data_7HH5
# 
_entry.id   7HH5 
# 
_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   7HH5         pdb_00007hh5 10.2210/pdb7hh5/pdb 
WWPDB D_1001407467 ?            ?                   
# 
_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                        7HH5 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '1-(1,4-diazepan-1-yl)ethan-1-one'                 142.199   2   ? ?    ? ? 
5 water       nat water                                              18.015    232 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                      SO4 
3 1,2-ETHANEDIOL                     EDO 
4 '1-(1,4-diazepan-1-yl)ethan-1-one' WO7 
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 
WO7 non-polymer         . '1-(1,4-diazepan-1-yl)ethan-1-one' ?                 'C7 H14 N2 O'    142.199 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 ?  ?   ?   B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 30 ASP ASP C . n 
C 1 32 GLY 32 31 31 GLY GLY C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        WO7 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   WO7 
_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 4 WO7 1   104 101 WO7 LIG A . 
H 2 SO4 1   105 4   SO4 SO4 A . 
I 3 EDO 1   101 101 EDO EDO B . 
J 2 SO4 1   102 1   SO4 SO4 B . 
K 2 SO4 1   103 3   SO4 SO4 B . 
L 2 SO4 1   101 5   SO4 SO4 C . 
M 4 WO7 1   102 101 WO7 LIG C . 
N 5 HOH 1   201 307 HOH HOH A . 
N 5 HOH 2   202 202 HOH HOH A . 
N 5 HOH 3   203 84  HOH HOH A . 
N 5 HOH 4   204 287 HOH HOH A . 
N 5 HOH 5   205 91  HOH HOH A . 
N 5 HOH 6   206 66  HOH HOH A . 
N 5 HOH 7   207 71  HOH HOH A . 
N 5 HOH 8   208 165 HOH HOH A . 
N 5 HOH 9   209 139 HOH HOH A . 
N 5 HOH 10  210 26  HOH HOH A . 
N 5 HOH 11  211 199 HOH HOH A . 
N 5 HOH 12  212 55  HOH HOH A . 
N 5 HOH 13  213 94  HOH HOH A . 
N 5 HOH 14  214 260 HOH HOH A . 
N 5 HOH 15  215 289 HOH HOH A . 
N 5 HOH 16  216 188 HOH HOH A . 
N 5 HOH 17  217 87  HOH HOH A . 
N 5 HOH 18  218 86  HOH HOH A . 
N 5 HOH 19  219 95  HOH HOH A . 
N 5 HOH 20  220 293 HOH HOH A . 
N 5 HOH 21  221 190 HOH HOH A . 
N 5 HOH 22  222 304 HOH HOH A . 
N 5 HOH 23  223 290 HOH HOH A . 
N 5 HOH 24  224 28  HOH HOH A . 
N 5 HOH 25  225 142 HOH HOH A . 
N 5 HOH 26  226 32  HOH HOH A . 
N 5 HOH 27  227 99  HOH HOH A . 
N 5 HOH 28  228 37  HOH HOH A . 
N 5 HOH 29  229 8   HOH HOH A . 
N 5 HOH 30  230 60  HOH HOH A . 
N 5 HOH 31  231 85  HOH HOH A . 
N 5 HOH 32  232 97  HOH HOH A . 
N 5 HOH 33  233 296 HOH HOH A . 
N 5 HOH 34  234 179 HOH HOH A . 
N 5 HOH 35  235 167 HOH HOH A . 
N 5 HOH 36  236 203 HOH HOH A . 
N 5 HOH 37  237 93  HOH HOH A . 
N 5 HOH 38  238 34  HOH HOH A . 
N 5 HOH 39  239 301 HOH HOH A . 
N 5 HOH 40  240 288 HOH HOH A . 
N 5 HOH 41  241 38  HOH HOH A . 
N 5 HOH 42  242 41  HOH HOH A . 
N 5 HOH 43  243 259 HOH HOH A . 
N 5 HOH 44  244 7   HOH HOH A . 
N 5 HOH 45  245 23  HOH HOH A . 
N 5 HOH 46  246 297 HOH HOH A . 
N 5 HOH 47  247 267 HOH HOH A . 
N 5 HOH 48  248 2   HOH HOH A . 
N 5 HOH 49  249 1   HOH HOH A . 
N 5 HOH 50  250 12  HOH HOH A . 
N 5 HOH 51  251 274 HOH HOH A . 
N 5 HOH 52  252 27  HOH HOH A . 
N 5 HOH 53  253 292 HOH HOH A . 
N 5 HOH 54  254 111 HOH HOH A . 
N 5 HOH 55  255 20  HOH HOH A . 
N 5 HOH 56  256 109 HOH HOH A . 
N 5 HOH 57  257 78  HOH HOH A . 
N 5 HOH 58  258 18  HOH HOH A . 
N 5 HOH 59  259 145 HOH HOH A . 
N 5 HOH 60  260 21  HOH HOH A . 
N 5 HOH 61  261 47  HOH HOH A . 
N 5 HOH 62  262 77  HOH HOH A . 
N 5 HOH 63  263 211 HOH HOH A . 
N 5 HOH 64  264 31  HOH HOH A . 
N 5 HOH 65  265 218 HOH HOH A . 
N 5 HOH 66  266 116 HOH HOH A . 
N 5 HOH 67  267 14  HOH HOH A . 
N 5 HOH 68  268 300 HOH HOH A . 
N 5 HOH 69  269 58  HOH HOH A . 
N 5 HOH 70  270 164 HOH HOH A . 
N 5 HOH 71  271 222 HOH HOH A . 
N 5 HOH 72  272 19  HOH HOH A . 
N 5 HOH 73  273 42  HOH HOH A . 
N 5 HOH 74  274 115 HOH HOH A . 
N 5 HOH 75  275 143 HOH HOH A . 
N 5 HOH 76  276 152 HOH HOH A . 
N 5 HOH 77  277 9   HOH HOH A . 
N 5 HOH 78  278 318 HOH HOH A . 
N 5 HOH 79  279 16  HOH HOH A . 
N 5 HOH 80  280 281 HOH HOH A . 
N 5 HOH 81  281 64  HOH HOH A . 
N 5 HOH 82  282 208 HOH HOH A . 
N 5 HOH 83  283 73  HOH HOH A . 
N 5 HOH 84  284 113 HOH HOH A . 
N 5 HOH 85  285 131 HOH HOH A . 
N 5 HOH 86  286 22  HOH HOH A . 
N 5 HOH 87  287 210 HOH HOH A . 
N 5 HOH 88  288 327 HOH HOH A . 
N 5 HOH 89  289 83  HOH HOH A . 
N 5 HOH 90  290 63  HOH HOH A . 
N 5 HOH 91  291 108 HOH HOH A . 
N 5 HOH 92  292 185 HOH HOH A . 
N 5 HOH 93  293 219 HOH HOH A . 
N 5 HOH 94  294 205 HOH HOH A . 
N 5 HOH 95  295 283 HOH HOH A . 
N 5 HOH 96  296 57  HOH HOH A . 
N 5 HOH 97  297 35  HOH HOH A . 
N 5 HOH 98  298 75  HOH HOH A . 
N 5 HOH 99  299 156 HOH HOH A . 
N 5 HOH 100 300 125 HOH HOH A . 
N 5 HOH 101 301 313 HOH HOH A . 
N 5 HOH 102 302 332 HOH HOH A . 
O 5 HOH 1   201 272 HOH HOH B . 
O 5 HOH 2   202 331 HOH HOH B . 
O 5 HOH 3   203 258 HOH HOH B . 
O 5 HOH 4   204 89  HOH HOH B . 
O 5 HOH 5   205 123 HOH HOH B . 
O 5 HOH 6   206 184 HOH HOH B . 
O 5 HOH 7   207 329 HOH HOH B . 
O 5 HOH 8   208 98  HOH HOH B . 
O 5 HOH 9   209 153 HOH HOH B . 
O 5 HOH 10  210 247 HOH HOH B . 
O 5 HOH 11  211 242 HOH HOH B . 
O 5 HOH 12  212 69  HOH HOH B . 
O 5 HOH 13  213 137 HOH HOH B . 
O 5 HOH 14  214 172 HOH HOH B . 
O 5 HOH 15  215 54  HOH HOH B . 
O 5 HOH 16  216 249 HOH HOH B . 
O 5 HOH 17  217 320 HOH HOH B . 
O 5 HOH 18  218 6   HOH HOH B . 
O 5 HOH 19  219 215 HOH HOH B . 
O 5 HOH 20  220 117 HOH HOH B . 
O 5 HOH 21  221 150 HOH HOH B . 
O 5 HOH 22  222 17  HOH HOH B . 
O 5 HOH 23  223 280 HOH HOH B . 
O 5 HOH 24  224 5   HOH HOH B . 
O 5 HOH 25  225 119 HOH HOH B . 
O 5 HOH 26  226 10  HOH HOH B . 
O 5 HOH 27  227 157 HOH HOH B . 
O 5 HOH 28  228 96  HOH HOH B . 
O 5 HOH 29  229 169 HOH HOH B . 
O 5 HOH 30  230 168 HOH HOH B . 
O 5 HOH 31  231 79  HOH HOH B . 
O 5 HOH 32  232 261 HOH HOH B . 
O 5 HOH 33  233 61  HOH HOH B . 
O 5 HOH 34  234 24  HOH HOH B . 
O 5 HOH 35  235 217 HOH HOH B . 
O 5 HOH 36  236 101 HOH HOH B . 
O 5 HOH 37  237 315 HOH HOH B . 
O 5 HOH 38  238 120 HOH HOH B . 
O 5 HOH 39  239 25  HOH HOH B . 
O 5 HOH 40  240 175 HOH HOH B . 
O 5 HOH 41  241 68  HOH HOH B . 
O 5 HOH 42  242 59  HOH HOH B . 
O 5 HOH 43  243 36  HOH HOH B . 
O 5 HOH 44  244 279 HOH HOH B . 
O 5 HOH 45  245 197 HOH HOH B . 
O 5 HOH 46  246 223 HOH HOH B . 
O 5 HOH 47  247 76  HOH HOH B . 
O 5 HOH 48  248 74  HOH HOH B . 
O 5 HOH 49  249 13  HOH HOH B . 
O 5 HOH 50  250 104 HOH HOH B . 
O 5 HOH 51  251 72  HOH HOH B . 
O 5 HOH 52  252 214 HOH HOH B . 
O 5 HOH 53  253 46  HOH HOH B . 
O 5 HOH 54  254 182 HOH HOH B . 
O 5 HOH 55  255 303 HOH HOH B . 
O 5 HOH 56  256 224 HOH HOH B . 
O 5 HOH 57  257 44  HOH HOH B . 
O 5 HOH 58  258 319 HOH HOH B . 
O 5 HOH 59  259 316 HOH HOH B . 
O 5 HOH 60  260 177 HOH HOH B . 
O 5 HOH 61  261 322 HOH HOH B . 
O 5 HOH 62  262 170 HOH HOH B . 
O 5 HOH 63  263 163 HOH HOH B . 
O 5 HOH 64  264 291 HOH HOH B . 
O 5 HOH 65  265 160 HOH HOH B . 
O 5 HOH 66  266 201 HOH HOH B . 
O 5 HOH 67  267 314 HOH HOH B . 
O 5 HOH 68  268 107 HOH HOH B . 
O 5 HOH 69  269 312 HOH HOH B . 
P 5 HOH 1   201 323 HOH HOH C . 
P 5 HOH 2   202 317 HOH HOH C . 
P 5 HOH 3   203 173 HOH HOH C . 
P 5 HOH 4   204 309 HOH HOH C . 
P 5 HOH 5   205 226 HOH HOH C . 
P 5 HOH 6   206 161 HOH HOH C . 
P 5 HOH 7   207 271 HOH HOH C . 
P 5 HOH 8   208 134 HOH HOH C . 
P 5 HOH 9   209 321 HOH HOH C . 
P 5 HOH 10  210 254 HOH HOH C . 
P 5 HOH 11  211 269 HOH HOH C . 
P 5 HOH 12  212 284 HOH HOH C . 
P 5 HOH 13  213 151 HOH HOH C . 
P 5 HOH 14  214 15  HOH HOH C . 
P 5 HOH 15  215 333 HOH HOH C . 
P 5 HOH 16  216 118 HOH HOH C . 
P 5 HOH 17  217 49  HOH HOH C . 
P 5 HOH 18  218 90  HOH HOH C . 
P 5 HOH 19  219 53  HOH HOH C . 
P 5 HOH 20  220 126 HOH HOH C . 
P 5 HOH 21  221 45  HOH HOH C . 
P 5 HOH 22  222 56  HOH HOH C . 
P 5 HOH 23  223 335 HOH HOH C . 
P 5 HOH 24  224 302 HOH HOH C . 
P 5 HOH 25  225 275 HOH HOH C . 
P 5 HOH 26  226 122 HOH HOH C . 
P 5 HOH 27  227 102 HOH HOH C . 
P 5 HOH 28  228 4   HOH HOH C . 
P 5 HOH 29  229 40  HOH HOH C . 
P 5 HOH 30  230 43  HOH HOH C . 
P 5 HOH 31  231 294 HOH HOH C . 
P 5 HOH 32  232 82  HOH HOH C . 
P 5 HOH 33  233 148 HOH HOH C . 
P 5 HOH 34  234 67  HOH HOH C . 
P 5 HOH 35  235 48  HOH HOH C . 
P 5 HOH 36  236 298 HOH HOH C . 
P 5 HOH 37  237 299 HOH HOH C . 
P 5 HOH 38  238 328 HOH HOH C . 
P 5 HOH 39  239 171 HOH HOH C . 
P 5 HOH 40  240 135 HOH HOH C . 
P 5 HOH 41  241 130 HOH HOH C . 
P 5 HOH 42  242 198 HOH HOH C . 
P 5 HOH 43  243 149 HOH HOH C . 
P 5 HOH 44  244 62  HOH HOH C . 
P 5 HOH 45  245 132 HOH HOH C . 
P 5 HOH 46  246 295 HOH HOH C . 
P 5 HOH 47  247 209 HOH HOH C . 
P 5 HOH 48  248 65  HOH HOH C . 
P 5 HOH 49  249 334 HOH HOH C . 
P 5 HOH 50  250 324 HOH HOH C . 
P 5 HOH 51  251 330 HOH HOH C . 
P 5 HOH 52  252 305 HOH HOH C . 
P 5 HOH 53  253 146 HOH HOH C . 
P 5 HOH 54  254 70  HOH HOH C . 
P 5 HOH 55  255 270 HOH HOH C . 
P 5 HOH 56  256 241 HOH HOH C . 
P 5 HOH 57  257 246 HOH HOH C . 
P 5 HOH 58  258 103 HOH HOH C . 
P 5 HOH 59  259 92  HOH HOH C . 
P 5 HOH 60  260 310 HOH HOH C . 
P 5 HOH 61  261 206 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
19 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
20 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
21 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
22 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
23 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
24 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
25 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
26 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
27 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
28 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
29 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
30 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
31 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
32 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
33 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
34 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
35 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
36 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
37 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
38 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
39 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
40 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
41 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
42 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
43 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
44 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
45 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
46 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
47 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
48 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
49 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
50 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
51 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
52 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
53 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
54 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HH5 
_cell.length_a           41.667 
_cell.length_b           42.113 
_cell.length_c           159.183 
_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                         7HH5 
_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          7HH5 
_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                     7HH5 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.59 
_reflns.d_resolution_high            1.66 
_reflns.number_obs                   33976 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.105 
_reflns.pdbx_netI_over_sigmaI        8.0 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.115 
_reflns.pdbx_Rpim_I_all              0.045 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     217555 
_reflns.pdbx_chi_squared             0.88 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.66 
_reflns_shell.d_res_low                   1.75 
_reflns_shell.number_measured_all         30312 
_reflns_shell.number_unique_obs           4875 
_reflns_shell.Rmerge_I_obs                1.694 
_reflns_shell.pdbx_chi_squared            0.69 
_reflns_shell.pdbx_redundancy             6.2 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.849 
_reflns_shell.pdbx_Rpim_I_all             0.733 
_reflns_shell.pdbx_CC_half                0.425 
_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                                 7HH5 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     32055 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             79.59 
_refine.ls_d_res_high                            1.66 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_R_factor_obs                          0.20687 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20435 
_refine.ls_R_factor_R_free                       0.25195 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  1791 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.B_iso_mean                               39.959 
_refine.aniso_B[1][1]                            0.49 
_refine.aniso_B[2][2]                            -0.19 
_refine.aniso_B[3][3]                            -0.30 
_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                       0.115 
_refine.pdbx_overall_ESU_R_Free                  0.118 
_refine.overall_SU_ML                            0.102 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.208 
_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        2141 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             232 
_refine_hist.number_atoms_total               2431 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        79.59 
# 
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             0.008  0.012  ? 2301 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.722  1.835  ? 3128 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.145  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.050  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.745 10.000 ? 299  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 287  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1888 '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                  3.475  3.767  ? 1076 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.693  6.733  ? 1344 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.595  4.088  ? 1225 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.928  56.72  ? 3550 '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                       1.663 
_refine_ls_shell.d_res_low                        1.706 
_refine_ls_shell.number_reflns_R_work             2244 
_refine_ls_shell.R_factor_R_work                  0.347 
_refine_ls_shell.percent_reflns_obs               97.62 
_refine_ls_shell.R_factor_R_free                  0.336 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             138 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH5 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z168883358' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH5 
_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 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P 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 7HH5 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH5 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH5 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 7HH5 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH5 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH5 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH5 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH5 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH5 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O LEU B 54 ? O LEU B 53 N TYR B 41 ? N TYR B 40 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HH5 
_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 223 ? ? O B HOH 261 ? ? 1.56 
2 1 O  C HOH 250 ? ? O C HOH 253 ? ? 1.95 
3 1 O2 A SO4 105 ? ? O A HOH 201 ? ? 2.05 
4 1 O  B HOH 214 ? ? O B HOH 234 ? ? 2.11 
5 1 O  B HOH 255 ? ? O B HOH 261 ? ? 2.14 
# 
_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    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     216 
_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    B 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     267 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_654 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -151.46 65.35  
2 1 HIS B 20 ? ? -39.94  126.01 
3 1 ASN B 87 ? ? -161.14 59.77  
4 1 ASN C 87 ? ? -154.69 52.84  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.76 
# 
_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            0.086 
_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 ILE 28 ? B ILE 29 
4  1 Y 1 B ALA 29 ? B ALA 30 
5  1 Y 1 B ASP 30 ? B ASP 31 
6  1 Y 1 B GLY 31 ? B GLY 32 
7  1 Y 1 B ALA 32 ? B ALA 33 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ASP 27 ? C ASP 28 
12 1 Y 1 C ILE 28 ? C ILE 29 
13 1 Y 1 C ALA 29 ? C ALA 30 
14 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 
WO7 C10  C N N 406 
WO7 C01  C N N 407 
WO7 C02  C N N 408 
WO7 C05  C N N 409 
WO7 C06  C N N 410 
WO7 C07  C N N 411 
WO7 C09  C N N 412 
WO7 N04  N N N 413 
WO7 N08  N N N 414 
WO7 O03  O N N 415 
WO7 H1   H N N 416 
WO7 H2   H N N 417 
WO7 H3   H N N 418 
WO7 H4   H N N 419 
WO7 H5   H N N 420 
WO7 H6   H N N 421 
WO7 H7   H N N 422 
WO7 H8   H N N 423 
WO7 H9   H N N 424 
WO7 H10  H N N 425 
WO7 H11  H N N 426 
WO7 H12  H N N 427 
WO7 H13  H N N 428 
WO7 H14  H N N 429 
# 
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 
WO7 C10 C09  sing N N 389 
WO7 C10 N04  sing N N 390 
WO7 C09 N08  sing N N 391 
WO7 C01 C02  sing N N 392 
WO7 N08 C07  sing N N 393 
WO7 N04 C02  sing N N 394 
WO7 N04 C05  sing N N 395 
WO7 C02 O03  doub N N 396 
WO7 C07 C06  sing N N 397 
WO7 C06 C05  sing N N 398 
WO7 C10 H1   sing N N 399 
WO7 C10 H2   sing N N 400 
WO7 C01 H3   sing N N 401 
WO7 C01 H4   sing N N 402 
WO7 C01 H5   sing N N 403 
WO7 C05 H6   sing N N 404 
WO7 C05 H7   sing N N 405 
WO7 C06 H8   sing N N 406 
WO7 C06 H9   sing N N 407 
WO7 C07 H10  sing N N 408 
WO7 C07 H11  sing N N 409 
WO7 C09 H12  sing N N 410 
WO7 C09 H13  sing N N 411 
WO7 N08 H14  sing N N 412 
# 
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                    7HH5 
_atom_sites.fract_transf_matrix[1][1]   0.024000 
_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]   0.023746 
_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]   0.006282 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 0.577   4.415   2.303   1.00 57.24  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.459  3.586   1.636   1.00 59.87  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.185   2.493   0.779   1.00 55.25  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.322   2.622   0.332   1.00 50.89  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.433  4.453   0.832   1.00 66.65  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.443  5.201   1.692   1.00 78.83  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.710  4.221   2.532   1.00 72.15  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.389  5.391   3.719   1.00 76.49  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.497  1.339   0.597   1.00 47.68  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.017  0.259   -0.278  1.00 43.33  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.211   0.643   -1.742  1.00 41.06  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.526  1.449   -2.312  1.00 45.49  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.217  -0.748  -0.149  1.00 46.08  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.680  -0.526  1.277   1.00 49.38  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.740  0.985   1.307   1.00 48.96  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.196   -0.009  -2.359  1.00 39.66  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.418   0.090   -3.783  1.00 39.00  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.882   -1.208  -4.378  1.00 38.90  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.368   -2.064  -3.650  1.00 38.06  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.928   0.207   -4.045  1.00 46.45  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.561   1.500   -3.620  1.00 62.55  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.646   1.922   -2.310  1.00 66.65  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.141   2.469   -4.348  1.00 68.79  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.249   3.102   -2.260  1.00 63.99  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.563   3.449   -3.484  1.00 62.74  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.001   -1.359  -5.695  1.00 32.08  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.740   -2.651  -6.308  1.00 31.22  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.864   -3.623  -5.943  1.00 29.41  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.952   -3.197  -5.532  1.00 30.78  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.616   -2.492  -7.804  1.00 37.94  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.582   -4.915  -6.080  1.00 31.45  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.609   -5.929  -5.879  1.00 30.58  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.746   -5.731  -6.885  1.00 32.50  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.527   -5.389  -8.048  1.00 31.78  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.082   -7.363  -5.966  1.00 28.13  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.298   -7.732  -4.711  1.00 30.04  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.956   -7.944  -3.493  1.00 28.88  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.096  -7.902  -4.772  1.00 26.30  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.258   -8.276  -2.341  1.00 30.09  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.786  -8.294  -3.610  1.00 25.69  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.128  -8.452  -2.415  1.00 27.97  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.971   -6.005  -6.420  1.00 26.82  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.119   -5.965  -7.312  1.00 28.49  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.003   -7.174  -7.007  1.00 25.03  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.968   -7.755  -5.928  1.00 23.47  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.888   -4.654  -7.084  1.00 30.58  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.483   -4.550  -5.696  1.00 32.77  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.147   -3.201  -5.394  1.00 39.38  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.788   -3.196  -4.037  1.00 38.67  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.823   -3.255  -2.937  1.00 34.55  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.888   -7.551  -7.938  1.00 26.08  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.807   -8.660  -7.686  1.00 26.17  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.623   -8.394  -6.417  1.00 24.96  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.078  -7.269  -6.175  1.00 27.14  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.677   -8.666  -8.997  1.00 28.03  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.773   -8.036  -10.039 1.00 30.86  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.059   -6.910  -9.267  1.00 31.34  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.816   -9.444  -5.612  1.00 23.91  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.546  -9.353  -4.358  1.00 24.43  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.616   -9.218  -3.151  1.00 25.79  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.994   -9.495  -1.995  1.00 24.95  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.360   -8.762  -3.386  1.00 21.38  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.443   -8.740  -2.257  1.00 22.24  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.221   -10.123 -1.630  1.00 21.25  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.050   -11.100 -2.345  1.00 23.05  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.089   -8.131  -2.649  1.00 22.14  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.093   -6.631  -2.881  1.00 25.11  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.057   -5.945  -2.414  1.00 26.92  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.144   -6.123  -3.515  1.00 25.10  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.111   -10.175 -0.282  1.00 21.19  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.915   -11.433 0.450   1.00 21.60  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.447   -11.514 0.866   1.00 23.38  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.870   -10.505 1.305   1.00 25.12  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.840   -11.481 1.673   1.00 22.49  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.325   -11.258 1.323   1.00 23.24  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.166  -11.381 2.611   1.00 23.41  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.752   -12.261 0.248   1.00 23.35  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.877   -12.712 0.719   1.00 22.98  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.443   -12.913 0.948   1.00 21.87  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.204   -14.272 1.589   1.00 23.71  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.072   -15.151 1.638   1.00 23.07  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.639   -12.791 -0.366  1.00 21.89  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.825   -11.373 -0.941  1.00 23.47  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.026   -13.901 -1.368  1.00 21.41  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.976   -14.466 2.106   1.00 24.18  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.425   -15.800 2.101   1.00 25.42  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.464   -15.898 0.919   1.00 25.50  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.357  -14.982 0.735   1.00 24.11  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.651   -16.161 3.385   1.00 23.63  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.603   -16.245 4.571   1.00 26.74  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.931   -15.092 5.274   1.00 28.41  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.124   -17.466 4.998   1.00 27.73  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.814   -15.150 6.351   1.00 36.32  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.038   -17.525 6.058   1.00 30.89  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.363   -16.370 6.739   1.00 32.38  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.557   -17.019 0.171   1.00 23.30  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.213  -17.159 -1.056  1.00 24.85  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.200  -18.316 -0.869  1.00 27.20  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.838  -19.386 -0.336  1.00 27.44  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.691   -17.350 -2.281  1.00 22.82  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.458  -18.076 -1.295  1.00 25.64  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.500  -19.042 -0.997  1.00 27.84  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.883  -19.788 -2.277  1.00 30.31  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.259  -19.188 -3.286  1.00 31.47  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.670  -18.354 -0.287  1.00 27.30  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.772  -19.315 0.188   1.00 35.20  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.321  -20.283 1.293   1.00 35.05  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.444  -21.126 1.877   1.00 35.24  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.917  -22.173 0.959   1.00 36.73  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.815  -21.118 -2.187  1.00 30.91  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.481  -21.935 -3.179  1.00 35.39  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.453  -22.934 -2.570  1.00 35.78  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.239  -23.374 -1.458  1.00 32.77  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.453  -22.635 -4.039  1.00 36.24  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.355  -21.747 -5.253  1.00 46.54  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.691  -21.988 -5.831  1.00 39.06  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.736  -23.423 -6.896  1.00 41.28  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.501  -23.230 -3.346  1.00 43.50  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.528  -24.211 -3.032  1.00 42.12  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.860  -25.462 -2.484  1.00 37.52  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.956  -26.008 -3.104  1.00 39.36  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.217  -24.567 -4.353  1.00 47.82  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.642  -25.078 -4.259  1.00 53.73  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.588 -24.194 -5.069  1.00 53.31  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.282  -25.901 -1.292  1.00 39.20  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.827  -27.188 -0.800  1.00 40.04  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.576  -27.056 0.059   1.00 45.26  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.177  -28.007 0.728   1.00 46.11  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.961  -25.865 0.047   1.00 38.27  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.707  -25.713 0.756   1.00 34.43  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.789  -24.547 1.719   1.00 34.05  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.458  -23.558 1.459   1.00 34.44  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.466  -25.591 -0.141  1.00 39.73  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.372  -26.695 -1.179  1.00 39.99  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.826  -27.927 -0.863  1.00 50.13  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.895  -26.514 -2.459  1.00 42.77  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.795  -28.950 -1.795  1.00 53.14  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.844  -27.525 -3.409  1.00 50.93  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -2.301  -28.755 -3.072  1.00 60.47  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -2.255  -29.774 -4.002  1.00 63.96  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.038  -24.614 2.834   1.00 31.57  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.999  -23.522 3.812   1.00 33.48  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.277  -22.333 3.147   1.00 30.80  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.558  -22.543 2.186   1.00 30.12  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.199  -24.121 4.971   1.00 36.53  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.357  -25.204 4.308   1.00 33.61  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.143  -25.750 3.156   1.00 35.82  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.566  -21.121 3.600   1.00 29.07  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.845  -19.913 3.202   1.00 26.46  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.339  -20.210 3.295   1.00 30.94  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.141   -20.601 4.356   1.00 30.36  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.241  -18.746 4.099   1.00 27.63  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.692  -18.361 3.923   1.00 29.69  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.708  -18.984 4.635   1.00 34.03  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.290  -17.390 3.155   1.00 28.62  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.882  -18.416 4.312   1.00 31.78  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.654  -17.461 3.411   1.00 33.82  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.403   -20.011 2.190   1.00 27.92  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.731   -20.609 2.065   1.00 25.85  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.797   -19.518 1.932   1.00 24.96  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.639   -18.620 1.132   1.00 26.48  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.776   -21.503 0.824   1.00 26.85  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.871   -22.545 0.908   1.00 26.36  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.220   -22.386 0.683   1.00 28.21  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.668   -23.932 1.221   1.00 27.15  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.867   -23.593 0.829   1.00 28.41  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.937   -24.557 1.170   1.00 30.94  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.542   -24.702 1.555   1.00 29.61  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.108   -25.914 1.443   1.00 32.76  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.713   -26.054 1.788   1.00 34.53  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.984   -26.647 1.764   1.00 36.03  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.934   -19.576 2.665   1.00 23.21  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.996   -18.571 2.479   1.00 22.77  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.516   -18.558 1.039   1.00 22.51  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.793   -19.611 0.446   1.00 25.48  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.088   -19.031 3.507   1.00 24.30  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.837   -20.508 3.702   1.00 23.68  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.285   -20.613 3.648   1.00 24.78  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.600   -17.357 0.473   1.00 21.55  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.875   -17.223 -0.952  1.00 22.84  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.445   -15.828 -1.259  1.00 22.20  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.427   -14.923 -0.433  1.00 22.78  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.614   -17.539 -1.768  1.00 24.28  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.953   -15.657 -2.487  1.00 23.45  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.346   -14.334 -2.938  1.00 21.56  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.812   -14.086 -4.342  1.00 22.48  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.510   -15.057 -5.077  1.00 23.00  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.864   -14.171 -2.902  1.00 23.17  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.530   -15.095 -3.903  1.00 21.21  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.094  -14.849 -3.798  1.00 22.34  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.765  -15.698 -4.812  1.00 24.22  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.044  -16.108 -4.745  1.00 26.01  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.703  -15.971 -3.611  1.00 26.52  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.626  -16.733 -5.769  1.00 26.82  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.683   -12.801 -4.684  1.00 24.01  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.446   -12.408 -6.076  1.00 22.64  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.765   -12.565 -6.818  1.00 24.57  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.736   -11.939 -6.415  1.00 25.48  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.974   -10.954 -6.207  1.00 26.95  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.770   -10.622 -5.273  1.00 31.45  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.647   -10.649 -7.694  1.00 25.18  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.467   -11.241 -5.699  1.00 34.89  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.791   -13.371 -7.876  1.00 24.88  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.038   -13.578 -8.611  1.00 28.53  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.194   -12.586 -9.760  1.00 30.44  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.256   -11.937 -10.173 1.00 29.45  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.143   -14.975 -9.186  1.00 27.16  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.170  -15.881 -8.525  1.00 28.72  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.786  -15.452 -7.534  1.00 34.59  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.299  -17.025 -8.945  1.00 31.65  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.446  -12.430 -10.236 1.00 31.32  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.694  -11.778 -11.506 1.00 36.25  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.400  -12.800 -12.605 1.00 33.79  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.297  -13.995 -12.364 1.00 35.18  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.162  -11.363 -11.607 1.00 40.29  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.567  -10.028 -10.986 1.00 48.65  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.154  -8.971  -11.511 1.00 50.74  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.329  -10.056 -9.997  1.00 54.36  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.237  -12.328 -13.829 1.00 37.76  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.203  -13.247 -14.958 1.00 34.97  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.546  -13.059 -15.651 1.00 33.85  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.915  -11.917 -15.910 1.00 36.59  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.062   -12.778 -15.858 1.00 36.68  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.698   -12.829 -15.121 1.00 40.10  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.053   -13.565 -17.167 1.00 33.02  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.726   -11.763 -15.587 1.00 40.06  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.320  -14.130 -15.826 1.00 36.11  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.621  -13.991 -16.483 1.00 34.29  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.412  -13.667 -17.970 1.00 35.51  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.391  -14.021 -18.572 1.00 34.25  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.416  -15.269 -16.330 1.00 35.71  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.411  -13.001 -18.558 1.00 36.84  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.448  -12.823 -20.009 1.00 37.05  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.260  -14.190 -20.643 1.00 30.43  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.897  -15.155 -20.237 1.00 34.30  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.777  -12.220 -20.457 1.00 38.26  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.940  -10.723 -20.223 1.00 41.87  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.924  -10.049 -20.037 1.00 42.63  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.103  -10.244 -20.216 1.00 44.15  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.340  -14.260 -21.607 1.00 33.20  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.138  -15.449 -22.410 1.00 34.62  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.178  -16.446 -21.776 1.00 38.00  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.804  -17.412 -22.423 1.00 39.50  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.793  -16.215 -20.512 1.00 34.65  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.931  -17.150 -19.795 1.00 38.27  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.450   -16.844 -20.040 1.00 33.86  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.058   -15.746 -20.445 1.00 37.17  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.267  -17.077 -18.301 1.00 38.81  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.595   -17.827 -19.721 1.00 38.42  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.159   -17.751 -19.984 1.00 37.83  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.506   -16.720 -19.068 1.00 37.22  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.702   -16.783 -17.862 1.00 40.14  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.601   -19.158 -19.680 1.00 41.59  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.077   -19.187 -19.728 1.00 41.48  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.225   -20.211 -20.598 1.00 41.45  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.742   -15.789 -19.652 1.00 36.51  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.073   -14.710 -18.932 1.00 37.40  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.786   -15.235 -18.310 1.00 39.39  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.183   -16.153 -18.851 1.00 40.31  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.733   -13.510 -19.824 1.00 38.67  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.953   -12.716 -20.324 1.00 35.19  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.616   -11.512 -21.200 1.00 45.76  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.221   -11.884 -22.598 1.00 44.03  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 4.918   -10.699 -23.401 1.00 47.51  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.313   -14.663 -17.175 1.00 38.15  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.045   -15.098 -16.588 1.00 39.52  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.886   -14.597 -17.438 1.00 37.22  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.031   -13.651 -18.195 1.00 42.26  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.990   -14.450 -15.191 1.00 39.18  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.051   -13.364 -15.186 1.00 42.37  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.916   -13.543 -16.445 1.00 38.28  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.342  -15.104 -17.220 1.00 40.84  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.539  -14.501 -17.816 1.00 42.91  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.728  -13.061 -17.365 1.00 45.62  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.211  -12.664 -16.321 1.00 36.87  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.696  -15.369 -17.301 1.00 41.14  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.045  -16.650 -16.866 1.00 38.65  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.645  -16.280 -16.391 1.00 40.50  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.504  -12.243 -18.108 1.00 45.15  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.896  -10.915 -17.631 1.00 48.48  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.454  -10.952 -16.213 1.00 42.05  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.150  -11.892 -15.845 1.00 44.51  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.959  -10.407 -18.642 1.00 47.29  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.163  -11.560 -19.594 1.00 40.62  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.015  -12.548 -19.465 1.00 47.05  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.083  -9.935  -15.434 1.00 44.14  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.541  -9.687  -14.078 1.00 45.33  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.016  -10.726 -13.085 1.00 38.29  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.415  -10.678 -11.919 1.00 36.91  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.054  -9.516  -14.004 1.00 54.08  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.478  -8.338  -14.843 1.00 57.98  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.292  -7.184  -14.434 1.00 60.39  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -5.997  -8.619  -16.028 1.00 55.78  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.124  -11.630 -13.534 1.00 33.17  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.582  -12.657 -12.650 1.00 27.76  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.115  -12.350 -12.394 1.00 26.29  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.549   -11.669 -13.202 1.00 31.16  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.767  -14.112 -13.099 1.00 31.40  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.222  -14.581 -13.371 1.00 36.46  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.128  -14.102 -12.242 1.00 43.18  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.591  -14.395 -12.427 1.00 51.60  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.792  -15.844 -12.399 1.00 47.22  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.358   -12.780 -11.224 1.00 25.17  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.764   -12.624 -10.873 1.00 26.06  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.406   -13.996 -10.805 1.00 24.32  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.781   -14.974 -10.399 1.00 26.22  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.893   -12.016 -9.455  1.00 25.92  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.373   -10.594 -9.421  1.00 27.18  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.006   -10.319 -9.296  1.00 33.78  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.233   -9.527  -9.606  1.00 30.89  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.465  -9.016  -9.353  1.00 34.07  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.776   -8.218  -9.628  1.00 31.09  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.425   -7.969  -9.501  1.00 35.41  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.013  -6.681  -9.583  1.00 37.05  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.726   -14.130 -11.089 1.00 23.84  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.390   -15.398 -10.827 1.00 23.19  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.752   -15.546 -9.356  1.00 23.79  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.457   -14.695 -8.810  1.00 26.87  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.629   -15.310 -11.735 1.00 24.64  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.932   -13.855 -11.805 1.00 25.38  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.612   -13.080 -11.627 1.00 27.61  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.187   -16.572 -8.711  1.00 23.37  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.392   -16.715 -7.275  1.00 22.67  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.358   -17.888 -7.067  1.00 24.33  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.083   -19.010 -7.516  1.00 26.80  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.053   -16.956 -6.560  1.00 22.04  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.038   -15.825 -6.878  1.00 24.02  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.286   -17.133 -5.041  1.00 21.32  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.523   -14.416 -6.548  1.00 25.34  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.460   -17.649 -6.320  1.00 21.31  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.362   -18.724 -5.970  1.00 21.66  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.085   -19.130 -4.527  1.00 22.40  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.121   -18.288 -3.627  1.00 25.84  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.806   -18.201 -6.105  1.00 24.54  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.831   -19.240 -5.680  1.00 24.72  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.198  -20.262 -6.566  1.00 26.59  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.404  -19.214 -4.393  1.00 28.93  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.153  -21.207 -6.198  1.00 27.86  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.340  -20.192 -4.024  1.00 27.40  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.708  -21.176 -4.922  1.00 28.40  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.761   -20.416 -4.331  1.00 22.70  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.345   -20.950 -3.040  1.00 21.07  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.607   -21.448 -2.362  1.00 25.81  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.316   -22.328 -2.908  1.00 27.26  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.360   -22.115 -3.316  1.00 26.04  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.991   -21.583 -3.715  1.00 26.81  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.716   -21.223 -5.035  1.00 30.49  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.989   -21.444 -2.762  1.00 27.45  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.478   -20.683 -5.374  1.00 30.90  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.753   -20.886 -3.098  1.00 25.46  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.516   -20.501 -4.402  1.00 27.57  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.898   -20.871 -1.192  1.00 24.22  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.072   -21.356 -0.473  1.00 27.54  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.833   -22.792 0.005   1.00 27.56  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.683   -23.223 0.187   1.00 27.84  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.338   -20.424 0.724   1.00 26.03  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.831   -19.037 0.336   1.00 24.89  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.084  -18.841 -0.240  1.00 25.15  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.090   -17.891 0.643   1.00 24.86  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.508  -17.562 -0.608  1.00 21.41  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.547   -16.613 0.304   1.00 23.59  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.772  -16.443 -0.313  1.00 23.27  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.938   -23.513 0.247   1.00 25.26  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.861   -24.863 0.764   1.00 26.90  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.635   -25.879 -0.360  1.00 34.64  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.491  -26.725 -0.597  1.00 36.02  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.521   -25.759 -1.109  1.00 32.21  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.257   -26.648 -2.232  1.00 33.67  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.040   -26.204 -3.466  1.00 34.79  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.296   -26.988 -4.382  1.00 31.69  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.762   -26.758 -2.541  1.00 31.64  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.355   -25.487 -3.045  1.00 31.42  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.955   -27.207 -1.346  1.00 33.03  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.333   -24.902 -3.533  1.00 28.51  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.016  -24.285 -4.657  1.00 29.61  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.203   -24.380 -5.945  1.00 29.42  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.772   -24.324 -7.024  1.00 32.44  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.463  -24.786 -4.809  1.00 27.64  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.204  -24.821 -3.517  1.00 31.88  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.058  -25.844 -3.183  1.00 32.85  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.247  -23.944 -2.493  1.00 30.16  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.535  -25.632 -1.961  1.00 38.79  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.088  -24.459 -1.537  1.00 33.97  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.875   -24.498 -5.833  1.00 30.28  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.990   -24.522 -6.989  1.00 29.27  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.562   -23.102 -7.378  1.00 32.55  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.755   -22.167 -6.592  1.00 30.46  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.709   -25.268 -6.631  1.00 31.76  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 5.926   -26.718 -6.217  1.00 38.93  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.692   -27.110 -5.415  1.00 46.01  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 4.215   -26.355 -4.535  1.00 47.69  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 4.227   -28.218 -5.638  1.00 45.22  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.108   -22.942 -8.636  1.00 27.72  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.611   -21.670 -9.138  1.00 27.76  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.147   -21.840 -9.545  1.00 30.65  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.768   -22.871 -10.107 1.00 34.48  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.437   -21.133 -10.312 1.00 33.01  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.709   -20.747 -9.799  1.00 31.33  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.831   -19.885 -10.933 1.00 34.74  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.321   -20.847 -9.211  1.00 27.10  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.970   -20.773 -9.734  1.00 27.18  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.647   -19.320 -10.041 1.00 28.80  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.311   -18.410 -9.541  1.00 28.84  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.975   -21.403 -8.766  1.00 28.76  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.600   -19.102 -10.850 1.00 25.30  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.214   -17.764 -11.241 1.00 27.19  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.041  -17.407 -10.464 1.00 30.35  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.017  -18.151 -10.484 1.00 34.63  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.102  -17.706 -12.736 1.00 31.07  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.112   -18.059 -13.572 1.00 29.87  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.261   -17.266 -13.507 1.00 32.85  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 1.059   -19.087 -14.512 1.00 34.97  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.389   -17.583 -14.265 1.00 46.50  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.180   -19.374 -15.284 1.00 38.95  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.332   -18.620 -15.174 1.00 37.37  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.967  -16.299 -9.734  1.00 26.22  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.047  -15.922 -8.834  1.00 26.25  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.341  -14.433 -8.965  1.00 27.70  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.482  -13.590 -9.284  1.00 27.27  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.678  -16.254 -7.383  1.00 27.74  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.628  -17.735 -7.026  1.00 30.38  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.302  -17.726 -5.547  1.00 30.66  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -2.992  -18.397 -7.255  1.00 36.00  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.605  -14.095 -8.682  1.00 25.67  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.967  -12.700 -8.633  1.00 27.63  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.965  -12.204 -7.183  1.00 24.37  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.911  -13.027 -6.242  1.00 24.29  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.020  -10.868 -6.987  1.00 25.88  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -3.978  -10.246 -5.648  1.00 26.19  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.977  -10.779 -4.618  1.00 25.51  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.712  -10.717 -3.419  1.00 23.01  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.196  -8.751  -5.944  1.00 28.93  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.632  -8.576  -7.344  1.00 28.40  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.062  -9.865  -8.063  1.00 26.50  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.108  -11.357 -5.090  1.00 26.64  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.089  -11.859 -4.128  1.00 25.90  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.548  -13.016 -3.282  1.00 24.02  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.021  -13.256 -2.168  1.00 24.43  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.387  -12.401 -4.752  1.00 29.34  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.184  -13.641 -5.584  1.00 30.69  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.483  -14.013 -6.298  1.00 40.32  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.386  -15.294 -7.070  1.00 42.99  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.142  -16.483 -6.245  1.00 45.81  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.499  -13.692 -3.796  1.00 25.24  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.925  -14.819 -3.109  1.00 24.42  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.565  -14.463 -2.482  1.00 24.95  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.885  -15.377 -2.008  1.00 24.16  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.855  -16.001 -4.074  1.00 27.22  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.243  -16.565 -4.374  1.00 29.50  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.065  -16.531 -3.441  1.00 30.10  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.488  -17.013 -5.526  1.00 31.56  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.217  -13.169 -2.418  1.00 23.43  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.892  -12.750 -1.941  1.00 20.79  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.027  -11.898 -0.678  1.00 21.73  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.632  -10.823 -0.693  1.00 23.69  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.178  -11.966 -3.051  1.00 21.73  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.029  -12.714 -4.382  1.00 25.03  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.326  -11.859 -5.420  1.00 24.52  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.245  -14.009 -4.224  1.00 24.68  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.463  -12.384 0.436   1.00 21.81  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.548  -11.636 1.692   1.00 23.22  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.151  -11.148 2.090   1.00 24.85  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.741   -11.979 2.285   1.00 26.28  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.991  -12.648 2.735   1.00 23.26  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.427  -13.093 2.478   1.00 23.94  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.730  -13.989 1.455   1.00 26.72  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.449  -12.579 3.267   1.00 28.27  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.045  -14.368 1.195   1.00 29.27  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.765  -12.958 2.997   1.00 27.13  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.045  -13.880 2.010   1.00 28.95  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.071   -9.828  2.249   1.00 28.37  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.417   -9.327  2.591   1.00 25.93  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.971   -9.992  3.850   1.00 26.71  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.266   -10.210 4.832   1.00 27.90  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.196   -7.791  2.689   1.00 26.07  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.083   -7.526  1.646   1.00 29.72  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.851  -8.737  1.879   1.00 29.03  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.270   -10.389 3.810   1.00 25.78  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.820   -11.270 4.828   1.00 26.83  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.864   -10.619 6.225   1.00 25.27  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.516   -11.294 7.201   1.00 30.16  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.230   -11.673 4.358   1.00 26.32  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.995   -12.471 5.410   1.00 26.62  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.706   -13.807 5.713   1.00 27.70  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.040   -11.858 6.091   1.00 31.30  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.431   -14.529 6.665   1.00 30.29  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.775   -12.579 7.014   1.00 30.97  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.458   -13.879 7.328   1.00 31.95  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.226   -14.508 8.285   1.00 35.01  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.298   -9.359  6.300   1.00 27.79  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.439   -8.684  7.594   1.00 32.93  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.094   -8.612  8.324   1.00 32.12  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.995   -9.056  9.470   1.00 41.74  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.231   -7.388  7.473   1.00 28.70  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 2.037   -8.180  7.621   1.00 38.88  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.701   -8.099  8.203   1.00 35.05  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? 