data_7HGO
# 
_entry.id   7HGO 
# 
_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   7HGO         pdb_00007hgo 10.2210/pdb7hgo/pdb 
WWPDB D_1001407450 ?            ?                   
# 
_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                        7HGO 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2'       10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                            96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                           62.068    2   ? ?    ? ? 
4 non-polymer syn 'N-methyl-3-oxo-N-(propan-2-yl)piperazine-1-sulfonamide' 235.304   1   ? ?    ? ? 
5 water       nat water                                                    18.015    272 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                            SO4 
3 1,2-ETHANEDIOL                                           EDO 
4 'N-methyl-3-oxo-N-(propan-2-yl)piperazine-1-sulfonamide' 8DH 
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 
8DH non-polymer         . 'N-methyl-3-oxo-N-(propan-2-yl)piperazine-1-sulfonamide' ?                 'C8 H17 N3 O3 S' 235.304 
ALA 'L-peptide linking' y ALANINE                                                  ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                                 ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                               ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                          ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                                 ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                           'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                          ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                                  ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                                ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                    ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                               ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                                  ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                   ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                               ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                            ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                  ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                   ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                            ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                                ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                               ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                 ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                   ?                 'C5 H11 N O2'    117.146 
# 
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        8DH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   8DH 
_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 8DH 1   103 101 8DH 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   202 333 HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 84  HOH HOH A . 
M 5 HOH 5   205 346 HOH HOH A . 
M 5 HOH 6   206 304 HOH HOH A . 
M 5 HOH 7   207 71  HOH HOH A . 
M 5 HOH 8   208 208 HOH HOH A . 
M 5 HOH 9   209 87  HOH HOH A . 
M 5 HOH 10  210 86  HOH HOH A . 
M 5 HOH 11  211 95  HOH HOH A . 
M 5 HOH 12  212 55  HOH HOH A . 
M 5 HOH 13  213 66  HOH HOH A . 
M 5 HOH 14  214 341 HOH HOH A . 
M 5 HOH 15  215 139 HOH HOH A . 
M 5 HOH 16  216 142 HOH HOH A . 
M 5 HOH 17  217 334 HOH HOH A . 
M 5 HOH 18  218 28  HOH HOH A . 
M 5 HOH 19  219 91  HOH HOH A . 
M 5 HOH 20  220 293 HOH HOH A . 
M 5 HOH 21  221 26  HOH HOH A . 
M 5 HOH 22  222 355 HOH HOH A . 
M 5 HOH 23  223 289 HOH HOH A . 
M 5 HOH 24  224 8   HOH HOH A . 
M 5 HOH 25  225 27  HOH HOH A . 
M 5 HOH 26  226 37  HOH HOH A . 
M 5 HOH 27  227 188 HOH HOH A . 
M 5 HOH 28  228 34  HOH HOH A . 
M 5 HOH 29  229 260 HOH HOH A . 
M 5 HOH 30  230 267 HOH HOH A . 
M 5 HOH 31  231 278 HOH HOH A . 
M 5 HOH 32  232 199 HOH HOH A . 
M 5 HOH 33  233 211 HOH HOH A . 
M 5 HOH 34  234 259 HOH HOH A . 
M 5 HOH 35  235 190 HOH HOH A . 
M 5 HOH 36  236 7   HOH HOH A . 
M 5 HOH 37  237 32  HOH HOH A . 
M 5 HOH 38  238 41  HOH HOH A . 
M 5 HOH 39  239 290 HOH HOH A . 
M 5 HOH 40  240 339 HOH HOH A . 
M 5 HOH 41  241 97  HOH HOH A . 
M 5 HOH 42  242 179 HOH HOH A . 
M 5 HOH 43  243 299 HOH HOH A . 
M 5 HOH 44  244 12  HOH HOH A . 
M 5 HOH 45  245 21  HOH HOH A . 
M 5 HOH 46  246 111 HOH HOH A . 
M 5 HOH 47  247 42  HOH HOH A . 
M 5 HOH 48  248 2   HOH HOH A . 
M 5 HOH 49  249 60  HOH HOH A . 
M 5 HOH 50  250 1   HOH HOH A . 
M 5 HOH 51  251 218 HOH HOH A . 
M 5 HOH 52  252 23  HOH HOH A . 
M 5 HOH 53  253 115 HOH HOH A . 
M 5 HOH 54  254 288 HOH HOH A . 
M 5 HOH 55  255 274 HOH HOH A . 
M 5 HOH 56  256 18  HOH HOH A . 
M 5 HOH 57  257 116 HOH HOH A . 
M 5 HOH 58  258 347 HOH HOH A . 
M 5 HOH 59  259 73  HOH HOH A . 
M 5 HOH 60  260 77  HOH HOH A . 
M 5 HOH 61  261 58  HOH HOH A . 
M 5 HOH 62  262 342 HOH HOH A . 
M 5 HOH 63  263 300 HOH HOH A . 
M 5 HOH 64  264 109 HOH HOH A . 
M 5 HOH 65  265 145 HOH HOH A . 
M 5 HOH 66  266 64  HOH HOH A . 
M 5 HOH 67  267 167 HOH HOH A . 
M 5 HOH 68  268 164 HOH HOH A . 
M 5 HOH 69  269 143 HOH HOH A . 
M 5 HOH 70  270 20  HOH HOH A . 
M 5 HOH 71  271 47  HOH HOH A . 
M 5 HOH 72  272 93  HOH HOH A . 
M 5 HOH 73  273 94  HOH HOH A . 
M 5 HOH 74  274 99  HOH HOH A . 
M 5 HOH 75  275 78  HOH HOH A . 
M 5 HOH 76  276 222 HOH HOH A . 
M 5 HOH 77  277 35  HOH HOH A . 
M 5 HOH 78  278 336 HOH HOH A . 
M 5 HOH 79  279 203 HOH HOH A . 
M 5 HOH 80  280 14  HOH HOH A . 
M 5 HOH 81  281 292 HOH HOH A . 
M 5 HOH 82  282 357 HOH HOH A . 
M 5 HOH 83  283 16  HOH HOH A . 
M 5 HOH 84  284 9   HOH HOH A . 
M 5 HOH 85  285 131 HOH HOH A . 
M 5 HOH 86  286 38  HOH HOH A . 
M 5 HOH 87  287 31  HOH HOH A . 
M 5 HOH 88  288 281 HOH HOH A . 
M 5 HOH 89  289 19  HOH HOH A . 
M 5 HOH 90  290 165 HOH HOH A . 
M 5 HOH 91  291 113 HOH HOH A . 
M 5 HOH 92  292 301 HOH HOH A . 
M 5 HOH 93  293 152 HOH HOH A . 
M 5 HOH 94  294 327 HOH HOH A . 
M 5 HOH 95  295 318 HOH HOH A . 
M 5 HOH 96  296 63  HOH HOH A . 
M 5 HOH 97  297 22  HOH HOH A . 
M 5 HOH 98  298 146 HOH HOH A . 
M 5 HOH 99  299 108 HOH HOH A . 
M 5 HOH 100 300 210 HOH HOH A . 
M 5 HOH 101 301 270 HOH HOH A . 
M 5 HOH 102 302 296 HOH HOH A . 
M 5 HOH 103 303 356 HOH HOH A . 
M 5 HOH 104 304 185 HOH HOH A . 
M 5 HOH 105 305 358 HOH HOH A . 
M 5 HOH 106 306 83  HOH HOH A . 
M 5 HOH 107 307 219 HOH HOH A . 
M 5 HOH 108 308 205 HOH HOH A . 
M 5 HOH 109 309 57  HOH HOH A . 
M 5 HOH 110 310 343 HOH HOH A . 
M 5 HOH 111 311 332 HOH HOH A . 
M 5 HOH 112 312 283 HOH HOH A . 
M 5 HOH 113 313 313 HOH HOH A . 
M 5 HOH 114 314 156 HOH HOH A . 
M 5 HOH 115 315 75  HOH HOH A . 
M 5 HOH 116 316 125 HOH HOH A . 
M 5 HOH 117 317 365 HOH HOH A . 
M 5 HOH 118 318 359 HOH HOH A . 
N 5 HOH 1   201 329 HOH HOH B . 
N 5 HOH 2   202 331 HOH HOH B . 
N 5 HOH 3   203 272 HOH HOH B . 
N 5 HOH 4   204 363 HOH HOH B . 
N 5 HOH 5   205 172 HOH HOH B . 
N 5 HOH 6   206 247 HOH HOH B . 
N 5 HOH 7   207 123 HOH HOH B . 
N 5 HOH 8   208 98  HOH HOH B . 
N 5 HOH 9   209 258 HOH HOH B . 
N 5 HOH 10  210 68  HOH HOH B . 
N 5 HOH 11  211 72  HOH HOH B . 
N 5 HOH 12  212 17  HOH HOH B . 
N 5 HOH 13  213 360 HOH HOH B . 
N 5 HOH 14  214 224 HOH HOH B . 
N 5 HOH 15  215 242 HOH HOH B . 
N 5 HOH 16  216 184 HOH HOH B . 
N 5 HOH 17  217 366 HOH HOH B . 
N 5 HOH 18  218 69  HOH HOH B . 
N 5 HOH 19  219 249 HOH HOH B . 
N 5 HOH 20  220 137 HOH HOH B . 
N 5 HOH 21  221 361 HOH HOH B . 
N 5 HOH 22  222 150 HOH HOH B . 
N 5 HOH 23  223 89  HOH HOH B . 
N 5 HOH 24  224 6   HOH HOH B . 
N 5 HOH 25  225 280 HOH HOH B . 
N 5 HOH 26  226 10  HOH HOH B . 
N 5 HOH 27  227 320 HOH HOH B . 
N 5 HOH 28  228 54  HOH HOH B . 
N 5 HOH 29  229 117 HOH HOH B . 
N 5 HOH 30  230 177 HOH HOH B . 
N 5 HOH 31  231 153 HOH HOH B . 
N 5 HOH 32  232 261 HOH HOH B . 
N 5 HOH 33  233 119 HOH HOH B . 
N 5 HOH 34  234 315 HOH HOH B . 
N 5 HOH 35  235 59  HOH HOH B . 
N 5 HOH 36  236 372 HOH HOH B . 
N 5 HOH 37  237 13  HOH HOH B . 
N 5 HOH 38  238 5   HOH HOH B . 
N 5 HOH 39  239 168 HOH HOH B . 
N 5 HOH 40  240 25  HOH HOH B . 
N 5 HOH 41  241 215 HOH HOH B . 
N 5 HOH 42  242 120 HOH HOH B . 
N 5 HOH 43  243 24  HOH HOH B . 
N 5 HOH 44  244 223 HOH HOH B . 
N 5 HOH 45  245 169 HOH HOH B . 
N 5 HOH 46  246 217 HOH HOH B . 
N 5 HOH 47  247 61  HOH HOH B . 
N 5 HOH 48  248 157 HOH HOH B . 
N 5 HOH 49  249 170 HOH HOH B . 
N 5 HOH 50  250 76  HOH HOH B . 
N 5 HOH 51  251 74  HOH HOH B . 
N 5 HOH 52  252 96  HOH HOH B . 
N 5 HOH 53  253 36  HOH HOH B . 
N 5 HOH 54  254 214 HOH HOH B . 
N 5 HOH 55  255 101 HOH HOH B . 
N 5 HOH 56  256 104 HOH HOH B . 
N 5 HOH 57  257 79  HOH HOH B . 
N 5 HOH 58  258 46  HOH HOH B . 
N 5 HOH 59  259 175 HOH HOH B . 
N 5 HOH 60  260 197 HOH HOH B . 
N 5 HOH 61  261 44  HOH HOH B . 
N 5 HOH 62  262 354 HOH HOH B . 
N 5 HOH 63  263 322 HOH HOH B . 
N 5 HOH 64  264 303 HOH HOH B . 
N 5 HOH 65  265 371 HOH HOH B . 
N 5 HOH 66  266 182 HOH HOH B . 
N 5 HOH 67  267 279 HOH HOH B . 
N 5 HOH 68  268 367 HOH HOH B . 
N 5 HOH 69  269 316 HOH HOH B . 
N 5 HOH 70  270 291 HOH HOH B . 
N 5 HOH 71  271 368 HOH HOH B . 
N 5 HOH 72  272 160 HOH HOH B . 
N 5 HOH 73  273 163 HOH HOH B . 
N 5 HOH 74  274 348 HOH HOH B . 
N 5 HOH 75  275 201 HOH HOH B . 
N 5 HOH 76  276 103 HOH HOH B . 
N 5 HOH 77  277 335 HOH HOH B . 
N 5 HOH 78  278 314 HOH HOH B . 
N 5 HOH 79  279 107 HOH HOH B . 
N 5 HOH 80  280 312 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 254 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 353 HOH HOH C . 
O 5 HOH 5   205 349 HOH HOH C . 
O 5 HOH 6   206 351 HOH HOH C . 
O 5 HOH 7   207 226 HOH HOH C . 
O 5 HOH 8   208 302 HOH HOH C . 
O 5 HOH 9   209 338 HOH HOH C . 
O 5 HOH 10  210 317 HOH HOH C . 
O 5 HOH 11  211 309 HOH HOH C . 
O 5 HOH 12  212 161 HOH HOH C . 
O 5 HOH 13  213 118 HOH HOH C . 
O 5 HOH 14  214 271 HOH HOH C . 
O 5 HOH 15  215 85  HOH HOH C . 
O 5 HOH 16  216 325 HOH HOH C . 
O 5 HOH 17  217 326 HOH HOH C . 
O 5 HOH 18  218 90  HOH HOH C . 
O 5 HOH 19  219 134 HOH HOH C . 
O 5 HOH 20  220 132 HOH HOH C . 
O 5 HOH 21  221 340 HOH HOH C . 
O 5 HOH 22  222 82  HOH HOH C . 
O 5 HOH 23  223 126 HOH HOH C . 
O 5 HOH 24  224 15  HOH HOH C . 
O 5 HOH 25  225 189 HOH HOH C . 
O 5 HOH 26  226 284 HOH HOH C . 
O 5 HOH 27  227 173 HOH HOH C . 
O 5 HOH 28  228 53  HOH HOH C . 
O 5 HOH 29  229 102 HOH HOH C . 
O 5 HOH 30  230 48  HOH HOH C . 
O 5 HOH 31  231 295 HOH HOH C . 
O 5 HOH 32  232 148 HOH HOH C . 
O 5 HOH 33  233 337 HOH HOH C . 
O 5 HOH 34  234 4   HOH HOH C . 
O 5 HOH 35  235 45  HOH HOH C . 
O 5 HOH 36  236 350 HOH HOH C . 
O 5 HOH 37  237 269 HOH HOH C . 
O 5 HOH 38  238 298 HOH HOH C . 
O 5 HOH 39  239 122 HOH HOH C . 
O 5 HOH 40  240 370 HOH HOH C . 
O 5 HOH 41  241 330 HOH HOH C . 
O 5 HOH 42  242 294 HOH HOH C . 
O 5 HOH 43  243 49  HOH HOH C . 
O 5 HOH 44  244 56  HOH HOH C . 
O 5 HOH 45  245 43  HOH HOH C . 
O 5 HOH 46  246 151 HOH HOH C . 
O 5 HOH 47  247 40  HOH HOH C . 
O 5 HOH 48  248 275 HOH HOH C . 
O 5 HOH 49  249 130 HOH HOH C . 
O 5 HOH 50  250 135 HOH HOH C . 
O 5 HOH 51  251 369 HOH HOH C . 
O 5 HOH 52  252 62  HOH HOH C . 
O 5 HOH 53  253 328 HOH HOH C . 
O 5 HOH 54  254 198 HOH HOH C . 
O 5 HOH 55  255 287 HOH HOH C . 
O 5 HOH 56  256 149 HOH HOH C . 
O 5 HOH 57  257 65  HOH HOH C . 
O 5 HOH 58  258 67  HOH HOH C . 
O 5 HOH 59  259 344 HOH HOH C . 
O 5 HOH 60  260 171 HOH HOH C . 
O 5 HOH 61  261 305 HOH HOH C . 
O 5 HOH 62  262 246 HOH HOH C . 
O 5 HOH 63  263 241 HOH HOH C . 
O 5 HOH 64  264 209 HOH HOH C . 
O 5 HOH 65  265 70  HOH HOH C . 
O 5 HOH 66  266 345 HOH HOH C . 
O 5 HOH 67  267 352 HOH HOH C . 
O 5 HOH 68  268 319 HOH HOH C . 
O 5 HOH 69  269 324 HOH HOH C . 
O 5 HOH 70  270 362 HOH HOH C . 
O 5 HOH 71  271 92  HOH HOH C . 
O 5 HOH 72  272 206 HOH HOH C . 
O 5 HOH 73  273 310 HOH HOH C . 
O 5 HOH 74  274 364 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 65 ? CD  ? B LYS 66 CD  
19 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
20 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
21 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
22 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
23 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
24 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
25 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
26 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
27 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
28 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
29 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
30 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
31 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
32 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
33 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
34 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
35 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
36 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
37 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
38 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
39 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
40 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
41 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
42 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
43 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
44 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
45 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
46 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
47 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
48 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
49 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
50 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
51 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
52 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
53 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
54 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGO 
_cell.length_a           41.620 
_cell.length_b           42.200 
_cell.length_c           159.100 
_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                         7HGO 
_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          7HGO 
_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                     7HGO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.03 
_reflns.d_resolution_high            1.44 
_reflns.number_obs                   51879 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_netI_over_sigmaI        16.3 
_reflns.pdbx_redundancy              5.9 
_reflns.pdbx_Rrim_I_all              0.044 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     305178 
_reflns.pdbx_chi_squared             0.93 
_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                  1.44 
_reflns_shell.d_res_low                   1.48 
_reflns_shell.number_measured_all         15965 
_reflns_shell.number_unique_obs           3769 
_reflns_shell.Rmerge_I_obs                1.429 
_reflns_shell.pdbx_chi_squared            0.77 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.634 
_reflns_shell.pdbx_Rpim_I_all             0.780 
_reflns_shell.pdbx_CC_half                0.385 
_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                                 7HGO 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     49053 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.82 
_refine.ls_d_res_high                            1.44 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_R_factor_obs                          0.20825 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20667 
_refine.ls_R_factor_R_free                       0.23641 
_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                  2745 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.B_iso_mean                               35.793 
_refine.aniso_B[1][1]                            0.47 
_refine.aniso_B[2][2]                            -0.41 
_refine.aniso_B[3][3]                            -0.06 
_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                       0.076 
_refine.pdbx_overall_ESU_R_Free                  0.078 
_refine.overall_SU_ML                            0.066 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.798 
_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        2134 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             272 
_refine_hist.number_atoms_total               2459 
_refine_hist.d_res_high                       1.44 
_refine_hist.d_res_low                        40.82 
# 
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             0.011  0.012  ? 2290 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.023  1.835  ? 3118 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.916  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.364  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.187 10.000 ? 299  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.133  0.200  ? 288  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.012  0.020  ? 1884 '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                  3.230  3.289  ? 1069 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.336  5.888  ? 1333 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.502  3.625  ? 1221 '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       8.615  46.80  ? 3559 '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                       1.440 
_refine_ls_shell.d_res_low                        1.477 
_refine_ls_shell.number_reflns_R_work             3566 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               99.89 
_refine_ls_shell.R_factor_R_free                  0.363 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             195 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGO 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z431807512' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGO 
_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 7HGO A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGO B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGO 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 7HGO GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGO SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGO GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGO SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGO GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGO 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                   7HGO 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 243 ? ? O C HOH 209 ? ? 1.42 
2  1 O   B HOH 225 ? ? O B HOH 263 ? ? 1.70 
3  1 CE  A LYS 39  ? ? O A HOH 278 ? ? 1.81 
4  1 O   A HOH 301 ? ? O C HOH 206 ? ? 1.85 
5  1 O   B HOH 230 ? ? O B HOH 274 ? ? 1.95 
6  1 O   A HOH 262 ? ? O A HOH 275 ? ? 1.98 
7  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.01 
8  1 O   C HOH 242 ? ? O C HOH 268 ? ? 2.01 
9  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 2.04 
10 1 O2  C SO4 102 ? ? O C HOH 202 ? ? 2.07 
11 1 O   A HOH 258 ? ? O A HOH 272 ? ? 2.07 
12 1 OE1 A GLN 85  ? ? O A HOH 202 ? ? 2.10 
13 1 O4  A SO4 104 ? ? O A HOH 203 ? ? 2.16 
14 1 OD1 C ASP 9   ? ? O C HOH 203 ? ? 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 276 ? ? 1_555 O A HOH 281 ? ? 4_445 2.11 
2 1 O A HOH 270 ? ? 1_555 O A HOH 312 ? ? 4_545 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 24 ? ? CZ A ARG 24 ? ? NH2 A ARG 24 ? ? 116.65 120.30 -3.65 0.50 N 
2 1 NE C ARG 74 ? ? CZ C ARG 74 ? ? NH2 C ARG 74 ? ? 117.06 120.30 -3.24 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -157.37 66.20 
2 1 ASN B 38 ? ? 76.62   -2.32 
3 1 ASN B 87 ? ? -160.03 63.85 
4 1 ASN C 87 ? ? -140.46 53.58 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            147.74 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       274 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.30 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
8DH C10  C N N 1   
8DH N12  N N N 2   
8DH C13  C N N 3   
8DH C15  C N N 4   
8DH C01  C N N 5   
8DH C02  C N N 6   
8DH C03  C N N 7   
8DH N04  N N N 8   
8DH C05  C N N 9   
8DH S06  S N N 10  
8DH O07  O N N 11  
8DH O08  O N N 12  
8DH N09  N N N 13  
8DH C11  C N N 14  
8DH O14  O N N 15  
8DH H1   H N N 16  
8DH H2   H N N 17  
8DH H3   H N N 18  
8DH H4   H N N 19  
8DH H5   H N N 20  
8DH H6   H N N 21  
8DH H7   H N N 22  
8DH H8   H N N 23  
8DH H9   H N N 24  
8DH H10  H N N 25  
8DH H11  H N N 26  
8DH H12  H N N 27  
8DH H13  H N N 28  
8DH H14  H N N 29  
8DH H15  H N N 30  
8DH H16  H N N 31  
8DH H17  H N N 32  
ALA N    N N N 33  
ALA CA   C N S 34  
ALA C    C N N 35  
ALA O    O N N 36  
ALA CB   C N N 37  
ALA OXT  O N N 38  
ALA H    H N N 39  
ALA H2   H N N 40  
ALA HA   H N N 41  
ALA HB1  H N N 42  
ALA HB2  H N N 43  
ALA HB3  H N N 44  
ALA HXT  H N N 45  
ARG N    N N N 46  
ARG CA   C N S 47  
ARG C    C N N 48  
ARG O    O N N 49  
ARG CB   C N N 50  
ARG CG   C N N 51  
ARG CD   C N N 52  
ARG NE   N N N 53  
ARG CZ   C N N 54  
ARG NH1  N N N 55  
ARG NH2  N N N 56  
ARG OXT  O N N 57  
ARG H    H N N 58  
ARG H2   H N N 59  
ARG HA   H N N 60  
ARG HB2  H N N 61  
ARG HB3  H N N 62  
ARG HG2  H N N 63  
ARG HG3  H N N 64  
ARG HD2  H N N 65  
ARG HD3  H N N 66  
ARG HE   H N N 67  
ARG HH11 H N N 68  
ARG HH12 H N N 69  
ARG HH21 H N N 70  
ARG HH22 H N N 71  
ARG HXT  H N N 72  
ASN N    N N N 73  
ASN CA   C N S 74  
ASN C    C N N 75  
ASN O    O N N 76  
ASN CB   C N N 77  
ASN CG   C N N 78  
ASN OD1  O N N 79  
ASN ND2  N N N 80  
ASN OXT  O N N 81  
ASN H    H N N 82  
ASN H2   H N N 83  
ASN HA   H N N 84  
ASN HB2  H N N 85  
ASN HB3  H N N 86  
ASN HD21 H N N 87  
ASN HD22 H N N 88  
ASN HXT  H N N 89  
ASP N    N N N 90  
ASP CA   C N S 91  
ASP C    C N N 92  
ASP O    O N N 93  
ASP CB   C N N 94  
ASP CG   C N N 95  
ASP OD1  O N N 96  
ASP OD2  O N N 97  
ASP OXT  O N N 98  
ASP H    H N N 99  
ASP H2   H N N 100 
ASP HA   H N N 101 
ASP HB2  H N N 102 
ASP HB3  H N N 103 
ASP HD2  H N N 104 
ASP HXT  H N N 105 
CYS N    N N N 106 
CYS CA   C N R 107 
CYS C    C N N 108 
CYS O    O N N 109 
CYS CB   C N N 110 
CYS SG   S N N 111 
CYS OXT  O N N 112 
CYS H    H N N 113 
CYS H2   H N N 114 
CYS HA   H N N 115 
CYS HB2  H N N 116 
CYS HB3  H N N 117 
CYS HG   H N N 118 
CYS HXT  H N N 119 
EDO C1   C N N 120 
EDO O1   O N N 121 
EDO C2   C N N 122 
EDO O2   O N N 123 
EDO H11  H N N 124 
EDO H12  H N N 125 
EDO HO1  H N N 126 
EDO H21  H N N 127 
EDO H22  H N N 128 
EDO HO2  H N N 129 
GLN N    N N N 130 
GLN CA   C N S 131 
GLN C    C N N 132 
GLN O    O N N 133 
GLN CB   C N N 134 
GLN CG   C N N 135 
GLN CD   C N N 136 
GLN OE1  O N N 137 
GLN NE2  N N N 138 
GLN OXT  O N N 139 
GLN H    H N N 140 
GLN H2   H N N 141 
GLN HA   H N N 142 
GLN HB2  H N N 143 
GLN HB3  H N N 144 
GLN HG2  H N N 145 
GLN HG3  H N N 146 
GLN HE21 H N N 147 
GLN HE22 H N N 148 
GLN HXT  H N N 149 
GLU N    N N N 150 
GLU CA   C N S 151 
GLU C    C N N 152 
GLU O    O N N 153 
GLU CB   C N N 154 
GLU CG   C N N 155 
GLU CD   C N N 156 
GLU OE1  O N N 157 
GLU OE2  O N N 158 
GLU OXT  O N N 159 
GLU H    H N N 160 
GLU H2   H N N 161 
GLU HA   H N N 162 
GLU HB2  H N N 163 
GLU HB3  H N N 164 
GLU HG2  H N N 165 
GLU HG3  H N N 166 
GLU HE2  H N N 167 
GLU HXT  H N N 168 
GLY N    N N N 169 
GLY CA   C N N 170 
GLY C    C N N 171 
GLY O    O N N 172 
GLY OXT  O N N 173 
GLY H    H N N 174 
GLY H2   H N N 175 
GLY HA2  H N N 176 
GLY HA3  H N N 177 
GLY HXT  H N N 178 
HIS N    N N N 179 
HIS CA   C N S 180 
HIS C    C N N 181 
HIS O    O N N 182 
HIS CB   C N N 183 
HIS CG   C Y N 184 
HIS ND1  N Y N 185 
HIS CD2  C Y N 186 
HIS CE1  C Y N 187 
HIS NE2  N Y N 188 
HIS OXT  O N N 189 
HIS H    H N N 190 
HIS H2   H N N 191 
HIS HA   H N N 192 
HIS HB2  H N N 193 
HIS HB3  H N N 194 
HIS HD1  H N N 195 
HIS HD2  H N N 196 
HIS HE1  H N N 197 
HIS HE2  H N N 198 
HIS HXT  H N N 199 
HOH O    O N N 200 
HOH H1   H N N 201 
HOH H2   H N N 202 
ILE N    N N N 203 
ILE CA   C N S 204 
ILE C    C N N 205 
ILE O    O N N 206 
ILE CB   C N S 207 
ILE CG1  C N N 208 
ILE CG2  C N N 209 
ILE CD1  C N N 210 
ILE OXT  O N N 211 
ILE H    H N N 212 
ILE H2   H N N 213 
ILE HA   H N N 214 
ILE HB   H N N 215 
ILE HG12 H N N 216 
ILE HG13 H N N 217 
ILE HG21 H N N 218 
ILE HG22 H N N 219 
ILE HG23 H N N 220 
ILE HD11 H N N 221 
ILE HD12 H N N 222 
ILE HD13 H N N 223 
ILE HXT  H N N 224 
LEU N    N N N 225 
LEU CA   C N S 226 
LEU C    C N N 227 
LEU O    O N N 228 
LEU CB   C N N 229 
LEU CG   C N N 230 
LEU CD1  C N N 231 
LEU CD2  C N N 232 
LEU OXT  O N N 233 
LEU H    H N N 234 
LEU H2   H N N 235 
LEU HA   H N N 236 
LEU HB2  H N N 237 
LEU HB3  H N N 238 
LEU HG   H N N 239 
LEU HD11 H N N 240 
LEU HD12 H N N 241 
LEU HD13 H N N 242 
LEU HD21 H N N 243 
LEU HD22 H N N 244 
LEU HD23 H N N 245 
LEU HXT  H N N 246 
LYS N    N N N 247 
LYS CA   C N S 248 
LYS C    C N N 249 
LYS O    O N N 250 
LYS CB   C N N 251 
LYS CG   C N N 252 
LYS CD   C N N 253 
LYS CE   C N N 254 
LYS NZ   N N N 255 
LYS OXT  O N N 256 
LYS H    H N N 257 
LYS H2   H N N 258 
LYS HA   H N N 259 
LYS HB2  H N N 260 
LYS HB3  H N N 261 
LYS HG2  H N N 262 
LYS HG3  H N N 263 
LYS HD2  H N N 264 
LYS HD3  H N N 265 
LYS HE2  H N N 266 
LYS HE3  H N N 267 
LYS HZ1  H N N 268 
LYS HZ2  H N N 269 
LYS HZ3  H N N 270 
LYS HXT  H N N 271 
MET N    N N N 272 
MET CA   C N S 273 
MET C    C N N 274 
MET O    O N N 275 
MET CB   C N N 276 
MET CG   C N N 277 
MET SD   S N N 278 
MET CE   C N N 279 
MET OXT  O N N 280 
MET H    H N N 281 
MET H2   H N N 282 
MET HA   H N N 283 
MET HB2  H N N 284 
MET HB3  H N N 285 
MET HG2  H N N 286 
MET HG3  H N N 287 
MET HE1  H N N 288 
MET HE2  H N N 289 
MET HE3  H N N 290 
MET HXT  H N N 291 
PHE N    N N N 292 
PHE CA   C N S 293 
PHE C    C N N 294 
PHE O    O N N 295 
PHE CB   C N N 296 
PHE CG   C Y N 297 
PHE CD1  C Y N 298 
PHE CD2  C Y N 299 
PHE CE1  C Y N 300 
PHE CE2  C Y N 301 
PHE CZ   C Y N 302 
PHE OXT  O N N 303 
PHE H    H N N 304 
PHE H2   H N N 305 
PHE HA   H N N 306 
PHE HB2  H N N 307 
PHE HB3  H N N 308 
PHE HD1  H N N 309 
PHE HD2  H N N 310 
PHE HE1  H N N 311 
PHE HE2  H N N 312 
PHE HZ   H N N 313 
PHE HXT  H N N 314 
PRO N    N N N 315 
PRO CA   C N S 316 
PRO C    C N N 317 
PRO O    O N N 318 
PRO CB   C N N 319 
PRO CG   C N N 320 
PRO CD   C N N 321 
PRO OXT  O N N 322 
PRO H    H N N 323 
PRO HA   H N N 324 
PRO HB2  H N N 325 
PRO HB3  H N N 326 
PRO HG2  H N N 327 
PRO HG3  H N N 328 
PRO HD2  H N N 329 
PRO HD3  H N N 330 
PRO HXT  H N N 331 
SER N    N N N 332 
SER CA   C N S 333 
SER C    C N N 334 
SER O    O N N 335 
SER CB   C N N 336 
SER OG   O N N 337 
SER OXT  O N N 338 
SER H    H N N 339 
SER H2   H N N 340 
SER HA   H N N 341 
SER HB2  H N N 342 
SER HB3  H N N 343 
SER HG   H N N 344 
SER HXT  H N N 345 
SO4 S    S N N 346 
SO4 O1   O N N 347 
SO4 O2   O N N 348 
SO4 O3   O N N 349 
SO4 O4   O N N 350 
THR N    N N N 351 
THR CA   C N S 352 
THR C    C N N 353 
THR O    O N N 354 
THR CB   C N R 355 
THR OG1  O N N 356 
THR CG2  C N N 357 
THR OXT  O N N 358 
THR H    H N N 359 
THR H2   H N N 360 
THR HA   H N N 361 
THR HB   H N N 362 
THR HG1  H N N 363 
THR HG21 H N N 364 
THR HG22 H N N 365 
THR HG23 H N N 366 
THR HXT  H N N 367 
TRP N    N N N 368 
TRP CA   C N S 369 
TRP C    C N N 370 
TRP O    O N N 371 
TRP CB   C N N 372 
TRP CG   C Y N 373 
TRP CD1  C Y N 374 
TRP CD2  C Y N 375 
TRP NE1  N Y N 376 
TRP CE2  C Y N 377 
TRP CE3  C Y N 378 
TRP CZ2  C Y N 379 
TRP CZ3  C Y N 380 
TRP CH2  C Y N 381 
TRP OXT  O N N 382 
TRP H    H N N 383 
TRP H2   H N N 384 
TRP HA   H N N 385 
TRP HB2  H N N 386 
TRP HB3  H N N 387 
TRP HD1  H N N 388 
TRP HE1  H N N 389 
TRP HE3  H N N 390 
TRP HZ2  H N N 391 
TRP HZ3  H N N 392 
TRP HH2  H N N 393 
TRP HXT  H N N 394 
TYR N    N N N 395 
TYR CA   C N S 396 
TYR C    C N N 397 
TYR O    O N N 398 
TYR CB   C N N 399 
TYR CG   C Y N 400 
TYR CD1  C Y N 401 
TYR CD2  C Y N 402 
TYR CE1  C Y N 403 
TYR CE2  C Y N 404 
TYR CZ   C Y N 405 
TYR OH   O N N 406 
TYR OXT  O N N 407 
TYR H    H N N 408 
TYR H2   H N N 409 
TYR HA   H N N 410 
TYR HB2  H N N 411 
TYR HB3  H N N 412 
TYR HD1  H N N 413 
TYR HD2  H N N 414 
TYR HE1  H N N 415 
TYR HE2  H N N 416 
TYR HH   H N N 417 
TYR HXT  H N N 418 
VAL N    N N N 419 
VAL CA   C N S 420 
VAL C    C N N 421 
VAL O    O N N 422 
VAL CB   C N N 423 
VAL CG1  C N N 424 
VAL CG2  C N N 425 
VAL OXT  O N N 426 
VAL H    H N N 427 
VAL H2   H N N 428 
VAL HA   H N N 429 
VAL HB   H N N 430 
VAL HG11 H N N 431 
VAL HG12 H N N 432 
VAL HG13 H N N 433 
VAL HG21 H N N 434 
VAL HG22 H N N 435 
VAL HG23 H N N 436 
VAL HXT  H N N 437 
# 
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 
8DH C11 C10  sing N N 1   
8DH C11 N12  sing N N 2   
8DH C10 N09  sing N N 3   
8DH N12 C13  sing N N 4   
8DH C05 N04  sing N N 5   
8DH C13 O14  doub N N 6   
8DH C13 C15  sing N N 7   
8DH N09 C15  sing N N 8   
8DH N09 S06  sing N N 9   
8DH O07 S06  doub N N 10  
8DH S06 N04  sing N N 11  
8DH S06 O08  doub N N 12  
8DH N04 C02  sing N N 13  
8DH C01 C02  sing N N 14  
8DH C02 C03  sing N N 15  
8DH C10 H1   sing N N 16  
8DH C10 H2   sing N N 17  
8DH N12 H3   sing N N 18  
8DH C15 H4   sing N N 19  
8DH C15 H5   sing N N 20  
8DH C01 H6   sing N N 21  
8DH C01 H7   sing N N 22  
8DH C01 H8   sing N N 23  
8DH C02 H9   sing N N 24  
8DH C03 H10  sing N N 25  
8DH C03 H11  sing N N 26  
8DH C03 H12  sing N N 27  
8DH C05 H13  sing N N 28  
8DH C05 H14  sing N N 29  
8DH C05 H15  sing N N 30  
8DH C11 H16  sing N N 31  
8DH C11 H17  sing N N 32  
ALA N   CA   sing N N 33  
ALA N   H    sing N N 34  
ALA N   H2   sing N N 35  
ALA CA  C    sing N N 36  
ALA CA  CB   sing N N 37  
ALA CA  HA   sing N N 38  
ALA C   O    doub N N 39  
ALA C   OXT  sing N N 40  
ALA CB  HB1  sing N N 41  
ALA CB  HB2  sing N N 42  
ALA CB  HB3  sing N N 43  
ALA OXT HXT  sing N N 44  
ARG N   CA   sing N N 45  
ARG N   H    sing N N 46  
ARG N   H2   sing N N 47  
ARG CA  C    sing N N 48  
ARG CA  CB   sing N N 49  
ARG CA  HA   sing N N 50  
ARG C   O    doub N N 51  
ARG C   OXT  sing N N 52  
ARG CB  CG   sing N N 53  
ARG CB  HB2  sing N N 54  
ARG CB  HB3  sing N N 55  
ARG CG  CD   sing N N 56  
ARG CG  HG2  sing N N 57  
ARG CG  HG3  sing N N 58  
ARG CD  NE   sing N N 59  
ARG CD  HD2  sing N N 60  
ARG CD  HD3  sing N N 61  
ARG NE  CZ   sing N N 62  
ARG NE  HE   sing N N 63  
ARG CZ  NH1  sing N N 64  
ARG CZ  NH2  doub N N 65  
ARG NH1 HH11 sing N N 66  
ARG NH1 HH12 sing N N 67  
ARG NH2 HH21 sing N N 68  
ARG NH2 HH22 sing N N 69  
ARG OXT HXT  sing N N 70  
ASN N   CA   sing N N 71  
ASN N   H    sing N N 72  
ASN N   H2   sing N N 73  
ASN CA  C    sing N N 74  
ASN CA  CB   sing N N 75  
ASN CA  HA   sing N N 76  
ASN C   O    doub N N 77  
ASN C   OXT  sing N N 78  
ASN CB  CG   sing N N 79  
ASN CB  HB2  sing N N 80  
ASN CB  HB3  sing N N 81  
ASN CG  OD1  doub N N 82  
ASN CG  ND2  sing N N 83  
ASN ND2 HD21 sing N N 84  
ASN ND2 HD22 sing N N 85  
ASN OXT HXT  sing N N 86  
ASP N   CA   sing N N 87  
ASP N   H    sing N N 88  
ASP N   H2   sing N N 89  
ASP CA  C    sing N N 90  
ASP CA  CB   sing N N 91  
ASP CA  HA   sing N N 92  
ASP C   O    doub N N 93  
ASP C   OXT  sing N N 94  
ASP CB  CG   sing N N 95  
