data_7HH7
# 
_entry.id   7HH7 
# 
_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   7HH7         pdb_00007hh7 10.2210/pdb7hh7/pdb 
WWPDB D_1001407469 ?            ?                   
# 
_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                        7HH7 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn 1-cyclohexyl-N-methylmethanesulfonamide            191.291   1   ? ?    ? ? 
5 water       nat water                                              18.015    233 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                           SO4 
3 1,2-ETHANEDIOL                          EDO 
4 1-cyclohexyl-N-methylmethanesulfonamide LJR 
5 water                                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                 ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                              ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                         ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                          'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                               ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                         ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                 ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                               ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                   ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                              ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                 ?                 'C6 H13 N O2'    131.173 
LJR non-polymer         . 1-cyclohexyl-N-methylmethanesulfonamide ?                 'C8 H17 N O2 S'  191.291 
LYS 'L-peptide linking' y LYSINE                                  ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                              ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                           ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                 ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                  ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                           ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                               ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                              ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                  ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 ?  ?   ?   B . n 
B 1 35 LYS 35 34 ?  ?   ?   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 ?  ?   ?   B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  ?  ?   ?   C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   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        LJR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LJR 
_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 LJR 1   103 101 LJR LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 304 HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 84  HOH HOH A . 
M 5 HOH 5   205 259 HOH HOH A . 
M 5 HOH 6   206 71  HOH HOH A . 
M 5 HOH 7   207 208 HOH HOH A . 
M 5 HOH 8   208 66  HOH HOH A . 
M 5 HOH 9   209 293 HOH HOH A . 
M 5 HOH 10  210 292 HOH HOH A . 
M 5 HOH 11  211 152 HOH HOH A . 
M 5 HOH 12  212 55  HOH HOH A . 
M 5 HOH 13  213 289 HOH HOH A . 
M 5 HOH 14  214 95  HOH HOH A . 
M 5 HOH 15  215 139 HOH HOH A . 
M 5 HOH 16  216 86  HOH HOH A . 
M 5 HOH 17  217 301 HOH HOH A . 
M 5 HOH 18  218 167 HOH HOH A . 
M 5 HOH 19  219 38  HOH HOH A . 
M 5 HOH 20  220 116 HOH HOH A . 
M 5 HOH 21  221 97  HOH HOH A . 
M 5 HOH 22  222 188 HOH HOH A . 
M 5 HOH 23  223 8   HOH HOH A . 
M 5 HOH 24  224 87  HOH HOH A . 
M 5 HOH 25  225 91  HOH HOH A . 
M 5 HOH 26  226 290 HOH HOH A . 
M 5 HOH 27  227 94  HOH HOH A . 
M 5 HOH 28  228 23  HOH HOH A . 
M 5 HOH 29  229 142 HOH HOH A . 
M 5 HOH 30  230 199 HOH HOH A . 
M 5 HOH 31  231 32  HOH HOH A . 
M 5 HOH 32  232 34  HOH HOH A . 
M 5 HOH 33  233 28  HOH HOH A . 
M 5 HOH 34  234 37  HOH HOH A . 
M 5 HOH 35  235 26  HOH HOH A . 
M 5 HOH 36  236 7   HOH HOH A . 
M 5 HOH 37  237 1   HOH HOH A . 
M 5 HOH 38  238 260 HOH HOH A . 
M 5 HOH 39  239 41  HOH HOH A . 
M 5 HOH 40  240 93  HOH HOH A . 
M 5 HOH 41  241 58  HOH HOH A . 
M 5 HOH 42  242 274 HOH HOH A . 
M 5 HOH 43  243 111 HOH HOH A . 
M 5 HOH 44  244 2   HOH HOH A . 
M 5 HOH 45  245 18  HOH HOH A . 
M 5 HOH 46  246 60  HOH HOH A . 
M 5 HOH 47  247 278 HOH HOH A . 
M 5 HOH 48  248 42  HOH HOH A . 
M 5 HOH 49  249 12  HOH HOH A . 
M 5 HOH 50  250 77  HOH HOH A . 
M 5 HOH 51  251 78  HOH HOH A . 
M 5 HOH 52  252 99  HOH HOH A . 
M 5 HOH 53  253 288 HOH HOH A . 
M 5 HOH 54  254 190 HOH HOH A . 
M 5 HOH 55  255 267 HOH HOH A . 
M 5 HOH 56  256 27  HOH HOH A . 
M 5 HOH 57  257 203 HOH HOH A . 
M 5 HOH 58  258 300 HOH HOH A . 
M 5 HOH 59  259 299 HOH HOH A . 
M 5 HOH 60  260 20  HOH HOH A . 
M 5 HOH 61  261 287 HOH HOH A . 
M 5 HOH 62  262 73  HOH HOH A . 
M 5 HOH 63  263 179 HOH HOH A . 
M 5 HOH 64  264 222 HOH HOH A . 
M 5 HOH 65  265 109 HOH HOH A . 
M 5 HOH 66  266 297 HOH HOH A . 
M 5 HOH 67  267 14  HOH HOH A . 
M 5 HOH 68  268 165 HOH HOH A . 
M 5 HOH 69  269 115 HOH HOH A . 
M 5 HOH 70  270 21  HOH HOH A . 
M 5 HOH 71  271 281 HOH HOH A . 
M 5 HOH 72  272 143 HOH HOH A . 
M 5 HOH 73  273 318 HOH HOH A . 
M 5 HOH 74  274 211 HOH HOH A . 
M 5 HOH 75  275 31  HOH HOH A . 
M 5 HOH 76  276 9   HOH HOH A . 
M 5 HOH 77  277 164 HOH HOH A . 
M 5 HOH 78  278 145 HOH HOH A . 
M 5 HOH 79  279 19  HOH HOH A . 
M 5 HOH 80  280 47  HOH HOH A . 
M 5 HOH 81  281 218 HOH HOH A . 
M 5 HOH 82  282 16  HOH HOH A . 
M 5 HOH 83  283 64  HOH HOH A . 
M 5 HOH 84  284 131 HOH HOH A . 
M 5 HOH 85  285 113 HOH HOH A . 
M 5 HOH 86  286 22  HOH HOH A . 
M 5 HOH 87  287 327 HOH HOH A . 
M 5 HOH 88  288 296 HOH HOH A . 
M 5 HOH 89  289 210 HOH HOH A . 
M 5 HOH 90  290 83  HOH HOH A . 
M 5 HOH 91  291 270 HOH HOH A . 
M 5 HOH 92  292 63  HOH HOH A . 
M 5 HOH 93  293 219 HOH HOH A . 
M 5 HOH 94  294 185 HOH HOH A . 
M 5 HOH 95  295 324 HOH HOH A . 
M 5 HOH 96  296 283 HOH HOH A . 
M 5 HOH 97  297 205 HOH HOH A . 
M 5 HOH 98  298 35  HOH HOH A . 
M 5 HOH 99  299 57  HOH HOH A . 
M 5 HOH 100 300 332 HOH HOH A . 
M 5 HOH 101 301 75  HOH HOH A . 
M 5 HOH 102 302 156 HOH HOH A . 
M 5 HOH 103 303 313 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 89  HOH HOH B . 
N 5 HOH 3   203 184 HOH HOH B . 
N 5 HOH 4   204 331 HOH HOH B . 
N 5 HOH 5   205 258 HOH HOH B . 
N 5 HOH 6   206 98  HOH HOH B . 
N 5 HOH 7   207 249 HOH HOH B . 
N 5 HOH 8   208 272 HOH HOH B . 
N 5 HOH 9   209 123 HOH HOH B . 
N 5 HOH 10  210 69  HOH HOH B . 
N 5 HOH 11  211 279 HOH HOH B . 
N 5 HOH 12  212 214 HOH HOH B . 
N 5 HOH 13  213 172 HOH HOH B . 
N 5 HOH 14  214 54  HOH HOH B . 
N 5 HOH 15  215 329 HOH HOH B . 
N 5 HOH 16  216 117 HOH HOH B . 
N 5 HOH 17  217 224 HOH HOH B . 
N 5 HOH 18  218 261 HOH HOH B . 
N 5 HOH 19  219 215 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  222 119 HOH HOH B . 
N 5 HOH 23  223 5   HOH HOH B . 
N 5 HOH 24  224 6   HOH HOH B . 
N 5 HOH 25  225 169 HOH HOH B . 
N 5 HOH 26  226 10  HOH HOH B . 
N 5 HOH 27  227 36  HOH HOH B . 
N 5 HOH 28  228 137 HOH HOH B . 
N 5 HOH 29  229 168 HOH HOH B . 
N 5 HOH 30  230 17  HOH HOH B . 
N 5 HOH 31  231 59  HOH HOH B . 
N 5 HOH 32  232 153 HOH HOH B . 
N 5 HOH 33  233 175 HOH HOH B . 
N 5 HOH 34  234 101 HOH HOH B . 
N 5 HOH 35  235 242 HOH HOH B . 
N 5 HOH 36  236 25  HOH HOH B . 
N 5 HOH 37  237 96  HOH HOH B . 
N 5 HOH 38  238 24  HOH HOH B . 
N 5 HOH 39  239 280 HOH HOH B . 
N 5 HOH 40  240 61  HOH HOH B . 
N 5 HOH 41  241 320 HOH HOH B . 
N 5 HOH 42  242 197 HOH HOH B . 
N 5 HOH 43  243 157 HOH HOH B . 
N 5 HOH 44  244 79  HOH HOH B . 
N 5 HOH 45  245 76  HOH HOH B . 
N 5 HOH 46  246 120 HOH HOH B . 
N 5 HOH 47  247 223 HOH HOH B . 
N 5 HOH 48  248 46  HOH HOH B . 
N 5 HOH 49  249 315 HOH HOH B . 
N 5 HOH 50  250 303 HOH HOH B . 
N 5 HOH 51  251 72  HOH HOH B . 
N 5 HOH 52  252 74  HOH HOH B . 
N 5 HOH 53  253 319 HOH HOH B . 
N 5 HOH 54  254 44  HOH HOH B . 
N 5 HOH 55  255 217 HOH HOH B . 
N 5 HOH 56  256 13  HOH HOH B . 
N 5 HOH 57  257 182 HOH HOH B . 
N 5 HOH 58  258 104 HOH HOH B . 
N 5 HOH 59  259 316 HOH HOH B . 
N 5 HOH 60  260 201 HOH HOH B . 
N 5 HOH 61  261 291 HOH HOH B . 
N 5 HOH 62  262 170 HOH HOH B . 
N 5 HOH 63  263 322 HOH HOH B . 
N 5 HOH 64  264 163 HOH HOH B . 
N 5 HOH 65  265 160 HOH HOH B . 
N 5 HOH 66  266 177 HOH HOH B . 
N 5 HOH 67  267 314 HOH HOH B . 
N 5 HOH 68  268 92  HOH HOH B . 
N 5 HOH 69  269 107 HOH HOH B . 
N 5 HOH 70  270 312 HOH HOH B . 
N 5 HOH 71  271 310 HOH HOH B . 
O 5 HOH 1   201 323 HOH HOH C . 
O 5 HOH 2   202 321 HOH HOH C . 
O 5 HOH 3   203 254 HOH HOH C . 
O 5 HOH 4   204 226 HOH HOH C . 
O 5 HOH 5   205 161 HOH HOH C . 
O 5 HOH 6   206 317 HOH HOH C . 
O 5 HOH 7   207 173 HOH HOH C . 
O 5 HOH 8   208 271 HOH HOH C . 
O 5 HOH 9   209 85  HOH HOH C . 
O 5 HOH 10  210 134 HOH HOH C . 
O 5 HOH 11  211 118 HOH HOH C . 
O 5 HOH 12  212 189 HOH HOH C . 
O 5 HOH 13  213 284 HOH HOH C . 
O 5 HOH 14  214 15  HOH HOH C . 
O 5 HOH 15  215 102 HOH HOH C . 
O 5 HOH 16  216 269 HOH HOH C . 
O 5 HOH 17  217 49  HOH HOH C . 
O 5 HOH 18  218 90  HOH HOH C . 
O 5 HOH 19  219 298 HOH HOH C . 
O 5 HOH 20  220 126 HOH HOH C . 
O 5 HOH 21  221 4   HOH HOH C . 
O 5 HOH 22  222 122 HOH HOH C . 
O 5 HOH 23  223 325 HOH HOH C . 
O 5 HOH 24  224 40  HOH HOH C . 
O 5 HOH 25  225 82  HOH HOH C . 
O 5 HOH 26  226 149 HOH HOH C . 
O 5 HOH 27  227 45  HOH HOH C . 
O 5 HOH 28  228 295 HOH HOH C . 
O 5 HOH 29  229 209 HOH HOH C . 
O 5 HOH 30  230 302 HOH HOH C . 
O 5 HOH 31  231 56  HOH HOH C . 
O 5 HOH 32  232 275 HOH HOH C . 
O 5 HOH 33  233 48  HOH HOH C . 
O 5 HOH 34  234 43  HOH HOH C . 
O 5 HOH 35  235 62  HOH HOH C . 
O 5 HOH 36  236 53  HOH HOH C . 
O 5 HOH 37  237 326 HOH HOH C . 
O 5 HOH 38  238 151 HOH HOH C . 
O 5 HOH 39  239 148 HOH HOH C . 
O 5 HOH 40  240 132 HOH HOH C . 
O 5 HOH 41  241 198 HOH HOH C . 
O 5 HOH 42  242 130 HOH HOH C . 
O 5 HOH 43  243 328 HOH HOH C . 
O 5 HOH 44  244 67  HOH HOH C . 
O 5 HOH 45  245 294 HOH HOH C . 
O 5 HOH 46  246 305 HOH HOH C . 
O 5 HOH 47  247 135 HOH HOH C . 
O 5 HOH 48  248 246 HOH HOH C . 
O 5 HOH 49  249 241 HOH HOH C . 
O 5 HOH 50  250 65  HOH HOH C . 
O 5 HOH 51  251 146 HOH HOH C . 
O 5 HOH 52  252 330 HOH HOH C . 
O 5 HOH 53  253 171 HOH HOH C . 
O 5 HOH 54  254 108 HOH HOH C . 
O 5 HOH 55  255 70  HOH HOH C . 
O 5 HOH 56  256 103 HOH HOH C . 
O 5 HOH 57  257 309 HOH HOH C . 
O 5 HOH 58  258 206 HOH HOH C . 
O 5 HOH 59  259 125 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
15 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
16 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
17 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
18 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
19 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
20 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
21 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
22 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
23 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
24 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
25 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
26 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
27 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
28 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
29 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
30 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
31 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
32 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
33 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
34 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
35 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
36 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
37 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
38 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
39 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
40 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
41 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
42 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
43 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
44 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
45 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
46 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
47 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
48 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
49 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
50 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
51 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
52 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
53 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HH7 
_cell.length_a           41.520 
_cell.length_b           42.080 
_cell.length_c           158.230 
_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                         7HH7 
_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          7HH7 
_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                     7HH7 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.08 
_reflns.d_resolution_high            1.73 
_reflns.number_obs                   29935 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.120 
_reflns.pdbx_netI_over_sigmaI        8.3 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.131 
_reflns.pdbx_Rpim_I_all              0.051 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     194552 
_reflns.pdbx_chi_squared             0.99 
_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                  1.73 
_reflns_shell.d_res_low                   1.77 
_reflns_shell.number_measured_all         14379 
_reflns_shell.number_unique_obs           2137 
_reflns_shell.Rmerge_I_obs                2.795 
_reflns_shell.pdbx_chi_squared            0.90 
_reflns_shell.pdbx_redundancy             6.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             3.029 
_reflns_shell.pdbx_Rpim_I_all             1.157 
_reflns_shell.pdbx_CC_half                0.305 
_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                                 7HH7 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     28294 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.70 
_refine.ls_d_res_high                            1.73 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_R_factor_obs                          0.21129 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20921 
_refine.ls_R_factor_R_free                       0.24831 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  1572 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               36.982 
_refine.aniso_B[1][1]                            0.74 
_refine.aniso_B[2][2]                            0.09 
_refine.aniso_B[3][3]                            -0.83 
_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                       0.132 
_refine.pdbx_overall_ESU_R_Free                  0.127 
_refine.overall_SU_ML                            0.115 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.858 
_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        2091 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             233 
_refine_hist.number_atoms_total               2374 
_refine_hist.d_res_high                       1.73 
_refine_hist.d_res_low                        40.70 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.012  ? 2242 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.741  1.833  ? 3050 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.211  5.000  ? 259  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       4.821  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.653 10.000 ? 291  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.124  0.200  ? 281  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1830 '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                  3.454  3.451  ? 1049 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.887  6.157  ? 1304 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.412  3.780  ? 1193 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.482  51.27  ? 3458 '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                       1.730 
_refine_ls_shell.d_res_low                        1.775 
_refine_ls_shell.number_reflns_R_work             1985 
_refine_ls_shell.R_factor_R_work                  0.370 
_refine_ls_shell.percent_reflns_obs               99.86 
_refine_ls_shell.R_factor_R_free                  0.375 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             146 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH7 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1003207278' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH7 
_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 7HH7 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH7 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH7 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 7HH7 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH7 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH7 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH7 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH7 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH7 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 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P5 AA5 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P6 AA6 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P7 AA7 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P8 AA8 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HH7 
_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 239 ? ? O B HOH 263 ? ? 1.68 
2 1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.01 
3 1 OD1 C ASP 9   ? ? O C HOH 201 ? ? 2.05 
4 1 O   B HOH 225 ? ? O B HOH 264 ? ? 2.08 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     295 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     251 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_445 
_pdbx_validate_symm_contact.dist              1.91 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -151.57 65.66   
2 1 ASN B 87 ? ? -159.69 58.88   
3 1 ASN C 87 ? ? -153.89 54.64   
4 1 ALA C 90 ? ? -61.10  -179.36 
# 
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 A 11 ? ? PHE A 12 ? ? 149.69 
2 1 VAL B 11 ? ? PHE B 12 ? ? 149.73 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 B VAL 33 ? B VAL 34 
8  1 Y 1 B LYS 34 ? B LYS 35 
9  1 Y 1 B LYS 56 ? B LYS 57 
10 1 Y 1 C GLY 0  ? C GLY 1  
11 1 Y 1 C MET 1  ? C MET 2  
12 1 Y 1 C PRO 2  ? C PRO 3  
13 1 Y 1 C HIS 3  ? C HIS 4  
14 1 Y 1 C ASP 27 ? C ASP 28 
15 1 Y 1 C ILE 28 ? C ILE 29 
16 1 Y 1 C ALA 29 ? C ALA 30 
17 1 Y 1 C ASP 30 ? C ASP 31 
18 1 Y 1 C GLY 31 ? C GLY 32 
19 1 Y 1 C ALA 32 ? C ALA 33 
20 1 Y 1 C VAL 33 ? C VAL 34 
21 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LJR N1   N N N 215 
LJR C4   C N N 216 
LJR C5   C N N 217 
LJR C6   C N N 218 
LJR C7   C N N 219 
LJR C8   C N N 220 
LJR C1   C N N 221 
LJR S1   S N N 222 
LJR O1   O N N 223 
LJR O2   O N N 224 
LJR C2   C N N 225 
LJR C3   C N N 226 
LJR H1   H N N 227 
LJR H2   H N N 228 
LJR H3   H N N 229 
LJR H4   H N N 230 
LJR H5   H N N 231 
LJR H6   H N N 232 
LJR H7   H N N 233 
LJR H8   H N N 234 
LJR H9   H N N 235 
LJR H10  H N N 236 
LJR H11  H N N 237 
LJR H12  H N N 238 
LJR H13  H N N 239 
LJR H14  H N N 240 
LJR H15  H N N 241 
LJR H16  H N N 242 
LJR H17  H N N 243 
LYS N    N N N 244 
LYS CA   C N S 245 
LYS C    C N N 246 
LYS O    O N N 247 
LYS CB   C N N 248 
LYS CG   C N N 249 
LYS CD   C N N 250 
LYS CE   C N N 251 
LYS NZ   N N N 252 
LYS OXT  O N N 253 
LYS H    H N N 254 
LYS H2   H N N 255 
LYS HA   H N N 256 
LYS HB2  H N N 257 
LYS HB3  H N N 258 
LYS HG2  H N N 259 
LYS HG3  H N N 260 
LYS HD2  H N N 261 
LYS HD3  H N N 262 
LYS HE2  H N N 263 
LYS HE3  H N N 264 
LYS HZ1  H N N 265 
LYS HZ2  H N N 266 
LYS HZ3  H N N 267 
LYS HXT  H N N 268 
MET N    N N N 269 
MET CA   C N S 270 
MET C    C N N 271 
MET O    O N N 272 
MET CB   C N N 273 
MET CG   C N N 274 
MET SD   S N N 275 
MET CE   C N N 276 
MET OXT  O N N 277 
MET H    H N N 278 
MET H2   H N N 279 
MET HA   H N N 280 
MET HB2  H N N 281 
MET HB3  H N N 282 
MET HG2  H N N 283 
MET HG3  H N N 284 
MET HE1  H N N 285 
MET HE2  H N N 286 
MET HE3  H N N 287 
MET HXT  H N N 288 
PHE N    N N N 289 
PHE CA   C N S 290 
PHE C    C N N 291 
PHE O    O N N 292 
PHE CB   C N N 293 
PHE CG   C Y N 294 
PHE CD1  C Y N 295 
PHE CD2  C Y N 296 
PHE CE1  C Y N 297 
PHE CE2  C Y N 298 
PHE CZ   C Y N 299 
PHE OXT  O N N 300 
PHE H    H N N 301 
PHE H2   H N N 302 
PHE HA   H N N 303 
PHE HB2  H N N 304 
PHE HB3  H N N 305 
PHE HD1  H N N 306 
PHE HD2  H N N 307 
PHE HE1  H N N 308 
PHE HE2  H N N 309 
PHE HZ   H N N 310 
PHE HXT  H N N 311 
PRO N    N N N 312 
PRO CA   C N S 313 
PRO C    C N N 314 
PRO O    O N N 315 
PRO CB   C N N 316 
PRO CG   C N N 317 
PRO CD   C N N 318 
PRO OXT  O N N 319 
PRO H    H N N 320 
PRO HA   H N N 321 
PRO HB2  H N N 322 
PRO HB3  H N N 323 
PRO HG2  H N N 324 
PRO HG3  H N N 325 
PRO HD2  H N N 326 
PRO HD3  H N N 327 
PRO HXT  H N N 328 
SER N    N N N 329 
SER CA   C N S 330 
SER C    C N N 331 
SER O    O N N 332 
SER CB   C N N 333 
SER OG   O N N 334 
SER OXT  O N N 335 
SER H    H N N 336 
SER H2   H N N 337 
SER HA   H N N 338 
SER HB2  H N N 339 
SER HB3  H N N 340 
SER HG   H N N 341 
SER HXT  H N N 342 
SO4 S    S N N 343 
SO4 O1   O N N 344 
SO4 O2   O N N 345 
SO4 O3   O N N 346 
SO4 O4   O N N 347 
THR N    N N N 348 
THR CA   C N S 349 
THR C    C N N 350 
THR O    O N N 351 
THR CB   C N R 352 
THR OG1  O N N 353 
THR CG2  C N N 354 
THR OXT  O N N 355 
THR H    H N N 356 
THR H2   H N N 357 
THR HA   H N N 358 
THR HB   H N N 359 
THR HG1  H N N 360 
THR HG21 H N N 361 
THR HG22 H N N 362 
THR HG23 H N N 363 
THR HXT  H N N 364 
TRP N    N N N 365 
TRP CA   C N S 366 
TRP C    C N N 367 
TRP O    O N N 368 
TRP CB   C N N 369 
TRP CG   C Y N 370 
TRP CD1  C Y N 371 
TRP CD2  C Y N 372 
TRP NE1  N Y N 373 
TRP CE2  C Y N 374 
TRP CE3  C Y N 375 
TRP CZ2  C Y N 376 
TRP CZ3  C Y N 377 
TRP CH2  C Y N 378 
TRP OXT  O N N 379 
TRP H    H N N 380 
TRP H2   H N N 381 
TRP HA   H N N 382 
TRP HB2  H N N 383 
TRP HB3  H N N 384 
TRP HD1  H N N 385 
TRP HE1  H N N 386 
TRP HE3  H N N 387 
TRP HZ2  H N N 388 
TRP HZ3  H N N 389 
TRP HH2  H N N 390 
TRP HXT  H N N 391 
TYR N    N N N 392 
TYR CA   C N S 393 
TYR C    C N N 394 
TYR O    O N N 395 
