data_7HGQ
# 
_entry.id   7HGQ 
# 
_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   7HGQ         pdb_00007hgq 10.2210/pdb7hgq/pdb 
WWPDB D_1001407452 ?            ?                   
# 
_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                        7HGQ 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn N,N,3,5-tetramethyl-1H-pyrazole-4-sulfonamide      203.262   1   ? ?    ? ? 
5 water       nat water                                              18.015    261 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                 SO4 
3 1,2-ETHANEDIOL                                EDO 
4 N,N,3,5-tetramethyl-1H-pyrazole-4-sulfonamide K2S 
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 
K2S non-polymer         . N,N,3,5-tetramethyl-1H-pyrazole-4-sulfonamide ?                 'C7 H13 N3 O2 S' 203.262 
LEU 'L-peptide linking' y LEUCINE                                       ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                        ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                    ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                 ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                       ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                        ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                 ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                     ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                      ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                        ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 29 ALA ALA B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        K2S 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   K2S 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 K2S 1   103 101 K2S LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 357 HOH HOH A . 
M 5 HOH 2   202 292 HOH HOH A . 
M 5 HOH 3   203 358 HOH HOH A . 
M 5 HOH 4   204 28  HOH HOH A . 
M 5 HOH 5   205 7   HOH HOH A . 
M 5 HOH 6   206 208 HOH HOH A . 
M 5 HOH 7   207 91  HOH HOH A . 
M 5 HOH 8   208 307 HOH HOH A . 
M 5 HOH 9   209 84  HOH HOH A . 
M 5 HOH 10  210 218 HOH HOH A . 
M 5 HOH 11  211 202 HOH HOH A . 
M 5 HOH 12  212 304 HOH HOH A . 
M 5 HOH 13  213 278 HOH HOH A . 
M 5 HOH 14  214 12  HOH HOH A . 
M 5 HOH 15  215 35  HOH HOH A . 
M 5 HOH 16  216 85  HOH HOH A . 
M 5 HOH 17  217 300 HOH HOH A . 
M 5 HOH 18  218 299 HOH HOH A . 
M 5 HOH 19  219 289 HOH HOH A . 
M 5 HOH 20  220 71  HOH HOH A . 
M 5 HOH 21  221 23  HOH HOH A . 
M 5 HOH 22  222 152 HOH HOH A . 
M 5 HOH 23  223 37  HOH HOH A . 
M 5 HOH 24  224 55  HOH HOH A . 
M 5 HOH 25  225 32  HOH HOH A . 
M 5 HOH 26  226 290 HOH HOH A . 
M 5 HOH 27  227 42  HOH HOH A . 
M 5 HOH 28  228 18  HOH HOH A . 
M 5 HOH 29  229 1   HOH HOH A . 
M 5 HOH 30  230 288 HOH HOH A . 
M 5 HOH 31  231 27  HOH HOH A . 
M 5 HOH 32  232 38  HOH HOH A . 
M 5 HOH 33  233 362 HOH HOH A . 
M 5 HOH 34  234 66  HOH HOH A . 
M 5 HOH 35  235 2   HOH HOH A . 
M 5 HOH 36  236 318 HOH HOH A . 
M 5 HOH 37  237 60  HOH HOH A . 
M 5 HOH 38  238 260 HOH HOH A . 
M 5 HOH 39  239 8   HOH HOH A . 
M 5 HOH 40  240 335 HOH HOH A . 
M 5 HOH 41  241 164 HOH HOH A . 
M 5 HOH 42  242 99  HOH HOH A . 
M 5 HOH 43  243 20  HOH HOH A . 
M 5 HOH 44  244 203 HOH HOH A . 
M 5 HOH 45  245 9   HOH HOH A . 
M 5 HOH 46  246 293 HOH HOH A . 
M 5 HOH 47  247 26  HOH HOH A . 
M 5 HOH 48  248 59  HOH HOH A . 
M 5 HOH 49  249 188 HOH HOH A . 
M 5 HOH 50  250 267 HOH HOH A . 
M 5 HOH 51  251 327 HOH HOH A . 
M 5 HOH 52  252 94  HOH HOH A . 
M 5 HOH 53  253 190 HOH HOH A . 
M 5 HOH 54  254 274 HOH HOH A . 
M 5 HOH 55  255 34  HOH HOH A . 
M 5 HOH 56  256 179 HOH HOH A . 
M 5 HOH 57  257 87  HOH HOH A . 
M 5 HOH 58  258 95  HOH HOH A . 
M 5 HOH 59  259 222 HOH HOH A . 
M 5 HOH 60  260 109 HOH HOH A . 
M 5 HOH 61  261 165 HOH HOH A . 
M 5 HOH 62  262 86  HOH HOH A . 
M 5 HOH 63  263 40  HOH HOH A . 
M 5 HOH 64  264 167 HOH HOH A . 
M 5 HOH 65  265 115 HOH HOH A . 
M 5 HOH 66  266 78  HOH HOH A . 
M 5 HOH 67  267 22  HOH HOH A . 
M 5 HOH 68  268 146 HOH HOH A . 
M 5 HOH 69  269 113 HOH HOH A . 
M 5 HOH 70  270 297 HOH HOH A . 
M 5 HOH 71  271 47  HOH HOH A . 
M 5 HOH 72  272 93  HOH HOH A . 
M 5 HOH 73  273 199 HOH HOH A . 
M 5 HOH 74  274 301 HOH HOH A . 
M 5 HOH 75  275 131 HOH HOH A . 
M 5 HOH 76  276 14  HOH HOH A . 
M 5 HOH 77  277 58  HOH HOH A . 
M 5 HOH 78  278 19  HOH HOH A . 
M 5 HOH 79  279 111 HOH HOH A . 
M 5 HOH 80  280 296 HOH HOH A . 
M 5 HOH 81  281 16  HOH HOH A . 
M 5 HOH 82  282 143 HOH HOH A . 
M 5 HOH 83  283 97  HOH HOH A . 
M 5 HOH 84  284 145 HOH HOH A . 
M 5 HOH 85  285 77  HOH HOH A . 
M 5 HOH 86  286 281 HOH HOH A . 
M 5 HOH 87  287 345 HOH HOH A . 
M 5 HOH 88  288 259 HOH HOH A . 
M 5 HOH 89  289 31  HOH HOH A . 
M 5 HOH 90  290 156 HOH HOH A . 
M 5 HOH 91  291 211 HOH HOH A . 
M 5 HOH 92  292 116 HOH HOH A . 
M 5 HOH 93  293 132 HOH HOH A . 
M 5 HOH 94  294 350 HOH HOH A . 
M 5 HOH 95  295 210 HOH HOH A . 
M 5 HOH 96  296 283 HOH HOH A . 
M 5 HOH 97  297 83  HOH HOH A . 
M 5 HOH 98  298 73  HOH HOH A . 
M 5 HOH 99  299 64  HOH HOH A . 
M 5 HOH 100 300 185 HOH HOH A . 
M 5 HOH 101 301 21  HOH HOH A . 
M 5 HOH 102 302 57  HOH HOH A . 
M 5 HOH 103 303 63  HOH HOH A . 
M 5 HOH 104 304 206 HOH HOH A . 
M 5 HOH 105 305 332 HOH HOH A . 
M 5 HOH 106 306 205 HOH HOH A . 
M 5 HOH 107 307 219 HOH HOH A . 
M 5 HOH 108 308 125 HOH HOH A . 
M 5 HOH 109 309 365 HOH HOH A . 
M 5 HOH 110 310 75  HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 46  HOH HOH B . 
N 5 HOH 3   203 69  HOH HOH B . 
N 5 HOH 4   204 316 HOH HOH B . 
N 5 HOH 5   205 329 HOH HOH B . 
N 5 HOH 6   206 6   HOH HOH B . 
N 5 HOH 7   207 24  HOH HOH B . 
N 5 HOH 8   208 364 HOH HOH B . 
N 5 HOH 9   209 351 HOH HOH B . 
N 5 HOH 10  210 272 HOH HOH B . 
N 5 HOH 11  211 123 HOH HOH B . 
N 5 HOH 12  212 10  HOH HOH B . 
N 5 HOH 13  213 153 HOH HOH B . 
N 5 HOH 14  214 258 HOH HOH B . 
N 5 HOH 15  215 54  HOH HOH B . 
N 5 HOH 16  216 89  HOH HOH B . 
N 5 HOH 17  217 163 HOH HOH B . 
N 5 HOH 18  218 224 HOH HOH B . 
N 5 HOH 19  219 279 HOH HOH B . 
N 5 HOH 20  220 68  HOH HOH B . 
N 5 HOH 21  221 150 HOH HOH B . 
N 5 HOH 22  222 17  HOH HOH B . 
N 5 HOH 23  223 137 HOH HOH B . 
N 5 HOH 24  224 5   HOH HOH B . 
N 5 HOH 25  225 96  HOH HOH B . 
N 5 HOH 26  226 333 HOH HOH B . 
N 5 HOH 27  227 242 HOH HOH B . 
N 5 HOH 28  228 13  HOH HOH B . 
N 5 HOH 29  229 347 HOH HOH B . 
N 5 HOH 30  230 25  HOH HOH B . 
N 5 HOH 31  231 303 HOH HOH B . 
N 5 HOH 32  232 261 HOH HOH B . 
N 5 HOH 33  233 320 HOH HOH B . 
N 5 HOH 34  234 61  HOH HOH B . 
N 5 HOH 35  235 169 HOH HOH B . 
N 5 HOH 36  236 98  HOH HOH B . 
N 5 HOH 37  237 74  HOH HOH B . 
N 5 HOH 38  238 315 HOH HOH B . 
N 5 HOH 39  239 36  HOH HOH B . 
N 5 HOH 40  240 184 HOH HOH B . 
N 5 HOH 41  241 280 HOH HOH B . 
N 5 HOH 42  242 249 HOH HOH B . 
N 5 HOH 43  243 331 HOH HOH B . 
N 5 HOH 44  244 117 HOH HOH B . 
N 5 HOH 45  245 119 HOH HOH B . 
N 5 HOH 46  246 309 HOH HOH B . 
N 5 HOH 47  247 175 HOH HOH B . 
N 5 HOH 48  248 182 HOH HOH B . 
N 5 HOH 49  249 101 HOH HOH B . 
N 5 HOH 50  250 79  HOH HOH B . 
N 5 HOH 51  251 104 HOH HOH B . 
N 5 HOH 52  252 120 HOH HOH B . 
N 5 HOH 53  253 214 HOH HOH B . 
N 5 HOH 54  254 201 HOH HOH B . 
N 5 HOH 55  255 197 HOH HOH B . 
N 5 HOH 56  256 72  HOH HOH B . 
N 5 HOH 57  257 70  HOH HOH B . 
N 5 HOH 58  258 177 HOH HOH B . 
N 5 HOH 59  259 340 HOH HOH B . 
N 5 HOH 60  260 334 HOH HOH B . 
N 5 HOH 61  261 160 HOH HOH B . 
N 5 HOH 62  262 44  HOH HOH B . 
N 5 HOH 63  263 217 HOH HOH B . 
N 5 HOH 64  264 76  HOH HOH B . 
N 5 HOH 65  265 360 HOH HOH B . 
N 5 HOH 66  266 343 HOH HOH B . 
N 5 HOH 67  267 223 HOH HOH B . 
N 5 HOH 68  268 348 HOH HOH B . 
N 5 HOH 69  269 291 HOH HOH B . 
N 5 HOH 70  270 170 HOH HOH B . 
N 5 HOH 71  271 341 HOH HOH B . 
N 5 HOH 72  272 312 HOH HOH B . 
N 5 HOH 73  273 313 HOH HOH B . 
N 5 HOH 74  274 172 HOH HOH B . 
N 5 HOH 75  275 353 HOH HOH B . 
N 5 HOH 76  276 322 HOH HOH B . 
N 5 HOH 77  277 314 HOH HOH B . 
N 5 HOH 78  278 92  HOH HOH B . 
N 5 HOH 79  279 349 HOH HOH B . 
N 5 HOH 80  280 359 HOH HOH B . 
N 5 HOH 81  281 107 HOH HOH B . 
N 5 HOH 82  282 310 HOH HOH B . 
N 5 HOH 83  283 355 HOH HOH B . 
O 5 HOH 1   201 305 HOH HOH C . 
O 5 HOH 2   202 254 HOH HOH C . 
O 5 HOH 3   203 15  HOH HOH C . 
O 5 HOH 4   204 45  HOH HOH C . 
O 5 HOH 5   205 90  HOH HOH C . 
O 5 HOH 6   206 134 HOH HOH C . 
O 5 HOH 7   207 321 HOH HOH C . 
O 5 HOH 8   208 336 HOH HOH C . 
O 5 HOH 9   209 346 HOH HOH C . 
O 5 HOH 10  210 269 HOH HOH C . 
O 5 HOH 11  211 294 HOH HOH C . 
O 5 HOH 12  212 326 HOH HOH C . 
O 5 HOH 13  213 325 HOH HOH C . 
O 5 HOH 14  214 142 HOH HOH C . 
O 5 HOH 15  215 102 HOH HOH C . 
O 5 HOH 16  216 41  HOH HOH C . 
O 5 HOH 17  217 287 HOH HOH C . 
O 5 HOH 18  218 122 HOH HOH C . 
O 5 HOH 19  219 173 HOH HOH C . 
O 5 HOH 20  220 126 HOH HOH C . 
O 5 HOH 21  221 284 HOH HOH C . 
O 5 HOH 22  222 4   HOH HOH C . 
O 5 HOH 23  223 49  HOH HOH C . 
O 5 HOH 24  224 118 HOH HOH C . 
O 5 HOH 25  225 189 HOH HOH C . 
O 5 HOH 26  226 103 HOH HOH C . 
O 5 HOH 27  227 67  HOH HOH C . 
O 5 HOH 28  228 168 HOH HOH C . 
O 5 HOH 29  229 298 HOH HOH C . 
O 5 HOH 30  230 275 HOH HOH C . 
O 5 HOH 31  231 342 HOH HOH C . 
O 5 HOH 32  232 352 HOH HOH C . 
O 5 HOH 33  233 356 HOH HOH C . 
O 5 HOH 34  234 48  HOH HOH C . 
O 5 HOH 35  235 148 HOH HOH C . 
O 5 HOH 36  236 82  HOH HOH C . 
O 5 HOH 37  237 171 HOH HOH C . 
O 5 HOH 38  238 56  HOH HOH C . 
O 5 HOH 39  239 319 HOH HOH C . 
O 5 HOH 40  240 354 HOH HOH C . 
O 5 HOH 41  241 65  HOH HOH C . 
O 5 HOH 42  242 53  HOH HOH C . 
O 5 HOH 43  243 135 HOH HOH C . 
O 5 HOH 44  244 226 HOH HOH C . 
O 5 HOH 45  245 43  HOH HOH C . 
O 5 HOH 46  246 161 HOH HOH C . 
O 5 HOH 47  247 139 HOH HOH C . 
O 5 HOH 48  248 317 HOH HOH C . 
O 5 HOH 49  249 324 HOH HOH C . 
O 5 HOH 50  250 149 HOH HOH C . 
O 5 HOH 51  251 151 HOH HOH C . 
O 5 HOH 52  252 198 HOH HOH C . 
O 5 HOH 53  253 130 HOH HOH C . 
O 5 HOH 54  254 328 HOH HOH C . 
O 5 HOH 55  255 295 HOH HOH C . 
O 5 HOH 56  256 62  HOH HOH C . 
O 5 HOH 57  257 209 HOH HOH C . 
O 5 HOH 58  258 344 HOH HOH C . 
O 5 HOH 59  259 270 HOH HOH C . 
O 5 HOH 60  260 323 HOH HOH C . 
O 5 HOH 61  261 330 HOH HOH C . 
O 5 HOH 62  262 361 HOH HOH C . 
O 5 HOH 63  263 271 HOH HOH C . 
O 5 HOH 64  264 108 HOH HOH C . 
O 5 HOH 65  265 339 HOH HOH C . 
O 5 HOH 66  266 246 HOH HOH C . 
O 5 HOH 67  267 337 HOH HOH C . 
O 5 HOH 68  268 363 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
8  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
9  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
17 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
18 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
19 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
20 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
21 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
22 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
23 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
24 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
25 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
26 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
27 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
28 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
29 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
30 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
31 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
32 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
33 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
34 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
35 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
36 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
37 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
38 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
39 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           7HGQ 
_cell.length_a           40.904 
_cell.length_b           41.172 
_cell.length_c           155.822 
_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                         7HGQ 
_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          7HGQ 
_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                     7HGQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             77.91 
_reflns.d_resolution_high            1.90 
_reflns.number_obs                   16809 
_reflns.percent_possible_obs         77.2 
_reflns.pdbx_Rmerge_I_obs            0.089 
_reflns.pdbx_netI_over_sigmaI        8.9 
_reflns.pdbx_redundancy              5.0 
_reflns.pdbx_Rrim_I_all              0.099 
_reflns.pdbx_Rpim_I_all              0.042 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     83514 
_reflns.pdbx_chi_squared             0.90 
_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                  1.90 
_reflns_shell.d_res_low                   2.00 
_reflns_shell.number_measured_all         8827 
_reflns_shell.number_unique_obs           1919 
_reflns_shell.Rmerge_I_obs                1.039 
_reflns_shell.pdbx_chi_squared            0.68 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        61.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             1.164 
_reflns_shell.pdbx_Rpim_I_all             0.508 
_reflns_shell.pdbx_CC_half                0.508 
_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                                 7HGQ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     14894 
_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                             77.91 
_refine.ls_d_res_high                            1.76 
_refine.ls_percent_reflns_obs                    57.75 
_refine.ls_R_factor_obs                          0.19144 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18609 
_refine.ls_R_factor_R_free                       0.28852 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  815 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.913 
_refine.B_iso_mean                               39.058 
_refine.aniso_B[1][1]                            0.11 
_refine.aniso_B[2][2]                            -0.79 
_refine.aniso_B[3][3]                            0.68 
_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                       0.281 
_refine.pdbx_overall_ESU_R_Free                  0.252 
_refine.overall_SU_ML                            0.172 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.823 
_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        2145 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.number_atoms_solvent             261 
_refine_hist.number_atoms_total               2457 
_refine_hist.d_res_high                       1.76 
_refine_hist.d_res_low                        77.91 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.012  ? 2298 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.824  1.837  ? 3127 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.690  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.972  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.087 10.000 ? 312  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.130  0.200  ? 287  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1904 '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                  3.605  3.688  ? 1070 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.310  6.589  ? 1332 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.263  3.946  ? 1228 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       10.873 59.13  ? 3743 '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                       1.756 
_refine_ls_shell.d_res_low                        1.801 
_refine_ls_shell.number_reflns_R_work             62 
_refine_ls_shell.R_factor_R_work                  0.337 
_refine_ls_shell.percent_reflns_obs               3.29 
_refine_ls_shell.R_factor_R_free                  0.525 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             3 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HGQ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z94597856' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HGQ 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HGQ A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HGQ B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HGQ 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 7HGQ GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HGQ SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HGQ GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HGQ SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HGQ GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HGQ SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HGQ 
_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 207 ? ? O B HOH 274 ? ? 1.80 
2  1 O  B HOH 221 ? ? O B HOH 236 ? ? 1.87 
3  1 O  A HOH 218 ? ? O C HOH 244 ? ? 2.00 
4  1 O  A HOH 238 ? ? O A HOH 283 ? ? 2.00 
5  1 O  A HOH 273 ? ? O A HOH 301 ? ? 2.04 
6  1 OG A SER 64  ? ? O A HOH 201 ? ? 2.07 
7  1 O  A HOH 271 ? ? O B HOH 273 ? ? 2.08 
8  1 OH C TYR 40  ? ? O C HOH 201 ? ? 2.08 
9  1 O  B HOH 241 ? ? O B HOH 276 ? ? 2.11 
10 1 O  B HOH 234 ? ? O B HOH 272 ? ? 2.13 
11 1 O  A HOH 205 ? ? O A HOH 210 ? ? 2.13 
12 1 O  B HOH 228 ? ? O B HOH 229 ? ? 2.14 
13 1 O4 C SO4 102 ? ? O C HOH 202 ? ? 2.17 
14 1 O  A HOH 203 ? ? O A HOH 297 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 202 ? ? 1_555 O A HOH 259 ? ? 4_545 2.02 
2 1 O A HOH 268 ? ? 1_555 O C HOH 249 ? ? 4_445 2.07 
3 1 O A HOH 258 ? ? 1_555 O A HOH 281 ? ? 4_545 2.09 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_1              37 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_2              37 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             PRO 
_pdbx_validate_rmsd_angle.auth_seq_id_3              37 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                92.18 
_pdbx_validate_rmsd_angle.angle_target_value         103.30 
_pdbx_validate_rmsd_angle.angle_deviation            -11.12 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.20 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PRO A 37 ? ? -39.14  135.94 
2 1 ASN A 87 ? ? -161.77 62.19  
3 1 PRO B 7  ? ? -29.90  127.94 
4 1 PRO B 37 ? ? -2.14   -97.30 
5 1 PRO B 60 ? ? -34.82  124.31 
6 1 ASN B 87 ? ? -157.34 63.76  
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 VAL B 11 ? ? PHE B 12 ? ? 149.18 
2 1 VAL C 11 ? ? PHE C 12 ? ? 149.63 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       283 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   . 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          7.94 
# 
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 ASP 30 ? B ASP 31 
4  1 Y 1 B GLY 31 ? B GLY 32 
5  1 Y 1 B ALA 32 ? B ALA 33 
6  1 Y 1 C GLY 0  ? C GLY 1  
7  1 Y 1 C MET 1  ? C MET 2  
8  1 Y 1 C PRO 2  ? C PRO 3  
9  1 Y 1 C ASP 27 ? C ASP 28 
10 1 Y 1 C ILE 28 ? C ILE 29 
11 1 Y 1 C ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
K2S N1   N Y N 193 
K2S C4   C N N 194 
K2S C5   C Y N 195 
K2S C6   C N N 196 
K2S N    N N N 197 
K2S C    C N N 198 
K2S O    O N N 199 
K2S C1   C N N 200 
K2S C2   C Y N 201 
K2S C3   C Y N 202 
K2S N2   N Y N 203 
K2S O1   O N N 204 
K2S S    S N N 205 
K2S H1   H N N 206 
K2S H2   H N N 207 
K2S H3   H N N 208 
K2S H4   H N N 209 
K2S H5   H N N 210 
K2S H6   H N N 211 
K2S H7   H N N 212 
K2S H8   H N N 213 
K2S H9   H N N 214 
K2S H10  H N N 215 
K2S H11  H N N 216 
K2S H12  H N N 217 
K2S H13  H N N 218 
LEU N    N N N 219 
LEU CA   C N S 220 
LEU C    C N N 221 
LEU O    O N N 222 
LEU CB   C N N 223 
LEU CG   C N N 224 
LEU CD1  C N N 225 
LEU CD2  C N N 226 
LEU OXT  O N N 227 
LEU H    H N N 228 
LEU H2   H N N 229 
LEU HA   H N N 230 
LEU HB2  H N N 231 
LEU HB3  H N N 232 
LEU HG   H N N 233 
LEU HD11 H N N 234 
LEU HD12 H N N 235 
LEU HD13 H N N 236 
LEU HD21 H N N 237 
LEU HD22 H N N 238 
LEU HD23 H N N 239 
LEU HXT  H N N 240 
LYS N    N N N 241 
LYS CA   C N S 242 
LYS C    C N N 243 
LYS O    O N N 244 
LYS CB   C N N 245 
LYS CG   C N N 246 
LYS CD   C N N 247 
LYS CE   C N N 248 
LYS NZ   N N N 249 
LYS OXT  O N N 250 
LYS H    H N N 251 
LYS H2   H N N 252 
LYS HA   H N N 253 
LYS HB2  H N N 254 
LYS HB3  H N N 255 
LYS HG2  H N N 256 
LYS HG3  H N N 257 
LYS HD2  H N N 258 
LYS HD3  H N N 259 
LYS HE2  H N N 260 
LYS HE3  H N N 261 
LYS HZ1  H N N 262 
LYS HZ2  H N N 263 
LYS HZ3  H N N 264 
LYS HXT  H N N 265 
MET N    N N N 266 
MET CA   C N S 267 
MET C    C N N 268 
MET O    O N N 269 
MET CB   C N N 270 
MET CG   C N N 271 
MET SD   S N N 272 
MET CE   C N N 273 
MET OXT  O N N 274 
MET H    H N N 275 
MET H2   H N N 276 
MET HA   H N N 277 
MET HB2  H N N 278 
MET HB3  H N N 279 
MET HG2  H N N 280 
MET HG3  H N N 281 
MET HE1  H N N 282 
MET HE2  H N N 283 
MET HE3  H N N 284 
MET HXT  H N N 285 
PHE N    N N N 286 
PHE CA   C N S 287 
PHE C    C N N 288 
PHE O    O N N 289 
PHE CB   C N N 290 
PHE CG   C Y N 291 
PHE CD1  C Y N 292 
PHE CD2  C Y N 293 
PHE CE1  C Y N 294 
PHE CE2  C Y N 295 
PHE CZ   C Y N 296 
PHE OXT  O N N 297 
PHE H    H N N 298 
PHE H2   H N N 299 
PHE HA   H N N 300 
PHE HB2  H N N 301 
PHE HB3  H N N 302 
PHE HD1  H N N 303 
PHE HD2  H N N 304 
PHE HE1  H N N 305 
PHE HE2  H N N 306 
PHE HZ   H N N 307 
PHE HXT  H N N 308 
PRO N    N N N 309 
PRO CA   C N S 310 
PRO C    C N N 311 
PRO O    O N N 312 
PRO CB   C N N 313 
PRO CG   C N N 314 
PRO CD   C N N 315 
PRO OXT  O N N 316 
PRO H    H N N 317 
PRO HA   H N N 318 
PRO HB2  H N N 319 
PRO HB3  H N N 320 
PRO HG2  H N N 321 
PRO HG3  H N N 322 
PRO HD2  H N N 323 
PRO HD3  H N N 324 
PRO HXT  H N N 325 
SER N    N N N 326 
SER CA   C N S 327 
SER C    C N N 328 
SER O    O N N 329 
SER CB   C N N 330 
SER OG   O N N 331 
SER OXT  O N N 332 
SER H    H N N 333 
SER H2   H N N 334 
SER HA   H N N 335 
SER HB2  H N N 336 
SER HB3  H N N 337 
SER HG   H N N 338 
SER HXT  H N N 339 
SO4 S    S N N 340 
SO4 O1   O N N 341 
SO4 O2   O N N 342 
SO4 O3   O N N 343 
SO4 O4   O N N 344 
THR N    N N N 345 
THR CA   C N S 346 
THR C    C N N 347 
THR O    O N N 348 
THR CB   C N R 349 
THR OG1  O N N 350 
THR CG2  C N N 351 
THR OXT  O N N 352 
THR H    H N N 353 
THR H2   H N N 354 
THR HA   H N N 355 
THR HB   H N N 356 
THR HG1  H N N 357 
THR HG21 H N N 358 
THR HG22 H N N 359 
THR HG23 H N N 360 
THR HXT  H N N 361 
TRP N    N N N 362 
TRP CA   C N S 363 
TRP C    C N N 364 
TRP O    O N N 365 
TRP CB   C N N 366 
TRP CG   C Y N 367 
TRP CD1  C Y N 368 
TRP CD2  C Y N 369 
TRP NE1  N Y N 370 
TRP CE2  C Y N 371 
TRP CE3  C Y N 372 
TRP CZ2  C Y N 373 
TRP CZ3  C Y N 374 
TRP CH2  C Y N 375 
TRP OXT  O N N 376 
TRP H    H N N 377 
TRP H2   H N N 378 
TRP HA   H N N 379 
TRP HB2  H N N 380 
TRP HB3  H N N 381 
TRP HD1  H N N 382 
TRP HE1  H N N 383 
TRP HE3  H N N 384 
TRP HZ2  H N N 385 
TRP HZ3  H N N 386 
TRP HH2  H N N 387 
TRP HXT  H N N 388 
TYR N    N N N 389 
TYR CA   C N S 390 
TYR C    C N N 391 
TYR O    O N N 392 
TYR CB   C N N 393 
TYR CG   C Y N 394 
TYR CD1  C Y N 395 
TYR CD2  C Y N 396 
TYR CE1  C Y N 397 
TYR CE2  C Y N 398 
TYR CZ   C Y N 399 
TYR OH   O N N 400 
TYR OXT  O N N 401 
TYR H    H N N 402 
TYR H2   H N N 403 
TYR HA   H N N 404 
TYR HB2  H N N 405 
TYR HB3  H N N 406 
TYR HD1  H N N 407 
TYR HD2  H N N 408 
TYR HE1  H N N 409 
TYR HE2  H N N 410 
TYR HH   H N N 411 
TYR HXT  H N N 412 
VAL N    N N N 413 
VAL CA   C N S 414 
VAL C    C N N 415 
VAL O    O N N 416 
VAL CB   C N N 417 
VAL CG1  C N N 418 
VAL CG2  C N N 419 
VAL OXT  O N N 420 
VAL H    H N N 421 
VAL H2   H N N 422 
VAL HA   H N N 423 
VAL HB   H N N 424 
VAL HG11 H N N 425 
VAL HG12 H N N 426 
VAL HG13 H N N 427 
VAL HG21 H N N 428 
VAL HG22 H N N 429 
VAL HG23 H N N 430 
VAL HXT  H N N 431 
# 
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 
K2S C1  N    sing N N 182 
K2S C4  C3   sing N N 183 
K2S O   S    doub N N 184 
K2S N   C    sing N N 185 
K2S N   S    sing N N 186 
K2S C3  C2   doub Y N 187 
K2S C3  N1   sing Y N 188 
K2S S   C2   sing N N 189 
K2S S   O1   doub N N 190 
K2S C2  C5   sing Y N 191 
K2S N1  N2   sing Y N 192 
K2S C5  N2   doub Y N 193 
K2S C5  C6   sing N N 194 
K2S N1  H1   sing N N 195 
K2S C4  H2   sing N N 196 
K2S C4  H3   sing N N 197 
K2S C4  H4   sing N N 198 
K2S C6  H5   sing N N 199 
K2S C6  H6   sing N N 200 
K2S C6  H7   sing N N 201 
K2S C   H8   sing N N 202 
K2S C   H9   sing N N 203 
K2S C   H10  sing N N 204 
K2S C1  H11  sing N N 205 
K2S C1  H12  sing N N 206 
K2S C1  H13  sing N N 207 
LEU N   CA   sing N N 208 
LEU N   H    sing N N 209 
LEU N   H2   sing N N 210 
LEU CA  C    sing N N 211 
LEU CA  CB   sing N N 212 
LEU CA  HA   sing N N 213 
LEU C   O    doub N N 214 
LEU C   OXT  sing N N 215 
LEU CB  CG   sing N N 216 
LEU CB  HB2  sing N N 217 
LEU CB  HB3  sing N N 218 
LEU CG  CD1  sing N N 219 
LEU CG  CD2  sing N N 220 
LEU CG  HG   sing N N 221 
LEU CD1 HD11 sing N N 222 
LEU CD1 HD12 sing N N 223 
LEU CD1 HD13 sing N N 224 
LEU CD2 HD21 sing N N 225 
LEU CD2 HD22 sing N N 226 
LEU CD2 HD23 sing N N 227 
LEU OXT HXT  sing N N 228 
LYS N   CA   sing N N 229 
LYS N   H    sing N N 230 
LYS N   H2   sing N N 231 
LYS CA  C    sing N N 232 
LYS CA  CB   sing N N 233 
LYS CA  HA   sing N N 234 
LYS C   O    doub N N 235 
LYS C   OXT  sing N N 236 
LYS CB  CG   sing N N 237 
LYS CB  HB2  sing N N 238 
LYS CB  HB3  sing N N 239 
LYS CG  CD   sing N N 240 
LYS CG  HG2  sing N N 241 
LYS CG  HG3  sing N N 242 
LYS CD  CE   sing N N 243 
LYS CD  HD2  sing N N 244 
LYS CD  HD3  sing N N 245 
LYS CE  NZ   sing N N 246 
LYS CE  HE2  sing N N 247 
LYS CE  HE3  sing N N 248 
LYS NZ  HZ1  sing N N 249 
LYS NZ  HZ2  sing N N 250 
LYS NZ  HZ3  sing N N 251 
LYS OXT HXT  sing N N 252 
MET N   CA   sing N N 253 
MET N   H    sing N N 254 
MET N   H2   sing N N 255 
MET CA  C    sing N N 256 
MET CA  CB   sing N N 257 
MET CA  HA   sing N N 258 
MET C   O    doub N N 259 
MET C   OXT  sing N N 260 
MET CB  CG   sing N N 261 
MET CB  HB2  sing N N 262 
MET CB  HB3  sing N N 263 
MET CG  SD   sing N N 264 
MET CG  HG2  sing N N 265 
MET CG  HG3  sing N N 266 
MET SD  CE   sing N N 267 
MET CE  HE1  sing N N 268 
MET CE  HE2  sing N N 269 
MET CE  HE3  sing N N 270 
MET OXT HXT  sing N N 271 
PHE N   CA   sing N N 272 
PHE N   H    sing N N 273 
PHE N   H2   sing N N 274 
PHE CA  C    sing N N 275 
PHE CA  CB   sing N N 276 
PHE CA  HA   sing N N 277 
PHE C   O    doub N N 278 
PHE C   OXT  sing N N 279 
PHE CB  CG   sing N N 280 
PHE CB  HB2  sing N N 281 
PHE CB  HB3  sing N N 282 
PHE CG  CD1  doub Y N 283 
PHE CG  CD2  sing Y N 284 
PHE CD1 CE1  sing Y N 285 
PHE CD1 HD1  sing N N 286 
PHE CD2 CE2  doub Y N 287 
PHE CD2 HD2  sing N N 288 
PHE CE1 CZ   doub Y N 289 
PHE CE1 HE1  sing N N 290 
PHE CE2 CZ   sing Y N 291 
PHE CE2 HE2  sing N N 292 
PHE CZ  HZ   sing N N 293 
PHE OXT HXT  sing N N 294 
PRO N   CA   sing N N 295 
PRO N   CD   sing N N 296 
PRO N   H    sing N N 297 
PRO CA  C    sing N N 298 
PRO CA  CB   sing N N 299 
PRO CA  HA   sing N N 300 
PRO C   O    doub N N 301 
PRO C   OXT  sing N N 302 
PRO CB  CG   sing N N 303 
PRO CB  HB2  sing N N 304 
PRO CB  HB3  sing N N 305 
PRO CG  CD   sing N N 306 
PRO CG  HG2  sing N N 307 
PRO CG  HG3  sing N N 308 
PRO CD  HD2  sing N N 309 
PRO CD  HD3  sing N N 310 
PRO OXT HXT  sing N N 311 
SER N   CA   sing N N 312 
SER N   H    sing N N 313 
SER N   H2   sing N N 314 
SER CA  C    sing N N 315 
SER CA  CB   sing N N 316 
SER CA  HA   sing N N 317 
SER C   O    doub N N 318 
SER C   OXT  sing N N 319 
SER CB  OG   sing N N 320 
SER CB  HB2  sing N N 321 
SER CB  HB3  sing N N 322 
SER OG  HG   sing N N 323 
SER OXT HXT  sing N N 324 
SO4 S   O1   doub N N 325 
SO4 S   O2   doub N N 326 
SO4 S   O3   sing N N 327 
SO4 S   O4   sing N N 328 
THR N   CA   sing N N 329 
THR N   H    sing N N 330 
THR N   H2   sing N N 331 
THR CA  C    sing N N 332 
THR CA  CB   sing N N 333 
THR CA  HA   sing N N 334 
THR C   O    doub N N 335 
THR C   OXT  sing N N 336 
THR CB  OG1  sing N N 337 
THR CB  CG2  sing N N 338 
THR CB  HB   sing N N 339 
THR OG1 HG1  sing N N 340 
THR CG2 HG21 sing N N 341 
THR CG2 HG22 sing N N 342 
THR CG2 HG23 sing N N 343 
THR OXT HXT  sing N N 344 
TRP N   CA   sing N N 345 
TRP N   H    sing N N 346 
TRP N   H2   sing N N 347 
TRP CA  C    sing N N 348 
TRP CA  CB   sing N N 349 
TRP CA  HA   sing N N 350 
TRP C   O    doub N N 351 
TRP C   OXT  sing N N 352 
TRP CB  CG   sing N N 353 
TRP CB  HB2  sing N N 354 
TRP CB  HB3  sing N N 355 
TRP CG  CD1  doub Y N 356 
TRP CG  CD2  sing Y N 357 
TRP CD1 NE1  sing Y N 358 
TRP CD1 HD1  sing N N 359 
TRP CD2 CE2  doub Y N 360 
TRP CD2 CE3  sing Y N 361 
TRP NE1 CE2  sing Y N 362 
TRP NE1 HE1  sing N N 363 
TRP CE2 CZ2  sing Y N 364 
TRP CE3 CZ3  doub Y N 365 
TRP CE3 HE3  sing N N 366 
TRP CZ2 CH2  doub Y N 367 
TRP CZ2 HZ2  sing N N 368 
TRP CZ3 CH2  sing Y N 369 
TRP CZ3 HZ3  sing N N 370 
TRP CH2 HH2  sing N N 371 
TRP OXT HXT  sing N N 372 
TYR N   CA   sing N N 373 
TYR N   H    sing N N 374 
TYR N   H2   sing N N 375 
TYR CA  C    sing N N 376 
TYR CA  CB   sing N N 377 
TYR CA  HA   sing N N 378 
TYR C   O    doub N N 379 
TYR C   OXT  sing N N 380 
TYR CB  CG   sing N N 381 
TYR CB  HB2  sing N N 382 
TYR CB  HB3  sing N N 383 
TYR CG  CD1  doub Y N 384 
TYR CG  CD2  sing Y N 385 
TYR CD1 CE1  sing Y N 386 
TYR CD1 HD1  sing N N 387 
TYR CD2 CE2  doub Y N 388 
TYR CD2 HD2  sing N N 389 
TYR CE1 CZ   doub Y N 390 
TYR CE1 HE1  sing N N 391 
TYR CE2 CZ   sing Y N 392 
TYR CE2 HE2  sing N N 393 
TYR CZ  OH   sing N N 394 
TYR OH  HH   sing N N 395 
TYR OXT HXT  sing N N 396 
VAL N   CA   sing N N 397 
VAL N   H    sing N N 398 
VAL N   H2   sing N N 399 
VAL CA  C    sing N N 400 
VAL CA  CB   sing N N 401 
VAL CA  HA   sing N N 402 
VAL C   O    doub N N 403 
VAL C   OXT  sing N N 404 
VAL CB  CG1  sing N N 405 
VAL CB  CG2  sing N N 406 
VAL CB  HB   sing N N 407 
VAL CG1 HG11 sing N N 408 
VAL CG1 HG12 sing N N 409 
VAL CG1 HG13 sing N N 410 
VAL CG2 HG21 sing N N 411 
VAL CG2 HG22 sing N N 412 
VAL CG2 HG23 sing N N 413 
VAL OXT HXT  sing N N 414 
# 
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                    7HGQ 
_atom_sites.fract_transf_matrix[1][1]   0.024447 
_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]   0.024288 
_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]   0.006418 