ASP CB  HB2  sing N N 96  
ASP CB  HB3  sing N N 97  
ASP CG  OD1  doub N N 98  
ASP CG  OD2  sing N N 99  
ASP OD2 HD2  sing N N 100 
ASP OXT HXT  sing N N 101 
CYS N   CA   sing N N 102 
CYS N   H    sing N N 103 
CYS N   H2   sing N N 104 
CYS CA  C    sing N N 105 
CYS CA  CB   sing N N 106 
CYS CA  HA   sing N N 107 
CYS C   O    doub N N 108 
CYS C   OXT  sing N N 109 
CYS CB  SG   sing N N 110 
CYS CB  HB2  sing N N 111 
CYS CB  HB3  sing N N 112 
CYS SG  HG   sing N N 113 
CYS OXT HXT  sing N N 114 
EDO C1  O1   sing N N 115 
EDO C1  C2   sing N N 116 
EDO C1  H11  sing N N 117 
EDO C1  H12  sing N N 118 
EDO O1  HO1  sing N N 119 
EDO C2  O2   sing N N 120 
EDO C2  H21  sing N N 121 
EDO C2  H22  sing N N 122 
EDO O2  HO2  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
SO4 S   O1   doub N N 331 
SO4 S   O2   doub N N 332 
SO4 S   O3   sing N N 333 
SO4 S   O4   sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
# 
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                    7HGO 
_atom_sites.fract_transf_matrix[1][1]   0.024027 
_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]   0.023697 
_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]   0.006285 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 0.843   4.292   2.374   1.00 45.79  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.225  3.521   1.679   1.00 49.54  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.386   2.454   0.770   1.00 46.09  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.516   2.603   0.308   1.00 41.40  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.210  4.420   0.918   1.00 55.57  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.205  5.145   1.818   1.00 57.87  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.453  4.248   2.787   1.00 58.94  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.852  5.518   4.000   1.00 60.02  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.310  1.304   0.593   1.00 38.72  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.132   0.199   -0.268  1.00 39.20  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.347   0.567   -1.731  1.00 38.83  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.387  1.366   -2.326  1.00 37.98  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.087  -0.790  -0.115  1.00 40.18  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.533  -0.552  1.318   1.00 44.66  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.534  0.958   1.339   1.00 38.44  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.329   -0.102  -2.330  1.00 35.50  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.528   0.016   -3.751  1.00 36.26  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.962   -1.267  -4.352  1.00 30.49  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.515   -2.173  -3.626  1.00 30.70  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.032   0.131   -4.050  1.00 41.11  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.652   1.445   -3.643  1.00 51.95  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.832   1.815   -2.326  1.00 55.47  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.131   2.469   -4.372  1.00 57.39  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.377   3.025   -2.269  1.00 59.12  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.575   3.439   -3.495  1.00 53.70  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.999   -1.372  -5.667  1.00 28.09  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.792   -2.665  -6.285  1.00 27.49  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.939   -3.622  -5.933  1.00 25.63  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.055   -3.223  -5.514  1.00 27.58  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.664   -2.498  -7.794  1.00 32.09  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.624   -4.900  -6.042  1.00 24.70  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.613   -5.962  -5.884  1.00 22.64  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.737   -5.775  -6.906  1.00 25.73  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.516   -5.306  -8.035  1.00 28.46  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.101   -7.398  -5.962  1.00 24.79  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.315   -7.746  -4.711  1.00 26.40  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.966   -7.924  -3.491  1.00 22.87  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.077  -7.902  -4.786  1.00 24.48  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.269   -8.294  -2.331  1.00 22.27  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.758  -8.280  -3.623  1.00 23.45  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.118  -8.444  -2.417  1.00 23.73  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.971   -6.036  -6.417  1.00 22.38  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.132   -5.980  -7.304  1.00 23.94  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.050   -7.170  -7.011  1.00 22.82  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.997   -7.762  -5.937  1.00 23.22  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.882   -4.660  -7.054  1.00 26.76  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.512   -4.568  -5.693  1.00 30.14  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.123   -3.200  -5.328  1.00 35.82  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.747   -3.238  -3.942  1.00 34.82  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.748   -3.196  -2.867  1.00 33.80  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.964   -7.538  -7.941  1.00 24.44  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.914   -8.618  -7.672  1.00 23.20  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.726   -8.366  -6.407  1.00 21.13  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.142  -7.232  -6.125  1.00 23.13  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.809   -8.590  -8.951  1.00 25.14  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.897   -8.006  -10.019 1.00 27.30  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.128   -6.912  -9.287  1.00 25.51  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.859   -9.450  -5.631  1.00 20.39  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.559  -9.384  -4.361  1.00 20.63  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.633   -9.245  -3.160  1.00 21.94  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.032  -9.493  -2.029  1.00 22.33  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.378   -8.811  -3.393  1.00 18.84  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.504   -8.765  -2.241  1.00 18.80  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.232   -10.157 -1.640  1.00 17.15  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.060   -11.127 -2.356  1.00 19.14  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.173   -8.164  -2.687  1.00 18.89  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.168   -6.670  -2.906  1.00 22.57  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.076   -5.974  -2.431  1.00 24.09  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.148   -6.154  -3.472  1.00 24.07  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.102   -10.201 -0.309  1.00 19.29  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.945   -11.442 0.440   1.00 18.16  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.464   -11.544 0.825   1.00 19.54  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.888   -10.540 1.271   1.00 21.51  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.889   -11.463 1.659   1.00 18.68  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.381   -11.298 1.280   1.00 19.87  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.224  -11.390 2.543   1.00 22.41  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.784   -12.331 0.248   1.00 21.57  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.926   -12.771 0.714   1.00 17.85  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.480   -12.950 0.916   1.00 18.18  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.253   -14.313 1.543   1.00 19.55  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.096   -15.200 1.603   1.00 20.38  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.648   -12.850 -0.371  1.00 18.51  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.826   -11.480 -1.026  1.00 20.25  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.094   -13.906 -1.385  1.00 20.52  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.017   -14.511 2.077   1.00 18.83  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.440   -15.841 2.051   1.00 20.02  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.454   -15.902 0.895   1.00 20.07  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.311  -14.941 0.693   1.00 21.93  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.688   -16.229 3.354   1.00 21.35  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.634   -16.279 4.528   1.00 20.34  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.932   -15.101 5.203   1.00 22.52  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.132   -17.508 4.962   1.00 22.36  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.834   -15.181 6.285   1.00 27.65  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.058   -17.572 6.022   1.00 23.70  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.384   -16.419 6.658   1.00 25.34  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.581   -16.966 0.093   1.00 19.71  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.191  -17.148 -1.126  1.00 20.53  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.188  -18.290 -0.894  1.00 21.83  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.797  -19.354 -0.412  1.00 23.20  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.699   -17.416 -2.341  1.00 21.33  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.469  -18.086 -1.283  1.00 21.89  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.461  -19.139 -1.077  1.00 24.14  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.825  -19.828 -2.389  1.00 24.90  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.188  -19.170 -3.345  1.00 28.67  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.670  -18.473 -0.414  1.00 24.37  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.801  -19.506 -0.027  1.00 27.41  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.325  -20.352 1.156   1.00 30.14  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.409  -21.195 1.806   1.00 32.65  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.780  -22.322 0.939   1.00 34.54  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.771  -21.173 -2.337  1.00 26.16  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.168  -22.111 -3.370  1.00 30.44  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.290  -22.947 -2.748  1.00 30.09  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.248  -23.268 -1.573  1.00 27.89  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -2.961  -23.037 -3.630  1.00 31.69  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.672  -22.298 -4.097  1.00 31.65  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.865  -21.773 -5.813  1.00 35.09  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.530  -23.314 -6.575  1.00 28.86  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.248  -23.328 -3.592  1.00 35.92  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.347  -24.183 -3.163  1.00 40.08  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.778  -25.469 -2.585  1.00 32.78  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.852  -26.071 -3.140  1.00 35.06  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.068  -24.590 -4.449  1.00 43.38  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.245  -25.527 -4.221  1.00 49.01  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.503 -24.753 -4.604  1.00 61.85  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.255  -25.860 -1.389  1.00 37.02  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.804  -27.124 -0.837  1.00 33.09  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.494  -27.050 -0.065  1.00 37.89  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.046  -28.027 0.516   1.00 42.65  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.873  -25.862 -0.056  1.00 33.01  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.635  -25.753 0.681   1.00 34.44  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.739  -24.615 1.673   1.00 28.65  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.470  -23.662 1.462   1.00 29.73  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.467  -25.397 -0.235  1.00 35.25  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -1.990  -26.419 -1.254  1.00 37.87  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -0.865  -27.186 -0.986  1.00 49.47  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.607  -26.549 -2.496  1.00 39.75  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.389  -28.096 -1.918  1.00 47.73  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.127  -27.447 -3.448  1.00 46.47  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.009  -28.216 -3.149  1.00 50.34  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.477  -29.142 -4.016  1.00 61.74  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -2.967  -24.682 2.769   1.00 29.40  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.923  -23.591 3.755   1.00 27.82  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.228  -22.388 3.080   1.00 25.72  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.448  -22.580 2.149   1.00 26.60  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.089  -24.204 4.906   1.00 31.48  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.250  -25.283 4.218   1.00 32.53  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.036  -25.804 3.060   1.00 32.02  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.510  -21.214 3.604   1.00 25.27  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.823  -19.988 3.163   1.00 22.60  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.314  -20.222 3.283   1.00 25.74  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.150   -20.665 4.323   1.00 24.44  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.265  -18.793 4.006   1.00 24.23  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.703  -18.387 3.856   1.00 23.89  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.716  -19.073 4.513   1.00 29.61  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.262  -17.390 3.139   1.00 25.25  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.876  -18.499 4.156   1.00 28.89  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.636  -17.460 3.362   1.00 30.71  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.436   -19.996 2.174   1.00 22.81  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.753   -20.644 2.036   1.00 22.52  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.803   -19.547 1.893   1.00 22.15  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.644   -18.652 1.084   1.00 21.90  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.792   -21.522 0.785   1.00 21.90  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.883   -22.562 0.837   1.00 24.40  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.232   -22.393 0.649   1.00 26.66  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.687   -23.951 1.162   1.00 26.38  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.868   -23.606 0.785   1.00 24.73  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.954   -24.570 1.116   1.00 27.17  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.574   -24.737 1.475   1.00 29.98  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.148   -25.929 1.370   1.00 31.53  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.767   -26.085 1.726   1.00 31.36  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 3.036   -26.667 1.681   1.00 35.34  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.954   -19.651 2.601   1.00 21.56  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.996   -18.623 2.432   1.00 20.26  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.534   -18.580 0.994   1.00 19.05  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.852   -19.609 0.398   1.00 20.76  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.072   -19.080 3.436   1.00 19.61  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.905   -20.570 3.583   1.00 19.95  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.348   -20.764 3.495   1.00 22.78  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.621   -17.376 0.432   1.00 17.27  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.931   -17.252 -0.982  1.00 18.67  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.442   -15.846 -1.292  1.00 18.24  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.438   -14.957 -0.463  1.00 18.01  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.637   -17.593 -1.831  1.00 20.39  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.958   -15.684 -2.517  1.00 17.95  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.365   -14.363 -2.987  1.00 17.64  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.835   -14.080 -4.385  1.00 18.50  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.573   -15.040 -5.135  1.00 19.68  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.899   -14.247 -2.934  1.00 19.58  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.653   -15.083 -3.954  1.00 19.84  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.202  -14.920 -3.800  1.00 20.85  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.833  -15.705 -4.882  1.00 22.24  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.119  -16.119 -4.732  1.00 21.95  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.764  -15.938 -3.609  1.00 22.27  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.667  -16.738 -5.764  1.00 26.44  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.691   -12.796 -4.734  1.00 19.63  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.496   -12.446 -6.136  1.00 18.95  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.826   -12.573 -6.854  1.00 21.63  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.781   -11.918 -6.459  1.00 22.21  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 6.041   -10.989 -6.237  1.00 20.91  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.866   -10.709 -5.263  1.00 26.20  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.688   -10.644 -7.701  1.00 22.99  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.551   -11.353 -5.621  1.00 31.43  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.856   -13.405 -7.874  1.00 22.13  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.115   -13.581 -8.599  1.00 23.13  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.244   -12.562 -9.725  1.00 25.83  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.306   -11.950 -10.233 1.00 25.05  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.233   -14.955 -9.198  1.00 23.99  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.217  -15.897 -8.542  1.00 23.75  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.847  -15.483 -7.512  1.00 29.45  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.349  -17.016 -9.004  1.00 27.22  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.494  -12.447 -10.216 1.00 29.07  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.710  -11.781 -11.483 1.00 34.99  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.474  -12.796 -12.606 1.00 31.85  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.336  -13.997 -12.389 1.00 33.44  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.161  -11.348 -11.660 1.00 38.97  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.652  -10.130 -10.888 1.00 47.20  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.266  -8.993  -11.251 1.00 48.92  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.437  -10.341 -9.936  1.00 48.61  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.399  -12.280 -13.822 1.00 36.06  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.293  -13.173 -14.970 1.00 31.71  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.632  -12.999 -15.682 1.00 30.52  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.986  -11.867 -15.950 1.00 33.04  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.145   -12.655 -15.845 1.00 35.92  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.810   -12.686 -15.085 1.00 38.02  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.071   -13.470 -17.135 1.00 33.15  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.825   -11.659 -15.587 1.00 37.64  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.384  -14.090 -15.815 1.00 34.30  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.679  -14.031 -16.491 1.00 28.77  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.470  -13.702 -17.979 1.00 32.61  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.435  -14.005 -18.570 1.00 32.91  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.346  -15.373 -16.323 1.00 34.43  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.449  -13.023 -18.578 1.00 31.66  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.432  -12.897 -20.038 1.00 32.92  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.216  -14.273 -20.657 1.00 27.31  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.843  -15.233 -20.244 1.00 31.71  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.773  -12.339 -20.497 1.00 31.63  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.966  -10.845 -20.315 1.00 34.54  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.974  -10.128 -20.239 1.00 37.53  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.136  -10.390 -20.261 1.00 38.08  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.317  -14.350 -21.653 1.00 26.63  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.053  -15.581 -22.370 1.00 26.49  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.104  -16.556 -21.681 1.00 34.98  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.714  -17.563 -22.277 1.00 36.79  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.709  -16.230 -20.447 1.00 32.27  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.868  -17.129 -19.663 1.00 33.84  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.398   -16.908 -20.001 1.00 32.31  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.971   -15.858 -20.443 1.00 30.14  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.106  -16.824 -18.188 1.00 33.98  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.569   -17.933 -19.739 1.00 33.92  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.124   -17.796 -19.940 1.00 35.55  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.484   -16.744 -19.018 1.00 34.37  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.692   -16.794 -17.818 1.00 35.76  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.522   -19.187 -19.654 1.00 38.26  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.994   -19.123 -19.677 1.00 40.47  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.049   -20.243 -20.632 1.00 39.36  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.734   -15.802 -19.596 1.00 34.83  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.061   -14.712 -18.881 1.00 32.16  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.738   -15.201 -18.289 1.00 37.65  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.073   -16.065 -18.839 1.00 37.41  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.782   -13.447 -19.693 1.00 34.78  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.060   -12.791 -20.247 1.00 36.23  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.847   -11.539 -21.099 1.00 43.06  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.249   -11.874 -22.446 1.00 50.12  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.194   -10.718 -23.338 1.00 51.08  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.272   -14.606 -17.169 1.00 35.56  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.002   -15.021 -16.575 1.00 36.74  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.872   -14.481 -17.440 1.00 36.37  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.046   -13.545 -18.204 1.00 37.76  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.959   -14.401 -15.180 1.00 37.12  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.038   -13.317 -15.190 1.00 37.32  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.874   -13.460 -16.492 1.00 34.93  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.352  -14.993 -17.244 1.00 38.44  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.545  -14.350 -17.825 1.00 41.35  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.750  -12.910 -17.357 1.00 44.22  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.285  -12.548 -16.276 1.00 34.88  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.658  -15.264 -17.292 1.00 39.48  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -1.992  -16.585 -16.994 1.00 37.39  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.624  -16.212 -16.460 1.00 39.33  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.487  -12.032 -18.084 1.00 37.25  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.841  -10.710 -17.560 1.00 38.75  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.439  -10.764 -16.155 1.00 34.22  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.202  -11.671 -15.823 1.00 38.01  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.833  -10.110 -18.591 1.00 46.79  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.196  -11.296 -19.446 1.00 40.96  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.044  -12.274 -19.440 1.00 44.87  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.069  -9.774  -15.339 1.00 38.57  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.573  -9.576  -13.997 1.00 38.81  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.078  -10.668 -13.053 1.00 33.35  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.555  -10.699 -11.921 1.00 34.98  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.097  -9.479  -13.952 1.00 45.96  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.591  -8.349  -14.827 1.00 49.46  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.333  -7.173  -14.530 1.00 45.44  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.277  -8.687  -15.907 1.00 52.06  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.112  -11.506 -13.509 1.00 28.97  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.590  -12.568 -12.649 1.00 23.95  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.099  -12.278 -12.409 1.00 25.00  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.574   -11.560 -13.155 1.00 27.51  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.717  -14.007 -13.140 1.00 26.81  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.108  -14.535 -13.643 1.00 29.88  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.007  -14.551 -12.422 1.00 33.79  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.408  -15.117 -12.734 1.00 36.50  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.548  -16.560 -12.968 1.00 48.11  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.387   -12.791 -11.275 1.00 22.15  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.789   -12.656 -10.895 1.00 22.55  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.417   -14.028 -10.819 1.00 21.70  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.799   -15.004 -10.413 1.00 22.47  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.904   -12.016 -9.487  1.00 22.44  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.432   -10.577 -9.479  1.00 24.20  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.066   -10.319 -9.279  1.00 26.42  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.265   -9.497  -9.653  1.00 26.09  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.451  -9.038  -9.384  1.00 27.42  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.772   -8.194  -9.685  1.00 26.13  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.411   -7.980  -9.569  1.00 31.31  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.118  -6.728  -9.733  1.00 31.94  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.753   -14.139 -11.052 1.00 22.41  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.421   -15.409 -10.833 1.00 21.61  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.796   -15.522 -9.365  1.00 20.64  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.460   -14.631 -8.831  1.00 22.81  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.693   -15.294 -11.726 1.00 22.80  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.900   -13.852 -11.913 1.00 23.00  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.611   -13.052 -11.518 1.00 24.97  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.260   -16.554 -8.732  1.00 21.02  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.443   -16.727 -7.293  1.00 19.73  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.383   -17.903 -7.087  1.00 22.52  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.096   -19.049 -7.541  1.00 24.18  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.098   -16.995 -6.623  1.00 20.68  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.096   -15.863 -6.894  1.00 21.89  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.314   -17.226 -5.119  1.00 20.52  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.627   -14.470 -6.543  1.00 22.13  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.521   -17.674 -6.398  1.00 20.19  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.372   -18.764 -6.029  1.00 21.48  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.063   -19.142 -4.592  1.00 20.38  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.123   -18.321 -3.677  1.00 21.07  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.817   -18.257 -6.219  1.00 21.79  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.835   -19.293 -5.775  1.00 22.16  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.226  -20.293 -6.674  1.00 24.92  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.435  -19.232 -4.505  1.00 25.80  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.209  -21.208 -6.280  1.00 27.49  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.380  -20.197 -4.115  1.00 26.67  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.767  -21.162 -5.027  1.00 27.27  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.788   -20.415 -4.391  1.00 21.45  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.422   -20.945 -3.113  1.00 21.23  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.667   -21.474 -2.411  1.00 23.23  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.395   -22.344 -2.956  1.00 23.59  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.381   -22.072 -3.318  1.00 23.03  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.992   -21.609 -3.703  1.00 21.66  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.676   -21.419 -5.017  1.00 26.14  