data_7HGY
# 
_entry.id   7HGY 
# 
_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   7HGY         pdb_00007hgy 10.2210/pdb7hgy/pdb 
WWPDB D_1001407460 ?            ?                   
# 
_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                        7HGY 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn 'N-methyl-2-(methylsulfonyl)aniline'               185.243   1   ? ?    ? ? 
5 water       nat water                                              18.015    269 ? ?    ? ? 
# 
_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-methyl-2-(methylsulfonyl)aniline' UVA 
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 
UVA non-polymer         . 'N-methyl-2-(methylsulfonyl)aniline' ?                 'C8 H11 N O2 S'  185.243 
VAL 'L-peptide linking' y VALINE                               ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 ?  ?   ?   B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 ?  ?   ?   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 ?  ?   ?   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        UVA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UVA 
_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 4 UVA 1   105 101 UVA LIG A . 
I 2 SO4 1   101 1   SO4 SO4 B . 
J 2 SO4 1   102 3   SO4 SO4 B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 351 HOH HOH A . 
M 5 HOH 2   202 307 HOH HOH A . 
M 5 HOH 3   203 365 HOH HOH A . 
M 5 HOH 4   204 84  HOH HOH A . 
M 5 HOH 5   205 202 HOH HOH A . 
M 5 HOH 6   206 358 HOH HOH A . 
M 5 HOH 7   207 66  HOH HOH A . 
M 5 HOH 8   208 301 HOH HOH A . 
M 5 HOH 9   209 304 HOH HOH A . 
M 5 HOH 10  210 333 HOH HOH A . 
M 5 HOH 11  211 37  HOH HOH A . 
M 5 HOH 12  212 55  HOH HOH A . 
M 5 HOH 13  213 139 HOH HOH A . 
M 5 HOH 14  214 278 HOH HOH A . 
M 5 HOH 15  215 71  HOH HOH A . 
M 5 HOH 16  216 95  HOH HOH A . 
M 5 HOH 17  217 293 HOH HOH A . 
M 5 HOH 18  218 86  HOH HOH A . 
M 5 HOH 19  219 91  HOH HOH A . 
M 5 HOH 20  220 97  HOH HOH A . 
M 5 HOH 21  221 199 HOH HOH A . 
M 5 HOH 22  222 203 HOH HOH A . 
M 5 HOH 23  223 218 HOH HOH A . 
M 5 HOH 24  224 87  HOH HOH A . 
M 5 HOH 25  225 260 HOH HOH A . 
M 5 HOH 26  226 42  HOH HOH A . 
M 5 HOH 27  227 26  HOH HOH A . 
M 5 HOH 28  228 34  HOH HOH A . 
M 5 HOH 29  229 7   HOH HOH A . 
M 5 HOH 30  230 111 HOH HOH A . 
M 5 HOH 31  231 292 HOH HOH A . 
M 5 HOH 32  232 188 HOH HOH A . 
M 5 HOH 33  233 274 HOH HOH A . 
M 5 HOH 34  234 8   HOH HOH A . 
M 5 HOH 35  235 334 HOH HOH A . 
M 5 HOH 36  236 27  HOH HOH A . 
M 5 HOH 37  237 267 HOH HOH A . 
M 5 HOH 38  238 28  HOH HOH A . 
M 5 HOH 39  239 179 HOH HOH A . 
M 5 HOH 40  240 41  HOH HOH A . 
M 5 HOH 41  241 60  HOH HOH A . 
M 5 HOH 42  242 12  HOH HOH A . 
M 5 HOH 43  243 21  HOH HOH A . 
M 5 HOH 44  244 1   HOH HOH A . 
M 5 HOH 45  245 290 HOH HOH A . 
M 5 HOH 46  246 23  HOH HOH A . 
M 5 HOH 47  247 2   HOH HOH A . 
M 5 HOH 48  248 289 HOH HOH A . 
M 5 HOH 49  249 297 HOH HOH A . 
M 5 HOH 50  250 342 HOH HOH A . 
M 5 HOH 51  251 20  HOH HOH A . 
M 5 HOH 52  252 259 HOH HOH A . 
M 5 HOH 53  253 32  HOH HOH A . 
M 5 HOH 54  254 18  HOH HOH A . 
M 5 HOH 55  255 47  HOH HOH A . 
M 5 HOH 56  256 77  HOH HOH A . 
M 5 HOH 57  257 336 HOH HOH A . 
M 5 HOH 58  258 288 HOH HOH A . 
M 5 HOH 59  259 78  HOH HOH A . 
M 5 HOH 60  260 14  HOH HOH A . 
M 5 HOH 61  261 300 HOH HOH A . 
M 5 HOH 62  262 116 HOH HOH A . 
M 5 HOH 63  263 113 HOH HOH A . 
M 5 HOH 64  264 115 HOH HOH A . 
M 5 HOH 65  265 190 HOH HOH A . 
M 5 HOH 66  266 222 HOH HOH A . 
M 5 HOH 67  267 287 HOH HOH A . 
M 5 HOH 68  268 167 HOH HOH A . 
M 5 HOH 69  269 143 HOH HOH A . 
M 5 HOH 70  270 93  HOH HOH A . 
M 5 HOH 71  271 109 HOH HOH A . 
M 5 HOH 72  272 38  HOH HOH A . 
M 5 HOH 73  273 145 HOH HOH A . 
M 5 HOH 74  274 99  HOH HOH A . 
M 5 HOH 75  275 164 HOH HOH A . 
M 5 HOH 76  276 58  HOH HOH A . 
M 5 HOH 77  277 354 HOH HOH A . 
M 5 HOH 78  278 211 HOH HOH A . 
M 5 HOH 79  279 9   HOH HOH A . 
M 5 HOH 80  280 318 HOH HOH A . 
M 5 HOH 81  281 19  HOH HOH A . 
M 5 HOH 82  282 335 HOH HOH A . 
M 5 HOH 83  283 35  HOH HOH A . 
M 5 HOH 84  284 208 HOH HOH A . 
M 5 HOH 85  285 131 HOH HOH A . 
M 5 HOH 86  286 16  HOH HOH A . 
M 5 HOH 87  287 327 HOH HOH A . 
M 5 HOH 88  288 31  HOH HOH A . 
M 5 HOH 89  289 338 HOH HOH A . 
M 5 HOH 90  290 64  HOH HOH A . 
M 5 HOH 91  291 281 HOH HOH A . 
M 5 HOH 92  292 73  HOH HOH A . 
M 5 HOH 93  293 152 HOH HOH A . 
M 5 HOH 94  294 75  HOH HOH A . 
M 5 HOH 95  295 362 HOH HOH A . 
M 5 HOH 96  296 63  HOH HOH A . 
M 5 HOH 97  297 165 HOH HOH A . 
M 5 HOH 98  298 296 HOH HOH A . 
M 5 HOH 99  299 22  HOH HOH A . 
M 5 HOH 100 300 205 HOH HOH A . 
M 5 HOH 101 301 340 HOH HOH A . 
M 5 HOH 102 302 210 HOH HOH A . 
M 5 HOH 103 303 83  HOH HOH A . 
M 5 HOH 104 304 337 HOH HOH A . 
M 5 HOH 105 305 347 HOH HOH A . 
M 5 HOH 106 306 219 HOH HOH A . 
M 5 HOH 107 307 156 HOH HOH A . 
M 5 HOH 108 308 185 HOH HOH A . 
M 5 HOH 109 309 283 HOH HOH A . 
M 5 HOH 110 310 369 HOH HOH A . 
M 5 HOH 111 311 57  HOH HOH A . 
M 5 HOH 112 312 125 HOH HOH A . 
M 5 HOH 113 313 313 HOH HOH A . 
M 5 HOH 114 314 332 HOH HOH A . 
N 5 HOH 1   201 249 HOH HOH B . 
N 5 HOH 2   202 272 HOH HOH B . 
N 5 HOH 3   203 247 HOH HOH B . 
N 5 HOH 4   204 89  HOH HOH B . 
N 5 HOH 5   205 168 HOH HOH B . 
N 5 HOH 6   206 123 HOH HOH B . 
N 5 HOH 7   207 17  HOH HOH B . 
N 5 HOH 8   208 258 HOH HOH B . 
N 5 HOH 9   209 329 HOH HOH B . 
N 5 HOH 10  210 184 HOH HOH B . 
N 5 HOH 11  211 69  HOH HOH B . 
N 5 HOH 12  212 331 HOH HOH B . 
N 5 HOH 13  213 177 HOH HOH B . 
N 5 HOH 14  214 72  HOH HOH B . 
N 5 HOH 15  215 346 HOH HOH B . 
N 5 HOH 16  216 137 HOH HOH B . 
N 5 HOH 17  217 280 HOH HOH B . 
N 5 HOH 18  218 175 HOH HOH B . 
N 5 HOH 19  219 360 HOH HOH B . 
N 5 HOH 20  220 320 HOH HOH B . 
N 5 HOH 21  221 10  HOH HOH B . 
N 5 HOH 22  222 117 HOH HOH B . 
N 5 HOH 23  223 119 HOH HOH B . 
N 5 HOH 24  224 25  HOH HOH B . 
N 5 HOH 25  225 6   HOH HOH B . 
N 5 HOH 26  226 98  HOH HOH B . 
N 5 HOH 27  227 315 HOH HOH B . 
N 5 HOH 28  228 172 HOH HOH B . 
N 5 HOH 29  229 215 HOH HOH B . 
N 5 HOH 30  230 68  HOH HOH B . 
N 5 HOH 31  231 5   HOH HOH B . 
N 5 HOH 32  232 54  HOH HOH B . 
N 5 HOH 33  233 368 HOH HOH B . 
N 5 HOH 34  234 59  HOH HOH B . 
N 5 HOH 35  235 170 HOH HOH B . 
N 5 HOH 36  236 242 HOH HOH B . 
N 5 HOH 37  237 169 HOH HOH B . 
N 5 HOH 38  238 96  HOH HOH B . 
N 5 HOH 39  239 61  HOH HOH B . 
N 5 HOH 40  240 319 HOH HOH B . 
N 5 HOH 41  241 150 HOH HOH B . 
N 5 HOH 42  242 13  HOH HOH B . 
N 5 HOH 43  243 24  HOH HOH B . 
N 5 HOH 44  244 157 HOH HOH B . 
N 5 HOH 45  245 261 HOH HOH B . 
N 5 HOH 46  246 101 HOH HOH B . 
N 5 HOH 47  247 79  HOH HOH B . 
N 5 HOH 48  248 223 HOH HOH B . 
N 5 HOH 49  249 153 HOH HOH B . 
N 5 HOH 50  250 197 HOH HOH B . 
N 5 HOH 51  251 74  HOH HOH B . 
N 5 HOH 52  252 214 HOH HOH B . 
N 5 HOH 53  253 217 HOH HOH B . 
N 5 HOH 54  254 36  HOH HOH B . 
N 5 HOH 55  255 120 HOH HOH B . 
N 5 HOH 56  256 182 HOH HOH B . 
N 5 HOH 57  257 46  HOH HOH B . 
N 5 HOH 58  258 350 HOH HOH B . 
N 5 HOH 59  259 76  HOH HOH B . 
N 5 HOH 60  260 104 HOH HOH B . 
N 5 HOH 61  261 339 HOH HOH B . 
N 5 HOH 62  262 303 HOH HOH B . 
N 5 HOH 63  263 279 HOH HOH B . 
N 5 HOH 64  264 322 HOH HOH B . 
N 5 HOH 65  265 291 HOH HOH B . 
N 5 HOH 66  266 44  HOH HOH B . 
N 5 HOH 67  267 316 HOH HOH B . 
N 5 HOH 68  268 160 HOH HOH B . 
N 5 HOH 69  269 163 HOH HOH B . 
N 5 HOH 70  270 224 HOH HOH B . 
N 5 HOH 71  271 201 HOH HOH B . 
N 5 HOH 72  272 359 HOH HOH B . 
N 5 HOH 73  273 344 HOH HOH B . 
N 5 HOH 74  274 343 HOH HOH B . 
N 5 HOH 75  275 314 HOH HOH B . 
N 5 HOH 76  276 107 HOH HOH B . 
N 5 HOH 77  277 312 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 366 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 254 HOH HOH C . 
O 5 HOH 5   205 352 HOH HOH C . 
O 5 HOH 6   206 353 HOH HOH C . 
O 5 HOH 7   207 345 HOH HOH C . 
O 5 HOH 8   208 271 HOH HOH C . 
O 5 HOH 9   209 118 HOH HOH C . 
O 5 HOH 10  210 142 HOH HOH C . 
O 5 HOH 11  211 325 HOH HOH C . 
O 5 HOH 12  212 49  HOH HOH C . 
O 5 HOH 13  213 209 HOH HOH C . 
O 5 HOH 14  214 173 HOH HOH C . 
O 5 HOH 15  215 294 HOH HOH C . 
O 5 HOH 16  216 269 HOH HOH C . 
O 5 HOH 17  217 326 HOH HOH C . 
O 5 HOH 18  218 161 HOH HOH C . 
O 5 HOH 19  219 302 HOH HOH C . 
O 5 HOH 20  220 85  HOH HOH C . 
O 5 HOH 21  221 90  HOH HOH C . 
O 5 HOH 22  222 198 HOH HOH C . 
O 5 HOH 23  223 275 HOH HOH C . 
O 5 HOH 24  224 15  HOH HOH C . 
O 5 HOH 25  225 361 HOH HOH C . 
O 5 HOH 26  226 284 HOH HOH C . 
O 5 HOH 27  227 134 HOH HOH C . 
O 5 HOH 28  228 82  HOH HOH C . 
O 5 HOH 29  229 126 HOH HOH C . 
O 5 HOH 30  230 45  HOH HOH C . 
O 5 HOH 31  231 328 HOH HOH C . 
O 5 HOH 32  232 67  HOH HOH C . 
O 5 HOH 33  233 309 HOH HOH C . 
O 5 HOH 34  234 53  HOH HOH C . 
O 5 HOH 35  235 4   HOH HOH C . 
O 5 HOH 36  236 132 HOH HOH C . 
O 5 HOH 37  237 40  HOH HOH C . 
O 5 HOH 38  238 43  HOH HOH C . 
O 5 HOH 39  239 102 HOH HOH C . 
O 5 HOH 40  240 122 HOH HOH C . 
O 5 HOH 41  241 48  HOH HOH C . 
O 5 HOH 42  242 148 HOH HOH C . 
O 5 HOH 43  243 56  HOH HOH C . 
O 5 HOH 44  244 189 HOH HOH C . 
O 5 HOH 45  245 295 HOH HOH C . 
O 5 HOH 46  246 62  HOH HOH C . 
O 5 HOH 47  247 226 HOH HOH C . 
O 5 HOH 48  248 298 HOH HOH C . 
O 5 HOH 49  249 299 HOH HOH C . 
O 5 HOH 50  250 367 HOH HOH C . 
O 5 HOH 51  251 317 HOH HOH C . 
O 5 HOH 52  252 135 HOH HOH C . 
O 5 HOH 53  253 171 HOH HOH C . 
O 5 HOH 54  254 364 HOH HOH C . 
O 5 HOH 55  255 305 HOH HOH C . 
O 5 HOH 56  256 65  HOH HOH C . 
O 5 HOH 57  257 348 HOH HOH C . 
O 5 HOH 58  258 146 HOH HOH C . 
O 5 HOH 59  259 149 HOH HOH C . 
O 5 HOH 60  260 246 HOH HOH C . 
O 5 HOH 61  261 108 HOH HOH C . 
O 5 HOH 62  262 355 HOH HOH C . 
O 5 HOH 63  263 241 HOH HOH C . 
O 5 HOH 64  264 151 HOH HOH C . 
O 5 HOH 65  265 349 HOH HOH C . 
O 5 HOH 66  266 70  HOH HOH C . 
O 5 HOH 67  267 270 HOH HOH C . 
O 5 HOH 68  268 130 HOH HOH C . 
O 5 HOH 69  269 330 HOH HOH C . 
O 5 HOH 70  270 324 HOH HOH C . 
O 5 HOH 71  271 341 HOH HOH C . 
O 5 HOH 72  272 310 HOH HOH C . 
O 5 HOH 73  273 103 HOH HOH C . 
O 5 HOH 74  274 356 HOH HOH C . 
O 5 HOH 75  275 92  HOH HOH C . 
O 5 HOH 76  276 357 HOH HOH C . 
O 5 HOH 77  277 363 HOH HOH C . 
O 5 HOH 78  278 206 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
2  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
3  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
4  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
5  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
6  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
7  1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
8  1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
9  1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
10 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
11 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
12 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
13 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
14 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
15 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
16 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
17 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
18 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
19 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
20 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
21 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
22 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
23 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
24 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
25 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
26 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
27 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
28 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
29 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
30 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
31 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
32 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
33 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
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  
54 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
55 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGY 
_cell.length_a           41.691 
_cell.length_b           42.206 
_cell.length_c           159.159 
_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                         7HGY 
_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          7HGY 
_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                     7HGY 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             40.80 
_reflns.d_resolution_high            1.61 
_reflns.number_obs                   37156 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            0.078 
_reflns.pdbx_netI_over_sigmaI        9.2 
_reflns.pdbx_redundancy              4.2 
_reflns.pdbx_Rrim_I_all              0.090 
_reflns.pdbx_Rpim_I_all              0.043 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     154341 
_reflns.pdbx_chi_squared             0.88 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.61 
_reflns_shell.d_res_low                   1.69 
_reflns_shell.number_measured_all         18062 
_reflns_shell.number_unique_obs           5296 
_reflns_shell.Rmerge_I_obs                1.070 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.percent_possible_obs        98.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.255 
_reflns_shell.pdbx_Rpim_I_all             0.639 
_reflns_shell.pdbx_CC_half                0.467 
_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                                 7HGY 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     35139 
_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                             40.83 
_refine.ls_d_res_high                            1.61 
_refine.ls_percent_reflns_obs                    98.77 
_refine.ls_R_factor_obs                          0.20722 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20505 
_refine.ls_R_factor_R_free                       0.24560 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1936 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               42.444 
_refine.aniso_B[1][1]                            0.73 
_refine.aniso_B[2][2]                            -0.16 
_refine.aniso_B[3][3]                            -0.57 
_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                       0.105 
_refine.pdbx_overall_ESU_R_Free                  0.107 
_refine.overall_SU_ML                            0.091 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.762 
_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        2137 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             269 
_refine_hist.number_atoms_total               2456 
_refine_hist.d_res_high                       1.61 
_refine_hist.d_res_low                        40.83 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.009  0.012  ? 2288 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.776  1.832  ? 3113 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.025  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.845  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.369 10.000 ? 306  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.129  0.200  ? 287  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1902 '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                  3.677  3.997  ? 1073 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.809  7.146  ? 1333 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.004  4.310  ? 1215 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.793  59.03  ? 3572 '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                       1.608 
_refine_ls_shell.d_res_low                        1.649 
_refine_ls_shell.number_reflns_R_work             2570 
_refine_ls_shell.R_factor_R_work                  0.328 
_refine_ls_shell.percent_reflns_obs               98.89 
_refine_ls_shell.R_factor_R_free                  0.403 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             108 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGY 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z285782452' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGY 
_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 4 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGY A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGY B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGY 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 7HGY GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGY SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGY GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGY SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGY GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGY 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,H,M 
2 1 B,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 ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O ALA C 52 ? O ALA C 51 N ILE C 43 ? N ILE C 42 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGY 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 217 ? ? O B HOH 264 ? ? 1.50 
2  1 O   C HOH 205 ? ? O C HOH 216 ? ? 1.59 
3  1 O   C HOH 206 ? ? O C HOH 267 ? ? 1.84 
4  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 1.89 
5  1 OH  C TYR 40  ? ? O C HOH 202 ? ? 1.93 
6  1 CE  A LYS 39  ? ? O A HOH 282 ? ? 1.99 
7  1 O   C HOH 258 ? ? O C HOH 270 ? ? 2.04 
8  1 O   A HOH 232 ? ? O A HOH 300 ? ? 2.05 
9  1 O   A HOH 300 ? ? O A HOH 305 ? ? 2.06 
10 1 OD1 C ASP 9   ? ? O C HOH 203 ? ? 2.10 
11 1 O   B HOH 256 ? ? O B HOH 261 ? ? 2.12 
12 1 OE1 A GLN 85  ? ? O A HOH 201 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 231 ? ? 1_555 O A HOH 266 ? ? 4_545 2.17 
2 1 O A HOH 236 ? ? 1_555 O C HOH 271 ? ? 4_445 2.18 
# 
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 ? ? -151.37 66.37  
2 1 ASN B 87 ? ? -159.77 61.15  
3 1 ALA C 4  ? ? -171.94 122.96 
4 1 ASN C 87 ? ? -141.94 52.19  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 B VAL 33 ? B VAL 34 
9  1 Y 1 C GLY 0  ? C GLY 1  
10 1 Y 1 C MET 1  ? C MET 2  
11 1 Y 1 C PRO 2  ? C PRO 3  
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 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 
UVA C4   C Y N 387 
UVA C5   C Y N 388 
UVA C6   C Y N 389 
UVA C7   C N N 390 
UVA N    N N N 391 
UVA C    C N N 392 
UVA O    O N N 393 
UVA C1   C Y N 394 
UVA C2   C Y N 395 
UVA C3   C Y N 396 
UVA O1   O N N 397 
UVA S    S N N 398 
UVA H1   H N N 399 
UVA H2   H N N 400 
UVA H3   H N N 401 
UVA H4   H N N 402 
UVA H5   H N N 403 
UVA H6   H N N 404 
UVA H7   H N N 405 
UVA H8   H N N 406 
UVA H9   H N N 407 
UVA H10  H N N 408 
UVA H11  H N N 409 
VAL N    N N N 410 
VAL CA   C N S 411 
VAL C    C N N 412 
VAL O    O N N 413 
VAL CB   C N N 414 
VAL CG1  C N N 415 
VAL CG2  C N N 416 
VAL OXT  O N N 417 
VAL H    H N N 418 
VAL H2   H N N 419 
VAL HA   H N N 420 
VAL HB   H N N 421 
VAL HG11 H N N 422 
VAL HG12 H N N 423 
VAL HG13 H N N 424 
VAL HG21 H N N 425 
VAL HG22 H N N 426 
VAL HG23 H N N 427 
VAL HXT  H N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
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 
UVA C4  C5   doub Y N 371 
UVA C4  C3   sing Y N 372 
UVA C5  C6   sing Y N 373 
UVA O   S    doub N N 374 
UVA C3  C2   doub Y N 375 
UVA C6  S    sing N N 376 
UVA C6  C1   doub Y N 377 
UVA S   O1   doub N N 378 
UVA S   C7   sing N N 379 
UVA C2  C1   sing Y N 380 
UVA C1  N    sing N N 381 
UVA N   C    sing N N 382 
UVA C4  H1   sing N N 383 
UVA C5  H2   sing N N 384 
UVA C7  H3   sing N N 385 
UVA C7  H4   sing N N 386 
UVA C7  H5   sing N N 387 
UVA N   H6   sing N N 388 
UVA C   H7   sing N N 389 
UVA C   H8   sing N N 390 
UVA C   H9   sing N N 391 
UVA C2  H10  sing N N 392 
UVA C3  H11  sing N N 393 
VAL N   CA   sing N N 394 
VAL N   H    sing N N 395 
VAL N   H2   sing N N 396 
VAL CA  C    sing N N 397 
VAL CA  CB   sing N N 398 
VAL CA  HA   sing N N 399 
VAL C   O    doub N N 400 
VAL C   OXT  sing N N 401 
VAL CB  CG1  sing N N 402 
VAL CB  CG2  sing N N 403 
VAL CB  HB   sing N N 404 
VAL CG1 HG11 sing N N 405 
VAL CG1 HG12 sing N N 406 
VAL CG1 HG13 sing N N 407 
VAL CG2 HG21 sing N N 408 
VAL CG2 HG22 sing N N 409 
VAL CG2 HG23 sing N N 410 
VAL OXT HXT  sing N N 411 
# 
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                    7HGY 
_atom_sites.fract_transf_matrix[1][1]   0.023986 
_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]   0.023693 
_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]   0.006283 
_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  ? 1.241   4.287   2.457   1.00 54.57  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? 0.140   3.524   1.811   1.00 54.90  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.732   2.472   0.876   1.00 52.56  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.837   2.647   0.371   1.00 53.21  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -0.820  4.449   1.053   1.00 61.52  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -1.794  5.203   1.948   1.00 74.17  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.160  4.281   2.699   1.00 72.99  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.593  5.430   4.016   1.00 71.22  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? 0.029   1.339   0.633   1.00 45.03  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.549   0.243   -0.194  1.00 44.53  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.683   0.566   -1.682  1.00 45.44  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.028  1.410   -2.221  1.00 44.32  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -0.548  -0.851  0.030   1.00 47.41  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.198  -0.459  1.358   1.00 49.94  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.306  1.046   1.184   1.00 45.97  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.595   -0.150  -2.339  1.00 43.23  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.822   -0.029  -3.768  1.00 42.27  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 1.225   -1.293  -4.379  1.00 39.27  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.735   -2.141  -3.637  1.00 41.18  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.336   0.057   -4.026  1.00 50.12  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.961   1.364   -3.631  1.00 65.61  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 4.096   1.793   -2.327  1.00 68.82  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.460   2.358   -4.391  1.00 72.53  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.661   2.996   -2.312  1.00 73.49  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.896   3.358   -3.552  1.00 69.78  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.225   -1.408  -5.706  1.00 35.93  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 1.037   -2.712  -6.330  1.00 34.86  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 2.161   -3.656  -5.917  1.00 31.95  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.245   -3.196  -5.530  1.00 33.23  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 1.021   -2.560  -7.833  1.00 39.24  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.900   -4.959  -6.062  1.00 31.03  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.939   -5.970  -5.896  1.00 32.97  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 4.050   -5.760  -6.933  1.00 34.65  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.786   -5.357  -8.077  1.00 32.51  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.403   -7.399  -5.968  1.00 33.40  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.607   -7.774  -4.724  1.00 33.71  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 2.264   -8.007  -3.509  1.00 29.83  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? 0.211   -7.866  -4.754  1.00 33.44  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.565   -8.302  -2.337  1.00 30.20  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.471  -8.272  -3.593  1.00 29.34  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? 0.175   -8.429  -2.401  1.00 29.24  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 5.287   -6.044  -6.492  1.00 30.15  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.480   -5.969  -7.327  1.00 31.03  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.387   -7.168  -7.011  1.00 28.89  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.347   -7.758  -5.922  1.00 28.50  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 7.180   -4.628  -7.077  1.00 32.84  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.859   -4.551  -5.737  1.00 35.20  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.513   -3.194  -5.438  1.00 41.85  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 9.097   -3.173  -4.046  1.00 42.32  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 8.087   -3.183  -2.967  1.00 44.12  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 8.265   -7.550  -7.950  1.00 30.78  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 9.208   -8.646  -7.725  1.00 29.92  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.980   -8.352  -6.437  1.00 28.18  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.452  -7.231  -6.193  1.00 29.37  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 10.119  -8.530  -8.996  1.00 29.72  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 9.157   -7.971  -10.052 1.00 33.14  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.378   -6.930  -9.291  1.00 35.94  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 10.160  -9.401  -5.632  1.00 26.86  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.876  -9.282  -4.385  1.00 27.04  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.939   -9.180  -3.197  1.00 28.97  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.329  -9.481  -2.068  1.00 28.28  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.677   -8.783  -3.438  1.00 25.03  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.802   -8.751  -2.271  1.00 23.96  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.601   -10.134 -1.649  1.00 23.71  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.410   -11.112 -2.373  1.00 26.20  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.449   -8.157  -2.658  1.00 24.95  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.434   -6.658  -2.888  1.00 29.35  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.402   -5.958  -2.454  1.00 30.33  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.460   -6.199  -3.532  1.00 27.41  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.487   -10.165 -0.310  1.00 25.86  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 7.283   -11.407 0.424   1.00 24.56  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.802   -11.504 0.822   1.00 24.99  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 5.214   -10.499 1.258   1.00 26.07  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 8.243   -11.456 1.631   1.00 23.58  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.718   -11.262 1.251   1.00 25.05  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.571  -11.392 2.552   1.00 27.24  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 10.162  -12.261 0.204   1.00 26.21  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 5.247   -12.721 0.708   1.00 24.57  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.798   -12.903 0.926   1.00 25.09  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.527   -14.268 1.543   1.00 28.99  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.374   -15.163 1.548   1.00 25.56  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 3.021   -12.805 -0.406  1.00 25.25  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 3.155   -11.427 -1.074  1.00 25.90  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.426   -13.906 -1.383  1.00 25.63  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.297   -14.458 2.060   1.00 25.28  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.786   -15.815 2.037   1.00 26.20  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.817   -15.920 0.860   1.00 28.85  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? 0.023   -15.004 0.659   1.00 26.25  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.993   -16.152 3.325   1.00 26.22  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.955   -16.263 4.511   1.00 26.64  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 2.281   -15.127 5.251   1.00 27.73  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.504   -17.491 4.874   1.00 30.08  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 3.214   -15.201 6.297   1.00 32.51  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.434   -17.565 5.917   1.00 29.18  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.752   -16.433 6.632   1.00 31.16  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.887   -17.035 0.112   1.00 26.30  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? 0.103   -17.148 -1.107  1.00 28.02  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -0.879  -18.295 -0.922  1.00 29.53  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.498  -19.349 -0.383  1.00 30.14  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.995   -17.295 -2.349  1.00 27.60  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.144  -18.070 -1.352  1.00 28.72  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.186  -19.054 -1.097  1.00 29.02  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.503  -19.775 -2.403  1.00 30.84  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -3.854  -19.130 -3.387  1.00 34.00  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.418  -18.383 -0.461  1.00 28.71  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.499  -19.395 0.043   1.00 36.69  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.064  -20.358 1.154   1.00 33.89  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.244  -21.133 1.761   1.00 36.96  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.490  -22.260 0.868   1.00 39.08  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.475  -21.115 -2.329  1.00 33.42  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -3.995  -21.976 -3.380  1.00 34.56  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.052  -22.885 -2.742  1.00 41.52  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -4.910  -23.296 -1.591  1.00 35.24  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -2.894  -22.933 -3.853  1.00 35.59  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.534  -22.322 -4.149  1.00 43.89  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.538  -21.813 -5.879  1.00 45.96  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.142  -23.365 -6.641  1.00 38.65  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.076  -23.236 -3.518  1.00 43.09  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.110  -24.146 -3.039  1.00 46.02  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.486  -25.432 -2.535  1.00 42.01  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.617  -26.016 -3.174  1.00 42.86  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.089  -24.540 -4.150  1.00 59.72  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.323  -23.658 -4.200  1.00 65.94  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.527 -24.424 -4.737  1.00 75.55  ? 16  LYS A CD  1 
