data_7HGJ
# 
_entry.id   7HGJ 
# 
_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   7HGJ         pdb_00007hgj 10.2210/pdb7hgj/pdb 
WWPDB D_1001407445 ?            ?                   
# 
_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                        7HGJ 
_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    1   ? ?    ? ? 
4 non-polymer syn N,N-dimethylpyridine-3-sulfonamide                 186.231   2   ? ?    ? ? 
5 water       nat water                                              18.015    249 ? ?    ? ? 
# 
_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 N,N-dimethylpyridine-3-sulfonamide ZUG 
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 
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 
ZUG non-polymer         . N,N-dimethylpyridine-3-sulfonamide ?                 'C7 H10 N2 O2 S' 186.231 
# 
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 28 ILE ILE 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  3  HIS HIS 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 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL 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        ZUG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZUG 
_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 ZUG 1   103 101 ZUG LIG B . 
K 2 SO4 1   101 5   SO4 SO4 C . 
L 4 ZUG 1   102 101 ZUG LIG C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 66  HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 333 HOH HOH A . 
M 5 HOH 5   205 208 HOH HOH A . 
M 5 HOH 6   206 71  HOH HOH A . 
M 5 HOH 7   207 304 HOH HOH A . 
M 5 HOH 8   208 351 HOH HOH A . 
M 5 HOH 9   209 84  HOH HOH A . 
M 5 HOH 10  210 259 HOH HOH A . 
M 5 HOH 11  211 55  HOH HOH A . 
M 5 HOH 12  212 293 HOH HOH A . 
M 5 HOH 13  213 167 HOH HOH A . 
M 5 HOH 14  214 341 HOH HOH A . 
M 5 HOH 15  215 97  HOH HOH A . 
M 5 HOH 16  216 292 HOH HOH A . 
M 5 HOH 17  217 23  HOH HOH A . 
M 5 HOH 18  218 85  HOH HOH A . 
M 5 HOH 19  219 91  HOH HOH A . 
M 5 HOH 20  220 35  HOH HOH A . 
M 5 HOH 21  221 188 HOH HOH A . 
M 5 HOH 22  222 26  HOH HOH A . 
M 5 HOH 23  223 87  HOH HOH A . 
M 5 HOH 24  224 28  HOH HOH A . 
M 5 HOH 25  225 7   HOH HOH A . 
M 5 HOH 26  226 142 HOH HOH A . 
M 5 HOH 27  227 27  HOH HOH A . 
M 5 HOH 28  228 86  HOH HOH A . 
M 5 HOH 29  229 37  HOH HOH A . 
M 5 HOH 30  230 111 HOH HOH A . 
M 5 HOH 31  231 290 HOH HOH A . 
M 5 HOH 32  232 8   HOH HOH A . 
M 5 HOH 33  233 95  HOH HOH A . 
M 5 HOH 34  234 139 HOH HOH A . 
M 5 HOH 35  235 2   HOH HOH A . 
M 5 HOH 36  236 260 HOH HOH A . 
M 5 HOH 37  237 32  HOH HOH A . 
M 5 HOH 38  238 115 HOH HOH A . 
M 5 HOH 39  239 301 HOH HOH A . 
M 5 HOH 40  240 152 HOH HOH A . 
M 5 HOH 41  241 12  HOH HOH A . 
M 5 HOH 42  242 289 HOH HOH A . 
M 5 HOH 43  243 99  HOH HOH A . 
M 5 HOH 44  244 199 HOH HOH A . 
M 5 HOH 45  245 34  HOH HOH A . 
M 5 HOH 46  246 190 HOH HOH A . 
M 5 HOH 47  247 41  HOH HOH A . 
M 5 HOH 48  248 38  HOH HOH A . 
M 5 HOH 49  249 1   HOH HOH A . 
M 5 HOH 50  250 274 HOH HOH A . 
M 5 HOH 51  251 288 HOH HOH A . 
M 5 HOH 52  252 300 HOH HOH A . 
M 5 HOH 53  253 93  HOH HOH A . 
M 5 HOH 54  254 109 HOH HOH A . 
M 5 HOH 55  255 267 HOH HOH A . 
M 5 HOH 56  256 337 HOH HOH A . 
M 5 HOH 57  257 203 HOH HOH A . 
M 5 HOH 58  258 78  HOH HOH A . 
M 5 HOH 59  259 179 HOH HOH A . 
M 5 HOH 60  260 145 HOH HOH A . 
M 5 HOH 61  261 143 HOH HOH A . 
M 5 HOH 62  262 20  HOH HOH A . 
M 5 HOH 63  263 60  HOH HOH A . 
M 5 HOH 64  264 18  HOH HOH A . 
M 5 HOH 65  265 340 HOH HOH A . 
M 5 HOH 66  266 299 HOH HOH A . 
M 5 HOH 67  267 77  HOH HOH A . 
M 5 HOH 68  268 164 HOH HOH A . 
M 5 HOH 69  269 222 HOH HOH A . 
M 5 HOH 70  270 75  HOH HOH A . 
M 5 HOH 71  271 94  HOH HOH A . 
M 5 HOH 72  272 42  HOH HOH A . 
M 5 HOH 73  273 211 HOH HOH A . 
M 5 HOH 74  274 218 HOH HOH A . 
M 5 HOH 75  275 131 HOH HOH A . 
M 5 HOH 76  276 281 HOH HOH A . 
M 5 HOH 77  277 58  HOH HOH A . 
M 5 HOH 78  278 14  HOH HOH A . 
M 5 HOH 79  279 47  HOH HOH A . 
M 5 HOH 80  280 327 HOH HOH A . 
M 5 HOH 81  281 116 HOH HOH A . 
M 5 HOH 82  282 318 HOH HOH A . 
M 5 HOH 83  283 9   HOH HOH A . 
M 5 HOH 84  284 19  HOH HOH A . 
M 5 HOH 85  285 16  HOH HOH A . 
M 5 HOH 86  286 113 HOH HOH A . 
M 5 HOH 87  287 165 HOH HOH A . 
M 5 HOH 88  288 278 HOH HOH A . 
M 5 HOH 89  289 21  HOH HOH A . 
M 5 HOH 90  290 73  HOH HOH A . 
M 5 HOH 91  291 22  HOH HOH A . 
M 5 HOH 92  292 296 HOH HOH A . 
M 5 HOH 93  293 350 HOH HOH A . 
M 5 HOH 94  294 31  HOH HOH A . 
M 5 HOH 95  295 210 HOH HOH A . 
M 5 HOH 96  296 83  HOH HOH A . 
M 5 HOH 97  297 270 HOH HOH A . 
M 5 HOH 98  298 339 HOH HOH A . 
M 5 HOH 99  299 63  HOH HOH A . 
M 5 HOH 100 300 156 HOH HOH A . 
M 5 HOH 101 301 108 HOH HOH A . 
M 5 HOH 102 302 185 HOH HOH A . 
M 5 HOH 103 303 219 HOH HOH A . 
M 5 HOH 104 304 64  HOH HOH A . 
M 5 HOH 105 305 283 HOH HOH A . 
M 5 HOH 106 306 332 HOH HOH A . 
M 5 HOH 107 307 57  HOH HOH A . 
M 5 HOH 108 308 205 HOH HOH A . 
M 5 HOH 109 309 206 HOH HOH A . 
N 5 HOH 1   201 258 HOH HOH B . 
N 5 HOH 2   202 247 HOH HOH B . 
N 5 HOH 3   203 331 HOH HOH B . 
N 5 HOH 4   204 123 HOH HOH B . 
N 5 HOH 5   205 249 HOH HOH B . 
N 5 HOH 6   206 215 HOH HOH B . 
N 5 HOH 7   207 279 HOH HOH B . 
N 5 HOH 8   208 272 HOH HOH B . 
N 5 HOH 9   209 242 HOH HOH B . 
N 5 HOH 10  210 89  HOH HOH B . 
N 5 HOH 11  211 69  HOH HOH B . 
N 5 HOH 12  212 98  HOH HOH B . 
N 5 HOH 13  213 168 HOH HOH B . 
N 5 HOH 14  214 172 HOH HOH B . 
N 5 HOH 15  215 137 HOH HOH B . 
N 5 HOH 16  216 59  HOH HOH B . 
N 5 HOH 17  217 54  HOH HOH B . 
N 5 HOH 18  218 261 HOH HOH B . 
N 5 HOH 19  219 117 HOH HOH B . 
N 5 HOH 20  220 150 HOH HOH B . 
N 5 HOH 21  221 224 HOH HOH B . 
N 5 HOH 22  222 17  HOH HOH B . 
N 5 HOH 23  223 5   HOH HOH B . 
N 5 HOH 24  224 169 HOH HOH B . 
N 5 HOH 25  225 329 HOH HOH B . 
N 5 HOH 26  226 217 HOH HOH B . 
N 5 HOH 27  227 119 HOH HOH B . 
N 5 HOH 28  228 153 HOH HOH B . 
N 5 HOH 29  229 6   HOH HOH B . 
N 5 HOH 30  230 10  HOH HOH B . 
N 5 HOH 31  231 157 HOH HOH B . 
N 5 HOH 32  232 44  HOH HOH B . 
N 5 HOH 33  233 96  HOH HOH B . 
N 5 HOH 34  234 101 HOH HOH B . 
N 5 HOH 35  235 280 HOH HOH B . 
N 5 HOH 36  236 352 HOH HOH B . 
N 5 HOH 37  237 175 HOH HOH B . 
N 5 HOH 38  238 24  HOH HOH B . 
N 5 HOH 39  239 68  HOH HOH B . 
N 5 HOH 40  240 160 HOH HOH B . 
N 5 HOH 41  241 320 HOH HOH B . 
N 5 HOH 42  242 223 HOH HOH B . 
N 5 HOH 43  243 334 HOH HOH B . 
N 5 HOH 44  244 315 HOH HOH B . 
N 5 HOH 45  245 74  HOH HOH B . 
N 5 HOH 46  246 61  HOH HOH B . 
N 5 HOH 47  247 25  HOH HOH B . 
N 5 HOH 48  248 197 HOH HOH B . 
N 5 HOH 49  249 79  HOH HOH B . 
N 5 HOH 50  250 303 HOH HOH B . 
N 5 HOH 51  251 120 HOH HOH B . 
N 5 HOH 52  252 76  HOH HOH B . 
N 5 HOH 53  253 46  HOH HOH B . 
N 5 HOH 54  254 72  HOH HOH B . 
N 5 HOH 55  255 36  HOH HOH B . 
N 5 HOH 56  256 214 HOH HOH B . 
N 5 HOH 57  257 104 HOH HOH B . 
N 5 HOH 58  258 13  HOH HOH B . 
N 5 HOH 59  259 163 HOH HOH B . 
N 5 HOH 60  260 182 HOH HOH B . 
N 5 HOH 61  261 316 HOH HOH B . 
N 5 HOH 62  262 170 HOH HOH B . 
N 5 HOH 63  263 201 HOH HOH B . 
N 5 HOH 64  264 177 HOH HOH B . 
N 5 HOH 65  265 291 HOH HOH B . 
N 5 HOH 66  266 322 HOH HOH B . 
N 5 HOH 67  267 335 HOH HOH B . 
N 5 HOH 68  268 346 HOH HOH B . 
N 5 HOH 69  269 314 HOH HOH B . 
N 5 HOH 70  270 313 HOH HOH B . 
N 5 HOH 71  271 107 HOH HOH B . 
N 5 HOH 72  272 312 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 348 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 226 HOH HOH C . 
O 5 HOH 5   205 344 HOH HOH C . 
O 5 HOH 6   206 317 HOH HOH C . 
O 5 HOH 7   207 173 HOH HOH C . 
O 5 HOH 8   208 15  HOH HOH C . 
O 5 HOH 9   209 49  HOH HOH C . 
O 5 HOH 10  210 102 HOH HOH C . 
O 5 HOH 11  211 336 HOH HOH C . 
O 5 HOH 12  212 254 HOH HOH C . 
O 5 HOH 13  213 134 HOH HOH C . 
O 5 HOH 14  214 118 HOH HOH C . 
O 5 HOH 15  215 269 HOH HOH C . 
O 5 HOH 16  216 338 HOH HOH C . 
O 5 HOH 17  217 184 HOH HOH C . 
O 5 HOH 18  218 309 HOH HOH C . 
O 5 HOH 19  219 45  HOH HOH C . 
O 5 HOH 20  220 90  HOH HOH C . 
O 5 HOH 21  221 4   HOH HOH C . 
O 5 HOH 22  222 271 HOH HOH C . 
O 5 HOH 23  223 126 HOH HOH C . 
O 5 HOH 24  224 62  HOH HOH C . 
O 5 HOH 25  225 284 HOH HOH C . 
O 5 HOH 26  226 43  HOH HOH C . 
O 5 HOH 27  227 148 HOH HOH C . 
O 5 HOH 28  228 56  HOH HOH C . 
O 5 HOH 29  229 275 HOH HOH C . 
O 5 HOH 30  230 82  HOH HOH C . 
O 5 HOH 31  231 122 HOH HOH C . 
O 5 HOH 32  232 171 HOH HOH C . 
O 5 HOH 33  233 132 HOH HOH C . 
O 5 HOH 34  234 135 HOH HOH C . 
O 5 HOH 35  235 53  HOH HOH C . 
O 5 HOH 36  236 189 HOH HOH C . 
O 5 HOH 37  237 40  HOH HOH C . 
O 5 HOH 38  238 48  HOH HOH C . 
O 5 HOH 39  239 67  HOH HOH C . 
O 5 HOH 40  240 209 HOH HOH C . 
O 5 HOH 41  241 294 HOH HOH C . 
O 5 HOH 42  242 295 HOH HOH C . 
O 5 HOH 43  243 198 HOH HOH C . 
O 5 HOH 44  244 287 HOH HOH C . 
O 5 HOH 45  245 349 HOH HOH C . 
O 5 HOH 46  246 302 HOH HOH C . 
O 5 HOH 47  247 246 HOH HOH C . 
O 5 HOH 48  248 65  HOH HOH C . 
O 5 HOH 49  249 130 HOH HOH C . 
O 5 HOH 50  250 149 HOH HOH C . 
O 5 HOH 51  251 298 HOH HOH C . 
O 5 HOH 52  252 328 HOH HOH C . 
O 5 HOH 53  253 342 HOH HOH C . 
O 5 HOH 54  254 70  HOH HOH C . 
O 5 HOH 55  255 305 HOH HOH C . 
O 5 HOH 56  256 146 HOH HOH C . 
O 5 HOH 57  257 241 HOH HOH C . 
O 5 HOH 58  258 319 HOH HOH C . 
O 5 HOH 59  259 151 HOH HOH C . 
O 5 HOH 60  260 343 HOH HOH C . 
O 5 HOH 61  261 330 HOH HOH C . 
O 5 HOH 62  262 103 HOH HOH C . 
O 5 HOH 63  263 324 HOH HOH C . 
O 5 HOH 64  264 92  HOH HOH C . 
O 5 HOH 65  265 345 HOH HOH C . 
O 5 HOH 66  266 310 HOH HOH C . 
O 5 HOH 67  267 347 HOH HOH C . 
O 5 HOH 68  268 125 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 70 ? CE  ? A LYS 71 CE  
2  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
3  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
8  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
9  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
17 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
18 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
19 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
20 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
21 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
22 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
23 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
24 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
25 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
26 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
27 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
28 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
29 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
30 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
31 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
32 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
33 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
34 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
35 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
36 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
37 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
38 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
39 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
40 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
41 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
42 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
43 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
44 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
45 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
46 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
47 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
48 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
49 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
50 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
51 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
52 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
53 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 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           7HGJ 
_cell.length_a           41.528 
_cell.length_b           41.998 
_cell.length_c           157.954 
_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                         7HGJ 
_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          7HGJ 
_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                     7HGJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             78.98 
_reflns.d_resolution_high            1.75 
_reflns.number_obs                   28396 
_reflns.percent_possible_obs         98.6 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_netI_over_sigmaI        12.0 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.080 
_reflns.pdbx_Rpim_I_all              0.034 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     149796 
_reflns.pdbx_chi_squared             0.92 
_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                  1.75 
_reflns_shell.d_res_low                   1.84 
_reflns_shell.number_measured_all         22558 
_reflns_shell.number_unique_obs           4089 
_reflns_shell.Rmerge_I_obs                1.552 
_reflns_shell.pdbx_chi_squared            0.81 
_reflns_shell.pdbx_redundancy             5.5 
_reflns_shell.percent_possible_obs        99.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.713 
_reflns_shell.pdbx_Rpim_I_all             0.714 
_reflns_shell.pdbx_CC_half                0.481 
_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                                 7HGJ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     26869 
_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                             78.98 
_refine.ls_d_res_high                            1.75 
_refine.ls_percent_reflns_obs                    98.37 
_refine.ls_R_factor_obs                          0.19447 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19238 
_refine.ls_R_factor_R_free                       0.23210 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1448 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               38.820 
_refine.aniso_B[1][1]                            0.71 
_refine.aniso_B[2][2]                            -0.39 
_refine.aniso_B[3][3]                            -0.31 
_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                       0.132 
_refine.pdbx_overall_ESU_R_Free                  0.126 
_refine.overall_SU_ML                            0.112 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.713 
_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        2159 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             249 
_refine_hist.number_atoms_total               2466 
_refine_hist.d_res_high                       1.75 
_refine_hist.d_res_low                        78.98 
# 
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             0.008  0.012  ? 2321 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.634  1.827  ? 3162 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.342  5.000  ? 269  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.062  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.959 10.000 ? 311  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.118  0.200  ? 294  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1940 '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                  3.466  3.622  ? 1087 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.872  6.463  ? 1353 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.638  3.965  ? 1234 '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       9.574  56.51  ? 3632 '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                       1.750 
_refine_ls_shell.d_res_low                        1.795 
_refine_ls_shell.number_reflns_R_work             1937 
_refine_ls_shell.R_factor_R_work                  0.316 
_refine_ls_shell.percent_reflns_obs               99.13 
_refine_ls_shell.R_factor_R_free                  0.329 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             115 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z751811134' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGJ 
_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 2 ? 
L N N 4 ? 
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 7HGJ A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGJ B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGJ 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 7HGJ GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGJ SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGJ GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGJ SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGJ GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGJ 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 THR B 51 ? LEU B 54 ? THR B 50 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 TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
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 TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGJ 
_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   A HOH 266 ? ? O C HOH 211 ? ? 1.57 
2  1 O   B HOH 235 ? ? O B HOH 266 ? ? 1.79 
3  1 O   B HOH 224 ? ? O B HOH 259 ? ? 1.91 
4  1 O2  C SO4 101 ? ? O C HOH 201 ? ? 1.99 
5  1 O   B HOH 250 ? ? O B HOH 266 ? ? 2.05 
6  1 O   C HOH 241 ? ? O C HOH 258 ? ? 2.07 
7  1 O   A HOH 297 ? ? O C HOH 202 ? ? 2.08 
8  1 O   B HOH 214 ? ? O B HOH 238 ? ? 2.09 
9  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.10 
10 1 O   C HOH 256 ? ? O C HOH 263 ? ? 2.16 
11 1 OD2 B ASP 26  ? ? O B HOH 201 ? ? 2.17 
12 1 OE1 C GLN 85  ? ? O C HOH 202 ? ? 2.17 
# 
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 214 ? ? 1_555 O C HOH 259 ? ? 1_455 2.08 
2 1 O A HOH 216 ? ? 1_555 O A HOH 269 ? ? 4_545 2.14 
3 1 O A HOH 233 ? ? 1_555 O A HOH 285 ? ? 4_545 2.17 
# 
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 ASN A 87 ? ? -150.98 65.27  
2 1 ASN B 38 ? ? 87.09   -13.30 
3 1 ASN B 87 ? ? -160.08 60.71  
4 1 ASN C 87 ? ? -157.20 53.00  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.31 
# 
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 ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ASP 30 ? C ASP 31 
11 1 Y 1 C GLY 31 ? C GLY 32 
12 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 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
VAL N    N N N 387 
VAL CA   C N S 388 
VAL C    C N N 389 
VAL O    O N N 390 
VAL CB   C N N 391 
VAL CG1  C N N 392 
VAL CG2  C N N 393 
VAL OXT  O N N 394 
VAL H    H N N 395 
VAL H2   H N N 396 
VAL HA   H N N 397 
VAL HB   H N N 398 
VAL HG11 H N N 399 
VAL HG12 H N N 400 
VAL HG13 H N N 401 
VAL HG21 H N N 402 
VAL HG22 H N N 403 
VAL HG23 H N N 404 
VAL HXT  H N N 405 
ZUG N1   N N N 406 
ZUG C4   C Y N 407 
ZUG C5   C Y N 408 
ZUG C6   C Y N 409 
ZUG C7   C Y N 410 
ZUG C1   C N N 411 
ZUG C2   C N N 412 
ZUG S1   S N N 413 
ZUG O1   O N N 414 
ZUG O2   O N N 415 
ZUG C3   C Y N 416 
ZUG N2   N Y N 417 
ZUG H1   H N N 418 
ZUG H2   H N N 419 
ZUG H3   H N N 420 
ZUG H4   H N N 421 
ZUG H5   H N N 422 
ZUG H6   H N N 423 
ZUG H7   H N N 424 
ZUG H8   H N N 425 
ZUG H9   H N N 426 
ZUG H10  H N N 427 
# 
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 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
ZUG C5  C6   doub Y N 389 
ZUG C5  C4   sing Y N 390 
ZUG C2  N1   sing N N 391 
ZUG C6  N2   sing Y N 392 
ZUG C4  C3   doub Y N 393 
ZUG N2  C7   doub Y N 394 
ZUG N1  C1   sing N N 395 
ZUG N1  S1   sing N N 396 
ZUG C3  C7   sing Y N 397 
ZUG C3  S1   sing N N 398 
ZUG O1  S1   doub N N 399 
ZUG S1  O2   doub N N 400 
ZUG C4  H1   sing N N 401 
ZUG C5  H2   sing N N 402 
ZUG C6  H3   sing N N 403 
ZUG C7  H4   sing N N 404 
ZUG C1  H5   sing N N 405 
ZUG C1  H6   sing N N 406 
ZUG C1  H7   sing N N 407 
ZUG C2  H8   sing N N 408 
ZUG C2  H9   sing N N 409 
ZUG C2  H10  sing N N 410 
# 
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                    7HGJ 
_atom_sites.fract_transf_matrix[1][1]   0.024080 
_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]   0.023811 
_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]   0.006331 
_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  ? 0.291   4.365   2.523   1.00 55.04  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.732  3.556   1.806   1.00 61.93  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? -0.064  2.496   0.923   1.00 54.04  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.056   2.688   0.462   1.00 49.31  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.685  4.431   0.978   1.00 62.16  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.765  5.176   1.770   1.00 77.42  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.807  4.353   3.001   1.00 71.27  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -2.845  4.777   4.463   1.00 78.30  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.710  1.313   0.743   1.00 48.92  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.250  0.259   -0.175  1.00 43.38  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.037   0.692   -1.619  1.00 42.61  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.671  1.531   -2.178  1.00 43.05  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.518  -0.680  -0.123  1.00 41.34  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.964  -0.583  1.323   1.00 43.52  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.913  0.914   1.497   1.00 46.52  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.058   0.090   -2.233  1.00 39.11  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.222   0.204   -3.668  1.00 36.58  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.653   -1.082  -4.255  1.00 35.40  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.168   -1.930  -3.505  1.00 34.95  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.709   0.330   -4.028  1.00 45.12  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.358   1.609   -3.602  1.00 59.33  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.175   2.196   -2.364  1.00 65.59  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.212   2.406   -4.264  1.00 64.94  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.881   3.316   -2.294  1.00 62.89  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.525   3.456   -3.433  1.00 62.83  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.715   -1.214  -5.587  1.00 31.37  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.464   -2.471  -6.267  1.00 31.45  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.558   -3.456  -5.867  1.00 28.45  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.620   -3.044  -5.403  1.00 28.00  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.434   -2.225  -7.773  1.00 33.20  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.298   -4.747  -6.049  1.00 29.21  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.313   -5.764  -5.818  1.00 28.57  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.482   -5.609  -6.798  1.00 31.28  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.278   -5.326  -7.977  1.00 31.50  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.711   -7.162  -5.942  1.00 26.39  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 0.969   -7.570  -4.676  1.00 28.85  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.667   -7.776  -3.487  1.00 28.09  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.405  -7.810  -4.691  1.00 26.67  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.011   -8.143  -2.321  1.00 28.69  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -1.053  -8.243  -3.532  1.00 25.23  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.353  -8.391  -2.350  1.00 26.40  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.710   -5.880  -6.318  1.00 25.46  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.844   -5.850  -7.221  1.00 25.81  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.743   -7.054  -6.948  1.00 24.58  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.732   -7.631  -5.855  1.00 25.78  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.609   -4.531  -7.000  1.00 28.99  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.236   -4.447  -5.611  1.00 32.82  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.837   -3.081  -5.265  1.00 37.57  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.471   -3.034  -3.904  1.00 37.55  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.485   -3.133  -2.835  1.00 36.49  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.609   -7.446  -7.902  1.00 25.72  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.571   -8.527  -7.661  1.00 26.59  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.391   -8.278  -6.392  1.00 26.18  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.845   -7.152  -6.148  1.00 25.85  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.449   -8.542  -8.963  1.00 27.97  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.556   -7.887  -10.001 1.00 31.04  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.721   -6.848  -9.243  1.00 28.23  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.559   -9.346  -5.586  1.00 24.66  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.283  -9.312  -4.321  1.00 21.31  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.332   -9.196  -3.130  1.00 23.88  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.711   -9.460  -1.970  1.00 26.25  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.100   -8.725  -3.379  1.00 21.37  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.137   -8.684  -2.281  1.00 21.53  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.920   -10.065 -1.652  1.00 21.19  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.748   -11.046 -2.349  1.00 22.15  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.811   -8.068  -2.710  1.00 24.13  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.822   -6.553  -2.865  1.00 25.76  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.797   -5.909  -2.426  1.00 26.08  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.912   -6.026  -3.505  1.00 26.13  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.816   -10.119 -0.313  1.00 21.39  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.636   -11.386 0.392   1.00 21.36  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.169   -11.489 0.824   1.00 22.62  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.595   -10.523 1.339   1.00 22.81  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.555   -11.527 1.610   1.00 20.25  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.045   -11.280 1.318   1.00 24.15  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.914   -11.451 2.547   1.00 25.05  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.441   -12.243 0.197   1.00 21.89  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.597   -12.680 0.668   1.00 20.15  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.171   -12.878 0.913   1.00 20.60  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.925   -14.263 1.522   1.00 23.82  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.813   -15.123 1.545   1.00 22.74  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.403   -12.759 -0.423  1.00 19.77  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.540   -11.362 -1.011  1.00 21.34  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.800   -13.855 -1.421  1.00 19.36  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.697   -14.462 2.008   1.00 22.41  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.074   -15.778 2.061   1.00 23.95  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.111   -15.847 0.888   1.00 24.30  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.694  -14.930 0.699   1.00 22.31  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.267   -16.061 3.345   1.00 23.26  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.202   -16.177 4.537   1.00 22.40  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.637   -15.035 5.203   1.00 26.17  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.687   -17.419 4.932   1.00 24.98  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.525   -15.137 6.263   1.00 29.57  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.609   -17.518 5.966   1.00 30.86  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.030   -16.376 6.623   1.00 29.42  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.232   -16.927 0.101   1.00 24.28  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.570  -17.072 -1.105  1.00 26.26  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.550  -18.224 -0.877  1.00 26.48  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.170  -19.291 -0.359  1.00 27.99  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.317   -17.291 -2.330  1.00 21.67  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.817  -17.980 -1.237  1.00 25.19  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.869  -18.959 -1.001  1.00 25.98  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.245  -19.646 -2.317  1.00 28.87  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.626  -18.975 -3.291  1.00 31.97  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.068  -18.330 -0.285  1.00 28.13  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.163  -19.373 0.021   1.00 35.41  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.707  -20.308 1.149   1.00 35.66  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.805  -21.179 1.697   1.00 41.02  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.178  -22.173 0.690   1.00 39.19  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.140  -20.987 -2.299  1.00 27.89  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.681  -21.839 -3.350  1.00 30.92  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.726  -22.764 -2.727  1.00 34.71  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.557  -23.207 -1.586  1.00 30.90  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.607  -22.790 -3.870  1.00 33.14  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.285  -22.115 -4.160  1.00 44.57  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.233  -21.736 -5.919  1.00 43.48  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.533  -23.257 -6.563  1.00 45.98  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.779  -23.028 -3.508  1.00 41.52  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.847  -23.967 -3.204  1.00 42.20  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.258  -25.238 -2.614  1.00 40.70  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.377  -25.865 -3.209  1.00 40.65  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.561  -24.359 -4.502  1.00 49.14  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.957  -24.920 -4.295  1.00 62.03  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.911 -23.863 -3.739  1.00 73.99  ? 16  LYS A CD  1 
