data_7HGX
# 
_entry.id   7HGX 
# 
_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   7HGX         pdb_00007hgx 10.2210/pdb7hgx/pdb 
WWPDB D_1001407459 ?            ?                   
# 
_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                        7HGX 
_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           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?    ? ? 
4 non-polymer syn '(2R)-1-(2-methyl-1H-imidazol-1-yl)propan-2-ol'    140.183   2   ? ?    ? ? 
5 water       nat water                                              18.015    259 ? ?    ? ? 
# 
_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 '(2R)-1-(2-methyl-1H-imidazol-1-yl)propan-2-ol' A1A31 
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 
A1A31 non-polymer         . '(2R)-1-(2-methyl-1H-imidazol-1-yl)propan-2-ol' ?                 'C7 H12 N2 O'    140.183 
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 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A31 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A31 
_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 A1A31 1   103 102 A1A31 LIG B . 
K 2 SO4   1   101 5   SO4   SO4 C . 
L 4 A1A31 1   102 101 A1A31 LIG C . 
M 5 HOH   1   201 307 HOH   HOH A . 
M 5 HOH   2   202 357 HOH   HOH A . 
M 5 HOH   3   203 202 HOH   HOH A . 
M 5 HOH   4   204 345 HOH   HOH A . 
M 5 HOH   5   205 259 HOH   HOH A . 
M 5 HOH   6   206 347 HOH   HOH A . 
M 5 HOH   7   207 66  HOH   HOH A . 
M 5 HOH   8   208 208 HOH   HOH A . 
M 5 HOH   9   209 91  HOH   HOH A . 
M 5 HOH   10  210 84  HOH   HOH A . 
M 5 HOH   11  211 71  HOH   HOH A . 
M 5 HOH   12  212 304 HOH   HOH A . 
M 5 HOH   13  213 260 HOH   HOH A . 
M 5 HOH   14  214 293 HOH   HOH A . 
M 5 HOH   15  215 55  HOH   HOH A . 
M 5 HOH   16  216 139 HOH   HOH A . 
M 5 HOH   17  217 301 HOH   HOH A . 
M 5 HOH   18  218 292 HOH   HOH A . 
M 5 HOH   19  219 86  HOH   HOH A . 
M 5 HOH   20  220 8   HOH   HOH A . 
M 5 HOH   21  221 87  HOH   HOH A . 
M 5 HOH   22  222 26  HOH   HOH A . 
M 5 HOH   23  223 142 HOH   HOH A . 
M 5 HOH   24  224 28  HOH   HOH A . 
M 5 HOH   25  225 199 HOH   HOH A . 
M 5 HOH   26  226 42  HOH   HOH A . 
M 5 HOH   27  227 37  HOH   HOH A . 
M 5 HOH   28  228 99  HOH   HOH A . 
M 5 HOH   29  229 95  HOH   HOH A . 
M 5 HOH   30  230 290 HOH   HOH A . 
M 5 HOH   31  231 167 HOH   HOH A . 
M 5 HOH   32  232 179 HOH   HOH A . 
M 5 HOH   33  233 1   HOH   HOH A . 
M 5 HOH   34  234 27  HOH   HOH A . 
M 5 HOH   35  235 288 HOH   HOH A . 
M 5 HOH   36  236 34  HOH   HOH A . 
M 5 HOH   37  237 188 HOH   HOH A . 
M 5 HOH   38  238 97  HOH   HOH A . 
M 5 HOH   39  239 203 HOH   HOH A . 
M 5 HOH   40  240 116 HOH   HOH A . 
M 5 HOH   41  241 32  HOH   HOH A . 
M 5 HOH   42  242 287 HOH   HOH A . 
M 5 HOH   43  243 190 HOH   HOH A . 
M 5 HOH   44  244 334 HOH   HOH A . 
M 5 HOH   45  245 289 HOH   HOH A . 
M 5 HOH   46  246 12  HOH   HOH A . 
M 5 HOH   47  247 7   HOH   HOH A . 
M 5 HOH   48  248 300 HOH   HOH A . 
M 5 HOH   49  249 78  HOH   HOH A . 
M 5 HOH   50  250 23  HOH   HOH A . 
M 5 HOH   51  251 111 HOH   HOH A . 
M 5 HOH   52  252 2   HOH   HOH A . 
M 5 HOH   53  253 145 HOH   HOH A . 
M 5 HOH   54  254 152 HOH   HOH A . 
M 5 HOH   55  255 267 HOH   HOH A . 
M 5 HOH   56  256 58  HOH   HOH A . 
M 5 HOH   57  257 60  HOH   HOH A . 
M 5 HOH   58  258 93  HOH   HOH A . 
M 5 HOH   59  259 278 HOH   HOH A . 
M 5 HOH   60  260 211 HOH   HOH A . 
M 5 HOH   61  261 115 HOH   HOH A . 
M 5 HOH   62  262 20  HOH   HOH A . 
M 5 HOH   63  263 38  HOH   HOH A . 
M 5 HOH   64  264 274 HOH   HOH A . 
M 5 HOH   65  265 337 HOH   HOH A . 
M 5 HOH   66  266 21  HOH   HOH A . 
M 5 HOH   67  267 18  HOH   HOH A . 
M 5 HOH   68  268 131 HOH   HOH A . 
M 5 HOH   69  269 94  HOH   HOH A . 
M 5 HOH   70  270 297 HOH   HOH A . 
M 5 HOH   71  271 222 HOH   HOH A . 
M 5 HOH   72  272 109 HOH   HOH A . 
M 5 HOH   73  273 14  HOH   HOH A . 
M 5 HOH   74  274 359 HOH   HOH A . 
M 5 HOH   75  275 164 HOH   HOH A . 
M 5 HOH   76  276 35  HOH   HOH A . 
M 5 HOH   77  277 77  HOH   HOH A . 
M 5 HOH   78  278 356 HOH   HOH A . 
M 5 HOH   79  279 218 HOH   HOH A . 
M 5 HOH   80  280 143 HOH   HOH A . 
M 5 HOH   81  281 19  HOH   HOH A . 
M 5 HOH   82  282 327 HOH   HOH A . 
M 5 HOH   83  283 31  HOH   HOH A . 
M 5 HOH   84  284 165 HOH   HOH A . 
M 5 HOH   85  285 9   HOH   HOH A . 
M 5 HOH   86  286 16  HOH   HOH A . 
M 5 HOH   87  287 113 HOH   HOH A . 
M 5 HOH   88  288 47  HOH   HOH A . 
M 5 HOH   89  289 338 HOH   HOH A . 
M 5 HOH   90  290 156 HOH   HOH A . 
M 5 HOH   91  291 318 HOH   HOH A . 
M 5 HOH   92  292 358 HOH   HOH A . 
M 5 HOH   93  293 281 HOH   HOH A . 
M 5 HOH   94  294 210 HOH   HOH A . 
M 5 HOH   95  295 22  HOH   HOH A . 
M 5 HOH   96  296 63  HOH   HOH A . 
M 5 HOH   97  297 73  HOH   HOH A . 
M 5 HOH   98  298 83  HOH   HOH A . 
M 5 HOH   99  299 354 HOH   HOH A . 
M 5 HOH   100 300 64  HOH   HOH A . 
M 5 HOH   101 301 185 HOH   HOH A . 
M 5 HOH   102 302 219 HOH   HOH A . 
M 5 HOH   103 303 108 HOH   HOH A . 
M 5 HOH   104 304 57  HOH   HOH A . 
M 5 HOH   105 305 283 HOH   HOH A . 
M 5 HOH   106 306 205 HOH   HOH A . 
M 5 HOH   107 307 75  HOH   HOH A . 
M 5 HOH   108 308 206 HOH   HOH A . 
M 5 HOH   109 309 313 HOH   HOH A . 
M 5 HOH   110 310 332 HOH   HOH A . 
M 5 HOH   111 311 125 HOH   HOH A . 
N 5 HOH   1   201 247 HOH   HOH B . 
N 5 HOH   2   202 258 HOH   HOH B . 
N 5 HOH   3   203 272 HOH   HOH B . 
N 5 HOH   4   204 329 HOH   HOH B . 
N 5 HOH   5   205 215 HOH   HOH B . 
N 5 HOH   6   206 68  HOH   HOH B . 
N 5 HOH   7   207 123 HOH   HOH B . 
N 5 HOH   8   208 279 HOH   HOH B . 
N 5 HOH   9   209 89  HOH   HOH B . 
N 5 HOH   10  210 54  HOH   HOH B . 
N 5 HOH   11  211 69  HOH   HOH B . 
N 5 HOH   12  212 353 HOH   HOH B . 
N 5 HOH   13  213 119 HOH   HOH B . 
N 5 HOH   14  214 331 HOH   HOH B . 
N 5 HOH   15  215 242 HOH   HOH B . 
N 5 HOH   16  216 46  HOH   HOH B . 
N 5 HOH   17  217 346 HOH   HOH B . 
N 5 HOH   18  218 333 HOH   HOH B . 
N 5 HOH   19  219 172 HOH   HOH B . 
N 5 HOH   20  220 98  HOH   HOH B . 
N 5 HOH   21  221 224 HOH   HOH B . 
N 5 HOH   22  222 249 HOH   HOH B . 
N 5 HOH   23  223 184 HOH   HOH B . 
N 5 HOH   24  224 5   HOH   HOH B . 
N 5 HOH   25  225 168 HOH   HOH B . 
N 5 HOH   26  226 169 HOH   HOH B . 
N 5 HOH   27  227 10  HOH   HOH B . 
N 5 HOH   28  228 261 HOH   HOH B . 
N 5 HOH   29  229 17  HOH   HOH B . 
N 5 HOH   30  230 6   HOH   HOH B . 
N 5 HOH   31  231 117 HOH   HOH B . 
N 5 HOH   32  232 59  HOH   HOH B . 
N 5 HOH   33  233 137 HOH   HOH B . 
N 5 HOH   34  234 96  HOH   HOH B . 
N 5 HOH   35  235 335 HOH   HOH B . 
N 5 HOH   36  236 355 HOH   HOH B . 
N 5 HOH   37  237 25  HOH   HOH B . 
N 5 HOH   38  238 24  HOH   HOH B . 
N 5 HOH   39  239 315 HOH   HOH B . 
N 5 HOH   40  240 352 HOH   HOH B . 
N 5 HOH   41  241 197 HOH   HOH B . 
N 5 HOH   42  242 223 HOH   HOH B . 
N 5 HOH   43  243 214 HOH   HOH B . 
N 5 HOH   44  244 351 HOH   HOH B . 
N 5 HOH   45  245 150 HOH   HOH B . 
N 5 HOH   46  246 175 HOH   HOH B . 
N 5 HOH   47  247 280 HOH   HOH B . 
N 5 HOH   48  248 61  HOH   HOH B . 
N 5 HOH   49  249 153 HOH   HOH B . 
N 5 HOH   50  250 101 HOH   HOH B . 
N 5 HOH   51  251 320 HOH   HOH B . 
N 5 HOH   52  252 36  HOH   HOH B . 
N 5 HOH   53  253 303 HOH   HOH B . 
N 5 HOH   54  254 79  HOH   HOH B . 
N 5 HOH   55  255 120 HOH   HOH B . 
N 5 HOH   56  256 157 HOH   HOH B . 
N 5 HOH   57  257 76  HOH   HOH B . 
N 5 HOH   58  258 74  HOH   HOH B . 
N 5 HOH   59  259 13  HOH   HOH B . 
N 5 HOH   60  260 170 HOH   HOH B . 
N 5 HOH   61  261 72  HOH   HOH B . 
N 5 HOH   62  262 217 HOH   HOH B . 
N 5 HOH   63  263 182 HOH   HOH B . 
N 5 HOH   64  264 104 HOH   HOH B . 
N 5 HOH   65  265 316 HOH   HOH B . 
N 5 HOH   66  266 44  HOH   HOH B . 
N 5 HOH   67  267 163 HOH   HOH B . 
N 5 HOH   68  268 177 HOH   HOH B . 
N 5 HOH   69  269 201 HOH   HOH B . 
N 5 HOH   70  270 291 HOH   HOH B . 
N 5 HOH   71  271 322 HOH   HOH B . 
N 5 HOH   72  272 160 HOH   HOH B . 
N 5 HOH   73  273 319 HOH   HOH B . 
N 5 HOH   74  274 107 HOH   HOH B . 
N 5 HOH   75  275 314 HOH   HOH B . 
N 5 HOH   76  276 92  HOH   HOH B . 
N 5 HOH   77  277 312 HOH   HOH B . 
N 5 HOH   78  278 336 HOH   HOH B . 
N 5 HOH   79  279 310 HOH   HOH B . 
O 5 HOH   1   201 349 HOH   HOH C . 
O 5 HOH   2   202 254 HOH   HOH C . 
O 5 HOH   3   203 321 HOH   HOH C . 
O 5 HOH   4   204 173 HOH   HOH C . 
O 5 HOH   5   205 317 HOH   HOH C . 
O 5 HOH   6   206 161 HOH   HOH C . 
O 5 HOH   7   207 323 HOH   HOH C . 
O 5 HOH   8   208 85  HOH   HOH C . 
O 5 HOH   9   209 226 HOH   HOH C . 
O 5 HOH   10  210 118 HOH   HOH C . 
O 5 HOH   11  211 15  HOH   HOH C . 
O 5 HOH   12  212 330 HOH   HOH C . 
O 5 HOH   13  213 305 HOH   HOH C . 
O 5 HOH   14  214 134 HOH   HOH C . 
O 5 HOH   15  215 90  HOH   HOH C . 
O 5 HOH   16  216 284 HOH   HOH C . 
O 5 HOH   17  217 269 HOH   HOH C . 
O 5 HOH   18  218 48  HOH   HOH C . 
O 5 HOH   19  219 45  HOH   HOH C . 
O 5 HOH   20  220 149 HOH   HOH C . 
O 5 HOH   21  221 41  HOH   HOH C . 
O 5 HOH   22  222 271 HOH   HOH C . 
O 5 HOH   23  223 348 HOH   HOH C . 
O 5 HOH   24  224 49  HOH   HOH C . 
O 5 HOH   25  225 325 HOH   HOH C . 
O 5 HOH   26  226 151 HOH   HOH C . 
O 5 HOH   27  227 122 HOH   HOH C . 
O 5 HOH   28  228 102 HOH   HOH C . 
O 5 HOH   29  229 275 HOH   HOH C . 
O 5 HOH   30  230 40  HOH   HOH C . 
O 5 HOH   31  231 209 HOH   HOH C . 
O 5 HOH   32  232 189 HOH   HOH C . 
O 5 HOH   33  233 4   HOH   HOH C . 
O 5 HOH   34  234 43  HOH   HOH C . 
O 5 HOH   35  235 341 HOH   HOH C . 
O 5 HOH   36  236 56  HOH   HOH C . 
O 5 HOH   37  237 295 HOH   HOH C . 
O 5 HOH   38  238 82  HOH   HOH C . 
O 5 HOH   39  239 126 HOH   HOH C . 
O 5 HOH   40  240 132 HOH   HOH C . 
O 5 HOH   41  241 298 HOH   HOH C . 
O 5 HOH   42  242 302 HOH   HOH C . 
O 5 HOH   43  243 344 HOH   HOH C . 
O 5 HOH   44  244 148 HOH   HOH C . 
O 5 HOH   45  245 294 HOH   HOH C . 
O 5 HOH   46  246 198 HOH   HOH C . 
O 5 HOH   47  247 67  HOH   HOH C . 
O 5 HOH   48  248 53  HOH   HOH C . 
O 5 HOH   49  249 130 HOH   HOH C . 
O 5 HOH   50  250 328 HOH   HOH C . 
O 5 HOH   51  251 342 HOH   HOH C . 
O 5 HOH   52  252 299 HOH   HOH C . 
O 5 HOH   53  253 246 HOH   HOH C . 
O 5 HOH   54  254 62  HOH   HOH C . 
O 5 HOH   55  255 135 HOH   HOH C . 
O 5 HOH   56  256 339 HOH   HOH C . 
O 5 HOH   57  257 309 HOH   HOH C . 
O 5 HOH   58  258 171 HOH   HOH C . 
O 5 HOH   59  259 65  HOH   HOH C . 
O 5 HOH   60  260 296 HOH   HOH C . 
O 5 HOH   61  261 146 HOH   HOH C . 
O 5 HOH   62  262 340 HOH   HOH C . 
O 5 HOH   63  263 343 HOH   HOH C . 
O 5 HOH   64  264 270 HOH   HOH C . 
O 5 HOH   65  265 324 HOH   HOH C . 
O 5 HOH   66  266 241 HOH   HOH C . 
O 5 HOH   67  267 70  HOH   HOH C . 
O 5 HOH   68  268 103 HOH   HOH C . 
O 5 HOH   69  269 350 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 GLU 79 ? CD  ? B GLU 80 CD  
22 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
23 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
24 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
25 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
26 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
27 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
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 LYS 34 ? CG  ? C LYS 35 CG  
33 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
34 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
35 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
36 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
37 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
38 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
39 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
40 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
41 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
42 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
43 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
44 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
45 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
46 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
47 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HGX 
_cell.length_a           41.410 
_cell.length_b           42.030 
_cell.length_c           158.320 
_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                         7HGX 
_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          7HGX 
_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                     7HGX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.77 
_reflns.d_resolution_high            1.57 
_reflns.number_obs                   39705 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.061 
_reflns.pdbx_netI_over_sigmaI        12.8 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.066 
_reflns.pdbx_Rpim_I_all              0.026 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     245433 
_reflns.pdbx_chi_squared             0.97 
_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                  1.57 
_reflns_shell.d_res_low                   1.61 
_reflns_shell.number_measured_all         15191 
_reflns_shell.number_unique_obs           2890 
_reflns_shell.Rmerge_I_obs                1.975 
_reflns_shell.pdbx_chi_squared            0.85 
_reflns_shell.pdbx_redundancy             5.3 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.197 
_reflns_shell.pdbx_Rpim_I_all             0.950 
_reflns_shell.pdbx_CC_half                0.365 
_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                                 7HGX 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     37533 
_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                             40.66 
_refine.ls_d_res_high                            1.57 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_R_factor_obs                          0.20363 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20096 
_refine.ls_R_factor_R_free                       0.25151 
_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                  2094 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.968 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_refine.B_iso_mean                               36.372 
_refine.aniso_B[1][1]                            0.97 
_refine.aniso_B[2][2]                            0.15 
_refine.aniso_B[3][3]                            -1.12 
_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                       0.096 
_refine.pdbx_overall_ESU_R_Free                  0.103 
_refine.overall_SU_ML                            0.089 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.678 
_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        2132 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             259 
_refine_hist.number_atoms_total               2445 
_refine_hist.d_res_high                       1.57 
_refine_hist.d_res_low                        40.66 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.009  0.012  ? 2290 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.782  1.830  ? 3116 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.026  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.047  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.004 10.000 ? 306  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.129  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1920 '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                  3.267  3.334  ? 1065 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.609  5.956  ? 1328 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.450  3.694  ? 1225 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.149  50.80  ? 3525 '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                       1.570 
_refine_ls_shell.d_res_low                        1.611 
_refine_ls_shell.number_reflns_R_work             2714 
_refine_ls_shell.R_factor_R_work                  0.360 
_refine_ls_shell.percent_reflns_obs               99.83 
_refine_ls_shell.R_factor_R_free                  0.396 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             168 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGX 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1362754425' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGX 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGX A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGX B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGX 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 7HGX GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGX SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGX GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGX SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGX GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGX SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O 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                   7HGX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 253 ? ? O B HOH 271 ? ? 1.60 
2  1 NE2 C HIS 89  ? ? O C HOH 201 ? ? 1.87 
3  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.01 
4  1 O   B HOH 219 ? ? O B HOH 238 ? ? 2.03 
5  1 OD1 A ASP 62  ? ? O A HOH 202 ? ? 2.06 
6  1 O2  C SO4 101 ? ? O C HOH 202 ? ? 2.08 
7  1 O   B ASP 27  ? A O B HOH 201 ? ? 2.12 
8  1 O   C HOH 261 ? ? O C HOH 265 ? ? 2.15 
9  1 O4  A SO4 104 ? ? O A HOH 203 ? ? 2.17 
10 1 O   B HOH 244 ? ? O B HOH 263 ? ? 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 262 ? ? 1_555 O A HOH 305 ? ? 4_545 2.10 
2 1 O A HOH 276 ? ? 1_555 O A HOH 305 ? ? 4_545 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 38 ? ? 57.48   17.47  
2 1 ASN A 87 ? ? -154.38 66.05  
3 1 ASN B 87 ? ? -160.60 57.93  
4 1 ASN C 87 ? ? -158.37 56.94  
5 1 ALA C 90 ? ? -59.06  170.79 
# 
_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            149.74 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ASP 27 ? C ASP 28 
11 1 Y 1 C ILE 28 ? C ILE 29 
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C ALA 32 ? C ALA 33 
16 1 Y 1 C VAL 33 ? C VAL 34 
17 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 
A1A31 N1   N Y N 1   
A1A31 C4   C Y N 2   
A1A31 C5   C Y N 3   
A1A31 C6   C N N 4   
A1A31 O    O N N 5   
A1A31 C1   C N R 6   
A1A31 C    C N N 7   
A1A31 C2   C N N 8   
A1A31 N    N Y N 9   
A1A31 C3   C Y N 10  
A1A31 H8   H N N 11  
A1A31 H11  H N N 12  
A1A31 H10  H N N 13  
A1A31 H9   H N N 14  
A1A31 H4   H N N 15  
A1A31 H3   H N N 16  
A1A31 H2   H N N 17  
A1A31 H1   H N N 18  
A1A31 H    H N N 19  
A1A31 H6   H N N 20  
A1A31 H5   H N N 21  
A1A31 H7   H N N 22  
ALA   N    N N N 23  
ALA   CA   C N S 24  
ALA   C    C N N 25  
ALA   O    O N N 26  
ALA   CB   C N N 27  
ALA   OXT  O N N 28  
ALA   H    H N N 29  
ALA   H2   H N N 30  
ALA   HA   H N N 31  
ALA   HB1  H N N 32  
ALA   HB2  H N N 33  
ALA   HB3  H N N 34  
ALA   HXT  H N N 35  
ARG   N    N N N 36  
ARG   CA   C N S 37  
ARG   C    C N N 38  
ARG   O    O N N 39  
ARG   CB   C N N 40  
ARG   CG   C N N 41  
ARG   CD   C N N 42  
ARG   NE   N N N 43  
ARG   CZ   C N N 44  
ARG   NH1  N N N 45  
ARG   NH2  N N N 46  
ARG   OXT  O N N 47  
ARG   H    H N N 48  
ARG   H2   H N N 49  
ARG   HA   H N N 50  
ARG   HB2  H N N 51  
ARG   HB3  H N N 52  
ARG   HG2  H N N 53  
ARG   HG3  H N N 54  
ARG   HD2  H N N 55  
ARG   HD3  H N N 56  
ARG   HE   H N N 57  
ARG   HH11 H N N 58  
ARG   HH12 H N N 59  
ARG   HH21 H N N 60  
ARG   HH22 H N N 61  
ARG   HXT  H N N 62  
ASN   N    N N N 63  
ASN   CA   C N S 64  
ASN   C    C N N 65  
ASN   O    O N N 66  
ASN   CB   C N N 67  
ASN   CG   C N N 68  
ASN   OD1  O N N 69  
ASN   ND2  N N N 70  
ASN   OXT  O N N 71  
ASN   H    H N N 72  
ASN   H2   H N N 73  
ASN   HA   H N N 74  
ASN   HB2  H N N 75  
ASN   HB3  H N N 76  
ASN   HD21 H N N 77  
ASN   HD22 H N N 78  
ASN   HXT  H N N 79  
ASP   N    N N N 80  
ASP   CA   C N S 81  
ASP   C    C N N 82  
ASP   O    O N N 83  
ASP   CB   C N N 84  
ASP   CG   C N N 85  
ASP   OD1  O N N 86  
ASP   OD2  O N N 87  
ASP   OXT  O N N 88  
ASP   H    H N N 89  
ASP   H2   H N N 90  
ASP   HA   H N N 91  
ASP   HB2  H N N 92  
ASP   HB3  H N N 93  
ASP   HD2  H N N 94  
ASP   HXT  H N N 95  
CYS   N    N N N 96  
CYS   CA   C N R 97  
CYS   C    C N N 98  
CYS   O    O N N 99  
CYS   CB   C N N 100 
CYS   SG   S N N 101 
CYS   OXT  O N N 102 
CYS   H    H N N 103 
CYS   H2   H N N 104 
CYS   HA   H N N 105 
CYS   HB2  H N N 106 
CYS   HB3  H N N 107 
CYS   HG   H N N 108 
CYS   HXT  H N N 109 
EDO   C1   C N N 110 
EDO   O1   O N N 111 
EDO   C2   C N N 112 
EDO   O2   O N N 113 
EDO   H11  H N N 114 
EDO   H12  H N N 115 
EDO   HO1  H N N 116 
EDO   H21  H N N 117 
EDO   H22  H N N 118 
EDO   HO2  H N N 119 
GLN   N    N N N 120 
GLN   CA   C N S 121 
GLN   C    C N N 122 
GLN   O    O N N 123 
GLN   CB   C N N 124 
GLN   CG   C N N 125 
GLN   CD   C N N 126 
GLN   OE1  O N N 127 
GLN   NE2  N N N 128 
GLN   OXT  O N N 129 
GLN   H    H N N 130 
GLN   H2   H N N 131 
GLN   HA   H N N 132 
GLN   HB2  H N N 133 
GLN   HB3  H N N 134 
GLN   HG2  H N N 135 
GLN   HG3  H N N 136 
GLN   HE21 H N N 137 
GLN   HE22 H N N 138 
GLN   HXT  H N N 139 
GLU   N    N N N 140 
GLU   CA   C N S 141 
GLU   C    C N N 142 
GLU   O    O N N 143 
GLU   CB   C N N 144 
GLU   CG   C N N 145 
GLU   CD   C N N 146 
GLU   OE1  O N N 147 
GLU   OE2  O N N 148 
GLU   OXT  O N N 149 
GLU   H    H N N 150 
GLU   H2   H N N 151 
GLU   HA   H N N 152 
GLU   HB2  H N N 153 
GLU   HB3  H N N 154 
GLU   HG2  H N N 155 
GLU   HG3  H N N 156 
GLU   HE2  H N N 157 
GLU   HXT  H N N 158 
GLY   N    N N N 159 
GLY   CA   C N N 160 
GLY   C    C N N 161 
GLY   O    O N N 162 
GLY   OXT  O N N 163 
GLY   H    H N N 164 
GLY   H2   H N N 165 
GLY   HA2  H N N 166 
GLY   HA3  H N N 167 
GLY   HXT  H N N 168 
HIS   N    N N N 169 
HIS   CA   C N S 170 
HIS   C    C N N 171 
HIS   O    O N N 172 
HIS   CB   C N N 173 
HIS   CG   C Y N 174 
HIS   ND1  N Y N 175 
HIS   CD2  C Y N 176 
HIS   CE1  C Y N 177 
HIS   NE2  N Y N 178 
HIS   OXT  O N N 179 
HIS   H    H N N 180 
HIS   H2   H N N 181 
HIS   HA   H N N 182 
HIS   HB2  H N N 183 
HIS   HB3  H N N 184 
HIS   HD1  H N N 185 
HIS   HD2  H N N 186 
HIS   HE1  H N N 187 
HIS   HE2  H N N 188 
HIS   HXT  H N N 189 
HOH   O    O N N 190 
HOH   H1   H N N 191 
HOH   H2   H N N 192 
ILE   N    N N N 193 
ILE   CA   C N S 194 
ILE   C    C N N 195 
ILE   O    O N N 196 
ILE   CB   C N S 197 
ILE   CG1  C N N 198 
ILE   CG2  C N N 199 
ILE   CD1  C N N 200 
ILE   OXT  O N N 201 
ILE   H    H N N 202 
ILE   H2   H N N 203 
ILE   HA   H N N 204 
ILE   HB   H N N 205 
ILE   HG12 H N N 206 
ILE   HG13 H N N 207 
ILE   HG21 H N N 208 
ILE   HG22 H N N 209 
ILE   HG23 H N N 210 
ILE   HD11 H N N 211 
ILE   HD12 H N N 212 
ILE   HD13 H N N 213 
ILE   HXT  H N N 214 
LEU   N    N N N 215 
LEU   CA   C N S 216 
LEU   C    C N N 217 
LEU   O    O N N 218 
LEU   CB   C N N 219 
LEU   CG   C N N 220 
LEU   CD1  C N N 221 
LEU   CD2  C N N 222 
LEU   OXT  O N N 223 
LEU   H    H N N 224 
LEU   H2   H N N 225 
LEU   HA   H N N 226 
LEU   HB2  H N N 227 
LEU   HB3  H N N 228 
LEU   HG   H N N 229 
LEU   HD11 H N N 230 
LEU   HD12 H N N 231 
LEU   HD13 H N N 232 
LEU   HD21 H N N 233 
LEU   HD22 H N N 234 
LEU   HD23 H N N 235 
LEU   HXT  H N N 236 
LYS   N    N N N 237 
LYS   CA   C N S 238 
LYS   C    C N N 239 
LYS   O    O N N 240 
LYS   CB   C N N 241 
LYS   CG   C N N 242 
LYS   CD   C N N 243 
LYS   CE   C N N 244 
LYS   NZ   N N N 245 
LYS   OXT  O N N 246 
LYS   H    H N N 247 
LYS   H2   H N N 248 
LYS   HA   H N N 249 
LYS   HB2  H N N 250 
LYS   HB3  H N N 251 
LYS   HG2  H N N 252 
LYS   HG3  H N N 253 
LYS   HD2  H N N 254 
LYS   HD3  H N N 255 
LYS   HE2  H N N 256 
LYS   HE3  H N N 257 
LYS   HZ1  H N N 258 
LYS   HZ2  H N N 259 
LYS   HZ3  H N N 260 
LYS   HXT  H N N 261 
MET   N    N N N 262 
MET   CA   C N S 263 
MET   C    C N N 264 
MET   O    O N N 265 
MET   CB   C N N 266 
MET   CG   C N N 267 
MET   SD   S N N 268 
MET   CE   C N N 269 
MET   OXT  O N N 270 
MET   H    H N N 271 
MET   H2   H N N 272 
MET   HA   H N N 273 
MET   HB2  H N N 274 
MET   HB3  H N N 275 
MET   HG2  H N N 276 
MET   HG3  H N N 277 
MET   HE1  H N N 278 
MET   HE2  H N N 279 
MET   HE3  H N N 280 
MET   HXT  H N N 281 
PHE   N    N N N 282 
PHE   CA   C N S 283 
PHE   C    C N N 284 
PHE   O    O N N 285 
PHE   CB   C N N 286 
PHE   CG   C Y N 287 
PHE   CD1  C Y N 288 
PHE   CD2  C Y N 289 
PHE   CE1  C Y N 290 
PHE   CE2  C Y N 291 
PHE   CZ   C Y N 292 
PHE   OXT  O N N 293 
PHE   H    H N N 294 
PHE   H2   H N N 295 
PHE   HA   H N N 296 
PHE   HB2  H N N 297 
PHE   HB3  H N N 298 
PHE   HD1  H N N 299 
PHE   HD2  H N N 300 
PHE   HE1  H N N 301 
PHE   HE2  H N N 302 
PHE   HZ   H N N 303 
PHE   HXT  H N N 304 
PRO   N    N N N 305 
PRO   CA   C N S 306 
PRO   C    C N N 307 
PRO   O    O N N 308 
PRO   CB   C N N 309 
PRO   CG   C N N 310 
PRO   CD   C N N 311 
PRO   OXT  O N N 312 
PRO   H    H N N 313 
PRO   HA   H N N 314 
PRO   HB2  H N N 315 
PRO   HB3  H N N 316 
PRO   HG2  H N N 317 
PRO   HG3  H N N 318 
PRO   HD2  H N N 319 
PRO   HD3  H N N 320 
PRO   HXT  H N N 321 
SER   N    N N N 322 
SER   CA   C N S 323 
SER   C    C N N 324 
SER   O    O N N 325 
SER   CB   C N N 326 
SER   OG   O N N 327 
SER   OXT  O N N 328 
SER   H    H N N 329 
SER   H2   H N N 330 
SER   HA   H N N 331 
SER   HB2  H N N 332 
SER   HB3  H N N 333 
SER   HG   H N N 334 
SER   HXT  H N N 335 
SO4   S    S N N 336 
SO4   O1   O N N 337 
SO4   O2   O N N 338 
SO4   O3   O N N 339 
SO4   O4   O N N 340 
THR   N    N N N 341 
THR   CA   C N S 342 
THR   C    C N N 343 
THR   O    O N N 344 
THR   CB   C N R 345 
THR   OG1  O N N 346 
THR   CG2  C N N 347 
THR   OXT  O N N 348 
THR   H    H N N 349 
THR   H2   H N N 350 
THR   HA   H N N 351 
THR   HB   H N N 352 
THR   HG1  H N N 353 
THR   HG21 H N N 354 
THR   HG22 H N N 355 
THR   HG23 H N N 356 
THR   HXT  H N N 357 
TRP   N    N N N 358 
TRP   CA   C N S 359 
TRP   C    C N N 360 
TRP   O    O N N 361 
TRP   CB   C N N 362 
TRP   CG   C Y N 363 
TRP   CD1  C Y N 364 
TRP   CD2  C Y N 365 
TRP   NE1  N Y N 366 
TRP   CE2  C Y N 367 
TRP   CE3  C Y N 368 
TRP   CZ2  C Y N 369 
TRP   CZ3  C Y N 370 
TRP   CH2  C Y N 371 
TRP   OXT  O N N 372 
TRP   H    H N N 373 
TRP   H2   H N N 374 
TRP   HA   H N N 375 
TRP   HB2  H N N 376 
TRP   HB3  H N N 377 
TRP   HD1  H N N 378 
TRP   HE1  H N N 379 
TRP   HE3  H N N 380 
TRP   HZ2  H N N 381 
TRP   HZ3  H N N 382 
TRP   HH2  H N N 383 
TRP   HXT  H N N 384 
TYR   N    N N N 385 
TYR   CA   C N S 386 
TYR   C    C N N 387 
TYR   O    O N N 388 
TYR   CB   C N N 389 
TYR   CG   C Y N 390 
TYR   CD1  C Y N 391 
TYR   CD2  C Y N 392 
TYR   CE1  C Y N 393 
TYR   CE2  C Y N 394 
TYR   CZ   C Y N 395 
TYR   OH   O N N 396 
TYR   OXT  O N N 397 
TYR   H    H N N 398 
TYR   H2   H N N 399 
TYR   HA   H N N 400 
TYR   HB2  H N N 401 
TYR   HB3  H N N 402 
TYR   HD1  H N N 403 
TYR   HD2  H N N 404 
TYR   HE1  H N N 405 
TYR   HE2  H N N 406 
TYR   HH   H N N 407 
TYR   HXT  H N N 408 
VAL   N    N N N 409 
VAL   CA   C N S 410 
VAL   C    C N N 411 
VAL   O    O N N 412 
VAL   CB   C N N 413 
VAL   CG1  C N N 414 
VAL   CG2  C N N 415 
VAL   OXT  O N N 416 
VAL   H    H N N 417 
VAL   H2   H N N 418 
VAL   HA   H N N 419 
VAL   HB   H N N 420 
VAL   HG11 H N N 421 
VAL   HG12 H N N 422 
VAL   HG13 H N N 423 
VAL   HG21 H N N 424 
VAL   HG22 H N N 425 
VAL   HG23 H N N 426 
VAL   HXT  H N N 427 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A31 C   C1   sing N N 1   
A1A31 C1  O    sing N N 2   
A1A31 C2  C1   sing N N 3   
A1A31 N   C2   sing N N 4   
A1A31 N   C3   sing Y N 5   
A1A31 C3  C4   doub Y N 6   
A1A31 C4  N1   sing Y N 7   
A1A31 N1  C5   doub Y N 8   
A1A31 C5  N    sing Y N 9   
A1A31 C6  C5   sing N N 10  
A1A31 C4  H8   sing N N 11  
A1A31 C6  H11  sing N N 12  
A1A31 C6  H10  sing N N 13  
A1A31 C6  H9   sing N N 14  
A1A31 O   H4   sing N N 15  
A1A31 C1  H3   sing N N 16  
A1A31 C   H2   sing N N 17  
A1A31 C   H1   sing N N 18  
A1A31 C   H    sing N N 19  
A1A31 C2  H6   sing N N 20  
A1A31 C2  H5   sing N N 21  
A1A31 C3  H7   sing N N 22  
ALA   N   CA   sing N N 23  
ALA   N   H    sing N N 24  
ALA   N   H2   sing N N 25  
ALA   CA  C    sing N N 26  
ALA   CA  CB   sing N N 27  
ALA   CA  HA   sing N N 28  
ALA   C   O    doub N N 29  
ALA   C   OXT  sing N N 30  
ALA   CB  HB1  sing N N 31  
ALA   CB  HB2  sing N N 32  
ALA   CB  HB3  sing N N 33  
ALA   OXT HXT  sing N N 34  
ARG   N   CA   sing N N 35  
ARG   N   H    sing N N 36  
ARG   N   H2   sing N N 37  
ARG   CA  C    sing N N 38  
ARG   CA  CB   sing N N 39  
ARG   CA  HA   sing N N 40  
ARG   C   O    doub N N 41  
ARG   C   OXT  sing N N 42  
ARG   CB  CG   sing N N 43  
ARG   CB  HB2  sing N N 44  
ARG   CB  HB3  sing N N 45  
ARG   CG  CD   sing N N 46  
ARG   CG  HG2  sing N N 47  
ARG   CG  HG3  sing N N 48  
ARG   CD  NE   sing N N 49  
ARG   CD  HD2  sing N N 50  
ARG   CD  HD3  sing N N 51  
ARG   NE  CZ   sing N N 52  
ARG   NE  HE   sing N N 53  
ARG   CZ  NH1  sing N N 54  
ARG   CZ  NH2  doub N N 55  
ARG   NH1 HH11 sing N N 56  
ARG   NH1 HH12 sing N N 57  
ARG   NH2 HH21 sing N N 58  
ARG   NH2 HH22 sing N N 59  
ARG   OXT HXT  sing N N 60  
ASN   N   CA   sing N N 61  
ASN   N   H    sing N N 62  
ASN   N   H2   sing N N 63  
ASN   CA  C    sing N N 64  
ASN   CA  CB   sing N N 65  
ASN   CA  HA   sing N N 66  
ASN   C   O    doub N N 67  
ASN   C   OXT  sing N N 68  
ASN   CB  CG   sing N N 69  
ASN   CB  HB2  sing N N 70  
ASN   CB  HB3  sing N N 71  
ASN   CG  OD1  doub N N 72  
ASN   CG  ND2  sing N N 73  
ASN   ND2 HD21 sing N N 74  
ASN   ND2 HD22 sing N N 75  
ASN   OXT HXT  sing N N 76  
ASP   N   CA   sing N N 77  
ASP   N   H    sing N N 78  
ASP   N   H2   sing N N 79  
ASP   CA  C    sing N N 80  
ASP   CA  CB   sing N N 81  
ASP   CA  HA   sing N N 82  
ASP   C   O    doub N N 83  
ASP   C   OXT  sing N N 84  
ASP   CB  CG   sing N N 85  
ASP   CB  HB2  sing N N 86  
ASP   CB  HB3  sing N N 87  
ASP   CG  OD1  doub N N 88  
ASP   CG  OD2  sing N N 89  
ASP   OD2 HD2  sing N N 90  
ASP   OXT HXT  sing N N 91  
CYS   N   CA   sing N N 92  
CYS   N   H    sing N N 93  
CYS   N   H2   sing N N 94  
CYS   CA  C    sing N N 95  
CYS   CA  CB   sing N N 96  
CYS   CA  HA   sing N N 97  
CYS   C   O    doub N N 98  
CYS   C   OXT  sing N N 99  
CYS   CB  SG   sing N N 100 
CYS   CB  HB2  sing N N 101 
CYS   CB  HB3  sing N N 102 
CYS   SG  HG   sing N N 103 
CYS   OXT HXT  sing N N 104 
EDO   C1  O1   sing N N 105 
EDO   C1  C2   sing N N 106 
EDO   C1  H11  sing N N 107 
EDO   C1  H12  sing N N 108 
EDO   O1  HO1  sing N N 109 
EDO   C2  O2   sing N N 110 
EDO   C2  H21  sing N N 111 
EDO   C2  H22  sing N N 112 
EDO   O2  HO2  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
PHE   N   CA   sing N N 268 
PHE   N   H    sing N N 269 
PHE   N   H2   sing N N 270 
PHE   CA  C    sing N N 271 
PHE   CA  CB   sing N N 272 
PHE   CA  HA   sing N N 273 
PHE   C   O    doub N N 274 
PHE   C   OXT  sing N N 275 
PHE   CB  CG   sing N N 276 
PHE   CB  HB2  sing N N 277 
PHE   CB  HB3  sing N N 278 
PHE   CG  CD1  doub Y N 279 
PHE   CG  CD2  sing Y N 280 
PHE   CD1 CE1  sing Y N 281 
PHE   CD1 HD1  sing N N 282 
PHE   CD2 CE2  doub Y N 283 
PHE   CD2 HD2  sing N N 284 
PHE   CE1 CZ   doub Y N 285 
PHE   CE1 HE1  sing N N 286 
PHE   CE2 CZ   sing Y N 287 
PHE   CE2 HE2  sing N N 288 
PHE   CZ  HZ   sing N N 289 
PHE   OXT HXT  sing N N 290 
PRO   N   CA   sing N N 291 
PRO   N   CD   sing N N 292 
PRO   N   H    sing N N 293 
PRO   CA  C    sing N N 294 
PRO   CA  CB   sing N N 295 
PRO   CA  HA   sing N N 296 
PRO   C   O    doub N N 297 
PRO   C   OXT  sing N N 298 
PRO   CB  CG   sing N N 299 
PRO   CB  HB2  sing N N 300 
PRO   CB  HB3  sing N N 301 
PRO   CG  CD   sing N N 302 
PRO   CG  HG2  sing N N 303 
PRO   CG  HG3  sing N N 304 
PRO   CD  HD2  sing N N 305 
PRO   CD  HD3  sing N N 306 
PRO   OXT HXT  sing N N 307 
SER   N   CA   sing N N 308 
SER   N   H    sing N N 309 
SER   N   H2   sing N N 310 
SER   CA  C    sing N N 311 
SER   CA  CB   sing N N 312 
SER   CA  HA   sing N N 313 
SER   C   O    doub N N 314 
SER   C   OXT  sing N N 315 
SER   CB  OG   sing N N 316 
SER   CB  HB2  sing N N 317 
SER   CB  HB3  sing N N 318 
SER   OG  HG   sing N N 319 
SER   OXT HXT  sing N N 320 
SO4   S   O1   doub N N 321 
SO4   S   O2   doub N N 322 
SO4   S   O3   sing N N 323 
SO4   S   O4   sing N N 324 
