 40.10  ? 63  LYS C C   1 
ATOM   1888 O O   . LYS C 1 64 ? 27.921  -18.980 15.382  1.00 41.10  ? 63  LYS C O   1 
ATOM   1889 C CB  . LYS C 1 64 ? 28.166  -18.752 18.511  1.00 42.36  ? 63  LYS C CB  1 
ATOM   1890 N N   . SER C 1 65 ? 26.184  -20.141 16.236  1.00 37.60  ? 64  SER C N   1 
ATOM   1891 C CA  . SER C 1 65 ? 26.361  -21.222 15.271  1.00 34.33  ? 64  SER C CA  1 
ATOM   1892 C C   . SER C 1 65 ? 25.195  -21.324 14.274  1.00 32.14  ? 64  SER C C   1 
ATOM   1893 O O   . SER C 1 65 ? 25.237  -22.134 13.355  1.00 34.67  ? 64  SER C O   1 
ATOM   1894 C CB  . SER C 1 65 ? 26.664  -22.550 15.955  1.00 37.49  ? 64  SER C CB  1 
ATOM   1895 O OG  . SER C 1 65 ? 25.542  -23.036 16.683  1.00 39.31  ? 64  SER C OG  1 
ATOM   1896 N N   . LYS C 1 66 ? 24.151  -20.516 14.455  1.00 35.50  ? 65  LYS C N   1 
ATOM   1897 C CA  . LYS C 1 66 ? 22.991  -20.713 13.590  1.00 36.50  ? 65  LYS C CA  1 
ATOM   1898 C C   . LYS C 1 66 ? 23.323  -20.410 12.130  1.00 36.00  ? 65  LYS C C   1 
ATOM   1899 O O   . LYS C 1 66 ? 22.729  -21.007 11.242  1.00 35.28  ? 65  LYS C O   1 
ATOM   1900 C CB  . LYS C 1 66 ? 21.790  -19.860 13.974  1.00 35.34  ? 65  LYS C CB  1 
ATOM   1901 C CG  . LYS C 1 66 ? 22.123  -18.392 14.042  1.00 34.68  ? 65  LYS C CG  1 
ATOM   1902 C CD  . LYS C 1 66 ? 20.861  -17.680 14.512  1.00 39.93  ? 65  LYS C CD  1 
ATOM   1903 C CE  . LYS C 1 66 ? 21.014  -16.216 14.633  1.00 44.50  ? 65  LYS C CE  1 
ATOM   1904 N NZ  . LYS C 1 66 ? 19.713  -15.784 15.136  1.00 48.48  ? 65  LYS C NZ  1 
ATOM   1905 N N   . ASP C 1 67 ? 24.260  -19.481 11.878  1.00 37.63  ? 66  ASP C N   1 
ATOM   1906 C CA  . ASP C 1 67 ? 24.692  -19.206 10.507  1.00 43.06  ? 66  ASP C CA  1 
ATOM   1907 C C   . ASP C 1 67 ? 25.181  -20.495 9.853   1.00 41.30  ? 66  ASP C C   1 
ATOM   1908 O O   . ASP C 1 67 ? 25.002  -20.687 8.653   1.00 41.67  ? 66  ASP C O   1 
ATOM   1909 C CB  . ASP C 1 67 ? 25.686  -18.044 10.402  1.00 44.64  ? 66  ASP C CB  1 
ATOM   1910 C CG  . ASP C 1 67 ? 27.085  -18.262 10.986  1.00 59.12  ? 66  ASP C CG  1 
ATOM   1911 O OD1 . ASP C 1 67 ? 27.300  -19.271 11.710  1.00 57.46  ? 66  ASP C OD1 1 
ATOM   1912 O OD2 . ASP C 1 67 ? 27.963  -17.398 10.742  1.00 62.13  ? 66  ASP C OD2 1 
ATOM   1913 N N   . LYS C 1 68 ? 25.749  -21.411 10.653  1.00 39.26  ? 67  LYS C N   1 
ATOM   1914 C CA  . LYS C 1 68 ? 26.268  -22.663 10.136  1.00 35.18  ? 67  LYS C CA  1 
ATOM   1915 C C   . LYS C 1 68 ? 25.234  -23.806 10.169  1.00 37.63  ? 67  LYS C C   1 
ATOM   1916 O O   . LYS C 1 68 ? 25.157  -24.588 9.233   1.00 38.05  ? 67  LYS C O   1 
ATOM   1917 C CB  . LYS C 1 68 ? 27.585  -22.997 10.845  1.00 40.86  ? 67  LYS C CB  1 
ATOM   1918 C CG  . LYS C 1 68 ? 28.250  -24.295 10.438  1.00 45.20  ? 67  LYS C CG  1 
ATOM   1919 C CD  . LYS C 1 68 ? 29.534  -24.499 11.247  1.00 56.20  ? 67  LYS C CD  1 
ATOM   1920 C CE  . LYS C 1 68 ? 30.094  -25.890 11.185  1.00 60.79  ? 67  LYS C CE  1 
ATOM   1921 N NZ  . LYS C 1 68 ? 30.653  -26.241 9.877   1.00 66.05  ? 67  LYS C NZ  1 
ATOM   1922 N N   . TYR C 1 69 ? 24.462  -23.959 11.255  1.00 31.23  ? 68  TYR C N   1 
ATOM   1923 C CA  . TYR C 1 69 ? 23.678  -25.181 11.404  1.00 29.77  ? 68  TYR C CA  1 
ATOM   1924 C C   . TYR C 1 69 ? 22.190  -24.895 11.172  1.00 30.88  ? 68  TYR C C   1 
ATOM   1925 O O   . TYR C 1 69 ? 21.382  -25.815 11.101  1.00 33.05  ? 68  TYR C O   1 
ATOM   1926 C CB  . TYR C 1 69 ? 23.859  -25.766 12.818  1.00 29.92  ? 68  TYR C CB  1 
ATOM   1927 C CG  . TYR C 1 69 ? 25.291  -26.208 13.106  1.00 28.89  ? 68  TYR C CG  1 
ATOM   1928 C CD1 . TYR C 1 69 ? 25.991  -27.032 12.230  1.00 32.02  ? 68  TYR C CD1 1 
ATOM   1929 C CD2 . TYR C 1 69 ? 25.930  -25.794 14.267  1.00 34.55  ? 68  TYR C CD2 1 
ATOM   1930 C CE1 . TYR C 1 69 ? 27.290  -27.454 12.497  1.00 32.84  ? 68  TYR C CE1 1 
ATOM   1931 C CE2 . TYR C 1 69 ? 27.222  -26.225 14.558  1.00 34.78  ? 68  TYR C CE2 1 
ATOM   1932 C CZ  . TYR C 1 69 ? 27.895  -27.060 13.683  1.00 36.27  ? 68  TYR C CZ  1 
ATOM   1933 O OH  . TYR C 1 69 ? 29.187  -27.407 14.011  1.00 39.50  ? 68  TYR C OH  1 
ATOM   1934 N N   . GLY C 1 70 ? 21.825  -23.623 11.103  1.00 29.11  ? 69  GLY C N   1 
ATOM   1935 C CA  . GLY C 1 70 ? 20.399  -23.316 11.049  1.00 33.41  ? 69  GLY C CA  1 
ATOM   1936 C C   . GLY C 1 70 ? 19.998  -23.175 9.593   1.00 33.68  ? 69  GLY C C   1 
ATOM   1937 O O   . GLY C 1 70 ? 19.870  -22.073 9.068   1.00 35.39  ? 69  GLY C O   1 
ATOM   1938 N N   . LYS C 1 71 ? 19.883  -24.320 8.943   1.00 35.41  ? 70  LYS C N   1 
ATOM   1939 C CA  . LYS C 1 71 ? 19.514  -24.362 7.543   1.00 33.02  ? 70  LYS C CA  1 
ATOM   1940 C C   . LYS C 1 71 ? 18.652  -25.599 7.434   1.00 36.60  ? 70  LYS C C   1 
ATOM   1941 O O   . LYS C 1 71 ? 18.854  -26.551 8.193   1.00 36.09  ? 70  LYS C O   1 
ATOM   1942 C CB  . LYS C 1 71 ? 20.758  -24.495 6.661   1.00 37.55  ? 70  LYS C CB  1 
ATOM   1943 C CG  . LYS C 1 71 ? 21.767  -25.498 7.207   1.00 44.74  ? 70  LYS C CG  1 
ATOM   1944 C CD  . LYS C 1 71 ? 22.970  -25.926 6.376   1.00 49.83  ? 70  LYS C CD  1 
ATOM   1945 C CE  . LYS C 1 71 ? 23.894  -26.780 7.201   1.00 54.77  ? 70  LYS C CE  1 
ATOM   1946 N N   . PRO C 1 72 ? 17.612  -25.579 6.577   1.00 31.16  ? 71  PRO C N   1 
ATOM   1947 C CA  . PRO C 1 72 ? 16.684  -26.698 6.523   1.00 27.76  ? 71  PRO C CA  1 
ATOM   1948 C C   . PRO C 1 72 ? 17.356  -28.011 6.148   1.00 34.45  ? 71  PRO C C   1 
ATOM   1949 O O   . PRO C 1 72 ? 18.403  -28.029 5.502   1.00 36.34  ? 71  PRO C O   1 
ATOM   1950 C CB  . PRO C 1 72 ? 15.737  -26.228 5.407   1.00 33.22  ? 71  PRO C CB  1 
ATOM   1951 C CG  . PRO C 1 72 ? 15.686  -24.744 5.633   1.00 30.67  ? 71  PRO C CG  1 
ATOM   1952 C CD  . PRO C 1 72 ? 17.197  -24.431 5.750   1.00 28.38  ? 71  PRO C CD  1 
ATOM   1953 N N   . ASN C 1 73 ? 16.697  -29.089 6.541   1.00 33.52  ? 72  ASN C N   1 
ATOM   1954 C CA  . ASN C 1 73 ? 16.985  -30.372 5.945   1.00 41.20  ? 72  ASN C CA  1 