ATOM   125  C CE  . LYS A 1 17 ? -11.364 -22.860 -4.763  1.00 78.50  ? 16  LYS A CE  1 
ATOM   126  N NZ  . LYS A 1 17 ? -12.284 -23.494 -5.718  1.00 84.68  ? 16  LYS A NZ  1 
ATOM   127  N N   . GLY A 1 18 ? -7.727  -25.579 -1.412  1.00 36.61  ? 17  GLY A N   1 
ATOM   128  C CA  . GLY A 1 18 ? -7.350  -26.849 -0.827  1.00 37.08  ? 17  GLY A CA  1 
ATOM   129  C C   . GLY A 1 18 ? -5.966  -26.829 -0.193  1.00 46.24  ? 17  GLY A C   1 
ATOM   130  O O   . GLY A 1 18 ? -5.487  -27.879 0.215   1.00 47.90  ? 17  GLY A O   1 
ATOM   131  N N   . TYR A 1 19 ? -5.331  -25.648 -0.082  1.00 37.44  ? 18  TYR A N   1 
ATOM   132  C CA  . TYR A 1 19 ? -4.080  -25.597 0.657   1.00 35.88  ? 18  TYR A CA  1 
ATOM   133  C C   . TYR A 1 19 ? -4.132  -24.478 1.678   1.00 33.43  ? 18  TYR A C   1 
ATOM   134  O O   . TYR A 1 19 ? -4.829  -23.491 1.476   1.00 33.71  ? 18  TYR A O   1 
ATOM   135  C CB  . TYR A 1 19 ? -2.876  -25.219 -0.204  1.00 41.38  ? 18  TYR A CB  1 
ATOM   136  C CG  . TYR A 1 19 ? -2.555  -26.251 -1.269  1.00 45.02  ? 18  TYR A CG  1 
ATOM   137  C CD1 . TYR A 1 19 ? -1.669  -27.291 -1.015  1.00 53.42  ? 18  TYR A CD1 1 
ATOM   138  C CD2 . TYR A 1 19 ? -3.147  -26.176 -2.523  1.00 49.48  ? 18  TYR A CD2 1 
ATOM   139  C CE1 . TYR A 1 19 ? -1.382  -28.233 -1.991  1.00 62.34  ? 18  TYR A CE1 1 
ATOM   140  C CE2 . TYR A 1 19 ? -2.865  -27.107 -3.509  1.00 54.23  ? 18  TYR A CE2 1 
ATOM   141  C CZ  . TYR A 1 19 ? -1.983  -28.138 -3.236  1.00 66.79  ? 18  TYR A CZ  1 
ATOM   142  O OH  . TYR A 1 19 ? -1.723  -29.055 -4.213  1.00 84.51  ? 18  TYR A OH  1 
ATOM   143  N N   . PRO A 1 20 ? -3.354  -24.574 2.778   1.00 30.89  ? 19  PRO A N   1 
ATOM   144  C CA  . PRO A 1 20 ? -3.291  -23.495 3.769   1.00 31.99  ? 19  PRO A CA  1 
ATOM   145  C C   . PRO A 1 20 ? -2.587  -22.306 3.099   1.00 29.21  ? 19  PRO A C   1 
ATOM   146  O O   . PRO A 1 20 ? -1.843  -22.495 2.134   1.00 27.19  ? 19  PRO A O   1 
ATOM   147  C CB  . PRO A 1 20 ? -2.457  -24.094 4.906   1.00 30.89  ? 19  PRO A CB  1 
ATOM   148  C CG  . PRO A 1 20 ? -1.587  -25.119 4.221   1.00 30.93  ? 19  PRO A CG  1 
ATOM   149  C CD  . PRO A 1 20 ? -2.407  -25.667 3.052   1.00 34.81  ? 19  PRO A CD  1 
ATOM   150  N N   . HIS A 1 21 ? -2.884  -21.102 3.583   1.00 25.83  ? 20  HIS A N   1 
ATOM   151  C CA  . HIS A 1 21 ? -2.155  -19.903 3.175   1.00 27.74  ? 20  HIS A CA  1 
ATOM   152  C C   . HIS A 1 21 ? -0.656  -20.181 3.278   1.00 29.08  ? 20  HIS A C   1 
ATOM   153  O O   . HIS A 1 21 ? -0.183  -20.584 4.347   1.00 26.56  ? 20  HIS A O   1 
ATOM   154  C CB  . HIS A 1 21 ? -2.588  -18.693 4.008   1.00 26.11  ? 20  HIS A CB  1 
ATOM   155  C CG  . HIS A 1 21 ? -4.046  -18.327 3.849   1.00 28.26  ? 20  HIS A CG  1 
ATOM   156  N ND1 . HIS A 1 21 ? -5.076  -18.976 4.523   1.00 32.57  ? 20  HIS A ND1 1 
ATOM   157  C CD2 . HIS A 1 21 ? -4.629  -17.352 3.110   1.00 28.35  ? 20  HIS A CD2 1 
ATOM   158  C CE1 . HIS A 1 21 ? -6.248  -18.425 4.191   1.00 31.58  ? 20  HIS A CE1 1 
ATOM   159  N NE2 . HIS A 1 21 ? -6.012  -17.422 3.335   1.00 29.93  ? 20  HIS A NE2 1 
ATOM   160  N N   . TRP A 1 22 ? 0.082   -19.942 2.174   1.00 26.44  ? 21  TRP A N   1 
ATOM   161  C CA  . TRP A 1 22 ? 1.394   -20.578 2.020   1.00 24.69  ? 21  TRP A CA  1 
ATOM   162  C C   . TRP A 1 22 ? 2.488   -19.514 1.839   1.00 26.85  ? 21  TRP A C   1 
ATOM   163  O O   . TRP A 1 22 ? 2.304   -18.610 1.034   1.00 25.52  ? 21  TRP A O   1 
ATOM   164  C CB  . TRP A 1 22 ? 1.374   -21.516 0.805   1.00 26.15  ? 21  TRP A CB  1 
ATOM   165  C CG  . TRP A 1 22 ? 2.485   -22.533 0.852   1.00 26.94  ? 21  TRP A CG  1 
ATOM   166  C CD1 . TRP A 1 22 ? 3.810   -22.315 0.615   1.00 29.39  ? 21  TRP A CD1 1 
ATOM   167  C CD2 . TRP A 1 22 ? 2.359   -23.933 1.185   1.00 26.97  ? 21  TRP A CD2 1 
ATOM   168  N NE1 . TRP A 1 22 ? 4.518   -23.481 0.745   1.00 28.93  ? 21  TRP A NE1 1 
ATOM   169  C CE2 . TRP A 1 22 ? 3.649   -24.500 1.076   1.00 31.11  ? 21  TRP A CE2 1 
ATOM   170  C CE3 . TRP A 1 22 ? 1.279   -24.773 1.490   1.00 31.79  ? 21  TRP A CE3 1 
ATOM   171  C CZ2 . TRP A 1 22 ? 3.899   -25.854 1.330   1.00 30.97  ? 21  TRP A CZ2 1 
ATOM   172  C CZ3 . TRP A 1 22 ? 1.528   -26.119 1.717   1.00 32.02  ? 21  TRP A CZ3 1 
ATOM   173  C CH2 . TRP A 1 22 ? 2.823   -26.650 1.657   1.00 32.47  ? 21  TRP A CH2 1 
ATOM   174  N N   . PRO A 1 23 ? 3.644   -19.582 2.556   1.00 22.44  ? 22  PRO A N   1 
ATOM   175  C CA  . PRO A 1 23 ? 4.700   -18.560 2.421   1.00 22.22  ? 22  PRO A CA  1 
ATOM   176  C C   . PRO A 1 23 ? 5.196   -18.536 0.973   1.00 22.77  ? 22  PRO A C   1 
ATOM   177  O O   . PRO A 1 23 ? 5.378   -19.595 0.351   1.00 23.50  ? 22  PRO A O   1 
ATOM   178  C CB  . PRO A 1 23 ? 5.766   -18.997 3.475   1.00 23.34  ? 22  PRO A CB  1 
ATOM   179  C CG  . PRO A 1 23 ? 5.488   -20.504 3.654   1.00 22.15  ? 22  PRO A CG  1 
ATOM   180  C CD  . PRO A 1 23 ? 3.941   -20.562 3.602   1.00 21.27  ? 22  PRO A CD  1 
ATOM   181  N N   . ALA A 1 24 ? 5.314   -17.321 0.415   1.00 20.30  ? 23  ALA A N   1 
ATOM   182  C CA  . ALA A 1 24 ? 5.583   -17.186 -1.015  1.00 20.39  ? 23  ALA A CA  1 
ATOM   183  C C   . ALA A 1 24 ? 6.161   -15.804 -1.337  1.00 22.57  ? 23  ALA A C   1 
ATOM   184  O O   . ALA A 1 24 ? 6.170   -14.902 -0.509  1.00 21.63  ? 23  ALA A O   1 
ATOM   185  C CB  . ALA A 1 24 ? 4.296   -17.445 -1.796  1.00 20.68  ? 23  ALA A CB  1 
ATOM   186  N N   . ARG A 1 25 ? 6.644   -15.631 -2.576  1.00 21.81  ? 24  ARG A N   1 
ATOM   187  C CA  . ARG A 1 25 ? 7.099   -14.318 -2.973  1.00 21.21  ? 24  ARG A CA  1 
ATOM   188  C C   . ARG A 1 25 ? 6.567   -14.044 -4.373  1.00 20.53  ? 24  ARG A C   1 
ATOM   189  O O   . ARG A 1 25 ? 6.220   -14.980 -5.100  1.00 23.20  ? 24  ARG A O   1 
ATOM   190  C CB  . ARG A 1 25 ? 8.626   -14.166 -2.910  1.00 19.72  ? 24  ARG A CB  1 
ATOM   191  C CG  . ARG A 1 25 ? 9.338   -15.112 -3.865  1.00 20.67  ? 24  ARG A CG  1 
ATOM   192  C CD  . ARG A 1 25 ? 10.872  -14.861 -3.858  1.00 21.82  ? 24  ARG A CD  1 
ATOM   193  N NE  . ARG A 1 25 ? 11.536  -15.711 -4.873  1.00 21.76  ? 24  ARG A NE  1 
ATOM   194  C CZ  . ARG A 1 25 ? 12.796  -16.137 -4.768  1.00 24.58  ? 24  ARG A CZ  1 
ATOM   195  N NH1 . ARG A 1 25 ? 13.475  -15.992 -3.632  1.00 22.89  ? 24  ARG A NH1 1 
ATOM   196  N NH2 . ARG A 1 25 ? 13.341  -16.783 -5.785  1.00 26.77  ? 24  ARG A NH2 1 
ATOM   197  N N   . ILE A 1 26 ? 6.459   -12.767 -4.692  1.00 20.41  ? 25  ILE A N   1 
ATOM   198  C CA  . ILE A 1 26 ? 6.229   -12.396 -6.090  1.00 22.29  ? 25  ILE A CA  1 
ATOM   199  C C   . ILE A 1 26 ? 7.562   -12.526 -6.815  1.00 23.81  ? 25  ILE A C   1 
ATOM   200  O O   . ILE A 1 26 ? 8.514   -11.852 -6.459  1.00 25.86  ? 25  ILE A O   1 
ATOM   201  C CB  . ILE A 1 26 ? 5.715   -10.942 -6.220  1.00 25.70  ? 25  ILE A CB  1 
ATOM   202  C CG1 . ILE A 1 26 ? 4.512   -10.611 -5.297  1.00 30.07  ? 25  ILE A CG1 1 
ATOM   203  C CG2 . ILE A 1 26 ? 5.447   -10.605 -7.695  1.00 25.12  ? 25  ILE A CG2 1 
ATOM   204  C CD1 . ILE A 1 26 ? 3.177   -11.132 -5.751  1.00 31.94  ? 25  ILE A CD1 1 
ATOM   205  N N   . ASP A 1 27 ? 7.617   -13.356 -7.855  1.00 25.12  ? 26  ASP A N   1 
ATOM   206  C CA  . ASP A 1 27 ? 8.869   -13.543 -8.570  1.00 29.68  ? 26  ASP A CA  1 
ATOM   207  C C   . ASP A 1 27 ? 9.025   -12.526 -9.696  1.00 31.39  ? 26  ASP A C   1 
ATOM   208  O O   . ASP A 1 27 ? 8.053   -11.938 -10.158 1.00 29.55  ? 26  ASP A O   1 
ATOM   209  C CB  . ASP A 1 27 ? 8.960   -14.912 -9.224  1.00 29.04  ? 26  ASP A CB  1 
ATOM   210  C CG  . ASP A 1 27 ? 9.907   -15.882 -8.549  1.00 33.16  ? 26  ASP A CG  1 
ATOM   211  O OD1 . ASP A 1 27 ? 10.508  -15.512 -7.519  1.00 36.82  ? 26  ASP A OD1 1 
ATOM   212  O OD2 . ASP A 1 27 ? 10.018  -17.000 -9.048  1.00 33.79  ? 26  ASP A OD2 1 
ATOM   213  N N   . ASP A 1 28 ? 10.289  -12.314 -10.097 1.00 35.58  ? 27  ASP A N   1 
ATOM   214  C CA  . ASP A 1 28 ? 10.604  -11.675 -11.361 1.00 39.44  ? 27  ASP A CA  1 
ATOM   215  C C   . ASP A 1 28 ? 10.267  -12.661 -12.479 1.00 35.08  ? 27  ASP A C   1 
ATOM   216  O O   . ASP A 1 28 ? 10.109  -13.850 -12.247 1.00 36.50  ? 27  ASP A O   1 
ATOM   217  C CB  . ASP A 1 28 ? 12.074  -11.281 -11.430 1.00 47.09  ? 27  ASP A CB  1 
ATOM   218  C CG  . ASP A 1 28 ? 12.476  -10.029 -10.657 1.00 54.46  ? 27  ASP A CG  1 
ATOM   219  O OD1 . ASP A 1 28 ? 12.153  -8.906  -11.126 1.00 52.78  ? 27  ASP A OD1 1 
ATOM   220  O OD2 . ASP A 1 28 ? 13.116  -10.185 -9.589  1.00 56.62  ? 27  ASP A OD2 1 
ATOM   221  N N   . ILE A 1 29 ? 10.081  -12.148 -13.686 1.00 37.05  ? 28  ILE A N   1 
ATOM   222  C CA  . ILE A 1 29 ? 9.984   -13.005 -14.854 1.00 36.33  ? 28  ILE A CA  1 
ATOM   223  C C   . ILE A 1 29 ? 11.326  -12.857 -15.555 1.00 36.03  ? 28  ILE A C   1 
ATOM   224  O O   . ILE A 1 29 ? 11.659  -11.728 -15.905 1.00 34.84  ? 28  ILE A O   1 
ATOM   225  C CB  . ILE A 1 29 ? 8.871   -12.454 -15.755 1.00 36.16  ? 28  ILE A CB  1 
ATOM   226  C CG1 . ILE A 1 29 ? 7.507   -12.443 -15.023 1.00 37.44  ? 28  ILE A CG1 1 
ATOM   227  C CG2 . ILE A 1 29 ? 8.842   -13.211 -17.093 1.00 31.59  ? 28  ILE A CG2 1 
ATOM   228  C CD1 . ILE A 1 29 ? 6.627   -11.248 -15.365 1.00 38.30  ? 28  ILE A CD1 1 
ATOM   229  N N   . ALA A 1 30 ? 12.077  -13.957 -15.707 1.00 34.75  ? 29  ALA A N   1 
ATOM   230  C CA  . ALA A 1 30 ? 13.388  -13.898 -16.352 1.00 33.93  ? 29  ALA A CA  1 
ATOM   231  C C   . ALA A 1 30 ? 13.212  -13.625 -17.851 1.00 34.25  ? 29  ALA A C   1 
ATOM   232  O O   . ALA A 1 30 ? 12.164  -13.901 -18.456 1.00 32.46  ? 29  ALA A O   1 
ATOM   233  C CB  . ALA A 1 30 ? 14.144  -15.195 -16.135 1.00 34.36  ? 29  ALA A CB  1 
ATOM   234  N N   . ASP A 1 31 ? 14.232  -12.992 -18.425 1.00 34.26  ? 30  ASP A N   1 
ATOM   235  C CA  . ASP A 1 31 ? 14.296  -12.864 -19.873 1.00 32.57  ? 30  ASP A CA  1 
ATOM   236  C C   . ASP A 1 31 ? 14.034  -14.239 -20.466 1.00 26.94  ? 30  ASP A C   1 
ATOM   237  O O   . ASP A 1 31 ? 14.647  -15.212 -20.039 1.00 30.27  ? 30  ASP A O   1 
ATOM   238  C CB  . ASP A 1 31 ? 15.671  -12.352 -20.268 1.00 31.07  ? 30  ASP A CB  1 
ATOM   239  C CG  . ASP A 1 31 ? 15.844  -10.846 -20.138 1.00 32.33  ? 30  ASP A CG  1 
ATOM   240  O OD1 . ASP A 1 31 ? 14.834  -10.128 -20.140 1.00 35.81  ? 30  ASP A OD1 1 
ATOM   241  O OD2 . ASP A 1 31 ? 16.999  -10.403 -20.085 1.00 35.93  ? 30  ASP A OD2 1 
ATOM   242  N N   . GLY A 1 32 ? 13.070  -14.320 -21.400 1.00 31.62  ? 31  GLY A N   1 
ATOM   243  C CA  . GLY A 1 32 ? 12.828  -15.544 -22.145 1.00 29.42  ? 31  GLY A CA  1 
ATOM   244  C C   . GLY A 1 32 ? 11.829  -16.475 -21.454 1.00 35.68  ? 31  GLY A C   1 
ATOM   245  O O   . GLY A 1 32 ? 11.426  -17.468 -22.044 1.00 36.55  ? 31  GLY A O   1 
ATOM   246  N N   . ALA A 1 33 ? 11.454  -16.173 -20.202 1.00 32.55  ? 32  ALA A N   1 
ATOM   247  C CA  . ALA A 1 33 ? 10.527  -17.007 -19.438 1.00 33.25  ? 32  ALA A CA  1 
ATOM   248  C C   . ALA A 1 33 ? 9.077   -16.734 -19.840 1.00 30.73  ? 32  ALA A C   1 
ATOM   249  O O   . ALA A 1 33 ? 8.713   -15.643 -20.265 1.00 31.81  ? 32  ALA A O   1 
ATOM   250  C CB  . ALA A 1 33 ? 10.710  -16.755 -17.941 1.00 31.92  ? 32  ALA A CB  1 
ATOM   251  N N   . VAL A 1 34 ? 8.209   -17.724 -19.609 1.00 33.19  ? 33  VAL A N   1 
ATOM   252  C CA  . VAL A 1 34 ? 6.784   -17.561 -19.864 1.00 31.64  ? 33  VAL A CA  1 
ATOM   253  C C   . VAL A 1 34 ? 6.185   -16.511 -18.931 1.00 32.40  ? 33  VAL A C   1 
ATOM   254  O O   . VAL A 1 34 ? 6.357   -16.586 -17.717 1.00 37.57  ? 33  VAL A O   1 
ATOM   255  C CB  . VAL A 1 34 ? 6.118   -18.942 -19.678 1.00 36.23  ? 33  VAL A CB  1 
ATOM   256  C CG1 . VAL A 1 34 ? 4.591   -18.833 -19.709 1.00 32.96  ? 33  VAL A CG1 1 
ATOM   257  C CG2 . VAL A 1 34 ? 6.610   -19.903 -20.764 1.00 36.85  ? 33  VAL A CG2 1 
ATOM   258  N N   . LYS A 1 35 ? 5.487   -15.533 -19.520 1.00 31.10  ? 34  LYS A N   1 
ATOM   259  C CA  . LYS A 1 35 ? 4.837   -14.450 -18.789 1.00 35.97  ? 34  LYS A CA  1 
ATOM   260  C C   . LYS A 1 35 ? 3.512   -14.951 -18.207 1.00 38.29  ? 34  LYS A C   1 
ATOM   261  O O   . LYS A 1 35 ? 2.887   -15.849 -18.761 1.00 31.85  ? 34  LYS A O   1 
ATOM   262  C CB  . LYS A 1 35 ? 4.550   -13.245 -19.693 1.00 36.67  ? 34  LYS A CB  1 
ATOM   263  C CG  . LYS A 1 35 ? 5.836   -12.521 -20.143 1.00 35.36  ? 34  LYS A CG  1 
ATOM   264  C CD  . LYS A 1 35 ? 5.633   -11.323 -21.072 1.00 41.78  ? 34  LYS A CD  1 
ATOM   265  C CE  . LYS A 1 35 ? 5.388   -11.777 -22.474 1.00 40.31  ? 34  LYS A CE  1 
ATOM   266  N NZ  . LYS A 1 35 ? 5.158   -10.636 -23.358 1.00 42.92  ? 34  LYS A NZ  1 
ATOM   267  N N   . PRO A 1 36 ? 3.049   -14.394 -17.065 1.00 35.65  ? 35  PRO A N   1 
ATOM   268  C CA  . PRO A 1 36 ? 1.732   -14.748 -16.519 1.00 32.69  ? 35  PRO A CA  1 
ATOM   269  C C   . PRO A 1 36 ? 0.598   -14.210 -17.387 1.00 35.55  ? 35  PRO A C   1 
ATOM   270  O O   . PRO A 1 36 ? 0.786   -13.271 -18.157 1.00 36.75  ? 35  PRO A O   1 
ATOM   271  C CB  . PRO A 1 36 ? 1.695   -14.087 -15.107 1.00 32.93  ? 35  PRO A CB  1 
ATOM   272  C CG  . PRO A 1 36 ? 2.858   -13.091 -15.073 1.00 36.65  ? 35  PRO A CG  1 
ATOM   273  C CD  . PRO A 1 36 ? 3.784   -13.430 -16.236 1.00 37.56  ? 35  PRO A CD  1 
ATOM   274  N N   . PRO A 1 37 ? -0.643  -14.718 -17.236 1.00 36.24  ? 36  PRO A N   1 
ATOM   275  C CA  . PRO A 1 37 ? -1.806  -14.073 -17.861 1.00 38.84  ? 36  PRO A CA  1 
ATOM   276  C C   . PRO A 1 37 ? -2.027  -12.669 -17.318 1.00 42.14  ? 36  PRO A C   1 
ATOM   277  O O   . PRO A 1 37 ? -1.487  -12.314 -16.261 1.00 34.58  ? 36  PRO A O   1 
ATOM   278  C CB  . PRO A 1 37 ? -2.999  -15.006 -17.537 1.00 37.71  ? 36  PRO A CB  1 
ATOM   279  C CG  . PRO A 1 37 ? -2.347  -16.311 -17.070 1.00 35.17  ? 36  PRO A CG  1 
ATOM   280  C CD  . PRO A 1 37 ? -0.981  -15.957 -16.515 1.00 37.12  ? 36  PRO A CD  1 
ATOM   281  N N   . PRO A 1 38 ? -2.793  -11.822 -18.046 1.00 41.30  ? 37  PRO A N   1 
ATOM   282  C CA  . PRO A 1 38 ? -3.196  -10.503 -17.543 1.00 42.79  ? 37  PRO A CA  1 
ATOM   283  C C   . PRO A 1 38 ? -3.749  -10.555 -16.119 1.00 35.39  ? 37  PRO A C   1 
ATOM   284  O O   . PRO A 1 38 ? -4.460  -11.479 -15.762 1.00 38.88  ? 37  PRO A O   1 
ATOM   285  C CB  . PRO A 1 38 ? -4.258  -10.000 -18.537 1.00 43.16  ? 37  PRO A CB  1 
ATOM   286  C CG  . PRO A 1 38 ? -4.395  -11.104 -19.579 1.00 39.35  ? 37  PRO A CG  1 
ATOM   287  C CD  . PRO A 1 38 ? -3.244  -12.072 -19.429 1.00 45.80  ? 37  PRO A CD  1 
ATOM   288  N N   . ASN A 1 39 ? -3.367  -9.563  -15.317 1.00 40.40  ? 38  ASN A N   1 
ATOM   289  C CA  . ASN A 1 39 ? -3.819  -9.378  -13.948 1.00 44.19  ? 38  ASN A CA  1 
ATOM   290  C C   . ASN A 1 39 ? -3.285  -10.452 -13.003 1.00 42.08  ? 38  ASN A C   1 
ATOM   291  O O   . ASN A 1 39 ? -3.677  -10.424 -11.835 1.00 42.86  ? 38  ASN A O   1 
ATOM   292  C CB  . ASN A 1 39 ? -5.328  -9.181  -13.861 1.00 48.20  ? 38  ASN A CB  1 
ATOM   293  C CG  . ASN A 1 39 ? -5.740  -8.034  -14.747 1.00 49.44  ? 38  ASN A CG  1 
ATOM   294  O OD1 . ASN A 1 39 ? -5.475  -6.873  -14.417 1.00 48.00  ? 38  ASN A OD1 1 
ATOM   295  N ND2 . ASN A 1 39 ? -6.309  -8.344  -15.902 1.00 52.16  ? 38  ASN A ND2 1 
ATOM   296  N N   . LYS A 1 40 ? -2.404  -11.359 -13.488 1.00 33.93  ? 39  LYS A N   1 
ATOM   297  C CA  . LYS A 1 40 ? -1.831  -12.405 -12.638 1.00 30.98  ? 39  LYS A CA  1 
ATOM   298  C C   . LYS A 1 40 ? -0.333  -12.148 -12.402 1.00 30.22  ? 39  LYS A C   1 
ATOM   299  O O   . LYS A 1 40 ? 0.336   -11.452 -13.176 1.00 32.07  ? 39  LYS A O   1 
ATOM   300  C CB  . LYS A 1 40 ? -2.075  -13.831 -13.148 1.00 31.32  ? 39  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 40 ? -3.531  -14.217 -13.435 1.00 38.73  ? 39  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 40 ? -4.468  -13.833 -12.299 1.00 41.69  ? 39  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 40 ? -5.927  -14.151 -12.540 1.00 46.90  ? 39  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 40 ? -6.068  -15.607 -12.630 1.00 45.91  ? 39  LYS A NZ  1 
ATOM   305  N N   . TYR A 1 41 ? 0.171   -12.678 -11.284 1.00 23.68  ? 40  TYR A N   1 
ATOM   306  C CA  . TYR A 1 41 ? 1.553   -12.485 -10.874 1.00 22.58  ? 40  TYR A CA  1 
ATOM   307  C C   . TYR A 1 41 ? 2.177   -13.864 -10.795 1.00 22.53  ? 40  TYR A C   1 
ATOM   308  O O   . TYR A 1 41 ? 1.504   -14.823 -10.421 1.00 22.76  ? 40  TYR A O   1 
ATOM   309  C CB  . TYR A 1 41 ? 1.613   -11.885 -9.455  1.00 23.63  ? 40  TYR A CB  1 
ATOM   310  C CG  . TYR A 1 41 ? 1.171   -10.442 -9.437  1.00 25.76  ? 40  TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 41 ? -0.184  -10.129 -9.307  1.00 29.58  ? 40  TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 41 ? 2.067   -9.404  -9.657  1.00 29.02  ? 40  TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 41 ? -0.618  -8.815  -9.338  1.00 30.23  ? 40  TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 41 ? 1.648   -8.082  -9.693  1.00 31.05  ? 40  TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 41 ? 0.299   -7.803  -9.531  1.00 32.84  ? 40  TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 41 ? -0.193  -6.540  -9.567  1.00 34.67  ? 40  TYR A OH  1 
ATOM   317  N N   . PRO A 1 42 ? 3.486   -14.018 -11.094 1.00 24.72  ? 41  PRO A N   1 
ATOM   318  C CA  . PRO A 1 42 ? 4.146   -15.304 -10.887 1.00 21.82  ? 41  PRO A CA  1 
ATOM   319  C C   . PRO A 1 42 ? 4.441   -15.493 -9.401  1.00 21.74  ? 41  PRO A C   1 
ATOM   320  O O   . PRO A 1 42 ? 5.096   -14.638 -8.807  1.00 25.67  ? 41  PRO A O   1 
ATOM   321  C CB  . PRO A 1 42 ? 5.439   -15.207 -11.669 1.00 23.73  ? 41  PRO A CB  1 
ATOM   322  C CG  . PRO A 1 42 ? 5.687   -13.730 -11.815 1.00 24.51  ? 41  PRO A CG  1 
ATOM   323  C CD  . PRO A 1 42 ? 4.385   -12.948 -11.560 1.00 27.46  ? 41  PRO A CD  1 
ATOM   324  N N   . ILE A 1 43 ? 3.878   -16.542 -8.804  1.00 22.23  ? 42  ILE A N   1 
ATOM   325  C CA  . ILE A 1 43 ? 4.056   -16.711 -7.365  1.00 22.08  ? 42  ILE A CA  1 
ATOM   326  C C   . ILE A 1 43 ? 5.029   -17.864 -7.145  1.00 23.46  ? 42  ILE A C   1 
ATOM   327  O O   . ILE A 1 43 ? 4.768   -18.999 -7.572  1.00 26.70  ? 42  ILE A O   1 
ATOM   328  C CB  . ILE A 1 43 ? 2.716   -16.946 -6.645  1.00 21.44  ? 42  ILE A CB  1 
ATOM   329  C CG1 . ILE A 1 43 ? 1.717   -15.775 -6.919  1.00 20.29  ? 42  ILE A CG1 1 
ATOM   330  C CG2 . ILE A 1 43 ? 2.991   -17.104 -5.128  1.00 20.83  ? 42  ILE A CG2 1 
ATOM   331  C CD1 . ILE A 1 43 ? 2.296   -14.396 -6.580  1.00 20.72  ? 42  ILE A CD1 1 
ATOM   332  N N   . PHE A 1 44 ? 6.100   -17.613 -6.382  1.00 22.20  ? 43  PHE A N   1 
ATOM   333  C CA  . PHE A 1 44 ? 7.043   -18.671 -6.036  1.00 20.58  ? 43  PHE A CA  1 
ATOM   334  C C   . PHE A 1 44 ? 6.774   -19.110 -4.599  1.00 22.42  ? 43  PHE A C   1 
ATOM   335  O O   . PHE A 1 44 ? 6.818   -18.284 -3.692  1.00 22.96  ? 43  PHE A O   1 
ATOM   336  C CB  . PHE A 1 44 ? 8.491   -18.173 -6.188  1.00 21.36  ? 43  PHE A CB  1 
ATOM   337  C CG  . PHE A 1 44 ? 9.530   -19.201 -5.744  1.00 24.86  ? 43  PHE A CG  1 
ATOM   338  C CD1 . PHE A 1 44 ? 9.948   -20.202 -6.625  1.00 28.81  ? 43  PHE A CD1 1 
ATOM   339  C CD2 . PHE A 1 44 ? 10.065  -19.186 -4.452  1.00 28.44  ? 43  PHE A CD2 1 
ATOM   340  C CE1 . PHE A 1 44 ? 10.889  -21.147 -6.235  1.00 31.13  ? 43  PHE A CE1 1 
ATOM   341  C CE2 . PHE A 1 44 ? 10.993  -20.156 -4.059  1.00 30.85  ? 43  PHE A CE2 1 
ATOM   342  C CZ  . PHE A 1 44 ? 11.418  -21.125 -4.955  1.00 29.45  ? 43  PHE A CZ  1 
ATOM   343  N N   . PHE A 1 45 ? 6.431   -20.396 -4.411  1.00 24.02  ? 44  PHE A N   1 
ATOM   344  C CA  . PHE A 1 45 ? 5.999   -20.887 -3.103  1.00 21.90  ? 44  PHE A CA  1 
ATOM   345  C C   . PHE A 1 45 ? 7.267   -21.372 -2.421  1.00 23.06  ? 44  PHE A C   1 
ATOM   346  O O   . PHE A 1 45 ? 7.968   -22.239 -2.971  1.00 24.40  ? 44  PHE A O   1 
ATOM   347  C CB  . PHE A 1 45 ? 5.012   -22.072 -3.206  1.00 24.42  ? 44  PHE A CB  1 
ATOM   348  C CG  . PHE A 1 45 ? 3.637   -21.597 -3.667  1.00 24.48  ? 44  PHE A CG  1 
ATOM   349  C CD1 . PHE A 1 45 ? 3.358   -21.439 -5.031  1.00 27.49  ? 44  PHE A CD1 1 
ATOM   350  C CD2 . PHE A 1 45 ? 2.662   -21.244 -2.740  1.00 26.41  ? 44  PHE A CD2 1 
ATOM   351  C CE1 . PHE A 1 45 ? 2.136   -20.916 -5.453  1.00 26.95  ? 44  PHE A CE1 1 
ATOM   352  C CE2 . PHE A 1 45 ? 1.437   -20.738 -3.161  1.00 28.33  ? 44  PHE A CE2 1 
ATOM   353  C CZ  . PHE A 1 45 ? 1.172   -20.590 -4.513  1.00 30.23  ? 44  PHE A CZ  1 
ATOM   354  N N   . PHE A 1 46 ? 7.551   -20.839 -1.228  1.00 21.34  ? 45  PHE A N   1 
ATOM   355  C CA  . PHE A 1 46 ? 8.701   -21.347 -0.483  1.00 25.27  ? 45  PHE A CA  1 
ATOM   356  C C   . PHE A 1 46 ? 8.461   -22.792 -0.033  1.00 23.42  ? 45  PHE A C   1 
ATOM   357  O O   . PHE A 1 46 ? 7.322   -23.244 0.127   1.00 25.93  ? 45  PHE A O   1 
ATOM   358  C CB  . PHE A 1 46 ? 9.017   -20.426 0.715   1.00 22.16  ? 45  PHE A CB  1 
ATOM   359  C CG  . PHE A 1 46 ? 9.457   -19.021 0.320   1.00 23.32  ? 45  PHE A CG  1 
ATOM   360  C CD1 . PHE A 1 46 ? 10.684  -18.802 -0.310  1.00 21.80  ? 45  PHE A CD1 1 
ATOM   361  C CD2 . PHE A 1 46 ? 8.679   -17.899 0.627   1.00 22.93  ? 45  PHE A CD2 1 
ATOM   362  C CE1 . PHE A 1 46 ? 11.102  -17.512 -0.655  1.00 21.16  ? 45  PHE A CE1 1 
ATOM   363  C CE2 . PHE A 1 46 ? 9.098   -16.601 0.267   1.00 22.86  ? 45  PHE A CE2 1 
ATOM   364  C CZ  . PHE A 1 46 ? 10.323  -16.402 -0.375  1.00 22.86  ? 45  PHE A CZ  1 
ATOM   365  N N   . GLY A 1 47 ? 9.555   -23.540 0.158   1.00 25.26  ? 46  GLY A N   1 
ATOM   366  C CA  . GLY A 1 47 ? 9.446   -24.910 0.634   1.00 28.07  ? 46  GLY A CA  1 
ATOM   367  C C   . GLY A 1 47 ? 9.242   -25.886 -0.530  1.00 33.60  ? 46  GLY A C   1 
ATOM   368  O O   . GLY A 1 47 ? 10.097  -26.740 -0.776  1.00 33.36  ? 46  GLY A O   1 
ATOM   369  N N   . THR A 1 48 ? 8.122   -25.751 -1.259  1.00 31.19  ? 47  THR A N   1 
ATOM   370  C CA  . THR A 1 48 ? 7.853   -26.619 -2.395  1.00 32.56  ? 47  THR A CA  1 
ATOM   371  C C   . THR A 1 48 ? 8.680   -26.166 -3.594  1.00 31.91  ? 47  THR A C   1 
ATOM   372  O O   . THR A 1 48 ? 9.022   -26.966 -4.476  1.00 30.21  ? 47  THR A O   1 
ATOM   373  C CB  . THR A 1 48 ? 6.365   -26.639 -2.723  1.00 33.48  ? 47  THR A CB  1 
ATOM   374  O OG1 . THR A 1 48 ? 6.081   -25.275 -3.013  1.00 34.32  ? 47  THR A OG1 1 
ATOM   375  C CG2 . THR A 1 48 ? 5.498   -27.100 -1.570  1.00 33.88  ? 47  THR A CG2 1 
ATOM   376  N N   . HIS A 1 49 ? 8.937   -24.853 -3.668  1.00 27.96  ? 48  HIS A N   1 
ATOM   377  C CA  . HIS A 1 49 ? 9.647   -24.245 -4.791  1.00 29.43  ? 48  HIS A CA  1 
ATOM   378  C C   . HIS A 1 49 ? 8.872   -24.315 -6.105  1.00 29.80  ? 48  HIS A C   1 
ATOM   379  O O   . HIS A 1 49 ? 9.476   -24.206 -7.173  1.00 33.79  ? 48  HIS A O   1 
ATOM   380  C CB  . HIS A 1 49 ? 11.100  -24.749 -4.900  1.00 31.19  ? 48  HIS A CB  1 
ATOM   381  C CG  . HIS A 1 49 ? 11.820  -24.791 -3.592  1.00 32.73  ? 48  HIS A CG  1 
ATOM   382  N ND1 . HIS A 1 49 ? 12.593  -25.856 -3.205  1.00 33.24  ? 48  HIS A ND1 1 
ATOM   383  C CD2 . HIS A 1 49 ? 11.887  -23.891 -2.570  1.00 32.82  ? 48  HIS A CD2 1 
ATOM   384  C CE1 . HIS A 1 49 ? 13.101  -25.618 -1.995  1.00 39.89  ? 48  HIS A CE1 1 
ATOM   385  N NE2 . HIS A 1 49 ? 12.716  -24.416 -1.605  1.00 33.22  ? 48  HIS A NE2 1 
ATOM   386  N N   . GLU A 1 50 ? 7.543   -24.454 -6.033  1.00 31.09  ? 49  GLU A N   1 
ATOM   387  C CA  . GLU A 1 50 ? 6.676   -24.463 -7.207  1.00 34.04  ? 49  GLU A CA  1 
ATOM   388  C C   . GLU A 1 50 ? 6.183   -23.054 -7.516  1.00 30.61  ? 49  GLU A C   1 
ATOM   389  O O   . GLU A 1 50 ? 6.200   -22.200 -6.638  1.00 29.13  ? 49  GLU A O   1 
ATOM   390  C CB  . GLU A 1 50 ? 5.499   -25.367 -6.857  1.00 37.74  ? 49  GLU A CB  1 
ATOM   391  C CG  . GLU A 1 50 ? 5.950   -26.813 -6.687  1.00 45.81  ? 49  GLU A CG  1 
ATOM   392  C CD  . GLU A 1 50 ? 4.888   -27.746 -6.148  1.00 54.44  ? 49  GLU A CD  1 
ATOM   393  O OE1 . GLU A 1 50 ? 3.690   -27.369 -6.064  1.00 56.95  ? 49  GLU A OE1 1 
ATOM   394  O OE2 . GLU A 1 50 ? 5.303   -28.865 -5.775  1.00 62.28  ? 49  GLU A OE2 1 
ATOM   395  N N   . THR A 1 51 ? 5.849   -22.803 -8.791  1.00 27.24  ? 50  THR A N   1 
ATOM   396  C CA  . THR A 1 51 ? 5.303   -21.523 -9.226  1.00 28.28  ? 50  THR A CA  1 
ATOM   397  C C   . THR A 1 51 ? 3.863   -21.732 -9.662  1.00 28.34  ? 50  THR A C   1 
ATOM   398  O O   . THR A 1 51 ? 3.579   -22.723 -10.330 1.00 32.92  ? 50  THR A O   1 
ATOM   399  C CB  . THR A 1 51 ? 6.138   -20.943 -10.378 1.00 31.49  ? 50  THR A CB  1 
ATOM   400  O OG1 . THR A 1 51 ? 7.432   -20.635 -9.866  1.00 31.38  ? 50  THR A OG1 1 
ATOM   401  C CG2 . THR A 1 51 ? 5.529   -19.674 -10.969 1.00 30.31  ? 50  THR A CG2 1 
ATOM   402  N N   . ALA A 1 52 ? 2.978   -20.793 -9.293  1.00 25.36  ? 51  ALA A N   1 
ATOM   403  C CA  . ALA A 1 52 ? 1.655   -20.685 -9.889  1.00 27.65  ? 51  ALA A CA  1 
ATOM   404  C C   . ALA A 1 52 ? 1.381   -19.215 -10.200 1.00 28.65  ? 51  ALA A C   1 
ATOM   405  O O   . ALA A 1 52 ? 2.062   -18.323 -9.689  1.00 25.99  ? 51  ALA A O   1 
ATOM   406  C CB  . ALA A 1 52 ? 0.559   -21.287 -9.002  1.00 27.70  ? 51  ALA A CB  1 
ATOM   407  N N   . PHE A 1 53 ? 0.359   -18.966 -11.034 1.00 25.99  ? 52  PHE A N   1 
ATOM   408  C CA  . PHE A 1 53 ? -0.020  -17.608 -11.379 1.00 28.77  ? 52  PHE A CA  1 
ATOM   409  C C   . PHE A 1 53 ? -1.253  -17.237 -10.574 1.00 30.07  ? 52  PHE A C   1 
ATOM   410  O O   . PHE A 1 53 ? -2.272  -17.933 -10.673 1.00 33.71  ? 52  PHE A O   1 
ATOM   411  C CB  . PHE A 1 53 ? -0.272  -17.615 -12.894 1.00 28.68  ? 52  PHE A CB  1 
ATOM   412  C CG  . PHE A 1 53 ? 1.004   -17.825 -13.701 1.00 31.52  ? 52  PHE A CG  1 
ATOM   413  C CD1 . PHE A 1 53 ? 2.108   -16.999 -13.507 1.00 31.45  ? 52  PHE A CD1 1 
ATOM   414  C CD2 . PHE A 1 53 ? 1.069   -18.796 -14.699 1.00 37.11  ? 52  PHE A CD2 1 
ATOM   415  C CE1 . PHE A 1 53 ? 3.273   -17.191 -14.253 1.00 42.58  ? 52  PHE A CE1 1 
ATOM   416  C CE2 . PHE A 1 53 ? 2.230   -18.982 -15.446 1.00 36.90  ? 52  PHE A CE2 1 
ATOM   417  C CZ  . PHE A 1 53 ? 3.329   -18.183 -15.225 1.00 39.81  ? 52  PHE A CZ  1 
ATOM   418  N N   . LEU A 1 54 ? -1.174  -16.141 -9.798  1.00 27.05  ? 53  LEU A N   1 
ATOM   419  C CA  . LEU A 1 54 ? -2.284  -15.788 -8.923  1.00 27.78  ? 53  LEU A CA  1 
ATOM   420  C C   . LEU A 1 54 ? -2.601  -14.302 -9.024  1.00 27.73  ? 53  LEU A C   1 
ATOM   421  O O   . LEU A 1 54 ? -1.718  -13.499 -9.307  1.00 27.09  ? 53  LEU A O   1 
ATOM   422  C CB  . LEU A 1 54 ? -1.991  -16.161 -7.462  1.00 27.71  ? 53  LEU A CB  1 
ATOM   423  C CG  . LEU A 1 54 ? -1.949  -17.659 -7.122  1.00 28.01  ? 53  LEU A CG  1 
ATOM   424  C CD1 . LEU A 1 54 ? -1.626  -17.739 -5.634  1.00 29.61  ? 53  LEU A CD1 1 
ATOM   425  C CD2 . LEU A 1 54 ? -3.329  -18.263 -7.367  1.00 35.79  ? 53  LEU A CD2 1 
ATOM   426  N N   . GLY A 1 55 ? -3.877  -13.941 -8.768  1.00 25.28  ? 54  GLY A N   1 
ATOM   427  C CA  . GLY A 1 55 ? -4.251  -12.525 -8.712  1.00 22.43  ? 54  GLY A CA  1 
ATOM   428  C C   . GLY A 1 55 ? -4.244  -12.029 -7.257  1.00 22.65  ? 54  GLY A C   1 
ATOM   429  O O   . GLY A 1 55 ? -4.167  -12.849 -6.335  1.00 23.33  ? 54  GLY A O   1 
ATOM   430  N N   . PRO A 1 56 ? -4.315  -10.695 -7.023  1.00 21.90  ? 55  PRO A N   1 
ATOM   431  C CA  . PRO A 1 56 ? -4.248  -10.129 -5.674  1.00 22.98  ? 55  PRO A CA  1 
ATOM   432  C C   . PRO A 1 56 ? -5.218  -10.680 -4.637  1.00 22.98  ? 55  PRO A C   1 
ATOM   433  O O   . PRO A 1 56 ? -4.925  -10.648 -3.448  1.00 22.24  ? 55  PRO A O   1 
ATOM   434  C CB  . PRO A 1 56 ? -4.429  -8.633  -5.905  1.00 25.83  ? 55  PRO A CB  1 
ATOM   435  C CG  . PRO A 1 56 ? -3.884  -8.419  -7.285  1.00 26.25  ? 55  PRO A CG  1 
ATOM   436  C CD  . PRO A 1 56 ? -4.356  -9.645  -8.061  1.00 23.57  ? 55  PRO A CD  1 
ATOM   437  N N   . LYS A 1 57 ? -6.371  -11.199 -5.090  1.00 23.16  ? 56  LYS A N   1 
ATOM   438  C CA  . LYS A 1 57 ? -7.363  -11.719 -4.150  1.00 26.33  ? 56  LYS A CA  1 
ATOM   439  C C   . LYS A 1 57 ? -6.815  -12.878 -3.313  1.00 25.44  ? 56  LYS A C   1 
ATOM   440  O O   . LYS A 1 57 ? -7.280  -13.122 -2.194  1.00 23.82  ? 56  LYS A O   1 
ATOM   441  C CB  . LYS A 1 57 ? -8.636  -12.222 -4.850  1.00 29.00  ? 56  LYS A CB  1 
ATOM   442  C CG  . LYS A 1 57 ? -8.453  -13.497 -5.656  1.00 31.62  ? 56  LYS A CG  1 
ATOM   443  C CD  . LYS A 1 57 ? -9.776  -13.800 -6.378  1.00 44.36  ? 56  LYS A CD  1 
ATOM   444  C CE  . LYS A 1 57 ? -9.738  -15.036 -7.229  1.00 43.33  ? 56  LYS A CE  1 
ATOM   445  N NZ  . LYS A 1 57 ? -9.495  -16.232 -6.411  1.00 47.50  ? 56  LYS A NZ  1 
ATOM   446  N N   . ASP A 1 58 ? -5.781  -13.566 -3.827  1.00 24.15  ? 57  ASP A N   1 
ATOM   447  C CA  . ASP A 1 58 ? -5.172  -14.713 -3.193  1.00 23.61  ? 57  ASP A CA  1 
ATOM   448  C C   . ASP A 1 58 ? -3.829  -14.370 -2.519  1.00 24.48  ? 57  ASP A C   1 
ATOM   449  O O   . ASP A 1 58 ? -3.148  -15.299 -2.075  1.00 23.87  ? 57  ASP A O   1 
ATOM   450  C CB  . ASP A 1 58 ? -5.095  -15.843 -4.215  1.00 25.38  ? 57  ASP A CB  1 
ATOM   451  C CG  . ASP A 1 58 ? -6.482  -16.419 -4.503  1.00 32.60  ? 57  ASP A CG  1 
ATOM   452  O OD1 . ASP A 1 58 ? -7.271  -16.483 -3.533  1.00 30.79  ? 57  ASP A OD1 1 
