data_7HGF
# 
_entry.id   7HGF 
# 
_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   7HGF         pdb_00007hgf 10.2210/pdb7hgf/pdb 
WWPDB D_1001407441 ?            ?                   
# 
_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                        7HGF 
_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 '1-[(thiophen-3-yl)methyl]piperidin-4-ol'          197.297   1   ? ?    ? ? 
5 water       nat water                                              18.015    254 ? ?    ? ? 
# 
_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 '1-[(thiophen-3-yl)methyl]piperidin-4-ol' T0Y 
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  
T0Y non-polymer         . '1-[(thiophen-3-yl)methyl]piperidin-4-ol' ?                 'C10 H15 N O S'  197.297 
THR 'L-peptide linking' y THREONINE                                 ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                  ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                    ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 ?  ?   ?   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 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        T0Y 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   T0Y 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 T0Y 1   103 101 T0Y LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 202 HOH HOH A . 
M 5 HOH 3   203 344 HOH HOH A . 
M 5 HOH 4   204 84  HOH HOH A . 
M 5 HOH 5   205 304 HOH HOH A . 
M 5 HOH 6   206 351 HOH HOH A . 
M 5 HOH 7   207 95  HOH HOH A . 
M 5 HOH 8   208 66  HOH HOH A . 
M 5 HOH 9   209 139 HOH HOH A . 
M 5 HOH 10  210 55  HOH HOH A . 
M 5 HOH 11  211 91  HOH HOH A . 
M 5 HOH 12  212 86  HOH HOH A . 
M 5 HOH 13  213 26  HOH HOH A . 
M 5 HOH 14  214 87  HOH HOH A . 
M 5 HOH 15  215 37  HOH HOH A . 
M 5 HOH 16  216 167 HOH HOH A . 
M 5 HOH 17  217 345 HOH HOH A . 
M 5 HOH 18  218 293 HOH HOH A . 
M 5 HOH 19  219 278 HOH HOH A . 
M 5 HOH 20  220 71  HOH HOH A . 
M 5 HOH 21  221 85  HOH HOH A . 
M 5 HOH 22  222 335 HOH HOH A . 
M 5 HOH 23  223 28  HOH HOH A . 
M 5 HOH 24  224 260 HOH HOH A . 
M 5 HOH 25  225 12  HOH HOH A . 
M 5 HOH 26  226 259 HOH HOH A . 
M 5 HOH 27  227 97  HOH HOH A . 
M 5 HOH 28  228 111 HOH HOH A . 
M 5 HOH 29  229 288 HOH HOH A . 
M 5 HOH 30  230 34  HOH HOH A . 
M 5 HOH 31  231 333 HOH HOH A . 
M 5 HOH 32  232 41  HOH HOH A . 
M 5 HOH 33  233 8   HOH HOH A . 
M 5 HOH 34  234 267 HOH HOH A . 
M 5 HOH 35  235 7   HOH HOH A . 
M 5 HOH 36  236 23  HOH HOH A . 
M 5 HOH 37  237 289 HOH HOH A . 
M 5 HOH 38  238 203 HOH HOH A . 
M 5 HOH 39  239 78  HOH HOH A . 
M 5 HOH 40  240 32  HOH HOH A . 
M 5 HOH 41  241 1   HOH HOH A . 
M 5 HOH 42  242 60  HOH HOH A . 
M 5 HOH 43  243 58  HOH HOH A . 
M 5 HOH 44  244 21  HOH HOH A . 
M 5 HOH 45  245 188 HOH HOH A . 
M 5 HOH 46  246 274 HOH HOH A . 
M 5 HOH 47  247 340 HOH HOH A . 
M 5 HOH 48  248 99  HOH HOH A . 
M 5 HOH 49  249 199 HOH HOH A . 
M 5 HOH 50  250 93  HOH HOH A . 
M 5 HOH 51  251 2   HOH HOH A . 
M 5 HOH 52  252 152 HOH HOH A . 
M 5 HOH 53  253 290 HOH HOH A . 
M 5 HOH 54  254 77  HOH HOH A . 
M 5 HOH 55  255 27  HOH HOH A . 
M 5 HOH 56  256 218 HOH HOH A . 
M 5 HOH 57  257 292 HOH HOH A . 
M 5 HOH 58  258 109 HOH HOH A . 
M 5 HOH 59  259 297 HOH HOH A . 
M 5 HOH 60  260 300 HOH HOH A . 
M 5 HOH 61  261 190 HOH HOH A . 
M 5 HOH 62  262 20  HOH HOH A . 
M 5 HOH 63  263 38  HOH HOH A . 
M 5 HOH 64  264 14  HOH HOH A . 
M 5 HOH 65  265 179 HOH HOH A . 
M 5 HOH 66  266 287 HOH HOH A . 
M 5 HOH 67  267 18  HOH HOH A . 
M 5 HOH 68  268 164 HOH HOH A . 
M 5 HOH 69  269 47  HOH HOH A . 
M 5 HOH 70  270 42  HOH HOH A . 
M 5 HOH 71  271 222 HOH HOH A . 
M 5 HOH 72  272 165 HOH HOH A . 
M 5 HOH 73  273 145 HOH HOH A . 
M 5 HOH 74  274 115 HOH HOH A . 
M 5 HOH 75  275 143 HOH HOH A . 
M 5 HOH 76  276 208 HOH HOH A . 
M 5 HOH 77  277 64  HOH HOH A . 
M 5 HOH 78  278 131 HOH HOH A . 
M 5 HOH 79  279 296 HOH HOH A . 
M 5 HOH 80  280 73  HOH HOH A . 
M 5 HOH 81  281 211 HOH HOH A . 
M 5 HOH 82  282 19  HOH HOH A . 
M 5 HOH 83  283 116 HOH HOH A . 
M 5 HOH 84  284 16  HOH HOH A . 
M 5 HOH 85  285 94  HOH HOH A . 
M 5 HOH 86  286 9   HOH HOH A . 
M 5 HOH 87  287 113 HOH HOH A . 
M 5 HOH 88  288 327 HOH HOH A . 
M 5 HOH 89  289 281 HOH HOH A . 
M 5 HOH 90  290 301 HOH HOH A . 
M 5 HOH 91  291 63  HOH HOH A . 
M 5 HOH 92  292 318 HOH HOH A . 
M 5 HOH 93  293 31  HOH HOH A . 
M 5 HOH 94  294 146 HOH HOH A . 
M 5 HOH 95  295 22  HOH HOH A . 
M 5 HOH 96  296 210 HOH HOH A . 
M 5 HOH 97  297 83  HOH HOH A . 
M 5 HOH 98  298 205 HOH HOH A . 
M 5 HOH 99  299 185 HOH HOH A . 
M 5 HOH 100 300 336 HOH HOH A . 
M 5 HOH 101 301 219 HOH HOH A . 
M 5 HOH 102 302 35  HOH HOH A . 
M 5 HOH 103 303 283 HOH HOH A . 
M 5 HOH 104 304 352 HOH HOH A . 
M 5 HOH 105 305 57  HOH HOH A . 
M 5 HOH 106 306 75  HOH HOH A . 
M 5 HOH 107 307 156 HOH HOH A . 
M 5 HOH 108 308 125 HOH HOH A . 
M 5 HOH 109 309 332 HOH HOH A . 
N 5 HOH 1   201 346 HOH HOH B . 
N 5 HOH 2   202 272 HOH HOH B . 
N 5 HOH 3   203 17  HOH HOH B . 
N 5 HOH 4   204 242 HOH HOH B . 
N 5 HOH 5   205 69  HOH HOH B . 
N 5 HOH 6   206 331 HOH HOH B . 
N 5 HOH 7   207 89  HOH HOH B . 
N 5 HOH 8   208 223 HOH HOH B . 
N 5 HOH 9   209 258 HOH HOH B . 
N 5 HOH 10  210 168 HOH HOH B . 
N 5 HOH 11  211 59  HOH HOH B . 
N 5 HOH 12  212 247 HOH HOH B . 
N 5 HOH 13  213 249 HOH HOH B . 
N 5 HOH 14  214 177 HOH HOH B . 
N 5 HOH 15  215 334 HOH HOH B . 
N 5 HOH 16  216 315 HOH HOH B . 
N 5 HOH 17  217 215 HOH HOH B . 
N 5 HOH 18  218 280 HOH HOH B . 
N 5 HOH 19  219 172 HOH HOH B . 
N 5 HOH 20  220 68  HOH HOH B . 
N 5 HOH 21  221 137 HOH HOH B . 
N 5 HOH 22  222 123 HOH HOH B . 
N 5 HOH 23  223 98  HOH HOH B . 
N 5 HOH 24  224 150 HOH HOH B . 
N 5 HOH 25  225 320 HOH HOH B . 
N 5 HOH 26  226 5   HOH HOH B . 
N 5 HOH 27  227 6   HOH HOH B . 
N 5 HOH 28  228 347 HOH HOH B . 
N 5 HOH 29  229 10  HOH HOH B . 
N 5 HOH 30  230 117 HOH HOH B . 
N 5 HOH 31  231 24  HOH HOH B . 
N 5 HOH 32  232 224 HOH HOH B . 
N 5 HOH 33  233 153 HOH HOH B . 
N 5 HOH 34  234 25  HOH HOH B . 
N 5 HOH 35  235 349 HOH HOH B . 
N 5 HOH 36  236 119 HOH HOH B . 
N 5 HOH 37  237 329 HOH HOH B . 
N 5 HOH 38  238 170 HOH HOH B . 
N 5 HOH 39  239 261 HOH HOH B . 
N 5 HOH 40  240 54  HOH HOH B . 
N 5 HOH 41  241 169 HOH HOH B . 
N 5 HOH 42  242 175 HOH HOH B . 
N 5 HOH 43  243 279 HOH HOH B . 
N 5 HOH 44  244 96  HOH HOH B . 
N 5 HOH 45  245 13  HOH HOH B . 
N 5 HOH 46  246 61  HOH HOH B . 
N 5 HOH 47  247 74  HOH HOH B . 
N 5 HOH 48  248 76  HOH HOH B . 
N 5 HOH 49  249 101 HOH HOH B . 
N 5 HOH 50  250 120 HOH HOH B . 
N 5 HOH 51  251 79  HOH HOH B . 
N 5 HOH 52  252 157 HOH HOH B . 
N 5 HOH 53  253 46  HOH HOH B . 
N 5 HOH 54  254 217 HOH HOH B . 
N 5 HOH 55  255 72  HOH HOH B . 
N 5 HOH 56  256 44  HOH HOH B . 
N 5 HOH 57  257 197 HOH HOH B . 
N 5 HOH 58  258 104 HOH HOH B . 
N 5 HOH 59  259 36  HOH HOH B . 
N 5 HOH 60  260 214 HOH HOH B . 
N 5 HOH 61  261 303 HOH HOH B . 
N 5 HOH 62  262 322 HOH HOH B . 
N 5 HOH 63  263 182 HOH HOH B . 
N 5 HOH 64  264 350 HOH HOH B . 
N 5 HOH 65  265 291 HOH HOH B . 
N 5 HOH 66  266 201 HOH HOH B . 
N 5 HOH 67  267 163 HOH HOH B . 
N 5 HOH 68  268 348 HOH HOH B . 
N 5 HOH 69  269 160 HOH HOH B . 
N 5 HOH 70  270 343 HOH HOH B . 
N 5 HOH 71  271 314 HOH HOH B . 
N 5 HOH 72  272 316 HOH HOH B . 
N 5 HOH 73  273 103 HOH HOH B . 
N 5 HOH 74  274 107 HOH HOH B . 
N 5 HOH 75  275 312 HOH HOH B . 
O 5 HOH 1   201 254 HOH HOH C . 
O 5 HOH 2   202 321 HOH HOH C . 
O 5 HOH 3   203 337 HOH HOH C . 
O 5 HOH 4   204 325 HOH HOH C . 
O 5 HOH 5   205 302 HOH HOH C . 
O 5 HOH 6   206 271 HOH HOH C . 
O 5 HOH 7   207 90  HOH HOH C . 
O 5 HOH 8   208 184 HOH HOH C . 
O 5 HOH 9   209 142 HOH HOH C . 
O 5 HOH 10  210 309 HOH HOH C . 
O 5 HOH 11  211 118 HOH HOH C . 
O 5 HOH 12  212 173 HOH HOH C . 
O 5 HOH 13  213 132 HOH HOH C . 
O 5 HOH 14  214 323 HOH HOH C . 
O 5 HOH 15  215 15  HOH HOH C . 
O 5 HOH 16  216 226 HOH HOH C . 
O 5 HOH 17  217 294 HOH HOH C . 
O 5 HOH 18  218 326 HOH HOH C . 
O 5 HOH 19  219 49  HOH HOH C . 
O 5 HOH 20  220 275 HOH HOH C . 
O 5 HOH 21  221 53  HOH HOH C . 
O 5 HOH 22  222 189 HOH HOH C . 
O 5 HOH 23  223 284 HOH HOH C . 
O 5 HOH 24  224 269 HOH HOH C . 
O 5 HOH 25  225 45  HOH HOH C . 
O 5 HOH 26  226 43  HOH HOH C . 
O 5 HOH 27  227 161 HOH HOH C . 
O 5 HOH 28  228 317 HOH HOH C . 
O 5 HOH 29  229 82  HOH HOH C . 
O 5 HOH 30  230 134 HOH HOH C . 
O 5 HOH 31  231 126 HOH HOH C . 
O 5 HOH 32  232 122 HOH HOH C . 
O 5 HOH 33  233 4   HOH HOH C . 
O 5 HOH 34  234 102 HOH HOH C . 
O 5 HOH 35  235 56  HOH HOH C . 
O 5 HOH 36  236 198 HOH HOH C . 
O 5 HOH 37  237 298 HOH HOH C . 
O 5 HOH 38  238 40  HOH HOH C . 
O 5 HOH 39  239 148 HOH HOH C . 
O 5 HOH 40  240 209 HOH HOH C . 
O 5 HOH 41  241 48  HOH HOH C . 
O 5 HOH 42  242 130 HOH HOH C . 
O 5 HOH 43  243 62  HOH HOH C . 
O 5 HOH 44  244 67  HOH HOH C . 
O 5 HOH 45  245 135 HOH HOH C . 
O 5 HOH 46  246 299 HOH HOH C . 
O 5 HOH 47  247 151 HOH HOH C . 
O 5 HOH 48  248 171 HOH HOH C . 
O 5 HOH 49  249 328 HOH HOH C . 
O 5 HOH 50  250 319 HOH HOH C . 
O 5 HOH 51  251 305 HOH HOH C . 
O 5 HOH 52  252 65  HOH HOH C . 
O 5 HOH 53  253 149 HOH HOH C . 
O 5 HOH 54  254 338 HOH HOH C . 
O 5 HOH 55  255 330 HOH HOH C . 
O 5 HOH 56  256 270 HOH HOH C . 
O 5 HOH 57  257 241 HOH HOH C . 
O 5 HOH 58  258 324 HOH HOH C . 
O 5 HOH 59  259 70  HOH HOH C . 
O 5 HOH 60  260 339 HOH HOH C . 
O 5 HOH 61  261 108 HOH HOH C . 
O 5 HOH 62  262 342 HOH HOH C . 
O 5 HOH 63  263 353 HOH HOH C . 
O 5 HOH 64  264 310 HOH HOH C . 
O 5 HOH 65  265 341 HOH HOH C . 
O 5 HOH 66  266 246 HOH HOH C . 
O 5 HOH 67  267 295 HOH HOH C . 
O 5 HOH 68  268 313 HOH HOH C . 
O 5 HOH 69  269 92  HOH HOH C . 
O 5 HOH 70  270 206 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
19 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
20 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
21 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
22 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
23 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
24 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
25 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
26 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
27 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
28 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
29 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
30 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
31 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
32 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
33 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
34 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
35 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
36 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
37 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
38 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
39 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
40 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
41 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
42 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
43 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
44 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
45 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
46 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
47 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
48 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
49 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
50 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
51 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
52 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
53 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
54 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
55 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
56 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
57 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
58 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
59 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
60 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
61 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' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGF 
_cell.length_a           41.740 
_cell.length_b           42.330 
_cell.length_c           159.880 
_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                         7HGF 
_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          7HGF 
_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                     7HGF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.94 
_reflns.d_resolution_high            1.55 
_reflns.number_obs                   42240 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.057 
_reflns.pdbx_netI_over_sigmaI        12.8 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.062 
_reflns.pdbx_Rpim_I_all              0.025 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     260045 
_reflns.pdbx_chi_squared             0.96 
_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                  1.55 
_reflns_shell.d_res_low                   1.59 
_reflns_shell.number_measured_all         15511 
_reflns_shell.number_unique_obs           3058 
_reflns_shell.Rmerge_I_obs                1.643 
_reflns_shell.pdbx_chi_squared            0.78 
_reflns_shell.pdbx_redundancy             5.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.835 
_reflns_shell.pdbx_Rpim_I_all             0.810 
_reflns_shell.pdbx_CC_half                0.353 
_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                                 7HGF 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     39925 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             79.94 
_refine.ls_d_res_high                            1.55 
_refine.ls_percent_reflns_obs                    99.95 
_refine.ls_R_factor_obs                          0.20580 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20374 
_refine.ls_R_factor_R_free                       0.24232 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2238 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.957 
_refine.B_iso_mean                               36.425 
_refine.aniso_B[1][1]                            0.59 
_refine.aniso_B[2][2]                            -0.36 
_refine.aniso_B[3][3]                            -0.23 
_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                       0.092 
_refine.pdbx_overall_ESU_R_Free                  0.095 
_refine.overall_SU_ML                            0.082 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.410 
_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        2127 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             254 
_refine_hist.number_atoms_total               2432 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        79.94 
# 
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             0.010  0.012  ? 2281 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.868  1.834  ? 3103 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.100  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.431  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.708 10.000 ? 300  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.131  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1886 '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                  3.304  3.389  ? 1070 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.532  6.063  ? 1331 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.526  3.702  ? 1211 '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       8.430  46.96  ? 3457 '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                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_R_work             2870 
_refine_ls_shell.R_factor_R_work                  0.334 
_refine_ls_shell.percent_reflns_obs               99.90 
_refine_ls_shell.R_factor_R_free                  0.325 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             180 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGF 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1262433643' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGF 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGF A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGF B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGF 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 7HGF GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGF SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGF GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGF SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGF GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGF SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGF 
_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 218 ? ? O B HOH 262 ? ? 1.45 
2  1 N   B LYS 6   ? ? O B HOH 201 ? ? 1.59 
3  1 OD2 B ASP 9   ? ? O B HOH 201 ? ? 1.59 
4  1 O   C HOH 203 ? ? O C HOH 256 ? ? 1.98 
5  1 O   A HOH 245 ? ? O A HOH 298 ? ? 2.02 
6  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 2.04 
7  1 O   A HOH 217 ? ? O A HOH 295 ? ? 2.06 
8  1 O   A HOH 245 ? ? O A HOH 304 ? ? 2.12 
9  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.15 
10 1 O4  A SO4 104 ? ? O A HOH 202 ? ? 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 257 ? ? 1_555 O A HOH 271 ? ? 4_545 1.99 
2 1 O A HOH 294 ? ? 1_555 O C HOH 258 ? ? 4_445 2.14 
# 
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 ? ? -152.06 65.96 
2 1 ASN B 87 ? ? -159.80 63.74 
3 1 ASN C 87 ? ? -147.65 51.33 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 B VAL 33 ? B VAL 34 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 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 
T0Y C13  C N N 319 
T0Y C02  C N N 320 
T0Y C03  C N N 321 
T0Y C04  C N N 322 
T0Y C06  C N N 323 
T0Y C07  C Y N 324 
T0Y C08  C Y N 325 
T0Y C09  C Y N 326 
T0Y C11  C Y N 327 
T0Y C12  C N N 328 
T0Y N05  N N N 329 
T0Y O01  O N N 330 
T0Y S10  S Y N 331 
T0Y H131 H N N 332 
T0Y H132 H N N 333 
T0Y H021 H N N 334 
T0Y H031 H N N 335 
T0Y H032 H N N 336 
T0Y H041 H N N 337 
T0Y H042 H N N 338 
T0Y H061 H N N 339 
T0Y H062 H N N 340 
T0Y H081 H N N 341 
T0Y H091 H N N 342 
T0Y H111 H N N 343 
T0Y H121 H N N 344 
T0Y H122 H N N 345 
T0Y H011 H N N 346 
THR N    N N N 347 
THR CA   C N S 348 
THR C    C N N 349 
THR O    O N N 350 
THR CB   C N R 351 
THR OG1  O N N 352 
THR CG2  C N N 353 
THR OXT  O N N 354 
THR H    H N N 355 
THR H2   H N N 356 
THR HA   H N N 357 
THR HB   H N N 358 
THR HG1  H N N 359 
THR HG21 H N N 360 
THR HG22 H N N 361 
THR HG23 H N N 362 
THR HXT  H N N 363 
TRP N    N N N 364 
TRP CA   C N S 365 
TRP C    C N N 366 
TRP O    O N N 367 
TRP CB   C N N 368 
TRP CG   C Y N 369 
TRP CD1  C Y N 370 
TRP CD2  C Y N 371 
TRP NE1  N Y N 372 
TRP CE2  C Y N 373 
TRP CE3  C Y N 374 
TRP CZ2  C Y N 375 
TRP CZ3  C Y N 376 
TRP CH2  C Y N 377 
TRP OXT  O N N 378 
TRP H    H N N 379 
TRP H2   H N N 380 
TRP HA   H N N 381 
TRP HB2  H N N 382 
TRP HB3  H N N 383 
TRP HD1  H N N 384 
TRP HE1  H N N 385 
TRP HE3  H N N 386 
TRP HZ2  H N N 387 
TRP HZ3  H N N 388 
TRP HH2  H N N 389 
TRP HXT  H N N 390 
TYR N    N N N 391 
TYR CA   C N S 392 
TYR C    C N N 393 
TYR O    O N N 394 
TYR CB   C N N 395 
TYR CG   C Y N 396 
TYR CD1  C Y N 397 
TYR CD2  C Y N 398 
TYR CE1  C Y N 399 
TYR CE2  C Y N 400 
TYR CZ   C Y N 401 
TYR OH   O N N 402 
TYR OXT  O N N 403 
TYR H    H N N 404 
TYR H2   H N N 405 
TYR HA   H N N 406 
TYR HB2  H N N 407 
TYR HB3  H N N 408 
TYR HD1  H N N 409 
TYR HD2  H N N 410 
TYR HE1  H N N 411 
TYR HE2  H N N 412 
TYR HH   H N N 413 
TYR HXT  H N N 414 
VAL N    N N N 415 
VAL CA   C N S 416 
VAL C    C N N 417 
VAL O    O N N 418 
VAL CB   C N N 419 
VAL CG1  C N N 420 
VAL CG2  C N N 421 
VAL OXT  O N N 422 
VAL H    H N N 423 
VAL H2   H N N 424 
VAL HA   H N N 425 
VAL HB   H N N 426 
VAL HG11 H N N 427 
VAL HG12 H N N 428 
VAL HG13 H N N 429 
VAL HG21 H N N 430 
VAL HG22 H N N 431 
VAL HG23 H N N 432 
VAL HXT  H N N 433 
# 
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 
T0Y C02 O01  sing N N 303 
T0Y C03 C02  sing N N 304 
T0Y C04 C03  sing N N 305 
T0Y N05 C04  sing N N 306 
T0Y C07 C06  sing N N 307 
T0Y C08 C07  sing Y N 308 
T0Y C09 C08  doub Y N 309 
T0Y S10 C09  sing Y N 310 
T0Y C11 S10  sing Y N 311 
T0Y C06 N05  sing N N 312 
T0Y C12 N05  sing N N 313 
T0Y C13 C12  sing N N 314 
T0Y C02 C13  sing N N 315 
T0Y C07 C11  doub Y N 316 
T0Y C13 H131 sing N N 317 
T0Y C13 H132 sing N N 318 
T0Y C02 H021 sing N N 319 
T0Y C03 H031 sing N N 320 
T0Y C03 H032 sing N N 321 
T0Y C04 H041 sing N N 322 
T0Y C04 H042 sing N N 323 
T0Y C06 H061 sing N N 324 
T0Y C06 H062 sing N N 325 
T0Y C08 H081 sing N N 326 
T0Y C09 H091 sing N N 327 
T0Y C11 H111 sing N N 328 
T0Y C12 H121 sing N N 329 
T0Y C12 H122 sing N N 330 
T0Y O01 H011 sing N N 331 
THR N   CA   sing N N 332 
THR N   H    sing N N 333 
THR N   H2   sing N N 334 
THR CA  C    sing N N 335 
THR CA  CB   sing N N 336 
THR CA  HA   sing N N 337 
THR C   O    doub N N 338 
THR C   OXT  sing N N 339 
THR CB  OG1  sing N N 340 
THR CB  CG2  sing N N 341 
THR CB  HB   sing N N 342 
THR OG1 HG1  sing N N 343 
THR CG2 HG21 sing N N 344 
THR CG2 HG22 sing N N 345 
THR CG2 HG23 sing N N 346 
THR OXT HXT  sing N N 347 
TRP N   CA   sing N N 348 
TRP N   H    sing N N 349 
TRP N   H2   sing N N 350 
TRP CA  C    sing N N 351 
TRP CA  CB   sing N N 352 
TRP CA  HA   sing N N 353 
TRP C   O    doub N N 354 
TRP C   OXT  sing N N 355 
TRP CB  CG   sing N N 356 
TRP CB  HB2  sing N N 357 
TRP CB  HB3  sing N N 358 
TRP CG  CD1  doub Y N 359 
TRP CG  CD2  sing Y N 360 
TRP CD1 NE1  sing Y N 361 
TRP CD1 HD1  sing N N 362 
TRP CD2 CE2  doub Y N 363 
TRP CD2 CE3  sing Y N 364 
TRP NE1 CE2  sing Y N 365 
TRP NE1 HE1  sing N N 366 
TRP CE2 CZ2  sing Y N 367 
TRP CE3 CZ3  doub Y N 368 
TRP CE3 HE3  sing N N 369 
TRP CZ2 CH2  doub Y N 370 
TRP CZ2 HZ2  sing N N 371 
TRP CZ3 CH2  sing Y N 372 
TRP CZ3 HZ3  sing N N 373 
TRP CH2 HH2  sing N N 374 
TRP OXT HXT  sing N N 375 
TYR N   CA   sing N N 376 
TYR N   H    sing N N 377 
TYR N   H2   sing N N 378 
TYR CA  C    sing N N 379 
TYR CA  CB   sing N N 380 
TYR CA  HA   sing N N 381 
TYR C   O    doub N N 382 
TYR C   OXT  sing N N 383 
TYR CB  CG   sing N N 384 
TYR CB  HB2  sing N N 385 
TYR CB  HB3  sing N N 386 
TYR CG  CD1  doub Y N 387 
TYR CG  CD2  sing Y N 388 
TYR CD1 CE1  sing Y N 389 
TYR CD1 HD1  sing N N 390 
TYR CD2 CE2  doub Y N 391 
TYR CD2 HD2  sing N N 392 
TYR CE1 CZ   doub Y N 393 
TYR CE1 HE1  sing N N 394 
TYR CE2 CZ   sing Y N 395 
TYR CE2 HE2  sing N N 396 
TYR CZ  OH   sing N N 397 
TYR OH  HH   sing N N 398 
TYR OXT HXT  sing N N 399 
VAL N   CA   sing N N 400 
VAL N   H    sing N N 401 
VAL N   H2   sing N N 402 
VAL CA  C    sing N N 403 
VAL CA  CB   sing N N 404 
VAL CA  HA   sing N N 405 
VAL C   O    doub N N 406 
VAL C   OXT  sing N N 407 
VAL CB  CG1  sing N N 408 
VAL CB  CG2  sing N N 409 
VAL CB  HB   sing N N 410 
VAL CG1 HG11 sing N N 411 
VAL CG1 HG12 sing N N 412 
VAL CG1 HG13 sing N N 413 
VAL CG2 HG21 sing N N 414 
VAL CG2 HG22 sing N N 415 
VAL CG2 HG23 sing N N 416 
VAL OXT HXT  sing N N 417 
# 
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                    7HGF 
_atom_sites.fract_transf_matrix[1][1]   0.023958 
_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]   0.023624 
_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]   0.006255 
_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  ? 1.151   4.265   2.462   1.00 53.40  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? 0.054   3.510   1.799   1.00 53.52  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.645   2.471   0.843   1.00 49.28  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.732   2.659   0.303   1.00 47.63  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -0.922  4.443   1.067   1.00 56.56  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -1.951  5.141   1.961   1.00 72.58  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.325  4.219   2.701   1.00 74.02  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.954  5.479   3.821   1.00 73.79  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.041  1.322   0.637   1.00 42.01  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.457   0.235   -0.215  1.00 41.06  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.602   0.538   -1.707  1.00 37.64  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.132  1.326   -2.293  1.00 40.23  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -0.638  -0.860  0.035   1.00 39.26  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.215  -0.508  1.411   1.00 40.54  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.342  0.996   1.259   1.00 43.03  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.561   -0.135  -2.337  1.00 36.05  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.723   -0.017  -3.772  1.00 34.94  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 1.206   -1.321  -4.373  1.00 29.31  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.774   -2.211  -3.632  1.00 32.44  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.212   0.204   -4.099  1.00 46.36  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.782   1.506   -3.604  1.00 56.80  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 4.698   2.244   -4.327  1.00 68.11  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 3.555   2.219   -2.486  1.00 62.03  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 5.002   3.358   -3.665  1.00 61.01  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.310   3.364   -2.547  1.00 64.09  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.213   -1.441  -5.700  1.00 27.36  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 1.011   -2.746  -6.316  1.00 27.46  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 2.154   -3.681  -5.951  1.00 26.87  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.238   -3.224  -5.553  1.00 28.55  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.895   -2.618  -7.825  1.00 33.51  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.864   -4.973  -6.070  1.00 25.66  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.862   -6.036  -5.942  1.00 25.25  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 4.012   -5.809  -6.933  1.00 27.17  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.783   -5.407  -8.079  1.00 28.16  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.322   -7.474  -5.998  1.00 25.52  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.536   -7.823  -4.732  1.00 25.44  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 2.184   -8.039  -3.516  1.00 23.88  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? 0.149   -7.964  -4.771  1.00 26.24  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.520   -8.333  -2.336  1.00 24.59  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.523  -8.329  -3.586  1.00 22.87  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? 0.142   -8.471  -2.390  1.00 25.87  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 5.241   -6.112  -6.466  1.00 23.45  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.420   -6.016  -7.333  1.00 24.37  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.341   -7.203  -7.035  1.00 24.33  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.293   -7.792  -5.960  1.00 23.15  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 7.131   -4.684  -7.052  1.00 26.73  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.705   -4.582  -5.679  1.00 30.31  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.480   -3.274  -5.423  1.00 37.79  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 9.093   -3.256  -4.027  1.00 35.17  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 8.122   -3.158  -2.916  1.00 36.06  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 8.222   -7.605  -7.973  1.00 23.56  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 9.176   -8.679  -7.701  1.00 22.43  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.951   -8.399  -6.423  1.00 21.14  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.416  -7.274  -6.184  1.00 24.22  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 10.095  -8.560  -8.979  1.00 25.28  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 9.114   -8.113  -10.048 1.00 27.37  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.365   -7.017  -9.332  1.00 25.85  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 10.152  -9.470  -5.645  1.00 21.52  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.837  -9.380  -4.376  1.00 22.37  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.903   -9.273  -3.177  1.00 22.23  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.290  -9.540  -2.041  1.00 21.88  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.661   -8.844  -3.422  1.00 19.53  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.740   -8.795  -2.292  1.00 18.52  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.506   -10.176 -1.665  1.00 19.16  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.368   -11.166 -2.376  1.00 19.37  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.416   -8.199  -2.754  1.00 19.35  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.396   -6.694  -2.903  1.00 23.56  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.361   -6.010  -2.453  1.00 25.79  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.401   -6.189  -3.512  1.00 23.77  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.394   -10.194 -0.331  1.00 19.79  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 7.205   -11.433 0.421   1.00 17.21  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.736   -11.546 0.830   1.00 18.69  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 5.143   -10.549 1.278   1.00 21.45  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 8.151   -11.458 1.644   1.00 19.26  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.634   -11.293 1.248   1.00 20.25  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.487  -11.404 2.546   1.00 23.19  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 10.107  -12.301 0.218   1.00 22.03  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 5.218   -12.782 0.703   1.00 18.70  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.772   -12.990 0.911   1.00 20.46  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.510   -14.352 1.535   1.00 20.42  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.371   -15.214 1.589   1.00 20.38  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.945   -12.876 -0.379  1.00 18.68  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 3.079   -11.505 -1.016  1.00 20.85  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.365   -13.919 -1.424  1.00 21.26  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.270   -14.539 2.038   1.00 19.15  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.707   -15.873 2.062   1.00 21.19  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.739   -15.957 0.888   1.00 23.01  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.054  -15.029 0.707   1.00 21.52  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.944   -16.271 3.354   1.00 21.23  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.891   -16.338 4.545   1.00 21.43  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 2.203   -15.169 5.225   1.00 23.55  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.444   -17.548 4.960   1.00 24.32  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 3.115   -15.207 6.294   1.00 28.20  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.375   -17.591 6.015   1.00 23.13  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.646   -16.431 6.695   1.00 27.37  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.833   -17.052 0.116   1.00 21.05  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? 