0.192   -9.468  8.663   1.00 35.26  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.538  -9.527  9.655   1.00 33.93  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.277  -7.454  7.206   1.00 39.01  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.724  -7.255  7.677   1.00 44.78  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.594  -6.582  6.617   1.00 42.68  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.649  -5.692  7.212   1.00 44.52  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.734  -6.393  7.886   1.00 50.41  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.522   -10.558 7.930   1.00 30.30  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.172  -11.834 8.045   1.00 29.20  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.606   -12.887 8.836   1.00 26.59  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? 0.091   -13.988 9.029   1.00 31.03  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.502  -12.398 6.690   1.00 30.13  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.283  -11.433 5.999   1.00 41.45  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.865   -12.612 9.202   1.00 30.52  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.691   -13.727 9.662   1.00 32.18  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.254   -14.245 11.036  1.00 31.48  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.423   -15.438 11.326  1.00 36.83  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 4.190   -13.398 9.631   1.00 36.05  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.600   -12.193 10.414  1.00 36.49  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 6.125   -12.202 10.471  1.00 49.71  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.657   -11.055 11.276  1.00 55.43  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.530   -9.800  10.525  1.00 66.79  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.683   -13.356 11.865  0.50 37.08  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.710   -13.353 11.879  0.50 36.21  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.194   -13.743 13.182  0.50 37.59  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.197   -13.787 13.170  0.50 35.63  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? 0.045   -14.743 13.042  0.50 38.25  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? 0.157   -14.880 12.940  0.50 35.84  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.159  -15.580 13.911  0.50 42.82  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? 0.160   -15.906 13.611  0.50 35.16  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.874   -12.538 14.056  0.50 41.03  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.628   -12.640 13.990  0.50 38.65  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 2.069   -11.799 14.650  0.50 44.83  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? 0.123   -13.040 15.369  0.50 42.24  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.184   -12.364 14.642  0.50 45.60  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.976   -13.244 16.270  0.50 43.33  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.877   -10.658 15.116  0.50 47.33  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.113  -13.192 15.516  0.50 46.03  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.694  -14.682 11.928  1.00 33.16  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -1.812  -15.579 11.705  1.00 33.50  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.386  -16.844 10.982  1.00 36.11  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -1.925  -17.913 11.264  1.00 37.17  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -2.878  -14.849 10.887  1.00 35.53  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.134  -15.652 10.646  1.00 37.90  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.100  -14.733 9.893   1.00 44.24  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.528  -15.207 9.883   1.00 49.29  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.439  -14.191 9.336   1.00 44.09  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.490  -16.709 9.983   1.00 33.07  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.303  -17.768 9.007   1.00 32.15  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 1.067   -18.440 9.164   1.00 31.74  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.287   -19.506 8.605   1.00 33.55  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.481  -17.295 7.548   1.00 31.57  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -1.884  -16.854 7.151   1.00 34.27  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.017  -17.584 7.542   1.00 31.58  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.071  -15.687 6.403   1.00 31.76  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.294  -17.176 7.174   1.00 32.10  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.345  -15.256 6.059   1.00 33.21  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.451  -16.003 6.451   1.00 32.65  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.698  -15.586 6.085   1.00 34.61  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.968   -17.806 9.905   1.00 29.83  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.347   -18.268 9.983   1.00 32.08  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.576   -19.224 11.160  1.00 33.00  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.408   -18.968 12.000  1.00 40.57  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.820   -20.316 11.209  1.00 38.85  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.987   -21.328 12.235  1.00 42.29  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.217   -22.669 11.541  1.00 38.13  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.787   -22.891 10.408  1.00 36.55  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.772   -21.320 13.177  1.00 46.10  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.691   -20.099 14.087  1.00 48.52  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? 0.299   -19.803 14.644  1.00 61.59  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.943   -23.618 12.173  1.00 37.62  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 4.257   -24.883 11.507  1.00 33.89  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 3.010   -25.628 11.081  1.00 37.05  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.981   -25.514 11.734  1.00 41.98  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 5.027   -25.675 12.603  1.00 39.42  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.609   -24.588 13.472  1.00 40.25  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.557   -23.474 13.503  1.00 40.20  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 3.153   -26.417 10.025  1.00 39.54  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 2.082   -27.144 9.378   1.00 44.40  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.654   -28.499 9.004   1.00 50.81  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.854   -28.625 8.782   1.00 50.72  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.689   -26.461 8.070   1.00 44.80  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? 0.278   -26.784 7.644   1.00 53.04  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? 0.065   -27.591 6.734   1.00 50.09  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -0.702  -26.175 8.295   1.00 62.32  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.776   -29.492 8.904   1.00 50.75  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 2.169   -30.855 8.604   1.00 53.72  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.511   -31.001 7.119   1.00 48.39  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.209   -31.937 6.736   1.00 48.07  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 1.028   -31.761 9.099   1.00 54.24  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.193  -31.846 8.177   1.00 58.94  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 2.056   -30.062 6.275   1.00 43.20  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 2.166   -30.233 4.834   1.00 42.52  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.625   -30.219 4.374   1.00 40.80  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.433   -29.448 4.890   1.00 39.02  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 1.318   -29.197 4.082   1.00 42.87  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.161  -29.357 4.402   1.00 50.32  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -0.789  -30.591 3.760   1.00 48.97  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.699  -30.204 2.680   1.00 62.31  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -2.853  -29.559 2.882   1.00 62.68  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.550  -29.148 1.839   1.00 62.87  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.299  -29.314 4.112   1.00 60.49  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.902   -31.028 3.339   1.00 41.80  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 5.230   -31.229 2.782   1.00 43.42  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.796   -29.880 2.345   1.00 37.59  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 5.228   -29.202 1.488   1.00 34.73  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 5.180   -32.124 1.539   1.00 43.05  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.507   -32.602 0.981   1.00 50.82  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.410   -33.595 -0.175  1.00 53.73  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.755   -34.005 -0.704  1.00 54.41  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.937   -29.499 2.921   1.00 38.24  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.613   -28.321 2.398   1.00 33.32  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.317   -27.082 3.237   1.00 34.42  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 8.075   -26.126 3.174   1.00 31.65  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.229   -27.100 4.010   1.00 29.47  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.767   -25.890 4.665   1.00 31.36  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.799   -25.305 5.644   1.00 34.90  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 7.057   -24.093 5.667   1.00 32.02  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.424   -26.171 5.342   1.00 29.96  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.710   -24.882 5.709   1.00 32.89  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.976   -24.214 6.893   1.00 34.81  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.784   -24.330 4.820   1.00 33.06  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.333   -23.021 7.202   1.00 35.26  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 2.117   -23.149 5.133   1.00 31.75  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.402   -22.489 6.320   1.00 29.93  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.327   -26.143 6.545   1.00 29.15  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 8.213   -25.621 7.579   1.00 30.25  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.558   -25.161 6.995   1.00 29.12  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 10.154  -24.186 7.497   1.00 30.15  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.378   -26.641 8.700   1.00 31.99  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 7.045   -26.942 9.351   1.00 40.03  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 6.124   -26.111 9.310   1.00 35.45  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.936   -28.100 9.995   1.00 34.06  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 10.048  -25.875 5.970   1.00 30.01  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 11.221  -25.382 5.252   1.00 29.72  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.893  -24.011 4.644   1.00 28.52  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.713  -23.073 4.676   1.00 26.19  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.679  -26.377 4.190   1.00 30.67  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.875  -25.916 3.359   1.00 32.25  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.494  -27.057 2.544   1.00 41.32  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.988  -28.197 2.570   1.00 46.72  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.509  -26.842 1.879   1.00 40.72  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.668   -23.897 4.117   1.00 27.71  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 9.215   -22.619 3.571   1.00 29.88  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 9.241   -21.481 4.601   1.00 27.95  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.593   -20.342 4.264   1.00 25.92  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.812   -21.760 5.843   1.00 25.82  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.838   -20.735 6.867   1.00 26.69  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 10.276  -20.283 7.140   1.00 26.71  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.520  -19.102 7.416   1.00 24.61  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 8.164   -21.243 8.150   1.00 30.27  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.670   -21.579 8.010   1.00 32.93  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.222   -22.216 9.318   1.00 32.46  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.789   -20.377 7.726   1.00 30.58  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 11.228  -21.241 7.077   1.00 27.45  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.608  -20.868 7.369   1.00 28.02  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 13.104  -19.949 6.256   1.00 24.78  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.760  -18.952 6.507   1.00 26.76  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.537  -22.102 7.539   1.00 27.73  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.997  -21.746 7.752   1.00 27.05  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.643  -21.602 8.946   1.00 29.28  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.966  -21.465 6.726   1.00 28.08  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.949  -21.271 8.733   1.00 30.84  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 17.165  -21.146 7.378   1.00 30.67  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.903  -21.437 5.321   1.00 27.22  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.324  -20.821 6.666   1.00 27.94  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 17.032  -21.082 4.610   1.00 31.58  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 18.231  -20.794 5.292   1.00 28.10  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.773  -20.291 5.005   1.00 23.37  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 13.276  -19.549 3.877   1.00 23.77  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.773  -18.110 3.909   1.00 27.05  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.528  -17.184 3.688   1.00 24.09  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.904  -20.198 2.546   1.00 23.70  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.534  -21.583 2.408   1.00 22.68  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 13.131  -22.354 1.144   1.00 26.64  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 12.184  -21.903 0.463   1.00 28.75  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.767  -23.411 0.771   1.00 28.36  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.460  -17.944 4.101   1.00 25.42  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.875  -16.614 4.009   1.00 27.00  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.452  -15.717 5.108   1.00 23.77  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.632  -14.517 4.905   1.00 24.19  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.336   -16.664 4.041   1.00 23.68  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.728   -15.306 3.562   1.00 23.98  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.822   -17.012 5.454   1.00 25.19  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.272   -15.445 3.085   1.00 24.32  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.795  -16.311 6.266   1.00 24.32  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 12.297  -15.502 7.379   1.00 24.99  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.796  -15.241 7.269   1.00 29.75  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 14.252  -14.165 7.707   1.00 30.37  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.884  -16.194 8.684   1.00 28.63  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.494  -15.600 9.948   1.00 37.99  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.799  -16.138 11.188  1.00 46.27  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.485  -17.337 11.288  1.00 40.90  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.514  -15.244 12.127  1.00 47.40  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.546  -16.221 6.724   1.00 24.13  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 16.000  -16.242 6.811   1.00 27.66  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.702  -15.891 5.503   1.00 27.82  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.779  -15.270 5.555   1.00 29.01  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.537  -17.515 7.461   1.00 29.38  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 16.018  -17.601 8.881   1.00 29.85  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 16.357  -16.744 9.714   1.00 32.79  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 15.088  -18.509 9.141   1.00 27.97  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 16.162  -16.291 4.338   1.00 24.84  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.808  -15.889 3.091   1.00 24.69  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.765  -15.794 1.962   1.00 24.50  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.761  -16.550 0.976   1.00 24.96  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 18.001  -16.803 2.759   1.00 27.51  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 19.044  -16.192 1.846   1.00 28.43  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.797  -15.193 1.167   1.00 26.23  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 20.233  -16.801 1.748   1.00 28.63  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.820  -14.845 2.083   1.00 24.14  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.672  -14.822 1.178   1.00 22.09  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 14.013  -14.379 -0.237  1.00 25.89  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 13.230  -14.620 -1.131  1.00 24.62  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.711  -13.878 1.877   1.00 22.93  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.645  -12.906 2.596   1.00 22.68  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.737  -13.843 3.164   1.00 23.62  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 15.199  -13.798 -0.452  1.00 22.97  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.534  -13.303 -1.783  1.00 22.56  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.665  -14.109 -2.442  1.00 24.46  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 17.174  -13.688 -3.487  1.00 24.66  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.990  -11.842 -1.606  1.00 22.09  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.905  -10.969 -1.055  1.00 21.70  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.657  -10.874 -1.648  1.00 23.10  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.860  -10.212 0.045   1.00 21.48  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.909  -10.022 -0.950  1.00 22.67  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.611  -9.607  0.078   1.00 24.79  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.935  -15.309 -1.921  1.00 25.72  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.998  -16.163 -2.448  1.00 25.45  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.555  -16.882 -3.718  1.00 29.81  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.379  -17.014 -4.026  1.00 27.85  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.461  -17.157 -1.403  1.00 25.88  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.554  -17.369 -4.445  1.00 27.92  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 18.294  -18.301 -5.526  1.00 33.56  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.987  -19.686 -4.954  1.00 33.19  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.775  -20.258 -4.196  1.00 35.87  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.463  -18.315 -6.481  1.00 36.09  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 19.255  -19.343 -7.424  1.00 41.89  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.824  -20.232 -5.323  1.00 29.78  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.439  -21.566 -4.902  1.00 36.36  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.335  -22.498 -6.108  1.00 42.21  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.826  -23.605 -5.975  1.00 49.41  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 15.113  -21.572 -4.131  1.00 30.00  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 15.262  -20.962 -2.752  1.00 28.99  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.690  -21.733 -1.663  1.00 29.63  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.963  -19.618 -2.544  1.00 29.81  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.876  -21.154 -0.418  1.00 32.24  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 15.108  -19.053 -1.288  1.00 27.37  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.549  -19.816 -0.226  1.00 29.87  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.782  -19.275 1.003   1.00 32.14  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.815  -22.050 -7.267  1.00 50.14  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 17.036  -22.959 -8.383  1.00 68.39  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 18.050  -24.033 -7.952  1.00 77.03  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 19.160  -23.634 -7.517  1.00 75.53  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.494  -22.208 -9.617  1.00 67.87  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 16.508  -21.269 -10.028 1.00 72.23  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 17.688  -25.232 -8.021  1.00 86.32  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.852  -11.324 -42.195 1.00 62.35  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.429  -12.260 -43.269 1.00 66.04  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 36.901  -12.337 -43.265 1.00 58.11  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.302  -12.491 -42.199 1.00 61.59  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.070  -13.638 -43.054 1.00 73.03  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.177  -14.515 -44.299 1.00 85.54  ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.070  -13.849 -45.724 1.00 91.81  ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 41.377  -12.863 -44.979 1.00 66.80  ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.226  -12.172 -44.434 1.00 54.17  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.765  -12.322 -44.517 1.00 52.68  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.398  -13.777 -44.226 1.00 51.55  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.126  -14.673 -44.627 1.00 45.97  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.418  -11.914 -45.954 1.00 53.13  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.665  -11.201 -46.465 1.00 50.15  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.839  -11.817 -45.727 1.00 48.81  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.310  -14.004 -43.474 1.00 48.76  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.895  -15.365 -43.165 1.00 53.40  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.509  -15.626 -43.741 1.00 49.15  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.913  -14.725 -44.352 1.00 43.24  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 33.024  -15.660 -41.669 1.00 57.38  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.438  -15.626 -41.209 1.00 63.46  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.393  -16.488 -41.713 1.00 66.63  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 35.075  -14.821 -40.344 1.00 63.41  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.564  -16.221 -41.141 1.00 58.43  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.394  -15.212 -40.309 1.00 64.38  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 31.007  -16.860 -43.551 1.00 43.48  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.684  -17.187 -44.063 1.00 46.04  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.684  -16.166 -43.532 1.00 45.84  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 27.826  -15.692 -44.268 1.00 47.75  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.277  -18.595 -43.675 1.00 43.71  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.795  -15.861 -42.238 1.00 44.36  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 27.988  -14.821 -41.614 1.00 46.37  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.847  -13.571 -41.396 1.00 42.10  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 29.966  -13.649 -40.884 1.00 43.48  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.398  -15.307 -40.283 1.00 42.84  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.308  -16.369 -40.381 1.00 39.52  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 24.980  -16.013 -40.580 1.00 36.64  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.611  -17.719 -40.273 1.00 46.68  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 23.985  -16.977 -40.682 1.00 41.19  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.614  -18.682 -40.386 1.00 36.12  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.296  -18.308 -40.552 1.00 36.02  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.278  -12.413 -41.738 1.00 44.31  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 28.969  -11.141 -41.582 1.00 40.99  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.221  -10.262 -40.567 1.00 41.85  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 26.991  -10.337 -40.445 1.00 37.42  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 28.989  -10.467 -42.953 1.00 42.46  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 27.666  -9.967  -43.494 1.00 43.03  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 27.877  -9.501  -44.939 1.00 49.58  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 26.668  -8.983  -45.660 1.00 48.95  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 25.761  -10.081 -46.010 1.00 54.38  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.926  -9.340  -39.863 1.00 44.63  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.276  -8.405  -38.935 1.00 37.01  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.110  -7.712  -39.609 1.00 39.43  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.243  -7.254  -40.750 1.00 43.70  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.439  -7.443  -38.684 1.00 40.79  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.646  -8.360  -38.654 1.00 41.81  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.388  -9.136  -39.933 1.00 44.87  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 25.962  -7.708  -38.927 1.00 33.93  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.749  -7.078  -39.405 1.00 33.36  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.768  -8.053  -40.052 1.00 32.83  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.637  -7.677  -40.311 1.00 33.70  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.196  -9.294  -40.359 1.00 34.09  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.244  -10.248 -40.906 1.00 34.78  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.189  -10.571 -39.841 1.00 27.16  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.498  -10.627 -38.654 1.00 32.99  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 23.893  -11.570 -41.242 1.00 34.89  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.650  -11.659 -42.561 1.00 45.08  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.412  -10.802 -43.417 1.00 43.11  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.475  -12.597 -42.693 1.00 39.54  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 20.958  -10.772 -40.281 1.00 29.86  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.877  -10.985 -39.336 1.00 30.24  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.583  -12.473 -39.346 1.00 33.22  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.657  -13.098 -40.414 1.00 38.17  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.680  -10.168 -39.817 1.00 30.55  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 18.945  -8.658  -39.929 1.00 30.47  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.648  -7.917  -40.182 1.00 34.17  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.722  -8.183  -38.704 1.00 31.44  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.202  -13.011 -38.176 1.00 30.03  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 19.052  -14.459 -38.046 1.00 27.66  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.971  -14.733 -37.008 1.00 32.00  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.559  -13.827 -36.270 1.00 30.20  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.359  -15.169 -37.605 1.00 28.26  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.509  -15.053 -38.634 1.00 31.08  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.828  -14.746 -36.202 1.00 31.52  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.524  -15.995 -36.967 1.00 31.37  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 17.011  -16.551 -35.728 1.00 29.27  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 18.101  -17.411 -35.132 1.00 29.90  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.730  -18.178 -35.876 1.00 29.77  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.755  -17.395 -35.944 1.00 27.64  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.567  -16.546 -36.346 1.00 31.26  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.341  -16.259 -37.685 1.00 30.97  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.700  -16.027 -35.391 1.00 32.43  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.248  -15.501 -38.065 1.00 32.93  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.601  -15.267 -35.769 1.00 32.55  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.376  -15.012 -37.113 1.00 35.55  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.312  -17.268 -33.801 1.00 25.94  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.368  -17.957 -33.091 1.00 26.88  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.749  -18.902 -32.056 1.00 26.22  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.832  -18.525 -31.334 1.00 27.90  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.329  -16.965 -32.427 1.00 26.56  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.274  -20.126 -31.987 1.00 27.23  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.641  -21.181 -31.200 1.00 28.55  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.520  -21.520 -30.011 1.00 33.20  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.700  -21.840 -30.170 1.00 33.69  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.412  -22.444 -32.048 1.00 34.36  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.712  -23.587 -31.270 1.00 31.62  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 16.256  -23.178 -31.018 1.00 32.12  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.395  -24.300 -30.409 1.00 34.27  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.876  -24.559 -29.048 1.00 32.13  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.901  -21.463 -28.828 1.00 34.61  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.515  -21.853 -27.566 1.00 37.71  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.640  -22.926 -26.919 1.00 36.08  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.411  -22.891 -26.996 1.00 31.90  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.586  -20.678 -26.584 1.00 40.78  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.226  -19.405 -27.090 1.00 43.32  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 22.008  -19.253 -26.856 1.00 46.32  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 22.404  -19.539 -25.130 1.00 44.99  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 19.288  -23.899 -26.281 1.00 34.76  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.558  -24.901 -25.520 1.00 36.69  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.585  -24.210 -24.549 1.00 34.57  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.960  -23.254 -23.876 1.00 36.57  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.630  -25.768 -24.835 1.00 47.14  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 19.169  -27.122 -24.276 1.00 49.75  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 20.026  -27.629 -23.117 1.00 53.57  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 16.318  -24.651 -24.560 1.00 37.16  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.298  -24.146 -23.651 1.00 38.26  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.472  -22.984 -24.204 1.00 39.69  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.551  -22.527 -23.536 1.00 38.82  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.798  -22.483 -25.406 1.00 34.81  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 14.096  -21.306 -25.900 1.00 32.82  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.739  -21.507 -27.372 1.00 31.96  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.429  -22.218 -28.093 1.00 33.99  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 15.049  -20.109 -25.807 1.00 31.74  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.490  -19.801 -24.382 1.00 33.65  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.722  -18.979 -23.554 1.00 38.53  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.612  -20.410 -23.831 1.00 34.44  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 15.101  -18.721 -22.241 1.00 38.44  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 16.993  -20.160 -22.517 1.00 40.72  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 16.240  -19.311 -21.723 1.00 43.97  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 16.622  -19.079 -20.430 1.00 45.80  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.690  -20.835 -27.882 1.00 32.19  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.400  -20.869 -29.315 1.00 29.41  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.469  -20.131 -30.122 1.00 28.02  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 14.139  -19.282 -29.558 1.00 29.00  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 11.069  -20.170 -29.391 1.00 29.92  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 11.049  -19.234 -28.195 1.00 31.53  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.794  -19.964 -27.097 1.00 31.44  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.680  -20.530 -31.398 1.00 27.79  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.505  -19.755 -32.336 1.00 30.26  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.236  -18.259 -32.153 1.00 28.17  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 13.086  -17.835 -32.188 1.00 27.72  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 14.180  -20.216 -33.772 1.00 28.44  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.404  -21.696 -33.942 1.00 30.96  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.460  -22.648 -33.565 1.00 33.34  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.456  -22.388 -34.439 1.00 32.20  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.933  -23.862 -33.850 1.00 33.58  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 15.134  -23.729 -34.374 1.00 32.56  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.294  -17.466 -31.928 1.00 30.84  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 15.082  -16.146 -31.339 1.00 29.07  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.592  -15.065 -32.295 1.00 28.93  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.693  -15.217 -32.802 1.00 30.58  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.811  -16.040 -29.992 1.00 27.81  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.285  -14.892 -29.155 1.00 30.88  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.559  -13.553 -29.269 1.00 30.35  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.359  -15.005 -28.039 1.00 31.98  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.826  -12.829 -28.343 1.00 31.16  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 14.108  -13.696 -27.556 1.00 30.16  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.739  -16.095 -27.399 1.00 32.88  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.253  -13.434 -26.475 1.00 27.79  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.904  -15.842 -26.326 1.00 31.09  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.633  -14.530 -25.904 1.00 29.85  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.824  -13.990 -32.609 1.00 30.27  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.270  -12.970 -33.568 1.00 27.03  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.564  -12.365 -33.047 1.00 26.78  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.701  -12.054 -31.870 1.00 28.41  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 14.119  -11.940 -33.636 1.00 26.85  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.380  -12.188 -32.316 1.00 28.80  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.477  -13.704 -32.118 1.00 28.16  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.571  -12.277 -33.917 1.00 27.86  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.892  -11.906 -33.456 1.00 25.01  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.716  -11.369 -34.624 1.00 26.85  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.252  -11.397 -35.775 1.00 28.81  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.614  -13.059 -32.760 1.00 29.46  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.906  -10.865 -34.282 1.00 29.57  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.836  -10.398 -35.314 1.00 31.90  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.256  -10.844 -34.991 1.00 31.31  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.593  -11.130 -33.851 1.00 31.11  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.838  -8.874  -35.454 1.00 32.85  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.511  -8.130  -34.310 1.00 31.70  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.269  -6.626  -34.451 1.00 32.61  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.871  -5.904  -33.326 1.00 34.38  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.580  -4.655  -32.957 1.00 36.19  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.593  -4.008  -33.576 1.00 32.45  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.251  -4.106  -31.945 1.00 33.16  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.101  -10.914 -36.043 1.00 30.92  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.523  -11.104 -35.855 1.00 35.02  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 26.090  -9.731  -35.512 1.00 38.65  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.828  -8.768  -36.233 1.00 37.73  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.154  -11.599 -37.171 1.00 38.50  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.409  -12.804 -37.713 1.00 36.58  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.656  -11.846 -36.995 1.00 38.38  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.475  -14.019 -36.797 1.00 36.46  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.873  -9.684  -34.438 1.00 35.79  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.530  -8.453  -34.009 1.00 44.63  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 28.981  -8.426  -34.491 1.00 46.37  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.536  -9.466  -34.830 1.00 49.59  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.472  -8.315  -32.499 1.00 38.62  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.281  -7.559  -31.925 1.00 45.69  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.430  -7.070  -32.707 1.00 41.05  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 26.220  -7.457  -30.679 1.00 40.54  ? 26  ASP B OD2 1 
ATOM   964  N N   A ASP B 1 28 ? 29.586  -7.231  -34.420 0.50 54.12  ? 27  ASP B N   1 
ATOM   965  N N   B ASP B 1 28 ? 29.591  -7.233  -34.542 0.50 49.92  ? 27  ASP B N   1 
ATOM   966  C CA  A ASP B 1 28 ? 30.971  -6.967  -34.778 0.50 57.24  ? 27  ASP B CA  1 
ATOM   967  C CA  B ASP B 1 28 ? 30.955  -7.119  -35.040 0.50 48.80  ? 27  ASP B CA  1 
ATOM   968  C C   A ASP B 1 28 ? 31.920  -7.678  -33.803 0.50 57.55  ? 27  ASP B C   1 
ATOM   969  C C   B ASP B 1 28 ? 31.950  -7.418  -33.910 0.50 49.41  ? 27  ASP B C   1 
ATOM   970  O O   A ASP B 1 28 ? 31.637  -7.622  -32.588 0.50 62.53  ? 27  ASP B O   1 
ATOM   971  O O   B ASP B 1 28 ? 31.531  -7.305  -32.740 0.50 52.29  ? 27  ASP B O   1 
ATOM   972  C CB  A ASP B 1 28 ? 31.233  -5.470  -34.767 0.50 53.92  ? 27  ASP B CB  1 
ATOM   973  C CB  B ASP B 1 28 ? 31.234  -5.758  -35.661 0.50 45.62  ? 27  ASP B CB  1 
ATOM   974  C CG  A ASP B 1 28 ? 30.198  -4.648  -35.517 0.50 49.87  ? 27  ASP B CG  1 
ATOM   975  C CG  B ASP B 1 28 ? 32.230  -5.771  -36.813 0.50 40.26  ? 27  ASP B CG  1 
ATOM   976  O OD1 A ASP B 1 28 ? 30.324  -4.529  -36.756 0.50 51.81  ? 27  ASP B OD1 1 
ATOM   977  O OD1 B ASP B 1 28 ? 33.168  -6.602  -36.788 0.50 46.13  ? 27  ASP B OD1 1 
ATOM   978  O OD2 A ASP B 1 28 ? 29.244  -4.182  -34.861 0.50 50.89  ? 27  ASP B OD2 1 
ATOM   979  O OD2 B ASP B 1 28 ? 32.072  -4.944  -37.719 0.50 39.34  ? 27  ASP B OD2 1 
ATOM   980  N N   . VAL B 1 34 ? 37.042  -9.969  -24.995 1.00 78.03  ? 33  VAL B N   1 
ATOM   981  C CA  . VAL B 1 34 ? 36.857  -11.390 -25.414 1.00 71.79  ? 33  VAL B CA  1 
ATOM   982  C C   . VAL B 1 34 ? 36.737  -11.407 -26.935 1.00 81.47  ? 33  VAL B C   1 
ATOM   983  O O   . VAL B 1 34 ? 36.298  -10.424 -27.531 1.00 90.02  ? 33  VAL B O   1 
ATOM   984  C CB  . VAL B 1 34 ? 35.617  -11.975 -24.699 1.00 70.74  ? 33  VAL B CB  1 
ATOM   985  C CG1 . VAL B 1 34 ? 34.311  -11.310 -25.128 1.00 70.78  ? 33  VAL B CG1 1 
ATOM   986  C CG2 . VAL B 1 34 ? 35.521  -13.492 -24.818 1.00 62.40  ? 33  VAL B CG2 1 
ATOM   987  N N   . LYS B 1 35 ? 37.201  -12.496 -27.560 1.00 81.04  ? 34  LYS B N   1 
ATOM   988  C CA  . LYS B 1 35 ? 36.868  -12.795 -28.947 1.00 75.47  ? 34  LYS B CA  1 
ATOM   989  C C   . LYS B 1 35 ? 36.117  -14.131 -28.973 1.00 72.62  ? 34  LYS B C   1 
ATOM   990  O O   . LYS B 1 35 ? 36.324  -14.960 -28.085 1.00 72.18  ? 34  LYS B O   1 
ATOM   991  C CB  . LYS B 1 35 ? 38.113  -12.705 -29.840 1.00 72.54  ? 34  LYS B CB  1 
ATOM   992  N N   . PRO B 1 36 ? 35.190  -14.381 -29.939 1.00 67.49  ? 35  PRO B N   1 
ATOM   993  C CA  . PRO B 1 36 ? 34.403  -15.622 -29.942 1.00 57.69  ? 35  PRO B CA  1 
ATOM   994  C C   . PRO B 1 36 ? 35.285  -16.863 -29.854 1.00 49.35  ? 35  PRO B C   1 
ATOM   995  O O   . PRO B 1 36 ? 36.423  -16.827 -30.300 1.00 54.19  ? 35  PRO B O   1 
ATOM   996  C CB  . PRO B 1 36 ? 33.592  -15.578 -31.255 1.00 56.60  ? 35  PRO B CB  1 
ATOM   997  C CG  . PRO B 1 36 ? 34.192  -14.431 -32.054 1.00 61.37  ? 35  PRO B CG  1 
ATOM   998  C CD  . PRO B 1 36 ? 34.841  -13.485 -31.056 1.00 60.50  ? 35  PRO B CD  1 
ATOM   999  N N   . PRO B 1 37 ? 34.815  -17.988 -29.260 1.00 51.56  ? 36  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 37 ? 35.538  -19.255 -29.351 1.00 49.52  ? 36  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 37 ? 35.621  -19.629 -30.829 1.00 56.00  ? 36  PRO B C   1 
ATOM   1002 O O   . PRO B 1 37 ? 34.843  -19.114 -31.639 1.00 56.51  ? 36  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 37 ? 34.699  -20.282 -28.554 1.00 52.36  ? 36  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 37 ? 33.673  -19.459 -27.789 1.00 52.36  ? 36  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 37 ? 33.579  -18.092 -28.465 1.00 51.77  ? 36  PRO B CD  1 
ATOM   1006 N N   . PRO B 1 38 ? 36.545  -20.539 -31.231 1.00 58.94  ? 37  PRO B N   1 
ATOM   1007 C CA  . PRO B 1 38 ? 36.614  -21.012 -32.623 1.00 52.68  ? 37  PRO B CA  1 
ATOM   1008 C C   . PRO B 1 38 ? 35.270  -21.430 -33.234 1.00 50.95  ? 37  PRO B C   1 
ATOM   1009 O O   . PRO B 1 38 ? 34.481  -22.122 -32.588 1.00 53.91  ? 37  PRO B O   1 
ATOM   1010 C CB  . PRO B 1 38 ? 37.614  -22.199 -32.510 1.00 53.96  ? 37  PRO B CB  1 
ATOM   1011 C CG  . PRO B 1 38 ? 38.544  -21.797 -31.372 1.00 53.30  ? 37  PRO B CG  1 
ATOM   1012 C CD  . PRO B 1 38 ? 37.594  -21.132 -30.374 1.00 61.65  ? 37  PRO B CD  1 
ATOM   1013 N N   . ASN B 1 39 ? 35.009  -20.971 -34.469 1.00 50.68  ? 38  ASN B N   1 
ATOM   1014 C CA  . ASN B 1 39 ? 33.846  -21.381 -35.256 1.00 52.81  ? 38  ASN B CA  1 
ATOM   1015 C C   . ASN B 1 39 ? 32.560  -20.678 -34.814 1.00 43.53  ? 38  ASN B C   1 
ATOM   1016 O O   . ASN B 1 39 ? 31.494  -20.957 -35.356 1.00 45.37  ? 38  ASN B O   1 
ATOM   1017 C CB  . ASN B 1 39 ? 33.629  -22.892 -35.214 1.00 52.58  ? 38  ASN B CB  1 
ATOM   1018 C CG  . ASN B 1 39 ? 34.843  -23.659 -35.692 1.00 59.84  ? 38  ASN B CG  1 
ATOM   1019 O OD1 . ASN B 1 39 ? 35.273  -24.617 -35.036 1.00 61.89  ? 38  ASN B OD1 1 
ATOM   1020 N ND2 . ASN B 1 39 ? 35.408  -23.261 -36.824 1.00 56.02  ? 38  ASN B ND2 1 
ATOM   1021 N N   . LYS B 1 40 ? 32.641  -19.776 -33.827 1.00 47.10  ? 39  LYS B N   1 
ATOM   1022 C CA  . LYS B 1 40 ? 31.450  -19.163 -33.250 1.00 42.69  ? 39  LYS B CA  1 
ATOM   1023 C C   . LYS B 1 40 ? 31.372  -17.678 -33.598 1.00 41.90  ? 39  LYS B C   1 
ATOM   1024 O O   . LYS B 1 40 ? 32.375  -17.056 -33.919 1.00 42.54  ? 39  LYS B O   1 
ATOM   1025 C CB  . LYS B 1 40 ? 31.460  -19.427 -31.741 1.00 43.19  ? 39  LYS B CB  1 
ATOM   1026 C CG  . LYS B 1 40 ? 31.100  -20.861 -31.416 1.00 47.31  ? 39  LYS B CG  1 
ATOM   1027 C CD  . LYS B 1 40 ? 30.949  -21.032 -29.909 1.00 58.49  ? 39  LYS B CD  1 
ATOM   1028 C CE  . LYS B 1 40 ? 29.935  -22.035 -29.461 1.00 67.87  ? 39  LYS B CE  1 
ATOM   1029 N NZ  . LYS B 1 40 ? 30.270  -23.359 -29.976 1.00 68.91  ? 39  LYS B NZ  1 
ATOM   1030 N N   . TYR B 1 41 ? 30.161  -17.120 -33.517 1.00 38.66  ? 40  TYR B N   1 
ATOM   1031 C CA  . TYR B 1 41 ? 29.929  -15.711 -33.789 1.00 37.56  ? 40  TYR B CA  1 
ATOM   1032 C C   . TYR B 1 41 ? 29.354  -15.020 -32.556 1.00 40.50  ? 40  TYR B C   1 
ATOM   1033 O O   . TYR B 1 41 ? 28.590  -15.620 -31.794 1.00 37.86  ? 40  TYR B O   1 
ATOM   1034 C CB  . TYR B 1 41 ? 28.866  -15.566 -34.877 1.00 37.35  ? 40  TYR B CB  1 
ATOM   1035 C CG  . TYR B 1 41 ? 29.305  -16.036 -36.257 1.00 40.28  ? 40  TYR B CG  1 
ATOM   1036 C CD1 . TYR B 1 41 ? 30.001  -15.184 -37.114 1.00 36.26  ? 40  TYR B CD1 1 
ATOM   1037 C CD2 . TYR B 1 41 ? 29.007  -17.317 -36.708 1.00 36.79  ? 40  TYR B CD2 1 
ATOM   1038 C CE1 . TYR B 1 41 ? 30.407  -15.609 -38.377 1.00 43.64  ? 40  TYR B CE1 1 
ATOM   1039 C CE2 . TYR B 1 41 ? 29.405  -17.754 -37.965 1.00 40.82  ? 40  TYR B CE2 1 
ATOM   1040 C CZ  . TYR B 1 41 ? 30.123  -16.900 -38.799 1.00 44.03  ? 40  TYR B CZ  1 
ATOM   1041 O OH  . TYR B 1 41 ? 30.497  -17.302 -40.062 1.00 43.05  ? 40  TYR B OH  1 
ATOM   1042 N N   . PRO B 1 42 ? 29.626  -13.704 -32.374 1.00 42.77  ? 41  PRO B N   1 
ATOM   1043 C CA  . PRO B 1 42 ? 28.888  -12.912 -31.381 1.00 34.28  ? 41  PRO B CA  1 
ATOM   1044 C C   . PRO B 1 42 ? 27.458  -12.655 -31.841 1.00 35.49  ? 41  PRO B C   1 
ATOM   1045 O O   . PRO B 1 42 ? 27.241  -12.064 -32.908 1.00 38.61  ? 41  PRO B O   1 
ATOM   1046 C CB  . PRO B 1 42 ? 29.709  -11.606 -31.222 1.00 37.97  ? 41  PRO B CB  1 
ATOM   1047 C CG  . PRO B 1 42 ? 30.603  -11.538 -32.457 1.00 38.83  ? 41  PRO B CG  1 
ATOM   1048 C CD  . PRO B 1 42 ? 30.605  -12.909 -33.151 1.00 41.24  ? 41  PRO B CD  1 
ATOM   1049 N N   . ILE B 1 43 ? 26.492  -13.107 -31.019 1.00 33.93  ? 42  ILE B N   1 
ATOM   1050 C CA  . ILE B 1 43 ? 25.066  -12.947 -31.299 1.00 31.80  ? 42  ILE B CA  1 
ATOM   1051 C C   . ILE B 1 43 ? 24.480  -11.897 -30.359 1.00 29.20  ? 42  ILE B C   1 
ATOM   1052 O O   . ILE B 1 43 ? 24.813  -11.899 -29.190 1.00 33.84  ? 42  ILE B O   1 
ATOM   1053 C CB  . ILE B 1 43 ? 24.328  -14.284 -31.120 1.00 31.61  ? 42  ILE B CB  1 
ATOM   1054 C CG1 . ILE B 1 43 ? 25.075  -15.438 -31.840 1.00 34.38  ? 42  ILE B CG1 1 
ATOM   1055 C CG2 . ILE B 1 43 ? 22.868  -14.189 -31.586 1.00 32.27  ? 42  ILE B CG2 1 
ATOM   1056 C CD1 . ILE B 1 43 ? 25.363  -15.184 -33.312 1.00 32.88  ? 42  ILE B CD1 1 
ATOM   1057 N N   . PHE B 1 44 ? 23.620  -11.032 -30.905 1.00 30.01  ? 43  PHE B N   1 
ATOM   1058 C CA  . PHE B 1 44 ? 22.806  -10.115 -30.119 1.00 30.87  ? 43  PHE B CA  1 
ATOM   1059 C C   . PHE B 1 44 ? 21.350  -10.517 -30.305 1.00 31.28  ? 43  PHE B C   1 
ATOM   1060 O O   . PHE B 1 44 ? 20.849  -10.580 -31.423 1.00 30.82  ? 43  PHE B O   1 
ATOM   1061 C CB  . PHE B 1 44 ? 23.097  -8.652  -30.501 1.00 31.50  ? 43  PHE B CB  1 
ATOM   1062 C CG  . PHE B 1 44 ? 22.147  -7.628  -29.877 1.00 32.53  ? 43  PHE B CG  1 
ATOM   1063 C CD1 . PHE B 1 44 ? 20.957  -7.254  -30.504 1.00 31.06  ? 43  PHE B CD1 1 
ATOM   1064 C CD2 . PHE B 1 44 ? 22.433  -7.057  -28.645 1.00 36.46  ? 43  PHE B CD2 1 
ATOM   1065 C CE1 . PHE B 1 44 ? 20.096  -6.323  -29.933 1.00 33.06  ? 43  PHE B CE1 1 
ATOM   1066 C CE2 . PHE B 1 44 ? 21.564  -6.132  -28.067 1.00 33.10  ? 43  PHE B CE2 1 
ATOM   1067 C CZ  . PHE B 1 44 ? 20.404  -5.769  -28.711 1.00 39.22  ? 43  PHE B CZ  1 
ATOM   1068 N N   . PHE B 1 45 ? 20.662  -10.798 -29.185 1.00 31.72  ? 44  PHE B N   1 
ATOM   1069 C CA  . PHE B 1 45 ? 19.279  -11.226 -29.195 1.00 31.10  ? 44  PHE B CA  1 
ATOM   1070 C C   . PHE B 1 45 ? 18.408  -9.993  -29.046 1.00 29.35  ? 44  PHE B C   1 
ATOM   1071 O O   . PHE B 1 45 ? 18.539  -9.254  -28.066 1.00 32.71  ? 44  PHE B O   1 
ATOM   1072 C CB  . PHE B 1 45 ? 19.063  -12.198 -28.017 1.00 30.70  ? 44  PHE B CB  1 
ATOM   1073 C CG  . PHE B 1 45 ? 19.798  -13.524 -28.183 1.00 28.27  ? 44  PHE B CG  1 
ATOM   1074 C CD1 . PHE B 1 45 ? 21.111  -13.687 -27.776 1.00 33.58  ? 44  PHE B CD1 1 
ATOM   1075 C CD2 . PHE B 1 45 ? 19.163  -14.619 -28.773 1.00 29.57  ? 44  PHE B CD2 1 
ATOM   1076 C CE1 . PHE B 1 45 ? 21.775  -14.892 -27.971 1.00 37.31  ? 44  PHE B CE1 1 
ATOM   1077 C CE2 . PHE B 1 45 ? 19.817  -15.844 -28.909 1.00 32.67  ? 44  PHE B CE2 1 
ATOM   1078 C CZ  . PHE B 1 45 ? 21.136  -15.967 -28.553 1.00 31.92  ? 44  PHE B CZ  1 
ATOM   1079 N N   . PHE B 1 46 ? 17.551  -9.778  -30.044 1.00 29.38  ? 45  PHE B N   1 
ATOM   1080 C CA  . PHE B 1 46 ? 16.637  -8.664  -29.994 1.00 30.29  ? 45  PHE B CA  1 
ATOM   1081 C C   . PHE B 1 46 ? 15.644  -8.867  -28.842 1.00 33.31  ? 45  PHE B C   1 
ATOM   1082 O O   . PHE B 1 46 ? 15.337  -9.996  -28.436 1.00 32.56  ? 45  PHE B O   1 
ATOM   1083 C CB  . PHE B 1 46 ? 15.893  -8.480  -31.308 1.00 27.48  ? 45  PHE B CB  1 
ATOM   1084 C CG  . PHE B 1 46 ? 16.821  -8.034  -32.429 1.00 32.80  ? 45  PHE B CG  1 
ATOM   1085 C CD1 . PHE B 1 46 ? 17.332  -6.729  -32.435 1.00 35.76  ? 45  PHE B CD1 1 
ATOM   1086 C CD2 . PHE B 1 46 ? 17.147  -8.893  -33.488 1.00 33.14  ? 45  PHE B CD2 1 
ATOM   1087 C CE1 . PHE B 1 46 ? 18.175  -6.292  -33.461 1.00 33.98  ? 45  PHE B CE1 1 
ATOM   1088 C CE2 . PHE B 1 46 ? 17.975  -8.440  -34.524 1.00 33.27  ? 45  PHE B CE2 1 
ATOM   1089 C CZ  . PHE B 1 46 ? 18.480  -7.146  -34.499 1.00 33.07  ? 45  PHE B CZ  1 
ATOM   1090 N N   . GLY B 1 47 ? 15.124  -7.743  -28.334 1.00 34.23  ? 46  GLY B N   1 
ATOM   1091 C CA  . GLY B 1 47 ? 14.092  -7.806  -27.312 1.00 32.25  ? 46  GLY B CA  1 
ATOM   1092 C C   . GLY B 1 47 ? 14.730  -7.910  -25.933 1.00 32.54  ? 46  GLY B C   1 
ATOM   1093 O O   . GLY B 1 47 ? 14.599  -6.994  -25.130 1.00 34.62  ? 46  GLY B O   1 
ATOM   1094 N N   . THR B 1 48 ? 15.455  -8.999  -25.665 1.00 34.08  ? 47  THR B N   1 
ATOM   1095 C CA  . THR B 1 48 ? 16.136  -9.177  -24.397 1.00 34.60  ? 47  THR B CA  1 
ATOM   1096 C C   . THR B 1 48 ? 17.414  -8.351  -24.368 1.00 37.23  ? 47  THR B C   1 
ATOM   1097 O O   . THR B 1 48 ? 17.925  -8.038  -23.297 1.00 35.44  ? 47  THR B O   1 
ATOM   1098 C CB  . THR B 1 48 ? 16.427  -10.657 -24.108 1.00 35.23  ? 47  THR B CB  1 
ATOM   1099 O OG1 . THR B 1 48 ? 17.401  -11.143 -25.030 1.00 33.22  ? 47  THR B OG1 1 
ATOM   1100 C CG2 . THR B 1 48 ? 15.150  -11.480 -24.045 1.00 31.70  ? 47  THR B CG2 1 
ATOM   1101 N N   . HIS B 1 49 ? 17.966  -8.110  -25.558 1.00 33.11  ? 48  HIS B N   1 
ATOM   1102 C CA  . HIS B 1 49 ? 19.252  -7.461  -25.715 1.00 38.18  ? 48  HIS B CA  1 
ATOM   1103 C C   . HIS B 1 49 ? 20.347  -8.258  -25.026 1.00 36.48  ? 48  HIS B C   1 
ATOM   1104 O O   . HIS B 1 49 ? 21.361  -7.678  -24.651 1.00 41.11  ? 48  HIS B O   1 
ATOM   1105 C CB  . HIS B 1 49 ? 19.211  -5.997  -25.254 1.00 33.48  ? 48  HIS B CB  1 
ATOM   1106 C CG  . HIS B 1 49 ? 18.040  -5.271  -25.802 1.00 36.51  ? 48  HIS B CG  1 
ATOM   1107 N ND1 . HIS B 1 49 ? 17.382  -4.318  -25.062 1.00 39.77  ? 48  HIS B ND1 1 
ATOM   1108 C CD2 . HIS B 1 49 ? 17.362  -5.358  -26.970 1.00 32.99  ? 48  HIS B CD2 1 
ATOM   1109 C CE1 . HIS B 1 49 ? 16.343  -3.864  -25.762 1.00 43.33  ? 48  HIS B CE1 1 
ATOM   1110 N NE2 . HIS B 1 49 ? 16.330  -4.463  -26.941 1.00 40.24  ? 48  HIS B NE2 1 
ATOM   1111 N N   . GLU B 1 50 ? 20.170  -9.573  -24.866 1.00 35.49  ? 49  GLU B N   1 
ATOM   1112 C CA  . GLU B 1 50 ? 21.263  -10.385 -24.343 1.00 35.99  ? 49  GLU B CA  1 
ATOM   1113 C C   . GLU B 1 50 ? 22.225  -10.742 -25.486 1.00 37.42  ? 49  GLU B C   1 
ATOM   1114 O O   . GLU B 1 50 ? 21.927  -10.517 -26.669 1.00 36.69  ? 49  GLU B O   1 
ATOM   1115 C CB  . GLU B 1 50 ? 20.784  -11.702 -23.729 1.00 42.44  ? 49  GLU B CB  1 
ATOM   1116 C CG  . GLU B 1 50 ? 19.952  -11.500 -22.462 1.00 44.79  ? 49  GLU B CG  1 
ATOM   1117 C CD  . GLU B 1 50 ? 19.316  -12.759 -21.888 1.00 56.02  ? 49  GLU B CD  1 
ATOM   1118 O OE1 . GLU B 1 50 ? 18.503  -13.400 -22.584 1.00 65.09  ? 49  GLU B OE1 1 
ATOM   1119 O OE2 . GLU B 1 50 ? 19.610  -13.105 -20.731 1.00 59.82  ? 49  GLU B OE2 1 