ATOM   453  O OD2 . ASP A 1 58 ? -6.771  -16.760 -5.672  1.00 29.97  ? 57  ASP A OD2 1 
ATOM   454  N N   . LEU A 1 59 ? -3.476  -13.069 -2.415  1.00 22.47  ? 58  LEU A N   1 
ATOM   455  C CA  . LEU A 1 59 ? -2.136  -12.649 -1.967  1.00 20.06  ? 58  LEU A CA  1 
ATOM   456  C C   . LEU A 1 59 ? -2.265  -11.794 -0.699  1.00 18.70  ? 58  LEU A C   1 
ATOM   457  O O   . LEU A 1 59 ? -2.857  -10.724 -0.729  1.00 22.58  ? 58  LEU A O   1 
ATOM   458  C CB  . LEU A 1 59 ? -1.397  -11.864 -3.056  1.00 19.58  ? 58  LEU A CB  1 
ATOM   459  C CG  . LEU A 1 59 ? -1.297  -12.559 -4.410  1.00 21.23  ? 58  LEU A CG  1 
ATOM   460  C CD1 . LEU A 1 59 ? -0.599  -11.718 -5.435  1.00 22.79  ? 58  LEU A CD1 1 
ATOM   461  C CD2 . LEU A 1 59 ? -0.552  -13.898 -4.234  1.00 21.31  ? 58  LEU A CD2 1 
ATOM   462  N N   . PHE A 1 60 ? -1.738  -12.287 0.420   1.00 19.52  ? 59  PHE A N   1 
ATOM   463  C CA  . PHE A 1 60 ? -1.832  -11.591 1.705   1.00 21.78  ? 59  PHE A CA  1 
ATOM   464  C C   . PHE A 1 60 ? -0.442  -11.140 2.125   1.00 22.42  ? 59  PHE A C   1 
ATOM   465  O O   . PHE A 1 60 ? 0.451   -11.970 2.326   1.00 24.81  ? 59  PHE A O   1 
ATOM   466  C CB  . PHE A 1 60 ? -2.283  -12.642 2.719   1.00 24.31  ? 59  PHE A CB  1 
ATOM   467  C CG  . PHE A 1 60 ? -3.730  -13.072 2.461   1.00 25.00  ? 59  PHE A CG  1 
ATOM   468  C CD1 . PHE A 1 60 ? -4.041  -13.991 1.450   1.00 24.91  ? 59  PHE A CD1 1 
ATOM   469  C CD2 . PHE A 1 60 ? -4.769  -12.522 3.207   1.00 28.36  ? 59  PHE A CD2 1 
ATOM   470  C CE1 . PHE A 1 60 ? -5.362  -14.368 1.210   1.00 30.03  ? 59  PHE A CE1 1 
ATOM   471  C CE2 . PHE A 1 60 ? -6.097  -12.887 2.954   1.00 27.05  ? 59  PHE A CE2 1 
ATOM   472  C CZ  . PHE A 1 60 ? -6.391  -13.822 1.981   1.00 26.00  ? 59  PHE A CZ  1 
ATOM   473  N N   . PRO A 1 61 ? -0.189  -9.824  2.224   1.00 25.39  ? 60  PRO A N   1 
ATOM   474  C CA  . PRO A 1 61 ? 1.162   -9.350  2.588   1.00 24.66  ? 60  PRO A CA  1 
ATOM   475  C C   . PRO A 1 61 ? 1.698   -9.984  3.871   1.00 25.51  ? 60  PRO A C   1 
ATOM   476  O O   . PRO A 1 61 ? 0.992   -10.121 4.870   1.00 25.28  ? 60  PRO A O   1 
ATOM   477  C CB  . PRO A 1 61 ? 0.980   -7.811  2.672   1.00 28.96  ? 60  PRO A CB  1 
ATOM   478  C CG  . PRO A 1 61 ? -0.127  -7.575  1.619   1.00 31.73  ? 60  PRO A CG  1 
ATOM   479  C CD  . PRO A 1 61 ? -1.123  -8.727  1.895   1.00 27.55  ? 60  PRO A CD  1 
ATOM   480  N N   . TYR A 1 62 ? 2.976   -10.393 3.808   1.00 25.61  ? 61  TYR A N   1 
ATOM   481  C CA  . TYR A 1 62 ? 3.586   -11.216 4.841   1.00 24.86  ? 61  TYR A CA  1 
ATOM   482  C C   . TYR A 1 62 ? 3.580   -10.519 6.202   1.00 23.91  ? 61  TYR A C   1 
ATOM   483  O O   . TYR A 1 62 ? 3.183   -11.147 7.185   1.00 28.16  ? 61  TYR A O   1 
ATOM   484  C CB  . TYR A 1 62 ? 4.998   -11.588 4.375   1.00 28.12  ? 61  TYR A CB  1 
ATOM   485  C CG  . TYR A 1 62 ? 5.770   -12.372 5.429   1.00 27.22  ? 61  TYR A CG  1 
ATOM   486  C CD1 . TYR A 1 62 ? 5.512   -13.715 5.653   1.00 26.76  ? 61  TYR A CD1 1 
ATOM   487  C CD2 . TYR A 1 62 ? 6.784   -11.757 6.166   1.00 29.58  ? 61  TYR A CD2 1 
ATOM   488  C CE1 . TYR A 1 62 ? 6.218   -14.438 6.605   1.00 30.68  ? 61  TYR A CE1 1 
ATOM   489  C CE2 . TYR A 1 62 ? 7.498   -12.467 7.124   1.00 30.58  ? 61  TYR A CE2 1 
ATOM   490  C CZ  . TYR A 1 62 ? 7.213   -13.805 7.335   1.00 32.42  ? 61  TYR A CZ  1 
ATOM   491  O OH  . TYR A 1 62 ? 7.914   -14.514 8.264   1.00 37.63  ? 61  TYR A OH  1 
ATOM   492  N N   . ASP A 1 63 ? 4.020   -9.259  6.248   1.00 27.09  ? 62  ASP A N   1 
ATOM   493  C CA  . ASP A 1 63 ? 4.177   -8.598  7.544   1.00 34.16  ? 62  ASP A CA  1 
ATOM   494  C C   . ASP A 1 63 ? 2.848   -8.570  8.305   1.00 34.91  ? 62  ASP A C   1 
ATOM   495  O O   . ASP A 1 63 ? 2.792   -8.985  9.460   1.00 38.90  ? 62  ASP A O   1 
ATOM   496  C CB  . ASP A 1 63 ? 4.908   -7.268  7.438   1.00 37.06  ? 62  ASP A CB  1 
ATOM   497  C CG  . ASP A 1 63 ? 6.422   -7.358  7.253   1.00 54.04  ? 62  ASP A CG  1 
ATOM   498  O OD1 . ASP A 1 63 ? 6.950   -6.597  6.403   1.00 60.81  ? 62  ASP A OD1 1 
ATOM   499  O OD2 . ASP A 1 63 ? 7.075   -8.178  7.966   1.00 63.40  ? 62  ASP A OD2 1 
ATOM   500  N N   . LYS A 1 64 ? 1.777   -8.149  7.624   1.00 36.17  ? 63  LYS A N   1 
ATOM   501  C CA  . LYS A 1 64 ? 0.436   -8.078  8.197   1.00 35.17  ? 63  LYS A CA  1 
ATOM   502  C C   . LYS A 1 64 ? -0.104  -9.448  8.614   1.00 32.57  ? 63  LYS A C   1 
ATOM   503  O O   . LYS A 1 64 ? -0.872  -9.525  9.586   1.00 30.03  ? 63  LYS A O   1 
ATOM   504  C CB  . LYS A 1 64 ? -0.499  -7.383  7.199   1.00 35.89  ? 63  LYS A CB  1 
ATOM   505  C CG  . LYS A 1 64 ? -1.988  -7.349  7.582   1.00 40.36  ? 63  LYS A CG  1 
ATOM   506  C CD  . LYS A 1 64 ? -2.773  -6.529  6.569   1.00 35.99  ? 63  LYS A CD  1 
ATOM   507  C CE  . LYS A 1 64 ? -3.887  -5.730  7.186   1.00 40.75  ? 63  LYS A CE  1 
ATOM   508  N NZ  . LYS A 1 64 ? -4.894  -6.548  7.853   1.00 41.75  ? 63  LYS A NZ  1 
ATOM   509  N N   . SER A 1 65 ? 0.266   -10.525 7.892   1.00 28.68  ? 64  SER A N   1 
ATOM   510  C CA  . SER A 1 65 ? -0.431  -11.811 7.987   1.00 28.44  ? 64  SER A CA  1 
ATOM   511  C C   . SER A 1 65 ? 0.323   -12.879 8.777   1.00 29.24  ? 64  SER A C   1 
ATOM   512  O O   . SER A 1 65 ? -0.232  -13.962 8.988   1.00 29.96  ? 64  SER A O   1 
ATOM   513  C CB  . SER A 1 65 ? -0.705  -12.360 6.596   1.00 29.62  ? 64  SER A CB  1 
ATOM   514  O OG  . SER A 1 65 ? -1.560  -11.445 5.936   1.00 41.04  ? 64  SER A OG  1 
ATOM   515  N N   . LYS A 1 66 ? 1.593   -12.620 9.132   1.00 30.55  ? 65  LYS A N   1 
ATOM   516  C CA  . LYS A 1 66 ? 2.450   -13.699 9.635   1.00 35.22  ? 65  LYS A CA  1 
ATOM   517  C C   . LYS A 1 66 ? 1.978   -14.211 11.003  1.00 32.56  ? 65  LYS A C   1 
ATOM   518  O O   . LYS A 1 66 ? 2.107   -15.404 11.304  1.00 34.20  ? 65  LYS A O   1 
ATOM   519  C CB  . LYS A 1 66 ? 3.952   -13.371 9.613   1.00 37.63  ? 65  LYS A CB  1 
ATOM   520  C CG  . LYS A 1 66 ? 4.348   -12.224 10.522  1.00 41.18  ? 65  LYS A CG  1 
ATOM   521  C CD  . LYS A 1 66 ? 5.861   -12.058 10.519  1.00 51.55  ? 65  LYS A CD  1 
ATOM   522  C CE  . LYS A 1 66 ? 6.304   -10.779 11.179  1.00 58.98  ? 65  LYS A CE  1 
ATOM   523  N NZ  . LYS A 1 66 ? 6.113   -9.605  10.318  1.00 67.41  ? 65  LYS A NZ  1 
ATOM   524  N N   A ASP A 1 67 ? 1.366   -13.332 11.807  0.50 33.42  ? 66  ASP A N   1 
ATOM   525  N N   B ASP A 1 67 ? 1.412   -13.316 11.817  0.50 33.25  ? 66  ASP A N   1 
ATOM   526  C CA  A ASP A 1 67 ? 0.879   -13.748 13.119  0.50 35.53  ? 66  ASP A CA  1 
ATOM   527  C CA  B ASP A 1 67 ? 0.885   -13.773 13.093  0.50 35.17  ? 66  ASP A CA  1 
ATOM   528  C C   A ASP A 1 67 ? -0.311  -14.706 12.987  0.50 34.91  ? 66  ASP A C   1 
ATOM   529  C C   B ASP A 1 67 ? -0.144  -14.877 12.850  0.50 34.92  ? 66  ASP A C   1 
ATOM   530  O O   A ASP A 1 67 ? -0.591  -15.500 13.876  0.50 37.81  ? 66  ASP A O   1 
ATOM   531  O O   B ASP A 1 67 ? -0.121  -15.924 13.495  0.50 35.02  ? 66  ASP A O   1 
ATOM   532  C CB  A ASP A 1 67 ? 0.636   -12.561 14.038  0.50 37.28  ? 66  ASP A CB  1 
ATOM   533  C CB  B ASP A 1 67 ? 0.266   -12.646 13.900  0.50 36.85  ? 66  ASP A CB  1 
ATOM   534  C CG  A ASP A 1 67 ? 1.889   -11.901 14.599  0.50 40.36  ? 66  ASP A CG  1 
ATOM   535  C CG  B ASP A 1 67 ? -0.111  -13.052 15.314  0.50 40.15  ? 66  ASP A CG  1 
ATOM   536  O OD1 A ASP A 1 67 ? 2.993   -12.460 14.401  0.50 41.74  ? 66  ASP A OD1 1 
ATOM   537  O OD1 B ASP A 1 67 ? 0.796   -13.061 16.175  0.50 40.98  ? 66  ASP A OD1 1 
ATOM   538  O OD2 A ASP A 1 67 ? 1.757   -10.819 15.217  0.50 42.35  ? 66  ASP A OD2 1 
ATOM   539  O OD2 B ASP A 1 67 ? -1.294  -13.404 15.521  0.50 46.31  ? 66  ASP A OD2 1 
ATOM   540  N N   . LYS A 1 68 ? -1.012  -14.664 11.856  1.00 34.96  ? 67  LYS A N   1 
ATOM   541  C CA  . LYS A 1 68 ? -2.115  -15.580 11.633  1.00 33.56  ? 67  LYS A CA  1 
ATOM   542  C C   . LYS A 1 68 ? -1.662  -16.854 10.927  1.00 35.78  ? 67  LYS A C   1 
ATOM   543  O O   . LYS A 1 68 ? -2.117  -17.949 11.253  1.00 34.47  ? 67  LYS A O   1 
ATOM   544  C CB  . LYS A 1 68 ? -3.173  -14.813 10.840  1.00 36.27  ? 67  LYS A CB  1 
ATOM   545  C CG  . LYS A 1 68 ? -4.497  -15.512 10.683  1.00 43.71  ? 67  LYS A CG  1 
ATOM   546  C CD  . LYS A 1 68 ? -5.466  -14.520 10.036  1.00 45.25  ? 67  LYS A CD  1 
ATOM   547  C CE  . LYS A 1 68 ? -6.780  -15.141 9.680   1.00 53.44  ? 67  LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 68 ? -7.745  -14.157 9.173   1.00 47.56  ? 67  LYS A NZ  1 
ATOM   549  N N   . TYR A 1 69 ? -0.771  -16.713 9.947   1.00 32.63  ? 68  TYR A N   1 
ATOM   550  C CA  . TYR A 1 69 ? -0.595  -17.785 8.982   1.00 31.65  ? 68  TYR A CA  1 
ATOM   551  C C   . TYR A 1 69 ? 0.775   -18.444 9.142   1.00 31.19  ? 68  TYR A C   1 
ATOM   552  O O   . TYR A 1 69 ? 0.995   -19.521 8.584   1.00 34.41  ? 68  TYR A O   1 
ATOM   553  C CB  . TYR A 1 69 ? -0.759  -17.299 7.533   1.00 27.65  ? 68  TYR A CB  1 
ATOM   554  C CG  . TYR A 1 69 ? -2.165  -16.862 7.140   1.00 30.56  ? 68  TYR A CG  1 
ATOM   555  C CD1 . TYR A 1 69 ? -3.305  -17.600 7.479   1.00 34.38  ? 68  TYR A CD1 1 
ATOM   556  C CD2 . TYR A 1 69 ? -2.352  -15.697 6.394   1.00 32.22  ? 68  TYR A CD2 1 
ATOM   557  C CE1 . TYR A 1 69 ? -4.585  -17.163 7.140   1.00 34.31  ? 68  TYR A CE1 1 
ATOM   558  C CE2 . TYR A 1 69 ? -3.623  -15.263 6.034   1.00 33.77  ? 68  TYR A CE2 1 
ATOM   559  C CZ  . TYR A 1 69 ? -4.739  -16.004 6.392   1.00 34.86  ? 68  TYR A CZ  1 
ATOM   560  O OH  . TYR A 1 69 ? -5.962  -15.535 5.995   1.00 34.52  ? 68  TYR A OH  1 
ATOM   561  N N   . GLY A 1 70 ? 1.682   -17.806 9.880   1.00 29.26  ? 69  GLY A N   1 
ATOM   562  C CA  . GLY A 1 70 ? 3.065   -18.273 9.912   1.00 33.01  ? 69  GLY A CA  1 
ATOM   563  C C   . GLY A 1 70 ? 3.318   -19.213 11.098  1.00 34.66  ? 69  GLY A C   1 
ATOM   564  O O   . GLY A 1 70 ? 4.102   -18.908 11.983  1.00 38.26  ? 69  GLY A O   1 
ATOM   565  N N   . LYS A 1 71 ? 2.609   -20.339 11.117  1.00 39.47  ? 70  LYS A N   1 
ATOM   566  C CA  . LYS A 1 71 ? 2.725   -21.329 12.178  1.00 39.83  ? 70  LYS A CA  1 
ATOM   567  C C   . LYS A 1 71 ? 2.961   -22.676 11.505  1.00 37.50  ? 70  LYS A C   1 
ATOM   568  O O   . LYS A 1 71 ? 2.534   -22.863 10.369  1.00 33.80  ? 70  LYS A O   1 
ATOM   569  C CB  . LYS A 1 71 ? 1.472   -21.323 13.067  1.00 43.61  ? 70  LYS A CB  1 
ATOM   570  C CG  . LYS A 1 71 ? 1.253   -20.030 13.866  1.00 46.96  ? 70  LYS A CG  1 
ATOM   571  C CD  . LYS A 1 71 ? -0.118  -19.893 14.522  1.00 54.16  ? 70  LYS A CD  1 
ATOM   572  N N   . PRO A 1 72 ? 3.674   -23.638 12.148  1.00 35.68  ? 71  PRO A N   1 
ATOM   573  C CA  . PRO A 1 72 ? 3.982   -24.916 11.504  1.00 34.81  ? 71  PRO A CA  1 
ATOM   574  C C   . PRO A 1 72 ? 2.725   -25.604 10.994  1.00 34.18  ? 71  PRO A C   1 
ATOM   575  O O   . PRO A 1 72 ? 1.668   -25.460 11.586  1.00 38.15  ? 71  PRO A O   1 
ATOM   576  C CB  . PRO A 1 72 ? 4.656   -25.709 12.642  1.00 40.15  ? 71  PRO A CB  1 
ATOM   577  C CG  . PRO A 1 72 ? 5.311   -24.622 13.481  1.00 42.30  ? 71  PRO A CG  1 
ATOM   578  C CD  . PRO A 1 72 ? 4.254   -23.516 13.497  1.00 36.78  ? 71  PRO A CD  1 
ATOM   579  N N   . ASN A 1 73 ? 2.869   -26.351 9.900   1.00 36.76  ? 72  ASN A N   1 
ATOM   580  C CA  . ASN A 1 73 ? 1.778   -27.068 9.273   1.00 41.39  ? 72  ASN A CA  1 
ATOM   581  C C   . ASN A 1 73 ? 2.298   -28.434 8.835   1.00 47.65  ? 72  ASN A C   1 
ATOM   582  O O   . ASN A 1 73 ? 3.455   -28.563 8.437   1.00 45.86  ? 72  ASN A O   1 
ATOM   583  C CB  . ASN A 1 73 ? 1.230   -26.234 8.117   1.00 44.50  ? 72  ASN A CB  1 
ATOM   584  C CG  . ASN A 1 73 ? -0.105  -26.724 7.621   1.00 48.07  ? 72  ASN A CG  1 
ATOM   585  O OD1 . ASN A 1 73 ? -0.158  -27.651 6.815   1.00 47.87  ? 72  ASN A OD1 1 
ATOM   586  N ND2 . ASN A 1 73 ? -1.188  -26.080 8.031   1.00 50.10  ? 72  ASN A ND2 1 
ATOM   587  N N   . LYS A 1 74 ? 1.420   -29.445 8.886   1.00 49.38  ? 73  LYS A N   1 
ATOM   588  C CA  . LYS A 1 74 ? 1.751   -30.812 8.522   1.00 49.09  ? 73  LYS A CA  1 
ATOM   589  C C   . LYS A 1 74 ? 2.254   -30.883 7.080   1.00 50.09  ? 73  LYS A C   1 
ATOM   590  O O   . LYS A 1 74 ? 3.129   -31.691 6.762   1.00 47.75  ? 73  LYS A O   1 
ATOM   591  C CB  . LYS A 1 74 ? 0.531   -31.708 8.787   1.00 52.33  ? 73  LYS A CB  1 
ATOM   592  C CG  . LYS A 1 74 ? -0.486  -31.853 7.642   1.00 53.14  ? 73  LYS A CG  1 
ATOM   593  N N   . ARG A 1 75 ? 1.718   -30.016 6.209   1.00 46.24  ? 74  ARG A N   1 
ATOM   594  C CA  . ARG A 1 75 ? 1.851   -30.193 4.768   1.00 45.27  ? 74  ARG A CA  1 
ATOM   595  C C   . ARG A 1 75 ? 3.317   -30.189 4.337   1.00 41.94  ? 74  ARG A C   1 
ATOM   596  O O   . ARG A 1 75 ? 4.141   -29.468 4.912   1.00 41.28  ? 74  ARG A O   1 
ATOM   597  C CB  . ARG A 1 75 ? 0.975   -29.186 4.006   1.00 46.85  ? 74  ARG A CB  1 
ATOM   598  C CG  . ARG A 1 75 ? -0.511  -29.383 4.259   1.00 52.20  ? 74  ARG A CG  1 
ATOM   599  C CD  . ARG A 1 75 ? -1.099  -30.521 3.430   1.00 50.03  ? 74  ARG A CD  1 
ATOM   600  N NE  . ARG A 1 75 ? -1.996  -30.025 2.379   1.00 66.72  ? 74  ARG A NE  1 
ATOM   601  C CZ  . ARG A 1 75 ? -3.155  -29.390 2.620   1.00 67.88  ? 74  ARG A CZ  1 
ATOM   602  N NH1 . ARG A 1 75 ? -3.947  -29.067 1.612   1.00 59.73  ? 74  ARG A NH1 1 
ATOM   603  N NH2 . ARG A 1 75 ? -3.539  -29.106 3.864   1.00 66.01  ? 74  ARG A NH2 1 
ATOM   604  N N   . LYS A 1 76 ? 3.611   -30.997 3.308   1.00 40.03  ? 75  LYS A N   1 
ATOM   605  C CA  . LYS A 1 76 ? 4.955   -31.195 2.789   1.00 42.21  ? 75  LYS A CA  1 
ATOM   606  C C   . LYS A 1 76 ? 5.505   -29.860 2.301   1.00 36.95  ? 75  LYS A C   1 
ATOM   607  O O   . LYS A 1 76 ? 4.932   -29.235 1.411   1.00 33.96  ? 75  LYS A O   1 
ATOM   608  C CB  . LYS A 1 76 ? 4.940   -32.095 1.550   1.00 40.71  ? 75  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 76 ? 6.238   -32.313 0.788   1.00 46.39  ? 75  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 76 ? 6.153   -33.517 -0.155  1.00 51.42  ? 75  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 76 ? 7.454   -33.972 -0.767  1.00 48.81  ? 75  LYS A CE  1 
ATOM   612  N N   . GLY A 1 77 ? 6.656   -29.473 2.849   1.00 36.57  ? 76  GLY A N   1 
ATOM   613  C CA  . GLY A 1 77 ? 7.346   -28.307 2.336   1.00 31.70  ? 76  GLY A CA  1 
ATOM   614  C C   . GLY A 1 77 ? 6.989   -27.060 3.139   1.00 32.14  ? 76  GLY A C   1 
ATOM   615  O O   . GLY A 1 77 ? 7.692   -26.068 3.051   1.00 30.75  ? 76  GLY A O   1 
ATOM   616  N N   . PHE A 1 78 ? 5.938   -27.122 3.952   1.00 31.08  ? 77  PHE A N   1 
ATOM   617  C CA  . PHE A 1 78 ? 5.437   -25.900 4.558   1.00 31.68  ? 77  PHE A CA  1 
ATOM   618  C C   . PHE A 1 78 ? 6.458   -25.300 5.536   1.00 31.83  ? 77  PHE A C   1 
ATOM   619  O O   . PHE A 1 78 ? 6.638   -24.076 5.609   1.00 28.57  ? 77  PHE A O   1 
ATOM   620  C CB  . PHE A 1 78 ? 4.104   -26.168 5.256   1.00 31.70  ? 77  PHE A CB  1 
ATOM   621  C CG  . PHE A 1 78 ? 3.383   -24.885 5.636   1.00 30.49  ? 77  PHE A CG  1 
ATOM   622  C CD1 . PHE A 1 78 ? 3.656   -24.232 6.839   1.00 28.42  ? 77  PHE A CD1 1 
ATOM   623  C CD2 . PHE A 1 78 ? 2.424   -24.338 4.780   1.00 29.61  ? 77  PHE A CD2 1 
ATOM   624  C CE1 . PHE A 1 78 ? 3.040   -23.026 7.159   1.00 29.72  ? 77  PHE A CE1 1 
ATOM   625  C CE2 . PHE A 1 78 ? 1.789   -23.150 5.122   1.00 24.68  ? 77  PHE A CE2 1 
ATOM   626  C CZ  . PHE A 1 78 ? 2.087   -22.496 6.302   1.00 26.18  ? 77  PHE A CZ  1 
ATOM   627  N N   . ASN A 1 79 ? 7.040   -26.154 6.384   1.00 31.37  ? 78  ASN A N   1 
ATOM   628  C CA  . ASN A 1 79 ? 7.889   -25.687 7.477   1.00 30.11  ? 78  ASN A CA  1 
ATOM   629  C C   . ASN A 1 79 ? 9.233   -25.214 6.913   1.00 28.50  ? 78  ASN A C   1 
ATOM   630  O O   . ASN A 1 79 ? 9.861   -24.260 7.409   1.00 27.32  ? 78  ASN A O   1 
ATOM   631  C CB  . ASN A 1 79 ? 8.019   -26.789 8.535   1.00 31.34  ? 78  ASN A CB  1 
ATOM   632  C CG  . ASN A 1 79 ? 6.725   -26.968 9.297   1.00 37.96  ? 78  ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 79 ? 5.865   -26.080 9.268   1.00 32.82  ? 78  ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 79 ? 6.574   -28.080 10.016  1.00 34.54  ? 78  ASN A ND2 1 
ATOM   635  N N   . GLU A 1 80 ? 9.681   -25.925 5.875   1.00 26.94  ? 79  GLU A N   1 
ATOM   636  C CA  . GLU A 1 80 ? 10.817  -25.466 5.096   1.00 30.75  ? 79  GLU A CA  1 
ATOM   637  C C   . GLU A 1 80 ? 10.493  -24.081 4.542   1.00 29.68  ? 79  GLU A C   1 
ATOM   638  O O   . GLU A 1 80 ? 11.320  -23.158 4.609   1.00 26.28  ? 79  GLU A O   1 
ATOM   639  C CB  . GLU A 1 80 ? 11.191  -26.413 3.959   1.00 31.65  ? 79  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 80 ? 12.475  -26.012 3.225   1.00 34.49  ? 79  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 80 ? 12.987  -26.998 2.182   1.00 43.77  ? 79  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 80 ? 12.311  -28.013 1.950   1.00 47.15  ? 79  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 80 ? 14.058  -26.762 1.596   1.00 47.98  ? 79  GLU A OE2 1 
ATOM   644  N N   . GLY A 1 81 ? 9.274   -23.946 4.012   1.00 26.59  ? 80  GLY A N   1 
ATOM   645  C CA  . GLY A 1 81 ? 8.838   -22.658 3.477   1.00 25.58  ? 80  GLY A CA  1 
ATOM   646  C C   . GLY A 1 81 ? 8.883   -21.534 4.514   1.00 24.82  ? 80  GLY A C   1 
ATOM   647  O O   . GLY A 1 81 ? 9.242   -20.399 4.199   1.00 23.13  ? 80  GLY A O   1 
ATOM   648  N N   . LEU A 1 82 ? 8.522   -21.829 5.759   1.00 23.99  ? 81  LEU A N   1 
ATOM   649  C CA  . LEU A 1 82 ? 8.534   -20.784 6.772   1.00 24.01  ? 81  LEU A CA  1 
ATOM   650  C C   . LEU A 1 82 ? 9.972   -20.330 7.065   1.00 25.25  ? 81  LEU A C   1 
ATOM   651  O O   . LEU A 1 82 ? 10.219  -19.152 7.315   1.00 24.27  ? 81  LEU A O   1 
ATOM   652  C CB  . LEU A 1 82 ? 7.855   -21.247 8.061   1.00 26.93  ? 81  LEU A CB  1 
ATOM   653  C CG  . LEU A 1 82 ? 6.359   -21.551 7.992   1.00 26.62  ? 81  LEU A CG  1 
ATOM   654  C CD1 . LEU A 1 82 ? 6.037   -22.109 9.372   1.00 28.63  ? 81  LEU A CD1 1 
ATOM   655  C CD2 . LEU A 1 82 ? 5.464   -20.336 7.757   1.00 27.13  ? 81  LEU A CD2 1 
ATOM   656  N N   . TRP A 1 83 ? 10.918  -21.282 7.094   1.00 25.99  ? 82  TRP A N   1 
ATOM   657  C CA  . TRP A 1 83 ? 12.314  -20.932 7.302   1.00 26.06  ? 82  TRP A CA  1 
ATOM   658  C C   . TRP A 1 83 ? 12.772  -20.011 6.172   1.00 24.05  ? 82  TRP A C   1 
ATOM   659  O O   . TRP A 1 83 ? 13.420  -19.000 6.408   1.00 25.18  ? 82  TRP A O   1 
ATOM   660  C CB  . TRP A 1 83 ? 13.223  -22.176 7.461   1.00 26.70  ? 82  TRP A CB  1 
ATOM   661  C CG  . TRP A 1 83 ? 14.669  -21.809 7.696   1.00 26.89  ? 82  TRP A CG  1 
ATOM   662  C CD1 . TRP A 1 83 ? 15.287  -21.612 8.905   1.00 27.03  ? 82  TRP A CD1 1 
ATOM   663  C CD2 . TRP A 1 83 ? 15.643  -21.480 6.682   1.00 25.20  ? 82  TRP A CD2 1 
ATOM   664  N NE1 . TRP A 1 83 ? 16.584  -21.221 8.707   1.00 27.17  ? 82  TRP A NE1 1 
ATOM   665  C CE2 . TRP A 1 83 ? 16.818  -21.105 7.354   1.00 26.69  ? 82  TRP A CE2 1 
ATOM   666  C CE3 . TRP A 1 83 ? 15.616  -21.458 5.280   1.00 26.21  ? 82  TRP A CE3 1 
ATOM   667  C CZ2 . TRP A 1 83 ? 17.970  -20.707 6.672   1.00 26.40  ? 82  TRP A CZ2 1 
ATOM   668  C CZ3 . TRP A 1 83 ? 16.739  -21.050 4.596   1.00 26.94  ? 82  TRP A CZ3 1 
ATOM   669  C CH2 . TRP A 1 83 ? 17.904  -20.664 5.292   1.00 28.22  ? 82  TRP A CH2 1 
ATOM   670  N N   . GLU A 1 84 ? 12.396  -20.321 4.934   1.00 22.76  ? 83  GLU A N   1 
ATOM   671  C CA  . GLU A 1 84 ? 12.964  -19.561 3.829   1.00 20.88  ? 83  GLU A CA  1 
ATOM   672  C C   . GLU A 1 84 ? 12.464  -18.115 3.825   1.00 24.54  ? 83  GLU A C   1 
ATOM   673  O O   . GLU A 1 84 ? 13.234  -17.178 3.619   1.00 24.69  ? 83  GLU A O   1 
ATOM   674  C CB  . GLU A 1 84 ? 12.527  -20.249 2.550   1.00 20.59  ? 83  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 84 ? 13.256  -21.574 2.320   1.00 24.17  ? 83  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 84 ? 12.841  -22.344 1.061   1.00 28.09  ? 83  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 84 ? 11.918  -21.914 0.363   1.00 26.71  ? 83  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 84 ? 13.402  -23.441 0.772   1.00 28.94  ? 83  GLU A OE2 1 
ATOM   679  N N   . ILE A 1 85 ? 11.161  -17.926 4.029   1.00 22.74  ? 84  ILE A N   1 
ATOM   680  C CA  . ILE A 1 85 ? 10.603  -16.585 3.957   1.00 21.31  ? 84  ILE A CA  1 
ATOM   681  C C   . ILE A 1 85 ? 11.177  -15.710 5.077   1.00 25.05  ? 84  ILE A C   1 
ATOM   682  O O   . ILE A 1 85 ? 11.331  -14.491 4.915   1.00 21.86  ? 84  ILE A O   1 
ATOM   683  C CB  . ILE A 1 85 ? 9.058   -16.631 3.958   1.00 22.43  ? 84  ILE A CB  1 
ATOM   684  C CG1 . ILE A 1 85 ? 8.439   -15.269 3.464   1.00 21.28  ? 84  ILE A CG1 1 
ATOM   685  C CG2 . ILE A 1 85 ? 8.490   -17.055 5.333   1.00 20.54  ? 84  ILE A CG2 1 
ATOM   686  C CD1 . ILE A 1 85 ? 6.960   -15.355 3.069   1.00 21.16  ? 84  ILE A CD1 1 
ATOM   687  N N   . GLN A 1 86 ? 11.445  -16.322 6.248   1.00 22.61  ? 85  GLN A N   1 
ATOM   688  C CA  . GLN A 1 86 ? 11.956  -15.552 7.369   1.00 24.81  ? 85  GLN A CA  1 
ATOM   689  C C   . GLN A 1 86 ? 13.468  -15.330 7.246   1.00 25.76  ? 85  GLN A C   1 
ATOM   690  O O   . GLN A 1 86 ? 13.950  -14.286 7.689   1.00 30.44  ? 85  GLN A O   1 
ATOM   691  C CB  . GLN A 1 86 ? 11.593  -16.297 8.662   1.00 29.40  ? 85  GLN A CB  1 
ATOM   692  C CG  . GLN A 1 86 ? 12.049  -15.587 9.936   1.00 38.89  ? 85  GLN A CG  1 
ATOM   693  C CD  . GLN A 1 86 ? 11.354  -16.067 11.203  1.00 47.56  ? 85  GLN A CD  1 
ATOM   694  O OE1 . GLN A 1 86 ? 10.981  -17.243 11.342  1.00 44.27  ? 85  GLN A OE1 1 
ATOM   695  N NE2 . GLN A 1 86 ? 11.150  -15.148 12.139  1.00 42.88  ? 85  GLN A NE2 1 
ATOM   696  N N   . ASN A 1 87 ? 14.209  -16.301 6.675   1.00 23.36  ? 86  ASN A N   1 
ATOM   697  C CA  . ASN A 1 87 ? 15.666  -16.324 6.800   1.00 24.46  ? 86  ASN A CA  1 
ATOM   698  C C   . ASN A 1 87 ? 16.374  -15.955 5.496   1.00 23.66  ? 86  ASN A C   1 
ATOM   699  O O   . ASN A 1 87 ? 17.471  -15.375 5.555   1.00 24.00  ? 86  ASN A O   1 
ATOM   700  C CB  . ASN A 1 87 ? 16.171  -17.599 7.477   1.00 25.12  ? 86  ASN A CB  1 
ATOM   701  C CG  . ASN A 1 87 ? 15.651  -17.632 8.903   1.00 29.85  ? 86  ASN A CG  1 
ATOM   702  O OD1 . ASN A 1 87 ? 15.994  -16.756 9.701   1.00 31.61  ? 86  ASN A OD1 1 
ATOM   703  N ND2 . ASN A 1 87 ? 14.694  -18.495 9.206   1.00 25.96  ? 86  ASN A ND2 1 
ATOM   704  N N   . ASN A 1 88 ? 15.834  -16.356 4.322   1.00 23.74  ? 87  ASN A N   1 
ATOM   705  C CA  . ASN A 1 88 ? 16.495  -15.960 3.073   1.00 22.38  ? 87  ASN A CA  1 
ATOM   706  C C   . ASN A 1 88 ? 15.473  -15.844 1.937   1.00 23.41  ? 87  ASN A C   1 
ATOM   707  O O   . ASN A 1 88 ? 15.518  -16.596 0.962   1.00 23.83  ? 87  ASN A O   1 
ATOM   708  C CB  . ASN A 1 88 ? 17.640  -16.902 2.662   1.00 26.52  ? 87  ASN A CB  1 
ATOM   709  C CG  . ASN A 1 88 ? 18.717  -16.247 1.809   1.00 26.70  ? 87  ASN A CG  1 
ATOM   710  O OD1 . ASN A 1 88 ? 18.503  -15.200 1.184   1.00 24.88  ? 87  ASN A OD1 1 
ATOM   711  N ND2 . ASN A 1 88 ? 19.919  -16.829 1.768   1.00 27.08  ? 87  ASN A ND2 1 
ATOM   712  N N   . PRO A 1 89 ? 14.532  -14.882 2.035   1.00 22.62  ? 88  PRO A N   1 
ATOM   713  C CA  . PRO A 1 89 ? 13.392  -14.849 1.121   1.00 22.96  ? 88  PRO A CA  1 
ATOM   714  C C   . PRO A 1 89 ? 13.736  -14.443 -0.305  1.00 23.56  ? 88  PRO A C   1 
ATOM   715  O O   . PRO A 1 89 ? 12.919  -14.662 -1.173  1.00 23.34  ? 88  PRO A O   1 
ATOM   716  C CB  . PRO A 1 89 ? 12.417  -13.894 1.806   1.00 22.38  ? 88  PRO A CB  1 
ATOM   717  C CG  . PRO A 1 89 ? 13.348  -12.930 2.563   1.00 21.62  ? 88  PRO A CG  1 
ATOM   718  C CD  . PRO A 1 89 ? 14.487  -13.828 3.062   1.00 21.95  ? 88  PRO A CD  1 
ATOM   719  N N   . HIS A 1 90 ? 14.911  -13.822 -0.528  1.00 21.27  ? 89  HIS A N   1 
ATOM   720  C CA  . HIS A 1 90 ? 15.283  -13.282 -1.836  1.00 22.31  ? 89  HIS A CA  1 
ATOM   721  C C   . HIS A 1 90 ? 16.412  -14.088 -2.490  1.00 22.07  ? 89  HIS A C   1 
ATOM   722  O O   . HIS A 1 90 ? 16.922  -13.699 -3.553  1.00 24.56  ? 89  HIS A O   1 
ATOM   723  C CB  . HIS A 1 90 ? 15.671  -11.812 -1.639  1.00 21.02  ? 89  HIS A CB  1 
ATOM   724  C CG  . HIS A 1 90 ? 14.580  -10.988 -1.046  1.00 22.67  ? 89  HIS A CG  1 
ATOM   725  N ND1 . HIS A 1 90 ? 13.327  -10.900 -1.621  1.00 23.14  ? 89  HIS A ND1 1 
ATOM   726  C CD2 . HIS A 1 90 ? 14.541  -10.235 0.071   1.00 22.03  ? 89  HIS A CD2 1 
ATOM   727  C CE1 . HIS A 1 90 ? 12.587  -10.059 -0.893  1.00 24.80  ? 89  HIS A CE1 1 
ATOM   728  N NE2 . HIS A 1 90 ? 13.302  -9.659  0.148   1.00 24.49  ? 89  HIS A NE2 1 
ATOM   729  N N   . ALA A 1 91 ? 16.698  -15.290 -1.954  1.00 23.77  ? 90  ALA A N   1 
ATOM   730  C CA  . ALA A 1 91 ? 17.756  -16.149 -2.495  1.00 23.59  ? 90  ALA A CA  1 
ATOM   731  C C   . ALA A 1 91 ? 17.310  -16.845 -3.779  1.00 27.37  ? 90  ALA A C   1 
ATOM   732  O O   . ALA A 1 91 ? 16.126  -16.965 -4.067  1.00 26.40  ? 90  ALA A O   1 
ATOM   733  C CB  . ALA A 1 91 ? 18.184  -17.209 -1.488  1.00 24.40  ? 90  ALA A CB  1 
ATOM   734  N N   . SER A 1 92 ? 18.296  -17.370 -4.507  1.00 28.12  ? 91  SER A N   1 
ATOM   735  C CA  . SER A 1 92 ? 18.025  -18.275 -5.613  1.00 33.33  ? 91  SER A CA  1 
ATOM   736  C C   . SER A 1 92 ? 17.713  -19.679 -5.079  1.00 34.50  ? 91  SER A C   1 
ATOM   737  O O   . SER A 1 92 ? 18.491  -20.255 -4.312  1.00 35.20  ? 91  SER A O   1 
ATOM   738  C CB  . SER A 1 92 ? 19.184  -18.253 -6.563  1.00 34.23  ? 91  SER A CB  1 
ATOM   739  O OG  . SER A 1 92 ? 19.068  -19.320 -7.478  1.00 44.21  ? 91  SER A OG  1 
ATOM   740  N N   . TYR A 1 93 ? 16.524  -20.196 -5.403  1.00 29.48  ? 92  TYR A N   1 
ATOM   741  C CA  . TYR A 1 93 ? 16.154  -21.541 -4.996  1.00 31.51  ? 92  TYR A CA  1 
ATOM   742  C C   . TYR A 1 93 ? 16.087  -22.442 -6.232  1.00 36.47  ? 92  TYR A C   1 
ATOM   743  O O   . TYR A 1 93 ? 15.476  -23.500 -6.178  1.00 43.02  ? 92  TYR A O   1 
ATOM   744  C CB  . TYR A 1 93 ? 14.804  -21.584 -4.257  1.00 29.62  ? 92  TYR A CB  1 
ATOM   745  C CG  . TYR A 1 93 ? 14.924  -20.959 -2.878  1.00 29.85  ? 92  TYR A CG  1 
ATOM   746  C CD1 . TYR A 1 93 ? 15.365  -21.719 -1.801  1.00 29.70  ? 92  TYR A CD1 1 
ATOM   747  C CD2 . TYR A 1 93 ? 14.624  -19.612 -2.669  1.00 28.59  ? 92  TYR A CD2 1 
ATOM   748  C CE1 . TYR A 1 93 ? 15.520  -21.158 -0.542  1.00 34.80  ? 92  TYR A CE1 1 
ATOM   749  C CE2 . TYR A 1 93 ? 14.734  -19.054 -1.408  1.00 28.59  ? 92  TYR A CE2 1 
ATOM   750  C CZ  . TYR A 1 93 ? 15.190  -19.822 -0.343  1.00 30.28  ? 92  TYR A CZ  1 
ATOM   751  O OH  . TYR A 1 93 ? 15.395  -19.307 0.907   1.00 30.53  ? 92  TYR A OH  1 
ATOM   752  N N   . SER A 1 94 ? 16.717  -21.999 -7.325  1.00 48.00  ? 93  SER A N   1 
ATOM   753  C CA  . SER A 1 94 ? 16.945  -22.787 -8.531  1.00 65.04  ? 93  SER A CA  1 
ATOM   754  C C   . SER A 1 94 ? 17.617  -24.124 -8.171  1.00 76.06  ? 93  SER A C   1 
ATOM   755  O O   . SER A 1 94 ? 18.559  -24.100 -7.342  1.00 81.47  ? 93  SER A O   1 
ATOM   756  C CB  . SER A 1 94 ? 17.796  -22.016 -9.533  1.00 61.80  ? 93  SER A CB  1 
ATOM   757  O OG  . SER A 1 94 ? 17.329  -20.684 -9.711  1.00 73.55  ? 93  SER A OG  1 
ATOM   758  O OXT . SER A 1 94 ? 17.192  -25.147 -8.745  1.00 95.17  ? 93  SER A OXT 1 
ATOM   759  N N   . MET B 1 2  ? 38.822  -11.059 -41.667 1.00 66.01  ? 1   MET B N   1 
ATOM   760  C CA  . MET B 1 2  ? 38.543  -11.979 -42.801 1.00 70.40  ? 1   MET B CA  1 
ATOM   761  C C   . MET B 1 2  ? 37.029  -12.192 -42.892 1.00 62.32  ? 1   MET B C   1 
ATOM   762  O O   . MET B 1 2  ? 36.382  -12.454 -41.873 1.00 53.83  ? 1   MET B O   1 
ATOM   763  C CB  . MET B 1 2  ? 39.291  -13.307 -42.609 1.00 79.74  ? 1   MET B CB  1 
ATOM   764  C CG  . MET B 1 2  ? 39.422  -14.172 -43.864 1.00 95.12  ? 1   MET B CG  1 
ATOM   765  S SD  . MET B 1 2  ? 40.527  -13.569 -45.162 1.00 95.11  ? 1   MET B SD  1 
ATOM   766  C CE  . MET B 1 2  ? 42.009  -13.227 -44.203 1.00 93.98  ? 1   MET B CE  1 
ATOM   767  N N   . PRO B 1 3  ? 36.403  -12.057 -44.091 1.00 50.56  ? 2   PRO B N   1 
ATOM   768  C CA  . PRO B 1 3  ? 34.972  -12.328 -44.227 1.00 50.42  ? 2   PRO B CA  1 
ATOM   769  C C   . PRO B 1 3  ? 34.676  -13.754 -43.758 1.00 54.50  ? 2   PRO B C   1 
ATOM   770  O O   . PRO B 1 3  ? 35.545  -14.628 -43.794 1.00 50.24  ? 2   PRO B O   1 
ATOM   771  C CB  . PRO B 1 3  ? 34.678  -12.087 -45.714 1.00 54.10  ? 2   PRO B CB  1 
ATOM   772  C CG  . PRO B 1 3  ? 35.798  -11.156 -46.143 1.00 46.96  ? 2   PRO B CG  1 
ATOM   773  C CD  . PRO B 1 3  ? 37.015  -11.626 -45.360 1.00 47.20  ? 2   PRO B CD  1 
ATOM   774  N N   . HIS B 1 4  ? 33.471  -13.933 -43.209 1.00 56.56  ? 3   HIS B N   1 
ATOM   775  C CA  . HIS B 1 4  ? 32.999  -15.224 -42.735 1.00 55.51  ? 3   HIS B CA  1 
ATOM   776  C C   . HIS B 1 4  ? 31.597  -15.466 -43.291 1.00 54.91  ? 3   HIS B C   1 
ATOM   777  O O   . HIS B 1 4  ? 31.000  -14.560 -43.879 1.00 51.25  ? 3   HIS B O   1 
ATOM   778  C CB  . HIS B 1 4  ? 33.111  -15.319 -41.211 1.00 62.10  ? 3   HIS B CB  1 
ATOM   779  C CG  . HIS B 1 4  ? 34.495  -15.604 -40.717 1.00 73.18  ? 3   HIS B CG  1 
ATOM   780  N ND1 . HIS B 1 4  ? 35.332  -16.530 -41.309 1.00 72.28  ? 3   HIS B ND1 1 
ATOM   781  C CD2 . HIS B 1 4  ? 35.164  -15.110 -39.657 1.00 64.62  ? 3   HIS B CD2 1 
ATOM   782  C CE1 . HIS B 1 4  ? 36.467  -16.582 -40.627 1.00 66.84  ? 3   HIS B CE1 1 
ATOM   783  N NE2 . HIS B 1 4  ? 36.385  -15.724 -39.626 1.00 67.38  ? 3   HIS B NE2 1 
ATOM   784  N N   . ALA B 1 5  ? 31.095  -16.703 -43.123 1.00 44.64  ? 4   ALA B N   1 
ATOM   785  C CA  . ALA B 1 5  ? 29.803  -17.079 -43.661 1.00 42.45  ? 4   ALA B CA  1 
ATOM   786  C C   . ALA B 1 5  ? 28.758  -16.099 -43.146 1.00 42.72  ? 4   ALA B C   1 
ATOM   787  O O   . ALA B 1 5  ? 27.948  -15.606 -43.933 1.00 42.15  ? 4   ALA B O   1 
ATOM   788  C CB  . ALA B 1 5  ? 29.467  -18.501 -43.262 1.00 42.48  ? 4   ALA B CB  1 
ATOM   789  N N   . PHE B 1 6  ? 28.803  -15.848 -41.827 1.00 38.81  ? 5   PHE B N   1 
ATOM   790  C CA  . PHE B 1 6  ? 28.012  -14.797 -41.188 1.00 49.53  ? 5   PHE B CA  1 
ATOM   791  C C   . PHE B 1 6  ? 28.864  -13.538 -40.959 1.00 42.64  ? 5   PHE B C   1 
ATOM   792  O O   . PHE B 1 6  ? 29.987  -13.624 -40.459 1.00 43.86  ? 5   PHE B O   1 