THR   N   CA   sing N N 325 
THR   N   H    sing N N 326 
THR   N   H2   sing N N 327 
THR   CA  C    sing N N 328 
THR   CA  CB   sing N N 329 
THR   CA  HA   sing N N 330 
THR   C   O    doub N N 331 
THR   C   OXT  sing N N 332 
THR   CB  OG1  sing N N 333 
THR   CB  CG2  sing N N 334 
THR   CB  HB   sing N N 335 
THR   OG1 HG1  sing N N 336 
THR   CG2 HG21 sing N N 337 
THR   CG2 HG22 sing N N 338 
THR   CG2 HG23 sing N N 339 
THR   OXT HXT  sing N N 340 
TRP   N   CA   sing N N 341 
TRP   N   H    sing N N 342 
TRP   N   H2   sing N N 343 
TRP   CA  C    sing N N 344 
TRP   CA  CB   sing N N 345 
TRP   CA  HA   sing N N 346 
TRP   C   O    doub N N 347 
TRP   C   OXT  sing N N 348 
TRP   CB  CG   sing N N 349 
TRP   CB  HB2  sing N N 350 
TRP   CB  HB3  sing N N 351 
TRP   CG  CD1  doub Y N 352 
TRP   CG  CD2  sing Y N 353 
TRP   CD1 NE1  sing Y N 354 
TRP   CD1 HD1  sing N N 355 
TRP   CD2 CE2  doub Y N 356 
TRP   CD2 CE3  sing Y N 357 
TRP   NE1 CE2  sing Y N 358 
TRP   NE1 HE1  sing N N 359 
TRP   CE2 CZ2  sing Y N 360 
TRP   CE3 CZ3  doub Y N 361 
TRP   CE3 HE3  sing N N 362 
TRP   CZ2 CH2  doub Y N 363 
TRP   CZ2 HZ2  sing N N 364 
TRP   CZ3 CH2  sing Y N 365 
TRP   CZ3 HZ3  sing N N 366 
TRP   CH2 HH2  sing N N 367 
TRP   OXT HXT  sing N N 368 
TYR   N   CA   sing N N 369 
TYR   N   H    sing N N 370 
TYR   N   H2   sing N N 371 
TYR   CA  C    sing N N 372 
TYR   CA  CB   sing N N 373 
TYR   CA  HA   sing N N 374 
TYR   C   O    doub N N 375 
TYR   C   OXT  sing N N 376 
TYR   CB  CG   sing N N 377 
TYR   CB  HB2  sing N N 378 
TYR   CB  HB3  sing N N 379 
TYR   CG  CD1  doub Y N 380 
TYR   CG  CD2  sing Y N 381 
TYR   CD1 CE1  sing Y N 382 
TYR   CD1 HD1  sing N N 383 
TYR   CD2 CE2  doub Y N 384 
TYR   CD2 HD2  sing N N 385 
TYR   CE1 CZ   doub Y N 386 
TYR   CE1 HE1  sing N N 387 
TYR   CE2 CZ   sing Y N 388 
TYR   CE2 HE2  sing N N 389 
TYR   CZ  OH   sing N N 390 
TYR   OH  HH   sing N N 391 
TYR   OXT HXT  sing N N 392 
VAL   N   CA   sing N N 393 
VAL   N   H    sing N N 394 
VAL   N   H2   sing N N 395 
VAL   CA  C    sing N N 396 
VAL   CA  CB   sing N N 397 
VAL   CA  HA   sing N N 398 
VAL   C   O    doub N N 399 
VAL   C   OXT  sing N N 400 
VAL   CB  CG1  sing N N 401 
VAL   CB  CG2  sing N N 402 
VAL   CB  HB   sing N N 403 
VAL   CG1 HG11 sing N N 404 
VAL   CG1 HG12 sing N N 405 
VAL   CG1 HG13 sing N N 406 
VAL   CG2 HG21 sing N N 407 
VAL   CG2 HG22 sing N N 408 
VAL   CG2 HG23 sing N N 409 
VAL   OXT HXT  sing N N 410 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Research Foundation - Flanders (FWO)' Belgium 1SC9822N 1 
'Research Foundation - Flanders (FWO)' Belgium 1SC9824N 2 
'Research Foundation - Flanders (FWO)' Belgium G053822N 3 
# 
_pdbx_deposit_group.group_id            G_1002305 
_pdbx_deposit_group.group_title         'PanDDA analysis group deposition' 
_pdbx_deposit_group.group_description   
'Fragment screening against HRP-2 PWWP domain at the XChem facility of Diamond Light Source' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7HGX 
_atom_sites.fract_transf_matrix[1][1]   0.024149 
_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]   0.023793 
_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]   0.006316 
_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  ? 0.389   4.281   2.473   1.00 52.14  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.733  3.580   1.794   1.00 55.06  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? -0.183  2.552   0.803   1.00 48.88  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 0.881   2.753   0.237   1.00 44.21  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.674  4.581   1.114   1.00 58.30  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.615  5.279   2.083   1.00 66.09  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.874  4.254   2.884   1.00 59.54  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.745  5.555   3.774   1.00 61.21  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.858  1.390   0.624   1.00 45.22  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.401  0.327   -0.282  1.00 41.76  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? -0.155  0.725   -1.738  1.00 35.44  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.876  1.538   -2.304  1.00 38.61  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.579  -0.708  -0.203  1.00 42.79  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -2.161  -0.480  1.176   1.00 45.48  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -2.095  1.027   1.341   1.00 44.72  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 0.842   0.077   -2.344  1.00 34.72  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.042   0.187   -3.771  1.00 35.77  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.486   -1.097  -4.367  1.00 34.77  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.009   -1.968  -3.635  1.00 32.07  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.550   0.246   -4.065  1.00 41.09  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.244   1.483   -3.579  1.00 58.57  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.411   1.802   -2.248  1.00 62.92  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 3.798   2.497   -4.268  1.00 66.44  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.046   2.963   -2.143  1.00 65.88  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.297   3.398   -3.358  1.00 64.31  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.593   -1.229  -5.690  1.00 28.48  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.340   -2.505  -6.334  1.00 27.19  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.449   -3.485  -5.944  1.00 26.36  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.521   -3.068  -5.502  1.00 28.07  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.381   -2.229  -7.813  1.00 29.75  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.157   -4.785  -6.073  1.00 27.96  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.175   -5.820  -5.872  1.00 25.58  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.307   -5.677  -6.889  1.00 25.77  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.071   -5.281  -8.038  1.00 29.20  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.523   -7.200  -6.017  1.00 24.82  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 0.777   -7.629  -4.766  1.00 26.14  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.488   -7.858  -3.589  1.00 24.06  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.618  -7.836  -4.774  1.00 23.50  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 0.835   -8.220  -2.410  1.00 23.51  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -1.261  -8.275  -3.610  1.00 22.93  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.554  -8.442  -2.432  1.00 25.06  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.555   -5.964  -6.442  1.00 22.47  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.699   -5.927  -7.335  1.00 22.48  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.601   -7.128  -7.024  1.00 22.35  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.582   -7.681  -5.913  1.00 22.55  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.533   -4.656  -7.091  1.00 26.75  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.126   -4.517  -5.695  1.00 27.98  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.720   -3.127  -5.458  1.00 36.70  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.392   -3.119  -4.121  1.00 34.29  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.473   -3.376  -3.014  1.00 35.19  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.478   -7.534  -7.964  1.00 22.68  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.367   -8.666  -7.731  1.00 22.52  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.149   -8.383  -6.451  1.00 22.89  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.609   -7.258  -6.231  1.00 23.65  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.248   -8.707  -8.992  1.00 25.93  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.333   -8.061  -10.026 1.00 26.13  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.644   -6.920  -9.297  1.00 26.63  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.361   -9.452  -5.652  1.00 21.75  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.069  -9.341  -4.386  1.00 21.69  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.137   -9.190  -3.188  1.00 21.89  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.503   -9.528  -2.042  1.00 22.82  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 7.873   -8.772  -3.416  1.00 19.55  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 6.989   -8.718  -2.268  1.00 19.70  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 6.720   -10.101 -1.659  1.00 18.98  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.527   -11.074 -2.382  1.00 20.22  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.651   -8.119  -2.687  1.00 21.37  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.679   -6.610  -2.906  1.00 22.43  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.663   -5.957  -2.478  1.00 24.35  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 4.728   -6.089  -3.519  1.00 24.29  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.616   -10.141 -0.317  1.00 18.31  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.436   -11.420 0.388   1.00 18.41  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 4.980   -11.512 0.810   1.00 18.86  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.398   -10.509 1.297   1.00 21.99  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.364   -11.517 1.614   1.00 19.39  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 8.845   -11.316 1.255   1.00 20.06  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 9.693   -11.440 2.496   1.00 21.23  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.274   -12.298 0.160   1.00 19.55  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.430   -12.732 0.686   1.00 18.34  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 2.996   -12.924 0.925   1.00 18.83  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 2.732   -14.275 1.565   1.00 20.59  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.601   -15.146 1.582   1.00 19.68  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.200   -12.812 -0.396  1.00 17.75  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.264   -11.377 -0.945  1.00 20.64  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.552   -13.926 -1.412  1.00 17.47  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.503   -14.437 2.086   1.00 19.28  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 0.917   -15.777 2.105   1.00 20.51  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? -0.082  -15.869 0.947   1.00 22.12  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.879  -14.965 0.740   1.00 21.75  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.149   -16.094 3.412   1.00 21.22  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.073   -16.178 4.608   1.00 22.42  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.439   -15.029 5.305   1.00 22.50  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.585   -17.414 4.997   1.00 23.74  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.346   -15.115 6.352   1.00 27.41  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.461   -17.493 6.061   1.00 27.00  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 2.846   -16.353 6.719   1.00 26.68  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.035   -16.933 0.133   1.00 21.81  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.753  -17.085 -1.073  1.00 21.36  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.747  -18.233 -0.840  1.00 23.61  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -1.377  -19.296 -0.319  1.00 24.13  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.142   -17.361 -2.293  1.00 20.23  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -3.005  -18.002 -1.228  1.00 22.36  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -4.026  -19.026 -1.005  1.00 23.68  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -4.392  -19.700 -2.319  1.00 25.29  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.816  -19.035 -3.270  1.00 28.12  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -5.215  -18.366 -0.288  1.00 26.37  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -6.341  -19.405 0.083   1.00 30.88  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.851  -20.347 1.197   1.00 31.33  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.949  -21.204 1.826   1.00 34.67  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -7.413  -22.198 0.852   1.00 31.36  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -4.382  -21.044 -2.278  1.00 26.19  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.888  -21.885 -3.348  1.00 28.55  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.949  -22.799 -2.734  1.00 31.30  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.801  -23.209 -1.584  1.00 27.06  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.796  -22.860 -3.801  1.00 28.81  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.439  -22.214 -4.081  1.00 36.07  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -2.351  -21.881 -5.852  1.00 37.71  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.786  -23.443 -6.498  1.00 36.88  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.973  -23.103 -3.536  1.00 35.75  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -8.020  -24.051 -3.186  1.00 41.86  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -7.393  -25.295 -2.583  1.00 36.24  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -6.480  -25.891 -3.151  1.00 38.66  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.788  -24.480 -4.443  1.00 47.46  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -10.241 -24.901 -4.187  1.00 55.67  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -11.052 -23.975 -3.278  1.00 56.58  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.868  -25.671 -1.391  1.00 38.92  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -7.447  -26.944 -0.852  1.00 36.58  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -6.126  -26.899 -0.099  1.00 42.26  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.711  -27.938 0.417   1.00 41.03  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -5.457  -25.725 -0.041  1.00 35.90  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -4.216  -25.631 0.712   1.00 33.92  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -4.331  -24.516 1.747   1.00 30.99  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -5.055  -23.549 1.523   1.00 32.51  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.965  -25.305 -0.120  1.00 36.78  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.710  -26.323 -1.222  1.00 38.24  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -1.875  -27.411 -1.018  1.00 48.68  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -3.336  -26.192 -2.452  1.00 39.51  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -1.666  -28.342 -2.025  1.00 55.97  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -3.127  -27.109 -3.472  1.00 45.57  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -2.295  -28.190 -3.251  1.00 57.98  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -2.127  -29.077 -4.280  1.00 69.57  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -3.580  -24.580 2.871   1.00 28.99  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -3.544  -23.482 3.840   1.00 30.24  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.831  -22.304 3.152   1.00 30.33  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -2.112  -22.508 2.174   1.00 27.33  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.725  -24.047 5.011   1.00 31.07  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.855  -25.120 4.384   1.00 33.68  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -2.661  -25.679 3.227   1.00 35.21  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -3.090  -21.099 3.654   1.00 25.28  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -2.368  -19.902 3.203   1.00 25.00  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.871  -20.193 3.304   1.00 25.06  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? -0.420  -20.659 4.360   1.00 25.68  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.767  -18.689 4.042   1.00 24.63  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -4.212  -18.329 3.904   1.00 28.09  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -5.236  -19.008 4.548   1.00 29.39  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.791  -17.319 3.217   1.00 26.97  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -6.399  -18.428 4.239   1.00 28.22  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -6.160  -17.398 3.412   1.00 29.40  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? -0.099  -19.964 2.206   1.00 23.37  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.201   -20.611 2.070   1.00 22.97  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.272   -19.520 1.922   1.00 24.40  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.082   -18.621 1.111   1.00 23.02  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.229   -21.517 0.829   1.00 22.62  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 2.316   -22.558 0.878   1.00 23.51  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 3.656   -22.376 0.689   1.00 24.87  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.147   -23.956 1.222   1.00 26.31  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 4.324   -23.573 0.815   1.00 25.55  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 3.430   -24.557 1.169   1.00 29.07  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.049   -24.759 1.540   1.00 30.15  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 3.651   -25.914 1.435   1.00 30.96  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.269   -26.103 1.794   1.00 37.20  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 2.548   -26.677 1.757   1.00 32.87  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 3.426   -19.594 2.631   1.00 22.02  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 4.479   -18.572 2.482   1.00 20.17  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 4.979   -18.546 1.037   1.00 18.92  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.264   -19.592 0.432   1.00 21.49  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 5.570   -19.002 3.489   1.00 21.62  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 5.354   -20.508 3.636   1.00 21.35  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 3.813   -20.649 3.581   1.00 20.19  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.054   -17.337 0.469   1.00 17.71  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 5.341   -17.215 -0.958  1.00 19.08  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 5.942   -15.832 -1.268  1.00 18.33  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 5.965   -14.919 -0.439  1.00 19.09  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.086   -17.524 -1.814  1.00 20.15  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 6.453   -15.694 -2.509  1.00 20.04  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 6.865   -14.380 -2.993  1.00 19.75  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.299   -14.103 -4.386  1.00 17.99  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.027   -15.049 -5.140  1.00 20.11  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 8.402   -14.190 -2.937  1.00 18.30  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.136   -15.117 -3.897  1.00 18.45  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 10.686  -14.865 -3.758  1.00 18.50  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.266  -15.767 -4.783  1.00 20.42  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 12.572  -16.147 -4.720  1.00 21.09  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.254  -15.988 -3.601  1.00 22.83  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.102  -16.777 -5.760  1.00 23.29  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.168   -12.807 -4.723  1.00 17.83  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 5.941   -12.459 -6.124  1.00 18.67  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.284   -12.551 -6.842  1.00 21.52  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.243   -11.881 -6.463  1.00 21.62  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 5.420   -11.020 -6.246  1.00 19.98  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 4.241   -10.647 -5.288  1.00 28.69  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.203   -10.687 -7.731  1.00 21.63  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 2.874   -11.133 -5.658  1.00 32.89  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 7.328   -13.364 -7.894  1.00 21.15  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 8.598   -13.567 -8.578  1.00 24.36  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 8.733   -12.604 -9.752  1.00 25.12  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 7.767   -11.986 -10.190 1.00 24.39  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 8.692   -14.955 -9.163  1.00 22.79  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 9.695   -15.895 -8.529  1.00 25.74  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.330  -15.539 -7.506  1.00 29.65  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 9.762   -17.010 -8.995  1.00 27.24  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 9.999   -12.408 -10.177 1.00 30.02  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.298  -11.781 -11.445 1.00 34.03  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.032  -12.806 -12.542 1.00 28.19  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 9.920   -13.988 -12.291 1.00 30.23  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 11.777  -11.409 -11.544 1.00 35.19  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.229  -10.221 -10.694 1.00 43.89  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 11.880  -9.068  -11.056 1.00 46.58  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 12.938  -10.455 -9.681  1.00 50.68  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 9.880   -12.328 -13.771 1.00 33.47  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 9.840   -13.206 -14.936 1.00 32.46  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.190  -13.026 -15.614 1.00 30.16  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.538  -11.885 -15.901 1.00 31.10  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 8.713   -12.719 -15.855 1.00 33.79  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.346   -12.715 -15.151 1.00 39.84  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 8.688   -13.522 -17.159 1.00 30.31  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.433   -11.591 -15.613 1.00 37.84  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 11.942  -14.119 -15.785 1.00 30.82  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.267  -14.018 -16.400 1.00 30.88  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.090  -13.650 -17.875 1.00 31.50  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.030  -13.869 -18.477 1.00 31.16  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.034  -15.312 -16.240 1.00 32.02  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.099  -12.944 -18.400 1.00 29.26  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.094  -12.727 -19.843 1.00 30.34  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 13.992  -14.089 -20.513 1.00 24.79  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.701  -15.022 -20.143 1.00 31.25  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.387  -12.028 -20.209 1.00 32.17  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.367  -10.521 -20.042 1.00 34.79  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.276  -9.918  -20.137 1.00 40.28  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 16.465  -9.966  -19.890 1.00 39.94  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.115  -14.188 -21.524 1.00 28.51  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 12.953  -15.405 -22.296 1.00 29.45  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 11.979  -16.403 -21.673 1.00 36.33  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.686  -17.419 -22.298 1.00 32.90  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.495  -16.119 -20.446 1.00 31.87  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.634  -17.060 -19.727 1.00 33.62  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.154   -16.813 -20.039 1.00 29.97  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 8.743   -15.738 -20.461 1.00 29.80  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 10.909  -16.966 -18.222 1.00 35.41  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.323   -17.822 -19.746 1.00 34.56  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 6.881   -17.736 -19.929 1.00 28.93  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.254   -16.706 -18.984 1.00 29.51  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.495   -16.736 -17.776 1.00 34.87  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.340   -19.161 -19.657 1.00 32.86  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 4.815   -19.170 -19.646 1.00 35.93  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 6.891   -20.157 -20.688 1.00 32.17  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.505   -15.767 -19.570 1.00 33.03  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 4.773   -14.719 -18.871 1.00 31.50  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.481   -15.297 -18.297 1.00 35.18  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 2.927   -16.250 -18.839 1.00 34.78  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.421   -13.514 -19.749 1.00 34.29  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 5.675   -12.730 -20.227 1.00 34.90  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.290   -11.557 -21.123 1.00 41.68  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.044   -11.932 -22.549 1.00 41.86  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 4.866   -10.701 -23.322 1.00 45.81  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 2.978   -14.724 -17.179 1.00 36.47  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 1.677   -15.111 -16.624 1.00 32.42  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.571   -14.576 -17.513 1.00 32.18  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 0.777   -13.641 -18.287 1.00 34.51  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 1.610   -14.440 -15.218 1.00 34.05  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.712   -13.399 -15.206 1.00 41.09  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.672   -13.718 -16.363 1.00 35.74  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.674  -15.073 -17.363 1.00 35.47  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.821  -14.399 -17.978 1.00 36.66  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -2.023  -12.983 -17.472 1.00 40.96  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.521  -12.635 -16.396 1.00 32.04  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -3.020  -15.254 -17.564 1.00 38.98  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.436  -16.557 -17.099 1.00 34.80  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -1.038  -16.280 -16.594 1.00 36.60  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.811  -12.151 -18.199 1.00 39.42  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -3.226  -10.835 -17.710 1.00 43.44  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.879  -10.868 -16.329 1.00 36.08  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.591  -11.815 -15.979 1.00 38.66  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -4.203  -10.327 -18.800 1.00 47.05  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.599  -11.575 -19.545 1.00 42.25  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.333  -12.428 -19.557 1.00 46.87  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -3.572  -9.827  -15.564 1.00 38.05  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.978  -9.616  -14.189 1.00 36.95  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -3.543  -10.752 -13.259 1.00 34.52  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -4.035  -10.781 -12.129 1.00 36.24  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -5.456  -9.261  -14.067 1.00 43.78  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.756  -8.033  -14.887 1.00 47.75  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.578  -6.906  -14.406 1.00 49.77  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.087  -8.234  -16.153 1.00 51.03  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.573  -11.598 -13.673 1.00 30.61  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -2.025  -12.604 -12.754 1.00 24.96  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? -0.519  -12.346 -12.518 1.00 24.70  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.133   -11.688 -13.321 1.00 26.46  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -2.200  -14.059 -13.193 1.00 28.91  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.653  -14.474 -13.560 1.00 33.12  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.585  -14.187 -12.392 1.00 37.42  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -6.053  -14.517 -12.631 1.00 46.01  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -6.245  -15.969 -12.662 1.00 48.01  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? -0.031  -12.735 -11.334 1.00 19.97  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.364   -12.589 -10.934 1.00 21.25  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 1.982   -13.972 -10.824 1.00 21.22  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.320   -14.936 -10.447 1.00 22.46  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 1.486   -12.005 -9.504  1.00 21.68  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 0.944   -10.585 -9.465  1.00 24.93  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? -0.417  -10.336 -9.310  1.00 29.50  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 1.791   -9.514  -9.686  1.00 26.25  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.907  -9.033  -9.332  1.00 31.49  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.317   -8.209  -9.701  1.00 28.77  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? -0.038  -7.983  -9.514  1.00 28.78  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.544  -6.717  -9.618  1.00 33.34  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.292   -14.122 -11.096 1.00 21.70  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 3.963   -15.406 -10.885 1.00 20.00  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.271   -15.557 -9.400  1.00 21.14  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 4.961   -14.706 -8.843  1.00 24.18  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.230   -15.285 -11.738 1.00 22.46  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 5.430   -13.823 -11.925 1.00 22.23  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.174   -13.034 -11.554 1.00 24.34  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 3.692   -16.573 -8.755  1.00 18.42  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 3.869   -16.747 -7.310  1.00 17.74  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 4.819   -17.904 -7.103  1.00 21.13  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 4.528   -19.033 -7.530  1.00 23.16  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 2.513   -16.931 -6.599  1.00 19.46  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 1.575   -15.739 -6.944  1.00 20.08  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 2.736   -17.111 -5.079  1.00 20.09  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.130   -14.364 -6.582  1.00 20.85  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 5.932   -17.638 -6.394  1.00 18.86  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 6.834   -18.714 -6.023  1.00 19.94  