ATOM   125  C CE  . LYS A 1 17 ? -11.802 -23.656 -4.574  1.00 84.42  ? 16  LYS A CE  1 
ATOM   126  N NZ  . LYS A 1 17 ? -12.973 -24.422 -5.017  1.00 77.92  ? 16  LYS A NZ  1 
ATOM   127  N N   . GLY A 1 18 ? -6.939  -25.863 -1.355  1.00 46.63  ? 17  GLY A N   1 
ATOM   128  C CA  . GLY A 1 18 ? -6.523  -27.143 -0.839  1.00 42.63  ? 17  GLY A CA  1 
ATOM   129  C C   . GLY A 1 18 ? -5.207  -27.046 -0.079  1.00 49.98  ? 17  GLY A C   1 
ATOM   130  O O   . GLY A 1 18 ? -4.769  -28.016 0.523   1.00 49.80  ? 17  GLY A O   1 
ATOM   131  N N   . TYR A 1 19 ? -4.579  -25.863 -0.100  1.00 43.25  ? 18  TYR A N   1 
ATOM   132  C CA  . TYR A 1 19 ? -3.323  -25.726 0.599   1.00 37.43  ? 18  TYR A CA  1 
ATOM   133  C C   . TYR A 1 19 ? -3.443  -24.616 1.631   1.00 35.35  ? 18  TYR A C   1 
ATOM   134  O O   . TYR A 1 19 ? -4.170  -23.645 1.439   1.00 34.56  ? 18  TYR A O   1 
ATOM   135  C CB  . TYR A 1 19 ? -2.209  -25.310 -0.366  1.00 40.52  ? 18  TYR A CB  1 
ATOM   136  C CG  . TYR A 1 19 ? -1.806  -26.311 -1.442  1.00 47.87  ? 18  TYR A CG  1 
ATOM   137  C CD1 . TYR A 1 19 ? -0.733  -27.176 -1.248  1.00 61.61  ? 18  TYR A CD1 1 
ATOM   138  C CD2 . TYR A 1 19 ? -2.475  -26.376 -2.662  1.00 50.96  ? 18  TYR A CD2 1 
ATOM   139  C CE1 . TYR A 1 19 ? -0.354  -28.085 -2.229  1.00 63.18  ? 18  TYR A CE1 1 
ATOM   140  C CE2 . TYR A 1 19 ? -2.103  -27.277 -3.656  1.00 50.96  ? 18  TYR A CE2 1 
ATOM   141  C CZ  . TYR A 1 19 ? -1.033  -28.127 -3.437  1.00 60.41  ? 18  TYR A CZ  1 
ATOM   142  O OH  . TYR A 1 19 ? -0.669  -29.022 -4.411  1.00 72.22  ? 18  TYR A OH  1 
ATOM   143  N N   . PRO A 1 20 ? -2.675  -24.702 2.728   1.00 34.41  ? 19  PRO A N   1 
ATOM   144  C CA  . PRO A 1 20 ? -2.601  -23.625 3.720   1.00 35.02  ? 19  PRO A CA  1 
ATOM   145  C C   . PRO A 1 20 ? -1.904  -22.425 3.069   1.00 34.30  ? 19  PRO A C   1 
ATOM   146  O O   . PRO A 1 20 ? -1.150  -22.622 2.143   1.00 36.14  ? 19  PRO A O   1 
ATOM   147  C CB  . PRO A 1 20 ? -1.736  -24.257 4.816   1.00 40.51  ? 19  PRO A CB  1 
ATOM   148  C CG  . PRO A 1 20 ? -0.861  -25.238 4.055   1.00 41.92  ? 19  PRO A CG  1 
ATOM   149  C CD  . PRO A 1 20 ? -1.788  -25.844 3.019   1.00 40.60  ? 19  PRO A CD  1 
ATOM   150  N N   . HIS A 1 21 ? -2.195  -21.214 3.552   1.00 31.13  ? 20  HIS A N   1 
ATOM   151  C CA  . HIS A 1 21 ? -1.493  -20.003 3.139   1.00 29.39  ? 20  HIS A CA  1 
ATOM   152  C C   . HIS A 1 21 ? 0.008   -20.255 3.265   1.00 33.29  ? 20  HIS A C   1 
ATOM   153  O O   . HIS A 1 21 ? 0.462   -20.680 4.329   1.00 29.64  ? 20  HIS A O   1 
ATOM   154  C CB  . HIS A 1 21 ? -1.928  -18.833 4.018   1.00 33.00  ? 20  HIS A CB  1 
ATOM   155  C CG  . HIS A 1 21 ? -3.373  -18.441 3.829   1.00 31.32  ? 20  HIS A CG  1 
ATOM   156  N ND1 . HIS A 1 21 ? -4.406  -19.121 4.453   1.00 34.01  ? 20  HIS A ND1 1 
ATOM   157  C CD2 . HIS A 1 21 ? -3.929  -17.436 3.125   1.00 32.84  ? 20  HIS A CD2 1 
ATOM   158  C CE1 . HIS A 1 21 ? -5.553  -18.517 4.164   1.00 35.41  ? 20  HIS A CE1 1 
ATOM   159  N NE2 . HIS A 1 21 ? -5.313  -17.496 3.343   1.00 33.40  ? 20  HIS A NE2 1 
ATOM   160  N N   . TRP A 1 22 ? 0.748   -20.012 2.162   1.00 29.39  ? 21  TRP A N   1 
ATOM   161  C CA  . TRP A 1 22 ? 2.069   -20.626 2.002   1.00 28.02  ? 21  TRP A CA  1 
ATOM   162  C C   . TRP A 1 22 ? 3.157   -19.552 1.859   1.00 27.84  ? 21  TRP A C   1 
ATOM   163  O O   . TRP A 1 22 ? 3.007   -18.654 1.058   1.00 27.78  ? 21  TRP A O   1 
ATOM   164  C CB  . TRP A 1 22 ? 2.064   -21.540 0.775   1.00 30.66  ? 21  TRP A CB  1 
ATOM   165  C CG  . TRP A 1 22 ? 3.181   -22.556 0.801   1.00 31.54  ? 21  TRP A CG  1 
ATOM   166  C CD1 . TRP A 1 22 ? 4.524   -22.366 0.588   1.00 29.48  ? 21  TRP A CD1 1 
ATOM   167  C CD2 . TRP A 1 22 ? 3.007   -23.959 1.093   1.00 32.01  ? 21  TRP A CD2 1 
ATOM   168  N NE1 . TRP A 1 22 ? 5.186   -23.573 0.712   1.00 31.71  ? 21  TRP A NE1 1 
ATOM   169  C CE2 . TRP A 1 22 ? 4.283   -24.562 1.009   1.00 33.31  ? 21  TRP A CE2 1 
ATOM   170  C CE3 . TRP A 1 22 ? 1.889   -24.753 1.399   1.00 38.09  ? 21  TRP A CE3 1 
ATOM   171  C CZ2 . TRP A 1 22 ? 4.485   -25.926 1.250   1.00 43.52  ? 21  TRP A CZ2 1 
ATOM   172  C CZ3 . TRP A 1 22 ? 2.097   -26.103 1.620   1.00 38.78  ? 21  TRP A CZ3 1 
ATOM   173  C CH2 . TRP A 1 22 ? 3.375   -26.681 1.539   1.00 43.35  ? 21  TRP A CH2 1 
ATOM   174  N N   . PRO A 1 23 ? 4.308   -19.625 2.575   1.00 26.70  ? 22  PRO A N   1 
ATOM   175  C CA  . PRO A 1 23 ? 5.371   -18.620 2.410   1.00 26.46  ? 22  PRO A CA  1 
ATOM   176  C C   . PRO A 1 23 ? 5.905   -18.572 0.970   1.00 26.05  ? 22  PRO A C   1 
ATOM   177  O O   . PRO A 1 23 ? 6.215   -19.604 0.370   1.00 25.96  ? 22  PRO A O   1 
ATOM   178  C CB  . PRO A 1 23 ? 6.450   -19.110 3.421   1.00 27.29  ? 22  PRO A CB  1 
ATOM   179  C CG  . PRO A 1 23 ? 6.192   -20.597 3.575   1.00 27.83  ? 22  PRO A CG  1 
ATOM   180  C CD  . PRO A 1 23 ? 4.654   -20.669 3.553   1.00 26.68  ? 22  PRO A CD  1 
ATOM   181  N N   . ALA A 1 24 ? 5.937   -17.372 0.397   1.00 24.45  ? 23  ALA A N   1 
ATOM   182  C CA  . ALA A 1 24 ? 6.243   -17.252 -1.023  1.00 25.62  ? 23  ALA A CA  1 
ATOM   183  C C   . ALA A 1 24 ? 6.787   -15.859 -1.328  1.00 23.20  ? 23  ALA A C   1 
ATOM   184  O O   . ALA A 1 24 ? 6.773   -14.987 -0.456  1.00 23.96  ? 23  ALA A O   1 
ATOM   185  C CB  . ALA A 1 24 ? 4.985   -17.590 -1.846  1.00 24.99  ? 23  ALA A CB  1 
ATOM   186  N N   . ARG A 1 25 ? 7.332   -15.670 -2.538  1.00 24.24  ? 24  ARG A N   1 
ATOM   187  C CA  . ARG A 1 25 ? 7.710   -14.334 -2.970  1.00 24.61  ? 24  ARG A CA  1 
ATOM   188  C C   . ARG A 1 25 ? 7.193   -14.075 -4.389  1.00 24.84  ? 24  ARG A C   1 
ATOM   189  O O   . ARG A 1 25 ? 6.928   -15.017 -5.154  1.00 26.47  ? 24  ARG A O   1 
ATOM   190  C CB  . ARG A 1 25 ? 9.242   -14.205 -2.917  1.00 27.41  ? 24  ARG A CB  1 
ATOM   191  C CG  . ARG A 1 25 ? 9.910   -15.085 -3.966  1.00 27.38  ? 24  ARG A CG  1 
ATOM   192  C CD  . ARG A 1 25 ? 11.458  -14.917 -3.817  1.00 25.75  ? 24  ARG A CD  1 
ATOM   193  N NE  . ARG A 1 25 ? 12.152  -15.712 -4.851  1.00 25.81  ? 24  ARG A NE  1 
ATOM   194  C CZ  . ARG A 1 25 ? 13.443  -16.118 -4.768  1.00 27.29  ? 24  ARG A CZ  1 
ATOM   195  N NH1 . ARG A 1 25 ? 14.141  -16.014 -3.630  1.00 28.49  ? 24  ARG A NH1 1 
ATOM   196  N NH2 . ARG A 1 25 ? 13.985  -16.742 -5.818  1.00 29.42  ? 24  ARG A NH2 1 
ATOM   197  N N   . ILE A 1 26 ? 7.076   -12.801 -4.734  1.00 25.91  ? 25  ILE A N   1 
ATOM   198  C CA  . ILE A 1 26 ? 6.848   -12.418 -6.129  1.00 24.40  ? 25  ILE A CA  1 
ATOM   199  C C   . ILE A 1 26 ? 8.176   -12.530 -6.855  1.00 28.23  ? 25  ILE A C   1 
ATOM   200  O O   . ILE A 1 26 ? 9.122   -11.863 -6.455  1.00 28.50  ? 25  ILE A O   1 
ATOM   201  C CB  . ILE A 1 26 ? 6.344   -10.968 -6.250  1.00 25.52  ? 25  ILE A CB  1 
ATOM   202  C CG1 . ILE A 1 26 ? 5.180   -10.628 -5.269  1.00 30.85  ? 25  ILE A CG1 1 
ATOM   203  C CG2 . ILE A 1 26 ? 5.965   -10.639 -7.715  1.00 25.98  ? 25  ILE A CG2 1 
ATOM   204  C CD1 . ILE A 1 26 ? 3.854   -11.274 -5.592  1.00 38.07  ? 25  ILE A CD1 1 
ATOM   205  N N   . ASP A 1 27 ? 8.225   -13.397 -7.871  1.00 29.10  ? 26  ASP A N   1 
ATOM   206  C CA  . ASP A 1 27 ? 9.447   -13.559 -8.643  1.00 30.46  ? 26  ASP A CA  1 
ATOM   207  C C   . ASP A 1 27 ? 9.566   -12.542 -9.765  1.00 33.51  ? 26  ASP A C   1 
ATOM   208  O O   . ASP A 1 27 ? 8.594   -11.922 -10.198 1.00 31.32  ? 26  ASP A O   1 
ATOM   209  C CB  . ASP A 1 27 ? 9.515   -14.943 -9.247  1.00 28.77  ? 26  ASP A CB  1 
ATOM   210  C CG  . ASP A 1 27 ? 10.521  -15.881 -8.588  1.00 31.20  ? 26  ASP A CG  1 
ATOM   211  O OD1 . ASP A 1 27 ? 11.150  -15.477 -7.575  1.00 35.35  ? 26  ASP A OD1 1 
ATOM   212  O OD2 . ASP A 1 27 ? 10.656  -16.999 -9.069  1.00 31.98  ? 26  ASP A OD2 1 
ATOM   213  N N   . ASP A 1 28 ? 10.822  -12.361 -10.237 1.00 35.45  ? 27  ASP A N   1 
ATOM   214  C CA  . ASP A 1 28 ? 11.046  -11.672 -11.493 1.00 35.93  ? 27  ASP A CA  1 
ATOM   215  C C   . ASP A 1 28 ? 10.731  -12.657 -12.622 1.00 33.35  ? 27  ASP A C   1 
ATOM   216  O O   . ASP A 1 28 ? 10.572  -13.855 -12.395 1.00 35.97  ? 27  ASP A O   1 
ATOM   217  C CB  . ASP A 1 28 ? 12.494  -11.216 -11.619 1.00 42.90  ? 27  ASP A CB  1 
ATOM   218  C CG  . ASP A 1 28 ? 12.813  -9.842  -11.036 1.00 47.26  ? 27  ASP A CG  1 
ATOM   219  O OD1 . ASP A 1 28 ? 12.377  -8.826  -11.620 1.00 53.53  ? 27  ASP A OD1 1 
ATOM   220  O OD2 . ASP A 1 28 ? 13.488  -9.801  -9.988  1.00 54.60  ? 27  ASP A OD2 1 
ATOM   221  N N   . ILE A 1 29 ? 10.636  -12.149 -13.837 1.00 35.83  ? 28  ILE A N   1 
ATOM   222  C CA  . ILE A 1 29 ? 10.608  -13.038 -14.990 1.00 35.67  ? 28  ILE A CA  1 
ATOM   223  C C   . ILE A 1 29 ? 11.929  -12.811 -15.732 1.00 33.21  ? 28  ILE A C   1 
ATOM   224  O O   . ILE A 1 29 ? 12.238  -11.666 -16.026 1.00 37.24  ? 28  ILE A O   1 
ATOM   225  C CB  . ILE A 1 29 ? 9.404   -12.653 -15.869 1.00 39.23  ? 28  ILE A CB  1 
ATOM   226  C CG1 . ILE A 1 29 ? 8.062   -12.736 -15.092 1.00 37.20  ? 28  ILE A CG1 1 
ATOM   227  C CG2 . ILE A 1 29 ? 9.397   -13.482 -17.156 1.00 35.44  ? 28  ILE A CG2 1 
ATOM   228  C CD1 . ILE A 1 29 ? 7.027   -11.744 -15.588 1.00 40.02  ? 28  ILE A CD1 1 
ATOM   229  N N   . ALA A 1 30 ? 12.706  -13.891 -15.934 1.00 34.41  ? 29  ALA A N   1 
ATOM   230  C CA  . ALA A 1 30 ? 13.968  -13.820 -16.664 1.00 38.15  ? 29  ALA A CA  1 
ATOM   231  C C   . ALA A 1 30 ? 13.699  -13.472 -18.133 1.00 35.12  ? 29  ALA A C   1 
ATOM   232  O O   . ALA A 1 30 ? 12.637  -13.758 -18.687 1.00 34.30  ? 29  ALA A O   1 
ATOM   233  C CB  . ALA A 1 30 ? 14.707  -15.137 -16.542 1.00 37.61  ? 29  ALA A CB  1 
ATOM   234  N N   . ASP A 1 31 ? 14.653  -12.769 -18.761 1.00 35.44  ? 30  ASP A N   1 
ATOM   235  C CA  . ASP A 1 31 ? 14.621  -12.659 -20.222 1.00 30.80  ? 30  ASP A CA  1 
ATOM   236  C C   . ASP A 1 31 ? 14.419  -14.042 -20.820 1.00 29.42  ? 30  ASP A C   1 
ATOM   237  O O   . ASP A 1 31 ? 15.088  -14.985 -20.424 1.00 34.65  ? 30  ASP A O   1 
ATOM   238  C CB  . ASP A 1 31 ? 15.955  -12.067 -20.678 1.00 33.12  ? 30  ASP A CB  1 
ATOM   239  C CG  . ASP A 1 31 ? 16.094  -10.567 -20.488 1.00 35.39  ? 30  ASP A CG  1 
ATOM   240  O OD1 . ASP A 1 31 ? 15.061  -9.908  -20.367 1.00 37.49  ? 30  ASP A OD1 1 
ATOM   241  O OD2 . ASP A 1 31 ? 17.257  -10.078 -20.458 1.00 36.63  ? 30  ASP A OD2 1 
ATOM   242  N N   . GLY A 1 32 ? 13.473  -14.123 -21.771 1.00 33.06  ? 31  GLY A N   1 
ATOM   243  C CA  . GLY A 1 32 ? 13.235  -15.318 -22.570 1.00 32.27  ? 31  GLY A CA  1 
ATOM   244  C C   . GLY A 1 32 ? 12.347  -16.347 -21.877 1.00 37.06  ? 31  GLY A C   1 
ATOM   245  O O   . GLY A 1 32 ? 12.027  -17.366 -22.475 1.00 37.81  ? 31  GLY A O   1 
ATOM   246  N N   . ALA A 1 33 ? 12.009  -16.107 -20.604 1.00 37.54  ? 32  ALA A N   1 
ATOM   247  C CA  . ALA A 1 33 ? 11.167  -17.036 -19.857 1.00 35.89  ? 32  ALA A CA  1 
ATOM   248  C C   . ALA A 1 33 ? 9.679   -16.751 -20.122 1.00 34.97  ? 32  ALA A C   1 
ATOM   249  O O   . ALA A 1 33 ? 9.277   -15.648 -20.519 1.00 35.73  ? 32  ALA A O   1 
ATOM   250  C CB  . ALA A 1 33 ? 11.513  -16.896 -18.373 1.00 36.47  ? 32  ALA A CB  1 
ATOM   251  N N   . VAL A 1 34 ? 8.859   -17.784 -19.857 1.00 38.46  ? 33  VAL A N   1 
ATOM   252  C CA  . VAL A 1 34 ? 7.409   -17.720 -19.969 1.00 39.09  ? 33  VAL A CA  1 
ATOM   253  C C   . VAL A 1 34 ? 6.838   -16.672 -19.019 1.00 36.81  ? 33  VAL A C   1 
ATOM   254  O O   . VAL A 1 34 ? 7.148   -16.687 -17.834 1.00 39.42  ? 33  VAL A O   1 
ATOM   255  C CB  . VAL A 1 34 ? 6.860   -19.116 -19.615 1.00 38.80  ? 33  VAL A CB  1 
ATOM   256  C CG1 . VAL A 1 34 ? 5.334   -19.097 -19.568 1.00 39.75  ? 33  VAL A CG1 1 
ATOM   257  C CG2 . VAL A 1 34 ? 7.368   -20.171 -20.608 1.00 40.81  ? 33  VAL A CG2 1 
ATOM   258  N N   . LYS A 1 35 ? 6.006   -15.784 -19.567 1.00 39.26  ? 34  LYS A N   1 
ATOM   259  C CA  . LYS A 1 35 ? 5.378   -14.690 -18.837 1.00 38.83  ? 34  LYS A CA  1 
ATOM   260  C C   . LYS A 1 35 ? 4.064   -15.162 -18.213 1.00 40.45  ? 34  LYS A C   1 
ATOM   261  O O   . LYS A 1 35 ? 3.450   -16.113 -18.689 1.00 39.23  ? 34  LYS A O   1 
ATOM   262  C CB  . LYS A 1 35 ? 5.099   -13.506 -19.763 1.00 42.33  ? 34  LYS A CB  1 
ATOM   263  C CG  . LYS A 1 35 ? 6.361   -12.788 -20.230 1.00 41.59  ? 34  LYS A CG  1 
ATOM   264  C CD  . LYS A 1 35 ? 6.100   -11.535 -21.065 1.00 50.26  ? 34  LYS A CD  1 
ATOM   265  C CE  . LYS A 1 35 ? 5.468   -11.957 -22.357 1.00 44.49  ? 34  LYS A CE  1 
ATOM   266  N NZ  . LYS A 1 35 ? 5.406   -10.851 -23.304 1.00 45.17  ? 34  LYS A NZ  1 
ATOM   267  N N   . PRO A 1 36 ? 3.586   -14.538 -17.112 1.00 41.94  ? 35  PRO A N   1 
ATOM   268  C CA  . PRO A 1 36 ? 2.332   -14.990 -16.494 1.00 40.10  ? 35  PRO A CA  1 
ATOM   269  C C   . PRO A 1 36 ? 1.183   -14.514 -17.364 1.00 40.25  ? 35  PRO A C   1 
ATOM   270  O O   . PRO A 1 36 ? 1.335   -13.579 -18.148 1.00 40.42  ? 35  PRO A O   1 
ATOM   271  C CB  . PRO A 1 36 ? 2.260   -14.318 -15.105 1.00 40.26  ? 35  PRO A CB  1 
ATOM   272  C CG  . PRO A 1 36 ? 3.353   -13.237 -15.144 1.00 50.46  ? 35  PRO A CG  1 
ATOM   273  C CD  . PRO A 1 36 ? 4.151   -13.342 -16.465 1.00 44.28  ? 35  PRO A CD  1 
ATOM   274  N N   . PRO A 1 37 ? -0.030  -15.065 -17.181 1.00 42.45  ? 36  PRO A N   1 
ATOM   275  C CA  . PRO A 1 37 ? -1.207  -14.459 -17.794 1.00 42.06  ? 36  PRO A CA  1 
ATOM   276  C C   . PRO A 1 37 ? -1.419  -13.029 -17.323 1.00 43.81  ? 36  PRO A C   1 
ATOM   277  O O   . PRO A 1 37 ? -0.870  -12.624 -16.302 1.00 35.98  ? 36  PRO A O   1 
ATOM   278  C CB  . PRO A 1 37 ? -2.356  -15.345 -17.333 1.00 40.35  ? 36  PRO A CB  1 
ATOM   279  C CG  . PRO A 1 37 ? -1.728  -16.654 -16.961 1.00 41.31  ? 36  PRO A CG  1 
ATOM   280  C CD  . PRO A 1 37 ? -0.314  -16.324 -16.474 1.00 39.75  ? 36  PRO A CD  1 
ATOM   281  N N   . PRO A 1 38 ? -2.290  -12.246 -18.007 1.00 41.55  ? 37  PRO A N   1 
ATOM   282  C CA  . PRO A 1 38 ? -2.655  -10.905 -17.558 1.00 42.44  ? 37  PRO A CA  1 
ATOM   283  C C   . PRO A 1 38 ? -3.214  -10.868 -16.139 1.00 38.17  ? 37  PRO A C   1 
ATOM   284  O O   . PRO A 1 38 ? -3.916  -11.791 -15.733 1.00 42.53  ? 37  PRO A O   1 
ATOM   285  C CB  . PRO A 1 38 ? -3.694  -10.380 -18.592 1.00 48.44  ? 37  PRO A CB  1 
ATOM   286  C CG  . PRO A 1 38 ? -3.728  -11.419 -19.679 1.00 44.06  ? 37  PRO A CG  1 
ATOM   287  C CD  . PRO A 1 38 ? -2.924  -12.625 -19.291 1.00 50.61  ? 37  PRO A CD  1 
ATOM   288  N N   . ASN A 1 39 ? -2.833  -9.816  -15.390 1.00 40.24  ? 38  ASN A N   1 
ATOM   289  C CA  . ASN A 1 39 ? -3.274  -9.572  -14.032 1.00 42.39  ? 38  ASN A CA  1 
ATOM   290  C C   . ASN A 1 39 ? -2.799  -10.658 -13.062 1.00 36.50  ? 38  ASN A C   1 
ATOM   291  O O   . ASN A 1 39 ? -3.309  -10.696 -11.940 1.00 37.04  ? 38  ASN A O   1 
ATOM   292  C CB  . ASN A 1 39 ? -4.793  -9.454  -13.967 1.00 50.02  ? 38  ASN A CB  1 
ATOM   293  C CG  . ASN A 1 39 ? -5.261  -8.368  -14.904 1.00 58.60  ? 38  ASN A CG  1 
ATOM   294  O OD1 . ASN A 1 39 ? -5.003  -7.184  -14.649 1.00 58.60  ? 38  ASN A OD1 1 
ATOM   295  N ND2 . ASN A 1 39 ? -5.896  -8.759  -15.998 1.00 61.01  ? 38  ASN A ND2 1 
ATOM   296  N N   . LYS A 1 40 ? -1.878  -11.546 -13.492 1.00 35.56  ? 39  LYS A N   1 
ATOM   297  C CA  . LYS A 1 40 ? -1.307  -12.533 -12.575 1.00 29.10  ? 39  LYS A CA  1 
ATOM   298  C C   . LYS A 1 40 ? 0.205   -12.277 -12.399 1.00 28.30  ? 39  LYS A C   1 
ATOM   299  O O   . LYS A 1 40 ? 0.850   -11.543 -13.177 1.00 32.77  ? 39  LYS A O   1 
ATOM   300  C CB  . LYS A 1 40 ? -1.442  -13.941 -13.151 1.00 31.94  ? 39  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 40 ? -2.848  -14.406 -13.581 1.00 35.56  ? 39  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 40 ? -3.591  -14.767 -12.311 1.00 40.23  ? 39  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 40 ? -5.062  -15.005 -12.611 1.00 49.81  ? 39  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 40 ? -5.331  -16.398 -12.972 1.00 52.29  ? 39  LYS A NZ  1 
ATOM   305  N N   . TYR A 1 41 ? 0.709   -12.793 -11.280 1.00 26.54  ? 40  TYR A N   1 
ATOM   306  C CA  . TYR A 1 41 ? 2.093   -12.634 -10.859 1.00 29.04  ? 40  TYR A CA  1 
ATOM   307  C C   . TYR A 1 41 ? 2.739   -14.003 -10.797 1.00 26.36  ? 40  TYR A C   1 
ATOM   308  O O   . TYR A 1 41 ? 2.129   -15.002 -10.415 1.00 26.81  ? 40  TYR A O   1 
ATOM   309  C CB  . TYR A 1 41 ? 2.151   -12.065 -9.416  1.00 28.36  ? 40  TYR A CB  1 
ATOM   310  C CG  . TYR A 1 41 ? 1.683   -10.617 -9.417  1.00 30.24  ? 40  TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 41 ? 0.323   -10.325 -9.336  1.00 35.13  ? 40  TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 41 ? 2.566   -9.550  -9.591  1.00 30.50  ? 40  TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 41 ? -0.126  -9.017  -9.427  1.00 38.76  ? 40  TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 41 ? 2.127   -8.228  -9.646  1.00 36.81  ? 40  TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 41 ? 0.767   -7.976  -9.573  1.00 36.59  ? 40  TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 41 ? 0.264   -6.703  -9.701  1.00 38.76  ? 40  TYR A OH  1 
ATOM   317  N N   . PRO A 1 42 ? 4.059   -14.113 -11.078 1.00 27.46  ? 41  PRO A N   1 
ATOM   318  C CA  . PRO A 1 42 ? 4.737   -15.395 -10.876 1.00 27.48  ? 41  PRO A CA  1 
ATOM   319  C C   . PRO A 1 42 ? 5.089   -15.515 -9.397  1.00 27.23  ? 41  PRO A C   1 
ATOM   320  O O   . PRO A 1 42 ? 5.722   -14.582 -8.855  1.00 27.88  ? 41  PRO A O   1 
ATOM   321  C CB  . PRO A 1 42 ? 6.002   -15.273 -11.723 1.00 28.03  ? 41  PRO A CB  1 
ATOM   322  C CG  . PRO A 1 42 ? 6.242   -13.816 -11.870 1.00 29.23  ? 41  PRO A CG  1 
ATOM   323  C CD  . PRO A 1 42 ? 4.907   -13.055 -11.666 1.00 30.27  ? 41  PRO A CD  1 
ATOM   324  N N   . ILE A 1 43 ? 4.549   -16.573 -8.762  1.00 29.42  ? 42  ILE A N   1 
ATOM   325  C CA  . ILE A 1 43 ? 4.721   -16.755 -7.322  1.00 26.71  ? 42  ILE A CA  1 
ATOM   326  C C   . ILE A 1 43 ? 5.681   -17.920 -7.118  1.00 28.86  ? 42  ILE A C   1 
ATOM   327  O O   . ILE A 1 43 ? 5.374   -19.065 -7.506  1.00 31.45  ? 42  ILE A O   1 
ATOM   328  C CB  . ILE A 1 43 ? 3.366   -17.006 -6.639  1.00 27.63  ? 42  ILE A CB  1 
ATOM   329  C CG1 . ILE A 1 43 ? 2.399   -15.868 -6.927  1.00 27.41  ? 42  ILE A CG1 1 
ATOM   330  C CG2 . ILE A 1 43 ? 3.589   -17.174 -5.121  1.00 27.19  ? 42  ILE A CG2 1 
ATOM   331  C CD1 . ILE A 1 43 ? 2.921   -14.482 -6.521  1.00 28.79  ? 42  ILE A CD1 1 
ATOM   332  N N   . PHE A 1 44 ? 6.793   -17.655 -6.405  1.00 25.59  ? 43  PHE A N   1 
ATOM   333  C CA  . PHE A 1 44 ? 7.693   -18.731 -6.042  1.00 27.11  ? 43  PHE A CA  1 
ATOM   334  C C   . PHE A 1 44 ? 7.442   -19.140 -4.602  1.00 27.93  ? 43  PHE A C   1 
ATOM   335  O O   . PHE A 1 44 ? 7.494   -18.311 -3.696  1.00 27.52  ? 43  PHE A O   1 
ATOM   336  C CB  . PHE A 1 44 ? 9.136   -18.218 -6.242  1.00 26.83  ? 43  PHE A CB  1 
ATOM   337  C CG  . PHE A 1 44 ? 10.177  -19.232 -5.787  1.00 30.37  ? 43  PHE A CG  1 
ATOM   338  C CD1 . PHE A 1 44 ? 10.560  -20.279 -6.651  1.00 31.30  ? 43  PHE A CD1 1 
ATOM   339  C CD2 . PHE A 1 44 ? 10.759  -19.165 -4.517  1.00 30.78  ? 43  PHE A CD2 1 
ATOM   340  C CE1 . PHE A 1 44 ? 11.517  -21.211 -6.259  1.00 31.94  ? 43  PHE A CE1 1 
ATOM   341  C CE2 . PHE A 1 44 ? 11.712  -20.123 -4.133  1.00 32.48  ? 43  PHE A CE2 1 
ATOM   342  C CZ  . PHE A 1 44 ? 12.109  -21.122 -5.012  1.00 30.31  ? 43  PHE A CZ  1 
ATOM   343  N N   . PHE A 1 45 ? 7.113   -20.427 -4.413  1.00 27.54  ? 44  PHE A N   1 
ATOM   344  C CA  . PHE A 1 45 ? 6.727   -20.950 -3.117  1.00 26.95  ? 44  PHE A CA  1 
ATOM   345  C C   . PHE A 1 45 ? 7.995   -21.439 -2.427  1.00 29.86  ? 44  PHE A C   1 
ATOM   346  O O   . PHE A 1 45 ? 8.696   -22.319 -2.962  1.00 30.40  ? 44  PHE A O   1 
ATOM   347  C CB  . PHE A 1 45 ? 5.736   -22.124 -3.305  1.00 29.60  ? 44  PHE A CB  1 
ATOM   348  C CG  . PHE A 1 45 ? 4.350   -21.640 -3.725  1.00 28.80  ? 44  PHE A CG  1 
ATOM   349  C CD1 . PHE A 1 45 ? 4.041   -21.421 -5.061  1.00 36.25  ? 44  PHE A CD1 1 
ATOM   350  C CD2 . PHE A 1 45 ? 3.358   -21.404 -2.769  1.00 31.15  ? 44  PHE A CD2 1 
ATOM   351  C CE1 . PHE A 1 45 ? 2.787   -20.930 -5.433  1.00 34.75  ? 44  PHE A CE1 1 
ATOM   352  C CE2 . PHE A 1 45 ? 2.093   -20.947 -3.142  1.00 31.50  ? 44  PHE A CE2 1 
ATOM   353  C CZ  . PHE A 1 45 ? 1.827   -20.682 -4.464  1.00 33.92  ? 44  PHE A CZ  1 
ATOM   354  N N   . PHE A 1 46 ? 8.287   -20.858 -1.259  1.00 28.34  ? 45  PHE A N   1 
ATOM   355  C CA  . PHE A 1 46 ? 9.449   -21.344 -0.507  1.00 26.60  ? 45  PHE A CA  1 
ATOM   356  C C   . PHE A 1 46 ? 9.207   -22.790 -0.067  1.00 29.91  ? 45  PHE A C   1 
ATOM   357  O O   . PHE A 1 46 ? 8.065   -23.265 0.010   1.00 30.11  ? 45  PHE A O   1 
ATOM   358  C CB  . PHE A 1 46 ? 9.721   -20.426 0.695   1.00 26.58  ? 45  PHE A CB  1 
ATOM   359  C CG  . PHE A 1 46 ? 10.153  -19.030 0.272   1.00 26.54  ? 45  PHE A CG  1 
ATOM   360  C CD1 . PHE A 1 46 ? 11.425  -18.823 -0.263  1.00 26.57  ? 45  PHE A CD1 1 
ATOM   361  C CD2 . PHE A 1 46 ? 9.400   -17.903 0.580   1.00 26.65  ? 45  PHE A CD2 1 
ATOM   362  C CE1 . PHE A 1 46 ? 11.827  -17.555 -0.633  1.00 25.54  ? 45  PHE A CE1 1 
ATOM   363  C CE2 . PHE A 1 46 ? 9.806   -16.632 0.217   1.00 23.96  ? 45  PHE A CE2 1 
ATOM   364  C CZ  . PHE A 1 46 ? 11.038  -16.448 -0.371  1.00 27.80  ? 45  PHE A CZ  1 
ATOM   365  N N   . GLY A 1 47 ? 10.308  -23.519 0.102   1.00 30.38  ? 46  GLY A N   1 
ATOM   366  C CA  . GLY A 1 47 ? 10.267  -24.884 0.607   1.00 29.89  ? 46  GLY A CA  1 
ATOM   367  C C   . GLY A 1 47 ? 10.033  -25.878 -0.540  1.00 37.54  ? 46  GLY A C   1 
ATOM   368  O O   . GLY A 1 47 ? 10.908  -26.685 -0.838  1.00 36.45  ? 46  GLY A O   1 
ATOM   369  N N   . THR A 1 48 ? 8.877   -25.790 -1.220  1.00 36.07  ? 47  THR A N   1 
ATOM   370  C CA  . THR A 1 48 ? 8.640   -26.622 -2.397  1.00 36.48  ? 47  THR A CA  1 
ATOM   371  C C   . THR A 1 48 ? 9.461   -26.132 -3.589  1.00 38.17  ? 47  THR A C   1 
ATOM   372  O O   . THR A 1 48 ? 9.761   -26.899 -4.501  1.00 33.69  ? 47  THR A O   1 
ATOM   373  C CB  . THR A 1 48 ? 7.157   -26.706 -2.763  1.00 38.42  ? 47  THR A CB  1 
ATOM   374  O OG1 . THR A 1 48 ? 6.782   -25.415 -3.235  1.00 35.21  ? 47  THR A OG1 1 
ATOM   375  C CG2 . THR A 1 48 ? 6.263   -27.133 -1.618  1.00 37.98  ? 47  THR A CG2 1 
ATOM   376  N N   . HIS A 1 49 ? 9.745   -24.824 -3.639  1.00 30.86  ? 48  HIS A N   1 
ATOM   377  C CA  . HIS A 1 49 ? 10.427  -24.208 -4.764  1.00 33.87  ? 48  HIS A CA  1 
ATOM   378  C C   . HIS A 1 49 ? 9.605   -24.345 -6.047  1.00 34.33  ? 48  HIS A C   1 
ATOM   379  O O   . HIS A 1 49 ? 10.191  -24.324 -7.119  1.00 35.74  ? 48  HIS A O   1 
ATOM   380  C CB  . HIS A 1 49 ? 11.854  -24.765 -4.950  1.00 33.54  ? 48  HIS A CB  1 
ATOM   381  C CG  . HIS A 1 49 ? 12.613  -24.792 -3.654  1.00 37.16  ? 48  HIS A CG  1 
ATOM   382  N ND1 . HIS A 1 49 ? 13.457  -25.815 -3.283  1.00 35.94  ? 48  HIS A ND1 1 
ATOM   383  C CD2 . HIS A 1 49 ? 12.654  -23.892 -2.642  1.00 35.17  ? 48  HIS A CD2 1 
ATOM   384  C CE1 . HIS A 1 49 ? 13.975  -25.547 -2.090  1.00 45.13  ? 48  HIS A CE1 1 
ATOM   385  N NE2 . HIS A 1 49 ? 13.514  -24.376 -1.681  1.00 35.81  ? 48  HIS A NE2 1 
ATOM   386  N N   . GLU A 1 50 ? 8.271   -24.433 -5.917  1.00 33.50  ? 49  GLU A N   1 
ATOM   387  C CA  . GLU A 1 50 ? 7.386   -24.456 -7.074  1.00 34.09  ? 49  GLU A CA  1 
ATOM   388  C C   . GLU A 1 50 ? 6.966   -23.041 -7.475  1.00 35.09  ? 49  GLU A C   1 
ATOM   389  O O   . GLU A 1 50 ? 7.098   -22.076 -6.703  1.00 32.46  ? 49  GLU A O   1 
ATOM   390  C CB  . GLU A 1 50 ? 6.148   -25.302 -6.785  1.00 36.11  ? 49  GLU A CB  1 
ATOM   391  C CG  . GLU A 1 50 ? 6.460   -26.793 -6.698  1.00 45.40  ? 49  GLU A CG  1 
ATOM   392  C CD  . GLU A 1 50 ? 5.370   -27.695 -6.141  1.00 53.87  ? 49  GLU A CD  1 
ATOM   393  O OE1 . GLU A 1 50 ? 4.196   -27.297 -5.970  1.00 58.91  ? 49  GLU A OE1 1 
ATOM   394  O OE2 . GLU A 1 50 ? 5.759   -28.838 -5.822  1.00 59.91  ? 49  GLU A OE2 1 
ATOM   395  N N   . THR A 1 51 ? 6.492   -22.905 -8.717  1.00 31.78  ? 50  THR A N   1 
ATOM   396  C CA  . THR A 1 51 ? 6.013   -21.617 -9.191  1.00 30.93  ? 50  THR A CA  1 
ATOM   397  C C   . THR A 1 51 ? 4.565   -21.790 -9.640  1.00 30.65  ? 50  THR A C   1 
ATOM   398  O O   . THR A 1 51 ? 4.222   -22.766 -10.298 1.00 35.40  ? 50  THR A O   1 
ATOM   399  C CB  . THR A 1 51 ? 6.860   -21.056 -10.332 1.00 35.44  ? 50  THR A CB  1 
ATOM   400  O OG1 . THR A 1 51 ? 8.142   -20.685 -9.844  1.00 37.21  ? 50  THR A OG1 1 
ATOM   401  C CG2 . THR A 1 51 ? 6.287   -19.786 -10.948 1.00 37.79  ? 50  THR A CG2 1 
ATOM   402  N N   . ALA A 1 52 ? 3.707   -20.847 -9.273  1.00 31.26  ? 51  ALA A N   1 
ATOM   403  C CA  . ALA A 1 52 ? 2.361   -20.791 -9.823  1.00 30.06  ? 51  ALA A CA  1 
ATOM   404  C C   . ALA A 1 52 ? 2.029   -19.340 -10.115 1.00 32.14  ? 51  ALA A C   1 
ATOM   405  O O   . ALA A 1 52 ? 2.724   -18.425 -9.658  1.00 30.64  ? 51  ALA A O   1 
ATOM   406  C CB  . ALA A 1 52 ? 1.362   -21.399 -8.868  1.00 32.29  ? 51  ALA A CB  1 
ATOM   407  N N   . PHE A 1 53 ? 0.977   -19.127 -10.914 1.00 29.95  ? 52  PHE A N   1 
ATOM   408  C CA  . PHE A 1 53 ? 0.618   -17.770 -11.291 1.00 31.23  ? 52  PHE A CA  1 
ATOM   409  C C   . PHE A 1 53 ? -0.653  -17.402 -10.546 1.00 34.92  ? 52  PHE A C   1 
ATOM   410  O O   . PHE A 1 53 ? -1.635  -18.151 -10.605 1.00 37.97  ? 52  PHE A O   1 
ATOM   411  C CB  . PHE A 1 53 ? 0.340   -17.765 -12.802 1.00 35.11  ? 52  PHE A CB  1 
ATOM   412  C CG  . PHE A 1 53 ? 1.548   -18.049 -13.677 1.00 37.83  ? 52  PHE A CG  1 
ATOM   413  C CD1 . PHE A 1 53 ? 2.715   -17.285 -13.571 1.00 43.38  ? 52  PHE A CD1 1 
ATOM   414  C CD2 . PHE A 1 53 ? 1.506   -19.092 -14.607 1.00 44.63  ? 52  PHE A CD2 1 
ATOM   415  C CE1 . PHE A 1 53 ? 3.824   -17.549 -14.389 1.00 46.24  ? 52  PHE A CE1 1 
ATOM   416  C CE2 . PHE A 1 53 ? 2.613   -19.358 -15.407 1.00 44.31  ? 52  PHE A CE2 1 
ATOM   417  C CZ  . PHE A 1 53 ? 3.757   -18.582 -15.311 1.00 41.81  ? 52  PHE A CZ  1 
ATOM   418  N N   . LEU A 1 54 ? -0.602  -16.299 -9.774  1.00 28.79  ? 53  LEU A N   1 
ATOM   419  C CA  . LEU A 1 54 ? -1.727  -15.956 -8.917  1.00 27.74  ? 53  LEU A CA  1 
ATOM   420  C C   . LEU A 1 54 ? -1.999  -14.458 -9.014  1.00 30.72  ? 53  LEU A C   1 
ATOM   421  O O   . LEU A 1 54 ? -1.108  -13.642 -9.305  1.00 29.05  ? 53  LEU A O   1 
ATOM   422  C CB  . LEU A 1 54 ? -1.299  -16.245 -7.471  1.00 30.35  ? 53  LEU A CB  1 
ATOM   423  C CG  . LEU A 1 54 ? -1.255  -17.722 -7.082  1.00 31.05  ? 53  LEU A CG  1 
ATOM   424  C CD1 . LEU A 1 54 ? -0.969  -17.818 -5.589  1.00 32.00  ? 53  LEU A CD1 1 
ATOM   425  C CD2 . LEU A 1 54 ? -2.615  -18.369 -7.379  1.00 37.67  ? 53  LEU A CD2 1 
ATOM   426  N N   . GLY A 1 55 ? -3.242  -14.094 -8.667  1.00 26.50  ? 54  GLY A N   1 
ATOM   427  C CA  . GLY A 1 55 ? -3.623  -12.685 -8.648  1.00 27.38  ? 54  GLY A CA  1 
ATOM   428  C C   . GLY A 1 55 ? -3.635  -12.186 -7.190  1.00 23.45  ? 54  GLY A C   1 
ATOM   429  O O   . GLY A 1 55 ? -3.580  -13.009 -6.247  1.00 24.57  ? 54  GLY A O   1 
ATOM   430  N N   . PRO A 1 56 ? -3.728  -10.858 -6.976  1.00 27.30  ? 55  PRO A N   1 
ATOM   431  C CA  . PRO A 1 56 ? -3.683  -10.262 -5.630  1.00 29.24  ? 55  PRO A CA  1 
ATOM   432  C C   . PRO A 1 56 ? -4.655  -10.788 -4.580  1.00 28.75  ? 55  PRO A C   1 
ATOM   433  O O   . PRO A 1 56 ? -4.361  -10.733 -3.389  1.00 25.82  ? 55  PRO A O   1 
ATOM   434  C CB  . PRO A 1 56 ? -3.950  -8.783  -5.915  1.00 29.30  ? 55  PRO A CB  1 
ATOM   435  C CG  . PRO A 1 56 ? -3.322  -8.538  -7.283  1.00 29.20  ? 55  PRO A CG  1 
ATOM   436  C CD  . PRO A 1 56 ? -3.685  -9.823  -8.033  1.00 28.68  ? 55  PRO A CD  1 
ATOM   437  N N   . LYS A 1 57 ? -5.802  -11.330 -5.040  1.00 29.04  ? 56  LYS A N   1 
ATOM   438  C CA  . LYS A 1 57 ? -6.781  -11.861 -4.086  1.00 29.37  ? 56  LYS A CA  1 
ATOM   439  C C   . LYS A 1 57 ? -6.221  -13.008 -3.234  1.00 28.15  ? 56  LYS A C   1 
ATOM   440  O O   . LYS A 1 57 ? -6.691  -13.263 -2.122  1.00 28.53  ? 56  LYS A O   1 
ATOM   441  C CB  . LYS A 1 57 ? -8.054  -12.337 -4.799  1.00 30.81  ? 56  LYS A CB  1 
ATOM   442  C CG  . LYS A 1 57 ? -7.835  -13.531 -5.703  1.00 33.20  ? 56  LYS A CG  1 
ATOM   443  C CD  . LYS A 1 57 ? -9.159  -13.934 -6.368  1.00 40.55  ? 56  LYS A CD  1 
ATOM   444  C CE  . LYS A 1 57 ? -9.136  -15.275 -7.063  1.00 42.17  ? 56  LYS A CE  1 
ATOM   445  N NZ  . LYS A 1 57 ? -8.783  -16.420 -6.210  1.00 44.50  ? 56  LYS A NZ  1 
ATOM   446  N N   . ASP A 1 58 ? -5.163  -13.691 -3.747  1.00 25.54  ? 57  ASP A N   1 
ATOM   447  C CA  . ASP A 1 58 ? -4.589  -14.826 -3.075  1.00 26.80  ? 57  ASP A CA  1 