TYR CB   C N N 396 
TYR CG   C Y N 397 
TYR CD1  C Y N 398 
TYR CD2  C Y N 399 
TYR CE1  C Y N 400 
TYR CE2  C Y N 401 
TYR CZ   C Y N 402 
TYR OH   O N N 403 
TYR OXT  O N N 404 
TYR H    H N N 405 
TYR H2   H N N 406 
TYR HA   H N N 407 
TYR HB2  H N N 408 
TYR HB3  H N N 409 
TYR HD1  H N N 410 
TYR HD2  H N N 411 
TYR HE1  H N N 412 
TYR HE2  H N N 413 
TYR HH   H N N 414 
TYR HXT  H N N 415 
VAL N    N N N 416 
VAL CA   C N S 417 
VAL C    C N N 418 
VAL O    O N N 419 
VAL CB   C N N 420 
VAL CG1  C N N 421 
VAL CG2  C N N 422 
VAL OXT  O N N 423 
VAL H    H N N 424 
VAL H2   H N N 425 
VAL HA   H N N 426 
VAL HB   H N N 427 
VAL HG11 H N N 428 
VAL HG12 H N N 429 
VAL HG13 H N N 430 
VAL HG21 H N N 431 
VAL HG22 H N N 432 
VAL HG23 H N N 433 
VAL HXT  H N N 434 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LJR C1  N1   sing N N 203 
LJR N1  S1   sing N N 204 
LJR C2  S1   sing N N 205 
LJR C2  C3   sing N N 206 
LJR C4  C3   sing N N 207 
LJR C4  C5   sing N N 208 
LJR S1  O1   doub N N 209 
LJR S1  O2   doub N N 210 
LJR C3  C8   sing N N 211 
LJR C5  C6   sing N N 212 
LJR C8  C7   sing N N 213 
LJR C6  C7   sing N N 214 
LJR N1  H1   sing N N 215 
LJR C4  H2   sing N N 216 
LJR C4  H3   sing N N 217 
LJR C5  H4   sing N N 218 
LJR C5  H5   sing N N 219 
LJR C6  H6   sing N N 220 
LJR C6  H7   sing N N 221 
LJR C7  H8   sing N N 222 
LJR C7  H9   sing N N 223 
LJR C8  H10  sing N N 224 
LJR C8  H11  sing N N 225 
LJR C1  H12  sing N N 226 
LJR C1  H13  sing N N 227 
LJR C1  H14  sing N N 228 
LJR C2  H15  sing N N 229 
LJR C2  H16  sing N N 230 
LJR C3  H17  sing N N 231 
LYS N   CA   sing N N 232 
LYS N   H    sing N N 233 
LYS N   H2   sing N N 234 
LYS CA  C    sing N N 235 
LYS CA  CB   sing N N 236 
LYS CA  HA   sing N N 237 
LYS C   O    doub N N 238 
LYS C   OXT  sing N N 239 
LYS CB  CG   sing N N 240 
LYS CB  HB2  sing N N 241 
LYS CB  HB3  sing N N 242 
LYS CG  CD   sing N N 243 
LYS CG  HG2  sing N N 244 
LYS CG  HG3  sing N N 245 
LYS CD  CE   sing N N 246 
LYS CD  HD2  sing N N 247 
LYS CD  HD3  sing N N 248 
LYS CE  NZ   sing N N 249 
LYS CE  HE2  sing N N 250 
LYS CE  HE3  sing N N 251 
LYS NZ  HZ1  sing N N 252 
LYS NZ  HZ2  sing N N 253 
LYS NZ  HZ3  sing N N 254 
LYS OXT HXT  sing N N 255 
MET N   CA   sing N N 256 
MET N   H    sing N N 257 
MET N   H2   sing N N 258 
MET CA  C    sing N N 259 
MET CA  CB   sing N N 260 
MET CA  HA   sing N N 261 
MET C   O    doub N N 262 
MET C   OXT  sing N N 263 
MET CB  CG   sing N N 264 
MET CB  HB2  sing N N 265 
MET CB  HB3  sing N N 266 
MET CG  SD   sing N N 267 
MET CG  HG2  sing N N 268 
MET CG  HG3  sing N N 269 
MET SD  CE   sing N N 270 
MET CE  HE1  sing N N 271 
MET CE  HE2  sing N N 272 
MET CE  HE3  sing N N 273 
MET OXT HXT  sing N N 274 
PHE N   CA   sing N N 275 
PHE N   H    sing N N 276 
PHE N   H2   sing N N 277 
PHE CA  C    sing N N 278 
PHE CA  CB   sing N N 279 
PHE CA  HA   sing N N 280 
PHE C   O    doub N N 281 
PHE C   OXT  sing N N 282 
PHE CB  CG   sing N N 283 
PHE CB  HB2  sing N N 284 
PHE CB  HB3  sing N N 285 
PHE CG  CD1  doub Y N 286 
PHE CG  CD2  sing Y N 287 
PHE CD1 CE1  sing Y N 288 
PHE CD1 HD1  sing N N 289 
PHE CD2 CE2  doub Y N 290 
PHE CD2 HD2  sing N N 291 
PHE CE1 CZ   doub Y N 292 
PHE CE1 HE1  sing N N 293 
PHE CE2 CZ   sing Y N 294 
PHE CE2 HE2  sing N N 295 
PHE CZ  HZ   sing N N 296 
PHE OXT HXT  sing N N 297 
PRO N   CA   sing N N 298 
PRO N   CD   sing N N 299 
PRO N   H    sing N N 300 
PRO CA  C    sing N N 301 
PRO CA  CB   sing N N 302 
PRO CA  HA   sing N N 303 
PRO C   O    doub N N 304 
PRO C   OXT  sing N N 305 
PRO CB  CG   sing N N 306 
PRO CB  HB2  sing N N 307 
PRO CB  HB3  sing N N 308 
PRO CG  CD   sing N N 309 
PRO CG  HG2  sing N N 310 
PRO CG  HG3  sing N N 311 
PRO CD  HD2  sing N N 312 
PRO CD  HD3  sing N N 313 
PRO OXT HXT  sing N N 314 
SER N   CA   sing N N 315 
SER N   H    sing N N 316 
SER N   H2   sing N N 317 
SER CA  C    sing N N 318 
SER CA  CB   sing N N 319 
SER CA  HA   sing N N 320 
SER C   O    doub N N 321 
SER C   OXT  sing N N 322 
SER CB  OG   sing N N 323 
SER CB  HB2  sing N N 324 
SER CB  HB3  sing N N 325 
SER OG  HG   sing N N 326 
SER OXT HXT  sing N N 327 
SO4 S   O1   doub N N 328 
SO4 S   O2   doub N N 329 
SO4 S   O3   sing N N 330 
SO4 S   O4   sing N N 331 
THR N   CA   sing N N 332 
THR N   H    sing N N 333 
THR N   H2   sing N N 334 
THR CA  C    sing N N 335 
THR CA  CB   sing N N 336 
THR CA  HA   sing N N 337 
THR C   O    doub N N 338 
THR C   OXT  sing N N 339 
THR CB  OG1  sing N N 340 
THR CB  CG2  sing N N 341 
THR CB  HB   sing N N 342 
THR OG1 HG1  sing N N 343 
THR CG2 HG21 sing N N 344 
THR CG2 HG22 sing N N 345 
THR CG2 HG23 sing N N 346 
THR OXT HXT  sing N N 347 
TRP N   CA   sing N N 348 
TRP N   H    sing N N 349 
TRP N   H2   sing N N 350 
TRP CA  C    sing N N 351 
TRP CA  CB   sing N N 352 
TRP CA  HA   sing N N 353 
TRP C   O    doub N N 354 
TRP C   OXT  sing N N 355 
TRP CB  CG   sing N N 356 
TRP CB  HB2  sing N N 357 
TRP CB  HB3  sing N N 358 
TRP CG  CD1  doub Y N 359 
TRP CG  CD2  sing Y N 360 
TRP CD1 NE1  sing Y N 361 
TRP CD1 HD1  sing N N 362 
TRP CD2 CE2  doub Y N 363 
TRP CD2 CE3  sing Y N 364 
TRP NE1 CE2  sing Y N 365 
TRP NE1 HE1  sing N N 366 
TRP CE2 CZ2  sing Y N 367 
TRP CE3 CZ3  doub Y N 368 
TRP CE3 HE3  sing N N 369 
TRP CZ2 CH2  doub Y N 370 
TRP CZ2 HZ2  sing N N 371 
TRP CZ3 CH2  sing Y N 372 
TRP CZ3 HZ3  sing N N 373 
TRP CH2 HH2  sing N N 374 
TRP OXT HXT  sing N N 375 
TYR N   CA   sing N N 376 
TYR N   H    sing N N 377 
TYR N   H2   sing N N 378 
TYR CA  C    sing N N 379 
TYR CA  CB   sing N N 380 
TYR CA  HA   sing N N 381 
TYR C   O    doub N N 382 
TYR C   OXT  sing N N 383 
TYR CB  CG   sing N N 384 
TYR CB  HB2  sing N N 385 
TYR CB  HB3  sing N N 386 
TYR CG  CD1  doub Y N 387 
TYR CG  CD2  sing Y N 388 
TYR CD1 CE1  sing Y N 389 
TYR CD1 HD1  sing N N 390 
TYR CD2 CE2  doub Y N 391 
TYR CD2 HD2  sing N N 392 
TYR CE1 CZ   doub Y N 393 
TYR CE1 HE1  sing N N 394 
TYR CE2 CZ   sing Y N 395 
TYR CE2 HE2  sing N N 396 
TYR CZ  OH   sing N N 397 
TYR OH  HH   sing N N 398 
TYR OXT HXT  sing N N 399 
VAL N   CA   sing N N 400 
VAL N   H    sing N N 401 
VAL N   H2   sing N N 402 
VAL CA  C    sing N N 403 
VAL CA  CB   sing N N 404 
VAL CA  HA   sing N N 405 
VAL C   O    doub N N 406 
VAL C   OXT  sing N N 407 
VAL CB  CG1  sing N N 408 
VAL CB  CG2  sing N N 409 
VAL CB  HB   sing N N 410 
VAL CG1 HG11 sing N N 411 
VAL CG1 HG12 sing N N 412 
VAL CG1 HG13 sing N N 413 
VAL CG2 HG21 sing N N 414 
VAL CG2 HG22 sing N N 415 
VAL CG2 HG23 sing N N 416 
VAL OXT HXT  sing N N 417 
# 
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                    7HH7 
_atom_sites.fract_transf_matrix[1][1]   0.024085 
_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]   0.023764 
_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]   0.006320 
_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  ? 0.469   4.381   2.438   1.00 50.73  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.525  3.538   1.723   1.00 59.31  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.159   2.447   0.890   1.00 52.04  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.288   2.606   0.433   1.00 49.63  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.478  4.384   0.868   1.00 62.79  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.484  5.191   1.681   1.00 77.82  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.621  4.277   2.752   1.00 79.36  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.555  5.604   3.531   1.00 76.95  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.501  1.272   0.731   1.00 47.51  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.069  0.212   -0.193  1.00 41.11  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.190   0.606   -1.650  1.00 40.05  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.525  1.431   -2.218  1.00 38.34  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.295  -0.781  -0.104  1.00 40.83  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.768  -0.615  1.329   1.00 43.15  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.700  0.889   1.504   1.00 44.68  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.209   -0.014  -2.255  1.00 37.32  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.397   0.103   -3.686  1.00 37.63  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.772   -1.145  -4.286  1.00 37.89  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.201   -1.961  -3.549  1.00 36.69  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.889   0.210   -4.034  1.00 41.04  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.533   1.502   -3.622  1.00 54.41  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.447   2.049   -2.358  1.00 62.54  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.301   2.351   -4.331  1.00 62.78  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.118   3.194   -2.319  1.00 62.48  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.655   3.391   -3.503  1.00 62.84  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.871   -1.265  -5.610  1.00 32.39  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.613   -2.533  -6.272  1.00 33.23  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.721   -3.521  -5.908  1.00 29.86  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.801   -3.133  -5.451  1.00 29.52  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.480   -2.319  -7.761  1.00 35.64  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.440   -4.816  -6.067  1.00 29.28  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.459   -5.827  -5.839  1.00 28.38  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.605   -5.694  -6.841  1.00 26.70  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.382   -5.363  -8.002  1.00 27.94  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.868   -7.230  -5.972  1.00 24.43  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.130   -7.631  -4.700  1.00 26.79  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.843   -7.869  -3.517  1.00 24.80  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.254  -7.821  -4.707  1.00 22.40  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.181   -8.219  -2.344  1.00 26.70  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.898  -8.271  -3.542  1.00 22.18  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.189  -8.425  -2.366  1.00 24.92  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.835   -5.967  -6.371  1.00 22.70  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.000   -5.896  -7.237  1.00 24.99  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.917   -7.100  -6.962  1.00 23.99  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.863   -7.726  -5.915  1.00 21.67  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.740   -4.572  -6.988  1.00 30.64  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.426   -4.511  -5.635  1.00 29.88  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.165   -3.190  -5.375  1.00 37.38  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.770   -3.058  -4.010  1.00 39.49  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.766   -3.157  -2.952  1.00 31.99  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.751   -7.505  -7.940  1.00 24.06  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.672   -8.621  -7.736  1.00 25.35  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.466   -8.358  -6.449  1.00 22.42  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.900   -7.229  -6.195  1.00 24.90  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.530   -8.567  -9.063  1.00 24.27  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.591   -7.924  -10.120 1.00 28.10  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.827   -6.895  -9.291  1.00 26.14  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.612   -9.406  -5.615  1.00 22.17  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.350  -9.313  -4.372  1.00 19.21  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.436   -9.156  -3.153  1.00 22.08  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.841   -9.433  -2.005  1.00 24.41  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.184   -8.716  -3.371  1.00 19.68  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.242   -8.707  -2.255  1.00 19.34  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.036   -10.090 -1.628  1.00 19.07  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.896   -11.078 -2.328  1.00 20.49  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.898   -8.125  -2.688  1.00 20.92  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.914   -6.615  -2.879  1.00 24.33  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.886   -5.953  -2.402  1.00 24.83  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 4.973   -6.105  -3.511  1.00 23.63  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.899   -10.146 -0.292  1.00 18.99  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.731   -11.440 0.366   1.00 18.65  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.280   -11.528 0.823   1.00 20.57  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.715   -10.532 1.350   1.00 21.43  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.667   -11.495 1.581   1.00 18.46  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.147   -11.253 1.252   1.00 18.67  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.001  -11.349 2.503   1.00 21.55  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.521   -12.247 0.144   1.00 19.62  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.723   -12.733 0.681   1.00 19.09  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.308   -12.907 0.920   1.00 17.38  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.059   -14.268 1.565   1.00 21.87  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.937   -15.129 1.584   1.00 20.88  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.499   -12.793 -0.386  1.00 17.95  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.622   -11.391 -0.998  1.00 18.60  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.873   -13.898 -1.375  1.00 18.04  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.829   -14.460 2.075   1.00 20.29  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.235   -15.788 2.111   1.00 21.36  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.275   -15.873 0.927   1.00 24.35  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.509  -14.943 0.717   1.00 21.77  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.454   -16.151 3.395   1.00 20.53  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.409   -16.261 4.573   1.00 20.71  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.796   -15.120 5.283   1.00 21.92  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.933   -17.495 4.953   1.00 23.03  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.717   -15.206 6.324   1.00 28.13  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.875   -17.578 5.977   1.00 27.48  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.252   -16.446 6.672   1.00 27.78  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.375   -16.968 0.139   1.00 24.57  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.415  -17.126 -1.077  1.00 23.27  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.407  -18.281 -0.877  1.00 25.69  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.074  -19.337 -0.312  1.00 23.39  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.502   -17.326 -2.300  1.00 20.08  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.640  -18.069 -1.341  1.00 23.46  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.699  -19.015 -1.028  1.00 24.33  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.111  -19.696 -2.321  1.00 26.71  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.464  -19.020 -3.297  1.00 28.22  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.919  -18.393 -0.334  1.00 27.47  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.998  -19.433 0.055   1.00 32.26  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.550  -20.436 1.130   1.00 31.59  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.675  -21.300 1.714   1.00 35.00  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.225  -22.210 0.699   1.00 32.32  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.026  -21.032 -2.283  1.00 27.41  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.649  -21.842 -3.305  1.00 32.30  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.619  -22.856 -2.720  1.00 34.58  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.463  -23.279 -1.577  1.00 27.54  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.579  -22.522 -4.132  1.00 37.18  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.092  -21.462 -5.111  1.00 40.86  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.795  -22.196 -6.075  1.00 42.44  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -2.642  -23.069 -7.395  1.00 56.55  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.620  -23.185 -3.545  1.00 40.02  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.718  -24.067 -3.181  1.00 40.45  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.126  -25.310 -2.543  1.00 38.54  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.195  -25.906 -3.086  1.00 36.32  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.530  -24.422 -4.434  1.00 48.57  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.887  -25.071 -4.161  1.00 50.80  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.862 -24.209 -3.352  1.00 54.68  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.617  -25.642 -1.342  1.00 34.47  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -7.226  -26.907 -0.755  1.00 35.95  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.846  -26.874 -0.111  1.00 43.48  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.377  -27.908 0.357   1.00 43.51  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.197  -25.696 -0.057  1.00 36.56  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.932  -25.647 0.656   1.00 33.79  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.958  -24.526 1.673   1.00 30.87  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.635  -23.527 1.473   1.00 30.49  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.792  -25.252 -0.285  1.00 39.92  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.459  -26.278 -1.354  1.00 39.50  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -1.557  -27.305 -1.116  1.00 49.66  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -3.046  -26.199 -2.611  1.00 45.63  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -1.249  -28.229 -2.105  1.00 56.23  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.746  -27.109 -3.610  1.00 50.76  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.846  -28.126 -3.353  1.00 64.03  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -1.569  -29.004 -4.366  1.00 85.47  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.190  -24.631 2.777   1.00 29.76  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.140  -23.542 3.762   1.00 30.85  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.451  -22.336 3.104   1.00 30.82  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.693  -22.515 2.158   1.00 27.71  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.306  -24.161 4.902   1.00 31.27  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.413  -25.205 4.200   1.00 32.18  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.261  -25.743 3.067   1.00 32.33  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.738  -21.127 3.593   1.00 25.81  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.993  -19.934 3.211   1.00 25.37  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.489  -20.248 3.289   1.00 27.45  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? -0.011  -20.696 4.332   1.00 27.56  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.444  -18.767 4.090   1.00 25.35  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.897  -18.433 3.897   1.00 26.35  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.933  -19.060 4.579   1.00 32.10  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.467  -17.450 3.176   1.00 26.63  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -6.098  -18.502 4.225   1.00 29.38  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.838  -17.514 3.374   1.00 31.22  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.261   -19.982 2.194   1.00 24.18  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.574   -20.609 2.035   1.00 23.59  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.633   -19.530 1.848   1.00 22.78  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.424   -18.611 1.081   1.00 22.81  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.584   -21.510 0.793   1.00 22.72  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.678   -22.545 0.830   1.00 25.87  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.017   -22.385 0.611   1.00 26.50  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.493   -23.936 1.175   1.00 26.50  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.671   -23.587 0.738   1.00 28.01  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.760   -24.559 1.082   1.00 30.23  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.377   -24.717 1.497   1.00 29.71  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 3.953   -25.920 1.350   1.00 30.54  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.567   -26.071 1.729   1.00 33.41  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.842   -26.653 1.708   1.00 32.04  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.781   -19.583 2.558   1.00 21.54  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.792   -18.524 2.416   1.00 20.17  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.306   -18.506 0.978   1.00 20.56  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.603   -19.570 0.399   1.00 22.34  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.884   -18.971 3.459   1.00 21.53  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.675   -20.495 3.628   1.00 22.84  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.144   -20.629 3.514   1.00 20.59  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.376   -17.304 0.391   1.00 18.34  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.687   -17.198 -1.021  1.00 18.42  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.249   -15.806 -1.326  1.00 19.10  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.301   -14.925 -0.455  1.00 20.85  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.436   -17.517 -1.854  1.00 20.68  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.760   -15.654 -2.550  1.00 21.13  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.182   -14.336 -2.981  1.00 20.49  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.639   -14.078 -4.373  1.00 19.89  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.352   -15.035 -5.118  1.00 21.51  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.693   -14.174 -2.891  1.00 19.74  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.415   -15.072 -3.884  1.00 19.99  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 10.950  -14.851 -3.858  1.00 20.26  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.619  -15.714 -4.859  1.00 20.67  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.893  -16.133 -4.751  1.00 23.16  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.577  -15.963 -3.624  1.00 20.03  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.431  -16.817 -5.746  1.00 26.97  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.541   -12.788 -4.704  1.00 19.98  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.299   -12.377 -6.091  1.00 21.16  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.617   -12.504 -6.843  1.00 21.93  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.589   -11.852 -6.462  1.00 23.43  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.800   -10.925 -6.200  1.00 24.24  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.617   -10.623 -5.264  1.00 30.35  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.478   -10.597 -7.675  1.00 21.50  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.274   -11.093 -5.747  1.00 31.53  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.661   -13.348 -7.879  1.00 21.87  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.905   -13.522 -8.622  1.00 25.61  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.031   -12.491 -9.743  1.00 28.88  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.046   -11.896 -10.182 1.00 25.87  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.029   -14.904 -9.255  1.00 26.50  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 9.968   -15.876 -8.556  1.00 27.14  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.570  -15.499 -7.543  1.00 29.06  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.072  -17.012 -9.010  1.00 29.35  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.286  -12.302 -10.194 1.00 29.47  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.576  -11.648 -11.454 1.00 34.58  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.290  -12.648 -12.584 1.00 29.50  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.181  -13.853 -12.366 1.00 30.08  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.049  -11.273 -11.526 1.00 38.40  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.457  -10.006 -10.784 1.00 44.95  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.087  -8.907  -11.259 1.00 45.89  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.154  -10.135 -9.752  1.00 50.69  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.079  -12.134 -13.783 1.00 35.93  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.039  -12.991 -14.959 1.00 33.94  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.373  -12.745 -15.654 1.00 35.22  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.667  -11.590 -15.958 1.00 33.01  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 8.889   -12.517 -15.858 1.00 38.92  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.540   -12.533 -15.111 1.00 37.66  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 8.847   -13.341 -17.151 1.00 34.16  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.591   -11.426 -15.534 1.00 40.10  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.174  -13.796 -15.838 1.00 33.57  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.466  -13.651 -16.513 1.00 35.47  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.226  -13.422 -18.007 1.00 33.90  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.215  -13.857 -18.572 1.00 31.39  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.329  -14.885 -16.297 1.00 34.27  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.156  -12.700 -18.633 1.00 33.62  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.152  -12.576 -20.074 1.00 30.84  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.014  -13.977 -20.633 1.00 25.49  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.724  -14.861 -20.205 1.00 27.08  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.488  -12.011 -20.533 1.00 33.34  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 15.667  -10.515 -20.317 1.00 37.00  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 14.660  -9.813  -20.235 1.00 40.51  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 16.823  -10.061 -20.280 1.00 40.01  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.090  -14.165 -21.570 1.00 28.71  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 12.991  -15.415 -22.300 1.00 29.25  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.004  -16.369 -21.638 1.00 36.63  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.632  -17.377 -22.235 1.00 32.81  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.589  -16.044 -20.404 1.00 31.74  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.724  -16.943 -19.640 1.00 36.25  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.242   -16.713 -19.954 1.00 29.37  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 8.816   -15.640 -20.390 1.00 33.31  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 10.995  -16.773 -18.140 1.00 39.78  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.435   -17.747 -19.681 1.00 35.94  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 6.987   -17.705 -19.844 1.00 34.14  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.393   -16.653 -18.919 1.00 32.75  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.640   -16.687 -17.719 1.00 35.24  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.449   -19.113 -19.514 1.00 39.08  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 4.923   -19.152 -19.525 1.00 38.57  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.031   -20.154 -20.476 1.00 40.97  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.657   -15.704 -19.503 1.00 31.69  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 4.972   -14.641 -18.787 1.00 32.53  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.654   -15.173 -18.214 1.00 38.03  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.080   -16.123 -18.751 1.00 34.82  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.630   -13.453 -19.693 1.00 34.42  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 5.852   -12.704 -20.258 1.00 31.33  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.532   -11.488 -21.127 1.00 42.16  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.084   -11.921 -22.493 1.00 40.47  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.026   -10.785 -23.407 1.00 38.30  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.123   -14.550 -17.135 1.00 38.06  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 1.848   -14.969 -16.538 1.00 36.34  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.706   -14.447 -17.402 1.00 35.98  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 0.893   -13.489 -18.152 1.00 34.56  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.819   -14.273 -15.146 1.00 36.77  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 3.086   -13.438 -15.070 1.00 41.44  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.667   -13.348 -16.486 1.00 37.01  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.542  -14.947 -17.224 1.00 38.55  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.717  -14.325 -17.852 1.00 39.22  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.867  -12.893 -17.364 1.00 42.70  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.249  -12.522 -16.362 1.00 34.56  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.904  -15.202 -17.404 1.00 37.96  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.275  -16.510 -16.966 1.00 32.50  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.890  -16.144 -16.441 1.00 36.13  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.652  -12.033 -18.059 1.00 39.40  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.907  -10.673 -17.574 1.00 44.20  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.556  -10.668 -16.189 1.00 37.42  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.324  -11.562 -15.849 1.00 41.92  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.831  -10.040 -18.651 1.00 41.88  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.382  -11.229 -19.412 1.00 37.63  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.318  -12.312 -19.348 1.00 44.95  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.213  -9.650  -15.401 1.00 38.52  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.682  -9.466  -14.036 1.00 41.51  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.192  -10.569 -13.092 1.00 38.42  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.645  -10.582 -11.949 1.00 38.63  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.193  -9.265  -13.968 1.00 48.06  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.606  -8.050  -14.763 1.00 48.12  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.334  -6.912  -14.357 1.00 48.72  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.214  -8.274  -15.915 1.00 50.68  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.304  -11.485 -13.548 1.00 32.81  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.763  -12.539 -12.668 1.00 27.99  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.269  -12.293 -12.401 1.00 25.59  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.410   -11.629 -13.190 1.00 30.42  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.926  -14.012 -13.094 1.00 28.90  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.336  -14.552 -13.379 1.00 38.93  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.338  -14.068 -12.332 1.00 40.71  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.809  -14.335 -12.613 1.00 45.03  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -6.056  -15.780 -12.589 1.00 41.49  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.219   -12.773 -11.255 1.00 20.73  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.620   -12.579 -10.878 1.00 22.32  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.270   -13.936 -10.786 1.00 22.30  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.616   -14.913 -10.405 1.00 22.07  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.799   -11.982 -9.471  1.00 22.40  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.269   -10.559 -9.432  1.00 25.36  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.100  -10.300 -9.351  1.00 30.51  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.133   -9.480  -9.576  1.00 27.34  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.579  -8.999  -9.412  1.00 33.27  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.676   -8.174  -9.579  1.00 28.01  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.316   -7.948  -9.488  1.00 33.22  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.112  -6.671  -9.557  1.00 34.15  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.593   -14.052 -11.053 1.00 22.69  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.256   -15.339 -10.877 1.00 21.11  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.603   -15.519 -9.406  1.00 21.22  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.257   -14.651 -8.827  1.00 24.31  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.524   -15.217 -11.731 1.00 23.70  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.743   -13.746 -11.944 1.00 23.15  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.468   -12.970 -11.559 1.00 24.92  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.062   -16.569 -8.795  1.00 22.79  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.199   -16.731 -7.353  1.00 20.64  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.157   -17.898 -7.121  1.00 24.30  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.929   -19.028 -7.596  1.00 24.23  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.855   -16.943 -6.622  1.00 22.10  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.824   -15.828 -6.923  1.00 19.72  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.109   -17.090 -5.103  1.00 19.10  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.329   -14.419 -6.582  1.00 20.23  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.230   -17.620 -6.362  1.00 20.19  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.161   -18.671 -5.997  1.00 20.91  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.903   -19.099 -4.554  1.00 20.80  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 6.927   -18.273 -3.644  1.00 22.87  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.606   -18.183 -6.186  1.00 21.24  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.631   -19.229 -5.749  1.00 23.35  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.012  -20.256 -6.619  1.00 24.16  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.200  -19.192 -4.471  1.00 24.52  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 10.949  -21.207 -6.237  1.00 27.53  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.134  -20.165 -4.087  1.00 29.92  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.526  -21.153 -4.982  1.00 27.75  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.570   -20.387 -4.386  1.00 21.77  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.139   -20.919 -3.093  1.00 20.68  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.387   -21.458 -2.421  1.00 23.51  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.103   -22.303 -3.006  1.00 24.55  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.145   -22.085 -3.292  1.00 22.68  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.771   -21.583 -3.722  1.00 23.98  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.477   -21.356 -5.067  1.00 27.71  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.791   -21.301 -2.763  1.00 27.79  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.228   -20.854 -5.448  1.00 29.09  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.550   -20.798 -3.144  1.00 24.80  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.279   -20.578 -4.479  1.00 29.98  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.677   -20.916 -1.232  1.00 21.38  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 8.851   -21.367 -0.503  1.00 24.71  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.618   -22.807 -0.033  1.00 22.28  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.478   -23.264 0.131   1.00 23.08  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.128   -20.458 0.715   1.00 23.52  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.589   -19.055 0.331   1.00 23.06  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.814  -18.831 -0.302  1.00 21.71  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.816   -17.941 0.649   1.00 20.91  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.225  -17.526 -0.618  1.00 21.18  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.214   -16.654 0.275   1.00 20.33  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.437  -16.435 -0.336  1.00 20.81  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.714   -23.521 0.162   1.00 24.56  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.647   -24.893 0.641   1.00 26.83  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.429   -25.880 -0.509  1.00 35.03  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.306  -26.694 -0.779  1.00 31.38  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.293   -25.786 -1.220  1.00 31.90  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.040   -26.669 -2.356  1.00 32.19  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 8.831   -26.222 -3.577  1.00 31.27  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.137   -27.021 -4.483  1.00 29.13  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.545   -26.722 -2.678  1.00 31.42  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.162   -25.400 -3.033  1.00 33.67  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.692   -27.191 -1.527  1.00 31.65  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.076   -24.904 -3.640  1.00 25.47  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.764   -24.265 -4.746  1.00 26.67  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 8.973   -24.370 -6.042  1.00 27.86  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.576   -24.358 -7.106  1.00 31.31  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.213  -24.782 -4.886  1.00 28.05  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 11.953  -24.800 -3.598  1.00 32.53  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.792  -25.830 -3.242  1.00 34.55  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 11.988  -23.915 -2.569  1.00 31.17  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.317  -25.578 -2.047  1.00 42.84  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 12.853  -24.416 -1.618  1.00 34.16  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.635   -24.472 -5.967  1.00 29.47  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.784   -24.481 -7.154  1.00 32.11  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.308   -23.063 -7.474  1.00 31.36  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.383   -22.175 -6.613  1.00 28.78  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.588   -25.392 -6.893  1.00 38.00  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.023   -26.822 -6.591  1.00 46.81  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 4.915   -27.687 -6.022  1.00 52.92  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.767   -27.217 -5.853  1.00 50.25  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.243   -28.849 -5.709  1.00 59.76  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 5.953   -22.839 -8.750  1.00 25.78  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.413   -21.571 -9.211  1.00 26.87  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 3.958   -21.776 -9.610  1.00 29.82  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.615   -22.787 -10.229 1.00 31.63  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.199   -21.018 -10.405 1.00 30.90  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.515   -20.750 -9.927  1.00 28.31  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.560   -19.764 -10.994 1.00 32.05  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.104   -20.823 -9.237  1.00 26.09  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.784   -20.725 -9.836  1.00 26.39  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.475   -19.266 -10.152 1.00 28.59  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.146   -18.357 -9.661  1.00 27.24  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.737   -21.341 -8.934  1.00 29.09  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.426   -19.053 -10.963 1.00 23.76  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.057   -17.699 -11.330 1.00 26.30  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.165  -17.311 -10.524 1.00 27.39  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.170  -18.023 -10.586 1.00 30.89  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.269  -17.746 -12.825 1.00 28.29  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 0.971   -18.008 -13.662 1.00 29.00  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.091   -17.210 -13.514 1.00 29.66  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.973   -18.997 -14.646 1.00 35.83  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.228   -17.442 -14.287 1.00 45.43  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.104   -19.214 -15.424 1.00 35.33  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.226   -18.445 -15.243 1.00 38.16  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.078  -16.188 -9.789  1.00 23.55  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.190  -15.831 -8.923  1.00 24.15  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.486  -14.337 -9.014  1.00 23.87  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.605  -13.518 -9.302  1.00 24.85  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.871  -16.213 -7.472  1.00 25.47  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.832  -17.698 -7.120  1.00 25.50  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.464  -17.712 -5.655  1.00 25.37  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.208  -18.327 -7.326  1.00 31.41  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.758  -13.985 -8.727  1.00 23.36  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -4.157  -12.582 -8.690  1.00 22.84  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.170  -12.109 -7.230  1.00 21.35  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.079  -12.933 -6.312  1.00 21.90  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.186  -10.779 -7.004  1.00 21.38  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.132  -10.201 -5.652  1.00 22.78  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.130  -10.734 -4.617  1.00 21.81  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.847  -10.732 -3.427  1.00 20.61  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.394  -8.742  -5.955  1.00 24.51  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.756  -8.564  -7.284  1.00 24.16  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.229  -9.771  -8.082  1.00 22.13  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.298  -11.226 -5.076  1.00 22.32  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.282  -11.728 -4.116  1.00 24.07  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.705  -12.870 -3.277  1.00 21.94  