ATOM   1955 C C   . ASN C 1 73 ? 15.779  -31.256 6.194   1.00 33.65  ? 72  ASN C C   1 
ATOM   1956 O O   . ASN C 1 73 ? 14.858  -30.881 6.927   1.00 34.38  ? 72  ASN C O   1 
ATOM   1957 C CB  . ASN C 1 73 ? 18.322  -30.959 6.376   1.00 46.71  ? 72  ASN C CB  1 
ATOM   1958 C CG  . ASN C 1 73 ? 18.234  -31.548 7.760   1.00 44.68  ? 72  ASN C CG  1 
ATOM   1959 O OD1 . ASN C 1 73 ? 17.548  -32.559 7.971   1.00 41.61  ? 72  ASN C OD1 1 
ATOM   1960 N ND2 . ASN C 1 73 ? 18.933  -30.931 8.694   1.00 51.17  ? 72  ASN C ND2 1 
ATOM   1961 N N   . LYS C 1 74 ? 15.805  -32.431 5.568   1.00 35.69  ? 73  LYS C N   1 
ATOM   1962 C CA  . LYS C 1 74 ? 14.575  -33.184 5.382   1.00 32.10  ? 73  LYS C CA  1 
ATOM   1963 C C   . LYS C 1 74 ? 14.364  -34.190 6.502   1.00 36.86  ? 73  LYS C C   1 
ATOM   1964 O O   . LYS C 1 74 ? 13.411  -34.960 6.454   1.00 39.93  ? 73  LYS C O   1 
ATOM   1965 C CB  . LYS C 1 74 ? 14.621  -33.885 4.015   1.00 37.10  ? 73  LYS C CB  1 
ATOM   1966 N N   . ARG C 1 75 ? 15.239  -34.221 7.514   1.00 33.02  ? 74  ARG C N   1 
ATOM   1967 C CA  . ARG C 1 75 ? 15.019  -35.183 8.589   1.00 29.96  ? 74  ARG C CA  1 
ATOM   1968 C C   . ARG C 1 75 ? 13.759  -34.857 9.375   1.00 34.72  ? 74  ARG C C   1 
ATOM   1969 O O   . ARG C 1 75 ? 13.458  -33.688 9.630   1.00 31.40  ? 74  ARG C O   1 
ATOM   1970 C CB  . ARG C 1 75 ? 16.199  -35.326 9.570   1.00 34.49  ? 74  ARG C CB  1 
ATOM   1971 C CG  . ARG C 1 75 ? 17.559  -35.423 8.886   1.00 47.11  ? 74  ARG C CG  1 
ATOM   1972 C CD  . ARG C 1 75 ? 17.906  -36.775 8.254   1.00 44.54  ? 74  ARG C CD  1 
ATOM   1973 N NE  . ARG C 1 75 ? 17.956  -37.760 9.341   1.00 41.30  ? 74  ARG C NE  1 
ATOM   1974 C CZ  . ARG C 1 75 ? 19.103  -38.183 9.888   1.00 36.63  ? 74  ARG C CZ  1 
ATOM   1975 N NH1 . ARG C 1 75 ? 19.054  -38.756 11.073  1.00 39.47  ? 74  ARG C NH1 1 
ATOM   1976 N NH2 . ARG C 1 75 ? 20.263  -37.891 9.331   1.00 37.26  ? 74  ARG C NH2 1 
ATOM   1977 N N   . LYS C 1 76 ? 13.062  -35.933 9.790   1.00 35.06  ? 75  LYS C N   1 
ATOM   1978 C CA  . LYS C 1 76 ? 11.794  -35.864 10.496  1.00 41.27  ? 75  LYS C CA  1 
ATOM   1979 C C   . LYS C 1 76 ? 11.861  -34.867 11.642  1.00 37.94  ? 75  LYS C C   1 
ATOM   1980 O O   . LYS C 1 76 ? 12.609  -35.035 12.616  1.00 34.13  ? 75  LYS C O   1 
ATOM   1981 C CB  . LYS C 1 76 ? 11.234  -37.232 10.910  1.00 40.18  ? 75  LYS C CB  1 
ATOM   1982 C CG  . LYS C 1 76 ? 9.724   -37.387 10.691  1.00 51.07  ? 75  LYS C CG  1 
ATOM   1983 C CD  . LYS C 1 76 ? 8.978   -38.072 11.838  1.00 54.48  ? 75  LYS C CD  1 
ATOM   1984 N N   . GLY C 1 77 ? 11.059  -33.802 11.514  1.00 36.64  ? 76  GLY C N   1 
ATOM   1985 C CA  . GLY C 1 77 ? 10.869  -32.930 12.664  1.00 31.38  ? 76  GLY C CA  1 
ATOM   1986 C C   . GLY C 1 77 ? 11.814  -31.723 12.640  1.00 28.14  ? 76  GLY C C   1 
ATOM   1987 O O   . GLY C 1 77 ? 11.607  -30.778 13.388  1.00 32.49  ? 76  GLY C O   1 
ATOM   1988 N N   . PHE C 1 78 ? 12.806  -31.743 11.746  1.00 28.21  ? 77  PHE C N   1 
ATOM   1989 C CA  . PHE C 1 78 ? 13.897  -30.788 11.803  1.00 26.27  ? 77  PHE C CA  1 
ATOM   1990 C C   . PHE C 1 78 ? 13.388  -29.364 11.534  1.00 32.07  ? 77  PHE C C   1 
ATOM   1991 O O   . PHE C 1 78 ? 13.735  -28.421 12.247  1.00 31.77  ? 77  PHE C O   1 
ATOM   1992 C CB  . PHE C 1 78 ? 15.012  -31.157 10.823  1.00 33.51  ? 77  PHE C CB  1 
ATOM   1993 C CG  . PHE C 1 78 ? 16.272  -30.346 11.081  1.00 32.64  ? 77  PHE C CG  1 
ATOM   1994 C CD1 . PHE C 1 78 ? 16.456  -29.111 10.476  1.00 30.42  ? 77  PHE C CD1 1 
ATOM   1995 C CD2 . PHE C 1 78 ? 17.272  -30.836 11.919  1.00 33.70  ? 77  PHE C CD2 1 
ATOM   1996 C CE1 . PHE C 1 78 ? 17.612  -28.365 10.708  1.00 27.85  ? 77  PHE C CE1 1 
ATOM   1997 C CE2 . PHE C 1 78 ? 18.427  -30.096 12.146  1.00 30.36  ? 77  PHE C CE2 1 
ATOM   1998 C CZ  . PHE C 1 78 ? 18.595  -28.869 11.551  1.00 30.00  ? 77  PHE C CZ  1 
ATOM   1999 N N   . ASN C 1 79 ? 12.651  -29.204 10.432  1.00 30.25  ? 78  ASN C N   1 
ATOM   2000 C CA  . ASN C 1 79 ? 12.291  -27.863 10.004  1.00 32.22  ? 78  ASN C CA  1 
ATOM   2001 C C   . ASN C 1 79 ? 11.295  -27.268 10.986  1.00 30.18  ? 78  ASN C C   1 
ATOM   2002 O O   . ASN C 1 79 ? 11.306  -26.060 11.264  1.00 27.40  ? 78  ASN C O   1 
ATOM   2003 C CB  . ASN C 1 79 ? 11.819  -27.852 8.554   1.00 30.76  ? 78  ASN C CB  1 
ATOM   2004 C CG  . ASN C 1 79 ? 12.963  -28.207 7.638   1.00 31.48  ? 78  ASN C CG  1 
ATOM   2005 O OD1 . ASN C 1 79 ? 14.120  -27.928 7.971   1.00 29.97  ? 78  ASN C OD1 1 
ATOM   2006 N ND2 . ASN C 1 79 ? 12.668  -28.744 6.472   1.00 31.76  ? 78  ASN C ND2 1 
ATOM   2007 N N   . GLU C 1 80 ? 10.400  -28.110 11.499  1.00 33.50  ? 79  GLU C N   1 
ATOM   2008 C CA  . GLU C 1 80 ? 9.511   -27.618 12.537  1.00 31.68  ? 79  GLU C CA  1 
ATOM   2009 C C   . GLU C 1 80 ? 10.347  -27.219 13.753  1.00 33.61  ? 79  GLU C C   1 
ATOM   2010 O O   . GLU C 1 80 ? 10.034  -26.236 14.412  1.00 30.03  ? 79  GLU C O   1 
ATOM   2011 C CB  . GLU C 1 80 ? 8.440   -28.653 12.899  1.00 35.85  ? 79  GLU C CB  1 
ATOM   2012 C CG  . GLU C 1 80 ? 7.512   -28.164 14.014  1.00 34.86  ? 79  GLU C CG  1 
ATOM   2013 C CD  . GLU C 1 80 ? 6.258   -28.987 14.246  1.00 45.80  ? 79  GLU C CD  1 
ATOM   2014 O OE1 . GLU C 1 80 ? 6.242   -30.152 13.814  1.00 42.94  ? 79  GLU C OE1 1 
ATOM   2015 O OE2 . GLU C 1 80 ? 5.276   -28.466 14.825  1.00 44.73  ? 79  GLU C OE2 1 
ATOM   2016 N N   . GLY C 1 81 ? 11.442  -27.968 14.029  1.00 30.12  ? 80  GLY C N   1 
ATOM   2017 C CA  . GLY C 1 81 ? 12.326  -27.564 15.121  1.00 28.84  ? 80  GLY C CA  1 
ATOM   2018 C C   . GLY C 1 81 ? 12.931  -26.179 14.884  1.00 29.24  ? 80  GLY C C   1 
ATOM   2019 O O   . GLY C 1 81 ? 13.092  -25.391 15.809  1.00 30.30  ? 80  GLY C O   1 
ATOM   2020 N N   . LEU C 1 82 ? 13.359  -25.914 13.647  1.00 28.82  ? 81  LEU C N   1 
ATOM   2021 C CA  . LEU C 1 82 ? 13.948  -24.609 13.336  1.00 27.71  ? 81  LEU C CA  1 