ATOM   448  C C   . ASP A 1 58 ? -3.228  -14.477 -2.450  1.00 28.21  ? 57  ASP A C   1 
ATOM   449  O O   . ASP A 1 58 ? -2.524  -15.409 -2.050  1.00 27.73  ? 57  ASP A O   1 
ATOM   450  C CB  . ASP A 1 58 ? -4.464  -15.997 -4.045  1.00 28.05  ? 57  ASP A CB  1 
ATOM   451  C CG  . ASP A 1 58 ? -5.852  -16.552 -4.401  1.00 31.36  ? 57  ASP A CG  1 
ATOM   452  O OD1 . ASP A 1 58 ? -6.669  -16.691 -3.457  1.00 32.85  ? 57  ASP A OD1 1 
ATOM   453  O OD2 . ASP A 1 58 ? -6.056  -16.922 -5.547  1.00 32.73  ? 57  ASP A OD2 1 
ATOM   454  N N   . LEU A 1 59 ? -2.880  -13.180 -2.418  1.00 26.63  ? 58  LEU A N   1 
ATOM   455  C CA  . LEU A 1 59 ? -1.556  -12.762 -1.948  1.00 24.68  ? 58  LEU A CA  1 
ATOM   456  C C   . LEU A 1 59 ? -1.723  -11.901 -0.696  1.00 22.78  ? 58  LEU A C   1 
ATOM   457  O O   . LEU A 1 59 ? -2.323  -10.821 -0.756  1.00 26.73  ? 58  LEU A O   1 
ATOM   458  C CB  . LEU A 1 59 ? -0.844  -12.005 -3.084  1.00 24.00  ? 58  LEU A CB  1 
ATOM   459  C CG  . LEU A 1 59 ? -0.644  -12.829 -4.364  1.00 26.95  ? 58  LEU A CG  1 
ATOM   460  C CD1 . LEU A 1 59 ? 0.077   -11.956 -5.381  1.00 29.43  ? 58  LEU A CD1 1 
ATOM   461  C CD2 . LEU A 1 59 ? 0.192   -14.078 -4.169  1.00 25.62  ? 58  LEU A CD2 1 
ATOM   462  N N   . PHE A 1 60 ? -1.085  -12.332 0.401   1.00 24.40  ? 59  PHE A N   1 
ATOM   463  C CA  . PHE A 1 60 ? -1.193  -11.653 1.697   1.00 22.92  ? 59  PHE A CA  1 
ATOM   464  C C   . PHE A 1 60 ? 0.196   -11.188 2.102   1.00 27.32  ? 59  PHE A C   1 
ATOM   465  O O   . PHE A 1 60 ? 1.083   -12.022 2.294   1.00 30.11  ? 59  PHE A O   1 
ATOM   466  C CB  . PHE A 1 60 ? -1.670  -12.693 2.710   1.00 25.32  ? 59  PHE A CB  1 
ATOM   467  C CG  . PHE A 1 60 ? -3.112  -13.130 2.454   1.00 26.44  ? 59  PHE A CG  1 
ATOM   468  C CD1 . PHE A 1 60 ? -3.407  -14.045 1.452   1.00 28.45  ? 59  PHE A CD1 1 
ATOM   469  C CD2 . PHE A 1 60 ? -4.141  -12.621 3.252   1.00 30.88  ? 59  PHE A CD2 1 
ATOM   470  C CE1 . PHE A 1 60 ? -4.724  -14.412 1.176   1.00 34.27  ? 59  PHE A CE1 1 
ATOM   471  C CE2 . PHE A 1 60 ? -5.446  -13.018 2.983   1.00 28.71  ? 59  PHE A CE2 1 
ATOM   472  C CZ  . PHE A 1 60 ? -5.719  -13.925 1.969   1.00 29.26  ? 59  PHE A CZ  1 
ATOM   473  N N   . PRO A 1 61 ? 0.437   -9.867  2.213   1.00 30.57  ? 60  PRO A N   1 
ATOM   474  C CA  . PRO A 1 61 ? 1.780   -9.395  2.563   1.00 29.80  ? 60  PRO A CA  1 
ATOM   475  C C   . PRO A 1 61 ? 2.317   -10.056 3.830   1.00 28.89  ? 60  PRO A C   1 
ATOM   476  O O   . PRO A 1 61 ? 1.623   -10.252 4.839   1.00 28.07  ? 60  PRO A O   1 
ATOM   477  C CB  . PRO A 1 61 ? 1.572   -7.875  2.644   1.00 31.61  ? 60  PRO A CB  1 
ATOM   478  C CG  . PRO A 1 61 ? 0.472   -7.620  1.547   1.00 33.82  ? 60  PRO A CG  1 
ATOM   479  C CD  . PRO A 1 61 ? -0.474  -8.767  1.864   1.00 30.10  ? 60  PRO A CD  1 
ATOM   480  N N   . TYR A 1 62 ? 3.610   -10.463 3.768   1.00 28.10  ? 61  TYR A N   1 
ATOM   481  C CA  . TYR A 1 62 ? 4.182   -11.348 4.776   1.00 26.92  ? 61  TYR A CA  1 
ATOM   482  C C   . TYR A 1 62 ? 4.241   -10.685 6.166   1.00 27.69  ? 61  TYR A C   1 
ATOM   483  O O   . TYR A 1 62 ? 3.818   -11.310 7.148   1.00 30.91  ? 61  TYR A O   1 
ATOM   484  C CB  . TYR A 1 62 ? 5.589   -11.747 4.275   1.00 29.36  ? 61  TYR A CB  1 
ATOM   485  C CG  . TYR A 1 62 ? 6.372   -12.514 5.334   1.00 28.79  ? 61  TYR A CG  1 
ATOM   486  C CD1 . TYR A 1 62 ? 6.130   -13.857 5.573   1.00 29.20  ? 61  TYR A CD1 1 
ATOM   487  C CD2 . TYR A 1 62 ? 7.383   -11.894 6.073   1.00 35.82  ? 61  TYR A CD2 1 
ATOM   488  C CE1 . TYR A 1 62 ? 6.825   -14.563 6.553   1.00 31.12  ? 61  TYR A CE1 1 
ATOM   489  C CE2 . TYR A 1 62 ? 8.101   -12.601 7.029   1.00 34.70  ? 61  TYR A CE2 1 
ATOM   490  C CZ  . TYR A 1 62 ? 7.821   -13.929 7.272   1.00 35.96  ? 61  TYR A CZ  1 
ATOM   491  O OH  . TYR A 1 62 ? 8.516   -14.661 8.226   1.00 33.35  ? 61  TYR A OH  1 
ATOM   492  N N   . ASP A 1 63 ? 4.646   -9.414  6.222   1.00 30.03  ? 62  ASP A N   1 
ATOM   493  C CA  . ASP A 1 63 ? 4.785   -8.763  7.525   1.00 36.77  ? 62  ASP A CA  1 
ATOM   494  C C   . ASP A 1 63 ? 3.438   -8.734  8.253   1.00 33.54  ? 62  ASP A C   1 
ATOM   495  O O   . ASP A 1 63 ? 3.382   -9.176  9.398   1.00 38.81  ? 62  ASP A O   1 
ATOM   496  C CB  . ASP A 1 63 ? 5.423   -7.388  7.415   1.00 37.04  ? 62  ASP A CB  1 
ATOM   497  C CG  . ASP A 1 63 ? 6.942   -7.376  7.275   1.00 56.59  ? 62  ASP A CG  1 
ATOM   498  O OD1 . ASP A 1 63 ? 7.582   -8.346  7.739   1.00 68.78  ? 62  ASP A OD1 1 
ATOM   499  O OD2 . ASP A 1 63 ? 7.482   -6.398  6.691   1.00 69.74  ? 62  ASP A OD2 1 
ATOM   500  N N   . LYS A 1 64 ? 2.386   -8.250  7.566   1.00 35.40  ? 63  LYS A N   1 
ATOM   501  C CA  . LYS A 1 64 ? 1.055   -8.190  8.183   1.00 37.59  ? 63  LYS A CA  1 
ATOM   502  C C   . LYS A 1 64 ? 0.565   -9.568  8.627   1.00 37.78  ? 63  LYS A C   1 
ATOM   503  O O   . LYS A 1 64 ? -0.184  -9.659  9.610   1.00 34.91  ? 63  LYS A O   1 
ATOM   504  C CB  . LYS A 1 64 ? 0.048   -7.555  7.214   1.00 37.00  ? 63  LYS A CB  1 
ATOM   505  C CG  . LYS A 1 64 ? -1.429  -7.425  7.696   1.00 41.19  ? 63  LYS A CG  1 
ATOM   506  C CD  . LYS A 1 64 ? -2.297  -6.704  6.661   1.00 44.04  ? 63  LYS A CD  1 
ATOM   507  C CE  . LYS A 1 64 ? -3.697  -6.501  7.172   1.00 46.01  ? 63  LYS A CE  1 
ATOM   508  N NZ  . LYS A 1 64 ? -3.667  -5.600  8.329   1.00 53.05  ? 63  LYS A NZ  1 
ATOM   509  N N   . SER A 1 65 ? 0.909   -10.637 7.888   1.00 30.50  ? 64  SER A N   1 
ATOM   510  C CA  . SER A 1 65 ? 0.176   -11.896 8.000   1.00 31.24  ? 64  SER A CA  1 
ATOM   511  C C   . SER A 1 65 ? 0.926   -12.982 8.777   1.00 33.46  ? 64  SER A C   1 
ATOM   512  O O   . SER A 1 65 ? 0.379   -14.070 8.984   1.00 33.96  ? 64  SER A O   1 
ATOM   513  C CB  . SER A 1 65 ? -0.151  -12.476 6.631   1.00 34.17  ? 64  SER A CB  1 
ATOM   514  O OG  . SER A 1 65 ? -0.959  -11.547 5.927   1.00 44.39  ? 64  SER A OG  1 
ATOM   515  N N   . LYS A 1 66 ? 2.197   -12.740 9.132   1.00 33.63  ? 65  LYS A N   1 
ATOM   516  C CA  . LYS A 1 66 ? 3.022   -13.852 9.587   1.00 36.20  ? 65  LYS A CA  1 
ATOM   517  C C   . LYS A 1 66 ? 2.592   -14.369 10.964  1.00 35.67  ? 65  LYS A C   1 
ATOM   518  O O   . LYS A 1 66 ? 2.761   -15.560 11.268  1.00 36.42  ? 65  LYS A O   1 
ATOM   519  C CB  . LYS A 1 66 ? 4.514   -13.508 9.564   1.00 35.79  ? 65  LYS A CB  1 
ATOM   520  C CG  . LYS A 1 66 ? 4.941   -12.368 10.419  1.00 40.52  ? 65  LYS A CG  1 
ATOM   521  C CD  . LYS A 1 66 ? 6.437   -12.187 10.164  1.00 51.36  ? 65  LYS A CD  1 
ATOM   522  C CE  . LYS A 1 66 ? 7.073   -11.326 11.206  1.00 58.75  ? 65  LYS A CE  1 
ATOM   523  N NZ  . LYS A 1 66 ? 6.456   -9.995  11.207  1.00 69.02  ? 65  LYS A NZ  1 
ATOM   524  N N   A ASP A 1 67 ? 2.033   -13.473 11.787  0.50 37.53  ? 66  ASP A N   1 
ATOM   525  N N   B ASP A 1 67 ? 2.049   -13.474 11.796  0.50 38.14  ? 66  ASP A N   1 
ATOM   526  C CA  A ASP A 1 67 ? 1.500   -13.865 13.084  0.50 39.84  ? 66  ASP A CA  1 
ATOM   527  C CA  B ASP A 1 67 ? 1.491   -13.891 13.073  0.50 41.02  ? 66  ASP A CA  1 
ATOM   528  C C   A ASP A 1 67 ? 0.413   -14.931 12.910  0.50 40.31  ? 66  ASP A C   1 
ATOM   529  C C   B ASP A 1 67 ? 0.476   -15.008 12.842  0.50 41.27  ? 66  ASP A C   1 
ATOM   530  O O   A ASP A 1 67 ? 0.342   -15.881 13.682  0.50 41.61  ? 66  ASP A O   1 
ATOM   531  O O   B ASP A 1 67 ? 0.508   -16.045 13.502  0.50 42.62  ? 66  ASP A O   1 
ATOM   532  C CB  A ASP A 1 67 ? 1.106   -12.653 13.922  0.50 41.38  ? 66  ASP A CB  1 
ATOM   533  C CB  B ASP A 1 67 ? 0.828   -12.727 13.793  0.50 44.04  ? 66  ASP A CB  1 
ATOM   534  C CG  A ASP A 1 67 ? 2.247   -11.947 14.649  0.50 44.46  ? 66  ASP A CG  1 
ATOM   535  C CG  B ASP A 1 67 ? 0.256   -13.042 15.169  0.50 50.19  ? 66  ASP A CG  1 
ATOM   536  O OD1 A ASP A 1 67 ? 3.369   -12.476 14.620  0.50 43.54  ? 66  ASP A OD1 1 
ATOM   537  O OD1 B ASP A 1 67 ? 1.046   -13.084 16.138  0.50 53.37  ? 66  ASP A OD1 1 
ATOM   538  O OD2 A ASP A 1 67 ? 2.012   -10.866 15.239  0.50 45.71  ? 66  ASP A OD2 1 
ATOM   539  O OD2 B ASP A 1 67 ? -0.977  -13.266 15.255  0.50 56.65  ? 66  ASP A OD2 1 
ATOM   540  N N   . LYS A 1 68 ? -0.412  -14.798 11.865  1.00 34.75  ? 67  LYS A N   1 
ATOM   541  C CA  . LYS A 1 68 ? -1.502  -15.726 11.638  1.00 35.44  ? 67  LYS A CA  1 
ATOM   542  C C   . LYS A 1 68 ? -0.998  -16.973 10.921  1.00 39.07  ? 67  LYS A C   1 
ATOM   543  O O   . LYS A 1 68 ? -1.422  -18.082 11.230  1.00 42.81  ? 67  LYS A O   1 
ATOM   544  C CB  . LYS A 1 68 ? -2.553  -14.997 10.803  1.00 36.85  ? 67  LYS A CB  1 
ATOM   545  C CG  . LYS A 1 68 ? -3.860  -15.715 10.637  1.00 41.04  ? 67  LYS A CG  1 
ATOM   546  C CD  . LYS A 1 68 ? -4.835  -14.829 9.861   1.00 45.44  ? 67  LYS A CD  1 
ATOM   547  C CE  . LYS A 1 68 ? -6.267  -15.274 9.931   1.00 55.11  ? 67  LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 68 ? -7.143  -14.271 9.309   1.00 48.77  ? 67  LYS A NZ  1 
ATOM   549  N N   . TYR A 1 69 ? -0.158  -16.790 9.896   1.00 36.47  ? 68  TYR A N   1 
ATOM   550  C CA  . TYR A 1 69 ? 0.061   -17.860 8.937   1.00 31.48  ? 68  TYR A CA  1 
ATOM   551  C C   . TYR A 1 69 ? 1.434   -18.519 9.110   1.00 30.78  ? 68  TYR A C   1 
ATOM   552  O O   . TYR A 1 69 ? 1.695   -19.582 8.548   1.00 35.72  ? 68  TYR A O   1 
ATOM   553  C CB  . TYR A 1 69 ? -0.095  -17.330 7.502   1.00 31.54  ? 68  TYR A CB  1 
ATOM   554  C CG  . TYR A 1 69 ? -1.499  -16.890 7.114   1.00 33.55  ? 68  TYR A CG  1 
ATOM   555  C CD1 . TYR A 1 69 ? -2.626  -17.624 7.498   1.00 34.41  ? 68  TYR A CD1 1 
ATOM   556  C CD2 . TYR A 1 69 ? -1.692  -15.716 6.391   1.00 34.93  ? 68  TYR A CD2 1 
ATOM   557  C CE1 . TYR A 1 69 ? -3.898  -17.214 7.134   1.00 39.11  ? 68  TYR A CE1 1 
ATOM   558  C CE2 . TYR A 1 69 ? -2.963  -15.294 6.033   1.00 36.53  ? 68  TYR A CE2 1 
ATOM   559  C CZ  . TYR A 1 69 ? -4.065  -16.035 6.422   1.00 34.16  ? 68  TYR A CZ  1 
ATOM   560  O OH  . TYR A 1 69 ? -5.318  -15.633 6.049   1.00 36.42  ? 68  TYR A OH  1 
ATOM   561  N N   . GLY A 1 70 ? 2.327   -17.907 9.876   1.00 32.63  ? 69  GLY A N   1 
ATOM   562  C CA  . GLY A 1 70 ? 3.708   -18.383 9.899   1.00 35.21  ? 69  GLY A CA  1 
ATOM   563  C C   . GLY A 1 70 ? 3.928   -19.331 11.077  1.00 37.34  ? 69  GLY A C   1 
ATOM   564  O O   . GLY A 1 70 ? 4.694   -19.047 11.961  1.00 41.75  ? 69  GLY A O   1 
ATOM   565  N N   . LYS A 1 71 ? 3.192   -20.429 11.093  1.00 41.74  ? 70  LYS A N   1 
ATOM   566  C CA  . LYS A 1 71 ? 3.369   -21.449 12.110  1.00 43.15  ? 70  LYS A CA  1 
ATOM   567  C C   . LYS A 1 71 ? 3.628   -22.764 11.395  1.00 37.97  ? 70  LYS A C   1 
ATOM   568  O O   . LYS A 1 71 ? 3.205   -22.975 10.253  1.00 40.00  ? 70  LYS A O   1 
ATOM   569  C CB  . LYS A 1 71 ? 2.120   -21.470 13.002  1.00 48.56  ? 70  LYS A CB  1 
ATOM   570  C CG  . LYS A 1 71 ? 1.944   -20.240 13.880  1.00 47.61  ? 70  LYS A CG  1 
ATOM   571  C CD  . LYS A 1 71 ? 0.472   -20.170 14.261  1.00 54.41  ? 70  LYS A CD  1 
ATOM   572  C CE  . LYS A 1 71 ? -0.001  -18.873 14.826  1.00 64.55  ? 70  LYS A CE  1 
ATOM   573  N NZ  . LYS A 1 71 ? -1.463  -18.776 14.710  1.00 66.51  ? 70  LYS A NZ  1 
ATOM   574  N N   . PRO A 1 72 ? 4.382   -23.707 12.008  1.00 43.83  ? 71  PRO A N   1 
ATOM   575  C CA  . PRO A 1 72 ? 4.654   -24.981 11.346  1.00 41.22  ? 71  PRO A CA  1 
ATOM   576  C C   . PRO A 1 72 ? 3.436   -25.726 10.830  1.00 37.59  ? 71  PRO A C   1 
ATOM   577  O O   . PRO A 1 72 ? 2.383   -25.640 11.445  1.00 47.28  ? 71  PRO A O   1 
ATOM   578  C CB  . PRO A 1 72 ? 5.400   -25.789 12.423  1.00 42.44  ? 71  PRO A CB  1 
ATOM   579  C CG  . PRO A 1 72 ? 6.093   -24.724 13.251  1.00 47.00  ? 71  PRO A CG  1 
ATOM   580  C CD  . PRO A 1 72 ? 5.092   -23.548 13.289  1.00 45.53  ? 71  PRO A CD  1 
ATOM   581  N N   . ASN A 1 73 ? 3.633   -26.525 9.774   1.00 41.92  ? 72  ASN A N   1 
ATOM   582  C CA  . ASN A 1 73 ? 2.578   -27.239 9.080   1.00 48.33  ? 72  ASN A CA  1 
ATOM   583  C C   . ASN A 1 73 ? 3.161   -28.567 8.618   1.00 52.00  ? 72  ASN A C   1 
ATOM   584  O O   . ASN A 1 73 ? 4.327   -28.652 8.244   1.00 55.78  ? 72  ASN A O   1 
ATOM   585  C CB  . ASN A 1 73 ? 2.093   -26.408 7.893   1.00 50.44  ? 72  ASN A CB  1 
ATOM   586  C CG  . ASN A 1 73 ? 0.720   -26.769 7.380   1.00 62.11  ? 72  ASN A CG  1 
ATOM   587  O OD1 . ASN A 1 73 ? 0.574   -27.691 6.573   1.00 59.90  ? 72  ASN A OD1 1 
ATOM   588  N ND2 . ASN A 1 73 ? -0.296  -26.009 7.767   1.00 68.12  ? 72  ASN A ND2 1 
ATOM   589  N N   . LYS A 1 74 ? 2.336   -29.609 8.625   1.00 51.24  ? 73  LYS A N   1 
ATOM   590  C CA  . LYS A 1 74 ? 2.798   -30.947 8.311   1.00 55.46  ? 73  LYS A CA  1 
ATOM   591  C C   . LYS A 1 74 ? 3.067   -31.111 6.813   1.00 54.38  ? 73  LYS A C   1 
ATOM   592  O O   . LYS A 1 74 ? 3.723   -32.071 6.399   1.00 51.62  ? 73  LYS A O   1 
ATOM   593  C CB  . LYS A 1 74 ? 1.747   -31.921 8.868   1.00 67.50  ? 73  LYS A CB  1 
ATOM   594  C CG  . LYS A 1 74 ? 0.382   -31.941 8.165   1.00 65.06  ? 73  LYS A CG  1 
ATOM   595  N N   . ARG A 1 75 ? 2.561   -30.185 5.986   1.00 45.96  ? 74  ARG A N   1 
ATOM   596  C CA  . ARG A 1 75 ? 2.587   -30.376 4.545   1.00 48.78  ? 74  ARG A CA  1 
ATOM   597  C C   . ARG A 1 75 ? 4.029   -30.310 4.049   1.00 43.61  ? 74  ARG A C   1 
ATOM   598  O O   . ARG A 1 75 ? 4.815   -29.548 4.598   1.00 43.34  ? 74  ARG A O   1 
ATOM   599  C CB  . ARG A 1 75 ? 1.696   -29.349 3.825   1.00 52.86  ? 74  ARG A CB  1 
ATOM   600  C CG  . ARG A 1 75 ? 0.244   -29.616 4.192   1.00 59.04  ? 74  ARG A CG  1 
ATOM   601  C CD  . ARG A 1 75 ? -0.376  -30.742 3.381   1.00 45.66  ? 74  ARG A CD  1 
ATOM   602  N NE  . ARG A 1 75 ? -1.111  -30.251 2.212   1.00 64.16  ? 74  ARG A NE  1 
ATOM   603  C CZ  . ARG A 1 75 ? -2.231  -29.533 2.321   1.00 66.18  ? 74  ARG A CZ  1 
ATOM   604  N NH1 . ARG A 1 75 ? -2.911  -29.208 1.235   1.00 68.66  ? 74  ARG A NH1 1 
ATOM   605  N NH2 . ARG A 1 75 ? -2.688  -29.184 3.515   1.00 72.94  ? 74  ARG A NH2 1 
ATOM   606  N N   . LYS A 1 76 ? 4.335   -31.122 3.023   1.00 41.52  ? 75  LYS A N   1 
ATOM   607  C CA  . LYS A 1 76 ? 5.690   -31.291 2.518   1.00 44.61  ? 75  LYS A CA  1 
ATOM   608  C C   . LYS A 1 76 ? 6.245   -29.928 2.118   1.00 42.03  ? 75  LYS A C   1 
ATOM   609  O O   . LYS A 1 76 ? 5.640   -29.244 1.288   1.00 39.14  ? 75  LYS A O   1 
ATOM   610  C CB  . LYS A 1 76 ? 5.674   -32.202 1.289   1.00 43.21  ? 75  LYS A CB  1 
ATOM   611  C CG  . LYS A 1 76 ? 7.011   -32.588 0.670   1.00 51.22  ? 75  LYS A CG  1 
ATOM   612  C CD  . LYS A 1 76 ? 6.887   -33.837 -0.200  1.00 59.94  ? 75  LYS A CD  1 
ATOM   613  C CE  . LYS A 1 76 ? 8.188   -34.232 -0.822  1.00 64.98  ? 75  LYS A CE  1 
ATOM   614  N N   . GLY A 1 77 ? 7.394   -29.560 2.699   1.00 43.75  ? 76  GLY A N   1 
ATOM   615  C CA  . GLY A 1 77 ? 8.146   -28.389 2.259   1.00 39.32  ? 76  GLY A CA  1 
ATOM   616  C C   . GLY A 1 77 ? 7.799   -27.130 3.053   1.00 38.66  ? 76  GLY A C   1 
ATOM   617  O O   . GLY A 1 77 ? 8.530   -26.144 2.993   1.00 37.19  ? 76  GLY A O   1 
ATOM   618  N N   . PHE A 1 78 ? 6.710   -27.158 3.824   1.00 34.05  ? 77  PHE A N   1 
ATOM   619  C CA  . PHE A 1 78 ? 6.238   -25.939 4.470   1.00 34.85  ? 77  PHE A CA  1 
ATOM   620  C C   . PHE A 1 78 ? 7.234   -25.370 5.493   1.00 38.16  ? 77  PHE A C   1 
ATOM   621  O O   . PHE A 1 78 ? 7.496   -24.164 5.524   1.00 34.48  ? 77  PHE A O   1 
ATOM   622  C CB  . PHE A 1 78 ? 4.856   -26.266 5.034   1.00 35.87  ? 77  PHE A CB  1 
ATOM   623  C CG  . PHE A 1 78 ? 4.127   -25.001 5.448   1.00 38.76  ? 77  PHE A CG  1 
ATOM   624  C CD1 . PHE A 1 78 ? 4.412   -24.373 6.650   1.00 37.73  ? 77  PHE A CD1 1 
ATOM   625  C CD2 . PHE A 1 78 ? 3.149   -24.459 4.623   1.00 40.24  ? 77  PHE A CD2 1 
ATOM   626  C CE1 . PHE A 1 78 ? 3.734   -23.220 7.024   1.00 39.28  ? 77  PHE A CE1 1 
ATOM   627  C CE2 . PHE A 1 78 ? 2.475   -23.289 4.989   1.00 32.94  ? 77  PHE A CE2 1 
ATOM   628  C CZ  . PHE A 1 78 ? 2.776   -22.661 6.186   1.00 33.57  ? 77  PHE A CZ  1 
ATOM   629  N N   . ASN A 1 79 ? 7.756   -26.230 6.387   1.00 34.74  ? 78  ASN A N   1 
ATOM   630  C CA  . ASN A 1 79 ? 8.663   -25.763 7.425   1.00 36.46  ? 78  ASN A CA  1 
ATOM   631  C C   . ASN A 1 79 ? 9.985   -25.275 6.817   1.00 31.27  ? 78  ASN A C   1 
ATOM   632  O O   . ASN A 1 79 ? 10.551  -24.284 7.320   1.00 35.27  ? 78  ASN A O   1 
ATOM   633  C CB  . ASN A 1 79 ? 8.788   -26.799 8.552   1.00 34.28  ? 78  ASN A CB  1 
ATOM   634  C CG  . ASN A 1 79 ? 7.427   -27.057 9.165   1.00 39.59  ? 78  ASN A CG  1 
ATOM   635  O OD1 . ASN A 1 79 ? 6.531   -26.208 9.099   1.00 38.51  ? 78  ASN A OD1 1 
ATOM   636  N ND2 . ASN A 1 79 ? 7.253   -28.214 9.787   1.00 41.12  ? 78  ASN A ND2 1 
ATOM   637  N N   . GLU A 1 80 ? 10.497  -25.959 5.777   1.00 31.92  ? 79  GLU A N   1 
ATOM   638  C CA  . GLU A 1 80 ? 11.643  -25.439 5.045   1.00 33.29  ? 79  GLU A CA  1 
ATOM   639  C C   . GLU A 1 80 ? 11.289  -24.057 4.495   1.00 33.64  ? 79  GLU A C   1 
ATOM   640  O O   . GLU A 1 80 ? 12.069  -23.111 4.566   1.00 28.84  ? 79  GLU A O   1 
ATOM   641  C CB  . GLU A 1 80 ? 12.111  -26.396 3.946   1.00 32.53  ? 79  GLU A CB  1 
ATOM   642  C CG  . GLU A 1 80 ? 13.332  -25.894 3.181   1.00 33.63  ? 79  GLU A CG  1 
ATOM   643  C CD  . GLU A 1 80 ? 13.820  -26.937 2.168   1.00 45.80  ? 79  GLU A CD  1 
ATOM   644  O OE1 . GLU A 1 80 ? 13.144  -27.954 1.933   1.00 50.41  ? 79  GLU A OE1 1 
ATOM   645  O OE2 . GLU A 1 80 ? 14.899  -26.743 1.607   1.00 45.29  ? 79  GLU A OE2 1 
ATOM   646  N N   . GLY A 1 81 ? 10.079  -23.932 3.948   1.00 29.75  ? 80  GLY A N   1 
ATOM   647  C CA  . GLY A 1 81 ? 9.661   -22.636 3.421   1.00 30.12  ? 80  GLY A CA  1 
ATOM   648  C C   . GLY A 1 81 ? 9.661   -21.509 4.463   1.00 28.38  ? 80  GLY A C   1 
ATOM   649  O O   . GLY A 1 81 ? 10.020  -20.395 4.096   1.00 28.50  ? 80  GLY A O   1 
ATOM   650  N N   . LEU A 1 82 ? 9.214   -21.787 5.709   1.00 28.62  ? 81  LEU A N   1 
ATOM   651  C CA  . LEU A 1 82 ? 9.195   -20.814 6.782   1.00 28.74  ? 81  LEU A CA  1 
ATOM   652  C C   . LEU A 1 82 ? 10.633  -20.367 7.048   1.00 29.14  ? 81  LEU A C   1 
ATOM   653  O O   . LEU A 1 82 ? 10.875  -19.192 7.335   1.00 29.65  ? 81  LEU A O   1 
ATOM   654  C CB  . LEU A 1 82 ? 8.536   -21.295 8.077   1.00 32.32  ? 81  LEU A CB  1 
ATOM   655  C CG  . LEU A 1 82 ? 7.059   -21.687 7.949   1.00 31.97  ? 81  LEU A CG  1 
ATOM   656  C CD1 . LEU A 1 82 ? 6.723   -22.331 9.296   1.00 35.23  ? 81  LEU A CD1 1 
ATOM   657  C CD2 . LEU A 1 82 ? 6.134   -20.507 7.666   1.00 33.61  ? 81  LEU A CD2 1 
ATOM   658  N N   . TRP A 1 83 ? 11.581  -21.311 6.939   1.00 28.53  ? 82  TRP A N   1 
ATOM   659  C CA  . TRP A 1 83 ? 12.961  -20.944 7.241   1.00 32.39  ? 82  TRP A CA  1 
ATOM   660  C C   . TRP A 1 83 ? 13.480  -20.001 6.156   1.00 27.77  ? 82  TRP A C   1 
ATOM   661  O O   . TRP A 1 83 ? 14.146  -19.033 6.448   1.00 29.07  ? 82  TRP A O   1 
ATOM   662  C CB  . TRP A 1 83 ? 13.866  -22.197 7.365   1.00 31.90  ? 82  TRP A CB  1 
ATOM   663  C CG  . TRP A 1 83 ? 15.308  -21.853 7.664   1.00 31.72  ? 82  TRP A CG  1 
ATOM   664  C CD1 . TRP A 1 83 ? 15.909  -21.759 8.891   1.00 35.01  ? 82  TRP A CD1 1 
ATOM   665  C CD2 . TRP A 1 83 ? 16.321  -21.485 6.699   1.00 33.34  ? 82  TRP A CD2 1 
ATOM   666  N NE1 . TRP A 1 83 ? 17.232  -21.396 8.746   1.00 33.83  ? 82  TRP A NE1 1 
ATOM   667  C CE2 . TRP A 1 83 ? 17.502  -21.203 7.417   1.00 31.51  ? 82  TRP A CE2 1 
ATOM   668  C CE3 . TRP A 1 83 ? 16.354  -21.378 5.300   1.00 33.76  ? 82  TRP A CE3 1 
ATOM   669  C CZ2 . TRP A 1 83 ? 18.683  -20.820 6.776   1.00 30.08  ? 82  TRP A CZ2 1 
ATOM   670  C CZ3 . TRP A 1 83 ? 17.514  -20.988 4.667   1.00 32.46  ? 82  TRP A CZ3 1 
ATOM   671  C CH2 . TRP A 1 83 ? 18.677  -20.723 5.405   1.00 34.65  ? 82  TRP A CH2 1 
ATOM   672  N N   . GLU A 1 84 ? 13.160  -20.305 4.894   1.00 27.49  ? 83  GLU A N   1 
ATOM   673  C CA  . GLU A 1 84 ? 13.690  -19.566 3.768   1.00 26.42  ? 83  GLU A CA  1 
ATOM   674  C C   . GLU A 1 84 ? 13.146  -18.146 3.786   1.00 28.47  ? 83  GLU A C   1 
ATOM   675  O O   . GLU A 1 84 ? 13.889  -17.202 3.628   1.00 26.39  ? 83  GLU A O   1 
ATOM   676  C CB  . GLU A 1 84 ? 13.257  -20.283 2.492   1.00 28.26  ? 83  GLU A CB  1 
ATOM   677  C CG  . GLU A 1 84 ? 14.023  -21.597 2.305   1.00 27.87  ? 83  GLU A CG  1 
ATOM   678  C CD  . GLU A 1 84 ? 13.586  -22.333 1.041   1.00 32.93  ? 83  GLU A CD  1 
ATOM   679  O OE1 . GLU A 1 84 ? 12.660  -21.905 0.330   1.00 30.84  ? 83  GLU A OE1 1 
ATOM   680  O OE2 . GLU A 1 84 ? 14.141  -23.433 0.769   1.00 31.77  ? 83  GLU A OE2 1 
ATOM   681  N N   . ILE A 1 85 ? 11.840  -18.001 4.015   1.00 26.82  ? 84  ILE A N   1 
ATOM   682  C CA  . ILE A 1 85 ? 11.260  -16.663 3.946   1.00 27.45  ? 84  ILE A CA  1 
ATOM   683  C C   . ILE A 1 85 ? 11.806  -15.796 5.085   1.00 25.89  ? 84  ILE A C   1 
ATOM   684  O O   . ILE A 1 85 ? 11.959  -14.587 4.932   1.00 26.80  ? 84  ILE A O   1 
ATOM   685  C CB  . ILE A 1 85 ? 9.710   -16.713 3.910   1.00 25.14  ? 84  ILE A CB  1 
ATOM   686  C CG1 . ILE A 1 85 ? 9.156   -15.320 3.482   1.00 25.44  ? 84  ILE A CG1 1 
ATOM   687  C CG2 . ILE A 1 85 ? 9.146   -17.082 5.281   1.00 27.26  ? 84  ILE A CG2 1 
ATOM   688  C CD1 . ILE A 1 85 ? 7.684   -15.407 3.028   1.00 24.46  ? 84  ILE A CD1 1 
ATOM   689  N N   . GLN A 1 86 ? 12.105  -16.417 6.235   1.00 24.11  ? 85  GLN A N   1 
ATOM   690  C CA  . GLN A 1 86 ? 12.631  -15.648 7.372   1.00 29.29  ? 85  GLN A CA  1 
ATOM   691  C C   . GLN A 1 86 ? 14.123  -15.335 7.241   1.00 31.01  ? 85  GLN A C   1 
ATOM   692  O O   . GLN A 1 86 ? 14.569  -14.253 7.679   1.00 32.03  ? 85  GLN A O   1 
ATOM   693  C CB  . GLN A 1 86 ? 12.309  -16.403 8.671   1.00 31.45  ? 85  GLN A CB  1 
ATOM   694  C CG  . GLN A 1 86 ? 12.715  -15.649 9.930   1.00 36.75  ? 85  GLN A CG  1 
ATOM   695  C CD  . GLN A 1 86 ? 12.070  -16.256 11.166  1.00 45.72  ? 85  GLN A CD  1 
ATOM   696  O OE1 . GLN A 1 86 ? 11.905  -17.482 11.275  1.00 38.22  ? 85  GLN A OE1 1 
ATOM   697  N NE2 . GLN A 1 86 ? 11.671  -15.399 12.096  1.00 50.45  ? 85  GLN A NE2 1 
ATOM   698  N N   . ASN A 1 87 ? 14.890  -16.263 6.649   1.00 27.60  ? 86  ASN A N   1 
ATOM   699  C CA  . ASN A 1 87 ? 16.336  -16.239 6.788   1.00 28.33  ? 86  ASN A CA  1 
ATOM   700  C C   . ASN A 1 87 ? 17.062  -15.909 5.489   1.00 27.31  ? 86  ASN A C   1 
ATOM   701  O O   . ASN A 1 87 ? 18.152  -15.333 5.547   1.00 30.17  ? 86  ASN A O   1 
ATOM   702  C CB  . ASN A 1 87 ? 16.822  -17.560 7.363   1.00 27.88  ? 86  ASN A CB  1 
ATOM   703  C CG  . ASN A 1 87 ? 16.389  -17.674 8.807   1.00 34.11  ? 86  ASN A CG  1 
ATOM   704  O OD1 . ASN A 1 87 ? 16.731  -16.812 9.630   1.00 34.86  ? 86  ASN A OD1 1 
ATOM   705  N ND2 . ASN A 1 87 ? 15.456  -18.565 9.103   1.00 32.73  ? 86  ASN A ND2 1 
ATOM   706  N N   . ASN A 1 88 ? 16.526  -16.309 4.320   1.00 27.24  ? 87  ASN A N   1 
ATOM   707  C CA  . ASN A 1 88 ? 17.172  -15.873 3.093   1.00 26.96  ? 87  ASN A CA  1 
ATOM   708  C C   . ASN A 1 88 ? 16.124  -15.785 1.981   1.00 27.23  ? 87  ASN A C   1 
ATOM   709  O O   . ASN A 1 88 ? 16.137  -16.540 1.013   1.00 26.60  ? 87  ASN A O   1 
ATOM   710  C CB  . ASN A 1 88 ? 18.338  -16.810 2.755   1.00 27.35  ? 87  ASN A CB  1 
ATOM   711  C CG  . ASN A 1 88 ? 19.362  -16.204 1.831   1.00 30.38  ? 87  ASN A CG  1 
ATOM   712  O OD1 . ASN A 1 88 ? 19.109  -15.207 1.145   1.00 29.67  ? 87  ASN A OD1 1 
ATOM   713  N ND2 . ASN A 1 88 ? 20.555  -16.803 1.812   1.00 32.27  ? 87  ASN A ND2 1 
ATOM   714  N N   . PRO A 1 89 ? 15.154  -14.853 2.087   1.00 27.11  ? 88  PRO A N   1 
ATOM   715  C CA  . PRO A 1 89 ? 14.036  -14.856 1.140   1.00 24.18  ? 88  PRO A CA  1 
ATOM   716  C C   . PRO A 1 89 ? 14.401  -14.408 -0.272  1.00 27.90  ? 88  PRO A C   1 
ATOM   717  O O   . PRO A 1 89 ? 13.611  -14.582 -1.196  1.00 26.36  ? 88  PRO A O   1 
ATOM   718  C CB  . PRO A 1 89 ? 13.072  -13.914 1.840   1.00 25.30  ? 88  PRO A CB  1 
ATOM   719  C CG  . PRO A 1 89 ? 13.984  -12.893 2.526   1.00 25.30  ? 88  PRO A CG  1 
ATOM   720  C CD  . PRO A 1 89 ? 15.032  -13.836 3.128   1.00 24.54  ? 88  PRO A CD  1 
ATOM   721  N N   . HIS A 1 90 ? 15.597  -13.827 -0.456  1.00 26.06  ? 89  HIS A N   1 
ATOM   722  C CA  . HIS A 1 90 ? 15.954  -13.314 -1.770  1.00 24.65  ? 89  HIS A CA  1 
ATOM   723  C C   . HIS A 1 90 ? 17.057  -14.120 -2.463  1.00 27.79  ? 89  HIS A C   1 
ATOM   724  O O   . HIS A 1 90 ? 17.519  -13.714 -3.536  1.00 28.80  ? 89  HIS A O   1 
ATOM   725  C CB  . HIS A 1 90 ? 16.324  -11.824 -1.681  1.00 25.00  ? 89  HIS A CB  1 
ATOM   726  C CG  . HIS A 1 90 ? 15.265  -10.984 -1.085  1.00 26.53  ? 89  HIS A CG  1 
ATOM   727  N ND1 . HIS A 1 90 ? 14.027  -10.874 -1.711  1.00 25.31  ? 89  HIS A ND1 1 
ATOM   728  C CD2 . HIS A 1 90 ? 15.196  -10.269 0.032   1.00 28.13  ? 89  HIS A CD2 1 
ATOM   729  C CE1 . HIS A 1 90 ? 13.271  -10.026 -0.998  1.00 26.65  ? 89  HIS A CE1 1 
ATOM   730  N NE2 . HIS A 1 90 ? 13.962  -9.654  0.076   1.00 28.69  ? 89  HIS A NE2 1 
ATOM   731  N N   . ALA A 1 91 ? 17.343  -15.304 -1.929  1.00 27.86  ? 90  ALA A N   1 
ATOM   732  C CA  . ALA A 1 91 ? 18.401  -16.131 -2.505  1.00 27.63  ? 90  ALA A CA  1 
ATOM   733  C C   . ALA A 1 91 ? 17.935  -16.830 -3.776  1.00 31.69  ? 90  ALA A C   1 
ATOM   734  O O   . ALA A 1 91 ? 16.733  -17.006 -4.047  1.00 29.56  ? 90  ALA A O   1 
ATOM   735  C CB  . ALA A 1 91 ? 18.882  -17.120 -1.466  1.00 28.59  ? 90  ALA A CB  1 
ATOM   736  N N   . SER A 1 92 ? 18.928  -17.317 -4.534  1.00 30.40  ? 91  SER A N   1 
ATOM   737  C CA  . SER A 1 92 ? 18.606  -18.256 -5.601  1.00 34.17  ? 91  SER A CA  1 
ATOM   738  C C   . SER A 1 92 ? 18.334  -19.645 -5.025  1.00 39.23  ? 91  SER A C   1 
ATOM   739  O O   . SER A 1 92 ? 19.158  -20.181 -4.287  1.00 38.96  ? 91  SER A O   1 
ATOM   740  C CB  . SER A 1 92 ? 19.770  -18.267 -6.576  1.00 41.34  ? 91  SER A CB  1 
ATOM   741  O OG  . SER A 1 92 ? 19.626  -19.416 -7.388  1.00 42.64  ? 91  SER A OG  1 
ATOM   742  N N   . TYR A 1 93 ? 17.192  -20.250 -5.393  1.00 34.54  ? 92  TYR A N   1 
ATOM   743  C CA  . TYR A 1 93 ? 16.846  -21.592 -4.970  1.00 34.48  ? 92  TYR A CA  1 
ATOM   744  C C   . TYR A 1 93 ? 16.893  -22.510 -6.195  1.00 43.75  ? 92  TYR A C   1 
ATOM   745  O O   . TYR A 1 93 ? 16.479  -23.661 -6.111  1.00 50.77  ? 92  TYR A O   1 
ATOM   746  C CB  . TYR A 1 93 ? 15.512  -21.592 -4.187  1.00 33.29  ? 92  TYR A CB  1 
ATOM   747  C CG  . TYR A 1 93 ? 15.661  -20.995 -2.794  1.00 30.73  ? 92  TYR A CG  1 
ATOM   748  C CD1 . TYR A 1 93 ? 16.139  -21.767 -1.735  1.00 30.55  ? 92  TYR A CD1 1 
ATOM   749  C CD2 . TYR A 1 93 ? 15.343  -19.656 -2.537  1.00 32.54  ? 92  TYR A CD2 1 
ATOM   750  C CE1 . TYR A 1 93 ? 16.308  -21.215 -0.469  1.00 36.24  ? 92  TYR A CE1 1 
ATOM   751  C CE2 . TYR A 1 93 ? 15.505  -19.096 -1.280  1.00 33.22  ? 92  TYR A CE2 1 
ATOM   752  C CZ  . TYR A 1 93 ? 15.975  -19.886 -0.239  1.00 32.69  ? 92  TYR A CZ  1 
ATOM   753  O OH  . TYR A 1 93 ? 16.210  -19.374 1.012   1.00 33.39  ? 92  TYR A OH  1 
ATOM   754  N N   . SER A 1 94 ? 17.493  -21.994 -7.283  1.00 51.82  ? 93  SER A N   1 
ATOM   755  C CA  . SER A 1 94 ? 17.716  -22.649 -8.570  1.00 67.22  ? 93  SER A CA  1 
ATOM   756  C C   . SER A 1 94 ? 18.444  -23.991 -8.397  1.00 76.82  ? 93  SER A C   1 
ATOM   757  O O   . SER A 1 94 ? 19.366  -24.046 -7.547  1.00 75.02  ? 93  SER A O   1 
ATOM   758  C CB  . SER A 1 94 ? 18.528  -21.762 -9.508  1.00 62.80  ? 93  SER A CB  1 
ATOM   759  O OG  . SER A 1 94 ? 17.993  -20.451 -9.611  1.00 69.59  ? 93  SER A OG  1 
ATOM   760  O OXT . SER A 1 94 ? 18.103  -24.919 -9.167  1.00 83.14  ? 93  SER A OXT 1 
ATOM   761  N N   . MET B 1 2  ? 38.999  -11.220 -42.230 1.00 71.87  ? 1   MET B N   1 
ATOM   762  C CA  . MET B 1 2  ? 38.604  -12.162 -43.309 1.00 65.54  ? 1   MET B CA  1 
ATOM   763  C C   . MET B 1 2  ? 37.092  -12.372 -43.260 1.00 66.38  ? 1   MET B C   1 
ATOM   764  O O   . MET B 1 2  ? 36.571  -12.774 -42.220 1.00 74.67  ? 1   MET B O   1 
ATOM   765  C CB  . MET B 1 2  ? 39.329  -13.504 -43.140 1.00 70.55  ? 1   MET B CB  1 
ATOM   766  C CG  . MET B 1 2  ? 39.348  -14.395 -44.378 1.00 85.10  ? 1   MET B CG  1 
ATOM   767  S SD  . MET B 1 2  ? 40.230  -13.738 -45.815 1.00 86.21  ? 1   MET B SD  1 
ATOM   768  C CE  . MET B 1 2  ? 41.563  -12.806 -45.046 1.00 64.60  ? 1   MET B CE  1 
ATOM   769  N N   . PRO B 1 3  ? 36.355  -12.114 -44.375 1.00 58.96  ? 2   PRO B N   1 
ATOM   770  C CA  . PRO B 1 3  ? 34.898  -12.264 -44.411 1.00 56.51  ? 2   PRO B CA  1 
ATOM   771  C C   . PRO B 1 3  ? 34.533  -13.699 -44.057 1.00 54.51  ? 2   PRO B C   1 
ATOM   772  O O   . PRO B 1 3  ? 35.305  -14.596 -44.348 1.00 48.33  ? 2   PRO B O   1 
ATOM   773  C CB  . PRO B 1 3  ? 34.553  -11.942 -45.860 1.00 54.86  ? 2   PRO B CB  1 
ATOM   774  C CG  . PRO B 1 3  ? 35.666  -11.007 -46.285 1.00 51.65  ? 2   PRO B CG  1 
ATOM   775  C CD  . PRO B 1 3  ? 36.893  -11.653 -45.667 1.00 56.65  ? 2   PRO B CD  1 
ATOM   776  N N   . HIS B 1 4  ? 33.395  -13.885 -43.374 1.00 52.75  ? 3   HIS B N   1 
ATOM   777  C CA  . HIS B 1 4  ? 32.926  -15.218 -43.032 1.00 52.26  ? 3   HIS B CA  1 
ATOM   778  C C   . HIS B 1 4  ? 31.561  -15.452 -43.669 1.00 47.86  ? 3   HIS B C   1 
ATOM   779  O O   . HIS B 1 4  ? 30.992  -14.549 -44.288 1.00 44.14  ? 3   HIS B O   1 
ATOM   780  C CB  . HIS B 1 4  ? 32.988  -15.454 -41.519 1.00 60.67  ? 3   HIS B CB  1 
ATOM   781  C CG  . HIS B 1 4  ? 34.379  -15.422 -40.970 1.00 71.66  ? 3   HIS B CG  1 
ATOM   782  N ND1 . HIS B 1 4  ? 35.358  -16.310 -41.373 1.00 72.94  ? 3   HIS B ND1 1 
ATOM   783  C CD2 . HIS B 1 4  ? 34.965  -14.598 -40.085 1.00 65.40  ? 3   HIS B CD2 1 
ATOM   784  C CE1 . HIS B 1 4  ? 36.487  -16.039 -40.729 1.00 68.47  ? 3   HIS B CE1 1 
ATOM   785  N NE2 . HIS B 1 4  ? 36.269  -15.005 -39.939 1.00 72.02  ? 3   HIS B NE2 1 
ATOM   786  N N   . ALA B 1 5  ? 31.040  -16.677 -43.520 1.00 43.07  ? 4   ALA B N   1 
ATOM   787  C CA  . ALA B 1 5  ? 29.720  -16.996 -44.035 1.00 42.45  ? 4   ALA B CA  1 
ATOM   788  C C   . ALA B 1 5  ? 28.702  -15.960 -43.548 1.00 45.73  ? 4   ALA B C   1 