ATOM   793  C CB  . PHE B 1 6  ? 27.420  -15.273 -39.850 1.00 44.93  ? 5   PHE B CB  1 
ATOM   794  C CG  . PHE B 1 6  ? 26.301  -16.306 -39.954 1.00 39.87  ? 5   PHE B CG  1 
ATOM   795  C CD1 . PHE B 1 6  ? 24.984  -15.916 -40.186 1.00 35.24  ? 5   PHE B CD1 1 
ATOM   796  C CD2 . PHE B 1 6  ? 26.570  -17.665 -39.825 1.00 38.69  ? 5   PHE B CD2 1 
ATOM   797  C CE1 . PHE B 1 6  ? 23.973  -16.865 -40.308 1.00 38.42  ? 5   PHE B CE1 1 
ATOM   798  C CE2 . PHE B 1 6  ? 25.555  -18.607 -39.924 1.00 35.10  ? 5   PHE B CE2 1 
ATOM   799  C CZ  . PHE B 1 6  ? 24.261  -18.213 -40.152 1.00 34.96  ? 5   PHE B CZ  1 
ATOM   800  N N   . LYS B 1 7  ? 28.302  -12.359 -41.263 1.00 44.88  ? 6   LYS B N   1 
ATOM   801  C CA  . LYS B 1 7  ? 29.027  -11.104 -41.063 1.00 46.01  ? 6   LYS B CA  1 
ATOM   802  C C   . LYS B 1 7  ? 28.278  -10.193 -40.077 1.00 48.32  ? 6   LYS B C   1 
ATOM   803  O O   . LYS B 1 7  ? 27.051  -10.265 -39.966 1.00 41.81  ? 6   LYS B O   1 
ATOM   804  C CB  . LYS B 1 7  ? 29.231  -10.447 -42.426 1.00 47.90  ? 6   LYS B CB  1 
ATOM   805  C CG  . LYS B 1 7  ? 27.957  -10.016 -43.125 1.00 47.28  ? 6   LYS B CG  1 
ATOM   806  C CD  . LYS B 1 7  ? 28.292  -9.665  -44.572 1.00 54.19  ? 6   LYS B CD  1 
ATOM   807  C CE  . LYS B 1 7  ? 27.116  -9.144  -45.332 1.00 55.99  ? 6   LYS B CE  1 
ATOM   808  N NZ  . LYS B 1 7  ? 26.096  -10.196 -45.449 1.00 60.24  ? 6   LYS B NZ  1 
ATOM   809  N N   . PRO B 1 8  ? 28.973  -9.275  -39.355 1.00 46.71  ? 7   PRO B N   1 
ATOM   810  C CA  . PRO B 1 8  ? 28.307  -8.404  -38.382 1.00 42.19  ? 7   PRO B CA  1 
ATOM   811  C C   . PRO B 1 8  ? 27.165  -7.667  -39.060 1.00 39.64  ? 7   PRO B C   1 
ATOM   812  O O   . PRO B 1 8  ? 27.294  -7.263  -40.218 1.00 42.08  ? 7   PRO B O   1 
ATOM   813  C CB  . PRO B 1 8  ? 29.472  -7.495  -38.008 1.00 46.42  ? 7   PRO B CB  1 
ATOM   814  C CG  . PRO B 1 8  ? 30.658  -8.441  -38.046 1.00 45.61  ? 7   PRO B CG  1 
ATOM   815  C CD  . PRO B 1 8  ? 30.422  -9.005  -39.434 1.00 46.93  ? 7   PRO B CD  1 
ATOM   816  N N   . GLY B 1 9  ? 26.022  -7.574  -38.360 1.00 32.19  ? 8   GLY B N   1 
ATOM   817  C CA  . GLY B 1 9  ? 24.826  -6.974  -38.919 1.00 32.64  ? 8   GLY B CA  1 
ATOM   818  C C   . GLY B 1 9  ? 23.875  -8.000  -39.526 1.00 31.12  ? 8   GLY B C   1 
ATOM   819  O O   . GLY B 1 9  ? 22.753  -7.664  -39.866 1.00 31.65  ? 8   GLY B O   1 
ATOM   820  N N   . ASP B 1 10 ? 24.337  -9.240  -39.746 1.00 35.16  ? 9   ASP B N   1 
ATOM   821  C CA  . ASP B 1 10 ? 23.445  -10.245 -40.308 1.00 33.66  ? 9   ASP B CA  1 
ATOM   822  C C   . ASP B 1 10 ? 22.325  -10.535 -39.301 1.00 30.56  ? 9   ASP B C   1 
ATOM   823  O O   . ASP B 1 10 ? 22.558  -10.564 -38.089 1.00 32.49  ? 9   ASP B O   1 
ATOM   824  C CB  . ASP B 1 10 ? 24.206  -11.516 -40.645 1.00 37.39  ? 9   ASP B CB  1 
ATOM   825  C CG  . ASP B 1 10 ? 24.903  -11.543 -42.002 1.00 44.40  ? 9   ASP B CG  1 
ATOM   826  O OD1 . ASP B 1 10 ? 24.652  -10.643 -42.821 1.00 46.00  ? 9   ASP B OD1 1 
ATOM   827  O OD2 . ASP B 1 10 ? 25.701  -12.475 -42.223 1.00 45.42  ? 9   ASP B OD2 1 
ATOM   828  N N   . LEU B 1 11 ? 21.114  -10.716 -39.813 1.00 29.54  ? 10  LEU B N   1 
ATOM   829  C CA  . LEU B 1 11 ? 19.989  -10.949 -38.927 1.00 30.78  ? 10  LEU B CA  1 
ATOM   830  C C   . LEU B 1 11 ? 19.635  -12.431 -38.949 1.00 30.59  ? 10  LEU B C   1 
ATOM   831  O O   . LEU B 1 11 ? 19.674  -13.053 -40.015 1.00 32.37  ? 10  LEU B O   1 
ATOM   832  C CB  . LEU B 1 11 ? 18.837  -10.099 -39.433 1.00 27.74  ? 10  LEU B CB  1 
ATOM   833  C CG  . LEU B 1 11 ? 19.125  -8.594  -39.520 1.00 26.23  ? 10  LEU B CG  1 
ATOM   834  C CD1 . LEU B 1 11 ? 17.804  -7.965  -39.893 1.00 27.92  ? 10  LEU B CD1 1 
ATOM   835  C CD2 . LEU B 1 11 ? 19.652  -8.132  -38.183 1.00 28.28  ? 10  LEU B CD2 1 
ATOM   836  N N   . VAL B 1 12 ? 19.270  -12.973 -37.777 1.00 27.59  ? 11  VAL B N   1 
ATOM   837  C CA  . VAL B 1 12 ? 19.031  -14.409 -37.692 1.00 26.29  ? 11  VAL B CA  1 
ATOM   838  C C   . VAL B 1 12 ? 17.907  -14.671 -36.683 1.00 29.70  ? 11  VAL B C   1 
ATOM   839  O O   . VAL B 1 12 ? 17.471  -13.767 -35.947 1.00 26.60  ? 11  VAL B O   1 
ATOM   840  C CB  . VAL B 1 12 ? 20.329  -15.130 -37.246 1.00 27.11  ? 11  VAL B CB  1 
ATOM   841  C CG1 . VAL B 1 12 ? 21.488  -14.929 -38.227 1.00 26.89  ? 11  VAL B CG1 1 
ATOM   842  C CG2 . VAL B 1 12 ? 20.742  -14.772 -35.804 1.00 26.23  ? 11  VAL B CG2 1 
ATOM   843  N N   . PHE B 1 13 ? 17.449  -15.930 -36.655 1.00 28.06  ? 12  PHE B N   1 
ATOM   844  C CA  . PHE B 1 13 ? 16.958  -16.479 -35.402 1.00 27.25  ? 12  PHE B CA  1 
ATOM   845  C C   . PHE B 1 13 ? 18.052  -17.355 -34.807 1.00 28.63  ? 12  PHE B C   1 
ATOM   846  O O   . PHE B 1 13 ? 18.685  -18.139 -35.537 1.00 27.22  ? 12  PHE B O   1 
ATOM   847  C CB  . PHE B 1 13 ? 15.659  -17.264 -35.577 1.00 25.98  ? 12  PHE B CB  1 
ATOM   848  C CG  . PHE B 1 13 ? 14.486  -16.410 -36.000 1.00 30.53  ? 12  PHE B CG  1 
ATOM   849  C CD1 . PHE B 1 13 ? 14.276  -16.117 -37.351 1.00 29.99  ? 12  PHE B CD1 1 
ATOM   850  C CD2 . PHE B 1 13 ? 13.580  -15.942 -35.057 1.00 28.92  ? 12  PHE B CD2 1 
ATOM   851  C CE1 . PHE B 1 13 ? 13.192  -15.343 -37.737 1.00 33.17  ? 12  PHE B CE1 1 
ATOM   852  C CE2 . PHE B 1 13 ? 12.487  -15.182 -35.441 1.00 28.87  ? 12  PHE B CE2 1 
ATOM   853  C CZ  . PHE B 1 13 ? 12.297  -14.884 -36.787 1.00 34.31  ? 12  PHE B CZ  1 
ATOM   854  N N   . ALA B 1 14 ? 18.248  -17.220 -33.472 1.00 25.54  ? 13  ALA B N   1 
ATOM   855  C CA  . ALA B 1 14 ? 19.289  -17.957 -32.780 1.00 26.37  ? 13  ALA B CA  1 
ATOM   856  C C   . ALA B 1 14 ? 18.656  -18.884 -31.746 1.00 27.04  ? 13  ALA B C   1 
ATOM   857  O O   . ALA B 1 14 ? 17.705  -18.477 -31.071 1.00 26.58  ? 13  ALA B O   1 
ATOM   858  C CB  . ALA B 1 14 ? 20.229  -16.990 -32.105 1.00 27.79  ? 13  ALA B CB  1 
ATOM   859  N N   . LYS B 1 15 ? 19.169  -20.115 -31.662 1.00 27.52  ? 14  LYS B N   1 
ATOM   860  C CA  . LYS B 1 15 ? 18.530  -21.167 -30.878 1.00 29.67  ? 14  LYS B CA  1 
ATOM   861  C C   . LYS B 1 15 ? 19.350  -21.433 -29.622 1.00 28.98  ? 14  LYS B C   1 
ATOM   862  O O   . LYS B 1 15 ? 20.539  -21.729 -29.714 1.00 32.65  ? 14  LYS B O   1 
ATOM   863  C CB  . LYS B 1 15 ? 18.414  -22.492 -31.651 1.00 31.67  ? 14  LYS B CB  1 
ATOM   864  C CG  . LYS B 1 15 ? 17.602  -23.613 -30.934 1.00 27.95  ? 14  LYS B CG  1 
ATOM   865  C CD  . LYS B 1 15 ? 16.165  -23.158 -30.645 1.00 29.64  ? 14  LYS B CD  1 
ATOM   866  C CE  . LYS B 1 15 ? 15.223  -24.268 -30.130 1.00 33.64  ? 14  LYS B CE  1 
ATOM   867  N NZ  . LYS B 1 15 ? 15.627  -24.569 -28.752 1.00 29.26  ? 14  LYS B NZ  1 
ATOM   868  N N   . MET B 1 16 ? 18.712  -21.287 -28.453 1.00 32.59  ? 15  MET B N   1 
ATOM   869  C CA  . MET B 1 16 ? 19.307  -21.714 -27.191 1.00 35.46  ? 15  MET B CA  1 
ATOM   870  C C   . MET B 1 16 ? 18.466  -22.862 -26.634 1.00 33.83  ? 15  MET B C   1 
ATOM   871  O O   . MET B 1 16 ? 17.253  -22.862 -26.805 1.00 28.85  ? 15  MET B O   1 
ATOM   872  C CB  . MET B 1 16 ? 19.277  -20.589 -26.148 1.00 38.54  ? 15  MET B CB  1 
ATOM   873  C CG  . MET B 1 16 ? 19.912  -19.289 -26.588 1.00 42.57  ? 15  MET B CG  1 
ATOM   874  S SD  . MET B 1 16 ? 21.704  -19.201 -26.421 1.00 47.61  ? 15  MET B SD  1 
ATOM   875  C CE  . MET B 1 16 ? 21.849  -18.978 -24.641 1.00 42.52  ? 15  MET B CE  1 
ATOM   876  N N   . LYS B 1 17 ? 19.100  -23.797 -25.919 1.00 31.24  ? 16  LYS B N   1 
ATOM   877  C CA  . LYS B 1 17 ? 18.364  -24.881 -25.276 1.00 36.05  ? 16  LYS B CA  1 
ATOM   878  C C   . LYS B 1 17 ? 17.316  -24.306 -24.317 1.00 32.43  ? 16  LYS B C   1 
ATOM   879  O O   . LYS B 1 17 ? 17.602  -23.384 -23.560 1.00 37.66  ? 16  LYS B O   1 
ATOM   880  C CB  . LYS B 1 17 ? 19.332  -25.856 -24.588 1.00 42.24  ? 16  LYS B CB  1 
ATOM   881  C CG  . LYS B 1 17 ? 18.656  -27.089 -23.979 1.00 49.09  ? 16  LYS B CG  1 
ATOM   882  C CD  . LYS B 1 17 ? 19.506  -27.905 -23.007 1.00 46.12  ? 16  LYS B CD  1 
ATOM   883  N N   . GLY B 1 18 ? 16.091  -24.830 -24.400 1.00 35.94  ? 17  GLY B N   1 
ATOM   884  C CA  . GLY B 1 18 ? 14.997  -24.395 -23.546 1.00 35.93  ? 17  GLY B CA  1 
ATOM   885  C C   . GLY B 1 18 ? 14.190  -23.226 -24.117 1.00 35.79  ? 17  GLY B C   1 
ATOM   886  O O   . GLY B 1 18 ? 13.252  -22.767 -23.479 1.00 36.97  ? 17  GLY B O   1 
ATOM   887  N N   . TYR B 1 19 ? 14.552  -22.699 -25.295 1.00 30.22  ? 18  TYR B N   1 
ATOM   888  C CA  . TYR B 1 19 ? 13.854  -21.503 -25.741 1.00 27.73  ? 18  TYR B CA  1 
ATOM   889  C C   . TYR B 1 19 ? 13.522  -21.633 -27.220 1.00 28.06  ? 18  TYR B C   1 
ATOM   890  O O   . TYR B 1 19 ? 14.213  -22.334 -27.947 1.00 32.97  ? 18  TYR B O   1 
ATOM   891  C CB  . TYR B 1 19 ? 14.725  -20.253 -25.562 1.00 27.26  ? 18  TYR B CB  1 
ATOM   892  C CG  . TYR B 1 19 ? 15.019  -20.033 -24.089 1.00 31.73  ? 18  TYR B CG  1 
ATOM   893  C CD1 . TYR B 1 19 ? 14.105  -19.383 -23.252 1.00 33.72  ? 18  TYR B CD1 1 
ATOM   894  C CD2 . TYR B 1 19 ? 16.215  -20.476 -23.542 1.00 31.26  ? 18  TYR B CD2 1 
ATOM   895  C CE1 . TYR B 1 19 ? 14.375  -19.202 -21.902 1.00 34.42  ? 18  TYR B CE1 1 
ATOM   896  C CE2 . TYR B 1 19 ? 16.490  -20.298 -22.188 1.00 38.02  ? 18  TYR B CE2 1 
ATOM   897  C CZ  . TYR B 1 19 ? 15.575  -19.651 -21.377 1.00 36.51  ? 18  TYR B CZ  1 
ATOM   898  O OH  . TYR B 1 19 ? 15.868  -19.491 -20.052 1.00 40.37  ? 18  TYR B OH  1 
ATOM   899  N N   . PRO B 1 20 ? 12.479  -20.942 -27.709 1.00 28.49  ? 19  PRO B N   1 
ATOM   900  C CA  . PRO B 1 20 ? 12.208  -20.902 -29.151 1.00 26.36  ? 19  PRO B CA  1 
ATOM   901  C C   . PRO B 1 20 ? 13.306  -20.141 -29.902 1.00 26.56  ? 19  PRO B C   1 
ATOM   902  O O   . PRO B 1 20 ? 13.995  -19.288 -29.328 1.00 23.64  ? 19  PRO B O   1 
ATOM   903  C CB  . PRO B 1 20 ? 10.887  -20.150 -29.177 1.00 26.87  ? 19  PRO B CB  1 
ATOM   904  C CG  . PRO B 1 20 ? 10.979  -19.202 -27.971 1.00 31.09  ? 19  PRO B CG  1 
ATOM   905  C CD  . PRO B 1 20 ? 11.548  -20.115 -26.907 1.00 27.81  ? 19  PRO B CD  1 
ATOM   906  N N   . HIS B 1 21 ? 13.484  -20.490 -31.188 1.00 23.18  ? 20  HIS B N   1 
ATOM   907  C CA  . HIS B 1 21 ? 14.362  -19.726 -32.083 1.00 26.32  ? 20  HIS B CA  1 
ATOM   908  C C   . HIS B 1 21 ? 14.130  -18.226 -31.892 1.00 24.22  ? 20  HIS B C   1 
ATOM   909  O O   . HIS B 1 21 ? 12.988  -17.767 -31.987 1.00 25.60  ? 20  HIS B O   1 
ATOM   910  C CB  . HIS B 1 21 ? 14.061  -20.152 -33.526 1.00 24.75  ? 20  HIS B CB  1 
ATOM   911  C CG  . HIS B 1 21 ? 14.303  -21.628 -33.692 1.00 28.09  ? 20  HIS B CG  1 
ATOM   912  N ND1 . HIS B 1 21 ? 13.386  -22.611 -33.366 1.00 28.74  ? 20  HIS B ND1 1 
ATOM   913  C CD2 . HIS B 1 21 ? 15.391  -22.271 -34.127 1.00 28.75  ? 20  HIS B CD2 1 
ATOM   914  C CE1 . HIS B 1 21 ? 13.911  -23.805 -33.640 1.00 30.38  ? 20  HIS B CE1 1 
ATOM   915  N NE2 . HIS B 1 21 ? 15.133  -23.626 -34.104 1.00 29.21  ? 20  HIS B NE2 1 
ATOM   916  N N   . TRP B 1 22 ? 15.194  -17.460 -31.619 1.00 25.27  ? 21  TRP B N   1 
ATOM   917  C CA  . TRP B 1 22 ? 14.987  -16.142 -31.027 1.00 24.36  ? 21  TRP B CA  1 
ATOM   918  C C   . TRP B 1 22 ? 15.491  -15.061 -31.983 1.00 26.36  ? 21  TRP B C   1 
ATOM   919  O O   . TRP B 1 22 ? 16.619  -15.167 -32.438 1.00 27.64  ? 21  TRP B O   1 
ATOM   920  C CB  . TRP B 1 22 ? 15.719  -16.040 -29.676 1.00 25.20  ? 21  TRP B CB  1 
ATOM   921  C CG  . TRP B 1 22 ? 15.202  -14.906 -28.831 1.00 26.19  ? 21  TRP B CG  1 
ATOM   922  C CD1 . TRP B 1 22 ? 15.443  -13.566 -28.969 1.00 27.70  ? 21  TRP B CD1 1 
ATOM   923  C CD2 . TRP B 1 22 ? 14.251  -15.038 -27.738 1.00 27.82  ? 21  TRP B CD2 1 
ATOM   924  N NE1 . TRP B 1 22 ? 14.728  -12.857 -28.031 1.00 28.94  ? 21  TRP B NE1 1 
ATOM   925  C CE2 . TRP B 1 22 ? 13.977  -13.729 -27.268 1.00 28.26  ? 21  TRP B CE2 1 
ATOM   926  C CE3 . TRP B 1 22 ? 13.623  -16.136 -27.125 1.00 25.47  ? 21  TRP B CE3 1 
ATOM   927  C CZ2 . TRP B 1 22 ? 13.110  -13.490 -26.195 1.00 27.26  ? 21  TRP B CZ2 1 
ATOM   928  C CZ3 . TRP B 1 22 ? 12.738  -15.901 -26.081 1.00 26.98  ? 21  TRP B CZ3 1 
ATOM   929  C CH2 . TRP B 1 22 ? 12.450  -14.586 -25.662 1.00 24.57  ? 21  TRP B CH2 1 
ATOM   930  N N   . PRO B 1 23 ? 14.716  -13.994 -32.298 1.00 26.58  ? 22  PRO B N   1 
ATOM   931  C CA  . PRO B 1 23 ? 15.204  -12.939 -33.204 1.00 27.10  ? 22  PRO B CA  1 
ATOM   932  C C   . PRO B 1 23 ? 16.512  -12.343 -32.679 1.00 25.72  ? 22  PRO B C   1 
ATOM   933  O O   . PRO B 1 23 ? 16.657  -12.019 -31.494 1.00 25.05  ? 22  PRO B O   1 
ATOM   934  C CB  . PRO B 1 23 ? 14.031  -11.922 -33.246 1.00 27.63  ? 22  PRO B CB  1 
ATOM   935  C CG  . PRO B 1 23 ? 13.278  -12.186 -31.945 1.00 26.90  ? 22  PRO B CG  1 
ATOM   936  C CD  . PRO B 1 23 ? 13.367  -13.717 -31.808 1.00 25.50  ? 22  PRO B CD  1 
ATOM   937  N N   . ALA B 1 24 ? 17.520  -12.247 -33.549 1.00 26.15  ? 23  ALA B N   1 
ATOM   938  C CA  . ALA B 1 24 ? 18.849  -11.890 -33.085 1.00 24.66  ? 23  ALA B CA  1 
ATOM   939  C C   . ALA B 1 24 ? 19.679  -11.326 -34.243 1.00 26.84  ? 23  ALA B C   1 
ATOM   940  O O   . ALA B 1 24 ? 19.230  -11.305 -35.391 1.00 28.91  ? 23  ALA B O   1 
ATOM   941  C CB  . ALA B 1 24 ? 19.538  -13.073 -32.426 1.00 26.24  ? 23  ALA B CB  1 
ATOM   942  N N   . ARG B 1 25 ? 20.884  -10.850 -33.899 1.00 28.05  ? 24  ARG B N   1 
ATOM   943  C CA  . ARG B 1 25 ? 21.810  -10.350 -34.905 1.00 29.91  ? 24  ARG B CA  1 
ATOM   944  C C   . ARG B 1 25 ? 23.220  -10.797 -34.543 1.00 25.46  ? 24  ARG B C   1 
ATOM   945  O O   . ARG B 1 25 ? 23.529  -11.047 -33.375 1.00 27.61  ? 24  ARG B O   1 
ATOM   946  C CB  . ARG B 1 25 ? 21.764  -8.828  -35.051 1.00 28.10  ? 24  ARG B CB  1 
ATOM   947  C CG  . ARG B 1 25 ? 22.485  -8.040  -33.961 1.00 30.42  ? 24  ARG B CG  1 
ATOM   948  C CD  . ARG B 1 25 ? 22.232  -6.522  -34.088 1.00 27.98  ? 24  ARG B CD  1 
ATOM   949  N NE  . ARG B 1 25 ? 22.786  -5.837  -32.907 1.00 27.20  ? 24  ARG B NE  1 
ATOM   950  C CZ  . ARG B 1 25 ? 22.517  -4.575  -32.549 1.00 29.74  ? 24  ARG B CZ  1 
ATOM   951  N NH1 . ARG B 1 25 ? 21.544  -3.936  -33.183 1.00 28.10  ? 24  ARG B NH1 1 
ATOM   952  N NH2 . ARG B 1 25 ? 23.213  -3.986  -31.565 1.00 26.17  ? 24  ARG B NH2 1 
ATOM   953  N N   . ILE B 1 26 ? 24.064  -10.895 -35.583 1.00 27.38  ? 25  ILE B N   1 
ATOM   954  C CA  . ILE B 1 26 ? 25.509  -11.044 -35.441 1.00 31.19  ? 25  ILE B CA  1 
ATOM   955  C C   . ILE B 1 26 ? 26.079  -9.660  -35.128 1.00 33.91  ? 25  ILE B C   1 
ATOM   956  O O   . ILE B 1 26 ? 25.860  -8.709  -35.875 1.00 36.89  ? 25  ILE B O   1 
ATOM   957  C CB  . ILE B 1 26 ? 26.151  -11.562 -36.744 1.00 31.57  ? 25  ILE B CB  1 
ATOM   958  C CG1 . ILE B 1 26 ? 25.389  -12.748 -37.325 1.00 31.24  ? 25  ILE B CG1 1 
ATOM   959  C CG2 . ILE B 1 26 ? 27.646  -11.851 -36.547 1.00 36.44  ? 25  ILE B CG2 1 
ATOM   960  C CD1 . ILE B 1 26 ? 25.425  -13.989 -36.461 1.00 29.92  ? 25  ILE B CD1 1 
ATOM   961  N N   . ASP B 1 27 ? 26.817  -9.581  -34.031 1.00 36.03  ? 26  ASP B N   1 
ATOM   962  C CA  . ASP B 1 27 ? 27.502  -8.362  -33.643 1.00 44.41  ? 26  ASP B CA  1 
ATOM   963  C C   . ASP B 1 27 ? 28.992  -8.436  -34.010 1.00 49.73  ? 26  ASP B C   1 
ATOM   964  O O   . ASP B 1 27 ? 29.558  -9.526  -34.106 1.00 43.17  ? 26  ASP B O   1 
ATOM   965  C CB  . ASP B 1 27 ? 27.414  -8.231  -32.137 1.00 40.04  ? 26  ASP B CB  1 
ATOM   966  C CG  . ASP B 1 27 ? 26.223  -7.476  -31.562 1.00 41.82  ? 26  ASP B CG  1 
ATOM   967  O OD1 . ASP B 1 27 ? 25.415  -6.918  -32.348 1.00 39.74  ? 26  ASP B OD1 1 
ATOM   968  O OD2 . ASP B 1 27 ? 26.144  -7.419  -30.310 1.00 39.17  ? 26  ASP B OD2 1 
ATOM   969  N N   A ASP B 1 28 ? 29.620  -7.265  -34.195 0.50 56.48  ? 27  ASP B N   1 
ATOM   970  N N   B ASP B 1 28 ? 29.622  -7.260  -34.171 0.50 54.77  ? 27  ASP B N   1 
ATOM   971  C CA  A ASP B 1 28 ? 31.065  -7.153  -34.358 0.50 57.74  ? 27  ASP B CA  1 
ATOM   972  C CA  B ASP B 1 28 ? 31.062  -7.134  -34.361 0.50 54.41  ? 27  ASP B CA  1 
ATOM   973  C C   A ASP B 1 28 ? 31.744  -7.346  -33.003 0.50 59.57  ? 27  ASP B C   1 
ATOM   974  C C   B ASP B 1 28 ? 31.736  -7.375  -33.010 0.50 57.29  ? 27  ASP B C   1 
ATOM   975  O O   A ASP B 1 28 ? 31.112  -7.148  -31.966 0.50 62.21  ? 27  ASP B O   1 
ATOM   976  O O   B ASP B 1 28 ? 31.088  -7.235  -31.974 0.50 60.06  ? 27  ASP B O   1 
ATOM   977  C CB  A ASP B 1 28 ? 31.436  -5.851  -35.051 0.50 57.72  ? 27  ASP B CB  1 
ATOM   978  C CB  B ASP B 1 28 ? 31.404  -5.757  -34.914 0.50 50.73  ? 27  ASP B CB  1 
ATOM   979  C CG  A ASP B 1 28 ? 30.440  -4.714  -34.881 0.50 54.04  ? 27  ASP B CG  1 
ATOM   980  C CG  B ASP B 1 28 ? 32.209  -5.733  -36.208 0.50 46.01  ? 27  ASP B CG  1 
ATOM   981  O OD1 A ASP B 1 28 ? 30.023  -4.148  -35.910 0.50 56.41  ? 27  ASP B OD1 1 
ATOM   982  O OD1 B ASP B 1 28 ? 33.259  -6.410  -36.276 0.50 45.94  ? 27  ASP B OD1 1 
ATOM   983  O OD2 A ASP B 1 28 ? 30.073  -4.420  -33.725 0.50 57.83  ? 27  ASP B OD2 1 
ATOM   984  O OD2 B ASP B 1 28 ? 31.781  -5.025  -37.138 0.50 41.21  ? 27  ASP B OD2 1 
ATOM   985  N N   . ILE B 1 29 ? 33.031  -7.725  -33.024 1.00 63.27  ? 28  ILE B N   1 
ATOM   986  C CA  . ILE B 1 29 ? 33.752  -8.118  -31.812 1.00 68.27  ? 28  ILE B CA  1 
ATOM   987  C C   . ILE B 1 29 ? 34.580  -6.950  -31.237 1.00 69.47  ? 28  ILE B C   1 
ATOM   988  O O   . ILE B 1 29 ? 34.309  -5.784  -31.619 1.00 70.47  ? 28  ILE B O   1 
ATOM   989  C CB  . ILE B 1 29 ? 34.620  -9.369  -32.052 1.00 65.39  ? 28  ILE B CB  1 
ATOM   990  N N   . VAL B 1 34 ? 36.836  -10.285 -24.170 1.00 82.91  ? 33  VAL B N   1 
ATOM   991  C CA  . VAL B 1 34 ? 36.746  -11.682 -24.689 1.00 77.16  ? 33  VAL B CA  1 
ATOM   992  C C   . VAL B 1 34 ? 36.621  -11.605 -26.207 1.00 77.50  ? 33  VAL B C   1 
ATOM   993  O O   . VAL B 1 34 ? 36.175  -10.588 -26.726 1.00 84.47  ? 33  VAL B O   1 
ATOM   994  C CB  . VAL B 1 34 ? 35.510  -12.338 -24.040 1.00 75.58  ? 33  VAL B CB  1 
ATOM   995  C CG1 . VAL B 1 34 ? 34.218  -11.617 -24.412 1.00 80.28  ? 33  VAL B CG1 1 
ATOM   996  C CG2 . VAL B 1 34 ? 35.403  -13.827 -24.345 1.00 67.50  ? 33  VAL B CG2 1 
ATOM   997  N N   . LYS B 1 35 ? 37.061  -12.661 -26.904 1.00 78.14  ? 34  LYS B N   1 
ATOM   998  C CA  . LYS B 1 35 ? 36.672  -12.922 -28.288 1.00 72.16  ? 34  LYS B CA  1 
ATOM   999  C C   . LYS B 1 35 ? 35.840  -14.212 -28.336 1.00 66.69  ? 34  LYS B C   1 
ATOM   1000 O O   . LYS B 1 35 ? 35.890  -15.032 -27.414 1.00 62.47  ? 34  LYS B O   1 
ATOM   1001 C CB  . LYS B 1 35 ? 37.880  -12.942 -29.239 1.00 58.92  ? 34  LYS B CB  1 
ATOM   1002 N N   . PRO B 1 36 ? 35.027  -14.451 -29.394 1.00 62.27  ? 35  PRO B N   1 
ATOM   1003 C CA  . PRO B 1 36 ? 34.242  -15.685 -29.465 1.00 55.50  ? 35  PRO B CA  1 
ATOM   1004 C C   . PRO B 1 36 ? 35.168  -16.895 -29.477 1.00 51.11  ? 35  PRO B C   1 
ATOM   1005 O O   . PRO B 1 36 ? 36.243  -16.835 -30.063 1.00 54.28  ? 35  PRO B O   1 
ATOM   1006 C CB  . PRO B 1 36 ? 33.443  -15.538 -30.780 1.00 56.47  ? 35  PRO B CB  1 
ATOM   1007 C CG  . PRO B 1 36 ? 34.232  -14.524 -31.596 1.00 60.71  ? 35  PRO B CG  1 
ATOM   1008 C CD  . PRO B 1 36 ? 34.823  -13.571 -30.561 1.00 60.38  ? 35  PRO B CD  1 
ATOM   1009 N N   . PRO B 1 37 ? 34.797  -18.029 -28.839 1.00 51.16  ? 36  PRO B N   1 
ATOM   1010 C CA  . PRO B 1 37 ? 35.524  -19.278 -29.038 1.00 50.69  ? 36  PRO B CA  1 
ATOM   1011 C C   . PRO B 1 37 ? 35.583  -19.556 -30.540 1.00 55.07  ? 36  PRO B C   1 
ATOM   1012 O O   . PRO B 1 37 ? 34.821  -18.982 -31.322 1.00 51.23  ? 36  PRO B O   1 
ATOM   1013 C CB  . PRO B 1 37 ? 34.676  -20.326 -28.301 1.00 48.95  ? 36  PRO B CB  1 
ATOM   1014 C CG  . PRO B 1 37 ? 33.899  -19.535 -27.281 1.00 48.78  ? 36  PRO B CG  1 
ATOM   1015 C CD  . PRO B 1 37 ? 33.660  -18.174 -27.917 1.00 50.01  ? 36  PRO B CD  1 
ATOM   1016 N N   . PRO B 1 38 ? 36.473  -20.462 -31.001 1.00 55.83  ? 37  PRO B N   1 
ATOM   1017 C CA  . PRO B 1 38 ? 36.534  -20.808 -32.426 1.00 60.05  ? 37  PRO B CA  1 
ATOM   1018 C C   . PRO B 1 38 ? 35.218  -21.408 -32.932 1.00 54.26  ? 37  PRO B C   1 
ATOM   1019 O O   . PRO B 1 38 ? 34.582  -22.205 -32.238 1.00 50.79  ? 37  PRO B O   1 
ATOM   1020 C CB  . PRO B 1 38 ? 37.708  -21.810 -32.530 1.00 60.17  ? 37  PRO B CB  1 
ATOM   1021 C CG  . PRO B 1 38 ? 38.445  -21.697 -31.200 1.00 56.61  ? 37  PRO B CG  1 
ATOM   1022 C CD  . PRO B 1 38 ? 37.433  -21.212 -30.174 1.00 60.20  ? 37  PRO B CD  1 
ATOM   1023 N N   . ASN B 1 39 ? 34.827  -21.008 -34.149 1.00 46.79  ? 38  ASN B N   1 
ATOM   1024 C CA  . ASN B 1 39 ? 33.632  -21.489 -34.836 1.00 50.34  ? 38  ASN B CA  1 
ATOM   1025 C C   . ASN B 1 39 ? 32.381  -20.683 -34.471 1.00 42.38  ? 38  ASN B C   1 
ATOM   1026 O O   . ASN B 1 39 ? 31.375  -20.817 -35.146 1.00 42.45  ? 38  ASN B O   1 
ATOM   1027 C CB  . ASN B 1 39 ? 33.351  -22.975 -34.625 1.00 49.30  ? 38  ASN B CB  1 
ATOM   1028 C CG  . ASN B 1 39 ? 34.514  -23.874 -34.977 1.00 62.41  ? 38  ASN B CG  1 
ATOM   1029 O OD1 . ASN B 1 39 ? 34.728  -24.888 -34.302 1.00 71.42  ? 38  ASN B OD1 1 
ATOM   1030 N ND2 . ASN B 1 39 ? 35.255  -23.549 -36.028 1.00 56.42  ? 38  ASN B ND2 1 
ATOM   1031 N N   . LYS B 1 40 ? 32.436  -19.857 -33.416 1.00 44.10  ? 39  LYS B N   1 
ATOM   1032 C CA  . LYS B 1 40 ? 31.242  -19.257 -32.847 1.00 39.26  ? 39  LYS B CA  1 
ATOM   1033 C C   . LYS B 1 40 ? 31.222  -17.750 -33.092 1.00 42.62  ? 39  LYS B C   1 
ATOM   1034 O O   . LYS B 1 40 ? 32.258  -17.131 -33.349 1.00 42.94  ? 39  LYS B O   1 
ATOM   1035 C CB  . LYS B 1 40 ? 31.208  -19.581 -31.352 1.00 41.90  ? 39  LYS B CB  1 
ATOM   1036 C CG  . LYS B 1 40 ? 31.110  -21.049 -30.984 1.00 43.92  ? 39  LYS B CG  1 
ATOM   1037 C CD  . LYS B 1 40 ? 30.795  -21.054 -29.491 1.00 55.13  ? 39  LYS B CD  1 
ATOM   1038 C CE  . LYS B 1 40 ? 29.741  -22.026 -29.046 1.00 63.32  ? 39  LYS B CE  1 
ATOM   1039 N NZ  . LYS B 1 40 ? 30.271  -23.344 -28.700 1.00 69.10  ? 39  LYS B NZ  1 
ATOM   1040 N N   . TYR B 1 41 ? 30.019  -17.170 -33.037 1.00 39.32  ? 40  TYR B N   1 
ATOM   1041 C CA  . TYR B 1 41 ? 29.850  -15.750 -33.277 1.00 36.74  ? 40  TYR B CA  1 
ATOM   1042 C C   . TYR B 1 41 ? 29.279  -15.051 -32.045 1.00 38.80  ? 40  TYR B C   1 
ATOM   1043 O O   . TYR B 1 41 ? 28.519  -15.646 -31.283 1.00 37.00  ? 40  TYR B O   1 
ATOM   1044 C CB  . TYR B 1 41 ? 28.859  -15.534 -34.416 1.00 34.69  ? 40  TYR B CB  1 
ATOM   1045 C CG  . TYR B 1 41 ? 29.335  -16.012 -35.779 1.00 38.43  ? 40  TYR B CG  1 
ATOM   1046 C CD1 . TYR B 1 41 ? 29.932  -15.116 -36.668 1.00 36.80  ? 40  TYR B CD1 1 
ATOM   1047 C CD2 . TYR B 1 41 ? 29.166  -17.333 -36.191 1.00 38.67  ? 40  TYR B CD2 1 
ATOM   1048 C CE1 . TYR B 1 41 ? 30.379  -15.534 -37.913 1.00 42.50  ? 40  TYR B CE1 1 
ATOM   1049 C CE2 . TYR B 1 41 ? 29.596  -17.755 -37.445 1.00 38.39  ? 40  TYR B CE2 1 
ATOM   1050 C CZ  . TYR B 1 41 ? 30.225  -16.855 -38.299 1.00 39.41  ? 40  TYR B CZ  1 
ATOM   1051 O OH  . TYR B 1 41 ? 30.658  -17.207 -39.557 1.00 42.90  ? 40  TYR B OH  1 
ATOM   1052 N N   . PRO B 1 42 ? 29.545  -13.730 -31.886 1.00 39.74  ? 41  PRO B N   1 
ATOM   1053 C CA  . PRO B 1 42 ? 28.855  -12.928 -30.878 1.00 34.03  ? 41  PRO B CA  1 
ATOM   1054 C C   . PRO B 1 42 ? 27.429  -12.680 -31.361 1.00 33.80  ? 41  PRO B C   1 
ATOM   1055 O O   . PRO B 1 42 ? 27.224  -12.047 -32.408 1.00 37.74  ? 41  PRO B O   1 
ATOM   1056 C CB  . PRO B 1 42 ? 29.683  -11.616 -30.779 1.00 36.03  ? 41  PRO B CB  1 
ATOM   1057 C CG  . PRO B 1 42 ? 30.496  -11.559 -32.064 1.00 37.41  ? 41  PRO B CG  1 
ATOM   1058 C CD  . PRO B 1 42 ? 30.479  -12.941 -32.710 1.00 35.77  ? 41  PRO B CD  1 
ATOM   1059 N N   . ILE B 1 43 ? 26.451  -13.170 -30.569 1.00 31.10  ? 42  ILE B N   1 
ATOM   1060 C CA  . ILE B 1 43 ? 25.034  -12.948 -30.834 1.00 27.99  ? 42  ILE B CA  1 
ATOM   1061 C C   . ILE B 1 43 ? 24.438  -11.913 -29.874 1.00 28.17  ? 42  ILE B C   1 
ATOM   1062 O O   . ILE B 1 43 ? 24.698  -11.958 -28.676 1.00 33.02  ? 42  ILE B O   1 
ATOM   1063 C CB  . ILE B 1 43 ? 24.287  -14.288 -30.732 1.00 27.45  ? 42  ILE B CB  1 
ATOM   1064 C CG1 . ILE B 1 43 ? 25.007  -15.405 -31.558 1.00 29.90  ? 42  ILE B CG1 1 
ATOM   1065 C CG2 . ILE B 1 43 ? 22.823  -14.113 -31.149 1.00 29.84  ? 42  ILE B CG2 1 
ATOM   1066 C CD1 . ILE B 1 43 ? 25.324  -15.052 -33.002 1.00 26.75  ? 42  ILE B CD1 1 
ATOM   1067 N N   . PHE B 1 44 ? 23.605  -11.026 -30.428 1.00 28.75  ? 43  PHE B N   1 
ATOM   1068 C CA  . PHE B 1 44 ? 22.785  -10.072 -29.688 1.00 31.13  ? 43  PHE B CA  1 
ATOM   1069 C C   . PHE B 1 44 ? 21.323  -10.473 -29.866 1.00 27.00  ? 43  PHE B C   1 
ATOM   1070 O O   . PHE B 1 44 ? 20.824  -10.545 -30.997 1.00 26.44  ? 43  PHE B O   1 
ATOM   1071 C CB  . PHE B 1 44 ? 23.016  -8.615  -30.131 1.00 29.19  ? 43  PHE B CB  1 
ATOM   1072 C CG  . PHE B 1 44 ? 22.091  -7.586  -29.478 1.00 28.48  ? 43  PHE B CG  1 
ATOM   1073 C CD1 . PHE B 1 44 ? 20.914  -7.181  -30.109 1.00 30.75  ? 43  PHE B CD1 1 
ATOM   1074 C CD2 . PHE B 1 44 ? 22.366  -7.079  -28.212 1.00 35.99  ? 43  PHE B CD2 1 
ATOM   1075 C CE1 . PHE B 1 44 ? 20.060  -6.254  -29.511 1.00 31.17  ? 43  PHE B CE1 1 
ATOM   1076 C CE2 . PHE B 1 44 ? 21.517  -6.152  -27.601 1.00 30.72  ? 43  PHE B CE2 1 
ATOM   1077 C CZ  . PHE B 1 44 ? 20.369  -5.747  -28.261 1.00 31.80  ? 43  PHE B CZ  1 
ATOM   1078 N N   . PHE B 1 45 ? 20.637  -10.776 -28.747 1.00 26.26  ? 44  PHE B N   1 
ATOM   1079 C CA  . PHE B 1 45 ? 19.232  -11.153 -28.839 1.00 24.83  ? 44  PHE B CA  1 
ATOM   1080 C C   . PHE B 1 45 ? 18.350  -9.921  -28.728 1.00 26.31  ? 44  PHE B C   1 
ATOM   1081 O O   . PHE B 1 45 ? 18.380  -9.239  -27.710 1.00 26.84  ? 44  PHE B O   1 
ATOM   1082 C CB  . PHE B 1 45 ? 18.874  -12.131 -27.706 1.00 25.09  ? 44  PHE B CB  1 
ATOM   1083 C CG  . PHE B 1 45 ? 19.609  -13.457 -27.858 1.00 26.42  ? 44  PHE B CG  1 
ATOM   1084 C CD1 . PHE B 1 45 ? 20.914  -13.613 -27.419 1.00 29.39  ? 44  PHE B CD1 1 
ATOM   1085 C CD2 . PHE B 1 45 ? 18.975  -14.560 -28.431 1.00 26.19  ? 44  PHE B CD2 1 
ATOM   1086 C CE1 . PHE B 1 45 ? 21.580  -14.823 -27.601 1.00 31.71  ? 44  PHE B CE1 1 
ATOM   1087 C CE2 . PHE B 1 45 ? 19.647  -15.774 -28.594 1.00 32.26  ? 44  PHE B CE2 1 
ATOM   1088 C CZ  . PHE B 1 45 ? 20.958  -15.897 -28.211 1.00 27.96  ? 44  PHE B CZ  1 
ATOM   1089 N N   . PHE B 1 46 ? 17.504  -9.669  -29.749 1.00 26.90  ? 45  PHE B N   1 
ATOM   1090 C CA  . PHE B 1 46 ? 16.572  -8.564  -29.644 1.00 28.02  ? 45  PHE B CA  1 
ATOM   1091 C C   . PHE B 1 46 ? 15.540  -8.783  -28.523 1.00 30.00  ? 45  PHE B C   1 
ATOM   1092 O O   . PHE B 1 46 ? 15.235  -9.917  -28.153 1.00 28.29  ? 45  PHE B O   1 
ATOM   1093 C CB  . PHE B 1 46 ? 15.835  -8.377  -30.958 1.00 25.36  ? 45  PHE B CB  1 
ATOM   1094 C CG  . PHE B 1 46 ? 16.770  -7.956  -32.084 1.00 32.36  ? 45  PHE B CG  1 
ATOM   1095 C CD1 . PHE B 1 46 ? 17.239  -6.638  -32.168 1.00 33.85  ? 45  PHE B CD1 1 
ATOM   1096 C CD2 . PHE B 1 46 ? 17.135  -8.847  -33.094 1.00 28.28  ? 45  PHE B CD2 1 
ATOM   1097 C CE1 . PHE B 1 46 ? 18.063  -6.233  -33.222 1.00 32.35  ? 45  PHE B CE1 1 
ATOM   1098 C CE2 . PHE B 1 46 ? 17.988  -8.432  -34.129 1.00 28.42  ? 45  PHE B CE2 1 
ATOM   1099 C CZ  . PHE B 1 46 ? 18.432  -7.129  -34.199 1.00 28.13  ? 45  PHE B CZ  1 
ATOM   1100 N N   . GLY B 1 47 ? 14.941  -7.676  -28.063 1.00 29.13  ? 46  GLY B N   1 
ATOM   1101 C CA  . GLY B 1 47 ? 13.919  -7.694  -27.020 1.00 30.65  ? 46  GLY B CA  1 
ATOM   1102 C C   . GLY B 1 47 ? 14.552  -7.829  -25.631 1.00 32.96  ? 46  GLY B C   1 
ATOM   1103 O O   . GLY B 1 47 ? 14.364  -6.958  -24.794 1.00 34.30  ? 46  GLY B O   1 
ATOM   1104 N N   . THR B 1 48 ? 15.266  -8.931  -25.376 1.00 29.87  ? 47  THR B N   1 
ATOM   1105 C CA  . THR B 1 48 ? 15.906  -9.142  -24.088 1.00 32.12  ? 47  THR B CA  1 
ATOM   1106 C C   . THR B 1 48 ? 17.222  -8.370  -23.999 1.00 34.19  ? 47  THR B C   1 
ATOM   1107 O O   . THR B 1 48 ? 17.716  -8.114  -22.894 1.00 30.55  ? 47  THR B O   1 
ATOM   1108 C CB  . THR B 1 48 ? 16.173  -10.627 -23.840 1.00 31.99  ? 47  THR B CB  1 
ATOM   1109 O OG1 . THR B 1 48 ? 17.117  -11.076 -24.814 1.00 27.97  ? 47  THR B OG1 1 
ATOM   1110 C CG2 . THR B 1 48 ? 14.897  -11.441 -23.848 1.00 28.85  ? 47  THR B CG2 1 
ATOM   1111 N N   . HIS B 1 49 ? 17.828  -8.119  -25.169 1.00 29.31  ? 48  HIS B N   1 
ATOM   1112 C CA  . HIS B 1 49 ? 19.122  -7.459  -25.311 1.00 32.77  ? 48  HIS B CA  1 
ATOM   1113 C C   . HIS B 1 49 ? 20.227  -8.225  -24.604 1.00 35.50  ? 48  HIS B C   1 
ATOM   1114 O O   . HIS B 1 49 ? 21.226  -7.617  -24.219 1.00 39.79  ? 48  HIS B O   1 
ATOM   1115 C CB  . HIS B 1 49 ? 19.086  -5.974  -24.901 1.00 32.25  ? 48  HIS B CB  1 
ATOM   1116 C CG  . HIS B 1 49 ? 17.930  -5.243  -25.493 1.00 36.12  ? 48  HIS B CG  1 
ATOM   1117 N ND1 . HIS B 1 49 ? 17.191  -4.358  -24.740 1.00 39.46  ? 48  HIS B ND1 1 
ATOM   1118 C CD2 . HIS B 1 49 ? 17.330  -5.292  -26.705 1.00 32.36  ? 48  HIS B CD2 1 
ATOM   1119 C CE1 . HIS B 1 49 ? 16.193  -3.884  -25.483 1.00 42.05  ? 48  HIS B CE1 1 
ATOM   1120 N NE2 . HIS B 1 49 ? 16.254  -4.442  -26.682 1.00 40.66  ? 48  HIS B NE2 1 
ATOM   1121 N N   . GLU B 1 50 ? 20.070  -9.540  -24.457 1.00 29.42  ? 49  GLU B N   1 
ATOM   1122 C CA  . GLU B 1 50 ? 21.164  -10.357 -23.952 1.00 34.12  ? 49  GLU B CA  1 
ATOM   1123 C C   . GLU B 1 50 ? 22.111  -10.745 -25.087 1.00 33.37  ? 49  GLU B C   1 
ATOM   1124 O O   . GLU B 1 50 ? 21.804  -10.497 -26.253 1.00 32.46  ? 49  GLU B O   1 
ATOM   1125 C CB  . GLU B 1 50 ? 20.609  -11.610 -23.293 1.00 40.89  ? 49  GLU B CB  1 
ATOM   1126 C CG  . GLU B 1 50 ? 19.729  -11.207 -22.118 1.00 45.07  ? 49  GLU B CG  1 
ATOM   1127 C CD  . GLU B 1 50 ? 19.848  -12.129 -20.933 1.00 48.64  ? 49  GLU B CD  1 
ATOM   1128 O OE1 . GLU B 1 50 ? 20.706  -13.026 -20.952 1.00 52.65  ? 49  GLU B OE1 1 
ATOM   1129 O OE2 . GLU B 1 50 ? 19.047  -11.949 -20.004 1.00 50.00  ? 49  GLU B OE2 1 
ATOM   1130 N N   . THR B 1 51 ? 23.267  -11.300 -24.713 1.00 32.95  ? 50  THR B N   1 
ATOM   1131 C CA  . THR B 1 51 ? 24.280  -11.741 -25.664 1.00 35.01  ? 50  THR B CA  1 
ATOM   1132 C C   . THR B 1 51 ? 24.668  -13.170 -25.306 1.00 36.77  ? 50  THR B C   1 
ATOM   1133 O O   . THR B 1 51 ? 24.475  -13.616 -24.171 1.00 36.02  ? 50  THR B O   1 
ATOM   1134 C CB  . THR B 1 51 ? 25.493  -10.794 -25.673 1.00 38.01  ? 50  THR B CB  1 