0.061   -17.189 -1.113  1.00 20.53  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -0.918  -18.351 -0.891  1.00 23.41  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.525  -19.409 -0.382  1.00 22.51  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.956   -17.424 -2.323  1.00 20.97  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.198  -18.142 -1.264  1.00 23.17  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.215  -19.181 -1.065  1.00 23.66  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.547  -19.891 -2.380  1.00 25.02  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -3.905  -19.261 -3.359  1.00 27.95  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.444  -18.480 -0.433  1.00 23.76  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.576  -19.511 -0.048  1.00 29.78  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.093  -20.448 1.065   1.00 30.22  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.159  -21.281 1.772   1.00 31.69  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.530  -22.403 0.909   1.00 32.80  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.508  -21.241 -2.331  1.00 25.81  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -3.953  -22.122 -3.403  1.00 28.92  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.056  -22.992 -2.785  1.00 32.80  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -4.992  -23.311 -1.611  1.00 28.35  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -2.815  -23.090 -3.757  1.00 31.57  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.485  -22.444 -4.154  1.00 34.77  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.576  -21.799 -5.839  1.00 36.98  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.188  -23.322 -6.652  1.00 31.71  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.014  -23.430 -3.601  1.00 37.78  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.061  -24.359 -3.177  1.00 40.96  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.453  -25.618 -2.571  1.00 35.52  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.530  -26.207 -3.135  1.00 35.85  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -7.746  -24.790 -4.479  1.00 45.93  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.024  -25.606 -4.303  1.00 48.34  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.251 -24.696 -4.301  1.00 59.92  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -6.953  -26.019 -1.391  1.00 37.53  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.532  -27.267 -0.787  1.00 36.14  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.189  -27.158 -0.080  1.00 40.21  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -4.651  -28.146 0.407   1.00 42.31  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.625  -25.946 -0.026  1.00 35.87  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.357  -25.822 0.664   1.00 33.04  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.465  -24.711 1.692   1.00 29.78  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.206  -23.762 1.484   1.00 29.01  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.247  -25.398 -0.300  1.00 36.36  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -1.782  -26.433 -1.316  1.00 40.98  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -0.716  -27.275 -1.027  1.00 53.61  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.383  -26.543 -2.570  1.00 45.66  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.275  -28.215 -1.948  1.00 52.90  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -1.941  -27.473 -3.508  1.00 45.31  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -0.880  -28.305 -3.191  1.00 52.54  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.427  -29.241 -4.087  1.00 63.70  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -2.709  -24.771 2.808   1.00 29.35  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.636  -23.666 3.771   1.00 27.60  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -1.944  -22.469 3.105   1.00 26.43  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.183  -22.677 2.183   1.00 28.05  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -1.789  -24.231 4.931   1.00 32.91  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -0.956  -25.321 4.276   1.00 32.84  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -1.839  -25.907 3.178   1.00 34.44  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.250  -21.270 3.571   1.00 24.94  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.528  -20.051 3.188   1.00 23.54  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.023  -20.314 3.292   1.00 25.59  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.447   -20.735 4.340   1.00 25.45  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -1.999  -18.874 4.060   1.00 26.27  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.437  -18.437 3.847   1.00 25.52  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.474  -19.124 4.468   1.00 30.26  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.004  -17.453 3.121   1.00 27.88  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.630  -18.547 4.137   1.00 32.49  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.392  -17.513 3.359   1.00 30.55  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.723   -20.078 2.175   1.00 23.03  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 2.038   -20.696 2.047   1.00 23.19  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 3.101   -19.600 1.895   1.00 22.08  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.938   -18.706 1.070   1.00 21.97  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 2.044   -21.601 0.812   1.00 24.10  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 3.162   -22.601 0.859   1.00 24.47  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.505   -22.406 0.637   1.00 23.82  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.990   -23.997 1.170   1.00 27.35  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 5.164   -23.622 0.740   1.00 23.93  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 4.270   -24.594 1.095   1.00 25.12  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.887   -24.797 1.515   1.00 33.08  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.473   -25.961 1.344   1.00 35.01  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 2.097   -26.143 1.778   1.00 34.43  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 3.374   -26.719 1.684   1.00 34.55  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 4.257   -19.668 2.610   1.00 21.21  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 5.328   -18.677 2.418   1.00 20.96  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.858   -18.632 0.977   1.00 18.81  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 6.175   -19.671 0.371   1.00 20.19  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.407   -19.136 3.443   1.00 19.73  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 6.187   -20.628 3.594   1.00 19.82  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.646   -20.745 3.542   1.00 22.20  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.881   -17.422 0.404   1.00 18.03  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 6.252   -17.292 -1.004  1.00 18.21  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.763   -15.887 -1.317  1.00 18.27  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.725   -14.995 -0.496  1.00 19.76  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.998   -17.615 -1.857  1.00 19.75  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 7.250   -15.704 -2.552  1.00 18.15  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.659   -14.379 -2.994  1.00 18.95  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 7.134   -14.123 -4.403  1.00 19.07  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.873   -15.067 -5.148  1.00 20.64  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 9.191   -14.241 -2.948  1.00 19.97  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.888   -15.097 -3.999  1.00 21.85  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.438  -14.968 -3.818  1.00 20.56  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 12.124  -15.753 -4.870  1.00 20.88  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.391  -16.147 -4.771  1.00 24.52  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 14.074  -16.020 -3.622  1.00 23.71  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.926  -16.764 -5.826  1.00 26.62  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.994   -12.850 -4.738  1.00 19.46  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.771   -12.465 -6.133  1.00 19.22  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 8.089   -12.590 -6.861  1.00 24.29  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 9.058   -11.964 -6.463  1.00 22.43  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 6.265   -11.012 -6.206  1.00 21.05  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 5.086   -10.760 -5.231  1.00 26.08  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.906   -10.591 -7.653  1.00 21.18  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.775   -11.396 -5.621  1.00 31.10  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 8.116   -13.434 -7.877  1.00 23.03  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.347   -13.612 -8.651  1.00 23.45  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.476   -12.603 -9.791  1.00 25.58  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.540   -11.941 -10.237 1.00 25.45  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.441   -15.009 -9.232  1.00 24.61  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.463  -15.934 -8.593  1.00 27.58  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 11.103  -15.515 -7.608  1.00 31.54  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.624  -17.044 -9.078  1.00 27.56  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.731  -12.433 -10.265 1.00 28.95  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.958  -11.774 -11.540 1.00 33.89  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.649  -12.774 -12.665 1.00 30.89  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.503  -13.973 -12.437 1.00 33.13  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.423  -11.351 -11.673 1.00 38.25  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.847  -10.059 -10.974 1.00 44.08  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.418  -8.963  -11.412 1.00 49.46  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.610  -10.152 -9.990  1.00 52.09  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.586  -12.276 -13.896 1.00 34.82  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.554  -13.162 -15.061 1.00 31.02  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.863  -12.886 -15.808 1.00 28.22  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 12.140  -11.722 -16.080 1.00 31.76  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.343   -12.744 -15.907 1.00 35.92  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 8.048   -12.919 -15.097 1.00 36.66  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.294   -13.499 -17.230 1.00 31.24  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.959   -11.990 -15.576 1.00 36.86  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.661  -13.949 -15.994 1.00 31.85  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.928  -13.891 -16.718 1.00 31.73  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.664  -13.521 -18.183 1.00 31.31  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.609  -13.821 -18.750 1.00 31.25  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.632  -15.237 -16.600 1.00 33.68  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.601  -12.784 -18.797 1.00 29.17  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.541  -12.657 -20.255 1.00 29.81  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.437  -14.043 -20.886 1.00 26.60  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 15.111  -14.955 -20.466 1.00 30.88  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.789  -11.918 -20.734 1.00 32.21  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.824  -10.422 -20.491 1.00 40.03  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.740  -9.830  -20.349 1.00 46.66  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.951  -9.874  -20.452 1.00 45.73  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.523  -14.178 -21.859 1.00 29.08  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.291  -15.385 -22.628 1.00 30.78  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.423  -16.421 -21.916 1.00 33.49  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 12.192  -17.493 -22.459 1.00 35.39  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.965  -16.104 -20.698 1.00 31.48  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 11.137  -17.047 -19.957 1.00 33.42  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.650   -16.800 -20.221 1.00 30.14  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.212   -15.706 -20.602 1.00 31.64  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.454  -16.937 -18.464 1.00 32.27  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.865   -17.869 -19.950 1.00 31.81  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.413   -17.805 -20.075 1.00 34.23  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.833   -16.780 -19.103 1.00 32.59  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 7.131   -16.817 -17.915 1.00 33.57  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.841   -19.198 -19.754 1.00 35.97  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.323   -19.125 -19.677 1.00 37.16  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.301   -20.229 -20.788 1.00 34.92  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.995   -15.898 -19.641 1.00 34.15  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.360   -14.824 -18.890 1.00 35.62  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 4.067   -15.355 -18.281 1.00 39.23  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.534   -16.357 -18.744 1.00 37.09  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.995   -13.669 -19.819 1.00 37.77  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.188   -12.863 -20.322 1.00 42.50  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.871   -11.641 -21.178 1.00 48.24  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.280   -12.075 -22.482 1.00 49.45  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.324   -10.994 -23.465 1.00 48.17  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.533   -14.729 -17.213 1.00 40.88  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.279   -15.201 -16.617 1.00 37.35  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 1.125   -14.694 -17.475 1.00 35.93  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.273   -13.746 -18.229 1.00 37.10  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 2.230   -14.533 -15.229 1.00 35.07  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.108   -13.298 -15.369 1.00 43.18  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 4.024   -13.486 -16.597 1.00 41.35  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.094  -15.237 -17.291 1.00 39.02  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.289  -14.608 -17.854 1.00 40.98  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.449  -13.158 -17.421 1.00 40.92  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -0.977  -12.775 -16.353 1.00 33.34  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.443  -15.442 -17.287 1.00 40.16  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -1.833  -16.761 -16.878 1.00 37.79  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.371  -16.483 -16.562 1.00 37.83  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.196  -12.314 -18.178 1.00 38.79  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.605  -10.992 -17.697 1.00 40.17  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.226  -10.992 -16.301 1.00 36.78  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -3.924  -11.928 -15.930 1.00 40.07  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.580  -10.482 -18.792 1.00 46.36  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -3.912  -11.719 -19.568 1.00 40.95  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -2.673  -12.584 -19.557 1.00 46.25  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -2.867  -9.958  -15.529 1.00 37.67  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.317  -9.709  -14.177 1.00 39.10  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -2.838  -10.781 -13.196 1.00 32.77  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.334  -10.781 -12.071 1.00 33.85  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -4.839  -9.629  -14.115 1.00 47.71  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.324  -8.427  -14.890 1.00 53.00  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.121  -7.282  -14.460 1.00 49.68  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -5.922  -8.676  -16.040 1.00 54.65  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -1.913  -11.686 -13.610 1.00 30.26  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.355  -12.673 -12.681 1.00 23.93  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? 0.142   -12.382 -12.453 1.00 23.78  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.793   -11.683 -13.259 1.00 26.58  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.462  -14.126 -13.146 1.00 27.70  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -2.864  -14.659 -13.576 1.00 29.90  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -3.756  -14.645 -12.337 1.00 36.49  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.222  -14.934 -12.611 1.00 43.03  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.385  -16.368 -12.850 1.00 46.97  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.633   -12.854 -11.295 1.00 21.97  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 2.026   -12.689 -10.895 1.00 24.15  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.673   -14.061 -10.822 1.00 21.77  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 2.063   -15.058 -10.432 1.00 21.12  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 2.104   -12.111 -9.456  1.00 22.95  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.648   -10.664 -9.462  1.00 24.65  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.286   -10.393 -9.347  1.00 26.83  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.510   -9.594  -9.636  1.00 25.36  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.184  -9.091  -9.433  1.00 31.48  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 2.039   -8.277  -9.703  1.00 27.71  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.684   -8.033  -9.586  1.00 32.24  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? 0.129   -6.769  -9.746  1.00 33.19  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 4.000   -14.186 -11.091 1.00 22.47  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.662   -15.473 -10.886 1.00 23.55  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 5.013   -15.590 -9.411  1.00 22.41  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.704   -14.702 -8.910  1.00 23.41  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.934   -15.367 -11.744 1.00 23.70  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 6.151   -13.926 -11.944 1.00 24.77  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.858   -13.128 -11.648 1.00 24.79  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.434   -16.601 -8.752  1.00 22.75  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.682   -16.788 -7.319  1.00 21.21  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.647   -17.960 -7.144  1.00 21.76  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.335   -19.118 -7.519  1.00 23.80  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.345   -17.052 -6.607  1.00 21.36  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.328   -15.927 -6.864  1.00 22.28  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.631   -17.241 -5.100  1.00 20.88  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.857   -14.526 -6.528  1.00 24.07  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.753   -17.709 -6.409  1.00 20.55  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.638   -18.790 -6.063  1.00 21.86  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.386   -19.192 -4.620  1.00 22.03  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.458   -18.366 -3.704  1.00 20.81  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 9.092   -18.286 -6.257  1.00 22.37  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 10.117  -19.312 -5.804  1.00 24.13  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.521  -20.344 -6.686  1.00 25.07  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.667  -19.266 -4.511  1.00 24.11  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.461  -21.285 -6.245  1.00 24.86  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.632  -20.208 -4.098  1.00 26.13  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 12.027  -21.206 -4.984  1.00 26.06  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 7.119   -20.490 -4.438  1.00 20.52  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.734   -20.991 -3.123  1.00 21.49  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.957   -21.509 -2.378  1.00 23.44  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.657   -22.397 -2.907  1.00 24.69  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.731   -22.139 -3.350  1.00 23.61  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 4.341   -21.638 -3.743  1.00 21.04  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.992   -21.503 -5.074  1.00 25.72  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 3.375   -21.390 -2.762  1.00 24.63  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.728   -21.011 -5.437  1.00 26.95  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 2.111   -20.925 -3.127  1.00 27.29  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.806   -20.720 -4.453  1.00 26.59  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 8.265   -20.916 -1.215  1.00 22.10  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.425   -21.422 -0.478  1.00 21.10  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 9.183   -22.869 -0.042  1.00 25.20  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 8.043   -23.311 0.072   1.00 24.72  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.657   -20.501 0.726   1.00 22.26  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 10.101  -19.116 0.292   1.00 21.56  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.386  -18.923 -0.252  1.00 19.74  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.349   -17.973 0.583   1.00 22.05  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.785  -17.643 -0.590  1.00 18.62  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.775   -16.696 0.260   1.00 18.79  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.997  -16.531 -0.362  1.00 19.49  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 10.282  -23.600 0.146   1.00 24.16  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 10.225  -24.975 0.647   1.00 23.97  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 10.009  -25.964 -0.509  1.00 29.03  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.881  -26.769 -0.810  1.00 30.87  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.864   -25.891 -1.194  1.00 29.83  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.608   -26.716 -2.372  1.00 29.67  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.387   -26.211 -3.580  1.00 30.66  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.682   -26.976 -4.507  1.00 29.27  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 7.108   -26.765 -2.687  1.00 32.86  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.743   -25.457 -3.128  1.00 29.00  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 6.231   -27.249 -1.554  1.00 32.89  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.654   -24.889 -3.630  1.00 25.40  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.354  -24.277 -4.756  1.00 26.90  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.537   -24.405 -6.047  1.00 28.12  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 10.115  -24.381 -7.135  1.00 28.03  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.796  -24.799 -4.940  1.00 26.85  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.540  -24.856 -3.646  1.00 30.79  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.343  -25.909 -3.269  1.00 31.26  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.586  -23.965 -2.627  1.00 27.50  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.860  -25.652 -2.081  1.00 36.59  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.434  -24.479 -1.674  1.00 33.16  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 8.208   -24.517 -5.907  1.00 28.31  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 7.325   -24.528 -7.076  1.00 29.24  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.891   -23.116 -7.489  1.00 29.29  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 7.005   -22.154 -6.709  1.00 27.69  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 6.125   -25.438 -6.853  1.00 30.55  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.529   -26.909 -6.735  1.00 38.70  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.458   -27.789 -6.107  1.00 47.87  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 4.324   -27.324 -5.882  1.00 51.54  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.794   -28.959 -5.798  1.00 50.63  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.459   -22.961 -8.753  1.00 25.59  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.952   -21.680 -9.202  1.00 24.49  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.508   -21.886 -9.646  1.00 26.70  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 4.210   -22.857 -10.344 1.00 29.01  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.768   -21.110 -10.355 1.00 29.79  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 8.100   -20.837 -9.920  1.00 30.56  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 6.147   -19.855 -10.965 1.00 29.59  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.616   -20.971 -9.254  1.00 26.15  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 2.281   -20.898 -9.817  1.00 25.09  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.922   -19.445 -10.100 1.00 25.95  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.629   -18.508 -9.703  1.00 27.98  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 1.291   -21.519 -8.843  1.00 26.58  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.864   -19.218 -10.905 1.00 24.19  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.498   -17.870 -11.292 1.00 24.92  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -0.766  -17.492 -10.533 1.00 29.99  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -1.759  -18.229 -10.557 1.00 32.61  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? 