ATOM   789  O O   . ALA B 1 5  ? 27.810  -15.564 -44.298 1.00 48.47  ? 4   ALA B O   1 
ATOM   790  C CB  . ALA B 1 5  ? 29.336  -18.373 -43.567 1.00 41.55  ? 4   ALA B CB  1 
ATOM   791  N N   . PHE B 1 6  ? 28.829  -15.573 -42.273 1.00 48.76  ? 5   PHE B N   1 
ATOM   792  C CA  . PHE B 1 6  ? 27.989  -14.564 -41.639 1.00 46.97  ? 5   PHE B CA  1 
ATOM   793  C C   . PHE B 1 6  ? 28.826  -13.306 -41.400 1.00 45.03  ? 5   PHE B C   1 
ATOM   794  O O   . PHE B 1 6  ? 29.935  -13.392 -40.884 1.00 45.93  ? 5   PHE B O   1 
ATOM   795  C CB  . PHE B 1 6  ? 27.480  -15.018 -40.260 1.00 45.13  ? 5   PHE B CB  1 
ATOM   796  C CG  . PHE B 1 6  ? 26.413  -16.100 -40.323 1.00 41.34  ? 5   PHE B CG  1 
ATOM   797  C CD1 . PHE B 1 6  ? 25.081  -15.766 -40.544 1.00 37.75  ? 5   PHE B CD1 1 
ATOM   798  C CD2 . PHE B 1 6  ? 26.750  -17.447 -40.202 1.00 41.61  ? 5   PHE B CD2 1 
ATOM   799  C CE1 . PHE B 1 6  ? 24.109  -16.744 -40.674 1.00 41.37  ? 5   PHE B CE1 1 
ATOM   800  C CE2 . PHE B 1 6  ? 25.763  -18.427 -40.304 1.00 37.52  ? 5   PHE B CE2 1 
ATOM   801  C CZ  . PHE B 1 6  ? 24.449  -18.078 -40.517 1.00 36.80  ? 5   PHE B CZ  1 
ATOM   802  N N   . LYS B 1 7  ? 28.269  -12.138 -41.743 1.00 50.05  ? 6   LYS B N   1 
ATOM   803  C CA  . LYS B 1 7  ? 28.988  -10.892 -41.514 1.00 44.88  ? 6   LYS B CA  1 
ATOM   804  C C   . LYS B 1 7  ? 28.240  -10.048 -40.468 1.00 45.39  ? 6   LYS B C   1 
ATOM   805  O O   . LYS B 1 7  ? 27.010  -10.135 -40.364 1.00 40.39  ? 6   LYS B O   1 
ATOM   806  C CB  . LYS B 1 7  ? 29.101  -10.188 -42.871 1.00 50.45  ? 6   LYS B CB  1 
ATOM   807  C CG  . LYS B 1 7  ? 27.787  -9.833  -43.551 1.00 53.66  ? 6   LYS B CG  1 
ATOM   808  C CD  . LYS B 1 7  ? 27.943  -9.162  -44.915 1.00 54.43  ? 6   LYS B CD  1 
ATOM   809  C CE  . LYS B 1 7  ? 26.649  -8.820  -45.597 1.00 50.38  ? 6   LYS B CE  1 
ATOM   810  N NZ  . LYS B 1 7  ? 25.867  -10.008 -45.949 1.00 59.22  ? 6   LYS B NZ  1 
ATOM   811  N N   . PRO B 1 8  ? 28.932  -9.153  -39.715 1.00 51.19  ? 7   PRO B N   1 
ATOM   812  C CA  . PRO B 1 8  ? 28.268  -8.221  -38.794 1.00 40.26  ? 7   PRO B CA  1 
ATOM   813  C C   . PRO B 1 8  ? 27.103  -7.550  -39.495 1.00 41.28  ? 7   PRO B C   1 
ATOM   814  O O   . PRO B 1 8  ? 27.226  -7.102  -40.641 1.00 45.27  ? 7   PRO B O   1 
ATOM   815  C CB  . PRO B 1 8  ? 29.443  -7.263  -38.560 1.00 48.53  ? 7   PRO B CB  1 
ATOM   816  C CG  . PRO B 1 8  ? 30.609  -8.229  -38.426 1.00 48.87  ? 7   PRO B CG  1 
ATOM   817  C CD  . PRO B 1 8  ? 30.396  -8.967  -39.725 1.00 46.66  ? 7   PRO B CD  1 
ATOM   818  N N   . GLY B 1 9  ? 25.944  -7.537  -38.824 1.00 37.39  ? 8   GLY B N   1 
ATOM   819  C CA  . GLY B 1 9  ? 24.777  -6.862  -39.357 1.00 36.78  ? 8   GLY B CA  1 
ATOM   820  C C   . GLY B 1 9  ? 23.792  -7.831  -40.006 1.00 34.83  ? 8   GLY B C   1 
ATOM   821  O O   . GLY B 1 9  ? 22.639  -7.484  -40.252 1.00 37.30  ? 8   GLY B O   1 
ATOM   822  N N   . ASP B 1 10 ? 24.249  -9.058  -40.301 1.00 34.46  ? 9   ASP B N   1 
ATOM   823  C CA  . ASP B 1 10 ? 23.322  -10.047 -40.846 1.00 33.56  ? 9   ASP B CA  1 
ATOM   824  C C   . ASP B 1 10 ? 22.238  -10.360 -39.800 1.00 29.66  ? 9   ASP B C   1 
ATOM   825  O O   . ASP B 1 10 ? 22.545  -10.464 -38.626 1.00 36.38  ? 9   ASP B O   1 
ATOM   826  C CB  . ASP B 1 10 ? 24.027  -11.364 -41.118 1.00 35.82  ? 9   ASP B CB  1 
ATOM   827  C CG  . ASP B 1 10 ? 24.839  -11.393 -42.409 1.00 47.55  ? 9   ASP B CG  1 
ATOM   828  O OD1 . ASP B 1 10 ? 24.566  -10.529 -43.271 1.00 45.12  ? 9   ASP B OD1 1 
ATOM   829  O OD2 . ASP B 1 10 ? 25.725  -12.279 -42.535 1.00 45.98  ? 9   ASP B OD2 1 
ATOM   830  N N   . LEU B 1 11 ? 21.017  -10.539 -40.264 1.00 32.80  ? 10  LEU B N   1 
ATOM   831  C CA  . LEU B 1 11 ? 19.891  -10.781 -39.372 1.00 32.55  ? 10  LEU B CA  1 
ATOM   832  C C   . LEU B 1 11 ? 19.607  -12.272 -39.386 1.00 34.97  ? 10  LEU B C   1 
ATOM   833  O O   . LEU B 1 11 ? 19.712  -12.874 -40.451 1.00 33.19  ? 10  LEU B O   1 
ATOM   834  C CB  . LEU B 1 11 ? 18.694  -9.946  -39.812 1.00 34.55  ? 10  LEU B CB  1 
ATOM   835  C CG  . LEU B 1 11 ? 18.997  -8.442  -39.877 1.00 31.23  ? 10  LEU B CG  1 
ATOM   836  C CD1 . LEU B 1 11 ? 17.697  -7.776  -40.305 1.00 34.22  ? 10  LEU B CD1 1 
ATOM   837  C CD2 . LEU B 1 11 ? 19.571  -7.928  -38.561 1.00 32.26  ? 10  LEU B CD2 1 
ATOM   838  N N   . VAL B 1 12 ? 19.283  -12.843 -38.207 1.00 32.28  ? 11  VAL B N   1 
ATOM   839  C CA  . VAL B 1 12 ? 19.076  -14.288 -38.105 1.00 30.83  ? 11  VAL B CA  1 
ATOM   840  C C   . VAL B 1 12 ? 17.978  -14.545 -37.073 1.00 35.40  ? 11  VAL B C   1 
ATOM   841  O O   . VAL B 1 12 ? 17.573  -13.642 -36.321 1.00 32.62  ? 11  VAL B O   1 
ATOM   842  C CB  . VAL B 1 12 ? 20.360  -14.990 -37.626 1.00 30.90  ? 11  VAL B CB  1 
ATOM   843  C CG1 . VAL B 1 12 ? 21.516  -14.873 -38.641 1.00 31.39  ? 11  VAL B CG1 1 
ATOM   844  C CG2 . VAL B 1 12 ? 20.825  -14.518 -36.243 1.00 32.92  ? 11  VAL B CG2 1 
ATOM   845  N N   . PHE B 1 13 ? 17.518  -15.802 -37.028 1.00 32.85  ? 12  PHE B N   1 
ATOM   846  C CA  . PHE B 1 13 ? 17.010  -16.336 -35.768 1.00 30.03  ? 12  PHE B CA  1 
ATOM   847  C C   . PHE B 1 13 ? 18.099  -17.203 -35.163 1.00 30.13  ? 12  PHE B C   1 
ATOM   848  O O   . PHE B 1 13 ? 18.692  -18.005 -35.908 1.00 30.21  ? 12  PHE B O   1 
ATOM   849  C CB  . PHE B 1 13 ? 15.768  -17.188 -35.988 1.00 30.98  ? 12  PHE B CB  1 
ATOM   850  C CG  . PHE B 1 13 ? 14.562  -16.366 -36.391 1.00 32.08  ? 12  PHE B CG  1 
ATOM   851  C CD1 . PHE B 1 13 ? 14.349  -16.034 -37.728 1.00 33.27  ? 12  PHE B CD1 1 
ATOM   852  C CD2 . PHE B 1 13 ? 13.663  -15.924 -35.427 1.00 32.37  ? 12  PHE B CD2 1 
ATOM   853  C CE1 . PHE B 1 13 ? 13.239  -15.280 -38.083 1.00 37.08  ? 12  PHE B CE1 1 
ATOM   854  C CE2 . PHE B 1 13 ? 12.553  -15.173 -35.788 1.00 36.81  ? 12  PHE B CE2 1 
ATOM   855  C CZ  . PHE B 1 13 ? 12.352  -14.840 -37.118 1.00 39.24  ? 12  PHE B CZ  1 
ATOM   856  N N   . ALA B 1 14 ? 18.357  -17.017 -33.849 1.00 27.17  ? 13  ALA B N   1 
ATOM   857  C CA  . ALA B 1 14 ? 19.379  -17.724 -33.107 1.00 29.04  ? 13  ALA B CA  1 
ATOM   858  C C   . ALA B 1 14 ? 18.725  -18.703 -32.133 1.00 32.85  ? 13  ALA B C   1 
ATOM   859  O O   . ALA B 1 14 ? 17.768  -18.356 -31.432 1.00 31.76  ? 13  ALA B O   1 
ATOM   860  C CB  . ALA B 1 14 ? 20.298  -16.751 -32.378 1.00 30.19  ? 13  ALA B CB  1 
ATOM   861  N N   . LYS B 1 15 ? 19.268  -19.917 -32.080 1.00 30.70  ? 14  LYS B N   1 
ATOM   862  C CA  . LYS B 1 15 ? 18.658  -20.984 -31.274 1.00 30.05  ? 14  LYS B CA  1 
ATOM   863  C C   . LYS B 1 15 ? 19.538  -21.282 -30.065 1.00 31.33  ? 14  LYS B C   1 
ATOM   864  O O   . LYS B 1 15 ? 20.725  -21.568 -30.204 1.00 35.90  ? 14  LYS B O   1 
ATOM   865  C CB  . LYS B 1 15 ? 18.410  -22.243 -32.123 1.00 32.22  ? 14  LYS B CB  1 
ATOM   866  C CG  . LYS B 1 15 ? 17.701  -23.352 -31.257 1.00 33.11  ? 14  LYS B CG  1 
ATOM   867  C CD  . LYS B 1 15 ? 16.225  -23.009 -31.041 1.00 35.23  ? 14  LYS B CD  1 
ATOM   868  C CE  . LYS B 1 15 ? 15.392  -24.113 -30.346 1.00 38.54  ? 14  LYS B CE  1 
ATOM   869  N NZ  . LYS B 1 15 ? 15.935  -24.339 -29.003 1.00 33.45  ? 14  LYS B NZ  1 
ATOM   870  N N   . MET B 1 16 ? 18.964  -21.113 -28.863 1.00 34.93  ? 15  MET B N   1 
ATOM   871  C CA  . MET B 1 16 ? 19.586  -21.470 -27.592 1.00 36.78  ? 15  MET B CA  1 
ATOM   872  C C   . MET B 1 16 ? 18.745  -22.576 -26.943 1.00 37.19  ? 15  MET B C   1 
ATOM   873  O O   . MET B 1 16 ? 17.515  -22.540 -26.989 1.00 36.77  ? 15  MET B O   1 
ATOM   874  C CB  . MET B 1 16 ? 19.590  -20.295 -26.599 1.00 40.25  ? 15  MET B CB  1 
ATOM   875  C CG  . MET B 1 16 ? 20.270  -19.012 -27.042 1.00 48.62  ? 15  MET B CG  1 
ATOM   876  S SD  . MET B 1 16 ? 22.049  -19.042 -26.745 1.00 55.59  ? 15  MET B SD  1 
ATOM   877  C CE  . MET B 1 16 ? 22.093  -19.055 -24.946 1.00 50.01  ? 15  MET B CE  1 
ATOM   878  N N   . LYS B 1 17 ? 19.410  -23.511 -26.265 1.00 39.17  ? 16  LYS B N   1 
ATOM   879  C CA  . LYS B 1 17 ? 18.681  -24.582 -25.597 1.00 38.55  ? 16  LYS B CA  1 
ATOM   880  C C   . LYS B 1 17 ? 17.675  -23.981 -24.603 1.00 34.31  ? 16  LYS B C   1 
ATOM   881  O O   . LYS B 1 17 ? 18.026  -23.094 -23.831 1.00 38.63  ? 16  LYS B O   1 
ATOM   882  C CB  . LYS B 1 17 ? 19.718  -25.413 -24.830 1.00 41.71  ? 16  LYS B CB  1 
ATOM   883  C CG  . LYS B 1 17 ? 19.145  -26.735 -24.290 1.00 53.44  ? 16  LYS B CG  1 
ATOM   884  C CD  . LYS B 1 17 ? 19.986  -27.456 -23.240 1.00 58.93  ? 16  LYS B CD  1 
ATOM   885  N N   . GLY B 1 18 ? 16.437  -24.478 -24.628 1.00 39.87  ? 17  GLY B N   1 
ATOM   886  C CA  . GLY B 1 18 ? 15.392  -24.027 -23.721 1.00 39.28  ? 17  GLY B CA  1 
ATOM   887  C C   . GLY B 1 18 ? 14.608  -22.826 -24.256 1.00 42.50  ? 17  GLY B C   1 
ATOM   888  O O   . GLY B 1 18 ? 13.710  -22.327 -23.582 1.00 38.57  ? 17  GLY B O   1 
ATOM   889  N N   . TYR B 1 19 ? 14.967  -22.311 -25.443 1.00 37.32  ? 18  TYR B N   1 
ATOM   890  C CA  . TYR B 1 19 ? 14.281  -21.110 -25.907 1.00 35.48  ? 18  TYR B CA  1 
ATOM   891  C C   . TYR B 1 19 ? 13.867  -21.283 -27.363 1.00 34.36  ? 18  TYR B C   1 
ATOM   892  O O   . TYR B 1 19 ? 14.554  -22.004 -28.084 1.00 35.28  ? 18  TYR B O   1 
ATOM   893  C CB  . TYR B 1 19 ? 15.224  -19.902 -25.912 1.00 34.17  ? 18  TYR B CB  1 
ATOM   894  C CG  . TYR B 1 19 ? 15.742  -19.536 -24.529 1.00 36.20  ? 18  TYR B CG  1 
ATOM   895  C CD1 . TYR B 1 19 ? 15.000  -18.718 -23.674 1.00 36.03  ? 18  TYR B CD1 1 
ATOM   896  C CD2 . TYR B 1 19 ? 16.936  -20.059 -24.056 1.00 38.90  ? 18  TYR B CD2 1 
ATOM   897  C CE1 . TYR B 1 19 ? 15.463  -18.420 -22.392 1.00 34.68  ? 18  TYR B CE1 1 
ATOM   898  C CE2 . TYR B 1 19 ? 17.402  -19.760 -22.781 1.00 42.67  ? 18  TYR B CE2 1 
ATOM   899  C CZ  . TYR B 1 19 ? 16.660  -18.946 -21.946 1.00 39.50  ? 18  TYR B CZ  1 
ATOM   900  O OH  . TYR B 1 19 ? 17.164  -18.636 -20.708 1.00 39.97  ? 18  TYR B OH  1 
ATOM   901  N N   . PRO B 1 20 ? 12.796  -20.620 -27.851 1.00 32.80  ? 19  PRO B N   1 
ATOM   902  C CA  . PRO B 1 20 ? 12.417  -20.686 -29.264 1.00 32.19  ? 19  PRO B CA  1 
ATOM   903  C C   . PRO B 1 20 ? 13.456  -19.948 -30.113 1.00 32.06  ? 19  PRO B C   1 
ATOM   904  O O   . PRO B 1 20 ? 14.171  -19.118 -29.572 1.00 30.65  ? 19  PRO B O   1 
ATOM   905  C CB  . PRO B 1 20 ? 11.066  -20.027 -29.356 1.00 32.71  ? 19  PRO B CB  1 
ATOM   906  C CG  . PRO B 1 20 ? 11.092  -19.060 -28.182 1.00 33.84  ? 19  PRO B CG  1 
ATOM   907  C CD  . PRO B 1 20 ? 11.917  -19.713 -27.092 1.00 32.56  ? 19  PRO B CD  1 
ATOM   908  N N   . HIS B 1 21 ? 13.578  -20.326 -31.388 1.00 30.66  ? 20  HIS B N   1 
ATOM   909  C CA  . HIS B 1 21 ? 14.375  -19.564 -32.366 1.00 28.91  ? 20  HIS B CA  1 
ATOM   910  C C   . HIS B 1 21 ? 14.116  -18.064 -32.215 1.00 27.58  ? 20  HIS B C   1 
ATOM   911  O O   . HIS B 1 21 ? 12.974  -17.621 -32.331 1.00 30.69  ? 20  HIS B O   1 
ATOM   912  C CB  . HIS B 1 21 ? 14.023  -20.038 -33.776 1.00 29.57  ? 20  HIS B CB  1 
ATOM   913  C CG  . HIS B 1 21 ? 14.296  -21.513 -33.966 1.00 31.92  ? 20  HIS B CG  1 
ATOM   914  N ND1 . HIS B 1 21 ? 13.476  -22.509 -33.457 1.00 34.50  ? 20  HIS B ND1 1 
ATOM   915  C CD2 . HIS B 1 21 ? 15.322  -22.156 -34.545 1.00 34.79  ? 20  HIS B CD2 1 
ATOM   916  C CE1 . HIS B 1 21 ? 13.971  -23.711 -33.763 1.00 35.62  ? 20  HIS B CE1 1 
ATOM   917  N NE2 . HIS B 1 21 ? 15.104  -23.536 -34.418 1.00 32.63  ? 20  HIS B NE2 1 
ATOM   918  N N   . TRP B 1 22 ? 15.189  -17.287 -31.990 1.00 29.29  ? 21  TRP B N   1 
ATOM   919  C CA  . TRP B 1 22 ? 14.987  -15.967 -31.407 1.00 29.31  ? 21  TRP B CA  1 
ATOM   920  C C   . TRP B 1 22 ? 15.470  -14.888 -32.375 1.00 31.91  ? 21  TRP B C   1 
ATOM   921  O O   . TRP B 1 22 ? 16.605  -15.016 -32.865 1.00 30.84  ? 21  TRP B O   1 
ATOM   922  C CB  . TRP B 1 22 ? 15.795  -15.863 -30.106 1.00 29.26  ? 21  TRP B CB  1 
ATOM   923  C CG  . TRP B 1 22 ? 15.275  -14.731 -29.242 1.00 30.37  ? 21  TRP B CG  1 
ATOM   924  C CD1 . TRP B 1 22 ? 15.488  -13.387 -29.386 1.00 32.22  ? 21  TRP B CD1 1 
ATOM   925  C CD2 . TRP B 1 22 ? 14.353  -14.859 -28.121 1.00 31.27  ? 21  TRP B CD2 1 
ATOM   926  N NE1 . TRP B 1 22 ? 14.792  -12.674 -28.422 1.00 33.59  ? 21  TRP B NE1 1 
ATOM   927  C CE2 . TRP B 1 22 ? 14.085  -13.552 -27.639 1.00 30.84  ? 21  TRP B CE2 1 
ATOM   928  C CE3 . TRP B 1 22 ? 13.729  -15.957 -27.503 1.00 33.58  ? 21  TRP B CE3 1 
ATOM   929  C CZ2 . TRP B 1 22 ? 13.209  -13.307 -26.570 1.00 32.71  ? 21  TRP B CZ2 1 
ATOM   930  C CZ3 . TRP B 1 22 ? 12.865  -15.723 -26.454 1.00 31.00  ? 21  TRP B CZ3 1 
ATOM   931  C CH2 . TRP B 1 22 ? 12.581  -14.413 -26.028 1.00 32.95  ? 21  TRP B CH2 1 
ATOM   932  N N   . PRO B 1 23 ? 14.708  -13.791 -32.649 1.00 30.42  ? 22  PRO B N   1 
ATOM   933  C CA  . PRO B 1 23 ? 15.202  -12.791 -33.606 1.00 30.03  ? 22  PRO B CA  1 
ATOM   934  C C   . PRO B 1 23 ? 16.507  -12.182 -33.103 1.00 28.86  ? 22  PRO B C   1 
ATOM   935  O O   . PRO B 1 23 ? 16.611  -11.771 -31.945 1.00 30.43  ? 22  PRO B O   1 
ATOM   936  C CB  . PRO B 1 23 ? 14.059  -11.755 -33.711 1.00 29.76  ? 22  PRO B CB  1 
ATOM   937  C CG  . PRO B 1 23 ? 13.339  -11.885 -32.361 1.00 32.27  ? 22  PRO B CG  1 
ATOM   938  C CD  . PRO B 1 23 ? 13.420  -13.410 -32.036 1.00 30.52  ? 22  PRO B CD  1 
ATOM   939  N N   . ALA B 1 24 ? 17.522  -12.086 -33.967 1.00 29.07  ? 23  ALA B N   1 
ATOM   940  C CA  . ALA B 1 24 ? 18.840  -11.696 -33.499 1.00 27.22  ? 23  ALA B CA  1 
ATOM   941  C C   . ALA B 1 24 ? 19.692  -11.145 -34.654 1.00 28.73  ? 23  ALA B C   1 
ATOM   942  O O   . ALA B 1 24 ? 19.272  -11.170 -35.814 1.00 32.07  ? 23  ALA B O   1 
ATOM   943  C CB  . ALA B 1 24 ? 19.553  -12.855 -32.773 1.00 30.23  ? 23  ALA B CB  1 
ATOM   944  N N   . ARG B 1 25 ? 20.858  -10.622 -34.284 1.00 31.43  ? 24  ARG B N   1 
ATOM   945  C CA  . ARG B 1 25 ? 21.796  -10.171 -35.309 1.00 32.68  ? 24  ARG B CA  1 
ATOM   946  C C   . ARG B 1 25 ? 23.205  -10.610 -34.952 1.00 31.32  ? 24  ARG B C   1 
ATOM   947  O O   . ARG B 1 25 ? 23.569  -10.850 -33.807 1.00 33.87  ? 24  ARG B O   1 
ATOM   948  C CB  . ARG B 1 25 ? 21.722  -8.662  -35.532 1.00 34.12  ? 24  ARG B CB  1 
ATOM   949  C CG  . ARG B 1 25 ? 22.331  -7.917  -34.356 1.00 33.84  ? 24  ARG B CG  1 
ATOM   950  C CD  . ARG B 1 25 ? 22.120  -6.390  -34.443 1.00 33.08  ? 24  ARG B CD  1 
ATOM   951  N NE  . ARG B 1 25 ? 22.765  -5.695  -33.327 1.00 35.49  ? 24  ARG B NE  1 
ATOM   952  C CZ  . ARG B 1 25 ? 22.477  -4.442  -32.919 1.00 34.08  ? 24  ARG B CZ  1 
ATOM   953  N NH1 . ARG B 1 25 ? 21.524  -3.772  -33.513 1.00 34.16  ? 24  ARG B NH1 1 
ATOM   954  N NH2 . ARG B 1 25 ? 23.126  -3.893  -31.914 1.00 32.60  ? 24  ARG B NH2 1 
ATOM   955  N N   . ILE B 1 26 ? 24.030  -10.689 -36.004 1.00 34.32  ? 25  ILE B N   1 
ATOM   956  C CA  . ILE B 1 26 ? 25.447  -10.876 -35.814 1.00 31.84  ? 25  ILE B CA  1 
ATOM   957  C C   . ILE B 1 26 ? 26.006  -9.492  -35.471 1.00 37.16  ? 25  ILE B C   1 
ATOM   958  O O   . ILE B 1 26 ? 25.735  -8.542  -36.201 1.00 37.91  ? 25  ILE B O   1 
ATOM   959  C CB  . ILE B 1 26 ? 26.081  -11.346 -37.131 1.00 34.97  ? 25  ILE B CB  1 
ATOM   960  C CG1 . ILE B 1 26 ? 25.364  -12.534 -37.748 1.00 35.30  ? 25  ILE B CG1 1 
ATOM   961  C CG2 . ILE B 1 26 ? 27.589  -11.548 -36.935 1.00 39.29  ? 25  ILE B CG2 1 
ATOM   962  C CD1 . ILE B 1 26 ? 25.324  -13.751 -36.838 1.00 35.49  ? 25  ILE B CD1 1 
ATOM   963  N N   . ASP B 1 27 ? 26.789  -9.426  -34.394 1.00 36.24  ? 26  ASP B N   1 
ATOM   964  C CA  . ASP B 1 27 ? 27.475  -8.208  -33.965 1.00 44.71  ? 26  ASP B CA  1 
ATOM   965  C C   . ASP B 1 27 ? 28.925  -8.191  -34.448 1.00 47.57  ? 26  ASP B C   1 
ATOM   966  O O   . ASP B 1 27 ? 29.417  -9.203  -34.924 1.00 48.26  ? 26  ASP B O   1 
ATOM   967  C CB  . ASP B 1 27 ? 27.462  -8.102  -32.458 1.00 44.10  ? 26  ASP B CB  1 
ATOM   968  C CG  . ASP B 1 27 ? 26.277  -7.352  -31.877 1.00 43.64  ? 26  ASP B CG  1 
ATOM   969  O OD1 . ASP B 1 27 ? 25.476  -6.789  -32.663 1.00 45.66  ? 26  ASP B OD1 1 
ATOM   970  O OD2 . ASP B 1 27 ? 26.190  -7.325  -30.636 1.00 43.36  ? 26  ASP B OD2 1 
ATOM   971  N N   A ASP B 1 28 ? 29.574  -7.027  -34.288 0.50 55.00  ? 27  ASP B N   1 
ATOM   972  N N   B ASP B 1 28 ? 29.591  -7.032  -34.347 0.50 55.30  ? 27  ASP B N   1 
ATOM   973  C CA  A ASP B 1 28 ? 30.960  -6.767  -34.653 0.50 58.52  ? 27  ASP B CA  1 
ATOM   974  C CA  B ASP B 1 28 ? 30.977  -6.909  -34.779 0.50 59.75  ? 27  ASP B CA  1 
ATOM   975  C C   A ASP B 1 28 ? 31.912  -7.416  -33.639 0.50 54.90  ? 27  ASP B C   1 
ATOM   976  C C   B ASP B 1 28 ? 31.924  -7.203  -33.607 0.50 59.03  ? 27  ASP B C   1 
ATOM   977  O O   A ASP B 1 28 ? 31.484  -7.593  -32.478 0.50 58.72  ? 27  ASP B O   1 
ATOM   978  O O   B ASP B 1 28 ? 31.414  -7.300  -32.469 0.50 64.94  ? 27  ASP B O   1 
ATOM   979  C CB  A ASP B 1 28 ? 31.210  -5.270  -34.781 0.50 53.14  ? 27  ASP B CB  1 
ATOM   980  C CB  B ASP B 1 28 ? 31.271  -5.555  -35.410 0.50 55.98  ? 27  ASP B CB  1 
ATOM   981  C CG  A ASP B 1 28 ? 30.440  -4.585  -35.902 0.50 55.15  ? 27  ASP B CG  1 
ATOM   982  C CG  B ASP B 1 28 ? 32.307  -5.598  -36.523 0.50 53.33  ? 27  ASP B CG  1 
ATOM   983  O OD1 A ASP B 1 28 ? 30.812  -4.783  -37.079 0.50 54.83  ? 27  ASP B OD1 1 
ATOM   984  O OD1 B ASP B 1 28 ? 33.253  -6.405  -36.408 0.50 57.85  ? 27  ASP B OD1 1 
ATOM   985  O OD2 A ASP B 1 28 ? 29.458  -3.882  -35.594 0.50 56.90  ? 27  ASP B OD2 1 
ATOM   986  O OD2 B ASP B 1 28 ? 32.170  -4.822  -37.490 0.50 47.48  ? 27  ASP B OD2 1 
ATOM   987  N N   . LYS B 1 35 ? 36.967  -12.095 -27.544 1.00 81.30  ? 34  LYS B N   1 
ATOM   988  C CA  . LYS B 1 35 ? 36.730  -12.579 -28.935 1.00 73.41  ? 34  LYS B CA  1 
ATOM   989  C C   . LYS B 1 35 ? 35.985  -13.923 -28.902 1.00 69.77  ? 34  LYS B C   1 
ATOM   990  O O   . LYS B 1 35 ? 36.168  -14.712 -27.974 1.00 63.49  ? 34  LYS B O   1 
ATOM   991  C CB  . LYS B 1 35 ? 38.049  -12.552 -29.721 1.00 67.02  ? 34  LYS B CB  1 
ATOM   992  N N   . PRO B 1 36 ? 35.095  -14.237 -29.884 1.00 60.43  ? 35  PRO B N   1 
ATOM   993  C CA  . PRO B 1 36 ? 34.348  -15.505 -29.862 1.00 59.73  ? 35  PRO B CA  1 
ATOM   994  C C   . PRO B 1 36 ? 35.245  -16.734 -29.720 1.00 55.70  ? 35  PRO B C   1 
ATOM   995  O O   . PRO B 1 36 ? 36.388  -16.696 -30.148 1.00 55.15  ? 35  PRO B O   1 
ATOM   996  C CB  . PRO B 1 36 ? 33.560  -15.539 -31.186 1.00 62.90  ? 35  PRO B CB  1 
ATOM   997  C CG  . PRO B 1 36 ? 33.639  -14.128 -31.748 1.00 62.82  ? 35  PRO B CG  1 
ATOM   998  C CD  . PRO B 1 36 ? 34.752  -13.379 -31.029 1.00 59.22  ? 35  PRO B CD  1 
ATOM   999  N N   . PRO B 1 37 ? 34.790  -17.866 -29.127 1.00 56.16  ? 36  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 37 ? 35.544  -19.115 -29.223 1.00 54.54  ? 36  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 37 ? 35.634  -19.416 -30.713 1.00 61.16  ? 36  PRO B C   1 
ATOM   1002 O O   . PRO B 1 37 ? 34.902  -18.814 -31.501 1.00 55.89  ? 36  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 37 ? 34.681  -20.165 -28.507 1.00 59.11  ? 36  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 37 ? 33.679  -19.366 -27.691 1.00 55.01  ? 36  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 37 ? 33.557  -18.004 -28.336 1.00 51.02  ? 36  PRO B CD  1 
ATOM   1006 N N   . PRO B 1 38 ? 36.506  -20.366 -31.137 1.00 61.39  ? 37  PRO B N   1 
ATOM   1007 C CA  . PRO B 1 38 ? 36.579  -20.772 -32.547 1.00 61.65  ? 37  PRO B CA  1 
ATOM   1008 C C   . PRO B 1 38 ? 35.206  -21.119 -33.133 1.00 51.33  ? 37  PRO B C   1 
ATOM   1009 O O   . PRO B 1 38 ? 34.401  -21.756 -32.452 1.00 54.38  ? 37  PRO B O   1 
ATOM   1010 C CB  . PRO B 1 38 ? 37.500  -22.018 -32.454 1.00 58.26  ? 37  PRO B CB  1 
ATOM   1011 C CG  . PRO B 1 38 ? 38.420  -21.698 -31.298 1.00 58.69  ? 37  PRO B CG  1 
ATOM   1012 C CD  . PRO B 1 38 ? 37.457  -21.098 -30.277 1.00 62.40  ? 37  PRO B CD  1 
ATOM   1013 N N   . ASN B 1 39 ? 34.962  -20.690 -34.386 1.00 51.30  ? 38  ASN B N   1 
ATOM   1014 C CA  . ASN B 1 39 ? 33.815  -21.131 -35.187 1.00 53.56  ? 38  ASN B CA  1 
ATOM   1015 C C   . ASN B 1 39 ? 32.503  -20.452 -34.770 1.00 44.08  ? 38  ASN B C   1 
ATOM   1016 O O   . ASN B 1 39 ? 31.451  -20.791 -35.280 1.00 42.10  ? 38  ASN B O   1 
ATOM   1017 C CB  . ASN B 1 39 ? 33.584  -22.638 -35.091 1.00 58.10  ? 38  ASN B CB  1 
ATOM   1018 C CG  . ASN B 1 39 ? 34.772  -23.449 -35.562 1.00 67.43  ? 38  ASN B CG  1 
ATOM   1019 O OD1 . ASN B 1 39 ? 35.138  -24.445 -34.925 1.00 65.39  ? 38  ASN B OD1 1 
ATOM   1020 N ND2 . ASN B 1 39 ? 35.361  -23.060 -36.685 1.00 58.54  ? 38  ASN B ND2 1 
ATOM   1021 N N   . LYS B 1 40 ? 32.565  -19.485 -33.846 1.00 45.99  ? 39  LYS B N   1 
ATOM   1022 C CA  . LYS B 1 40 ? 31.357  -18.927 -33.258 1.00 44.42  ? 39  LYS B CA  1 
ATOM   1023 C C   . LYS B 1 40 ? 31.322  -17.432 -33.514 1.00 42.49  ? 39  LYS B C   1 
ATOM   1024 O O   . LYS B 1 40 ? 32.333  -16.853 -33.903 1.00 46.18  ? 39  LYS B O   1 
ATOM   1025 C CB  . LYS B 1 40 ? 31.287  -19.227 -31.763 1.00 41.76  ? 39  LYS B CB  1 
ATOM   1026 C CG  . LYS B 1 40 ? 31.050  -20.692 -31.471 1.00 42.75  ? 39  LYS B CG  1 
ATOM   1027 C CD  . LYS B 1 40 ? 30.767  -20.798 -29.981 1.00 51.45  ? 39  LYS B CD  1 
ATOM   1028 C CE  . LYS B 1 40 ? 29.815  -21.860 -29.570 1.00 64.84  ? 39  LYS B CE  1 
ATOM   1029 N NZ  . LYS B 1 40 ? 30.421  -23.188 -29.639 1.00 57.84  ? 39  LYS B NZ  1 
ATOM   1030 N N   . TYR B 1 41 ? 30.127  -16.854 -33.362 1.00 38.92  ? 40  TYR B N   1 
ATOM   1031 C CA  . TYR B 1 41 ? 29.851  -15.479 -33.736 1.00 34.31  ? 40  TYR B CA  1 
ATOM   1032 C C   . TYR B 1 41 ? 29.233  -14.775 -32.532 1.00 40.73  ? 40  TYR B C   1 
ATOM   1033 O O   . TYR B 1 41 ? 28.532  -15.405 -31.729 1.00 35.91  ? 40  TYR B O   1 
ATOM   1034 C CB  . TYR B 1 41 ? 28.812  -15.401 -34.852 1.00 35.79  ? 40  TYR B CB  1 
ATOM   1035 C CG  . TYR B 1 41 ? 29.289  -15.875 -36.222 1.00 39.37  ? 40  TYR B CG  1 
ATOM   1036 C CD1 . TYR B 1 41 ? 29.929  -15.004 -37.095 1.00 39.25  ? 40  TYR B CD1 1 
ATOM   1037 C CD2 . TYR B 1 41 ? 29.100  -17.187 -36.633 1.00 38.93  ? 40  TYR B CD2 1 
ATOM   1038 C CE1 . TYR B 1 41 ? 30.366  -15.429 -38.344 1.00 46.62  ? 40  TYR B CE1 1 
ATOM   1039 C CE2 . TYR B 1 41 ? 29.538  -17.630 -37.870 1.00 40.32  ? 40  TYR B CE2 1 
ATOM   1040 C CZ  . TYR B 1 41 ? 30.163  -16.743 -38.736 1.00 45.82  ? 40  TYR B CZ  1 
ATOM   1041 O OH  . TYR B 1 41 ? 30.529  -17.156 -39.993 1.00 41.76  ? 40  TYR B OH  1 
ATOM   1042 N N   . PRO B 1 42 ? 29.463  -13.453 -32.364 1.00 41.26  ? 41  PRO B N   1 
ATOM   1043 C CA  . PRO B 1 42 ? 28.775  -12.717 -31.307 1.00 35.49  ? 41  PRO B CA  1 
ATOM   1044 C C   . PRO B 1 42 ? 27.353  -12.445 -31.776 1.00 36.18  ? 41  PRO B C   1 
ATOM   1045 O O   . PRO B 1 42 ? 27.145  -11.795 -32.805 1.00 35.97  ? 41  PRO B O   1 
ATOM   1046 C CB  . PRO B 1 42 ? 29.604  -11.431 -31.092 1.00 38.76  ? 41  PRO B CB  1 
ATOM   1047 C CG  . PRO B 1 42 ? 30.389  -11.271 -32.393 1.00 40.24  ? 41  PRO B CG  1 
ATOM   1048 C CD  . PRO B 1 42 ? 30.417  -12.618 -33.128 1.00 38.15  ? 41  PRO B CD  1 
ATOM   1049 N N   . ILE B 1 43 ? 26.385  -12.952 -30.991 1.00 35.44  ? 42  ILE B N   1 
ATOM   1050 C CA  . ILE B 1 43 ? 24.968  -12.747 -31.273 1.00 31.47  ? 42  ILE B CA  1 
ATOM   1051 C C   . ILE B 1 43 ? 24.390  -11.715 -30.291 1.00 29.58  ? 42  ILE B C   1 
ATOM   1052 O O   . ILE B 1 43 ? 24.684  -11.774 -29.119 1.00 37.03  ? 42  ILE B O   1 
ATOM   1053 C CB  . ILE B 1 43 ? 24.227  -14.089 -31.132 1.00 31.25  ? 42  ILE B CB  1 
ATOM   1054 C CG1 . ILE B 1 43 ? 24.966  -15.200 -31.920 1.00 35.49  ? 42  ILE B CG1 1 
ATOM   1055 C CG2 . ILE B 1 43 ? 22.775  -13.971 -31.611 1.00 31.45  ? 42  ILE B CG2 1 
ATOM   1056 C CD1 . ILE B 1 43 ? 25.235  -14.860 -33.366 1.00 33.23  ? 42  ILE B CD1 1 
ATOM   1057 N N   . PHE B 1 44 ? 23.566  -10.810 -30.812 1.00 33.91  ? 43  PHE B N   1 
ATOM   1058 C CA  . PHE B 1 44 ? 22.754  -9.904  -30.011 1.00 35.89  ? 43  PHE B CA  1 
ATOM   1059 C C   . PHE B 1 44 ? 21.303  -10.326 -30.221 1.00 32.38  ? 43  PHE B C   1 
ATOM   1060 O O   . PHE B 1 44 ? 20.800  -10.338 -31.345 1.00 32.56  ? 43  PHE B O   1 
ATOM   1061 C CB  . PHE B 1 44 ? 22.958  -8.480  -30.553 1.00 34.91  ? 43  PHE B CB  1 
ATOM   1062 C CG  . PHE B 1 44 ? 22.059  -7.447  -29.874 1.00 34.33  ? 43  PHE B CG  1 
ATOM   1063 C CD1 . PHE B 1 44 ? 20.878  -7.025  -30.481 1.00 34.79  ? 43  PHE B CD1 1 
ATOM   1064 C CD2 . PHE B 1 44 ? 22.401  -6.891  -28.641 1.00 40.28  ? 43  PHE B CD2 1 
ATOM   1065 C CE1 . PHE B 1 44 ? 20.032  -6.094  -29.871 1.00 38.62  ? 43  PHE B CE1 1 
ATOM   1066 C CE2 . PHE B 1 44 ? 21.556  -5.952  -28.036 1.00 36.66  ? 43  PHE B CE2 1 
ATOM   1067 C CZ  . PHE B 1 44 ? 20.390  -5.564  -28.655 1.00 39.13  ? 43  PHE B CZ  1 
ATOM   1068 N N   . PHE B 1 45 ? 20.573  -10.602 -29.120 1.00 30.41  ? 44  PHE B N   1 
ATOM   1069 C CA  . PHE B 1 45 ? 19.193  -11.010 -29.203 1.00 31.39  ? 44  PHE B CA  1 
ATOM   1070 C C   . PHE B 1 45 ? 18.315  -9.783  -29.055 1.00 31.54  ? 44  PHE B C   1 
ATOM   1071 O O   . PHE B 1 45 ? 18.419  -9.052  -28.053 1.00 33.09  ? 44  PHE B O   1 
ATOM   1072 C CB  . PHE B 1 45 ? 18.978  -12.031 -28.072 1.00 30.52  ? 44  PHE B CB  1 
ATOM   1073 C CG  . PHE B 1 45 ? 19.706  -13.365 -28.236 1.00 31.49  ? 44  PHE B CG  1 
ATOM   1074 C CD1 . PHE B 1 45 ? 21.059  -13.486 -27.971 1.00 31.83  ? 44  PHE B CD1 1 
ATOM   1075 C CD2 . PHE B 1 45 ? 19.005  -14.501 -28.669 1.00 30.40  ? 44  PHE B CD2 1 
ATOM   1076 C CE1 . PHE B 1 45 ? 21.729  -14.687 -28.158 1.00 31.67  ? 44  PHE B CE1 1 
ATOM   1077 C CE2 . PHE B 1 45 ? 19.659  -15.722 -28.794 1.00 31.23  ? 44  PHE B CE2 1 
ATOM   1078 C CZ  . PHE B 1 45 ? 21.015  -15.803 -28.583 1.00 32.69  ? 44  PHE B CZ  1 
ATOM   1079 N N   . PHE B 1 46 ? 17.469  -9.576  -30.066 1.00 29.73  ? 45  PHE B N   1 
ATOM   1080 C CA  . PHE B 1 46 ? 16.532  -8.453  -30.077 1.00 29.01  ? 45  PHE B CA  1 
ATOM   1081 C C   . PHE B 1 46 ? 15.517  -8.603  -28.924 1.00 31.23  ? 45  PHE B C   1 
ATOM   1082 O O   . PHE B 1 46 ? 15.204  -9.724  -28.488 1.00 31.43  ? 45  PHE B O   1 
ATOM   1083 C CB  . PHE B 1 46 ? 15.774  -8.259  -31.388 1.00 30.12  ? 45  PHE B CB  1 
ATOM   1084 C CG  . PHE B 1 46 ? 16.711  -7.771  -32.487 1.00 34.75  ? 45  PHE B CG  1 
ATOM   1085 C CD1 . PHE B 1 46 ? 17.250  -6.477  -32.439 1.00 34.15  ? 45  PHE B CD1 1 
ATOM   1086 C CD2 . PHE B 1 46 ? 17.028  -8.614  -33.563 1.00 33.00  ? 45  PHE B CD2 1 
ATOM   1087 C CE1 . PHE B 1 46 ? 18.118  -6.036  -33.443 1.00 33.46  ? 45  PHE B CE1 1 
ATOM   1088 C CE2 . PHE B 1 46 ? 17.852  -8.152  -34.600 1.00 34.08  ? 45  PHE B CE2 1 
ATOM   1089 C CZ  . PHE B 1 46 ? 18.387  -6.874  -34.524 1.00 32.83  ? 45  PHE B CZ  1 
ATOM   1090 N N   . GLY B 1 47 ? 15.008  -7.466  -28.445 1.00 32.63  ? 46  GLY B N   1 
ATOM   1091 C CA  . GLY B 1 47 ? 13.960  -7.463  -27.410 1.00 32.54  ? 46  GLY B CA  1 
ATOM   1092 C C   . GLY B 1 47 ? 14.568  -7.604  -26.011 1.00 34.99  ? 46  GLY B C   1 
ATOM   1093 O O   . GLY B 1 47 ? 14.407  -6.726  -25.164 1.00 38.75  ? 46  GLY B O   1 
ATOM   1094 N N   . THR B 1 48 ? 15.279  -8.701  -25.761 1.00 31.41  ? 47  THR B N   1 
ATOM   1095 C CA  . THR B 1 48 ? 15.950  -8.970  -24.500 1.00 33.87  ? 47  THR B CA  1 
ATOM   1096 C C   . THR B 1 48 ? 17.254  -8.188  -24.411 1.00 37.21  ? 47  THR B C   1 
ATOM   1097 O O   . THR B 1 48 ? 17.716  -7.830  -23.315 1.00 35.80  ? 47  THR B O   1 
ATOM   1098 C CB  . THR B 1 48 ? 16.220  -10.473 -24.301 1.00 37.71  ? 47  THR B CB  1 
ATOM   1099 O OG1 . THR B 1 48 ? 17.098  -10.909 -25.348 1.00 35.88  ? 47  THR B OG1 1 
ATOM   1100 C CG2 . THR B 1 48 ? 14.964  -11.328 -24.185 1.00 31.71  ? 47  THR B CG2 1 
ATOM   1101 N N   . HIS B 1 49 ? 17.858  -7.953  -25.581 1.00 35.36  ? 48  HIS B N   1 
ATOM   1102 C CA  . HIS B 1 49 ? 19.170  -7.330  -25.670 1.00 36.71  ? 48  HIS B CA  1 
ATOM   1103 C C   . HIS B 1 49 ? 20.232  -8.135  -24.933 1.00 34.25  ? 48  HIS B C   1 
ATOM   1104 O O   . HIS B 1 49 ? 21.218  -7.538  -24.484 1.00 39.96  ? 48  HIS B O   1 
ATOM   1105 C CB  . HIS B 1 49 ? 19.169  -5.843  -25.256 1.00 36.01  ? 48  HIS B CB  1 
ATOM   1106 C CG  . HIS B 1 49 ? 18.014  -5.096  -25.807 1.00 34.60  ? 48  HIS B CG  1 
ATOM   1107 N ND1 . HIS B 1 49 ? 17.284  -4.242  -25.015 1.00 38.49  ? 48  HIS B ND1 1 
ATOM   1108 C CD2 . HIS B 1 49 ? 17.400  -5.087  -26.997 1.00 32.96  ? 48  HIS B CD2 1 
ATOM   1109 C CE1 . HIS B 1 49 ? 16.280  -3.735  -25.715 1.00 45.82  ? 48  HIS B CE1 1 
ATOM   1110 N NE2 . HIS B 1 49 ? 16.321  -4.247  -26.926 1.00 41.60  ? 48  HIS B NE2 1 
ATOM   1111 N N   . GLU B 1 50 ? 20.074  -9.465  -24.846 1.00 31.33  ? 49  GLU B N   1 
ATOM   1112 C CA  . GLU B 1 50 ? 21.064  -10.377 -24.296 1.00 33.06  ? 49  GLU B CA  1 
ATOM   1113 C C   . GLU B 1 50 ? 22.113  -10.689 -25.381 1.00 34.26  ? 49  GLU B C   1 
ATOM   1114 O O   . GLU B 1 50 ? 21.867  -10.436 -26.580 1.00 34.76  ? 49  GLU B O   1 
ATOM   1115 C CB  . GLU B 1 50 ? 20.416  -11.732 -23.958 1.00 34.22  ? 49  GLU B CB  1 
ATOM   1116 C CG  . GLU B 1 50 ? 19.437  -11.695 -22.778 1.00 33.76  ? 49  GLU B CG  1 
ATOM   1117 C CD  . GLU B 1 50 ? 20.072  -11.748 -21.389 1.00 40.76  ? 49  GLU B CD  1 
ATOM   1118 O OE1 . GLU B 1 50 ? 21.260  -12.046 -21.239 1.00 42.95  ? 49  GLU B OE1 1 
ATOM   1119 O OE2 . GLU B 1 50 ? 19.343  -11.422 -20.426 1.00 40.96  ? 49  GLU B OE2 1 
ATOM   1120 N N   . THR B 1 51 ? 23.246  -11.275 -24.953 1.00 35.70  ? 50  THR B N   1 
ATOM   1121 C CA  . THR B 1 51 ? 24.296  -11.656 -25.905 1.00 37.30  ? 50  THR B CA  1 
ATOM   1122 C C   . THR B 1 51 ? 24.746  -13.080 -25.597 1.00 42.09  ? 50  THR B C   1 
ATOM   1123 O O   . THR B 1 51 ? 24.645  -13.565 -24.473 1.00 39.39  ? 50  THR B O   1 
ATOM   1124 C CB  . THR B 1 51 ? 25.471  -10.663 -25.960 1.00 41.42  ? 50  THR B CB  1 
ATOM   1125 O OG1 . THR B 1 51 ? 26.040  -10.632 -24.666 1.00 46.84  ? 50  THR B OG1 1 
ATOM   1126 C CG2 . THR B 1 51 ? 25.091  -9.227  -26.272 1.00 39.56  ? 50  THR B CG2 1 
ATOM   1127 N N   . ALA B 1 52 ? 25.189  -13.797 -26.631 1.00 38.76  ? 51  ALA B N   1 
ATOM   1128 C CA  . ALA B 1 52 ? 25.881  -15.057 -26.455 1.00 39.72  ? 51  ALA B CA  1 
ATOM   1129 C C   . ALA B 1 52 ? 26.761  -15.283 -27.676 1.00 36.80  ? 51  ALA B C   1 
ATOM   1130 O O   . ALA B 1 52 ? 26.644  -14.540 -28.645 1.00 35.72  ? 51  ALA B O   1 
