data_7HHJ
# 
_entry.id   7HHJ 
# 
_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   7HHJ         pdb_00007hhj 10.2210/pdb7hhj/pdb 
WWPDB D_1001407481 ?            ?                   
# 
_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                        7HHJ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn 2-bromo-4-fluoro-N,N-dimethylbenzamide             246.076   1   ? ?    ? ? 
5 water       nat water                                              18.015    268 ? ?    ? ? 
# 
_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 2-bromo-4-fluoro-N,N-dimethylbenzamide WJ7 
5 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                               ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                             ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                        ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                               ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                         'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                              ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                        ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                              ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                  ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                             ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                 ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                             ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                          ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                 ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                          ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                              ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                             ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                               ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                 ?                 'C5 H11 N O2'    117.146 
WJ7 non-polymer         . 2-bromo-4-fluoro-N,N-dimethylbenzamide ?                 'C9 H9 Br F N O' 246.076 
# 
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  ?  ?   ?   C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 ?  ?   ?   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        WJ7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WJ7 
_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 WJ7 1   103 101 WJ7 LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 368 HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 335 HOH HOH A . 
M 5 HOH 5   205 340 HOH HOH A . 
M 5 HOH 6   206 35  HOH HOH A . 
M 5 HOH 7   207 334 HOH HOH A . 
M 5 HOH 8   208 139 HOH HOH A . 
M 5 HOH 9   209 337 HOH HOH A . 
M 5 HOH 10  210 66  HOH HOH A . 
M 5 HOH 11  211 167 HOH HOH A . 
M 5 HOH 12  212 91  HOH HOH A . 
M 5 HOH 13  213 27  HOH HOH A . 
M 5 HOH 14  214 278 HOH HOH A . 
M 5 HOH 15  215 208 HOH HOH A . 
M 5 HOH 16  216 71  HOH HOH A . 
M 5 HOH 17  217 38  HOH HOH A . 
M 5 HOH 18  218 86  HOH HOH A . 
M 5 HOH 19  219 357 HOH HOH A . 
M 5 HOH 20  220 85  HOH HOH A . 
M 5 HOH 21  221 301 HOH HOH A . 
M 5 HOH 22  222 55  HOH HOH A . 
M 5 HOH 23  223 293 HOH HOH A . 
M 5 HOH 24  224 350 HOH HOH A . 
M 5 HOH 25  225 23  HOH HOH A . 
M 5 HOH 26  226 299 HOH HOH A . 
M 5 HOH 27  227 97  HOH HOH A . 
M 5 HOH 28  228 289 HOH HOH A . 
M 5 HOH 29  229 142 HOH HOH A . 
M 5 HOH 30  230 8   HOH HOH A . 
M 5 HOH 31  231 28  HOH HOH A . 
M 5 HOH 32  232 188 HOH HOH A . 
M 5 HOH 33  233 37  HOH HOH A . 
M 5 HOH 34  234 12  HOH HOH A . 
M 5 HOH 35  235 87  HOH HOH A . 
M 5 HOH 36  236 260 HOH HOH A . 
M 5 HOH 37  237 93  HOH HOH A . 
M 5 HOH 38  238 1   HOH HOH A . 
M 5 HOH 39  239 7   HOH HOH A . 
M 5 HOH 40  240 222 HOH HOH A . 
M 5 HOH 41  241 99  HOH HOH A . 
M 5 HOH 42  242 290 HOH HOH A . 
M 5 HOH 43  243 26  HOH HOH A . 
M 5 HOH 44  244 32  HOH HOH A . 
M 5 HOH 45  245 60  HOH HOH A . 
M 5 HOH 46  246 267 HOH HOH A . 
M 5 HOH 47  247 2   HOH HOH A . 
M 5 HOH 48  248 109 HOH HOH A . 
M 5 HOH 49  249 364 HOH HOH A . 
M 5 HOH 50  250 292 HOH HOH A . 
M 5 HOH 51  251 151 HOH HOH A . 
M 5 HOH 52  252 111 HOH HOH A . 
M 5 HOH 53  253 345 HOH HOH A . 
M 5 HOH 54  254 34  HOH HOH A . 
M 5 HOH 55  255 365 HOH HOH A . 
M 5 HOH 56  256 145 HOH HOH A . 
M 5 HOH 57  257 42  HOH HOH A . 
M 5 HOH 58  258 84  HOH HOH A . 
M 5 HOH 59  259 18  HOH HOH A . 
M 5 HOH 60  260 199 HOH HOH A . 
M 5 HOH 61  261 78  HOH HOH A . 
M 5 HOH 62  262 274 HOH HOH A . 
M 5 HOH 63  263 20  HOH HOH A . 
M 5 HOH 64  264 190 HOH HOH A . 
M 5 HOH 65  265 116 HOH HOH A . 
M 5 HOH 66  266 179 HOH HOH A . 
M 5 HOH 67  267 300 HOH HOH A . 
M 5 HOH 68  268 203 HOH HOH A . 
M 5 HOH 69  269 344 HOH HOH A . 
M 5 HOH 70  270 359 HOH HOH A . 
M 5 HOH 71  271 115 HOH HOH A . 
M 5 HOH 72  272 281 HOH HOH A . 
M 5 HOH 73  273 259 HOH HOH A . 
M 5 HOH 74  274 165 HOH HOH A . 
M 5 HOH 75  275 164 HOH HOH A . 
M 5 HOH 76  276 143 HOH HOH A . 
M 5 HOH 77  277 9   HOH HOH A . 
M 5 HOH 78  278 47  HOH HOH A . 
M 5 HOH 79  279 288 HOH HOH A . 
M 5 HOH 80  280 211 HOH HOH A . 
M 5 HOH 81  281 95  HOH HOH A . 
M 5 HOH 82  282 19  HOH HOH A . 
M 5 HOH 83  283 21  HOH HOH A . 
M 5 HOH 84  284 218 HOH HOH A . 
M 5 HOH 85  285 58  HOH HOH A . 
M 5 HOH 86  286 360 HOH HOH A . 
M 5 HOH 87  287 113 HOH HOH A . 
M 5 HOH 88  288 22  HOH HOH A . 
M 5 HOH 89  289 77  HOH HOH A . 
M 5 HOH 90  290 16  HOH HOH A . 
M 5 HOH 91  291 94  HOH HOH A . 
M 5 HOH 92  292 327 HOH HOH A . 
M 5 HOH 93  293 31  HOH HOH A . 
M 5 HOH 94  294 367 HOH HOH A . 
M 5 HOH 95  295 131 HOH HOH A . 
M 5 HOH 96  296 318 HOH HOH A . 
M 5 HOH 97  297 73  HOH HOH A . 
M 5 HOH 98  298 210 HOH HOH A . 
M 5 HOH 99  299 83  HOH HOH A . 
M 5 HOH 100 300 296 HOH HOH A . 
M 5 HOH 101 301 156 HOH HOH A . 
M 5 HOH 102 302 185 HOH HOH A . 
M 5 HOH 103 303 219 HOH HOH A . 
M 5 HOH 104 304 354 HOH HOH A . 
M 5 HOH 105 305 63  HOH HOH A . 
M 5 HOH 106 306 75  HOH HOH A . 
M 5 HOH 107 307 283 HOH HOH A . 
M 5 HOH 108 308 149 HOH HOH A . 
M 5 HOH 109 309 108 HOH HOH A . 
M 5 HOH 110 310 57  HOH HOH A . 
M 5 HOH 111 311 152 HOH HOH A . 
M 5 HOH 112 312 205 HOH HOH A . 
M 5 HOH 113 313 125 HOH HOH A . 
M 5 HOH 114 314 332 HOH HOH A . 
N 5 HOH 1   201 258 HOH HOH B . 
N 5 HOH 2   202 247 HOH HOH B . 
N 5 HOH 3   203 347 HOH HOH B . 
N 5 HOH 4   204 279 HOH HOH B . 
N 5 HOH 5   205 343 HOH HOH B . 
N 5 HOH 6   206 331 HOH HOH B . 
N 5 HOH 7   207 89  HOH HOH B . 
N 5 HOH 8   208 123 HOH HOH B . 
N 5 HOH 9   209 68  HOH HOH B . 
N 5 HOH 10  210 172 HOH HOH B . 
N 5 HOH 11  211 215 HOH HOH B . 
N 5 HOH 12  212 98  HOH HOH B . 
N 5 HOH 13  213 272 HOH HOH B . 
N 5 HOH 14  214 348 HOH HOH B . 
N 5 HOH 15  215 336 HOH HOH B . 
N 5 HOH 16  216 168 HOH HOH B . 
N 5 HOH 17  217 169 HOH HOH B . 
N 5 HOH 18  218 341 HOH HOH B . 
N 5 HOH 19  219 184 HOH HOH B . 
N 5 HOH 20  220 72  HOH HOH B . 
N 5 HOH 21  221 249 HOH HOH B . 
N 5 HOH 22  222 137 HOH HOH B . 
N 5 HOH 23  223 242 HOH HOH B . 
N 5 HOH 24  224 117 HOH HOH B . 
N 5 HOH 25  225 69  HOH HOH B . 
N 5 HOH 26  226 5   HOH HOH B . 
N 5 HOH 27  227 17  HOH HOH B . 
N 5 HOH 28  228 329 HOH HOH B . 
N 5 HOH 29  229 223 HOH HOH B . 
N 5 HOH 30  230 150 HOH HOH B . 
N 5 HOH 31  231 24  HOH HOH B . 
N 5 HOH 32  232 76  HOH HOH B . 
N 5 HOH 33  233 6   HOH HOH B . 
N 5 HOH 34  234 96  HOH HOH B . 
N 5 HOH 35  235 10  HOH HOH B . 
N 5 HOH 36  236 261 HOH HOH B . 
N 5 HOH 37  237 46  HOH HOH B . 
N 5 HOH 38  238 59  HOH HOH B . 
N 5 HOH 39  239 119 HOH HOH B . 
N 5 HOH 40  240 101 HOH HOH B . 
N 5 HOH 41  241 61  HOH HOH B . 
N 5 HOH 42  242 54  HOH HOH B . 
N 5 HOH 43  243 74  HOH HOH B . 
N 5 HOH 44  244 280 HOH HOH B . 
N 5 HOH 45  245 356 HOH HOH B . 
N 5 HOH 46  246 197 HOH HOH B . 
N 5 HOH 47  247 217 HOH HOH B . 
N 5 HOH 48  248 214 HOH HOH B . 
N 5 HOH 49  249 120 HOH HOH B . 
N 5 HOH 50  250 175 HOH HOH B . 
N 5 HOH 51  251 25  HOH HOH B . 
N 5 HOH 52  252 320 HOH HOH B . 
N 5 HOH 53  253 170 HOH HOH B . 
N 5 HOH 54  254 224 HOH HOH B . 
N 5 HOH 55  255 36  HOH HOH B . 
N 5 HOH 56  256 13  HOH HOH B . 
N 5 HOH 57  257 153 HOH HOH B . 
N 5 HOH 58  258 79  HOH HOH B . 
N 5 HOH 59  259 44  HOH HOH B . 
N 5 HOH 60  260 315 HOH HOH B . 
N 5 HOH 61  261 303 HOH HOH B . 
N 5 HOH 62  262 157 HOH HOH B . 
N 5 HOH 63  263 104 HOH HOH B . 
N 5 HOH 64  264 349 HOH HOH B . 
N 5 HOH 65  265 346 HOH HOH B . 
N 5 HOH 66  266 370 HOH HOH B . 
N 5 HOH 67  267 182 HOH HOH B . 
N 5 HOH 68  268 201 HOH HOH B . 
N 5 HOH 69  269 163 HOH HOH B . 
N 5 HOH 70  270 319 HOH HOH B . 
N 5 HOH 71  271 353 HOH HOH B . 
N 5 HOH 72  272 309 HOH HOH B . 
N 5 HOH 73  273 338 HOH HOH B . 
N 5 HOH 74  274 291 HOH HOH B . 
N 5 HOH 75  275 177 HOH HOH B . 
N 5 HOH 76  276 322 HOH HOH B . 
N 5 HOH 77  277 160 HOH HOH B . 
N 5 HOH 78  278 316 HOH HOH B . 
N 5 HOH 79  279 314 HOH HOH B . 
N 5 HOH 80  280 355 HOH HOH B . 
N 5 HOH 81  281 369 HOH HOH B . 
N 5 HOH 82  282 92  HOH HOH B . 
N 5 HOH 83  283 312 HOH HOH B . 
N 5 HOH 84  284 107 HOH HOH B . 
N 5 HOH 85  285 313 HOH HOH B . 
N 5 HOH 86  286 310 HOH HOH B . 
O 5 HOH 1   201 317 HOH HOH C . 
O 5 HOH 2   202 173 HOH HOH C . 
O 5 HOH 3   203 134 HOH HOH C . 
O 5 HOH 4   204 321 HOH HOH C . 
O 5 HOH 5   205 333 HOH HOH C . 
O 5 HOH 6   206 148 HOH HOH C . 
O 5 HOH 7   207 254 HOH HOH C . 
O 5 HOH 8   208 161 HOH HOH C . 
O 5 HOH 9   209 15  HOH HOH C . 
O 5 HOH 10  210 323 HOH HOH C . 
O 5 HOH 11  211 226 HOH HOH C . 
O 5 HOH 12  212 90  HOH HOH C . 
O 5 HOH 13  213 45  HOH HOH C . 
O 5 HOH 14  214 269 HOH HOH C . 
O 5 HOH 15  215 49  HOH HOH C . 
O 5 HOH 16  216 358 HOH HOH C . 
O 5 HOH 17  217 41  HOH HOH C . 
O 5 HOH 18  218 325 HOH HOH C . 
O 5 HOH 19  219 284 HOH HOH C . 
O 5 HOH 20  220 102 HOH HOH C . 
O 5 HOH 21  221 118 HOH HOH C . 
O 5 HOH 22  222 304 HOH HOH C . 
O 5 HOH 23  223 189 HOH HOH C . 
O 5 HOH 24  224 4   HOH HOH C . 
O 5 HOH 25  225 82  HOH HOH C . 
O 5 HOH 26  226 126 HOH HOH C . 
O 5 HOH 27  227 132 HOH HOH C . 
O 5 HOH 28  228 40  HOH HOH C . 
O 5 HOH 29  229 366 HOH HOH C . 
O 5 HOH 30  230 351 HOH HOH C . 
O 5 HOH 31  231 122 HOH HOH C . 
O 5 HOH 32  232 56  HOH HOH C . 
O 5 HOH 33  233 135 HOH HOH C . 
O 5 HOH 34  234 361 HOH HOH C . 
O 5 HOH 35  235 62  HOH HOH C . 
O 5 HOH 36  236 363 HOH HOH C . 
O 5 HOH 37  237 302 HOH HOH C . 
O 5 HOH 38  238 48  HOH HOH C . 
O 5 HOH 39  239 43  HOH HOH C . 
O 5 HOH 40  240 130 HOH HOH C . 
O 5 HOH 41  241 287 HOH HOH C . 
O 5 HOH 42  242 352 HOH HOH C . 
O 5 HOH 43  243 294 HOH HOH C . 
O 5 HOH 44  244 67  HOH HOH C . 
O 5 HOH 45  245 64  HOH HOH C . 
O 5 HOH 46  246 362 HOH HOH C . 
O 5 HOH 47  247 275 HOH HOH C . 
O 5 HOH 48  248 271 HOH HOH C . 
O 5 HOH 49  249 53  HOH HOH C . 
O 5 HOH 50  250 198 HOH HOH C . 
O 5 HOH 51  251 246 HOH HOH C . 
O 5 HOH 52  252 328 HOH HOH C . 
O 5 HOH 53  253 209 HOH HOH C . 
O 5 HOH 54  254 305 HOH HOH C . 
O 5 HOH 55  255 326 HOH HOH C . 
O 5 HOH 56  256 146 HOH HOH C . 
O 5 HOH 57  257 171 HOH HOH C . 
O 5 HOH 58  258 298 HOH HOH C . 
O 5 HOH 59  259 65  HOH HOH C . 
O 5 HOH 60  260 241 HOH HOH C . 
O 5 HOH 61  261 330 HOH HOH C . 
O 5 HOH 62  262 70  HOH HOH C . 
O 5 HOH 63  263 342 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  266 103 HOH HOH C . 
O 5 HOH 67  267 206 HOH HOH C . 
O 5 HOH 68  268 295 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
2  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
3  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
4  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
5  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
6  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
7  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
8  1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
9  1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
10 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
11 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
12 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
13 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
14 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
15 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
16 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
17 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
18 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
19 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
20 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
21 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
22 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
23 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
24 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
25 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
26 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
27 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
28 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
29 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
30 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
31 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
32 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
33 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
34 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
35 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
36 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
37 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
38 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
39 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
40 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
41 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
42 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHJ 
_cell.length_a           41.400 
_cell.length_b           41.980 
_cell.length_c           157.860 
_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                         7HHJ 
_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          7HHJ 
_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                     7HHJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.62 
_reflns.d_resolution_high            1.78 
_reflns.number_obs                   27335 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.101 
_reflns.pdbx_netI_over_sigmaI        9.8 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.110 
_reflns.pdbx_Rpim_I_all              0.043 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     173614 
_reflns.pdbx_chi_squared             0.98 
_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                  1.78 
_reflns_shell.d_res_low                   1.83 
_reflns_shell.number_measured_all         13344 
_reflns_shell.number_unique_obs           1992 
_reflns_shell.Rmerge_I_obs                2.642 
_reflns_shell.pdbx_chi_squared            0.83 
_reflns_shell.pdbx_redundancy             6.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             2.862 
_reflns_shell.pdbx_Rpim_I_all             1.091 
_reflns_shell.pdbx_CC_half                0.328 
_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                                 7HHJ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     25867 
_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                             40.60 
_refine.ls_d_res_high                            1.78 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_R_factor_obs                          0.20135 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19834 
_refine.ls_R_factor_R_free                       0.25503 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1399 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.B_iso_mean                               43.236 
_refine.aniso_B[1][1]                            0.71 
_refine.aniso_B[2][2]                            0.34 
_refine.aniso_B[3][3]                            -1.05 
_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                       0.141 
_refine.pdbx_overall_ESU_R_Free                  0.143 
_refine.overall_SU_ML                            0.146 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.107 
_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        2139 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             268 
_refine_hist.number_atoms_total               2458 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        40.60 
# 
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             0.007  0.012  ? 2292 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.578  1.836  ? 3116 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.137  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.402  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.898 10.000 ? 315  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.122  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 1910 '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                  3.663  4.076  ? 1070 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.149  7.281  ? 1332 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.432  4.360  ? 1222 '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       10.094 59.20  ? 3632 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.780 
_refine_ls_shell.d_res_low                        1.826 
_refine_ls_shell.number_reflns_R_work             1892 
_refine_ls_shell.R_factor_R_work                  0.371 
_refine_ls_shell.percent_reflns_obs               99.75 
_refine_ls_shell.R_factor_R_free                  0.402 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             89 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z100642432' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHJ 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHJ A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHJ B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHJ 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 7HHJ GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHJ SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHJ GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHJ SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHJ GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHJ SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O 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                   7HHJ 
_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 244 ? ? O B HOH 276 ? ? 1.74 
2  1 O   A HOH 281 ? ? O A HOH 290 ? ? 1.78 
3  1 O   A HOH 226 ? ? O C HOH 205 ? ? 1.82 
4  1 O2  A SO4 104 ? ? O A HOH 201 ? ? 1.91 
5  1 O   C HOH 216 ? ? O C HOH 255 ? ? 1.98 
6  1 O   C HOH 206 ? ? O C HOH 236 ? ? 1.99 
7  1 O   B HOH 241 ? ? O B HOH 283 ? ? 2.03 
8  1 OD1 C ASP 26  ? ? O C HOH 201 ? ? 2.05 
9  1 O   C HOH 256 ? ? O C HOH 265 ? ? 2.06 
10 1 OD1 A ASP 62  ? ? O A HOH 202 ? ? 2.08 
11 1 O   B HOH 212 ? ? O B HOH 273 ? ? 2.13 
12 1 O   B HOH 261 ? ? O B HOH 276 ? ? 2.14 
13 1 O4  A SO4 104 ? ? O A HOH 203 ? ? 2.14 
14 1 O   B HOH 210 ? ? O B HOH 231 ? ? 2.15 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     237 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     229 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_435 
_pdbx_validate_symm_contact.dist              2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                110.63 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            10.43 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -154.23 66.78   
2 1 ASN B 38 ? ? 80.29   -11.24  
3 1 PRO B 60 ? ? -37.62  127.52  
4 1 ASN B 87 ? ? -157.53 62.08   
5 1 ASN C 87 ? ? -159.38 57.12   
6 1 ALA C 90 ? ? -68.33  -173.26 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.094 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 HIS 3  ? C HIS 4  
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
15 1 Y 1 C LYS 34 ? C LYS 35 
16 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
SO4 S    S  N N 314 
SO4 O1   O  N N 315 
SO4 O2   O  N N 316 
SO4 O3   O  N N 317 
SO4 O4   O  N N 318 
THR N    N  N N 319 
THR CA   C  N S 320 
THR C    C  N N 321 
THR O    O  N N 322 
THR CB   C  N R 323 
THR OG1  O  N N 324 
THR CG2  C  N N 325 
THR OXT  O  N N 326 
THR H    H  N N 327 
THR H2   H  N N 328 
THR HA   H  N N 329 
THR HB   H  N N 330 
THR HG1  H  N N 331 
THR HG21 H  N N 332 
THR HG22 H  N N 333 
THR HG23 H  N N 334 
THR HXT  H  N N 335 
TRP N    N  N N 336 
TRP CA   C  N S 337 
TRP C    C  N N 338 
TRP O    O  N N 339 
TRP CB   C  N N 340 
TRP CG   C  Y N 341 
TRP CD1  C  Y N 342 
TRP CD2  C  Y N 343 
TRP NE1  N  Y N 344 
TRP CE2  C  Y N 345 
TRP CE3  C  Y N 346 
TRP CZ2  C  Y N 347 
TRP CZ3  C  Y N 348 
TRP CH2  C  Y N 349 
TRP OXT  O  N N 350 
TRP H    H  N N 351 
TRP H2   H  N N 352 
TRP HA   H  N N 353 
TRP HB2  H  N N 354 
TRP HB3  H  N N 355 
TRP HD1  H  N N 356 
TRP HE1  H  N N 357 
TRP HE3  H  N N 358 
TRP HZ2  H  N N 359 
TRP HZ3  H  N N 360 
TRP HH2  H  N N 361 
TRP HXT  H  N N 362 
TYR N    N  N N 363 
TYR CA   C  N S 364 
TYR C    C  N N 365 
TYR O    O  N N 366 
TYR CB   C  N N 367 
TYR CG   C  Y N 368 
TYR CD1  C  Y N 369 
TYR CD2  C  Y N 370 
TYR CE1  C  Y N 371 
TYR CE2  C  Y N 372 
TYR CZ   C  Y N 373 
TYR OH   O  N N 374 
TYR OXT  O  N N 375 
TYR H    H  N N 376 
TYR H2   H  N N 377 
TYR HA   H  N N 378 
TYR HB2  H  N N 379 
TYR HB3  H  N N 380 
TYR HD1  H  N N 381 
TYR HD2  H  N N 382 
TYR HE1  H  N N 383 
TYR HE2  H  N N 384 
TYR HH   H  N N 385 
TYR HXT  H  N N 386 
VAL N    N  N N 387 
VAL CA   C  N S 388 
VAL C    C  N N 389 
VAL O    O  N N 390 
VAL CB   C  N N 391 
VAL CG1  C  N N 392 
VAL CG2  C  N N 393 
VAL OXT  O  N N 394 
VAL H    H  N N 395 
VAL H2   H  N N 396 
VAL HA   H  N N 397 
VAL HB   H  N N 398 
VAL HG11 H  N N 399 
VAL HG12 H  N N 400 
VAL HG13 H  N N 401 
VAL HG21 H  N N 402 
VAL HG22 H  N N 403 
VAL HG23 H  N N 404 
VAL HXT  H  N N 405 
WJ7 C4   C  Y N 406 
WJ7 C5   C  Y N 407 
WJ7 C6   C  Y N 408 
WJ7 C7   C  Y N 409 
WJ7 C8   C  Y N 410 
WJ7 N    N  N N 411 
WJ7 C    C  N N 412 
WJ7 O    O  N N 413 
WJ7 C1   C  N N 414 
WJ7 C2   C  N N 415 
WJ7 C3   C  Y N 416 
WJ7 F    F  N N 417 
WJ7 BR   BR N N 418 
WJ7 H6   H  N N 419 
WJ7 H7   H  N N 420 
WJ7 H8   H  N N 421 
WJ7 H2   H  N N 422 
WJ7 H    H  N N 423 
WJ7 H1   H  N N 424 
WJ7 H4   H  N N 425 
WJ7 H5   H  N N 426 
WJ7 H3   H  N N 427 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
WJ7 C   N    sing N N 389 
WJ7 C1  N    sing N N 390 
WJ7 N   C2   sing N N 391 
WJ7 O   C2   doub N N 392 
WJ7 C2  C3   sing N N 393 
WJ7 C3  C4   sing Y N 394 
WJ7 C4  C5   doub Y N 395 
WJ7 C5  C6   sing Y N 396 
WJ7 F   C6   sing N N 397 
WJ7 C6  C7   doub Y N 398 
WJ7 C7  C8   sing Y N 399 
WJ7 C3  C8   doub Y N 400 
WJ7 C8  BR   sing N N 401 
WJ7 C4  H6   sing N N 402 
WJ7 C5  H7   sing N N 403 
WJ7 C7  H8   sing N N 404 
WJ7 C   H2   sing N N 405 
WJ7 C   H    sing N N 406 
WJ7 C   H1   sing N N 407 
WJ7 C1  H4   sing N N 408 
WJ7 C1  H5   sing N N 409 
WJ7 C1  H3   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                    7HHJ 
_atom_sites.fract_transf_matrix[1][1]   0.024155 
_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]   0.023821 
_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]   0.006335 
_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 
BR 
C  
F  
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  ? 0.680   4.261   2.473   1.00 65.33  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 2  ? -0.444  3.564   1.793   1.00 66.56  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 2  ? 0.087   2.496   0.833   1.00 61.11  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 2  ? 1.180   2.624   0.285   1.00 56.33  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 2  ? -1.363  4.559   1.071   1.00 74.39  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 2  ? -2.350  5.274   1.988   1.00 82.02  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 2  ? -3.734  4.316   2.650   1.00 81.84  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 2  ? -4.660  5.613   3.482   1.00 74.76  ? 1   MET A CE  1 
ATOM   9    N  N   . PRO A 1 3  ? -0.656  1.378   0.648   1.00 59.64  ? 2   PRO A N   1 
ATOM   10   C  CA  . PRO A 1 3  ? -0.268  0.316   -0.291  1.00 55.47  ? 2   PRO A CA  1 
ATOM   11   C  C   . PRO A 1 3  ? -0.052  0.741   -1.747  1.00 51.27  ? 2   PRO A C   1 
ATOM   12   O  O   . PRO A 1 3  ? -0.796  1.561   -2.285  1.00 48.96  ? 2   PRO A O   1 
ATOM   13   C  CB  . PRO A 1 3  ? -1.477  -0.669  -0.150  1.00 53.44  ? 2   PRO A CB  1 
ATOM   14   C  CG  . PRO A 1 3  ? -1.934  -0.457  1.287   1.00 53.14  ? 2   PRO A CG  1 
ATOM   15   C  CD  . PRO A 1 3  ? -1.892  1.054   1.390   1.00 54.89  ? 2   PRO A CD  1 
ATOM   16   N  N   . HIS A 1 4  ? 0.976   0.156   -2.367  1.00 44.90  ? 3   HIS A N   1 
ATOM   17   C  CA  . HIS A 1 4  ? 1.167   0.216   -3.801  1.00 43.02  ? 3   HIS A CA  1 
ATOM   18   C  C   . HIS A 1 4  ? 0.580   -1.072  -4.373  1.00 42.28  ? 3   HIS A C   1 
ATOM   19   O  O   . HIS A 1 4  ? 0.067   -1.898  -3.612  1.00 41.28  ? 3   HIS A O   1 
ATOM   20   C  CB  . HIS A 1 4  ? 2.668   0.272   -4.113  1.00 51.29  ? 3   HIS A CB  1 
ATOM   21   C  CG  . HIS A 1 4  ? 3.376   1.491   -3.616  1.00 62.93  ? 3   HIS A CG  1 
ATOM   22   N  ND1 . HIS A 1 4  ? 3.186   2.044   -2.367  1.00 69.57  ? 3   HIS A ND1 1 
ATOM   23   C  CD2 . HIS A 1 4  ? 4.291   2.255   -4.225  1.00 68.87  ? 3   HIS A CD2 1 
ATOM   24   C  CE1 . HIS A 1 4  ? 3.958   3.112   -2.238  1.00 69.96  ? 3   HIS A CE1 1 
ATOM   25   N  NE2 . HIS A 1 4  ? 4.644   3.253   -3.353  1.00 72.63  ? 3   HIS A NE2 1 
ATOM   26   N  N   . ALA A 1 5  ? 0.654   -1.224  -5.703  1.00 36.01  ? 4   ALA A N   1 
ATOM   27   C  CA  . ALA A 1 5  ? 0.465   -2.493  -6.386  1.00 36.44  ? 4   ALA A CA  1 
ATOM   28   C  C   . ALA A 1 5  ? 1.570   -3.462  -5.973  1.00 33.50  ? 4   ALA A C   1 
ATOM   29   O  O   . ALA A 1 5  ? 2.605   -3.034  -5.470  1.00 34.19  ? 4   ALA A O   1 
ATOM   30   C  CB  . ALA A 1 5  ? 0.494   -2.277  -7.891  1.00 38.90  ? 4   ALA A CB  1 
ATOM   31   N  N   . PHE A 1 6  ? 1.313   -4.766  -6.152  1.00 33.59  ? 5   PHE A N   1 
ATOM   32   C  CA  . PHE A 1 6  ? 2.302   -5.807  -5.910  1.00 31.08  ? 5   PHE A CA  1 
ATOM   33   C  C   . PHE A 1 6  ? 3.494   -5.610  -6.853  1.00 32.00  ? 5   PHE A C   1 
ATOM   34   O  O   . PHE A 1 6  ? 3.308   -5.254  -8.018  1.00 34.72  ? 5   PHE A O   1 
ATOM   35   C  CB  . PHE A 1 6  ? 1.651   -7.194  -6.018  1.00 25.66  ? 5   PHE A CB  1 
ATOM   36   C  CG  . PHE A 1 6  ? 0.917   -7.602  -4.741  1.00 29.42  ? 5   PHE A CG  1 
ATOM   37   C  CD1 . PHE A 1 6  ? 1.609   -7.741  -3.529  1.00 28.71  ? 5   PHE A CD1 1 
ATOM   38   C  CD2 . PHE A 1 6  ? -0.458  -7.858  -4.752  1.00 27.94  ? 5   PHE A CD2 1 
ATOM   39   C  CE1 . PHE A 1 6  ? 0.934   -8.085  -2.351  1.00 28.64  ? 5   PHE A CE1 1 
ATOM   40   C  CE2 . PHE A 1 6  ? -1.124  -8.223  -3.576  1.00 23.89  ? 5   PHE A CE2 1 
ATOM   41   C  CZ  . PHE A 1 6  ? -0.433  -8.330  -2.390  1.00 27.36  ? 5   PHE A CZ  1 
ATOM   42   N  N   . LYS A 1 7  ? 4.714   -5.858  -6.348  1.00 29.36  ? 6   LYS A N   1 
ATOM   43   C  CA  . LYS A 1 7  ? 5.896   -5.809  -7.201  1.00 32.35  ? 6   LYS A CA  1 
ATOM   44   C  C   . LYS A 1 7  ? 6.792   -7.032  -6.950  1.00 30.02  ? 6   LYS A C   1 
ATOM   45   O  O   . LYS A 1 7  ? 6.783   -7.613  -5.858  1.00 29.57  ? 6   LYS A O   1 
ATOM   46   C  CB  . LYS A 1 7  ? 6.662   -4.508  -6.924  1.00 34.92  ? 6   LYS A CB  1 
ATOM   47   C  CG  . LYS A 1 7  ? 7.323   -4.463  -5.550  1.00 34.49  ? 6   LYS A CG  1 
ATOM   48   C  CD  . LYS A 1 7  ? 7.831   -3.062  -5.200  1.00 43.63  ? 6   LYS A CD  1 
ATOM   49   C  CE  . LYS A 1 7  ? 8.431   -2.981  -3.823  1.00 47.78  ? 6   LYS A CE  1 
ATOM   50   N  NZ  . LYS A 1 7  ? 7.462   -3.292  -2.768  1.00 49.11  ? 6   LYS A NZ  1 
ATOM   51   N  N   . PRO A 1 8  ? 7.603   -7.459  -7.944  1.00 27.26  ? 7   PRO A N   1 
ATOM   52   C  CA  . PRO A 1 8  ? 8.572   -8.540  -7.743  1.00 27.68  ? 7   PRO A CA  1 
ATOM   53   C  C   . PRO A 1 8  ? 9.352   -8.279  -6.448  1.00 26.79  ? 7   PRO A C   1 
ATOM   54   O  O   . PRO A 1 8  ? 9.712   -7.138  -6.142  1.00 26.88  ? 7   PRO A O   1 
ATOM   55   C  CB  . PRO A 1 8  ? 9.451   -8.399  -9.019  1.00 31.13  ? 7   PRO A CB  1 
ATOM   56   C  CG  . PRO A 1 8  ? 8.443   -7.989  -10.072 1.00 31.21  ? 7   PRO A CG  1 
ATOM   57   C  CD  . PRO A 1 8  ? 7.567   -6.972  -9.344  1.00 29.14  ? 7   PRO A CD  1 
ATOM   58   N  N   . GLY A 1 9  ? 9.481   -9.333  -5.642  1.00 25.13  ? 8   GLY A N   1 
ATOM   59   C  CA  . GLY A 1 9  ? 10.214  -9.280  -4.390  1.00 24.44  ? 8   GLY A CA  1 
ATOM   60   C  C   . GLY A 1 9  ? 9.273   -9.179  -3.183  1.00 28.30  ? 8   GLY A C   1 
ATOM   61   O  O   . GLY A 1 9  ? 9.694   -9.448  -2.042  1.00 29.00  ? 8   GLY A O   1 
ATOM   62   N  N   . ASP A 1 10 ? 8.004   -8.793  -3.403  1.00 27.35  ? 9   ASP A N   1 
ATOM   63   C  CA  . ASP A 1 10 ? 7.073   -8.685  -2.277  1.00 25.78  ? 9   ASP A CA  1 
ATOM   64   C  C   . ASP A 1 10 ? 6.839   -10.049 -1.631  1.00 24.21  ? 9   ASP A C   1 
ATOM   65   O  O   . ASP A 1 10 ? 6.699   -11.036 -2.324  1.00 25.03  ? 9   ASP A O   1 
ATOM   66   C  CB  . ASP A 1 10 ? 5.746   -8.054  -2.680  1.00 27.98  ? 9   ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 10 ? 5.786   -6.546  -2.871  1.00 30.40  ? 9   ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 10 ? 6.748   -5.922  -2.395  1.00 29.03  ? 9   ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 10 ? 4.875   -6.020  -3.522  1.00 30.47  ? 9   ASP A OD2 1 
ATOM   70   N  N   . LEU A 1 11 ? 6.756   -10.116 -0.286  1.00 23.76  ? 10  LEU A N   1 
ATOM   71   C  CA  . LEU A 1 11 ? 6.565   -11.400 0.379   1.00 24.70  ? 10  LEU A CA  1 
ATOM   72   C  C   . LEU A 1 11 ? 5.105   -11.466 0.839   1.00 25.41  ? 10  LEU A C   1 
ATOM   73   O  O   . LEU A 1 11 ? 4.543   -10.454 1.296   1.00 25.70  ? 10  LEU A O   1 
ATOM   74   C  CB  . LEU A 1 11 ? 7.487   -11.541 1.601   1.00 24.53  ? 10  LEU A CB  1 
ATOM   75   C  CG  . LEU A 1 11 ? 8.974   -11.229 1.361   1.00 25.36  ? 10  LEU A CG  1 
ATOM   76   C  CD1 . LEU A 1 11 ? 9.812   -11.382 2.614   1.00 29.34  ? 10  LEU A CD1 1 
ATOM   77   C  CD2 . LEU A 1 11 ? 9.504   -12.086 0.227   1.00 28.27  ? 10  LEU A CD2 1 
ATOM   78   N  N   . VAL A 1 12 ? 4.527   -12.666 0.767   1.00 22.40  ? 11  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 12 ? 3.096   -12.848 0.973   1.00 24.07  ? 11  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 12 ? 2.846   -14.234 1.555   1.00 28.03  ? 11  VAL A C   1 