0.179   -17.835 -12.797 1.00 26.23  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.379   -18.177 -13.660 1.00 29.20  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.579   -17.477 -13.536 1.00 37.34  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.293   -19.206 -14.592 1.00 35.63  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.687   -17.792 -14.330 1.00 42.76  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.393   -19.503 -15.380 1.00 35.20  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.578   -18.802 -15.259 1.00 36.78  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.714  -16.376 -9.785  1.00 23.38  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -1.807  -16.022 -8.883  1.00 22.82  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.096  -14.532 -8.999  1.00 24.96  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.223  -13.711 -9.336  1.00 24.53  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.391  -16.307 -7.435  1.00 25.56  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.408  -17.782 -7.054  1.00 24.59  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.015  -17.923 -5.575  1.00 24.77  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -2.836  -18.363 -7.295  1.00 30.57  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.354  -14.171 -8.707  1.00 22.07  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.694  -12.759 -8.631  1.00 22.91  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.700  -12.269 -7.171  1.00 19.74  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.653  -13.092 -6.222  1.00 20.33  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -3.815  -10.942 -6.986  1.00 22.33  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -3.718  -10.329 -5.644  1.00 21.36  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.687  -10.844 -4.586  1.00 21.91  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.411  -10.789 -3.398  1.00 20.94  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -3.995  -8.851  -5.926  1.00 22.40  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.458  -8.633  -7.335  1.00 22.32  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -3.779  -9.935  -8.066  1.00 22.61  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -5.847  -11.358 -5.053  1.00 23.44  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -6.809  -11.903 -4.088  1.00 22.82  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.252  -13.065 -3.250  1.00 22.33  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -6.697  -13.321 -2.138  1.00 22.29  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.091  -12.405 -4.781  1.00 25.04  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -7.939  -13.680 -5.574  1.00 30.04  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.309  -14.105 -6.124  1.00 34.12  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.285  -15.358 -6.939  1.00 37.29  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -8.859  -16.520 -6.159  1.00 41.11  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.197  -13.755 -3.760  1.00 20.71  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.610  -14.889 -3.090  1.00 21.63  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.263  -14.514 -2.462  1.00 20.86  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.596  -15.455 -2.017  1.00 22.52  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.510  -16.083 -4.038  1.00 23.57  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -5.889  -16.654 -4.388  1.00 28.06  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -6.714  -16.770 -3.426  1.00 29.16  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.114  -16.982 -5.562  1.00 28.71  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -2.923  -13.210 -2.447  1.00 19.68  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.607  -12.783 -1.937  1.00 19.54  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -1.755  -11.925 -0.682  1.00 17.95  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.363  -10.853 -0.715  1.00 21.01  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -0.847  -12.076 -3.069  1.00 20.35  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -0.725  -12.861 -4.372  1.00 22.09  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.072  -11.968 -5.419  1.00 24.36  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? 0.146   -14.098 -4.214  1.00 21.57  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.148  -12.394 0.423   1.00 20.45  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.243  -11.735 1.726   1.00 19.82  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? 0.139   -11.231 2.132   1.00 22.30  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 1.035   -12.049 2.353   1.00 24.50  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.731  -12.777 2.740   1.00 20.91  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.181  -13.204 2.468   1.00 21.75  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.476  -14.114 1.459   1.00 23.92  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.202  -12.679 3.261   1.00 23.86  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -4.811  -14.468 1.176   1.00 26.15  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.513  -13.047 2.967   1.00 24.21  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -5.788  -13.935 1.972   1.00 22.74  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.366   -9.919  2.261   1.00 24.29  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.720   -9.436  2.576   1.00 23.19  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 2.281   -10.070 3.839   1.00 22.09  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.606   -10.301 4.861   1.00 23.93  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.521   -7.930  2.700   1.00 25.13  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.397   -7.652  1.671   1.00 29.07  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.568  -8.802  1.961   1.00 25.95  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.584   -10.449 3.776   1.00 23.46  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 4.139   -11.334 4.789   1.00 21.82  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 4.184   -10.687 6.196   1.00 21.98  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.811   -11.364 7.162   1.00 25.28  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.549   -11.758 4.309   1.00 22.69  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 6.339   -12.538 5.351   1.00 23.85  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 6.035   -13.878 5.635   1.00 25.59  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.378   -11.941 6.060   1.00 29.42  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.717   -14.630 6.597   1.00 26.22  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 8.058   -12.691 7.012   1.00 26.97  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.737   -14.003 7.288   1.00 28.10  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.452   -14.725 8.242   1.00 29.68  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.556   -9.409  6.253   1.00 26.79  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.749   -8.759  7.553   1.00 31.37  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.434   -8.748  8.333   1.00 27.19  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 3.434   -9.260  9.449   1.00 32.93  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.434   -7.410  7.462   1.00 34.12  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 5.868   -6.853  8.812   1.00 58.58  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 6.526   -7.602  9.581   1.00 57.52  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 5.529   -5.680  9.094   1.00 71.26  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 2.347   -8.325  7.662   1.00 29.84  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 1.020   -8.234  8.284   1.00 31.10  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? 0.491   -9.600  8.710   1.00 31.24  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.213  -9.689  9.719   1.00 28.16  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? 0.092   -7.585  7.251   1.00 29.31  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -1.398  -7.491  7.649   1.00 35.94  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.176  -6.765  6.553   1.00 34.07  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -3.315  -6.039  7.200   1.00 37.72  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.430  -6.917  7.533   1.00 47.05  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.801   -10.665 7.950   1.00 28.29  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? 0.127   -11.960 8.008   1.00 26.15  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.885   -13.051 8.797   1.00 26.35  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? 0.333   -14.132 9.003   1.00 28.76  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.143  -12.491 6.606   1.00 26.55  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.008  -11.578 5.934   1.00 36.81  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 2.162   -12.815 9.164   1.00 26.81  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.994   -13.910 9.646   1.00 29.04  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 2.550   -14.418 11.020  1.00 29.58  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.681   -15.604 11.312  1.00 32.93  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 4.482   -13.548 9.602   1.00 29.62  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.867   -12.388 10.456  1.00 32.54  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 6.335   -12.116 10.130  1.00 39.61  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.960   -11.287 11.212  1.00 48.32  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.244   -10.011 11.276  1.00 51.37  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.978   -13.525 11.839  0.50 33.79  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 2.033   -13.513 11.861  0.50 33.14  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 1.450   -13.919 13.141  0.50 36.30  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 1.443   -13.932 13.126  0.50 35.63  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? 0.329   -14.954 12.996  0.50 33.92  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? 0.469   -15.082 12.866  0.50 32.92  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? 0.147   -15.810 13.858  0.50 35.90  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? 0.563   -16.146 13.482  0.50 36.32  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 1.017   -12.701 13.943  0.50 37.65  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.725   -12.772 13.798  0.50 36.27  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 2.134   -11.930 14.636  0.50 43.38  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? 0.255   -13.007 15.229  0.50 43.73  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 3.289   -12.414 14.614  0.50 44.04  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 1.116   -13.021 16.141  0.50 45.54  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.848   -10.847 15.198  0.50 42.72  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -0.973  -13.172 15.425  0.50 45.67  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -0.446  -14.864 11.910  1.00 30.61  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -1.541  -15.779 11.671  1.00 29.11  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.074  -17.018 10.915  1.00 32.19  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -1.506  -18.128 11.217  1.00 35.80  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -2.594  -15.027 10.861  1.00 29.88  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -3.848  -15.786 10.621  1.00 32.31  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -4.907  -14.849 10.034  1.00 39.07  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.274  -15.483 10.019  1.00 42.79  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.191  -14.573 9.319   1.00 45.83  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.203  -16.839 9.902   1.00 28.03  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? 0.008   -17.913 8.941   1.00 27.85  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 1.375   -18.585 9.125   1.00 26.41  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 1.631   -19.651 8.557   1.00 30.22  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.169  -17.394 7.505   1.00 25.61  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -1.576  -16.970 7.128   1.00 27.29  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -2.695  -17.718 7.525   1.00 28.53  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -1.778  -15.777 6.439   1.00 27.88  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -3.964  -17.324 7.138   1.00 29.71  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.050  -15.364 6.074   1.00 29.89  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.141  -16.123 6.461   1.00 28.92  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -5.372  -15.681 6.055   1.00 31.15  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 2.235   -17.969 9.928   1.00 26.79  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 3.632   -18.390 9.992   1.00 28.68  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.877   -19.351 11.156  1.00 31.69  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 4.685   -19.078 12.021  1.00 41.61  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 3.118   -20.433 11.181  1.00 35.80  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 3.338   -21.441 12.199  1.00 39.07  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 3.602   -22.756 11.489  1.00 33.37  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 3.164   -22.987 10.359  1.00 35.71  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 2.150   -21.505 13.162  1.00 41.49  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 2.055   -20.253 14.013  1.00 41.53  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? 0.964   -20.292 15.072  1.00 46.94  ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 4.373   -23.682 12.112  1.00 35.32  ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 4.650   -24.955 11.453  1.00 34.23  ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 3.390   -25.701 11.037  1.00 32.94  ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 2.367   -25.610 11.715  1.00 41.33  ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 5.509   -25.718 12.499  1.00 36.32  ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 6.106   -24.625 13.359  1.00 41.13  ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 5.083   -23.479 13.389  1.00 37.85  ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 3.488   -26.457 9.949   1.00 37.14  ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 2.405   -27.171 9.310   1.00 40.30  ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.996   -28.496 8.860   1.00 46.50  ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 4.171   -28.581 8.531   1.00 49.42  ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.929   -26.356 8.106   1.00 45.57  ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? 0.616   -26.802 7.511   1.00 56.01  ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? 0.577   -27.754 6.729   1.00 57.35  ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -0.456  -26.070 7.782   1.00 53.17  ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 2.174   -29.537 8.830   1.00 48.07  ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 2.689   -30.859 8.546   1.00 43.78  ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.962   -31.038 7.052   1.00 48.70  ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 3.572   -32.033 6.652   1.00 46.98  ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 1.659   -31.849 9.110   1.00 54.49  ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? 0.399   -32.060 8.257   1.00 55.46  ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 2.510   -30.091 6.212   1.00 41.56  ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 2.536   -30.328 4.777   1.00 40.97  ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.964   -30.291 4.232   1.00 36.18  ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 4.791   -29.534 4.732   1.00 36.26  ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 1.645   -29.336 4.017   1.00 40.59  ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? 0.186   -29.566 4.374   1.00 50.70  ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -0.353  -30.795 3.661   1.00 44.89  ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -1.040  -30.415 2.423   1.00 55.74  ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -2.177  -29.713 2.400   1.00 56.74  ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -2.741  -29.431 1.241   1.00 59.29  ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -2.759  -29.327 3.528   1.00 58.45  ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 4.209   -31.118 3.207   1.00 34.97  ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 5.545   -31.306 2.663   1.00 36.19  ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 6.120   -29.956 2.223   1.00 35.79  ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 5.512   -29.278 1.386   1.00 32.59  ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 5.521   -32.251 1.464   1.00 40.19  ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.882   -32.545 0.871   1.00 43.24  ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.930   -33.746 -0.070  1.00 51.36  ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 8.316   -33.946 -0.605  1.00 53.54  ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 7.309   -29.630 2.750   1.00 33.21  ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 8.066   -28.451 2.342   1.00 32.06  ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 7.708   -27.205 3.155   1.00 30.15  ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 8.442   -26.208 3.087   1.00 29.59  ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 6.603   -27.235 3.903   1.00 29.69  ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 6.143   -26.018 4.563   1.00 28.44  ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 7.175   -25.466 5.572   1.00 31.87  ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 7.463   -24.263 5.628   1.00 28.86  ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 4.755   -26.290 5.153   1.00 29.69  ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 4.064   -25.004 5.583   1.00 32.14  ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 4.343   -24.412 6.800   1.00 31.88  ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 3.102   -24.400 4.758   1.00 33.28  ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 3.718   -23.230 7.184   1.00 29.11  ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 2.480   -23.205 5.147   1.00 25.82  ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 2.771   -22.628 6.352   1.00 27.39  ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 7.741   -26.330 6.425   1.00 29.39  ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 8.607   -25.817 7.481   1.00 29.79  ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.941   -25.337 6.889   1.00 23.43  ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 10.520  -24.332 7.378   1.00 28.18  ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 8.760   -26.853 8.607   1.00 28.61  ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 7.426   -27.120 9.269   1.00 36.37  ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 6.536   -26.266 9.237   1.00 32.71  ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 7.275   -28.282 9.900   1.00 33.51  ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 10.428  -26.013 5.834   1.00 24.91  ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 11.593  -25.515 5.131   1.00 24.62  ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 11.243  -24.138 4.557   1.00 24.56  ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 12.063  -23.217 4.608   1.00 23.95  ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 12.036  -26.405 3.963   1.00 27.69  ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 13.315  -25.907 3.300   1.00 27.58  ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 13.818  -26.959 2.314   1.00 41.86  ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 13.142  -27.976 2.074   1.00 46.55  ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 14.919  -26.775 1.789   1.00 39.43  ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 10.035  -24.019 3.987   1.00 25.54  ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 9.585   -22.717 3.486   1.00 27.70  ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 9.599   -21.602 4.532   1.00 22.89  ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.967   -20.473 4.184   1.00 23.00  ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 9.158   -21.871 5.786   1.00 22.22  ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 9.154   -20.882 6.836   1.00 22.69  ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 10.591  -20.428 7.118   1.00 22.95  ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.816  -19.244 7.354   1.00 23.01  ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 8.497   -21.380 8.130   1.00 26.21  ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 7.010   -21.715 7.978   1.00 26.62  ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 6.663   -22.317 9.353   1.00 31.82  ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 6.208   -20.438 7.744   1.00 27.14  ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 11.562  -21.372 7.024   1.00 24.74  ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.941  -21.006 7.291   1.00 25.93  ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 13.438  -20.073 6.184   1.00 21.58  ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 14.083  -19.070 6.466   1.00 22.50  ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.845  -22.262 7.421   1.00 26.34  ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 15.280  -21.897 7.709   1.00 24.62  ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.889  -21.816 8.930   1.00 28.60  ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 16.283  -21.546 6.732   1.00 26.15  ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 17.203  -21.449 8.774   1.00 27.93  ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 17.473  -21.288 7.444   1.00 25.65  ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 16.305  -21.461 5.330   1.00 27.01  ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 18.653  -20.917 6.798   1.00 25.29  ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 17.462  -21.058 4.699   1.00 26.97  ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 18.629  -20.800 5.432   1.00 28.28  ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 13.111  -20.393 4.931   1.00 21.12  ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 13.638  -19.650 3.802   1.00 20.46  ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 13.101  -18.222 3.837   1.00 22.01  ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.859  -17.282 3.631   1.00 20.56  ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 13.202  -20.344 2.522   1.00 21.92  ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.974  -21.652 2.368   1.00 21.36  ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 13.566  -22.372 1.085   1.00 26.81  ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 12.626  -21.943 0.373   1.00 25.63  ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 14.133  -23.472 0.810   1.00 26.50  ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 11.788  -18.057 4.099   1.00 21.83  ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 11.239  -16.700 3.974   1.00 20.51  ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 11.772  -15.799 5.117   1.00 20.24  ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.921  -14.589 4.947   1.00 21.26  ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 9.685   -16.745 3.949   1.00 18.79  ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 9.117   -15.373 3.547   1.00 21.10  ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 9.166   -17.101 5.333   1.00 20.93  ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 7.678   -15.517 3.045   1.00 20.13  ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 12.057  -16.416 6.271   1.00 19.97  ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 12.626  -15.685 7.428   1.00 24.24  ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 14.114  -15.377 7.269   1.00 23.78  ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 14.551  -14.267 7.674   1.00 25.98  ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 12.291  -16.425 8.737   1.00 24.87  ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 12.734  -15.707 10.010  1.00 31.19  ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 12.050  -16.313 11.236  1.00 36.21  ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 11.825  -17.532 11.309  1.00 35.29  ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 11.649  -15.475 12.186  1.00 43.06  ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.871  -16.310 6.677   1.00 21.29  ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 16.328  -16.282 6.807   1.00 20.63  ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 17.040  -15.934 5.505   1.00 22.52  ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 18.140  -15.353 5.547   1.00 24.50  ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 16.838  -17.589 7.413   1.00 22.65  ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 16.396  -17.697 8.857   1.00 27.13  ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 16.756  -16.846 9.687   1.00 30.42  ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 15.448  -18.574 9.155   1.00 26.48  ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 16.505  -16.326 4.340   1.00 21.28  ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 17.149  -15.922 3.112   1.00 21.01  ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 16.123  -15.833 1.980   1.00 22.37  ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 16.137  -16.612 1.024   1.00 22.01  ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 18.295  -16.870 2.744   1.00 22.38  ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 19.329  -16.229 1.844   1.00 25.00  ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 19.089  -15.235 1.149   1.00 23.67  ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 20.548  -16.782 1.834   1.00 28.75  ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 15.178  -14.884 2.086   1.00 20.69  ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 14.048  -14.900 1.151   1.00 19.85  ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 14.384  -14.454 -0.262  1.00 22.54  ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 13.583  -14.643 -1.172  1.00 21.03  ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 13.111  -13.914 1.833   1.00 20.75  ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 14.029  -12.939 2.561   1.00 21.03  ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 15.044  -13.897 3.168   1.00 20.79  ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 15.583  -13.882 -0.469  1.00 19.98  ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.919  -13.359 -1.793  1.00 20.05  ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 17.034  -14.166 -2.487  1.00 20.85  ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 17.468  -13.762 -3.575  1.00 22.60  ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 16.315  -11.874 -1.705  1.00 20.44  ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 15.240  -11.029 -1.129  1.00 20.93  ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.970  -10.968 -1.717  1.00 20.10  ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 15.199  -10.286 -0.014  1.00 21.66  ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 13.224  -10.105 -0.997  1.00 19.78  ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.944  -9.706  0.060   1.00 21.50  ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 17.326  -15.344 -1.950  1.00 21.47  ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 18.384  -16.183 -2.535  1.00 22.00  ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.908  -16.894 -3.792  1.00 27.54  ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 16.718  -17.038 -4.064  1.00 25.33  ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.862  -17.163 -1.518  1.00 23.91  ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.892  -17.389 -4.554  1.00 26.99  ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 18.603  -18.334 -5.617  1.00 29.96  ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 18.337  -19.722 -5.042  1.00 32.24  ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 19.158  -20.269 -4.302  1.00 31.89  ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.783  -18.344 -6.578  1.00 33.84  ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 19.621  -19.509 -7.362  1.00 35.66  ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 17.186  -20.306 -5.414  1.00 27.78  ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.784  -21.628 -4.968  1.00 29.24  ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 16.704  -22.564 -6.172  1.00 36.87  ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 16.226  -23.680 -6.040  1.00 46.40  ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 15.452  -21.599 -4.197  1.00 28.38  ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 15.612  -21.014 -2.797  1.00 25.20  ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 16.042  -21.808 -1.727  1.00 26.91  ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 15.305  -19.673 -2.527  1.00 25.89  ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 16.223  -21.269 -0.452  1.00 30.26  ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 15.465  -19.130 -1.264  1.00 26.72  ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.906  -19.929 -0.219  1.00 27.05  ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 16.116  -19.403 1.017   1.00 28.50  ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 17.233  -22.120 -7.312  1.00 46.31  ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 17.390  -22.996 -8.462  1.00 61.80  ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 18.637  -23.874 -8.282  1.00 70.54  ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 19.679  -23.322 -7.854  1.00 69.89  ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 17.444  -22.210 -9.743  1.00 65.47  ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 16.132  -21.803 -10.103 1.00 69.08  ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 