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 3.031   -21.354 -2.739  1.00 24.11  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.426   -20.950 -5.404  1.00 27.47  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.787   -20.861 -3.118  1.00 26.20  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.498   -20.679 -4.435  1.00 25.90  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.933   -20.917 -1.233  1.00 21.18  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.109   -21.371 -0.488  1.00 21.82  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.887   -22.818 -0.059  1.00 23.62  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.762   -23.285 0.102   1.00 25.10  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.390   -20.443 0.699   1.00 23.79  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.837   -19.062 0.280   1.00 20.64  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.118  -18.875 -0.255  1.00 20.31  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.069   -17.937 0.572   1.00 21.63  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.504  -17.594 -0.621  1.00 19.15  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.476   -16.660 0.256   1.00 19.85  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.736  -16.481 -0.319  1.00 19.21  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 10.008  -23.527 0.139   1.00 24.87  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.943   -24.896 0.647   1.00 24.54  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.697   -25.880 -0.508  1.00 29.53  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.547  -26.696 -0.842  1.00 32.34  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.542   -25.783 -1.187  1.00 28.30  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.310   -26.626 -2.356  1.00 28.88  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.110   -26.162 -3.569  1.00 29.46  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.394   -26.928 -4.490  1.00 29.57  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.821   -26.714 -2.687  1.00 30.23  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.399   -25.410 -3.129  1.00 29.87  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.987   -27.253 -1.557  1.00 29.62  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.392   -24.857 -3.639  1.00 25.02  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.091  -24.252 -4.752  1.00 25.86  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.288   -24.395 -6.039  1.00 26.98  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.837   -24.333 -7.126  1.00 29.70  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.530  -24.773 -4.911  1.00 25.81  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.261  -24.797 -3.602  1.00 27.88  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.071  -25.841 -3.196  1.00 31.52  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.320  -23.874 -2.599  1.00 26.73  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.563  -25.568 -1.989  1.00 33.15  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.153  -24.344 -1.625  1.00 28.72  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.963   -24.432 -5.896  1.00 28.13  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 7.103   -24.462 -7.072  1.00 29.31  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.604   -23.061 -7.450  1.00 27.93  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.770   -22.100 -6.679  1.00 25.94  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.901   -25.368 -6.835  1.00 32.04  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.351   -26.818 -6.656  1.00 42.83  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.318   -27.799 -6.147  1.00 51.13  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 4.106   -27.489 -6.055  1.00 46.47  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.791   -28.915 -5.833  1.00 49.56  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.140   -22.884 -8.698  1.00 25.68  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.661   -21.615 -9.211  1.00 24.72  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.223   -21.830 -9.653  1.00 27.22  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.933   -22.828 -10.343 1.00 28.96  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.470   -21.064 -10.390 1.00 30.20  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.784   -20.723 -9.936  1.00 29.70  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.870   -19.787 -10.973 1.00 33.81  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.320   -20.936 -9.238  1.00 24.15  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.993   -20.834 -9.832  1.00 24.06  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.706   -19.363 -10.138 1.00 25.18  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.381   -18.427 -9.664  1.00 25.57  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.959   -21.385 -8.854  1.00 25.48  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.642   -19.103 -10.924 1.00 24.86  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.291   -17.749 -11.283 1.00 24.84  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -0.975  -17.410 -10.502 1.00 29.60  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -1.971  -18.125 -10.542 1.00 31.89  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.016  -17.644 -12.786 1.00 26.28  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.171   -18.010 -13.642 1.00 29.85  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.316   -17.221 -13.590 1.00 33.45  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.114   -19.076 -14.523 1.00 37.65  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.429   -17.527 -14.371 1.00 44.32  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.221   -19.367 -15.296 1.00 39.02  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.360   -18.603 -15.239 1.00 37.59  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.910  -16.322 -9.749  1.00 23.09  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.016  -15.959 -8.874  1.00 22.29  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.297  -14.474 -8.992  1.00 23.10  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.459  -13.641 -9.351  1.00 22.85  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.674  -16.258 -7.412  1.00 24.12  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.610  -17.733 -7.084  1.00 22.62  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.234  -17.892 -5.602  1.00 24.19  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.052  -18.329 -7.289  1.00 27.99  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.576  -14.130 -8.706  1.00 21.41  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.859  -12.717 -8.630  1.00 21.67  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.903  -12.228 -7.180  1.00 19.08  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.891  -13.024 -6.247  1.00 20.16  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.006  -10.913 -7.001  1.00 21.22  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.006  -10.294 -5.675  1.00 21.09  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.967  -10.798 -4.609  1.00 20.90  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.667  -10.768 -3.420  1.00 21.95  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.218  -8.806  -5.945  1.00 22.31  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.635  -8.607  -7.354  1.00 23.84  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -3.982  -9.908  -8.074  1.00 22.46  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.112  -11.323 -5.099  1.00 22.90  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.074  -11.839 -4.133  1.00 20.34  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.534  -13.001 -3.290  1.00 22.16  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -6.957  -13.238 -2.163  1.00 21.92  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.361  -12.335 -4.839  1.00 25.98  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.208  -13.686 -5.508  1.00 30.41  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.498  -14.168 -6.186  1.00 32.34  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.313  -15.506 -6.861  1.00 33.20  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.319  -16.615 -5.911  1.00 41.44  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.447  -13.675 -3.781  1.00 20.19  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.884  -14.824 -3.107  1.00 22.13  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.514  -14.459 -2.478  1.00 18.87  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.850  -15.369 -2.009  1.00 22.04  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.819  -15.990 -4.102  1.00 23.31  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.217  -16.556 -4.400  1.00 25.42  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.006  -16.608 -3.448  1.00 29.09  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.474  -16.929 -5.539  1.00 29.61  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.192  -13.162 -2.446  1.00 19.44  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.858  -12.750 -1.940  1.00 18.65  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.013  -11.885 -0.692  1.00 17.41  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.596  -10.791 -0.706  1.00 19.07  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.124  -11.993 -3.049  1.00 19.73  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -0.962  -12.762 -4.352  1.00 20.30  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.238  -11.923 -5.445  1.00 21.28  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.273  -14.088 -4.207  1.00 22.12  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.402  -12.372 0.404   1.00 19.23  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.499  -11.710 1.716   1.00 19.71  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.113  -11.187 2.099   1.00 20.69  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.787   -12.000 2.310   1.00 21.96  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.982  -12.751 2.736   1.00 20.87  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.427  -13.183 2.474   1.00 22.00  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.708  -14.085 1.493   1.00 23.02  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.417  -12.619 3.254   1.00 23.23  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.028  -14.432 1.201   1.00 24.45  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.730  -12.997 2.969   1.00 23.05  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -5.994  -13.887 1.999   1.00 23.87  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.096   -9.881  2.259   1.00 22.71  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.451   -9.371  2.557   1.00 22.20  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.977   -10.030 3.819   1.00 21.97  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.320   -10.246 4.834   1.00 23.57  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.209   -7.869  2.747   1.00 24.96  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.101   -7.553  1.683   1.00 27.21  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.836  -8.776  1.925   1.00 24.82  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.269   -10.480 3.797   1.00 22.32  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.815   -11.331 4.834   1.00 21.29  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.891   -10.678 6.232   1.00 22.05  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.547   -11.367 7.167   1.00 25.84  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.243   -11.697 4.341   1.00 22.05  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 6.032   -12.500 5.367   1.00 21.98  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.771   -13.842 5.646   1.00 21.91  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.103   -11.890 6.033   1.00 26.81  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.446   -14.574 6.630   1.00 25.50  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.817   -12.652 6.959   1.00 25.29  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.505   -13.954 7.265   1.00 25.91  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.246   -14.698 8.207   1.00 28.55  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.296   -9.416  6.272   1.00 24.85  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.450   -8.719  7.573   1.00 29.89  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.129   -8.705  8.356   1.00 26.78  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 3.083   -9.274  9.450   1.00 36.78  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.137   -7.367  7.443   1.00 32.50  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 6.655   -7.387  7.254   1.00 50.98  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 7.193   -6.412  6.655   1.00 58.90  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 7.310   -8.323  7.771   1.00 60.44  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 2.070   -8.255  7.670   1.00 30.21  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 0.742   -8.159  8.284   1.00 29.27  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? 0.222   -9.535  8.680   1.00 30.50  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.488  -9.639  9.681   1.00 30.01  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -0.202  -7.572  7.235   1.00 29.47  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -1.680  -7.375  7.721   1.00 32.04  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.442  -6.651  6.613   1.00 34.35  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -3.560  -5.842  7.163   1.00 43.27  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.631  -6.680  7.685   1.00 48.97  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.549   -10.605 7.922   1.00 27.73  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -0.114  -11.891 7.986   1.00 27.20  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.620   -12.984 8.771   1.00 26.72  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? 0.079   -14.080 8.973   1.00 27.64  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.404  -12.415 6.581   1.00 30.41  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.241  -11.469 5.935   1.00 36.68  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 1.884   -12.722 9.127   1.00 28.01  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.719   -13.798 9.638   1.00 31.03  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 2.271   -14.331 11.001  1.00 27.65  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.400   -15.527 11.277  1.00 30.62  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 4.209   -13.428 9.602   1.00 28.76  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.561   -12.230 10.431  1.00 29.92  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 6.043   -11.982 10.165  1.00 39.91  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.564   -11.046 11.219  1.00 46.20  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 5.927   -9.730  11.099  1.00 54.76  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.666   -13.449 11.807  0.50 32.43  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 1.698   -13.449 11.827  0.50 32.01  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 1.155   -13.853 13.114  0.50 34.71  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 1.154   -13.900 13.103  0.50 33.40  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? 0.041   -14.896 12.978  0.50 33.82  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? 0.152   -15.028 12.870  0.50 32.47  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? -0.126  -15.761 13.825  0.50 35.41  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? 0.203   -16.079 13.503  0.50 34.94  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.817   -12.632 13.956  0.50 37.37  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.512   -12.742 13.847  0.50 36.35  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 2.005   -11.934 14.606  0.50 39.83  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? 0.031   -13.054 15.258  0.50 38.20  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 3.100   -12.535 14.636  0.50 42.43  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.892   -13.192 16.155  0.50 43.48  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.841   -10.789 15.085  0.50 42.14  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.204  -13.151 15.446  0.50 49.15  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -0.745  -14.821 11.901  1.00 30.80  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -1.817  -15.759 11.675  1.00 29.66  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.372  -16.988 10.905  1.00 32.04  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -1.860  -18.084 11.155  1.00 34.62  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -2.888  -14.953 10.937  1.00 31.98  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -4.139  -15.735 10.674  1.00 33.54  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -5.226  -14.816 10.106  1.00 39.37  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.502  -15.544 9.784   1.00 44.09  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.463  -14.613 9.159   1.00 44.13  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.512  -16.800 9.880   1.00 28.38  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -0.270  -17.880 8.934   1.00 27.71  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 1.118   -18.531 9.082   1.00 25.49  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 1.315   -19.618 8.558   1.00 29.54  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.438  -17.359 7.493   1.00 24.98  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -1.843  -16.928 7.105   1.00 27.70  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -2.969  -17.659 7.497   1.00 29.67  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -2.008  -15.740 6.393   1.00 27.26  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.244  -17.244 7.104   1.00 29.93  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.278  -15.311 6.024   1.00 29.27  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.389  -16.068 6.385   1.00 30.37  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -5.624  -15.627 5.987   1.00 29.22  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 1.994   -17.911 9.875   1.00 26.52  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 3.400   -18.331 9.978   1.00 25.96  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.613   -19.321 11.128  1.00 30.30  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 4.374   -19.035 12.023  1.00 37.26  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.866   -20.409 11.125  1.00 32.96  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 2.989   -21.429 12.155  1.00 34.64  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 3.275   -22.751 11.450  1.00 31.19  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 2.881   -22.968 10.307  1.00 34.62  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 1.749   -21.433 13.061  1.00 41.65  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 1.624   -20.142 13.874  1.00 41.91  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? 0.641   -20.162 15.038  1.00 49.56  ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 3.988   -23.725 12.078  1.00 34.55  ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 4.282   -24.974 11.371  1.00 32.70  ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 3.059   -25.740 10.907  1.00 32.79  ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 2.000   -25.646 11.532  1.00 39.84  ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 5.145   -25.772 12.378  1.00 38.89  ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 5.647   -24.725 13.346  1.00 43.28  ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 4.553   -23.649 13.433  1.00 43.42  ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 3.233   -26.495 9.830   1.00 37.14  ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 2.147   -27.218 9.203   1.00 38.84  ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.751   -28.537 8.755   1.00 45.64  ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 3.928   -28.610 8.394   1.00 44.66  ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.597   -26.377 8.046   1.00 39.91  ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? 0.281   -26.854 7.471   1.00 50.57  ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? 0.263   -27.641 6.520   1.00 46.14  ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -0.827  -26.309 7.960   1.00 50.64  ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 1.934   -29.581 8.796   1.00 48.51  ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 2.387   -30.912 8.461   1.00 45.61  ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.693   -31.051 6.971   1.00 44.18  ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 3.345   -32.014 6.570   1.00 43.81  ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 1.290   -31.866 8.964   1.00 56.86  ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? 0.009   -31.946 8.125   1.00 58.86  ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 2.241   -30.113 6.121   1.00 40.33  ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 2.337   -30.354 4.689   1.00 38.41  ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.785   -30.297 4.199   1.00 36.15  ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 4.571   -29.489 4.703   1.00 33.45  ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 1.480   -29.372 3.876   1.00 40.61  ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? -0.004  -29.482 4.208   1.00 47.64  ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -0.703  -30.641 3.504   1.00 43.43  ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -1.420  -30.229 2.293   1.00 55.22  ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -2.560  -29.514 2.288   1.00 49.67  ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -3.174  -29.283 1.144   1.00 60.57  ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -3.115  -29.100 3.417   1.00 58.39  ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 4.082   -31.136 3.198   1.00 37.62  ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 5.402   -31.285 2.604   1.00 37.48  ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 5.932   -29.910 2.199   1.00 33.99  ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 5.314   -29.224 1.379   1.00 32.26  ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 5.360   -32.232 1.396   1.00 39.91  ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.646   -32.507 0.610   1.00 45.52  ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.538   -33.579 -0.478  1.00 47.78  ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 7.812   -33.796 -1.257  1.00 52.92  ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 7.095   -29.557 2.758   1.00 31.97  ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 7.821   -28.371 2.316   1.00 30.10  ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 7.448   -27.135 3.124   1.00 31.03  ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 8.152   -26.138 2.999   1.00 30.55  ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 6.383   -27.181 3.925   1.00 28.83  ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 5.902   -25.965 4.554   1.00 27.46  ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 6.925   -25.389 5.542   1.00 30.03  ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 7.193   -24.179 5.591   1.00 27.68  ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 4.511   -26.226 5.147   1.00 28.38  ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 3.797   -24.946 5.542   1.00 29.16  ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 4.049   -24.289 6.739   1.00 28.47  ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 2.822   -24.417 4.679   1.00 30.05  ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 3.398   -23.113 7.083   1.00 30.74  ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 2.135   -23.263 5.048   1.00 27.61  ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 2.423   -22.601 6.219   1.00 27.14  ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 7.448   -26.235 6.435   1.00 28.03  ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 8.325   -25.731 7.489   1.00 26.72  ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.686   -25.286 6.895   1.00 25.04  ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 10.268  -24.283 7.377   1.00 26.60  ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 8.457   -26.809 8.574   1.00 29.30  ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 7.103   -27.086 9.191   1.00 34.11  ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 6.206   -26.223 9.219   1.00 32.03  ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 6.960   -28.273 9.778   1.00 32.43  ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 10.141  -25.949 5.818   1.00 25.74  ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 11.293  -25.452 5.087   1.00 25.95  ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 10.952  -24.053 4.558   1.00 24.93  ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 11.769  -23.113 4.608   1.00 24.38  ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 11.738  -26.357 3.931   1.00 27.26  ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 13.018  -25.893 3.232   1.00 29.27  ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 13.492  -26.938 2.221   1.00 39.41  ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 12.739  -27.887 1.908   1.00 45.28  ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 14.617  -26.823 1.757   1.00 39.76  ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 9.727   -23.945 4.033   1.00 24.99  ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 9.362   -22.652 3.453   1.00 25.87  ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 9.315   -21.549 4.511   1.00 22.73  ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.611   -20.386 4.215   1.00 22.32  ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 8.838   -21.837 5.740   1.00 22.21  ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 8.862   -20.856 6.803   1.00 23.10  ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 10.288  -20.388 7.098   1.00 21.93  ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.502  -19.207 7.365   1.00 22.59  ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 8.191   -21.335 8.102   1.00 25.28  ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 6.683   -21.632 7.996   1.00 25.25  ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 6.312   -22.194 9.357   1.00 28.20  ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 5.924   -20.345 7.782   1.00 26.55  ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 11.260  -21.334 7.025   1.00 23.30  ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.631  -20.925 7.286   1.00 24.59  ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 13.110  -19.990 6.185   1.00 23.15  ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 13.771  -19.005 6.480   1.00 23.10  ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.541  -22.179 7.418   1.00 24.73  ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 14.995  -21.823 7.687   1.00 23.47  ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.595  -21.711 8.910   1.00 26.91  ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 15.980  -21.501 6.669   1.00 22.29  ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 16.916  -21.357 8.721   1.00 27.78  ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 17.164  -21.207 7.377   1.00 24.93  ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 15.966  -21.437 5.262   1.00 24.19  ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 18.336  -20.854 6.703   1.00 25.77  ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 17.129  -21.078 4.583   1.00 25.16  ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 18.294  -20.802 5.319   1.00 26.84  ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 12.826  -20.345 4.935   1.00 20.73  ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 13.310  -19.600 3.803   1.00 20.69  ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 12.795  -18.166 3.856   1.00 22.49  ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.525  -17.219 3.634   1.00 21.44  ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 12.892  -20.239 2.495   1.00 20.92  ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.632  -21.561 2.345   1.00 22.29  ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 13.225  -22.306 1.085   1.00 24.76  ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 12.267  -21.910 0.379   1.00 24.17  ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 13.841  -23.401 0.773   1.00 25.61  ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 11.459  -17.994 4.062   1.00 19.43  ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 10.909  -16.648 3.976   1.00 19.48  ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 11.440  -15.758 5.108   1.00 20.15  ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.582  -14.569 4.922   1.00 21.43  ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 9.353   -16.698 3.961   1.00 19.44  ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 8.760   -15.334 3.569   1.00 19.32  ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 8.786   -17.086 5.334   1.00 21.78  ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 7.317   -15.434 3.064   1.00 19.06  ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 11.780  -16.343 6.276   1.00 21.06  ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 12.311  -15.580 7.416   1.00 21.44  ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 13.810  -15.321 7.277   1.00 22.35  ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 14.255  -14.196 7.645   1.00 26.55  ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 12.000  -16.357 8.694   1.00 25.77  ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 12.483  -15.679 9.970   1.00 29.55  ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 11.868  -16.274 11.232  1.00 34.19  ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 11.577  -17.483 11.317  1.00 36.19  ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 11.579  -15.403 12.192  1.00 42.02  ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.549  -16.274 6.719   1.00 21.38  ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 16.008  -16.244 6.801   1.00 20.87  ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 16.733  -15.935 5.504   1.00 23.34  ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 17.845  -15.380 5.571   1.00 24.90  ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 16.550  -17.533 7.419   1.00 23.05  ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 16.069  -17.619 8.858   1.00 27.09  ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 16.383  -16.733 9.686   1.00 31.26  ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 15.162  -18.532 9.172   1.00 25.28  ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 16.174  -16.252 4.338   1.00 22.27  ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 16.828  -15.895 3.096   1.00 20.91  ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 