ATOM   2022 C C   . LEU C 1 82 ? 12.929  -23.492 13.571  1.00 25.92  ? 81  LEU C C   1 
ATOM   2023 O O   . LEU C 1 82 ? 13.307  -22.393 14.025  1.00 30.33  ? 81  LEU C O   1 
ATOM   2024 C CB  . LEU C 1 82 ? 14.416  -24.588 11.878  1.00 29.24  ? 81  LEU C CB  1 
ATOM   2025 C CG  . LEU C 1 82 ? 15.697  -25.355 11.511  1.00 28.59  ? 81  LEU C CG  1 
ATOM   2026 C CD1 . LEU C 1 82 ? 15.926  -25.254 9.998   1.00 29.73  ? 81  LEU C CD1 1 
ATOM   2027 C CD2 . LEU C 1 82 ? 16.979  -24.851 12.187  1.00 28.38  ? 81  LEU C CD2 1 
ATOM   2028 N N   . TRP C 1 83 ? 11.659  -23.757 13.268  1.00 29.15  ? 82  TRP C N   1 
ATOM   2029 C CA  . TRP C 1 83 ? 10.642  -22.731 13.503  1.00 32.94  ? 82  TRP C CA  1 
ATOM   2030 C C   . TRP C 1 83 ? 10.497  -22.449 15.003  1.00 33.57  ? 82  TRP C C   1 
ATOM   2031 O O   . TRP C 1 83 ? 10.520  -21.287 15.413  1.00 34.22  ? 82  TRP C O   1 
ATOM   2032 C CB  . TRP C 1 83 ? 9.299   -23.055 12.834  1.00 31.34  ? 82  TRP C CB  1 
ATOM   2033 C CG  . TRP C 1 83 ? 8.282   -21.945 12.994  1.00 35.53  ? 82  TRP C CG  1 
ATOM   2034 C CD1 . TRP C 1 83 ? 8.023   -20.915 12.129  1.00 35.74  ? 82  TRP C CD1 1 
ATOM   2035 C CD2 . TRP C 1 83 ? 7.376   -21.769 14.108  1.00 34.22  ? 82  TRP C CD2 1 
ATOM   2036 N NE1 . TRP C 1 83 ? 7.026   -20.116 12.621  1.00 36.77  ? 82  TRP C NE1 1 
ATOM   2037 C CE2 . TRP C 1 83 ? 6.610   -20.613 13.831  1.00 36.61  ? 82  TRP C CE2 1 
ATOM   2038 C CE3 . TRP C 1 83 ? 7.158   -22.474 15.306  1.00 35.51  ? 82  TRP C CE3 1 
ATOM   2039 C CZ2 . TRP C 1 83 ? 5.631   -20.159 14.711  1.00 40.27  ? 82  TRP C CZ2 1 
ATOM   2040 C CZ3 . TRP C 1 83 ? 6.195   -22.019 16.181  1.00 41.35  ? 82  TRP C CZ3 1 
ATOM   2041 C CH2 . TRP C 1 83 ? 5.451   -20.870 15.885  1.00 44.78  ? 82  TRP C CH2 1 
ATOM   2042 N N   . GLU C 1 84 ? 10.479  -23.515 15.813  1.00 34.79  ? 83  GLU C N   1 
ATOM   2043 C CA  . GLU C 1 84 ? 10.295  -23.382 17.259  1.00 37.17  ? 83  GLU C CA  1 
ATOM   2044 C C   . GLU C 1 84 ? 11.431  -22.584 17.896  1.00 35.13  ? 83  GLU C C   1 
ATOM   2045 O O   . GLU C 1 84 ? 11.208  -21.724 18.761  1.00 35.65  ? 83  GLU C O   1 
ATOM   2046 C CB  . GLU C 1 84 ? 10.179  -24.741 17.959  1.00 32.94  ? 83  GLU C CB  1 
ATOM   2047 C CG  . GLU C 1 84 ? 8.946   -25.511 17.501  1.00 37.57  ? 83  GLU C CG  1 
ATOM   2048 C CD  . GLU C 1 84 ? 8.853   -26.923 18.022  1.00 40.49  ? 83  GLU C CD  1 
ATOM   2049 O OE1 . GLU C 1 84 ? 9.835   -27.346 18.691  1.00 39.03  ? 83  GLU C OE1 1 
ATOM   2050 O OE2 . GLU C 1 84 ? 7.816   -27.588 17.758  1.00 41.93  ? 83  GLU C OE2 1 
ATOM   2051 N N   . ILE C 1 85 ? 12.674  -22.874 17.488  1.00 32.14  ? 84  ILE C N   1 
ATOM   2052 C CA  . ILE C 1 85 ? 13.823  -22.278 18.144  1.00 33.36  ? 84  ILE C CA  1 
ATOM   2053 C C   . ILE C 1 85 ? 13.900  -20.771 17.890  1.00 36.80  ? 84  ILE C C   1 
ATOM   2054 O O   . ILE C 1 85 ? 14.465  -20.044 18.697  1.00 35.57  ? 84  ILE C O   1 
ATOM   2055 C CB  . ILE C 1 85 ? 15.142  -22.990 17.802  1.00 31.16  ? 84  ILE C CB  1 
ATOM   2056 C CG1 . ILE C 1 85 ? 16.239  -22.514 18.751  1.00 32.16  ? 84  ILE C CG1 1 
ATOM   2057 C CG2 . ILE C 1 85 ? 15.558  -22.833 16.334  1.00 31.80  ? 84  ILE C CG2 1 
ATOM   2058 C CD1 . ILE C 1 85 ? 17.411  -23.465 18.871  1.00 32.20  ? 84  ILE C CD1 1 
ATOM   2059 N N   . GLN C 1 86 ? 13.439  -20.342 16.708  1.00 33.77  ? 85  GLN C N   1 
ATOM   2060 C CA  . GLN C 1 86 ? 13.446  -18.935 16.343  1.00 33.55  ? 85  GLN C CA  1 
ATOM   2061 C C   . GLN C 1 86 ? 12.182  -18.233 16.838  1.00 30.44  ? 85  GLN C C   1 
ATOM   2062 O O   . GLN C 1 86 ? 12.234  -17.053 17.188  1.00 39.04  ? 85  GLN C O   1 
ATOM   2063 C CB  . GLN C 1 86 ? 13.485  -18.865 14.807  1.00 34.53  ? 85  GLN C CB  1 
ATOM   2064 C CG  . GLN C 1 86 ? 13.707  -17.451 14.265  1.00 36.85  ? 85  GLN C CG  1 
ATOM   2065 C CD  . GLN C 1 86 ? 14.199  -17.448 12.827  1.00 38.47  ? 85  GLN C CD  1 
ATOM   2066 O OE1 . GLN C 1 86 ? 14.095  -18.448 12.102  1.00 36.09  ? 85  GLN C OE1 1 
ATOM   2067 N NE2 . GLN C 1 86 ? 14.790  -16.339 12.410  1.00 37.82  ? 85  GLN C NE2 1 
ATOM   2068 N N   . ASN C 1 87 ? 11.056  -18.951 16.871  1.00 34.91  ? 86  ASN C N   1 
ATOM   2069 C CA  . ASN C 1 87 ? 9.743   -18.326 16.989  1.00 42.49  ? 86  ASN C CA  1 
ATOM   2070 C C   . ASN C 1 87 ? 9.039   -18.656 18.311  1.00 41.99  ? 86  ASN C C   1 
ATOM   2071 O O   . ASN C 1 87 ? 8.219   -17.862 18.741  1.00 43.87  ? 86  ASN C O   1 
ATOM   2072 C CB  . ASN C 1 87 ? 8.845   -18.617 15.791  1.00 39.16  ? 86  ASN C CB  1 
ATOM   2073 C CG  . ASN C 1 87 ? 9.458   -18.017 14.545  1.00 42.15  ? 86  ASN C CG  1 
ATOM   2074 O OD1 . ASN C 1 87 ? 9.508   -16.790 14.438  1.00 40.15  ? 86  ASN C OD1 1 
ATOM   2075 N ND2 . ASN C 1 87 ? 10.011  -18.842 13.660  1.00 37.56  ? 86  ASN C ND2 1 
ATOM   2076 N N   . ASN C 1 88 ? 9.305   -19.815 18.936  1.00 42.66  ? 87  ASN C N   1 
ATOM   2077 C CA  . ASN C 1 88 ? 8.553   -20.182 20.140  1.00 38.86  ? 87  ASN C CA  1 
ATOM   2078 C C   . ASN C 1 88 ? 9.406   -21.059 21.055  1.00 40.37  ? 87  ASN C C   1 
ATOM   2079 O O   . ASN C 1 88 ? 9.011   -22.184 21.374  1.00 44.37  ? 87  ASN C O   1 
ATOM   2080 C CB  . ASN C 1 88 ? 7.305   -20.987 19.787  1.00 41.76  ? 87  ASN C CB  1 
ATOM   2081 C CG  . ASN C 1 88 ? 6.273   -20.984 20.893  1.00 49.54  ? 87  ASN C CG  1 
ATOM   2082 O OD1 . ASN C 1 88 ? 6.333   -20.141 21.794  1.00 47.01  ? 87  ASN C OD1 1 
ATOM   2083 N ND2 . ASN C 1 88 ? 5.311   -21.895 20.825  1.00 49.82  ? 87  ASN C ND2 1 
ATOM   2084 N N   . PRO C 1 89 ? 10.609  -20.595 21.461  1.00 36.31  ? 88  PRO C N   1 
ATOM   2085 C CA  . PRO C 1 89 ? 11.624  -21.478 22.041  1.00 39.77  ? 88  PRO C CA  1 
ATOM   2086 C C   . PRO C 1 89 ? 11.425  -21.924 23.485  1.00 43.81  ? 88  PRO C C   1 
ATOM   2087 O O   . PRO C 1 89 ? 12.210  -22.748 23.972  1.00 42.58  ? 88  PRO C O   1 
ATOM   2088 C CB  . PRO C 1 89 ? 12.912  -20.688 21.942  1.00 34.49  ? 88  PRO C CB  1 
ATOM   2089 C CG  . PRO C 1 89 ? 12.471  -19.262 21.885  1.00 37.71  ? 88  PRO C CG  1 