18.521  -25.081 -8.577  1.00 83.10  ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 38.844  -11.098 -42.565 1.00 67.30  ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.516  -12.058 -43.650 1.00 64.16  ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 37.002  -12.273 -43.662 1.00 59.29  ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.446  -12.652 -42.632 1.00 68.64  ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.264  -13.380 -43.421 1.00 73.88  ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 39.265  -14.363 -44.595 1.00 88.62  ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 40.115  -13.869 -46.114 1.00 87.04  ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 41.515  -12.902 -45.530 1.00 72.60  ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.281  -12.004 -44.786 1.00 50.68  ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.829  -12.204 -44.834 1.00 47.45  ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.520  -13.652 -44.474 1.00 47.48  ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.315  -14.530 -44.787 1.00 45.78  ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.438  -11.862 -46.267 1.00 47.59  ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.543  -10.918 -46.714 1.00 44.06  ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.802  -11.443 -46.044 1.00 42.41  ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.406  -13.862 -43.758 1.00 42.73  ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.962  -15.206 -43.406 1.00 43.42  ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.569  -15.434 -43.980 1.00 38.96  ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 31.001  -14.539 -44.603 1.00 38.57  ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 33.099  -15.468 -41.904 1.00 49.34  ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.508  -15.455 -41.418 1.00 62.25  ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.452  -16.372 -41.841 1.00 63.45  ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 35.141  -14.631 -40.559 1.00 60.35  ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.611  -16.108 -41.245 1.00 57.08  ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.445  -15.059 -40.459 1.00 63.29  ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 31.019  -16.640 -43.769 1.00 35.70  ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.699  -16.960 -44.291 1.00 37.08  ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.676  -15.931 -43.812 1.00 34.42  ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.785  -15.536 -44.552 1.00 40.16  ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.322  -18.339 -43.808 1.00 38.34  ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.822  -15.551 -42.545 1.00 39.27  ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 28.030  -14.501 -41.929 1.00 39.94  ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.924  -13.286 -41.679 1.00 36.39  ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 30.066  -13.439 -41.257 1.00 39.11  ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.535  -14.935 -40.546 1.00 37.89  ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.493  -16.044 -40.603 1.00 36.35  ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 25.149  -15.742 -40.801 1.00 34.90  ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.864  -17.386 -40.509 1.00 34.01  ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 24.181  -16.736 -40.865 1.00 35.88  ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.886  -18.381 -40.564 1.00 30.94  ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.557  -18.064 -40.732 1.00 31.86  ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.383  -12.104 -41.988 1.00 39.30  ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 29.085  -10.848 -41.777 1.00 35.84  ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.283  -10.009 -40.776 1.00 38.57  ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 27.054  -10.146 -40.656 1.00 33.45  ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 29.188  -10.154 -43.139 1.00 43.95  ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 27.866  -9.807  -43.797 1.00 47.80  ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 28.012  -9.252  -45.215 1.00 53.46  ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 26.698  -8.840  -45.821 1.00 51.76  ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 25.808  -9.988  -46.010 1.00 52.53  ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.950  -9.073  -40.060 1.00 42.07  ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.268  -8.133  -39.162 1.00 33.57  ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.088  -7.469  -39.837 1.00 33.67  ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.186  -6.988  -40.979 1.00 38.30  ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.440  -7.162  -38.944 1.00 35.73  ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.619  -8.090  -38.830 1.00 40.39  ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.410  -8.870  -40.095 1.00 41.82  ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.949  -7.480  -39.137 1.00 30.77  ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.742  -6.825  -39.603 1.00 28.44  ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.764  -7.814  -40.226 1.00 26.76  ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.613  -7.467  -40.468 1.00 29.17  ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.230  -9.050  -40.517 1.00 26.59  ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.285  -10.004 -41.070 1.00 26.62  ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.230  -10.364 -39.996 1.00 24.53  ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.556  -10.448 -38.818 1.00 29.06  ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 23.942  -11.316 -41.451 1.00 27.95  ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.694  -11.343 -42.777 1.00 37.50  ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.460  -10.441 -43.612 1.00 36.40  ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.480  -12.305 -42.953 1.00 35.41  ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 20.996  -10.487 -40.443 1.00 24.72  ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.859  -10.772 -39.547 1.00 23.91  ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.600  -12.278 -39.547 1.00 26.22  ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.667  -12.901 -40.618 1.00 27.29  ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.655  -9.959  -40.011 1.00 27.18  ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 18.913  -8.442  -40.088 1.00 26.81  ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.633  -7.716  -40.459 1.00 27.06  ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.544  -7.920  -38.796 1.00 28.12  ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.268  -12.843 -38.358 1.00 26.61  ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 19.064  -14.294 -38.242 1.00 23.59  ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.992  -14.559 -37.187 1.00 26.72  ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.608  -13.667 -36.440 1.00 25.99  ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.360  -14.993 -37.774 1.00 24.30  ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.503  -14.881 -38.805 1.00 26.36  ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.841  -14.537 -36.389 1.00 25.96  ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.554  -15.821 -37.094 1.00 25.71  ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 17.032  -16.338 -35.830 1.00 25.45  ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 18.132  -17.218 -35.250 1.00 23.90  ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.752  -17.982 -36.013 1.00 25.11  ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.807  -17.218 -36.059 1.00 23.86  ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.601  -16.410 -36.517 1.00 25.39  ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.384  -16.141 -37.870 1.00 28.70  ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.703  -15.915 -35.587 1.00 28.37  ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 13.305  -15.381 -38.268 1.00 30.87  ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.599  -15.161 -35.989 1.00 29.85  ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.406  -14.894 -37.333 1.00 30.93  ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.408  -17.057 -33.936 1.00 21.92  ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.446  -17.781 -33.248 1.00 24.27  ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.793  -18.741 -32.259 1.00 26.11  ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.835  -18.368 -31.554 1.00 26.08  ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.370  -16.811 -32.532 1.00 25.87  ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 19.329  -19.976 -32.223 1.00 24.17  ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.682  -21.013 -31.426 1.00 26.89  ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.575  -21.389 -30.248 1.00 27.91  ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.765  -21.680 -30.387 1.00 31.31  ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.347  -22.218 -32.325 1.00 26.51  ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.696  -23.429 -31.541 1.00 27.31  ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 16.262  -23.042 -31.198 1.00 26.86  ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 15.358  -24.137 -30.545 1.00 31.07  ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.950  -24.397 -29.237 1.00 28.04  ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.973  -21.338 -29.054 1.00 28.93  ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.642  -21.845 -27.863 1.00 30.66  ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.725  -22.825 -27.141 1.00 29.80  ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.502  -22.673 -27.145 1.00 31.07  ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 20.054  -20.689 -26.957 1.00 34.33  ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 21.126  -19.904 -27.679 1.00 34.89  ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 21.937  -18.721 -26.610 1.00 40.80  ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 22.930  -19.789 -25.547 1.00 34.41  ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 19.354  -23.782 -26.452 1.00 32.00  ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.567  -24.823 -25.802 1.00 31.50  ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.632  -24.169 -24.776 1.00 30.12  ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 18.059  -23.308 -24.007 1.00 34.67  ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.577  -25.773 -25.147 1.00 37.47  ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 18.941  -26.964 -24.415 1.00 43.15  ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 19.844  -27.701 -23.431 1.00 52.85  ? 16  LYS B CD  1 
ATOM   881  N N   . GLY B 1 18 ? 16.390  -24.656 -24.752 1.00 33.55  ? 17  GLY B N   1 
ATOM   882  C CA  . GLY B 1 18 ? 15.322  -24.180 -23.882 1.00 35.51  ? 17  GLY B CA  1 
ATOM   883  C C   . GLY B 1 18 ? 14.578  -22.965 -24.434 1.00 34.90  ? 17  GLY B C   1 
ATOM   884  O O   . GLY B 1 18 ? 13.662  -22.468 -23.780 1.00 32.43  ? 17  GLY B O   1 
ATOM   885  N N   . TYR B 1 19 ? 14.989  -22.438 -25.604 1.00 29.62  ? 18  TYR B N   1 
ATOM   886  C CA  . TYR B 1 19 ? 14.317  -21.231 -26.077 1.00 26.04  ? 18  TYR B CA  1 
ATOM   887  C C   . TYR B 1 19 ? 13.919  -21.391 -27.543 1.00 25.49  ? 18  TYR B C   1 
ATOM   888  O O   . TYR B 1 19 ? 14.577  -22.144 -28.256 1.00 28.14  ? 18  TYR B O   1 
ATOM   889  C CB  . TYR B 1 19 ? 15.261  -20.018 -26.043 1.00 27.11  ? 18  TYR B CB  1 
ATOM   890  C CG  . TYR B 1 19 ? 15.703  -19.717 -24.616 1.00 32.73  ? 18  TYR B CG  1 
ATOM   891  C CD1 . TYR B 1 19 ? 14.948  -18.889 -23.796 1.00 31.42  ? 18  TYR B CD1 1 
ATOM   892  C CD2 . TYR B 1 19 ? 16.789  -20.391 -24.058 1.00 32.90  ? 18  TYR B CD2 1 
ATOM   893  C CE1 . TYR B 1 19 ? 15.334  -18.654 -22.478 1.00 31.80  ? 18  TYR B CE1 1 
ATOM   894  C CE2 . TYR B 1 19 ? 17.171  -20.177 -22.736 1.00 36.03  ? 18  TYR B CE2 1 
ATOM   895  C CZ  . TYR B 1 19 ? 16.424  -19.320 -21.946 1.00 31.96  ? 18  TYR B CZ  1 
ATOM   896  O OH  . TYR B 1 19 ? 16.810  -19.103 -20.645 1.00 36.99  ? 18  TYR B OH  1 
ATOM   897  N N   . PRO B 1 20 ? 12.894  -20.679 -28.036 1.00 26.89  ? 19  PRO B N   1 
ATOM   898  C CA  . PRO B 1 20 ? 12.519  -20.734 -29.451 1.00 26.75  ? 19  PRO B CA  1 
ATOM   899  C C   . PRO B 1 20 ? 13.586  -19.997 -30.257 1.00 25.54  ? 19  PRO B C   1 
ATOM   900  O O   . PRO B 1 20 ? 14.259  -19.127 -29.725 1.00 26.49  ? 19  PRO B O   1 
ATOM   901  C CB  . PRO B 1 20 ? 11.169  -20.033 -29.536 1.00 28.10  ? 19  PRO B CB  1 
ATOM   902  C CG  . PRO B 1 20 ? 11.167  -19.096 -28.340 1.00 28.41  ? 19  PRO B CG  1 
ATOM   903  C CD  . PRO B 1 20 ? 12.035  -19.764 -27.274 1.00 29.63  ? 19  PRO B CD  1 
ATOM   904  N N   . HIS B 1 21 ? 13.686  -20.356 -31.538 1.00 25.90  ? 20  HIS B N   1 
ATOM   905  C CA  . HIS B 1 21 ? 14.495  -19.587 -32.491 1.00 24.05  ? 20  HIS B CA  1 
ATOM   906  C C   . HIS B 1 21 ? 14.222  -18.087 -32.304 1.00 23.80  ? 20  HIS B C   1 
ATOM   907  O O   . HIS B 1 21 ? 13.077  -17.654 -32.389 1.00 25.64  ? 20  HIS B O   1 
ATOM   908  C CB  . HIS B 1 21 ? 14.114  -20.034 -33.894 1.00 24.98  ? 20  HIS B CB  1 
ATOM   909  C CG  . HIS B 1 21 ? 14.344  -21.523 -34.094 1.00 26.25  ? 20  HIS B CG  1 
ATOM   910  N ND1 . HIS B 1 21 ? 13.500  -22.527 -33.620 1.00 29.91  ? 20  HIS B ND1 1 
ATOM   911  C CD2 . HIS B 1 21 ? 15.365  -22.163 -34.708 1.00 28.44  ? 20  HIS B CD2 1 
ATOM   912  C CE1 . HIS B 1 21 ? 13.988  -23.711 -33.956 1.00 30.40  ? 20  HIS B CE1 1 
ATOM   913  N NE2 . HIS B 1 21 ? 15.117  -23.534 -34.628 1.00 26.25  ? 20  HIS B NE2 1 
ATOM   914  N N   . TRP B 1 22 ? 15.285  -17.295 -32.091 1.00 23.88  ? 21  TRP B N   1 
ATOM   915  C CA  . TRP B 1 22 ? 15.068  -15.963 -31.527 1.00 23.14  ? 21  TRP B CA  1 
ATOM   916  C C   . TRP B 1 22 ? 15.582  -14.898 -32.496 1.00 24.80  ? 21  TRP B C   1 
ATOM   917  O O   . TRP B 1 22 ? 16.728  -15.031 -32.960 1.00 24.38  ? 21  TRP B O   1 
ATOM   918  C CB  . TRP B 1 22 ? 15.844  -15.846 -30.212 1.00 24.83  ? 21  TRP B CB  1 
ATOM   919  C CG  . TRP B 1 22 ? 15.296  -14.722 -29.359 1.00 24.25  ? 21  TRP B CG  1 
ATOM   920  C CD1 . TRP B 1 22 ? 15.544  -13.380 -29.496 1.00 24.26  ? 21  TRP B CD1 1 
ATOM   921  C CD2 . TRP B 1 22 ? 14.368  -14.839 -28.245 1.00 26.49  ? 21  TRP B CD2 1 
ATOM   922  N NE1 . TRP B 1 22 ? 14.868  -12.671 -28.519 1.00 25.26  ? 21  TRP B NE1 1 
ATOM   923  C CE2 . TRP B 1 22 ? 14.132  -13.537 -27.754 1.00 25.15  ? 21  TRP B CE2 1 
ATOM   924  C CE3 . TRP B 1 22 ? 13.713  -15.930 -27.648 1.00 28.18  ? 21  TRP B CE3 1 
ATOM   925  C CZ2 . TRP B 1 22 ? 13.273  -13.283 -26.673 1.00 27.26  ? 21  TRP B CZ2 1 
ATOM   926  C CZ3 . TRP B 1 22 ? 12.870  -15.684 -26.582 1.00 29.34  ? 21  TRP B CZ3 1 
ATOM   927  C CH2 . TRP B 1 22 ? 12.634  -14.377 -26.122 1.00 28.53  ? 21  TRP B CH2 1 
ATOM   928  N N   . PRO B 1 23 ? 14.816  -13.812 -32.774 1.00 23.57  ? 22  PRO B N   1 
ATOM   929  C CA  . PRO B 1 23 ? 15.287  -12.783 -33.714 1.00 21.39  ? 22  PRO B CA  1 
ATOM   930  C C   . PRO B 1 23 ? 16.593  -12.164 -33.215 1.00 23.80  ? 22  PRO B C   1 
ATOM   931  O O   . PRO B 1 23 ? 16.726  -11.780 -32.036 1.00 23.80  ? 22  PRO B O   1 
ATOM   932  C CB  . PRO B 1 23 ? 14.123  -11.744 -33.795 1.00 22.22  ? 22  PRO B CB  1 
ATOM   933  C CG  . PRO B 1 23 ? 13.416  -11.962 -32.449 1.00 23.25  ? 22  PRO B CG  1 
ATOM   934  C CD  . PRO B 1 23 ? 13.480  -13.509 -32.237 1.00 22.89  ? 22  PRO B CD  1 
ATOM   935  N N   . ALA B 1 24 ? 17.611  -12.073 -34.096 1.00 23.71  ? 23  ALA B N   1 
ATOM   936  C CA  . ALA B 1 24 ? 18.938  -11.701 -33.630 1.00 22.05  ? 23  ALA B CA  1 
ATOM   937  C C   . ALA B 1 24 ? 19.767  -11.164 -34.810 1.00 23.33  ? 23  ALA B C   1 
ATOM   938  O O   . ALA B 1 24 ? 19.308  -11.180 -35.954 1.00 24.80  ? 23  ALA B O   1 
ATOM   939  C CB  . ALA B 1 24 ? 19.647  -12.875 -32.944 1.00 24.72  ? 23  ALA B CB  1 
ATOM   940  N N   . ARG B 1 25 ? 20.946  -10.622 -34.475 1.00 25.56  ? 24  ARG B N   1 
ATOM   941  C CA  . ARG B 1 25 ? 21.825  -10.135 -35.532 1.00 27.14  ? 24  ARG B CA  1 
ATOM   942  C C   . ARG B 1 25 ? 23.247  -10.580 -35.243 1.00 26.00  ? 24  ARG B C   1 
ATOM   943  O O   . ARG B 1 25 ? 23.655  -10.826 -34.105 1.00 26.15  ? 24  ARG B O   1 
ATOM   944  C CB  . ARG B 1 25 ? 21.802  -8.615  -35.710 1.00 26.46  ? 24  ARG B CB  1 
ATOM   945  C CG  . ARG B 1 25 ? 22.399  -7.821  -34.553 1.00 28.46  ? 24  ARG B CG  1 
ATOM   946  C CD  . ARG B 1 25 ? 22.166  -6.306  -34.651 1.00 26.31  ? 24  ARG B CD  1 
ATOM   947  N NE  . ARG B 1 25 ? 22.840  -5.643  -33.533 1.00 27.90  ? 24  ARG B NE  1 
ATOM   948  C CZ  . ARG B 1 25 ? 22.539  -4.397  -33.111 1.00 30.58  ? 24  ARG B CZ  1 
ATOM   949  N NH1 . ARG B 1 25 ? 21.558  -3.741  -33.709 1.00 30.37  ? 24  ARG B NH1 1 
ATOM   950  N NH2 . ARG B 1 25 ? 23.202  -3.865  -32.098 1.00 29.37  ? 24  ARG B NH2 1 
ATOM   951  N N   . ILE B 1 26 ? 24.055  -10.627 -36.315 1.00 26.38  ? 25  ILE B N   1 
ATOM   952  C CA  . ILE B 1 26 ? 25.473  -10.812 -36.100 1.00 26.89  ? 25  ILE B CA  1 
ATOM   953  C C   . ILE B 1 26 ? 26.049  -9.436  -35.772 1.00 30.01  ? 25  ILE B C   1 
ATOM   954  O O   . ILE B 1 26 ? 25.794  -8.500  -36.535 1.00 33.85  ? 25  ILE B O   1 
ATOM   955  C CB  . ILE B 1 26 ? 26.118  -11.290 -37.411 1.00 30.02  ? 25  ILE B CB  1 
ATOM   956  C CG1 . ILE B 1 26 ? 25.432  -12.533 -37.990 1.00 29.47  ? 25  ILE B CG1 1 
ATOM   957  C CG2 . ILE B 1 26 ? 27.621  -11.504 -37.232 1.00 34.62  ? 25  ILE B CG2 1 
ATOM   958  C CD1 . ILE B 1 26 ? 25.477  -13.730 -37.061 1.00 32.17  ? 25  ILE B CD1 1 
ATOM   959  N N   . ASP B 1 27 ? 26.859  -9.389  -34.707 1.00 30.28  ? 26  ASP B N   1 
ATOM   960  C CA  . ASP B 1 27 ? 27.542  -8.162  -34.274 1.00 38.35  ? 26  ASP B CA  1 
ATOM   961  C C   . ASP B 1 27 ? 28.985  -8.101  -34.783 1.00 42.60  ? 26  ASP B C   1 
ATOM   962  O O   . ASP B 1 27 ? 29.512  -9.096  -35.256 1.00 40.53  ? 26  ASP B O   1 
ATOM   963  C CB  . ASP B 1 27 ? 27.523  -8.043  -32.760 1.00 34.77  ? 26  ASP B CB  1 
ATOM   964  C CG  . ASP B 1 27 ? 26.353  -7.299  -32.139 1.00 39.00  ? 26  ASP B CG  1 
ATOM   965  O OD1 . ASP B 1 27 ? 25.509  -6.759  -32.907 1.00 43.50  ? 26  ASP B OD1 1 
ATOM   966  O OD2 . ASP B 1 27 ? 26.308  -7.261  -30.876 1.00 38.58  ? 26  ASP B OD2 1 
ATOM   967  N N   A ASP B 1 28 ? 29.599  -6.911  -34.660 0.50 49.91  ? 27  ASP B N   1 
ATOM   968  N N   B ASP B 1 28 ? 29.615  -6.920  -34.691 0.50 48.25  ? 27  ASP B N   1 
ATOM   969  C CA  A ASP B 1 28 ? 31.009  -6.674  -34.936 0.50 56.56  ? 27  ASP B CA  1 
ATOM   970  C CA  B ASP B 1 28 ? 31.031  -6.776  -34.997 0.50 54.03  ? 27  ASP B CA  1 
ATOM   971  C C   A ASP B 1 28 ? 31.844  -7.085  -33.720 0.50 60.14  ? 27  ASP B C   1 
ATOM   972  C C   B ASP B 1 28 ? 31.844  -6.939  -33.711 0.50 58.96  ? 27  ASP B C   1 
ATOM   973  O O   A ASP B 1 28 ? 31.298  -7.464  -32.686 0.50 61.57  ? 27  ASP B O   1 
ATOM   974  O O   B ASP B 1 28 ? 31.279  -7.000  -32.621 0.50 62.57  ? 27  ASP B O   1 
ATOM   975  C CB  A ASP B 1 28 ? 31.267  -5.212  -35.280 0.50 55.96  ? 27  ASP B CB  1 
ATOM   976  C CB  B ASP B 1 28 ? 31.325  -5.466  -35.714 0.50 50.88  ? 27  ASP B CB  1 
ATOM   977  C CG  A ASP B 1 28 ? 30.101  -4.452  -35.902 0.50 55.22  ? 27  ASP B CG  1 
ATOM   978  C CG  B ASP B 1 28 ? 32.387  -5.542  -36.801 0.50 48.05  ? 27  ASP B CG  1 
ATOM   979  O OD1 A ASP B 1 28 ? 30.148  -4.185  -37.124 0.50 55.59  ? 27  ASP B OD1 1 
ATOM   980  O OD1 B ASP B 1 28 ? 33.382  -6.274  -36.600 0.50 48.75  ? 27  ASP B OD1 1 
ATOM   981  O OD2 A ASP B 1 28 ? 29.160  -4.118  -35.153 0.50 52.32  ? 27  ASP B OD2 1 
ATOM   982  O OD2 B ASP B 1 28 ? 32.219  -4.852  -37.831 0.50 43.78  ? 27  ASP B OD2 1 
ATOM   983  N N   . ILE B 1 29 ? 33.175  -7.008  -33.851 1.00 64.49  ? 28  ILE B N   1 
ATOM   984  C CA  . ILE B 1 29 ? 34.074  -7.289  -32.738 1.00 67.75  ? 28  ILE B CA  1 
ATOM   985  C C   . ILE B 1 29 ? 34.908  -6.032  -32.429 1.00 67.66  ? 28  ILE B C   1 
ATOM   986  O O   . ILE B 1 29 ? 34.310  -5.084  -31.874 1.00 66.08  ? 28  ILE B O   1 
ATOM   987  C CB  . ILE B 1 29 ? 34.959  -8.522  -33.015 1.00 70.86  ? 28  ILE B CB  1 
ATOM   988  N N   . LYS B 1 35 ? 37.543  -12.101 -28.185 1.00 66.55  ? 34  LYS B N   1 
ATOM   989  C CA  . LYS B 1 35 ? 37.077  -12.580 -29.515 1.00 62.66  ? 34  LYS B CA  1 
ATOM   990  C C   . LYS B 1 35 ? 36.214  -13.833 -29.337 1.00 63.03  ? 34  LYS B C   1 
ATOM   991  O O   . LYS B 1 35 ? 36.319  -14.523 -28.316 1.00 56.80  ? 34  LYS B O   1 
ATOM   992  C CB  . LYS B 1 35 ? 38.307  -12.733 -30.419 1.00 66.48  ? 34  LYS B CB  1 
ATOM   993  N N   . PRO B 1 36 ? 35.301  -14.160 -30.294 1.00 57.73  ? 35  PRO B N   1 
ATOM   994  C CA  . PRO B 1 36 ? 34.524  -15.407 -30.215 1.00 56.42  ? 35  PRO B CA  1 
ATOM   995  C C   . PRO B 1 36 ? 35.431  -16.625 -30.044 1.00 48.88  ? 35  PRO B C   1 
ATOM   996  O O   . PRO B 1 36 ? 36.599  -16.563 -30.409 1.00 55.65  ? 35  PRO B O   1 
ATOM   997  C CB  . PRO B 1 36 ? 33.764  -15.464 -31.553 1.00 55.68  ? 35  PRO B CB  1 
ATOM   998  C CG  . PRO B 1 36 ? 33.785  -14.044 -32.103 1.00 54.59  ? 35  PRO B CG  1 
ATOM   999  C CD  . PRO B 1 36 ? 34.953  -13.320 -31.455 1.00 54.28  ? 35  PRO B CD  1 
ATOM   1000 N N   . PRO B 1 37 ? 34.971  -17.765 -29.476 1.00 48.03  ? 36  PRO B N   1 
ATOM   1001 C CA  . PRO B 1 37 ? 35.687  -19.023 -29.679 1.00 45.74  ? 36  PRO B CA  1 
ATOM   1002 C C   . PRO B 1 37 ? 35.733  -19.228 -31.195 1.00 56.70  ? 36  PRO B C   1 
ATOM   1003 O O   . PRO B 1 37 ? 34.876  -18.711 -31.913 1.00 58.38  ? 36  PRO B O   1 
ATOM   1004 C CB  . PRO B 1 37 ? 34.820  -20.054 -28.943 1.00 48.32  ? 36  PRO B CB  1 
ATOM   1005 C CG  . PRO B 1 37 ? 34.078  -19.234 -27.894 1.00 49.57  ? 36  PRO B CG  1 
ATOM   1006 C CD  . PRO B 1 37 ? 33.827  -17.894 -28.561 1.00 48.86  ? 36  PRO B CD  1 
ATOM   1007 N N   . PRO B 1 38 ? 36.750  -19.925 -31.759 1.00 57.71  ? 37  PRO B N   1 
ATOM   1008 C CA  . PRO B 1 38 ? 36.776  -20.199 -33.205 1.00 56.75  ? 37  PRO B CA  1 
ATOM   1009 C C   . PRO B 1 38 ? 35.464  -20.790 -33.743 1.00 44.73  ? 37  PRO B C   1 
ATOM   1010 O O   . PRO B 1 38 ? 34.756  -21.489 -33.016 1.00 49.52  ? 37  PRO B O   1 
ATOM   1011 C CB  . PRO B 1 38 ? 37.984  -21.173 -33.351 1.00 59.50  ? 37  PRO B CB  1 
ATOM   1012 C CG  . PRO B 1 38 ? 38.283  -21.659 -31.932 1.00 57.28  ? 37  PRO B CG  1 
ATOM   1013 C CD  . PRO B 1 38 ? 37.917  -20.478 -31.045 1.00 61.15  ? 37  PRO B CD  1 
ATOM   1014 N N   . ASN B 1 39 ? 35.125  -20.474 -35.003 1.00 48.82  ? 38  ASN B N   1 
ATOM   1015 C CA  . ASN B 1 39 ? 33.925  -20.996 -35.662 1.00 51.85  ? 38  ASN B CA  1 
ATOM   1016 C C   . ASN B 1 39 ? 32.624  -20.367 -35.139 1.00 47.00  ? 38  ASN B C   1 
ATOM   1017 O O   . ASN B 1 39 ? 31.548  -20.772 -35.554 1.00 41.53  ? 38  ASN B O   1 
ATOM   1018 C CB  . ASN B 1 39 ? 33.746  -22.501 -35.452 1.00 55.66  ? 38  ASN B CB  1 
ATOM   1019 C CG  . ASN B 1 39 ? 34.944  -23.313 -35.892 1.00 66.21  ? 38  ASN B CG  1 
ATOM   1020 O OD1 . ASN B 1 39 ? 35.336  -24.258 -35.194 1.00 65.76  ? 38  ASN B OD1 1 
ATOM   1021 N ND2 . ASN B 1 39 ? 35.522  -22.976 -37.040 1.00 60.61  ? 38  ASN B ND2 1 
ATOM   1022 N N   . LYS B 1 40 ? 32.698  -19.388 -34.225 1.00 44.78  ? 39  LYS B N   1 
ATOM   1023 C CA  . LYS B 1 40 ? 31.488  -18.860 -33.611 1.00 39.08  ? 39  LYS B CA  1 
ATOM   1024 C C   . LYS B 1 40 ? 31.434  -17.367 -33.866 1.00 37.06  ? 39  LYS B C   1 
ATOM   1025 O O   . LYS B 1 40 ? 32.438  -16.775 -34.253 1.00 42.22  ? 39  LYS B O   1 
ATOM   1026 C CB  . LYS B 1 40 ? 31.407  -19.202 -32.124 1.00 40.62  ? 39  LYS B CB  1 
ATOM   1027 C CG  . LYS B 1 40 ? 31.417  -20.713 -31.896 1.00 37.32  ? 39  LYS B CG  1 
ATOM   1028 C CD  . LYS B 1 40 ? 30.864  -21.078 -30.529 1.00 44.59  ? 39  LYS B CD  1 
ATOM   1029 C CE  . LYS B 1 40 ? 30.765  -22.551 -30.358 1.00 43.47  ? 39  LYS B CE  1 
ATOM   1030 N NZ  . LYS B 1 40 ? 30.397  -22.835 -28.963 1.00 52.44  ? 39  LYS B NZ  1 
ATOM   1031 N N   . TYR B 1 41 ? 30.228  -16.797 -33.735 1.00 32.68  ? 40  TYR B N   1 
ATOM   1032 C CA  . TYR B 1 41 ? 29.957  -15.415 -34.076 1.00 28.95  ? 40  TYR B CA  1 
ATOM   1033 C C   . TYR B 1 41 ? 29.414  -14.714 -32.830 1.00 34.71  ? 40  TYR B C   1 
ATOM   1034 O O   . TYR B 1 41 ? 28.687  -15.323 -32.026 1.00 30.06  ? 40  TYR B O   1 
ATOM   1035 C CB  . TYR B 1 41 ? 28.906  -15.312 -35.189 1.00 29.37  ? 40  TYR B CB  1 
ATOM   1036 C CG  . TYR B 1 41 ? 29.379  -15.791 -36.553 1.00 31.63  ? 40  TYR B CG  1 
ATOM   1037 C CD1 . TYR B 1 41 ? 29.936  -14.916 -37.479 1.00 33.90  ? 40  TYR B CD1 1 
ATOM   1038 C CD2 . TYR B 1 41 ? 29.221  -17.121 -36.920 1.00 30.05  ? 40  TYR B CD2 1 
ATOM   1039 C CE1 . TYR B 1 41 ? 30.358  -15.366 -38.724 1.00 39.35  ? 40  TYR B CE1 1 
ATOM   1040 C CE2 . TYR B 1 41 ? 29.649  -17.587 -38.149 1.00 34.68  ? 40  TYR B CE2 1 
ATOM   1041 C CZ  . TYR B 1 41 ? 30.212  -16.707 -39.060 1.00 38.59  ? 40  TYR B CZ  1 
ATOM   1042 O OH  . TYR B 1 41 ? 30.568  -17.182 -40.300 1.00 35.62  ? 40  TYR B OH  1 
ATOM   1043 N N   . PRO B 1 42 ? 29.648  -13.389 -32.683 1.00 35.89  ? 41  PRO B N   1 
ATOM   1044 C CA  . PRO B 1 42 ? 28.946  -12.621 -31.655 1.00 32.05  ? 41  PRO B CA  1 
ATOM   1045 C C   . PRO B 1 42 ? 27.523  -12.355 -32.107 1.00 30.09  ? 41  PRO B C   1 
ATOM   1046 O O   . PRO B 1 42 ? 27.291  -11.731 -33.149 1.00 30.26  ? 41  PRO B O   1 
ATOM   1047 C CB  . PRO B 1 42 ? 29.740  -11.299 -31.515 1.00 32.68  ? 41  PRO B CB  1 
ATOM   1048 C CG  . PRO B 1 42 ? 30.553  -11.194 -32.790 1.00 36.00  ? 41  PRO B CG  1 
ATOM   1049 C CD  . PRO B 1 42 ? 30.574  -12.562 -33.484 1.00 33.54  ? 41  PRO B CD  1 
ATOM   1050 N N   . ILE B 1 43 ? 26.567  -12.813 -31.270 1.00 28.95  ? 42  ILE B N   1 
ATOM   1051 C CA  . ILE B 1 43 ? 25.136  -12.642 -31.504 1.00 27.85  ? 42  ILE B CA  1 
ATOM   1052 C C   . ILE B 1 43 ? 24.564  -11.599 -30.542 1.00 26.99  ? 42  ILE B C   1 
ATOM   1053 O O   . ILE B 1 43 ? 24.849  -11.649 -29.366 1.00 31.45  ? 42  ILE B O   1 
ATOM   1054 C CB  . ILE B 1 43 ? 24.442  -14.005 -31.340 1.00 27.02  ? 42  ILE B CB  1 
ATOM   1055 C CG1 . ILE B 1 43 ? 25.185  -15.079 -32.227 1.00 28.59  ? 42  ILE B CG1 1 
ATOM   1056 C CG2 . ILE B 1 43 ? 22.934  -13.870 -31.673 1.00 27.05  ? 42  ILE B CG2 1 
ATOM   1057 C CD1 . ILE B 1 43 ? 25.240  -14.765 -33.715 1.00 27.50  ? 42  ILE B CD1 1 
ATOM   1058 N N   . PHE B 1 44 ? 23.758  -10.677 -31.072 1.00 27.70  ? 43  PHE B N   1 
ATOM   1059 C CA  . PHE B 1 44 ? 22.893  -9.824  -30.263 1.00 28.06  ? 43  PHE B CA  1 
ATOM   1060 C C   . PHE B 1 44 ? 21.454  -10.286 -30.462 1.00 25.73  ? 43  PHE B C   1 
ATOM   1061 O O   . PHE B 1 44 ? 20.944  -10.296 -31.587 1.00 25.55  ? 43  PHE B O   1 
ATOM   1062 C CB  . PHE B 1 44 ? 23.089  -8.383  -30.744 1.00 27.35  ? 43  PHE B CB  1 
ATOM   1063 C CG  . PHE B 1 44 ? 22.154  -7.384  -30.066 1.00 27.96  ? 43  PHE B CG  1 
ATOM   1064 C CD1 . PHE B 1 44 ? 20.961  -7.007  -30.673 1.00 28.27  ? 43  PHE B CD1 1 
ATOM   1065 C CD2 . PHE B 1 44 ? 22.493  -6.815  -28.846 1.00 35.69  ? 43  PHE B CD2 1 
ATOM   1066 C CE1 . PHE B 1 44 ? 20.096  -6.106  -30.073 1.00 30.84  ? 43  PHE B CE1 1 
ATOM   1067 C CE2 . PHE B 1 44 ? 21.630  -5.887  -28.254 1.00 31.14  ? 43  PHE B CE2 1 
ATOM   1068 C CZ  . PHE B 1 44 ? 20.445  -5.551  -28.865 1.00 32.74  ? 43  PHE B CZ  1 
ATOM   1069 N N   . PHE B 1 45 ? 20.744  -10.553 -29.344 1.00 25.58  ? 44  PHE B N   1 
ATOM   1070 C CA  . PHE B 1 45 ? 19.349  -10.944 -29.353 1.00 24.85  ? 44  PHE B CA  1 
ATOM   1071 C C   . PHE B 1 45 ? 18.469  -9.720  -29.222 1.00 25.20  ? 44  PHE B C   1 
ATOM   1072 O O   . PHE B 1 45 ? 18.550  -8.968  -28.233 1.00 27.62  ? 44  PHE B O   1 
ATOM   1073 C CB  . PHE B 1 45 ? 19.111  -11.956 -28.209 1.00 25.75  ? 44  PHE B CB  1 
ATOM   1074 C CG  . PHE B 1 45 ? 19.839  -13.294 -28.331 1.00 25.36  ? 44  PHE B CG  1 
ATOM   1075 C CD1 . PHE B 1 45 ? 21.127  -13.466 -27.878 1.00 28.29  ? 44  PHE B CD1 1 
ATOM   1076 C CD2 . PHE B 1 45 ? 19.187  -14.393 -28.901 1.00 25.84  ? 44  PHE B CD2 1 
ATOM   1077 C CE1 . PHE B 1 45 ? 21.796  -14.666 -28.038 1.00 30.05  ? 44  PHE B CE1 1 
ATOM   1078 C CE2 . PHE B 1 45 ? 19.824  -15.609 -28.993 1.00 26.07  ? 44  PHE B CE2 1 
ATOM   1079 C CZ  . PHE B 1 45 ? 21.136  -15.741 -28.593 1.00 26.42  ? 44  PHE B CZ  1 
ATOM   1080 N N   . PHE B 1 46 ? 17.621  -9.536  -30.232 1.00 25.45  ? 45  PHE B N   1 
ATOM   1081 C CA  . PHE B 1 46 ? 16.644  -8.462  -30.206 1.00 23.96  ? 45  PHE B CA  1 
ATOM   1082 C C   . PHE B 1 46 ? 15.659  -8.668  -29.037 1.00 28.42  ? 45  PHE B C   1 
ATOM   1083 O O   . PHE B 1 46 ? 15.345  -9.786  -28.638 1.00 26.60  ? 45  PHE B O   1 
ATOM   1084 C CB  . PHE B 1 46 ? 15.863  -8.264  -31.499 1.00 25.17  ? 45  PHE B CB  1 
ATOM   1085 C CG  . PHE B 1 46 ? 16.793  -7.800  -32.617 1.00 26.35  ? 45  PHE B CG  1 
ATOM   1086 C CD1 . PHE B 1 46 ? 17.308  -6.485  -32.604 1.00 27.49  ? 45  PHE B CD1 1 
ATOM   1087 C CD2 . PHE B 1 46 ? 17.105  -8.663  -33.680 1.00 25.18  ? 45  PHE B CD2 1 
ATOM   1088 C CE1 . PHE B 1 46 ? 18.155  -6.072  -33.635 1.00 26.69  ? 45  PHE B CE1 1 
ATOM   1089 C CE2 . PHE B 1 46 ? 17.926  -8.225  -34.723 1.00 26.64  ? 45  PHE B CE2 1 
ATOM   1090 C CZ  . PHE B 1 46 ? 18.437  -6.927  -34.689 1.00 27.66  ? 45  PHE B CZ  1 
ATOM   1091 N N   . GLY B 1 47 ? 15.148  -7.563  -28.495 1.00 27.15  ? 46  GLY B N   1 
ATOM   1092 C CA  . GLY B 1 47 ? 14.114  -7.644  -27.450 1.00 27.15  ? 46  GLY B CA  1 
ATOM   1093 C C   . GLY B 1 47 ? 14.752  -7.776  -26.065 1.00 28.77  ? 46  GLY B C   1 
ATOM   1094 O O   . GLY B 1 47 ? 14.555  -6.923  -25.200 1.00 35.84  ? 46  GLY B O   1 
ATOM   1095 N N   . THR B 1 48 ? 15.551  -8.820  -25.850 1.00 28.59  ? 47  THR B N   1 
ATOM   1096 C CA  . THR B 1 48 ? 16.252  -9.048  -24.600 1.00 28.33  ? 47  THR B CA  1 
ATOM   1097 C C   . THR B 1 48 ? 17.487  -8.165  -24.520 1.00 30.24  ? 47  THR B C   1 
ATOM   1098 O O   . THR B 1 48 ? 17.947  -7.788  -23.429 1.00 32.43  ? 47  THR B O   1 