ATOM   1120 N N   . THR B 1 51 ? 23.362  -11.310 -25.111 1.00 34.12  ? 50  THR B N   1 
ATOM   1121 C CA  . THR B 1 51 ? 24.390  -11.745 -26.053 1.00 36.79  ? 50  THR B CA  1 
ATOM   1122 C C   . THR B 1 51 ? 24.826  -13.168 -25.703 1.00 40.03  ? 50  THR B C   1 
ATOM   1123 O O   . THR B 1 51 ? 24.673  -13.618 -24.564 1.00 39.32  ? 50  THR B O   1 
ATOM   1124 C CB  . THR B 1 51 ? 25.570  -10.764 -26.120 1.00 41.44  ? 50  THR B CB  1 
ATOM   1125 O OG1 . THR B 1 51 ? 26.160  -10.730 -24.828 1.00 41.65  ? 50  THR B OG1 1 
ATOM   1126 C CG2 . THR B 1 51 ? 25.182  -9.327  -26.427 1.00 38.34  ? 50  THR B CG2 1 
ATOM   1127 N N   . ALA B 1 52 ? 25.348  -13.897 -26.707 1.00 38.07  ? 51  ALA B N   1 
ATOM   1128 C CA  . ALA B 1 52 ? 25.990  -15.182 -26.500 1.00 37.39  ? 51  ALA B CA  1 
ATOM   1129 C C   . ALA B 1 52 ? 26.883  -15.461 -27.703 1.00 37.08  ? 51  ALA B C   1 
ATOM   1130 O O   . ALA B 1 52 ? 26.892  -14.684 -28.663 1.00 37.99  ? 51  ALA B O   1 
ATOM   1131 C CB  . ALA B 1 52 ? 24.975  -16.283 -26.272 1.00 34.42  ? 51  ALA B CB  1 
ATOM   1132 N N   . PHE B 1 53 ? 27.689  -16.519 -27.597 1.00 36.18  ? 52  PHE B N   1 
ATOM   1133 C CA  . PHE B 1 53 ? 28.456  -16.962 -28.751 1.00 38.45  ? 52  PHE B CA  1 
ATOM   1134 C C   . PHE B 1 53 ? 27.812  -18.239 -29.303 1.00 35.93  ? 52  PHE B C   1 
ATOM   1135 O O   . PHE B 1 53 ? 27.608  -19.193 -28.560 1.00 40.02  ? 52  PHE B O   1 
ATOM   1136 C CB  . PHE B 1 53 ? 29.912  -17.199 -28.332 1.00 38.58  ? 52  PHE B CB  1 
ATOM   1137 C CG  . PHE B 1 53 ? 30.704  -15.955 -27.956 1.00 45.15  ? 52  PHE B CG  1 
ATOM   1138 C CD1 . PHE B 1 53 ? 30.974  -14.973 -28.901 1.00 48.36  ? 52  PHE B CD1 1 
ATOM   1139 C CD2 . PHE B 1 53 ? 31.202  -15.792 -26.668 1.00 48.41  ? 52  PHE B CD2 1 
ATOM   1140 C CE1 . PHE B 1 53 ? 31.693  -13.833 -28.564 1.00 45.36  ? 52  PHE B CE1 1 
ATOM   1141 C CE2 . PHE B 1 53 ? 31.920  -14.654 -26.326 1.00 46.71  ? 52  PHE B CE2 1 
ATOM   1142 C CZ  . PHE B 1 53 ? 32.165  -13.680 -27.271 1.00 43.00  ? 52  PHE B CZ  1 
ATOM   1143 N N   . LEU B 1 54 ? 27.503  -18.271 -30.611 1.00 35.77  ? 53  LEU B N   1 
ATOM   1144 C CA  . LEU B 1 54 ? 26.897  -19.456 -31.209 1.00 36.01  ? 53  LEU B CA  1 
ATOM   1145 C C   . LEU B 1 54 ? 27.629  -19.809 -32.512 1.00 36.43  ? 53  LEU B C   1 
ATOM   1146 O O   . LEU B 1 54 ? 28.153  -18.922 -33.207 1.00 34.68  ? 53  LEU B O   1 
ATOM   1147 C CB  . LEU B 1 54 ? 25.397  -19.299 -31.480 1.00 34.42  ? 53  LEU B CB  1 
ATOM   1148 C CG  . LEU B 1 54 ? 24.444  -19.215 -30.284 1.00 34.48  ? 53  LEU B CG  1 
ATOM   1149 C CD1 . LEU B 1 54 ? 23.062  -18.835 -30.764 1.00 34.79  ? 53  LEU B CD1 1 
ATOM   1150 C CD2 . LEU B 1 54 ? 24.420  -20.554 -29.562 1.00 37.25  ? 53  LEU B CD2 1 
ATOM   1151 N N   . GLY B 1 55 ? 27.607  -21.110 -32.836 1.00 37.71  ? 54  GLY B N   1 
ATOM   1152 C CA  . GLY B 1 55 ? 28.082  -21.646 -34.101 1.00 32.42  ? 54  GLY B CA  1 
ATOM   1153 C C   . GLY B 1 55 ? 26.960  -21.722 -35.140 1.00 33.65  ? 54  GLY B C   1 
ATOM   1154 O O   . GLY B 1 55 ? 25.768  -21.636 -34.811 1.00 34.52  ? 54  GLY B O   1 
ATOM   1155 N N   . PRO B 1 56 ? 27.303  -21.919 -36.438 1.00 31.81  ? 55  PRO B N   1 
ATOM   1156 C CA  . PRO B 1 56 ? 26.312  -21.967 -37.504 1.00 31.58  ? 55  PRO B CA  1 
ATOM   1157 C C   . PRO B 1 56 ? 25.144  -22.921 -37.332 1.00 30.80  ? 55  PRO B C   1 
ATOM   1158 O O   . PRO B 1 56 ? 24.097  -22.667 -37.886 1.00 30.19  ? 55  PRO B O   1 
ATOM   1159 C CB  . PRO B 1 56 ? 27.116  -22.361 -38.743 1.00 37.17  ? 55  PRO B CB  1 
ATOM   1160 C CG  . PRO B 1 56 ? 28.523  -22.008 -38.431 1.00 34.55  ? 55  PRO B CG  1 
ATOM   1161 C CD  . PRO B 1 56 ? 28.678  -22.093 -36.937 1.00 35.38  ? 55  PRO B CD  1 
ATOM   1162 N N   . LYS B 1 57 ? 25.324  -24.042 -36.622 1.00 34.11  ? 56  LYS B N   1 
ATOM   1163 C CA  . LYS B 1 57 ? 24.245  -25.023 -36.575 1.00 35.12  ? 56  LYS B CA  1 
ATOM   1164 C C   . LYS B 1 57 ? 23.022  -24.391 -35.911 1.00 32.44  ? 56  LYS B C   1 
ATOM   1165 O O   . LYS B 1 57 ? 21.900  -24.849 -36.112 1.00 31.66  ? 56  LYS B O   1 
ATOM   1166 C CB  . LYS B 1 57 ? 24.660  -26.297 -35.825 1.00 38.43  ? 56  LYS B CB  1 
ATOM   1167 C CG  . LYS B 1 57 ? 24.806  -26.187 -34.317 1.00 41.78  ? 56  LYS B CG  1 
ATOM   1168 C CD  . LYS B 1 57 ? 24.904  -27.574 -33.687 1.00 44.13  ? 56  LYS B CD  1 
ATOM   1169 C CE  . LYS B 1 57 ? 25.294  -27.568 -32.222 1.00 47.22  ? 56  LYS B CE  1 
ATOM   1170 N NZ  . LYS B 1 57 ? 24.246  -26.987 -31.377 1.00 47.63  ? 56  LYS B NZ  1 
ATOM   1171 N N   . ASP B 1 58 ? 23.260  -23.320 -35.137 1.00 30.84  ? 57  ASP B N   1 
ATOM   1172 C CA  . ASP B 1 58 ? 22.210  -22.705 -34.342 1.00 30.23  ? 57  ASP B CA  1 
ATOM   1173 C C   . ASP B 1 58 ? 21.749  -21.377 -34.936 1.00 29.11  ? 57  ASP B C   1 
ATOM   1174 O O   . ASP B 1 58 ? 20.963  -20.661 -34.287 1.00 30.28  ? 57  ASP B O   1 
ATOM   1175 C CB  . ASP B 1 58 ? 22.645  -22.589 -32.892 1.00 30.93  ? 57  ASP B CB  1 
ATOM   1176 C CG  . ASP B 1 58 ? 22.808  -23.924 -32.172 1.00 38.35  ? 57  ASP B CG  1 
ATOM   1177 O OD1 . ASP B 1 58 ? 21.894  -24.753 -32.312 1.00 35.50  ? 57  ASP B OD1 1 
ATOM   1178 O OD2 . ASP B 1 58 ? 23.812  -24.080 -31.448 1.00 40.67  ? 57  ASP B OD2 1 
ATOM   1179 N N   . LEU B 1 59 ? 22.211  -21.082 -36.167 1.00 30.05  ? 58  LEU B N   1 
ATOM   1180 C CA  . LEU B 1 59 ? 21.980  -19.794 -36.807 1.00 28.85  ? 58  LEU B CA  1 
ATOM   1181 C C   . LEU B 1 59 ? 21.223  -19.969 -38.117 1.00 29.16  ? 58  LEU B C   1 
ATOM   1182 O O   . LEU B 1 59 ? 21.714  -20.628 -39.035 1.00 30.65  ? 58  LEU B O   1 
ATOM   1183 C CB  . LEU B 1 59 ? 23.277  -19.011 -37.009 1.00 29.46  ? 58  LEU B CB  1 
ATOM   1184 C CG  . LEU B 1 59 ? 24.098  -18.746 -35.744 1.00 29.74  ? 58  LEU B CG  1 
ATOM   1185 C CD1 . LEU B 1 59 ? 25.379  -18.022 -36.085 1.00 35.68  ? 58  LEU B CD1 1 
ATOM   1186 C CD2 . LEU B 1 59 ? 23.319  -17.954 -34.693 1.00 31.55  ? 58  LEU B CD2 1 
ATOM   1187 N N   . PHE B 1 60 ? 20.033  -19.371 -38.172 1.00 27.84  ? 59  PHE B N   1 
ATOM   1188 C CA  . PHE B 1 60 ? 19.086  -19.519 -39.259 1.00 29.39  ? 59  PHE B CA  1 
ATOM   1189 C C   . PHE B 1 60 ? 18.898  -18.154 -39.933 1.00 30.66  ? 59  PHE B C   1 
ATOM   1190 O O   . PHE B 1 60 ? 18.280  -17.245 -39.376 1.00 28.95  ? 59  PHE B O   1 
ATOM   1191 C CB  . PHE B 1 60 ? 17.759  -20.058 -38.705 1.00 27.96  ? 59  PHE B CB  1 
ATOM   1192 C CG  . PHE B 1 60 ? 17.881  -21.466 -38.118 1.00 26.20  ? 59  PHE B CG  1 
ATOM   1193 C CD1 . PHE B 1 60 ? 18.441  -21.656 -36.855 1.00 28.17  ? 59  PHE B CD1 1 
ATOM   1194 C CD2 . PHE B 1 60 ? 17.447  -22.576 -38.839 1.00 31.82  ? 59  PHE B CD2 1 
ATOM   1195 C CE1 . PHE B 1 60 ? 18.613  -22.933 -36.323 1.00 32.04  ? 59  PHE B CE1 1 
ATOM   1196 C CE2 . PHE B 1 60 ? 17.584  -23.858 -38.298 1.00 34.84  ? 59  PHE B CE2 1 
ATOM   1197 C CZ  . PHE B 1 60 ? 18.195  -24.037 -37.059 1.00 33.81  ? 59  PHE B CZ  1 
ATOM   1198 N N   . PRO B 1 61 ? 19.431  -17.936 -41.158 1.00 36.99  ? 60  PRO B N   1 
ATOM   1199 C CA  . PRO B 1 61 ? 19.152  -16.680 -41.871 1.00 35.35  ? 60  PRO B CA  1 
ATOM   1200 C C   . PRO B 1 61 ? 17.699  -16.211 -41.772 1.00 32.38  ? 60  PRO B C   1 
ATOM   1201 O O   . PRO B 1 61 ? 16.758  -16.957 -42.041 1.00 33.70  ? 60  PRO B O   1 
ATOM   1202 C CB  . PRO B 1 61 ? 19.615  -17.005 -43.307 1.00 33.41  ? 60  PRO B CB  1 
ATOM   1203 C CG  . PRO B 1 61 ? 20.775  -17.971 -43.092 1.00 43.43  ? 60  PRO B CG  1 
ATOM   1204 C CD  . PRO B 1 61 ? 20.372  -18.827 -41.870 1.00 37.86  ? 60  PRO B CD  1 
ATOM   1205 N N   . TYR B 1 62 ? 17.511  -14.915 -41.458 1.00 34.38  ? 61  TYR B N   1 
ATOM   1206 C CA  . TYR B 1 62 ? 16.201  -14.371 -41.149 1.00 33.29  ? 61  TYR B CA  1 
ATOM   1207 C C   . TYR B 1 62 ? 15.235  -14.433 -42.317 1.00 37.06  ? 61  TYR B C   1 
ATOM   1208 O O   . TYR B 1 62 ? 14.084  -14.829 -42.125 1.00 38.47  ? 61  TYR B O   1 
ATOM   1209 C CB  . TYR B 1 62 ? 16.381  -12.925 -40.678 1.00 35.51  ? 61  TYR B CB  1 
ATOM   1210 C CG  . TYR B 1 62 ? 15.056  -12.238 -40.405 1.00 34.88  ? 61  TYR B CG  1 
ATOM   1211 C CD1 . TYR B 1 62 ? 14.363  -12.457 -39.226 1.00 33.89  ? 61  TYR B CD1 1 
ATOM   1212 C CD2 . TYR B 1 62 ? 14.533  -11.339 -41.326 1.00 39.36  ? 61  TYR B CD2 1 
ATOM   1213 C CE1 . TYR B 1 62 ? 13.171  -11.798 -38.978 1.00 38.36  ? 61  TYR B CE1 1 
ATOM   1214 C CE2 . TYR B 1 62 ? 13.342  -10.677 -41.093 1.00 42.49  ? 61  TYR B CE2 1 
ATOM   1215 C CZ  . TYR B 1 62 ? 12.667  -10.907 -39.910 1.00 40.80  ? 61  TYR B CZ  1 
ATOM   1216 O OH  . TYR B 1 62 ? 11.494  -10.249 -39.714 1.00 45.18  ? 61  TYR B OH  1 
ATOM   1217 N N   . ASP B 1 63 ? 15.724  -14.071 -43.519 1.00 41.51  ? 62  ASP B N   1 
ATOM   1218 C CA  . ASP B 1 63 ? 14.888  -14.021 -44.713 1.00 44.53  ? 62  ASP B CA  1 
ATOM   1219 C C   . ASP B 1 63 ? 14.289  -15.397 -44.998 1.00 36.85  ? 62  ASP B C   1 
ATOM   1220 O O   . ASP B 1 63 ? 13.077  -15.533 -45.132 1.00 45.75  ? 62  ASP B O   1 
ATOM   1221 C CB  . ASP B 1 63 ? 15.636  -13.436 -45.901 1.00 54.03  ? 62  ASP B CB  1 
ATOM   1222 C CG  . ASP B 1 63 ? 15.439  -11.943 -46.109 1.00 66.84  ? 62  ASP B CG  1 
ATOM   1223 O OD1 . ASP B 1 63 ? 14.798  -11.311 -45.237 1.00 68.05  ? 62  ASP B OD1 1 
ATOM   1224 O OD2 . ASP B 1 63 ? 15.894  -11.431 -47.157 1.00 74.93  ? 62  ASP B OD2 1 
ATOM   1225 N N   . LYS B 1 64 ? 15.157  -16.407 -45.029 1.00 39.75  ? 63  LYS B N   1 
ATOM   1226 C CA  . LYS B 1 64 ? 14.744  -17.768 -45.294 1.00 42.06  ? 63  LYS B CA  1 
ATOM   1227 C C   . LYS B 1 64 ? 13.723  -18.239 -44.259 1.00 41.95  ? 63  LYS B C   1 
ATOM   1228 O O   . LYS B 1 64 ? 12.773  -18.945 -44.593 1.00 43.32  ? 63  LYS B O   1 
ATOM   1229 C CB  . LYS B 1 64 ? 15.990  -18.659 -45.263 1.00 45.64  ? 63  LYS B CB  1 
ATOM   1230 C CG  . LYS B 1 64 ? 15.708  -20.061 -45.766 1.00 44.78  ? 63  LYS B CG  1 
ATOM   1231 C CD  . LYS B 1 64 ? 16.839  -21.050 -45.528 1.00 53.56  ? 63  LYS B CD  1 
ATOM   1232 C CE  . LYS B 1 64 ? 16.709  -22.370 -46.256 1.00 47.04  ? 63  LYS B CE  1 
ATOM   1233 N NZ  . LYS B 1 64 ? 15.356  -22.904 -46.421 1.00 47.41  ? 63  LYS B NZ  1 
ATOM   1234 N N   . SER B 1 65 ? 13.912  -17.855 -42.994 1.00 44.43  ? 64  SER B N   1 
ATOM   1235 C CA  . SER B 1 65 ? 13.220  -18.588 -41.930 1.00 42.01  ? 64  SER B CA  1 
ATOM   1236 C C   . SER B 1 65 ? 12.118  -17.790 -41.213 1.00 41.66  ? 64  SER B C   1 
ATOM   1237 O O   . SER B 1 65 ? 11.482  -18.315 -40.295 1.00 40.90  ? 64  SER B O   1 
ATOM   1238 C CB  . SER B 1 65 ? 14.219  -19.184 -40.984 1.00 40.30  ? 64  SER B CB  1 
ATOM   1239 O OG  . SER B 1 65 ? 15.106  -18.169 -40.552 1.00 52.58  ? 64  SER B OG  1 
ATOM   1240 N N   . LYS B 1 66 ? 11.816  -16.563 -41.670 1.00 40.00  ? 65  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 66 ? 10.959  -15.678 -40.879 1.00 38.84  ? 65  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 66 ? 9.512   -16.168 -40.765 1.00 44.18  ? 65  LYS B C   1 
ATOM   1243 O O   . LYS B 1 66 ? 8.850   -15.896 -39.769 1.00 45.33  ? 65  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 66 ? 11.016  -14.189 -41.262 1.00 40.70  ? 65  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 66 ? 10.511  -13.837 -42.660 1.00 43.01  ? 65  LYS B CG  1 
ATOM   1246 N N   . ASP B 1 67 ? 8.970   -16.866 -41.764 1.00 40.76  ? 66  ASP B N   1 
ATOM   1247 C CA  . ASP B 1 67 ? 7.551   -17.159 -41.637 1.00 49.26  ? 66  ASP B CA  1 
ATOM   1248 C C   . ASP B 1 67 ? 7.350   -18.409 -40.780 1.00 49.05  ? 66  ASP B C   1 
ATOM   1249 O O   . ASP B 1 67 ? 6.279   -18.602 -40.191 1.00 50.48  ? 66  ASP B O   1 
ATOM   1250 C CB  . ASP B 1 67 ? 6.825   -17.037 -42.967 1.00 62.34  ? 66  ASP B CB  1 
ATOM   1251 C CG  . ASP B 1 67 ? 7.488   -17.783 -44.109 1.00 70.30  ? 66  ASP B CG  1 
ATOM   1252 O OD1 . ASP B 1 67 ? 8.237   -18.733 -43.807 1.00 75.19  ? 66  ASP B OD1 1 
ATOM   1253 O OD2 . ASP B 1 67 ? 7.286   -17.380 -45.279 1.00 75.25  ? 66  ASP B OD2 1 
ATOM   1254 N N   . LYS B 1 68 ? 8.419   -19.203 -40.670 1.00 43.76  ? 67  LYS B N   1 
ATOM   1255 C CA  . LYS B 1 68 ? 8.497   -20.353 -39.787 1.00 39.90  ? 67  LYS B CA  1 
ATOM   1256 C C   . LYS B 1 68 ? 8.742   -19.925 -38.337 1.00 40.13  ? 67  LYS B C   1 
ATOM   1257 O O   . LYS B 1 68 ? 8.020   -20.382 -37.452 1.00 41.21  ? 67  LYS B O   1 
ATOM   1258 C CB  . LYS B 1 68 ? 9.582   -21.284 -40.334 1.00 45.08  ? 67  LYS B CB  1 
ATOM   1259 C CG  . LYS B 1 68 ? 9.802   -22.572 -39.551 1.00 50.82  ? 67  LYS B CG  1 
ATOM   1260 C CD  . LYS B 1 68 ? 10.710  -23.502 -40.349 1.00 63.01  ? 67  LYS B CD  1 
ATOM   1261 C CE  . LYS B 1 68 ? 11.173  -24.698 -39.575 1.00 71.25  ? 67  LYS B CE  1 
ATOM   1262 N NZ  . LYS B 1 68 ? 10.068  -25.590 -39.211 1.00 73.25  ? 67  LYS B NZ  1 
ATOM   1263 N N   . TYR B 1 69 ? 9.750   -19.066 -38.075 1.00 34.25  ? 68  TYR B N   1 
ATOM   1264 C CA  . TYR B 1 69 ? 10.169  -18.803 -36.697 1.00 29.55  ? 68  TYR B CA  1 
ATOM   1265 C C   . TYR B 1 69 ? 9.668   -17.462 -36.177 1.00 37.05  ? 68  TYR B C   1 
ATOM   1266 O O   . TYR B 1 69 ? 9.802   -17.188 -34.976 1.00 35.99  ? 68  TYR B O   1 
ATOM   1267 C CB  . TYR B 1 69 ? 11.687  -18.878 -36.541 1.00 31.65  ? 68  TYR B CB  1 
ATOM   1268 C CG  . TYR B 1 69 ? 12.287  -20.250 -36.838 1.00 31.86  ? 68  TYR B CG  1 
ATOM   1269 C CD1 . TYR B 1 69 ? 11.738  -21.409 -36.289 1.00 34.73  ? 68  TYR B CD1 1 
ATOM   1270 C CD2 . TYR B 1 69 ? 13.389  -20.387 -37.677 1.00 36.89  ? 68  TYR B CD2 1 
ATOM   1271 C CE1 . TYR B 1 69 ? 12.286  -22.661 -36.542 1.00 35.67  ? 68  TYR B CE1 1 
ATOM   1272 C CE2 . TYR B 1 69 ? 13.939  -21.633 -37.949 1.00 41.13  ? 68  TYR B CE2 1 
ATOM   1273 C CZ  . TYR B 1 69 ? 13.376  -22.770 -37.389 1.00 40.18  ? 68  TYR B CZ  1 
ATOM   1274 O OH  . TYR B 1 69 ? 13.904  -23.992 -37.685 1.00 35.76  ? 68  TYR B OH  1 
ATOM   1275 N N   . GLY B 1 70 ? 9.118   -16.631 -37.076 1.00 35.17  ? 69  GLY B N   1 
ATOM   1276 C CA  . GLY B 1 70 ? 8.864   -15.246 -36.714 1.00 41.04  ? 69  GLY B CA  1 
ATOM   1277 C C   . GLY B 1 70 ? 7.441   -15.012 -36.209 1.00 43.21  ? 69  GLY B C   1 
ATOM   1278 O O   . GLY B 1 70 ? 6.877   -13.962 -36.486 1.00 42.28  ? 69  GLY B O   1 
ATOM   1279 N N   . LYS B 1 71 ? 6.881   -15.974 -35.459 1.00 45.38  ? 70  LYS B N   1 
ATOM   1280 C CA  . LYS B 1 71 ? 5.524   -15.876 -34.945 1.00 46.61  ? 70  LYS B CA  1 
ATOM   1281 C C   . LYS B 1 71 ? 5.575   -15.446 -33.487 1.00 47.53  ? 70  LYS B C   1 
ATOM   1282 O O   . LYS B 1 71 ? 6.428   -15.917 -32.737 1.00 43.27  ? 70  LYS B O   1 
ATOM   1283 C CB  . LYS B 1 71 ? 4.793   -17.223 -34.952 1.00 50.15  ? 70  LYS B CB  1 
ATOM   1284 C CG  . LYS B 1 71 ? 3.831   -17.516 -36.104 1.00 64.11  ? 70  LYS B CG  1 
ATOM   1285 C CD  . LYS B 1 71 ? 4.454   -17.673 -37.485 1.00 66.76  ? 70  LYS B CD  1 
ATOM   1286 C CE  . LYS B 1 71 ? 3.450   -17.946 -38.568 1.00 69.06  ? 70  LYS B CE  1 
ATOM   1287 N NZ  . LYS B 1 71 ? 3.948   -17.450 -39.858 1.00 70.30  ? 70  LYS B NZ  1 
ATOM   1288 N N   . PRO B 1 72 ? 4.665   -14.561 -33.025 1.00 46.33  ? 71  PRO B N   1 
ATOM   1289 C CA  . PRO B 1 72 ? 4.677   -14.145 -31.622 1.00 45.83  ? 71  PRO B CA  1 
ATOM   1290 C C   . PRO B 1 72 ? 4.444   -15.349 -30.711 1.00 43.97  ? 71  PRO B C   1 
ATOM   1291 O O   . PRO B 1 72 ? 3.785   -16.310 -31.111 1.00 40.47  ? 71  PRO B O   1 
ATOM   1292 C CB  . PRO B 1 72 ? 3.559   -13.099 -31.503 1.00 47.04  ? 71  PRO B CB  1 
ATOM   1293 C CG  . PRO B 1 72 ? 3.269   -12.705 -32.932 1.00 53.64  ? 71  PRO B CG  1 
ATOM   1294 C CD  . PRO B 1 72 ? 3.607   -13.913 -33.813 1.00 50.28  ? 71  PRO B CD  1 
ATOM   1295 N N   . ASN B 1 73 ? 4.983   -15.264 -29.488 1.00 40.02  ? 72  ASN B N   1 
ATOM   1296 C CA  . ASN B 1 73 ? 4.735   -16.235 -28.431 1.00 40.78  ? 72  ASN B CA  1 
ATOM   1297 C C   . ASN B 1 73 ? 4.696   -15.490 -27.090 1.00 44.99  ? 72  ASN B C   1 
ATOM   1298 O O   . ASN B 1 73 ? 4.738   -14.259 -27.046 1.00 46.43  ? 72  ASN B O   1 
ATOM   1299 C CB  . ASN B 1 73 ? 5.750   -17.377 -28.448 1.00 40.46  ? 72  ASN B CB  1 
ATOM   1300 C CG  . ASN B 1 73 ? 7.165   -16.903 -28.213 1.00 40.73  ? 72  ASN B CG  1 
ATOM   1301 O OD1 . ASN B 1 73 ? 7.413   -16.114 -27.290 1.00 39.03  ? 72  ASN B OD1 1 
ATOM   1302 N ND2 . ASN B 1 73 ? 8.107   -17.351 -29.044 1.00 36.49  ? 72  ASN B ND2 1 
ATOM   1303 N N   . LYS B 1 74 ? 4.670   -16.249 -25.995 1.00 44.05  ? 73  LYS B N   1 
ATOM   1304 C CA  . LYS B 1 74 ? 4.495   -15.697 -24.655 1.00 50.68  ? 73  LYS B CA  1 
ATOM   1305 C C   . LYS B 1 74 ? 5.830   -15.636 -23.890 1.00 47.45  ? 73  LYS B C   1 
ATOM   1306 O O   . LYS B 1 74 ? 5.834   -15.471 -22.671 1.00 46.66  ? 73  LYS B O   1 
ATOM   1307 C CB  . LYS B 1 74 ? 3.373   -16.484 -23.950 1.00 45.05  ? 73  LYS B CB  1 
ATOM   1308 N N   . ARG B 1 75 ? 6.977   -15.776 -24.578 1.00 34.99  ? 74  ARG B N   1 
ATOM   1309 C CA  . ARG B 1 75 ? 8.255   -15.610 -23.900 1.00 35.46  ? 74  ARG B CA  1 
ATOM   1310 C C   . ARG B 1 75 ? 8.555   -14.111 -23.731 1.00 38.91  ? 74  ARG B C   1 
ATOM   1311 O O   . ARG B 1 75 ? 8.351   -13.302 -24.649 1.00 40.41  ? 74  ARG B O   1 
ATOM   1312 C CB  . ARG B 1 75 ? 9.406   -16.406 -24.537 1.00 35.87  ? 74  ARG B CB  1 
ATOM   1313 C CG  . ARG B 1 75 ? 9.322   -17.918 -24.719 1.00 36.01  ? 74  ARG B CG  1 
ATOM   1314 C CD  . ARG B 1 75 ? 9.158   -18.756 -23.460 1.00 36.07  ? 74  ARG B CD  1 
ATOM   1315 N NE  . ARG B 1 75 ? 9.408   -20.180 -23.712 1.00 38.39  ? 74  ARG B NE  1 
ATOM   1316 C CZ  . ARG B 1 75 ? 10.545  -20.801 -23.514 1.00 39.28  ? 74  ARG B CZ  1 
ATOM   1317 N NH1 . ARG B 1 75 ? 11.593  -20.167 -23.007 1.00 46.75  ? 74  ARG B NH1 1 
ATOM   1318 N NH2 . ARG B 1 75 ? 10.661  -22.054 -23.903 1.00 40.62  ? 74  ARG B NH2 1 
ATOM   1319 N N   . LYS B 1 76 ? 9.021   -13.736 -22.533 1.00 36.16  ? 75  LYS B N   1 
ATOM   1320 C CA  . LYS B 1 76 ? 9.418   -12.373 -22.200 1.00 33.36  ? 75  LYS B CA  1 
ATOM   1321 C C   . LYS B 1 76 ? 10.530  -11.868 -23.132 1.00 31.67  ? 75  LYS B C   1 
ATOM   1322 O O   . LYS B 1 76 ? 11.644  -12.411 -23.161 1.00 30.75  ? 75  LYS B O   1 
ATOM   1323 C CB  . LYS B 1 76 ? 9.998   -12.291 -20.775 1.00 35.27  ? 75  LYS B CB  1 
ATOM   1324 C CG  . LYS B 1 76 ? 10.337  -10.873 -20.318 1.00 36.31  ? 75  LYS B CG  1 
ATOM   1325 C CD  . LYS B 1 76 ? 10.758  -10.731 -18.859 1.00 39.30  ? 75  LYS B CD  1 
ATOM   1326 C CE  . LYS B 1 76 ? 11.112  -9.321  -18.445 1.00 46.17  ? 75  LYS B CE  1 
ATOM   1327 N NZ  . LYS B 1 76 ? 11.557  -9.298  -17.041 1.00 52.25  ? 75  LYS B NZ  1 
ATOM   1328 N N   . GLY B 1 77 ? 10.195  -10.810 -23.859 1.00 29.14  ? 76  GLY B N   1 
ATOM   1329 C CA  . GLY B 1 77 ? 11.170  -10.139 -24.712 1.00 32.32  ? 76  GLY B CA  1 
ATOM   1330 C C   . GLY B 1 77 ? 11.043  -10.579 -26.170 1.00 30.88  ? 76  GLY B C   1 
ATOM   1331 O O   . GLY B 1 77 ? 11.579  -9.927  -27.049 1.00 32.09  ? 76  GLY B O   1 
ATOM   1332 N N   . PHE B 1 78 ? 10.317  -11.674 -26.433 1.00 30.93  ? 77  PHE B N   1 
ATOM   1333 C CA  . PHE B 1 78 ? 10.230  -12.193 -27.805 1.00 28.29  ? 77  PHE B CA  1 
ATOM   1334 C C   . PHE B 1 78 ? 9.482   -11.258 -28.753 1.00 31.24  ? 77  PHE B C   1 
ATOM   1335 O O   . PHE B 1 78 ? 9.956   -10.999 -29.861 1.00 29.77  ? 77  PHE B O   1 
ATOM   1336 C CB  . PHE B 1 78 ? 9.491   -13.531 -27.841 1.00 31.61  ? 77  PHE B CB  1 
ATOM   1337 C CG  . PHE B 1 78 ? 9.784   -14.293 -29.125 1.00 30.88  ? 77  PHE B CG  1 
ATOM   1338 C CD1 . PHE B 1 78 ? 10.879  -15.139 -29.192 1.00 28.18  ? 77  PHE B CD1 1 
ATOM   1339 C CD2 . PHE B 1 78 ? 8.932   -14.199 -30.218 1.00 35.27  ? 77  PHE B CD2 1 
ATOM   1340 C CE1 . PHE B 1 78 ? 11.143  -15.846 -30.359 1.00 29.96  ? 77  PHE B CE1 1 
ATOM   1341 C CE2 . PHE B 1 78 ? 9.197   -14.910 -31.379 1.00 33.14  ? 77  PHE B CE2 1 
ATOM   1342 C CZ  . PHE B 1 78 ? 10.302  -15.745 -31.430 1.00 30.55  ? 77  PHE B CZ  1 
ATOM   1343 N N   . ASN B 1 79 ? 8.271   -10.797 -28.394 1.00 29.77  ? 78  ASN B N   1 
ATOM   1344 C CA  . ASN B 1 79 ? 7.537   -9.984  -29.355 1.00 35.14  ? 78  ASN B CA  1 
ATOM   1345 C C   . ASN B 1 79 ? 8.250   -8.640  -29.531 1.00 35.42  ? 78  ASN B C   1 
ATOM   1346 O O   . ASN B 1 79 ? 8.235   -8.043  -30.611 1.00 37.37  ? 78  ASN B O   1 
ATOM   1347 C CB  . ASN B 1 79 ? 6.058   -9.840  -29.018 1.00 36.34  ? 78  ASN B CB  1 
ATOM   1348 C CG  . ASN B 1 79 ? 5.326   -11.164 -28.962 1.00 41.48  ? 78  ASN B CG  1 
ATOM   1349 O OD1 . ASN B 1 79 ? 5.800   -12.167 -29.512 1.00 40.18  ? 78  ASN B OD1 1 
ATOM   1350 N ND2 . ASN B 1 79 ? 4.186   -11.198 -28.281 1.00 40.68  ? 78  ASN B ND2 1 
ATOM   1351 N N   . GLU B 1 80 ? 8.928   -8.185  -28.489 1.00 33.39  ? 79  GLU B N   1 
ATOM   1352 C CA  . GLU B 1 80 ? 9.667   -6.947  -28.656 1.00 36.72  ? 79  GLU B CA  1 
ATOM   1353 C C   . GLU B 1 80 ? 10.792  -7.184  -29.667 1.00 36.04  ? 79  GLU B C   1 
ATOM   1354 O O   . GLU B 1 80 ? 11.096  -6.304  -30.476 1.00 37.20  ? 79  GLU B O   1 
ATOM   1355 C CB  . GLU B 1 80 ? 10.288  -6.421  -27.368 1.00 37.47  ? 79  GLU B CB  1 
ATOM   1356 C CG  . GLU B 1 80 ? 9.298   -5.677  -26.471 1.00 44.07  ? 79  GLU B CG  1 
ATOM   1357 N N   . GLY B 1 81 ? 11.414  -8.370  -29.585 1.00 32.89  ? 80  GLY B N   1 
ATOM   1358 C CA  . GLY B 1 81 ? 12.521  -8.734  -30.471 1.00 30.42  ? 80  GLY B CA  1 
ATOM   1359 C C   . GLY B 1 81 ? 12.042  -8.820  -31.913 1.00 30.74  ? 80  GLY B C   1 
ATOM   1360 O O   . GLY B 1 81 ? 12.778  -8.458  -32.835 1.00 33.05  ? 80  GLY B O   1 
ATOM   1361 N N   . LEU B 1 82 ? 10.825  -9.314  -32.093 1.00 28.45  ? 81  LEU B N   1 
ATOM   1362 C CA  . LEU B 1 82 ? 10.203  -9.367  -33.401 1.00 32.95  ? 81  LEU B CA  1 
ATOM   1363 C C   . LEU B 1 82 ? 10.036  -7.941  -33.921 1.00 35.87  ? 81  LEU B C   1 
ATOM   1364 O O   . LEU B 1 82 ? 10.238  -7.705  -35.111 1.00 33.54  ? 81  LEU B O   1 
ATOM   1365 C CB  . LEU B 1 82 ? 8.860   -10.108 -33.372 1.00 32.82  ? 81  LEU B CB  1 
ATOM   1366 C CG  . LEU B 1 82 ? 8.937   -11.636 -33.243 1.00 29.26  ? 81  LEU B CG  1 
ATOM   1367 C CD1 . LEU B 1 82 ? 7.543   -12.275 -33.277 1.00 30.85  ? 81  LEU B CD1 1 
ATOM   1368 C CD2 . LEU B 1 82 ? 9.860   -12.249 -34.289 1.00 30.50  ? 81  LEU B CD2 1 
ATOM   1369 N N   . TRP B 1 83 ? 9.657   -7.008  -33.025 1.00 33.33  ? 82  TRP B N   1 
ATOM   1370 C CA  . TRP B 1 83 ? 9.531   -5.604  -33.387 1.00 33.87  ? 82  TRP B CA  1 
ATOM   1371 C C   . TRP B 1 83 ? 10.876  -5.033  -33.840 1.00 32.86  ? 82  TRP B C   1 
ATOM   1372 O O   . TRP B 1 83 ? 10.917  -4.399  -34.899 1.00 34.27  ? 82  TRP B O   1 
ATOM   1373 C CB  . TRP B 1 83 ? 8.909   -4.735  -32.280 1.00 34.46  ? 82  TRP B CB  1 
ATOM   1374 C CG  . TRP B 1 83 ? 8.658   -3.335  -32.781 1.00 37.60  ? 82  TRP B CG  1 
ATOM   1375 C CD1 . TRP B 1 83 ? 7.529   -2.876  -33.388 1.00 41.84  ? 82  TRP B CD1 1 
ATOM   1376 C CD2 . TRP B 1 83 ? 9.603   -2.242  -32.807 1.00 39.16  ? 82  TRP B CD2 1 
ATOM   1377 N NE1 . TRP B 1 83 ? 7.706   -1.576  -33.786 1.00 42.86  ? 82  TRP B NE1 1 
ATOM   1378 C CE2 . TRP B 1 83 ? 8.964   -1.162  -33.448 1.00 39.96  ? 82  TRP B CE2 1 
ATOM   1379 C CE3 . TRP B 1 83 ? 10.920  -2.069  -32.353 1.00 37.04  ? 82  TRP B CE3 1 
ATOM   1380 C CZ2 . TRP B 1 83 ? 9.588   0.075   -33.612 1.00 42.01  ? 82  TRP B CZ2 1 
ATOM   1381 C CZ3 . TRP B 1 83 ? 11.534  -0.844  -32.507 1.00 41.35  ? 82  TRP B CZ3 1 
ATOM   1382 C CH2 . TRP B 1 83 ? 10.876  0.212   -33.134 1.00 37.42  ? 82  TRP B CH2 1 
ATOM   1383 N N   . GLU B 1 84 ? 11.955  -5.350  -33.109 1.00 31.82  ? 83  GLU B N   1 
ATOM   1384 C CA  . GLU B 1 84 ? 13.271  -4.772  -33.344 1.00 32.87  ? 83  GLU B CA  1 
ATOM   1385 C C   . GLU B 1 84 ? 13.867  -5.288  -34.655 1.00 33.92  ? 83  GLU B C   1 
ATOM   1386 O O   . GLU B 1 84 ? 14.440  -4.494  -35.423 1.00 32.86  ? 83  GLU B O   1 
ATOM   1387 C CB  . GLU B 1 84 ? 14.250  -4.942  -32.197 1.00 30.29  ? 83  GLU B CB  1 
ATOM   1388 C CG  . GLU B 1 84 ? 13.758  -4.268  -30.913 1.00 35.16  ? 83  GLU B CG  1 
ATOM   1389 C CD  . GLU B 1 84 ? 14.609  -4.635  -29.725 1.00 35.28  ? 83  GLU B CD  1 
ATOM   1390 O OE1 . GLU B 1 84 ? 15.529  -5.482  -29.869 1.00 32.76  ? 83  GLU B OE1 1 
ATOM   1391 O OE2 . GLU B 1 84 ? 14.398  -4.041  -28.623 1.00 36.31  ? 83  GLU B OE2 1 
ATOM   1392 N N   . ILE B 1 85 ? 13.752  -6.601  -34.913 1.00 31.65  ? 84  ILE B N   1 
ATOM   1393 C CA  . ILE B 1 85 ? 14.439  -7.154  -36.082 1.00 29.74  ? 84  ILE B CA  1 
ATOM   1394 C C   . ILE B 1 85 ? 13.792  -6.590  -37.348 1.00 31.29  ? 84  ILE B C   1 
ATOM   1395 O O   . ILE B 1 85 ? 14.467  -6.395  -38.372 1.00 30.44  ? 84  ILE B O   1 
ATOM   1396 C CB  . ILE B 1 85 ? 14.487  -8.699  -36.069 1.00 30.45  ? 84  ILE B CB  1 
ATOM   1397 C CG1 . ILE B 1 85 ? 15.526  -9.273  -37.082 1.00 30.78  ? 84  ILE B CG1 1 
ATOM   1398 C CG2 . ILE B 1 85 ? 13.098  -9.278  -36.325 1.00 30.90  ? 84  ILE B CG2 1 
ATOM   1399 C CD1 . ILE B 1 85 ? 16.105  -10.642 -36.714 1.00 32.18  ? 84  ILE B CD1 1 
ATOM   1400 N N   . GLN B 1 86 ? 12.494  -6.295  -37.243 1.00 31.49  ? 85  GLN B N   1 
ATOM   1401 C CA  . GLN B 1 86 ? 11.672  -5.773  -38.317 1.00 35.86  ? 85  GLN B CA  1 
ATOM   1402 C C   . GLN B 1 86 ? 11.898  -4.270  -38.515 1.00 35.77  ? 85  GLN B C   1 
ATOM   1403 O O   . GLN B 1 86 ? 11.989  -3.815  -39.656 1.00 35.81  ? 85  GLN B O   1 
ATOM   1404 C CB  . GLN B 1 86 ? 10.204  -6.112  -38.057 1.00 40.13  ? 85  GLN B CB  1 
ATOM   1405 N N   . ASN B 1 87 ? 11.990  -3.481  -37.434 1.00 32.97  ? 86  ASN B N   1 
ATOM   1406 C CA  . ASN B 1 87 ? 11.850  -2.037  -37.620 1.00 35.36  ? 86  ASN B CA  1 
ATOM   1407 C C   . ASN B 1 87 ? 13.166  -1.291  -37.436 1.00 34.39  ? 86  ASN B C   1 
ATOM   1408 O O   . ASN B 1 87 ? 13.289  -0.158  -37.914 1.00 39.62  ? 86  ASN B O   1 
ATOM   1409 C CB  . ASN B 1 87 ? 10.791  -1.470  -36.674 1.00 37.78  ? 86  ASN B CB  1 
ATOM   1410 C CG  . ASN B 1 87 ? 9.441   -2.005  -37.061 1.00 43.03  ? 86  ASN B CG  1 
ATOM   1411 O OD1 . ASN B 1 87 ? 8.914   -1.620  -38.103 1.00 48.31  ? 86  ASN B OD1 1 
ATOM   1412 N ND2 . ASN B 1 87 ? 8.922   -2.972  -36.320 1.00 45.51  ? 86  ASN B ND2 1 
ATOM   1413 N N   . ASN B 1 88 ? 14.130  -1.876  -36.711 1.00 32.76  ? 87  ASN B N   1 
ATOM   1414 C CA  . ASN B 1 88 ? 15.397  -1.195  -36.467 1.00 35.08  ? 87  ASN B CA  1 
ATOM   1415 C C   . ASN B 1 88 ? 16.463  -2.195  -36.047 1.00 34.16  ? 87  ASN B C   1 
ATOM   1416 O O   . ASN B 1 88 ? 17.095  -2.064  -34.990 1.00 32.92  ? 87  ASN B O   1 
ATOM   1417 C CB  . ASN B 1 88 ? 15.293  -0.014  -35.498 1.00 39.64  ? 87  ASN B CB  1 
ATOM   1418 C CG  . ASN B 1 88 ? 16.393  1.022   -35.676 1.00 38.72  ? 87  ASN B CG  1 
ATOM   1419 O OD1 . ASN B 1 88 ? 17.455  0.784   -36.271 1.00 36.07  ? 87  ASN B OD1 1 
ATOM   1420 N ND2 . ASN B 1 88 ? 16.169  2.209   -35.135 1.00 40.68  ? 87  ASN B ND2 1 
ATOM   1421 N N   . PRO B 1 89 ? 16.742  -3.179  -36.934 1.00 33.67  ? 88  PRO B N   1 
ATOM   1422 C CA  . PRO B 1 89 ? 17.734  -4.216  -36.665 1.00 30.75  ? 88  PRO B CA  1 
ATOM   1423 C C   . PRO B 1 89 ? 19.153  -3.758  -36.384 1.00 28.42  ? 88  PRO B C   1 
ATOM   1424 O O   . PRO B 1 89 ? 19.919  -4.484  -35.770 1.00 31.06  ? 88  PRO B O   1 
ATOM   1425 C CB  . PRO B 1 89 ? 17.679  -5.109  -37.949 1.00 31.29  ? 88  PRO B CB  1 
ATOM   1426 C CG  . PRO B 1 89 ? 17.126  -4.186  -39.013 1.00 30.15  ? 88  PRO B CG  1 
ATOM   1427 C CD  . PRO B 1 89 ? 16.123  -3.298  -38.272 1.00 29.62  ? 88  PRO B CD  1 
ATOM   1428 N N   . HIS B 1 90 ? 19.540  -2.563  -36.869 1.00 30.07  ? 89  HIS B N   1 
ATOM   1429 C CA  . HIS B 1 90 ? 20.948  -2.204  -36.808 1.00 27.75  ? 89  HIS B CA  1 
ATOM   1430 C C   . HIS B 1 90 ? 21.206  -1.117  -35.759 1.00 33.20  ? 89  HIS B C   1 
ATOM   1431 O O   . HIS B 1 90 ? 22.318  -0.592  -35.683 1.00 34.08  ? 89  HIS B O   1 
ATOM   1432 C CB  . HIS B 1 90 ? 21.453  -1.768  -38.200 1.00 28.98  ? 89  HIS B CB  1 
ATOM   1433 C CG  . HIS B 1 90 ? 21.269  -2.834  -39.244 1.00 31.28  ? 89  HIS B CG  1 
ATOM   1434 N ND1 . HIS B 1 90 ? 21.890  -4.060  -39.146 1.00 31.50  ? 89  HIS B ND1 1 
ATOM   1435 C CD2 . HIS B 1 90 ? 20.534  -2.872  -40.376 1.00 29.18  ? 89  HIS B CD2 1 
ATOM   1436 C CE1 . HIS B 1 90 ? 21.550  -4.803  -40.194 1.00 29.44  ? 89  HIS B CE1 1 
ATOM   1437 N NE2 . HIS B 1 90 ? 20.754  -4.083  -40.950 1.00 30.90  ? 89  HIS B NE2 1 
ATOM   1438 N N   . ALA B 1 91 ? 20.210  -0.838  -34.910 1.00 33.66  ? 90  ALA B N   1 
ATOM   1439 C CA  . ALA B 1 91 ? 20.351  0.186   -33.878 1.00 32.45  ? 90  ALA B CA  1 
ATOM   1440 C C   . ALA B 1 91 ? 21.309  -0.203  -32.751 1.00 36.59  ? 90  ALA B C   1 
ATOM   1441 O O   . ALA B 1 91 ? 21.681  -1.358  -32.554 1.00 33.73  ? 90  ALA B O   1 
ATOM   1442 C CB  . ALA B 1 91 ? 18.982  0.605   -33.374 1.00 31.02  ? 90  ALA B CB  1 
ATOM   1443 N N   . SER B 1 92 ? 21.763  0.822   -32.011 1.00 38.59  ? 91  SER B N   1 
ATOM   1444 C CA  . SER B 1 92 ? 22.445  0.662   -30.747 1.00 41.73  ? 91  SER B CA  1 
ATOM   1445 C C   . SER B 1 92 ? 21.387  0.418   -29.675 1.00 46.46  ? 91  SER B C   1 
ATOM   1446 O O   . SER B 1 92 ? 20.485  1.246   -29.500 1.00 44.89  ? 91  SER B O   1 
ATOM   1447 C CB  . SER B 1 92 ? 23.251  1.915   -30.422 1.00 39.79  ? 91  SER B CB  1 
ATOM   1448 O OG  . SER B 1 92 ? 23.928  1.728   -29.193 1.00 48.82  ? 91  SER B OG  1 
ATOM   1449 N N   . TYR B 1 93 ? 21.508  -0.728  -28.992 1.00 47.67  ? 92  TYR B N   1 
ATOM   1450 C CA  . TYR B 1 93 ? 20.632  -1.122  -27.902 1.00 45.79  ? 92  TYR B CA  1 