ATOM   1135 O OG1 . THR B 1 51 ? 26.059  -10.894 -24.370 1.00 44.75  ? 50  THR B OG1 1 
ATOM   1136 C CG2 . THR B 1 51 ? 25.138  -9.338  -25.930 1.00 40.45  ? 50  THR B CG2 1 
ATOM   1137 N N   . ALA B 1 52 ? 25.181  -13.898 -26.304 1.00 38.37  ? 51  ALA B N   1 
ATOM   1138 C CA  . ALA B 1 52 ? 25.833  -15.174 -26.082 1.00 36.42  ? 51  ALA B CA  1 
ATOM   1139 C C   . ALA B 1 52 ? 26.716  -15.498 -27.285 1.00 38.78  ? 51  ALA B C   1 
ATOM   1140 O O   . ALA B 1 52 ? 26.677  -14.773 -28.279 1.00 38.80  ? 51  ALA B O   1 
ATOM   1141 C CB  . ALA B 1 52 ? 24.821  -16.262 -25.821 1.00 30.50  ? 51  ALA B CB  1 
ATOM   1142 N N   . PHE B 1 53 ? 27.514  -16.567 -27.165 1.00 36.98  ? 52  PHE B N   1 
ATOM   1143 C CA  . PHE B 1 53 ? 28.323  -17.065 -28.271 1.00 41.04  ? 52  PHE B CA  1 
ATOM   1144 C C   . PHE B 1 53 ? 27.659  -18.321 -28.838 1.00 40.23  ? 52  PHE B C   1 
ATOM   1145 O O   . PHE B 1 53 ? 27.422  -19.273 -28.098 1.00 36.09  ? 52  PHE B O   1 
ATOM   1146 C CB  . PHE B 1 53 ? 29.768  -17.365 -27.843 1.00 43.11  ? 52  PHE B CB  1 
ATOM   1147 C CG  . PHE B 1 53 ? 30.565  -16.136 -27.431 1.00 42.02  ? 52  PHE B CG  1 
ATOM   1148 C CD1 . PHE B 1 53 ? 30.696  -15.057 -28.295 1.00 43.71  ? 52  PHE B CD1 1 
ATOM   1149 C CD2 . PHE B 1 53 ? 31.119  -16.036 -26.155 1.00 49.07  ? 52  PHE B CD2 1 
ATOM   1150 C CE1 . PHE B 1 53 ? 31.384  -13.917 -27.910 1.00 44.21  ? 52  PHE B CE1 1 
ATOM   1151 C CE2 . PHE B 1 53 ? 31.813  -14.894 -25.769 1.00 48.42  ? 52  PHE B CE2 1 
ATOM   1152 C CZ  . PHE B 1 53 ? 31.937  -13.839 -26.641 1.00 47.12  ? 52  PHE B CZ  1 
ATOM   1153 N N   . LEU B 1 54 ? 27.380  -18.334 -30.156 1.00 33.86  ? 53  LEU B N   1 
ATOM   1154 C CA  . LEU B 1 54 ? 26.718  -19.489 -30.753 1.00 31.62  ? 53  LEU B CA  1 
ATOM   1155 C C   . LEU B 1 54 ? 27.421  -19.858 -32.059 1.00 34.59  ? 53  LEU B C   1 
ATOM   1156 O O   . LEU B 1 54 ? 27.901  -18.966 -32.771 1.00 32.03  ? 53  LEU B O   1 
ATOM   1157 C CB  . LEU B 1 54 ? 25.249  -19.196 -31.070 1.00 30.96  ? 53  LEU B CB  1 
ATOM   1158 C CG  . LEU B 1 54 ? 24.266  -19.148 -29.897 1.00 32.78  ? 53  LEU B CG  1 
ATOM   1159 C CD1 . LEU B 1 54 ? 22.911  -18.686 -30.427 1.00 31.89  ? 53  LEU B CD1 1 
ATOM   1160 C CD2 . LEU B 1 54 ? 24.149  -20.527 -29.235 1.00 32.73  ? 53  LEU B CD2 1 
ATOM   1161 N N   . GLY B 1 55 ? 27.392  -21.155 -32.390 1.00 32.91  ? 54  GLY B N   1 
ATOM   1162 C CA  . GLY B 1 55 ? 27.914  -21.633 -33.660 1.00 32.60  ? 54  GLY B CA  1 
ATOM   1163 C C   . GLY B 1 55 ? 26.821  -21.700 -34.721 1.00 34.07  ? 54  GLY B C   1 
ATOM   1164 O O   . GLY B 1 55 ? 25.621  -21.628 -34.421 1.00 33.42  ? 54  GLY B O   1 
ATOM   1165 N N   . PRO B 1 56 ? 27.183  -21.872 -36.012 1.00 30.25  ? 55  PRO B N   1 
ATOM   1166 C CA  . PRO B 1 56 ? 26.188  -21.902 -37.078 1.00 28.48  ? 55  PRO B CA  1 
ATOM   1167 C C   . PRO B 1 56 ? 25.025  -22.885 -36.981 1.00 29.59  ? 55  PRO B C   1 
ATOM   1168 O O   . PRO B 1 56 ? 23.977  -22.582 -37.504 1.00 28.58  ? 55  PRO B O   1 
ATOM   1169 C CB  . PRO B 1 56 ? 27.017  -22.163 -38.353 1.00 31.87  ? 55  PRO B CB  1 
ATOM   1170 C CG  . PRO B 1 56 ? 28.436  -21.852 -37.969 1.00 31.77  ? 55  PRO B CG  1 
ATOM   1171 C CD  . PRO B 1 56 ? 28.562  -22.063 -36.484 1.00 31.31  ? 55  PRO B CD  1 
ATOM   1172 N N   . LYS B 1 57 ? 25.187  -24.053 -36.312 1.00 30.76  ? 56  LYS B N   1 
ATOM   1173 C CA  . LYS B 1 57 ? 24.100  -25.028 -36.229 1.00 33.48  ? 56  LYS B CA  1 
ATOM   1174 C C   . LYS B 1 57 ? 22.883  -24.380 -35.560 1.00 31.95  ? 56  LYS B C   1 
ATOM   1175 O O   . LYS B 1 57 ? 21.739  -24.792 -35.788 1.00 28.47  ? 56  LYS B O   1 
ATOM   1176 C CB  . LYS B 1 57 ? 24.492  -26.329 -35.505 1.00 34.48  ? 56  LYS B CB  1 
ATOM   1177 C CG  . LYS B 1 57 ? 24.742  -26.208 -34.018 1.00 35.71  ? 56  LYS B CG  1 
ATOM   1178 C CD  . LYS B 1 57 ? 24.830  -27.581 -33.357 1.00 40.18  ? 56  LYS B CD  1 
ATOM   1179 C CE  . LYS B 1 57 ? 25.115  -27.502 -31.877 1.00 48.61  ? 56  LYS B CE  1 
ATOM   1180 N NZ  . LYS B 1 57 ? 24.008  -26.947 -31.089 1.00 51.32  ? 56  LYS B NZ  1 
ATOM   1181 N N   . ASP B 1 58 ? 23.139  -23.298 -34.814 1.00 30.47  ? 57  ASP B N   1 
ATOM   1182 C CA  . ASP B 1 58 ? 22.084  -22.686 -34.018 1.00 30.96  ? 57  ASP B CA  1 
ATOM   1183 C C   . ASP B 1 58 ? 21.644  -21.341 -34.600 1.00 31.19  ? 57  ASP B C   1 
ATOM   1184 O O   . ASP B 1 58 ? 20.901  -20.595 -33.934 1.00 27.06  ? 57  ASP B O   1 
ATOM   1185 C CB  . ASP B 1 58 ? 22.489  -22.585 -32.553 1.00 29.95  ? 57  ASP B CB  1 
ATOM   1186 C CG  . ASP B 1 58 ? 22.616  -23.909 -31.808 1.00 36.05  ? 57  ASP B CG  1 
ATOM   1187 O OD1 . ASP B 1 58 ? 21.719  -24.746 -31.969 1.00 32.25  ? 57  ASP B OD1 1 
ATOM   1188 O OD2 . ASP B 1 58 ? 23.581  -24.054 -31.032 1.00 37.42  ? 57  ASP B OD2 1 
ATOM   1189 N N   . LEU B 1 59 ? 22.079  -21.053 -35.845 1.00 27.88  ? 58  LEU B N   1 
ATOM   1190 C CA  . LEU B 1 59 ? 21.911  -19.732 -36.441 1.00 27.58  ? 58  LEU B CA  1 
ATOM   1191 C C   . LEU B 1 59 ? 21.198  -19.885 -37.776 1.00 30.30  ? 58  LEU B C   1 
ATOM   1192 O O   . LEU B 1 59 ? 21.681  -20.595 -38.654 1.00 30.57  ? 58  LEU B O   1 
ATOM   1193 C CB  . LEU B 1 59 ? 23.270  -19.047 -36.609 1.00 29.10  ? 58  LEU B CB  1 
ATOM   1194 C CG  . LEU B 1 59 ? 24.032  -18.754 -35.313 1.00 31.35  ? 58  LEU B CG  1 
ATOM   1195 C CD1 . LEU B 1 59 ? 25.348  -18.059 -35.642 1.00 29.36  ? 58  LEU B CD1 1 
ATOM   1196 C CD2 . LEU B 1 59 ? 23.196  -17.886 -34.370 1.00 28.35  ? 58  LEU B CD2 1 
ATOM   1197 N N   . PHE B 1 60 ? 20.022  -19.266 -37.869 1.00 26.76  ? 59  PHE B N   1 
ATOM   1198 C CA  . PHE B 1 60 ? 19.073  -19.449 -38.949 1.00 27.16  ? 59  PHE B CA  1 
ATOM   1199 C C   . PHE B 1 60 ? 18.886  -18.091 -39.624 1.00 30.10  ? 59  PHE B C   1 
ATOM   1200 O O   . PHE B 1 60 ? 18.251  -17.195 -39.074 1.00 28.55  ? 59  PHE B O   1 
ATOM   1201 C CB  . PHE B 1 60 ? 17.725  -19.962 -38.425 1.00 25.52  ? 59  PHE B CB  1 
ATOM   1202 C CG  . PHE B 1 60 ? 17.808  -21.358 -37.820 1.00 25.75  ? 59  PHE B CG  1 
ATOM   1203 C CD1 . PHE B 1 60 ? 18.332  -21.545 -36.545 1.00 27.42  ? 59  PHE B CD1 1 
ATOM   1204 C CD2 . PHE B 1 60 ? 17.411  -22.480 -38.559 1.00 29.38  ? 59  PHE B CD2 1 
ATOM   1205 C CE1 . PHE B 1 60 ? 18.430  -22.833 -36.001 1.00 30.44  ? 59  PHE B CE1 1 
ATOM   1206 C CE2 . PHE B 1 60 ? 17.497  -23.767 -38.013 1.00 31.66  ? 59  PHE B CE2 1 
ATOM   1207 C CZ  . PHE B 1 60 ? 18.024  -23.936 -36.737 1.00 30.74  ? 59  PHE B CZ  1 
ATOM   1208 N N   . PRO B 1 61 ? 19.442  -17.878 -40.841 1.00 34.58  ? 60  PRO B N   1 
ATOM   1209 C CA  . PRO B 1 61 ? 19.202  -16.618 -41.564 1.00 33.28  ? 60  PRO B CA  1 
ATOM   1210 C C   . PRO B 1 61 ? 17.748  -16.137 -41.523 1.00 31.42  ? 60  PRO B C   1 
ATOM   1211 O O   . PRO B 1 61 ? 16.822  -16.891 -41.822 1.00 31.82  ? 60  PRO B O   1 
ATOM   1212 C CB  . PRO B 1 61 ? 19.728  -16.925 -42.987 1.00 31.86  ? 60  PRO B CB  1 
ATOM   1213 C CG  . PRO B 1 61 ? 20.855  -17.917 -42.725 1.00 41.59  ? 60  PRO B CG  1 
ATOM   1214 C CD  . PRO B 1 61 ? 20.376  -18.788 -41.534 1.00 38.93  ? 60  PRO B CD  1 
ATOM   1215 N N   . TYR B 1 62 ? 17.543  -14.838 -41.208 1.00 30.40  ? 61  TYR B N   1 
ATOM   1216 C CA  . TYR B 1 62 ? 16.228  -14.323 -40.854 1.00 29.46  ? 61  TYR B CA  1 
ATOM   1217 C C   . TYR B 1 62 ? 15.245  -14.338 -42.015 1.00 32.21  ? 61  TYR B C   1 
ATOM   1218 O O   . TYR B 1 62 ? 14.112  -14.785 -41.861 1.00 34.02  ? 61  TYR B O   1 
ATOM   1219 C CB  . TYR B 1 62 ? 16.370  -12.865 -40.414 1.00 36.22  ? 61  TYR B CB  1 
ATOM   1220 C CG  . TYR B 1 62 ? 15.049  -12.157 -40.161 1.00 33.06  ? 61  TYR B CG  1 
ATOM   1221 C CD1 . TYR B 1 62 ? 14.321  -12.396 -38.998 1.00 33.12  ? 61  TYR B CD1 1 
ATOM   1222 C CD2 . TYR B 1 62 ? 14.573  -11.203 -41.055 1.00 37.81  ? 61  TYR B CD2 1 
ATOM   1223 C CE1 . TYR B 1 62 ? 13.142  -11.712 -38.751 1.00 33.68  ? 61  TYR B CE1 1 
ATOM   1224 C CE2 . TYR B 1 62 ? 13.394  -10.516 -40.820 1.00 42.22  ? 61  TYR B CE2 1 
ATOM   1225 C CZ  . TYR B 1 62 ? 12.681  -10.773 -39.661 1.00 36.89  ? 61  TYR B CZ  1 
ATOM   1226 O OH  . TYR B 1 62 ? 11.514  -10.094 -39.446 1.00 44.52  ? 61  TYR B OH  1 
ATOM   1227 N N   . ASP B 1 63 ? 15.708  -13.902 -43.196 1.00 37.68  ? 62  ASP B N   1 
ATOM   1228 C CA  . ASP B 1 63 ? 14.883  -13.895 -44.400 1.00 41.97  ? 62  ASP B CA  1 
ATOM   1229 C C   . ASP B 1 63 ? 14.320  -15.274 -44.729 1.00 36.79  ? 62  ASP B C   1 
ATOM   1230 O O   . ASP B 1 63 ? 13.120  -15.402 -44.945 1.00 39.91  ? 62  ASP B O   1 
ATOM   1231 C CB  . ASP B 1 63 ? 15.619  -13.305 -45.588 1.00 50.96  ? 62  ASP B CB  1 
ATOM   1232 C CG  . ASP B 1 63 ? 15.236  -11.868 -45.889 1.00 65.93  ? 62  ASP B CG  1 
ATOM   1233 O OD1 . ASP B 1 63 ? 14.712  -11.192 -44.965 1.00 65.03  ? 62  ASP B OD1 1 
ATOM   1234 O OD2 . ASP B 1 63 ? 15.410  -11.463 -47.059 1.00 75.44  ? 62  ASP B OD2 1 
ATOM   1235 N N   . LYS B 1 64 ? 15.184  -16.296 -44.732 1.00 41.99  ? 63  LYS B N   1 
ATOM   1236 C CA  . LYS B 1 64 ? 14.758  -17.653 -45.039 1.00 41.00  ? 63  LYS B CA  1 
ATOM   1237 C C   . LYS B 1 64 ? 13.735  -18.172 -44.020 1.00 38.56  ? 63  LYS B C   1 
ATOM   1238 O O   . LYS B 1 64 ? 12.843  -18.939 -44.371 1.00 41.03  ? 63  LYS B O   1 
ATOM   1239 C CB  . LYS B 1 64 ? 15.979  -18.580 -45.043 1.00 43.07  ? 63  LYS B CB  1 
ATOM   1240 C CG  . LYS B 1 64 ? 15.594  -19.987 -45.478 1.00 41.58  ? 63  LYS B CG  1 
ATOM   1241 C CD  . LYS B 1 64 ? 16.796  -20.881 -45.707 1.00 48.62  ? 63  LYS B CD  1 
ATOM   1242 C CE  . LYS B 1 64 ? 16.457  -22.135 -46.470 1.00 50.25  ? 63  LYS B CE  1 
ATOM   1243 N NZ  . LYS B 1 64 ? 15.348  -22.895 -45.902 1.00 44.97  ? 63  LYS B NZ  1 
ATOM   1244 N N   . SER B 1 65 ? 13.868  -17.773 -42.752 1.00 36.80  ? 64  SER B N   1 
ATOM   1245 C CA  . SER B 1 65 ? 13.210  -18.520 -41.689 1.00 36.57  ? 64  SER B CA  1 
ATOM   1246 C C   . SER B 1 65 ? 12.122  -17.730 -40.952 1.00 36.91  ? 64  SER B C   1 
ATOM   1247 O O   . SER B 1 65 ? 11.484  -18.269 -40.050 1.00 35.46  ? 64  SER B O   1 
ATOM   1248 C CB  . SER B 1 65 ? 14.234  -19.142 -40.764 1.00 37.43  ? 64  SER B CB  1 
ATOM   1249 O OG  . SER B 1 65 ? 14.992  -18.123 -40.142 1.00 46.26  ? 64  SER B OG  1 
ATOM   1250 N N   . LYS B 1 66 ? 11.851  -16.481 -41.355 1.00 35.51  ? 65  LYS B N   1 
ATOM   1251 C CA  . LYS B 1 66 ? 10.937  -15.640 -40.585 1.00 36.11  ? 65  LYS B CA  1 
ATOM   1252 C C   . LYS B 1 66 ? 9.512   -16.188 -40.591 1.00 41.06  ? 65  LYS B C   1 
ATOM   1253 O O   . LYS B 1 66 ? 8.798   -16.044 -39.599 1.00 41.81  ? 65  LYS B O   1 
ATOM   1254 C CB  . LYS B 1 66 ? 10.947  -14.159 -40.984 1.00 39.52  ? 65  LYS B CB  1 
ATOM   1255 C CG  . LYS B 1 66 ? 10.696  -13.943 -42.466 1.00 41.20  ? 65  LYS B CG  1 
ATOM   1256 C CD  . LYS B 1 66 ? 10.802  -12.485 -42.892 1.00 54.53  ? 65  LYS B CD  1 
ATOM   1257 C CE  . LYS B 1 66 ? 10.565  -12.331 -44.372 1.00 61.03  ? 65  LYS B CE  1 
ATOM   1258 N NZ  . LYS B 1 66 ? 11.007  -11.001 -44.804 1.00 67.09  ? 65  LYS B NZ  1 
ATOM   1259 N N   . ASP B 1 67 ? 9.093   -16.815 -41.697 1.00 38.93  ? 66  ASP B N   1 
ATOM   1260 C CA  . ASP B 1 67 ? 7.744   -17.350 -41.770 1.00 45.65  ? 66  ASP B CA  1 
ATOM   1261 C C   . ASP B 1 67 ? 7.587   -18.441 -40.716 1.00 42.63  ? 66  ASP B C   1 
ATOM   1262 O O   . ASP B 1 67 ? 6.540   -18.558 -40.086 1.00 46.19  ? 66  ASP B O   1 
ATOM   1263 C CB  . ASP B 1 67 ? 7.441   -17.930 -43.146 1.00 60.01  ? 66  ASP B CB  1 
ATOM   1264 C CG  . ASP B 1 67 ? 7.586   -16.982 -44.330 1.00 78.84  ? 66  ASP B CG  1 
ATOM   1265 O OD1 . ASP B 1 67 ? 7.858   -15.777 -44.104 1.00 92.10  ? 66  ASP B OD1 1 
ATOM   1266 O OD2 . ASP B 1 67 ? 7.436   -17.458 -45.479 1.00 79.19  ? 66  ASP B OD2 1 
ATOM   1267 N N   . LYS B 1 68 ? 8.639   -19.244 -40.525 1.00 39.71  ? 67  LYS B N   1 
ATOM   1268 C CA  . LYS B 1 68 ? 8.558   -20.366 -39.603 1.00 36.56  ? 67  LYS B CA  1 
ATOM   1269 C C   . LYS B 1 68 ? 8.725   -19.882 -38.167 1.00 33.95  ? 67  LYS B C   1 
ATOM   1270 O O   . LYS B 1 68 ? 7.986   -20.314 -37.280 1.00 34.04  ? 67  LYS B O   1 
ATOM   1271 C CB  . LYS B 1 68 ? 9.604   -21.386 -40.046 1.00 40.08  ? 67  LYS B CB  1 
ATOM   1272 C CG  . LYS B 1 68 ? 9.676   -22.707 -39.292 1.00 49.39  ? 67  LYS B CG  1 
ATOM   1273 C CD  . LYS B 1 68 ? 10.390  -23.680 -40.227 1.00 63.26  ? 67  LYS B CD  1 
ATOM   1274 C CE  . LYS B 1 68 ? 11.071  -24.831 -39.558 1.00 73.67  ? 67  LYS B CE  1 
ATOM   1275 N NZ  . LYS B 1 68 ? 10.126  -25.742 -38.908 1.00 78.17  ? 67  LYS B NZ  1 
ATOM   1276 N N   . TYR B 1 69 ? 9.704   -19.001 -37.909 1.00 31.10  ? 68  TYR B N   1 
ATOM   1277 C CA  . TYR B 1 69 ? 10.058  -18.782 -36.502 1.00 29.71  ? 68  TYR B CA  1 
ATOM   1278 C C   . TYR B 1 69 ? 9.538   -17.441 -35.983 1.00 34.09  ? 68  TYR B C   1 
ATOM   1279 O O   . TYR B 1 69 ? 9.635   -17.157 -34.785 1.00 30.81  ? 68  TYR B O   1 
ATOM   1280 C CB  . TYR B 1 69 ? 11.564  -18.852 -36.246 1.00 29.70  ? 68  TYR B CB  1 
ATOM   1281 C CG  . TYR B 1 69 ? 12.174  -20.218 -36.574 1.00 30.00  ? 68  TYR B CG  1 
ATOM   1282 C CD1 . TYR B 1 69 ? 11.658  -21.392 -36.031 1.00 34.73  ? 68  TYR B CD1 1 
ATOM   1283 C CD2 . TYR B 1 69 ? 13.246  -20.322 -37.455 1.00 34.27  ? 68  TYR B CD2 1 
ATOM   1284 C CE1 . TYR B 1 69 ? 12.212  -22.636 -36.322 1.00 35.70  ? 68  TYR B CE1 1 
ATOM   1285 C CE2 . TYR B 1 69 ? 13.804  -21.549 -37.772 1.00 36.90  ? 68  TYR B CE2 1 
ATOM   1286 C CZ  . TYR B 1 69 ? 13.281  -22.703 -37.203 1.00 37.02  ? 68  TYR B CZ  1 
ATOM   1287 O OH  . TYR B 1 69 ? 13.841  -23.895 -37.505 1.00 34.50  ? 68  TYR B OH  1 
ATOM   1288 N N   . GLY B 1 70 ? 9.024   -16.608 -36.892 1.00 31.40  ? 69  GLY B N   1 
ATOM   1289 C CA  . GLY B 1 70 ? 8.768   -15.223 -36.539 1.00 34.67  ? 69  GLY B CA  1 
ATOM   1290 C C   . GLY B 1 70 ? 7.376   -14.982 -35.957 1.00 38.70  ? 69  GLY B C   1 
ATOM   1291 O O   . GLY B 1 70 ? 6.800   -13.944 -36.219 1.00 37.05  ? 69  GLY B O   1 
ATOM   1292 N N   . LYS B 1 71 ? 6.849   -15.915 -35.162 1.00 40.17  ? 70  LYS B N   1 
ATOM   1293 C CA  . LYS B 1 71 ? 5.477   -15.788 -34.703 1.00 40.99  ? 70  LYS B CA  1 
ATOM   1294 C C   . LYS B 1 71 ? 5.475   -15.408 -33.232 1.00 35.79  ? 70  LYS B C   1 
ATOM   1295 O O   . LYS B 1 71 ? 6.283   -15.921 -32.473 1.00 34.98  ? 70  LYS B O   1 
ATOM   1296 C CB  . LYS B 1 71 ? 4.663   -17.067 -34.915 1.00 45.93  ? 70  LYS B CB  1 
ATOM   1297 C CG  . LYS B 1 71 ? 4.297   -17.157 -36.389 1.00 52.31  ? 70  LYS B CG  1 
ATOM   1298 C CD  . LYS B 1 71 ? 3.857   -18.530 -36.867 1.00 50.96  ? 70  LYS B CD  1 
ATOM   1299 C CE  . LYS B 1 71 ? 3.243   -18.471 -38.235 1.00 55.12  ? 70  LYS B CE  1 
ATOM   1300 N NZ  . LYS B 1 71 ? 4.098   -17.815 -39.235 1.00 61.69  ? 70  LYS B NZ  1 
ATOM   1301 N N   . PRO B 1 72 ? 4.589   -14.492 -32.797 1.00 36.05  ? 71  PRO B N   1 
ATOM   1302 C CA  . PRO B 1 72 ? 4.631   -14.017 -31.410 1.00 36.96  ? 71  PRO B CA  1 
ATOM   1303 C C   . PRO B 1 72 ? 4.385   -15.162 -30.428 1.00 37.69  ? 71  PRO B C   1 
ATOM   1304 O O   . PRO B 1 72 ? 3.754   -16.166 -30.774 1.00 34.93  ? 71  PRO B O   1 
ATOM   1305 C CB  . PRO B 1 72 ? 3.588   -12.882 -31.311 1.00 36.41  ? 71  PRO B CB  1 
ATOM   1306 C CG  . PRO B 1 72 ? 2.784   -13.011 -32.578 1.00 42.23  ? 71  PRO B CG  1 
ATOM   1307 C CD  . PRO B 1 72 ? 3.556   -13.834 -33.617 1.00 38.69  ? 71  PRO B CD  1 
ATOM   1308 N N   . ASN B 1 73 ? 4.914   -15.016 -29.206 1.00 32.92  ? 72  ASN B N   1 
ATOM   1309 C CA  . ASN B 1 73 ? 4.566   -15.956 -28.154 1.00 35.16  ? 72  ASN B CA  1 
ATOM   1310 C C   . ASN B 1 73 ? 4.537   -15.222 -26.807 1.00 35.53  ? 72  ASN B C   1 
ATOM   1311 O O   . ASN B 1 73 ? 4.612   -13.995 -26.748 1.00 35.98  ? 72  ASN B O   1 
ATOM   1312 C CB  . ASN B 1 73 ? 5.475   -17.180 -28.193 1.00 33.81  ? 72  ASN B CB  1 
ATOM   1313 C CG  . ASN B 1 73 ? 6.920   -16.794 -28.020 1.00 34.00  ? 72  ASN B CG  1 
ATOM   1314 O OD1 . ASN B 1 73 ? 7.230   -16.001 -27.127 1.00 34.78  ? 72  ASN B OD1 1 
ATOM   1315 N ND2 . ASN B 1 73 ? 7.807   -17.263 -28.893 1.00 33.86  ? 72  ASN B ND2 1 
ATOM   1316 N N   . LYS B 1 74 ? 4.489   -15.989 -25.720 1.00 37.28  ? 73  LYS B N   1 
ATOM   1317 C CA  . LYS B 1 74 ? 4.282   -15.435 -24.387 1.00 36.81  ? 73  LYS B CA  1 
ATOM   1318 C C   . LYS B 1 74 ? 5.612   -15.354 -23.612 1.00 41.84  ? 73  LYS B C   1 
ATOM   1319 O O   . LYS B 1 74 ? 5.606   -15.089 -22.406 1.00 38.49  ? 73  LYS B O   1 
ATOM   1320 C CB  . LYS B 1 74 ? 3.235   -16.335 -23.693 1.00 36.00  ? 73  LYS B CB  1 
ATOM   1321 N N   . ARG B 1 75 ? 6.757   -15.605 -24.276 1.00 32.46  ? 74  ARG B N   1 
ATOM   1322 C CA  . ARG B 1 75 ? 8.045   -15.466 -23.604 1.00 34.77  ? 74  ARG B CA  1 
ATOM   1323 C C   . ARG B 1 75 ? 8.469   -13.991 -23.510 1.00 33.00  ? 74  ARG B C   1 
ATOM   1324 O O   . ARG B 1 75 ? 8.409   -13.245 -24.489 1.00 37.41  ? 74  ARG B O   1 
ATOM   1325 C CB  . ARG B 1 75 ? 9.177   -16.265 -24.247 1.00 35.26  ? 74  ARG B CB  1 
ATOM   1326 C CG  . ARG B 1 75 ? 8.968   -17.705 -24.693 1.00 37.71  ? 74  ARG B CG  1 
ATOM   1327 C CD  . ARG B 1 75 ? 8.774   -18.587 -23.523 1.00 39.92  ? 74  ARG B CD  1 
ATOM   1328 N NE  . ARG B 1 75 ? 9.036   -19.982 -23.878 1.00 41.12  ? 74  ARG B NE  1 
ATOM   1329 C CZ  . ARG B 1 75 ? 9.901   -20.659 -23.180 1.00 35.65  ? 74  ARG B CZ  1 
ATOM   1330 N NH1 . ARG B 1 75 ? 10.637  -20.029 -22.276 1.00 42.31  ? 74  ARG B NH1 1 
ATOM   1331 N NH2 . ARG B 1 75 ? 10.025  -21.951 -23.381 1.00 43.26  ? 74  ARG B NH2 1 
ATOM   1332 N N   . LYS B 1 76 ? 8.894   -13.574 -22.301 1.00 30.42  ? 75  LYS B N   1 
ATOM   1333 C CA  . LYS B 1 76 ? 9.308   -12.210 -22.006 1.00 29.24  ? 75  LYS B CA  1 
ATOM   1334 C C   . LYS B 1 76 ? 10.410  -11.757 -22.972 1.00 28.29  ? 75  LYS B C   1 
ATOM   1335 O O   . LYS B 1 76 ? 11.488  -12.360 -23.032 1.00 27.37  ? 75  LYS B O   1 
ATOM   1336 C CB  . LYS B 1 76 ? 9.891   -12.167 -20.586 1.00 32.15  ? 75  LYS B CB  1 
ATOM   1337 C CG  . LYS B 1 76 ? 10.304  -10.745 -20.166 1.00 31.86  ? 75  LYS B CG  1 
ATOM   1338 C CD  . LYS B 1 76 ? 10.837  -10.628 -18.751 1.00 37.23  ? 75  LYS B CD  1 
ATOM   1339 C CE  . LYS B 1 76 ? 11.283  -9.207  -18.463 1.00 40.66  ? 75  LYS B CE  1 
ATOM   1340 N NZ  . LYS B 1 76 ? 11.641  -9.038  -17.048 1.00 48.47  ? 75  LYS B NZ  1 
ATOM   1341 N N   . GLY B 1 77 ? 10.132  -10.662 -23.676 1.00 28.74  ? 76  GLY B N   1 
ATOM   1342 C CA  . GLY B 1 77 ? 11.106  -10.034 -24.557 1.00 30.31  ? 76  GLY B CA  1 
ATOM   1343 C C   . GLY B 1 77 ? 10.928  -10.493 -26.007 1.00 30.60  ? 76  GLY B C   1 
ATOM   1344 O O   . GLY B 1 77 ? 11.513  -9.891  -26.907 1.00 28.99  ? 76  GLY B O   1 
ATOM   1345 N N   . PHE B 1 78 ? 10.160  -11.583 -26.251 1.00 27.20  ? 77  PHE B N   1 
ATOM   1346 C CA  . PHE B 1 78 ? 10.086  -12.118 -27.618 1.00 25.85  ? 77  PHE B CA  1 
ATOM   1347 C C   . PHE B 1 78 ? 9.353   -11.185 -28.576 1.00 29.29  ? 77  PHE B C   1 
ATOM   1348 O O   . PHE B 1 78 ? 9.841   -10.908 -29.680 1.00 27.42  ? 77  PHE B O   1 
ATOM   1349 C CB  . PHE B 1 78 ? 9.423   -13.496 -27.621 1.00 28.32  ? 77  PHE B CB  1 
ATOM   1350 C CG  . PHE B 1 78 ? 9.677   -14.257 -28.907 1.00 28.58  ? 77  PHE B CG  1 
ATOM   1351 C CD1 . PHE B 1 78 ? 10.789  -15.087 -29.012 1.00 26.97  ? 77  PHE B CD1 1 
ATOM   1352 C CD2 . PHE B 1 78 ? 8.797   -14.140 -29.972 1.00 30.83  ? 77  PHE B CD2 1 
ATOM   1353 C CE1 . PHE B 1 78 ? 11.043  -15.766 -30.187 1.00 29.31  ? 77  PHE B CE1 1 
ATOM   1354 C CE2 . PHE B 1 78 ? 9.065   -14.819 -31.155 1.00 32.09  ? 77  PHE B CE2 1 
ATOM   1355 C CZ  . PHE B 1 78 ? 10.156  -15.659 -31.234 1.00 27.41  ? 77  PHE B CZ  1 
ATOM   1356 N N   . ASN B 1 79 ? 8.159   -10.716 -28.194 1.00 25.65  ? 78  ASN B N   1 
ATOM   1357 C CA  . ASN B 1 79 ? 7.422   -9.895  -29.144 1.00 29.43  ? 78  ASN B CA  1 
ATOM   1358 C C   . ASN B 1 79 ? 8.140   -8.553  -29.341 1.00 30.01  ? 78  ASN B C   1 
ATOM   1359 O O   . ASN B 1 79 ? 8.096   -7.964  -30.422 1.00 31.93  ? 78  ASN B O   1 
ATOM   1360 C CB  . ASN B 1 79 ? 5.956   -9.765  -28.757 1.00 30.64  ? 78  ASN B CB  1 
ATOM   1361 C CG  . ASN B 1 79 ? 5.250   -11.107 -28.690 1.00 39.46  ? 78  ASN B CG  1 
ATOM   1362 O OD1 . ASN B 1 79 ? 5.752   -12.115 -29.202 1.00 36.50  ? 78  ASN B OD1 1 
ATOM   1363 N ND2 . ASN B 1 79 ? 4.090   -11.156 -28.051 1.00 37.50  ? 78  ASN B ND2 1 
ATOM   1364 N N   . GLU B 1 80 ? 8.797   -8.070  -28.294 1.00 27.44  ? 79  GLU B N   1 
ATOM   1365 C CA  . GLU B 1 80 ? 9.599   -6.863  -28.463 1.00 35.63  ? 79  GLU B CA  1 
ATOM   1366 C C   . GLU B 1 80 ? 10.740  -7.121  -29.448 1.00 30.80  ? 79  GLU B C   1 
ATOM   1367 O O   . GLU B 1 80 ? 11.056  -6.242  -30.249 1.00 33.53  ? 79  GLU B O   1 
ATOM   1368 C CB  . GLU B 1 80 ? 10.188  -6.350  -27.154 1.00 33.87  ? 79  GLU B CB  1 
ATOM   1369 C CG  . GLU B 1 80 ? 9.146   -5.608  -26.326 1.00 40.58  ? 79  GLU B CG  1 
ATOM   1370 N N   . GLY B 1 81 ? 11.363  -8.313  -29.345 1.00 29.57  ? 80  GLY B N   1 
ATOM   1371 C CA  . GLY B 1 81 ? 12.460  -8.712  -30.214 1.00 25.48  ? 80  GLY B CA  1 
ATOM   1372 C C   . GLY B 1 81 ? 11.989  -8.748  -31.663 1.00 27.62  ? 80  GLY B C   1 
ATOM   1373 O O   . GLY B 1 81 ? 12.709  -8.304  -32.571 1.00 29.83  ? 80  GLY B O   1 
ATOM   1374 N N   . LEU B 1 82 ? 10.760  -9.249  -31.856 1.00 25.81  ? 81  LEU B N   1 
ATOM   1375 C CA  . LEU B 1 82 ? 10.160  -9.267  -33.178 1.00 32.69  ? 81  LEU B CA  1 
ATOM   1376 C C   . LEU B 1 82 ? 10.013  -7.835  -33.683 1.00 33.77  ? 81  LEU B C   1 
ATOM   1377 O O   . LEU B 1 82 ? 10.215  -7.585  -34.870 1.00 29.95  ? 81  LEU B O   1 
ATOM   1378 C CB  . LEU B 1 82 ? 8.820   -10.012 -33.229 1.00 28.46  ? 81  LEU B CB  1 
ATOM   1379 C CG  . LEU B 1 82 ? 8.889   -11.520 -32.955 1.00 27.15  ? 81  LEU B CG  1 
ATOM   1380 C CD1 . LEU B 1 82 ? 7.489   -12.126 -32.977 1.00 28.28  ? 81  LEU B CD1 1 
ATOM   1381 C CD2 . LEU B 1 82 ? 9.805   -12.247 -33.937 1.00 26.48  ? 81  LEU B CD2 1 
ATOM   1382 N N   . TRP B 1 83 ? 9.656   -6.903  -32.792 1.00 29.70  ? 82  TRP B N   1 
ATOM   1383 C CA  . TRP B 1 83 ? 9.515   -5.519  -33.223 1.00 29.26  ? 82  TRP B CA  1 
ATOM   1384 C C   . TRP B 1 83 ? 10.872  -4.944  -33.637 1.00 29.27  ? 82  TRP B C   1 
ATOM   1385 O O   . TRP B 1 83 ? 10.946  -4.282  -34.678 1.00 30.01  ? 82  TRP B O   1 
ATOM   1386 C CB  . TRP B 1 83 ? 8.846   -4.639  -32.157 1.00 31.09  ? 82  TRP B CB  1 
ATOM   1387 C CG  . TRP B 1 83 ? 8.561   -3.260  -32.680 1.00 33.68  ? 82  TRP B CG  1 
ATOM   1388 C CD1 . TRP B 1 83 ? 7.424   -2.818  -33.291 1.00 37.39  ? 82  TRP B CD1 1 
ATOM   1389 C CD2 . TRP B 1 83 ? 9.489   -2.153  -32.693 1.00 35.53  ? 82  TRP B CD2 1 
ATOM   1390 N NE1 . TRP B 1 83 ? 7.571   -1.503  -33.648 1.00 39.24  ? 82  TRP B NE1 1 
ATOM   1391 C CE2 . TRP B 1 83 ? 8.827   -1.072  -33.308 1.00 37.80  ? 82  TRP B CE2 1 
ATOM   1392 C CE3 . TRP B 1 83 ? 10.806  -1.978  -32.236 1.00 39.69  ? 82  TRP B CE3 1 
ATOM   1393 C CZ2 . TRP B 1 83 ? 9.444   0.170   -33.477 1.00 39.49  ? 82  TRP B CZ2 1 
ATOM   1394 C CZ3 . TRP B 1 83 ? 11.422  -0.753  -32.413 1.00 40.28  ? 82  TRP B CZ3 1 
ATOM   1395 C CH2 . TRP B 1 83 ? 10.743  0.298   -33.025 1.00 40.71  ? 82  TRP B CH2 1 
ATOM   1396 N N   . GLU B 1 84 ? 11.931  -5.261  -32.869 1.00 27.19  ? 83  GLU B N   1 
ATOM   1397 C CA  . GLU B 1 84 ? 13.257  -4.685  -33.059 1.00 28.60  ? 83  GLU B CA  1 
ATOM   1398 C C   . GLU B 1 84 ? 13.901  -5.199  -34.351 1.00 32.05  ? 83  GLU B C   1 
ATOM   1399 O O   . GLU B 1 84 ? 14.550  -4.430  -35.085 1.00 28.88  ? 83  GLU B O   1 
ATOM   1400 C CB  . GLU B 1 84 ? 14.210  -4.989  -31.913 1.00 26.71  ? 83  GLU B CB  1 
ATOM   1401 C CG  . GLU B 1 84 ? 13.790  -4.266  -30.640 1.00 28.82  ? 83  GLU B CG  1 
ATOM   1402 C CD  . GLU B 1 84 ? 14.624  -4.612  -29.444 1.00 30.53  ? 83  GLU B CD  1 
ATOM   1403 O OE1 . GLU B 1 84 ? 15.571  -5.437  -29.543 1.00 30.80  ? 83  GLU B OE1 1 
ATOM   1404 O OE2 . GLU B 1 84 ? 14.325  -4.017  -28.372 1.00 30.22  ? 83  GLU B OE2 1 
ATOM   1405 N N   . ILE B 1 85 ? 13.719  -6.494  -34.629 1.00 27.24  ? 84  ILE B N   1 
ATOM   1406 C CA  . ILE B 1 85 ? 14.406  -7.063  -35.785 1.00 27.91  ? 84  ILE B CA  1 
ATOM   1407 C C   . ILE B 1 85 ? 13.782  -6.532  -37.075 1.00 28.14  ? 84  ILE B C   1 
ATOM   1408 O O   . ILE B 1 85 ? 14.471  -6.387  -38.090 1.00 26.56  ? 84  ILE B O   1 
ATOM   1409 C CB  . ILE B 1 85 ? 14.442  -8.598  -35.751 1.00 28.79  ? 84  ILE B CB  1 
ATOM   1410 C CG1 . ILE B 1 85 ? 15.533  -9.137  -36.687 1.00 30.74  ? 84  ILE B CG1 1 
ATOM   1411 C CG2 . ILE B 1 85 ? 13.071  -9.211  -36.054 1.00 26.96  ? 84  ILE B CG2 1 
ATOM   1412 C CD1 . ILE B 1 85 ? 15.880  -10.599 -36.445 1.00 29.95  ? 84  ILE B CD1 1 
ATOM   1413 N N   . GLN B 1 86 ? 12.482  -6.223  -37.026 1.00 29.49  ? 85  GLN B N   1 
ATOM   1414 C CA  . GLN B 1 86 ? 11.729  -5.728  -38.173 1.00 33.64  ? 85  GLN B CA  1 
ATOM   1415 C C   . GLN B 1 86 ? 11.891  -4.212  -38.344 1.00 34.45  ? 85  GLN B C   1 
ATOM   1416 O O   . GLN B 1 86 ? 11.990  -3.744  -39.480 1.00 31.90  ? 85  GLN B O   1 
ATOM   1417 C CB  . GLN B 1 86 ? 10.246  -6.106  -38.097 1.00 34.36  ? 85  GLN B CB  1 
ATOM   1418 N N   . ASN B 1 87 ? 11.939  -3.443  -37.241 1.00 29.73  ? 86  ASN B N   1 
ATOM   1419 C CA  . ASN B 1 87 ? 11.809  -1.989  -37.371 1.00 31.12  ? 86  ASN B CA  1 
ATOM   1420 C C   . ASN B 1 87 ? 13.140  -1.252  -37.215 1.00 30.64  ? 86  ASN B C   1 
ATOM   1421 O O   . ASN B 1 87 ? 13.272  -0.130  -37.719 1.00 32.69  ? 86  ASN B O   1 
ATOM   1422 C CB  . ASN B 1 87 ? 10.721  -1.461  -36.429 1.00 36.94  ? 86  ASN B CB  1 
ATOM   1423 C CG  . ASN B 1 87 ? 9.361   -1.965  -36.861 1.00 38.66  ? 86  ASN B CG  1 
ATOM   1424 O OD1 . ASN B 1 87 ? 8.801   -1.438  -37.819 1.00 44.92  ? 86  ASN B OD1 1 
ATOM   1425 N ND2 . ASN B 1 87 ? 8.839   -3.013  -36.232 1.00 37.78  ? 86  ASN B ND2 1 
ATOM   1426 N N   . ASN B 1 88 ? 14.100  -1.834  -36.480 1.00 26.85  ? 87  ASN B N   1 
ATOM   1427 C CA  . ASN B 1 88 ? 15.348  -1.133  -36.208 1.00 30.24  ? 87  ASN B CA  1 
ATOM   1428 C C   . ASN B 1 88 ? 16.440  -2.121  -35.806 1.00 28.91  ? 87  ASN B C   1 
ATOM   1429 O O   . ASN B 1 88 ? 17.019  -2.051  -34.717 1.00 29.48  ? 87  ASN B O   1 
ATOM   1430 C CB  . ASN B 1 88 ? 15.168  0.052   -35.248 1.00 30.65  ? 87  ASN B CB  1 
ATOM   1431 C CG  . ASN B 1 88 ? 16.260  1.095   -35.429 1.00 35.41  ? 87  ASN B CG  1 
ATOM   1432 O OD1 . ASN B 1 88 ? 17.287  0.862   -36.081 1.00 34.77  ? 87  ASN B OD1 1 
ATOM   1433 N ND2 . ASN B 1 88 ? 16.072  2.269   -34.851 1.00 35.22  ? 87  ASN B ND2 1 
ATOM   1434 N N   . PRO B 1 89 ? 16.786  -3.072  -36.701 1.00 30.03  ? 88  PRO B N   1 
ATOM   1435 C CA  . PRO B 1 89 ? 17.703  -4.156  -36.348 1.00 27.35  ? 88  PRO B CA  1 
ATOM   1436 C C   . PRO B 1 89 ? 19.129  -3.716  -36.050 1.00 25.09  ? 88  PRO B C   1 
ATOM   1437 O O   . PRO B 1 89 ? 19.865  -4.426  -35.374 1.00 28.82  ? 88  PRO B O   1 
ATOM   1438 C CB  . PRO B 1 89 ? 17.636  -5.086  -37.595 1.00 23.63  ? 88  PRO B CB  1 
ATOM   1439 C CG  . PRO B 1 89 ? 17.276  -4.158  -38.736 1.00 24.29  ? 88  PRO B CG  1 
ATOM   1440 C CD  . PRO B 1 89 ? 16.307  -3.153  -38.098 1.00 25.94  ? 88  PRO B CD  1 
ATOM   1441 N N   . HIS B 1 90 ? 19.543  -2.543  -36.568 1.00 27.73  ? 89  HIS B N   1 
ATOM   1442 C CA  . HIS B 1 90 ? 20.945  -2.151  -36.486 1.00 25.27  ? 89  HIS B CA  1 
ATOM   1443 C C   . HIS B 1 90 ? 21.163  -1.030  -35.455 1.00 30.78  ? 89  HIS B C   1 
ATOM   1444 O O   . HIS B 1 90 ? 22.254  -0.465  -35.370 1.00 30.79  ? 89  HIS B O   1 
ATOM   1445 C CB  . HIS B 1 90 ? 21.444  -1.731  -37.878 1.00 25.90  ? 89  HIS B CB  1 
ATOM   1446 C CG  . HIS B 1 90 ? 21.233  -2.833  -38.873 1.00 26.01  ? 89  HIS B CG  1 
ATOM   1447 N ND1 . HIS B 1 90 ? 21.748  -4.098  -38.679 1.00 29.21  ? 89  HIS B ND1 1 
ATOM   1448 C CD2 . HIS B 1 90 ? 20.584  -2.862  -40.049 1.00 25.27  ? 89  HIS B CD2 1 
ATOM   1449 C CE1 . HIS B 1 90 ? 21.456  -4.852  -39.740 1.00 27.23  ? 89  HIS B CE1 1 
ATOM   1450 N NE2 . HIS B 1 90 ? 20.785  -4.109  -40.590 1.00 27.57  ? 89  HIS B NE2 1 
ATOM   1451 N N   . ALA B 1 91 ? 20.173  -0.796  -34.596 1.00 29.73  ? 90  ALA B N   1 
ATOM   1452 C CA  . ALA B 1 91 ? 20.256  0.268   -33.600 1.00 30.85  ? 90  ALA B CA  1 
ATOM   1453 C C   . ALA B 1 91 ? 21.214  -0.097  -32.469 1.00 33.52  ? 90  ALA B C   1 
ATOM   1454 O O   . ALA B 1 91 ? 21.543  -1.261  -32.241 1.00 30.43  ? 90  ALA B O   1 
ATOM   1455 C CB  . ALA B 1 91 ? 18.855  0.598   -33.061 1.00 28.19  ? 90  ALA B CB  1 
ATOM   1456 N N   . SER B 1 92 ? 21.636  0.928   -31.718 1.00 33.64  ? 91  SER B N   1 
ATOM   1457 C CA  . SER B 1 92 ? 22.327  0.721   -30.452 1.00 36.06  ? 91  SER B CA  1 
ATOM   1458 C C   . SER B 1 92 ? 21.276  0.442   -29.366 1.00 39.17  ? 91  SER B C   1 
ATOM   1459 O O   . SER B 1 92 ? 20.316  1.203   -29.236 1.00 39.59  ? 91  SER B O   1 
ATOM   1460 C CB  . SER B 1 92 ? 23.128  1.967   -30.131 1.00 33.09  ? 91  SER B CB  1 
ATOM   1461 O OG  . SER B 1 92 ? 23.735  1.804   -28.865 1.00 46.66  ? 91  SER B OG  1 
ATOM   1462 N N   . TYR B 1 93 ? 21.426  -0.674  -28.633 1.00 39.97  ? 92  TYR B N   1 
ATOM   1463 C CA  . TYR B 1 93 ? 20.490  -1.082  -27.593 1.00 41.22  ? 92  TYR B CA  1 
ATOM   1464 C C   . TYR B 1 93 ? 21.222  -1.098  -26.251 1.00 45.43  ? 92  TYR B C   1 
ATOM   1465 O O   . TYR B 1 93 ? 20.711  -1.616  -25.267 1.00 49.94  ? 92  TYR B O   1 
ATOM   1466 C CB  . TYR B 1 93 ? 19.814  -2.430  -27.905 1.00 34.90  ? 92  TYR B CB  1 
ATOM   1467 C CG  . TYR B 1 93 ? 18.815  -2.339  -29.049 1.00 30.50  ? 92  TYR B CG  1 
ATOM   1468 C CD1 . TYR B 1 93 ? 17.539  -1.837  -28.838 1.00 30.84  ? 92  TYR B CD1 1 
ATOM   1469 C CD2 . TYR B 1 93 ? 19.132  -2.786  -30.337 1.00 27.80  ? 92  TYR B CD2 1 
ATOM   1470 C CE1 . TYR B 1 93 ? 16.640  -1.699  -29.884 1.00 31.33  ? 92  TYR B CE1 1 
ATOM   1471 C CE2 . TYR B 1 93 ? 18.219  -2.688  -31.379 1.00 27.24  ? 92  TYR B CE2 1 
ATOM   1472 C CZ  . TYR B 1 93 ? 16.968  -2.150  -31.155 1.00 30.35  ? 92  TYR B CZ  1 
ATOM   1473 O OH  . TYR B 1 93 ? 16.042  -2.060  -32.168 1.00 31.15  ? 92  TYR B OH  1 
ATOM   1474 N N   . SER B 1 94 ? 22.392  -0.449  -26.219 1.00 61.62  ? 93  SER B N   1 
ATOM   1475 C CA  . SER B 1 94 ? 23.332  -0.503  -25.110 1.00 67.28  ? 93  SER B CA  1 