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.187  -13.151 -2.173  1.00 21.15  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.551  -12.273 -4.808  1.00 25.16  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.357  -13.571 -5.579  1.00 28.47  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.596  -13.915 -6.415  1.00 38.24  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.506  -15.288 -7.011  1.00 41.26  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.497  -16.357 -6.003  1.00 42.64  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.687  -13.563 -3.818  1.00 23.26  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.106  -14.704 -3.157  1.00 21.54  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.748  -14.360 -2.507  1.00 21.41  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -3.061  -15.282 -2.058  1.00 22.41  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -5.021  -15.891 -4.120  1.00 23.37  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.407  -16.444 -4.419  1.00 28.06  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.218  -16.422 -3.464  1.00 28.46  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.656  -16.846 -5.580  1.00 27.01  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.398  -13.062 -2.419  1.00 20.31  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -2.050  -12.666 -1.967  1.00 19.55  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.160  -11.831 -0.690  1.00 19.02  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.742  -10.756 -0.712  1.00 21.59  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.320  -11.870 -3.062  1.00 17.64  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.212  -12.603 -4.397  1.00 18.51  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.444  -11.806 -5.409  1.00 21.43  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.490  -13.935 -4.237  1.00 18.06  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.605  -12.344 0.422   1.00 21.16  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.699  -11.663 1.717   1.00 21.36  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.313  -11.169 2.105   1.00 21.67  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.576   -11.980 2.327   1.00 24.05  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.144  -12.702 2.746   1.00 20.55  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.586  -13.123 2.472   1.00 22.33  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.881  -14.038 1.450   1.00 21.31  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.622  -12.606 3.244   1.00 24.21  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.203  -14.404 1.183   1.00 27.63  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.944  -12.975 2.972   1.00 22.88  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.223  -13.911 1.989   1.00 22.16  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.073  -9.845  2.203   1.00 23.40  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.265   -9.364  2.596   1.00 23.50  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.762   -10.024 3.878   1.00 22.40  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.058   -10.160 4.865   1.00 24.47  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.071   -7.839  2.674   1.00 23.23  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.001   -7.597  1.559   1.00 25.63  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.984  -8.747  1.843   1.00 23.12  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.041   -10.417 3.843   1.00 24.56  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.645   -11.297 4.829   1.00 23.44  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.729   -10.604 6.197   1.00 22.98  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.316   -11.208 7.177   1.00 26.88  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.071   -11.605 4.335   1.00 25.05  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.840   -12.405 5.379   1.00 23.85  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.545   -13.739 5.638   1.00 24.16  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.862   -11.803 6.104   1.00 26.46  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.245   -14.479 6.586   1.00 26.46  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.594   -12.541 7.023   1.00 28.25  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.268   -13.853 7.284   1.00 27.80  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 7.977   -14.540 8.238   1.00 31.51  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.146   -9.329  6.226   1.00 23.28  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.270   -8.594  7.493   1.00 28.49  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.941   -8.594  8.263   1.00 32.40  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.873   -9.084  9.397   1.00 37.77  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 4.874   -7.215  7.268   1.00 27.46  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 1.876   -8.105  7.608   1.00 31.38  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.544   -8.042  8.207   1.00 31.05  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? 0.032   -9.429  8.605   1.00 29.82  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.711  -9.553  9.592   1.00 30.49  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.409  -7.386  7.192   1.00 33.71  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.885  -7.241  7.646   1.00 37.62  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.725  -6.442  6.664   1.00 35.02  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.829  -5.693  7.348   1.00 42.03  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.837  -6.593  7.890   1.00 45.12  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.408   -10.486 7.866   1.00 25.81  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.281  -11.770 7.960   1.00 27.29  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.475   -12.829 8.756   1.00 27.27  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? -0.073  -13.911 8.934   1.00 26.88  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.575  -12.364 6.591   1.00 31.32  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.528  -11.545 5.946   1.00 39.83  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.733   -12.580 9.136   1.00 27.72  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.554   -13.695 9.622   1.00 31.44  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.097   -14.225 10.988  1.00 30.47  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.203   -15.434 11.261  1.00 33.16  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 4.047   -13.357 9.628   1.00 33.30  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.459   -12.179 10.472  1.00 41.02  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 5.980   -12.265 10.524  1.00 51.08  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.619   -11.115 11.244  1.00 57.82  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.629   -9.917  10.395  1.00 68.81  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.557   -13.340 11.834  0.50 32.92  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.567   -13.331 11.835  0.50 33.00  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.065   -13.784 13.135  0.50 34.62  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.025   -13.761 13.119  0.50 34.98  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? -0.060  -14.811 12.956  0.50 35.32  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? -0.005  -14.866 12.894  0.50 35.77  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.162  -15.772 13.716  0.50 37.06  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? 0.005   -15.900 13.563  0.50 37.42  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.783   -12.611 14.070  0.50 36.79  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.368   -12.619 13.884  0.50 36.64  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 1.999   -11.815 14.532  0.50 38.42  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? -0.019  -12.950 15.319  0.50 38.87  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.139   -12.271 14.293  0.50 38.36  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.881   -12.918 16.190  0.50 39.79  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.805   -10.719 15.098  0.50 39.92  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.206  -13.268 15.553  0.50 43.26  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.884  -14.659 11.909  1.00 34.34  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -1.980  -15.586 11.689  1.00 33.88  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.542  -16.849 10.958  1.00 34.32  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -2.014  -17.957 11.252  1.00 30.38  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -3.055  -14.844 10.897  1.00 32.76  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.278  -15.663 10.690  1.00 36.78  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.339  -14.745 10.074  1.00 40.54  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.675  -15.419 9.976   1.00 48.16  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.596  -14.549 9.230   1.00 45.67  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.665  -16.683 9.964   1.00 31.70  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.443  -17.762 9.013   1.00 31.86  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 0.938   -18.398 9.182   1.00 31.14  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.152   -19.487 8.660   1.00 32.34  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.632  -17.321 7.549   1.00 27.85  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -2.034  -16.878 7.160   1.00 29.09  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -3.168  -17.625 7.508   1.00 30.45  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.219  -15.707 6.414   1.00 27.27  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.448  -17.225 7.123   1.00 30.26  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.490  -15.303 6.021   1.00 31.25  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.603  -16.047 6.393   1.00 30.35  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.834  -15.607 5.993   1.00 31.11  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.857   -17.748 9.901   1.00 30.11  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.224   -18.260 9.959   1.00 30.82  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.421   -19.239 11.129  1.00 29.59  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.140   -18.953 12.059  1.00 36.16  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.731   -20.370 11.096  1.00 33.32  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.859   -21.364 12.152  1.00 34.67  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.125   -22.697 11.464  1.00 35.48  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.692   -22.891 10.329  1.00 32.27  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.552   -21.404 12.961  1.00 36.38  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.381   -20.231 13.926  1.00 39.91  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? 0.004   -20.177 14.582  1.00 48.87  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.829   -23.667 12.095  1.00 34.48  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 4.080   -24.956 11.441  1.00 32.75  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.839   -25.673 10.948  1.00 35.86  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.768   -25.547 11.522  1.00 38.59  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 4.831   -25.765 12.529  1.00 37.92  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.478   -24.675 13.362  1.00 40.48  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.405   -23.579 13.446  1.00 36.37  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 2.997   -26.409 9.852   1.00 37.88  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 1.890   -27.103 9.231   1.00 41.40  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.428   -28.461 8.819   1.00 46.20  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.613   -28.588 8.534   1.00 44.78  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.389   -26.285 8.046   1.00 44.88  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? 0.051   -26.739 7.527   1.00 50.77  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? -0.014  -27.647 6.694   1.00 49.38  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -1.018  -26.088 7.965   1.00 54.34  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.547   -29.461 8.764   1.00 49.79  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 1.962   -30.823 8.481   1.00 49.13  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.375   -30.960 7.017   1.00 49.08  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.054   -31.922 6.662   1.00 46.99  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 0.852   -31.807 8.890   1.00 52.87  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.309  -31.974 7.895   1.00 53.37  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 1.973   -30.004 6.165   1.00 43.05  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 2.064   -30.209 4.725   1.00 43.56  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.516   -30.224 4.241   1.00 39.33  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.366   -29.501 4.766   1.00 39.75  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 1.145   -29.260 3.946   1.00 45.95  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.317  -29.526 4.265   1.00 49.57  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -0.916  -30.621 3.405   1.00 44.13  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.888  -30.012 2.491   1.00 64.47  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -3.022  -29.397 2.867   1.00 63.28  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.828  -28.913 1.938   1.00 58.90  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.364  -29.283 4.149   1.00 62.09  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.770   -31.056 3.217   1.00 34.93  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 5.102   -31.262 2.679   1.00 35.71  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.673   -29.905 2.278   1.00 34.10  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 5.118   -29.228 1.418   1.00 30.25  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 5.066   -32.138 1.424   1.00 38.10  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.403   -32.470 0.809   1.00 41.78  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.403   -33.675 -0.132  1.00 48.51  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 7.781   -33.974 -0.671  1.00 48.72  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.788   -29.526 2.901   1.00 32.60  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.535   -28.406 2.369   1.00 31.07  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.203   -27.121 3.125   1.00 29.45  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 7.925   -26.142 2.988   1.00 28.57  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.139   -27.145 3.930   1.00 27.30  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.634   -25.937 4.565   1.00 30.44  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.627   -25.333 5.565   1.00 31.30  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 6.837   -24.105 5.621   1.00 28.70  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.253   -26.197 5.174   1.00 28.68  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.501   -24.925 5.535   1.00 29.20  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 3.747   -24.267 6.742   1.00 28.15  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.533   -24.402 4.673   1.00 29.86  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.107   -23.073 7.057   1.00 29.68  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 1.861   -23.228 5.006   1.00 23.49  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.140   -22.575 6.202   1.00 26.72  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.167   -26.173 6.444   1.00 28.90  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 8.032   -25.662 7.494   1.00 30.21  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.373   -25.203 6.909   1.00 27.81  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 9.977   -24.236 7.398   1.00 28.75  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.220   -26.725 8.573   1.00 31.45  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 6.897   -26.982 9.261   1.00 38.59  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 5.995   -26.131 9.204   1.00 31.36  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.778   -28.120 9.940   1.00 32.06  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 9.843   -25.926 5.886   1.00 27.03  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 11.000  -25.465 5.137   1.00 27.71  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.664  -24.100 4.539   1.00 25.25  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.466  -23.170 4.609   1.00 25.07  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.442  -26.394 4.003   1.00 29.46  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.711  -25.931 3.278   1.00 29.15  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.316  -26.929 2.288   1.00 39.05  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.694  -27.973 2.065   1.00 44.00  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.413  -26.701 1.737   1.00 42.50  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.445   -23.963 4.004   1.00 25.59  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 9.015   -22.666 3.473   1.00 24.02  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 9.023   -21.533 4.512   1.00 23.56  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.388   -20.382 4.195   1.00 23.47  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.590   -21.834 5.743   1.00 22.33  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.616   -20.832 6.799   1.00 22.84  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 10.045  -20.360 7.082   1.00 25.71  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.266  -19.167 7.307   1.00 22.78  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 7.967   -21.307 8.103   1.00 25.09  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.461   -21.573 8.020   1.00 26.32  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.054   -22.262 9.328   1.00 26.88  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.590   -20.352 7.774   1.00 24.88  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 11.013  -21.302 7.071   1.00 25.78  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.407  -20.935 7.307   1.00 25.11  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 12.871  -19.999 6.195   1.00 25.00  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.525  -18.993 6.439   1.00 24.99  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.322  -22.179 7.454   1.00 24.38  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 14.771  -21.828 7.708   1.00 25.01  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.396  -21.688 8.919   1.00 26.90  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 15.748  -21.485 6.702   1.00 25.09  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.706  -21.331 8.722   1.00 25.46  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 16.934  -21.161 7.378   1.00 26.46  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.708  -21.408 5.298   1.00 24.56  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.093  -20.779 6.698   1.00 25.53  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 16.834  -20.996 4.616   1.00 26.81  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 18.013  -20.688 5.323   1.00 27.45  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.481  -20.300 4.957   1.00 22.82  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 13.047  -19.569 3.831   1.00 21.77  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.543  -18.123 3.831   1.00 24.96  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.304  -17.188 3.602   1.00 20.43  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.661  -20.267 2.532   1.00 19.94  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.396  -21.593 2.327   1.00 21.96  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 12.987  -22.333 1.055   1.00 27.70  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 12.052  -21.874 0.370   1.00 26.64  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.563  -23.404 0.729   1.00 28.22  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.247  -17.949 4.095   1.00 21.38  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.643  -16.635 3.975   1.00 21.30  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.211  -15.716 5.064   1.00 22.09  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.331  -14.495 4.882   1.00 21.60  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.102   -16.695 4.011   1.00 21.43  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.525   -15.302 3.572   1.00 21.52  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.556   -17.141 5.380   1.00 20.45  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.096   -15.327 3.021   1.00 20.25  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.548  -16.316 6.214   1.00 21.71  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 12.027  -15.534 7.350   1.00 22.75  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.532  -15.298 7.249   1.00 24.96  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 13.973  -14.236 7.677   1.00 29.01  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.630  -16.232 8.663   1.00 23.85  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.257  -15.699 9.949   1.00 36.22  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.534  -16.220 11.189  1.00 44.93  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.221  -17.417 11.320  1.00 40.22  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.216  -15.310 12.100  1.00 42.95  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.295  -16.275 6.710   1.00 23.23  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 15.754  -16.303 6.796   1.00 23.55  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.481  -15.957 5.492   1.00 25.50  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.560  -15.353 5.578   1.00 