ATOM   81   O  O   . VAL A 1 12 ? 3.741   -15.076 1.570   1.00 27.21  ? 11  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 12 ? 2.360   -12.717 -0.378  1.00 21.56  ? 11  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 12 ? 2.513   -11.299 -0.944  1.00 24.10  ? 11  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 12 ? 2.737   -13.818 -1.372  1.00 22.89  ? 11  VAL A CG2 1 
ATOM   85   N  N   . PHE A 1 13 ? 1.631   -14.435 2.069   1.00 24.73  ? 12  PHE A N   1 
ATOM   86   C  CA  . PHE A 1 13 ? 1.032   -15.757 2.092   1.00 26.02  ? 12  PHE A CA  1 
ATOM   87   C  C   . PHE A 1 13 ? 0.067   -15.804 0.912   1.00 28.88  ? 12  PHE A C   1 
ATOM   88   O  O   . PHE A 1 13 ? -0.663  -14.836 0.694   1.00 27.84  ? 12  PHE A O   1 
ATOM   89   C  CB  . PHE A 1 13 ? 0.237   -16.031 3.377   1.00 26.58  ? 12  PHE A CB  1 
ATOM   90   C  CG  . PHE A 1 13 ? 1.175   -16.155 4.563   1.00 26.07  ? 12  PHE A CG  1 
ATOM   91   C  CD1 . PHE A 1 13 ? 1.582   -15.027 5.268   1.00 28.03  ? 12  PHE A CD1 1 
ATOM   92   C  CD2 . PHE A 1 13 ? 1.671   -17.396 4.923   1.00 26.23  ? 12  PHE A CD2 1 
ATOM   93   C  CE1 . PHE A 1 13 ? 2.460   -15.155 6.336   1.00 33.98  ? 12  PHE A CE1 1 
ATOM   94   C  CE2 . PHE A 1 13 ? 2.539   -17.517 5.999   1.00 33.56  ? 12  PHE A CE2 1 
ATOM   95   C  CZ  . PHE A 1 13 ? 2.941   -16.399 6.684   1.00 35.04  ? 12  PHE A CZ  1 
ATOM   96   N  N   . ALA A 1 14 ? 0.156   -16.885 0.115   1.00 28.37  ? 13  ALA A N   1 
ATOM   97   C  CA  . ALA A 1 14 ? -0.652  -16.996 -1.089  1.00 28.34  ? 13  ALA A CA  1 
ATOM   98   C  C   . ALA A 1 14 ? -1.644  -18.138 -0.885  1.00 29.24  ? 13  ALA A C   1 
ATOM   99   O  O   . ALA A 1 14 ? -1.264  -19.209 -0.376  1.00 30.18  ? 13  ALA A O   1 
ATOM   100  C  CB  . ALA A 1 14 ? 0.239   -17.248 -2.310  1.00 24.07  ? 13  ALA A CB  1 
ATOM   101  N  N   . LYS A 1 15 ? -2.903  -17.892 -1.280  1.00 30.82  ? 14  LYS A N   1 
ATOM   102  C  CA  . LYS A 1 15 ? -3.962  -18.857 -1.044  1.00 31.24  ? 14  LYS A CA  1 
ATOM   103  C  C   . LYS A 1 15 ? -4.323  -19.549 -2.357  1.00 34.74  ? 14  LYS A C   1 
ATOM   104  O  O   . LYS A 1 15 ? -4.654  -18.889 -3.342  1.00 37.29  ? 14  LYS A O   1 
ATOM   105  C  CB  . LYS A 1 15 ? -5.196  -18.221 -0.392  1.00 34.78  ? 14  LYS A CB  1 
ATOM   106  C  CG  . LYS A 1 15 ? -6.274  -19.251 -0.011  1.00 42.28  ? 14  LYS A CG  1 
ATOM   107  C  CD  . LYS A 1 15 ? -5.887  -20.161 1.159   1.00 44.44  ? 14  LYS A CD  1 
ATOM   108  C  CE  . LYS A 1 15 ? -7.002  -21.021 1.710   1.00 42.18  ? 14  LYS A CE  1 
ATOM   109  N  NZ  . LYS A 1 15 ? -7.324  -22.107 0.774   1.00 41.35  ? 14  LYS A NZ  1 
ATOM   110  N  N   . MET A 1 16 ? -4.219  -20.882 -2.340  1.00 35.74  ? 15  MET A N   1 
ATOM   111  C  CA  . MET A 1 16 ? -4.740  -21.757 -3.379  1.00 38.17  ? 15  MET A CA  1 
ATOM   112  C  C   . MET A 1 16 ? -5.763  -22.685 -2.743  1.00 41.49  ? 15  MET A C   1 
ATOM   113  O  O   . MET A 1 16 ? -5.598  -23.093 -1.589  1.00 34.09  ? 15  MET A O   1 
ATOM   114  C  CB  . MET A 1 16 ? -3.672  -22.738 -3.854  1.00 39.33  ? 15  MET A CB  1 
ATOM   115  C  CG  . MET A 1 16 ? -2.337  -22.083 -4.135  1.00 46.81  ? 15  MET A CG  1 
ATOM   116  S  SD  . MET A 1 16 ? -2.337  -21.783 -5.911  1.00 49.59  ? 15  MET A SD  1 
ATOM   117  C  CE  . MET A 1 16 ? -1.487  -23.280 -6.416  1.00 45.61  ? 15  MET A CE  1 
ATOM   118  N  N   . LYS A 1 17 ? -6.759  -23.047 -3.557  1.00 46.05  ? 16  LYS A N   1 
ATOM   119  C  CA  . LYS A 1 17 ? -7.863  -23.917 -3.188  1.00 50.68  ? 16  LYS A CA  1 
ATOM   120  C  C   . LYS A 1 17 ? -7.311  -25.211 -2.610  1.00 51.60  ? 16  LYS A C   1 
ATOM   121  O  O   . LYS A 1 17 ? -6.447  -25.841 -3.214  1.00 47.35  ? 16  LYS A O   1 
ATOM   122  C  CB  . LYS A 1 17 ? -8.654  -24.286 -4.447  1.00 55.19  ? 16  LYS A CB  1 
ATOM   123  C  CG  . LYS A 1 17 ? -10.078 -24.752 -4.185  1.00 66.38  ? 16  LYS A CG  1 
ATOM   124  C  CD  . LYS A 1 17 ? -11.074 -23.598 -4.156  1.00 73.81  ? 16  LYS A CD  1 
ATOM   125  C  CE  . LYS A 1 17 ? -11.403 -23.163 -5.554  1.00 74.45  ? 16  LYS A CE  1 
ATOM   126  N  NZ  . LYS A 1 17 ? -12.204 -21.938 -5.584  1.00 82.31  ? 16  LYS A NZ  1 
ATOM   127  N  N   . GLY A 1 18 ? -7.801  -25.567 -1.419  1.00 44.64  ? 17  GLY A N   1 
ATOM   128  C  CA  . GLY A 1 18 ? -7.427  -26.827 -0.802  1.00 48.02  ? 17  GLY A CA  1 
ATOM   129  C  C   . GLY A 1 18 ? -6.063  -26.780 -0.118  1.00 53.61  ? 17  GLY A C   1 
ATOM   130  O  O   . GLY A 1 18 ? -5.608  -27.806 0.381   1.00 55.15  ? 17  GLY A O   1 
ATOM   131  N  N   . TYR A 1 19 ? -5.411  -25.609 -0.081  1.00 44.51  ? 18  TYR A N   1 
ATOM   132  C  CA  . TYR A 1 19 ? -4.154  -25.513 0.646   1.00 43.40  ? 18  TYR A CA  1 
ATOM   133  C  C   . TYR A 1 19 ? -4.241  -24.425 1.704   1.00 39.95  ? 18  TYR A C   1 
ATOM   134  O  O   . TYR A 1 19 ? -4.914  -23.428 1.494   1.00 39.05  ? 18  TYR A O   1 
ATOM   135  C  CB  . TYR A 1 19 ? -2.984  -25.132 -0.263  1.00 47.00  ? 18  TYR A CB  1 
ATOM   136  C  CG  . TYR A 1 19 ? -2.604  -26.236 -1.235  1.00 50.01  ? 18  TYR A CG  1 
ATOM   137  C  CD1 . TYR A 1 19 ? -1.727  -27.246 -0.859  1.00 56.97  ? 18  TYR A CD1 1 
ATOM   138  C  CD2 . TYR A 1 19 ? -3.131  -26.265 -2.520  1.00 55.47  ? 18  TYR A CD2 1 
ATOM   139  C  CE1 . TYR A 1 19 ? -1.389  -28.262 -1.736  1.00 64.52  ? 18  TYR A CE1 1 
ATOM   140  C  CE2 . TYR A 1 19 ? -2.796  -27.273 -3.410  1.00 59.11  ? 18  TYR A CE2 1 
ATOM   141  C  CZ  . TYR A 1 19 ? -1.926  -28.275 -3.014  1.00 68.47  ? 18  TYR A CZ  1 
ATOM   142  O  OH  . TYR A 1 19 ? -1.603  -29.277 -3.887  1.00 79.03  ? 18  TYR A OH  1 
ATOM   143  N  N   . PRO A 1 20 ? -3.490  -24.532 2.826   1.00 37.88  ? 19  PRO A N   1 
ATOM   144  C  CA  . PRO A 1 20 ? -3.431  -23.443 3.799   1.00 39.51  ? 19  PRO A CA  1 
ATOM   145  C  C   . PRO A 1 20 ? -2.712  -22.260 3.131   1.00 35.21  ? 19  PRO A C   1 
ATOM   146  O  O   . PRO A 1 20 ? -1.985  -22.447 2.152   1.00 34.00  ? 19  PRO A O   1 
ATOM   147  C  CB  . PRO A 1 20 ? -2.653  -24.081 4.970   1.00 39.26  ? 19  PRO A CB  1 
ATOM   148  C  CG  . PRO A 1 20 ? -1.748  -25.094 4.314   1.00 39.62  ? 19  PRO A CG  1 
ATOM   149  C  CD  . PRO A 1 20 ? -2.576  -25.639 3.143   1.00 41.38  ? 19  PRO A CD  1 
ATOM   150  N  N   . HIS A 1 21 ? -2.955  -21.045 3.634   1.00 30.56  ? 20  HIS A N   1 
ATOM   151  C  CA  . HIS A 1 21 ? -2.198  -19.869 3.238   1.00 28.84  ? 20  HIS A CA  1 
ATOM   152  C  C   . HIS A 1 21 ? -0.700  -20.172 3.330   1.00 33.89  ? 20  HIS A C   1 
ATOM   153  O  O   . HIS A 1 21 ? -0.219  -20.574 4.391   1.00 31.14  ? 20  HIS A O   1 
ATOM   154  C  CB  . HIS A 1 21 ? -2.646  -18.629 4.026   1.00 27.08  ? 20  HIS A CB  1 
ATOM   155  C  CG  . HIS A 1 21 ? -4.107  -18.304 3.860   1.00 35.48  ? 20  HIS A CG  1 
ATOM   156  N  ND1 . HIS A 1 21 ? -5.109  -18.987 4.533   1.00 37.19  ? 20  HIS A ND1 1 
ATOM   157  C  CD2 . HIS A 1 21 ? -4.729  -17.334 3.155   1.00 32.38  ? 20  HIS A CD2 1 
ATOM   158  C  CE1 . HIS A 1 21 ? -6.298  -18.470 4.204   1.00 32.78  ? 20  HIS A CE1 1 
ATOM   159  N  NE2 . HIS A 1 21 ? -6.093  -17.453 3.381   1.00 36.30  ? 20  HIS A NE2 1 
ATOM   160  N  N   . TRP A 1 22 ? 0.037   -19.926 2.228   1.00 32.04  ? 21  TRP A N   1 
ATOM   161  C  CA  . TRP A 1 22 ? 1.360   -20.516 2.076   1.00 31.80  ? 21  TRP A CA  1 
ATOM   162  C  C   . TRP A 1 22 ? 2.433   -19.441 1.876   1.00 31.77  ? 21  TRP A C   1 
ATOM   163  O  O   . TRP A 1 22 ? 2.246   -18.518 1.096   1.00 31.26  ? 21  TRP A O   1 
ATOM   164  C  CB  . TRP A 1 22 ? 1.352   -21.516 0.911   1.00 32.42  ? 21  TRP A CB  1 
ATOM   165  C  CG  . TRP A 1 22 ? 2.448   -22.544 0.975   1.00 31.69  ? 21  TRP A CG  1 
ATOM   166  C  CD1 . TRP A 1 22 ? 3.776   -22.348 0.735   1.00 30.86  ? 21  TRP A CD1 1 
ATOM   167  C  CD2 . TRP A 1 22 ? 2.294   -23.950 1.263   1.00 32.12  ? 21  TRP A CD2 1 
ATOM   168  N  NE1 . TRP A 1 22 ? 4.463   -23.532 0.841   1.00 34.65  ? 21  TRP A NE1 1 
ATOM   169  C  CE2 . TRP A 1 22 ? 3.580   -24.533 1.163   1.00 37.13  ? 21  TRP A CE2 1 
ATOM   170  C  CE3 . TRP A 1 22 ? 1.203   -24.773 1.560   1.00 39.49  ? 21  TRP A CE3 1 
ATOM   171  C  CZ2 . TRP A 1 22 ? 3.801   -25.895 1.373   1.00 38.60  ? 21  TRP A CZ2 1 
ATOM   172  C  CZ3 . TRP A 1 22 ? 1.426   -26.124 1.757   1.00 40.00  ? 21  TRP A CZ3 1 
ATOM   173  C  CH2 . TRP A 1 22 ? 2.707   -26.674 1.678   1.00 40.67  ? 21  TRP A CH2 1 
ATOM   174  N  N   . PRO A 1 23 ? 3.582   -19.517 2.593   1.00 28.35  ? 22  PRO A N   1 
ATOM   175  C  CA  . PRO A 1 23 ? 4.638   -18.511 2.473   1.00 25.80  ? 22  PRO A CA  1 
ATOM   176  C  C   . PRO A 1 23 ? 5.125   -18.523 1.029   1.00 25.51  ? 22  PRO A C   1 
ATOM   177  O  O   . PRO A 1 23 ? 5.345   -19.598 0.471   1.00 27.89  ? 22  PRO A O   1 
ATOM   178  C  CB  . PRO A 1 23 ? 5.714   -18.966 3.492   1.00 25.67  ? 22  PRO A CB  1 
ATOM   179  C  CG  . PRO A 1 23 ? 5.451   -20.459 3.644   1.00 24.93  ? 22  PRO A CG  1 
ATOM   180  C  CD  . PRO A 1 23 ? 3.909   -20.556 3.570   1.00 25.49  ? 22  PRO A CD  1 
ATOM   181  N  N   . ALA A 1 24 ? 5.195   -17.325 0.428   1.00 23.07  ? 23  ALA A N   1 
ATOM   182  C  CA  . ALA A 1 24 ? 5.505   -17.165 -0.990  1.00 25.46  ? 23  ALA A CA  1 
ATOM   183  C  C   . ALA A 1 24 ? 6.084   -15.780 -1.296  1.00 24.51  ? 23  ALA A C   1 
ATOM   184  O  O   . ALA A 1 24 ? 6.134   -14.897 -0.451  1.00 26.27  ? 23  ALA A O   1 
ATOM   185  C  CB  . ALA A 1 24 ? 4.231   -17.413 -1.805  1.00 25.03  ? 23  ALA A CB  1 
ATOM   186  N  N   . ARG A 1 25 ? 6.563   -15.588 -2.541  1.00 25.92  ? 24  ARG A N   1 
ATOM   187  C  CA  . ARG A 1 25 ? 7.003   -14.274 -2.958  1.00 23.52  ? 24  ARG A CA  1 
ATOM   188  C  C   . ARG A 1 25 ? 6.486   -14.017 -4.376  1.00 23.25  ? 24  ARG A C   1 
ATOM   189  O  O   . ARG A 1 25 ? 6.174   -14.960 -5.098  1.00 24.60  ? 24  ARG A O   1 
ATOM   190  C  CB  . ARG A 1 25 ? 8.533   -14.154 -2.847  1.00 22.99  ? 24  ARG A CB  1 
ATOM   191  C  CG  . ARG A 1 25 ? 9.207   -15.052 -3.881  1.00 23.15  ? 24  ARG A CG  1 
ATOM   192  C  CD  . ARG A 1 25 ? 10.739  -14.881 -3.775  1.00 24.22  ? 24  ARG A CD  1 
ATOM   193  N  NE  . ARG A 1 25 ? 11.461  -15.708 -4.756  1.00 25.16  ? 24  ARG A NE  1 
ATOM   194  C  CZ  . ARG A 1 25 ? 12.712  -16.165 -4.667  1.00 30.26  ? 24  ARG A CZ  1 
ATOM   195  N  NH1 . ARG A 1 25 ? 13.467  -15.979 -3.591  1.00 27.05  ? 24  ARG A NH1 1 
ATOM   196  N  NH2 . ARG A 1 25 ? 13.201  -16.854 -5.680  1.00 33.39  ? 24  ARG A NH2 1 
ATOM   197  N  N   . ILE A 1 26 ? 6.334   -12.737 -4.726  1.00 24.12  ? 25  ILE A N   1 
ATOM   198  C  CA  . ILE A 1 26 ? 6.114   -12.346 -6.112  1.00 24.40  ? 25  ILE A CA  1 
ATOM   199  C  C   . ILE A 1 26 ? 7.468   -12.446 -6.826  1.00 28.24  ? 25  ILE A C   1 
ATOM   200  O  O   . ILE A 1 26 ? 8.425   -11.784 -6.416  1.00 26.84  ? 25  ILE A O   1 
ATOM   201  C  CB  . ILE A 1 26 ? 5.623   -10.885 -6.210  1.00 30.69  ? 25  ILE A CB  1 
ATOM   202  C  CG1 . ILE A 1 26 ? 4.424   -10.548 -5.268  1.00 34.14  ? 25  ILE A CG1 1 
ATOM   203  C  CG2 . ILE A 1 26 ? 5.340   -10.535 -7.677  1.00 26.98  ? 25  ILE A CG2 1 
ATOM   204  C  CD1 . ILE A 1 26 ? 3.061   -10.880 -5.803  1.00 35.24  ? 25  ILE A CD1 1 
ATOM   205  N  N   . ASP A 1 27 ? 7.525   -13.263 -7.880  1.00 26.90  ? 26  ASP A N   1 
ATOM   206  C  CA  . ASP A 1 27 ? 8.745   -13.443 -8.657  1.00 31.69  ? 26  ASP A CA  1 
ATOM   207  C  C   . ASP A 1 27 ? 8.835   -12.440 -9.799  1.00 32.81  ? 26  ASP A C   1 
ATOM   208  O  O   . ASP A 1 27 ? 7.840   -11.821 -10.206 1.00 30.03  ? 26  ASP A O   1 
ATOM   209  C  CB  . ASP A 1 27 ? 8.867   -14.845 -9.229  1.00 31.99  ? 26  ASP A CB  1 
ATOM   210  C  CG  . ASP A 1 27 ? 9.812   -15.785 -8.502  1.00 32.62  ? 26  ASP A CG  1 
ATOM   211  O  OD1 . ASP A 1 27 ? 10.379  -15.390 -7.469  1.00 38.42  ? 26  ASP A OD1 1 
ATOM   212  O  OD2 . ASP A 1 27 ? 9.944   -16.925 -8.951  1.00 34.82  ? 26  ASP A OD2 1 
ATOM   213  N  N   . ASP A 1 28 ? 10.076  -12.281 -10.281 1.00 32.35  ? 27  ASP A N   1 
ATOM   214  C  CA  . ASP A 1 28 ? 10.377  -11.644 -11.546 1.00 38.71  ? 27  ASP A CA  1 
ATOM   215  C  C   . ASP A 1 28 ? 10.067  -12.657 -12.644 1.00 31.75  ? 27  ASP A C   1 
ATOM   216  O  O   . ASP A 1 28 ? 9.981   -13.853 -12.382 1.00 36.09  ? 27  ASP A O   1 
ATOM   217  C  CB  . ASP A 1 28 ? 11.860  -11.307 -11.625 1.00 46.08  ? 27  ASP A CB  1 
ATOM   218  C  CG  . ASP A 1 28 ? 12.362  -10.201 -10.698 1.00 56.00  ? 27  ASP A CG  1 
ATOM   219  O  OD1 . ASP A 1 28 ? 12.080  -9.009  -10.986 1.00 53.96  ? 27  ASP A OD1 1 
ATOM   220  O  OD2 . ASP A 1 28 ? 13.042  -10.534 -9.698  1.00 61.92  ? 27  ASP A OD2 1 
ATOM   221  N  N   . ILE A 1 29 ? 9.853   -12.171 -13.867 1.00 37.80  ? 28  ILE A N   1 
ATOM   222  C  CA  . ILE A 1 29 ? 9.845   -13.036 -15.036 1.00 36.18  ? 28  ILE A CA  1 
ATOM   223  C  C   . ILE A 1 29 ? 11.225  -12.873 -15.673 1.00 37.99  ? 28  ILE A C   1 
ATOM   224  O  O   . ILE A 1 29 ? 11.609  -11.740 -15.957 1.00 34.61  ? 28  ILE A O   1 
ATOM   225  C  CB  . ILE A 1 29 ? 8.742   -12.536 -15.982 1.00 40.85  ? 28  ILE A CB  1 
ATOM   226  C  CG1 . ILE A 1 29 ? 7.389   -12.450 -15.240 1.00 38.86  ? 28  ILE A CG1 1 
ATOM   227  C  CG2 . ILE A 1 29 ? 8.670   -13.403 -17.247 1.00 35.10  ? 28  ILE A CG2 1 
ATOM   228  C  CD1 . ILE A 1 29 ? 6.487   -11.310 -15.682 1.00 38.30  ? 28  ILE A CD1 1 
ATOM   229  N  N   . ALA A 1 30 ? 11.985  -13.969 -15.821 1.00 33.57  ? 29  ALA A N   1 
ATOM   230  C  CA  . ALA A 1 30 ? 13.298  -13.890 -16.450 1.00 35.67  ? 29  ALA A CA  1 
ATOM   231  C  C   . ALA A 1 30 ? 13.121  -13.577 -17.942 1.00 34.53  ? 29  ALA A C   1 
ATOM   232  O  O   . ALA A 1 30 ? 12.100  -13.892 -18.546 1.00 31.68  ? 29  ALA A O   1 
ATOM   233  C  CB  . ALA A 1 30 ? 14.044  -15.196 -16.255 1.00 39.03  ? 29  ALA A CB  1 
ATOM   234  N  N   . ASP A 1 31 ? 14.090  -12.858 -18.508 1.00 38.05  ? 30  ASP A N   1 
ATOM   235  C  CA  . ASP A 1 31 ? 14.195  -12.709 -19.953 1.00 34.68  ? 30  ASP A CA  1 
ATOM   236  C  C   . ASP A 1 31 ? 13.989  -14.072 -20.587 1.00 29.23  ? 30  ASP A C   1 
ATOM   237  O  O   . ASP A 1 31 ? 14.647  -15.011 -20.178 1.00 31.09  ? 30  ASP A O   1 
ATOM   238  C  CB  . ASP A 1 31 ? 15.586  -12.199 -20.274 1.00 34.45  ? 30  ASP A CB  1 
ATOM   239  C  CG  . ASP A 1 31 ? 15.703  -10.691 -20.127 1.00 35.38  ? 30  ASP A CG  1 
ATOM   240  O  OD1 . ASP A 1 31 ? 14.659  -10.035 -20.134 1.00 37.48  ? 30  ASP A OD1 1 
ATOM   241  O  OD2 . ASP A 1 31 ? 16.828  -10.202 -20.061 1.00 36.82  ? 30  ASP A OD2 1 
ATOM   242  N  N   . GLY A 1 32 ? 13.060  -14.163 -21.552 1.00 35.63  ? 31  GLY A N   1 
ATOM   243  C  CA  . GLY A 1 32 ? 12.874  -15.363 -22.351 1.00 32.05  ? 31  GLY A CA  1 
ATOM   244  C  C   . GLY A 1 32 ? 11.943  -16.385 -21.702 1.00 37.82  ? 31  GLY A C   1 
ATOM   245  O  O   . GLY A 1 32 ? 11.671  -17.425 -22.300 1.00 37.33  ? 31  GLY A O   1 
ATOM   246  N  N   . ALA A 1 33 ? 11.513  -16.116 -20.457 1.00 34.80  ? 32  ALA A N   1 
ATOM   247  C  CA  . ALA A 1 33 ? 10.665  -17.040 -19.708 1.00 38.80  ? 32  ALA A CA  1 
ATOM   248  C  C   . ALA A 1 33 ? 9.186   -16.792 -20.008 1.00 34.08  ? 32  ALA A C   1 
ATOM   249  O  O   . ALA A 1 33 ? 8.800   -15.719 -20.452 1.00 35.13  ? 32  ALA A O   1 
ATOM   250  C  CB  . ALA A 1 33 ? 10.952  -16.939 -18.209 1.00 35.64  ? 32  ALA A CB  1 
ATOM   251  N  N   . VAL A 1 34 ? 8.356   -17.796 -19.715 1.00 40.61  ? 33  VAL A N   1 
ATOM   252  C  CA  . VAL A 1 34 ? 6.903   -17.726 -19.861 1.00 39.47  ? 33  VAL A CA  1 
ATOM   253  C  C   . VAL A 1 34 ? 6.319   -16.651 -18.939 1.00 39.83  ? 33  VAL A C   1 
ATOM   254  O  O   . VAL A 1 34 ? 6.588   -16.630 -17.735 1.00 39.71  ? 33  VAL A O   1 
ATOM   255  C  CB  . VAL A 1 34 ? 6.318   -19.132 -19.582 1.00 42.90  ? 33  VAL A CB  1 
ATOM   256  C  CG1 . VAL A 1 34 ? 4.792   -19.129 -19.509 1.00 43.52  ? 33  VAL A CG1 1 
ATOM   257  C  CG2 . VAL A 1 34 ? 6.788   -20.151 -20.624 1.00 41.96  ? 33  VAL A CG2 1 
ATOM   258  N  N   . LYS A 1 35 ? 5.521   -15.750 -19.526 1.00 38.73  ? 34  LYS A N   1 
ATOM   259  C  CA  . LYS A 1 35 ? 4.860   -14.657 -18.822 1.00 40.60  ? 34  LYS A CA  1 
ATOM   260  C  C   . LYS A 1 35 ? 3.543   -15.152 -18.233 1.00 43.86  ? 34  LYS A C   1 
ATOM   261  O  O   . LYS A 1 35 ? 2.978   -16.110 -18.749 1.00 34.99  ? 34  LYS A O   1 
ATOM   262  C  CB  . LYS A 1 35 ? 4.521   -13.482 -19.745 1.00 40.82  ? 34  LYS A CB  1 
ATOM   263  C  CG  . LYS A 1 35 ? 5.765   -12.734 -20.267 1.00 39.09  ? 34  LYS A CG  1 
ATOM   264  C  CD  . LYS A 1 35 ? 5.416   -11.557 -21.168 1.00 43.47  ? 34  LYS A CD  1 
ATOM   265  C  CE  . LYS A 1 35 ? 4.890   -11.953 -22.512 1.00 46.27  ? 34  LYS A CE  1 
ATOM   266  N  NZ  . LYS A 1 35 ? 4.789   -10.722 -23.289 1.00 47.18  ? 34  LYS A NZ  1 
ATOM   267  N  N   . PRO A 1 36 ? 3.029   -14.525 -17.144 1.00 42.67  ? 35  PRO A N   1 
ATOM   268  C  CA  . PRO A 1 36 ? 1.727   -14.881 -16.571 1.00 40.21  ? 35  PRO A CA  1 
ATOM   269  C  C   . PRO A 1 36 ? 0.608   -14.387 -17.473 1.00 38.41  ? 35  PRO A C   1 
ATOM   270  O  O   . PRO A 1 36 ? 0.816   -13.501 -18.294 1.00 40.07  ? 35  PRO A O   1 
ATOM   271  C  CB  . PRO A 1 36 ? 1.668   -14.176 -15.191 1.00 38.94  ? 35  PRO A CB  1 
ATOM   272  C  CG  . PRO A 1 36 ? 3.061   -13.579 -14.976 1.00 39.97  ? 35  PRO A CG  1 
ATOM   273  C  CD  . PRO A 1 36 ? 3.687   -13.462 -16.376 1.00 42.63  ? 35  PRO A CD  1 
ATOM   274  N  N   . PRO A 1 37 ? -0.629  -14.901 -17.313 1.00 40.60  ? 36  PRO A N   1 
ATOM   275  C  CA  . PRO A 1 37 ? -1.804  -14.263 -17.910 1.00 39.97  ? 36  PRO A CA  1 
ATOM   276  C  C   . PRO A 1 37 ? -1.973  -12.852 -17.372 1.00 45.01  ? 36  PRO A C   1 
ATOM   277  O  O   . PRO A 1 37 ? -1.418  -12.513 -16.318 1.00 40.66  ? 36  PRO A O   1 
ATOM   278  C  CB  . PRO A 1 37 ? -2.978  -15.146 -17.486 1.00 39.43  ? 36  PRO A CB  1 
ATOM   279  C  CG  . PRO A 1 37 ? -2.350  -16.448 -17.115 1.00 38.83  ? 36  PRO A CG  1 
ATOM   280  C  CD  . PRO A 1 37 ? -0.951  -16.151 -16.606 1.00 41.21  ? 36  PRO A CD  1 
ATOM   281  N  N   . PRO A 1 38 ? -2.744  -12.000 -18.086 1.00 45.30  ? 37  PRO A N   1 
ATOM   282  C  CA  . PRO A 1 38 ? -3.060  -10.648 -17.619 1.00 46.89  ? 37  PRO A CA  1 
ATOM   283  C  C   . PRO A 1 38 ? -3.712  -10.676 -16.239 1.00 43.47  ? 37  PRO A C   1 
ATOM   284  O  O   . PRO A 1 38 ? -4.468  -11.580 -15.911 1.00 48.29  ? 37  PRO A O   1 
ATOM   285  C  CB  . PRO A 1 38 ? -4.024  -10.101 -18.692 1.00 48.39  ? 37  PRO A CB  1 
ATOM   286  C  CG  . PRO A 1 38 ? -4.490  -11.318 -19.459 1.00 40.84  ? 37  PRO A CG  1 
ATOM   287  C  CD  . PRO A 1 38 ? -3.339  -12.297 -19.402 1.00 51.96  ? 37  PRO A CD  1 
ATOM   288  N  N   . ASN A 1 39 ? -3.375  -9.683  -15.426 1.00 43.85  ? 38  ASN A N   1 
ATOM   289  C  CA  . ASN A 1 39 ? -3.912  -9.569  -14.083 1.00 46.87  ? 38  ASN A CA  1 
ATOM   290  C  C   . ASN A 1 39 ? -3.362  -10.636 -13.130 1.00 44.08  ? 38  ASN A C   1 
ATOM   291  O  O   . ASN A 1 39 ? -3.773  -10.639 -11.971 1.00 43.07  ? 38  ASN A O   1 
ATOM   292  C  CB  . ASN A 1 39 ? -5.425  -9.363  -14.115 1.00 51.03  ? 38  ASN A CB  1 
ATOM   293  C  CG  . ASN A 1 39 ? -5.773  -8.066  -14.809 1.00 53.06  ? 38  ASN A CG  1 
ATOM   294  O  OD1 . ASN A 1 39 ? -5.538  -6.986  -14.256 1.00 57.40  ? 38  ASN A OD1 1 
ATOM   295  N  ND2 . ASN A 1 39 ? -6.285  -8.149  -16.027 1.00 57.09  ? 38  ASN A ND2 1 
ATOM   296  N  N   . LYS A 1 40 ? -2.411  -11.485 -13.579 1.00 38.76  ? 39  LYS A N   1 
ATOM   297  C  CA  . LYS A 1 40 ? -1.825  -12.513 -12.720 1.00 31.98  ? 39  LYS A CA  1 
ATOM   298  C  C   . LYS A 1 40 ? -0.335  -12.241 -12.462 1.00 32.73  ? 39  LYS A C   1 
ATOM   299  O  O   . LYS A 1 40 ? 0.352   -11.656 -13.291 1.00 36.28  ? 39  LYS A O   1 
ATOM   300  C  CB  . LYS A 1 40 ? -2.072  -13.971 -13.133 1.00 35.05  ? 39  LYS A CB  1 
ATOM   301  C  CG  . LYS A 1 40 ? -3.523  -14.416 -13.423 1.00 39.46  ? 39  LYS A CG  1 
ATOM   302  C  CD  . LYS A 1 40 ? -4.550  -13.972 -12.385 1.00 41.12  ? 39  LYS A CD  1 
ATOM   303  C  CE  . LYS A 1 40 ? -5.997  -14.395 -12.612 1.00 42.48  ? 39  LYS A CE  1 
ATOM   304  N  NZ  . LYS A 1 40 ? -6.128  -15.853 -12.474 1.00 43.45  ? 39  LYS A NZ  1 
ATOM   305  N  N   . TYR A 1 41 ? 0.150   -12.665 -11.289 1.00 26.36  ? 40  TYR A N   1 
ATOM   306  C  CA  . TYR A 1 41 ? 1.538   -12.466 -10.877 1.00 26.24  ? 40  TYR A CA  1 
ATOM   307  C  C   . TYR A 1 41 ? 2.164   -13.844 -10.795 1.00 23.06  ? 40  TYR A C   1 
ATOM   308  O  O   . TYR A 1 41 ? 1.460   -14.790 -10.460 1.00 25.67  ? 40  TYR A O   1 
ATOM   309  C  CB  . TYR A 1 41 ? 1.686   -11.858 -9.472  1.00 24.51  ? 40  TYR A CB  1 
ATOM   310  C  CG  . TYR A 1 41 ? 1.246   -10.400 -9.442  1.00 30.08  ? 40  TYR A CG  1 
ATOM   311  C  CD1 . TYR A 1 41 ? -0.094  -10.070 -9.267  1.00 34.45  ? 40  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A 1 41 ? 2.143   -9.362  -9.629  1.00 31.11  ? 40  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A 1 41 ? -0.524  -8.754  -9.298  1.00 33.45  ? 40  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A 1 41 ? 1.732   -8.035  -9.659  1.00 35.97  ? 40  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A 1 41 ? 0.392   -7.736  -9.475  1.00 37.26  ? 40  TYR A CZ  1 
ATOM   316  O  OH  . TYR A 1 41 ? -0.077  -6.447  -9.497  1.00 39.76  ? 40  TYR A OH  1 
ATOM   317  N  N   . PRO A 1 42 ? 3.485   -14.000 -11.062 1.00 25.31  ? 41  PRO A N   1 
ATOM   318  C  CA  . PRO A 1 42 ? 4.146   -15.300 -10.928 1.00 22.86  ? 41  PRO A CA  1 
ATOM   319  C  C   . PRO A 1 42 ? 4.416   -15.481 -9.436  1.00 26.14  ? 41  PRO A C   1 
ATOM   320  O  O   . PRO A 1 42 ? 5.053   -14.629 -8.821  1.00 29.74  ? 41  PRO A O   1 
ATOM   321  C  CB  . PRO A 1 42 ? 5.436   -15.167 -11.742 1.00 24.76  ? 41  PRO A CB  1 
ATOM   322  C  CG  . PRO A 1 42 ? 5.638   -13.703 -11.936 1.00 27.13  ? 41  PRO A CG  1 
ATOM   323  C  CD  . PRO A 1 42 ? 4.385   -12.921 -11.501 1.00 26.77  ? 41  PRO A CD  1 
ATOM   324  N  N   . ILE A 1 43 ? 3.883   -16.549 -8.839  1.00 25.51  ? 42  ILE A N   1 
ATOM   325  C  CA  . ILE A 1 43 ? 4.051   -16.692 -7.390  1.00 24.49  ? 42  ILE A CA  1 
ATOM   326  C  C   . ILE A 1 43 ? 4.991   -17.853 -7.127  1.00 28.39  ? 42  ILE A C   1 
ATOM   327  O  O   . ILE A 1 43 ? 4.688   -18.976 -7.529  1.00 29.70  ? 42  ILE A O   1 
ATOM   328  C  CB  . ILE A 1 43 ? 2.710   -16.900 -6.659  1.00 23.94  ? 42  ILE A CB  1 
ATOM   329  C  CG1 . ILE A 1 43 ? 1.737   -15.778 -6.938  1.00 25.76  ? 42  ILE A CG1 1 
ATOM   330  C  CG2 . ILE A 1 43 ? 2.983   -17.051 -5.144  1.00 24.42  ? 42  ILE A CG2 1 
ATOM   331  C  CD1 . ILE A 1 43 ? 2.245   -14.377 -6.608  1.00 23.33  ? 42  ILE A CD1 1 
ATOM   332  N  N   . PHE A 1 44 ? 6.086   -17.594 -6.393  1.00 26.98  ? 43  PHE A N   1 
ATOM   333  C  CA  . PHE A 1 44 ? 6.992   -18.658 -6.008  1.00 27.44  ? 43  PHE A CA  1 
ATOM   334  C  C   . PHE A 1 44 ? 6.680   -19.082 -4.578  1.00 26.71  ? 43  PHE A C   1 
ATOM   335  O  O   . PHE A 1 44 ? 6.710   -18.266 -3.673  1.00 26.29  ? 43  PHE A O   1 
ATOM   336  C  CB  . PHE A 1 44 ? 8.456   -18.202 -6.123  1.00 26.62  ? 43  PHE A CB  1 
ATOM   337  C  CG  . PHE A 1 44 ? 9.490   -19.250 -5.714  1.00 30.58  ? 43  PHE A CG  1 
ATOM   338  C  CD1 . PHE A 1 44 ? 9.878   -20.257 -6.599  1.00 33.98  ? 43  PHE A CD1 1 
ATOM   339  C  CD2 . PHE A 1 44 ? 10.094  -19.220 -4.453  1.00 30.60  ? 43  PHE A CD2 1 
ATOM   340  C  CE1 . PHE A 1 44 ? 10.830  -21.201 -6.240  1.00 36.73  ? 43  PHE A CE1 1 
ATOM   341  C  CE2 . PHE A 1 44 ? 11.039  -20.182 -4.088  1.00 36.41  ? 43  PHE A CE2 1 
ATOM   342  C  CZ  . PHE A 1 44 ? 11.419  -21.160 -4.990  1.00 35.06  ? 43  PHE A CZ  1 
ATOM   343  N  N   . PHE A 1 45 ? 6.364   -20.372 -4.379  1.00 28.24  ? 44  PHE A N   1 
ATOM   344  C  CA  . PHE A 1 45 ? 5.952   -20.858 -3.070  1.00 26.60  ? 44  PHE A CA  1 
ATOM   345  C  C   . PHE A 1 45 ? 7.221   -21.358 -2.380  1.00 27.71  ? 44  PHE A C   1 
ATOM   346  O  O   . PHE A 1 45 ? 7.926   -22.241 -2.916  1.00 28.19  ? 44  PHE A O   1 
ATOM   347  C  CB  . PHE A 1 45 ? 4.913   -21.990 -3.235  1.00 30.89  ? 44  PHE A CB  1 
ATOM   348  C  CG  . PHE A 1 45 ? 3.531   -21.502 -3.674  1.00 28.43  ? 44  PHE A CG  1 
ATOM   349  C  CD1 . PHE A 1 45 ? 3.242   -21.261 -5.022  1.00 29.30  ? 44  PHE A CD1 1 
ATOM   350  C  CD2 . PHE A 1 45 ? 2.549   -21.221 -2.726  1.00 28.07  ? 44  PHE A CD2 1 
ATOM   351  C  CE1 . PHE A 1 45 ? 1.996   -20.758 -5.424  1.00 29.51  ? 44  PHE A CE1 1 
ATOM   352  C  CE2 . PHE A 1 45 ? 1.313   -20.732 -3.120  1.00 29.39  ? 44  PHE A CE2 1 
ATOM   353  C  CZ  . PHE A 1 45 ? 1.023   -20.522 -4.466  1.00 30.07  ? 44  PHE A CZ  1 
ATOM   354  N  N   . PHE A 1 46 ? 7.512   -20.804 -1.201  1.00 25.92  ? 45  PHE A N   1 
ATOM   355  C  CA  . PHE A 1 46 ? 8.646   -21.303 -0.432  1.00 31.73  ? 45  PHE A CA  1 
ATOM   356  C  C   . PHE A 1 46 ? 8.397   -22.750 0.006   1.00 28.96  ? 45  PHE A C   1 
ATOM   357  O  O   . PHE A 1 46 ? 7.250   -23.180 0.200   1.00 33.80  ? 45  PHE A O   1 
ATOM   358  C  CB  . PHE A 1 46 ? 8.963   -20.384 0.757   1.00 29.65  ? 45  PHE A CB  1 
ATOM   359  C  CG  . PHE A 1 46 ? 9.414   -18.983 0.354   1.00 23.22  ? 45  PHE A CG  1 
ATOM   360  C  CD1 . PHE A 1 46 ? 10.693  -18.768 -0.174  1.00 24.74  ? 45  PHE A CD1 1 
ATOM   361  C  CD2 . PHE A 1 46 ? 8.603   -17.880 0.591   1.00 24.78  ? 45  PHE A CD2 1 
ATOM   362  C  CE1 . PHE A 1 46 ? 11.104  -17.495 -0.535  1.00 24.88  ? 45  PHE A CE1 1 
ATOM   363  C  CE2 . PHE A 1 46 ? 9.024   -16.595 0.221   1.00 23.14  ? 45  PHE A CE2 1 
ATOM   364  C  CZ  . PHE A 1 46 ? 10.283  -16.403 -0.327  1.00 27.06  ? 45  PHE A CZ  1 
ATOM   365  N  N   . GLY A 1 47 ? 9.484   -23.516 0.151   1.00 28.93  ? 46  GLY A N   1 
ATOM   366  C  CA  . GLY A 1 47 ? 9.369   -24.874 0.655   1.00 30.84  ? 46  GLY A CA  1 
ATOM   367  C  C   . GLY A 1 47 ? 9.126   -25.877 -0.471  1.00 37.55  ? 46  GLY A C   1 
ATOM   368  O  O   . GLY A 1 47 ? 9.927   -26.780 -0.644  1.00 38.60  ? 46  GLY A O   1 
ATOM   369  N  N   . THR A 1 48 ? 8.036   -25.713 -1.234  1.00 34.23  ? 47  THR A N   1 
ATOM   370  C  CA  . THR A 1 48 ? 7.720   -26.618 -2.332  1.00 36.98  ? 47  THR A CA  1 
ATOM   371  C  C   . THR A 1 48 ? 8.540   -26.196 -3.545  1.00 36.06  ? 47  THR A C   1 
ATOM   372  O  O   . THR A 1 48 ? 8.905   -27.019 -4.388  1.00 37.32  ? 47  THR A O   1 
ATOM   373  C  CB  . THR A 1 48 ? 6.220   -26.608 -2.631  1.00 37.81  ? 47  THR A CB  1 
ATOM   374  O  OG1 . THR A 1 48 ? 5.929   -25.243 -2.903  1.00 38.76  ? 47  THR A OG1 1 
ATOM   375  C  CG2 . THR A 1 48 ? 5.366   -27.054 -1.463  1.00 39.90  ? 47  THR A CG2 1 
ATOM   376  N  N   . HIS A 1 49 ? 8.812   -24.889 -3.615  1.00 28.75  ? 48  HIS A N   1 
ATOM   377  C  CA  . HIS A 1 49 ? 9.545   -24.267 -4.706  1.00 31.13  ? 48  HIS A CA  1 
ATOM   378  C  C   . HIS A 1 49 ? 8.770   -24.318 -6.022  1.00 30.28  ? 48  HIS A C   1 
ATOM   379  O  O   . HIS A 1 49 ? 9.379   -24.179 -7.080  1.00 34.14  ? 48  HIS A O   1 
ATOM   380  C  CB  . HIS A 1 49 ? 10.991  -24.782 -4.820  1.00 32.16  ? 48  HIS A CB  1 
ATOM   381  C  CG  . HIS A 1 49 ? 11.708  -24.799 -3.518  1.00 34.59  ? 48  HIS A CG  1 
ATOM   382  N  ND1 . HIS A 1 49 ? 12.477  -25.862 -3.112  1.00 38.64  ? 48  HIS A ND1 1 
ATOM   383  C  CD2 . HIS A 1 49 ? 11.765  -23.893 -2.523  1.00 34.23  ? 48  HIS A CD2 1 
ATOM   384  C  CE1 . HIS A 1 49 ? 12.983  -25.605 -1.904  1.00 42.50  ? 48  HIS A CE1 1 
ATOM   385  N  NE2 . HIS A 1 49 ? 12.587  -24.398 -1.538  1.00 36.98  ? 48  HIS A NE2 1 
ATOM   386  N  N   . GLU A 1 50 ? 7.440   -24.465 -5.960  1.00 33.63  ? 49  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 50 ? 6.585   -24.461 -7.146  1.00 36.31  ? 49  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 50 ? 6.177   -23.025 -7.494  1.00 35.88  ? 49  GLU A C   1 
ATOM   389  O  O   . GLU A 1 50 ? 6.189   -22.166 -6.616  1.00 32.86  ? 49  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 50 ? 5.295   -25.223 -6.827  1.00 43.76  ? 49  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 50 ? 5.481   -26.719 -6.575  1.00 53.72  ? 49  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 50 ? 4.270   -27.421 -5.974  1.00 67.88  ? 49  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 50 ? 3.159   -26.835 -5.884  1.00 69.53  ? 49  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 50 ? 4.464   -28.584 -5.561  1.00 76.39  ? 49  GLU A OE2 1 
ATOM   395  N  N   . THR A 1 51 ? 5.875   -22.762 -8.779  1.00 28.44  ? 50  THR A N   1 
ATOM   396  C  CA  . THR A 1 51 ? 5.289   -21.506 -9.225  1.00 33.38  ? 50  THR A CA  1 
ATOM   397  C  C   . THR A 1 51 ? 3.824   -21.717 -9.597  1.00 32.88  ? 50  THR A C   1 
ATOM   398  O  O   . THR A 1 51 ? 3.475   -22.732 -10.199 1.00 40.45  ? 50  THR A O   1 
ATOM   399  C  CB  . THR A 1 51 ? 6.081   -20.908 -10.393 1.00 36.66  ? 50  THR A CB  1 
ATOM   400  O  OG1 . THR A 1 51 ? 7.367   -20.631 -9.837  1.00 34.31  ? 50  THR A OG1 1 
ATOM   401  C  CG2 . THR A 1 51 ? 5.454   -19.626 -10.929 1.00 35.69  ? 50  THR A CG2 1 
ATOM   402  N  N   . ALA A 1 52 ? 2.963   -20.761 -9.222  1.00 32.63  ? 51  ALA A N   1 
ATOM   403  C  CA  . ALA A 1 52 ? 1.634   -20.656 -9.809  1.00 29.62  ? 51  ALA A CA  1 
ATOM   404  C  C   . ALA A 1 52 ? 1.341   -19.186 -10.106 1.00 35.37  ? 51  ALA A C   1 
ATOM   405  O  O   . ALA A 1 52 ? 2.058   -18.300 -9.633  1.00 32.06  ? 51  ALA A O   1 
ATOM   406  C  CB  . ALA A 1 52 ? 0.562   -21.321 -8.937  1.00 32.02  ? 51  ALA A CB  1 
ATOM   407  N  N   . PHE A 1 53 ? 0.325   -18.951 -10.946 1.00 31.98  ? 52  PHE A N   1 
ATOM   408  C  CA  . PHE A 1 53 ? -0.067  -17.606 -11.338 1.00 31.75  ? 52  PHE A CA  1 
ATOM   409  C  C   . PHE A 1 53 ? -1.299  -17.253 -10.524 1.00 36.35  ? 52  PHE A C   1 
ATOM   410  O  O   . PHE A 1 53 ? -2.261  -18.009 -10.578 1.00 41.54  ? 52  PHE A O   1 
ATOM   411  C  CB  . PHE A 1 53 ? -0.367  -17.683 -12.846 1.00 28.45  ? 52  PHE A CB  1 
ATOM   412  C  CG  . PHE A 1 53 ? 0.868   -17.950 -13.702 1.00 35.68  ? 52  PHE A CG  1 
ATOM   413  C  CD1 . PHE A 1 53 ? 2.040   -17.211 -13.514 1.00 34.73  ? 52  PHE A CD1 1 
ATOM   414  C  CD2 . PHE A 1 53 ? 0.843   -18.910 -14.719 1.00 39.23  ? 52  PHE A CD2 1 
ATOM   415  C  CE1 . PHE A 1 53 ? 3.158   -17.444 -14.306 1.00 47.34  ? 52  PHE A CE1 1 
ATOM   416  C  CE2 . PHE A 1 53 ? 1.968   -19.135 -15.511 1.00 41.76  ? 52  PHE A CE2 1 
ATOM   417  C  CZ  . PHE A 1 53 ? 3.120   -18.412 -15.301 1.00 40.54  ? 52  PHE A CZ  1 
ATOM   418  N  N   . LEU A 1 54 ? -1.260  -16.139 -9.762  1.00 31.99  ? 53  LEU A N   1 
ATOM   419  C  CA  . LEU A 1 54 ? -2.382  -15.762 -8.916  1.00 31.07  ? 53  LEU A CA  1 