ATOM   1451 C C   . TYR B 1 93 ? 21.408  -1.048  -26.590 1.00 51.95  ? 92  TYR B C   1 
ATOM   1452 O O   . TYR B 1 93 ? 20.943  -1.543  -25.567 1.00 53.63  ? 92  TYR B O   1 
ATOM   1453 C CB  . TYR B 1 93 ? 20.000  -2.493  -28.176 1.00 41.54  ? 92  TYR B CB  1 
ATOM   1454 C CG  . TYR B 1 93 ? 18.984  -2.392  -29.299 1.00 36.66  ? 92  TYR B CG  1 
ATOM   1455 C CD1 . TYR B 1 93 ? 17.709  -1.885  -29.067 1.00 33.74  ? 92  TYR B CD1 1 
ATOM   1456 C CD2 . TYR B 1 93 ? 19.298  -2.795  -30.597 1.00 34.92  ? 92  TYR B CD2 1 
ATOM   1457 C CE1 . TYR B 1 93 ? 16.784  -1.734  -30.083 1.00 36.03  ? 92  TYR B CE1 1 
ATOM   1458 C CE2 . TYR B 1 93 ? 18.376  -2.645  -31.619 1.00 33.95  ? 92  TYR B CE2 1 
ATOM   1459 C CZ  . TYR B 1 93 ? 17.114  -2.149  -31.361 1.00 36.84  ? 92  TYR B CZ  1 
ATOM   1460 O OH  . TYR B 1 93 ? 16.173  -2.056  -32.344 1.00 34.85  ? 92  TYR B OH  1 
ATOM   1461 N N   . SER B 1 94 ? 22.579  -0.396  -26.651 1.00 63.73  ? 93  SER B N   1 
ATOM   1462 C CA  . SER B 1 94 ? 23.333  0.058   -25.491 1.00 71.74  ? 93  SER B CA  1 
ATOM   1463 C C   . SER B 1 94 ? 22.371  0.678   -24.467 1.00 80.49  ? 93  SER B C   1 
ATOM   1464 O O   . SER B 1 94 ? 21.786  1.736   -24.796 1.00 78.68  ? 93  SER B O   1 
ATOM   1465 C CB  . SER B 1 94 ? 24.385  1.065   -25.895 1.00 73.81  ? 93  SER B CB  1 
ATOM   1466 O OG  . SER B 1 94 ? 25.355  0.478   -26.751 1.00 75.24  ? 93  SER B OG  1 
ATOM   1467 O OXT . SER B 1 94 ? 22.228  0.075   -23.383 1.00 95.24  ? 93  SER B OXT 1 
ATOM   1468 N N   . HIS C 1 4  ? 33.106  -23.931 27.326  1.00 77.03  ? 3   HIS C N   1 
ATOM   1469 C CA  . HIS C 1 4  ? 32.041  -22.897 27.439  1.00 84.02  ? 3   HIS C CA  1 
ATOM   1470 C C   . HIS C 1 4  ? 31.289  -23.127 28.755  1.00 84.62  ? 3   HIS C C   1 
ATOM   1471 O O   . HIS C 1 4  ? 31.820  -23.735 29.685  1.00 77.06  ? 3   HIS C O   1 
ATOM   1472 C CB  . HIS C 1 4  ? 31.221  -22.867 26.139  1.00 89.74  ? 3   HIS C CB  1 
ATOM   1473 C CG  . HIS C 1 4  ? 30.349  -21.663 25.940  1.00 103.09 ? 3   HIS C CG  1 
ATOM   1474 N ND1 . HIS C 1 4  ? 29.007  -21.639 26.263  1.00 106.65 ? 3   HIS C ND1 1 
ATOM   1475 C CD2 . HIS C 1 4  ? 30.622  -20.453 25.427  1.00 101.54 ? 3   HIS C CD2 1 
ATOM   1476 C CE1 . HIS C 1 4  ? 28.500  -20.448 25.969  1.00 103.98 ? 3   HIS C CE1 1 
ATOM   1477 N NE2 . HIS C 1 4  ? 29.466  -19.712 25.460  1.00 104.33 ? 3   HIS C NE2 1 
ATOM   1478 N N   . ALA C 1 5  ? 30.048  -22.637 28.821  1.00 82.43  ? 4   ALA C N   1 
ATOM   1479 C CA  . ALA C 1 5  ? 29.211  -22.701 30.006  1.00 79.16  ? 4   ALA C CA  1 
ATOM   1480 C C   . ALA C 1 5  ? 27.758  -22.822 29.574  1.00 80.41  ? 4   ALA C C   1 
ATOM   1481 O O   . ALA C 1 5  ? 27.251  -21.960 28.854  1.00 88.76  ? 4   ALA C O   1 
ATOM   1482 C CB  . ALA C 1 5  ? 29.379  -21.419 30.767  1.00 84.27  ? 4   ALA C CB  1 
ATOM   1483 N N   . PHE C 1 6  ? 27.085  -23.875 30.032  1.00 65.74  ? 5   PHE C N   1 
ATOM   1484 C CA  . PHE C 1 6  ? 25.692  -24.034 29.658  1.00 59.17  ? 5   PHE C CA  1 
ATOM   1485 C C   . PHE C 1 6  ? 24.858  -24.044 30.929  1.00 64.65  ? 5   PHE C C   1 
ATOM   1486 O O   . PHE C 1 6  ? 25.017  -24.924 31.769  1.00 78.53  ? 5   PHE C O   1 
ATOM   1487 C CB  . PHE C 1 6  ? 25.455  -25.241 28.734  1.00 50.28  ? 5   PHE C CB  1 
ATOM   1488 C CG  . PHE C 1 6  ? 26.236  -25.206 27.425  1.00 46.35  ? 5   PHE C CG  1 
ATOM   1489 C CD1 . PHE C 1 6  ? 25.846  -24.378 26.376  1.00 49.95  ? 5   PHE C CD1 1 
ATOM   1490 C CD2 . PHE C 1 6  ? 27.375  -25.982 27.245  1.00 47.80  ? 5   PHE C CD2 1 
ATOM   1491 C CE1 . PHE C 1 6  ? 26.560  -24.351 25.185  1.00 48.61  ? 5   PHE C CE1 1 
ATOM   1492 C CE2 . PHE C 1 6  ? 28.094  -25.950 26.048  1.00 54.21  ? 5   PHE C CE2 1 
ATOM   1493 C CZ  . PHE C 1 6  ? 27.678  -25.133 25.014  1.00 48.65  ? 5   PHE C CZ  1 
ATOM   1494 N N   . LYS C 1 7  ? 24.001  -23.034 31.068  1.00 63.02  ? 6   LYS C N   1 
ATOM   1495 C CA  . LYS C 1 7  ? 23.016  -23.000 32.135  1.00 63.62  ? 6   LYS C CA  1 
ATOM   1496 C C   . LYS C 1 7  ? 21.721  -23.488 31.500  1.00 57.76  ? 6   LYS C C   1 
ATOM   1497 O O   . LYS C 1 7  ? 21.639  -23.517 30.272  1.00 63.23  ? 6   LYS C O   1 
ATOM   1498 C CB  . LYS C 1 7  ? 22.908  -21.579 32.709  1.00 61.91  ? 6   LYS C CB  1 
ATOM   1499 N N   . PRO C 1 8  ? 20.689  -23.904 32.274  1.00 57.24  ? 7   PRO C N   1 
ATOM   1500 C CA  . PRO C 1 8  ? 19.398  -24.274 31.683  1.00 52.61  ? 7   PRO C CA  1 
ATOM   1501 C C   . PRO C 1 8  ? 18.844  -23.110 30.861  1.00 61.35  ? 7   PRO C C   1 
ATOM   1502 O O   . PRO C 1 8  ? 19.093  -21.946 31.189  1.00 63.27  ? 7   PRO C O   1 
ATOM   1503 C CB  . PRO C 1 8  ? 18.516  -24.617 32.886  1.00 55.10  ? 7   PRO C CB  1 
ATOM   1504 C CG  . PRO C 1 8  ? 19.506  -24.956 33.978  1.00 56.52  ? 7   PRO C CG  1 
ATOM   1505 C CD  . PRO C 1 8  ? 20.715  -24.068 33.739  1.00 59.07  ? 7   PRO C CD  1 
ATOM   1506 N N   . GLY C 1 9  ? 18.138  -23.438 29.769  1.00 54.18  ? 8   GLY C N   1 
ATOM   1507 C CA  . GLY C 1 9  ? 17.508  -22.445 28.912  1.00 50.31  ? 8   GLY C CA  1 
ATOM   1508 C C   . GLY C 1 9  ? 18.386  -21.959 27.754  1.00 52.50  ? 8   GLY C C   1 
ATOM   1509 O O   . GLY C 1 9  ? 17.845  -21.406 26.798  1.00 60.65  ? 8   GLY C O   1 
ATOM   1510 N N   . ASP C 1 10 ? 19.719  -22.148 27.845  1.00 45.60  ? 9   ASP C N   1 
ATOM   1511 C CA  . ASP C 1 10 ? 20.662  -21.819 26.787  1.00 46.31  ? 9   ASP C CA  1 
ATOM   1512 C C   . ASP C 1 10 ? 20.256  -22.543 25.506  1.00 45.40  ? 9   ASP C C   1 
ATOM   1513 O O   . ASP C 1 10 ? 19.899  -23.717 25.540  1.00 40.35  ? 9   ASP C O   1 
ATOM   1514 C CB  . ASP C 1 10 ? 22.106  -22.105 27.178  1.00 54.26  ? 9   ASP C CB  1 
ATOM   1515 C CG  . ASP C 1 10 ? 22.711  -21.218 28.265  1.00 58.41  ? 9   ASP C CG  1 
ATOM   1516 O OD1 . ASP C 1 10 ? 22.121  -20.169 28.561  1.00 64.69  ? 9   ASP C OD1 1 
ATOM   1517 O OD2 . ASP C 1 10 ? 23.769  -21.589 28.822  1.00 65.61  ? 9   ASP C OD2 1 
ATOM   1518 N N   . LEU C 1 11 ? 20.270  -21.811 24.386  1.00 44.17  ? 10  LEU C N   1 
ATOM   1519 C CA  . LEU C 1 11 ? 19.865  -22.376 23.105  1.00 43.34  ? 10  LEU C CA  1 
ATOM   1520 C C   . LEU C 1 11 ? 21.105  -22.880 22.387  1.00 38.87  ? 10  LEU C C   1 
ATOM   1521 O O   . LEU C 1 11 ? 22.152  -22.234 22.441  1.00 38.43  ? 10  LEU C O   1 
ATOM   1522 C CB  . LEU C 1 11 ? 19.106  -21.351 22.257  1.00 42.77  ? 10  LEU C CB  1 
ATOM   1523 C CG  . LEU C 1 11 ? 17.828  -20.797 22.883  1.00 39.93  ? 10  LEU C CG  1 
ATOM   1524 C CD1 . LEU C 1 11 ? 17.179  -19.847 21.884  1.00 44.52  ? 10  LEU C CD1 1 
ATOM   1525 C CD2 . LEU C 1 11 ? 16.860  -21.898 23.319  1.00 42.15  ? 10  LEU C CD2 1 
ATOM   1526 N N   . VAL C 1 12 ? 20.995  -24.056 21.732  1.00 34.36  ? 11  VAL C N   1 
ATOM   1527 C CA  . VAL C 1 12 ? 22.180  -24.708 21.215  1.00 34.68  ? 11  VAL C CA  1 
ATOM   1528 C C   . VAL C 1 12 ? 21.783  -25.484 19.949  1.00 33.27  ? 11  VAL C C   1 
ATOM   1529 O O   . VAL C 1 12 ? 20.585  -25.656 19.699  1.00 32.09  ? 11  VAL C O   1 
ATOM   1530 C CB  . VAL C 1 12 ? 22.798  -25.661 22.267  1.00 39.17  ? 11  VAL C CB  1 
ATOM   1531 C CG1 . VAL C 1 12 ? 23.082  -24.976 23.614  1.00 40.71  ? 11  VAL C CG1 1 
ATOM   1532 C CG2 . VAL C 1 12 ? 21.948  -26.908 22.497  1.00 32.86  ? 11  VAL C CG2 1 
ATOM   1533 N N   . PHE C 1 13 ? 22.809  -25.917 19.198  1.00 35.45  ? 12  PHE C N   1 
ATOM   1534 C CA  . PHE C 1 13 ? 22.784  -27.077 18.313  1.00 32.56  ? 12  PHE C CA  1 
ATOM   1535 C C   . PHE C 1 13 ? 23.490  -28.238 19.018  1.00 31.92  ? 12  PHE C C   1 
ATOM   1536 O O   . PHE C 1 13 ? 24.587  -28.097 19.563  1.00 35.55  ? 12  PHE C O   1 
ATOM   1537 C CB  . PHE C 1 13 ? 23.429  -26.856 16.933  1.00 35.27  ? 12  PHE C CB  1 
ATOM   1538 C CG  . PHE C 1 13 ? 22.664  -25.846 16.096  1.00 38.08  ? 12  PHE C CG  1 
ATOM   1539 C CD1 . PHE C 1 13 ? 21.595  -26.254 15.293  1.00 33.44  ? 12  PHE C CD1 1 
ATOM   1540 C CD2 . PHE C 1 13 ? 23.006  -24.491 16.119  1.00 38.76  ? 12  PHE C CD2 1 
ATOM   1541 C CE1 . PHE C 1 13 ? 20.878  -25.334 14.540  1.00 36.77  ? 12  PHE C CE1 1 
ATOM   1542 C CE2 . PHE C 1 13 ? 22.282  -23.578 15.371  1.00 41.81  ? 12  PHE C CE2 1 
ATOM   1543 C CZ  . PHE C 1 13 ? 21.224  -24.000 14.589  1.00 41.86  ? 12  PHE C CZ  1 
ATOM   1544 N N   . ALA C 1 14 ? 22.812  -29.398 19.033  1.00 29.23  ? 13  ALA C N   1 
ATOM   1545 C CA  . ALA C 1 14 ? 23.288  -30.562 19.768  1.00 28.04  ? 13  ALA C CA  1 
ATOM   1546 C C   . ALA C 1 14 ? 23.574  -31.678 18.771  1.00 33.26  ? 13  ALA C C   1 
ATOM   1547 O O   . ALA C 1 14 ? 22.685  -32.000 17.981  1.00 30.23  ? 13  ALA C O   1 
ATOM   1548 C CB  . ALA C 1 14 ? 22.186  -31.001 20.712  1.00 27.70  ? 13  ALA C CB  1 
ATOM   1549 N N   . LYS C 1 15 ? 24.770  -32.276 18.854  1.00 33.15  ? 14  LYS C N   1 
ATOM   1550 C CA  . LYS C 1 15 ? 25.177  -33.265 17.868  1.00 32.75  ? 14  LYS C CA  1 
ATOM   1551 C C   . LYS C 1 15 ? 25.152  -34.652 18.495  1.00 33.19  ? 14  LYS C C   1 
ATOM   1552 O O   . LYS C 1 15 ? 25.813  -34.896 19.500  1.00 35.36  ? 14  LYS C O   1 
ATOM   1553 C CB  . LYS C 1 15 ? 26.554  -32.925 17.281  1.00 34.57  ? 14  LYS C CB  1 
ATOM   1554 C CG  . LYS C 1 15 ? 27.060  -33.914 16.214  1.00 38.12  ? 14  LYS C CG  1 
ATOM   1555 C CD  . LYS C 1 15 ? 26.278  -33.812 14.898  1.00 38.02  ? 14  LYS C CD  1 
ATOM   1556 C CE  . LYS C 1 15 ? 26.770  -34.738 13.785  1.00 32.58  ? 14  LYS C CE  1 
ATOM   1557 N NZ  . LYS C 1 15 ? 26.497  -36.134 14.138  1.00 34.46  ? 14  LYS C NZ  1 
ATOM   1558 N N   . MET C 1 16 ? 24.374  -35.563 17.899  1.00 31.79  ? 15  MET C N   1 
ATOM   1559 C CA  . MET C 1 16 ? 24.439  -36.982 18.242  1.00 30.03  ? 15  MET C CA  1 
ATOM   1560 C C   . MET C 1 16 ? 24.858  -37.756 16.999  1.00 35.13  ? 15  MET C C   1 
ATOM   1561 O O   . MET C 1 16 ? 24.533  -37.371 15.883  1.00 30.16  ? 15  MET C O   1 
ATOM   1562 C CB  . MET C 1 16 ? 23.062  -37.511 18.660  1.00 32.42  ? 15  MET C CB  1 
ATOM   1563 C CG  . MET C 1 16 ? 22.556  -36.810 19.931  1.00 36.80  ? 15  MET C CG  1 
ATOM   1564 S SD  . MET C 1 16 ? 20.945  -37.441 20.428  1.00 43.84  ? 15  MET C SD  1 
ATOM   1565 C CE  . MET C 1 16 ? 20.032  -36.878 18.984  1.00 49.88  ? 15  MET C CE  1 
ATOM   1566 N N   . LYS C 1 17 ? 25.551  -38.877 17.217  1.00 34.37  ? 16  LYS C N   1 
ATOM   1567 C CA  . LYS C 1 17 ? 25.926  -39.750 16.117  1.00 35.54  ? 16  LYS C CA  1 
ATOM   1568 C C   . LYS C 1 17 ? 24.657  -40.172 15.369  1.00 29.07  ? 16  LYS C C   1 
ATOM   1569 O O   . LYS C 1 17 ? 23.695  -40.635 15.992  1.00 33.57  ? 16  LYS C O   1 
ATOM   1570 C CB  . LYS C 1 17 ? 26.616  -40.972 16.748  1.00 34.78  ? 16  LYS C CB  1 
ATOM   1571 C CG  . LYS C 1 17 ? 27.252  -41.922 15.740  1.00 41.16  ? 16  LYS C CG  1 
ATOM   1572 C CD  . LYS C 1 17 ? 28.358  -41.187 15.006  1.00 44.73  ? 16  LYS C CD  1 
ATOM   1573 C CE  . LYS C 1 17 ? 29.214  -42.155 14.244  1.00 51.32  ? 16  LYS C CE  1 
ATOM   1574 N NZ  . LYS C 1 17 ? 30.424  -41.484 13.774  1.00 48.17  ? 16  LYS C NZ  1 
ATOM   1575 N N   . GLY C 1 18 ? 24.701  -40.060 14.036  1.00 34.94  ? 17  GLY C N   1 
ATOM   1576 C CA  . GLY C 1 18 ? 23.603  -40.532 13.201  1.00 30.59  ? 17  GLY C CA  1 
ATOM   1577 C C   . GLY C 1 18 ? 22.646  -39.399 12.815  1.00 35.13  ? 17  GLY C C   1 
ATOM   1578 O O   . GLY C 1 18 ? 21.650  -39.637 12.124  1.00 32.13  ? 17  GLY C O   1 
ATOM   1579 N N   . TYR C 1 19 ? 22.933  -38.177 13.286  1.00 31.48  ? 18  TYR C N   1 
ATOM   1580 C CA  . TYR C 1 19 ? 22.001  -37.050 13.155  1.00 30.74  ? 18  TYR C CA  1 
ATOM   1581 C C   . TYR C 1 19 ? 22.771  -35.764 12.886  1.00 31.21  ? 18  TYR C C   1 
ATOM   1582 O O   . TYR C 1 19 ? 23.892  -35.562 13.388  1.00 30.98  ? 18  TYR C O   1 
ATOM   1583 C CB  . TYR C 1 19 ? 21.138  -36.793 14.399  1.00 29.57  ? 18  TYR C CB  1 
ATOM   1584 C CG  . TYR C 1 19 ? 20.314  -38.007 14.774  1.00 31.67  ? 18  TYR C CG  1 
ATOM   1585 C CD1 . TYR C 1 19 ? 20.831  -39.023 15.585  1.00 31.92  ? 18  TYR C CD1 1 
ATOM   1586 C CD2 . TYR C 1 19 ? 19.029  -38.148 14.272  1.00 32.66  ? 18  TYR C CD2 1 
ATOM   1587 C CE1 . TYR C 1 19 ? 20.056  -40.131 15.904  1.00 34.51  ? 18  TYR C CE1 1 
ATOM   1588 C CE2 . TYR C 1 19 ? 18.269  -39.266 14.571  1.00 40.77  ? 18  TYR C CE2 1 
ATOM   1589 C CZ  . TYR C 1 19 ? 18.782  -40.256 15.386  1.00 40.32  ? 18  TYR C CZ  1 
ATOM   1590 O OH  . TYR C 1 19 ? 17.976  -41.326 15.673  1.00 45.92  ? 18  TYR C OH  1 
ATOM   1591 N N   . PRO C 1 20 ? 22.188  -34.839 12.083  1.00 29.77  ? 19  PRO C N   1 
ATOM   1592 C CA  . PRO C 1 20 ? 22.798  -33.524 11.880  1.00 26.85  ? 19  PRO C CA  1 
ATOM   1593 C C   . PRO C 1 20 ? 22.729  -32.737 13.188  1.00 28.39  ? 19  PRO C C   1 
ATOM   1594 O O   . PRO C 1 20 ? 21.946  -33.066 14.075  1.00 27.34  ? 19  PRO C O   1 
ATOM   1595 C CB  . PRO C 1 20 ? 21.871  -32.900 10.800  1.00 30.49  ? 19  PRO C CB  1 
ATOM   1596 C CG  . PRO C 1 20 ? 20.521  -33.515 11.092  1.00 33.50  ? 19  PRO C CG  1 
ATOM   1597 C CD  . PRO C 1 20 ? 20.878  -34.981 11.411  1.00 28.19  ? 19  PRO C CD  1 
ATOM   1598 N N   . HIS C 1 21 ? 23.588  -31.720 13.299  1.00 31.90  ? 20  HIS C N   1 
ATOM   1599 C CA  . HIS C 1 21 ? 23.512  -30.779 14.412  1.00 31.80  ? 20  HIS C CA  1 
ATOM   1600 C C   . HIS C 1 21 ? 22.080  -30.256 14.531  1.00 29.53  ? 20  HIS C C   1 
ATOM   1601 O O   . HIS C 1 21 ? 21.528  -29.728 13.560  1.00 30.62  ? 20  HIS C O   1 
ATOM   1602 C CB  . HIS C 1 21 ? 24.500  -29.628 14.176  1.00 32.52  ? 20  HIS C CB  1 
ATOM   1603 C CG  . HIS C 1 21 ? 25.934  -30.079 14.213  1.00 34.69  ? 20  HIS C CG  1 
ATOM   1604 N ND1 . HIS C 1 21 ? 26.585  -30.734 13.191  1.00 35.67  ? 20  HIS C ND1 1 
ATOM   1605 C CD2 . HIS C 1 21 ? 26.843  -29.922 15.195  1.00 38.94  ? 20  HIS C CD2 1 
ATOM   1606 C CE1 . HIS C 1 21 ? 27.845  -30.974 13.556  1.00 41.53  ? 20  HIS C CE1 1 
ATOM   1607 N NE2 . HIS C 1 21 ? 28.025  -30.471 14.772  1.00 35.68  ? 20  HIS C NE2 1 
ATOM   1608 N N   . TRP C 1 22 ? 21.488  -30.411 15.726  1.00 28.53  ? 21  TRP C N   1 
ATOM   1609 C CA  . TRP C 1 22 ? 20.037  -30.313 15.871  1.00 29.56  ? 21  TRP C CA  1 
ATOM   1610 C C   . TRP C 1 22 ? 19.674  -29.130 16.770  1.00 30.61  ? 21  TRP C C   1 
ATOM   1611 O O   . TRP C 1 22 ? 20.233  -29.001 17.857  1.00 29.70  ? 21  TRP C O   1 
ATOM   1612 C CB  . TRP C 1 22 ? 19.463  -31.611 16.466  1.00 30.65  ? 21  TRP C CB  1 
ATOM   1613 C CG  . TRP C 1 22 ? 18.001  -31.812 16.137  1.00 31.21  ? 21  TRP C CG  1 
ATOM   1614 C CD1 . TRP C 1 22 ? 16.907  -31.214 16.709  1.00 32.27  ? 21  TRP C CD1 1 
ATOM   1615 C CD2 . TRP C 1 22 ? 17.483  -32.702 15.117  1.00 30.40  ? 21  TRP C CD2 1 
ATOM   1616 N NE1 . TRP C 1 22 ? 15.749  -31.670 16.119  1.00 31.72  ? 21  TRP C NE1 1 
ATOM   1617 C CE2 . TRP C 1 22 ? 16.070  -32.584 15.146  1.00 29.33  ? 21  TRP C CE2 1 
ATOM   1618 C CE3 . TRP C 1 22 ? 18.080  -33.574 14.192  1.00 29.01  ? 21  TRP C CE3 1 
ATOM   1619 C CZ2 . TRP C 1 22 ? 15.253  -33.304 14.257  1.00 27.10  ? 21  TRP C CZ2 1 
ATOM   1620 C CZ3 . TRP C 1 22 ? 17.272  -34.285 13.322  1.00 31.08  ? 21  TRP C CZ3 1 
ATOM   1621 C CH2 . TRP C 1 22 ? 15.878  -34.181 13.398  1.00 28.39  ? 21  TRP C CH2 1 
ATOM   1622 N N   . PRO C 1 23 ? 18.688  -28.274 16.416  1.00 31.87  ? 22  PRO C N   1 
ATOM   1623 C CA  . PRO C 1 23 ? 18.311  -27.151 17.289  1.00 28.05  ? 22  PRO C CA  1 
ATOM   1624 C C   . PRO C 1 23 ? 17.757  -27.690 18.603  1.00 27.33  ? 22  PRO C C   1 
ATOM   1625 O O   . PRO C 1 23 ? 16.921  -28.589 18.619  1.00 30.16  ? 22  PRO C O   1 
ATOM   1626 C CB  . PRO C 1 23 ? 17.238  -26.410 16.458  1.00 31.61  ? 22  PRO C CB  1 
ATOM   1627 C CG  . PRO C 1 23 ? 16.646  -27.496 15.563  1.00 30.11  ? 22  PRO C CG  1 
ATOM   1628 C CD  . PRO C 1 23 ? 17.889  -28.305 15.163  1.00 30.34  ? 22  PRO C CD  1 
ATOM   1629 N N   . ALA C 1 24 ? 18.257  -27.141 19.722  1.00 30.98  ? 23  ALA C N   1 
ATOM   1630 C CA  . ALA C 1 24 ? 17.932  -27.731 21.019  1.00 34.42  ? 23  ALA C CA  1 
ATOM   1631 C C   . ALA C 1 24 ? 18.073  -26.670 22.112  1.00 36.72  ? 23  ALA C C   1 
ATOM   1632 O O   . ALA C 1 24 ? 18.543  -25.560 21.856  1.00 35.92  ? 23  ALA C O   1 
ATOM   1633 C CB  . ALA C 1 24 ? 18.867  -28.916 21.294  1.00 31.14  ? 23  ALA C CB  1 
ATOM   1634 N N   . ARG C 1 25 ? 17.727  -27.044 23.351  1.00 38.64  ? 24  ARG C N   1 
ATOM   1635 C CA  . ARG C 1 25 ? 18.100  -26.218 24.488  1.00 36.28  ? 24  ARG C CA  1 
ATOM   1636 C C   . ARG C 1 25 ? 18.573  -27.095 25.657  1.00 37.11  ? 24  ARG C C   1 
ATOM   1637 O O   . ARG C 1 25 ? 18.256  -28.283 25.720  1.00 37.12  ? 24  ARG C O   1 
ATOM   1638 C CB  . ARG C 1 25 ? 16.882  -25.406 24.930  1.00 36.91  ? 24  ARG C CB  1 
ATOM   1639 C CG  . ARG C 1 25 ? 15.652  -26.149 25.414  1.00 45.14  ? 24  ARG C CG  1 
ATOM   1640 C CD  . ARG C 1 25 ? 14.691  -25.182 26.101  1.00 46.68  ? 24  ARG C CD  1 
ATOM   1641 N NE  . ARG C 1 25 ? 13.540  -25.980 26.532  1.00 50.37  ? 24  ARG C NE  1 
ATOM   1642 C CZ  . ARG C 1 25 ? 12.265  -25.802 26.201  1.00 51.83  ? 24  ARG C CZ  1 
ATOM   1643 N NH1 . ARG C 1 25 ? 11.901  -24.749 25.484  1.00 53.46  ? 24  ARG C NH1 1 
ATOM   1644 N NH2 . ARG C 1 25 ? 11.348  -26.666 26.626  1.00 50.81  ? 24  ARG C NH2 1 
ATOM   1645 N N   . ILE C 1 26 ? 19.270  -26.455 26.597  1.00 38.27  ? 25  ILE C N   1 
ATOM   1646 C CA  . ILE C 1 26 ? 19.643  -27.045 27.875  1.00 38.75  ? 25  ILE C CA  1 
ATOM   1647 C C   . ILE C 1 26 ? 18.417  -26.994 28.777  1.00 45.37  ? 25  ILE C C   1 
ATOM   1648 O O   . ILE C 1 26 ? 17.834  -25.928 28.980  1.00 48.24  ? 25  ILE C O   1 
ATOM   1649 C CB  . ILE C 1 26 ? 20.808  -26.254 28.498  1.00 43.61  ? 25  ILE C CB  1 
ATOM   1650 C CG1 . ILE C 1 26 ? 21.912  -25.931 27.498  1.00 47.79  ? 25  ILE C CG1 1 
ATOM   1651 C CG2 . ILE C 1 26 ? 21.335  -26.931 29.767  1.00 44.54  ? 25  ILE C CG2 1 
ATOM   1652 C CD1 . ILE C 1 26 ? 22.848  -27.068 27.136  1.00 47.23  ? 25  ILE C CD1 1 
ATOM   1653 N N   . ASP C 1 27 ? 18.027  -28.157 29.292  1.00 43.49  ? 26  ASP C N   1 
ATOM   1654 C CA  . ASP C 1 27 ? 16.952  -28.263 30.266  1.00 54.21  ? 26  ASP C CA  1 
ATOM   1655 C C   . ASP C 1 27 ? 17.479  -27.977 31.680  1.00 55.58  ? 26  ASP C C   1 
ATOM   1656 O O   . ASP C 1 27 ? 18.506  -28.595 32.043  1.00 59.00  ? 26  ASP C O   1 
ATOM   1657 C CB  . ASP C 1 27 ? 16.260  -29.614 30.168  1.00 51.79  ? 26  ASP C CB  1 
ATOM   1658 C CG  . ASP C 1 27 ? 14.979  -29.629 29.350  1.00 60.11  ? 26  ASP C CG  1 
ATOM   1659 O OD1 . ASP C 1 27 ? 14.635  -28.554 28.799  1.00 53.74  ? 26  ASP C OD1 1 
ATOM   1660 O OD2 . ASP C 1 27 ? 14.318  -30.705 29.319  1.00 59.25  ? 26  ASP C OD2 1 
ATOM   1661 N N   . ASP C 1 31 ? 14.936  -31.758 40.890  1.00 52.80  ? 30  ASP C N   1 
ATOM   1662 C CA  . ASP C 1 31 ? 15.401  -32.488 42.106  1.00 58.10  ? 30  ASP C CA  1 
ATOM   1663 C C   . ASP C 1 31 ? 14.604  -33.779 42.313  1.00 61.94  ? 30  ASP C C   1 
ATOM   1664 O O   . ASP C 1 31 ? 13.367  -33.793 42.294  1.00 60.61  ? 30  ASP C O   1 
ATOM   1665 C CB  . ASP C 1 31 ? 15.286  -31.649 43.366  1.00 60.91  ? 30  ASP C CB  1 
ATOM   1666 C CG  . ASP C 1 31 ? 16.235  -32.078 44.472  1.00 67.86  ? 30  ASP C CG  1 
ATOM   1667 O OD1 . ASP C 1 31 ? 17.365  -31.549 44.500  1.00 71.99  ? 30  ASP C OD1 1 
ATOM   1668 O OD2 . ASP C 1 31 ? 15.861  -32.980 45.252  1.00 75.09  ? 30  ASP C OD2 1 
ATOM   1669 N N   . GLY C 1 32 ? 15.345  -34.862 42.555  1.00 66.35  ? 31  GLY C N   1 
ATOM   1670 C CA  . GLY C 1 32 ? 14.747  -36.154 42.849  1.00 72.19  ? 31  GLY C CA  1 
ATOM   1671 C C   . GLY C 1 32 ? 14.697  -37.042 41.612  1.00 68.47  ? 31  GLY C C   1 
ATOM   1672 O O   . GLY C 1 32 ? 14.449  -38.242 41.739  1.00 64.61  ? 31  GLY C O   1 
ATOM   1673 N N   . ALA C 1 33 ? 14.898  -36.422 40.435  1.00 60.60  ? 32  ALA C N   1 
ATOM   1674 C CA  . ALA C 1 33 ? 15.017  -37.121 39.165  1.00 61.81  ? 32  ALA C CA  1 
ATOM   1675 C C   . ALA C 1 33 ? 16.359  -37.857 39.114  1.00 64.94  ? 32  ALA C C   1 
ATOM   1676 O O   . ALA C 1 33 ? 17.176  -37.733 40.027  1.00 63.87  ? 32  ALA C O   1 
ATOM   1677 C CB  . ALA C 1 33 ? 14.869  -36.136 38.026  1.00 57.67  ? 32  ALA C CB  1 
ATOM   1678 N N   . VAL C 1 34 ? 16.580  -38.656 38.062  1.00 64.74  ? 33  VAL C N   1 
ATOM   1679 C CA  . VAL C 1 34 ? 17.848  -39.366 37.964  1.00 74.55  ? 33  VAL C CA  1 
ATOM   1680 C C   . VAL C 1 34 ? 18.885  -38.448 37.316  1.00 72.70  ? 33  VAL C C   1 
ATOM   1681 O O   . VAL C 1 34 ? 18.579  -37.714 36.372  1.00 61.38  ? 33  VAL C O   1 
ATOM   1682 C CB  . VAL C 1 34 ? 17.910  -40.833 37.483  1.00 72.88  ? 33  VAL C CB  1 
ATOM   1683 C CG1 . VAL C 1 34 ? 19.076  -41.108 36.533  1.00 74.39  ? 33  VAL C CG1 1 
ATOM   1684 C CG2 . VAL C 1 34 ? 17.948  -41.786 38.674  1.00 68.90  ? 33  VAL C CG2 1 
ATOM   1685 N N   . LYS C 1 35 ? 20.091  -38.485 37.904  1.00 65.18  ? 34  LYS C N   1 
ATOM   1686 C CA  . LYS C 1 35 ? 21.199  -37.610 37.572  1.00 63.09  ? 34  LYS C CA  1 
ATOM   1687 C C   . LYS C 1 35 ? 21.683  -37.943 36.159  1.00 58.86  ? 34  LYS C C   1 
ATOM   1688 O O   . LYS C 1 35 ? 21.610  -39.095 35.713  1.00 52.18  ? 34  LYS C O   1 
ATOM   1689 C CB  . LYS C 1 35 ? 22.281  -37.778 38.648  1.00 59.09  ? 34  LYS C CB  1 
ATOM   1690 N N   . PRO C 1 36 ? 22.173  -36.937 35.400  1.00 57.64  ? 35  PRO C N   1 
ATOM   1691 C CA  . PRO C 1 36 ? 22.844  -37.220 34.131  1.00 56.06  ? 35  PRO C CA  1 
ATOM   1692 C C   . PRO C 1 36 ? 23.976  -38.208 34.415  1.00 58.91  ? 35  PRO C C   1 
ATOM   1693 O O   . PRO C 1 36 ? 24.384  -38.397 35.566  1.00 50.32  ? 35  PRO C O   1 
ATOM   1694 C CB  . PRO C 1 36 ? 23.376  -35.832 33.686  1.00 66.83  ? 35  PRO C CB  1 
ATOM   1695 C CG  . PRO C 1 36 ? 22.545  -34.812 34.450  1.00 62.63  ? 35  PRO C CG  1 
ATOM   1696 C CD  . PRO C 1 36 ? 22.102  -35.501 35.734  1.00 60.46  ? 35  PRO C CD  1 
ATOM   1697 N N   . PRO C 1 37 ? 24.528  -38.900 33.396  1.00 52.37  ? 36  PRO C N   1 
ATOM   1698 C CA  . PRO C 1 37 ? 25.875  -39.445 33.544  1.00 49.08  ? 36  PRO C CA  1 
ATOM   1699 C C   . PRO C 1 37 ? 26.797  -38.282 33.915  1.00 50.91  ? 36  PRO C C   1 
ATOM   1700 O O   . PRO C 1 37 ? 26.450  -37.116 33.717  1.00 44.19  ? 36  PRO C O   1 
ATOM   1701 C CB  . PRO C 1 37 ? 26.159  -40.035 32.148  1.00 46.11  ? 36  PRO C CB  1 
ATOM   1702 C CG  . PRO C 1 37 ? 24.768  -40.410 31.646  1.00 46.22  ? 36  PRO C CG  1 
ATOM   1703 C CD  . PRO C 1 37 ? 23.881  -39.271 32.125  1.00 49.16  ? 36  PRO C CD  1 
ATOM   1704 N N   . PRO C 1 38 ? 27.994  -38.559 34.480  1.00 47.10  ? 37  PRO C N   1 
ATOM   1705 C CA  . PRO C 1 38 ? 28.954  -37.504 34.796  1.00 46.15  ? 37  PRO C CA  1 
ATOM   1706 C C   . PRO C 1 38 ? 29.209  -36.591 33.605  1.00 45.46  ? 37  PRO C C   1 
ATOM   1707 O O   . PRO C 1 38 ? 29.453  -37.070 32.497  1.00 46.99  ? 37  PRO C O   1 
ATOM   1708 C CB  . PRO C 1 38 ? 30.224  -38.296 35.166  1.00 48.12  ? 37  PRO C CB  1 
ATOM   1709 C CG  . PRO C 1 38 ? 29.686  -39.611 35.667  1.00 45.39  ? 37  PRO C CG  1 
ATOM   1710 C CD  . PRO C 1 38 ? 28.490  -39.909 34.799  1.00 48.96  ? 37  PRO C CD  1 
ATOM   1711 N N   . ASN C 1 39 ? 29.116  -35.279 33.860  1.00 43.24  ? 38  ASN C N   1 
ATOM   1712 C CA  . ASN C 1 39 ? 29.548  -34.244 32.940  1.00 41.52  ? 38  ASN C CA  1 
ATOM   1713 C C   . ASN C 1 39 ? 28.618  -34.178 31.728  1.00 41.02  ? 38  ASN C C   1 
ATOM   1714 O O   . ASN C 1 39 ? 29.049  -33.732 30.666  1.00 50.07  ? 38  ASN C O   1 
ATOM   1715 C CB  . ASN C 1 39 ? 31.028  -34.363 32.571  1.00 40.75  ? 38  ASN C CB  1 
ATOM   1716 C CG  . ASN C 1 39 ? 31.601  -33.097 31.963  1.00 53.46  ? 38  ASN C CG  1 
ATOM   1717 O OD1 . ASN C 1 39 ? 31.256  -31.985 32.384  1.00 64.64  ? 38  ASN C OD1 1 
ATOM   1718 N ND2 . ASN C 1 39 ? 32.451  -33.224 30.952  1.00 50.37  ? 38  ASN C ND2 1 
ATOM   1719 N N   . LYS C 1 40 ? 27.357  -34.620 31.877  1.00 40.31  ? 39  LYS C N   1 
ATOM   1720 C CA  . LYS C 1 40 ? 26.417  -34.556 30.763  1.00 36.30  ? 39  LYS C CA  1 
ATOM   1721 C C   . LYS C 1 40 ? 25.283  -33.590 31.094  1.00 42.31  ? 39  LYS C C   1 
ATOM   1722 O O   . LYS C 1 40 ? 24.857  -33.516 32.237  1.00 43.70  ? 39  LYS C O   1 
ATOM   1723 C CB  . LYS C 1 40 ? 25.724  -35.882 30.445  1.00 38.33  ? 39  LYS C CB  1 
ATOM   1724 C CG  . LYS C 1 40 ? 26.650  -37.024 30.101  1.00 40.62  ? 39  LYS C CG  1 
ATOM   1725 C CD  . LYS C 1 40 ? 27.472  -36.884 28.839  1.00 46.38  ? 39  LYS C CD  1 
ATOM   1726 C CE  . LYS C 1 40 ? 28.140  -38.197 28.539  1.00 50.82  ? 39  LYS C CE  1 
ATOM   1727 N NZ  . LYS C 1 40 ? 29.169  -38.039 27.512  1.00 54.15  ? 39  LYS C NZ  1 
ATOM   1728 N N   . TYR C 1 41 ? 24.795  -32.867 30.076  1.00 37.32  ? 40  TYR C N   1 
ATOM   1729 C CA  . TYR C 1 41 ? 23.660  -31.959 30.226  1.00 36.52  ? 40  TYR C CA  1 
ATOM   1730 C C   . TYR C 1 41 ? 22.395  -32.626 29.713  1.00 37.20  ? 40  TYR C C   1 
ATOM   1731 O O   . TYR C 1 41 ? 22.465  -33.412 28.766  1.00 37.73  ? 40  TYR C O   1 
ATOM   1732 C CB  . TYR C 1 41 ? 23.790  -30.748 29.299  1.00 33.55  ? 40  TYR C CB  1 
ATOM   1733 C CG  . TYR C 1 41 ? 24.966  -29.894 29.729  1.00 33.81  ? 40  TYR C CG  1 
ATOM   1734 C CD1 . TYR C 1 41 ? 26.262  -30.178 29.291  1.00 35.70  ? 40  TYR C CD1 1 
ATOM   1735 C CD2 . TYR C 1 41 ? 24.776  -28.810 30.595  1.00 39.39  ? 40  TYR C CD2 1 
ATOM   1736 C CE1 . TYR C 1 41 ? 27.338  -29.419 29.713  1.00 41.67  ? 40  TYR C CE1 1 
ATOM   1737 C CE2 . TYR C 1 41 ? 25.853  -28.032 31.002  1.00 39.63  ? 40  TYR C CE2 1 
ATOM   1738 C CZ  . TYR C 1 41 ? 27.126  -28.344 30.564  1.00 43.15  ? 40  TYR C CZ  1 
ATOM   1739 O OH  . TYR C 1 41 ? 28.201  -27.594 30.948  1.00 61.43  ? 40  TYR C OH  1 
ATOM   1740 N N   . PRO C 1 42 ? 21.220  -32.327 30.321  1.00 38.70  ? 41  PRO C N   1 
ATOM   1741 C CA  . PRO C 1 42 ? 19.932  -32.788 29.796  1.00 38.79  ? 41  PRO C CA  1 
ATOM   1742 C C   . PRO C 1 42 ? 19.601  -31.816 28.669  1.00 38.80  ? 41  PRO C C   1 
ATOM   1743 O O   . PRO C 1 42 ? 19.620  -30.591 28.857  1.00 38.55  ? 41  PRO C O   1 
ATOM   1744 C CB  . PRO C 1 42 ? 18.929  -32.705 30.960  1.00 38.75  ? 41  PRO C CB  1 
ATOM   1745 C CG  . PRO C 1 42 ? 19.614  -31.792 31.950  1.00 40.03  ? 41  PRO C CG  1 
ATOM   1746 C CD  . PRO C 1 42 ? 21.070  -31.528 31.553  1.00 41.52  ? 41  PRO C CD  1 
ATOM   1747 N N   . ILE C 1 43 ? 19.371  -32.398 27.490  1.00 37.16  ? 42  ILE C N   1 
ATOM   1748 C CA  . ILE C 1 43 ? 19.096  -31.624 26.288  1.00 35.53  ? 42  ILE C CA  1 
ATOM   1749 C C   . ILE C 1 43 ? 17.658  -31.901 25.876  1.00 34.31  ? 42  ILE C C   1 
ATOM   1750 O O   . ILE C 1 43 ? 17.184  -33.033 25.941  1.00 38.09  ? 42  ILE C O   1 
ATOM   1751 C CB  . ILE C 1 43 ? 20.064  -32.029 25.166  1.00 36.62  ? 42  ILE C CB  1 
ATOM   1752 C CG1 . ILE C 1 43 ? 21.537  -31.791 25.557  1.00 35.39  ? 42  ILE C CG1 1 
ATOM   1753 C CG2 . ILE C 1 43 ? 19.682  -31.348 23.842  1.00 37.15  ? 42  ILE C CG2 1 
ATOM   1754 C CD1 . ILE C 1 43 ? 21.879  -30.384 26.022  1.00 37.00  ? 42  ILE C CD1 1 
ATOM   1755 N N   . PHE C 1 44 ? 16.958  -30.850 25.436  1.00 36.95  ? 43  PHE C N   1 
ATOM   1756 C CA  . PHE C 1 44 ? 15.652  -31.045 24.831  1.00 31.93  ? 43  PHE C CA  1 
ATOM   1757 C C   . PHE C 1 44 ? 15.767  -30.628 23.369  1.00 30.03  ? 43  PHE C C   1 
ATOM   1758 O O   . PHE C 1 44 ? 16.343  -29.578 23.088  1.00 32.17  ? 43  PHE C O   1 
ATOM   1759 C CB  . PHE C 1 44 ? 14.666  -30.097 25.527  1.00 37.75  ? 43  PHE C CB  1 
ATOM   1760 C CG  . PHE C 1 44 ? 13.299  -29.958 24.876  1.00 36.63  ? 43  PHE C CG  1 
ATOM   1761 C CD1 . PHE C 1 44 ? 12.286  -30.895 25.120  1.00 41.75  ? 43  PHE C CD1 1 
ATOM   1762 C CD2 . PHE C 1 44 ? 13.025  -28.891 24.015  1.00 39.32  ? 43  PHE C CD2 1 
ATOM   1763 C CE1 . PHE C 1 44 ? 11.030  -30.771 24.523  1.00 48.03  ? 43  PHE C CE1 1 
ATOM   1764 C CE2 . PHE C 1 44 ? 11.774  -28.775 23.410  1.00 42.36  ? 43  PHE C CE2 1 
ATOM   1765 C CZ  . PHE C 1 44 ? 10.777  -29.695 23.677  1.00 45.40  ? 43  PHE C CZ  1 
ATOM   1766 N N   . PHE C 1 45 ? 15.248  -31.473 22.476  1.00 33.01  ? 44  PHE C N   1 
ATOM   1767 C CA  . PHE C 1 45 ? 15.408  -31.282 21.041  1.00 35.25  ? 44  PHE C CA  1 
ATOM   1768 C C   . PHE C 1 45 ? 14.147  -30.634 20.482  1.00 35.58  ? 44  PHE C C   1 
ATOM   1769 O O   . PHE C 1 45 ? 13.057  -31.192 20.613  1.00 37.36  ? 44  PHE C O   1 
ATOM   1770 C CB  . PHE C 1 45 ? 15.728  -32.590 20.315  1.00 30.93  ? 44  PHE C CB  1 
ATOM   1771 C CG  . PHE C 1 45 ? 17.108  -33.141 20.644  1.00 33.50  ? 44  PHE C CG  1 
ATOM   1772 C CD1 . PHE C 1 45 ? 17.296  -33.933 21.772  1.00 32.18  ? 44  PHE C CD1 1 
ATOM   1773 C CD2 . PHE C 1 45 ? 18.209  -32.866 19.834  1.00 31.29  ? 44  PHE C CD2 1 
ATOM   1774 C CE1 . PHE C 1 45 ? 18.562  -34.434 22.096  1.00 36.64  ? 44  PHE C CE1 1 
ATOM   1775 C CE2 . PHE C 1 45 ? 19.471  -33.386 20.142  1.00 35.07  ? 44  PHE C CE2 1 
ATOM   1776 C CZ  . PHE C 1 45 ? 19.650  -34.154 21.285  1.00 36.03  ? 44  PHE C CZ  1 
ATOM   1777 N N   . PHE C 1 46 ? 14.324  -29.488 19.802  1.00 31.54  ? 45  PHE C N   1 
ATOM   1778 C CA  . PHE C 1 46 ? 13.172  -28.864 19.159  1.00 30.51  ? 45  PHE C CA  1 
ATOM   1779 C C   . PHE C 1 46 ? 12.674  -29.709 17.988  1.00 34.90  ? 45  PHE C C   1 
ATOM   1780 O O   . PHE C 1 46 ? 13.437  -30.472 17.375  1.00 33.86  ? 45  PHE C O   1 
ATOM   1781 C CB  . PHE C 1 46 ? 13.522  -27.443 18.713  1.00 31.42  ? 45  PHE C CB  1 
ATOM   1782 C CG  . PHE C 1 46 ? 13.820  -26.463 19.832  1.00 33.98  ? 45  PHE C CG  1 
ATOM   1783 C CD1 . PHE C 1 46 ? 12.796  -26.027 20.672  1.00 36.85  ? 45  PHE C CD1 1 