ATOM   1131 C CB  . ALA B 1 52 ? 24.910  -16.204 -26.305 1.00 38.49  ? 51  ALA B CB  1 
ATOM   1132 N N   . PHE B 1 53 ? 27.648  -16.286 -27.582 1.00 37.41  ? 52  PHE B N   1 
ATOM   1133 C CA  . PHE B 1 53 ? 28.348  -16.816 -28.742 1.00 38.43  ? 52  PHE B CA  1 
ATOM   1134 C C   . PHE B 1 53 ? 27.662  -18.096 -29.235 1.00 37.68  ? 52  PHE B C   1 
ATOM   1135 O O   . PHE B 1 53 ? 27.385  -19.017 -28.461 1.00 42.35  ? 52  PHE B O   1 
ATOM   1136 C CB  . PHE B 1 53 ? 29.774  -17.132 -28.267 1.00 39.44  ? 52  PHE B CB  1 
ATOM   1137 C CG  . PHE B 1 53 ? 30.614  -15.926 -27.858 1.00 45.03  ? 52  PHE B CG  1 
ATOM   1138 C CD1 . PHE B 1 53 ? 30.816  -14.869 -28.732 1.00 42.95  ? 52  PHE B CD1 1 
ATOM   1139 C CD2 . PHE B 1 53 ? 31.159  -15.844 -26.579 1.00 44.63  ? 52  PHE B CD2 1 
ATOM   1140 C CE1 . PHE B 1 53 ? 31.591  -13.773 -28.365 1.00 46.14  ? 52  PHE B CE1 1 
ATOM   1141 C CE2 . PHE B 1 53 ? 31.908  -14.734 -26.198 1.00 50.89  ? 52  PHE B CE2 1 
ATOM   1142 C CZ  . PHE B 1 53 ? 32.127  -13.707 -27.088 1.00 43.76  ? 52  PHE B CZ  1 
ATOM   1143 N N   . LEU B 1 54 ? 27.394  -18.165 -30.548 1.00 37.37  ? 53  LEU B N   1 
ATOM   1144 C CA  . LEU B 1 54 ? 26.760  -19.325 -31.163 1.00 34.05  ? 53  LEU B CA  1 
ATOM   1145 C C   . LEU B 1 54 ? 27.509  -19.655 -32.457 1.00 34.90  ? 53  LEU B C   1 
ATOM   1146 O O   . LEU B 1 54 ? 27.999  -18.746 -33.130 1.00 35.24  ? 53  LEU B O   1 
ATOM   1147 C CB  . LEU B 1 54 ? 25.287  -19.049 -31.488 1.00 34.09  ? 53  LEU B CB  1 
ATOM   1148 C CG  . LEU B 1 54 ? 24.322  -19.006 -30.300 1.00 34.34  ? 53  LEU B CG  1 
ATOM   1149 C CD1 . LEU B 1 54 ? 22.946  -18.635 -30.793 1.00 31.93  ? 53  LEU B CD1 1 
ATOM   1150 C CD2 . LEU B 1 54 ? 24.319  -20.364 -29.634 1.00 40.20  ? 53  LEU B CD2 1 
ATOM   1151 N N   . GLY B 1 55 ? 27.512  -20.954 -32.790 1.00 37.81  ? 54  GLY B N   1 
ATOM   1152 C CA  . GLY B 1 55 ? 28.008  -21.522 -34.029 1.00 36.18  ? 54  GLY B CA  1 
ATOM   1153 C C   . GLY B 1 55 ? 26.912  -21.565 -35.093 1.00 34.99  ? 54  GLY B C   1 
ATOM   1154 O O   . GLY B 1 55 ? 25.724  -21.380 -34.797 1.00 34.55  ? 54  GLY B O   1 
ATOM   1155 N N   . PRO B 1 56 ? 27.286  -21.737 -36.380 1.00 33.43  ? 55  PRO B N   1 
ATOM   1156 C CA  . PRO B 1 56 ? 26.323  -21.734 -37.479 1.00 33.51  ? 55  PRO B CA  1 
ATOM   1157 C C   . PRO B 1 56 ? 25.164  -22.710 -37.363 1.00 32.10  ? 55  PRO B C   1 
ATOM   1158 O O   . PRO B 1 56 ? 24.132  -22.439 -37.948 1.00 32.05  ? 55  PRO B O   1 
ATOM   1159 C CB  . PRO B 1 56 ? 27.165  -21.966 -38.777 1.00 37.87  ? 55  PRO B CB  1 
ATOM   1160 C CG  . PRO B 1 56 ? 28.598  -21.925 -38.344 1.00 39.79  ? 55  PRO B CG  1 
ATOM   1161 C CD  . PRO B 1 56 ? 28.691  -21.773 -36.838 1.00 36.91  ? 55  PRO B CD  1 
ATOM   1162 N N   . LYS B 1 57 ? 25.344  -23.833 -36.642 1.00 30.78  ? 56  LYS B N   1 
ATOM   1163 C CA  . LYS B 1 57 ? 24.263  -24.815 -36.552 1.00 32.43  ? 56  LYS B CA  1 
ATOM   1164 C C   . LYS B 1 57 ? 23.031  -24.189 -35.899 1.00 35.77  ? 56  LYS B C   1 
ATOM   1165 O O   . LYS B 1 57 ? 21.904  -24.639 -36.137 1.00 33.36  ? 56  LYS B O   1 
ATOM   1166 C CB  . LYS B 1 57 ? 24.642  -26.116 -35.828 1.00 39.60  ? 56  LYS B CB  1 
ATOM   1167 C CG  . LYS B 1 57 ? 24.840  -26.016 -34.331 1.00 45.94  ? 56  LYS B CG  1 
ATOM   1168 C CD  . LYS B 1 57 ? 24.700  -27.379 -33.655 1.00 54.78  ? 56  LYS B CD  1 
ATOM   1169 C CE  . LYS B 1 57 ? 25.012  -27.374 -32.180 1.00 54.80  ? 56  LYS B CE  1 
ATOM   1170 N NZ  . LYS B 1 57 ? 23.965  -26.758 -31.354 1.00 57.25  ? 56  LYS B NZ  1 
ATOM   1171 N N   . ASP B 1 58 ? 23.273  -23.145 -35.092 1.00 31.75  ? 57  ASP B N   1 
ATOM   1172 C CA  . ASP B 1 58 ? 22.207  -22.486 -34.347 1.00 33.79  ? 57  ASP B CA  1 
ATOM   1173 C C   . ASP B 1 58 ? 21.769  -21.153 -34.960 1.00 34.79  ? 57  ASP B C   1 
ATOM   1174 O O   . ASP B 1 58 ? 20.986  -20.427 -34.333 1.00 33.55  ? 57  ASP B O   1 
ATOM   1175 C CB  . ASP B 1 58 ? 22.647  -22.354 -32.905 1.00 33.06  ? 57  ASP B CB  1 
ATOM   1176 C CG  . ASP B 1 58 ? 22.828  -23.682 -32.187 1.00 39.27  ? 57  ASP B CG  1 
ATOM   1177 O OD1 . ASP B 1 58 ? 21.895  -24.529 -32.288 1.00 36.60  ? 57  ASP B OD1 1 
ATOM   1178 O OD2 . ASP B 1 58 ? 23.863  -23.818 -31.510 1.00 40.94  ? 57  ASP B OD2 1 
ATOM   1179 N N   . LEU B 1 59 ? 22.273  -20.823 -36.164 1.00 33.16  ? 58  LEU B N   1 
ATOM   1180 C CA  . LEU B 1 59 ? 21.986  -19.531 -36.788 1.00 33.00  ? 58  LEU B CA  1 
ATOM   1181 C C   . LEU B 1 59 ? 21.223  -19.732 -38.089 1.00 31.39  ? 58  LEU B C   1 
ATOM   1182 O O   . LEU B 1 59 ? 21.703  -20.402 -39.012 1.00 31.61  ? 58  LEU B O   1 
ATOM   1183 C CB  . LEU B 1 59 ? 23.292  -18.780 -37.017 1.00 32.10  ? 58  LEU B CB  1 
ATOM   1184 C CG  . LEU B 1 59 ? 24.116  -18.523 -35.758 1.00 31.53  ? 58  LEU B CG  1 
ATOM   1185 C CD1 . LEU B 1 59 ? 25.427  -17.850 -36.110 1.00 33.53  ? 58  LEU B CD1 1 
ATOM   1186 C CD2 . LEU B 1 59 ? 23.316  -17.640 -34.747 1.00 36.21  ? 58  LEU B CD2 1 
ATOM   1187 N N   . PHE B 1 60 ? 20.049  -19.112 -38.160 1.00 29.69  ? 59  PHE B N   1 
ATOM   1188 C CA  . PHE B 1 60 ? 19.102  -19.318 -39.242 1.00 32.60  ? 59  PHE B CA  1 
ATOM   1189 C C   . PHE B 1 60 ? 18.907  -17.985 -39.961 1.00 35.24  ? 59  PHE B C   1 
ATOM   1190 O O   . PHE B 1 60 ? 18.320  -17.066 -39.399 1.00 31.92  ? 59  PHE B O   1 
ATOM   1191 C CB  . PHE B 1 60 ? 17.770  -19.873 -38.720 1.00 30.00  ? 59  PHE B CB  1 
ATOM   1192 C CG  . PHE B 1 60 ? 17.888  -21.284 -38.133 1.00 30.00  ? 59  PHE B CG  1 
ATOM   1193 C CD1 . PHE B 1 60 ? 18.401  -21.472 -36.857 1.00 30.92  ? 59  PHE B CD1 1 
ATOM   1194 C CD2 . PHE B 1 60 ? 17.427  -22.394 -38.853 1.00 34.16  ? 59  PHE B CD2 1 
ATOM   1195 C CE1 . PHE B 1 60 ? 18.502  -22.751 -36.317 1.00 33.01  ? 59  PHE B CE1 1 
ATOM   1196 C CE2 . PHE B 1 60 ? 17.523  -23.675 -38.318 1.00 32.96  ? 59  PHE B CE2 1 
ATOM   1197 C CZ  . PHE B 1 60 ? 18.080  -23.853 -37.057 1.00 34.55  ? 59  PHE B CZ  1 
ATOM   1198 N N   . PRO B 1 61 ? 19.465  -17.777 -41.178 1.00 37.08  ? 60  PRO B N   1 
ATOM   1199 C CA  . PRO B 1 61 ? 19.205  -16.519 -41.894 1.00 33.60  ? 60  PRO B CA  1 
ATOM   1200 C C   . PRO B 1 61 ? 17.755  -16.017 -41.868 1.00 33.66  ? 60  PRO B C   1 
ATOM   1201 O O   . PRO B 1 61 ? 16.800  -16.761 -42.099 1.00 36.11  ? 60  PRO B O   1 
ATOM   1202 C CB  . PRO B 1 61 ? 19.776  -16.830 -43.309 1.00 37.47  ? 60  PRO B CB  1 
ATOM   1203 C CG  . PRO B 1 61 ? 20.966  -17.720 -42.989 1.00 43.42  ? 60  PRO B CG  1 
ATOM   1204 C CD  . PRO B 1 61 ? 20.405  -18.682 -41.883 1.00 40.43  ? 60  PRO B CD  1 
ATOM   1205 N N   . TYR B 1 62 ? 17.587  -14.728 -41.494 1.00 36.02  ? 61  TYR B N   1 
ATOM   1206 C CA  . TYR B 1 62 ? 16.299  -14.155 -41.180 1.00 37.61  ? 61  TYR B CA  1 
ATOM   1207 C C   . TYR B 1 62 ? 15.288  -14.256 -42.316 1.00 37.30  ? 61  TYR B C   1 
ATOM   1208 O O   . TYR B 1 62 ? 14.175  -14.695 -42.070 1.00 36.36  ? 61  TYR B O   1 
ATOM   1209 C CB  . TYR B 1 62 ? 16.443  -12.713 -40.682 1.00 36.63  ? 61  TYR B CB  1 
ATOM   1210 C CG  . TYR B 1 62 ? 15.123  -12.003 -40.438 1.00 40.05  ? 61  TYR B CG  1 
ATOM   1211 C CD1 . TYR B 1 62 ? 14.365  -12.275 -39.306 1.00 41.36  ? 61  TYR B CD1 1 
ATOM   1212 C CD2 . TYR B 1 62 ? 14.663  -11.020 -41.313 1.00 47.73  ? 61  TYR B CD2 1 
ATOM   1213 C CE1 . TYR B 1 62 ? 13.165  -11.628 -39.076 1.00 42.11  ? 61  TYR B CE1 1 
ATOM   1214 C CE2 . TYR B 1 62 ? 13.475  -10.340 -41.080 1.00 48.69  ? 61  TYR B CE2 1 
ATOM   1215 C CZ  . TYR B 1 62 ? 12.728  -10.651 -39.955 1.00 47.70  ? 61  TYR B CZ  1 
ATOM   1216 O OH  . TYR B 1 62 ? 11.563  -10.004 -39.703 1.00 45.10  ? 61  TYR B OH  1 
ATOM   1217 N N   . ASP B 1 63 ? 15.664  -13.790 -43.519 1.00 44.01  ? 62  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 63 ? 14.796  -13.770 -44.695 1.00 49.63  ? 62  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 63 ? 14.230  -15.159 -44.989 1.00 38.21  ? 62  ASP B C   1 
ATOM   1220 O O   . ASP B 1 63 ? 13.014  -15.336 -45.067 1.00 49.32  ? 62  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 63 ? 15.497  -13.149 -45.891 1.00 55.82  ? 62  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 63 ? 15.298  -11.649 -46.066 1.00 72.30  ? 62  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 63 ? 14.527  -11.050 -45.273 1.00 74.16  ? 62  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 63 ? 15.914  -11.086 -47.001 1.00 77.09  ? 62  ASP B OD2 1 
ATOM   1225 N N   . LYS B 1 64 ? 15.120  -16.136 -45.119 1.00 46.71  ? 63  LYS B N   1 
ATOM   1226 C CA  . LYS B 1 64 ? 14.744  -17.519 -45.355 1.00 46.99  ? 63  LYS B CA  1 
ATOM   1227 C C   . LYS B 1 64 ? 13.785  -18.022 -44.276 1.00 42.89  ? 63  LYS B C   1 
ATOM   1228 O O   . LYS B 1 64 ? 12.863  -18.778 -44.587 1.00 51.44  ? 63  LYS B O   1 
ATOM   1229 C CB  . LYS B 1 64 ? 16.005  -18.386 -45.371 1.00 48.19  ? 63  LYS B CB  1 
ATOM   1230 C CG  . LYS B 1 64 ? 15.700  -19.863 -45.558 1.00 49.43  ? 63  LYS B CG  1 
ATOM   1231 C CD  . LYS B 1 64 ? 16.950  -20.644 -45.915 1.00 49.61  ? 63  LYS B CD  1 
ATOM   1232 C CE  . LYS B 1 64 ? 16.636  -21.870 -46.731 1.00 50.27  ? 63  LYS B CE  1 
ATOM   1233 N NZ  . LYS B 1 64 ? 15.802  -22.803 -45.984 1.00 50.12  ? 63  LYS B NZ  1 
ATOM   1234 N N   . SER B 1 65 ? 13.974  -17.588 -43.020 1.00 39.37  ? 64  SER B N   1 
ATOM   1235 C CA  . SER B 1 65 ? 13.344  -18.310 -41.906 1.00 43.61  ? 64  SER B CA  1 
ATOM   1236 C C   . SER B 1 65 ? 12.221  -17.552 -41.186 1.00 44.54  ? 64  SER B C   1 
ATOM   1237 O O   . SER B 1 65 ? 11.574  -18.105 -40.299 1.00 43.09  ? 64  SER B O   1 
ATOM   1238 C CB  . SER B 1 65 ? 14.385  -18.844 -40.967 1.00 47.44  ? 64  SER B CB  1 
ATOM   1239 O OG  . SER B 1 65 ? 15.139  -17.762 -40.440 1.00 61.79  ? 64  SER B OG  1 
ATOM   1240 N N   . LYS B 1 66 ? 11.894  -16.325 -41.617 1.00 42.92  ? 65  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 66 ? 10.984  -15.491 -40.838 1.00 40.79  ? 65  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 66 ? 9.550   -16.026 -40.821 1.00 45.74  ? 65  LYS B C   1 
ATOM   1243 O O   . LYS B 1 66 ? 8.832   -15.865 -39.838 1.00 47.15  ? 65  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 66 ? 11.065  -14.007 -41.216 1.00 40.62  ? 65  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 66 ? 10.480  -13.663 -42.583 1.00 46.48  ? 65  LYS B CG  1 
ATOM   1246 N N   . ASP B 1 67 ? 9.087   -16.674 -41.886 1.00 43.94  ? 66  ASP B N   1 
ATOM   1247 C CA  . ASP B 1 67 ? 7.678   -17.034 -41.816 1.00 46.03  ? 66  ASP B CA  1 
ATOM   1248 C C   . ASP B 1 67 ? 7.495   -18.248 -40.896 1.00 47.12  ? 66  ASP B C   1 
ATOM   1249 O O   . ASP B 1 67 ? 6.426   -18.431 -40.307 1.00 54.92  ? 66  ASP B O   1 
ATOM   1250 C CB  . ASP B 1 67 ? 7.005   -16.969 -43.179 1.00 56.69  ? 66  ASP B CB  1 
ATOM   1251 C CG  . ASP B 1 67 ? 7.499   -17.970 -44.208 1.00 69.37  ? 66  ASP B CG  1 
ATOM   1252 O OD1 . ASP B 1 67 ? 7.429   -17.653 -45.418 1.00 85.08  ? 66  ASP B OD1 1 
ATOM   1253 O OD2 . ASP B 1 67 ? 7.926   -19.063 -43.794 1.00 82.85  ? 66  ASP B OD2 1 
ATOM   1254 N N   . LYS B 1 68 ? 8.564   -19.032 -40.728 1.00 45.57  ? 67  LYS B N   1 
ATOM   1255 C CA  . LYS B 1 68 ? 8.546   -20.195 -39.848 1.00 42.90  ? 67  LYS B CA  1 
ATOM   1256 C C   . LYS B 1 68 ? 8.707   -19.792 -38.380 1.00 37.45  ? 67  LYS B C   1 
ATOM   1257 O O   . LYS B 1 68 ? 7.944   -20.249 -37.532 1.00 41.44  ? 67  LYS B O   1 
ATOM   1258 C CB  . LYS B 1 68 ? 9.651   -21.153 -40.290 1.00 41.95  ? 67  LYS B CB  1 
ATOM   1259 C CG  . LYS B 1 68 ? 9.683   -22.484 -39.540 1.00 49.15  ? 67  LYS B CG  1 
ATOM   1260 C CD  . LYS B 1 68 ? 10.831  -23.314 -40.112 1.00 61.98  ? 67  LYS B CD  1 
ATOM   1261 C CE  . LYS B 1 68 ? 11.029  -24.612 -39.398 1.00 59.06  ? 67  LYS B CE  1 
ATOM   1262 N NZ  . LYS B 1 68 ? 9.816   -25.427 -39.490 1.00 63.69  ? 67  LYS B NZ  1 
ATOM   1263 N N   . TYR B 1 69 ? 9.704   -18.954 -38.070 1.00 36.75  ? 68  TYR B N   1 
ATOM   1264 C CA  . TYR B 1 69 ? 10.095  -18.666 -36.691 1.00 33.69  ? 68  TYR B CA  1 
ATOM   1265 C C   . TYR B 1 69 ? 9.586   -17.297 -36.239 1.00 37.09  ? 68  TYR B C   1 
ATOM   1266 O O   . TYR B 1 69 ? 9.660   -16.983 -35.058 1.00 42.24  ? 68  TYR B O   1 
ATOM   1267 C CB  . TYR B 1 69 ? 11.618  -18.739 -36.535 1.00 34.42  ? 68  TYR B CB  1 
ATOM   1268 C CG  . TYR B 1 69 ? 12.238  -20.109 -36.814 1.00 36.95  ? 68  TYR B CG  1 
ATOM   1269 C CD1 . TYR B 1 69 ? 11.717  -21.265 -36.244 1.00 36.42  ? 68  TYR B CD1 1 
ATOM   1270 C CD2 . TYR B 1 69 ? 13.361  -20.234 -37.634 1.00 40.03  ? 68  TYR B CD2 1 
ATOM   1271 C CE1 . TYR B 1 69 ? 12.295  -22.510 -36.487 1.00 40.46  ? 68  TYR B CE1 1 
ATOM   1272 C CE2 . TYR B 1 69 ? 13.930  -21.472 -37.906 1.00 41.43  ? 68  TYR B CE2 1 
ATOM   1273 C CZ  . TYR B 1 69 ? 13.389  -22.615 -37.327 1.00 41.45  ? 68  TYR B CZ  1 
ATOM   1274 O OH  . TYR B 1 69 ? 13.948  -23.826 -37.574 1.00 39.86  ? 68  TYR B OH  1 
ATOM   1275 N N   . GLY B 1 70 ? 9.120   -16.454 -37.165 1.00 39.47  ? 69  GLY B N   1 
ATOM   1276 C CA  . GLY B 1 70 ? 8.810   -15.081 -36.787 1.00 42.51  ? 69  GLY B CA  1 
ATOM   1277 C C   . GLY B 1 70 ? 7.399   -14.871 -36.235 1.00 48.89  ? 69  GLY B C   1 
ATOM   1278 O O   . GLY B 1 70 ? 6.782   -13.836 -36.515 1.00 46.62  ? 69  GLY B O   1 
ATOM   1279 N N   . LYS B 1 71 ? 6.881   -15.835 -35.454 1.00 46.43  ? 70  LYS B N   1 
ATOM   1280 C CA  . LYS B 1 71 ? 5.521   -15.714 -34.946 1.00 47.90  ? 70  LYS B CA  1 
ATOM   1281 C C   . LYS B 1 71 ? 5.582   -15.264 -33.497 1.00 49.84  ? 70  LYS B C   1 
ATOM   1282 O O   . LYS B 1 71 ? 6.442   -15.733 -32.753 1.00 41.15  ? 70  LYS B O   1 
ATOM   1283 C CB  . LYS B 1 71 ? 4.700   -17.010 -34.954 1.00 55.32  ? 70  LYS B CB  1 
ATOM   1284 C CG  . LYS B 1 71 ? 4.029   -17.368 -36.281 1.00 64.93  ? 70  LYS B CG  1 
ATOM   1285 C CD  . LYS B 1 71 ? 4.836   -18.304 -37.176 1.00 69.56  ? 70  LYS B CD  1 
ATOM   1286 C CE  . LYS B 1 71 ? 4.109   -18.897 -38.358 1.00 75.01  ? 70  LYS B CE  1 
ATOM   1287 N NZ  . LYS B 1 71 ? 3.972   -17.955 -39.477 1.00 78.92  ? 70  LYS B NZ  1 
ATOM   1288 N N   . PRO B 1 72 ? 4.665   -14.378 -33.038 1.00 47.85  ? 71  PRO B N   1 
ATOM   1289 C CA  . PRO B 1 72 ? 4.602   -14.033 -31.613 1.00 46.95  ? 71  PRO B CA  1 
ATOM   1290 C C   . PRO B 1 72 ? 4.432   -15.221 -30.667 1.00 41.96  ? 71  PRO B C   1 
ATOM   1291 O O   . PRO B 1 72 ? 3.840   -16.238 -31.034 1.00 39.48  ? 71  PRO B O   1 
ATOM   1292 C CB  . PRO B 1 72 ? 3.462   -13.002 -31.537 1.00 47.25  ? 71  PRO B CB  1 
ATOM   1293 C CG  . PRO B 1 72 ? 3.484   -12.391 -32.922 1.00 51.53  ? 71  PRO B CG  1 
ATOM   1294 C CD  . PRO B 1 72 ? 3.723   -13.592 -33.853 1.00 47.06  ? 71  PRO B CD  1 
ATOM   1295 N N   . ASN B 1 73 ? 5.012   -15.097 -29.463 1.00 43.27  ? 72  ASN B N   1 
ATOM   1296 C CA  . ASN B 1 73 ? 4.817   -16.084 -28.406 1.00 40.06  ? 72  ASN B CA  1 
ATOM   1297 C C   . ASN B 1 73 ? 4.830   -15.371 -27.040 1.00 45.24  ? 72  ASN B C   1 
ATOM   1298 O O   . ASN B 1 73 ? 4.870   -14.137 -26.965 1.00 42.83  ? 72  ASN B O   1 
ATOM   1299 C CB  . ASN B 1 73 ? 5.820   -17.231 -28.476 1.00 41.21  ? 72  ASN B CB  1 
ATOM   1300 C CG  . ASN B 1 73 ? 7.247   -16.784 -28.230 1.00 41.21  ? 72  ASN B CG  1 
ATOM   1301 O OD1 . ASN B 1 73 ? 7.503   -16.030 -27.285 1.00 38.53  ? 72  ASN B OD1 1 
ATOM   1302 N ND2 . ASN B 1 73 ? 8.195   -17.201 -29.078 1.00 36.54  ? 72  ASN B ND2 1 
ATOM   1303 N N   . LYS B 1 74 ? 4.846   -16.158 -25.953 1.00 44.39  ? 73  LYS B N   1 
ATOM   1304 C CA  . LYS B 1 74 ? 4.702   -15.598 -24.611 1.00 46.16  ? 73  LYS B CA  1 
ATOM   1305 C C   . LYS B 1 74 ? 6.046   -15.533 -23.860 1.00 49.28  ? 73  LYS B C   1 
ATOM   1306 O O   . LYS B 1 74 ? 6.063   -15.428 -22.632 1.00 48.37  ? 73  LYS B O   1 
ATOM   1307 C CB  . LYS B 1 74 ? 3.595   -16.376 -23.867 1.00 44.35  ? 73  LYS B CB  1 
ATOM   1308 N N   . ARG B 1 75 ? 7.190   -15.628 -24.558 1.00 37.25  ? 74  ARG B N   1 
ATOM   1309 C CA  . ARG B 1 75 ? 8.467   -15.485 -23.863 1.00 35.78  ? 74  ARG B CA  1 
ATOM   1310 C C   . ARG B 1 75 ? 8.763   -13.984 -23.687 1.00 36.33  ? 74  ARG B C   1 
ATOM   1311 O O   . ARG B 1 75 ? 8.497   -13.163 -24.579 1.00 37.39  ? 74  ARG B O   1 
ATOM   1312 C CB  . ARG B 1 75 ? 9.603   -16.270 -24.543 1.00 35.86  ? 74  ARG B CB  1 
ATOM   1313 C CG  . ARG B 1 75 ? 9.475   -17.772 -24.808 1.00 36.42  ? 74  ARG B CG  1 
ATOM   1314 C CD  . ARG B 1 75 ? 9.261   -18.554 -23.501 1.00 37.47  ? 74  ARG B CD  1 
ATOM   1315 N NE  . ARG B 1 75 ? 9.452   -19.992 -23.705 1.00 36.30  ? 74  ARG B NE  1 
ATOM   1316 C CZ  . ARG B 1 75 ? 10.580  -20.627 -23.512 1.00 39.01  ? 74  ARG B CZ  1 
ATOM   1317 N NH1 . ARG B 1 75 ? 11.641  -20.001 -22.999 1.00 40.86  ? 74  ARG B NH1 1 
ATOM   1318 N NH2 . ARG B 1 75 ? 10.654  -21.892 -23.880 1.00 42.19  ? 74  ARG B NH2 1 
ATOM   1319 N N   . LYS B 1 76 ? 9.273   -13.611 -22.503 1.00 34.36  ? 75  LYS B N   1 
ATOM   1320 C CA  . LYS B 1 76 ? 9.630   -12.231 -22.201 1.00 32.58  ? 75  LYS B CA  1 
ATOM   1321 C C   . LYS B 1 76 ? 10.666  -11.726 -23.213 1.00 32.64  ? 75  LYS B C   1 
ATOM   1322 O O   . LYS B 1 76 ? 11.725  -12.342 -23.363 1.00 33.31  ? 75  LYS B O   1 
ATOM   1323 C CB  . LYS B 1 76 ? 10.169  -12.104 -20.767 1.00 34.28  ? 75  LYS B CB  1 
ATOM   1324 C CG  . LYS B 1 76 ? 10.570  -10.672 -20.402 1.00 36.01  ? 75  LYS B CG  1 
ATOM   1325 C CD  . LYS B 1 76 ? 11.079  -10.591 -18.969 1.00 40.38  ? 75  LYS B CD  1 
ATOM   1326 C CE  . LYS B 1 76 ? 11.385  -9.156  -18.604 1.00 47.05  ? 75  LYS B CE  1 
ATOM   1327 N NZ  . LYS B 1 76 ? 11.895  -9.048  -17.227 1.00 51.34  ? 75  LYS B NZ  1 
ATOM   1328 N N   . GLY B 1 77 ? 10.301  -10.626 -23.886 1.00 33.57  ? 76  GLY B N   1 
ATOM   1329 C CA  . GLY B 1 77 ? 11.200  -9.878  -24.774 1.00 34.83  ? 76  GLY B CA  1 
ATOM   1330 C C   . GLY B 1 77 ? 11.055  -10.327 -26.234 1.00 36.62  ? 76  GLY B C   1 
ATOM   1331 O O   . GLY B 1 77 ? 11.610  -9.687  -27.131 1.00 35.29  ? 76  GLY B O   1 
ATOM   1332 N N   . PHE B 1 78 ? 10.292  -11.404 -26.486 1.00 32.49  ? 77  PHE B N   1 
ATOM   1333 C CA  . PHE B 1 78 ? 10.197  -11.990 -27.828 1.00 30.70  ? 77  PHE B CA  1 
ATOM   1334 C C   . PHE B 1 78 ? 9.451   -11.064 -28.777 1.00 34.31  ? 77  PHE B C   1 
ATOM   1335 O O   . PHE B 1 78 ? 9.906   -10.794 -29.890 1.00 32.64  ? 77  PHE B O   1 
ATOM   1336 C CB  . PHE B 1 78 ? 9.520   -13.365 -27.841 1.00 31.78  ? 77  PHE B CB  1 
ATOM   1337 C CG  . PHE B 1 78 ? 9.763   -14.095 -29.145 1.00 33.13  ? 77  PHE B CG  1 
ATOM   1338 C CD1 . PHE B 1 78 ? 10.847  -14.960 -29.288 1.00 30.00  ? 77  PHE B CD1 1 
ATOM   1339 C CD2 . PHE B 1 78 ? 8.883   -13.936 -30.208 1.00 33.80  ? 77  PHE B CD2 1 
ATOM   1340 C CE1 . PHE B 1 78 ? 11.079  -15.615 -30.502 1.00 29.95  ? 77  PHE B CE1 1 
ATOM   1341 C CE2 . PHE B 1 78 ? 9.116   -14.609 -31.407 1.00 35.11  ? 77  PHE B CE2 1 
ATOM   1342 C CZ  . PHE B 1 78 ? 10.201  -15.458 -31.531 1.00 32.50  ? 77  PHE B CZ  1 
ATOM   1343 N N   . ASN B 1 79 ? 8.292   -10.555 -28.364 1.00 32.02  ? 78  ASN B N   1 
ATOM   1344 C CA  . ASN B 1 79 ? 7.484   -9.772  -29.290 1.00 36.95  ? 78  ASN B CA  1 
ATOM   1345 C C   . ASN B 1 79 ? 8.164   -8.415  -29.541 1.00 36.63  ? 78  ASN B C   1 
ATOM   1346 O O   . ASN B 1 79 ? 8.095   -7.868  -30.656 1.00 36.54  ? 78  ASN B O   1 
ATOM   1347 C CB  . ASN B 1 79 ? 6.014   -9.751  -28.857 1.00 41.01  ? 78  ASN B CB  1 
ATOM   1348 C CG  . ASN B 1 79 ? 5.305   -11.097 -28.936 1.00 43.42  ? 78  ASN B CG  1 
ATOM   1349 O OD1 . ASN B 1 79 ? 5.778   -12.042 -29.581 1.00 42.59  ? 78  ASN B OD1 1 
ATOM   1350 N ND2 . ASN B 1 79 ? 4.166   -11.231 -28.267 1.00 43.55  ? 78  ASN B ND2 1 
ATOM   1351 N N   . GLU B 1 80 ? 8.872   -7.897  -28.529 1.00 34.17  ? 79  GLU B N   1 
ATOM   1352 C CA  . GLU B 1 80 ? 9.614   -6.657  -28.678 1.00 37.77  ? 79  GLU B CA  1 
ATOM   1353 C C   . GLU B 1 80 ? 10.764  -6.893  -29.660 1.00 39.88  ? 79  GLU B C   1 
ATOM   1354 O O   . GLU B 1 80 ? 11.122  -5.985  -30.407 1.00 38.88  ? 79  GLU B O   1 
ATOM   1355 C CB  . GLU B 1 80 ? 10.254  -6.155  -27.382 1.00 37.48  ? 79  GLU B CB  1 
ATOM   1356 C CG  . GLU B 1 80 ? 9.290   -5.441  -26.434 1.00 46.69  ? 79  GLU B CG  1 
ATOM   1357 N N   . GLY B 1 81 ? 11.360  -8.097  -29.600 1.00 34.78  ? 80  GLY B N   1 
ATOM   1358 C CA  . GLY B 1 81 ? 12.475  -8.480  -30.467 1.00 36.79  ? 80  GLY B CA  1 
ATOM   1359 C C   . GLY B 1 81 ? 12.005  -8.575  -31.915 1.00 35.50  ? 80  GLY B C   1 
ATOM   1360 O O   . GLY B 1 81 ? 12.744  -8.211  -32.848 1.00 35.65  ? 80  GLY B O   1 
ATOM   1361 N N   . LEU B 1 82 ? 10.772  -9.051  -32.101 1.00 31.88  ? 81  LEU B N   1 
ATOM   1362 C CA  . LEU B 1 82 ? 10.190  -9.117  -33.435 1.00 38.66  ? 81  LEU B CA  1 
ATOM   1363 C C   . LEU B 1 82 ? 10.044  -7.697  -33.987 1.00 36.71  ? 81  LEU B C   1 
ATOM   1364 O O   . LEU B 1 82 ? 10.368  -7.445  -35.139 1.00 35.93  ? 81  LEU B O   1 
ATOM   1365 C CB  . LEU B 1 82 ? 8.848   -9.855  -33.482 1.00 36.34  ? 81  LEU B CB  1 
ATOM   1366 C CG  . LEU B 1 82 ? 8.886   -11.371 -33.271 1.00 36.97  ? 81  LEU B CG  1 
ATOM   1367 C CD1 . LEU B 1 82 ? 7.502   -12.057 -33.314 1.00 34.48  ? 81  LEU B CD1 1 
ATOM   1368 C CD2 . LEU B 1 82 ? 9.851   -12.027 -34.262 1.00 33.04  ? 81  LEU B CD2 1 
ATOM   1369 N N   . TRP B 1 83 ? 9.524   -6.780  -33.164 1.00 34.28  ? 82  TRP B N   1 
ATOM   1370 C CA  . TRP B 1 83 ? 9.406   -5.382  -33.549 1.00 37.00  ? 82  TRP B CA  1 
ATOM   1371 C C   . TRP B 1 83 ? 10.757  -4.805  -33.977 1.00 37.22  ? 82  TRP B C   1 
ATOM   1372 O O   . TRP B 1 83 ? 10.831  -4.156  -35.028 1.00 36.46  ? 82  TRP B O   1 
ATOM   1373 C CB  . TRP B 1 83 ? 8.816   -4.543  -32.409 1.00 41.34  ? 82  TRP B CB  1 
ATOM   1374 C CG  . TRP B 1 83 ? 8.532   -3.140  -32.873 1.00 40.82  ? 82  TRP B CG  1 
ATOM   1375 C CD1 . TRP B 1 83 ? 7.391   -2.706  -33.479 1.00 44.21  ? 82  TRP B CD1 1 
ATOM   1376 C CD2 . TRP B 1 83 ? 9.459   -2.037  -32.900 1.00 43.04  ? 82  TRP B CD2 1 
ATOM   1377 N NE1 . TRP B 1 83 ? 7.526   -1.392  -33.848 1.00 45.69  ? 82  TRP B NE1 1 
ATOM   1378 C CE2 . TRP B 1 83 ? 8.785   -0.961  -33.515 1.00 44.75  ? 82  TRP B CE2 1 
ATOM   1379 C CE3 . TRP B 1 83 ? 10.781  -1.858  -32.465 1.00 42.49  ? 82  TRP B CE3 1 
ATOM   1380 C CZ2 . TRP B 1 83 ? 9.389   0.281   -33.689 1.00 43.06  ? 82  TRP B CZ2 1 
ATOM   1381 C CZ3 . TRP B 1 83 ? 11.376  -0.632  -32.647 1.00 45.16  ? 82  TRP B CZ3 1 
ATOM   1382 C CH2 . TRP B 1 83 ? 10.692  0.410   -33.276 1.00 40.06  ? 82  TRP B CH2 1 
ATOM   1383 N N   . GLU B 1 84 ? 11.801  -5.081  -33.181 1.00 33.79  ? 83  GLU B N   1 
ATOM   1384 C CA  . GLU B 1 84 ? 13.126  -4.503  -33.384 1.00 35.23  ? 83  GLU B CA  1 
ATOM   1385 C C   . GLU B 1 84 ? 13.751  -4.984  -34.699 1.00 34.89  ? 83  GLU B C   1 
ATOM   1386 O O   . GLU B 1 84 ? 14.277  -4.176  -35.472 1.00 35.64  ? 83  GLU B O   1 
ATOM   1387 C CB  . GLU B 1 84 ? 14.078  -4.809  -32.237 1.00 34.95  ? 83  GLU B CB  1 
ATOM   1388 C CG  . GLU B 1 84 ? 13.649  -4.076  -30.960 1.00 39.83  ? 83  GLU B CG  1 
ATOM   1389 C CD  . GLU B 1 84 ? 14.530  -4.337  -29.766 1.00 37.74  ? 83  GLU B CD  1 
ATOM   1390 O OE1 . GLU B 1 84 ? 15.459  -5.173  -29.885 1.00 34.98  ? 83  GLU B OE1 1 
ATOM   1391 O OE2 . GLU B 1 84 ? 14.335  -3.689  -28.700 1.00 39.91  ? 83  GLU B OE2 1 
ATOM   1392 N N   . ILE B 1 85 ? 13.701  -6.297  -34.930 1.00 33.06  ? 84  ILE B N   1 
ATOM   1393 C CA  . ILE B 1 85 ? 14.336  -6.889  -36.112 1.00 33.23  ? 84  ILE B CA  1 
ATOM   1394 C C   . ILE B 1 85 ? 13.711  -6.351  -37.398 1.00 31.76  ? 84  ILE B C   1 
ATOM   1395 O O   . ILE B 1 85 ? 14.420  -6.153  -38.406 1.00 32.85  ? 84  ILE B O   1 
ATOM   1396 C CB  . ILE B 1 85 ? 14.341  -8.425  -36.089 1.00 31.94  ? 84  ILE B CB  1 
ATOM   1397 C CG1 . ILE B 1 85 ? 15.368  -8.985  -37.107 1.00 32.56  ? 84  ILE B CG1 1 
ATOM   1398 C CG2 . ILE B 1 85 ? 12.945  -8.994  -36.344 1.00 32.95  ? 84  ILE B CG2 1 
ATOM   1399 C CD1 . ILE B 1 85 ? 15.917  -10.369 -36.757 1.00 33.25  ? 84  ILE B CD1 1 
ATOM   1400 N N   . GLN B 1 86 ? 12.401  -6.089  -37.335 1.00 34.50  ? 85  GLN B N   1 
ATOM   1401 C CA  . GLN B 1 86 ? 11.608  -5.480  -38.390 1.00 36.52  ? 85  GLN B CA  1 
ATOM   1402 C C   . GLN B 1 86 ? 11.884  -3.980  -38.559 1.00 41.65  ? 85  GLN B C   1 
ATOM   1403 O O   . GLN B 1 86 ? 11.913  -3.482  -39.682 1.00 42.61  ? 85  GLN B O   1 
ATOM   1404 C CB  . GLN B 1 86 ? 10.134  -5.783  -38.121 1.00 44.48  ? 85  GLN B CB  1 
ATOM   1405 N N   . ASN B 1 87 ? 12.033  -3.220  -37.476 1.00 36.99  ? 86  ASN B N   1 
ATOM   1406 C CA  . ASN B 1 87 ? 11.885  -1.778  -37.643 1.00 34.72  ? 86  ASN B CA  1 
ATOM   1407 C C   . ASN B 1 87 ? 13.194  -1.036  -37.429 1.00 36.25  ? 86  ASN B C   1 
ATOM   1408 O O   . ASN B 1 87 ? 13.365  0.085   -37.933 1.00 39.13  ? 86  ASN B O   1 
ATOM   1409 C CB  . ASN B 1 87 ? 10.906  -1.221  -36.616 1.00 39.91  ? 86  ASN B CB  1 
ATOM   1410 C CG  . ASN B 1 87 ? 9.514   -1.664  -36.981 1.00 44.54  ? 86  ASN B CG  1 
ATOM   1411 O OD1 . ASN B 1 87 ? 8.891   -1.057  -37.852 1.00 54.02  ? 86  ASN B OD1 1 
ATOM   1412 N ND2 . ASN B 1 87 ? 9.048   -2.760  -36.406 1.00 49.28  ? 86  ASN B ND2 1 
ATOM   1413 N N   . ASN B 1 88 ? 14.127  -1.625  -36.693 1.00 35.16  ? 87  ASN B N   1 
ATOM   1414 C CA  . ASN B 1 88 ? 15.389  -0.930  -36.502 1.00 33.47  ? 87  ASN B CA  1 
ATOM   1415 C C   . ASN B 1 88 ? 16.470  -1.920  -36.088 1.00 33.62  ? 87  ASN B C   1 
ATOM   1416 O O   . ASN B 1 88 ? 17.075  -1.830  -35.007 1.00 33.18  ? 87  ASN B O   1 
ATOM   1417 C CB  . ASN B 1 88 ? 15.229  0.267   -35.560 1.00 42.53  ? 87  ASN B CB  1 
ATOM   1418 C CG  . ASN B 1 88 ? 16.356  1.282   -35.655 1.00 40.42  ? 87  ASN B CG  1 
ATOM   1419 O OD1 . ASN B 1 88 ? 17.393  1.061   -36.302 1.00 38.15  ? 87  ASN B OD1 1 
ATOM   1420 N ND2 . ASN B 1 88 ? 16.165  2.424   -35.002 1.00 40.58  ? 87  ASN B ND2 1 
ATOM   1421 N N   . PRO B 1 89 ? 16.750  -2.915  -36.980 1.00 35.22  ? 88  PRO B N   1 
ATOM   1422 C CA  . PRO B 1 89 ? 17.685  -3.994  -36.660 1.00 30.88  ? 88  PRO B CA  1 
ATOM   1423 C C   . PRO B 1 89 ? 19.099  -3.546  -36.341 1.00 30.68  ? 88  PRO B C   1 
ATOM   1424 O O   . PRO B 1 89 ? 19.868  -4.291  -35.719 1.00 33.01  ? 88  PRO B O   1 
ATOM   1425 C CB  . PRO B 1 89 ? 17.638  -4.900  -37.916 1.00 30.82  ? 88  PRO B CB  1 
ATOM   1426 C CG  . PRO B 1 89 ? 17.108  -3.982  -39.037 1.00 30.18  ? 88  PRO B CG  1 
ATOM   1427 C CD  . PRO B 1 89 ? 16.113  -3.070  -38.299 1.00 33.44  ? 88  PRO B CD  1 
ATOM   1428 N N   . HIS B 1 90 ? 19.474  -2.361  -36.881 1.00 30.82  ? 89  HIS B N   1 
ATOM   1429 C CA  . HIS B 1 90 ? 20.855  -1.940  -36.811 1.00 31.14  ? 89  HIS B CA  1 
ATOM   1430 C C   . HIS B 1 90 ? 21.095  -0.879  -35.734 1.00 34.53  ? 89  HIS B C   1 
ATOM   1431 O O   . HIS B 1 90 ? 22.212  -0.380  -35.650 1.00 35.64  ? 89  HIS B O   1 
ATOM   1432 C CB  . HIS B 1 90 ? 21.362  -1.498  -38.205 1.00 30.43  ? 89  HIS B CB  1 
ATOM   1433 C CG  . HIS B 1 90 ? 21.245  -2.597  -39.219 1.00 32.77  ? 89  HIS B CG  1 
ATOM   1434 N ND1 . HIS B 1 90 ? 21.867  -3.815  -39.102 1.00 31.47  ? 89  HIS B ND1 1 
ATOM   1435 C CD2 . HIS B 1 90 ? 20.580  -2.637  -40.356 1.00 32.39  ? 89  HIS B CD2 1 
ATOM   1436 C CE1 . HIS B 1 90 ? 21.546  -4.570  -40.143 1.00 30.66  ? 89  HIS B CE1 1 
ATOM   1437 N NE2 . HIS B 1 90 ? 20.754  -3.861  -40.911 1.00 33.25  ? 89  HIS B NE2 1 
ATOM   1438 N N   . ALA B 1 91 ? 20.076  -0.576  -34.911 1.00 34.56  ? 90  ALA B N   1 
ATOM   1439 C CA  . ALA B 1 91 ? 20.224  0.431   -33.863 1.00 34.43  ? 90  ALA B CA  1 
ATOM   1440 C C   . ALA B 1 91 ? 21.246  0.038   -32.801 1.00 40.61  ? 90  ALA B C   1 
ATOM   1441 O O   . ALA B 1 91 ? 21.531  -1.142  -32.573 1.00 37.19  ? 90  ALA B O   1 
ATOM   1442 C CB  . ALA B 1 91 ? 18.889  0.770   -33.248 1.00 35.22  ? 90  ALA B CB  1 
ATOM   1443 N N   . SER B 1 92 ? 21.775  1.066   -32.109 1.00 39.32  ? 91  SER B N   1 
ATOM   1444 C CA  . SER B 1 92 ? 22.454  0.873   -30.842 1.00 42.71  ? 91  SER B CA  1 
ATOM   1445 C C   . SER B 1 92 ? 21.409  0.662   -29.747 1.00 46.98  ? 91  SER B C   1 
ATOM   1446 O O   . SER B 1 92 ? 20.502  1.496   -29.585 1.00 46.13  ? 91  SER B O   1 
ATOM   1447 C CB  . SER B 1 92 ? 23.307  2.100   -30.513 1.00 48.90  ? 91  SER B CB  1 
ATOM   1448 O OG  . SER B 1 92 ? 23.919  1.930   -29.245 1.00 53.90  ? 91  SER B OG  1 
ATOM   1449 N N   . TYR B 1 93 ? 21.535  -0.472  -29.032 1.00 45.22  ? 92  TYR B N   1 
ATOM   1450 C CA  . TYR B 1 93 ? 20.646  -0.877  -27.951 1.00 50.57  ? 92  TYR B CA  1 
ATOM   1451 C C   . TYR B 1 93 ? 21.403  -0.735  -26.631 1.00 58.91  ? 92  TYR B C   1 
ATOM   1452 O O   . TYR B 1 93 ? 21.118  -1.430  -25.656 1.00 57.32  ? 92  TYR B O   1 
ATOM   1453 C CB  . TYR B 1 93 ? 19.980  -2.245  -28.184 1.00 40.86  ? 92  TYR B CB  1 
ATOM   1454 C CG  . TYR B 1 93 ? 18.965  -2.171  -29.317 1.00 39.75  ? 92  TYR B CG  1 
ATOM   1455 C CD1 . TYR B 1 93 ? 17.713  -1.618  -29.100 1.00 41.99  ? 92  TYR B CD1 1 
ATOM   1456 C CD2 . TYR B 1 93 ? 19.262  -2.617  -30.616 1.00 41.12  ? 92  TYR B CD2 1 
ATOM   1457 C CE1 . TYR B 1 93 ? 16.775  -1.506  -30.104 1.00 42.81  ? 92  TYR B CE1 1 
ATOM   1458 C CE2 . TYR B 1 93 ? 18.322  -2.490  -31.636 1.00 34.72  ? 92  TYR B CE2 1 
ATOM   1459 C CZ  . TYR B 1 93 ? 17.082  -1.940  -31.378 1.00 38.29  ? 92  TYR B CZ  1 
ATOM   1460 O OH  . TYR B 1 93 ? 16.127  -1.805  -32.340 1.00 38.94  ? 92  TYR B OH  1 
ATOM   1461 N N   . SER B 1 94 ? 22.364  0.197   -26.624 1.00 67.34  ? 93  SER B N   1 
ATOM   1462 C CA  . SER B 1 94 ? 23.178  0.488   -25.454 1.00 79.19  ? 93  SER B CA  1 
ATOM   1463 C C   . SER B 1 94 ? 22.332  1.220   -24.398 1.00 83.59  ? 93  SER B C   1 
ATOM   1464 O O   . SER B 1 94 ? 21.348  1.886   -24.803 1.00 77.62  ? 93  SER B O   1 
ATOM   1465 C CB  . SER B 1 94 ? 24.429  1.268   -25.820 1.00 76.07  ? 93  SER B CB  1 
ATOM   1466 O OG  . SER B 1 94 ? 25.394  0.428   -26.444 1.00 77.13  ? 93  SER B OG  1 
ATOM   1467 O OXT . SER B 1 94 ? 22.674  1.080   -23.201 1.00 93.38  ? 93  SER B OXT 1 
ATOM   1468 N N   . HIS C 1 4  ? 33.205  -24.022 26.636  1.00 81.27  ? 3   HIS C N   1 
ATOM   1469 C CA  . HIS C 1 4  ? 32.244  -22.988 27.109  1.00 84.59  ? 3   HIS C CA  1 
ATOM   1470 C C   . HIS C 1 4  ? 31.725  -23.412 28.484  1.00 93.63  ? 3   HIS C C   1 