ATOM   420  C  C   . LEU A 1 54 ? -2.650  -14.264 -9.050  1.00 31.77  ? 53  LEU A C   1 
ATOM   421  O  O   . LEU A 1 54 ? -1.743  -13.496 -9.359  1.00 30.71  ? 53  LEU A O   1 
ATOM   422  C  CB  . LEU A 1 54 ? -2.091  -16.114 -7.448  1.00 29.91  ? 53  LEU A CB  1 
ATOM   423  C  CG  . LEU A 1 54 ? -1.956  -17.599 -7.105  1.00 32.88  ? 53  LEU A CG  1 
ATOM   424  C  CD1 . LEU A 1 54 ? -1.612  -17.706 -5.625  1.00 32.20  ? 53  LEU A CD1 1 
ATOM   425  C  CD2 . LEU A 1 54 ? -3.291  -18.266 -7.366  1.00 35.90  ? 53  LEU A CD2 1 
ATOM   426  N  N   . GLY A 1 55 ? -3.912  -13.870 -8.815  1.00 27.47  ? 54  GLY A N   1 
ATOM   427  C  CA  . GLY A 1 55 ? -4.292  -12.462 -8.744  1.00 25.06  ? 54  GLY A CA  1 
ATOM   428  C  C   . GLY A 1 55 ? -4.264  -12.000 -7.284  1.00 24.83  ? 54  GLY A C   1 
ATOM   429  O  O   . GLY A 1 55 ? -4.147  -12.824 -6.379  1.00 26.24  ? 54  GLY A O   1 
ATOM   430  N  N   . PRO A 1 56 ? -4.310  -10.675 -7.041  1.00 25.76  ? 55  PRO A N   1 
ATOM   431  C  CA  . PRO A 1 56 ? -4.254  -10.107 -5.692  1.00 27.86  ? 55  PRO A CA  1 
ATOM   432  C  C   . PRO A 1 56 ? -5.245  -10.646 -4.663  1.00 27.86  ? 55  PRO A C   1 
ATOM   433  O  O   . PRO A 1 56 ? -4.938  -10.678 -3.478  1.00 27.56  ? 55  PRO A O   1 
ATOM   434  C  CB  . PRO A 1 56 ? -4.472  -8.616  -5.995  1.00 25.84  ? 55  PRO A CB  1 
ATOM   435  C  CG  . PRO A 1 56 ? -3.823  -8.445  -7.349  1.00 29.87  ? 55  PRO A CG  1 
ATOM   436  C  CD  . PRO A 1 56 ? -4.359  -9.651  -8.096  1.00 28.14  ? 55  PRO A CD  1 
ATOM   437  N  N   . LYS A 1 57 ? -6.423  -11.107 -5.107  1.00 28.65  ? 56  LYS A N   1 
ATOM   438  C  CA  . LYS A 1 57 ? -7.401  -11.646 -4.162  1.00 33.28  ? 56  LYS A CA  1 
ATOM   439  C  C   . LYS A 1 57 ? -6.852  -12.811 -3.333  1.00 32.30  ? 56  LYS A C   1 
ATOM   440  O  O   . LYS A 1 57 ? -7.360  -13.071 -2.235  1.00 27.68  ? 56  LYS A O   1 
ATOM   441  C  CB  . LYS A 1 57 ? -8.702  -12.135 -4.815  1.00 35.50  ? 56  LYS A CB  1 
ATOM   442  C  CG  . LYS A 1 57 ? -8.596  -13.406 -5.646  1.00 36.70  ? 56  LYS A CG  1 
ATOM   443  C  CD  . LYS A 1 57 ? -9.867  -13.584 -6.484  1.00 45.67  ? 56  LYS A CD  1 
ATOM   444  C  CE  . LYS A 1 57 ? -9.823  -14.788 -7.348  1.00 48.40  ? 56  LYS A CE  1 
ATOM   445  N  NZ  . LYS A 1 57 ? -9.615  -15.960 -6.491  1.00 50.10  ? 56  LYS A NZ  1 
ATOM   446  N  N   . ASP A 1 58 ? -5.789  -13.470 -3.827  1.00 27.00  ? 57  ASP A N   1 
ATOM   447  C  CA  . ASP A 1 58 ? -5.206  -14.624 -3.172  1.00 26.69  ? 57  ASP A CA  1 
ATOM   448  C  C   . ASP A 1 58 ? -3.844  -14.324 -2.526  1.00 25.88  ? 57  ASP A C   1 
ATOM   449  O  O   . ASP A 1 58 ? -3.190  -15.257 -2.040  1.00 26.78  ? 57  ASP A O   1 
ATOM   450  C  CB  . ASP A 1 58 ? -5.158  -15.796 -4.141  1.00 28.78  ? 57  ASP A CB  1 
ATOM   451  C  CG  . ASP A 1 58 ? -6.523  -16.390 -4.478  1.00 36.51  ? 57  ASP A CG  1 
ATOM   452  O  OD1 . ASP A 1 58 ? -7.327  -16.527 -3.544  1.00 34.48  ? 57  ASP A OD1 1 
ATOM   453  O  OD2 . ASP A 1 58 ? -6.778  -16.673 -5.670  1.00 34.07  ? 57  ASP A OD2 1 
ATOM   454  N  N   . LEU A 1 59 ? -3.455  -13.035 -2.462  1.00 25.48  ? 58  LEU A N   1 
ATOM   455  C  CA  . LEU A 1 59 ? -2.131  -12.611 -1.993  1.00 25.54  ? 58  LEU A CA  1 
ATOM   456  C  C   . LEU A 1 59 ? -2.289  -11.778 -0.723  1.00 24.69  ? 58  LEU A C   1 
ATOM   457  O  O   . LEU A 1 59 ? -2.922  -10.722 -0.746  1.00 27.99  ? 58  LEU A O   1 
ATOM   458  C  CB  . LEU A 1 59 ? -1.420  -11.831 -3.104  1.00 25.72  ? 58  LEU A CB  1 
ATOM   459  C  CG  . LEU A 1 59 ? -1.337  -12.584 -4.432  1.00 24.04  ? 58  LEU A CG  1 
ATOM   460  C  CD1 . LEU A 1 59 ? -0.621  -11.791 -5.504  1.00 26.64  ? 58  LEU A CD1 1 
ATOM   461  C  CD2 . LEU A 1 59 ? -0.597  -13.924 -4.186  1.00 23.39  ? 58  LEU A CD2 1 
ATOM   462  N  N   . PHE A 1 60 ? -1.766  -12.294 0.396   1.00 25.49  ? 59  PHE A N   1 
ATOM   463  C  CA  . PHE A 1 60 ? -1.842  -11.593 1.674   1.00 26.29  ? 59  PHE A CA  1 
ATOM   464  C  C   . PHE A 1 60 ? -0.450  -11.123 2.082   1.00 25.01  ? 59  PHE A C   1 
ATOM   465  O  O   . PHE A 1 60 ? 0.430   -11.936 2.332   1.00 26.32  ? 59  PHE A O   1 
ATOM   466  C  CB  . PHE A 1 60 ? -2.331  -12.640 2.675   1.00 27.14  ? 59  PHE A CB  1 
ATOM   467  C  CG  . PHE A 1 60 ? -3.768  -13.060 2.416   1.00 28.72  ? 59  PHE A CG  1 
ATOM   468  C  CD1 . PHE A 1 60 ? -4.077  -13.934 1.380   1.00 26.04  ? 59  PHE A CD1 1 
ATOM   469  C  CD2 . PHE A 1 60 ? -4.804  -12.554 3.210   1.00 30.82  ? 59  PHE A CD2 1 
ATOM   470  C  CE1 . PHE A 1 60 ? -5.397  -14.318 1.150   1.00 33.55  ? 59  PHE A CE1 1 
ATOM   471  C  CE2 . PHE A 1 60 ? -6.129  -12.928 2.969   1.00 33.08  ? 59  PHE A CE2 1 
ATOM   472  C  CZ  . PHE A 1 60 ? -6.424  -13.825 1.963   1.00 29.65  ? 59  PHE A CZ  1 
ATOM   473  N  N   . PRO A 1 61 ? -0.197  -9.800  2.139   1.00 27.67  ? 60  PRO A N   1 
ATOM   474  C  CA  . PRO A 1 61 ? 1.114   -9.302  2.569   1.00 28.48  ? 60  PRO A CA  1 
ATOM   475  C  C   . PRO A 1 61 ? 1.648   -9.889  3.876   1.00 28.48  ? 60  PRO A C   1 
ATOM   476  O  O   . PRO A 1 61 ? 0.967   -9.937  4.897   1.00 27.02  ? 60  PRO A O   1 
ATOM   477  C  CB  . PRO A 1 61 ? 0.921   -7.752  2.606   1.00 29.55  ? 60  PRO A CB  1 
ATOM   478  C  CG  . PRO A 1 61 ? -0.194  -7.514  1.581   1.00 32.28  ? 60  PRO A CG  1 
ATOM   479  C  CD  . PRO A 1 61 ? -1.127  -8.733  1.748   1.00 29.42  ? 60  PRO A CD  1 
ATOM   480  N  N   . TYR A 1 62 ? 2.915   -10.327 3.821   1.00 29.43  ? 61  TYR A N   1 
ATOM   481  C  CA  . TYR A 1 62 ? 3.522   -11.169 4.836   1.00 29.76  ? 61  TYR A CA  1 
ATOM   482  C  C   . TYR A 1 62 ? 3.552   -10.463 6.191   1.00 29.54  ? 61  TYR A C   1 
ATOM   483  O  O   . TYR A 1 62 ? 3.138   -11.050 7.173   1.00 34.63  ? 61  TYR A O   1 
ATOM   484  C  CB  . TYR A 1 62 ? 4.942   -11.536 4.383   1.00 31.58  ? 61  TYR A CB  1 
ATOM   485  C  CG  . TYR A 1 62 ? 5.700   -12.301 5.452   1.00 31.04  ? 61  TYR A CG  1 
ATOM   486  C  CD1 . TYR A 1 62 ? 5.409   -13.642 5.689   1.00 32.84  ? 61  TYR A CD1 1 
ATOM   487  C  CD2 . TYR A 1 62 ? 6.747   -11.713 6.166   1.00 33.69  ? 61  TYR A CD2 1 
ATOM   488  C  CE1 . TYR A 1 62 ? 6.097   -14.373 6.644   1.00 34.06  ? 61  TYR A CE1 1 
ATOM   489  C  CE2 . TYR A 1 62 ? 7.463   -12.448 7.103   1.00 33.20  ? 61  TYR A CE2 1 
ATOM   490  C  CZ  . TYR A 1 62 ? 7.127   -13.770 7.348   1.00 37.86  ? 61  TYR A CZ  1 
ATOM   491  O  OH  . TYR A 1 62 ? 7.802   -14.527 8.264   1.00 41.19  ? 61  TYR A OH  1 
ATOM   492  N  N   . ASP A 1 63 ? 4.016   -9.214  6.241   1.00 32.21  ? 62  ASP A N   1 
ATOM   493  C  CA  . ASP A 1 63 ? 4.116   -8.498  7.512   1.00 39.06  ? 62  ASP A CA  1 
ATOM   494  C  C   . ASP A 1 63 ? 2.779   -8.471  8.261   1.00 38.28  ? 62  ASP A C   1 
ATOM   495  O  O   . ASP A 1 63 ? 2.714   -8.832  9.432   1.00 40.56  ? 62  ASP A O   1 
ATOM   496  C  CB  . ASP A 1 63 ? 4.777   -7.142  7.337   1.00 41.60  ? 62  ASP A CB  1 
ATOM   497  C  CG  . ASP A 1 63 ? 6.286   -7.198  7.136   1.00 58.72  ? 62  ASP A CG  1 
ATOM   498  O  OD1 . ASP A 1 63 ? 7.003   -7.555  8.099   1.00 69.75  ? 62  ASP A OD1 1 
ATOM   499  O  OD2 . ASP A 1 63 ? 6.737   -6.881  6.019   1.00 67.81  ? 62  ASP A OD2 1 
ATOM   500  N  N   . LYS A 1 64 ? 1.698   -8.119  7.560   1.00 39.80  ? 63  LYS A N   1 
ATOM   501  C  CA  . LYS A 1 64 ? 0.367   -8.030  8.152   1.00 37.74  ? 63  LYS A CA  1 
ATOM   502  C  C   . LYS A 1 64 ? -0.172  -9.399  8.574   1.00 37.27  ? 63  LYS A C   1 
ATOM   503  O  O   . LYS A 1 64 ? -0.905  -9.487  9.561   1.00 38.20  ? 63  LYS A O   1 
ATOM   504  C  CB  . LYS A 1 64 ? -0.586  -7.307  7.187   1.00 39.26  ? 63  LYS A CB  1 
ATOM   505  C  CG  . LYS A 1 64 ? -2.016  -7.137  7.707   1.00 40.09  ? 63  LYS A CG  1 
ATOM   506  C  CD  . LYS A 1 64 ? -2.884  -6.517  6.630   1.00 42.64  ? 63  LYS A CD  1 
ATOM   507  C  CE  . LYS A 1 64 ? -3.959  -5.663  7.213   1.00 44.55  ? 63  LYS A CE  1 
ATOM   508  N  NZ  . LYS A 1 64 ? -4.980  -6.404  7.947   1.00 43.46  ? 63  LYS A NZ  1 
ATOM   509  N  N   . SER A 1 65 ? 0.230   -10.472 7.880   1.00 34.12  ? 64  SER A N   1 
ATOM   510  C  CA  . SER A 1 65 ? -0.462  -11.755 7.950   1.00 34.10  ? 64  SER A CA  1 
ATOM   511  C  C   . SER A 1 65 ? 0.302   -12.815 8.735   1.00 34.36  ? 64  SER A C   1 
ATOM   512  O  O   . SER A 1 65 ? -0.242  -13.888 8.982   1.00 32.87  ? 64  SER A O   1 
ATOM   513  C  CB  . SER A 1 65 ? -0.739  -12.285 6.555   1.00 38.22  ? 64  SER A CB  1 
ATOM   514  O  OG  . SER A 1 65 ? -1.740  -11.484 5.960   1.00 47.34  ? 64  SER A OG  1 
ATOM   515  N  N   . LYS A 1 66 ? 1.560   -12.533 9.093   1.00 35.29  ? 65  LYS A N   1 
ATOM   516  C  CA  . LYS A 1 66 ? 2.410   -13.578 9.658   1.00 39.80  ? 65  LYS A CA  1 
ATOM   517  C  C   . LYS A 1 66 ? 1.877   -14.106 10.993  1.00 35.29  ? 65  LYS A C   1 
ATOM   518  O  O   . LYS A 1 66 ? 1.965   -15.310 11.257  1.00 35.04  ? 65  LYS A O   1 
ATOM   519  C  CB  . LYS A 1 66 ? 3.889   -13.182 9.716   1.00 42.67  ? 65  LYS A CB  1 
ATOM   520  C  CG  . LYS A 1 66 ? 4.226   -12.014 10.607  1.00 50.68  ? 65  LYS A CG  1 
ATOM   521  C  CD  . LYS A 1 66 ? 5.738   -11.829 10.644  1.00 59.68  ? 65  LYS A CD  1 
ATOM   522  C  CE  . LYS A 1 66 ? 6.152   -10.572 11.365  1.00 63.30  ? 65  LYS A CE  1 
ATOM   523  N  NZ  . LYS A 1 66 ? 5.926   -9.336  10.601  1.00 64.10  ? 65  LYS A NZ  1 
ATOM   524  N  N   A ASP A 1 67 ? 1.260   -13.225 11.791  0.50 37.96  ? 66  ASP A N   1 
ATOM   525  N  N   B ASP A 1 67 ? 1.313   -13.223 11.824  0.50 37.11  ? 66  ASP A N   1 
ATOM   526  C  CA  A ASP A 1 67 ? 0.763   -13.611 13.109  0.50 41.28  ? 66  ASP A CA  1 
ATOM   527  C  CA  B ASP A 1 67 ? 0.798   -13.701 13.101  0.50 39.05  ? 66  ASP A CA  1 
ATOM   528  C  C   A ASP A 1 67 ? -0.412  -14.584 13.011  0.50 40.79  ? 66  ASP A C   1 
ATOM   529  C  C   B ASP A 1 67 ? -0.226  -14.807 12.860  0.50 38.41  ? 66  ASP A C   1 
ATOM   530  O  O   A ASP A 1 67 ? -0.683  -15.327 13.948  0.50 43.52  ? 66  ASP A O   1 
ATOM   531  O  O   B ASP A 1 67 ? -0.185  -15.847 13.514  0.50 33.35  ? 66  ASP A O   1 
ATOM   532  C  CB  A ASP A 1 67 ? 0.509   -12.407 14.002  0.50 44.17  ? 66  ASP A CB  1 
ATOM   533  C  CB  B ASP A 1 67 ? 0.250   -12.595 13.987  0.50 42.22  ? 66  ASP A CB  1 
ATOM   534  C  CG  A ASP A 1 67 ? 1.762   -11.750 14.563  0.50 46.58  ? 66  ASP A CG  1 
ATOM   535  C  CG  B ASP A 1 67 ? -0.063  -13.036 15.411  0.50 44.42  ? 66  ASP A CG  1 
ATOM   536  O  OD1 A ASP A 1 67 ? 2.865   -12.305 14.342  0.50 43.45  ? 66  ASP A OD1 1 
ATOM   537  O  OD1 B ASP A 1 67 ? 0.900   -13.252 16.183  0.50 44.50  ? 66  ASP A OD1 1 
ATOM   538  O  OD2 A ASP A 1 67 ? 1.627   -10.680 15.200  0.50 48.72  ? 66  ASP A OD2 1 
ATOM   539  O  OD2 B ASP A 1 67 ? -1.263  -13.198 15.723  0.50 46.45  ? 66  ASP A OD2 1 
ATOM   540  N  N   . LYS A 1 68 ? -1.097  -14.604 11.863  1.00 41.00  ? 67  LYS A N   1 
ATOM   541  C  CA  . LYS A 1 68 ? -2.201  -15.526 11.649  1.00 40.10  ? 67  LYS A CA  1 
ATOM   542  C  C   . LYS A 1 68 ? -1.747  -16.801 10.945  1.00 38.77  ? 67  LYS A C   1 
ATOM   543  O  O   . LYS A 1 68 ? -2.221  -17.888 11.257  1.00 37.81  ? 67  LYS A O   1 
ATOM   544  C  CB  . LYS A 1 68 ? -3.276  -14.796 10.836  1.00 41.56  ? 67  LYS A CB  1 
ATOM   545  C  CG  . LYS A 1 68 ? -4.559  -15.540 10.595  1.00 46.10  ? 67  LYS A CG  1 
ATOM   546  C  CD  . LYS A 1 68 ? -5.620  -14.554 10.117  1.00 49.61  ? 67  LYS A CD  1 
ATOM   547  C  CE  . LYS A 1 68 ? -6.818  -15.239 9.537   1.00 59.23  ? 67  LYS A CE  1 
ATOM   548  N  NZ  . LYS A 1 68 ? -7.846  -14.297 9.081   1.00 55.89  ? 67  LYS A NZ  1 
ATOM   549  N  N   . TYR A 1 69 ? -0.869  -16.669 9.947   1.00 39.74  ? 68  TYR A N   1 
ATOM   550  C  CA  . TYR A 1 69 ? -0.696  -17.758 9.003   1.00 33.49  ? 68  TYR A CA  1 
ATOM   551  C  C   . TYR A 1 69 ? 0.677   -18.405 9.163   1.00 34.21  ? 68  TYR A C   1 
ATOM   552  O  O   . TYR A 1 69 ? 0.904   -19.462 8.581   1.00 35.65  ? 68  TYR A O   1 
ATOM   553  C  CB  . TYR A 1 69 ? -0.868  -17.291 7.549   1.00 32.21  ? 68  TYR A CB  1 
ATOM   554  C  CG  . TYR A 1 69 ? -2.266  -16.823 7.179   1.00 33.18  ? 68  TYR A CG  1 
ATOM   555  C  CD1 . TYR A 1 69 ? -3.407  -17.555 7.519   1.00 39.15  ? 68  TYR A CD1 1 
ATOM   556  C  CD2 . TYR A 1 69 ? -2.441  -15.650 6.446   1.00 38.87  ? 68  TYR A CD2 1 
ATOM   557  C  CE1 . TYR A 1 69 ? -4.679  -17.123 7.167   1.00 36.03  ? 68  TYR A CE1 1 
ATOM   558  C  CE2 . TYR A 1 69 ? -3.705  -15.223 6.061   1.00 38.64  ? 68  TYR A CE2 1 
ATOM   559  C  CZ  . TYR A 1 69 ? -4.822  -15.950 6.439   1.00 38.87  ? 68  TYR A CZ  1 
ATOM   560  O  OH  . TYR A 1 69 ? -6.047  -15.493 6.039   1.00 38.33  ? 68  TYR A OH  1 
ATOM   561  N  N   . GLY A 1 70 ? 1.562   -17.779 9.947   1.00 34.35  ? 69  GLY A N   1 
ATOM   562  C  CA  . GLY A 1 70 ? 2.965   -18.161 10.024  1.00 35.99  ? 69  GLY A CA  1 
ATOM   563  C  C   . GLY A 1 70 ? 3.223   -19.081 11.219  1.00 38.95  ? 69  GLY A C   1 
ATOM   564  O  O   . GLY A 1 70 ? 3.847   -18.686 12.189  1.00 44.39  ? 69  GLY A O   1 
ATOM   565  N  N   . LYS A 1 71 ? 2.719   -20.306 11.113  1.00 40.65  ? 70  LYS A N   1 
ATOM   566  C  CA  . LYS A 1 71 ? 2.713   -21.282 12.185  1.00 45.89  ? 70  LYS A CA  1 
ATOM   567  C  C   . LYS A 1 71 ? 2.894   -22.640 11.529  1.00 43.33  ? 70  LYS A C   1 
ATOM   568  O  O   . LYS A 1 71 ? 2.464   -22.820 10.392  1.00 39.80  ? 70  LYS A O   1 
ATOM   569  C  CB  . LYS A 1 71 ? 1.398   -21.271 12.980  1.00 44.81  ? 70  LYS A CB  1 
ATOM   570  C  CG  . LYS A 1 71 ? 1.255   -20.071 13.897  1.00 54.09  ? 70  LYS A CG  1 
ATOM   571  C  CD  . LYS A 1 71 ? -0.114  -19.869 14.535  1.00 63.85  ? 70  LYS A CD  1 
ATOM   572  C  CE  . LYS A 1 71 ? -0.077  -18.665 15.430  1.00 69.70  ? 70  LYS A CE  1 
ATOM   573  N  NZ  . LYS A 1 71 ? -1.388  -18.341 15.998  1.00 79.47  ? 70  LYS A NZ  1 
ATOM   574  N  N   . PRO A 1 72 ? 3.575   -23.604 12.193  1.00 42.77  ? 71  PRO A N   1 
ATOM   575  C  CA  . PRO A 1 72 ? 3.813   -24.919 11.595  1.00 41.78  ? 71  PRO A CA  1 
ATOM   576  C  C   . PRO A 1 72 ? 2.559   -25.582 11.051  1.00 39.60  ? 71  PRO A C   1 
ATOM   577  O  O   . PRO A 1 72 ? 1.486   -25.443 11.612  1.00 43.90  ? 71  PRO A O   1 
ATOM   578  C  CB  . PRO A 1 72 ? 4.423   -25.720 12.747  1.00 43.74  ? 71  PRO A CB  1 
ATOM   579  C  CG  . PRO A 1 72 ? 5.129   -24.667 13.565  1.00 45.89  ? 71  PRO A CG  1 
ATOM   580  C  CD  . PRO A 1 72 ? 4.220   -23.444 13.508  1.00 43.64  ? 71  PRO A CD  1 
ATOM   581  N  N   . ASN A 1 73 ? 2.731   -26.309 9.954   1.00 42.38  ? 72  ASN A N   1 
ATOM   582  C  CA  . ASN A 1 73 ? 1.639   -27.014 9.318   1.00 50.02  ? 72  ASN A CA  1 
ATOM   583  C  C   . ASN A 1 73 ? 2.160   -28.388 8.911   1.00 55.53  ? 72  ASN A C   1 
ATOM   584  O  O   . ASN A 1 73 ? 3.328   -28.530 8.545   1.00 56.06  ? 72  ASN A O   1 
ATOM   585  C  CB  . ASN A 1 73 ? 1.093   -26.150 8.187   1.00 52.27  ? 72  ASN A CB  1 
ATOM   586  C  CG  . ASN A 1 73 ? -0.225  -26.628 7.643   1.00 54.08  ? 72  ASN A CG  1 
ATOM   587  O  OD1 . ASN A 1 73 ? -0.243  -27.473 6.746   1.00 51.54  ? 72  ASN A OD1 1 
ATOM   588  N  ND2 . ASN A 1 73 ? -1.325  -26.050 8.107   1.00 60.25  ? 72  ASN A ND2 1 
ATOM   589  N  N   . LYS A 1 74 ? 1.280   -29.394 8.985   1.00 55.79  ? 73  LYS A N   1 
ATOM   590  C  CA  . LYS A 1 74 ? 1.627   -30.764 8.643   1.00 54.51  ? 73  LYS A CA  1 
ATOM   591  C  C   . LYS A 1 74 ? 2.092   -30.852 7.188   1.00 54.08  ? 73  LYS A C   1 
ATOM   592  O  O   . LYS A 1 74 ? 2.944   -31.677 6.856   1.00 49.06  ? 73  LYS A O   1 
ATOM   593  C  CB  . LYS A 1 74 ? 0.469   -31.693 9.035   1.00 56.47  ? 73  LYS A CB  1 
ATOM   594  C  CG  . LYS A 1 74 ? -0.718  -31.747 8.074   1.00 60.61  ? 73  LYS A CG  1 
ATOM   595  N  N   . ARG A 1 75 ? 1.564   -29.969 6.328   1.00 56.45  ? 74  ARG A N   1 
ATOM   596  C  CA  . ARG A 1 75 ? 1.694   -30.112 4.879   1.00 54.29  ? 74  ARG A CA  1 
ATOM   597  C  C   . ARG A 1 75 ? 3.158   -30.135 4.439   1.00 48.59  ? 74  ARG A C   1 
ATOM   598  O  O   . ARG A 1 75 ? 4.009   -29.487 5.057   1.00 45.22  ? 74  ARG A O   1 
ATOM   599  C  CB  . ARG A 1 75 ? 0.858   -29.072 4.124   1.00 51.40  ? 74  ARG A CB  1 
ATOM   600  C  CG  . ARG A 1 75 ? -0.625  -29.311 4.347   1.00 50.72  ? 74  ARG A CG  1 
ATOM   601  C  CD  . ARG A 1 75 ? -1.132  -30.442 3.464   1.00 49.49  ? 74  ARG A CD  1 
ATOM   602  N  NE  . ARG A 1 75 ? -2.080  -29.954 2.454   1.00 64.99  ? 74  ARG A NE  1 
ATOM   603  C  CZ  . ARG A 1 75 ? -3.271  -29.390 2.717   1.00 69.64  ? 74  ARG A CZ  1 
ATOM   604  N  NH1 . ARG A 1 75 ? -4.071  -29.058 1.715   1.00 60.00  ? 74  ARG A NH1 1 
ATOM   605  N  NH2 . ARG A 1 75 ? -3.675  -29.184 3.971   1.00 65.05  ? 74  ARG A NH2 1 
ATOM   606  N  N   . LYS A 1 76 ? 3.414   -30.884 3.355   1.00 44.50  ? 75  LYS A N   1 
ATOM   607  C  CA  . LYS A 1 76 ? 4.751   -31.126 2.837   1.00 48.63  ? 75  LYS A CA  1 
ATOM   608  C  C   . LYS A 1 76 ? 5.390   -29.820 2.374   1.00 43.86  ? 75  LYS A C   1 
ATOM   609  O  O   . LYS A 1 76 ? 4.880   -29.158 1.472   1.00 37.98  ? 75  LYS A O   1 
ATOM   610  C  CB  . LYS A 1 76 ? 4.721   -32.082 1.641   1.00 46.65  ? 75  LYS A CB  1 
ATOM   611  C  CG  . LYS A 1 76 ? 6.041   -32.293 0.919   1.00 50.38  ? 75  LYS A CG  1 
ATOM   612  C  CD  . LYS A 1 76 ? 6.030   -33.508 -0.008  1.00 53.14  ? 75  LYS A CD  1 
ATOM   613  C  CE  . LYS A 1 76 ? 7.405   -33.901 -0.481  1.00 50.11  ? 75  LYS A CE  1 
ATOM   614  N  N   . GLY A 1 77 ? 6.535   -29.483 2.978   1.00 44.41  ? 76  GLY A N   1 
ATOM   615  C  CA  . GLY A 1 77 ? 7.322   -28.362 2.505   1.00 40.06  ? 76  GLY A CA  1 
ATOM   616  C  C   . GLY A 1 77 ? 6.945   -27.063 3.211   1.00 39.79  ? 76  GLY A C   1 
ATOM   617  O  O   . GLY A 1 77 ? 7.666   -26.084 3.086   1.00 37.43  ? 76  GLY A O   1 
ATOM   618  N  N   . PHE A 1 78 ? 5.840   -27.059 3.969   1.00 35.86  ? 77  PHE A N   1 
ATOM   619  C  CA  . PHE A 1 78 ? 5.367   -25.827 4.577   1.00 35.93  ? 77  PHE A CA  1 
ATOM   620  C  C   . PHE A 1 78 ? 6.373   -25.238 5.572   1.00 37.08  ? 77  PHE A C   1 
ATOM   621  O  O   . PHE A 1 78 ? 6.564   -24.014 5.650   1.00 32.80  ? 77  PHE A O   1 
ATOM   622  C  CB  . PHE A 1 78 ? 4.046   -26.116 5.292   1.00 35.50  ? 77  PHE A CB  1 
ATOM   623  C  CG  . PHE A 1 78 ? 3.294   -24.849 5.668   1.00 34.62  ? 77  PHE A CG  1 
ATOM   624  C  CD1 . PHE A 1 78 ? 3.558   -24.190 6.868   1.00 34.17  ? 77  PHE A CD1 1 
ATOM   625  C  CD2 . PHE A 1 78 ? 2.305   -24.339 4.825   1.00 32.44  ? 77  PHE A CD2 1 
ATOM   626  C  CE1 . PHE A 1 78 ? 2.888   -23.018 7.196   1.00 36.03  ? 77  PHE A CE1 1 
ATOM   627  C  CE2 . PHE A 1 78 ? 1.649   -23.161 5.151   1.00 28.41  ? 77  PHE A CE2 1 
ATOM   628  C  CZ  . PHE A 1 78 ? 1.910   -22.525 6.351   1.00 32.07  ? 77  PHE A CZ  1 
ATOM   629  N  N   . ASN A 1 79 ? 6.942   -26.100 6.415   1.00 35.92  ? 78  ASN A N   1 
ATOM   630  C  CA  . ASN A 1 79 ? 7.797   -25.632 7.496   1.00 36.32  ? 78  ASN A CA  1 
ATOM   631  C  C   . ASN A 1 79 ? 9.136   -25.170 6.918   1.00 36.97  ? 78  ASN A C   1 
ATOM   632  O  O   . ASN A 1 79 ? 9.701   -24.163 7.360   1.00 33.96  ? 78  ASN A O   1 
ATOM   633  C  CB  . ASN A 1 79 ? 7.906   -26.668 8.608   1.00 37.31  ? 78  ASN A CB  1 
ATOM   634  C  CG  . ASN A 1 79 ? 6.587   -26.870 9.318   1.00 44.11  ? 78  ASN A CG  1 
ATOM   635  O  OD1 . ASN A 1 79 ? 5.734   -25.976 9.323   1.00 36.68  ? 78  ASN A OD1 1 
ATOM   636  N  ND2 . ASN A 1 79 ? 6.394   -28.036 9.922   1.00 36.82  ? 78  ASN A ND2 1 
ATOM   637  N  N   . GLU A 1 80 ? 9.632   -25.918 5.925   1.00 34.47  ? 79  GLU A N   1 
ATOM   638  C  CA  . GLU A 1 80 ? 10.764  -25.440 5.148   1.00 35.67  ? 79  GLU A CA  1 
ATOM   639  C  C   . GLU A 1 80 ? 10.442  -24.039 4.635   1.00 36.17  ? 79  GLU A C   1 
ATOM   640  O  O   . GLU A 1 80 ? 11.287  -23.147 4.705   1.00 29.85  ? 79  GLU A O   1 
ATOM   641  C  CB  . GLU A 1 80 ? 11.123  -26.329 3.964   1.00 36.80  ? 79  GLU A CB  1 
ATOM   642  C  CG  . GLU A 1 80 ? 12.392  -25.860 3.252   1.00 40.82  ? 79  GLU A CG  1 
ATOM   643  C  CD  . GLU A 1 80 ? 13.031  -26.889 2.340   1.00 49.00  ? 79  GLU A CD  1 
ATOM   644  O  OE1 . GLU A 1 80 ? 12.406  -27.938 2.108   1.00 52.41  ? 79  GLU A OE1 1 
ATOM   645  O  OE2 . GLU A 1 80 ? 14.161  -26.660 1.879   1.00 53.04  ? 79  GLU A OE2 1 
ATOM   646  N  N   . GLY A 1 81 ? 9.205   -23.869 4.145   1.00 35.48  ? 80  GLY A N   1 
ATOM   647  C  CA  . GLY A 1 81 ? 8.748   -22.605 3.580   1.00 32.73  ? 80  GLY A CA  1 
ATOM   648  C  C   . GLY A 1 81 ? 8.780   -21.457 4.583   1.00 27.99  ? 80  GLY A C   1 
ATOM   649  O  O   . GLY A 1 81 ? 9.169   -20.339 4.241   1.00 30.38  ? 80  GLY A O   1 
ATOM   650  N  N   . LEU A 1 82 ? 8.364   -21.723 5.822   1.00 26.19  ? 81  LEU A N   1 
ATOM   651  C  CA  . LEU A 1 82 ? 8.436   -20.718 6.872   1.00 29.91  ? 81  LEU A CA  1 
ATOM   652  C  C   . LEU A 1 82 ? 9.887   -20.296 7.125   1.00 28.55  ? 81  LEU A C   1 
ATOM   653  O  O   . LEU A 1 82 ? 10.166  -19.104 7.298   1.00 27.33  ? 81  LEU A O   1 
ATOM   654  C  CB  . LEU A 1 82 ? 7.740   -21.188 8.153   1.00 29.89  ? 81  LEU A CB  1 
ATOM   655  C  CG  . LEU A 1 82 ? 6.248   -21.522 8.031   1.00 32.31  ? 81  LEU A CG  1 
ATOM   656  C  CD1 . LEU A 1 82 ? 5.804   -22.170 9.359   1.00 31.36  ? 81  LEU A CD1 1 
ATOM   657  C  CD2 . LEU A 1 82 ? 5.416   -20.270 7.790   1.00 32.49  ? 81  LEU A CD2 1 
ATOM   658  N  N   . TRP A 1 83 ? 10.823  -21.260 7.125   1.00 29.21  ? 82  TRP A N   1 
ATOM   659  C  CA  . TRP A 1 83 ? 12.223  -20.910 7.354   1.00 32.51  ? 82  TRP A CA  1 
ATOM   660  C  C   . TRP A 1 83 ? 12.704  -19.991 6.227   1.00 31.22  ? 82  TRP A C   1 
ATOM   661  O  O   . TRP A 1 83 ? 13.368  -18.985 6.470   1.00 28.70  ? 82  TRP A O   1 
ATOM   662  C  CB  . TRP A 1 83 ? 13.130  -22.154 7.493   1.00 31.44  ? 82  TRP A CB  1 
ATOM   663  C  CG  . TRP A 1 83 ? 14.579  -21.785 7.726   1.00 31.35  ? 82  TRP A CG  1 
ATOM   664  C  CD1 . TRP A 1 83 ? 15.200  -21.610 8.934   1.00 30.67  ? 82  TRP A CD1 1 
ATOM   665  C  CD2 . TRP A 1 83 ? 15.559  -21.478 6.718   1.00 27.91  ? 82  TRP A CD2 1 
ATOM   666  N  NE1 . TRP A 1 83 ? 16.502  -21.245 8.750   1.00 32.58  ? 82  TRP A NE1 1 
ATOM   667  C  CE2 . TRP A 1 83 ? 16.744  -21.133 7.397   1.00 31.94  ? 82  TRP A CE2 1 
ATOM   668  C  CE3 . TRP A 1 83 ? 15.534  -21.450 5.314   1.00 28.49  ? 82  TRP A CE3 1 
ATOM   669  C  CZ2 . TRP A 1 83 ? 17.907  -20.770 6.712   1.00 28.71  ? 82  TRP A CZ2 1 
ATOM   670  C  CZ3 . TRP A 1 83 ? 16.673  -21.072 4.636   1.00 33.38  ? 82  TRP A CZ3 1 
ATOM   671  C  CH2 . TRP A 1 83 ? 17.847  -20.741 5.336   1.00 32.67  ? 82  TRP A CH2 1 
ATOM   672  N  N   . GLU A 1 84 ? 12.311  -20.309 4.984   1.00 29.41  ? 83  GLU A N   1 
ATOM   673  C  CA  . GLU A 1 84 ? 12.864  -19.585 3.848   1.00 26.17  ? 83  GLU A CA  1 
ATOM   674  C  C   . GLU A 1 84 ? 12.379  -18.134 3.846   1.00 28.48  ? 83  GLU A C   1 
ATOM   675  O  O   . GLU A 1 84 ? 13.156  -17.217 3.612   1.00 25.37  ? 83  GLU A O   1 
ATOM   676  C  CB  . GLU A 1 84 ? 12.494  -20.274 2.542   1.00 27.25  ? 83  GLU A CB  1 
ATOM   677  C  CG  . GLU A 1 84 ? 13.234  -21.593 2.319   1.00 28.42  ? 83  GLU A CG  1 
ATOM   678  C  CD  . GLU A 1 84 ? 12.787  -22.334 1.071   1.00 32.22  ? 83  GLU A CD  1 
ATOM   679  O  OE1 . GLU A 1 84 ? 11.822  -21.874 0.412   1.00 31.29  ? 83  GLU A OE1 1 
ATOM   680  O  OE2 . GLU A 1 84 ? 13.340  -23.443 0.825   1.00 32.35  ? 83  GLU A OE2 1 
ATOM   681  N  N   . ILE A 1 85 ? 11.073  -17.927 4.073   1.00 27.76  ? 84  ILE A N   1 
ATOM   682  C  CA  . ILE A 1 85 ? 10.529  -16.583 3.990   1.00 27.56  ? 84  ILE A CA  1 
ATOM   683  C  C   . ILE A 1 85 ? 11.103  -15.709 5.106   1.00 28.14  ? 84  ILE A C   1 
ATOM   684  O  O   . ILE A 1 85 ? 11.231  -14.483 4.946   1.00 27.38  ? 84  ILE A O   1 
ATOM   685  C  CB  . ILE A 1 85 ? 8.988   -16.597 3.967   1.00 26.93  ? 84  ILE A CB  1 
ATOM   686  C  CG1 . ILE A 1 85 ? 8.396   -15.207 3.500   1.00 25.42  ? 84  ILE A CG1 1 
ATOM   687  C  CG2 . ILE A 1 85 ? 8.421   -17.043 5.328   1.00 24.61  ? 84  ILE A CG2 1 
ATOM   688  C  CD1 . ILE A 1 85 ? 6.955   -15.270 3.018   1.00 23.47  ? 84  ILE A CD1 1 
ATOM   689  N  N   . GLN A 1 86 ? 11.365  -16.333 6.266   1.00 26.82  ? 85  GLN A N   1 
ATOM   690  C  CA  . GLN A 1 86 ? 11.895  -15.607 7.411   1.00 28.33  ? 85  GLN A CA  1 
ATOM   691  C  C   . GLN A 1 86 ? 13.405  -15.377 7.272   1.00 28.40  ? 85  GLN A C   1 
ATOM   692  O  O   . GLN A 1 86 ? 13.879  -14.312 7.657   1.00 32.90  ? 85  GLN A O   1 
ATOM   693  C  CB  . GLN A 1 86 ? 11.522  -16.288 8.733   1.00 26.92  ? 85  GLN A CB  1 
ATOM   694  C  CG  . GLN A 1 86 ? 12.043  -15.572 9.975   1.00 37.99  ? 85  GLN A CG  1 
ATOM   695  C  CD  . GLN A 1 86 ? 11.340  -16.019 11.245  1.00 45.30  ? 85  GLN A CD  1 
ATOM   696  O  OE1 . GLN A 1 86 ? 10.946  -17.186 11.390  1.00 47.71  ? 85  GLN A OE1 1 
ATOM   697  N  NE2 . GLN A 1 86 ? 11.133  -15.079 12.158  1.00 39.60  ? 85  GLN A NE2 1 
ATOM   698  N  N   . ASN A 1 87 ? 14.140  -16.327 6.674   1.00 27.61  ? 86  ASN A N   1 
ATOM   699  C  CA  . ASN A 1 87 ? 15.599  -16.314 6.797   1.00 28.97  ? 86  ASN A CA  1 
ATOM   700  C  C   . ASN A 1 87 ? 16.342  -15.949 5.511   1.00 30.29  ? 86  ASN A C   1 
ATOM   701  O  O   . ASN A 1 87 ? 17.461  -15.419 5.590   1.00 31.23  ? 86  ASN A O   1 
ATOM   702  C  CB  . ASN A 1 87 ? 16.111  -17.566 7.494   1.00 31.27  ? 86  ASN A CB  1 
ATOM   703  C  CG  . ASN A 1 87 ? 15.562  -17.623 8.905   1.00 34.69  ? 86  ASN A CG  1 
ATOM   704  O  OD1 . ASN A 1 87 ? 15.931  -16.803 9.747   1.00 38.83  ? 86  ASN A OD1 1 
ATOM   705  N  ND2 . ASN A 1 87 ? 14.635  -18.524 9.176   1.00 32.75  ? 86  ASN A ND2 1 
ATOM   706  N  N   . ASN A 1 88 ? 15.796  -16.306 4.342   1.00 27.27  ? 87  ASN A N   1 
ATOM   707  C  CA  . ASN A 1 88 ? 16.439  -15.914 3.093   1.00 28.62  ? 87  ASN A CA  1 
ATOM   708  C  C   . ASN A 1 88 ? 15.391  -15.844 1.974   1.00 27.26  ? 87  ASN A C   1 
ATOM   709  O  O   . ASN A 1 88 ? 15.433  -16.627 1.013   1.00 28.48  ? 87  ASN A O   1 
ATOM   710  C  CB  . ASN A 1 88 ? 17.615  -16.836 2.768   1.00 32.57  ? 87  ASN A CB  1 
ATOM   711  C  CG  . ASN A 1 88 ? 18.643  -16.206 1.847   1.00 34.20  ? 87  ASN A CG  1 
ATOM   712  O  OD1 . ASN A 1 88 ? 18.383  -15.178 1.202   1.00 29.23  ? 87  ASN A OD1 1 
ATOM   713  N  ND2 . ASN A 1 88 ? 19.835  -16.802 1.791   1.00 34.03  ? 87  ASN A ND2 1 
ATOM   714  N  N   . PRO A 1 89 ? 14.432  -14.887 2.044   1.00 27.19  ? 88  PRO A N   1 
ATOM   715  C  CA  . PRO A 1 89 ? 13.291  -14.886 1.127   1.00 24.83  ? 88  PRO A CA  1 
ATOM   716  C  C   . PRO A 1 89 ? 13.621  -14.405 -0.289  1.00 26.36  ? 88  PRO A C   1 
ATOM   717  O  O   . PRO A 1 89 ? 12.814  -14.587 -1.175  1.00 24.78  ? 88  PRO A O   1 
ATOM   718  C  CB  . PRO A 1 89 ? 12.321  -13.979 1.841   1.00 24.67  ? 88  PRO A CB  1 
ATOM   719  C  CG  . PRO A 1 89 ? 13.230  -12.935 2.487   1.00 25.19  ? 88  PRO A CG  1 
ATOM   720  C  CD  . PRO A 1 89 ? 14.358  -13.797 3.036   1.00 27.06  ? 88  PRO A CD  1 
ATOM   721  N  N   . HIS A 1 90 ? 14.836  -13.870 -0.506  1.00 27.08  ? 89  HIS A N   1 
ATOM   722  C  CA  . HIS A 1 90 ? 15.224  -13.310 -1.795  1.00 26.74  ? 89  HIS A CA  1 
ATOM   723  C  C   . HIS A 1 90 ? 16.337  -14.130 -2.458  1.00 28.03  ? 89  HIS A C   1 
ATOM   724  O  O   . HIS A 1 90 ? 16.868  -13.715 -3.501  1.00 30.15  ? 89  HIS A O   1 
ATOM   725  C  CB  . HIS A 1 90 ? 15.585  -11.825 -1.596  1.00 26.59  ? 89  HIS A CB  1 
ATOM   726  C  CG  . HIS A 1 90 ? 14.452  -11.015 -1.074  1.00 29.93  ? 89  HIS A CG  1 
ATOM   727  N  ND1 . HIS A 1 90 ? 13.191  -10.939 -1.661  1.00 27.53  ? 89  HIS A ND1 1 
ATOM   728  C  CD2 . HIS A 1 90 ? 14.399  -10.275 0.041   1.00 28.76  ? 89  HIS A CD2 1 
ATOM   729  C  CE1 . HIS A 1 90 ? 12.428  -10.122 -0.924  1.00 26.71  ? 89  HIS A CE1 1 
ATOM   730  N  NE2 . HIS A 1 90 ? 13.131  -9.723  0.117   1.00 29.07  ? 89  HIS A NE2 1 
ATOM   731  N  N   . ALA A 1 91 ? 16.642  -15.314 -1.903  1.00 30.62  ? 90  ALA A N   1 
ATOM   732  C  CA  . ALA A 1 91 ? 17.688  -16.208 -2.405  1.00 29.57  ? 90  ALA A CA  1 
ATOM   733  C  C   . ALA A 1 91 ? 17.255  -16.860 -3.717  1.00 32.05  ? 90  ALA A C   1 
ATOM   734  O  O   . ALA A 1 91 ? 16.075  -16.958 -3.995  1.00 30.43  ? 90  ALA A O   1 
ATOM   735  C  CB  . ALA A 1 91 ? 17.960  -17.304 -1.402  1.00 27.47  ? 90  ALA A CB  1 
ATOM   736  N  N   . SER A 1 92 ? 18.225  -17.373 -4.489  1.00 29.27  ? 91  SER A N   1 
ATOM   737  C  CA  . SER A 1 92 ? 17.916  -18.265 -5.598  1.00 32.63  ? 91  SER A CA  1 
ATOM   738  C  C   . SER A 1 92 ? 17.599  -19.665 -5.075  1.00 35.78  ? 91  SER A C   1 
ATOM   739  O  O   . SER A 1 92 ? 18.364  -20.245 -4.307  1.00 38.52  ? 91  SER A O   1 
ATOM   740  C  CB  . SER A 1 92 ? 19.052  -18.285 -6.585  1.00 37.70  ? 91  SER A CB  1 
ATOM   741  O  OG  . SER A 1 92 ? 19.047  -19.533 -7.252  1.00 45.68  ? 91  SER A OG  1 
ATOM   742  N  N   . TYR A 1 93 ? 16.418  -20.182 -5.409  1.00 33.71  ? 92  TYR A N   1 
ATOM   743  C  CA  . TYR A 1 93 ? 16.059  -21.528 -4.992  1.00 36.48  ? 92  TYR A CA  1 
ATOM   744  C  C   . TYR A 1 93 ? 15.999  -22.449 -6.215  1.00 46.39  ? 92  TYR A C   1 
ATOM   745  O  O   . TYR A 1 93 ? 15.486  -23.563 -6.122  1.00 50.06  ? 92  TYR A O   1 
ATOM   746  C  CB  . TYR A 1 93 ? 14.735  -21.559 -4.214  1.00 35.76  ? 92  TYR A CB  1 
ATOM   747  C  CG  . TYR A 1 93 ? 14.875  -20.938 -2.833  1.00 32.66  ? 92  TYR A CG  1 
ATOM   748  C  CD1 . TYR A 1 93 ? 15.270  -21.705 -1.742  1.00 35.89  ? 92  TYR A CD1 1 
ATOM   749  C  CD2 . TYR A 1 93 ? 14.601  -19.586 -2.625  1.00 31.29  ? 92  TYR A CD2 1 
ATOM   750  C  CE1 . TYR A 1 93 ? 15.422  -21.129 -0.486  1.00 38.62  ? 92  TYR A CE1 1 
ATOM   751  C  CE2 . TYR A 1 93 ? 14.710  -19.012 -1.369  1.00 32.04  ? 92  TYR A CE2 1 
ATOM   752  C  CZ  . TYR A 1 93 ? 15.137  -19.786 -0.300  1.00 31.86  ? 92  TYR A CZ  1 
ATOM   753  O  OH  . TYR A 1 93 ? 15.291  -19.244 0.938   1.00 31.86  ? 92  TYR A OH  1 
ATOM   754  N  N   . SER A 1 94 ? 16.519  -21.956 -7.346  1.00 52.21  ? 93  SER A N   1 
ATOM   755  C  CA  . SER A 1 94 ? 16.808  -22.733 -8.548  1.00 68.29  ? 93  SER A CA  1 
ATOM   756  C  C   . SER A 1 94 ? 17.545  -24.030 -8.178  1.00 76.34  ? 93  SER A C   1 
ATOM   757  O  O   . SER A 1 94 ? 18.688  -23.927 -7.658  1.00 79.23  ? 93  SER A O   1 
ATOM   758  C  CB  . SER A 1 94 ? 17.634  -21.923 -9.535  1.00 68.52  ? 93  SER A CB  1 
ATOM   759  O  OG  . SER A 1 94 ? 17.074  -20.634 -9.756  1.00 82.64  ? 93  SER A OG  1 
ATOM   760  O  OXT . SER A 1 94 ? 16.962  -25.102 -8.432  1.00 88.92  ? 93  SER A OXT 1 
ATOM   761  N  N   . MET B 1 2  ? 38.830  -10.839 -41.784 1.00 92.78  ? 1   MET B N   1 
ATOM   762  C  CA  . MET B 1 2  ? 38.477  -11.889 -42.777 1.00 94.61  ? 1   MET B CA  1 