ATOM   1099 C CB  . THR B 1 48 ? 16.618  -10.524 -24.380 1.00 31.20  ? 47  THR B CB  1 
ATOM   1100 O OG1 . THR B 1 48 ? 17.627  -10.884 -25.336 1.00 31.86  ? 47  THR B OG1 1 
ATOM   1101 C CG2 . THR B 1 48 ? 15.409  -11.453 -24.419 1.00 29.15  ? 47  THR B CG2 1 
ATOM   1102 N N   . HIS B 1 49 ? 18.064  -7.887  -25.692 1.00 31.20  ? 48  HIS B N   1 
ATOM   1103 C CA  . HIS B 1 49 ? 19.345  -7.206  -25.808 1.00 31.56  ? 48  HIS B CA  1 
ATOM   1104 C C   . HIS B 1 49 ? 20.463  -7.976  -25.128 1.00 32.57  ? 48  HIS B C   1 
ATOM   1105 O O   . HIS B 1 49 ? 21.459  -7.355  -24.755 1.00 36.39  ? 48  HIS B O   1 
ATOM   1106 C CB  . HIS B 1 49 ? 19.279  -5.737  -25.347 1.00 30.14  ? 48  HIS B CB  1 
ATOM   1107 C CG  . HIS B 1 49 ? 18.069  -5.066  -25.881 1.00 32.58  ? 48  HIS B CG  1 
ATOM   1108 N ND1 . HIS B 1 49 ? 17.301  -4.240  -25.087 1.00 36.55  ? 48  HIS B ND1 1 
ATOM   1109 C CD2 . HIS B 1 49 ? 17.447  -5.101  -27.080 1.00 32.51  ? 48  HIS B CD2 1 
ATOM   1110 C CE1 . HIS B 1 49 ? 16.244  -3.815  -25.784 1.00 43.64  ? 48  HIS B CE1 1 
ATOM   1111 N NE2 . HIS B 1 49 ? 16.320  -4.311  -27.013 1.00 37.93  ? 48  HIS B NE2 1 
ATOM   1112 N N   . GLU B 1 50 ? 20.329  -9.308  -24.987 1.00 31.77  ? 49  GLU B N   1 
ATOM   1113 C CA  . GLU B 1 50 ? 21.425  -10.128 -24.474 1.00 31.70  ? 49  GLU B CA  1 
ATOM   1114 C C   . GLU B 1 50 ? 22.381  -10.498 -25.618 1.00 31.18  ? 49  GLU B C   1 
ATOM   1115 O O   . GLU B 1 50 ? 22.071  -10.279 -26.806 1.00 29.52  ? 49  GLU B O   1 
ATOM   1116 C CB  . GLU B 1 50 ? 20.936  -11.438 -23.860 1.00 31.21  ? 49  GLU B CB  1 
ATOM   1117 C CG  . GLU B 1 50 ? 20.010  -11.232 -22.663 1.00 34.97  ? 49  GLU B CG  1 
ATOM   1118 C CD  . GLU B 1 50 ? 19.507  -12.517 -22.014 1.00 41.70  ? 49  GLU B CD  1 
ATOM   1119 O OE1 . GLU B 1 50 ? 19.085  -13.416 -22.736 1.00 46.44  ? 49  GLU B OE1 1 
ATOM   1120 O OE2 . GLU B 1 50 ? 19.478  -12.629 -20.780 1.00 43.90  ? 49  GLU B OE2 1 
ATOM   1121 N N   . THR B 1 51 ? 23.521  -11.079 -25.234 1.00 30.72  ? 50  THR B N   1 
ATOM   1122 C CA  . THR B 1 51 ? 24.557  -11.462 -26.193 1.00 32.79  ? 50  THR B CA  1 
ATOM   1123 C C   . THR B 1 51 ? 25.012  -12.887 -25.914 1.00 35.46  ? 50  THR B C   1 
ATOM   1124 O O   . THR B 1 51 ? 24.914  -13.382 -24.790 1.00 38.99  ? 50  THR B O   1 
ATOM   1125 C CB  . THR B 1 51 ? 25.724  -10.463 -26.287 1.00 34.78  ? 50  THR B CB  1 
ATOM   1126 O OG1 . THR B 1 51 ? 26.367  -10.387 -25.023 1.00 36.90  ? 50  THR B OG1 1 
ATOM   1127 C CG2 . THR B 1 51 ? 25.311  -9.047  -26.639 1.00 37.04  ? 50  THR B CG2 1 
ATOM   1128 N N   . ALA B 1 52 ? 25.495  -13.583 -26.961 1.00 33.04  ? 51  ALA B N   1 
ATOM   1129 C CA  . ALA B 1 52 ? 26.160  -14.865 -26.786 1.00 31.97  ? 51  ALA B CA  1 
ATOM   1130 C C   . ALA B 1 52 ? 27.054  -15.137 -27.997 1.00 32.60  ? 51  ALA B C   1 
ATOM   1131 O O   . ALA B 1 52 ? 26.925  -14.465 -29.009 1.00 31.11  ? 51  ALA B O   1 
ATOM   1132 C CB  . ALA B 1 52 ? 25.160  -15.996 -26.590 1.00 33.36  ? 51  ALA B CB  1 
ATOM   1133 N N   . PHE B 1 53 ? 27.907  -16.157 -27.881 1.00 31.21  ? 52  PHE B N   1 
ATOM   1134 C CA  . PHE B 1 53 ? 28.642  -16.670 -29.029 1.00 32.93  ? 52  PHE B CA  1 
ATOM   1135 C C   . PHE B 1 53 ? 27.998  -17.971 -29.517 1.00 31.80  ? 52  PHE B C   1 
ATOM   1136 O O   . PHE B 1 53 ? 27.863  -18.947 -28.772 1.00 36.95  ? 52  PHE B O   1 
ATOM   1137 C CB  . PHE B 1 53 ? 30.096  -16.923 -28.619 1.00 36.25  ? 52  PHE B CB  1 
ATOM   1138 C CG  . PHE B 1 53 ? 30.912  -15.691 -28.261 1.00 37.88  ? 52  PHE B CG  1 
ATOM   1139 C CD1 . PHE B 1 53 ? 31.097  -14.670 -29.184 1.00 40.34  ? 52  PHE B CD1 1 
ATOM   1140 C CD2 . PHE B 1 53 ? 31.458  -15.544 -26.992 1.00 42.76  ? 52  PHE B CD2 1 
ATOM   1141 C CE1 . PHE B 1 53 ? 31.842  -13.543 -28.883 1.00 41.85  ? 52  PHE B CE1 1 
ATOM   1142 C CE2 . PHE B 1 53 ? 32.176  -14.391 -26.672 1.00 41.86  ? 52  PHE B CE2 1 
ATOM   1143 C CZ  . PHE B 1 53 ? 32.381  -13.405 -27.618 1.00 44.74  ? 52  PHE B CZ  1 
ATOM   1144 N N   . LEU B 1 54 ? 27.601  -17.989 -30.796 1.00 32.07  ? 53  LEU B N   1 
ATOM   1145 C CA  . LEU B 1 54 ? 27.002  -19.185 -31.368 1.00 28.25  ? 53  LEU B CA  1 
ATOM   1146 C C   . LEU B 1 54 ? 27.698  -19.533 -32.681 1.00 29.36  ? 53  LEU B C   1 
ATOM   1147 O O   . LEU B 1 54 ? 28.195  -18.642 -33.394 1.00 32.91  ? 53  LEU B O   1 
ATOM   1148 C CB  . LEU B 1 54 ? 25.497  -19.031 -31.611 1.00 30.49  ? 53  LEU B CB  1 
ATOM   1149 C CG  . LEU B 1 54 ? 24.625  -18.853 -30.365 1.00 31.20  ? 53  LEU B CG  1 
ATOM   1150 C CD1 . LEU B 1 54 ? 23.220  -18.610 -30.852 1.00 28.61  ? 53  LEU B CD1 1 
ATOM   1151 C CD2 . LEU B 1 54 ? 24.752  -20.150 -29.582 1.00 34.62  ? 53  LEU B CD2 1 
ATOM   1152 N N   . GLY B 1 55 ? 27.648  -20.838 -32.994 1.00 30.74  ? 54  GLY B N   1 
ATOM   1153 C CA  . GLY B 1 55 ? 28.144  -21.429 -34.225 1.00 30.31  ? 54  GLY B CA  1 
ATOM   1154 C C   . GLY B 1 55 ? 27.060  -21.423 -35.304 1.00 27.37  ? 54  GLY B C   1 
ATOM   1155 O O   . GLY B 1 55 ? 25.873  -21.318 -35.010 1.00 29.46  ? 54  GLY B O   1 
ATOM   1156 N N   . PRO B 1 56 ? 27.426  -21.617 -36.596 1.00 28.99  ? 55  PRO B N   1 
ATOM   1157 C CA  . PRO B 1 56 ? 26.437  -21.730 -37.672 1.00 28.10  ? 55  PRO B CA  1 
ATOM   1158 C C   . PRO B 1 56 ? 25.276  -22.709 -37.553 1.00 26.55  ? 55  PRO B C   1 
ATOM   1159 O O   . PRO B 1 56 ? 24.218  -22.439 -38.102 1.00 26.05  ? 55  PRO B O   1 
ATOM   1160 C CB  . PRO B 1 56 ? 27.293  -22.052 -38.945 1.00 30.17  ? 55  PRO B CB  1 
ATOM   1161 C CG  . PRO B 1 56 ? 28.726  -21.938 -38.546 1.00 37.03  ? 55  PRO B CG  1 
ATOM   1162 C CD  . PRO B 1 56 ? 28.817  -21.696 -37.068 1.00 31.97  ? 55  PRO B CD  1 
ATOM   1163 N N   . LYS B 1 57 ? 25.459  -23.839 -36.850 1.00 25.82  ? 56  LYS B N   1 
ATOM   1164 C CA  . LYS B 1 57 ? 24.360  -24.795 -36.757 1.00 27.37  ? 56  LYS B CA  1 
ATOM   1165 C C   . LYS B 1 57 ? 23.151  -24.191 -36.042 1.00 28.70  ? 56  LYS B C   1 
ATOM   1166 O O   . LYS B 1 57 ? 22.037  -24.665 -36.216 1.00 29.38  ? 56  LYS B O   1 
ATOM   1167 C CB  . LYS B 1 57 ? 24.842  -26.055 -36.024 1.00 35.54  ? 56  LYS B CB  1 
ATOM   1168 C CG  . LYS B 1 57 ? 25.020  -25.956 -34.519 1.00 43.53  ? 56  LYS B CG  1 
ATOM   1169 C CD  . LYS B 1 57 ? 25.164  -27.350 -33.908 1.00 49.31  ? 56  LYS B CD  1 
ATOM   1170 C CE  . LYS B 1 57 ? 25.359  -27.361 -32.420 1.00 50.05  ? 56  LYS B CE  1 
ATOM   1171 N NZ  . LYS B 1 57 ? 24.196  -26.898 -31.659 1.00 53.53  ? 56  LYS B NZ  1 
ATOM   1172 N N   . ASP B 1 58 ? 23.374  -23.086 -35.303 1.00 25.13  ? 57  ASP B N   1 
ATOM   1173 C CA  . ASP B 1 58 ? 22.303  -22.493 -34.514 1.00 26.04  ? 57  ASP B CA  1 
ATOM   1174 C C   . ASP B 1 58 ? 21.852  -21.164 -35.120 1.00 27.18  ? 57  ASP B C   1 
ATOM   1175 O O   . ASP B 1 58 ? 21.100  -20.426 -34.461 1.00 27.01  ? 57  ASP B O   1 
ATOM   1176 C CB  . ASP B 1 58 ? 22.786  -22.318 -33.090 1.00 27.37  ? 57  ASP B CB  1 
ATOM   1177 C CG  . ASP B 1 58 ? 22.981  -23.632 -32.333 1.00 31.85  ? 57  ASP B CG  1 
ATOM   1178 O OD1 . ASP B 1 58 ? 22.064  -24.513 -32.431 1.00 34.16  ? 57  ASP B OD1 1 
ATOM   1179 O OD2 . ASP B 1 58 ? 23.997  -23.718 -31.610 1.00 33.84  ? 57  ASP B OD2 1 
ATOM   1180 N N   . LEU B 1 59 ? 22.348  -20.844 -36.335 1.00 26.54  ? 58  LEU B N   1 
ATOM   1181 C CA  . LEU B 1 59 ? 22.034  -19.548 -36.953 1.00 25.61  ? 58  LEU B CA  1 
ATOM   1182 C C   . LEU B 1 59 ? 21.272  -19.773 -38.253 1.00 25.29  ? 58  LEU B C   1 
ATOM   1183 O O   . LEU B 1 59 ? 21.755  -20.432 -39.180 1.00 28.14  ? 58  LEU B O   1 
ATOM   1184 C CB  . LEU B 1 59 ? 23.350  -18.797 -37.176 1.00 25.66  ? 58  LEU B CB  1 
ATOM   1185 C CG  . LEU B 1 59 ? 24.177  -18.525 -35.916 1.00 25.14  ? 58  LEU B CG  1 
ATOM   1186 C CD1 . LEU B 1 59 ? 25.472  -17.809 -36.320 1.00 27.44  ? 58  LEU B CD1 1 
ATOM   1187 C CD2 . LEU B 1 59 ? 23.392  -17.608 -34.899 1.00 26.15  ? 58  LEU B CD2 1 
ATOM   1188 N N   . PHE B 1 60 ? 20.097  -19.162 -38.332 1.00 22.99  ? 59  PHE B N   1 
ATOM   1189 C CA  . PHE B 1 60 ? 19.161  -19.330 -39.427 1.00 25.05  ? 59  PHE B CA  1 
ATOM   1190 C C   . PHE B 1 60 ? 18.929  -17.975 -40.090 1.00 26.02  ? 59  PHE B C   1 
ATOM   1191 O O   . PHE B 1 60 ? 18.338  -17.082 -39.490 1.00 25.71  ? 59  PHE B O   1 
ATOM   1192 C CB  . PHE B 1 60 ? 17.835  -19.869 -38.871 1.00 24.70  ? 59  PHE B CB  1 
ATOM   1193 C CG  . PHE B 1 60 ? 17.929  -21.274 -38.286 1.00 25.66  ? 59  PHE B CG  1 
ATOM   1194 C CD1 . PHE B 1 60 ? 18.485  -21.434 -37.019 1.00 26.61  ? 59  PHE B CD1 1 
ATOM   1195 C CD2 . PHE B 1 60 ? 17.469  -22.383 -39.007 1.00 25.89  ? 59  PHE B CD2 1 
ATOM   1196 C CE1 . PHE B 1 60 ? 18.586  -22.699 -36.464 1.00 29.99  ? 59  PHE B CE1 1 
ATOM   1197 C CE2 . PHE B 1 60 ? 17.585  -23.662 -38.443 1.00 27.42  ? 59  PHE B CE2 1 
ATOM   1198 C CZ  . PHE B 1 60 ? 18.158  -23.805 -37.190 1.00 27.87  ? 59  PHE B CZ  1 
ATOM   1199 N N   . PRO B 1 61 ? 19.382  -17.768 -41.348 1.00 28.91  ? 60  PRO B N   1 
ATOM   1200 C CA  . PRO B 1 61 ? 19.165  -16.483 -42.022 1.00 27.03  ? 60  PRO B CA  1 
ATOM   1201 C C   . PRO B 1 61 ? 17.707  -16.021 -41.966 1.00 24.72  ? 60  PRO B C   1 
ATOM   1202 O O   . PRO B 1 61 ? 16.752  -16.756 -42.229 1.00 29.32  ? 60  PRO B O   1 
ATOM   1203 C CB  . PRO B 1 61 ? 19.646  -16.739 -43.465 1.00 31.24  ? 60  PRO B CB  1 
ATOM   1204 C CG  . PRO B 1 61 ? 20.678  -17.816 -43.309 1.00 36.43  ? 60  PRO B CG  1 
ATOM   1205 C CD  . PRO B 1 61 ? 20.119  -18.743 -42.181 1.00 31.83  ? 60  PRO B CD  1 
ATOM   1206 N N   . TYR B 1 62 ? 17.538  -14.715 -41.650 1.00 27.08  ? 61  TYR B N   1 
ATOM   1207 C CA  . TYR B 1 62 ? 16.244  -14.182 -41.313 1.00 28.64  ? 61  TYR B CA  1 
ATOM   1208 C C   . TYR B 1 62 ? 15.240  -14.201 -42.460 1.00 29.46  ? 61  TYR B C   1 
ATOM   1209 O O   . TYR B 1 62 ? 14.128  -14.609 -42.198 1.00 29.48  ? 61  TYR B O   1 
ATOM   1210 C CB  . TYR B 1 62 ? 16.399  -12.763 -40.749 1.00 29.52  ? 61  TYR B CB  1 
ATOM   1211 C CG  . TYR B 1 62 ? 15.088  -12.034 -40.517 1.00 32.46  ? 61  TYR B CG  1 
ATOM   1212 C CD1 . TYR B 1 62 ? 14.303  -12.297 -39.408 1.00 33.07  ? 61  TYR B CD1 1 
ATOM   1213 C CD2 . TYR B 1 62 ? 14.694  -10.998 -41.363 1.00 38.99  ? 61  TYR B CD2 1 
ATOM   1214 C CE1 . TYR B 1 62 ? 13.128  -11.606 -39.183 1.00 34.89  ? 61  TYR B CE1 1 
ATOM   1215 C CE2 . TYR B 1 62 ? 13.534  -10.272 -41.140 1.00 37.46  ? 61  TYR B CE2 1 
ATOM   1216 C CZ  . TYR B 1 62 ? 12.743  -10.593 -40.051 1.00 41.54  ? 61  TYR B CZ  1 
ATOM   1217 O OH  . TYR B 1 62 ? 11.585  -9.923  -39.849 1.00 39.54  ? 61  TYR B OH  1 
ATOM   1218 N N   . ASP B 1 63 ? 15.618  -13.768 -43.683 1.00 32.90  ? 62  ASP B N   1 
ATOM   1219 C CA  . ASP B 1 63 ? 14.682  -13.711 -44.807 1.00 44.62  ? 62  ASP B CA  1 
ATOM   1220 C C   . ASP B 1 63 ? 14.105  -15.092 -45.106 1.00 36.58  ? 62  ASP B C   1 
ATOM   1221 O O   . ASP B 1 63 ? 12.884  -15.269 -45.119 1.00 45.11  ? 62  ASP B O   1 
ATOM   1222 C CB  . ASP B 1 63 ? 15.287  -13.032 -46.028 1.00 51.14  ? 62  ASP B CB  1 
ATOM   1223 C CG  . ASP B 1 63 ? 15.235  -11.510 -46.037 1.00 64.09  ? 62  ASP B CG  1 
ATOM   1224 O OD1 . ASP B 1 63 ? 14.459  -10.928 -45.234 1.00 64.88  ? 62  ASP B OD1 1 
ATOM   1225 O OD2 . ASP B 1 63 ? 15.985  -10.911 -46.842 1.00 71.42  ? 62  ASP B OD2 1 
ATOM   1226 N N   . LYS B 1 64 ? 14.992  -16.061 -45.292 1.00 40.27  ? 63  LYS B N   1 
ATOM   1227 C CA  . LYS B 1 64 ? 14.624  -17.449 -45.523 1.00 39.60  ? 63  LYS B CA  1 
ATOM   1228 C C   . LYS B 1 64 ? 13.696  -17.978 -44.431 1.00 38.34  ? 63  LYS B C   1 
ATOM   1229 O O   . LYS B 1 64 ? 12.782  -18.746 -44.730 1.00 42.12  ? 63  LYS B O   1 
ATOM   1230 C CB  . LYS B 1 64 ? 15.887  -18.320 -45.565 1.00 44.63  ? 63  LYS B CB  1 
ATOM   1231 C CG  . LYS B 1 64 ? 15.603  -19.809 -45.752 1.00 46.37  ? 63  LYS B CG  1 
ATOM   1232 C CD  . LYS B 1 64 ? 16.854  -20.632 -46.032 1.00 48.76  ? 63  LYS B CD  1 
ATOM   1233 C CE  . LYS B 1 64 ? 16.536  -21.909 -46.779 1.00 46.37  ? 63  LYS B CE  1 
ATOM   1234 N NZ  . LYS B 1 64 ? 15.732  -22.816 -45.958 1.00 47.44  ? 63  LYS B NZ  1 
ATOM   1235 N N   . SER B 1 65 ? 13.900  -17.559 -43.174 1.00 31.91  ? 64  SER B N   1 
ATOM   1236 C CA  . SER B 1 65 ? 13.289  -18.310 -42.071 1.00 37.41  ? 64  SER B CA  1 
ATOM   1237 C C   . SER B 1 65 ? 12.167  -17.566 -41.338 1.00 37.20  ? 64  SER B C   1 
ATOM   1238 O O   . SER B 1 65 ? 11.499  -18.151 -40.492 1.00 36.42  ? 64  SER B O   1 
ATOM   1239 C CB  . SER B 1 65 ? 14.344  -18.855 -41.148 1.00 39.01  ? 64  SER B CB  1 
ATOM   1240 O OG  . SER B 1 65 ? 15.199  -17.809 -40.718 1.00 55.10  ? 64  SER B OG  1 
ATOM   1241 N N   . LYS B 1 66 ? 11.851  -16.322 -41.731 1.00 35.91  ? 65  LYS B N   1 
ATOM   1242 C CA  . LYS B 1 66 ? 10.918  -15.539 -40.921 1.00 33.95  ? 65  LYS B CA  1 
ATOM   1243 C C   . LYS B 1 66 ? 9.485   -16.074 -40.923 1.00 39.29  ? 65  LYS B C   1 
ATOM   1244 O O   . LYS B 1 66 ? 8.758   -15.950 -39.930 1.00 39.22  ? 65  LYS B O   1 
ATOM   1245 C CB  . LYS B 1 66 ? 10.966  -14.056 -41.308 1.00 34.85  ? 65  LYS B CB  1 
ATOM   1246 C CG  . LYS B 1 66 ? 10.534  -13.755 -42.745 1.00 39.82  ? 65  LYS B CG  1 
ATOM   1247 C CD  . LYS B 1 66 ? 10.625  -12.263 -43.074 1.00 52.09  ? 65  LYS B CD  1 
ATOM   1248 C CE  . LYS B 1 66 ? 10.517  -11.982 -44.551 1.00 56.96  ? 65  LYS B CE  1 
ATOM   1249 N NZ  . LYS B 1 66 ? 9.403   -12.677 -45.212 1.00 62.61  ? 65  LYS B NZ  1 
ATOM   1250 N N   . ASP B 1 67 ? 9.029   -16.655 -42.031 1.00 40.22  ? 66  ASP B N   1 
ATOM   1251 C CA  . ASP B 1 67 ? 7.634   -17.063 -42.021 1.00 45.57  ? 66  ASP B CA  1 
ATOM   1252 C C   . ASP B 1 67 ? 7.446   -18.227 -41.040 1.00 46.60  ? 66  ASP B C   1 
ATOM   1253 O O   . ASP B 1 67 ? 6.407   -18.337 -40.388 1.00 50.30  ? 66  ASP B O   1 
ATOM   1254 C CB  . ASP B 1 67 ? 7.065   -17.192 -43.426 1.00 54.33  ? 66  ASP B CB  1 
ATOM   1255 C CG  . ASP B 1 67 ? 7.438   -18.451 -44.190 1.00 68.79  ? 66  ASP B CG  1 
ATOM   1256 O OD1 . ASP B 1 67 ? 8.118   -18.318 -45.229 1.00 85.74  ? 66  ASP B OD1 1 
ATOM   1257 O OD2 . ASP B 1 67 ? 7.013   -19.551 -43.763 1.00 83.83  ? 66  ASP B OD2 1 
ATOM   1258 N N   . LYS B 1 68 ? 8.482   -19.064 -40.913 1.00 42.65  ? 67  LYS B N   1 
ATOM   1259 C CA  . LYS B 1 68 ? 8.470   -20.205 -40.008 1.00 39.77  ? 67  LYS B CA  1 
ATOM   1260 C C   . LYS B 1 68 ? 8.678   -19.805 -38.544 1.00 36.73  ? 67  LYS B C   1 
ATOM   1261 O O   . LYS B 1 68 ? 7.922   -20.247 -37.682 1.00 38.21  ? 67  LYS B O   1 
ATOM   1262 C CB  . LYS B 1 68 ? 9.552   -21.190 -40.462 1.00 37.84  ? 67  LYS B CB  1 
ATOM   1263 C CG  . LYS B 1 68 ? 9.700   -22.439 -39.615 1.00 44.79  ? 67  LYS B CG  1 
ATOM   1264 C CD  . LYS B 1 68 ? 10.657  -23.402 -40.314 1.00 55.63  ? 67  LYS B CD  1 
ATOM   1265 C CE  . LYS B 1 68 ? 10.847  -24.684 -39.548 1.00 52.29  ? 67  LYS B CE  1 
ATOM   1266 N NZ  . LYS B 1 68 ? 9.591   -25.428 -39.385 1.00 55.37  ? 67  LYS B NZ  1 
ATOM   1267 N N   . TYR B 1 69 ? 9.694   -18.983 -38.250 1.00 33.12  ? 68  TYR B N   1 
ATOM   1268 C CA  . TYR B 1 69 ? 10.094  -18.712 -36.873 1.00 28.98  ? 68  TYR B CA  1 
ATOM   1269 C C   . TYR B 1 69 ? 9.633   -17.336 -36.388 1.00 32.89  ? 68  TYR B C   1 
ATOM   1270 O O   . TYR B 1 69 ? 9.785   -17.033 -35.204 1.00 37.29  ? 68  TYR B O   1 
ATOM   1271 C CB  . TYR B 1 69 ? 11.610  -18.746 -36.697 1.00 30.05  ? 68  TYR B CB  1 
ATOM   1272 C CG  . TYR B 1 69 ? 12.254  -20.101 -36.960 1.00 31.30  ? 68  TYR B CG  1 
ATOM   1273 C CD1 . TYR B 1 69 ? 11.716  -21.277 -36.450 1.00 31.43  ? 68  TYR B CD1 1 
ATOM   1274 C CD2 . TYR B 1 69 ? 13.365  -20.191 -37.791 1.00 33.61  ? 68  TYR B CD2 1 
ATOM   1275 C CE1 . TYR B 1 69 ? 12.299  -22.507 -36.732 1.00 33.54  ? 68  TYR B CE1 1 
ATOM   1276 C CE2 . TYR B 1 69 ? 13.935  -21.416 -38.110 1.00 33.97  ? 68  TYR B CE2 1 
ATOM   1277 C CZ  . TYR B 1 69 ? 13.421  -22.572 -37.536 1.00 34.71  ? 68  TYR B CZ  1 
ATOM   1278 O OH  . TYR B 1 69 ? 13.996  -23.769 -37.844 1.00 35.05  ? 68  TYR B OH  1 
ATOM   1279 N N   . GLY B 1 70 ? 9.142   -16.482 -37.296 1.00 36.82  ? 69  GLY B N   1 
ATOM   1280 C CA  . GLY B 1 70 ? 8.866   -15.094 -36.940 1.00 40.12  ? 69  GLY B CA  1 
ATOM   1281 C C   . GLY B 1 70 ? 7.451   -14.856 -36.400 1.00 44.70  ? 69  GLY B C   1 
ATOM   1282 O O   . GLY B 1 70 ? 6.840   -13.832 -36.724 1.00 44.06  ? 69  GLY B O   1 
ATOM   1283 N N   . LYS B 1 71 ? 6.934   -15.788 -35.582 1.00 43.62  ? 70  LYS B N   1 
ATOM   1284 C CA  . LYS B 1 71 ? 5.575   -15.686 -35.068 1.00 44.60  ? 70  LYS B CA  1 
ATOM   1285 C C   . LYS B 1 71 ? 5.626   -15.269 -33.609 1.00 48.86  ? 70  LYS B C   1 
ATOM   1286 O O   . LYS B 1 71 ? 6.498   -15.728 -32.871 1.00 39.62  ? 70  LYS B O   1 
ATOM   1287 C CB  . LYS B 1 71 ? 4.822   -17.021 -35.016 1.00 47.73  ? 70  LYS B CB  1 
ATOM   1288 C CG  . LYS B 1 71 ? 3.841   -17.262 -36.148 1.00 57.56  ? 70  LYS B CG  1 
ATOM   1289 C CD  . LYS B 1 71 ? 4.522   -17.602 -37.466 1.00 55.92  ? 70  LYS B CD  1 
ATOM   1290 C CE  . LYS B 1 71 ? 3.566   -18.142 -38.483 1.00 63.58  ? 70  LYS B CE  1 
ATOM   1291 N NZ  . LYS B 1 71 ? 4.218   -18.250 -39.788 1.00 65.93  ? 70  LYS B NZ  1 
ATOM   1292 N N   . PRO B 1 72 ? 4.700   -14.403 -33.135 1.00 46.38  ? 71  PRO B N   1 
ATOM   1293 C CA  . PRO B 1 72 ? 4.628   -14.107 -31.704 1.00 45.50  ? 71  PRO B CA  1 
ATOM   1294 C C   . PRO B 1 72 ? 4.466   -15.337 -30.812 1.00 40.93  ? 71  PRO B C   1 
ATOM   1295 O O   . PRO B 1 72 ? 3.866   -16.341 -31.206 1.00 42.46  ? 71  PRO B O   1 
ATOM   1296 C CB  . PRO B 1 72 ? 3.468   -13.104 -31.588 1.00 45.36  ? 71  PRO B CB  1 
ATOM   1297 C CG  . PRO B 1 72 ? 3.472   -12.438 -32.944 1.00 47.02  ? 71  PRO B CG  1 
ATOM   1298 C CD  . PRO B 1 72 ? 3.800   -13.560 -33.943 1.00 44.32  ? 71  PRO B CD  1 
ATOM   1299 N N   . ASN B 1 73 ? 5.064   -15.240 -29.619 1.00 42.11  ? 72  ASN B N   1 
ATOM   1300 C CA  . ASN B 1 73 ? 4.881   -16.216 -28.555 1.00 37.79  ? 72  ASN B CA  1 
ATOM   1301 C C   . ASN B 1 73 ? 4.838   -15.471 -27.210 1.00 43.06  ? 72  ASN B C   1 
ATOM   1302 O O   . ASN B 1 73 ? 4.852   -14.231 -27.169 1.00 48.41  ? 72  ASN B O   1 
ATOM   1303 C CB  . ASN B 1 73 ? 5.920   -17.333 -28.591 1.00 40.54  ? 72  ASN B CB  1 
ATOM   1304 C CG  . ASN B 1 73 ? 7.323   -16.851 -28.289 1.00 36.12  ? 72  ASN B CG  1 
ATOM   1305 O OD1 . ASN B 1 73 ? 7.531   -16.114 -27.316 1.00 34.82  ? 72  ASN B OD1 1 
ATOM   1306 N ND2 . ASN B 1 73 ? 8.298   -17.199 -29.132 1.00 30.54  ? 72  ASN B ND2 1 
ATOM   1307 N N   . LYS B 1 74 ? 4.840   -16.239 -26.116 1.00 41.41  ? 73  LYS B N   1 
ATOM   1308 C CA  . LYS B 1 74 ? 4.712   -15.682 -24.772 1.00 43.92  ? 73  LYS B CA  1 
ATOM   1309 C C   . LYS B 1 74 ? 6.043   -15.623 -24.007 1.00 45.51  ? 73  LYS B C   1 
ATOM   1310 O O   . LYS B 1 74 ? 6.046   -15.469 -22.780 1.00 43.72  ? 73  LYS B O   1 
ATOM   1311 C CB  . LYS B 1 74 ? 3.594   -16.421 -24.012 1.00 42.64  ? 73  LYS B CB  1 
ATOM   1312 N N   . ARG B 1 75 ? 7.188   -15.754 -24.702 1.00 33.34  ? 74  ARG B N   1 
ATOM   1313 C CA  . ARG B 1 75 ? 8.466   -15.606 -24.017 1.00 32.19  ? 74  ARG B CA  1 
ATOM   1314 C C   . ARG B 1 75 ? 8.773   -14.116 -23.835 1.00 31.87  ? 74  ARG B C   1 
ATOM   1315 O O   . ARG B 1 75 ? 8.561   -13.294 -24.735 1.00 32.94  ? 74  ARG B O   1 
ATOM   1316 C CB  . ARG B 1 75 ? 9.610   -16.358 -24.708 1.00 30.53  ? 74  ARG B CB  1 
ATOM   1317 C CG  . ARG B 1 75 ? 9.435   -17.862 -24.923 1.00 31.35  ? 74  ARG B CG  1 
ATOM   1318 C CD  . ARG B 1 75 ? 9.315   -18.663 -23.624 1.00 35.02  ? 74  ARG B CD  1 
ATOM   1319 N NE  . ARG B 1 75 ? 9.550   -20.098 -23.832 1.00 30.64  ? 74  ARG B NE  1 
ATOM   1320 C CZ  . ARG B 1 75 ? 10.699  -20.711 -23.609 1.00 33.58  ? 74  ARG B CZ  1 
ATOM   1321 N NH1 . ARG B 1 75 ? 11.740  -20.035 -23.118 1.00 35.42  ? 74  ARG B NH1 1 
ATOM   1322 N NH2 . ARG B 1 75 ? 10.827  -21.988 -23.945 1.00 37.99  ? 74  ARG B NH2 1 
ATOM   1323 N N   . LYS B 1 76 ? 9.267   -13.765 -22.640 1.00 31.63  ? 75  LYS B N   1 
ATOM   1324 C CA  . LYS B 1 76 ? 9.620   -12.390 -22.306 1.00 27.34  ? 75  LYS B CA  1 
ATOM   1325 C C   . LYS B 1 76 ? 10.690  -11.838 -23.262 1.00 28.52  ? 75  LYS B C   1 
ATOM   1326 O O   . LYS B 1 76 ? 11.789  -12.416 -23.344 1.00 28.76  ? 75  LYS B O   1 
ATOM   1327 C CB  . LYS B 1 76 ? 10.136  -12.271 -20.865 1.00 29.89  ? 75  LYS B CB  1 
ATOM   1328 C CG  . LYS B 1 76 ? 10.449  -10.822 -20.523 1.00 30.80  ? 75  LYS B CG  1 
ATOM   1329 C CD  . LYS B 1 76 ? 10.895  -10.659 -19.074 1.00 33.19  ? 75  LYS B CD  1 
ATOM   1330 C CE  . LYS B 1 76 ? 11.023  -9.195  -18.720 1.00 38.06  ? 75  LYS B CE  1 
ATOM   1331 N NZ  . LYS B 1 76 ? 11.479  -9.023  -17.332 1.00 47.01  ? 75  LYS B NZ  1 
ATOM   1332 N N   . GLY B 1 77 ? 10.312  -10.748 -23.949 1.00 28.66  ? 76  GLY B N   1 
ATOM   1333 C CA  . GLY B 1 77 ? 11.212  -10.024 -24.864 1.00 27.60  ? 76  GLY B CA  1 
ATOM   1334 C C   . GLY B 1 77 ? 11.038  -10.428 -26.333 1.00 32.04  ? 76  GLY B C   1 
ATOM   1335 O O   . GLY B 1 77 ? 11.589  -9.796  -27.237 1.00 30.17  ? 76  GLY B O   1 
ATOM   1336 N N   . PHE B 1 78 ? 10.313  -11.512 -26.598 1.00 27.85  ? 77  PHE B N   1 
ATOM   1337 C CA  . PHE B 1 78 ? 10.237  -12.031 -27.962 1.00 26.88  ? 77  PHE B CA  1 
ATOM   1338 C C   . PHE B 1 78 ? 9.495   -11.073 -28.895 1.00 30.03  ? 77  PHE B C   1 
ATOM   1339 O O   . PHE B 1 78 ? 9.964   -10.782 -29.999 1.00 28.63  ? 77  PHE B O   1 
ATOM   1340 C CB  . PHE B 1 78 ? 9.480   -13.365 -27.997 1.00 28.56  ? 77  PHE B CB  1 
ATOM   1341 C CG  . PHE B 1 78 ? 9.724   -14.103 -29.301 1.00 28.15  ? 77  PHE B CG  1 
ATOM   1342 C CD1 . PHE B 1 78 ? 10.837  -14.935 -29.438 1.00 27.12  ? 77  PHE B CD1 1 
ATOM   1343 C CD2 . PHE B 1 78 ? 8.838   -13.970 -30.361 1.00 29.70  ? 77  PHE B CD2 1 
ATOM   1344 C CE1 . PHE B 1 78 ? 11.056  -15.612 -30.651 1.00 26.99  ? 77  PHE B CE1 1 
ATOM   1345 C CE2 . PHE B 1 78 ? 9.058   -14.658 -31.560 1.00 29.70  ? 77  PHE B CE2 1 
ATOM   1346 C CZ  . PHE B 1 78 ? 10.164  -15.482 -31.677 1.00 28.02  ? 77  PHE B CZ  1 
ATOM   1347 N N   . ASN B 1 79 ? 8.312   -10.582 -28.506 1.00 29.23  ? 78  ASN B N   1 
ATOM   1348 C CA  . ASN B 1 79 ? 7.523   -9.762  -29.423 1.00 32.57  ? 78  ASN B CA  1 
ATOM   1349 C C   . ASN B 1 79 ? 8.215   -8.413  -29.655 1.00 32.00  ? 78  ASN B C   1 
ATOM   1350 O O   . ASN B 1 79 ? 8.152   -7.861  -30.767 1.00 31.29  ? 78  ASN B O   1 
ATOM   1351 C CB  . ASN B 1 79 ? 6.051   -9.651  -29.004 1.00 36.34  ? 78  ASN B CB  1 
ATOM   1352 C CG  . ASN B 1 79 ? 5.281   -10.958 -29.042 1.00 41.74  ? 78  ASN B CG  1 
ATOM   1353 O OD1 . ASN B 1 79 ? 5.708   -11.942 -29.655 1.00 39.92  ? 78  ASN B OD1 1 
ATOM   1354 N ND2 . ASN B 1 79 ? 4.137   -11.019 -28.374 1.00 44.67  ? 78  ASN B ND2 1 
ATOM   1355 N N   . GLU B 1 80 ? 8.918   -7.914  -28.636 1.00 29.59  ? 79  GLU B N   1 
ATOM   1356 C CA  . GLU B 1 80 ? 9.673   -6.687  -28.806 1.00 31.55  ? 79  GLU B CA  1 
ATOM   1357 C C   . GLU B 1 80 ? 10.828  -6.943  -29.777 1.00 31.28  ? 79  GLU B C   1 
ATOM   1358 O O   . GLU B 1 80 ? 11.179  -6.039  -30.559 1.00 31.00  ? 79  GLU B O   1 
ATOM   1359 C CB  . GLU B 1 80 ? 10.255  -6.185  -27.490 1.00 29.97  ? 79  GLU B CB  1 
ATOM   1360 C CG  . GLU B 1 80 ? 9.207   -5.560  -26.571 1.00 41.43  ? 79  GLU B CG  1 
ATOM   1361 N N   . GLY B 1 81 ? 11.413  -8.159  -29.692 1.00 28.41  ? 80  GLY B N   1 
ATOM   1362 C CA  . GLY B 1 81 ? 12.523  -8.545  -30.565 1.00 31.94  ? 80  GLY B CA  1 
ATOM   1363 C C   . GLY B 1 81 ? 12.062  -8.615  -32.017 1.00 28.09  ? 80  GLY B C   1 
ATOM   1364 O O   . GLY B 1 81 ? 12.802  -8.228  -32.950 1.00 27.96  ? 80  GLY B O   1 
ATOM   1365 N N   . LEU B 1 82 ? 10.851  -9.115  -32.225 1.00 27.15  ? 81  LEU B N   1 
ATOM   1366 C CA  . LEU B 1 82 ? 10.241  -9.117  -33.549 1.00 30.03  ? 81  LEU B CA  1 
ATOM   1367 C C   . LEU B 1 82 ? 10.117  -7.684  -34.069 1.00 28.00  ? 81  LEU B C   1 
ATOM   1368 O O   . LEU B 1 82 ? 10.400  -7.423  -35.235 1.00 29.67  ? 81  LEU B O   1 
ATOM   1369 C CB  . LEU B 1 82 ? 8.894   -9.846  -33.589 1.00 31.83  ? 81  LEU B CB  1 
ATOM   1370 C CG  . LEU B 1 82 ? 8.926   -11.367 -33.378 1.00 31.17  ? 81  LEU B CG  1 
ATOM   1371 C CD1 . LEU B 1 82 ? 7.525   -11.964 -33.483 1.00 31.87  ? 81  LEU B CD1 1 
ATOM   1372 C CD2 . LEU B 1 82 ? 9.907   -12.046 -34.330 1.00 29.47  ? 81  LEU B CD2 1 
ATOM   1373 N N   . TRP B 1 83 ? 9.690   -6.764  -33.189 1.00 28.42  ? 82  TRP B N   1 
ATOM   1374 C CA  . TRP B 1 83 ? 9.514   -5.358  -33.528 1.00 33.32  ? 82  TRP B CA  1 
ATOM   1375 C C   . TRP B 1 83 ? 10.841  -4.773  -34.014 1.00 32.31  ? 82  TRP B C   1 
ATOM   1376 O O   . TRP B 1 83 ? 10.886  -4.178  -35.097 1.00 31.10  ? 82  TRP B O   1 
ATOM   1377 C CB  . TRP B 1 83 ? 8.982   -4.537  -32.341 1.00 32.75  ? 82  TRP B CB  1 
ATOM   1378 C CG  . TRP B 1 83 ? 8.620   -3.160  -32.837 1.00 30.91  ? 82  TRP B CG  1 
ATOM   1379 C CD1 . TRP B 1 83 ? 7.439   -2.801  -33.411 1.00 37.90  ? 82  TRP B CD1 1 
ATOM   1380 C CD2 . TRP B 1 83 ? 9.506   -2.031  -32.960 1.00 35.68  ? 82  TRP B CD2 1 
ATOM   1381 N NE1 . TRP B 1 83 ? 7.511   -1.502  -33.848 1.00 42.11  ? 82  TRP B NE1 1 
ATOM   1382 C CE2 . TRP B 1 83 ? 8.763   -1.008  -33.591 1.00 37.40  ? 82  TRP B CE2 1 
ATOM   1383 C CE3 . TRP B 1 83 ? 10.835  -1.780  -32.591 1.00 34.86  ? 82  TRP B CE3 1 
ATOM   1384 C CZ2 . TRP B 1 83 ? 9.307   0.252   -33.844 1.00 34.19  ? 82  TRP B CZ2 1 
ATOM   1385 C CZ3 . TRP B 1 83 ? 11.372  -0.534  -32.845 1.00 38.85  ? 82  TRP B CZ3 1 
ATOM   1386 C CH2 . TRP B 1 83 ? 10.613  0.455   -33.480 1.00 32.01  ? 82  TRP B CH2 1 
ATOM   1387 N N   . GLU B 1 84 ? 11.909  -5.020  -33.246 1.00 27.02  ? 83  GLU B N   1 
ATOM   1388 C CA  . GLU B 1 84 ? 13.223  -4.460  -33.506 1.00 28.41  ? 83  GLU B CA  1 
ATOM   1389 C C   . GLU B 1 84 ? 13.819  -4.983  -34.815 1.00 28.81  ? 83  GLU B C   1 
ATOM   1390 O O   . GLU B 1 84 ? 14.386  -4.222  -35.599 1.00 29.28  ? 83  GLU B O   1 
ATOM   1391 C CB  . GLU B 1 84 ? 14.160  -4.779  -32.355 1.00 26.90  ? 83  GLU B CB  1 
ATOM   1392 C CG  . GLU B 1 84 ? 13.763  -4.014  -31.086 1.00 29.59  ? 83  GLU B CG  1 
ATOM   1393 C CD  . GLU B 1 84 ? 14.591  -4.358  -29.874 1.00 31.75  ? 83  GLU B CD  1 
ATOM   1394 O OE1 . GLU B 1 84 ? 15.487  -5.232  -30.025 1.00 29.61  ? 83  GLU B OE1 1 
ATOM   1395 O OE2 . GLU B 1 84 ? 14.363  -3.767  -28.755 1.00 31.49  ? 83  GLU B OE2 1 
ATOM   1396 N N   . ILE B 1 85 ? 13.722  -6.293  -35.044 1.00 27.39  ? 84  ILE B N   1 
ATOM   1397 C CA  . ILE B 1 85 ? 14.352  -6.877  -36.236 1.00 27.10  ? 84  ILE B CA  1 
ATOM   1398 C C   . ILE B 1 85 ? 13.693  -6.347  -37.512 1.00 26.57  ? 84  ILE B C   1 
ATOM   1399 O O   . ILE B 1 85 ? 14.375  -6.148  -38.534 1.00 27.76  ? 84  ILE B O   1 
ATOM   1400 C CB  . ILE B 1 85 ? 14.438  -8.415  -36.193 1.00 24.86  ? 84  ILE B CB  1 
ATOM   1401 C CG1 . ILE B 1 85 ? 15.478  -8.933  -37.240 1.00 25.09  ? 84  ILE B CG1 1 
ATOM   1402 C CG2 . ILE B 1 85 ? 13.069  -9.059  -36.403 1.00 27.41  ? 84  ILE B CG2 1 
ATOM   1403 C CD1 . ILE B 1 85 ? 16.016  -10.335 -36.916 1.00 26.14  ? 84  ILE B CD1 1 
ATOM   1404 N N   . GLN B 1 86 ? 12.391  -6.076  -37.416 1.00 28.47  ? 85  GLN B N   1 
ATOM   1405 C CA  . GLN B 1 86 ? 11.585  -5.535  -38.506 1.00 29.96  ? 85  GLN B CA  1 
ATOM   1406 C C   . GLN B 1 86 ? 11.836  -4.036  -38.723 1.00 33.90  ? 85  GLN B C   1 
ATOM   1407 O O   . GLN B 1 86 ? 11.885  -3.565  -39.860 1.00 36.11  ? 85  GLN B O   1 
ATOM   1408 C CB  . GLN B 1 86 ? 10.121  -5.826  -38.191 1.00 35.03  ? 85  GLN B CB  1 
ATOM   1409 N N   . ASN B 1 87 ? 11.967  -3.266  -37.652 1.00 29.33  ? 86  ASN B N   1 
ATOM   1410 C CA  . ASN B 1 87 ? 11.814  -1.820  -37.820 1.00 28.38  ? 86  ASN B CA  1 
ATOM   1411 C C   . ASN B 1 87 ? 13.107  -1.047  -37.618 1.00 29.34  ? 86  ASN B C   1 
ATOM   1412 O O   . ASN B 1 87 ? 13.225  0.073   -38.142 1.00 30.23  ? 86  ASN B O   1 
ATOM   1413 C CB  . ASN B 1 87 ? 10.858  -1.236  -36.782 1.00 33.59  ? 86  ASN B CB  1 
ATOM   1414 C CG  . ASN B 1 87 ? 9.466   -1.708  -37.087 1.00 40.20  ? 86  ASN B CG  1 
ATOM   1415 O OD1 . ASN B 1 87 ? 8.844   -1.192  -38.019 1.00 47.72  ? 86  ASN B OD1 1 
ATOM   1416 N ND2 . ASN B 1 87 ? 9.011   -2.741  -36.393 1.00 44.80  ? 86  ASN B ND2 1 
ATOM   1417 N N   . ASN B 1 88 ? 14.079  -1.584  -36.878 1.00 29.97  ? 87  ASN B N   1 
ATOM   1418 C CA  . ASN B 1 88 ? 15.362  -0.909  -36.689 1.00 29.47  ? 87  ASN B CA  1 
ATOM   1419 C C   . ASN B 1 88 ? 16.427  -1.911  -36.253 1.00 31.65  ? 87  ASN B C   1 
ATOM   1420 O O   . ASN B 1 88 ? 17.017  -1.865  -35.159 1.00 28.79  ? 87  ASN B O   1 
ATOM   1421 C CB  . ASN B 1 88 ? 15.245  0.318   -35.780 1.00 35.92  ? 87  ASN B CB  1 
ATOM   1422 C CG  . ASN B 1 88 ? 16.408  1.287   -35.895 1.00 29.26  ? 87  ASN B CG  1 
ATOM   1423 O OD1 . ASN B 1 88 ? 17.412  1.064   -36.587 1.00 33.69  ? 87  ASN B OD1 1 
ATOM   1424 N ND2 . ASN B 1 88 ? 16.290  2.406   -35.194 1.00 38.35  ? 87  ASN B ND2 1 
ATOM   1425 N N   . PRO B 1 89 ? 16.729  -2.885  -37.148 1.00 29.91  ? 88  PRO B N   1 
ATOM   1426 C CA  . PRO B 1 89 ? 17.673  -3.944  -36.798 1.00 26.63  ? 88  PRO B CA  1 
ATOM   1427 C C   . PRO B 1 89 ? 19.102  -3.495  -36.540 1.00 25.40  ? 88  PRO B C   1 
ATOM   1428 O O   . PRO B 1 89 ? 19.901  -4.242  -35.964 1.00 26.02  ? 88  PRO B O   1 
ATOM   1429 C CB  . PRO B 1 89 ? 17.563  -4.894  -38.024 1.00 26.87  ? 88  PRO B CB  1 
ATOM   1430 C CG  . PRO B 1 89 ? 17.097  -4.000  -39.183 1.00 24.25  ? 88  PRO B CG  1 
ATOM   1431 C CD  . PRO B 1 89 ? 16.123  -3.054  -38.483 1.00 28.84  ? 88  PRO B CD  1 
ATOM   1432 N N   . HIS B 1 90 ? 19.464  -2.282  -37.049 1.00 25.60  ? 89  HIS B N   1 
ATOM   1433 C CA  . HIS B 1 90 ? 20.863  -1.915  -36.988 1.00 26.74  ? 89  HIS B CA  1 
ATOM   1434 C C   . HIS B 1 90 ? 21.163  -0.855  -35.922 1.00 29.29  ? 89  HIS B C   1 
ATOM   1435 O O   . HIS B 1 90 ? 22.321  -0.420  -35.832 1.00 29.08  ? 89  HIS B O   1 
ATOM   1436 C CB  . HIS B 1 90 ? 21.365  -1.488  -38.377 1.00 27.42  ? 89  HIS B CB  1 
ATOM   1437 C CG  . HIS B 1 90 ? 21.183  -2.556  -39.415 1.00 29.16  ? 89  HIS B CG  1 
ATOM   1438 N ND1 . HIS B 1 90 ? 21.795  -3.787  -39.313 1.00 25.91  ? 89  HIS B ND1 1 
ATOM   1439 C CD2 . HIS B 1 90 ? 20.511  -2.565  -40.568 1.00 26.85  ? 89  HIS B CD2 1 
ATOM   1440 C CE1 . HIS B 1 90 ? 21.457  -4.518  -40.351 1.00 25.43  ? 89  HIS B CE1 1 
ATOM   1441 N NE2 . HIS B 1 90 ? 20.693  -3.792  -41.143 1.00 27.78  ? 89  HIS B NE2 1 
ATOM   1442 N N   . ALA B 1 91 ? 20.144  -0.527  -35.113 1.00 27.84  ? 90  ALA B N   1 