15.784  -15.845 1.980   1.00 22.19  ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 15.793  -16.583 0.991   1.00 20.88  ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 18.024  -16.818 2.774   1.00 23.09  ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 19.062  -16.189 1.874   1.00 25.20  ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 18.865  -15.189 1.197   1.00 22.28  ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 20.286  -16.716 1.889   1.00 28.05  ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 14.864  -14.873 2.097   1.00 20.83  ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 13.734  -14.889 1.169   1.00 19.67  ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 14.083  -14.419 -0.229  1.00 22.75  ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 13.316  -14.684 -1.132  1.00 20.62  ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 12.805  -13.872 1.815   1.00 20.34  ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 13.721  -12.913 2.561   1.00 20.41  ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 14.731  -13.874 3.177   1.00 20.50  ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 15.298  -13.854 -0.453  1.00 18.79  ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.640  -13.331 -1.762  1.00 19.51  ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 16.777  -14.134 -2.440  1.00 18.36  ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 17.211  -13.749 -3.524  1.00 23.12  ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 16.028  -11.834 -1.691  1.00 19.24  ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 14.951  -11.003 -1.075  1.00 18.48  ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.695  -10.924 -1.687  1.00 19.97  ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 14.907  -10.270 0.007   1.00 18.74  ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 12.942  -10.117 -0.958  1.00 19.93  ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.633  -9.692  0.101   1.00 22.04  ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 17.015  -15.317 -1.918  1.00 20.13  ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 18.078  -16.159 -2.484  1.00 22.55  ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.600  -16.868 -3.739  1.00 26.04  ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 16.412  -17.010 -4.012  1.00 25.49  ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.462  -17.195 -1.454  1.00 24.43  ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.566  -17.403 -4.496  1.00 25.97  ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 18.298  -18.337 -5.569  1.00 28.47  ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 18.049  -19.717 -4.980  1.00 27.82  ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 18.901  -20.241 -4.249  1.00 32.01  ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.506  -18.318 -6.470  1.00 32.87  ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 19.439  -19.393 -7.387  1.00 39.47  ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 16.898  -20.308 -5.342  1.00 27.87  ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.537  -21.655 -4.927  1.00 28.64  ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 16.396  -22.605 -6.116  1.00 33.67  ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 15.987  -23.743 -5.915  1.00 43.64  ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 15.194  -21.588 -4.164  1.00 27.39  ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 15.344  -20.970 -2.789  1.00 26.85  ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 15.801  -21.727 -1.692  1.00 26.91  ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 15.024  -19.618 -2.555  1.00 24.52  ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 15.947  -21.162 -0.423  1.00 28.40  ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 15.154  -19.078 -1.290  1.00 26.63  ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.636  -19.818 -0.231  1.00 25.54  ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 15.873  -19.302 1.009   1.00 28.06  ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 16.748  -22.145 -7.314  1.00 44.24  ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 16.944  -22.973 -8.496  1.00 54.62  ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 17.974  -24.078 -8.209  1.00 65.61  ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 19.040  -23.744 -7.638  1.00 66.78  ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 17.391  -22.111 -9.650  1.00 53.73  ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 16.331  -21.242 -10.029 1.00 62.23  ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 17.682  -25.242 -8.577  1.00 84.38  ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 38.890  -11.427 -42.210 1.00 56.82  ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.454  -12.209 -43.396 1.00 58.21  ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 36.923  -12.271 -43.385 1.00 51.95  ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.333  -12.486 -42.321 1.00 60.45  ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.088  -13.608 -43.338 1.00 60.61  ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 39.133  -14.395 -44.650 1.00 75.85  ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 40.237  -13.850 -45.976 1.00 78.00  ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 41.530  -12.896 -45.165 1.00 61.91  ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.220  -12.039 -44.530 1.00 43.05  ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.769  -12.263 -44.593 1.00 41.82  ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.452  -13.716 -44.249 1.00 45.88  ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.256  -14.595 -44.529 1.00 47.10  ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.366  -11.918 -46.011 1.00 36.89  ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.519  -11.056 -46.527 1.00 37.12  ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.765  -11.532 -45.795 1.00 37.11  ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.309  -13.942 -43.589 1.00 45.35  ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.869  -15.286 -43.235 1.00 40.90  ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.466  -15.529 -43.779 1.00 40.37  ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 30.857  -14.653 -44.401 1.00 38.29  ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 32.963  -15.528 -41.728 1.00 47.03  ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.364  -15.551 -41.224 1.00 57.07  ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.293  -16.492 -41.621 1.00 54.26  ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 35.003  -14.733 -40.363 1.00 58.48  ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.450  -16.250 -41.007 1.00 52.13  ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.294  -15.192 -40.236 1.00 57.05  ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 30.950  -16.750 -43.591 1.00 35.36  ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.629  -17.036 -44.128 1.00 37.44  ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.614  -16.018 -43.612 1.00 32.94  ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.664  -15.662 -44.309 1.00 36.14  ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.220  -18.424 -43.685 1.00 38.25  ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.738  -15.696 -42.325 1.00 40.33  ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 27.942  -14.648 -41.707 1.00 41.15  ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.799  -13.401 -41.482 1.00 35.30  ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 29.954  -13.489 -41.059 1.00 42.56  ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.403  -15.083 -40.336 1.00 38.51  ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.337  -16.168 -40.400 1.00 34.27  ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 25.007  -15.825 -40.585 1.00 32.19  ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.667  -17.524 -40.350 1.00 35.73  ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 24.023  -16.790 -40.669 1.00 34.94  ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.661  -18.480 -40.400 1.00 32.87  ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.355  -18.131 -40.549 1.00 31.49  ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.199  -12.262 -41.818 1.00 38.38  ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 28.879  -10.987 -41.662 1.00 37.46  ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.138  -10.155 -40.612 1.00 35.08  ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 26.907  -10.236 -40.476 1.00 32.38  ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 28.915  -10.253 -43.002 1.00 40.56  ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 27.606  -9.989  -43.701 1.00 45.90  ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 27.827  -9.389  -45.090 1.00 50.50  ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 26.559  -8.913  -45.728 1.00 51.70  ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 25.723  -10.037 -46.163 1.00 52.89  ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.849  -9.238  -39.927 1.00 38.42  ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.222  -8.269  -39.022 1.00 32.04  ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.026  -7.604  -39.664 1.00 34.16  ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.094  -7.118  -40.815 1.00 37.72  ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.375  -7.281  -38.846 1.00 37.66  ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.589  -8.180  -38.834 1.00 39.29  ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.312  -9.060  -40.019 1.00 44.72  ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.929  -7.545  -38.905 1.00 30.83  ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.703  -6.936  -39.370 1.00 30.16  ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.720  -7.911  -40.008 1.00 27.22  ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.585  -7.548  -40.299 1.00 29.76  ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.189  -9.141  -40.331 1.00 29.85  ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.253  -10.130 -40.839 1.00 31.12  ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.207  -10.486 -39.761 1.00 25.84  ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.521  -10.541 -38.561 1.00 28.47  ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 23.930  -11.434 -41.228 1.00 30.83  ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.698  -11.502 -42.547 1.00 37.54  ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.418  -10.668 -43.410 1.00 36.59  ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.536  -12.439 -42.680 1.00 38.05  ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 21.003  -10.640 -40.234 1.00 25.37  ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.837  -10.844 -39.370 1.00 25.17  ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.571  -12.342 -39.346 1.00 26.73  ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.624  -12.953 -40.428 1.00 28.93  ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.617  -10.026 -39.779 1.00 27.10  ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 18.904  -8.519  -39.924 1.00 26.74  ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.615  -7.816  -40.257 1.00 27.72  ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.547  -8.045  -38.651 1.00 29.47  ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.209  -12.891 -38.156 1.00 24.23  ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 19.029  -14.340 -38.054 1.00 24.61  ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.948  -14.606 -37.016 1.00 25.18  ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.556  -13.718 -36.255 1.00 25.16  ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.344  -15.000 -37.593 1.00 23.93  ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.470  -14.807 -38.624 1.00 27.73  ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.804  -14.612 -36.172 1.00 25.76  ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.531  -15.882 -36.952 1.00 23.17  ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 17.024  -16.427 -35.702 1.00 23.77  ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 18.103  -17.298 -35.092 1.00 25.10  ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.719  -18.081 -35.838 1.00 26.00  ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.761  -17.242 -35.934 1.00 24.30  ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.538  -16.438 -36.346 1.00 23.95  ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.300  -16.148 -37.684 1.00 28.22  ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.663  -15.946 -35.384 1.00 26.51  ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 13.198  -15.413 -38.057 1.00 31.16  ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.544  -15.213 -35.755 1.00 28.87  ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.311  -14.951 -37.098 1.00 32.50  ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.335  -17.141 -33.778 1.00 23.45  ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.382  -17.845 -33.077 1.00 23.21  ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.745  -18.825 -32.071 1.00 24.52  ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.818  -18.471 -31.339 1.00 24.77  ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.327  -16.901 -32.348 1.00 25.99  ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 19.232  -20.063 -32.072 1.00 24.57  ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.629  -21.094 -31.216 1.00 26.99  ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.508  -21.385 -30.011 1.00 27.63  ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.689  -21.695 -30.150 1.00 28.67  ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.434  -22.354 -32.067 1.00 27.70  ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.777  -23.505 -31.228 1.00 25.37  ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 16.306  -23.171 -31.007 1.00 29.13  ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 15.393  -24.281 -30.357 1.00 30.06  ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.909  -24.494 -29.015 1.00 31.06  ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.884  -21.313 -28.822 1.00 28.02  ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.507  -21.714 -27.558 1.00 29.94  ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.656  -22.806 -26.912 1.00 30.24  ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.424  -22.786 -27.029 1.00 27.94  ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 19.551  -20.537 -26.582 1.00 33.49  ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 20.159  -19.282 -27.135 1.00 38.60  ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 21.943  -19.319 -26.878 1.00 46.87  ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 22.114  -19.086 -25.104 1.00 44.72  ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 19.338  -23.766 -26.251 1.00 31.40  ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.611  -24.833 -25.559 1.00 31.94  ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.627  -24.213 -24.555 1.00 29.55  ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 17.985  -23.323 -23.797 1.00 33.44  ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.638  -25.748 -24.872 1.00 41.15  ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 19.017  -27.009 -24.248 1.00 44.23  ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 19.951  -27.934 -23.476 1.00 48.50  ? 16  LYS B CD  1 
ATOM   881  N N   . GLY B 1 18 ? 16.366  -24.652 -24.645 1.00 31.98  ? 17  GLY B N   1 
ATOM   882  C CA  . GLY B 1 18 ? 15.318  -24.208 -23.733 1.00 32.37  ? 17  GLY B CA  1 
ATOM   883  C C   . GLY B 1 18 ? 14.476  -23.047 -24.262 1.00 33.02  ? 17  GLY B C   1 
ATOM   884  O O   . GLY B 1 18 ? 13.496  -22.631 -23.623 1.00 35.54  ? 17  GLY B O   1 
ATOM   885  N N   . TYR B 1 19 ? 14.853  -22.499 -25.439 1.00 30.62  ? 18  TYR B N   1 
ATOM   886  C CA  . TYR B 1 19 ? 14.114  -21.333 -25.916 1.00 28.87  ? 18  TYR B CA  1 
ATOM   887  C C   . TYR B 1 19 ? 13.779  -21.491 -27.390 1.00 27.30  ? 18  TYR B C   1 
ATOM   888  O O   . TYR B 1 19 ? 14.520  -22.156 -28.103 1.00 28.21  ? 18  TYR B O   1 
ATOM   889  C CB  . TYR B 1 19 ? 15.000  -20.088 -25.860 1.00 29.07  ? 18  TYR B CB  1 
ATOM   890  C CG  . TYR B 1 19 ? 15.429  -19.824 -24.423 1.00 33.15  ? 18  TYR B CG  1 
ATOM   891  C CD1 . TYR B 1 19 ? 14.582  -19.156 -23.558 1.00 32.15  ? 18  TYR B CD1 1 
ATOM   892  C CD2 . TYR B 1 19 ? 16.596  -20.392 -23.907 1.00 30.28  ? 18  TYR B CD2 1 
ATOM   893  C CE1 . TYR B 1 19 ? 14.940  -18.969 -22.227 1.00 31.83  ? 18  TYR B CE1 1 
ATOM   894  C CE2 . TYR B 1 19 ? 16.972  -20.192 -22.585 1.00 34.84  ? 18  TYR B CE2 1 
ATOM   895  C CZ  . TYR B 1 19 ? 16.139  -19.470 -21.752 1.00 32.37  ? 18  TYR B CZ  1 
ATOM   896  O OH  . TYR B 1 19 ? 16.509  -19.293 -20.432 1.00 39.02  ? 18  TYR B OH  1 
ATOM   897  N N   . PRO B 1 20 ? 12.747  -20.793 -27.893 1.00 27.57  ? 19  PRO B N   1 
ATOM   898  C CA  . PRO B 1 20 ? 12.388  -20.831 -29.307 1.00 26.35  ? 19  PRO B CA  1 
ATOM   899  C C   . PRO B 1 20 ? 13.426  -20.063 -30.120 1.00 24.84  ? 19  PRO B C   1 
ATOM   900  O O   . PRO B 1 20 ? 14.102  -19.209 -29.577 1.00 25.74  ? 19  PRO B O   1 
ATOM   901  C CB  . PRO B 1 20 ? 11.054  -20.147 -29.412 1.00 28.76  ? 19  PRO B CB  1 
ATOM   902  C CG  . PRO B 1 20 ? 11.044  -19.220 -28.209 1.00 29.03  ? 19  PRO B CG  1 
ATOM   903  C CD  . PRO B 1 20 ? 11.810  -19.964 -27.117 1.00 25.40  ? 19  PRO B CD  1 
ATOM   904  N N   . HIS B 1 21 ? 13.579  -20.457 -31.400 1.00 25.57  ? 20  HIS B N   1 
ATOM   905  C CA  . HIS B 1 21 ? 14.432  -19.678 -32.316 1.00 25.50  ? 20  HIS B CA  1 
ATOM   906  C C   . HIS B 1 21 ? 14.189  -18.167 -32.132 1.00 25.14  ? 20  HIS B C   1 
ATOM   907  O O   . HIS B 1 21 ? 13.067  -17.722 -32.209 1.00 25.21  ? 20  HIS B O   1 
ATOM   908  C CB  . HIS B 1 21 ? 14.112  -20.157 -33.739 1.00 26.73  ? 20  HIS B CB  1 
ATOM   909  C CG  . HIS B 1 21 ? 14.354  -21.620 -33.960 1.00 27.75  ? 20  HIS B CG  1 
ATOM   910  N ND1 . HIS B 1 21 ? 13.477  -22.600 -33.496 1.00 27.72  ? 20  HIS B ND1 1 
ATOM   911  C CD2 . HIS B 1 21 ? 15.385  -22.251 -34.516 1.00 29.00  ? 20  HIS B CD2 1 
ATOM   912  C CE1 . HIS B 1 21 ? 13.970  -23.796 -33.820 1.00 29.74  ? 20  HIS B CE1 1 
ATOM   913  N NE2 . HIS B 1 21 ? 15.118  -23.617 -34.455 1.00 28.50  ? 20  HIS B NE2 1 
ATOM   914  N N   . TRP B 1 22 ? 15.259  -17.387 -31.944 1.00 24.17  ? 21  TRP B N   1 
ATOM   915  C CA  . TRP B 1 22 ? 15.025  -16.060 -31.363 1.00 23.15  ? 21  TRP B CA  1 
ATOM   916  C C   . TRP B 1 22 ? 15.538  -14.989 -32.312 1.00 24.35  ? 21  TRP B C   1 
ATOM   917  O O   . TRP B 1 22 ? 16.660  -15.121 -32.775 1.00 24.24  ? 21  TRP B O   1 
ATOM   918  C CB  . TRP B 1 22 ? 15.744  -15.996 -30.012 1.00 25.36  ? 21  TRP B CB  1 
ATOM   919  C CG  . TRP B 1 22 ? 15.263  -14.848 -29.160 1.00 24.40  ? 21  TRP B CG  1 
ATOM   920  C CD1 . TRP B 1 22 ? 15.540  -13.509 -29.280 1.00 24.95  ? 21  TRP B CD1 1 
ATOM   921  C CD2 . TRP B 1 22 ? 14.315  -14.961 -28.064 1.00 26.22  ? 21  TRP B CD2 1 
ATOM   922  N NE1 . TRP B 1 22 ? 14.838  -12.796 -28.315 1.00 26.43  ? 21  TRP B NE1 1 
ATOM   923  C CE2 . TRP B 1 22 ? 14.083  -13.665 -27.549 1.00 25.50  ? 21  TRP B CE2 1 
ATOM   924  C CE3 . TRP B 1 22 ? 13.667  -16.062 -27.477 1.00 28.33  ? 21  TRP B CE3 1 
ATOM   925  C CZ2 . TRP B 1 22 ? 13.209  -13.421 -26.468 1.00 27.25  ? 21  TRP B CZ2 1 
ATOM   926  C CZ3 . TRP B 1 22 ? 12.815  -15.825 -26.411 1.00 28.70  ? 21  TRP B CZ3 1 
ATOM   927  C CH2 . TRP B 1 22 ? 12.590  -14.525 -25.924 1.00 27.71  ? 21  TRP B CH2 1 
ATOM   928  N N   . PRO B 1 23 ? 14.798  -13.886 -32.577 1.00 24.70  ? 22  PRO B N   1 
ATOM   929  C CA  . PRO B 1 23 ? 15.299  -12.862 -33.523 1.00 21.97  ? 22  PRO B CA  1 
ATOM   930  C C   . PRO B 1 23 ? 16.598  -12.281 -32.968 1.00 25.23  ? 22  PRO B C   1 
ATOM   931  O O   . PRO B 1 23 ? 16.735  -11.923 -31.793 1.00 25.48  ? 22  PRO B O   1 
ATOM   932  C CB  . PRO B 1 23 ? 14.162  -11.788 -33.561 1.00 23.29  ? 22  PRO B CB  1 
ATOM   933  C CG  . PRO B 1 23 ? 13.422  -12.017 -32.229 1.00 24.51  ? 22  PRO B CG  1 
ATOM   934  C CD  . PRO B 1 23 ? 13.475  -13.551 -32.032 1.00 25.15  ? 22  PRO B CD  1 
ATOM   935  N N   . ALA B 1 24 ? 17.600  -12.132 -33.857 1.00 23.99  ? 23  ALA B N   1 
ATOM   936  C CA  . ALA B 1 24 ? 18.933  -11.782 -33.420 1.00 22.51  ? 23  ALA B CA  1 
ATOM   937  C C   . ALA B 1 24 ? 19.707  -11.223 -34.625 1.00 22.50  ? 23  ALA B C   1 
ATOM   938  O O   . ALA B 1 24 ? 19.219  -11.300 -35.739 1.00 24.78  ? 23  ALA B O   1 
ATOM   939  C CB  . ALA B 1 24 ? 19.670  -12.944 -32.745 1.00 24.93  ? 23  ALA B CB  1 
ATOM   940  N N   . ARG B 1 25 ? 20.893  -10.705 -34.296 1.00 25.21  ? 24  ARG B N   1 
ATOM   941  C CA  . ARG B 1 25 ? 21.808  -10.203 -35.333 1.00 24.45  ? 24  ARG B CA  1 
ATOM   942  C C   . ARG B 1 25 ? 23.216  -10.670 -35.006 1.00 25.45  ? 24  ARG B C   1 
ATOM   943  O O   . ARG B 1 25 ? 23.591  -10.901 -33.872 1.00 25.82  ? 24  ARG B O   1 
ATOM   944  C CB  . ARG B 1 25 ? 21.783  -8.672  -35.446 1.00 26.95  ? 24  ARG B CB  1 
ATOM   945  C CG  . ARG B 1 25 ? 22.415  -7.941  -34.269 1.00 26.46  ? 24  ARG B CG  1 
ATOM   946  C CD  . ARG B 1 25 ? 22.175  -6.439  -34.463 1.00 26.91  ? 24  ARG B CD  1 
ATOM   947  N NE  . ARG B 1 25 ? 22.818  -5.762  -33.344 1.00 28.65  ? 24  ARG B NE  1 
ATOM   948  C CZ  . ARG B 1 25 ? 22.509  -4.522  -32.940 1.00 28.71  ? 24  ARG B CZ  1 
ATOM   949  N NH1 . ARG B 1 25 ? 21.523  -3.897  -33.545 1.00 29.04  ? 24  ARG B NH1 1 
ATOM   950  N NH2 . ARG B 1 25 ? 23.156  -4.005  -31.899 1.00 28.02  ? 24  ARG B NH2 1 
ATOM   951  N N   . ILE B 1 26 ? 24.038  -10.788 -36.066 1.00 25.70  ? 25  ILE B N   1 
ATOM   952  C CA  . ILE B 1 26 ? 25.466  -10.940 -35.898 1.00 26.89  ? 25  ILE B CA  1 
ATOM   953  C C   . ILE B 1 26 ? 26.042  -9.569  -35.569 1.00 31.54  ? 25  ILE B C   1 
ATOM   954  O O   . ILE B 1 26 ? 25.794  -8.615  -36.295 1.00 32.42  ? 25  ILE B O   1 
ATOM   955  C CB  . ILE B 1 26 ? 26.087  -11.428 -37.234 1.00 32.19  ? 25  ILE B CB  1 
ATOM   956  C CG1 . ILE B 1 26 ? 25.353  -12.634 -37.821 1.00 33.32  ? 25  ILE B CG1 1 
ATOM   957  C CG2 . ILE B 1 26 ? 27.583  -11.679 -37.090 1.00 35.17  ? 25  ILE B CG2 1 
ATOM   958  C CD1 . ILE B 1 26 ? 25.436  -13.874 -36.950 1.00 33.92  ? 25  ILE B CD1 1 
ATOM   959  N N   . ASP B 1 27 ? 26.830  -9.546  -34.508 1.00 29.74  ? 26  ASP B N   1 
ATOM   960  C CA  . ASP B 1 27 ? 27.498  -8.306  -34.094 1.00 35.32  ? 26  ASP B CA  1 
ATOM   961  C C   . ASP B 1 27 ? 28.952  -8.282  -34.583 1.00 41.26  ? 26  ASP B C   1 
ATOM   962  O O   . ASP B 1 27 ? 29.467  -9.301  -35.030 1.00 43.98  ? 26  ASP B O   1 
ATOM   963  C CB  . ASP B 1 27 ? 27.445  -8.165  -32.588 1.00 32.72  ? 26  ASP B CB  1 
ATOM   964  C CG  . ASP B 1 27 ? 26.271  -7.397  -32.002 1.00 38.90  ? 26  ASP B CG  1 
ATOM   965  O OD1 . ASP B 1 27 ? 25.463  -6.831  -32.782 1.00 39.09  ? 26  ASP B OD1 1 
ATOM   966  O OD2 . ASP B 1 27 ? 26.189  -7.371  -30.740 1.00 39.39  ? 26  ASP B OD2 1 
ATOM   967  N N   A ASP B 1 28 ? 29.599  -7.110  -34.453 0.50 47.76  ? 27  ASP B N   1 
ATOM   968  N N   B ASP B 1 28 ? 29.608  -7.113  -34.481 0.50 45.91  ? 27  ASP B N   1 
ATOM   969  C CA  A ASP B 1 28 ? 31.011  -6.914  -34.760 0.50 55.61  ? 27  ASP B CA  1 
ATOM   970  C CA  B ASP B 1 28 ? 31.022  -6.973  -34.807 0.50 52.37  ? 27  ASP B CA  1 
ATOM   971  C C   A ASP B 1 28 ? 31.851  -7.364  -33.565 0.50 56.51  ? 27  ASP B C   1 
ATOM   972  C C   B ASP B 1 28 ? 31.838  -7.174  -33.529 0.50 54.88  ? 27  ASP B C   1 
ATOM   973  O O   A ASP B 1 28 ? 31.312  -7.866  -32.580 0.50 60.60  ? 27  ASP B O   1 
ATOM   974  O O   B ASP B 1 28 ? 31.266  -7.315  -32.449 0.50 58.45  ? 27  ASP B O   1 
ATOM   975  C CB  A ASP B 1 28 ? 31.313  -5.454  -35.068 0.50 53.13  ? 27  ASP B CB  1 
ATOM   976  C CB  B ASP B 1 28 ? 31.310  -5.629  -35.463 0.50 46.97  ? 27  ASP B CB  1 
ATOM   977  C CG  A ASP B 1 28 ? 30.160  -4.654  -35.655 0.50 52.40  ? 27  ASP B CG  1 
ATOM   978  C CG  B ASP B 1 28 ? 32.238  -5.666  -36.670 0.50 43.50  ? 27  ASP B CG  1 
ATOM   979  O OD1 A ASP B 1 28 ? 30.162  -4.438  -36.888 0.50 53.27  ? 27  ASP B OD1 1 
ATOM   980  O OD1 B ASP B 1 28 ? 33.193  -6.473  -36.659 0.50 45.37  ? 27  ASP B OD1 1 
ATOM   981  O OD2 A ASP B 1 28 ? 29.268  -4.257  -34.874 0.50 53.21  ? 27  ASP B OD2 1 
ATOM   982  O OD2 B ASP B 1 28 ? 32.015  -4.861  -37.601 0.50 43.25  ? 27  ASP B OD2 1 
ATOM   983  N N   . ILE B 1 29 ? 33.173  -7.170  -33.655 1.00 63.06  ? 28  ILE B N   1 
ATOM   984  C CA  . ILE B 1 29 ? 34.070  -7.434  -32.538 1.00 63.14  ? 28  ILE B CA  1 
ATOM   985  C C   . ILE B 1 29 ? 34.914  -6.177  -32.271 1.00 69.84  ? 28  ILE B C   1 
ATOM   986  O O   . ILE B 1 29 ? 34.313  -5.189  -31.795 1.00 70.76  ? 28  ILE B O   1 
ATOM   987  C CB  . ILE B 1 29 ? 34.945  -8.679  -32.793 1.00 63.39  ? 28  ILE B CB  1 
ATOM   988  N N   . LYS B 1 35 ? 36.944  -12.119 -27.612 1.00 69.03  ? 34  LYS B N   1 
ATOM   989  C CA  . LYS B 1 35 ? 36.784  -12.640 -29.003 1.00 67.53  ? 34  LYS B CA  1 
ATOM   990  C C   . LYS B 1 35 ? 36.046  -13.986 -28.979 1.00 63.41  ? 34  LYS B C   1 
ATOM   991  O O   . LYS B 1 35 ? 36.221  -14.777 -28.049 1.00 59.29  ? 34  LYS B O   1 
ATOM   992  C CB  . LYS B 1 35 ? 38.149  -12.670 -29.705 1.00 67.29  ? 34  LYS B CB  1 
ATOM   993  N N   . PRO B 1 36 ? 35.194  -14.312 -29.988 1.00 60.27  ? 35  PRO B N   1 
ATOM   994  C CA  . PRO B 1 36 ? 34.430  -15.569 -29.971 1.00 54.69  ? 35  PRO B CA  1 
ATOM   995  C C   . PRO B 1 36 ? 35.318  -16.807 -29.901 1.00 47.22  ? 35  PRO B C   1 
ATOM   996  O O   . PRO B 1 36 ? 36.432  -16.783 -30.402 1.00 56.53  ? 35  PRO B O   1 
ATOM   997  C CB  . PRO B 1 36 ? 33.627  -15.522 -31.285 1.00 50.90  ? 35  PRO B CB  1 
ATOM   998  C CG  . PRO B 1 36 ? 34.366  -14.525 -32.158 1.00 56.35  ? 35  PRO B CG  1 
ATOM   999  C CD  . PRO B 1 36 ? 34.924  -13.499 -31.186 1.00 54.02  ? 35  PRO B CD  1 
ATOM   1000 N N   . PRO B 1 37 ? 34.873  -17.930 -29.293 1.00 47.66  ? 36  PRO B N   1 
ATOM   1001 C CA  . PRO B 1 37 ? 35.614  -19.178 -29.427 1.00 47.50  ? 36  PRO B CA  1 
ATOM   1002 C C   . PRO B 1 37 ? 35.690  -19.523 -30.914 1.00 56.99  ? 36  PRO B C   1 
ATOM   1003 O O   . PRO B 1 37 ? 34.918  -18.995 -31.721 1.00 56.15  ? 36  PRO B O   1 
ATOM   1004 C CB  . PRO B 1 37 ? 34.790  -20.207 -28.616 1.00 49.10  ? 36  PRO B CB  1 
ATOM   1005 C CG  . PRO B 1 37 ? 33.894  -19.367 -27.710 1.00 48.24  ? 36  PRO B CG  1 
ATOM   1006 C CD  . PRO B 1 37 ? 33.675  -18.053 -28.446 1.00 50.68  ? 36  PRO B CD  1 
ATOM   1007 N N   . PRO B 1 38 ? 36.619  -20.415 -31.338 1.00 56.95  ? 37  PRO B N   1 
ATOM   1008 C CA  . PRO B 1 38 ? 36.689  -20.844 -32.743 1.00 56.97  ? 37  PRO B CA  1 
ATOM   1009 C C   . PRO B 1 38 ? 35.325  -21.234 -33.325 1.00 48.70  ? 37  PRO B C   1 
ATOM   1010 O O   . PRO B 1 38 ? 34.515  -21.866 -32.638 1.00 49.07  ? 37  PRO B O   1 
ATOM   1011 C CB  . PRO B 1 38 ? 37.649  -22.060 -32.639 1.00 56.41  ? 37  PRO B CB  1 
ATOM   1012 C CG  . PRO B 1 38 ? 38.578  -21.709 -31.488 1.00 54.28  ? 37  PRO B CG  1 
ATOM   1013 C CD  . PRO B 1 38 ? 37.639  -21.058 -30.483 1.00 63.55  ? 37  PRO B CD  1 
ATOM   1014 N N   . ASN B 1 39 ? 35.070  -20.846 -34.583 1.00 45.62  ? 38  ASN B N   1 
ATOM   1015 C CA  . ASN B 1 39 ? 33.878  -21.291 -35.310 1.00 51.32  ? 38  ASN B CA  1 
ATOM   1016 C C   . ASN B 1 39 ? 32.592  -20.572 -34.884 1.00 42.28  ? 38  ASN B C   1 
ATOM   1017 O O   . ASN B 1 39 ? 31.539  -20.848 -35.437 1.00 41.26  ? 38  ASN B O   1 
ATOM   1018 C CB  . ASN B 1 39 ? 33.587  -22.782 -35.116 1.00 48.82  ? 38  ASN B CB  1 
ATOM   1019 C CG  . ASN B 1 39 ? 34.756  -23.671 -35.485 1.00 60.50  ? 38  ASN B CG  1 
ATOM   1020 O OD1 . ASN B 1 39 ? 35.086  -24.602 -34.741 1.00 65.68  ? 38  ASN B OD1 1 
ATOM   1021 N ND2 . ASN B 1 39 ? 35.392  -23.411 -36.620 1.00 56.19  ? 38  ASN B ND2 1 
ATOM   1022 N N   . LYS B 1 40 ? 32.644  -19.666 -33.889 1.00 44.06  ? 39  LYS B N   1 
ATOM   1023 C CA  . LYS B 1 40 ? 31.425  -19.050 -33.365 1.00 37.68  ? 39  LYS B CA  1 
ATOM   1024 C C   . LYS B 1 40 ? 31.398  -17.557 -33.664 1.00 34.80  ? 39  LYS B C   1 
ATOM   1025 O O   . LYS B 1 40 ? 32.420  -16.974 -33.996 1.00 41.52  ? 39  LYS B O   1 
ATOM   1026 C CB  . LYS B 1 40 ? 31.361  -19.271 -31.856 1.00 41.37  ? 39  LYS B CB  1 
ATOM   1027 C CG  . LYS B 1 40 ? 31.167  -20.720 -31.459 1.00 41.31  ? 39  LYS B CG  1 
ATOM   1028 C CD  . LYS B 1 40 ? 31.202  -20.848 -29.942 1.00 53.79  ? 39  LYS B CD  1 
ATOM   1029 C CE  . LYS B 1 40 ? 30.276  -21.860 -29.349 1.00 61.53  ? 39  LYS B CE  1 
ATOM   1030 N NZ  . LYS B 1 40 ? 30.389  -23.157 -30.018 1.00 66.52  ? 39  LYS B NZ  1 
ATOM   1031 N N   . TYR B 1 41 ? 30.209  -16.957 -33.525 1.00 34.63  ? 40  TYR B N   1 
ATOM   1032 C CA  . TYR B 1 41 ? 29.949  -15.564 -33.861 1.00 33.23  ? 40  TYR B CA  1 
ATOM   1033 C C   . TYR B 1 41 ? 29.385  -14.864 -32.634 1.00 34.35  ? 40  TYR B C   1 
ATOM   1034 O O   . TYR B 1 41 ? 28.644  -15.457 -31.842 1.00 32.59  ? 40  TYR B O   1 
ATOM   1035 C CB  . TYR B 1 41 ? 28.886  -15.431 -34.955 1.00 33.30  ? 40  TYR B CB  1 
ATOM   1036 C CG  . TYR B 1 41 ? 29.350  -15.915 -36.323 1.00 33.83  ? 40  TYR B CG  1 
ATOM   1037 C CD1 . TYR B 1 41 ? 29.972  -15.055 -37.220 1.00 33.01  ? 40  TYR B CD1 1 
ATOM   1038 C CD2 . TYR B 1 41 ? 29.140  -17.235 -36.707 1.00 33.01  ? 40  TYR B CD2 1 
ATOM   1039 C CE1 . TYR B 1 41 ? 30.376  -15.500 -38.470 1.00 38.31  ? 40  TYR B CE1 1 
ATOM   1040 C CE2 . TYR B 1 41 ? 29.548  -17.697 -37.948 1.00 36.40  ? 40  TYR B CE2 1 
ATOM   1041 C CZ  . TYR B 1 41 ? 30.180  -16.823 -38.828 1.00 37.61  ? 40  TYR B CZ  1 
ATOM   1042 O OH  . TYR B 1 41 ? 30.541  -17.235 -40.087 1.00 35.35  ? 40  TYR B OH  1 
ATOM   1043 N N   . PRO B 1 42 ? 29.641  -13.546 -32.480 1.00 34.86  ? 41  PRO B N   1 
ATOM   1044 C CA  . PRO B 1 42 ? 28.938  -12.767 -31.460 1.00 32.80  ? 41  PRO B CA  1 
ATOM   1045 C C   . PRO B 1 42 ? 27.515  -12.473 -31.911 1.00 30.37  ? 41  PRO B C   1 
ATOM   1046 O O   . PRO B 1 42 ? 27.280  -11.867 -32.978 1.00 30.93  ? 41  PRO B O   1 
ATOM   1047 C CB  . PRO B 1 42 ? 29.765  -11.470 -31.302 1.00 32.76  ? 41  PRO B CB  1 
ATOM   1048 C CG  . PRO B 1 42 ? 30.665  -11.423 -32.520 1.00 35.56  ? 41  PRO B CG  1 
ATOM   1049 C CD  . PRO B 1 42 ? 30.577  -12.743 -33.286 1.00 35.93  ? 41  PRO B CD  1 
ATOM   1050 N N   . ILE B 1 43 ? 26.549  -12.955 -31.094 1.00 30.13  ? 42  ILE B N   1 
ATOM   1051 C CA  . ILE B 1 43 ? 25.124  -12.772 -31.362 1.00 29.38  ? 42  ILE B CA  1 
ATOM   1052 C C   . ILE B 1 43 ? 24.505  -11.747 -30.413 1.00 29.25  ? 42  ILE B C   1 
ATOM   1053 O O   . ILE B 1 43 ? 24.729  -11.852 -29.233 1.00 32.02  ? 42  ILE B O   1 
ATOM   1054 C CB  . ILE B 1 43 ? 24.419  -14.134 -31.222 1.00 27.74  ? 42  ILE B CB  1 
ATOM   1055 C CG1 . ILE B 1 43 ? 25.161  -15.174 -32.132 1.00 28.04  ? 42  ILE B CG1 1 
ATOM   1056 C CG2 . ILE B 1 43 ? 22.934  -13.978 -31.596 1.00 29.00  ? 42  ILE B CG2 1 
ATOM   1057 C CD1 . ILE B 1 43 ? 25.199  -14.811 -33.599 1.00 28.30  ? 42  ILE B CD1 1 
ATOM   1058 N N   . PHE B 1 44 ? 23.680  -10.861 -30.952 1.00 27.55  ? 43  PHE B N   1 
ATOM   1059 C CA  . PHE B 1 44 ? 22.891  -9.968  -30.109 1.00 29.98  ? 43  PHE B CA  1 
ATOM   1060 C C   . PHE B 1 44 ? 21.447  -10.394 -30.287 1.00 27.01  ? 43  PHE B C   1 
ATOM   1061 O O   . PHE B 1 44 ? 20.954  -10.437 -31.398 1.00 26.58  ? 43  PHE B O   1 
ATOM   1062 C CB  . PHE B 1 44 ? 23.102  -8.502  -30.523 1.00 28.24  ? 43  PHE B CB  1 