ATOM   763  C  C   . MET B 1 2  ? 36.958  -12.077 -42.791 1.00 84.76  ? 1   MET B C   1 
ATOM   764  O  O   . MET B 1 2  ? 36.353  -12.309 -41.742 1.00 75.49  ? 1   MET B O   1 
ATOM   765  C  CB  . MET B 1 2  ? 39.177  -13.212 -42.439 1.00 106.99 ? 1   MET B CB  1 
ATOM   766  C  CG  . MET B 1 2  ? 39.471  -14.098 -43.644 1.00 119.28 ? 1   MET B CG  1 
ATOM   767  S  SD  . MET B 1 2  ? 40.848  -13.541 -44.672 1.00 120.70 ? 1   MET B SD  1 
ATOM   768  C  CE  . MET B 1 2  ? 42.223  -13.689 -43.520 1.00 119.64 ? 1   MET B CE  1 
ATOM   769  N  N   . PRO B 1 3  ? 36.292  -11.951 -43.968 1.00 74.71  ? 2   PRO B N   1 
ATOM   770  C  CA  . PRO B 1 3  ? 34.853  -12.204 -44.071 1.00 72.85  ? 2   PRO B CA  1 
ATOM   771  C  C   . PRO B 1 3  ? 34.496  -13.642 -43.689 1.00 69.27  ? 2   PRO B C   1 
ATOM   772  O  O   . PRO B 1 3  ? 35.270  -14.568 -43.943 1.00 60.66  ? 2   PRO B O   1 
ATOM   773  C  CB  . PRO B 1 3  ? 34.511  -11.866 -45.542 1.00 71.93  ? 2   PRO B CB  1 
ATOM   774  C  CG  . PRO B 1 3  ? 35.671  -11.007 -46.011 1.00 66.79  ? 2   PRO B CG  1 
ATOM   775  C  CD  . PRO B 1 3  ? 36.882  -11.521 -45.249 1.00 65.82  ? 2   PRO B CD  1 
ATOM   776  N  N   . HIS B 1 4  ? 33.332  -13.808 -43.043 1.00 62.51  ? 3   HIS B N   1 
ATOM   777  C  CA  . HIS B 1 4  ? 32.873  -15.126 -42.622 1.00 62.18  ? 3   HIS B CA  1 
ATOM   778  C  C   . HIS B 1 4  ? 31.498  -15.414 -43.226 1.00 59.33  ? 3   HIS B C   1 
ATOM   779  O  O   . HIS B 1 4  ? 30.907  -14.533 -43.858 1.00 55.47  ? 3   HIS B O   1 
ATOM   780  C  CB  . HIS B 1 4  ? 32.980  -15.271 -41.101 1.00 66.41  ? 3   HIS B CB  1 
ATOM   781  C  CG  . HIS B 1 4  ? 34.382  -15.490 -40.625 1.00 76.56  ? 3   HIS B CG  1 
ATOM   782  N  ND1 . HIS B 1 4  ? 35.299  -16.246 -41.328 1.00 78.98  ? 3   HIS B ND1 1 
ATOM   783  C  CD2 . HIS B 1 4  ? 35.010  -15.083 -39.508 1.00 72.60  ? 3   HIS B CD2 1 
ATOM   784  C  CE1 . HIS B 1 4  ? 36.442  -16.282 -40.656 1.00 76.70  ? 3   HIS B CE1 1 
ATOM   785  N  NE2 . HIS B 1 4  ? 36.286  -15.584 -39.548 1.00 77.98  ? 3   HIS B NE2 1 
ATOM   786  N  N   . ALA B 1 5  ? 31.006  -16.657 -43.055 1.00 49.37  ? 4   ALA B N   1 
ATOM   787  C  CA  . ALA B 1 5  ? 29.698  -16.995 -43.586 1.00 47.75  ? 4   ALA B CA  1 
ATOM   788  C  C   . ALA B 1 5  ? 28.729  -15.937 -43.085 1.00 46.74  ? 4   ALA B C   1 
ATOM   789  O  O   . ALA B 1 5  ? 28.050  -15.303 -43.887 1.00 47.31  ? 4   ALA B O   1 
ATOM   790  C  CB  . ALA B 1 5  ? 29.270  -18.371 -43.140 1.00 48.88  ? 4   ALA B CB  1 
ATOM   791  N  N   . PHE B 1 6  ? 28.713  -15.750 -41.758 1.00 39.11  ? 5   PHE B N   1 
ATOM   792  C  CA  . PHE B 1 6  ? 27.909  -14.710 -41.133 1.00 50.80  ? 5   PHE B CA  1 
ATOM   793  C  C   . PHE B 1 6  ? 28.770  -13.477 -40.854 1.00 45.32  ? 5   PHE B C   1 
ATOM   794  O  O   . PHE B 1 6  ? 29.889  -13.591 -40.356 1.00 49.88  ? 5   PHE B O   1 
ATOM   795  C  CB  . PHE B 1 6  ? 27.276  -15.154 -39.809 1.00 45.63  ? 5   PHE B CB  1 
ATOM   796  C  CG  . PHE B 1 6  ? 26.193  -16.216 -39.937 1.00 42.11  ? 5   PHE B CG  1 
ATOM   797  C  CD1 . PHE B 1 6  ? 24.870  -15.859 -40.196 1.00 38.39  ? 5   PHE B CD1 1 
ATOM   798  C  CD2 . PHE B 1 6  ? 26.500  -17.562 -39.757 1.00 40.06  ? 5   PHE B CD2 1 
ATOM   799  C  CE1 . PHE B 1 6  ? 23.881  -16.819 -40.297 1.00 35.16  ? 5   PHE B CE1 1 
ATOM   800  C  CE2 . PHE B 1 6  ? 25.511  -18.532 -39.874 1.00 36.33  ? 5   PHE B CE2 1 
ATOM   801  C  CZ  . PHE B 1 6  ? 24.201  -18.159 -40.116 1.00 33.91  ? 5   PHE B CZ  1 
ATOM   802  N  N   . LYS B 1 7  ? 28.211  -12.299 -41.136 1.00 48.31  ? 6   LYS B N   1 
ATOM   803  C  CA  . LYS B 1 7  ? 28.941  -11.054 -40.955 1.00 49.20  ? 6   LYS B CA  1 
ATOM   804  C  C   . LYS B 1 7  ? 28.181  -10.144 -39.988 1.00 50.60  ? 6   LYS B C   1 
ATOM   805  O  O   . LYS B 1 7  ? 26.948  -10.193 -39.929 1.00 43.34  ? 6   LYS B O   1 
ATOM   806  C  CB  . LYS B 1 7  ? 29.162  -10.396 -42.318 1.00 47.98  ? 6   LYS B CB  1 
ATOM   807  C  CG  . LYS B 1 7  ? 27.925  -9.968  -43.076 1.00 53.18  ? 6   LYS B CG  1 
ATOM   808  C  CD  . LYS B 1 7  ? 28.275  -9.550  -44.500 1.00 59.68  ? 6   LYS B CD  1 
ATOM   809  C  CE  . LYS B 1 7  ? 27.121  -8.942  -45.237 1.00 64.60  ? 6   LYS B CE  1 
ATOM   810  N  NZ  . LYS B 1 7  ? 26.035  -9.905  -45.437 1.00 70.94  ? 6   LYS B NZ  1 
ATOM   811  N  N   . PRO B 1 8  ? 28.881  -9.241  -39.254 1.00 50.65  ? 7   PRO B N   1 
ATOM   812  C  CA  . PRO B 1 8  ? 28.227  -8.362  -38.288 1.00 43.37  ? 7   PRO B CA  1 
ATOM   813  C  C   . PRO B 1 8  ? 27.089  -7.641  -38.984 1.00 43.36  ? 7   PRO B C   1 
ATOM   814  O  O   . PRO B 1 8  ? 27.227  -7.206  -40.135 1.00 47.97  ? 7   PRO B O   1 
ATOM   815  C  CB  . PRO B 1 8  ? 29.372  -7.430  -37.898 1.00 50.22  ? 7   PRO B CB  1 
ATOM   816  C  CG  . PRO B 1 8  ? 30.587  -8.332  -37.985 1.00 49.18  ? 7   PRO B CG  1 
ATOM   817  C  CD  . PRO B 1 8  ? 30.332  -8.989  -39.328 1.00 55.01  ? 7   PRO B CD  1 
ATOM   818  N  N   . GLY B 1 9  ? 25.944  -7.596  -38.290 1.00 38.38  ? 8   GLY B N   1 
ATOM   819  C  CA  . GLY B 1 9  ? 24.760  -6.964  -38.827 1.00 33.95  ? 8   GLY B CA  1 
ATOM   820  C  C   . GLY B 1 9  ? 23.833  -7.959  -39.512 1.00 34.42  ? 8   GLY B C   1 
ATOM   821  O  O   . GLY B 1 9  ? 22.729  -7.604  -39.887 1.00 34.86  ? 8   GLY B O   1 
ATOM   822  N  N   . ASP B 1 10 ? 24.283  -9.205  -39.690 1.00 36.51  ? 9   ASP B N   1 
ATOM   823  C  CA  . ASP B 1 10 ? 23.431  -10.237 -40.264 1.00 35.32  ? 9   ASP B CA  1 
ATOM   824  C  C   . ASP B 1 10 ? 22.278  -10.525 -39.296 1.00 34.08  ? 9   ASP B C   1 
ATOM   825  O  O   . ASP B 1 10 ? 22.487  -10.566 -38.084 1.00 33.36  ? 9   ASP B O   1 
ATOM   826  C  CB  . ASP B 1 10 ? 24.239  -11.491 -40.543 1.00 34.80  ? 9   ASP B CB  1 
ATOM   827  C  CG  . ASP B 1 10 ? 24.932  -11.524 -41.902 1.00 38.86  ? 9   ASP B CG  1 
ATOM   828  O  OD1 . ASP B 1 10 ? 24.517  -10.762 -42.797 1.00 41.82  ? 9   ASP B OD1 1 
ATOM   829  O  OD2 . ASP B 1 10 ? 25.864  -12.343 -42.057 1.00 42.40  ? 9   ASP B OD2 1 
ATOM   830  N  N   . LEU B 1 11 ? 21.068  -10.676 -39.836 1.00 31.65  ? 10  LEU B N   1 
ATOM   831  C  CA  . LEU B 1 11 ? 19.910  -10.934 -38.995 1.00 34.41  ? 10  LEU B CA  1 
ATOM   832  C  C   . LEU B 1 11 ? 19.565  -12.418 -39.033 1.00 33.98  ? 10  LEU B C   1 
ATOM   833  O  O   . LEU B 1 11 ? 19.624  -13.033 -40.096 1.00 33.19  ? 10  LEU B O   1 
ATOM   834  C  CB  . LEU B 1 11 ? 18.757  -10.063 -39.472 1.00 32.34  ? 10  LEU B CB  1 
ATOM   835  C  CG  . LEU B 1 11 ? 19.087  -8.565  -39.528 1.00 31.59  ? 10  LEU B CG  1 
ATOM   836  C  CD1 . LEU B 1 11 ? 17.863  -7.801  -39.956 1.00 30.90  ? 10  LEU B CD1 1 
ATOM   837  C  CD2 . LEU B 1 11 ? 19.637  -8.096  -38.189 1.00 30.38  ? 10  LEU B CD2 1 
ATOM   838  N  N   . VAL B 1 12 ? 19.206  -12.975 -37.862 1.00 32.28  ? 11  VAL B N   1 
ATOM   839  C  CA  . VAL B 1 12 ? 19.001  -14.409 -37.718 1.00 28.27  ? 11  VAL B CA  1 
ATOM   840  C  C   . VAL B 1 12 ? 17.859  -14.643 -36.726 1.00 31.45  ? 11  VAL B C   1 
ATOM   841  O  O   . VAL B 1 12 ? 17.435  -13.719 -36.020 1.00 27.07  ? 11  VAL B O   1 
ATOM   842  C  CB  . VAL B 1 12 ? 20.276  -15.165 -37.268 1.00 30.92  ? 11  VAL B CB  1 
ATOM   843  C  CG1 . VAL B 1 12 ? 21.433  -15.044 -38.273 1.00 31.88  ? 11  VAL B CG1 1 
ATOM   844  C  CG2 . VAL B 1 12 ? 20.727  -14.781 -35.855 1.00 26.89  ? 11  VAL B CG2 1 
ATOM   845  N  N   . PHE B 1 13 ? 17.369  -15.892 -36.694 1.00 30.09  ? 12  PHE B N   1 
ATOM   846  C  CA  . PHE B 1 13 ? 16.804  -16.427 -35.464 1.00 31.98  ? 12  PHE B CA  1 
ATOM   847  C  C   . PHE B 1 13 ? 17.872  -17.311 -34.834 1.00 33.35  ? 12  PHE B C   1 
ATOM   848  O  O   . PHE B 1 13 ? 18.506  -18.113 -35.547 1.00 32.09  ? 12  PHE B O   1 
ATOM   849  C  CB  . PHE B 1 13 ? 15.528  -17.233 -35.707 1.00 28.58  ? 12  PHE B CB  1 
ATOM   850  C  CG  . PHE B 1 13 ? 14.316  -16.427 -36.128 1.00 31.84  ? 12  PHE B CG  1 
ATOM   851  C  CD1 . PHE B 1 13 ? 14.068  -16.155 -37.471 1.00 33.30  ? 12  PHE B CD1 1 
ATOM   852  C  CD2 . PHE B 1 13 ? 13.429  -15.940 -35.176 1.00 30.68  ? 12  PHE B CD2 1 
ATOM   853  C  CE1 . PHE B 1 13 ? 12.947  -15.437 -37.844 1.00 40.53  ? 12  PHE B CE1 1 
ATOM   854  C  CE2 . PHE B 1 13 ? 12.294  -15.239 -35.551 1.00 34.84  ? 12  PHE B CE2 1 
ATOM   855  C  CZ  . PHE B 1 13 ? 12.054  -14.991 -36.891 1.00 41.91  ? 12  PHE B CZ  1 
ATOM   856  N  N   . ALA B 1 14 ? 18.066  -17.139 -33.507 1.00 28.09  ? 13  ALA B N   1 
ATOM   857  C  CA  . ALA B 1 14 ? 19.104  -17.837 -32.771 1.00 29.70  ? 13  ALA B CA  1 
ATOM   858  C  C   . ALA B 1 14 ? 18.470  -18.790 -31.749 1.00 29.41  ? 13  ALA B C   1 
ATOM   859  O  O   . ALA B 1 14 ? 17.485  -18.438 -31.098 1.00 31.25  ? 13  ALA B O   1 
ATOM   860  C  CB  . ALA B 1 14 ? 20.008  -16.849 -32.119 1.00 28.83  ? 13  ALA B CB  1 
ATOM   861  N  N   . LYS B 1 15 ? 18.986  -20.019 -31.687 1.00 30.72  ? 14  LYS B N   1 
ATOM   862  C  CA  . LYS B 1 15 ? 18.317  -21.100 -30.964 1.00 33.05  ? 14  LYS B CA  1 
ATOM   863  C  C   . LYS B 1 15 ? 19.151  -21.465 -29.751 1.00 32.81  ? 14  LYS B C   1 
ATOM   864  O  O   . LYS B 1 15 ? 20.333  -21.789 -29.885 1.00 36.41  ? 14  LYS B O   1 
ATOM   865  C  CB  . LYS B 1 15 ? 18.061  -22.388 -31.765 1.00 36.88  ? 14  LYS B CB  1 
ATOM   866  C  CG  . LYS B 1 15 ? 17.294  -23.504 -30.995 1.00 32.48  ? 14  LYS B CG  1 
ATOM   867  C  CD  . LYS B 1 15 ? 15.835  -23.102 -30.722 1.00 35.91  ? 14  LYS B CD  1 
ATOM   868  C  CE  . LYS B 1 15 ? 14.933  -24.172 -30.094 1.00 32.87  ? 14  LYS B CE  1 
ATOM   869  N  NZ  . LYS B 1 15 ? 15.459  -24.421 -28.748 1.00 30.30  ? 14  LYS B NZ  1 
ATOM   870  N  N   . MET B 1 16 ? 18.526  -21.369 -28.571 1.00 33.05  ? 15  MET B N   1 
ATOM   871  C  CA  . MET B 1 16 ? 19.163  -21.799 -27.336 1.00 39.57  ? 15  MET B CA  1 
ATOM   872  C  C   . MET B 1 16 ? 18.287  -22.853 -26.660 1.00 35.51  ? 15  MET B C   1 
ATOM   873  O  O   . MET B 1 16 ? 17.051  -22.784 -26.718 1.00 30.17  ? 15  MET B O   1 
ATOM   874  C  CB  . MET B 1 16 ? 19.373  -20.646 -26.347 1.00 39.60  ? 15  MET B CB  1 
ATOM   875  C  CG  . MET B 1 16 ? 20.104  -19.459 -26.927 1.00 45.42  ? 15  MET B CG  1 
ATOM   876  S  SD  . MET B 1 16 ? 21.473  -18.773 -25.971 1.00 48.26  ? 15  MET B SD  1 
ATOM   877  C  CE  . MET B 1 16 ? 21.355  -19.273 -24.246 1.00 52.13  ? 15  MET B CE  1 
ATOM   878  N  N   . LYS B 1 17 ? 18.940  -23.804 -25.985 1.00 35.63  ? 16  LYS B N   1 
ATOM   879  C  CA  . LYS B 1 17 ? 18.183  -24.839 -25.291 1.00 41.40  ? 16  LYS B CA  1 
ATOM   880  C  C   . LYS B 1 17 ? 17.223  -24.173 -24.296 1.00 37.60  ? 16  LYS B C   1 
ATOM   881  O  O   . LYS B 1 17 ? 17.618  -23.261 -23.581 1.00 41.45  ? 16  LYS B O   1 
ATOM   882  C  CB  . LYS B 1 17 ? 19.141  -25.885 -24.712 1.00 46.44  ? 16  LYS B CB  1 
ATOM   883  C  CG  . LYS B 1 17 ? 18.438  -27.063 -24.026 1.00 55.25  ? 16  LYS B CG  1 
ATOM   884  C  CD  . LYS B 1 17 ? 19.313  -27.776 -22.997 1.00 55.57  ? 16  LYS B CD  1 
ATOM   885  N  N   . GLY B 1 18 ? 15.950  -24.582 -24.320 1.00 39.04  ? 17  GLY B N   1 
ATOM   886  C  CA  . GLY B 1 18 ? 14.945  -24.080 -23.398 1.00 40.92  ? 17  GLY B CA  1 
ATOM   887  C  C   . GLY B 1 18 ? 14.126  -22.910 -23.949 1.00 41.92  ? 17  GLY B C   1 
ATOM   888  O  O   . GLY B 1 18 ? 13.218  -22.425 -23.270 1.00 39.69  ? 17  GLY B O   1 
ATOM   889  N  N   . TYR B 1 19 ? 14.444  -22.442 -25.171 1.00 35.07  ? 18  TYR B N   1 
ATOM   890  C  CA  . TYR B 1 19 ? 13.791  -21.248 -25.690 1.00 34.80  ? 18  TYR B CA  1 
ATOM   891  C  C   . TYR B 1 19 ? 13.447  -21.464 -27.155 1.00 33.57  ? 18  TYR B C   1 
ATOM   892  O  O   . TYR B 1 19 ? 14.104  -22.252 -27.822 1.00 36.57  ? 18  TYR B O   1 
ATOM   893  C  CB  . TYR B 1 19 ? 14.755  -20.062 -25.610 1.00 30.41  ? 18  TYR B CB  1 
ATOM   894  C  CG  . TYR B 1 19 ? 15.224  -19.775 -24.195 1.00 35.58  ? 18  TYR B CG  1 
ATOM   895  C  CD1 . TYR B 1 19 ? 14.549  -18.847 -23.394 1.00 32.40  ? 18  TYR B CD1 1 
ATOM   896  C  CD2 . TYR B 1 19 ? 16.340  -20.424 -23.673 1.00 35.73  ? 18  TYR B CD2 1 
ATOM   897  C  CE1 . TYR B 1 19 ? 14.956  -18.615 -22.088 1.00 36.54  ? 18  TYR B CE1 1 
ATOM   898  C  CE2 . TYR B 1 19 ? 16.764  -20.178 -22.374 1.00 40.39  ? 18  TYR B CE2 1 
ATOM   899  C  CZ  . TYR B 1 19 ? 16.073  -19.267 -21.589 1.00 41.24  ? 18  TYR B CZ  1 
ATOM   900  O  OH  . TYR B 1 19 ? 16.513  -19.035 -20.320 1.00 45.45  ? 18  TYR B OH  1 
ATOM   901  N  N   . PRO B 1 20 ? 12.414  -20.777 -27.685 1.00 32.86  ? 19  PRO B N   1 
ATOM   902  C  CA  . PRO B 1 20 ? 12.140  -20.820 -29.122 1.00 31.57  ? 19  PRO B CA  1 
ATOM   903  C  C   . PRO B 1 20 ? 13.215  -20.066 -29.908 1.00 30.83  ? 19  PRO B C   1 
ATOM   904  O  O   . PRO B 1 20 ? 13.921  -19.209 -29.376 1.00 26.67  ? 19  PRO B O   1 
ATOM   905  C  CB  . PRO B 1 20 ? 10.774  -20.155 -29.218 1.00 26.89  ? 19  PRO B CB  1 
ATOM   906  C  CG  . PRO B 1 20 ? 10.772  -19.152 -28.066 1.00 33.35  ? 19  PRO B CG  1 
ATOM   907  C  CD  . PRO B 1 20 ? 11.510  -19.877 -26.944 1.00 31.50  ? 19  PRO B CD  1 
ATOM   908  N  N   . HIS B 1 21 ? 13.350  -20.418 -31.188 1.00 28.51  ? 20  HIS B N   1 
ATOM   909  C  CA  . HIS B 1 21 ? 14.198  -19.668 -32.109 1.00 29.16  ? 20  HIS B CA  1 
ATOM   910  C  C   . HIS B 1 21 ? 13.906  -18.176 -31.971 1.00 26.58  ? 20  HIS B C   1 
ATOM   911  O  O   . HIS B 1 21 ? 12.749  -17.754 -32.111 1.00 31.14  ? 20  HIS B O   1 
ATOM   912  C  CB  . HIS B 1 21 ? 13.861  -20.130 -33.536 1.00 25.47  ? 20  HIS B CB  1 
ATOM   913  C  CG  . HIS B 1 21 ? 14.115  -21.597 -33.734 1.00 28.36  ? 20  HIS B CG  1 
ATOM   914  N  ND1 . HIS B 1 21 ? 13.160  -22.536 -33.414 1.00 31.01  ? 20  HIS B ND1 1 
ATOM   915  C  CD2 . HIS B 1 21 ? 15.181  -22.292 -34.224 1.00 29.36  ? 20  HIS B CD2 1 
ATOM   916  C  CE1 . HIS B 1 21 ? 13.634  -23.760 -33.680 1.00 31.71  ? 20  HIS B CE1 1 
ATOM   917  N  NE2 . HIS B 1 21 ? 14.864  -23.645 -34.176 1.00 31.53  ? 20  HIS B NE2 1 
ATOM   918  N  N   . TRP B 1 22 ? 14.958  -17.382 -31.751 1.00 27.69  ? 21  TRP B N   1 
ATOM   919  C  CA  . TRP B 1 22 ? 14.746  -16.046 -31.190 1.00 28.59  ? 21  TRP B CA  1 
ATOM   920  C  C   . TRP B 1 22 ? 15.289  -14.982 -32.141 1.00 29.48  ? 21  TRP B C   1 
ATOM   921  O  O   . TRP B 1 22 ? 16.423  -15.135 -32.591 1.00 31.02  ? 21  TRP B O   1 
ATOM   922  C  CB  . TRP B 1 22 ? 15.440  -15.945 -29.824 1.00 26.06  ? 21  TRP B CB  1 
ATOM   923  C  CG  . TRP B 1 22 ? 14.917  -14.821 -28.966 1.00 29.34  ? 21  TRP B CG  1 
ATOM   924  C  CD1 . TRP B 1 22 ? 15.209  -13.488 -29.063 1.00 29.38  ? 21  TRP B CD1 1 
ATOM   925  C  CD2 . TRP B 1 22 ? 13.953  -14.948 -27.891 1.00 29.89  ? 21  TRP B CD2 1 
ATOM   926  N  NE1 . TRP B 1 22 ? 14.486  -12.774 -28.129 1.00 31.38  ? 21  TRP B NE1 1 
ATOM   927  C  CE2 . TRP B 1 22 ? 13.711  -13.645 -27.394 1.00 30.40  ? 21  TRP B CE2 1 
ATOM   928  C  CE3 . TRP B 1 22 ? 13.287  -16.037 -27.305 1.00 30.52  ? 21  TRP B CE3 1 
ATOM   929  C  CZ2 . TRP B 1 22 ? 12.831  -13.407 -26.331 1.00 31.41  ? 21  TRP B CZ2 1 
ATOM   930  C  CZ3 . TRP B 1 22 ? 12.407  -15.803 -26.262 1.00 31.41  ? 21  TRP B CZ3 1 
ATOM   931  C  CH2 . TRP B 1 22 ? 12.160  -14.494 -25.809 1.00 31.60  ? 21  TRP B CH2 1 
ATOM   932  N  N   . PRO B 1 23 ? 14.527  -13.892 -32.457 1.00 29.00  ? 22  PRO B N   1 
ATOM   933  C  CA  . PRO B 1 23 ? 15.025  -12.829 -33.346 1.00 29.20  ? 22  PRO B CA  1 
ATOM   934  C  C   . PRO B 1 23 ? 16.341  -12.278 -32.788 1.00 30.17  ? 22  PRO B C   1 
ATOM   935  O  O   . PRO B 1 23 ? 16.470  -11.986 -31.605 1.00 29.91  ? 22  PRO B O   1 
ATOM   936  C  CB  . PRO B 1 23 ? 13.856  -11.802 -33.344 1.00 28.77  ? 22  PRO B CB  1 
ATOM   937  C  CG  . PRO B 1 23 ? 13.164  -12.054 -32.002 1.00 28.38  ? 22  PRO B CG  1 
ATOM   938  C  CD  . PRO B 1 23 ? 13.162  -13.602 -31.969 1.00 26.74  ? 22  PRO B CD  1 
ATOM   939  N  N   . ALA B 1 24 ? 17.373  -12.170 -33.629 1.00 28.32  ? 23  ALA B N   1 
ATOM   940  C  CA  . ALA B 1 24 ? 18.703  -11.852 -33.122 1.00 26.51  ? 23  ALA B CA  1 
ATOM   941  C  C   . ALA B 1 24 ? 19.571  -11.283 -34.247 1.00 26.67  ? 23  ALA B C   1 
ATOM   942  O  O   . ALA B 1 24 ? 19.149  -11.278 -35.401 1.00 28.69  ? 23  ALA B O   1 
ATOM   943  C  CB  . ALA B 1 24 ? 19.351  -13.093 -32.550 1.00 28.18  ? 23  ALA B CB  1 
ATOM   944  N  N   . ARG B 1 25 ? 20.785  -10.845 -33.887 1.00 31.54  ? 24  ARG B N   1 
ATOM   945  C  CA  . ARG B 1 25 ? 21.737  -10.336 -34.866 1.00 32.32  ? 24  ARG B CA  1 
ATOM   946  C  C   . ARG B 1 25 ? 23.139  -10.808 -34.514 1.00 30.28  ? 24  ARG B C   1 
ATOM   947  O  O   . ARG B 1 25 ? 23.438  -11.115 -33.355 1.00 31.35  ? 24  ARG B O   1 
ATOM   948  C  CB  . ARG B 1 25 ? 21.689  -8.805  -34.951 1.00 28.89  ? 24  ARG B CB  1 
ATOM   949  C  CG  . ARG B 1 25 ? 22.364  -8.048  -33.821 1.00 35.04  ? 24  ARG B CG  1 
ATOM   950  C  CD  . ARG B 1 25 ? 21.973  -6.565  -33.915 1.00 32.73  ? 24  ARG B CD  1 
ATOM   951  N  NE  . ARG B 1 25 ? 22.631  -5.816  -32.843 1.00 30.42  ? 24  ARG B NE  1 
ATOM   952  C  CZ  . ARG B 1 25 ? 22.373  -4.556  -32.500 1.00 33.96  ? 24  ARG B CZ  1 
ATOM   953  N  NH1 . ARG B 1 25 ? 21.484  -3.867  -33.197 1.00 29.46  ? 24  ARG B NH1 1 
ATOM   954  N  NH2 . ARG B 1 25 ? 23.008  -4.019  -31.465 1.00 31.05  ? 24  ARG B NH2 1 
ATOM   955  N  N   . ILE B 1 26 ? 23.989  -10.888 -35.553 1.00 31.54  ? 25  ILE B N   1 
ATOM   956  C  CA  . ILE B 1 26 ? 25.428  -11.018 -35.381 1.00 32.13  ? 25  ILE B CA  1 
ATOM   957  C  C   . ILE B 1 26 ? 25.961  -9.623  -35.049 1.00 33.57  ? 25  ILE B C   1 
ATOM   958  O  O   . ILE B 1 26 ? 25.752  -8.682  -35.805 1.00 36.32  ? 25  ILE B O   1 
ATOM   959  C  CB  . ILE B 1 26 ? 26.095  -11.533 -36.675 1.00 36.04  ? 25  ILE B CB  1 
ATOM   960  C  CG1 . ILE B 1 26 ? 25.355  -12.733 -37.294 1.00 34.57  ? 25  ILE B CG1 1 
ATOM   961  C  CG2 . ILE B 1 26 ? 27.591  -11.808 -36.458 1.00 35.72  ? 25  ILE B CG2 1 
ATOM   962  C  CD1 . ILE B 1 26 ? 25.348  -13.989 -36.447 1.00 33.65  ? 25  ILE B CD1 1 
ATOM   963  N  N   . ASP B 1 27 ? 26.664  -9.521  -33.928 1.00 37.83  ? 26  ASP B N   1 
ATOM   964  C  CA  . ASP B 1 27 ? 27.337  -8.298  -33.525 1.00 46.50  ? 26  ASP B CA  1 
ATOM   965  C  C   . ASP B 1 27 ? 28.815  -8.350  -33.934 1.00 49.51  ? 26  ASP B C   1 
ATOM   966  O  O   . ASP B 1 27 ? 29.355  -9.437  -34.138 1.00 43.34  ? 26  ASP B O   1 
ATOM   967  C  CB  . ASP B 1 27 ? 27.268  -8.182  -32.012 1.00 44.07  ? 26  ASP B CB  1 
ATOM   968  C  CG  . ASP B 1 27 ? 26.034  -7.495  -31.441 1.00 42.47  ? 26  ASP B CG  1 
ATOM   969  O  OD1 . ASP B 1 27 ? 25.209  -6.998  -32.238 1.00 41.32  ? 26  ASP B OD1 1 
ATOM   970  O  OD2 . ASP B 1 27 ? 25.944  -7.409  -30.198 1.00 36.90  ? 26  ASP B OD2 1 
ATOM   971  N  N   A ASP B 1 28 ? 29.440  -7.165  -33.984 0.50 54.71  ? 27  ASP B N   1 
ATOM   972  N  N   B ASP B 1 28 ? 29.454  -7.174  -34.073 0.50 51.30  ? 27  ASP B N   1 
ATOM   973  C  CA  A ASP B 1 28 ? 30.877  -6.982  -34.125 0.50 60.49  ? 27  ASP B CA  1 
ATOM   974  C  CA  B ASP B 1 28 ? 30.905  -7.073  -34.209 0.50 54.57  ? 27  ASP B CA  1 
ATOM   975  C  C   A ASP B 1 28 ? 31.557  -7.491  -32.858 0.50 61.55  ? 27  ASP B C   1 
ATOM   976  C  C   B ASP B 1 28 ? 31.566  -7.447  -32.885 0.50 57.66  ? 27  ASP B C   1 
ATOM   977  O  O   A ASP B 1 28 ? 30.910  -7.597  -31.817 0.50 64.19  ? 27  ASP B O   1 
ATOM   978  O  O   B ASP B 1 28 ? 30.919  -7.414  -31.840 0.50 60.97  ? 27  ASP B O   1 
ATOM   979  C  CB  A ASP B 1 28 ? 31.199  -5.507  -34.305 0.50 58.32  ? 27  ASP B CB  1 
ATOM   980  C  CB  B ASP B 1 28 ? 31.372  -5.711  -34.712 0.50 47.64  ? 27  ASP B CB  1 
ATOM   981  C  CG  A ASP B 1 28 ? 30.067  -4.686  -34.905 0.50 59.29  ? 27  ASP B CG  1 
ATOM   982  C  CG  B ASP B 1 28 ? 31.921  -5.676  -36.134 0.50 45.83  ? 27  ASP B CG  1 
ATOM   983  O  OD1 A ASP B 1 28 ? 30.232  -4.206  -36.040 0.50 63.38  ? 27  ASP B OD1 1 
ATOM   984  O  OD1 B ASP B 1 28 ? 32.937  -6.352  -36.391 0.50 45.18  ? 27  ASP B OD1 1 
ATOM   985  O  OD2 A ASP B 1 28 ? 29.018  -4.548  -34.238 0.50 60.79  ? 27  ASP B OD2 1 
ATOM   986  O  OD2 B ASP B 1 28 ? 31.337  -4.971  -36.980 0.50 43.11  ? 27  ASP B OD2 1 
ATOM   987  N  N   . ILE B 1 29 ? 32.860  -7.789  -32.956 1.00 67.71  ? 28  ILE B N   1 
ATOM   988  C  CA  . ILE B 1 29 ? 33.614  -8.349  -31.841 1.00 68.51  ? 28  ILE B CA  1 
ATOM   989  C  C   . ILE B 1 29 ? 34.370  -7.231  -31.100 1.00 69.99  ? 28  ILE B C   1 
ATOM   990  O  O   . ILE B 1 29 ? 34.405  -6.094  -31.630 1.00 78.92  ? 28  ILE B O   1 
ATOM   991  C  CB  . ILE B 1 29 ? 34.555  -9.471  -32.323 1.00 65.89  ? 28  ILE B CB  1 
ATOM   992  N  N   . VAL B 1 34 ? 37.495  -10.113 -24.674 1.00 90.53  ? 33  VAL B N   1 
ATOM   993  C  CA  . VAL B 1 34 ? 36.987  -11.505 -24.865 1.00 77.74  ? 33  VAL B CA  1 
ATOM   994  C  C   . VAL B 1 34 ? 36.520  -11.640 -26.310 1.00 81.77  ? 33  VAL B C   1 
ATOM   995  O  O   . VAL B 1 34 ? 35.629  -10.910 -26.732 1.00 88.96  ? 33  VAL B O   1 
ATOM   996  C  CB  . VAL B 1 34 ? 35.869  -11.825 -23.848 1.00 73.52  ? 33  VAL B CB  1 
ATOM   997  C  CG1 . VAL B 1 34 ? 34.937  -10.638 -23.630 1.00 67.66  ? 33  VAL B CG1 1 
ATOM   998  C  CG2 . VAL B 1 34 ? 35.094  -13.098 -24.189 1.00 67.95  ? 33  VAL B CG2 1 
ATOM   999  N  N   . LYS B 1 35 ? 37.162  -12.546 -27.062 1.00 80.69  ? 34  LYS B N   1 
ATOM   1000 C  CA  . LYS B 1 35 ? 36.760  -12.893 -28.422 1.00 76.90  ? 34  LYS B CA  1 
ATOM   1001 C  C   . LYS B 1 35 ? 35.951  -14.194 -28.394 1.00 76.09  ? 34  LYS B C   1 
ATOM   1002 O  O   . LYS B 1 35 ? 36.204  -15.056 -27.550 1.00 77.74  ? 34  LYS B O   1 
ATOM   1003 C  CB  . LYS B 1 35 ? 37.991  -13.001 -29.333 1.00 63.03  ? 34  LYS B CB  1 
ATOM   1004 N  N   . PRO B 1 36 ? 34.958  -14.395 -29.301 1.00 70.54  ? 35  PRO B N   1 
ATOM   1005 C  CA  . PRO B 1 36 ? 34.153  -15.625 -29.310 1.00 60.87  ? 35  PRO B CA  1 
ATOM   1006 C  C   . PRO B 1 36 ? 35.012  -16.883 -29.374 1.00 56.88  ? 35  PRO B C   1 
ATOM   1007 O  O   . PRO B 1 36 ? 36.083  -16.848 -29.972 1.00 61.13  ? 35  PRO B O   1 
ATOM   1008 C  CB  . PRO B 1 36 ? 33.251  -15.484 -30.560 1.00 62.50  ? 35  PRO B CB  1 
ATOM   1009 C  CG  . PRO B 1 36 ? 33.892  -14.372 -31.377 1.00 63.65  ? 35  PRO B CG  1 
ATOM   1010 C  CD  . PRO B 1 36 ? 34.563  -13.456 -30.367 1.00 65.32  ? 35  PRO B CD  1 
ATOM   1011 N  N   . PRO B 1 37 ? 34.594  -18.019 -28.757 1.00 58.47  ? 36  PRO B N   1 
ATOM   1012 C  CA  . PRO B 1 37 ? 35.269  -19.299 -28.974 1.00 57.07  ? 36  PRO B CA  1 
ATOM   1013 C  C   . PRO B 1 37 ? 35.359  -19.539 -30.482 1.00 67.49  ? 36  PRO B C   1 
ATOM   1014 O  O   . PRO B 1 37 ? 34.565  -18.987 -31.251 1.00 61.35  ? 36  PRO B O   1 
ATOM   1015 C  CB  . PRO B 1 37 ? 34.359  -20.344 -28.287 1.00 59.45  ? 36  PRO B CB  1 
ATOM   1016 C  CG  . PRO B 1 37 ? 33.528  -19.551 -27.300 1.00 57.46  ? 36  PRO B CG  1 
ATOM   1017 C  CD  . PRO B 1 37 ? 33.455  -18.127 -27.829 1.00 57.90  ? 36  PRO B CD  1 
ATOM   1018 N  N   . PRO B 1 38 ? 36.317  -20.367 -30.963 1.00 69.01  ? 37  PRO B N   1 
ATOM   1019 C  CA  . PRO B 1 38 ? 36.380  -20.714 -32.388 1.00 69.85  ? 37  PRO B CA  1 
ATOM   1020 C  C   . PRO B 1 38 ? 35.060  -21.280 -32.925 1.00 63.70  ? 37  PRO B C   1 
ATOM   1021 O  O   . PRO B 1 38 ? 34.355  -22.001 -32.219 1.00 63.60  ? 37  PRO B O   1 
ATOM   1022 C  CB  . PRO B 1 38 ? 37.535  -21.734 -32.477 1.00 67.90  ? 37  PRO B CB  1 
ATOM   1023 C  CG  . PRO B 1 38 ? 38.364  -21.475 -31.229 1.00 70.57  ? 37  PRO B CG  1 
ATOM   1024 C  CD  . PRO B 1 38 ? 37.380  -21.004 -30.164 1.00 71.53  ? 37  PRO B CD  1 
ATOM   1025 N  N   . ASN B 1 39 ? 34.727  -20.918 -34.173 1.00 57.15  ? 38  ASN B N   1 
ATOM   1026 C  CA  . ASN B 1 39 ? 33.536  -21.402 -34.858 1.00 55.81  ? 38  ASN B CA  1 
ATOM   1027 C  C   . ASN B 1 39 ? 32.278  -20.642 -34.426 1.00 54.33  ? 38  ASN B C   1 
ATOM   1028 O  O   . ASN B 1 39 ? 31.242  -20.790 -35.054 1.00 48.46  ? 38  ASN B O   1 
ATOM   1029 C  CB  . ASN B 1 39 ? 33.283  -22.886 -34.610 1.00 55.05  ? 38  ASN B CB  1 
ATOM   1030 C  CG  . ASN B 1 39 ? 34.386  -23.807 -35.083 1.00 67.98  ? 38  ASN B CG  1 
ATOM   1031 O  OD1 . ASN B 1 39 ? 34.372  -24.994 -34.738 1.00 68.84  ? 38  ASN B OD1 1 
ATOM   1032 N  ND2 . ASN B 1 39 ? 35.351  -23.302 -35.843 1.00 69.88  ? 38  ASN B ND2 1 
ATOM   1033 N  N   . LYS B 1 40 ? 32.349  -19.831 -33.361 1.00 55.30  ? 39  LYS B N   1 
ATOM   1034 C  CA  . LYS B 1 40 ? 31.149  -19.227 -32.802 1.00 49.45  ? 39  LYS B CA  1 
ATOM   1035 C  C   . LYS B 1 40 ? 31.131  -17.717 -33.046 1.00 50.54  ? 39  LYS B C   1 
ATOM   1036 O  O   . LYS B 1 40 ? 32.153  -17.107 -33.328 1.00 46.48  ? 39  LYS B O   1 
ATOM   1037 C  CB  . LYS B 1 40 ? 31.113  -19.583 -31.315 1.00 46.59  ? 39  LYS B CB  1 
ATOM   1038 C  CG  . LYS B 1 40 ? 30.903  -21.046 -30.986 1.00 47.74  ? 39  LYS B CG  1 
ATOM   1039 C  CD  . LYS B 1 40 ? 30.633  -21.099 -29.483 1.00 55.67  ? 39  LYS B CD  1 
ATOM   1040 C  CE  . LYS B 1 40 ? 29.589  -22.082 -29.049 1.00 63.40  ? 39  LYS B CE  1 
ATOM   1041 N  NZ  . LYS B 1 40 ? 29.925  -23.477 -29.337 1.00 69.92  ? 39  LYS B NZ  1 
ATOM   1042 N  N   . TYR B 1 41 ? 29.952  -17.106 -32.934 1.00 44.71  ? 40  TYR B N   1 
ATOM   1043 C  CA  . TYR B 1 41 ? 29.839  -15.679 -33.186 1.00 43.00  ? 40  TYR B CA  1 
ATOM   1044 C  C   . TYR B 1 41 ? 29.198  -14.997 -31.988 1.00 41.85  ? 40  TYR B C   1 
ATOM   1045 O  O   . TYR B 1 41 ? 28.421  -15.629 -31.283 1.00 37.10  ? 40  TYR B O   1 
ATOM   1046 C  CB  . TYR B 1 41 ? 28.852  -15.472 -34.335 1.00 41.68  ? 40  TYR B CB  1 
ATOM   1047 C  CG  . TYR B 1 41 ? 29.350  -15.959 -35.684 1.00 42.87  ? 40  TYR B CG  1 
ATOM   1048 C  CD1 . TYR B 1 41 ? 29.920  -15.068 -36.584 1.00 44.79  ? 40  TYR B CD1 1 
ATOM   1049 C  CD2 . TYR B 1 41 ? 29.243  -17.296 -36.054 1.00 44.45  ? 40  TYR B CD2 1 
ATOM   1050 C  CE1 . TYR B 1 41 ? 30.393  -15.492 -37.816 1.00 46.48  ? 40  TYR B CE1 1 
ATOM   1051 C  CE2 . TYR B 1 41 ? 29.702  -17.728 -37.290 1.00 44.24  ? 40  TYR B CE2 1 
ATOM   1052 C  CZ  . TYR B 1 41 ? 30.294  -16.827 -38.161 1.00 44.37  ? 40  TYR B CZ  1 
ATOM   1053 O  OH  . TYR B 1 41 ? 30.731  -17.220 -39.395 1.00 48.53  ? 40  TYR B OH  1 
ATOM   1054 N  N   . PRO B 1 42 ? 29.421  -13.675 -31.780 1.00 43.26  ? 41  PRO B N   1 
ATOM   1055 C  CA  . PRO B 1 42 ? 28.674  -12.934 -30.767 1.00 36.60  ? 41  PRO B CA  1 
ATOM   1056 C  C   . PRO B 1 42 ? 27.251  -12.683 -31.255 1.00 38.92  ? 41  PRO B C   1 
ATOM   1057 O  O   . PRO B 1 42 ? 27.060  -12.046 -32.294 1.00 40.68  ? 41  PRO B O   1 
ATOM   1058 C  CB  . PRO B 1 42 ? 29.448  -11.605 -30.616 1.00 40.22  ? 41  PRO B CB  1 
ATOM   1059 C  CG  . PRO B 1 42 ? 30.252  -11.449 -31.900 1.00 42.05  ? 41  PRO B CG  1 
ATOM   1060 C  CD  . PRO B 1 42 ? 30.356  -12.828 -32.541 1.00 42.79  ? 41  PRO B CD  1 
ATOM   1061 N  N   . ILE B 1 43 ? 26.260  -13.133 -30.469 1.00 34.68  ? 42  ILE B N   1 
ATOM   1062 C  CA  . ILE B 1 43 ? 24.857  -12.947 -30.825 1.00 33.50  ? 42  ILE B CA  1 
ATOM   1063 C  C   . ILE B 1 43 ? 24.204  -11.917 -29.900 1.00 32.11  ? 42  ILE B C   1 
ATOM   1064 O  O   . ILE B 1 43 ? 24.430  -11.941 -28.697 1.00 36.26  ? 42  ILE B O   1 
ATOM   1065 C  CB  . ILE B 1 43 ? 24.111  -14.291 -30.762 1.00 31.89  ? 42  ILE B CB  1 
ATOM   1066 C  CG1 . ILE B 1 43 ? 24.861  -15.408 -31.546 1.00 32.95  ? 42  ILE B CG1 1 
ATOM   1067 C  CG2 . ILE B 1 43 ? 22.673  -14.118 -31.253 1.00 32.99  ? 42  ILE B CG2 1 
ATOM   1068 C  CD1 . ILE B 1 43 ? 25.215  -15.035 -32.980 1.00 33.01  ? 42  ILE B CD1 1 
ATOM   1069 N  N   . PHE B 1 44 ? 23.380  -11.038 -30.471 1.00 31.18  ? 43  PHE B N   1 
ATOM   1070 C  CA  . PHE B 1 44 ? 22.572  -10.105 -29.701 1.00 33.79  ? 43  PHE B CA  1 
ATOM   1071 C  C   . PHE B 1 44 ? 21.107  -10.496 -29.869 1.00 30.70  ? 43  PHE B C   1 
ATOM   1072 O  O   . PHE B 1 44 ? 20.589  -10.545 -30.991 1.00 31.46  ? 43  PHE B O   1 
ATOM   1073 C  CB  . PHE B 1 44 ? 22.831  -8.641  -30.093 1.00 32.19  ? 43  PHE B CB  1 
ATOM   1074 C  CG  . PHE B 1 44 ? 21.899  -7.628  -29.435 1.00 31.74  ? 43  PHE B CG  1 
ATOM   1075 C  CD1 . PHE B 1 44 ? 20.709  -7.237  -30.052 1.00 32.58  ? 43  PHE B CD1 1 
ATOM   1076 C  CD2 . PHE B 1 44 ? 22.198  -7.094  -28.181 1.00 38.02  ? 43  PHE B CD2 1 
ATOM   1077 C  CE1 . PHE B 1 44 ? 19.866  -6.304  -29.455 1.00 33.29  ? 43  PHE B CE1 1 
ATOM   1078 C  CE2 . PHE B 1 44 ? 21.355  -6.155  -27.583 1.00 32.42  ? 43  PHE B CE2 1 
ATOM   1079 C  CZ  . PHE B 1 44 ? 20.192  -5.775  -28.225 1.00 36.59  ? 43  PHE B CZ  1 
ATOM   1080 N  N   . PHE B 1 45 ? 20.450  -10.807 -28.743 1.00 29.96  ? 44  PHE B N   1 
ATOM   1081 C  CA  . PHE B 1 45 ? 19.041  -11.168 -28.799 1.00 29.03  ? 44  PHE B CA  1 
ATOM   1082 C  C   . PHE B 1 45 ? 18.175  -9.923  -28.699 1.00 29.49  ? 44  PHE B C   1 
ATOM   1083 O  O   . PHE B 1 45 ? 18.227  -9.208  -27.695 1.00 32.71  ? 44  PHE B O   1 
ATOM   1084 C  CB  . PHE B 1 45 ? 18.714  -12.145 -27.666 1.00 28.73  ? 44  PHE B CB  1 
ATOM   1085 C  CG  . PHE B 1 45 ? 19.422  -13.479 -27.838 1.00 28.07  ? 44  PHE B CG  1 
ATOM   1086 C  CD1 . PHE B 1 45 ? 20.780  -13.617 -27.545 1.00 30.47  ? 44  PHE B CD1 1 
ATOM   1087 C  CD2 . PHE B 1 45 ? 18.725  -14.600 -28.283 1.00 27.93  ? 44  PHE B CD2 1 
ATOM   1088 C  CE1 . PHE B 1 45 ? 21.423  -14.843 -27.714 1.00 35.34  ? 44  PHE B CE1 1 
ATOM   1089 C  CE2 . PHE B 1 45 ? 19.368  -15.830 -28.420 1.00 33.01  ? 44  PHE B CE2 1 
ATOM   1090 C  CZ  . PHE B 1 45 ? 20.720  -15.946 -28.160 1.00 31.63  ? 44  PHE B CZ  1 
ATOM   1091 N  N   . PHE B 1 46 ? 17.348  -9.678  -29.728 1.00 28.48  ? 45  PHE B N   1 
ATOM   1092 C  CA  . PHE B 1 46 ? 16.379  -8.592  -29.668 1.00 29.24  ? 45  PHE B CA  1 
ATOM   1093 C  C   . PHE B 1 46 ? 15.361  -8.810  -28.536 1.00 31.28  ? 45  PHE B C   1 
ATOM   1094 O  O   . PHE B 1 46 ? 15.056  -9.936  -28.143 1.00 29.16  ? 45  PHE B O   1 
ATOM   1095 C  CB  . PHE B 1 46 ? 15.665  -8.367  -30.995 1.00 27.93  ? 45  PHE B CB  1 
ATOM   1096 C  CG  . PHE B 1 46 ? 16.617  -7.929  -32.103 1.00 33.48  ? 45  PHE B CG  1 
ATOM   1097 C  CD1 . PHE B 1 46 ? 17.082  -6.607  -32.158 1.00 33.21  ? 45  PHE B CD1 1 
ATOM   1098 C  CD2 . PHE B 1 46 ? 16.981  -8.800  -33.131 1.00 31.43  ? 45  PHE B CD2 1 
ATOM   1099 C  CE1 . PHE B 1 46 ? 17.929  -6.183  -33.188 1.00 33.31  ? 45  PHE B CE1 1 
ATOM   1100 C  CE2 . PHE B 1 46 ? 17.863  -8.376  -34.132 1.00 29.68  ? 45  PHE B CE2 1 
ATOM   1101 C  CZ  . PHE B 1 46 ? 18.308  -7.061  -34.170 1.00 28.42  ? 45  PHE B CZ  1 
ATOM   1102 N  N   . GLY B 1 47 ? 14.811  -7.706  -28.035 1.00 29.65  ? 46  GLY B N   1 
ATOM   1103 C  CA  . GLY B 1 47 ? 13.762  -7.775  -27.019 1.00 31.69  ? 46  GLY B CA  1 
ATOM   1104 C  C   . GLY B 1 47 ? 14.369  -7.937  -25.628 1.00 33.93  ? 46  GLY B C   1 