ATOM   1443 C CA  . ALA B 1 91 ? 20.273  0.473   -34.049 1.00 29.40  ? 90  ALA B CA  1 
ATOM   1444 C C   . ALA B 1 91 ? 21.267  0.075   -32.958 1.00 35.25  ? 90  ALA B C   1 
ATOM   1445 O O   . ALA B 1 91 ? 21.545  -1.100  -32.699 1.00 31.08  ? 90  ALA B O   1 
ATOM   1446 C CB  . ALA B 1 91 ? 18.916  0.828   -33.469 1.00 30.00  ? 90  ALA B CB  1 
ATOM   1447 N N   . SER B 1 92 ? 21.810  1.108   -32.282 1.00 36.63  ? 91  SER B N   1 
ATOM   1448 C CA  . SER B 1 92 ? 22.461  0.947   -30.995 1.00 39.29  ? 91  SER B CA  1 
ATOM   1449 C C   . SER B 1 92 ? 21.404  0.679   -29.928 1.00 40.61  ? 91  SER B C   1 
ATOM   1450 O O   . SER B 1 92 ? 20.458  1.467   -29.771 1.00 44.51  ? 91  SER B O   1 
ATOM   1451 C CB  . SER B 1 92 ? 23.255  2.209   -30.618 1.00 41.62  ? 91  SER B CB  1 
ATOM   1452 O OG  . SER B 1 92 ? 23.696  2.073   -29.280 1.00 46.72  ? 91  SER B OG  1 
ATOM   1453 N N   . TYR B 1 93 ? 21.579  -0.430  -29.206 1.00 40.95  ? 92  TYR B N   1 
ATOM   1454 C CA  . TYR B 1 93 ? 20.697  -0.849  -28.127 1.00 42.76  ? 92  TYR B CA  1 
ATOM   1455 C C   . TYR B 1 93 ? 21.459  -0.737  -26.810 1.00 52.84  ? 92  TYR B C   1 
ATOM   1456 O O   . TYR B 1 93 ? 20.974  -1.205  -25.784 1.00 57.43  ? 92  TYR B O   1 
ATOM   1457 C CB  . TYR B 1 93 ? 20.067  -2.232  -28.348 1.00 34.86  ? 92  TYR B CB  1 
ATOM   1458 C CG  . TYR B 1 93 ? 19.037  -2.151  -29.461 1.00 30.94  ? 92  TYR B CG  1 
ATOM   1459 C CD1 . TYR B 1 93 ? 17.746  -1.709  -29.202 1.00 35.36  ? 92  TYR B CD1 1 
ATOM   1460 C CD2 . TYR B 1 93 ? 19.340  -2.547  -30.773 1.00 35.19  ? 92  TYR B CD2 1 
ATOM   1461 C CE1 . TYR B 1 93 ? 16.798  -1.587  -30.203 1.00 34.93  ? 92  TYR B CE1 1 
ATOM   1462 C CE2 . TYR B 1 93 ? 18.400  -2.387  -31.786 1.00 28.64  ? 92  TYR B CE2 1 
ATOM   1463 C CZ  . TYR B 1 93 ? 17.124  -1.950  -31.496 1.00 32.92  ? 92  TYR B CZ  1 
ATOM   1464 O OH  . TYR B 1 93 ? 16.174  -1.835  -32.460 1.00 32.12  ? 92  TYR B OH  1 
ATOM   1465 N N   . SER B 1 94 ? 22.640  -0.102  -26.881 1.00 62.55  ? 93  SER B N   1 
ATOM   1466 C CA  . SER B 1 94 ? 23.436  0.301   -25.727 1.00 68.79  ? 93  SER B CA  1 
ATOM   1467 C C   . SER B 1 94 ? 22.526  1.007   -24.709 1.00 77.58  ? 93  SER B C   1 
ATOM   1468 O O   . SER B 1 94 ? 22.127  2.157   -25.001 1.00 80.02  ? 93  SER B O   1 
ATOM   1469 C CB  . SER B 1 94 ? 24.578  1.218   -26.134 1.00 66.61  ? 93  SER B CB  1 
ATOM   1470 O OG  . SER B 1 94 ? 25.576  0.529   -26.875 1.00 66.19  ? 93  SER B OG  1 
ATOM   1471 O OXT . SER B 1 94 ? 22.232  0.376   -23.669 1.00 90.63  ? 93  SER B OXT 1 
ATOM   1472 N N   . HIS C 1 4  ? 33.119  -24.219 27.074  1.00 69.15  ? 3   HIS C N   1 
ATOM   1473 C CA  . HIS C 1 4  ? 32.105  -23.179 27.397  1.00 70.34  ? 3   HIS C CA  1 
ATOM   1474 C C   . HIS C 1 4  ? 31.458  -23.514 28.745  1.00 79.60  ? 3   HIS C C   1 
ATOM   1475 O O   . HIS C 1 4  ? 32.109  -24.065 29.634  1.00 75.84  ? 3   HIS C O   1 
ATOM   1476 C CB  . HIS C 1 4  ? 31.152  -22.989 26.208  1.00 67.74  ? 3   HIS C CB  1 
ATOM   1477 N N   . ALA C 1 5  ? 30.174  -23.164 28.893  1.00 78.45  ? 4   ALA C N   1 
ATOM   1478 C CA  . ALA C 1 5  ? 29.396  -23.499 30.074  1.00 69.98  ? 4   ALA C CA  1 
ATOM   1479 C C   . ALA C 1 5  ? 27.911  -23.347 29.770  1.00 78.39  ? 4   ALA C C   1 
ATOM   1480 O O   . ALA C 1 5  ? 27.487  -22.386 29.121  1.00 78.54  ? 4   ALA C O   1 
ATOM   1481 C CB  . ALA C 1 5  ? 29.781  -22.590 31.200  1.00 72.14  ? 4   ALA C CB  1 
ATOM   1482 N N   . PHE C 1 6  ? 27.123  -24.293 30.280  1.00 66.25  ? 5   PHE C N   1 
ATOM   1483 C CA  . PHE C 1 6  ? 25.729  -24.363 29.893  1.00 55.24  ? 5   PHE C CA  1 
ATOM   1484 C C   . PHE C 1 6  ? 24.897  -24.507 31.159  1.00 60.98  ? 5   PHE C C   1 
ATOM   1485 O O   . PHE C 1 6  ? 25.214  -25.336 32.008  1.00 74.27  ? 5   PHE C O   1 
ATOM   1486 C CB  . PHE C 1 6  ? 25.546  -25.530 28.904  1.00 53.62  ? 5   PHE C CB  1 
ATOM   1487 C CG  . PHE C 1 6  ? 26.383  -25.495 27.627  1.00 50.50  ? 5   PHE C CG  1 
ATOM   1488 C CD1 . PHE C 1 6  ? 27.562  -26.228 27.510  1.00 53.19  ? 5   PHE C CD1 1 
ATOM   1489 C CD2 . PHE C 1 6  ? 26.007  -24.710 26.538  1.00 54.73  ? 5   PHE C CD2 1 
ATOM   1490 C CE1 . PHE C 1 6  ? 28.328  -26.192 26.342  1.00 52.56  ? 5   PHE C CE1 1 
ATOM   1491 C CE2 . PHE C 1 6  ? 26.761  -24.696 25.365  1.00 47.68  ? 5   PHE C CE2 1 
ATOM   1492 C CZ  . PHE C 1 6  ? 27.918  -25.424 25.267  1.00 46.57  ? 5   PHE C CZ  1 
ATOM   1493 N N   . LYS C 1 7  ? 23.853  -23.682 31.275  1.00 52.70  ? 6   LYS C N   1 
ATOM   1494 C CA  . LYS C 1 7  ? 22.890  -23.752 32.365  1.00 57.08  ? 6   LYS C CA  1 
ATOM   1495 C C   . LYS C 1 7  ? 21.555  -24.042 31.698  1.00 49.63  ? 6   LYS C C   1 
ATOM   1496 O O   . LYS C 1 7  ? 21.468  -23.883 30.482  1.00 53.56  ? 6   LYS C O   1 
ATOM   1497 C CB  . LYS C 1 7  ? 22.874  -22.431 33.150  1.00 57.81  ? 6   LYS C CB  1 
ATOM   1498 N N   . PRO C 1 8  ? 20.489  -24.498 32.400  1.00 55.45  ? 7   PRO C N   1 
ATOM   1499 C CA  . PRO C 1 8  ? 19.220  -24.762 31.721  1.00 54.79  ? 7   PRO C CA  1 
ATOM   1500 C C   . PRO C 1 8  ? 18.768  -23.544 30.916  1.00 59.08  ? 7   PRO C C   1 
ATOM   1501 O O   . PRO C 1 8  ? 19.100  -22.407 31.258  1.00 60.17  ? 7   PRO C O   1 
ATOM   1502 C CB  . PRO C 1 8  ? 18.255  -25.133 32.850  1.00 57.62  ? 7   PRO C CB  1 
ATOM   1503 C CG  . PRO C 1 8  ? 19.167  -25.675 33.930  1.00 55.64  ? 7   PRO C CG  1 
ATOM   1504 C CD  . PRO C 1 8  ? 20.436  -24.810 33.842  1.00 50.81  ? 7   PRO C CD  1 
ATOM   1505 N N   . GLY C 1 9  ? 18.064  -23.810 29.810  1.00 56.82  ? 8   GLY C N   1 
ATOM   1506 C CA  . GLY C 1 9  ? 17.480  -22.763 28.988  1.00 53.59  ? 8   GLY C CA  1 
ATOM   1507 C C   . GLY C 1 9  ? 18.398  -22.309 27.854  1.00 51.49  ? 8   GLY C C   1 
ATOM   1508 O O   . GLY C 1 9  ? 17.906  -21.738 26.885  1.00 62.01  ? 8   GLY C O   1 
ATOM   1509 N N   . ASP C 1 10 ? 19.709  -22.580 27.960  1.00 44.90  ? 9   ASP C N   1 
ATOM   1510 C CA  . ASP C 1 10 ? 20.661  -22.232 26.923  1.00 39.34  ? 9   ASP C CA  1 
ATOM   1511 C C   . ASP C 1 10 ? 20.313  -22.960 25.610  1.00 43.46  ? 9   ASP C C   1 
ATOM   1512 O O   . ASP C 1 10 ? 19.932  -24.145 25.613  1.00 37.74  ? 9   ASP C O   1 
ATOM   1513 C CB  . ASP C 1 10 ? 22.104  -22.415 27.368  1.00 42.67  ? 9   ASP C CB  1 
ATOM   1514 C CG  . ASP C 1 10 ? 22.548  -21.619 28.598  1.00 53.88  ? 9   ASP C CG  1 
ATOM   1515 O OD1 . ASP C 1 10 ? 21.766  -20.772 29.076  1.00 57.19  ? 9   ASP C OD1 1 
ATOM   1516 O OD2 . ASP C 1 10 ? 23.671  -21.869 29.096  1.00 57.31  ? 9   ASP C OD2 1 
ATOM   1517 N N   . LEU C 1 11 ? 20.452  -22.221 24.496  1.00 42.09  ? 10  LEU C N   1 
ATOM   1518 C CA  . LEU C 1 11 ? 20.114  -22.706 23.161  1.00 37.53  ? 10  LEU C CA  1 
ATOM   1519 C C   . LEU C 1 11 ? 21.358  -23.212 22.434  1.00 38.04  ? 10  LEU C C   1 
ATOM   1520 O O   . LEU C 1 11 ? 22.380  -22.520 22.331  1.00 40.19  ? 10  LEU C O   1 
ATOM   1521 C CB  . LEU C 1 11 ? 19.353  -21.627 22.374  1.00 36.40  ? 10  LEU C CB  1 
ATOM   1522 C CG  . LEU C 1 11 ? 18.037  -21.132 22.986  1.00 36.24  ? 10  LEU C CG  1 
ATOM   1523 C CD1 . LEU C 1 11 ? 17.338  -20.147 22.037  1.00 39.03  ? 10  LEU C CD1 1 
ATOM   1524 C CD2 . LEU C 1 11 ? 17.087  -22.295 23.320  1.00 36.94  ? 10  LEU C CD2 1 
ATOM   1525 N N   . VAL C 1 12 ? 21.270  -24.430 21.853  1.00 33.16  ? 11  VAL C N   1 
ATOM   1526 C CA  . VAL C 1 12 ? 22.468  -25.074 21.340  1.00 33.66  ? 11  VAL C CA  1 
ATOM   1527 C C   . VAL C 1 12 ? 22.135  -25.776 20.013  1.00 30.48  ? 11  VAL C C   1 
ATOM   1528 O O   . VAL C 1 12 ? 20.947  -25.964 19.744  1.00 33.02  ? 11  VAL C O   1 
ATOM   1529 C CB  . VAL C 1 12 ? 23.055  -26.121 22.321  1.00 34.29  ? 11  VAL C CB  1 
ATOM   1530 C CG1 . VAL C 1 12 ? 23.625  -25.475 23.598  1.00 36.64  ? 11  VAL C CG1 1 
ATOM   1531 C CG2 . VAL C 1 12 ? 22.036  -27.213 22.640  1.00 34.52  ? 11  VAL C CG2 1 
ATOM   1532 N N   . PHE C 1 13 ? 23.189  -26.144 19.273  1.00 30.36  ? 12  PHE C N   1 
ATOM   1533 C CA  . PHE C 1 13 ? 23.133  -27.295 18.362  1.00 30.35  ? 12  PHE C CA  1 
ATOM   1534 C C   . PHE C 1 13 ? 23.768  -28.495 19.068  1.00 31.04  ? 12  PHE C C   1 
ATOM   1535 O O   . PHE C 1 13 ? 24.862  -28.388 19.658  1.00 31.11  ? 12  PHE C O   1 
ATOM   1536 C CB  . PHE C 1 13 ? 23.783  -27.081 16.984  1.00 33.15  ? 12  PHE C CB  1 
ATOM   1537 C CG  . PHE C 1 13 ? 22.980  -26.093 16.161  1.00 36.72  ? 12  PHE C CG  1 
ATOM   1538 C CD1 . PHE C 1 13 ? 21.959  -26.538 15.321  1.00 34.50  ? 12  PHE C CD1 1 
ATOM   1539 C CD2 . PHE C 1 13 ? 23.255  -24.728 16.226  1.00 35.73  ? 12  PHE C CD2 1 
ATOM   1540 C CE1 . PHE C 1 13 ? 21.217  -25.630 14.588  1.00 36.33  ? 12  PHE C CE1 1 
ATOM   1541 C CE2 . PHE C 1 13 ? 22.490  -23.823 15.506  1.00 37.31  ? 12  PHE C CE2 1 
ATOM   1542 C CZ  . PHE C 1 13 ? 21.498  -24.285 14.664  1.00 37.13  ? 12  PHE C CZ  1 
ATOM   1543 N N   . ALA C 1 14 ? 23.065  -29.648 19.072  1.00 27.72  ? 13  ALA C N   1 
ATOM   1544 C CA  . ALA C 1 14 ? 23.513  -30.828 19.803  1.00 26.42  ? 13  ALA C CA  1 
ATOM   1545 C C   . ALA C 1 14 ? 23.819  -31.934 18.791  1.00 31.17  ? 13  ALA C C   1 
ATOM   1546 O O   . ALA C 1 14 ? 22.975  -32.178 17.918  1.00 28.97  ? 13  ALA C O   1 
ATOM   1547 C CB  . ALA C 1 14 ? 22.435  -31.267 20.752  1.00 27.28  ? 13  ALA C CB  1 
ATOM   1548 N N   . LYS C 1 15 ? 24.998  -32.564 18.923  1.00 28.13  ? 14  LYS C N   1 
ATOM   1549 C CA  . LYS C 1 15 ? 25.429  -33.563 17.950  1.00 27.89  ? 14  LYS C CA  1 
ATOM   1550 C C   . LYS C 1 15 ? 25.422  -34.952 18.568  1.00 28.40  ? 14  LYS C C   1 
ATOM   1551 O O   . LYS C 1 15 ? 26.151  -35.234 19.530  1.00 31.24  ? 14  LYS C O   1 
ATOM   1552 C CB  . LYS C 1 15 ? 26.843  -33.239 17.431  1.00 29.80  ? 14  LYS C CB  1 
ATOM   1553 C CG  . LYS C 1 15 ? 27.318  -34.239 16.360  1.00 29.52  ? 14  LYS C CG  1 
ATOM   1554 C CD  . LYS C 1 15 ? 26.539  -34.027 15.065  1.00 33.07  ? 14  LYS C CD  1 
ATOM   1555 C CE  . LYS C 1 15 ? 26.967  -34.833 13.863  1.00 35.42  ? 14  LYS C CE  1 
ATOM   1556 N NZ  . LYS C 1 15 ? 26.870  -36.271 14.068  1.00 31.70  ? 14  LYS C NZ  1 
ATOM   1557 N N   . MET C 1 16 ? 24.594  -35.849 18.013  1.00 25.66  ? 15  MET C N   1 
ATOM   1558 C CA  . MET C 1 16 ? 24.645  -37.270 18.354  1.00 26.43  ? 15  MET C CA  1 
ATOM   1559 C C   . MET C 1 16 ? 25.120  -38.066 17.141  1.00 31.93  ? 15  MET C C   1 
ATOM   1560 O O   . MET C 1 16 ? 24.868  -37.703 15.994  1.00 27.89  ? 15  MET C O   1 
ATOM   1561 C CB  . MET C 1 16 ? 23.236  -37.794 18.649  1.00 29.03  ? 15  MET C CB  1 
ATOM   1562 C CG  . MET C 1 16 ? 22.499  -37.031 19.762  1.00 31.08  ? 15  MET C CG  1 
ATOM   1563 S SD  . MET C 1 16 ? 20.935  -37.800 20.222  1.00 37.68  ? 15  MET C SD  1 
ATOM   1564 C CE  . MET C 1 16 ? 19.921  -37.226 18.848  1.00 36.71  ? 15  MET C CE  1 
ATOM   1565 N N   . LYS C 1 17 ? 25.752  -39.214 17.399  1.00 30.16  ? 16  LYS C N   1 
ATOM   1566 C CA  . LYS C 1 17 ? 26.156  -40.057 16.279  1.00 33.66  ? 16  LYS C CA  1 
ATOM   1567 C C   . LYS C 1 17 ? 24.904  -40.443 15.487  1.00 28.72  ? 16  LYS C C   1 
ATOM   1568 O O   . LYS C 1 17 ? 23.912  -40.903 16.053  1.00 31.28  ? 16  LYS C O   1 
ATOM   1569 C CB  . LYS C 1 17 ? 26.812  -41.318 16.848  1.00 33.43  ? 16  LYS C CB  1 
ATOM   1570 C CG  . LYS C 1 17 ? 27.352  -42.314 15.798  1.00 34.79  ? 16  LYS C CG  1 
ATOM   1571 C CD  . LYS C 1 17 ? 28.650  -41.717 15.260  1.00 41.74  ? 16  LYS C CD  1 
ATOM   1572 C CE  . LYS C 1 17 ? 29.484  -42.600 14.382  1.00 50.20  ? 16  LYS C CE  1 
ATOM   1573 N NZ  . LYS C 1 17 ? 30.643  -41.813 13.940  1.00 45.61  ? 16  LYS C NZ  1 
ATOM   1574 N N   . GLY C 1 18 ? 25.010  -40.303 14.167  1.00 33.03  ? 17  GLY C N   1 
ATOM   1575 C CA  . GLY C 1 18 ? 23.948  -40.781 13.289  1.00 32.09  ? 17  GLY C CA  1 
ATOM   1576 C C   . GLY C 1 18 ? 22.965  -39.674 12.928  1.00 30.63  ? 17  GLY C C   1 
ATOM   1577 O O   . GLY C 1 18 ? 21.973  -39.962 12.259  1.00 29.28  ? 17  GLY C O   1 
ATOM   1578 N N   . TYR C 1 19 ? 23.203  -38.442 13.436  1.00 29.40  ? 18  TYR C N   1 
ATOM   1579 C CA  . TYR C 1 19 ? 22.284  -37.319 13.204  1.00 29.66  ? 18  TYR C CA  1 
ATOM   1580 C C   . TYR C 1 19 ? 23.063  -36.046 12.911  1.00 28.51  ? 18  TYR C C   1 
ATOM   1581 O O   . TYR C 1 19 ? 24.148  -35.852 13.439  1.00 28.98  ? 18  TYR C O   1 
ATOM   1582 C CB  . TYR C 1 19 ? 21.424  -37.007 14.440  1.00 25.60  ? 18  TYR C CB  1 
ATOM   1583 C CG  . TYR C 1 19 ? 20.589  -38.207 14.834  1.00 30.12  ? 18  TYR C CG  1 
ATOM   1584 C CD1 . TYR C 1 19 ? 21.119  -39.225 15.626  1.00 29.36  ? 18  TYR C CD1 1 
ATOM   1585 C CD2 . TYR C 1 19 ? 19.287  -38.318 14.379  1.00 30.36  ? 18  TYR C CD2 1 
ATOM   1586 C CE1 . TYR C 1 19 ? 20.358  -40.333 15.967  1.00 29.67  ? 18  TYR C CE1 1 
ATOM   1587 C CE2 . TYR C 1 19 ? 18.515  -39.415 14.730  1.00 33.57  ? 18  TYR C CE2 1 
ATOM   1588 C CZ  . TYR C 1 19 ? 19.051  -40.407 15.529  1.00 33.32  ? 18  TYR C CZ  1 
ATOM   1589 O OH  . TYR C 1 19 ? 18.267  -41.492 15.824  1.00 41.95  ? 18  TYR C OH  1 
ATOM   1590 N N   . PRO C 1 20 ? 22.492  -35.105 12.125  1.00 29.99  ? 19  PRO C N   1 
ATOM   1591 C CA  . PRO C 1 20 ? 23.135  -33.820 11.897  1.00 28.84  ? 19  PRO C CA  1 
ATOM   1592 C C   . PRO C 1 20 ? 23.087  -33.016 13.203  1.00 28.91  ? 19  PRO C C   1 
ATOM   1593 O O   . PRO C 1 20 ? 22.293  -33.311 14.122  1.00 26.57  ? 19  PRO C O   1 
ATOM   1594 C CB  . PRO C 1 20 ? 22.264  -33.168 10.780  1.00 31.84  ? 19  PRO C CB  1 
ATOM   1595 C CG  . PRO C 1 20 ? 20.902  -33.775 11.020  1.00 28.59  ? 19  PRO C CG  1 
ATOM   1596 C CD  . PRO C 1 20 ? 21.160  -35.214 11.480  1.00 28.21  ? 19  PRO C CD  1 
ATOM   1597 N N   . HIS C 1 21 ? 23.911  -31.970 13.254  1.00 29.73  ? 20  HIS C N   1 
ATOM   1598 C CA  . HIS C 1 21 ? 23.855  -31.085 14.421  1.00 28.97  ? 20  HIS C CA  1 
ATOM   1599 C C   . HIS C 1 21 ? 22.439  -30.536 14.548  1.00 31.26  ? 20  HIS C C   1 
ATOM   1600 O O   . HIS C 1 21 ? 21.916  -29.977 13.576  1.00 29.39  ? 20  HIS C O   1 
ATOM   1601 C CB  . HIS C 1 21 ? 24.819  -29.918 14.214  1.00 34.45  ? 20  HIS C CB  1 
ATOM   1602 C CG  . HIS C 1 21 ? 26.253  -30.334 14.229  1.00 32.12  ? 20  HIS C CG  1 
ATOM   1603 N ND1 . HIS C 1 21 ? 26.960  -30.929 13.195  1.00 35.68  ? 20  HIS C ND1 1 
ATOM   1604 C CD2 . HIS C 1 21 ? 27.123  -30.206 15.250  1.00 36.97  ? 20  HIS C CD2 1 
ATOM   1605 C CE1 . HIS C 1 21 ? 28.205  -31.154 13.589  1.00 41.70  ? 20  HIS C CE1 1 
ATOM   1606 N NE2 . HIS C 1 21 ? 28.327  -30.708 14.831  1.00 36.61  ? 20  HIS C NE2 1 
ATOM   1607 N N   . TRP C 1 22 ? 21.829  -30.641 15.756  1.00 27.63  ? 21  TRP C N   1 
ATOM   1608 C CA  . TRP C 1 22 ? 20.387  -30.524 15.828  1.00 27.19  ? 21  TRP C CA  1 
ATOM   1609 C C   . TRP C 1 22 ? 19.981  -29.350 16.722  1.00 26.24  ? 21  TRP C C   1 
ATOM   1610 O O   . TRP C 1 22 ? 20.500  -29.182 17.836  1.00 27.53  ? 21  TRP C O   1 
ATOM   1611 C CB  . TRP C 1 22 ? 19.803  -31.846 16.375  1.00 25.27  ? 21  TRP C CB  1 
ATOM   1612 C CG  . TRP C 1 22 ? 18.338  -32.016 16.048  1.00 25.68  ? 21  TRP C CG  1 
ATOM   1613 C CD1 . TRP C 1 22 ? 17.244  -31.449 16.630  1.00 26.65  ? 21  TRP C CD1 1 
ATOM   1614 C CD2 . TRP C 1 22 ? 17.853  -32.895 15.002  1.00 27.31  ? 21  TRP C CD2 1 
ATOM   1615 N NE1 . TRP C 1 22 ? 16.108  -31.868 15.967  1.00 29.16  ? 21  TRP C NE1 1 
ATOM   1616 C CE2 . TRP C 1 22 ? 16.450  -32.766 14.986  1.00 28.84  ? 21  TRP C CE2 1 
ATOM   1617 C CE3 . TRP C 1 22 ? 18.483  -33.784 14.113  1.00 27.06  ? 21  TRP C CE3 1 
ATOM   1618 C CZ2 . TRP C 1 22 ? 15.666  -33.501 14.088  1.00 26.94  ? 21  TRP C CZ2 1 
ATOM   1619 C CZ3 . TRP C 1 22 ? 17.710  -34.485 13.208  1.00 29.36  ? 21  TRP C CZ3 1 
ATOM   1620 C CH2 . TRP C 1 22 ? 16.317  -34.344 13.213  1.00 27.20  ? 21  TRP C CH2 1 
ATOM   1621 N N   . PRO C 1 23 ? 19.011  -28.495 16.336  1.00 30.01  ? 22  PRO C N   1 
ATOM   1622 C CA  . PRO C 1 23 ? 18.568  -27.447 17.270  1.00 27.01  ? 22  PRO C CA  1 
ATOM   1623 C C   . PRO C 1 23 ? 18.001  -27.987 18.581  1.00 27.22  ? 22  PRO C C   1 
ATOM   1624 O O   . PRO C 1 23 ? 17.112  -28.843 18.573  1.00 27.02  ? 22  PRO C O   1 
ATOM   1625 C CB  . PRO C 1 23 ? 17.513  -26.677 16.428  1.00 28.61  ? 22  PRO C CB  1 
ATOM   1626 C CG  . PRO C 1 23 ? 16.984  -27.732 15.477  1.00 27.41  ? 22  PRO C CG  1 
ATOM   1627 C CD  . PRO C 1 23 ? 18.234  -28.502 15.065  1.00 27.06  ? 22  PRO C CD  1 
ATOM   1628 N N   . ALA C 1 24 ? 18.533  -27.462 19.705  1.00 28.77  ? 23  ALA C N   1 
ATOM   1629 C CA  . ALA C 1 24 ? 18.248  -28.051 21.010  1.00 30.77  ? 23  ALA C CA  1 
ATOM   1630 C C   . ALA C 1 24 ? 18.384  -27.001 22.113  1.00 29.59  ? 23  ALA C C   1 
ATOM   1631 O O   . ALA C 1 24 ? 18.863  -25.881 21.859  1.00 32.19  ? 23  ALA C O   1 
ATOM   1632 C CB  . ALA C 1 24 ? 19.205  -29.239 21.233  1.00 28.98  ? 23  ALA C CB  1 
ATOM   1633 N N   . ARG C 1 25 ? 17.958  -27.376 23.322  1.00 32.90  ? 24  ARG C N   1 
ATOM   1634 C CA  . ARG C 1 25 ? 18.241  -26.572 24.501  1.00 35.26  ? 24  ARG C CA  1 
ATOM   1635 C C   . ARG C 1 25 ? 18.718  -27.460 25.659  1.00 35.25  ? 24  ARG C C   1 
ATOM   1636 O O   . ARG C 1 25 ? 18.411  -28.655 25.684  1.00 35.97  ? 24  ARG C O   1 
ATOM   1637 C CB  . ARG C 1 25 ? 17.007  -25.779 24.938  1.00 33.49  ? 24  ARG C CB  1 
ATOM   1638 C CG  . ARG C 1 25 ? 15.753  -26.541 25.351  1.00 42.42  ? 24  ARG C CG  1 
ATOM   1639 C CD  . ARG C 1 25 ? 14.714  -25.661 26.067  1.00 45.18  ? 24  ARG C CD  1 
ATOM   1640 N NE  . ARG C 1 25 ? 13.510  -26.488 26.245  1.00 52.42  ? 24  ARG C NE  1 
ATOM   1641 C CZ  . ARG C 1 25 ? 12.250  -26.191 25.964  1.00 51.15  ? 24  ARG C CZ  1 
ATOM   1642 N NH1 . ARG C 1 25 ? 11.925  -24.991 25.511  1.00 48.52  ? 24  ARG C NH1 1 
ATOM   1643 N NH2 . ARG C 1 25 ? 11.305  -27.100 26.156  1.00 52.56  ? 24  ARG C NH2 1 
ATOM   1644 N N   . ILE C 1 26 ? 19.443  -26.850 26.602  1.00 35.58  ? 25  ILE C N   1 
ATOM   1645 C CA  . ILE C 1 26 ? 19.730  -27.457 27.904  1.00 38.44  ? 25  ILE C CA  1 
ATOM   1646 C C   . ILE C 1 26 ? 18.466  -27.478 28.762  1.00 45.45  ? 25  ILE C C   1 
ATOM   1647 O O   . ILE C 1 26 ? 17.805  -26.457 28.911  1.00 50.32  ? 25  ILE C O   1 
ATOM   1648 C CB  . ILE C 1 26 ? 20.855  -26.691 28.625  1.00 39.29  ? 25  ILE C CB  1 
ATOM   1649 C CG1 . ILE C 1 26 ? 22.034  -26.354 27.724  1.00 38.72  ? 25  ILE C CG1 1 
ATOM   1650 C CG2 . ILE C 1 26 ? 21.298  -27.445 29.892  1.00 40.13  ? 25  ILE C CG2 1 
ATOM   1651 C CD1 . ILE C 1 26 ? 22.805  -27.549 27.193  1.00 41.19  ? 25  ILE C CD1 1 
ATOM   1652 N N   . ASP C 1 27 ? 18.131  -28.636 29.336  1.00 46.00  ? 26  ASP C N   1 
ATOM   1653 C CA  . ASP C 1 27 ? 17.015  -28.723 30.268  1.00 54.28  ? 26  ASP C CA  1 
ATOM   1654 C C   . ASP C 1 27 ? 17.519  -28.662 31.709  1.00 56.67  ? 26  ASP C C   1 
ATOM   1655 O O   . ASP C 1 27 ? 18.721  -28.792 31.957  1.00 59.01  ? 26  ASP C O   1 
ATOM   1656 C CB  . ASP C 1 27 ? 16.289  -30.052 30.156  1.00 49.63  ? 26  ASP C CB  1 
ATOM   1657 C CG  . ASP C 1 27 ? 15.064  -30.088 29.259  1.00 58.62  ? 26  ASP C CG  1 
ATOM   1658 O OD1 . ASP C 1 27 ? 14.846  -29.092 28.526  1.00 51.85  ? 26  ASP C OD1 1 
ATOM   1659 O OD2 . ASP C 1 27 ? 14.324  -31.102 29.346  1.00 59.82  ? 26  ASP C OD2 1 
ATOM   1660 N N   . ASP C 1 28 ? 16.570  -28.490 32.644  1.00 63.86  ? 27  ASP C N   1 
ATOM   1661 C CA  . ASP C 1 28 ? 16.759  -28.760 34.063  1.00 61.39  ? 27  ASP C CA  1 
ATOM   1662 C C   . ASP C 1 28 ? 16.671  -30.265 34.274  1.00 63.19  ? 27  ASP C C   1 
ATOM   1663 O O   . ASP C 1 28 ? 16.135  -30.972 33.424  1.00 59.21  ? 27  ASP C O   1 
ATOM   1664 C CB  . ASP C 1 28 ? 15.636  -28.170 34.901  1.00 58.76  ? 27  ASP C CB  1 
ATOM   1665 N N   . ILE C 1 29 ? 17.199  -30.746 35.407  1.00 70.15  ? 28  ILE C N   1 
ATOM   1666 C CA  . ILE C 1 29 ? 17.005  -32.132 35.805  1.00 67.00  ? 28  ILE C CA  1 
ATOM   1667 C C   . ILE C 1 29 ? 15.920  -32.168 36.893  1.00 66.45  ? 28  ILE C C   1 
ATOM   1668 O O   . ILE C 1 29 ? 16.146  -31.503 37.924  1.00 72.18  ? 28  ILE C O   1 
ATOM   1669 C CB  . ILE C 1 29 ? 18.325  -32.768 36.278  1.00 60.15  ? 28  ILE C CB  1 
ATOM   1670 N N   . LYS C 1 35 ? 20.122  -39.181 37.939  1.00 50.86  ? 34  LYS C N   1 
ATOM   1671 C CA  . LYS C 1 35 ? 20.926  -38.002 37.517  1.00 50.98  ? 34  LYS C CA  1 
ATOM   1672 C C   . LYS C 1 35 ? 21.607  -38.335 36.194  1.00 46.06  ? 34  LYS C C   1 
ATOM   1673 O O   . LYS C 1 35 ? 21.654  -39.496 35.796  1.00 49.31  ? 34  LYS C O   1 
ATOM   1674 C CB  . LYS C 1 35 ? 21.977  -37.657 38.580  1.00 49.94  ? 34  LYS C CB  1 
ATOM   1675 N N   . PRO C 1 36 ? 22.155  -37.331 35.473  1.00 46.60  ? 35  PRO C N   1 
ATOM   1676 C CA  . PRO C 1 36 ? 22.891  -37.607 34.246  1.00 51.48  ? 35  PRO C CA  1 
ATOM   1677 C C   . PRO C 1 36 ? 24.011  -38.596 34.552  1.00 49.66  ? 35  PRO C C   1 
ATOM   1678 O O   . PRO C 1 36 ? 24.422  -38.780 35.712  1.00 46.99  ? 35  PRO C O   1 
ATOM   1679 C CB  . PRO C 1 36 ? 23.432  -36.229 33.795  1.00 51.40  ? 35  PRO C CB  1 
ATOM   1680 C CG  . PRO C 1 36 ? 22.552  -35.215 34.514  1.00 52.27  ? 35  PRO C CG  1 
ATOM   1681 C CD  . PRO C 1 36 ? 22.088  -35.890 35.800  1.00 47.73  ? 35  PRO C CD  1 
ATOM   1682 N N   . PRO C 1 37 ? 24.537  -39.281 33.519  1.00 48.70  ? 36  PRO C N   1 
ATOM   1683 C CA  . PRO C 1 37 ? 25.851  -39.898 33.644  1.00 44.37  ? 36  PRO C CA  1 
ATOM   1684 C C   . PRO C 1 37 ? 26.776  -38.740 34.006  1.00 41.58  ? 36  PRO C C   1 
ATOM   1685 O O   . PRO C 1 37 ? 26.443  -37.567 33.801  1.00 38.57  ? 36  PRO C O   1 
ATOM   1686 C CB  . PRO C 1 37 ? 26.076  -40.437 32.220  1.00 44.14  ? 36  PRO C CB  1 
ATOM   1687 C CG  . PRO C 1 37 ? 24.669  -40.745 31.779  1.00 49.36  ? 36  PRO C CG  1 
ATOM   1688 C CD  . PRO C 1 37 ? 23.914  -39.502 32.198  1.00 46.02  ? 36  PRO C CD  1 
ATOM   1689 N N   . PRO C 1 38 ? 27.954  -39.037 34.599  1.00 36.19  ? 37  PRO C N   1 
ATOM   1690 C CA  . PRO C 1 38 ? 28.924  -37.995 34.932  1.00 37.09  ? 37  PRO C CA  1 
ATOM   1691 C C   . PRO C 1 38 ? 29.262  -37.120 33.736  1.00 33.03  ? 37  PRO C C   1 
ATOM   1692 O O   . PRO C 1 38 ? 29.517  -37.623 32.638  1.00 37.91  ? 37  PRO C O   1 
ATOM   1693 C CB  . PRO C 1 38 ? 30.149  -38.817 35.390  1.00 40.76  ? 37  PRO C CB  1 
ATOM   1694 C CG  . PRO C 1 38 ? 29.528  -40.090 35.922  1.00 38.34  ? 37  PRO C CG  1 
ATOM   1695 C CD  . PRO C 1 38 ? 28.404  -40.397 34.950  1.00 37.65  ? 37  PRO C CD  1 
ATOM   1696 N N   . ASN C 1 39 ? 29.193  -35.807 33.984  1.00 35.80  ? 38  ASN C N   1 
ATOM   1697 C CA  . ASN C 1 39 ? 29.596  -34.738 33.087  1.00 33.80  ? 38  ASN C CA  1 
ATOM   1698 C C   . ASN C 1 39 ? 28.738  -34.712 31.821  1.00 36.61  ? 38  ASN C C   1 
ATOM   1699 O O   . ASN C 1 39 ? 29.240  -34.292 30.776  1.00 42.30  ? 38  ASN C O   1 
ATOM   1700 C CB  . ASN C 1 39 ? 31.042  -34.865 32.638  1.00 37.77  ? 38  ASN C CB  1 
ATOM   1701 C CG  . ASN C 1 39 ? 31.614  -33.594 32.053  1.00 48.84  ? 38  ASN C CG  1 
ATOM   1702 O OD1 . ASN C 1 39 ? 31.241  -32.493 32.470  1.00 58.88  ? 38  ASN C OD1 1 
ATOM   1703 N ND2 . ASN C 1 39 ? 32.498  -33.714 31.070  1.00 46.65  ? 38  ASN C ND2 1 
ATOM   1704 N N   . LYS C 1 40 ? 27.466  -35.119 31.939  1.00 32.34  ? 39  LYS C N   1 
ATOM   1705 C CA  . LYS C 1 40 ? 26.546  -34.989 30.817  1.00 30.84  ? 39  LYS C CA  1 
ATOM   1706 C C   . LYS C 1 40 ? 25.425  -34.016 31.164  1.00 32.52  ? 39  LYS C C   1 
ATOM   1707 O O   . LYS C 1 40 ? 25.047  -33.873 32.315  1.00 35.73  ? 39  LYS C O   1 
ATOM   1708 C CB  . LYS C 1 40 ? 25.832  -36.319 30.535  1.00 30.83  ? 39  LYS C CB  1 
ATOM   1709 C CG  . LYS C 1 40 ? 26.734  -37.459 30.164  1.00 35.01  ? 39  LYS C CG  1 
ATOM   1710 C CD  . LYS C 1 40 ? 27.455  -37.350 28.839  1.00 40.50  ? 39  LYS C CD  1 
ATOM   1711 C CE  . LYS C 1 40 ? 28.306  -38.563 28.552  1.00 42.51  ? 39  LYS C CE  1 
ATOM   1712 N NZ  . LYS C 1 40 ? 29.244  -38.348 27.446  1.00 49.66  ? 39  LYS C NZ  1 
ATOM   1713 N N   . TYR C 1 41 ? 24.864  -33.354 30.132  1.00 30.01  ? 40  TYR C N   1 
ATOM   1714 C CA  . TYR C 1 41 ? 23.777  -32.393 30.292  1.00 34.14  ? 40  TYR C CA  1 
ATOM   1715 C C   . TYR C 1 41 ? 22.496  -33.036 29.782  1.00 32.45  ? 40  TYR C C   1 
ATOM   1716 O O   . TYR C 1 41 ? 22.581  -33.781 28.810  1.00 31.79  ? 40  TYR C O   1 
ATOM   1717 C CB  . TYR C 1 41 ? 23.972  -31.175 29.378  1.00 29.62  ? 40  TYR C CB  1 
ATOM   1718 C CG  . TYR C 1 41 ? 25.117  -30.258 29.775  1.00 32.39  ? 40  TYR C CG  1 
ATOM   1719 C CD1 . TYR C 1 41 ? 26.415  -30.471 29.316  1.00 32.17  ? 40  TYR C CD1 1 
ATOM   1720 C CD2 . TYR C 1 41 ? 24.916  -29.209 30.678  1.00 36.94  ? 40  TYR C CD2 1 
ATOM   1721 C CE1 . TYR C 1 41 ? 27.483  -29.693 29.725  1.00 41.01  ? 40  TYR C CE1 1 
ATOM   1722 C CE2 . TYR C 1 41 ? 25.981  -28.413 31.078  1.00 37.29  ? 40  TYR C CE2 1 
ATOM   1723 C CZ  . TYR C 1 41 ? 27.258  -28.649 30.610  1.00 41.41  ? 40  TYR C CZ  1 
ATOM   1724 O OH  . TYR C 1 41 ? 28.291  -27.869 31.026  1.00 50.39  ? 40  TYR C OH  1 
ATOM   1725 N N   . PRO C 1 42 ? 21.302  -32.692 30.347  1.00 33.33  ? 41  PRO C N   1 
ATOM   1726 C CA  . PRO C 1 42 ? 20.004  -33.129 29.819  1.00 32.00  ? 41  PRO C CA  1 
ATOM   1727 C C   . PRO C 1 42 ? 19.683  -32.242 28.623  1.00 33.60  ? 41  PRO C C   1 
ATOM   1728 O O   . PRO C 1 42 ? 19.713  -31.012 28.737  1.00 34.20  ? 41  PRO C O   1 
ATOM   1729 C CB  . PRO C 1 42 ? 18.992  -32.906 30.977  1.00 34.63  ? 41  PRO C CB  1 
ATOM   1730 C CG  . PRO C 1 42 ? 19.747  -32.070 31.974  1.00 39.40  ? 41  PRO C CG  1 
ATOM   1731 C CD  . PRO C 1 42 ? 21.149  -31.753 31.478  1.00 38.32  ? 41  PRO C CD  1 
ATOM   1732 N N   . ILE C 1 43 ? 19.431  -32.890 27.477  1.00 30.97  ? 42  ILE C N   1 
ATOM   1733 C CA  . ILE C 1 43 ? 19.205  -32.084 26.281  1.00 32.65  ? 42  ILE C CA  1 
ATOM   1734 C C   . ILE C 1 43 ? 17.767  -32.302 25.837  1.00 29.92  ? 42  ILE C C   1 
ATOM   1735 O O   . ILE C 1 43 ? 17.235  -33.406 25.903  1.00 33.03  ? 42  ILE C O   1 
ATOM   1736 C CB  . ILE C 1 43 ? 20.205  -32.460 25.171  1.00 28.89  ? 42  ILE C CB  1 
ATOM   1737 C CG1 . ILE C 1 43 ? 21.680  -32.290 25.584  1.00 31.65  ? 42  ILE C CG1 1 
ATOM   1738 C CG2 . ILE C 1 43 ? 19.871  -31.700 23.868  1.00 32.94  ? 42  ILE C CG2 1 
ATOM   1739 C CD1 . ILE C 1 43 ? 22.131  -30.860 25.849  1.00 30.02  ? 42  ILE C CD1 1 
ATOM   1740 N N   . PHE C 1 44 ? 17.101  -31.239 25.345  1.00 32.87  ? 43  PHE C N   1 
ATOM   1741 C CA  . PHE C 1 44 ? 15.808  -31.426 24.697  1.00 29.92  ? 43  PHE C CA  1 
ATOM   1742 C C   . PHE C 1 44 ? 15.966  -30.940 23.251  1.00 28.98  ? 43  PHE C C   1 
ATOM   1743 O O   . PHE C 1 44 ? 16.557  -29.872 23.037  1.00 31.09  ? 43  PHE C O   1 
ATOM   1744 C CB  . PHE C 1 44 ? 14.822  -30.454 25.362  1.00 36.77  ? 43  PHE C CB  1 
ATOM   1745 C CG  . PHE C 1 44 ? 13.443  -30.369 24.722  1.00 37.07  ? 43  PHE C CG  1 
ATOM   1746 C CD1 . PHE C 1 44 ? 12.481  -31.342 24.978  1.00 38.52  ? 43  PHE C CD1 1 
ATOM   1747 C CD2 . PHE C 1 44 ? 13.120  -29.317 23.858  1.00 40.10  ? 43  PHE C CD2 1 
ATOM   1748 C CE1 . PHE C 1 44 ? 11.235  -31.288 24.363  1.00 41.04  ? 43  PHE C CE1 1 
ATOM   1749 C CE2 . PHE C 1 44 ? 11.859  -29.252 23.262  1.00 36.78  ? 43  PHE C CE2 1 
ATOM   1750 C CZ  . PHE C 1 44 ? 10.931  -30.239 23.520  1.00 41.60  ? 43  PHE C CZ  1 
ATOM   1751 N N   . PHE C 1 45 ? 15.509  -31.774 22.310  1.00 31.28  ? 44  PHE C N   1 
ATOM   1752 C CA  . PHE C 1 45 ? 15.704  -31.565 20.877  1.00 30.96  ? 44  PHE C CA  1 
ATOM   1753 C C   . PHE C 1 45 ? 14.437  -30.914 20.335  1.00 28.56  ? 44  PHE C C   1 
ATOM   1754 O O   . PHE C 1 45 ? 13.343  -31.432 20.517  1.00 34.13  ? 44  PHE C O   1 
ATOM   1755 C CB  . PHE C 1 45 ? 16.010  -32.865 20.137  1.00 28.82  ? 44  PHE C CB  1 
ATOM   1756 C CG  . PHE C 1 45 ? 17.370  -33.438 20.492  1.00 27.57  ? 44  PHE C CG  1 
ATOM   1757 C CD1 . PHE C 1 45 ? 18.502  -33.075 19.774  1.00 27.62  ? 44  PHE C CD1 1 
ATOM   1758 C CD2 . PHE C 1 45 ? 17.495  -34.382 21.526  1.00 29.30  ? 44  PHE C CD2 1 
ATOM   1759 C CE1 . PHE C 1 45 ? 19.759  -33.615 20.078  1.00 31.79  ? 44  PHE C CE1 1 
ATOM   1760 C CE2 . PHE C 1 45 ? 18.743  -34.918 21.825  1.00 33.07  ? 44  PHE C CE2 1 
ATOM   1761 C CZ  . PHE C 1 45 ? 19.867  -34.514 21.115  1.00 29.01  ? 44  PHE C CZ  1 
ATOM   1762 N N   . PHE C 1 46 ? 14.596  -29.716 19.737  1.00 29.81  ? 45  PHE C N   1 
ATOM   1763 C CA  . PHE C 1 46 ? 13.435  -29.122 19.086  1.00 29.04  ? 45  PHE C CA  1 
ATOM   1764 C C   . PHE C 1 46 ? 12.978  -29.967 17.901  1.00 30.67  ? 45  PHE C C   1 
ATOM   1765 O O   . PHE C 1 46 ? 13.771  -30.683 17.276  1.00 28.77  ? 45  PHE C O   1 
ATOM   1766 C CB  . PHE C 1 46 ? 13.704  -27.682 18.642  1.00 29.80  ? 45  PHE C CB  1 
ATOM   1767 C CG  . PHE C 1 46 ? 13.988  -26.703 19.763  1.00 31.71  ? 45  PHE C CG  1 
ATOM   1768 C CD1 . PHE C 1 46 ? 12.954  -26.223 20.569  1.00 33.98  ? 45  PHE C CD1 1 
ATOM   1769 C CD2 . PHE C 1 46 ? 15.296  -26.248 19.974  1.00 28.71  ? 45  PHE C CD2 1 
ATOM   1770 C CE1 . PHE C 1 46 ? 13.254  -25.310 21.582  1.00 36.14  ? 45  PHE C CE1 1 
ATOM   1771 C CE2 . PHE C 1 46 ? 15.581  -25.368 21.007  1.00 34.54  ? 45  PHE C CE2 1 
ATOM   1772 C CZ  . PHE C 1 46 ? 14.552  -24.894 21.794  1.00 33.36  ? 45  PHE C CZ  1 
ATOM   1773 N N   . GLY C 1 47 ? 11.692  -29.834 17.535  1.00 28.24  ? 46  GLY C N   1 
ATOM   1774 C CA  . GLY C 1 47 ? 11.214  -30.559 16.375  1.00 31.34  ? 46  GLY C CA  1 
ATOM   1775 C C   . GLY C 1 47 ? 10.721  -31.961 16.739  1.00 35.86  ? 46  GLY C C   1 
ATOM   1776 O O   . GLY C 1 47 ? 9.536   -32.246 16.629  1.00 40.27  ? 46  GLY C O   1 
ATOM   1777 N N   . THR C 1 48 ? 11.635  -32.835 17.193  1.00 31.41  ? 47  THR C N   1 
ATOM   1778 C CA  . THR C 1 48 ? 11.289  -34.192 17.597  1.00 33.06  ? 47  THR C CA  1 
ATOM   1779 C C   . THR C 1 48 ? 10.736  -34.176 19.019  1.00 33.72  ? 47  THR C C   1 
ATOM   1780 O O   . THR C 1 48 ? 9.917   -35.025 19.347  1.00 39.05  ? 47  THR C O   1 
ATOM   1781 C CB  . THR C 1 48 ? 12.531  -35.076 17.507  1.00 30.81  ? 47  THR C CB  1 
ATOM   1782 O OG1 . THR C 1 48 ? 13.355  -34.526 18.541  1.00 34.85  ? 47  THR C OG1 1 
ATOM   1783 C CG2 . THR C 1 48 ? 13.100  -35.181 16.111  1.00 31.57  ? 47  THR C CG2 1 
ATOM   1784 N N   . HIS C 1 49 ? 11.168  -33.210 19.836  1.00 34.30  ? 48  HIS C N   1 
ATOM   1785 C CA  . HIS C 1 49 ? 10.801  -33.055 21.245  1.00 39.51  ? 48  HIS C CA  1 