_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  ? -0.538  4.116   2.873   1.00 52.97  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -1.514  3.603   1.870   1.00 53.47  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? -0.837  2.652   0.880   1.00 50.94  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 0.209   2.956   0.311   1.00 54.59  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -2.296  4.715   1.158   1.00 48.72  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -3.233  5.455   2.084   1.00 56.61  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -4.477  4.417   2.886   1.00 60.48  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.467  5.108   4.547   1.00 51.81  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -1.408  1.439   0.712   1.00 51.94  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.945  0.459   -0.269  1.00 46.99  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? -0.702  0.948   -1.700  1.00 48.16  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -1.377  1.846   -2.223  1.00 41.48  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -2.110  -0.576  -0.232  1.00 49.54  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -2.605  -0.541  1.182   1.00 54.20  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -2.531  0.935   1.527   1.00 57.74  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 0.285   0.312   -2.321  1.00 41.38  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 0.494   0.399   -3.747  1.00 41.59  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? -0.080  -0.896  -4.317  1.00 40.43  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? -0.540  -1.744  -3.549  1.00 35.83  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 1.996   0.518   -4.018  1.00 47.85  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 2.667   1.756   -3.522  1.00 63.85  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 2.858   2.046   -2.185  1.00 66.38  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 3.220   2.776   -4.210  1.00 68.23  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.488   3.209   -2.074  1.00 69.63  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 3.722   3.665   -3.293  1.00 74.92  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? -0.036  -1.049  -5.651  1.00 31.05  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? -0.243  -2.326  -6.306  1.00 27.80  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 0.891   -3.262  -5.895  1.00 27.28  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 1.939   -2.823  -5.420  1.00 28.90  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? -0.241  -2.125  -7.824  1.00 23.60  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 0.681   -4.565  -6.064  1.00 25.48  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 1.723   -5.532  -5.782  1.00 23.26  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 2.887   -5.354  -6.747  1.00 27.88  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 2.687   -4.986  -7.910  1.00 27.03  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.095   -6.929  -5.895  1.00 24.65  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 0.312   -7.312  -4.648  1.00 26.60  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 0.957   -7.396  -3.403  1.00 28.14  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -1.067  -7.584  -4.725  1.00 23.68  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 0.241   -7.751  -2.258  1.00 28.73  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -1.759  -7.962  -3.589  1.00 21.27  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -1.124  -8.033  -2.358  1.00 25.22  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.116   -5.625  -6.275  1.00 25.51  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.268   -5.539  -7.162  1.00 26.50  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.150   -6.771  -6.932  1.00 25.24  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.051   -7.381  -5.859  1.00 28.68  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 5.920   -4.181  -6.883  1.00 27.04  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 6.453   -4.111  -5.479  1.00 31.47  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.162   -2.792  -5.184  1.00 41.08  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 7.797   -2.739  -3.816  1.00 38.89  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 6.822   -2.973  -2.739  1.00 42.72  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.022   -7.186  -7.886  1.00 23.50  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 7.960   -8.293  -7.657  1.00 23.55  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 8.721   -8.140  -6.339  1.00 21.30  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.173   -7.033  -6.023  1.00 24.63  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 8.900   -8.149  -8.883  1.00 22.77  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 7.984   -7.677  -9.971  1.00 27.28  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.164   -6.626  -9.241  1.00 23.77  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 8.826   -9.229  -5.566  1.00 19.90  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 9.475   -9.206  -4.254  1.00 18.56  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 8.522   -9.026  -3.057  1.00 20.99  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 8.940   -9.193  -1.921  1.00 24.38  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 7.261   -8.591  -3.272  1.00 21.22  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 6.307   -8.453  -2.191  1.00 21.00  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.049   -9.812  -1.579  1.00 20.25  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 5.841   -10.764 -2.300  1.00 21.10  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.002   -7.772  -2.587  1.00 23.12  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.060   -6.257  -2.762  1.00 25.81  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.064   -5.639  -2.340  1.00 24.06  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.132   -5.705  -3.400  1.00 28.06  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.066   -9.894  -0.243  1.00 20.12  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 5.826   -11.173 0.419   1.00 19.96  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 4.359   -11.213 0.805   1.00 20.08  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 3.803   -10.192 1.189   1.00 21.76  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 6.735   -11.366 1.645   1.00 18.70  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 8.236   -11.256 1.353   1.00 18.65  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.113   -11.422 2.561   1.00 17.87  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 8.650   -12.233 0.277   1.00 19.09  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 3.748   -12.398 0.753   1.00 20.44  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 2.309   -12.524 0.979   1.00 21.85  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.061   -13.910 1.540   1.00 20.74  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 2.951   -14.771 1.463   1.00 24.65  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 1.566   -12.441 -0.375  1.00 22.68  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 1.729   -11.069 -1.032  1.00 22.97  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.060   -13.540 -1.326  1.00 20.97  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 0.847   -14.117 2.044   1.00 20.11  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 0.269   -15.451 2.072   1.00 21.69  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? -0.696  -15.539 0.897   1.00 21.08  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -1.484  -14.624 0.648   1.00 24.69  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? -0.486  -15.778 3.352   1.00 20.42  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 0.481   -15.902 4.517   1.00 20.55  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 0.947   -14.782 5.191   1.00 21.37  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.003   -17.138 4.871   1.00 20.48  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 1.883   -14.892 6.217   1.00 23.65  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 1.896   -17.248 5.941   1.00 23.50  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 2.364   -16.126 6.586   1.00 23.47  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? -0.642  -16.644 0.170   1.00 20.39  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -1.359  -16.666 -1.087  1.00 21.21  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -2.393  -17.764 -0.909  1.00 27.03  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -2.078  -18.797 -0.316  1.00 30.91  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? -0.380  -16.883 -2.235  1.00 20.67  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -3.653  -17.494 -1.271  1.00 27.60  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -4.686  -18.494 -1.033  1.00 29.40  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -5.039  -19.224 -2.331  1.00 34.16  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -5.506  -18.623 -3.303  1.00 29.82  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -5.947  -17.884 -0.413  1.00 32.43  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -7.021  -18.875 0.009   1.00 33.01  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -6.507  -19.840 1.073   1.00 39.98  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -7.594  -20.692 1.661   1.00 35.09  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -8.178  -21.525 0.618   1.00 32.26  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.839  -20.543 -2.311  1.00 34.31  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -5.440  -21.391 -3.322  1.00 38.07  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -6.505  -22.320 -2.733  1.00 38.12  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -6.363  -22.787 -1.606  1.00 37.17  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -4.329  -22.170 -4.006  1.00 40.62  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.398  -21.196 -4.645  1.00 48.28  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -2.620  -22.001 -6.038  1.00 48.66  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -3.796  -22.051 -7.395  1.00 57.37  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -7.545  -22.608 -3.536  1.00 39.48  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -8.619  -23.526 -3.179  1.00 46.51  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -8.008  -24.843 -2.724  1.00 47.29  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -7.125  -25.374 -3.396  1.00 45.88  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -9.626  -23.774 -4.313  1.00 50.90  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -11.065 -24.078 -3.864  1.00 52.77  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -12.148 -24.068 -4.941  1.00 44.90  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -8.440  -25.284 -1.532  1.00 43.10  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -8.050  -26.554 -0.946  1.00 41.05  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -6.688  -26.518 -0.264  1.00 42.59  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -6.206  -27.557 0.163   1.00 41.32  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -6.041  -25.342 -0.224  1.00 42.20  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -4.794  -25.171 0.505   1.00 37.24  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -4.999  -24.082 1.545   1.00 32.37  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -5.807  -23.189 1.327   1.00 35.20  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -3.601  -24.810 -0.385  1.00 46.47  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -3.271  -25.921 -1.365  1.00 54.53  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -2.386  -26.941 -1.027  1.00 56.99  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.896  -25.964 -2.607  1.00 57.81  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -2.118  -27.965 -1.920  1.00 67.35  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -3.644  -26.984 -3.505  1.00 61.50  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -2.752  -27.983 -3.156  1.00 68.75  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -2.514  -28.969 -4.069  1.00 81.82  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -4.300  -24.112 2.705   1.00 34.02  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -4.323  -22.974 3.632   1.00 33.30  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -3.557  -21.784 3.023   1.00 32.72  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -2.785  -21.952 2.072   1.00 32.06  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -3.643  -23.568 4.869   1.00 33.19  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -2.626  -24.518 4.278   1.00 34.30  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -3.434  -25.201 3.178   1.00 33.69  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -3.797  -20.578 3.553   1.00 29.47  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -3.019  -19.430 3.148   1.00 30.22  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -1.555  -19.819 3.299   1.00 28.57  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -1.166  -20.266 4.371   1.00 24.58  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -3.424  -18.199 3.962   1.00 30.77  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -4.864  -17.843 3.803   1.00 30.61  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -5.878  -18.601 4.361   1.00 34.30  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -5.464  -16.826 3.184   1.00 32.11  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -7.058  -18.052 4.075   1.00 30.07  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -6.832  -16.967 3.355   1.00 31.90  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? -0.776  -19.649 2.211   1.00 26.55  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 0.539   -20.245 2.055   1.00 27.51  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 1.601   -19.168 1.885   1.00 27.40  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 1.460   -18.327 1.007   1.00 27.14  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 0.589   -21.084 0.771   1.00 30.28  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 1.651   -22.149 0.857   1.00 30.15  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 2.995   -22.012 0.684   1.00 29.04  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 1.426   -23.533 1.184   1.00 30.51  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 3.628   -23.216 0.844   1.00 32.54  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 2.691   -24.170 1.150   1.00 34.79  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 0.280   -24.292 1.460   1.00 31.12  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 2.840   -25.537 1.402   1.00 35.55  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 0.427   -25.645 1.689   1.00 35.24  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 1.688   -26.256 1.660   1.00 37.58  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 2.732   -19.221 2.634   1.00 25.78  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 3.836   -18.275 2.424   1.00 24.21  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 4.371   -18.272 0.981   1.00 21.88  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 4.746   -19.303 0.430   1.00 21.17  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 4.901   -18.781 3.399   1.00 23.11  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 4.565   -20.242 3.614   1.00 23.74  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 3.042   -20.250 3.639   1.00 24.29  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 4.433   -17.080 0.392   1.00 19.10  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 4.589   -16.892 -1.038  1.00 18.69  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 5.165   -15.491 -1.290  1.00 17.96  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 5.212   -14.674 -0.391  1.00 16.72  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 3.242   -17.154 -1.737  1.00 17.26  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 5.679   -15.228 -2.510  1.00 20.07  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 6.183   -13.903 -2.862  1.00 19.49  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 5.729   -13.643 -4.307  1.00 19.04  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 5.426   -14.596 -5.007  1.00 17.25  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 7.719   -13.890 -2.796  1.00 19.15  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 8.381   -14.843 -3.789  1.00 20.41  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 9.913   -14.718 -3.754  1.00 20.00  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 10.591  -15.588 -4.730  1.00 19.32  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 11.888  -15.899 -4.690  1.00 21.01  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 12.644  -15.560 -3.648  1.00 21.47  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 12.426  -16.598 -5.660  1.00 19.80  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 5.604   -12.373 -4.716  1.00 19.33  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 5.405   -12.056 -6.128  1.00 21.15  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 6.783   -12.234 -6.777  1.00 24.56  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 7.720   -11.502 -6.460  1.00 27.74  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 4.849   -10.626 -6.350  1.00 18.99  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 3.628   -10.301 -5.448  1.00 22.12  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 4.548   -10.357 -7.845  1.00 17.43  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 2.468   -11.288 -5.502  1.00 25.36  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 6.911   -13.229 -7.653  1.00 24.06  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.124   -13.390 -8.430  1.00 29.28  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 8.225   -12.361 -9.539  1.00 28.21  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 7.218   -11.936 -10.090 1.00 30.45  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 8.180   -14.743 -9.111  1.00 25.59  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.100   -15.768 -8.482  1.00 25.29  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 9.766   -15.468 -7.469  1.00 30.67  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 9.155   -16.856 -9.018  1.00 29.56  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 9.469   -11.995 -9.868  1.00 31.00  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 9.780   -11.363 -11.147 1.00 35.40  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 9.529   -12.327 -12.298 1.00 33.68  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 9.697   -13.533 -12.152 1.00 40.59  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 11.252  -11.002 -11.207 1.00 40.90  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 11.666  -9.876  -10.280 1.00 44.89  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 11.506  -8.700  -10.708 1.00 48.59  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 12.076  -10.187 -9.129  1.00 45.57  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 9.195   -11.796 -13.474 1.00 34.40  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 9.204   -12.644 -14.664 1.00 33.67  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 10.580  -12.502 -15.335 1.00 35.83  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 10.990  -11.391 -15.675 1.00 36.17  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.030   -12.283 -15.590 1.00 30.50  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 6.678   -12.406 -14.850 1.00 33.71  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.072   -13.101 -16.881 1.00 28.01  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 5.702   -11.287 -15.160 1.00 36.80  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 11.322  -13.615 -15.426 1.00 29.10  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 12.683  -13.633 -15.921 1.00 31.55  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 12.630  -13.472 -17.434 1.00 31.08  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 11.646  -13.848 -18.058 1.00 26.98  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 13.336  -14.953 -15.585 1.00 39.89  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 13.708  -12.940 -18.008 1.00 32.99  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 13.766  -12.803 -19.460 1.00 26.65  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 13.421  -14.158 -20.042 1.00 29.02  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 13.978  -15.159 -19.585 1.00 26.97  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.149  -12.330 -19.849 1.00 24.02  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.381  -10.822 -19.774 1.00 29.73  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.392  -10.042 -19.733 1.00 34.69  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.554  -10.409 -19.730 1.00 32.30  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 12.467  -14.188 -20.991 1.00 30.28  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.147  -15.422 -21.693 1.00 33.88  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 11.151  -16.366 -21.003 1.00 33.23  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 10.862  -17.418 -21.544 1.00 33.02  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 10.680  -16.038 -19.793 1.00 34.46  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 9.787   -16.889 -19.019 1.00 30.83  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 8.363   -16.581 -19.418 1.00 31.16  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.048   -15.442 -19.749 1.00 32.62  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 9.939   -16.619 -17.514 1.00 28.84  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 7.501   -17.596 -19.290 1.00 32.97  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.085   -17.450 -19.551 1.00 32.15  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 5.503   -16.342 -18.672 1.00 31.12  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 5.740   -16.300 -17.461 1.00 32.40  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 5.347   -18.806 -19.466 1.00 35.74  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 3.844   -18.658 -19.695 1.00 37.14  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 5.898   -19.755 -20.536 1.00 34.41  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 4.808   -15.398 -19.317 1.00 27.66  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.172   -14.273 -18.635 1.00 30.66  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 2.839   -14.717 -18.034 1.00 33.80  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 2.176   -15.609 -18.566 1.00 32.87  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 3.869   -13.061 -19.525 1.00 30.10  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.157   -12.420 -20.025 1.00 36.05  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.064   -11.266 -21.002 1.00 38.23  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 4.731   -11.668 -22.399 1.00 37.37  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.081   -10.498 -23.209 1.00 39.43  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 2.407   -14.095 -16.920 1.00 31.62  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.059   -14.311 -16.396 1.00 33.40  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? -0.064  -13.783 -17.283 1.00 39.16  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.147   -12.888 -18.107 1.00 40.46  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.041   -13.646 -15.009 1.00 34.52  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.277   -12.758 -14.955 1.00 36.40  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.205   -13.170 -16.108 1.00 33.38  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -1.309  -14.293 -17.130 1.00 36.02  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -2.449  -13.689 -17.803 1.00 40.74  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -2.600  -12.280 -17.236 1.00 39.98  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -2.079  -11.984 -16.160 1.00 36.55  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -3.654  -14.623 -17.454 1.00 37.50  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.997  -15.910 -17.018 1.00 38.04  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -1.687  -15.491 -16.370 1.00 36.22  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -3.305  -11.391 -17.971 1.00 38.62  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -3.766  -10.107 -17.439 1.00 37.39  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -4.269  -10.137 -15.994 1.00 39.63  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -5.021  -11.024 -15.594 1.00 38.53  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -4.891  -9.715  -18.432 1.00 44.55  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -5.039  -10.920 -19.383 1.00 42.30  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.689  -11.603 -19.380 1.00 42.26  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.851  -9.138  -15.222 1.00 39.63  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -4.278  -8.949  -13.836 1.00 44.69  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.905  -10.130 -12.936 1.00 34.21  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -4.471  -10.237 -11.848 1.00 35.74  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.761  -8.579  -13.708 1.00 49.32  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -6.206  -7.484  -14.658 1.00 51.90  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.766  -6.331  -14.561 1.00 52.91  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -7.075  -7.822  -15.598 1.00 51.41  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.984  -11.003 -13.390 1.00 28.06  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -2.406  -12.075 -12.577 1.00 28.80  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.895  -11.832 -12.373 1.00 25.49  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? -0.222  -11.279 -13.235 1.00 25.68  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -2.648  -13.480 -13.137 1.00 28.86  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -4.067  -13.905 -13.512 1.00 26.59  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.951  -13.838 -12.296 1.00 30.69  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -6.413  -13.986 -12.607 1.00 37.22  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.791  -15.398 -12.612 1.00 34.92  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? -0.392  -12.228 -11.190 1.00 20.80  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 0.985   -12.188 -10.761 1.00 19.44  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 1.527   -13.600 -10.761 1.00 19.97  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 0.778   -14.540 -10.522 1.00 22.56  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.028   -11.618 -9.341  1.00 18.54  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 0.563   -10.165 -9.373  1.00 21.68  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.790  -9.841  -9.271  1.00 23.75  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 1.476   -9.114  -9.558  1.00 24.36  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -1.235  -8.529  -9.361  1.00 23.84  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.035   -7.797  -9.675  1.00 25.72  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? -0.320  -7.511  -9.567  1.00 27.29  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.783  -6.226  -9.646  1.00 32.91  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 2.835   -13.795 -11.041 1.00 19.39  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 3.465   -15.094 -10.837 1.00 20.47  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 3.751   -15.157 -9.327  1.00 19.54  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 4.470   -14.308 -8.804  1.00 21.50  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 4.753   -14.989 -11.656 1.00 22.18  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.098   -13.500 -11.607 1.00 24.13  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 3.752   -12.788 -11.585 1.00 22.40  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 3.208   -16.176 -8.676  1.00 17.54  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 3.369   -16.374 -7.244  1.00 19.26  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 4.284   -17.576 -7.050  1.00 23.04  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.037   -18.658 -7.580  1.00 24.95  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.020   -16.583 -6.531  1.00 20.17  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.027   -15.458 -6.851  1.00 19.64  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 2.255   -16.748 -5.015  1.00 18.78  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 1.550   -14.064 -6.528  1.00 19.42  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 5.391   -17.349 -6.348  1.00 21.65  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 6.249   -18.432 -5.966  1.00 22.35  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 5.931   -18.730 -4.510  1.00 23.50  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.062   -17.850 -3.663  1.00 21.91  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 7.709   -17.980 -6.123  1.00 21.38  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 8.714   -19.023 -5.654  1.00 24.26  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 9.168   -20.012 -6.522  1.00 27.43  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 9.238   -18.982 -4.354  1.00 29.93  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.123  -20.923 -6.099  1.00 32.76  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 10.175  -19.917 -3.931  1.00 34.31  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 10.616  -20.881 -4.819  1.00 30.35  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 5.526   -19.985 -4.270  1.00 26.01  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 5.111   -20.509 -2.988  1.00 25.22  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 6.359   -21.089 -2.337  1.00 23.68  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 7.051   -21.916 -2.933  1.00 23.85  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 4.117   -21.659 -3.215  1.00 25.12  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 2.748   -21.192 -3.658  1.00 26.43  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 2.487   -20.969 -5.008  1.00 26.07  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 1.738   -20.974 -2.727  1.00 26.38  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 1.243   -20.525 -5.403  1.00 24.91  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 0.490   -20.524 -3.135  1.00 27.41  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 0.259   -20.301 -4.485  1.00 25.48  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 6.639   -20.642 -1.112  1.00 26.67  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 7.820   -21.086 -0.382  1.00 26.49  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 7.583   -22.524 0.059   1.00 28.89  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 6.421   -22.913 0.258   1.00 28.80  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 8.098   -20.130 0.778   1.00 22.92  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 8.538   -18.735 0.370   1.00 20.17  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 9.797   -18.522 -0.204  1.00 19.72  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 7.718   -17.638 0.613   1.00 17.78  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 10.221  -17.250 -0.567  1.00 17.31  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 8.155   -16.351 0.284   1.00 19.56  