ATOM   1105 O  O   . GLY B 1 47 ? 14.182  -7.092  -24.776 1.00 38.45  ? 46  GLY B O   1 
ATOM   1106 N  N   . THR B 1 48 ? 15.087  -9.029  -25.386 1.00 34.46  ? 47  THR B N   1 
ATOM   1107 C  CA  . THR B 1 48 ? 15.713  -9.222  -24.091 1.00 33.54  ? 47  THR B CA  1 
ATOM   1108 C  C   . THR B 1 48 ? 17.010  -8.424  -24.016 1.00 37.39  ? 47  THR B C   1 
ATOM   1109 O  O   . THR B 1 48 ? 17.496  -8.117  -22.924 1.00 33.55  ? 47  THR B O   1 
ATOM   1110 C  CB  . THR B 1 48 ? 15.994  -10.707 -23.856 1.00 35.74  ? 47  THR B CB  1 
ATOM   1111 O  OG1 . THR B 1 48 ? 17.012  -11.126 -24.767 1.00 31.88  ? 47  THR B OG1 1 
ATOM   1112 C  CG2 . THR B 1 48 ? 14.726  -11.539 -23.899 1.00 35.90  ? 47  THR B CG2 1 
ATOM   1113 N  N   . HIS B 1 49 ? 17.615  -8.177  -25.184 1.00 33.46  ? 48  HIS B N   1 
ATOM   1114 C  CA  . HIS B 1 49 ? 18.889  -7.480  -25.258 1.00 34.18  ? 48  HIS B CA  1 
ATOM   1115 C  C   . HIS B 1 49 ? 19.992  -8.259  -24.552 1.00 34.38  ? 48  HIS B C   1 
ATOM   1116 O  O   . HIS B 1 49 ? 20.963  -7.650  -24.120 1.00 40.76  ? 48  HIS B O   1 
ATOM   1117 C  CB  . HIS B 1 49 ? 18.776  -6.014  -24.792 1.00 37.10  ? 48  HIS B CB  1 
ATOM   1118 C  CG  . HIS B 1 49 ? 17.623  -5.281  -25.393 1.00 34.87  ? 48  HIS B CG  1 
ATOM   1119 N  ND1 . HIS B 1 49 ? 16.892  -4.358  -24.678 1.00 38.96  ? 48  HIS B ND1 1 
ATOM   1120 C  CD2 . HIS B 1 49 ? 17.025  -5.360  -26.608 1.00 33.75  ? 48  HIS B CD2 1 
ATOM   1121 C  CE1 . HIS B 1 49 ? 15.904  -3.892  -25.436 1.00 40.61  ? 48  HIS B CE1 1 
ATOM   1122 N  NE2 . HIS B 1 49 ? 15.975  -4.474  -26.623 1.00 36.13  ? 48  HIS B NE2 1 
ATOM   1123 N  N   . GLU B 1 50 ? 19.856  -9.587  -24.460 1.00 33.70  ? 49  GLU B N   1 
ATOM   1124 C  CA  . GLU B 1 50 ? 20.912  -10.456 -23.966 1.00 37.63  ? 49  GLU B CA  1 
ATOM   1125 C  C   . GLU B 1 50 ? 21.876  -10.795 -25.103 1.00 36.74  ? 49  GLU B C   1 
ATOM   1126 O  O   . GLU B 1 50 ? 21.548  -10.586 -26.275 1.00 36.39  ? 49  GLU B O   1 
ATOM   1127 C  CB  . GLU B 1 50 ? 20.314  -11.785 -23.516 1.00 41.86  ? 49  GLU B CB  1 
ATOM   1128 C  CG  . GLU B 1 50 ? 19.336  -11.644 -22.352 1.00 42.13  ? 49  GLU B CG  1 
ATOM   1129 C  CD  . GLU B 1 50 ? 19.954  -11.740 -20.968 1.00 48.36  ? 49  GLU B CD  1 
ATOM   1130 O  OE1 . GLU B 1 50 ? 21.167  -12.019 -20.860 1.00 50.76  ? 49  GLU B OE1 1 
ATOM   1131 O  OE2 . GLU B 1 50 ? 19.198  -11.554 -19.988 1.00 46.80  ? 49  GLU B OE2 1 
ATOM   1132 N  N   . THR B 1 51 ? 23.054  -11.318 -24.730 1.00 33.94  ? 50  THR B N   1 
ATOM   1133 C  CA  . THR B 1 51 ? 24.090  -11.755 -25.663 1.00 36.35  ? 50  THR B CA  1 
ATOM   1134 C  C   . THR B 1 51 ? 24.514  -13.168 -25.266 1.00 39.14  ? 50  THR B C   1 
ATOM   1135 O  O   . THR B 1 51 ? 24.371  -13.580 -24.113 1.00 37.31  ? 50  THR B O   1 
ATOM   1136 C  CB  . THR B 1 51 ? 25.303  -10.821 -25.667 1.00 38.88  ? 50  THR B CB  1 
ATOM   1137 O  OG1 . THR B 1 51 ? 25.756  -10.931 -24.324 1.00 48.44  ? 50  THR B OG1 1 
ATOM   1138 C  CG2 . THR B 1 51 ? 24.976  -9.362  -25.948 1.00 40.49  ? 50  THR B CG2 1 
ATOM   1139 N  N   . ALA B 1 52 ? 25.018  -13.908 -26.251 1.00 34.95  ? 51  ALA B N   1 
ATOM   1140 C  CA  . ALA B 1 52 ? 25.622  -15.214 -26.049 1.00 35.84  ? 51  ALA B CA  1 
ATOM   1141 C  C   . ALA B 1 52 ? 26.520  -15.501 -27.247 1.00 40.64  ? 51  ALA B C   1 
ATOM   1142 O  O   . ALA B 1 52 ? 26.494  -14.750 -28.228 1.00 42.69  ? 51  ALA B O   1 
ATOM   1143 C  CB  . ALA B 1 52 ? 24.562  -16.260 -25.892 1.00 35.00  ? 51  ALA B CB  1 
ATOM   1144 N  N   . PHE B 1 53 ? 27.309  -16.576 -27.150 1.00 36.67  ? 52  PHE B N   1 
ATOM   1145 C  CA  . PHE B 1 53 ? 28.108  -17.031 -28.280 1.00 47.68  ? 52  PHE B CA  1 
ATOM   1146 C  C   . PHE B 1 53 ? 27.469  -18.302 -28.838 1.00 44.92  ? 52  PHE B C   1 
ATOM   1147 O  O   . PHE B 1 53 ? 27.290  -19.266 -28.096 1.00 42.85  ? 52  PHE B O   1 
ATOM   1148 C  CB  . PHE B 1 53 ? 29.547  -17.311 -27.822 1.00 46.71  ? 52  PHE B CB  1 
ATOM   1149 C  CG  . PHE B 1 53 ? 30.364  -16.112 -27.365 1.00 46.14  ? 52  PHE B CG  1 
ATOM   1150 C  CD1 . PHE B 1 53 ? 30.527  -15.004 -28.187 1.00 51.43  ? 52  PHE B CD1 1 
ATOM   1151 C  CD2 . PHE B 1 53 ? 30.977  -16.101 -26.115 1.00 52.39  ? 52  PHE B CD2 1 
ATOM   1152 C  CE1 . PHE B 1 53 ? 31.279  -13.914 -27.772 1.00 50.47  ? 52  PHE B CE1 1 
ATOM   1153 C  CE2 . PHE B 1 53 ? 31.730  -15.008 -25.700 1.00 53.27  ? 52  PHE B CE2 1 
ATOM   1154 C  CZ  . PHE B 1 53 ? 31.882  -13.919 -26.528 1.00 49.21  ? 52  PHE B CZ  1 
ATOM   1155 N  N   . LEU B 1 54 ? 27.133  -18.303 -30.142 1.00 37.99  ? 53  LEU B N   1 
ATOM   1156 C  CA  . LEU B 1 54 ? 26.512  -19.474 -30.746 1.00 36.01  ? 53  LEU B CA  1 
ATOM   1157 C  C   . LEU B 1 54 ? 27.252  -19.840 -32.035 1.00 38.62  ? 53  LEU B C   1 
ATOM   1158 O  O   . LEU B 1 54 ? 27.773  -18.962 -32.718 1.00 37.14  ? 53  LEU B O   1 
ATOM   1159 C  CB  . LEU B 1 54 ? 25.039  -19.216 -31.062 1.00 34.94  ? 53  LEU B CB  1 
ATOM   1160 C  CG  . LEU B 1 54 ? 24.079  -19.114 -29.870 1.00 36.39  ? 53  LEU B CG  1 
ATOM   1161 C  CD1 . LEU B 1 54 ? 22.758  -18.636 -30.464 1.00 34.03  ? 53  LEU B CD1 1 
ATOM   1162 C  CD2 . LEU B 1 54 ? 23.936  -20.496 -29.189 1.00 34.30  ? 53  LEU B CD2 1 
ATOM   1163 N  N   . GLY B 1 55 ? 27.247  -21.132 -32.365 1.00 37.19  ? 54  GLY B N   1 
ATOM   1164 C  CA  . GLY B 1 55 ? 27.765  -21.602 -33.637 1.00 36.41  ? 54  GLY B CA  1 
ATOM   1165 C  C   . GLY B 1 55 ? 26.659  -21.661 -34.686 1.00 32.75  ? 54  GLY B C   1 
ATOM   1166 O  O   . GLY B 1 55 ? 25.459  -21.587 -34.376 1.00 37.26  ? 54  GLY B O   1 
ATOM   1167 N  N   . PRO B 1 56 ? 27.042  -21.808 -35.972 1.00 30.44  ? 55  PRO B N   1 
ATOM   1168 C  CA  . PRO B 1 56 ? 26.079  -21.802 -37.070 1.00 29.77  ? 55  PRO B CA  1 
ATOM   1169 C  C   . PRO B 1 56 ? 24.917  -22.786 -37.012 1.00 30.76  ? 55  PRO B C   1 
ATOM   1170 O  O   . PRO B 1 56 ? 23.880  -22.524 -37.603 1.00 30.93  ? 55  PRO B O   1 
ATOM   1171 C  CB  . PRO B 1 56 ? 26.935  -21.994 -38.350 1.00 29.99  ? 55  PRO B CB  1 
ATOM   1172 C  CG  . PRO B 1 56 ? 28.373  -21.822 -37.909 1.00 31.52  ? 55  PRO B CG  1 
ATOM   1173 C  CD  . PRO B 1 56 ? 28.441  -21.968 -36.401 1.00 32.57  ? 55  PRO B CD  1 
ATOM   1174 N  N   . LYS B 1 57 ? 25.081  -23.913 -36.297 1.00 36.65  ? 56  LYS B N   1 
ATOM   1175 C  CA  . LYS B 1 57 ? 24.041  -24.935 -36.273 1.00 38.27  ? 56  LYS B CA  1 
ATOM   1176 C  C   . LYS B 1 57 ? 22.793  -24.347 -35.621 1.00 35.92  ? 56  LYS B C   1 
ATOM   1177 O  O   . LYS B 1 57 ? 21.679  -24.814 -35.866 1.00 32.43  ? 56  LYS B O   1 
ATOM   1178 C  CB  . LYS B 1 57 ? 24.433  -26.231 -35.544 1.00 37.08  ? 56  LYS B CB  1 
ATOM   1179 C  CG  . LYS B 1 57 ? 24.622  -26.143 -34.039 1.00 39.71  ? 56  LYS B CG  1 
ATOM   1180 C  CD  . LYS B 1 57 ? 24.747  -27.541 -33.440 1.00 43.54  ? 56  LYS B CD  1 
ATOM   1181 C  CE  . LYS B 1 57 ? 25.081  -27.536 -31.974 1.00 54.02  ? 56  LYS B CE  1 
ATOM   1182 N  NZ  . LYS B 1 57 ? 23.986  -27.014 -31.147 1.00 58.66  ? 56  LYS B NZ  1 
ATOM   1183 N  N   . ASP B 1 58 ? 23.017  -23.304 -34.814 1.00 34.56  ? 57  ASP B N   1 
ATOM   1184 C  CA  . ASP B 1 58 ? 21.957  -22.685 -34.034 1.00 35.75  ? 57  ASP B CA  1 
ATOM   1185 C  C   . ASP B 1 58 ? 21.544  -21.324 -34.600 1.00 34.15  ? 57  ASP B C   1 
ATOM   1186 O  O   . ASP B 1 58 ? 20.775  -20.604 -33.953 1.00 31.61  ? 57  ASP B O   1 
ATOM   1187 C  CB  . ASP B 1 58 ? 22.361  -22.606 -32.569 1.00 37.71  ? 57  ASP B CB  1 
ATOM   1188 C  CG  . ASP B 1 58 ? 22.444  -23.939 -31.838 1.00 39.62  ? 57  ASP B CG  1 
ATOM   1189 O  OD1 . ASP B 1 58 ? 21.525  -24.753 -32.022 1.00 36.34  ? 57  ASP B OD1 1 
ATOM   1190 O  OD2 . ASP B 1 58 ? 23.412  -24.129 -31.080 1.00 41.84  ? 57  ASP B OD2 1 
ATOM   1191 N  N   . LEU B 1 59 ? 22.015  -20.992 -35.819 1.00 35.58  ? 58  LEU B N   1 
ATOM   1192 C  CA  . LEU B 1 59 ? 21.768  -19.679 -36.400 1.00 32.39  ? 58  LEU B CA  1 
ATOM   1193 C  C   . LEU B 1 59 ? 21.041  -19.841 -37.728 1.00 34.68  ? 58  LEU B C   1 
ATOM   1194 O  O   . LEU B 1 59 ? 21.541  -20.494 -38.642 1.00 35.56  ? 58  LEU B O   1 
ATOM   1195 C  CB  . LEU B 1 59 ? 23.065  -18.890 -36.580 1.00 35.05  ? 58  LEU B CB  1 
ATOM   1196 C  CG  . LEU B 1 59 ? 23.901  -18.660 -35.319 1.00 34.74  ? 58  LEU B CG  1 
ATOM   1197 C  CD1 . LEU B 1 59 ? 25.218  -18.021 -35.676 1.00 33.28  ? 58  LEU B CD1 1 
ATOM   1198 C  CD2 . LEU B 1 59 ? 23.153  -17.808 -34.301 1.00 31.08  ? 58  LEU B CD2 1 
ATOM   1199 N  N   . PHE B 1 60 ? 19.868  -19.226 -37.818 1.00 31.31  ? 59  PHE B N   1 
ATOM   1200 C  CA  . PHE B 1 60 ? 18.978  -19.389 -38.953 1.00 32.62  ? 59  PHE B CA  1 
ATOM   1201 C  C   . PHE B 1 60 ? 18.793  -18.029 -39.630 1.00 35.78  ? 59  PHE B C   1 
ATOM   1202 O  O   . PHE B 1 60 ? 18.132  -17.155 -39.082 1.00 30.76  ? 59  PHE B O   1 
ATOM   1203 C  CB  . PHE B 1 60 ? 17.645  -19.949 -38.448 1.00 32.30  ? 59  PHE B CB  1 
ATOM   1204 C  CG  . PHE B 1 60 ? 17.734  -21.363 -37.862 1.00 28.28  ? 59  PHE B CG  1 
ATOM   1205 C  CD1 . PHE B 1 60 ? 18.199  -21.573 -36.567 1.00 30.59  ? 59  PHE B CD1 1 
ATOM   1206 C  CD2 . PHE B 1 60 ? 17.354  -22.469 -38.621 1.00 30.50  ? 59  PHE B CD2 1 
ATOM   1207 C  CE1 . PHE B 1 60 ? 18.315  -22.868 -36.055 1.00 32.60  ? 59  PHE B CE1 1 
ATOM   1208 C  CE2 . PHE B 1 60 ? 17.415  -23.757 -38.099 1.00 31.19  ? 59  PHE B CE2 1 
ATOM   1209 C  CZ  . PHE B 1 60 ? 17.909  -23.952 -36.812 1.00 30.24  ? 59  PHE B CZ  1 
ATOM   1210 N  N   . PRO B 1 61 ? 19.344  -17.810 -40.850 1.00 38.49  ? 60  PRO B N   1 
ATOM   1211 C  CA  . PRO B 1 61 ? 19.024  -16.602 -41.624 1.00 36.48  ? 60  PRO B CA  1 
ATOM   1212 C  C   . PRO B 1 61 ? 17.577  -16.119 -41.540 1.00 34.70  ? 60  PRO B C   1 
ATOM   1213 O  O   . PRO B 1 61 ? 16.645  -16.883 -41.789 1.00 34.56  ? 60  PRO B O   1 
ATOM   1214 C  CB  . PRO B 1 61 ? 19.480  -16.988 -43.045 1.00 37.91  ? 60  PRO B CB  1 
ATOM   1215 C  CG  . PRO B 1 61 ? 20.690  -17.858 -42.788 1.00 41.58  ? 60  PRO B CG  1 
ATOM   1216 C  CD  . PRO B 1 61 ? 20.361  -18.656 -41.507 1.00 41.19  ? 60  PRO B CD  1 
ATOM   1217 N  N   . TYR B 1 62 ? 17.395  -14.824 -41.201 1.00 32.30  ? 61  TYR B N   1 
ATOM   1218 C  CA  . TYR B 1 62 ? 16.094  -14.296 -40.803 1.00 36.53  ? 61  TYR B CA  1 
ATOM   1219 C  C   . TYR B 1 62 ? 15.101  -14.309 -41.960 1.00 40.11  ? 61  TYR B C   1 
ATOM   1220 O  O   . TYR B 1 62 ? 13.940  -14.696 -41.798 1.00 39.07  ? 61  TYR B O   1 
ATOM   1221 C  CB  . TYR B 1 62 ? 16.252  -12.853 -40.308 1.00 39.52  ? 61  TYR B CB  1 
ATOM   1222 C  CG  . TYR B 1 62 ? 14.939  -12.116 -40.108 1.00 38.12  ? 61  TYR B CG  1 
ATOM   1223 C  CD1 . TYR B 1 62 ? 14.167  -12.322 -38.971 1.00 40.74  ? 61  TYR B CD1 1 
ATOM   1224 C  CD2 . TYR B 1 62 ? 14.511  -11.162 -41.023 1.00 45.10  ? 61  TYR B CD2 1 
ATOM   1225 C  CE1 . TYR B 1 62 ? 12.988  -11.623 -38.768 1.00 42.58  ? 61  TYR B CE1 1 
ATOM   1226 C  CE2 . TYR B 1 62 ? 13.332  -10.462 -40.837 1.00 46.44  ? 61  TYR B CE2 1 
ATOM   1227 C  CZ  . TYR B 1 62 ? 12.574  -10.691 -39.702 1.00 42.14  ? 61  TYR B CZ  1 
ATOM   1228 O  OH  . TYR B 1 62 ? 11.419  -9.995  -39.534 1.00 49.71  ? 61  TYR B OH  1 
ATOM   1229 N  N   . ASP B 1 63 ? 15.586  -13.885 -43.130 1.00 49.60  ? 62  ASP B N   1 
ATOM   1230 C  CA  . ASP B 1 63 ? 14.791  -13.851 -44.346 1.00 52.37  ? 62  ASP B CA  1 
ATOM   1231 C  C   . ASP B 1 63 ? 14.241  -15.232 -44.690 1.00 46.72  ? 62  ASP B C   1 
ATOM   1232 O  O   . ASP B 1 63 ? 13.034  -15.377 -44.875 1.00 46.06  ? 62  ASP B O   1 
ATOM   1233 C  CB  . ASP B 1 63 ? 15.529  -13.150 -45.470 1.00 61.43  ? 62  ASP B CB  1 
ATOM   1234 C  CG  . ASP B 1 63 ? 14.972  -11.773 -45.783 1.00 74.04  ? 62  ASP B CG  1 
ATOM   1235 O  OD1 . ASP B 1 63 ? 15.034  -10.892 -44.891 1.00 74.75  ? 62  ASP B OD1 1 
ATOM   1236 O  OD2 . ASP B 1 63 ? 14.432  -11.619 -46.901 1.00 85.91  ? 62  ASP B OD2 1 
ATOM   1237 N  N   . LYS B 1 64 ? 15.120  -16.240 -44.730 1.00 48.70  ? 63  LYS B N   1 
ATOM   1238 C  CA  . LYS B 1 64 ? 14.699  -17.598 -45.044 1.00 46.34  ? 63  LYS B CA  1 
ATOM   1239 C  C   . LYS B 1 64 ? 13.625  -18.093 -44.066 1.00 47.55  ? 63  LYS B C   1 
ATOM   1240 O  O   . LYS B 1 64 ? 12.676  -18.749 -44.477 1.00 47.22  ? 63  LYS B O   1 
ATOM   1241 C  CB  . LYS B 1 64 ? 15.896  -18.554 -45.040 1.00 45.78  ? 63  LYS B CB  1 
ATOM   1242 C  CG  . LYS B 1 64 ? 15.599  -19.936 -45.630 1.00 46.07  ? 63  LYS B CG  1 
ATOM   1243 C  CD  . LYS B 1 64 ? 16.774  -20.904 -45.592 1.00 53.88  ? 63  LYS B CD  1 
ATOM   1244 C  CE  . LYS B 1 64 ? 16.581  -22.230 -46.282 1.00 50.03  ? 63  LYS B CE  1 
ATOM   1245 N  NZ  . LYS B 1 64 ? 15.260  -22.823 -46.080 1.00 50.05  ? 63  LYS B NZ  1 
ATOM   1246 N  N   . SER B 1 65 ? 13.755  -17.764 -42.774 1.00 43.40  ? 64  SER B N   1 
ATOM   1247 C  CA  . SER B 1 65 ? 13.056  -18.526 -41.745 1.00 40.14  ? 64  SER B CA  1 
ATOM   1248 C  C   . SER B 1 65 ? 11.951  -17.741 -41.015 1.00 39.94  ? 64  SER B C   1 
ATOM   1249 O  O   . SER B 1 65 ? 11.285  -18.288 -40.133 1.00 38.97  ? 64  SER B O   1 
ATOM   1250 C  CB  . SER B 1 65 ? 14.072  -19.084 -40.792 1.00 40.95  ? 64  SER B CB  1 
ATOM   1251 O  OG  . SER B 1 65 ? 14.774  -18.011 -40.198 1.00 48.66  ? 64  SER B OG  1 
ATOM   1252 N  N   . LYS B 1 66 ? 11.704  -16.481 -41.407 1.00 40.05  ? 65  LYS B N   1 
ATOM   1253 C  CA  . LYS B 1 66 ? 10.847  -15.573 -40.655 1.00 44.13  ? 65  LYS B CA  1 
ATOM   1254 C  C   . LYS B 1 66 ? 9.404   -16.061 -40.613 1.00 47.33  ? 65  LYS B C   1 
ATOM   1255 O  O   . LYS B 1 66 ? 8.701   -15.768 -39.650 1.00 55.48  ? 65  LYS B O   1 
ATOM   1256 C  CB  . LYS B 1 66 ? 10.893  -14.098 -41.092 1.00 45.94  ? 65  LYS B CB  1 
ATOM   1257 C  CG  . LYS B 1 66 ? 10.757  -13.880 -42.593 1.00 49.15  ? 65  LYS B CG  1 
ATOM   1258 C  CD  . LYS B 1 66 ? 10.695  -12.442 -43.099 1.00 55.56  ? 65  LYS B CD  1 
ATOM   1259 C  CE  . LYS B 1 66 ? 10.497  -12.434 -44.593 1.00 60.02  ? 65  LYS B CE  1 
ATOM   1260 N  NZ  . LYS B 1 66 ? 9.427   -13.352 -45.013 1.00 62.87  ? 65  LYS B NZ  1 
ATOM   1261 N  N   . ASP B 1 67 ? 8.943   -16.808 -41.624 1.00 50.06  ? 66  ASP B N   1 
ATOM   1262 C  CA  . ASP B 1 67 ? 7.550   -17.221 -41.525 1.00 55.68  ? 66  ASP B CA  1 
ATOM   1263 C  C   . ASP B 1 67 ? 7.429   -18.489 -40.677 1.00 52.13  ? 66  ASP B C   1 
ATOM   1264 O  O   . ASP B 1 67 ? 6.364   -18.786 -40.139 1.00 51.45  ? 66  ASP B O   1 
ATOM   1265 C  CB  . ASP B 1 67 ? 6.785   -17.151 -42.839 1.00 69.66  ? 66  ASP B CB  1 
ATOM   1266 C  CG  . ASP B 1 67 ? 7.073   -18.236 -43.865 1.00 83.64  ? 66  ASP B CG  1 
ATOM   1267 O  OD1 . ASP B 1 67 ? 7.277   -17.877 -45.048 1.00 96.37  ? 66  ASP B OD1 1 
ATOM   1268 O  OD2 . ASP B 1 67 ? 7.076   -19.425 -43.480 1.00 85.22  ? 66  ASP B OD2 1 
ATOM   1269 N  N   . LYS B 1 68 ? 8.531   -19.223 -40.532 1.00 46.57  ? 67  LYS B N   1 
ATOM   1270 C  CA  . LYS B 1 68 ? 8.524   -20.377 -39.647 1.00 42.21  ? 67  LYS B CA  1 
ATOM   1271 C  C   . LYS B 1 68 ? 8.666   -19.917 -38.195 1.00 41.63  ? 67  LYS B C   1 
ATOM   1272 O  O   . LYS B 1 68 ? 7.881   -20.326 -37.342 1.00 40.20  ? 67  LYS B O   1 
ATOM   1273 C  CB  . LYS B 1 68 ? 9.597   -21.343 -40.144 1.00 46.55  ? 67  LYS B CB  1 
ATOM   1274 C  CG  . LYS B 1 68 ? 9.715   -22.654 -39.400 1.00 59.23  ? 67  LYS B CG  1 
ATOM   1275 C  CD  . LYS B 1 68 ? 10.615  -23.556 -40.235 1.00 67.83  ? 67  LYS B CD  1 
ATOM   1276 C  CE  . LYS B 1 68 ? 11.060  -24.784 -39.503 1.00 79.56  ? 67  LYS B CE  1 
ATOM   1277 N  NZ  . LYS B 1 68 ? 9.955   -25.693 -39.187 1.00 80.74  ? 67  LYS B NZ  1 
ATOM   1278 N  N   . TYR B 1 69 ? 9.642   -19.038 -37.917 1.00 37.49  ? 68  TYR B N   1 
ATOM   1279 C  CA  . TYR B 1 69 ? 10.006  -18.751 -36.527 1.00 33.53  ? 68  TYR B CA  1 
ATOM   1280 C  C   . TYR B 1 69 ? 9.419   -17.432 -36.018 1.00 40.57  ? 68  TYR B C   1 
ATOM   1281 O  O   . TYR B 1 69 ? 9.500   -17.132 -34.821 1.00 38.99  ? 68  TYR B O   1 
ATOM   1282 C  CB  . TYR B 1 69 ? 11.536  -18.776 -36.443 1.00 32.67  ? 68  TYR B CB  1 
ATOM   1283 C  CG  . TYR B 1 69 ? 12.106  -20.160 -36.757 1.00 32.98  ? 68  TYR B CG  1 
ATOM   1284 C  CD1 . TYR B 1 69 ? 11.513  -21.316 -36.255 1.00 33.57  ? 68  TYR B CD1 1 
ATOM   1285 C  CD2 . TYR B 1 69 ? 13.240  -20.305 -37.552 1.00 33.21  ? 68  TYR B CD2 1 
ATOM   1286 C  CE1 . TYR B 1 69 ? 12.028  -22.578 -36.529 1.00 38.87  ? 68  TYR B CE1 1 
ATOM   1287 C  CE2 . TYR B 1 69 ? 13.765  -21.552 -37.841 1.00 36.05  ? 68  TYR B CE2 1 
ATOM   1288 C  CZ  . TYR B 1 69 ? 13.149  -22.690 -37.338 1.00 38.90  ? 68  TYR B CZ  1 
ATOM   1289 O  OH  . TYR B 1 69 ? 13.669  -23.906 -37.635 1.00 37.11  ? 68  TYR B OH  1 
ATOM   1290 N  N   . GLY B 1 70 ? 8.820   -16.637 -36.909 1.00 39.43  ? 69  GLY B N   1 
ATOM   1291 C  CA  . GLY B 1 70 ? 8.490   -15.274 -36.523 1.00 49.53  ? 69  GLY B CA  1 
ATOM   1292 C  C   . GLY B 1 70 ? 7.095   -15.109 -35.921 1.00 49.93  ? 69  GLY B C   1 
ATOM   1293 O  O   . GLY B 1 70 ? 6.501   -14.048 -36.078 1.00 54.12  ? 69  GLY B O   1 
ATOM   1294 N  N   . LYS B 1 71 ? 6.581   -16.137 -35.237 1.00 48.19  ? 70  LYS B N   1 
ATOM   1295 C  CA  . LYS B 1 71 ? 5.243   -16.077 -34.675 1.00 53.63  ? 70  LYS B CA  1 
ATOM   1296 C  C   . LYS B 1 71 ? 5.324   -15.640 -33.219 1.00 55.93  ? 70  LYS B C   1 
ATOM   1297 O  O   . LYS B 1 71 ? 6.061   -16.256 -32.447 1.00 53.37  ? 70  LYS B O   1 
ATOM   1298 C  CB  . LYS B 1 71 ? 4.520   -17.428 -34.664 1.00 52.64  ? 70  LYS B CB  1 
ATOM   1299 C  CG  . LYS B 1 71 ? 3.608   -17.714 -35.850 1.00 63.28  ? 70  LYS B CG  1 
ATOM   1300 C  CD  . LYS B 1 71 ? 4.336   -17.780 -37.184 1.00 66.43  ? 70  LYS B CD  1 
ATOM   1301 C  CE  . LYS B 1 71 ? 3.435   -18.044 -38.354 1.00 69.02  ? 70  LYS B CE  1 
ATOM   1302 N  NZ  . LYS B 1 71 ? 4.149   -17.788 -39.610 1.00 60.29  ? 70  LYS B NZ  1 
ATOM   1303 N  N   . PRO B 1 72 ? 4.515   -14.632 -32.803 1.00 57.12  ? 71  PRO B N   1 
ATOM   1304 C  CA  . PRO B 1 72 ? 4.526   -14.140 -31.420 1.00 52.52  ? 71  PRO B CA  1 
ATOM   1305 C  C   . PRO B 1 72 ? 4.193   -15.287 -30.472 1.00 53.50  ? 71  PRO B C   1 
ATOM   1306 O  O   . PRO B 1 72 ? 3.510   -16.225 -30.881 1.00 44.78  ? 71  PRO B O   1 
ATOM   1307 C  CB  . PRO B 1 72 ? 3.462   -13.021 -31.367 1.00 52.49  ? 71  PRO B CB  1 
ATOM   1308 C  CG  . PRO B 1 72 ? 3.147   -12.721 -32.818 1.00 58.10  ? 71  PRO B CG  1 
ATOM   1309 C  CD  . PRO B 1 72 ? 3.500   -13.957 -33.633 1.00 56.90  ? 71  PRO B CD  1 
ATOM   1310 N  N   . ASN B 1 73 ? 4.696   -15.204 -29.225 1.00 47.64  ? 72  ASN B N   1 
ATOM   1311 C  CA  . ASN B 1 73 ? 4.423   -16.212 -28.208 1.00 46.28  ? 72  ASN B CA  1 
ATOM   1312 C  C   . ASN B 1 73 ? 4.431   -15.538 -26.828 1.00 44.19  ? 72  ASN B C   1 
ATOM   1313 O  O   . ASN B 1 73 ? 4.450   -14.310 -26.738 1.00 48.05  ? 72  ASN B O   1 
ATOM   1314 C  CB  . ASN B 1 73 ? 5.387   -17.390 -28.326 1.00 42.27  ? 72  ASN B CB  1 
ATOM   1315 C  CG  . ASN B 1 73 ? 6.817   -16.943 -28.151 1.00 40.82  ? 72  ASN B CG  1 
ATOM   1316 O  OD1 . ASN B 1 73 ? 7.114   -16.205 -27.202 1.00 42.58  ? 72  ASN B OD1 1 
ATOM   1317 N  ND2 . ASN B 1 73 ? 7.705   -17.339 -29.054 1.00 39.87  ? 72  ASN B ND2 1 
ATOM   1318 N  N   . LYS B 1 74 ? 4.511   -16.336 -25.763 0.52 40.08  ? 73  LYS B N   1 
ATOM   1319 C  CA  . LYS B 1 74 ? 4.300   -15.825 -24.416 0.52 41.70  ? 73  LYS B CA  1 
ATOM   1320 C  C   . LYS B 1 74 ? 5.616   -15.654 -23.663 0.52 36.60  ? 73  LYS B C   1 
ATOM   1321 O  O   . LYS B 1 74 ? 5.619   -15.487 -22.443 0.52 28.90  ? 73  LYS B O   1 
ATOM   1322 C  CB  . LYS B 1 74 ? 3.451   -16.861 -23.679 1.00 50.49  ? 73  LYS B CB  1 
ATOM   1323 C  CG  . LYS B 1 74 ? 1.960   -16.735 -23.940 1.00 58.93  ? 73  LYS B CG  1 
ATOM   1324 C  CD  . LYS B 1 74 ? 1.221   -18.069 -23.900 1.00 70.70  ? 73  LYS B CD  1 
ATOM   1325 C  CE  . LYS B 1 74 ? 1.768   -19.083 -22.939 1.00 70.42  ? 73  LYS B CE  1 
ATOM   1326 N  NZ  . LYS B 1 74 ? 0.979   -20.314 -23.014 1.00 74.99  ? 73  LYS B NZ  1 
ATOM   1327 N  N   . ARG B 1 75 ? 6.732   -15.743 -24.390 1.00 32.87  ? 74  ARG B N   1 
ATOM   1328 C  CA  . ARG B 1 75 ? 8.040   -15.579 -23.785 1.00 33.31  ? 74  ARG B CA  1 
ATOM   1329 C  C   . ARG B 1 75 ? 8.326   -14.084 -23.653 1.00 36.12  ? 74  ARG B C   1 
ATOM   1330 O  O   . ARG B 1 75 ? 8.037   -13.319 -24.574 1.00 34.53  ? 74  ARG B O   1 
ATOM   1331 C  CB  . ARG B 1 75 ? 9.139   -16.379 -24.500 1.00 40.49  ? 74  ARG B CB  1 
ATOM   1332 C  CG  . ARG B 1 75 ? 8.934   -17.881 -24.684 1.00 36.49  ? 74  ARG B CG  1 
ATOM   1333 C  CD  . ARG B 1 75 ? 8.978   -18.656 -23.358 1.00 36.32  ? 74  ARG B CD  1 
ATOM   1334 N  NE  . ARG B 1 75 ? 9.161   -20.096 -23.572 1.00 38.46  ? 74  ARG B NE  1 
ATOM   1335 C  CZ  . ARG B 1 75 ? 10.279  -20.758 -23.379 1.00 35.43  ? 74  ARG B CZ  1 
ATOM   1336 N  NH1 . ARG B 1 75 ? 11.369  -20.158 -22.918 1.00 41.82  ? 74  ARG B NH1 1 
ATOM   1337 N  NH2 . ARG B 1 75 ? 10.309  -22.042 -23.681 1.00 41.28  ? 74  ARG B NH2 1 
ATOM   1338 N  N   . LYS B 1 76 ? 8.860   -13.683 -22.479 1.00 32.20  ? 75  LYS B N   1 
ATOM   1339 C  CA  . LYS B 1 76 ? 9.162   -12.300 -22.153 1.00 32.38  ? 75  LYS B CA  1 
ATOM   1340 C  C   . LYS B 1 76 ? 10.248  -11.782 -23.102 1.00 29.17  ? 75  LYS B C   1 
ATOM   1341 O  O   . LYS B 1 76 ? 11.313  -12.388 -23.197 1.00 31.49  ? 75  LYS B O   1 
ATOM   1342 C  CB  . LYS B 1 76 ? 9.677   -12.240 -20.705 1.00 34.06  ? 75  LYS B CB  1 
ATOM   1343 C  CG  . LYS B 1 76 ? 10.004  -10.796 -20.262 1.00 36.67  ? 75  LYS B CG  1 
ATOM   1344 C  CD  . LYS B 1 76 ? 10.597  -10.718 -18.858 1.00 37.98  ? 75  LYS B CD  1 
ATOM   1345 C  CE  . LYS B 1 76 ? 10.894  -9.303  -18.430 1.00 46.80  ? 75  LYS B CE  1 
ATOM   1346 N  NZ  . LYS B 1 76 ? 11.262  -9.264  -17.008 1.00 52.24  ? 75  LYS B NZ  1 
ATOM   1347 N  N   . GLY B 1 77 ? 9.965   -10.656 -23.762 1.00 32.54  ? 76  GLY B N   1 
ATOM   1348 C  CA  . GLY B 1 77 ? 10.888  -9.971  -24.664 1.00 32.03  ? 76  GLY B CA  1 
ATOM   1349 C  C   . GLY B 1 77 ? 10.683  -10.366 -26.134 1.00 34.08  ? 76  GLY B C   1 
ATOM   1350 O  O   . GLY B 1 77 ? 11.240  -9.741  -27.025 1.00 35.49  ? 76  GLY B O   1 
ATOM   1351 N  N   . PHE B 1 78 ? 9.882   -11.409 -26.397 1.00 34.87  ? 77  PHE B N   1 
ATOM   1352 C  CA  . PHE B 1 78 ? 9.822   -12.013 -27.723 1.00 32.99  ? 77  PHE B CA  1 
ATOM   1353 C  C   . PHE B 1 78 ? 9.102   -11.106 -28.706 1.00 34.86  ? 77  PHE B C   1 
ATOM   1354 O  O   . PHE B 1 78 ? 9.593   -10.872 -29.816 1.00 32.39  ? 77  PHE B O   1 
ATOM   1355 C  CB  . PHE B 1 78 ? 9.146   -13.387 -27.718 1.00 31.07  ? 77  PHE B CB  1 
ATOM   1356 C  CG  . PHE B 1 78 ? 9.369   -14.116 -29.035 1.00 32.32  ? 77  PHE B CG  1 
ATOM   1357 C  CD1 . PHE B 1 78 ? 10.507  -14.903 -29.221 1.00 29.96  ? 77  PHE B CD1 1 
ATOM   1358 C  CD2 . PHE B 1 78 ? 8.437   -14.016 -30.068 1.00 33.70  ? 77  PHE B CD2 1 
ATOM   1359 C  CE1 . PHE B 1 78 ? 10.720  -15.579 -30.413 1.00 29.96  ? 77  PHE B CE1 1 
ATOM   1360 C  CE2 . PHE B 1 78 ? 8.652   -14.696 -31.260 1.00 37.72  ? 77  PHE B CE2 1 
ATOM   1361 C  CZ  . PHE B 1 78 ? 9.789   -15.483 -31.418 1.00 33.26  ? 77  PHE B CZ  1 
ATOM   1362 N  N   . ASN B 1 79 ? 7.931   -10.602 -28.315 1.00 32.73  ? 78  ASN B N   1 
ATOM   1363 C  CA  . ASN B 1 79 ? 7.185   -9.766  -29.241 1.00 33.70  ? 78  ASN B CA  1 
ATOM   1364 C  C   . ASN B 1 79 ? 7.919   -8.440  -29.451 1.00 36.09  ? 78  ASN B C   1 
ATOM   1365 O  O   . ASN B 1 79 ? 7.870   -7.855  -30.534 1.00 38.57  ? 78  ASN B O   1 
ATOM   1366 C  CB  . ASN B 1 79 ? 5.741   -9.559  -28.801 1.00 38.37  ? 78  ASN B CB  1 
ATOM   1367 C  CG  . ASN B 1 79 ? 4.965   -10.854 -28.820 1.00 46.18  ? 78  ASN B CG  1 
ATOM   1368 O  OD1 . ASN B 1 79 ? 5.405   -11.853 -29.405 1.00 48.81  ? 78  ASN B OD1 1 
ATOM   1369 N  ND2 . ASN B 1 79 ? 3.831   -10.875 -28.138 1.00 47.83  ? 78  ASN B ND2 1 
ATOM   1370 N  N   . GLU B 1 80 ? 8.607   -7.980  -28.414 1.00 32.96  ? 79  GLU B N   1 
ATOM   1371 C  CA  . GLU B 1 80 ? 9.413   -6.775  -28.530 1.00 40.63  ? 79  GLU B CA  1 
ATOM   1372 C  C   . GLU B 1 80 ? 10.609  -7.033  -29.462 1.00 34.62  ? 79  GLU B C   1 
ATOM   1373 O  O   . GLU B 1 80 ? 10.985  -6.143  -30.212 1.00 34.02  ? 79  GLU B O   1 
ATOM   1374 C  CB  . GLU B 1 80 ? 9.776   -6.212  -27.152 1.00 39.84  ? 79  GLU B CB  1 
ATOM   1375 C  CG  . GLU B 1 80 ? 10.677  -4.978  -27.204 1.00 55.91  ? 79  GLU B CG  1 
ATOM   1376 C  CD  . GLU B 1 80 ? 10.226  -3.605  -27.726 1.00 77.08  ? 79  GLU B CD  1 
ATOM   1377 O  OE1 . GLU B 1 80 ? 9.061   -3.375  -28.169 1.00 72.19  ? 79  GLU B OE1 1 
ATOM   1378 O  OE2 . GLU B 1 80 ? 11.120  -2.720  -27.688 1.00 80.29  ? 79  GLU B OE2 1 
ATOM   1379 N  N   . GLY B 1 81 ? 11.194  -8.245  -29.405 1.00 33.55  ? 80  GLY B N   1 
ATOM   1380 C  CA  . GLY B 1 81 ? 12.329  -8.622  -30.237 1.00 30.78  ? 80  GLY B CA  1 
ATOM   1381 C  C   . GLY B 1 81 ? 11.908  -8.678  -31.702 1.00 34.19  ? 80  GLY B C   1 
ATOM   1382 O  O   . GLY B 1 81 ? 12.679  -8.300  -32.597 1.00 32.98  ? 80  GLY B O   1 
ATOM   1383 N  N   . LEU B 1 82 ? 10.669  -9.136  -31.916 1.00 28.61  ? 81  LEU B N   1 
ATOM   1384 C  CA  . LEU B 1 82 ? 10.078  -9.136  -33.245 1.00 35.02  ? 81  LEU B CA  1 
ATOM   1385 C  C   . LEU B 1 82 ? 9.957   -7.700  -33.745 1.00 33.70  ? 81  LEU B C   1 
ATOM   1386 O  O   . LEU B 1 82 ? 10.232  -7.417  -34.911 1.00 35.48  ? 81  LEU B O   1 
ATOM   1387 C  CB  . LEU B 1 82 ? 8.744   -9.880  -33.323 1.00 33.06  ? 81  LEU B CB  1 
ATOM   1388 C  CG  . LEU B 1 82 ? 8.813   -11.405 -33.138 1.00 30.56  ? 81  LEU B CG  1 
ATOM   1389 C  CD1 . LEU B 1 82 ? 7.422   -11.966 -33.271 1.00 35.18  ? 81  LEU B CD1 1 
ATOM   1390 C  CD2 . LEU B 1 82 ? 9.750   -12.041 -34.156 1.00 27.42  ? 81  LEU B CD2 1 
ATOM   1391 N  N   . TRP B 1 83 ? 9.520   -6.790  -32.877 1.00 31.49  ? 82  TRP B N   1 
ATOM   1392 C  CA  . TRP B 1 83 ? 9.431   -5.391  -33.277 1.00 35.05  ? 82  TRP B CA  1 
ATOM   1393 C  C   . TRP B 1 83 ? 10.812  -4.833  -33.640 1.00 32.80  ? 82  TRP B C   1 
ATOM   1394 O  O   . TRP B 1 83 ? 10.948  -4.083  -34.598 1.00 37.24  ? 82  TRP B O   1 
ATOM   1395 C  CB  . TRP B 1 83 ? 8.791   -4.527  -32.186 1.00 35.05  ? 82  TRP B CB  1 
ATOM   1396 C  CG  . TRP B 1 83 ? 8.516   -3.133  -32.681 1.00 38.09  ? 82  TRP B CG  1 
ATOM   1397 C  CD1 . TRP B 1 83 ? 7.362   -2.687  -33.260 1.00 39.65  ? 82  TRP B CD1 1 
ATOM   1398 C  CD2 . TRP B 1 83 ? 9.443   -2.019  -32.695 1.00 39.40  ? 82  TRP B CD2 1 
ATOM   1399 N  NE1 . TRP B 1 83 ? 7.500   -1.369  -33.612 1.00 40.15  ? 82  TRP B NE1 1 
ATOM   1400 C  CE2 . TRP B 1 83 ? 8.761   -0.932  -33.285 1.00 38.69  ? 82  TRP B CE2 1 
ATOM   1401 C  CE3 . TRP B 1 83 ? 10.773  -1.834  -32.267 1.00 39.57  ? 82  TRP B CE3 1 
ATOM   1402 C  CZ2 . TRP B 1 83 ? 9.365   0.317   -33.457 1.00 40.85  ? 82  TRP B CZ2 1 
ATOM   1403 C  CZ3 . TRP B 1 83 ? 11.371  -0.599  -32.437 1.00 40.23  ? 82  TRP B CZ3 1 
ATOM   1404 C  CH2 . TRP B 1 83 ? 10.674  0.457   -33.030 1.00 42.19  ? 82  TRP B CH2 1 
ATOM   1405 N  N   . GLU B 1 84 ? 11.833  -5.206  -32.870 1.00 31.74  ? 83  GLU B N   1 
ATOM   1406 C  CA  . GLU B 1 84 ? 13.160  -4.642  -33.042 1.00 34.31  ? 83  GLU B CA  1 
ATOM   1407 C  C   . GLU B 1 84 ? 13.788  -5.087  -34.366 1.00 35.06  ? 83  GLU B C   1 
ATOM   1408 O  O   . GLU B 1 84 ? 14.380  -4.275  -35.079 1.00 32.27  ? 83  GLU B O   1 
ATOM   1409 C  CB  . GLU B 1 84 ? 14.051  -5.035  -31.873 1.00 30.85  ? 83  GLU B CB  1 
ATOM   1410 C  CG  . GLU B 1 84 ? 13.599  -4.373  -30.576 1.00 34.28  ? 83  GLU B CG  1 
ATOM   1411 C  CD  . GLU B 1 84 ? 14.514  -4.620  -29.400 1.00 35.37  ? 83  GLU B CD  1 
ATOM   1412 O  OE1 . GLU B 1 84 ? 15.470  -5.415  -29.486 1.00 34.99  ? 83  GLU B OE1 1 
ATOM   1413 O  OE2 . GLU B 1 84 ? 14.277  -3.957  -28.371 1.00 35.59  ? 83  GLU B OE2 1 
ATOM   1414 N  N   . ILE B 1 85 ? 13.664  -6.382  -34.684 1.00 30.58  ? 84  ILE B N   1 
ATOM   1415 C  CA  . ILE B 1 85 ? 14.376  -6.938  -35.826 1.00 30.36  ? 84  ILE B CA  1 
ATOM   1416 C  C   . ILE B 1 85 ? 13.728  -6.438  -37.118 1.00 30.45  ? 84  ILE B C   1 
ATOM   1417 O  O   . ILE B 1 85 ? 14.384  -6.352  -38.175 1.00 29.13  ? 84  ILE B O   1 
ATOM   1418 C  CB  . ILE B 1 85 ? 14.385  -8.483  -35.752 1.00 31.74  ? 84  ILE B CB  1 
ATOM   1419 C  CG1 . ILE B 1 85 ? 15.414  -9.086  -36.721 1.00 32.93  ? 84  ILE B CG1 1 
ATOM   1420 C  CG2 . ILE B 1 85 ? 12.975  -9.051  -35.979 1.00 29.87  ? 84  ILE B CG2 1 
ATOM   1421 C  CD1 . ILE B 1 85 ? 15.720  -10.562 -36.454 1.00 32.05  ? 84  ILE B CD1 1 
ATOM   1422 N  N   . GLN B 1 86 ? 12.427  -6.129  -37.026 1.00 31.15  ? 85  GLN B N   1 
ATOM   1423 C  CA  . GLN B 1 86 ? 11.640  -5.614  -38.138 1.00 36.87  ? 85  GLN B CA  1 
ATOM   1424 C  C   . GLN B 1 86 ? 11.806  -4.101  -38.312 1.00 35.90  ? 85  GLN B C   1 
ATOM   1425 O  O   . GLN B 1 86 ? 11.861  -3.637  -39.437 1.00 37.03  ? 85  GLN B O   1 
ATOM   1426 C  CB  . GLN B 1 86 ? 10.155  -5.961  -37.988 1.00 40.79  ? 85  GLN B CB  1 
ATOM   1427 N  N   . ASN B 1 87 ? 11.922  -3.322  -37.230 1.00 33.51  ? 86  ASN B N   1 
ATOM   1428 C  CA  . ASN B 1 87 ? 11.797  -1.875  -37.383 1.00 33.03  ? 86  ASN B CA  1 
ATOM   1429 C  C   . ASN B 1 87 ? 13.111  -1.139  -37.152 1.00 33.35  ? 86  ASN B C   1 
ATOM   1430 O  O   . ASN B 1 87 ? 13.255  -0.000  -37.615 1.00 33.44  ? 86  ASN B O   1 
ATOM   1431 C  CB  . ASN B 1 87 ? 10.695  -1.286  -36.494 1.00 38.04  ? 86  ASN B CB  1 
ATOM   1432 C  CG  . ASN B 1 87 ? 9.337   -1.782  -36.928 1.00 38.38  ? 86  ASN B CG  1 
ATOM   1433 O  OD1 . ASN B 1 87 ? 8.814   -1.317  -37.942 1.00 43.57  ? 86  ASN B OD1 1 
ATOM   1434 N  ND2 . ASN B 1 87 ? 8.788   -2.768  -36.237 1.00 38.74  ? 86  ASN B ND2 1 
ATOM   1435 N  N   . ASN B 1 88 ? 14.034  -1.728  -36.381 1.00 30.64  ? 87  ASN B N   1 
ATOM   1436 C  CA  . ASN B 1 88 ? 15.298  -1.042  -36.144 1.00 37.40  ? 87  ASN B CA  1 
ATOM   1437 C  C   . ASN B 1 88 ? 16.378  -2.045  -35.748 1.00 33.30  ? 87  ASN B C   1 
ATOM   1438 O  O   . ASN B 1 88 ? 16.924  -1.975  -34.639 1.00 30.94  ? 87  ASN B O   1 
ATOM   1439 C  CB  . ASN B 1 88 ? 15.173  0.129   -35.162 1.00 39.26  ? 87  ASN B CB  1 
ATOM   1440 C  CG  . ASN B 1 88 ? 16.249  1.177   -35.366 1.00 41.49  ? 87  ASN B CG  1 
ATOM   1441 O  OD1 . ASN B 1 88 ? 17.279  0.930   -36.006 1.00 38.37  ? 87  ASN B OD1 1 
ATOM   1442 N  ND2 . ASN B 1 88 ? 16.030  2.376   -34.847 1.00 42.46  ? 87  ASN B ND2 1 
ATOM   1443 N  N   . PRO B 1 89 ? 16.716  -3.006  -36.645 1.00 31.65  ? 88  PRO B N   1 
ATOM   1444 C  CA  . PRO B 1 89 ? 17.615  -4.109  -36.307 1.00 30.57  ? 88  PRO B CA  1 
ATOM   1445 C  C   . PRO B 1 89 ? 19.060  -3.708  -36.044 1.00 31.33  ? 88  PRO B C   1 
ATOM   1446 O  O   . PRO B 1 89 ? 19.803  -4.468  -35.426 1.00 32.53  ? 88  PRO B O   1 
ATOM   1447 C  CB  . PRO B 1 89 ? 17.518  -5.031  -37.539 1.00 29.26  ? 88  PRO B CB  1 