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 6.563   -19.137 -4.581  1.00 20.51  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 6.653   -18.325 -3.659  1.00 22.04  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.287   -18.190 -6.146  1.00 19.50  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 9.322   -19.239 -5.740  1.00 23.73  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 9.686   -20.244 -6.640  1.00 25.57  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 9.874   -19.264 -4.457  1.00 25.93  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 10.633  -21.206 -6.279  1.00 29.61  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 10.810  -20.232 -4.090  1.00 27.42  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.187  -21.211 -5.014  1.00 26.75  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.173   -20.414 -4.394  1.00 20.57  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 5.828   -20.936 -3.079  1.00 19.32  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.108   -21.431 -2.408  1.00 21.25  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 7.806   -22.304 -2.964  1.00 23.23  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 4.839   -22.111 -3.259  1.00 23.61  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 3.462   -21.600 -3.676  1.00 21.04  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.165   -21.347 -5.009  1.00 25.09  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 2.481   -21.345 -2.720  1.00 25.49  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 1.927   -20.787 -5.368  1.00 25.81  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.244   -20.798 -3.079  1.00 25.24  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 0.963   -20.551 -4.398  1.00 26.26  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 7.432   -20.863 -1.245  1.00 21.26  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 8.572   -21.373 -0.488  1.00 23.15  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.311   -22.810 -0.035  1.00 24.78  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.157   -23.261 0.083   1.00 26.89  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 8.814   -20.495 0.748   1.00 24.25  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.254   -19.093 0.359   1.00 20.01  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 10.500  -18.887 -0.244  1.00 21.22  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 8.474   -17.960 0.619   1.00 20.56  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 10.924  -17.605 -0.598  1.00 21.45  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 8.914   -16.665 0.277   1.00 22.10  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.141  -16.478 -0.351  1.00 22.96  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 9.401   -23.545 0.162   1.00 24.98  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.278   -24.906 0.660   1.00 25.37  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.040   -25.913 -0.468  1.00 30.28  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 9.911   -26.750 -0.751  1.00 31.55  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 7.899   -25.799 -1.170  1.00 28.76  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 7.644   -26.650 -2.323  1.00 29.25  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 8.465   -26.199 -3.525  1.00 29.23  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 8.792   -27.002 -4.407  1.00 30.19  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.157   -26.685 -2.657  1.00 30.34  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 5.821   -25.354 -3.054  1.00 29.90  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.275   -27.131 -1.510  1.00 34.72  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 8.762   -24.887 -3.594  1.00 26.22  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 9.475   -24.273 -4.708  1.00 25.53  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 8.676   -24.372 -6.017  1.00 27.73  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.267   -24.302 -7.090  1.00 32.06  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 10.916  -24.805 -4.846  1.00 27.22  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 11.649  -24.838 -3.542  1.00 30.19  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 12.449  -25.884 -3.114  1.00 28.56  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 11.658  -23.923 -2.532  1.00 26.45  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 12.907  -25.611 -1.893  1.00 34.73  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 12.473  -24.406 -1.534  1.00 28.85  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 7.337   -24.450 -5.925  1.00 29.62  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 6.468   -24.496 -7.090  1.00 29.93  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.044   -23.081 -7.461  1.00 26.93  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.137   -22.191 -6.614  1.00 26.96  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.222   -25.321 -6.752  1.00 31.54  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 5.555   -26.804 -6.604  1.00 41.70  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 4.409   -27.641 -6.076  1.00 49.31  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 3.243   -27.175 -6.054  1.00 53.06  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 4.729   -28.762 -5.629  1.00 59.58  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 5.672   -22.879 -8.731  1.00 26.89  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.137   -21.592 -9.181  1.00 24.82  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 3.679   -21.800 -9.579  1.00 27.20  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 3.350   -22.776 -10.268 1.00 29.74  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 5.938   -20.968 -10.336 1.00 28.91  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.261   -20.595 -9.928  1.00 27.18  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 5.266   -19.734 -10.935 1.00 29.41  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 2.811   -20.853 -9.205  1.00 24.35  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 1.484   -20.782 -9.807  1.00 23.74  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.168   -19.323 -10.138 1.00 24.78  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 1.834   -18.405 -9.643  1.00 24.18  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 0.452   -21.342 -8.854  1.00 25.22  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.123   -19.101 -10.951 1.00 24.03  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? -0.268  -17.753 -11.311 1.00 26.30  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -1.513  -17.377 -10.518 1.00 29.53  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -2.550  -18.061 -10.612 1.00 29.46  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? -0.519  -17.713 -12.825 1.00 28.64  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 0.681   -18.092 -13.682 1.00 29.42  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 1.899   -17.443 -13.551 1.00 33.20  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 0.553   -19.056 -14.686 1.00 35.92  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 2.983   -17.783 -14.350 1.00 41.37  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 1.634   -19.368 -15.503 1.00 35.83  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 2.851   -18.763 -15.314 1.00 35.09  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -1.422  -16.270 -9.760  1.00 24.05  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -2.532  -15.890 -8.901  1.00 23.54  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.811  -14.399 -9.029  1.00 23.99  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.929  -13.593 -9.329  1.00 22.79  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -2.270  -16.219 -7.428  1.00 23.93  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -2.082  -17.693 -7.098  1.00 24.81  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.725  -17.717 -5.633  1.00 26.22  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -3.474  -18.312 -7.307  1.00 28.52  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -4.073  -14.031 -8.753  1.00 21.61  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -4.399  -12.612 -8.690  1.00 22.76  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -4.418  -12.118 -7.235  1.00 20.10  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -4.374  -12.936 -6.298  1.00 20.51  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -4.487  -10.784 -7.029  1.00 22.04  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -4.425  -10.196 -5.687  1.00 23.18  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -5.414  -10.723 -4.649  1.00 22.21  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -5.132  -10.728 -3.457  1.00 21.00  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.563  -8.711  -5.950  1.00 24.92  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -4.042  -8.534  -7.358  1.00 22.80  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.544  -9.770  -8.094  1.00 22.56  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -6.583  -11.210 -5.106  1.00 22.09  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -7.522  -11.729 -4.102  1.00 23.04  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -7.011  -12.918 -3.287  1.00 23.69  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -7.478  -13.177 -2.158  1.00 22.29  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.808  -12.211 -4.796  1.00 27.87  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.655  -13.493 -5.608  1.00 28.56  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.955  -13.740 -6.399  1.00 38.15  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.863  -14.957 -7.269  1.00 36.63  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.691  -16.142 -6.418  1.00 38.14  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.958  -13.581 -3.795  1.00 22.84  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -5.370  -14.715 -3.131  1.00 22.19  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -4.026  -14.373 -2.472  1.00 21.09  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -3.343  -15.286 -2.028  1.00 22.28  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -5.301  -15.859 -4.135  1.00 23.34  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.690  -16.444 -4.413  1.00 27.87  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -7.474  -16.526 -3.435  1.00 29.45  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.985  -16.801 -5.576  1.00 30.44  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.680  -13.074 -2.401  1.00 19.32  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -2.327  -12.673 -1.954  1.00 18.99  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -2.458  -11.810 -0.686  1.00 17.59  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -3.066  -10.727 -0.723  1.00 20.94  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.561  -11.936 -3.051  1.00 19.66  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -1.439  -12.667 -4.385  1.00 21.55  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.741  -11.793 -5.414  1.00 20.44  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.691  -14.005 -4.180  1.00 20.74  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.936  -12.321 0.433   1.00 18.19  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -2.002  -11.638 1.732   1.00 18.94  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? -0.622  -11.152 2.157   1.00 20.76  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.297   -11.964 2.329   1.00 22.84  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -2.500  -12.663 2.751   1.00 20.39  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.944  -13.084 2.476   1.00 21.91  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -4.235  -13.981 1.443   1.00 23.77  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.989  -12.539 3.215   1.00 24.64  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -5.542  -14.398 1.186   1.00 26.98  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -6.294  -12.930 2.916   1.00 23.59  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -6.573  -13.861 1.942   1.00 24.14  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? -0.380  -9.833  2.229   1.00 23.53  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 0.958   -9.332  2.570   1.00 21.78  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 1.507   -9.954  3.847   1.00 20.17  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 0.799   -10.137 4.837   1.00 22.29  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 0.792   -7.803  2.630   1.00 25.43  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? -0.321  -7.536  1.575   1.00 28.16  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -1.280  -8.732  1.840   1.00 25.31  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 2.789   -10.386 3.791   1.00 22.14  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.388   -11.214 4.824   1.00 22.86  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 3.426   -10.529 6.193   1.00 23.64  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.016   -11.172 7.151   1.00 27.18  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 4.789   -11.667 4.359   1.00 24.34  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 5.571   -12.425 5.436   1.00 22.77  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.277   -13.746 5.693   1.00 24.69  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 6.627   -11.824 6.119   1.00 28.51  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 5.962   -14.489 6.643   1.00 26.80  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.343   -12.567 7.061   1.00 27.47  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.004   -13.881 7.316   1.00 29.99  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 7.649   -14.668 8.249   1.00 31.78  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 3.841   -9.253  6.249   1.00 25.05  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.011   -8.591  7.550   1.00 30.09  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 2.683   -8.537  8.319   1.00 31.10  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 2.625   -8.913  9.495   1.00 33.57  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 4.616   -7.212  7.363   1.00 30.42  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.102   -7.112  7.027   1.00 49.91  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 6.844   -8.081  7.292   1.00 51.71  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 6.519   -6.039  6.506   1.00 65.44  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 1.611   -8.130  7.621   1.00 31.35  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.268   -8.051  8.203   1.00 31.45  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? -0.268  -9.423  8.624   1.00 30.09  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.988  -9.528  9.632   1.00 27.98  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.677  -7.393  7.188   1.00 28.21  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -2.155  -7.289  7.616   1.00 31.10  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.872  -6.521  6.516   1.00 33.41  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -4.012  -5.736  7.073   1.00 34.74  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.951  -6.605  7.761   1.00 37.17  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.076   -10.494 7.885   1.00 26.55  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? -0.587  -11.790 8.002   1.00 26.56  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.184   -12.853 8.793   1.00 26.83  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? -0.356  -13.932 9.003   1.00 26.72  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.877  -12.341 6.609   1.00 31.64  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.841  -11.492 6.018   1.00 40.52  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 1.438   -12.583 9.179   1.00 27.77  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.277   -13.670 9.692   1.00 30.56  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 1.815   -14.193 11.057  1.00 29.32  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 1.984   -15.371 11.365  1.00 32.03  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 3.770   -13.310 9.654   1.00 31.30  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.138   -12.101 10.454  1.00 36.62  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 5.650   -11.964 10.340  1.00 46.95  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.192   -10.918 11.273  1.00 56.26  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 5.904   -9.551  10.817  1.00 59.04  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.193   -13.326 11.865  0.50 33.50  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.218   -13.329 11.883  0.50 32.69  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 0.702   -13.742 13.177  0.50 36.35  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 0.695   -13.797 13.162  0.50 34.54  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? -0.462  -14.731 13.035  0.50 34.90  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? -0.338  -14.896 12.921  0.50 33.39  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? -0.688  -15.556 13.908  0.50 36.55  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? -0.339  -15.934 13.578  0.50 31.73  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.475   -12.550 14.103  0.50 37.51  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.104   -12.656 13.975  0.50 35.24  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 1.728   -11.886 14.673  0.50 42.05  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? -0.203  -12.988 15.428  0.50 38.75  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 2.819   -12.499 14.607  0.50 37.32  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 0.751   -13.030 16.244  0.50 40.86  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.620   -10.745 15.180  0.50 44.19  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -1.394  -13.215 15.731  0.50 40.44  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -1.184  -14.689 11.908  1.00 31.36  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -2.308  -15.581 11.679  1.00 29.93  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.871  -16.855 10.972  1.00 33.73  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -2.333  -17.942 11.297  1.00 30.13  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -3.350  -14.796 10.879  1.00 32.35  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -4.662  -15.524 10.679  1.00 38.78  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -5.694  -14.578 10.051  1.00 45.31  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -7.027  -15.244 9.850   1.00 53.50  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -8.055  -14.322 9.354   1.00 51.78  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.975  -16.726 9.983   1.00 29.86  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.807  -17.808 9.030   1.00 29.07  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 0.579   -18.455 9.157   1.00 28.17  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 0.778   -19.525 8.585   1.00 28.69  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.946  -17.297 7.585   1.00 24.01  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -2.349  -16.863 7.188   1.00 28.16  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -3.474  -17.628 7.530   1.00 28.42  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -2.548  -15.689 6.459   1.00 27.36  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.758  -17.220 7.176   1.00 29.28  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.824  -15.291 6.075   1.00 29.25  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.926  -16.029 6.478   1.00 29.15  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -6.152  -15.591 6.064   1.00 31.36  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 1.481   -17.855 9.939   1.00 27.51  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 2.873   -18.296 9.990   1.00 29.88  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.104   -19.254 11.164  1.00 30.15  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 3.833   -18.923 12.074  1.00 36.87  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 2.374   -20.360 11.172  1.00 35.95  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 2.488   -21.369 12.214  1.00 37.47  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 2.747   -22.700 11.517  1.00 31.48  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 2.324   -22.908 10.386  1.00 33.09  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.226   -21.421 13.089  1.00 39.21  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 0.794   -20.099 13.738  1.00 44.20  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? 0.410   -20.199 15.212  1.00 53.21  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 3.475   -23.657 12.155  1.00 33.43  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 3.747   -24.949 11.517  1.00 32.46  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 2.510   -25.696 11.051  1.00 36.36  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 1.440   -25.558 11.646  1.00 39.11  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 4.539   -25.697 12.604  1.00 35.25  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.204   -24.587 13.367  1.00 37.02  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.128   -23.497 13.462  1.00 35.56  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 2.671   -26.427 9.956   1.00 35.63  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 1.589   -27.112 9.289   1.00 45.14  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 2.126   -28.476 8.874   1.00 51.48  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 3.306   -28.615 8.546   1.00 44.52  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.047   -26.235 8.162   1.00 45.22  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? -0.271  -26.709 7.608   1.00 49.77  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? -0.306  -27.693 6.868   1.00 48.58  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -1.352  -26.000 7.907   1.00 55.67  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 1.242   -29.480 8.911   1.00 52.51  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 1.620   -30.845 8.604   1.00 51.35  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.048   -30.970 7.144   1.00 49.74  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 2.799   -31.887 6.806   1.00 49.26  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 0.484   -31.800 9.007   1.00 56.18  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? -0.799  -31.756 8.176   1.00 61.30  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 1.600   -30.035 6.286   1.00 42.63  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 1.661   -30.202 4.838   1.00 42.49  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.106   -30.197 4.332   1.00 39.91  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 3.944   -29.461 4.850   1.00 38.87  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 0.795   -29.153 4.122   1.00 44.32  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? -0.690  -29.385 4.343   1.00 48.61  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -1.145  -30.576 3.508   1.00 47.22  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -2.060  -30.179 2.433   1.00 60.37  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -3.212  -29.506 2.593   1.00 58.56  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -3.972  -29.258 1.545   1.00 52.39  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -3.616  -29.105 3.793   1.00 63.25  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 3.350   -30.988 3.283   1.00 36.45  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 4.692   -31.195 2.751   1.00 38.65  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 5.294   -29.859 2.318   1.00 32.18  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 4.751   -29.166 1.461   1.00 32.96  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 4.709   -32.108 1.517   1.00 41.43  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.089   -32.392 0.915   1.00 42.86  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 6.157   -33.433 -0.202  1.00 46.50  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 7.554   -33.788 -0.615  1.00 51.98  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 6.449   -29.527 2.890   1.00 34.83  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 7.135   -28.363 2.366   1.00 29.97  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 6.773   -27.100 3.137   1.00 28.90  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 7.514   -26.120 3.040   1.00 30.47  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 5.714   -27.137 3.943   1.00 28.00  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 5.256   -25.914 4.577   1.00 29.63  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 6.296   -25.332 5.546   1.00 28.79  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 6.520   -24.125 5.596   1.00 28.34  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 3.933   -26.168 5.300   1.00 29.33  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 3.200   -24.887 5.672   1.00 29.68  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 3.455   -24.256 6.881   1.00 28.81  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 2.282   -24.307 4.776   1.00 29.06  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 2.816   -23.072 7.244   1.00 31.33  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 1.631   -23.131 5.155   1.00 26.23  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 1.925   -22.510 6.363   1.00 25.42  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 6.882   -26.171 6.414   1.00 25.42  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 7.679   -25.649 7.512   1.00 24.67  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.041   -25.198 6.967   1.00 25.90  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 9.650   -24.247 7.481   1.00 27.96  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 7.846   -26.740 8.570   1.00 29.38  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 6.546   -27.018 9.302   1.00 37.44  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 5.633   -26.182 9.325   1.00 29.79  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 6.457   -28.169 9.966   1.00 33.04  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 9.508   -25.888 5.915   1.00 24.30  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 10.681  -25.426 5.185   1.00 27.64  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 10.364  -24.046 4.617   1.00 25.38  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 11.207  -23.123 4.661   1.00 24.99  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 11.038  -26.357 4.032   1.00 26.55  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 12.327  -25.926 3.311   1.00 28.30  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 12.858  -26.973 2.350   1.00 37.49  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 12.246  -28.053 2.224   1.00 46.41  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 13.896  -26.717 1.730   1.00 39.14  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 9.124   -23.920 4.129   1.00 27.04  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 8.667   -22.647 3.553   1.00 24.59  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 8.688   -21.503 4.574   1.00 21.86  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.058   -20.354 4.259   1.00 22.68  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 8.260   -21.798 5.807   1.00 21.77  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 8.285   -20.806 6.868   1.00 23.01  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 9.722   -20.343 7.098   1.00 23.80  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 9.987   -19.170 7.309   1.00 22.89  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 7.658   -21.333 8.160   1.00 24.28  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.161   -21.635 8.058   1.00 27.42  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 5.773   -22.182 9.429   1.00 28.68  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 5.340   -20.399 7.792   1.00 26.89  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 10.680  -21.289 7.064   1.00 23.96  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.060  -20.912 7.315   1.00 23.84  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 12.560  -19.983 6.215   1.00 22.20  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 13.215  -18.968 6.490   1.00 22.78  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 12.991  -22.141 7.477   1.00 23.82  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 14.435  -21.756 7.717   1.00 24.76  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.048  -21.581 8.930   1.00 26.32  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 15.422  -21.451 6.711   1.00 25.45  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 16.359  -21.233 8.747   1.00 25.64  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 16.599  -21.101 7.397   1.00 25.59  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 15.405  -21.412 5.306   1.00 25.95  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 17.772  -20.744 6.720   1.00 23.74  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 16.547  -21.028 4.628   1.00 27.07  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 17.711  -20.682 5.336   1.00 27.55  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 12.225  -20.327 4.974   1.00 21.31  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 12.745  -19.584 3.828   1.00 18.71  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 12.222  -18.148 3.862   1.00 21.55  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 12.971  -17.192 3.647   1.00 21.64  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 12.370  -20.229 2.505   1.00 20.47  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.038  -21.604 2.418   1.00 21.30  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 12.664  -22.350 1.143   1.00 25.34  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 11.750  -21.905 0.435   1.00 28.12  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 13.251  -23.429 0.847   1.00 26.54  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 10.925  -17.981 4.118   1.00 20.34  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 10.359  -16.640 4.011   1.00 21.00  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 10.938  -15.730 5.103   1.00 22.81  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.081  -14.525 4.885   1.00 22.03  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 8.804   -16.646 4.011   1.00 21.61  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.190   -15.259 3.563   1.00 18.93  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 8.180   -17.096 5.370   1.00 19.52  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 6.744   -15.362 3.061   1.00 20.16  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 11.224  -16.303 6.291   1.00 22.42  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 11.752  -15.549 7.431   1.00 22.75  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 13.252  -15.282 7.319   1.00 24.72  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 13.704  -14.203 7.718   1.00 25.81  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 11.393  -16.284 8.731   1.00 24.10  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 11.928  -15.600 9.982   1.00 30.60  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 11.310  -16.115 11.273  1.00 38.55  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 10.886  -17.279 11.373  1.00 35.94  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.224  -15.224 12.255  1.00 39.47  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 13.988  -16.240 6.740   1.00 21.03  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 15.447  -16.247 6.843   1.00 22.46  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.183  -15.933 5.550   1.00 22.31  