ATOM   2090 C CD  . PRO C 1 89 ? 11.090  -19.217 21.293  1.00 36.48  ? 88  PRO C CD  1 
ATOM   2091 N N   . HIS C 1 90 ? 10.411  -21.340 24.140  1.00 48.90  ? 89  HIS C N   1 
ATOM   2092 C CA  . HIS C 1 90 ? 10.193  -21.565 25.561  1.00 45.80  ? 89  HIS C CA  1 
ATOM   2093 C C   . HIS C 1 90 ? 8.762   -22.015 25.826  1.00 51.11  ? 89  HIS C C   1 
ATOM   2094 O O   . HIS C 1 90 ? 8.324   -22.006 26.970  1.00 53.37  ? 89  HIS C O   1 
ATOM   2095 C CB  . HIS C 1 90 ? 10.705  -20.385 26.399  1.00 43.59  ? 89  HIS C CB  1 
ATOM   2096 C CG  . HIS C 1 90 ? 12.183  -20.137 26.287  1.00 42.42  ? 89  HIS C CG  1 
ATOM   2097 N ND1 . HIS C 1 90 ? 12.673  -18.918 25.864  1.00 44.90  ? 89  HIS C ND1 1 
ATOM   2098 C CD2 . HIS C 1 90 ? 13.272  -20.911 26.487  1.00 41.83  ? 89  HIS C CD2 1 
ATOM   2099 C CE1 . HIS C 1 90 ? 14.002  -18.935 25.830  1.00 39.41  ? 89  HIS C CE1 1 
ATOM   2100 N NE2 . HIS C 1 90 ? 14.393  -20.134 26.226  1.00 41.49  ? 89  HIS C NE2 1 
ATOM   2101 N N   . ALA C 1 91 ? 8.043   -22.426 24.775  1.00 53.31  ? 90  ALA C N   1 
ATOM   2102 C CA  . ALA C 1 91 ? 6.797   -23.158 24.954  1.00 59.54  ? 90  ALA C CA  1 
ATOM   2103 C C   . ALA C 1 91 ? 7.106   -24.552 25.511  1.00 66.05  ? 90  ALA C C   1 
ATOM   2104 O O   . ALA C 1 91 ? 8.246   -25.013 25.429  1.00 67.94  ? 90  ALA C O   1 
ATOM   2105 C CB  . ALA C 1 91 ? 6.018   -23.211 23.649  1.00 57.16  ? 90  ALA C CB  1 
ATOM   2106 N N   . SER C 1 92 ? 6.079   -25.224 26.055  1.00 74.58  ? 91  SER C N   1 
ATOM   2107 C CA  . SER C 1 92 ? 6.234   -26.423 26.872  1.00 74.21  ? 91  SER C CA  1 
ATOM   2108 C C   . SER C 1 92 ? 6.361   -27.687 26.024  1.00 73.06  ? 91  SER C C   1 
ATOM   2109 O O   . SER C 1 92 ? 7.051   -28.627 26.419  1.00 71.63  ? 91  SER C O   1 
ATOM   2110 C CB  . SER C 1 92 ? 5.086   -26.560 27.845  1.00 77.45  ? 91  SER C CB  1 
ATOM   2111 O OG  . SER C 1 92 ? 5.071   -25.473 28.759  1.00 75.12  ? 91  SER C OG  1 
ATOM   2112 N N   . TYR C 1 93 ? 5.643   -27.709 24.893  1.00 75.03  ? 92  TYR C N   1 
ATOM   2113 C CA  . TYR C 1 93 ? 5.549   -28.857 24.001  1.00 75.71  ? 92  TYR C CA  1 
ATOM   2114 C C   . TYR C 1 93 ? 5.344   -30.135 24.831  1.00 80.05  ? 92  TYR C C   1 
ATOM   2115 O O   . TYR C 1 93 ? 5.218   -31.218 24.217  1.00 86.91  ? 92  TYR C O   1 
ATOM   2116 C CB  . TYR C 1 93 ? 6.741   -28.929 23.038  1.00 70.61  ? 92  TYR C CB  1 
ATOM   2117 C CG  . TYR C 1 93 ? 6.992   -27.653 22.239  1.00 63.39  ? 92  TYR C CG  1 
ATOM   2118 C CD1 . TYR C 1 93 ? 6.185   -27.316 21.155  1.00 55.86  ? 92  TYR C CD1 1 
ATOM   2119 C CD2 . TYR C 1 93 ? 8.042   -26.796 22.557  1.00 58.00  ? 92  TYR C CD2 1 
ATOM   2120 C CE1 . TYR C 1 93 ? 6.397   -26.158 20.430  1.00 50.36  ? 92  TYR C CE1 1 
ATOM   2121 C CE2 . TYR C 1 93 ? 8.279   -25.643 21.823  1.00 51.47  ? 92  TYR C CE2 1 
ATOM   2122 C CZ  . TYR C 1 93 ? 7.446   -25.318 20.769  1.00 51.65  ? 92  TYR C CZ  1 
ATOM   2123 O OH  . TYR C 1 93 ? 7.679   -24.171 20.062  1.00 50.30  ? 92  TYR C OH  1 
HETATM 2124 S S   . SO4 D 2 .  ? 1.282   -33.832 1.593   1.00 83.14  ? 101 SO4 A S   1 
HETATM 2125 O O1  . SO4 D 2 .  ? 1.723   -34.221 0.276   1.00 68.40  ? 101 SO4 A O1  1 
HETATM 2126 O O2  . SO4 D 2 .  ? 1.265   -32.394 1.692   1.00 73.44  ? 101 SO4 A O2  1 
HETATM 2127 O O3  . SO4 D 2 .  ? -0.044  -34.353 1.827   1.00 88.68  ? 101 SO4 A O3  1 
HETATM 2128 O O4  . SO4 D 2 .  ? 2.179   -34.364 2.582   1.00 84.35  ? 101 SO4 A O4  1 
HETATM 2129 S S   . SO4 E 2 .  ? -9.808  -24.553 0.994   1.00 99.54  ? 102 SO4 A S   1 
HETATM 2130 O O1  . SO4 E 2 .  ? -9.686  -24.490 -0.438  1.00 100.96 ? 102 SO4 A O1  1 
HETATM 2131 O O2  . SO4 E 2 .  ? -10.243 -23.275 1.495   1.00 106.88 ? 102 SO4 A O2  1 
HETATM 2132 O O3  . SO4 E 2 .  ? -10.774 -25.567 1.340   1.00 105.98 ? 102 SO4 A O3  1 
HETATM 2133 O O4  . SO4 E 2 .  ? -8.536  -24.882 1.580   1.00 96.30  ? 102 SO4 A O4  1 
HETATM 2134 C C1  . EDO F 3 .  ? 13.831  -19.460 -7.371  1.00 42.04  ? 103 EDO A C1  1 
HETATM 2135 O O1  . EDO F 3 .  ? 15.034  -18.704 -7.302  1.00 34.21  ? 103 EDO A O1  1 
HETATM 2136 C C2  . EDO F 3 .  ? 12.953  -19.002 -8.519  1.00 37.39  ? 103 EDO A C2  1 
HETATM 2137 O O2  . EDO F 3 .  ? 12.407  -17.698 -8.340  1.00 33.99  ? 103 EDO A O2  1 
HETATM 2138 S S   . SO4 G 2 .  ? 8.940   -29.371 5.687   1.00 54.08  ? 104 SO4 A S   1 
HETATM 2139 O O1  . SO4 G 2 .  ? 9.806   -28.719 4.791   1.00 50.33  ? 104 SO4 A O1  1 
HETATM 2140 O O2  . SO4 G 2 .  ? 8.408   -30.553 5.048   1.00 66.99  ? 104 SO4 A O2  1 
HETATM 2141 O O3  . SO4 G 2 .  ? 9.664   -29.762 6.878   1.00 61.80  ? 104 SO4 A O3  1 
HETATM 2142 O O4  . SO4 G 2 .  ? 7.848   -28.501 6.033   1.00 69.34  ? 104 SO4 A O4  1 
HETATM 2143 S S   . SO4 H 2 .  ? 7.273   -8.606  -24.827 1.00 63.76  ? 101 SO4 B S   1 
HETATM 2144 O O1  . SO4 H 2 .  ? 8.446   -8.686  -25.678 1.00 42.81  ? 101 SO4 B O1  1 
HETATM 2145 O O2  . SO4 H 2 .  ? 6.147   -9.203  -25.472 1.00 49.26  ? 101 SO4 B O2  1 
HETATM 2146 O O3  . SO4 H 2 .  ? 7.447   -9.304  -23.571 1.00 41.54  ? 101 SO4 B O3  1 
HETATM 2147 O O4  . SO4 H 2 .  ? 7.052   -7.202  -24.578 1.00 57.09  ? 101 SO4 B O4  1 
HETATM 2148 S S   . SO4 I 2 .  ? 14.370  -27.068 -26.306 1.00 59.06  ? 102 SO4 B S   1 
HETATM 2149 O O1  . SO4 I 2 .  ? 15.709  -26.758 -25.932 1.00 52.09  ? 102 SO4 B O1  1 
HETATM 2150 O O2  . SO4 I 2 .  ? 14.352  -28.342 -26.975 1.00 65.51  ? 102 SO4 B O2  1 
HETATM 2151 O O3  . SO4 I 2 .  ? 13.548  -27.125 -25.131 1.00 67.16  ? 102 SO4 B O3  1 
HETATM 2152 O O4  . SO4 I 2 .  ? 13.853  -26.054 -27.196 1.00 59.80  ? 102 SO4 B O4  1 
HETATM 2153 N N1  . NW4 J 4 .  ? 18.240  -16.147 -23.068 0.60 47.09  ? 103 NW4 B N1  1 
HETATM 2154 C C4  . NW4 J 4 .  ? 21.753  -17.346 -21.282 0.60 58.70  ? 103 NW4 B C4  1 
HETATM 2155 C C5  . NW4 J 4 .  ? 22.104  -17.704 -19.836 0.60 58.48  ? 103 NW4 B C5  1 
HETATM 2156 C C6  . NW4 J 4 .  ? 23.219  -16.831 -19.259 0.60 60.83  ? 103 NW4 B C6  1 