ATOM   1448 C  CG  . PRO B 1 89 ? 17.235  -4.099  -38.687 1.00 30.09  ? 88  PRO B CG  1 
ATOM   1449 C  CD  . PRO B 1 89 ? 16.272  -3.070  -38.051 1.00 32.70  ? 88  PRO B CD  1 
ATOM   1450 N  N   . HIS B 1 90 ? 19.454  -2.506  -36.503 1.00 28.31  ? 89  HIS B N   1 
ATOM   1451 C  CA  . HIS B 1 90 ? 20.851  -2.109  -36.423 1.00 31.19  ? 89  HIS B CA  1 
ATOM   1452 C  C   . HIS B 1 90 ? 21.043  -1.013  -35.372 1.00 36.10  ? 89  HIS B C   1 
ATOM   1453 O  O   . HIS B 1 90 ? 22.122  -0.444  -35.289 1.00 37.90  ? 89  HIS B O   1 
ATOM   1454 C  CB  . HIS B 1 90 ? 21.405  -1.685  -37.799 1.00 29.76  ? 89  HIS B CB  1 
ATOM   1455 C  CG  . HIS B 1 90 ? 21.193  -2.722  -38.860 1.00 29.97  ? 89  HIS B CG  1 
ATOM   1456 N  ND1 . HIS B 1 90 ? 21.729  -3.985  -38.731 1.00 31.99  ? 89  HIS B ND1 1 
ATOM   1457 C  CD2 . HIS B 1 90 ? 20.477  -2.738  -40.010 1.00 31.13  ? 89  HIS B CD2 1 
ATOM   1458 C  CE1 . HIS B 1 90 ? 21.361  -4.728  -39.775 1.00 30.91  ? 89  HIS B CE1 1 
ATOM   1459 N  NE2 . HIS B 1 90 ? 20.649  -3.968  -40.575 1.00 28.85  ? 89  HIS B NE2 1 
ATOM   1460 N  N   . ALA B 1 91 ? 20.032  -0.795  -34.521 1.00 35.50  ? 90  ALA B N   1 
ATOM   1461 C  CA  . ALA B 1 91 ? 20.115  0.241   -33.500 1.00 35.95  ? 90  ALA B CA  1 
ATOM   1462 C  C   . ALA B 1 91 ? 21.088  -0.146  -32.384 1.00 39.79  ? 90  ALA B C   1 
ATOM   1463 O  O   . ALA B 1 91 ? 21.434  -1.318  -32.185 1.00 34.47  ? 90  ALA B O   1 
ATOM   1464 C  CB  . ALA B 1 91 ? 18.728  0.561   -32.961 1.00 35.28  ? 90  ALA B CB  1 
ATOM   1465 N  N   . SER B 1 92 ? 21.526  0.870   -31.633 1.00 36.88  ? 91  SER B N   1 
ATOM   1466 C  CA  . SER B 1 92 ? 22.176  0.670   -30.346 1.00 40.25  ? 91  SER B CA  1 
ATOM   1467 C  C   . SER B 1 92 ? 21.116  0.438   -29.255 1.00 43.37  ? 91  SER B C   1 
ATOM   1468 O  O   . SER B 1 92 ? 20.191  1.243   -29.126 1.00 42.97  ? 91  SER B O   1 
ATOM   1469 C  CB  . SER B 1 92 ? 23.043  1.867   -30.020 1.00 38.96  ? 91  SER B CB  1 
ATOM   1470 O  OG  . SER B 1 92 ? 23.537  1.740   -28.696 1.00 49.80  ? 91  SER B OG  1 
ATOM   1471 N  N   . TYR B 1 93 ? 21.239  -0.681  -28.509 1.00 40.62  ? 92  TYR B N   1 
ATOM   1472 C  CA  . TYR B 1 93 ? 20.319  -1.094  -27.446 1.00 41.90  ? 92  TYR B CA  1 
ATOM   1473 C  C   . TYR B 1 93 ? 21.056  -1.072  -26.100 1.00 47.33  ? 92  TYR B C   1 
ATOM   1474 O  O   . TYR B 1 93 ? 20.475  -1.350  -25.051 1.00 54.59  ? 92  TYR B O   1 
ATOM   1475 C  CB  . TYR B 1 93 ? 19.621  -2.431  -27.749 1.00 32.79  ? 92  TYR B CB  1 
ATOM   1476 C  CG  . TYR B 1 93 ? 18.645  -2.344  -28.909 1.00 31.36  ? 92  TYR B CG  1 
ATOM   1477 C  CD1 . TYR B 1 93 ? 17.361  -1.832  -28.728 1.00 31.67  ? 92  TYR B CD1 1 
ATOM   1478 C  CD2 . TYR B 1 93 ? 19.022  -2.725  -30.194 1.00 29.87  ? 92  TYR B CD2 1 
ATOM   1479 C  CE1 . TYR B 1 93 ? 16.458  -1.733  -29.774 1.00 33.58  ? 92  TYR B CE1 1 
ATOM   1480 C  CE2 . TYR B 1 93 ? 18.123  -2.631  -31.246 1.00 29.15  ? 92  TYR B CE2 1 
ATOM   1481 C  CZ  . TYR B 1 93 ? 16.846  -2.134  -31.039 1.00 31.81  ? 92  TYR B CZ  1 
ATOM   1482 O  OH  . TYR B 1 93 ? 15.964  -2.032  -32.085 1.00 30.15  ? 92  TYR B OH  1 
ATOM   1483 N  N   . SER B 1 94 ? 22.343  -0.717  -26.169 1.00 57.96  ? 93  SER B N   1 
ATOM   1484 C  CA  . SER B 1 94 ? 23.219  -0.277  -25.091 1.00 68.60  ? 93  SER B CA  1 
ATOM   1485 C  C   . SER B 1 94 ? 22.448  0.417   -23.955 1.00 76.51  ? 93  SER B C   1 
ATOM   1486 O  O   . SER B 1 94 ? 21.489  1.176   -24.265 1.00 77.63  ? 93  SER B O   1 
ATOM   1487 C  CB  . SER B 1 94 ? 24.249  0.680   -25.640 1.00 68.87  ? 93  SER B CB  1 
ATOM   1488 O  OG  . SER B 1 94 ? 25.004  0.098   -26.694 1.00 76.89  ? 93  SER B OG  1 
ATOM   1489 O  OXT . SER B 1 94 ? 22.880  0.233   -22.795 1.00 75.82  ? 93  SER B OXT 1 
ATOM   1490 N  N   . ALA C 1 5  ? 29.686  -23.562 29.507  1.00 62.17  ? 4   ALA C N   1 
ATOM   1491 C  CA  . ALA C 1 5  ? 28.760  -22.510 29.985  1.00 69.15  ? 4   ALA C CA  1 
ATOM   1492 C  C   . ALA C 1 5  ? 27.362  -22.724 29.401  1.00 75.99  ? 4   ALA C C   1 
ATOM   1493 O  O   . ALA C 1 5  ? 27.010  -22.108 28.394  1.00 76.36  ? 4   ALA C O   1 
ATOM   1494 C  CB  . ALA C 1 5  ? 29.316  -21.151 29.615  1.00 66.02  ? 4   ALA C CB  1 
ATOM   1495 N  N   . PHE C 1 6  ? 26.559  -23.576 30.056  1.00 69.25  ? 5   PHE C N   1 
ATOM   1496 C  CA  . PHE C 1 6  ? 25.202  -23.839 29.603  1.00 65.37  ? 5   PHE C CA  1 
ATOM   1497 C  C   . PHE C 1 6  ? 24.271  -23.955 30.805  1.00 72.95  ? 5   PHE C C   1 
ATOM   1498 O  O   . PHE C 1 6  ? 24.428  -24.863 31.619  1.00 86.44  ? 5   PHE C O   1 
ATOM   1499 C  CB  . PHE C 1 6  ? 25.125  -25.129 28.774  1.00 52.78  ? 5   PHE C CB  1 
ATOM   1500 C  CG  . PHE C 1 6  ? 25.857  -25.119 27.438  1.00 50.50  ? 5   PHE C CG  1 
ATOM   1501 C  CD1 . PHE C 1 6  ? 27.035  -25.833 27.260  1.00 46.59  ? 5   PHE C CD1 1 
ATOM   1502 C  CD2 . PHE C 1 6  ? 25.384  -24.363 26.369  1.00 51.79  ? 5   PHE C CD2 1 
ATOM   1503 C  CE1 . PHE C 1 6  ? 27.694  -25.831 26.035  1.00 52.55  ? 5   PHE C CE1 1 
ATOM   1504 C  CE2 . PHE C 1 6  ? 26.058  -24.347 25.154  1.00 51.09  ? 5   PHE C CE2 1 
ATOM   1505 C  CZ  . PHE C 1 6  ? 27.201  -25.086 24.981  1.00 51.12  ? 5   PHE C CZ  1 
ATOM   1506 N  N   . LYS C 1 7  ? 23.290  -23.048 30.887  1.00 66.56  ? 6   LYS C N   1 
ATOM   1507 C  CA  . LYS C 1 7  ? 22.304  -23.060 31.959  1.00 65.10  ? 6   LYS C CA  1 
ATOM   1508 C  C   . LYS C 1 7  ? 20.952  -23.481 31.385  1.00 62.36  ? 6   LYS C C   1 
ATOM   1509 O  O   . LYS C 1 7  ? 20.724  -23.350 30.182  1.00 62.63  ? 6   LYS C O   1 
ATOM   1510 C  CB  . LYS C 1 7  ? 22.263  -21.693 32.656  1.00 71.35  ? 6   LYS C CB  1 
ATOM   1511 N  N   . PRO C 1 8  ? 20.001  -23.994 32.202  1.00 62.25  ? 7   PRO C N   1 
ATOM   1512 C  CA  . PRO C 1 8  ? 18.728  -24.489 31.666  1.00 67.37  ? 7   PRO C CA  1 
ATOM   1513 C  C   . PRO C 1 8  ? 18.031  -23.376 30.882  1.00 74.64  ? 7   PRO C C   1 
ATOM   1514 O  O   . PRO C 1 8  ? 17.977  -22.239 31.345  1.00 84.49  ? 7   PRO C O   1 
ATOM   1515 C  CB  . PRO C 1 8  ? 17.941  -24.933 32.916  1.00 65.35  ? 7   PRO C CB  1 
ATOM   1516 C  CG  . PRO C 1 8  ? 19.017  -25.164 33.956  1.00 63.12  ? 7   PRO C CG  1 
ATOM   1517 C  CD  . PRO C 1 8  ? 20.081  -24.111 33.669  1.00 65.15  ? 7   PRO C CD  1 
ATOM   1518 N  N   . GLY C 1 9  ? 17.559  -23.697 29.670  1.00 71.39  ? 8   GLY C N   1 
ATOM   1519 C  CA  . GLY C 1 9  ? 16.846  -22.742 28.836  1.00 64.46  ? 8   GLY C CA  1 
ATOM   1520 C  C   . GLY C 1 9  ? 17.698  -22.175 27.697  1.00 59.12  ? 8   GLY C C   1 
ATOM   1521 O  O   . GLY C 1 9  ? 17.141  -21.624 26.748  1.00 64.35  ? 8   GLY C O   1 
ATOM   1522 N  N   . ASP C 1 10 ? 19.032  -22.298 27.813  1.00 50.40  ? 9   ASP C N   1 
ATOM   1523 C  CA  . ASP C 1 10 ? 19.992  -21.871 26.805  1.00 48.42  ? 9   ASP C CA  1 
ATOM   1524 C  C   . ASP C 1 10 ? 19.757  -22.606 25.485  1.00 50.55  ? 9   ASP C C   1 
ATOM   1525 O  O   . ASP C 1 10 ? 19.615  -23.822 25.469  1.00 50.42  ? 9   ASP C O   1 
ATOM   1526 C  CB  . ASP C 1 10 ? 21.430  -22.141 27.225  1.00 48.57  ? 9   ASP C CB  1 
ATOM   1527 C  CG  . ASP C 1 10 ? 22.098  -21.116 28.135  1.00 62.41  ? 9   ASP C CG  1 
ATOM   1528 O  OD1 . ASP C 1 10 ? 21.425  -20.127 28.511  1.00 70.08  ? 9   ASP C OD1 1 
ATOM   1529 O  OD2 . ASP C 1 10 ? 23.295  -21.317 28.470  1.00 68.12  ? 9   ASP C OD2 1 
ATOM   1530 N  N   . LEU C 1 11 ? 19.786  -21.855 24.377  1.00 48.40  ? 10  LEU C N   1 
ATOM   1531 C  CA  . LEU C 1 11 ? 19.407  -22.361 23.068  1.00 47.33  ? 10  LEU C CA  1 
ATOM   1532 C  C   . LEU C 1 11 ? 20.649  -22.835 22.313  1.00 43.92  ? 10  LEU C C   1 
ATOM   1533 O  O   . LEU C 1 11 ? 21.608  -22.085 22.178  1.00 42.31  ? 10  LEU C O   1 
ATOM   1534 C  CB  . LEU C 1 11 ? 18.666  -21.254 22.315  1.00 46.70  ? 10  LEU C CB  1 
ATOM   1535 C  CG  . LEU C 1 11 ? 17.311  -20.803 22.868  1.00 46.86  ? 10  LEU C CG  1 
ATOM   1536 C  CD1 . LEU C 1 11 ? 16.655  -19.848 21.874  1.00 51.65  ? 10  LEU C CD1 1 
ATOM   1537 C  CD2 . LEU C 1 11 ? 16.355  -21.949 23.190  1.00 46.99  ? 10  LEU C CD2 1 
ATOM   1538 N  N   . VAL C 1 12 ? 20.602  -24.066 21.769  1.00 42.82  ? 11  VAL C N   1 
ATOM   1539 C  CA  . VAL C 1 12 ? 21.765  -24.678 21.140  1.00 39.96  ? 11  VAL C CA  1 
ATOM   1540 C  C   . VAL C 1 12 ? 21.352  -25.430 19.865  1.00 36.70  ? 11  VAL C C   1 
ATOM   1541 O  O   . VAL C 1 12 ? 20.166  -25.600 19.590  1.00 35.84  ? 11  VAL C O   1 
ATOM   1542 C  CB  . VAL C 1 12 ? 22.395  -25.666 22.142  1.00 38.04  ? 11  VAL C CB  1 
ATOM   1543 C  CG1 . VAL C 1 12 ? 22.776  -25.000 23.462  1.00 36.86  ? 11  VAL C CG1 1 
ATOM   1544 C  CG2 . VAL C 1 12 ? 21.470  -26.854 22.399  1.00 36.22  ? 11  VAL C CG2 1 
ATOM   1545 N  N   . PHE C 1 13 ? 22.360  -25.835 19.075  1.00 33.70  ? 12  PHE C N   1 
ATOM   1546 C  CA  . PHE C 1 13 ? 22.279  -27.003 18.213  1.00 31.34  ? 12  PHE C CA  1 
ATOM   1547 C  C   . PHE C 1 13 ? 22.979  -28.152 18.919  1.00 31.42  ? 12  PHE C C   1 
ATOM   1548 O  O   . PHE C 1 13 ? 24.065  -27.996 19.491  1.00 37.62  ? 12  PHE C O   1 
ATOM   1549 C  CB  . PHE C 1 13 ? 22.904  -26.812 16.827  1.00 36.44  ? 12  PHE C CB  1 
ATOM   1550 C  CG  . PHE C 1 13 ? 22.159  -25.792 15.989  1.00 38.63  ? 12  PHE C CG  1 
ATOM   1551 C  CD1 . PHE C 1 13 ? 21.118  -26.191 15.150  1.00 38.03  ? 12  PHE C CD1 1 
ATOM   1552 C  CD2 . PHE C 1 13 ? 22.453  -24.433 16.092  1.00 39.51  ? 12  PHE C CD2 1 
ATOM   1553 C  CE1 . PHE C 1 13 ? 20.405  -25.249 14.424  1.00 39.16  ? 12  PHE C CE1 1 
ATOM   1554 C  CE2 . PHE C 1 13 ? 21.733  -23.498 15.361  1.00 42.34  ? 12  PHE C CE2 1 
ATOM   1555 C  CZ  . PHE C 1 13 ? 20.731  -23.907 14.513  1.00 41.94  ? 12  PHE C CZ  1 
ATOM   1556 N  N   . ALA C 1 14 ? 22.335  -29.315 18.869  1.00 32.76  ? 13  ALA C N   1 
ATOM   1557 C  CA  . ALA C 1 14 ? 22.773  -30.462 19.638  1.00 31.56  ? 13  ALA C CA  1 
ATOM   1558 C  C   . ALA C 1 14 ? 22.995  -31.609 18.665  1.00 34.18  ? 13  ALA C C   1 
ATOM   1559 O  O   . ALA C 1 14 ? 22.131  -31.911 17.843  1.00 31.30  ? 13  ALA C O   1 
ATOM   1560 C  CB  . ALA C 1 14 ? 21.714  -30.826 20.662  1.00 33.93  ? 13  ALA C CB  1 
ATOM   1561 N  N   . LYS C 1 15 ? 24.174  -32.217 18.758  1.00 35.16  ? 14  LYS C N   1 
ATOM   1562 C  CA  . LYS C 1 15 ? 24.591  -33.185 17.766  1.00 38.29  ? 14  LYS C CA  1 
ATOM   1563 C  C   . LYS C 1 15 ? 24.615  -34.545 18.439  1.00 36.09  ? 14  LYS C C   1 
ATOM   1564 O  O   . LYS C 1 15 ? 25.335  -34.722 19.416  1.00 38.08  ? 14  LYS C O   1 
ATOM   1565 C  CB  . LYS C 1 15 ? 26.004  -32.919 17.224  1.00 41.02  ? 14  LYS C CB  1 
ATOM   1566 C  CG  . LYS C 1 15 ? 26.493  -34.001 16.242  1.00 36.90  ? 14  LYS C CG  1 
ATOM   1567 C  CD  . LYS C 1 15 ? 25.654  -33.980 14.962  1.00 35.97  ? 14  LYS C CD  1 
ATOM   1568 C  CE  . LYS C 1 15 ? 26.175  -34.866 13.827  1.00 38.21  ? 14  LYS C CE  1 
ATOM   1569 N  NZ  . LYS C 1 15 ? 25.918  -36.296 14.074  1.00 33.22  ? 14  LYS C NZ  1 
ATOM   1570 N  N   . MET C 1 16 ? 23.802  -35.459 17.908  1.00 33.43  ? 15  MET C N   1 
ATOM   1571 C  CA  . MET C 1 16 ? 23.738  -36.851 18.318  1.00 35.14  ? 15  MET C CA  1 
ATOM   1572 C  C   . MET C 1 16 ? 24.189  -37.708 17.149  1.00 39.33  ? 15  MET C C   1 
ATOM   1573 O  O   . MET C 1 16 ? 24.012  -37.325 15.986  1.00 34.37  ? 15  MET C O   1 
ATOM   1574 C  CB  . MET C 1 16 ? 22.300  -37.267 18.638  1.00 35.37  ? 15  MET C CB  1 
ATOM   1575 C  CG  . MET C 1 16 ? 21.811  -36.757 19.982  1.00 38.84  ? 15  MET C CG  1 
ATOM   1576 S  SD  . MET C 1 16 ? 20.284  -37.560 20.506  1.00 52.18  ? 15  MET C SD  1 
ATOM   1577 C  CE  . MET C 1 16 ? 19.240  -37.148 19.095  1.00 54.64  ? 15  MET C CE  1 
ATOM   1578 N  N   . LYS C 1 17 ? 24.723  -38.894 17.465  1.00 42.47  ? 16  LYS C N   1 
ATOM   1579 C  CA  . LYS C 1 17 ? 25.218  -39.754 16.399  1.00 45.58  ? 16  LYS C CA  1 
ATOM   1580 C  C   . LYS C 1 17 ? 24.031  -40.181 15.538  1.00 36.44  ? 16  LYS C C   1 
ATOM   1581 O  O   . LYS C 1 17 ? 23.057  -40.711 16.058  1.00 35.40  ? 16  LYS C O   1 
ATOM   1582 C  CB  . LYS C 1 17 ? 25.947  -40.968 16.994  1.00 43.82  ? 16  LYS C CB  1 
ATOM   1583 C  CG  . LYS C 1 17 ? 26.646  -41.899 16.006  1.00 48.57  ? 16  LYS C CG  1 
ATOM   1584 C  CD  . LYS C 1 17 ? 27.794  -41.217 15.275  1.00 48.54  ? 16  LYS C CD  1 
ATOM   1585 C  CE  . LYS C 1 17 ? 28.337  -42.053 14.163  1.00 58.27  ? 16  LYS C CE  1 
ATOM   1586 N  NZ  . LYS C 1 17 ? 29.611  -41.503 13.694  1.00 50.99  ? 16  LYS C NZ  1 
ATOM   1587 N  N   . GLY C 1 18 ? 24.140  -39.980 14.218  1.00 35.46  ? 17  GLY C N   1 
ATOM   1588 C  CA  . GLY C 1 18 ? 23.121  -40.470 13.304  1.00 38.79  ? 17  GLY C CA  1 
ATOM   1589 C  C   . GLY C 1 18 ? 22.083  -39.394 12.940  1.00 41.57  ? 17  GLY C C   1 
ATOM   1590 O  O   . GLY C 1 18 ? 21.082  -39.697 12.303  1.00 38.19  ? 17  GLY C O   1 
ATOM   1591 N  N   . TYR C 1 19 ? 22.324  -38.145 13.359  1.00 38.13  ? 18  TYR C N   1 
ATOM   1592 C  CA  . TYR C 1 19 ? 21.373  -37.047 13.192  1.00 35.99  ? 18  TYR C CA  1 
ATOM   1593 C  C   . TYR C 1 19 ? 22.174  -35.793 12.879  1.00 35.41  ? 18  TYR C C   1 
ATOM   1594 O  O   . TYR C 1 19 ? 23.277  -35.619 13.389  1.00 34.60  ? 18  TYR C O   1 
ATOM   1595 C  CB  . TYR C 1 19 ? 20.599  -36.752 14.489  1.00 33.26  ? 18  TYR C CB  1 
ATOM   1596 C  CG  . TYR C 1 19 ? 19.711  -37.914 14.879  1.00 33.78  ? 18  TYR C CG  1 
ATOM   1597 C  CD1 . TYR C 1 19 ? 20.202  -38.988 15.627  1.00 34.41  ? 18  TYR C CD1 1 
ATOM   1598 C  CD2 . TYR C 1 19 ? 18.409  -37.971 14.414  1.00 36.55  ? 18  TYR C CD2 1 
ATOM   1599 C  CE1 . TYR C 1 19 ? 19.398  -40.074 15.924  1.00 38.18  ? 18  TYR C CE1 1 
ATOM   1600 C  CE2 . TYR C 1 19 ? 17.595  -39.045 14.720  1.00 44.41  ? 18  TYR C CE2 1 
ATOM   1601 C  CZ  . TYR C 1 19 ? 18.092  -40.096 15.464  1.00 43.66  ? 18  TYR C CZ  1 
ATOM   1602 O  OH  . TYR C 1 19 ? 17.233  -41.114 15.727  1.00 47.09  ? 18  TYR C OH  1 
ATOM   1603 N  N   . PRO C 1 20 ? 21.645  -34.880 12.042  1.00 38.48  ? 19  PRO C N   1 
ATOM   1604 C  CA  . PRO C 1 20 ? 22.281  -33.569 11.857  1.00 33.64  ? 19  PRO C CA  1 
ATOM   1605 C  C   . PRO C 1 20 ? 22.271  -32.761 13.161  1.00 35.25  ? 19  PRO C C   1 
ATOM   1606 O  O   . PRO C 1 20 ? 21.499  -33.058 14.074  1.00 33.56  ? 19  PRO C O   1 
ATOM   1607 C  CB  . PRO C 1 20 ? 21.375  -32.934 10.796  1.00 36.20  ? 19  PRO C CB  1 
ATOM   1608 C  CG  . PRO C 1 20 ? 20.035  -33.573 11.017  1.00 36.28  ? 19  PRO C CG  1 
ATOM   1609 C  CD  . PRO C 1 20 ? 20.358  -35.029 11.331  1.00 37.70  ? 19  PRO C CD  1 
ATOM   1610 N  N   . HIS C 1 21 ? 23.120  -31.726 13.233  1.00 38.02  ? 20  HIS C N   1 
ATOM   1611 C  CA  . HIS C 1 21 ? 23.056  -30.757 14.320  1.00 36.11  ? 20  HIS C CA  1 
ATOM   1612 C  C   . HIS C 1 21 ? 21.624  -30.231 14.429  1.00 34.23  ? 20  HIS C C   1 
ATOM   1613 O  O   . HIS C 1 21 ? 21.058  -29.740 13.445  1.00 34.91  ? 20  HIS C O   1 
ATOM   1614 C  CB  . HIS C 1 21 ? 24.049  -29.615 14.098  1.00 37.36  ? 20  HIS C CB  1 
ATOM   1615 C  CG  . HIS C 1 21 ? 25.465  -30.065 14.166  1.00 37.71  ? 20  HIS C CG  1 
ATOM   1616 N  ND1 . HIS C 1 21 ? 26.086  -30.710 13.117  1.00 38.15  ? 20  HIS C ND1 1 
ATOM   1617 C  CD2 . HIS C 1 21 ? 26.363  -30.011 15.169  1.00 43.75  ? 20  HIS C CD2 1 
ATOM   1618 C  CE1 . HIS C 1 21 ? 27.327  -31.017 13.475  1.00 43.35  ? 20  HIS C CE1 1 
ATOM   1619 N  NE2 . HIS C 1 21 ? 27.525  -30.587 14.713  1.00 41.64  ? 20  HIS C NE2 1 
ATOM   1620 N  N   . TRP C 1 22 ? 21.043  -30.349 15.632  1.00 30.92  ? 21  TRP C N   1 
ATOM   1621 C  CA  . TRP C 1 22 ? 19.592  -30.267 15.776  1.00 30.27  ? 21  TRP C CA  1 
ATOM   1622 C  C   . TRP C 1 22 ? 19.237  -29.095 16.694  1.00 29.43  ? 21  TRP C C   1 
ATOM   1623 O  O   . TRP C 1 22 ? 19.812  -28.974 17.783  1.00 31.75  ? 21  TRP C O   1 
ATOM   1624 C  CB  . TRP C 1 22 ? 19.034  -31.577 16.366  1.00 33.00  ? 21  TRP C CB  1 
ATOM   1625 C  CG  . TRP C 1 22 ? 17.576  -31.807 16.030  1.00 35.40  ? 21  TRP C CG  1 
ATOM   1626 C  CD1 . TRP C 1 22 ? 16.478  -31.225 16.604  1.00 32.01  ? 21  TRP C CD1 1 
ATOM   1627 C  CD2 . TRP C 1 22 ? 17.065  -32.689 14.996  1.00 34.31  ? 21  TRP C CD2 1 
ATOM   1628 N  NE1 . TRP C 1 22 ? 15.328  -31.668 15.995  1.00 32.82  ? 21  TRP C NE1 1 
ATOM   1629 C  CE2 . TRP C 1 22 ? 15.656  -32.571 15.014  1.00 33.81  ? 21  TRP C CE2 1 
ATOM   1630 C  CE3 . TRP C 1 22 ? 17.655  -33.556 14.063  1.00 33.47  ? 21  TRP C CE3 1 
ATOM   1631 C  CZ2 . TRP C 1 22 ? 14.848  -33.292 14.129  1.00 33.25  ? 21  TRP C CZ2 1 
ATOM   1632 C  CZ3 . TRP C 1 22 ? 16.852  -34.274 13.193  1.00 33.07  ? 21  TRP C CZ3 1 
ATOM   1633 C  CH2 . TRP C 1 22 ? 15.467  -34.156 13.254  1.00 30.67  ? 21  TRP C CH2 1 
ATOM   1634 N  N   . PRO C 1 23 ? 18.259  -28.223 16.340  1.00 32.13  ? 22  PRO C N   1 
ATOM   1635 C  CA  . PRO C 1 23 ? 17.879  -27.132 17.235  1.00 32.33  ? 22  PRO C CA  1 
ATOM   1636 C  C   . PRO C 1 23 ? 17.252  -27.666 18.524  1.00 30.74  ? 22  PRO C C   1 
ATOM   1637 O  O   . PRO C 1 23 ? 16.380  -28.530 18.498  1.00 32.90  ? 22  PRO C O   1 
ATOM   1638 C  CB  . PRO C 1 23 ? 16.915  -26.316 16.354  1.00 36.50  ? 22  PRO C CB  1 
ATOM   1639 C  CG  . PRO C 1 23 ? 16.257  -27.383 15.504  1.00 31.63  ? 22  PRO C CG  1 
ATOM   1640 C  CD  . PRO C 1 23 ? 17.480  -28.200 15.081  1.00 31.06  ? 22  PRO C CD  1 
ATOM   1641 N  N   . ALA C 1 24 ? 17.710  -27.124 19.653  1.00 34.52  ? 23  ALA C N   1 
ATOM   1642 C  CA  . ALA C 1 24 ? 17.409  -27.698 20.955  1.00 33.05  ? 23  ALA C CA  1 
ATOM   1643 C  C   . ALA C 1 24 ? 17.617  -26.644 22.042  1.00 36.67  ? 23  ALA C C   1 
ATOM   1644 O  O   . ALA C 1 24 ? 18.141  -25.563 21.773  1.00 37.24  ? 23  ALA C O   1 
ATOM   1645 C  CB  . ALA C 1 24 ? 18.325  -28.899 21.188  1.00 31.36  ? 23  ALA C CB  1 
ATOM   1646 N  N   . ARG C 1 25 ? 17.242  -26.985 23.287  1.00 37.93  ? 24  ARG C N   1 
ATOM   1647 C  CA  . ARG C 1 25 ? 17.624  -26.167 24.432  1.00 39.32  ? 24  ARG C CA  1 
ATOM   1648 C  C   . ARG C 1 25 ? 18.048  -27.044 25.613  1.00 39.28  ? 24  ARG C C   1 
ATOM   1649 O  O   . ARG C 1 25 ? 17.657  -28.213 25.696  1.00 35.86  ? 24  ARG C O   1 
ATOM   1650 C  CB  . ARG C 1 25 ? 16.439  -25.327 24.917  1.00 39.77  ? 24  ARG C CB  1 
ATOM   1651 C  CG  . ARG C 1 25 ? 15.169  -26.046 25.344  1.00 43.78  ? 24  ARG C CG  1 
ATOM   1652 C  CD  . ARG C 1 25 ? 14.170  -25.040 25.939  1.00 43.19  ? 24  ARG C CD  1 
ATOM   1653 N  NE  . ARG C 1 25 ? 12.999  -25.801 26.390  1.00 50.32  ? 24  ARG C NE  1 
ATOM   1654 C  CZ  . ARG C 1 25 ? 11.714  -25.642 26.079  1.00 55.45  ? 24  ARG C CZ  1 
ATOM   1655 N  NH1 . ARG C 1 25 ? 11.315  -24.668 25.279  1.00 52.90  ? 24  ARG C NH1 1 
ATOM   1656 N  NH2 . ARG C 1 25 ? 10.819  -26.474 26.589  1.00 57.24  ? 24  ARG C NH2 1 
ATOM   1657 N  N   . ILE C 1 26 ? 18.821  -26.447 26.527  1.00 40.55  ? 25  ILE C N   1 
ATOM   1658 C  CA  . ILE C 1 26 ? 19.203  -27.064 27.797  1.00 48.35  ? 25  ILE C CA  1 
ATOM   1659 C  C   . ILE C 1 26 ? 17.973  -27.127 28.701  1.00 53.15  ? 25  ILE C C   1 
ATOM   1660 O  O   . ILE C 1 26 ? 17.356  -26.106 29.002  1.00 57.38  ? 25  ILE C O   1 
ATOM   1661 C  CB  . ILE C 1 26 ? 20.331  -26.292 28.515  1.00 47.93  ? 25  ILE C CB  1 
ATOM   1662 C  CG1 . ILE C 1 26 ? 21.439  -25.792 27.601  1.00 46.87  ? 25  ILE C CG1 1 
ATOM   1663 C  CG2 . ILE C 1 26 ? 20.882  -27.067 29.716  1.00 45.19  ? 25  ILE C CG2 1 
ATOM   1664 C  CD1 . ILE C 1 26 ? 22.382  -26.850 27.070  1.00 44.12  ? 25  ILE C CD1 1 
ATOM   1665 N  N   . ASP C 1 27 ? 17.639  -28.337 29.145  1.00 55.05  ? 26  ASP C N   1 
ATOM   1666 C  CA  . ASP C 1 27 ? 16.558  -28.546 30.092  1.00 65.03  ? 26  ASP C CA  1 
ATOM   1667 C  C   . ASP C 1 27 ? 17.035  -28.311 31.523  1.00 71.38  ? 26  ASP C C   1 
ATOM   1668 O  O   . ASP C 1 27 ? 18.236  -28.267 31.783  1.00 70.17  ? 26  ASP C O   1 
ATOM   1669 C  CB  . ASP C 1 27 ? 15.944  -29.927 29.937  1.00 65.34  ? 26  ASP C CB  1 
ATOM   1670 C  CG  . ASP C 1 27 ? 14.543  -29.924 29.350  1.00 69.24  ? 26  ASP C CG  1 
ATOM   1671 O  OD1 . ASP C 1 27 ? 14.189  -28.890 28.747  1.00 63.64  ? 26  ASP C OD1 1 
ATOM   1672 O  OD2 . ASP C 1 27 ? 13.805  -30.923 29.563  1.00 65.80  ? 26  ASP C OD2 1 
ATOM   1673 N  N   . ASP C 1 28 ? 16.060  -28.155 32.432  1.00 78.60  ? 27  ASP C N   1 
ATOM   1674 C  CA  . ASP C 1 28 ? 16.279  -28.146 33.871  1.00 79.43  ? 27  ASP C CA  1 
ATOM   1675 C  C   . ASP C 1 28 ? 16.200  -29.582 34.373  1.00 79.34  ? 27  ASP C C   1 
ATOM   1676 O  O   . ASP C 1 28 ? 15.294  -30.311 33.984  1.00 80.65  ? 27  ASP C O   1 
ATOM   1677 C  CB  . ASP C 1 28 ? 15.221  -27.320 34.584  1.00 81.64  ? 27  ASP C CB  1 
ATOM   1678 N  N   . ILE C 1 29 ? 17.145  -29.971 35.239  1.00 83.62  ? 28  ILE C N   1 
ATOM   1679 C  CA  . ILE C 1 29 ? 17.188  -31.321 35.780  1.00 84.10  ? 28  ILE C CA  1 
ATOM   1680 C  C   . ILE C 1 29 ? 16.548  -31.304 37.166  1.00 87.76  ? 28  ILE C C   1 
ATOM   1681 O  O   . ILE C 1 29 ? 17.143  -30.784 38.108  1.00 94.75  ? 28  ILE C O   1 
ATOM   1682 C  CB  . ILE C 1 29 ? 18.630  -31.865 35.807  1.00 84.52  ? 28  ILE C CB  1 
ATOM   1683 N  N   . ALA C 1 30 ? 15.340  -31.885 37.266  1.00 83.31  ? 29  ALA C N   1 
ATOM   1684 C  CA  . ALA C 1 30 ? 14.498  -31.833 38.456  1.00 82.21  ? 29  ALA C CA  1 
ATOM   1685 C  C   . ALA C 1 30 ? 15.167  -32.530 39.649  1.00 79.65  ? 29  ALA C C   1 
ATOM   1686 O  O   . ALA C 1 30 ? 15.621  -33.690 39.494  1.00 68.45  ? 29  ALA C O   1 
ATOM   1687 C  CB  . ALA C 1 30 ? 13.128  -32.416 38.156  1.00 77.95  ? 29  ALA C CB  1 
ATOM   1688 N  N   . PRO C 1 36 ? 21.469  -37.533 35.635  1.00 49.78  ? 35  PRO C N   1 
ATOM   1689 C  CA  . PRO C 1 36 ? 22.286  -37.390 34.433  1.00 58.04  ? 35  PRO C CA  1 
ATOM   1690 C  C   . PRO C 1 36 ? 23.633  -38.098 34.598  1.00 65.30  ? 35  PRO C C   1 
ATOM   1691 O  O   . PRO C 1 36 ? 24.239  -38.053 35.671  1.00 60.37  ? 35  PRO C O   1 
ATOM   1692 C  CB  . PRO C 1 36 ? 22.448  -35.872 34.205  1.00 54.05  ? 35  PRO C CB  1 
ATOM   1693 C  CG  . PRO C 1 36 ? 22.110  -35.245 35.544  1.00 57.47  ? 35  PRO C CG  1 
ATOM   1694 C  CD  . PRO C 1 36 ? 21.349  -36.282 36.368  1.00 57.63  ? 35  PRO C CD  1 
ATOM   1695 N  N   . PRO C 1 37 ? 24.164  -38.777 33.555  1.00 59.79  ? 36  PRO C N   1 
ATOM   1696 C  CA  . PRO C 1 37 ? 25.521  -39.322 33.640  1.00 57.90  ? 36  PRO C CA  1 
ATOM   1697 C  C   . PRO C 1 37 ? 26.496  -38.163 33.858  1.00 54.89  ? 36  PRO C C   1 
ATOM   1698 O  O   . PRO C 1 37 ? 26.172  -37.022 33.528  1.00 49.25  ? 36  PRO C O   1 
ATOM   1699 C  CB  . PRO C 1 37 ? 25.680  -40.021 32.272  1.00 54.99  ? 36  PRO C CB  1 
ATOM   1700 C  CG  . PRO C 1 37 ? 24.250  -40.348 31.887  1.00 53.67  ? 36  PRO C CG  1 
ATOM   1701 C  CD  . PRO C 1 37 ? 23.500  -39.081 32.278  1.00 54.40  ? 36  PRO C CD  1 
ATOM   1702 N  N   . PRO C 1 38 ? 27.692  -38.402 34.452  1.00 51.45  ? 37  PRO C N   1 
ATOM   1703 C  CA  . PRO C 1 38 ? 28.650  -37.331 34.723  1.00 51.93  ? 37  PRO C CA  1 
ATOM   1704 C  C   . PRO C 1 38 ? 28.928  -36.476 33.495  1.00 46.80  ? 37  PRO C C   1 
ATOM   1705 O  O   . PRO C 1 38 ? 29.159  -37.013 32.413  1.00 42.20  ? 37  PRO C O   1 
ATOM   1706 C  CB  . PRO C 1 38 ? 29.931  -38.087 35.164  1.00 55.73  ? 37  PRO C CB  1 
ATOM   1707 C  CG  . PRO C 1 38 ? 29.425  -39.416 35.673  1.00 51.67  ? 37  PRO C CG  1 
ATOM   1708 C  CD  . PRO C 1 38 ? 28.182  -39.724 34.878  1.00 50.38  ? 37  PRO C CD  1 
ATOM   1709 N  N   . ASN C 1 39 ? 28.888  -35.154 33.709  1.00 43.94  ? 38  ASN C N   1 
ATOM   1710 C  CA  . ASN C 1 39 ? 29.197  -34.112 32.749  1.00 46.92  ? 38  ASN C CA  1 
ATOM   1711 C  C   . ASN C 1 39 ? 28.262  -34.155 31.538  1.00 47.16  ? 38  ASN C C   1 
ATOM   1712 O  O   . ASN C 1 39 ? 28.697  -33.786 30.446  1.00 49.44  ? 38  ASN C O   1 
ATOM   1713 C  CB  . ASN C 1 39 ? 30.653  -34.146 32.300  1.00 55.84  ? 38  ASN C CB  1 
ATOM   1714 C  CG  . ASN C 1 39 ? 31.093  -32.811 31.742  1.00 68.78  ? 38  ASN C CG  1 
ATOM   1715 O  OD1 . ASN C 1 39 ? 30.424  -31.791 31.954  1.00 79.32  ? 38  ASN C OD1 1 
ATOM   1716 N  ND2 . ASN C 1 39 ? 32.218  -32.789 31.043  1.00 74.02  ? 38  ASN C ND2 1 
ATOM   1717 N  N   . LYS C 1 40 ? 27.006  -34.596 31.728  1.00 42.28  ? 39  LYS C N   1 
ATOM   1718 C  CA  . LYS C 1 40 ? 26.041  -34.594 30.633  1.00 44.02  ? 39  LYS C CA  1 
ATOM   1719 C  C   . LYS C 1 40 ? 24.906  -33.633 30.946  1.00 44.32  ? 39  LYS C C   1 
ATOM   1720 O  O   . LYS C 1 40 ? 24.436  -33.575 32.081  1.00 46.42  ? 39  LYS C O   1 
ATOM   1721 C  CB  . LYS C 1 40 ? 25.373  -35.945 30.347  1.00 43.01  ? 39  LYS C CB  1 
ATOM   1722 C  CG  . LYS C 1 40 ? 26.310  -37.078 30.014  1.00 45.95  ? 39  LYS C CG  1 
ATOM   1723 C  CD  . LYS C 1 40 ? 27.021  -36.934 28.679  1.00 50.27  ? 39  LYS C CD  1 
ATOM   1724 C  CE  . LYS C 1 40 ? 27.764  -38.192 28.368  1.00 55.26  ? 39  LYS C CE  1 
ATOM   1725 N  NZ  . LYS C 1 40 ? 28.738  -37.935 27.302  1.00 63.76  ? 39  LYS C NZ  1 
ATOM   1726 N  N   . TYR C 1 41 ? 24.454  -32.908 29.917  1.00 39.99  ? 40  TYR C N   1 
ATOM   1727 C  CA  . TYR C 1 41 ? 23.369  -31.950 30.073  1.00 39.57  ? 40  TYR C CA  1 
ATOM   1728 C  C   . TYR C 1 41 ? 22.080  -32.581 29.552  1.00 44.60  ? 40  TYR C C   1 
ATOM   1729 O  O   . TYR C 1 41 ? 22.094  -33.340 28.570  1.00 40.79  ? 40  TYR C O   1 
ATOM   1730 C  CB  . TYR C 1 41 ? 23.585  -30.660 29.266  1.00 40.59  ? 40  TYR C CB  1 
ATOM   1731 C  CG  . TYR C 1 41 ? 24.774  -29.793 29.655  1.00 44.73  ? 40  TYR C CG  1 
ATOM   1732 C  CD1 . TYR C 1 41 ? 26.060  -30.088 29.201  1.00 48.37  ? 40  TYR C CD1 1 
ATOM   1733 C  CD2 . TYR C 1 41 ? 24.610  -28.657 30.448  1.00 44.45  ? 40  TYR C CD2 1 
ATOM   1734 C  CE1 . TYR C 1 41 ? 27.149  -29.310 29.560  1.00 52.92  ? 40  TYR C CE1 1 
ATOM   1735 C  CE2 . TYR C 1 41 ? 25.690  -27.857 30.784  1.00 48.99  ? 40  TYR C CE2 1 
ATOM   1736 C  CZ  . TYR C 1 41 ? 26.962  -28.185 30.348  1.00 54.41  ? 40  TYR C CZ  1 
ATOM   1737 O  OH  . TYR C 1 41 ? 28.037  -27.407 30.676  1.00 65.36  ? 40  TYR C OH  1 
ATOM   1738 N  N   . PRO C 1 42 ? 20.927  -32.291 30.203  1.00 45.70  ? 41  PRO C N   1 
ATOM   1739 C  CA  . PRO C 1 42 ? 19.625  -32.734 29.703  1.00 35.64  ? 41  PRO C CA  1 
ATOM   1740 C  C   . PRO C 1 42 ? 19.214  -31.801 28.572  1.00 36.39  ? 41  PRO C C   1 
ATOM   1741 O  O   . PRO C 1 42 ? 19.217  -30.582 28.741  1.00 40.07  ? 41  PRO C O   1 
ATOM   1742 C  CB  . PRO C 1 42 ? 18.725  -32.607 30.948  1.00 40.09  ? 41  PRO C CB  1 
ATOM   1743 C  CG  . PRO C 1 42 ? 19.319  -31.431 31.684  1.00 46.15  ? 41  PRO C CG  1 
ATOM   1744 C  CD  . PRO C 1 42 ? 20.829  -31.501 31.447  1.00 46.50  ? 41  PRO C CD  1 
ATOM   1745 N  N   . ILE C 1 43 ? 18.960  -32.387 27.394  1.00 37.92  ? 42  ILE C N   1 
ATOM   1746 C  CA  . ILE C 1 43 ? 18.646  -31.623 26.192  1.00 37.59  ? 42  ILE C CA  1 
ATOM   1747 C  C   . ILE C 1 43 ? 17.208  -31.911 25.779  1.00 40.53  ? 42  ILE C C   1 
ATOM   1748 O  O   . ILE C 1 43 ? 16.786  -33.067 25.756  1.00 43.45  ? 42  ILE C O   1 
ATOM   1749 C  CB  . ILE C 1 43 ? 19.628  -31.969 25.053  1.00 35.51  ? 42  ILE C CB  1 
ATOM   1750 C  CG1 . ILE C 1 43 ? 21.102  -31.677 25.472  1.00 34.76  ? 42  ILE C CG1 1 
ATOM   1751 C  CG2 . ILE C 1 43 ? 19.228  -31.304 23.721  1.00 28.11  ? 42  ILE C CG2 1 
ATOM   1752 C  CD1 . ILE C 1 43 ? 21.361  -30.252 25.909  1.00 36.98  ? 42  ILE C CD1 1 
ATOM   1753 N  N   . PHE C 1 44 ? 16.483  -30.844 25.404  1.00 43.30  ? 43  PHE C N   1 
ATOM   1754 C  CA  . PHE C 1 44 ? 15.200  -30.983 24.729  1.00 36.94  ? 43  PHE C CA  1 
ATOM   1755 C  C   . PHE C 1 44 ? 15.373  -30.582 23.260  1.00 36.79  ? 43  PHE C C   1 
ATOM   1756 O  O   . PHE C 1 44 ? 15.857  -29.486 22.972  1.00 36.78  ? 43  PHE C O   1 
ATOM   1757 C  CB  . PHE C 1 44 ? 14.266  -29.991 25.425  1.00 39.69  ? 43  PHE C CB  1 
ATOM   1758 C  CG  . PHE C 1 44 ? 12.882  -29.886 24.800  1.00 42.65  ? 43  PHE C CG  1 
ATOM   1759 C  CD1 . PHE C 1 44 ? 11.900  -30.837 25.082  1.00 42.39  ? 43  PHE C CD1 1 
ATOM   1760 C  CD2 . PHE C 1 44 ? 12.559  -28.833 23.942  1.00 42.59  ? 43  PHE C CD2 1 
ATOM   1761 C  CE1 . PHE C 1 44 ? 10.629  -30.743 24.523  1.00 45.71  ? 43  PHE C CE1 1 
ATOM   1762 C  CE2 . PHE C 1 44 ? 11.290  -28.753 23.366  1.00 42.15  ? 43  PHE C CE2 1 
ATOM   1763 C  CZ  . PHE C 1 44 ? 10.328  -29.699 23.666  1.00 46.68  ? 43  PHE C CZ  1 
ATOM   1764 N  N   . PHE C 1 45 ? 14.942  -31.457 22.348  1.00 34.15  ? 44  PHE C N   1 
ATOM   1765 C  CA  . PHE C 1 45 ? 15.061  -31.245 20.912  1.00 36.99  ? 44  PHE C CA  1 
ATOM   1766 C  C   . PHE C 1 45 ? 13.792  -30.582 20.381  1.00 39.92  ? 44  PHE C C   1 
ATOM   1767 O  O   . PHE C 1 45 ? 12.683  -31.077 20.604  1.00 39.36  ? 44  PHE C O   1 
ATOM   1768 C  CB  . PHE C 1 45 ? 15.342  -32.570 20.203  1.00 35.76  ? 44  PHE C CB  1 
ATOM   1769 C  CG  . PHE C 1 45 ? 16.736  -33.110 20.496  1.00 36.85  ? 44  PHE C CG  1 
ATOM   1770 C  CD1 . PHE C 1 45 ? 17.806  -32.818 19.657  1.00 34.34  ? 44  PHE C CD1 1 
ATOM   1771 C  CD2 . PHE C 1 45 ? 16.975  -33.883 21.632  1.00 37.08  ? 44  PHE C CD2 1 
ATOM   1772 C  CE1 . PHE C 1 45 ? 19.083  -33.317 19.933  1.00 35.41  ? 44  PHE C CE1 1 
ATOM   1773 C  CE2 . PHE C 1 45 ? 18.255  -34.357 21.919  1.00 40.39  ? 44  PHE C CE2 1 
ATOM   1774 C  CZ  . PHE C 1 45 ? 19.309  -34.067 21.073  1.00 37.88  ? 44  PHE C CZ  1 
ATOM   1775 N  N   . PHE C 1 46 ? 13.967  -29.449 19.685  1.00 39.07  ? 45  PHE C N   1 
ATOM   1776 C  CA  . PHE C 1 46 ? 12.825  -28.781 19.068  1.00 36.61  ? 45  PHE C CA  1 
ATOM   1777 C  C   . PHE C 1 46 ? 12.281  -29.664 17.946  1.00 36.07  ? 45  PHE C C   1 
ATOM   1778 O  O   . PHE C 1 46 ? 13.007  -30.511 17.408  1.00 36.67  ? 45  PHE C O   1 
ATOM   1779 C  CB  . PHE C 1 46 ? 13.092  -27.322 18.656  1.00 33.96  ? 45  PHE C CB  1 
ATOM   1780 C  CG  . PHE C 1 46 ? 13.375  -26.357 19.799  1.00 36.47  ? 45  PHE C CG  1 
ATOM   1781 C  CD1 . PHE C 1 46 ? 12.358  -25.969 20.668  1.00 36.18  ? 45  PHE C CD1 1 
ATOM   1782 C  CD2 . PHE C 1 46 ? 14.651  -25.827 19.996  1.00 35.29  ? 45  PHE C CD2 1 
ATOM   1783 C  CE1 . PHE C 1 46 ? 12.636  -25.106 21.721  1.00 36.21  ? 45  PHE C CE1 1 
ATOM   1784 C  CE2 . PHE C 1 46 ? 14.920  -24.947 21.038  1.00 35.56  ? 45  PHE C CE2 1 
ATOM   1785 C  CZ  . PHE C 1 46 ? 13.908  -24.578 21.895  1.00 34.90  ? 45  PHE C CZ  1 
ATOM   1786 N  N   . GLY C 1 47 ? 10.983  -29.486 17.637  1.00 34.16  ? 46  GLY C N   1 
ATOM   1787 C  CA  . GLY C 1 47 ? 10.357  -30.194 16.531  1.00 40.32  ? 46  GLY C CA  1 
ATOM   1788 C  C   . GLY C 1 47 ? 9.915   -31.602 16.929  1.00 49.81  ? 46  GLY C C   1 
ATOM   1789 O  O   . GLY C 1 47 ? 8.730   -31.934 16.829  1.00 47.38  ? 46  GLY C O   1 