25.20  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.293  -17.571 7.458   1.00 23.95  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 15.782  -17.641 8.882   1.00 29.78  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 16.120  -16.776 9.701   1.00 32.09  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 14.855  -18.538 9.161   1.00 25.65  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 15.948  -16.338 4.306   1.00 21.49  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.589  -15.929 3.050   1.00 21.67  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.553  -15.819 1.905   1.00 21.51  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.547  -16.590 0.922   1.00 22.12  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 17.775  -16.837 2.689   1.00 23.96  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 18.841  -16.195 1.823   1.00 26.55  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.608  -15.180 1.150   1.00 24.29  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 20.041  -16.774 1.807   1.00 26.79  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.608  -14.864 2.007   1.00 20.47  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.468  -14.842 1.104   1.00 22.16  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 13.831  -14.413 -0.316  1.00 24.74  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 13.028  -14.635 -1.201  1.00 22.66  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.502  -13.870 1.799   1.00 20.06  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.456  -12.897 2.523   1.00 18.82  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.513  -13.846 3.078   1.00 18.96  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 15.034  -13.847 -0.514  1.00 21.39  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.416  -13.281 -1.811  1.00 21.53  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.501  -14.113 -2.502  1.00 22.08  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 17.023  -13.697 -3.551  1.00 24.26  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 15.791  -11.799 -1.638  1.00 20.50  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.695  -10.972 -1.074  1.00 20.36  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.416  -10.892 -1.616  1.00 22.40  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.698  -10.219 0.001   1.00 19.38  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.690  -10.048 -0.893  1.00 22.00  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.442  -9.639  0.114   1.00 23.08  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 16.806  -15.309 -1.962  1.00 23.49  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 17.881  -16.143 -2.498  1.00 22.14  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.418  -16.861 -3.761  1.00 26.62  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.234  -16.977 -4.033  1.00 24.50  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.374  -17.165 -1.473  1.00 22.24  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.391  -17.409 -4.495  1.00 24.70  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 18.100  -18.253 -5.635  1.00 27.56  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 17.767  -19.637 -5.097  1.00 30.94  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.546  -20.200 -4.326  1.00 34.48  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.328  -18.287 -6.513  1.00 31.41  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 19.161  -19.306 -7.474  1.00 37.43  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.596  -20.165 -5.446  1.00 27.36  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.273  -21.503 -4.992  1.00 27.87  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.182  -22.444 -6.196  1.00 34.93  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 15.612  -23.527 -6.077  1.00 44.12  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 14.962  -21.574 -4.195  1.00 27.42  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 15.090  -20.965 -2.812  1.00 26.49  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.557  -21.717 -1.726  1.00 26.24  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 14.791  -19.611 -2.613  1.00 26.11  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.747  -21.122 -0.484  1.00 28.87  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 14.923  -19.034 -1.365  1.00 25.57  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.394  -19.790 -0.300  1.00 27.12  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.591  -19.236 0.939   1.00 26.92  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.740  -22.014 -7.327  1.00 44.13  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.870  -22.834 -8.526  1.00 65.46  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 17.734  -24.062 -8.195  1.00 75.01  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 18.958  -23.863 -8.005  1.00 73.91  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.480  -22.043 -9.670  1.00 62.67  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 16.889  -20.755 -9.788  1.00 69.13  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 17.152  -25.168 -8.103  1.00 86.38  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.794  -11.013 -41.876 1.00 66.80  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.491  -12.021 -42.925 1.00 68.99  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 36.977  -12.229 -42.962 1.00 66.85  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.376  -12.508 -41.923 1.00 63.60  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.218  -13.342 -42.638 1.00 79.21  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.406  -14.242 -43.854 1.00 91.83  ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.521  -13.614 -45.131 1.00 96.71  ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 42.096  -13.436 -44.280 1.00 103.41 ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.307  -12.071 -44.134 1.00 57.09  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.851  -12.215 -44.198 1.00 55.10  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.486  -13.664 -43.873 1.00 55.26  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.284  -14.568 -44.105 1.00 48.44  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.468  -11.765 -45.620 1.00 53.24  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.728  -11.090 -46.154 1.00 52.77  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.901  -11.757 -45.446 1.00 51.87  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.306  -13.856 -43.265 1.00 54.54  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.849  -15.166 -42.815 1.00 55.24  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.461  -15.473 -43.385 1.00 52.57  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.825  -14.598 -43.993 1.00 48.18  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 32.931  -15.254 -41.289 1.00 57.65  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.321  -15.408 -40.763 1.00 69.04  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.221  -16.322 -41.277 1.00 71.16  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 34.948  -14.793 -39.738 1.00 63.87  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.353  -16.250 -40.584 1.00 68.82  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.209  -15.323 -39.650 1.00 68.56  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 30.999  -16.726 -43.210 1.00 41.51  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.688  -17.111 -43.704 1.00 42.43  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.680  -16.074 -43.232 1.00 43.42  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 27.898  -15.558 -44.032 1.00 44.29  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.295  -18.471 -43.176 1.00 41.24  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.732  -15.795 -41.924 1.00 38.30  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 27.958  -14.724 -41.307 1.00 45.43  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.857  -13.520 -40.997 1.00 40.90  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 29.985  -13.674 -40.524 1.00 41.61  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.258  -15.178 -40.019 1.00 43.27  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.162  -16.228 -40.167 1.00 39.11  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 24.836  -15.861 -40.408 1.00 33.89  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.445  -17.581 -39.994 1.00 38.56  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 23.835  -16.816 -40.529 1.00 34.82  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.435  -18.536 -40.084 1.00 32.14  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.129  -18.157 -40.327 1.00 33.68  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.321  -12.317 -41.220 1.00 46.03  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 29.049  -11.082 -40.951 1.00 46.46  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.233  -10.163 -40.036 1.00 44.50  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 26.999  -10.210 -40.029 1.00 35.86  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 29.241  -10.386 -42.296 1.00 46.15  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 27.938  -10.064 -42.998 1.00 40.19  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 28.151  -9.703  -44.465 1.00 51.47  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 26.944  -9.103  -45.127 1.00 54.54  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 25.856  -10.058 -45.407 1.00 57.27  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.884  -9.214  -39.319 1.00 45.69  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.170  -8.326  -38.397 1.00 36.94  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.035  -7.601  -39.100 1.00 38.27  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.189  -7.175  -40.245 1.00 42.64  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.321  -7.406  -37.998 1.00 44.70  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.524  -8.336  -38.008 1.00 46.41  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.327  -8.914  -39.389 1.00 46.23  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 25.865  -7.531  -38.438 1.00 31.54  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.679  -6.928  -39.017 1.00 31.50  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.736  -7.947  -39.654 1.00 30.86  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.603  -7.618  -39.989 1.00 31.03  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.212  -9.181  -39.891 1.00 33.91  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.326  -10.198 -40.437 1.00 29.08  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.228  -10.516 -39.413 1.00 24.70  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.489  -10.547 -38.218 1.00 28.65  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 24.108  -11.468 -40.728 1.00 31.85  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.845  -11.511 -42.067 1.00 41.76  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.539  -10.668 -42.948 1.00 41.33  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.699  -12.413 -42.224 1.00 36.71  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 20.994  -10.663 -39.883 1.00 25.90  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.891  -10.914 -38.977 1.00 26.68  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.547  -12.396 -39.029 1.00 26.77  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.574  -12.974 -40.118 1.00 30.30  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.726  -10.087 -39.492 1.00 25.89  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 19.055  -8.591  -39.613 1.00 26.43  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.776  -7.915  -40.020 1.00 28.78  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.661  -8.090  -38.289 1.00 25.15  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.177  -12.971 -37.874 1.00 24.73  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 18.944  -14.410 -37.801 1.00 23.27  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.839  -14.667 -36.786 1.00 26.66  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.418  -13.757 -36.065 1.00 23.84  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.233  -15.141 -37.360 1.00 25.12  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.376  -14.940 -38.363 1.00 26.36  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.683  -14.800 -35.918 1.00 24.50  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.369  -15.920 -36.753 1.00 24.35  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 16.866  -16.438 -35.496 1.00 25.58  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 17.977  -17.300 -34.921 1.00 27.26  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.565  -18.081 -35.685 1.00 27.68  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.600  -17.264 -35.720 1.00 24.44  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.399  -16.435 -36.141 1.00 27.80  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.175  -16.147 -37.488 1.00 30.92  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.499  -15.947 -35.202 1.00 28.60  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.072  -15.407 -37.887 1.00 31.87  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.380  -15.206 -35.599 1.00 27.55  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.174  -14.936 -36.949 1.00 32.30  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.189  -17.181 -33.589 1.00 23.41  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.244  -17.908 -32.896 1.00 25.60  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.639  -18.847 -31.853 1.00 25.23  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.689  -18.474 -31.155 1.00 26.26  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.222  -16.948 -32.253 1.00 26.16  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.157  -20.078 -31.794 1.00 24.72  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.493  -21.127 -31.026 1.00 26.79  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.324  -21.454 -29.791 1.00 27.81  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.512  -21.747 -29.910 1.00 30.96  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.287  -22.419 -31.841 1.00 27.86  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.559  -23.559 -31.073 1.00 26.22  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 16.120  -23.134 -30.764 1.00 30.58  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.200  -24.211 -30.189 1.00 32.27  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.659  -24.499 -28.825 1.00 28.24  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.699  -21.336 -28.604 1.00 29.82  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.326  -21.753 -27.350 1.00 34.58  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.448  -22.839 -26.722 1.00 31.71  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.226  -22.766 -26.831 1.00 29.33  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.384  -20.600 -26.344 1.00 34.32  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.020  -19.334 -26.874 1.00 45.70  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 21.782  -19.181 -26.526 1.00 51.84  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 21.816  -19.022 -24.737 1.00 47.41  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 19.073  -23.824 -26.062 1.00 30.48  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.318  -24.806 -25.282 1.00 31.75  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.379  -24.088 -24.299 1.00 30.66  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.774  -23.131 -23.637 1.00 35.78  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.333  -25.750 -24.614 1.00 43.77  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 18.785  -27.061 -24.025 1.00 47.76  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 19.702  -27.750 -23.014 1.00 44.82  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 16.112  -24.516 -24.250 1.00 34.79  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.125  -23.943 -23.347 1.00 35.09  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.294  -22.806 -23.948 1.00 36.01  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.329  -22.342 -23.324 1.00 36.27  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.649  -22.342 -25.157 1.00 32.05  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 13.951  -21.183 -25.694 1.00 29.19  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.572  -21.433 -27.149 1.00 30.02  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.249  -22.164 -27.859 1.00 33.61  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 14.881  -19.965 -25.670 1.00 26.47  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.348  -19.651 -24.257 1.00 30.38  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.610  -18.805 -23.419 1.00 31.22  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.485  -20.268 -23.744 1.00 35.04  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 15.037  -18.549 -22.118 1.00 34.25  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 16.922  -20.012 -22.451 1.00 40.56  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 16.192  -19.155 -21.642 1.00 38.32  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 16.680  -18.948 -20.389 1.00 42.28  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.541  -20.740 -27.669 1.00 26.52  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.237  -20.809 -29.099 1.00 24.64  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.310  -20.074 -29.903 1.00 28.44  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 13.984  -19.201 -29.361 1.00 24.90  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 10.889  -20.113 -29.182 1.00 24.48  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 10.940  -19.071 -28.041 1.00 26.52  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.702  -19.785 -26.924 1.00 25.96  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.494  -20.484 -31.169 1.00 24.98  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.344  -19.730 -32.106 1.00 27.03  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.062  -18.236 -31.965 1.00 23.64  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 12.912  -17.810 -32.075 1.00 23.99  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 14.037  -20.190 -33.540 1.00 25.42  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.284  -21.656 -33.741 1.00 25.72  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.333  -22.613 -33.440 1.00 26.83  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.357  -22.330 -34.201 1.00 27.87  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.817  -23.818 -33.721 1.00 28.58  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 15.042  -23.676 -34.191 1.00 28.20  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.105  -17.435 -31.733 1.00 23.53  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 14.860  -16.099 -31.182 1.00 22.29  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.395  -15.020 -32.134 1.00 24.15  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.553  -15.135 -32.529 1.00 24.66  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.561  -15.993 -29.820 1.00 22.44  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.046  -14.845 -28.976 1.00 24.86  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.325  -13.511 -29.117 1.00 26.18  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.111  -14.937 -27.869 1.00 27.03  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.597  -12.765 -28.208 1.00 26.06  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 13.864  -13.618 -27.413 1.00 25.49  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.477  -16.009 -27.221 1.00 25.58  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.016  -13.341 -26.334 1.00 24.64  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.654  -15.742 -26.146 1.00 26.59  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.402  -14.426 -25.731 1.00 25.77  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.645  -13.927 -32.460 1.00 25.36  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.133  -12.884 -33.389 1.00 23.25  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.434  -12.299 -32.851 1.00 24.17  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.526  -11.969 -31.673 1.00 25.16  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 13.974  -11.848 -33.422 1.00 25.42  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.208  -12.088 -32.120 1.00 24.69  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.288  -13.630 -31.970 1.00 25.56  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.478  -12.226 -33.686 1.00 22.88  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.785  -11.840 -33.188 1.00 22.85  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.626  -11.292 -34.336 1.00 23.24  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.169  -11.287 -35.483 1.00 27.04  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.476  -13.027 -32.522 1.00 23.57  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.831  -10.825 -33.984 1.00 26.64  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.768  -10.313 -34.978 1.00 27.56  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.170  -10.777 -34.619 1.00 26.06  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.444  -11.094 -33.458 1.00 26.95  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.750  -8.786  -35.124 1.00 27.32  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.379  -8.076  -33.934 1.00 28.69  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.170  -6.557  -34.061 1.00 28.47  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.783  -5.849  -32.935 1.00 27.29  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.472  -4.590  -32.592 1.00 32.69  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.524  -3.953  -33.272 1.00 27.21  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.150  -3.990  -31.614 1.00 28.36  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.021  -10.876 -35.659 1.00 27.23  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.451  -11.042 -35.485 1.00 30.66  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 25.990  -9.655  -35.138 1.00 30.82  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.714  -8.711  -35.871 1.00 31.97  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.093  -11.504 -36.804 1.00 32.02  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.353  -12.686 -37.415 1.00 31.67  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.587  -11.780 -36.606 1.00 34.72  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.373  -13.920 -36.544 1.00 29.22  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.716  -9.568  -34.023 1.00 33.01  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.388  -8.350  -33.593 1.00 41.56  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 28.863  -8.358  -34.026 1.00 47.42  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.415  -9.417  -34.310 1.00 45.56  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.313  -8.249  -32.081 1.00 36.27  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.103  -7.516  -31.512 1.00 40.24  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.267  -7.018  -32.302 1.00 42.02  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 26.017  -7.429  -30.276 1.00 37.69  ? 26  ASP B OD2 1 