HETATM 2157 C C7  . NW4 J 4 .  ? 24.464  -16.852 -20.139 0.60 65.07  ? 103 NW4 B C7  1 
HETATM 2158 C C8  . NW4 J 4 .  ? 24.124  -16.461 -21.569 0.60 61.06  ? 103 NW4 B C8  1 
HETATM 2159 C C10 . NW4 J 4 .  ? 18.548  -16.794 -24.351 0.60 40.82  ? 103 NW4 B C10 1 
HETATM 2160 C C13 . NW4 J 4 .  ? 17.441  -14.915 -23.162 0.60 47.44  ? 103 NW4 B C13 1 
HETATM 2161 C C1  . NW4 J 4 .  ? 18.766  -16.559 -21.885 0.60 54.93  ? 103 NW4 B C1  1 
HETATM 2162 C C11 . NW4 J 4 .  ? 17.342  -16.818 -25.249 0.60 38.30  ? 103 NW4 B C11 1 
HETATM 2163 C C12 . NW4 J 4 .  ? 16.302  -15.087 -24.130 0.60 45.36  ? 103 NW4 B C12 1 
HETATM 2164 C C2  . NW4 J 4 .  ? 19.208  -17.999 -21.748 0.60 54.10  ? 103 NW4 B C2  1 
HETATM 2165 C C3  . NW4 J 4 .  ? 20.707  -18.319 -21.859 0.60 54.03  ? 103 NW4 B C3  1 
HETATM 2166 C C9  . NW4 J 4 .  ? 23.022  -17.349 -22.137 0.60 58.23  ? 103 NW4 B C9  1 
HETATM 2167 O O1  . NW4 J 4 .  ? 18.885  -15.809 -20.931 0.60 61.03  ? 103 NW4 B O1  1 
HETATM 2168 O O2  . NW4 J 4 .  ? 16.763  -15.527 -25.396 0.60 45.03  ? 103 NW4 B O2  1 
HETATM 2169 C C1  . EDO K 3 .  ? 16.686  -36.145 16.445  1.00 41.72  ? 101 EDO C C1  1 
HETATM 2170 O O1  . EDO K 3 .  ? 15.687  -36.919 15.788  1.00 47.70  ? 101 EDO C O1  1 
HETATM 2171 C C2  . EDO K 3 .  ? 16.176  -35.182 17.476  1.00 35.32  ? 101 EDO C C2  1 
HETATM 2172 O O2  . EDO K 3 .  ? 15.227  -35.730 18.355  1.00 34.08  ? 101 EDO C O2  1 
HETATM 2173 S S   . SO4 L 2 .  ? 28.723  -38.192 12.197  1.00 83.13  ? 102 SO4 C S   1 
HETATM 2174 O O1  . SO4 L 2 .  ? 29.747  -37.188 12.052  1.00 87.66  ? 102 SO4 C O1  1 
HETATM 2175 O O2  . SO4 L 2 .  ? 27.708  -38.011 11.177  1.00 72.89  ? 102 SO4 C O2  1 
HETATM 2176 O O3  . SO4 L 2 .  ? 29.310  -39.497 12.057  1.00 60.86  ? 102 SO4 C O3  1 
HETATM 2177 O O4  . SO4 L 2 .  ? 28.135  -38.074 13.507  1.00 94.77  ? 102 SO4 C O4  1 
HETATM 2178 O O   . HOH M 5 .  ? 8.395   -32.070 4.071   1.00 52.92  ? 201 HOH A O   1 
HETATM 2179 O O   . HOH M 5 .  ? 3.806   -34.490 4.165   1.00 57.26  ? 202 HOH A O   1 
HETATM 2180 O O   . HOH M 5 .  ? 10.846  -29.578 2.959   1.00 44.10  ? 203 HOH A O   1 
HETATM 2181 O O   . HOH M 5 .  ? 5.650   -29.081 6.697   1.00 50.27  ? 204 HOH A O   1 
HETATM 2182 O O   . HOH M 5 .  ? -5.863  -13.534 -16.399 1.00 53.84  ? 205 HOH A O   1 
HETATM 2183 O O   . HOH M 5 .  ? 1.011   -24.719 13.738  1.00 58.10  ? 206 HOH A O   1 
HETATM 2184 O O   . HOH M 5 .  ? -2.538  3.040   -1.959  1.00 43.03  ? 207 HOH A O   1 
HETATM 2185 O O   . HOH M 5 .  ? -3.936  -11.044 6.916   1.00 42.46  ? 208 HOH A O   1 
HETATM 2186 O O   . HOH M 5 .  ? 8.875   -17.986 -11.057 1.00 35.79  ? 209 HOH A O   1 
HETATM 2187 O O   . HOH M 5 .  ? 9.284   -5.959  -1.545  1.00 38.15  ? 210 HOH A O   1 
HETATM 2188 O O   . HOH M 5 .  ? 15.662  -24.483 2.042   1.00 40.54  ? 211 HOH A O   1 
HETATM 2189 O O   . HOH M 5 .  ? 10.694  -5.174  -7.655  1.00 35.33  ? 212 HOH A O   1 
HETATM 2190 O O   . HOH M 5 .  ? 9.233   -22.604 -9.522  1.00 38.72  ? 213 HOH A O   1 
HETATM 2191 O O   . HOH M 5 .  ? -7.897  -17.225 6.607   1.00 46.91  ? 214 HOH A O   1 
HETATM 2192 O O   . HOH M 5 .  ? -3.002  -30.665 -3.553  1.00 65.25  ? 215 HOH A O   1 
HETATM 2193 O O   . HOH M 5 .  ? 7.908   -17.673 -15.679 1.00 54.05  ? 216 HOH A O   1 
HETATM 2194 O O   . HOH M 5 .  ? 0.339   -10.511 -15.666 1.00 60.55  ? 217 HOH A O   1 
HETATM 2195 O O   . HOH M 5 .  ? 10.818  -23.690 9.789   1.00 36.34  ? 218 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? 16.934  -18.110 -9.655  1.00 50.93  ? 219 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? -0.794  -29.474 9.698   1.00 60.97  ? 220 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? 0.077   -33.706 4.435   1.00 53.86  ? 221 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? 12.792  -9.514  -7.132  1.00 45.64  ? 222 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? -6.890  -5.417  9.270   1.00 39.15  ? 223 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 6.893   -10.252 -12.083 1.00 46.71  ? 224 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 11.330  -11.972 5.887   1.00 39.46  ? 225 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? -0.948  -21.057 6.824   1.00 34.89  ? 226 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 19.650  -15.586 7.311   1.00 30.36  ? 227 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 13.183  -11.549 7.896   1.00 51.85  ? 228 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 4.336   -3.413  -3.159  1.00 36.80  ? 229 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 9.916   -13.176 9.572   1.00 40.69  ? 230 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? -4.496  -21.274 6.007   1.00 41.51  ? 231 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? -4.845  -25.836 -5.604  1.00 47.58  ? 232 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? -8.235  -15.792 -1.027  1.00 37.08  ? 233 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? -1.880  -21.999 -0.682  1.00 29.59  ? 234 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 4.436   -7.756  1.203   1.00 37.47  ? 235 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 2.446   -25.204 -10.094 1.00 40.27  ? 236 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 13.237  -27.925 -5.014  1.00 56.66  ? 237 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? -0.954  -20.583 11.363  1.00 62.69  ? 238 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? -8.065  -16.695 1.757   1.00 42.15  ? 239 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? -8.671  -21.073 -1.327  1.00 49.50  ? 240 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 15.567  -12.009 -5.316  1.00 35.78  ? 241 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -6.348  -11.324 -11.301 1.00 40.71  ? 242 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 2.333   -25.231 -6.611  1.00 54.42  ? 243 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 6.259   -15.820 -14.992 1.00 45.32  ? 