ATOM   1471 O O   . HIS C 1 4  ? 32.470  -23.992 29.278  1.00 81.00  ? 3   HIS C O   1 
ATOM   1472 C CB  . HIS C 1 4  ? 31.182  -22.714 26.031  1.00 77.32  ? 3   HIS C CB  1 
ATOM   1473 N N   . ALA C 1 5  ? 30.449  -23.108 28.760  1.00 91.94  ? 4   ALA C N   1 
ATOM   1474 C CA  . ALA C 1 5  ? 29.763  -23.627 29.931  1.00 83.40  ? 4   ALA C CA  1 
ATOM   1475 C C   . ALA C 1 5  ? 28.281  -23.275 29.874  1.00 87.25  ? 4   ALA C C   1 
ATOM   1476 O O   . ALA C 1 5  ? 27.903  -22.106 29.796  1.00 92.06  ? 4   ALA C O   1 
ATOM   1477 C CB  . ALA C 1 5  ? 30.408  -23.105 31.180  1.00 92.76  ? 4   ALA C CB  1 
ATOM   1478 N N   . PHE C 1 6  ? 27.455  -24.320 29.934  1.00 80.17  ? 5   PHE C N   1 
ATOM   1479 C CA  . PHE C 1 6  ? 26.050  -24.217 29.593  1.00 61.87  ? 5   PHE C CA  1 
ATOM   1480 C C   . PHE C 1 6  ? 25.250  -24.256 30.883  1.00 64.47  ? 5   PHE C C   1 
ATOM   1481 O O   . PHE C 1 6  ? 25.671  -24.908 31.835  1.00 73.38  ? 5   PHE C O   1 
ATOM   1482 C CB  . PHE C 1 6  ? 25.706  -25.393 28.664  1.00 63.03  ? 5   PHE C CB  1 
ATOM   1483 C CG  . PHE C 1 6  ? 26.556  -25.466 27.399  1.00 57.33  ? 5   PHE C CG  1 
ATOM   1484 C CD1 . PHE C 1 6  ? 27.721  -26.230 27.353  1.00 62.86  ? 5   PHE C CD1 1 
ATOM   1485 C CD2 . PHE C 1 6  ? 26.221  -24.728 26.266  1.00 60.90  ? 5   PHE C CD2 1 
ATOM   1486 C CE1 . PHE C 1 6  ? 28.509  -26.276 26.207  1.00 59.39  ? 5   PHE C CE1 1 
ATOM   1487 C CE2 . PHE C 1 6  ? 27.002  -24.790 25.118  1.00 52.23  ? 5   PHE C CE2 1 
ATOM   1488 C CZ  . PHE C 1 6  ? 28.140  -25.554 25.088  1.00 57.12  ? 5   PHE C CZ  1 
ATOM   1489 N N   . LYS C 1 7  ? 24.110  -23.557 30.892  1.00 55.62  ? 6   LYS C N   1 
ATOM   1490 C CA  . LYS C 1 7  ? 23.158  -23.580 31.996  1.00 61.79  ? 6   LYS C CA  1 
ATOM   1491 C C   . LYS C 1 7  ? 21.780  -23.861 31.408  1.00 57.94  ? 6   LYS C C   1 
ATOM   1492 O O   . LYS C 1 7  ? 21.607  -23.750 30.194  1.00 57.73  ? 6   LYS C O   1 
ATOM   1493 C CB  . LYS C 1 7  ? 23.169  -22.254 32.773  1.00 65.63  ? 6   LYS C CB  1 
ATOM   1494 N N   . PRO C 1 8  ? 20.753  -24.251 32.199  1.00 64.43  ? 7   PRO C N   1 
ATOM   1495 C CA  . PRO C 1 8  ? 19.435  -24.531 31.622  1.00 65.28  ? 7   PRO C CA  1 
ATOM   1496 C C   . PRO C 1 8  ? 18.929  -23.340 30.811  1.00 69.77  ? 7   PRO C C   1 
ATOM   1497 O O   . PRO C 1 8  ? 19.264  -22.191 31.113  1.00 72.60  ? 7   PRO C O   1 
ATOM   1498 C CB  . PRO C 1 8  ? 18.532  -24.856 32.814  1.00 66.80  ? 7   PRO C CB  1 
ATOM   1499 C CG  . PRO C 1 8  ? 19.506  -25.261 33.891  1.00 69.90  ? 7   PRO C CG  1 
ATOM   1500 C CD  . PRO C 1 8  ? 20.792  -24.466 33.655  1.00 64.75  ? 7   PRO C CD  1 
ATOM   1501 N N   . GLY C 1 9  ? 18.147  -23.646 29.767  1.00 60.42  ? 8   GLY C N   1 
ATOM   1502 C CA  . GLY C 1 9  ? 17.506  -22.657 28.916  1.00 57.07  ? 8   GLY C CA  1 
ATOM   1503 C C   . GLY C 1 9  ? 18.365  -22.251 27.718  1.00 57.69  ? 8   GLY C C   1 
ATOM   1504 O O   . GLY C 1 9  ? 17.818  -21.798 26.716  1.00 70.14  ? 8   GLY C O   1 
ATOM   1505 N N   . ASP C 1 10 ? 19.693  -22.425 27.827  1.00 49.66  ? 9   ASP C N   1 
ATOM   1506 C CA  . ASP C 1 10 ? 20.651  -22.083 26.790  1.00 49.41  ? 9   ASP C CA  1 
ATOM   1507 C C   . ASP C 1 10 ? 20.307  -22.819 25.490  1.00 56.57  ? 9   ASP C C   1 
ATOM   1508 O O   . ASP C 1 10 ? 20.084  -24.035 25.499  1.00 47.70  ? 9   ASP C O   1 
ATOM   1509 C CB  . ASP C 1 10 ? 22.090  -22.371 27.198  1.00 56.94  ? 9   ASP C CB  1 
ATOM   1510 C CG  . ASP C 1 10 ? 22.733  -21.433 28.220  1.00 65.51  ? 9   ASP C CG  1 
ATOM   1511 O OD1 . ASP C 1 10 ? 22.057  -20.487 28.660  1.00 65.33  ? 9   ASP C OD1 1 
ATOM   1512 O OD2 . ASP C 1 10 ? 23.919  -21.652 28.570  1.00 65.95  ? 9   ASP C OD2 1 
ATOM   1513 N N   . LEU C 1 11 ? 20.289  -22.062 24.381  1.00 53.13  ? 10  LEU C N   1 
ATOM   1514 C CA  . LEU C 1 11 ? 20.000  -22.605 23.058  1.00 48.99  ? 10  LEU C CA  1 
ATOM   1515 C C   . LEU C 1 11 ? 21.289  -23.080 22.384  1.00 45.26  ? 10  LEU C C   1 
ATOM   1516 O O   . LEU C 1 11 ? 22.305  -22.373 22.377  1.00 48.41  ? 10  LEU C O   1 
ATOM   1517 C CB  . LEU C 1 11 ? 19.219  -21.590 22.217  1.00 43.00  ? 10  LEU C CB  1 
ATOM   1518 C CG  . LEU C 1 11 ? 17.947  -21.012 22.844  1.00 42.54  ? 10  LEU C CG  1 
ATOM   1519 C CD1 . LEU C 1 11 ? 17.283  -20.058 21.855  1.00 46.10  ? 10  LEU C CD1 1 
ATOM   1520 C CD2 . LEU C 1 11 ? 16.935  -22.081 23.308  1.00 45.58  ? 10  LEU C CD2 1 
ATOM   1521 N N   . VAL C 1 12 ? 21.247  -24.291 21.776  1.00 38.14  ? 11  VAL C N   1 
ATOM   1522 C CA  . VAL C 1 12 ? 22.447  -24.919 21.244  1.00 37.10  ? 11  VAL C CA  1 
ATOM   1523 C C   . VAL C 1 12 ? 22.107  -25.655 19.934  1.00 36.25  ? 11  VAL C C   1 
ATOM   1524 O O   . VAL C 1 12 ? 20.927  -25.871 19.659  1.00 40.16  ? 11  VAL C O   1 
ATOM   1525 C CB  . VAL C 1 12 ? 23.081  -25.943 22.217  1.00 38.22  ? 11  VAL C CB  1 
ATOM   1526 C CG1 . VAL C 1 12 ? 23.572  -25.294 23.524  1.00 43.97  ? 11  VAL C CG1 1 
ATOM   1527 C CG2 . VAL C 1 12 ? 22.128  -27.095 22.483  1.00 40.18  ? 11  VAL C CG2 1 
ATOM   1528 N N   . PHE C 1 13 ? 23.153  -26.036 19.183  1.00 35.43  ? 12  PHE C N   1 
ATOM   1529 C CA  . PHE C 1 13 ? 23.086  -27.198 18.287  1.00 34.62  ? 12  PHE C CA  1 
ATOM   1530 C C   . PHE C 1 13 ? 23.700  -28.394 19.017  1.00 35.53  ? 12  PHE C C   1 
ATOM   1531 O O   . PHE C 1 13 ? 24.791  -28.283 19.580  1.00 37.54  ? 12  PHE C O   1 
ATOM   1532 C CB  . PHE C 1 13 ? 23.775  -26.995 16.931  1.00 39.21  ? 12  PHE C CB  1 
ATOM   1533 C CG  . PHE C 1 13 ? 23.003  -25.998 16.091  1.00 42.59  ? 12  PHE C CG  1 
ATOM   1534 C CD1 . PHE C 1 13 ? 21.959  -26.422 15.266  1.00 41.45  ? 12  PHE C CD1 1 
ATOM   1535 C CD2 . PHE C 1 13 ? 23.298  -24.637 16.151  1.00 41.23  ? 12  PHE C CD2 1 
ATOM   1536 C CE1 . PHE C 1 13 ? 21.226  -25.509 14.524  1.00 42.77  ? 12  PHE C CE1 1 
ATOM   1537 C CE2 . PHE C 1 13 ? 22.546  -23.733 15.416  1.00 44.93  ? 12  PHE C CE2 1 
ATOM   1538 C CZ  . PHE C 1 13 ? 21.529  -24.175 14.594  1.00 43.55  ? 12  PHE C CZ  1 
ATOM   1539 N N   . ALA C 1 14 ? 22.995  -29.542 19.015  1.00 33.72  ? 13  ALA C N   1 
ATOM   1540 C CA  . ALA C 1 14 ? 23.463  -30.708 19.760  1.00 33.01  ? 13  ALA C CA  1 
ATOM   1541 C C   . ALA C 1 14 ? 23.774  -31.810 18.750  1.00 36.41  ? 13  ALA C C   1 
ATOM   1542 O O   . ALA C 1 14 ? 22.941  -32.054 17.857  1.00 35.44  ? 13  ALA C O   1 
ATOM   1543 C CB  . ALA C 1 14 ? 22.403  -31.152 20.737  1.00 32.95  ? 13  ALA C CB  1 
ATOM   1544 N N   . LYS C 1 15 ? 24.969  -32.417 18.885  1.00 34.36  ? 14  LYS C N   1 
ATOM   1545 C CA  . LYS C 1 15 ? 25.400  -33.414 17.912  1.00 34.55  ? 14  LYS C CA  1 
ATOM   1546 C C   . LYS C 1 15 ? 25.393  -34.805 18.528  1.00 35.76  ? 14  LYS C C   1 
ATOM   1547 O O   . LYS C 1 15 ? 26.169  -35.082 19.448  1.00 38.41  ? 14  LYS C O   1 
ATOM   1548 C CB  . LYS C 1 15 ? 26.814  -33.112 17.389  1.00 39.12  ? 14  LYS C CB  1 
ATOM   1549 C CG  . LYS C 1 15 ? 27.316  -34.122 16.338  1.00 40.13  ? 14  LYS C CG  1 
ATOM   1550 C CD  . LYS C 1 15 ? 26.489  -34.090 15.059  1.00 39.68  ? 14  LYS C CD  1 
ATOM   1551 C CE  . LYS C 1 15 ? 27.017  -34.878 13.875  1.00 40.55  ? 14  LYS C CE  1 
ATOM   1552 N NZ  . LYS C 1 15 ? 26.864  -36.311 14.130  1.00 36.88  ? 14  LYS C NZ  1 
ATOM   1553 N N   . MET C 1 16 ? 24.559  -35.694 17.970  1.00 34.16  ? 15  MET C N   1 
ATOM   1554 C CA  . MET C 1 16 ? 24.563  -37.116 18.301  1.00 31.53  ? 15  MET C CA  1 
ATOM   1555 C C   . MET C 1 16 ? 25.051  -37.927 17.092  1.00 39.08  ? 15  MET C C   1 
ATOM   1556 O O   . MET C 1 16 ? 24.805  -37.565 15.934  1.00 32.55  ? 15  MET C O   1 
ATOM   1557 C CB  . MET C 1 16 ? 23.136  -37.576 18.602  1.00 34.80  ? 15  MET C CB  1 
ATOM   1558 C CG  . MET C 1 16 ? 22.477  -36.882 19.779  1.00 38.27  ? 15  MET C CG  1 
ATOM   1559 S SD  . MET C 1 16 ? 20.902  -37.664 20.179  1.00 46.54  ? 15  MET C SD  1 
ATOM   1560 C CE  . MET C 1 16 ? 19.934  -36.922 18.855  1.00 46.29  ? 15  MET C CE  1 
ATOM   1561 N N   . LYS C 1 17 ? 25.703  -39.072 17.373  1.00 35.34  ? 16  LYS C N   1 
ATOM   1562 C CA  . LYS C 1 17 ? 26.120  -39.980 16.310  1.00 38.94  ? 16  LYS C CA  1 
ATOM   1563 C C   . LYS C 1 17 ? 24.878  -40.364 15.501  1.00 35.52  ? 16  LYS C C   1 
ATOM   1564 O O   . LYS C 1 17 ? 23.871  -40.784 16.064  1.00 36.27  ? 16  LYS C O   1 
ATOM   1565 C CB  . LYS C 1 17 ? 26.850  -41.205 16.893  1.00 37.33  ? 16  LYS C CB  1 
ATOM   1566 C CG  . LYS C 1 17 ? 27.388  -42.225 15.886  1.00 40.82  ? 16  LYS C CG  1 
ATOM   1567 C CD  . LYS C 1 17 ? 28.646  -41.630 15.259  1.00 43.62  ? 16  LYS C CD  1 
ATOM   1568 C CE  . LYS C 1 17 ? 29.380  -42.535 14.317  1.00 50.36  ? 16  LYS C CE  1 
ATOM   1569 N NZ  . LYS C 1 17 ? 30.587  -41.804 13.911  1.00 43.59  ? 16  LYS C NZ  1 
ATOM   1570 N N   . GLY C 1 18 ? 24.970  -40.165 14.186  1.00 41.03  ? 17  GLY C N   1 
ATOM   1571 C CA  . GLY C 1 18 ? 23.926  -40.654 13.298  1.00 40.19  ? 17  GLY C CA  1 
ATOM   1572 C C   . GLY C 1 18 ? 22.963  -39.544 12.905  1.00 38.33  ? 17  GLY C C   1 
ATOM   1573 O O   . GLY C 1 18 ? 21.968  -39.824 12.252  1.00 35.92  ? 17  GLY C O   1 
ATOM   1574 N N   . TYR C 1 19 ? 23.224  -38.316 13.387  1.00 33.46  ? 18  TYR C N   1 
ATOM   1575 C CA  . TYR C 1 19 ? 22.295  -37.208 13.152  1.00 35.22  ? 18  TYR C CA  1 
ATOM   1576 C C   . TYR C 1 19 ? 23.096  -35.945 12.901  1.00 34.53  ? 18  TYR C C   1 
ATOM   1577 O O   . TYR C 1 19 ? 24.191  -35.773 13.431  1.00 36.18  ? 18  TYR C O   1 
ATOM   1578 C CB  . TYR C 1 19 ? 21.403  -36.878 14.361  1.00 28.53  ? 18  TYR C CB  1 
ATOM   1579 C CG  . TYR C 1 19 ? 20.566  -38.067 14.772  1.00 33.07  ? 18  TYR C CG  1 
ATOM   1580 C CD1 . TYR C 1 19 ? 21.093  -39.090 15.558  1.00 33.91  ? 18  TYR C CD1 1 
ATOM   1581 C CD2 . TYR C 1 19 ? 19.268  -38.174 14.314  1.00 33.41  ? 18  TYR C CD2 1 
ATOM   1582 C CE1 . TYR C 1 19 ? 20.330  -40.195 15.887  1.00 34.67  ? 18  TYR C CE1 1 
ATOM   1583 C CE2 . TYR C 1 19 ? 18.495  -39.262 14.663  1.00 39.15  ? 18  TYR C CE2 1 
ATOM   1584 C CZ  . TYR C 1 19 ? 19.025  -40.265 15.447  1.00 39.00  ? 18  TYR C CZ  1 
ATOM   1585 O OH  . TYR C 1 19 ? 18.220  -41.342 15.715  1.00 47.37  ? 18  TYR C OH  1 
ATOM   1586 N N   . PRO C 1 20 ? 22.527  -35.011 12.108  1.00 35.54  ? 19  PRO C N   1 
ATOM   1587 C CA  . PRO C 1 20 ? 23.169  -33.723 11.849  1.00 34.12  ? 19  PRO C CA  1 
ATOM   1588 C C   . PRO C 1 20 ? 23.106  -32.910 13.147  1.00 36.50  ? 19  PRO C C   1 
ATOM   1589 O O   . PRO C 1 20 ? 22.298  -33.197 14.051  1.00 31.65  ? 19  PRO C O   1 
ATOM   1590 C CB  . PRO C 1 20 ? 22.231  -33.120 10.756  1.00 36.28  ? 19  PRO C CB  1 
ATOM   1591 C CG  . PRO C 1 20 ? 20.879  -33.727 11.016  1.00 33.90  ? 19  PRO C CG  1 
ATOM   1592 C CD  . PRO C 1 20 ? 21.162  -35.125 11.533  1.00 32.38  ? 19  PRO C CD  1 
ATOM   1593 N N   . HIS C 1 21 ? 23.942  -31.874 13.225  1.00 35.47  ? 20  HIS C N   1 
ATOM   1594 C CA  . HIS C 1 21 ? 23.849  -30.954 14.361  1.00 37.81  ? 20  HIS C CA  1 
ATOM   1595 C C   . HIS C 1 21 ? 22.425  -30.404 14.476  1.00 38.76  ? 20  HIS C C   1 
ATOM   1596 O O   . HIS C 1 21 ? 21.888  -29.845 13.515  1.00 37.23  ? 20  HIS C O   1 
ATOM   1597 C CB  . HIS C 1 21 ? 24.841  -29.806 14.188  1.00 38.26  ? 20  HIS C CB  1 
ATOM   1598 C CG  . HIS C 1 21 ? 26.262  -30.224 14.292  1.00 37.85  ? 20  HIS C CG  1 
ATOM   1599 N ND1 . HIS C 1 21 ? 26.959  -30.825 13.266  1.00 40.16  ? 20  HIS C ND1 1 
ATOM   1600 C CD2 . HIS C 1 21 ? 27.116  -30.123 15.319  1.00 41.22  ? 20  HIS C CD2 1 
ATOM   1601 C CE1 . HIS C 1 21 ? 28.191  -31.096 13.671  1.00 44.95  ? 20  HIS C CE1 1 
ATOM   1602 N NE2 . HIS C 1 21 ? 28.316  -30.645 14.902  1.00 43.33  ? 20  HIS C NE2 1 
ATOM   1603 N N   . TRP C 1 22 ? 21.818  -30.534 15.669  1.00 35.53  ? 21  TRP C N   1 
ATOM   1604 C CA  . TRP C 1 22 ? 20.372  -30.435 15.788  1.00 32.92  ? 21  TRP C CA  1 
ATOM   1605 C C   . TRP C 1 22 ? 19.965  -29.274 16.690  1.00 34.35  ? 21  TRP C C   1 
ATOM   1606 O O   . TRP C 1 22 ? 20.523  -29.132 17.775  1.00 33.30  ? 21  TRP C O   1 
ATOM   1607 C CB  . TRP C 1 22 ? 19.811  -31.753 16.348  1.00 32.47  ? 21  TRP C CB  1 
ATOM   1608 C CG  . TRP C 1 22 ? 18.378  -31.964 15.956  1.00 35.00  ? 21  TRP C CG  1 
ATOM   1609 C CD1 . TRP C 1 22 ? 17.265  -31.405 16.507  1.00 33.52  ? 21  TRP C CD1 1 
ATOM   1610 C CD2 . TRP C 1 22 ? 17.929  -32.842 14.897  1.00 33.95  ? 21  TRP C CD2 1 
ATOM   1611 N NE1 . TRP C 1 22 ? 16.147  -31.850 15.836  1.00 33.90  ? 21  TRP C NE1 1 
ATOM   1612 C CE2 . TRP C 1 22 ? 16.522  -32.748 14.866  1.00 33.65  ? 21  TRP C CE2 1 
ATOM   1613 C CE3 . TRP C 1 22 ? 18.581  -33.699 14.003  1.00 32.00  ? 21  TRP C CE3 1 
ATOM   1614 C CZ2 . TRP C 1 22 ? 15.753  -33.490 13.959  1.00 35.30  ? 21  TRP C CZ2 1 
ATOM   1615 C CZ3 . TRP C 1 22 ? 17.828  -34.417 13.090  1.00 35.35  ? 21  TRP C CZ3 1 
ATOM   1616 C CH2 . TRP C 1 22 ? 16.428  -34.318 13.078  1.00 35.08  ? 21  TRP C CH2 1 
ATOM   1617 N N   . PRO C 1 23 ? 18.972  -28.422 16.333  1.00 38.81  ? 22  PRO C N   1 
ATOM   1618 C CA  . PRO C 1 23 ? 18.555  -27.339 17.223  1.00 35.82  ? 22  PRO C CA  1 
ATOM   1619 C C   . PRO C 1 23 ? 17.974  -27.909 18.513  1.00 34.34  ? 22  PRO C C   1 
ATOM   1620 O O   . PRO C 1 23 ? 17.115  -28.789 18.506  1.00 33.61  ? 22  PRO C O   1 
ATOM   1621 C CB  . PRO C 1 23 ? 17.493  -26.594 16.376  1.00 35.96  ? 22  PRO C CB  1 
ATOM   1622 C CG  . PRO C 1 23 ? 16.892  -27.693 15.517  1.00 34.39  ? 22  PRO C CG  1 
ATOM   1623 C CD  . PRO C 1 23 ? 18.163  -28.445 15.091  1.00 37.21  ? 22  PRO C CD  1 
ATOM   1624 N N   . ALA C 1 24 ? 18.473  -27.374 19.638  1.00 34.49  ? 23  ALA C N   1 
ATOM   1625 C CA  . ALA C 1 24 ? 18.191  -27.962 20.940  1.00 38.45  ? 23  ALA C CA  1 
ATOM   1626 C C   . ALA C 1 24 ? 18.370  -26.886 22.013  1.00 38.38  ? 23  ALA C C   1 
ATOM   1627 O O   . ALA C 1 24 ? 18.893  -25.787 21.743  1.00 41.38  ? 23  ALA C O   1 
ATOM   1628 C CB  . ALA C 1 24 ? 19.180  -29.106 21.158  1.00 37.79  ? 23  ALA C CB  1 
ATOM   1629 N N   . ARG C 1 25 ? 18.006  -27.252 23.244  1.00 41.52  ? 24  ARG C N   1 
ATOM   1630 C CA  . ARG C 1 25 ? 18.228  -26.419 24.409  1.00 38.06  ? 24  ARG C CA  1 
ATOM   1631 C C   . ARG C 1 25 ? 18.718  -27.292 25.569  1.00 40.19  ? 24  ARG C C   1 
ATOM   1632 O O   . ARG C 1 25 ? 18.352  -28.460 25.640  1.00 42.49  ? 24  ARG C O   1 
ATOM   1633 C CB  . ARG C 1 25 ? 16.919  -25.751 24.844  1.00 36.69  ? 24  ARG C CB  1 
ATOM   1634 C CG  . ARG C 1 25 ? 15.655  -26.526 25.182  1.00 42.46  ? 24  ARG C CG  1 
ATOM   1635 C CD  . ARG C 1 25 ? 14.662  -25.660 25.967  1.00 49.56  ? 24  ARG C CD  1 
ATOM   1636 N NE  . ARG C 1 25 ? 13.453  -26.459 26.212  1.00 52.63  ? 24  ARG C NE  1 
ATOM   1637 C CZ  . ARG C 1 25 ? 12.200  -26.174 25.882  1.00 55.61  ? 24  ARG C CZ  1 
ATOM   1638 N NH1 . ARG C 1 25 ? 11.890  -25.024 25.301  1.00 56.55  ? 24  ARG C NH1 1 
ATOM   1639 N NH2 . ARG C 1 25 ? 11.245  -27.045 26.156  1.00 56.56  ? 24  ARG C NH2 1 
ATOM   1640 N N   . ILE C 1 26 ? 19.536  -26.702 26.450  1.00 42.65  ? 25  ILE C N   1 
ATOM   1641 C CA  . ILE C 1 26 ? 19.819  -27.307 27.751  1.00 45.56  ? 25  ILE C CA  1 
ATOM   1642 C C   . ILE C 1 26 ? 18.563  -27.255 28.620  1.00 51.44  ? 25  ILE C C   1 
ATOM   1643 O O   . ILE C 1 26 ? 18.001  -26.180 28.842  1.00 52.24  ? 25  ILE C O   1 
ATOM   1644 C CB  . ILE C 1 26 ? 20.991  -26.615 28.472  1.00 44.30  ? 25  ILE C CB  1 
ATOM   1645 C CG1 . ILE C 1 26 ? 22.201  -26.403 27.587  1.00 42.21  ? 25  ILE C CG1 1 
ATOM   1646 C CG2 . ILE C 1 26 ? 21.356  -27.397 29.745  1.00 47.22  ? 25  ILE C CG2 1 
ATOM   1647 C CD1 . ILE C 1 26 ? 22.865  -27.678 27.092  1.00 46.84  ? 25  ILE C CD1 1 
ATOM   1648 N N   . ASP C 1 27 ? 18.151  -28.424 29.124  1.00 51.84  ? 26  ASP C N   1 
ATOM   1649 C CA  . ASP C 1 27 ? 17.111  -28.551 30.132  1.00 63.89  ? 26  ASP C CA  1 
ATOM   1650 C C   . ASP C 1 27 ? 17.710  -28.589 31.539  1.00 66.48  ? 26  ASP C C   1 
ATOM   1651 O O   . ASP C 1 27 ? 18.922  -28.740 31.714  1.00 62.42  ? 26  ASP C O   1 
ATOM   1652 C CB  . ASP C 1 27 ? 16.304  -29.823 29.939  1.00 58.29  ? 26  ASP C CB  1 
ATOM   1653 C CG  . ASP C 1 27 ? 15.052  -29.685 29.090  1.00 67.06  ? 26  ASP C CG  1 
ATOM   1654 O OD1 . ASP C 1 27 ? 14.863  -28.595 28.497  1.00 64.83  ? 26  ASP C OD1 1 
ATOM   1655 O OD2 . ASP C 1 27 ? 14.263  -30.658 29.078  1.00 69.16  ? 26  ASP C OD2 1 
ATOM   1656 N N   . ASP C 1 28 ? 16.828  -28.436 32.536  1.00 74.11  ? 27  ASP C N   1 
ATOM   1657 C CA  . ASP C 1 28 ? 17.172  -28.640 33.932  1.00 73.15  ? 27  ASP C CA  1 
ATOM   1658 C C   . ASP C 1 28 ? 16.815  -30.082 34.270  1.00 73.08  ? 27  ASP C C   1 
ATOM   1659 O O   . ASP C 1 28 ? 16.047  -30.695 33.539  1.00 67.61  ? 27  ASP C O   1 
ATOM   1660 C CB  . ASP C 1 28 ? 16.471  -27.636 34.834  1.00 77.92  ? 27  ASP C CB  1 
ATOM   1661 C CG  . ASP C 1 28 ? 17.138  -27.387 36.181  1.00 87.48  ? 27  ASP C CG  1 
ATOM   1662 O OD1 . ASP C 1 28 ? 18.160  -28.053 36.475  1.00 86.16  ? 27  ASP C OD1 1 
ATOM   1663 O OD2 . ASP C 1 28 ? 16.641  -26.518 36.922  1.00 87.71  ? 27  ASP C OD2 1 
ATOM   1664 N N   . ILE C 1 29 ? 17.394  -30.615 35.355  1.00 75.32  ? 28  ILE C N   1 
ATOM   1665 C CA  . ILE C 1 29 ? 17.195  -32.009 35.715  1.00 69.49  ? 28  ILE C CA  1 
ATOM   1666 C C   . ILE C 1 29 ? 16.111  -32.092 36.803  1.00 69.27  ? 28  ILE C C   1 
ATOM   1667 O O   . ILE C 1 29 ? 16.149  -31.219 37.690  1.00 68.22  ? 28  ILE C O   1 
ATOM   1668 C CB  . ILE C 1 29 ? 18.525  -32.650 36.153  1.00 66.49  ? 28  ILE C CB  1 
ATOM   1669 N N   . ALA C 1 33 ? 14.976  -36.732 40.393  1.00 61.30  ? 32  ALA C N   1 
ATOM   1670 C CA  . ALA C 1 33 ? 15.112  -37.437 39.095  1.00 67.70  ? 32  ALA C CA  1 
ATOM   1671 C C   . ALA C 1 33 ? 16.428  -38.217 39.063  1.00 75.79  ? 32  ALA C C   1 
ATOM   1672 O O   . ALA C 1 33 ? 17.264  -38.063 39.955  1.00 69.12  ? 32  ALA C O   1 
ATOM   1673 C CB  . ALA C 1 33 ? 15.017  -36.446 37.946  1.00 64.10  ? 32  ALA C CB  1 
ATOM   1674 N N   . VAL C 1 34 ? 16.585  -39.065 38.031  1.00 78.82  ? 33  VAL C N   1 
ATOM   1675 C CA  . VAL C 1 34 ? 17.831  -39.770 37.749  1.00 79.43  ? 33  VAL C CA  1 
ATOM   1676 C C   . VAL C 1 34 ? 18.836  -38.748 37.223  1.00 75.68  ? 33  VAL C C   1 
ATOM   1677 O O   . VAL C 1 34 ? 18.533  -37.978 36.307  1.00 62.55  ? 33  VAL C O   1 
ATOM   1678 C CB  . VAL C 1 34 ? 17.718  -40.986 36.800  1.00 87.13  ? 33  VAL C CB  1 
ATOM   1679 C CG1 . VAL C 1 34 ? 19.076  -41.485 36.306  1.00 88.89  ? 33  VAL C CG1 1 
ATOM   1680 C CG2 . VAL C 1 34 ? 16.936  -42.133 37.428  1.00 98.35  ? 33  VAL C CG2 1 
ATOM   1681 N N   . LYS C 1 35 ? 20.030  -38.754 37.832  1.00 67.23  ? 34  LYS C N   1 
ATOM   1682 C CA  . LYS C 1 35 ? 21.085  -37.814 37.496  1.00 65.87  ? 34  LYS C CA  1 
ATOM   1683 C C   . LYS C 1 35 ? 21.628  -38.188 36.122  1.00 59.16  ? 34  LYS C C   1 
ATOM   1684 O O   . LYS C 1 35 ? 21.551  -39.350 35.711  1.00 55.94  ? 34  LYS C O   1 
ATOM   1685 C CB  . LYS C 1 35 ? 22.186  -37.824 38.566  1.00 62.96  ? 34  LYS C CB  1 
ATOM   1686 N N   . PRO C 1 36 ? 22.161  -37.202 35.366  1.00 54.66  ? 35  PRO C N   1 
ATOM   1687 C CA  . PRO C 1 36 ? 22.884  -37.502 34.133  1.00 57.76  ? 35  PRO C CA  1 
ATOM   1688 C C   . PRO C 1 36 ? 23.988  -38.523 34.404  1.00 55.30  ? 35  PRO C C   1 
ATOM   1689 O O   . PRO C 1 36 ? 24.403  -38.732 35.559  1.00 48.53  ? 35  PRO C O   1 
ATOM   1690 C CB  . PRO C 1 36 ? 23.444  -36.112 33.717  1.00 57.17  ? 35  PRO C CB  1 
ATOM   1691 C CG  . PRO C 1 36 ? 22.507  -35.105 34.351  1.00 58.41  ? 35  PRO C CG  1 
ATOM   1692 C CD  . PRO C 1 36 ? 22.050  -35.756 35.645  1.00 60.82  ? 35  PRO C CD  1 
ATOM   1693 N N   . PRO C 1 37 ? 24.512  -39.191 33.355  1.00 55.19  ? 36  PRO C N   1 
ATOM   1694 C CA  . PRO C 1 37 ? 25.850  -39.763 33.452  1.00 52.94  ? 36  PRO C CA  1 
ATOM   1695 C C   . PRO C 1 37 ? 26.758  -38.591 33.821  1.00 49.86  ? 36  PRO C C   1 
ATOM   1696 O O   . PRO C 1 37 ? 26.415  -37.413 33.613  1.00 45.91  ? 36  PRO C O   1 
ATOM   1697 C CB  . PRO C 1 37 ? 26.115  -40.337 32.050  1.00 51.41  ? 36  PRO C CB  1 
ATOM   1698 C CG  . PRO C 1 37 ? 24.718  -40.592 31.523  1.00 55.61  ? 36  PRO C CG  1 
ATOM   1699 C CD  . PRO C 1 37 ? 23.873  -39.443 32.050  1.00 52.22  ? 36  PRO C CD  1 
ATOM   1700 N N   . PRO C 1 38 ? 27.929  -38.877 34.432  1.00 46.06  ? 37  PRO C N   1 
ATOM   1701 C CA  . PRO C 1 38 ? 28.853  -37.819 34.840  1.00 46.15  ? 37  PRO C CA  1 
ATOM   1702 C C   . PRO C 1 38 ? 29.215  -36.947 33.646  1.00 40.34  ? 37  PRO C C   1 
ATOM   1703 O O   . PRO C 1 38 ? 29.504  -37.455 32.561  1.00 42.80  ? 37  PRO C O   1 
ATOM   1704 C CB  . PRO C 1 38 ? 30.068  -38.629 35.339  1.00 50.01  ? 37  PRO C CB  1 
ATOM   1705 C CG  . PRO C 1 38 ? 29.460  -39.942 35.802  1.00 51.48  ? 37  PRO C CG  1 
ATOM   1706 C CD  . PRO C 1 38 ? 28.431  -40.232 34.720  1.00 50.58  ? 37  PRO C CD  1 
ATOM   1707 N N   . ASN C 1 39 ? 29.190  -35.630 33.891  1.00 42.27  ? 38  ASN C N   1 
ATOM   1708 C CA  . ASN C 1 39 ? 29.607  -34.578 32.982  1.00 38.10  ? 38  ASN C CA  1 
ATOM   1709 C C   . ASN C 1 39 ? 28.697  -34.482 31.756  1.00 45.04  ? 38  ASN C C   1 
ATOM   1710 O O   . ASN C 1 39 ? 29.137  -33.959 30.727  1.00 48.47  ? 38  ASN C O   1 
ATOM   1711 C CB  . ASN C 1 39 ? 31.038  -34.758 32.495  1.00 41.53  ? 38  ASN C CB  1 
ATOM   1712 C CG  . ASN C 1 39 ? 31.671  -33.485 31.984  1.00 53.83  ? 38  ASN C CG  1 
ATOM   1713 O OD1 . ASN C 1 39 ? 31.440  -32.403 32.535  1.00 63.70  ? 38  ASN C OD1 1 
ATOM   1714 N ND2 . ASN C 1 39 ? 32.459  -33.581 30.922  1.00 54.96  ? 38  ASN C ND2 1 
ATOM   1715 N N   . LYS C 1 40 ? 27.443  -34.955 31.863  1.00 40.35  ? 39  LYS C N   1 
ATOM   1716 C CA  . LYS C 1 40 ? 26.544  -34.828 30.723  1.00 36.88  ? 39  LYS C CA  1 
ATOM   1717 C C   . LYS C 1 40 ? 25.420  -33.867 31.080  1.00 38.29  ? 39  LYS C C   1 
ATOM   1718 O O   . LYS C 1 40 ? 25.067  -33.728 32.237  1.00 41.36  ? 39  LYS C O   1 
ATOM   1719 C CB  . LYS C 1 40 ? 25.853  -36.152 30.377  1.00 36.30  ? 39  LYS C CB  1 
ATOM   1720 C CG  . LYS C 1 40 ? 26.807  -37.284 30.087  1.00 39.83  ? 39  LYS C CG  1 
ATOM   1721 C CD  . LYS C 1 40 ? 27.664  -37.088 28.852  1.00 46.31  ? 39  LYS C CD  1 
ATOM   1722 C CE  . LYS C 1 40 ? 28.383  -38.359 28.463  1.00 50.66  ? 39  LYS C CE  1 
ATOM   1723 N NZ  . LYS C 1 40 ? 29.287  -38.156 27.327  1.00 53.23  ? 39  LYS C NZ  1 
ATOM   1724 N N   . TYR C 1 41 ? 24.844  -33.223 30.052  1.00 36.59  ? 40  TYR C N   1 
ATOM   1725 C CA  . TYR C 1 41 ? 23.748  -32.283 30.211  1.00 39.33  ? 40  TYR C CA  1 
ATOM   1726 C C   . TYR C 1 41 ? 22.473  -32.899 29.656  1.00 39.59  ? 40  TYR C C   1 
ATOM   1727 O O   . TYR C 1 41 ? 22.539  -33.624 28.664  1.00 38.20  ? 40  TYR C O   1 
ATOM   1728 C CB  . TYR C 1 41 ? 23.972  -31.078 29.287  1.00 36.77  ? 40  TYR C CB  1 
ATOM   1729 C CG  . TYR C 1 41 ? 25.112  -30.174 29.724  1.00 37.56  ? 40  TYR C CG  1 
ATOM   1730 C CD1 . TYR C 1 41 ? 26.428  -30.417 29.323  1.00 40.42  ? 40  TYR C CD1 1 
ATOM   1731 C CD2 . TYR C 1 41 ? 24.867  -29.103 30.589  1.00 44.48  ? 40  TYR C CD2 1 
ATOM   1732 C CE1 . TYR C 1 41 ? 27.471  -29.629 29.773  1.00 48.19  ? 40  TYR C CE1 1 
ATOM   1733 C CE2 . TYR C 1 41 ? 25.903  -28.281 31.005  1.00 43.94  ? 40  TYR C CE2 1 
ATOM   1734 C CZ  . TYR C 1 41 ? 27.202  -28.560 30.616  1.00 51.28  ? 40  TYR C CZ  1 
ATOM   1735 O OH  . TYR C 1 41 ? 28.211  -27.771 31.068  1.00 53.18  ? 40  TYR C OH  1 
ATOM   1736 N N   . PRO C 1 42 ? 21.287  -32.563 30.226  1.00 39.21  ? 41  PRO C N   1 
ATOM   1737 C CA  . PRO C 1 42 ? 20.010  -33.050 29.707  1.00 37.68  ? 41  PRO C CA  1 
ATOM   1738 C C   . PRO C 1 42 ? 19.676  -32.133 28.536  1.00 38.29  ? 41  PRO C C   1 
ATOM   1739 O O   . PRO C 1 42 ? 19.666  -30.904 28.677  1.00 42.19  ? 41  PRO C O   1 
ATOM   1740 C CB  . PRO C 1 42 ? 19.023  -32.891 30.872  1.00 40.22  ? 41  PRO C CB  1 
ATOM   1741 C CG  . PRO C 1 42 ? 19.715  -31.974 31.843  1.00 44.52  ? 41  PRO C CG  1 
ATOM   1742 C CD  . PRO C 1 42 ? 21.124  -31.643 31.372  1.00 42.80  ? 41  PRO C CD  1 
ATOM   1743 N N   . ILE C 1 43 ? 19.409  -32.761 27.383  1.00 36.88  ? 42  ILE C N   1 
ATOM   1744 C CA  . ILE C 1 43 ? 19.182  -31.978 26.166  1.00 38.03  ? 42  ILE C CA  1 
ATOM   1745 C C   . ILE C 1 43 ? 17.751  -32.222 25.714  1.00 36.73  ? 42  ILE C C   1 
ATOM   1746 O O   . ILE C 1 43 ? 17.251  -33.350 25.737  1.00 41.44  ? 42  ILE C O   1 
ATOM   1747 C CB  . ILE C 1 43 ? 20.191  -32.347 25.060  1.00 33.81  ? 42  ILE C CB  1 
ATOM   1748 C CG1 . ILE C 1 43 ? 21.640  -32.128 25.506  1.00 36.56  ? 42  ILE C CG1 1 
ATOM   1749 C CG2 . ILE C 1 43 ? 19.890  -31.575 23.755  1.00 36.46  ? 42  ILE C CG2 1 
ATOM   1750 C CD1 . ILE C 1 43 ? 22.011  -30.680 25.795  1.00 37.41  ? 42  ILE C CD1 1 
ATOM   1751 N N   . PHE C 1 44 ? 17.082  -31.146 25.267  1.00 38.69  ? 43  PHE C N   1 
ATOM   1752 C CA  . PHE C 1 44 ? 15.779  -31.313 24.649  1.00 35.67  ? 43  PHE C CA  1 
ATOM   1753 C C   . PHE C 1 44 ? 15.927  -30.864 23.198  1.00 36.43  ? 43  PHE C C   1 
ATOM   1754 O O   . PHE C 1 44 ? 16.531  -29.819 22.957  1.00 35.30  ? 43  PHE C O   1 
ATOM   1755 C CB  . PHE C 1 44 ? 14.836  -30.293 25.295  1.00 38.68  ? 43  PHE C CB  1 
ATOM   1756 C CG  . PHE C 1 44 ? 13.469  -30.229 24.631  1.00 43.78  ? 43  PHE C CG  1 
ATOM   1757 C CD1 . PHE C 1 44 ? 12.519  -31.215 24.868  1.00 44.11  ? 43  PHE C CD1 1 
ATOM   1758 C CD2 . PHE C 1 44 ? 13.143  -29.170 23.782  1.00 46.11  ? 43  PHE C CD2 1 
ATOM   1759 C CE1 . PHE C 1 44 ? 11.275  -31.168 24.251  1.00 49.59  ? 43  PHE C CE1 1 
ATOM   1760 C CE2 . PHE C 1 44 ? 11.892  -29.117 23.181  1.00 45.02  ? 43  PHE C CE2 1 
ATOM   1761 C CZ  . PHE C 1 44 ? 10.966  -30.110 23.421  1.00 47.84  ? 43  PHE C CZ  1 
ATOM   1762 N N   . PHE C 1 45 ? 15.482  -31.724 22.279  1.00 36.85  ? 44  PHE C N   1 
ATOM   1763 C CA  . PHE C 1 45 ? 15.694  -31.511 20.854  1.00 40.68  ? 44  PHE C CA  1 
ATOM   1764 C C   . PHE C 1 45 ? 14.434  -30.888 20.273  1.00 35.90  ? 44  PHE C C   1 
ATOM   1765 O O   . PHE C 1 45 ? 13.340  -31.424 20.436  1.00 41.86  ? 44  PHE C O   1 
ATOM   1766 C CB  . PHE C 1 45 ? 16.042  -32.785 20.094  1.00 36.05  ? 44  PHE C CB  1 
ATOM   1767 C CG  . PHE C 1 45 ? 17.408  -33.345 20.453  1.00 34.79  ? 44  PHE C CG  1 
ATOM   1768 C CD1 . PHE C 1 45 ? 18.528  -33.058 19.675  1.00 33.26  ? 44  PHE C CD1 1 
ATOM   1769 C CD2 . PHE C 1 45 ? 17.569  -34.152 21.585  1.00 35.47  ? 44  PHE C CD2 1 
ATOM   1770 C CE1 . PHE C 1 45 ? 19.790  -33.583 19.991  1.00 35.84  ? 44  PHE C CE1 1 
ATOM   1771 C CE2 . PHE C 1 45 ? 18.829  -34.651 21.919  1.00 39.70  ? 44  PHE C CE2 1 
ATOM   1772 C CZ  . PHE C 1 45 ? 19.940  -34.361 21.126  1.00 35.62  ? 44  PHE C CZ  1 
ATOM   1773 N N   . PHE C 1 46 ? 14.602  -29.730 19.619  1.00 39.60  ? 45  PHE C N   1 
ATOM   1774 C CA  . PHE C 1 46 ? 13.449  -29.109 18.981  1.00 38.08  ? 45  PHE C CA  1 
ATOM   1775 C C   . PHE C 1 46 ? 12.977  -29.949 17.802  1.00 39.09  ? 45  PHE C C   1 
ATOM   1776 O O   . PHE C 1 46 ? 13.740  -30.720 17.197  1.00 35.90  ? 45  PHE C O   1 
ATOM   1777 C CB  . PHE C 1 46 ? 13.728  -27.678 18.517  1.00 36.33  ? 45  PHE C CB  1 
ATOM   1778 C CG  . PHE C 1 46 ? 13.995  -26.705 19.652  1.00 37.09  ? 45  PHE C CG  1 
ATOM   1779 C CD1 . PHE C 1 46 ? 12.960  -26.202 20.444  1.00 41.77  ? 45  PHE C CD1 1 
ATOM   1780 C CD2 . PHE C 1 46 ? 15.290  -26.236 19.863  1.00 36.39  ? 45  PHE C CD2 1 
ATOM   1781 C CE1 . PHE C 1 46 ? 13.250  -25.290 21.466  1.00 42.16  ? 45  PHE C CE1 1 
ATOM   1782 C CE2 . PHE C 1 46 ? 15.570  -25.348 20.891  1.00 41.65  ? 45  PHE C CE2 1 
ATOM   1783 C CZ  . PHE C 1 46 ? 14.548  -24.863 21.677  1.00 38.39  ? 45  PHE C CZ  1 
ATOM   1784 N N   . GLY C 1 47 ? 11.697  -29.759 17.464  1.00 34.60  ? 46  GLY C N   1 
ATOM   1785 C CA  . GLY C 1 47 ? 11.127  -30.445 16.320  1.00 38.49  ? 46  GLY C CA  1 
ATOM   1786 C C   . GLY C 1 47 ? 10.720  -31.864 16.698  1.00 42.05  ? 46  GLY C C   1 
ATOM   1787 O O   . GLY C 1 47 ? 9.547   -32.201 16.612  1.00 43.56  ? 46  GLY C O   1 
ATOM   1788 N N   . THR C 1 48 ? 11.687  -32.701 17.107  1.00 37.72  ? 47  THR C N   1 
ATOM   1789 C CA  . THR C 1 48 ? 11.343  -34.057 17.517  1.00 39.80  ? 47  THR C CA  1 
ATOM   1790 C C   . THR C 1 48 ? 10.794  -34.047 18.946  1.00 38.32  ? 47  THR C C   1 
ATOM   1791 O O   . THR C 1 48 ? 10.012  -34.934 19.296  1.00 44.23  ? 47  THR C O   1 
ATOM   1792 C CB  . THR C 1 48 ? 12.555  -34.991 17.427  1.00 36.85  ? 47  THR C CB  1 
ATOM   1793 O OG1 . THR C 1 48 ? 13.423  -34.517 18.453  1.00 39.85  ? 47  THR C OG1 1 
ATOM   1794 C CG2 . THR C 1 48 ? 13.160  -35.119 16.045  1.00 40.38  ? 47  THR C CG2 1 
ATOM   1795 N N   . HIS C 1 49 ? 11.231  -33.084 19.772  1.00 38.52  ? 48  HIS C N   1 
ATOM   1796 C CA  . HIS C 1 49 ? 10.869  -32.965 21.190  1.00 44.37  ? 48  HIS C CA  1 
ATOM   1797 C C   . HIS C 1 49 ? 11.351  -34.172 22.011  1.00 42.88  ? 48  HIS C C   1 
ATOM   1798 O O   . HIS C 1 49 ? 10.784  -34.498 23.056  1.00 47.03  ? 48  HIS C O   1 
ATOM   1799 C CB  . HIS C 1 49 ? 9.364   -32.712 21.376  1.00 42.03  ? 48  HIS C CB  1 
ATOM   1800 C CG  . HIS C 1 49 ? 8.802   -31.662 20.471  1.00 49.16  ? 48  HIS C CG  1 
ATOM   1801 N ND1 . HIS C 1 49 ? 7.612   -31.853 19.796  1.00 51.90  ? 48  HIS C ND1 1 
ATOM   1802 C CD2 . HIS C 1 49 ? 9.234   -30.435 20.137  1.00 53.10  ? 48  HIS C CD2 1 
ATOM   1803 C CE1 . HIS C 1 49 ? 7.344   -30.772 19.069  1.00 57.61  ? 48  HIS C CE1 1 
ATOM   1804 N NE2 . HIS C 1 49 ? 8.315   -29.897 19.252  1.00 48.65  ? 48  HIS C NE2 1 
ATOM   1805 N N   . GLU C 1 50 ? 12.415  -34.825 21.551  1.00 40.39  ? 49  GLU C N   1 
ATOM   1806 C CA  . GLU C 1 50 ? 12.996  -35.925 22.304  1.00 42.96  ? 49  GLU C CA  1 
ATOM   1807 C C   . GLU C 1 50 ? 14.085  -35.392 23.240  1.00 42.03  ? 49  GLU C C   1 
ATOM   1808 O O   . GLU C 1 50 ? 14.451  -34.210 23.216  1.00 43.18  ? 49  GLU C O   1 
ATOM   1809 C CB  . GLU C 1 50 ? 13.457  -37.007 21.330  1.00 44.13  ? 49  GLU C CB  1 
ATOM   1810 C CG  . GLU C 1 50 ? 12.318  -37.631 20.527  1.00 55.44  ? 49  GLU C CG  1 
ATOM   1811 C CD  . GLU C 1 50 ? 12.818  -38.600 19.475  1.00 63.21  ? 49  GLU C CD  1 
ATOM   1812 O OE1 . GLU C 1 50 ? 14.039  -38.859 19.473  1.00 77.34  ? 49  GLU C OE1 1 