ATOM   1786 C C   . HIS C 1 49 ? 11.311  -34.217 22.112  1.00 37.97  ? 48  HIS C C   1 
ATOM   1787 O O   . HIS C 1 49 ? 10.760  -34.481 23.180  1.00 42.11  ? 48  HIS C O   1 
ATOM   1788 C CB  . HIS C 1 49 ? 9.283   -32.856 21.416  1.00 36.77  ? 48  HIS C CB  1 
ATOM   1789 C CG  . HIS C 1 49 ? 8.721   -31.751 20.570  1.00 43.06  ? 48  HIS C CG  1 
ATOM   1790 N ND1 . HIS C 1 49 ? 7.508   -31.883 19.931  1.00 48.03  ? 48  HIS C ND1 1 
ATOM   1791 C CD2 . HIS C 1 49 ? 9.178   -30.530 20.245  1.00 47.11  ? 48  HIS C CD2 1 
ATOM   1792 C CE1 . HIS C 1 49 ? 7.246   -30.783 19.236  1.00 51.47  ? 48  HIS C CE1 1 
ATOM   1793 N NE2 . HIS C 1 49 ? 8.247   -29.944 19.400  1.00 45.11  ? 48  HIS C NE2 1 
ATOM   1794 N N   . GLU C 1 50 ? 12.345  -34.922 21.645  1.00 34.58  ? 49  GLU C N   1 
ATOM   1795 C CA  . GLU C 1 50 ? 12.951  -36.010 22.397  1.00 36.02  ? 49  GLU C CA  1 
ATOM   1796 C C   . GLU C 1 50 ? 14.050  -35.472 23.321  1.00 36.16  ? 49  GLU C C   1 
ATOM   1797 O O   . GLU C 1 50 ? 14.421  -34.302 23.299  1.00 35.30  ? 49  GLU C O   1 
ATOM   1798 C CB  . GLU C 1 50 ? 13.433  -37.075 21.416  1.00 38.12  ? 49  GLU C CB  1 
ATOM   1799 C CG  . GLU C 1 50 ? 12.310  -37.645 20.552  1.00 44.97  ? 49  GLU C CG  1 
ATOM   1800 C CD  . GLU C 1 50 ? 12.816  -38.580 19.477  1.00 51.95  ? 49  GLU C CD  1 
ATOM   1801 O OE1 . GLU C 1 50 ? 14.035  -38.848 19.450  1.00 61.72  ? 49  GLU C OE1 1 
ATOM   1802 O OE2 . GLU C 1 50 ? 11.994  -39.037 18.660  1.00 57.64  ? 49  GLU C OE2 1 
ATOM   1803 N N   . THR C 1 51 ? 14.529  -36.337 24.222  1.00 38.26  ? 50  THR C N   1 
ATOM   1804 C CA  . THR C 1 51 ? 15.540  -35.944 25.199  1.00 34.43  ? 50  THR C CA  1 
ATOM   1805 C C   . THR C 1 51 ? 16.643  -36.995 25.158  1.00 31.62  ? 50  THR C C   1 
ATOM   1806 O O   . THR C 1 51 ? 16.414  -38.129 24.746  1.00 38.49  ? 50  THR C O   1 
ATOM   1807 C CB  . THR C 1 51 ? 14.946  -35.865 26.607  1.00 37.61  ? 50  THR C CB  1 
ATOM   1808 O OG1 . THR C 1 51 ? 14.513  -37.200 26.886  1.00 40.44  ? 50  THR C OG1 1 
ATOM   1809 C CG2 . THR C 1 51 ? 13.877  -34.796 26.750  1.00 40.54  ? 50  THR C CG2 1 
ATOM   1810 N N   . ALA C 1 52 ? 17.845  -36.562 25.530  1.00 32.40  ? 51  ALA C N   1 
ATOM   1811 C CA  . ALA C 1 52 ? 19.018  -37.405 25.691  1.00 34.55  ? 51  ALA C CA  1 
ATOM   1812 C C   . ALA C 1 52 ? 20.016  -36.705 26.617  1.00 36.75  ? 51  ALA C C   1 
ATOM   1813 O O   . ALA C 1 52 ? 19.857  -35.538 26.982  1.00 36.08  ? 51  ALA C O   1 
ATOM   1814 C CB  . ALA C 1 52 ? 19.633  -37.694 24.342  1.00 34.24  ? 51  ALA C CB  1 
ATOM   1815 N N   . PHE C 1 53 ? 21.062  -37.442 27.019  1.00 35.74  ? 52  PHE C N   1 
ATOM   1816 C CA  . PHE C 1 53 ? 22.158  -36.842 27.768  1.00 36.83  ? 52  PHE C CA  1 
ATOM   1817 C C   . PHE C 1 53 ? 23.361  -36.706 26.858  1.00 34.11  ? 52  PHE C C   1 
ATOM   1818 O O   . PHE C 1 53 ? 23.754  -37.676 26.199  1.00 37.32  ? 52  PHE C O   1 
ATOM   1819 C CB  . PHE C 1 53 ? 22.571  -37.802 28.888  1.00 37.37  ? 52  PHE C CB  1 
ATOM   1820 C CG  . PHE C 1 53 ? 21.517  -37.806 29.982  1.00 40.34  ? 52  PHE C CG  1 
ATOM   1821 C CD1 . PHE C 1 53 ? 21.320  -36.681 30.772  1.00 39.18  ? 52  PHE C CD1 1 
ATOM   1822 C CD2 . PHE C 1 53 ? 20.703  -38.919 30.193  1.00 49.10  ? 52  PHE C CD2 1 
ATOM   1823 C CE1 . PHE C 1 53 ? 20.372  -36.672 31.780  1.00 45.09  ? 52  PHE C CE1 1 
ATOM   1824 C CE2 . PHE C 1 53 ? 19.749  -38.899 31.201  1.00 51.81  ? 52  PHE C CE2 1 
ATOM   1825 C CZ  . PHE C 1 53 ? 19.585  -37.775 31.989  1.00 45.26  ? 52  PHE C CZ  1 
ATOM   1826 N N   . LEU C 1 54 ? 23.984  -35.528 26.861  1.00 30.92  ? 53  LEU C N   1 
ATOM   1827 C CA  . LEU C 1 54 ? 25.152  -35.334 26.016  1.00 28.70  ? 53  LEU C CA  1 
ATOM   1828 C C   . LEU C 1 54 ? 26.242  -34.580 26.777  1.00 29.83  ? 53  LEU C C   1 
ATOM   1829 O O   . LEU C 1 54 ? 25.945  -33.802 27.680  1.00 33.58  ? 53  LEU C O   1 
ATOM   1830 C CB  . LEU C 1 54 ? 24.823  -34.611 24.705  1.00 30.13  ? 53  LEU C CB  1 
ATOM   1831 C CG  . LEU C 1 54 ? 24.031  -35.401 23.656  1.00 34.78  ? 53  LEU C CG  1 
ATOM   1832 C CD1 . LEU C 1 54 ? 23.744  -34.417 22.559  1.00 33.53  ? 53  LEU C CD1 1 
ATOM   1833 C CD2 . LEU C 1 54 ? 24.822  -36.626 23.083  1.00 35.17  ? 53  LEU C CD2 1 
ATOM   1834 N N   . GLY C 1 55 ? 27.494  -34.804 26.375  1.00 32.78  ? 54  GLY C N   1 
ATOM   1835 C CA  . GLY C 1 55 ? 28.631  -34.132 26.991  1.00 36.09  ? 54  GLY C CA  1 
ATOM   1836 C C   . GLY C 1 55 ? 28.984  -32.837 26.259  1.00 41.87  ? 54  GLY C C   1 
ATOM   1837 O O   . GLY C 1 55 ? 28.499  -32.558 25.144  1.00 37.78  ? 54  GLY C O   1 
ATOM   1838 N N   . PRO C 1 56 ? 29.822  -31.967 26.866  1.00 41.66  ? 55  PRO C N   1 
ATOM   1839 C CA  . PRO C 1 56 ? 30.108  -30.664 26.278  1.00 42.66  ? 55  PRO C CA  1 
ATOM   1840 C C   . PRO C 1 56 ? 30.756  -30.710 24.901  1.00 36.26  ? 55  PRO C C   1 
ATOM   1841 O O   . PRO C 1 56 ? 30.561  -29.783 24.133  1.00 48.10  ? 55  PRO C O   1 
ATOM   1842 C CB  . PRO C 1 56 ? 30.991  -29.942 27.353  1.00 41.52  ? 55  PRO C CB  1 
ATOM   1843 C CG  . PRO C 1 56 ? 31.585  -31.080 28.138  1.00 39.60  ? 55  PRO C CG  1 
ATOM   1844 C CD  . PRO C 1 56 ? 30.494  -32.145 28.170  1.00 44.53  ? 55  PRO C CD  1 
ATOM   1845 N N   . LYS C 1 57 ? 31.478  -31.794 24.577  1.00 41.70  ? 56  LYS C N   1 
ATOM   1846 C CA  . LYS C 1 57 ? 32.099  -31.864 23.259  1.00 43.06  ? 56  LYS C CA  1 
ATOM   1847 C C   . LYS C 1 57 ? 31.020  -31.836 22.171  1.00 47.50  ? 56  LYS C C   1 
ATOM   1848 O O   . LYS C 1 57 ? 31.295  -31.456 21.028  1.00 44.80  ? 56  LYS C O   1 
ATOM   1849 C CB  . LYS C 1 57 ? 32.947  -33.123 23.048  1.00 48.50  ? 56  LYS C CB  1 
ATOM   1850 N N   . ASP C 1 58 ? 29.791  -32.231 22.538  1.00 42.73  ? 57  ASP C N   1 
ATOM   1851 C CA  . ASP C 1 58 ? 28.738  -32.444 21.552  1.00 42.75  ? 57  ASP C CA  1 
ATOM   1852 C C   . ASP C 1 58 ? 27.825  -31.232 21.403  1.00 38.77  ? 57  ASP C C   1 
ATOM   1853 O O   . ASP C 1 58 ? 26.819  -31.329 20.699  1.00 35.36  ? 57  ASP C O   1 
ATOM   1854 C CB  . ASP C 1 58 ? 27.903  -33.670 21.891  1.00 41.51  ? 57  ASP C CB  1 
ATOM   1855 C CG  . ASP C 1 58 ? 28.718  -34.942 22.049  1.00 45.41  ? 57  ASP C CG  1 
ATOM   1856 O OD1 . ASP C 1 58 ? 29.679  -35.099 21.284  1.00 45.38  ? 57  ASP C OD1 1 
ATOM   1857 O OD2 . ASP C 1 58 ? 28.378  -35.742 22.924  1.00 51.66  ? 57  ASP C OD2 1 
ATOM   1858 N N   . LEU C 1 59 ? 28.138  -30.115 22.076  1.00 34.60  ? 58  LEU C N   1 
ATOM   1859 C CA  . LEU C 1 59 ? 27.203  -29.007 22.237  1.00 36.15  ? 58  LEU C CA  1 
ATOM   1860 C C   . LEU C 1 59 ? 27.803  -27.720 21.679  1.00 42.46  ? 58  LEU C C   1 
ATOM   1861 O O   . LEU C 1 59 ? 28.986  -27.456 21.911  1.00 46.36  ? 58  LEU C O   1 
ATOM   1862 C CB  . LEU C 1 59 ? 26.768  -28.824 23.695  1.00 35.33  ? 58  LEU C CB  1 
ATOM   1863 C CG  . LEU C 1 59 ? 26.164  -30.072 24.352  1.00 32.86  ? 58  LEU C CG  1 
ATOM   1864 C CD1 . LEU C 1 59 ? 25.826  -29.901 25.816  1.00 33.50  ? 58  LEU C CD1 1 
ATOM   1865 C CD2 . LEU C 1 59 ? 24.921  -30.521 23.562  1.00 28.73  ? 58  LEU C CD2 1 
ATOM   1866 N N   . PHE C 1 60 ? 26.983  -26.939 20.958  1.00 41.95  ? 59  PHE C N   1 
ATOM   1867 C CA  . PHE C 1 60 ? 27.456  -25.743 20.254  1.00 41.16  ? 59  PHE C CA  1 
ATOM   1868 C C   . PHE C 1 60 ? 26.499  -24.585 20.534  1.00 43.35  ? 59  PHE C C   1 
ATOM   1869 O O   . PHE C 1 60 ? 25.300  -24.671 20.266  1.00 40.64  ? 59  PHE C O   1 
ATOM   1870 C CB  . PHE C 1 60 ? 27.668  -25.999 18.752  1.00 39.03  ? 59  PHE C CB  1 
ATOM   1871 C CG  . PHE C 1 60 ? 28.631  -27.143 18.465  1.00 36.63  ? 59  PHE C CG  1 
ATOM   1872 C CD1 . PHE C 1 60 ? 28.218  -28.470 18.511  1.00 39.11  ? 59  PHE C CD1 1 
ATOM   1873 C CD2 . PHE C 1 60 ? 29.980  -26.895 18.218  1.00 43.73  ? 59  PHE C CD2 1 
ATOM   1874 C CE1 . PHE C 1 60 ? 29.113  -29.510 18.307  1.00 40.38  ? 59  PHE C CE1 1 
ATOM   1875 C CE2 . PHE C 1 60 ? 30.873  -27.940 17.994  1.00 39.86  ? 59  PHE C CE2 1 
ATOM   1876 C CZ  . PHE C 1 60 ? 30.446  -29.245 18.037  1.00 42.40  ? 59  PHE C CZ  1 
ATOM   1877 N N   . PRO C 1 61 ? 26.959  -23.437 21.091  1.00 42.85  ? 60  PRO C N   1 
ATOM   1878 C CA  . PRO C 1 61 ? 26.022  -22.356 21.417  1.00 43.85  ? 60  PRO C CA  1 
ATOM   1879 C C   . PRO C 1 61 ? 25.314  -21.879 20.146  1.00 36.79  ? 60  PRO C C   1 
ATOM   1880 O O   . PRO C 1 61 ? 25.923  -21.774 19.079  1.00 39.92  ? 60  PRO C O   1 
ATOM   1881 C CB  . PRO C 1 61 ? 26.875  -21.254 22.092  1.00 45.45  ? 60  PRO C CB  1 
ATOM   1882 C CG  . PRO C 1 61 ? 28.196  -21.943 22.352  1.00 41.33  ? 60  PRO C CG  1 
ATOM   1883 C CD  . PRO C 1 61 ? 28.363  -23.121 21.397  1.00 42.70  ? 60  PRO C CD  1 
ATOM   1884 N N   . TYR C 1 62 ? 24.006  -21.641 20.281  1.00 43.27  ? 61  TYR C N   1 
ATOM   1885 C CA  . TYR C 1 62 ? 23.114  -21.436 19.156  1.00 42.92  ? 61  TYR C CA  1 
ATOM   1886 C C   . TYR C 1 62 ? 23.553  -20.209 18.370  1.00 54.35  ? 61  TYR C C   1 
ATOM   1887 O O   . TYR C 1 62 ? 23.851  -20.314 17.177  1.00 55.63  ? 61  TYR C O   1 
ATOM   1888 C CB  . TYR C 1 62 ? 21.678  -21.172 19.612  1.00 41.66  ? 61  TYR C CB  1 
ATOM   1889 C CG  . TYR C 1 62 ? 20.717  -20.839 18.474  1.00 44.19  ? 61  TYR C CG  1 
ATOM   1890 C CD1 . TYR C 1 62 ? 20.603  -21.660 17.345  1.00 45.37  ? 61  TYR C CD1 1 
ATOM   1891 C CD2 . TYR C 1 62 ? 19.924  -19.696 18.528  1.00 47.14  ? 61  TYR C CD2 1 
ATOM   1892 C CE1 . TYR C 1 62 ? 19.718  -21.351 16.318  1.00 48.51  ? 61  TYR C CE1 1 
ATOM   1893 C CE2 . TYR C 1 62 ? 19.044  -19.377 17.504  1.00 50.11  ? 61  TYR C CE2 1 
ATOM   1894 C CZ  . TYR C 1 62 ? 18.938  -20.201 16.396  1.00 46.89  ? 61  TYR C CZ  1 
ATOM   1895 O OH  . TYR C 1 62 ? 18.056  -19.824 15.415  1.00 45.50  ? 61  TYR C OH  1 
ATOM   1896 N N   . ASP C 1 63 ? 23.612  -19.062 19.069  1.00 52.67  ? 62  ASP C N   1 
ATOM   1897 C CA  . ASP C 1 63 ? 23.921  -17.796 18.420  1.00 50.56  ? 62  ASP C CA  1 
ATOM   1898 C C   . ASP C 1 63 ? 25.271  -17.867 17.719  1.00 46.87  ? 62  ASP C C   1 
ATOM   1899 O O   . ASP C 1 63 ? 25.410  -17.354 16.609  1.00 55.96  ? 62  ASP C O   1 
ATOM   1900 C CB  . ASP C 1 63 ? 23.648  -16.595 19.315  1.00 53.12  ? 62  ASP C CB  1 
ATOM   1901 C CG  . ASP C 1 63 ? 22.186  -16.173 19.322  1.00 69.12  ? 62  ASP C CG  1 
ATOM   1902 O OD1 . ASP C 1 63 ? 21.612  -16.049 20.425  1.00 68.24  ? 62  ASP C OD1 1 
ATOM   1903 O OD2 . ASP C 1 63 ? 21.621  -16.001 18.212  1.00 77.82  ? 62  ASP C OD2 1 
ATOM   1904 N N   . LYS C 1 64 ? 26.236  -18.546 18.337  1.00 44.45  ? 63  LYS C N   1 
ATOM   1905 C CA  . LYS C 1 64 ? 27.581  -18.600 17.788  1.00 48.68  ? 63  LYS C CA  1 
ATOM   1906 C C   . LYS C 1 64 ? 27.615  -19.472 16.536  1.00 49.33  ? 63  LYS C C   1 
ATOM   1907 O O   . LYS C 1 64 ? 28.376  -19.182 15.619  1.00 43.73  ? 63  LYS C O   1 
ATOM   1908 C CB  . LYS C 1 64 ? 28.648  -19.030 18.807  1.00 56.07  ? 63  LYS C CB  1 
ATOM   1909 N N   . SER C 1 65 ? 26.765  -20.516 16.467  1.00 43.72  ? 64  SER C N   1 
ATOM   1910 C CA  . SER C 1 65 ? 26.966  -21.503 15.414  1.00 38.49  ? 64  SER C CA  1 
ATOM   1911 C C   . SER C 1 65 ? 25.781  -21.607 14.444  1.00 35.90  ? 64  SER C C   1 
ATOM   1912 O O   . SER C 1 65 ? 25.854  -22.404 13.521  1.00 38.12  ? 64  SER C O   1 
ATOM   1913 C CB  . SER C 1 65 ? 27.317  -22.851 15.979  1.00 43.83  ? 64  SER C CB  1 
ATOM   1914 O OG  . SER C 1 65 ? 26.192  -23.311 16.709  1.00 44.22  ? 64  SER C OG  1 
ATOM   1915 N N   . LYS C 1 66 ? 24.736  -20.794 14.599  1.00 37.13  ? 65  LYS C N   1 
ATOM   1916 C CA  . LYS C 1 66 ? 23.592  -20.949 13.705  1.00 41.28  ? 65  LYS C CA  1 
ATOM   1917 C C   . LYS C 1 66 ? 23.975  -20.679 12.251  1.00 48.88  ? 65  LYS C C   1 
ATOM   1918 O O   . LYS C 1 66 ? 23.455  -21.324 11.337  1.00 42.67  ? 65  LYS C O   1 
ATOM   1919 C CB  . LYS C 1 66 ? 22.370  -20.096 14.038  1.00 44.46  ? 65  LYS C CB  1 
ATOM   1920 C CG  . LYS C 1 66 ? 22.643  -18.618 14.194  1.00 36.70  ? 65  LYS C CG  1 
ATOM   1921 C CD  . LYS C 1 66 ? 21.294  -17.939 14.379  1.00 49.50  ? 65  LYS C CD  1 
ATOM   1922 C CE  . LYS C 1 66 ? 21.457  -16.549 14.881  1.00 49.46  ? 65  LYS C CE  1 
ATOM   1923 N NZ  . LYS C 1 66 ? 20.124  -15.997 15.099  1.00 53.00  ? 65  LYS C NZ  1 
ATOM   1924 N N   . ASP C 1 67 ? 24.870  -19.712 12.020  1.00 41.18  ? 66  ASP C N   1 
ATOM   1925 C CA  . ASP C 1 67 ? 25.236  -19.428 10.638  1.00 42.98  ? 66  ASP C CA  1 
ATOM   1926 C C   . ASP C 1 67 ? 25.644  -20.727 9.917   1.00 43.04  ? 66  ASP C C   1 
ATOM   1927 O O   . ASP C 1 67 ? 25.339  -20.902 8.742   1.00 40.82  ? 66  ASP C O   1 
ATOM   1928 C CB  . ASP C 1 67 ? 26.086  -18.159 10.531  1.00 44.37  ? 66  ASP C CB  1 
ATOM   1929 C CG  . ASP C 1 67 ? 27.602  -18.261 10.659  1.00 62.85  ? 66  ASP C CG  1 
ATOM   1930 O OD1 . ASP C 1 67 ? 28.170  -19.338 10.343  1.00 64.84  ? 66  ASP C OD1 1 
ATOM   1931 O OD2 . ASP C 1 67 ? 28.214  -17.236 11.057  1.00 63.34  ? 66  ASP C OD2 1 
ATOM   1932 N N   . LYS C 1 68 ? 26.256  -21.680 10.648  1.00 40.84  ? 67  LYS C N   1 
ATOM   1933 C CA  . LYS C 1 68 ? 26.771  -22.914 10.064  1.00 37.51  ? 67  LYS C CA  1 
ATOM   1934 C C   . LYS C 1 68 ? 25.761  -24.082 10.129  1.00 35.30  ? 67  LYS C C   1 
ATOM   1935 O O   . LYS C 1 68 ? 25.610  -24.855 9.181   1.00 39.09  ? 67  LYS C O   1 
ATOM   1936 C CB  . LYS C 1 68 ? 28.004  -23.242 10.910  1.00 32.36  ? 67  LYS C CB  1 
ATOM   1937 C CG  . LYS C 1 68 ? 28.873  -24.381 10.443  1.00 37.21  ? 67  LYS C CG  1 
ATOM   1938 C CD  . LYS C 1 68 ? 30.133  -24.335 11.311  1.00 47.45  ? 67  LYS C CD  1 
ATOM   1939 C CE  . LYS C 1 68 ? 30.987  -25.565 11.473  1.00 58.92  ? 67  LYS C CE  1 
ATOM   1940 N NZ  . LYS C 1 68 ? 31.376  -26.261 10.240  1.00 64.76  ? 67  LYS C NZ  1 
ATOM   1941 N N   . TYR C 1 69 ? 25.074  -24.242 11.266  1.00 34.83  ? 68  TYR C N   1 
ATOM   1942 C CA  . TYR C 1 69 ? 24.228  -25.420 11.425  1.00 35.30  ? 68  TYR C CA  1 
ATOM   1943 C C   . TYR C 1 69 ? 22.752  -25.085 11.243  1.00 33.64  ? 68  TYR C C   1 
ATOM   1944 O O   . TYR C 1 69 ? 21.951  -26.000 11.100  1.00 30.46  ? 68  TYR C O   1 
ATOM   1945 C CB  . TYR C 1 69 ? 24.414  -25.977 12.847  1.00 32.12  ? 68  TYR C CB  1 
ATOM   1946 C CG  . TYR C 1 69 ? 25.832  -26.467 13.123  1.00 29.53  ? 68  TYR C CG  1 
ATOM   1947 C CD1 . TYR C 1 69 ? 26.531  -27.273 12.220  1.00 37.55  ? 68  TYR C CD1 1 
ATOM   1948 C CD2 . TYR C 1 69 ? 26.450  -26.119 14.321  1.00 36.74  ? 68  TYR C CD2 1 
ATOM   1949 C CE1 . TYR C 1 69 ? 27.810  -27.737 12.501  1.00 36.87  ? 68  TYR C CE1 1 
ATOM   1950 C CE2 . TYR C 1 69 ? 27.730  -26.572 14.600  1.00 35.84  ? 68  TYR C CE2 1 
ATOM   1951 C CZ  . TYR C 1 69 ? 28.399  -27.367 13.694  1.00 40.06  ? 68  TYR C CZ  1 
ATOM   1952 O OH  . TYR C 1 69 ? 29.660  -27.722 14.081  1.00 43.12  ? 68  TYR C OH  1 
ATOM   1953 N N   . GLY C 1 70 ? 22.378  -23.790 11.284  1.00 34.07  ? 69  GLY C N   1 
ATOM   1954 C CA  . GLY C 1 70 ? 20.962  -23.451 11.212  1.00 31.60  ? 69  GLY C CA  1 
ATOM   1955 C C   . GLY C 1 70 ? 20.560  -23.307 9.751   1.00 34.66  ? 69  GLY C C   1 
ATOM   1956 O O   . GLY C 1 70 ? 20.499  -22.201 9.229   1.00 35.01  ? 69  GLY C O   1 
ATOM   1957 N N   . LYS C 1 71 ? 20.440  -24.453 9.092   1.00 31.22  ? 70  LYS C N   1 
ATOM   1958 C CA  . LYS C 1 71 ? 20.048  -24.538 7.695   1.00 32.76  ? 70  LYS C CA  1 
ATOM   1959 C C   . LYS C 1 71 ? 19.147  -25.756 7.574   1.00 35.26  ? 70  LYS C C   1 
ATOM   1960 O O   . LYS C 1 71 ? 19.261  -26.732 8.333   1.00 37.44  ? 70  LYS C O   1 
ATOM   1961 C CB  . LYS C 1 71 ? 21.271  -24.705 6.775   1.00 34.00  ? 70  LYS C CB  1 
ATOM   1962 C CG  . LYS C 1 71 ? 22.224  -25.753 7.265   1.00 40.60  ? 70  LYS C CG  1 
ATOM   1963 C CD  . LYS C 1 71 ? 23.537  -25.933 6.510   1.00 44.94  ? 70  LYS C CD  1 
ATOM   1964 C CE  . LYS C 1 71 ? 24.217  -27.157 7.052   1.00 49.16  ? 70  LYS C CE  1 
ATOM   1965 N N   . PRO C 1 72 ? 18.194  -25.737 6.628   1.00 30.08  ? 71  PRO C N   1 
ATOM   1966 C CA  . PRO C 1 72 ? 17.279  -26.859 6.507   1.00 26.67  ? 71  PRO C CA  1 
ATOM   1967 C C   . PRO C 1 72 ? 17.953  -28.181 6.175   1.00 29.78  ? 71  PRO C C   1 
ATOM   1968 O O   . PRO C 1 72 ? 19.008  -28.256 5.515   1.00 33.07  ? 71  PRO C O   1 
ATOM   1969 C CB  . PRO C 1 72 ? 16.303  -26.430 5.404   1.00 27.39  ? 71  PRO C CB  1 
ATOM   1970 C CG  . PRO C 1 72 ? 16.389  -24.940 5.482   1.00 27.53  ? 71  PRO C CG  1 
ATOM   1971 C CD  . PRO C 1 72 ? 17.843  -24.574 5.792   1.00 28.18  ? 71  PRO C CD  1 
ATOM   1972 N N   . ASN C 1 73 ? 17.241  -29.205 6.602   1.00 29.88  ? 72  ASN C N   1 
ATOM   1973 C CA  . ASN C 1 73 ? 17.535  -30.511 6.048   1.00 36.13  ? 72  ASN C CA  1 
ATOM   1974 C C   . ASN C 1 73 ? 16.321  -31.410 6.209   1.00 32.87  ? 72  ASN C C   1 
ATOM   1975 O O   . ASN C 1 73 ? 15.333  -31.090 6.875   1.00 35.22  ? 72  ASN C O   1 
ATOM   1976 C CB  . ASN C 1 73 ? 18.920  -31.054 6.402   1.00 42.87  ? 72  ASN C CB  1 
ATOM   1977 C CG  . ASN C 1 73 ? 18.975  -31.751 7.735   1.00 42.29  ? 72  ASN C CG  1 
ATOM   1978 O OD1 . ASN C 1 73 ? 18.300  -32.766 7.930   1.00 39.78  ? 72  ASN C OD1 1 
ATOM   1979 N ND2 . ASN C 1 73 ? 19.869  -31.303 8.597   1.00 45.80  ? 72  ASN C ND2 1 
ATOM   1980 N N   . LYS C 1 74 ? 16.427  -32.572 5.575   1.00 32.14  ? 73  LYS C N   1 
ATOM   1981 C CA  . LYS C 1 74 ? 15.229  -33.342 5.296   1.00 29.60  ? 73  LYS C CA  1 
ATOM   1982 C C   . LYS C 1 74 ? 14.965  -34.324 6.425   1.00 30.69  ? 73  LYS C C   1 
ATOM   1983 O O   . LYS C 1 74 ? 13.912  -34.964 6.456   1.00 36.13  ? 73  LYS C O   1 
ATOM   1984 C CB  . LYS C 1 74 ? 15.467  -33.988 3.924   1.00 36.42  ? 73  LYS C CB  1 
ATOM   1985 C CG  . LYS C 1 74 ? 15.373  -33.028 2.705   1.00 40.50  ? 73  LYS C CG  1 
ATOM   1986 N N   . ARG C 1 75 ? 15.872  -34.382 7.420   1.00 28.41  ? 74  ARG C N   1 
ATOM   1987 C CA  . ARG C 1 75 ? 15.662  -35.345 8.500   1.00 29.02  ? 74  ARG C CA  1 
ATOM   1988 C C   . ARG C 1 75 ? 14.371  -35.044 9.275   1.00 30.25  ? 74  ARG C C   1 
ATOM   1989 O O   . ARG C 1 75 ? 14.009  -33.876 9.480   1.00 30.47  ? 74  ARG C O   1 
ATOM   1990 C CB  . ARG C 1 75 ? 16.924  -35.388 9.391   1.00 31.98  ? 74  ARG C CB  1 
ATOM   1991 C CG  . ARG C 1 75 ? 18.229  -35.675 8.647   1.00 36.87  ? 74  ARG C CG  1 
ATOM   1992 C CD  . ARG C 1 75 ? 18.528  -37.075 8.075   1.00 40.79  ? 74  ARG C CD  1 
ATOM   1993 N NE  . ARG C 1 75 ? 18.529  -37.982 9.218   1.00 35.61  ? 74  ARG C NE  1 
ATOM   1994 C CZ  . ARG C 1 75 ? 19.656  -38.434 9.821   1.00 31.67  ? 74  ARG C CZ  1 
ATOM   1995 N NH1 . ARG C 1 75 ? 19.539  -39.019 10.988  1.00 33.32  ? 74  ARG C NH1 1 
ATOM   1996 N NH2 . ARG C 1 75 ? 20.827  -38.170 9.290   1.00 34.25  ? 74  ARG C NH2 1 
ATOM   1997 N N   . LYS C 1 76 ? 13.655  -36.101 9.697   1.00 32.41  ? 75  LYS C N   1 
ATOM   1998 C CA  . LYS C 1 76 ? 12.387  -35.985 10.402  1.00 36.44  ? 75  LYS C CA  1 
ATOM   1999 C C   . LYS C 1 76 ? 12.472  -35.008 11.570  1.00 36.15  ? 75  LYS C C   1 
ATOM   2000 O O   . LYS C 1 76 ? 13.227  -35.193 12.534  1.00 32.79  ? 75  LYS C O   1 
ATOM   2001 C CB  . LYS C 1 76 ? 11.770  -37.332 10.819  1.00 35.82  ? 75  LYS C CB  1 
ATOM   2002 C CG  . LYS C 1 76 ? 10.309  -37.261 11.194  1.00 38.07  ? 75  LYS C CG  1 
ATOM   2003 C CD  . LYS C 1 76 ? 9.676   -38.641 11.352  1.00 48.77  ? 75  LYS C CD  1 
ATOM   2004 N N   . GLY C 1 77 ? 11.682  -33.935 11.440  1.00 36.40  ? 76  GLY C N   1 
ATOM   2005 C CA  . GLY C 1 77 ? 11.392  -33.031 12.541  1.00 30.21  ? 76  GLY C CA  1 
ATOM   2006 C C   . GLY C 1 77 ? 12.402  -31.877 12.598  1.00 26.87  ? 76  GLY C C   1 
ATOM   2007 O O   . GLY C 1 77 ? 12.266  -30.962 13.402  1.00 34.46  ? 76  GLY C O   1 
ATOM   2008 N N   . PHE C 1 78 ? 13.376  -31.888 11.689  1.00 28.59  ? 77  PHE C N   1 
ATOM   2009 C CA  . PHE C 1 78 ? 14.473  -30.944 11.790  1.00 27.38  ? 77  PHE C CA  1 
ATOM   2010 C C   . PHE C 1 78 ? 13.969  -29.522 11.519  1.00 28.75  ? 77  PHE C C   1 
ATOM   2011 O O   . PHE C 1 78 ? 14.308  -28.567 12.219  1.00 26.78  ? 77  PHE C O   1 
ATOM   2012 C CB  . PHE C 1 78 ? 15.589  -31.325 10.821  1.00 31.36  ? 77  PHE C CB  1 
ATOM   2013 C CG  . PHE C 1 78 ? 16.869  -30.553 11.089  1.00 31.33  ? 77  PHE C CG  1 
ATOM   2014 C CD1 . PHE C 1 78 ? 17.062  -29.273 10.560  1.00 31.31  ? 77  PHE C CD1 1 
ATOM   2015 C CD2 . PHE C 1 78 ? 17.918  -31.125 11.809  1.00 28.61  ? 77  PHE C CD2 1 
ATOM   2016 C CE1 . PHE C 1 78 ? 18.242  -28.579 10.781  1.00 31.01  ? 77  PHE C CE1 1 
ATOM   2017 C CE2 . PHE C 1 78 ? 19.100  -30.420 12.032  1.00 27.49  ? 77  PHE C CE2 1 
ATOM   2018 C CZ  . PHE C 1 78 ? 19.292  -29.165 11.487  1.00 29.03  ? 77  PHE C CZ  1 
ATOM   2019 N N   . ASN C 1 79 ? 13.182  -29.394 10.441  1.00 31.66  ? 78  ASN C N   1 
ATOM   2020 C CA  . ASN C 1 79 ? 12.858  -28.040 10.016  1.00 33.44  ? 78  ASN C CA  1 
ATOM   2021 C C   . ASN C 1 79 ? 11.857  -27.390 10.962  1.00 30.28  ? 78  ASN C C   1 
ATOM   2022 O O   . ASN C 1 79 ? 11.916  -26.174 11.237  1.00 29.51  ? 78  ASN C O   1 
ATOM   2023 C CB  . ASN C 1 79 ? 12.377  -27.989 8.577   1.00 29.82  ? 78  ASN C CB  1 
ATOM   2024 C CG  . ASN C 1 79 ? 13.484  -28.339 7.608   1.00 29.19  ? 78  ASN C CG  1 
ATOM   2025 O OD1 . ASN C 1 79 ? 14.652  -28.092 7.893   1.00 27.91  ? 78  ASN C OD1 1 
ATOM   2026 N ND2 . ASN C 1 79 ? 13.152  -28.983 6.492   1.00 31.84  ? 78  ASN C ND2 1 
ATOM   2027 N N   . GLU C 1 80 ? 10.939  -28.196 11.479  1.00 30.50  ? 79  GLU C N   1 
ATOM   2028 C CA  . GLU C 1 80 ? 10.116  -27.687 12.561  1.00 31.53  ? 79  GLU C CA  1 
ATOM   2029 C C   . GLU C 1 80 ? 10.998  -27.296 13.751  1.00 37.61  ? 79  GLU C C   1 
ATOM   2030 O O   . GLU C 1 80 ? 10.742  -26.291 14.412  1.00 32.64  ? 79  GLU C O   1 
ATOM   2031 C CB  . GLU C 1 80 ? 8.960   -28.647 12.840  1.00 37.53  ? 79  GLU C CB  1 
ATOM   2032 C CG  . GLU C 1 80 ? 8.133   -28.238 14.050  1.00 36.51  ? 79  GLU C CG  1 
ATOM   2033 C CD  . GLU C 1 80 ? 6.950   -29.158 14.290  1.00 49.31  ? 79  GLU C CD  1 
ATOM   2034 O OE1 . GLU C 1 80 ? 7.136   -30.385 14.166  1.00 56.02  ? 79  GLU C OE1 1 
ATOM   2035 O OE2 . GLU C 1 80 ? 5.852   -28.661 14.605  1.00 47.04  ? 79  GLU C OE2 1 
ATOM   2036 N N   . GLY C 1 81 ? 12.047  -28.090 14.037  1.00 32.48  ? 80  GLY C N   1 
ATOM   2037 C CA  . GLY C 1 81 ? 12.967  -27.690 15.096  1.00 33.14  ? 80  GLY C CA  1 
ATOM   2038 C C   . GLY C 1 81 ? 13.643  -26.336 14.849  1.00 30.22  ? 80  GLY C C   1 
ATOM   2039 O O   . GLY C 1 81 ? 13.828  -25.576 15.793  1.00 31.76  ? 80  GLY C O   1 
ATOM   2040 N N   . LEU C 1 82 ? 14.114  -26.069 13.605  1.00 29.27  ? 81  LEU C N   1 
ATOM   2041 C CA  . LEU C 1 82 ? 14.668  -24.756 13.273  1.00 32.10  ? 81  LEU C CA  1 
ATOM   2042 C C   . LEU C 1 82 ? 13.627  -23.669 13.568  1.00 30.09  ? 81  LEU C C   1 
ATOM   2043 O O   . LEU C 1 82 ? 13.962  -22.591 14.078  1.00 31.56  ? 81  LEU C O   1 
ATOM   2044 C CB  . LEU C 1 82 ? 15.082  -24.709 11.805  1.00 32.36  ? 81  LEU C CB  1 
ATOM   2045 C CG  . LEU C 1 82 ? 16.308  -25.536 11.427  1.00 28.23  ? 81  LEU C CG  1 
ATOM   2046 C CD1 . LEU C 1 82 ? 16.632  -25.375 9.969   1.00 29.43  ? 81  LEU C CD1 1 
ATOM   2047 C CD2 . LEU C 1 82 ? 17.519  -25.159 12.242  1.00 25.00  ? 81  LEU C CD2 1 
ATOM   2048 N N   . TRP C 1 83 ? 12.368  -23.922 13.217  1.00 30.74  ? 82  TRP C N   1 
ATOM   2049 C CA  . TRP C 1 83 ? 11.380  -22.878 13.462  1.00 36.14  ? 82  TRP C CA  1 
ATOM   2050 C C   . TRP C 1 83 ? 11.272  -22.600 14.971  1.00 37.91  ? 82  TRP C C   1 
ATOM   2051 O O   . TRP C 1 83 ? 11.328  -21.444 15.398  1.00 36.35  ? 82  TRP C O   1 
ATOM   2052 C CB  . TRP C 1 83 ? 10.009  -23.235 12.865  1.00 35.33  ? 82  TRP C CB  1 
ATOM   2053 C CG  . TRP C 1 83 ? 9.027   -22.093 12.993  1.00 37.38  ? 82  TRP C CG  1 
ATOM   2054 C CD1 . TRP C 1 83 ? 8.831   -21.086 12.082  1.00 36.46  ? 82  TRP C CD1 1 
ATOM   2055 C CD2 . TRP C 1 83 ? 8.153   -21.798 14.108  1.00 42.50  ? 82  TRP C CD2 1 
ATOM   2056 N NE1 . TRP C 1 83 ? 7.867   -20.219 12.530  1.00 36.18  ? 82  TRP C NE1 1 
ATOM   2057 C CE2 . TRP C 1 83 ? 7.432   -20.623 13.763  1.00 40.32  ? 82  TRP C CE2 1 
ATOM   2058 C CE3 . TRP C 1 83 ? 7.901   -22.409 15.349  1.00 39.90  ? 82  TRP C CE3 1 
ATOM   2059 C CZ2 . TRP C 1 83 ? 6.490   -20.051 14.616  1.00 47.40  ? 82  TRP C CZ2 1 
ATOM   2060 C CZ3 . TRP C 1 83 ? 6.965   -21.842 16.188  1.00 49.33  ? 82  TRP C CZ3 1 
ATOM   2061 C CH2 . TRP C 1 83 ? 6.278   -20.681 15.825  1.00 44.31  ? 82  TRP C CH2 1 
ATOM   2062 N N   . GLU C 1 84 ? 11.184  -23.672 15.774  1.00 32.33  ? 83  GLU C N   1 
ATOM   2063 C CA  . GLU C 1 84 ? 11.078  -23.539 17.224  1.00 37.16  ? 83  GLU C CA  1 
ATOM   2064 C C   . GLU C 1 84 ? 12.258  -22.788 17.853  1.00 34.95  ? 83  GLU C C   1 
ATOM   2065 O O   . GLU C 1 84 ? 12.061  -21.877 18.672  1.00 38.10  ? 83  GLU C O   1 
ATOM   2066 C CB  . GLU C 1 84 ? 10.872  -24.895 17.901  1.00 33.87  ? 83  GLU C CB  1 
ATOM   2067 C CG  . GLU C 1 84 ? 9.544   -25.554 17.553  1.00 36.95  ? 83  GLU C CG  1 
ATOM   2068 C CD  . GLU C 1 84 ? 9.452   -26.984 18.039  1.00 41.71  ? 83  GLU C CD  1 
ATOM   2069 O OE1 . GLU C 1 84 ? 10.430  -27.533 18.619  1.00 39.39  ? 83  GLU C OE1 1 
ATOM   2070 O OE2 . GLU C 1 84 ? 8.380   -27.550 17.817  1.00 43.14  ? 83  GLU C OE2 1 
ATOM   2071 N N   . ILE C 1 85 ? 13.504  -23.178 17.554  1.00 33.83  ? 84  ILE C N   1 
ATOM   2072 C CA  . ILE C 1 85 ? 14.646  -22.538 18.189  1.00 36.40  ? 84  ILE C CA  1 
ATOM   2073 C C   . ILE C 1 85 ? 14.674  -21.029 17.907  1.00 37.39  ? 84  ILE C C   1 
ATOM   2074 O O   . ILE C 1 85 ? 15.116  -20.264 18.758  1.00 36.15  ? 84  ILE C O   1 
ATOM   2075 C CB  . ILE C 1 85 ? 15.965  -23.249 17.845  1.00 33.68  ? 84  ILE C CB  1 
ATOM   2076 C CG1 . ILE C 1 85 ? 17.046  -22.898 18.866  1.00 34.77  ? 84  ILE C CG1 1 
ATOM   2077 C CG2 . ILE C 1 85 ? 16.398  -22.977 16.396  1.00 34.95  ? 84  ILE C CG2 1 
ATOM   2078 C CD1 . ILE C 1 85 ? 18.234  -23.848 18.922  1.00 33.08  ? 84  ILE C CD1 1 
ATOM   2079 N N   . GLN C 1 86 ? 14.182  -20.612 16.725  1.00 32.48  ? 85  GLN C N   1 
ATOM   2080 C CA  . GLN C 1 86 ? 14.274  -19.204 16.341  1.00 39.58  ? 85  GLN C CA  1 
ATOM   2081 C C   . GLN C 1 86 ? 13.059  -18.418 16.837  1.00 37.73  ? 85  GLN C C   1 
ATOM   2082 O O   . GLN C 1 86 ? 13.193  -17.237 17.158  1.00 43.34  ? 85  GLN C O   1 
ATOM   2083 C CB  . GLN C 1 86 ? 14.388  -19.046 14.819  1.00 37.36  ? 85  GLN C CB  1 
ATOM   2084 C CG  . GLN C 1 86 ? 14.634  -17.614 14.322  1.00 33.54  ? 85  GLN C CG  1 
ATOM   2085 C CD  . GLN C 1 86 ? 14.995  -17.571 12.847  1.00 38.70  ? 85  GLN C CD  1 
ATOM   2086 O OE1 . GLN C 1 86 ? 14.851  -18.554 12.101  1.00 35.04  ? 85  GLN C OE1 1 
ATOM   2087 N NE2 . GLN C 1 86 ? 15.539  -16.439 12.417  1.00 41.29  ? 85  GLN C NE2 1 
ATOM   2088 N N   . ASN C 1 87 ? 11.894  -19.062 16.908  1.00 38.30  ? 86  ASN C N   1 
ATOM   2089 C CA  . ASN C 1 87 ? 10.641  -18.344 17.081  1.00 40.64  ? 86  ASN C CA  1 
ATOM   2090 C C   . ASN C 1 87 ? 10.020  -18.570 18.460  1.00 44.90  ? 86  ASN C C   1 
ATOM   2091 O O   . ASN C 1 87 ? 9.383   -17.661 18.988  1.00 46.47  ? 86  ASN C O   1 
ATOM   2092 C CB  . ASN C 1 87 ? 9.644   -18.624 15.963  1.00 40.06  ? 86  ASN C CB  1 
ATOM   2093 C CG  . ASN C 1 87 ? 10.182  -18.072 14.672  1.00 46.07  ? 86  ASN C CG  1 
ATOM   2094 O OD1 . ASN C 1 87 ? 10.246  -16.849 14.515  1.00 42.08  ? 86  ASN C OD1 1 
ATOM   2095 N ND2 . ASN C 1 87 ? 10.663  -18.932 13.789  1.00 39.42  ? 86  ASN C ND2 1 
ATOM   2096 N N   . ASN C 1 88 ? 10.213  -19.761 19.042  1.00 42.94  ? 87  ASN C N   1 
ATOM   2097 C CA  . ASN C 1 88 ? 9.488   -20.110 20.257  1.00 42.21  ? 87  ASN C CA  1 
ATOM   2098 C C   . ASN C 1 88 ? 10.332  -21.019 21.158  1.00 41.61  ? 87  ASN C C   1 
ATOM   2099 O O   . ASN C 1 88 ? 9.855   -22.092 21.561  1.00 45.52  ? 87  ASN C O   1 
ATOM   2100 C CB  . ASN C 1 88 ? 8.143   -20.737 19.912  1.00 48.29  ? 87  ASN C CB  1 
ATOM   2101 C CG  . ASN C 1 88 ? 7.215   -20.746 21.106  1.00 51.61  ? 87  ASN C CG  1 
ATOM   2102 O OD1 . ASN C 1 88 ? 7.500   -20.093 22.119  1.00 57.16  ? 87  ASN C OD1 1 
ATOM   2103 N ND2 . ASN C 1 88 ? 6.103   -21.452 20.990  1.00 51.38  ? 87  ASN C ND2 1 
ATOM   2104 N N   . PRO C 1 89 ? 11.592  -20.630 21.464  1.00 37.45  ? 88  PRO C N   1 
ATOM   2105 C CA  . PRO C 1 89 ? 12.572  -21.539 22.079  1.00 42.05  ? 88  PRO C CA  1 
ATOM   2106 C C   . PRO C 1 89 ? 12.352  -21.971 23.528  1.00 48.49  ? 88  PRO C C   1 
ATOM   2107 O O   . PRO C 1 89 ? 12.989  -22.922 23.981  1.00 44.62  ? 88  PRO C O   1 
ATOM   2108 C CB  . PRO C 1 89 ? 13.912  -20.818 21.948  1.00 38.84  ? 88  PRO C CB  1 
ATOM   2109 C CG  . PRO C 1 89 ? 13.512  -19.345 21.904  1.00 45.03  ? 88  PRO C CG  1 
ATOM   2110 C CD  . PRO C 1 89 ? 12.182  -19.315 21.160  1.00 37.87  ? 88  PRO C CD  1 
ATOM   2111 N N   . HIS C 1 90 ? 11.466  -21.265 24.243  1.00 51.66  ? 89  HIS C N   1 
ATOM   2112 C CA  . HIS C 1 90 ? 11.290  -21.502 25.670  1.00 50.38  ? 89  HIS C CA  1 
ATOM   2113 C C   . HIS C 1 90 ? 9.867   -21.951 26.006  1.00 54.48  ? 89  HIS C C   1 
ATOM   2114 O O   . HIS C 1 90 ? 9.496   -21.964 27.172  1.00 58.99  ? 89  HIS C O   1 
ATOM   2115 C CB  . HIS C 1 90 ? 11.830  -20.322 26.484  1.00 41.72  ? 89  HIS C CB  1 
ATOM   2116 C CG  . HIS C 1 90 ? 13.288  -20.035 26.279  1.00 38.22  ? 89  HIS C CG  1 
ATOM   2117 N ND1 . HIS C 1 90 ? 13.766  -18.868 25.723  1.00 40.16  ? 89  HIS C ND1 1 
ATOM   2118 C CD2 . HIS C 1 90 ? 14.389  -20.748 26.615  1.00 42.08  ? 89  HIS C CD2 1 
ATOM   2119 C CE1 . HIS C 1 90 ? 15.096  -18.885 25.684  1.00 42.19  ? 89  HIS C CE1 1 
ATOM   2120 N NE2 . HIS C 1 90 ? 15.499  -20.020 26.242  1.00 43.48  ? 89  HIS C NE2 1 
ATOM   2121 N N   . ALA C 1 91 ? 9.079   -22.348 25.001  1.00 55.90  ? 90  ALA C N   1 
ATOM   2122 C CA  . ALA C 1 91 ? 7.755   -22.916 25.224  1.00 58.11  ? 90  ALA C CA  1 
ATOM   2123 C C   . ALA C 1 91 ? 7.837   -24.360 25.730  1.00 63.75  ? 90  ALA C C   1 
ATOM   2124 O O   . ALA C 1 91 ? 8.880   -25.008 25.658  1.00 64.80  ? 90  ALA C O   1 
ATOM   2125 C CB  . ALA C 1 91 ? 6.908   -22.817 23.971  1.00 57.48  ? 90  ALA C CB  1 
ATOM   2126 N N   . SER C 1 92 ? 6.688   -24.871 26.191  1.00 71.43  ? 91  SER C N   1 
ATOM   2127 C CA  . SER C 1 92 ? 6.572   -26.118 26.935  1.00 72.34  ? 91  SER C CA  1 
ATOM   2128 C C   . SER C 1 92 ? 6.845   -27.345 26.074  1.00 68.77  ? 91  SER C C   1 