ATOM   1063 C CG  . PHE B 1 44 ? 22.142  -7.498  -29.883 1.00 28.79  ? 43  PHE B CG  1 
ATOM   1064 C CD1 . PHE B 1 44 ? 20.951  -7.149  -30.525 1.00 26.69  ? 43  PHE B CD1 1 
ATOM   1065 C CD2 . PHE B 1 44 ? 22.435  -6.898  -28.672 1.00 35.70  ? 43  PHE B CD2 1 
ATOM   1066 C CE1 . PHE B 1 44 ? 20.063  -6.222  -29.989 1.00 31.21  ? 43  PHE B CE1 1 
ATOM   1067 C CE2 . PHE B 1 44 ? 21.539  -5.974  -28.122 1.00 30.05  ? 43  PHE B CE2 1 
ATOM   1068 C CZ  . PHE B 1 44 ? 20.370  -5.648  -28.774 1.00 32.50  ? 43  PHE B CZ  1 
ATOM   1069 N N   . PHE B 1 45 ? 20.759  -10.697 -29.169 1.00 25.78  ? 44  PHE B N   1 
ATOM   1070 C CA  . PHE B 1 45 ? 19.365  -11.077 -29.177 1.00 25.16  ? 44  PHE B CA  1 
ATOM   1071 C C   . PHE B 1 45 ? 18.468  -9.873  -29.022 1.00 25.59  ? 44  PHE B C   1 
ATOM   1072 O O   . PHE B 1 45 ? 18.560  -9.122  -28.029 1.00 27.19  ? 44  PHE B O   1 
ATOM   1073 C CB  . PHE B 1 45 ? 19.131  -12.081 -28.030 1.00 23.80  ? 44  PHE B CB  1 
ATOM   1074 C CG  . PHE B 1 45 ? 19.825  -13.429 -28.180 1.00 25.66  ? 44  PHE B CG  1 
ATOM   1075 C CD1 . PHE B 1 45 ? 21.174  -13.585 -27.903 1.00 28.16  ? 44  PHE B CD1 1 
ATOM   1076 C CD2 . PHE B 1 45 ? 19.153  -14.512 -28.727 1.00 25.33  ? 44  PHE B CD2 1 
ATOM   1077 C CE1 . PHE B 1 45 ? 21.830  -14.788 -28.128 1.00 31.06  ? 44  PHE B CE1 1 
ATOM   1078 C CE2 . PHE B 1 45 ? 19.788  -15.738 -28.838 1.00 26.29  ? 44  PHE B CE2 1 
ATOM   1079 C CZ  . PHE B 1 45 ? 21.135  -15.877 -28.584 1.00 26.35  ? 44  PHE B CZ  1 
ATOM   1080 N N   . PHE B 1 46 ? 17.610  -9.680  -30.019 1.00 26.34  ? 45  PHE B N   1 
ATOM   1081 C CA  . PHE B 1 46 ? 16.669  -8.582  -29.973 1.00 25.44  ? 45  PHE B CA  1 
ATOM   1082 C C   . PHE B 1 46 ? 15.668  -8.790  -28.822 1.00 28.31  ? 45  PHE B C   1 
ATOM   1083 O O   . PHE B 1 46 ? 15.376  -9.914  -28.406 1.00 27.18  ? 45  PHE B O   1 
ATOM   1084 C CB  . PHE B 1 46 ? 15.894  -8.378  -31.270 1.00 25.21  ? 45  PHE B CB  1 
ATOM   1085 C CG  . PHE B 1 46 ? 16.823  -7.910  -32.380 1.00 25.59  ? 45  PHE B CG  1 
ATOM   1086 C CD1 . PHE B 1 46 ? 17.304  -6.596  -32.367 1.00 28.65  ? 45  PHE B CD1 1 
ATOM   1087 C CD2 . PHE B 1 46 ? 17.132  -8.761  -33.445 1.00 25.52  ? 45  PHE B CD2 1 
ATOM   1088 C CE1 . PHE B 1 46 ? 18.154  -6.176  -33.397 1.00 26.55  ? 45  PHE B CE1 1 
ATOM   1089 C CE2 . PHE B 1 46 ? 17.934  -8.323  -34.504 1.00 27.37  ? 45  PHE B CE2 1 
ATOM   1090 C CZ  . PHE B 1 46 ? 18.413  -7.008  -34.461 1.00 25.55  ? 45  PHE B CZ  1 
ATOM   1091 N N   . GLY B 1 47 ? 15.134  -7.686  -28.303 1.00 26.60  ? 46  GLY B N   1 
ATOM   1092 C CA  . GLY B 1 47 ? 14.148  -7.794  -27.220 1.00 27.74  ? 46  GLY B CA  1 
ATOM   1093 C C   . GLY B 1 47 ? 14.828  -7.888  -25.852 1.00 29.24  ? 46  GLY B C   1 
ATOM   1094 O O   . GLY B 1 47 ? 14.619  -7.021  -24.990 1.00 32.76  ? 46  GLY B O   1 
ATOM   1095 N N   . THR B 1 48 ? 15.621  -8.936  -25.607 1.00 29.42  ? 47  THR B N   1 
ATOM   1096 C CA  . THR B 1 48 ? 16.317  -9.144  -24.352 1.00 30.51  ? 47  THR B CA  1 
ATOM   1097 C C   . THR B 1 48 ? 17.545  -8.256  -24.300 1.00 32.19  ? 47  THR B C   1 
ATOM   1098 O O   . THR B 1 48 ? 18.052  -7.955  -23.211 1.00 33.94  ? 47  THR B O   1 
ATOM   1099 C CB  . THR B 1 48 ? 16.686  -10.614 -24.106 1.00 31.07  ? 47  THR B CB  1 
ATOM   1100 O OG1 . THR B 1 48 ? 17.676  -11.019 -25.072 1.00 29.65  ? 47  THR B OG1 1 
ATOM   1101 C CG2 . THR B 1 48 ? 15.458  -11.510 -24.209 1.00 29.28  ? 47  THR B CG2 1 
ATOM   1102 N N   . HIS B 1 49 ? 18.080  -7.964  -25.484 1.00 29.52  ? 48  HIS B N   1 
ATOM   1103 C CA  . HIS B 1 49 ? 19.316  -7.218  -25.669 1.00 33.15  ? 48  HIS B CA  1 
ATOM   1104 C C   . HIS B 1 49 ? 20.483  -7.907  -24.979 1.00 33.65  ? 48  HIS B C   1 
ATOM   1105 O O   . HIS B 1 49 ? 21.417  -7.227  -24.577 1.00 42.20  ? 48  HIS B O   1 
ATOM   1106 C CB  . HIS B 1 49 ? 19.202  -5.748  -25.239 1.00 31.04  ? 48  HIS B CB  1 
ATOM   1107 C CG  . HIS B 1 49 ? 17.952  -5.154  -25.736 1.00 31.96  ? 48  HIS B CG  1 
ATOM   1108 N ND1 . HIS B 1 49 ? 17.163  -4.378  -24.917 1.00 36.06  ? 48  HIS B ND1 1 
ATOM   1109 C CD2 . HIS B 1 49 ? 17.329  -5.181  -26.927 1.00 30.23  ? 48  HIS B CD2 1 
ATOM   1110 C CE1 . HIS B 1 49 ? 16.073  -4.005  -25.593 1.00 40.69  ? 48  HIS B CE1 1 
ATOM   1111 N NE2 . HIS B 1 49 ? 16.184  -4.450  -26.849 1.00 33.12  ? 48  HIS B NE2 1 
ATOM   1112 N N   . GLU B 1 50 ? 20.445  -9.238  -24.839 1.00 32.96  ? 49  GLU B N   1 
ATOM   1113 C CA  . GLU B 1 50 ? 21.597  -9.950  -24.299 1.00 31.60  ? 49  GLU B CA  1 
ATOM   1114 C C   . GLU B 1 50 ? 22.460  -10.490 -25.457 1.00 28.99  ? 49  GLU B C   1 
ATOM   1115 O O   . GLU B 1 50 ? 22.033  -10.453 -26.625 1.00 29.05  ? 49  GLU B O   1 
ATOM   1116 C CB  . GLU B 1 50 ? 21.204  -11.182 -23.479 1.00 36.89  ? 49  GLU B CB  1 
ATOM   1117 C CG  . GLU B 1 50 ? 20.305  -10.886 -22.275 1.00 41.26  ? 49  GLU B CG  1 
ATOM   1118 C CD  . GLU B 1 50 ? 20.990  -9.992  -21.243 1.00 55.91  ? 49  GLU B CD  1 
ATOM   1119 O OE1 . GLU B 1 50 ? 22.182  -10.258 -20.954 1.00 52.16  ? 49  GLU B OE1 1 
ATOM   1120 O OE2 . GLU B 1 50 ? 20.360  -9.027  -20.728 1.00 62.01  ? 49  GLU B OE2 1 
ATOM   1121 N N   . THR B 1 51 ? 23.611  -11.054 -25.098 1.00 32.48  ? 50  THR B N   1 
ATOM   1122 C CA  . THR B 1 51 ? 24.609  -11.495 -26.071 1.00 33.34  ? 50  THR B CA  1 
ATOM   1123 C C   . THR B 1 51 ? 25.095  -12.887 -25.709 1.00 35.00  ? 50  THR B C   1 
ATOM   1124 O O   . THR B 1 51 ? 25.014  -13.307 -24.560 1.00 39.89  ? 50  THR B O   1 
ATOM   1125 C CB  . THR B 1 51 ? 25.762  -10.501 -26.245 1.00 37.42  ? 50  THR B CB  1 
ATOM   1126 O OG1 . THR B 1 51 ? 26.258  -10.346 -24.922 1.00 39.28  ? 50  THR B OG1 1 
ATOM   1127 C CG2 . THR B 1 51 ? 25.291  -9.133  -26.708 1.00 35.42  ? 50  THR B CG2 1 
ATOM   1128 N N   . ALA B 1 52 ? 25.532  -13.644 -26.731 1.00 32.44  ? 51  ALA B N   1 
ATOM   1129 C CA  . ALA B 1 52 ? 26.196  -14.912 -26.531 1.00 34.26  ? 51  ALA B CA  1 
ATOM   1130 C C   . ALA B 1 52 ? 26.985  -15.226 -27.795 1.00 31.67  ? 51  ALA B C   1 
ATOM   1131 O O   . ALA B 1 52 ? 26.794  -14.556 -28.823 1.00 31.96  ? 51  ALA B O   1 
ATOM   1132 C CB  . ALA B 1 52 ? 25.209  -16.033 -26.208 1.00 33.03  ? 51  ALA B CB  1 
ATOM   1133 N N   . PHE B 1 53 ? 27.827  -16.260 -27.691 1.00 33.29  ? 52  PHE B N   1 
ATOM   1134 C CA  . PHE B 1 53 ? 28.542  -16.792 -28.841 1.00 35.07  ? 52  PHE B CA  1 
ATOM   1135 C C   . PHE B 1 53 ? 27.862  -18.083 -29.301 1.00 34.64  ? 52  PHE B C   1 
ATOM   1136 O O   . PHE B 1 53 ? 27.741  -19.044 -28.541 1.00 33.60  ? 52  PHE B O   1 
ATOM   1137 C CB  . PHE B 1 53 ? 30.010  -17.047 -28.482 1.00 33.02  ? 52  PHE B CB  1 
ATOM   1138 C CG  . PHE B 1 53 ? 30.815  -15.826 -28.070 1.00 39.18  ? 52  PHE B CG  1 
ATOM   1139 C CD1 . PHE B 1 53 ? 31.096  -14.819 -28.984 1.00 40.15  ? 52  PHE B CD1 1 
ATOM   1140 C CD2 . PHE B 1 53 ? 31.303  -15.712 -26.776 1.00 44.23  ? 52  PHE B CD2 1 
ATOM   1141 C CE1 . PHE B 1 53 ? 31.827  -13.697 -28.618 1.00 43.86  ? 52  PHE B CE1 1 
ATOM   1142 C CE2 . PHE B 1 53 ? 32.039  -14.588 -26.407 1.00 45.17  ? 52  PHE B CE2 1 
ATOM   1143 C CZ  . PHE B 1 53 ? 32.311  -13.601 -27.324 1.00 45.30  ? 52  PHE B CZ  1 
ATOM   1144 N N   . LEU B 1 54 ? 27.481  -18.130 -30.586 1.00 31.79  ? 53  LEU B N   1 
ATOM   1145 C CA  . LEU B 1 54 ? 26.865  -19.307 -31.178 1.00 27.88  ? 53  LEU B CA  1 
ATOM   1146 C C   . LEU B 1 54 ? 27.592  -19.663 -32.479 1.00 29.89  ? 53  LEU B C   1 
ATOM   1147 O O   . LEU B 1 54 ? 28.100  -18.783 -33.185 1.00 32.04  ? 53  LEU B O   1 
ATOM   1148 C CB  . LEU B 1 54 ? 25.378  -19.119 -31.501 1.00 29.59  ? 53  LEU B CB  1 
ATOM   1149 C CG  . LEU B 1 54 ? 24.399  -19.005 -30.329 1.00 29.34  ? 53  LEU B CG  1 
ATOM   1150 C CD1 . LEU B 1 54 ? 23.054  -18.713 -30.903 1.00 29.55  ? 53  LEU B CD1 1 
ATOM   1151 C CD2 . LEU B 1 54 ? 24.422  -20.344 -29.608 1.00 36.30  ? 53  LEU B CD2 1 
ATOM   1152 N N   . GLY B 1 55 ? 27.547  -20.951 -32.813 1.00 32.27  ? 54  GLY B N   1 
ATOM   1153 C CA  . GLY B 1 55 ? 28.068  -21.499 -34.060 1.00 30.93  ? 54  GLY B CA  1 
ATOM   1154 C C   . GLY B 1 55 ? 26.963  -21.542 -35.114 1.00 29.27  ? 54  GLY B C   1 
ATOM   1155 O O   . GLY B 1 55 ? 25.772  -21.437 -34.798 1.00 29.09  ? 54  GLY B O   1 
ATOM   1156 N N   . PRO B 1 56 ? 27.306  -21.720 -36.413 1.00 29.06  ? 55  PRO B N   1 
ATOM   1157 C CA  . PRO B 1 56 ? 26.310  -21.783 -37.474 1.00 28.66  ? 55  PRO B CA  1 
ATOM   1158 C C   . PRO B 1 56 ? 25.156  -22.773 -37.378 1.00 25.55  ? 55  PRO B C   1 
ATOM   1159 O O   . PRO B 1 56 ? 24.100  -22.526 -37.951 1.00 27.60  ? 55  PRO B O   1 
ATOM   1160 C CB  . PRO B 1 56 ? 27.148  -22.067 -38.744 1.00 31.52  ? 55  PRO B CB  1 
ATOM   1161 C CG  . PRO B 1 56 ? 28.579  -21.955 -38.357 1.00 34.04  ? 55  PRO B CG  1 
ATOM   1162 C CD  . PRO B 1 56 ? 28.704  -21.814 -36.883 1.00 30.42  ? 55  PRO B CD  1 
ATOM   1163 N N   . LYS B 1 57 ? 25.364  -23.894 -36.661 1.00 29.26  ? 56  LYS B N   1 
ATOM   1164 C CA  . LYS B 1 57 ? 24.285  -24.869 -36.544 1.00 27.63  ? 56  LYS B CA  1 
ATOM   1165 C C   . LYS B 1 57 ? 23.045  -24.259 -35.887 1.00 27.99  ? 56  LYS B C   1 
ATOM   1166 O O   . LYS B 1 57 ? 21.947  -24.749 -36.075 1.00 28.95  ? 56  LYS B O   1 
ATOM   1167 C CB  . LYS B 1 57 ? 24.717  -26.164 -35.831 1.00 32.37  ? 56  LYS B CB  1 
ATOM   1168 C CG  . LYS B 1 57 ? 24.814  -26.049 -34.317 1.00 37.47  ? 56  LYS B CG  1 
ATOM   1169 C CD  . LYS B 1 57 ? 24.834  -27.436 -33.665 1.00 44.05  ? 56  LYS B CD  1 
ATOM   1170 C CE  . LYS B 1 57 ? 25.182  -27.476 -32.194 1.00 48.34  ? 56  LYS B CE  1 
ATOM   1171 N NZ  . LYS B 1 57 ? 24.186  -26.843 -31.327 1.00 50.41  ? 56  LYS B NZ  1 
ATOM   1172 N N   . ASP B 1 58 ? 23.265  -23.158 -35.133 1.00 26.64  ? 57  ASP B N   1 
ATOM   1173 C CA  . ASP B 1 58 ? 22.220  -22.554 -34.323 1.00 28.13  ? 57  ASP B CA  1 
ATOM   1174 C C   . ASP B 1 58 ? 21.792  -21.211 -34.929 1.00 26.16  ? 57  ASP B C   1 
ATOM   1175 O O   . ASP B 1 58 ? 21.045  -20.467 -34.284 1.00 27.04  ? 57  ASP B O   1 
ATOM   1176 C CB  . ASP B 1 58 ? 22.740  -22.414 -32.904 1.00 29.13  ? 57  ASP B CB  1 
ATOM   1177 C CG  . ASP B 1 58 ? 22.851  -23.729 -32.131 1.00 33.62  ? 57  ASP B CG  1 
ATOM   1178 O OD1 . ASP B 1 58 ? 21.923  -24.571 -32.278 1.00 33.11  ? 57  ASP B OD1 1 
ATOM   1179 O OD2 . ASP B 1 58 ? 23.834  -23.862 -31.361 1.00 38.17  ? 57  ASP B OD2 1 
ATOM   1180 N N   . LEU B 1 59 ? 22.251  -20.888 -36.163 1.00 24.79  ? 58  LEU B N   1 
ATOM   1181 C CA  . LEU B 1 59 ? 21.950  -19.595 -36.770 1.00 24.54  ? 58  LEU B CA  1 
ATOM   1182 C C   . LEU B 1 59 ? 21.194  -19.811 -38.068 1.00 25.81  ? 58  LEU B C   1 
ATOM   1183 O O   . LEU B 1 59 ? 21.683  -20.494 -38.986 1.00 27.50  ? 58  LEU B O   1 
ATOM   1184 C CB  . LEU B 1 59 ? 23.272  -18.864 -36.983 1.00 26.94  ? 58  LEU B CB  1 
ATOM   1185 C CG  . LEU B 1 59 ? 24.129  -18.589 -35.751 1.00 26.80  ? 58  LEU B CG  1 
ATOM   1186 C CD1 . LEU B 1 59 ? 25.398  -17.842 -36.135 1.00 29.47  ? 58  LEU B CD1 1 
ATOM   1187 C CD2 . LEU B 1 59 ? 23.302  -17.737 -34.757 1.00 28.09  ? 58  LEU B CD2 1 
ATOM   1188 N N   . PHE B 1 60 ? 20.020  -19.224 -38.151 1.00 23.54  ? 59  PHE B N   1 
ATOM   1189 C CA  . PHE B 1 60 ? 19.089  -19.400 -39.248 1.00 24.31  ? 59  PHE B CA  1 
ATOM   1190 C C   . PHE B 1 60 ? 18.883  -18.052 -39.942 1.00 25.86  ? 59  PHE B C   1 
ATOM   1191 O O   . PHE B 1 60 ? 18.298  -17.149 -39.355 1.00 26.34  ? 59  PHE B O   1 
ATOM   1192 C CB  . PHE B 1 60 ? 17.773  -19.971 -38.699 1.00 24.53  ? 59  PHE B CB  1 
ATOM   1193 C CG  . PHE B 1 60 ? 17.882  -21.365 -38.082 1.00 24.36  ? 59  PHE B CG  1 
ATOM   1194 C CD1 . PHE B 1 60 ? 18.464  -21.533 -36.825 1.00 25.61  ? 59  PHE B CD1 1 
ATOM   1195 C CD2 . PHE B 1 60 ? 17.466  -22.464 -38.811 1.00 27.13  ? 59  PHE B CD2 1 
ATOM   1196 C CE1 . PHE B 1 60 ? 18.599  -22.810 -36.274 1.00 27.97  ? 59  PHE B CE1 1 
ATOM   1197 C CE2 . PHE B 1 60 ? 17.537  -23.733 -38.225 1.00 27.13  ? 59  PHE B CE2 1 
ATOM   1198 C CZ  . PHE B 1 60 ? 18.170  -23.901 -37.009 1.00 29.20  ? 59  PHE B CZ  1 
ATOM   1199 N N   . PRO B 1 61 ? 19.334  -17.849 -41.201 1.00 26.73  ? 60  PRO B N   1 
ATOM   1200 C CA  . PRO B 1 61 ? 19.118  -16.543 -41.861 1.00 27.78  ? 60  PRO B CA  1 
ATOM   1201 C C   . PRO B 1 61 ? 17.670  -16.078 -41.815 1.00 26.51  ? 60  PRO B C   1 
ATOM   1202 O O   . PRO B 1 61 ? 16.742  -16.844 -42.023 1.00 29.41  ? 60  PRO B O   1 
ATOM   1203 C CB  . PRO B 1 61 ? 19.626  -16.842 -43.302 1.00 29.49  ? 60  PRO B CB  1 
ATOM   1204 C CG  . PRO B 1 61 ? 20.688  -17.888 -43.111 1.00 37.45  ? 60  PRO B CG  1 
ATOM   1205 C CD  . PRO B 1 61 ? 20.113  -18.811 -42.012 1.00 30.61  ? 60  PRO B CD  1 
ATOM   1206 N N   . TYR B 1 62 ? 17.470  -14.761 -41.496 1.00 27.61  ? 61  TYR B N   1 
ATOM   1207 C CA  . TYR B 1 62 ? 16.167  -14.294 -41.101 1.00 29.69  ? 61  TYR B CA  1 
ATOM   1208 C C   . TYR B 1 62 ? 15.184  -14.328 -42.251 1.00 29.97  ? 61  TYR B C   1 
ATOM   1209 O O   . TYR B 1 62 ? 14.039  -14.734 -42.051 1.00 33.03  ? 61  TYR B O   1 
ATOM   1210 C CB  . TYR B 1 62 ? 16.352  -12.839 -40.632 1.00 33.42  ? 61  TYR B CB  1 
ATOM   1211 C CG  . TYR B 1 62 ? 15.033  -12.128 -40.379 1.00 31.71  ? 61  TYR B CG  1 
ATOM   1212 C CD1 . TYR B 1 62 ? 14.289  -12.385 -39.245 1.00 32.93  ? 61  TYR B CD1 1 
ATOM   1213 C CD2 . TYR B 1 62 ? 14.602  -11.107 -41.233 1.00 37.66  ? 61  TYR B CD2 1 
ATOM   1214 C CE1 . TYR B 1 62 ? 13.086  -11.732 -39.014 1.00 34.93  ? 61  TYR B CE1 1 
ATOM   1215 C CE2 . TYR B 1 62 ? 13.430  -10.403 -40.986 1.00 42.43  ? 61  TYR B CE2 1 
ATOM   1216 C CZ  . TYR B 1 62 ? 12.664  -10.735 -39.880 1.00 39.35  ? 61  TYR B CZ  1 
ATOM   1217 O OH  . TYR B 1 62 ? 11.507  -10.066 -39.650 1.00 40.74  ? 61  TYR B OH  1 
ATOM   1218 N N   . ASP B 1 63 ? 15.646  -13.870 -43.443 1.00 35.18  ? 62  ASP B N   1 
ATOM   1219 C CA  . ASP B 1 63 ? 14.835  -13.890 -44.662 1.00 40.81  ? 62  ASP B CA  1 
ATOM   1220 C C   . ASP B 1 63 ? 14.260  -15.280 -44.938 1.00 32.21  ? 62  ASP B C   1 
ATOM   1221 O O   . ASP B 1 63 ? 13.050  -15.434 -45.074 1.00 42.18  ? 62  ASP B O   1 
ATOM   1222 C CB  . ASP B 1 63 ? 15.579  -13.311 -45.854 1.00 48.36  ? 62  ASP B CB  1 
ATOM   1223 C CG  . ASP B 1 63 ? 15.376  -11.821 -46.076 1.00 64.56  ? 62  ASP B CG  1 
ATOM   1224 O OD1 . ASP B 1 63 ? 14.682  -11.187 -45.240 1.00 68.07  ? 62  ASP B OD1 1 
ATOM   1225 O OD2 . ASP B 1 63 ? 15.896  -11.312 -47.095 1.00 71.62  ? 62  ASP B OD2 1 
ATOM   1226 N N   . LYS B 1 64 ? 15.138  -16.273 -45.032 1.00 36.84  ? 63  LYS B N   1 
ATOM   1227 C CA  . LYS B 1 64 ? 14.716  -17.644 -45.271 1.00 37.58  ? 63  LYS B CA  1 
ATOM   1228 C C   . LYS B 1 64 ? 13.724  -18.115 -44.209 1.00 37.47  ? 63  LYS B C   1 
ATOM   1229 O O   . LYS B 1 64 ? 12.748  -18.792 -44.529 1.00 40.04  ? 63  LYS B O   1 
ATOM   1230 C CB  . LYS B 1 64 ? 15.916  -18.590 -45.294 1.00 42.88  ? 63  LYS B CB  1 
ATOM   1231 C CG  . LYS B 1 64 ? 15.587  -19.990 -45.800 1.00 41.05  ? 63  LYS B CG  1 
ATOM   1232 C CD  . LYS B 1 64 ? 16.803  -20.870 -45.562 1.00 48.06  ? 63  LYS B CD  1 
ATOM   1233 C CE  . LYS B 1 64 ? 16.734  -22.287 -46.116 1.00 45.93  ? 63  LYS B CE  1 
ATOM   1234 N NZ  . LYS B 1 64 ? 15.390  -22.848 -46.244 1.00 49.55  ? 63  LYS B NZ  1 
ATOM   1235 N N   . SER B 1 65 ? 13.939  -17.717 -42.947 1.00 34.69  ? 64  SER B N   1 
ATOM   1236 C CA  . SER B 1 65 ? 13.272  -18.452 -41.866 1.00 35.99  ? 64  SER B CA  1 
ATOM   1237 C C   . SER B 1 65 ? 12.151  -17.681 -41.149 1.00 34.87  ? 64  SER B C   1 
ATOM   1238 O O   . SER B 1 65 ? 11.486  -18.231 -40.280 1.00 35.99  ? 64  SER B O   1 
ATOM   1239 C CB  . SER B 1 65 ? 14.301  -19.025 -40.946 1.00 39.76  ? 64  SER B CB  1 
ATOM   1240 O OG  . SER B 1 65 ? 15.057  -17.993 -40.337 1.00 49.95  ? 64  SER B OG  1 
ATOM   1241 N N   . LYS B 1 66 ? 11.831  -16.451 -41.581 1.00 36.40  ? 65  LYS B N   1 
ATOM   1242 C CA  . LYS B 1 66 ? 10.931  -15.606 -40.803 1.00 35.25  ? 65  LYS B CA  1 
ATOM   1243 C C   . LYS B 1 66 ? 9.490   -16.123 -40.764 1.00 37.32  ? 65  LYS B C   1 
ATOM   1244 O O   . LYS B 1 66 ? 8.782   -15.924 -39.774 1.00 38.20  ? 65  LYS B O   1 
ATOM   1245 C CB  . LYS B 1 66 ? 10.973  -14.133 -41.227 1.00 35.67  ? 65  LYS B CB  1 
ATOM   1246 C CG  . LYS B 1 66 ? 10.427  -13.878 -42.628 1.00 37.07  ? 65  LYS B CG  1 
ATOM   1247 N N   . ASP B 1 67 ? 9.011   -16.776 -41.823 1.00 37.13  ? 66  ASP B N   1 
ATOM   1248 C CA  . ASP B 1 67 ? 7.600   -17.130 -41.737 1.00 44.57  ? 66  ASP B CA  1 
ATOM   1249 C C   . ASP B 1 67 ? 7.422   -18.336 -40.811 1.00 43.92  ? 66  ASP B C   1 
ATOM   1250 O O   . ASP B 1 67 ? 6.359   -18.503 -40.198 1.00 47.24  ? 66  ASP B O   1 
ATOM   1251 C CB  . ASP B 1 67 ? 6.901   -17.114 -43.089 1.00 61.11  ? 66  ASP B CB  1 
ATOM   1252 C CG  . ASP B 1 67 ? 7.650   -17.803 -44.215 1.00 74.33  ? 66  ASP B CG  1 
ATOM   1253 O OD1 . ASP B 1 67 ? 7.286   -17.583 -45.392 1.00 84.94  ? 66  ASP B OD1 1 
ATOM   1254 O OD2 . ASP B 1 67 ? 8.597   -18.549 -43.899 1.00 77.46  ? 66  ASP B OD2 1 
ATOM   1255 N N   . LYS B 1 68 ? 8.494   -19.128 -40.673 1.00 42.47  ? 67  LYS B N   1 
ATOM   1256 C CA  . LYS B 1 68 ? 8.499   -20.285 -39.795 1.00 36.22  ? 67  LYS B CA  1 
ATOM   1257 C C   . LYS B 1 68 ? 8.690   -19.893 -38.329 1.00 38.11  ? 67  LYS B C   1 
ATOM   1258 O O   . LYS B 1 68 ? 7.933   -20.371 -37.487 1.00 36.75  ? 67  LYS B O   1 
ATOM   1259 C CB  . LYS B 1 68 ? 9.574   -21.282 -40.221 1.00 38.74  ? 67  LYS B CB  1 
ATOM   1260 C CG  . LYS B 1 68 ? 9.701   -22.547 -39.399 1.00 44.37  ? 67  LYS B CG  1 
ATOM   1261 C CD  . LYS B 1 68 ? 10.746  -23.414 -40.104 1.00 51.33  ? 67  LYS B CD  1 
ATOM   1262 C CE  . LYS B 1 68 ? 11.109  -24.703 -39.429 1.00 55.32  ? 67  LYS B CE  1 
ATOM   1263 N NZ  . LYS B 1 68 ? 9.961   -25.594 -39.243 1.00 50.44  ? 67  LYS B NZ  1 
ATOM   1264 N N   . TYR B 1 69 ? 9.665   -19.013 -38.034 1.00 31.14  ? 68  TYR B N   1 
ATOM   1265 C CA  . TYR B 1 69 ? 10.090  -18.750 -36.657 1.00 27.24  ? 68  TYR B CA  1 
ATOM   1266 C C   . TYR B 1 69 ? 9.621   -17.386 -36.145 1.00 30.62  ? 68  TYR B C   1 
ATOM   1267 O O   . TYR B 1 69 ? 9.820   -17.100 -34.960 1.00 32.33  ? 68  TYR B O   1 
ATOM   1268 C CB  . TYR B 1 69 ? 11.613  -18.830 -36.525 1.00 26.97  ? 68  TYR B CB  1 
ATOM   1269 C CG  . TYR B 1 69 ? 12.239  -20.183 -36.809 1.00 30.29  ? 68  TYR B CG  1 
ATOM   1270 C CD1 . TYR B 1 69 ? 11.684  -21.341 -36.278 1.00 29.82  ? 68  TYR B CD1 1 
ATOM   1271 C CD2 . TYR B 1 69 ? 13.347  -20.309 -37.636 1.00 32.00  ? 68  TYR B CD2 1 
ATOM   1272 C CE1 . TYR B 1 69 ? 12.220  -22.591 -36.561 1.00 31.13  ? 68  TYR B CE1 1 
ATOM   1273 C CE2 . TYR B 1 69 ? 13.889  -21.549 -37.942 1.00 33.12  ? 68  TYR B CE2 1 
ATOM   1274 C CZ  . TYR B 1 69 ? 13.345  -22.690 -37.367 1.00 34.83  ? 68  TYR B CZ  1 
ATOM   1275 O OH  . TYR B 1 69 ? 13.886  -23.905 -37.681 1.00 34.82  ? 68  TYR B OH  1 
ATOM   1276 N N   . GLY B 1 70 ? 9.085   -16.517 -37.020 1.00 34.20  ? 69  GLY B N   1 
ATOM   1277 C CA  . GLY B 1 70 ? 8.799   -15.133 -36.650 1.00 35.85  ? 69  GLY B CA  1 
ATOM   1278 C C   . GLY B 1 70 ? 7.355   -14.922 -36.176 1.00 38.32  ? 69  GLY B C   1 
ATOM   1279 O O   . GLY B 1 70 ? 6.752   -13.891 -36.451 1.00 40.87  ? 69  GLY B O   1 
ATOM   1280 N N   . LYS B 1 71 ? 6.803   -15.898 -35.451 1.00 39.39  ? 70  LYS B N   1 
ATOM   1281 C CA  . LYS B 1 71 ? 5.452   -15.771 -34.942 1.00 40.61  ? 70  LYS B CA  1 
ATOM   1282 C C   . LYS B 1 71 ? 5.545   -15.323 -33.496 1.00 43.54  ? 70  LYS B C   1 
ATOM   1283 O O   . LYS B 1 71 ? 6.437   -15.781 -32.778 1.00 38.52  ? 70  LYS B O   1 
ATOM   1284 C CB  . LYS B 1 71 ? 4.734   -17.123 -34.832 1.00 42.20  ? 70  LYS B CB  1 
ATOM   1285 C CG  . LYS B 1 71 ? 3.825   -17.500 -35.995 1.00 57.79  ? 70  LYS B CG  1 
ATOM   1286 C CD  . LYS B 1 71 ? 4.564   -17.719 -37.307 1.00 55.58  ? 70  LYS B CD  1 
ATOM   1287 C CE  . LYS B 1 71 ? 3.617   -18.028 -38.435 1.00 64.67  ? 70  LYS B CE  1 
ATOM   1288 N NZ  . LYS B 1 71 ? 4.159   -17.539 -39.707 1.00 64.42  ? 70  LYS B NZ  1 
ATOM   1289 N N   . PRO B 1 72 ? 4.622   -14.448 -33.033 1.00 44.73  ? 71  PRO B N   1 
ATOM   1290 C CA  . PRO B 1 72 ? 4.589   -14.057 -31.621 1.00 43.90  ? 71  PRO B CA  1 
ATOM   1291 C C   . PRO B 1 72 ? 4.387   -15.236 -30.670 1.00 38.02  ? 71  PRO B C   1 
ATOM   1292 O O   . PRO B 1 72 ? 3.771   -16.249 -31.021 1.00 38.31  ? 71  PRO B O   1 
ATOM   1293 C CB  . PRO B 1 72 ? 3.471   -13.012 -31.525 1.00 42.46  ? 71  PRO B CB  1 
ATOM   1294 C CG  . PRO B 1 72 ? 3.304   -12.537 -32.954 1.00 45.27  ? 71  PRO B CG  1 
ATOM   1295 C CD  . PRO B 1 72 ? 3.641   -13.731 -33.855 1.00 39.67  ? 71  PRO B CD  1 
ATOM   1296 N N   . ASN B 1 73 ? 4.973   -15.115 -29.472 1.00 38.17  ? 72  ASN B N   1 
ATOM   1297 C CA  . ASN B 1 73 ? 4.760   -16.102 -28.426 1.00 34.64  ? 72  ASN B CA  1 
ATOM   1298 C C   . ASN B 1 73 ? 4.668   -15.367 -27.082 1.00 37.19  ? 72  ASN B C   1 
ATOM   1299 O O   . ASN B 1 73 ? 4.679   -14.124 -27.033 1.00 44.35  ? 72  ASN B O   1 
ATOM   1300 C CB  . ASN B 1 73 ? 5.797   -17.230 -28.460 1.00 38.49  ? 72  ASN B CB  1 
ATOM   1301 C CG  . ASN B 1 73 ? 7.215   -16.795 -28.155 1.00 34.49  ? 72  ASN B CG  1 
ATOM   1302 O OD1 . ASN B 1 73 ? 7.467   -16.063 -27.184 1.00 33.81  ? 72  ASN B OD1 1 
ATOM   1303 N ND2 . ASN B 1 73 ? 8.179   -17.231 -28.960 1.00 32.80  ? 72  ASN B ND2 1 
ATOM   1304 N N   . LYS B 1 74 ? 4.633   -16.130 -25.983 1.00 40.57  ? 73  LYS B N   1 
ATOM   1305 C CA  . LYS B 1 74 ? 4.506   -15.508 -24.662 1.00 44.45  ? 73  LYS B CA  1 
ATOM   1306 C C   . LYS B 1 74 ? 5.824   -15.483 -23.863 1.00 43.85  ? 73  LYS B C   1 
ATOM   1307 O O   . LYS B 1 74 ? 5.795   -15.257 -22.647 1.00 40.10  ? 73  LYS B O   1 
ATOM   1308 C CB  . LYS B 1 74 ? 3.346   -16.145 -23.877 1.00 42.14  ? 73  LYS B CB  1 
ATOM   1309 N N   . ARG B 1 75 ? 6.981   -15.730 -24.509 1.00 33.19  ? 74  ARG B N   1 
ATOM   1310 C CA  . ARG B 1 75 ? 8.272   -15.603 -23.841 1.00 32.06  ? 74  ARG B CA  1 
ATOM   1311 C C   . ARG B 1 75 ? 8.641   -14.116 -23.691 1.00 33.20  ? 74  ARG B C   1 
ATOM   1312 O O   . ARG B 1 75 ? 8.505   -13.311 -24.611 1.00 32.98  ? 74  ARG B O   1 
ATOM   1313 C CB  . ARG B 1 75 ? 9.396   -16.394 -24.526 1.00 32.57  ? 74  ARG B CB  1 
ATOM   1314 C CG  . ARG B 1 75 ? 9.235   -17.894 -24.781 1.00 32.11  ? 74  ARG B CG  1 
ATOM   1315 C CD  . ARG B 1 75 ? 9.199   -18.667 -23.477 1.00 34.70  ? 74  ARG B CD  1 
ATOM   1316 N NE  . ARG B 1 75 ? 9.414   -20.104 -23.708 1.00 31.07  ? 74  ARG B NE  1 
ATOM   1317 C CZ  . ARG B 1 75 ? 10.523  -20.755 -23.454 1.00 34.07  ? 74  ARG B CZ  1 
ATOM   1318 N NH1 . ARG B 1 75 ? 11.542  -20.155 -22.863 1.00 39.85  ? 74  ARG B NH1 1 
ATOM   1319 N NH2 . ARG B 1 75 ? 10.619  -22.036 -23.792 1.00 40.65  ? 74  ARG B NH2 1 
ATOM   1320 N N   . LYS B 1 76 ? 9.043   -13.706 -22.485 1.00 30.20  ? 75  LYS B N   1 
ATOM   1321 C CA  . LYS B 1 76 ? 9.510   -12.355 -22.207 1.00 28.71  ? 75  LYS B CA  1 
ATOM   1322 C C   . LYS B 1 76 ? 10.644  -11.897 -23.157 1.00 27.90  ? 75  LYS B C   1 
ATOM   1323 O O   . LYS B 1 76 ? 11.724  -12.524 -23.197 1.00 28.52  ? 75  LYS B O   1 
ATOM   1324 C CB  . LYS B 1 76 ? 10.037  -12.353 -20.754 1.00 30.53  ? 75  LYS B CB  1 
ATOM   1325 C CG  . LYS B 1 76 ? 10.350  -10.929 -20.277 1.00 32.39  ? 75  LYS B CG  1 
ATOM   1326 C CD  . LYS B 1 76 ? 10.851  -10.835 -18.836 1.00 34.23  ? 75  LYS B CD  1 
ATOM   1327 C CE  . LYS B 1 76 ? 11.312  -9.451  -18.473 1.00 37.62  ? 75  LYS B CE  1 
ATOM   1328 N NZ  . LYS B 1 76 ? 11.562  -9.363  -17.023 1.00 44.63  ? 75  LYS B NZ  1 
ATOM   1329 N N   . GLY B 1 77 ? 10.328  -10.792 -23.847 1.00 28.08  ? 76  GLY B N   1 
ATOM   1330 C CA  . GLY B 1 77 ? 11.260  -10.122 -24.768 1.00 27.31  ? 76  GLY B CA  1 
ATOM   1331 C C   . GLY B 1 77 ? 11.052  -10.556 -26.217 1.00 30.49  ? 76  GLY B C   1 
ATOM   1332 O O   . GLY B 1 77 ? 11.550  -9.934  -27.149 1.00 28.02  ? 76  GLY B O   1 
ATOM   1333 N N   . PHE B 1 78 ? 10.361  -11.660 -26.438 1.00 26.82  ? 77  PHE B N   1 
ATOM   1334 C CA  . PHE B 1 78 ? 10.174  -12.152 -27.816 1.00 26.52  ? 77  PHE B CA  1 
ATOM   1335 C C   . PHE B 1 78 ? 9.441   -11.169 -28.744 1.00 28.98  ? 77  PHE B C   1 
ATOM   1336 O O   . PHE B 1 78 ? 9.895   -10.876 -29.872 1.00 28.31  ? 77  PHE B O   1 
ATOM   1337 C CB  . PHE B 1 78 ? 9.459   -13.496 -27.837 1.00 27.43  ? 77  PHE B CB  1 
ATOM   1338 C CG  . PHE B 1 78 ? 9.706   -14.196 -29.159 1.00 26.14  ? 77  PHE B CG  1 
ATOM   1339 C CD1 . PHE B 1 78 ? 10.805  -15.035 -29.292 1.00 25.33  ? 77  PHE B CD1 1 
ATOM   1340 C CD2 . PHE B 1 78 ? 8.796   -14.049 -30.203 1.00 29.74  ? 77  PHE B CD2 1 
ATOM   1341 C CE1 . PHE B 1 78 ? 11.032  -15.678 -30.522 1.00 25.96  ? 77  PHE B CE1 1 
ATOM   1342 C CE2 . PHE B 1 78 ? 9.031   -14.714 -31.419 1.00 30.11  ? 77  PHE B CE2 1 
ATOM   1343 C CZ  . PHE B 1 78 ? 10.122  -15.560 -31.533 1.00 28.56  ? 77  PHE B CZ  1 
ATOM   1344 N N   . ASN B 1 79 ? 8.244   -10.681 -28.408 1.00 29.02  ? 78  ASN B N   1 
ATOM   1345 C CA  . ASN B 1 79 ? 7.517   -9.808  -29.319 1.00 30.69  ? 78  ASN B CA  1 
ATOM   1346 C C   . ASN B 1 79 ? 8.242   -8.457  -29.479 1.00 29.67  ? 78  ASN B C   1 
ATOM   1347 O O   . ASN B 1 79 ? 8.221   -7.894  -30.576 1.00 30.83  ? 78  ASN B O   1 
ATOM   1348 C CB  . ASN B 1 79 ? 6.035   -9.698  -28.943 1.00 34.38  ? 78  ASN B CB  1 
ATOM   1349 C CG  . ASN B 1 79 ? 5.323   -11.034 -28.950 1.00 39.42  ? 78  ASN B CG  1 
ATOM   1350 O OD1 . ASN B 1 79 ? 5.846   -12.038 -29.451 1.00 36.10  ? 78  ASN B OD1 1 
ATOM   1351 N ND2 . ASN B 1 79 ? 4.142   -11.087 -28.348 1.00 40.00  ? 78  ASN B ND2 1 
ATOM   1352 N N   . GLU B 1 80 ? 8.927   -7.992  -28.432 1.00 29.64  ? 79  GLU B N   1 
ATOM   1353 C CA  . GLU B 1 80 ? 9.732   -6.777  -28.551 1.00 31.68  ? 79  GLU B CA  1 
ATOM   1354 C C   . GLU B 1 80 ? 10.841  -7.030  -29.577 1.00 29.35  ? 79  GLU B C   1 
ATOM   1355 O O   . GLU B 1 80 ? 11.102  -6.171  -30.439 1.00 28.55  ? 79  GLU B O   1 
ATOM   1356 C CB  . GLU B 1 80 ? 10.322  -6.295  -27.228 1.00 30.46  ? 79  GLU B CB  1 
ATOM   1357 C CG  . GLU B 1 80 ? 9.256   -5.776  -26.262 1.00 40.66  ? 79  GLU B CG  1 
ATOM   1358 N N   . GLY B 1 81 ? 11.435  -8.234  -29.488 1.00 27.52  ? 80  GLY B N   1 
ATOM   1359 C CA  . GLY B 1 81 ? 12.524  -8.632  -30.393 1.00 28.06  ? 80  GLY B CA  1 
ATOM   1360 C C   . GLY B 1 81 ? 12.049  -8.720  -31.836 1.00 28.23  ? 80  GLY B C   1 
ATOM   1361 O O   . GLY B 1 81 ? 12.805  -8.313  -32.732 1.00 26.29  ? 80  GLY B O   1 
ATOM   1362 N N   . LEU B 1 82 ? 10.822  -9.185  -32.071 1.00 27.46  ? 81  LEU B N   1 
ATOM   1363 C CA  . LEU B 1 82 ? 10.225  -9.209  -33.392 1.00 29.13  ? 81  LEU B CA  1 
ATOM   1364 C C   . LEU B 1 82 ? 10.088  -7.783  -33.913 1.00 28.71  ? 81  LEU B C   1 
ATOM   1365 O O   . LEU B 1 82 ? 10.303  -7.548  -35.110 1.00 30.35  ? 81  LEU B O   1 
ATOM   1366 C CB  . LEU B 1 82 ? 8.884   -9.955  -33.433 1.00 31.39  ? 81  LEU B CB  1 
ATOM   1367 C CG  . LEU B 1 82 ? 8.959   -11.475 -33.253 1.00 28.16  ? 81  LEU B CG  1 
ATOM   1368 C CD1 . LEU B 1 82 ? 7.521   -12.052 -33.282 1.00 30.77  ? 81  LEU B CD1 1 
ATOM   1369 C CD2 . LEU B 1 82 ? 9.886   -12.188 -34.263 1.00 28.10  ? 81  LEU B CD2 1 
ATOM   1370 N N   . TRP B 1 83 ? 9.714   -6.853  -33.018 1.00 27.95  ? 82  TRP B N   1 
ATOM   1371 C CA  . TRP B 1 83 ? 9.528   -5.466  -33.397 1.00 30.29  ? 82  TRP B CA  1 
ATOM   1372 C C   . TRP B 1 83 ? 10.875  -4.896  -33.838 1.00 30.43  ? 82  TRP B C   1 
ATOM   1373 O O   . TRP B 1 83 ? 10.974  -4.259  -34.897 1.00 29.63  ? 82  TRP B O   1 
ATOM   1374 C CB  . TRP B 1 83 ? 8.909   -4.635  -32.258 1.00 32.23  ? 82  TRP B CB  1 
ATOM   1375 C CG  . TRP B 1 83 ? 8.606   -3.233  -32.735 1.00 30.76  ? 82  TRP B CG  1 
ATOM   1376 C CD1 . TRP B 1 83 ? 7.459   -2.789  -33.322 1.00 39.42  ? 82  TRP B CD1 1 
ATOM   1377 C CD2 . TRP B 1 83 ? 9.542   -2.135  -32.772 1.00 35.53  ? 82  TRP B CD2 1 
ATOM   1378 N NE1 . TRP B 1 83 ? 7.608   -1.478  -33.701 1.00 38.85  ? 82  TRP B NE1 1 
ATOM   1379 C CE2 . TRP B 1 83 ? 8.867   -1.049  -33.372 1.00 34.61  ? 82  TRP B CE2 1 
ATOM   1380 C CE3 . TRP B 1 83 ? 10.865  -1.961  -32.338 1.00 32.41  ? 82  TRP B CE3 1 
ATOM   1381 C CZ2 . TRP B 1 83 ? 9.490   0.198   -33.550 1.00 32.14  ? 82  TRP B CZ2 1 
ATOM   1382 C CZ3 . TRP B 1 83 ? 11.467  -0.728  -32.495 1.00 37.71  ? 82  TRP B CZ3 1 
ATOM   1383 C CH2 . TRP B 1 83 ? 10.787  0.325   -33.107 1.00 34.02  ? 82  TRP B CH2 1 
ATOM   1384 N N   . GLU B 1 84 ? 11.911  -5.160  -33.040 1.00 25.73  ? 83  GLU B N   1 
ATOM   1385 C CA  . GLU B 1 84 ? 13.240  -4.639  -33.294 1.00 28.06  ? 83  GLU B CA  1 
ATOM   1386 C C   . GLU B 1 84 ? 13.825  -5.151  -34.612 1.00 28.47  ? 83  GLU B C   1 
ATOM   1387 O O   . GLU B 1 84 ? 14.387  -4.370  -35.389 1.00 27.04  ? 83  GLU B O   1 
ATOM   1388 C CB  . GLU B 1 84 ? 14.186  -4.856  -32.141 1.00 25.19  ? 83  GLU B CB  1 
ATOM   1389 C CG  . GLU B 1 84 ? 13.688  -4.182  -30.859 1.00 27.25  ? 83  GLU B CG  1 
ATOM   1390 C CD  . GLU B 1 84 ? 14.559  -4.539  -29.694 1.00 29.47  ? 83  GLU B CD  1 
ATOM   1391 O OE1 . GLU B 1 84 ? 15.465  -5.398  -29.793 1.00 29.54  ? 83  GLU B OE1 1 
ATOM   1392 O OE2 . GLU B 1 84 ? 14.379  -3.907  -28.591 1.00 31.08  ? 83  GLU B OE2 1 
ATOM   1393 N N   . ILE B 1 85 ? 13.727  -6.450  -34.871 1.00 27.51  ? 84  ILE B N   1 
ATOM   1394 C CA  . ILE B 1 85 ? 14.425  -6.986  -36.049 1.00 24.65  ? 84  ILE B CA  1 
ATOM   1395 C C   . ILE B 1 85 ? 13.760  -6.440  -37.323 1.00 25.72  ? 84  ILE B C   1 
ATOM   1396 O O   . ILE B 1 85 ? 14.420  -6.252  -38.345 1.00 26.57  ? 84  ILE B O   1 
ATOM   1397 C CB  . ILE B 1 85 ? 14.471  -8.531  -36.023 1.00 23.62  ? 84  ILE B CB  1 
ATOM   1398 C CG1 . ILE B 1 85 ? 15.528  -9.072  -37.026 1.00 25.56  ? 84  ILE B CG1 1 
ATOM   1399 C CG2 . ILE B 1 85 ? 13.098  -9.159  -36.267 1.00 26.21  ? 84  ILE B CG2 1 
ATOM   1400 C CD1 . ILE B 1 85 ? 15.981  -10.492 -36.704 1.00 25.81  ? 84  ILE B CD1 1 
ATOM   1401 N N   . GLN B 1 86 ? 12.464  -6.153  -37.244 1.00 26.26  ? 85  GLN B N   1 
ATOM   1402 C CA  . GLN B 1 86 ? 11.642  -5.629  -38.320 1.00 29.81  ? 85  GLN B CA  1 
ATOM   1403 C C   . GLN B 1 86 ? 11.914  -4.141  -38.535 1.00 32.35  ? 85  GLN B C   1 
ATOM   1404 O O   . GLN B 1 86 ? 12.087  -3.727  -39.680 1.00 35.53  ? 85  GLN B O   1 
ATOM   1405 C CB  . GLN B 1 86 ? 10.173  -5.942  -38.013 1.00 34.76  ? 85  GLN B CB  1 
ATOM   1406 C CG  . GLN B 1 86 ? 9.743   -7.376  -38.352 1.00 46.65  ? 85  GLN B CG  1 
ATOM   1407 C CD  . GLN B 1 86 ? 8.580   -7.948  -37.547 1.00 55.77  ? 85  GLN B CD  1 
ATOM   1408 O OE1 . GLN B 1 86 ? 7.462   -7.408  -37.496 1.00 56.98  ? 85  GLN B OE1 1 
ATOM   1409 N NE2 . GLN B 1 86 ? 8.837   -9.094  -36.922 1.00 50.72  ? 85  GLN B NE2 1 
ATOM   1410 N N   . ASN B 1 87 ? 11.960  -3.356  -37.445 1.00 27.19  ? 86  ASN B N   1 
ATOM   1411 C CA  . ASN B 1 87 ? 11.836  -1.901  -37.583 1.00 27.41  ? 86  ASN B CA  1 
ATOM   1412 C C   . ASN B 1 87 ? 13.148  -1.172  -37.362 1.00 28.44  ? 86  ASN B C   1 
ATOM   1413 O O   . ASN B 1 87 ? 13.294  -0.028  -37.827 1.00 30.57  ? 86  ASN B O   1 
ATOM   1414 C CB  . ASN B 1 87 ? 10.844  -1.358  -36.554 1.00 31.84  ? 86  ASN B CB  1 
ATOM   1415 C CG  . ASN B 1 87 ? 9.474   -1.869  -36.898 1.00 37.93  ? 86  ASN B CG  1 
ATOM   1416 O OD1 . ASN B 1 87 ? 8.883   -1.425  -37.886 1.00 46.54  ? 86  ASN B OD1 1 
ATOM   1417 N ND2 . ASN B 1 87 ? 8.979   -2.845  -36.161 1.00 43.57  ? 86  ASN B ND2 1 
ATOM   1418 N N   . ASN B 1 88 ? 14.089  -1.747  -36.624 1.00 27.38  ? 87  ASN B N   1 
ATOM   1419 C CA  . ASN B 1 88 ? 15.348  -1.043  -36.429 1.00 29.05  ? 87  ASN B CA  1 
ATOM   1420 C C   . ASN B 1 88 ? 16.406  -2.046  -36.008 1.00 28.75  ? 87  ASN B C   1 
ATOM   1421 O O   . ASN B 1 88 ? 17.004  -1.966  -34.940 1.00 27.04  ? 87  ASN B O   1 