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 9.398   -16.160 -0.324  1.00 18.22  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 8.680   -23.289 0.209   1.00 27.68  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 8.585   -24.672 0.667   1.00 32.41  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 8.372   -25.660 -0.488  1.00 36.27  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 9.192   -26.559 -0.696  1.00 35.81  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 7.268   -25.483 -1.230  1.00 36.04  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 6.950   -26.277 -2.413  1.00 33.93  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 7.680   -25.702 -3.623  1.00 35.05  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 7.897   -26.374 -4.641  1.00 41.01  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 5.432   -26.311 -2.637  1.00 33.12  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 5.073   -24.967 -2.947  1.00 36.46  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 4.632   -26.730 -1.417  1.00 36.35  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 8.017   -24.420 -3.544  1.00 29.27  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 8.703   -23.786 -4.646  1.00 29.91  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 7.908   -23.960 -5.941  1.00 27.38  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 8.502   -23.899 -7.003  1.00 29.92  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 10.138  -24.306 -4.804  1.00 28.53  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 10.868  -24.391 -3.500  1.00 32.20  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 11.551  -25.519 -3.112  1.00 32.06  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 10.976  -23.528 -2.499  1.00 33.20  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 12.065  -25.322 -1.899  1.00 35.83  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 11.744  -24.112 -1.516  1.00 34.10  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 6.577   -24.114 -5.857  1.00 32.81  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 5.719   -24.117 -7.042  1.00 32.21  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 5.375   -22.682 -7.393  1.00 29.77  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 5.463   -21.833 -6.519  1.00 29.45  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 4.406   -24.830 -6.734  1.00 37.36  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 4.560   -26.345 -6.637  1.00 41.90  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 3.421   -26.933 -5.829  1.00 55.39  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 2.525   -26.169 -5.366  1.00 54.21  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 3.471   -28.167 -5.620  1.00 62.03  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.014   -22.426 -8.668  1.00 31.11  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 4.472   -21.143 -9.121  1.00 27.51  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.006   -21.357 -9.493  1.00 31.96  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 2.638   -22.440 -9.960  1.00 37.14  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 5.271   -20.517 -10.275 1.00 28.15  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 6.543   -20.138 -9.752  1.00 28.33  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 4.639   -19.271 -10.876 1.00 23.42  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 2.165   -20.350 -9.215  1.00 23.74  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 0.860   -20.278 -9.851  1.00 23.71  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 0.607   -18.806 -10.118 1.00 25.76  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 1.281   -17.959 -9.526  1.00 24.82  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? -0.250  -20.891 -9.010  1.00 23.55  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? -0.330  -18.540 -11.026 1.00 20.66  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? -0.724  -17.187 -11.370 1.00 25.48  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.974  -16.829 -10.574 1.00 28.45  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -3.006  -17.463 -10.756 1.00 33.52  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -1.007  -17.239 -12.880 1.00 26.31  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.238   -17.440 -13.736 1.00 30.61  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 1.449   -16.817 -13.409 1.00 30.41  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.188   -18.206 -14.901 1.00 34.36  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 2.576   -16.981 -14.203 1.00 36.65  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 1.335   -18.370 -15.679 1.00 34.24  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 2.525   -17.760 -15.330 1.00 30.00  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.871  -15.827 -9.678  1.00 26.60  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.996  -15.425 -8.842  1.00 23.52  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -3.298  -13.953 -9.062  1.00 22.20  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -2.382  -13.181 -9.360  1.00 23.25  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -2.699  -15.688 -7.367  1.00 22.56  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -2.419  -17.156 -7.030  1.00 25.63  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -2.227  -17.280 -5.521  1.00 24.59  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.564  -18.042 -7.528  1.00 25.58  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -4.579  -13.590 -8.890  1.00 24.41  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -5.004  -12.199 -8.777  1.00 22.07  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.892  -11.727 -7.325  1.00 25.79  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.805  -12.570 -6.424  1.00 21.12  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.891  -10.386 -7.074  1.00 23.50  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.810  -9.827  -5.726  1.00 23.44  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.851  -10.260 -4.700  1.00 28.38  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -5.626  -10.083 -3.503  1.00 26.38  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.861  -8.300  -5.969  1.00 23.47  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -4.357  -8.126  -7.388  1.00 24.04  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.902  -9.337  -8.109  1.00 23.19  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.986  -10.819 -5.163  1.00 26.80  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.984  -11.288 -4.209  1.00 28.53  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -7.429  -12.461 -3.411  1.00 28.01  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.937  -12.776 -2.333  1.00 25.80  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -9.329  -11.685 -4.840  1.00 30.12  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -9.395  -12.994 -5.604  1.00 38.18  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -10.727 -13.207 -6.356  1.00 41.50  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -10.708 -14.330 -7.346  1.00 40.71  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -10.345 -15.607 -6.718  1.00 40.92  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -6.405  -13.128 -3.954  1.00 22.82  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.913  -14.301 -3.258  1.00 23.79  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -4.585  -14.012 -2.556  1.00 22.51  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.908  -14.945 -2.088  1.00 24.29  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.830  -15.449 -4.228  1.00 26.39  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -7.219  -15.879 -4.623  1.00 29.28  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.987  -16.133 -3.678  1.00 28.54  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -7.523  -15.843 -5.842  1.00 27.12  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -4.225  -12.718 -2.496  1.00 20.55  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.891  -12.305 -2.056  1.00 20.40  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -3.040  -11.454 -0.796  1.00 20.14  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -3.593  -10.361 -0.865  1.00 19.52  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -2.199  -11.538 -3.181  1.00 21.17  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -2.024  -12.298 -4.498  1.00 21.42  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -1.197  -11.495 -5.499  1.00 19.46  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -1.378  -13.688 -4.291  1.00 22.11  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -2.490  -11.955 0.310   1.00 20.15  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -2.573  -11.316 1.623   1.00 21.06  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -1.184  -10.844 2.057   1.00 20.95  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? -0.295  -11.653 2.317   1.00 19.56  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -3.089  -12.377 2.589   1.00 23.52  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -4.522  -12.793 2.341   1.00 24.94  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -4.819  -13.759 1.387   1.00 26.14  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -5.553  -12.291 3.140   1.00 28.54  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -6.134  -14.156 1.189   1.00 27.64  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -6.864  -12.687 2.922   1.00 26.79  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -7.147  -13.620 1.949   1.00 26.17  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.913  -9.523  2.067   1.00 22.61  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 0.409   -9.009  2.432   1.00 22.58  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 0.985   -9.575  3.731   1.00 26.29  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 0.317   -9.556  4.767   1.00 25.19  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 0.116   -7.486  2.513   1.00 23.60  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? -0.884  -7.257  1.403   1.00 26.65  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -1.815  -8.468  1.569   1.00 26.98  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 2.252   -10.028 3.671   1.00 24.01  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 2.862   -10.885 4.686   1.00 27.04  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 2.771   -10.287 6.094   1.00 26.50  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 2.267   -10.932 7.040   1.00 25.69  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 4.316   -11.205 4.294   1.00 25.50  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.052   -11.985 5.382   1.00 26.28  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 4.777   -13.335 5.620   1.00 24.08  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.058   -11.392 6.135   1.00 23.95  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 5.479   -14.055 6.576   1.00 23.47  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 6.723   -12.087 7.135   1.00 25.32  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 6.436   -13.421 7.342   1.00 25.80  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.089   -14.135 8.294   1.00 28.10  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 3.262   -9.054  6.240   1.00 26.69  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 3.421   -8.474  7.571   1.00 28.76  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.079   -8.318  8.289   1.00 28.18  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 1.998   -8.614  9.480   1.00 27.80  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.206   -7.177  7.507   1.00 35.06  ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 5.719   -7.363  7.514   1.00 46.58  ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 6.274   -7.859  8.542   1.00 49.31  ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 6.331   -7.010  6.492   1.00 54.72  ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 1.030   -7.871  7.557   1.00 31.07  ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? -0.327  -7.760  8.097   1.00 31.85  ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? -0.887  -9.122  8.525   1.00 32.49  ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -1.574  -9.203  9.537   1.00 35.76  ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -1.299  -7.081  7.120   1.00 35.77  ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -2.796  -7.147  7.494   1.00 37.32  ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -3.679  -6.226  6.677   1.00 37.21  ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -4.883  -5.799  7.480   1.00 39.96  ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -5.823  -6.894  7.700   1.00 34.22  ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? -0.592  -10.191 7.768   1.00 31.90  ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -1.307  -11.454 7.908   1.00 32.47  ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? -0.508  -12.490 8.678   1.00 28.58  ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? -1.061  -13.549 8.968   1.00 28.58  ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -1.676  -12.028 6.570   1.00 36.20  ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -2.585  -11.144 5.937   1.00 42.77  ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 0.773   -12.212 8.951   1.00 28.62  ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 1.632   -13.251 9.522   1.00 36.67  ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 1.160   -13.717 10.903  1.00 35.07  ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 1.376   -14.884 11.237  1.00 39.04  ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 3.143   -13.019 9.596   1.00 36.94  ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 3.636   -11.757 10.237  1.00 37.91  ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 5.135   -11.955 10.394  1.00 45.91  ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 5.751   -10.862 11.217  1.00 48.81  ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 5.453   -9.573  10.589  1.00 50.99  ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 0.507   -12.815 11.654  0.50 33.94  ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 0.520   -12.853 11.704  0.50 34.91  ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? -0.025  -13.133 12.975  0.50 36.86  ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 0.071   -13.367 12.995  0.50 37.27  ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? -1.097  -14.218 12.857  0.50 34.58  ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? -1.021  -14.405 12.780  0.50 35.14  ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? -1.213  -15.055 13.741  0.50 35.27  ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? -1.073  -15.383 13.515  0.50 35.52  ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? -0.566  -11.907 13.706  0.50 40.53  ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? -0.398  -12.320 13.995  0.50 43.38  ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 0.434   -10.885 14.248  0.50 39.88  ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? -0.773  -12.883 15.363  0.50 43.62  ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 1.643   -10.963 13.898  0.50 38.36  ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.125   -13.419 16.049  0.50 48.61  ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? -0.011  -10.009 15.032  0.50 36.73  ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.960  -12.811 15.730  0.50 47.46  ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -1.869  -14.203 11.760  1.00 32.64  ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -2.940  -15.169 11.508  1.00 33.52  ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -2.423  -16.456 10.848  1.00 36.30  ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -2.697  -17.545 11.334  1.00 36.67  ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -4.149  -14.540 10.797  1.00 35.18  ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -5.396  -15.412 10.677  1.00 40.44  ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -6.477  -14.596 9.984   1.00 47.84  ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -7.881  -15.055 10.215  1.00 52.27  ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -8.664  -14.409 9.163   1.00 48.75  ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -1.692  -16.332 9.724   1.00 33.41  ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -1.367  -17.471 8.885   1.00 31.01  ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 0.026   -18.023 9.167   1.00 30.43  ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 0.291   -19.146 8.771   1.00 32.50  ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -1.512  -17.069 7.409   1.00 30.15  ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -2.898  -16.561 7.057   1.00 32.14  ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -4.034  -17.298 7.352   1.00 36.99  ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -3.070  -15.335 6.433   1.00 39.70  ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -5.300  -16.831 7.029   1.00 38.50  ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -4.326  -14.856 6.100   1.00 36.41  ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -5.443  -15.607 6.404   1.00 40.48  ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -6.678  -15.144 6.070   1.00 35.18  ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 0.906   -17.253 9.826   1.00 35.05  ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 2.304   -17.630 10.037  1.00 32.90  ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 2.473   -18.610 11.191  1.00 36.00  ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 3.179   -18.330 12.158  1.00 40.14  ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 1.802   -19.761 11.081  1.00 41.49  ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 1.801   -20.798 12.107  1.00 43.47  ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 2.031   -22.149 11.436  1.00 37.85  ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 1.670   -22.343 10.275  1.00 39.68  ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 0.532   -20.690 12.968  1.00 42.16  ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 0.658   -19.681 14.096  1.00 46.21  ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? -0.691  -19.304 14.687  1.00 54.77  ? 70  LYS A CD  1 
ATOM   570  C CE  . LYS A 1 71 ? -0.521  -18.301 15.774  1.00 61.26  ? 70  LYS A CE  1 
ATOM   571  N NZ  . LYS A 1 71 ? -1.815  -17.641 15.949  1.00 66.82  ? 70  LYS A NZ  1 
ATOM   572  N N   . PRO A 1 72 ? 2.708   -23.113 12.092  1.00 34.84  ? 71  PRO A N   1 
ATOM   573  C CA  . PRO A 1 72 ? 3.046   -24.368 11.421  1.00 34.57  ? 71  PRO A CA  1 
ATOM   574  C C   . PRO A 1 72 ? 1.772   -25.046 10.929  1.00 41.60  ? 71  PRO A C   1 
ATOM   575  O O   . PRO A 1 72 ? 0.718   -24.865 11.530  1.00 43.27  ? 71  PRO A O   1 
ATOM   576  C CB  . PRO A 1 72 ? 3.771   -25.155 12.529  1.00 34.20  ? 71  PRO A CB  1 
ATOM   577  C CG  . PRO A 1 72 ? 4.326   -24.083 13.432  1.00 35.69  ? 71  PRO A CG  1 
ATOM   578  C CD  . PRO A 1 72 ? 3.201   -23.048 13.480  1.00 35.09  ? 71  PRO A CD  1 
ATOM   579  N N   . ASN A 1 73 ? 1.878   -25.773 9.803   1.00 48.49  ? 72  ASN A N   1 
ATOM   580  C CA  . ASN A 1 73 ? 0.785   -26.514 9.181   1.00 49.76  ? 72  ASN A CA  1 
ATOM   581  C C   . ASN A 1 73 ? 1.276   -27.925 8.863   1.00 49.22  ? 72  ASN A C   1 
ATOM   582  O O   . ASN A 1 73 ? 2.463   -28.128 8.592   1.00 42.92  ? 72  ASN A O   1 
ATOM   583  C CB  . ASN A 1 73 ? 0.278   -25.820 7.916   1.00 47.12  ? 72  ASN A CB  1 
ATOM   584  C CG  . ASN A 1 73 ? -1.044  -26.360 7.413   1.00 55.16  ? 72  ASN A CG  1 
ATOM   585  O OD1 . ASN A 1 73 ? -1.090  -27.432 6.805   1.00 65.08  ? 72  ASN A OD1 1 
ATOM   586  N ND2 . ASN A 1 73 ? -2.134  -25.637 7.624   1.00 57.78  ? 72  ASN A ND2 1 
ATOM   587  N N   . LYS A 1 74 ? 0.322   -28.865 8.842   1.00 51.62  ? 73  LYS A N   1 
ATOM   588  C CA  . LYS A 1 74 ? 0.543   -30.279 8.575   1.00 54.91  ? 73  LYS A CA  1 
ATOM   589  C C   . LYS A 1 74 ? 1.009   -30.507 7.130   1.00 58.93  ? 73  LYS A C   1 
ATOM   590  O O   . LYS A 1 74 ? 1.569   -31.564 6.840   1.00 68.93  ? 73  LYS A O   1 
ATOM   591  C CB  . LYS A 1 74 ? -0.664  -31.104 9.069   1.00 54.82  ? 73  LYS A CB  1 
ATOM   592  C CG  . LYS A 1 74 ? -1.802  -31.477 8.097   1.00 50.87  ? 73  LYS A CG  1 
ATOM   593  N N   . ARG A 1 75 ? 0.855   -29.508 6.244   1.00 53.79  ? 74  ARG A N   1 
ATOM   594  C CA  . ARG A 1 75 ? 1.001   -29.705 4.801   1.00 49.53  ? 74  ARG A CA  1 
ATOM   595  C C   . ARG A 1 75 ? 2.462   -29.733 4.333   1.00 47.01  ? 74  ARG A C   1 
ATOM   596  O O   . ARG A 1 75 ? 3.348   -29.124 4.936   1.00 44.16  ? 74  ARG A O   1 
ATOM   597  C CB  . ARG A 1 75 ? 0.200   -28.645 4.038   1.00 53.17  ? 74  ARG A CB  1 
ATOM   598  C CG  . ARG A 1 75 ? -1.264  -28.729 4.429   1.00 53.44  ? 74  ARG A CG  1 
ATOM   599  C CD  . ARG A 1 75 ? -1.874  -29.947 3.769   1.00 57.47  ? 74  ARG A CD  1 
ATOM   600  N NE  . ARG A 1 75 ? -2.651  -29.599 2.576   1.00 60.95  ? 74  ARG A NE  1 
ATOM   601  C CZ  . ARG A 1 75 ? -3.811  -28.944 2.639   1.00 60.90  ? 74  ARG A CZ  1 
ATOM   602  N NH1 . ARG A 1 75 ? -4.435  -28.665 1.508   1.00 59.10  ? 74  ARG A NH1 1 
ATOM   603  N NH2 . ARG A 1 75 ? -4.327  -28.578 3.818   1.00 55.55  ? 74  ARG A NH2 1 
ATOM   604  N N   . LYS A 1 76 ? 2.696   -30.422 3.203   1.00 46.13  ? 75  LYS A N   1 
ATOM   605  C CA  . LYS A 1 76 ? 4.030   -30.643 2.652   1.00 47.21  ? 75  LYS A CA  1 
ATOM   606  C C   . LYS A 1 76 ? 4.642   -29.295 2.264   1.00 42.60  ? 75  LYS A C   1 
ATOM   607  O O   . LYS A 1 76 ? 4.022   -28.518 1.551   1.00 43.93  ? 75  LYS A O   1 
ATOM   608  C CB  . LYS A 1 76 ? 4.019   -31.679 1.512   1.00 45.68  ? 75  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 76 ? 5.351   -32.296 1.070   1.00 49.88  ? 75  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 76 ? 5.211   -33.198 -0.158  1.00 48.75  ? 75  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 76 ? 6.521   -33.687 -0.709  1.00 48.38  ? 75  LYS A CE  1 
ATOM   612  N N   . GLY A 1 77 ? 5.839   -29.020 2.800   1.00 38.26  ? 76  GLY A N   1 
ATOM   613  C CA  . GLY A 1 77 ? 6.663   -27.879 2.450   1.00 33.01  ? 76  GLY A CA  1 
ATOM   614  C C   . GLY A 1 77 ? 6.201   -26.606 3.151   1.00 33.29  ? 76  GLY A C   1 
ATOM   615  O O   . GLY A 1 77 ? 6.770   -25.535 2.945   1.00 32.89  ? 76  GLY A O   1 
ATOM   616  N N   . PHE A 1 78 ? 5.160   -26.723 3.978   1.00 31.66  ? 77  PHE A N   1 
ATOM   617  C CA  . PHE A 1 78 ? 4.573   -25.528 4.562   1.00 33.60  ? 77  PHE A CA  1 
ATOM   618  C C   . PHE A 1 78 ? 5.542   -24.867 5.547   1.00 33.80  ? 77  PHE A C   1 
ATOM   619  O O   . PHE A 1 78 ? 5.791   -23.669 5.480   1.00 32.32  ? 77  PHE A O   1 
ATOM   620  C CB  . PHE A 1 78 ? 3.195   -25.825 5.169   1.00 32.22  ? 77  PHE A CB  1 
ATOM   621  C CG  . PHE A 1 78 ? 2.510   -24.533 5.593   1.00 34.52  ? 77  PHE A CG  1 
ATOM   622  C CD1 . PHE A 1 78 ? 2.839   -23.919 6.801   1.00 30.82  ? 77  PHE A CD1 1 
ATOM   623  C CD2 . PHE A 1 78 ? 1.542   -23.940 4.779   1.00 32.68  ? 77  PHE A CD2 1 
ATOM   624  C CE1 . PHE A 1 78 ? 2.219   -22.741 7.175   1.00 31.37  ? 77  PHE A CE1 1 
ATOM   625  C CE2 . PHE A 1 78 ? 0.909   -22.773 5.175   1.00 28.73  ? 77  PHE A CE2 1 
ATOM   626  C CZ  . PHE A 1 78 ? 1.260   -22.179 6.364   1.00 31.79  ? 77  PHE A CZ  1 
ATOM   627  N N   . ASN A 1 79 ? 6.042   -25.634 6.514   1.00 36.55  ? 78  ASN A N   1 
ATOM   628  C CA  . ASN A 1 79 ? 6.891   -25.081 7.558   1.00 33.59  ? 78  ASN A CA  1 
ATOM   629  C C   . ASN A 1 79 ? 8.258   -24.732 6.986   1.00 31.60  ? 78  ASN A C   1 
ATOM   630  O O   . ASN A 1 79 ? 8.914   -23.781 7.428   1.00 33.14  ? 78  ASN A O   1 
ATOM   631  C CB  . ASN A 1 79 ? 7.004   -26.030 8.740   1.00 37.88  ? 78  ASN A CB  1 
ATOM   632  C CG  . ASN A 1 79 ? 5.672   -26.312 9.386   1.00 38.28  ? 78  ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 79 ? 4.769   -25.475 9.364   1.00 38.49  ? 78  ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 79 ? 5.543   -27.476 9.998   1.00 46.04  ? 78  ASN A ND2 1 
ATOM   635  N N   . GLU A 1 80 ? 8.681   -25.502 5.983   1.00 31.64  ? 79  GLU A N   1 
ATOM   636  C CA  . GLU A 1 80 ? 9.854   -25.094 5.237   1.00 33.01  ? 79  GLU A CA  1 
ATOM   637  C C   . GLU A 1 80 ? 9.559   -23.732 4.613   1.00 33.92  ? 79  GLU A C   1 
ATOM   638  O O   . GLU A 1 80 ? 10.413  -22.852 4.597   1.00 28.92  ? 79  GLU A O   1 
ATOM   639  C CB  . GLU A 1 80 ? 10.333  -26.151 4.249   1.00 33.43  ? 79  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 80 ? 11.506  -25.670 3.401   1.00 38.29  ? 79  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 80 ? 11.971  -26.591 2.283   1.00 48.34  ? 79  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 80 ? 11.241  -27.539 1.905   1.00 46.26  ? 79  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 80 ? 13.098  -26.354 1.780   1.00 49.77  ? 79  GLU A OE2 1 
ATOM   644  N N   . GLY A 1 81 ? 8.321   -23.559 4.140   1.00 33.67  ? 80  GLY A N   1 
ATOM   645  C CA  . GLY A 1 81 ? 7.952   -22.309 3.495   1.00 30.79  ? 80  GLY A CA  1 
ATOM   646  C C   . GLY A 1 81 ? 7.982   -21.156 4.493   1.00 24.34  ? 80  GLY A C   1 
ATOM   647  O O   . GLY A 1 81 ? 8.383   -20.049 4.159   1.00 25.76  ? 80  GLY A O   1 
ATOM   648  N N   . LEU A 1 82 ? 7.533   -21.427 5.717   1.00 26.02  ? 81  LEU A N   1 
ATOM   649  C CA  . LEU A 1 82 ? 7.576   -20.462 6.812   1.00 26.00  ? 81  LEU A CA  1 
ATOM   650  C C   . LEU A 1 82 ? 9.021   -20.046 7.100   1.00 26.91  ? 81  LEU A C   1 
ATOM   651  O O   . LEU A 1 82 ? 9.290   -18.863 7.292   1.00 25.27  ? 81  LEU A O   1 
ATOM   652  C CB  . LEU A 1 82 ? 6.879   -20.946 8.080   1.00 25.92  ? 81  LEU A CB  1 
ATOM   653  C CG  . LEU A 1 82 ? 5.360   -21.135 8.035   1.00 28.47  ? 81  LEU A CG  1 
ATOM   654  C CD1 . LEU A 1 82 ? 4.983   -21.625 9.431   1.00 31.78  ? 81  LEU A CD1 1 
ATOM   655  C CD2 . LEU A 1 82 ? 4.569   -19.857 7.748   1.00 28.49  ? 81  LEU A CD2 1 
ATOM   656  N N   . TRP A 1 83 ? 9.950   -21.015 7.144   1.00 26.58  ? 82  TRP A N   1 
ATOM   657  C CA  . TRP A 1 83 ? 11.350  -20.659 7.334   1.00 25.82  ? 82  TRP A CA  1 
ATOM   658  C C   . TRP A 1 83 ? 11.817  -19.723 6.213   1.00 24.84  ? 82  TRP A C   1 
ATOM   659  O O   . TRP A 1 83 ? 12.441  -18.702 6.476   1.00 24.07  ? 82  TRP A O   1 
ATOM   660  C CB  . TRP A 1 83 ? 12.267  -21.893 7.453   1.00 26.34  ? 82  TRP A CB  1 
ATOM   661  C CG  . TRP A 1 83 ? 13.727  -21.505 7.610   1.00 26.64  ? 82  TRP A CG  1 
ATOM   662  C CD1 . TRP A 1 83 ? 14.399  -21.376 8.789   1.00 26.01  ? 82  TRP A CD1 1 
ATOM   663  C CD2 . TRP A 1 83 ? 14.655  -21.135 6.562   1.00 27.57  ? 82  TRP A CD2 1 
ATOM   664  N NE1 . TRP A 1 83 ? 15.682  -20.967 8.555   1.00 27.99  ? 82  TRP A NE1 1 
ATOM   665  C CE2 . TRP A 1 83 ? 15.873  -20.819 7.197   1.00 31.17  ? 82  TRP A CE2 1 
ATOM   666  C CE3 . TRP A 1 83 ? 14.581  -21.052 5.161   1.00 27.02  ? 82  TRP A CE3 1 
ATOM   667  C CZ2 . TRP A 1 83 ? 17.005  -20.424 6.481   1.00 28.73  ? 82  TRP A CZ2 1 
ATOM   668  C CZ3 . TRP A 1 83 ? 15.694  -20.662 4.440   1.00 27.76  ? 82  TRP A CZ3 1 
ATOM   669  C CH2 . TRP A 1 83 ? 16.891  -20.334 5.103   1.00 29.96  ? 82  TRP A CH2 1 
ATOM   670  N N   . GLU A 1 84 ? 11.484  -20.032 4.950   1.00 24.22  ? 83  GLU A N   1 
ATOM   671  C CA  . GLU A 1 84 ? 12.060  -19.280 3.849   1.00 24.08  ? 83  GLU A CA  1 
ATOM   672  C C   . GLU A 1 84 ? 11.515  -17.863 3.868   1.00 23.74  ? 83  GLU A C   1 
ATOM   673  O O   . GLU A 1 84 ? 12.248  -16.892 3.654   1.00 24.48  ? 83  GLU A O   1 
ATOM   674  C CB  . GLU A 1 84 ? 11.738  -19.939 2.517   1.00 27.42  ? 83  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 84 ? 12.311  -21.351 2.414   1.00 31.77  ? 83  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 84 ? 11.868  -22.023 1.118   1.00 30.11  ? 83  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 84 ? 10.987  -21.474 0.386   1.00 27.89  ? 83  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 84 ? 12.431  -23.108 0.850   1.00 28.26  ? 83  GLU A OE2 1 
ATOM   679  N N   . ILE A 1 85 ? 10.213  -17.733 4.134   1.00 23.30  ? 84  ILE A N   1 
ATOM   680  C CA  . ILE A 1 85 ? 9.652   -16.399 3.991   1.00 22.97  ? 84  ILE A CA  1 
ATOM   681  C C   . ILE A 1 85 ? 10.219  -15.491 5.085   1.00 22.72  ? 84  ILE A C   1 
ATOM   682  O O   . ILE A 1 85 ? 10.380  -14.297 4.875   1.00 23.71  ? 84  ILE A O   1 
ATOM   683  C CB  . ILE A 1 85 ? 8.114   -16.449 3.966   1.00 20.56  ? 84  ILE A CB  1 
ATOM   684  C CG1 . ILE A 1 85 ? 7.532   -15.108 3.495   1.00 21.01  ? 84  ILE A CG1 1 
ATOM   685  C CG2 . ILE A 1 85 ? 7.546   -16.886 5.304   1.00 18.53  ? 84  ILE A CG2 1 
ATOM   686  C CD1 . ILE A 1 85 ? 6.055   -15.185 3.133   1.00 18.70  ? 84  ILE A CD1 1 
ATOM   687  N N   . GLN A 1 86 ? 10.539  -16.080 6.249   1.00 22.25  ? 85  GLN A N   1 
ATOM   688  C CA  . GLN A 1 86 ? 11.022  -15.348 7.412   1.00 27.27  ? 85  GLN A CA  1 
ATOM   689  C C   . GLN A 1 86 ? 12.526  -15.085 7.303   1.00 27.29  ? 85  GLN A C   1 
ATOM   690  O O   . GLN A 1 86 ? 12.961  -14.009 7.672   1.00 27.86  ? 85  GLN A O   1 
ATOM   691  C CB  . GLN A 1 86 ? 10.660  -16.128 8.672   1.00 26.36  ? 85  GLN A CB  1 
ATOM   692  C CG  . GLN A 1 86 ? 10.735  -15.340 9.975   1.00 39.21  ? 85  GLN A CG  1 
ATOM   693  C CD  . GLN A 1 86 ? 9.988   -16.039 11.101  1.00 45.63  ? 85  GLN A CD  1 
ATOM   694  O OE1 . GLN A 1 86 ? 9.521   -17.189 10.989  1.00 49.83  ? 85  GLN A OE1 1 
ATOM   695  N NE2 . GLN A 1 86 ? 9.857   -15.322 12.205  1.00 50.35  ? 85  GLN A NE2 1 
ATOM   696  N N   . ASN A 1 87 ? 13.280  -16.019 6.705   1.00 25.30  ? 86  ASN A N   1 
ATOM   697  C CA  . ASN A 1 87 ? 14.724  -16.050 6.830   1.00 25.71  ? 86  ASN A CA  1 
ATOM   698  C C   . ASN A 1 87 ? 15.474  -15.701 5.532   1.00 27.05  ? 86  ASN A C   1 
ATOM   699  O O   . ASN A 1 87 ? 16.600  -15.187 5.576   1.00 25.66  ? 86  ASN A O   1 
ATOM   700  C CB  . ASN A 1 87 ? 15.117  -17.367 7.463   1.00 26.36  ? 86  ASN A CB  1 
ATOM   701  C CG  . ASN A 1 87 ? 14.646  -17.369 8.899   1.00 27.93  ? 86  ASN A CG  1 
ATOM   702  O OD1 . ASN A 1 87 ? 15.100  -16.551 9.695   1.00 28.47  ? 86  ASN A OD1 1 
ATOM   703  N ND2 . ASN A 1 87 ? 13.702  -18.226 9.244   1.00 27.61  ? 86  ASN A ND2 1 
ATOM   704  N N   . ASN A 1 88 ? 14.876  -15.990 4.371   1.00 22.49  ? 87  ASN A N   1 
ATOM   705  C CA  . ASN A 1 88 ? 15.546  -15.675 3.121   1.00 23.14  ? 87  ASN A CA  1 
ATOM   706  C C   . ASN A 1 88 ? 14.505  -15.672 1.998   1.00 21.60  ? 87  ASN A C   1 
ATOM   707  O O   . ASN A 1 88 ? 14.634  -16.442 1.049   1.00 20.85  ? 87  ASN A O   1 
ATOM   708  C CB  . ASN A 1 88 ? 16.759  -16.573 2.864   1.00 25.35  ? 87  ASN A CB  1 
ATOM   709  C CG  . ASN A 1 88 ? 17.800  -15.968 1.930   1.00 30.08  ? 87  ASN A CG  1 
ATOM   710  O OD1 . ASN A 1 88 ? 17.519  -15.007 1.202   1.00 27.51  ? 87  ASN A OD1 1 
ATOM   711  N ND2 . ASN A 1 88 ? 19.005  -16.533 1.906   1.00 25.11  ? 87  ASN A ND2 1 
ATOM   712  N N   . PRO A 1 89 ? 13.495  -14.770 2.060   1.00 21.34  ? 88  PRO A N   1 