ATOM   964  N N   A ASP B 1 28 ? 29.475  -7.162  -34.040 0.50 54.74  ? 27  ASP B N   1 
ATOM   965  N N   B ASP B 1 28 ? 29.499  -7.175  -34.066 0.50 54.52  ? 27  ASP B N   1 
ATOM   966  C CA  A ASP B 1 28 ? 30.913  -6.953  -34.165 0.50 56.61  ? 27  ASP B CA  1 
ATOM   967  C CA  B ASP B 1 28 ? 30.941  -7.076  -34.269 0.50 55.96  ? 27  ASP B CA  1 
ATOM   968  C C   A ASP B 1 28 ? 31.602  -7.437  -32.891 0.50 60.60  ? 27  ASP B C   1 
ATOM   969  C C   B ASP B 1 28 ? 31.633  -7.278  -32.919 0.50 60.90  ? 27  ASP B C   1 
ATOM   970  O O   A ASP B 1 28 ? 30.945  -7.612  -31.864 0.50 64.15  ? 27  ASP B O   1 
ATOM   971  O O   B ASP B 1 28 ? 31.005  -7.110  -31.874 0.50 66.73  ? 27  ASP B O   1 
ATOM   972  C CB  A ASP B 1 28 ? 31.222  -5.471  -34.325 0.50 52.38  ? 27  ASP B CB  1 
ATOM   973  C CB  B ASP B 1 28 ? 31.329  -5.762  -34.935 0.50 52.90  ? 27  ASP B CB  1 
ATOM   974  C CG  A ASP B 1 28 ? 30.337  -4.733  -35.317 0.50 50.92  ? 27  ASP B CG  1 
ATOM   975  C CG  B ASP B 1 28 ? 32.301  -5.877  -36.104 0.50 49.71  ? 27  ASP B CG  1 
ATOM   976  O OD1 A ASP B 1 28 ? 30.601  -4.834  -36.528 0.50 55.69  ? 27  ASP B OD1 1 
ATOM   977  O OD1 B ASP B 1 28 ? 33.273  -6.655  -36.002 0.50 50.75  ? 27  ASP B OD1 1 
ATOM   978  O OD2 A ASP B 1 28 ? 29.373  -4.088  -34.870 0.50 53.29  ? 27  ASP B OD2 1 
ATOM   979  O OD2 B ASP B 1 28 ? 32.084  -5.175  -37.110 0.50 49.16  ? 27  ASP B OD2 1 
ATOM   980  N N   . ILE B 1 29 ? 32.927  -7.629  -32.949 1.00 64.94  ? 28  ILE B N   1 
ATOM   981  C CA  . ILE B 1 29 ? 33.668  -8.060  -31.765 1.00 69.44  ? 28  ILE B CA  1 
ATOM   982  C C   . ILE B 1 29 ? 34.096  -6.849  -30.910 1.00 72.90  ? 28  ILE B C   1 
ATOM   983  O O   . ILE B 1 29 ? 34.566  -5.839  -31.492 1.00 77.57  ? 28  ILE B O   1 
ATOM   984  C CB  . ILE B 1 29 ? 34.850  -8.978  -32.129 1.00 64.86  ? 28  ILE B CB  1 
ATOM   985  N N   . PRO B 1 36 ? 34.992  -14.273 -29.323 1.00 56.57  ? 35  PRO B N   1 
ATOM   986  C CA  . PRO B 1 36 ? 34.218  -15.504 -29.475 1.00 54.45  ? 35  PRO B CA  1 
ATOM   987  C C   . PRO B 1 36 ? 35.123  -16.729 -29.515 1.00 47.37  ? 35  PRO B C   1 
ATOM   988  O O   . PRO B 1 36 ? 36.196  -16.663 -30.098 1.00 55.88  ? 35  PRO B O   1 
ATOM   989  C CB  . PRO B 1 36 ? 33.463  -15.313 -30.811 1.00 54.65  ? 35  PRO B CB  1 
ATOM   990  C CG  . PRO B 1 36 ? 34.276  -14.264 -31.541 1.00 58.71  ? 35  PRO B CG  1 
ATOM   991  C CD  . PRO B 1 36 ? 34.711  -13.343 -30.416 1.00 56.25  ? 35  PRO B CD  1 
ATOM   992  N N   . PRO B 1 37 ? 34.728  -17.886 -28.928 1.00 50.59  ? 36  PRO B N   1 
ATOM   993  C CA  . PRO B 1 37 ? 35.480  -19.127 -29.113 1.00 48.37  ? 36  PRO B CA  1 
ATOM   994  C C   . PRO B 1 37 ? 35.511  -19.454 -30.609 1.00 57.06  ? 36  PRO B C   1 
ATOM   995  O O   . PRO B 1 37 ? 34.786  -18.845 -31.395 1.00 51.67  ? 36  PRO B O   1 
ATOM   996  C CB  . PRO B 1 37 ? 34.725  -20.195 -28.296 1.00 51.00  ? 36  PRO B CB  1 
ATOM   997  C CG  . PRO B 1 37 ? 33.717  -19.423 -27.456 1.00 52.40  ? 36  PRO B CG  1 
ATOM   998  C CD  . PRO B 1 37 ? 33.531  -18.059 -28.089 1.00 46.60  ? 36  PRO B CD  1 
ATOM   999  N N   . PRO B 1 38 ? 36.337  -20.425 -31.070 1.00 61.30  ? 37  PRO B N   1 
ATOM   1000 C CA  . PRO B 1 38 ? 36.435  -20.723 -32.507 1.00 60.23  ? 37  PRO B CA  1 
ATOM   1001 C C   . PRO B 1 38 ? 35.132  -21.256 -33.110 1.00 51.56  ? 37  PRO B C   1 
ATOM   1002 O O   . PRO B 1 38 ? 34.405  -22.003 -32.460 1.00 51.87  ? 37  PRO B O   1 
ATOM   1003 C CB  . PRO B 1 38 ? 37.588  -21.753 -32.599 1.00 61.52  ? 37  PRO B CB  1 
ATOM   1004 C CG  . PRO B 1 38 ? 38.298  -21.666 -31.251 1.00 58.05  ? 37  PRO B CG  1 
ATOM   1005 C CD  . PRO B 1 38 ? 37.219  -21.271 -30.245 1.00 65.93  ? 37  PRO B CD  1 
ATOM   1006 N N   . ASN B 1 39 ? 34.844  -20.862 -34.356 1.00 47.75  ? 38  ASN B N   1 
ATOM   1007 C CA  . ASN B 1 39 ? 33.647  -21.306 -35.068 1.00 51.44  ? 38  ASN B CA  1 
ATOM   1008 C C   . ASN B 1 39 ? 32.361  -20.674 -34.520 1.00 45.30  ? 38  ASN B C   1 
ATOM   1009 O O   . ASN B 1 39 ? 31.286  -21.031 -34.984 1.00 42.49  ? 38  ASN B O   1 
ATOM   1010 C CB  . ASN B 1 39 ? 33.406  -22.816 -34.982 1.00 50.03  ? 38  ASN B CB  1 
ATOM   1011 C CG  . ASN B 1 39 ? 34.636  -23.663 -35.230 1.00 64.50  ? 38  ASN B CG  1 
ATOM   1012 O OD1 . ASN B 1 39 ? 34.885  -24.609 -34.474 1.00 71.98  ? 38  ASN B OD1 1 
ATOM   1013 N ND2 . ASN B 1 39 ? 35.405  -23.364 -36.269 1.00 63.47  ? 38  ASN B ND2 1 
ATOM   1014 N N   . LYS B 1 40 ? 32.454  -19.761 -33.534 1.00 44.93  ? 39  LYS B N   1 
ATOM   1015 C CA  . LYS B 1 40 ? 31.268  -19.197 -32.898 1.00 44.15  ? 39  LYS B CA  1 
ATOM   1016 C C   . LYS B 1 40 ? 31.178  -17.698 -33.159 1.00 40.77  ? 39  LYS B C   1 
ATOM   1017 O O   . LYS B 1 40 ? 32.174  -17.056 -33.466 1.00 40.61  ? 39  LYS B O   1 
ATOM   1018 C CB  . LYS B 1 40 ? 31.258  -19.498 -31.398 1.00 45.89  ? 39  LYS B CB  1 
ATOM   1019 C CG  . LYS B 1 40 ? 30.939  -20.942 -31.047 1.00 50.11  ? 39  LYS B CG  1 
ATOM   1020 C CD  . LYS B 1 40 ? 30.907  -21.087 -29.529 1.00 61.82  ? 39  LYS B CD  1 
ATOM   1021 C CE  . LYS B 1 40 ? 29.750  -21.871 -28.983 1.00 70.21  ? 39  LYS B CE  1 
ATOM   1022 N NZ  . LYS B 1 40 ? 29.604  -23.199 -29.581 1.00 70.52  ? 39  LYS B NZ  1 
ATOM   1023 N N   . TYR B 1 41 ? 29.971  -17.143 -33.046 1.00 37.58  ? 40  TYR B N   1 
ATOM   1024 C CA  . TYR B 1 41 ? 29.788  -15.730 -33.346 1.00 36.37  ? 40  TYR B CA  1 
ATOM   1025 C C   . TYR B 1 41 ? 29.193  -15.017 -32.140 1.00 39.18  ? 40  TYR B C   1 
ATOM   1026 O O   . TYR B 1 41 ? 28.396  -15.595 -31.413 1.00 35.82  ? 40  TYR B O   1 
ATOM   1027 C CB  . TYR B 1 41 ? 28.768  -15.577 -34.475 1.00 35.56  ? 40  TYR B CB  1 
ATOM   1028 C CG  . TYR B 1 41 ? 29.245  -16.028 -35.850 1.00 37.95  ? 40  TYR B CG  1 
ATOM   1029 C CD1 . TYR B 1 41 ? 29.840  -15.127 -36.729 1.00 34.77  ? 40  TYR B CD1 1 
ATOM   1030 C CD2 . TYR B 1 41 ? 29.099  -17.346 -36.269 1.00 37.54  ? 40  TYR B CD2 1 
ATOM   1031 C CE1 . TYR B 1 41 ? 30.309  -15.536 -37.970 1.00 38.01  ? 40  TYR B CE1 1 
ATOM   1032 C CE2 . TYR B 1 41 ? 29.535  -17.758 -37.519 1.00 35.30  ? 40  TYR B CE2 1 
ATOM   1033 C CZ  . TYR B 1 41 ? 30.160  -16.854 -38.365 1.00 38.50  ? 40  TYR B CZ  1 
ATOM   1034 O OH  . TYR B 1 41 ? 30.598  -17.221 -39.613 1.00 40.69  ? 40  TYR B OH  1 
ATOM   1035 N N   . PRO B 1 42 ? 29.469  -13.704 -31.956 1.00 40.44  ? 41  PRO B N   1 
ATOM   1036 C CA  . PRO B 1 42 ? 28.728  -12.912 -30.975 1.00 33.18  ? 41  PRO B CA  1 
ATOM   1037 C C   . PRO B 1 42 ? 27.299  -12.646 -31.442 1.00 29.59  ? 41  PRO B C   1 
ATOM   1038 O O   . PRO B 1 42 ? 27.094  -11.988 -32.476 1.00 34.75  ? 41  PRO B O   1 
ATOM   1039 C CB  . PRO B 1 42 ? 29.559  -11.612 -30.861 1.00 37.41  ? 41  PRO B CB  1 
ATOM   1040 C CG  . PRO B 1 42 ? 30.305  -11.502 -32.180 1.00 39.32  ? 41  PRO B CG  1 
ATOM   1041 C CD  . PRO B 1 42 ? 30.442  -12.915 -32.732 1.00 36.67  ? 41  PRO B CD  1 
ATOM   1042 N N   . ILE B 1 43 ? 26.322  -13.127 -30.647 1.00 30.40  ? 42  ILE B N   1 
ATOM   1043 C CA  . ILE B 1 43 ? 24.896  -12.934 -30.910 1.00 28.63  ? 42  ILE B CA  1 
ATOM   1044 C C   . ILE B 1 43 ? 24.305  -11.904 -29.942 1.00 30.11  ? 42  ILE B C   1 
ATOM   1045 O O   . ILE B 1 43 ? 24.596  -11.965 -28.759 1.00 31.29  ? 42  ILE B O   1 
ATOM   1046 C CB  . ILE B 1 43 ? 24.147  -14.271 -30.765 1.00 28.04  ? 42  ILE B CB  1 
ATOM   1047 C CG1 . ILE B 1 43 ? 24.868  -15.408 -31.542 1.00 27.25  ? 42  ILE B CG1 1 
ATOM   1048 C CG2 . ILE B 1 43 ? 22.689  -14.124 -31.211 1.00 29.38  ? 42  ILE B CG2 1 
ATOM   1049 C CD1 . ILE B 1 43 ? 25.217  -15.072 -32.981 1.00 29.21  ? 42  ILE B CD1 1 
ATOM   1050 N N   . PHE B 1 44 ? 23.456  -11.003 -30.460 1.00 29.51  ? 43  PHE B N   1 
ATOM   1051 C CA  . PHE B 1 44 ? 22.605  -10.118 -29.663 1.00 29.59  ? 43  PHE B CA  1 
ATOM   1052 C C   . PHE B 1 44 ? 21.147  -10.519 -29.884 1.00 26.90  ? 43  PHE B C   1 
ATOM   1053 O O   . PHE B 1 44 ? 20.665  -10.598 -31.019 1.00 26.18  ? 43  PHE B O   1 
ATOM   1054 C CB  . PHE B 1 44 ? 22.830  -8.661  -30.105 1.00 28.54  ? 43  PHE B CB  1 
ATOM   1055 C CG  . PHE B 1 44 ? 21.886  -7.641  -29.472 1.00 31.14  ? 43  PHE B CG  1 
ATOM   1056 C CD1 . PHE B 1 44 ? 20.736  -7.209  -30.138 1.00 28.75  ? 43  PHE B CD1 1 
ATOM   1057 C CD2 . PHE B 1 44 ? 22.157  -7.108  -28.220 1.00 40.05  ? 43  PHE B CD2 1 
ATOM   1058 C CE1 . PHE B 1 44 ? 19.882  -6.279  -29.569 1.00 32.94  ? 43  PHE B CE1 1 
ATOM   1059 C CE2 . PHE B 1 44 ? 21.310  -6.159  -27.653 1.00 38.13  ? 43  PHE B CE2 1 
ATOM   1060 C CZ  . PHE B 1 44 ? 20.170  -5.766  -28.323 1.00 39.56  ? 43  PHE B CZ  1 
ATOM   1061 N N   . PHE B 1 45 ? 20.429  -10.811 -28.789 1.00 28.65  ? 44  PHE B N   1 
ATOM   1062 C CA  . PHE B 1 45 ? 19.033  -11.192 -28.894 1.00 25.76  ? 44  PHE B CA  1 
ATOM   1063 C C   . PHE B 1 45 ? 18.179  -9.942  -28.774 1.00 27.74  ? 44  PHE B C   1 
ATOM   1064 O O   . PHE B 1 45 ? 18.225  -9.245  -27.752 1.00 29.67  ? 44  PHE B O   1 
ATOM   1065 C CB  . PHE B 1 45 ? 18.717  -12.165 -27.746 1.00 25.70  ? 44  PHE B CB  1 
ATOM   1066 C CG  . PHE B 1 45 ? 19.468  -13.485 -27.888 1.00 25.29  ? 44  PHE B CG  1 
ATOM   1067 C CD1 . PHE B 1 45 ? 20.719  -13.665 -27.310 1.00 29.83  ? 44  PHE B CD1 1 
ATOM   1068 C CD2 . PHE B 1 45 ? 18.912  -14.559 -28.578 1.00 26.21  ? 44  PHE B CD2 1 
ATOM   1069 C CE1 . PHE B 1 45 ? 21.405  -14.863 -27.459 1.00 35.29  ? 44  PHE B CE1 1 
ATOM   1070 C CE2 . PHE B 1 45 ? 19.594  -15.765 -28.712 1.00 28.92  ? 44  PHE B CE2 1 
ATOM   1071 C CZ  . PHE B 1 45 ? 20.851  -15.910 -28.180 1.00 31.25  ? 44  PHE B CZ  1 
ATOM   1072 N N   . PHE B 1 46 ? 17.350  -9.694  -29.800 1.00 25.94  ? 45  PHE B N   1 
ATOM   1073 C CA  . PHE B 1 46 ? 16.484  -8.538  -29.741 1.00 26.77  ? 45  PHE B CA  1 
ATOM   1074 C C   . PHE B 1 46 ? 15.450  -8.756  -28.621 1.00 28.55  ? 45  PHE B C   1 
ATOM   1075 O O   . PHE B 1 46 ? 15.179  -9.886  -28.214 1.00 24.85  ? 45  PHE B O   1 
ATOM   1076 C CB  . PHE B 1 46 ? 15.770  -8.409  -31.078 1.00 24.60  ? 45  PHE B CB  1 
ATOM   1077 C CG  . PHE B 1 46 ? 16.712  -7.962  -32.185 1.00 29.36  ? 45  PHE B CG  1 
ATOM   1078 C CD1 . PHE B 1 46 ? 17.217  -6.656  -32.201 1.00 31.96  ? 45  PHE B CD1 1 
ATOM   1079 C CD2 . PHE B 1 46 ? 17.037  -8.819  -33.236 1.00 27.47  ? 45  PHE B CD2 1 
ATOM   1080 C CE1 . PHE B 1 46 ? 18.076  -6.227  -33.216 1.00 28.41  ? 45  PHE B CE1 1 
ATOM   1081 C CE2 . PHE B 1 46 ? 17.863  -8.370  -34.272 1.00 28.84  ? 45  PHE B CE2 1 
ATOM   1082 C CZ  . PHE B 1 46 ? 18.360  -7.067  -34.267 1.00 25.92  ? 45  PHE B CZ  1 
ATOM   1083 N N   . GLY B 1 47 ? 14.895  -7.660  -28.099 1.00 30.91  ? 46  GLY B N   1 
ATOM   1084 C CA  . GLY B 1 47 ? 13.884  -7.771  -27.061 1.00 29.77  ? 46  GLY B CA  1 
ATOM   1085 C C   . GLY B 1 47 ? 14.534  -7.837  -25.681 1.00 32.77  ? 46  GLY B C   1 
ATOM   1086 O O   . GLY B 1 47 ? 14.265  -6.992  -24.853 1.00 36.97  ? 46  GLY B O   1 
ATOM   1087 N N   . THR B 1 48 ? 15.369  -8.836  -25.427 1.00 34.13  ? 47  THR B N   1 
ATOM   1088 C CA  . THR B 1 48 ? 15.962  -9.059  -24.122 1.00 33.74  ? 47  THR B CA  1 
ATOM   1089 C C   . THR B 1 48 ? 17.251  -8.272  -24.023 1.00 36.02  ? 47  THR B C   1 
ATOM   1090 O O   . THR B 1 48 ? 17.808  -8.072  -22.936 1.00 31.37  ? 47  THR B O   1 
ATOM   1091 C CB  . THR B 1 48 ? 16.295  -10.542 -23.970 1.00 31.95  ? 47  THR B CB  1 
ATOM   1092 O OG1 . THR B 1 48 ? 17.266  -10.856 -24.961 1.00 29.24  ? 47  THR B OG1 1 
ATOM   1093 C CG2 . THR B 1 48 ? 15.079  -11.425 -24.171 1.00 33.85  ? 47  THR B CG2 1 
ATOM   1094 N N   . HIS B 1 49 ? 17.796  -7.997  -25.206 1.00 37.47  ? 48  HIS B N   1 
ATOM   1095 C CA  . HIS B 1 49 ? 19.112  -7.418  -25.340 1.00 40.74  ? 48  HIS B CA  1 
ATOM   1096 C C   . HIS B 1 49 ? 20.199  -8.252  -24.650 1.00 43.72  ? 48  HIS B C   1 
ATOM   1097 O O   . HIS B 1 49 ? 21.232  -7.679  -24.318 1.00 43.91  ? 48  HIS B O   1 
ATOM   1098 C CB  . HIS B 1 49 ? 19.073  -5.942  -24.926 1.00 40.01  ? 48  HIS B CB  1 
ATOM   1099 C CG  . HIS B 1 49 ? 17.905  -5.205  -25.487 1.00 39.22  ? 48  HIS B CG  1 
ATOM   1100 N ND1 . HIS B 1 49 ? 17.187  -4.313  -24.723 1.00 41.16  ? 48  HIS B ND1 1 
ATOM   1101 C CD2 . HIS B 1 49 ? 17.278  -5.249  -26.691 1.00 39.83  ? 48  HIS B CD2 1 
ATOM   1102 C CE1 . HIS B 1 49 ? 16.170  -3.832  -25.440 1.00 44.09  ? 48  HIS B CE1 1 
ATOM   1103 N NE2 . HIS B 1 49 ? 16.199  -4.392  -26.639 1.00 43.52  ? 48  HIS B NE2 1 
ATOM   1104 N N   . GLU B 1 50 ? 19.987  -9.568  -24.433 1.00 39.12  ? 49  GLU B N   1 
ATOM   1105 C CA  . GLU B 1 50 ? 21.015  -10.475 -23.910 1.00 40.37  ? 49  GLU B CA  1 
ATOM   1106 C C   . GLU B 1 50 ? 21.972  -10.870 -25.038 1.00 35.86  ? 49  GLU B C   1 
ATOM   1107 O O   . GLU B 1 50 ? 21.659  -10.646 -26.205 1.00 36.29  ? 49  GLU B O   1 
ATOM   1108 C CB  . GLU B 1 50 ? 20.416  -11.824 -23.515 1.00 43.81  ? 49  GLU B CB  1 
ATOM   1109 C CG  . GLU B 1 50 ? 19.358  -11.712 -22.423 1.00 48.77  ? 49  GLU B CG  1 
ATOM   1110 C CD  . GLU B 1 50 ? 19.864  -12.127 -21.059 1.00 60.63  ? 49  GLU B CD  1 
ATOM   1111 O OE1 . GLU B 1 50 ? 19.342  -11.608 -20.053 1.00 64.25  ? 49  GLU B OE1 1 
ATOM   1112 O OE2 . GLU B 1 50 ? 20.758  -12.994 -21.000 1.00 67.60  ? 49  GLU B OE2 1 
ATOM   1113 N N   . THR B 1 51 ? 23.149  -11.406 -24.689 1.00 32.69  ? 50  THR B N   1 
ATOM   1114 C CA  . THR B 1 51 ? 24.149  -11.826 -25.665 1.00 33.05  ? 50  THR B CA  1 
ATOM   1115 C C   . THR B 1 51 ? 24.613  -13.248 -25.354 1.00 34.85  ? 50  THR B C   1 
ATOM   1116 O O   . THR B 1 51 ? 24.436  -13.757 -24.249 1.00 34.19  ? 50  THR B O   1 
ATOM   1117 C CB  . THR B 1 51 ? 25.320  -10.839 -25.731 1.00 39.51  ? 50  THR B CB  1 
ATOM   1118 O OG1 . THR B 1 51 ? 25.946  -10.936 -24.457 1.00 42.71  ? 50  THR B OG1 1 
ATOM   1119 C CG2 . THR B 1 51 ? 24.885  -9.396  -25.914 1.00 35.66  ? 50  THR B CG2 1 
ATOM   1120 N N   . ALA B 1 52 ? 25.176  -13.917 -26.365 1.00 35.55  ? 51  ALA B N   1 
ATOM   1121 C CA  . ALA B 1 52 ? 25.823  -15.201 -26.163 1.00 36.30  ? 51  ALA B CA  1 
ATOM   1122 C C   . ALA B 1 52 ? 26.697  -15.483 -27.381 1.00 34.28  ? 51  ALA B C   1 
ATOM   1123 O O   . ALA B 1 52 ? 26.686  -14.716 -28.343 1.00 36.11  ? 51  ALA B O   1 
ATOM   1124 C CB  . ALA B 1 52 ? 24.797  -16.282 -25.903 1.00 32.53  ? 51  ALA B CB  1 
ATOM   1125 N N   . PHE B 1 53 ? 27.506  -16.536 -27.287 1.00 31.60  ? 52  PHE B N   1 
ATOM   1126 C CA  . PHE B 1 53 ? 28.316  -17.003 -28.403 1.00 40.01  ? 52  PHE B CA  1 
ATOM   1127 C C   . PHE B 1 53 ? 27.665  -18.272 -28.951 1.00 37.88  ? 52  PHE B C   1 
ATOM   1128 O O   . PHE B 1 53 ? 27.430  -19.222 -28.198 1.00 36.72  ? 52  PHE B O   1 
ATOM   1129 C CB  . PHE B 1 53 ? 29.750  -17.283 -27.929 1.00 41.40  ? 52  PHE B CB  1 
ATOM   1130 C CG  . PHE B 1 53 ? 30.543  -16.050 -27.525 1.00 42.88  ? 52  PHE B CG  1 
ATOM   1131 C CD1 . PHE B 1 53 ? 30.722  -15.003 -28.419 1.00 44.90  ? 52  PHE B CD1 1 
ATOM   1132 C CD2 . PHE B 1 53 ? 31.076  -15.933 -26.243 1.00 47.10  ? 52  PHE B CD2 1 
ATOM   1133 C CE1 . PHE B 1 53 ? 31.418  -13.865 -28.048 1.00 42.30  ? 52  PHE B CE1 1 
ATOM   1134 C CE2 . PHE B 1 53 ? 31.770  -14.789 -25.871 1.00 45.88  ? 52  PHE B CE2 1 
ATOM   1135 C CZ  . PHE B 1 53 ? 31.939  -13.762 -26.770 1.00 42.05  ? 52  PHE B CZ  1 
ATOM   1136 N N   . LEU B 1 54 ? 27.359  -18.271 -30.256 1.00 34.29  ? 53  LEU B N   1 
ATOM   1137 C CA  . LEU B 1 54 ? 26.710  -19.429 -30.861 1.00 31.63  ? 53  LEU B CA  1 
ATOM   1138 C C   . LEU B 1 54 ? 27.423  -19.813 -32.161 1.00 31.64  ? 53  LEU B C   1 
ATOM   1139 O O   . LEU B 1 54 ? 27.958  -18.957 -32.879 1.00 33.02  ? 53  LEU B O   1 
ATOM   1140 C CB  . LEU B 1 54 ? 25.221  -19.225 -31.151 1.00 30.12  ? 53  LEU B CB  1 
ATOM   1141 C CG  . LEU B 1 54 ? 24.266  -19.119 -29.958 1.00 31.47  ? 53  LEU B CG  1 
ATOM   1142 C CD1 . LEU B 1 54 ? 22.940  -18.680 -30.531 1.00 28.99  ? 53  LEU B CD1 1 
ATOM   1143 C CD2 . LEU B 1 54 ? 24.124  -20.476 -29.249 1.00 29.06  ? 53  LEU B CD2 1 
ATOM   1144 N N   . GLY B 1 55 ? 27.323  -21.096 -32.496 1.00 29.93  ? 54  GLY B N   1 
ATOM   1145 C CA  . GLY B 1 55 ? 27.848  -21.574 -33.767 1.00 30.63  ? 54  GLY B CA  1 
ATOM   1146 C C   . GLY B 1 55 ? 26.737  -21.663 -34.819 1.00 33.78  ? 54  GLY B C   1 
ATOM   1147 O O   . GLY B 1 55 ? 25.541  -21.602 -34.503 1.00 31.10  ? 54  GLY B O   1 
ATOM   1148 N N   . PRO B 1 56 ? 27.101  -21.813 -36.112 1.00 28.40  ? 55  PRO B N   1 
ATOM   1149 C CA  . PRO B 1 56 ? 26.111  -21.928 -37.184 1.00 29.80  ? 55  PRO B CA  1 
ATOM   1150 C C   . PRO B 1 56 ? 25.025  -22.993 -36.960 1.00 30.79  ? 55  PRO B C   1 
ATOM   1151 O O   . PRO B 1 56 ? 23.994  -22.647 -37.606 1.00 25.59  ? 55  PRO B O   1 
ATOM   1152 C CB  . PRO B 1 56 ? 26.968  -22.265 -38.423 1.00 32.88  ? 55  PRO B CB  1 
ATOM   1153 C CG  . PRO B 1 56 ? 28.386  -21.903 -38.075 1.00 30.33  ? 55  PRO B CG  1 
ATOM   1154 C CD  . PRO B 1 56 ? 28.493  -21.898 -36.573 1.00 31.22  ? 55  PRO B CD  1 
ATOM   1155 N N   . ASP B 1 58 ? 23.038  -23.370 -35.028 1.00 27.77  ? 57  ASP B N   1 
ATOM   1156 C CA  . ASP B 1 58 ? 22.019  -22.688 -34.170 1.00 28.91  ? 57  ASP B CA  1 
ATOM   1157 C C   . ASP B 1 58 ? 21.599  -21.327 -34.725 1.00 30.88  ? 57  ASP B C   1 
ATOM   1158 O O   . ASP B 1 58 ? 20.859  -20.577 -34.036 1.00 26.90  ? 57  ASP B O   1 
ATOM   1159 C CB  . ASP B 1 58 ? 22.479  -22.577 -32.723 1.00 30.88  ? 57  ASP B CB  1 
ATOM   1160 C CG  . ASP B 1 58 ? 22.529  -23.888 -31.937 1.00 34.69  ? 57  ASP B CG  1 
ATOM   1161 O OD1 . ASP B 1 58 ? 21.600  -24.693 -32.082 1.00 34.09  ? 57  ASP B OD1 1 
ATOM   1162 O OD2 . ASP B 1 58 ? 23.463  -24.052 -31.138 1.00 34.87  ? 57  ASP B OD2 1 
ATOM   1163 N N   . LEU B 1 59 ? 22.079  -21.008 -35.942 1.00 27.60  ? 58  LEU B N   1 
ATOM   1164 C CA  . LEU B 1 59 ? 21.844  -19.702 -36.561 1.00 27.50  ? 58  LEU B CA  1 
ATOM   1165 C C   . LEU B 1 59 ? 21.087  -19.860 -37.875 1.00 27.62  ? 58  LEU B C   1 
ATOM   1166 O O   . LEU B 1 59 ? 21.569  -20.491 -38.817 1.00 28.44  ? 58  LEU B O   1 
ATOM   1167 C CB  . LEU B 1 59 ? 23.152  -18.935 -36.767 1.00 30.75  ? 58  LEU B CB  1 
ATOM   1168 C CG  . LEU B 1 59 ? 23.962  -18.681 -35.497 1.00 27.70  ? 58  LEU B CG  1 
ATOM   1169 C CD1 . LEU B 1 59 ? 25.275  -17.999 -35.805 1.00 30.72  ? 58  LEU B CD1 1 
ATOM   1170 C CD2 . LEU B 1 59 ? 23.144  -17.832 -34.525 1.00 28.32  ? 58  LEU B CD2 1 
ATOM   1171 N N   . PHE B 1 60 ? 19.894  -19.268 -37.923 1.00 24.59  ? 59  PHE B N   1 
ATOM   1172 C CA  . PHE B 1 60 ? 18.989  -19.437 -39.038 1.00 24.77  ? 59  PHE B CA  1 
ATOM   1173 C C   . PHE B 1 60 ? 18.854  -18.074 -39.715 1.00 27.23  ? 59  PHE B C   1 
ATOM   1174 O O   . PHE B 1 60 ? 18.244  -17.170 -39.152 1.00 26.05  ? 59  PHE B O   1 
ATOM   1175 C CB  . PHE B 1 60 ? 17.640  -19.968 -38.538 1.00 26.30  ? 59  PHE B CB  1 
ATOM   1176 C CG  . PHE B 1 60 ? 17.753  -21.392 -37.974 1.00 25.00  ? 59  PHE B CG  1 
ATOM   1177 C CD1 . PHE B 1 60 ? 18.277  -21.614 -36.703 1.00 29.53  ? 59  PHE B CD1 1 
ATOM   1178 C CD2 . PHE B 1 60 ? 17.328  -22.488 -38.725 1.00 28.82  ? 59  PHE B CD2 1 
ATOM   1179 C CE1 . PHE B 1 60 ? 18.415  -22.904 -36.187 1.00 33.03  ? 59  PHE B CE1 1 
ATOM   1180 C CE2 . PHE B 1 60 ? 17.430  -23.784 -38.204 1.00 31.56  ? 59  PHE B CE2 1 
ATOM   1181 C CZ  . PHE B 1 60 ? 17.985  -23.988 -36.941 1.00 34.21  ? 59  PHE B CZ  1 
ATOM   1182 N N   . PRO B 1 61 ? 19.373  -17.881 -40.954 1.00 32.11  ? 60  PRO B N   1 
ATOM   1183 C CA  . PRO B 1 61 ? 19.132  -16.609 -41.658 1.00 31.40  ? 60  PRO B CA  1 
ATOM   1184 C C   . PRO B 1 61 ? 17.688  -16.098 -41.589 1.00 29.69  ? 60  PRO B C   1 
ATOM   1185 O O   . PRO B 1 61 ? 16.714  -16.825 -41.848 1.00 27.96  ? 60  PRO B O   1 
ATOM   1186 C CB  . PRO B 1 61 ? 19.649  -16.866 -43.098 1.00 30.88  ? 60  PRO B CB  1 
ATOM   1187 C CG  . PRO B 1 61 ? 20.709  -17.942 -42.911 1.00 35.84  ? 60  PRO B CG  1 
ATOM   1188 C CD  . PRO B 1 61 ? 20.216  -18.821 -41.724 1.00 32.15  ? 60  PRO B CD  1 
ATOM   1189 N N   . TYR B 1 62 ? 17.538  -14.795 -41.266 1.00 28.55  ? 61  TYR B N   1 
ATOM   1190 C CA  . TYR B 1 62 ? 16.237  -14.276 -40.888 1.00 30.02  ? 61  TYR B CA  1 
ATOM   1191 C C   . TYR B 1 62 ? 15.244  -14.308 -42.037 1.00 32.16  ? 61  TYR B C   1 
ATOM   1192 O O   . TYR B 1 62 ? 14.090  -14.677 -41.845 1.00 32.52  ? 61  TYR B O   1 
ATOM   1193 C CB  . TYR B 1 62 ? 16.363  -12.819 -40.433 1.00 31.30  ? 61  TYR B CB  1 
ATOM   1194 C CG  . TYR B 1 62 ? 15.023  -12.163 -40.168 1.00 33.06  ? 61  TYR B CG  1 
ATOM   1195 C CD1 . TYR B 1 62 ? 14.306  -12.433 -39.003 1.00 34.42  ? 61  TYR B CD1 1 
ATOM   1196 C CD2 . TYR B 1 62 ? 14.512  -11.232 -41.065 1.00 39.44  ? 61  TYR B CD2 1 
ATOM   1197 C CE1 . TYR B 1 62 ? 13.099  -11.797 -38.755 1.00 35.67  ? 61  TYR B CE1 1 
ATOM   1198 C CE2 . TYR B 1 62 ? 13.311  -10.584 -40.823 1.00 44.21  ? 61  TYR B CE2 1 
ATOM   1199 C CZ  . TYR B 1 62 ? 12.606  -10.879 -39.670 1.00 37.98  ? 61  TYR B CZ  1 
ATOM   1200 O OH  . TYR B 1 62 ? 11.430  -10.233 -39.464 1.00 41.25  ? 61  TYR B OH  1 
ATOM   1201 N N   . ASP B 1 63 ? 15.699  -13.906 -43.231 1.00 38.36  ? 62  ASP B N   1 
ATOM   1202 C CA  . ASP B 1 63 ? 14.814  -13.835 -44.389 1.00 45.48  ? 62  ASP B CA  1 
ATOM   1203 C C   . ASP B 1 63 ? 14.270  -15.217 -44.747 1.00 38.99  ? 62  ASP B C   1 
ATOM   1204 O O   . ASP B 1 63 ? 13.063  -15.373 -44.926 1.00 43.00  ? 62  ASP B O   1 
ATOM   1205 C CB  . ASP B 1 63 ? 15.484  -13.180 -45.581 1.00 51.16  ? 62  ASP B CB  1 
ATOM   1206 C CG  . ASP B 1 63 ? 15.144  -11.713 -45.785 1.00 67.21  ? 62  ASP B CG  1 
ATOM   1207 O OD1 . ASP B 1 63 ? 14.596  -11.080 -44.843 1.00 63.34  ? 62  ASP B OD1 1 
ATOM   1208 O OD2 . ASP B 1 63 ? 15.394  -11.226 -46.906 1.00 74.95  ? 62  ASP B OD2 1 
ATOM   1209 N N   . LYS B 1 64 ? 15.153  -16.215 -44.790 1.00 39.90  ? 63  LYS B N   1 