ATOM   1476 C C   . SER B 1 94 ? 22.815  0.324   -23.920 1.00 78.92  ? 93  SER B C   1 
ATOM   1477 O O   . SER B 1 94 ? 21.721  0.927   -24.056 1.00 78.00  ? 93  SER B O   1 
ATOM   1478 C CB  . SER B 1 94 ? 24.683  -0.001  -25.537 1.00 69.54  ? 93  SER B CB  1 
ATOM   1479 O OG  . SER B 1 94 ? 24.890  -0.150  -26.934 1.00 78.24  ? 93  SER B OG  1 
ATOM   1480 O OXT . SER B 1 94 ? 23.538  0.354   -22.892 1.00 83.94  ? 93  SER B OXT 1 
ATOM   1481 N N   . HIS C 1 4  ? 33.100  -23.452 26.890  1.00 83.59  ? 3   HIS C N   1 
ATOM   1482 C CA  . HIS C 1 4  ? 31.863  -22.650 27.104  1.00 88.39  ? 3   HIS C CA  1 
ATOM   1483 C C   . HIS C 1 4  ? 31.221  -23.081 28.427  1.00 88.54  ? 3   HIS C C   1 
ATOM   1484 O O   . HIS C 1 4  ? 31.864  -23.762 29.228  1.00 88.98  ? 3   HIS C O   1 
ATOM   1485 C CB  . HIS C 1 4  ? 30.972  -22.733 25.853  1.00 92.09  ? 3   HIS C CB  1 
ATOM   1486 C CG  . HIS C 1 4  ? 30.065  -21.555 25.663  1.00 95.41  ? 3   HIS C CG  1 
ATOM   1487 N ND1 . HIS C 1 4  ? 28.750  -21.529 26.076  1.00 92.73  ? 3   HIS C ND1 1 
ATOM   1488 C CD2 . HIS C 1 4  ? 30.300  -20.353 25.113  1.00 92.57  ? 3   HIS C CD2 1 
ATOM   1489 C CE1 . HIS C 1 4  ? 28.217  -20.351 25.781  1.00 91.91  ? 3   HIS C CE1 1 
ATOM   1490 N NE2 . HIS C 1 4  ? 29.144  -19.619 25.200  1.00 87.89  ? 3   HIS C NE2 1 
ATOM   1491 N N   . ALA C 1 5  ? 29.964  -22.657 28.651  1.00 83.10  ? 4   ALA C N   1 
ATOM   1492 C CA  . ALA C 1 5  ? 29.129  -23.118 29.753  1.00 77.03  ? 4   ALA C CA  1 
ATOM   1493 C C   . ALA C 1 5  ? 27.651  -22.869 29.457  1.00 79.63  ? 4   ALA C C   1 
ATOM   1494 O O   . ALA C 1 5  ? 27.303  -21.884 28.802  1.00 82.81  ? 4   ALA C O   1 
ATOM   1495 C CB  . ALA C 1 5  ? 29.526  -22.417 31.017  1.00 82.86  ? 4   ALA C CB  1 
ATOM   1496 N N   . PHE C 1 6  ? 26.785  -23.742 29.994  1.00 65.27  ? 5   PHE C N   1 
ATOM   1497 C CA  . PHE C 1 6  ? 25.382  -23.755 29.613  1.00 59.13  ? 5   PHE C CA  1 
ATOM   1498 C C   . PHE C 1 6  ? 24.511  -23.853 30.857  1.00 64.74  ? 5   PHE C C   1 
ATOM   1499 O O   . PHE C 1 6  ? 24.836  -24.613 31.763  1.00 75.34  ? 5   PHE C O   1 
ATOM   1500 C CB  . PHE C 1 6  ? 25.128  -24.986 28.733  1.00 50.22  ? 5   PHE C CB  1 
ATOM   1501 C CG  . PHE C 1 6  ? 25.892  -25.002 27.417  1.00 44.58  ? 5   PHE C CG  1 
ATOM   1502 C CD1 . PHE C 1 6  ? 26.963  -25.862 27.219  1.00 45.47  ? 5   PHE C CD1 1 
ATOM   1503 C CD2 . PHE C 1 6  ? 25.566  -24.120 26.389  1.00 52.69  ? 5   PHE C CD2 1 
ATOM   1504 C CE1 . PHE C 1 6  ? 27.656  -25.862 26.010  1.00 50.65  ? 5   PHE C CE1 1 
ATOM   1505 C CE2 . PHE C 1 6  ? 26.258  -24.129 25.181  1.00 46.37  ? 5   PHE C CE2 1 
ATOM   1506 C CZ  . PHE C 1 6  ? 27.296  -24.998 24.993  1.00 48.70  ? 5   PHE C CZ  1 
ATOM   1507 N N   . LYS C 1 7  ? 23.398  -23.107 30.873  1.00 57.32  ? 6   LYS C N   1 
ATOM   1508 C CA  . LYS C 1 7  ? 22.432  -23.153 31.965  1.00 55.41  ? 6   LYS C CA  1 
ATOM   1509 C C   . LYS C 1 7  ? 21.079  -23.537 31.378  1.00 51.45  ? 6   LYS C C   1 
ATOM   1510 O O   . LYS C 1 7  ? 20.881  -23.434 30.167  1.00 54.04  ? 6   LYS C O   1 
ATOM   1511 C CB  . LYS C 1 7  ? 22.363  -21.813 32.713  1.00 57.18  ? 6   LYS C CB  1 
ATOM   1512 N N   . PRO C 1 8  ? 20.082  -23.978 32.180  1.00 53.52  ? 7   PRO C N   1 
ATOM   1513 C CA  . PRO C 1 8  ? 18.798  -24.392 31.606  1.00 52.35  ? 7   PRO C CA  1 
ATOM   1514 C C   . PRO C 1 8  ? 18.199  -23.233 30.805  1.00 61.53  ? 7   PRO C C   1 
ATOM   1515 O O   . PRO C 1 8  ? 18.375  -22.075 31.180  1.00 68.80  ? 7   PRO C O   1 
ATOM   1516 C CB  . PRO C 1 8  ? 17.976  -24.784 32.843  1.00 56.23  ? 7   PRO C CB  1 
ATOM   1517 C CG  . PRO C 1 8  ? 19.025  -25.127 33.885  1.00 52.21  ? 7   PRO C CG  1 
ATOM   1518 C CD  . PRO C 1 8  ? 20.126  -24.100 33.649  1.00 55.49  ? 7   PRO C CD  1 
ATOM   1519 N N   . GLY C 1 9  ? 17.550  -23.537 29.671  1.00 57.69  ? 8   GLY C N   1 
ATOM   1520 C CA  . GLY C 1 9  ? 16.906  -22.511 28.862  1.00 53.05  ? 8   GLY C CA  1 
ATOM   1521 C C   . GLY C 1 9  ? 17.763  -22.031 27.685  1.00 50.01  ? 8   GLY C C   1 
ATOM   1522 O O   . GLY C 1 9  ? 17.214  -21.514 26.715  1.00 52.80  ? 8   GLY C O   1 
ATOM   1523 N N   . ASP C 1 10 ? 19.093  -22.193 27.777  1.00 45.08  ? 9   ASP C N   1 
ATOM   1524 C CA  . ASP C 1 10 ? 20.039  -21.828 26.735  1.00 39.35  ? 9   ASP C CA  1 
ATOM   1525 C C   . ASP C 1 10 ? 19.753  -22.566 25.425  1.00 41.88  ? 9   ASP C C   1 
ATOM   1526 O O   . ASP C 1 10 ? 19.454  -23.748 25.415  1.00 37.74  ? 9   ASP C O   1 
ATOM   1527 C CB  . ASP C 1 10 ? 21.468  -22.130 27.143  1.00 41.44  ? 9   ASP C CB  1 
ATOM   1528 C CG  . ASP C 1 10 ? 22.102  -21.133 28.109  1.00 52.56  ? 9   ASP C CG  1 
ATOM   1529 O OD1 . ASP C 1 10 ? 21.417  -20.133 28.453  1.00 53.53  ? 9   ASP C OD1 1 
ATOM   1530 O OD2 . ASP C 1 10 ? 23.272  -21.368 28.525  1.00 52.13  ? 9   ASP C OD2 1 
ATOM   1531 N N   . LEU C 1 11 ? 19.877  -21.852 24.305  1.00 40.87  ? 10  LEU C N   1 
ATOM   1532 C CA  . LEU C 1 11 ? 19.500  -22.385 23.006  1.00 37.38  ? 10  LEU C CA  1 
ATOM   1533 C C   . LEU C 1 11 ? 20.759  -22.845 22.286  1.00 36.06  ? 10  LEU C C   1 
ATOM   1534 O O   . LEU C 1 11 ? 21.751  -22.123 22.258  1.00 34.17  ? 10  LEU C O   1 
ATOM   1535 C CB  . LEU C 1 11 ? 18.760  -21.317 22.193  1.00 38.72  ? 10  LEU C CB  1 
ATOM   1536 C CG  . LEU C 1 11 ? 17.437  -20.802 22.766  1.00 35.27  ? 10  LEU C CG  1 
ATOM   1537 C CD1 . LEU C 1 11 ? 16.808  -19.798 21.803  1.00 37.20  ? 10  LEU C CD1 1 
ATOM   1538 C CD2 . LEU C 1 11 ? 16.424  -21.893 23.116  1.00 36.74  ? 10  LEU C CD2 1 
ATOM   1539 N N   . VAL C 1 12 ? 20.700  -24.048 21.688  1.00 33.44  ? 11  VAL C N   1 
ATOM   1540 C CA  . VAL C 1 12 ? 21.886  -24.653 21.111  1.00 30.44  ? 11  VAL C CA  1 
ATOM   1541 C C   . VAL C 1 12 ? 21.494  -25.415 19.832  1.00 29.86  ? 11  VAL C C   1 
ATOM   1542 O O   . VAL C 1 12 ? 20.312  -25.601 19.535  1.00 30.12  ? 11  VAL C O   1 
ATOM   1543 C CB  . VAL C 1 12 ? 22.481  -25.619 22.161  1.00 29.32  ? 11  VAL C CB  1 
ATOM   1544 C CG1 . VAL C 1 12 ? 22.844  -24.935 23.491  1.00 28.96  ? 11  VAL C CG1 1 
ATOM   1545 C CG2 . VAL C 1 12 ? 21.572  -26.817 22.431  1.00 25.72  ? 11  VAL C CG2 1 
ATOM   1546 N N   . PHE C 1 13 ? 22.500  -25.812 19.045  1.00 29.81  ? 12  PHE C N   1 
ATOM   1547 C CA  . PHE C 1 13 ? 22.385  -26.991 18.203  1.00 27.16  ? 12  PHE C CA  1 
ATOM   1548 C C   . PHE C 1 13 ? 23.077  -28.147 18.925  1.00 29.38  ? 12  PHE C C   1 
ATOM   1549 O O   . PHE C 1 13 ? 24.172  -27.990 19.479  1.00 33.45  ? 12  PHE C O   1 
ATOM   1550 C CB  . PHE C 1 13 ? 22.965  -26.799 16.795  1.00 28.78  ? 12  PHE C CB  1 
ATOM   1551 C CG  . PHE C 1 13 ? 22.199  -25.784 15.975  1.00 31.69  ? 12  PHE C CG  1 
ATOM   1552 C CD1 . PHE C 1 13 ? 21.147  -26.195 15.155  1.00 31.84  ? 12  PHE C CD1 1 
ATOM   1553 C CD2 . PHE C 1 13 ? 22.495  -24.422 16.063  1.00 31.55  ? 12  PHE C CD2 1 
ATOM   1554 C CE1 . PHE C 1 13 ? 20.411  -25.262 14.430  1.00 33.11  ? 12  PHE C CE1 1 
ATOM   1555 C CE2 . PHE C 1 13 ? 21.743  -23.496 15.347  1.00 36.47  ? 12  PHE C CE2 1 
ATOM   1556 C CZ  . PHE C 1 13 ? 20.718  -23.919 14.523  1.00 36.54  ? 12  PHE C CZ  1 
ATOM   1557 N N   . ALA C 1 14 ? 22.407  -29.304 18.940  1.00 30.32  ? 13  ALA C N   1 
ATOM   1558 C CA  . ALA C 1 14 ? 22.873  -30.466 19.679  1.00 29.58  ? 13  ALA C CA  1 
ATOM   1559 C C   . ALA C 1 14 ? 23.148  -31.588 18.685  1.00 31.24  ? 13  ALA C C   1 
ATOM   1560 O O   . ALA C 1 14 ? 22.281  -31.903 17.871  1.00 27.25  ? 13  ALA C O   1 
ATOM   1561 C CB  . ALA C 1 14 ? 21.819  -30.879 20.678  1.00 29.87  ? 13  ALA C CB  1 
ATOM   1562 N N   . LYS C 1 15 ? 24.341  -32.189 18.773  1.00 30.25  ? 14  LYS C N   1 
ATOM   1563 C CA  . LYS C 1 15 ? 24.745  -33.206 17.812  1.00 30.62  ? 14  LYS C CA  1 
ATOM   1564 C C   . LYS C 1 15 ? 24.709  -34.573 18.482  1.00 32.67  ? 14  LYS C C   1 
ATOM   1565 O O   . LYS C 1 15 ? 25.397  -34.792 19.469  1.00 31.62  ? 14  LYS C O   1 
ATOM   1566 C CB  . LYS C 1 15 ? 26.173  -32.975 17.298  1.00 34.41  ? 14  LYS C CB  1 
ATOM   1567 C CG  . LYS C 1 15 ? 26.635  -34.001 16.232  1.00 34.75  ? 14  LYS C CG  1 
ATOM   1568 C CD  . LYS C 1 15 ? 25.768  -33.938 14.972  1.00 30.68  ? 14  LYS C CD  1 
ATOM   1569 C CE  . LYS C 1 15 ? 26.299  -34.764 13.779  1.00 31.26  ? 14  LYS C CE  1 
ATOM   1570 N NZ  . LYS C 1 15 ? 26.123  -36.196 14.056  1.00 30.13  ? 14  LYS C NZ  1 
ATOM   1571 N N   . MET C 1 16 ? 23.914  -35.481 17.911  1.00 30.36  ? 15  MET C N   1 
ATOM   1572 C CA  . MET C 1 16 ? 23.848  -36.874 18.324  1.00 33.86  ? 15  MET C CA  1 
ATOM   1573 C C   . MET C 1 16 ? 24.300  -37.742 17.158  1.00 37.02  ? 15  MET C C   1 
ATOM   1574 O O   . MET C 1 16 ? 24.159  -37.357 15.985  1.00 30.09  ? 15  MET C O   1 
ATOM   1575 C CB  . MET C 1 16 ? 22.410  -37.298 18.620  1.00 31.76  ? 15  MET C CB  1 
ATOM   1576 C CG  . MET C 1 16 ? 21.866  -36.728 19.923  1.00 41.43  ? 15  MET C CG  1 
ATOM   1577 S SD  . MET C 1 16 ? 20.397  -37.627 20.460  1.00 53.07  ? 15  MET C SD  1 
ATOM   1578 C CE  . MET C 1 16 ? 21.299  -38.976 21.246  1.00 55.17  ? 15  MET C CE  1 
ATOM   1579 N N   . LYS C 1 17 ? 24.802  -38.937 17.490  1.00 36.94  ? 16  LYS C N   1 
ATOM   1580 C CA  . LYS C 1 17 ? 25.285  -39.814 16.430  1.00 42.73  ? 16  LYS C CA  1 
ATOM   1581 C C   . LYS C 1 17 ? 24.079  -40.226 15.594  1.00 33.88  ? 16  LYS C C   1 
ATOM   1582 O O   . LYS C 1 17 ? 23.090  -40.728 16.138  1.00 33.33  ? 16  LYS C O   1 
ATOM   1583 C CB  . LYS C 1 17 ? 25.977  -41.050 17.033  1.00 42.01  ? 16  LYS C CB  1 
ATOM   1584 C CG  . LYS C 1 17 ? 26.642  -41.994 16.035  1.00 45.65  ? 16  LYS C CG  1 
ATOM   1585 C CD  . LYS C 1 17 ? 27.810  -41.294 15.347  1.00 46.93  ? 16  LYS C CD  1 
ATOM   1586 C CE  . LYS C 1 17 ? 28.449  -42.124 14.281  1.00 57.10  ? 16  LYS C CE  1 
ATOM   1587 N NZ  . LYS C 1 17 ? 29.671  -41.471 13.811  1.00 50.15  ? 16  LYS C NZ  1 
ATOM   1588 N N   . GLY C 1 18 ? 24.193  -40.049 14.276  1.00 34.56  ? 17  GLY C N   1 
ATOM   1589 C CA  . GLY C 1 18 ? 23.152  -40.527 13.381  1.00 33.92  ? 17  GLY C CA  1 
ATOM   1590 C C   . GLY C 1 18 ? 22.121  -39.452 13.008  1.00 36.96  ? 17  GLY C C   1 
ATOM   1591 O O   . GLY C 1 18 ? 21.078  -39.773 12.436  1.00 33.61  ? 17  GLY C O   1 
ATOM   1592 N N   . TYR C 1 19 ? 22.409  -38.184 13.347  1.00 35.80  ? 18  TYR C N   1 
ATOM   1593 C CA  . TYR C 1 19 ? 21.451  -37.085 13.184  1.00 31.56  ? 18  TYR C CA  1 
ATOM   1594 C C   . TYR C 1 19 ? 22.242  -35.830 12.873  1.00 29.47  ? 18  TYR C C   1 
ATOM   1595 O O   . TYR C 1 19 ? 23.320  -35.629 13.419  1.00 31.84  ? 18  TYR C O   1 
ATOM   1596 C CB  . TYR C 1 19 ? 20.707  -36.765 14.488  1.00 28.45  ? 18  TYR C CB  1 
ATOM   1597 C CG  . TYR C 1 19 ? 19.844  -37.925 14.922  1.00 32.02  ? 18  TYR C CG  1 
ATOM   1598 C CD1 . TYR C 1 19 ? 20.379  -38.968 15.679  1.00 32.72  ? 18  TYR C CD1 1 
ATOM   1599 C CD2 . TYR C 1 19 ? 18.518  -38.003 14.525  1.00 31.39  ? 18  TYR C CD2 1 
ATOM   1600 C CE1 . TYR C 1 19 ? 19.603  -40.052 16.046  1.00 36.41  ? 18  TYR C CE1 1 
ATOM   1601 C CE2 . TYR C 1 19 ? 17.732  -39.087 14.893  1.00 41.03  ? 18  TYR C CE2 1 
ATOM   1602 C CZ  . TYR C 1 19 ? 18.282  -40.110 15.646  1.00 39.56  ? 18  TYR C CZ  1 
ATOM   1603 O OH  . TYR C 1 19 ? 17.520  -41.176 16.022  1.00 46.15  ? 18  TYR C OH  1 
ATOM   1604 N N   . PRO C 1 20 ? 21.707  -34.908 12.046  1.00 32.82  ? 19  PRO C N   1 
ATOM   1605 C CA  . PRO C 1 20 ? 22.357  -33.612 11.857  1.00 29.16  ? 19  PRO C CA  1 
ATOM   1606 C C   . PRO C 1 20 ? 22.344  -32.797 13.158  1.00 25.17  ? 19  PRO C C   1 
ATOM   1607 O O   . PRO C 1 20 ? 21.621  -33.114 14.107  1.00 28.29  ? 19  PRO C O   1 
ATOM   1608 C CB  . PRO C 1 20 ? 21.478  -32.963 10.759  1.00 31.49  ? 19  PRO C CB  1 
ATOM   1609 C CG  . PRO C 1 20 ? 20.107  -33.564 10.999  1.00 29.42  ? 19  PRO C CG  1 
ATOM   1610 C CD  . PRO C 1 20 ? 20.393  -35.015 11.378  1.00 28.78  ? 19  PRO C CD  1 
ATOM   1611 N N   . HIS C 1 21 ? 23.177  -31.758 13.194  1.00 27.93  ? 20  HIS C N   1 
ATOM   1612 C CA  . HIS C 1 21 ? 23.123  -30.817 14.311  1.00 29.80  ? 20  HIS C CA  1 
ATOM   1613 C C   . HIS C 1 21 ? 21.697  -30.271 14.443  1.00 28.49  ? 20  HIS C C   1 
ATOM   1614 O O   . HIS C 1 21 ? 21.112  -29.790 13.464  1.00 31.32  ? 20  HIS C O   1 
ATOM   1615 C CB  . HIS C 1 21 ? 24.117  -29.668 14.109  1.00 28.11  ? 20  HIS C CB  1 
ATOM   1616 C CG  . HIS C 1 21 ? 25.532  -30.143 14.091  1.00 33.70  ? 20  HIS C CG  1 
ATOM   1617 N ND1 . HIS C 1 21 ? 26.132  -30.798 13.034  1.00 36.03  ? 20  HIS C ND1 1 
ATOM   1618 C CD2 . HIS C 1 21 ? 26.452  -30.079 15.079  1.00 36.52  ? 20  HIS C CD2 1 
ATOM   1619 C CE1 . HIS C 1 21 ? 27.380  -31.099 13.368  1.00 39.17  ? 20  HIS C CE1 1 
ATOM   1620 N NE2 . HIS C 1 21 ? 27.598  -30.650 14.602  1.00 35.59  ? 20  HIS C NE2 1 
ATOM   1621 N N   . TRP C 1 22 ? 21.140  -30.345 15.659  1.00 27.01  ? 21  TRP C N   1 
ATOM   1622 C CA  . TRP C 1 22 ? 19.693  -30.263 15.790  1.00 25.67  ? 21  TRP C CA  1 
ATOM   1623 C C   . TRP C 1 22 ? 19.321  -29.107 16.719  1.00 26.00  ? 21  TRP C C   1 
ATOM   1624 O O   . TRP C 1 22 ? 19.919  -28.980 17.790  1.00 25.46  ? 21  TRP C O   1 
ATOM   1625 C CB  . TRP C 1 22 ? 19.131  -31.582 16.348  1.00 28.92  ? 21  TRP C CB  1 
ATOM   1626 C CG  . TRP C 1 22 ? 17.672  -31.800 16.006  1.00 32.54  ? 21  TRP C CG  1 
ATOM   1627 C CD1 . TRP C 1 22 ? 16.575  -31.214 16.582  1.00 30.81  ? 21  TRP C CD1 1 
ATOM   1628 C CD2 . TRP C 1 22 ? 17.158  -32.705 14.989  1.00 30.59  ? 21  TRP C CD2 1 
ATOM   1629 N NE1 . TRP C 1 22 ? 15.423  -31.673 15.992  1.00 30.86  ? 21  TRP C NE1 1 
ATOM   1630 C CE2 . TRP C 1 22 ? 15.749  -32.587 15.019  1.00 29.41  ? 21  TRP C CE2 1 
ATOM   1631 C CE3 . TRP C 1 22 ? 17.742  -33.591 14.064  1.00 29.16  ? 21  TRP C CE3 1 
ATOM   1632 C CZ2 . TRP C 1 22 ? 14.938  -33.315 14.145  1.00 28.05  ? 21  TRP C CZ2 1 
ATOM   1633 C CZ3 . TRP C 1 22 ? 16.930  -34.320 13.212  1.00 28.59  ? 21  TRP C CZ3 1 
ATOM   1634 C CH2 . TRP C 1 22 ? 15.545  -34.204 13.281  1.00 26.51  ? 21  TRP C CH2 1 
ATOM   1635 N N   . PRO C 1 23 ? 18.301  -28.274 16.380  1.00 26.41  ? 22  PRO C N   1 
ATOM   1636 C CA  . PRO C 1 23 ? 17.919  -27.160 17.240  1.00 25.78  ? 22  PRO C CA  1 
ATOM   1637 C C   . PRO C 1 23 ? 17.348  -27.704 18.542  1.00 26.08  ? 22  PRO C C   1 
ATOM   1638 O O   . PRO C 1 23 ? 16.501  -28.603 18.528  1.00 27.58  ? 22  PRO C O   1 
ATOM   1639 C CB  . PRO C 1 23 ? 16.880  -26.386 16.389  1.00 28.66  ? 22  PRO C CB  1 
ATOM   1640 C CG  . PRO C 1 23 ? 16.315  -27.435 15.453  1.00 25.17  ? 22  PRO C CG  1 
ATOM   1641 C CD  . PRO C 1 23 ? 17.548  -28.274 15.109  1.00 26.67  ? 22  PRO C CD  1 
ATOM   1642 N N   . ALA C 1 24 ? 17.819  -27.143 19.652  1.00 26.28  ? 23  ALA C N   1 
ATOM   1643 C CA  . ALA C 1 24 ? 17.543  -27.730 20.952  1.00 27.61  ? 23  ALA C CA  1 
ATOM   1644 C C   . ALA C 1 24 ? 17.719  -26.669 22.036  1.00 29.64  ? 23  ALA C C   1 
ATOM   1645 O O   . ALA C 1 24 ? 18.221  -25.584 21.768  1.00 29.80  ? 23  ALA C O   1 
ATOM   1646 C CB  . ALA C 1 24 ? 18.505  -28.904 21.163  1.00 25.63  ? 23  ALA C CB  1 
ATOM   1647 N N   . ARG C 1 25 ? 17.364  -27.017 23.279  1.00 31.63  ? 24  ARG C N   1 
ATOM   1648 C CA  . ARG C 1 25 ? 17.742  -26.167 24.398  1.00 33.04  ? 24  ARG C CA  1 
ATOM   1649 C C   . ARG C 1 25 ? 18.192  -27.026 25.584  1.00 33.29  ? 24  ARG C C   1 
ATOM   1650 O O   . ARG C 1 25 ? 17.842  -28.203 25.671  1.00 33.97  ? 24  ARG C O   1 
ATOM   1651 C CB  . ARG C 1 25 ? 16.516  -25.359 24.843  1.00 35.78  ? 24  ARG C CB  1 
ATOM   1652 C CG  . ARG C 1 25 ? 15.262  -26.137 25.203  1.00 40.78  ? 24  ARG C CG  1 
ATOM   1653 C CD  . ARG C 1 25 ? 14.230  -25.256 25.907  1.00 42.98  ? 24  ARG C CD  1 
ATOM   1654 N NE  . ARG C 1 25 ? 13.040  -26.061 26.219  1.00 44.46  ? 24  ARG C NE  1 
ATOM   1655 C CZ  . ARG C 1 25 ? 11.762  -25.772 25.998  1.00 48.75  ? 24  ARG C CZ  1 
ATOM   1656 N NH1 . ARG C 1 25 ? 11.412  -24.637 25.415  1.00 45.07  ? 24  ARG C NH1 1 
ATOM   1657 N NH2 . ARG C 1 25 ? 10.826  -26.630 26.371  1.00 52.23  ? 24  ARG C NH2 1 
ATOM   1658 N N   . ILE C 1 26 ? 18.898  -26.393 26.519  1.00 34.57  ? 25  ILE C N   1 
ATOM   1659 C CA  . ILE C 1 26 ? 19.277  -26.998 27.790  1.00 39.84  ? 25  ILE C CA  1 
ATOM   1660 C C   . ILE C 1 26 ? 18.044  -27.001 28.688  1.00 47.89  ? 25  ILE C C   1 
ATOM   1661 O O   . ILE C 1 26 ? 17.395  -25.966 28.889  1.00 46.13  ? 25  ILE C O   1 
ATOM   1662 C CB  . ILE C 1 26 ? 20.443  -26.235 28.447  1.00 39.71  ? 25  ILE C CB  1 
ATOM   1663 C CG1 . ILE C 1 26 ? 21.557  -25.873 27.488  1.00 42.55  ? 25  ILE C CG1 1 
ATOM   1664 C CG2 . ILE C 1 26 ? 20.979  -26.960 29.681  1.00 41.26  ? 25  ILE C CG2 1 
ATOM   1665 C CD1 . ILE C 1 26 ? 22.476  -27.006 27.076  1.00 39.93  ? 25  ILE C CD1 1 
ATOM   1666 N N   . ASP C 1 27 ? 17.714  -28.183 29.205  1.00 46.86  ? 26  ASP C N   1 
ATOM   1667 C CA  . ASP C 1 27 ? 16.669  -28.316 30.206  1.00 55.53  ? 26  ASP C CA  1 
ATOM   1668 C C   . ASP C 1 27 ? 17.254  -28.146 31.601  1.00 56.41  ? 26  ASP C C   1 
ATOM   1669 O O   . ASP C 1 27 ? 18.470  -28.160 31.756  1.00 64.29  ? 26  ASP C O   1 
ATOM   1670 C CB  . ASP C 1 27 ? 16.006  -29.680 30.135  1.00 57.18  ? 26  ASP C CB  1 
ATOM   1671 C CG  . ASP C 1 27 ? 14.730  -29.726 29.316  1.00 63.95  ? 26  ASP C CG  1 
ATOM   1672 O OD1 . ASP C 1 27 ? 14.435  -28.694 28.666  1.00 59.89  ? 26  ASP C OD1 1 
ATOM   1673 O OD2 . ASP C 1 27 ? 14.031  -30.774 29.376  1.00 61.10  ? 26  ASP C OD2 1 
ATOM   1674 N N   . ASP C 1 28 ? 16.374  -27.988 32.602  1.00 71.10  ? 27  ASP C N   1 
ATOM   1675 C CA  . ASP C 1 28 ? 16.742  -28.177 33.999  1.00 67.51  ? 27  ASP C CA  1 
ATOM   1676 C C   . ASP C 1 28 ? 16.620  -29.666 34.306  1.00 66.14  ? 27  ASP C C   1 
ATOM   1677 O O   . ASP C 1 28 ? 16.074  -30.403 33.494  1.00 66.45  ? 27  ASP C O   1 
ATOM   1678 C CB  . ASP C 1 28 ? 15.950  -27.278 34.937  1.00 68.69  ? 27  ASP C CB  1 
ATOM   1679 N N   . ILE C 1 29 ? 17.182  -30.096 35.445  1.00 63.93  ? 28  ILE C N   1 
ATOM   1680 C CA  . ILE C 1 29 ? 17.018  -31.451 35.950  1.00 68.80  ? 28  ILE C CA  1 
ATOM   1681 C C   . ILE C 1 29 ? 16.346  -31.353 37.317  1.00 74.36  ? 28  ILE C C   1 
ATOM   1682 O O   . ILE C 1 29 ? 16.867  -30.679 38.203  1.00 82.69  ? 28  ILE C O   1 
ATOM   1683 C CB  . ILE C 1 29 ? 18.378  -32.171 36.039  1.00 68.78  ? 28  ILE C CB  1 
ATOM   1684 N N   . ALA C 1 30 ? 15.194  -32.021 37.478  1.00 69.82  ? 29  ALA C N   1 
ATOM   1685 C CA  . ALA C 1 30 ? 14.380  -31.916 38.685  1.00 68.44  ? 29  ALA C CA  1 
ATOM   1686 C C   . ALA C 1 30 ? 15.090  -32.522 39.906  1.00 62.47  ? 29  ALA C C   1 
ATOM   1687 O O   . ALA C 1 30 ? 15.602  -33.677 39.800  1.00 51.60  ? 29  ALA C O   1 
ATOM   1688 C CB  . ALA C 1 30 ? 13.014  -32.532 38.445  1.00 65.46  ? 29  ALA C CB  1 
ATOM   1689 N N   . ALA C 1 33 ? 14.697  -36.608 40.744  1.00 66.12  ? 32  ALA C N   1 
ATOM   1690 C CA  . ALA C 1 33 ? 14.772  -37.272 39.419  1.00 64.22  ? 32  ALA C CA  1 
ATOM   1691 C C   . ALA C 1 33 ? 16.145  -37.909 39.228  1.00 73.31  ? 32  ALA C C   1 
ATOM   1692 O O   . ALA C 1 33 ? 17.038  -37.721 40.054  1.00 75.61  ? 32  ALA C O   1 
ATOM   1693 C CB  . ALA C 1 33 ? 14.463  -36.298 38.312  1.00 53.19  ? 32  ALA C CB  1 
ATOM   1694 N N   . VAL C 1 34 ? 16.291  -38.670 38.132  1.00 79.93  ? 33  VAL C N   1 
ATOM   1695 C CA  . VAL C 1 34 ? 17.525  -39.380 37.825  1.00 82.28  ? 33  VAL C CA  1 
ATOM   1696 C C   . VAL C 1 34 ? 18.505  -38.407 37.177  1.00 79.73  ? 33  VAL C C   1 
ATOM   1697 O O   . VAL C 1 34 ? 18.180  -37.760 36.178  1.00 62.33  ? 33  VAL C O   1 
ATOM   1698 C CB  . VAL C 1 34 ? 17.404  -40.717 37.060  1.00 82.73  ? 33  VAL C CB  1 
ATOM   1699 C CG1 . VAL C 1 34 ? 18.469  -40.893 35.978  1.00 82.15  ? 33  VAL C CG1 1 
ATOM   1700 C CG2 . VAL C 1 34 ? 17.397  -41.899 38.025  1.00 84.67  ? 33  VAL C CG2 1 
ATOM   1701 N N   . LYS C 1 35 ? 19.699  -38.336 37.789  1.00 78.82  ? 34  LYS C N   1 
ATOM   1702 C CA  . LYS C 1 35 ? 20.729  -37.356 37.490  1.00 69.84  ? 34  LYS C CA  1 
ATOM   1703 C C   . LYS C 1 35 ? 21.404  -37.735 36.172  1.00 63.38  ? 34  LYS C C   1 
ATOM   1704 O O   . LYS C 1 35 ? 21.406  -38.905 35.778  1.00 61.96  ? 34  LYS C O   1 
ATOM   1705 C CB  . LYS C 1 35 ? 21.644  -37.229 38.717  1.00 67.38  ? 34  LYS C CB  1 
ATOM   1706 N N   . PRO C 1 36 ? 21.969  -36.751 35.431  1.00 62.33  ? 35  PRO C N   1 
ATOM   1707 C CA  . PRO C 1 36 ? 22.672  -37.046 34.181  1.00 59.04  ? 35  PRO C CA  1 
ATOM   1708 C C   . PRO C 1 36 ? 23.830  -38.019 34.417  1.00 62.76  ? 35  PRO C C   1 
ATOM   1709 O O   . PRO C 1 36 ? 24.328  -38.173 35.536  1.00 53.86  ? 35  PRO C O   1 
ATOM   1710 C CB  . PRO C 1 36 ? 23.175  -35.656 33.728  1.00 63.29  ? 35  PRO C CB  1 
ATOM   1711 C CG  . PRO C 1 36 ? 22.274  -34.664 34.433  1.00 60.19  ? 35  PRO C CG  1 
ATOM   1712 C CD  . PRO C 1 36 ? 21.972  -35.316 35.773  1.00 60.66  ? 35  PRO C CD  1 
ATOM   1713 N N   . PRO C 1 37 ? 24.315  -38.723 33.373  1.00 53.48  ? 36  PRO C N   1 
ATOM   1714 C CA  . PRO C 1 37 ? 25.642  -39.327 33.456  1.00 50.86  ? 36  PRO C CA  1 
ATOM   1715 C C   . PRO C 1 37 ? 26.603  -38.169 33.733  1.00 53.43  ? 36  PRO C C   1 
ATOM   1716 O O   . PRO C 1 37 ? 26.287  -37.014 33.422  1.00 47.39  ? 36  PRO C O   1 
ATOM   1717 C CB  . PRO C 1 37 ? 25.831  -39.943 32.055  1.00 44.87  ? 36  PRO C CB  1 
ATOM   1718 C CG  . PRO C 1 37 ? 24.410  -40.184 31.587  1.00 45.40  ? 36  PRO C CG  1 
ATOM   1719 C CD  . PRO C 1 37 ? 23.627  -38.985 32.101  1.00 48.26  ? 36  PRO C CD  1 
ATOM   1720 N N   . PRO C 1 38 ? 27.790  -38.440 34.330  1.00 46.71  ? 37  PRO C N   1 
ATOM   1721 C CA  . PRO C 1 38 ? 28.735  -37.385 34.697  1.00 49.08  ? 37  PRO C CA  1 
ATOM   1722 C C   . PRO C 1 38 ? 29.015  -36.462 33.518  1.00 47.23  ? 37  PRO C C   1 
ATOM   1723 O O   . PRO C 1 38 ? 29.331  -36.939 32.426  1.00 38.42  ? 37  PRO C O   1 
ATOM   1724 C CB  . PRO C 1 38 ? 29.992  -38.207 35.078  1.00 51.59  ? 37  PRO C CB  1 
ATOM   1725 C CG  . PRO C 1 38 ? 29.432  -39.504 35.611  1.00 46.97  ? 37  PRO C CG  1 
ATOM   1726 C CD  . PRO C 1 38 ? 28.285  -39.786 34.666  1.00 49.49  ? 37  PRO C CD  1 
ATOM   1727 N N   . ASN C 1 39 ? 28.855  -35.155 33.770  1.00 45.46  ? 38  ASN C N   1 
ATOM   1728 C CA  . ASN C 1 39 ? 29.227  -34.079 32.862  1.00 43.44  ? 38  ASN C CA  1 
ATOM   1729 C C   . ASN C 1 39 ? 28.341  -34.062 31.613  1.00 42.99  ? 38  ASN C C   1 
ATOM   1730 O O   . ASN C 1 39 ? 28.791  -33.599 30.561  1.00 45.69  ? 38  ASN C O   1 
ATOM   1731 C CB  . ASN C 1 39 ? 30.690  -34.141 32.438  1.00 49.86  ? 38  ASN C CB  1 
ATOM   1732 C CG  . ASN C 1 39 ? 31.151  -32.846 31.801  1.00 61.46  ? 38  ASN C CG  1 
ATOM   1733 O OD1 . ASN C 1 39 ? 30.628  -31.764 32.110  1.00 68.09  ? 38  ASN C OD1 1 
ATOM   1734 N ND2 . ASN C 1 39 ? 32.137  -32.929 30.920  1.00 63.73  ? 38  ASN C ND2 1 
ATOM   1735 N N   . LYS C 1 40 ? 27.095  -34.544 31.730  1.00 36.38  ? 39  LYS C N   1 
ATOM   1736 C CA  . LYS C 1 40 ? 26.166  -34.465 30.608  1.00 35.80  ? 39  LYS C CA  1 
ATOM   1737 C C   . LYS C 1 40 ? 25.024  -33.517 30.954  1.00 36.06  ? 39  LYS C C   1 
ATOM   1738 O O   . LYS C 1 40 ? 24.619  -33.433 32.105  1.00 36.70  ? 39  LYS C O   1 
ATOM   1739 C CB  . LYS C 1 40 ? 25.477  -35.805 30.344  1.00 35.45  ? 39  LYS C CB  1 
ATOM   1740 C CG  . LYS C 1 40 ? 26.422  -36.947 30.070  1.00 40.18  ? 39  LYS C CG  1 
ATOM   1741 C CD  . LYS C 1 40 ? 27.190  -36.851 28.769  1.00 46.84  ? 39  LYS C CD  1 
ATOM   1742 C CE  . LYS C 1 40 ? 27.732  -38.213 28.463  1.00 54.17  ? 39  LYS C CE  1 
ATOM   1743 N NZ  . LYS C 1 40 ? 28.772  -38.078 27.443  1.00 63.62  ? 39  LYS C NZ  1 
ATOM   1744 N N   . TYR C 1 41 ? 24.497  -32.809 29.946  1.00 32.26  ? 40  TYR C N   1 
ATOM   1745 C CA  . TYR C 1 41 ? 23.385  -31.891 30.152  1.00 32.22  ? 40  TYR C CA  1 
ATOM   1746 C C   . TYR C 1 41 ? 22.103  -32.525 29.618  1.00 35.95  ? 40  TYR C C   1 
ATOM   1747 O O   . TYR C 1 41 ? 22.157  -33.270 28.628  1.00 36.77  ? 40  TYR C O   1 
ATOM   1748 C CB  . TYR C 1 41 ? 23.605  -30.718 29.192  1.00 32.42  ? 40  TYR C CB  1 
ATOM   1749 C CG  . TYR C 1 41 ? 24.725  -29.783 29.592  1.00 34.84  ? 40  TYR C CG  1 
ATOM   1750 C CD1 . TYR C 1 41 ? 26.025  -29.968 29.119  1.00 37.88  ? 40  TYR C CD1 1 
ATOM   1751 C CD2 . TYR C 1 41 ? 24.477  -28.727 30.465  1.00 35.45  ? 40  TYR C CD2 1 
ATOM   1752 C CE1 . TYR C 1 41 ? 27.047  -29.113 29.493  1.00 47.00  ? 40  TYR C CE1 1 
ATOM   1753 C CE2 . TYR C 1 41 ? 25.483  -27.838 30.800  1.00 40.35  ? 40  TYR C CE2 1 
ATOM   1754 C CZ  . TYR C 1 41 ? 26.767  -28.043 30.330  1.00 42.96  ? 40  TYR C CZ  1 
ATOM   1755 O OH  . TYR C 1 41 ? 27.757  -27.174 30.674  1.00 57.71  ? 40  TYR C OH  1 
ATOM   1756 N N   . PRO C 1 42 ? 20.928  -32.243 30.239  1.00 37.19  ? 41  PRO C N   1 
ATOM   1757 C CA  . PRO C 1 42 ? 19.646  -32.710 29.710  1.00 33.37  ? 41  PRO C CA  1 
ATOM   1758 C C   . PRO C 1 42 ? 19.290  -31.776 28.560  1.00 34.96  ? 41  PRO C C   1 
ATOM   1759 O O   . PRO C 1 42 ? 19.316  -30.555 28.713  1.00 35.33  ? 41  PRO C O   1 
ATOM   1760 C CB  . PRO C 1 42 ? 18.680  -32.620 30.892  1.00 35.03  ? 41  PRO C CB  1 
ATOM   1761 C CG  . PRO C 1 42 ? 19.277  -31.551 31.770  1.00 40.69  ? 41  PRO C CG  1 
ATOM   1762 C CD  . PRO C 1 42 ? 20.781  -31.475 31.495  1.00 37.34  ? 41  PRO C CD  1 
ATOM   1763 N N   . ILE C 1 43 ? 19.028  -32.384 27.398  1.00 33.48  ? 42  ILE C N   1 
ATOM   1764 C CA  . ILE C 1 43 ? 18.696  -31.636 26.195  1.00 32.20  ? 42  ILE C CA  1 
ATOM   1765 C C   . ILE C 1 43 ? 17.265  -31.967 25.799  1.00 36.41  ? 42  ILE C C   1 
ATOM   1766 O O   . ILE C 1 43 ? 16.882  -33.137 25.754  1.00 36.50  ? 42  ILE C O   1 
ATOM   1767 C CB  . ILE C 1 43 ? 19.670  -32.036 25.074  1.00 30.79  ? 42  ILE C CB  1 
ATOM   1768 C CG1 . ILE C 1 43 ? 21.148  -31.753 25.479  1.00 31.48  ? 42  ILE C CG1 1 
ATOM   1769 C CG2 . ILE C 1 43 ? 19.279  -31.434 23.712  1.00 26.36  ? 42  ILE C CG2 1 
ATOM   1770 C CD1 . ILE C 1 43 ? 21.448  -30.329 25.910  1.00 32.81  ? 42  ILE C CD1 1 
ATOM   1771 N N   . PHE C 1 44 ? 16.499  -30.920 25.453  1.00 36.09  ? 43  PHE C N   1 
ATOM   1772 C CA  . PHE C 1 44 ? 15.228  -31.072 24.770  1.00 30.30  ? 43  PHE C CA  1 
ATOM   1773 C C   . PHE C 1 44 ? 15.410  -30.658 23.308  1.00 30.51  ? 43  PHE C C   1 
ATOM   1774 O O   . PHE C 1 44 ? 15.889  -29.565 23.038  1.00 31.60  ? 43  PHE C O   1 
ATOM   1775 C CB  . PHE C 1 44 ? 14.309  -30.035 25.418  1.00 32.20  ? 43  PHE C CB  1 
ATOM   1776 C CG  . PHE C 1 44 ? 12.939  -29.948 24.757  1.00 37.53  ? 43  PHE C CG  1 
ATOM   1777 C CD1 . PHE C 1 44 ? 11.940  -30.885 25.055  1.00 41.66  ? 43  PHE C CD1 1 
ATOM   1778 C CD2 . PHE C 1 44 ? 12.642  -28.914 23.861  1.00 37.18  ? 43  PHE C CD2 1 
ATOM   1779 C CE1 . PHE C 1 44 ? 10.687  -30.813 24.453  1.00 45.54  ? 43  PHE C CE1 1 
ATOM   1780 C CE2 . PHE C 1 44 ? 11.390  -28.848 23.260  1.00 39.49  ? 43  PHE C CE2 1 
ATOM   1781 C CZ  . PHE C 1 44 ? 10.418  -29.795 23.553  1.00 44.99  ? 43  PHE C CZ  1 
ATOM   1782 N N   . PHE C 1 45 ? 14.971  -31.503 22.382  1.00 28.75  ? 44  PHE C N   1 
ATOM   1783 C CA  . PHE C 1 45 ? 15.113  -31.258 20.956  1.00 30.35  ? 44  PHE C CA  1 
ATOM   1784 C C   . PHE C 1 45 ? 13.846  -30.608 20.409  1.00 32.98  ? 44  PHE C C   1 
ATOM   1785 O O   . PHE C 1 45 ? 12.754  -31.147 20.575  1.00 32.43  ? 44  PHE C O   1 
ATOM   1786 C CB  . PHE C 1 45 ? 15.340  -32.593 20.247  1.00 30.40  ? 44  PHE C CB  1 
ATOM   1787 C CG  . PHE C 1 45 ? 16.724  -33.162 20.524  1.00 33.46  ? 44  PHE C CG  1 
ATOM   1788 C CD1 . PHE C 1 45 ? 17.829  -32.764 19.768  1.00 30.26  ? 44  PHE C CD1 1 
ATOM   1789 C CD2 . PHE C 1 45 ? 16.921  -34.047 21.587  1.00 32.44  ? 44  PHE C CD2 1 
ATOM   1790 C CE1 . PHE C 1 45 ? 19.095  -33.304 20.040  1.00 32.83  ? 44  PHE C CE1 1 
ATOM   1791 C CE2 . PHE C 1 45 ? 18.174  -34.590 21.840  1.00 33.20  ? 44  PHE C CE2 1 
ATOM   1792 C CZ  . PHE C 1 45 ? 19.252  -34.211 21.079  1.00 31.89  ? 44  PHE C CZ  1 
ATOM   1793 N N   . PHE C 1 46 ? 14.002  -29.464 19.716  1.00 29.66  ? 45  PHE C N   1 
ATOM   1794 C CA  . PHE C 1 46 ? 12.841  -28.848 19.090  1.00 30.17  ? 45  PHE C CA  1 
ATOM   1795 C C   . PHE C 1 46 ? 12.339  -29.729 17.945  1.00 30.55  ? 45  PHE C C   1 
ATOM   1796 O O   . PHE C 1 46 ? 13.089  -30.513 17.379  1.00 29.61  ? 45  PHE C O   1 
ATOM   1797 C CB  . PHE C 1 46 ? 13.175  -27.417 18.643  1.00 28.83  ? 45  PHE C CB  1 
ATOM   1798 C CG  . PHE C 1 46 ? 13.434  -26.440 19.780  1.00 29.81  ? 45  PHE C CG  1 
ATOM   1799 C CD1 . PHE C 1 46 ? 12.381  -26.027 20.593  1.00 33.36  ? 45  PHE C CD1 1 
ATOM   1800 C CD2 . PHE C 1 46 ? 14.695  -25.897 20.003  1.00 28.39  ? 45  PHE C CD2 1 
ATOM   1801 C CE1 . PHE C 1 46 ? 12.617  -25.120 21.620  1.00 32.61  ? 45  PHE C CE1 1 
ATOM   1802 C CE2 . PHE C 1 46 ? 14.912  -24.970 21.023  1.00 29.10  ? 45  PHE C CE2 1 
ATOM   1803 C CZ  . PHE C 1 46 ? 13.873  -24.585 21.825  1.00 29.64  ? 45  PHE C CZ  1 
ATOM   1804 N N   . GLY C 1 47 ? 11.052  -29.593 17.615  1.00 30.41  ? 46  GLY C N   1 
ATOM   1805 C CA  . GLY C 1 47 ? 10.480  -30.316 16.483  1.00 36.92  ? 46  GLY C CA  1 
ATOM   1806 C C   . GLY C 1 47 ? 10.009  -31.710 16.889  1.00 43.96  ? 46  GLY C C   1 
ATOM   1807 O O   . GLY C 1 47 ? 8.807   -31.995 16.852  1.00 41.93  ? 46  GLY C O   1 
ATOM   1808 N N   . THR C 1 48 ? 10.962  -32.560 17.305  1.00 42.35  ? 47  THR C N   1 
ATOM   1809 C CA  . THR C 1 48 ? 10.601  -33.906 17.733  1.00 38.65  ? 47  THR C CA  1 
ATOM   1810 C C   . THR C 1 48 ? 10.126  -33.861 19.180  1.00 37.05  ? 47  THR C C   1 
ATOM   1811 O O   . THR C 1 48 ? 9.347   -34.729 19.575  1.00 39.99  ? 47  THR C O   1 
ATOM   1812 C CB  . THR C 1 48 ? 11.764  -34.883 17.587  1.00 34.58  ? 47  THR C CB  1 
ATOM   1813 O OG1 . THR C 1 48 ? 12.649  -34.398 18.599  1.00 35.05  ? 47  THR C OG1 1 
ATOM   1814 C CG2 . THR C 1 48 ? 12.375  -34.867 16.201  1.00 34.08  ? 47  THR C CG2 1 
ATOM   1815 N N   . HIS C 1 49 ? 10.609  -32.870 19.951  1.00 35.93  ? 48  HIS C N   1 
ATOM   1816 C CA  . HIS C 1 49 ? 10.328  -32.710 21.379  1.00 41.77  ? 48  HIS C CA  1 
ATOM   1817 C C   . HIS C 1 49 ? 10.742  -33.932 22.204  1.00 40.03  ? 48  HIS C C   1 