ATOM   1784 C CD2 . PHE C 1 46 ? 15.107  -25.957 20.025  1.00 32.07  ? 45  PHE C CD2 1 
ATOM   1785 C CE1 . PHE C 1 46 ? 13.075  -25.123 21.693  1.00 37.16  ? 45  PHE C CE1 1 
ATOM   1786 C CE2 . PHE C 1 46 ? 15.367  -25.050 21.044  1.00 35.63  ? 45  PHE C CE2 1 
ATOM   1787 C CZ  . PHE C 1 46 ? 14.357  -24.631 21.872  1.00 35.31  ? 45  PHE C CZ  1 
ATOM   1788 N N   . GLY C 1 47 ? 11.383  -29.541 17.654  1.00 29.73  ? 46  GLY C N   1 
ATOM   1789 C CA  . GLY C 1 47 ? 10.827  -30.258 16.525  1.00 35.26  ? 46  GLY C CA  1 
ATOM   1790 C C   . GLY C 1 47 ? 10.376  -31.649 16.943  1.00 43.47  ? 46  GLY C C   1 
ATOM   1791 O O   . GLY C 1 47 ? 9.182   -31.942 16.915  1.00 47.70  ? 46  GLY C O   1 
ATOM   1792 N N   . THR C 1 48 ? 11.339  -32.500 17.333  1.00 37.40  ? 47  THR C N   1 
ATOM   1793 C CA  . THR C 1 48 ? 10.976  -33.844 17.769  1.00 38.16  ? 47  THR C CA  1 
ATOM   1794 C C   . THR C 1 48 ? 10.494  -33.794 19.216  1.00 36.10  ? 47  THR C C   1 
ATOM   1795 O O   . THR C 1 48 ? 9.776   -34.698 19.642  1.00 41.71  ? 47  THR C O   1 
ATOM   1796 C CB  . THR C 1 48 ? 12.150  -34.813 17.666  1.00 34.86  ? 47  THR C CB  1 
ATOM   1797 O OG1 . THR C 1 48 ? 13.047  -34.245 18.628  1.00 34.88  ? 47  THR C OG1 1 
ATOM   1798 C CG2 . THR C 1 48 ? 12.680  -34.978 16.248  1.00 33.55  ? 47  THR C CG2 1 
ATOM   1799 N N   . HIS C 1 49 ? 10.935  -32.786 19.977  1.00 35.85  ? 48  HIS C N   1 
ATOM   1800 C CA  . HIS C 1 49 ? 10.653  -32.662 21.405  1.00 41.22  ? 48  HIS C CA  1 
ATOM   1801 C C   . HIS C 1 49 ? 11.078  -33.896 22.207  1.00 39.94  ? 48  HIS C C   1 
ATOM   1802 O O   . HIS C 1 49 ? 10.443  -34.212 23.217  1.00 44.72  ? 48  HIS C O   1 
ATOM   1803 C CB  . HIS C 1 49 ? 9.170   -32.380 21.678  1.00 43.26  ? 48  HIS C CB  1 
ATOM   1804 C CG  . HIS C 1 49 ? 8.584   -31.331 20.796  1.00 44.65  ? 48  HIS C CG  1 
ATOM   1805 N ND1 . HIS C 1 49 ? 7.487   -31.583 19.997  1.00 49.69  ? 48  HIS C ND1 1 
ATOM   1806 C CD2 . HIS C 1 49 ? 8.961   -30.077 20.539  1.00 42.72  ? 48  HIS C CD2 1 
ATOM   1807 C CE1 . HIS C 1 49 ? 7.203   -30.494 19.296  1.00 48.98  ? 48  HIS C CE1 1 
ATOM   1808 N NE2 . HIS C 1 49 ? 8.088   -29.570 19.612  1.00 45.98  ? 48  HIS C NE2 1 
ATOM   1809 N N   . GLU C 1 50 ? 12.164  -34.551 21.792  1.00 37.48  ? 49  GLU C N   1 
ATOM   1810 C CA  . GLU C 1 50 ? 12.788  -35.624 22.549  1.00 37.84  ? 49  GLU C CA  1 
ATOM   1811 C C   . GLU C 1 50 ? 13.866  -35.076 23.484  1.00 39.46  ? 49  GLU C C   1 
ATOM   1812 O O   . GLU C 1 50 ? 14.172  -33.890 23.478  1.00 35.48  ? 49  GLU C O   1 
ATOM   1813 C CB  . GLU C 1 50 ? 13.341  -36.665 21.582  1.00 38.77  ? 49  GLU C CB  1 
ATOM   1814 C CG  . GLU C 1 50 ? 12.262  -37.293 20.704  1.00 45.93  ? 49  GLU C CG  1 
ATOM   1815 C CD  . GLU C 1 50 ? 12.798  -38.077 19.515  1.00 55.77  ? 49  GLU C CD  1 
ATOM   1816 O OE1 . GLU C 1 50 ? 12.207  -39.115 19.173  1.00 72.89  ? 49  GLU C OE1 1 
ATOM   1817 O OE2 . GLU C 1 50 ? 13.795  -37.646 18.917  1.00 58.80  ? 49  GLU C OE2 1 
ATOM   1818 N N   . THR C 1 51 ? 14.402  -35.958 24.340  1.00 42.02  ? 50  THR C N   1 
ATOM   1819 C CA  . THR C 1 51 ? 15.411  -35.593 25.327  1.00 39.57  ? 50  THR C CA  1 
ATOM   1820 C C   . THR C 1 51 ? 16.544  -36.615 25.245  1.00 36.36  ? 50  THR C C   1 
ATOM   1821 O O   . THR C 1 51 ? 16.354  -37.744 24.805  1.00 37.80  ? 50  THR C O   1 
ATOM   1822 C CB  . THR C 1 51 ? 14.838  -35.518 26.749  1.00 43.32  ? 50  THR C CB  1 
ATOM   1823 O OG1 . THR C 1 51 ? 14.277  -36.803 27.021  1.00 45.07  ? 50  THR C OG1 1 
ATOM   1824 C CG2 . THR C 1 51 ? 13.866  -34.371 26.964  1.00 42.38  ? 50  THR C CG2 1 
ATOM   1825 N N   . ALA C 1 52 ? 17.740  -36.170 25.620  1.00 37.60  ? 51  ALA C N   1 
ATOM   1826 C CA  . ALA C 1 52 ? 18.918  -37.016 25.739  1.00 37.99  ? 51  ALA C CA  1 
ATOM   1827 C C   . ALA C 1 52 ? 19.913  -36.307 26.648  1.00 41.35  ? 51  ALA C C   1 
ATOM   1828 O O   . ALA C 1 52 ? 19.716  -35.146 27.007  1.00 40.76  ? 51  ALA C O   1 
ATOM   1829 C CB  . ALA C 1 52 ? 19.520  -37.314 24.377  1.00 37.53  ? 51  ALA C CB  1 
ATOM   1830 N N   . PHE C 1 53 ? 20.981  -37.017 27.023  1.00 42.55  ? 52  PHE C N   1 
ATOM   1831 C CA  . PHE C 1 53 ? 22.062  -36.447 27.806  1.00 40.50  ? 52  PHE C CA  1 
ATOM   1832 C C   . PHE C 1 53 ? 23.254  -36.315 26.882  1.00 38.44  ? 52  PHE C C   1 
ATOM   1833 O O   . PHE C 1 53 ? 23.614  -37.279 26.211  1.00 37.84  ? 52  PHE C O   1 
ATOM   1834 C CB  . PHE C 1 53 ? 22.419  -37.424 28.939  1.00 42.31  ? 52  PHE C CB  1 
ATOM   1835 C CG  . PHE C 1 53 ? 21.422  -37.332 30.079  1.00 39.93  ? 52  PHE C CG  1 
ATOM   1836 C CD1 . PHE C 1 53 ? 21.174  -36.112 30.703  1.00 43.93  ? 52  PHE C CD1 1 
ATOM   1837 C CD2 . PHE C 1 53 ? 20.697  -38.447 30.493  1.00 50.22  ? 52  PHE C CD2 1 
ATOM   1838 C CE1 . PHE C 1 53 ? 20.253  -36.016 31.745  1.00 51.45  ? 52  PHE C CE1 1 
ATOM   1839 C CE2 . PHE C 1 53 ? 19.775  -38.347 31.537  1.00 52.98  ? 52  PHE C CE2 1 
ATOM   1840 C CZ  . PHE C 1 53 ? 19.540  -37.125 32.149  1.00 46.89  ? 52  PHE C CZ  1 
ATOM   1841 N N   . LEU C 1 54 ? 23.901  -35.146 26.898  1.00 32.53  ? 53  LEU C N   1 
ATOM   1842 C CA  . LEU C 1 54 ? 25.037  -34.935 26.015  1.00 33.22  ? 53  LEU C CA  1 
ATOM   1843 C C   . LEU C 1 54 ? 26.121  -34.172 26.765  1.00 35.83  ? 53  LEU C C   1 
ATOM   1844 O O   . LEU C 1 54 ? 25.826  -33.346 27.625  1.00 37.15  ? 53  LEU C O   1 
ATOM   1845 C CB  . LEU C 1 54 ? 24.611  -34.137 24.780  1.00 33.33  ? 53  LEU C CB  1 
ATOM   1846 C CG  . LEU C 1 54 ? 23.778  -34.870 23.723  1.00 39.10  ? 53  LEU C CG  1 
ATOM   1847 C CD1 . LEU C 1 54 ? 23.405  -33.907 22.594  1.00 35.82  ? 53  LEU C CD1 1 
ATOM   1848 C CD2 . LEU C 1 54 ? 24.520  -36.078 23.148  1.00 46.81  ? 53  LEU C CD2 1 
ATOM   1849 N N   . GLY C 1 55 ? 27.362  -34.402 26.347  1.00 38.02  ? 54  GLY C N   1 
ATOM   1850 C CA  . GLY C 1 55 ? 28.510  -33.709 26.905  1.00 36.90  ? 54  GLY C CA  1 
ATOM   1851 C C   . GLY C 1 55 ? 28.821  -32.434 26.131  1.00 41.67  ? 54  GLY C C   1 
ATOM   1852 O O   . GLY C 1 55 ? 28.280  -32.192 25.032  1.00 38.17  ? 54  GLY C O   1 
ATOM   1853 N N   . PRO C 1 56 ? 29.698  -31.570 26.697  1.00 42.20  ? 55  PRO C N   1 
ATOM   1854 C CA  . PRO C 1 56 ? 29.914  -30.231 26.162  1.00 44.83  ? 55  PRO C CA  1 
ATOM   1855 C C   . PRO C 1 56 ? 30.512  -30.278 24.761  1.00 40.67  ? 55  PRO C C   1 
ATOM   1856 O O   . PRO C 1 56 ? 30.262  -29.381 23.959  1.00 53.94  ? 55  PRO C O   1 
ATOM   1857 C CB  . PRO C 1 56 ? 30.815  -29.478 27.193  1.00 45.99  ? 55  PRO C CB  1 
ATOM   1858 C CG  . PRO C 1 56 ? 31.230  -30.522 28.190  1.00 38.44  ? 55  PRO C CG  1 
ATOM   1859 C CD  . PRO C 1 56 ? 30.522  -31.836 27.890  1.00 41.21  ? 55  PRO C CD  1 
ATOM   1860 N N   . LYS C 1 57 ? 31.266  -31.342 24.462  1.00 45.57  ? 56  LYS C N   1 
ATOM   1861 C CA  . LYS C 1 57 ? 31.865  -31.513 23.149  1.00 45.18  ? 56  LYS C CA  1 
ATOM   1862 C C   . LYS C 1 57 ? 30.783  -31.474 22.065  1.00 47.92  ? 56  LYS C C   1 
ATOM   1863 O O   . LYS C 1 57 ? 31.085  -31.176 20.908  1.00 44.55  ? 56  LYS C O   1 
ATOM   1864 C CB  . LYS C 1 57 ? 32.579  -32.869 23.050  1.00 48.06  ? 56  LYS C CB  1 
ATOM   1865 N N   . ASP C 1 58 ? 29.532  -31.772 22.450  1.00 43.12  ? 57  ASP C N   1 
ATOM   1866 C CA  . ASP C 1 58 ? 28.480  -32.085 21.482  1.00 40.90  ? 57  ASP C CA  1 
ATOM   1867 C C   . ASP C 1 58 ? 27.526  -30.913 21.305  1.00 41.86  ? 57  ASP C C   1 
ATOM   1868 O O   . ASP C 1 58 ? 26.504  -31.041 20.623  1.00 38.45  ? 57  ASP C O   1 
ATOM   1869 C CB  . ASP C 1 58 ? 27.724  -33.340 21.882  1.00 43.60  ? 57  ASP C CB  1 
ATOM   1870 C CG  . ASP C 1 58 ? 28.552  -34.613 21.831  1.00 45.76  ? 57  ASP C CG  1 
ATOM   1871 O OD1 . ASP C 1 58 ? 29.328  -34.744 20.878  1.00 50.06  ? 57  ASP C OD1 1 
ATOM   1872 O OD2 . ASP C 1 58 ? 28.355  -35.482 22.696  1.00 53.74  ? 57  ASP C OD2 1 
ATOM   1873 N N   . LEU C 1 59 ? 27.835  -29.791 21.965  1.00 35.15  ? 58  LEU C N   1 
ATOM   1874 C CA  . LEU C 1 59 ? 26.896  -28.692 22.106  1.00 39.50  ? 58  LEU C CA  1 
ATOM   1875 C C   . LEU C 1 59 ? 27.513  -27.411 21.556  1.00 43.14  ? 58  LEU C C   1 
ATOM   1876 O O   . LEU C 1 59 ? 28.692  -27.171 21.791  1.00 46.79  ? 58  LEU C O   1 
ATOM   1877 C CB  . LEU C 1 59 ? 26.585  -28.555 23.595  1.00 36.65  ? 58  LEU C CB  1 
ATOM   1878 C CG  . LEU C 1 59 ? 25.938  -29.788 24.233  1.00 36.23  ? 58  LEU C CG  1 
ATOM   1879 C CD1 . LEU C 1 59 ? 25.812  -29.617 25.728  1.00 37.84  ? 58  LEU C CD1 1 
ATOM   1880 C CD2 . LEU C 1 59 ? 24.559  -30.133 23.622  1.00 29.34  ? 58  LEU C CD2 1 
ATOM   1881 N N   . PHE C 1 60 ? 26.704  -26.607 20.847  1.00 43.87  ? 59  PHE C N   1 
ATOM   1882 C CA  . PHE C 1 60 ? 27.177  -25.404 20.163  1.00 41.71  ? 59  PHE C CA  1 
ATOM   1883 C C   . PHE C 1 60 ? 26.203  -24.254 20.421  1.00 43.89  ? 59  PHE C C   1 
ATOM   1884 O O   . PHE C 1 60 ? 25.008  -24.378 20.171  1.00 41.92  ? 59  PHE C O   1 
ATOM   1885 C CB  . PHE C 1 60 ? 27.425  -25.698 18.677  1.00 44.89  ? 59  PHE C CB  1 
ATOM   1886 C CG  . PHE C 1 60 ? 28.378  -26.855 18.389  1.00 42.46  ? 59  PHE C CG  1 
ATOM   1887 C CD1 . PHE C 1 60 ? 27.923  -28.172 18.356  1.00 39.72  ? 59  PHE C CD1 1 
ATOM   1888 C CD2 . PHE C 1 60 ? 29.736  -26.627 18.151  1.00 45.01  ? 59  PHE C CD2 1 
ATOM   1889 C CE1 . PHE C 1 60 ? 28.792  -29.229 18.125  1.00 39.84  ? 59  PHE C CE1 1 
ATOM   1890 C CE2 . PHE C 1 60 ? 30.605  -27.684 17.888  1.00 44.66  ? 59  PHE C CE2 1 
ATOM   1891 C CZ  . PHE C 1 60 ? 30.135  -28.983 17.869  1.00 46.07  ? 59  PHE C CZ  1 
ATOM   1892 N N   . PRO C 1 61 ? 26.635  -23.092 20.985  1.00 47.62  ? 60  PRO C N   1 
ATOM   1893 C CA  . PRO C 1 61 ? 25.675  -22.036 21.334  1.00 47.09  ? 60  PRO C CA  1 
ATOM   1894 C C   . PRO C 1 61 ? 24.977  -21.589 20.050  1.00 40.74  ? 60  PRO C C   1 
ATOM   1895 O O   . PRO C 1 61 ? 25.598  -21.538 18.988  1.00 46.75  ? 60  PRO C O   1 
ATOM   1896 C CB  . PRO C 1 61 ? 26.475  -20.913 22.032  1.00 46.71  ? 60  PRO C CB  1 
ATOM   1897 C CG  . PRO C 1 61 ? 27.889  -21.463 22.129  1.00 46.09  ? 60  PRO C CG  1 
ATOM   1898 C CD  . PRO C 1 61 ? 28.030  -22.737 21.301  1.00 51.62  ? 60  PRO C CD  1 
ATOM   1899 N N   . TYR C 1 62 ? 23.657  -21.376 20.155  1.00 47.18  ? 61  TYR C N   1 
ATOM   1900 C CA  . TYR C 1 62 ? 22.780  -21.176 19.014  1.00 47.47  ? 61  TYR C CA  1 
ATOM   1901 C C   . TYR C 1 62 ? 23.218  -19.950 18.212  1.00 57.95  ? 61  TYR C C   1 
ATOM   1902 O O   . TYR C 1 62 ? 23.507  -20.068 17.018  1.00 58.86  ? 61  TYR C O   1 
ATOM   1903 C CB  . TYR C 1 62 ? 21.319  -21.100 19.460  1.00 51.57  ? 61  TYR C CB  1 
ATOM   1904 C CG  . TYR C 1 62 ? 20.349  -20.714 18.352  1.00 47.88  ? 61  TYR C CG  1 
ATOM   1905 C CD1 . TYR C 1 62 ? 20.166  -21.531 17.233  1.00 46.40  ? 61  TYR C CD1 1 
ATOM   1906 C CD2 . TYR C 1 62 ? 19.587  -19.550 18.450  1.00 47.48  ? 61  TYR C CD2 1 
ATOM   1907 C CE1 . TYR C 1 62 ? 19.257  -21.182 16.236  1.00 44.39  ? 61  TYR C CE1 1 
ATOM   1908 C CE2 . TYR C 1 62 ? 18.686  -19.190 17.458  1.00 50.37  ? 61  TYR C CE2 1 
ATOM   1909 C CZ  . TYR C 1 62 ? 18.519  -20.009 16.350  1.00 46.36  ? 61  TYR C CZ  1 
ATOM   1910 O OH  . TYR C 1 62 ? 17.633  -19.632 15.375  1.00 46.71  ? 61  TYR C OH  1 
ATOM   1911 N N   . ASP C 1 63 ? 23.306  -18.796 18.891  1.00 56.96  ? 62  ASP C N   1 
ATOM   1912 C CA  . ASP C 1 63 ? 23.660  -17.532 18.255  1.00 58.37  ? 62  ASP C CA  1 
ATOM   1913 C C   . ASP C 1 63 ? 24.993  -17.615 17.524  1.00 52.55  ? 62  ASP C C   1 
ATOM   1914 O O   . ASP C 1 63 ? 25.122  -17.073 16.425  1.00 59.97  ? 62  ASP C O   1 
ATOM   1915 C CB  . ASP C 1 63 ? 23.579  -16.355 19.211  1.00 62.60  ? 62  ASP C CB  1 
ATOM   1916 C CG  . ASP C 1 63 ? 22.269  -15.593 19.099  1.00 78.69  ? 62  ASP C CG  1 
ATOM   1917 O OD1 . ASP C 1 63 ? 22.108  -14.859 18.092  1.00 80.68  ? 62  ASP C OD1 1 
ATOM   1918 O OD2 . ASP C 1 63 ? 21.403  -15.787 19.983  1.00 79.16  ? 62  ASP C OD2 1 
ATOM   1919 N N   . LYS C 1 64 ? 25.959  -18.312 18.124  1.00 44.39  ? 63  LYS C N   1 
ATOM   1920 C CA  . LYS C 1 64 ? 27.310  -18.377 17.590  1.00 46.95  ? 63  LYS C CA  1 
ATOM   1921 C C   . LYS C 1 64 ? 27.349  -19.273 16.351  1.00 46.93  ? 63  LYS C C   1 
ATOM   1922 O O   . LYS C 1 64 ? 28.104  -19.004 15.420  1.00 42.99  ? 63  LYS C O   1 
ATOM   1923 C CB  . LYS C 1 64 ? 28.294  -18.834 18.675  1.00 50.81  ? 63  LYS C CB  1 
ATOM   1924 N N   . SER C 1 65 ? 26.494  -20.312 16.299  1.00 42.52  ? 64  SER C N   1 
ATOM   1925 C CA  . SER C 1 65 ? 26.709  -21.321 15.267  1.00 43.20  ? 64  SER C CA  1 
ATOM   1926 C C   . SER C 1 65 ? 25.526  -21.437 14.297  1.00 41.97  ? 64  SER C C   1 
ATOM   1927 O O   . SER C 1 65 ? 25.591  -22.215 13.354  1.00 40.65  ? 64  SER C O   1 
ATOM   1928 C CB  . SER C 1 65 ? 27.106  -22.657 15.866  1.00 46.87  ? 64  SER C CB  1 
ATOM   1929 O OG  . SER C 1 65 ? 26.017  -23.177 16.619  1.00 44.24  ? 64  SER C OG  1 
ATOM   1930 N N   . LYS C 1 66 ? 24.470  -20.640 14.493  1.00 38.01  ? 65  LYS C N   1 
ATOM   1931 C CA  . LYS C 1 66 ? 23.294  -20.748 13.633  1.00 43.72  ? 65  LYS C CA  1 
ATOM   1932 C C   . LYS C 1 66 ? 23.621  -20.486 12.161  1.00 44.64  ? 65  LYS C C   1 
ATOM   1933 O O   . LYS C 1 66 ? 23.015  -21.108 11.294  1.00 41.43  ? 65  LYS C O   1 
ATOM   1934 C CB  . LYS C 1 66 ? 22.090  -19.915 14.077  1.00 45.08  ? 65  LYS C CB  1 
ATOM   1935 C CG  . LYS C 1 66 ? 22.398  -18.435 14.171  1.00 42.70  ? 65  LYS C CG  1 
ATOM   1936 C CD  . LYS C 1 66 ? 21.093  -17.659 14.280  1.00 54.60  ? 65  LYS C CD  1 
ATOM   1937 C CE  . LYS C 1 66 ? 21.370  -16.221 14.573  1.00 54.00  ? 65  LYS C CE  1 
ATOM   1938 N NZ  . LYS C 1 66 ? 20.123  -15.650 15.072  1.00 56.13  ? 65  LYS C NZ  1 
ATOM   1939 N N   . ASP C 1 67 ? 24.595  -19.611 11.868  1.00 41.69  ? 66  ASP C N   1 
ATOM   1940 C CA  . ASP C 1 67 ? 24.962  -19.356 10.475  1.00 45.26  ? 66  ASP C CA  1 
ATOM   1941 C C   . ASP C 1 67 ? 25.371  -20.659 9.785   1.00 44.68  ? 66  ASP C C   1 
ATOM   1942 O O   . ASP C 1 67 ? 25.029  -20.880 8.622   1.00 41.87  ? 66  ASP C O   1 
ATOM   1943 C CB  . ASP C 1 67 ? 25.932  -18.182 10.305  1.00 46.15  ? 66  ASP C CB  1 
ATOM   1944 C CG  . ASP C 1 67 ? 27.334  -18.304 10.897  1.00 55.47  ? 66  ASP C CG  1 
ATOM   1945 O OD1 . ASP C 1 67 ? 27.626  -19.323 11.565  1.00 56.12  ? 66  ASP C OD1 1 
ATOM   1946 O OD2 . ASP C 1 67 ? 28.128  -17.349 10.719  1.00 56.41  ? 66  ASP C OD2 1 
ATOM   1947 N N   . LYS C 1 68 ? 26.049  -21.543 10.537  1.00 39.20  ? 67  LYS C N   1 
ATOM   1948 C CA  . LYS C 1 68 ? 26.526  -22.817 10.026  1.00 37.42  ? 67  LYS C CA  1 
ATOM   1949 C C   . LYS C 1 68 ? 25.475  -23.941 10.126  1.00 37.50  ? 67  LYS C C   1 
ATOM   1950 O O   . LYS C 1 68 ? 25.328  -24.714 9.186   1.00 40.87  ? 67  LYS C O   1 
ATOM   1951 C CB  . LYS C 1 68 ? 27.836  -23.115 10.758  1.00 38.53  ? 67  LYS C CB  1 
ATOM   1952 C CG  . LYS C 1 68 ? 28.597  -24.347 10.332  1.00 46.90  ? 67  LYS C CG  1 
ATOM   1953 C CD  . LYS C 1 68 ? 29.836  -24.527 11.213  1.00 52.55  ? 67  LYS C CD  1 
ATOM   1954 C CE  . LYS C 1 68 ? 30.453  -25.890 11.128  1.00 61.99  ? 67  LYS C CE  1 
ATOM   1955 N NZ  . LYS C 1 68 ? 30.809  -26.281 9.760   1.00 74.27  ? 67  LYS C NZ  1 
ATOM   1956 N N   . TYR C 1 69 ? 24.750  -24.074 11.247  1.00 34.47  ? 68  TYR C N   1 
ATOM   1957 C CA  . TYR C 1 69 ? 23.928  -25.275 11.401  1.00 33.10  ? 68  TYR C CA  1 
ATOM   1958 C C   . TYR C 1 69 ? 22.448  -24.983 11.190  1.00 34.58  ? 68  TYR C C   1 
ATOM   1959 O O   . TYR C 1 69 ? 21.646  -25.913 11.055  1.00 33.54  ? 68  TYR C O   1 
ATOM   1960 C CB  . TYR C 1 69 ? 24.065  -25.862 12.809  1.00 33.41  ? 68  TYR C CB  1 
ATOM   1961 C CG  . TYR C 1 69 ? 25.493  -26.289 13.111  1.00 33.63  ? 68  TYR C CG  1 
ATOM   1962 C CD1 . TYR C 1 69 ? 26.228  -27.064 12.215  1.00 37.00  ? 68  TYR C CD1 1 
ATOM   1963 C CD2 . TYR C 1 69 ? 26.121  -25.869 14.283  1.00 38.83  ? 68  TYR C CD2 1 
ATOM   1964 C CE1 . TYR C 1 69 ? 27.517  -27.488 12.507  1.00 38.80  ? 68  TYR C CE1 1 
ATOM   1965 C CE2 . TYR C 1 69 ? 27.413  -26.285 14.578  1.00 40.16  ? 68  TYR C CE2 1 
ATOM   1966 C CZ  . TYR C 1 69 ? 28.119  -27.075 13.686  1.00 39.11  ? 68  TYR C CZ  1 
ATOM   1967 O OH  . TYR C 1 69 ? 29.406  -27.426 14.019  1.00 41.66  ? 68  TYR C OH  1 
ATOM   1968 N N   . GLY C 1 70 ? 22.090  -23.700 11.209  1.00 34.04  ? 69  GLY C N   1 
ATOM   1969 C CA  . GLY C 1 70 ? 20.687  -23.332 11.116  1.00 35.29  ? 69  GLY C CA  1 
ATOM   1970 C C   . GLY C 1 70 ? 20.290  -23.197 9.653   1.00 37.98  ? 69  GLY C C   1 
ATOM   1971 O O   . GLY C 1 70 ? 20.224  -22.086 9.120   1.00 35.67  ? 69  GLY C O   1 
ATOM   1972 N N   . LYS C 1 71 ? 20.139  -24.356 9.010   1.00 36.57  ? 70  LYS C N   1 
ATOM   1973 C CA  . LYS C 1 71 ? 19.777  -24.453 7.604   1.00 37.48  ? 70  LYS C CA  1 
ATOM   1974 C C   . LYS C 1 71 ? 18.891  -25.683 7.495   1.00 37.97  ? 70  LYS C C   1 
ATOM   1975 O O   . LYS C 1 71 ? 19.077  -26.653 8.240   1.00 37.84  ? 70  LYS C O   1 
ATOM   1976 C CB  . LYS C 1 71 ? 21.025  -24.579 6.721   1.00 41.69  ? 70  LYS C CB  1 
ATOM   1977 C CG  . LYS C 1 71 ? 22.109  -25.490 7.279   1.00 45.28  ? 70  LYS C CG  1 
ATOM   1978 C CD  . LYS C 1 71 ? 23.133  -26.133 6.349   1.00 54.97  ? 70  LYS C CD  1 
ATOM   1979 C CE  . LYS C 1 71 ? 24.047  -26.998 7.166   1.00 53.27  ? 70  LYS C CE  1 
ATOM   1980 N N   . PRO C 1 72 ? 17.858  -25.652 6.628   1.00 32.03  ? 71  PRO C N   1 
ATOM   1981 C CA  . PRO C 1 72 ? 16.887  -26.740 6.589   1.00 28.12  ? 71  PRO C CA  1 
ATOM   1982 C C   . PRO C 1 72 ? 17.516  -28.078 6.220   1.00 31.93  ? 71  PRO C C   1 
ATOM   1983 O O   . PRO C 1 72 ? 18.538  -28.130 5.563   1.00 33.64  ? 71  PRO C O   1 
ATOM   1984 C CB  . PRO C 1 72 ? 15.925  -26.261 5.486   1.00 32.38  ? 71  PRO C CB  1 
ATOM   1985 C CG  . PRO C 1 72 ? 16.044  -24.779 5.584   1.00 33.62  ? 71  PRO C CG  1 
ATOM   1986 C CD  . PRO C 1 72 ? 17.526  -24.515 5.743   1.00 31.85  ? 71  PRO C CD  1 
ATOM   1987 N N   . ASN C 1 73 ? 16.851  -29.153 6.604   1.00 34.91  ? 72  ASN C N   1 
ATOM   1988 C CA  . ASN C 1 73 ? 17.134  -30.428 5.975   1.00 39.70  ? 72  ASN C CA  1 
ATOM   1989 C C   . ASN C 1 73 ? 15.893  -31.291 6.139   1.00 36.43  ? 72  ASN C C   1 
ATOM   1990 O O   . ASN C 1 73 ? 14.925  -30.862 6.762   1.00 38.46  ? 72  ASN C O   1 
ATOM   1991 C CB  . ASN C 1 73 ? 18.402  -31.071 6.515   1.00 43.35  ? 72  ASN C CB  1 
ATOM   1992 C CG  . ASN C 1 73 ? 18.219  -31.448 7.958   1.00 44.16  ? 72  ASN C CG  1 
ATOM   1993 O OD1 . ASN C 1 73 ? 17.357  -32.272 8.298   1.00 47.43  ? 72  ASN C OD1 1 
ATOM   1994 N ND2 . ASN C 1 73 ? 19.035  -30.859 8.803   1.00 46.01  ? 72  ASN C ND2 1 
ATOM   1995 N N   . LYS C 1 74 ? 15.944  -32.511 5.602   1.00 35.75  ? 73  LYS C N   1 
ATOM   1996 C CA  . LYS C 1 74 ? 14.695  -33.247 5.448   1.00 33.93  ? 73  LYS C CA  1 
ATOM   1997 C C   . LYS C 1 74 ? 14.487  -34.244 6.584   1.00 39.17  ? 73  LYS C C   1 
ATOM   1998 O O   . LYS C 1 74 ? 13.532  -35.008 6.539   1.00 38.46  ? 73  LYS C O   1 
ATOM   1999 C CB  . LYS C 1 74 ? 14.617  -33.927 4.071   1.00 37.20  ? 73  LYS C CB  1 
ATOM   2000 N N   . ARG C 1 75 ? 15.359  -34.249 7.609   1.00 35.66  ? 74  ARG C N   1 
ATOM   2001 C CA  . ARG C 1 75 ? 15.190  -35.211 8.697   1.00 33.96  ? 74  ARG C CA  1 
ATOM   2002 C C   . ARG C 1 75 ? 13.924  -34.893 9.495   1.00 37.89  ? 74  ARG C C   1 
ATOM   2003 O O   . ARG C 1 75 ? 13.545  -33.729 9.662   1.00 34.15  ? 74  ARG C O   1 
ATOM   2004 C CB  . ARG C 1 75 ? 16.424  -35.256 9.622   1.00 36.89  ? 74  ARG C CB  1 
ATOM   2005 C CG  . ARG C 1 75 ? 17.765  -35.363 8.898   1.00 43.98  ? 74  ARG C CG  1 
ATOM   2006 C CD  . ARG C 1 75 ? 18.117  -36.720 8.256   1.00 42.10  ? 74  ARG C CD  1 
ATOM   2007 N NE  . ARG C 1 75 ? 18.121  -37.728 9.323   1.00 38.14  ? 74  ARG C NE  1 
ATOM   2008 C CZ  . ARG C 1 75 ? 19.268  -38.166 9.886   1.00 35.46  ? 74  ARG C CZ  1 
ATOM   2009 N NH1 . ARG C 1 75 ? 19.227  -38.777 11.044  1.00 36.29  ? 74  ARG C NH1 1 
ATOM   2010 N NH2 . ARG C 1 75 ? 20.441  -37.876 9.337   1.00 36.30  ? 74  ARG C NH2 1 
ATOM   2011 N N   . LYS C 1 76 ? 13.283  -35.951 10.010  1.00 38.03  ? 75  LYS C N   1 
ATOM   2012 C CA  . LYS C 1 76 ? 11.997  -35.839 10.687  1.00 43.51  ? 75  LYS C CA  1 
ATOM   2013 C C   . LYS C 1 76 ? 12.049  -34.823 11.824  1.00 38.72  ? 75  LYS C C   1 
ATOM   2014 O O   . LYS C 1 76 ? 12.795  -34.967 12.801  1.00 34.47  ? 75  LYS C O   1 
ATOM   2015 C CB  . LYS C 1 76 ? 11.362  -37.171 11.119  1.00 44.14  ? 75  LYS C CB  1 
ATOM   2016 C CG  . LYS C 1 76 ? 9.835   -37.210 10.970  1.00 54.49  ? 75  LYS C CG  1 
ATOM   2017 C CD  . LYS C 1 76 ? 9.064   -37.903 12.094  1.00 63.13  ? 75  LYS C CD  1 
ATOM   2018 N N   . GLY C 1 77 ? 11.206  -33.795 11.698  1.00 37.11  ? 76  GLY C N   1 
ATOM   2019 C CA  . GLY C 1 77 ? 11.005  -32.874 12.800  1.00 31.15  ? 76  GLY C CA  1 
ATOM   2020 C C   . GLY C 1 77 ? 12.010  -31.720 12.761  1.00 29.95  ? 76  GLY C C   1 
ATOM   2021 O O   . GLY C 1 77 ? 11.879  -30.778 13.537  1.00 35.68  ? 76  GLY C O   1 
ATOM   2022 N N   . PHE C 1 78 ? 12.965  -31.756 11.821  1.00 29.46  ? 77  PHE C N   1 
ATOM   2023 C CA  . PHE C 1 78 ? 14.061  -30.794 11.845  1.00 28.50  ? 77  PHE C CA  1 
ATOM   2024 C C   . PHE C 1 78 ? 13.585  -29.350 11.618  1.00 34.06  ? 77  PHE C C   1 
ATOM   2025 O O   . PHE C 1 78 ? 14.011  -28.411 12.308  1.00 31.70  ? 77  PHE C O   1 
ATOM   2026 C CB  . PHE C 1 78 ? 15.187  -31.154 10.866  1.00 34.02  ? 77  PHE C CB  1 
ATOM   2027 C CG  . PHE C 1 78 ? 16.476  -30.366 11.105  1.00 31.77  ? 77  PHE C CG  1 
ATOM   2028 C CD1 . PHE C 1 78 ? 16.665  -29.116 10.525  1.00 32.37  ? 77  PHE C CD1 1 
ATOM   2029 C CD2 . PHE C 1 78 ? 17.509  -30.897 11.879  1.00 28.33  ? 77  PHE C CD2 1 
ATOM   2030 C CE1 . PHE C 1 78 ? 17.836  -28.388 10.736  1.00 31.97  ? 77  PHE C CE1 1 
ATOM   2031 C CE2 . PHE C 1 78 ? 18.681  -30.167 12.094  1.00 30.38  ? 77  PHE C CE2 1 
ATOM   2032 C CZ  . PHE C 1 78 ? 18.842  -28.920 11.531  1.00 33.03  ? 77  PHE C CZ  1 
ATOM   2033 N N   . ASN C 1 79 ? 12.782  -29.168 10.568  1.00 30.86  ? 78  ASN C N   1 
ATOM   2034 C CA  . ASN C 1 79 ? 12.496  -27.820 10.100  1.00 35.42  ? 78  ASN C CA  1 
ATOM   2035 C C   . ASN C 1 79 ? 11.494  -27.196 11.053  1.00 31.76  ? 78  ASN C C   1 
ATOM   2036 O O   . ASN C 1 79 ? 11.585  -26.012 11.391  1.00 33.44  ? 78  ASN C O   1 
ATOM   2037 C CB  . ASN C 1 79 ? 12.010  -27.804 8.661   1.00 33.14  ? 78  ASN C CB  1 
ATOM   2038 C CG  . ASN C 1 79 ? 13.086  -28.260 7.714   1.00 31.08  ? 78  ASN C CG  1 
ATOM   2039 O OD1 . ASN C 1 79 ? 14.282  -28.045 7.973   1.00 30.46  ? 78  ASN C OD1 1 
ATOM   2040 N ND2 . ASN C 1 79 ? 12.661  -28.799 6.581   1.00 30.18  ? 78  ASN C ND2 1 
ATOM   2041 N N   . GLU C 1 80 ? 10.640  -28.044 11.611  1.00 34.28  ? 79  GLU C N   1 
ATOM   2042 C CA  . GLU C 1 80 ? 9.757   -27.535 12.649  1.00 33.09  ? 79  GLU C CA  1 
ATOM   2043 C C   . GLU C 1 80 ? 10.599  -27.133 13.857  1.00 38.54  ? 79  GLU C C   1 
ATOM   2044 O O   . GLU C 1 80 ? 10.287  -26.146 14.519  1.00 35.84  ? 79  GLU C O   1 
ATOM   2045 C CB  . GLU C 1 80 ? 8.678   -28.561 13.001  1.00 36.39  ? 79  GLU C CB  1 
ATOM   2046 C CG  . GLU C 1 80 ? 7.813   -28.078 14.160  1.00 37.79  ? 79  GLU C CG  1 
ATOM   2047 C CD  . GLU C 1 80 ? 6.534   -28.841 14.403  1.00 48.45  ? 79  GLU C CD  1 
ATOM   2048 O OE1 . GLU C 1 80 ? 6.323   -29.928 13.812  1.00 51.08  ? 79  GLU C OE1 1 
ATOM   2049 O OE2 . GLU C 1 80 ? 5.723   -28.303 15.184  1.00 49.99  ? 79  GLU C OE2 1 
ATOM   2050 N N   . GLY C 1 81 ? 11.670  -27.909 14.152  1.00 32.85  ? 80  GLY C N   1 
ATOM   2051 C CA  . GLY C 1 81 ? 12.596  -27.522 15.206  1.00 34.09  ? 80  GLY C CA  1 
ATOM   2052 C C   . GLY C 1 81 ? 13.284  -26.179 14.947  1.00 37.34  ? 80  GLY C C   1 
ATOM   2053 O O   . GLY C 1 81 ? 13.522  -25.416 15.875  1.00 33.83  ? 80  GLY C O   1 
ATOM   2054 N N   . LEU C 1 82 ? 13.669  -25.910 13.688  1.00 33.66  ? 81  LEU C N   1 
ATOM   2055 C CA  . LEU C 1 82 ? 14.298  -24.637 13.360  1.00 33.51  ? 81  LEU C CA  1 
ATOM   2056 C C   . LEU C 1 82 ? 13.308  -23.495 13.595  1.00 34.39  ? 81  LEU C C   1 
ATOM   2057 O O   . LEU C 1 82 ? 13.715  -22.399 13.984  1.00 35.31  ? 81  LEU C O   1 
ATOM   2058 C CB  . LEU C 1 82 ? 14.769  -24.578 11.906  1.00 33.38  ? 81  LEU C CB  1 
ATOM   2059 C CG  . LEU C 1 82 ? 15.980  -25.423 11.510  1.00 36.18  ? 81  LEU C CG  1 
ATOM   2060 C CD1 . LEU C 1 82 ? 16.185  -25.256 9.998   1.00 31.01  ? 81  LEU C CD1 1 
ATOM   2061 C CD2 . LEU C 1 82 ? 17.237  -25.014 12.233  1.00 31.74  ? 81  LEU C CD2 1 
ATOM   2062 N N   . TRP C 1 83 ? 12.027  -23.749 13.332  1.00 31.03  ? 82  TRP C N   1 
ATOM   2063 C CA  . TRP C 1 83 ? 11.032  -22.709 13.579  1.00 42.11  ? 82  TRP C CA  1 
ATOM   2064 C C   . TRP C 1 83 ? 10.961  -22.402 15.086  1.00 41.60  ? 82  TRP C C   1 
ATOM   2065 O O   . TRP C 1 83 ? 11.027  -21.233 15.496  1.00 39.49  ? 82  TRP C O   1 
ATOM   2066 C CB  . TRP C 1 83 ? 9.660   -23.092 13.008  1.00 39.47  ? 82  TRP C CB  1 
ATOM   2067 C CG  . TRP C 1 83 ? 8.678   -21.954 13.105  1.00 45.22  ? 82  TRP C CG  1 
ATOM   2068 C CD1 . TRP C 1 83 ? 8.494   -20.955 12.194  1.00 47.03  ? 82  TRP C CD1 1 
ATOM   2069 C CD2 . TRP C 1 83 ? 7.781   -21.665 14.202  1.00 44.53  ? 82  TRP C CD2 1 
ATOM   2070 N NE1 . TRP C 1 83 ? 7.533   -20.079 12.631  1.00 44.11  ? 82  TRP C NE1 1 
ATOM   2071 C CE2 . TRP C 1 83 ? 7.083   -20.481 13.859  1.00 45.52  ? 82  TRP C CE2 1 
ATOM   2072 C CE3 . TRP C 1 83 ? 7.505   -22.284 15.431  1.00 43.89  ? 82  TRP C CE3 1 
ATOM   2073 C CZ2 . TRP C 1 83 ? 6.133   -19.911 14.702  1.00 47.93  ? 82  TRP C CZ2 1 
ATOM   2074 C CZ3 . TRP C 1 83 ? 6.564   -21.716 16.269  1.00 49.21  ? 82  TRP C CZ3 1 
ATOM   2075 C CH2 . TRP C 1 83 ? 5.902   -20.539 15.911  1.00 50.36  ? 82  TRP C CH2 1 
ATOM   2076 N N   . GLU C 1 84 ? 10.876  -23.470 15.892  1.00 38.30  ? 83  GLU C N   1 
ATOM   2077 C CA  . GLU C 1 84 ? 10.745  -23.364 17.342  1.00 37.51  ? 83  GLU C CA  1 
ATOM   2078 C C   . GLU C 1 84 ? 11.906  -22.604 17.973  1.00 38.58  ? 83  GLU C C   1 
ATOM   2079 O O   . GLU C 1 84 ? 11.680  -21.779 18.871  1.00 43.16  ? 83  GLU C O   1 
ATOM   2080 C CB  . GLU C 1 84 ? 10.566  -24.727 18.020  1.00 33.78  ? 83  GLU C CB  1 
ATOM   2081 C CG  . GLU C 1 84 ? 9.237   -25.378 17.653  1.00 34.88  ? 83  GLU C CG  1 
ATOM   2082 C CD  . GLU C 1 84 ? 9.097   -26.775 18.196  1.00 42.86  ? 83  GLU C CD  1 
ATOM   2083 O OE1 . GLU C 1 84 ? 10.109  -27.274 18.737  1.00 38.73  ? 83  GLU C OE1 1 
ATOM   2084 O OE2 . GLU C 1 84 ? 8.009   -27.372 18.042  1.00 40.99  ? 83  GLU C OE2 1 
ATOM   2085 N N   . ILE C 1 85 ? 13.145  -22.863 17.523  1.00 35.84  ? 84  ILE C N   1 
ATOM   2086 C CA  . ILE C 1 85 ? 14.312  -22.264 18.166  1.00 36.71  ? 84  ILE C CA  1 
ATOM   2087 C C   . ILE C 1 85 ? 14.418  -20.749 17.929  1.00 39.04  ? 84  ILE C C   1 
ATOM   2088 O O   . ILE C 1 85 ? 14.885  -20.016 18.797  1.00 36.53  ? 84  ILE C O   1 
ATOM   2089 C CB  . ILE C 1 85 ? 15.613  -23.004 17.842  1.00 34.22  ? 84  ILE C CB  1 
ATOM   2090 C CG1 . ILE C 1 85 ? 16.677  -22.708 18.920  1.00 36.57  ? 84  ILE C CG1 1 
ATOM   2091 C CG2 . ILE C 1 85 ? 16.096  -22.741 16.406  1.00 35.33  ? 84  ILE C CG2 1 
ATOM   2092 C CD1 . ILE C 1 85 ? 17.957  -23.535 18.851  1.00 38.10  ? 84  ILE C CD1 1 
ATOM   2093 N N   . GLN C 1 86 ? 13.983  -20.291 16.752  1.00 36.77  ? 85  GLN C N   1 
ATOM   2094 C CA  . GLN C 1 86 ? 14.024  -18.881 16.404  1.00 39.73  ? 85  GLN C CA  1 
ATOM   2095 C C   . GLN C 1 86 ? 12.770  -18.145 16.880  1.00 38.46  ? 85  GLN C C   1 
ATOM   2096 O O   . GLN C 1 86 ? 12.852  -16.961 17.188  1.00 42.60  ? 85  GLN C O   1 
ATOM   2097 C CB  . GLN C 1 86 ? 14.193  -18.791 14.887  1.00 37.80  ? 85  GLN C CB  1 
ATOM   2098 C CG  . GLN C 1 86 ? 14.283  -17.376 14.323  1.00 35.94  ? 85  GLN C CG  1 
ATOM   2099 C CD  . GLN C 1 86 ? 14.664  -17.401 12.855  1.00 43.05  ? 85  GLN C CD  1 
ATOM   2100 O OE1 . GLN C 1 86 ? 14.551  -18.434 12.173  1.00 42.40  ? 85  GLN C OE1 1 
ATOM   2101 N NE2 . GLN C 1 86 ? 15.168  -16.275 12.367  1.00 44.36  ? 85  GLN C NE2 1 
ATOM   2102 N N   . ASN C 1 87 ? 11.628  -18.835 16.919  1.00 38.56  ? 86  ASN C N   1 
ATOM   2103 C CA  . ASN C 1 87 ? 10.336  -18.179 17.072  1.00 47.53  ? 86  ASN C CA  1 
ATOM   2104 C C   . ASN C 1 87 ? 9.701   -18.419 18.445  1.00 51.21  ? 86  ASN C C   1 
ATOM   2105 O O   . ASN C 1 87 ? 8.888   -17.616 18.880  1.00 48.13  ? 86  ASN C O   1 
ATOM   2106 C CB  . ASN C 1 87 ? 9.378   -18.509 15.934  1.00 45.42  ? 86  ASN C CB  1 
ATOM   2107 C CG  . ASN C 1 87 ? 9.896   -17.896 14.658  1.00 49.95  ? 86  ASN C CG  1 
ATOM   2108 O OD1 . ASN C 1 87 ? 9.919   -16.665 14.550  1.00 46.99  ? 86  ASN C OD1 1 
ATOM   2109 N ND2 . ASN C 1 87 ? 10.394  -18.711 13.735  1.00 42.53  ? 86  ASN C ND2 1 
ATOM   2110 N N   . ASN C 1 88 ? 10.026  -19.528 19.117  1.00 51.23  ? 87  ASN C N   1 
ATOM   2111 C CA  . ASN C 1 88 ? 9.298   -19.866 20.334  1.00 48.20  ? 87  ASN C CA  1 
ATOM   2112 C C   . ASN C 1 88 ? 10.179  -20.732 21.230  1.00 42.69  ? 87  ASN C C   1 
ATOM   2113 O O   . ASN C 1 88 ? 9.764   -21.826 21.620  1.00 51.92  ? 87  ASN C O   1 
ATOM   2114 C CB  . ASN C 1 88 ? 7.993   -20.599 20.021  1.00 50.97  ? 87  ASN C CB  1 
ATOM   2115 C CG  . ASN C 1 88 ? 7.003   -20.538 21.164  1.00 57.43  ? 87  ASN C CG  1 