ATOM   1210 C CA  . LYS B 1 64 ? 14.732  -17.575 -45.094 1.00 39.35  ? 63  LYS B CA  1 
ATOM   1211 C C   . LYS B 1 64 ? 13.705  -18.071 -44.073 1.00 37.42  ? 63  LYS B C   1 
ATOM   1212 O O   . LYS B 1 64 ? 12.792  -18.829 -44.406 1.00 38.21  ? 63  LYS B O   1 
ATOM   1213 C CB  . LYS B 1 64 ? 15.931  -18.529 -45.098 1.00 44.63  ? 63  LYS B CB  1 
ATOM   1214 C CG  . LYS B 1 64 ? 15.614  -19.909 -45.668 1.00 44.57  ? 63  LYS B CG  1 
ATOM   1215 C CD  . LYS B 1 64 ? 16.798  -20.863 -45.680 1.00 49.96  ? 63  LYS B CD  1 
ATOM   1216 C CE  . LYS B 1 64 ? 16.546  -22.190 -46.384 1.00 47.31  ? 63  LYS B CE  1 
ATOM   1217 N NZ  . LYS B 1 64 ? 15.263  -22.840 -46.106 1.00 48.43  ? 63  LYS B NZ  1 
ATOM   1218 N N   . SER B 1 65 ? 13.854  -17.664 -42.815 1.00 36.09  ? 64  SER B N   1 
ATOM   1219 C CA  . SER B 1 65 ? 13.204  -18.460 -41.776 1.00 39.32  ? 64  SER B CA  1 
ATOM   1220 C C   . SER B 1 65 ? 12.081  -17.711 -41.048 1.00 37.81  ? 64  SER B C   1 
ATOM   1221 O O   . SER B 1 65 ? 11.431  -18.272 -40.167 1.00 33.38  ? 64  SER B O   1 
ATOM   1222 C CB  . SER B 1 65 ? 14.240  -19.080 -40.856 1.00 37.65  ? 64  SER B CB  1 
ATOM   1223 O OG  . SER B 1 65 ? 15.064  -18.083 -40.276 1.00 50.56  ? 64  SER B OG  1 
ATOM   1224 N N   . LYS B 1 66 ? 11.779  -16.475 -41.474 1.00 36.19  ? 65  LYS B N   1 
ATOM   1225 C CA  . LYS B 1 66 ? 10.899  -15.623 -40.677 1.00 35.93  ? 65  LYS B CA  1 
ATOM   1226 C C   . LYS B 1 66 ? 9.457   -16.126 -40.635 1.00 39.21  ? 65  LYS B C   1 
ATOM   1227 O O   . LYS B 1 66 ? 8.747   -15.887 -39.668 1.00 42.09  ? 65  LYS B O   1 
ATOM   1228 C CB  . LYS B 1 66 ? 10.953  -14.131 -41.041 1.00 37.59  ? 65  LYS B CB  1 
ATOM   1229 C CG  . LYS B 1 66 ? 10.626  -13.797 -42.493 1.00 34.38  ? 65  LYS B CG  1 
ATOM   1230 N N   . ASP B 1 67 ? 8.970   -16.807 -41.668 1.00 42.75  ? 66  ASP B N   1 
ATOM   1231 C CA  . ASP B 1 67 ? 7.572   -17.194 -41.554 1.00 47.03  ? 66  ASP B CA  1 
ATOM   1232 C C   . ASP B 1 67 ? 7.445   -18.444 -40.680 1.00 44.80  ? 66  ASP B C   1 
ATOM   1233 O O   . ASP B 1 67 ? 6.386   -18.701 -40.093 1.00 45.07  ? 66  ASP B O   1 
ATOM   1234 C CB  . ASP B 1 67 ? 6.809   -17.126 -42.869 1.00 67.35  ? 66  ASP B CB  1 
ATOM   1235 C CG  . ASP B 1 67 ? 7.446   -17.832 -44.056 1.00 80.43  ? 66  ASP B CG  1 
ATOM   1236 O OD1 . ASP B 1 67 ? 7.549   -17.198 -45.135 1.00 82.73  ? 66  ASP B OD1 1 
ATOM   1237 O OD2 . ASP B 1 67 ? 7.832   -19.009 -43.889 1.00 90.92  ? 66  ASP B OD2 1 
ATOM   1238 N N   . LYS B 1 68 ? 8.547   -19.191 -40.559 1.00 39.43  ? 67  LYS B N   1 
ATOM   1239 C CA  . LYS B 1 68 ? 8.535   -20.360 -39.696 1.00 35.51  ? 67  LYS B CA  1 
ATOM   1240 C C   . LYS B 1 68 ? 8.706   -19.919 -38.244 1.00 33.21  ? 67  LYS B C   1 
ATOM   1241 O O   . LYS B 1 68 ? 7.956   -20.368 -37.370 1.00 34.01  ? 67  LYS B O   1 
ATOM   1242 C CB  . LYS B 1 68 ? 9.604   -21.358 -40.146 1.00 39.21  ? 67  LYS B CB  1 
ATOM   1243 C CG  . LYS B 1 68 ? 9.729   -22.641 -39.322 1.00 46.87  ? 67  LYS B CG  1 
ATOM   1244 C CD  . LYS B 1 68 ? 10.567  -23.629 -40.129 1.00 59.51  ? 67  LYS B CD  1 
ATOM   1245 C CE  . LYS B 1 68 ? 11.014  -24.864 -39.406 1.00 69.27  ? 67  LYS B CE  1 
ATOM   1246 N NZ  . LYS B 1 68 ? 9.898   -25.737 -39.033 1.00 71.25  ? 67  LYS B NZ  1 
ATOM   1247 N N   . TYR B 1 69 ? 9.695   -19.050 -37.976 1.00 29.93  ? 68  TYR B N   1 
ATOM   1248 C CA  . TYR B 1 69 ? 10.051  -18.811 -36.575 1.00 26.29  ? 68  TYR B CA  1 
ATOM   1249 C C   . TYR B 1 69 ? 9.501   -17.480 -36.062 1.00 33.55  ? 68  TYR B C   1 
ATOM   1250 O O   . TYR B 1 69 ? 9.584   -17.215 -34.854 1.00 32.02  ? 68  TYR B O   1 
ATOM   1251 C CB  . TYR B 1 69 ? 11.558  -18.859 -36.349 1.00 27.81  ? 68  TYR B CB  1 
ATOM   1252 C CG  . TYR B 1 69 ? 12.152  -20.223 -36.664 1.00 29.35  ? 68  TYR B CG  1 
ATOM   1253 C CD1 . TYR B 1 69 ? 11.638  -21.375 -36.078 1.00 31.36  ? 68  TYR B CD1 1 
ATOM   1254 C CD2 . TYR B 1 69 ? 13.237  -20.347 -37.522 1.00 31.44  ? 68  TYR B CD2 1 
ATOM   1255 C CE1 . TYR B 1 69 ? 12.164  -22.630 -36.351 1.00 32.03  ? 68  TYR B CE1 1 
ATOM   1256 C CE2 . TYR B 1 69 ? 13.778  -21.591 -37.807 1.00 33.40  ? 68  TYR B CE2 1 
ATOM   1257 C CZ  . TYR B 1 69 ? 13.241  -22.724 -37.214 1.00 32.29  ? 68  TYR B CZ  1 
ATOM   1258 O OH  . TYR B 1 69 ? 13.785  -23.928 -37.487 1.00 31.16  ? 68  TYR B OH  1 
ATOM   1259 N N   . GLY B 1 70 ? 8.981   -16.630 -36.965 1.00 32.39  ? 69  GLY B N   1 
ATOM   1260 C CA  . GLY B 1 70 ? 8.750   -15.243 -36.576 1.00 38.00  ? 69  GLY B CA  1 
ATOM   1261 C C   . GLY B 1 70 ? 7.339   -14.999 -36.043 1.00 44.19  ? 69  GLY B C   1 
ATOM   1262 O O   . GLY B 1 70 ? 6.743   -13.970 -36.348 1.00 41.90  ? 69  GLY B O   1 
ATOM   1263 N N   . LYS B 1 71 ? 6.798   -15.956 -35.284 1.00 47.01  ? 70  LYS B N   1 
ATOM   1264 C CA  . LYS B 1 71 ? 5.428   -15.846 -34.828 1.00 47.12  ? 70  LYS B CA  1 
ATOM   1265 C C   . LYS B 1 71 ? 5.455   -15.489 -33.354 1.00 50.39  ? 70  LYS B C   1 
ATOM   1266 O O   . LYS B 1 71 ? 6.297   -16.012 -32.628 1.00 44.70  ? 70  LYS B O   1 
ATOM   1267 C CB  . LYS B 1 71 ? 4.686   -17.167 -35.049 1.00 50.62  ? 70  LYS B CB  1 
ATOM   1268 C CG  . LYS B 1 71 ? 4.326   -17.337 -36.528 1.00 58.28  ? 70  LYS B CG  1 
ATOM   1269 C CD  . LYS B 1 71 ? 3.918   -18.718 -37.029 1.00 56.21  ? 70  LYS B CD  1 
ATOM   1270 C CE  . LYS B 1 71 ? 3.355   -18.645 -38.429 1.00 62.45  ? 70  LYS B CE  1 
ATOM   1271 N NZ  . LYS B 1 71 ? 4.100   -17.782 -39.360 1.00 64.49  ? 70  LYS B NZ  1 
ATOM   1272 N N   . PRO B 1 72 ? 4.556   -14.586 -32.891 1.00 52.44  ? 71  PRO B N   1 
ATOM   1273 C CA  . PRO B 1 72 ? 4.511   -14.207 -31.475 1.00 50.58  ? 71  PRO B CA  1 
ATOM   1274 C C   . PRO B 1 72 ? 4.257   -15.384 -30.528 1.00 49.52  ? 71  PRO B C   1 
ATOM   1275 O O   . PRO B 1 72 ? 3.640   -16.372 -30.921 1.00 41.96  ? 71  PRO B O   1 
ATOM   1276 C CB  . PRO B 1 72 ? 3.430   -13.098 -31.403 1.00 51.54  ? 71  PRO B CB  1 
ATOM   1277 C CG  . PRO B 1 72 ? 3.291   -12.628 -32.836 1.00 57.46  ? 71  PRO B CG  1 
ATOM   1278 C CD  . PRO B 1 72 ? 3.585   -13.844 -33.717 1.00 53.63  ? 71  PRO B CD  1 
ATOM   1279 N N   . ASN B 1 73 ? 4.770   -15.275 -29.287 1.00 41.32  ? 72  ASN B N   1 
ATOM   1280 C CA  . ASN B 1 73 ? 4.521   -16.272 -28.250 1.00 39.78  ? 72  ASN B CA  1 
ATOM   1281 C C   . ASN B 1 73 ? 4.513   -15.585 -26.874 1.00 40.23  ? 72  ASN B C   1 
ATOM   1282 O O   . ASN B 1 73 ? 4.569   -14.356 -26.789 1.00 42.46  ? 72  ASN B O   1 
ATOM   1283 C CB  . ASN B 1 73 ? 5.539   -17.410 -28.303 1.00 37.05  ? 72  ASN B CB  1 
ATOM   1284 C CG  . ASN B 1 73 ? 6.955   -16.916 -28.109 1.00 34.55  ? 72  ASN B CG  1 
ATOM   1285 O OD1 . ASN B 1 73 ? 7.218   -16.159 -27.165 1.00 34.07  ? 72  ASN B OD1 1 
ATOM   1286 N ND2 . ASN B 1 73 ? 7.876   -17.299 -28.989 1.00 32.80  ? 72  ASN B ND2 1 
ATOM   1287 N N   . LYS B 1 74 ? 4.563   -16.392 -25.811 1.00 42.09  ? 73  LYS B N   1 
ATOM   1288 C CA  . LYS B 1 74 ? 4.396   -15.901 -24.448 1.00 46.51  ? 73  LYS B CA  1 
ATOM   1289 C C   . LYS B 1 74 ? 5.732   -15.640 -23.729 1.00 46.17  ? 73  LYS B C   1 
ATOM   1290 O O   . LYS B 1 74 ? 5.721   -15.330 -22.538 1.00 40.19  ? 73  LYS B O   1 
ATOM   1291 C CB  . LYS B 1 74 ? 3.566   -16.927 -23.657 1.00 42.94  ? 73  LYS B CB  1 
ATOM   1292 N N   . ARG B 1 75 ? 6.879   -15.768 -24.416 1.00 33.13  ? 74  ARG B N   1 
ATOM   1293 C CA  . ARG B 1 75 ? 8.165   -15.566 -23.765 1.00 30.61  ? 74  ARG B CA  1 
ATOM   1294 C C   . ARG B 1 75 ? 8.451   -14.072 -23.650 1.00 32.47  ? 74  ARG B C   1 
ATOM   1295 O O   . ARG B 1 75 ? 8.231   -13.292 -24.597 1.00 33.05  ? 74  ARG B O   1 
ATOM   1296 C CB  . ARG B 1 75 ? 9.325   -16.318 -24.432 1.00 33.21  ? 74  ARG B CB  1 
ATOM   1297 C CG  . ARG B 1 75 ? 9.100   -17.807 -24.659 1.00 31.53  ? 74  ARG B CG  1 
ATOM   1298 C CD  . ARG B 1 75 ? 9.007   -18.559 -23.333 1.00 36.57  ? 74  ARG B CD  1 
ATOM   1299 N NE  . ARG B 1 75 ? 9.183   -19.991 -23.585 1.00 33.27  ? 74  ARG B NE  1 
ATOM   1300 C CZ  . ARG B 1 75 ? 10.293  -20.658 -23.387 1.00 32.44  ? 74  ARG B CZ  1 
ATOM   1301 N NH1 . ARG B 1 75 ? 11.373  -20.045 -22.911 1.00 38.48  ? 74  ARG B NH1 1 
ATOM   1302 N NH2 . ARG B 1 75 ? 10.335  -21.930 -23.737 1.00 36.64  ? 74  ARG B NH2 1 
ATOM   1303 N N   . LYS B 1 76 ? 8.942   -13.674 -22.462 1.00 30.51  ? 75  LYS B N   1 
ATOM   1304 C CA  . LYS B 1 76 ? 9.210   -12.277 -22.162 1.00 26.62  ? 75  LYS B CA  1 
ATOM   1305 C C   . LYS B 1 76 ? 10.309  -11.749 -23.099 1.00 25.41  ? 75  LYS B C   1 
ATOM   1306 O O   . LYS B 1 76 ? 11.394  -12.338 -23.155 1.00 25.98  ? 75  LYS B O   1 
ATOM   1307 C CB  . LYS B 1 76 ? 9.692   -12.169 -20.708 1.00 33.78  ? 75  LYS B CB  1 
ATOM   1308 C CG  . LYS B 1 76 ? 10.124  -10.749 -20.306 1.00 33.23  ? 75  LYS B CG  1 
ATOM   1309 C CD  . LYS B 1 76 ? 10.655  -10.630 -18.887 1.00 34.30  ? 75  LYS B CD  1 
ATOM   1310 C CE  . LYS B 1 76 ? 11.017  -9.196  -18.511 1.00 44.23  ? 75  LYS B CE  1 
ATOM   1311 N NZ  . LYS B 1 76 ? 11.284  -9.061  -17.073 1.00 50.12  ? 75  LYS B NZ  1 
ATOM   1312 N N   . GLY B 1 77 ? 10.010  -10.644 -23.789 1.00 26.84  ? 76  GLY B N   1 
ATOM   1313 C CA  . GLY B 1 77 ? 10.962  -9.987  -24.685 1.00 29.76  ? 76  GLY B CA  1 
ATOM   1314 C C   . GLY B 1 77 ? 10.820  -10.444 -26.144 1.00 29.50  ? 76  GLY B C   1 
ATOM   1315 O O   . GLY B 1 77 ? 11.320  -9.787  -27.050 1.00 30.55  ? 76  GLY B O   1 
ATOM   1316 N N   . PHE B 1 78 ? 10.110  -11.556 -26.401 1.00 28.62  ? 77  PHE B N   1 
ATOM   1317 C CA  . PHE B 1 78 ? 9.990   -12.085 -27.767 1.00 25.38  ? 77  PHE B CA  1 
ATOM   1318 C C   . PHE B 1 78 ? 9.246   -11.145 -28.709 1.00 27.38  ? 77  PHE B C   1 
ATOM   1319 O O   . PHE B 1 78 ? 9.674   -10.893 -29.831 1.00 23.61  ? 77  PHE B O   1 
ATOM   1320 C CB  . PHE B 1 78 ? 9.291   -13.444 -27.754 1.00 26.09  ? 77  PHE B CB  1 
ATOM   1321 C CG  . PHE B 1 78 ? 9.528   -14.196 -29.049 1.00 27.85  ? 77  PHE B CG  1 
ATOM   1322 C CD1 . PHE B 1 78 ? 10.677  -14.967 -29.212 1.00 26.46  ? 77  PHE B CD1 1 
ATOM   1323 C CD2 . PHE B 1 78 ? 8.590   -14.141 -30.074 1.00 30.12  ? 77  PHE B CD2 1 
ATOM   1324 C CE1 . PHE B 1 78 ? 10.887  -15.667 -30.390 1.00 28.06  ? 77  PHE B CE1 1 
ATOM   1325 C CE2 . PHE B 1 78 ? 8.814   -14.835 -31.255 1.00 32.31  ? 77  PHE B CE2 1 
ATOM   1326 C CZ  . PHE B 1 78 ? 9.962   -15.582 -31.404 1.00 28.46  ? 77  PHE B CZ  1 
ATOM   1327 N N   . ASN B 1 79 ? 8.093   -10.622 -28.307 1.00 27.59  ? 78  ASN B N   1 
ATOM   1328 C CA  . ASN B 1 79 ? 7.363   -9.828  -29.284 1.00 28.25  ? 78  ASN B CA  1 
ATOM   1329 C C   . ASN B 1 79 ? 8.063   -8.483  -29.474 1.00 30.16  ? 78  ASN B C   1 
ATOM   1330 O O   . ASN B 1 79 ? 8.013   -7.892  -30.553 1.00 32.35  ? 78  ASN B O   1 
ATOM   1331 C CB  . ASN B 1 79 ? 5.891   -9.658  -28.911 1.00 33.16  ? 78  ASN B CB  1 
ATOM   1332 C CG  . ASN B 1 79 ? 5.149   -10.976 -28.890 1.00 41.74  ? 78  ASN B CG  1 
ATOM   1333 O OD1 . ASN B 1 79 ? 5.607   -11.969 -29.470 1.00 39.51  ? 78  ASN B OD1 1 
ATOM   1334 N ND2 . ASN B 1 79 ? 4.024   -11.024 -28.191 1.00 40.67  ? 78  ASN B ND2 1 
ATOM   1335 N N   . GLU B 1 80 ? 8.722   -8.009  -28.423 1.00 28.65  ? 79  GLU B N   1 
ATOM   1336 C CA  . GLU B 1 80 ? 9.523   -6.799  -28.547 1.00 33.86  ? 79  GLU B CA  1 
ATOM   1337 C C   . GLU B 1 80 ? 10.676  -7.056  -29.521 1.00 28.24  ? 79  GLU B C   1 
ATOM   1338 O O   . GLU B 1 80 ? 11.024  -6.163  -30.296 1.00 29.41  ? 79  GLU B O   1 
ATOM   1339 C CB  . GLU B 1 80 ? 10.104  -6.277  -27.236 1.00 31.48  ? 79  GLU B CB  1 
ATOM   1340 C CG  . GLU B 1 80 ? 9.164   -5.314  -26.526 1.00 42.33  ? 79  GLU B CG  1 
ATOM   1341 N N   . GLY B 1 81 ? 11.241  -8.277  -29.468 1.00 26.80  ? 80  GLY B N   1 
ATOM   1342 C CA  . GLY B 1 81 ? 12.380  -8.663  -30.304 1.00 26.68  ? 80  GLY B CA  1 
ATOM   1343 C C   . GLY B 1 81 ? 11.951  -8.733  -31.762 1.00 28.00  ? 80  GLY B C   1 
ATOM   1344 O O   . GLY B 1 81 ? 12.685  -8.326  -32.665 1.00 28.26  ? 80  GLY B O   1 
ATOM   1345 N N   . LEU B 1 82 ? 10.713  -9.171  -31.967 1.00 23.84  ? 81  LEU B N   1 
ATOM   1346 C CA  . LEU B 1 82 ? 10.177  -9.224  -33.321 1.00 29.95  ? 81  LEU B CA  1 
ATOM   1347 C C   . LEU B 1 82 ? 10.019  -7.796  -33.831 1.00 32.10  ? 81  LEU B C   1 
ATOM   1348 O O   . LEU B 1 82 ? 10.249  -7.538  -35.008 1.00 29.54  ? 81  LEU B O   1 
ATOM   1349 C CB  . LEU B 1 82 ? 8.848   -9.988  -33.368 1.00 26.40  ? 81  LEU B CB  1 
ATOM   1350 C CG  . LEU B 1 82 ? 8.919   -11.510 -33.165 1.00 26.31  ? 81  LEU B CG  1 
ATOM   1351 C CD1 . LEU B 1 82 ? 7.523   -12.125 -33.198 1.00 27.99  ? 81  LEU B CD1 1 
ATOM   1352 C CD2 . LEU B 1 82 ? 9.833   -12.157 -34.193 1.00 25.40  ? 81  LEU B CD2 1 
ATOM   1353 N N   . TRP B 1 83 ? 9.626   -6.868  -32.945 1.00 28.93  ? 82  TRP B N   1 
ATOM   1354 C CA  . TRP B 1 83 ? 9.469   -5.480  -33.362 1.00 28.81  ? 82  TRP B CA  1 
ATOM   1355 C C   . TRP B 1 83 ? 10.814  -4.882  -33.761 1.00 26.61  ? 82  TRP B C   1 
ATOM   1356 O O   . TRP B 1 83 ? 10.887  -4.190  -34.775 1.00 29.05  ? 82  TRP B O   1 
ATOM   1357 C CB  . TRP B 1 83 ? 8.791   -4.606  -32.296 1.00 29.69  ? 82  TRP B CB  1 
ATOM   1358 C CG  . TRP B 1 83 ? 8.534   -3.210  -32.804 1.00 33.11  ? 82  TRP B CG  1 
ATOM   1359 C CD1 . TRP B 1 83 ? 7.407   -2.737  -33.413 1.00 36.63  ? 82  TRP B CD1 1 
ATOM   1360 C CD2 . TRP B 1 83 ? 9.480   -2.119  -32.799 1.00 32.66  ? 82  TRP B CD2 1 
ATOM   1361 N NE1 . TRP B 1 83 ? 7.590   -1.426  -33.781 1.00 35.23  ? 82  TRP B NE1 1 
ATOM   1362 C CE2 . TRP B 1 83 ? 8.848   -1.024  -33.417 1.00 35.28  ? 82  TRP B CE2 1 
ATOM   1363 C CE3 . TRP B 1 83 ? 10.791  -1.966  -32.323 1.00 35.71  ? 82  TRP B CE3 1 
ATOM   1364 C CZ2 . TRP B 1 83 ? 9.488   0.211   -33.548 1.00 39.47  ? 82  TRP B CZ2 1 
ATOM   1365 C CZ3 . TRP B 1 83 ? 11.420  -0.743  -32.449 1.00 38.46  ? 82  TRP B CZ3 1 
ATOM   1366 C CH2 . TRP B 1 83 ? 10.777  0.321   -33.070 1.00 37.91  ? 82  TRP B CH2 1 
ATOM   1367 N N   . GLU B 1 84 ? 11.869  -5.219  -33.012 1.00 25.53  ? 83  GLU B N   1 
ATOM   1368 C CA  . GLU B 1 84 ? 13.183  -4.638  -33.206 1.00 28.43  ? 83  GLU B CA  1 
ATOM   1369 C C   . GLU B 1 84 ? 13.812  -5.132  -34.511 1.00 30.02  ? 83  GLU B C   1 
ATOM   1370 O O   . GLU B 1 84 ? 14.397  -4.329  -35.261 1.00 28.20  ? 83  GLU B O   1 
ATOM   1371 C CB  . GLU B 1 84 ? 14.094  -4.950  -32.029 1.00 27.08  ? 83  GLU B CB  1 
ATOM   1372 C CG  . GLU B 1 84 ? 13.650  -4.207  -30.768 1.00 32.82  ? 83  GLU B CG  1 
ATOM   1373 C CD  . GLU B 1 84 ? 14.502  -4.529  -29.578 1.00 30.92  ? 83  GLU B CD  1 
ATOM   1374 O OE1 . GLU B 1 84 ? 15.394  -5.403  -29.695 1.00 27.72  ? 83  GLU B OE1 1 
ATOM   1375 O OE2 . GLU B 1 84 ? 14.271  -3.910  -28.503 1.00 30.63  ? 83  GLU B OE2 1 
ATOM   1376 N N   . ILE B 1 85 ? 13.699  -6.447  -34.766 1.00 30.15  ? 84  ILE B N   1 
ATOM   1377 C CA  . ILE B 1 85 ? 14.384  -7.021  -35.917 1.00 26.86  ? 84  ILE B CA  1 
ATOM   1378 C C   . ILE B 1 85 ? 13.747  -6.472  -37.198 1.00 28.98  ? 84  ILE B C   1 
ATOM   1379 O O   . ILE B 1 85 ? 14.423  -6.310  -38.216 1.00 25.92  ? 84  ILE B O   1 
ATOM   1380 C CB  . ILE B 1 85 ? 14.423  -8.563  -35.872 1.00 27.84  ? 84  ILE B CB  1 
ATOM   1381 C CG1 . ILE B 1 85 ? 15.480  -9.134  -36.834 1.00 29.14  ? 84  ILE B CG1 1 
ATOM   1382 C CG2 . ILE B 1 85 ? 13.041  -9.171  -36.119 1.00 27.96  ? 84  ILE B CG2 1 
ATOM   1383 C CD1 . ILE B 1 85 ? 15.903  -10.565 -36.528 1.00 27.63  ? 84  ILE B CD1 1 
ATOM   1384 N N   . GLN B 1 86 ? 12.453  -6.160  -37.127 1.00 27.08  ? 85  GLN B N   1 
ATOM   1385 C CA  . GLN B 1 86 ? 11.671  -5.652  -38.246 1.00 30.61  ? 85  GLN B CA  1 
ATOM   1386 C C   . GLN B 1 86 ? 11.875  -4.143  -38.436 1.00 31.62  ? 85  GLN B C   1 
ATOM   1387 O O   . GLN B 1 86 ? 11.983  -3.683  -39.565 1.00 32.77  ? 85  GLN B O   1 
ATOM   1388 C CB  . GLN B 1 86 ? 10.205  -6.023  -38.029 1.00 35.07  ? 85  GLN B CB  1 
ATOM   1389 N N   . ASN B 1 87 ? 12.001  -3.374  -37.352 1.00 28.93  ? 86  ASN B N   1 
ATOM   1390 C CA  . ASN B 1 87 ? 11.855  -1.923  -37.476 1.00 30.99  ? 86  ASN B CA  1 
ATOM   1391 C C   . ASN B 1 87 ? 13.165  -1.180  -37.268 1.00 30.70  ? 86  ASN B C   1 
ATOM   1392 O O   . ASN B 1 87 ? 13.292  -0.037  -37.710 1.00 32.37  ? 86  ASN B O   1 
ATOM   1393 C CB  . ASN B 1 87 ? 10.784  -1.413  -36.500 1.00 33.53  ? 86  ASN B CB  1 
ATOM   1394 C CG  . ASN B 1 87 ? 9.437   -1.910  -36.956 1.00 38.22  ? 86  ASN B CG  1 
ATOM   1395 O OD1 . ASN B 1 87 ? 8.927   -1.409  -37.956 1.00 40.31  ? 86  ASN B OD1 1 
ATOM   1396 N ND2 . ASN B 1 87 ? 8.896   -2.947  -36.327 1.00 38.27  ? 86  ASN B ND2 1 
ATOM   1397 N N   . ASN B 1 88 ? 14.106  -1.770  -36.526 1.00 29.94  ? 87  ASN B N   1 
ATOM   1398 C CA  . ASN B 1 88 ? 15.348  -1.071  -36.253 1.00 31.61  ? 87  ASN B CA  1 
ATOM   1399 C C   . ASN B 1 88 ? 16.422  -2.072  -35.852 1.00 27.71  ? 87  ASN B C   1 
ATOM   1400 O O   . ASN B 1 88 ? 17.016  -1.969  -34.775 1.00 26.64  ? 87  ASN B O   1 
ATOM   1401 C CB  . ASN B 1 88 ? 15.152  0.124   -35.312 1.00 32.50  ? 87  ASN B CB  1 
ATOM   1402 C CG  . ASN B 1 88 ? 16.276  1.135   -35.415 1.00 33.22  ? 87  ASN B CG  1 
ATOM   1403 O OD1 . ASN B 1 88 ? 17.315  0.925   -36.055 1.00 30.64  ? 87  ASN B OD1 1 
ATOM   1404 N ND2 . ASN B 1 88 ? 16.080  2.282   -34.789 1.00 32.82  ? 87  ASN B ND2 1 
ATOM   1405 N N   . PRO B 1 89 ? 16.732  -3.052  -36.740 1.00 27.85  ? 88  PRO B N   1 
ATOM   1406 C CA  . PRO B 1 89 ? 17.676  -4.126  -36.420 1.00 26.19  ? 88  PRO B CA  1 
ATOM   1407 C C   . PRO B 1 89 ? 19.106  -3.696  -36.127 1.00 26.96  ? 88  PRO B C   1 
ATOM   1408 O O   . PRO B 1 89 ? 19.851  -4.434  -35.488 1.00 27.53  ? 88  PRO B O   1 
ATOM   1409 C CB  . PRO B 1 89 ? 17.652  -5.057  -37.662 1.00 23.17  ? 88  PRO B CB  1 
ATOM   1410 C CG  . PRO B 1 89 ? 17.229  -4.143  -38.787 1.00 22.35  ? 88  PRO B CG  1 
ATOM   1411 C CD  . PRO B 1 89 ? 16.233  -3.144  -38.123 1.00 24.87  ? 88  PRO B CD  1 
ATOM   1412 N N   . HIS B 1 90 ? 19.508  -2.503  -36.627 1.00 26.26  ? 89  HIS B N   1 
ATOM   1413 C CA  . HIS B 1 90 ? 20.895  -2.103  -36.524 1.00 26.11  ? 89  HIS B CA  1 
ATOM   1414 C C   . HIS B 1 90 ? 21.129  -1.005  -35.479 1.00 26.08  ? 89  HIS B C   1 
ATOM   1415 O O   . HIS B 1 90 ? 22.254  -0.498  -35.382 1.00 28.83  ? 89  HIS B O   1 
ATOM   1416 C CB  . HIS B 1 90 ? 21.439  -1.695  -37.900 1.00 27.98  ? 89  HIS B CB  1 
ATOM   1417 C CG  . HIS B 1 90 ? 21.257  -2.786  -38.903 1.00 30.58  ? 89  HIS B CG  1 
ATOM   1418 N ND1 . HIS B 1 90 ? 21.891  -4.000  -38.717 1.00 27.45  ? 89  HIS B ND1 1 
ATOM   1419 C CD2 . HIS B 1 90 ? 20.564  -2.877  -40.055 1.00 26.64  ? 89  HIS B CD2 1 
ATOM   1420 C CE1 . HIS B 1 90 ? 21.583  -4.798  -39.734 1.00 27.69  ? 89  HIS B CE1 1 
ATOM   1421 N NE2 . HIS B 1 90 ? 20.813  -4.122  -40.559 1.00 25.96  ? 89  HIS B NE2 1 
ATOM   1422 N N   . ALA B 1 91 ? 20.132  -0.762  -34.618 1.00 27.87  ? 90  ALA B N   1 
ATOM   1423 C CA  . ALA B 1 91 ? 20.202  0.280   -33.595 1.00 29.18  ? 90  ALA B CA  1 
ATOM   1424 C C   . ALA B 1 91 ? 21.138  -0.133  -32.461 1.00 33.86  ? 90  ALA B C   1 
ATOM   1425 O O   . ALA B 1 91 ? 21.383  -1.311  -32.239 1.00 29.80  ? 90  ALA B O   1 
ATOM   1426 C CB  . ALA B 1 91 ? 18.807  0.555   -33.048 1.00 29.49  ? 90  ALA B CB  1 
ATOM   1427 N N   . SER B 1 92 ? 21.625  0.861   -31.706 1.00 33.08  ? 91  SER B N   1 
ATOM   1428 C CA  . SER B 1 92 ? 22.268  0.644   -30.427 1.00 36.07  ? 91  SER B CA  1 
ATOM   1429 C C   . SER B 1 92 ? 21.176  0.395   -29.379 1.00 40.67  ? 91  SER B C   1 
ATOM   1430 O O   . SER B 1 92 ? 20.259  1.205   -29.232 1.00 41.89  ? 91  SER B O   1 
ATOM   1431 C CB  . SER B 1 92 ? 23.108  1.878   -30.084 1.00 36.64  ? 91  SER B CB  1 
ATOM   1432 O OG  . SER B 1 92 ? 23.645  1.745   -28.780 1.00 51.54  ? 91  SER B OG  1 
ATOM   1433 N N   . TYR B 1 93 ? 21.251  -0.764  -28.709 1.00 34.84  ? 92  TYR B N   1 
ATOM   1434 C CA  . TYR B 1 93 ? 20.373  -1.169  -27.625 1.00 40.27  ? 92  TYR B CA  1 
ATOM   1435 C C   . TYR B 1 93 ? 21.189  -1.182  -26.336 1.00 47.32  ? 92  TYR B C   1 
ATOM   1436 O O   . TYR B 1 93 ? 20.768  -1.751  -25.334 1.00 51.65  ? 92  TYR B O   1 
ATOM   1437 C CB  . TYR B 1 93 ? 19.775  -2.542  -27.957 1.00 35.73  ? 92  TYR B CB  1 
ATOM   1438 C CG  . TYR B 1 93 ? 18.787  -2.420  -29.105 1.00 35.02  ? 92  TYR B CG  1 
ATOM   1439 C CD1 . TYR B 1 93 ? 17.518  -1.906  -28.880 1.00 31.12  ? 92  TYR B CD1 1 
ATOM   1440 C CD2 . TYR B 1 93 ? 19.117  -2.819  -30.403 1.00 29.00  ? 92  TYR B CD2 1 
ATOM   1441 C CE1 . TYR B 1 93 ? 16.605  -1.751  -29.907 1.00 31.63  ? 92  TYR B CE1 1 
ATOM   1442 C CE2 . TYR B 1 93 ? 18.192  -2.704  -31.428 1.00 29.35  ? 92  TYR B CE2 1 
ATOM   1443 C CZ  . TYR B 1 93 ? 16.947  -2.146  -31.193 1.00 29.83  ? 92  TYR B CZ  1 
ATOM   1444 O OH  . TYR B 1 93 ? 16.002  -2.019  -32.186 1.00 28.51  ? 92  TYR B OH  1 
ATOM   1445 N N   . SER B 1 94 ? 22.347  -0.511  -26.398 1.00 67.11  ? 93  SER B N   1 
ATOM   1446 C CA  . SER B 1 94 ? 23.340  -0.425  -25.337 1.00 79.71  ? 93  SER B CA  1 
ATOM   1447 C C   . SER B 1 94 ? 22.657  -0.228  -23.976 1.00 91.52  ? 93  SER B C   1 
ATOM   1448 O O   . SER B 1 94 ? 21.675  0.559   -23.927 1.00 93.16  ? 93  SER B O   1 
ATOM   1449 C CB  . SER B 1 94 ? 24.332  0.688   -25.613 1.00 82.31  ? 93  SER B CB  1 
ATOM   1450 O OG  . SER B 1 94 ? 25.105  0.434   -26.779 1.00 76.63  ? 93  SER B OG  1 
ATOM   1451 O OXT . SER B 1 94 ? 23.129  -0.869  -23.011 1.00 101.42 ? 93  SER B OXT 1 
ATOM   1452 N N   . ALA C 1 5  ? 30.022  -22.786 29.061  1.00 64.30  ? 4   ALA C N   1 
ATOM   1453 C CA  . ALA C 1 5  ? 29.050  -23.502 29.926  1.00 64.38  ? 4   ALA C CA  1 
ATOM   1454 C C   . ALA C 1 5  ? 27.613  -23.113 29.583  1.00 73.63  ? 4   ALA C C   1 
ATOM   1455 O O   . ALA C 1 5  ? 27.382  -22.134 28.869  1.00 74.10  ? 4   ALA C O   1 
ATOM   1456 C CB  . ALA C 1 5  ? 29.348  -23.194 31.363  1.00 76.04  ? 4   ALA C CB  1 
ATOM   1457 N N   . PHE C 1 6  ? 26.654  -23.859 30.157  1.00 62.33  ? 5   PHE C N   1 
ATOM   1458 C CA  . PHE C 1 6  ? 25.289  -23.877 29.664  1.00 60.69  ? 5   PHE C CA  1 
ATOM   1459 C C   . PHE C 1 6  ? 24.322  -24.053 30.834  1.00 67.75  ? 5   PHE C C   1 
ATOM   1460 O O   . PHE C 1 6  ? 24.395  -25.053 31.544  1.00 78.72  ? 5   PHE C O   1 
ATOM   1461 C CB  . PHE C 1 6  ? 25.161  -25.071 28.701  1.00 50.91  ? 5   PHE C CB  1 
ATOM   1462 C CG  . PHE C 1 6  ? 26.031  -25.111 27.442  1.00 49.06  ? 5   PHE C CG  1 
ATOM   1463 C CD1 . PHE C 1 6  ? 27.128  -25.960 27.348  1.00 47.18  ? 5   PHE C CD1 1 
ATOM   1464 C CD2 . PHE C 1 6  ? 25.745  -24.312 26.331  1.00 53.65  ? 5   PHE C CD2 1 
ATOM   1465 C CE1 . PHE C 1 6  ? 27.909  -26.014 26.189  1.00 54.26  ? 5   PHE C CE1 1 
ATOM   1466 C CE2 . PHE C 1 6  ? 26.520  -24.377 25.170  1.00 47.30  ? 5   PHE C CE2 1 