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 17.283  -15.355 5.612   1.00 23.34  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 15.946  -17.523 7.510   1.00 21.61  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 15.478  -17.571 8.946   1.00 25.96  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 15.838  -16.686 9.739   1.00 28.25  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 14.556  -18.469 9.248   1.00 25.68  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 15.632  -16.299 4.376   1.00 21.41  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 16.291  -15.889 3.140   1.00 20.23  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 15.280  -15.813 1.992   1.00 22.08  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 15.308  -16.587 1.015   1.00 22.55  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 17.440  -16.840 2.789   1.00 22.16  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 18.479  -16.207 1.877   1.00 24.97  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 18.243  -15.196 1.174   1.00 22.43  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 19.679  -16.800 1.894   1.00 27.15  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 14.327  -14.859 2.098   1.00 21.85  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.178  -14.850 1.198   1.00 20.60  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 13.515  -14.421 -0.226  1.00 21.20  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 12.725  -14.675 -1.115  1.00 21.78  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 12.243  -13.867 1.868   1.00 20.51  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.198  -12.896 2.547   1.00 19.96  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.263  -13.833 3.150   1.00 21.35  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 14.730  -13.860 -0.462  1.00 18.68  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.049  -13.354 -1.802  1.00 19.46  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.189  -14.151 -2.461  1.00 21.43  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 16.700  -13.785 -3.531  1.00 23.18  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 15.471  -11.869 -1.673  1.00 19.68  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 14.421  -10.998 -1.055  1.00 19.53  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.166  -10.914 -1.640  1.00 18.45  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 14.357  -10.305 0.094   1.00 21.16  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 12.409  -10.082 -0.927  1.00 20.95  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.109  -9.703  0.128   1.00 21.65  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 16.472  -15.346 -1.911  1.00 21.09  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 17.551  -16.146 -2.492  1.00 21.93  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.095  -16.858 -3.761  1.00 23.69  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 15.911  -17.052 -4.013  1.00 24.45  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.060  -17.151 -1.459  1.00 23.64  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.087  -17.403 -4.482  1.00 24.72  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 17.857  -18.354 -5.548  1.00 26.68  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 17.536  -19.734 -4.968  1.00 27.72  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 18.307  -20.300 -4.186  1.00 30.81  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 19.072  -18.400 -6.442  1.00 29.31  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 18.840  -19.442 -7.366  1.00 39.50  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 16.381  -20.291 -5.347  1.00 25.39  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 15.986  -21.613 -4.910  1.00 30.30  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 15.881  -22.545 -6.119  1.00 36.38  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 15.326  -23.631 -6.003  1.00 41.85  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 14.626  -21.592 -4.188  1.00 27.95  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 14.762  -20.986 -2.800  1.00 27.22  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.192  -21.749 -1.719  1.00 27.61  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 14.463  -19.638 -2.573  1.00 27.62  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 15.376  -21.189 -0.460  1.00 29.91  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 14.590  -19.085 -1.308  1.00 26.02  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.055  -19.853 -0.245  1.00 26.36  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 15.254  -19.350 1.020   1.00 29.40  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 16.419  -22.103 -7.259  1.00 38.09  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 16.535  -22.913 -8.467  1.00 56.95  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 17.116  -24.297 -8.136  1.00 68.93  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 18.144  -24.337 -7.414  1.00 72.96  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 17.388  -22.220 -9.505  1.00 53.33  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 16.981  -20.870 -9.674  1.00 66.26  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 16.533  -25.289 -8.630  1.00 85.26  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 38.825  -11.447 -41.811 1.00 74.44  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.411  -12.244 -42.997 1.00 75.74  ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 36.882  -12.299 -43.034 1.00 66.78  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.239  -12.532 -42.009 1.00 68.01  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.014  -13.655 -42.933 1.00 83.14  ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.350  -14.285 -44.283 1.00 96.85  ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.659  -13.517 -45.266 1.00 95.02  ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 42.020  -13.305 -44.107 1.00 97.77  ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.243  -12.041 -44.201 1.00 53.17  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 34.801  -12.253 -44.336 1.00 50.99  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.481  -13.689 -43.910 1.00 55.00  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.280  -14.596 -44.135 1.00 48.59  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.482  -11.941 -45.813 1.00 51.78  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.660  -11.084 -46.272 1.00 46.07  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 36.859  -11.486 -45.415 1.00 43.49  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.363  -13.858 -43.190 1.00 50.04  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.898  -15.170 -42.756 1.00 50.74  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.532  -15.442 -43.374 1.00 48.93  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 30.969  -14.561 -44.027 1.00 47.31  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 32.911  -15.266 -41.229 1.00 57.29  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.295  -15.428 -40.692 1.00 69.24  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.211  -16.276 -41.281 1.00 70.32  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 34.910  -14.881 -39.629 1.00 66.14  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.342  -16.233 -40.589 1.00 70.71  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.180  -15.389 -39.586 1.00 71.35  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 31.018  -16.672 -43.198 1.00 42.38  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.734  -17.000 -43.792 1.00 44.43  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.699  -15.996 -43.292 1.00 43.34  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.903  -15.481 -44.076 1.00 43.01  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.328  -18.408 -43.445 1.00 46.83  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.721  -15.769 -41.976 1.00 41.76  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 27.907  -14.745 -41.339 1.00 41.87  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.772  -13.524 -41.028 1.00 37.33  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 29.888  -13.662 -40.541 1.00 42.78  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.289  -15.218 -40.019 1.00 44.15  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.204  -16.284 -40.127 1.00 36.58  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 24.872  -15.929 -40.323 1.00 32.53  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.517  -17.631 -39.967 1.00 35.40  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 23.890  -16.907 -40.386 1.00 34.02  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.529  -18.607 -40.049 1.00 32.90  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.225  -18.248 -40.243 1.00 32.07  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.235  -12.330 -41.280 1.00 41.45  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 29.007  -11.121 -41.038 1.00 42.27  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.226  -10.190 -40.114 1.00 43.27  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 26.991  -10.250 -40.061 1.00 36.21  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 29.250  -10.416 -42.366 1.00 46.83  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.986  -10.062 -43.112 1.00 41.89  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 28.366  -9.895  -44.582 1.00 52.47  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 27.314  -9.200  -45.379 1.00 50.81  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 26.125  -10.042 -45.545 1.00 61.20  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 28.910  -9.259  -39.411 1.00 45.40  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.214  -8.332  -38.523 1.00 38.60  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.063  -7.611  -39.208 1.00 37.20  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.186  -7.173  -40.357 1.00 39.64  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.378  -7.441  -38.086 1.00 43.61  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.555  -8.398  -38.052 1.00 45.34  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.371  -9.036  -39.422 1.00 45.66  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 25.900  -7.572  -38.525 1.00 33.40  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.685  -6.969  -39.028 1.00 32.84  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.738  -7.974  -39.675 1.00 30.50  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.605  -7.637  -39.979 1.00 33.01  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.199  -9.213  -39.923 1.00 32.66  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.335  -10.243 -40.478 1.00 33.07  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.228  -10.557 -39.461 1.00 26.60  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.487  -10.553 -38.256 1.00 30.33  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 24.119  -11.513 -40.769 1.00 36.88  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 24.868  -11.564 -42.098 1.00 41.40  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.649  -10.666 -42.919 1.00 41.18  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.665  -12.520 -42.288 1.00 38.05  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 21.010  -10.738 -39.950 1.00 27.14  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.893  -10.954 -39.044 1.00 27.73  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.567  -12.437 -39.060 1.00 25.70  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.597  -13.044 -40.142 1.00 29.63  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.708  -10.119 -39.507 1.00 28.59  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 19.030  -8.609  -39.594 1.00 25.21  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.776  -7.896  -40.019 1.00 28.68  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.612  -8.137  -38.269 1.00 27.90  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.175  -12.985 -37.892 1.00 23.81  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 18.967  -14.433 -37.830 1.00 24.14  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.868  -14.678 -36.802 1.00 27.31  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.458  -13.753 -36.083 1.00 25.19  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.270  -15.119 -37.370 1.00 27.23  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.442  -14.888 -38.345 1.00 27.84  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.669  -14.776 -35.920 1.00 27.69  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.385  -15.931 -36.765 1.00 24.80  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 16.841  -16.484 -35.539 1.00 24.98  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 17.946  -17.353 -34.953 1.00 26.94  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.559  -18.134 -35.708 1.00 26.90  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.583  -17.313 -35.795 1.00 22.70  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.393  -16.483 -36.208 1.00 25.69  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.179  -16.156 -37.549 1.00 29.27  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.474  -16.057 -35.247 1.00 27.61  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 13.084  -15.400 -37.927 1.00 31.12  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.375  -15.288 -35.635 1.00 26.55  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.168  -14.997 -36.976 1.00 33.85  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.149  -17.241 -33.615 1.00 23.27  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.206  -17.961 -32.935 1.00 23.31  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.585  -18.904 -31.896 1.00 25.28  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.642  -18.510 -31.216 1.00 25.21  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.140  -16.954 -32.289 1.00 26.18  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 19.060  -20.154 -31.847 1.00 26.18  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.424  -21.182 -31.012 1.00 25.87  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.301  -21.527 -29.821 1.00 27.21  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.466  -21.882 -29.984 1.00 31.00  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.174  -22.436 -31.874 1.00 27.13  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 17.392  -23.567 -31.161 1.00 25.51  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 15.936  -23.198 -30.868 1.00 27.08  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.083  -24.295 -30.154 1.00 28.97  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 15.580  -24.464 -28.793 1.00 28.80  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 18.704  -21.398 -28.629 1.00 27.32  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.306  -21.761 -27.352 1.00 29.71  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.416  -22.813 -26.692 1.00 28.82  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.193  -22.756 -26.817 1.00 27.53  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.512  -20.503 -26.507 1.00 34.52  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.625  -19.675 -27.101 1.00 40.18  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 21.343  -18.504 -25.943 1.00 46.84  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 21.826  -19.433 -24.480 1.00 43.92  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 19.057  -23.802 -26.057 1.00 30.24  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.290  -24.805 -25.333 1.00 33.49  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.346  -24.123 -24.330 1.00 30.74  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 17.762  -23.231 -23.593 1.00 35.13  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.268  -25.755 -24.630 1.00 40.05  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 18.593  -26.941 -23.909 1.00 45.19  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 19.587  -27.785 -23.116 1.00 48.78  ? 16  LYS   B CD  1 
ATOM   881  N N   . GLY   B 1 18 ? 16.076  -24.511 -24.375 1.00 35.44  ? 17  GLY   B N   1 
ATOM   882  C CA  . GLY   B 1 18 ? 15.067  -23.971 -23.475 1.00 34.20  ? 17  GLY   B CA  1 
ATOM   883  C C   . GLY   B 1 18 ? 14.257  -22.819 -24.069 1.00 34.59  ? 17  GLY   B C   1 
ATOM   884  O O   . GLY   B 1 18 ? 13.332  -22.341 -23.413 1.00 34.18  ? 17  GLY   B O   1 
ATOM   885  N N   . TYR   B 1 19 ? 14.610  -22.350 -25.287 1.00 29.14  ? 18  TYR   B N   1 
ATOM   886  C CA  . TYR   B 1 19 ? 13.958  -21.151 -25.789 1.00 26.39  ? 18  TYR   B CA  1 
ATOM   887  C C   . TYR   B 1 19 ? 13.539  -21.412 -27.233 1.00 26.52  ? 18  TYR   B C   1 
ATOM   888  O O   . TYR   B 1 19 ? 14.211  -22.167 -27.928 1.00 30.90  ? 18  TYR   B O   1 
ATOM   889  C CB  . TYR   B 1 19 ? 15.003  -20.025 -25.749 1.00 25.51  ? 18  TYR   B CB  1 
ATOM   890  C CG  . TYR   B 1 19 ? 15.406  -19.698 -24.319 1.00 28.18  ? 18  TYR   B CG  1 
ATOM   891  C CD1 . TYR   B 1 19 ? 14.658  -18.793 -23.560 1.00 29.82  ? 18  TYR   B CD1 1 
ATOM   892  C CD2 . TYR   B 1 19 ? 16.489  -20.347 -23.728 1.00 31.34  ? 18  TYR   B CD2 1 
ATOM   893  C CE1 . TYR   B 1 19 ? 15.002  -18.548 -22.233 1.00 32.08  ? 18  TYR   B CE1 1 
ATOM   894  C CE2 . TYR   B 1 19 ? 16.852  -20.082 -22.415 1.00 35.35  ? 18  TYR   B CE2 1 
ATOM   895  C CZ  . TYR   B 1 19 ? 16.106  -19.172 -21.682 1.00 33.66  ? 18  TYR   B CZ  1 
ATOM   896  O OH  . TYR   B 1 19 ? 16.489  -18.950 -20.388 1.00 38.11  ? 18  TYR   B OH  1 
ATOM   897  N N   . PRO   B 1 20 ? 12.496  -20.725 -27.723 1.00 26.73  ? 19  PRO   B N   1 
ATOM   898  C CA  . PRO   B 1 20 ? 12.139  -20.774 -29.143 1.00 25.82  ? 19  PRO   B CA  1 
ATOM   899  C C   . PRO   B 1 20 ? 13.228  -20.070 -29.954 1.00 26.42  ? 19  PRO   B C   1 
ATOM   900  O O   . PRO   B 1 20 ? 13.966  -19.232 -29.431 1.00 27.01  ? 19  PRO   B O   1 
ATOM   901  C CB  . PRO   B 1 20 ? 10.832  -20.075 -29.234 1.00 26.00  ? 19  PRO   B CB  1 
ATOM   902  C CG  . PRO   B 1 20 ? 10.877  -19.061 -28.088 1.00 26.92  ? 19  PRO   B CG  1 
ATOM   903  C CD  . PRO   B 1 20 ? 11.681  -19.761 -26.971 1.00 25.89  ? 19  PRO   B CD  1 
ATOM   904  N N   . HIS   B 1 21 ? 13.352  -20.472 -31.228 1.00 24.09  ? 20  HIS   B N   1 
ATOM   905  C CA  . HIS   B 1 21 ? 14.220  -19.739 -32.159 1.00 24.37  ? 20  HIS   B CA  1 
ATOM   906  C C   . HIS   B 1 21 ? 13.979  -18.230 -32.025 1.00 23.57  ? 20  HIS   B C   1 
ATOM   907  O O   . HIS   B 1 21 ? 12.840  -17.780 -32.117 1.00 24.00  ? 20  HIS   B O   1 
ATOM   908  C CB  . HIS   B 1 21 ? 13.906  -20.215 -33.587 1.00 24.72  ? 20  HIS   B CB  1 
ATOM   909  C CG  . HIS   B 1 21 ? 14.174  -21.679 -33.789 1.00 26.54  ? 20  HIS   B CG  1 
ATOM   910  N ND1 . HIS   B 1 21 ? 13.270  -22.653 -33.385 1.00 26.89  ? 20  HIS   B ND1 1 
ATOM   911  C CD2 . HIS   B 1 21 ? 15.196  -22.336 -34.378 1.00 27.02  ? 20  HIS   B CD2 1 
ATOM   912  C CE1 . HIS   B 1 21 ? 13.747  -23.852 -33.720 1.00 28.08  ? 20  HIS   B CE1 1 
ATOM   913  N NE2 . HIS   B 1 21 ? 14.925  -23.703 -34.308 1.00 26.75  ? 20  HIS   B NE2 1 
ATOM   914  N N   . TRP   B 1 22 ? 15.036  -17.447 -31.806 1.00 24.37  ? 21  TRP   B N   1 
ATOM   915  C CA  . TRP   B 1 22 ? 14.821  -16.121 -31.207 1.00 23.73  ? 21  TRP   B CA  1 
ATOM   916  C C   . TRP   B 1 22 ? 15.326  -15.052 -32.180 1.00 24.67  ? 21  TRP   B C   1 
ATOM   917  O O   . TRP   B 1 22 ? 16.468  -15.207 -32.615 1.00 24.27  ? 21  TRP   B O   1 
ATOM   918  C CB  . TRP   B 1 22 ? 15.555  -16.014 -29.870 1.00 23.38  ? 21  TRP   B CB  1 
ATOM   919  C CG  . TRP   B 1 22 ? 15.046  -14.880 -29.010 1.00 23.39  ? 21  TRP   B CG  1 
ATOM   920  C CD1 . TRP   B 1 22 ? 15.309  -13.544 -29.140 1.00 24.09  ? 21  TRP   B CD1 1 
ATOM   921  C CD2 . TRP   B 1 22 ? 14.086  -14.991 -27.924 1.00 25.75  ? 21  TRP   B CD2 1 
ATOM   922  N NE1 . TRP   B 1 22 ? 14.580  -12.805 -28.229 1.00 25.37  ? 21  TRP   B NE1 1 
ATOM   923  C CE2 . TRP   B 1 22 ? 13.834  -13.679 -27.453 1.00 27.54  ? 21  TRP   B CE2 1 
ATOM   924  C CE3 . TRP   B 1 22 ? 13.437  -16.078 -27.315 1.00 25.53  ? 21  TRP   B CE3 1 
ATOM   925  C CZ2 . TRP   B 1 22 ? 12.945  -13.413 -26.401 1.00 28.52  ? 21  TRP   B CZ2 1 
ATOM   926  C CZ3 . TRP   B 1 22 ? 12.553  -15.806 -26.278 1.00 26.18  ? 21  TRP   B CZ3 1 
ATOM   927  C CH2 . TRP   B 1 22 ? 12.285  -14.494 -25.853 1.00 26.56  ? 21  TRP   B CH2 1 
ATOM   928  N N   . PRO   B 1 23 ? 14.582  -13.955 -32.495 1.00 24.47  ? 22  PRO   B N   1 
ATOM   929  C CA  . PRO   B 1 23 ? 15.121  -12.919 -33.409 1.00 24.33  ? 22  PRO   B CA  1 
ATOM   930  C C   . PRO   B 1 23 ? 16.426  -12.337 -32.858 1.00 24.59  ? 22  PRO   B C   1 
ATOM   931  O O   . PRO   B 1 23 ? 16.537  -11.994 -31.670 1.00 23.17  ? 22  PRO   B O   1 
ATOM   932  C CB  . PRO   B 1 23 ? 13.970  -11.861 -33.481 1.00 22.76  ? 22  PRO   B CB  1 
ATOM   933  C CG  . PRO   B 1 23 ? 13.200  -12.055 -32.160 1.00 24.82  ? 22  PRO   B CG  1 
ATOM   934  C CD  . PRO   B 1 23 ? 13.257  -13.572 -31.965 1.00 24.17  ? 22  PRO   B CD  1 
ATOM   935  N N   . ALA   B 1 24 ? 17.471  -12.238 -33.694 1.00 24.11  ? 23  ALA   B N   1 
ATOM   936  C CA  . ALA   B 1 24 ? 18.783  -11.855 -33.193 1.00 22.20  ? 23  ALA   B CA  1 
ATOM   937  C C   . ALA   B 1 24 ? 19.627  -11.301 -34.355 1.00 23.18  ? 23  ALA   B C   1 
ATOM   938  O O   . ALA   B 1 24 ? 19.166  -11.336 -35.494 1.00 26.01  ? 23  ALA   B O   1 
ATOM   939  C CB  . ALA   B 1 24 ? 19.478  -13.018 -32.530 1.00 23.38  ? 23  ALA   B CB  1 
ATOM   940  N N   . ARG   B 1 25 ? 20.812  -10.795 -33.999 1.00 27.67  ? 24  ARG   B N   1 
ATOM   941  C CA  . ARG   B 1 25 ? 21.795  -10.312 -34.965 1.00 25.48  ? 24  ARG   B CA  1 
ATOM   942  C C   . ARG   B 1 25 ? 23.187  -10.808 -34.615 1.00 24.70  ? 24  ARG   B C   1 
ATOM   943  O O   . ARG   B 1 25 ? 23.541  -11.069 -33.465 1.00 26.21  ? 24  ARG   B O   1 
ATOM   944  C CB  . ARG   B 1 25 ? 21.764  -8.788  -35.115 1.00 25.32  ? 24  ARG   B CB  1 
ATOM   945  C CG  . ARG   B 1 25 ? 22.379  -8.049  -33.947 1.00 25.64  ? 24  ARG   B CG  1 
ATOM   946  C CD  . ARG   B 1 25 ? 22.063  -6.559  -34.100 1.00 26.91  ? 24  ARG   B CD  1 
ATOM   947  N NE  . ARG   B 1 25 ? 22.677  -5.853  -32.972 1.00 26.37  ? 24  ARG   B NE  1 
ATOM   948  C CZ  . ARG   B 1 25 ? 22.420  -4.582  -32.603 1.00 26.31  ? 24  ARG   B CZ  1 
ATOM   949  N NH1 . ARG   B 1 25 ? 21.476  -3.907  -33.227 1.00 26.72  ? 24  ARG   B NH1 1 
ATOM   950  N NH2 . ARG   B 1 25 ? 23.117  -4.004  -31.621 1.00 26.78  ? 24  ARG   B NH2 1 
ATOM   951  N N   . ILE   B 1 26 ? 24.031  -10.875 -35.663 1.00 27.40  ? 25  ILE   B N   1 
ATOM   952  C CA  . ILE   B 1 26 ? 25.462  -11.053 -35.487 1.00 28.99  ? 25  ILE   B CA  1 
ATOM   953  C C   . ILE   B 1 26 ? 26.028  -9.684  -35.126 1.00 31.60  ? 25  ILE   B C   1 
ATOM   954  O O   . ILE   B 1 26 ? 25.743  -8.703  -35.812 1.00 31.47  ? 25  ILE   B O   1 
ATOM   955  C CB  . ILE   B 1 26 ? 26.111  -11.526 -36.797 1.00 32.07  ? 25  ILE   B CB  1 
ATOM   956  C CG1 . ILE   B 1 26 ? 25.344  -12.705 -37.388 1.00 30.65  ? 25  ILE   B CG1 1 
ATOM   957  C CG2 . ILE   B 1 26 ? 27.596  -11.835 -36.568 1.00 34.02  ? 25  ILE   B CG2 1 
ATOM   958  C CD1 . ILE   B 1 26 ? 25.399  -13.942 -36.524 1.00 32.29  ? 25  ILE   B CD1 1 
ATOM   959  N N   . ASP   B 1 27 ? 26.799  -9.641  -34.053 1.00 32.85  ? 26  ASP   B N   1 
ATOM   960  C CA  . ASP   B 1 27 ? 27.462  -8.401  -33.665 1.00 40.71  ? 26  ASP   B CA  1 
ATOM   961  C C   . ASP   B 1 27 ? 28.935  -8.464  -34.079 1.00 44.65  ? 26  ASP   B C   1 
ATOM   962  O O   . ASP   B 1 27 ? 29.428  -9.536  -34.426 1.00 41.06  ? 26  ASP   B O   1 
ATOM   963  C CB  . ASP   B 1 27 ? 27.393  -8.251  -32.158 1.00 36.37  ? 26  ASP   B CB  1 
ATOM   964  C CG  . ASP   B 1 27 ? 26.177  -7.541  -31.579 1.00 36.57  ? 26  ASP   B CG  1 
ATOM   965  O OD1 . ASP   B 1 27 ? 25.350  -7.016  -32.353 1.00 39.19  ? 26  ASP   B OD1 1 
ATOM   966  O OD2 . ASP   B 1 27 ? 26.088  -7.492  -30.326 1.00 35.11  ? 26  ASP   B OD2 1 
ATOM   967  N N   A ASP   B 1 28 ? 29.614  -7.306  -34.023 0.50 50.66  ? 27  ASP   B N   1 
ATOM   968  N N   B ASP   B 1 28 ? 29.631  -7.314  -34.015 0.50 49.20  ? 27  ASP   B N   1 
ATOM   969  C CA  A ASP   B 1 28 ? 31.047  -7.185  -34.255 0.50 53.56  ? 27  ASP   B CA  1 
ATOM   970  C CA  B ASP   B 1 28 ? 31.058  -7.210  -34.303 0.50 50.89  ? 27  ASP   B CA  1 
ATOM   971  C C   A ASP   B 1 28 ? 31.766  -7.564  -32.965 0.50 57.02  ? 27  ASP   B C   1 
ATOM   972  C C   B ASP   B 1 28 ? 31.820  -7.413  -32.994 0.50 54.96  ? 27  ASP   B C   1 
ATOM   973  O O   A ASP   B 1 28 ? 31.178  -7.469  -31.891 0.50 60.97  ? 27  ASP   B O   1 
ATOM   974  O O   B ASP   B 1 28 ? 31.316  -7.047  -31.934 0.50 57.81  ? 27  ASP   B O   1 
ATOM   975  C CB  A ASP   B 1 28 ? 31.413  -5.753  -34.619 0.50 51.60  ? 27  ASP   B CB  1 
ATOM   976  C CB  B ASP   B 1 28 ? 31.388  -5.859  -34.928 0.50 47.45  ? 27  ASP   B CB  1 
ATOM   977  C CG  A ASP   B 1 28 ? 30.290  -4.954  -35.264 0.50 51.98  ? 27  ASP   B CG  1 
ATOM   978  C CG  B ASP   B 1 28 ? 32.265  -5.886  -36.174 0.50 46.36  ? 27  ASP   B CG  1 
ATOM   979  O OD1 A ASP   B 1 28 ? 30.494  -4.442  -36.381 0.50 56.63  ? 27  ASP   B OD1 1 
ATOM   980  O OD1 B ASP   B 1 28 ? 33.325  -6.545  -36.136 0.50 49.73  ? 27  ASP   B OD1 1 
ATOM   981  O OD2 A ASP   B 1 28 ? 29.210  -4.858  -34.645 0.50 55.63  ? 27  ASP   B OD2 1 
ATOM   982  O OD2 B ASP   B 1 28 ? 31.887  -5.236  -37.174 0.50 41.08  ? 27  ASP   B OD2 1 
ATOM   983  N N   . ILE   B 1 29 ? 33.035  -7.981  -33.079 1.00 63.16  ? 28  ILE   B N   1 
ATOM   984  C CA  . ILE   B 1 29 ? 33.818  -8.369  -31.909 1.00 64.31  ? 28  ILE   B CA  1 
ATOM   985  C C   . ILE   B 1 29 ? 34.351  -7.115  -31.191 1.00 71.77  ? 28  ILE   B C   1 
ATOM   986  O O   . ILE   B 1 29 ? 34.469  -6.062  -31.863 1.00 80.58  ? 28  ILE   B O   1 
ATOM   987  C CB  . ILE   B 1 29 ? 34.950  -9.343  -32.286 1.00 60.15  ? 28  ILE   B CB  1 
ATOM   988  N N   . VAL   B 1 34 ? 36.299  -10.015 -24.285 1.00 73.85  ? 33  VAL   B N   1 
ATOM   989  C CA  . VAL   B 1 34 ? 36.341  -11.443 -24.724 1.00 72.63  ? 33  VAL   B CA  1 
ATOM   990  C C   . VAL   B 1 34 ? 36.616  -11.474 -26.226 1.00 76.54  ? 33  VAL   B C   1 
ATOM   991  O O   . VAL   B 1 34 ? 36.765  -10.424 -26.847 1.00 83.02  ? 33  VAL   B O   1 
ATOM   992  C CB  . VAL   B 1 34 ? 34.972  -12.062 -24.384 1.00 70.12  ? 33  VAL   B CB  1 
ATOM   993  C CG1 . VAL   B 1 34 ? 33.876  -11.564 -25.321 1.00 65.95  ? 33  VAL   B CG1 1 
ATOM   994  C CG2 . VAL   B 1 34 ? 35.005  -13.586 -24.355 1.00 64.12  ? 33  VAL   B CG2 1 
ATOM   995  N N   . LYS   B 1 35 ? 36.726  -12.689 -26.779 1.00 75.66  ? 34  LYS   B N   1 
ATOM   996  C CA  . LYS   B 1 35 ? 36.527  -12.973 -28.196 1.00 72.61  ? 34  LYS   B CA  1 
ATOM   997  C C   . LYS   B 1 35 ? 35.666  -14.236 -28.302 1.00 67.33  ? 34  LYS   B C   1 
ATOM   998  O O   . LYS   B 1 35 ? 35.691  -15.070 -27.391 1.00 65.28  ? 34  LYS   B O   1 
ATOM   999  C CB  . LYS   B 1 35 ? 37.861  -13.116 -28.944 1.00 69.53  ? 34  LYS   B CB  1 
ATOM   1000 N N   . PRO   B 1 36 ? 34.855  -14.427 -29.377 1.00 65.62  ? 35  PRO   B N   1 
ATOM   1001 C CA  . PRO   B 1 36 ? 34.085  -15.667 -29.522 1.00 56.69  ? 35  PRO   B CA  1 
ATOM   1002 C C   . PRO   B 1 36 ? 35.034  -16.855 -29.588 1.00 51.91  ? 35  PRO   B C   1 
ATOM   1003 O O   . PRO   B 1 36 ? 36.075  -16.776 -30.236 1.00 53.70  ? 35  PRO   B O   1 
ATOM   1004 C CB  . PRO   B 1 36 ? 33.277  -15.495 -30.824 1.00 55.78  ? 35  PRO   B CB  1 
ATOM   1005 C CG  . PRO   B 1 36 ? 33.961  -14.348 -31.552 1.00 61.14  ? 35  PRO   B CG  1 
ATOM   1006 C CD  . PRO   B 1 36 ? 34.611  -13.477 -30.480 1.00 58.35  ? 35  PRO   B CD  1 
ATOM   1007 N N   . PRO   B 1 37 ? 34.702  -17.992 -28.938 1.00 53.10  ? 36  PRO   B N   1 
ATOM   1008 C CA  . PRO   B 1 37 ? 35.476  -19.217 -29.115 1.00 53.49  ? 36  PRO   B CA  1 
ATOM   1009 C C   . PRO   B 1 37 ? 35.535  -19.517 -30.613 1.00 61.59  ? 36  PRO   B C   1 
ATOM   1010 O O   . PRO   B 1 37 ? 34.793  -18.933 -31.406 1.00 56.46  ? 36  PRO   B O   1 
ATOM   1011 C CB  . PRO   B 1 37 ? 34.682  -20.294 -28.351 1.00 52.96  ? 36  PRO   B CB  1 
ATOM   1012 C CG  . PRO   B 1 37 ? 33.770  -19.528 -27.419 1.00 54.62  ? 36  PRO   B CG  1 
ATOM   1013 C CD  . PRO   B 1 37 ? 33.555  -18.158 -28.031 1.00 51.08  ? 36  PRO   B CD  1 
ATOM   1014 N N   . PRO   B 1 38 ? 36.412  -20.448 -31.052 1.00 61.51  ? 37  PRO   B N   1 
ATOM   1015 C CA  . PRO   B 1 38 ? 36.478  -20.827 -32.470 1.00 62.65  ? 37  PRO   B CA  1 
ATOM   1016 C C   . PRO   B 1 38 ? 35.150  -21.355 -33.016 1.00 56.44  ? 37  PRO   B C   1 
ATOM   1017 O O   . PRO   B 1 38 ? 34.450  -22.108 -32.340 1.00 56.85  ? 37  PRO   B O   1 
ATOM   1018 C CB  . PRO   B 1 38 ? 37.600  -21.888 -32.531 1.00 63.09  ? 37  PRO   B CB  1 
ATOM   1019 C CG  . PRO   B 1 38 ? 38.363  -21.711 -31.226 1.00 59.84  ? 37  PRO   B CG  1 
ATOM   1020 C CD  . PRO   B 1 38 ? 37.377  -21.172 -30.204 1.00 63.49  ? 37  PRO   B CD  1 
ATOM   1021 N N   . ASN   B 1 39 ? 34.812  -20.911 -34.233 1.00 50.81  ? 38  ASN   B N   1 
ATOM   1022 C CA  . ASN   B 1 39 ? 33.646  -21.349 -34.990 1.00 49.95  ? 38  ASN   B CA  1 
ATOM   1023 C C   . ASN   B 1 39 ? 32.364  -20.662 -34.527 1.00 45.13  ? 38  ASN   B C   1 
ATOM   1024 O O   . ASN   B 1 39 ? 31.306  -20.975 -35.053 1.00 40.84  ? 38  ASN   B O   1 
ATOM   1025 C CB  . ASN   B 1 39 ? 33.364  -22.846 -34.899 1.00 48.73  ? 38  ASN   B CB  1 
ATOM   1026 C CG  . ASN   B 1 39 ? 34.569  -23.712 -35.177 1.00 61.30  ? 38  ASN   B CG  1 
ATOM   1027 O OD1 . ASN   B 1 39 ? 34.850  -24.638 -34.408 1.00 69.69  ? 38  ASN   B OD1 1 
ATOM   1028 N ND2 . ASN   B 1 39 ? 35.281  -23.444 -36.262 1.00 51.81  ? 38  ASN   B ND2 1 
ATOM   1029 N N   . LYS   B 1 40 ? 32.441  -19.752 -33.545 1.00 41.72  ? 39  LYS   B N   1 
ATOM   1030 C CA  . LYS   B 1 40 ? 31.233  -19.179 -32.970 1.00 42.08  ? 39  LYS   B CA  1 
ATOM   1031 C C   . LYS   B 1 40 ? 31.180  -17.681 -33.254 1.00 43.73  ? 39  LYS   B C   1 
ATOM   1032 O O   . LYS   B 1 40 ? 32.194  -17.049 -33.543 1.00 41.83  ? 39  LYS   B O   1 
ATOM   1033 C CB  . LYS   B 1 40 ? 31.229  -19.457 -31.465 1.00 42.12  ? 39  LYS   B CB  1 
ATOM   1034 C CG  . LYS   B 1 40 ? 31.039  -20.906 -31.066 1.00 46.39  ? 39  LYS   B CG  1 
ATOM   1035 C CD  . LYS   B 1 40 ? 30.783  -20.925 -29.562 1.00 56.09  ? 39  LYS   B CD  1 
ATOM   1036 C CE  . LYS   B 1 40 ? 29.704  -21.842 -29.083 1.00 65.30  ? 39  LYS   B CE  1 
ATOM   1037 N NZ  . LYS   B 1 40 ? 30.009  -23.250 -29.347 1.00 73.68  ? 39  LYS   B NZ  1 
ATOM   1038 N N   . TYR   B 1 41 ? 29.980  -17.111 -33.139 1.00 36.33  ? 40  TYR   B N   1 
ATOM   1039 C CA  . TYR   B 1 41 ? 29.802  -15.690 -33.387 1.00 36.04  ? 40  TYR   B CA  1 
ATOM   1040 C C   . TYR   B 1 41 ? 29.182  -15.047 -32.158 1.00 37.02  ? 40  TYR   B C   1 
ATOM   1041 O O   . TYR   B 1 41 ? 28.440  -15.709 -31.441 1.00 32.56  ? 40  TYR   B O   1 
ATOM   1042 C CB  . TYR   B 1 41 ? 28.759  -15.546 -34.490 1.00 33.31  ? 40  TYR   B CB  1 
ATOM   1043 C CG  . TYR   B 1 41 ? 29.252  -16.008 -35.851 1.00 40.77  ? 40  TYR   B CG  1 
ATOM   1044 C CD1 . TYR   B 1 41 ? 29.890  -15.113 -36.708 1.00 39.35  ? 40  TYR   B CD1 1 
ATOM   1045 C CD2 . TYR   B 1 41 ? 29.065  -17.319 -36.280 1.00 38.26  ? 40  TYR   B CD2 1 
ATOM   1046 C CE1 . TYR   B 1 41 ? 30.341  -15.510 -37.958 1.00 41.44  ? 40  TYR   B CE1 1 
ATOM   1047 C CE2 . TYR   B 1 41 ? 29.519  -17.730 -37.527 1.00 38.33  ? 40  TYR   B CE2 1 
ATOM   1048 C CZ  . TYR   B 1 41 ? 30.176  -16.826 -38.354 1.00 39.81  ? 40  TYR   B CZ  1 
ATOM   1049 O OH  . TYR   B 1 41 ? 30.592  -17.177 -39.610 1.00 39.35  ? 40  TYR   B OH  1 
ATOM   1050 N N   . PRO   B 1 42 ? 29.434  -13.736 -31.922 1.00 37.98  ? 41  PRO   B N   1 
ATOM   1051 C CA  . PRO   B 1 42 ? 28.719  -12.999 -30.882 1.00 33.99  ? 41  PRO   B CA  1 
ATOM   1052 C C   . PRO   B 1 42 ? 27.308  -12.705 -31.379 1.00 31.51  ? 41  PRO   B C   1 
ATOM   1053 O O   . PRO   B 1 42 ? 27.103  -12.044 -32.400 1.00 34.20  ? 41  PRO   B O   1 
ATOM   1054 C CB  . PRO   B 1 42 ? 29.557  -11.728 -30.683 1.00 35.63  ? 41  PRO   B CB  1 
ATOM   1055 C CG  . PRO   B 1 42 ? 30.266  -11.510 -32.010 1.00 36.97  ? 41  PRO   B CG  1 
ATOM   1056 C CD  . PRO   B 1 42 ? 30.353  -12.884 -32.689 1.00 37.65  ? 41  PRO   B CD  1 
ATOM   1057 N N   . ILE   B 1 43 ? 26.326  -13.206 -30.620 1.00 29.30  ? 42  ILE   B N   1 