ATOM   2116 O OD1 . ASN C 1 88 ? 7.175   -19.730 22.085  1.00 58.96  ? 87  ASN C OD1 1 
ATOM   2117 N ND2 . ASN C 1 88 ? 5.964   -21.363 21.115  1.00 50.00  ? 87  ASN C ND2 1 
ATOM   2118 N N   . PRO C 1 89 ? 11.416  -20.291 21.543  1.00 44.88  ? 88  PRO C N   1 
ATOM   2119 C CA  . PRO C 1 89 ? 12.419  -21.174 22.140  1.00 48.20  ? 88  PRO C CA  1 
ATOM   2120 C C   . PRO C 1 89 ? 12.119  -21.696 23.546  1.00 54.03  ? 88  PRO C C   1 
ATOM   2121 O O   . PRO C 1 89 ? 12.729  -22.681 23.973  1.00 46.33  ? 88  PRO C O   1 
ATOM   2122 C CB  . PRO C 1 89 ? 13.727  -20.370 22.072  1.00 47.55  ? 88  PRO C CB  1 
ATOM   2123 C CG  . PRO C 1 89 ? 13.270  -18.930 22.014  1.00 49.60  ? 88  PRO C CG  1 
ATOM   2124 C CD  . PRO C 1 89 ? 11.934  -18.941 21.282  1.00 48.19  ? 88  PRO C CD  1 
ATOM   2125 N N   . HIS C 1 90 ? 11.164  -21.061 24.243  1.00 53.12  ? 89  HIS C N   1 
ATOM   2126 C CA  . HIS C 1 90 ? 10.967  -21.375 25.654  1.00 56.37  ? 89  HIS C CA  1 
ATOM   2127 C C   . HIS C 1 90 ? 9.533   -21.802 25.982  1.00 59.49  ? 89  HIS C C   1 
ATOM   2128 O O   . HIS C 1 90 ? 9.153   -21.796 27.144  1.00 71.81  ? 89  HIS C O   1 
ATOM   2129 C CB  . HIS C 1 90 ? 11.524  -20.269 26.557  1.00 48.65  ? 89  HIS C CB  1 
ATOM   2130 C CG  . HIS C 1 90 ? 12.942  -19.861 26.285  1.00 45.87  ? 89  HIS C CG  1 
ATOM   2131 N ND1 . HIS C 1 90 ? 13.274  -18.612 25.809  1.00 48.25  ? 89  HIS C ND1 1 
ATOM   2132 C CD2 . HIS C 1 90 ? 14.116  -20.489 26.490  1.00 43.18  ? 89  HIS C CD2 1 
ATOM   2133 C CE1 . HIS C 1 90 ? 14.595  -18.505 25.682  1.00 42.22  ? 89  HIS C CE1 1 
ATOM   2134 N NE2 . HIS C 1 90 ? 15.133  -19.629 26.113  1.00 46.58  ? 89  HIS C NE2 1 
ATOM   2135 N N   . ALA C 1 91 ? 8.748   -22.213 24.978  1.00 66.65  ? 90  ALA C N   1 
ATOM   2136 C CA  . ALA C 1 91 ? 7.453   -22.846 25.211  1.00 70.08  ? 90  ALA C CA  1 
ATOM   2137 C C   . ALA C 1 91 ? 7.633   -24.279 25.729  1.00 76.63  ? 90  ALA C C   1 
ATOM   2138 O O   . ALA C 1 91 ? 8.757   -24.770 25.817  1.00 75.77  ? 90  ALA C O   1 
ATOM   2139 C CB  . ALA C 1 91 ? 6.603   -22.805 23.952  1.00 63.79  ? 90  ALA C CB  1 
ATOM   2140 N N   . SER C 1 92 ? 6.509   -24.958 26.016  1.00 74.37  ? 91  SER C N   1 
ATOM   2141 C CA  . SER C 1 92 ? 6.472   -26.150 26.857  1.00 77.48  ? 91  SER C CA  1 
ATOM   2142 C C   . SER C 1 92 ? 6.650   -27.443 26.062  1.00 76.23  ? 91  SER C C   1 
ATOM   2143 O O   . SER C 1 92 ? 7.413   -28.315 26.469  1.00 78.82  ? 91  SER C O   1 
ATOM   2144 C CB  . SER C 1 92 ? 5.196   -26.201 27.669  1.00 80.65  ? 91  SER C CB  1 
ATOM   2145 O OG  . SER C 1 92 ? 5.106   -25.081 28.536  1.00 83.96  ? 91  SER C OG  1 
ATOM   2146 N N   . TYR C 1 93 ? 5.874   -27.591 24.982  1.00 79.22  ? 92  TYR C N   1 
ATOM   2147 C CA  . TYR C 1 93 ? 5.933   -28.742 24.089  1.00 84.13  ? 92  TYR C CA  1 
ATOM   2148 C C   . TYR C 1 93 ? 5.811   -30.049 24.888  1.00 89.26  ? 92  TYR C C   1 
ATOM   2149 O O   . TYR C 1 93 ? 4.700   -30.355 25.381  1.00 96.43  ? 92  TYR C O   1 
ATOM   2150 C CB  . TYR C 1 93 ? 7.224   -28.703 23.263  1.00 81.33  ? 92  TYR C CB  1 
ATOM   2151 C CG  . TYR C 1 93 ? 7.508   -27.396 22.528  1.00 69.31  ? 92  TYR C CG  1 
ATOM   2152 C CD1 . TYR C 1 93 ? 6.756   -27.021 21.417  1.00 61.40  ? 92  TYR C CD1 1 
ATOM   2153 C CD2 . TYR C 1 93 ? 8.542   -26.550 22.924  1.00 66.84  ? 92  TYR C CD2 1 
ATOM   2154 C CE1 . TYR C 1 93 ? 7.003   -25.840 20.738  1.00 60.58  ? 92  TYR C CE1 1 
ATOM   2155 C CE2 . TYR C 1 93 ? 8.806   -25.369 22.245  1.00 64.67  ? 92  TYR C CE2 1 
ATOM   2156 C CZ  . TYR C 1 93 ? 8.035   -25.014 21.150  1.00 64.98  ? 92  TYR C CZ  1 
ATOM   2157 O OH  . TYR C 1 93 ? 8.271   -23.844 20.478  1.00 60.75  ? 92  TYR C OH  1 
HETATM 2158 S S   . SO4 D 2 .  ? 1.072   -33.486 1.827   1.00 111.03 ? 101 SO4 A S   1 
HETATM 2159 O O1  . SO4 D 2 .  ? 1.768   -34.099 0.723   1.00 101.24 ? 101 SO4 A O1  1 
HETATM 2160 O O2  . SO4 D 2 .  ? 0.951   -32.069 1.600   1.00 103.55 ? 101 SO4 A O2  1 
HETATM 2161 O O3  . SO4 D 2 .  ? -0.242  -34.066 1.939   1.00 117.64 ? 101 SO4 A O3  1 
HETATM 2162 O O4  . SO4 D 2 .  ? 1.807   -33.718 3.041   1.00 101.63 ? 101 SO4 A O4  1 
HETATM 2163 S S   . SO4 E 2 .  ? -9.407  -24.888 1.523   1.00 94.96  ? 102 SO4 A S   1 
HETATM 2164 O O1  . SO4 E 2 .  ? -9.424  -24.521 0.131   1.00 79.68  ? 102 SO4 A O1  1 
HETATM 2165 O O2  . SO4 E 2 .  ? -9.147  -23.721 2.329   1.00 83.84  ? 102 SO4 A O2  1 
HETATM 2166 O O3  . SO4 E 2 .  ? -10.686 -25.450 1.876   1.00 105.62 ? 102 SO4 A O3  1 
HETATM 2167 O O4  . SO4 E 2 .  ? -8.375  -25.867 1.760   1.00 91.91  ? 102 SO4 A O4  1 
HETATM 2168 C C1  . EDO F 3 .  ? 14.016  -19.482 -7.385  1.00 39.20  ? 103 EDO A C1  1 
HETATM 2169 O O1  . EDO F 3 .  ? 15.221  -18.729 -7.290  1.00 35.46  ? 103 EDO A O1  1 
HETATM 2170 C C2  . EDO F 3 .  ? 13.123  -18.955 -8.460  1.00 35.79  ? 103 EDO A C2  1 
HETATM 2171 O O2  . EDO F 3 .  ? 12.611  -17.658 -8.229  1.00 37.04  ? 103 EDO A O2  1 
HETATM 2172 C C10 . WO7 G 4 .  ? 0.866   -24.365 -3.381  0.70 45.09  ? 104 WO7 A C10 1 
HETATM 2173 C C01 . WO7 G 4 .  ? 2.028   -24.299 -6.070  0.70 41.11  ? 104 WO7 A C01 1 
HETATM 2174 C C02 . WO7 G 4 .  ? 1.050   -25.336 -5.621  0.70 42.19  ? 104 WO7 A C02 1 
HETATM 2175 C C05 . WO7 G 4 .  ? 0.519   -26.837 -3.735  0.70 43.66  ? 104 WO7 A C05 1 
HETATM 2176 C C06 . WO7 G 4 .  ? 1.696   -27.604 -3.125  0.70 38.49  ? 104 WO7 A C06 1 
HETATM 2177 C C07 . WO7 G 4 .  ? 2.315   -26.894 -1.947  0.70 38.64  ? 104 WO7 A C07 1 
HETATM 2178 C C09 . WO7 G 4 .  ? 1.683   -24.572 -2.113  0.70 45.05  ? 104 WO7 A C09 1 
HETATM 2179 N N04 . WO7 G 4 .  ? 0.864   -25.516 -4.292  0.70 39.35  ? 104 WO7 A N04 1 
HETATM 2180 N N08 . WO7 G 4 .  ? 2.812   -25.484 -2.261  0.70 40.90  ? 104 WO7 A N08 1 
HETATM 2181 O O03 . WO7 G 4 .  ? 0.424   -25.989 -6.426  0.70 50.60  ? 104 WO7 A O03 1 
HETATM 2182 S S   . SO4 H 2 .  ? 9.026   -29.336 5.956   1.00 64.37  ? 105 SO4 A S   1 
HETATM 2183 O O1  . SO4 H 2 .  ? 9.859   -28.514 5.151   1.00 58.85  ? 105 SO4 A O1  1 
HETATM 2184 O O2  . SO4 H 2 .  ? 8.632   -30.498 5.195   1.00 71.79  ? 105 SO4 A O2  1 
HETATM 2185 O O3  . SO4 H 2 .  ? 9.748   -29.748 7.138   1.00 75.49  ? 105 SO4 A O3  1 
HETATM 2186 O O4  . SO4 H 2 .  ? 7.838   -28.610 6.328   1.00 81.50  ? 105 SO4 A O4  1 
HETATM 2187 C C1  . EDO I 3 .  ? 17.153  -16.111 -24.273 1.00 50.39  ? 101 EDO B C1  1 
HETATM 2188 O O1  . EDO I 3 .  ? 18.322  -16.862 -24.585 1.00 61.93  ? 101 EDO B O1  1 
HETATM 2189 C C2  . EDO I 3 .  ? 16.959  -15.014 -25.265 1.00 50.92  ? 101 EDO B C2  1 
HETATM 2190 O O2  . EDO I 3 .  ? 17.906  -13.978 -25.050 1.00 49.10  ? 101 EDO B O2  1 
HETATM 2191 S S   . SO4 J 2 .  ? 7.709   -8.523  -24.865 1.00 86.34  ? 102 SO4 B S   1 
HETATM 2192 O O1  . SO4 J 2 .  ? 8.823   -8.662  -25.766 1.00 49.34  ? 102 SO4 B O1  1 
HETATM 2193 O O2  . SO4 J 2 .  ? 6.520   -9.074  -25.492 1.00 63.86  ? 102 SO4 B O2  1 
HETATM 2194 O O3  . SO4 J 2 .  ? 7.928   -9.243  -23.602 1.00 55.57  ? 102 SO4 B O3  1 
HETATM 2195 O O4  . SO4 J 2 .  ? 7.568   -7.095  -24.619 1.00 62.77  ? 102 SO4 B O4  1 
HETATM 2196 S S   . SO4 K 2 .  ? 14.566  -27.110 -26.532 1.00 58.08  ? 103 SO4 B S   1 
HETATM 2197 O O1  . SO4 K 2 .  ? 15.887  -26.737 -26.119 1.00 58.96  ? 103 SO4 B O1  1 
HETATM 2198 O O2  . SO4 K 2 .  ? 14.656  -28.320 -27.311 1.00 62.89  ? 103 SO4 B O2  1 
HETATM 2199 O O3  . SO4 K 2 .  ? 13.745  -27.344 -25.369 1.00 68.86  ? 103 SO4 B O3  1 
HETATM 2200 O O4  . SO4 K 2 .  ? 13.972  -26.069 -27.324 1.00 54.68  ? 103 SO4 B O4  1 
HETATM 2201 S S   . SO4 L 2 .  ? 29.363  -37.935 12.241  1.00 108.45 ? 101 SO4 C S   1 
HETATM 2202 O O1  . SO4 L 2 .  ? 30.636  -37.414 11.810  1.00 100.42 ? 101 SO4 C O1  1 
HETATM 2203 O O2  . SO4 L 2 .  ? 28.318  -37.029 11.847  1.00 106.21 ? 101 SO4 C O2  1 
HETATM 2204 O O3  . SO4 L 2 .  ? 29.129  -39.223 11.642  1.00 95.58  ? 101 SO4 C O3  1 
HETATM 2205 O O4  . SO4 L 2 .  ? 29.367  -38.071 13.673  1.00 114.21 ? 101 SO4 C O4  1 
HETATM 2206 C C10 . WO7 M 4 .  ? 17.222  -38.736 17.721  0.60 44.62  ? 102 WO7 C C10 1 
HETATM 2207 C C01 . WO7 M 4 .  ? 16.606  -37.012 21.032  0.60 33.44  ? 102 WO7 C C01 1 
HETATM 2208 C C02 . WO7 M 4 .  ? 16.940  -38.088 20.051  0.60 37.46  ? 102 WO7 C C02 1 
HETATM 2209 C C05 . WO7 M 4 .  ? 17.669  -36.363 18.394  0.60 43.23  ? 102 WO7 C C05 1 
HETATM 2210 C C06 . WO7 M 4 .  ? 16.627  -35.633 17.552  0.60 38.55  ? 102 WO7 C C06 1 
HETATM 2211 C C07 . WO7 M 4 .  ? 16.438  -36.321 16.219  0.60 31.11  ? 102 WO7 C C07 1 
HETATM 2212 C C09 . WO7 M 4 .  ? 15.853  -38.769 17.005  0.60 37.00  ? 102 WO7 C C09 1 
HETATM 2213 N N04 . WO7 M 4 .  ? 17.281  -37.726 18.787  0.60 40.72  ? 102 WO7 C N04 1 
HETATM 2214 N N08 . WO7 M 4 .  ? 15.505  -37.467 16.282  0.60 36.38  ? 102 WO7 C N08 1 
HETATM 2215 O O03 . WO7 M 4 .  ? 16.909  -39.261 20.379  0.60 42.67  ? 102 WO7 C O03 1 
HETATM 2216 O O   . HOH N 5 .  ? 8.256   -32.255 4.204   1.00 63.50  ? 201 HOH A O   1 
HETATM 2217 O O   . HOH N 5 .  ? 5.355   -29.054 6.933   1.00 57.99  ? 202 HOH A O   1 
HETATM 2218 O O   . HOH N 5 .  ? -5.639  -13.443 -16.718 1.00 55.24  ? 203 HOH A O   1 
HETATM 2219 O O   . HOH N 5 .  ? 14.363  -29.466 4.089   1.00 47.25  ? 204 HOH A O   1 
HETATM 2220 O O   . HOH N 5 .  ? -2.269  3.167   -2.038  1.00 51.88  ? 205 HOH A O   1 
HETATM 2221 O O   . HOH N 5 .  ? 10.994  -29.629 3.258   1.00 43.24  ? 206 HOH A O   1 
HETATM 2222 O O   . HOH N 5 .  ? 0.055   -33.704 4.858   1.00 58.35  ? 207 HOH A O   1 
HETATM 2223 O O   . HOH N 5 .  ? 12.014  -15.861 -12.257 1.00 65.72  ? 208 HOH A O   1 
HETATM 2224 O O   . HOH N 5 .  ? 0.615   -10.514 -15.473 1.00 46.16  ? 209 HOH A O   1 
HETATM 2225 O O   . HOH N 5 .  ? 11.068  -23.724 9.833   1.00 39.89  ? 210 HOH A O   1 
HETATM 2226 O O   . HOH N 5 .  ? 8.135   -17.851 -16.034 1.00 51.48  ? 211 HOH A O   1 
HETATM 2227 O O   . HOH N 5 .  ? 9.156   -18.185 -10.920 1.00 37.01  ? 212 HOH A O   1 
HETATM 2228 O O   . HOH N 5 .  ? -6.819  -22.079 -5.639  1.00 60.92  ? 213 HOH A O   1 
HETATM 2229 O O   . HOH N 5 .  ? -7.703  -17.089 6.728   1.00 52.58  ? 214 HOH A O   1 
HETATM 2230 O O   . HOH N 5 .  ? 14.096  -15.776 -9.204  1.00 35.06  ? 215 HOH A O   1 
HETATM 2231 O O   . HOH N 5 .  ? -4.231  -21.025 6.176   1.00 43.33  ? 216 HOH A O   1 
HETATM 2232 O O   . HOH N 5 .  ? 7.108   -10.598 -12.089 1.00 43.70  ? 217 HOH A O   1 
HETATM 2233 O O   . HOH N 5 .  ? 15.884  -24.624 1.838   1.00 37.83  ? 218 HOH A O   1 
HETATM 2234 O O   . HOH N 5 .  ? 12.993  -11.901 8.050   1.00 54.77  ? 219 HOH A O   1 
HETATM 2235 O O   . HOH N 5 .  ? -3.693  -10.776 6.769   1.00 38.43  ? 220 HOH A O   1 
HETATM 2236 O O   . HOH N 5 .  ? 9.952   -13.071 9.658   1.00 42.83  ? 221 HOH A O   1 
HETATM 2237 O O   . HOH N 5 .  ? -0.454  -31.552 -3.263  1.00 60.18  ? 222 HOH A O   1 
HETATM 2238 O O   . HOH N 5 .  ? 2.532   -25.209 -9.989  1.00 40.36  ? 223 HOH A O   1 
HETATM 2239 O O   . HOH N 5 .  ? 4.500   -3.548  -3.299  1.00 36.63  ? 224 HOH A O   1 
HETATM 2240 O O   . HOH N 5 .  ? 4.829   -1.474  -6.345  1.00 40.92  ? 225 HOH A O   1 
HETATM 2241 O O   . HOH N 5 .  ? -7.987  -15.879 -1.005  1.00 39.51  ? 226 HOH A O   1 
HETATM 2242 O O   . HOH N 5 .  ? 1.514   -18.253 -18.625 1.00 63.96  ? 227 HOH A O   1 
HETATM 2243 O O   . HOH N 5 .  ? 4.649   -7.827  1.112   1.00 38.34  ? 228 HOH A O   1 
HETATM 2244 O O   . HOH N 5 .  ? -0.959  -5.612  -7.295  1.00 32.96  ? 229 HOH A O   1 
HETATM 2245 O O   . HOH N 5 .  ? -5.732  -19.689 -5.495  1.00 41.04  ? 230 HOH A O   1 
HETATM 2246 O O   . HOH N 5 .  ? 9.473   -22.788 -9.446  1.00 35.82  ? 231 HOH A O   1 
HETATM 2247 O O   . HOH N 5 .  ? 10.804  -5.125  -7.688  1.00 35.47  ? 232 HOH A O   1 
HETATM 2248 O O   . HOH N 5 .  ? 0.179   -28.516 -7.414  1.00 71.04  ? 233 HOH A O   1 
HETATM 2249 O O   . HOH N 5 .  ? 13.135  -28.185 -4.587  1.00 55.69  ? 234 HOH A O   1 
HETATM 2250 O O   . HOH N 5 .  ? -0.522  -29.253 10.364  1.00 53.84  ? 235 HOH A O   1 
HETATM 2251 O O   . HOH N 5 .  ? 0.257   -23.171 9.382   1.00 48.35  ? 236 HOH A O   1 
HETATM 2252 O O   . HOH N 5 .  ? -4.432  -25.866 -5.393  1.00 53.70  ? 237 HOH A O   1 
HETATM 2253 O O   . HOH N 5 .  ? 9.709   -6.052  -1.644  1.00 38.18  ? 238 HOH A O   1 
HETATM 2254 O O   . HOH N 5 .  ? 16.721  -18.291 -9.582  1.00 56.91  ? 239 HOH A O   1 
HETATM 2255 O O   . HOH N 5 .  ? 15.798  -12.077 -5.280  1.00 35.26  ? 240 HOH A O   1 
HETATM 2256 O O   . HOH N 5 .  ? -8.428  -21.118 -1.118  1.00 40.39  ? 241 HOH A O   1 
HETATM 2257 O O   . HOH N 5 .  ? 1.781   0.640   -7.475  1.00 46.79  ? 242 HOH A O   1 
HETATM 2258 O O   . HOH N 5 .  ? 3.921   -34.809 4.497   1.00 59.84  ? 243 HOH A O   1 
HETATM 2259 O O   . HOH N 5 .  ? -0.709  -20.932 6.994   1.00 34.73  ? 244 HOH A O   1 
HETATM 2260 O O   . HOH N 5 .  ? 11.500  -11.903 5.894   1.00 36.65  ? 245 HOH A O   1 
HETATM 2261 O O   . HOH N 5 .  ? 2.563   -6.363  5.555   1.00 38.55  ? 246 HOH A O   1 
HETATM 2262 O O   . HOH N 5 .  ? 13.355  -11.973 -4.217  1.00 24.56  ? 247 HOH A O   1 
HETATM 2263 O O   . HOH N 5 .  ? -1.692  -22.072 -0.584  1.00 31.29  ? 248 HOH A O   1 
HETATM 2264 O O   . HOH N 5 .  ? 17.216  -12.874 1.381   1.00 21.40  ? 249 HOH A O   1 
HETATM 2265 O O   . HOH N 5 .  ? -5.685  -15.861 -7.989  1.00 31.28  ? 250 HOH A O   1 
HETATM 2266 O O   . HOH N 5 .  ? 11.514  -12.327 -6.159  1.00 28.83  ? 251 HOH A O   1 
HETATM 2267 O O   . HOH N 5 .  ? 1.920   -4.780  -10.365 1.00 42.51  ? 252 HOH A O   1 
HETATM 2268 O O   . HOH N 5 .  ? 12.885  -9.457  -7.273  1.00 49.00  ? 253 HOH A O   1 
HETATM 2269 O O   . HOH N 5 .  ? 3.246   -29.503 -0.559  1.00 40.71  ? 254 HOH A O   1 
HETATM 2270 O O   . HOH N 5 .  ? 7.902   -7.850  1.203   1.00 34.05  ? 255 HOH A O   1 
HETATM 2271 O O   . HOH N 5 .  ? 11.280  -6.037  -3.876  1.00 49.85  ? 256 HOH A O   1 
HETATM 2272 O O   . HOH N 5 .  ? -7.959  -16.691 1.847   1.00 45.20  ? 257 HOH A O   1 
HETATM 2273 O O   . HOH N 5 .  ? 1.777   -10.461 11.774  1.00 39.71  ? 258 HOH A O   1 
HETATM 2274 O O   . HOH N 5 .  ? -1.421  -7.470  11.501  1.00 49.59  ? 259 HOH A O   1 
HETATM 2275 O O   . HOH N 5 .  ? 8.954   -16.483 -13.050 1.00 40.33  ? 260 HOH A O   1 
HETATM 2276 O O   . HOH N 5 .  ? 9.172   -20.295 -18.289 1.00 56.73  ? 261 HOH A O   1 
HETATM 2277 O O   . HOH N 5 .  ? 16.577  -12.001 -16.882 1.00 48.79  ? 262 HOH A O   1 
HETATM 2278 O O   . HOH N 5 .  ? 15.288  -28.049 -0.684  1.00 53.71  ? 263 HOH A O   1 
HETATM 2279 O O   . HOH N 5 .  ? -6.094  -26.581 3.515   1.00 54.88  ? 264 HOH A O   1 
HETATM 2280 O O   . HOH N 5 .  ? -0.459  -20.486 11.433  1.00 56.05  ? 265 HOH A O   1 
HETATM 2281 O O   . HOH N 5 .  ? 2.930   -9.902  -13.363 1.00 45.80  ? 266 HOH A O   1 
HETATM 2282 O O   . HOH N 5 .  ? 5.254   -7.724  4.012   1.00 34.55  ? 267 HOH A O   1 
HETATM 2283 O O   . HOH N 5 .  ? -1.427  -11.842 11.305  1.00 40.06  ? 268 HOH A O   1 
HETATM 2284 O O   . HOH N 5 .  ? 8.119   -17.484 8.687   1.00 46.74  ? 269 HOH A O   1 
HETATM 2285 O O   . HOH N 5 .  ? 12.756  -13.352 -8.535  1.00 41.96  ? 270 HOH A O   1 
HETATM 2286 O O   . HOH N 5 .  ? -5.968  -12.654 6.735   1.00 38.86  ? 271 HOH A O   1 
HETATM 2287 O O   . HOH N 5 .  ? 21.334  -16.614 -3.522  1.00 33.07  ? 272 HOH A O   1 
HETATM 2288 O O   . HOH N 5 .  ? -6.299  -11.490 -11.376 1.00 45.57  ? 273 HOH A O   1 
HETATM 2289 O O   . HOH N 5 .  ? 6.565   -16.239 -14.863 1.00 57.97  ? 274 HOH A O   1 
HETATM 2290 O O   . HOH N 5 .  ? 6.313   -5.835  0.570   1.00 50.17  ? 275 HOH A O   1 
HETATM 2291 O O   . HOH N 5 .  ? 9.310   -2.761  -0.254  1.00 68.49  ? 276 HOH A O   1 
HETATM 2292 O O   . HOH N 5 .  ? 11.072  -7.805  0.385   1.00 27.83  ? 277 HOH A O   1 
HETATM 2293 O O   . HOH N 5 .  ? -3.768  -7.793  10.497  1.00 55.41  ? 278 HOH A O   1 
HETATM 2294 O O   . HOH N 5 .  ? -7.289  -11.447 -7.991  1.00 31.49  ? 279 HOH A O   1 
HETATM 2295 O O   . HOH N 5 .  ? 22.390  -16.694 -0.522  1.00 42.48  ? 280 HOH A O   1 
HETATM 2296 O O   . HOH N 5 .  ? 9.627   -27.713 -7.423  1.00 57.26  ? 281 HOH A O   1 
HETATM 2297 O O   . HOH N 5 .  ? 2.033   -24.753 14.830  1.00 65.65  ? 282 HOH A O   1 
HETATM 2298 O O   . HOH N 5 .  ? -11.065 -16.038 -3.661  1.00 57.06  ? 283 HOH A O   1 
HETATM 2299 O O   . HOH N 5 .  ? -8.002  -19.737 -3.381  1.00 51.21  ? 284 HOH A O   1 
HETATM 2300 O O   . HOH N 5 .  ? 16.833  -13.571 10.814  1.00 62.70  ? 285 HOH A O   1 
HETATM 2301 O O   . HOH N 5 .  ? 8.784   -9.206  -13.733 1.00 47.78  ? 286 HOH A O   1 
HETATM 2302 O O   . HOH N 5 .  ? -3.802  -10.993 9.633   1.00 55.79  ? 287 HOH A O   1 
HETATM 2303 O O   . HOH N 5 .  ? -4.145  -26.744 7.210   1.00 58.42  ? 288 HOH A O   1 
HETATM 2304 O O   . HOH N 5 .  ? -7.280  -14.049 -9.235  1.00 43.77  ? 289 HOH A O   1 
HETATM 2305 O O   . HOH N 5 .  ? -5.565  -23.611 -6.968  1.00 43.24  ? 290 HOH A O   1 
HETATM 2306 O O   . HOH N 5 .  ? 5.061   -7.227  -10.996 1.00 48.44  ? 291 HOH A O   1 
HETATM 2307 O O   . HOH N 5 .  ? -10.133 -28.383 -1.746  1.00 57.20  ? 292 HOH A O   1 
HETATM 2308 O O   . HOH N 5 .  ? -9.426  -19.280 1.302   1.00 50.97  ? 293 HOH A O   1 
HETATM 2309 O O   . HOH N 5 .  ? -6.394  -22.761 5.496   1.00 58.30  ? 294 HOH A O   1 
HETATM 2310 O O   . HOH N 5 .  ? -11.200 -13.330 -2.849  1.00 48.40  ? 295 HOH A O   1 
HETATM 2311 O O   . HOH N 5 .  ? 4.802   -9.723  -11.357 1.00 48.03  ? 296 HOH A O   1 
HETATM 2312 O O   . HOH N 5 .  ? 8.126   -8.241  4.565   1.00 40.41  ? 297 HOH A O   1 
HETATM 2313 O O   . HOH N 5 .  ? 7.885   -30.638 -2.191  1.00 55.45  ? 298 HOH A O   1 
HETATM 2314 O O   . HOH N 5 .  ? -6.862  -19.208 8.565   1.00 52.86  ? 299 HOH A O   1 
HETATM 2315 O O   . HOH N 5 .  ? -5.005  -20.899 -8.385  1.00 58.65  ? 300 HOH A O   1 
HETATM 2316 O O   . HOH N 5 .  ? 8.568   -22.541 -19.614 1.00 64.26  ? 301 HOH A O   1 
HETATM 2317 O O   . HOH N 5 .  ? 4.475   -3.247  1.785   1.00 67.09  ? 302 HOH A O   1 
HETATM 2318 O O   . HOH O 5 .  ? 10.195  -11.413 -38.240 1.00 59.27  ? 201 HOH B O   1 
HETATM 2319 O O   . HOH O 5 .  ? 20.003  -22.140 -23.402 1.00 56.51  ? 202 HOH B O   1 
HETATM 2320 O O   . HOH O 5 .  ? 27.784  -8.185  -29.009 1.00 44.11  ? 203 HOH B O   1 
HETATM 2321 O O   . HOH O 5 .  ? 6.775   -12.311 -26.233 1.00 38.57  ? 204 HOH B O   1 
HETATM 2322 O O   . HOH O 5 .  ? 26.081  -4.920  -33.694 1.00 59.26  ? 205 HOH B O   1 
HETATM 2323 O O   . HOH O 5 .  ? 30.189  -12.846 -45.765 1.00 65.33  ? 206 HOH B O   1 
HETATM 2324 O O   . HOH O 5 .  ? 10.386  -19.876 -43.275 1.00 53.93  ? 207 HOH B O   1 
HETATM 2325 O O   . HOH O 5 .  ? 25.077  -5.261  -29.960 1.00 44.71  ? 208 HOH B O   1 
HETATM 2326 O O   . HOH O 5 .  ? 21.166  -25.572 -29.974 1.00 58.85  ? 209 HOH B O   1 
HETATM 2327 O O   . HOH O 5 .  ? 30.973  -8.322  -30.158 1.00 58.73  ? 210 HOH B O   1 
HETATM 2328 O O   . HOH O 5 .  ? 6.305   -7.675  -32.361 1.00 67.81  ? 211 HOH B O   1 
HETATM 2329 O O   . HOH O 5 .  ? 30.407  -19.913 -40.379 1.00 38.12  ? 212 HOH B O   1 
HETATM 2330 O O   . HOH O 5 .  ? 20.852  -13.639 -42.735 1.00 45.86  ? 213 HOH B O   1 
HETATM 2331 O O   . HOH O 5 .  ? 12.986  -4.931  -41.882 1.00 52.77  ? 214 HOH B O   1 
HETATM 2332 O O   . HOH O 5 .  ? 25.570  -6.111  -35.958 1.00 43.98  ? 215 HOH B O   1 
HETATM 2333 O O   . HOH O 5 .  ? 24.530  -1.835  -36.588 1.00 52.94  ? 216 HOH B O   1 
HETATM 2334 O O   . HOH O 5 .  ? 17.600  -19.728 -42.108 1.00 61.50  ? 217 HOH B O   1 
HETATM 2335 O O   . HOH O 5 .  ? 10.658  -18.938 -33.048 1.00 32.14  ? 218 HOH B O   1 
HETATM 2336 O O   . HOH O 5 .  ? 34.656  -23.259 -30.092 1.00 55.85  ? 219 HOH B O   1 
HETATM 2337 O O   . HOH O 5 .  ? 27.939  -17.632 -25.095 1.00 48.93  ? 220 HOH B O   1 
HETATM 2338 O O   . HOH O 5 .  ? 23.613  -2.496  -29.191 1.00 46.81  ? 221 HOH B O   1 
HETATM 2339 O O   . HOH O 5 .  ? 26.399  -23.164 -31.171 1.00 39.97  ? 222 HOH B O   1 
HETATM 2340 O O   . HOH O 5 .  ? 21.583  3.445   -32.871 1.00 43.24  ? 223 HOH B O   1 
HETATM 2341 O O   . HOH O 5 .  ? 18.171  -0.675  -38.519 1.00 35.39  ? 224 HOH B O   1 
HETATM 2342 O O   . HOH O 5 .  ? 32.720  -18.827 -42.598 1.00 58.11  ? 225 HOH B O   1 
HETATM 2343 O O   . HOH O 5 .  ? 16.833  -19.410 -28.884 1.00 28.81  ? 226 HOH B O   1 
HETATM 2344 O O   . HOH O 5 .  ? 7.616   -12.589 -38.805 1.00 51.22  ? 227 HOH B O   1 
HETATM 2345 O O   . HOH O 5 .  ? 19.865  -25.654 -34.016 1.00 49.33  ? 228 HOH B O   1 
HETATM 2346 O O   . HOH O 5 .  ? 13.044  -22.252 -20.772 1.00 61.89  ? 229 HOH B O   1 
HETATM 2347 O O   . HOH O 5 .  ? 8.523   -27.779 -38.312 1.00 57.26  ? 230 HOH B O   1 
HETATM 2348 O O   . HOH O 5 .  ? 17.628  -3.690  -22.289 1.00 59.29  ? 231 HOH B O   1 
HETATM 2349 O O   . HOH O 5 .  ? 22.805  -23.199 -28.789 1.00 43.10  ? 232 HOH B O   1 
HETATM 2350 O O   . HOH O 5 .  ? 20.494  -10.205 -43.062 1.00 38.58  ? 233 HOH B O   1 
HETATM 2351 O O   . HOH O 5 .  ? 14.334  -6.422  -41.247 1.00 50.40  ? 234 HOH B O   1 
HETATM 2352 O O   . HOH O 5 .  ? 31.995  -21.162 -38.194 1.00 43.81  ? 235 HOH B O   1 
HETATM 2353 O O   . HOH O 5 .  ? 7.527   -18.430 -31.812 1.00 49.52  ? 236 HOH B O   1 
HETATM 2354 O O   . HOH O 5 .  ? 7.276   -19.150 -34.926 1.00 54.10  ? 237 HOH B O   1 
HETATM 2355 O O   . HOH O 5 .  ? 18.396  -26.004 -28.837 1.00 44.14  ? 238 HOH B O   1 
HETATM 2356 O O   . HOH O 5 .  ? 23.833  -4.308  -36.965 1.00 34.25  ? 239 HOH B O   1 
HETATM 2357 O O   . HOH O 5 .  ? 27.510  -10.781 -28.889 1.00 53.89  ? 240 HOH B O   1 
HETATM 2358 O O   . HOH O 5 .  ? 10.501  -16.931 -44.300 1.00 47.97  ? 241 HOH B O   1 
HETATM 2359 O O   . HOH O 5 .  ? 8.724   -8.640  -16.522 1.00 46.99  ? 242 HOH B O   1 
HETATM 2360 O O   . HOH O 5 .  ? 21.199  -6.617  -42.673 1.00 42.92  ? 243 HOH B O   1 
HETATM 2361 O O   . HOH O 5 .  ? 26.141  -0.478  -29.446 1.00 49.00  ? 244 HOH B O   1 
HETATM 2362 O O   . HOH O 5 .  ? 1.808   -12.954 -28.535 1.00 54.66  ? 245 HOH B O   1 
HETATM 2363 O O   . HOH O 5 .  ? 3.198   -8.567  -27.252 1.00 58.74  ? 246 HOH B O   1 
HETATM 2364 O O   . HOH O 5 .  ? 7.390   -8.055  -20.892 1.00 51.31  ? 247 HOH B O   1 
HETATM 2365 O O   . HOH O 5 .  ? 14.553  -24.634 -40.559 1.00 48.75  ? 248 HOH B O   1 
HETATM 2366 O O   . HOH O 5 .  ? 10.583  -21.873 -32.823 1.00 39.10  ? 249 HOH B O   1 
HETATM 2367 O O   . HOH O 5 .  ? 27.924  -25.042 -35.215 1.00 38.13  ? 250 HOH B O   1 
HETATM 2368 O O   . HOH O 5 .  ? 23.615  -11.399 -21.965 1.00 48.09  ? 251 HOH B O   1 
HETATM 2369 O O   . HOH O 5 .  ? 18.176  -16.003 -45.865 1.00 43.80  ? 252 HOH B O   1 
HETATM 2370 O O   . HOH O 5 .  ? 17.223  -9.709  -43.985 1.00 50.95  ? 253 HOH B O   1 
HETATM 2371 O O   . HOH O 5 .  ? 6.576   -20.631 -25.066 1.00 51.07  ? 254 HOH B O   1 
HETATM 2372 O O   . HOH O 5 .  ? 18.379  4.408   -34.367 1.00 39.94  ? 255 HOH B O   1 
HETATM 2373 O O   . HOH O 5 .  ? 19.830  -3.231  -22.945 1.00 68.87  ? 256 HOH B O   1 
HETATM 2374 O O   . HOH O 5 .  ? 24.746  -6.606  -42.835 1.00 50.98  ? 257 HOH B O   1 
HETATM 2375 O O   . HOH O 5 .  ? 7.695   -23.510 -24.367 1.00 65.10  ? 258 HOH B O   1 
HETATM 2376 O O   . HOH O 5 .  ? 39.288  -13.095 -39.334 1.00 70.33  ? 259 HOH B O   1 
HETATM 2377 O O   . HOH O 5 .  ? 17.664  -0.383  -25.767 1.00 61.79  ? 260 HOH B O   1 
HETATM 2378 O O   . HOH O 5 .  ? 20.121  3.760   -33.313 1.00 44.74  ? 261 HOH B O   1 
HETATM 2379 O O   . HOH O 5 .  ? 31.666  -12.064 -38.121 1.00 68.47  ? 262 HOH B O   1 
HETATM 2380 O O   . HOH O 5 .  ? 12.910  -20.378 -19.473 1.00 53.63  ? 263 HOH B O   1 
HETATM 2381 O O   . HOH O 5 .  ? 9.572   -6.358  -41.055 1.00 51.38  ? 264 HOH B O   1 
HETATM 2382 O O   . HOH O 5 .  ? 17.377  -25.820 -20.998 1.00 60.75  ? 265 HOH B O   1 
HETATM 2383 O O   . HOH O 5 .  ? 15.014  -8.065  -43.014 1.00 48.35  ? 266 HOH B O   1 
HETATM 2384 O O   . HOH O 5 .  ? 15.373  -22.063 -42.003 1.00 53.47  ? 267 HOH B O   1 
HETATM 2385 O O   . HOH O 5 .  ? 7.487   -10.060 -18.580 1.00 45.61  ? 268 HOH B O   1 
HETATM 2386 O O   . HOH O 5 .  ? 22.385  -29.418 -35.649 1.00 49.27  ? 269 HOH B O   1 
HETATM 2387 O O   . HOH P 5 .  ? 20.410  -19.890 30.065  1.00 58.14  ? 201 HOH C O   1 
HETATM 2388 O O   . HOH P 5 .  ? 12.469  -27.926 28.252  1.00 53.50  ? 202 HOH C O   1 
HETATM 2389 O O   . HOH P 5 .  ? 5.813   -26.506 16.750  1.00 57.71  ? 203 HOH C O   1 
HETATM 2390 O O   . HOH P 5 .  ? 33.313  -24.294 31.529  1.00 50.80  ? 204 HOH C O   1 
HETATM 2391 O O   . HOH P 5 .  ? 7.717   -31.473 12.509  1.00 46.69  ? 205 HOH C O   1 
HETATM 2392 O O   . HOH P 5 .  ? 8.871   -36.689 18.437  1.00 48.85  ? 206 HOH C O   1 
HETATM 2393 O O   . HOH P 5 .  ? 19.322  -20.225 10.558  1.00 40.66  ? 207 HOH C O   1 
HETATM 2394 O O   . HOH P 5 .  ? 23.075  -41.369 18.324  1.00 48.50  ? 208 HOH C O   1 
HETATM 2395 O O   . HOH P 5 .  ? 26.767  -37.671 9.963   1.00 39.68  ? 209 HOH C O   1 
HETATM 2396 O O   . HOH P 5 .  ? 26.767  -38.922 12.595  1.00 39.73  ? 210 HOH C O   1 
HETATM 2397 O O   . HOH P 5 .  ? 15.177  -21.019 12.361  1.00 42.32  ? 211 HOH C O   1 
HETATM 2398 O O   . HOH P 5 .  ? 30.378  -31.290 15.518  1.00 53.44  ? 212 HOH C O   1 
HETATM 2399 O O   . HOH P 5 .  ? 30.492  -17.514 9.616   1.00 50.14  ? 213 HOH C O   1 
HETATM 2400 O O   . HOH P 5 .  ? 20.090  -41.805 12.138  1.00 32.67  ? 214 HOH C O   1 
HETATM 2401 O O   . HOH P 5 .  ? 14.073  -37.091 14.058  1.00 46.40  ? 215 HOH C O   1 
HETATM 2402 O O   . HOH P 5 .  ? 17.796  -16.953 14.807  1.00 48.82  ? 216 HOH C O   1 
HETATM 2403 O O   . HOH P 5 .  ? 28.288  -37.253 15.993  1.00 46.38  ? 217 HOH C O   1 
HETATM 2404 O O   . HOH P 5 .  ? 12.774  -31.441 8.443   1.00 34.49  ? 218 HOH C O   1 
HETATM 2405 O O   . HOH P 5 .  ? 23.385  -18.295 21.559  1.00 60.48  ? 219 HOH C O   1 
HETATM 2406 O O   . HOH P 5 .  ? 15.893  -17.540 19.338  1.00 53.05  ? 220 HOH C O   1 
HETATM 2407 O O   . HOH P 5 .  ? 22.381  -28.542 11.132  1.00 32.51  ? 221 HOH C O   1 
HETATM 2408 O O   . HOH P 5 .  ? 31.242  -39.787 27.118  1.00 49.68  ? 222 HOH C O   1 
HETATM 2409 O O   . HOH P 5 .  ? 15.557  -41.528 14.362  1.00 64.26  ? 223 HOH C O   1 
HETATM 2410 O O   . HOH P 5 .  ? 31.995  -33.560 25.944  1.00 53.29  ? 224 HOH C O   1 
HETATM 2411 O O   . HOH P 5 .  ? 26.051  -17.569 13.868  1.00 52.17  ? 225 HOH C O   1 
HETATM 2412 O O   . HOH P 5 .  ? 20.965  -28.663 8.533   1.00 38.75  ? 226 HOH C O   1 
HETATM 2413 O O   . HOH P 5 .  ? 25.315  -31.318 10.769  1.00 36.45  ? 227 HOH C O   1 
HETATM 2414 O O   . HOH P 5 .  ? 22.130  -34.371 16.590  1.00 28.86  ? 228 HOH C O   1 
HETATM 2415 O O   . HOH P 5 .  ? 7.066   -18.011 10.783  1.00 42.39  ? 229 HOH C O   1 
HETATM 2416 O O   . HOH P 5 .  ? 20.930  -39.789 26.488  1.00 41.81  ? 230 HOH C O   1 
HETATM 2417 O O   . HOH P 5 .  ? 27.892  -37.355 25.073  1.00 54.53  ? 231 HOH C O   1 
HETATM 2418 O O   . HOH P 5 .  ? 25.715  -33.521 34.942  1.00 53.82  ? 232 HOH C O   1 
HETATM 2419 O O   . HOH P 5 .  ? 9.288   -18.845 23.764  1.00 58.00  ? 233 HOH C O   1 
HETATM 2420 O O   . HOH P 5 .  ? 26.055  -17.894 20.933  1.00 69.24  ? 234 HOH C O   1 
HETATM 2421 O O   . HOH P 5 .  ? 29.834  -39.686 31.440  1.00 42.28  ? 235 HOH C O   1 
HETATM 2422 O O   . HOH P 5 .  ? 30.294  -35.706 28.753  1.00 55.97  ? 236 HOH C O   1 
HETATM 2423 O O   . HOH P 5 .  ? 9.642   -30.305 10.131  1.00 36.56  ? 237 HOH C O   1 
HETATM 2424 O O   . HOH P 5 .  ? 14.330  -38.693 10.024  1.00 56.12  ? 238 HOH C O   1 
HETATM 2425 O O   . HOH P 5 .  ? 2.797   -28.329 14.628  1.00 57.74  ? 239 HOH C O   1 
HETATM 2426 O O   . HOH P 5 .  ? 31.454  -43.445 15.784  1.00 52.50  ? 240 HOH C O   1 
HETATM 2427 O O   . HOH P 5 .  ? 21.051  -29.541 4.746   1.00 61.97  ? 241 HOH C O   1 
HETATM 2428 O O   . HOH P 5 .  ? 20.141  -18.854 24.917  1.00 59.49  ? 242 HOH C O   1 
HETATM 2429 O O   . HOH P 5 .  ? 31.905  -43.266 11.858  1.00 49.19  ? 243 HOH C O   1 
HETATM 2430 O O   . HOH P 5 .  ? 25.583  -39.567 20.154  1.00 38.73  ? 244 HOH C O   1 
HETATM 2431 O O   . HOH P 5 .  ? 19.341  -26.765 2.930   1.00 55.86  ? 245 HOH C O   1 
HETATM 2432 O O   . HOH P 5 .  ? 20.992  -41.037 39.519  1.00 78.96  ? 246 HOH C O   1 
HETATM 2433 O O   . HOH P 5 .  ? 28.042  -15.054 12.891  1.00 61.12  ? 247 HOH C O   1 
HETATM 2434 O O   . HOH P 5 .  ? 30.366  -32.804 18.286  1.00 46.82  ? 248 HOH C O   1 
HETATM 2435 O O   . HOH P 5 .  ? 16.079  -38.458 11.815  1.00 57.02  ? 249 HOH C O   1 
HETATM 2436 O O   . HOH P 5 .  ? 22.459  -14.011 13.235  1.00 54.84  ? 250 HOH C O   1 
HETATM 2437 O O   . HOH P 5 .  ? 14.482  -22.310 28.099  1.00 73.55  ? 251 HOH C O   1 
HETATM 2438 O O   . HOH P 5 .  ? 29.874  -25.130 32.663  1.00 55.09  ? 252 HOH C O   1 
HETATM 2439 O O   . HOH P 5 .  ? 20.905  -12.839 13.206  1.00 46.23  ? 253 HOH C O   1 
HETATM 2440 O O   . HOH P 5 .  ? 29.275  -41.547 27.236  1.00 48.04  ? 254 HOH C O   1 
HETATM 2441 O O   . HOH P 5 .  ? 11.918  -21.092 10.751  1.00 43.41  ? 255 HOH C O   1 
HETATM 2442 O O   . HOH P 5 .  ? 17.193  -36.307 29.571  1.00 61.71  ? 256 HOH C O   1 
HETATM 2443 O O   . HOH P 5 .  ? 4.950   -24.186 18.538  1.00 58.84  ? 257 HOH C O   1 
HETATM 2444 O O   . HOH P 5 .  ? 32.250  -38.962 29.921  1.00 54.72  ? 258 HOH C O   1 
HETATM 2445 O O   . HOH P 5 .  ? 28.523  -41.418 30.000  1.00 52.09  ? 259 HOH C O   1 
HETATM 2446 O O   . HOH P 5 .  ? 37.608  -24.437 27.009  1.00 78.19  ? 260 HOH C O   1 
HETATM 2447 O O   . HOH P 5 .  ? 33.584  -44.446 15.256  1.00 42.33  ? 261 HOH C O   1 
# 