ATOM   1422 C CB  . ASN B 1 88 ? 15.239  0.133   -35.457 1.00 34.88  ? 87  ASN B CB  1 
ATOM   1423 C CG  . ASN B 1 88 ? 16.326  1.162   -35.653 1.00 31.03  ? 87  ASN B CG  1 
ATOM   1424 O OD1 . ASN B 1 88 ? 17.374  0.939   -36.284 1.00 31.57  ? 87  ASN B OD1 1 
ATOM   1425 N ND2 . ASN B 1 88 ? 16.098  2.330   -35.062 1.00 35.07  ? 87  ASN B ND2 1 
ATOM   1426 N N   . PRO B 1 89 ? 16.714  -3.005  -36.922 1.00 27.62  ? 88  PRO B N   1 
ATOM   1427 C CA  . PRO B 1 89 ? 17.668  -4.051  -36.578 1.00 25.93  ? 88  PRO B CA  1 
ATOM   1428 C C   . PRO B 1 89 ? 19.106  -3.641  -36.320 1.00 24.75  ? 88  PRO B C   1 
ATOM   1429 O O   . PRO B 1 89 ? 19.895  -4.369  -35.751 1.00 26.85  ? 88  PRO B O   1 
ATOM   1430 C CB  . PRO B 1 89 ? 17.570  -5.003  -37.806 1.00 26.52  ? 88  PRO B CB  1 
ATOM   1431 C CG  . PRO B 1 89 ? 17.179  -4.076  -38.979 1.00 25.32  ? 88  PRO B CG  1 
ATOM   1432 C CD  . PRO B 1 89 ? 16.202  -3.117  -38.303 1.00 27.16  ? 88  PRO B CD  1 
ATOM   1433 N N   . HIS B 1 90 ? 19.494  -2.433  -36.830 1.00 25.52  ? 89  HIS B N   1 
ATOM   1434 C CA  . HIS B 1 90 ? 20.889  -2.014  -36.794 1.00 26.73  ? 89  HIS B CA  1 
ATOM   1435 C C   . HIS B 1 90 ? 21.158  -0.905  -35.754 1.00 26.23  ? 89  HIS B C   1 
ATOM   1436 O O   . HIS B 1 90 ? 22.293  -0.446  -35.622 1.00 29.08  ? 89  HIS B O   1 
ATOM   1437 C CB  . HIS B 1 90 ? 21.386  -1.595  -38.200 1.00 25.66  ? 89  HIS B CB  1 
ATOM   1438 C CG  . HIS B 1 90 ? 21.221  -2.707  -39.192 1.00 28.91  ? 89  HIS B CG  1 
ATOM   1439 N ND1 . HIS B 1 90 ? 21.795  -3.949  -39.064 1.00 26.93  ? 89  HIS B ND1 1 
ATOM   1440 C CD2 . HIS B 1 90 ? 20.565  -2.719  -40.357 1.00 25.64  ? 89  HIS B CD2 1 
ATOM   1441 C CE1 . HIS B 1 90 ? 21.468  -4.660  -40.140 1.00 25.56  ? 89  HIS B CE1 1 
ATOM   1442 N NE2 . HIS B 1 90 ? 20.687  -3.960  -40.913 1.00 26.40  ? 89  HIS B NE2 1 
ATOM   1443 N N   . ALA B 1 91 ? 20.161  -0.668  -34.895 1.00 27.47  ? 90  ALA B N   1 
ATOM   1444 C CA  . ALA B 1 91 ? 20.305  0.367   -33.867 1.00 29.57  ? 90  ALA B CA  1 
ATOM   1445 C C   . ALA B 1 91 ? 21.268  -0.043  -32.751 1.00 33.71  ? 90  ALA B C   1 
ATOM   1446 O O   . ALA B 1 91 ? 21.530  -1.213  -32.482 1.00 31.05  ? 90  ALA B O   1 
ATOM   1447 C CB  . ALA B 1 91 ? 18.920  0.724   -33.359 1.00 29.54  ? 90  ALA B CB  1 
ATOM   1448 N N   . SER B 1 92 ? 21.761  0.965   -32.004 1.00 33.16  ? 91  SER B N   1 
ATOM   1449 C CA  . SER B 1 92 ? 22.412  0.733   -30.738 1.00 34.56  ? 91  SER B CA  1 
ATOM   1450 C C   . SER B 1 92 ? 21.318  0.520   -29.691 1.00 36.79  ? 91  SER B C   1 
ATOM   1451 O O   . SER B 1 92 ? 20.387  1.336   -29.605 1.00 39.80  ? 91  SER B O   1 
ATOM   1452 C CB  . SER B 1 92 ? 23.180  2.018   -30.385 1.00 38.67  ? 91  SER B CB  1 
ATOM   1453 O OG  . SER B 1 92 ? 23.603  1.957   -29.041 1.00 49.82  ? 91  SER B OG  1 
ATOM   1454 N N   . TYR B 1 93 ? 21.444  -0.588  -28.948 1.00 37.72  ? 92  TYR B N   1 
ATOM   1455 C CA  . TYR B 1 93 ? 20.553  -0.982  -27.878 1.00 40.08  ? 92  TYR B CA  1 
ATOM   1456 C C   . TYR B 1 93 ? 21.317  -0.891  -26.560 1.00 49.60  ? 92  TYR B C   1 
ATOM   1457 O O   . TYR B 1 93 ? 20.902  -1.477  -25.562 1.00 53.99  ? 92  TYR B O   1 
ATOM   1458 C CB  . TYR B 1 93 ? 19.927  -2.356  -28.151 1.00 36.00  ? 92  TYR B CB  1 
ATOM   1459 C CG  . TYR B 1 93 ? 18.936  -2.276  -29.297 1.00 29.34  ? 92  TYR B CG  1 
ATOM   1460 C CD1 . TYR B 1 93 ? 17.620  -1.900  -29.064 1.00 32.02  ? 92  TYR B CD1 1 
ATOM   1461 C CD2 . TYR B 1 93 ? 19.286  -2.640  -30.613 1.00 32.36  ? 92  TYR B CD2 1 
ATOM   1462 C CE1 . TYR B 1 93 ? 16.701  -1.758  -30.091 1.00 29.69  ? 92  TYR B CE1 1 
ATOM   1463 C CE2 . TYR B 1 93 ? 18.377  -2.487  -31.650 1.00 30.09  ? 92  TYR B CE2 1 
ATOM   1464 C CZ  . TYR B 1 93 ? 17.073  -2.089  -31.385 1.00 31.86  ? 92  TYR B CZ  1 
ATOM   1465 O OH  . TYR B 1 93 ? 16.075  -1.955  -32.305 1.00 32.58  ? 92  TYR B OH  1 
ATOM   1466 N N   . SER B 1 94 ? 22.415  -0.115  -26.581 1.00 64.10  ? 93  SER B N   1 
ATOM   1467 C CA  . SER B 1 94 ? 23.102  0.364   -25.387 1.00 72.57  ? 93  SER B CA  1 
ATOM   1468 C C   . SER B 1 94 ? 22.059  0.825   -24.357 1.00 79.11  ? 93  SER B C   1 
ATOM   1469 O O   . SER B 1 94 ? 21.345  1.808   -24.662 1.00 76.29  ? 93  SER B O   1 
ATOM   1470 C CB  . SER B 1 94 ? 24.063  1.499   -25.707 1.00 65.94  ? 93  SER B CB  1 
ATOM   1471 O OG  . SER B 1 94 ? 25.075  1.093   -26.618 1.00 67.91  ? 93  SER B OG  1 
ATOM   1472 O OXT . SER B 1 94 ? 21.974  0.173   -23.296 1.00 92.21  ? 93  SER B OXT 1 
ATOM   1473 N N   . HIS C 1 4  ? 33.021  -23.908 27.299  1.00 74.16  ? 3   HIS C N   1 
ATOM   1474 C CA  . HIS C 1 4  ? 31.851  -23.003 27.482  1.00 78.05  ? 3   HIS C CA  1 
ATOM   1475 C C   . HIS C 1 4  ? 31.139  -23.387 28.784  1.00 77.72  ? 3   HIS C C   1 
ATOM   1476 O O   . HIS C 1 4  ? 31.711  -24.088 29.621  1.00 71.02  ? 3   HIS C O   1 
ATOM   1477 C CB  . HIS C 1 4  ? 31.012  -23.011 26.194  1.00 83.08  ? 3   HIS C CB  1 
ATOM   1478 C CG  . HIS C 1 4  ? 30.178  -21.790 25.951  1.00 90.19  ? 3   HIS C CG  1 
ATOM   1479 N ND1 . HIS C 1 4  ? 30.712  -20.593 25.520  1.00 87.59  ? 3   HIS C ND1 1 
ATOM   1480 C CD2 . HIS C 1 4  ? 28.856  -21.575 26.079  1.00 90.69  ? 3   HIS C CD2 1 
ATOM   1481 C CE1 . HIS C 1 4  ? 29.742  -19.695 25.391  1.00 88.26  ? 3   HIS C CE1 1 
ATOM   1482 N NE2 . HIS C 1 4  ? 28.605  -20.270 25.723  1.00 93.99  ? 3   HIS C NE2 1 
ATOM   1483 N N   . ALA C 1 5  ? 29.900  -22.902 28.956  1.00 75.71  ? 4   ALA C N   1 
ATOM   1484 C CA  . ALA C 1 5  ? 29.013  -23.287 30.045  1.00 68.69  ? 4   ALA C CA  1 
ATOM   1485 C C   . ALA C 1 5  ? 27.557  -23.122 29.620  1.00 70.69  ? 4   ALA C C   1 
ATOM   1486 O O   . ALA C 1 5  ? 27.222  -22.178 28.897  1.00 67.61  ? 4   ALA C O   1 
ATOM   1487 C CB  . ALA C 1 5  ? 29.270  -22.417 31.235  1.00 71.54  ? 4   ALA C CB  1 
ATOM   1488 N N   . PHE C 1 6  ? 26.704  -24.023 30.126  1.00 52.22  ? 5   PHE C N   1 
ATOM   1489 C CA  . PHE C 1 6  ? 25.302  -24.055 29.764  1.00 48.00  ? 5   PHE C CA  1 
ATOM   1490 C C   . PHE C 1 6  ? 24.452  -24.158 31.026  1.00 51.01  ? 5   PHE C C   1 
ATOM   1491 O O   . PHE C 1 6  ? 24.707  -25.013 31.870  1.00 64.51  ? 5   PHE C O   1 
ATOM   1492 C CB  . PHE C 1 6  ? 25.117  -25.282 28.851  1.00 41.79  ? 5   PHE C CB  1 
ATOM   1493 C CG  . PHE C 1 6  ? 25.933  -25.259 27.558  1.00 42.40  ? 5   PHE C CG  1 
ATOM   1494 C CD1 . PHE C 1 6  ? 27.049  -26.071 27.384  1.00 45.00  ? 5   PHE C CD1 1 
ATOM   1495 C CD2 . PHE C 1 6  ? 25.618  -24.379 26.522  1.00 46.38  ? 5   PHE C CD2 1 
ATOM   1496 C CE1 . PHE C 1 6  ? 27.788  -26.053 26.200  1.00 46.99  ? 5   PHE C CE1 1 
ATOM   1497 C CE2 . PHE C 1 6  ? 26.365  -24.359 25.349  1.00 42.33  ? 5   PHE C CE2 1 
ATOM   1498 C CZ  . PHE C 1 6  ? 27.434  -25.204 25.171  1.00 38.74  ? 5   PHE C CZ  1 
ATOM   1499 N N   . LYS C 1 7  ? 23.455  -23.277 31.152  1.00 54.24  ? 6   LYS C N   1 
ATOM   1500 C CA  . LYS C 1 7  ? 22.476  -23.353 32.229  1.00 55.80  ? 6   LYS C CA  1 
ATOM   1501 C C   . LYS C 1 7  ? 21.179  -23.826 31.590  1.00 43.29  ? 6   LYS C C   1 
ATOM   1502 O O   . LYS C 1 7  ? 21.074  -23.778 30.361  1.00 49.02  ? 6   LYS C O   1 
ATOM   1503 C CB  . LYS C 1 7  ? 22.307  -21.998 32.936  1.00 51.53  ? 6   LYS C CB  1 
ATOM   1504 N N   . PRO C 1 8  ? 20.164  -24.313 32.348  1.00 51.00  ? 7   PRO C N   1 
ATOM   1505 C CA  . PRO C 1 8  ? 18.881  -24.677 31.744  1.00 50.06  ? 7   PRO C CA  1 
ATOM   1506 C C   . PRO C 1 8  ? 18.361  -23.496 30.922  1.00 53.84  ? 7   PRO C C   1 
ATOM   1507 O O   . PRO C 1 8  ? 18.560  -22.341 31.302  1.00 58.43  ? 7   PRO C O   1 
ATOM   1508 C CB  . PRO C 1 8  ? 18.004  -25.014 32.965  1.00 54.11  ? 7   PRO C CB  1 
ATOM   1509 C CG  . PRO C 1 8  ? 19.004  -25.512 33.984  1.00 48.94  ? 7   PRO C CG  1 
ATOM   1510 C CD  . PRO C 1 8  ? 20.211  -24.594 33.800  1.00 44.97  ? 7   PRO C CD  1 
ATOM   1511 N N   . GLY C 1 9  ? 17.756  -23.794 29.764  1.00 48.91  ? 8   GLY C N   1 
ATOM   1512 C CA  . GLY C 1 9  ? 17.115  -22.781 28.936  1.00 46.81  ? 8   GLY C CA  1 
ATOM   1513 C C   . GLY C 1 9  ? 17.998  -22.278 27.791  1.00 48.01  ? 8   GLY C C   1 
ATOM   1514 O O   . GLY C 1 9  ? 17.461  -21.767 26.808  1.00 50.34  ? 8   GLY C O   1 
ATOM   1515 N N   . ASP C 1 10 ? 19.326  -22.437 27.916  1.00 45.07  ? 9   ASP C N   1 
ATOM   1516 C CA  . ASP C 1 10 ? 20.312  -22.125 26.891  1.00 36.95  ? 9   ASP C CA  1 
ATOM   1517 C C   . ASP C 1 10 ? 20.015  -22.841 25.568  1.00 38.89  ? 9   ASP C C   1 
ATOM   1518 O O   . ASP C 1 10 ? 19.719  -24.035 25.540  1.00 37.40  ? 9   ASP C O   1 
ATOM   1519 C CB  . ASP C 1 10 ? 21.740  -22.401 27.332  1.00 42.03  ? 9   ASP C CB  1 
ATOM   1520 C CG  . ASP C 1 10 ? 22.357  -21.463 28.373  1.00 52.52  ? 9   ASP C CG  1 
ATOM   1521 O OD1 . ASP C 1 10 ? 21.723  -20.450 28.690  1.00 56.60  ? 9   ASP C OD1 1 
ATOM   1522 O OD2 . ASP C 1 10 ? 23.474  -21.763 28.868  1.00 53.90  ? 9   ASP C OD2 1 
ATOM   1523 N N   . LEU C 1 11 ? 20.096  -22.089 24.468  1.00 39.65  ? 10  LEU C N   1 
ATOM   1524 C CA  . LEU C 1 11 ? 19.729  -22.605 23.161  1.00 35.44  ? 10  LEU C CA  1 
ATOM   1525 C C   . LEU C 1 11 ? 20.981  -23.075 22.457  1.00 34.36  ? 10  LEU C C   1 
ATOM   1526 O O   . LEU C 1 11 ? 21.993  -22.385 22.492  1.00 34.60  ? 10  LEU C O   1 
ATOM   1527 C CB  . LEU C 1 11 ? 19.079  -21.466 22.374  1.00 36.34  ? 10  LEU C CB  1 
ATOM   1528 C CG  . LEU C 1 11 ? 17.759  -20.986 22.974  1.00 32.25  ? 10  LEU C CG  1 
ATOM   1529 C CD1 . LEU C 1 11 ? 17.200  -19.949 22.027  1.00 35.55  ? 10  LEU C CD1 1 
ATOM   1530 C CD2 . LEU C 1 11 ? 16.756  -22.089 23.276  1.00 35.20  ? 10  LEU C CD2 1 
ATOM   1531 N N   . VAL C 1 12 ? 20.901  -24.252 21.801  1.00 30.87  ? 11  VAL C N   1 
ATOM   1532 C CA  . VAL C 1 12 ? 22.082  -24.880 21.248  1.00 30.27  ? 11  VAL C CA  1 
ATOM   1533 C C   . VAL C 1 12 ? 21.714  -25.611 19.935  1.00 28.50  ? 11  VAL C C   1 
ATOM   1534 O O   . VAL C 1 12 ? 20.516  -25.838 19.660  1.00 29.31  ? 11  VAL C O   1 
ATOM   1535 C CB  . VAL C 1 12 ? 22.689  -25.880 22.264  1.00 33.18  ? 11  VAL C CB  1 
ATOM   1536 C CG1 . VAL C 1 12 ? 23.078  -25.194 23.589  1.00 36.14  ? 11  VAL C CG1 1 
ATOM   1537 C CG2 . VAL C 1 12 ? 21.779  -27.071 22.534  1.00 33.51  ? 11  VAL C CG2 1 
ATOM   1538 N N   . PHE C 1 13 ? 22.771  -26.009 19.225  1.00 30.95  ? 12  PHE C N   1 
ATOM   1539 C CA  . PHE C 1 13 ? 22.746  -27.153 18.316  1.00 27.41  ? 12  PHE C CA  1 
ATOM   1540 C C   . PHE C 1 13 ? 23.462  -28.321 18.988  1.00 29.06  ? 12  PHE C C   1 
ATOM   1541 O O   . PHE C 1 13 ? 24.569  -28.203 19.553  1.00 29.46  ? 12  PHE C O   1 
ATOM   1542 C CB  . PHE C 1 13 ? 23.379  -26.909 16.938  1.00 32.45  ? 12  PHE C CB  1 
ATOM   1543 C CG  . PHE C 1 13 ? 22.601  -25.902 16.110  1.00 33.50  ? 12  PHE C CG  1 
ATOM   1544 C CD1 . PHE C 1 13 ? 21.576  -26.314 15.255  1.00 31.32  ? 12  PHE C CD1 1 
ATOM   1545 C CD2 . PHE C 1 13 ? 22.902  -24.545 16.184  1.00 35.88  ? 12  PHE C CD2 1 
ATOM   1546 C CE1 . PHE C 1 13 ? 20.881  -25.391 14.490  1.00 32.68  ? 12  PHE C CE1 1 
ATOM   1547 C CE2 . PHE C 1 13 ? 22.184  -23.628 15.453  1.00 36.60  ? 12  PHE C CE2 1 
ATOM   1548 C CZ  . PHE C 1 13 ? 21.185  -24.052 14.594  1.00 36.68  ? 12  PHE C CZ  1 
ATOM   1549 N N   . ALA C 1 14 ? 22.813  -29.498 18.953  1.00 28.75  ? 13  ALA C N   1 
ATOM   1550 C CA  . ALA C 1 14 ? 23.247  -30.655 19.726  1.00 24.67  ? 13  ALA C CA  1 
ATOM   1551 C C   . ALA C 1 14 ? 23.521  -31.792 18.746  1.00 29.77  ? 13  ALA C C   1 
ATOM   1552 O O   . ALA C 1 14 ? 22.676  -32.066 17.893  1.00 27.37  ? 13  ALA C O   1 
ATOM   1553 C CB  . ALA C 1 14 ? 22.163  -31.038 20.724  1.00 24.42  ? 13  ALA C CB  1 
ATOM   1554 N N   . LYS C 1 15 ? 24.736  -32.350 18.807  1.00 28.84  ? 14  LYS C N   1 
ATOM   1555 C CA  . LYS C 1 15 ? 25.151  -33.369 17.856  1.00 27.88  ? 14  LYS C CA  1 
ATOM   1556 C C   . LYS C 1 15 ? 25.118  -34.736 18.515  1.00 27.75  ? 14  LYS C C   1 
ATOM   1557 O O   . LYS C 1 15 ? 25.834  -34.999 19.493  1.00 30.85  ? 14  LYS C O   1 
ATOM   1558 C CB  . LYS C 1 15 ? 26.545  -33.019 17.322  1.00 28.56  ? 14  LYS C CB  1 
ATOM   1559 C CG  . LYS C 1 15 ? 27.055  -33.992 16.228  1.00 29.84  ? 14  LYS C CG  1 
ATOM   1560 C CD  . LYS C 1 15 ? 26.256  -33.853 14.925  1.00 28.73  ? 14  LYS C CD  1 
ATOM   1561 C CE  . LYS C 1 15 ? 26.711  -34.711 13.738  1.00 31.30  ? 14  LYS C CE  1 
ATOM   1562 N NZ  . LYS C 1 15 ? 26.578  -36.144 14.010  1.00 32.18  ? 14  LYS C NZ  1 
ATOM   1563 N N   . MET C 1 16 ? 24.346  -35.664 17.923  1.00 26.02  ? 15  MET C N   1 
ATOM   1564 C CA  . MET C 1 16 ? 24.351  -37.094 18.254  1.00 25.72  ? 15  MET C CA  1 
ATOM   1565 C C   . MET C 1 16 ? 24.846  -37.849 17.021  1.00 30.65  ? 15  MET C C   1 
ATOM   1566 O O   . MET C 1 16 ? 24.568  -37.461 15.884  1.00 28.47  ? 15  MET C O   1 
ATOM   1567 C CB  . MET C 1 16 ? 22.943  -37.593 18.591  1.00 31.51  ? 15  MET C CB  1 
ATOM   1568 C CG  . MET C 1 16 ? 22.367  -36.920 19.833  1.00 31.99  ? 15  MET C CG  1 
ATOM   1569 S SD  . MET C 1 16 ? 20.744  -37.598 20.218  1.00 36.98  ? 15  MET C SD  1 
ATOM   1570 C CE  . MET C 1 16 ? 19.733  -36.955 18.863  1.00 36.65  ? 15  MET C CE  1 
ATOM   1571 N N   . LYS C 1 17 ? 25.553  -38.971 17.262  1.00 30.69  ? 16  LYS C N   1 
ATOM   1572 C CA  . LYS C 1 17 ? 25.868  -39.902 16.175  1.00 34.12  ? 16  LYS C CA  1 
ATOM   1573 C C   . LYS C 1 17 ? 24.587  -40.340 15.455  1.00 26.14  ? 16  LYS C C   1 
ATOM   1574 O O   . LYS C 1 17 ? 23.614  -40.799 16.070  1.00 31.14  ? 16  LYS C O   1 
ATOM   1575 C CB  . LYS C 1 17 ? 26.617  -41.107 16.770  1.00 29.83  ? 16  LYS C CB  1 
ATOM   1576 C CG  . LYS C 1 17 ? 27.167  -42.120 15.755  1.00 33.86  ? 16  LYS C CG  1 
ATOM   1577 C CD  . LYS C 1 17 ? 28.342  -41.357 15.155  1.00 35.27  ? 16  LYS C CD  1 
ATOM   1578 C CE  . LYS C 1 17 ? 29.172  -42.268 14.280  1.00 45.10  ? 16  LYS C CE  1 
ATOM   1579 N NZ  . LYS C 1 17 ? 30.375  -41.570 13.830  1.00 43.26  ? 16  LYS C NZ  1 
ATOM   1580 N N   . GLY C 1 18 ? 24.643  -40.230 14.123  1.00 30.19  ? 17  GLY C N   1 
ATOM   1581 C CA  . GLY C 1 18 ? 23.555  -40.706 13.283  1.00 30.79  ? 17  GLY C CA  1 
ATOM   1582 C C   . GLY C 1 18 ? 22.629  -39.560 12.884  1.00 30.58  ? 17  GLY C C   1 
ATOM   1583 O O   . GLY C 1 18 ? 21.653  -39.801 12.202  1.00 29.65  ? 17  GLY C O   1 
ATOM   1584 N N   . TYR C 1 19 ? 22.905  -38.334 13.356  1.00 29.21  ? 18  TYR C N   1 
ATOM   1585 C CA  . TYR C 1 19 ? 21.962  -37.221 13.138  1.00 28.79  ? 18  TYR C CA  1 
ATOM   1586 C C   . TYR C 1 19 ? 22.729  -35.943 12.874  1.00 27.32  ? 18  TYR C C   1 
ATOM   1587 O O   . TYR C 1 19 ? 23.836  -35.769 13.394  1.00 27.20  ? 18  TYR C O   1 
ATOM   1588 C CB  . TYR C 1 19 ? 21.133  -36.897 14.387  1.00 25.86  ? 18  TYR C CB  1 
ATOM   1589 C CG  . TYR C 1 19 ? 20.295  -38.094 14.783  1.00 26.95  ? 18  TYR C CG  1 
ATOM   1590 C CD1 . TYR C 1 19 ? 20.791  -39.111 15.595  1.00 29.59  ? 18  TYR C CD1 1 
ATOM   1591 C CD2 . TYR C 1 19 ? 19.007  -38.194 14.292  1.00 30.39  ? 18  TYR C CD2 1 
ATOM   1592 C CE1 . TYR C 1 19 ? 20.001  -40.201 15.926  1.00 31.89  ? 18  TYR C CE1 1 
ATOM   1593 C CE2 . TYR C 1 19 ? 18.207  -39.270 14.633  1.00 37.46  ? 18  TYR C CE2 1 
ATOM   1594 C CZ  . TYR C 1 19 ? 18.698  -40.255 15.467  1.00 34.91  ? 18  TYR C CZ  1 
ATOM   1595 O OH  . TYR C 1 19 ? 17.877  -41.318 15.751  1.00 45.55  ? 18  TYR C OH  1 
ATOM   1596 N N   . PRO C 1 20 ? 22.183  -34.995 12.085  1.00 27.65  ? 19  PRO C N   1 
ATOM   1597 C CA  . PRO C 1 20 ? 22.842  -33.709 11.881  1.00 26.37  ? 19  PRO C CA  1 
ATOM   1598 C C   . PRO C 1 20 ? 22.792  -32.874 13.166  1.00 28.50  ? 19  PRO C C   1 
ATOM   1599 O O   . PRO C 1 20 ? 22.009  -33.134 14.080  1.00 26.50  ? 19  PRO C O   1 
ATOM   1600 C CB  . PRO C 1 20 ? 21.960  -33.105 10.736  1.00 30.11  ? 19  PRO C CB  1 
ATOM   1601 C CG  . PRO C 1 20 ? 20.594  -33.656 11.000  1.00 28.30  ? 19  PRO C CG  1 
ATOM   1602 C CD  . PRO C 1 20 ? 20.875  -35.097 11.401  1.00 26.19  ? 19  PRO C CD  1 
ATOM   1603 N N   . HIS C 1 21 ? 23.621  -31.857 13.226  1.00 27.96  ? 20  HIS C N   1 
ATOM   1604 C CA  . HIS C 1 21 ? 23.526  -30.933 14.355  1.00 26.83  ? 20  HIS C CA  1 
ATOM   1605 C C   . HIS C 1 21 ? 22.101  -30.403 14.487  1.00 30.23  ? 20  HIS C C   1 
ATOM   1606 O O   . HIS C 1 21 ? 21.553  -29.873 13.537  1.00 28.27  ? 20  HIS C O   1 
ATOM   1607 C CB  . HIS C 1 21 ? 24.500  -29.778 14.135  1.00 31.85  ? 20  HIS C CB  1 
ATOM   1608 C CG  . HIS C 1 21 ? 25.941  -30.217 14.156  1.00 31.77  ? 20  HIS C CG  1 
ATOM   1609 N ND1 . HIS C 1 21 ? 26.597  -30.836 13.114  1.00 35.37  ? 20  HIS C ND1 1 
ATOM   1610 C CD2 . HIS C 1 21 ? 26.860  -30.039 15.135  1.00 34.32  ? 20  HIS C CD2 1 
ATOM   1611 C CE1 . HIS C 1 21 ? 27.857  -31.064 13.464  1.00 40.01  ? 20  HIS C CE1 1 
ATOM   1612 N NE2 . HIS C 1 21 ? 28.041  -30.580 14.679  1.00 38.09  ? 20  HIS C NE2 1 
ATOM   1613 N N   . TRP C 1 22 ? 21.512  -30.513 15.699  1.00 26.13  ? 21  TRP C N   1 
ATOM   1614 C CA  . TRP C 1 22 ? 20.061  -30.414 15.813  1.00 25.50  ? 21  TRP C CA  1 
ATOM   1615 C C   . TRP C 1 22 ? 19.686  -29.233 16.705  1.00 25.40  ? 21  TRP C C   1 
ATOM   1616 O O   . TRP C 1 22 ? 20.261  -29.064 17.796  1.00 24.94  ? 21  TRP C O   1 
ATOM   1617 C CB  . TRP C 1 22 ? 19.494  -31.712 16.421  1.00 24.32  ? 21  TRP C CB  1 
ATOM   1618 C CG  . TRP C 1 22 ? 18.051  -31.919 16.036  1.00 23.72  ? 21  TRP C CG  1 
ATOM   1619 C CD1 . TRP C 1 22 ? 16.967  -31.324 16.604  1.00 27.72  ? 21  TRP C CD1 1 
ATOM   1620 C CD2 . TRP C 1 22 ? 17.575  -32.814 14.995  1.00 25.30  ? 21  TRP C CD2 1 
ATOM   1621 N NE1 . TRP C 1 22 ? 15.838  -31.748 15.938  1.00 26.38  ? 21  TRP C NE1 1 
ATOM   1622 C CE2 . TRP C 1 22 ? 16.171  -32.653 14.970  1.00 25.50  ? 21  TRP C CE2 1 
ATOM   1623 C CE3 . TRP C 1 22 ? 18.202  -33.702 14.102  1.00 27.46  ? 21  TRP C CE3 1 
ATOM   1624 C CZ2 . TRP C 1 22 ? 15.385  -33.403 14.070  1.00 26.39  ? 21  TRP C CZ2 1 
ATOM   1625 C CZ3 . TRP C 1 22 ? 17.437  -34.396 13.176  1.00 26.51  ? 21  TRP C CZ3 1 
ATOM   1626 C CH2 . TRP C 1 22 ? 16.046  -34.267 13.231  1.00 26.72  ? 21  TRP C CH2 1 
ATOM   1627 N N   . PRO C 1 23 ? 18.676  -28.405 16.348  1.00 26.69  ? 22  PRO C N   1 
ATOM   1628 C CA  . PRO C 1 23 ? 18.264  -27.321 17.244  1.00 25.13  ? 22  PRO C CA  1 
ATOM   1629 C C   . PRO C 1 23 ? 17.717  -27.873 18.555  1.00 24.28  ? 22  PRO C C   1 
ATOM   1630 O O   . PRO C 1 23 ? 16.907  -28.778 18.538  1.00 26.22  ? 22  PRO C O   1 
ATOM   1631 C CB  . PRO C 1 23 ? 17.222  -26.595 16.368  1.00 29.20  ? 22  PRO C CB  1 
ATOM   1632 C CG  . PRO C 1 23 ? 16.674  -27.670 15.453  1.00 26.28  ? 22  PRO C CG  1 
ATOM   1633 C CD  . PRO C 1 23 ? 17.962  -28.373 15.049  1.00 25.86  ? 22  PRO C CD  1 
ATOM   1634 N N   . ALA C 1 24 ? 18.217  -27.331 19.682  1.00 26.99  ? 23  ALA C N   1 
ATOM   1635 C CA  . ALA C 1 24 ? 17.921  -27.931 20.982  1.00 30.00  ? 23  ALA C CA  1 
ATOM   1636 C C   . ALA C 1 24 ? 18.032  -26.880 22.083  1.00 34.02  ? 23  ALA C C   1 
ATOM   1637 O O   . ALA C 1 24 ? 18.542  -25.786 21.843  1.00 31.66  ? 23  ALA C O   1 
ATOM   1638 C CB  . ALA C 1 24 ? 18.904  -29.074 21.247  1.00 29.62  ? 23  ALA C CB  1 
ATOM   1639 N N   . ARG C 1 25 ? 17.593  -27.247 23.303  1.00 33.09  ? 24  ARG C N   1 
ATOM   1640 C CA  . ARG C 1 25 ? 17.927  -26.438 24.464  1.00 33.37  ? 24  ARG C CA  1 
ATOM   1641 C C   . ARG C 1 25 ? 18.419  -27.338 25.608  1.00 34.48  ? 24  ARG C C   1 
ATOM   1642 O O   . ARG C 1 25 ? 18.137  -28.536 25.616  1.00 34.38  ? 24  ARG C O   1 
ATOM   1643 C CB  . ARG C 1 25 ? 16.708  -25.643 24.936  1.00 34.53  ? 24  ARG C CB  1 
ATOM   1644 C CG  . ARG C 1 25 ? 15.493  -26.480 25.309  1.00 40.54  ? 24  ARG C CG  1 
ATOM   1645 C CD  . ARG C 1 25 ? 14.487  -25.534 25.967  1.00 44.01  ? 24  ARG C CD  1 
ATOM   1646 N NE  . ARG C 1 25 ? 13.278  -26.333 26.221  1.00 52.49  ? 24  ARG C NE  1 
ATOM   1647 C CZ  . ARG C 1 25 ? 12.007  -26.067 25.963  1.00 52.67  ? 24  ARG C CZ  1 
ATOM   1648 N NH1 . ARG C 1 25 ? 11.646  -24.913 25.431  1.00 48.15  ? 24  ARG C NH1 1 
ATOM   1649 N NH2 . ARG C 1 25 ? 11.082  -26.968 26.265  1.00 53.88  ? 24  ARG C NH2 1 
ATOM   1650 N N   . ILE C 1 26 ? 19.114  -26.715 26.556  1.00 35.37  ? 25  ILE C N   1 
ATOM   1651 C CA  . ILE C 1 26 ? 19.474  -27.326 27.832  1.00 33.89  ? 25  ILE C CA  1 
ATOM   1652 C C   . ILE C 1 26 ? 18.248  -27.304 28.726  1.00 42.08  ? 25  ILE C C   1 
ATOM   1653 O O   . ILE C 1 26 ? 17.665  -26.250 28.940  1.00 42.45  ? 25  ILE C O   1 
ATOM   1654 C CB  . ILE C 1 26 ? 20.626  -26.559 28.503  1.00 36.82  ? 25  ILE C CB  1 
ATOM   1655 C CG1 . ILE C 1 26 ? 21.769  -26.216 27.573  1.00 39.29  ? 25  ILE C CG1 1 
ATOM   1656 C CG2 . ILE C 1 26 ? 21.094  -27.298 29.767  1.00 38.22  ? 25  ILE C CG2 1 
ATOM   1657 C CD1 . ILE C 1 26 ? 22.584  -27.380 27.041  1.00 40.46  ? 25  ILE C CD1 1 
ATOM   1658 N N   . ASP C 1 27 ? 17.873  -28.473 29.227  1.00 40.04  ? 26  ASP C N   1 
ATOM   1659 C CA  . ASP C 1 27 ? 16.813  -28.607 30.214  1.00 51.37  ? 26  ASP C CA  1 
ATOM   1660 C C   . ASP C 1 27 ? 17.388  -28.511 31.623  1.00 54.80  ? 26  ASP C C   1 
ATOM   1661 O O   . ASP C 1 27 ? 18.603  -28.603 31.798  1.00 52.61  ? 26  ASP C O   1 
ATOM   1662 C CB  . ASP C 1 27 ? 16.152  -29.969 30.110  1.00 50.95  ? 26  ASP C CB  1 
ATOM   1663 C CG  . ASP C 1 27 ? 14.888  -30.018 29.271  1.00 61.71  ? 26  ASP C CG  1 
ATOM   1664 O OD1 . ASP C 1 27 ? 14.587  -28.979 28.640  1.00 55.34  ? 26  ASP C OD1 1 
ATOM   1665 O OD2 . ASP C 1 27 ? 14.205  -31.077 29.303  1.00 57.37  ? 26  ASP C OD2 1 
ATOM   1666 N N   . ASP C 1 28 ? 16.498  -28.321 32.612  1.00 64.11  ? 27  ASP C N   1 
ATOM   1667 C CA  . ASP C 1 28 ? 16.796  -28.515 34.028  1.00 62.81  ? 27  ASP C CA  1 
ATOM   1668 C C   . ASP C 1 28 ? 16.668  -30.005 34.340  1.00 62.93  ? 27  ASP C C   1 
ATOM   1669 O O   . ASP C 1 28 ? 16.247  -30.767 33.477  1.00 57.53  ? 27  ASP C O   1 
ATOM   1670 C CB  . ASP C 1 28 ? 15.886  -27.676 34.911  1.00 63.42  ? 27  ASP C CB  1 
ATOM   1671 N N   . ILE C 1 29 ? 17.052  -30.419 35.558  1.00 64.40  ? 28  ILE C N   1 
ATOM   1672 C CA  . ILE C 1 29 ? 16.839  -31.792 35.995  1.00 62.41  ? 28  ILE C CA  1 
ATOM   1673 C C   . ILE C 1 29 ? 15.742  -31.803 37.070  1.00 64.67  ? 28  ILE C C   1 
ATOM   1674 O O   . ILE C 1 29 ? 16.054  -31.309 38.175  1.00 73.36  ? 28  ILE C O   1 
ATOM   1675 C CB  . ILE C 1 29 ? 18.140  -32.412 36.535  1.00 58.45  ? 28  ILE C CB  1 
ATOM   1676 N N   . LYS C 1 35 ? 19.735  -38.907 37.706  1.00 53.34  ? 34  LYS C N   1 
ATOM   1677 C CA  . LYS C 1 35 ? 20.831  -37.923 37.492  1.00 53.90  ? 34  LYS C CA  1 
ATOM   1678 C C   . LYS C 1 35 ? 21.489  -38.210 36.142  1.00 48.33  ? 34  LYS C C   1 
ATOM   1679 O O   . LYS C 1 35 ? 21.502  -39.348 35.671  1.00 51.38  ? 34  LYS C O   1 
ATOM   1680 C CB  . LYS C 1 35 ? 21.835  -37.920 38.654  1.00 54.53  ? 34  LYS C CB  1 
ATOM   1681 N N   . PRO C 1 36 ? 22.014  -37.178 35.448  1.00 51.31  ? 35  PRO C N   1 
ATOM   1682 C CA  . PRO C 1 36 ? 22.725  -37.413 34.194  1.00 46.92  ? 35  PRO C CA  1 
ATOM   1683 C C   . PRO C 1 36 ? 23.880  -38.378 34.455  1.00 52.73  ? 35  PRO C C   1 
ATOM   1684 O O   . PRO C 1 36 ? 24.302  -38.594 35.601  1.00 49.49  ? 35  PRO C O   1 
ATOM   1685 C CB  . PRO C 1 36 ? 23.204  -35.998 33.811  1.00 54.88  ? 35  PRO C CB  1 
ATOM   1686 C CG  . PRO C 1 36 ? 22.203  -35.082 34.477  1.00 54.20  ? 35  PRO C CG  1 
ATOM   1687 C CD  . PRO C 1 36 ? 21.931  -35.752 35.823  1.00 51.66  ? 35  PRO C CD  1 
ATOM   1688 N N   . PRO C 1 37 ? 24.425  -39.019 33.404  1.00 50.53  ? 36  PRO C N   1 
ATOM   1689 C CA  . PRO C 1 37 ? 25.733  -39.643 33.533  1.00 48.46  ? 36  PRO C CA  1 
ATOM   1690 C C   . PRO C 1 37 ? 26.648  -38.485 33.910  1.00 44.02  ? 36  PRO C C   1 
ATOM   1691 O O   . PRO C 1 37 ? 26.312  -37.305 33.726  1.00 38.81  ? 36  PRO C O   1 
ATOM   1692 C CB  . PRO C 1 37 ? 26.000  -40.178 32.114  1.00 47.12  ? 36  PRO C CB  1 
ATOM   1693 C CG  . PRO C 1 37 ? 24.603  -40.406 31.594  1.00 46.29  ? 36  PRO C CG  1 
ATOM   1694 C CD  . PRO C 1 37 ? 23.831  -39.190 32.068  1.00 46.04  ? 36  PRO C CD  1 
ATOM   1695 N N   . PRO C 1 38 ? 27.828  -38.803 34.481  1.00 39.47  ? 37  PRO C N   1 
ATOM   1696 C CA  . PRO C 1 38 ? 28.829  -37.787 34.784  1.00 40.13  ? 37  PRO C CA  1 
ATOM   1697 C C   . PRO C 1 38 ? 29.119  -36.879 33.597  1.00 35.37  ? 37  PRO C C   1 
ATOM   1698 O O   . PRO C 1 38 ? 29.381  -37.347 32.485  1.00 37.50  ? 37  PRO C O   1 
ATOM   1699 C CB  . PRO C 1 38 ? 30.016  -38.720 35.133  1.00 41.91  ? 37  PRO C CB  1 
ATOM   1700 C CG  . PRO C 1 38 ? 29.332  -39.870 35.829  1.00 41.15  ? 37  PRO C CG  1 
ATOM   1701 C CD  . PRO C 1 38 ? 28.251  -40.177 34.832  1.00 42.36  ? 37  PRO C CD  1 
ATOM   1702 N N   . ASN C 1 39 ? 29.016  -35.566 33.853  1.00 35.91  ? 38  ASN C N   1 
ATOM   1703 C CA  . ASN C 1 39 ? 29.442  -34.514 32.955  1.00 36.22  ? 38  ASN C CA  1 
ATOM   1704 C C   . ASN C 1 39 ? 28.531  -34.460 31.732  1.00 38.70  ? 38  ASN C C   1 
ATOM   1705 O O   . ASN C 1 39 ? 29.001  -34.057 30.676  1.00 42.23  ? 38  ASN C O   1 
ATOM   1706 C CB  . ASN C 1 39 ? 30.907  -34.642 32.546  1.00 38.93  ? 38  ASN C CB  1 
ATOM   1707 C CG  . ASN C 1 39 ? 31.472  -33.402 31.884  1.00 46.85  ? 38  ASN C CG  1 
ATOM   1708 O OD1 . ASN C 1 39 ? 31.040  -32.277 32.165  1.00 59.98  ? 38  ASN C OD1 1 
ATOM   1709 N ND2 . ASN C 1 39 ? 32.454  -33.574 31.006  1.00 49.10  ? 38  ASN C ND2 1 
ATOM   1710 N N   . LYS C 1 40 ? 27.266  -34.881 31.877  1.00 33.92  ? 39  LYS C N   1 
ATOM   1711 C CA  . LYS C 1 40 ? 26.338  -34.746 30.766  1.00 30.37  ? 39  LYS C CA  1 
ATOM   1712 C C   . LYS C 1 40 ? 25.186  -33.811 31.113  1.00 32.79  ? 39  LYS C C   1 
ATOM   1713 O O   . LYS C 1 40 ? 24.764  -33.688 32.253  1.00 35.34  ? 39  LYS C O   1 
ATOM   1714 C CB  . LYS C 1 40 ? 25.702  -36.084 30.375  1.00 32.94  ? 39  LYS C CB  1 
ATOM   1715 C CG  . LYS C 1 40 ? 26.677  -37.181 30.076  1.00 38.21  ? 39  LYS C CG  1 
ATOM   1716 C CD  . LYS C 1 40 ? 27.682  -36.963 28.961  1.00 45.53  ? 39  LYS C CD  1 
ATOM   1717 C CE  . LYS C 1 40 ? 28.417  -38.242 28.646  1.00 44.10  ? 39  LYS C CE  1 
ATOM   1718 N NZ  . LYS C 1 40 ? 29.269  -38.046 27.471  1.00 51.75  ? 39  LYS C NZ  1 
ATOM   1719 N N   . TYR C 1 41 ? 24.672  -33.166 30.064  1.00 30.53  ? 40  TYR C N   1 
ATOM   1720 C CA  . TYR C 1 41 ? 23.593  -32.192 30.155  1.00 32.38  ? 40  TYR C CA  1 
ATOM   1721 C C   . TYR C 1 41 ? 22.318  -32.866 29.675  1.00 31.71  ? 40  TYR C C   1 
ATOM   1722 O O   . TYR C 1 41 ? 22.348  -33.600 28.684  1.00 30.85  ? 40  TYR C O   1 
ATOM   1723 C CB  . TYR C 1 41 ? 23.772  -30.977 29.231  1.00 29.58  ? 40  TYR C CB  1 
ATOM   1724 C CG  . TYR C 1 41 ? 24.911  -30.058 29.654  1.00 28.73  ? 40  TYR C CG  1 
ATOM   1725 C CD1 . TYR C 1 41 ? 26.196  -30.264 29.170  1.00 30.02  ? 40  TYR C CD1 1 
ATOM   1726 C CD2 . TYR C 1 41 ? 24.703  -29.058 30.602  1.00 33.60  ? 40  TYR C CD2 1 
ATOM   1727 C CE1 . TYR C 1 41 ? 27.257  -29.475 29.578  1.00 39.24  ? 40  TYR C CE1 1 
ATOM   1728 C CE2 . TYR C 1 41 ? 25.751  -28.231 30.975  1.00 34.08  ? 40  TYR C CE2 1 
ATOM   1729 C CZ  . TYR C 1 41 ? 27.024  -28.456 30.493  1.00 37.70  ? 40  TYR C CZ  1 
ATOM   1730 O OH  . TYR C 1 41 ? 28.055  -27.666 30.906  1.00 46.76  ? 40  TYR C OH  1 
ATOM   1731 N N   . PRO C 1 42 ? 21.152  -32.549 30.282  1.00 35.06  ? 41  PRO C N   1 
ATOM   1732 C CA  . PRO C 1 42 ? 19.863  -32.961 29.725  1.00 31.41  ? 41  PRO C CA  1 
ATOM   1733 C C   . PRO C 1 42 ? 19.523  -32.018 28.582  1.00 31.72  ? 41  PRO C C   1 
ATOM   1734 O O   . PRO C 1 42 ? 19.580  -30.786 28.743  1.00 32.62  ? 41  PRO C O   1 
ATOM   1735 C CB  . PRO C 1 42 ? 18.851  -32.840 30.882  1.00 35.36  ? 41  PRO C CB  1 
ATOM   1736 C CG  . PRO C 1 42 ? 19.562  -31.932 31.853  1.00 39.77  ? 41  PRO C CG  1 
ATOM   1737 C CD  . PRO C 1 42 ? 21.019  -31.716 31.492  1.00 40.03  ? 41  PRO C CD  1 
ATOM   1738 N N   . ILE C 1 43 ? 19.277  -32.649 27.423  1.00 30.60  ? 42  ILE C N   1 
ATOM   1739 C CA  . ILE C 1 43 ? 18.968  -31.879 26.218  1.00 28.93  ? 42  ILE C CA  1 
ATOM   1740 C C   . ILE C 1 43 ? 17.545  -32.158 25.772  1.00 28.99  ? 42  ILE C C   1 
ATOM   1741 O O   . ILE C 1 43 ? 17.064  -33.298 25.778  1.00 33.20  ? 42  ILE C O   1 
ATOM   1742 C CB  . ILE C 1 43 ? 19.948  -32.297 25.112  1.00 27.92  ? 42  ILE C CB  1 
ATOM   1743 C CG1 . ILE C 1 43 ? 21.427  -32.135 25.528  1.00 29.45  ? 42  ILE C CG1 1 
ATOM   1744 C CG2 . ILE C 1 43 ? 19.599  -31.559 23.808  1.00 31.67  ? 42  ILE C CG2 1 
ATOM   1745 C CD1 . ILE C 1 43 ? 21.835  -30.711 25.880  1.00 30.53  ? 42  ILE C CD1 1 
ATOM   1746 N N   . PHE C 1 44 ? 16.866  -31.102 25.286  1.00 31.33  ? 43  PHE C N   1 
ATOM   1747 C CA  . PHE C 1 44 ? 15.571  -31.303 24.661  1.00 30.48  ? 43  PHE C CA  1 
ATOM   1748 C C   . PHE C 1 44 ? 15.711  -30.832 23.214  1.00 27.47  ? 43  PHE C C   1 
ATOM   1749 O O   . PHE C 1 44 ? 16.244  -29.729 22.982  1.00 30.55  ? 43  PHE C O   1 
ATOM   1750 C CB  . PHE C 1 44 ? 14.554  -30.352 25.308  1.00 34.22  ? 43  PHE C CB  1 
ATOM   1751 C CG  . PHE C 1 44 ? 13.167  -30.259 24.678  1.00 33.20  ? 43  PHE C CG  1 
ATOM   1752 C CD1 . PHE C 1 44 ? 12.176  -31.213 24.952  1.00 36.29  ? 43  PHE C CD1 1 
ATOM   1753 C CD2 . PHE C 1 44 ? 12.857  -29.202 23.810  1.00 36.66  ? 43  PHE C CD2 1 
ATOM   1754 C CE1 . PHE C 1 44 ? 10.906  -31.124 24.368  1.00 38.81  ? 43  PHE C CE1 1 
ATOM   1755 C CE2 . PHE C 1 44 ? 11.590  -29.112 23.228  1.00 35.49  ? 43  PHE C CE2 1 
ATOM   1756 C CZ  . PHE C 1 44 ? 10.623  -30.062 23.515  1.00 42.16  ? 43  PHE C CZ  1 
ATOM   1757 N N   . PHE C 1 45 ? 15.258  -31.695 22.304  1.00 27.98  ? 44  PHE C N   1 
ATOM   1758 C CA  . PHE C 1 45 ? 15.417  -31.480 20.869  1.00 30.17  ? 44  PHE C CA  1 
ATOM   1759 C C   . PHE C 1 45 ? 14.156  -30.823 20.327  1.00 29.50  ? 44  PHE C C   1 
ATOM   1760 O O   . PHE C 1 45 ? 13.034  -31.332 20.466  1.00 30.95  ? 44  PHE C O   1 
ATOM   1761 C CB  . PHE C 1 45 ? 15.747  -32.768 20.125  1.00 27.69  ? 44  PHE C CB  1 
ATOM   1762 C CG  . PHE C 1 45 ? 17.112  -33.324 20.461  1.00 27.99  ? 44  PHE C CG  1 
ATOM   1763 C CD1 . PHE C 1 45 ? 18.234  -32.940 19.735  1.00 27.05  ? 44  PHE C CD1 1 
ATOM   1764 C CD2 . PHE C 1 45 ? 17.251  -34.258 21.491  1.00 28.92  ? 44  PHE C CD2 1 
ATOM   1765 C CE1 . PHE C 1 45 ? 19.498  -33.451 20.036  1.00 32.13  ? 44  PHE C CE1 1 
ATOM   1766 C CE2 . PHE C 1 45 ? 18.520  -34.781 21.769  1.00 30.41  ? 44  PHE C CE2 1 
ATOM   1767 C CZ  . PHE C 1 45 ? 19.629  -34.380 21.053  1.00 30.01  ? 44  PHE C CZ  1 
ATOM   1768 N N   . PHE C 1 46 ? 14.336  -29.638 19.722  1.00 29.34  ? 45  PHE C N   1 
ATOM   1769 C CA  . PHE C 1 46 ? 13.164  -29.073 19.067  1.00 27.44  ? 45  PHE C CA  1 
ATOM   1770 C C   . PHE C 1 46 ? 12.699  -29.911 17.880  1.00 29.43  ? 45  PHE C C   1 
ATOM   1771 O O   . PHE C 1 46 ? 13.456  -30.666 17.258  1.00 28.42  ? 45  PHE C O   1 
ATOM   1772 C CB  . PHE C 1 46 ? 13.450  -27.633 18.628  1.00 27.40  ? 45  PHE C CB  1 
ATOM   1773 C CG  . PHE C 1 46 ? 13.684  -26.627 19.739  1.00 28.96  ? 45  PHE C CG  1 
ATOM   1774 C CD1 . PHE C 1 46 ? 12.622  -26.191 20.531  1.00 30.51  ? 45  PHE C CD1 1 
ATOM   1775 C CD2 . PHE C 1 46 ? 14.965  -26.129 19.966  1.00 28.56  ? 45  PHE C CD2 1 
ATOM   1776 C CE1 . PHE C 1 46 ? 12.874  -25.249 21.534  1.00 31.65  ? 45  PHE C CE1 1 
ATOM   1777 C CE2 . PHE C 1 46 ? 15.216  -25.226 21.000  1.00 33.03  ? 45  PHE C CE2 1 
ATOM   1778 C CZ  . PHE C 1 46 ? 14.156  -24.771 21.763  1.00 30.67  ? 45  PHE C CZ  1 
ATOM   1779 N N   . GLY C 1 47 ? 11.413  -29.771 17.542  1.00 27.80  ? 46  GLY C N   1 
ATOM   1780 C CA  . GLY C 1 47 ? 10.870  -30.473 16.394  1.00 31.74  ? 46  GLY C CA  1 
ATOM   1781 C C   . GLY C 1 47 ? 10.443  -31.894 16.763  1.00 35.68  ? 46  GLY C C   1 