ATOM   2129 O O   . SER C 1 92 ? 7.675   -28.175 26.433  1.00 74.10  ? 91  SER C O   1 
ATOM   2130 C CB  . SER C 1 92 ? 5.211   -26.236 27.577  1.00 66.28  ? 91  SER C CB  1 
ATOM   2131 O OG  . SER C 1 92 ? 5.191   -25.501 28.787  1.00 71.74  ? 91  SER C OG  1 
ATOM   2132 N N   . TYR C 1 93 ? 6.078   -27.480 24.987  1.00 68.68  ? 92  TYR C N   1 
ATOM   2133 C CA  . TYR C 1 93 ? 6.035   -28.700 24.196  1.00 72.84  ? 92  TYR C CA  1 
ATOM   2134 C C   . TYR C 1 93 ? 5.727   -29.878 25.135  1.00 71.76  ? 92  TYR C C   1 
ATOM   2135 O O   . TYR C 1 93 ? 5.649   -31.023 24.649  1.00 78.47  ? 92  TYR C O   1 
ATOM   2136 C CB  . TYR C 1 93 ? 7.319   -28.840 23.364  1.00 68.77  ? 92  TYR C CB  1 
ATOM   2137 C CG  . TYR C 1 93 ? 7.692   -27.591 22.570  1.00 60.30  ? 92  TYR C CG  1 
ATOM   2138 C CD1 . TYR C 1 93 ? 7.040   -27.265 21.381  1.00 54.67  ? 92  TYR C CD1 1 
ATOM   2139 C CD2 . TYR C 1 93 ? 8.694   -26.737 23.016  1.00 55.23  ? 92  TYR C CD2 1 
ATOM   2140 C CE1 . TYR C 1 93 ? 7.367   -26.125 20.665  1.00 56.81  ? 92  TYR C CE1 1 
ATOM   2141 C CE2 . TYR C 1 93 ? 9.028   -25.593 22.306  1.00 57.78  ? 92  TYR C CE2 1 
ATOM   2142 C CZ  . TYR C 1 93 ? 8.371   -25.288 21.126  1.00 60.51  ? 92  TYR C CZ  1 
ATOM   2143 O OH  . TYR C 1 93 ? 8.722   -24.153 20.438  1.00 62.32  ? 92  TYR C OH  1 
HETATM 2144 S S   . SO4 D 2 .  ? 1.699   -33.679 1.936   1.00 99.14  ? 101 SO4 A S   1 
HETATM 2145 O O1  . SO4 D 2 .  ? 2.357   -34.561 1.000   1.00 76.24  ? 101 SO4 A O1  1 
HETATM 2146 O O2  . SO4 D 2 .  ? 1.628   -32.349 1.387   1.00 89.29  ? 101 SO4 A O2  1 
HETATM 2147 O O3  . SO4 D 2 .  ? 0.366   -34.163 2.193   1.00 105.37 ? 101 SO4 A O3  1 
HETATM 2148 O O4  . SO4 D 2 .  ? 2.442   -33.647 3.168   1.00 98.73  ? 101 SO4 A O4  1 
HETATM 2149 S S   . SO4 E 2 .  ? -8.974  -24.827 1.421   1.00 93.25  ? 102 SO4 A S   1 
HETATM 2150 O O1  . SO4 E 2 .  ? -9.610  -24.322 0.229   1.00 73.73  ? 102 SO4 A O1  1 
HETATM 2151 O O2  . SO4 E 2 .  ? -9.071  -23.850 2.478   1.00 81.70  ? 102 SO4 A O2  1 
HETATM 2152 O O3  . SO4 E 2 .  ? -9.607  -26.056 1.834   1.00 93.04  ? 102 SO4 A O3  1 
HETATM 2153 O O4  . SO4 E 2 .  ? -7.589  -25.088 1.151   1.00 101.45 ? 102 SO4 A O4  1 
HETATM 2154 C C1  . EDO F 3 .  ? 14.318  -19.618 -7.372  1.00 35.61  ? 103 EDO A C1  1 
HETATM 2155 O O1  . EDO F 3 .  ? 15.530  -18.930 -7.169  1.00 33.66  ? 103 EDO A O1  1 
HETATM 2156 C C2  . EDO F 3 .  ? 13.461  -19.136 -8.514  1.00 36.79  ? 103 EDO A C2  1 
HETATM 2157 O O2  . EDO F 3 .  ? 12.897  -17.855 -8.310  1.00 32.50  ? 103 EDO A O2  1 
HETATM 2158 S S   . SO4 G 2 .  ? 9.366   -29.601 5.829   1.00 57.81  ? 104 SO4 A S   1 
HETATM 2159 O O1  . SO4 G 2 .  ? 10.147  -28.858 4.920   1.00 44.77  ? 104 SO4 A O1  1 
HETATM 2160 O O2  . SO4 G 2 .  ? 8.799   -30.749 5.121   1.00 58.50  ? 104 SO4 A O2  1 
HETATM 2161 O O3  . SO4 G 2 .  ? 10.196  -30.065 6.931   1.00 61.64  ? 104 SO4 A O3  1 
HETATM 2162 O O4  . SO4 G 2 .  ? 8.290   -28.767 6.319   1.00 67.01  ? 104 SO4 A O4  1 
HETATM 2163 S S   . SO4 H 2 .  ? 7.545   -8.562  -25.012 1.00 73.93  ? 101 SO4 B S   1 
HETATM 2164 O O1  . SO4 H 2 .  ? 8.709   -8.461  -25.865 1.00 44.03  ? 101 SO4 B O1  1 
HETATM 2165 O O2  . SO4 H 2 .  ? 6.490   -9.301  -25.670 1.00 56.70  ? 101 SO4 B O2  1 
HETATM 2166 O O3  . SO4 H 2 .  ? 7.865   -9.247  -23.764 1.00 52.66  ? 101 SO4 B O3  1 
HETATM 2167 O O4  . SO4 H 2 .  ? 7.125   -7.205  -24.742 1.00 69.22  ? 101 SO4 B O4  1 
HETATM 2168 S S   . SO4 I 2 .  ? 14.550  -27.059 -26.804 1.00 56.13  ? 102 SO4 B S   1 
HETATM 2169 O O1  . SO4 I 2 .  ? 15.780  -26.487 -26.334 1.00 62.64  ? 102 SO4 B O1  1 
HETATM 2170 O O2  . SO4 I 2 .  ? 14.851  -28.289 -27.503 1.00 70.87  ? 102 SO4 B O2  1 
HETATM 2171 O O3  . SO4 I 2 .  ? 13.685  -27.361 -25.692 1.00 71.89  ? 102 SO4 B O3  1 
HETATM 2172 O O4  . SO4 I 2 .  ? 13.887  -26.134 -27.691 1.00 53.96  ? 102 SO4 B O4  1 
HETATM 2173 C C13 . T0Y J 4 .  ? 21.985  -16.107 -24.022 0.70 58.76  ? 103 T0Y B C13 1 
HETATM 2174 C C02 . T0Y J 4 .  ? 22.892  -15.770 -22.862 0.70 57.48  ? 103 T0Y B C02 1 
HETATM 2175 C C03 . T0Y J 4 .  ? 22.091  -15.619 -21.584 0.70 56.56  ? 103 T0Y B C03 1 
HETATM 2176 C C04 . T0Y J 4 .  ? 20.819  -16.473 -21.626 0.70 51.33  ? 103 T0Y B C04 1 
HETATM 2177 C C06 . T0Y J 4 .  ? 18.963  -17.077 -23.073 0.70 41.66  ? 103 T0Y B C06 1 
HETATM 2178 C C07 . T0Y J 4 .  ? 17.966  -16.659 -24.125 0.70 29.44  ? 103 T0Y B C07 1 
HETATM 2179 C C08 . T0Y J 4 .  ? 16.859  -15.780 -23.979 0.70 30.75  ? 103 T0Y B C08 1 
HETATM 2180 C C09 . T0Y J 4 .  ? 16.134  -15.626 -25.127 0.70 31.89  ? 103 T0Y B C09 1 
HETATM 2181 C C11 . T0Y J 4 .  ? 18.064  -17.142 -25.395 0.70 33.46  ? 103 T0Y B C11 1 
HETATM 2182 C C12 . T0Y J 4 .  ? 20.621  -15.464 -23.845 0.70 50.89  ? 103 T0Y B C12 1 
HETATM 2183 N N05 . T0Y J 4 .  ? 19.889  -16.015 -22.675 0.70 49.63  ? 103 T0Y B N05 1 
HETATM 2184 O O01 . T0Y J 4 .  ? 23.866  -16.803 -22.723 0.70 62.34  ? 103 T0Y B O01 1 
HETATM 2185 S S10 . T0Y J 4 .  ? 16.831  -16.583 -26.400 0.70 31.48  ? 103 T0Y B S10 1 
HETATM 2186 C C1  . EDO K 3 .  ? 17.013  -36.437 16.311  1.00 34.92  ? 101 EDO C C1  1 
HETATM 2187 O O1  . EDO K 3 .  ? 15.894  -37.158 15.787  1.00 38.84  ? 101 EDO C O1  1 
HETATM 2188 C C2  . EDO K 3 .  ? 16.624  -35.493 17.400  1.00 31.31  ? 101 EDO C C2  1 
HETATM 2189 O O2  . EDO K 3 .  ? 15.765  -36.050 18.364  1.00 32.20  ? 101 EDO C O2  1 
HETATM 2190 S S   . SO4 L 2 .  ? 29.737  -38.633 12.338  1.00 103.05 ? 102 SO4 C S   1 
HETATM 2191 O O1  . SO4 L 2 .  ? 30.679  -37.850 11.581  1.00 98.60  ? 102 SO4 C O1  1 
HETATM 2192 O O2  . SO4 L 2 .  ? 28.400  -38.229 11.999  1.00 91.93  ? 102 SO4 C O2  1 
HETATM 2193 O O3  . SO4 L 2 .  ? 29.899  -40.028 12.031  1.00 83.91  ? 102 SO4 C O3  1 
HETATM 2194 O O4  . SO4 L 2 .  ? 29.967  -38.419 13.747  1.00 105.04 ? 102 SO4 C O4  1 
HETATM 2195 O O   . HOH M 5 .  ? 9.546   -32.386 3.952   1.00 55.33  ? 201 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? 6.222   -29.132 6.947   1.00 50.77  ? 202 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? 4.009   2.349   0.238   1.00 58.17  ? 203 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? -5.448  -13.491 -16.688 1.00 48.82  ? 204 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? -1.997  -30.984 -3.809  1.00 48.50  ? 205 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? 4.305   -10.453 13.691  1.00 54.39  ? 206 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 13.400  -12.121 7.994   1.00 54.72  ? 207 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 11.331  -29.828 2.969   1.00 48.57  ? 208 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? 0.888   -10.670 -15.522 1.00 43.99  ? 209 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 9.426   -18.250 -10.938 1.00 36.65  ? 210 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? -1.969  3.134   -2.152  1.00 39.85  ? 211 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 16.250  -24.525 1.896   1.00 36.72  ? 212 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 11.513  -23.919 9.769   1.00 36.77  ? 213 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 7.264   -10.607 -12.112 1.00 37.65  ? 214 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 4.911   -7.924  1.209   1.00 31.79  ? 215 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? -0.154  -29.586 10.086  1.00 53.53  ? 216 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 10.901  -9.553  -13.500 1.00 59.76  ? 217 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? -3.452  -10.901 6.721   1.00 39.03  ? 218 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 2.770   -25.264 -6.511  1.00 50.73  ? 219 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 0.619   -33.793 5.097   1.00 52.24  ? 220 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.741   -22.894 -9.513  1.00 41.45  ? 221 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 15.312  -17.319 -19.256 1.00 40.10  ? 222 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 4.779   -3.588  -3.276  1.00 34.45  ? 223 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? -7.515  -17.176 6.807   1.00 43.51  ? 224 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -5.422  -16.013 -8.013  1.00 27.60  ? 225 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 4.551   -34.858 4.400   1.00 60.45  ? 226 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 11.235  -5.250  -7.818  1.00 33.25  ? 227 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 3.645   -29.709 -0.564  1.00 41.69  ? 228 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 16.070  -12.183 -5.315  1.00 34.35  ? 229 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 10.004  -6.115  -1.710  1.00 34.37  ? 230 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 11.917  -16.411 -15.017 1.00 39.51  ? 231 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 2.023   0.491   -7.494  1.00 40.73  ? 232 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 20.257  -15.498 7.314   1.00 28.34  ? 233 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 13.657  -12.057 -4.237  1.00 24.27  ? 234 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -0.260  -21.063 6.996   1.00 34.38  ? 235 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 11.823  -11.998 5.937   1.00 36.77  ? 236 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 14.344  -15.668 -9.221  1.00 38.04  ? 237 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 0.674   -23.441 9.205   1.00 48.26  ? 238 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? -7.458  -16.723 1.656   1.00 40.39  ? 239 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? -7.722  -15.827 -0.999  1.00 35.51  ? 240 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 17.532  -12.911 1.338   1.00 21.87  ? 241 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? -5.502  -19.888 -5.581  1.00 37.34  ? 242 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 8.384   -17.505 8.657   1.00 41.52  ? 243 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 9.114   -16.315 -13.147 1.00 37.74  ? 244 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -3.763  -21.302 6.108   1.00 39.64  ? 245 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 11.825  -12.409 -6.167  1.00 27.79  ? 246 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 21.934  -20.258 -3.795  1.00 51.44  ? 247 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 1.927   -18.678 -18.705 1.00 44.76  ? 248 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 8.724   -17.890 -15.839 1.00 53.52  ? 249 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -4.167  -25.941 -5.599  1.00 44.37  ? 250 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -1.396  -22.094 -0.634  1.00 27.06  ? 251 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 9.346   -2.454  -0.450  1.00 61.77  ? 252 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 2.832   -25.328 -9.952  1.00 37.61  ? 253 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 16.906  -11.917 -17.313 1.00 39.19  ? 254 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 2.095   -4.656  -10.288 1.00 37.62  ? 255 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -0.225  -20.709 11.275  1.00 66.11  ? 256 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 13.384  -9.438  -7.207  1.00 44.46  ? 257 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 11.659  -6.069  -3.879  1.00 49.56  ? 258 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 2.843   -6.487  5.496   1.00 36.94  ? 259 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -1.065  -11.895 11.378  1.00 38.84  ? 260 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 10.366  -13.098 9.704   1.00 37.32  ? 261 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 8.245   -7.869  1.209   1.00 31.44  ? 262 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? -8.213  -21.293 -1.205  1.00 42.52  ? 263 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 5.440   -7.729  4.029   1.00 35.47  ? 264 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 13.883  -28.340 -4.806  1.00 56.88  ? 265 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 14.742  -29.577 3.942   1.00 42.84  ? 266 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 1.988   -10.578 11.684  1.00 35.56  ? 267 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 13.272  -13.630 -8.258  1.00 44.66  ? 268 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 9.849   -20.260 -18.534 1.00 45.27  ? 269 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -5.984  -11.824 -11.301 1.00 41.52  ? 270 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? -5.920  -12.850 6.709   1.00 41.20  ? 271 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 12.474  -16.117 -11.909 1.00 61.85  ? 272 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? -1.231  -7.584  11.548  1.00 43.14  ? 273 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 6.461   -16.385 -15.037 1.00 47.51  ? 274 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 6.846   -6.071  0.491   1.00 46.26  ? 275 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 2.201   -24.905 14.618  1.00 46.94  ? 276 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 10.449  -27.642 -7.340  1.00 52.67  ? 277 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 15.456  -13.621 10.481  1.00 51.60  ? 278 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 0.571   -28.991 -6.934  1.00 75.42  ? 279 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -10.464 -16.200 -3.600  1.00 57.07  ? 280 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 16.019  -28.278 -0.660  1.00 54.17  ? 281 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 21.747  -16.813 -3.559  1.00 32.21  ? 282 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 3.242   -9.806  -13.292 1.00 47.07  ? 283 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? -6.978  -11.531 -7.938  1.00 28.83  ? 284 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? -7.189  -21.516 -5.747  1.00 60.29  ? 285 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 11.406  -7.898  0.361   1.00 29.09  ? 286 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -7.792  -19.712 -3.436  1.00 55.96  ? 287 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? -3.563  -26.610 7.504   1.00 55.23  ? 288 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 22.779  -16.678 -0.501  1.00 40.14  ? 289 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 17.730  -18.236 -9.676  1.00 53.72  ? 290 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -5.135  -23.701 -6.739  1.00 39.55  ? 291 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -3.457  -7.907  10.548  1.00 51.22  ? 292 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? -5.711  -26.691 3.499   1.00 51.31  ? 293 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 0.262   -8.179  -13.238 1.00 46.50  ? 294 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 8.917   -9.130  -13.829 1.00 38.02  ? 295 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 17.172  -9.938  -9.448  1.00 50.77  ? 296 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -7.011  -14.176 -9.283  1.00 38.58  ? 297 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -5.557  -22.218 6.200   1.00 58.19  ? 298 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -9.856  -28.479 -1.799  1.00 54.45  ? 299 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? -0.531  -3.235  -11.093 1.00 60.01  ? 300 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 11.727  -1.998  -1.749  1.00 47.02  ? 301 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 8.447   -8.332  4.522   1.00 36.42  ? 302 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? -11.042 -13.572 -2.822  1.00 43.60  ? 303 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -2.728  -21.486 7.948   1.00 47.95  ? 304 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 4.955   -9.622  -11.348 1.00 43.09  ? 305 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 7.989   -30.692 -2.011  1.00 61.43  ? 306 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? -6.878  -19.327 8.474   1.00 49.02  ? 307 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? -4.696  -21.097 -8.225  1.00 48.44  ? 308 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? 4.702   -3.448  1.756   1.00 61.34  ? 309 HOH A O   1 
HETATM 2304 O O   . HOH N 5 .  ? 26.798  -12.160 -42.076 1.00 50.44  ? 201 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 10.151  -11.296 -38.307 1.00 54.30  ? 202 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 26.379  -22.864 -31.445 1.00 39.04  ? 203 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 6.129   -7.450  -32.260 1.00 48.42  ? 204 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 30.508  -19.718 -40.601 1.00 37.41  ? 205 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 20.345  -22.232 -23.586 1.00 40.70  ? 206 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 6.730   -12.345 -26.273 1.00 41.99  ? 207 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 3.117   -8.838  -27.459 1.00 58.89  ? 208 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 28.046  -7.944  -29.092 1.00 42.02  ? 209 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 8.498   -27.607 -38.528 1.00 55.68  ? 210 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 9.002   -8.758  -16.613 1.00 42.34  ? 211 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 30.573  -7.820  -30.208 1.00 50.70  ? 212 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 24.550  -1.610  -36.505 1.00 45.18  ? 213 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 18.483  -0.400  -25.559 1.00 58.86  ? 214 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 11.177  -7.924  -41.562 1.00 44.29  ? 215 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 7.160   -19.172 -35.350 1.00 52.73  ? 216 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 35.202  -22.609 -30.624 1.00 74.62  ? 217 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 21.932  3.731   -32.861 1.00 48.57  ? 218 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 13.108  -4.394  -42.111 1.00 52.69  ? 219 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 10.225  -16.771 -44.551 1.00 42.67  ? 220 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 20.829  -13.349 -43.018 1.00 41.00  ? 221 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 15.625  -25.524 -45.826 1.00 54.93  ? 222 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 25.210  -4.874  -30.166 1.00 40.21  ? 223 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 23.696  -2.105  -29.562 1.00 47.52  ? 224 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 17.662  -19.672 -42.299 1.00 53.17  ? 225 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 18.113  -0.438  -38.782 1.00 31.74  ? 226 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 10.716  -18.834 -33.177 1.00 30.07  ? 227 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 19.253  -20.003 -19.729 1.00 50.21  ? 228 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 16.939  -19.276 -29.036 1.00 27.51  ? 229 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 28.129  -17.379 -25.391 1.00 46.48  ? 230 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 14.250  -6.244  -41.334 1.00 41.70  ? 231 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 20.047  -2.500  -23.475 1.00 84.05  ? 232 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 20.992  -25.099 -29.904 1.00 55.66  ? 233 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 23.765  -4.025  -37.263 1.00 32.70  ? 234 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 22.180  -24.043 -26.821 1.00 46.62  ? 235 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 32.743  -18.700 -42.756 1.00 55.98  ? 236 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 10.222  -19.398 -43.179 1.00 55.81  ? 237 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 31.742  -12.285 -39.205 1.00 58.66  ? 238 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 22.985  -23.035 -28.985 1.00 41.91  ? 239 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 25.266  -5.668  -36.182 1.00 43.60  ? 240 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 13.435  -22.552 -20.872 1.00 48.55  ? 241 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 27.466  -10.357 -29.249 1.00 57.85  ? 242 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 26.280  -0.288  -29.601 1.00 54.28  ? 243 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 19.982  -25.519 -34.250 1.00 45.27  ? 244 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 10.748  -21.781 -32.885 1.00 37.66  ? 245 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 20.335  -10.112 -43.292 1.00 36.61  ? 246 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 14.823  -24.471 -40.596 1.00 41.09  ? 247 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 7.798   -8.080  -21.015 1.00 52.20  ? 248 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 7.746   -18.388 -31.826 1.00 52.19  ? 249 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 18.561  -25.917 -29.189 1.00 39.52  ? 250 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 17.847  -3.548  -22.186 1.00 57.14  ? 251 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 7.579   -12.485 -39.355 1.00 50.40  ? 252 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 16.972  -9.480  -44.199 1.00 46.20  ? 253 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 32.100  -21.241 -38.556 1.00 42.67  ? 254 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 23.911  -10.834 -22.176 1.00 41.47  ? 255 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 24.897  -6.407  -42.990 1.00 47.33  ? 256 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 1.946   -13.237 -28.474 1.00 52.80  ? 257 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 28.115  -24.709 -35.406 1.00 38.50  ? 258 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 20.922  -6.410  -42.930 1.00 36.71  ? 259 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 18.099  -15.856 -46.142 1.00 50.21  ? 260 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 18.466  4.711   -34.545 1.00 41.19  ? 261 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 20.541  3.955   -33.220 1.00 39.51  ? 262 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 6.630   -20.665 -25.172 1.00 39.36  ? 263 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 18.247  -28.041 -27.884 1.00 49.18  ? 264 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 9.718   -5.783  -41.221 1.00 55.55  ? 265 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 15.237  -8.035  -43.305 1.00 42.68  ? 266 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 13.425  -20.423 -19.960 1.00 60.24  ? 267 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 20.852  -19.642 -22.347 1.00 43.33  ? 268 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 16.910  -25.743 -21.148 1.00 64.60  ? 269 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 22.441  -23.572 -24.199 1.00 49.94  ? 270 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 15.148  -21.675 -42.198 1.00 50.00  ? 271 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 39.854  -13.607 -39.020 1.00 65.92  ? 272 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 11.462  -24.059 -30.103 1.00 44.40  ? 273 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 7.484   -10.017 -18.667 1.00 44.41  ? 274 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 22.864  -29.297 -35.835 1.00 43.34  ? 275 HOH B O   1 
HETATM 2379 O O   . HOH O 5 .  ? 26.961  -39.457 12.770  1.00 40.05  ? 201 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 27.114  -37.963 10.212  1.00 41.94  ? 202 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 13.374  -19.905 10.975  1.00 52.90  ? 203 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 15.096  -39.177 16.753  1.00 58.54  ? 204 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 32.017  -33.713 26.033  1.00 54.81  ? 205 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 19.502  -20.366 10.609  1.00 39.98  ? 206 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 13.226  -31.669 8.164   1.00 32.32  ? 207 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 31.492  -29.963 32.338  1.00 60.82  ? 208 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 25.882  -19.666 6.559   1.00 40.09  ? 209 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 33.519  -24.622 31.711  1.00 46.70  ? 210 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 17.621  -17.289 15.111  1.00 45.07  ? 211 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 6.266   -26.361 16.855  1.00 58.84  ? 212 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 20.332  -26.755 3.836   1.00 60.10  ? 213 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 21.969  -19.002 31.034  1.00 77.39  ? 214 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 20.341  -42.049 12.183  1.00 27.61  ? 215 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 8.204   -31.733 12.093  1.00 58.65  ? 216 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 28.055  -37.502 25.179  1.00 50.84  ? 217 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 16.574  -38.015 20.026  1.00 48.31  ? 218 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 28.453  -37.446 15.910  1.00 44.71  ? 219 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 26.069  -17.634 14.007  1.00 45.30  ? 220 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 23.441  -18.700 21.765  1.00 59.09  ? 221 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 14.783  -37.355 13.300  1.00 40.12  ? 222 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 30.737  -31.631 15.738  1.00 55.28  ? 223 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 15.515  -21.210 12.263  1.00 38.43  ? 224 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 22.537  -28.702 11.122  1.00 33.97  ? 225 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 20.969  -40.177 26.601  1.00 40.27  ? 226 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 9.629   -37.523 18.159  1.00 55.41  ? 227 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 11.856  -29.236 27.857  1.00 61.39  ? 228 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 25.792  -33.954 35.000  1.00 53.36  ? 229 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 23.292  -41.882 18.606  1.00 37.01  ? 230 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 16.280  -17.787 19.389  1.00 43.80  ? 231 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 21.320  -28.901 8.480   1.00 37.92  ? 232 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 22.439  -34.633 16.606  1.00 27.44  ? 233 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 25.596  -31.544 10.805  1.00 38.07  ? 234 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 31.417  -40.154 27.375  1.00 42.20  ? 235 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 21.113  -19.496 24.893  1.00 58.73  ? 236 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 30.502  -36.145 28.718  1.00 54.60  ? 237 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 7.244   -18.070 10.784  1.00 40.73  ? 238 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 9.574   -18.975 23.707  1.00 44.56  ? 239 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 28.645  -15.055 12.847  1.00 54.20  ? 240 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 30.014  -40.259 31.600  1.00 41.60  ? 241 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 21.456  -29.660 4.916   1.00 59.15  ? 242 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 25.897  -39.910 20.203  1.00 36.85  ? 243 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 25.846  -18.108 21.204  1.00 63.69  ? 244 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 31.907  -43.409 16.059  1.00 49.55  ? 245 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 10.030  -30.530 9.879   1.00 33.41  ? 246 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 30.817  -17.486 9.605   1.00 44.04  ? 247 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 2.886   -28.277 14.313  1.00 61.27  ? 248 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 14.107  -39.062 9.394   1.00 63.56  ? 249 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 29.080  -39.556 24.466  1.00 54.02  ? 250 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 29.084  -25.330 32.864  1.00 51.52  ? 251 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 30.571  -32.993 18.277  1.00 46.97  ? 252 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 32.372  -43.751 11.845  1.00 51.26  ? 253 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 20.360  -36.883 40.502  1.00 58.73  ? 254 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 13.568  -23.118 27.909  1.00 56.09  ? 255 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 12.135  -21.414 10.621  1.00 44.56  ? 256 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 17.397  -37.313 29.077  1.00 55.30  ? 257 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 22.889  -14.150 13.585  1.00 48.31  ? 258 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 29.405  -42.000 27.384  1.00 40.23  ? 259 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 25.161  -36.241 9.806   1.00 50.19  ? 260 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 26.136  -14.107 11.158  1.00 47.27  ? 261 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 14.875  -34.642 35.598  1.00 61.11  ? 262 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 33.088  -28.099 29.223  1.00 57.51  ? 263 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 37.360  -24.354 27.016  1.00 71.75  ? 264 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 17.601  -26.749 36.784  1.00 73.03  ? 265 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 4.712   -24.356 18.109  1.00 64.16  ? 266 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 21.670  -41.936 40.919  1.00 56.31  ? 267 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 29.268  -40.917 19.341  1.00 68.33  ? 268 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 28.639  -41.910 29.932  1.00 42.33  ? 269 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 33.829  -44.859 15.319  1.00 38.72  ? 270 HOH C O   1 
# 