ATOM   1813 O OE2 . GLU C 1 50 ? 12.011  -39.096 18.660  1.00 70.43  ? 49  GLU C OE2 1 
ATOM   1814 N N   . THR C 1 51 ? 14.573  -36.263 24.131  1.00 44.53  ? 50  THR C N   1 
ATOM   1815 C CA  . THR C 1 51 ? 15.606  -35.870 25.093  1.00 40.51  ? 50  THR C CA  1 
ATOM   1816 C C   . THR C 1 51 ? 16.736  -36.894 25.042  1.00 38.39  ? 50  THR C C   1 
ATOM   1817 O O   . THR C 1 51 ? 16.536  -38.031 24.618  1.00 44.81  ? 50  THR C O   1 
ATOM   1818 C CB  . THR C 1 51 ? 15.075  -35.768 26.526  1.00 45.95  ? 50  THR C CB  1 
ATOM   1819 O OG1 . THR C 1 51 ? 14.464  -37.038 26.762  1.00 48.00  ? 50  THR C OG1 1 
ATOM   1820 C CG2 . THR C 1 51 ? 14.130  -34.600 26.757  1.00 49.73  ? 50  THR C CG2 1 
ATOM   1821 N N   . ALA C 1 52 ? 17.920  -36.445 25.444  1.00 38.10  ? 51  ALA C N   1 
ATOM   1822 C CA  . ALA C 1 52 ? 19.094  -37.283 25.630  1.00 39.53  ? 51  ALA C CA  1 
ATOM   1823 C C   . ALA C 1 52 ? 20.067  -36.547 26.546  1.00 42.64  ? 51  ALA C C   1 
ATOM   1824 O O   . ALA C 1 52 ? 19.855  -35.391 26.893  1.00 41.78  ? 51  ALA C O   1 
ATOM   1825 C CB  . ALA C 1 52 ? 19.721  -37.646 24.309  1.00 44.02  ? 51  ALA C CB  1 
ATOM   1826 N N   . PHE C 1 53 ? 21.109  -37.254 26.994  1.00 41.36  ? 52  PHE C N   1 
ATOM   1827 C CA  . PHE C 1 53 ? 22.182  -36.629 27.746  1.00 41.90  ? 52  PHE C CA  1 
ATOM   1828 C C   . PHE C 1 53 ? 23.383  -36.539 26.828  1.00 40.98  ? 52  PHE C C   1 
ATOM   1829 O O   . PHE C 1 53 ? 23.736  -37.523 26.182  1.00 43.59  ? 52  PHE C O   1 
ATOM   1830 C CB  . PHE C 1 53 ? 22.579  -37.546 28.910  1.00 41.68  ? 52  PHE C CB  1 
ATOM   1831 C CG  . PHE C 1 53 ? 21.505  -37.629 29.979  1.00 42.79  ? 52  PHE C CG  1 
ATOM   1832 C CD1 . PHE C 1 53 ? 21.186  -36.521 30.756  1.00 42.11  ? 52  PHE C CD1 1 
ATOM   1833 C CD2 . PHE C 1 53 ? 20.822  -38.823 30.205  1.00 57.20  ? 52  PHE C CD2 1 
ATOM   1834 C CE1 . PHE C 1 53 ? 20.223  -36.608 31.749  1.00 49.17  ? 52  PHE C CE1 1 
ATOM   1835 C CE2 . PHE C 1 53 ? 19.840  -38.895 31.187  1.00 54.61  ? 52  PHE C CE2 1 
ATOM   1836 C CZ  . PHE C 1 53 ? 19.540  -37.784 31.948  1.00 52.79  ? 52  PHE C CZ  1 
ATOM   1837 N N   . LEU C 1 54 ? 24.023  -35.367 26.792  1.00 35.73  ? 53  LEU C N   1 
ATOM   1838 C CA  . LEU C 1 54 ? 25.192  -35.181 25.942  1.00 35.72  ? 53  LEU C CA  1 
ATOM   1839 C C   . LEU C 1 54 ? 26.271  -34.424 26.714  1.00 34.23  ? 53  LEU C C   1 
ATOM   1840 O O   . LEU C 1 54 ? 25.973  -33.669 27.633  1.00 38.82  ? 53  LEU C O   1 
ATOM   1841 C CB  . LEU C 1 54 ? 24.826  -34.440 24.650  1.00 36.80  ? 53  LEU C CB  1 
ATOM   1842 C CG  . LEU C 1 54 ? 23.958  -35.182 23.626  1.00 41.96  ? 53  LEU C CG  1 
ATOM   1843 C CD1 . LEU C 1 54 ? 23.612  -34.205 22.514  1.00 41.11  ? 53  LEU C CD1 1 
ATOM   1844 C CD2 . LEU C 1 54 ? 24.716  -36.379 23.040  1.00 47.05  ? 53  LEU C CD2 1 
ATOM   1845 N N   . GLY C 1 55 ? 27.526  -34.628 26.304  1.00 37.93  ? 54  GLY C N   1 
ATOM   1846 C CA  . GLY C 1 55 ? 28.678  -33.934 26.860  1.00 44.21  ? 54  GLY C CA  1 
ATOM   1847 C C   . GLY C 1 55 ? 28.960  -32.613 26.147  1.00 49.92  ? 54  GLY C C   1 
ATOM   1848 O O   . GLY C 1 55 ? 28.465  -32.337 25.039  1.00 40.48  ? 54  GLY C O   1 
ATOM   1849 N N   . PRO C 1 56 ? 29.744  -31.708 26.781  1.00 48.39  ? 55  PRO C N   1 
ATOM   1850 C CA  . PRO C 1 56 ? 29.962  -30.376 26.229  1.00 49.17  ? 55  PRO C CA  1 
ATOM   1851 C C   . PRO C 1 56 ? 30.604  -30.327 24.849  1.00 44.57  ? 55  PRO C C   1 
ATOM   1852 O O   . PRO C 1 56 ? 30.371  -29.368 24.117  1.00 56.03  ? 55  PRO C O   1 
ATOM   1853 C CB  . PRO C 1 56 ? 30.834  -29.681 27.310  1.00 49.73  ? 55  PRO C CB  1 
ATOM   1854 C CG  . PRO C 1 56 ? 31.504  -30.835 28.007  1.00 43.49  ? 55  PRO C CG  1 
ATOM   1855 C CD  . PRO C 1 56 ? 30.417  -31.887 28.080  1.00 48.28  ? 55  PRO C CD  1 
ATOM   1856 N N   . LYS C 1 57 ? 31.392  -31.353 24.503  1.00 43.62  ? 56  LYS C N   1 
ATOM   1857 C CA  . LYS C 1 57 ? 32.051  -31.364 23.206  1.00 49.35  ? 56  LYS C CA  1 
ATOM   1858 C C   . LYS C 1 57 ? 30.988  -31.486 22.111  1.00 51.05  ? 56  LYS C C   1 
ATOM   1859 O O   . LYS C 1 57 ? 31.255  -31.215 20.936  1.00 47.45  ? 56  LYS C O   1 
ATOM   1860 C CB  . LYS C 1 57 ? 32.950  -32.592 23.031  1.00 52.32  ? 56  LYS C CB  1 
ATOM   1861 N N   . ASP C 1 58 ? 29.792  -31.936 22.512  1.00 44.69  ? 57  ASP C N   1 
ATOM   1862 C CA  . ASP C 1 58 ? 28.758  -32.240 21.535  1.00 50.60  ? 57  ASP C CA  1 
ATOM   1863 C C   . ASP C 1 58 ? 27.811  -31.066 21.367  1.00 42.85  ? 57  ASP C C   1 
ATOM   1864 O O   . ASP C 1 58 ? 26.839  -31.187 20.622  1.00 39.76  ? 57  ASP C O   1 
ATOM   1865 C CB  . ASP C 1 58 ? 27.957  -33.483 21.881  1.00 45.29  ? 57  ASP C CB  1 
ATOM   1866 C CG  . ASP C 1 58 ? 28.782  -34.754 21.968  1.00 49.49  ? 57  ASP C CG  1 
ATOM   1867 O OD1 . ASP C 1 58 ? 29.720  -34.874 21.178  1.00 48.98  ? 57  ASP C OD1 1 
ATOM   1868 O OD2 . ASP C 1 58 ? 28.456  -35.602 22.816  1.00 54.52  ? 57  ASP C OD2 1 
ATOM   1869 N N   . LEU C 1 59 ? 28.084  -29.950 22.056  1.00 38.65  ? 58  LEU C N   1 
ATOM   1870 C CA  . LEU C 1 59 ? 27.138  -28.853 22.117  1.00 38.39  ? 58  LEU C CA  1 
ATOM   1871 C C   . LEU C 1 59 ? 27.781  -27.580 21.575  1.00 45.78  ? 58  LEU C C   1 
ATOM   1872 O O   . LEU C 1 59 ? 28.963  -27.366 21.823  1.00 51.12  ? 58  LEU C O   1 
ATOM   1873 C CB  . LEU C 1 59 ? 26.696  -28.664 23.568  1.00 41.18  ? 58  LEU C CB  1 
ATOM   1874 C CG  . LEU C 1 59 ? 26.112  -29.917 24.233  1.00 38.27  ? 58  LEU C CG  1 
ATOM   1875 C CD1 . LEU C 1 59 ? 25.890  -29.738 25.732  1.00 37.20  ? 58  LEU C CD1 1 
ATOM   1876 C CD2 . LEU C 1 59 ? 24.784  -30.281 23.572  1.00 32.78  ? 58  LEU C CD2 1 
ATOM   1877 N N   . PHE C 1 60 ? 26.991  -26.755 20.871  1.00 48.59  ? 59  PHE C N   1 
ATOM   1878 C CA  . PHE C 1 60 ? 27.474  -25.532 20.226  1.00 49.62  ? 59  PHE C CA  1 
ATOM   1879 C C   . PHE C 1 60 ? 26.470  -24.408 20.483  1.00 53.80  ? 59  PHE C C   1 
ATOM   1880 O O   . PHE C 1 60 ? 25.286  -24.533 20.166  1.00 49.29  ? 59  PHE C O   1 
ATOM   1881 C CB  . PHE C 1 60 ? 27.745  -25.718 18.726  1.00 49.53  ? 59  PHE C CB  1 
ATOM   1882 C CG  . PHE C 1 60 ? 28.647  -26.907 18.436  1.00 44.33  ? 59  PHE C CG  1 
ATOM   1883 C CD1 . PHE C 1 60 ? 28.145  -28.202 18.439  1.00 41.86  ? 59  PHE C CD1 1 
ATOM   1884 C CD2 . PHE C 1 60 ? 30.011  -26.741 18.193  1.00 49.07  ? 59  PHE C CD2 1 
ATOM   1885 C CE1 . PHE C 1 60 ? 28.979  -29.294 18.237  1.00 36.90  ? 59  PHE C CE1 1 
ATOM   1886 C CE2 . PHE C 1 60 ? 30.839  -27.836 17.947  1.00 44.24  ? 59  PHE C CE2 1 
ATOM   1887 C CZ  . PHE C 1 60 ? 30.326  -29.113 17.983  1.00 46.54  ? 59  PHE C CZ  1 
ATOM   1888 N N   . PRO C 1 61 ? 26.875  -23.266 21.089  1.00 49.44  ? 60  PRO C N   1 
ATOM   1889 C CA  . PRO C 1 61 ? 25.898  -22.223 21.417  1.00 48.81  ? 60  PRO C CA  1 
ATOM   1890 C C   . PRO C 1 61 ? 25.198  -21.759 20.133  1.00 40.21  ? 60  PRO C C   1 
ATOM   1891 O O   . PRO C 1 61 ? 25.805  -21.684 19.070  1.00 47.48  ? 60  PRO C O   1 
ATOM   1892 C CB  . PRO C 1 61 ? 26.679  -21.110 22.166  1.00 52.68  ? 60  PRO C CB  1 
ATOM   1893 C CG  . PRO C 1 61 ? 28.106  -21.648 22.270  1.00 48.30  ? 60  PRO C CG  1 
ATOM   1894 C CD  . PRO C 1 61 ? 28.265  -22.910 21.426  1.00 53.19  ? 60  PRO C CD  1 
ATOM   1895 N N   . TYR C 1 62 ? 23.881  -21.532 20.240  1.00 48.00  ? 61  TYR C N   1 
ATOM   1896 C CA  . TYR C 1 62 ? 23.030  -21.324 19.080  1.00 48.22  ? 61  TYR C CA  1 
ATOM   1897 C C   . TYR C 1 62 ? 23.490  -20.092 18.308  1.00 58.22  ? 61  TYR C C   1 
ATOM   1898 O O   . TYR C 1 62 ? 23.749  -20.172 17.107  1.00 58.17  ? 61  TYR C O   1 
ATOM   1899 C CB  . TYR C 1 62 ? 21.596  -21.050 19.519  1.00 44.88  ? 61  TYR C CB  1 
ATOM   1900 C CG  . TYR C 1 62 ? 20.644  -20.714 18.377  1.00 48.95  ? 61  TYR C CG  1 
ATOM   1901 C CD1 . TYR C 1 62 ? 20.504  -21.550 17.269  1.00 49.28  ? 61  TYR C CD1 1 
ATOM   1902 C CD2 . TYR C 1 62 ? 19.892  -19.546 18.413  1.00 51.15  ? 61  TYR C CD2 1 
ATOM   1903 C CE1 . TYR C 1 62 ? 19.609  -21.245 16.250  1.00 52.78  ? 61  TYR C CE1 1 
ATOM   1904 C CE2 . TYR C 1 62 ? 19.012  -19.223 17.392  1.00 58.96  ? 61  TYR C CE2 1 
ATOM   1905 C CZ  . TYR C 1 62 ? 18.859  -20.077 16.311  1.00 52.66  ? 61  TYR C CZ  1 
ATOM   1906 O OH  . TYR C 1 62 ? 17.969  -19.725 15.322  1.00 49.48  ? 61  TYR C OH  1 
ATOM   1907 N N   . ASP C 1 63 ? 23.588  -18.960 19.020  1.00 57.40  ? 62  ASP C N   1 
ATOM   1908 C CA  . ASP C 1 63 ? 23.882  -17.692 18.372  1.00 56.28  ? 62  ASP C CA  1 
ATOM   1909 C C   . ASP C 1 63 ? 25.216  -17.755 17.647  1.00 51.44  ? 62  ASP C C   1 
ATOM   1910 O O   . ASP C 1 63 ? 25.329  -17.237 16.538  1.00 62.16  ? 62  ASP C O   1 
ATOM   1911 C CB  . ASP C 1 63 ? 23.583  -16.491 19.256  1.00 64.00  ? 62  ASP C CB  1 
ATOM   1912 C CG  . ASP C 1 63 ? 22.095  -16.175 19.345  1.00 74.85  ? 62  ASP C CG  1 
ATOM   1913 O OD1 . ASP C 1 63 ? 21.639  -15.769 20.435  1.00 71.27  ? 62  ASP C OD1 1 
ATOM   1914 O OD2 . ASP C 1 63 ? 21.390  -16.375 18.324  1.00 76.53  ? 62  ASP C OD2 1 
ATOM   1915 N N   . LYS C 1 64 ? 26.189  -18.434 18.246  1.00 49.79  ? 63  LYS C N   1 
ATOM   1916 C CA  . LYS C 1 64 ? 27.542  -18.479 17.714  1.00 54.37  ? 63  LYS C CA  1 
ATOM   1917 C C   . LYS C 1 64 ? 27.611  -19.366 16.470  1.00 53.89  ? 63  LYS C C   1 
ATOM   1918 O O   . LYS C 1 64 ? 28.405  -19.095 15.569  1.00 51.16  ? 63  LYS C O   1 
ATOM   1919 C CB  . LYS C 1 64 ? 28.541  -18.882 18.806  1.00 60.07  ? 63  LYS C CB  1 
ATOM   1920 N N   . SER C 1 65 ? 26.730  -20.383 16.378  1.00 51.36  ? 64  SER C N   1 
ATOM   1921 C CA  . SER C 1 65 ? 26.910  -21.409 15.357  1.00 44.46  ? 64  SER C CA  1 
ATOM   1922 C C   . SER C 1 65 ? 25.735  -21.506 14.368  1.00 45.67  ? 64  SER C C   1 
ATOM   1923 O O   . SER C 1 65 ? 25.784  -22.314 13.451  1.00 46.21  ? 64  SER C O   1 
ATOM   1924 C CB  . SER C 1 65 ? 27.218  -22.748 15.996  1.00 49.78  ? 64  SER C CB  1 
ATOM   1925 O OG  . SER C 1 65 ? 26.049  -23.205 16.666  1.00 44.24  ? 64  SER C OG  1 
ATOM   1926 N N   . LYS C 1 66 ? 24.691  -20.686 14.514  1.00 49.10  ? 65  LYS C N   1 
ATOM   1927 C CA  . LYS C 1 66 ? 23.537  -20.838 13.631  1.00 49.12  ? 65  LYS C CA  1 
ATOM   1928 C C   . LYS C 1 66 ? 23.895  -20.552 12.174  1.00 56.07  ? 65  LYS C C   1 
ATOM   1929 O O   . LYS C 1 66 ? 23.291  -21.123 11.260  1.00 46.94  ? 65  LYS C O   1 
ATOM   1930 C CB  . LYS C 1 66 ? 22.307  -20.018 14.011  1.00 48.40  ? 65  LYS C CB  1 
ATOM   1931 C CG  . LYS C 1 66 ? 22.575  -18.540 14.164  1.00 42.15  ? 65  LYS C CG  1 
ATOM   1932 C CD  . LYS C 1 66 ? 21.234  -17.862 14.377  1.00 51.76  ? 65  LYS C CD  1 
ATOM   1933 C CE  . LYS C 1 66 ? 21.339  -16.539 15.029  1.00 49.48  ? 65  LYS C CE  1 
ATOM   1934 N NZ  . LYS C 1 66 ? 20.002  -15.965 14.963  1.00 59.28  ? 65  LYS C NZ  1 
ATOM   1935 N N   . ASP C 1 67 ? 24.888  -19.685 11.945  1.00 50.25  ? 66  ASP C N   1 
ATOM   1936 C CA  . ASP C 1 67 ? 25.219  -19.384 10.558  1.00 54.01  ? 66  ASP C CA  1 
ATOM   1937 C C   . ASP C 1 67 ? 25.666  -20.665 9.847   1.00 52.15  ? 66  ASP C C   1 
ATOM   1938 O O   . ASP C 1 67 ? 25.406  -20.842 8.664   1.00 47.57  ? 66  ASP C O   1 
ATOM   1939 C CB  . ASP C 1 67 ? 26.036  -18.107 10.376  1.00 51.11  ? 66  ASP C CB  1 
ATOM   1940 C CG  . ASP C 1 67 ? 27.493  -18.109 10.817  1.00 70.33  ? 66  ASP C CG  1 
ATOM   1941 O OD1 . ASP C 1 67 ? 28.183  -19.131 10.596  1.00 63.37  ? 66  ASP C OD1 1 
ATOM   1942 O OD2 . ASP C 1 67 ? 27.949  -17.047 11.304  1.00 74.21  ? 66  ASP C OD2 1 
ATOM   1943 N N   . LYS C 1 68 ? 26.255  -21.595 10.610  1.00 48.21  ? 67  LYS C N   1 
ATOM   1944 C CA  . LYS C 1 68 ? 26.774  -22.837 10.065  1.00 43.90  ? 67  LYS C CA  1 
ATOM   1945 C C   . LYS C 1 68 ? 25.762  -23.994 10.152  1.00 42.27  ? 67  LYS C C   1 
ATOM   1946 O O   . LYS C 1 68 ? 25.656  -24.781 9.215   1.00 45.58  ? 67  LYS C O   1 
ATOM   1947 C CB  . LYS C 1 68 ? 28.001  -23.149 10.919  1.00 40.89  ? 67  LYS C CB  1 
ATOM   1948 C CG  . LYS C 1 68 ? 28.788  -24.350 10.480  1.00 42.41  ? 67  LYS C CG  1 
ATOM   1949 C CD  . LYS C 1 68 ? 29.994  -24.492 11.417  1.00 53.59  ? 67  LYS C CD  1 
ATOM   1950 C CE  . LYS C 1 68 ? 30.779  -25.755 11.251  1.00 66.61  ? 67  LYS C CE  1 
ATOM   1951 N NZ  . LYS C 1 68 ? 31.335  -25.941 9.906   1.00 75.47  ? 67  LYS C NZ  1 
ATOM   1952 N N   . TYR C 1 69 ? 25.033  -24.127 11.271  1.00 40.22  ? 68  TYR C N   1 
ATOM   1953 C CA  . TYR C 1 69 ? 24.218  -25.330 11.444  1.00 39.13  ? 68  TYR C CA  1 
ATOM   1954 C C   . TYR C 1 69 ? 22.742  -25.039 11.210  1.00 36.67  ? 68  TYR C C   1 
ATOM   1955 O O   . TYR C 1 69 ? 21.950  -25.978 11.053  1.00 36.49  ? 68  TYR C O   1 
ATOM   1956 C CB  . TYR C 1 69 ? 24.395  -25.869 12.874  1.00 35.26  ? 68  TYR C CB  1 
ATOM   1957 C CG  . TYR C 1 69 ? 25.801  -26.378 13.148  1.00 37.27  ? 68  TYR C CG  1 
ATOM   1958 C CD1 . TYR C 1 69 ? 26.482  -27.214 12.264  1.00 42.53  ? 68  TYR C CD1 1 
ATOM   1959 C CD2 . TYR C 1 69 ? 26.436  -25.995 14.326  1.00 42.06  ? 68  TYR C CD2 1 
ATOM   1960 C CE1 . TYR C 1 69 ? 27.765  -27.670 12.549  1.00 41.89  ? 68  TYR C CE1 1 
ATOM   1961 C CE2 . TYR C 1 69 ? 27.704  -26.459 14.629  1.00 42.48  ? 68  TYR C CE2 1 
ATOM   1962 C CZ  . TYR C 1 69 ? 28.363  -27.276 13.736  1.00 42.24  ? 68  TYR C CZ  1 
ATOM   1963 O OH  . TYR C 1 69 ? 29.614  -27.658 14.111  1.00 47.12  ? 68  TYR C OH  1 
ATOM   1964 N N   . GLY C 1 70 ? 22.363  -23.747 11.227  1.00 37.15  ? 69  GLY C N   1 
ATOM   1965 C CA  . GLY C 1 70 ? 20.947  -23.400 11.177  1.00 38.86  ? 69  GLY C CA  1 
ATOM   1966 C C   . GLY C 1 70 ? 20.557  -23.255 9.713   1.00 38.92  ? 69  GLY C C   1 
ATOM   1967 O O   . GLY C 1 70 ? 20.529  -22.153 9.184   1.00 39.04  ? 69  GLY C O   1 
ATOM   1968 N N   . LYS C 1 71 ? 20.406  -24.404 9.059   1.00 35.56  ? 70  LYS C N   1 
ATOM   1969 C CA  . LYS C 1 71 ? 20.061  -24.473 7.648   1.00 39.48  ? 70  LYS C CA  1 
ATOM   1970 C C   . LYS C 1 71 ? 19.153  -25.680 7.512   1.00 45.39  ? 70  LYS C C   1 
ATOM   1971 O O   . LYS C 1 71 ? 19.272  -26.628 8.293   1.00 47.03  ? 70  LYS C O   1 
ATOM   1972 C CB  . LYS C 1 71 ? 21.283  -24.688 6.747   1.00 38.30  ? 70  LYS C CB  1 
ATOM   1973 C CG  . LYS C 1 71 ? 22.189  -25.800 7.185   1.00 48.14  ? 70  LYS C CG  1 
ATOM   1974 C CD  . LYS C 1 71 ? 23.431  -26.050 6.336   1.00 52.91  ? 70  LYS C CD  1 
ATOM   1975 C CE  . LYS C 1 71 ? 24.161  -27.273 6.819   1.00 55.63  ? 70  LYS C CE  1 
ATOM   1976 N N   . PRO C 1 72 ? 18.185  -25.662 6.576   1.00 37.24  ? 71  PRO C N   1 
ATOM   1977 C CA  . PRO C 1 72 ? 17.276  -26.793 6.456   1.00 34.72  ? 71  PRO C CA  1 
ATOM   1978 C C   . PRO C 1 72 ? 17.953  -28.118 6.112   1.00 35.19  ? 71  PRO C C   1 
ATOM   1979 O O   . PRO C 1 72 ? 19.002  -28.174 5.466   1.00 40.25  ? 71  PRO C O   1 
ATOM   1980 C CB  . PRO C 1 72 ? 16.284  -26.369 5.370   1.00 34.87  ? 71  PRO C CB  1 
ATOM   1981 C CG  . PRO C 1 72 ? 16.369  -24.866 5.417   1.00 35.90  ? 71  PRO C CG  1 
ATOM   1982 C CD  . PRO C 1 72 ? 17.811  -24.509 5.737   1.00 33.82  ? 71  PRO C CD  1 
ATOM   1983 N N   . ASN C 1 73 ? 17.257  -29.182 6.493   1.00 37.47  ? 72  ASN C N   1 
ATOM   1984 C CA  . ASN C 1 73 ? 17.570  -30.486 5.955   1.00 42.37  ? 72  ASN C CA  1 
ATOM   1985 C C   . ASN C 1 73 ? 16.342  -31.369 6.139   1.00 40.83  ? 72  ASN C C   1 
ATOM   1986 O O   . ASN C 1 73 ? 15.394  -31.026 6.843   1.00 41.26  ? 72  ASN C O   1 
ATOM   1987 C CB  . ASN C 1 73 ? 18.948  -31.007 6.365   1.00 53.01  ? 72  ASN C CB  1 
ATOM   1988 C CG  . ASN C 1 73 ? 18.948  -31.644 7.732   1.00 47.77  ? 72  ASN C CG  1 
ATOM   1989 O OD1 . ASN C 1 73 ? 18.213  -32.607 7.967   1.00 44.55  ? 72  ASN C OD1 1 
ATOM   1990 N ND2 . ASN C 1 73 ? 19.817  -31.165 8.605   1.00 51.49  ? 72  ASN C ND2 1 
ATOM   1991 N N   . LYS C 1 74 ? 16.390  -32.522 5.487   1.00 39.04  ? 73  LYS C N   1 
ATOM   1992 C CA  . LYS C 1 74 ? 15.176  -33.290 5.258   1.00 34.16  ? 73  LYS C CA  1 
ATOM   1993 C C   . LYS C 1 74 ? 14.932  -34.270 6.395   1.00 36.00  ? 73  LYS C C   1 
ATOM   1994 O O   . LYS C 1 74 ? 13.911  -34.969 6.409   1.00 41.29  ? 73  LYS C O   1 
ATOM   1995 C CB  . LYS C 1 74 ? 15.456  -34.087 3.975   1.00 43.19  ? 73  LYS C CB  1 
ATOM   1996 N N   . ARG C 1 75 ? 15.852  -34.319 7.368   1.00 34.79  ? 74  ARG C N   1 
ATOM   1997 C CA  . ARG C 1 75 ? 15.688  -35.305 8.430   1.00 34.63  ? 74  ARG C CA  1 
ATOM   1998 C C   . ARG C 1 75 ? 14.417  -35.005 9.224   1.00 35.34  ? 74  ARG C C   1 
ATOM   1999 O O   . ARG C 1 75 ? 14.064  -33.846 9.441   1.00 35.75  ? 74  ARG C O   1 
ATOM   2000 C CB  . ARG C 1 75 ? 16.922  -35.420 9.358   1.00 37.76  ? 74  ARG C CB  1 
ATOM   2001 C CG  . ARG C 1 75 ? 18.287  -35.623 8.701   1.00 42.73  ? 74  ARG C CG  1 
ATOM   2002 C CD  . ARG C 1 75 ? 18.563  -36.997 8.084   1.00 47.11  ? 74  ARG C CD  1 
ATOM   2003 N NE  . ARG C 1 75 ? 18.509  -37.941 9.202   1.00 42.82  ? 74  ARG C NE  1 
ATOM   2004 C CZ  . ARG C 1 75 ? 19.642  -38.355 9.798   1.00 37.80  ? 74  ARG C CZ  1 
ATOM   2005 N NH1 . ARG C 1 75 ? 19.559  -38.955 10.956  1.00 40.40  ? 74  ARG C NH1 1 
ATOM   2006 N NH2 . ARG C 1 75 ? 20.806  -38.072 9.253   1.00 43.59  ? 74  ARG C NH2 1 
ATOM   2007 N N   . LYS C 1 76 ? 13.764  -36.066 9.717   1.00 38.05  ? 75  LYS C N   1 
ATOM   2008 C CA  . LYS C 1 76 ? 12.475  -35.962 10.376  1.00 42.93  ? 75  LYS C CA  1 
ATOM   2009 C C   . LYS C 1 76 ? 12.525  -34.951 11.517  1.00 41.88  ? 75  LYS C C   1 
ATOM   2010 O O   . LYS C 1 76 ? 13.344  -35.068 12.434  1.00 38.20  ? 75  LYS C O   1 
ATOM   2011 C CB  . LYS C 1 76 ? 11.914  -37.315 10.840  1.00 46.05  ? 75  LYS C CB  1 
ATOM   2012 C CG  . LYS C 1 76 ? 10.407  -37.275 11.056  1.00 46.37  ? 75  LYS C CG  1 
ATOM   2013 C CD  . LYS C 1 76 ? 9.761   -38.533 11.632  1.00 57.82  ? 75  LYS C CD  1 
ATOM   2014 N N   . GLY C 1 77 ? 11.658  -33.932 11.417  1.00 42.91  ? 76  GLY C N   1 
ATOM   2015 C CA  . GLY C 1 77 ? 11.426  -33.003 12.514  1.00 39.23  ? 76  GLY C CA  1 
ATOM   2016 C C   . GLY C 1 77 ? 12.420  -31.833 12.526  1.00 33.94  ? 76  GLY C C   1 
ATOM   2017 O O   . GLY C 1 77 ? 12.280  -30.914 13.319  1.00 41.70  ? 76  GLY C O   1 
ATOM   2018 N N   . PHE C 1 78 ? 13.415  -31.856 11.645  1.00 36.77  ? 77  PHE C N   1 
ATOM   2019 C CA  . PHE C 1 78 ? 14.479  -30.877 11.709  1.00 33.81  ? 77  PHE C CA  1 
ATOM   2020 C C   . PHE C 1 78 ? 13.947  -29.465 11.446  1.00 38.76  ? 77  PHE C C   1 
ATOM   2021 O O   . PHE C 1 78 ? 14.286  -28.519 12.155  1.00 33.38  ? 77  PHE C O   1 
ATOM   2022 C CB  . PHE C 1 78 ? 15.586  -31.185 10.710  1.00 36.70  ? 77  PHE C CB  1 
ATOM   2023 C CG  . PHE C 1 78 ? 16.880  -30.442 11.020  1.00 38.50  ? 77  PHE C CG  1 
ATOM   2024 C CD1 . PHE C 1 78 ? 17.119  -29.169 10.503  1.00 37.57  ? 77  PHE C CD1 1 
ATOM   2025 C CD2 . PHE C 1 78 ? 17.895  -31.033 11.769  1.00 33.08  ? 77  PHE C CD2 1 
ATOM   2026 C CE1 . PHE C 1 78 ? 18.295  -28.491 10.782  1.00 38.42  ? 77  PHE C CE1 1 
ATOM   2027 C CE2 . PHE C 1 78 ? 19.087  -30.359 12.036  1.00 32.69  ? 77  PHE C CE2 1 
ATOM   2028 C CZ  . PHE C 1 78 ? 19.308  -29.101 11.522  1.00 36.13  ? 77  PHE C CZ  1 
ATOM   2029 N N   . ASN C 1 79 ? 13.193  -29.314 10.358  1.00 38.72  ? 78  ASN C N   1 
ATOM   2030 C CA  . ASN C 1 79 ? 12.851  -27.976 9.910   1.00 40.09  ? 78  ASN C CA  1 
ATOM   2031 C C   . ASN C 1 79 ? 11.871  -27.353 10.901  1.00 35.99  ? 78  ASN C C   1 
ATOM   2032 O O   . ASN C 1 79 ? 11.972  -26.162 11.223  1.00 37.27  ? 78  ASN C O   1 
ATOM   2033 C CB  . ASN C 1 79 ? 12.415  -27.978 8.449   1.00 37.51  ? 78  ASN C CB  1 
ATOM   2034 C CG  . ASN C 1 79 ? 13.565  -28.304 7.521   1.00 36.01  ? 78  ASN C CG  1 
ATOM   2035 O OD1 . ASN C 1 79 ? 14.713  -28.009 7.840   1.00 35.68  ? 78  ASN C OD1 1 
ATOM   2036 N ND2 . ASN C 1 79 ? 13.292  -28.913 6.370   1.00 35.69  ? 78  ASN C ND2 1 
ATOM   2037 N N   . GLU C 1 80 ? 10.970  -28.168 11.454  1.00 38.87  ? 79  GLU C N   1 
ATOM   2038 C CA  . GLU C 1 80 ? 10.145  -27.653 12.543  1.00 39.07  ? 79  GLU C CA  1 
ATOM   2039 C C   . GLU C 1 80 ? 11.031  -27.252 13.733  1.00 44.86  ? 79  GLU C C   1 
ATOM   2040 O O   . GLU C 1 80 ? 10.793  -26.229 14.388  1.00 39.12  ? 79  GLU C O   1 
ATOM   2041 C CB  . GLU C 1 80 ? 9.017   -28.657 12.831  1.00 45.12  ? 79  GLU C CB  1 
ATOM   2042 C CG  . GLU C 1 80 ? 8.102   -28.254 13.984  1.00 39.11  ? 79  GLU C CG  1 
ATOM   2043 C CD  . GLU C 1 80 ? 6.827   -29.064 14.177  1.00 50.50  ? 79  GLU C CD  1 
ATOM   2044 O OE1 . GLU C 1 80 ? 6.718   -30.179 13.629  1.00 52.97  ? 79  GLU C OE1 1 
ATOM   2045 O OE2 . GLU C 1 80 ? 5.911   -28.566 14.868  1.00 50.46  ? 79  GLU C OE2 1 
ATOM   2046 N N   . GLY C 1 81 ? 12.070  -28.063 14.023  1.00 38.87  ? 80  GLY C N   1 
ATOM   2047 C CA  . GLY C 1 81 ? 13.021  -27.696 15.074  1.00 37.20  ? 80  GLY C CA  1 
ATOM   2048 C C   . GLY C 1 81 ? 13.655  -26.319 14.828  1.00 38.30  ? 80  GLY C C   1 
ATOM   2049 O O   . GLY C 1 81 ? 13.818  -25.525 15.750  1.00 38.88  ? 80  GLY C O   1 
ATOM   2050 N N   . LEU C 1 82 ? 14.085  -26.055 13.581  1.00 37.59  ? 81  LEU C N   1 
ATOM   2051 C CA  . LEU C 1 82 ? 14.604  -24.733 13.224  1.00 38.10  ? 81  LEU C CA  1 
ATOM   2052 C C   . LEU C 1 82 ? 13.569  -23.640 13.506  1.00 35.06  ? 81  LEU C C   1 
ATOM   2053 O O   . LEU C 1 82 ? 13.935  -22.577 13.992  1.00 39.65  ? 81  LEU C O   1 
ATOM   2054 C CB  . LEU C 1 82 ? 15.047  -24.661 11.761  1.00 40.25  ? 81  LEU C CB  1 
ATOM   2055 C CG  . LEU C 1 82 ? 16.294  -25.471 11.391  1.00 35.32  ? 81  LEU C CG  1 
ATOM   2056 C CD1 . LEU C 1 82 ? 16.614  -25.228 9.928   1.00 34.97  ? 81  LEU C CD1 1 
ATOM   2057 C CD2 . LEU C 1 82 ? 17.513  -25.121 12.219  1.00 32.69  ? 81  LEU C CD2 1 
ATOM   2058 N N   . TRP C 1 83 ? 12.301  -23.882 13.187  1.00 37.73  ? 82  TRP C N   1 
ATOM   2059 C CA  . TRP C 1 83 ? 11.300  -22.851 13.431  1.00 43.76  ? 82  TRP C CA  1 
ATOM   2060 C C   . TRP C 1 83 ? 11.181  -22.581 14.940  1.00 43.19  ? 82  TRP C C   1 
ATOM   2061 O O   . TRP C 1 83 ? 11.166  -21.426 15.378  1.00 42.57  ? 82  TRP C O   1 
ATOM   2062 C CB  . TRP C 1 83 ? 9.941   -23.198 12.799  1.00 42.83  ? 82  TRP C CB  1 
ATOM   2063 C CG  . TRP C 1 83 ? 8.972   -22.055 12.950  1.00 47.41  ? 82  TRP C CG  1 
ATOM   2064 C CD1 . TRP C 1 83 ? 8.786   -21.004 12.090  1.00 49.29  ? 82  TRP C CD1 1 
ATOM   2065 C CD2 . TRP C 1 83 ? 8.114   -21.799 14.087  1.00 50.61  ? 82  TRP C CD2 1 
ATOM   2066 N NE1 . TRP C 1 83 ? 7.834   -20.143 12.586  1.00 48.70  ? 82  TRP C NE1 1 
ATOM   2067 C CE2 . TRP C 1 83 ? 7.406   -20.601 13.805  1.00 48.99  ? 82  TRP C CE2 1 
ATOM   2068 C CE3 . TRP C 1 83 ? 7.865   -22.471 15.296  1.00 43.77  ? 82  TRP C CE3 1 
ATOM   2069 C CZ2 . TRP C 1 83 ? 6.474   -20.066 14.693  1.00 51.92  ? 82  TRP C CZ2 1 
ATOM   2070 C CZ3 . TRP C 1 83 ? 6.936   -21.939 16.166  1.00 56.97  ? 82  TRP C CZ3 1 
ATOM   2071 C CH2 . TRP C 1 83 ? 6.265   -20.750 15.872  1.00 56.64  ? 82  TRP C CH2 1 
ATOM   2072 N N   . GLU C 1 84 ? 11.191  -23.658 15.735  1.00 38.53  ? 83  GLU C N   1 
ATOM   2073 C CA  . GLU C 1 84 ? 11.069  -23.564 17.189  1.00 43.50  ? 83  GLU C CA  1 
ATOM   2074 C C   . GLU C 1 84 ? 12.229  -22.791 17.822  1.00 43.24  ? 83  GLU C C   1 
ATOM   2075 O O   . GLU C 1 84 ? 11.996  -21.877 18.627  1.00 47.00  ? 83  GLU C O   1 
ATOM   2076 C CB  . GLU C 1 84 ? 10.908  -24.955 17.803  1.00 40.39  ? 83  GLU C CB  1 
ATOM   2077 C CG  . GLU C 1 84 ? 9.541   -25.577 17.534  1.00 42.35  ? 83  GLU C CG  1 
ATOM   2078 C CD  . GLU C 1 84 ? 9.448   -27.023 17.962  1.00 48.63  ? 83  GLU C CD  1 
ATOM   2079 O OE1 . GLU C 1 84 ? 10.468  -27.548 18.494  1.00 41.79  ? 83  GLU C OE1 1 
ATOM   2080 O OE2 . GLU C 1 84 ? 8.365   -27.621 17.750  1.00 50.27  ? 83  GLU C OE2 1 
ATOM   2081 N N   . ILE C 1 85 ? 13.480  -23.145 17.488  1.00 42.58  ? 84  ILE C N   1 
ATOM   2082 C CA  . ILE C 1 85 ? 14.607  -22.497 18.131  1.00 41.12  ? 84  ILE C CA  1 
ATOM   2083 C C   . ILE C 1 85 ? 14.630  -20.989 17.847  1.00 44.17  ? 84  ILE C C   1 
ATOM   2084 O O   . ILE C 1 85 ? 15.130  -20.225 18.657  1.00 40.79  ? 84  ILE C O   1 
ATOM   2085 C CB  . ILE C 1 85 ? 15.936  -23.183 17.784  1.00 39.03  ? 84  ILE C CB  1 
ATOM   2086 C CG1 . ILE C 1 85 ? 17.021  -22.835 18.791  1.00 41.53  ? 84  ILE C CG1 1 
ATOM   2087 C CG2 . ILE C 1 85 ? 16.362  -22.926 16.332  1.00 39.26  ? 84  ILE C CG2 1 
ATOM   2088 C CD1 . ILE C 1 85 ? 18.219  -23.774 18.796  1.00 43.04  ? 84  ILE C CD1 1 
ATOM   2089 N N   . GLN C 1 86 ? 14.137  -20.568 16.677  1.00 42.14  ? 85  GLN C N   1 
ATOM   2090 C CA  . GLN C 1 86 ? 14.264  -19.174 16.273  1.00 47.63  ? 85  GLN C CA  1 
ATOM   2091 C C   . GLN C 1 86 ? 13.064  -18.363 16.754  1.00 42.89  ? 85  GLN C C   1 
ATOM   2092 O O   . GLN C 1 86 ? 13.192  -17.165 16.992  1.00 47.16  ? 85  GLN C O   1 
ATOM   2093 C CB  . GLN C 1 86 ? 14.429  -19.034 14.753  1.00 41.47  ? 85  GLN C CB  1 
ATOM   2094 C CG  . GLN C 1 86 ? 14.596  -17.596 14.258  1.00 44.62  ? 85  GLN C CG  1 
ATOM   2095 C CD  . GLN C 1 86 ? 14.976  -17.540 12.790  1.00 44.73  ? 85  GLN C CD  1 
ATOM   2096 O OE1 . GLN C 1 86 ? 14.890  -18.551 12.075  1.00 42.20  ? 85  GLN C OE1 1 
ATOM   2097 N NE2 . GLN C 1 86 ? 15.455  -16.389 12.334  1.00 42.67  ? 85  GLN C NE2 1 
ATOM   2098 N N   . ASN C 1 87 ? 11.916  -19.015 16.908  1.00 45.85  ? 86  ASN C N   1 
ATOM   2099 C CA  . ASN C 1 87 ? 10.656  -18.305 17.052  1.00 51.52  ? 86  ASN C CA  1 
ATOM   2100 C C   . ASN C 1 87 ? 10.029  -18.535 18.434  1.00 53.31  ? 86  ASN C C   1 
ATOM   2101 O O   . ASN C 1 87 ? 9.440   -17.613 18.996  1.00 49.30  ? 86  ASN C O   1 
ATOM   2102 C CB  . ASN C 1 87 ? 9.711   -18.585 15.887  1.00 43.78  ? 86  ASN C CB  1 
ATOM   2103 C CG  . ASN C 1 87 ? 10.270  -18.039 14.597  1.00 54.03  ? 86  ASN C CG  1 
ATOM   2104 O OD1 . ASN C 1 87 ? 10.443  -16.822 14.462  1.00 52.10  ? 86  ASN C OD1 1 
ATOM   2105 N ND2 . ASN C 1 87 ? 10.608  -18.920 13.670  1.00 44.44  ? 86  ASN C ND2 1 
ATOM   2106 N N   . ASN C 1 88 ? 10.156  -19.755 18.977  1.00 52.23  ? 87  ASN C N   1 
ATOM   2107 C CA  . ASN C 1 88 ? 9.445   -20.129 20.193  1.00 49.25  ? 87  ASN C CA  1 
ATOM   2108 C C   . ASN C 1 88 ? 10.332  -21.005 21.076  1.00 51.12  ? 87  ASN C C   1 
ATOM   2109 O O   . ASN C 1 88 ? 9.921   -22.108 21.461  1.00 54.75  ? 87  ASN C O   1 
ATOM   2110 C CB  . ASN C 1 88 ? 8.167   -20.901 19.876  1.00 56.54  ? 87  ASN C CB  1 
ATOM   2111 C CG  . ASN C 1 88 ? 7.200   -20.859 21.037  1.00 61.84  ? 87  ASN C CG  1 
ATOM   2112 O OD1 . ASN C 1 88 ? 7.467   -20.181 22.041  1.00 64.23  ? 87  ASN C OD1 1 
ATOM   2113 N ND2 . ASN C 1 88 ? 6.077   -21.547 20.905  1.00 61.91  ? 87  ASN C ND2 1 
ATOM   2114 N N   . PRO C 1 89 ? 11.573  -20.572 21.391  1.00 47.80  ? 88  PRO C N   1 
ATOM   2115 C CA  . PRO C 1 89 ? 12.551  -21.460 22.034  1.00 50.84  ? 88  PRO C CA  1 
ATOM   2116 C C   . PRO C 1 89 ? 12.361  -21.872 23.493  1.00 56.04  ? 88  PRO C C   1 
ATOM   2117 O O   . PRO C 1 89 ? 13.039  -22.796 23.946  1.00 50.41  ? 88  PRO C O   1 
ATOM   2118 C CB  . PRO C 1 89 ? 13.881  -20.756 21.828  1.00 44.99  ? 88  PRO C CB  1 
ATOM   2119 C CG  . PRO C 1 89 ? 13.489  -19.297 21.749  1.00 50.72  ? 88  PRO C CG  1 
ATOM   2120 C CD  . PRO C 1 89 ? 12.135  -19.254 21.059  1.00 47.60  ? 88  PRO C CD  1 
ATOM   2121 N N   . HIS C 1 90 ? 11.424  -21.220 24.199  1.00 59.12  ? 89  HIS C N   1 
ATOM   2122 C CA  . HIS C 1 90 ? 11.248  -21.451 25.630  1.00 58.28  ? 89  HIS C CA  1 
ATOM   2123 C C   . HIS C 1 90 ? 9.820   -21.881 25.979  1.00 64.17  ? 89  HIS C C   1 
ATOM   2124 O O   . HIS C 1 90 ? 9.413   -21.749 27.129  1.00 71.02  ? 89  HIS C O   1 
ATOM   2125 C CB  . HIS C 1 90 ? 11.792  -20.277 26.451  1.00 47.07  ? 89  HIS C CB  1 
ATOM   2126 C CG  . HIS C 1 90 ? 13.236  -19.965 26.201  1.00 43.49  ? 89  HIS C CG  1 
ATOM   2127 N ND1 . HIS C 1 90 ? 13.639  -18.804 25.574  1.00 46.60  ? 89  HIS C ND1 1 
ATOM   2128 C CD2 . HIS C 1 90 ? 14.365  -20.613 26.520  1.00 46.46  ? 89  HIS C CD2 1 
ATOM   2129 C CE1 . HIS C 1 90 ? 14.966  -18.751 25.513  1.00 49.34  ? 89  HIS C CE1 1 
ATOM   2130 N NE2 . HIS C 1 90 ? 15.431  -19.853 26.077  1.00 49.86  ? 89  HIS C NE2 1 
ATOM   2131 N N   . ALA C 1 91 ? 9.082   -22.442 25.012  1.00 66.83  ? 90  ALA C N   1 
ATOM   2132 C CA  . ALA C 1 91 ? 7.748   -22.991 25.248  1.00 68.19  ? 90  ALA C CA  1 
ATOM   2133 C C   . ALA C 1 91 ? 7.817   -24.460 25.682  1.00 68.26  ? 90  ALA C C   1 
ATOM   2134 O O   . ALA C 1 91 ? 8.875   -25.084 25.634  1.00 71.69  ? 90  ALA C O   1 
ATOM   2135 C CB  . ALA C 1 91 ? 6.874   -22.815 24.022  1.00 66.49  ? 90  ALA C CB  1 
ATOM   2136 N N   . SER C 1 92 ? 6.649   -25.017 26.033  1.00 83.55  ? 91  SER C N   1 
ATOM   2137 C CA  . SER C 1 92 ? 6.502   -26.278 26.752  1.00 86.11  ? 91  SER C CA  1 
ATOM   2138 C C   . SER C 1 92 ? 6.759   -27.494 25.866  1.00 79.51  ? 91  SER C C   1 
ATOM   2139 O O   . SER C 1 92 ? 7.611   -28.317 26.187  1.00 82.06  ? 91  SER C O   1 
ATOM   2140 C CB  . SER C 1 92 ? 5.128   -26.387 27.381  1.00 86.97  ? 91  SER C CB  1 
ATOM   2141 O OG  . SER C 1 92 ? 4.914   -25.348 28.323  1.00 92.27  ? 91  SER C OG  1 
ATOM   2142 N N   . TYR C 1 93 ? 5.945   -27.630 24.809  1.00 85.74  ? 92  TYR C N   1 
ATOM   2143 C CA  . TYR C 1 93 ? 5.920   -28.776 23.905  1.00 86.12  ? 92  TYR C CA  1 
ATOM   2144 C C   . TYR C 1 93 ? 5.655   -30.078 24.682  1.00 87.96  ? 92  TYR C C   1 
ATOM   2145 O O   . TYR C 1 93 ? 4.883   -30.107 25.673  1.00 100.47 ? 92  TYR C O   1 
ATOM   2146 C CB  . TYR C 1 93 ? 7.175   -28.877 23.026  1.00 86.63  ? 92  TYR C CB  1 
ATOM   2147 C CG  . TYR C 1 93 ? 7.527   -27.611 22.252  1.00 77.28  ? 92  TYR C CG  1 
ATOM   2148 C CD1 . TYR C 1 93 ? 6.831   -27.251 21.098  1.00 70.13  ? 92  TYR C CD1 1 
ATOM   2149 C CD2 . TYR C 1 93 ? 8.564   -26.780 22.672  1.00 68.23  ? 92  TYR C CD2 1 
ATOM   2150 C CE1 . TYR C 1 93 ? 7.141   -26.099 20.393  1.00 65.61  ? 92  TYR C CE1 1 
ATOM   2151 C CE2 . TYR C 1 93 ? 8.894   -25.636 21.963  1.00 60.60  ? 92  TYR C CE2 1 
ATOM   2152 C CZ  . TYR C 1 93 ? 8.180   -25.292 20.827  1.00 63.87  ? 92  TYR C CZ  1 
ATOM   2153 O OH  . TYR C 1 93 ? 8.507   -24.150 20.147  1.00 63.50  ? 92  TYR C OH  1 
HETATM 2154 S S   . SO4 D 2 .  ? 1.804   -34.104 1.792   1.00 100.73 ? 101 SO4 A S   1 