ATOM   1782 O O   . GLY C 1 47 ? 9.269   -32.254 16.668  1.00 37.87  ? 46  GLY C O   1 
ATOM   1783 N N   . THR C 1 48 ? 11.416  -32.742 17.142  1.00 31.33  ? 47  THR C N   1 
ATOM   1784 C CA  . THR C 1 48 ? 11.053  -34.083 17.589  1.00 31.92  ? 47  THR C CA  1 
ATOM   1785 C C   . THR C 1 48 ? 10.513  -34.055 19.024  1.00 34.73  ? 47  THR C C   1 
ATOM   1786 O O   . THR C 1 48 ? 9.764   -34.961 19.402  1.00 39.81  ? 47  THR C O   1 
ATOM   1787 C CB  . THR C 1 48 ? 12.276  -34.983 17.509  1.00 29.53  ? 47  THR C CB  1 
ATOM   1788 O OG1 . THR C 1 48 ? 13.119  -34.385 18.504  1.00 33.02  ? 47  THR C OG1 1 
ATOM   1789 C CG2 . THR C 1 48 ? 12.834  -35.091 16.101  1.00 31.24  ? 47  THR C CG2 1 
ATOM   1790 N N   . HIS C 1 49 ? 10.863  -33.035 19.804  1.00 32.16  ? 48  HIS C N   1 
ATOM   1791 C CA  . HIS C 1 49 ? 10.541  -32.937 21.225  1.00 36.24  ? 48  HIS C CA  1 
ATOM   1792 C C   . HIS C 1 49 ? 11.014  -34.154 22.029  1.00 35.29  ? 48  HIS C C   1 
ATOM   1793 O O   . HIS C 1 49 ? 10.415  -34.479 23.065  1.00 42.48  ? 48  HIS C O   1 
ATOM   1794 C CB  . HIS C 1 49 ? 9.029   -32.744 21.412  1.00 33.78  ? 48  HIS C CB  1 
ATOM   1795 C CG  . HIS C 1 49 ? 8.491   -31.635 20.566  1.00 37.60  ? 48  HIS C CG  1 
ATOM   1796 N ND1 . HIS C 1 49 ? 7.278   -31.768 19.921  1.00 43.68  ? 48  HIS C ND1 1 
ATOM   1797 C CD2 . HIS C 1 49 ? 8.970   -30.429 20.237  1.00 37.61  ? 48  HIS C CD2 1 
ATOM   1798 C CE1 . HIS C 1 49 ? 7.035   -30.666 19.221  1.00 44.94  ? 48  HIS C CE1 1 
ATOM   1799 N NE2 . HIS C 1 49 ? 8.056   -29.847 19.385  1.00 43.35  ? 48  HIS C NE2 1 
ATOM   1800 N N   . GLU C 1 50 ? 12.123  -34.775 21.611  1.00 35.42  ? 49  GLU C N   1 
ATOM   1801 C CA  . GLU C 1 50 ? 12.704  -35.861 22.385  1.00 37.12  ? 49  GLU C CA  1 
ATOM   1802 C C   . GLU C 1 50 ? 13.806  -35.340 23.309  1.00 37.03  ? 49  GLU C C   1 
ATOM   1803 O O   . GLU C 1 50 ? 14.190  -34.176 23.250  1.00 34.77  ? 49  GLU C O   1 
ATOM   1804 C CB  . GLU C 1 50 ? 13.174  -36.944 21.424  1.00 35.67  ? 49  GLU C CB  1 
ATOM   1805 C CG  . GLU C 1 50 ? 12.037  -37.544 20.593  1.00 40.28  ? 49  GLU C CG  1 
ATOM   1806 C CD  . GLU C 1 50 ? 12.601  -38.415 19.488  1.00 52.93  ? 49  GLU C CD  1 
ATOM   1807 O OE1 . GLU C 1 50 ? 13.846  -38.583 19.438  1.00 58.79  ? 49  GLU C OE1 1 
ATOM   1808 O OE2 . GLU C 1 50 ? 11.809  -38.900 18.654  1.00 58.84  ? 49  GLU C OE2 1 
ATOM   1809 N N   . THR C 1 51 ? 14.276  -36.203 24.232  1.00 38.70  ? 50  THR C N   1 
ATOM   1810 C CA  . THR C 1 51 ? 15.350  -35.842 25.163  1.00 36.17  ? 50  THR C CA  1 
ATOM   1811 C C   . THR C 1 51 ? 16.467  -36.875 25.090  1.00 30.16  ? 50  THR C C   1 
ATOM   1812 O O   . THR C 1 51 ? 16.263  -38.024 24.685  1.00 35.05  ? 50  THR C O   1 
ATOM   1813 C CB  . THR C 1 51 ? 14.837  -35.727 26.602  1.00 38.13  ? 50  THR C CB  1 
ATOM   1814 O OG1 . THR C 1 51 ? 14.376  -37.053 26.867  1.00 40.51  ? 50  THR C OG1 1 
ATOM   1815 C CG2 . THR C 1 51 ? 13.796  -34.641 26.792  1.00 40.57  ? 50  THR C CG2 1 
ATOM   1816 N N   . ALA C 1 52 ? 17.675  -36.423 25.439  1.00 33.64  ? 51  ALA C N   1 
ATOM   1817 C CA  . ALA C 1 52 ? 18.864  -37.250 25.566  1.00 34.99  ? 51  ALA C CA  1 
ATOM   1818 C C   . ALA C 1 52 ? 19.803  -36.567 26.558  1.00 36.73  ? 51  ALA C C   1 
ATOM   1819 O O   . ALA C 1 52 ? 19.566  -35.435 26.960  1.00 36.18  ? 51  ALA C O   1 
ATOM   1820 C CB  . ALA C 1 52 ? 19.535  -37.431 24.228  1.00 35.78  ? 51  ALA C CB  1 
ATOM   1821 N N   . PHE C 1 53 ? 20.872  -37.266 26.977  1.00 35.20  ? 52  PHE C N   1 
ATOM   1822 C CA  . PHE C 1 53 ? 21.944  -36.648 27.754  1.00 34.66  ? 52  PHE C CA  1 
ATOM   1823 C C   . PHE C 1 53 ? 23.159  -36.529 26.844  1.00 34.19  ? 52  PHE C C   1 
ATOM   1824 O O   . PHE C 1 53 ? 23.514  -37.486 26.163  1.00 35.99  ? 52  PHE C O   1 
ATOM   1825 C CB  . PHE C 1 53 ? 22.339  -37.562 28.921  1.00 34.05  ? 52  PHE C CB  1 
ATOM   1826 C CG  . PHE C 1 53 ? 21.350  -37.497 30.064  1.00 32.62  ? 52  PHE C CG  1 
ATOM   1827 C CD1 . PHE C 1 53 ? 21.028  -36.301 30.683  1.00 35.79  ? 52  PHE C CD1 1 
ATOM   1828 C CD2 . PHE C 1 53 ? 20.684  -38.650 30.479  1.00 48.38  ? 52  PHE C CD2 1 
ATOM   1829 C CE1 . PHE C 1 53 ? 20.098  -36.253 31.717  1.00 41.89  ? 52  PHE C CE1 1 
ATOM   1830 C CE2 . PHE C 1 53 ? 19.741  -38.593 31.504  1.00 45.50  ? 52  PHE C CE2 1 
ATOM   1831 C CZ  . PHE C 1 53 ? 19.448  -37.394 32.117  1.00 44.14  ? 52  PHE C CZ  1 
ATOM   1832 N N   . LEU C 1 54 ? 23.815  -35.361 26.832  1.00 30.43  ? 53  LEU C N   1 
ATOM   1833 C CA  . LEU C 1 54 ? 24.972  -35.161 25.963  1.00 27.79  ? 53  LEU C CA  1 
ATOM   1834 C C   . LEU C 1 54 ? 26.075  -34.392 26.681  1.00 31.56  ? 53  LEU C C   1 
ATOM   1835 O O   . LEU C 1 54 ? 25.800  -33.570 27.538  1.00 32.59  ? 53  LEU C O   1 
ATOM   1836 C CB  . LEU C 1 54 ? 24.600  -34.405 24.679  1.00 30.50  ? 53  LEU C CB  1 
ATOM   1837 C CG  . LEU C 1 54 ? 23.702  -35.153 23.690  1.00 35.03  ? 53  LEU C CG  1 
ATOM   1838 C CD1 . LEU C 1 54 ? 23.492  -34.237 22.504  1.00 34.54  ? 53  LEU C CD1 1 
ATOM   1839 C CD2 . LEU C 1 54 ? 24.305  -36.497 23.221  1.00 40.71  ? 53  LEU C CD2 1 
ATOM   1840 N N   . GLY C 1 55 ? 27.322  -34.629 26.278  1.00 34.24  ? 54  GLY C N   1 
ATOM   1841 C CA  . GLY C 1 55 ? 28.441  -33.908 26.857  1.00 34.30  ? 54  GLY C CA  1 
ATOM   1842 C C   . GLY C 1 55 ? 28.720  -32.601 26.119  1.00 42.05  ? 54  GLY C C   1 
ATOM   1843 O O   . GLY C 1 55 ? 28.181  -32.324 25.037  1.00 37.41  ? 54  GLY C O   1 
ATOM   1844 N N   . PRO C 1 56 ? 29.561  -31.714 26.693  1.00 36.24  ? 55  PRO C N   1 
ATOM   1845 C CA  . PRO C 1 56 ? 29.797  -30.399 26.106  1.00 37.76  ? 55  PRO C CA  1 
ATOM   1846 C C   . PRO C 1 56 ? 30.467  -30.408 24.731  1.00 35.86  ? 55  PRO C C   1 
ATOM   1847 O O   . PRO C 1 56 ? 30.307  -29.454 23.963  1.00 47.61  ? 55  PRO C O   1 
ATOM   1848 C CB  . PRO C 1 56 ? 30.629  -29.634 27.201  1.00 43.18  ? 55  PRO C CB  1 
ATOM   1849 C CG  . PRO C 1 56 ? 31.224  -30.740 28.042  1.00 39.39  ? 55  PRO C CG  1 
ATOM   1850 C CD  . PRO C 1 56 ? 30.275  -31.918 27.970  1.00 40.10  ? 55  PRO C CD  1 
ATOM   1851 N N   . LYS C 1 57 ? 31.175  -31.494 24.411  1.00 43.95  ? 56  LYS C N   1 
ATOM   1852 C CA  . LYS C 1 57 ? 31.818  -31.591 23.108  1.00 46.45  ? 56  LYS C CA  1 
ATOM   1853 C C   . LYS C 1 57 ? 30.742  -31.618 22.023  1.00 47.35  ? 56  LYS C C   1 
ATOM   1854 O O   . LYS C 1 57 ? 31.013  -31.304 20.861  1.00 44.44  ? 56  LYS C O   1 
ATOM   1855 C CB  . LYS C 1 57 ? 32.668  -32.861 22.978  1.00 46.67  ? 56  LYS C CB  1 
ATOM   1856 N N   . ASP C 1 58 ? 29.522  -31.975 22.440  1.00 40.14  ? 57  ASP C N   1 
ATOM   1857 C CA  . ASP C 1 58 ? 28.441  -32.259 21.496  1.00 37.83  ? 57  ASP C CA  1 
ATOM   1858 C C   . ASP C 1 58 ? 27.509  -31.064 21.321  1.00 36.62  ? 57  ASP C C   1 
ATOM   1859 O O   . ASP C 1 58 ? 26.493  -31.178 20.612  1.00 34.16  ? 57  ASP C O   1 
ATOM   1860 C CB  . ASP C 1 58 ? 27.633  -33.455 21.961  1.00 37.28  ? 57  ASP C CB  1 
ATOM   1861 C CG  . ASP C 1 58 ? 28.398  -34.766 22.009  1.00 43.42  ? 57  ASP C CG  1 
ATOM   1862 O OD1 . ASP C 1 58 ? 29.392  -34.862 21.295  1.00 44.54  ? 57  ASP C OD1 1 
ATOM   1863 O OD2 . ASP C 1 58 ? 27.971  -35.673 22.737  1.00 51.62  ? 57  ASP C OD2 1 
ATOM   1864 N N   . LEU C 1 59 ? 27.824  -29.929 21.953  1.00 33.29  ? 58  LEU C N   1 
ATOM   1865 C CA  . LEU C 1 59 ? 26.908  -28.813 22.100  1.00 33.00  ? 58  LEU C CA  1 
ATOM   1866 C C   . LEU C 1 59 ? 27.504  -27.518 21.558  1.00 34.59  ? 58  LEU C C   1 
ATOM   1867 O O   . LEU C 1 59 ? 28.682  -27.267 21.803  1.00 42.16  ? 58  LEU C O   1 
ATOM   1868 C CB  . LEU C 1 59 ? 26.500  -28.634 23.566  1.00 32.51  ? 58  LEU C CB  1 
ATOM   1869 C CG  . LEU C 1 59 ? 25.946  -29.912 24.196  1.00 31.68  ? 58  LEU C CG  1 
ATOM   1870 C CD1 . LEU C 1 59 ? 25.738  -29.690 25.678  1.00 36.57  ? 58  LEU C CD1 1 
ATOM   1871 C CD2 . LEU C 1 59 ? 24.594  -30.286 23.548  1.00 29.54  ? 58  LEU C CD2 1 
ATOM   1872 N N   . PHE C 1 60 ? 26.678  -26.718 20.861  1.00 36.23  ? 59  PHE C N   1 
ATOM   1873 C CA  . PHE C 1 60 ? 27.159  -25.519 20.158  1.00 37.42  ? 59  PHE C CA  1 
ATOM   1874 C C   . PHE C 1 60 ? 26.194  -24.366 20.432  1.00 37.79  ? 59  PHE C C   1 
ATOM   1875 O O   . PHE C 1 60 ? 24.994  -24.476 20.188  1.00 34.38  ? 59  PHE C O   1 
ATOM   1876 C CB  . PHE C 1 60 ? 27.356  -25.753 18.647  1.00 34.52  ? 59  PHE C CB  1 
ATOM   1877 C CG  . PHE C 1 60 ? 28.306  -26.901 18.341  1.00 33.16  ? 59  PHE C CG  1 
ATOM   1878 C CD1 . PHE C 1 60 ? 27.867  -28.222 18.365  1.00 35.85  ? 59  PHE C CD1 1 
ATOM   1879 C CD2 . PHE C 1 60 ? 29.678  -26.683 18.150  1.00 40.07  ? 59  PHE C CD2 1 
ATOM   1880 C CE1 . PHE C 1 60 ? 28.743  -29.284 18.167  1.00 38.81  ? 59  PHE C CE1 1 
ATOM   1881 C CE2 . PHE C 1 60 ? 30.551  -27.748 17.922  1.00 37.14  ? 59  PHE C CE2 1 
ATOM   1882 C CZ  . PHE C 1 60 ? 30.086  -29.046 17.917  1.00 40.24  ? 59  PHE C CZ  1 
ATOM   1883 N N   . PRO C 1 61 ? 26.620  -23.201 20.985  1.00 38.31  ? 60  PRO C N   1 
ATOM   1884 C CA  . PRO C 1 61 ? 25.641  -22.160 21.309  1.00 38.28  ? 60  PRO C CA  1 
ATOM   1885 C C   . PRO C 1 61 ? 24.919  -21.661 20.059  1.00 35.15  ? 60  PRO C C   1 
ATOM   1886 O O   . PRO C 1 61 ? 25.524  -21.562 18.998  1.00 40.42  ? 60  PRO C O   1 
ATOM   1887 C CB  . PRO C 1 61 ? 26.400  -21.051 22.085  1.00 40.81  ? 60  PRO C CB  1 
ATOM   1888 C CG  . PRO C 1 61 ? 27.832  -21.532 22.093  1.00 41.36  ? 60  PRO C CG  1 
ATOM   1889 C CD  . PRO C 1 61 ? 28.004  -22.856 21.363  1.00 44.81  ? 60  PRO C CD  1 
ATOM   1890 N N   . TYR C 1 62 ? 23.592  -21.492 20.198  1.00 38.84  ? 61  TYR C N   1 
ATOM   1891 C CA  . TYR C 1 62 ? 22.656  -21.237 19.114  1.00 35.61  ? 61  TYR C CA  1 
ATOM   1892 C C   . TYR C 1 62 ? 23.055  -19.977 18.348  1.00 44.23  ? 61  TYR C C   1 
ATOM   1893 O O   . TYR C 1 62 ? 23.197  -20.019 17.123  1.00 45.40  ? 61  TYR C O   1 
ATOM   1894 C CB  . TYR C 1 62 ? 21.202  -21.126 19.566  1.00 42.04  ? 61  TYR C CB  1 
ATOM   1895 C CG  . TYR C 1 62 ? 20.276  -20.757 18.414  1.00 42.57  ? 61  TYR C CG  1 
ATOM   1896 C CD1 . TYR C 1 62 ? 20.099  -21.623 17.324  1.00 40.60  ? 61  TYR C CD1 1 
ATOM   1897 C CD2 . TYR C 1 62 ? 19.577  -19.552 18.426  1.00 44.06  ? 61  TYR C CD2 1 
ATOM   1898 C CE1 . TYR C 1 62 ? 19.253  -21.287 16.267  1.00 37.78  ? 61  TYR C CE1 1 
ATOM   1899 C CE2 . TYR C 1 62 ? 18.713  -19.223 17.389  1.00 43.42  ? 61  TYR C CE2 1 
ATOM   1900 C CZ  . TYR C 1 62 ? 18.570  -20.076 16.302  1.00 39.43  ? 61  TYR C CZ  1 
ATOM   1901 O OH  . TYR C 1 62 ? 17.736  -19.701 15.278  1.00 42.04  ? 61  TYR C OH  1 
ATOM   1902 N N   . ASP C 1 63 ? 23.275  -18.868 19.070  1.00 44.11  ? 62  ASP C N   1 
ATOM   1903 C CA  . ASP C 1 63 ? 23.559  -17.620 18.375  1.00 48.36  ? 62  ASP C CA  1 
ATOM   1904 C C   . ASP C 1 63 ? 24.878  -17.680 17.616  1.00 44.07  ? 62  ASP C C   1 
ATOM   1905 O O   . ASP C 1 63 ? 24.966  -17.138 16.513  1.00 47.26  ? 62  ASP C O   1 
ATOM   1906 C CB  . ASP C 1 63 ? 23.273  -16.394 19.225  1.00 46.53  ? 62  ASP C CB  1 
ATOM   1907 C CG  . ASP C 1 63 ? 21.788  -16.054 19.247  1.00 65.14  ? 62  ASP C CG  1 
ATOM   1908 O OD1 . ASP C 1 63 ? 21.245  -15.848 20.351  1.00 67.93  ? 62  ASP C OD1 1 
ATOM   1909 O OD2 . ASP C 1 63 ? 21.170  -16.044 18.149  1.00 66.21  ? 62  ASP C OD2 1 
ATOM   1910 N N   . LYS C 1 64 ? 25.873  -18.353 18.185  1.00 40.37  ? 63  LYS C N   1 
ATOM   1911 C CA  . LYS C 1 64 ? 27.208  -18.402 17.622  1.00 44.35  ? 63  LYS C CA  1 
ATOM   1912 C C   . LYS C 1 64 ? 27.263  -19.330 16.410  1.00 45.28  ? 63  LYS C C   1 
ATOM   1913 O O   . LYS C 1 64 ? 28.096  -19.125 15.532  1.00 41.00  ? 63  LYS C O   1 
ATOM   1914 C CB  . LYS C 1 64 ? 28.263  -18.787 18.673  1.00 48.78  ? 63  LYS C CB  1 
ATOM   1915 N N   . SER C 1 65 ? 26.372  -20.345 16.329  1.00 37.51  ? 64  SER C N   1 
ATOM   1916 C CA  . SER C 1 65 ? 26.619  -21.368 15.325  1.00 34.26  ? 64  SER C CA  1 
ATOM   1917 C C   . SER C 1 65 ? 25.482  -21.501 14.316  1.00 33.20  ? 64  SER C C   1 
ATOM   1918 O O   . SER C 1 65 ? 25.622  -22.309 13.398  1.00 33.54  ? 64  SER C O   1 
ATOM   1919 C CB  . SER C 1 65 ? 26.953  -22.714 15.945  1.00 38.75  ? 64  SER C CB  1 
ATOM   1920 O OG  . SER C 1 65 ? 25.813  -23.194 16.642  1.00 40.97  ? 64  SER C OG  1 
ATOM   1921 N N   . LYS C 1 66 ? 24.427  -20.686 14.471  1.00 33.78  ? 65  LYS C N   1 
ATOM   1922 C CA  . LYS C 1 66 ? 23.269  -20.826 13.591  1.00 35.77  ? 65  LYS C CA  1 
ATOM   1923 C C   . LYS C 1 66 ? 23.618  -20.507 12.140  1.00 37.37  ? 65  LYS C C   1 
ATOM   1924 O O   . LYS C 1 66 ? 23.054  -21.105 11.235  1.00 34.94  ? 65  LYS C O   1 
ATOM   1925 C CB  . LYS C 1 66 ? 22.051  -20.010 14.006  1.00 40.62  ? 65  LYS C CB  1 
ATOM   1926 C CG  . LYS C 1 66 ? 22.377  -18.534 14.093  1.00 33.63  ? 65  LYS C CG  1 
ATOM   1927 C CD  . LYS C 1 66 ? 21.077  -17.865 14.499  1.00 43.87  ? 65  LYS C CD  1 
ATOM   1928 C CE  . LYS C 1 66 ? 21.275  -16.414 14.751  1.00 45.60  ? 65  LYS C CE  1 
ATOM   1929 N NZ  . LYS C 1 66 ? 19.948  -15.940 15.117  1.00 49.83  ? 65  LYS C NZ  1 
ATOM   1930 N N   . ASP C 1 67 ? 24.577  -19.606 11.891  1.00 37.55  ? 66  ASP C N   1 
ATOM   1931 C CA  . ASP C 1 67 ? 24.940  -19.357 10.500  1.00 39.56  ? 66  ASP C CA  1 
ATOM   1932 C C   . ASP C 1 67 ? 25.353  -20.658 9.800   1.00 40.53  ? 66  ASP C C   1 
ATOM   1933 O O   . ASP C 1 67 ? 25.007  -20.876 8.639   1.00 39.37  ? 66  ASP C O   1 
ATOM   1934 C CB  . ASP C 1 67 ? 25.825  -18.117 10.341  1.00 40.37  ? 66  ASP C CB  1 
ATOM   1935 C CG  . ASP C 1 67 ? 27.271  -18.221 10.810  1.00 53.23  ? 66  ASP C CG  1 
ATOM   1936 O OD1 . ASP C 1 67 ? 27.715  -19.350 11.122  1.00 55.95  ? 66  ASP C OD1 1 
ATOM   1937 O OD2 . ASP C 1 67 ? 27.943  -17.157 10.882  1.00 53.08  ? 66  ASP C OD2 1 
ATOM   1938 N N   . LYS C 1 68 ? 26.008  -21.565 10.548  1.00 35.79  ? 67  LYS C N   1 
ATOM   1939 C CA  . LYS C 1 68 ? 26.508  -22.832 10.042  1.00 34.69  ? 67  LYS C CA  1 
ATOM   1940 C C   . LYS C 1 68 ? 25.473  -23.982 10.110  1.00 32.73  ? 67  LYS C C   1 
ATOM   1941 O O   . LYS C 1 68 ? 25.317  -24.756 9.157   1.00 36.07  ? 67  LYS C O   1 
ATOM   1942 C CB  . LYS C 1 68 ? 27.761  -23.113 10.870  1.00 35.59  ? 67  LYS C CB  1 
ATOM   1943 C CG  . LYS C 1 68 ? 28.553  -24.311 10.427  1.00 39.91  ? 67  LYS C CG  1 
ATOM   1944 C CD  . LYS C 1 68 ? 29.817  -24.410 11.290  1.00 46.89  ? 67  LYS C CD  1 
ATOM   1945 C CE  . LYS C 1 68 ? 30.627  -25.671 11.199  1.00 61.09  ? 67  LYS C CE  1 
ATOM   1946 N NZ  . LYS C 1 68 ? 30.887  -26.139 9.832   1.00 70.62  ? 67  LYS C NZ  1 
ATOM   1947 N N   . TYR C 1 69 ? 24.773  -24.123 11.243  1.00 33.48  ? 68  TYR C N   1 
ATOM   1948 C CA  . TYR C 1 69 ? 23.932  -25.307 11.406  1.00 30.78  ? 68  TYR C CA  1 
ATOM   1949 C C   . TYR C 1 69 ? 22.455  -24.982 11.203  1.00 32.46  ? 68  TYR C C   1 
ATOM   1950 O O   . TYR C 1 69 ? 21.662  -25.892 11.014  1.00 31.52  ? 68  TYR C O   1 
ATOM   1951 C CB  . TYR C 1 69 ? 24.117  -25.897 12.818  1.00 30.40  ? 68  TYR C CB  1 
ATOM   1952 C CG  . TYR C 1 69 ? 25.542  -26.355 13.105  1.00 28.56  ? 68  TYR C CG  1 
ATOM   1953 C CD1 . TYR C 1 69 ? 26.252  -27.140 12.200  1.00 33.13  ? 68  TYR C CD1 1 
ATOM   1954 C CD2 . TYR C 1 69 ? 26.162  -25.944 14.289  1.00 32.56  ? 68  TYR C CD2 1 
ATOM   1955 C CE1 . TYR C 1 69 ? 27.552  -27.551 12.466  1.00 32.76  ? 68  TYR C CE1 1 
ATOM   1956 C CE2 . TYR C 1 69 ? 27.455  -26.364 14.564  1.00 32.36  ? 68  TYR C CE2 1 
ATOM   1957 C CZ  . TYR C 1 69 ? 28.140  -27.149 13.652  1.00 34.32  ? 68  TYR C CZ  1 
ATOM   1958 O OH  . TYR C 1 69 ? 29.432  -27.521 13.963  1.00 39.16  ? 68  TYR C OH  1 
ATOM   1959 N N   . GLY C 1 70 ? 22.087  -23.698 11.240  1.00 30.78  ? 69  GLY C N   1 
ATOM   1960 C CA  . GLY C 1 70 ? 20.671  -23.359 11.160  1.00 29.50  ? 69  GLY C CA  1 
ATOM   1961 C C   . GLY C 1 70 ? 20.234  -23.220 9.703   1.00 32.43  ? 69  GLY C C   1 
ATOM   1962 O O   . GLY C 1 70 ? 20.167  -22.122 9.147   1.00 32.96  ? 69  GLY C O   1 
ATOM   1963 N N   . LYS C 1 71 ? 20.079  -24.363 9.058   1.00 29.70  ? 70  LYS C N   1 
ATOM   1964 C CA  . LYS C 1 71 ? 19.720  -24.416 7.652   1.00 32.58  ? 70  LYS C CA  1 
ATOM   1965 C C   . LYS C 1 71 ? 18.887  -25.667 7.504   1.00 32.96  ? 70  LYS C C   1 
ATOM   1966 O O   . LYS C 1 71 ? 19.035  -26.642 8.247   1.00 32.08  ? 70  LYS C O   1 
ATOM   1967 C CB  . LYS C 1 71 ? 20.922  -24.561 6.709   1.00 33.57  ? 70  LYS C CB  1 
ATOM   1968 C CG  . LYS C 1 71 ? 21.953  -25.544 7.189   1.00 38.71  ? 70  LYS C CG  1 
ATOM   1969 C CD  . LYS C 1 71 ? 23.097  -25.980 6.281   1.00 45.29  ? 70  LYS C CD  1 
ATOM   1970 C CE  . LYS C 1 71 ? 23.673  -27.200 6.930   1.00 47.79  ? 70  LYS C CE  1 
ATOM   1971 N N   . PRO C 1 72 ? 17.907  -25.671 6.589   1.00 27.64  ? 71  PRO C N   1 
ATOM   1972 C CA  . PRO C 1 72 ? 16.981  -26.797 6.547   1.00 25.80  ? 71  PRO C CA  1 
ATOM   1973 C C   . PRO C 1 72 ? 17.645  -28.116 6.195   1.00 27.59  ? 71  PRO C C   1 
ATOM   1974 O O   . PRO C 1 72 ? 18.630  -28.164 5.457   1.00 33.43  ? 71  PRO C O   1 
ATOM   1975 C CB  . PRO C 1 72 ? 16.054  -26.355 5.420   1.00 28.48  ? 71  PRO C CB  1 
ATOM   1976 C CG  . PRO C 1 72 ? 16.108  -24.843 5.498   1.00 29.59  ? 71  PRO C CG  1 
ATOM   1977 C CD  . PRO C 1 72 ? 17.562  -24.533 5.711   1.00 27.60  ? 71  PRO C CD  1 
ATOM   1978 N N   . ASN C 1 73 ? 16.959  -29.150 6.630   1.00 30.35  ? 72  ASN C N   1 
ATOM   1979 C CA  . ASN C 1 73 ? 17.272  -30.436 6.045   1.00 36.08  ? 72  ASN C CA  1 
ATOM   1980 C C   . ASN C 1 73 ? 16.035  -31.310 6.149   1.00 30.90  ? 72  ASN C C   1 
ATOM   1981 O O   . ASN C 1 73 ? 15.095  -30.996 6.856   1.00 31.80  ? 72  ASN C O   1 
ATOM   1982 C CB  . ASN C 1 73 ? 18.631  -31.004 6.440   1.00 44.68  ? 72  ASN C CB  1 
ATOM   1983 C CG  . ASN C 1 73 ? 18.573  -31.674 7.786   1.00 41.78  ? 72  ASN C CG  1 
ATOM   1984 O OD1 . ASN C 1 73 ? 17.894  -32.695 7.955   1.00 42.25  ? 72  ASN C OD1 1 
ATOM   1985 N ND2 . ASN C 1 73 ? 19.319  -31.138 8.727   1.00 47.83  ? 72  ASN C ND2 1 
ATOM   1986 N N   . LYS C 1 74 ? 16.107  -32.461 5.487   1.00 32.29  ? 73  LYS C N   1 
ATOM   1987 C CA  . LYS C 1 74 ? 14.898  -33.244 5.275   1.00 30.95  ? 73  LYS C CA  1 
ATOM   1988 C C   . LYS C 1 74 ? 14.646  -34.231 6.408   1.00 31.60  ? 73  LYS C C   1 
ATOM   1989 O O   . LYS C 1 74 ? 13.592  -34.863 6.448   1.00 32.72  ? 73  LYS C O   1 
ATOM   1990 C CB  . LYS C 1 74 ? 15.087  -34.029 3.973   1.00 35.65  ? 73  LYS C CB  1 
ATOM   1991 C CG  . LYS C 1 74 ? 15.496  -33.161 2.788   1.00 43.21  ? 73  LYS C CG  1 
ATOM   1992 C CD  . LYS C 1 74 ? 14.195  -32.445 2.444   1.00 43.50  ? 73  LYS C CD  1 
ATOM   1993 N N   . ARG C 1 75 ? 15.543  -34.296 7.402   1.00 27.50  ? 74  ARG C N   1 
ATOM   1994 C CA  . ARG C 1 75 ? 15.323  -35.252 8.482   1.00 27.53  ? 74  ARG C CA  1 
ATOM   1995 C C   . ARG C 1 75 ? 14.051  -34.941 9.278   1.00 29.85  ? 74  ARG C C   1 
ATOM   1996 O O   . ARG C 1 75 ? 13.640  -33.781 9.485   1.00 29.89  ? 74  ARG C O   1 
ATOM   1997 C CB  . ARG C 1 75 ? 16.573  -35.333 9.393   1.00 31.12  ? 74  ARG C CB  1 
ATOM   1998 C CG  . ARG C 1 75 ? 17.946  -35.576 8.761   1.00 35.31  ? 74  ARG C CG  1 
ATOM   1999 C CD  . ARG C 1 75 ? 18.242  -36.992 8.227   1.00 39.80  ? 74  ARG C CD  1 
ATOM   2000 N NE  . ARG C 1 75 ? 18.088  -37.912 9.352   1.00 35.68  ? 74  ARG C NE  1 
ATOM   2001 C CZ  . ARG C 1 75 ? 19.158  -38.394 10.011  1.00 34.86  ? 74  ARG C CZ  1 
ATOM   2002 N NH1 . ARG C 1 75 ? 18.962  -38.985 11.175  1.00 39.94  ? 74  ARG C NH1 1 
ATOM   2003 N NH2 . ARG C 1 75 ? 20.346  -38.139 9.495   1.00 34.58  ? 74  ARG C NH2 1 
ATOM   2004 N N   . LYS C 1 76 ? 13.416  -36.016 9.752   1.00 31.80  ? 75  LYS C N   1 
ATOM   2005 C CA  . LYS C 1 76 ? 12.116  -35.919 10.398  1.00 33.17  ? 75  LYS C CA  1 
ATOM   2006 C C   . LYS C 1 76 ? 12.164  -34.948 11.573  1.00 32.13  ? 75  LYS C C   1 
ATOM   2007 O O   . LYS C 1 76 ? 12.979  -35.086 12.498  1.00 30.26  ? 75  LYS C O   1 
ATOM   2008 C CB  . LYS C 1 76 ? 11.529  -37.286 10.783  1.00 34.75  ? 75  LYS C CB  1 
ATOM   2009 C CG  . LYS C 1 76 ? 10.062  -37.177 11.203  1.00 40.84  ? 75  LYS C CG  1 
ATOM   2010 C CD  . LYS C 1 76 ? 9.401   -38.428 11.787  1.00 52.95  ? 75  LYS C CD  1 
ATOM   2011 N N   . GLY C 1 77 ? 11.311  -33.913 11.489  1.00 32.74  ? 76  GLY C N   1 
ATOM   2012 C CA  . GLY C 1 77 ? 11.104  -33.002 12.605  1.00 28.44  ? 76  GLY C CA  1 
ATOM   2013 C C   . GLY C 1 77 ? 12.086  -31.820 12.574  1.00 27.72  ? 76  GLY C C   1 
ATOM   2014 O O   . GLY C 1 77 ? 11.942  -30.895 13.357  1.00 31.66  ? 76  GLY C O   1 
ATOM   2015 N N   . PHE C 1 78 ? 13.063  -31.821 11.662  1.00 28.08  ? 77  PHE C N   1 
ATOM   2016 C CA  . PHE C 1 78 ? 14.158  -30.862 11.753  1.00 28.14  ? 77  PHE C CA  1 
ATOM   2017 C C   . PHE C 1 78 ? 13.684  -29.426 11.480  1.00 29.27  ? 77  PHE C C   1 
ATOM   2018 O O   . PHE C 1 78 ? 14.020  -28.487 12.203  1.00 28.22  ? 77  PHE C O   1 
ATOM   2019 C CB  . PHE C 1 78 ? 15.241  -31.280 10.758  1.00 30.22  ? 77  PHE C CB  1 
ATOM   2020 C CG  . PHE C 1 78 ? 16.516  -30.496 10.998  1.00 26.38  ? 77  PHE C CG  1 
ATOM   2021 C CD1 . PHE C 1 78 ? 16.674  -29.219 10.465  1.00 29.51  ? 77  PHE C CD1 1 
ATOM   2022 C CD2 . PHE C 1 78 ? 17.541  -31.032 11.780  1.00 26.59  ? 77  PHE C CD2 1 
ATOM   2023 C CE1 . PHE C 1 78 ? 17.851  -28.520 10.706  1.00 28.25  ? 77  PHE C CE1 1 
ATOM   2024 C CE2 . PHE C 1 78 ? 18.704  -30.312 12.007  1.00 27.17  ? 77  PHE C CE2 1 
ATOM   2025 C CZ  . PHE C 1 78 ? 18.864  -29.047 11.492  1.00 27.55  ? 77  PHE C CZ  1 
ATOM   2026 N N   . ASN C 1 79 ? 12.910  -29.267 10.392  1.00 28.87  ? 78  ASN C N   1 
ATOM   2027 C CA  . ASN C 1 79 ? 12.555  -27.910 9.997   1.00 30.15  ? 78  ASN C CA  1 
ATOM   2028 C C   . ASN C 1 79 ? 11.544  -27.305 10.960  1.00 29.22  ? 78  ASN C C   1 
ATOM   2029 O O   . ASN C 1 79 ? 11.582  -26.108 11.284  1.00 29.53  ? 78  ASN C O   1 
ATOM   2030 C CB  . ASN C 1 79 ? 12.042  -27.909 8.569   1.00 27.62  ? 78  ASN C CB  1 
ATOM   2031 C CG  . ASN C 1 79 ? 13.151  -28.276 7.612   1.00 28.25  ? 78  ASN C CG  1 
ATOM   2032 O OD1 . ASN C 1 79 ? 14.328  -27.987 7.877   1.00 27.11  ? 78  ASN C OD1 1 
ATOM   2033 N ND2 . ASN C 1 79 ? 12.804  -28.830 6.456   1.00 28.66  ? 78  ASN C ND2 1 
ATOM   2034 N N   . GLU C 1 80 ? 10.674  -28.154 11.483  1.00 29.26  ? 79  GLU C N   1 
ATOM   2035 C CA  . GLU C 1 80 ? 9.817   -27.637 12.540  1.00 28.13  ? 79  GLU C CA  1 
ATOM   2036 C C   . GLU C 1 80 ? 10.649  -27.209 13.753  1.00 33.35  ? 79  GLU C C   1 
ATOM   2037 O O   . GLU C 1 80 ? 10.346  -26.204 14.401  1.00 32.06  ? 79  GLU C O   1 
ATOM   2038 C CB  . GLU C 1 80 ? 8.715   -28.662 12.810  1.00 35.80  ? 79  GLU C CB  1 
ATOM   2039 C CG  . GLU C 1 80 ? 7.832   -28.282 13.990  1.00 32.68  ? 79  GLU C CG  1 
ATOM   2040 C CD  . GLU C 1 80 ? 6.570   -29.101 14.132  1.00 47.94  ? 79  GLU C CD  1 
ATOM   2041 O OE1 . GLU C 1 80 ? 6.461   -30.225 13.601  1.00 50.90  ? 79  GLU C OE1 1 
ATOM   2042 O OE2 . GLU C 1 80 ? 5.653   -28.575 14.762  1.00 45.82  ? 79  GLU C OE2 1 
ATOM   2043 N N   . GLY C 1 81 ? 11.711  -28.000 14.064  1.00 28.56  ? 80  GLY C N   1 
ATOM   2044 C CA  . GLY C 1 81 ? 12.659  -27.627 15.103  1.00 28.78  ? 80  GLY C CA  1 
ATOM   2045 C C   . GLY C 1 81 ? 13.267  -26.247 14.868  1.00 29.75  ? 80  GLY C C   1 
ATOM   2046 O O   . GLY C 1 81 ? 13.456  -25.495 15.811  1.00 29.59  ? 80  GLY C O   1 
ATOM   2047 N N   . LEU C 1 82 ? 13.689  -25.980 13.615  1.00 29.57  ? 81  LEU C N   1 
ATOM   2048 C CA  . LEU C 1 82 ? 14.295  -24.691 13.283  1.00 30.53  ? 81  LEU C CA  1 
ATOM   2049 C C   . LEU C 1 82 ? 13.280  -23.581 13.543  1.00 28.71  ? 81  LEU C C   1 
ATOM   2050 O O   . LEU C 1 82 ? 13.667  -22.500 14.002  1.00 31.47  ? 81  LEU C O   1 
ATOM   2051 C CB  . LEU C 1 82 ? 14.741  -24.673 11.819  1.00 29.38  ? 81  LEU C CB  1 
ATOM   2052 C CG  . LEU C 1 82 ? 16.006  -25.461 11.451  1.00 27.11  ? 81  LEU C CG  1 
ATOM   2053 C CD1 . LEU C 1 82 ? 16.265  -25.336 9.972   1.00 25.97  ? 81  LEU C CD1 1 
ATOM   2054 C CD2 . LEU C 1 82 ? 17.267  -25.058 12.205  1.00 25.67  ? 81  LEU C CD2 1 
ATOM   2055 N N   . TRP C 1 83 ? 12.007  -23.871 13.250  1.00 26.53  ? 82  TRP C N   1 
ATOM   2056 C CA  . TRP C 1 83 ? 11.003  -22.834 13.465  1.00 34.69  ? 82  TRP C CA  1 
ATOM   2057 C C   . TRP C 1 83 ? 10.903  -22.572 14.977  1.00 35.47  ? 82  TRP C C   1 
ATOM   2058 O O   . TRP C 1 83 ? 10.962  -21.412 15.418  1.00 34.06  ? 82  TRP C O   1 
ATOM   2059 C CB  . TRP C 1 83 ? 9.649   -23.190 12.825  1.00 33.08  ? 82  TRP C CB  1 
ATOM   2060 C CG  . TRP C 1 83 ? 8.662   -22.062 12.989  1.00 34.96  ? 82  TRP C CG  1 
ATOM   2061 C CD1 . TRP C 1 83 ? 8.515   -20.992 12.144  1.00 37.29  ? 82  TRP C CD1 1 
ATOM   2062 C CD2 . TRP C 1 83 ? 7.780   -21.815 14.108  1.00 38.88  ? 82  TRP C CD2 1 
ATOM   2063 N NE1 . TRP C 1 83 ? 7.565   -20.136 12.629  1.00 35.97  ? 82  TRP C NE1 1 
ATOM   2064 C CE2 . TRP C 1 83 ? 7.091   -20.609 13.823  1.00 38.08  ? 82  TRP C CE2 1 
ATOM   2065 C CE3 . TRP C 1 83 ? 7.479   -22.512 15.291  1.00 38.18  ? 82  TRP C CE3 1 
ATOM   2066 C CZ2 . TRP C 1 83 ? 6.151   -20.078 14.702  1.00 44.93  ? 82  TRP C CZ2 1 
ATOM   2067 C CZ3 . TRP C 1 83 ? 6.547   -21.986 16.161  1.00 46.16  ? 82  TRP C CZ3 1 
ATOM   2068 C CH2 . TRP C 1 83 ? 5.921   -20.770 15.879  1.00 43.19  ? 82  TRP C CH2 1 
ATOM   2069 N N   . GLU C 1 84 ? 10.831  -23.659 15.773  1.00 31.48  ? 83  GLU C N   1 
ATOM   2070 C CA  . GLU C 1 84 ? 10.696  -23.507 17.220  1.00 34.26  ? 83  GLU C CA  1 
ATOM   2071 C C   . GLU C 1 84 ? 11.853  -22.735 17.869  1.00 34.94  ? 83  GLU C C   1 
ATOM   2072 O O   . GLU C 1 84 ? 11.620  -21.864 18.730  1.00 38.16  ? 83  GLU C O   1 
ATOM   2073 C CB  . GLU C 1 84 ? 10.510  -24.868 17.892  1.00 30.96  ? 83  GLU C CB  1 
ATOM   2074 C CG  . GLU C 1 84 ? 9.224   -25.567 17.470  1.00 34.68  ? 83  GLU C CG  1 
ATOM   2075 C CD  . GLU C 1 84 ? 9.140   -26.981 17.974  1.00 37.48  ? 83  GLU C CD  1 
ATOM   2076 O OE1 . GLU C 1 84 ? 10.125  -27.409 18.648  1.00 37.08  ? 83  GLU C OE1 1 
ATOM   2077 O OE2 . GLU C 1 84 ? 8.127   -27.651 17.657  1.00 40.29  ? 83  GLU C OE2 1 
ATOM   2078 N N   . ILE C 1 85 ? 13.108  -23.013 17.476  1.00 31.47  ? 84  ILE C N   1 
ATOM   2079 C CA  . ILE C 1 85 ? 14.280  -22.423 18.117  1.00 33.48  ? 84  ILE C CA  1 
ATOM   2080 C C   . ILE C 1 85 ? 14.389  -20.914 17.847  1.00 35.91  ? 84  ILE C C   1 
ATOM   2081 O O   . ILE C 1 85 ? 14.832  -20.157 18.710  1.00 34.71  ? 84  ILE C O   1 
ATOM   2082 C CB  . ILE C 1 85 ? 15.576  -23.178 17.796  1.00 32.87  ? 84  ILE C CB  1 
ATOM   2083 C CG1 . ILE C 1 85 ? 16.682  -22.806 18.797  1.00 33.12  ? 84  ILE C CG1 1 
ATOM   2084 C CG2 . ILE C 1 85 ? 15.999  -22.974 16.332  1.00 32.30  ? 84  ILE C CG2 1 
ATOM   2085 C CD1 . ILE C 1 85 ? 17.856  -23.780 18.881  1.00 30.52  ? 84  ILE C CD1 1 
ATOM   2086 N N   . GLN C 1 86 ? 13.947  -20.490 16.655  1.00 30.58  ? 85  GLN C N   1 
ATOM   2087 C CA  . GLN C 1 86 ? 13.950  -19.064 16.346  1.00 33.97  ? 85  GLN C CA  1 
ATOM   2088 C C   . GLN C 1 86 ? 12.699  -18.327 16.833  1.00 34.45  ? 85  GLN C C   1 
ATOM   2089 O O   . GLN C 1 86 ? 12.815  -17.144 17.155  1.00 39.66  ? 85  GLN C O   1 
ATOM   2090 C CB  . GLN C 1 86 ? 14.069  -18.961 14.824  1.00 33.23  ? 85  GLN C CB  1 
ATOM   2091 C CG  . GLN C 1 86 ? 14.153  -17.528 14.298  1.00 32.53  ? 85  GLN C CG  1 
ATOM   2092 C CD  . GLN C 1 86 ? 14.584  -17.494 12.841  1.00 35.84  ? 85  GLN C CD  1 
ATOM   2093 O OE1 . GLN C 1 86 ? 14.504  -18.491 12.103  1.00 37.27  ? 85  GLN C OE1 1 
ATOM   2094 N NE2 . GLN C 1 86 ? 15.112  -16.362 12.407  1.00 36.86  ? 85  GLN C NE2 1 
ATOM   2095 N N   . ASN C 1 87 ? 11.540  -18.982 16.863  1.00 34.70  ? 86  ASN C N   1 
ATOM   2096 C CA  . ASN C 1 87 ? 10.250  -18.322 17.055  1.00 39.02  ? 86  ASN C CA  1 
ATOM   2097 C C   . ASN C 1 87 ? 9.666   -18.561 18.450  1.00 43.48  ? 86  ASN C C   1 
ATOM   2098 O O   . ASN C 1 87 ? 9.093   -17.635 19.016  1.00 44.88  ? 86  ASN C O   1 
ATOM   2099 C CB  . ASN C 1 87 ? 9.262   -18.597 15.921  1.00 38.72  ? 86  ASN C CB  1 
ATOM   2100 C CG  . ASN C 1 87 ? 9.797   -17.993 14.647  1.00 39.37  ? 86  ASN C CG  1 
ATOM   2101 O OD1 . ASN C 1 87 ? 9.801   -16.764 14.524  1.00 41.64  ? 86  ASN C OD1 1 
ATOM   2102 N ND2 . ASN C 1 87 ? 10.312  -18.816 13.739  1.00 34.55  ? 86  ASN C ND2 1 
ATOM   2103 N N   . ASN C 1 88 ? 9.775   -19.785 18.998  1.00 42.11  ? 87  ASN C N   1 
ATOM   2104 C CA  . ASN C 1 88 ? 9.073   -20.134 20.235  1.00 40.18  ? 87  ASN C CA  1 
ATOM   2105 C C   . ASN C 1 88 ? 9.963   -20.999 21.135  1.00 40.77  ? 87  ASN C C   1 
ATOM   2106 O O   . ASN C 1 88 ? 9.538   -22.096 21.531  1.00 45.34  ? 87  ASN C O   1 
ATOM   2107 C CB  . ASN C 1 88 ? 7.774   -20.884 19.946  1.00 46.41  ? 87  ASN C CB  1 
ATOM   2108 C CG  . ASN C 1 88 ? 6.796   -20.820 21.100  1.00 49.51  ? 87  ASN C CG  1 
ATOM   2109 O OD1 . ASN C 1 88 ? 7.024   -20.091 22.073  1.00 53.64  ? 87  ASN C OD1 1 
ATOM   2110 N ND2 . ASN C 1 88 ? 5.701   -21.558 21.001  1.00 53.75  ? 87  ASN C ND2 1 
ATOM   2111 N N   . PRO C 1 89 ? 11.200  -20.552 21.456  1.00 37.90  ? 88  PRO C N   1 
ATOM   2112 C CA  . PRO C 1 89 ? 12.222  -21.429 22.051  1.00 39.29  ? 88  PRO C CA  1 
ATOM   2113 C C   . PRO C 1 89 ? 12.012  -21.893 23.490  1.00 44.59  ? 88  PRO C C   1 
ATOM   2114 O O   . PRO C 1 89 ? 12.730  -22.787 23.960  1.00 40.54  ? 88  PRO C O   1 
ATOM   2115 C CB  . PRO C 1 89 ? 13.527  -20.659 21.908  1.00 37.89  ? 88  PRO C CB  1 
ATOM   2116 C CG  . PRO C 1 89 ? 13.065  -19.206 21.883  1.00 43.46  ? 88  PRO C CG  1 
ATOM   2117 C CD  . PRO C 1 89 ? 11.762  -19.239 21.102  1.00 38.89  ? 88  PRO C CD  1 
ATOM   2118 N N   . HIS C 1 90 ? 11.046  -21.266 24.173  1.00 44.66  ? 89  HIS C N   1 
ATOM   2119 C CA  . HIS C 1 90 ? 10.817  -21.561 25.583  1.00 51.42  ? 89  HIS C CA  1 
ATOM   2120 C C   . HIS C 1 90 ? 9.365   -21.971 25.827  1.00 51.52  ? 89  HIS C C   1 
ATOM   2121 O O   . HIS C 1 90 ? 8.905   -21.966 26.963  1.00 58.15  ? 89  HIS C O   1 
ATOM   2122 C CB  . HIS C 1 90 ? 11.293  -20.416 26.484  1.00 41.20  ? 89  HIS C CB  1 
ATOM   2123 C CG  . HIS C 1 90 ? 12.688  -19.936 26.245  1.00 39.10  ? 89  HIS C CG  1 
ATOM   2124 N ND1 . HIS C 1 90 ? 13.800  -20.704 26.538  1.00 43.01  ? 89  HIS C ND1 1 
ATOM   2125 C CD2 . HIS C 1 90 ? 13.159  -18.790 25.736  1.00 40.65  ? 89  HIS C CD2 1 
ATOM   2126 C CE1 . HIS C 1 90 ? 14.910  -20.018 26.244  1.00 42.39  ? 89  HIS C CE1 1 
ATOM   2127 N NE2 . HIS C 1 90 ? 14.541  -18.852 25.737  1.00 43.43  ? 89  HIS C NE2 1 
ATOM   2128 N N   . ALA C 1 91 ? 8.644   -22.352 24.771  1.00 53.90  ? 90  ALA C N   1 
ATOM   2129 C CA  . ALA C 1 91 ? 7.354   -22.998 24.950  1.00 51.85  ? 90  ALA C CA  1 
ATOM   2130 C C   . ALA C 1 91 ? 7.550   -24.392 25.550  1.00 63.45  ? 90  ALA C C   1 
ATOM   2131 O O   . ALA C 1 91 ? 8.636   -24.977 25.464  1.00 58.70  ? 90  ALA C O   1 
ATOM   2132 C CB  . ALA C 1 91 ? 6.564   -23.037 23.655  1.00 52.24  ? 90  ALA C CB  1 
ATOM   2133 N N   . SER C 1 92 ? 6.462   -24.914 26.137  1.00 68.08  ? 91  SER C N   1 
ATOM   2134 C CA  . SER C 1 92 ? 6.437   -26.158 26.894  1.00 73.19  ? 91  SER C CA  1 
ATOM   2135 C C   . SER C 1 92 ? 6.772   -27.348 25.999  1.00 68.71  ? 91  SER C C   1 
ATOM   2136 O O   . SER C 1 92 ? 7.755   -28.042 26.236  1.00 77.26  ? 91  SER C O   1 
ATOM   2137 C CB  . SER C 1 92 ? 5.085   -26.368 27.552  1.00 75.71  ? 91  SER C CB  1 
ATOM   2138 O OG  . SER C 1 92 ? 4.620   -25.180 28.174  1.00 82.73  ? 91  SER C OG  1 
ATOM   2139 N N   . TYR C 1 93 ? 5.919   -27.586 24.996  1.00 68.55  ? 92  TYR C N   1 
ATOM   2140 C CA  . TYR C 1 93 ? 5.966   -28.786 24.174  1.00 73.25  ? 92  TYR C CA  1 