ATOM   1058 C CA  . ILE   B 1 43 ? 24.930  -12.979 -30.934 1.00 25.94  ? 42  ILE   B CA  1 
ATOM   1059 C C   . ILE   B 1 43 ? 24.305  -11.963 -29.968 1.00 28.01  ? 42  ILE   B C   1 
ATOM   1060 O O   . ILE   B 1 43 ? 24.545  -12.033 -28.773 1.00 33.56  ? 42  ILE   B O   1 
ATOM   1061 C CB  . ILE   B 1 43 ? 24.167  -14.304 -30.832 1.00 26.86  ? 42  ILE   B CB  1 
ATOM   1062 C CG1 . ILE   B 1 43 ? 24.909  -15.451 -31.577 1.00 29.33  ? 42  ILE   B CG1 1 
ATOM   1063 C CG2 . ILE   B 1 43 ? 22.747  -14.098 -31.348 1.00 27.59  ? 42  ILE   B CG2 1 
ATOM   1064 C CD1 . ILE   B 1 43 ? 25.210  -15.157 -33.035 1.00 29.69  ? 42  ILE   B CD1 1 
ATOM   1065 N N   . PHE   B 1 44 ? 23.499  -11.062 -30.524 1.00 25.61  ? 43  PHE   B N   1 
ATOM   1066 C CA  . PHE   B 1 44 ? 22.665  -10.115 -29.791 1.00 28.12  ? 43  PHE   B CA  1 
ATOM   1067 C C   . PHE   B 1 44 ? 21.200  -10.480 -30.003 1.00 26.99  ? 43  PHE   B C   1 
ATOM   1068 O O   . PHE   B 1 44 ? 20.673  -10.531 -31.136 1.00 26.77  ? 43  PHE   B O   1 
ATOM   1069 C CB  . PHE   B 1 44 ? 22.896  -8.652  -30.223 1.00 25.64  ? 43  PHE   B CB  1 
ATOM   1070 C CG  . PHE   B 1 44 ? 21.962  -7.626  -29.580 1.00 24.61  ? 43  PHE   B CG  1 
ATOM   1071 C CD1 . PHE   B 1 44 ? 20.788  -7.207  -30.219 1.00 24.77  ? 43  PHE   B CD1 1 
ATOM   1072 C CD2 . PHE   B 1 44 ? 22.253  -7.128  -28.318 1.00 30.94  ? 43  PHE   B CD2 1 
ATOM   1073 C CE1 . PHE   B 1 44 ? 19.940  -6.282  -29.606 1.00 31.01  ? 43  PHE   B CE1 1 
ATOM   1074 C CE2 . PHE   B 1 44 ? 21.417  -6.200  -27.700 1.00 27.60  ? 43  PHE   B CE2 1 
ATOM   1075 C CZ  . PHE   B 1 44 ? 20.277  -5.769  -28.366 1.00 31.22  ? 43  PHE   B CZ  1 
ATOM   1076 N N   . PHE   B 1 45 ? 20.532  -10.782 -28.877 1.00 28.24  ? 44  PHE   B N   1 
ATOM   1077 C CA  . PHE   B 1 45 ? 19.140  -11.156 -28.955 1.00 24.64  ? 44  PHE   B CA  1 
ATOM   1078 C C   . PHE   B 1 45 ? 18.251  -9.946  -28.787 1.00 23.64  ? 44  PHE   B C   1 
ATOM   1079 O O   . PHE   B 1 45 ? 18.297  -9.256  -27.745 1.00 26.92  ? 44  PHE   B O   1 
ATOM   1080 C CB  . PHE   B 1 45 ? 18.847  -12.169 -27.838 1.00 23.71  ? 44  PHE   B CB  1 
ATOM   1081 C CG  . PHE   B 1 45 ? 19.517  -13.519 -28.023 1.00 23.76  ? 44  PHE   B CG  1 
ATOM   1082 C CD1 . PHE   B 1 45 ? 20.867  -13.690 -27.749 1.00 25.54  ? 44  PHE   B CD1 1 
ATOM   1083 C CD2 . PHE   B 1 45 ? 18.798  -14.610 -28.490 1.00 24.43  ? 44  PHE   B CD2 1 
ATOM   1084 C CE1 . PHE   B 1 45 ? 21.492  -14.910 -27.990 1.00 28.92  ? 44  PHE   B CE1 1 
ATOM   1085 C CE2 . PHE   B 1 45 ? 19.423  -15.853 -28.648 1.00 29.33  ? 44  PHE   B CE2 1 
ATOM   1086 C CZ  . PHE   B 1 45 ? 20.782  -15.993 -28.458 1.00 27.13  ? 44  PHE   B CZ  1 
ATOM   1087 N N   . PHE   B 1 46 ? 17.377  -9.743  -29.780 1.00 23.11  ? 45  PHE   B N   1 
ATOM   1088 C CA  . PHE   B 1 46 ? 16.427  -8.647  -29.741 1.00 23.81  ? 45  PHE   B CA  1 
ATOM   1089 C C   . PHE   B 1 46 ? 15.432  -8.861  -28.594 1.00 27.36  ? 45  PHE   B C   1 
ATOM   1090 O O   . PHE   B 1 46 ? 15.161  -9.997  -28.201 1.00 25.56  ? 45  PHE   B O   1 
ATOM   1091 C CB  . PHE   B 1 46 ? 15.695  -8.392  -31.058 1.00 24.50  ? 45  PHE   B CB  1 
ATOM   1092 C CG  . PHE   B 1 46 ? 16.636  -7.954  -32.182 1.00 29.13  ? 45  PHE   B CG  1 
ATOM   1093 C CD1 . PHE   B 1 46 ? 17.154  -6.655  -32.203 1.00 29.75  ? 45  PHE   B CD1 1 
ATOM   1094 C CD2 . PHE   B 1 46 ? 17.014  -8.832  -33.207 1.00 25.94  ? 45  PHE   B CD2 1 
ATOM   1095 C CE1 . PHE   B 1 46 ? 17.994  -6.237  -33.239 1.00 29.52  ? 45  PHE   B CE1 1 
ATOM   1096 C CE2 . PHE   B 1 46 ? 17.847  -8.395  -34.261 1.00 26.68  ? 45  PHE   B CE2 1 
ATOM   1097 C CZ  . PHE   B 1 46 ? 18.335  -7.089  -34.264 1.00 26.46  ? 45  PHE   B CZ  1 
ATOM   1098 N N   . GLY   B 1 47 ? 14.870  -7.751  -28.109 1.00 27.77  ? 46  GLY   B N   1 
ATOM   1099 C CA  . GLY   B 1 47 ? 13.828  -7.790  -27.078 1.00 27.05  ? 46  GLY   B CA  1 
ATOM   1100 C C   . GLY   B 1 47 ? 14.462  -7.898  -25.690 1.00 30.78  ? 46  GLY   B C   1 
ATOM   1101 O O   . GLY   B 1 47 ? 14.297  -7.007  -24.850 1.00 30.94  ? 46  GLY   B O   1 
ATOM   1102 N N   . THR   B 1 48 ? 15.151  -9.007  -25.443 1.00 28.95  ? 47  THR   B N   1 
ATOM   1103 C CA  . THR   B 1 48 ? 15.832  -9.233  -24.182 1.00 27.90  ? 47  THR   B CA  1 
ATOM   1104 C C   . THR   B 1 48 ? 17.100  -8.389  -24.085 1.00 29.65  ? 47  THR   B C   1 
ATOM   1105 O O   . THR   B 1 48 ? 17.509  -8.065  -22.970 1.00 31.35  ? 47  THR   B O   1 
ATOM   1106 C CB  . THR   B 1 48 ? 16.176  -10.696 -23.914 1.00 27.35  ? 47  THR   B CB  1 
ATOM   1107 O OG1 . THR   B 1 48 ? 17.144  -11.140 -24.879 1.00 27.54  ? 47  THR   B OG1 1 
ATOM   1108 C CG2 . THR   B 1 48 ? 14.934  -11.571 -23.881 1.00 25.68  ? 47  THR   B CG2 1 
ATOM   1109 N N   . HIS   B 1 49 ? 17.747  -8.151  -25.235 1.00 28.87  ? 48  HIS   B N   1 
ATOM   1110 C CA  . HIS   B 1 49 ? 19.037  -7.474  -25.332 1.00 29.33  ? 48  HIS   B CA  1 
ATOM   1111 C C   . HIS   B 1 49 ? 20.173  -8.239  -24.663 1.00 30.86  ? 48  HIS   B C   1 
ATOM   1112 O O   . HIS   B 1 49 ? 21.181  -7.632  -24.318 1.00 36.33  ? 48  HIS   B O   1 
ATOM   1113 C CB  . HIS   B 1 49 ? 18.933  -5.999  -24.902 1.00 29.47  ? 48  HIS   B CB  1 
ATOM   1114 C CG  . HIS   B 1 49 ? 17.756  -5.299  -25.480 1.00 30.23  ? 48  HIS   B CG  1 
ATOM   1115 N ND1 . HIS   B 1 49 ? 16.955  -4.477  -24.712 1.00 35.00  ? 48  HIS   B ND1 1 
ATOM   1116 C CD2 . HIS   B 1 49 ? 17.168  -5.315  -26.709 1.00 26.68  ? 48  HIS   B CD2 1 
ATOM   1117 C CE1 . HIS   B 1 49 ? 15.946  -4.019  -25.442 1.00 33.28  ? 48  HIS   B CE1 1 
ATOM   1118 N NE2 . HIS   B 1 49 ? 16.072  -4.482  -26.680 1.00 32.56  ? 48  HIS   B NE2 1 
ATOM   1119 N N   . GLU   B 1 50 ? 20.031  -9.553  -24.500 1.00 27.81  ? 49  GLU   B N   1 
ATOM   1120 C CA  . GLU   B 1 50 ? 21.089  -10.413 -23.998 1.00 32.50  ? 49  GLU   B CA  1 
ATOM   1121 C C   . GLU   B 1 50 ? 22.004  -10.833 -25.149 1.00 29.74  ? 49  GLU   B C   1 
ATOM   1122 O O   . GLU   B 1 50 ? 21.657  -10.626 -26.312 1.00 32.65  ? 49  GLU   B O   1 
ATOM   1123 C CB  . GLU   B 1 50 ? 20.447  -11.654 -23.380 1.00 37.23  ? 49  GLU   B CB  1 
ATOM   1124 C CG  . GLU   B 1 50 ? 19.767  -11.331 -22.048 1.00 34.05  ? 49  GLU   B CG  1 
ATOM   1125 C CD  . GLU   B 1 50 ? 19.038  -12.539 -21.493 1.00 41.40  ? 49  GLU   B CD  1 
ATOM   1126 O OE1 . GLU   B 1 50 ? 18.211  -13.118 -22.197 1.00 41.36  ? 49  GLU   B OE1 1 
ATOM   1127 O OE2 . GLU   B 1 50 ? 19.281  -12.894 -20.336 1.00 52.62  ? 49  GLU   B OE2 1 
ATOM   1128 N N   . THR   B 1 51 ? 23.168  -11.382 -24.790 1.00 31.32  ? 50  THR   B N   1 
ATOM   1129 C CA  . THR   B 1 51 ? 24.195  -11.834 -25.729 1.00 31.12  ? 50  THR   B CA  1 
ATOM   1130 C C   . THR   B 1 51 ? 24.632  -13.252 -25.358 1.00 35.20  ? 50  THR   B C   1 
ATOM   1131 O O   . THR   B 1 51 ? 24.549  -13.678 -24.210 1.00 34.30  ? 50  THR   B O   1 
ATOM   1132 C CB  . THR   B 1 51 ? 25.389  -10.865 -25.781 1.00 34.13  ? 50  THR   B CB  1 
ATOM   1133 O OG1 . THR   B 1 51 ? 25.861  -10.910 -24.442 1.00 40.11  ? 50  THR   B OG1 1 
ATOM   1134 C CG2 . THR   B 1 51 ? 25.007  -9.432  -26.113 1.00 36.29  ? 50  THR   B CG2 1 
ATOM   1135 N N   . ALA   B 1 52 ? 25.074  -14.013 -26.364 1.00 34.03  ? 51  ALA   B N   1 
ATOM   1136 C CA  . ALA   B 1 52 ? 25.674  -15.318 -26.158 1.00 32.76  ? 51  ALA   B CA  1 
ATOM   1137 C C   . ALA   B 1 52 ? 26.565  -15.590 -27.363 1.00 34.25  ? 51  ALA   B C   1 
ATOM   1138 O O   . ALA   B 1 52 ? 26.531  -14.840 -28.338 1.00 36.36  ? 51  ALA   B O   1 
ATOM   1139 C CB  . ALA   B 1 52 ? 24.605  -16.365 -26.017 1.00 31.63  ? 51  ALA   B CB  1 
ATOM   1140 N N   . PHE   B 1 53 ? 27.386  -16.631 -27.267 1.00 34.05  ? 52  PHE   B N   1 
ATOM   1141 C CA  . PHE   B 1 53 ? 28.172  -17.065 -28.410 1.00 37.30  ? 52  PHE   B CA  1 
ATOM   1142 C C   . PHE   B 1 53 ? 27.533  -18.335 -28.966 1.00 36.38  ? 52  PHE   B C   1 
ATOM   1143 O O   . PHE   B 1 53 ? 27.350  -19.302 -28.243 1.00 34.90  ? 52  PHE   B O   1 
ATOM   1144 C CB  . PHE   B 1 53 ? 29.630  -17.359 -28.034 1.00 38.76  ? 52  PHE   B CB  1 
ATOM   1145 C CG  . PHE   B 1 53 ? 30.392  -16.150 -27.528 1.00 38.95  ? 52  PHE   B CG  1 
ATOM   1146 C CD1 . PHE   B 1 53 ? 30.629  -15.072 -28.369 1.00 42.50  ? 52  PHE   B CD1 1 
ATOM   1147 C CD2 . PHE   B 1 53 ? 30.875  -16.100 -26.223 1.00 44.39  ? 52  PHE   B CD2 1 
ATOM   1148 C CE1 . PHE   B 1 53 ? 31.328  -13.961 -27.918 1.00 43.17  ? 52  PHE   B CE1 1 
ATOM   1149 C CE2 . PHE   B 1 53 ? 31.570  -14.979 -25.771 1.00 45.68  ? 52  PHE   B CE2 1 
ATOM   1150 C CZ  . PHE   B 1 53 ? 31.786  -13.918 -26.618 1.00 43.10  ? 52  PHE   B CZ  1 
ATOM   1151 N N   . LEU   B 1 54 ? 27.245  -18.342 -30.268 1.00 34.19  ? 53  LEU   B N   1 
ATOM   1152 C CA  . LEU   B 1 54 ? 26.603  -19.507 -30.854 1.00 33.62  ? 53  LEU   B CA  1 
ATOM   1153 C C   . LEU   B 1 54 ? 27.292  -19.852 -32.171 1.00 31.47  ? 53  LEU   B C   1 
ATOM   1154 O O   . LEU   B 1 54 ? 27.841  -18.975 -32.842 1.00 31.28  ? 53  LEU   B O   1 
ATOM   1155 C CB  . LEU   B 1 54 ? 25.130  -19.250 -31.153 1.00 30.19  ? 53  LEU   B CB  1 
ATOM   1156 C CG  . LEU   B 1 54 ? 24.163  -19.152 -29.969 1.00 32.30  ? 53  LEU   B CG  1 
ATOM   1157 C CD1 . LEU   B 1 54 ? 22.851  -18.784 -30.607 1.00 33.68  ? 53  LEU   B CD1 1 
ATOM   1158 C CD2 . LEU   B 1 54 ? 24.088  -20.498 -29.232 1.00 30.04  ? 53  LEU   B CD2 1 
ATOM   1159 N N   . GLY   B 1 55 ? 27.148  -21.122 -32.552 1.00 32.47  ? 54  GLY   B N   1 
ATOM   1160 C CA  . GLY   B 1 55 ? 27.730  -21.599 -33.796 1.00 32.54  ? 54  GLY   B CA  1 
ATOM   1161 C C   . GLY   B 1 55 ? 26.657  -21.712 -34.874 1.00 30.24  ? 54  GLY   B C   1 
ATOM   1162 O O   . GLY   B 1 55 ? 25.453  -21.660 -34.588 1.00 30.99  ? 54  GLY   B O   1 
ATOM   1163 N N   . PRO   B 1 56 ? 27.056  -21.895 -36.153 1.00 29.34  ? 55  PRO   B N   1 
ATOM   1164 C CA  . PRO   B 1 56 ? 26.106  -21.908 -37.257 1.00 29.20  ? 55  PRO   B CA  1 
ATOM   1165 C C   . PRO   B 1 56 ? 24.927  -22.869 -37.165 1.00 26.02  ? 55  PRO   B C   1 
ATOM   1166 O O   . PRO   B 1 56 ? 23.884  -22.568 -37.699 1.00 28.53  ? 55  PRO   B O   1 
ATOM   1167 C CB  . PRO   B 1 56 ? 26.970  -22.160 -38.488 1.00 31.97  ? 55  PRO   B CB  1 
ATOM   1168 C CG  . PRO   B 1 56 ? 28.379  -21.818 -38.059 1.00 32.03  ? 55  PRO   B CG  1 
ATOM   1169 C CD  . PRO   B 1 56 ? 28.450  -22.071 -36.585 1.00 32.35  ? 55  PRO   B CD  1 
ATOM   1170 N N   . LYS   B 1 57 ? 25.066  -24.017 -36.465 1.00 27.86  ? 56  LYS   B N   1 
ATOM   1171 C CA  . LYS   B 1 57 ? 23.997  -25.008 -36.440 1.00 27.99  ? 56  LYS   B CA  1 
ATOM   1172 C C   . LYS   B 1 57 ? 22.771  -24.398 -35.759 1.00 28.25  ? 56  LYS   B C   1 
ATOM   1173 O O   . LYS   B 1 57 ? 21.641  -24.857 -35.970 1.00 26.38  ? 56  LYS   B O   1 
ATOM   1174 C CB  . LYS   B 1 57 ? 24.417  -26.305 -35.723 1.00 30.83  ? 56  LYS   B CB  1 
ATOM   1175 C CG  . LYS   B 1 57 ? 24.642  -26.191 -34.223 1.00 31.72  ? 56  LYS   B CG  1 
ATOM   1176 C CD  . LYS   B 1 57 ? 24.718  -27.548 -33.520 1.00 37.87  ? 56  LYS   B CD  1 
ATOM   1177 C CE  . LYS   B 1 57 ? 24.908  -27.463 -32.024 1.00 44.57  ? 56  LYS   B CE  1 
ATOM   1178 N NZ  . LYS   B 1 57 ? 23.718  -26.913 -31.356 1.00 47.93  ? 56  LYS   B NZ  1 
ATOM   1179 N N   . ASP   B 1 58 ? 23.017  -23.338 -34.971 1.00 28.67  ? 57  ASP   B N   1 
ATOM   1180 C CA  . ASP   B 1 58 ? 21.964  -22.715 -34.179 1.00 30.76  ? 57  ASP   B CA  1 
ATOM   1181 C C   . ASP   B 1 58 ? 21.587  -21.344 -34.746 1.00 28.59  ? 57  ASP   B C   1 
ATOM   1182 O O   . ASP   B 1 58 ? 20.828  -20.601 -34.099 1.00 26.75  ? 57  ASP   B O   1 
ATOM   1183 C CB  . ASP   B 1 58 ? 22.366  -22.595 -32.711 1.00 29.56  ? 57  ASP   B CB  1 
ATOM   1184 C CG  . ASP   B 1 58 ? 22.441  -23.930 -31.985 1.00 38.34  ? 57  ASP   B CG  1 
ATOM   1185 O OD1 . ASP   B 1 58 ? 21.527  -24.725 -32.182 1.00 34.28  ? 57  ASP   B OD1 1 
ATOM   1186 O OD2 . ASP   B 1 58 ? 23.417  -24.157 -31.256 1.00 37.23  ? 57  ASP   B OD2 1 
ATOM   1187 N N   . LEU   B 1 59 ? 22.072  -21.038 -35.968 1.00 26.57  ? 58  LEU   B N   1 
ATOM   1188 C CA  . LEU   B 1 59 ? 21.816  -19.726 -36.570 1.00 24.73  ? 58  LEU   B CA  1 
ATOM   1189 C C   . LEU   B 1 59 ? 21.070  -19.897 -37.893 1.00 28.43  ? 58  LEU   B C   1 
ATOM   1190 O O   . LEU   B 1 59 ? 21.515  -20.607 -38.806 1.00 28.59  ? 58  LEU   B O   1 
ATOM   1191 C CB  . LEU   B 1 59 ? 23.140  -18.979 -36.770 1.00 27.49  ? 58  LEU   B CB  1 
ATOM   1192 C CG  . LEU   B 1 59 ? 23.923  -18.683 -35.493 1.00 27.58  ? 58  LEU   B CG  1 
ATOM   1193 C CD1 . LEU   B 1 59 ? 25.241  -17.992 -35.844 1.00 28.51  ? 58  LEU   B CD1 1 
ATOM   1194 C CD2 . LEU   B 1 59 ? 23.112  -17.838 -34.490 1.00 28.53  ? 58  LEU   B CD2 1 
ATOM   1195 N N   . PHE   B 1 60 ? 19.904  -19.279 -37.969 1.00 24.16  ? 59  PHE   B N   1 
ATOM   1196 C CA  . PHE   B 1 60 ? 18.981  -19.454 -39.068 1.00 24.57  ? 59  PHE   B CA  1 
ATOM   1197 C C   . PHE   B 1 60 ? 18.802  -18.095 -39.728 1.00 25.29  ? 59  PHE   B C   1 
ATOM   1198 O O   . PHE   B 1 60 ? 18.185  -17.186 -39.165 1.00 25.22  ? 59  PHE   B O   1 
ATOM   1199 C CB  . PHE   B 1 60 ? 17.630  -19.934 -38.539 1.00 22.38  ? 59  PHE   B CB  1 
ATOM   1200 C CG  . PHE   B 1 60 ? 17.718  -21.350 -37.967 1.00 23.88  ? 59  PHE   B CG  1 
ATOM   1201 C CD1 . PHE   B 1 60 ? 18.170  -21.559 -36.664 1.00 27.87  ? 59  PHE   B CD1 1 
ATOM   1202 C CD2 . PHE   B 1 60 ? 17.292  -22.444 -38.725 1.00 27.22  ? 59  PHE   B CD2 1 
ATOM   1203 C CE1 . PHE   B 1 60 ? 18.273  -22.848 -36.127 1.00 27.95  ? 59  PHE   B CE1 1 
ATOM   1204 C CE2 . PHE   B 1 60 ? 17.371  -23.735 -38.185 1.00 28.89  ? 59  PHE   B CE2 1 
ATOM   1205 C CZ  . PHE   B 1 60 ? 17.872  -23.930 -36.897 1.00 29.71  ? 59  PHE   B CZ  1 
ATOM   1206 N N   . PRO   B 1 61 ? 19.358  -17.909 -40.954 1.00 28.49  ? 60  PRO   B N   1 
ATOM   1207 C CA  . PRO   B 1 61 ? 19.164  -16.638 -41.672 1.00 28.67  ? 60  PRO   B CA  1 
ATOM   1208 C C   . PRO   B 1 61 ? 17.713  -16.142 -41.646 1.00 25.54  ? 60  PRO   B C   1 
ATOM   1209 O O   . PRO   B 1 61 ? 16.750  -16.862 -41.936 1.00 28.91  ? 60  PRO   B O   1 
ATOM   1210 C CB  . PRO   B 1 61 ? 19.730  -16.958 -43.083 1.00 27.57  ? 60  PRO   B CB  1 
ATOM   1211 C CG  . PRO   B 1 61 ? 20.807  -17.997 -42.818 1.00 33.70  ? 60  PRO   B CG  1 
ATOM   1212 C CD  . PRO   B 1 61 ? 20.244  -18.857 -41.655 1.00 29.88  ? 60  PRO   B CD  1 
ATOM   1213 N N   . TYR   B 1 62 ? 17.515  -14.848 -41.292 1.00 27.83  ? 61  TYR   B N   1 
ATOM   1214 C CA  . TYR   B 1 62 ? 16.192  -14.347 -40.956 1.00 27.47  ? 61  TYR   B CA  1 
ATOM   1215 C C   . TYR   B 1 62 ? 15.192  -14.340 -42.107 1.00 28.92  ? 61  TYR   B C   1 
ATOM   1216 O O   . TYR   B 1 62 ? 14.030  -14.706 -41.933 1.00 32.04  ? 61  TYR   B O   1 
ATOM   1217 C CB  . TYR   B 1 62 ? 16.378  -12.901 -40.468 1.00 32.46  ? 61  TYR   B CB  1 
ATOM   1218 C CG  . TYR   B 1 62 ? 15.061  -12.178 -40.235 1.00 33.77  ? 61  TYR   B CG  1 
ATOM   1219 C CD1 . TYR   B 1 62 ? 14.319  -12.424 -39.087 1.00 32.83  ? 61  TYR   B CD1 1 
ATOM   1220 C CD2 . TYR   B 1 62 ? 14.604  -11.216 -41.125 1.00 39.01  ? 61  TYR   B CD2 1 
ATOM   1221 C CE1 . TYR   B 1 62 ? 13.125  -11.763 -38.848 1.00 33.69  ? 61  TYR   B CE1 1 
ATOM   1222 C CE2 . TYR   B 1 62 ? 13.424  -10.530 -40.891 1.00 39.20  ? 61  TYR   B CE2 1 
ATOM   1223 C CZ  . TYR   B 1 62 ? 12.691  -10.809 -39.752 1.00 37.72  ? 61  TYR   B CZ  1 
ATOM   1224 O OH  . TYR   B 1 62 ? 11.532  -10.145 -39.530 1.00 39.52  ? 61  TYR   B OH  1 
ATOM   1225 N N   . ASP   B 1 63 ? 15.654  -13.884 -43.284 1.00 37.46  ? 62  ASP   B N   1 
ATOM   1226 C CA  . ASP   B 1 63 ? 14.870  -13.885 -44.510 1.00 43.32  ? 62  ASP   B CA  1 
ATOM   1227 C C   . ASP   B 1 63 ? 14.292  -15.263 -44.830 1.00 36.64  ? 62  ASP   B C   1 
ATOM   1228 O O   . ASP   B 1 63 ? 13.091  -15.379 -45.051 1.00 39.97  ? 62  ASP   B O   1 
ATOM   1229 C CB  . ASP   B 1 63 ? 15.657  -13.283 -45.657 1.00 50.22  ? 62  ASP   B CB  1 
ATOM   1230 C CG  . ASP   B 1 63 ? 15.231  -11.870 -46.000 1.00 64.63  ? 62  ASP   B CG  1 
ATOM   1231 O OD1 . ASP   B 1 63 ? 15.348  -10.995 -45.118 1.00 70.64  ? 62  ASP   B OD1 1 
ATOM   1232 O OD2 . ASP   B 1 63 ? 14.745  -11.678 -47.134 1.00 76.43  ? 62  ASP   B OD2 1 
ATOM   1233 N N   . LYS   B 1 64 ? 15.154  -16.288 -44.827 1.00 39.18  ? 63  LYS   B N   1 
ATOM   1234 C CA  . LYS   B 1 64 ? 14.728  -17.641 -45.144 1.00 37.30  ? 63  LYS   B CA  1 
ATOM   1235 C C   . LYS   B 1 64 ? 13.671  -18.138 -44.148 1.00 38.58  ? 63  LYS   B C   1 
ATOM   1236 O O   . LYS   B 1 64 ? 12.761  -18.871 -44.523 1.00 40.27  ? 63  LYS   B O   1 
ATOM   1237 C CB  . LYS   B 1 64 ? 15.943  -18.568 -45.123 1.00 42.01  ? 63  LYS   B CB  1 
ATOM   1238 C CG  . LYS   B 1 64 ? 15.656  -19.936 -45.737 1.00 37.49  ? 63  LYS   B CG  1 
ATOM   1239 C CD  . LYS   B 1 64 ? 16.694  -20.975 -45.335 1.00 48.22  ? 63  LYS   B CD  1 
ATOM   1240 C CE  . LYS   B 1 64 ? 16.640  -22.336 -46.005 1.00 40.57  ? 63  LYS   B CE  1 
ATOM   1241 N NZ  . LYS   B 1 64 ? 15.322  -22.678 -46.536 1.00 42.80  ? 63  LYS   B NZ  1 
ATOM   1242 N N   . SER   B 1 65 ? 13.801  -17.758 -42.871 1.00 36.44  ? 64  SER   B N   1 
ATOM   1243 C CA  . SER   B 1 65 ? 13.152  -18.523 -41.809 1.00 34.42  ? 64  SER   B CA  1 
ATOM   1244 C C   . SER   B 1 65 ? 12.043  -17.745 -41.082 1.00 33.36  ? 64  SER   B C   1 
ATOM   1245 O O   . SER   B 1 65 ? 11.378  -18.306 -40.207 1.00 32.55  ? 64  SER   B O   1 
ATOM   1246 C CB  . SER   B 1 65 ? 14.198  -19.027 -40.861 1.00 38.92  ? 64  SER   B CB  1 
ATOM   1247 O OG  . SER   B 1 65 ? 14.886  -17.922 -40.302 1.00 47.22  ? 64  SER   B OG  1 
ATOM   1248 N N   . LYS   B 1 66 ? 11.796  -16.488 -41.477 1.00 33.72  ? 65  LYS   B N   1 
ATOM   1249 C CA  . LYS   B 1 66 ? 10.888  -15.615 -40.739 1.00 39.23  ? 65  LYS   B CA  1 
ATOM   1250 C C   . LYS   B 1 66 ? 9.456   -16.141 -40.728 1.00 40.91  ? 65  LYS   B C   1 
ATOM   1251 O O   . LYS   B 1 66 ? 8.723   -15.885 -39.776 1.00 40.20  ? 65  LYS   B O   1 
ATOM   1252 C CB  . LYS   B 1 66 ? 10.814  -14.133 -41.138 1.00 37.94  ? 65  LYS   B CB  1 
ATOM   1253 C CG  . LYS   B 1 66 ? 10.704  -13.856 -42.629 1.00 37.06  ? 65  LYS   B CG  1 
ATOM   1254 N N   . ASP   B 1 67 ? 8.995   -16.815 -41.785 1.00 40.72  ? 66  ASP   B N   1 
ATOM   1255 C CA  . ASP   B 1 67 ? 7.592   -17.198 -41.676 1.00 43.82  ? 66  ASP   B CA  1 
ATOM   1256 C C   . ASP   B 1 67 ? 7.426   -18.424 -40.780 1.00 42.11  ? 66  ASP   B C   1 
ATOM   1257 O O   . ASP   B 1 67 ? 6.356   -18.613 -40.200 1.00 45.78  ? 66  ASP   B O   1 
ATOM   1258 C CB  . ASP   B 1 67 ? 6.799   -17.121 -42.975 1.00 60.30  ? 66  ASP   B CB  1 
ATOM   1259 C CG  . ASP   B 1 67 ? 7.498   -17.629 -44.226 1.00 73.45  ? 66  ASP   B CG  1 
ATOM   1260 O OD1 . ASP   B 1 67 ? 6.926   -17.454 -45.329 1.00 73.81  ? 66  ASP   B OD1 1 
ATOM   1261 O OD2 . ASP   B 1 67 ? 8.606   -18.191 -44.086 1.00 78.42  ? 66  ASP   B OD2 1 
ATOM   1262 N N   . LYS   B 1 68 ? 8.500   -19.204 -40.621 1.00 38.44  ? 67  LYS   B N   1 
ATOM   1263 C CA  . LYS   B 1 68 ? 8.471   -20.363 -39.736 1.00 34.69  ? 67  LYS   B CA  1 
ATOM   1264 C C   . LYS   B 1 68 ? 8.640   -19.929 -38.276 1.00 35.64  ? 67  LYS   B C   1 
ATOM   1265 O O   . LYS   B 1 68 ? 7.900   -20.395 -37.392 1.00 36.74  ? 67  LYS   B O   1 
ATOM   1266 C CB  . LYS   B 1 68 ? 9.544   -21.364 -40.170 1.00 39.39  ? 67  LYS   B CB  1 
ATOM   1267 C CG  . LYS   B 1 68 ? 9.556   -22.701 -39.441 1.00 52.02  ? 67  LYS   B CG  1 
ATOM   1268 C CD  . LYS   B 1 68 ? 10.536  -23.635 -40.148 1.00 62.85  ? 67  LYS   B CD  1 
ATOM   1269 C CE  . LYS   B 1 68 ? 10.958  -24.844 -39.363 1.00 62.89  ? 67  LYS   B CE  1 
ATOM   1270 N NZ  . LYS   B 1 68 ? 9.876   -25.806 -39.148 1.00 67.73  ? 67  LYS   B NZ  1 
ATOM   1271 N N   . TYR   B 1 69 ? 9.603   -19.033 -38.012 1.00 31.19  ? 68  TYR   B N   1 
ATOM   1272 C CA  . TYR   B 1 69 ? 9.967   -18.767 -36.623 1.00 26.99  ? 68  TYR   B CA  1 
ATOM   1273 C C   . TYR   B 1 69 ? 9.413   -17.439 -36.109 1.00 34.28  ? 68  TYR   B C   1 
ATOM   1274 O O   . TYR   B 1 69 ? 9.466   -17.167 -34.902 1.00 34.25  ? 68  TYR   B O   1 
ATOM   1275 C CB  . TYR   B 1 69 ? 11.478  -18.787 -36.486 1.00 25.56  ? 68  TYR   B CB  1 
ATOM   1276 C CG  . TYR   B 1 69 ? 12.078  -20.163 -36.778 1.00 28.33  ? 68  TYR   B CG  1 
ATOM   1277 C CD1 . TYR   B 1 69 ? 11.538  -21.321 -36.233 1.00 30.03  ? 68  TYR   B CD1 1 
ATOM   1278 C CD2 . TYR   B 1 69 ? 13.174  -20.297 -37.623 1.00 30.75  ? 68  TYR   B CD2 1 
ATOM   1279 C CE1 . TYR   B 1 69 ? 12.085  -22.576 -36.496 1.00 31.92  ? 68  TYR   B CE1 1 
ATOM   1280 C CE2 . TYR   B 1 69 ? 13.728  -21.538 -37.892 1.00 35.43  ? 68  TYR   B CE2 1 
ATOM   1281 C CZ  . TYR   B 1 69 ? 13.167  -22.685 -37.348 1.00 36.67  ? 68  TYR   B CZ  1 
ATOM   1282 O OH  . TYR   B 1 69 ? 13.753  -23.891 -37.628 1.00 35.47  ? 68  TYR   B OH  1 
ATOM   1283 N N   . GLY   B 1 70 ? 8.945   -16.592 -37.024 1.00 32.73  ? 69  GLY   B N   1 
ATOM   1284 C CA  . GLY   B 1 70 ? 8.645   -15.210 -36.669 1.00 34.68  ? 69  GLY   B CA  1 
ATOM   1285 C C   . GLY   B 1 70 ? 7.240   -14.987 -36.113 1.00 38.48  ? 69  GLY   B C   1 
ATOM   1286 O O   . GLY   B 1 70 ? 6.672   -13.926 -36.356 1.00 40.87  ? 69  GLY   B O   1 
ATOM   1287 N N   . LYS   B 1 71 ? 6.693   -15.950 -35.358 1.00 39.73  ? 70  LYS   B N   1 
ATOM   1288 C CA  . LYS   B 1 71 ? 5.346   -15.796 -34.838 1.00 43.21  ? 70  LYS   B CA  1 
ATOM   1289 C C   . LYS   B 1 71 ? 5.405   -15.384 -33.374 1.00 40.71  ? 70  LYS   B C   1 
ATOM   1290 O O   . LYS   B 1 71 ? 6.186   -15.945 -32.617 1.00 38.26  ? 70  LYS   B O   1 
ATOM   1291 C CB  . LYS   B 1 71 ? 4.529   -17.088 -34.935 1.00 42.05  ? 70  LYS   B CB  1 
ATOM   1292 C CG  . LYS   B 1 71 ? 4.246   -17.375 -36.412 1.00 51.32  ? 70  LYS   B CG  1 
ATOM   1293 C CD  . LYS   B 1 71 ? 3.615   -18.717 -36.752 1.00 51.74  ? 70  LYS   B CD  1 
ATOM   1294 C CE  . LYS   B 1 71 ? 3.133   -18.727 -38.176 1.00 61.22  ? 70  LYS   B CE  1 
ATOM   1295 N NZ  . LYS   B 1 71 ? 4.119   -18.197 -39.125 1.00 67.48  ? 70  LYS   B NZ  1 
ATOM   1296 N N   . PRO   B 1 72 ? 4.524   -14.462 -32.927 1.00 42.29  ? 71  PRO   B N   1 
ATOM   1297 C CA  . PRO   B 1 72 ? 4.486   -14.052 -31.521 1.00 41.52  ? 71  PRO   B CA  1 
ATOM   1298 C C   . PRO   B 1 72 ? 4.245   -15.226 -30.575 1.00 42.02  ? 71  PRO   B C   1 
ATOM   1299 O O   . PRO   B 1 72 ? 3.620   -16.225 -30.945 1.00 37.35  ? 71  PRO   B O   1 
ATOM   1300 C CB  . PRO   B 1 72 ? 3.387   -12.960 -31.427 1.00 42.32  ? 71  PRO   B CB  1 
ATOM   1301 C CG  . PRO   B 1 72 ? 2.648   -13.034 -32.747 1.00 47.95  ? 71  PRO   B CG  1 
ATOM   1302 C CD  . PRO   B 1 72 ? 3.503   -13.800 -33.755 1.00 44.92  ? 71  PRO   B CD  1 
ATOM   1303 N N   . ASN   B 1 73 ? 4.794   -15.112 -29.358 1.00 35.95  ? 72  ASN   B N   1 
ATOM   1304 C CA  . ASN   B 1 73 ? 4.580   -16.119 -28.332 1.00 36.52  ? 72  ASN   B CA  1 
ATOM   1305 C C   . ASN   B 1 73 ? 4.526   -15.409 -26.971 1.00 38.78  ? 72  ASN   B C   1 
ATOM   1306 O O   . ASN   B 1 73 ? 4.597   -14.173 -26.878 1.00 39.67  ? 72  ASN   B O   1 
ATOM   1307 C CB  . ASN   B 1 73 ? 5.556   -17.297 -28.453 1.00 36.85  ? 72  ASN   B CB  1 
ATOM   1308 C CG  . ASN   B 1 73 ? 6.993   -16.895 -28.210 1.00 38.47  ? 72  ASN   B CG  1 
ATOM   1309 O OD1 . ASN   B 1 73 ? 7.264   -16.195 -27.228 1.00 34.75  ? 72  ASN   B OD1 1 
ATOM   1310 N ND2 . ASN   B 1 73 ? 7.936   -17.308 -29.062 1.00 31.12  ? 72  ASN   B ND2 1 
ATOM   1311 N N   . LYS   B 1 74 ? 4.422   -16.198 -25.905 1.00 39.80  ? 73  LYS   B N   1 
ATOM   1312 C CA  . LYS   B 1 74 ? 4.261   -15.598 -24.579 1.00 42.28  ? 73  LYS   B CA  1 
ATOM   1313 C C   . LYS   B 1 74 ? 5.572   -15.561 -23.778 1.00 44.24  ? 73  LYS   B C   1 
ATOM   1314 O O   . LYS   B 1 74 ? 5.544   -15.379 -22.551 1.00 37.69  ? 73  LYS   B O   1 
ATOM   1315 C CB  . LYS   B 1 74 ? 3.145   -16.339 -23.829 1.00 46.97  ? 73  LYS   B CB  1 
ATOM   1316 C CG  . LYS   B 1 74 ? 3.486   -17.783 -23.479 1.00 57.90  ? 73  LYS   B CG  1 
ATOM   1317 C CD  . LYS   B 1 74 ? 2.358   -18.607 -22.866 1.00 65.06  ? 73  LYS   B CD  1 
ATOM   1318 C CE  . LYS   B 1 74 ? 1.074   -18.531 -23.637 1.00 69.47  ? 73  LYS   B CE  1 
ATOM   1319 N NZ  . LYS   B 1 74 ? 0.103   -19.509 -23.138 1.00 70.54  ? 73  LYS   B NZ  1 
ATOM   1320 N N   . ARG   B 1 75 ? 6.722   -15.756 -24.445 1.00 31.10  ? 74  ARG   B N   1 
ATOM   1321 C CA  . ARG   B 1 75 ? 8.014   -15.599 -23.790 1.00 29.54  ? 74  ARG   B CA  1 
ATOM   1322 C C   . ARG   B 1 75 ? 8.326   -14.101 -23.631 1.00 29.85  ? 74  ARG   B C   1 
ATOM   1323 O O   . ARG   B 1 75 ? 8.102   -13.308 -24.553 1.00 33.06  ? 74  ARG   B O   1 
ATOM   1324 C CB  . ARG   B 1 75 ? 9.161   -16.347 -24.485 1.00 31.97  ? 74  ARG   B CB  1 
ATOM   1325 C CG  . ARG   B 1 75 ? 8.981   -17.846 -24.720 1.00 28.92  ? 74  ARG   B CG  1 
ATOM   1326 C CD  . ARG   B 1 75 ? 8.944   -18.605 -23.404 1.00 34.11  ? 74  ARG   B CD  1 
ATOM   1327 N NE  . ARG   B 1 75 ? 9.124   -20.043 -23.621 1.00 33.76  ? 74  ARG   B NE  1 
ATOM   1328 C CZ  . ARG   B 1 75 ? 10.295  -20.645 -23.477 1.00 29.00  ? 74  ARG   B CZ  1 
ATOM   1329 N NH1 . ARG   B 1 75 ? 11.356  -19.996 -23.006 1.00 33.23  ? 74  ARG   B NH1 1 
ATOM   1330 N NH2 . ARG   B 1 75 ? 10.402  -21.930 -23.783 1.00 32.77  ? 74  ARG   B NH2 1 
ATOM   1331 N N   . LYS   B 1 76 ? 8.790   -13.718 -22.420 1.00 29.52  ? 75  LYS   B N   1 
ATOM   1332 C CA  . LYS   B 1 76 ? 9.169   -12.351 -22.114 1.00 25.99  ? 75  LYS   B CA  1 
ATOM   1333 C C   . LYS   B 1 76 ? 10.273  -11.875 -23.073 1.00 23.34  ? 75  LYS   B C   1 
ATOM   1334 O O   . LYS   B 1 76 ? 11.347  -12.478 -23.125 1.00 27.50  ? 75  LYS   B O   1 
ATOM   1335 C CB  . LYS   B 1 76 ? 9.719   -12.324 -20.677 1.00 29.67  ? 75  LYS   B CB  1 
ATOM   1336 C CG  . LYS   B 1 76 ? 10.053  -10.907 -20.184 1.00 29.20  ? 75  LYS   B CG  1 
ATOM   1337 C CD  . LYS   B 1 76 ? 10.635  -10.768 -18.788 1.00 31.60  ? 75  LYS   B CD  1 
ATOM   1338 C CE  . LYS   B 1 76 ? 10.810  -9.307  -18.412 1.00 36.40  ? 75  LYS   B CE  1 
ATOM   1339 N NZ  . LYS   B 1 76 ? 11.123  -9.208  -16.971 1.00 42.24  ? 75  LYS   B NZ  1 
ATOM   1340 N N   . GLY   B 1 77 ? 9.987   -10.784 -23.773 1.00 26.81  ? 76  GLY   B N   1 
ATOM   1341 C CA  . GLY   B 1 77 ? 10.966  -10.160 -24.662 1.00 28.30  ? 76  GLY   B CA  1 
ATOM   1342 C C   . GLY   B 1 77 ? 10.752  -10.556 -26.123 1.00 27.29  ? 76  GLY   B C   1 
ATOM   1343 O O   . GLY   B 1 77 ? 11.285  -9.912  -27.032 1.00 25.41  ? 76  GLY   B O   1 
ATOM   1344 N N   . PHE   B 1 78 ? 9.980   -11.632 -26.386 1.00 25.51  ? 77  PHE   B N   1 
ATOM   1345 C CA  . PHE   B 1 78 ? 9.917   -12.123 -27.777 1.00 25.23  ? 77  PHE   B CA  1 
ATOM   1346 C C   . PHE   B 1 78 ? 9.222   -11.152 -28.724 1.00 30.64  ? 77  PHE   B C   1 
ATOM   1347 O O   . PHE   B 1 78 ? 9.740   -10.859 -29.814 1.00 27.11  ? 77  PHE   B O   1 
ATOM   1348 C CB  . PHE   B 1 78 ? 9.213   -13.481 -27.813 1.00 27.81  ? 77  PHE   B CB  1 
ATOM   1349 C CG  . PHE   B 1 78 ? 9.471   -14.216 -29.119 1.00 25.38  ? 77  PHE   B CG  1 
ATOM   1350 C CD1 . PHE   B 1 78 ? 10.591  -15.048 -29.213 1.00 25.46  ? 77  PHE   B CD1 1 
ATOM   1351 C CD2 . PHE   B 1 78 ? 8.574   -14.116 -30.178 1.00 31.91  ? 77  PHE   B CD2 1 
ATOM   1352 C CE1 . PHE   B 1 78 ? 10.853  -15.721 -30.405 1.00 27.57  ? 77  PHE   B CE1 1 
ATOM   1353 C CE2 . PHE   B 1 78 ? 8.822   -14.818 -31.356 1.00 31.36  ? 77  PHE   B CE2 1 
ATOM   1354 C CZ  . PHE   B 1 78 ? 9.949   -15.633 -31.438 1.00 26.94  ? 77  PHE   B CZ  1 
ATOM   1355 N N   . ASN   B 1 79 ? 8.019   -10.689 -28.361 1.00 28.36  ? 78  ASN   B N   1 
ATOM   1356 C CA  . ASN   B 1 79 ? 7.268   -9.831  -29.261 1.00 29.27  ? 78  ASN   B CA  1 
ATOM   1357 C C   . ASN   B 1 79 ? 7.980   -8.498  -29.469 1.00 29.25  ? 78  ASN   B C   1 
ATOM   1358 O O   . ASN   B 1 79 ? 7.949   -7.972  -30.580 1.00 30.89  ? 78  ASN   B O   1 
ATOM   1359 C CB  . ASN   B 1 79 ? 5.794   -9.717  -28.900 1.00 32.66  ? 78  ASN   B CB  1 
ATOM   1360 C CG  . ASN   B 1 79 ? 5.115   -11.066 -28.897 1.00 39.09  ? 78  ASN   B CG  1 
ATOM   1361 O OD1 . ASN   B 1 79 ? 5.647   -12.046 -29.445 1.00 39.94  ? 78  ASN   B OD1 1 
ATOM   1362 N ND2 . ASN   B 1 79 ? 3.981   -11.153 -28.222 1.00 40.20  ? 78  ASN   B ND2 1 
ATOM   1363 N N   . GLU   B 1 80 ? 8.652   -8.010  -28.426 1.00 27.49  ? 79  GLU   B N   1 
ATOM   1364 C CA  . GLU   B 1 80 ? 9.468   -6.805  -28.540 1.00 32.22  ? 79  GLU   B CA  1 
ATOM   1365 C C   . GLU   B 1 80 ? 10.628  -7.060  -29.503 1.00 27.44  ? 79  GLU   B C   1 
ATOM   1366 O O   . GLU   B 1 80 ? 10.938  -6.195  -30.326 1.00 27.33  ? 79  GLU   B O   1 
ATOM   1367 C CB  . GLU   B 1 80 ? 9.996   -6.327  -27.197 1.00 30.87  ? 79  GLU   B CB  1 
ATOM   1368 C CG  . GLU   B 1 80 ? 8.893   -5.678  -26.364 1.00 39.06  ? 79  GLU   B CG  1 
ATOM   1369 N N   . GLY   B 1 81 ? 11.237  -8.256  -29.393 1.00 25.70  ? 80  GLY   B N   1 
ATOM   1370 C CA  . GLY   B 1 81 ? 12.338  -8.675  -30.261 1.00 26.01  ? 80  GLY   B CA  1 
ATOM   1371 C C   . GLY   B 1 81 ? 11.879  -8.725  -31.717 1.00 28.78  ? 80  GLY   B C   1 
ATOM   1372 O O   . GLY   B 1 81 ? 12.635  -8.317  -32.607 1.00 26.49  ? 80  GLY   B O   1 
ATOM   1373 N N   . LEU   B 1 82 ? 10.656  -9.219  -31.948 1.00 25.60  ? 81  LEU   B N   1 
ATOM   1374 C CA  . LEU   B 1 82 ? 10.065  -9.201  -33.282 1.00 28.42  ? 81  LEU   B CA  1 
ATOM   1375 C C   . LEU   B 1 82 ? 9.937   -7.772  -33.822 1.00 31.30  ? 81  LEU   B C   1 
ATOM   1376 O O   . LEU   B 1 82 ? 10.211  -7.510  -34.999 1.00 28.73  ? 81  LEU   B O   1 
ATOM   1377 C CB  . LEU   B 1 82 ? 8.735   -9.968  -33.356 1.00 27.11  ? 81  LEU   B CB  1 
ATOM   1378 C CG  . LEU   B 1 82 ? 8.826   -11.486 -33.140 1.00 28.65  ? 81  LEU   B CG  1 
ATOM   1379 C CD1 . LEU   B 1 82 ? 7.451   -12.100 -33.196 1.00 26.00  ? 81  LEU   B CD1 1 
ATOM   1380 C CD2 . LEU   B 1 82 ? 9.743   -12.178 -34.166 1.00 26.42  ? 81  LEU   B CD2 1 
ATOM   1381 N N   . TRP   B 1 83 ? 9.466   -6.845  -32.983 1.00 27.39  ? 82  TRP   B N   1 
ATOM   1382 C CA  . TRP   B 1 83 ? 9.403   -5.435  -33.365 1.00 28.22  ? 82  TRP   B CA  1 
ATOM   1383 C C   . TRP   B 1 83 ? 10.785  -4.902  -33.732 1.00 28.37  ? 82  TRP   B C   1 
ATOM   1384 O O   . TRP   B 1 83 ? 10.902  -4.230  -34.765 1.00 29.53  ? 82  TRP   B O   1 
ATOM   1385 C CB  . TRP   B 1 83 ? 8.773   -4.565  -32.262 1.00 30.29  ? 82  TRP   B CB  1 
ATOM   1386 C CG  . TRP   B 1 83 ? 8.491   -3.159  -32.737 1.00 31.69  ? 82  TRP   B CG  1 
ATOM   1387 C CD1 . TRP   B 1 83 ? 7.345   -2.709  -33.323 1.00 34.57  ? 82  TRP   B CD1 1 
ATOM   1388 C CD2 . TRP   B 1 83 ? 9.420   -2.050  -32.755 1.00 33.87  ? 82  TRP   B CD2 1 
ATOM   1389 N NE1 . TRP   B 1 83 ? 7.477   -1.387  -33.669 1.00 38.39  ? 82  TRP   B NE1 1 
ATOM   1390 C CE2 . TRP   B 1 83 ? 8.735   -0.954  -33.339 1.00 33.78  ? 82  TRP   B CE2 1 
ATOM   1391 C CE3 . TRP   B 1 83 ? 10.749  -1.876  -32.333 1.00 33.84  ? 82  TRP   B CE3 1 
ATOM   1392 C CZ2 . TRP   B 1 83 ? 9.343   0.295   -33.498 1.00 37.06  ? 82  TRP   B CZ2 1 
ATOM   1393 C CZ3 . TRP   B 1 83 ? 11.339  -0.630  -32.472 1.00 34.70  ? 82  TRP   B CZ3 1 
ATOM   1394 C CH2 . TRP   B 1 83 ? 10.639  0.434   -33.047 1.00 34.24  ? 82  TRP   B CH2 1 
ATOM   1395 N N   . GLU   B 1 84 ? 11.802  -5.224  -32.928 1.00 26.14  ? 83  GLU   B N   1 
ATOM   1396 C CA  . GLU   B 1 84 ? 13.136  -4.672  -33.089 1.00 26.65  ? 83  GLU   B CA  1 
ATOM   1397 C C   . GLU   B 1 84 ? 13.757  -5.139  -34.412 1.00 29.05  ? 83  GLU   B C   1 
ATOM   1398 O O   . GLU   B 1 84 ? 14.395  -4.351  -35.145 1.00 29.32  ? 83  GLU   B O   1 
ATOM   1399 C CB  . GLU   B 1 84 ? 14.079  -4.998  -31.939 1.00 27.66  ? 83  GLU   B CB  1 
ATOM   1400 C CG  . GLU   B 1 84 ? 13.622  -4.295  -30.661 1.00 31.24  ? 83  GLU   B CG  1 
ATOM   1401 C CD  . GLU   B 1 84 ? 14.510  -4.589  -29.489 1.00 30.05  ? 83  GLU   B CD  1 
ATOM   1402 O OE1 . GLU   B 1 84 ? 15.466  -5.427  -29.565 1.00 26.97  ? 83  GLU   B OE1 1 
ATOM   1403 O OE2 . GLU   B 1 84 ? 14.181  -3.978  -28.405 1.00 29.78  ? 83  GLU   B OE2 1 
ATOM   1404 N N   . ILE   B 1 85 ? 13.579  -6.430  -34.730 1.00 26.42  ? 84  ILE   B N   1 
ATOM   1405 C CA  . ILE   B 1 85 ? 14.317  -6.981  -35.866 1.00 24.25  ? 84  ILE   B CA  1 
ATOM   1406 C C   . ILE   B 1 85 ? 13.709  -6.452  -37.168 1.00 25.77  ? 84  ILE   B C   1 
ATOM   1407 O O   . ILE   B 1 85 ? 14.424  -6.334  -38.187 1.00 25.57  ? 84  ILE   B O   1 
ATOM   1408 C CB  . ILE   B 1 85 ? 14.387  -8.521  -35.838 1.00 24.26  ? 84  ILE   B CB  1 
ATOM   1409 C CG1 . ILE   B 1 85 ? 15.407  -9.073  -36.860 1.00 26.75  ? 84  ILE   B CG1 1 
ATOM   1410 C CG2 . ILE   B 1 85 ? 12.997  -9.134  -36.046 1.00 25.48  ? 84  ILE   B CG2 1 
ATOM   1411 C CD1 . ILE   B 1 85 ? 15.923  -10.475 -36.490 1.00 25.84  ? 84  ILE   B CD1 1 