ATOM   713  C CA  . PRO A 1 89 ? 12.407  -14.718 1.084   1.00 20.44  ? 88  PRO A CA  1 
ATOM   714  C C   . PRO A 1 89 ? 12.801  -14.321 -0.320  1.00 20.25  ? 88  PRO A C   1 
ATOM   715  O O   . PRO A 1 89 ? 12.054  -14.615 -1.233  1.00 22.60  ? 88  PRO A O   1 
ATOM   716  C CB  . PRO A 1 89 ? 11.413  -13.716 1.679   1.00 20.82  ? 88  PRO A CB  1 
ATOM   717  C CG  . PRO A 1 89 ? 12.296  -12.831 2.526   1.00 20.00  ? 88  PRO A CG  1 
ATOM   718  C CD  . PRO A 1 89 ? 13.278  -13.796 3.146   1.00 23.27  ? 88  PRO A CD  1 
ATOM   719  N N   . HIS A 1 90 ? 13.978  -13.677 -0.482  1.00 25.02  ? 89  HIS A N   1 
ATOM   720  C CA  . HIS A 1 90 ? 14.384  -13.068 -1.741  1.00 23.91  ? 89  HIS A CA  1 
ATOM   721  C C   . HIS A 1 90 ? 15.490  -13.863 -2.432  1.00 26.62  ? 89  HIS A C   1 
ATOM   722  O O   . HIS A 1 90 ? 15.994  -13.416 -3.468  1.00 28.84  ? 89  HIS A O   1 
ATOM   723  C CB  . HIS A 1 90 ? 14.734  -11.603 -1.491  1.00 22.78  ? 89  HIS A CB  1 
ATOM   724  C CG  . HIS A 1 90 ? 13.563  -10.848 -0.950  1.00 23.19  ? 89  HIS A CG  1 
ATOM   725  N ND1 . HIS A 1 90 ? 12.406  -10.684 -1.686  1.00 19.28  ? 89  HIS A ND1 1 
ATOM   726  C CD2 . HIS A 1 90 ? 13.337  -10.265 0.239   1.00 20.78  ? 89  HIS A CD2 1 
ATOM   727  C CE1 . HIS A 1 90 ? 11.557  -9.977  -0.986  1.00 19.77  ? 89  HIS A CE1 1 
ATOM   728  N NE2 . HIS A 1 90 ? 12.086  -9.711  0.187   1.00 19.51  ? 89  HIS A NE2 1 
ATOM   729  N N   . ALA A 1 91 ? 15.811  -15.059 -1.890  1.00 28.19  ? 90  ALA A N   1 
ATOM   730  C CA  . ALA A 1 91 ? 16.835  -15.925 -2.474  1.00 27.64  ? 90  ALA A CA  1 
ATOM   731  C C   . ALA A 1 91 ? 16.336  -16.607 -3.742  1.00 26.72  ? 90  ALA A C   1 
ATOM   732  O O   . ALA A 1 91 ? 15.145  -16.648 -4.035  1.00 26.30  ? 90  ALA A O   1 
ATOM   733  C CB  . ALA A 1 91 ? 17.298  -16.960 -1.463  1.00 25.84  ? 90  ALA A CB  1 
ATOM   734  N N   . SER A 1 92 ? 17.292  -17.171 -4.487  1.00 29.77  ? 91  SER A N   1 
ATOM   735  C CA  . SER A 1 92 ? 17.019  -18.047 -5.610  1.00 31.64  ? 91  SER A CA  1 
ATOM   736  C C   . SER A 1 92 ? 16.716  -19.442 -5.081  1.00 32.39  ? 91  SER A C   1 
ATOM   737  O O   . SER A 1 92 ? 17.519  -19.990 -4.343  1.00 34.90  ? 91  SER A O   1 
ATOM   738  C CB  . SER A 1 92 ? 18.217  -18.064 -6.519  1.00 35.62  ? 91  SER A CB  1 
ATOM   739  O OG  . SER A 1 92 ? 18.200  -19.237 -7.322  1.00 39.98  ? 91  SER A OG  1 
ATOM   740  N N   . TYR A 1 93 ? 15.554  -20.007 -5.436  1.00 34.97  ? 92  TYR A N   1 
ATOM   741  C CA  . TYR A 1 93 ? 15.183  -21.359 -5.022  1.00 37.30  ? 92  TYR A CA  1 
ATOM   742  C C   . TYR A 1 93 ? 15.067  -22.276 -6.238  1.00 42.20  ? 92  TYR A C   1 
ATOM   743  O O   . TYR A 1 93 ? 14.502  -23.360 -6.138  1.00 46.49  ? 92  TYR A O   1 
ATOM   744  C CB  . TYR A 1 93 ? 13.850  -21.381 -4.249  1.00 37.78  ? 92  TYR A CB  1 
ATOM   745  C CG  . TYR A 1 93 ? 13.975  -20.781 -2.851  1.00 35.71  ? 92  TYR A CG  1 
ATOM   746  C CD1 . TYR A 1 93 ? 14.481  -21.536 -1.798  1.00 36.54  ? 92  TYR A CD1 1 
ATOM   747  C CD2 . TYR A 1 93 ? 13.602  -19.455 -2.581  1.00 35.36  ? 92  TYR A CD2 1 
ATOM   748  C CE1 . TYR A 1 93 ? 14.623  -20.994 -0.527  1.00 35.52  ? 92  TYR A CE1 1 
ATOM   749  C CE2 . TYR A 1 93 ? 13.716  -18.912 -1.309  1.00 37.30  ? 92  TYR A CE2 1 
ATOM   750  C CZ  . TYR A 1 93 ? 14.240  -19.684 -0.281  1.00 36.52  ? 92  TYR A CZ  1 
ATOM   751  O OH  . TYR A 1 93 ? 14.402  -19.172 0.976   1.00 35.52  ? 92  TYR A OH  1 
ATOM   752  N N   . SER A 1 94 ? 15.595  -21.813 -7.379  1.00 50.07  ? 93  SER A N   1 
ATOM   753  C CA  . SER A 1 94 ? 15.635  -22.508 -8.663  1.00 59.68  ? 93  SER A CA  1 
ATOM   754  C C   . SER A 1 94 ? 16.544  -23.758 -8.628  1.00 63.61  ? 93  SER A C   1 
ATOM   755  O O   . SER A 1 94 ? 17.091  -24.105 -7.533  1.00 59.18  ? 93  SER A O   1 
ATOM   756  C CB  . SER A 1 94 ? 16.085  -21.553 -9.773  1.00 64.87  ? 93  SER A CB  1 
ATOM   757  O OG  . SER A 1 94 ? 15.292  -20.372 -9.830  1.00 76.89  ? 93  SER A OG  1 
ATOM   758  O OXT . SER A 1 94 ? 16.690  -24.364 -9.723  1.00 74.91  ? 93  SER A OXT 1 
ATOM   759  N N   . MET B 1 2  ? 38.853  -11.463 -40.793 1.00 102.23 ? 1   MET B N   1 
ATOM   760  C CA  . MET B 1 2  ? 38.517  -12.459 -41.848 1.00 103.12 ? 1   MET B CA  1 
ATOM   761  C C   . MET B 1 2  ? 36.996  -12.638 -41.876 1.00 92.32  ? 1   MET B C   1 
ATOM   762  O O   . MET B 1 2  ? 36.380  -12.808 -40.826 1.00 87.98  ? 1   MET B O   1 
ATOM   763  C CB  . MET B 1 2  ? 39.261  -13.784 -41.599 1.00 102.96 ? 1   MET B CB  1 
ATOM   764  C CG  . MET B 1 2  ? 39.551  -14.644 -42.834 1.00 93.25  ? 1   MET B CG  1 
ATOM   765  S SD  . MET B 1 2  ? 40.624  -13.974 -44.127 1.00 83.50  ? 1   MET B SD  1 
ATOM   766  C CE  . MET B 1 2  ? 42.079  -13.498 -43.178 1.00 82.54  ? 1   MET B CE  1 
ATOM   767  N N   . PRO B 1 3  ? 36.336  -12.525 -43.059 1.00 81.34  ? 2   PRO B N   1 
ATOM   768  C CA  . PRO B 1 3  ? 34.912  -12.839 -43.191 1.00 75.47  ? 2   PRO B CA  1 
ATOM   769  C C   . PRO B 1 3  ? 34.546  -14.301 -42.950 1.00 80.15  ? 2   PRO B C   1 
ATOM   770  O O   . PRO B 1 3  ? 35.020  -15.199 -43.652 1.00 83.82  ? 2   PRO B O   1 
ATOM   771  C CB  . PRO B 1 3  ? 34.551  -12.395 -44.624 1.00 73.53  ? 2   PRO B CB  1 
ATOM   772  C CG  . PRO B 1 3  ? 35.687  -11.495 -45.038 1.00 74.76  ? 2   PRO B CG  1 
ATOM   773  C CD  . PRO B 1 3  ? 36.916  -12.015 -44.312 1.00 74.18  ? 2   PRO B CD  1 
ATOM   774  N N   . HIS B 1 4  ? 33.683  -14.505 -41.944 1.00 77.56  ? 3   HIS B N   1 
ATOM   775  C CA  . HIS B 1 4  ? 33.004  -15.766 -41.682 1.00 70.66  ? 3   HIS B CA  1 
ATOM   776  C C   . HIS B 1 4  ? 31.602  -15.691 -42.296 1.00 72.59  ? 3   HIS B C   1 
ATOM   777  O O   . HIS B 1 4  ? 31.194  -14.635 -42.791 1.00 71.71  ? 3   HIS B O   1 
ATOM   778  C CB  . HIS B 1 4  ? 32.937  -16.042 -40.175 1.00 72.74  ? 3   HIS B CB  1 
ATOM   779  C CG  . HIS B 1 4  ? 34.227  -15.905 -39.419 1.00 73.20  ? 3   HIS B CG  1 
ATOM   780  N ND1 . HIS B 1 4  ? 35.479  -16.029 -39.986 1.00 72.87  ? 3   HIS B ND1 1 
ATOM   781  C CD2 . HIS B 1 4  ? 34.436  -15.665 -38.111 1.00 66.93  ? 3   HIS B CD2 1 
ATOM   782  C CE1 . HIS B 1 4  ? 36.404  -15.858 -39.048 1.00 72.15  ? 3   HIS B CE1 1 
ATOM   783  N NE2 . HIS B 1 4  ? 35.790  -15.641 -37.899 1.00 69.39  ? 3   HIS B NE2 1 
ATOM   784  N N   . ALA B 1 5  ? 30.867  -16.815 -42.278 1.00 57.40  ? 4   ALA B N   1 
ATOM   785  C CA  . ALA B 1 5  ? 29.612  -16.898 -43.009 1.00 52.43  ? 4   ALA B CA  1 
ATOM   786  C C   . ALA B 1 5  ? 28.610  -15.934 -42.388 1.00 48.61  ? 4   ALA B C   1 
ATOM   787  O O   . ALA B 1 5  ? 27.875  -15.261 -43.102 1.00 47.57  ? 4   ALA B O   1 
ATOM   788  C CB  . ALA B 1 5  ? 29.099  -18.311 -42.993 1.00 64.69  ? 4   ALA B CB  1 
ATOM   789  N N   . PHE B 1 6  ? 28.599  -15.910 -41.047 1.00 41.31  ? 5   PHE B N   1 
ATOM   790  C CA  . PHE B 1 6  ? 27.916  -14.908 -40.246 1.00 43.17  ? 5   PHE B CA  1 
ATOM   791  C C   . PHE B 1 6  ? 28.875  -13.767 -39.883 1.00 41.06  ? 5   PHE B C   1 
ATOM   792  O O   . PHE B 1 6  ? 29.946  -13.989 -39.319 1.00 45.20  ? 5   PHE B O   1 
ATOM   793  C CB  . PHE B 1 6  ? 27.319  -15.538 -38.978 1.00 36.22  ? 5   PHE B CB  1 
ATOM   794  C CG  . PHE B 1 6  ? 26.094  -16.417 -39.211 1.00 35.57  ? 5   PHE B CG  1 
ATOM   795  C CD1 . PHE B 1 6  ? 24.852  -15.846 -39.497 1.00 29.53  ? 5   PHE B CD1 1 
ATOM   796  C CD2 . PHE B 1 6  ? 26.183  -17.802 -39.102 1.00 31.02  ? 5   PHE B CD2 1 
ATOM   797  C CE1 . PHE B 1 6  ? 23.717  -16.623 -39.664 1.00 27.56  ? 5   PHE B CE1 1 
ATOM   798  C CE2 . PHE B 1 6  ? 25.037  -18.574 -39.256 1.00 29.27  ? 5   PHE B CE2 1 
ATOM   799  C CZ  . PHE B 1 6  ? 23.821  -17.985 -39.560 1.00 31.35  ? 5   PHE B CZ  1 
ATOM   800  N N   . LYS B 1 7  ? 28.452  -12.536 -40.189 1.00 39.87  ? 6   LYS B N   1 
ATOM   801  C CA  . LYS B 1 7  ? 29.189  -11.329 -39.878 1.00 41.16  ? 6   LYS B CA  1 
ATOM   802  C C   . LYS B 1 7  ? 28.325  -10.439 -38.984 1.00 44.67  ? 6   LYS B C   1 
ATOM   803  O O   . LYS B 1 7  ? 27.104  -10.497 -39.075 1.00 41.85  ? 6   LYS B O   1 
ATOM   804  C CB  . LYS B 1 7  ? 29.474  -10.671 -41.230 1.00 43.37  ? 6   LYS B CB  1 
ATOM   805  C CG  . LYS B 1 7  ? 28.274  -10.643 -42.148 1.00 49.74  ? 6   LYS B CG  1 
ATOM   806  C CD  . LYS B 1 7  ? 28.438  -9.863  -43.444 1.00 54.90  ? 6   LYS B CD  1 
ATOM   807  C CE  . LYS B 1 7  ? 27.110  -9.564  -44.072 1.00 55.00  ? 6   LYS B CE  1 
ATOM   808  N NZ  . LYS B 1 7  ? 26.304  -10.785 -44.186 1.00 58.54  ? 6   LYS B NZ  1 
ATOM   809  N N   . PRO B 1 8  ? 28.914  -9.629  -38.066 1.00 48.38  ? 7   PRO B N   1 
ATOM   810  C CA  . PRO B 1 8  ? 28.189  -8.567  -37.361 1.00 46.24  ? 7   PRO B CA  1 
ATOM   811  C C   . PRO B 1 8  ? 27.023  -7.902  -38.086 1.00 38.24  ? 7   PRO B C   1 
ATOM   812  O O   . PRO B 1 8  ? 27.146  -7.481  -39.221 1.00 40.10  ? 7   PRO B O   1 
ATOM   813  C CB  . PRO B 1 8  ? 29.348  -7.615  -37.105 1.00 46.27  ? 7   PRO B CB  1 
ATOM   814  C CG  . PRO B 1 8  ? 30.455  -8.545  -36.666 1.00 51.02  ? 7   PRO B CG  1 
ATOM   815  C CD  . PRO B 1 8  ? 30.305  -9.738  -37.597 1.00 52.78  ? 7   PRO B CD  1 
ATOM   816  N N   . GLY B 1 9  ? 25.864  -7.856  -37.416 1.00 37.01  ? 8   GLY B N   1 
ATOM   817  C CA  . GLY B 1 9  ? 24.731  -7.162  -37.995 1.00 33.51  ? 8   GLY B CA  1 
ATOM   818  C C   . GLY B 1 9  ? 23.742  -8.101  -38.676 1.00 28.63  ? 8   GLY B C   1 
ATOM   819  O O   . GLY B 1 9  ? 22.639  -7.675  -38.989 1.00 32.43  ? 8   GLY B O   1 
ATOM   820  N N   . ASP B 1 10 ? 24.147  -9.359  -38.913 1.00 27.46  ? 9   ASP B N   1 
ATOM   821  C CA  . ASP B 1 10 ? 23.314  -10.352 -39.582 1.00 29.10  ? 9   ASP B CA  1 
ATOM   822  C C   . ASP B 1 10 ? 22.180  -10.757 -38.644 1.00 29.69  ? 9   ASP B C   1 
ATOM   823  O O   . ASP B 1 10 ? 22.419  -10.999 -37.453 1.00 27.23  ? 9   ASP B O   1 
ATOM   824  C CB  . ASP B 1 10 ? 24.096  -11.611 -39.910 1.00 34.18  ? 9   ASP B CB  1 
ATOM   825  C CG  . ASP B 1 10 ? 24.902  -11.566 -41.204 1.00 40.85  ? 9   ASP B CG  1 
ATOM   826  O OD1 . ASP B 1 10 ? 24.786  -10.546 -41.934 1.00 38.21  ? 9   ASP B OD1 1 
ATOM   827  O OD2 . ASP B 1 10 ? 25.612  -12.560 -41.477 1.00 39.63  ? 9   ASP B OD2 1 
ATOM   828  N N   . LEU B 1 11 ? 20.975  -10.856 -39.213 1.00 27.68  ? 10  LEU B N   1 
ATOM   829  C CA  . LEU B 1 11 ? 19.749  -10.992 -38.445 1.00 26.55  ? 10  LEU B CA  1 
ATOM   830  C C   . LEU B 1 11 ? 19.338  -12.460 -38.411 1.00 28.97  ? 10  LEU B C   1 
ATOM   831  O O   . LEU B 1 11 ? 19.326  -13.130 -39.442 1.00 30.64  ? 10  LEU B O   1 
ATOM   832  C CB  . LEU B 1 11 ? 18.655  -10.057 -38.958 1.00 25.49  ? 10  LEU B CB  1 
ATOM   833  C CG  . LEU B 1 11 ? 19.040  -8.567  -38.956 1.00 24.28  ? 10  LEU B CG  1 
ATOM   834  C CD1 . LEU B 1 11 ? 17.871  -7.739  -39.424 1.00 21.86  ? 10  LEU B CD1 1 
ATOM   835  C CD2 . LEU B 1 11 ? 19.571  -8.113  -37.572 1.00 22.52  ? 10  LEU B CD2 1 
ATOM   836  N N   . VAL B 1 12 ? 19.110  -12.987 -37.201 1.00 25.80  ? 11  VAL B N   1 
ATOM   837  C CA  . VAL B 1 12 ? 18.825  -14.402 -37.075 1.00 25.45  ? 11  VAL B CA  1 
ATOM   838  C C   . VAL B 1 12 ? 17.640  -14.615 -36.134 1.00 29.64  ? 11  VAL B C   1 
ATOM   839  O O   . VAL B 1 12 ? 17.219  -13.698 -35.413 1.00 26.61  ? 11  VAL B O   1 
ATOM   840  C CB  . VAL B 1 12 ? 20.055  -15.190 -36.599 1.00 23.13  ? 11  VAL B CB  1 
ATOM   841  C CG1 . VAL B 1 12 ? 21.214  -15.124 -37.600 1.00 26.73  ? 11  VAL B CG1 1 
ATOM   842  C CG2 . VAL B 1 12 ? 20.509  -14.823 -35.174 1.00 24.90  ? 11  VAL B CG2 1 
ATOM   843  N N   . PHE B 1 13 ? 17.138  -15.855 -36.129 1.00 26.65  ? 12  PHE B N   1 
ATOM   844  C CA  . PHE B 1 13 ? 16.539  -16.380 -34.918 1.00 27.38  ? 12  PHE B CA  1 
ATOM   845  C C   . PHE B 1 13 ? 17.562  -17.332 -34.315 1.00 27.75  ? 12  PHE B C   1 
ATOM   846  O O   . PHE B 1 13 ? 18.114  -18.153 -35.038 1.00 28.40  ? 12  PHE B O   1 
ATOM   847  C CB  . PHE B 1 13 ? 15.233  -17.109 -35.214 1.00 25.93  ? 12  PHE B CB  1 
ATOM   848  C CG  . PHE B 1 13 ? 14.091  -16.206 -35.646 1.00 26.91  ? 12  PHE B CG  1 
ATOM   849  C CD1 . PHE B 1 13 ? 13.941  -15.851 -36.983 1.00 25.33  ? 12  PHE B CD1 1 
ATOM   850  C CD2 . PHE B 1 13 ? 13.159  -15.742 -34.719 1.00 26.00  ? 12  PHE B CD2 1 
ATOM   851  C CE1 . PHE B 1 13 ? 12.882  -15.047 -37.369 1.00 28.78  ? 12  PHE B CE1 1 
ATOM   852  C CE2 . PHE B 1 13 ? 12.091  -14.952 -35.115 1.00 21.65  ? 12  PHE B CE2 1 
ATOM   853  C CZ  . PHE B 1 13 ? 11.966  -14.604 -36.435 1.00 25.22  ? 12  PHE B CZ  1 
ATOM   854  N N   . ALA B 1 14 ? 17.797  -17.219 -33.000 1.00 25.53  ? 13  ALA B N   1 
ATOM   855  C CA  . ALA B 1 14 ? 18.827  -17.971 -32.316 1.00 25.34  ? 13  ALA B CA  1 
ATOM   856  C C   . ALA B 1 14 ? 18.197  -18.953 -31.324 1.00 30.96  ? 13  ALA B C   1 
ATOM   857  O O   . ALA B 1 14 ? 17.325  -18.583 -30.544 1.00 35.40  ? 13  ALA B O   1 
ATOM   858  C CB  . ALA B 1 14 ? 19.747  -17.009 -31.638 1.00 23.82  ? 13  ALA B CB  1 
ATOM   859  N N   . LYS B 1 15 ? 18.627  -20.222 -31.348 1.00 29.27  ? 14  LYS B N   1 
ATOM   860  C CA  . LYS B 1 15 ? 17.964  -21.216 -30.524 1.00 29.55  ? 14  LYS B CA  1 
ATOM   861  C C   . LYS B 1 15 ? 18.790  -21.473 -29.272 1.00 30.45  ? 14  LYS B C   1 
ATOM   862  O O   . LYS B 1 15 ? 19.959  -21.827 -29.383 1.00 30.72  ? 14  LYS B O   1 
ATOM   863  C CB  . LYS B 1 15 ? 17.755  -22.472 -31.373 1.00 27.91  ? 14  LYS B CB  1 
ATOM   864  C CG  . LYS B 1 15 ? 16.906  -23.538 -30.722 1.00 27.15  ? 14  LYS B CG  1 
ATOM   865  C CD  . LYS B 1 15 ? 15.524  -23.129 -30.243 1.00 29.35  ? 14  LYS B CD  1 
ATOM   866  C CE  . LYS B 1 15 ? 14.840  -24.304 -29.604 1.00 28.81  ? 14  LYS B CE  1 
ATOM   867  N NZ  . LYS B 1 15 ? 15.220  -24.274 -28.203 1.00 29.45  ? 14  LYS B NZ  1 
ATOM   868  N N   . MET B 1 16 ? 18.182  -21.253 -28.093 1.00 34.43  ? 15  MET B N   1 
ATOM   869  C CA  . MET B 1 16 ? 18.785  -21.608 -26.812 1.00 34.24  ? 15  MET B CA  1 
ATOM   870  C C   . MET B 1 16 ? 17.983  -22.768 -26.232 1.00 36.96  ? 15  MET B C   1 
ATOM   871  O O   . MET B 1 16 ? 16.778  -22.845 -26.482 1.00 38.18  ? 15  MET B O   1 
ATOM   872  C CB  . MET B 1 16 ? 18.617  -20.503 -25.767 1.00 37.36  ? 15  MET B CB  1 
ATOM   873  C CG  . MET B 1 16 ? 19.229  -19.190 -26.109 1.00 41.13  ? 15  MET B CG  1 
ATOM   874  S SD  . MET B 1 16 ? 21.000  -19.292 -25.838 1.00 50.76  ? 15  MET B SD  1 
ATOM   875  C CE  . MET B 1 16 ? 21.204  -19.470 -24.059 1.00 50.98  ? 15  MET B CE  1 
ATOM   876  N N   . LYS B 1 17 ? 18.641  -23.638 -25.445 1.00 39.54  ? 16  LYS B N   1 
ATOM   877  C CA  . LYS B 1 17 ? 17.967  -24.724 -24.730 1.00 46.25  ? 16  LYS B CA  1 
ATOM   878  C C   . LYS B 1 17 ? 16.842  -24.160 -23.853 1.00 41.63  ? 16  LYS B C   1 
ATOM   879  O O   . LYS B 1 17 ? 17.048  -23.205 -23.113 1.00 40.30  ? 16  LYS B O   1 
ATOM   880  C CB  . LYS B 1 17 ? 18.916  -25.677 -23.978 1.00 46.33  ? 16  LYS B CB  1 
ATOM   881  C CG  . LYS B 1 17 ? 18.457  -27.153 -23.957 1.00 57.13  ? 16  LYS B CG  1 
ATOM   882  C CD  . LYS B 1 17 ? 18.319  -27.870 -22.613 1.00 53.66  ? 16  LYS B CD  1 
ATOM   883  N N   . GLY B 1 18 ? 15.630  -24.696 -24.033 1.00 44.09  ? 17  GLY B N   1 
ATOM   884  C CA  . GLY B 1 18 ? 14.460  -24.363 -23.227 1.00 43.22  ? 17  GLY B CA  1 
ATOM   885  C C   . GLY B 1 18 ? 13.719  -23.089 -23.650 1.00 46.39  ? 17  GLY B C   1 
ATOM   886  O O   . GLY B 1 18 ? 12.925  -22.577 -22.865 1.00 43.69  ? 17  GLY B O   1 
ATOM   887  N N   . TYR B 1 19 ? 13.967  -22.555 -24.867 1.00 37.99  ? 18  TYR B N   1 
ATOM   888  C CA  . TYR B 1 19 ? 13.256  -21.351 -25.282 1.00 33.45  ? 18  TYR B CA  1 
ATOM   889  C C   . TYR B 1 19 ? 12.948  -21.448 -26.765 1.00 29.62  ? 18  TYR B C   1 
ATOM   890  O O   . TYR B 1 19 ? 13.647  -22.140 -27.503 1.00 32.22  ? 18  TYR B O   1 
ATOM   891  C CB  . TYR B 1 19 ? 14.066  -20.061 -25.073 1.00 33.40  ? 18  TYR B CB  1 
ATOM   892  C CG  . TYR B 1 19 ? 14.447  -19.850 -23.618 1.00 35.16  ? 18  TYR B CG  1 
ATOM   893  C CD1 . TYR B 1 19 ? 13.569  -19.224 -22.740 1.00 36.26  ? 18  TYR B CD1 1 
ATOM   894  C CD2 . TYR B 1 19 ? 15.656  -20.337 -23.124 1.00 33.02  ? 18  TYR B CD2 1 
ATOM   895  C CE1 . TYR B 1 19 ? 13.892  -19.097 -21.402 1.00 33.80  ? 18  TYR B CE1 1 
ATOM   896  C CE2 . TYR B 1 19 ? 15.994  -20.188 -21.786 1.00 30.72  ? 18  TYR B CE2 1 
ATOM   897  C CZ  . TYR B 1 19 ? 15.116  -19.560 -20.935 1.00 34.27  ? 18  TYR B CZ  1 
ATOM   898  O OH  . TYR B 1 19 ? 15.492  -19.427 -19.627 1.00 41.29  ? 18  TYR B OH  1 
ATOM   899  N N   . PRO B 1 20 ? 11.944  -20.703 -27.257 1.00 25.83  ? 19  PRO B N   1 
ATOM   900  C CA  . PRO B 1 20 ? 11.694  -20.659 -28.696 1.00 24.65  ? 19  PRO B CA  1 
ATOM   901  C C   . PRO B 1 20 ? 12.853  -20.009 -29.459 1.00 25.86  ? 19  PRO B C   1 
ATOM   902  O O   . PRO B 1 20 ? 13.628  -19.204 -28.904 1.00 28.38  ? 19  PRO B O   1 
ATOM   903  C CB  . PRO B 1 20 ? 10.410  -19.847 -28.825 1.00 22.29  ? 19  PRO B CB  1 
ATOM   904  C CG  . PRO B 1 20 ? 10.293  -19.068 -27.529 1.00 22.41  ? 19  PRO B CG  1 
ATOM   905  C CD  . PRO B 1 20 ? 11.069  -19.828 -26.468 1.00 24.86  ? 19  PRO B CD  1 
ATOM   906  N N   . HIS B 1 21 ? 12.947  -20.329 -30.755 1.00 25.08  ? 20  HIS B N   1 
ATOM   907  C CA  . HIS B 1 21 ? 13.884  -19.633 -31.613 1.00 25.90  ? 20  HIS B CA  1 
ATOM   908  C C   . HIS B 1 21 ? 13.618  -18.153 -31.434 1.00 24.54  ? 20  HIS B C   1 
ATOM   909  O O   . HIS B 1 21 ? 12.497  -17.693 -31.608 1.00 28.56  ? 20  HIS B O   1 
ATOM   910  C CB  . HIS B 1 21 ? 13.640  -19.998 -33.078 1.00 25.32  ? 20  HIS B CB  1 
ATOM   911  C CG  . HIS B 1 21 ? 13.872  -21.458 -33.276 1.00 29.43  ? 20  HIS B CG  1 
ATOM   912  N ND1 . HIS B 1 21 ? 12.998  -22.417 -32.816 1.00 30.51  ? 20  HIS B ND1 1 
ATOM   913  C CD2 . HIS B 1 21 ? 14.899  -22.122 -33.800 1.00 28.95  ? 20  HIS B CD2 1 
ATOM   914  C CE1 . HIS B 1 21 ? 13.470  -23.618 -33.110 1.00 30.38  ? 20  HIS B CE1 1 
ATOM   915  N NE2 . HIS B 1 21 ? 14.627  -23.466 -33.694 1.00 28.60  ? 20  HIS B NE2 1 
ATOM   916  N N   . TRP B 1 22 ? 14.676  -17.422 -31.129 1.00 24.53  ? 21  TRP B N   1 
ATOM   917  C CA  . TRP B 1 22 ? 14.500  -16.097 -30.577 1.00 28.71  ? 21  TRP B CA  1 
ATOM   918  C C   . TRP B 1 22 ? 15.096  -15.081 -31.534 1.00 26.26  ? 21  TRP B C   1 
ATOM   919  O O   . TRP B 1 22 ? 16.202  -15.304 -32.003 1.00 29.11  ? 21  TRP B O   1 
ATOM   920  C CB  . TRP B 1 22 ? 15.178  -16.021 -29.200 1.00 25.04  ? 21  TRP B CB  1 
ATOM   921  C CG  . TRP B 1 22 ? 14.633  -14.890 -28.372 1.00 28.82  ? 21  TRP B CG  1 
ATOM   922  C CD1 . TRP B 1 22 ? 14.917  -13.567 -28.508 1.00 27.47  ? 21  TRP B CD1 1 
ATOM   923  C CD2 . TRP B 1 22 ? 13.675  -14.989 -27.289 1.00 28.74  ? 21  TRP B CD2 1 
ATOM   924  N NE1 . TRP B 1 22 ? 14.230  -12.844 -27.565 1.00 31.13  ? 21  TRP B NE1 1 
ATOM   925  C CE2 . TRP B 1 22 ? 13.453  -13.681 -26.812 1.00 28.49  ? 21  TRP B CE2 1 
ATOM   926  C CE3 . TRP B 1 22 ? 13.000  -16.050 -26.677 1.00 28.38  ? 21  TRP B CE3 1 
ATOM   927  C CZ2 . TRP B 1 22 ? 12.583  -13.399 -25.758 1.00 29.47  ? 21  TRP B CZ2 1 
ATOM   928  C CZ3 . TRP B 1 22 ? 12.149  -15.774 -25.629 1.00 30.21  ? 21  TRP B CZ3 1 
ATOM   929  C CH2 . TRP B 1 22 ? 11.911  -14.463 -25.209 1.00 28.72  ? 21  TRP B CH2 1 
ATOM   930  N N   . PRO B 1 23 ? 14.392  -13.962 -31.836 1.00 26.62  ? 22  PRO B N   1 
ATOM   931  C CA  . PRO B 1 23 ? 14.932  -12.908 -32.708 1.00 26.12  ? 22  PRO B CA  1 
ATOM   932  C C   . PRO B 1 23 ? 16.226  -12.314 -32.150 1.00 26.29  ? 22  PRO B C   1 
ATOM   933  O O   . PRO B 1 23 ? 16.312  -11.960 -30.978 1.00 26.51  ? 22  PRO B O   1 
ATOM   934  C CB  . PRO B 1 23 ? 13.769  -11.899 -32.876 1.00 24.87  ? 22  PRO B CB  1 
ATOM   935  C CG  . PRO B 1 23 ? 12.855  -12.200 -31.685 1.00 23.60  ? 22  PRO B CG  1 
ATOM   936  C CD  . PRO B 1 23 ? 13.012  -13.681 -31.401 1.00 23.88  ? 22  PRO B CD  1 
ATOM   937  N N   . ALA B 1 24 ? 17.285  -12.319 -32.972 1.00 22.88  ? 23  ALA B N   1 
ATOM   938  C CA  . ALA B 1 24 ? 18.620  -12.016 -32.489 1.00 24.77  ? 23  ALA B CA  1 
ATOM   939  C C   . ALA B 1 24 ? 19.452  -11.411 -33.631 1.00 30.52  ? 23  ALA B C   1 
ATOM   940  O O   . ALA B 1 24 ? 19.017  -11.430 -34.793 1.00 31.37  ? 23  ALA B O   1 
ATOM   941  C CB  . ALA B 1 24 ? 19.237  -13.262 -31.904 1.00 24.48  ? 23  ALA B CB  1 
ATOM   942  N N   . ARG B 1 25 ? 20.621  -10.844 -33.279 1.00 30.16  ? 24  ARG B N   1 
ATOM   943  C CA  . ARG B 1 25 ? 21.599  -10.398 -34.271 1.00 30.05  ? 24  ARG B CA  1 
ATOM   944  C C   . ARG B 1 25 ? 22.993  -10.903 -33.869 1.00 28.42  ? 24  ARG B C   1 
ATOM   945  O O   . ARG B 1 25 ? 23.299  -11.075 -32.673 1.00 26.98  ? 24  ARG B O   1 
ATOM   946  C CB  . ARG B 1 25 ? 21.486  -8.879  -34.470 1.00 27.61  ? 24  ARG B CB  1 
ATOM   947  C CG  . ARG B 1 25 ? 22.375  -8.098  -33.510 1.00 28.13  ? 24  ARG B CG  1 
ATOM   948  C CD  . ARG B 1 25 ? 21.994  -6.615  -33.457 1.00 29.58  ? 24  ARG B CD  1 
ATOM   949  N NE  . ARG B 1 25 ? 22.559  -5.955  -32.266 1.00 30.58  ? 24  ARG B NE  1 
ATOM   950  C CZ  . ARG B 1 25 ? 22.205  -4.733  -31.882 1.00 29.77  ? 24  ARG B CZ  1 
ATOM   951  N NH1 . ARG B 1 25 ? 21.272  -4.107  -32.571 1.00 26.17  ? 24  ARG B NH1 1 
ATOM   952  N NH2 . ARG B 1 25 ? 22.768  -4.156  -30.830 1.00 24.47  ? 24  ARG B NH2 1 
ATOM   953  N N   . ILE B 1 26 ? 23.853  -11.149 -34.871 1.00 30.15  ? 25  ILE B N   1 
ATOM   954  C CA  . ILE B 1 26 ? 25.273  -11.402 -34.644 1.00 28.78  ? 25  ILE B CA  1 
ATOM   955  C C   . ILE B 1 26 ? 25.865  -10.072 -34.196 1.00 33.43  ? 25  ILE B C   1 
ATOM   956  O O   . ILE B 1 26 ? 25.686  -9.062  -34.878 1.00 35.74  ? 25  ILE B O   1 
ATOM   957  C CB  . ILE B 1 26 ? 25.983  -11.905 -35.933 1.00 30.41  ? 25  ILE B CB  1 
ATOM   958  C CG1 . ILE B 1 26 ? 25.194  -12.997 -36.662 1.00 29.10  ? 25  ILE B CG1 1 
ATOM   959  C CG2 . ILE B 1 26 ? 27.447  -12.301 -35.662 1.00 27.50  ? 25  ILE B CG2 1 
ATOM   960  C CD1 . ILE B 1 26 ? 25.080  -14.320 -35.916 1.00 32.29  ? 25  ILE B CD1 1 
ATOM   961  N N   . ASP B 1 27 ? 26.562  -10.084 -33.051 1.00 40.20  ? 26  ASP B N   1 
ATOM   962  C CA  . ASP B 1 27 ? 27.252  -8.897  -32.558 1.00 44.50  ? 26  ASP B CA  1 
ATOM   963  C C   . ASP B 1 27 ? 28.736  -8.945  -32.943 1.00 45.35  ? 26  ASP B C   1 
ATOM   964  O O   . ASP B 1 27 ? 29.234  -10.010 -33.313 1.00 38.46  ? 26  ASP B O   1 
ATOM   965  C CB  . ASP B 1 27 ? 26.952  -8.665  -31.081 1.00 45.02  ? 26  ASP B CB  1 
ATOM   966  C CG  . ASP B 1 27 ? 25.820  -7.678  -30.826 1.00 42.62  ? 26  ASP B CG  1 
ATOM   967  O OD1 . ASP B 1 27 ? 25.174  -7.268  -31.803 1.00 37.66  ? 26  ASP B OD1 1 
ATOM   968  O OD2 . ASP B 1 27 ? 25.652  -7.265  -29.670 1.00 48.81  ? 26  ASP B OD2 1 
ATOM   969  N N   A ASP B 1 28 ? 29.398  -7.776  -32.826 0.50 51.63  ? 27  ASP B N   1 
ATOM   970  N N   B ASP B 1 28 ? 29.427  -7.799  -32.868 0.50 50.90  ? 27  ASP B N   1 
ATOM   971  C CA  A ASP B 1 28 ? 30.843  -7.573  -32.908 0.50 56.19  ? 27  ASP B CA  1 
ATOM   972  C CA  B ASP B 1 28 ? 30.877  -7.803  -33.013 0.50 54.75  ? 27  ASP B CA  1 
ATOM   973  C C   A ASP B 1 28 ? 31.487  -7.990  -31.584 0.50 57.89  ? 27  ASP B C   1 
ATOM   974  C C   B ASP B 1 28 ? 31.518  -7.929  -31.633 0.50 57.47  ? 27  ASP B C   1 
ATOM   975  O O   A ASP B 1 28 ? 30.835  -7.902  -30.543 0.50 57.04  ? 27  ASP B O   1 
ATOM   976  O O   B ASP B 1 28 ? 30.893  -7.596  -30.626 0.50 58.85  ? 27  ASP B O   1 
ATOM   977  C CB  A ASP B 1 28 ? 31.179  -6.099  -33.107 0.50 52.28  ? 27  ASP B CB  1 
ATOM   978  C CB  B ASP B 1 28 ? 31.407  -6.628  -33.819 0.50 49.28  ? 27  ASP B CB  1 
ATOM   979  C CG  A ASP B 1 28 ? 30.651  -5.421  -34.365 0.50 48.04  ? 27  ASP B CG  1 
ATOM   980  C CG  B ASP B 1 28 ? 32.740  -6.894  -34.507 0.50 45.56  ? 27  ASP B CG  1 
ATOM   981  O OD1 A ASP B 1 28 ? 31.479  -4.956  -35.178 0.50 47.44  ? 27  ASP B OD1 1 
ATOM   982  O OD1 B ASP B 1 28 ? 33.661  -7.397  -33.837 0.50 40.70  ? 27  ASP B OD1 1 
ATOM   983  O OD2 A ASP B 1 28 ? 29.418  -5.340  -34.522 0.50 50.01  ? 27  ASP B OD2 1 
ATOM   984  O OD2 B ASP B 1 28 ? 32.838  -6.609  -35.714 0.50 47.49  ? 27  ASP B OD2 1 
ATOM   985  N N   . ILE B 1 29 ? 32.765  -8.417  -31.618 1.00 57.12  ? 28  ILE B N   1 
ATOM   986  C CA  . ILE B 1 29 ? 33.476  -8.776  -30.393 1.00 61.45  ? 28  ILE B CA  1 
ATOM   987  C C   . ILE B 1 29 ? 34.317  -7.599  -29.881 1.00 68.24  ? 28  ILE B C   1 
ATOM   988  O O   . ILE B 1 29 ? 35.051  -6.992  -30.653 1.00 78.46  ? 28  ILE B O   1 
ATOM   989  C CB  . ILE B 1 29 ? 34.290  -10.075 -30.571 1.00 58.35  ? 28  ILE B CB  1 
ATOM   990  N N   . ALA B 1 30 ? 34.204  -7.300  -28.569 1.00 73.23  ? 29  ALA B N   1 
ATOM   991  C CA  . ALA B 1 30 ? 34.834  -6.185  -27.854 1.00 72.66  ? 29  ALA B CA  1 
ATOM   992  C C   . ALA B 1 30 ? 34.578  -4.844  -28.559 1.00 78.06  ? 29  ALA B C   1 
ATOM   993  O O   . ALA B 1 30 ? 33.471  -4.256  -28.390 1.00 66.68  ? 29  ALA B O   1 
ATOM   994  C CB  . ALA B 1 30 ? 36.313  -6.433  -27.598 1.00 62.55  ? 29  ALA B CB  1 
ATOM   995  N N   . VAL B 1 34 ? 34.580  -10.795 -23.545 1.00 55.33  ? 33  VAL B N   1 
ATOM   996  C CA  . VAL B 1 34 ? 35.057  -12.215 -23.598 1.00 63.24  ? 33  VAL B CA  1 
ATOM   997  C C   . VAL B 1 34 ? 34.896  -12.732 -25.028 1.00 73.68  ? 33  VAL B C   1 
ATOM   998  O O   . VAL B 1 34 ? 33.815  -12.606 -25.601 1.00 75.84  ? 33  VAL B O   1 
ATOM   999  C CB  . VAL B 1 34 ? 34.345  -13.126 -22.570 1.00 64.07  ? 33  VAL B CB  1 
ATOM   1000 C CG1 . VAL B 1 34 ? 32.992  -12.585 -22.124 1.00 65.16  ? 33  VAL B CG1 1 
ATOM   1001 C CG2 . VAL B 1 34 ? 34.209  -14.568 -23.048 1.00 60.47  ? 33  VAL B CG2 1 
ATOM   1002 N N   . LYS B 1 35 ? 35.965  -13.314 -25.592 1.00 72.93  ? 34  LYS B N   1 
ATOM   1003 C CA  . LYS B 1 35 ? 35.951  -13.772 -26.978 1.00 75.68  ? 34  LYS B CA  1 
ATOM   1004 C C   . LYS B 1 35 ? 35.121  -15.056 -27.103 1.00 77.29  ? 34  LYS B C   1 
ATOM   1005 O O   . LYS B 1 35 ? 35.006  -15.818 -26.137 1.00 71.09  ? 34  LYS B O   1 
ATOM   1006 C CB  . LYS B 1 35 ? 37.369  -13.896 -27.556 1.00 77.88  ? 34  LYS B CB  1 
ATOM   1007 N N   . PRO B 1 36 ? 34.468  -15.290 -28.275 1.00 74.57  ? 35  PRO B N   1 
ATOM   1008 C CA  . PRO B 1 36 ? 33.650  -16.492 -28.503 1.00 60.97  ? 35  PRO B CA  1 
ATOM   1009 C C   . PRO B 1 36 ? 34.338  -17.851 -28.345 1.00 57.98  ? 35  PRO B C   1 
ATOM   1010 O O   . PRO B 1 36 ? 35.476  -18.000 -28.773 1.00 57.36  ? 35  PRO B O   1 
ATOM   1011 C CB  . PRO B 1 36 ? 33.165  -16.278 -29.952 1.00 64.55  ? 35  PRO B CB  1 
ATOM   1012 C CG  . PRO B 1 36 ? 33.165  -14.778 -30.149 1.00 69.15  ? 35  PRO B CG  1 
ATOM   1013 C CD  . PRO B 1 36 ? 34.412  -14.343 -29.408 1.00 73.72  ? 35  PRO B CD  1 
ATOM   1014 N N   . PRO B 1 37 ? 33.682  -18.879 -27.736 1.00 56.43  ? 36  PRO B N   1 
ATOM   1015 C CA  . PRO B 1 37 ? 34.173  -20.265 -27.762 1.00 58.23  ? 36  PRO B CA  1 
ATOM   1016 C C   . PRO B 1 37 ? 34.269  -20.819 -29.183 1.00 64.67  ? 36  PRO B C   1 
ATOM   1017 O O   . PRO B 1 37 ? 33.509  -20.392 -30.054 1.00 61.64  ? 36  PRO B O   1 
ATOM   1018 C CB  . PRO B 1 37 ? 33.177  -21.101 -26.912 1.00 54.85  ? 36  PRO B CB  1 
ATOM   1019 C CG  . PRO B 1 37 ? 32.327  -20.077 -26.197 1.00 55.21  ? 36  PRO B CG  1 
ATOM   1020 C CD  . PRO B 1 37 ? 32.447  -18.752 -26.946 1.00 51.76  ? 36  PRO B CD  1 
ATOM   1021 N N   . PRO B 1 38 ? 35.168  -21.803 -29.452 1.00 70.87  ? 37  PRO B N   1 
ATOM   1022 C CA  . PRO B 1 38 ? 35.440  -22.276 -30.812 1.00 69.13  ? 37  PRO B CA  1 
ATOM   1023 C C   . PRO B 1 38 ? 34.689  -21.723 -32.033 1.00 68.33  ? 37  PRO B C   1 
ATOM   1024 O O   . PRO B 1 38 ? 35.059  -20.675 -32.566 1.00 73.64  ? 37  PRO B O   1 
ATOM   1025 C CB  . PRO B 1 38 ? 35.120  -23.728 -30.434 1.00 72.50  ? 37  PRO B CB  1 
ATOM   1026 C CG  . PRO B 1 38 ? 35.938  -23.940 -29.158 1.00 65.46  ? 37  PRO B CG  1 
ATOM   1027 C CD  . PRO B 1 38 ? 35.932  -22.587 -28.460 1.00 68.74  ? 37  PRO B CD  1 
ATOM   1028 N N   . ASN B 1 39 ? 33.645  -22.422 -32.493 1.00 63.44  ? 38  ASN B N   1 
ATOM   1029 C CA  . ASN B 1 39 ? 32.964  -22.044 -33.725 1.00 57.81  ? 38  ASN B CA  1 
ATOM   1030 C C   . ASN B 1 39 ? 31.729  -21.199 -33.424 1.00 52.89  ? 38  ASN B C   1 
ATOM   1031 O O   . ASN B 1 39 ? 30.808  -21.151 -34.233 1.00 55.96  ? 38  ASN B O   1 
ATOM   1032 C CB  . ASN B 1 39 ? 32.438  -23.264 -34.472 1.00 66.77  ? 38  ASN B CB  1 
ATOM   1033 C CG  . ASN B 1 39 ? 33.484  -24.339 -34.630 1.00 72.29  ? 38  ASN B CG  1 
ATOM   1034 O OD1 . ASN B 1 39 ? 33.257  -25.477 -34.201 1.00 66.52  ? 38  ASN B OD1 1 
ATOM   1035 N ND2 . ASN B 1 39 ? 34.617  -24.008 -35.242 1.00 67.66  ? 38  ASN B ND2 1 
ATOM   1036 N N   . LYS B 1 40 ? 31.720  -20.537 -32.264 1.00 49.67  ? 39  LYS B N   1 
ATOM   1037 C CA  . LYS B 1 40 ? 30.546  -19.835 -31.770 1.00 42.13  ? 39  LYS B CA  1 
ATOM   1038 C C   . LYS B 1 40 ? 30.660  -18.337 -32.092 1.00 42.06  ? 39  LYS B C   1 
ATOM   1039 O O   . LYS B 1 40 ? 31.759  -17.838 -32.386 1.00 40.11  ? 39  LYS B O   1 
ATOM   1040 C CB  . LYS B 1 40 ? 30.323  -20.295 -30.322 1.00 48.20  ? 39  LYS B CB  1 
ATOM   1041 C CG  . LYS B 1 40 ? 30.447  -21.808 -30.148 1.00 49.21  ? 39  LYS B CG  1 
ATOM   1042 C CD  . LYS B 1 40 ? 29.407  -22.509 -29.285 1.00 51.72  ? 39  LYS B CD  1 
ATOM   1043 C CE  . LYS B 1 40 ? 29.570  -22.308 -27.830 1.00 52.18  ? 39  LYS B CE  1 
ATOM   1044 N NZ  . LYS B 1 40 ? 28.448  -22.907 -27.097 1.00 54.56  ? 39  LYS B NZ  1 
ATOM   1045 N N   . TYR B 1 41 ? 29.504  -17.640 -32.091 1.00 36.71  ? 40  TYR B N   1 
ATOM   1046 C CA  . TYR B 1 41 ? 29.413  -16.206 -32.353 1.00 37.02  ? 40  TYR B CA  1 
ATOM   1047 C C   . TYR B 1 41 ? 28.802  -15.453 -31.171 1.00 40.94  ? 40  TYR B C   1 
ATOM   1048 O O   . TYR B 1 41 ? 27.977  -16.000 -30.448 1.00 42.61  ? 40  TYR B O   1 
ATOM   1049 C CB  . TYR B 1 41 ? 28.463  -15.949 -33.529 1.00 39.97  ? 40  TYR B CB  1 
ATOM   1050 C CG  . TYR B 1 41 ? 29.051  -16.338 -34.868 1.00 39.36  ? 40  TYR B CG  1 
ATOM   1051 C CD1 . TYR B 1 41 ? 29.693  -15.397 -35.662 1.00 44.34  ? 40  TYR B CD1 1 
ATOM   1052 C CD2 . TYR B 1 41 ? 28.952  -17.647 -35.336 1.00 48.12  ? 40  TYR B CD2 1 
ATOM   1053 C CE1 . TYR B 1 41 ? 30.234  -15.756 -36.891 1.00 52.70  ? 40  TYR B CE1 1 
ATOM   1054 C CE2 . TYR B 1 41 ? 29.490  -18.015 -36.563 1.00 52.22  ? 40  TYR B CE2 1 
ATOM   1055 C CZ  . TYR B 1 41 ? 30.140  -17.067 -37.336 1.00 53.67  ? 40  TYR B CZ  1 
ATOM   1056 O OH  . TYR B 1 41 ? 30.665  -17.432 -38.542 1.00 58.53  ? 40  TYR B OH  1 
ATOM   1057 N N   . PRO B 1 42 ? 29.096  -14.141 -31.006 1.00 41.67  ? 41  PRO B N   1 
ATOM   1058 C CA  . PRO B 1 42 ? 28.371  -13.310 -30.046 1.00 39.47  ? 41  PRO B CA  1 
ATOM   1059 C C   . PRO B 1 42 ? 26.959  -13.088 -30.577 1.00 36.14  ? 41  PRO B C   1 
ATOM   1060 O O   . PRO B 1 42 ? 26.765  -12.548 -31.655 1.00 41.64  ? 41  PRO B O   1 
ATOM   1061 C CB  . PRO B 1 42 ? 29.158  -11.984 -29.951 1.00 41.45  ? 41  PRO B CB  1 
ATOM   1062 C CG  . PRO B 1 42 ? 30.110  -11.989 -31.140 1.00 44.00  ? 41  PRO B CG  1 
ATOM   1063 C CD  . PRO B 1 42 ? 30.099  -13.380 -31.771 1.00 45.38  ? 41  PRO B CD  1 
ATOM   1064 N N   . ILE B 1 43 ? 25.955  -13.501 -29.801 1.00 35.82  ? 42  ILE B N   1 
ATOM   1065 C CA  . ILE B 1 43 ? 24.569  -13.274 -30.187 1.00 28.41  ? 42  ILE B CA  1 
ATOM   1066 C C   . ILE B 1 43 ? 23.979  -12.274 -29.208 1.00 30.90  ? 42  ILE B C   1 
ATOM   1067 O O   . ILE B 1 43 ? 24.172  -12.420 -27.996 1.00 30.56  ? 42  ILE B O   1 
ATOM   1068 C CB  . ILE B 1 43 ? 23.794  -14.599 -30.216 1.00 30.06  ? 42  ILE B CB  1 
ATOM   1069 C CG1 . ILE B 1 43 ? 24.536  -15.669 -31.019 1.00 28.27  ? 42  ILE B CG1 1 