244 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 1.727   -4.602  -10.200 1.00 36.66  ? 245 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 16.222  -11.322 -17.247 1.00 45.69  ? 246 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 3.155   -29.602 -0.658  1.00 38.76  ? 247 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 13.144  -11.943 -4.248  1.00 23.18  ? 248 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 1.730   0.589   -7.538  1.00 44.16  ? 249 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? -5.885  -15.820 -8.192  1.00 31.50  ? 250 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -1.521  -7.559  11.421  1.00 49.86  ? 251 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -11.605 -15.927 -4.069  1.00 58.57  ? 252 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 8.241   -17.836 8.802   1.00 45.93  ? 253 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 11.368  -12.312 -6.179  1.00 27.37  ? 254 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 17.012  -12.835 1.368   1.00 21.60  ? 255 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? -5.929  -19.655 -5.730  1.00 40.86  ? 256 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 0.048   -23.321 9.045   1.00 41.61  ? 257 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 11.141  -5.965  -3.805  1.00 45.30  ? 258 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 15.187  -28.149 -0.642  1.00 56.66  ? 259 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 2.166   -6.211  5.469   1.00 32.10  ? 260 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? -7.427  -21.586 -5.924  1.00 59.80  ? 261 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 7.631   -7.819  1.317   1.00 31.64  ? 262 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 1.576   -10.490 11.686  1.00 35.91  ? 263 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 6.044   -5.857  0.394   1.00 65.45  ? 264 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 1.602   -18.599 -18.518 1.00 49.55  ? 265 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? -4.156  -7.908  10.437  1.00 54.79  ? 266 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -6.252  -12.785 6.643   1.00 42.61  ? 267 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -1.484  -11.862 11.365  1.00 39.91  ? 268 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 4.959   -7.602  3.972   1.00 35.80  ? 269 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 2.907   -9.840  -13.285 1.00 43.86  ? 270 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 8.699   -16.197 -13.322 1.00 45.28  ? 271 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 12.596  -13.228 -8.515  1.00 42.62  ? 272 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 9.387   -30.509 9.834   1.00 37.19  ? 273 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 10.892  -7.800  0.429   1.00 27.12  ? 274 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 12.936  -14.923 -12.169 1.00 50.77  ? 275 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 22.087  -16.630 -0.454  1.00 38.09  ? 276 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 14.566  -13.359 10.592  1.00 50.52  ? 277 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 9.214   -2.316  -0.359  1.00 63.85  ? 278 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -7.463  -11.437 -8.058  1.00 30.27  ? 279 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 21.227  -16.591 -3.446  1.00 30.53  ? 280 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 9.760   -20.259 -18.354 1.00 45.05  ? 281 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 9.561   -27.771 -7.650  1.00 61.61  ? 282 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? -6.171  -26.681 3.300   1.00 47.00  ? 283 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 8.612   -8.967  -13.709 1.00 45.33  ? 284 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -0.496  -8.229  -13.363 1.00 49.32  ? 285 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -8.313  -19.728 -3.529  1.00 49.41  ? 286 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -4.114  -27.041 6.726   1.00 52.93  ? 287 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? -7.419  -14.157 -9.228  1.00 40.61  ? 288 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? -10.822 -27.741 -1.603  1.00 72.49  ? 289 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? -4.077  -11.188 9.633   1.00 49.13  ? 290 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 4.896   -7.063  -10.940 1.00 49.46  ? 291 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -5.882  -23.489 -7.216  1.00 43.79  ? 292 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? -9.633  -19.117 1.417   1.00 52.25  ? 293 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -11.381 -13.395 -2.705  1.00 49.55  ? 294 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 4.622   -9.580  -11.417 1.00 55.20  ? 295 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 7.909   -8.176  4.535   1.00 43.68  ? 296 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -6.329  -23.111 5.397   1.00 51.54  ? 297 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 7.789   -30.670 -1.842  1.00 56.62  ? 298 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 5.828   -3.261  1.145   1.00 51.97  ? 299 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -7.257  -19.326 8.290   1.00 55.93  ? 300 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 8.911   -22.201 -19.180 1.00 65.25  ? 301 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? -5.296  -21.014 -8.067  1.00 53.85  ? 302 HOH A O   1 
HETATM 2280 O O   . HOH N 5 .  ? 31.525  -8.340  -30.217 1.00 61.45  ? 201 HOH B O   1 
HETATM 2281 O O   . HOH N 5 .  ? 25.773  -0.747  -28.960 1.00 53.41  ? 202 HOH B O   1 
HETATM 2282 O O   . HOH N 5 .  ? 10.387  -16.740 -44.285 1.00 43.31  ? 203 HOH B O   1 
HETATM 2283 O O   . HOH N 5 .  ? 27.649  -8.177  -28.606 1.00 48.79  ? 204 HOH B O   1 