ATOM   1790 N  N   . THR C 1 48 ? 10.869  -32.430 17.376  1.00 48.06  ? 47  THR C N   1 
ATOM   1791 C  CA  . THR C 1 48 ? 10.513  -33.780 17.798  1.00 44.81  ? 47  THR C CA  1 
ATOM   1792 C  C   . THR C 1 48 ? 10.081  -33.747 19.261  1.00 44.29  ? 47  THR C C   1 
ATOM   1793 O  O   . THR C 1 48 ? 9.363   -34.643 19.702  1.00 52.24  ? 47  THR C O   1 
ATOM   1794 C  CB  . THR C 1 48 ? 11.654  -34.777 17.608  1.00 39.69  ? 47  THR C CB  1 
ATOM   1795 O  OG1 . THR C 1 48 ? 12.573  -34.360 18.615  1.00 40.11  ? 47  THR C OG1 1 
ATOM   1796 C  CG2 . THR C 1 48 ? 12.246  -34.781 16.209  1.00 38.60  ? 47  THR C CG2 1 
ATOM   1797 N  N   . HIS C 1 49 ? 10.529  -32.726 20.002  1.00 39.88  ? 48  HIS C N   1 
ATOM   1798 C  CA  . HIS C 1 49 ? 10.258  -32.592 21.434  1.00 45.61  ? 48  HIS C CA  1 
ATOM   1799 C  C   . HIS C 1 49 ? 10.731  -33.823 22.214  1.00 46.45  ? 48  HIS C C   1 
ATOM   1800 O  O   . HIS C 1 49 ? 10.111  -34.208 23.205  1.00 44.74  ? 48  HIS C O   1 
ATOM   1801 C  CB  . HIS C 1 49 ? 8.775   -32.297 21.705  1.00 49.95  ? 48  HIS C CB  1 
ATOM   1802 C  CG  . HIS C 1 49 ? 8.192   -31.362 20.702  1.00 52.43  ? 48  HIS C CG  1 
ATOM   1803 N  ND1 . HIS C 1 49 ? 7.258   -31.763 19.772  1.00 57.29  ? 48  HIS C ND1 1 
ATOM   1804 C  CD2 . HIS C 1 49 ? 8.442   -30.070 20.458  1.00 47.80  ? 48  HIS C CD2 1 
ATOM   1805 C  CE1 . HIS C 1 49 ? 6.948   -30.729 18.998  1.00 59.66  ? 48  HIS C CE1 1 
ATOM   1806 N  NE2 . HIS C 1 49 ? 7.651   -29.691 19.401  1.00 55.97  ? 48  HIS C NE2 1 
ATOM   1807 N  N   . GLU C 1 50 ? 11.841  -34.431 21.781  1.00 42.40  ? 49  GLU C N   1 
ATOM   1808 C  CA  . GLU C 1 50 ? 12.395  -35.537 22.547  1.00 46.88  ? 49  GLU C CA  1 
ATOM   1809 C  C   . GLU C 1 50 ? 13.463  -35.011 23.502  1.00 43.44  ? 49  GLU C C   1 
ATOM   1810 O  O   . GLU C 1 50 ? 13.823  -33.831 23.454  1.00 40.18  ? 49  GLU C O   1 
ATOM   1811 C  CB  . GLU C 1 50 ? 12.784  -36.677 21.616  1.00 46.92  ? 49  GLU C CB  1 
ATOM   1812 C  CG  . GLU C 1 50 ? 11.550  -37.286 20.954  1.00 57.61  ? 49  GLU C CG  1 
ATOM   1813 C  CD  . GLU C 1 50 ? 11.773  -38.253 19.808  1.00 62.88  ? 49  GLU C CD  1 
ATOM   1814 O  OE1 . GLU C 1 50 ? 12.933  -38.533 19.421  1.00 69.47  ? 49  GLU C OE1 1 
ATOM   1815 O  OE2 . GLU C 1 50 ? 10.739  -38.715 19.285  1.00 71.51  ? 49  GLU C OE2 1 
ATOM   1816 N  N   . THR C 1 51 ? 13.911  -35.877 24.415  1.00 42.71  ? 50  THR C N   1 
ATOM   1817 C  CA  . THR C 1 51 ? 14.945  -35.504 25.372  1.00 47.34  ? 50  THR C CA  1 
ATOM   1818 C  C   . THR C 1 51 ? 16.112  -36.492 25.296  1.00 43.89  ? 50  THR C C   1 
ATOM   1819 O  O   . THR C 1 51 ? 15.956  -37.616 24.830  1.00 43.27  ? 50  THR C O   1 
ATOM   1820 C  CB  . THR C 1 51 ? 14.376  -35.358 26.788  1.00 50.42  ? 50  THR C CB  1 
ATOM   1821 O  OG1 . THR C 1 51 ? 13.702  -36.588 27.038  1.00 51.06  ? 50  THR C OG1 1 
ATOM   1822 C  CG2 . THR C 1 51 ? 13.464  -34.150 26.956  1.00 41.98  ? 50  THR C CG2 1 
ATOM   1823 N  N   . ALA C 1 52 ? 17.297  -36.034 25.705  1.00 42.16  ? 51  ALA C N   1 
ATOM   1824 C  CA  . ALA C 1 52 ? 18.460  -36.897 25.837  1.00 40.75  ? 51  ALA C CA  1 
ATOM   1825 C  C   . ALA C 1 52 ? 19.501  -36.194 26.688  1.00 41.93  ? 51  ALA C C   1 
ATOM   1826 O  O   . ALA C 1 52 ? 19.393  -34.995 26.946  1.00 46.30  ? 51  ALA C O   1 
ATOM   1827 C  CB  . ALA C 1 52 ? 19.045  -37.228 24.477  1.00 41.17  ? 51  ALA C CB  1 
ATOM   1828 N  N   . PHE C 1 53 ? 20.516  -36.960 27.099  1.00 43.86  ? 52  PHE C N   1 
ATOM   1829 C  CA  . PHE C 1 53 ? 21.684  -36.406 27.760  1.00 42.53  ? 52  PHE C CA  1 
ATOM   1830 C  C   . PHE C 1 53 ? 22.794  -36.293 26.729  1.00 39.40  ? 52  PHE C C   1 
ATOM   1831 O  O   . PHE C 1 53 ? 23.086  -37.260 26.027  1.00 41.44  ? 52  PHE C O   1 
ATOM   1832 C  CB  . PHE C 1 53 ? 22.079  -37.397 28.856  1.00 40.87  ? 52  PHE C CB  1 
ATOM   1833 C  CG  . PHE C 1 53 ? 21.113  -37.358 30.025  1.00 45.14  ? 52  PHE C CG  1 
ATOM   1834 C  CD1 . PHE C 1 53 ? 20.844  -36.161 30.686  1.00 50.18  ? 52  PHE C CD1 1 
ATOM   1835 C  CD2 . PHE C 1 53 ? 20.434  -38.507 30.427  1.00 53.06  ? 52  PHE C CD2 1 
ATOM   1836 C  CE1 . PHE C 1 53 ? 19.952  -36.120 31.755  1.00 50.58  ? 52  PHE C CE1 1 
ATOM   1837 C  CE2 . PHE C 1 53 ? 19.544  -38.462 31.496  1.00 54.12  ? 52  PHE C CE2 1 
ATOM   1838 C  CZ  . PHE C 1 53 ? 19.297  -37.269 32.149  1.00 48.33  ? 52  PHE C CZ  1 
ATOM   1839 N  N   . LEU C 1 54 ? 23.402  -35.106 26.654  1.00 38.99  ? 53  LEU C N   1 
ATOM   1840 C  CA  . LEU C 1 54 ? 24.564  -34.895 25.800  1.00 41.21  ? 53  LEU C CA  1 
ATOM   1841 C  C   . LEU C 1 54 ? 25.655  -34.159 26.576  1.00 41.66  ? 53  LEU C C   1 
ATOM   1842 O  O   . LEU C 1 54 ? 25.369  -33.400 27.498  1.00 42.26  ? 53  LEU C O   1 
ATOM   1843 C  CB  . LEU C 1 54 ? 24.209  -34.164 24.500  1.00 38.22  ? 53  LEU C CB  1 
ATOM   1844 C  CG  . LEU C 1 54 ? 23.369  -34.938 23.482  1.00 40.24  ? 53  LEU C CG  1 
ATOM   1845 C  CD1 . LEU C 1 54 ? 23.020  -34.066 22.287  1.00 35.90  ? 53  LEU C CD1 1 
ATOM   1846 C  CD2 . LEU C 1 54 ? 24.104  -36.186 23.008  1.00 46.51  ? 53  LEU C CD2 1 
ATOM   1847 N  N   . GLY C 1 55 ? 26.908  -34.414 26.180  1.00 43.75  ? 54  GLY C N   1 
ATOM   1848 C  CA  . GLY C 1 55 ? 28.078  -33.735 26.708  1.00 41.34  ? 54  GLY C CA  1 
ATOM   1849 C  C   . GLY C 1 55 ? 28.296  -32.401 25.996  1.00 48.00  ? 54  GLY C C   1 
ATOM   1850 O  O   . GLY C 1 55 ? 27.834  -32.194 24.862  1.00 43.57  ? 54  GLY C O   1 
ATOM   1851 N  N   . PRO C 1 56 ? 29.025  -31.462 26.638  1.00 46.98  ? 55  PRO C N   1 
ATOM   1852 C  CA  . PRO C 1 56 ? 29.145  -30.095 26.123  1.00 51.97  ? 55  PRO C CA  1 
ATOM   1853 C  C   . PRO C 1 56 ? 29.824  -30.064 24.756  1.00 46.96  ? 55  PRO C C   1 
ATOM   1854 O  O   . PRO C 1 56 ? 29.571  -29.166 23.960  1.00 52.46  ? 55  PRO C O   1 
ATOM   1855 C  CB  . PRO C 1 56 ? 29.937  -29.357 27.217  1.00 53.49  ? 55  PRO C CB  1 
ATOM   1856 C  CG  . PRO C 1 56 ? 30.698  -30.470 27.915  1.00 52.62  ? 55  PRO C CG  1 
ATOM   1857 C  CD  . PRO C 1 56 ? 29.761  -31.671 27.902  1.00 51.60  ? 55  PRO C CD  1 
ATOM   1858 N  N   . LYS C 1 57 ? 30.633  -31.091 24.487  1.00 41.24  ? 56  LYS C N   1 
ATOM   1859 C  CA  . LYS C 1 57 ? 31.267  -31.321 23.198  1.00 43.90  ? 56  LYS C CA  1 
ATOM   1860 C  C   . LYS C 1 57 ? 30.233  -31.394 22.075  1.00 47.86  ? 56  LYS C C   1 
ATOM   1861 O  O   . LYS C 1 57 ? 30.564  -31.138 20.914  1.00 45.53  ? 56  LYS C O   1 
ATOM   1862 C  CB  . LYS C 1 57 ? 31.976  -32.682 23.156  1.00 44.98  ? 56  LYS C CB  1 
ATOM   1863 N  N   . ASP C 1 58 ? 28.994  -31.783 22.416  1.00 48.35  ? 57  ASP C N   1 
ATOM   1864 C  CA  . ASP C 1 58 ? 28.000  -32.064 21.395  1.00 45.25  ? 57  ASP C CA  1 
ATOM   1865 C  C   . ASP C 1 58 ? 27.039  -30.900 21.211  1.00 43.76  ? 57  ASP C C   1 
ATOM   1866 O  O   . ASP C 1 58 ? 26.050  -31.046 20.496  1.00 39.37  ? 57  ASP C O   1 
ATOM   1867 C  CB  . ASP C 1 58 ? 27.236  -33.335 21.708  1.00 53.17  ? 57  ASP C CB  1 
ATOM   1868 C  CG  . ASP C 1 58 ? 28.119  -34.566 21.755  1.00 53.14  ? 57  ASP C CG  1 
ATOM   1869 O  OD1 . ASP C 1 58 ? 28.955  -34.701 20.840  1.00 58.37  ? 57  ASP C OD1 1 
ATOM   1870 O  OD2 . ASP C 1 58 ? 27.947  -35.364 22.691  1.00 56.17  ? 57  ASP C OD2 1 
ATOM   1871 N  N   . LEU C 1 59 ? 27.346  -29.763 21.846  1.00 38.88  ? 58  LEU C N   1 
ATOM   1872 C  CA  . LEU C 1 59 ? 26.425  -28.645 21.974  1.00 44.88  ? 58  LEU C CA  1 
ATOM   1873 C  C   . LEU C 1 59 ? 27.091  -27.385 21.441  1.00 46.72  ? 58  LEU C C   1 
ATOM   1874 O  O   . LEU C 1 59 ? 28.271  -27.185 21.705  1.00 46.12  ? 58  LEU C O   1 
ATOM   1875 C  CB  . LEU C 1 59 ? 26.077  -28.445 23.446  1.00 39.58  ? 58  LEU C CB  1 
ATOM   1876 C  CG  . LEU C 1 59 ? 25.455  -29.637 24.169  1.00 41.52  ? 58  LEU C CG  1 
ATOM   1877 C  CD1 . LEU C 1 59 ? 25.216  -29.243 25.621  1.00 41.79  ? 58  LEU C CD1 1 
ATOM   1878 C  CD2 . LEU C 1 59 ? 24.154  -30.084 23.507  1.00 35.36  ? 58  LEU C CD2 1 
ATOM   1879 N  N   . PHE C 1 60 ? 26.306  -26.539 20.751  1.00 48.49  ? 59  PHE C N   1 
ATOM   1880 C  CA  . PHE C 1 60 ? 26.777  -25.305 20.130  1.00 44.93  ? 59  PHE C CA  1 
ATOM   1881 C  C   . PHE C 1 60 ? 25.777  -24.179 20.394  1.00 48.57  ? 59  PHE C C   1 
ATOM   1882 O  O   . PHE C 1 60 ? 24.594  -24.324 20.073  1.00 46.11  ? 59  PHE C O   1 
ATOM   1883 C  CB  . PHE C 1 60 ? 26.947  -25.514 18.623  1.00 41.18  ? 59  PHE C CB  1 
ATOM   1884 C  CG  . PHE C 1 60 ? 27.869  -26.666 18.254  1.00 45.60  ? 59  PHE C CG  1 
ATOM   1885 C  CD1 . PHE C 1 60 ? 27.426  -27.986 18.321  1.00 41.00  ? 59  PHE C CD1 1 
ATOM   1886 C  CD2 . PHE C 1 60 ? 29.182  -26.426 17.848  1.00 46.47  ? 59  PHE C CD2 1 
ATOM   1887 C  CE1 . PHE C 1 60 ? 28.280  -29.040 18.020  1.00 40.23  ? 59  PHE C CE1 1 
ATOM   1888 C  CE2 . PHE C 1 60 ? 30.028  -27.483 17.532  1.00 42.94  ? 59  PHE C CE2 1 
ATOM   1889 C  CZ  . PHE C 1 60 ? 29.570  -28.782 17.617  1.00 45.48  ? 59  PHE C CZ  1 
ATOM   1890 N  N   . PRO C 1 61 ? 26.199  -23.031 20.995  1.00 47.79  ? 60  PRO C N   1 
ATOM   1891 C  CA  . PRO C 1 61 ? 25.278  -21.918 21.246  1.00 49.75  ? 60  PRO C CA  1 
ATOM   1892 C  C   . PRO C 1 61 ? 24.567  -21.516 19.956  1.00 46.90  ? 60  PRO C C   1 
ATOM   1893 O  O   . PRO C 1 61 ? 25.200  -21.416 18.905  1.00 45.60  ? 60  PRO C O   1 
ATOM   1894 C  CB  . PRO C 1 61 ? 26.118  -20.762 21.848  1.00 49.58  ? 60  PRO C CB  1 
ATOM   1895 C  CG  . PRO C 1 61 ? 27.482  -21.378 22.119  1.00 53.79  ? 60  PRO C CG  1 
ATOM   1896 C  CD  . PRO C 1 61 ? 27.576  -22.747 21.448  1.00 51.72  ? 60  PRO C CD  1 
ATOM   1897 N  N   . TYR C 1 62 ? 23.248  -21.303 20.068  1.00 48.23  ? 61  TYR C N   1 
ATOM   1898 C  CA  . TYR C 1 62 ? 22.372  -21.060 18.932  1.00 50.64  ? 61  TYR C CA  1 
ATOM   1899 C  C   . TYR C 1 62 ? 22.772  -19.803 18.156  1.00 58.24  ? 61  TYR C C   1 
ATOM   1900 O  O   . TYR C 1 62 ? 22.857  -19.853 16.932  1.00 57.98  ? 61  TYR C O   1 
ATOM   1901 C  CB  . TYR C 1 62 ? 20.904  -21.017 19.358  1.00 47.76  ? 61  TYR C CB  1 
ATOM   1902 C  CG  . TYR C 1 62 ? 19.935  -20.602 18.262  1.00 51.74  ? 61  TYR C CG  1 
ATOM   1903 C  CD1 . TYR C 1 62 ? 19.755  -21.393 17.128  1.00 49.71  ? 61  TYR C CD1 1 
ATOM   1904 C  CD2 . TYR C 1 62 ? 19.173  -19.442 18.384  1.00 51.95  ? 61  TYR C CD2 1 
ATOM   1905 C  CE1 . TYR C 1 62 ? 18.858  -21.025 16.136  1.00 48.25  ? 61  TYR C CE1 1 
ATOM   1906 C  CE2 . TYR C 1 62 ? 18.285  -19.055 17.396  1.00 50.52  ? 61  TYR C CE2 1 
ATOM   1907 C  CZ  . TYR C 1 62 ? 18.132  -19.850 16.269  1.00 48.81  ? 61  TYR C CZ  1 
ATOM   1908 O  OH  . TYR C 1 62 ? 17.246  -19.477 15.304  1.00 45.56  ? 61  TYR C OH  1 
ATOM   1909 N  N   . ASP C 1 63 ? 23.024  -18.691 18.861  1.00 61.31  ? 62  ASP C N   1 
ATOM   1910 C  CA  . ASP C 1 63 ? 23.365  -17.434 18.208  1.00 64.70  ? 62  ASP C CA  1 
ATOM   1911 C  C   . ASP C 1 63 ? 24.717  -17.519 17.506  1.00 58.46  ? 62  ASP C C   1 
ATOM   1912 O  O   . ASP C 1 63 ? 24.925  -16.876 16.480  1.00 64.16  ? 62  ASP C O   1 
ATOM   1913 C  CB  . ASP C 1 63 ? 23.233  -16.242 19.145  1.00 66.87  ? 62  ASP C CB  1 
ATOM   1914 C  CG  . ASP C 1 63 ? 21.852  -15.604 19.135  1.00 76.30  ? 62  ASP C CG  1 
ATOM   1915 O  OD1 . ASP C 1 63 ? 21.176  -15.652 20.184  1.00 69.97  ? 62  ASP C OD1 1 
ATOM   1916 O  OD2 . ASP C 1 63 ? 21.455  -15.085 18.064  1.00 86.95  ? 62  ASP C OD2 1 
ATOM   1917 N  N   . LYS C 1 64 ? 25.629  -18.318 18.061  1.00 51.18  ? 63  LYS C N   1 
ATOM   1918 C  CA  . LYS C 1 64 ? 26.978  -18.412 17.523  1.00 49.02  ? 63  LYS C CA  1 
ATOM   1919 C  C   . LYS C 1 64 ? 26.996  -19.279 16.268  1.00 50.35  ? 63  LYS C C   1 
ATOM   1920 O  O   . LYS C 1 64 ? 27.845  -19.062 15.409  1.00 51.34  ? 63  LYS C O   1 
ATOM   1921 C  CB  . LYS C 1 64 ? 28.005  -18.916 18.549  1.00 49.60  ? 63  LYS C CB  1 
ATOM   1922 N  N   . SER C 1 65 ? 26.073  -20.257 16.160  1.00 47.78  ? 64  SER C N   1 
ATOM   1923 C  CA  . SER C 1 65 ? 26.266  -21.321 15.177  1.00 45.39  ? 64  SER C CA  1 
ATOM   1924 C  C   . SER C 1 65 ? 25.115  -21.416 14.161  1.00 42.94  ? 64  SER C C   1 
ATOM   1925 O  O   . SER C 1 65 ? 25.145  -22.257 13.266  1.00 40.79  ? 64  SER C O   1 
ATOM   1926 C  CB  . SER C 1 65 ? 26.535  -22.651 15.867  1.00 48.15  ? 64  SER C CB  1 
ATOM   1927 O  OG  . SER C 1 65 ? 25.375  -23.105 16.554  1.00 40.33  ? 64  SER C OG  1 
ATOM   1928 N  N   . LYS C 1 66 ? 24.092  -20.562 14.298  1.00 40.28  ? 65  LYS C N   1 
ATOM   1929 C  CA  . LYS C 1 66 ? 22.893  -20.706 13.479  1.00 41.59  ? 65  LYS C CA  1 
ATOM   1930 C  C   . LYS C 1 66 ? 23.168  -20.470 11.992  1.00 44.50  ? 65  LYS C C   1 
ATOM   1931 O  O   . LYS C 1 66 ? 22.482  -21.051 11.156  1.00 47.39  ? 65  LYS C O   1 
ATOM   1932 C  CB  . LYS C 1 66 ? 21.705  -19.880 13.970  1.00 40.84  ? 65  LYS C CB  1 
ATOM   1933 C  CG  . LYS C 1 66 ? 21.894  -18.385 13.862  1.00 42.20  ? 65  LYS C CG  1 
ATOM   1934 C  CD  . LYS C 1 66 ? 20.714  -17.668 14.493  1.00 51.69  ? 65  LYS C CD  1 
ATOM   1935 C  CE  . LYS C 1 66 ? 20.787  -16.186 14.328  1.00 55.35  ? 65  LYS C CE  1 
ATOM   1936 N  NZ  . LYS C 1 66 ? 19.757  -15.625 15.198  1.00 65.11  ? 65  LYS C NZ  1 
ATOM   1937 N  N   . ASP C 1 67 ? 24.158  -19.622 11.668  1.00 51.30  ? 66  ASP C N   1 
ATOM   1938 C  CA  . ASP C 1 67 ? 24.544  -19.373 10.280  1.00 47.81  ? 66  ASP C CA  1 
ATOM   1939 C  C   . ASP C 1 67 ? 24.948  -20.697 9.637   1.00 46.09  ? 66  ASP C C   1 
ATOM   1940 O  O   . ASP C 1 67 ? 24.629  -20.954 8.482   1.00 46.99  ? 66  ASP C O   1 
ATOM   1941 C  CB  . ASP C 1 67 ? 25.538  -18.222 10.132  1.00 50.90  ? 66  ASP C CB  1 
ATOM   1942 C  CG  . ASP C 1 67 ? 26.885  -18.355 10.841  1.00 59.45  ? 66  ASP C CG  1 
ATOM   1943 O  OD1 . ASP C 1 67 ? 27.094  -19.364 11.556  1.00 65.17  ? 66  ASP C OD1 1 
ATOM   1944 O  OD2 . ASP C 1 67 ? 27.723  -17.430 10.693  1.00 59.18  ? 66  ASP C OD2 1 
ATOM   1945 N  N   . LYS C 1 68 ? 25.576  -21.569 10.435  1.00 40.26  ? 67  LYS C N   1 
ATOM   1946 C  CA  . LYS C 1 68 ? 26.101  -22.836 9.951   1.00 41.43  ? 67  LYS C CA  1 
ATOM   1947 C  C   . LYS C 1 68 ? 25.036  -23.939 10.004  1.00 41.49  ? 67  LYS C C   1 
ATOM   1948 O  O   . LYS C 1 68 ? 24.810  -24.608 8.999   1.00 45.56  ? 67  LYS C O   1 
ATOM   1949 C  CB  . LYS C 1 68 ? 27.394  -23.137 10.721  1.00 44.56  ? 67  LYS C CB  1 
ATOM   1950 C  CG  . LYS C 1 68 ? 28.085  -24.443 10.386  1.00 48.20  ? 67  LYS C CG  1 
ATOM   1951 C  CD  . LYS C 1 68 ? 29.454  -24.517 11.067  1.00 57.90  ? 67  LYS C CD  1 
ATOM   1952 C  CE  . LYS C 1 68 ? 30.080  -25.884 11.074  1.00 65.44  ? 67  LYS C CE  1 
ATOM   1953 N  NZ  . LYS C 1 68 ? 30.271  -26.460 9.737   1.00 63.55  ? 67  LYS C NZ  1 
ATOM   1954 N  N   . TYR C 1 69 ? 24.373  -24.125 11.162  1.00 35.05  ? 68  TYR C N   1 
ATOM   1955 C  CA  . TYR C 1 69 ? 23.505  -25.281 11.341  1.00 38.73  ? 68  TYR C CA  1 
ATOM   1956 C  C   . TYR C 1 69 ? 22.027  -24.951 11.120  1.00 36.94  ? 68  TYR C C   1 
ATOM   1957 O  O   . TYR C 1 69 ? 21.226  -25.866 10.974  1.00 39.02  ? 68  TYR C O   1 
ATOM   1958 C  CB  . TYR C 1 69 ? 23.650  -25.845 12.760  1.00 35.87  ? 68  TYR C CB  1 
ATOM   1959 C  CG  . TYR C 1 69 ? 25.067  -26.284 13.076  1.00 38.46  ? 68  TYR C CG  1 
ATOM   1960 C  CD1 . TYR C 1 69 ? 25.808  -27.038 12.165  1.00 39.93  ? 68  TYR C CD1 1 
ATOM   1961 C  CD2 . TYR C 1 69 ? 25.672  -25.895 14.261  1.00 38.44  ? 68  TYR C CD2 1 
ATOM   1962 C  CE1 . TYR C 1 69 ? 27.109  -27.427 12.447  1.00 39.84  ? 68  TYR C CE1 1 
ATOM   1963 C  CE2 . TYR C 1 69 ? 26.978  -26.269 14.548  1.00 42.23  ? 68  TYR C CE2 1 
ATOM   1964 C  CZ  . TYR C 1 69 ? 27.687  -27.043 13.645  1.00 42.13  ? 68  TYR C CZ  1 
ATOM   1965 O  OH  . TYR C 1 69 ? 28.975  -27.374 13.946  1.00 47.00  ? 68  TYR C OH  1 
ATOM   1966 N  N   . GLY C 1 70 ? 21.655  -23.664 11.154  1.00 36.05  ? 69  GLY C N   1 
ATOM   1967 C  CA  . GLY C 1 70 ? 20.250  -23.291 11.057  1.00 39.27  ? 69  GLY C CA  1 
ATOM   1968 C  C   . GLY C 1 70 ? 19.842  -23.145 9.595   1.00 42.40  ? 69  GLY C C   1 
ATOM   1969 O  O   . GLY C 1 70 ? 19.767  -22.037 9.053   1.00 41.53  ? 69  GLY C O   1 
ATOM   1970 N  N   . LYS C 1 71 ? 19.662  -24.294 8.953   1.00 41.09  ? 70  LYS C N   1 
ATOM   1971 C  CA  . LYS C 1 71 ? 19.271  -24.365 7.557   1.00 43.77  ? 70  LYS C CA  1 
ATOM   1972 C  C   . LYS C 1 71 ? 18.386  -25.590 7.428   1.00 43.33  ? 70  LYS C C   1 
ATOM   1973 O  O   . LYS C 1 71 ? 18.602  -26.578 8.127   1.00 45.98  ? 70  LYS C O   1 
ATOM   1974 C  CB  . LYS C 1 71 ? 20.477  -24.444 6.613   1.00 40.68  ? 70  LYS C CB  1 
ATOM   1975 C  CG  . LYS C 1 71 ? 21.585  -25.388 7.057   1.00 49.63  ? 70  LYS C CG  1 
ATOM   1976 C  CD  . LYS C 1 71 ? 22.534  -25.917 5.989   1.00 57.08  ? 70  LYS C CD  1 
ATOM   1977 C  CE  . LYS C 1 71 ? 23.429  -26.959 6.591   1.00 62.58  ? 70  LYS C CE  1 
ATOM   1978 N  N   . PRO C 1 72 ? 17.358  -25.563 6.553   1.00 38.44  ? 71  PRO C N   1 
ATOM   1979 C  CA  . PRO C 1 72 ? 16.419  -26.674 6.488   1.00 36.53  ? 71  PRO C CA  1 
ATOM   1980 C  C   . PRO C 1 72 ? 17.102  -28.000 6.177   1.00 40.71  ? 71  PRO C C   1 
ATOM   1981 O  O   . PRO C 1 72 ? 18.187  -28.058 5.590   1.00 40.87  ? 71  PRO C O   1 
ATOM   1982 C  CB  . PRO C 1 72 ? 15.453  -26.211 5.387   1.00 36.66  ? 71  PRO C CB  1 
ATOM   1983 C  CG  . PRO C 1 72 ? 15.505  -24.709 5.506   1.00 36.92  ? 71  PRO C CG  1 
ATOM   1984 C  CD  . PRO C 1 72 ? 16.999  -24.439 5.671   1.00 39.32  ? 71  PRO C CD  1 
ATOM   1985 N  N   . ASN C 1 73 ? 16.456  -29.074 6.605   1.00 40.28  ? 72  ASN C N   1 
ATOM   1986 C  CA  . ASN C 1 73 ? 16.723  -30.349 5.976   1.00 49.29  ? 72  ASN C CA  1 
ATOM   1987 C  C   . ASN C 1 73 ? 15.469  -31.189 6.136   1.00 41.11  ? 72  ASN C C   1 
ATOM   1988 O  O   . ASN C 1 73 ? 14.516  -30.739 6.775   1.00 37.61  ? 72  ASN C O   1 
ATOM   1989 C  CB  . ASN C 1 73 ? 18.047  -30.969 6.406   1.00 51.15  ? 72  ASN C CB  1 
ATOM   1990 C  CG  . ASN C 1 73 ? 17.960  -31.481 7.816   1.00 46.29  ? 72  ASN C CG  1 
ATOM   1991 O  OD1 . ASN C 1 73 ? 17.186  -32.405 8.099   1.00 45.99  ? 72  ASN C OD1 1 
ATOM   1992 N  ND2 . ASN C 1 73 ? 18.751  -30.891 8.690   1.00 47.87  ? 72  ASN C ND2 1 
ATOM   1993 N  N   . LYS C 1 74 ? 15.501  -32.386 5.541   1.00 46.99  ? 73  LYS C N   1 
ATOM   1994 C  CA  . LYS C 1 74 ? 14.291  -33.162 5.335   1.00 42.34  ? 73  LYS C CA  1 
ATOM   1995 C  C   . LYS C 1 74 ? 14.030  -34.089 6.514   1.00 43.33  ? 73  LYS C C   1 
ATOM   1996 O  O   . LYS C 1 74 ? 12.963  -34.690 6.567   1.00 42.90  ? 73  LYS C O   1 
ATOM   1997 C  CB  . LYS C 1 74 ? 14.293  -33.911 3.993   1.00 41.59  ? 73  LYS C CB  1 
ATOM   1998 N  N   . ARG C 1 75 ? 14.979  -34.192 7.462   1.00 39.78  ? 74  ARG C N   1 
ATOM   1999 C  CA  . ARG C 1 75 ? 14.824  -35.130 8.568   1.00 38.74  ? 74  ARG C CA  1 
ATOM   2000 C  C   . ARG C 1 75 ? 13.544  -34.775 9.317   1.00 40.83  ? 74  ARG C C   1 
ATOM   2001 O  O   . ARG C 1 75 ? 13.232  -33.592 9.493   1.00 35.39  ? 74  ARG C O   1 
ATOM   2002 C  CB  . ARG C 1 75 ? 16.018  -35.252 9.541   1.00 39.51  ? 74  ARG C CB  1 
ATOM   2003 C  CG  . ARG C 1 75 ? 17.364  -35.531 8.874   1.00 47.47  ? 74  ARG C CG  1 
ATOM   2004 C  CD  . ARG C 1 75 ? 17.514  -36.917 8.236   1.00 48.13  ? 74  ARG C CD  1 
ATOM   2005 N  NE  . ARG C 1 75 ? 17.529  -37.936 9.291   1.00 46.25  ? 74  ARG C NE  1 
ATOM   2006 C  CZ  . ARG C 1 75 ? 18.624  -38.290 9.967   1.00 44.47  ? 74  ARG C CZ  1 
ATOM   2007 N  NH1 . ARG C 1 75 ? 18.502  -38.898 11.130  1.00 43.09  ? 74  ARG C NH1 1 
ATOM   2008 N  NH2 . ARG C 1 75 ? 19.821  -37.939 9.527   1.00 44.19  ? 74  ARG C NH2 1 
ATOM   2009 N  N   . LYS C 1 76 ? 12.854  -35.815 9.798   1.00 43.38  ? 75  LYS C N   1 
ATOM   2010 C  CA  . LYS C 1 76 ? 11.520  -35.687 10.364  1.00 47.84  ? 75  LYS C CA  1 
ATOM   2011 C  C   . LYS C 1 76 ? 11.567  -34.770 11.580  1.00 47.42  ? 75  LYS C C   1 
ATOM   2012 O  O   . LYS C 1 76 ? 12.286  -35.034 12.545  1.00 43.03  ? 75  LYS C O   1 
ATOM   2013 C  CB  . LYS C 1 76 ? 10.866  -37.050 10.642  1.00 55.88  ? 75  LYS C CB  1 
ATOM   2014 C  CG  . LYS C 1 76 ? 9.337   -37.079 10.476  1.00 61.39  ? 75  LYS C CG  1 
ATOM   2015 C  CD  . LYS C 1 76 ? 8.617   -37.932 11.518  1.00 63.20  ? 75  LYS C CD  1 
ATOM   2016 N  N   . GLY C 1 77 ? 10.812  -33.666 11.507  1.00 41.59  ? 76  GLY C N   1 
ATOM   2017 C  CA  . GLY C 1 77 ? 10.661  -32.820 12.679  1.00 41.95  ? 76  GLY C CA  1 
ATOM   2018 C  C   . GLY C 1 77 ? 11.618  -31.631 12.649  1.00 34.81  ? 76  GLY C C   1 
ATOM   2019 O  O   . GLY C 1 77 ? 11.455  -30.684 13.415  1.00 36.75  ? 76  GLY C O   1 
ATOM   2020 N  N   . PHE C 1 78 ? 12.613  -31.693 11.748  1.00 37.28  ? 77  PHE C N   1 
ATOM   2021 C  CA  . PHE C 1 78 ? 13.700  -30.736 11.731  1.00 33.32  ? 77  PHE C CA  1 
ATOM   2022 C  C   . PHE C 1 78 ? 13.166  -29.316 11.517  1.00 35.04  ? 77  PHE C C   1 
ATOM   2023 O  O   . PHE C 1 78 ? 13.523  -28.378 12.237  1.00 32.82  ? 77  PHE C O   1 
ATOM   2024 C  CB  . PHE C 1 78 ? 14.779  -31.069 10.690  1.00 33.71  ? 77  PHE C CB  1 
ATOM   2025 C  CG  . PHE C 1 78 ? 16.062  -30.306 10.997  1.00 36.62  ? 77  PHE C CG  1 
ATOM   2026 C  CD1 . PHE C 1 78 ? 16.282  -29.031 10.490  1.00 35.08  ? 77  PHE C CD1 1 
ATOM   2027 C  CD2 . PHE C 1 78 ? 17.052  -30.869 11.799  1.00 35.84  ? 77  PHE C CD2 1 
ATOM   2028 C  CE1 . PHE C 1 78 ? 17.450  -28.327 10.783  1.00 36.76  ? 77  PHE C CE1 1 
ATOM   2029 C  CE2 . PHE C 1 78 ? 18.220  -30.164 12.084  1.00 32.66  ? 77  PHE C CE2 1 
ATOM   2030 C  CZ  . PHE C 1 78 ? 18.411  -28.888 11.597  1.00 37.05  ? 77  PHE C CZ  1 
ATOM   2031 N  N   . ASN C 1 79 ? 12.379  -29.135 10.455  1.00 35.53  ? 78  ASN C N   1 
ATOM   2032 C  CA  . ASN C 1 79 ? 12.060  -27.774 10.058  1.00 38.57  ? 78  ASN C CA  1 
ATOM   2033 C  C   . ASN C 1 79 ? 11.090  -27.159 11.065  1.00 35.88  ? 78  ASN C C   1 
ATOM   2034 O  O   . ASN C 1 79 ? 11.152  -25.958 11.358  1.00 35.45  ? 78  ASN C O   1 
ATOM   2035 C  CB  . ASN C 1 79 ? 11.602  -27.714 8.606   1.00 39.79  ? 78  ASN C CB  1 
ATOM   2036 C  CG  . ASN C 1 79 ? 12.668  -28.187 7.644   1.00 40.96  ? 78  ASN C CG  1 
ATOM   2037 O  OD1 . ASN C 1 79 ? 13.869  -28.052 7.910   1.00 35.60  ? 78  ASN C OD1 1 
ATOM   2038 N  ND2 . ASN C 1 79 ? 12.253  -28.667 6.479   1.00 39.84  ? 78  ASN C ND2 1 
ATOM   2039 N  N   . GLU C 1 80 ? 10.181  -27.973 11.603  1.00 40.54  ? 79  GLU C N   1 
ATOM   2040 C  CA  . GLU C 1 80 ? 9.332   -27.499 12.685  1.00 37.80  ? 79  GLU C CA  1 
ATOM   2041 C  C   . GLU C 1 80 ? 10.191  -27.080 13.875  1.00 44.10  ? 79  GLU C C   1 
ATOM   2042 O  O   . GLU C 1 80 ? 9.887   -26.065 14.518  1.00 42.68  ? 79  GLU C O   1 
ATOM   2043 C  CB  . GLU C 1 80 ? 8.257   -28.511 13.080  1.00 42.22  ? 79  GLU C CB  1 
ATOM   2044 C  CG  . GLU C 1 80 ? 7.305   -27.977 14.146  1.00 41.46  ? 79  GLU C CG  1 
ATOM   2045 C  CD  . GLU C 1 80 ? 6.025   -28.785 14.282  1.00 54.60  ? 79  GLU C CD  1 
ATOM   2046 O  OE1 . GLU C 1 80 ? 5.918   -29.846 13.622  1.00 58.29  ? 79  GLU C OE1 1 
ATOM   2047 O  OE2 . GLU C 1 80 ? 5.122   -28.348 15.035  1.00 52.17  ? 79  GLU C OE2 1 
ATOM   2048 N  N   . GLY C 1 81 ? 11.266  -27.861 14.133  1.00 36.69  ? 80  GLY C N   1 
ATOM   2049 C  CA  . GLY C 1 81 ? 12.258  -27.515 15.151  1.00 33.98  ? 80  GLY C CA  1 
ATOM   2050 C  C   . GLY C 1 81 ? 12.857  -26.124 14.932  1.00 32.30  ? 80  GLY C C   1 
ATOM   2051 O  O   . GLY C 1 81 ? 13.119  -25.381 15.872  1.00 32.70  ? 80  GLY C O   1 
ATOM   2052 N  N   . LEU C 1 82 ? 13.155  -25.804 13.675  1.00 34.40  ? 81  LEU C N   1 
ATOM   2053 C  CA  . LEU C 1 82 ? 13.782  -24.537 13.347  1.00 35.80  ? 81  LEU C CA  1 
ATOM   2054 C  C   . LEU C 1 82 ? 12.817  -23.379 13.605  1.00 32.98  ? 81  LEU C C   1 
ATOM   2055 O  O   . LEU C 1 82 ? 13.231  -22.319 14.086  1.00 33.73  ? 81  LEU C O   1 
ATOM   2056 C  CB  . LEU C 1 82 ? 14.207  -24.586 11.879  1.00 41.07  ? 81  LEU C CB  1 
ATOM   2057 C  CG  . LEU C 1 82 ? 15.496  -25.349 11.560  1.00 35.88  ? 81  LEU C CG  1 
ATOM   2058 C  CD1 . LEU C 1 82 ? 15.766  -25.277 10.055  1.00 37.16  ? 81  LEU C CD1 1 
ATOM   2059 C  CD2 . LEU C 1 82 ? 16.653  -24.746 12.315  1.00 35.68  ? 81  LEU C CD2 1 
ATOM   2060 N  N   . TRP C 1 83 ? 11.539  -23.569 13.252  1.00 33.35  ? 82  TRP C N   1 
ATOM   2061 C  CA  . TRP C 1 83 ? 10.528  -22.563 13.560  1.00 37.86  ? 82  TRP C CA  1 
ATOM   2062 C  C   . TRP C 1 83 ? 10.413  -22.307 15.075  1.00 40.14  ? 82  TRP C C   1 
ATOM   2063 O  O   . TRP C 1 83 ? 10.372  -21.153 15.519  1.00 40.47  ? 82  TRP C O   1 
ATOM   2064 C  CB  . TRP C 1 83 ? 9.184   -22.935 12.920  1.00 36.03  ? 82  TRP C CB  1 
ATOM   2065 C  CG  . TRP C 1 83 ? 8.157   -21.840 13.063  1.00 45.71  ? 82  TRP C CG  1 
ATOM   2066 C  CD1 . TRP C 1 83 ? 7.878   -20.848 12.170  1.00 44.28  ? 82  TRP C CD1 1 
ATOM   2067 C  CD2 . TRP C 1 83 ? 7.298   -21.609 14.202  1.00 46.67  ? 82  TRP C CD2 1 
ATOM   2068 N  NE1 . TRP C 1 83 ? 6.903   -20.026 12.663  1.00 47.37  ? 82  TRP C NE1 1 
ATOM   2069 C  CE2 . TRP C 1 83 ? 6.528   -20.462 13.905  1.00 48.23  ? 82  TRP C CE2 1 
ATOM   2070 C  CE3 . TRP C 1 83 ? 7.109   -22.251 15.433  1.00 46.41  ? 82  TRP C CE3 1 
ATOM   2071 C  CZ2 . TRP C 1 83 ? 5.580   -19.958 14.794  1.00 56.07  ? 82  TRP C CZ2 1 
ATOM   2072 C  CZ3 . TRP C 1 83 ? 6.181   -21.747 16.318  1.00 46.29  ? 82  TRP C CZ3 1 
ATOM   2073 C  CH2 . TRP C 1 83 ? 5.427   -20.616 15.999  1.00 53.44  ? 82  TRP C CH2 1 
ATOM   2074 N  N   . GLU C 1 84 ? 10.418  -23.381 15.872  1.00 38.80  ? 83  GLU C N   1 
ATOM   2075 C  CA  . GLU C 1 84 ? 10.261  -23.282 17.321  1.00 38.70  ? 83  GLU C CA  1 
ATOM   2076 C  C   . GLU C 1 84 ? 11.417  -22.516 17.947  1.00 38.90  ? 83  GLU C C   1 
ATOM   2077 O  O   . GLU C 1 84 ? 11.174  -21.683 18.822  1.00 41.41  ? 83  GLU C O   1 
ATOM   2078 C  CB  . GLU C 1 84 ? 10.186  -24.635 18.032  1.00 34.26  ? 83  GLU C CB  1 
ATOM   2079 C  CG  . GLU C 1 84 ? 8.893   -25.370 17.702  1.00 40.07  ? 83  GLU C CG  1 
ATOM   2080 C  CD  . GLU C 1 84 ? 8.749   -26.790 18.184  1.00 46.32  ? 83  GLU C CD  1 
ATOM   2081 O  OE1 . GLU C 1 84 ? 9.720   -27.279 18.797  1.00 42.41  ? 83  GLU C OE1 1 
ATOM   2082 O  OE2 . GLU C 1 84 ? 7.680   -27.402 17.924  1.00 45.71  ? 83  GLU C OE2 1 
ATOM   2083 N  N   . ILE C 1 85 ? 12.658  -22.787 17.490  1.00 35.55  ? 84  ILE C N   1 
ATOM   2084 C  CA  . ILE C 1 85 ? 13.842  -22.227 18.131  1.00 34.90  ? 84  ILE C CA  1 
ATOM   2085 C  C   . ILE C 1 85 ? 13.936  -20.715 17.911  1.00 38.17  ? 84  ILE C C   1 
ATOM   2086 O  O   . ILE C 1 85 ? 14.532  -20.015 18.724  1.00 36.38  ? 84  ILE C O   1 
ATOM   2087 C  CB  . ILE C 1 85 ? 15.157  -22.967 17.803  1.00 32.31  ? 84  ILE C CB  1 
ATOM   2088 C  CG1 . ILE C 1 85 ? 16.255  -22.568 18.806  1.00 35.57  ? 84  ILE C CG1 1 
ATOM   2089 C  CG2 . ILE C 1 85 ? 15.613  -22.803 16.349  1.00 32.67  ? 84  ILE C CG2 1 
ATOM   2090 C  CD1 . ILE C 1 85 ? 17.526  -23.391 18.728  1.00 36.78  ? 84  ILE C CD1 1 
ATOM   2091 N  N   . GLN C 1 86 ? 13.392  -20.249 16.785  1.00 38.69  ? 85  GLN C N   1 
ATOM   2092 C  CA  . GLN C 1 86 ? 13.419  -18.857 16.358  1.00 40.60  ? 85  GLN C CA  1 
ATOM   2093 C  C   . GLN C 1 86 ? 12.196  -18.114 16.886  1.00 38.48  ? 85  GLN C C   1 
ATOM   2094 O  O   . GLN C 1 86 ? 12.311  -16.946 17.238  1.00 47.69  ? 85  GLN C O   1 
ATOM   2095 C  CB  . GLN C 1 86 ? 13.431  -18.744 14.827  1.00 40.74  ? 85  GLN C CB  1 
ATOM   2096 C  CG  . GLN C 1 86 ? 13.791  -17.357 14.280  1.00 44.29  ? 85  GLN C CG  1 
ATOM   2097 C  CD  . GLN C 1 86 ? 14.176  -17.350 12.803  1.00 44.03  ? 85  GLN C CD  1 
ATOM   2098 O  OE1 . GLN C 1 86 ? 14.055  -18.349 12.081  1.00 45.61  ? 85  GLN C OE1 1 
ATOM   2099 N  NE2 . GLN C 1 86 ? 14.670  -16.214 12.336  1.00 46.02  ? 85  GLN C NE2 1 
ATOM   2100 N  N   . ASN C 1 87 ? 11.046  -18.792 16.940  1.00 41.99  ? 86  ASN C N   1 
ATOM   2101 C  CA  . ASN C 1 87 ? 9.746   -18.147 17.098  1.00 49.38  ? 86  ASN C CA  1 
ATOM   2102 C  C   . ASN C 1 87 ? 9.047   -18.464 18.426  1.00 50.61  ? 86  ASN C C   1 
ATOM   2103 O  O   . ASN C 1 87 ? 8.138   -17.733 18.803  1.00 51.01  ? 86  ASN C O   1 
ATOM   2104 C  CB  . ASN C 1 87 ? 8.832   -18.410 15.903  1.00 45.54  ? 86  ASN C CB  1 
ATOM   2105 C  CG  . ASN C 1 87 ? 9.420   -17.794 14.654  1.00 47.09  ? 86  ASN C CG  1 
ATOM   2106 O  OD1 . ASN C 1 87 ? 9.417   -16.563 14.517  1.00 48.98  ? 86  ASN C OD1 1 
ATOM   2107 N  ND2 . ASN C 1 87 ? 9.998   -18.605 13.781  1.00 36.94  ? 86  ASN C ND2 1 
ATOM   2108 N  N   . ASN C 1 88 ? 9.406   -19.555 19.120  1.00 48.92  ? 87  ASN C N   1 
ATOM   2109 C  CA  . ASN C 1 88 ? 8.648   -19.945 20.315  1.00 45.73  ? 87  ASN C CA  1 
ATOM   2110 C  C   . ASN C 1 88 ? 9.526   -20.852 21.172  1.00 47.37  ? 87  ASN C C   1 
ATOM   2111 O  O   . ASN C 1 88 ? 9.183   -22.013 21.400  1.00 56.39  ? 87  ASN C O   1 
ATOM   2112 C  CB  . ASN C 1 88 ? 7.382   -20.717 19.936  1.00 51.02  ? 87  ASN C CB  1 
ATOM   2113 C  CG  . ASN C 1 88 ? 6.308   -20.769 21.003  1.00 55.24  ? 87  ASN C CG  1 
ATOM   2114 O  OD1 . ASN C 1 88 ? 6.317   -19.984 21.953  1.00 52.32  ? 87  ASN C OD1 1 
ATOM   2115 N  ND2 . ASN C 1 88 ? 5.346   -21.669 20.852  1.00 58.36  ? 87  ASN C ND2 1 
ATOM   2116 N  N   . PRO C 1 89 ? 10.727  -20.399 21.593  1.00 45.36  ? 88  PRO C N   1 
ATOM   2117 C  CA  . PRO C 1 89 ? 11.716  -21.312 22.167  1.00 47.00  ? 88  PRO C CA  1 
ATOM   2118 C  C   . PRO C 1 89 ? 11.574  -21.678 23.641  1.00 52.24  ? 88  PRO C C   1 
ATOM   2119 O  O   . PRO C 1 89 ? 12.398  -22.444 24.139  1.00 51.40  ? 88  PRO C O   1 
ATOM   2120 C  CB  . PRO C 1 89 ? 13.040  -20.588 21.898  1.00 37.94  ? 88  PRO C CB  1 
ATOM   2121 C  CG  . PRO C 1 89 ? 12.675  -19.117 21.955  1.00 41.11  ? 88  PRO C CG  1 
ATOM   2122 C  CD  . PRO C 1 89 ? 11.250  -19.036 21.422  1.00 41.06  ? 88  PRO C CD  1 
ATOM   2123 N  N   . HIS C 1 90 ? 10.548  -21.132 24.318  1.00 56.60  ? 89  HIS C N   1 
ATOM   2124 C  CA  . HIS C 1 90 ? 10.335  -21.419 25.730  1.00 53.60  ? 89  HIS C CA  1 
ATOM   2125 C  C   . HIS C 1 90 ? 8.892   -21.845 26.023  1.00 61.48  ? 89  HIS C C   1 
ATOM   2126 O  O   . HIS C 1 90 ? 8.451   -21.788 27.166  1.00 69.48  ? 89  HIS C O   1 
ATOM   2127 C  CB  . HIS C 1 90 ? 10.931  -20.326 26.633  1.00 50.40  ? 89  HIS C CB  1 
ATOM   2128 C  CG  . HIS C 1 90 ? 12.350  -19.916 26.335  1.00 51.91  ? 89  HIS C CG  1 
ATOM   2129 N  ND1 . HIS C 1 90 ? 12.674  -18.636 25.928  1.00 52.09  ? 89  HIS C ND1 1 
ATOM   2130 C  CD2 . HIS C 1 90 ? 13.532  -20.551 26.457  1.00 51.54  ? 89  HIS C CD2 1 
ATOM   2131 C  CE1 . HIS C 1 90 ? 13.994  -18.521 25.767  1.00 46.92  ? 89  HIS C CE1 1 
ATOM   2132 N  NE2 . HIS C 1 90 ? 14.538  -19.672 26.090  1.00 47.70  ? 89  HIS C NE2 1 