ATOM   1070 C CG2 . ILE B 1 43 ? 22.359  -14.404 -30.714 1.00 29.88  ? 42  ILE B CG2 1 
ATOM   1071 C CD1 . ILE B 1 43 ? 24.846  -15.273 -32.466 1.00 27.95  ? 42  ILE B CD1 1 
ATOM   1072 N N   . PHE B 1 44 ? 23.358  -11.224 -29.763 1.00 29.04  ? 43  PHE B N   1 
ATOM   1073 C CA  . PHE B 1 44 ? 22.546  -10.276 -29.029 1.00 28.24  ? 43  PHE B CA  1 
ATOM   1074 C C   . PHE B 1 44 ? 21.085  -10.605 -29.336 1.00 32.73  ? 43  PHE B C   1 
ATOM   1075 O O   . PHE B 1 44 ? 20.686  -10.603 -30.510 1.00 32.54  ? 43  PHE B O   1 
ATOM   1076 C CB  . PHE B 1 44 ? 22.884  -8.824  -29.373 1.00 27.82  ? 43  PHE B CB  1 
ATOM   1077 C CG  . PHE B 1 44 ? 21.960  -7.820  -28.692 1.00 29.83  ? 43  PHE B CG  1 
ATOM   1078 C CD1 . PHE B 1 44 ? 20.734  -7.475  -29.252 1.00 31.28  ? 43  PHE B CD1 1 
ATOM   1079 C CD2 . PHE B 1 44 ? 22.302  -7.260  -27.462 1.00 36.83  ? 43  PHE B CD2 1 
ATOM   1080 C CE1 . PHE B 1 44 ? 19.893  -6.564  -28.631 1.00 35.35  ? 43  PHE B CE1 1 
ATOM   1081 C CE2 . PHE B 1 44 ? 21.462  -6.345  -26.836 1.00 34.58  ? 43  PHE B CE2 1 
ATOM   1082 C CZ  . PHE B 1 44 ? 20.263  -6.000  -27.421 1.00 33.73  ? 43  PHE B CZ  1 
ATOM   1083 N N   . PHE B 1 45 ? 20.310  -10.901 -28.262 1.00 31.59  ? 44  PHE B N   1 
ATOM   1084 C CA  . PHE B 1 45 ? 18.900  -11.263 -28.347 1.00 28.29  ? 44  PHE B CA  1 
ATOM   1085 C C   . PHE B 1 45 ? 18.002  -10.036 -28.228 1.00 29.53  ? 44  PHE B C   1 
ATOM   1086 O O   . PHE B 1 45 ? 17.980  -9.335  -27.224 1.00 32.84  ? 44  PHE B O   1 
ATOM   1087 C CB  . PHE B 1 45 ? 18.553  -12.246 -27.234 1.00 28.27  ? 44  PHE B CB  1 
ATOM   1088 C CG  . PHE B 1 45 ? 19.207  -13.592 -27.473 1.00 26.33  ? 44  PHE B CG  1 
ATOM   1089 C CD1 . PHE B 1 45 ? 20.521  -13.795 -27.130 1.00 25.02  ? 44  PHE B CD1 1 
ATOM   1090 C CD2 . PHE B 1 45 ? 18.508  -14.634 -28.065 1.00 28.64  ? 44  PHE B CD2 1 
ATOM   1091 C CE1 . PHE B 1 45 ? 21.119  -15.023 -27.354 1.00 29.56  ? 44  PHE B CE1 1 
ATOM   1092 C CE2 . PHE B 1 45 ? 19.107  -15.869 -28.258 1.00 26.17  ? 44  PHE B CE2 1 
ATOM   1093 C CZ  . PHE B 1 45 ? 20.411  -16.049 -27.933 1.00 24.58  ? 44  PHE B CZ  1 
ATOM   1094 N N   . PHE B 1 46 ? 17.193  -9.824  -29.240 1.00 26.99  ? 45  PHE B N   1 
ATOM   1095 C CA  . PHE B 1 46 ? 16.256  -8.721  -29.181 1.00 28.97  ? 45  PHE B CA  1 
ATOM   1096 C C   . PHE B 1 46 ? 15.287  -8.959  -28.017 1.00 29.81  ? 45  PHE B C   1 
ATOM   1097 O O   . PHE B 1 46 ? 15.072  -10.098 -27.603 1.00 24.79  ? 45  PHE B O   1 
ATOM   1098 C CB  . PHE B 1 46 ? 15.596  -8.553  -30.546 1.00 25.82  ? 45  PHE B CB  1 
ATOM   1099 C CG  . PHE B 1 46 ? 16.547  -8.025  -31.624 1.00 30.31  ? 45  PHE B CG  1 
ATOM   1100 C CD1 . PHE B 1 46 ? 17.111  -6.747  -31.540 1.00 30.21  ? 45  PHE B CD1 1 
ATOM   1101 C CD2 . PHE B 1 46 ? 16.884  -8.804  -32.723 1.00 27.31  ? 45  PHE B CD2 1 
ATOM   1102 C CE1 . PHE B 1 46 ? 17.968  -6.274  -32.538 1.00 28.63  ? 45  PHE B CE1 1 
ATOM   1103 C CE2 . PHE B 1 46 ? 17.755  -8.324  -33.688 1.00 30.02  ? 45  PHE B CE2 1 
ATOM   1104 C CZ  . PHE B 1 46 ? 18.275  -7.061  -33.606 1.00 25.73  ? 45  PHE B CZ  1 
ATOM   1105 N N   . GLY B 1 47 ? 14.671  -7.873  -27.530 1.00 28.39  ? 46  GLY B N   1 
ATOM   1106 C CA  . GLY B 1 47 ? 13.614  -7.980  -26.539 1.00 29.25  ? 46  GLY B CA  1 
ATOM   1107 C C   . GLY B 1 47 ? 14.239  -8.086  -25.160 1.00 28.63  ? 46  GLY B C   1 
ATOM   1108 O O   . GLY B 1 47 ? 14.068  -7.198  -24.343 1.00 31.75  ? 46  GLY B O   1 
ATOM   1109 N N   . THR B 1 48 ? 15.011  -9.148  -24.927 1.00 32.20  ? 47  THR B N   1 
ATOM   1110 C CA  . THR B 1 48 ? 15.614  -9.360  -23.622 1.00 26.98  ? 47  THR B CA  1 
ATOM   1111 C C   . THR B 1 48 ? 16.879  -8.524  -23.540 1.00 28.42  ? 47  THR B C   1 
ATOM   1112 O O   . THR B 1 48 ? 17.299  -8.151  -22.462 1.00 28.61  ? 47  THR B O   1 
ATOM   1113 C CB  . THR B 1 48 ? 15.928  -10.844 -23.427 1.00 27.91  ? 47  THR B CB  1 
ATOM   1114 O OG1 . THR B 1 48 ? 16.990  -11.168 -24.326 1.00 28.54  ? 47  THR B OG1 1 
ATOM   1115 C CG2 . THR B 1 48 ? 14.701  -11.727 -23.612 1.00 28.11  ? 47  THR B CG2 1 
ATOM   1116 N N   . HIS B 1 49 ? 17.541  -8.324  -24.687 1.00 29.26  ? 48  HIS B N   1 
ATOM   1117 C CA  . HIS B 1 49 ? 18.820  -7.640  -24.751 1.00 28.41  ? 48  HIS B CA  1 
ATOM   1118 C C   . HIS B 1 49 ? 19.888  -8.397  -23.982 1.00 28.78  ? 48  HIS B C   1 
ATOM   1119 O O   . HIS B 1 49 ? 20.892  -7.812  -23.621 1.00 33.12  ? 48  HIS B O   1 
ATOM   1120 C CB  . HIS B 1 49 ? 18.744  -6.197  -24.247 1.00 30.02  ? 48  HIS B CB  1 
ATOM   1121 C CG  . HIS B 1 49 ? 17.643  -5.491  -24.916 1.00 31.24  ? 48  HIS B CG  1 
ATOM   1122 N ND1 . HIS B 1 49 ? 16.861  -4.563  -24.270 1.00 30.56  ? 48  HIS B ND1 1 
ATOM   1123 C CD2 . HIS B 1 49 ? 17.153  -5.627  -26.169 1.00 29.77  ? 48  HIS B CD2 1 
ATOM   1124 C CE1 . HIS B 1 49 ? 15.935  -4.140  -25.120 1.00 35.84  ? 48  HIS B CE1 1 
ATOM   1125 N NE2 . HIS B 1 49 ? 16.109  -4.762  -26.285 1.00 33.89  ? 48  HIS B NE2 1 
ATOM   1126 N N   . GLU B 1 50 ? 19.703  -9.705  -23.815 1.00 31.46  ? 49  GLU B N   1 
ATOM   1127 C CA  . GLU B 1 50 ? 20.772  -10.545 -23.317 1.00 27.66  ? 49  GLU B CA  1 
ATOM   1128 C C   . GLU B 1 50 ? 21.707  -10.945 -24.453 1.00 31.34  ? 49  GLU B C   1 
ATOM   1129 O O   . GLU B 1 50 ? 21.455  -10.637 -25.615 1.00 30.07  ? 49  GLU B O   1 
ATOM   1130 C CB  . GLU B 1 50 ? 20.103  -11.730 -22.625 1.00 37.21  ? 49  GLU B CB  1 
ATOM   1131 C CG  . GLU B 1 50 ? 19.639  -11.349 -21.224 1.00 39.02  ? 49  GLU B CG  1 
ATOM   1132 C CD  . GLU B 1 50 ? 19.234  -12.547 -20.383 1.00 48.71  ? 49  GLU B CD  1 
ATOM   1133 O OE1 . GLU B 1 50 ? 19.900  -13.604 -20.457 1.00 43.89  ? 49  GLU B OE1 1 
ATOM   1134 O OE2 . GLU B 1 50 ? 18.261  -12.420 -19.607 1.00 54.76  ? 49  GLU B OE2 1 
ATOM   1135 N N   . THR B 1 51 ? 22.820  -11.599 -24.095 1.00 35.18  ? 50  THR B N   1 
ATOM   1136 C CA  . THR B 1 51 ? 23.841  -12.044 -25.037 1.00 36.73  ? 50  THR B CA  1 
ATOM   1137 C C   . THR B 1 51 ? 24.209  -13.470 -24.658 1.00 33.26  ? 50  THR B C   1 
ATOM   1138 O O   . THR B 1 51 ? 24.125  -13.828 -23.493 1.00 39.50  ? 50  THR B O   1 
ATOM   1139 C CB  . THR B 1 51 ? 25.082  -11.139 -24.999 1.00 34.39  ? 50  THR B CB  1 
ATOM   1140 O OG1 . THR B 1 51 ? 25.670  -11.259 -23.702 1.00 36.78  ? 50  THR B OG1 1 
ATOM   1141 C CG2 . THR B 1 51 ? 24.761  -9.675  -25.248 1.00 34.10  ? 50  THR B CG2 1 
ATOM   1142 N N   . ALA B 1 52 ? 24.594  -14.269 -25.644 1.00 28.08  ? 51  ALA B N   1 
ATOM   1143 C CA  . ALA B 1 52 ? 25.170  -15.585 -25.404 1.00 29.82  ? 51  ALA B CA  1 
ATOM   1144 C C   . ALA B 1 52 ? 26.070  -15.947 -26.586 1.00 30.21  ? 51  ALA B C   1 
ATOM   1145 O O   . ALA B 1 52 ? 26.159  -15.189 -27.547 1.00 32.98  ? 51  ALA B O   1 
ATOM   1146 C CB  . ALA B 1 52 ? 24.078  -16.594 -25.146 1.00 28.06  ? 51  ALA B CB  1 
ATOM   1147 N N   . PHE B 1 53 ? 26.745  -17.093 -26.518 1.00 36.02  ? 52  PHE B N   1 
ATOM   1148 C CA  . PHE B 1 53 ? 27.577  -17.571 -27.618 1.00 34.26  ? 52  PHE B CA  1 
ATOM   1149 C C   . PHE B 1 53 ? 26.914  -18.802 -28.229 1.00 40.10  ? 52  PHE B C   1 
ATOM   1150 O O   . PHE B 1 53 ? 26.508  -19.707 -27.491 1.00 35.25  ? 52  PHE B O   1 
ATOM   1151 C CB  . PHE B 1 53 ? 29.011  -17.892 -27.165 1.00 38.01  ? 52  PHE B CB  1 
ATOM   1152 C CG  . PHE B 1 53 ? 29.827  -16.711 -26.647 1.00 39.52  ? 52  PHE B CG  1 
ATOM   1153 C CD1 . PHE B 1 53 ? 30.008  -15.570 -27.428 1.00 38.32  ? 52  PHE B CD1 1 
ATOM   1154 C CD2 . PHE B 1 53 ? 30.361  -16.723 -25.357 1.00 39.46  ? 52  PHE B CD2 1 
ATOM   1155 C CE1 . PHE B 1 53 ? 30.745  -14.494 -26.954 1.00 39.61  ? 52  PHE B CE1 1 
ATOM   1156 C CE2 . PHE B 1 53 ? 31.095  -15.643 -24.884 1.00 42.56  ? 52  PHE B CE2 1 
ATOM   1157 C CZ  . PHE B 1 53 ? 31.289  -14.532 -25.679 1.00 40.85  ? 52  PHE B CZ  1 
ATOM   1158 N N   . LEU B 1 54 ? 26.754  -18.795 -29.572 1.00 35.95  ? 53  LEU B N   1 
ATOM   1159 C CA  . LEU B 1 54 ? 26.035  -19.855 -30.262 1.00 34.15  ? 53  LEU B CA  1 
ATOM   1160 C C   . LEU B 1 54 ? 26.776  -20.183 -31.557 1.00 35.20  ? 53  LEU B C   1 
ATOM   1161 O O   . LEU B 1 54 ? 27.285  -19.275 -32.220 1.00 30.80  ? 53  LEU B O   1 
ATOM   1162 C CB  . LEU B 1 54 ? 24.589  -19.451 -30.544 1.00 32.54  ? 53  LEU B CB  1 
ATOM   1163 C CG  . LEU B 1 54 ? 23.613  -19.475 -29.360 1.00 27.53  ? 53  LEU B CG  1 
ATOM   1164 C CD1 . LEU B 1 54 ? 22.241  -19.175 -29.917 1.00 30.01  ? 53  LEU B CD1 1 
ATOM   1165 C CD2 . LEU B 1 54 ? 23.561  -20.809 -28.708 1.00 26.07  ? 53  LEU B CD2 1 
ATOM   1166 N N   . GLY B 1 55 ? 26.827  -21.486 -31.886 1.00 31.79  ? 54  GLY B N   1 
ATOM   1167 C CA  . GLY B 1 55 ? 27.429  -21.931 -33.128 1.00 30.41  ? 54  GLY B CA  1 
ATOM   1168 C C   . GLY B 1 55 ? 26.384  -21.895 -34.223 1.00 32.59  ? 54  GLY B C   1 
ATOM   1169 O O   . GLY B 1 55 ? 25.202  -21.737 -33.945 1.00 33.63  ? 54  GLY B O   1 
ATOM   1170 N N   . PRO B 1 56 ? 26.773  -21.988 -35.512 1.00 31.63  ? 55  PRO B N   1 
ATOM   1171 C CA  . PRO B 1 56 ? 25.784  -21.965 -36.581 1.00 29.03  ? 55  PRO B CA  1 
ATOM   1172 C C   . PRO B 1 56 ? 24.550  -22.856 -36.478 1.00 32.15  ? 55  PRO B C   1 
ATOM   1173 O O   . PRO B 1 56 ? 23.516  -22.483 -37.027 1.00 38.95  ? 55  PRO B O   1 
ATOM   1174 C CB  . PRO B 1 56 ? 26.633  -22.316 -37.807 1.00 27.10  ? 55  PRO B CB  1 
ATOM   1175 C CG  . PRO B 1 56 ? 27.973  -21.729 -37.460 1.00 28.46  ? 55  PRO B CG  1 
ATOM   1176 C CD  . PRO B 1 56 ? 28.162  -22.094 -35.992 1.00 30.13  ? 55  PRO B CD  1 
ATOM   1177 N N   . LYS B 1 57 ? 24.655  -24.035 -35.840 1.00 31.12  ? 56  LYS B N   1 
ATOM   1178 C CA  . LYS B 1 57 ? 23.544  -24.992 -35.838 1.00 32.16  ? 56  LYS B CA  1 
ATOM   1179 C C   . LYS B 1 57 ? 22.305  -24.385 -35.167 1.00 31.78  ? 56  LYS B C   1 
ATOM   1180 O O   . LYS B 1 57 ? 21.166  -24.758 -35.485 1.00 26.76  ? 56  LYS B O   1 
ATOM   1181 C CB  . LYS B 1 57 ? 23.895  -26.336 -35.190 1.00 33.05  ? 56  LYS B CB  1 
ATOM   1182 C CG  . LYS B 1 57 ? 23.930  -26.324 -33.663 1.00 36.32  ? 56  LYS B CG  1 
ATOM   1183 C CD  . LYS B 1 57 ? 24.258  -27.630 -32.942 1.00 39.75  ? 56  LYS B CD  1 
ATOM   1184 C CE  . LYS B 1 57 ? 24.536  -27.483 -31.472 1.00 40.15  ? 56  LYS B CE  1 
ATOM   1185 N NZ  . LYS B 1 57 ? 23.279  -27.297 -30.741 1.00 43.27  ? 56  LYS B NZ  1 
ATOM   1186 N N   . ASP B 1 58 ? 22.546  -23.401 -34.291 1.00 29.74  ? 57  ASP B N   1 
ATOM   1187 C CA  . ASP B 1 58 ? 21.489  -22.766 -33.524 1.00 32.19  ? 57  ASP B CA  1 
ATOM   1188 C C   . ASP B 1 58 ? 21.139  -21.408 -34.105 1.00 31.01  ? 57  ASP B C   1 
ATOM   1189 O O   . ASP B 1 58 ? 20.422  -20.647 -33.468 1.00 29.79  ? 57  ASP B O   1 
ATOM   1190 C CB  . ASP B 1 58 ? 21.864  -22.648 -32.053 1.00 31.82  ? 57  ASP B CB  1 
ATOM   1191 C CG  . ASP B 1 58 ? 21.992  -24.007 -31.390 1.00 34.08  ? 57  ASP B CG  1 
ATOM   1192 O OD1 . ASP B 1 58 ? 21.077  -24.811 -31.594 1.00 39.86  ? 57  ASP B OD1 1 
ATOM   1193 O OD2 . ASP B 1 58 ? 23.001  -24.255 -30.710 1.00 35.03  ? 57  ASP B OD2 1 
ATOM   1194 N N   . LEU B 1 59 ? 21.594  -21.143 -35.334 1.00 30.10  ? 58  LEU B N   1 
ATOM   1195 C CA  . LEU B 1 59 ? 21.462  -19.817 -35.902 1.00 28.95  ? 58  LEU B CA  1 
ATOM   1196 C C   . LEU B 1 59 ? 20.740  -19.942 -37.238 1.00 30.47  ? 58  LEU B C   1 
ATOM   1197 O O   . LEU B 1 59 ? 21.254  -20.540 -38.177 1.00 28.36  ? 58  LEU B O   1 
ATOM   1198 C CB  . LEU B 1 59 ? 22.834  -19.125 -36.032 1.00 27.30  ? 58  LEU B CB  1 
ATOM   1199 C CG  . LEU B 1 59 ? 23.620  -18.842 -34.740 1.00 25.89  ? 58  LEU B CG  1 
ATOM   1200 C CD1 . LEU B 1 59 ? 24.998  -18.249 -35.011 1.00 24.89  ? 58  LEU B CD1 1 
ATOM   1201 C CD2 . LEU B 1 59 ? 22.891  -17.954 -33.747 1.00 23.54  ? 58  LEU B CD2 1 
ATOM   1202 N N   . PHE B 1 60 ? 19.579  -19.302 -37.317 1.00 29.32  ? 59  PHE B N   1 
ATOM   1203 C CA  . PHE B 1 60 ? 18.707  -19.413 -38.461 1.00 29.89  ? 59  PHE B CA  1 
ATOM   1204 C C   . PHE B 1 60 ? 18.569  -18.044 -39.105 1.00 30.35  ? 59  PHE B C   1 
ATOM   1205 O O   . PHE B 1 60 ? 17.902  -17.191 -38.543 1.00 28.08  ? 59  PHE B O   1 
ATOM   1206 C CB  . PHE B 1 60 ? 17.351  -19.955 -38.009 1.00 29.30  ? 59  PHE B CB  1 
ATOM   1207 C CG  . PHE B 1 60 ? 17.400  -21.332 -37.357 1.00 27.46  ? 59  PHE B CG  1 
ATOM   1208 C CD1 . PHE B 1 60 ? 17.841  -21.485 -36.037 1.00 24.44  ? 59  PHE B CD1 1 
ATOM   1209 C CD2 . PHE B 1 60 ? 16.962  -22.457 -38.052 1.00 25.66  ? 59  PHE B CD2 1 
ATOM   1210 C CE1 . PHE B 1 60 ? 17.894  -22.740 -35.452 1.00 25.12  ? 59  PHE B CE1 1 
ATOM   1211 C CE2 . PHE B 1 60 ? 17.020  -23.709 -37.457 1.00 25.54  ? 59  PHE B CE2 1 
ATOM   1212 C CZ  . PHE B 1 60 ? 17.441  -23.841 -36.133 1.00 23.86  ? 59  PHE B CZ  1 
ATOM   1213 N N   . PRO B 1 61 ? 19.200  -17.798 -40.287 1.00 29.92  ? 60  PRO B N   1 
ATOM   1214 C CA  . PRO B 1 61 ? 18.942  -16.600 -41.084 1.00 31.14  ? 60  PRO B CA  1 
ATOM   1215 C C   . PRO B 1 61 ? 17.498  -16.137 -41.020 1.00 32.24  ? 60  PRO B C   1 
ATOM   1216 O O   . PRO B 1 61 ? 16.588  -16.916 -41.320 1.00 36.27  ? 60  PRO B O   1 
ATOM   1217 C CB  . PRO B 1 61 ? 19.369  -17.034 -42.502 1.00 30.04  ? 60  PRO B CB  1 
ATOM   1218 C CG  . PRO B 1 61 ? 20.530  -17.933 -42.229 1.00 28.19  ? 60  PRO B CG  1 
ATOM   1219 C CD  . PRO B 1 61 ? 20.263  -18.620 -40.891 1.00 29.37  ? 60  PRO B CD  1 
ATOM   1220 N N   . TYR B 1 62 ? 17.326  -14.868 -40.622 1.00 29.99  ? 61  TYR B N   1 
ATOM   1221 C CA  . TYR B 1 62 ? 16.027  -14.295 -40.314 1.00 31.37  ? 61  TYR B CA  1 
ATOM   1222 C C   . TYR B 1 62 ? 15.069  -14.395 -41.492 1.00 37.41  ? 61  TYR B C   1 
ATOM   1223 O O   . TYR B 1 62 ? 13.917  -14.789 -41.310 1.00 36.06  ? 61  TYR B O   1 
ATOM   1224 C CB  . TYR B 1 62 ? 16.181  -12.832 -39.912 1.00 32.98  ? 61  TYR B CB  1 
ATOM   1225 C CG  . TYR B 1 62 ? 14.854  -12.129 -39.638 1.00 37.29  ? 61  TYR B CG  1 
ATOM   1226 C CD1 . TYR B 1 62 ? 14.208  -12.248 -38.413 1.00 33.08  ? 61  TYR B CD1 1 
ATOM   1227 C CD2 . TYR B 1 62 ? 14.259  -11.337 -40.606 1.00 38.44  ? 61  TYR B CD2 1 
ATOM   1228 C CE1 . TYR B 1 62 ? 13.020  -11.586 -38.154 1.00 34.62  ? 61  TYR B CE1 1 
ATOM   1229 C CE2 . TYR B 1 62 ? 13.066  -10.680 -40.365 1.00 40.62  ? 61  TYR B CE2 1 
ATOM   1230 C CZ  . TYR B 1 62 ? 12.453  -10.800 -39.132 1.00 35.69  ? 61  TYR B CZ  1 
ATOM   1231 O OH  . TYR B 1 62 ? 11.286  -10.138 -38.927 1.00 36.38  ? 61  TYR B OH  1 
ATOM   1232 N N   . ASP B 1 63 ? 15.531  -13.990 -42.688 1.00 40.85  ? 62  ASP B N   1 
ATOM   1233 C CA  . ASP B 1 63 ? 14.629  -13.867 -43.830 1.00 45.15  ? 62  ASP B CA  1 
ATOM   1234 C C   . ASP B 1 63 ? 14.142  -15.243 -44.247 1.00 40.33  ? 62  ASP B C   1 
ATOM   1235 O O   . ASP B 1 63 ? 12.949  -15.412 -44.456 1.00 47.09  ? 62  ASP B O   1 
ATOM   1236 C CB  . ASP B 1 63 ? 15.174  -13.032 -44.975 1.00 52.47  ? 62  ASP B CB  1 
ATOM   1237 C CG  . ASP B 1 63 ? 15.298  -11.547 -44.661 1.00 68.71  ? 62  ASP B CG  1 
ATOM   1238 O OD1 . ASP B 1 63 ? 14.301  -10.954 -44.152 1.00 65.65  ? 62  ASP B OD1 1 
ATOM   1239 O OD2 . ASP B 1 63 ? 16.393  -10.992 -44.929 1.00 76.72  ? 62  ASP B OD2 1 
ATOM   1240 N N   . LYS B 1 64 ? 15.061  -16.223 -44.285 1.00 38.11  ? 63  LYS B N   1 
ATOM   1241 C CA  . LYS B 1 64 ? 14.682  -17.611 -44.527 1.00 35.63  ? 63  LYS B CA  1 
ATOM   1242 C C   . LYS B 1 64 ? 13.592  -18.107 -43.555 1.00 40.11  ? 63  LYS B C   1 
ATOM   1243 O O   . LYS B 1 64 ? 12.644  -18.776 -43.980 1.00 41.15  ? 63  LYS B O   1 
ATOM   1244 C CB  . LYS B 1 64 ? 15.933  -18.487 -44.604 1.00 35.22  ? 63  LYS B CB  1 
ATOM   1245 C CG  . LYS B 1 64 ? 15.578  -19.947 -44.766 1.00 36.28  ? 63  LYS B CG  1 
ATOM   1246 C CD  . LYS B 1 64 ? 16.715  -20.839 -45.203 1.00 34.54  ? 63  LYS B CD  1 
ATOM   1247 C CE  . LYS B 1 64 ? 16.126  -21.900 -46.068 1.00 47.08  ? 63  LYS B CE  1 
ATOM   1248 N NZ  . LYS B 1 64 ? 15.081  -22.658 -45.380 1.00 48.63  ? 63  LYS B NZ  1 
ATOM   1249 N N   . SER B 1 65 ? 13.710  -17.784 -42.253 1.00 35.64  ? 64  SER B N   1 
ATOM   1250 C CA  . SER B 1 65 ? 12.929  -18.495 -41.254 1.00 37.34  ? 64  SER B CA  1 
ATOM   1251 C C   . SER B 1 65 ? 11.959  -17.619 -40.461 1.00 33.97  ? 64  SER B C   1 
ATOM   1252 O O   . SER B 1 65 ? 11.434  -18.083 -39.455 1.00 33.55  ? 64  SER B O   1 
ATOM   1253 C CB  . SER B 1 65 ? 13.823  -19.309 -40.353 1.00 35.21  ? 64  SER B CB  1 
ATOM   1254 O OG  . SER B 1 65 ? 14.782  -18.472 -39.735 1.00 39.92  ? 64  SER B OG  1 
ATOM   1255 N N   . LYS B 1 66 ? 11.665  -16.399 -40.935 1.00 38.95  ? 65  LYS B N   1 
ATOM   1256 C CA  . LYS B 1 66 ? 10.827  -15.462 -40.197 1.00 40.41  ? 65  LYS B CA  1 
ATOM   1257 C C   . LYS B 1 66 ? 9.369   -15.913 -40.185 1.00 43.12  ? 65  LYS B C   1 
ATOM   1258 O O   . LYS B 1 66 ? 8.642   -15.644 -39.221 1.00 43.07  ? 65  LYS B O   1 
ATOM   1259 C CB  . LYS B 1 66 ? 10.992  -13.997 -40.618 1.00 42.16  ? 65  LYS B CB  1 
ATOM   1260 C CG  . LYS B 1 66 ? 10.866  -13.664 -42.088 1.00 45.95  ? 65  LYS B CG  1 
ATOM   1261 C CD  . LYS B 1 66 ? 10.941  -12.168 -42.372 1.00 53.40  ? 65  LYS B CD  1 
ATOM   1262 C CE  . LYS B 1 66 ? 10.848  -11.828 -43.829 1.00 53.43  ? 65  LYS B CE  1 
ATOM   1263 N NZ  . LYS B 1 66 ? 9.610   -12.381 -44.379 1.00 59.31  ? 65  LYS B NZ  1 
ATOM   1264 N N   . ASP B 1 67 ? 8.951   -16.667 -41.207 1.00 47.95  ? 66  ASP B N   1 
ATOM   1265 C CA  . ASP B 1 67 ? 7.565   -17.133 -41.251 1.00 51.77  ? 66  ASP B CA  1 
ATOM   1266 C C   . ASP B 1 67 ? 7.335   -18.310 -40.296 1.00 49.65  ? 66  ASP B C   1 
ATOM   1267 O O   . ASP B 1 67 ? 6.248   -18.447 -39.740 1.00 57.66  ? 66  ASP B O   1 
ATOM   1268 C CB  . ASP B 1 67 ? 6.988   -17.193 -42.663 1.00 63.48  ? 66  ASP B CB  1 
ATOM   1269 C CG  . ASP B 1 67 ? 7.481   -18.299 -43.587 1.00 73.37  ? 66  ASP B CG  1 
ATOM   1270 O OD1 . ASP B 1 67 ? 7.243   -18.178 -44.820 1.00 80.78  ? 66  ASP B OD1 1 
ATOM   1271 O OD2 . ASP B 1 67 ? 8.065   -19.284 -43.075 1.00 67.95  ? 66  ASP B OD2 1 
ATOM   1272 N N   . LYS B 1 68 ? 8.380   -19.113 -40.049 1.00 42.83  ? 67  LYS B N   1 
ATOM   1273 C CA  . LYS B 1 68 ? 8.335   -20.233 -39.127 1.00 36.30  ? 67  LYS B CA  1 
ATOM   1274 C C   . LYS B 1 68 ? 8.470   -19.757 -37.681 1.00 36.22  ? 67  LYS B C   1 
ATOM   1275 O O   . LYS B 1 68 ? 7.730   -20.191 -36.808 1.00 38.81  ? 67  LYS B O   1 
ATOM   1276 C CB  . LYS B 1 68 ? 9.552   -21.066 -39.519 1.00 42.83  ? 67  LYS B CB  1 
ATOM   1277 C CG  . LYS B 1 68 ? 9.532   -22.532 -39.167 1.00 51.41  ? 67  LYS B CG  1 
ATOM   1278 C CD  . LYS B 1 68 ? 10.457  -23.324 -40.089 1.00 58.97  ? 67  LYS B CD  1 
ATOM   1279 C CE  . LYS B 1 68 ? 10.500  -24.752 -39.691 1.00 63.46  ? 67  LYS B CE  1 
ATOM   1280 N NZ  . LYS B 1 68 ? 9.149   -25.301 -39.553 1.00 66.88  ? 67  LYS B NZ  1 
ATOM   1281 N N   . TYR B 1 69 ? 9.385   -18.820 -37.423 1.00 33.84  ? 68  TYR B N   1 
ATOM   1282 C CA  . TYR B 1 69 ? 9.767   -18.540 -36.042 1.00 33.04  ? 68  TYR B CA  1 
ATOM   1283 C C   . TYR B 1 69 ? 9.223   -17.199 -35.544 1.00 31.30  ? 68  TYR B C   1 
ATOM   1284 O O   . TYR B 1 69 ? 9.312   -16.902 -34.358 1.00 32.78  ? 68  TYR B O   1 
ATOM   1285 C CB  . TYR B 1 69 ? 11.284  -18.692 -35.875 1.00 31.45  ? 68  TYR B CB  1 
ATOM   1286 C CG  . TYR B 1 69 ? 11.820  -20.085 -36.167 1.00 30.79  ? 68  TYR B CG  1 
ATOM   1287 C CD1 . TYR B 1 69 ? 11.191  -21.223 -35.645 1.00 36.27  ? 68  TYR B CD1 1 
ATOM   1288 C CD2 . TYR B 1 69 ? 12.937  -20.264 -36.977 1.00 30.55  ? 68  TYR B CD2 1 
ATOM   1289 C CE1 . TYR B 1 69 ? 11.678  -22.503 -35.872 1.00 32.75  ? 68  TYR B CE1 1 
ATOM   1290 C CE2 . TYR B 1 69 ? 13.429  -21.539 -37.220 1.00 34.01  ? 68  TYR B CE2 1 
ATOM   1291 C CZ  . TYR B 1 69 ? 12.806  -22.650 -36.663 1.00 35.74  ? 68  TYR B CZ  1 
ATOM   1292 O OH  . TYR B 1 69 ? 13.279  -23.897 -36.926 1.00 39.56  ? 68  TYR B OH  1 
ATOM   1293 N N   . GLY B 1 70 ? 8.689   -16.381 -36.444 1.00 32.46  ? 69  GLY B N   1 
ATOM   1294 C CA  . GLY B 1 70 ? 8.337   -15.022 -36.088 1.00 40.45  ? 69  GLY B CA  1 
ATOM   1295 C C   . GLY B 1 70 ? 6.935   -14.917 -35.486 1.00 40.31  ? 69  GLY B C   1 
ATOM   1296 O O   . GLY B 1 70 ? 6.303   -13.874 -35.622 1.00 42.42  ? 69  GLY B O   1 
ATOM   1297 N N   . LYS B 1 71 ? 6.465   -15.981 -34.823 1.00 34.96  ? 70  LYS B N   1 
ATOM   1298 C CA  . LYS B 1 71 ? 5.133   -15.986 -34.259 1.00 36.63  ? 70  LYS B CA  1 
ATOM   1299 C C   . LYS B 1 71 ? 5.221   -15.388 -32.854 1.00 37.72  ? 70  LYS B C   1 
ATOM   1300 O O   . LYS B 1 71 ? 6.077   -15.790 -32.068 1.00 37.07  ? 70  LYS B O   1 
ATOM   1301 C CB  . LYS B 1 71 ? 4.607   -17.425 -34.142 1.00 42.68  ? 70  LYS B CB  1 
ATOM   1302 C CG  . LYS B 1 71 ? 3.762   -18.036 -35.260 1.00 47.48  ? 70  LYS B CG  1 
ATOM   1303 C CD  . LYS B 1 71 ? 4.394   -18.054 -36.648 1.00 51.43  ? 70  LYS B CD  1 
ATOM   1304 C CE  . LYS B 1 71 ? 3.470   -18.684 -37.649 1.00 56.97  ? 70  LYS B CE  1 
ATOM   1305 N NZ  . LYS B 1 71 ? 3.601   -18.093 -38.985 1.00 56.51  ? 70  LYS B NZ  1 
ATOM   1306 N N   . PRO B 1 72 ? 4.377   -14.388 -32.507 1.00 40.14  ? 71  PRO B N   1 
ATOM   1307 C CA  . PRO B 1 72 ? 4.266   -13.899 -31.124 1.00 36.34  ? 71  PRO B CA  1 
ATOM   1308 C C   . PRO B 1 72 ? 4.004   -15.044 -30.155 1.00 33.94  ? 71  PRO B C   1 
ATOM   1309 O O   . PRO B 1 72 ? 3.315   -15.995 -30.497 1.00 33.44  ? 71  PRO B O   1 
ATOM   1310 C CB  . PRO B 1 72 ? 3.094   -12.874 -31.104 1.00 38.44  ? 71  PRO B CB  1 
ATOM   1311 C CG  . PRO B 1 72 ? 2.521   -12.908 -32.515 1.00 41.96  ? 71  PRO B CG  1 
ATOM   1312 C CD  . PRO B 1 72 ? 3.491   -13.666 -33.439 1.00 41.32  ? 71  PRO B CD  1 
ATOM   1313 N N   . ASN B 1 73 ? 4.565   -14.942 -28.942 1.00 32.63  ? 72  ASN B N   1 
ATOM   1314 C CA  . ASN B 1 73 ? 4.322   -15.926 -27.898 1.00 32.65  ? 72  ASN B CA  1 
ATOM   1315 C C   . ASN B 1 73 ? 4.280   -15.239 -26.523 1.00 34.27  ? 72  ASN B C   1 
ATOM   1316 O O   . ASN B 1 73 ? 4.370   -14.012 -26.421 1.00 35.86  ? 72  ASN B O   1 
ATOM   1317 C CB  . ASN B 1 73 ? 5.269   -17.109 -28.036 1.00 31.18  ? 72  ASN B CB  1 
ATOM   1318 C CG  . ASN B 1 73 ? 6.705   -16.726 -27.762 1.00 33.03  ? 72  ASN B CG  1 
ATOM   1319 O OD1 . ASN B 1 73 ? 6.982   -15.987 -26.814 1.00 35.85  ? 72  ASN B OD1 1 
ATOM   1320 N ND2 . ASN B 1 73 ? 7.645   -17.246 -28.536 1.00 39.37  ? 72  ASN B ND2 1 
ATOM   1321 N N   . LYS B 1 74 ? 4.192   -16.030 -25.452 1.00 35.08  ? 73  LYS B N   1 
ATOM   1322 C CA  . LYS B 1 74 ? 3.923   -15.454 -24.138 1.00 35.04  ? 73  LYS B CA  1 
ATOM   1323 C C   . LYS B 1 74 ? 5.209   -15.354 -23.318 1.00 33.94  ? 73  LYS B C   1 
ATOM   1324 O O   . LYS B 1 74 ? 5.166   -15.237 -22.090 1.00 28.42  ? 73  LYS B O   1 
ATOM   1325 C CB  . LYS B 1 74 ? 2.850   -16.239 -23.369 1.00 41.93  ? 73  LYS B CB  1 
ATOM   1326 C CG  . LYS B 1 74 ? 1.501   -16.463 -24.093 1.00 49.33  ? 73  LYS B CG  1 
ATOM   1327 C CD  . LYS B 1 74 ? 0.733   -17.644 -23.506 1.00 49.56  ? 73  LYS B CD  1 
ATOM   1328 C CE  . LYS B 1 74 ? 1.576   -18.886 -23.547 1.00 52.88  ? 73  LYS B CE  1 
ATOM   1329 N NZ  . LYS B 1 74 ? 1.405   -19.701 -22.337 1.00 59.52  ? 73  LYS B NZ  1 
ATOM   1330 N N   . ARG B 1 75 ? 6.365   -15.423 -23.992 1.00 29.76  ? 74  ARG B N   1 
ATOM   1331 C CA  . ARG B 1 75 ? 7.609   -15.339 -23.239 1.00 30.94  ? 74  ARG B CA  1 
ATOM   1332 C C   . ARG B 1 75 ? 7.989   -13.866 -23.129 1.00 29.80  ? 74  ARG B C   1 
ATOM   1333 O O   . ARG B 1 75 ? 7.919   -13.153 -24.132 1.00 26.33  ? 74  ARG B O   1 
ATOM   1334 C CB  . ARG B 1 75 ? 8.809   -16.145 -23.739 1.00 28.19  ? 74  ARG B CB  1 
ATOM   1335 C CG  . ARG B 1 75 ? 8.680   -17.547 -24.307 1.00 30.57  ? 74  ARG B CG  1 
ATOM   1336 C CD  . ARG B 1 75 ? 8.134   -18.455 -23.265 1.00 37.86  ? 74  ARG B CD  1 
ATOM   1337 N NE  . ARG B 1 75 ? 8.596   -19.814 -23.558 1.00 36.60  ? 74  ARG B NE  1 
ATOM   1338 C CZ  . ARG B 1 75 ? 9.417   -20.513 -22.827 1.00 34.11  ? 74  ARG B CZ  1 
ATOM   1339 N NH1 . ARG B 1 75 ? 9.943   -20.003 -21.739 1.00 37.90  ? 74  ARG B NH1 1 
ATOM   1340 N NH2 . ARG B 1 75 ? 9.734   -21.725 -23.213 1.00 41.05  ? 74  ARG B NH2 1 
ATOM   1341 N N   . LYS B 1 76 ? 8.384   -13.463 -21.905 1.00 26.74  ? 75  LYS B N   1 
ATOM   1342 C CA  . LYS B 1 76 ? 8.918   -12.138 -21.602 1.00 27.32  ? 75  LYS B CA  1 
ATOM   1343 C C   . LYS B 1 76 ? 10.090  -11.833 -22.538 1.00 26.97  ? 75  LYS B C   1 
ATOM   1344 O O   . LYS B 1 76 ? 11.081  -12.584 -22.602 1.00 26.10  ? 75  LYS B O   1 
ATOM   1345 C CB  . LYS B 1 76 ? 9.417   -12.000 -20.160 1.00 26.61  ? 75  LYS B CB  1 
ATOM   1346 C CG  . LYS B 1 76 ? 9.726   -10.541 -19.785 1.00 30.16  ? 75  LYS B CG  1 
ATOM   1347 C CD  . LYS B 1 76 ? 10.561  -10.405 -18.518 1.00 38.25  ? 75  LYS B CD  1 
ATOM   1348 C CE  . LYS B 1 76 ? 11.194  -9.045  -18.318 1.00 43.22  ? 75  LYS B CE  1 
ATOM   1349 N NZ  . LYS B 1 76 ? 11.741  -8.931  -16.957 1.00 46.01  ? 75  LYS B NZ  1 
ATOM   1350 N N   . GLY B 1 77 ? 9.951   -10.720 -23.260 1.00 27.15  ? 76  GLY B N   1 
ATOM   1351 C CA  . GLY B 1 77 ? 10.992  -10.220 -24.151 1.00 29.02  ? 76  GLY B CA  1 
ATOM   1352 C C   . GLY B 1 77 ? 10.650  -10.489 -25.621 1.00 32.06  ? 76  GLY B C   1 
ATOM   1353 O O   . GLY B 1 77 ? 11.214  -9.857  -26.525 1.00 32.99  ? 76  GLY B O   1 
ATOM   1354 N N   . PHE B 1 78 ? 9.701   -11.402 -25.856 1.00 28.92  ? 77  PHE B N   1 
ATOM   1355 C CA  . PHE B 1 78 ? 9.642   -12.082 -27.135 1.00 29.07  ? 77  PHE B CA  1 
ATOM   1356 C C   . PHE B 1 78 ? 9.111   -11.168 -28.214 1.00 32.35  ? 77  PHE B C   1 
ATOM   1357 O O   . PHE B 1 78 ? 9.818   -10.926 -29.199 1.00 33.52  ? 77  PHE B O   1 
ATOM   1358 C CB  . PHE B 1 78 ? 8.937   -13.428 -27.162 1.00 29.66  ? 77  PHE B CB  1 
ATOM   1359 C CG  . PHE B 1 78 ? 9.246   -14.160 -28.461 1.00 33.74  ? 77  PHE B CG  1 
ATOM   1360 C CD1 . PHE B 1 78 ? 10.345  -15.006 -28.555 1.00 32.12  ? 77  PHE B CD1 1 
ATOM   1361 C CD2 . PHE B 1 78 ? 8.456   -13.959 -29.584 1.00 32.04  ? 77  PHE B CD2 1 
ATOM   1362 C CE1 . PHE B 1 78 ? 10.615  -15.649 -29.742 1.00 28.05  ? 77  PHE B CE1 1 
ATOM   1363 C CE2 . PHE B 1 78 ? 8.753   -14.596 -30.778 1.00 33.35  ? 77  PHE B CE2 1 
ATOM   1364 C CZ  . PHE B 1 78 ? 9.813   -15.457 -30.833 1.00 28.67  ? 77  PHE B CZ  1 
ATOM   1365 N N   . ASN B 1 79 ? 7.880   -10.686 -28.003 1.00 31.29  ? 78  ASN B N   1 
ATOM   1366 C CA  . ASN B 1 79 ? 7.186   -9.750  -28.882 1.00 34.18  ? 78  ASN B CA  1 
ATOM   1367 C C   . ASN B 1 79 ? 7.910   -8.395  -28.983 1.00 28.70  ? 78  ASN B C   1 
ATOM   1368 O O   . ASN B 1 79 ? 7.887   -7.736  -30.018 1.00 29.28  ? 78  ASN B O   1 
ATOM   1369 C CB  . ASN B 1 79 ? 5.728   -9.618  -28.445 1.00 35.28  ? 78  ASN B CB  1 
ATOM   1370 C CG  . ASN B 1 79 ? 5.050   -10.961 -28.347 1.00 37.37  ? 78  ASN B CG  1 
ATOM   1371 O OD1 . ASN B 1 79 ? 5.406   -11.913 -29.039 1.00 36.61  ? 78  ASN B OD1 1 
ATOM   1372 N ND2 . ASN B 1 79 ? 4.058   -11.062 -27.482 1.00 44.98  ? 78  ASN B ND2 1 
ATOM   1373 N N   . GLU B 1 80 ? 8.579   -7.998  -27.908 1.00 27.93  ? 79  GLU B N   1 
ATOM   1374 C CA  . GLU B 1 80 ? 9.519   -6.891  -27.936 1.00 29.98  ? 79  GLU B CA  1 
ATOM   1375 C C   . GLU B 1 80 ? 10.643  -7.161  -28.932 1.00 27.11  ? 79  GLU B C   1 
ATOM   1376 O O   . GLU B 1 80 ? 10.995  -6.254  -29.684 1.00 27.75  ? 79  GLU B O   1 
ATOM   1377 C CB  . GLU B 1 80 ? 10.147  -6.560  -26.591 1.00 32.68  ? 79  GLU B CB  1 
ATOM   1378 C CG  . GLU B 1 80 ? 10.460  -5.067  -26.477 1.00 46.63  ? 79  GLU B CG  1 
ATOM   1379 N N   . GLY B 1 81 ? 11.199  -8.389  -28.899 1.00 25.22  ? 80  GLY B N   1 
ATOM   1380 C CA  . GLY B 1 81 ? 12.318  -8.818  -29.719 1.00 24.70  ? 80  GLY B CA  1 
ATOM   1381 C C   . GLY B 1 81 ? 11.867  -8.885  -31.177 1.00 27.90  ? 80  GLY B C   1 
ATOM   1382 O O   . GLY B 1 81 ? 12.647  -8.602  -32.080 1.00 30.04  ? 80  GLY B O   1 
ATOM   1383 N N   . LEU B 1 82 ? 10.612  -9.289  -31.391 1.00 25.29  ? 81  LEU B N   1 
ATOM   1384 C CA  . LEU B 1 82 ? 10.029  -9.321  -32.732 1.00 26.91  ? 81  LEU B CA  1 
ATOM   1385 C C   . LEU B 1 82 ? 9.924   -7.890  -33.254 1.00 27.37  ? 81  LEU B C   1 
ATOM   1386 O O   . LEU B 1 82 ? 10.222  -7.619  -34.420 1.00 28.72  ? 81  LEU B O   1 
ATOM   1387 C CB  . LEU B 1 82 ? 8.664   -10.017 -32.793 1.00 27.97  ? 81  LEU B CB  1 
ATOM   1388 C CG  . LEU B 1 82 ? 8.639   -11.546 -32.657 1.00 28.71  ? 81  LEU B CG  1 
ATOM   1389 C CD1 . LEU B 1 82 ? 7.185   -12.018 -32.844 1.00 24.90  ? 81  LEU B CD1 1 
ATOM   1390 C CD2 . LEU B 1 82 ? 9.629   -12.271 -33.611 1.00 26.17  ? 81  LEU B CD2 1 
ATOM   1391 N N   . TRP B 1 83 ? 9.495   -6.973  -32.380 1.00 24.47  ? 82  TRP B N   1 
ATOM   1392 C CA  . TRP B 1 83 ? 9.342   -5.607  -32.825 1.00 25.36  ? 82  TRP B CA  1 
ATOM   1393 C C   . TRP B 1 83 ? 10.699  -5.040  -33.214 1.00 28.06  ? 82  TRP B C   1 
ATOM   1394 O O   . TRP B 1 83 ? 10.793  -4.400  -34.265 1.00 29.99  ? 82  TRP B O   1 
ATOM   1395 C CB  . TRP B 1 83 ? 8.645   -4.738  -31.777 1.00 30.26  ? 82  TRP B CB  1 
ATOM   1396 C CG  . TRP B 1 83 ? 8.441   -3.322  -32.234 1.00 28.58  ? 82  TRP B CG  1 
ATOM   1397 C CD1 . TRP B 1 83 ? 7.333   -2.788  -32.823 1.00 31.94  ? 82  TRP B CD1 1 
ATOM   1398 C CD2 . TRP B 1 83 ? 9.433   -2.271  -32.179 1.00 32.03  ? 82  TRP B CD2 1 
ATOM   1399 N NE1 . TRP B 1 83 ? 7.560   -1.463  -33.103 1.00 35.25  ? 82  TRP B NE1 1 
ATOM   1400 C CE2 . TRP B 1 83 ? 8.836   -1.118  -32.726 1.00 30.06  ? 82  TRP B CE2 1 
ATOM   1401 C CE3 . TRP B 1 83 ? 10.761  -2.192  -31.707 1.00 28.79  ? 82  TRP B CE3 1 
ATOM   1402 C CZ2 . TRP B 1 83 ? 9.528   0.087   -32.839 1.00 32.99  ? 82  TRP B CZ2 1 
ATOM   1403 C CZ3 . TRP B 1 83 ? 11.444  -1.000  -31.830 1.00 30.53  ? 82  TRP B CZ3 1 
ATOM   1404 C CH2 . TRP B 1 83 ? 10.836  0.120   -32.405 1.00 32.22  ? 82  TRP B CH2 1 
ATOM   1405 N N   . GLU B 1 84 ? 11.723  -5.344  -32.400 1.00 27.41  ? 83  GLU B N   1 
ATOM   1406 C CA  . GLU B 1 84 ? 13.087  -4.863  -32.543 1.00 29.26  ? 83  GLU B CA  1 
ATOM   1407 C C   . GLU B 1 84 ? 13.691  -5.271  -33.889 1.00 29.34  ? 83  GLU B C   1 
ATOM   1408 O O   . GLU B 1 84 ? 14.169  -4.420  -34.639 1.00 30.12  ? 83  GLU B O   1 
ATOM   1409 C CB  . GLU B 1 84 ? 13.919  -5.234  -31.320 1.00 31.04  ? 83  GLU B CB  1 
ATOM   1410 C CG  . GLU B 1 84 ? 13.395  -4.542  -30.056 1.00 32.49  ? 83  GLU B CG  1 
ATOM   1411 C CD  . GLU B 1 84 ? 14.281  -4.746  -28.852 1.00 32.34  ? 83  GLU B CD  1 
ATOM   1412 O OE1 . GLU B 1 84 ? 15.283  -5.522  -28.972 1.00 32.30  ? 83  GLU B OE1 1 
ATOM   1413 O OE2 . GLU B 1 84 ? 13.991  -4.101  -27.812 1.00 33.52  ? 83  GLU B OE2 1 
ATOM   1414 N N   . ILE B 1 85 ? 13.690  -6.568  -34.185 1.00 28.19  ? 84  ILE B N   1 
ATOM   1415 C CA  . ILE B 1 85 ? 14.377  -7.108  -35.350 1.00 29.56  ? 84  ILE B CA  1 
ATOM   1416 C C   . ILE B 1 85 ? 13.684  -6.633  -36.632 1.00 28.99  ? 84  ILE B C   1 
ATOM   1417 O O   . ILE B 1 85 ? 14.290  -6.604  -37.714 1.00 27.66  ? 84  ILE B O   1 
ATOM   1418 C CB  . ILE B 1 85 ? 14.417  -8.642  -35.222 1.00 27.98  ? 84  ILE B CB  1 
ATOM   1419 C CG1 . ILE B 1 85 ? 15.450  -9.278  -36.181 1.00 27.41  ? 84  ILE B CG1 1 
ATOM   1420 C CG2 . ILE B 1 85 ? 13.009  -9.252  -35.316 1.00 26.87  ? 84  ILE B CG2 1 
ATOM   1421 C CD1 . ILE B 1 85 ? 15.787  -10.723 -35.829 1.00 26.80  ? 84  ILE B CD1 1 
ATOM   1422 N N   . GLN B 1 86 ? 12.392  -6.278  -36.502 1.00 31.04  ? 85  GLN B N   1 
ATOM   1423 C CA  . GLN B 1 86 ? 11.577  -5.819  -37.616 1.00 34.33  ? 85  GLN B CA  1 
ATOM   1424 C C   . GLN B 1 86 ? 11.716  -4.313  -37.825 1.00 35.28  ? 85  GLN B C   1 
ATOM   1425 O O   . GLN B 1 86 ? 11.646  -3.862  -38.966 1.00 33.37  ? 85  GLN B O   1 