ATOM   1412 N N   . GLN   B 1 86 ? 12.405  -6.113  -37.117 1.00 27.60  ? 85  GLN   B N   1 
ATOM   1413 C CA  . GLN   B 1 86 ? 11.647  -5.631  -38.255 1.00 29.03  ? 85  GLN   B CA  1 
ATOM   1414 C C   . GLN   B 1 86 ? 11.841  -4.120  -38.412 1.00 31.62  ? 85  GLN   B C   1 
ATOM   1415 O O   . GLN   B 1 86 ? 11.923  -3.631  -39.533 1.00 33.02  ? 85  GLN   B O   1 
ATOM   1416 C CB  . GLN   B 1 86 ? 10.150  -5.942  -38.130 1.00 36.23  ? 85  GLN   B CB  1 
ATOM   1417 N N   . ASN   B 1 87 ? 11.957  -3.384  -37.296 1.00 28.74  ? 86  ASN   B N   1 
ATOM   1418 C CA  . ASN   B 1 87 ? 11.812  -1.928  -37.391 1.00 29.28  ? 86  ASN   B CA  1 
ATOM   1419 C C   . ASN   B 1 87 ? 13.118  -1.169  -37.191 1.00 28.23  ? 86  ASN   B C   1 
ATOM   1420 O O   . ASN   B 1 87 ? 13.221  -0.025  -37.668 1.00 28.88  ? 86  ASN   B O   1 
ATOM   1421 C CB  . ASN   B 1 87 ? 10.725  -1.406  -36.443 1.00 31.08  ? 86  ASN   B CB  1 
ATOM   1422 C CG  . ASN   B 1 87 ? 9.351   -1.817  -36.930 1.00 36.83  ? 86  ASN   B CG  1 
ATOM   1423 O OD1 . ASN   B 1 87 ? 8.862   -1.269  -37.916 1.00 41.94  ? 86  ASN   B OD1 1 
ATOM   1424 N ND2 . ASN   B 1 87 ? 8.730   -2.803  -36.305 1.00 34.81  ? 86  ASN   B ND2 1 
ATOM   1425 N N   . ASN   B 1 88 ? 14.088  -1.747  -36.477 1.00 26.78  ? 87  ASN   B N   1 
ATOM   1426 C CA  . ASN   B 1 88 ? 15.349  -1.056  -36.210 1.00 29.06  ? 87  ASN   B CA  1 
ATOM   1427 C C   . ASN   B 1 88 ? 16.431  -2.057  -35.817 1.00 27.46  ? 87  ASN   B C   1 
ATOM   1428 O O   . ASN   B 1 88 ? 17.006  -1.979  -34.738 1.00 27.21  ? 87  ASN   B O   1 
ATOM   1429 C CB  . ASN   B 1 88 ? 15.227  0.114   -35.220 1.00 32.32  ? 87  ASN   B CB  1 
ATOM   1430 C CG  . ASN   B 1 88 ? 16.307  1.156   -35.456 1.00 34.15  ? 87  ASN   B CG  1 
ATOM   1431 O OD1 . ASN   B 1 88 ? 17.318  0.901   -36.114 1.00 30.14  ? 87  ASN   B OD1 1 
ATOM   1432 N ND2 . ASN   B 1 88 ? 16.143  2.353   -34.905 1.00 34.65  ? 87  ASN   B ND2 1 
ATOM   1433 N N   . PRO   B 1 89 ? 16.723  -3.048  -36.694 1.00 26.55  ? 88  PRO   B N   1 
ATOM   1434 C CA  . PRO   B 1 89 ? 17.649  -4.125  -36.360 1.00 25.73  ? 88  PRO   B CA  1 
ATOM   1435 C C   . PRO   B 1 89 ? 19.086  -3.711  -36.094 1.00 25.65  ? 88  PRO   B C   1 
ATOM   1436 O O   . PRO   B 1 89 ? 19.831  -4.454  -35.466 1.00 25.97  ? 88  PRO   B O   1 
ATOM   1437 C CB  . PRO   B 1 89 ? 17.567  -5.070  -37.590 1.00 25.12  ? 88  PRO   B CB  1 
ATOM   1438 C CG  . PRO   B 1 89 ? 17.128  -4.172  -38.716 1.00 26.75  ? 88  PRO   B CG  1 
ATOM   1439 C CD  . PRO   B 1 89 ? 16.168  -3.150  -38.068 1.00 26.01  ? 88  PRO   B CD  1 
ATOM   1440 N N   . HIS   B 1 90 ? 19.485  -2.516  -36.604 1.00 24.97  ? 89  HIS   B N   1 
ATOM   1441 C CA  . HIS   B 1 90 ? 20.890  -2.151  -36.492 1.00 26.23  ? 89  HIS   B CA  1 
ATOM   1442 C C   . HIS   B 1 90 ? 21.122  -1.020  -35.475 1.00 26.77  ? 89  HIS   B C   1 
ATOM   1443 O O   . HIS   B 1 90 ? 22.229  -0.477  -35.376 1.00 28.71  ? 89  HIS   B O   1 
ATOM   1444 C CB  . HIS   B 1 90 ? 21.444  -1.763  -37.874 1.00 26.78  ? 89  HIS   B CB  1 
ATOM   1445 C CG  . HIS   B 1 90 ? 21.208  -2.828  -38.889 1.00 26.48  ? 89  HIS   B CG  1 
ATOM   1446 N ND1 . HIS   B 1 90 ? 21.845  -4.050  -38.780 1.00 28.81  ? 89  HIS   B ND1 1 
ATOM   1447 C CD2 . HIS   B 1 90 ? 20.505  -2.865  -40.038 1.00 28.02  ? 89  HIS   B CD2 1 
ATOM   1448 C CE1 . HIS   B 1 90 ? 21.491  -4.811  -39.817 1.00 27.39  ? 89  HIS   B CE1 1 
ATOM   1449 N NE2 . HIS   B 1 90 ? 20.713  -4.099  -40.596 1.00 27.47  ? 89  HIS   B NE2 1 
ATOM   1450 N N   . ALA   B 1 91 ? 20.143  -0.795  -34.604 1.00 27.40  ? 90  ALA   B N   1 
ATOM   1451 C CA  . ALA   B 1 91 ? 20.259  0.266   -33.612 1.00 27.25  ? 90  ALA   B CA  1 
ATOM   1452 C C   . ALA   B 1 91 ? 21.148  -0.146  -32.440 1.00 30.45  ? 90  ALA   B C   1 
ATOM   1453 O O   . ALA   B 1 91 ? 21.481  -1.317  -32.246 1.00 28.14  ? 90  ALA   B O   1 
ATOM   1454 C CB  . ALA   B 1 91 ? 18.870  0.701   -33.158 1.00 27.22  ? 90  ALA   B CB  1 
ATOM   1455 N N   . SER   B 1 92 ? 21.561  0.870   -31.658 1.00 32.27  ? 91  SER   B N   1 
ATOM   1456 C CA  . SER   B 1 92 ? 22.209  0.697   -30.369 1.00 35.49  ? 91  SER   B CA  1 
ATOM   1457 C C   . SER   B 1 92 ? 21.111  0.475   -29.320 1.00 37.51  ? 91  SER   B C   1 
ATOM   1458 O O   . SER   B 1 92 ? 20.178  1.278   -29.227 1.00 38.99  ? 91  SER   B O   1 
ATOM   1459 C CB  . SER   B 1 92 ? 23.043  1.949   -30.033 1.00 34.32  ? 91  SER   B CB  1 
ATOM   1460 O OG  . SER   B 1 92 ? 23.703  1.746   -28.790 1.00 41.73  ? 91  SER   B OG  1 
ATOM   1461 N N   . TYR   B 1 93 ? 21.180  -0.679  -28.627 1.00 34.02  ? 92  TYR   B N   1 
ATOM   1462 C CA  . TYR   B 1 93 ? 20.266  -1.090  -27.565 1.00 35.97  ? 92  TYR   B CA  1 
ATOM   1463 C C   . TYR   B 1 93 ? 21.059  -1.125  -26.257 1.00 45.39  ? 92  TYR   B C   1 
ATOM   1464 O O   . TYR   B 1 93 ? 20.592  -1.622  -25.239 1.00 49.89  ? 92  TYR   B O   1 
ATOM   1465 C CB  . TYR   B 1 93 ? 19.639  -2.452  -27.903 1.00 32.53  ? 92  TYR   B CB  1 
ATOM   1466 C CG  . TYR   B 1 93 ? 18.664  -2.337  -29.062 1.00 28.35  ? 92  TYR   B CG  1 
ATOM   1467 C CD1 . TYR   B 1 93 ? 17.368  -1.881  -28.871 1.00 28.77  ? 92  TYR   B CD1 1 
ATOM   1468 C CD2 . TYR   B 1 93 ? 19.018  -2.710  -30.365 1.00 29.07  ? 92  TYR   B CD2 1 
ATOM   1469 C CE1 . TYR   B 1 93 ? 16.473  -1.747  -29.921 1.00 33.27  ? 92  TYR   B CE1 1 
ATOM   1470 C CE2 . TYR   B 1 93 ? 18.125  -2.604  -31.422 1.00 29.48  ? 92  TYR   B CE2 1 
ATOM   1471 C CZ  . TYR   B 1 93 ? 16.842  -2.139  -31.202 1.00 29.84  ? 92  TYR   B CZ  1 
ATOM   1472 O OH  . TYR   B 1 93 ? 15.945  -2.013  -32.211 1.00 31.06  ? 92  TYR   B OH  1 
ATOM   1473 N N   . SER   B 1 94 ? 22.258  -0.536  -26.314 1.00 53.30  ? 93  SER   B N   1 
ATOM   1474 C CA  . SER   B 1 94 ? 23.129  -0.247  -25.184 1.00 65.55  ? 93  SER   B CA  1 
ATOM   1475 C C   . SER   B 1 94 ? 22.375  0.512   -24.078 1.00 74.85  ? 93  SER   B C   1 
ATOM   1476 O O   . SER   B 1 94 ? 21.272  1.041   -24.370 1.00 81.15  ? 93  SER   B O   1 
ATOM   1477 C CB  . SER   B 1 94 ? 24.300  0.583   -25.651 1.00 67.14  ? 93  SER   B CB  1 
ATOM   1478 O OG  . SER   B 1 94 ? 25.056  -0.084  -26.650 1.00 75.89  ? 93  SER   B OG  1 
ATOM   1479 O OXT . SER   B 1 94 ? 22.938  0.585   -22.962 1.00 79.94  ? 93  SER   B OXT 1 
ATOM   1480 N N   . HIS   C 1 4  ? 32.581  -23.591 28.644  1.00 72.84  ? 3   HIS   C N   1 
ATOM   1481 C CA  . HIS   C 1 4  ? 31.372  -22.798 28.280  1.00 81.63  ? 3   HIS   C CA  1 
ATOM   1482 C C   . HIS   C 1 4  ? 30.266  -23.095 29.297  1.00 81.41  ? 3   HIS   C C   1 
ATOM   1483 O O   . HIS   C 1 4  ? 30.367  -24.040 30.079  1.00 81.75  ? 3   HIS   C O   1 
ATOM   1484 C CB  . HIS   C 1 4  ? 31.001  -23.035 26.807  1.00 84.84  ? 3   HIS   C CB  1 
ATOM   1485 C CG  . HIS   C 1 4  ? 30.234  -21.912 26.171  1.00 94.90  ? 3   HIS   C CG  1 
ATOM   1486 N ND1 . HIS   C 1 4  ? 28.856  -21.835 26.160  1.00 90.28  ? 3   HIS   C ND1 1 
ATOM   1487 C CD2 . HIS   C 1 4  ? 30.662  -20.810 25.527  1.00 94.15  ? 3   HIS   C CD2 1 
ATOM   1488 C CE1 . HIS   C 1 4  ? 28.478  -20.724 25.539  1.00 86.33  ? 3   HIS   C CE1 1 
ATOM   1489 N NE2 . HIS   C 1 4  ? 29.558  -20.086 25.148  1.00 83.10  ? 3   HIS   C NE2 1 
ATOM   1490 N N   . ALA   C 1 5  ? 29.210  -22.276 29.276  1.00 78.64  ? 4   ALA   C N   1 
ATOM   1491 C CA  . ALA   C 1 5  ? 28.145  -22.330 30.264  1.00 80.11  ? 4   ALA   C CA  1 
ATOM   1492 C C   . ALA   C 1 5  ? 26.819  -22.669 29.594  1.00 74.65  ? 4   ALA   C C   1 
ATOM   1493 O O   . ALA   C 1 5  ? 26.461  -22.045 28.596  1.00 81.52  ? 4   ALA   C O   1 
ATOM   1494 C CB  . ALA   C 1 5  ? 28.030  -20.975 30.911  1.00 87.25  ? 4   ALA   C CB  1 
ATOM   1495 N N   . PHE   C 1 6  ? 26.081  -23.613 30.187  1.00 56.03  ? 5   PHE   C N   1 
ATOM   1496 C CA  . PHE   C 1 6  ? 24.732  -23.904 29.732  1.00 55.00  ? 5   PHE   C CA  1 
ATOM   1497 C C   . PHE   C 1 6  ? 23.817  -24.024 30.947  1.00 60.59  ? 5   PHE   C C   1 
ATOM   1498 O O   . PHE   C 1 6  ? 24.056  -24.855 31.822  1.00 69.43  ? 5   PHE   C O   1 
ATOM   1499 C CB  . PHE   C 1 6  ? 24.743  -25.173 28.861  1.00 49.92  ? 5   PHE   C CB  1 
ATOM   1500 C CG  . PHE   C 1 6  ? 25.575  -25.124 27.581  1.00 46.08  ? 5   PHE   C CG  1 
ATOM   1501 C CD1 . PHE   C 1 6  ? 26.765  -25.833 27.465  1.00 44.57  ? 5   PHE   C CD1 1 
ATOM   1502 C CD2 . PHE   C 1 6  ? 25.190  -24.324 26.504  1.00 50.54  ? 5   PHE   C CD2 1 
ATOM   1503 C CE1 . PHE   C 1 6  ? 27.519  -25.784 26.298  1.00 47.46  ? 5   PHE   C CE1 1 
ATOM   1504 C CE2 . PHE   C 1 6  ? 25.960  -24.267 25.344  1.00 47.89  ? 5   PHE   C CE2 1 
ATOM   1505 C CZ  . PHE   C 1 6  ? 27.112  -25.002 25.240  1.00 45.32  ? 5   PHE   C CZ  1 
ATOM   1506 N N   . LYS   C 1 7  ? 22.757  -23.208 30.991  1.00 53.72  ? 6   LYS   C N   1 
ATOM   1507 C CA  . LYS   C 1 7  ? 21.770  -23.307 32.060  1.00 50.85  ? 6   LYS   C CA  1 
ATOM   1508 C C   . LYS   C 1 7  ? 20.443  -23.734 31.438  1.00 46.77  ? 6   LYS   C C   1 
ATOM   1509 O O   . LYS   C 1 7  ? 20.253  -23.549 30.227  1.00 48.58  ? 6   LYS   C O   1 
ATOM   1510 C CB  . LYS   C 1 7  ? 21.706  -21.969 32.816  1.00 50.97  ? 6   LYS   C CB  1 
ATOM   1511 N N   . PRO   C 1 8  ? 19.487  -24.333 32.196  1.00 45.18  ? 7   PRO   C N   1 
ATOM   1512 C CA  . PRO   C 1 8  ? 18.196  -24.725 31.615  1.00 47.67  ? 7   PRO   C CA  1 
ATOM   1513 C C   . PRO   C 1 8  ? 17.547  -23.557 30.863  1.00 56.74  ? 7   PRO   C C   1 
ATOM   1514 O O   . PRO   C 1 8  ? 17.496  -22.439 31.379  1.00 62.45  ? 7   PRO   C O   1 
ATOM   1515 C CB  . PRO   C 1 8  ? 17.361  -25.217 32.822  1.00 51.96  ? 7   PRO   C CB  1 
ATOM   1516 C CG  . PRO   C 1 8  ? 18.411  -25.639 33.839  1.00 44.99  ? 7   PRO   C CG  1 
ATOM   1517 C CD  . PRO   C 1 8  ? 19.594  -24.687 33.630  1.00 43.76  ? 7   PRO   C CD  1 
ATOM   1518 N N   . GLY   C 1 9  ? 17.086  -23.812 29.629  1.00 58.43  ? 8   GLY   C N   1 
ATOM   1519 C CA  . GLY   C 1 9  ? 16.440  -22.786 28.822  1.00 50.69  ? 8   GLY   C CA  1 
ATOM   1520 C C   . GLY   C 1 9  ? 17.349  -22.190 27.741  1.00 51.26  ? 8   GLY   C C   1 
ATOM   1521 O O   . GLY   C 1 9  ? 16.838  -21.585 26.800  1.00 53.02  ? 8   GLY   C O   1 
ATOM   1522 N N   . ASP   C 1 10 ? 18.679  -22.357 27.856  1.00 45.01  ? 9   ASP   C N   1 
ATOM   1523 C CA  . ASP   C 1 10 ? 19.641  -21.876 26.869  1.00 38.44  ? 9   ASP   C CA  1 
ATOM   1524 C C   . ASP   C 1 10 ? 19.507  -22.606 25.525  1.00 42.05  ? 9   ASP   C C   1 
ATOM   1525 O O   . ASP   C 1 10 ? 19.512  -23.825 25.479  1.00 39.43  ? 9   ASP   C O   1 
ATOM   1526 C CB  . ASP   C 1 10 ? 21.085  -22.129 27.275  1.00 40.33  ? 9   ASP   C CB  1 
ATOM   1527 C CG  . ASP   C 1 10 ? 21.732  -21.119 28.221  1.00 54.05  ? 9   ASP   C CG  1 
ATOM   1528 O OD1 . ASP   C 1 10 ? 20.998  -20.258 28.759  1.00 60.66  ? 9   ASP   C OD1 1 
ATOM   1529 O OD2 . ASP   C 1 10 ? 22.976  -21.190 28.400  1.00 59.71  ? 9   ASP   C OD2 1 
ATOM   1530 N N   . LEU   C 1 11 ? 19.492  -21.853 24.415  1.00 37.68  ? 10  LEU   C N   1 
ATOM   1531 C CA  . LEU   C 1 11 ? 19.198  -22.404 23.099  1.00 39.20  ? 10  LEU   C CA  1 
ATOM   1532 C C   . LEU   C 1 11 ? 20.481  -22.880 22.407  1.00 34.93  ? 10  LEU   C C   1 
ATOM   1533 O O   . LEU   C 1 11 ? 21.490  -22.188 22.414  1.00 33.04  ? 10  LEU   C O   1 
ATOM   1534 C CB  . LEU   C 1 11 ? 18.503  -21.301 22.299  1.00 35.86  ? 10  LEU   C CB  1 
ATOM   1535 C CG  . LEU   C 1 11 ? 17.168  -20.793 22.849  1.00 35.89  ? 10  LEU   C CG  1 
ATOM   1536 C CD1 . LEU   C 1 11 ? 16.529  -19.773 21.884  1.00 35.31  ? 10  LEU   C CD1 1 
ATOM   1537 C CD2 . LEU   C 1 11 ? 16.170  -21.905 23.179  1.00 35.55  ? 10  LEU   C CD2 1 
ATOM   1538 N N   . VAL   C 1 12 ? 20.445  -24.071 21.763  1.00 30.98  ? 11  VAL   C N   1 
ATOM   1539 C CA  . VAL   C 1 12 ? 21.654  -24.662 21.209  1.00 30.35  ? 11  VAL   C CA  1 
ATOM   1540 C C   . VAL   C 1 12 ? 21.309  -25.419 19.910  1.00 29.10  ? 11  VAL   C C   1 
ATOM   1541 O O   . VAL   C 1 12 ? 20.140  -25.654 19.626  1.00 28.87  ? 11  VAL   C O   1 
ATOM   1542 C CB  . VAL   C 1 12 ? 22.305  -25.667 22.189  1.00 32.17  ? 11  VAL   C CB  1 
ATOM   1543 C CG1 . VAL   C 1 12 ? 22.793  -24.992 23.470  1.00 34.26  ? 11  VAL   C CG1 1 
ATOM   1544 C CG2 . VAL   C 1 12 ? 21.372  -26.849 22.518  1.00 30.71  ? 11  VAL   C CG2 1 
ATOM   1545 N N   . PHE   C 1 13 ? 22.346  -25.763 19.136  1.00 30.22  ? 12  PHE   C N   1 
ATOM   1546 C CA  . PHE   C 1 13 ? 22.305  -26.939 18.265  1.00 27.59  ? 12  PHE   C CA  1 
ATOM   1547 C C   . PHE   C 1 13 ? 22.981  -28.117 18.973  1.00 27.84  ? 12  PHE   C C   1 
ATOM   1548 O O   . PHE   C 1 13 ? 24.085  -27.996 19.518  1.00 32.59  ? 12  PHE   C O   1 
ATOM   1549 C CB  . PHE   C 1 13 ? 22.902  -26.733 16.859  1.00 30.66  ? 12  PHE   C CB  1 
ATOM   1550 C CG  . PHE   C 1 13 ? 22.110  -25.749 16.015  1.00 33.42  ? 12  PHE   C CG  1 
ATOM   1551 C CD1 . PHE   C 1 13 ? 21.085  -26.186 15.171  1.00 34.03  ? 12  PHE   C CD1 1 
ATOM   1552 C CD2 . PHE   C 1 13 ? 22.376  -24.382 16.094  1.00 35.35  ? 12  PHE   C CD2 1 
ATOM   1553 C CE1 . PHE   C 1 13 ? 20.352  -25.262 14.431  1.00 34.65  ? 12  PHE   C CE1 1 
ATOM   1554 C CE2 . PHE   C 1 13 ? 21.624  -23.465 15.370  1.00 34.19  ? 12  PHE   C CE2 1 
ATOM   1555 C CZ  . PHE   C 1 13 ? 20.621  -23.915 14.549  1.00 34.43  ? 12  PHE   C CZ  1 
ATOM   1556 N N   . ALA   C 1 14 ? 22.323  -29.285 18.946  1.00 28.37  ? 13  ALA   C N   1 
ATOM   1557 C CA  . ALA   C 1 14 ? 22.781  -30.471 19.666  1.00 25.69  ? 13  ALA   C CA  1 
ATOM   1558 C C   . ALA   C 1 14 ? 23.073  -31.580 18.663  1.00 28.72  ? 13  ALA   C C   1 
ATOM   1559 O O   . ALA   C 1 14 ? 22.218  -31.897 17.833  1.00 26.01  ? 13  ALA   C O   1 
ATOM   1560 C CB  . ALA   C 1 14 ? 21.690  -30.939 20.610  1.00 27.25  ? 13  ALA   C CB  1 
ATOM   1561 N N   . LYS   C 1 15 ? 24.267  -32.176 18.764  1.00 27.90  ? 14  LYS   C N   1 
ATOM   1562 C CA  . LYS   C 1 15 ? 24.658  -33.194 17.793  1.00 28.19  ? 14  LYS   C CA  1 
ATOM   1563 C C   . LYS   C 1 15 ? 24.654  -34.569 18.451  1.00 27.10  ? 14  LYS   C C   1 
ATOM   1564 O O   . LYS   C 1 15 ? 25.360  -34.785 19.428  1.00 29.86  ? 14  LYS   C O   1 
ATOM   1565 C CB  . LYS   C 1 15 ? 26.089  -32.952 17.281  1.00 30.26  ? 14  LYS   C CB  1 
ATOM   1566 C CG  . LYS   C 1 15 ? 26.544  -33.944 16.194  1.00 30.79  ? 14  LYS   C CG  1 
ATOM   1567 C CD  . LYS   C 1 15 ? 25.665  -33.864 14.943  1.00 27.74  ? 14  LYS   C CD  1 
ATOM   1568 C CE  . LYS   C 1 15 ? 26.171  -34.688 13.725  1.00 29.40  ? 14  LYS   C CE  1 
ATOM   1569 N NZ  . LYS   C 1 15 ? 26.023  -36.112 14.043  1.00 27.94  ? 14  LYS   C NZ  1 
ATOM   1570 N N   . MET   C 1 16 ? 23.866  -35.496 17.890  1.00 24.78  ? 15  MET   C N   1 
ATOM   1571 C CA  . MET   C 1 16 ? 23.841  -36.903 18.276  1.00 27.17  ? 15  MET   C CA  1 
ATOM   1572 C C   . MET   C 1 16 ? 24.259  -37.729 17.062  1.00 28.87  ? 15  MET   C C   1 
ATOM   1573 O O   . MET   C 1 16 ? 23.974  -37.348 15.922  1.00 26.41  ? 15  MET   C O   1 
ATOM   1574 C CB  . MET   C 1 16 ? 22.432  -37.368 18.672  1.00 27.24  ? 15  MET   C CB  1 
ATOM   1575 C CG  . MET   C 1 16 ? 21.900  -36.685 19.922  1.00 32.78  ? 15  MET   C CG  1 
ATOM   1576 S SD  . MET   C 1 16 ? 20.368  -37.496 20.399  1.00 41.73  ? 15  MET   C SD  1 
ATOM   1577 C CE  . MET   C 1 16 ? 21.034  -39.014 21.107  1.00 45.34  ? 15  MET   C CE  1 
ATOM   1578 N N   . LYS   C 1 17 ? 24.919  -38.872 17.327  1.00 29.36  ? 16  LYS   C N   1 
ATOM   1579 C CA  . LYS   C 1 17 ? 25.322  -39.753 16.237  1.00 32.86  ? 16  LYS   C CA  1 
ATOM   1580 C C   . LYS   C 1 17 ? 24.058  -40.188 15.500  1.00 26.61  ? 16  LYS   C C   1 
ATOM   1581 O O   . LYS   C 1 17 ? 23.091  -40.643 16.120  1.00 29.59  ? 16  LYS   C O   1 
ATOM   1582 C CB  . LYS   C 1 17 ? 25.976  -41.024 16.817  1.00 32.94  ? 16  LYS   C CB  1 
ATOM   1583 C CG  . LYS   C 1 17 ? 26.666  -41.941 15.798  1.00 39.85  ? 16  LYS   C CG  1 
ATOM   1584 C CD  . LYS   C 1 17 ? 27.910  -41.266 15.232  1.00 42.11  ? 16  LYS   C CD  1 
ATOM   1585 C CE  . LYS   C 1 17 ? 28.530  -42.047 14.106  1.00 50.88  ? 16  LYS   C CE  1 
ATOM   1586 N NZ  . LYS   C 1 17 ? 29.793  -41.405 13.728  1.00 45.43  ? 16  LYS   C NZ  1 
ATOM   1587 N N   . GLY   C 1 18 ? 24.125  -40.040 14.175  1.00 27.55  ? 17  GLY   C N   1 
ATOM   1588 C CA  . GLY   C 1 18 ? 23.072  -40.528 13.301  1.00 32.38  ? 17  GLY   C CA  1 
ATOM   1589 C C   . GLY   C 1 18 ? 22.069  -39.426 12.938  1.00 32.36  ? 17  GLY   C C   1 
ATOM   1590 O O   . GLY   C 1 18 ? 21.044  -39.742 12.333  1.00 30.38  ? 17  GLY   C O   1 
ATOM   1591 N N   . TYR   C 1 19 ? 22.336  -38.182 13.387  1.00 28.35  ? 18  TYR   C N   1 
ATOM   1592 C CA  . TYR   C 1 19 ? 21.417  -37.053 13.204  1.00 26.06  ? 18  TYR   C CA  1 
ATOM   1593 C C   . TYR   C 1 19 ? 22.213  -35.789 12.901  1.00 28.00  ? 18  TYR   C C   1 
ATOM   1594 O O   . TYR   C 1 19 ? 23.334  -35.606 13.387  1.00 28.85  ? 18  TYR   C O   1 
ATOM   1595 C CB  . TYR   C 1 19 ? 20.618  -36.749 14.482  1.00 25.95  ? 18  TYR   C CB  1 
ATOM   1596 C CG  . TYR   C 1 19 ? 19.759  -37.936 14.874  1.00 26.37  ? 18  TYR   C CG  1 
ATOM   1597 C CD1 . TYR   C 1 19 ? 20.290  -38.963 15.662  1.00 28.25  ? 18  TYR   C CD1 1 
ATOM   1598 C CD2 . TYR   C 1 19 ? 18.486  -38.079 14.356  1.00 28.14  ? 18  TYR   C CD2 1 
ATOM   1599 C CE1 . TYR   C 1 19 ? 19.525  -40.065 15.991  1.00 29.47  ? 18  TYR   C CE1 1 
ATOM   1600 C CE2 . TYR   C 1 19 ? 17.723  -39.191 14.671  1.00 33.56  ? 18  TYR   C CE2 1 
ATOM   1601 C CZ  . TYR   C 1 19 ? 18.245  -40.179 15.484  1.00 35.94  ? 18  TYR   C CZ  1 
ATOM   1602 O OH  . TYR   C 1 19 ? 17.457  -41.255 15.800  1.00 43.50  ? 18  TYR   C OH  1 
ATOM   1603 N N   . PRO   C 1 20 ? 21.662  -34.849 12.091  1.00 25.58  ? 19  PRO   C N   1 
ATOM   1604 C CA  . PRO   C 1 20 ? 22.318  -33.560 11.861  1.00 25.28  ? 19  PRO   C CA  1 
ATOM   1605 C C   . PRO   C 1 20 ? 22.279  -32.741 13.147  1.00 23.24  ? 19  PRO   C C   1 
ATOM   1606 O O   . PRO   C 1 20 ? 21.505  -33.024 14.059  1.00 24.79  ? 19  PRO   C O   1 
ATOM   1607 C CB  . PRO   C 1 20 ? 21.415  -32.913 10.760  1.00 27.29  ? 19  PRO   C CB  1 
ATOM   1608 C CG  . PRO   C 1 20 ? 20.062  -33.539 10.995  1.00 27.45  ? 19  PRO   C CG  1 
ATOM   1609 C CD  . PRO   C 1 20 ? 20.360  -34.966 11.409  1.00 26.52  ? 19  PRO   C CD  1 
ATOM   1610 N N   . HIS   C 1 21 ? 23.096  -31.690 13.172  1.00 26.03  ? 20  HIS   C N   1 
ATOM   1611 C CA  . HIS   C 1 21 ? 23.054  -30.762 14.287  1.00 25.84  ? 20  HIS   C CA  1 
ATOM   1612 C C   . HIS   C 1 21 ? 21.632  -30.220 14.408  1.00 25.52  ? 20  HIS   C C   1 
ATOM   1613 O O   . HIS   C 1 21 ? 21.083  -29.706 13.430  1.00 28.28  ? 20  HIS   C O   1 
ATOM   1614 C CB  . HIS   C 1 21 ? 24.050  -29.635 14.022  1.00 28.11  ? 20  HIS   C CB  1 
ATOM   1615 C CG  . HIS   C 1 21 ? 25.477  -30.057 14.113  1.00 28.72  ? 20  HIS   C CG  1 
ATOM   1616 N ND1 . HIS   C 1 21 ? 26.138  -30.726 13.099  1.00 34.67  ? 20  HIS   C ND1 1 
ATOM   1617 C CD2 . HIS   C 1 21 ? 26.389  -29.842 15.097  1.00 31.96  ? 20  HIS   C CD2 1 
ATOM   1618 C CE1 . HIS   C 1 21 ? 27.395  -30.964 13.490  1.00 34.82  ? 20  HIS   C CE1 1 
ATOM   1619 N NE2 . HIS   C 1 21 ? 27.585  -30.420 14.682  1.00 33.50  ? 20  HIS   C NE2 1 
ATOM   1620 N N   . TRP   C 1 22 ? 21.045  -30.341 15.614  1.00 23.65  ? 21  TRP   C N   1 
ATOM   1621 C CA  . TRP   C 1 22 ? 19.591  -30.236 15.721  1.00 22.39  ? 21  TRP   C CA  1 
ATOM   1622 C C   . TRP   C 1 22 ? 19.202  -29.087 16.650  1.00 23.77  ? 21  TRP   C C   1 
ATOM   1623 O O   . TRP   C 1 22 ? 19.796  -28.946 17.727  1.00 25.27  ? 21  TRP   C O   1 
ATOM   1624 C CB  . TRP   C 1 22 ? 19.075  -31.561 16.313  1.00 25.61  ? 21  TRP   C CB  1 
ATOM   1625 C CG  . TRP   C 1 22 ? 17.618  -31.789 15.985  1.00 26.93  ? 21  TRP   C CG  1 
ATOM   1626 C CD1 . TRP   C 1 22 ? 16.523  -31.201 16.564  1.00 25.46  ? 21  TRP   C CD1 1 
ATOM   1627 C CD2 . TRP   C 1 22 ? 17.117  -32.683 14.956  1.00 27.40  ? 21  TRP   C CD2 1 
ATOM   1628 N NE1 . TRP   C 1 22 ? 15.386  -31.660 15.953  1.00 27.37  ? 21  TRP   C NE1 1 
ATOM   1629 C CE2 . TRP   C 1 22 ? 15.711  -32.567 14.972  1.00 25.72  ? 21  TRP   C CE2 1 
ATOM   1630 C CE3 . TRP   C 1 22 ? 17.707  -33.565 14.038  1.00 24.98  ? 21  TRP   C CE3 1 
ATOM   1631 C CZ2 . TRP   C 1 22 ? 14.911  -33.298 14.080  1.00 24.95  ? 21  TRP   C CZ2 1 
ATOM   1632 C CZ3 . TRP   C 1 22 ? 16.913  -34.314 13.182  1.00 25.04  ? 21  TRP   C CZ3 1 
ATOM   1633 C CH2 . TRP   C 1 22 ? 15.522  -34.188 13.226  1.00 25.00  ? 21  TRP   C CH2 1 
ATOM   1634 N N   . PRO   C 1 23 ? 18.163  -28.271 16.321  1.00 25.16  ? 22  PRO   C N   1 
ATOM   1635 C CA  . PRO   C 1 23 ? 17.745  -27.201 17.234  1.00 25.52  ? 22  PRO   C CA  1 
ATOM   1636 C C   . PRO   C 1 23 ? 17.196  -27.784 18.534  1.00 23.75  ? 22  PRO   C C   1 
ATOM   1637 O O   . PRO   C 1 23 ? 16.398  -28.729 18.519  1.00 24.00  ? 22  PRO   C O   1 
ATOM   1638 C CB  . PRO   C 1 23 ? 16.672  -26.456 16.386  1.00 28.77  ? 22  PRO   C CB  1 
ATOM   1639 C CG  . PRO   C 1 23 ? 16.154  -27.480 15.393  1.00 26.40  ? 22  PRO   C CG  1 
ATOM   1640 C CD  . PRO   C 1 23 ? 17.431  -28.275 15.041  1.00 25.11  ? 22  PRO   C CD  1 
ATOM   1641 N N   . ALA   C 1 24 ? 17.664  -27.234 19.654  1.00 25.66  ? 23  ALA   C N   1 
ATOM   1642 C CA  . ALA   C 1 24 ? 17.396  -27.804 20.970  1.00 29.48  ? 23  ALA   C CA  1 
ATOM   1643 C C   . ALA   C 1 24 ? 17.560  -26.739 22.047  1.00 33.15  ? 23  ALA   C C   1 
ATOM   1644 O O   . ALA   C 1 24 ? 18.051  -25.632 21.796  1.00 30.27  ? 23  ALA   C O   1 
ATOM   1645 C CB  . ALA   C 1 24 ? 18.378  -28.957 21.240  1.00 28.31  ? 23  ALA   C CB  1 
ATOM   1646 N N   . ARG   C 1 25 ? 17.171  -27.110 23.279  1.00 32.19  ? 24  ARG   C N   1 
ATOM   1647 C CA  . ARG   C 1 25 ? 17.515  -26.294 24.434  1.00 32.60  ? 24  ARG   C CA  1 
ATOM   1648 C C   . ARG   C 1 25 ? 17.999  -27.199 25.572  1.00 33.12  ? 24  ARG   C C   1 
ATOM   1649 O O   . ARG   C 1 25 ? 17.661  -28.391 25.618  1.00 33.55  ? 24  ARG   C O   1 
ATOM   1650 C CB  . ARG   C 1 25 ? 16.286  -25.547 24.961  1.00 31.77  ? 24  ARG   C CB  1 
ATOM   1651 C CG  . ARG   C 1 25 ? 15.019  -26.364 25.184  1.00 37.71  ? 24  ARG   C CG  1 
ATOM   1652 C CD  . ARG   C 1 25 ? 14.005  -25.492 25.978  1.00 40.85  ? 24  ARG   C CD  1 
ATOM   1653 N NE  . ARG   C 1 25 ? 12.782  -26.256 26.266  1.00 46.78  ? 24  ARG   C NE  1 
ATOM   1654 C CZ  . ARG   C 1 25 ? 11.511  -25.969 26.005  1.00 54.03  ? 24  ARG   C CZ  1 
ATOM   1655 N NH1 . ARG   C 1 25 ? 11.174  -24.849 25.382  1.00 44.43  ? 24  ARG   C NH1 1 
ATOM   1656 N NH2 . ARG   C 1 25 ? 10.567  -26.830 26.370  1.00 53.82  ? 24  ARG   C NH2 1 
ATOM   1657 N N   . ILE   C 1 26 ? 18.691  -26.567 26.512  1.00 36.32  ? 25  ILE   C N   1 
ATOM   1658 C CA  . ILE   C 1 26 ? 19.061  -27.195 27.775  1.00 41.83  ? 25  ILE   C CA  1 
ATOM   1659 C C   . ILE   C 1 26 ? 17.834  -27.224 28.685  1.00 50.68  ? 25  ILE   C C   1 
ATOM   1660 O O   . ILE   C 1 26 ? 17.100  -26.240 28.812  1.00 54.71  ? 25  ILE   C O   1 
ATOM   1661 C CB  . ILE   C 1 26 ? 20.232  -26.453 28.442  1.00 41.38  ? 25  ILE   C CB  1 
ATOM   1662 C CG1 . ILE   C 1 26 ? 21.299  -25.982 27.474  1.00 41.34  ? 25  ILE   C CG1 1 
ATOM   1663 C CG2 . ILE   C 1 26 ? 20.809  -27.246 29.617  1.00 44.95  ? 25  ILE   C CG2 1 
ATOM   1664 C CD1 . ILE   C 1 26 ? 22.395  -26.976 27.135  1.00 42.79  ? 25  ILE   C CD1 1 
ATOM   1665 N N   . ASP   C 1 27 ? 17.619  -28.377 29.317  1.00 46.50  ? 26  ASP   C N   1 
ATOM   1666 C CA  . ASP   C 1 27 ? 16.585  -28.532 30.327  1.00 57.03  ? 26  ASP   C CA  1 
ATOM   1667 C C   . ASP   C 1 27 ? 17.138  -28.303 31.736  1.00 55.72  ? 26  ASP   C C   1 
ATOM   1668 O O   . ASP   C 1 27 ? 18.374  -28.323 31.873  1.00 59.35  ? 26  ASP   C O   1 
ATOM   1669 C CB  . ASP   C 1 27 ? 15.920  -29.891 30.238  1.00 59.23  ? 26  ASP   C CB  1 
ATOM   1670 C CG  . ASP   C 1 27 ? 14.630  -29.884 29.445  1.00 67.28  ? 26  ASP   C CG  1 
ATOM   1671 O OD1 . ASP   C 1 27 ? 14.437  -28.888 28.710  1.00 58.47  ? 26  ASP   C OD1 1 
ATOM   1672 O OD2 . ASP   C 1 27 ? 13.819  -30.831 29.630  1.00 60.34  ? 26  ASP   C OD2 1 
ATOM   1673 N N   . LYS   C 1 35 ? 19.524  -38.406 37.758  1.00 65.60  ? 34  LYS   C N   1 
ATOM   1674 C CA  . LYS   C 1 35 ? 20.723  -37.543 37.577  1.00 59.56  ? 34  LYS   C CA  1 
ATOM   1675 C C   . LYS   C 1 35 ? 21.370  -37.895 36.238  1.00 54.84  ? 34  LYS   C C   1 
ATOM   1676 O O   . LYS   C 1 35 ? 21.415  -39.068 35.867  1.00 59.88  ? 34  LYS   C O   1 
ATOM   1677 C CB  . LYS   C 1 35 ? 21.661  -37.688 38.784  1.00 58.76  ? 34  LYS   C CB  1 
ATOM   1678 N N   . PRO   C 1 36 ? 21.889  -36.902 35.472  1.00 50.18  ? 35  PRO   C N   1 
ATOM   1679 C CA  . PRO   C 1 36 ? 22.550  -37.186 34.195  1.00 53.69  ? 35  PRO   C CA  1 
ATOM   1680 C C   . PRO   C 1 36 ? 23.726  -38.134 34.436  1.00 58.11  ? 35  PRO   C C   1 
ATOM   1681 O O   . PRO   C 1 36 ? 24.255  -38.216 35.548  1.00 53.44  ? 35  PRO   C O   1 
ATOM   1682 C CB  . PRO   C 1 36 ? 23.043  -35.795 33.724  1.00 56.11  ? 35  PRO   C CB  1 
ATOM   1683 C CG  . PRO   C 1 36 ? 22.225  -34.788 34.508  1.00 55.36  ? 35  PRO   C CG  1 
ATOM   1684 C CD  . PRO   C 1 36 ? 21.910  -35.472 35.826  1.00 52.69  ? 35  PRO   C CD  1 
ATOM   1685 N N   . PRO   C 1 37 ? 24.204  -38.878 33.415  1.00 53.42  ? 36  PRO   C N   1 
ATOM   1686 C CA  . PRO   C 1 37 ? 25.559  -39.424 33.484  1.00 50.10  ? 36  PRO   C CA  1 
ATOM   1687 C C   . PRO   C 1 37 ? 26.502  -38.262 33.797  1.00 48.10  ? 36  PRO   C C   1 
ATOM   1688 O O   . PRO   C 1 37 ? 26.168  -37.100 33.540  1.00 39.10  ? 36  PRO   C O   1 
ATOM   1689 C CB  . PRO   C 1 37 ? 25.751  -40.000 32.068  1.00 46.48  ? 36  PRO   C CB  1 
ATOM   1690 C CG  . PRO   C 1 37 ? 24.352  -40.414 31.687  1.00 50.19  ? 36  PRO   C CG  1 
ATOM   1691 C CD  . PRO   C 1 37 ? 23.478  -39.273 32.195  1.00 51.92  ? 36  PRO   C CD  1 
ATOM   1692 N N   . PRO   C 1 38 ? 27.683  -38.536 34.402  1.00 41.10  ? 37  PRO   C N   1 
ATOM   1693 C CA  . PRO   C 1 38 ? 28.659  -37.494 34.713  1.00 42.23  ? 37  PRO   C CA  1 
ATOM   1694 C C   . PRO   C 1 38 ? 28.961  -36.612 33.513  1.00 39.18  ? 37  PRO   C C   1 
ATOM   1695 O O   . PRO   C 1 38 ? 29.228  -37.127 32.425  1.00 35.01  ? 37  PRO   C O   1 
ATOM   1696 C CB  . PRO   C 1 38 ? 29.901  -38.350 35.102  1.00 46.92  ? 37  PRO   C CB  1 
ATOM   1697 C CG  . PRO   C 1 38 ? 29.308  -39.591 35.700  1.00 43.44  ? 37  PRO   C CG  1 
ATOM   1698 C CD  . PRO   C 1 38 ? 28.133  -39.880 34.803  1.00 44.99  ? 37  PRO   C CD  1 
ATOM   1699 N N   . ASN   C 1 39 ? 28.870  -35.291 33.738  1.00 36.29  ? 38  ASN   C N   1 
ATOM   1700 C CA  . ASN   C 1 39 ? 29.254  -34.253 32.801  1.00 37.99  ? 38  ASN   C CA  1 
ATOM   1701 C C   . ASN   C 1 39 ? 28.320  -34.241 31.584  1.00 37.84  ? 38  ASN   C C   1 
ATOM   1702 O O   . ASN   C 1 39 ? 28.763  -33.876 30.492  1.00 42.37  ? 38  ASN   C O   1 
ATOM   1703 C CB  . ASN   C 1 39 ? 30.728  -34.334 32.416  1.00 44.41  ? 38  ASN   C CB  1 
ATOM   1704 C CG  . ASN   C 1 39 ? 31.250  -33.038 31.829  1.00 56.34  ? 38  ASN   C CG  1 
ATOM   1705 O OD1 . ASN   C 1 39 ? 30.770  -31.946 32.158  1.00 61.17  ? 38  ASN   C OD1 1 
ATOM   1706 N ND2 . ASN   C 1 39 ? 32.257  -33.132 30.975  1.00 58.53  ? 38  ASN   C ND2 1 
ATOM   1707 N N   . LYS   C 1 40 ? 27.058  -34.665 31.770  1.00 35.46  ? 39  LYS   C N   1 
ATOM   1708 C CA  . LYS   C 1 40 ? 26.061  -34.610 30.701  1.00 35.40  ? 39  LYS   C CA  1 
ATOM   1709 C C   . LYS   C 1 40 ? 24.938  -33.625 31.018  1.00 33.04  ? 39  LYS   C C   1 
ATOM   1710 O O   . LYS   C 1 40 ? 24.490  -33.479 32.151  1.00 36.94  ? 39  LYS   C O   1 
ATOM   1711 C CB  . LYS   C 1 40 ? 25.351  -35.939 30.412  1.00 34.12  ? 39  LYS   C CB  1 
ATOM   1712 C CG  . LYS   C 1 40 ? 26.307  -37.050 29.974  1.00 37.36  ? 39  LYS   C CG  1 
ATOM   1713 C CD  . LYS   C 1 40 ? 27.184  -36.766 28.769  1.00 42.06  ? 39  LYS   C CD  1 
ATOM   1714 C CE  . LYS   C 1 40 ? 27.987  -37.999 28.420  1.00 43.30  ? 39  LYS   C CE  1 
ATOM   1715 N NZ  . LYS   C 1 40 ? 29.003  -37.683 27.408  1.00 50.81  ? 39  LYS   C NZ  1 
ATOM   1716 N N   . TYR   C 1 41 ? 24.434  -32.972 29.970  1.00 32.03  ? 40  TYR   C N   1 
ATOM   1717 C CA  . TYR   C 1 41 ? 23.299  -32.061 30.112  1.00 30.81  ? 40  TYR   C CA  1 
ATOM   1718 C C   . TYR   C 1 41 ? 22.020  -32.718 29.585  1.00 34.87  ? 40  TYR   C C   1 
ATOM   1719 O O   . TYR   C 1 41 ? 22.052  -33.458 28.595  1.00 33.99  ? 40  TYR   C O   1 
ATOM   1720 C CB  . TYR   C 1 41 ? 23.528  -30.848 29.202  1.00 30.99  ? 40  TYR   C CB  1 
ATOM   1721 C CG  . TYR   C 1 41 ? 24.663  -29.933 29.630  1.00 34.79  ? 40  TYR   C CG  1 
ATOM   1722 C CD1 . TYR   C 1 41 ? 25.974  -30.150 29.209  1.00 38.35  ? 40  TYR   C CD1 1 
ATOM   1723 C CD2 . TYR   C 1 41 ? 24.409  -28.842 30.461  1.00 38.22  ? 40  TYR   C CD2 1 
ATOM   1724 C CE1 . TYR   C 1 41 ? 27.008  -29.315 29.602  1.00 44.11  ? 40  TYR   C CE1 1 
ATOM   1725 C CE2 . TYR   C 1 41 ? 25.432  -27.987 30.829  1.00 38.50  ? 40  TYR   C CE2 1 
ATOM   1726 C CZ  . TYR   C 1 41 ? 26.730  -28.231 30.419  1.00 46.46  ? 40  TYR   C CZ  1 
ATOM   1727 O OH  . TYR   C 1 41 ? 27.725  -27.372 30.784  1.00 54.86  ? 40  TYR   C OH  1 
ATOM   1728 N N   . PRO   C 1 42 ? 20.852  -32.432 30.215  1.00 34.08  ? 41  PRO   C N   1 
ATOM   1729 C CA  . PRO   C 1 42 ? 19.554  -32.866 29.701  1.00 31.31  ? 41  PRO   C CA  1 
ATOM   1730 C C   . PRO   C 1 42 ? 19.190  -31.914 28.566  1.00 32.87  ? 41  PRO   C C   1 
ATOM   1731 O O   . PRO   C 1 42 ? 19.217  -30.698 28.760  1.00 35.42  ? 41  PRO   C O   1 
ATOM   1732 C CB  . PRO   C 1 42 ? 18.616  -32.714 30.929  1.00 32.22  ? 41  PRO   C CB  1 
ATOM   1733 C CG  . PRO   C 1 42 ? 19.245  -31.619 31.727  1.00 37.33  ? 41  PRO   C CG  1 
ATOM   1734 C CD  . PRO   C 1 42 ? 20.748  -31.684 31.487  1.00 35.90  ? 41  PRO   C CD  1 
ATOM   1735 N N   . ILE   C 1 43 ? 18.954  -32.495 27.386  1.00 32.39  ? 42  ILE   C N   1 
ATOM   1736 C CA  . ILE   C 1 43 ? 18.636  -31.702 26.200  1.00 31.86  ? 42  ILE   C CA  1 
ATOM   1737 C C   . ILE   C 1 43 ? 17.196  -31.974 25.782  1.00 32.66  ? 42  ILE   C C   1 
ATOM   1738 O O   . ILE   C 1 43 ? 16.745  -33.124 25.759  1.00 32.94  ? 42  ILE   C O   1 
ATOM   1739 C CB  . ILE   C 1 43 ? 19.636  -32.018 25.068  1.00 27.12  ? 42  ILE   C CB  1 
ATOM   1740 C CG1 . ILE   C 1 43 ? 21.098  -31.740 25.503  1.00 29.61  ? 42  ILE   C CG1 1 
ATOM   1741 C CG2 . ILE   C 1 43 ? 19.225  -31.301 23.762  1.00 25.34  ? 42  ILE   C CG2 1 
ATOM   1742 C CD1 . ILE   C 1 43 ? 21.360  -30.340 26.026  1.00 30.91  ? 42  ILE   C CD1 1 
ATOM   1743 N N   . PHE   C 1 44 ? 16.462  -30.900 25.394  1.00 28.66  ? 43  PHE   C N   1 
ATOM   1744 C CA  . PHE   C 1 44 ? 15.169  -31.058 24.757  1.00 32.37  ? 43  PHE   C CA  1 
ATOM   1745 C C   . PHE   C 1 44 ? 15.327  -30.662 23.288  1.00 27.71  ? 43  PHE   C C   1 
ATOM   1746 O O   . PHE   C 1 44 ? 15.821  -29.565 23.019  1.00 30.56  ? 43  PHE   C O   1 
ATOM   1747 C CB  . PHE   C 1 44 ? 14.217  -30.036 25.393  1.00 32.86  ? 43  PHE   C CB  1 
ATOM   1748 C CG  . PHE   C 1 44 ? 12.828  -30.015 24.778  1.00 38.40  ? 43  PHE   C CG  1 
ATOM   1749 C CD1 . PHE   C 1 44 ? 11.908  -31.029 25.045  1.00 36.65  ? 43  PHE   C CD1 1 
ATOM   1750 C CD2 . PHE   C 1 44 ? 12.458  -28.987 23.903  1.00 39.94  ? 43  PHE   C CD2 1 
ATOM   1751 C CE1 . PHE   C 1 44 ? 10.639  -31.007 24.476  1.00 43.24  ? 43  PHE   C CE1 1 
ATOM   1752 C CE2 . PHE   C 1 44 ? 11.190  -28.976 23.327  1.00 36.85  ? 43  PHE   C CE2 1 
ATOM   1753 C CZ  . PHE   C 1 44 ? 10.290  -29.982 23.609  1.00 41.44  ? 43  PHE   C CZ  1 
ATOM   1754 N N   . PHE   C 1 45 ? 14.906  -31.550 22.393  1.00 26.12  ? 44  PHE   C N   1 
ATOM   1755 C CA  . PHE   C 1 45 ? 15.002  -31.332 20.958  1.00 28.38  ? 44  PHE   C CA  1 
ATOM   1756 C C   . PHE   C 1 45 ? 13.721  -30.673 20.446  1.00 29.70  ? 44  PHE   C C   1 
ATOM   1757 O O   . PHE   C 1 45 ? 12.627  -31.260 20.545  1.00 29.24  ? 44  PHE   C O   1 
ATOM   1758 C CB  . PHE   C 1 45 ? 15.279  -32.625 20.190  1.00 28.29  ? 44  PHE   C CB  1 
ATOM   1759 C CG  . PHE   C 1 45 ? 16.669  -33.154 20.482  1.00 28.06  ? 44  PHE   C CG  1 
ATOM   1760 C CD1 . PHE   C 1 45 ? 17.748  -32.866 19.644  1.00 30.09  ? 44  PHE   C CD1 1 
ATOM   1761 C CD2 . PHE   C 1 45 ? 16.904  -33.911 21.635  1.00 29.96  ? 44  PHE   C CD2 1 
ATOM   1762 C CE1 . PHE   C 1 45 ? 19.037  -33.359 19.917  1.00 30.15  ? 44  PHE   C CE1 1 
ATOM   1763 C CE2 . PHE   C 1 45 ? 18.185  -34.394 21.903  1.00 32.70  ? 44  PHE   C CE2 1 
ATOM   1764 C CZ  . PHE   C 1 45 ? 19.244  -34.115 21.069  1.00 31.66  ? 44  PHE   C CZ  1 
ATOM   1765 N N   . PHE   C 1 46 ? 13.888  -29.533 19.738  1.00 27.91  ? 45  PHE   C N   1 