ATOM   2141 C C   . TYR C 1 93 ? 5.876   -30.015 25.095  1.00 79.12  ? 92  TYR C C   1 
ATOM   2142 O O   . TYR C 1 93 ? 5.421   -31.087 24.631  1.00 85.00  ? 92  TYR C O   1 
ATOM   2143 C CB  . TYR C 1 93 ? 7.219   -28.796 23.287  1.00 65.79  ? 92  TYR C CB  1 
ATOM   2144 C CG  . TYR C 1 93 ? 7.447   -27.551 22.432  1.00 56.22  ? 92  TYR C CG  1 
ATOM   2145 C CD1 . TYR C 1 93 ? 6.673   -27.298 21.300  1.00 53.27  ? 92  TYR C CD1 1 
ATOM   2146 C CD2 . TYR C 1 93 ? 8.463   -26.648 22.736  1.00 54.48  ? 92  TYR C CD2 1 
ATOM   2147 C CE1 . TYR C 1 93 ? 6.879   -26.171 20.522  1.00 50.65  ? 92  TYR C CE1 1 
ATOM   2148 C CE2 . TYR C 1 93 ? 8.681   -25.521 21.960  1.00 51.48  ? 92  TYR C CE2 1 
ATOM   2149 C CZ  . TYR C 1 93 ? 7.891   -25.282 20.850  1.00 53.78  ? 92  TYR C CZ  1 
ATOM   2150 O OH  . TYR C 1 93 ? 8.123   -24.149 20.109  1.00 51.53  ? 92  TYR C OH  1 
HETATM 2151 S S   . SO4 D 2 .  ? 1.293   -33.615 1.818   1.00 101.03 ? 101 SO4 A S   1 
HETATM 2152 O O1  . SO4 D 2 .  ? 2.233   -34.390 1.050   1.00 66.43  ? 101 SO4 A O1  1 
HETATM 2153 O O2  . SO4 D 2 .  ? 1.266   -32.257 1.333   1.00 97.07  ? 101 SO4 A O2  1 
HETATM 2154 O O3  . SO4 D 2 .  ? -0.020  -34.201 1.684   1.00 110.39 ? 101 SO4 A O3  1 
HETATM 2155 O O4  . SO4 D 2 .  ? 1.686   -33.619 3.204   1.00 99.84  ? 101 SO4 A O4  1 
HETATM 2156 S S   . SO4 E 2 .  ? -9.342  -24.836 1.483   1.00 99.13  ? 102 SO4 A S   1 
HETATM 2157 O O1  . SO4 E 2 .  ? -9.408  -24.423 0.105   1.00 82.62  ? 102 SO4 A O1  1 
HETATM 2158 O O2  . SO4 E 2 .  ? -9.210  -23.677 2.331   1.00 87.60  ? 102 SO4 A O2  1 
HETATM 2159 O O3  . SO4 E 2 .  ? -10.541 -25.560 1.821   1.00 109.57 ? 102 SO4 A O3  1 
HETATM 2160 O O4  . SO4 E 2 .  ? -8.209  -25.701 1.682   1.00 96.79  ? 102 SO4 A O4  1 
HETATM 2161 C C1  . EDO F 3 .  ? 14.018  -19.518 -7.426  1.00 40.26  ? 103 EDO A C1  1 
HETATM 2162 O O1  . EDO F 3 .  ? 15.275  -18.857 -7.220  1.00 32.61  ? 103 EDO A O1  1 
HETATM 2163 C C2  . EDO F 3 .  ? 13.201  -18.985 -8.568  1.00 35.40  ? 103 EDO A C2  1 
HETATM 2164 O O2  . EDO F 3 .  ? 12.655  -17.726 -8.249  1.00 32.88  ? 103 EDO A O2  1 
HETATM 2165 S S   . SO4 G 2 .  ? 9.105   -29.534 5.828   1.00 56.08  ? 104 SO4 A S   1 
HETATM 2166 O O1  . SO4 G 2 .  ? 9.988   -28.764 5.046   1.00 45.97  ? 104 SO4 A O1  1 
HETATM 2167 O O2  . SO4 G 2 .  ? 8.602   -30.647 5.015   1.00 55.94  ? 104 SO4 A O2  1 
HETATM 2168 O O3  . SO4 G 2 .  ? 9.816   -30.047 6.995   1.00 60.75  ? 104 SO4 A O3  1 
HETATM 2169 O O4  . SO4 G 2 .  ? 7.987   -28.719 6.229   1.00 64.19  ? 104 SO4 A O4  1 
HETATM 2170 S S   . SO4 H 2 .  ? 7.599   -8.621  -24.784 1.00 67.42  ? 101 SO4 B S   1 
HETATM 2171 O O1  . SO4 H 2 .  ? 8.731   -8.638  -25.686 1.00 42.22  ? 101 SO4 B O1  1 
HETATM 2172 O O2  . SO4 H 2 .  ? 6.429   -9.212  -25.413 1.00 50.85  ? 101 SO4 B O2  1 
HETATM 2173 O O3  . SO4 H 2 .  ? 7.878   -9.370  -23.553 1.00 47.03  ? 101 SO4 B O3  1 
HETATM 2174 O O4  . SO4 H 2 .  ? 7.369   -7.225  -24.477 1.00 63.69  ? 101 SO4 B O4  1 
HETATM 2175 S S   . SO4 I 2 .  ? 14.689  -27.109 -26.639 1.00 51.40  ? 102 SO4 B S   1 
HETATM 2176 O O1  . SO4 I 2 .  ? 15.894  -26.444 -26.233 1.00 61.86  ? 102 SO4 B O1  1 
HETATM 2177 O O2  . SO4 I 2 .  ? 15.046  -28.353 -27.295 1.00 58.24  ? 102 SO4 B O2  1 
HETATM 2178 O O3  . SO4 I 2 .  ? 13.879  -27.397 -25.485 1.00 60.09  ? 102 SO4 B O3  1 
HETATM 2179 O O4  . SO4 I 2 .  ? 13.926  -26.277 -27.547 1.00 54.61  ? 102 SO4 B O4  1 
HETATM 2180 C C10 . 8DH J 4 .  ? 21.054  -15.340 -24.610 0.68 44.68  ? 103 8DH B C10 1 
HETATM 2181 N N12 . 8DH J 4 .  ? 23.002  -14.576 -23.315 0.68 50.37  ? 103 8DH B N12 1 
HETATM 2182 C C13 . 8DH J 4 .  ? 22.368  -14.598 -22.151 0.68 54.77  ? 103 8DH B C13 1 
HETATM 2183 C C15 . 8DH J 4 .  ? 20.933  -15.034 -22.151 0.68 45.22  ? 103 8DH B C15 1 
HETATM 2184 C C01 . 8DH J 4 .  ? 15.805  -15.770 -24.596 0.68 38.61  ? 103 8DH B C01 1 
HETATM 2185 C C02 . 8DH J 4 .  ? 17.179  -15.795 -25.255 0.68 34.05  ? 103 8DH B C02 1 
HETATM 2186 C C03 . 8DH J 4 .  ? 17.317  -16.915 -26.256 0.68 31.21  ? 103 8DH B C03 1 
HETATM 2187 N N04 . 8DH J 4 .  ? 18.126  -15.800 -24.155 0.68 33.30  ? 103 8DH B N04 1 
HETATM 2188 C C05 . 8DH J 4 .  ? 18.455  -17.041 -23.443 0.68 35.74  ? 103 8DH B C05 1 
HETATM 2189 S S06 . 8DH J 4 .  ? 18.771  -14.418 -23.703 0.68 34.18  ? 103 8DH B S06 1 
HETATM 2190 O O07 . 8DH J 4 .  ? 18.692  -13.531 -24.818 0.68 36.60  ? 103 8DH B O07 1 
HETATM 2191 O O08 . 8DH J 4 .  ? 18.222  -14.012 -22.456 0.68 37.70  ? 103 8DH B O08 1 
HETATM 2192 N N09 . 8DH J 4 .  ? 20.275  -14.857 -23.455 0.68 34.61  ? 103 8DH B N09 1 
HETATM 2193 C C11 . 8DH J 4 .  ? 22.390  -14.640 -24.642 0.68 53.46  ? 103 8DH B C11 1 
HETATM 2194 O O14 . 8DH J 4 .  ? 22.907  -14.241 -21.106 0.68 58.30  ? 103 8DH B O14 1 
HETATM 2195 C C1  . EDO K 3 .  ? 16.798  -36.368 16.303  1.00 33.83  ? 101 EDO C C1  1 
HETATM 2196 O O1  . EDO K 3 .  ? 15.719  -37.076 15.702  1.00 37.40  ? 101 EDO C O1  1 
HETATM 2197 C C2  . EDO K 3 .  ? 16.362  -35.386 17.362  1.00 32.01  ? 101 EDO C C2  1 
HETATM 2198 O O2  . EDO K 3 .  ? 15.478  -35.895 18.331  1.00 33.25  ? 101 EDO C O2  1 
HETATM 2199 S S   . SO4 L 2 .  ? 29.257  -38.554 12.233  1.00 93.39  ? 102 SO4 C S   1 
HETATM 2200 O O1  . SO4 L 2 .  ? 30.284  -37.783 11.576  1.00 92.85  ? 102 SO4 C O1  1 
HETATM 2201 O O2  . SO4 L 2 .  ? 27.969  -37.993 11.939  1.00 77.21  ? 102 SO4 C O2  1 
HETATM 2202 O O3  . SO4 L 2 .  ? 29.299  -39.912 11.766  1.00 81.12  ? 102 SO4 C O3  1 
HETATM 2203 O O4  . SO4 L 2 .  ? 29.479  -38.529 13.659  1.00 96.96  ? 102 SO4 C O4  1 
HETATM 2204 O O   . HOH M 5 .  ? 8.455   -32.429 4.106   1.00 51.35  ? 201 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 10.574  -19.077 10.394  1.00 58.27  ? 202 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 5.924   -29.050 6.764   1.00 50.42  ? 203 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? -5.631  -13.333 -16.576 1.00 47.55  ? 204 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? -2.517  -11.817 13.878  1.00 52.09  ? 205 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? -2.199  -30.939 -4.017  1.00 47.46  ? 206 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 0.266   -33.613 5.265   1.00 62.52  ? 207 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 1.060   -24.891 13.731  1.00 53.20  ? 208 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 7.191   -10.566 -12.051 1.00 36.88  ? 209 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 15.821  -24.582 1.979   1.00 36.96  ? 210 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 12.992  -12.040 8.202   1.00 54.49  ? 211 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 9.178   -18.282 -10.907 1.00 32.21  ? 212 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 11.189  -29.685 2.971   1.00 44.84  ? 213 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 6.119   -7.340  9.832   1.00 60.64  ? 214 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 0.667   -10.489 -15.531 1.00 45.32  ? 215 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 4.812   -1.504  -6.422  1.00 35.69  ? 216 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 4.213   -10.428 13.529  1.00 48.67  ? 217 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 4.502   -3.610  -3.272  1.00 31.79  ? 218 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? -2.238  3.227   -2.057  1.00 42.68  ? 219 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? -3.670  -10.777 6.763   1.00 37.71  ? 220 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 11.319  -23.762 9.769   1.00 36.81  ? 221 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 14.653  -17.669 -19.149 1.00 45.92  ? 222 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 14.113  -15.743 -9.318  1.00 35.86  ? 223 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 19.927  -15.583 7.278   1.00 29.44  ? 224 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 1.945   -4.640  -10.136 1.00 36.32  ? 225 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 4.695   -7.833  1.223   1.00 32.62  ? 226 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -4.203  -21.247 6.061   1.00 41.28  ? 227 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 9.704   -6.062  -1.631  1.00 34.90  ? 228 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -7.749  -17.246 6.636   1.00 44.65  ? 229 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 13.384  -11.985 -4.205  1.00 23.21  ? 230 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 2.499   -25.283 -6.476  1.00 44.79  ? 231 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 8.256   -17.977 -15.869 1.00 49.26  ? 232 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 15.429  -28.041 -0.591  1.00 48.07  ? 233 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 3.896   -34.719 4.462   1.00 49.74  ? 234 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 10.140  -13.171 9.535   1.00 37.59  ? 235 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -0.576  -20.967 6.981   1.00 35.08  ? 236 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? -8.032  -15.691 -1.041  1.00 35.94  ? 237 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 1.800   0.640   -7.402  1.00 36.60  ? 238 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 2.542   -25.226 -9.993  1.00 37.32  ? 239 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 11.783  -16.617 -14.779 1.00 41.67  ? 240 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 10.941  -5.089  -7.740  1.00 32.90  ? 241 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 13.350  -28.099 -4.842  1.00 46.33  ? 242 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 9.685   -30.527 9.760   1.00 32.42  ? 243 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -5.652  -15.920 -8.058  1.00 29.25  ? 244 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 8.942   -16.325 -13.153 1.00 39.38  ? 245 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 3.272   -29.602 -0.536  1.00 39.61  ? 246 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -6.178  -11.572 -11.330 1.00 39.34  ? 247 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? -1.697  -22.063 -0.634  1.00 27.25  ? 248 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? -5.751  -19.814 -5.613  1.00 36.59  ? 249 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? 17.233  -12.886 1.400   1.00 21.01  ? 250 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -0.627  -20.637 11.340  1.00 57.01  ? 251 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 11.604  -11.909 5.943   1.00 34.19  ? 252 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 6.553   -16.069 -15.062 1.00 48.47  ? 253 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 15.750  -12.091 -5.331  1.00 33.21  ? 254 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 11.576  -12.418 -6.157  1.00 27.56  ? 255 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 1.789   -10.595 11.732  1.00 36.70  ? 256 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 2.935   -9.948  -13.286 1.00 41.62  ? 257 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? -6.118  -25.612 -5.953  1.00 54.21  ? 258 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -10.910 -16.005 -3.610  1.00 51.14  ? 259 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 16.775  -12.386 -17.022 1.00 43.07  ? 260 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 8.214   -17.550 8.557   1.00 41.27  ? 261 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? -8.485  -17.011 3.322   1.00 54.77  ? 262 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? -1.386  -11.899 11.259  1.00 38.29  ? 263 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 11.528  -6.083  -3.841  1.00 44.81  ? 264 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -1.471  -7.617  11.544  1.00 45.45  ? 265 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 10.143  -27.700 -7.242  1.00 54.51  ? 266 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? -0.820  -29.355 9.851   1.00 60.72  ? 267 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 12.757  -13.443 -8.492  1.00 41.85  ? 268 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 6.549   -5.917  0.489   1.00 47.58  ? 269 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 8.112   -7.867  1.228   1.00 29.45  ? 270 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 9.681   -20.356 -18.422 1.00 44.82  ? 271 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? -4.113  -25.944 -5.552  1.00 40.77  ? 272 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -7.172  -21.787 -5.967  1.00 45.29  ? 273 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 1.705   -18.696 -18.551 1.00 43.83  ? 274 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? -7.835  -16.735 1.467   1.00 39.10  ? 275 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? -5.940  -12.749 6.759   1.00 36.61  ? 276 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 8.124   -8.313  4.532   1.00 34.73  ? 277 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -6.495  -13.899 -11.942 1.00 49.20  ? 278 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 0.231   -23.426 8.893   1.00 42.62  ? 279 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 5.129   -7.608  3.975   1.00 35.09  ? 280 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 13.064  -9.404  -7.058  1.00 43.13  ? 281 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? 17.465  -14.022 10.612  1.00 51.31  ? 282 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -7.166  -11.512 -7.968  1.00 27.50  ? 283 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 11.050  -7.876  0.369   1.00 26.61  ? 284 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 15.039  -13.246 10.455  1.00 47.55  ? 285 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? -8.526  -21.146 -1.295  1.00 38.85  ? 286 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? -5.824  -26.685 3.397   1.00 51.30  ? 287 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 22.338  -16.661 -0.446  1.00 40.14  ? 288 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 21.455  -16.748 -3.521  1.00 30.00  ? 289 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? 13.198  -15.248 -12.188 1.00 47.69  ? 290 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? -8.020  -19.574 -3.467  1.00 51.73  ? 291 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? 17.220  -18.216 -9.633  1.00 53.57  ? 292 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 9.566   -2.896  -0.192  1.00 60.90  ? 293 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? -4.085  -26.276 7.611   1.00 52.60  ? 294 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -3.787  -7.837  10.642  1.00 45.07  ? 295 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? -5.476  -23.595 -6.908  1.00 37.34  ? 296 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 9.013   -9.156  -13.732 1.00 40.83  ? 297 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? 0.037   -8.129  -13.247 1.00 45.73  ? 298 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 4.902   -6.895  -10.880 1.00 48.68  ? 299 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? -3.758  -11.094 9.706   1.00 51.16  ? 300 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? 11.959  -21.380 10.546  1.00 38.04  ? 301 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? 1.262   -29.596 -7.177  1.00 54.10  ? 302 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 4.076   -27.223 -9.704  1.00 51.30  ? 303 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? -9.965  -28.321 -1.617  1.00 56.58  ? 304 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? 8.800   -12.906 12.321  1.00 51.47  ? 305 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? -7.280  -14.193 -9.245  1.00 36.42  ? 306 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? 11.544  -2.058  -1.671  1.00 45.31  ? 307 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? -6.275  -22.791 5.560   1.00 54.54  ? 308 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? 4.829   -9.641  -11.393 1.00 41.31  ? 309 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? -2.938  -21.570 7.914   1.00 42.86  ? 310 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? 5.813   -3.307  1.027   1.00 57.02  ? 311 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? -11.269 -13.590 -2.849  1.00 39.12  ? 312 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? 8.417   -22.363 -19.478 1.00 57.98  ? 313 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? -6.898  -19.122 8.532   1.00 48.43  ? 314 HOH A O   1 
HETATM 2318 O O   . HOH M 5 .  ? 7.813   -30.709 -2.099  1.00 55.89  ? 315 HOH A O   1 
HETATM 2319 O O   . HOH M 5 .  ? -5.048  -20.992 -8.243  1.00 52.34  ? 316 HOH A O   1 
HETATM 2320 O O   . HOH M 5 .  ? -9.747  -21.587 -6.406  1.00 49.43  ? 317 HOH A O   1 
HETATM 2321 O O   . HOH M 5 .  ? 10.031  -7.471  12.653  1.00 60.30  ? 318 HOH A O   1 
HETATM 2322 O O   . HOH N 5 .  ? 10.393  -19.762 -43.202 1.00 45.03  ? 201 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 19.938  -22.139 -23.351 1.00 48.03  ? 202 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 10.092  -11.206 -38.035 1.00 45.47  ? 203 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 12.872  -26.100 -37.242 1.00 50.64  ? 204 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 12.887  -4.553  -41.917 1.00 49.49  ? 205 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 30.760  -8.155  -30.113 1.00 51.46  ? 206 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 26.119  -4.581  -33.766 1.00 49.45  ? 207 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 25.252  -5.116  -30.006 1.00 37.30  ? 208 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 27.985  -8.109  -29.084 1.00 47.55  ? 209 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 10.437  -16.845 -44.442 1.00 45.32  ? 210 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 24.379  -10.354 -22.298 1.00 46.26  ? 211 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 26.254  -22.954 -31.288 1.00 38.50  ? 212 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 17.630  -7.783  -20.646 1.00 43.73  ? 213 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 20.361  -2.496  -23.225 1.00 56.01  ? 214 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 6.210   -7.436  -32.189 1.00 55.45  ? 215 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 30.192  -12.796 -46.130 1.00 69.88  ? 216 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 4.577   -18.741 -25.699 1.00 59.27  ? 217 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 30.418  -19.848 -40.413 1.00 35.06  ? 218 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 24.461  -1.744  -36.399 1.00 47.47  ? 219 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 20.707  -13.290 -42.857 1.00 40.23  ? 220 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 11.360  -8.077  -41.455 1.00 44.94  ? 221 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 23.541  -2.285  -29.232 1.00 40.07  ? 222 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 6.652   -12.146 -26.251 1.00 36.20  ? 223 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 10.662  -18.887 -33.068 1.00 30.69  ? 224 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 22.279  3.541   -32.767 1.00 47.96  ? 225 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 16.754  -19.389 -28.913 1.00 25.61  ? 226 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 17.594  -19.765 -42.119 1.00 45.63  ? 227 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 25.436  -5.898  -36.045 1.00 41.14  ? 228 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 28.197  -17.378 -25.197 1.00 48.04  ? 229 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 18.571  0.001   -25.775 1.00 62.92  ? 230 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 21.309  -26.280 -30.185 1.00 51.73  ? 231 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 22.859  -22.861 -28.866 1.00 37.99  ? 232 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 32.420  -18.886 -42.571 1.00 45.09  ? 233 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 7.128   -19.130 -35.115 1.00 49.54  ? 234 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 8.884   -8.682  -16.500 1.00 39.86  ? 235 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 22.147  -23.935 -26.547 1.00 45.77  ? 236 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 10.803  -21.915 -32.852 1.00 36.27  ? 237 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 18.151  -0.554  -38.565 1.00 30.60  ? 238 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 8.688   -27.832 -38.040 1.00 63.48  ? 239 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 23.761  -4.148  -37.021 1.00 32.02  ? 240 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 34.900  -23.051 -30.080 1.00 69.00  ? 241 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 18.367  -26.004 -28.941 1.00 42.31  ? 242 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 14.333  -6.368  -41.235 1.00 40.21  ? 243 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 3.399   -8.506  -27.266 1.00 55.59  ? 244 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 13.315  -22.429 -20.708 1.00 55.44  ? 245 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 31.991  -21.212 -38.310 1.00 44.08  ? 246 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 20.352  -10.180 -43.069 1.00 40.14  ? 247 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 7.693   -12.461 -38.858 1.00 50.00  ? 248 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 31.881  -12.420 -39.048 1.00 54.23  ? 249 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 7.625   -8.298  -20.778 1.00 50.50  ? 250 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 14.743  -24.479 -40.503 1.00 42.47  ? 251 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 19.773  -25.585 -34.128 1.00 42.10  ? 252 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 21.055  -6.513  -42.679 1.00 37.59  ? 253 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 18.018  -15.899 -45.839 1.00 42.95  ? 254 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 7.644   -18.348 -31.724 1.00 44.01  ? 255 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 27.877  -24.821 -35.223 1.00 35.62  ? 256 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 17.926  -3.689  -22.039 1.00 53.89  ? 257 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 16.997  -9.589  -44.017 1.00 46.11  ? 258 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 27.505  -10.510 -29.011 1.00 60.23  ? 259 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 1.693   -13.041 -28.496 1.00 51.39  ? 260 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 24.687  -6.738  -42.834 1.00 48.88  ? 261 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 18.543  -13.188 -44.628 1.00 46.33  ? 262 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 20.614  3.798   -33.003 1.00 35.01  ? 263 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 18.354  4.530   -34.389 1.00 38.03  ? 264 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 25.184  -8.045  -22.919 1.00 50.45  ? 265 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 6.491   -20.712 -25.122 1.00 41.90  ? 266 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 26.384  -0.255  -29.370 1.00 51.41  ? 267 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 8.023   -5.157  -21.922 1.00 57.78  ? 268 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 39.013  -13.375 -39.422 1.00 81.18  ? 269 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 9.721   -6.083  -41.062 1.00 48.44  ? 270 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 22.189  -23.616 -24.003 1.00 53.63  ? 271 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 17.258  -25.675 -21.114 1.00 65.24  ? 272 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 12.920  -20.211 -19.480 1.00 48.93  ? 273 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 16.759  -0.651  -25.469 1.00 52.06  ? 274 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 15.085  -8.049  -43.147 1.00 42.50  ? 275 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 11.519  -24.213 -30.162 1.00 54.42  ? 276 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 24.668  -4.115  -28.024 1.00 56.46  ? 277 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 15.321  -21.970 -41.927 1.00 50.02  ? 278 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 7.545   -9.942  -18.646 1.00 41.99  ? 279 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 22.643  -29.225 -35.715 1.00 42.57  ? 280 HOH B O   1 
HETATM 2402 O O   . HOH O 5 .  ? 26.944  -37.856 10.183  1.00 39.94  ? 201 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 26.581  -39.314 12.722  1.00 39.82  ? 202 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 20.013  -19.891 29.935  1.00 61.23  ? 203 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 16.232  -17.626 24.945  1.00 62.15  ? 204 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 27.214  -25.450 31.888  1.00 112.20 ? 205 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 13.047  -19.975 11.061  1.00 55.02  ? 206 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 7.785   -31.737 12.293  1.00 51.70  ? 207 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 31.903  -33.388 25.773  1.00 49.36  ? 208 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 9.533   -30.343 11.163  1.00 58.44  ? 209 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 12.168  -28.688 28.019  1.00 61.21  ? 210 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 33.260  -24.420 31.585  1.00 51.11  ? 211 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 8.953   -37.039 18.211  1.00 54.18  ? 212 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 17.456  -17.193 14.943  1.00 43.95  ? 213 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 19.315  -20.208 10.619  1.00 38.71  ? 214 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 30.322  -40.509 9.492   1.00 34.62  ? 215 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 14.795  -39.238 16.804  1.00 52.13  ? 216 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 16.333  -37.935 19.925  1.00 52.30  ? 217 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 12.927  -31.555 8.215   1.00 32.19  ? 218 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 23.107  -41.676 18.489  1.00 44.86  ? 219 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 19.293  -26.822 3.295   1.00 47.93  ? 220 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 23.702  -20.927 23.918  1.00 47.12  ? 221 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 25.468  -33.869 34.824  1.00 51.16  ? 222 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 15.685  -17.715 19.420  1.00 42.85  ? 223 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 20.059  -41.963 12.164  1.00 28.72  ? 224 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 14.311  -37.329 13.421  1.00 44.01  ? 225 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 30.353  -31.261 15.883  1.00 48.49  ? 226 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 5.760   -26.582 16.938  1.00 50.33  ? 227 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 23.309  -18.560 21.764  1.00 50.44  ? 228 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 25.292  -31.420 10.805  1.00 36.60  ? 229 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 29.909  -39.781 31.392  1.00 37.44  ? 230 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 19.661  -41.225 39.162  1.00 66.97  ? 231 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 9.102   -19.014 23.551  1.00 50.45  ? 232 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 17.881  -21.214 12.945  1.00 43.24  ? 233 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 22.118  -34.444 16.548  1.00 25.99  ? 234 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 22.279  -28.616 11.042  1.00 32.33  ? 235 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 30.761  -29.212 12.174  1.00 50.67  ? 236 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 15.409  -21.143 12.259  1.00 36.67  ? 237 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 30.568  -35.786 28.542  1.00 60.30  ? 238 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 20.904  -28.803 8.467   1.00 35.63  ? 239 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 16.200  -38.435 11.501  1.00 48.75  ? 240 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 13.217  -23.088 27.960  1.00 75.45  ? 241 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 27.803  -37.535 25.091  1.00 48.16  ? 242 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 28.203  -37.372 15.993  1.00 40.91  ? 243 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 31.594  -39.678 27.183  1.00 45.84  ? 244 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 20.812  -40.068 26.367  1.00 39.51  ? 245 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 30.474  -17.510 9.566   1.00 45.46  ? 246 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 6.934   -18.018 10.788  1.00 41.45  ? 247 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 25.864  -17.577 13.805  1.00 44.54  ? 248 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 21.099  -29.595 4.924   1.00 55.84  ? 249 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 31.281  -43.659 15.681  1.00 56.52  ? 250 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 31.257  -34.372 35.390  1.00 55.89  ? 251 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 25.682  -39.709 20.165  1.00 36.32  ? 252 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 14.305  -38.892 9.693   1.00 60.34  ? 253 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 19.949  -19.095 24.900  1.00 44.20  ? 254 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 14.454  -29.532 4.008   1.00 38.07  ? 255 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 31.904  -43.457 11.997  1.00 50.14  ? 256 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 30.315  -32.715 18.257  1.00 45.21  ? 257 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 25.632  -17.844 21.199  1.00 68.17  ? 258 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 28.169  -36.810 18.652  1.00 44.72  ? 259 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 2.676   -28.801 13.772  1.00 56.66  ? 260 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 29.432  -25.311 32.670  1.00 57.84  ? 261 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 5.245   -24.219 18.586  1.00 57.96  ? 262 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 17.471  -36.411 29.282  1.00 59.20  ? 263 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 28.136  -14.540 13.105  1.00 52.41  ? 264 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 29.208  -41.684 27.288  1.00 43.00  ? 265 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 19.933  -32.805 35.156  1.00 66.79  ? 266 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 24.069  -15.845 11.977  1.00 43.84  ? 267 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 27.528  -39.392 24.371  1.00 53.71  ? 268 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 22.764  -14.061 13.361  1.00 47.22  ? 269 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 14.925  -34.197 35.162  1.00 62.39  ? 270 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 28.528  -41.662 29.994  1.00 44.43  ? 271 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 33.527  -44.524 15.240  1.00 42.19  ? 272 HOH C O   1 
HETATM 2474 O O   . HOH O 5 .  ? 37.720  -24.057 26.769  1.00 59.06  ? 273 HOH C O   1 
HETATM 2475 O O   . HOH O 5 .  ? 7.538   -38.725 5.118   1.00 58.88  ? 274 HOH C O   1 
# 