HETATM 2284 O O   . HOH N 5 .  ? 6.541   -12.301 -25.970 1.00 43.45  ? 205 HOH B O   1 
HETATM 2285 O O   . HOH N 5 .  ? 30.375  -12.893 -45.440 1.00 61.57  ? 206 HOH B O   1 
HETATM 2286 O O   . HOH N 5 .  ? 10.190  -11.599 -38.039 1.00 54.42  ? 207 HOH B O   1 
HETATM 2287 O O   . HOH N 5 .  ? 19.835  -1.269  -23.023 1.00 81.32  ? 208 HOH B O   1 
HETATM 2288 O O   . HOH N 5 .  ? 34.968  -23.284 -30.244 1.00 72.51  ? 209 HOH B O   1 
HETATM 2289 O O   . HOH N 5 .  ? 24.766  -5.482  -29.598 1.00 40.86  ? 210 HOH B O   1 
HETATM 2290 O O   . HOH N 5 .  ? 6.251   -7.471  -32.359 1.00 46.94  ? 211 HOH B O   1 
HETATM 2291 O O   . HOH N 5 .  ? 30.292  -19.730 -40.013 1.00 43.60  ? 212 HOH B O   1 
HETATM 2292 O O   . HOH N 5 .  ? 13.681  -5.081  -41.283 1.00 64.28  ? 213 HOH B O   1 
HETATM 2293 O O   . HOH N 5 .  ? 19.932  -21.870 -22.875 1.00 50.78  ? 214 HOH B O   1 
HETATM 2294 O O   . HOH N 5 .  ? 27.575  -17.867 -24.870 1.00 46.55  ? 215 HOH B O   1 
HETATM 2295 O O   . HOH N 5 .  ? 26.054  -4.908  -33.403 1.00 49.79  ? 216 HOH B O   1 
HETATM 2296 O O   . HOH N 5 .  ? 25.478  -6.171  -35.563 1.00 50.34  ? 217 HOH B O   1 
HETATM 2297 O O   . HOH N 5 .  ? 10.321  -19.854 -42.947 1.00 51.22  ? 218 HOH B O   1 
HETATM 2298 O O   . HOH N 5 .  ? 24.506  -2.082  -35.730 1.00 50.72  ? 219 HOH B O   1 
HETATM 2299 O O   . HOH N 5 .  ? 19.862  -25.755 -34.025 1.00 44.14  ? 220 HOH B O   1 
HETATM 2300 O O   . HOH N 5 .  ? 20.927  -26.747 -30.350 1.00 51.04  ? 221 HOH B O   1 
HETATM 2301 O O   . HOH N 5 .  ? 23.485  -2.554  -28.791 1.00 43.94  ? 222 HOH B O   1 
HETATM 2302 O O   . HOH N 5 .  ? 8.526   -8.577  -16.469 1.00 48.74  ? 223 HOH B O   1 
HETATM 2303 O O   . HOH N 5 .  ? 21.099  -13.634 -42.335 1.00 40.95  ? 224 HOH B O   1 
HETATM 2304 O O   . HOH N 5 .  ? 16.686  -19.328 -28.640 1.00 28.05  ? 225 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 8.264   -27.830 -38.388 1.00 58.46  ? 226 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 22.457  -23.351 -28.573 1.00 42.94  ? 227 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 21.574  3.472   -32.505 1.00 41.48  ? 228 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 26.133  -23.334 -30.929 1.00 38.08  ? 229 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 17.489  -19.843 -41.975 1.00 66.84  ? 230 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 10.455  -18.995 -32.848 1.00 29.91  ? 231 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 18.307  -0.641  -38.289 1.00 29.12  ? 232 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 7.650   -18.572 -31.525 1.00 46.45  ? 233 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 12.458  -22.178 -20.511 1.00 56.33  ? 234 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 1.902   -12.938 -28.174 1.00 47.93  ? 235 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 20.702  -10.189 -42.669 1.00 39.65  ? 236 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 14.693  -6.877  -41.167 1.00 45.81  ? 237 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 31.456  -12.311 -38.482 1.00 62.36  ? 238 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 18.003  -15.704 -45.575 1.00 40.55  ? 239 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 14.652  -24.556 -40.321 1.00 50.23  ? 240 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 21.316  -6.705  -42.331 1.00 41.19  ? 241 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 23.833  -4.374  -36.514 1.00 31.17  ? 242 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 7.799   -23.388 -24.114 1.00 49.06  ? 243 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 23.781  -11.850 -21.587 1.00 47.50  ? 244 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 7.104   -19.399 -34.764 1.00 46.43  ? 245 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 18.181  -26.162 -28.702 1.00 44.93  ? 246 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 22.166  -4.685  -24.128 1.00 65.60  ? 247 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 7.556   -12.539 -39.034 1.00 58.96  ? 248 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 2.948   -8.379  -27.090 1.00 54.10  ? 249 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 7.387   -8.026  -20.798 1.00 54.64  ? 250 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 9.609   -0.422  -40.954 1.00 52.05  ? 251 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 32.758  -18.696 -41.383 1.00 67.19  ? 252 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 27.179  -10.578 -28.649 1.00 50.44  ? 253 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 10.437  -21.883 -32.591 1.00 42.77  ? 254 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 25.051  -6.645  -42.298 1.00 53.05  ? 255 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 15.400  -8.560  -42.971 1.00 49.47  ? 256 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 17.151  -24.875 -20.688 1.00 70.38  ? 257 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 18.503  4.464   -34.130 1.00 45.12  ? 258 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 6.130   -20.356 -25.013 1.00 41.32  ? 259 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 27.977  -25.081 -34.828 1.00 38.06  ? 260 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 17.548  -9.641  -43.669 1.00 52.80  ? 261 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 12.897  -20.020 -19.538 1.00 54.81  ? 262 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 9.993   -6.261  -41.084 1.00 51.29  ? 263 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 17.780  -0.340  -25.485 1.00 51.42  ? 264 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 20.034  3.820   -32.926 1.00 45.42  ? 265 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 39.456  -13.304 -39.201 1.00 79.19  ? 266 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 11.129  -23.818 -29.716 1.00 55.60  ? 267 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 15.452  -21.885 -41.794 1.00 56.73  ? 268 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 7.263   -9.767  -18.581 1.00 53.55  ? 269 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 29.255  -17.574 -47.609 1.00 48.12  ? 270 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 22.052  -29.487 -35.481 1.00 48.20  ? 271 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 16.688  3.083   -26.636 1.00 60.57  ? 272 HOH B O   1 