ATOM   1766 C CA  . PHE   C 1 46 ? 12.734  -28.932 19.076  1.00 27.54  ? 45  PHE   C CA  1 
ATOM   1767 C C   . PHE   C 1 46 ? 12.228  -29.796 17.914  1.00 29.62  ? 45  PHE   C C   1 
ATOM   1768 O O   . PHE   C 1 46 ? 12.986  -30.549 17.305  1.00 28.94  ? 45  PHE   C O   1 
ATOM   1769 C CB  . PHE   C 1 46 ? 13.050  -27.481 18.680  1.00 26.61  ? 45  PHE   C CB  1 
ATOM   1770 C CG  . PHE   C 1 46 ? 13.288  -26.507 19.822  1.00 27.31  ? 45  PHE   C CG  1 
ATOM   1771 C CD1 . PHE   C 1 46 ? 12.212  -26.071 20.598  1.00 30.24  ? 45  PHE   C CD1 1 
ATOM   1772 C CD2 . PHE   C 1 46 ? 14.563  -26.016 20.111  1.00 26.90  ? 45  PHE   C CD2 1 
ATOM   1773 C CE1 . PHE   C 1 46 ? 12.449  -25.191 21.650  1.00 29.45  ? 45  PHE   C CE1 1 
ATOM   1774 C CE2 . PHE   C 1 46 ? 14.790  -25.096 21.140  1.00 31.23  ? 45  PHE   C CE2 1 
ATOM   1775 C CZ  . PHE   C 1 46 ? 13.725  -24.699 21.918  1.00 30.00  ? 45  PHE   C CZ  1 
ATOM   1776 N N   . GLY   C 1 47 ? 10.919  -29.689 17.612  1.00 27.50  ? 46  GLY   C N   1 
ATOM   1777 C CA  . GLY   C 1 47 ? 10.325  -30.409 16.492  1.00 30.30  ? 46  GLY   C CA  1 
ATOM   1778 C C   . GLY   C 1 47 ? 9.905   -31.834 16.857  1.00 38.53  ? 46  GLY   C C   1 
ATOM   1779 O O   . GLY   C 1 47 ? 8.710   -32.175 16.800  1.00 36.66  ? 46  GLY   C O   1 
ATOM   1780 N N   . THR   C 1 48 ? 10.893  -32.671 17.223  1.00 33.02  ? 47  THR   C N   1 
ATOM   1781 C CA  . THR   C 1 48 ? 10.597  -34.021 17.701  1.00 33.22  ? 47  THR   C CA  1 
ATOM   1782 C C   . THR   C 1 48 ? 10.116  -33.976 19.153  1.00 34.74  ? 47  THR   C C   1 
ATOM   1783 O O   . THR   C 1 48 ? 9.393   -34.885 19.573  1.00 35.61  ? 47  THR   C O   1 
ATOM   1784 C CB  . THR   C 1 48 ? 11.827  -34.926 17.556  1.00 29.02  ? 47  THR   C CB  1 
ATOM   1785 O OG1 . THR   C 1 48 ? 12.709  -34.354 18.524  1.00 31.49  ? 47  THR   C OG1 1 
ATOM   1786 C CG2 . THR   C 1 48 ? 12.371  -34.973 16.142  1.00 32.70  ? 47  THR   C CG2 1 
ATOM   1787 N N   . HIS   C 1 49 ? 10.514  -32.947 19.923  1.00 31.71  ? 48  HIS   C N   1 
ATOM   1788 C CA  . HIS   C 1 49 ? 10.220  -32.846 21.355  1.00 33.60  ? 48  HIS   C CA  1 
ATOM   1789 C C   . HIS   C 1 49 ? 10.726  -34.072 22.137  1.00 34.80  ? 48  HIS   C C   1 
ATOM   1790 O O   . HIS   C 1 49 ? 10.116  -34.465 23.136  1.00 38.73  ? 48  HIS   C O   1 
ATOM   1791 C CB  . HIS   C 1 49 ? 8.723   -32.588 21.598  1.00 40.61  ? 48  HIS   C CB  1 
ATOM   1792 C CG  . HIS   C 1 49 ? 8.165   -31.520 20.707  1.00 38.22  ? 48  HIS   C CG  1 
ATOM   1793 N ND1 . HIS   C 1 49 ? 7.062   -31.750 19.914  1.00 46.95  ? 48  HIS   C ND1 1 
ATOM   1794 C CD2 . HIS   C 1 49 ? 8.598   -30.281 20.403  1.00 40.78  ? 48  HIS   C CD2 1 
ATOM   1795 C CE1 . HIS   C 1 49 ? 6.812   -30.658 19.194  1.00 45.62  ? 48  HIS   C CE1 1 
ATOM   1796 N NE2 . HIS   C 1 49 ? 7.721   -29.750 19.489  1.00 45.35  ? 48  HIS   C NE2 1 
ATOM   1797 N N   . GLU   C 1 50 ? 11.843  -34.660 21.703  1.00 35.64  ? 49  GLU   C N   1 
ATOM   1798 C CA  . GLU   C 1 50 ? 12.479  -35.753 22.438  1.00 34.47  ? 49  GLU   C CA  1 
ATOM   1799 C C   . GLU   C 1 50 ? 13.546  -35.213 23.380  1.00 37.37  ? 49  GLU   C C   1 
ATOM   1800 O O   . GLU   C 1 50 ? 13.911  -34.039 23.331  1.00 35.28  ? 49  GLU   C O   1 
ATOM   1801 C CB  . GLU   C 1 50 ? 13.013  -36.788 21.456  1.00 38.69  ? 49  GLU   C CB  1 
ATOM   1802 C CG  . GLU   C 1 50 ? 11.867  -37.395 20.657  1.00 45.31  ? 49  GLU   C CG  1 
ATOM   1803 C CD  . GLU   C 1 50 ? 12.284  -38.327 19.549  1.00 52.50  ? 49  GLU   C CD  1 
ATOM   1804 O OE1 . GLU   C 1 50 ? 13.455  -38.322 19.118  1.00 55.70  ? 49  GLU   C OE1 1 
ATOM   1805 O OE2 . GLU   C 1 50 ? 11.387  -39.073 19.120  1.00 64.86  ? 49  GLU   C OE2 1 
ATOM   1806 N N   . THR   C 1 51 ? 14.043  -36.085 24.275  1.00 32.65  ? 50  THR   C N   1 
ATOM   1807 C CA  . THR   C 1 51 ? 15.071  -35.647 25.206  1.00 34.34  ? 50  THR   C CA  1 
ATOM   1808 C C   . THR   C 1 51 ? 16.238  -36.638 25.157  1.00 30.54  ? 50  THR   C C   1 
ATOM   1809 O O   . THR   C 1 51 ? 16.102  -37.782 24.720  1.00 36.55  ? 50  THR   C O   1 
ATOM   1810 C CB  . THR   C 1 51 ? 14.529  -35.439 26.630  1.00 40.24  ? 50  THR   C CB  1 
ATOM   1811 O OG1 . THR   C 1 51 ? 13.936  -36.674 27.032  1.00 43.75  ? 50  THR   C OG1 1 
ATOM   1812 C CG2 . THR   C 1 51 ? 13.553  -34.283 26.777  1.00 38.86  ? 50  THR   C CG2 1 
ATOM   1813 N N   . ALA   C 1 52 ? 17.414  -36.142 25.508  1.00 33.07  ? 51  ALA   C N   1 
ATOM   1814 C CA  . ALA   C 1 52 ? 18.582  -37.001 25.653  1.00 31.17  ? 51  ALA   C CA  1 
ATOM   1815 C C   . ALA   C 1 52 ? 19.579  -36.290 26.551  1.00 34.98  ? 51  ALA   C C   1 
ATOM   1816 O O   . ALA   C 1 52 ? 19.439  -35.107 26.840  1.00 38.32  ? 51  ALA   C O   1 
ATOM   1817 C CB  . ALA   C 1 52 ? 19.174  -37.332 24.290  1.00 29.73  ? 51  ALA   C CB  1 
ATOM   1818 N N   . PHE   C 1 53 ? 20.600  -37.028 27.012  1.00 36.10  ? 52  PHE   C N   1 
ATOM   1819 C CA  . PHE   C 1 53 ? 21.705  -36.411 27.731  1.00 33.95  ? 52  PHE   C CA  1 
ATOM   1820 C C   . PHE   C 1 53 ? 22.880  -36.314 26.781  1.00 33.55  ? 52  PHE   C C   1 
ATOM   1821 O O   . PHE   C 1 53 ? 23.256  -37.299 26.135  1.00 34.54  ? 52  PHE   C O   1 
ATOM   1822 C CB  . PHE   C 1 53 ? 22.122  -37.373 28.853  1.00 34.85  ? 52  PHE   C CB  1 
ATOM   1823 C CG  . PHE   C 1 53 ? 21.172  -37.337 30.033  1.00 36.36  ? 52  PHE   C CG  1 
ATOM   1824 C CD1 . PHE   C 1 53 ? 20.924  -36.149 30.722  1.00 38.40  ? 52  PHE   C CD1 1 
ATOM   1825 C CD2 . PHE   C 1 53 ? 20.511  -38.495 30.441  1.00 48.92  ? 52  PHE   C CD2 1 
ATOM   1826 C CE1 . PHE   C 1 53 ? 20.047  -36.114 31.805  1.00 39.19  ? 52  PHE   C CE1 1 
ATOM   1827 C CE2 . PHE   C 1 53 ? 19.641  -38.459 31.529  1.00 49.63  ? 52  PHE   C CE2 1 
ATOM   1828 C CZ  . PHE   C 1 53 ? 19.399  -37.272 32.197  1.00 40.04  ? 52  PHE   C CZ  1 
ATOM   1829 N N   . LEU   C 1 54 ? 23.527  -35.144 26.757  1.00 29.40  ? 53  LEU   C N   1 
ATOM   1830 C CA  . LEU   C 1 54 ? 24.674  -34.967 25.884  1.00 30.19  ? 53  LEU   C CA  1 
ATOM   1831 C C   . LEU   C 1 54 ? 25.753  -34.196 26.634  1.00 32.25  ? 53  LEU   C C   1 
ATOM   1832 O O   . LEU   C 1 54 ? 25.439  -33.401 27.507  1.00 32.82  ? 53  LEU   C O   1 
ATOM   1833 C CB  . LEU   C 1 54 ? 24.279  -34.206 24.612  1.00 29.95  ? 53  LEU   C CB  1 
ATOM   1834 C CG  . LEU   C 1 54 ? 23.478  -34.973 23.556  1.00 32.13  ? 53  LEU   C CG  1 
ATOM   1835 C CD1 . LEU   C 1 54 ? 23.056  -34.037 22.440  1.00 29.03  ? 53  LEU   C CD1 1 
ATOM   1836 C CD2 . LEU   C 1 54 ? 24.264  -36.133 22.959  1.00 42.02  ? 53  LEU   C CD2 1 
ATOM   1837 N N   . GLY   C 1 55 ? 27.008  -34.410 26.231  1.00 33.44  ? 54  GLY   C N   1 
ATOM   1838 C CA  . GLY   C 1 55 ? 28.132  -33.653 26.762  1.00 33.19  ? 54  GLY   C CA  1 
ATOM   1839 C C   . GLY   C 1 55 ? 28.337  -32.329 26.036  1.00 38.36  ? 54  GLY   C C   1 
ATOM   1840 O O   . GLY   C 1 55 ? 27.874  -32.108 24.896  1.00 32.50  ? 54  GLY   C O   1 
ATOM   1841 N N   . PRO   C 1 56 ? 29.084  -31.401 26.679  1.00 38.34  ? 55  PRO   C N   1 
ATOM   1842 C CA  . PRO   C 1 56 ? 29.208  -30.038 26.166  1.00 41.11  ? 55  PRO   C CA  1 
ATOM   1843 C C   . PRO   C 1 56 ? 29.861  -29.978 24.780  1.00 36.20  ? 55  PRO   C C   1 
ATOM   1844 O O   . PRO   C 1 56 ? 29.616  -29.051 24.017  1.00 45.29  ? 55  PRO   C O   1 
ATOM   1845 C CB  . PRO   C 1 56 ? 29.995  -29.315 27.297  1.00 41.27  ? 55  PRO   C CB  1 
ATOM   1846 C CG  . PRO   C 1 56 ? 30.799  -30.424 27.941  1.00 39.26  ? 55  PRO   C CG  1 
ATOM   1847 C CD  . PRO   C 1 56 ? 29.875  -31.636 27.911  1.00 40.17  ? 55  PRO   C CD  1 
ATOM   1848 N N   . LYS   C 1 57 ? 30.628  -31.013 24.438  1.00 34.38  ? 56  LYS   C N   1 
ATOM   1849 C CA  . LYS   C 1 57 ? 31.305  -31.143 23.163  1.00 39.63  ? 56  LYS   C CA  1 
ATOM   1850 C C   . LYS   C 1 57 ? 30.268  -31.177 22.042  1.00 42.65  ? 56  LYS   C C   1 
ATOM   1851 O O   . LYS   C 1 57 ? 30.585  -30.857 20.903  1.00 39.31  ? 56  LYS   C O   1 
ATOM   1852 C CB  . LYS   C 1 57 ? 32.054  -32.479 23.045  1.00 42.00  ? 56  LYS   C CB  1 
ATOM   1853 N N   . ASP   C 1 58 ? 29.051  -31.617 22.382  1.00 36.91  ? 57  ASP   C N   1 
ATOM   1854 C CA  . ASP   C 1 58 ? 28.044  -31.956 21.388  1.00 36.71  ? 57  ASP   C CA  1 
ATOM   1855 C C   . ASP   C 1 58 ? 27.063  -30.806 21.231  1.00 37.49  ? 57  ASP   C C   1 
ATOM   1856 O O   . ASP   C 1 58 ? 26.069  -30.961 20.528  1.00 34.37  ? 57  ASP   C O   1 
ATOM   1857 C CB  . ASP   C 1 58 ? 27.286  -33.212 21.779  1.00 41.80  ? 57  ASP   C CB  1 
ATOM   1858 C CG  . ASP   C 1 58 ? 28.141  -34.466 21.849  1.00 44.01  ? 57  ASP   C CG  1 
ATOM   1859 O OD1 . ASP   C 1 58 ? 29.153  -34.507 21.136  1.00 50.09  ? 57  ASP   C OD1 1 
ATOM   1860 O OD2 . ASP   C 1 58 ? 27.789  -35.363 22.637  1.00 49.44  ? 57  ASP   C OD2 1 
ATOM   1861 N N   . LEU   C 1 59 ? 27.383  -29.653 21.845  1.00 30.01  ? 58  LEU   C N   1 
ATOM   1862 C CA  . LEU   C 1 59 ? 26.432  -28.565 22.003  1.00 34.84  ? 58  LEU   C CA  1 
ATOM   1863 C C   . LEU   C 1 59 ? 27.057  -27.279 21.477  1.00 38.29  ? 58  LEU   C C   1 
ATOM   1864 O O   . LEU   C 1 59 ? 28.242  -27.044 21.744  1.00 39.63  ? 58  LEU   C O   1 
ATOM   1865 C CB  . LEU   C 1 59 ? 26.115  -28.402 23.486  1.00 34.81  ? 58  LEU   C CB  1 
ATOM   1866 C CG  . LEU   C 1 59 ? 25.557  -29.641 24.185  1.00 32.33  ? 58  LEU   C CG  1 
ATOM   1867 C CD1 . LEU   C 1 59 ? 25.330  -29.236 25.638  1.00 32.33  ? 58  LEU   C CD1 1 
ATOM   1868 C CD2 . LEU   C 1 59 ? 24.246  -30.089 23.522  1.00 27.59  ? 58  LEU   C CD2 1 
ATOM   1869 N N   . PHE   C 1 60 ? 26.238  -26.458 20.791  1.00 40.41  ? 59  PHE   C N   1 
ATOM   1870 C CA  . PHE   C 1 60 ? 26.660  -25.208 20.152  1.00 35.65  ? 59  PHE   C CA  1 
ATOM   1871 C C   . PHE   C 1 60 ? 25.649  -24.096 20.432  1.00 37.68  ? 59  PHE   C C   1 
ATOM   1872 O O   . PHE   C 1 60 ? 24.476  -24.257 20.150  1.00 34.62  ? 59  PHE   C O   1 
ATOM   1873 C CB  . PHE   C 1 60 ? 26.809  -25.488 18.654  1.00 33.28  ? 59  PHE   C CB  1 
ATOM   1874 C CG  . PHE   C 1 60 ? 27.741  -26.652 18.333  1.00 33.76  ? 59  PHE   C CG  1 
ATOM   1875 C CD1 . PHE   C 1 60 ? 27.299  -27.974 18.346  1.00 30.89  ? 59  PHE   C CD1 1 
ATOM   1876 C CD2 . PHE   C 1 60 ? 29.089  -26.419 18.039  1.00 40.72  ? 59  PHE   C CD2 1 
ATOM   1877 C CE1 . PHE   C 1 60 ? 28.163  -29.029 18.090  1.00 33.09  ? 59  PHE   C CE1 1 
ATOM   1878 C CE2 . PHE   C 1 60 ? 29.944  -27.480 17.756  1.00 35.94  ? 59  PHE   C CE2 1 
ATOM   1879 C CZ  . PHE   C 1 60 ? 29.477  -28.779 17.784  1.00 36.93  ? 59  PHE   C CZ  1 
ATOM   1880 N N   . PRO   C 1 61 ? 26.027  -22.914 21.003  1.00 36.88  ? 60  PRO   C N   1 
ATOM   1881 C CA  . PRO   C 1 61 ? 25.034  -21.866 21.289  1.00 35.70  ? 60  PRO   C CA  1 
ATOM   1882 C C   . PRO   C 1 61 ? 24.306  -21.474 20.004  1.00 32.78  ? 60  PRO   C C   1 
ATOM   1883 O O   . PRO   C 1 61 ? 24.956  -21.338 18.963  1.00 40.70  ? 60  PRO   C O   1 
ATOM   1884 C CB  . PRO   C 1 61 ? 25.853  -20.681 21.870  1.00 38.72  ? 60  PRO   C CB  1 
ATOM   1885 C CG  . PRO   C 1 61 ? 27.185  -21.288 22.250  1.00 37.68  ? 60  PRO   C CG  1 
ATOM   1886 C CD  . PRO   C 1 61 ? 27.397  -22.541 21.398  1.00 43.59  ? 60  PRO   C CD  1 
ATOM   1887 N N   . TYR   C 1 62 ? 22.974  -21.327 20.114  1.00 35.80  ? 61  TYR   C N   1 
ATOM   1888 C CA  . TYR   C 1 62 ? 22.085  -21.071 18.990  1.00 35.58  ? 61  TYR   C CA  1 
ATOM   1889 C C   . TYR   C 1 62 ? 22.557  -19.841 18.205  1.00 45.62  ? 61  TYR   C C   1 
ATOM   1890 O O   . TYR   C 1 62 ? 22.694  -19.906 16.987  1.00 43.55  ? 61  TYR   C O   1 
ATOM   1891 C CB  . TYR   C 1 62 ? 20.620  -20.973 19.424  1.00 40.86  ? 61  TYR   C CB  1 
ATOM   1892 C CG  . TYR   C 1 62 ? 19.664  -20.576 18.310  1.00 39.57  ? 61  TYR   C CG  1 
ATOM   1893 C CD1 . TYR   C 1 62 ? 19.443  -21.422 17.223  1.00 40.73  ? 61  TYR   C CD1 1 
ATOM   1894 C CD2 . TYR   C 1 62 ? 18.958  -19.373 18.367  1.00 41.57  ? 61  TYR   C CD2 1 
ATOM   1895 C CE1 . TYR   C 1 62 ? 18.576  -21.062 16.201  1.00 39.91  ? 61  TYR   C CE1 1 
ATOM   1896 C CE2 . TYR   C 1 62 ? 18.081  -19.009 17.359  1.00 45.37  ? 61  TYR   C CE2 1 
ATOM   1897 C CZ  . TYR   C 1 62 ? 17.898  -19.853 16.272  1.00 43.37  ? 61  TYR   C CZ  1 
ATOM   1898 O OH  . TYR   C 1 62 ? 17.027  -19.506 15.277  1.00 44.72  ? 61  TYR   C OH  1 
ATOM   1899 N N   . ASP   C 1 63 ? 22.858  -18.743 18.909  1.00 50.22  ? 62  ASP   C N   1 
ATOM   1900 C CA  . ASP   C 1 63 ? 23.166  -17.480 18.245  1.00 56.79  ? 62  ASP   C CA  1 
ATOM   1901 C C   . ASP   C 1 63 ? 24.488  -17.526 17.486  1.00 47.80  ? 62  ASP   C C   1 
ATOM   1902 O O   . ASP   C 1 63 ? 24.543  -17.071 16.344  1.00 56.36  ? 62  ASP   C O   1 
ATOM   1903 C CB  . ASP   C 1 63 ? 23.006  -16.287 19.170  1.00 65.15  ? 62  ASP   C CB  1 
ATOM   1904 C CG  . ASP   C 1 63 ? 21.565  -15.813 19.287  1.00 78.96  ? 62  ASP   C CG  1 
ATOM   1905 O OD1 . ASP   C 1 63 ? 21.003  -15.916 20.397  1.00 76.62  ? 62  ASP   C OD1 1 
ATOM   1906 O OD2 . ASP   C 1 63 ? 21.012  -15.374 18.251  1.00 85.62  ? 62  ASP   C OD2 1 
ATOM   1907 N N   . LYS   C 1 64 ? 25.541  -18.055 18.119  1.00 42.88  ? 63  LYS   C N   1 
ATOM   1908 C CA  . LYS   C 1 64 ? 26.860  -18.184 17.510  1.00 41.02  ? 63  LYS   C CA  1 
ATOM   1909 C C   . LYS   C 1 64 ? 26.836  -19.100 16.286  1.00 39.84  ? 63  LYS   C C   1 
ATOM   1910 O O   . LYS   C 1 64 ? 27.613  -18.888 15.361  1.00 44.25  ? 63  LYS   C O   1 
ATOM   1911 C CB  . LYS   C 1 64 ? 27.928  -18.758 18.453  1.00 39.76  ? 63  LYS   C CB  1 
ATOM   1912 N N   . SER   C 1 65 ? 25.947  -20.113 16.257  1.00 38.20  ? 64  SER   C N   1 
ATOM   1913 C CA  . SER   C 1 65 ? 26.152  -21.177 15.277  1.00 34.00  ? 64  SER   C CA  1 
ATOM   1914 C C   . SER   C 1 65 ? 24.987  -21.317 14.277  1.00 31.35  ? 64  SER   C C   1 
ATOM   1915 O O   . SER   C 1 65 ? 25.049  -22.173 13.390  1.00 33.44  ? 64  SER   C O   1 
ATOM   1916 C CB  . SER   C 1 65 ? 26.471  -22.506 15.952  1.00 44.89  ? 64  SER   C CB  1 
ATOM   1917 O OG  . SER   C 1 65 ? 25.301  -23.045 16.560  1.00 41.09  ? 64  SER   C OG  1 
ATOM   1918 N N   . LYS   C 1 66 ? 23.921  -20.516 14.431  1.00 30.99  ? 65  LYS   C N   1 
ATOM   1919 C CA  . LYS   C 1 66 ? 22.756  -20.676 13.575  1.00 33.01  ? 65  LYS   C CA  1 
ATOM   1920 C C   . LYS   C 1 66 ? 23.070  -20.404 12.104  1.00 33.71  ? 65  LYS   C C   1 
ATOM   1921 O O   . LYS   C 1 66 ? 22.448  -21.010 11.246  1.00 36.11  ? 65  LYS   C O   1 
ATOM   1922 C CB  . LYS   C 1 66 ? 21.550  -19.849 14.019  1.00 36.91  ? 65  LYS   C CB  1 
ATOM   1923 C CG  . LYS   C 1 66 ? 21.838  -18.361 14.053  1.00 36.24  ? 65  LYS   C CG  1 
ATOM   1924 C CD  . LYS   C 1 66 ? 20.572  -17.614 14.450  1.00 45.10  ? 65  LYS   C CD  1 
ATOM   1925 C CE  . LYS   C 1 66 ? 20.781  -16.146 14.529  1.00 44.32  ? 65  LYS   C CE  1 
ATOM   1926 N NZ  . LYS   C 1 66 ? 19.674  -15.665 15.351  1.00 47.16  ? 65  LYS   C NZ  1 
ATOM   1927 N N   . ASP   C 1 67 ? 24.034  -19.521 11.812  1.00 37.74  ? 66  ASP   C N   1 
ATOM   1928 C CA  . ASP   C 1 67 ? 24.422  -19.256 10.426  1.00 38.56  ? 66  ASP   C CA  1 
ATOM   1929 C C   . ASP   C 1 67 ? 24.907  -20.559 9.778   1.00 39.90  ? 66  ASP   C C   1 
ATOM   1930 O O   . ASP   C 1 67 ? 24.649  -20.835 8.600   1.00 39.32  ? 66  ASP   C O   1 
ATOM   1931 C CB  . ASP   C 1 67 ? 25.312  -18.010 10.315  1.00 38.85  ? 66  ASP   C CB  1 
ATOM   1932 C CG  . ASP   C 1 67 ? 26.752  -18.147 10.806  1.00 51.80  ? 66  ASP   C CG  1 
ATOM   1933 O OD1 . ASP   C 1 67 ? 27.102  -19.218 11.352  1.00 54.51  ? 66  ASP   C OD1 1 
ATOM   1934 O OD2 . ASP   C 1 67 ? 27.523  -17.165 10.673  1.00 52.88  ? 66  ASP   C OD2 1 
ATOM   1935 N N   . LYS   C 1 68 ? 25.525  -21.431 10.579  1.00 35.89  ? 67  LYS   C N   1 
ATOM   1936 C CA  . LYS   C 1 68 ? 26.046  -22.693 10.077  1.00 32.30  ? 67  LYS   C CA  1 
ATOM   1937 C C   . LYS   C 1 68 ? 25.032  -23.857 10.095  1.00 36.65  ? 67  LYS   C C   1 
ATOM   1938 O O   . LYS   C 1 68 ? 24.994  -24.646 9.152   1.00 37.79  ? 67  LYS   C O   1 
ATOM   1939 C CB  . LYS   C 1 68 ? 27.315  -23.041 10.860  1.00 36.37  ? 67  LYS   C CB  1 
ATOM   1940 C CG  . LYS   C 1 68 ? 28.041  -24.284 10.394  1.00 41.39  ? 67  LYS   C CG  1 
ATOM   1941 C CD  . LYS   C 1 68 ? 29.402  -24.269 11.097  1.00 51.22  ? 67  LYS   C CD  1 
ATOM   1942 C CE  . LYS   C 1 68 ? 30.016  -25.605 11.368  1.00 58.07  ? 67  LYS   C CE  1 
ATOM   1943 N NZ  . LYS   C 1 68 ? 30.466  -26.310 10.165  1.00 67.44  ? 67  LYS   C NZ  1 
ATOM   1944 N N   . TYR   C 1 69 ? 24.254  -24.021 11.176  1.00 28.94  ? 68  TYR   C N   1 
ATOM   1945 C CA  . TYR   C 1 69 ? 23.444  -25.231 11.317  1.00 29.82  ? 68  TYR   C CA  1 
ATOM   1946 C C   . TYR   C 1 69 ? 21.955  -24.926 11.143  1.00 30.71  ? 68  TYR   C C   1 
ATOM   1947 O O   . TYR   C 1 69 ? 21.136  -25.838 11.025  1.00 29.79  ? 68  TYR   C O   1 
ATOM   1948 C CB  . TYR   C 1 69 ? 23.627  -25.836 12.721  1.00 28.42  ? 68  TYR   C CB  1 
ATOM   1949 C CG  . TYR   C 1 69 ? 25.054  -26.269 13.014  1.00 31.84  ? 68  TYR   C CG  1 
ATOM   1950 C CD1 . TYR   C 1 69 ? 25.765  -27.063 12.124  1.00 34.32  ? 68  TYR   C CD1 1 
ATOM   1951 C CD2 . TYR   C 1 69 ? 25.676  -25.855 14.186  1.00 34.50  ? 68  TYR   C CD2 1 
ATOM   1952 C CE1 . TYR   C 1 69 ? 27.052  -27.488 12.409  1.00 34.50  ? 68  TYR   C CE1 1 
ATOM   1953 C CE2 . TYR   C 1 69 ? 26.959  -26.286 14.484  1.00 34.35  ? 68  TYR   C CE2 1 
ATOM   1954 C CZ  . TYR   C 1 69 ? 27.644  -27.084 13.590  1.00 38.21  ? 68  TYR   C CZ  1 
ATOM   1955 O OH  . TYR   C 1 69 ? 28.936  -27.418 13.924  1.00 42.75  ? 68  TYR   C OH  1 
ATOM   1956 N N   . GLY   C 1 70 ? 21.594  -23.641 11.156  1.00 29.18  ? 69  GLY   C N   1 
ATOM   1957 C CA  . GLY   C 1 70 ? 20.178  -23.307 11.082  1.00 30.98  ? 69  GLY   C CA  1 
ATOM   1958 C C   . GLY   C 1 70 ? 19.758  -23.152 9.622   1.00 33.56  ? 69  GLY   C C   1 
ATOM   1959 O O   . GLY   C 1 70 ? 19.695  -22.049 9.071   1.00 33.90  ? 69  GLY   C O   1 
ATOM   1960 N N   . LYS   C 1 71 ? 19.580  -24.290 8.980   1.00 30.01  ? 70  LYS   C N   1 
ATOM   1961 C CA  . LYS   C 1 71 ? 19.174  -24.301 7.584   1.00 32.27  ? 70  LYS   C CA  1 
ATOM   1962 C C   . LYS   C 1 71 ? 18.329  -25.556 7.447   1.00 31.18  ? 70  LYS   C C   1 
ATOM   1963 O O   . LYS   C 1 71 ? 18.572  -26.538 8.145   1.00 33.40  ? 70  LYS   C O   1 
ATOM   1964 C CB  . LYS   C 1 71 ? 20.381  -24.400 6.646   1.00 36.07  ? 70  LYS   C CB  1 
ATOM   1965 C CG  . LYS   C 1 71 ? 21.421  -25.387 7.146   1.00 40.80  ? 70  LYS   C CG  1 
ATOM   1966 C CD  . LYS   C 1 71 ? 22.528  -25.953 6.262   1.00 51.78  ? 70  LYS   C CD  1 
ATOM   1967 C CE  . LYS   C 1 71 ? 23.442  -26.821 7.093   1.00 46.07  ? 70  LYS   C CE  1 
ATOM   1968 N N   . PRO   C 1 72 ? 17.296  -25.572 6.586   1.00 28.67  ? 71  PRO   C N   1 
ATOM   1969 C CA  . PRO   C 1 72 ? 16.382  -26.711 6.544   1.00 26.37  ? 71  PRO   C CA  1 
ATOM   1970 C C   . PRO   C 1 72 ? 17.059  -28.030 6.187   1.00 30.10  ? 71  PRO   C C   1 
ATOM   1971 O O   . PRO   C 1 72 ? 18.101  -28.077 5.513   1.00 31.77  ? 71  PRO   C O   1 
ATOM   1972 C CB  . PRO   C 1 72 ? 15.434  -26.289 5.442   1.00 29.22  ? 71  PRO   C CB  1 
ATOM   1973 C CG  . PRO   C 1 72 ? 15.424  -24.778 5.573   1.00 28.11  ? 71  PRO   C CG  1 
ATOM   1974 C CD  . PRO   C 1 72 ? 16.890  -24.433 5.750   1.00 29.04  ? 71  PRO   C CD  1 
ATOM   1975 N N   . ASN   C 1 73 ? 16.381  -29.097 6.573   1.00 31.75  ? 72  ASN   C N   1 
ATOM   1976 C CA  . ASN   C 1 73 ? 16.718  -30.375 5.980   1.00 34.82  ? 72  ASN   C CA  1 
ATOM   1977 C C   . ASN   C 1 73 ? 15.490  -31.254 6.125   1.00 31.44  ? 72  ASN   C C   1 
ATOM   1978 O O   . ASN   C 1 73 ? 14.536  -30.875 6.798   1.00 31.82  ? 72  ASN   C O   1 
ATOM   1979 C CB  . ASN   C 1 73 ? 18.052  -30.941 6.446   1.00 42.30  ? 72  ASN   C CB  1 
ATOM   1980 C CG  . ASN   C 1 73 ? 17.951  -31.497 7.841   1.00 39.12  ? 72  ASN   C CG  1 
ATOM   1981 O OD1 . ASN   C 1 73 ? 17.175  -32.428 8.100   1.00 36.53  ? 72  ASN   C OD1 1 
ATOM   1982 N ND2 . ASN   C 1 73 ? 18.743  -30.949 8.737   1.00 41.03  ? 72  ASN   C ND2 1 
ATOM   1983 N N   . LYS   C 1 74 ? 15.519  -32.413 5.466   1.00 33.33  ? 73  LYS   C N   1 
ATOM   1984 C CA  . LYS   C 1 74 ? 14.290  -33.170 5.318   1.00 30.28  ? 73  LYS   C CA  1 
ATOM   1985 C C   . LYS   C 1 74 ? 14.099  -34.166 6.452   1.00 34.11  ? 73  LYS   C C   1 
ATOM   1986 O O   . LYS   C 1 74 ? 13.126  -34.921 6.433   1.00 35.79  ? 73  LYS   C O   1 
ATOM   1987 C CB  . LYS   C 1 74 ? 14.226  -33.815 3.925   1.00 32.87  ? 73  LYS   C CB  1 
ATOM   1988 C CG  . LYS   C 1 74 ? 13.583  -32.865 2.878   1.00 40.25  ? 73  LYS   C CG  1 
ATOM   1989 N N   . ARG   C 1 75 ? 14.975  -34.154 7.470   1.00 29.02  ? 74  ARG   C N   1 
ATOM   1990 C CA  . ARG   C 1 75 ? 14.800  -35.131 8.538   1.00 29.28  ? 74  ARG   C CA  1 
ATOM   1991 C C   . ARG   C 1 75 ? 13.529  -34.811 9.320   1.00 31.24  ? 74  ARG   C C   1 
ATOM   1992 O O   . ARG   C 1 75 ? 13.174  -33.639 9.540   1.00 30.90  ? 74  ARG   C O   1 
ATOM   1993 C CB  . ARG   C 1 75 ? 15.980  -35.248 9.533   1.00 32.13  ? 74  ARG   C CB  1 
ATOM   1994 C CG  . ARG   C 1 75 ? 17.357  -35.439 8.900   1.00 37.79  ? 74  ARG   C CG  1 
ATOM   1995 C CD  . ARG   C 1 75 ? 17.663  -36.796 8.232   1.00 39.29  ? 74  ARG   C CD  1 
ATOM   1996 N NE  . ARG   C 1 75 ? 17.671  -37.797 9.300   1.00 39.50  ? 74  ARG   C NE  1 
ATOM   1997 C CZ  . ARG   C 1 75 ? 18.803  -38.234 9.878   1.00 32.42  ? 74  ARG   C CZ  1 
ATOM   1998 N NH1 . ARG   C 1 75 ? 18.706  -38.869 11.014  1.00 39.35  ? 74  ARG   C NH1 1 
ATOM   1999 N NH2 . ARG   C 1 75 ? 19.978  -37.939 9.340   1.00 33.51  ? 74  ARG   C NH2 1 
ATOM   2000 N N   . LYS   C 1 76 ? 12.865  -35.880 9.777   1.00 32.88  ? 75  LYS   C N   1 
ATOM   2001 C CA  . LYS   C 1 76 ? 11.578  -35.796 10.453  1.00 36.73  ? 75  LYS   C CA  1 
ATOM   2002 C C   . LYS   C 1 76 ? 11.601  -34.824 11.633  1.00 34.74  ? 75  LYS   C C   1 
ATOM   2003 O O   . LYS   C 1 76 ? 12.350  -34.969 12.613  1.00 33.85  ? 75  LYS   C O   1 
ATOM   2004 C CB  . LYS   C 1 76 ? 11.056  -37.176 10.871  1.00 43.48  ? 75  LYS   C CB  1 
ATOM   2005 C CG  . LYS   C 1 76 ? 9.612   -37.131 11.357  1.00 50.49  ? 75  LYS   C CG  1 
ATOM   2006 C CD  . LYS   C 1 76 ? 9.056   -38.486 11.776  1.00 63.23  ? 75  LYS   C CD  1 
ATOM   2007 C CE  . LYS   C 1 76 ? 7.732   -38.343 12.457  1.00 64.75  ? 75  LYS   C CE  1 
ATOM   2008 N NZ  . LYS   C 1 76 ? 7.219   -39.663 12.831  1.00 68.23  ? 75  LYS   C NZ  1 
ATOM   2009 N N   . GLY   C 1 77 ? 10.766  -33.787 11.520  1.00 35.47  ? 76  GLY   C N   1 
ATOM   2010 C CA  . GLY   C 1 77 ? 10.606  -32.901 12.658  1.00 30.98  ? 76  GLY   C CA  1 
ATOM   2011 C C   . GLY   C 1 77 ? 11.573  -31.717 12.612  1.00 26.92  ? 76  GLY   C C   1 
ATOM   2012 O O   . GLY   C 1 77 ? 11.421  -30.786 13.390  1.00 31.00  ? 76  GLY   C O   1 
ATOM   2013 N N   . PHE   C 1 78 ? 12.547  -31.735 11.689  1.00 26.45  ? 77  PHE   C N   1 
ATOM   2014 C CA  . PHE   C 1 78 ? 13.650  -30.796 11.774  1.00 26.46  ? 77  PHE   C CA  1 
ATOM   2015 C C   . PHE   C 1 78 ? 13.122  -29.370 11.522  1.00 29.45  ? 77  PHE   C C   1 
ATOM   2016 O O   . PHE   C 1 78 ? 13.440  -28.417 12.236  1.00 28.20  ? 77  PHE   C O   1 
ATOM   2017 C CB  . PHE   C 1 78 ? 14.744  -31.141 10.754  1.00 28.17  ? 77  PHE   C CB  1 
ATOM   2018 C CG  . PHE   C 1 78 ? 16.029  -30.368 11.025  1.00 28.04  ? 77  PHE   C CG  1 
ATOM   2019 C CD1 . PHE   C 1 78 ? 16.237  -29.120 10.464  1.00 25.62  ? 77  PHE   C CD1 1 
ATOM   2020 C CD2 . PHE   C 1 78 ? 17.030  -30.901 11.831  1.00 28.33  ? 77  PHE   C CD2 1 
ATOM   2021 C CE1 . PHE   C 1 78 ? 17.414  -28.409 10.700  1.00 27.53  ? 77  PHE   C CE1 1 
ATOM   2022 C CE2 . PHE   C 1 78 ? 18.213  -30.189 12.065  1.00 26.12  ? 77  PHE   C CE2 1 
ATOM   2023 C CZ  . PHE   C 1 78 ? 18.396  -28.942 11.518  1.00 26.78  ? 77  PHE   C CZ  1 
ATOM   2024 N N   . ASN   C 1 79 ? 12.368  -29.213 10.438  1.00 27.62  ? 78  ASN   C N   1 
ATOM   2025 C CA  . ASN   C 1 79 ? 12.001  -27.859 10.023  1.00 30.26  ? 78  ASN   C CA  1 
ATOM   2026 C C   . ASN   C 1 79 ? 11.029  -27.241 11.013  1.00 31.11  ? 78  ASN   C C   1 
ATOM   2027 O O   . ASN   C 1 79 ? 11.092  -26.037 11.308  1.00 28.30  ? 78  ASN   C O   1 
ATOM   2028 C CB  . ASN   C 1 79 ? 11.505  -27.823 8.585   1.00 30.05  ? 78  ASN   C CB  1 
ATOM   2029 C CG  . ASN   C 1 79 ? 12.589  -28.267 7.634   1.00 30.36  ? 78  ASN   C CG  1 
ATOM   2030 O OD1 . ASN   C 1 79 ? 13.766  -28.020 7.918   1.00 29.88  ? 78  ASN   C OD1 1 
ATOM   2031 N ND2 . ASN   C 1 79 ? 12.212  -28.840 6.497   1.00 30.65  ? 78  ASN   C ND2 1 
ATOM   2032 N N   . GLU   C 1 80 ? 10.120  -28.059 11.539  1.00 32.46  ? 79  GLU   C N   1 
ATOM   2033 C CA  . GLU   C 1 80 ? 9.270   -27.593 12.625  1.00 30.79  ? 79  GLU   C CA  1 
ATOM   2034 C C   . GLU   C 1 80 ? 10.136  -27.179 13.811  1.00 31.63  ? 79  GLU   C C   1 
ATOM   2035 O O   . GLU   C 1 80 ? 9.866   -26.159 14.443  1.00 28.75  ? 79  GLU   C O   1 
ATOM   2036 C CB  . GLU   C 1 80 ? 8.214   -28.635 13.004  1.00 34.59  ? 79  GLU   C CB  1 
ATOM   2037 C CG  . GLU   C 1 80 ? 7.308   -28.175 14.147  1.00 34.61  ? 79  GLU   C CG  1 
ATOM   2038 C CD  . GLU   C 1 80 ? 6.010   -28.950 14.300  1.00 49.00  ? 79  GLU   C CD  1 
ATOM   2039 O OE1 . GLU   C 1 80 ? 5.868   -30.044 13.715  1.00 48.03  ? 79  GLU   C OE1 1 
ATOM   2040 O OE2 . GLU   C 1 80 ? 5.117   -28.433 15.012  1.00 46.75  ? 79  GLU   C OE2 1 
ATOM   2041 N N   . GLY   C 1 81 ? 11.230  -27.940 14.085  1.00 28.61  ? 80  GLY   C N   1 
ATOM   2042 C CA  . GLY   C 1 81 ? 12.144  -27.539 15.156  1.00 27.76  ? 80  GLY   C CA  1 
ATOM   2043 C C   . GLY   C 1 81 ? 12.781  -26.171 14.912  1.00 27.55  ? 80  GLY   C C   1 
ATOM   2044 O O   . GLY   C 1 81 ? 12.987  -25.393 15.845  1.00 28.28  ? 80  GLY   C O   1 
ATOM   2045 N N   . LEU   C 1 82 ? 13.139  -25.905 13.651  1.00 27.55  ? 81  LEU   C N   1 
ATOM   2046 C CA  . LEU   C 1 82 ? 13.724  -24.610 13.335  1.00 29.98  ? 81  LEU   C CA  1 
ATOM   2047 C C   . LEU   C 1 82 ? 12.696  -23.511 13.594  1.00 26.10  ? 81  LEU   C C   1 
ATOM   2048 O O   . LEU   C 1 82 ? 13.083  -22.396 13.981  1.00 30.04  ? 81  LEU   C O   1 
ATOM   2049 C CB  . LEU   C 1 82 ? 14.188  -24.545 11.880  1.00 28.24  ? 81  LEU   C CB  1 
ATOM   2050 C CG  . LEU   C 1 82 ? 15.417  -25.372 11.506  1.00 27.36  ? 81  LEU   C CG  1 
ATOM   2051 C CD1 . LEU   C 1 82 ? 15.633  -25.194 10.003  1.00 29.98  ? 81  LEU   C CD1 1 
ATOM   2052 C CD2 . LEU   C 1 82 ? 16.657  -24.891 12.244  1.00 26.24  ? 81  LEU   C CD2 1 
ATOM   2053 N N   . TRP   C 1 83 ? 11.427  -23.803 13.320  1.00 28.12  ? 82  TRP   C N   1 
ATOM   2054 C CA  . TRP   C 1 83 ? 10.428  -22.757 13.538  1.00 31.62  ? 82  TRP   C CA  1 
ATOM   2055 C C   . TRP   C 1 83 ? 10.262  -22.486 15.040  1.00 32.87  ? 82  TRP   C C   1 
ATOM   2056 O O   . TRP   C 1 83 ? 10.179  -21.339 15.480  1.00 32.06  ? 82  TRP   C O   1 
ATOM   2057 C CB  . TRP   C 1 83 ? 9.082   -23.106 12.900  1.00 33.61  ? 82  TRP   C CB  1 
ATOM   2058 C CG  . TRP   C 1 83 ? 8.093   -21.970 13.047  1.00 36.39  ? 82  TRP   C CG  1 
ATOM   2059 C CD1 . TRP   C 1 83 ? 7.875   -20.945 12.168  1.00 35.01  ? 82  TRP   C CD1 1 
ATOM   2060 C CD2 . TRP   C 1 83 ? 7.210   -21.737 14.171  1.00 33.79  ? 82  TRP   C CD2 1 
ATOM   2061 N NE1 . TRP   C 1 83 ? 6.922   -20.094 12.665  1.00 36.56  ? 82  TRP   C NE1 1 
ATOM   2062 C CE2 . TRP   C 1 83 ? 6.497   -20.543 13.886  1.00 36.40  ? 82  TRP   C CE2 1 
ATOM   2063 C CE3 . TRP   C 1 83 ? 6.975   -22.398 15.388  1.00 35.12  ? 82  TRP   C CE3 1 
ATOM   2064 C CZ2 . TRP   C 1 83 ? 5.548   -20.025 14.762  1.00 42.38  ? 82  TRP   C CZ2 1 
ATOM   2065 C CZ3 . TRP   C 1 83 ? 6.037   -21.883 16.254  1.00 41.29  ? 82  TRP   C CZ3 1 
ATOM   2066 C CH2 . TRP   C 1 83 ? 5.336   -20.714 15.939  1.00 45.38  ? 82  TRP   C CH2 1 
ATOM   2067 N N   . GLU   C 1 84 ? 10.290  -23.559 15.841  1.00 32.33  ? 83  GLU   C N   1 
ATOM   2068 C CA  . GLU   C 1 84 ? 10.125  -23.396 17.283  1.00 32.11  ? 83  GLU   C CA  1 
ATOM   2069 C C   . GLU   C 1 84 ? 11.278  -22.632 17.923  1.00 31.98  ? 83  GLU   C C   1 
ATOM   2070 O O   . GLU   C 1 84 ? 11.034  -21.776 18.786  1.00 33.17  ? 83  GLU   C O   1 
ATOM   2071 C CB  . GLU   C 1 84 ? 10.056  -24.745 17.995  1.00 29.73  ? 83  GLU   C CB  1 
ATOM   2072 C CG  . GLU   C 1 84 ? 8.784   -25.487 17.620  1.00 31.13  ? 83  GLU   C CG  1 
ATOM   2073 C CD  . GLU   C 1 84 ? 8.707   -26.912 18.099  1.00 38.01  ? 83  GLU   C CD  1 
ATOM   2074 O OE1 . GLU   C 1 84 ? 9.711   -27.337 18.713  1.00 34.96  ? 83  GLU   C OE1 1 
ATOM   2075 O OE2 . GLU   C 1 84 ? 7.658   -27.575 17.856  1.00 39.29  ? 83  GLU   C OE2 1 
ATOM   2076 N N   . ILE   C 1 85 ? 12.527  -22.932 17.520  1.00 30.65  ? 84  ILE   C N   1 
ATOM   2077 C CA  . ILE   C 1 85 ? 13.692  -22.325 18.149  1.00 30.21  ? 84  ILE   C CA  1 
ATOM   2078 C C   . ILE   C 1 85 ? 13.731  -20.804 17.932  1.00 34.22  ? 84  ILE   C C   1 
ATOM   2079 O O   . ILE   C 1 85 ? 14.234  -20.071 18.778  1.00 32.81  ? 84  ILE   C O   1 
ATOM   2080 C CB  . ILE   C 1 85 ? 15.016  -23.022 17.788  1.00 31.30  ? 84  ILE   C CB  1 
ATOM   2081 C CG1 . ILE   C 1 85 ? 16.119  -22.598 18.753  1.00 31.54  ? 84  ILE   C CG1 1 
ATOM   2082 C CG2 . ILE   C 1 85 ? 15.419  -22.793 16.329  1.00 30.42  ? 84  ILE   C CG2 1 
ATOM   2083 C CD1 . ILE   C 1 85 ? 17.336  -23.507 18.803  1.00 31.03  ? 84  ILE   C CD1 1 
ATOM   2084 N N   . GLN   C 1 86 ? 13.277  -20.368 16.755  1.00 30.12  ? 85  GLN   C N   1 
ATOM   2085 C CA  . GLN   C 1 86 ? 13.245  -18.964 16.362  1.00 32.90  ? 85  GLN   C CA  1 
ATOM   2086 C C   . GLN   C 1 86 ? 12.020  -18.240 16.917  1.00 32.44  ? 85  GLN   C C   1 
ATOM   2087 O O   . GLN   C 1 86 ? 12.141  -17.056 17.263  1.00 38.93  ? 85  GLN   C O   1 
ATOM   2088 C CB  . GLN   C 1 86 ? 13.202  -18.837 14.832  1.00 33.22  ? 85  GLN   C CB  1 
ATOM   2089 C CG  . GLN   C 1 86 ? 13.605  -17.447 14.315  1.00 34.19  ? 85  GLN   C CG  1 
ATOM   2090 C CD  . GLN   C 1 86 ? 14.047  -17.465 12.857  1.00 36.33  ? 85  GLN   C CD  1 
ATOM   2091 O OE1 . GLN   C 1 86 ? 13.863  -18.452 12.131  1.00 35.97  ? 85  GLN   C OE1 1 
ATOM   2092 N NE2 . GLN   C 1 86 ? 14.696  -16.392 12.421  1.00 37.70  ? 85  GLN   C NE2 1 
ATOM   2093 N N   . ASN   C 1 87 ? 10.876  -18.927 16.981  1.00 33.48  ? 86  ASN   C N   1 
ATOM   2094 C CA  . ASN   C 1 87 ? 9.569   -18.290 17.126  1.00 39.42  ? 86  ASN   C CA  1 
ATOM   2095 C C   . ASN   C 1 87 ? 8.845   -18.626 18.432  1.00 42.24  ? 86  ASN   C C   1 
ATOM   2096 O O   . ASN   C 1 87 ? 7.961   -17.868 18.805  1.00 40.81  ? 86  ASN   C O   1 
ATOM   2097 C CB  . ASN   C 1 87 ? 8.637   -18.549 15.949  1.00 35.90  ? 86  ASN   C CB  1 
ATOM   2098 C CG  . ASN   C 1 87 ? 9.224   -17.915 14.711  1.00 38.13  ? 86  ASN   C CG  1 
ATOM   2099 O OD1 . ASN   C 1 87 ? 9.360   -16.685 14.661  1.00 36.79  ? 86  ASN   C OD1 1 
ATOM   2100 N ND2 . ASN   C 1 87 ? 9.705   -18.726 13.779  1.00 35.79  ? 86  ASN   C ND2 1 
ATOM   2101 N N   . ASN   C 1 88 ? 9.180   -19.736 19.114  1.00 43.54  ? 87  ASN   C N   1 
ATOM   2102 C CA  . ASN   C 1 88 ? 8.458   -20.134 20.331  1.00 38.60  ? 87  ASN   C CA  1 
ATOM   2103 C C   . ASN   C 1 88 ? 9.332   -21.061 21.170  1.00 43.31  ? 87  ASN   C C   1 
ATOM   2104 O O   . ASN   C 1 88 ? 8.932   -22.198 21.468  1.00 44.76  ? 87  ASN   C O   1 
ATOM   2105 C CB  . ASN   C 1 88 ? 7.215   -20.971 20.017  1.00 40.79  ? 87  ASN   C CB  1 
ATOM   2106 C CG  . ASN   C 1 88 ? 6.140   -20.927 21.087  1.00 46.98  ? 87  ASN   C CG  1 
ATOM   2107 O OD1 . ASN   C 1 88 ? 6.233   -20.153 22.042  1.00 48.08  ? 87  ASN   C OD1 1 
ATOM   2108 N ND2 . ASN   C 1 88 ? 5.092   -21.730 20.932  1.00 45.66  ? 87  ASN   C ND2 1 
ATOM   2109 N N   . PRO   C 1 89 ? 10.546  -20.619 21.561  1.00 38.49  ? 88  PRO   C N   1 
ATOM   2110 C CA  . PRO   C 1 89 ? 11.538  -21.523 22.140  1.00 40.22  ? 88  PRO   C CA  1 
ATOM   2111 C C   . PRO   C 1 89 ? 11.294  -21.976 23.575  1.00 45.79  ? 88  PRO   C C   1 
ATOM   2112 O O   . PRO   C 1 89 ? 12.053  -22.811 24.078  1.00 42.46  ? 88  PRO   C O   1 
ATOM   2113 C CB  . PRO   C 1 89 ? 12.857  -20.747 22.011  1.00 34.08  ? 88  PRO   C CB  1 
ATOM   2114 C CG  . PRO   C 1 89 ? 12.454  -19.298 21.958  1.00 41.02  ? 88  PRO   C CG  1 
ATOM   2115 C CD  . PRO   C 1 89 ? 11.049  -19.246 21.414  1.00 39.76  ? 88  PRO   C CD  1 
ATOM   2116 N N   . HIS   C 1 90 ? 10.257  -21.409 24.219  1.00 43.40  ? 89  HIS   C N   1 
ATOM   2117 C CA  . HIS   C 1 90 ? 10.010  -21.689 25.629  1.00 41.68  ? 89  HIS   C CA  1 
ATOM   2118 C C   . HIS   C 1 90 ? 8.588   -22.176 25.889  1.00 44.38  ? 89  HIS   C C   1 
ATOM   2119 O O   . HIS   C 1 90 ? 8.217   -22.331 27.050  1.00 48.55  ? 89  HIS   C O   1 