ATOM   1426 C CB  . GLN B 1 86 ? 10.081  -6.043  -37.414 1.00 39.78  ? 85  GLN B CB  1 
ATOM   1427 C CG  . GLN B 1 86 ? 9.653   -7.506  -37.479 1.00 51.55  ? 85  GLN B CG  1 
ATOM   1428 C CD  . GLN B 1 86 ? 8.282   -7.779  -36.886 1.00 58.82  ? 85  GLN B CD  1 
ATOM   1429 O OE1 . GLN B 1 86 ? 7.261   -7.171  -37.247 1.00 61.27  ? 85  GLN B OE1 1 
ATOM   1430 N NE2 . GLN B 1 86 ? 8.254   -8.722  -35.957 1.00 55.15  ? 85  GLN B NE2 1 
ATOM   1431 N N   . ASN B 1 87 ? 11.918  -3.542  -36.739 1.00 29.49  ? 86  ASN B N   1 
ATOM   1432 C CA  . ASN B 1 87 ? 11.762  -2.103  -36.857 1.00 30.61  ? 86  ASN B CA  1 
ATOM   1433 C C   . ASN B 1 87 ? 13.081  -1.364  -36.685 1.00 30.62  ? 86  ASN B C   1 
ATOM   1434 O O   . ASN B 1 87 ? 13.234  -0.259  -37.194 1.00 34.09  ? 86  ASN B O   1 
ATOM   1435 C CB  . ASN B 1 87 ? 10.667  -1.549  -35.949 1.00 31.37  ? 86  ASN B CB  1 
ATOM   1436 C CG  . ASN B 1 87 ? 9.324   -2.052  -36.409 1.00 39.62  ? 86  ASN B CG  1 
ATOM   1437 O OD1 . ASN B 1 87 ? 8.667   -1.372  -37.204 1.00 42.41  ? 86  ASN B OD1 1 
ATOM   1438 N ND2 . ASN B 1 87 ? 8.948   -3.266  -36.016 1.00 36.55  ? 86  ASN B ND2 1 
ATOM   1439 N N   . ASN B 1 88 ? 14.002  -1.926  -35.906 1.00 30.80  ? 87  ASN B N   1 
ATOM   1440 C CA  . ASN B 1 88 ? 15.264  -1.237  -35.694 1.00 31.13  ? 87  ASN B CA  1 
ATOM   1441 C C   . ASN B 1 88 ? 16.303  -2.278  -35.281 1.00 28.59  ? 87  ASN B C   1 
ATOM   1442 O O   . ASN B 1 88 ? 16.790  -2.292  -34.150 1.00 31.50  ? 87  ASN B O   1 
ATOM   1443 C CB  . ASN B 1 88 ? 15.096  -0.006  -34.793 1.00 32.68  ? 87  ASN B CB  1 
ATOM   1444 C CG  . ASN B 1 88 ? 16.226  0.991   -34.943 1.00 33.07  ? 87  ASN B CG  1 
ATOM   1445 O OD1 . ASN B 1 88 ? 17.265  0.694   -35.545 1.00 36.62  ? 87  ASN B OD1 1 
ATOM   1446 N ND2 . ASN B 1 88 ? 16.069  2.177   -34.379 1.00 30.50  ? 87  ASN B ND2 1 
ATOM   1447 N N   . PRO B 1 89 ? 16.618  -3.234  -36.174 1.00 25.74  ? 88  PRO B N   1 
ATOM   1448 C CA  . PRO B 1 89 ? 17.523  -4.326  -35.823 1.00 25.02  ? 88  PRO B CA  1 
ATOM   1449 C C   . PRO B 1 89 ? 18.957  -3.958  -35.483 1.00 28.26  ? 88  PRO B C   1 
ATOM   1450 O O   . PRO B 1 89 ? 19.670  -4.773  -34.915 1.00 33.47  ? 88  PRO B O   1 
ATOM   1451 C CB  . PRO B 1 89 ? 17.443  -5.199  -37.067 1.00 25.61  ? 88  PRO B CB  1 
ATOM   1452 C CG  . PRO B 1 89 ? 17.108  -4.229  -38.183 1.00 24.62  ? 88  PRO B CG  1 
ATOM   1453 C CD  . PRO B 1 89 ? 16.081  -3.323  -37.545 1.00 25.44  ? 88  PRO B CD  1 
ATOM   1454 N N   . HIS B 1 90 ? 19.371  -2.733  -35.835 1.00 31.08  ? 89  HIS B N   1 
ATOM   1455 C CA  . HIS B 1 90 ? 20.768  -2.324  -35.786 1.00 32.19  ? 89  HIS B CA  1 
ATOM   1456 C C   . HIS B 1 90 ? 20.945  -1.213  -34.769 1.00 31.37  ? 89  HIS B C   1 
ATOM   1457 O O   . HIS B 1 90 ? 22.026  -0.638  -34.664 1.00 30.88  ? 89  HIS B O   1 
ATOM   1458 C CB  . HIS B 1 90 ? 21.236  -1.889  -37.191 1.00 30.31  ? 89  HIS B CB  1 
ATOM   1459 C CG  . HIS B 1 90 ? 21.054  -2.967  -38.204 1.00 24.13  ? 89  HIS B CG  1 
ATOM   1460 N ND1 . HIS B 1 90 ? 21.616  -4.206  -38.034 1.00 21.07  ? 89  HIS B ND1 1 
ATOM   1461 C CD2 . HIS B 1 90 ? 20.382  -2.999  -39.394 1.00 24.73  ? 89  HIS B CD2 1 
ATOM   1462 C CE1 . HIS B 1 90 ? 21.314  -4.959  -39.100 1.00 21.66  ? 89  HIS B CE1 1 
ATOM   1463 N NE2 . HIS B 1 90 ? 20.536  -4.256  -39.929 1.00 22.39  ? 89  HIS B NE2 1 
ATOM   1464 N N   . ALA B 1 91 ? 19.862  -0.916  -34.037 1.00 31.12  ? 90  ALA B N   1 
ATOM   1465 C CA  . ALA B 1 91 ? 19.891  0.057   -32.964 1.00 30.02  ? 90  ALA B CA  1 
ATOM   1466 C C   . ALA B 1 91 ? 20.810  -0.418  -31.842 1.00 30.66  ? 90  ALA B C   1 
ATOM   1467 O O   . ALA B 1 91 ? 21.095  -1.607  -31.719 1.00 29.93  ? 90  ALA B O   1 
ATOM   1468 C CB  . ALA B 1 91 ? 18.489  0.357   -32.467 1.00 28.66  ? 90  ALA B CB  1 
ATOM   1469 N N   . SER B 1 92 ? 21.301  0.544   -31.061 1.00 29.04  ? 91  SER B N   1 
ATOM   1470 C CA  . SER B 1 92 ? 21.939  0.275   -29.787 1.00 34.64  ? 91  SER B CA  1 
ATOM   1471 C C   . SER B 1 92 ? 20.852  0.094   -28.734 1.00 34.59  ? 91  SER B C   1 
ATOM   1472 O O   . SER B 1 92 ? 19.955  0.924   -28.623 1.00 34.81  ? 91  SER B O   1 
ATOM   1473 C CB  . SER B 1 92 ? 22.864  1.400   -29.391 1.00 38.64  ? 91  SER B CB  1 
ATOM   1474 O OG  . SER B 1 92 ? 23.469  1.109   -28.135 1.00 41.11  ? 91  SER B OG  1 
ATOM   1475 N N   . TYR B 1 93 ? 20.893  -1.028  -28.020 1.00 36.91  ? 92  TYR B N   1 
ATOM   1476 C CA  . TYR B 1 93 ? 19.897  -1.309  -26.995 1.00 36.26  ? 92  TYR B CA  1 
ATOM   1477 C C   . TYR B 1 93 ? 20.585  -1.391  -25.637 1.00 43.95  ? 92  TYR B C   1 
ATOM   1478 O O   . TYR B 1 93 ? 19.975  -1.856  -24.675 1.00 49.98  ? 92  TYR B O   1 
ATOM   1479 C CB  . TYR B 1 93 ? 19.146  -2.604  -27.309 1.00 34.01  ? 92  TYR B CB  1 
ATOM   1480 C CG  . TYR B 1 93 ? 18.222  -2.509  -28.511 1.00 29.85  ? 92  TYR B CG  1 
ATOM   1481 C CD1 . TYR B 1 93 ? 16.928  -2.022  -28.393 1.00 30.25  ? 92  TYR B CD1 1 
ATOM   1482 C CD2 . TYR B 1 93 ? 18.669  -2.873  -29.771 1.00 31.82  ? 92  TYR B CD2 1 
ATOM   1483 C CE1 . TYR B 1 93 ? 16.090  -1.935  -29.488 1.00 27.21  ? 92  TYR B CE1 1 
ATOM   1484 C CE2 . TYR B 1 93 ? 17.841  -2.798  -30.875 1.00 28.13  ? 92  TYR B CE2 1 
ATOM   1485 C CZ  . TYR B 1 93 ? 16.562  -2.305  -30.733 1.00 27.45  ? 92  TYR B CZ  1 
ATOM   1486 O OH  . TYR B 1 93 ? 15.782  -2.222  -31.830 1.00 26.92  ? 92  TYR B OH  1 
ATOM   1487 N N   . SER B 1 94 ? 21.871  -1.001  -25.626 1.00 55.68  ? 93  SER B N   1 
ATOM   1488 C CA  . SER B 1 94 ? 22.684  -0.582  -24.486 1.00 78.37  ? 93  SER B CA  1 
ATOM   1489 C C   . SER B 1 94 ? 22.098  -1.053  -23.146 1.00 88.72  ? 93  SER B C   1 
ATOM   1490 O O   . SER B 1 94 ? 21.211  -0.330  -22.630 1.00 89.10  ? 93  SER B O   1 
ATOM   1491 C CB  . SER B 1 94 ? 22.869  0.925   -24.471 1.00 83.01  ? 93  SER B CB  1 
ATOM   1492 O OG  . SER B 1 94 ? 23.427  1.402   -25.690 1.00 83.50  ? 93  SER B OG  1 
ATOM   1493 O OXT . SER B 1 94 ? 22.567  -2.108  -22.649 1.00 100.62 ? 93  SER B OXT 1 
ATOM   1494 N N   . HIS C 1 4  ? 32.210  -21.730 27.951  1.00 91.96  ? 3   HIS C N   1 
ATOM   1495 C CA  . HIS C 1 4  ? 30.869  -21.199 28.337  1.00 98.85  ? 3   HIS C CA  1 
ATOM   1496 C C   . HIS C 1 4  ? 29.966  -22.338 28.824  1.00 87.87  ? 3   HIS C C   1 
ATOM   1497 O O   . HIS C 1 4  ? 30.163  -23.485 28.423  1.00 86.59  ? 3   HIS C O   1 
ATOM   1498 C CB  . HIS C 1 4  ? 30.248  -20.398 27.182  1.00 103.05 ? 3   HIS C CB  1 
ATOM   1499 C CG  . HIS C 1 4  ? 29.337  -19.285 27.621  1.00 113.74 ? 3   HIS C CG  1 
ATOM   1500 N ND1 . HIS C 1 4  ? 27.995  -19.440 27.909  1.00 112.90 ? 3   HIS C ND1 1 
ATOM   1501 C CD2 . HIS C 1 4  ? 29.605  -17.982 27.830  1.00 100.93 ? 3   HIS C CD2 1 
ATOM   1502 C CE1 . HIS C 1 4  ? 27.480  -18.270 28.274  1.00 100.54 ? 3   HIS C CE1 1 
ATOM   1503 N NE2 . HIS C 1 4  ? 28.440  -17.371 28.228  1.00 94.31  ? 3   HIS C NE2 1 
ATOM   1504 N N   . ALA C 1 5  ? 28.998  -22.005 29.708  1.00 76.83  ? 4   ALA C N   1 
ATOM   1505 C CA  . ALA C 1 5  ? 27.932  -22.897 30.160  1.00 64.69  ? 4   ALA C CA  1 
ATOM   1506 C C   . ALA C 1 5  ? 26.563  -22.406 29.685  1.00 66.16  ? 4   ALA C C   1 
ATOM   1507 O O   . ALA C 1 5  ? 26.406  -21.276 29.208  1.00 61.94  ? 4   ALA C O   1 
ATOM   1508 C CB  . ALA C 1 5  ? 27.941  -23.143 31.671  1.00 54.17  ? 4   ALA C CB  1 
ATOM   1509 N N   . PHE C 1 6  ? 25.577  -23.297 29.835  1.00 58.63  ? 5   PHE C N   1 
ATOM   1510 C CA  . PHE C 1 6  ? 24.228  -23.068 29.354  1.00 61.78  ? 5   PHE C CA  1 
ATOM   1511 C C   . PHE C 1 6  ? 23.283  -22.986 30.552  1.00 65.81  ? 5   PHE C C   1 
ATOM   1512 O O   . PHE C 1 6  ? 23.316  -23.848 31.433  1.00 67.25  ? 5   PHE C O   1 
ATOM   1513 C CB  . PHE C 1 6  ? 23.894  -24.193 28.365  1.00 54.57  ? 5   PHE C CB  1 
ATOM   1514 C CG  . PHE C 1 6  ? 24.826  -24.279 27.164  1.00 51.29  ? 5   PHE C CG  1 
ATOM   1515 C CD1 . PHE C 1 6  ? 26.018  -24.998 27.235  1.00 48.74  ? 5   PHE C CD1 1 
ATOM   1516 C CD2 . PHE C 1 6  ? 24.514  -23.630 25.972  1.00 48.12  ? 5   PHE C CD2 1 
ATOM   1517 C CE1 . PHE C 1 6  ? 26.874  -25.073 26.140  1.00 53.25  ? 5   PHE C CE1 1 
ATOM   1518 C CE2 . PHE C 1 6  ? 25.371  -23.706 24.880  1.00 47.90  ? 5   PHE C CE2 1 
ATOM   1519 C CZ  . PHE C 1 6  ? 26.550  -24.425 24.965  1.00 51.08  ? 5   PHE C CZ  1 
ATOM   1520 N N   . LYS C 1 7  ? 22.466  -21.922 30.581  1.00 60.44  ? 6   LYS C N   1 
ATOM   1521 C CA  . LYS C 1 7  ? 21.472  -21.732 31.624  1.00 61.89  ? 6   LYS C CA  1 
ATOM   1522 C C   . LYS C 1 7  ? 20.140  -22.237 31.081  1.00 60.12  ? 6   LYS C C   1 
ATOM   1523 O O   . LYS C 1 7  ? 19.876  -22.104 29.884  1.00 55.53  ? 6   LYS C O   1 
ATOM   1524 C CB  . LYS C 1 7  ? 21.423  -20.268 32.090  1.00 57.29  ? 6   LYS C CB  1 
ATOM   1525 N N   . PRO C 1 8  ? 19.269  -22.841 31.924  1.00 59.47  ? 7   PRO C N   1 
ATOM   1526 C CA  . PRO C 1 8  ? 17.984  -23.367 31.449  1.00 65.23  ? 7   PRO C CA  1 
ATOM   1527 C C   . PRO C 1 8  ? 17.232  -22.311 30.632  1.00 68.80  ? 7   PRO C C   1 
ATOM   1528 O O   . PRO C 1 8  ? 17.283  -21.121 30.955  1.00 80.54  ? 7   PRO C O   1 
ATOM   1529 C CB  . PRO C 1 8  ? 17.239  -23.788 32.732  1.00 56.73  ? 7   PRO C CB  1 
ATOM   1530 C CG  . PRO C 1 8  ? 18.348  -24.006 33.733  1.00 51.20  ? 7   PRO C CG  1 
ATOM   1531 C CD  . PRO C 1 8  ? 19.458  -23.027 33.374  1.00 55.99  ? 7   PRO C CD  1 
ATOM   1532 N N   . GLY C 1 9  ? 16.577  -22.744 29.545  1.00 56.16  ? 8   GLY C N   1 
ATOM   1533 C CA  . GLY C 1 9  ? 15.956  -21.812 28.618  1.00 53.05  ? 8   GLY C CA  1 
ATOM   1534 C C   . GLY C 1 9  ? 16.869  -21.435 27.444  1.00 49.41  ? 8   GLY C C   1 
ATOM   1535 O O   . GLY C 1 9  ? 16.356  -21.020 26.407  1.00 49.63  ? 8   GLY C O   1 
ATOM   1536 N N   . ASP C 1 10 ? 18.200  -21.575 27.612  1.00 43.16  ? 9   ASP C N   1 
ATOM   1537 C CA  . ASP C 1 10 ? 19.207  -21.250 26.601  1.00 40.03  ? 9   ASP C CA  1 
ATOM   1538 C C   . ASP C 1 10 ? 18.919  -21.991 25.294  1.00 41.99  ? 9   ASP C C   1 
ATOM   1539 O O   . ASP C 1 10 ? 18.644  -23.187 25.302  1.00 42.44  ? 9   ASP C O   1 
ATOM   1540 C CB  . ASP C 1 10 ? 20.624  -21.524 27.075  1.00 48.31  ? 9   ASP C CB  1 
ATOM   1541 C CG  . ASP C 1 10 ? 21.307  -20.422 27.883  1.00 56.54  ? 9   ASP C CG  1 
ATOM   1542 O OD1 . ASP C 1 10 ? 20.650  -19.397 28.187  1.00 57.88  ? 9   ASP C OD1 1 
ATOM   1543 O OD2 . ASP C 1 10 ? 22.510  -20.578 28.190  1.00 57.42  ? 9   ASP C OD2 1 
ATOM   1544 N N   . LEU C 1 11 ? 18.925  -21.247 24.179  1.00 39.85  ? 10  LEU C N   1 
ATOM   1545 C CA  . LEU C 1 11 ? 18.536  -21.754 22.868  1.00 34.15  ? 10  LEU C CA  1 
ATOM   1546 C C   . LEU C 1 11 ? 19.808  -22.186 22.151  1.00 34.50  ? 10  LEU C C   1 
ATOM   1547 O O   . LEU C 1 11 ? 20.761  -21.408 22.072  1.00 34.31  ? 10  LEU C O   1 
ATOM   1548 C CB  . LEU C 1 11 ? 17.753  -20.737 22.032  1.00 34.05  ? 10  LEU C CB  1 
ATOM   1549 C CG  . LEU C 1 11 ? 16.455  -20.189 22.626  1.00 33.63  ? 10  LEU C CG  1 
ATOM   1550 C CD1 . LEU C 1 11 ? 15.774  -19.295 21.598  1.00 37.50  ? 10  LEU C CD1 1 
ATOM   1551 C CD2 . LEU C 1 11 ? 15.524  -21.285 23.074  1.00 30.89  ? 10  LEU C CD2 1 
ATOM   1552 N N   . VAL C 1 12 ? 19.788  -23.434 21.647  1.00 30.56  ? 11  VAL C N   1 
ATOM   1553 C CA  . VAL C 1 12 ? 20.944  -24.118 21.090  1.00 30.84  ? 11  VAL C CA  1 
ATOM   1554 C C   . VAL C 1 12 ? 20.572  -24.750 19.738  1.00 30.21  ? 11  VAL C C   1 
ATOM   1555 O O   . VAL C 1 12 ? 19.416  -24.761 19.315  1.00 29.69  ? 11  VAL C O   1 
ATOM   1556 C CB  . VAL C 1 12 ? 21.568  -25.159 22.054  1.00 32.23  ? 11  VAL C CB  1 
ATOM   1557 C CG1 . VAL C 1 12 ? 22.175  -24.517 23.299  1.00 37.39  ? 11  VAL C CG1 1 
ATOM   1558 C CG2 . VAL C 1 12 ? 20.554  -26.208 22.525  1.00 32.48  ? 11  VAL C CG2 1 
ATOM   1559 N N   . PHE C 1 13 ? 21.611  -25.214 19.036  1.00 29.98  ? 12  PHE C N   1 
ATOM   1560 C CA  . PHE C 1 13 ? 21.557  -26.341 18.120  1.00 27.64  ? 12  PHE C CA  1 
ATOM   1561 C C   . PHE C 1 13 ? 22.215  -27.509 18.839  1.00 28.80  ? 12  PHE C C   1 
ATOM   1562 O O   . PHE C 1 13 ? 23.286  -27.360 19.465  1.00 26.32  ? 12  PHE C O   1 
ATOM   1563 C CB  . PHE C 1 13 ? 22.148  -26.068 16.725  1.00 27.92  ? 12  PHE C CB  1 
ATOM   1564 C CG  . PHE C 1 13 ? 21.214  -25.211 15.883  1.00 30.69  ? 12  PHE C CG  1 
ATOM   1565 C CD1 . PHE C 1 13 ? 20.123  -25.780 15.211  1.00 30.52  ? 12  PHE C CD1 1 
ATOM   1566 C CD2 . PHE C 1 13 ? 21.351  -23.826 15.845  1.00 31.57  ? 12  PHE C CD2 1 
ATOM   1567 C CE1 . PHE C 1 13 ? 19.233  -25.000 14.477  1.00 34.28  ? 12  PHE C CE1 1 
ATOM   1568 C CE2 . PHE C 1 13 ? 20.462  -23.050 15.101  1.00 32.37  ? 12  PHE C CE2 1 
ATOM   1569 C CZ  . PHE C 1 13 ? 19.404  -23.633 14.429  1.00 35.91  ? 12  PHE C CZ  1 
ATOM   1570 N N   . ALA C 1 14 ? 21.504  -28.644 18.819  1.00 30.21  ? 13  ALA C N   1 
ATOM   1571 C CA  . ALA C 1 14 ? 21.914  -29.821 19.578  1.00 28.94  ? 13  ALA C CA  1 
ATOM   1572 C C   . ALA C 1 14 ? 22.187  -30.925 18.578  1.00 30.76  ? 13  ALA C C   1 
ATOM   1573 O O   . ALA C 1 14 ? 21.293  -31.264 17.793  1.00 33.33  ? 13  ALA C O   1 
ATOM   1574 C CB  . ALA C 1 14 ? 20.817  -30.240 20.534  1.00 24.75  ? 13  ALA C CB  1 
ATOM   1575 N N   . LYS C 1 15 ? 23.421  -31.446 18.620  1.00 29.39  ? 14  LYS C N   1 
ATOM   1576 C CA  . LYS C 1 15 ? 23.820  -32.482 17.689  1.00 26.41  ? 14  LYS C CA  1 
ATOM   1577 C C   . LYS C 1 15 ? 23.714  -33.830 18.373  1.00 27.60  ? 14  LYS C C   1 
ATOM   1578 O O   . LYS C 1 15 ? 24.347  -34.024 19.409  1.00 32.29  ? 14  LYS C O   1 
ATOM   1579 C CB  . LYS C 1 15 ? 25.275  -32.282 17.236  1.00 28.74  ? 14  LYS C CB  1 
ATOM   1580 C CG  . LYS C 1 15 ? 25.731  -33.304 16.171  1.00 30.08  ? 14  LYS C CG  1 
ATOM   1581 C CD  . LYS C 1 15 ? 24.731  -33.296 15.014  1.00 27.80  ? 14  LYS C CD  1 
ATOM   1582 C CE  . LYS C 1 15 ? 25.210  -33.978 13.758  1.00 29.31  ? 14  LYS C CE  1 
ATOM   1583 N NZ  . LYS C 1 15 ? 25.072  -35.432 13.941  1.00 30.49  ? 14  LYS C NZ  1 
ATOM   1584 N N   . MET C 1 16 ? 22.839  -34.701 17.860  1.00 24.21  ? 15  MET C N   1 
ATOM   1585 C CA  . MET C 1 16 ? 22.854  -36.115 18.195  1.00 27.13  ? 15  MET C CA  1 
ATOM   1586 C C   . MET C 1 16 ? 23.332  -36.928 16.991  1.00 32.52  ? 15  MET C C   1 
ATOM   1587 O O   . MET C 1 16 ? 23.064  -36.548 15.840  1.00 32.76  ? 15  MET C O   1 
ATOM   1588 C CB  . MET C 1 16 ? 21.470  -36.627 18.579  1.00 28.83  ? 15  MET C CB  1 
ATOM   1589 C CG  . MET C 1 16 ? 21.023  -36.155 19.933  1.00 35.75  ? 15  MET C CG  1 
ATOM   1590 S SD  . MET C 1 16 ? 19.412  -36.862 20.311  1.00 43.50  ? 15  MET C SD  1 
ATOM   1591 C CE  . MET C 1 16 ? 18.530  -36.617 18.758  1.00 46.14  ? 15  MET C CE  1 
ATOM   1592 N N   . LYS C 1 17 ? 24.025  -38.048 17.274  1.00 33.21  ? 16  LYS C N   1 
ATOM   1593 C CA  . LYS C 1 17 ? 24.406  -39.041 16.267  1.00 33.95  ? 16  LYS C CA  1 
ATOM   1594 C C   . LYS C 1 17 ? 23.129  -39.539 15.596  1.00 29.73  ? 16  LYS C C   1 
ATOM   1595 O O   . LYS C 1 17 ? 22.173  -39.936 16.274  1.00 26.57  ? 16  LYS C O   1 
ATOM   1596 C CB  . LYS C 1 17 ? 25.194  -40.232 16.854  1.00 32.05  ? 16  LYS C CB  1 
ATOM   1597 C CG  . LYS C 1 17 ? 25.860  -41.202 15.867  1.00 35.06  ? 16  LYS C CG  1 
ATOM   1598 C CD  . LYS C 1 17 ? 27.053  -40.459 15.268  1.00 39.36  ? 16  LYS C CD  1 
ATOM   1599 C CE  . LYS C 1 17 ? 27.815  -41.164 14.191  1.00 37.38  ? 16  LYS C CE  1 
ATOM   1600 N NZ  . LYS C 1 17 ? 28.773  -40.245 13.564  1.00 32.62  ? 16  LYS C NZ  1 
ATOM   1601 N N   . GLY C 1 18 ? 23.119  -39.461 14.258  1.00 31.51  ? 17  GLY C N   1 
ATOM   1602 C CA  . GLY C 1 18 ? 21.995  -39.913 13.458  1.00 32.35  ? 17  GLY C CA  1 
ATOM   1603 C C   . GLY C 1 18 ? 21.094  -38.768 12.992  1.00 37.00  ? 17  GLY C C   1 
ATOM   1604 O O   . GLY C 1 18 ? 20.063  -39.017 12.364  1.00 34.14  ? 17  GLY C O   1 
ATOM   1605 N N   . TYR C 1 19 ? 21.481  -37.523 13.309  1.00 38.55  ? 18  TYR C N   1 
ATOM   1606 C CA  . TYR C 1 19 ? 20.555  -36.395 13.260  1.00 39.22  ? 18  TYR C CA  1 
ATOM   1607 C C   . TYR C 1 19 ? 21.317  -35.133 12.874  1.00 41.08  ? 18  TYR C C   1 
ATOM   1608 O O   . TYR C 1 19 ? 22.471  -34.954 13.267  1.00 36.76  ? 18  TYR C O   1 
ATOM   1609 C CB  . TYR C 1 19 ? 19.816  -36.163 14.591  1.00 37.45  ? 18  TYR C CB  1 
ATOM   1610 C CG  . TYR C 1 19 ? 18.862  -37.286 14.979  1.00 38.87  ? 18  TYR C CG  1 
ATOM   1611 C CD1 . TYR C 1 19 ? 19.305  -38.433 15.644  1.00 40.48  ? 18  TYR C CD1 1 
ATOM   1612 C CD2 . TYR C 1 19 ? 17.516  -37.213 14.651  1.00 42.51  ? 18  TYR C CD2 1 
ATOM   1613 C CE1 . TYR C 1 19 ? 18.445  -39.467 15.986  1.00 37.20  ? 18  TYR C CE1 1 
ATOM   1614 C CE2 . TYR C 1 19 ? 16.640  -38.237 14.984  1.00 46.09  ? 18  TYR C CE2 1 
ATOM   1615 C CZ  . TYR C 1 19 ? 17.110  -39.357 15.645  1.00 42.10  ? 18  TYR C CZ  1 
ATOM   1616 O OH  . TYR C 1 19 ? 16.232  -40.337 15.949  1.00 56.48  ? 18  TYR C OH  1 
ATOM   1617 N N   . PRO C 1 20 ? 20.693  -34.239 12.067  1.00 40.05  ? 19  PRO C N   1 
ATOM   1618 C CA  . PRO C 1 20 ? 21.285  -32.930 11.776  1.00 33.41  ? 19  PRO C CA  1 
ATOM   1619 C C   . PRO C 1 20 ? 21.334  -32.140 13.082  1.00 30.72  ? 19  PRO C C   1 
ATOM   1620 O O   . PRO C 1 20 ? 20.551  -32.437 13.968  1.00 27.37  ? 19  PRO C O   1 
ATOM   1621 C CB  . PRO C 1 20 ? 20.257  -32.334 10.802  1.00 30.98  ? 19  PRO C CB  1 
ATOM   1622 C CG  . PRO C 1 20 ? 18.944  -33.046 11.087  1.00 31.68  ? 19  PRO C CG  1 
ATOM   1623 C CD  . PRO C 1 20 ? 19.381  -34.450 11.409  1.00 35.83  ? 19  PRO C CD  1 
ATOM   1624 N N   . HIS C 1 21 ? 22.226  -31.133 13.180  1.00 29.45  ? 20  HIS C N   1 
ATOM   1625 C CA  . HIS C 1 21 ? 22.173  -30.239 14.329  1.00 31.75  ? 20  HIS C CA  1 
ATOM   1626 C C   . HIS C 1 21 ? 20.749  -29.697 14.466  1.00 33.66  ? 20  HIS C C   1 
ATOM   1627 O O   . HIS C 1 21 ? 20.219  -29.153 13.487  1.00 31.10  ? 20  HIS C O   1 
ATOM   1628 C CB  . HIS C 1 21 ? 23.162  -29.098 14.129  1.00 31.48  ? 20  HIS C CB  1 
ATOM   1629 C CG  . HIS C 1 21 ? 24.579  -29.598 14.074  1.00 38.56  ? 20  HIS C CG  1 
ATOM   1630 N ND1 . HIS C 1 21 ? 25.111  -30.227 12.966  1.00 39.04  ? 20  HIS C ND1 1 
ATOM   1631 C CD2 . HIS C 1 21 ? 25.550  -29.576 14.993  1.00 37.71  ? 20  HIS C CD2 1 
ATOM   1632 C CE1 . HIS C 1 21 ? 26.372  -30.533 13.205  1.00 40.41  ? 20  HIS C CE1 1 
ATOM   1633 N NE2 . HIS C 1 21 ? 26.661  -30.148 14.433  1.00 38.12  ? 20  HIS C NE2 1 
ATOM   1634 N N   . TRP C 1 22 ? 20.142  -29.855 15.662  1.00 28.56  ? 21  TRP C N   1 
ATOM   1635 C CA  . TRP C 1 22 ? 18.683  -29.728 15.816  1.00 29.11  ? 21  TRP C CA  1 
ATOM   1636 C C   . TRP C 1 22 ? 18.328  -28.490 16.648  1.00 28.51  ? 21  TRP C C   1 
ATOM   1637 O O   . TRP C 1 22 ? 18.979  -28.236 17.662  1.00 28.04  ? 21  TRP C O   1 
ATOM   1638 C CB  . TRP C 1 22 ? 18.077  -30.984 16.474  1.00 31.51  ? 21  TRP C CB  1 
ATOM   1639 C CG  . TRP C 1 22 ? 16.621  -31.200 16.146  1.00 32.86  ? 21  TRP C CG  1 
ATOM   1640 C CD1 . TRP C 1 22 ? 15.527  -30.573 16.669  1.00 33.11  ? 21  TRP C CD1 1 
ATOM   1641 C CD2 . TRP C 1 22 ? 16.116  -32.112 15.149  1.00 32.08  ? 21  TRP C CD2 1 
ATOM   1642 N NE1 . TRP C 1 22 ? 14.383  -31.007 16.055  1.00 30.89  ? 21  TRP C NE1 1 
ATOM   1643 C CE2 . TRP C 1 22 ? 14.710  -31.955 15.127  1.00 34.62  ? 21  TRP C CE2 1 
ATOM   1644 C CE3 . TRP C 1 22 ? 16.714  -33.035 14.276  1.00 31.17  ? 21  TRP C CE3 1 
ATOM   1645 C CZ2 . TRP C 1 22 ? 13.903  -32.711 14.275  1.00 32.82  ? 21  TRP C CZ2 1 
ATOM   1646 C CZ3 . TRP C 1 22 ? 15.915  -33.772 13.415  1.00 33.11  ? 21  TRP C CZ3 1 
ATOM   1647 C CH2 . TRP C 1 22 ? 14.526  -33.620 13.434  1.00 33.42  ? 21  TRP C CH2 1 
ATOM   1648 N N   . PRO C 1 23 ? 17.279  -27.694 16.302  1.00 28.39  ? 22  PRO C N   1 
ATOM   1649 C CA  . PRO C 1 23 ? 16.899  -26.542 17.133  1.00 29.34  ? 22  PRO C CA  1 
ATOM   1650 C C   . PRO C 1 23 ? 16.360  -27.034 18.479  1.00 26.74  ? 22  PRO C C   1 
ATOM   1651 O O   . PRO C 1 23 ? 15.490  -27.891 18.531  1.00 28.28  ? 22  PRO C O   1 
ATOM   1652 C CB  . PRO C 1 23 ? 15.881  -25.780 16.253  1.00 27.35  ? 22  PRO C CB  1 
ATOM   1653 C CG  . PRO C 1 23 ? 15.215  -26.888 15.483  1.00 26.12  ? 22  PRO C CG  1 
ATOM   1654 C CD  . PRO C 1 23 ? 16.400  -27.821 15.133  1.00 27.78  ? 22  PRO C CD  1 
ATOM   1655 N N   . ALA C 1 24 ? 16.933  -26.543 19.581  1.00 26.24  ? 23  ALA C N   1 
ATOM   1656 C CA  . ALA C 1 24 ? 16.628  -27.140 20.873  1.00 25.58  ? 23  ALA C CA  1 
ATOM   1657 C C   . ALA C 1 24 ? 16.812  -26.097 21.973  1.00 29.33  ? 23  ALA C C   1 
ATOM   1658 O O   . ALA C 1 24 ? 17.165  -24.954 21.701  1.00 27.23  ? 23  ALA C O   1 
ATOM   1659 C CB  . ALA C 1 24 ? 17.488  -28.388 21.091  1.00 23.39  ? 23  ALA C CB  1 
ATOM   1660 N N   . ARG C 1 25 ? 16.538  -26.480 23.228  1.00 31.41  ? 24  ARG C N   1 
ATOM   1661 C CA  . ARG C 1 25 ? 16.755  -25.583 24.345  1.00 32.62  ? 24  ARG C CA  1 
ATOM   1662 C C   . ARG C 1 25 ? 17.256  -26.402 25.541  1.00 33.26  ? 24  ARG C C   1 
ATOM   1663 O O   . ARG C 1 25 ? 16.966  -27.591 25.636  1.00 33.62  ? 24  ARG C O   1 
ATOM   1664 C CB  . ARG C 1 25 ? 15.467  -24.782 24.584  1.00 32.08  ? 24  ARG C CB  1 
ATOM   1665 C CG  . ARG C 1 25 ? 14.333  -25.455 25.333  1.00 35.56  ? 24  ARG C CG  1 
ATOM   1666 C CD  . ARG C 1 25 ? 13.241  -24.498 25.809  1.00 36.93  ? 24  ARG C CD  1 
ATOM   1667 N NE  . ARG C 1 25 ? 12.160  -25.293 26.401  1.00 39.86  ? 24  ARG C NE  1 
ATOM   1668 C CZ  . ARG C 1 25 ? 10.872  -25.299 26.022  1.00 50.56  ? 24  ARG C CZ  1 
ATOM   1669 N NH1 . ARG C 1 25 ? 10.405  -24.374 25.193  1.00 54.43  ? 24  ARG C NH1 1 
ATOM   1670 N NH2 . ARG C 1 25 ? 10.025  -26.201 26.502  1.00 45.73  ? 24  ARG C NH2 1 
ATOM   1671 N N   . ILE C 1 26 ? 18.031  -25.775 26.431  1.00 32.82  ? 25  ILE C N   1 
ATOM   1672 C CA  . ILE C 1 26 ? 18.413  -26.376 27.707  1.00 35.32  ? 25  ILE C CA  1 
ATOM   1673 C C   . ILE C 1 26 ? 17.194  -26.388 28.644  1.00 41.46  ? 25  ILE C C   1 
ATOM   1674 O O   . ILE C 1 26 ? 16.700  -25.320 29.004  1.00 44.55  ? 25  ILE C O   1 
ATOM   1675 C CB  . ILE C 1 26 ? 19.577  -25.581 28.331  1.00 36.57  ? 25  ILE C CB  1 
ATOM   1676 C CG1 . ILE C 1 26 ? 20.743  -25.395 27.378  1.00 37.62  ? 25  ILE C CG1 1 
ATOM   1677 C CG2 . ILE C 1 26 ? 20.029  -26.195 29.659  1.00 32.24  ? 25  ILE C CG2 1 
ATOM   1678 C CD1 . ILE C 1 26 ? 21.345  -26.694 26.893  1.00 41.26  ? 25  ILE C CD1 1 
ATOM   1679 N N   . ASP C 1 27 ? 16.700  -27.579 29.036  1.00 40.93  ? 26  ASP C N   1 
ATOM   1680 C CA  . ASP C 1 27 ? 15.662  -27.712 30.062  1.00 51.59  ? 26  ASP C CA  1 
ATOM   1681 C C   . ASP C 1 27 ? 16.188  -27.413 31.478  1.00 51.38  ? 26  ASP C C   1 
ATOM   1682 O O   . ASP C 1 27 ? 17.213  -26.672 31.593  1.00 51.63  ? 26  ASP C O   1 
ATOM   1683 C CB  . ASP C 1 27 ? 15.051  -29.106 30.115  1.00 56.97  ? 26  ASP C CB  1 
ATOM   1684 C CG  . ASP C 1 27 ? 13.731  -29.308 29.379  1.00 60.29  ? 26  ASP C CG  1 
ATOM   1685 O OD1 . ASP C 1 27 ? 13.219  -28.326 28.792  1.00 64.16  ? 26  ASP C OD1 1 
ATOM   1686 O OD2 . ASP C 1 27 ? 13.217  -30.452 29.409  1.00 57.25  ? 26  ASP C OD2 1 
ATOM   1687 N N   . LYS C 1 35 ? 18.711  -36.662 37.882  1.00 90.48  ? 34  LYS C N   1 
ATOM   1688 C CA  . LYS C 1 35 ? 20.073  -36.067 37.794  1.00 86.77  ? 34  LYS C CA  1 
ATOM   1689 C C   . LYS C 1 35 ? 20.718  -36.465 36.461  1.00 87.46  ? 34  LYS C C   1 
ATOM   1690 O O   . LYS C 1 35 ? 20.762  -37.648 36.108  1.00 80.11  ? 34  LYS C O   1 
ATOM   1691 C CB  . LYS C 1 35 ? 20.907  -36.407 39.039  1.00 76.09  ? 34  LYS C CB  1 
ATOM   1692 N N   . PRO C 1 36 ? 21.242  -35.488 35.676  1.00 87.07  ? 35  PRO C N   1 
ATOM   1693 C CA  . PRO C 1 36 ? 21.819  -35.776 34.357  1.00 83.54  ? 35  PRO C CA  1 
ATOM   1694 C C   . PRO C 1 36 ? 23.115  -36.584 34.459  1.00 93.30  ? 35  PRO C C   1 
ATOM   1695 O O   . PRO C 1 36 ? 23.918  -36.339 35.363  1.00 92.72  ? 35  PRO C O   1 
ATOM   1696 C CB  . PRO C 1 36 ? 22.064  -34.384 33.718  1.00 74.41  ? 35  PRO C CB  1 
ATOM   1697 C CG  . PRO C 1 36 ? 21.493  -33.371 34.690  1.00 74.43  ? 35  PRO C CG  1 
ATOM   1698 C CD  . PRO C 1 36 ? 21.337  -34.060 36.036  1.00 80.78  ? 35  PRO C CD  1 
ATOM   1699 N N   . PRO C 1 37 ? 23.372  -37.565 33.554  1.00 88.35  ? 36  PRO C N   1 
ATOM   1700 C CA  . PRO C 1 37 ? 24.695  -38.187 33.457  1.00 83.50  ? 36  PRO C CA  1 
ATOM   1701 C C   . PRO C 1 37 ? 25.771  -37.102 33.530  1.00 76.77  ? 36  PRO C C   1 
ATOM   1702 O O   . PRO C 1 37 ? 25.531  -35.970 33.115  1.00 71.54  ? 36  PRO C O   1 
ATOM   1703 C CB  . PRO C 1 37 ? 24.651  -38.908 32.096  1.00 84.27  ? 36  PRO C CB  1 
ATOM   1704 C CG  . PRO C 1 37 ? 23.186  -39.242 31.893  1.00 85.16  ? 36  PRO C CG  1 
ATOM   1705 C CD  . PRO C 1 37 ? 22.407  -38.143 32.605  1.00 86.08  ? 36  PRO C CD  1 
ATOM   1706 N N   . PRO C 1 38 ? 26.973  -37.400 34.083  1.00 71.18  ? 37  PRO C N   1 
ATOM   1707 C CA  . PRO C 1 38 ? 27.979  -36.373 34.374  1.00 61.20  ? 37  PRO C CA  1 
ATOM   1708 C C   . PRO C 1 38 ? 28.397  -35.495 33.201  1.00 58.08  ? 37  PRO C C   1 
ATOM   1709 O O   . PRO C 1 38 ? 28.903  -35.983 32.190  1.00 62.31  ? 37  PRO C O   1 
ATOM   1710 C CB  . PRO C 1 38 ? 29.167  -37.155 34.938  1.00 66.41  ? 37  PRO C CB  1 
ATOM   1711 C CG  . PRO C 1 38 ? 28.536  -38.424 35.444  1.00 71.81  ? 37  PRO C CG  1 
ATOM   1712 C CD  . PRO C 1 38 ? 27.419  -38.747 34.464  1.00 70.82  ? 37  PRO C CD  1 
ATOM   1713 N N   . ASN C 1 39 ? 28.180  -34.189 33.392  1.00 55.46  ? 38  ASN C N   1 
ATOM   1714 C CA  . ASN C 1 39 ? 28.500  -33.124 32.455  1.00 57.21  ? 38  ASN C CA  1 
ATOM   1715 C C   . ASN C 1 39 ? 27.573  -33.149 31.235  1.00 47.98  ? 38  ASN C C   1 
ATOM   1716 O O   . ASN C 1 39 ? 27.983  -32.710 30.157  1.00 48.21  ? 38  ASN C O   1 
ATOM   1717 C CB  . ASN C 1 39 ? 29.980  -33.090 32.093  1.00 58.52  ? 38  ASN C CB  1 
ATOM   1718 C CG  . ASN C 1 39 ? 30.358  -31.773 31.460  1.00 69.80  ? 38  ASN C CG  1 
ATOM   1719 O OD1 . ASN C 1 39 ? 29.764  -30.730 31.773  1.00 69.14  ? 38  ASN C OD1 1 
ATOM   1720 N ND2 . ASN C 1 39 ? 31.350  -31.799 30.581  1.00 68.46  ? 38  ASN C ND2 1 
ATOM   1721 N N   . LYS C 1 40 ? 26.343  -33.654 31.432  1.00 45.37  ? 39  LYS C N   1 
ATOM   1722 C CA  . LYS C 1 40 ? 25.285  -33.675 30.425  1.00 45.23  ? 39  LYS C CA  1 
ATOM   1723 C C   . LYS C 1 40 ? 24.195  -32.674 30.824  1.00 48.06  ? 39  LYS C C   1 
ATOM   1724 O O   . LYS C 1 40 ? 23.784  -32.610 31.985  1.00 45.53  ? 39  LYS C O   1 
ATOM   1725 C CB  . LYS C 1 40 ? 24.625  -35.055 30.260  1.00 46.57  ? 39  LYS C CB  1 
ATOM   1726 C CG  . LYS C 1 40 ? 25.456  -36.291 29.900  1.00 40.56  ? 39  LYS C CG  1 
ATOM   1727 C CD  . LYS C 1 40 ? 26.198  -36.238 28.577  1.00 47.54  ? 39  LYS C CD  1 
ATOM   1728 C CE  . LYS C 1 40 ? 26.987  -37.495 28.390  1.00 50.22  ? 39  LYS C CE  1 
ATOM   1729 N NZ  . LYS C 1 40 ? 28.034  -37.349 27.377  1.00 50.42  ? 39  LYS C NZ  1 
ATOM   1730 N N   . TYR C 1 41 ? 23.747  -31.871 29.848  1.00 41.99  ? 40  TYR C N   1 
ATOM   1731 C CA  . TYR C 1 41 ? 22.626  -30.949 29.994  1.00 39.46  ? 40  TYR C CA  1 
ATOM   1732 C C   . TYR C 1 41 ? 21.333  -31.662 29.592  1.00 40.84  ? 40  TYR C C   1 
ATOM   1733 O O   . TYR C 1 41 ? 21.345  -32.535 28.700  1.00 35.89  ? 40  TYR C O   1 
ATOM   1734 C CB  . TYR C 1 41 ? 22.860  -29.723 29.096  1.00 38.52  ? 40  TYR C CB  1 
ATOM   1735 C CG  . TYR C 1 41 ? 24.071  -28.867 29.467  1.00 44.66  ? 40  TYR C CG  1 
ATOM   1736 C CD1 . TYR C 1 41 ? 25.360  -29.225 29.084  1.00 43.37  ? 40  TYR C CD1 1 
ATOM   1737 C CD2 . TYR C 1 41 ? 23.926  -27.694 30.197  1.00 46.34  ? 40  TYR C CD2 1 
ATOM   1738 C CE1 . TYR C 1 41 ? 26.462  -28.450 29.406  1.00 53.15  ? 40  TYR C CE1 1 
ATOM   1739 C CE2 . TYR C 1 41 ? 25.016  -26.895 30.502  1.00 52.81  ? 40  TYR C CE2 1 
ATOM   1740 C CZ  . TYR C 1 41 ? 26.286  -27.274 30.113  1.00 57.61  ? 40  TYR C CZ  1 
ATOM   1741 O OH  . TYR C 1 41 ? 27.357  -26.492 30.444  1.00 67.26  ? 40  TYR C OH  1 
ATOM   1742 N N   . PRO C 1 42 ? 20.175  -31.311 30.221  1.00 44.31  ? 41  PRO C N   1 
ATOM   1743 C CA  . PRO C 1 42 ? 18.883  -31.843 29.793  1.00 39.57  ? 41  PRO C CA  1 
ATOM   1744 C C   . PRO C 1 42 ? 18.434  -30.981 28.620  1.00 34.60  ? 41  PRO C C   1 
ATOM   1745 O O   . PRO C 1 42 ? 18.316  -29.777 28.769  1.00 38.56  ? 41  PRO C O   1 
ATOM   1746 C CB  . PRO C 1 42 ? 18.000  -31.674 31.035  1.00 40.15  ? 41  PRO C CB  1 
ATOM   1747 C CG  . PRO C 1 42 ? 18.584  -30.481 31.748  1.00 40.52  ? 41  PRO C CG  1 
ATOM   1748 C CD  . PRO C 1 42 ? 20.052  -30.401 31.378  1.00 39.00  ? 41  PRO C CD  1 
ATOM   1749 N N   . ILE C 1 43 ? 18.173  -31.606 27.475  1.00 37.27  ? 42  ILE C N   1 
ATOM   1750 C CA  . ILE C 1 43 ? 17.912  -30.882 26.232  1.00 34.09  ? 42  ILE C CA  1 
ATOM   1751 C C   . ILE C 1 43 ? 16.486  -31.165 25.781  1.00 35.25  ? 42  ILE C C   1 
ATOM   1752 O O   . ILE C 1 43 ? 16.057  -32.328 25.779  1.00 39.22  ? 42  ILE C O   1 
ATOM   1753 C CB  . ILE C 1 43 ? 18.924  -31.284 25.137  1.00 33.27  ? 42  ILE C CB  1 
ATOM   1754 C CG1 . ILE C 1 43 ? 20.385  -31.005 25.571  1.00 33.00  ? 42  ILE C CG1 1 
ATOM   1755 C CG2 . ILE C 1 43 ? 18.556  -30.707 23.757  1.00 26.56  ? 42  ILE C CG2 1 
ATOM   1756 C CD1 . ILE C 1 43 ? 20.671  -29.602 26.068  1.00 30.43  ? 42  ILE C CD1 1 
ATOM   1757 N N   . PHE C 1 44 ? 15.765  -30.082 25.432  1.00 34.38  ? 43  PHE C N   1 
ATOM   1758 C CA  . PHE C 1 44 ? 14.432  -30.143 24.831  1.00 32.23  ? 43  PHE C CA  1 
ATOM   1759 C C   . PHE C 1 44 ? 14.567  -29.755 23.364  1.00 27.97  ? 43  PHE C C   1 
ATOM   1760 O O   . PHE C 1 44 ? 15.041  -28.668 23.055  1.00 25.33  ? 43  PHE C O   1 
ATOM   1761 C CB  . PHE C 1 44 ? 13.390  -29.222 25.487  1.00 33.91  ? 43  PHE C CB  1 
ATOM   1762 C CG  . PHE C 1 44 ? 12.003  -29.218 24.841  1.00 43.38  ? 43  PHE C CG  1 
ATOM   1763 C CD1 . PHE C 1 44 ? 11.044  -30.186 25.175  1.00 43.70  ? 43  PHE C CD1 1 
ATOM   1764 C CD2 . PHE C 1 44 ? 11.639  -28.235 23.910  1.00 41.91  ? 43  PHE C CD2 1 
ATOM   1765 C CE1 . PHE C 1 44 ? 9.776   -30.185 24.595  1.00 46.83  ? 43  PHE C CE1 1 
ATOM   1766 C CE2 . PHE C 1 44 ? 10.372  -28.242 23.319  1.00 42.42  ? 43  PHE C CE2 1 
ATOM   1767 C CZ  . PHE C 1 44 ? 9.445   -29.221 23.649  1.00 45.86  ? 43  PHE C CZ  1 
ATOM   1768 N N   . PHE C 1 45 ? 14.144  -30.647 22.479  1.00 30.18  ? 44  PHE C N   1 
ATOM   1769 C CA  . PHE C 1 45 ? 14.292  -30.447 21.050  1.00 31.70  ? 44  PHE C CA  1 
ATOM   1770 C C   . PHE C 1 45 ? 12.998  -29.880 20.482  1.00 34.80  ? 44  PHE C C   1 
ATOM   1771 O O   . PHE C 1 45 ? 11.929  -30.456 20.651  1.00 40.88  ? 44  PHE C O   1 
ATOM   1772 C CB  . PHE C 1 45 ? 14.527  -31.785 20.343  1.00 31.93  ? 44  PHE C CB  1 
ATOM   1773 C CG  . PHE C 1 45 ? 15.879  -32.395 20.685  1.00 35.34  ? 44  PHE C CG  1 
ATOM   1774 C CD1 . PHE C 1 45 ? 16.958  -32.238 19.824  1.00 31.00  ? 44  PHE C CD1 1 
ATOM   1775 C CD2 . PHE C 1 45 ? 16.057  -33.137 21.854  1.00 33.59  ? 44  PHE C CD2 1 
ATOM   1776 C CE1 . PHE C 1 45 ? 18.196  -32.784 20.135  1.00 30.97  ? 44  PHE C CE1 1 
ATOM   1777 C CE2 . PHE C 1 45 ? 17.306  -33.681 22.150  1.00 37.52  ? 44  PHE C CE2 1 
ATOM   1778 C CZ  . PHE C 1 45 ? 18.367  -33.502 21.286  1.00 28.39  ? 44  PHE C CZ  1 
ATOM   1779 N N   . PHE C 1 46 ? 13.114  -28.748 19.794  1.00 34.06  ? 45  PHE C N   1 
ATOM   1780 C CA  . PHE C 1 46 ? 11.962  -28.136 19.154  1.00 38.09  ? 45  PHE C CA  1 
ATOM   1781 C C   . PHE C 1 46 ? 11.425  -29.062 18.060  1.00 38.38  ? 45  PHE C C   1 
ATOM   1782 O O   . PHE C 1 46 ? 12.184  -29.848 17.483  1.00 34.84  ? 45  PHE C O   1 