HETATM 2352 O O   . HOH O 5 .  ? 26.337  -39.032 12.711  1.00 40.79  ? 201 HOH C O   1 
HETATM 2353 O O   . HOH O 5 .  ? 12.227  -28.083 28.044  1.00 53.93  ? 202 HOH C O   1 
HETATM 2354 O O   . HOH O 5 .  ? 8.854   -36.801 18.385  1.00 55.66  ? 203 HOH C O   1 
HETATM 2355 O O   . HOH O 5 .  ? 19.516  -20.879 30.651  1.00 72.10  ? 204 HOH C O   1 
HETATM 2356 O O   . HOH O 5 .  ? 7.329   -31.648 12.185  1.00 49.06  ? 205 HOH C O   1 
HETATM 2357 O O   . HOH O 5 .  ? 5.567   -26.678 16.580  1.00 44.75  ? 206 HOH C O   1 
HETATM 2358 O O   . HOH O 5 .  ? 23.005  -41.362 18.540  1.00 43.83  ? 207 HOH C O   1 
HETATM 2359 O O   . HOH O 5 .  ? 30.162  -17.904 9.426   1.00 44.19  ? 208 HOH C O   1 
HETATM 2360 O O   . HOH O 5 .  ? 14.726  -20.992 12.203  1.00 39.22  ? 209 HOH C O   1 
HETATM 2361 O O   . HOH O 5 .  ? 30.051  -31.106 15.840  1.00 49.69  ? 210 HOH C O   1 
HETATM 2362 O O   . HOH O 5 .  ? 19.856  -41.721 12.279  1.00 33.87  ? 211 HOH C O   1 
HETATM 2363 O O   . HOH O 5 .  ? 20.890  -36.027 7.588   1.00 75.04  ? 212 HOH C O   1 
HETATM 2364 O O   . HOH O 5 .  ? 18.973  -20.076 10.543  1.00 42.06  ? 213 HOH C O   1 
HETATM 2365 O O   . HOH O 5 .  ? 17.213  -16.942 14.744  1.00 51.89  ? 214 HOH C O   1 
HETATM 2366 O O   . HOH O 5 .  ? 25.462  -19.594 6.254   1.00 36.89  ? 215 HOH C O   1 
HETATM 2367 O O   . HOH O 5 .  ? 13.964  -37.063 13.724  1.00 42.12  ? 216 HOH C O   1 
HETATM 2368 O O   . HOH O 5 .  ? 31.596  -33.031 25.971  1.00 48.62  ? 217 HOH C O   1 
HETATM 2369 O O   . HOH O 5 .  ? 22.072  -28.422 11.124  1.00 31.47  ? 218 HOH C O   1 
HETATM 2370 O O   . HOH O 5 .  ? 12.541  -31.512 8.321   1.00 35.91  ? 219 HOH C O   1 
HETATM 2371 O O   . HOH O 5 .  ? 21.947  -34.216 16.605  1.00 29.12  ? 220 HOH C O   1 
HETATM 2372 O O   . HOH O 5 .  ? 25.126  -31.221 10.784  1.00 36.97  ? 221 HOH C O   1 
HETATM 2373 O O   . HOH O 5 .  ? 28.097  -37.131 16.070  1.00 42.86  ? 222 HOH C O   1 
HETATM 2374 O O   . HOH O 5 .  ? 18.977  -26.725 3.161   1.00 52.95  ? 223 HOH C O   1 
HETATM 2375 O O   . HOH O 5 .  ? 20.660  -28.616 8.555   1.00 36.96  ? 224 HOH C O   1 
HETATM 2376 O O   . HOH O 5 .  ? 25.726  -17.443 13.717  1.00 47.96  ? 225 HOH C O   1 
HETATM 2377 O O   . HOH O 5 .  ? 16.196  -37.790 19.990  1.00 49.42  ? 226 HOH C O   1 
HETATM 2378 O O   . HOH O 5 .  ? 25.727  -33.608 34.731  1.00 55.29  ? 227 HOH C O   1 
HETATM 2379 O O   . HOH O 5 .  ? 20.579  -39.780 26.380  1.00 45.29  ? 228 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 27.569  -37.624 25.005  1.00 53.93  ? 229 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 6.638   -17.963 10.839  1.00 39.05  ? 230 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 30.361  -35.643 28.736  1.00 51.00  ? 231 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 29.721  -39.570 31.331  1.00 38.03  ? 232 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 15.385  -17.413 19.363  1.00 42.71  ? 233 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 25.319  -39.594 20.144  1.00 36.52  ? 234 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 31.076  -39.690 27.046  1.00 47.71  ? 235 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 31.680  -43.209 12.124  1.00 54.86  ? 236 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 27.502  -15.307 12.758  1.00 60.07  ? 237 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 22.615  -18.412 21.782  1.00 53.56  ? 238 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 19.592  -18.880 24.790  1.00 41.85  ? 239 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 14.232  -29.373 4.023   1.00 38.11  ? 240 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 31.047  -43.436 15.773  1.00 65.25  ? 241 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 14.829  -39.541 17.033  1.00 52.62  ? 242 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 4.538   -23.770 18.582  1.00 63.86  ? 243 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 20.965  -29.423 4.580   1.00 56.24  ? 244 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 8.517   -18.959 23.601  1.00 53.88  ? 245 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 2.458   -28.720 13.609  1.00 58.46  ? 246 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 25.240  -36.297 10.426  1.00 53.52  ? 247 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 14.148  -38.884 9.497   1.00 56.41  ? 248 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 29.741  -25.321 32.634  1.00 56.40  ? 249 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 30.037  -32.495 18.268  1.00 43.23  ? 250 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 25.006  -17.497 21.370  1.00 62.90  ? 251 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 15.661  -19.188 29.236  1.00 60.37  ? 252 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 20.262  -40.941 38.939  1.00 68.15  ? 253 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 17.500  -36.418 29.472  1.00 63.82  ? 254 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 28.982  -41.388 27.071  1.00 41.77  ? 255 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 11.760  -21.157 10.689  1.00 37.35  ? 256 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 22.294  -13.580 13.169  1.00 51.24  ? 257 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 28.315  -41.398 29.838  1.00 51.02  ? 258 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 33.179  -44.705 15.172  1.00 51.42  ? 259 HOH C O   1 
# 