ATOM   2120 C CB  . HIS   C 1 90 ? 10.416  -20.513 26.520  1.00 42.82  ? 89  HIS   C CB  1 
ATOM   2121 C CG  . HIS   C 1 90 ? 11.833  -20.082 26.325  1.00 45.65  ? 89  HIS   C CG  1 
ATOM   2122 N ND1 . HIS   C 1 90 ? 12.924  -20.905 26.514  1.00 45.71  ? 89  HIS   C ND1 1 
ATOM   2123 C CD2 . HIS   C 1 90 ? 12.334  -18.886 25.995  1.00 46.02  ? 89  HIS   C CD2 1 
ATOM   2124 C CE1 . HIS   C 1 90 ? 14.043  -20.216 26.303  1.00 45.02  ? 89  HIS   C CE1 1 
ATOM   2125 N NE2 . HIS   C 1 90 ? 13.706  -18.992 25.946  1.00 41.59  ? 89  HIS   C NE2 1 
ATOM   2126 N N   . ALA   C 1 91 ? 7.815   -22.474 24.834  1.00 48.44  ? 90  ALA   C N   1 
ATOM   2127 C CA  . ALA   C 1 91 ? 6.567   -23.212 25.013  1.00 58.72  ? 90  ALA   C CA  1 
ATOM   2128 C C   . ALA   C 1 91 ? 6.855   -24.571 25.662  1.00 65.13  ? 90  ALA   C C   1 
ATOM   2129 O O   . ALA   C 1 91 ? 8.014   -24.962 25.787  1.00 68.73  ? 90  ALA   C O   1 
ATOM   2130 C CB  . ALA   C 1 91 ? 5.809   -23.337 23.700  1.00 55.38  ? 90  ALA   C CB  1 
ATOM   2131 N N   . SER   C 1 92 ? 5.797   -25.288 26.066  1.00 72.38  ? 91  SER   C N   1 
ATOM   2132 C CA  . SER   C 1 92 ? 5.912   -26.441 26.951  1.00 69.89  ? 91  SER   C CA  1 
ATOM   2133 C C   . SER   C 1 92 ? 6.102   -27.748 26.180  1.00 73.58  ? 91  SER   C C   1 
ATOM   2134 O O   . SER   C 1 92 ? 6.795   -28.646 26.656  1.00 73.27  ? 91  SER   C O   1 
ATOM   2135 C CB  . SER   C 1 92 ? 4.726   -26.530 27.885  1.00 71.40  ? 91  SER   C CB  1 
ATOM   2136 O OG  . SER   C 1 92 ? 4.722   -25.437 28.794  1.00 74.58  ? 91  SER   C OG  1 
ATOM   2137 N N   . TYR   C 1 93 ? 5.429   -27.858 25.025  1.00 76.74  ? 92  TYR   C N   1 
ATOM   2138 C CA  . TYR   C 1 93 ? 5.514   -29.002 24.125  1.00 74.68  ? 92  TYR   C CA  1 
ATOM   2139 C C   . TYR   C 1 93 ? 5.382   -30.318 24.919  1.00 81.80  ? 92  TYR   C C   1 
ATOM   2140 O O   . TYR   C 1 93 ? 4.239   -30.759 25.210  1.00 86.99  ? 92  TYR   C O   1 
ATOM   2141 C CB  . TYR   C 1 93 ? 6.793   -28.936 23.279  1.00 72.70  ? 92  TYR   C CB  1 
ATOM   2142 C CG  . TYR   C 1 93 ? 6.982   -27.675 22.437  1.00 63.83  ? 92  TYR   C CG  1 
ATOM   2143 C CD1 . TYR   C 1 93 ? 6.251   -27.475 21.267  1.00 58.85  ? 92  TYR   C CD1 1 
ATOM   2144 C CD2 . TYR   C 1 93 ? 7.901   -26.694 22.799  1.00 60.42  ? 92  TYR   C CD2 1 
ATOM   2145 C CE1 . TYR   C 1 93 ? 6.416   -26.337 20.493  1.00 53.01  ? 92  TYR   C CE1 1 
ATOM   2146 C CE2 . TYR   C 1 93 ? 8.082   -25.556 22.026  1.00 53.81  ? 92  TYR   C CE2 1 
ATOM   2147 C CZ  . TYR   C 1 93 ? 7.333   -25.373 20.876  1.00 53.87  ? 92  TYR   C CZ  1 
ATOM   2148 O OH  . TYR   C 1 93 ? 7.491   -24.242 20.117  1.00 49.21  ? 92  TYR   C OH  1 
HETATM 2149 S S   . SO4   D 2 .  ? 0.696   -33.512 1.755   1.00 99.25  ? 101 SO4   A S   1 
HETATM 2150 O O1  . SO4   D 2 .  ? 1.444   -34.361 0.862   1.00 77.60  ? 101 SO4   A O1  1 
HETATM 2151 O O2  . SO4   D 2 .  ? 0.567   -32.194 1.184   1.00 102.36 ? 101 SO4   A O2  1 
HETATM 2152 O O3  . SO4   D 2 .  ? -0.614  -34.072 1.964   1.00 112.52 ? 101 SO4   A O3  1 
HETATM 2153 O O4  . SO4   D 2 .  ? 1.376   -33.418 3.015   1.00 90.70  ? 101 SO4   A O4  1 
HETATM 2154 S S   . SO4   E 2 .  ? -9.893  -24.681 1.340   1.00 92.03  ? 102 SO4   A S   1 
HETATM 2155 O O1  . SO4   E 2 .  ? -9.876  -24.499 -0.088  1.00 90.91  ? 102 SO4   A O1  1 
HETATM 2156 O O2  . SO4   E 2 .  ? -10.101 -23.412 1.989   1.00 87.51  ? 102 SO4   A O2  1 
HETATM 2157 O O3  . SO4   E 2 .  ? -10.958 -25.590 1.688   1.00 99.56  ? 102 SO4   A O3  1 
HETATM 2158 O O4  . SO4   E 2 .  ? -8.641  -25.233 1.779   1.00 89.18  ? 102 SO4   A O4  1 
HETATM 2159 C C1  . EDO   F 3 .  ? 13.493  -19.556 -7.460  1.00 36.40  ? 103 EDO   A C1  1 
HETATM 2160 O O1  . EDO   F 3 .  ? 14.707  -18.812 -7.213  1.00 29.89  ? 103 EDO   A O1  1 
HETATM 2161 C C2  . EDO   F 3 .  ? 12.631  -19.008 -8.561  1.00 32.60  ? 103 EDO   A C2  1 
HETATM 2162 O O2  . EDO   F 3 .  ? 12.124  -17.730 -8.267  1.00 30.59  ? 103 EDO   A O2  1 
HETATM 2163 S S   . SO4   G 2 .  ? 8.563   -29.401 5.794   1.00 57.37  ? 104 SO4   A S   1 
HETATM 2164 O O1  . SO4   G 2 .  ? 9.287   -28.517 4.950   1.00 52.49  ? 104 SO4   A O1  1 
HETATM 2165 O O2  . SO4   G 2 .  ? 8.181   -30.593 5.046   1.00 65.24  ? 104 SO4   A O2  1 
HETATM 2166 O O3  . SO4   G 2 .  ? 9.400   -29.778 6.915   1.00 60.98  ? 104 SO4   A O3  1 
HETATM 2167 O O4  . SO4   G 2 .  ? 7.359   -28.753 6.257   1.00 63.27  ? 104 SO4   A O4  1 
HETATM 2168 S S   . SO4   H 2 .  ? 7.253   -8.589  -24.690 1.00 70.06  ? 101 SO4   B S   1 
HETATM 2169 O O1  . SO4   H 2 .  ? 8.370   -8.638  -25.614 1.00 39.27  ? 101 SO4   B O1  1 
HETATM 2170 O O2  . SO4   H 2 .  ? 6.083   -9.107  -25.333 1.00 49.97  ? 101 SO4   B O2  1 
HETATM 2171 O O3  . SO4   H 2 .  ? 7.460   -9.399  -23.488 1.00 42.55  ? 101 SO4   B O3  1 
HETATM 2172 O O4  . SO4   H 2 .  ? 7.092   -7.180  -24.338 1.00 57.20  ? 101 SO4   B O4  1 
HETATM 2173 S S   . SO4   I 2 .  ? 14.135  -27.063 -26.422 1.00 52.87  ? 102 SO4   B S   1 
HETATM 2174 O O1  . SO4   I 2 .  ? 15.515  -26.825 -26.111 1.00 42.04  ? 102 SO4   B O1  1 
HETATM 2175 O O2  . SO4   I 2 .  ? 14.009  -28.376 -27.003 1.00 59.40  ? 102 SO4   B O2  1 
HETATM 2176 O O3  . SO4   I 2 .  ? 13.370  -26.980 -25.200 1.00 58.68  ? 102 SO4   B O3  1 
HETATM 2177 O O4  . SO4   I 2 .  ? 13.632  -26.078 -27.360 1.00 50.46  ? 102 SO4   B O4  1 
HETATM 2178 N N1  . A1A31 J 4 .  ? 21.153  -15.949 -22.756 0.84 49.00  ? 103 A1A31 B N1  1 
HETATM 2179 C C4  . A1A31 J 4 .  ? 21.331  -15.106 -23.833 0.84 46.52  ? 103 A1A31 B C4  1 
HETATM 2180 C C5  . A1A31 J 4 .  ? 19.957  -16.481 -22.921 0.84 43.81  ? 103 A1A31 B C5  1 
HETATM 2181 C C6  . A1A31 J 4 .  ? 19.323  -17.473 -22.016 0.84 45.91  ? 103 A1A31 B C6  1 
HETATM 2182 O O   . A1A31 J 4 .  ? 17.745  -13.817 -24.377 0.84 35.98  ? 103 A1A31 B O   1 
HETATM 2183 C C1  . A1A31 J 4 .  ? 17.343  -15.001 -25.083 0.84 44.04  ? 103 A1A31 B C1  1 
HETATM 2184 C C   . A1A31 J 4 .  ? 15.848  -15.107 -25.034 0.84 40.28  ? 103 A1A31 B C   1 
HETATM 2185 C C2  . A1A31 J 4 .  ? 17.991  -16.255 -24.522 0.84 38.77  ? 103 A1A31 B C2  1 
HETATM 2186 N N   . A1A31 J 4 .  ? 19.355  -16.003 -24.058 0.84 44.99  ? 103 A1A31 B N   1 
HETATM 2187 C C3  . A1A31 J 4 .  ? 20.246  -15.132 -24.644 0.84 46.14  ? 103 A1A31 B C3  1 
HETATM 2188 S S   . SO4   K 2 .  ? 28.767  -38.504 12.248  1.00 83.85  ? 101 SO4   C S   1 
HETATM 2189 O O1  . SO4   K 2 .  ? 29.855  -37.680 11.780  1.00 90.68  ? 101 SO4   C O1  1 
HETATM 2190 O O2  . SO4   K 2 .  ? 27.548  -38.131 11.580  1.00 71.70  ? 101 SO4   C O2  1 
HETATM 2191 O O3  . SO4   K 2 .  ? 29.056  -39.878 11.957  1.00 75.60  ? 101 SO4   C O3  1 
HETATM 2192 O O4  . SO4   K 2 .  ? 28.615  -38.330 13.671  1.00 91.15  ? 101 SO4   C O4  1 
HETATM 2193 N N1  . A1A31 L 4 .  ? 16.328  -39.505 20.958  0.68 40.71  ? 102 A1A31 C N1  1 
HETATM 2194 C C4  . A1A31 L 4 .  ? 16.525  -38.310 21.617  0.68 43.20  ? 102 A1A31 C C4  1 
HETATM 2195 C C5  . A1A31 L 4 .  ? 16.473  -39.224 19.673  0.68 42.89  ? 102 A1A31 C C5  1 
HETATM 2196 C C6  . A1A31 L 4 .  ? 16.340  -40.197 18.559  0.68 45.59  ? 102 A1A31 C C6  1 
HETATM 2197 O O   . A1A31 L 4 .  ? 14.922  -36.014 18.529  0.68 30.81  ? 102 A1A31 C O   1 
HETATM 2198 C C1  . A1A31 L 4 .  ? 16.266  -35.892 18.070  0.68 38.82  ? 102 A1A31 C C1  1 
HETATM 2199 C C   . A1A31 L 4 .  ? 16.230  -35.469 16.636  0.68 35.07  ? 102 A1A31 C C   1 
HETATM 2200 C C2  . A1A31 L 4 .  ? 17.023  -37.205 18.215  0.68 36.33  ? 102 A1A31 C C2  1 
HETATM 2201 N N   . A1A31 L 4 .  ? 16.765  -37.897 19.485  0.68 39.60  ? 102 A1A31 C N   1 
HETATM 2202 C C3  . A1A31 L 4 .  ? 16.789  -37.313 20.734  0.68 37.65  ? 102 A1A31 C C3  1 
HETATM 2203 O O   . HOH   M 5 .  ? 8.471   -32.125 3.775   1.00 53.79  ? 201 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? 7.788   -9.071  8.833   1.00 55.35  ? 202 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? 5.289   -29.007 6.853   1.00 49.21  ? 203 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? 10.637  -9.165  -12.866 1.00 54.17  ? 204 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 3.260   -34.297 4.073   1.00 52.08  ? 205 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? 3.600   -10.462 13.740  1.00 52.98  ? 206 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 10.581  -29.698 3.237   1.00 41.19  ? 207 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 0.998   -24.526 13.882  1.00 69.94  ? 208 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? -2.717  3.226   -2.037  1.00 40.62  ? 209 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? -5.952  -13.841 -16.574 1.00 59.75  ? 210 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? -0.107  -33.909 4.988   1.00 57.83  ? 211 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? -3.432  -30.818 -2.967  1.00 62.35  ? 212 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? -8.066  -17.181 6.609   1.00 40.90  ? 213 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? -4.257  -10.939 6.748   1.00 43.47  ? 214 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 8.629   -18.215 -10.986 1.00 29.30  ? 215 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 0.398   -10.624 -15.672 1.00 51.29  ? 216 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 16.869  -18.253 -9.583  1.00 48.03  ? 217 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 12.414  -9.660  -7.225  1.00 47.21  ? 218 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? 15.368  -24.430 2.065   1.00 42.86  ? 219 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 19.311  -15.608 7.286   1.00 29.18  ? 220 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 6.669   -10.610 -12.181 1.00 37.99  ? 221 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 10.658  -23.695 9.885   1.00 35.85  ? 222 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 4.486   -1.450  -6.293  1.00 34.32  ? 223 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 4.020   -3.523  -3.250  1.00 32.46  ? 224 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 8.046   -17.825 -15.874 1.00 47.18  ? 225 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? -6.508  -11.390 -11.256 1.00 40.42  ? 226 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 4.089   -7.836  1.102   1.00 34.66  ? 227 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 1.067   -18.216 -18.792 1.00 51.74  ? 228 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 12.550  -11.773 8.048   1.00 61.62  ? 229 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 2.072   -25.168 -10.175 1.00 34.40  ? 230 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? -1.247  -29.186 9.958   1.00 54.41  ? 231 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 12.642  -28.298 -4.345  1.00 59.30  ? 232 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 16.764  -12.912 1.332   1.00 21.25  ? 233 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 1.457   -4.659  -10.145 1.00 31.51  ? 234 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 15.345  -12.241 -5.341  1.00 31.88  ? 235 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 9.283   -6.106  -1.697  1.00 34.61  ? 236 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? -4.890  -21.224 6.125   1.00 38.43  ? 237 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 10.397  -5.178  -7.838  1.00 32.97  ? 238 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? -0.190  -23.165 9.311   1.00 44.27  ? 239 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 2.487   -10.253 -13.357 1.00 52.53  ? 240 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? -8.389  -15.691 -0.959  1.00 35.15  ? 241 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 13.839  -29.383 4.067   1.00 46.72  ? 242 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 9.544   -13.212 9.668   1.00 43.57  ? 243 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 11.249  -16.598 -14.733 1.00 41.21  ? 244 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 13.614  -15.597 -9.251  1.00 35.19  ? 245 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -6.165  -15.758 -8.136  1.00 29.23  ? 246 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? -1.288  -20.946 6.997   1.00 33.83  ? 247 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? -1.753  -11.631 11.303  1.00 39.15  ? 248 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? -8.459  -16.678 1.998   1.00 41.94  ? 249 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 10.981  -11.884 5.831   1.00 34.90  ? 250 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 2.718   -29.557 -0.454  1.00 38.81  ? 251 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? -2.266  -21.974 -0.593  1.00 27.85  ? 252 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? -1.813  -7.466  11.401  1.00 42.15  ? 253 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 7.102   -1.831  -0.654  1.00 75.28  ? 254 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 12.779  -12.013 -4.245  1.00 21.68  ? 255 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 7.942   -17.776 8.755   1.00 52.26  ? 256 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? -6.203  -19.583 -5.721  1.00 35.58  ? 257 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -4.866  -25.715 -5.519  1.00 45.35  ? 258 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 1.647   -24.817 -6.446  1.00 45.64  ? 259 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 14.930  -28.134 -0.551  1.00 57.32  ? 260 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? 6.053   -16.118 -14.971 1.00 42.58  ? 261 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 7.537   -7.865  1.241   1.00 28.83  ? 262 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? -9.043  -21.060 -1.272  1.00 41.90  ? 263 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 11.080  -12.439 -6.115  1.00 26.44  ? 264 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? -2.935  -11.536 13.901  1.00 51.13  ? 265 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 8.436   -16.375 -13.103 1.00 34.57  ? 266 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 1.381   -10.409 11.721  1.00 34.78  ? 267 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 13.920  -13.036 10.403  1.00 50.71  ? 268 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? -7.852  -21.446 -5.807  1.00 49.27  ? 269 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 2.040   -6.231  5.408   1.00 33.88  ? 270 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? -6.517  -12.717 6.687   1.00 35.45  ? 271 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? 10.866  -6.021  -3.832  1.00 44.71  ? 272 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 4.699   -7.547  3.963   1.00 33.59  ? 273 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -3.656  -5.100  9.989   1.00 78.59  ? 274 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 12.286  -13.397 -8.468  1.00 37.58  ? 275 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 7.706   -8.253  4.400   1.00 39.82  ? 276 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 16.581  -12.581 -16.682 1.00 42.90  ? 277 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? -6.210  -17.437 -9.985  1.00 43.71  ? 278 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? -0.900  -20.795 10.798  1.00 87.54  ? 279 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? 5.925   -5.856  0.495   1.00 44.46  ? 280 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 20.909  -16.638 -3.562  1.00 27.26  ? 281 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? -4.114  -26.957 6.970   1.00 59.19  ? 282 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -6.418  -26.506 3.534   1.00 43.84  ? 283 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 12.774  -15.209 -12.122 1.00 46.38  ? 284 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 10.615  -7.844  0.358   1.00 25.17  ? 285 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -7.734  -11.517 -8.008  1.00 29.70  ? 286 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? -8.421  -19.519 -3.419  1.00 44.40  ? 287 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 9.406   -20.430 -18.374 1.00 43.71  ? 288 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -0.570  -9.005  13.681  1.00 54.54  ? 289 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -7.132  -20.162 6.817   1.00 70.42  ? 290 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -4.167  -7.972  10.523  1.00 47.17  ? 291 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 7.726   -8.377  13.208  1.00 55.74  ? 292 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 21.807  -16.563 -0.536  1.00 39.37  ? 293 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -3.979  -11.072 9.835   1.00 46.32  ? 294 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 8.497   -9.217  -13.714 1.00 37.39  ? 295 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -6.323  -23.251 -6.945  1.00 51.04  ? 296 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? -11.668 -16.477 -3.548  1.00 61.90  ? 297 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? -7.634  -14.154 -9.360  1.00 44.32  ? 298 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? -0.897  -3.218  -11.029 1.00 51.01  ? 299 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 8.370   -27.836 -8.346  1.00 62.85  ? 300 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? -10.496 -28.467 -1.860  1.00 58.23  ? 301 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 10.561  -1.813  -1.273  1.00 57.99  ? 302 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 4.671   -7.114  -11.108 1.00 46.09  ? 303 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? 4.446   -9.741  -11.349 1.00 46.23  ? 304 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -11.705 -13.302 -2.733  1.00 47.82  ? 305 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? -6.661  -23.141 5.568   1.00 48.89  ? 306 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? 7.589   -30.716 -2.030  1.00 55.26  ? 307 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? 12.386  -18.660 -15.118 1.00 42.35  ? 308 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? 8.574   -22.418 -19.190 1.00 67.34  ? 309 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? 5.675   -3.385  1.311   1.00 47.36  ? 310 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? -5.604  -20.975 -7.868  1.00 58.81  ? 311 HOH   A O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 31.144  -8.537  -30.056 1.00 56.07  ? 201 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 27.618  -8.223  -28.715 1.00 48.49  ? 202 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 9.997   -11.273 -38.075 1.00 54.29  ? 203 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 10.174  -19.758 -43.174 1.00 49.40  ? 204 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 34.742  -23.222 -30.225 1.00 56.60  ? 205 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 10.555  -16.739 -44.340 1.00 50.97  ? 206 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 25.889  -4.855  -33.406 1.00 49.99  ? 207 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 25.847  -0.573  -28.988 1.00 51.93  ? 208 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 6.475   -12.093 -26.080 1.00 36.84  ? 209 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 25.427  -6.176  -35.658 1.00 45.65  ? 210 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 30.158  -19.666 -40.123 1.00 43.08  ? 211 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 27.914  -4.565  -36.857 1.00 66.76  ? 212 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 32.317  -18.497 -41.900 1.00 60.30  ? 213 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 20.037  -22.104 -23.069 1.00 49.35  ? 214 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 6.171   -7.425  -32.403 1.00 45.81  ? 215 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 17.128  -9.621  -43.797 1.00 47.35  ? 216 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 1.658   -16.694 -32.633 1.00 48.51  ? 217 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 14.855  -17.429 -18.986 1.00 36.52  ? 218 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 13.335  -4.685  -41.524 1.00 69.20  ? 219 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 24.952  -5.167  -29.702 1.00 37.78  ? 220 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 20.355  -3.164  -23.030 1.00 58.91  ? 221 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 24.416  -1.903  -36.168 1.00 56.15  ? 222 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 30.516  -12.529 -45.793 1.00 77.22  ? 223 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 18.205  -0.581  -38.236 1.00 27.55  ? 224 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 8.150   -27.825 -38.462 1.00 56.40  ? 225 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 13.077  -22.399 -20.672 1.00 50.20  ? 226 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 16.660  -19.338 -28.738 1.00 25.36  ? 227 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 22.461  -23.375 -28.732 1.00 43.21  ? 228 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 26.086  -23.189 -31.001 1.00 34.61  ? 229 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 10.381  -18.987 -32.971 1.00 27.53  ? 230 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 27.460  -17.994 -24.809 1.00 45.21  ? 231 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 8.370   -8.733  -16.497 1.00 44.89  ? 232 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 20.977  -13.412 -42.590 1.00 36.18  ? 233 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 19.629  -25.667 -34.121 1.00 41.60  ? 234 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 19.060  -19.732 -19.383 1.00 53.87  ? 235 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 22.089  -28.857 -32.738 1.00 58.51  ? 236 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 23.771  -4.237  -36.633 1.00 31.24  ? 237 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 14.459  -6.327  -41.099 1.00 43.06  ? 238 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 7.141   -19.025 -34.936 1.00 48.10  ? 239 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 16.775  -25.961 -34.311 1.00 46.31  ? 240 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 1.624   -12.876 -28.261 1.00 49.11  ? 241 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 2.895   -8.621  -27.231 1.00 53.74  ? 242 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 17.908  -15.662 -45.616 1.00 37.60  ? 243 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 4.644   -19.128 -25.721 1.00 58.98  ? 244 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 23.478  -2.510  -28.926 1.00 36.79  ? 245 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 27.120  -10.578 -28.758 1.00 56.11  ? 246 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 21.115  3.615   -32.673 1.00 35.07  ? 247 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 20.556  -10.051 -42.794 1.00 36.49  ? 248 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 20.626  -25.189 -29.399 1.00 65.50  ? 249 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 7.574   -18.441 -31.776 1.00 52.36  ? 250 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 17.236  -19.781 -42.166 1.00 55.38  ? 251 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 21.229  -6.602  -42.400 1.00 37.44  ? 252 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 17.938  4.689   -34.448 1.00 39.62  ? 253 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 17.931  -3.565  -22.044 1.00 52.36  ? 254 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 18.136  -26.026 -28.856 1.00 39.03  ? 255 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 7.590   -12.773 -38.972 1.00 56.03  ? 256 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 7.328   -8.163  -20.754 1.00 43.79  ? 257 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 14.577  -24.421 -40.502 1.00 43.16  ? 258 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 10.423  -21.781 -32.727 1.00 33.40  ? 259 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 31.158  -12.096 -38.164 1.00 57.50  ? 260 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 23.319  -11.406 -21.648 1.00 45.12  ? 261 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 31.884  -21.310 -38.213 1.00 49.30  ? 262 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 6.177   -20.521 -25.012 1.00 43.53  ? 263 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 27.843  -24.940 -34.945 1.00 36.91  ? 264 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 39.230  -13.044 -38.919 1.00 74.55  ? 265 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 24.737  -6.690  -42.578 1.00 52.07  ? 266 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 12.520  -20.430 -19.833 1.00 53.81  ? 267 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 17.388  -0.382  -25.465 1.00 50.73  ? 268 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 15.257  -8.289  -42.975 1.00 47.40  ? 269 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 9.671   -6.106  -40.942 1.00 48.72  ? 270 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 19.163  4.083   -33.625 1.00 45.16  ? 271 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 16.087  -26.144 -21.032 1.00 69.43  ? 272 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 6.813   -23.144 -24.189 1.00 60.62  ? 273 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 7.118   -9.784  -18.457 1.00 41.29  ? 274 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 14.919  -21.981 -41.764 1.00 52.82  ? 275 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 7.474   -21.579 -29.864 1.00 45.78  ? 276 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 21.996  -29.276 -35.397 1.00 52.15  ? 277 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 20.692  -20.922 -20.928 1.00 53.98  ? 278 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 16.520  3.259   -26.578 1.00 65.92  ? 279 HOH   B O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 15.243  -18.056 25.456  1.00 61.56  ? 201 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 26.038  -38.990 12.728  1.00 38.94  ? 202 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 26.131  -37.432 10.035  1.00 44.96  ? 203 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 5.299   -26.710 16.520  1.00 41.92  ? 204 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 12.350  -28.026 28.266  1.00 55.26  ? 205 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 8.520   -36.772 18.437  1.00 52.11  ? 206 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 19.435  -20.994 30.713  1.00 68.68  ? 207 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 29.644  -40.436 9.545   1.00 36.20  ? 208 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 7.174   -31.628 12.160  1.00 49.37  ? 209 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 17.080  -16.985 14.722  1.00 50.49  ? 210 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 19.443  -41.777 12.217  1.00 31.01  ? 211 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 12.851  -23.013 28.047  1.00 65.30  ? 212 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 30.007  -25.170 32.414  1.00 61.13  ? 213 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 22.604  -41.354 18.643  1.00 46.64  ? 214 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 12.324  -31.460 8.234   1.00 36.06  ? 215 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 29.851  -31.398 15.731  1.00 53.92  ? 216 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 14.651  -21.027 12.146  1.00 38.20  ? 217 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 29.611  -39.589 31.378  1.00 36.11  ? 218 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 21.904  -28.430 11.102  1.00 31.14  ? 219 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 31.204  -43.016 12.065  1.00 46.63  ? 220 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 22.346  -21.669 7.412   1.00 39.15  ? 221 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 18.625  -20.037 10.581  1.00 37.10  ? 222 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 9.059   -33.444 9.402   1.00 51.80  ? 223 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 27.935  -37.053 16.001  1.00 42.39  ? 224 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 13.929  -39.486 16.644  1.00 65.56  ? 225 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 30.168  -17.306 9.796   1.00 50.76  ? 226 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 20.377  -28.699 8.412   1.00 36.35  ? 227 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 24.809  -31.289 10.700  1.00 36.12  ? 228 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 25.390  -17.370 13.692  1.00 42.08  ? 229 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 6.440   -17.998 10.872  1.00 35.42  ? 230 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 27.250  -15.293 12.740  1.00 57.56  ? 231 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 13.810  -37.114 13.694  1.00 45.98  ? 232 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 21.665  -34.337 16.540  1.00 26.38  ? 233 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 20.566  -39.767 26.315  1.00 44.01  ? 234 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 16.719  -40.832 11.499  1.00 52.95  ? 235 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 31.041  -39.645 27.067  1.00 42.40  ? 236 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 20.450  -40.731 39.137  1.00 66.34  ? 237 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 25.989  -33.791 34.570  1.00 58.99  ? 238 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 15.432  -17.500 19.317  1.00 43.88  ? 239 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 18.723  -26.712 3.045   1.00 45.94  ? 240 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 30.601  -35.422 28.341  1.00 50.23  ? 241 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 31.609  -33.388 25.852  1.00 44.99  ? 242 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 30.231  -29.178 11.967  1.00 53.93  ? 243 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 8.389   -19.188 23.789  1.00 47.11  ? 244 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 27.286  -37.663 25.013  1.00 46.56  ? 245 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 19.281  -18.957 25.051  1.00 43.85  ? 246 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 25.491  -17.777 21.088  1.00 60.74  ? 247 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 22.560  -18.337 21.852  1.00 49.40  ? 248 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 20.695  -29.402 4.786   1.00 51.02  ? 249 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 14.027  -38.689 9.659   1.00 51.49  ? 250 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 27.792  -36.429 18.626  1.00 50.13  ? 251 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 9.208   -30.477 9.905   1.00 36.45  ? 252 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 4.843   -24.235 18.586  1.00 62.58  ? 253 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 24.970  -39.648 20.328  1.00 37.86  ? 254 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 30.774  -43.387 15.902  1.00 59.92  ? 255 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 14.547  -41.196 14.655  1.00 52.20  ? 256 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 32.963  -24.547 31.780  1.00 57.70  ? 257 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 2.206   -28.862 13.776  1.00 62.86  ? 258 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 29.715  -32.549 18.295  1.00 43.25  ? 259 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 20.898  -35.211 7.529   1.00 63.16  ? 260 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 20.043  -12.900 13.389  1.00 48.32  ? 261 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 16.926  -38.202 28.365  1.00 60.02  ? 262 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 29.776  -33.352 14.086  1.00 54.37  ? 263 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 11.597  -21.041 10.721  1.00 36.27  ? 264 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 22.080  -13.589 13.328  1.00 50.64  ? 265 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 17.184  -36.230 29.776  1.00 57.99  ? 266 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 28.877  -41.584 27.237  1.00 41.43  ? 267 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 31.743  -39.184 29.838  1.00 46.35  ? 268 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 16.861  -16.526 24.253  1.00 57.41  ? 269 HOH   C O   1 
# 