ATOM   1783 C CB  . PHE C 1 46 ? 12.275  -26.700 18.706  1.00 34.29  ? 45  PHE C CB  1 
ATOM   1784 C CG  . PHE C 1 46 ? 12.494  -25.736 19.864  1.00 33.42  ? 45  PHE C CG  1 
ATOM   1785 C CD1 . PHE C 1 46 ? 11.428  -25.312 20.650  1.00 32.02  ? 45  PHE C CD1 1 
ATOM   1786 C CD2 . PHE C 1 46 ? 13.771  -25.263 20.171  1.00 33.69  ? 45  PHE C CD2 1 
ATOM   1787 C CE1 . PHE C 1 46 ? 11.635  -24.436 21.710  1.00 35.37  ? 45  PHE C CE1 1 
ATOM   1788 C CE2 . PHE C 1 46 ? 13.968  -24.377 21.225  1.00 32.94  ? 45  PHE C CE2 1 
ATOM   1789 C CZ  . PHE C 1 46 ? 12.903  -23.977 22.008  1.00 32.57  ? 45  PHE C CZ  1 
ATOM   1790 N N   . GLY C 1 47 ? 10.114  -28.923 17.775  1.00 36.51  ? 46  GLY C N   1 
ATOM   1791 C CA  . GLY C 1 47 ? 9.470   -29.645 16.682  1.00 39.49  ? 46  GLY C CA  1 
ATOM   1792 C C   . GLY C 1 47 ? 8.976   -31.024 17.114  1.00 47.38  ? 46  GLY C C   1 
ATOM   1793 O O   . GLY C 1 47 ? 7.769   -31.269 17.114  1.00 45.76  ? 46  GLY C O   1 
ATOM   1794 N N   . THR C 1 48 ? 9.922   -31.898 17.503  1.00 46.09  ? 47  THR C N   1 
ATOM   1795 C CA  . THR C 1 48 ? 9.643   -33.256 17.944  1.00 39.87  ? 47  THR C CA  1 
ATOM   1796 C C   . THR C 1 48 ? 9.143   -33.228 19.382  1.00 40.18  ? 47  THR C C   1 
ATOM   1797 O O   . THR C 1 48 ? 8.309   -34.043 19.773  1.00 45.69  ? 47  THR C O   1 
ATOM   1798 C CB  . THR C 1 48 ? 10.918  -34.085 17.809  1.00 37.71  ? 47  THR C CB  1 
ATOM   1799 O OG1 . THR C 1 48 ? 11.876  -33.644 18.781  1.00 36.69  ? 47  THR C OG1 1 
ATOM   1800 C CG2 . THR C 1 48 ? 11.437  -34.036 16.392  1.00 34.88  ? 47  THR C CG2 1 
ATOM   1801 N N   . HIS C 1 49 ? 9.677   -32.283 20.163  1.00 46.86  ? 48  HIS C N   1 
ATOM   1802 C CA  . HIS C 1 49 ? 9.348   -32.088 21.570  1.00 49.12  ? 48  HIS C CA  1 
ATOM   1803 C C   . HIS C 1 49 ? 9.962   -33.188 22.438  1.00 47.99  ? 48  HIS C C   1 
ATOM   1804 O O   . HIS C 1 49 ? 9.474   -33.460 23.534  1.00 45.74  ? 48  HIS C O   1 
ATOM   1805 C CB  . HIS C 1 49 ? 7.843   -31.844 21.770  1.00 54.56  ? 48  HIS C CB  1 
ATOM   1806 C CG  . HIS C 1 49 ? 7.314   -30.723 20.935  1.00 58.46  ? 48  HIS C CG  1 
ATOM   1807 N ND1 . HIS C 1 49 ? 6.251   -30.877 20.068  1.00 61.44  ? 48  HIS C ND1 1 
ATOM   1808 C CD2 . HIS C 1 49 ? 7.745   -29.468 20.775  1.00 57.42  ? 48  HIS C CD2 1 
ATOM   1809 C CE1 . HIS C 1 49 ? 6.032   -29.731 19.442  1.00 63.98  ? 48  HIS C CE1 1 
ATOM   1810 N NE2 . HIS C 1 49 ? 6.927   -28.860 19.859  1.00 64.48  ? 48  HIS C NE2 1 
ATOM   1811 N N   . GLU C 1 50 ? 11.064  -33.783 21.967  1.00 45.81  ? 49  GLU C N   1 
ATOM   1812 C CA  . GLU C 1 50 ? 11.717  -34.818 22.747  1.00 53.61  ? 49  GLU C CA  1 
ATOM   1813 C C   . GLU C 1 50 ? 12.805  -34.212 23.640  1.00 48.08  ? 49  GLU C C   1 
ATOM   1814 O O   . GLU C 1 50 ? 13.189  -33.056 23.478  1.00 43.82  ? 49  GLU C O   1 
ATOM   1815 C CB  . GLU C 1 50 ? 12.140  -35.964 21.829  1.00 55.28  ? 49  GLU C CB  1 
ATOM   1816 C CG  . GLU C 1 50 ? 10.943  -36.718 21.251  1.00 55.37  ? 49  GLU C CG  1 
ATOM   1817 C CD  . GLU C 1 50 ? 11.289  -37.604 20.063  1.00 61.70  ? 49  GLU C CD  1 
ATOM   1818 O OE1 . GLU C 1 50 ? 12.481  -37.836 19.752  1.00 59.92  ? 49  GLU C OE1 1 
ATOM   1819 O OE2 . GLU C 1 50 ? 10.333  -38.051 19.409  1.00 69.55  ? 49  GLU C OE2 1 
ATOM   1820 N N   . THR C 1 51 ? 13.247  -35.004 24.621  1.00 51.16  ? 50  THR C N   1 
ATOM   1821 C CA  . THR C 1 51 ? 14.347  -34.662 25.515  1.00 52.75  ? 50  THR C CA  1 
ATOM   1822 C C   . THR C 1 51 ? 15.454  -35.719 25.390  1.00 50.86  ? 50  THR C C   1 
ATOM   1823 O O   . THR C 1 51 ? 15.207  -36.878 25.026  1.00 46.50  ? 50  THR C O   1 
ATOM   1824 C CB  . THR C 1 51 ? 13.854  -34.468 26.952  1.00 57.28  ? 50  THR C CB  1 
ATOM   1825 O OG1 . THR C 1 51 ? 13.059  -35.632 27.146  1.00 54.17  ? 50  THR C OG1 1 
ATOM   1826 C CG2 . THR C 1 51 ? 13.015  -33.214 27.150  1.00 50.60  ? 50  THR C CG2 1 
ATOM   1827 N N   . ALA C 1 52 ? 16.689  -35.268 25.629  1.00 40.71  ? 51  ALA C N   1 
ATOM   1828 C CA  . ALA C 1 52 ? 17.874  -36.108 25.685  1.00 41.03  ? 51  ALA C CA  1 
ATOM   1829 C C   . ALA C 1 52 ? 18.907  -35.423 26.576  1.00 43.25  ? 51  ALA C C   1 
ATOM   1830 O O   . ALA C 1 52 ? 18.744  -34.253 26.921  1.00 40.91  ? 51  ALA C O   1 
ATOM   1831 C CB  . ALA C 1 52 ? 18.418  -36.321 24.286  1.00 42.05  ? 51  ALA C CB  1 
ATOM   1832 N N   . PHE C 1 53 ? 19.961  -36.160 26.954  1.00 44.28  ? 52  PHE C N   1 
ATOM   1833 C CA  . PHE C 1 53 ? 21.078  -35.586 27.683  1.00 37.88  ? 52  PHE C CA  1 
ATOM   1834 C C   . PHE C 1 53 ? 22.229  -35.382 26.721  1.00 38.82  ? 52  PHE C C   1 
ATOM   1835 O O   . PHE C 1 53 ? 22.566  -36.283 25.974  1.00 40.86  ? 52  PHE C O   1 
ATOM   1836 C CB  . PHE C 1 53 ? 21.538  -36.522 28.794  1.00 40.38  ? 52  PHE C CB  1 
ATOM   1837 C CG  . PHE C 1 53 ? 20.622  -36.375 29.991  1.00 41.44  ? 52  PHE C CG  1 
ATOM   1838 C CD1 . PHE C 1 53 ? 20.410  -35.125 30.563  1.00 43.52  ? 52  PHE C CD1 1 
ATOM   1839 C CD2 . PHE C 1 53 ? 19.924  -37.465 30.495  1.00 43.29  ? 52  PHE C CD2 1 
ATOM   1840 C CE1 . PHE C 1 53 ? 19.551  -34.986 31.638  1.00 41.39  ? 52  PHE C CE1 1 
ATOM   1841 C CE2 . PHE C 1 53 ? 19.070  -37.317 31.578  1.00 45.48  ? 52  PHE C CE2 1 
ATOM   1842 C CZ  . PHE C 1 53 ? 18.889  -36.081 32.149  1.00 42.73  ? 52  PHE C CZ  1 
ATOM   1843 N N   . LEU C 1 54 ? 22.814  -34.190 26.741  1.00 37.24  ? 53  LEU C N   1 
ATOM   1844 C CA  . LEU C 1 54 ? 23.899  -33.944 25.811  1.00 39.22  ? 53  LEU C CA  1 
ATOM   1845 C C   . LEU C 1 54 ? 25.027  -33.252 26.567  1.00 36.98  ? 53  LEU C C   1 
ATOM   1846 O O   . LEU C 1 54 ? 24.754  -32.470 27.467  1.00 31.75  ? 53  LEU C O   1 
ATOM   1847 C CB  . LEU C 1 54 ? 23.445  -33.163 24.567  1.00 34.88  ? 53  LEU C CB  1 
ATOM   1848 C CG  . LEU C 1 54 ? 22.687  -33.942 23.476  1.00 34.71  ? 53  LEU C CG  1 
ATOM   1849 C CD1 . LEU C 1 54 ? 22.435  -33.072 22.229  1.00 25.26  ? 53  LEU C CD1 1 
ATOM   1850 C CD2 . LEU C 1 54 ? 23.392  -35.236 23.054  1.00 36.56  ? 53  LEU C CD2 1 
ATOM   1851 N N   . GLY C 1 55 ? 26.277  -33.577 26.197  1.00 43.55  ? 54  GLY C N   1 
ATOM   1852 C CA  . GLY C 1 55 ? 27.476  -32.887 26.656  1.00 39.66  ? 54  GLY C CA  1 
ATOM   1853 C C   . GLY C 1 55 ? 27.612  -31.558 25.912  1.00 45.03  ? 54  GLY C C   1 
ATOM   1854 O O   . GLY C 1 55 ? 27.000  -31.386 24.853  1.00 41.40  ? 54  GLY C O   1 
ATOM   1855 N N   . PRO C 1 56 ? 28.370  -30.562 26.433  1.00 42.78  ? 55  PRO C N   1 
ATOM   1856 C CA  . PRO C 1 56 ? 28.437  -29.259 25.775  1.00 41.49  ? 55  PRO C CA  1 
ATOM   1857 C C   . PRO C 1 56 ? 29.064  -29.360 24.387  1.00 42.81  ? 55  PRO C C   1 
ATOM   1858 O O   . PRO C 1 56 ? 28.880  -28.459 23.565  1.00 48.83  ? 55  PRO C O   1 
ATOM   1859 C CB  . PRO C 1 56 ? 29.201  -28.341 26.752  1.00 42.60  ? 55  PRO C CB  1 
ATOM   1860 C CG  . PRO C 1 56 ? 29.892  -29.291 27.706  1.00 39.95  ? 55  PRO C CG  1 
ATOM   1861 C CD  . PRO C 1 56 ? 29.147  -30.618 27.686  1.00 45.24  ? 55  PRO C CD  1 
ATOM   1862 N N   . LYS C 1 57 ? 29.762  -30.482 24.126  1.00 37.11  ? 56  LYS C N   1 
ATOM   1863 C CA  . LYS C 1 57 ? 30.450  -30.736 22.867  1.00 37.93  ? 56  LYS C CA  1 
ATOM   1864 C C   . LYS C 1 57 ? 29.441  -30.826 21.717  1.00 36.83  ? 56  LYS C C   1 
ATOM   1865 O O   . LYS C 1 57 ? 29.755  -30.579 20.551  1.00 33.79  ? 56  LYS C O   1 
ATOM   1866 C CB  . LYS C 1 57 ? 31.413  -31.936 22.982  1.00 45.70  ? 56  LYS C CB  1 
ATOM   1867 C CG  . LYS C 1 57 ? 30.950  -33.381 22.673  1.00 40.58  ? 56  LYS C CG  1 
ATOM   1868 N NZ  . LYS C 1 57 ? 35.471  -33.712 21.562  1.00 46.53  ? 56  LYS C NZ  1 
ATOM   1869 N N   . ASP C 1 58 ? 28.212  -31.191 22.054  1.00 36.76  ? 57  ASP C N   1 
ATOM   1870 C CA  . ASP C 1 58 ? 27.194  -31.367 21.033  1.00 40.78  ? 57  ASP C CA  1 
ATOM   1871 C C   . ASP C 1 58 ? 26.277  -30.153 21.007  1.00 36.44  ? 57  ASP C C   1 
ATOM   1872 O O   . ASP C 1 58 ? 25.219  -30.226 20.394  1.00 35.09  ? 57  ASP C O   1 
ATOM   1873 C CB  . ASP C 1 58 ? 26.275  -32.530 21.367  1.00 41.97  ? 57  ASP C CB  1 
ATOM   1874 C CG  . ASP C 1 58 ? 27.002  -33.803 21.741  1.00 44.65  ? 57  ASP C CG  1 
ATOM   1875 O OD1 . ASP C 1 58 ? 27.782  -34.270 20.900  1.00 47.28  ? 57  ASP C OD1 1 
ATOM   1876 O OD2 . ASP C 1 58 ? 26.779  -34.288 22.872  1.00 59.31  ? 57  ASP C OD2 1 
ATOM   1877 N N   . LEU C 1 59 ? 26.663  -29.085 21.722  1.00 34.41  ? 58  LEU C N   1 
ATOM   1878 C CA  . LEU C 1 59 ? 25.739  -27.990 21.964  1.00 34.12  ? 58  LEU C CA  1 
ATOM   1879 C C   . LEU C 1 59 ? 26.334  -26.705 21.401  1.00 38.13  ? 58  LEU C C   1 
ATOM   1880 O O   . LEU C 1 59 ? 27.468  -26.361 21.697  1.00 36.47  ? 58  LEU C O   1 
ATOM   1881 C CB  . LEU C 1 59 ? 25.402  -27.871 23.451  1.00 32.58  ? 58  LEU C CB  1 
ATOM   1882 C CG  . LEU C 1 59 ? 24.554  -28.988 24.072  1.00 29.12  ? 58  LEU C CG  1 
ATOM   1883 C CD1 . LEU C 1 59 ? 24.346  -28.661 25.558  1.00 29.15  ? 58  LEU C CD1 1 
ATOM   1884 C CD2 . LEU C 1 59 ? 23.235  -29.213 23.380  1.00 27.45  ? 58  LEU C CD2 1 
ATOM   1885 N N   . PHE C 1 60 ? 25.571  -26.020 20.542  1.00 41.63  ? 59  PHE C N   1 
ATOM   1886 C CA  . PHE C 1 60 ? 26.067  -24.795 19.936  1.00 41.89  ? 59  PHE C CA  1 
ATOM   1887 C C   . PHE C 1 60 ? 25.041  -23.706 20.212  1.00 45.12  ? 59  PHE C C   1 
ATOM   1888 O O   . PHE C 1 60 ? 23.852  -23.974 20.110  1.00 47.53  ? 59  PHE C O   1 
ATOM   1889 C CB  . PHE C 1 60 ? 26.245  -25.015 18.434  1.00 38.48  ? 59  PHE C CB  1 
ATOM   1890 C CG  . PHE C 1 60 ? 27.104  -26.223 18.114  1.00 36.90  ? 59  PHE C CG  1 
ATOM   1891 C CD1 . PHE C 1 60 ? 26.544  -27.501 18.079  1.00 34.89  ? 59  PHE C CD1 1 
ATOM   1892 C CD2 . PHE C 1 60 ? 28.473  -26.071 17.865  1.00 37.41  ? 59  PHE C CD2 1 
ATOM   1893 C CE1 . PHE C 1 60 ? 27.337  -28.609 17.807  1.00 34.03  ? 59  PHE C CE1 1 
ATOM   1894 C CE2 . PHE C 1 60 ? 29.259  -27.176 17.580  1.00 34.69  ? 59  PHE C CE2 1 
ATOM   1895 C CZ  . PHE C 1 60 ? 28.682  -28.439 17.546  1.00 36.53  ? 59  PHE C CZ  1 
ATOM   1896 N N   . PRO C 1 61 ? 25.445  -22.465 20.568  1.00 44.85  ? 60  PRO C N   1 
ATOM   1897 C CA  . PRO C 1 61 ? 24.466  -21.458 20.970  1.00 45.59  ? 60  PRO C CA  1 
ATOM   1898 C C   . PRO C 1 61 ? 23.724  -21.061 19.696  1.00 41.14  ? 60  PRO C C   1 
ATOM   1899 O O   . PRO C 1 61 ? 24.333  -21.034 18.622  1.00 43.32  ? 60  PRO C O   1 
ATOM   1900 C CB  . PRO C 1 61 ? 25.388  -20.367 21.559  1.00 51.20  ? 60  PRO C CB  1 
ATOM   1901 C CG  . PRO C 1 61 ? 26.725  -21.074 21.796  1.00 44.88  ? 60  PRO C CG  1 
ATOM   1902 C CD  . PRO C 1 61 ? 26.830  -21.964 20.579  1.00 46.86  ? 60  PRO C CD  1 
ATOM   1903 N N   . TYR C 1 62 ? 22.412  -20.813 19.827  1.00 37.96  ? 61  TYR C N   1 
ATOM   1904 C CA  . TYR C 1 62 ? 21.510  -20.538 18.717  1.00 38.82  ? 61  TYR C CA  1 
ATOM   1905 C C   . TYR C 1 62 ? 22.001  -19.351 17.907  1.00 43.86  ? 61  TYR C C   1 
ATOM   1906 O O   . TYR C 1 62 ? 22.222  -19.497 16.706  1.00 38.42  ? 61  TYR C O   1 
ATOM   1907 C CB  . TYR C 1 62 ? 20.064  -20.247 19.143  1.00 40.73  ? 61  TYR C CB  1 
ATOM   1908 C CG  . TYR C 1 62 ? 19.076  -19.875 18.044  1.00 35.81  ? 61  TYR C CG  1 
ATOM   1909 C CD1 . TYR C 1 62 ? 18.765  -20.769 17.022  1.00 35.65  ? 61  TYR C CD1 1 
ATOM   1910 C CD2 . TYR C 1 62 ? 18.382  -18.664 18.076  1.00 37.06  ? 61  TYR C CD2 1 
ATOM   1911 C CE1 . TYR C 1 62 ? 17.846  -20.456 16.023  1.00 32.75  ? 61  TYR C CE1 1 
ATOM   1912 C CE2 . TYR C 1 62 ? 17.442  -18.349 17.099  1.00 35.12  ? 61  TYR C CE2 1 
ATOM   1913 C CZ  . TYR C 1 62 ? 17.175  -19.243 16.072  1.00 33.44  ? 61  TYR C CZ  1 
ATOM   1914 O OH  . TYR C 1 62 ? 16.283  -18.936 15.088  1.00 36.45  ? 61  TYR C OH  1 
ATOM   1915 N N   . ASP C 1 63 ? 22.140  -18.191 18.571  1.00 45.97  ? 62  ASP C N   1 
ATOM   1916 C CA  . ASP C 1 63 ? 22.560  -16.960 17.916  1.00 48.51  ? 62  ASP C CA  1 
ATOM   1917 C C   . ASP C 1 63 ? 23.906  -17.118 17.210  1.00 42.98  ? 62  ASP C C   1 
ATOM   1918 O O   . ASP C 1 63 ? 24.040  -16.703 16.058  1.00 48.06  ? 62  ASP C O   1 
ATOM   1919 C CB  . ASP C 1 63 ? 22.519  -15.761 18.849  1.00 53.95  ? 62  ASP C CB  1 
ATOM   1920 C CG  . ASP C 1 63 ? 21.243  -14.935 18.780  1.00 59.53  ? 62  ASP C CG  1 
ATOM   1921 O OD1 . ASP C 1 63 ? 20.492  -14.930 19.777  1.00 62.87  ? 62  ASP C OD1 1 
ATOM   1922 O OD2 . ASP C 1 63 ? 21.014  -14.299 17.731  1.00 62.53  ? 62  ASP C OD2 1 
ATOM   1923 N N   . LYS C 1 64 ? 24.889  -17.720 17.888  1.00 42.26  ? 63  LYS C N   1 
ATOM   1924 C CA  . LYS C 1 64 ? 26.235  -17.845 17.342  1.00 40.50  ? 63  LYS C CA  1 
ATOM   1925 C C   . LYS C 1 64 ? 26.233  -18.706 16.070  1.00 39.28  ? 63  LYS C C   1 
ATOM   1926 O O   . LYS C 1 64 ? 27.016  -18.426 15.160  1.00 37.89  ? 63  LYS C O   1 
ATOM   1927 C CB  . LYS C 1 64 ? 27.278  -18.246 18.401  1.00 36.04  ? 63  LYS C CB  1 
ATOM   1928 N N   . SER C 1 65 ? 25.336  -19.720 15.980  1.00 38.91  ? 64  SER C N   1 
ATOM   1929 C CA  . SER C 1 65 ? 25.513  -20.824 15.032  1.00 40.81  ? 64  SER C CA  1 
ATOM   1930 C C   . SER C 1 65 ? 24.375  -20.998 14.009  1.00 40.72  ? 64  SER C C   1 
ATOM   1931 O O   . SER C 1 65 ? 24.466  -21.880 13.149  1.00 39.03  ? 64  SER C O   1 
ATOM   1932 C CB  . SER C 1 65 ? 25.787  -22.110 15.759  1.00 36.24  ? 64  SER C CB  1 
ATOM   1933 O OG  . SER C 1 65 ? 24.593  -22.521 16.403  1.00 36.01  ? 64  SER C OG  1 
ATOM   1934 N N   . LYS C 1 66 ? 23.329  -20.156 14.086  1.00 36.30  ? 65  LYS C N   1 
ATOM   1935 C CA  . LYS C 1 66 ? 22.077  -20.369 13.381  1.00 34.57  ? 65  LYS C CA  1 
ATOM   1936 C C   . LYS C 1 66 ? 22.260  -20.092 11.894  1.00 31.91  ? 65  LYS C C   1 
ATOM   1937 O O   . LYS C 1 66 ? 21.492  -20.596 11.078  1.00 38.45  ? 65  LYS C O   1 
ATOM   1938 C CB  . LYS C 1 66 ? 20.877  -19.584 13.928  1.00 37.42  ? 65  LYS C CB  1 
ATOM   1939 C CG  . LYS C 1 66 ? 20.912  -18.083 13.735  1.00 40.24  ? 65  LYS C CG  1 
ATOM   1940 C CD  . LYS C 1 66 ? 19.862  -17.284 14.499  1.00 45.61  ? 65  LYS C CD  1 
ATOM   1941 C CE  . LYS C 1 66 ? 19.814  -15.874 13.998  1.00 49.27  ? 65  LYS C CE  1 
ATOM   1942 N NZ  . LYS C 1 66 ? 19.546  -14.981 15.125  1.00 51.90  ? 65  LYS C NZ  1 
ATOM   1943 N N   . ASP C 1 67 ? 23.281  -19.299 11.556  1.00 35.67  ? 66  ASP C N   1 
ATOM   1944 C CA  . ASP C 1 67 ? 23.653  -19.094 10.157  1.00 43.24  ? 66  ASP C CA  1 
ATOM   1945 C C   . ASP C 1 67 ? 24.041  -20.437 9.535   1.00 40.34  ? 66  ASP C C   1 
ATOM   1946 O O   . ASP C 1 67 ? 23.782  -20.701 8.362   1.00 40.79  ? 66  ASP C O   1 
ATOM   1947 C CB  . ASP C 1 67 ? 24.614  -17.921 9.961   1.00 45.41  ? 66  ASP C CB  1 
ATOM   1948 C CG  . ASP C 1 67 ? 26.057  -18.077 10.433  1.00 58.51  ? 66  ASP C CG  1 
ATOM   1949 O OD1 . ASP C 1 67 ? 26.549  -19.228 10.537  1.00 70.46  ? 66  ASP C OD1 1 
ATOM   1950 O OD2 . ASP C 1 67 ? 26.693  -17.038 10.706  1.00 57.14  ? 66  ASP C OD2 1 
ATOM   1951 N N   . LYS C 1 68 ? 24.646  -21.297 10.357  1.00 36.79  ? 67  LYS C N   1 
ATOM   1952 C CA  . LYS C 1 68 ? 25.218  -22.534 9.869   1.00 36.65  ? 67  LYS C CA  1 
ATOM   1953 C C   . LYS C 1 68 ? 24.155  -23.635 9.931   1.00 36.85  ? 67  LYS C C   1 
ATOM   1954 O O   . LYS C 1 68 ? 23.980  -24.358 8.958   1.00 36.07  ? 67  LYS C O   1 
ATOM   1955 C CB  . LYS C 1 68 ? 26.516  -22.691 10.676  1.00 41.88  ? 67  LYS C CB  1 
ATOM   1956 C CG  . LYS C 1 68 ? 27.469  -23.860 10.414  1.00 48.86  ? 67  LYS C CG  1 
ATOM   1957 C CD  . LYS C 1 68 ? 28.626  -23.695 11.402  1.00 60.29  ? 67  LYS C CD  1 
ATOM   1958 C CE  . LYS C 1 68 ? 29.524  -24.879 11.623  1.00 68.23  ? 67  LYS C CE  1 
ATOM   1959 N NZ  . LYS C 1 68 ? 30.180  -25.329 10.392  1.00 70.81  ? 67  LYS C NZ  1 
ATOM   1960 N N   . TYR C 1 69 ? 23.450  -23.768 11.071  1.00 30.48  ? 68  TYR C N   1 
ATOM   1961 C CA  . TYR C 1 69 ? 22.602  -24.934 11.269  1.00 32.75  ? 68  TYR C CA  1 
ATOM   1962 C C   . TYR C 1 69 ? 21.117  -24.598 11.108  1.00 30.58  ? 68  TYR C C   1 
ATOM   1963 O O   . TYR C 1 69 ? 20.314  -25.525 10.967  1.00 31.31  ? 68  TYR C O   1 
ATOM   1964 C CB  . TYR C 1 69 ? 22.762  -25.576 12.656  1.00 35.19  ? 68  TYR C CB  1 
ATOM   1965 C CG  . TYR C 1 69 ? 24.176  -26.037 12.937  1.00 36.98  ? 68  TYR C CG  1 
ATOM   1966 C CD1 . TYR C 1 69 ? 24.927  -26.697 11.970  1.00 34.98  ? 68  TYR C CD1 1 
ATOM   1967 C CD2 . TYR C 1 69 ? 24.785  -25.715 14.131  1.00 35.45  ? 68  TYR C CD2 1 
ATOM   1968 C CE1 . TYR C 1 69 ? 26.224  -27.095 12.223  1.00 31.37  ? 68  TYR C CE1 1 
ATOM   1969 C CE2 . TYR C 1 69 ? 26.091  -26.081 14.382  1.00 35.68  ? 68  TYR C CE2 1 
ATOM   1970 C CZ  . TYR C 1 69 ? 26.810  -26.777 13.434  1.00 35.75  ? 68  TYR C CZ  1 
ATOM   1971 O OH  . TYR C 1 69 ? 28.099  -27.132 13.741  1.00 34.87  ? 68  TYR C OH  1 
ATOM   1972 N N   . GLY C 1 70 ? 20.762  -23.299 11.149  1.00 25.97  ? 69  GLY C N   1 
ATOM   1973 C CA  . GLY C 1 70 ? 19.370  -22.893 11.067  1.00 30.36  ? 69  GLY C CA  1 
ATOM   1974 C C   . GLY C 1 70 ? 18.970  -22.734 9.601   1.00 37.62  ? 69  GLY C C   1 
ATOM   1975 O O   . GLY C 1 70 ? 19.053  -21.649 9.032   1.00 40.94  ? 69  GLY C O   1 
ATOM   1976 N N   . LYS C 1 71 ? 18.569  -23.842 8.986   1.00 34.56  ? 70  LYS C N   1 
ATOM   1977 C CA  . LYS C 1 71 ? 18.247  -23.853 7.568   1.00 37.62  ? 70  LYS C CA  1 
ATOM   1978 C C   . LYS C 1 71 ? 17.443  -25.122 7.372   1.00 35.40  ? 70  LYS C C   1 
ATOM   1979 O O   . LYS C 1 71 ? 17.733  -26.125 8.021   1.00 40.34  ? 70  LYS C O   1 
ATOM   1980 C CB  . LYS C 1 71 ? 19.498  -23.900 6.684   1.00 37.45  ? 70  LYS C CB  1 
ATOM   1981 C CG  . LYS C 1 71 ? 20.273  -25.214 6.866   1.00 49.19  ? 70  LYS C CG  1 
ATOM   1982 C CD  . LYS C 1 71 ? 21.739  -25.346 6.465   1.00 46.80  ? 70  LYS C CD  1 
ATOM   1983 C CE  . LYS C 1 71 ? 22.207  -26.767 6.650   1.00 52.23  ? 70  LYS C CE  1 
ATOM   1984 N N   . PRO C 1 72 ? 16.408  -25.123 6.508   1.00 36.56  ? 71  PRO C N   1 
ATOM   1985 C CA  . PRO C 1 72 ? 15.396  -26.191 6.551   1.00 33.35  ? 71  PRO C CA  1 
ATOM   1986 C C   . PRO C 1 72 ? 15.984  -27.572 6.277   1.00 30.62  ? 71  PRO C C   1 
ATOM   1987 O O   . PRO C 1 72 ? 17.072  -27.704 5.714   1.00 31.54  ? 71  PRO C O   1 
ATOM   1988 C CB  . PRO C 1 72 ? 14.363  -25.743 5.498   1.00 33.43  ? 71  PRO C CB  1 
ATOM   1989 C CG  . PRO C 1 72 ? 14.622  -24.274 5.442   1.00 35.83  ? 71  PRO C CG  1 
ATOM   1990 C CD  . PRO C 1 72 ? 16.147  -24.098 5.491   1.00 32.42  ? 71  PRO C CD  1 
ATOM   1991 N N   . ASN C 1 73 ? 15.260  -28.616 6.670   1.00 31.84  ? 72  ASN C N   1 
ATOM   1992 C CA  . ASN C 1 73 ? 15.515  -29.910 6.045   1.00 40.51  ? 72  ASN C CA  1 
ATOM   1993 C C   . ASN C 1 73 ? 14.354  -30.836 6.358   1.00 36.40  ? 72  ASN C C   1 
ATOM   1994 O O   . ASN C 1 73 ? 13.525  -30.505 7.192   1.00 42.55  ? 72  ASN C O   1 
ATOM   1995 C CB  . ASN C 1 73 ? 16.907  -30.485 6.305   1.00 38.60  ? 72  ASN C CB  1 
ATOM   1996 C CG  . ASN C 1 73 ? 17.042  -30.964 7.723   1.00 38.61  ? 72  ASN C CG  1 
ATOM   1997 O OD1 . ASN C 1 73 ? 16.180  -31.704 8.205   1.00 40.01  ? 72  ASN C OD1 1 
ATOM   1998 N ND2 . ASN C 1 73 ? 18.093  -30.529 8.401   1.00 42.39  ? 72  ASN C ND2 1 
ATOM   1999 N N   . LYS C 1 74 ? 14.319  -31.990 5.683   1.00 45.53  ? 73  LYS C N   1 
ATOM   2000 C CA  . LYS C 1 74 ? 13.067  -32.719 5.547   1.00 45.34  ? 73  LYS C CA  1 
ATOM   2001 C C   . LYS C 1 74 ? 12.900  -33.727 6.680   1.00 45.90  ? 73  LYS C C   1 
ATOM   2002 O O   . LYS C 1 74 ? 11.846  -34.353 6.761   1.00 47.41  ? 73  LYS C O   1 
ATOM   2003 C CB  . LYS C 1 74 ? 12.889  -33.224 4.109   1.00 47.21  ? 73  LYS C CB  1 
ATOM   2004 N N   . ARG C 1 75 ? 13.919  -33.848 7.563   1.00 44.54  ? 74  ARG C N   1 
ATOM   2005 C CA  . ARG C 1 75 ? 13.857  -34.722 8.729   1.00 42.79  ? 74  ARG C CA  1 
ATOM   2006 C C   . ARG C 1 75 ? 12.604  -34.392 9.540   1.00 43.15  ? 74  ARG C C   1 
ATOM   2007 O O   . ARG C 1 75 ? 12.282  -33.218 9.687   1.00 51.75  ? 74  ARG C O   1 
ATOM   2008 C CB  . ARG C 1 75 ? 15.081  -34.518 9.640   1.00 48.12  ? 74  ARG C CB  1 
ATOM   2009 C CG  . ARG C 1 75 ? 16.474  -34.676 9.043   1.00 46.55  ? 74  ARG C CG  1 
ATOM   2010 C CD  . ARG C 1 75 ? 16.757  -36.042 8.395   1.00 52.86  ? 74  ARG C CD  1 
ATOM   2011 N NE  . ARG C 1 75 ? 16.497  -37.117 9.361   1.00 50.18  ? 74  ARG C NE  1 
ATOM   2012 C CZ  . ARG C 1 75 ? 17.426  -37.717 10.095  1.00 48.32  ? 74  ARG C CZ  1 
ATOM   2013 N NH1 . ARG C 1 75 ? 17.058  -38.505 11.091  1.00 46.28  ? 74  ARG C NH1 1 
ATOM   2014 N NH2 . ARG C 1 75 ? 18.703  -37.476 9.845   1.00 42.22  ? 74  ARG C NH2 1 
ATOM   2015 N N   . LYS C 1 76 ? 11.926  -35.408 10.104  1.00 46.92  ? 75  LYS C N   1 
ATOM   2016 C CA  . LYS C 1 76 ? 10.597  -35.225 10.685  1.00 46.46  ? 75  LYS C CA  1 
ATOM   2017 C C   . LYS C 1 76 ? 10.640  -34.222 11.838  1.00 48.07  ? 75  LYS C C   1 
ATOM   2018 O O   . LYS C 1 76 ? 11.340  -34.420 12.833  1.00 47.82  ? 75  LYS C O   1 
ATOM   2019 C CB  . LYS C 1 76 ? 9.885   -36.524 11.102  1.00 56.76  ? 75  LYS C CB  1 
ATOM   2020 C CG  . LYS C 1 76 ? 8.366   -36.648 10.898  1.00 53.46  ? 75  LYS C CG  1 
ATOM   2021 C CD  . LYS C 1 76 ? 7.621   -37.167 12.128  1.00 55.09  ? 75  LYS C CD  1 
ATOM   2022 N N   . GLY C 1 77 ? 9.861   -33.139 11.698  1.00 45.14  ? 76  GLY C N   1 
ATOM   2023 C CA  . GLY C 1 77 ? 9.683   -32.196 12.791  1.00 36.13  ? 76  GLY C CA  1 
ATOM   2024 C C   . GLY C 1 77 ? 10.751  -31.106 12.811  1.00 33.02  ? 76  GLY C C   1 
ATOM   2025 O O   . GLY C 1 77 ? 10.651  -30.181 13.613  1.00 38.16  ? 76  GLY C O   1 
ATOM   2026 N N   . PHE C 1 78 ? 11.757  -31.221 11.928  1.00 34.35  ? 77  PHE C N   1 
ATOM   2027 C CA  . PHE C 1 78 ? 12.858  -30.265 11.860  1.00 32.02  ? 77  PHE C CA  1 
ATOM   2028 C C   . PHE C 1 78 ? 12.306  -28.862 11.615  1.00 32.87  ? 77  PHE C C   1 
ATOM   2029 O O   . PHE C 1 78 ? 12.603  -27.949 12.368  1.00 31.78  ? 77  PHE C O   1 
ATOM   2030 C CB  . PHE C 1 78 ? 13.954  -30.606 10.842  1.00 32.56  ? 77  PHE C CB  1 
ATOM   2031 C CG  . PHE C 1 78 ? 15.214  -29.762 10.988  1.00 31.84  ? 77  PHE C CG  1 
ATOM   2032 C CD1 . PHE C 1 78 ? 15.339  -28.536 10.340  1.00 28.90  ? 77  PHE C CD1 1 
ATOM   2033 C CD2 . PHE C 1 78 ? 16.253  -30.167 11.821  1.00 30.76  ? 77  PHE C CD2 1 
ATOM   2034 C CE1 . PHE C 1 78 ? 16.478  -27.756 10.509  1.00 29.96  ? 77  PHE C CE1 1 
ATOM   2035 C CE2 . PHE C 1 78 ? 17.374  -29.370 11.992  1.00 27.48  ? 77  PHE C CE2 1 
ATOM   2036 C CZ  . PHE C 1 78 ? 17.497  -28.180 11.322  1.00 26.97  ? 77  PHE C CZ  1 
ATOM   2037 N N   . ASN C 1 79 ? 11.496  -28.710 10.556  1.00 32.96  ? 78  ASN C N   1 
ATOM   2038 C CA  . ASN C 1 79 ? 11.100  -27.414 10.040  1.00 32.27  ? 78  ASN C CA  1 
ATOM   2039 C C   . ASN C 1 79 ? 10.165  -26.737 11.031  1.00 31.45  ? 78  ASN C C   1 
ATOM   2040 O O   . ASN C 1 79 ? 10.296  -25.553 11.328  1.00 33.06  ? 78  ASN C O   1 
ATOM   2041 C CB  . ASN C 1 79 ? 10.528  -27.560 8.637   1.00 31.93  ? 78  ASN C CB  1 
ATOM   2042 C CG  . ASN C 1 79 ? 11.632  -27.781 7.635   1.00 38.90  ? 78  ASN C CG  1 
ATOM   2043 O OD1 . ASN C 1 79 ? 12.766  -27.332 7.861   1.00 41.60  ? 78  ASN C OD1 1 
ATOM   2044 N ND2 . ASN C 1 79 ? 11.318  -28.398 6.505   1.00 35.67  ? 78  ASN C ND2 1 
ATOM   2045 N N   . GLU C 1 80 ? 9.244   -27.513 11.575  1.00 31.23  ? 79  GLU C N   1 
ATOM   2046 C CA  . GLU C 1 80 ? 8.461   -27.019 12.689  1.00 33.25  ? 79  GLU C CA  1 
ATOM   2047 C C   . GLU C 1 80 ? 9.359   -26.624 13.862  1.00 33.98  ? 79  GLU C C   1 
ATOM   2048 O O   . GLU C 1 80 ? 9.060   -25.658 14.562  1.00 36.77  ? 79  GLU C O   1 
ATOM   2049 C CB  . GLU C 1 80 ? 7.459   -28.076 13.140  1.00 38.35  ? 79  GLU C CB  1 
ATOM   2050 C CG  . GLU C 1 80 ? 6.577   -27.589 14.279  1.00 42.32  ? 79  GLU C CG  1 
ATOM   2051 C CD  . GLU C 1 80 ? 5.349   -28.466 14.408  1.00 59.37  ? 79  GLU C CD  1 
ATOM   2052 O OE1 . GLU C 1 80 ? 5.319   -29.590 13.839  1.00 67.20  ? 79  GLU C OE1 1 
ATOM   2053 O OE2 . GLU C 1 80 ? 4.397   -27.984 15.060  1.00 53.84  ? 79  GLU C OE2 1 
ATOM   2054 N N   . GLY C 1 81 ? 10.445  -27.375 14.087  1.00 30.27  ? 80  GLY C N   1 
ATOM   2055 C CA  . GLY C 1 81 ? 11.356  -27.052 15.181  1.00 30.58  ? 80  GLY C CA  1 
ATOM   2056 C C   . GLY C 1 81 ? 11.982  -25.669 14.993  1.00 26.08  ? 80  GLY C C   1 
ATOM   2057 O O   . GLY C 1 81 ? 12.084  -24.909 15.941  1.00 24.88  ? 80  GLY C O   1 
ATOM   2058 N N   . LEU C 1 82 ? 12.368  -25.348 13.752  1.00 25.59  ? 81  LEU C N   1 
ATOM   2059 C CA  . LEU C 1 82 ? 12.932  -24.069 13.376  1.00 24.66  ? 81  LEU C CA  1 
ATOM   2060 C C   . LEU C 1 82 ? 11.916  -22.949 13.568  1.00 25.20  ? 81  LEU C C   1 
ATOM   2061 O O   . LEU C 1 82 ? 12.270  -21.839 13.957  1.00 27.27  ? 81  LEU C O   1 
ATOM   2062 C CB  . LEU C 1 82 ? 13.302  -24.129 11.893  1.00 25.31  ? 81  LEU C CB  1 
ATOM   2063 C CG  . LEU C 1 82 ? 14.575  -24.907 11.542  1.00 24.47  ? 81  LEU C CG  1 
ATOM   2064 C CD1 . LEU C 1 82 ? 14.758  -24.858 10.008  1.00 22.85  ? 81  LEU C CD1 1 
ATOM   2065 C CD2 . LEU C 1 82 ? 15.782  -24.373 12.275  1.00 23.28  ? 81  LEU C CD2 1 
ATOM   2066 N N   . TRP C 1 83 ? 10.662  -23.217 13.219  1.00 29.30  ? 82  TRP C N   1 
ATOM   2067 C CA  . TRP C 1 83 ? 9.617   -22.237 13.482  1.00 32.79  ? 82  TRP C CA  1 
ATOM   2068 C C   . TRP C 1 83 ? 9.554   -21.919 14.983  1.00 29.43  ? 82  TRP C C   1 
ATOM   2069 O O   . TRP C 1 83 ? 9.459   -20.754 15.379  1.00 27.38  ? 82  TRP C O   1 
ATOM   2070 C CB  . TRP C 1 83 ? 8.264   -22.700 12.917  1.00 36.66  ? 82  TRP C CB  1 
ATOM   2071 C CG  . TRP C 1 83 ? 7.258   -21.580 12.911  1.00 37.33  ? 82  TRP C CG  1 
ATOM   2072 C CD1 . TRP C 1 83 ? 7.019   -20.685 11.910  1.00 35.23  ? 82  TRP C CD1 1 
ATOM   2073 C CD2 . TRP C 1 83 ? 6.432   -21.183 14.018  1.00 34.77  ? 82  TRP C CD2 1 
ATOM   2074 N NE1 . TRP C 1 83 ? 6.075   -19.779 12.314  1.00 33.75  ? 82  TRP C NE1 1 
ATOM   2075 C CE2 . TRP C 1 83 ? 5.705   -20.056 13.598  1.00 33.15  ? 82  TRP C CE2 1 
ATOM   2076 C CE3 . TRP C 1 83 ? 6.223   -21.684 15.315  1.00 39.25  ? 82  TRP C CE3 1 
ATOM   2077 C CZ2 . TRP C 1 83 ? 4.778   -19.428 14.433  1.00 37.68  ? 82  TRP C CZ2 1 
ATOM   2078 C CZ3 . TRP C 1 83 ? 5.331   -21.043 16.147  1.00 34.61  ? 82  TRP C CZ3 1 
ATOM   2079 C CH2 . TRP C 1 83 ? 4.630   -19.919 15.713  1.00 35.07  ? 82  TRP C CH2 1 
ATOM   2080 N N   . GLU C 1 84 ? 9.662   -22.953 15.819  1.00 29.50  ? 83  GLU C N   1 
ATOM   2081 C CA  . GLU C 1 84 ? 9.501   -22.800 17.271  1.00 33.58  ? 83  GLU C CA  1 
ATOM   2082 C C   . GLU C 1 84 ? 10.661  -22.038 17.902  1.00 32.22  ? 83  GLU C C   1 
ATOM   2083 O O   . GLU C 1 84 ? 10.438  -21.133 18.689  1.00 35.67  ? 83  GLU C O   1 
ATOM   2084 C CB  . GLU C 1 84 ? 9.336   -24.103 18.052  1.00 31.87  ? 83  GLU C CB  1 
ATOM   2085 C CG  . GLU C 1 84 ? 7.998   -24.769 17.760  1.00 33.73  ? 83  GLU C CG  1 
ATOM   2086 C CD  . GLU C 1 84 ? 7.962   -26.200 18.242  1.00 37.90  ? 83  GLU C CD  1 
ATOM   2087 O OE1 . GLU C 1 84 ? 8.960   -26.654 18.857  1.00 35.50  ? 83  GLU C OE1 1 
ATOM   2088 O OE2 . GLU C 1 84 ? 6.942   -26.869 17.951  1.00 39.90  ? 83  GLU C OE2 1 
ATOM   2089 N N   . ILE C 1 85 ? 11.900  -22.384 17.544  1.00 32.81  ? 84  ILE C N   1 
ATOM   2090 C CA  . ILE C 1 85 ? 13.060  -21.745 18.144  1.00 27.13  ? 84  ILE C CA  1 
ATOM   2091 C C   . ILE C 1 85 ? 13.065  -20.243 17.855  1.00 28.11  ? 84  ILE C C   1 
ATOM   2092 O O   . ILE C 1 85 ? 13.538  -19.456 18.668  1.00 30.83  ? 84  ILE C O   1 
ATOM   2093 C CB  . ILE C 1 85 ? 14.346  -22.475 17.741  1.00 24.69  ? 84  ILE C CB  1 
ATOM   2094 C CG1 . ILE C 1 85 ? 15.490  -22.115 18.701  1.00 24.11  ? 84  ILE C CG1 1 
ATOM   2095 C CG2 . ILE C 1 85 ? 14.701  -22.272 16.259  1.00 23.84  ? 84  ILE C CG2 1 
ATOM   2096 C CD1 . ILE C 1 85 ? 16.613  -23.120 18.700  1.00 24.61  ? 84  ILE C CD1 1 
ATOM   2097 N N   . GLN C 1 86 ? 12.440  -19.842 16.739  1.00 31.56  ? 85  GLN C N   1 
ATOM   2098 C CA  . GLN C 1 86 ? 12.479  -18.458 16.287  1.00 30.53  ? 85  GLN C CA  1 
ATOM   2099 C C   . GLN C 1 86 ? 11.260  -17.703 16.783  1.00 28.10  ? 85  GLN C C   1 
ATOM   2100 O O   . GLN C 1 86 ? 11.354  -16.508 17.043  1.00 29.86  ? 85  GLN C O   1 
ATOM   2101 C CB  . GLN C 1 86 ? 12.394  -18.300 14.755  1.00 27.61  ? 85  GLN C CB  1 
ATOM   2102 C CG  . GLN C 1 86 ? 12.978  -16.986 14.268  1.00 29.71  ? 85  GLN C CG  1 
ATOM   2103 C CD  . GLN C 1 86 ? 13.219  -16.960 12.764  1.00 34.93  ? 85  GLN C CD  1 
ATOM   2104 O OE1 . GLN C 1 86 ? 13.203  -17.993 12.078  1.00 35.62  ? 85  GLN C OE1 1 
ATOM   2105 N NE2 . GLN C 1 86 ? 13.444  -15.766 12.230  1.00 35.94  ? 85  GLN C NE2 1 
ATOM   2106 N N   . ASN C 1 87 ? 10.117  -18.391 16.830  1.00 29.98  ? 86  ASN C N   1 
ATOM   2107 C CA  . ASN C 1 87 ? 8.830   -17.736 16.988  1.00 33.36  ? 86  ASN C CA  1 
ATOM   2108 C C   . ASN C 1 87 ? 8.263   -17.973 18.395  1.00 40.16  ? 86  ASN C C   1 
ATOM   2109 O O   . ASN C 1 87 ? 7.778   -17.042 19.037  1.00 39.80  ? 86  ASN C O   1 
ATOM   2110 C CB  . ASN C 1 87 ? 7.911   -18.062 15.809  1.00 38.98  ? 86  ASN C CB  1 
ATOM   2111 C CG  . ASN C 1 87 ? 8.485   -17.515 14.522  1.00 41.38  ? 86  ASN C CG  1 
ATOM   2112 O OD1 . ASN C 1 87 ? 8.469   -16.297 14.318  1.00 49.37  ? 86  ASN C OD1 1 
ATOM   2113 N ND2 . ASN C 1 87 ? 9.034   -18.370 13.670  1.00 39.96  ? 86  ASN C ND2 1 
ATOM   2114 N N   . ASN C 1 88 ? 8.328   -19.215 18.882  1.00 39.12  ? 87  ASN C N   1 
ATOM   2115 C CA  . ASN C 1 88 ? 7.678   -19.555 20.139  1.00 40.48  ? 87  ASN C CA  1 
ATOM   2116 C C   . ASN C 1 88 ? 8.603   -20.459 20.955  1.00 35.86  ? 87  ASN C C   1 
ATOM   2117 O O   . ASN C 1 88 ? 8.266   -21.631 21.129  1.00 32.25  ? 87  ASN C O   1 
ATOM   2118 C CB  . ASN C 1 88 ? 6.300   -20.167 19.880  1.00 46.80  ? 87  ASN C CB  1 
ATOM   2119 C CG  . ASN C 1 88 ? 5.342   -20.042 21.047  1.00 50.16  ? 87  ASN C CG  1 
ATOM   2120 O OD1 . ASN C 1 88 ? 5.722   -19.594 22.131  1.00 51.33  ? 87  ASN C OD1 1 
ATOM   2121 N ND2 . ASN C 1 88 ? 4.085   -20.404 20.836  1.00 48.76  ? 87  ASN C ND2 1 
ATOM   2122 N N   . PRO C 1 89 ? 9.791   -19.957 21.412  1.00 30.18  ? 88  PRO C N   1 
ATOM   2123 C CA  . PRO C 1 89 ? 10.828  -20.803 21.984  1.00 29.22  ? 88  PRO C CA  1 
ATOM   2124 C C   . PRO C 1 89 ? 10.706  -21.092 23.477  1.00 37.50  ? 88  PRO C C   1 
ATOM   2125 O O   . PRO C 1 89 ? 11.572  -21.785 24.005  1.00 43.60  ? 88  PRO C O   1 
ATOM   2126 C CB  . PRO C 1 89 ? 12.135  -20.035 21.682  1.00 26.18  ? 88  PRO C CB  1 
ATOM   2127 C CG  . PRO C 1 89 ? 11.724  -18.579 21.615  1.00 25.67  ? 88  PRO C CG  1 
ATOM   2128 C CD  . PRO C 1 89 ? 10.249  -18.556 21.289  1.00 29.34  ? 88  PRO C CD  1 
ATOM   2129 N N   . HIS C 1 90 ? 9.671   -20.555 24.140  1.00 45.74  ? 89  HIS C N   1 
ATOM   2130 C CA  . HIS C 1 90 ? 9.578   -20.668 25.595  1.00 48.85  ? 89  HIS C CA  1 
ATOM   2131 C C   . HIS C 1 90 ? 8.199   -21.168 26.016  1.00 47.81  ? 89  HIS C C   1 
ATOM   2132 O O   . HIS C 1 90 ? 7.893   -21.213 27.197  1.00 47.90  ? 89  HIS C O   1 
ATOM   2133 C CB  . HIS C 1 90 ? 10.048  -19.383 26.291  1.00 45.06  ? 89  HIS C CB  1 
ATOM   2134 C CG  . HIS C 1 90 ? 11.506  -19.086 26.143  1.00 44.59  ? 89  HIS C CG  1 
ATOM   2135 N ND1 . HIS C 1 90 ? 11.963  -17.847 25.754  1.00 46.42  ? 89  HIS C ND1 1 
ATOM   2136 C CD2 . HIS C 1 90 ? 12.607  -19.835 26.328  1.00 45.42  ? 89  HIS C CD2 1 
ATOM   2137 C CE1 . HIS C 1 90 ? 13.293  -17.848 25.708  1.00 46.54  ? 89  HIS C CE1 1 
ATOM   2138 N NE2 . HIS C 1 90 ? 13.703  -19.049 26.050  1.00 48.13  ? 89  HIS C NE2 1 
ATOM   2139 N N   . ALA C 1 91 ? 7.385   -21.557 25.038  1.00 50.77  ? 90  ALA C N   1 