HETATM 2155 O O1  . SO4 D 2 .  ? 2.733   -34.576 0.796   1.00 74.04  ? 101 SO4 A O1  1 
HETATM 2156 O O2  . SO4 D 2 .  ? 1.851   -32.661 1.867   1.00 74.17  ? 101 SO4 A O2  1 
HETATM 2157 O O3  . SO4 D 2 .  ? 0.466   -34.527 1.437   1.00 104.27 ? 101 SO4 A O3  1 
HETATM 2158 O O4  . SO4 D 2 .  ? 2.165   -34.665 3.072   1.00 98.37  ? 101 SO4 A O4  1 
HETATM 2159 S S   . SO4 E 2 .  ? -8.956  -24.690 1.308   1.00 104.42 ? 102 SO4 A S   1 
HETATM 2160 O O1  . SO4 E 2 .  ? -9.410  -24.363 -0.018  1.00 91.22  ? 102 SO4 A O1  1 
HETATM 2161 O O2  . SO4 E 2 .  ? -9.302  -23.620 2.210   1.00 98.15  ? 102 SO4 A O2  1 
HETATM 2162 O O3  . SO4 E 2 .  ? -9.570  -25.922 1.747   1.00 98.53  ? 102 SO4 A O3  1 
HETATM 2163 O O4  . SO4 E 2 .  ? -7.528  -24.855 1.298   1.00 111.99 ? 102 SO4 A O4  1 
HETATM 2164 C C1  . EDO F 3 .  ? 14.370  -19.619 -7.433  1.00 46.91  ? 103 EDO A C1  1 
HETATM 2165 O O1  . EDO F 3 .  ? 15.590  -18.926 -7.126  1.00 39.20  ? 103 EDO A O1  1 
HETATM 2166 C C2  . EDO F 3 .  ? 13.560  -19.065 -8.567  1.00 44.47  ? 103 EDO A C2  1 
HETATM 2167 O O2  . EDO F 3 .  ? 12.928  -17.814 -8.305  1.00 40.15  ? 103 EDO A O2  1 
HETATM 2168 S S   . SO4 G 2 .  ? 9.454   -29.492 5.782   1.00 67.14  ? 104 SO4 A S   1 
HETATM 2169 O O1  . SO4 G 2 .  ? 10.264  -28.896 4.774   1.00 52.17  ? 104 SO4 A O1  1 
HETATM 2170 O O2  . SO4 G 2 .  ? 8.752   -30.619 5.198   1.00 71.24  ? 104 SO4 A O2  1 
HETATM 2171 O O3  . SO4 G 2 .  ? 10.271  -29.942 6.892   1.00 70.27  ? 104 SO4 A O3  1 
HETATM 2172 O O4  . SO4 G 2 .  ? 8.489   -28.528 6.238   1.00 84.61  ? 104 SO4 A O4  1 
HETATM 2173 C C4  . UVA H 4 .  ? 21.185  -15.283 -24.372 0.78 31.51  ? 105 UVA A C4  1 
HETATM 2174 C C5  . UVA H 4 .  ? 19.901  -15.058 -24.810 0.78 31.35  ? 105 UVA A C5  1 
HETATM 2175 C C6  . UVA H 4 .  ? 18.864  -14.996 -23.879 0.78 29.52  ? 105 UVA A C6  1 
HETATM 2176 C C7  . UVA H 4 .  ? 16.781  -16.088 -25.371 0.78 30.74  ? 105 UVA A C7  1 
HETATM 2177 N N   . UVA H 4 .  ? 18.079  -15.076 -21.587 0.78 32.39  ? 105 UVA A N   1 
HETATM 2178 C C   . UVA H 4 .  ? 18.329  -15.240 -20.179 0.78 33.98  ? 105 UVA A C   1 
HETATM 2179 O O   . UVA H 4 .  ? 17.390  -13.580 -25.499 0.78 31.35  ? 105 UVA A O   1 
HETATM 2180 C C1  . UVA H 4 .  ? 19.113  -15.173 -22.506 0.78 33.04  ? 105 UVA A C1  1 
HETATM 2181 C C2  . UVA H 4 .  ? 20.419  -15.433 -22.088 0.78 32.79  ? 105 UVA A C2  1 
HETATM 2182 C C3  . UVA H 4 .  ? 21.447  -15.471 -23.024 0.78 30.72  ? 105 UVA A C3  1 
HETATM 2183 O O1  . UVA H 4 .  ? 16.346  -14.404 -23.444 0.78 29.70  ? 105 UVA A O1  1 
HETATM 2184 S S   . UVA H 4 .  ? 17.273  -14.628 -24.526 0.78 29.91  ? 105 UVA A S   1 
HETATM 2185 S S   . SO4 I 2 .  ? 7.535   -8.448  -24.898 1.00 84.23  ? 101 SO4 B S   1 
HETATM 2186 O O1  . SO4 I 2 .  ? 8.596   -8.459  -25.861 1.00 46.15  ? 101 SO4 B O1  1 
HETATM 2187 O O2  . SO4 I 2 .  ? 6.347   -9.037  -25.477 1.00 63.46  ? 101 SO4 B O2  1 
HETATM 2188 O O3  . SO4 I 2 .  ? 7.869   -9.223  -23.703 1.00 56.17  ? 101 SO4 B O3  1 
HETATM 2189 O O4  . SO4 I 2 .  ? 7.335   -7.052  -24.564 1.00 69.36  ? 101 SO4 B O4  1 
HETATM 2190 S S   . SO4 J 2 .  ? 14.569  -26.953 -26.645 1.00 65.99  ? 102 SO4 B S   1 
HETATM 2191 O O1  . SO4 J 2 .  ? 15.878  -26.573 -26.179 1.00 69.68  ? 102 SO4 B O1  1 
HETATM 2192 O O2  . SO4 J 2 .  ? 14.677  -28.151 -27.445 1.00 79.96  ? 102 SO4 B O2  1 
HETATM 2193 O O3  . SO4 J 2 .  ? 13.718  -27.213 -25.521 1.00 78.37  ? 102 SO4 B O3  1 
HETATM 2194 O O4  . SO4 J 2 .  ? 13.988  -25.895 -27.433 1.00 61.43  ? 102 SO4 B O4  1 
HETATM 2195 C C1  . EDO K 3 .  ? 17.058  -36.507 16.609  1.00 40.37  ? 101 EDO C C1  1 
HETATM 2196 O O1  . EDO K 3 .  ? 15.966  -37.050 15.876  1.00 49.81  ? 101 EDO C O1  1 
HETATM 2197 C C2  . EDO K 3 .  ? 16.620  -35.471 17.534  1.00 37.82  ? 101 EDO C C2  1 
HETATM 2198 O O2  . EDO K 3 .  ? 15.706  -35.976 18.404  1.00 41.76  ? 101 EDO C O2  1 
HETATM 2199 S S   . SO4 L 2 .  ? 29.695  -38.608 12.396  1.00 109.00 ? 102 SO4 C S   1 
HETATM 2200 O O1  . SO4 L 2 .  ? 30.738  -37.675 12.048  1.00 107.73 ? 102 SO4 C O1  1 
HETATM 2201 O O2  . SO4 L 2 .  ? 28.500  -38.294 11.663  1.00 97.99  ? 102 SO4 C O2  1 
HETATM 2202 O O3  . SO4 L 2 .  ? 30.102  -39.945 12.069  1.00 87.44  ? 102 SO4 C O3  1 
HETATM 2203 O O4  . SO4 L 2 .  ? 29.435  -38.521 13.810  1.00 117.58 ? 102 SO4 C O4  1 
HETATM 2204 O O   . HOH M 5 .  ? 10.922  -19.170 10.290  1.00 70.41  ? 201 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 9.510   -32.273 3.910   1.00 56.91  ? 202 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 4.121   2.717   0.174   1.00 73.52  ? 203 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? -5.502  -13.240 -16.538 1.00 48.00  ? 204 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 6.280   -29.134 6.738   1.00 55.22  ? 205 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? -1.546  -9.673  4.528   1.00 60.95  ? 206 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 11.428  -29.641 2.765   1.00 50.80  ? 207 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 17.498  -18.050 -9.663  1.00 54.48  ? 208 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? -1.934  -30.899 -3.381  1.00 58.58  ? 209 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 15.551  -17.097 -19.190 1.00 41.28  ? 210 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 5.033   -8.017  1.182   1.00 40.58  ? 211 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.489   -18.052 -11.008 1.00 41.27  ? 212 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 0.864   -10.542 -15.476 1.00 51.96  ? 213 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 2.910   -25.185 -6.636  1.00 61.41  ? 214 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 0.767   -33.712 5.008   1.00 61.17  ? 215 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 13.385  -11.965 7.920   1.00 60.02  ? 216 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? -3.354  -10.858 6.672   1.00 44.21  ? 217 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 16.272  -24.533 1.807   1.00 43.98  ? 218 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? -1.958  3.184   -2.113  1.00 45.82  ? 219 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 11.227  -5.288  -7.805  1.00 41.64  ? 220 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 8.597   -17.832 -15.936 1.00 57.24  ? 221 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 0.740   -23.152 9.278   1.00 50.39  ? 222 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? -0.380  -20.529 11.106  1.00 61.54  ? 223 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 7.389   -10.541 -12.155 1.00 42.12  ? 224 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? -7.476  -17.110 6.658   1.00 44.62  ? 225 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -5.855  -11.402 -11.446 1.00 46.94  ? 226 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 11.540  -23.773 9.781   1.00 44.43  ? 227 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 9.998   -6.112  -1.719  1.00 38.90  ? 228 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -0.095  -20.985 6.963   1.00 37.51  ? 229 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 3.707   -29.549 -0.597  1.00 44.25  ? 230 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 13.296  -9.498  -7.281  1.00 51.04  ? 231 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? -3.550  -21.174 6.040   1.00 48.80  ? 232 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 11.807  -12.326 -6.167  1.00 32.32  ? 233 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 20.269  -15.467 7.286   1.00 32.27  ? 234 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 11.803  -16.318 -15.009 1.00 44.57  ? 235 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 2.107   -4.743  -10.310 1.00 47.62  ? 236 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 13.688  -11.993 -4.217  1.00 27.86  ? 237 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 4.774   -3.533  -3.228  1.00 40.41  ? 238 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 14.167  -28.105 -4.675  1.00 68.04  ? 239 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 2.076   0.529   -7.498  1.00 46.16  ? 240 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -5.321  -19.716 -5.670  1.00 39.73  ? 241 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -5.326  -15.962 -8.051  1.00 34.74  ? 242 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 9.093   -16.065 -13.221 1.00 41.53  ? 243 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 17.608  -12.866 1.344   1.00 27.83  ? 244 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 2.828   -25.177 -10.044 1.00 42.57  ? 245 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 11.856  -11.928 5.798   1.00 39.90  ? 246 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -1.403  -22.083 -0.682  1.00 33.96  ? 247 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 14.473  -15.622 -9.212  1.00 43.05  ? 248 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 2.808   -6.377  5.480   1.00 39.80  ? 249 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -2.352  -11.407 13.600  1.00 48.60  ? 250 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 8.173   -7.846  1.188   1.00 37.08  ? 251 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 4.700   -35.054 4.313   1.00 66.06  ? 252 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -7.730  -15.727 -0.990  1.00 42.24  ? 253 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 2.041   -10.541 11.551  1.00 41.60  ? 254 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 9.998   -20.117 -18.600 1.00 46.30  ? 255 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 16.915  -11.944 -17.167 1.00 39.82  ? 256 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? -5.450  -16.895 -15.820 1.00 55.37  ? 257 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 16.072  -11.908 -5.289  1.00 38.42  ? 258 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -7.427  -16.629 1.546   1.00 44.23  ? 259 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 5.656   -7.744  4.063   1.00 39.65  ? 260 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -1.077  -11.801 11.370  1.00 41.92  ? 261 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 3.132   -9.709  -13.080 1.00 57.17  ? 262 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? -7.938  -19.333 -3.392  1.00 51.53  ? 263 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 6.470   -16.258 -15.011 1.00 54.67  ? 264 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 10.461  -12.971 9.631   1.00 43.48  ? 265 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -5.848  -12.802 6.661   1.00 46.57  ? 266 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 14.811  -29.401 3.887   1.00 44.87  ? 267 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -0.026  -29.463 10.392  1.00 57.04  ? 268 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 6.834   -5.924  0.446   1.00 63.65  ? 269 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -4.053  -25.969 -5.689  1.00 51.65  ? 270 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 11.693  -5.946  -3.828  1.00 53.79  ? 271 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? -8.114  -21.107 -1.329  1.00 46.93  ? 272 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -1.219  -7.508  11.371  1.00 50.56  ? 273 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 1.867   -18.625 -18.558 1.00 49.02  ? 274 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 13.061  -13.413 -8.563  1.00 48.83  ? 275 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 8.533   -17.618 8.649   1.00 46.25  ? 276 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 22.125  -20.269 -3.802  1.00 58.27  ? 277 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? 15.611  -28.311 -0.866  1.00 59.73  ? 278 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 11.524  -7.840  0.371   1.00 31.99  ? 279 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -3.614  -7.922  10.315  1.00 53.16  ? 280 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 21.778  -16.754 -3.428  1.00 35.15  ? 281 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -6.267  -13.730 -11.677 1.00 59.83  ? 282 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? 8.498   -8.403  4.529   1.00 41.64  ? 283 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 2.192   -24.900 14.481  1.00 58.21  ? 284 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 15.523  -13.389 10.540  1.00 63.30  ? 285 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? -6.932  -11.508 -7.966  1.00 34.18  ? 286 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? -3.352  -26.679 7.459   1.00 58.34  ? 287 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -5.409  -26.683 3.303   1.00 61.11  ? 288 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 8.475   -8.324  12.965  1.00 58.83  ? 289 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 10.694  -27.739 -7.448  1.00 60.65  ? 290 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 22.791  -16.732 -0.537  1.00 46.27  ? 291 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? -10.668 -16.137 -3.574  1.00 54.18  ? 292 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 9.932   -2.028  -0.534  1.00 93.97  ? 293 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 8.000   -30.183 -3.850  1.00 59.39  ? 294 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? 17.924  -13.926 10.647  1.00 54.74  ? 295 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? -5.114  -23.597 -6.649  1.00 48.13  ? 296 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 13.609  -15.125 -12.209 1.00 56.19  ? 297 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 1.102   -29.738 -7.148  1.00 67.34  ? 298 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 9.029   -9.090  -13.761 1.00 42.14  ? 299 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? -5.461  -21.833 6.376   1.00 58.25  ? 300 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? 0.176   -3.373  -11.040 1.00 59.05  ? 301 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? -3.496  -11.151 9.449   1.00 57.21  ? 302 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? -6.935  -14.051 -9.273  1.00 41.95  ? 303 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -9.005  -14.683 -12.959 1.00 65.70  ? 304 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? -5.549  -23.662 5.424   1.00 59.08  ? 305 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? 11.825  -1.911  -1.881  1.00 49.92  ? 306 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? -6.968  -19.011 7.918   1.00 58.34  ? 307 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? -10.399 -28.244 -1.932  1.00 66.04  ? 308 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? -10.864 -13.518 -2.971  1.00 49.88  ? 309 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? 15.656  -13.819 -12.820 1.00 52.62  ? 310 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? 5.098   -9.628  -11.290 1.00 54.75  ? 311 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? -4.493  -20.956 -8.237  1.00 59.72  ? 312 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? 8.908   -22.492 -19.221 1.00 61.01  ? 313 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? 4.537   -3.244  1.619   1.00 62.55  ? 314 HOH A O   1 
HETATM 2318 O O   . HOH N 5 .  ? 24.174  -1.613  -36.300 1.00 56.81  ? 201 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 10.105  -11.409 -38.272 1.00 57.07  ? 202 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 30.660  -8.169  -30.208 1.00 71.63  ? 203 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 6.777   -12.255 -26.153 1.00 43.35  ? 204 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 8.632   -27.352 -38.396 1.00 66.29  ? 205 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 26.070  -4.447  -33.354 1.00 52.12  ? 206 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 26.242  -22.971 -31.226 1.00 44.43  ? 207 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 27.776  -8.188  -28.779 1.00 44.73  ? 208 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 10.423  -19.367 -43.116 1.00 61.64  ? 209 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 30.320  -12.299 -45.416 1.00 81.01  ? 210 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 30.434  -19.739 -40.322 1.00 44.20  ? 211 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 20.328  -21.995 -23.191 1.00 62.04  ? 212 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 18.780  -0.250  -25.403 1.00 64.78  ? 213 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 23.596  -11.166 -22.074 1.00 41.61  ? 214 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 25.291  -15.464 -22.749 1.00 51.33  ? 215 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 20.665  -13.387 -42.868 1.00 45.30  ? 216 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 21.754  3.679   -32.696 1.00 51.41  ? 217 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 27.211  -10.775 -28.881 1.00 51.62  ? 218 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 23.358  -5.824  -24.665 1.00 56.15  ? 219 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 17.660  -19.611 -42.154 1.00 52.26  ? 220 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 16.849  -19.157 -28.929 1.00 33.11  ? 221 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 28.002  -17.435 -25.101 1.00 49.24  ? 222 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 32.535  -18.785 -42.548 1.00 59.92  ? 223 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 23.637  -4.138  -36.990 1.00 38.40  ? 224 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 10.571  -18.781 -33.105 1.00 32.21  ? 225 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 25.044  -4.875  -29.915 1.00 44.86  ? 226 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 7.291   -19.274 -34.990 1.00 50.45  ? 227 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 13.191  -4.444  -41.986 1.00 61.11  ? 228 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 34.810  -23.289 -30.128 1.00 74.97  ? 229 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 10.286  -16.771 -44.438 1.00 56.24  ? 230 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 18.166  -0.467  -38.560 1.00 36.06  ? 231 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 25.289  -5.754  -35.949 1.00 51.00  ? 232 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 32.418  -11.721 -41.822 1.00 52.09  ? 233 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 9.176   -8.666  -16.511 1.00 46.65  ? 234 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 31.568  -12.193 -38.893 1.00 67.06  ? 235 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 5.827   -7.367  -32.318 1.00 56.46  ? 236 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 13.301  -22.568 -20.751 1.00 63.92  ? 237 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 19.952  -25.507 -34.216 1.00 44.83  ? 238 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 20.368  -10.094 -43.048 1.00 47.38  ? 239 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 8.302   -23.526 -24.392 1.00 60.92  ? 240 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 23.815  -2.259  -29.389 1.00 57.27  ? 241 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 10.700  -21.828 -32.863 1.00 42.60  ? 242 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 14.315  -6.331  -41.322 1.00 48.39  ? 243 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 7.418   -12.524 -39.054 1.00 53.92  ? 244 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 22.783  -23.171 -28.860 1.00 43.97  ? 245 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 7.520   -18.281 -31.744 1.00 55.04  ? 246 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 17.672  -3.453  -22.202 1.00 70.53  ? 247 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 3.668   -8.674  -26.800 1.00 65.88  ? 248 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 21.422  -27.328 -29.843 1.00 68.20  ? 249 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 1.713   -12.979 -28.327 1.00 51.79  ? 250 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 14.805  -24.353 -40.432 1.00 47.81  ? 251 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 18.049  -15.926 -45.907 1.00 53.76  ? 252 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 31.926  -21.186 -38.265 1.00 48.46  ? 253 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 21.180  -6.332  -42.681 1.00 43.35  ? 254 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 18.592  -25.887 -28.905 1.00 47.29  ? 255 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 6.723   -20.598 -25.008 1.00 45.62  ? 256 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 16.903  -9.422  -44.166 1.00 52.52  ? 257 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 12.536  -4.245  -25.097 1.00 55.36  ? 258 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 7.858   -8.096  -20.776 1.00 57.17  ? 259 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 28.014  -24.769 -35.141 1.00 45.87  ? 260 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 5.190   -19.369 -25.804 1.00 57.01  ? 261 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 18.539  4.536   -34.314 1.00 44.97  ? 262 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 26.338  -0.294  -29.581 1.00 55.81  ? 263 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 20.423  4.056   -33.266 1.00 48.46  ? 264 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 9.865   -5.946  -41.102 1.00 52.15  ? 265 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 24.679  -6.220  -42.926 1.00 48.81  ? 266 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 39.319  -13.238 -39.268 1.00 70.07  ? 267 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 17.508  -25.441 -21.018 1.00 66.01  ? 268 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 13.334  -19.911 -19.650 1.00 63.90  ? 269 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 20.049  -3.305  -22.485 1.00 65.80  ? 270 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 15.218  -7.936  -43.121 1.00 51.56  ? 271 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 28.067  -24.754 -32.329 1.00 49.70  ? 272 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 17.662  -17.262 -16.960 1.00 48.23  ? 273 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 16.538  2.162   -30.833 1.00 59.16  ? 274 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 14.733  -21.958 -41.963 1.00 61.19  ? 275 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 7.596   -9.929  -18.596 1.00 45.63  ? 276 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 22.652  -29.164 -35.650 1.00 50.36  ? 277 HOH B O   1 
HETATM 2395 O O   . HOH O 5 .  ? 27.374  -38.047 10.168  1.00 49.98  ? 201 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 29.934  -27.425 30.260  1.00 62.45  ? 202 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 20.465  -19.978 29.929  1.00 67.32  ? 203 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 26.864  -39.376 12.698  1.00 44.45  ? 204 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 15.974  -21.806 13.441  1.00 53.23  ? 205 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 13.404  -19.866 11.003  1.00 60.20  ? 206 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 7.461   -18.674 18.559  1.00 75.89  ? 207 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 19.675  -20.271 10.482  1.00 45.01  ? 208 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 17.702  -17.242 15.076  1.00 55.05  ? 209 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 25.898  -19.598 6.540   1.00 49.21  ? 210 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 15.644  -39.261 17.076  1.00 62.98  ? 211 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 28.320  -37.385 15.925  1.00 58.81  ? 212 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 28.593  -15.029 12.735  1.00 58.74  ? 213 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 6.085   -26.848 16.876  1.00 58.49  ? 214 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 28.250  -37.815 24.985  1.00 58.54  ? 215 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 15.440  -21.095 12.118  1.00 39.37  ? 216 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 16.788  -37.826 19.886  1.00 54.24  ? 217 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 9.168   -37.063 18.043  1.00 65.79  ? 218 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 31.942  -33.510 25.870  1.00 51.10  ? 219 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 30.773  -40.574 9.624   1.00 47.25  ? 220 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 13.161  -31.561 8.153   1.00 38.06  ? 221 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 21.455  -19.683 24.410  1.00 61.36  ? 222 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 25.901  -17.580 13.968  1.00 49.56  ? 223 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 20.378  -41.948 12.137  1.00 36.07  ? 224 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 23.893  -21.008 24.017  1.00 58.07  ? 225 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 30.700  -31.493 15.794  1.00 52.00  ? 226 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 23.196  -41.677 18.515  1.00 46.95  ? 227 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 25.859  -33.872 34.812  1.00 54.35  ? 228 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 16.179  -17.823 19.324  1.00 45.29  ? 229 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 22.656  -28.618 11.083  1.00 39.23  ? 230 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 14.613  -38.646 9.330   1.00 68.39  ? 231 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 26.309  -18.087 20.969  1.00 59.14  ? 232 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 33.397  -24.861 31.717  1.00 58.59  ? 233 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 23.860  -18.608 21.734  1.00 68.16  ? 234 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 22.483  -34.446 16.560  1.00 31.67  ? 235 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 19.626  -26.832 3.128   1.00 61.82  ? 236 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 7.201   -18.157 10.736  1.00 44.98  ? 237 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 20.982  -40.019 26.600  1.00 45.23  ? 238 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 25.619  -31.378 10.834  1.00 43.39  ? 239 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 21.282  -28.744 8.491   1.00 42.09  ? 240 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 29.907  -40.032 31.411  1.00 49.00  ? 241 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 9.591   -19.085 23.599  1.00 54.02  ? 242 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 31.460  -40.023 27.373  1.00 49.38  ? 243 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 15.030  -37.277 13.177  1.00 42.81  ? 244 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 20.197  -41.052 39.553  1.00 68.40  ? 245 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 25.878  -39.643 20.219  1.00 43.91  ? 246 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 8.292   -31.989 11.964  1.00 56.37  ? 247 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 30.572  -35.903 28.697  1.00 54.67  ? 248 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 10.134  -30.461 9.802   1.00 40.75  ? 249 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 16.607  -38.319 11.453  1.00 54.35  ? 250 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 11.767  -29.557 27.667  1.00 69.12  ? 251 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 31.344  -44.069 15.732  1.00 72.70  ? 252 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 2.936   -28.042 14.585  1.00 65.75  ? 253 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 29.744  -34.808 11.937  1.00 68.02  ? 254 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 29.133  -25.241 32.668  1.00 56.78  ? 255 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 30.563  -32.855 18.216  1.00 48.84  ? 256 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 7.331   -32.009 24.587  1.00 75.37  ? 257 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 21.106  -13.211 13.289  1.00 53.54  ? 258 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 32.482  -43.981 11.911  1.00 59.36  ? 259 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 5.449   -23.897 18.345  1.00 77.76  ? 260 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 26.130  -14.017 11.119  1.00 49.36  ? 261 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 12.976  -38.297 13.864  1.00 61.21  ? 262 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 17.567  -37.145 28.982  1.00 61.21  ? 263 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 31.109  -17.233 9.662   1.00 56.90  ? 264 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 14.524  -32.784 2.410   1.00 64.22  ? 265 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 29.434  -41.803 27.223  1.00 46.96  ? 266 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 12.307  -21.276 10.570  1.00 50.49  ? 267 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 22.064  -27.141 3.525   1.00 80.37  ? 268 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 13.970  -22.879 27.983  1.00 64.69  ? 269 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 22.992  -13.908 13.603  1.00 53.69  ? 270 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 24.171  -15.864 12.045  1.00 51.36  ? 271 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 37.167  -24.994 26.640  1.00 90.90  ? 272 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 32.048  -39.507 30.115  1.00 57.07  ? 273 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 17.506  -42.691 40.176  1.00 68.36  ? 274 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 28.537  -41.706 29.826  1.00 44.12  ? 275 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 28.732  -17.877 28.829  1.00 63.93  ? 276 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 24.937  -29.239 9.448   1.00 54.79  ? 277 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 33.848  -44.776 15.316  1.00 44.22  ? 278 HOH C O   1 
# 