ATOM   1818 O O   . HIS C 1 49 ? 10.083  -34.279 23.186  1.00 43.33  ? 48  HIS C O   1 
ATOM   1819 C CB  . HIS C 1 49 ? 8.880   -32.284 21.672  1.00 42.13  ? 48  HIS C CB  1 
ATOM   1820 C CG  . HIS C 1 49 ? 8.341   -31.294 20.698  1.00 44.63  ? 48  HIS C CG  1 
ATOM   1821 N ND1 . HIS C 1 49 ? 7.422   -31.662 19.739  1.00 46.04  ? 48  HIS C ND1 1 
ATOM   1822 C CD2 . HIS C 1 49 ? 8.605   -29.993 20.493  1.00 43.25  ? 48  HIS C CD2 1 
ATOM   1823 C CE1 . HIS C 1 49 ? 7.135   -30.605 18.986  1.00 52.47  ? 48  HIS C CE1 1 
ATOM   1824 N NE2 . HIS C 1 49 ? 7.831   -29.579 19.439  1.00 48.47  ? 48  HIS C NE2 1 
ATOM   1825 N N   . GLU C 1 50 ? 11.847  -34.563 21.818  1.00 38.46  ? 49  GLU C N   1 
ATOM   1826 C CA  . GLU C 1 50 ? 12.418  -35.656 22.588  1.00 39.95  ? 49  GLU C CA  1 
ATOM   1827 C C   . GLU C 1 50 ? 13.527  -35.117 23.486  1.00 42.95  ? 49  GLU C C   1 
ATOM   1828 O O   . GLU C 1 50 ? 13.921  -33.955 23.365  1.00 41.12  ? 49  GLU C O   1 
ATOM   1829 C CB  . GLU C 1 50 ? 12.857  -36.706 21.578  1.00 38.59  ? 49  GLU C CB  1 
ATOM   1830 C CG  . GLU C 1 50 ? 11.656  -37.304 20.852  1.00 47.15  ? 49  GLU C CG  1 
ATOM   1831 C CD  . GLU C 1 50 ? 12.072  -38.354 19.845  1.00 52.84  ? 49  GLU C CD  1 
ATOM   1832 O OE1 . GLU C 1 50 ? 13.254  -38.761 19.847  1.00 64.83  ? 49  GLU C OE1 1 
ATOM   1833 O OE2 . GLU C 1 50 ? 11.210  -38.749 19.041  1.00 63.96  ? 49  GLU C OE2 1 
ATOM   1834 N N   . THR C 1 51 ? 14.004  -35.961 24.412  1.00 39.76  ? 50  THR C N   1 
ATOM   1835 C CA  . THR C 1 51 ? 15.062  -35.559 25.330  1.00 40.01  ? 50  THR C CA  1 
ATOM   1836 C C   . THR C 1 51 ? 16.216  -36.567 25.274  1.00 35.78  ? 50  THR C C   1 
ATOM   1837 O O   . THR C 1 51 ? 16.061  -37.699 24.829  1.00 39.15  ? 50  THR C O   1 
ATOM   1838 C CB  . THR C 1 51 ? 14.519  -35.348 26.749  1.00 41.61  ? 50  THR C CB  1 
ATOM   1839 O OG1 . THR C 1 51 ? 13.879  -36.564 27.129  1.00 44.21  ? 50  THR C OG1 1 
ATOM   1840 C CG2 . THR C 1 51 ? 13.521  -34.209 26.851  1.00 37.03  ? 50  THR C CG2 1 
ATOM   1841 N N   . ALA C 1 52 ? 17.402  -36.124 25.681  1.00 38.11  ? 51  ALA C N   1 
ATOM   1842 C CA  . ALA C 1 52 ? 18.557  -37.002 25.784  1.00 36.05  ? 51  ALA C CA  1 
ATOM   1843 C C   . ALA C 1 52 ? 19.574  -36.301 26.672  1.00 40.09  ? 51  ALA C C   1 
ATOM   1844 O O   . ALA C 1 52 ? 19.373  -35.140 27.019  1.00 38.94  ? 51  ALA C O   1 
ATOM   1845 C CB  . ALA C 1 52 ? 19.135  -37.297 24.415  1.00 38.49  ? 51  ALA C CB  1 
ATOM   1846 N N   . PHE C 1 53 ? 20.643  -37.018 27.056  1.00 39.42  ? 52  PHE C N   1 
ATOM   1847 C CA  . PHE C 1 53 ? 21.771  -36.400 27.739  1.00 39.34  ? 52  PHE C CA  1 
ATOM   1848 C C   . PHE C 1 53 ? 22.915  -36.289 26.747  1.00 35.80  ? 52  PHE C C   1 
ATOM   1849 O O   . PHE C 1 53 ? 23.243  -37.264 26.082  1.00 35.50  ? 52  PHE C O   1 
ATOM   1850 C CB  . PHE C 1 53 ? 22.243  -37.338 28.854  1.00 34.66  ? 52  PHE C CB  1 
ATOM   1851 C CG  . PHE C 1 53 ? 21.280  -37.315 30.020  1.00 40.76  ? 52  PHE C CG  1 
ATOM   1852 C CD1 . PHE C 1 53 ? 20.993  -36.124 30.678  1.00 40.98  ? 52  PHE C CD1 1 
ATOM   1853 C CD2 . PHE C 1 53 ? 20.645  -38.480 30.444  1.00 50.02  ? 52  PHE C CD2 1 
ATOM   1854 C CE1 . PHE C 1 53 ? 20.113  -36.097 31.751  1.00 46.29  ? 52  PHE C CE1 1 
ATOM   1855 C CE2 . PHE C 1 53 ? 19.766  -38.445 31.523  1.00 52.39  ? 52  PHE C CE2 1 
ATOM   1856 C CZ  . PHE C 1 53 ? 19.483  -37.253 32.155  1.00 45.54  ? 52  PHE C CZ  1 
ATOM   1857 N N   . LEU C 1 54 ? 23.551  -35.119 26.699  1.00 31.19  ? 53  LEU C N   1 
ATOM   1858 C CA  . LEU C 1 54 ? 24.706  -34.915 25.835  1.00 33.85  ? 53  LEU C CA  1 
ATOM   1859 C C   . LEU C 1 54 ? 25.803  -34.159 26.583  1.00 33.93  ? 53  LEU C C   1 
ATOM   1860 O O   . LEU C 1 54 ? 25.503  -33.347 27.453  1.00 34.34  ? 53  LEU C O   1 
ATOM   1861 C CB  . LEU C 1 54 ? 24.318  -34.151 24.568  1.00 32.09  ? 53  LEU C CB  1 
ATOM   1862 C CG  . LEU C 1 54 ? 23.525  -34.909 23.496  1.00 38.94  ? 53  LEU C CG  1 
ATOM   1863 C CD1 . LEU C 1 54 ? 23.267  -33.946 22.359  1.00 33.90  ? 53  LEU C CD1 1 
ATOM   1864 C CD2 . LEU C 1 54 ? 24.313  -36.102 22.964  1.00 42.98  ? 53  LEU C CD2 1 
ATOM   1865 N N   . GLY C 1 55 ? 27.056  -34.412 26.182  1.00 35.99  ? 54  GLY C N   1 
ATOM   1866 C CA  . GLY C 1 55 ? 28.228  -33.689 26.660  1.00 33.16  ? 54  GLY C CA  1 
ATOM   1867 C C   . GLY C 1 55 ? 28.477  -32.388 25.892  1.00 40.68  ? 54  GLY C C   1 
ATOM   1868 O O   . GLY C 1 55 ? 28.025  -32.195 24.743  1.00 35.44  ? 54  GLY C O   1 
ATOM   1869 N N   . PRO C 1 56 ? 29.249  -31.454 26.496  1.00 40.47  ? 55  PRO C N   1 
ATOM   1870 C CA  . PRO C 1 56 ? 29.423  -30.121 25.918  1.00 43.49  ? 55  PRO C CA  1 
ATOM   1871 C C   . PRO C 1 56 ? 30.152  -30.156 24.576  1.00 38.26  ? 55  PRO C C   1 
ATOM   1872 O O   . PRO C 1 56 ? 30.016  -29.246 23.764  1.00 48.82  ? 55  PRO C O   1 
ATOM   1873 C CB  . PRO C 1 56 ? 30.148  -29.327 27.030  1.00 46.06  ? 55  PRO C CB  1 
ATOM   1874 C CG  . PRO C 1 56 ? 30.871  -30.398 27.822  1.00 41.47  ? 55  PRO C CG  1 
ATOM   1875 C CD  . PRO C 1 56 ? 29.984  -31.636 27.766  1.00 42.48  ? 55  PRO C CD  1 
ATOM   1876 N N   . LYS C 1 57 ? 30.869  -31.254 24.325  1.00 41.07  ? 56  LYS C N   1 
ATOM   1877 C CA  . LYS C 1 57 ? 31.452  -31.542 23.025  1.00 44.44  ? 56  LYS C CA  1 
ATOM   1878 C C   . LYS C 1 57 ? 30.389  -31.427 21.931  1.00 47.57  ? 56  LYS C C   1 
ATOM   1879 O O   . LYS C 1 57 ? 30.700  -31.062 20.794  1.00 42.63  ? 56  LYS C O   1 
ATOM   1880 C CB  . LYS C 1 57 ? 31.993  -32.982 22.976  1.00 44.75  ? 56  LYS C CB  1 
ATOM   1881 N N   . ASP C 1 58 ? 29.142  -31.785 22.279  1.00 44.35  ? 57  ASP C N   1 
ATOM   1882 C CA  . ASP C 1 58 ? 28.108  -32.004 21.282  1.00 40.00  ? 57  ASP C CA  1 
ATOM   1883 C C   . ASP C 1 58 ? 27.159  -30.822 21.178  1.00 38.05  ? 57  ASP C C   1 
ATOM   1884 O O   . ASP C 1 58 ? 26.132  -30.944 20.520  1.00 34.42  ? 57  ASP C O   1 
ATOM   1885 C CB  . ASP C 1 58 ? 27.310  -33.257 21.586  1.00 44.46  ? 57  ASP C CB  1 
ATOM   1886 C CG  . ASP C 1 58 ? 28.165  -34.508 21.594  1.00 46.05  ? 57  ASP C CG  1 
ATOM   1887 O OD1 . ASP C 1 58 ? 29.046  -34.595 20.720  1.00 51.00  ? 57  ASP C OD1 1 
ATOM   1888 O OD2 . ASP C 1 58 ? 27.915  -35.372 22.444  1.00 48.40  ? 57  ASP C OD2 1 
ATOM   1889 N N   . LEU C 1 59 ? 27.493  -29.710 21.839  1.00 30.01  ? 58  LEU C N   1 
ATOM   1890 C CA  . LEU C 1 59 ? 26.566  -28.599 21.974  1.00 35.62  ? 58  LEU C CA  1 
ATOM   1891 C C   . LEU C 1 59 ? 27.237  -27.345 21.436  1.00 38.14  ? 58  LEU C C   1 
ATOM   1892 O O   . LEU C 1 59 ? 28.426  -27.151 21.679  1.00 43.15  ? 58  LEU C O   1 
ATOM   1893 C CB  . LEU C 1 59 ? 26.192  -28.434 23.448  1.00 33.53  ? 58  LEU C CB  1 
ATOM   1894 C CG  . LEU C 1 59 ? 25.598  -29.681 24.111  1.00 33.77  ? 58  LEU C CG  1 
ATOM   1895 C CD1 . LEU C 1 59 ? 25.466  -29.487 25.613  1.00 33.01  ? 58  LEU C CD1 1 
ATOM   1896 C CD2 . LEU C 1 59 ? 24.257  -30.072 23.474  1.00 24.97  ? 58  LEU C CD2 1 
ATOM   1897 N N   . PHE C 1 60 ? 26.459  -26.521 20.718  1.00 38.49  ? 59  PHE C N   1 
ATOM   1898 C CA  . PHE C 1 60 ? 26.918  -25.293 20.077  1.00 41.71  ? 59  PHE C CA  1 
ATOM   1899 C C   . PHE C 1 60 ? 25.908  -24.181 20.340  1.00 39.30  ? 59  PHE C C   1 
ATOM   1900 O O   . PHE C 1 60 ? 24.716  -24.348 20.086  1.00 37.68  ? 59  PHE C O   1 
ATOM   1901 C CB  . PHE C 1 60 ? 27.131  -25.518 18.577  1.00 40.67  ? 59  PHE C CB  1 
ATOM   1902 C CG  . PHE C 1 60 ? 28.036  -26.700 18.256  1.00 42.66  ? 59  PHE C CG  1 
ATOM   1903 C CD1 . PHE C 1 60 ? 27.541  -28.004 18.260  1.00 39.43  ? 59  PHE C CD1 1 
ATOM   1904 C CD2 . PHE C 1 60 ? 29.388  -26.506 17.959  1.00 42.78  ? 59  PHE C CD2 1 
ATOM   1905 C CE1 . PHE C 1 60 ? 28.370  -29.088 17.996  1.00 37.76  ? 59  PHE C CE1 1 
ATOM   1906 C CE2 . PHE C 1 60 ? 30.210  -27.592 17.670  1.00 42.60  ? 59  PHE C CE2 1 
ATOM   1907 C CZ  . PHE C 1 60 ? 29.700  -28.877 17.691  1.00 42.75  ? 59  PHE C CZ  1 
ATOM   1908 N N   . PRO C 1 61 ? 26.327  -23.015 20.891  1.00 42.04  ? 60  PRO C N   1 
ATOM   1909 C CA  . PRO C 1 61 ? 25.389  -21.924 21.168  1.00 41.38  ? 60  PRO C CA  1 
ATOM   1910 C C   . PRO C 1 61 ? 24.673  -21.543 19.878  1.00 40.26  ? 60  PRO C C   1 
ATOM   1911 O O   . PRO C 1 61 ? 25.300  -21.442 18.813  1.00 42.28  ? 60  PRO C O   1 
ATOM   1912 C CB  . PRO C 1 61 ? 26.263  -20.773 21.730  1.00 42.22  ? 60  PRO C CB  1 
ATOM   1913 C CG  . PRO C 1 61 ? 27.533  -21.473 22.177  1.00 42.10  ? 60  PRO C CG  1 
ATOM   1914 C CD  . PRO C 1 61 ? 27.714  -22.679 21.261  1.00 44.37  ? 60  PRO C CD  1 
ATOM   1915 N N   . TYR C 1 62 ? 23.350  -21.362 20.023  1.00 39.20  ? 61  TYR C N   1 
ATOM   1916 C CA  . TYR C 1 62 ? 22.423  -21.160 18.926  1.00 45.00  ? 61  TYR C CA  1 
ATOM   1917 C C   . TYR C 1 62 ? 22.810  -19.919 18.131  1.00 50.37  ? 61  TYR C C   1 
ATOM   1918 O O   . TYR C 1 62 ? 22.870  -19.979 16.902  1.00 48.03  ? 61  TYR C O   1 
ATOM   1919 C CB  . TYR C 1 62 ? 20.990  -20.944 19.416  1.00 44.14  ? 61  TYR C CB  1 
ATOM   1920 C CG  . TYR C 1 62 ? 20.018  -20.584 18.302  1.00 47.36  ? 61  TYR C CG  1 
ATOM   1921 C CD1 . TYR C 1 62 ? 19.844  -21.414 17.189  1.00 45.37  ? 61  TYR C CD1 1 
ATOM   1922 C CD2 . TYR C 1 62 ? 19.301  -19.388 18.349  1.00 43.84  ? 61  TYR C CD2 1 
ATOM   1923 C CE1 . TYR C 1 62 ? 18.953  -21.078 16.175  1.00 46.77  ? 61  TYR C CE1 1 
ATOM   1924 C CE2 . TYR C 1 62 ? 18.418  -19.041 17.337  1.00 46.56  ? 61  TYR C CE2 1 
ATOM   1925 C CZ  . TYR C 1 62 ? 18.251  -19.882 16.246  1.00 45.75  ? 61  TYR C CZ  1 
ATOM   1926 O OH  . TYR C 1 62 ? 17.366  -19.498 15.283  1.00 40.72  ? 61  TYR C OH  1 
ATOM   1927 N N   . ASP C 1 63 ? 23.070  -18.813 18.844  1.00 49.78  ? 62  ASP C N   1 
ATOM   1928 C CA  . ASP C 1 63 ? 23.404  -17.550 18.192  1.00 56.42  ? 62  ASP C CA  1 
ATOM   1929 C C   . ASP C 1 63 ? 24.748  -17.619 17.472  1.00 47.08  ? 62  ASP C C   1 
ATOM   1930 O O   . ASP C 1 63 ? 24.860  -17.147 16.346  1.00 56.30  ? 62  ASP C O   1 
ATOM   1931 C CB  . ASP C 1 63 ? 23.131  -16.347 19.077  1.00 63.66  ? 62  ASP C CB  1 
ATOM   1932 C CG  . ASP C 1 63 ? 21.804  -15.679 18.758  1.00 77.51  ? 62  ASP C CG  1 
ATOM   1933 O OD1 . ASP C 1 63 ? 20.836  -15.902 19.520  1.00 78.92  ? 62  ASP C OD1 1 
ATOM   1934 O OD2 . ASP C 1 63 ? 21.746  -14.963 17.729  1.00 83.95  ? 62  ASP C OD2 1 
ATOM   1935 N N   . LYS C 1 64 ? 25.742  -18.256 18.089  1.00 43.01  ? 63  LYS C N   1 
ATOM   1936 C CA  . LYS C 1 64 ? 27.065  -18.380 17.489  1.00 42.60  ? 63  LYS C CA  1 
ATOM   1937 C C   . LYS C 1 64 ? 27.028  -19.244 16.227  1.00 40.91  ? 63  LYS C C   1 
ATOM   1938 O O   . LYS C 1 64 ? 27.796  -18.983 15.298  1.00 41.51  ? 63  LYS C O   1 
ATOM   1939 C CB  . LYS C 1 64 ? 28.136  -18.884 18.471  1.00 42.13  ? 63  LYS C CB  1 
ATOM   1940 N N   . SER C 1 65 ? 26.125  -20.246 16.166  1.00 38.46  ? 64  SER C N   1 
ATOM   1941 C CA  . SER C 1 65 ? 26.313  -21.317 15.188  1.00 35.27  ? 64  SER C CA  1 
ATOM   1942 C C   . SER C 1 65 ? 25.151  -21.428 14.187  1.00 36.52  ? 64  SER C C   1 
ATOM   1943 O O   . SER C 1 65 ? 25.149  -22.281 13.300  1.00 34.94  ? 64  SER C O   1 
ATOM   1944 C CB  . SER C 1 65 ? 26.647  -22.634 15.870  1.00 40.22  ? 64  SER C CB  1 
ATOM   1945 O OG  . SER C 1 65 ? 25.516  -23.150 16.568  1.00 38.64  ? 64  SER C OG  1 
ATOM   1946 N N   . LYS C 1 66 ? 24.139  -20.567 14.324  1.00 35.31  ? 65  LYS C N   1 
ATOM   1947 C CA  . LYS C 1 66 ? 22.951  -20.747 13.502  1.00 37.85  ? 65  LYS C CA  1 
ATOM   1948 C C   . LYS C 1 66 ? 23.276  -20.519 12.028  1.00 36.68  ? 65  LYS C C   1 
ATOM   1949 O O   . LYS C 1 66 ? 22.663  -21.143 11.169  1.00 40.85  ? 65  LYS C O   1 
ATOM   1950 C CB  . LYS C 1 66 ? 21.765  -19.906 13.969  1.00 37.30  ? 65  LYS C CB  1 
ATOM   1951 C CG  . LYS C 1 66 ? 22.012  -18.412 13.949  1.00 38.55  ? 65  LYS C CG  1 
ATOM   1952 C CD  . LYS C 1 66 ? 20.742  -17.721 14.422  1.00 48.55  ? 65  LYS C CD  1 
ATOM   1953 C CE  . LYS C 1 66 ? 20.861  -16.240 14.460  1.00 50.54  ? 65  LYS C CE  1 
ATOM   1954 N NZ  . LYS C 1 66 ? 19.918  -15.779 15.478  1.00 56.98  ? 65  LYS C NZ  1 
ATOM   1955 N N   . ASP C 1 67 ? 24.267  -19.664 11.734  1.00 42.21  ? 66  ASP C N   1 
ATOM   1956 C CA  . ASP C 1 67 ? 24.632  -19.402 10.339  1.00 43.81  ? 66  ASP C CA  1 
ATOM   1957 C C   . ASP C 1 67 ? 25.077  -20.710 9.683   1.00 40.57  ? 66  ASP C C   1 
ATOM   1958 O O   . ASP C 1 67 ? 24.852  -20.925 8.496   1.00 41.81  ? 66  ASP C O   1 
ATOM   1959 C CB  . ASP C 1 67 ? 25.559  -18.195 10.173  1.00 48.07  ? 66  ASP C CB  1 
ATOM   1960 C CG  . ASP C 1 67 ? 26.942  -18.297 10.814  1.00 60.81  ? 66  ASP C CG  1 
ATOM   1961 O OD1 . ASP C 1 67 ? 27.200  -19.299 11.532  1.00 60.26  ? 66  ASP C OD1 1 
ATOM   1962 O OD2 . ASP C 1 67 ? 27.756  -17.356 10.620  1.00 60.14  ? 66  ASP C OD2 1 
ATOM   1963 N N   . LYS C 1 68 ? 25.652  -21.619 10.484  1.00 38.16  ? 67  LYS C N   1 
ATOM   1964 C CA  . LYS C 1 68 ? 26.174  -22.879 9.969   1.00 38.89  ? 67  LYS C CA  1 
ATOM   1965 C C   . LYS C 1 68 ? 25.128  -24.007 10.011  1.00 39.46  ? 67  LYS C C   1 
ATOM   1966 O O   . LYS C 1 68 ? 24.986  -24.747 9.039   1.00 36.65  ? 67  LYS C O   1 
ATOM   1967 C CB  . LYS C 1 68 ? 27.466  -23.195 10.730  1.00 39.46  ? 67  LYS C CB  1 
ATOM   1968 C CG  . LYS C 1 68 ? 28.190  -24.495 10.424  1.00 47.32  ? 67  LYS C CG  1 
ATOM   1969 C CD  . LYS C 1 68 ? 29.549  -24.456 11.128  1.00 55.15  ? 67  LYS C CD  1 
ATOM   1970 C CE  . LYS C 1 68 ? 30.227  -25.780 11.362  1.00 59.31  ? 67  LYS C CE  1 
ATOM   1971 N NZ  . LYS C 1 68 ? 30.361  -26.585 10.144  1.00 65.54  ? 67  LYS C NZ  1 
ATOM   1972 N N   . TYR C 1 69 ? 24.415  -24.173 11.137  1.00 31.43  ? 68  TYR C N   1 
ATOM   1973 C CA  . TYR C 1 69 ? 23.562  -25.347 11.301  1.00 31.70  ? 68  TYR C CA  1 
ATOM   1974 C C   . TYR C 1 69 ? 22.085  -25.003 11.080  1.00 29.78  ? 68  TYR C C   1 
ATOM   1975 O O   . TYR C 1 69 ? 21.249  -25.896 10.968  1.00 32.18  ? 68  TYR C O   1 
ATOM   1976 C CB  . TYR C 1 69 ? 23.758  -25.943 12.704  1.00 30.43  ? 68  TYR C CB  1 
ATOM   1977 C CG  . TYR C 1 69 ? 25.182  -26.365 13.025  1.00 35.05  ? 68  TYR C CG  1 
ATOM   1978 C CD1 . TYR C 1 69 ? 25.925  -27.167 12.161  1.00 35.44  ? 68  TYR C CD1 1 
ATOM   1979 C CD2 . TYR C 1 69 ? 25.794  -25.925 14.193  1.00 39.20  ? 68  TYR C CD2 1 
ATOM   1980 C CE1 . TYR C 1 69 ? 27.224  -27.551 12.471  1.00 34.52  ? 68  TYR C CE1 1 
ATOM   1981 C CE2 . TYR C 1 69 ? 27.083  -26.316 14.523  1.00 36.45  ? 68  TYR C CE2 1 
ATOM   1982 C CZ  . TYR C 1 69 ? 27.798  -27.135 13.663  1.00 38.95  ? 68  TYR C CZ  1 
ATOM   1983 O OH  . TYR C 1 69 ? 29.089  -27.457 14.017  1.00 39.82  ? 68  TYR C OH  1 
ATOM   1984 N N   . GLY C 1 70 ? 21.749  -23.709 11.073  1.00 31.57  ? 69  GLY C N   1 
ATOM   1985 C CA  . GLY C 1 70 ? 20.346  -23.341 10.992  1.00 36.92  ? 69  GLY C CA  1 
ATOM   1986 C C   . GLY C 1 70 ? 19.962  -23.214 9.525   1.00 37.13  ? 69  GLY C C   1 
ATOM   1987 O O   . GLY C 1 70 ? 19.920  -22.111 8.976   1.00 37.26  ? 69  GLY C O   1 
ATOM   1988 N N   . LYS C 1 71 ? 19.814  -24.371 8.891   1.00 38.70  ? 70  LYS C N   1 
ATOM   1989 C CA  . LYS C 1 71 ? 19.411  -24.456 7.500   1.00 38.17  ? 70  LYS C CA  1 
ATOM   1990 C C   . LYS C 1 71 ? 18.518  -25.685 7.396   1.00 37.85  ? 70  LYS C C   1 
ATOM   1991 O O   . LYS C 1 71 ? 18.728  -26.665 8.104   1.00 38.92  ? 70  LYS C O   1 
ATOM   1992 C CB  . LYS C 1 71 ? 20.624  -24.552 6.569   1.00 39.62  ? 70  LYS C CB  1 
ATOM   1993 C CG  . LYS C 1 71 ? 21.715  -25.516 7.021   1.00 49.04  ? 70  LYS C CG  1 
ATOM   1994 C CD  . LYS C 1 71 ? 22.779  -26.003 6.041   1.00 55.60  ? 70  LYS C CD  1 
ATOM   1995 C CE  . LYS C 1 71 ? 23.755  -26.912 6.744   1.00 58.78  ? 70  LYS C CE  1 
ATOM   1996 N N   . PRO C 1 72 ? 17.465  -25.650 6.555   1.00 32.43  ? 71  PRO C N   1 
ATOM   1997 C CA  . PRO C 1 72 ? 16.520  -26.755 6.507   1.00 31.03  ? 71  PRO C CA  1 
ATOM   1998 C C   . PRO C 1 72 ? 17.195  -28.082 6.179   1.00 32.72  ? 71  PRO C C   1 
ATOM   1999 O O   . PRO C 1 72 ? 18.224  -28.137 5.507   1.00 34.72  ? 71  PRO C O   1 
ATOM   2000 C CB  . PRO C 1 72 ? 15.616  -26.312 5.357   1.00 32.95  ? 71  PRO C CB  1 
ATOM   2001 C CG  . PRO C 1 72 ? 15.625  -24.801 5.511   1.00 33.11  ? 71  PRO C CG  1 
ATOM   2002 C CD  . PRO C 1 72 ? 17.118  -24.517 5.680   1.00 31.76  ? 71  PRO C CD  1 
ATOM   2003 N N   . ASN C 1 73 ? 16.531  -29.150 6.578   1.00 33.55  ? 72  ASN C N   1 
ATOM   2004 C CA  . ASN C 1 73 ? 16.810  -30.432 5.964   1.00 39.84  ? 72  ASN C CA  1 
ATOM   2005 C C   . ASN C 1 73 ? 15.574  -31.284 6.180   1.00 33.88  ? 72  ASN C C   1 
ATOM   2006 O O   . ASN C 1 73 ? 14.655  -30.860 6.878   1.00 32.56  ? 72  ASN C O   1 
ATOM   2007 C CB  . ASN C 1 73 ? 18.131  -31.048 6.419   1.00 46.32  ? 72  ASN C CB  1 
ATOM   2008 C CG  . ASN C 1 73 ? 18.021  -31.576 7.824   1.00 44.20  ? 72  ASN C CG  1 
ATOM   2009 O OD1 . ASN C 1 73 ? 17.229  -32.492 8.098   1.00 42.20  ? 72  ASN C OD1 1 
ATOM   2010 N ND2 . ASN C 1 73 ? 18.804  -30.998 8.716   1.00 45.99  ? 72  ASN C ND2 1 
ATOM   2011 N N   . LYS C 1 74 ? 15.578  -32.483 5.587   1.00 35.09  ? 73  LYS C N   1 
ATOM   2012 C CA  . LYS C 1 74 ? 14.328  -33.191 5.404   1.00 33.26  ? 73  LYS C CA  1 
ATOM   2013 C C   . LYS C 1 74 ? 14.153  -34.225 6.507   1.00 35.65  ? 73  LYS C C   1 
ATOM   2014 O O   . LYS C 1 74 ? 13.228  -35.030 6.438   1.00 38.70  ? 73  LYS C O   1 
ATOM   2015 C CB  . LYS C 1 74 ? 14.235  -33.786 3.988   1.00 34.92  ? 73  LYS C CB  1 
ATOM   2016 N N   . ARG C 1 75 ? 15.044  -34.234 7.512   1.00 33.93  ? 74  ARG C N   1 
ATOM   2017 C CA  . ARG C 1 75 ? 14.874  -35.174 8.609   1.00 33.57  ? 74  ARG C CA  1 
ATOM   2018 C C   . ARG C 1 75 ? 13.610  -34.822 9.380   1.00 35.34  ? 74  ARG C C   1 
ATOM   2019 O O   . ARG C 1 75 ? 13.314  -33.644 9.577   1.00 31.33  ? 74  ARG C O   1 
ATOM   2020 C CB  . ARG C 1 75 ? 16.060  -35.256 9.587   1.00 36.35  ? 74  ARG C CB  1 
ATOM   2021 C CG  . ARG C 1 75 ? 17.387  -35.595 8.921   1.00 41.80  ? 74  ARG C CG  1 
ATOM   2022 C CD  . ARG C 1 75 ? 17.594  -36.996 8.346   1.00 42.17  ? 74  ARG C CD  1 
ATOM   2023 N NE  . ARG C 1 75 ? 17.645  -37.937 9.466   1.00 41.10  ? 74  ARG C NE  1 
ATOM   2024 C CZ  . ARG C 1 75 ? 18.767  -38.345 10.064  1.00 37.07  ? 74  ARG C CZ  1 
ATOM   2025 N NH1 . ARG C 1 75 ? 18.668  -38.923 11.239  1.00 38.71  ? 74  ARG C NH1 1 
ATOM   2026 N NH2 . ARG C 1 75 ? 19.952  -38.051 9.547   1.00 40.05  ? 74  ARG C NH2 1 
ATOM   2027 N N   . LYS C 1 76 ? 12.908  -35.869 9.846   1.00 36.62  ? 75  LYS C N   1 
ATOM   2028 C CA  . LYS C 1 76 ? 11.608  -35.751 10.486  1.00 39.54  ? 75  LYS C CA  1 
ATOM   2029 C C   . LYS C 1 76 ? 11.662  -34.767 11.651  1.00 38.02  ? 75  LYS C C   1 
ATOM   2030 O O   . LYS C 1 76 ? 12.413  -34.943 12.616  1.00 31.80  ? 75  LYS C O   1 
ATOM   2031 C CB  . LYS C 1 76 ? 11.013  -37.116 10.867  1.00 42.47  ? 75  LYS C CB  1 
ATOM   2032 C CG  . LYS C 1 76 ? 9.504   -37.085 11.113  1.00 51.87  ? 75  LYS C CG  1 
ATOM   2033 C CD  . LYS C 1 76 ? 8.948   -38.311 11.829  1.00 56.53  ? 75  LYS C CD  1 
ATOM   2034 C CE  . LYS C 1 76 ? 7.647   -38.044 12.521  1.00 58.55  ? 75  LYS C CE  1 
ATOM   2035 N NZ  . LYS C 1 76 ? 7.320   -39.145 13.429  1.00 67.27  ? 75  LYS C NZ  1 
ATOM   2036 N N   . GLY C 1 77 ? 10.839  -33.717 11.558  1.00 35.10  ? 76  GLY C N   1 
ATOM   2037 C CA  . GLY C 1 77 ? 10.676  -32.829 12.696  1.00 30.62  ? 76  GLY C CA  1 
ATOM   2038 C C   . GLY C 1 77 ? 11.687  -31.679 12.662  1.00 28.11  ? 76  GLY C C   1 
ATOM   2039 O O   . GLY C 1 77 ? 11.592  -30.744 13.449  1.00 33.95  ? 76  GLY C O   1 
ATOM   2040 N N   . PHE C 1 78 ? 12.656  -31.742 11.748  1.00 30.14  ? 77  PHE C N   1 
ATOM   2041 C CA  . PHE C 1 78 ? 13.755  -30.789 11.802  1.00 28.96  ? 77  PHE C CA  1 
ATOM   2042 C C   . PHE C 1 78 ? 13.242  -29.362 11.546  1.00 32.07  ? 77  PHE C C   1 
ATOM   2043 O O   . PHE C 1 78 ? 13.625  -28.421 12.242  1.00 28.65  ? 77  PHE C O   1 
ATOM   2044 C CB  . PHE C 1 78 ? 14.857  -31.135 10.799  1.00 34.95  ? 77  PHE C CB  1 
ATOM   2045 C CG  . PHE C 1 78 ? 16.151  -30.377 11.081  1.00 33.14  ? 77  PHE C CG  1 
ATOM   2046 C CD1 . PHE C 1 78 ? 16.402  -29.148 10.474  1.00 30.25  ? 77  PHE C CD1 1 
ATOM   2047 C CD2 . PHE C 1 78 ? 17.121  -30.902 11.936  1.00 29.93  ? 77  PHE C CD2 1 
ATOM   2048 C CE1 . PHE C 1 78 ? 17.572  -28.450 10.744  1.00 30.34  ? 77  PHE C CE1 1 
ATOM   2049 C CE2 . PHE C 1 78 ? 18.306  -30.210 12.173  1.00 27.19  ? 77  PHE C CE2 1 
ATOM   2050 C CZ  . PHE C 1 78 ? 18.529  -28.996 11.581  1.00 29.21  ? 77  PHE C CZ  1 
ATOM   2051 N N   . ASN C 1 79 ? 12.456  -29.192 10.472  1.00 29.67  ? 78  ASN C N   1 
ATOM   2052 C CA  . ASN C 1 79 ? 12.099  -27.852 10.027  1.00 33.00  ? 78  ASN C CA  1 
ATOM   2053 C C   . ASN C 1 79 ? 11.120  -27.216 11.005  1.00 28.29  ? 78  ASN C C   1 
ATOM   2054 O O   . ASN C 1 79 ? 11.206  -26.019 11.286  1.00 28.21  ? 78  ASN C O   1 
ATOM   2055 C CB  . ASN C 1 79 ? 11.665  -27.832 8.566   1.00 33.01  ? 78  ASN C CB  1 
ATOM   2056 C CG  . ASN C 1 79 ? 12.800  -28.235 7.647   1.00 31.54  ? 78  ASN C CG  1 
ATOM   2057 O OD1 . ASN C 1 79 ? 13.964  -27.942 7.931   1.00 30.20  ? 78  ASN C OD1 1 
ATOM   2058 N ND2 . ASN C 1 79 ? 12.486  -28.808 6.495   1.00 33.07  ? 78  ASN C ND2 1 
ATOM   2059 N N   . GLU C 1 80 ? 10.228  -28.018 11.577  1.00 33.47  ? 79  GLU C N   1 
ATOM   2060 C CA  . GLU C 1 80 ? 9.389   -27.507 12.654  1.00 32.68  ? 79  GLU C CA  1 
ATOM   2061 C C   . GLU C 1 80 ? 10.261  -27.089 13.829  1.00 32.71  ? 79  GLU C C   1 
ATOM   2062 O O   . GLU C 1 80 ? 9.989   -26.071 14.471  1.00 31.34  ? 79  GLU C O   1 
ATOM   2063 C CB  . GLU C 1 80 ? 8.385   -28.558 13.131  1.00 35.69  ? 79  GLU C CB  1 
ATOM   2064 C CG  . GLU C 1 80 ? 7.483   -28.045 14.248  1.00 37.73  ? 79  GLU C CG  1 
ATOM   2065 C CD  . GLU C 1 80 ? 6.265   -28.936 14.411  1.00 51.63  ? 79  GLU C CD  1 
ATOM   2066 O OE1 . GLU C 1 80 ? 6.291   -30.067 13.880  1.00 51.65  ? 79  GLU C OE1 1 
ATOM   2067 O OE2 . GLU C 1 80 ? 5.276   -28.495 15.040  1.00 49.05  ? 79  GLU C OE2 1 
ATOM   2068 N N   . GLY C 1 81 ? 11.333  -27.873 14.084  1.00 31.76  ? 80  GLY C N   1 
ATOM   2069 C CA  . GLY C 1 81 ? 12.293  -27.523 15.130  1.00 28.59  ? 80  GLY C CA  1 
ATOM   2070 C C   . GLY C 1 81 ? 12.935  -26.145 14.912  1.00 30.33  ? 80  GLY C C   1 
ATOM   2071 O O   . GLY C 1 81 ? 13.176  -25.372 15.847  1.00 27.70  ? 80  GLY C O   1 
ATOM   2072 N N   . LEU C 1 82 ? 13.279  -25.850 13.657  1.00 27.93  ? 81  LEU C N   1 
ATOM   2073 C CA  . LEU C 1 82 ? 13.924  -24.580 13.348  1.00 31.09  ? 81  LEU C CA  1 
ATOM   2074 C C   . LEU C 1 82 ? 12.923  -23.440 13.581  1.00 29.04  ? 81  LEU C C   1 
ATOM   2075 O O   . LEU C 1 82 ? 13.316  -22.344 13.993  1.00 30.64  ? 81  LEU C O   1 
ATOM   2076 C CB  . LEU C 1 82 ? 14.369  -24.594 11.883  1.00 31.94  ? 81  LEU C CB  1 
ATOM   2077 C CG  . LEU C 1 82 ? 15.590  -25.431 11.496  1.00 32.88  ? 81  LEU C CG  1 
ATOM   2078 C CD1 . LEU C 1 82 ? 15.783  -25.269 9.977   1.00 28.58  ? 81  LEU C CD1 1 
ATOM   2079 C CD2 . LEU C 1 82 ? 16.820  -24.911 12.213  1.00 29.26  ? 81  LEU C CD2 1 
ATOM   2080 N N   . TRP C 1 83 ? 11.641  -23.677 13.260  1.00 29.59  ? 82  TRP C N   1 
ATOM   2081 C CA  . TRP C 1 83 ? 10.626  -22.659 13.539  1.00 33.09  ? 82  TRP C CA  1 
ATOM   2082 C C   . TRP C 1 83 ? 10.522  -22.373 15.049  1.00 34.91  ? 82  TRP C C   1 
ATOM   2083 O O   . TRP C 1 83 ? 10.522  -21.208 15.469  1.00 33.21  ? 82  TRP C O   1 
ATOM   2084 C CB  . TRP C 1 83 ? 9.275   -23.004 12.898  1.00 33.51  ? 82  TRP C CB  1 
ATOM   2085 C CG  . TRP C 1 83 ? 8.247   -21.900 13.045  1.00 39.26  ? 82  TRP C CG  1 
ATOM   2086 C CD1 . TRP C 1 83 ? 7.979   -20.887 12.162  1.00 36.06  ? 82  TRP C CD1 1 
ATOM   2087 C CD2 . TRP C 1 83 ? 7.379   -21.674 14.180  1.00 36.90  ? 82  TRP C CD2 1 
ATOM   2088 N NE1 . TRP C 1 83 ? 7.002   -20.067 12.655  1.00 38.49  ? 82  TRP C NE1 1 
ATOM   2089 C CE2 . TRP C 1 83 ? 6.617   -20.515 13.892  1.00 37.32  ? 82  TRP C CE2 1 
ATOM   2090 C CE3 . TRP C 1 83 ? 7.174   -22.332 15.401  1.00 35.90  ? 82  TRP C CE3 1 
ATOM   2091 C CZ2 . TRP C 1 83 ? 5.672   -20.012 14.783  1.00 40.21  ? 82  TRP C CZ2 1 
ATOM   2092 C CZ3 . TRP C 1 83 ? 6.252   -21.824 16.295  1.00 38.66  ? 82  TRP C CZ3 1 
ATOM   2093 C CH2 . TRP C 1 83 ? 5.514   -20.675 15.987  1.00 43.99  ? 82  TRP C CH2 1 
ATOM   2094 N N   . GLU C 1 84 ? 10.512  -23.439 15.864  1.00 34.20  ? 83  GLU C N   1 
ATOM   2095 C CA  . GLU C 1 84 ? 10.352  -23.325 17.311  1.00 35.84  ? 83  GLU C CA  1 
ATOM   2096 C C   . GLU C 1 84 ? 11.493  -22.546 17.952  1.00 34.27  ? 83  GLU C C   1 
ATOM   2097 O O   . GLU C 1 84 ? 11.229  -21.668 18.785  1.00 36.02  ? 83  GLU C O   1 
ATOM   2098 C CB  . GLU C 1 84 ? 10.188  -24.681 18.006  1.00 32.33  ? 83  GLU C CB  1 
ATOM   2099 C CG  . GLU C 1 84 ? 8.888   -25.359 17.574  1.00 36.36  ? 83  GLU C CG  1 
ATOM   2100 C CD  . GLU C 1 84 ? 8.764   -26.762 18.109  1.00 42.56  ? 83  GLU C CD  1 
ATOM   2101 O OE1 . GLU C 1 84 ? 9.755   -27.190 18.739  1.00 37.69  ? 83  GLU C OE1 1 
ATOM   2102 O OE2 . GLU C 1 84 ? 7.723   -27.428 17.892  1.00 41.53  ? 83  GLU C OE2 1 
ATOM   2103 N N   . ILE C 1 85 ? 12.741  -22.854 17.555  1.00 30.85  ? 84  ILE C N   1 
ATOM   2104 C CA  . ILE C 1 85 ? 13.931  -22.240 18.147  1.00 30.36  ? 84  ILE C CA  1 
ATOM   2105 C C   . ILE C 1 85 ? 13.989  -20.733 17.873  1.00 34.77  ? 84  ILE C C   1 
ATOM   2106 O O   . ILE C 1 85 ? 14.521  -19.992 18.697  1.00 31.68  ? 84  ILE C O   1 
ATOM   2107 C CB  . ILE C 1 85 ? 15.257  -22.956 17.803  1.00 28.84  ? 84  ILE C CB  1 
ATOM   2108 C CG1 . ILE C 1 85 ? 16.393  -22.519 18.762  1.00 30.40  ? 84  ILE C CG1 1 
ATOM   2109 C CG2 . ILE C 1 85 ? 15.674  -22.839 16.332  1.00 27.85  ? 84  ILE C CG2 1 
ATOM   2110 C CD1 . ILE C 1 85 ? 17.567  -23.490 18.877  1.00 28.44  ? 84  ILE C CD1 1 
ATOM   2111 N N   . GLN C 1 86 ? 13.508  -20.315 16.692  1.00 34.01  ? 85  GLN C N   1 
ATOM   2112 C CA  . GLN C 1 86 ? 13.482  -18.913 16.295  1.00 34.61  ? 85  GLN C CA  1 
ATOM   2113 C C   . GLN C 1 86 ? 12.268  -18.187 16.874  1.00 34.80  ? 85  GLN C C   1 
ATOM   2114 O O   . GLN C 1 86 ? 12.382  -17.030 17.279  1.00 37.37  ? 85  GLN C O   1 
ATOM   2115 C CB  . GLN C 1 86 ? 13.470  -18.797 14.766  1.00 33.84  ? 85  GLN C CB  1 
ATOM   2116 C CG  . GLN C 1 86 ? 13.666  -17.377 14.233  1.00 33.95  ? 85  GLN C CG  1 
ATOM   2117 C CD  . GLN C 1 86 ? 14.188  -17.367 12.800  1.00 36.04  ? 85  GLN C CD  1 
ATOM   2118 O OE1 . GLN C 1 86 ? 14.111  -18.364 12.072  1.00 38.81  ? 85  GLN C OE1 1 
ATOM   2119 N NE2 . GLN C 1 86 ? 14.783  -16.262 12.384  1.00 35.58  ? 85  GLN C NE2 1 
ATOM   2120 N N   . ASN C 1 87 ? 11.120  -18.865 16.897  1.00 35.29  ? 86  ASN C N   1 
ATOM   2121 C CA  . ASN C 1 87 ? 9.822   -18.217 17.050  1.00 41.78  ? 86  ASN C CA  1 
ATOM   2122 C C   . ASN C 1 87 ? 9.131   -18.541 18.382  1.00 43.51  ? 86  ASN C C   1 
ATOM   2123 O O   . ASN C 1 87 ? 8.223   -17.816 18.757  1.00 38.52  ? 86  ASN C O   1 
ATOM   2124 C CB  . ASN C 1 87 ? 8.911   -18.501 15.857  1.00 37.26  ? 86  ASN C CB  1 
ATOM   2125 C CG  . ASN C 1 87 ? 9.535   -17.938 14.599  1.00 40.92  ? 86  ASN C CG  1 
ATOM   2126 O OD1 . ASN C 1 87 ? 9.660   -16.716 14.476  1.00 40.50  ? 86  ASN C OD1 1 
ATOM   2127 N ND2 . ASN C 1 87 ? 10.013  -18.793 13.707  1.00 33.92  ? 86  ASN C ND2 1 
ATOM   2128 N N   . ASN C 1 88 ? 9.503   -19.626 19.083  1.00 45.10  ? 87  ASN C N   1 
ATOM   2129 C CA  . ASN C 1 88 ? 8.755   -20.028 20.281  1.00 39.70  ? 87  ASN C CA  1 
ATOM   2130 C C   . ASN C 1 88 ? 9.654   -20.880 21.180  1.00 39.39  ? 87  ASN C C   1 
ATOM   2131 O O   . ASN C 1 88 ? 9.304   -22.010 21.527  1.00 43.76  ? 87  ASN C O   1 
ATOM   2132 C CB  . ASN C 1 88 ? 7.505   -20.841 19.917  1.00 42.43  ? 87  ASN C CB  1 
ATOM   2133 C CG  . ASN C 1 88 ? 6.448   -20.880 21.004  1.00 53.15  ? 87  ASN C CG  1 
ATOM   2134 O OD1 . ASN C 1 88 ? 6.542   -20.148 21.995  1.00 55.77  ? 87  ASN C OD1 1 
ATOM   2135 N ND2 . ASN C 1 88 ? 5.431   -21.720 20.837  1.00 51.98  ? 87  ASN C ND2 1 
ATOM   2136 N N   . PRO C 1 89 ? 10.862  -20.405 21.544  1.00 38.99  ? 88  PRO C N   1 
ATOM   2137 C CA  . PRO C 1 89 ? 11.866  -21.299 22.110  1.00 38.74  ? 88  PRO C CA  1 
ATOM   2138 C C   . PRO C 1 89 ? 11.607  -21.771 23.539  1.00 45.28  ? 88  PRO C C   1 
ATOM   2139 O O   . PRO C 1 89 ? 12.331  -22.662 24.008  1.00 42.01  ? 88  PRO C O   1 
ATOM   2140 C CB  . PRO C 1 89 ? 13.174  -20.502 21.983  1.00 34.36  ? 88  PRO C CB  1 
ATOM   2141 C CG  . PRO C 1 89 ? 12.732  -19.064 22.022  1.00 40.77  ? 88  PRO C CG  1 
ATOM   2142 C CD  . PRO C 1 89 ? 11.356  -19.038 21.360  1.00 38.12  ? 88  PRO C CD  1 
ATOM   2143 N N   . HIS C 1 90 ? 10.598  -21.173 24.207  1.00 44.74  ? 89  HIS C N   1 
ATOM   2144 C CA  . HIS C 1 90 ? 10.350  -21.477 25.614  1.00 44.73  ? 89  HIS C CA  1 
ATOM   2145 C C   . HIS C 1 90 ? 8.899   -21.902 25.887  1.00 49.24  ? 89  HIS C C   1 
ATOM   2146 O O   . HIS C 1 90 ? 8.479   -21.925 27.038  1.00 54.59  ? 89  HIS C O   1 
ATOM   2147 C CB  . HIS C 1 90 ? 10.928  -20.409 26.554  1.00 39.87  ? 89  HIS C CB  1 
ATOM   2148 C CG  . HIS C 1 90 ? 12.309  -19.861 26.263  1.00 42.33  ? 89  HIS C CG  1 
ATOM   2149 N ND1 . HIS C 1 90 ? 13.481  -20.527 26.562  1.00 42.64  ? 89  HIS C ND1 1 
ATOM   2150 C CD2 . HIS C 1 90 ? 12.707  -18.682 25.727  1.00 42.22  ? 89  HIS C CD2 1 
ATOM   2151 C CE1 . HIS C 1 90 ? 14.535  -19.786 26.212  1.00 37.95  ? 89  HIS C CE1 1 
ATOM   2152 N NE2 . HIS C 1 90 ? 14.089  -18.657 25.698  1.00 39.89  ? 89  HIS C NE2 1 
ATOM   2153 N N   . ALA C 1 91 ? 8.126   -22.256 24.848  1.00 52.70  ? 90  ALA C N   1 
ATOM   2154 C CA  . ALA C 1 91 ? 6.840   -22.924 25.034  1.00 61.69  ? 90  ALA C CA  1 
ATOM   2155 C C   . ALA C 1 91 ? 7.039   -24.276 25.729  1.00 66.53  ? 90  ALA C C   1 
ATOM   2156 O O   . ALA C 1 91 ? 8.174   -24.672 25.975  1.00 66.80  ? 90  ALA C O   1 
ATOM   2157 C CB  . ALA C 1 91 ? 6.113   -23.071 23.710  1.00 58.80  ? 90  ALA C CB  1 
ATOM   2158 N N   . SER C 1 92 ? 5.932   -24.982 26.016  1.00 73.49  ? 91  SER C N   1 
ATOM   2159 C CA  . SER C 1 92 ? 5.918   -26.181 26.852  1.00 74.99  ? 91  SER C CA  1 