ATOM   2140 C CA  . ALA C 1 91 ? 6.135   -22.252 25.285  1.00 64.82  ? 90  ALA C CA  1 
ATOM   2141 C C   . ALA C 1 91 ? 6.431   -23.604 25.936  1.00 75.47  ? 90  ALA C C   1 
ATOM   2142 O O   . ALA C 1 91 ? 7.545   -24.114 25.796  1.00 72.31  ? 90  ALA C O   1 
ATOM   2143 C CB  . ALA C 1 91 ? 5.398   -22.407 23.969  1.00 65.60  ? 90  ALA C CB  1 
ATOM   2144 N N   . SER C 1 92 ? 5.425   -24.186 26.618  1.00 69.17  ? 91  SER C N   1 
ATOM   2145 C CA  . SER C 1 92 ? 5.604   -25.382 27.433  1.00 69.91  ? 91  SER C CA  1 
ATOM   2146 C C   . SER C 1 92 ? 5.515   -26.691 26.640  1.00 76.42  ? 91  SER C C   1 
ATOM   2147 O O   . SER C 1 92 ? 6.313   -27.604 26.859  1.00 75.76  ? 91  SER C O   1 
ATOM   2148 C CB  . SER C 1 92 ? 4.692   -25.383 28.630  1.00 62.09  ? 91  SER C CB  1 
ATOM   2149 O OG  . SER C 1 92 ? 5.354   -24.766 29.725  1.00 52.13  ? 91  SER C OG  1 
ATOM   2150 N N   . TYR C 1 93 ? 4.529   -26.799 25.744  1.00 77.04  ? 92  TYR C N   1 
ATOM   2151 C CA  . TYR C 1 93 ? 4.335   -28.022 24.981  1.00 77.58  ? 92  TYR C CA  1 
ATOM   2152 C C   . TYR C 1 93 ? 4.039   -29.185 25.953  1.00 90.58  ? 92  TYR C C   1 
ATOM   2153 O O   . TYR C 1 93 ? 3.369   -30.181 25.567  1.00 88.14  ? 92  TYR C O   1 
ATOM   2154 C CB  . TYR C 1 93 ? 5.582   -28.298 24.133  1.00 65.50  ? 92  TYR C CB  1 
ATOM   2155 C CG  . TYR C 1 93 ? 6.039   -27.141 23.250  1.00 55.70  ? 92  TYR C CG  1 
ATOM   2156 C CD1 . TYR C 1 93 ? 5.487   -26.941 21.983  1.00 54.17  ? 92  TYR C CD1 1 
ATOM   2157 C CD2 . TYR C 1 93 ? 7.020   -26.247 23.685  1.00 48.28  ? 92  TYR C CD2 1 
ATOM   2158 C CE1 . TYR C 1 93 ? 5.904   -25.899 21.168  1.00 50.38  ? 92  TYR C CE1 1 
ATOM   2159 C CE2 . TYR C 1 93 ? 7.442   -25.197 22.881  1.00 49.28  ? 92  TYR C CE2 1 
ATOM   2160 C CZ  . TYR C 1 93 ? 6.886   -25.027 21.621  1.00 47.39  ? 92  TYR C CZ  1 
ATOM   2161 O OH  . TYR C 1 93 ? 7.280   -23.991 20.828  1.00 44.79  ? 92  TYR C OH  1 
HETATM 2162 S S   . SO4 D 2 .  ? -0.165  -33.253 2.209   1.00 101.04 ? 101 SO4 A S   1 
HETATM 2163 O O1  . SO4 D 2 .  ? -0.406  -33.740 0.876   1.00 101.28 ? 101 SO4 A O1  1 
HETATM 2164 O O2  . SO4 D 2 .  ? 0.085   -31.839 2.159   1.00 102.17 ? 101 SO4 A O2  1 
HETATM 2165 O O3  . SO4 D 2 .  ? -1.320  -33.510 3.027   1.00 106.47 ? 101 SO4 A O3  1 
HETATM 2166 O O4  . SO4 D 2 .  ? 0.979   -33.922 2.774   1.00 108.33 ? 101 SO4 A O4  1 
HETATM 2167 S S   . SO4 E 2 .  ? -10.983 -24.135 0.808   1.00 96.60  ? 102 SO4 A S   1 
HETATM 2168 O O1  . SO4 E 2 .  ? -10.356 -24.247 -0.484  1.00 88.54  ? 102 SO4 A O1  1 
HETATM 2169 O O2  . SO4 E 2 .  ? -11.326 -22.760 1.054   1.00 99.22  ? 102 SO4 A O2  1 
HETATM 2170 O O3  . SO4 E 2 .  ? -12.184 -24.935 0.817   1.00 118.45 ? 102 SO4 A O3  1 
HETATM 2171 O O4  . SO4 E 2 .  ? -10.082 -24.597 1.840   1.00 93.51  ? 102 SO4 A O4  1 
HETATM 2172 C C1  . EDO F 3 .  ? 12.879  -19.398 -7.860  1.00 37.70  ? 103 EDO A C1  1 
HETATM 2173 O O1  . EDO F 3 .  ? 13.952  -18.669 -7.237  1.00 35.01  ? 103 EDO A O1  1 
HETATM 2174 C C2  . EDO F 3 .  ? 11.926  -18.619 -8.721  1.00 36.74  ? 103 EDO A C2  1 
HETATM 2175 O O2  . EDO F 3 .  ? 11.401  -17.411 -8.155  1.00 34.38  ? 103 EDO A O2  1 
HETATM 2176 S S   . SO4 G 2 .  ? 7.346   -29.047 5.993   1.00 86.32  ? 104 SO4 A S   1 
HETATM 2177 O O1  . SO4 G 2 .  ? 8.344   -28.152 5.459   1.00 73.28  ? 104 SO4 A O1  1 
HETATM 2178 O O2  . SO4 G 2 .  ? 7.074   -30.071 5.017   1.00 76.72  ? 104 SO4 A O2  1 
HETATM 2179 O O3  . SO4 G 2 .  ? 7.835   -29.650 7.202   1.00 88.48  ? 104 SO4 A O3  1 
HETATM 2180 O O4  . SO4 G 2 .  ? 6.125   -28.329 6.305   1.00 83.70  ? 104 SO4 A O4  1 
HETATM 2181 S S   . SO4 H 2 .  ? 7.430   -8.087  -24.365 1.00 64.54  ? 101 SO4 B S   1 
HETATM 2182 O O1  . SO4 H 2 .  ? 8.311   -8.640  -25.346 1.00 45.11  ? 101 SO4 B O1  1 
HETATM 2183 O O2  . SO4 H 2 .  ? 6.058   -8.241  -24.812 1.00 55.46  ? 101 SO4 B O2  1 
HETATM 2184 O O3  . SO4 H 2 .  ? 7.602   -8.763  -23.089 1.00 44.82  ? 101 SO4 B O3  1 
HETATM 2185 O O4  . SO4 H 2 .  ? 7.737   -6.687  -24.227 1.00 65.86  ? 101 SO4 B O4  1 
HETATM 2186 S S   . SO4 I 2 .  ? 14.047  -27.266 -25.958 1.00 87.37  ? 102 SO4 B S   1 
HETATM 2187 O O1  . SO4 I 2 .  ? 15.177  -26.508 -25.504 1.00 64.14  ? 102 SO4 B O1  1 
HETATM 2188 O O2  . SO4 I 2 .  ? 14.506  -28.259 -26.892 1.00 95.08  ? 102 SO4 B O2  1 
HETATM 2189 O O3  . SO4 I 2 .  ? 13.411  -27.913 -24.833 1.00 100.19 ? 102 SO4 B O3  1 
HETATM 2190 O O4  . SO4 I 2 .  ? 13.090  -26.400 -26.618 1.00 77.38  ? 102 SO4 B O4  1 
HETATM 2191 N N1  . K2S J 4 .  ? 20.115  -16.867 -22.055 0.76 28.22  ? 103 K2S B N1  1 
HETATM 2192 C C4  . K2S J 4 .  ? 20.053  -15.936 -24.360 0.76 39.52  ? 103 K2S B C4  1 
HETATM 2193 C C5  . K2S J 4 .  ? 18.250  -16.296 -21.175 0.76 29.23  ? 103 K2S B C5  1 
HETATM 2194 C C6  . K2S J 4 .  ? 17.199  -16.135 -20.130 0.76 29.77  ? 103 K2S B C6  1 
HETATM 2195 N N   . K2S J 4 .  ? 16.263  -15.790 -24.095 0.76 31.24  ? 103 K2S B N   1 
HETATM 2196 C C   . K2S J 4 .  ? 16.523  -15.741 -25.536 0.76 32.11  ? 103 K2S B C   1 
HETATM 2197 O O   . K2S J 4 .  ? 17.601  -13.693 -23.964 0.76 34.45  ? 103 K2S B O   1 
HETATM 2198 C C1  . K2S J 4 .  ? 14.907  -16.160 -23.692 0.76 32.75  ? 103 K2S B C1  1 
HETATM 2199 C C2  . K2S J 4 .  ? 18.316  -15.731 -22.462 0.76 30.86  ? 103 K2S B C2  1 
HETATM 2200 C C3  . K2S J 4 .  ? 19.498  -16.125 -22.985 0.76 31.37  ? 103 K2S B C3  1 
HETATM 2201 N N2  . K2S J 4 .  ? 19.353  -17.004 -20.932 0.76 30.28  ? 103 K2S B N2  1 
HETATM 2202 O O1  . K2S J 4 .  ? 16.210  -14.410 -22.042 0.76 40.15  ? 103 K2S B O1  1 
HETATM 2203 S S   . K2S J 4 .  ? 17.053  -14.733 -23.151 0.76 33.14  ? 103 K2S B S   1 
HETATM 2204 C C1  . EDO K 3 .  ? 15.412  -35.719 16.554  1.00 41.75  ? 101 EDO C C1  1 
HETATM 2205 O O1  . EDO K 3 .  ? 14.130  -36.258 16.279  1.00 45.81  ? 101 EDO C O1  1 
HETATM 2206 C C2  . EDO K 3 .  ? 15.214  -34.750 17.612  1.00 37.78  ? 101 EDO C C2  1 
HETATM 2207 O O2  . EDO K 3 .  ? 14.278  -35.304 18.494  1.00 40.05  ? 101 EDO C O2  1 
HETATM 2208 S S   . SO4 L 2 .  ? 27.339  -37.366 11.894  1.00 88.51  ? 102 SO4 C S   1 
HETATM 2209 O O1  . SO4 L 2 .  ? 27.381  -36.030 11.348  1.00 93.19  ? 102 SO4 C O1  1 
HETATM 2210 O O2  . SO4 L 2 .  ? 26.608  -38.227 11.004  1.00 95.81  ? 102 SO4 C O2  1 
HETATM 2211 O O3  . SO4 L 2 .  ? 28.680  -37.869 12.063  1.00 87.47  ? 102 SO4 C O3  1 
HETATM 2212 O O4  . SO4 L 2 .  ? 26.671  -37.340 13.168  1.00 108.97 ? 102 SO4 C O4  1 
HETATM 2213 O O   . HOH M 5 .  ? -2.507  -9.620  4.543   1.00 63.89  ? 201 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 12.062  -9.644  -6.907  1.00 39.09  ? 202 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? -6.991  -15.835 -10.342 1.00 48.86  ? 203 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 3.280   -3.540  -3.134  1.00 30.66  ? 204 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? -1.532  -20.574 6.665   1.00 32.05  ? 205 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 0.342   -24.220 13.765  1.00 51.11  ? 206 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -3.291  3.252   -2.231  1.00 36.35  ? 207 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 7.516   -32.220 4.066   1.00 61.25  ? 208 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -6.447  -12.586 -16.718 1.00 51.11  ? 209 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? -1.353  -20.889 8.766   1.00 48.68  ? 210 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 4.187   -29.347 7.441   1.00 48.00  ? 211 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? -3.989  -30.756 -3.424  1.00 59.13  ? 212 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 1.034   -24.449 -6.144  1.00 58.38  ? 213 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? -6.718  -15.421 -8.081  1.00 24.88  ? 214 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 7.126   -8.047  4.403   1.00 41.21  ? 215 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 7.960   -22.142 -9.516  1.00 29.36  ? 216 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -2.629  -11.905 11.251  1.00 43.34  ? 217 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 8.020   -30.063 9.646   1.00 40.37  ? 218 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 12.850  -15.643 -9.151  1.00 36.40  ? 219 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -0.133  -33.688 5.220   1.00 53.72  ? 220 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 10.351  -11.932 5.746   1.00 31.34  ? 221 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 7.221   -1.881  -0.501  1.00 63.92  ? 222 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 3.622   -7.677  1.240   1.00 24.16  ? 223 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 7.926   -17.809 -11.004 1.00 27.30  ? 224 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? -8.706  -15.683 -1.288  1.00 33.63  ? 225 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 1.300   -24.617 -10.039 1.00 35.44  ? 226 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -6.925  -10.886 -11.479 1.00 50.71  ? 227 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 0.761   -10.112 11.613  1.00 32.33  ? 228 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? -4.355  -7.933  -1.383  1.00 20.93  ? 229 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 14.853  -12.209 -5.472  1.00 54.92  ? 230 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 1.073   -4.455  -10.099 1.00 24.22  ? 231 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -9.659  -20.636 -1.348  1.00 40.61  ? 232 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 3.089   1.299   0.318   1.00 62.57  ? 233 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 9.814   -29.245 3.576   1.00 46.12  ? 234 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -3.169  -21.650 -0.600  1.00 32.16  ? 235 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? -5.259  -7.967  10.051  1.00 41.84  ? 236 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? -6.792  -18.734 -5.616  1.00 42.43  ? 237 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -9.056  -16.340 5.954   1.00 53.62  ? 238 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 18.651  -15.395 7.275   1.00 26.64  ? 239 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 2.246   -24.762 -3.112  1.00 33.02  ? 240 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -8.457  -7.105  8.130   1.00 27.32  ? 241 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 1.211   -18.122 -18.604 1.00 73.94  ? 242 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 6.750   -7.782  1.291   1.00 34.87  ? 243 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -0.647  -23.494 9.484   1.00 49.05  ? 244 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 9.831   -7.922  0.302   1.00 26.72  ? 245 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? -5.143  -10.873 6.813   1.00 52.04  ? 246 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 9.894   -23.060 9.865   1.00 30.44  ? 247 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 9.136   -9.389  -15.706 1.00 54.70  ? 248 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? -5.636  -20.817 5.982   1.00 38.25  ? 249 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? 12.167  -11.816 -4.207  1.00 21.14  ? 250 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? -4.513  -24.428 8.382   1.00 46.29  ? 251 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -8.438  -20.909 -5.542  1.00 57.87  ? 252 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 8.831   -12.686 9.933   1.00 50.15  ? 253 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 10.445  -12.003 -6.046  1.00 26.63  ? 254 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 8.815   -6.186  -2.160  1.00 57.14  ? 255 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 12.913  -26.868 -5.186  1.00 46.41  ? 256 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 6.199   -10.028 -11.907 1.00 43.26  ? 257 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 12.208  -11.292 7.871   1.00 50.63  ? 258 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -7.029  -12.360 6.441   1.00 47.51  ? 259 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 10.260  -5.376  -4.001  1.00 48.99  ? 260 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 12.251  -14.619 -11.579 1.00 52.27  ? 261 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 14.867  -24.127 2.022   1.00 35.58  ? 262 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 5.534   -17.225 10.974  1.00 37.11  ? 263 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -1.907  -29.126 10.680  1.00 63.41  ? 264 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 5.792   -15.434 -14.684 1.00 40.12  ? 265 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? -8.887  -16.074 1.491   1.00 50.19  ? 266 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 8.764   -8.909  -13.345 1.00 35.04  ? 267 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? -0.983  -8.463  -13.517 1.00 49.15  ? 268 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -9.516  -20.421 -3.548  1.00 55.63  ? 269 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 1.299   -5.991  5.300   1.00 37.26  ? 270 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? 8.487   -19.952 -17.813 1.00 50.65  ? 271 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? -5.905  -25.109 -6.085  1.00 48.60  ? 272 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? 6.824   -17.399 -14.923 1.00 42.57  ? 273 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? 16.222  -17.521 -9.573  1.00 37.19  ? 274 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? -4.544  -7.321  -11.083 1.00 44.12  ? 275 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 4.061   -7.428  3.826   1.00 38.71  ? 276 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 7.233   -17.254 8.856   1.00 63.34  ? 277 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 20.111  -16.606 -3.423  1.00 25.98  ? 278 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? 2.338   -29.380 -0.865  1.00 43.83  ? 279 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? -2.031  -27.551 -6.769  1.00 84.11  ? 280 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -7.976  -11.360 -8.051  1.00 30.17  ? 281 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 4.932   -5.738  0.554   1.00 36.96  ? 282 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? -10.449 -16.281 7.389   1.00 53.68  ? 283 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? -2.759  -6.863  11.283  1.00 50.32  ? 284 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 16.452  -13.175 -16.317 1.00 44.70  ? 285 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? 21.242  -16.321 -0.441  1.00 34.02  ? 286 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? -3.899  -29.318 7.023   1.00 57.12  ? 287 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 4.138   -33.949 3.878   1.00 70.80  ? 288 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? -6.957  -26.527 3.520   1.00 44.88  ? 289 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? -7.957  -18.851 7.015   1.00 87.37  ? 290 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? 14.321  -27.932 -1.049  1.00 50.98  ? 291 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? 2.660   -9.289  -13.139 1.00 50.71  ? 292 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? 0.369   5.002   -2.947  1.00 56.70  ? 293 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 8.356   -9.991  6.067   1.00 55.81  ? 294 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? 15.639  -9.621  -9.640  1.00 45.97  ? 295 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? -11.511 -12.068 -2.539  1.00 64.86  ? 296 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? -8.168  -14.264 -9.371  1.00 41.35  ? 297 HOH A O   1 
HETATM 2310 O O   . HOH M 5 .  ? -11.616 -16.627 -2.954  1.00 46.70  ? 298 HOH A O   1 
HETATM 2311 O O   . HOH M 5 .  ? 7.455   -28.889 -7.379  1.00 71.81  ? 299 HOH A O   1 
HETATM 2312 O O   . HOH M 5 .  ? -11.124 -27.989 -1.716  1.00 56.87  ? 300 HOH A O   1 
HETATM 2313 O O   . HOH M 5 .  ? 7.676   -16.712 -13.201 1.00 32.48  ? 301 HOH A O   1 
HETATM 2314 O O   . HOH M 5 .  ? 4.200   -9.409  -10.933 1.00 47.63  ? 302 HOH A O   1 
HETATM 2315 O O   . HOH M 5 .  ? -6.306  -21.182 -7.156  1.00 69.39  ? 303 HOH A O   1 
HETATM 2316 O O   . HOH M 5 .  ? 11.471  -17.615 -14.578 1.00 70.68  ? 304 HOH A O   1 
HETATM 2317 O O   . HOH M 5 .  ? 5.421   -2.626  1.106   1.00 52.28  ? 305 HOH A O   1 
HETATM 2318 O O   . HOH M 5 .  ? -7.419  -22.164 5.830   1.00 40.72  ? 306 HOH A O   1 
HETATM 2319 O O   . HOH M 5 .  ? -9.799  -19.872 4.868   1.00 53.15  ? 307 HOH A O   1 
HETATM 2320 O O   . HOH M 5 .  ? -6.263  -19.732 -8.926  1.00 50.10  ? 308 HOH A O   1 
HETATM 2321 O O   . HOH M 5 .  ? -5.995  -7.128  12.169  1.00 43.04  ? 309 HOH A O   1 
HETATM 2322 O O   . HOH M 5 .  ? 6.298   -29.883 -2.255  1.00 42.05  ? 310 HOH A O   1 
HETATM 2323 O O   . HOH N 5 .  ? 30.590  -9.105  -28.614 1.00 65.46  ? 201 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 17.423  -10.379 -42.823 1.00 52.63  ? 202 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 29.492  -19.245 -39.741 1.00 44.90  ? 203 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 38.762  -12.388 -38.468 1.00 62.28  ? 204 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 10.430  -20.150 -42.704 1.00 58.91  ? 205 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 10.161  -18.621 -32.614 1.00 34.55  ? 206 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 14.414  -6.585  -40.309 1.00 37.94  ? 207 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 13.931  -17.687 -18.473 1.00 35.27  ? 208 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 37.764  -11.452 -25.912 1.00 56.91  ? 209 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 9.310   -11.142 -37.522 1.00 62.77  ? 210 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 25.616  -4.741  -32.506 1.00 46.84  ? 211 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 16.283  -19.379 -28.088 1.00 24.20  ? 212 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 20.177  -24.843 -29.075 1.00 56.04  ? 213 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 27.387  -8.282  -27.902 1.00 47.82  ? 214 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 25.638  -6.306  -34.267 1.00 39.16  ? 215 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 6.210   -11.798 -25.717 1.00 32.94  ? 216 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 10.882  -20.923 -19.385 1.00 63.63  ? 217 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 19.590  -3.423  -22.488 1.00 54.44  ? 218 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 25.078  -1.078  -28.303 1.00 46.79  ? 219 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 10.171  -16.344 -43.623 1.00 47.35  ? 220 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 23.177  -2.714  -28.548 1.00 35.51  ? 221 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 25.636  -23.413 -30.341 1.00 31.85  ? 222 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 20.837  -13.588 -41.710 1.00 29.23  ? 223 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 17.997  -0.871  -37.707 1.00 28.17  ? 224 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 19.048  -25.398 -33.761 1.00 44.95  ? 225 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 21.190  -23.164 -24.354 1.00 54.30  ? 226 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 5.702   -7.636  -31.791 1.00 46.97  ? 227 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 10.277  -21.673 -32.456 1.00 41.59  ? 228 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 10.823  -23.348 -31.238 1.00 48.93  ? 229 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 23.649  -4.298  -36.034 1.00 29.74  ? 230 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 17.610  4.539   -33.916 1.00 41.65  ? 231 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 22.044  -23.690 -28.066 1.00 50.32  ? 232 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 24.176  0.341   -36.296 1.00 47.90  ? 233 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 20.873  -10.763 -42.092 1.00 34.40  ? 234 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 12.841  -22.415 -19.971 1.00 51.91  ? 235 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 24.131  -4.302  -28.262 1.00 54.97  ? 236 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 13.692  -24.596 -39.759 1.00 46.59  ? 237 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 6.607   -19.260 -34.223 1.00 47.44  ? 238 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 19.791  -27.354 -35.988 1.00 54.68  ? 239 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 29.550  -12.644 -44.295 1.00 56.32  ? 240 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 21.107  3.395   -31.942 1.00 38.96  ? 241 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 24.510  -2.174  -35.441 1.00 90.87  ? 242 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 19.184  -21.266 -22.184 1.00 58.00  ? 243 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 27.122  -17.059 -23.503 1.00 56.89  ? 244 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 7.300   1.369   -37.135 1.00 63.91  ? 245 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 28.072  -16.800 -45.782 1.00 53.16  ? 246 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 26.769  -10.678 -28.100 1.00 44.72  ? 247 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 4.566   -19.103 -24.989 1.00 48.83  ? 248 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 6.933   -18.718 -31.302 1.00 41.30  ? 249 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 17.185  -3.868  -21.207 1.00 46.29  ? 250 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 27.181  -25.003 -34.179 1.00 45.50  ? 251 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 17.806  -26.148 -28.380 1.00 34.76  ? 252 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 18.100  -15.469 -45.032 1.00 30.69  ? 253 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 15.514  -8.561  -42.369 1.00 54.15  ? 254 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 1.416   -12.955 -27.606 1.00 36.83  ? 255 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 23.686  -10.891 -21.029 1.00 41.27  ? 256 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 7.097   -20.476 -28.201 1.00 85.88  ? 257 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 16.986  -0.487  -24.936 1.00 45.56  ? 258 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 7.036   -14.467 -44.327 1.00 55.55  ? 259 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 27.660  -13.863 -23.112 1.00 41.76  ? 260 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 16.884  -23.350 -19.788 1.00 64.67  ? 261 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 24.377  -6.929  -41.733 1.00 43.30  ? 262 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 31.782  -21.927 -37.352 1.00 42.13  ? 263 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 6.717   -7.484  -20.019 1.00 69.23  ? 264 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 7.574   -3.269  -24.683 1.00 57.23  ? 265 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 16.679  1.735   -29.773 1.00 46.31  ? 266 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 2.227   -7.855  -27.103 1.00 52.53  ? 267 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 19.627  -20.613 -19.928 1.00 44.09  ? 268 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 9.793   -6.899  -40.244 1.00 44.68  ? 269 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 31.340  -12.065 -35.866 1.00 54.77  ? 270 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 27.090  -25.443 -31.760 1.00 36.74  ? 271 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 19.659  -9.066  -42.527 1.00 31.01  ? 272 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 8.653   -21.919 -18.476 1.00 37.53  ? 273 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 13.343  -6.380  -41.743 1.00 52.09  ? 274 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 8.097   -20.447 -32.598 1.00 70.94  ? 275 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 19.189  4.123   -32.431 1.00 60.48  ? 276 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 13.900  -22.559 -40.956 1.00 75.74  ? 277 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 5.914   -20.864 -30.165 1.00 62.03  ? 278 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 38.120  -19.428 -41.662 1.00 50.71  ? 279 HOH B O   1 
HETATM 2402 O O   . HOH N 5 .  ? 36.102  -11.245 -35.345 1.00 40.08  ? 280 HOH B O   1 
HETATM 2403 O O   . HOH N 5 .  ? 6.844   -9.325  -18.319 1.00 49.46  ? 281 HOH B O   1 
HETATM 2404 O O   . HOH N 5 .  ? 16.696  2.799   -24.961 1.00 50.30  ? 282 HOH B O   1 
HETATM 2405 O O   . HOH N 5 .  ? 18.360  -33.209 -21.592 1.00 51.11  ? 283 HOH B O   1 
HETATM 2406 O O   . HOH O 5 .  ? 29.283  -26.213 31.185  1.00 40.40  ? 201 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 24.861  -38.368 12.541  1.00 40.85  ? 202 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 18.684  -40.908 12.333  1.00 33.20  ? 203 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 20.873  -27.809 11.084  1.00 31.32  ? 204 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 11.552  -30.824 8.521   1.00 50.24  ? 205 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 21.688  -40.373 18.586  1.00 36.64  ? 206 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 25.004  -36.583 10.131  1.00 54.96  ? 207 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 20.265  -36.600 8.144   1.00 46.56  ? 208 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 3.274   -25.641 30.774  1.00 52.91  ? 209 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 13.554  -20.707 12.089  1.00 35.15  ? 210 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 26.259  -36.192 24.465  1.00 47.25  ? 211 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 15.387  -36.820 20.209  1.00 48.88  ? 212 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 13.169  -38.498 17.031  1.00 53.99  ? 213 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 24.786  -19.951 6.104   1.00 57.72  ? 214 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 23.779  -30.661 10.773  1.00 39.67  ? 215 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 21.424  -21.320 7.373   1.00 40.24  ? 216 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 12.457  -29.138 4.239   1.00 66.50  ? 217 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 19.755  -27.803 8.383   1.00 37.77  ? 218 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 4.272   -25.889 16.687  1.00 38.79  ? 219 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 14.731  -17.107 19.135  1.00 42.93  ? 220 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 28.810  -31.064 15.803  1.00 48.01  ? 221 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 20.642  -33.751 16.583  1.00 26.30  ? 222 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 26.476  -36.652 15.956  1.00 41.17  ? 223 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 16.591  -16.310 14.300  1.00 37.12  ? 224 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 13.479  -36.374 13.584  1.00 52.83  ? 225 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 30.199  -37.457 29.121  1.00 60.28  ? 226 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 25.035  -17.697 20.727  1.00 37.20  ? 227 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 29.817  -32.934 35.366  1.00 55.91  ? 228 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 29.412  -34.770 28.790  1.00 51.85  ? 229 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 24.905  -17.171 13.366  1.00 33.30  ? 230 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 10.904  -37.215 26.062  1.00 48.09  ? 231 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 7.806   -33.362 9.669   1.00 38.33  ? 232 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 9.252   -13.579 14.946  1.00 45.98  ? 233 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 28.806  -38.691 30.993  1.00 66.02  ? 234 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 8.187   -18.023 23.674  1.00 35.09  ? 235 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 25.386  -33.148 34.437  1.00 53.19  ? 236 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 2.197   -28.385 13.053  1.00 55.02  ? 237 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 28.344  -40.123 26.251  1.00 52.47  ? 238 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 27.205  -38.409 24.676  1.00 51.01  ? 239 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 29.655  -29.210 12.156  1.00 39.76  ? 240 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 28.873  -31.927 17.968  1.00 43.29  ? 241 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 21.413  -17.777 21.500  1.00 39.31  ? 242 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 30.639  -41.950 15.269  1.00 54.69  ? 243 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 7.693   -30.142 11.614  1.00 55.59  ? 244 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 19.125  -39.095 26.845  1.00 48.69  ? 245 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 5.064   -33.131 18.317  1.00 74.54  ? 246 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 20.043  -11.984 15.823  1.00 48.35  ? 247 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 10.573  -29.820 27.866  1.00 86.97  ? 248 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 21.158  -13.234 13.086  1.00 44.39  ? 249 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 30.782  -42.049 11.963  1.00 44.02  ? 250 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 29.733  -16.969 9.785   1.00 52.72  ? 251 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 18.548  -18.106 24.617  1.00 36.21  ? 252 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 20.039  -28.365 4.726   1.00 69.13  ? 253 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 11.680  -38.525 9.331   1.00 56.36  ? 254 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 20.136  -39.904 38.490  1.00 56.93  ? 255 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 23.699  -39.198 20.453  1.00 35.13  ? 256 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 26.953  -14.393 12.924  1.00 48.00  ? 257 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 22.952  -15.834 11.765  1.00 38.01  ? 258 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 10.872  -20.759 10.650  1.00 37.36  ? 259 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 15.979  -18.453 28.946  1.00 56.28  ? 260 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 12.791  -22.054 28.024  1.00 74.18  ? 261 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 32.056  -34.080 33.471  1.00 58.39  ? 262 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 18.469  -18.230 10.723  1.00 52.35  ? 263 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 24.717  -13.717 10.971  1.00 48.94  ? 264 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 15.839  -16.173 24.462  1.00 45.23  ? 265 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 3.854   -23.393 17.920  1.00 68.29  ? 266 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 28.656  -23.290 15.333  1.00 46.77  ? 267 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 1.349   -21.298 17.380  1.00 56.67  ? 268 HOH C O   1 
# 