ATOM   2133 N  N   . ALA C 1 91 ? 8.160   -22.308 25.003  1.00 68.74  ? 90  ALA C N   1 
ATOM   2134 C  CA  . ALA C 1 91 ? 6.864   -22.948 25.210  1.00 79.87  ? 90  ALA C CA  1 
ATOM   2135 C  C   . ALA C 1 91 ? 7.037   -24.300 25.916  1.00 85.44  ? 90  ALA C C   1 
ATOM   2136 O  O   . ALA C 1 91 ? 8.144   -24.644 26.328  1.00 88.65  ? 90  ALA C O   1 
ATOM   2137 C  CB  . ALA C 1 91 ? 6.116   -23.058 23.893  1.00 72.57  ? 90  ALA C CB  1 
ATOM   2138 N  N   . SER C 1 92 ? 5.941   -25.067 26.048  1.00 86.21  ? 91  SER C N   1 
ATOM   2139 C  CA  . SER C 1 92 ? 5.880   -26.212 26.952  1.00 86.18  ? 91  SER C CA  1 
ATOM   2140 C  C   . SER C 1 92 ? 5.988   -27.559 26.232  1.00 86.64  ? 91  SER C C   1 
ATOM   2141 O  O   . SER C 1 92 ? 6.769   -28.420 26.644  1.00 80.35  ? 91  SER C O   1 
ATOM   2142 C  CB  . SER C 1 92 ? 4.650   -26.153 27.827  1.00 81.74  ? 91  SER C CB  1 
ATOM   2143 O  OG  . SER C 1 92 ? 4.849   -25.238 28.895  1.00 88.90  ? 91  SER C OG  1 
ATOM   2144 N  N   . TYR C 1 93 ? 5.154   -27.756 25.201  1.00 90.17  ? 92  TYR C N   1 
ATOM   2145 C  CA  . TYR C 1 93 ? 5.153   -28.969 24.393  1.00 95.08  ? 92  TYR C CA  1 
ATOM   2146 C  C   . TYR C 1 93 ? 5.023   -30.205 25.305  1.00 100.43 ? 92  TYR C C   1 
ATOM   2147 O  O   . TYR C 1 93 ? 3.920   -30.793 25.434  1.00 98.26  ? 92  TYR C O   1 
ATOM   2148 C  CB  . TYR C 1 93 ? 6.420   -29.055 23.532  1.00 93.29  ? 92  TYR C CB  1 
ATOM   2149 C  CG  . TYR C 1 93 ? 6.801   -27.798 22.756  1.00 89.80  ? 92  TYR C CG  1 
ATOM   2150 C  CD1 . TYR C 1 93 ? 6.277   -27.549 21.489  1.00 87.51  ? 92  TYR C CD1 1 
ATOM   2151 C  CD2 . TYR C 1 93 ? 7.696   -26.867 23.282  1.00 79.04  ? 92  TYR C CD2 1 
ATOM   2152 C  CE1 . TYR C 1 93 ? 6.619   -26.411 20.772  1.00 79.14  ? 92  TYR C CE1 1 
ATOM   2153 C  CE2 . TYR C 1 93 ? 8.052   -25.730 22.570  1.00 78.84  ? 92  TYR C CE2 1 
ATOM   2154 C  CZ  . TYR C 1 93 ? 7.513   -25.502 21.314  1.00 79.03  ? 92  TYR C CZ  1 
ATOM   2155 O  OH  . TYR C 1 93 ? 7.847   -24.383 20.608  1.00 76.63  ? 92  TYR C OH  1 
HETATM 2156 S  S   . SO4 D 2 .  ? 0.882   -33.473 1.864   1.00 92.24  ? 101 SO4 A S   1 
HETATM 2157 O  O1  . SO4 D 2 .  ? 1.305   -34.205 0.696   1.00 77.69  ? 101 SO4 A O1  1 
HETATM 2158 O  O2  . SO4 D 2 .  ? 1.062   -32.062 1.640   1.00 91.46  ? 101 SO4 A O2  1 
HETATM 2159 O  O3  . SO4 D 2 .  ? -0.512  -33.737 2.127   1.00 98.83  ? 101 SO4 A O3  1 
HETATM 2160 O  O4  . SO4 D 2 .  ? 1.669   -33.884 2.995   1.00 80.40  ? 101 SO4 A O4  1 
HETATM 2161 S  S   . SO4 E 2 .  ? -9.936  -24.504 1.240   1.00 108.83 ? 102 SO4 A S   1 
HETATM 2162 O  O1  . SO4 E 2 .  ? -9.690  -24.230 -0.152  1.00 112.86 ? 102 SO4 A O1  1 
HETATM 2163 O  O2  . SO4 E 2 .  ? -9.752  -23.304 2.012   1.00 100.12 ? 102 SO4 A O2  1 
HETATM 2164 O  O3  . SO4 E 2 .  ? -11.288 -24.977 1.395   1.00 115.94 ? 102 SO4 A O3  1 
HETATM 2165 O  O4  . SO4 E 2 .  ? -9.016  -25.508 1.703   1.00 103.55 ? 102 SO4 A O4  1 
HETATM 2166 C  C1  . EDO F 3 .  ? 13.713  -19.568 -7.406  1.00 42.54  ? 103 EDO A C1  1 
HETATM 2167 O  O1  . EDO F 3 .  ? 14.890  -18.750 -7.267  1.00 34.41  ? 103 EDO A O1  1 
HETATM 2168 C  C2  . EDO F 3 .  ? 12.682  -19.127 -8.414  1.00 36.97  ? 103 EDO A C2  1 
HETATM 2169 O  O2  . EDO F 3 .  ? 12.328  -17.756 -8.308  1.00 33.88  ? 103 EDO A O2  1 
HETATM 2170 S  S   . SO4 G 2 .  ? 8.612   -29.354 5.866   1.00 70.30  ? 104 SO4 A S   1 
HETATM 2171 O  O1  . SO4 G 2 .  ? 9.307   -28.427 5.029   1.00 67.61  ? 104 SO4 A O1  1 
HETATM 2172 O  O2  . SO4 G 2 .  ? 8.331   -30.549 5.111   1.00 77.60  ? 104 SO4 A O2  1 
HETATM 2173 O  O3  . SO4 G 2 .  ? 9.428   -29.676 7.012   1.00 70.05  ? 104 SO4 A O3  1 
HETATM 2174 O  O4  . SO4 G 2 .  ? 7.366   -28.774 6.299   1.00 81.45  ? 104 SO4 A O4  1 
HETATM 2175 S  S   . SO4 H 2 .  ? 6.993   -8.841  -24.875 1.00 63.26  ? 101 SO4 B S   1 
HETATM 2176 O  O1  . SO4 H 2 .  ? 8.228   -8.544  -25.576 1.00 44.74  ? 101 SO4 B O1  1 
HETATM 2177 O  O2  . SO4 H 2 .  ? 6.320   -9.953  -25.492 1.00 61.28  ? 101 SO4 B O2  1 
HETATM 2178 O  O3  . SO4 H 2 .  ? 7.279   -9.169  -23.492 1.00 42.90  ? 101 SO4 B O3  1 
HETATM 2179 O  O4  . SO4 H 2 .  ? 6.145   -7.680  -24.947 1.00 70.85  ? 101 SO4 B O4  1 
HETATM 2180 S  S   . SO4 I 2 .  ? 13.959  -27.129 -26.404 1.00 65.41  ? 102 SO4 B S   1 
HETATM 2181 O  O1  . SO4 I 2 .  ? 15.359  -26.985 -26.128 1.00 52.53  ? 102 SO4 B O1  1 
HETATM 2182 O  O2  . SO4 I 2 .  ? 13.706  -28.430 -26.974 1.00 72.55  ? 102 SO4 B O2  1 
HETATM 2183 O  O3  . SO4 I 2 .  ? 13.226  -27.006 -25.167 1.00 65.25  ? 102 SO4 B O3  1 
HETATM 2184 O  O4  . SO4 I 2 .  ? 13.525  -26.111 -27.329 1.00 65.02  ? 102 SO4 B O4  1 
HETATM 2185 C  C4  . WJ7 J 4 .  ? 20.444  -15.042 -24.203 0.78 31.66  ? 103 WJ7 B C4  1 
HETATM 2186 C  C5  . WJ7 J 4 .  ? 21.574  -15.190 -23.414 0.78 38.36  ? 103 WJ7 B C5  1 
HETATM 2187 C  C6  . WJ7 J 4 .  ? 21.406  -15.364 -22.057 0.78 41.50  ? 103 WJ7 B C6  1 
HETATM 2188 C  C7  . WJ7 J 4 .  ? 20.180  -15.410 -21.447 0.78 35.70  ? 103 WJ7 B C7  1 
HETATM 2189 C  C8  . WJ7 J 4 .  ? 19.069  -15.261 -22.249 0.78 35.10  ? 103 WJ7 B C8  1 
HETATM 2190 N  N   . WJ7 J 4 .  ? 17.329  -15.924 -24.934 0.78 38.45  ? 103 WJ7 B N   1 
HETATM 2191 C  C   . WJ7 J 4 .  ? 16.139  -15.771 -25.757 0.78 39.62  ? 103 WJ7 B C   1 
HETATM 2192 O  O   . WJ7 J 4 .  ? 17.447  -13.735 -24.476 0.78 42.99  ? 103 WJ7 B O   1 
HETATM 2193 C  C1  . WJ7 J 4 .  ? 17.809  -17.278 -24.728 0.78 38.73  ? 103 WJ7 B C1  1 
HETATM 2194 C  C2  . WJ7 J 4 .  ? 17.935  -14.852 -24.425 0.78 37.47  ? 103 WJ7 B C2  1 
HETATM 2195 C  C3  . WJ7 J 4 .  ? 19.172  -15.063 -23.618 0.78 36.32  ? 103 WJ7 B C3  1 
HETATM 2196 F  F   . WJ7 J 4 .  ? 22.507  -15.503 -21.278 0.78 47.01  ? 103 WJ7 B F   1 
HETATM 2197 BR BR  . WJ7 J 4 .  ? 17.323  -15.291 -21.495 0.78 42.81  ? 103 WJ7 B BR  1 
HETATM 2198 C  C1  . EDO K 3 .  ? 16.483  -36.240 16.728  1.00 63.41  ? 101 EDO C C1  1 
HETATM 2199 O  O1  . EDO K 3 .  ? 15.645  -36.749 15.701  1.00 69.71  ? 101 EDO C O1  1 
HETATM 2200 C  C2  . EDO K 3 .  ? 15.809  -35.273 17.607  1.00 51.01  ? 101 EDO C C2  1 
HETATM 2201 O  O2  . EDO K 3 .  ? 15.009  -35.937 18.556  1.00 45.34  ? 101 EDO C O2  1 
HETATM 2202 S  S   . SO4 L 2 .  ? 28.821  -38.287 12.240  1.00 95.40  ? 102 SO4 C S   1 
HETATM 2203 O  O1  . SO4 L 2 .  ? 29.954  -37.428 12.010  1.00 98.58  ? 102 SO4 C O1  1 
HETATM 2204 O  O2  . SO4 L 2 .  ? 27.738  -37.904 11.373  1.00 94.07  ? 102 SO4 C O2  1 
HETATM 2205 O  O3  . SO4 L 2 .  ? 29.184  -39.649 11.966  1.00 87.85  ? 102 SO4 C O3  1 
HETATM 2206 O  O4  . SO4 L 2 .  ? 28.408  -38.170 13.612  1.00 106.06 ? 102 SO4 C O4  1 
HETATM 2207 O  O   . HOH M 5 .  ? 8.441   -32.054 3.947   1.00 60.12  ? 201 HOH A O   1 
HETATM 2208 O  O   . HOH M 5 .  ? 7.941   -9.294  8.761   1.00 58.60  ? 202 HOH A O   1 
HETATM 2209 O  O   . HOH M 5 .  ? 5.349   -28.944 7.004   1.00 59.38  ? 203 HOH A O   1 
HETATM 2210 O  O   . HOH M 5 .  ? 10.805  -9.051  -12.812 1.00 52.81  ? 204 HOH A O   1 
HETATM 2211 O  O   . HOH M 5 .  ? 3.674   -10.322 13.652  1.00 53.81  ? 205 HOH A O   1 
HETATM 2212 O  O   . HOH M 5 .  ? 7.882   -8.154  4.386   1.00 44.85  ? 206 HOH A O   1 
HETATM 2213 O  O   . HOH M 5 .  ? 15.151  -17.063 -19.086 1.00 44.00  ? 207 HOH A O   1 
HETATM 2214 O  O   . HOH M 5 .  ? 0.584   -10.862 -15.550 1.00 61.16  ? 208 HOH A O   1 
HETATM 2215 O  O   . HOH M 5 .  ? 9.578   -18.663 10.039  1.00 65.45  ? 209 HOH A O   1 
HETATM 2216 O  O   . HOH M 5 .  ? 10.607  -29.402 3.180   1.00 46.11  ? 210 HOH A O   1 
HETATM 2217 O  O   . HOH M 5 .  ? -0.971  -29.111 9.958   1.00 66.04  ? 211 HOH A O   1 
HETATM 2218 O  O   . HOH M 5 .  ? -2.614  3.219   -2.044  1.00 48.29  ? 212 HOH A O   1 
HETATM 2219 O  O   . HOH M 5 .  ? 1.644   -4.782  -10.130 1.00 44.97  ? 213 HOH A O   1 
HETATM 2220 O  O   . HOH M 5 .  ? 2.046   -24.743 -6.627  1.00 59.16  ? 214 HOH A O   1 
HETATM 2221 O  O   . HOH M 5 .  ? 0.302   -24.605 13.648  1.00 68.29  ? 215 HOH A O   1 
HETATM 2222 O  O   . HOH M 5 .  ? -0.053  -33.647 4.846   1.00 58.08  ? 216 HOH A O   1 
HETATM 2223 O  O   . HOH M 5 .  ? -8.687  -21.094 -1.120  1.00 52.13  ? 217 HOH A O   1 
HETATM 2224 O  O   . HOH M 5 .  ? 15.503  -24.372 1.855   1.00 51.73  ? 218 HOH A O   1 
HETATM 2225 O  O   . HOH M 5 .  ? -2.424  -9.614  4.307   1.00 67.97  ? 219 HOH A O   1 
HETATM 2226 O  O   . HOH M 5 .  ? 8.843   -22.728 -9.454  1.00 46.03  ? 220 HOH A O   1 
HETATM 2227 O  O   . HOH M 5 .  ? 16.727  -18.064 -9.934  1.00 43.62  ? 221 HOH A O   1 
HETATM 2228 O  O   . HOH M 5 .  ? 8.756   -18.052 -10.988 1.00 33.95  ? 222 HOH A O   1 
HETATM 2229 O  O   . HOH M 5 .  ? -4.222  -11.031 6.684   1.00 54.83  ? 223 HOH A O   1 
HETATM 2230 O  O   . HOH M 5 .  ? 17.334  -26.921 -6.572  1.00 65.17  ? 224 HOH A O   1 
HETATM 2231 O  O   . HOH M 5 .  ? 11.186  -12.047 5.941   1.00 37.83  ? 225 HOH A O   1 
HETATM 2232 O  O   . HOH M 5 .  ? 9.226   -30.354 9.547   1.00 34.56  ? 226 HOH A O   1 
HETATM 2233 O  O   . HOH M 5 .  ? 10.578  -5.217  -7.721  1.00 38.57  ? 227 HOH A O   1 
HETATM 2234 O  O   . HOH M 5 .  ? -7.032  -5.343  9.223   1.00 38.17  ? 228 HOH A O   1 
HETATM 2235 O  O   . HOH M 5 .  ? 4.556   -1.364  -6.079  1.00 40.20  ? 229 HOH A O   1 
HETATM 2236 O  O   . HOH M 5 .  ? 19.525  -15.629 7.234   1.00 34.72  ? 230 HOH A O   1 
HETATM 2237 O  O   . HOH M 5 .  ? 4.218   -3.452  -3.244  1.00 36.63  ? 231 HOH A O   1 
HETATM 2238 O  O   . HOH M 5 .  ? -4.739  -21.137 6.073   1.00 49.95  ? 232 HOH A O   1 
HETATM 2239 O  O   . HOH M 5 .  ? 4.287   -7.804  1.074   1.00 38.16  ? 233 HOH A O   1 
HETATM 2240 O  O   . HOH M 5 .  ? -6.003  -15.742 -8.070  1.00 31.18  ? 234 HOH A O   1 
HETATM 2241 O  O   . HOH M 5 .  ? 6.740   -10.591 -12.330 1.00 48.69  ? 235 HOH A O   1 
HETATM 2242 O  O   . HOH M 5 .  ? -8.072  -17.173 6.613   1.00 47.85  ? 236 HOH A O   1 
HETATM 2243 O  O   . HOH M 5 .  ? -4.827  -25.525 -5.344  1.00 56.27  ? 237 HOH A O   1 
HETATM 2244 O  O   . HOH M 5 .  ? 16.945  -12.905 1.401   1.00 24.89  ? 238 HOH A O   1 
HETATM 2245 O  O   . HOH M 5 .  ? -1.085  -20.854 6.930   1.00 38.46  ? 239 HOH A O   1 
HETATM 2246 O  O   . HOH M 5 .  ? -6.291  -12.865 6.613   1.00 51.28  ? 240 HOH A O   1 
HETATM 2247 O  O   . HOH M 5 .  ? 1.137   -18.087 -18.507 1.00 58.54  ? 241 HOH A O   1 
HETATM 2248 O  O   . HOH M 5 .  ? 2.252   -25.185 -10.089 1.00 51.95  ? 242 HOH A O   1 
HETATM 2249 O  O   . HOH M 5 .  ? 10.699  -23.612 9.871   1.00 52.16  ? 243 HOH A O   1 
HETATM 2250 O  O   . HOH M 5 .  ? -8.064  -15.744 -1.000  1.00 40.81  ? 244 HOH A O   1 
HETATM 2251 O  O   . HOH M 5 .  ? -5.991  -19.336 -5.771  1.00 46.05  ? 245 HOH A O   1 
HETATM 2252 O  O   . HOH M 5 .  ? 12.953  -11.958 -4.238  1.00 26.79  ? 246 HOH A O   1 
HETATM 2253 O  O   . HOH M 5 .  ? -2.217  -21.983 -0.582  1.00 34.32  ? 247 HOH A O   1 
HETATM 2254 O  O   . HOH M 5 .  ? 10.787  -5.909  -3.868  1.00 50.83  ? 248 HOH A O   1 
HETATM 2255 O  O   . HOH M 5 .  ? -2.782  -11.695 13.913  1.00 49.15  ? 249 HOH A O   1 
HETATM 2256 O  O   . HOH M 5 .  ? 12.670  -9.398  -7.162  1.00 48.02  ? 250 HOH A O   1 
HETATM 2257 O  O   . HOH M 5 .  ? -9.655  -15.709 10.694  1.00 61.87  ? 251 HOH A O   1 
HETATM 2258 O  O   . HOH M 5 .  ? 2.777   -29.659 -0.319  1.00 48.44  ? 252 HOH A O   1 
HETATM 2259 O  O   . HOH M 5 .  ? 4.747   -7.295  4.080   1.00 39.48  ? 253 HOH A O   1 
HETATM 2260 O  O   . HOH M 5 .  ? 9.459   -6.010  -1.654  1.00 42.84  ? 254 HOH A O   1 
HETATM 2261 O  O   . HOH M 5 .  ? 11.009  -16.461 -14.956 1.00 53.40  ? 255 HOH A O   1 
HETATM 2262 O  O   . HOH M 5 .  ? -1.463  -7.396  11.366  1.00 50.83  ? 256 HOH A O   1 
HETATM 2263 O  O   . HOH M 5 .  ? -6.396  -11.426 -11.299 1.00 47.90  ? 257 HOH A O   1 
HETATM 2264 O  O   . HOH M 5 .  ? -6.001  -13.822 -16.720 1.00 62.80  ? 258 HOH A O   1 
HETATM 2265 O  O   . HOH M 5 .  ? 1.545   -10.384 11.646  1.00 40.63  ? 259 HOH A O   1 
HETATM 2266 O  O   . HOH M 5 .  ? 8.324   -17.835 -15.809 1.00 55.30  ? 260 HOH A O   1 
HETATM 2267 O  O   . HOH M 5 .  ? -8.506  -16.542 2.144   1.00 50.40  ? 261 HOH A O   1 
HETATM 2268 O  O   . HOH M 5 .  ? 11.231  -12.328 -6.059  1.00 32.85  ? 262 HOH A O   1 
HETATM 2269 O  O   . HOH M 5 .  ? 7.461   -7.828  1.338   1.00 30.89  ? 263 HOH A O   1 
HETATM 2270 O  O   . HOH M 5 .  ? 9.691   -12.958 9.847   1.00 54.95  ? 264 HOH A O   1 
HETATM 2271 O  O   . HOH M 5 .  ? 2.816   -10.091 -13.090 1.00 61.44  ? 265 HOH A O   1 
HETATM 2272 O  O   . HOH M 5 .  ? 13.190  -28.214 -4.706  1.00 57.64  ? 266 HOH A O   1 
HETATM 2273 O  O   . HOH M 5 .  ? -1.597  -11.742 11.446  1.00 47.57  ? 267 HOH A O   1 
HETATM 2274 O  O   . HOH M 5 .  ? -0.144  -23.483 9.209   1.00 59.87  ? 268 HOH A O   1 
HETATM 2275 O  O   . HOH M 5 .  ? 2.173   -6.162  5.402   1.00 40.80  ? 269 HOH A O   1 
HETATM 2276 O  O   . HOH M 5 .  ? -5.931  -17.306 -9.898  1.00 52.98  ? 270 HOH A O   1 
HETATM 2277 O  O   . HOH M 5 .  ? 6.146   -15.906 -14.894 1.00 48.94  ? 271 HOH A O   1 
HETATM 2278 O  O   . HOH M 5 .  ? 21.869  -16.653 -0.370  1.00 45.40  ? 272 HOH A O   1 
HETATM 2279 O  O   . HOH M 5 .  ? 4.191   -34.693 4.348   1.00 67.93  ? 273 HOH A O   1 
HETATM 2280 O  O   . HOH M 5 .  ? 12.706  -15.008 -12.049 1.00 58.62  ? 274 HOH A O   1 
HETATM 2281 O  O   . HOH M 5 .  ? 12.461  -13.244 -8.557  1.00 38.83  ? 275 HOH A O   1 
HETATM 2282 O  O   . HOH M 5 .  ? 6.189   -5.902  0.554   1.00 58.35  ? 276 HOH A O   1 
HETATM 2283 O  O   . HOH M 5 .  ? 10.794  -7.860  0.424   1.00 27.59  ? 277 HOH A O   1 
HETATM 2284 O  O   . HOH M 5 .  ? 9.413   -20.387 -18.614 1.00 47.23  ? 278 HOH A O   1 
HETATM 2285 O  O   . HOH M 5 .  ? 15.436  -11.818 -5.351  1.00 36.29  ? 279 HOH A O   1 
HETATM 2286 O  O   . HOH M 5 .  ? 14.951  -28.184 -0.611  1.00 58.04  ? 280 HOH A O   1 
HETATM 2287 O  O   . HOH M 5 .  ? -7.461  -9.749  -7.605  1.00 58.62  ? 281 HOH A O   1 
HETATM 2288 O  O   . HOH M 5 .  ? 20.955  -16.540 -3.410  1.00 31.36  ? 282 HOH A O   1 
HETATM 2289 O  O   . HOH M 5 .  ? 8.592   -16.475 -13.128 1.00 42.07  ? 283 HOH A O   1 
HETATM 2290 O  O   . HOH M 5 .  ? -0.729  -21.214 10.494  1.00 118.69 ? 284 HOH A O   1 
HETATM 2291 O  O   . HOH M 5 .  ? 7.667   -17.544 8.833   1.00 57.31  ? 285 HOH A O   1 
HETATM 2292 O  O   . HOH M 5 .  ? 7.553   -8.334  13.038  1.00 56.76  ? 286 HOH A O   1 
HETATM 2293 O  O   . HOH M 5 .  ? -8.604  -19.390 -3.294  1.00 49.78  ? 287 HOH A O   1 
HETATM 2294 O  O   . HOH M 5 .  ? 8.826   -9.198  -13.790 1.00 41.12  ? 288 HOH A O   1 
HETATM 2295 O  O   . HOH M 5 .  ? 16.642  -12.532 -16.690 1.00 48.03  ? 289 HOH A O   1 
HETATM 2296 O  O   . HOH M 5 .  ? -7.495  -11.467 -8.082  1.00 35.73  ? 290 HOH A O   1 
HETATM 2297 O  O   . HOH M 5 .  ? -9.269  -20.913 -4.895  1.00 81.61  ? 291 HOH A O   1 
HETATM 2298 O  O   . HOH M 5 .  ? -4.296  -26.733 7.119   1.00 57.33  ? 292 HOH A O   1 
HETATM 2299 O  O   . HOH M 5 .  ? -6.436  -26.431 3.408   1.00 54.60  ? 293 HOH A O   1 
HETATM 2300 O  O   . HOH M 5 .  ? 16.420  -28.909 2.419   1.00 53.02  ? 294 HOH A O   1 
HETATM 2301 O  O   . HOH M 5 .  ? -4.683  -7.607  -11.113 1.00 61.79  ? 295 HOH A O   1 
HETATM 2302 O  O   . HOH M 5 .  ? -3.838  -8.198  10.497  1.00 50.17  ? 296 HOH A O   1 
HETATM 2303 O  O   . HOH M 5 .  ? -11.352 -15.894 -3.624  1.00 58.76  ? 297 HOH A O   1 
HETATM 2304 O  O   . HOH M 5 .  ? -3.850  -11.114 9.867   1.00 63.16  ? 298 HOH A O   1 
HETATM 2305 O  O   . HOH M 5 .  ? -7.278  -14.091 -9.297  1.00 64.86  ? 299 HOH A O   1 
HETATM 2306 O  O   . HOH M 5 .  ? 0.249   -27.924 -7.337  1.00 61.67  ? 300 HOH A O   1 
HETATM 2307 O  O   . HOH M 5 .  ? -7.458  -19.470 7.049   1.00 67.83  ? 301 HOH A O   1 
HETATM 2308 O  O   . HOH M 5 .  ? -10.382 -28.050 -1.883  1.00 60.88  ? 302 HOH A O   1 
HETATM 2309 O  O   . HOH M 5 .  ? 10.562  -1.942  -1.166  1.00 61.04  ? 303 HOH A O   1 
HETATM 2310 O  O   . HOH M 5 .  ? -13.773 -25.079 -4.275  1.00 77.39  ? 304 HOH A O   1 
HETATM 2311 O  O   . HOH M 5 .  ? -6.042  -23.168 -7.272  1.00 54.48  ? 305 HOH A O   1 
HETATM 2312 O  O   . HOH M 5 .  ? 6.692   -30.383 -3.044  1.00 57.82  ? 306 HOH A O   1 
HETATM 2313 O  O   . HOH M 5 .  ? -11.171 -12.999 -2.540  1.00 72.10  ? 307 HOH A O   1 
HETATM 2314 O  O   . HOH M 5 .  ? 12.167  -19.084 -11.938 1.00 57.54  ? 308 HOH A O   1 
HETATM 2315 O  O   . HOH M 5 .  ? 4.894   -6.958  -11.148 1.00 53.05  ? 309 HOH A O   1 
HETATM 2316 O  O   . HOH M 5 .  ? 4.717   -9.729  -11.285 1.00 69.43  ? 310 HOH A O   1 
HETATM 2317 O  O   . HOH M 5 .  ? 6.285   -3.156  1.203   1.00 63.68  ? 311 HOH A O   1 
HETATM 2318 O  O   . HOH M 5 .  ? -6.613  -22.948 5.329   1.00 50.99  ? 312 HOH A O   1 
HETATM 2319 O  O   . HOH M 5 .  ? -5.338  -20.814 -8.248  1.00 63.02  ? 313 HOH A O   1 
HETATM 2320 O  O   . HOH M 5 .  ? 23.511  -17.538 -2.023  1.00 68.81  ? 314 HOH A O   1 
HETATM 2321 O  O   . HOH N 5 .  ? 27.543  -8.187  -28.877 1.00 51.24  ? 201 HOH B O   1 
HETATM 2322 O  O   . HOH N 5 .  ? 31.281  -8.462  -29.733 1.00 61.56  ? 202 HOH B O   1 
HETATM 2323 O  O   . HOH N 5 .  ? 35.224  -16.078 -25.676 1.00 57.07  ? 203 HOH B O   1 
HETATM 2324 O  O   . HOH N 5 .  ? 25.889  -0.438  -28.859 1.00 48.82  ? 204 HOH B O   1 
HETATM 2325 O  O   . HOH N 5 .  ? 12.565  -25.963 -37.041 1.00 49.69  ? 205 HOH B O   1 
HETATM 2326 O  O   . HOH N 5 .  ? 19.774  -22.302 -23.031 1.00 61.40  ? 206 HOH B O   1 
HETATM 2327 O  O   . HOH N 5 .  ? 6.195   -12.414 -25.887 1.00 44.59  ? 207 HOH B O   1 
HETATM 2328 O  O   . HOH N 5 .  ? 25.882  -4.890  -33.272 1.00 46.38  ? 208 HOH B O   1 
HETATM 2329 O  O   . HOH N 5 .  ? 9.871   -16.947 -43.890 1.00 60.74  ? 209 HOH B O   1 
HETATM 2330 O  O   . HOH N 5 .  ? 12.826  -4.695  -41.444 1.00 82.76  ? 210 HOH B O   1 
HETATM 2331 O  O   . HOH N 5 .  ? 34.845  -23.141 -30.083 1.00 69.86  ? 211 HOH B O   1 
HETATM 2332 O  O   . HOH N 5 .  ? 24.869  -5.224  -29.677 1.00 40.38  ? 212 HOH B O   1 
HETATM 2333 O  O   . HOH N 5 .  ? 9.887   -11.406 -38.077 1.00 61.74  ? 213 HOH B O   1 
HETATM 2334 O  O   . HOH N 5 .  ? 1.510   -16.424 -32.456 1.00 61.17  ? 214 HOH B O   1 
HETATM 2335 O  O   . HOH N 5 .  ? 17.005  -7.515  -20.489 1.00 48.30  ? 215 HOH B O   1 
HETATM 2336 O  O   . HOH N 5 .  ? 8.348   -27.354 -38.091 1.00 70.74  ? 216 HOH B O   1 
HETATM 2337 O  O   . HOH N 5 .  ? 12.816  -22.476 -20.720 1.00 49.36  ? 217 HOH B O   1 
HETATM 2338 O  O   . HOH N 5 .  ? 27.781  -4.625  -36.742 1.00 64.69  ? 218 HOH B O   1 
HETATM 2339 O  O   . HOH N 5 .  ? 30.517  -12.591 -45.542 1.00 68.04  ? 219 HOH B O   1 
HETATM 2340 O  O   . HOH N 5 .  ? 23.611  -11.659 -21.693 1.00 48.93  ? 220 HOH B O   1 
HETATM 2341 O  O   . HOH N 5 .  ? 24.232  -1.730  -36.152 1.00 79.90  ? 221 HOH B O   1 
HETATM 2342 O  O   . HOH N 5 .  ? 20.800  -13.435 -42.417 1.00 39.42  ? 222 HOH B O   1 
HETATM 2343 O  O   . HOH N 5 .  ? 6.122   -7.428  -32.457 1.00 57.21  ? 223 HOH B O   1 
HETATM 2344 O  O   . HOH N 5 .  ? 27.454  -17.727 -24.780 1.00 43.31  ? 224 HOH B O   1 
HETATM 2345 O  O   . HOH N 5 .  ? 30.199  -19.712 -40.113 1.00 42.09  ? 225 HOH B O   1 
HETATM 2346 O  O   . HOH N 5 .  ? 18.196  -0.481  -38.102 1.00 33.51  ? 226 HOH B O   1 
HETATM 2347 O  O   . HOH N 5 .  ? 25.924  -23.140 -30.923 1.00 41.04  ? 227 HOH B O   1 
HETATM 2348 O  O   . HOH N 5 .  ? 9.748   -19.271 -43.077 1.00 61.87  ? 228 HOH B O   1 
HETATM 2349 O  O   . HOH N 5 .  ? 3.231   -8.675  -26.674 1.00 66.78  ? 229 HOH B O   1 
HETATM 2350 O  O   . HOH N 5 .  ? 23.272  -2.458  -28.781 1.00 41.89  ? 230 HOH B O   1 
HETATM 2351 O  O   . HOH N 5 .  ? 14.406  -6.047  -40.885 1.00 44.31  ? 231 HOH B O   1 
HETATM 2352 O  O   . HOH N 5 .  ? 7.382   -8.130  -20.961 1.00 45.47  ? 232 HOH B O   1 
HETATM 2353 O  O   . HOH N 5 .  ? 10.387  -18.952 -32.817 1.00 34.08  ? 233 HOH B O   1 
HETATM 2354 O  O   . HOH N 5 .  ? 19.676  -25.635 -33.850 1.00 43.94  ? 234 HOH B O   1 
HETATM 2355 O  O   . HOH N 5 .  ? 16.564  -19.260 -28.614 1.00 29.70  ? 235 HOH B O   1 
HETATM 2356 O  O   . HOH N 5 .  ? 22.473  -23.290 -28.623 1.00 50.31  ? 236 HOH B O   1 
HETATM 2357 O  O   . HOH N 5 .  ? 17.087  -9.586  -43.579 1.00 55.09  ? 237 HOH B O   1 
HETATM 2358 O  O   . HOH N 5 .  ? 8.595   -8.629  -16.425 1.00 49.24  ? 238 HOH B O   1 
HETATM 2359 O  O   . HOH N 5 .  ? 32.637  -18.505 -41.716 1.00 59.45  ? 239 HOH B O   1 
HETATM 2360 O  O   . HOH N 5 .  ? 7.444   -18.592 -31.560 1.00 51.38  ? 240 HOH B O   1 
HETATM 2361 O  O   . HOH N 5 .  ? 20.671  -10.188 -42.585 1.00 39.40  ? 241 HOH B O   1 
HETATM 2362 O  O   . HOH N 5 .  ? 25.479  -5.894  -35.463 1.00 48.40  ? 242 HOH B O   1 
HETATM 2363 O  O   . HOH N 5 .  ? 14.505  -24.408 -40.337 1.00 48.96  ? 243 HOH B O   1 
HETATM 2364 O  O   . HOH N 5 .  ? 21.213  3.627   -32.411 1.00 38.55  ? 244 HOH B O   1 
HETATM 2365 O  O   . HOH N 5 .  ? 15.462  -26.417 -34.708 1.00 49.19  ? 245 HOH B O   1 
HETATM 2366 O  O   . HOH N 5 .  ? 1.703   -12.826 -28.233 1.00 52.43  ? 246 HOH B O   1 
HETATM 2367 O  O   . HOH N 5 .  ? 31.903  -21.572 -37.786 1.00 53.99  ? 247 HOH B O   1 
HETATM 2368 O  O   . HOH N 5 .  ? 17.887  -15.752 -45.518 1.00 48.09  ? 248 HOH B O   1 
HETATM 2369 O  O   . HOH N 5 .  ? 17.887  -26.029 -28.946 1.00 40.45  ? 249 HOH B O   1 
HETATM 2370 O  O   . HOH N 5 .  ? 26.933  -10.433 -28.674 1.00 55.26  ? 250 HOH B O   1 
HETATM 2371 O  O   . HOH N 5 .  ? 23.728  -4.292  -36.593 1.00 32.24  ? 251 HOH B O   1 
HETATM 2372 O  O   . HOH N 5 .  ? 17.406  -19.728 -41.990 1.00 73.32  ? 252 HOH B O   1 
HETATM 2373 O  O   . HOH N 5 .  ? 31.208  -12.015 -38.224 1.00 68.19  ? 253 HOH B O   1 
HETATM 2374 O  O   . HOH N 5 .  ? 20.453  -3.484  -22.944 1.00 70.01  ? 254 HOH B O   1 
HETATM 2375 O  O   . HOH N 5 .  ? 21.341  -6.461  -42.348 1.00 44.98  ? 255 HOH B O   1 
HETATM 2376 O  O   . HOH N 5 .  ? 10.287  -21.698 -32.668 1.00 37.94  ? 256 HOH B O   1 
HETATM 2377 O  O   . HOH N 5 .  ? 19.864  -26.902 -30.560 1.00 55.98  ? 257 HOH B O   1 
HETATM 2378 O  O   . HOH N 5 .  ? 17.842  -3.433  -21.871 1.00 57.42  ? 258 HOH B O   1 
HETATM 2379 O  O   . HOH N 5 .  ? 24.913  -6.723  -42.194 1.00 56.43  ? 259 HOH B O   1 
HETATM 2380 O  O   . HOH N 5 .  ? 7.261   -19.287 -34.313 1.00 64.57  ? 260 HOH B O   1 
HETATM 2381 O  O   . HOH N 5 .  ? 17.990  4.779   -34.213 1.00 48.15  ? 261 HOH B O   1 
HETATM 2382 O  O   . HOH N 5 .  ? 7.599   -12.637 -38.730 1.00 70.46  ? 262 HOH B O   1 
HETATM 2383 O  O   . HOH N 5 .  ? 27.887  -24.678 -34.785 1.00 42.16  ? 263 HOH B O   1 
HETATM 2384 O  O   . HOH N 5 .  ? 24.980  -27.232 -28.068 1.00 53.75  ? 264 HOH B O   1 
HETATM 2385 O  O   . HOH N 5 .  ? 26.804  -22.556 -28.058 1.00 55.00  ? 265 HOH B O   1 
HETATM 2386 O  O   . HOH N 5 .  ? 28.418  -12.919 -24.817 1.00 56.33  ? 266 HOH B O   1 
HETATM 2387 O  O   . HOH N 5 .  ? 6.028   -20.369 -24.958 1.00 43.04  ? 267 HOH B O   1 
HETATM 2388 O  O   . HOH N 5 .  ? 15.052  -8.148  -42.812 1.00 60.40  ? 268 HOH B O   1 
HETATM 2389 O  O   . HOH N 5 .  ? 12.532  -20.272 -19.614 1.00 50.07  ? 269 HOH B O   1 
HETATM 2390 O  O   . HOH N 5 .  ? 6.868   -23.075 -24.188 1.00 51.52  ? 270 HOH B O   1 
HETATM 2391 O  O   . HOH N 5 .  ? 27.735  -24.791 -32.093 1.00 47.67  ? 271 HOH B O   1 
HETATM 2392 O  O   . HOH N 5 .  ? 28.789  -17.276 -46.978 1.00 58.31  ? 272 HOH B O   1 
HETATM 2393 O  O   . HOH N 5 .  ? 24.123  -4.441  -27.846 1.00 59.04  ? 273 HOH B O   1 
HETATM 2394 O  O   . HOH N 5 .  ? 9.576   -6.372  -40.950 1.00 47.49  ? 274 HOH B O   1 
HETATM 2395 O  O   . HOH N 5 .  ? 16.460  -0.470  -25.211 1.00 56.65  ? 275 HOH B O   1 
HETATM 2396 O  O   . HOH N 5 .  ? 19.689  4.030   -33.149 1.00 47.88  ? 276 HOH B O   1 
HETATM 2397 O  O   . HOH N 5 .  ? 14.736  -27.281 -21.488 1.00 76.71  ? 277 HOH B O   1 
HETATM 2398 O  O   . HOH N 5 .  ? 39.356  -13.039 -38.479 1.00 72.94  ? 278 HOH B O   1 
HETATM 2399 O  O   . HOH N 5 .  ? 14.755  -21.878 -41.659 1.00 56.83  ? 279 HOH B O   1 
HETATM 2400 O  O   . HOH N 5 .  ? 8.688   -6.005  -17.013 1.00 54.08  ? 280 HOH B O   1 
HETATM 2401 O  O   . HOH N 5 .  ? 28.201  -15.156 -23.022 1.00 58.60  ? 281 HOH B O   1 
HETATM 2402 O  O   . HOH N 5 .  ? 7.198   -21.558 -29.797 1.00 49.59  ? 282 HOH B O   1 
HETATM 2403 O  O   . HOH N 5 .  ? 19.371  -8.934  -43.511 1.00 50.88  ? 283 HOH B O   1 
HETATM 2404 O  O   . HOH N 5 .  ? 7.155   -9.675  -18.571 1.00 53.52  ? 284 HOH B O   1 
HETATM 2405 O  O   . HOH N 5 .  ? 8.868   -22.495 -19.269 1.00 61.32  ? 285 HOH B O   1 
HETATM 2406 O  O   . HOH N 5 .  ? 17.217  4.722   -26.368 1.00 69.04  ? 286 HOH B O   1 
HETATM 2407 O  O   . HOH O 5 .  ? 12.643  -27.610 28.346  1.00 57.03  ? 201 HOH C O   1 
HETATM 2408 O  O   . HOH O 5 .  ? 5.292   -26.645 16.551  1.00 54.12  ? 202 HOH C O   1 
HETATM 2409 O  O   . HOH O 5 .  ? 22.596  -41.207 18.287  1.00 51.40  ? 203 HOH C O   1 
HETATM 2410 O  O   . HOH O 5 .  ? 25.848  -37.142 10.140  1.00 60.42  ? 204 HOH C O   1 
HETATM 2411 O  O   . HOH O 5 .  ? 8.890   -30.015 11.308  1.00 48.85  ? 205 HOH C O   1 
HETATM 2412 O  O   . HOH O 5 .  ? 8.077   -19.241 23.463  1.00 54.80  ? 206 HOH C O   1 
HETATM 2413 O  O   . HOH O 5 .  ? 25.997  -38.982 12.697  1.00 44.54  ? 207 HOH C O   1 
HETATM 2414 O  O   . HOH O 5 .  ? 8.408   -36.494 18.403  1.00 64.23  ? 208 HOH C O   1 
HETATM 2415 O  O   . HOH O 5 .  ? 19.546  -41.618 12.223  1.00 40.67  ? 209 HOH C O   1 
HETATM 2416 O  O   . HOH O 5 .  ? 19.834  -20.823 30.521  1.00 70.66  ? 210 HOH C O   1 
HETATM 2417 O  O   . HOH O 5 .  ? 7.118   -31.553 12.237  1.00 53.63  ? 211 HOH C O   1 
HETATM 2418 O  O   . HOH O 5 .  ? 12.497  -31.348 8.165   1.00 43.86  ? 212 HOH C O   1 
HETATM 2419 O  O   . HOH O 5 .  ? 21.784  -28.338 11.042  1.00 36.72  ? 213 HOH C O   1 
HETATM 2420 O  O   . HOH O 5 .  ? 14.437  -20.866 12.031  1.00 49.60  ? 214 HOH C O   1 
HETATM 2421 O  O   . HOH O 5 .  ? 27.874  -37.068 15.847  1.00 47.83  ? 215 HOH C O   1 
HETATM 2422 O  O   . HOH O 5 .  ? 15.774  -38.034 19.903  1.00 55.52  ? 216 HOH C O   1 
HETATM 2423 O  O   . HOH O 5 .  ? 22.345  -21.675 7.429   1.00 51.83  ? 217 HOH C O   1 
HETATM 2424 O  O   . HOH O 5 .  ? 13.909  -39.047 17.037  1.00 50.50  ? 218 HOH C O   1 
HETATM 2425 O  O   . HOH O 5 .  ? 29.789  -31.687 15.481  1.00 65.62  ? 219 HOH C O   1 
HETATM 2426 O  O   . HOH O 5 .  ? 24.889  -31.178 10.817  1.00 41.04  ? 220 HOH C O   1 
HETATM 2427 O  O   . HOH O 5 .  ? 17.362  -16.912 14.626  1.00 52.77  ? 221 HOH C O   1 
HETATM 2428 O  O   . HOH O 5 .  ? 16.745  -32.530 3.189   1.00 78.80  ? 222 HOH C O   1 
HETATM 2429 O  O   . HOH O 5 .  ? 13.548  -37.181 13.536  1.00 52.43  ? 223 HOH C O   1 
HETATM 2430 O  O   . HOH O 5 .  ? 21.572  -34.225 16.579  1.00 31.17  ? 224 HOH C O   1 
HETATM 2431 O  O   . HOH O 5 .  ? 25.240  -33.986 34.633  1.00 66.47  ? 225 HOH C O   1 
HETATM 2432 O  O   . HOH O 5 .  ? 15.610  -17.553 19.183  1.00 47.78  ? 226 HOH C O   1 
HETATM 2433 O  O   . HOH O 5 .  ? 18.984  -26.773 3.301   1.00 50.65  ? 227 HOH C O   1 
HETATM 2434 O  O   . HOH O 5 .  ? 6.515   -17.926 10.938  1.00 45.21  ? 228 HOH C O   1 
HETATM 2435 O  O   . HOH O 5 .  ? 13.794  -37.248 5.988   1.00 73.61  ? 229 HOH C O   1 
HETATM 2436 O  O   . HOH O 5 .  ? 30.052  -29.118 12.109  1.00 59.75  ? 230 HOH C O   1 
HETATM 2437 O  O   . HOH O 5 .  ? 20.377  -28.672 8.545   1.00 43.43  ? 231 HOH C O   1 
HETATM 2438 O  O   . HOH O 5 .  ? 30.918  -39.649 27.009  1.00 45.02  ? 232 HOH C O   1 
HETATM 2439 O  O   . HOH O 5 .  ? 30.785  -43.018 15.749  1.00 62.45  ? 233 HOH C O   1 
HETATM 2440 O  O   . HOH O 5 .  ? 16.334  -33.507 28.502  1.00 58.26  ? 234 HOH C O   1 
HETATM 2441 O  O   . HOH O 5 .  ? 25.063  -39.545 20.186  1.00 40.23  ? 235 HOH C O   1 
HETATM 2442 O  O   . HOH O 5 .  ? 9.814   -18.401 23.949  1.00 59.27  ? 236 HOH C O   1 
HETATM 2443 O  O   . HOH O 5 .  ? 31.733  -33.403 25.754  1.00 49.73  ? 237 HOH C O   1 
HETATM 2444 O  O   . HOH O 5 .  ? 29.467  -39.640 31.331  1.00 43.53  ? 238 HOH C O   1 
HETATM 2445 O  O   . HOH O 5 .  ? 20.510  -39.688 26.243  1.00 48.27  ? 239 HOH C O   1 
HETATM 2446 O  O   . HOH O 5 .  ? 20.565  -29.296 4.551   1.00 56.21  ? 240 HOH C O   1 
HETATM 2447 O  O   . HOH O 5 .  ? 13.881  -29.460 4.242   1.00 59.29  ? 241 HOH C O   1 
HETATM 2448 O  O   . HOH O 5 .  ? 27.237  -24.225 32.870  1.00 79.83  ? 242 HOH C O   1 
HETATM 2449 O  O   . HOH O 5 .  ? 27.117  -37.662 24.820  1.00 54.70  ? 243 HOH C O   1 
HETATM 2450 O  O   . HOH O 5 .  ? 25.449  -17.899 21.005  1.00 56.38  ? 244 HOH C O   1 
HETATM 2451 O  O   . HOH O 5 .  ? 28.358  -35.649 9.510   1.00 60.58  ? 245 HOH C O   1 
HETATM 2452 O  O   . HOH O 5 .  ? 1.770   -29.782 27.253  1.00 63.27  ? 246 HOH C O   1 
HETATM 2453 O  O   . HOH O 5 .  ? 25.554  -17.741 13.681  1.00 55.25  ? 247 HOH C O   1 
HETATM 2454 O  O   . HOH O 5 .  ? 18.734  -19.714 10.645  1.00 47.77  ? 248 HOH C O   1 
HETATM 2455 O  O   . HOH O 5 .  ? 22.143  -18.344 21.773  1.00 56.42  ? 249 HOH C O   1 
HETATM 2456 O  O   . HOH O 5 .  ? 19.541  -18.860 25.063  1.00 62.63  ? 250 HOH C O   1 
HETATM 2457 O  O   . HOH O 5 .  ? 4.937   -23.828 18.682  1.00 56.68  ? 251 HOH C O   1 
HETATM 2458 O  O   . HOH O 5 .  ? 13.695  -38.793 9.628   1.00 68.34  ? 252 HOH C O   1 
HETATM 2459 O  O   . HOH O 5 .  ? 27.139  -15.192 12.764  1.00 53.17  ? 253 HOH C O   1 
HETATM 2460 O  O   . HOH O 5 .  ? 30.126  -25.104 32.203  1.00 71.74  ? 254 HOH C O   1 
HETATM 2461 O  O   . HOH O 5 .  ? 16.553  -36.742 21.180  1.00 43.18  ? 255 HOH C O   1 
HETATM 2462 O  O   . HOH O 5 .  ? 19.976  -13.090 13.324  1.00 46.94  ? 256 HOH C O   1 
HETATM 2463 O  O   . HOH O 5 .  ? 2.233   -29.147 13.783  1.00 75.51  ? 257 HOH C O   1 
HETATM 2464 O  O   . HOH O 5 .  ? 30.677  -35.478 28.442  1.00 51.80  ? 258 HOH C O   1 
HETATM 2465 O  O   . HOH O 5 .  ? 29.256  -32.759 18.101  1.00 69.43  ? 259 HOH C O   1 
HETATM 2466 O  O   . HOH O 5 .  ? 16.138  -37.995 28.946  1.00 65.89  ? 260 HOH C O   1 
HETATM 2467 O  O   . HOH O 5 .  ? 13.961  -22.102 28.420  1.00 70.89  ? 261 HOH C O   1 
HETATM 2468 O  O   . HOH O 5 .  ? 28.660  -41.391 27.107  1.00 46.44  ? 262 HOH C O   1 
HETATM 2469 O  O   . HOH O 5 .  ? 33.803  -35.934 31.660  1.00 61.22  ? 263 HOH C O   1 
HETATM 2470 O  O   . HOH O 5 .  ? 11.569  -20.963 10.727  1.00 47.70  ? 264 HOH C O   1 
HETATM 2471 O  O   . HOH O 5 .  ? 21.982  -13.520 13.116  1.00 63.15  ? 265 HOH C O   1 
HETATM 2472 O  O   . HOH O 5 .  ? 31.535  -39.057 29.819  1.00 65.81  ? 266 HOH C O   1 
HETATM 2473 O  O   . HOH O 5 .  ? 33.116  -44.317 15.186  1.00 46.01  ? 267 HOH C O   1 
HETATM 2474 O  O   . HOH O 5 .  ? 20.056  -40.955 38.954  1.00 78.60  ? 268 HOH C O   1 
# 