ATOM   2160 C C   . SER C 1 92 ? 6.167   -27.459 26.050  1.00 73.17  ? 91  SER C C   1 
ATOM   2161 O O   . SER C 1 92 ? 7.008   -28.273 26.421  1.00 66.15  ? 91  SER C O   1 
ATOM   2162 C CB  . SER C 1 92 ? 4.621   -26.305 27.631  1.00 73.67  ? 91  SER C CB  1 
ATOM   2163 O OG  . SER C 1 92 ? 4.587   -25.417 28.739  1.00 80.55  ? 91  SER C OG  1 
ATOM   2164 N N   . TYR C 1 93 ? 5.370   -27.664 24.996  1.00 75.06  ? 92  TYR C N   1 
ATOM   2165 C CA  . TYR C 1 93 ? 5.425   -28.867 24.176  1.00 82.38  ? 92  TYR C CA  1 
ATOM   2166 C C   . TYR C 1 93 ? 5.317   -30.117 25.065  1.00 85.39  ? 92  TYR C C   1 
ATOM   2167 O O   . TYR C 1 93 ? 4.238   -30.332 25.671  1.00 97.51  ? 92  TYR C O   1 
ATOM   2168 C CB  . TYR C 1 93 ? 6.696   -28.899 23.321  1.00 77.75  ? 92  TYR C CB  1 
ATOM   2169 C CG  . TYR C 1 93 ? 7.012   -27.635 22.525  1.00 74.99  ? 92  TYR C CG  1 
ATOM   2170 C CD1 . TYR C 1 93 ? 6.395   -27.378 21.300  1.00 65.72  ? 92  TYR C CD1 1 
ATOM   2171 C CD2 . TYR C 1 93 ? 7.950   -26.713 22.987  1.00 65.95  ? 92  TYR C CD2 1 
ATOM   2172 C CE1 . TYR C 1 93 ? 6.690   -26.239 20.567  1.00 57.04  ? 92  TYR C CE1 1 
ATOM   2173 C CE2 . TYR C 1 93 ? 8.261   -25.576 22.256  1.00 57.57  ? 92  TYR C CE2 1 
ATOM   2174 C CZ  . TYR C 1 93 ? 7.634   -25.344 21.044  1.00 55.77  ? 92  TYR C CZ  1 
ATOM   2175 O OH  . TYR C 1 93 ? 7.929   -24.206 20.344  1.00 58.65  ? 92  TYR C OH  1 
HETATM 2176 S S   . SO4 D 2 .  ? 0.984   -33.586 1.909   1.00 90.48  ? 101 SO4 A S   1 
HETATM 2177 O O1  . SO4 D 2 .  ? 1.333   -34.416 0.782   1.00 78.05  ? 101 SO4 A O1  1 
HETATM 2178 O O2  . SO4 D 2 .  ? 1.028   -32.201 1.518   1.00 92.64  ? 101 SO4 A O2  1 
HETATM 2179 O O3  . SO4 D 2 .  ? -0.346  -33.918 2.356   1.00 101.14 ? 101 SO4 A O3  1 
HETATM 2180 O O4  . SO4 D 2 .  ? 1.915   -33.807 2.981   1.00 86.85  ? 101 SO4 A O4  1 
HETATM 2181 S S   . SO4 E 2 .  ? -10.012 -24.435 1.210   1.00 110.35 ? 102 SO4 A S   1 
HETATM 2182 O O1  . SO4 E 2 .  ? -9.793  -24.605 -0.204  1.00 101.99 ? 102 SO4 A O1  1 
HETATM 2183 O O2  . SO4 E 2 .  ? -10.592 -23.138 1.451   1.00 111.53 ? 102 SO4 A O2  1 
HETATM 2184 O O3  . SO4 E 2 .  ? -10.909 -25.460 1.677   1.00 122.07 ? 102 SO4 A O3  1 
HETATM 2185 O O4  . SO4 E 2 .  ? -8.763  -24.539 1.917   1.00 97.56  ? 102 SO4 A O4  1 
HETATM 2186 C C1  . EDO F 3 .  ? 13.813  -19.436 -7.453  1.00 40.13  ? 103 EDO A C1  1 
HETATM 2187 O O1  . EDO F 3 .  ? 15.030  -18.711 -7.306  1.00 33.65  ? 103 EDO A O1  1 
HETATM 2188 C C2  . EDO F 3 .  ? 13.019  -19.021 -8.662  1.00 39.27  ? 103 EDO A C2  1 
HETATM 2189 O O2  . EDO F 3 .  ? 12.260  -17.857 -8.397  1.00 34.52  ? 103 EDO A O2  1 
HETATM 2190 S S   . SO4 G 2 .  ? 8.766   -29.379 5.737   1.00 62.25  ? 104 SO4 A S   1 
HETATM 2191 O O1  . SO4 G 2 .  ? 9.646   -28.743 4.808   1.00 62.07  ? 104 SO4 A O1  1 
HETATM 2192 O O2  . SO4 G 2 .  ? 8.185   -30.541 5.103   1.00 80.75  ? 104 SO4 A O2  1 
HETATM 2193 O O3  . SO4 G 2 .  ? 9.495   -29.781 6.920   1.00 62.32  ? 104 SO4 A O3  1 
HETATM 2194 O O4  . SO4 G 2 .  ? 7.710   -28.474 6.094   1.00 83.46  ? 104 SO4 A O4  1 
HETATM 2195 S S   . SO4 H 2 .  ? 7.544   -8.333  -24.664 1.00 76.46  ? 101 SO4 B S   1 
HETATM 2196 O O1  . SO4 H 2 .  ? 8.579   -8.703  -25.578 1.00 46.25  ? 101 SO4 B O1  1 
HETATM 2197 O O2  . SO4 H 2 .  ? 6.273   -8.546  -25.314 1.00 67.16  ? 101 SO4 B O2  1 
HETATM 2198 O O3  . SO4 H 2 .  ? 7.572   -9.146  -23.437 1.00 45.59  ? 101 SO4 B O3  1 
HETATM 2199 O O4  . SO4 H 2 .  ? 7.740   -6.930  -24.343 1.00 52.19  ? 101 SO4 B O4  1 
HETATM 2200 S S   . SO4 I 2 .  ? 14.428  -27.193 -26.520 1.00 67.13  ? 102 SO4 B S   1 
HETATM 2201 O O1  . SO4 I 2 .  ? 15.748  -26.752 -26.165 1.00 58.98  ? 102 SO4 B O1  1 
HETATM 2202 O O2  . SO4 I 2 .  ? 14.530  -28.469 -27.184 1.00 72.77  ? 102 SO4 B O2  1 
HETATM 2203 O O3  . SO4 I 2 .  ? 13.630  -27.324 -25.326 1.00 71.33  ? 102 SO4 B O3  1 
HETATM 2204 O O4  . SO4 I 2 .  ? 13.798  -26.238 -27.404 1.00 68.51  ? 102 SO4 B O4  1 
HETATM 2205 N N1  . ZUG J 4 .  ? 16.677  -15.910 -24.485 0.84 37.90  ? 103 ZUG B N1  1 
HETATM 2206 C C4  . ZUG J 4 .  ? 20.086  -15.040 -24.428 0.84 48.17  ? 103 ZUG B C4  1 
HETATM 2207 C C5  . ZUG J 4 .  ? 21.362  -15.434 -24.059 0.84 56.70  ? 103 ZUG B C5  1 
HETATM 2208 C C6  . ZUG J 4 .  ? 21.553  -15.944 -22.787 0.84 52.17  ? 103 ZUG B C6  1 
HETATM 2209 C C7  . ZUG J 4 .  ? 19.342  -15.708 -22.263 0.84 47.46  ? 103 ZUG B C7  1 
HETATM 2210 C C1  . ZUG J 4 .  ? 16.252  -16.903 -23.502 0.84 41.69  ? 103 ZUG B C1  1 
HETATM 2211 C C2  . ZUG J 4 .  ? 17.177  -16.465 -25.749 0.84 35.09  ? 103 ZUG B C2  1 
HETATM 2212 S S1  . ZUG J 4 .  ? 17.458  -14.621 -23.897 0.84 37.90  ? 103 ZUG B S1  1 
HETATM 2213 O O1  . ZUG J 4 .  ? 16.818  -14.233 -22.681 0.84 47.72  ? 103 ZUG B O1  1 
HETATM 2214 O O2  . ZUG J 4 .  ? 17.549  -13.698 -24.985 0.84 48.34  ? 103 ZUG B O2  1 
HETATM 2215 C C3  . ZUG J 4 .  ? 19.065  -15.174 -23.507 0.84 43.98  ? 103 ZUG B C3  1 
HETATM 2216 N N2  . ZUG J 4 .  ? 20.566  -16.090 -21.894 0.84 51.77  ? 103 ZUG B N2  1 
HETATM 2217 S S   . SO4 K 2 .  ? 28.804  -38.111 12.071  1.00 93.40  ? 101 SO4 C S   1 
HETATM 2218 O O1  . SO4 K 2 .  ? 30.050  -37.541 11.625  1.00 103.31 ? 101 SO4 C O1  1 
HETATM 2219 O O2  . SO4 K 2 .  ? 27.720  -37.563 11.306  1.00 88.76  ? 101 SO4 C O2  1 
HETATM 2220 O O3  . SO4 K 2 .  ? 28.835  -39.535 11.894  1.00 88.21  ? 101 SO4 C O3  1 
HETATM 2221 O O4  . SO4 K 2 .  ? 28.617  -37.799 13.463  1.00 104.38 ? 101 SO4 C O4  1 
HETATM 2222 N N1  . ZUG L 4 .  ? 17.239  -36.040 17.419  0.54 57.83  ? 102 ZUG C N1  1 
HETATM 2223 C C4  . ZUG L 4 .  ? 16.352  -37.380 20.435  0.54 52.10  ? 102 ZUG C C4  1 
HETATM 2224 C C5  . ZUG L 4 .  ? 16.670  -38.350 21.368  0.54 49.37  ? 102 ZUG C C5  1 
HETATM 2225 C C6  . ZUG L 4 .  ? 16.719  -39.668 20.963  0.54 51.37  ? 102 ZUG C C6  1 
HETATM 2226 C C7  . ZUG L 4 .  ? 16.168  -39.119 18.811  0.54 53.04  ? 102 ZUG C C7  1 
HETATM 2227 C C1  . ZUG L 4 .  ? 18.416  -36.677 18.020  0.54 54.74  ? 102 ZUG C C1  1 
HETATM 2228 C C2  . ZUG L 4 .  ? 17.355  -34.597 17.222  0.54 56.14  ? 102 ZUG C C2  1 
HETATM 2229 S S1  . ZUG L 4 .  ? 15.780  -36.563 17.881  0.54 55.84  ? 102 ZUG C S1  1 
HETATM 2230 O O1  . ZUG L 4 .  ? 15.211  -37.215 16.743  0.54 56.32  ? 102 ZUG C O1  1 
HETATM 2231 O O2  . ZUG L 4 .  ? 15.110  -35.455 18.476  0.54 33.68  ? 102 ZUG C O2  1 
HETATM 2232 C C3  . ZUG L 4 .  ? 16.103  -37.772 19.130  0.54 55.92  ? 102 ZUG C C3  1 
HETATM 2233 N N2  . ZUG L 4 .  ? 16.475  -40.063 19.708  0.54 52.33  ? 102 ZUG C N2  1 
HETATM 2234 O O   . HOH M 5 .  ? 8.552   -32.233 3.923   1.00 51.43  ? 201 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 10.659  -29.638 3.015   1.00 42.24  ? 202 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 5.608   -28.945 6.798   1.00 49.27  ? 203 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 9.797   -18.691 10.042  1.00 55.22  ? 204 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 0.965   -24.538 13.595  1.00 69.88  ? 205 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -0.068  -33.640 4.763   1.00 55.63  ? 206 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? -3.526  -30.533 -3.491  1.00 81.16  ? 207 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 4.070   -10.397 13.579  1.00 58.57  ? 208 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -5.925  -13.356 -16.510 1.00 48.22  ? 209 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 4.049   -34.507 4.091   1.00 57.87  ? 210 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 8.789   -18.068 -11.017 1.00 36.17  ? 211 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -3.939  -10.842 6.667   1.00 47.05  ? 212 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? -0.871  -29.441 10.079  1.00 61.36  ? 213 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -9.373  -15.289 10.847  1.00 56.42  ? 214 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 10.559  -5.146  -7.634  1.00 33.60  ? 215 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 12.665  -9.422  -7.143  1.00 42.01  ? 216 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 11.101  -12.049 5.855   1.00 37.62  ? 217 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 8.986   -22.719 -9.451  1.00 42.96  ? 218 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? -2.764  3.118   -1.927  1.00 44.53  ? 219 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 7.868   -8.198  4.505   1.00 39.30  ? 220 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -4.621  -21.094 6.053   1.00 40.69  ? 221 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 10.782  -23.633 9.820   1.00 37.27  ? 222 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 6.948   -10.488 -12.105 1.00 40.86  ? 223 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 4.331   -3.428  -3.178  1.00 35.12  ? 224 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? -0.920  -20.960 6.917   1.00 35.64  ? 225 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 4.571   -1.321  -6.130  1.00 40.18  ? 226 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 1.564   -4.616  -10.288 1.00 38.62  ? 227 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 15.562  -24.479 2.045   1.00 44.50  ? 228 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 4.346   -7.827  1.144   1.00 34.76  ? 229 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 3.015   -29.706 -0.456  1.00 42.47  ? 230 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 2.132   -25.027 -10.134 1.00 41.60  ? 231 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 19.568  -15.629 7.287   1.00 32.17  ? 232 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 13.047  -11.715 7.438   1.00 61.87  ? 233 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 0.566   -10.406 -15.699 1.00 56.97  ? 234 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -2.142  -21.906 -0.653  1.00 27.88  ? 235 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -8.004  -17.295 6.548   1.00 45.33  ? 236 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? -8.153  -15.790 -1.020  1.00 35.11  ? 237 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 6.425   -15.994 -15.030 1.00 47.63  ? 238 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 17.039  -17.947 -9.734  1.00 48.83  ? 239 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 8.552   -2.208  -0.464  1.00 69.28  ? 240 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -5.879  -15.716 -8.084  1.00 30.49  ? 241 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? -6.938  -5.298  9.228   1.00 38.88  ? 242 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 0.867   -17.741 -18.627 1.00 56.39  ? 243 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 7.808   -17.762 -15.667 1.00 50.23  ? 244 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 9.456   -6.115  -1.651  1.00 43.20  ? 245 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 9.842   -13.100 9.681   1.00 46.47  ? 246 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 1.536   0.714   -7.416  1.00 43.84  ? 247 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -8.877  -20.967 -1.160  1.00 43.78  ? 248 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 17.000  -12.861 1.422   1.00 21.82  ? 249 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 11.281  -12.337 -6.174  1.00 28.78  ? 250 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 15.588  -11.952 -5.341  1.00 41.32  ? 251 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -1.603  -11.689 11.266  1.00 42.04  ? 252 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -4.786  -25.637 -5.548  1.00 55.14  ? 253 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 10.963  -5.984  -3.813  1.00 55.13  ? 254 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 12.959  -11.994 -4.226  1.00 23.68  ? 255 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 11.380  -16.456 -14.528 1.00 44.09  ? 256 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? -0.131  -23.119 9.375   1.00 49.03  ? 257 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -8.404  -16.600 2.002   1.00 44.28  ? 258 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 12.689  -28.310 -4.669  1.00 46.89  ? 259 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -1.571  -7.410  11.382  1.00 55.47  ? 260 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 5.941   -5.899  0.313   1.00 53.15  ? 261 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 7.677   -7.904  1.306   1.00 30.29  ? 262 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? -6.038  -19.568 -5.725  1.00 42.27  ? 263 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 1.540   -10.440 11.651  1.00 33.02  ? 264 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -2.835  -11.648 13.811  1.00 48.74  ? 265 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 9.337   -30.490 9.725   1.00 37.23  ? 266 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 16.418  -11.886 -16.869 1.00 47.10  ? 267 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 12.511  -13.349 -8.537  1.00 40.76  ? 268 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? -6.363  -12.715 6.633   1.00 40.71  ? 269 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? 7.062   -30.027 -3.741  1.00 56.39  ? 270 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? -7.868  -21.236 -5.565  1.00 54.81  ? 271 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? -6.424  -11.296 -11.240 1.00 39.94  ? 272 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 14.797  -28.226 -0.867  1.00 54.63  ? 273 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -0.645  -20.538 11.203  1.00 62.59  ? 274 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? 14.496  -13.373 10.500  1.00 47.43  ? 275 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? 22.020  -16.531 -0.373  1.00 40.14  ? 276 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? 7.956   -17.782 8.767   1.00 47.54  ? 277 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? 4.802   -7.426  3.968   1.00 37.95  ? 278 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? 9.356   -20.279 -18.428 1.00 43.03  ? 279 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? -4.151  -27.242 6.186   1.00 63.47  ? 280 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? 2.917   -9.816  -13.276 1.00 48.80  ? 281 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? -3.880  -8.046  10.364  1.00 52.31  ? 282 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? 10.777  -7.813  0.434   1.00 25.15  ? 283 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? 21.148  -16.561 -3.450  1.00 32.48  ? 284 HOH A O   1 
HETATM 2318 O O   . HOH M 5 .  ? -7.496  -11.356 -8.039  1.00 30.08  ? 285 HOH A O   1 
HETATM 2319 O O   . HOH M 5 .  ? -8.490  -19.402 -3.383  1.00 45.19  ? 286 HOH A O   1 
HETATM 2320 O O   . HOH M 5 .  ? 12.933  -15.268 -11.896 1.00 48.42  ? 287 HOH A O   1 
HETATM 2321 O O   . HOH M 5 .  ? 1.796   -24.862 -6.946  1.00 57.00  ? 288 HOH A O   1 
HETATM 2322 O O   . HOH M 5 .  ? 8.432   -16.487 -13.245 1.00 46.04  ? 289 HOH A O   1 
HETATM 2323 O O   . HOH M 5 .  ? -11.676 -16.274 -3.926  1.00 55.75  ? 290 HOH A O   1 
HETATM 2324 O O   . HOH M 5 .  ? 8.812   -9.090  -13.665 1.00 42.24  ? 291 HOH A O   1 
HETATM 2325 O O   . HOH M 5 .  ? 1.098   -29.043 -7.284  1.00 69.93  ? 292 HOH A O   1 
HETATM 2326 O O   . HOH M 5 .  ? 8.719   -12.828 12.194  1.00 55.67  ? 293 HOH A O   1 
HETATM 2327 O O   . HOH M 5 .  ? -6.181  -26.650 3.317   1.00 48.99  ? 294 HOH A O   1 
HETATM 2328 O O   . HOH M 5 .  ? -3.905  -11.164 9.742   1.00 44.71  ? 295 HOH A O   1 
HETATM 2329 O O   . HOH M 5 .  ? -7.339  -14.091 -9.255  1.00 45.29  ? 296 HOH A O   1 
HETATM 2330 O O   . HOH M 5 .  ? 11.388  -21.162 10.579  1.00 42.63  ? 297 HOH A O   1 
HETATM 2331 O O   . HOH M 5 .  ? -0.677  -3.234  -10.840 1.00 54.07  ? 298 HOH A O   1 
HETATM 2332 O O   . HOH M 5 .  ? -6.007  -23.137 -7.146  1.00 50.83  ? 299 HOH A O   1 
HETATM 2333 O O   . HOH M 5 .  ? -7.404  -19.499 7.554   1.00 59.62  ? 300 HOH A O   1 
HETATM 2334 O O   . HOH M 5 .  ? 4.899   -7.052  -11.055 1.00 47.82  ? 301 HOH A O   1 
HETATM 2335 O O   . HOH M 5 .  ? -10.595 -28.186 -1.915  1.00 54.57  ? 302 HOH A O   1 
HETATM 2336 O O   . HOH M 5 .  ? 10.873  -2.023  -1.164  1.00 52.19  ? 303 HOH A O   1 
HETATM 2337 O O   . HOH M 5 .  ? 8.332   -28.053 -8.274  1.00 55.26  ? 304 HOH A O   1 
HETATM 2338 O O   . HOH M 5 .  ? -11.375 -13.230 -2.880  1.00 57.37  ? 305 HOH A O   1 
HETATM 2339 O O   . HOH M 5 .  ? 5.988   -3.172  1.187   1.00 55.18  ? 306 HOH A O   1 
HETATM 2340 O O   . HOH M 5 .  ? 4.453   -9.781  -11.305 1.00 53.49  ? 307 HOH A O   1 
HETATM 2341 O O   . HOH M 5 .  ? -6.504  -22.996 5.538   1.00 48.59  ? 308 HOH A O   1 
HETATM 2342 O O   . HOH M 5 .  ? 12.558  -18.665 -15.082 1.00 50.87  ? 309 HOH A O   1 
HETATM 2343 O O   . HOH N 5 .  ? 27.476  -8.058  -28.722 1.00 46.26  ? 201 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 31.099  -8.551  -30.165 1.00 52.07  ? 202 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 19.474  -22.131 -22.912 1.00 49.39  ? 203 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 26.067  -4.836  -33.244 1.00 49.43  ? 204 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 24.093  -1.940  -35.658 1.00 55.61  ? 205 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 34.941  -23.175 -30.052 1.00 66.52  ? 206 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 25.865  -0.490  -29.151 1.00 51.69  ? 207 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 10.063  -11.439 -37.986 1.00 54.82  ? 208 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 6.128   -7.519  -31.903 1.00 52.61  ? 209 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 6.574   -12.159 -25.920 1.00 36.05  ? 210 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 30.366  -19.733 -39.988 1.00 37.31  ? 211 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 25.105  -5.143  -29.652 1.00 39.24  ? 212 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 8.621   -27.674 -37.980 1.00 68.31  ? 213 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 13.469  -4.655  -41.482 1.00 70.38  ? 214 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 20.800  -13.300 -42.437 1.00 42.71  ? 215 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 9.069   -8.706  -16.310 1.00 43.61  ? 216 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 25.506  -6.054  -35.543 1.00 47.48  ? 217 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 22.431  -23.260 -28.531 1.00 43.14  ? 218 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 27.602  -17.805 -24.732 1.00 47.16  ? 219 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 23.568  -2.347  -28.920 1.00 40.79  ? 220 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 20.471  -3.107  -22.973 1.00 65.06  ? 221 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 26.238  -23.174 -30.917 1.00 35.62  ? 222 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 18.156  -0.645  -38.230 1.00 27.60  ? 223 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 12.656  -22.643 -20.774 1.00 49.90  ? 224 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 10.036  -19.575 -42.899 1.00 56.75  ? 225 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 31.808  -21.217 -37.858 1.00 48.01  ? 226 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 32.627  -18.581 -41.766 1.00 57.55  ? 227 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 20.890  -26.583 -30.056 1.00 52.90  ? 228 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 10.520  -18.972 -32.857 1.00 27.65  ? 229 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 16.703  -19.347 -28.545 1.00 25.56  ? 230 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 7.417   -12.631 -38.608 1.00 58.24  ? 231 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 25.215  -6.855  -42.083 1.00 61.68  ? 232 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 19.801  -25.741 -33.945 1.00 43.46  ? 233 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 7.562   -18.368 -31.764 1.00 46.25  ? 234 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 21.287  3.596   -32.665 1.00 35.45  ? 235 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 15.652  -26.362 -34.771 1.00 47.92  ? 236 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 27.185  -10.540 -28.767 1.00 55.81  ? 237 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 14.609  -6.322  -40.954 1.00 46.88  ? 238 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 10.663  -16.699 -44.225 1.00 52.82  ? 239 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 17.444  -23.792 -20.720 1.00 64.23  ? 240 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 17.617  -19.829 -41.906 1.00 57.78  ? 241 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 3.030   -8.610  -27.182 1.00 51.27  ? 242 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 4.495   -18.871 -25.418 1.00 48.98  ? 243 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 7.108   -19.037 -34.813 1.00 48.07  ? 244 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 14.588  -24.634 -40.223 1.00 57.16  ? 245 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 20.614  -10.144 -42.645 1.00 39.58  ? 246 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 23.835  -4.277  -36.627 1.00 31.13  ? 247 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 1.792   -13.024 -27.951 1.00 44.11  ? 248 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 17.759  -3.600  -21.917 1.00 52.98  ? 249 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 17.993  4.519   -34.295 1.00 38.44  ? 250 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 18.174  -26.181 -28.799 1.00 41.81  ? 251 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 7.632   -7.977  -20.555 1.00 48.69  ? 252 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 17.190  -9.758  -43.697 1.00 56.95  ? 253 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 23.723  -11.436 -21.597 1.00 46.37  ? 254 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 21.219  -6.604  -42.475 1.00 38.60  ? 255 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 18.188  -15.745 -45.547 1.00 37.36  ? 256 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 27.870  -24.890 -34.806 1.00 35.27  ? 257 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 10.353  -21.776 -32.697 1.00 36.66  ? 258 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 12.104  -21.227 -19.624 1.00 61.23  ? 259 HOH B O   1 
HETATM 2402 O O   . HOH N 5 .  ? 6.191   -20.574 -25.453 1.00 58.41  ? 260 HOH B O   1 
HETATM 2403 O O   . HOH N 5 .  ? 39.444  -13.547 -39.401 1.00 79.54  ? 261 HOH B O   1 
HETATM 2404 O O   . HOH N 5 .  ? 31.485  -12.068 -37.804 1.00 67.50  ? 262 HOH B O   1 
HETATM 2405 O O   . HOH N 5 .  ? 15.255  -8.265  -42.927 1.00 49.52  ? 263 HOH B O   1 
HETATM 2406 O O   . HOH N 5 .  ? 17.205  -0.573  -25.272 1.00 52.31  ? 264 HOH B O   1 
HETATM 2407 O O   . HOH N 5 .  ? 9.695   -6.364  -40.792 1.00 44.31  ? 265 HOH B O   1 
HETATM 2408 O O   . HOH N 5 .  ? 19.617  3.853   -33.244 1.00 43.40  ? 266 HOH B O   1 
HETATM 2409 O O   . HOH N 5 .  ? 24.372  -4.095  -27.810 1.00 57.72  ? 267 HOH B O   1 
HETATM 2410 O O   . HOH N 5 .  ? 13.362  -5.462  -17.955 1.00 56.65  ? 268 HOH B O   1 
HETATM 2411 O O   . HOH N 5 .  ? 15.412  -22.112 -41.543 1.00 57.89  ? 269 HOH B O   1 
HETATM 2412 O O   . HOH N 5 .  ? 8.788   -22.375 -19.000 1.00 58.50  ? 270 HOH B O   1 
HETATM 2413 O O   . HOH N 5 .  ? 7.449   -9.777  -18.448 1.00 44.50  ? 271 HOH B O   1 
HETATM 2414 O O   . HOH N 5 .  ? 19.427  -8.503  -43.649 1.00 51.74  ? 272 HOH B O   1 
HETATM 2415 O O   . HOH O 5 .  ? 26.231  -37.623 9.989   1.00 47.44  ? 201 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 12.980  -19.926 11.077  1.00 75.95  ? 202 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 20.011  -20.594 30.469  1.00 64.68  ? 203 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 7.003   -31.620 12.256  1.00 44.36  ? 204 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 14.520  -33.984 36.151  1.00 68.07  ? 205 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 12.055  -28.409 28.062  1.00 64.06  ? 206 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 5.546   -26.618 16.662  1.00 44.63  ? 207 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 19.656  -41.879 12.281  1.00 31.88  ? 208 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 27.516  -37.440 15.799  1.00 44.43  ? 209 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 24.947  -31.288 10.807  1.00 37.61  ? 210 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 8.866   -30.179 11.191  1.00 53.15  ? 211 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 25.986  -39.051 12.660  1.00 40.90  ? 212 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 22.365  -41.369 18.565  1.00 45.77  ? 213 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 17.612  -16.963 14.649  1.00 45.19  ? 214 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 14.736  -21.058 12.182  1.00 38.98  ? 215 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 13.846  -37.598 6.203   1.00 59.97  ? 216 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 30.994  -29.112 32.011  1.00 67.72  ? 217 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 33.184  -24.397 31.475  1.00 57.11  ? 218 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 21.988  -28.479 11.117  1.00 31.57  ? 219 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 12.426  -31.441 8.305   1.00 36.46  ? 220 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 21.757  -34.262 16.551  1.00 28.95  ? 221 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 18.799  -20.136 10.455  1.00 43.41  ? 222 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 15.525  -17.525 19.287  1.00 42.36  ? 223 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 25.232  -39.615 20.112  1.00 40.44  ? 224 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 30.043  -31.393 15.652  1.00 52.56  ? 225 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 20.464  -39.691 26.363  1.00 45.77  ? 226 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 9.240   -18.795 23.766  1.00 49.15  ? 227 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 31.028  -39.684 27.190  1.00 52.98  ? 228 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 25.866  -17.792 13.666  1.00 48.15  ? 229 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 25.675  -33.553 34.701  1.00 54.07  ? 230 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 20.644  -28.720 8.524   1.00 36.50  ? 231 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 2.575   -28.783 14.197  1.00 64.50  ? 232 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 19.037  -26.707 3.159   1.00 50.28  ? 233 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 31.143  -43.285 15.477  1.00 57.17  ? 234 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 22.631  -18.387 21.656  1.00 50.70  ? 235 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 13.943  -37.072 13.816  1.00 49.26  ? 236 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 6.611   -17.820 10.885  1.00 38.49  ? 237 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 29.648  -39.602 31.330  1.00 37.13  ? 238 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 25.373  -17.845 20.938  1.00 65.59  ? 239 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 27.327  -15.420 12.800  1.00 48.48  ? 240 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 27.403  -37.257 24.936  1.00 52.42  ? 241 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 20.374  -41.027 38.900  1.00 60.03  ? 242 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 19.764  -18.877 24.750  1.00 45.62  ? 243 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 14.169  -29.277 4.035   1.00 48.44  ? 244 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 23.930  -21.211 24.168  1.00 59.10  ? 245 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 31.849  -33.792 25.736  1.00 49.93  ? 246 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 4.755   -23.855 18.642  1.00 58.89  ? 247 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 29.679  -32.411 18.137  1.00 54.20  ? 248 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 20.899  -29.388 4.329   1.00 54.87  ? 249 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 31.939  -43.185 12.328  1.00 57.89  ? 250 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 30.526  -35.597 28.606  1.00 66.96  ? 251 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 14.145  -38.892 9.661   1.00 53.90  ? 252 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 16.466  -16.766 24.354  1.00 61.54  ? 253 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 28.739  -41.402 27.112  1.00 47.34  ? 254 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 30.349  -25.195 31.877  1.00 58.72  ? 255 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 20.171  -13.084 13.410  1.00 49.50  ? 256 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 17.236  -36.390 29.428  1.00 65.44  ? 257 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 27.553  -39.249 24.392  1.00 51.80  ? 258 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 31.130  -16.837 9.899   1.00 57.35  ? 259 HOH C O   1 
HETATM 2474 O O   . HOH O 5 .  ? 33.658  -36.209 31.402  1.00 58.44  ? 260 HOH C O   1 
HETATM 2475 O O   . HOH O 5 .  ? 15.832  -19.254 29.397  1.00 54.36  ? 261 HOH C O   1 
HETATM 2476 O O   . HOH O 5 .  ? 31.915  -38.340 30.057  1.00 64.06  ? 262 HOH C O   1 
HETATM 2477 O O   . HOH O 5 .  ? 22.204  -13.724 13.068  1.00 50.03  ? 263 HOH C O   1 
HETATM 2478 O O   . HOH O 5 .  ? 28.374  -41.202 29.841  1.00 50.21  ? 264 HOH C O   1 
HETATM 2479 O O   . HOH O 5 .  ? 5.353   -33.359 23.237  1.00 65.46  ? 265 HOH C O   1 
HETATM 2480 O O   . HOH O 5 .  ? 37.216  -23.955 26.815  1.00 59.81  ? 266 HOH C O   1 
HETATM 2481 O O   . HOH O 5 .  ? 36.478  -22.870 29.410  1.00 62.27  ? 267 HOH C O   1 
HETATM 2482 O O   . HOH O 5 .  ? 15.471  -42.113 8.134   1.00 54.47  ? 268 HOH C O   1 
# 