ATOM   1467 C CZ  . PHE C 1 6  ? 27.604  -25.220 25.101  1.00 54.32  ? 5   PHE C CZ  1 
ATOM   1468 N N   . LYS C 1 7  ? 23.402  -23.095 31.012  1.00 62.16  ? 6   LYS C N   1 
ATOM   1469 C CA  . LYS C 1 7  ? 22.389  -23.177 32.057  1.00 63.00  ? 6   LYS C CA  1 
ATOM   1470 C C   . LYS C 1 7  ? 21.086  -23.624 31.401  1.00 58.97  ? 6   LYS C C   1 
ATOM   1471 O O   . LYS C 1 7  ? 20.970  -23.548 30.178  1.00 65.11  ? 6   LYS C O   1 
ATOM   1472 C CB  . LYS C 1 7  ? 22.243  -21.834 32.789  1.00 66.12  ? 6   LYS C CB  1 
ATOM   1473 N N   . PRO C 1 8  ? 20.065  -24.114 32.145  1.00 57.29  ? 7   PRO C N   1 
ATOM   1474 C CA  . PRO C 1 8  ? 18.775  -24.437 31.527  1.00 61.45  ? 7   PRO C CA  1 
ATOM   1475 C C   . PRO C 1 8  ? 18.260  -23.246 30.713  1.00 70.64  ? 7   PRO C C   1 
ATOM   1476 O O   . PRO C 1 8  ? 18.619  -22.096 30.991  1.00 72.77  ? 7   PRO C O   1 
ATOM   1477 C CB  . PRO C 1 8  ? 17.860  -24.828 32.698  1.00 60.68  ? 7   PRO C CB  1 
ATOM   1478 C CG  . PRO C 1 8  ? 18.834  -25.285 33.760  1.00 57.96  ? 7   PRO C CG  1 
ATOM   1479 C CD  . PRO C 1 8  ? 20.095  -24.435 33.584  1.00 57.40  ? 7   PRO C CD  1 
ATOM   1480 N N   . GLY C 1 9  ? 17.481  -23.548 29.663  1.00 65.23  ? 8   GLY C N   1 
ATOM   1481 C CA  . GLY C 1 9  ? 16.869  -22.536 28.815  1.00 62.24  ? 8   GLY C CA  1 
ATOM   1482 C C   . GLY C 1 9  ? 17.757  -22.086 27.651  1.00 56.51  ? 8   GLY C C   1 
ATOM   1483 O O   . GLY C 1 9  ? 17.216  -21.606 26.658  1.00 63.19  ? 8   GLY C O   1 
ATOM   1484 N N   . ASP C 1 10 ? 19.093  -22.220 27.789  1.00 47.50  ? 9   ASP C N   1 
ATOM   1485 C CA  . ASP C 1 10 ? 20.092  -21.873 26.787  1.00 44.97  ? 9   ASP C CA  1 
ATOM   1486 C C   . ASP C 1 10 ? 19.833  -22.625 25.482  1.00 46.00  ? 9   ASP C C   1 
ATOM   1487 O O   . ASP C 1 10 ? 19.511  -23.803 25.491  1.00 40.77  ? 9   ASP C O   1 
ATOM   1488 C CB  . ASP C 1 10 ? 21.514  -22.192 27.226  1.00 46.54  ? 9   ASP C CB  1 
ATOM   1489 C CG  . ASP C 1 10 ? 22.219  -21.179 28.128  1.00 59.28  ? 9   ASP C CG  1 
ATOM   1490 O OD1 . ASP C 1 10 ? 21.572  -20.182 28.509  1.00 65.21  ? 9   ASP C OD1 1 
ATOM   1491 O OD2 . ASP C 1 10 ? 23.422  -21.383 28.446  1.00 56.93  ? 9   ASP C OD2 1 
ATOM   1492 N N   . LEU C 1 11 ? 19.977  -21.915 24.358  1.00 45.23  ? 10  LEU C N   1 
ATOM   1493 C CA  . LEU C 1 11 ? 19.562  -22.431 23.062  1.00 39.68  ? 10  LEU C CA  1 
ATOM   1494 C C   . LEU C 1 11 ? 20.811  -22.873 22.326  1.00 34.91  ? 10  LEU C C   1 
ATOM   1495 O O   . LEU C 1 11 ? 21.804  -22.165 22.322  1.00 34.03  ? 10  LEU C O   1 
ATOM   1496 C CB  . LEU C 1 11 ? 18.783  -21.375 22.272  1.00 38.89  ? 10  LEU C CB  1 
ATOM   1497 C CG  . LEU C 1 11 ? 17.474  -20.885 22.896  1.00 38.32  ? 10  LEU C CG  1 
ATOM   1498 C CD1 . LEU C 1 11 ? 16.894  -19.848 21.950  1.00 43.75  ? 10  LEU C CD1 1 
ATOM   1499 C CD2 . LEU C 1 11 ? 16.438  -21.971 23.174  1.00 44.82  ? 10  LEU C CD2 1 
ATOM   1500 N N   . VAL C 1 12 ? 20.766  -24.078 21.746  1.00 32.76  ? 11  VAL C N   1 
ATOM   1501 C CA  . VAL C 1 12 ? 21.946  -24.672 21.162  1.00 29.79  ? 11  VAL C CA  1 
ATOM   1502 C C   . VAL C 1 12 ? 21.542  -25.432 19.886  1.00 28.11  ? 11  VAL C C   1 
ATOM   1503 O O   . VAL C 1 12 ? 20.357  -25.649 19.640  1.00 28.72  ? 11  VAL C O   1 
ATOM   1504 C CB  . VAL C 1 12 ? 22.543  -25.671 22.182  1.00 33.86  ? 11  VAL C CB  1 
ATOM   1505 C CG1 . VAL C 1 12 ? 22.963  -25.011 23.505  1.00 31.53  ? 11  VAL C CG1 1 
ATOM   1506 C CG2 . VAL C 1 12 ? 21.600  -26.852 22.429  1.00 28.54  ? 11  VAL C CG2 1 
ATOM   1507 N N   . PHE C 1 13 ? 22.556  -25.848 19.108  1.00 28.56  ? 12  PHE C N   1 
ATOM   1508 C CA  . PHE C 1 13 ? 22.477  -27.018 18.245  1.00 27.58  ? 12  PHE C CA  1 
ATOM   1509 C C   . PHE C 1 13 ? 23.202  -28.164 18.941  1.00 27.67  ? 12  PHE C C   1 
ATOM   1510 O O   . PHE C 1 13 ? 24.311  -27.996 19.475  1.00 31.34  ? 12  PHE C O   1 
ATOM   1511 C CB  . PHE C 1 13 ? 23.091  -26.803 16.854  1.00 30.75  ? 12  PHE C CB  1 
ATOM   1512 C CG  . PHE C 1 13 ? 22.323  -25.798 16.018  1.00 33.11  ? 12  PHE C CG  1 
ATOM   1513 C CD1 . PHE C 1 13 ? 21.299  -26.215 15.171  1.00 31.67  ? 12  PHE C CD1 1 
ATOM   1514 C CD2 . PHE C 1 13 ? 22.606  -24.430 16.106  1.00 34.32  ? 12  PHE C CD2 1 
ATOM   1515 C CE1 . PHE C 1 13 ? 20.586  -25.286 14.421  1.00 32.24  ? 12  PHE C CE1 1 
ATOM   1516 C CE2 . PHE C 1 13 ? 21.880  -23.513 15.361  1.00 39.02  ? 12  PHE C CE2 1 
ATOM   1517 C CZ  . PHE C 1 13 ? 20.880  -23.944 14.513  1.00 36.40  ? 12  PHE C CZ  1 
ATOM   1518 N N   . ALA C 1 14 ? 22.552  -29.337 18.926  1.00 28.13  ? 13  ALA C N   1 
ATOM   1519 C CA  . ALA C 1 14 ? 23.034  -30.495 19.657  1.00 25.49  ? 13  ALA C CA  1 
ATOM   1520 C C   . ALA C 1 14 ? 23.280  -31.638 18.680  1.00 30.44  ? 13  ALA C C   1 
ATOM   1521 O O   . ALA C 1 14 ? 22.407  -31.970 17.878  1.00 25.40  ? 13  ALA C O   1 
ATOM   1522 C CB  . ALA C 1 14 ? 21.998  -30.916 20.679  1.00 27.20  ? 13  ALA C CB  1 
ATOM   1523 N N   . LYS C 1 15 ? 24.447  -32.267 18.800  1.00 29.50  ? 14  LYS C N   1 
ATOM   1524 C CA  . LYS C 1 15 ? 24.874  -33.247 17.813  1.00 31.75  ? 14  LYS C CA  1 
ATOM   1525 C C   . LYS C 1 15 ? 24.869  -34.627 18.454  1.00 30.97  ? 14  LYS C C   1 
ATOM   1526 O O   . LYS C 1 15 ? 25.582  -34.861 19.429  1.00 31.31  ? 14  LYS C O   1 
ATOM   1527 C CB  . LYS C 1 15 ? 26.294  -32.969 17.292  1.00 34.09  ? 14  LYS C CB  1 
ATOM   1528 C CG  . LYS C 1 15 ? 26.746  -33.961 16.194  1.00 34.93  ? 14  LYS C CG  1 
ATOM   1529 C CD  . LYS C 1 15 ? 25.883  -33.894 14.926  1.00 30.09  ? 14  LYS C CD  1 
ATOM   1530 C CE  . LYS C 1 15 ? 26.416  -34.804 13.792  1.00 30.94  ? 14  LYS C CE  1 
ATOM   1531 N NZ  . LYS C 1 15 ? 26.273  -36.228 14.172  1.00 28.46  ? 14  LYS C NZ  1 
ATOM   1532 N N   . MET C 1 16 ? 24.069  -35.531 17.884  1.00 28.26  ? 15  MET C N   1 
ATOM   1533 C CA  . MET C 1 16 ? 24.070  -36.945 18.252  1.00 29.68  ? 15  MET C CA  1 
ATOM   1534 C C   . MET C 1 16 ? 24.559  -37.748 17.055  1.00 32.94  ? 15  MET C C   1 
ATOM   1535 O O   . MET C 1 16 ? 24.324  -37.375 15.900  1.00 28.70  ? 15  MET C O   1 
ATOM   1536 C CB  . MET C 1 16 ? 22.648  -37.440 18.566  1.00 28.99  ? 15  MET C CB  1 
ATOM   1537 C CG  . MET C 1 16 ? 22.061  -36.855 19.840  1.00 33.42  ? 15  MET C CG  1 
ATOM   1538 S SD  . MET C 1 16 ? 20.441  -37.545 20.228  1.00 39.03  ? 15  MET C SD  1 
ATOM   1539 C CE  . MET C 1 16 ? 19.461  -36.959 18.832  1.00 36.82  ? 15  MET C CE  1 
ATOM   1540 N N   . LYS C 1 17 ? 25.186  -38.888 17.343  1.00 34.85  ? 16  LYS C N   1 
ATOM   1541 C CA  . LYS C 1 17 ? 25.640  -39.759 16.272  1.00 35.87  ? 16  LYS C CA  1 
ATOM   1542 C C   . LYS C 1 17 ? 24.402  -40.213 15.506  1.00 29.06  ? 16  LYS C C   1 
ATOM   1543 O O   . LYS C 1 17 ? 23.446  -40.723 16.092  1.00 31.44  ? 16  LYS C O   1 
ATOM   1544 C CB  . LYS C 1 17 ? 26.356  -40.990 16.855  1.00 34.36  ? 16  LYS C CB  1 
ATOM   1545 C CG  . LYS C 1 17 ? 26.997  -41.964 15.864  1.00 38.02  ? 16  LYS C CG  1 
ATOM   1546 C CD  . LYS C 1 17 ? 28.172  -41.292 15.166  1.00 38.68  ? 16  LYS C CD  1 
ATOM   1547 C CE  . LYS C 1 17 ? 28.944  -42.208 14.252  1.00 48.28  ? 16  LYS C CE  1 
ATOM   1548 N NZ  . LYS C 1 17 ? 30.099  -41.494 13.700  1.00 44.16  ? 16  LYS C NZ  1 
ATOM   1549 N N   . GLY C 1 18 ? 24.444  -40.041 14.190  1.00 31.08  ? 17  GLY C N   1 
ATOM   1550 C CA  . GLY C 1 18 ? 23.344  -40.537 13.376  1.00 29.90  ? 17  GLY C CA  1 
ATOM   1551 C C   . GLY C 1 18 ? 22.356  -39.436 12.976  1.00 32.52  ? 17  GLY C C   1 
ATOM   1552 O O   . GLY C 1 18 ? 21.364  -39.726 12.323  1.00 34.00  ? 17  GLY C O   1 
ATOM   1553 N N   . TYR C 1 19 ? 22.605  -38.186 13.399  1.00 32.28  ? 18  TYR C N   1 
ATOM   1554 C CA  . TYR C 1 19 ? 21.645  -37.098 13.202  1.00 30.69  ? 18  TYR C CA  1 
ATOM   1555 C C   . TYR C 1 19 ? 22.413  -35.826 12.907  1.00 27.75  ? 18  TYR C C   1 
ATOM   1556 O O   . TYR C 1 19 ? 23.509  -35.630 13.416  1.00 28.55  ? 18  TYR C O   1 
ATOM   1557 C CB  . TYR C 1 19 ? 20.859  -36.793 14.482  1.00 29.02  ? 18  TYR C CB  1 
ATOM   1558 C CG  . TYR C 1 19 ? 19.994  -37.970 14.874  1.00 28.36  ? 18  TYR C CG  1 
ATOM   1559 C CD1 . TYR C 1 19 ? 20.498  -39.007 15.658  1.00 28.35  ? 18  TYR C CD1 1 
ATOM   1560 C CD2 . TYR C 1 19 ? 18.709  -38.093 14.367  1.00 32.50  ? 18  TYR C CD2 1 
ATOM   1561 C CE1 . TYR C 1 19 ? 19.725  -40.107 15.964  1.00 31.81  ? 18  TYR C CE1 1 
ATOM   1562 C CE2 . TYR C 1 19 ? 17.920  -39.187 14.681  1.00 37.98  ? 18  TYR C CE2 1 
ATOM   1563 C CZ  . TYR C 1 19 ? 18.439  -40.199 15.466  1.00 37.54  ? 18  TYR C CZ  1 
ATOM   1564 O OH  . TYR C 1 19 ? 17.641  -41.266 15.759  1.00 41.04  ? 18  TYR C OH  1 
ATOM   1565 N N   . PRO C 1 20 ? 21.881  -34.913 12.072  1.00 28.51  ? 19  PRO C N   1 
ATOM   1566 C CA  . PRO C 1 20 ? 22.534  -33.620 11.877  1.00 27.64  ? 19  PRO C CA  1 
ATOM   1567 C C   . PRO C 1 20 ? 22.468  -32.783 13.161  1.00 27.35  ? 19  PRO C C   1 
ATOM   1568 O O   . PRO C 1 20 ? 21.739  -33.117 14.092  1.00 26.85  ? 19  PRO C O   1 
ATOM   1569 C CB  . PRO C 1 20 ? 21.665  -33.042 10.744  1.00 29.13  ? 19  PRO C CB  1 
ATOM   1570 C CG  . PRO C 1 20 ? 20.285  -33.578 11.046  1.00 29.41  ? 19  PRO C CG  1 
ATOM   1571 C CD  . PRO C 1 20 ? 20.586  -35.039 11.371  1.00 27.85  ? 19  PRO C CD  1 
ATOM   1572 N N   . HIS C 1 21 ? 23.292  -31.737 13.217  1.00 26.92  ? 20  HIS C N   1 
ATOM   1573 C CA  . HIS C 1 21 ? 23.271  -30.799 14.334  1.00 29.08  ? 20  HIS C CA  1 
ATOM   1574 C C   . HIS C 1 21 ? 21.844  -30.273 14.462  1.00 27.46  ? 20  HIS C C   1 
ATOM   1575 O O   . HIS C 1 21 ? 21.278  -29.822 13.460  1.00 30.11  ? 20  HIS C O   1 
ATOM   1576 C CB  . HIS C 1 21 ? 24.245  -29.643 14.081  1.00 30.16  ? 20  HIS C CB  1 
ATOM   1577 C CG  . HIS C 1 21 ? 25.681  -30.075 14.107  1.00 32.74  ? 20  HIS C CG  1 
ATOM   1578 N ND1 . HIS C 1 21 ? 26.309  -30.751 13.084  1.00 34.43  ? 20  HIS C ND1 1 
ATOM   1579 C CD2 . HIS C 1 21 ? 26.590  -29.966 15.097  1.00 35.96  ? 20  HIS C CD2 1 
ATOM   1580 C CE1 . HIS C 1 21 ? 27.562  -31.011 13.438  1.00 36.92  ? 20  HIS C CE1 1 
ATOM   1581 N NE2 . HIS C 1 21 ? 27.755  -30.532 14.653  1.00 34.20  ? 20  HIS C NE2 1 
ATOM   1582 N N   . TRP C 1 22 ? 21.241  -30.431 15.653  1.00 25.19  ? 21  TRP C N   1 
ATOM   1583 C CA  . TRP C 1 22 ? 19.790  -30.334 15.778  1.00 24.13  ? 21  TRP C CA  1 
ATOM   1584 C C   . TRP C 1 22 ? 19.448  -29.150 16.674  1.00 24.40  ? 21  TRP C C   1 
ATOM   1585 O O   . TRP C 1 22 ? 20.033  -29.016 17.751  1.00 25.18  ? 21  TRP C O   1 
ATOM   1586 C CB  . TRP C 1 22 ? 19.181  -31.618 16.380  1.00 25.77  ? 21  TRP C CB  1 
ATOM   1587 C CG  . TRP C 1 22 ? 17.732  -31.838 16.003  1.00 27.94  ? 21  TRP C CG  1 
ATOM   1588 C CD1 . TRP C 1 22 ? 16.621  -31.271 16.574  1.00 26.24  ? 21  TRP C CD1 1 
ATOM   1589 C CD2 . TRP C 1 22 ? 17.243  -32.737 14.975  1.00 27.77  ? 21  TRP C CD2 1 
ATOM   1590 N NE1 . TRP C 1 22 ? 15.484  -31.725 15.944  1.00 27.85  ? 21  TRP C NE1 1 
ATOM   1591 C CE2 . TRP C 1 22 ? 15.832  -32.635 14.975  1.00 26.96  ? 21  TRP C CE2 1 
ATOM   1592 C CE3 . TRP C 1 22 ? 17.854  -33.620 14.069  1.00 24.55  ? 21  TRP C CE3 1 
ATOM   1593 C CZ2 . TRP C 1 22 ? 15.045  -33.366 14.075  1.00 27.91  ? 21  TRP C CZ2 1 
ATOM   1594 C CZ3 . TRP C 1 22 ? 17.075  -34.343 13.183  1.00 25.70  ? 21  TRP C CZ3 1 
ATOM   1595 C CH2 . TRP C 1 22 ? 15.681  -34.246 13.220  1.00 26.09  ? 21  TRP C CH2 1 
ATOM   1596 N N   . PRO C 1 23 ? 18.457  -28.302 16.314  1.00 26.93  ? 22  PRO C N   1 
ATOM   1597 C CA  . PRO C 1 23 ? 18.048  -27.217 17.204  1.00 26.14  ? 22  PRO C CA  1 
ATOM   1598 C C   . PRO C 1 23 ? 17.437  -27.771 18.491  1.00 24.35  ? 22  PRO C C   1 
ATOM   1599 O O   . PRO C 1 23 ? 16.593  -28.677 18.479  1.00 26.21  ? 22  PRO C O   1 
ATOM   1600 C CB  . PRO C 1 23 ? 17.043  -26.441 16.317  1.00 27.12  ? 22  PRO C CB  1 
ATOM   1601 C CG  . PRO C 1 23 ? 16.449  -27.526 15.432  1.00 27.27  ? 22  PRO C CG  1 
ATOM   1602 C CD  . PRO C 1 23 ? 17.710  -28.289 15.029  1.00 26.20  ? 22  PRO C CD  1 
ATOM   1603 N N   . ALA C 1 24 ? 17.887  -27.209 19.612  1.00 27.12  ? 23  ALA C N   1 
ATOM   1604 C CA  . ALA C 1 24 ? 17.574  -27.757 20.928  1.00 32.62  ? 23  ALA C CA  1 
ATOM   1605 C C   . ALA C 1 24 ? 17.774  -26.696 22.012  1.00 33.57  ? 23  ALA C C   1 
ATOM   1606 O O   . ALA C 1 24 ? 18.331  -25.620 21.781  1.00 31.70  ? 23  ALA C O   1 
ATOM   1607 C CB  . ALA C 1 24 ? 18.492  -28.953 21.216  1.00 29.68  ? 23  ALA C CB  1 
ATOM   1608 N N   . ARG C 1 25 ? 17.410  -27.063 23.241  1.00 37.70  ? 24  ARG C N   1 
ATOM   1609 C CA  . ARG C 1 25 ? 17.838  -26.255 24.371  1.00 36.66  ? 24  ARG C CA  1 
ATOM   1610 C C   . ARG C 1 25 ? 18.239  -27.168 25.534  1.00 36.65  ? 24  ARG C C   1 
ATOM   1611 O O   . ARG C 1 25 ? 17.820  -28.329 25.593  1.00 34.84  ? 24  ARG C O   1 
ATOM   1612 C CB  . ARG C 1 25 ? 16.635  -25.418 24.809  1.00 37.41  ? 24  ARG C CB  1 
ATOM   1613 C CG  . ARG C 1 25 ? 15.416  -26.187 25.280  1.00 39.01  ? 24  ARG C CG  1 
ATOM   1614 C CD  . ARG C 1 25 ? 14.418  -25.212 25.906  1.00 41.27  ? 24  ARG C CD  1 
ATOM   1615 N NE  . ARG C 1 25 ? 13.280  -26.059 26.274  1.00 48.02  ? 24  ARG C NE  1 
ATOM   1616 C CZ  . ARG C 1 25 ? 11.989  -25.922 26.005  1.00 54.56  ? 24  ARG C CZ  1 
ATOM   1617 N NH1 . ARG C 1 25 ? 11.532  -24.862 25.349  1.00 53.60  ? 24  ARG C NH1 1 
ATOM   1618 N NH2 . ARG C 1 25 ? 11.150  -26.859 26.423  1.00 50.51  ? 24  ARG C NH2 1 
ATOM   1619 N N   . ILE C 1 26 ? 18.977  -26.566 26.469  1.00 36.59  ? 25  ILE C N   1 
ATOM   1620 C CA  . ILE C 1 26 ? 19.376  -27.136 27.749  1.00 42.61  ? 25  ILE C CA  1 
ATOM   1621 C C   . ILE C 1 26 ? 18.154  -27.148 28.661  1.00 51.37  ? 25  ILE C C   1 
ATOM   1622 O O   . ILE C 1 26 ? 17.539  -26.110 28.907  1.00 51.56  ? 25  ILE C O   1 
ATOM   1623 C CB  . ILE C 1 26 ? 20.499  -26.283 28.367  1.00 43.40  ? 25  ILE C CB  1 
ATOM   1624 C CG1 . ILE C 1 26 ? 21.566  -25.917 27.358  1.00 50.36  ? 25  ILE C CG1 1 
ATOM   1625 C CG2 . ILE C 1 26 ? 21.094  -26.934 29.621  1.00 46.18  ? 25  ILE C CG2 1 
ATOM   1626 C CD1 . ILE C 1 26 ? 22.668  -26.938 27.153  1.00 42.76  ? 25  ILE C CD1 1 
ATOM   1627 N N   . ASP C 1 27 ? 17.804  -28.336 29.146  1.00 50.76  ? 26  ASP C N   1 
ATOM   1628 C CA  . ASP C 1 27 ? 16.767  -28.475 30.155  1.00 57.86  ? 26  ASP C CA  1 
ATOM   1629 C C   . ASP C 1 27 ? 17.303  -28.097 31.541  1.00 58.39  ? 26  ASP C C   1 
ATOM   1630 O O   . ASP C 1 27 ? 18.390  -28.604 31.884  1.00 60.99  ? 26  ASP C O   1 
ATOM   1631 C CB  . ASP C 1 27 ? 16.140  -29.855 30.110  1.00 55.71  ? 26  ASP C CB  1 
ATOM   1632 C CG  . ASP C 1 27 ? 14.877  -29.911 29.276  1.00 59.48  ? 26  ASP C CG  1 
ATOM   1633 O OD1 . ASP C 1 27 ? 14.635  -28.906 28.575  1.00 56.66  ? 26  ASP C OD1 1 
ATOM   1634 O OD2 . ASP C 1 27 ? 14.124  -30.913 29.401  1.00 56.97  ? 26  ASP C OD2 1 
ATOM   1635 N N   . LYS C 1 35 ? 19.373  -38.475 37.574  1.00 63.79  ? 34  LYS C N   1 
ATOM   1636 C CA  . LYS C 1 35 ? 20.551  -37.572 37.455  1.00 62.43  ? 34  LYS C CA  1 
ATOM   1637 C C   . LYS C 1 35 ? 21.285  -37.899 36.152  1.00 56.94  ? 34  LYS C C   1 
ATOM   1638 O O   . LYS C 1 35 ? 21.340  -39.058 35.739  1.00 52.37  ? 34  LYS C O   1 
ATOM   1639 C CB  . LYS C 1 35 ? 21.426  -37.655 38.715  1.00 60.78  ? 34  LYS C CB  1 
ATOM   1640 N N   . PRO C 1 36 ? 21.866  -36.901 35.445  1.00 52.55  ? 35  PRO C N   1 
ATOM   1641 C CA  . PRO C 1 36 ? 22.584  -37.189 34.202  1.00 52.66  ? 35  PRO C CA  1 
ATOM   1642 C C   . PRO C 1 36 ? 23.721  -38.172 34.482  1.00 56.34  ? 35  PRO C C   1 
ATOM   1643 O O   . PRO C 1 36 ? 24.162  -38.351 35.623  1.00 46.33  ? 35  PRO C O   1 
ATOM   1644 C CB  . PRO C 1 36 ? 23.108  -35.806 33.746  1.00 54.61  ? 35  PRO C CB  1 
ATOM   1645 C CG  . PRO C 1 36 ? 22.267  -34.797 34.505  1.00 51.96  ? 35  PRO C CG  1 
ATOM   1646 C CD  . PRO C 1 36 ? 21.893  -35.473 35.818  1.00 52.40  ? 35  PRO C CD  1 
ATOM   1647 N N   . PRO C 1 37 ? 24.247  -38.866 33.454  1.00 55.72  ? 36  PRO C N   1 
ATOM   1648 C CA  . PRO C 1 37 ? 25.585  -39.446 33.577  1.00 49.37  ? 36  PRO C CA  1 
ATOM   1649 C C   . PRO C 1 37 ? 26.547  -38.287 33.842  1.00 50.27  ? 36  PRO C C   1 
ATOM   1650 O O   . PRO C 1 37 ? 26.223  -37.135 33.538  1.00 42.28  ? 36  PRO C O   1 
ATOM   1651 C CB  . PRO C 1 37 ? 25.795  -40.099 32.199  1.00 45.31  ? 36  PRO C CB  1 
ATOM   1652 C CG  . PRO C 1 37 ? 24.384  -40.369 31.722  1.00 42.54  ? 36  PRO C CG  1 
ATOM   1653 C CD  . PRO C 1 37 ? 23.577  -39.170 32.181  1.00 49.99  ? 36  PRO C CD  1 
ATOM   1654 N N   . PRO C 1 38 ? 27.743  -38.549 34.427  1.00 49.32  ? 37  PRO C N   1 
ATOM   1655 C CA  . PRO C 1 38 ? 28.716  -37.495 34.723  1.00 49.09  ? 37  PRO C CA  1 
ATOM   1656 C C   . PRO C 1 38 ? 29.032  -36.592 33.535  1.00 44.10  ? 37  PRO C C   1 
ATOM   1657 O O   . PRO C 1 38 ? 29.317  -37.093 32.448  1.00 37.38  ? 37  PRO C O   1 
ATOM   1658 C CB  . PRO C 1 38 ? 29.959  -38.322 35.157  1.00 47.71  ? 37  PRO C CB  1 
ATOM   1659 C CG  . PRO C 1 38 ? 29.360  -39.562 35.770  1.00 47.96  ? 37  PRO C CG  1 
ATOM   1660 C CD  . PRO C 1 38 ? 28.216  -39.884 34.833  1.00 50.44  ? 37  PRO C CD  1 
ATOM   1661 N N   . ASN C 1 39 ? 28.948  -35.272 33.767  1.00 38.93  ? 38  ASN C N   1 
ATOM   1662 C CA  . ASN C 1 39 ? 29.333  -34.235 32.824  1.00 37.61  ? 38  ASN C CA  1 
ATOM   1663 C C   . ASN C 1 39 ? 28.414  -34.228 31.596  1.00 40.97  ? 38  ASN C C   1 
ATOM   1664 O O   . ASN C 1 39 ? 28.859  -33.828 30.513  1.00 43.51  ? 38  ASN C O   1 
ATOM   1665 C CB  . ASN C 1 39 ? 30.805  -34.345 32.421  1.00 40.65  ? 38  ASN C CB  1 
ATOM   1666 C CG  . ASN C 1 39 ? 31.347  -33.098 31.754  1.00 50.08  ? 38  ASN C CG  1 
ATOM   1667 O OD1 . ASN C 1 39 ? 30.862  -31.984 31.998  1.00 56.88  ? 38  ASN C OD1 1 
ATOM   1668 N ND2 . ASN C 1 39 ? 32.359  -33.258 30.909  1.00 50.07  ? 38  ASN C ND2 1 
ATOM   1669 N N   . LYS C 1 40 ? 27.148  -34.653 31.749  1.00 34.82  ? 39  LYS C N   1 
ATOM   1670 C CA  . LYS C 1 40 ? 26.210  -34.564 30.630  1.00 34.23  ? 39  LYS C CA  1 
ATOM   1671 C C   . LYS C 1 40 ? 25.067  -33.615 30.969  1.00 37.70  ? 39  LYS C C   1 
ATOM   1672 O O   . LYS C 1 40 ? 24.617  -33.571 32.103  1.00 39.86  ? 39  LYS C O   1 
ATOM   1673 C CB  . LYS C 1 40 ? 25.483  -35.883 30.335  1.00 32.64  ? 39  LYS C CB  1 
ATOM   1674 C CG  . LYS C 1 40 ? 26.346  -37.102 30.107  1.00 36.47  ? 39  LYS C CG  1 
ATOM   1675 C CD  . LYS C 1 40 ? 27.177  -36.969 28.844  1.00 40.59  ? 39  LYS C CD  1 
ATOM   1676 C CE  . LYS C 1 40 ? 28.030  -38.187 28.592  1.00 48.14  ? 39  LYS C CE  1 
ATOM   1677 N NZ  . LYS C 1 40 ? 29.058  -37.860 27.595  1.00 52.53  ? 39  LYS C NZ  1 
ATOM   1678 N N   . TYR C 1 41 ? 24.549  -32.904 29.958  1.00 35.75  ? 40  TYR C N   1 
ATOM   1679 C CA  . TYR C 1 41 ? 23.402  -32.023 30.150  1.00 32.68  ? 40  TYR C CA  1 
ATOM   1680 C C   . TYR C 1 41 ? 22.146  -32.677 29.596  1.00 33.07  ? 40  TYR C C   1 
ATOM   1681 O O   . TYR C 1 41 ? 22.203  -33.469 28.643  1.00 33.45  ? 40  TYR C O   1 
ATOM   1682 C CB  . TYR C 1 41 ? 23.514  -30.781 29.258  1.00 33.80  ? 40  TYR C CB  1 
ATOM   1683 C CG  . TYR C 1 41 ? 24.688  -29.910 29.661  1.00 34.50  ? 40  TYR C CG  1 
ATOM   1684 C CD1 . TYR C 1 41 ? 25.977  -30.156 29.189  1.00 36.30  ? 40  TYR C CD1 1 
ATOM   1685 C CD2 . TYR C 1 41 ? 24.493  -28.828 30.506  1.00 36.40  ? 40  TYR C CD2 1 
ATOM   1686 C CE1 . TYR C 1 41 ? 27.046  -29.365 29.574  1.00 41.39  ? 40  TYR C CE1 1 
ATOM   1687 C CE2 . TYR C 1 41 ? 25.551  -28.012 30.868  1.00 36.93  ? 40  TYR C CE2 1 
ATOM   1688 C CZ  . TYR C 1 41 ? 26.822  -28.276 30.403  1.00 43.06  ? 40  TYR C CZ  1 
ATOM   1689 O OH  . TYR C 1 41 ? 27.835  -27.452 30.798  1.00 55.46  ? 40  TYR C OH  1 
ATOM   1690 N N   . PRO C 1 42 ? 20.970  -32.329 30.166  1.00 36.94  ? 41  PRO C N   1 
ATOM   1691 C CA  . PRO C 1 42 ? 19.701  -32.841 29.663  1.00 35.36  ? 41  PRO C CA  1 
ATOM   1692 C C   . PRO C 1 42 ? 19.370  -31.877 28.537  1.00 33.78  ? 41  PRO C C   1 
ATOM   1693 O O   . PRO C 1 42 ? 19.478  -30.650 28.702  1.00 33.67  ? 41  PRO C O   1 
ATOM   1694 C CB  . PRO C 1 42 ? 18.742  -32.736 30.837  1.00 35.72  ? 41  PRO C CB  1 
ATOM   1695 C CG  . PRO C 1 42 ? 19.342  -31.667 31.694  1.00 35.53  ? 41  PRO C CG  1 
ATOM   1696 C CD  . PRO C 1 42 ? 20.814  -31.448 31.335  1.00 37.17  ? 41  PRO C CD  1 
ATOM   1697 N N   . ILE C 1 43 ? 19.022  -32.476 27.394  1.00 32.15  ? 42  ILE C N   1 
ATOM   1698 C CA  . ILE C 1 43 ? 18.756  -31.698 26.193  1.00 32.14  ? 42  ILE C CA  1 
ATOM   1699 C C   . ILE C 1 43 ? 17.325  -31.978 25.777  1.00 35.33  ? 42  ILE C C   1 
ATOM   1700 O O   . ILE C 1 43 ? 16.874  -33.124 25.800  1.00 38.33  ? 42  ILE C O   1 
ATOM   1701 C CB  . ILE C 1 43 ? 19.715  -32.121 25.068  1.00 32.94  ? 42  ILE C CB  1 
ATOM   1702 C CG1 . ILE C 1 43 ? 21.188  -31.927 25.467  1.00 31.15  ? 42  ILE C CG1 1 
ATOM   1703 C CG2 . ILE C 1 43 ? 19.349  -31.456 23.723  1.00 29.06  ? 42  ILE C CG2 1 
ATOM   1704 C CD1 . ILE C 1 43 ? 21.584  -30.496 25.782  1.00 32.44  ? 42  ILE C CD1 1 
ATOM   1705 N N   . PHE C 1 44 ? 16.653  -30.922 25.306  1.00 36.76  ? 43  PHE C N   1 
ATOM   1706 C CA  . PHE C 1 44 ? 15.358  -31.072 24.669  1.00 33.70  ? 43  PHE C CA  1 
ATOM   1707 C C   . PHE C 1 44 ? 15.518  -30.646 23.214  1.00 30.37  ? 43  PHE C C   1 
ATOM   1708 O O   . PHE C 1 44 ? 15.997  -29.548 22.959  1.00 30.18  ? 43  PHE C O   1 
ATOM   1709 C CB  . PHE C 1 44 ? 14.422  -30.068 25.353  1.00 32.82  ? 43  PHE C CB  1 
ATOM   1710 C CG  . PHE C 1 44 ? 13.036  -29.999 24.727  1.00 38.30  ? 43  PHE C CG  1 
ATOM   1711 C CD1 . PHE C 1 44 ? 12.094  -31.005 24.968  1.00 37.45  ? 43  PHE C CD1 1 
ATOM   1712 C CD2 . PHE C 1 44 ? 12.683  -28.939 23.890  1.00 37.94  ? 43  PHE C CD2 1 
ATOM   1713 C CE1 . PHE C 1 44 ? 10.813  -30.947 24.421  1.00 43.96  ? 43  PHE C CE1 1 
ATOM   1714 C CE2 . PHE C 1 44 ? 11.408  -28.897 23.319  1.00 39.80  ? 43  PHE C CE2 1 
ATOM   1715 C CZ  . PHE C 1 44 ? 10.477  -29.889 23.590  1.00 45.19  ? 43  PHE C CZ  1 
ATOM   1716 N N   . PHE C 1 45 ? 15.117  -31.529 22.299  1.00 29.56  ? 44  PHE C N   1 
ATOM   1717 C CA  . PHE C 1 45 ? 15.214  -31.300 20.870  1.00 32.20  ? 44  PHE C CA  1 
ATOM   1718 C C   . PHE C 1 45 ? 13.927  -30.660 20.360  1.00 33.53  ? 44  PHE C C   1 
ATOM   1719 O O   . PHE C 1 45 ? 12.830  -31.218 20.506  1.00 32.57  ? 44  PHE C O   1 
ATOM   1720 C CB  . PHE C 1 45 ? 15.492  -32.602 20.122  1.00 29.44  ? 44  PHE C CB  1 
ATOM   1721 C CG  . PHE C 1 45 ? 16.863  -33.170 20.450  1.00 29.09  ? 44  PHE C CG  1 
ATOM   1722 C CD1 . PHE C 1 45 ? 17.995  -32.774 19.734  1.00 26.54  ? 44  PHE C CD1 1 
ATOM   1723 C CD2 . PHE C 1 45 ? 17.018  -34.073 21.505  1.00 29.07  ? 44  PHE C CD2 1 
ATOM   1724 C CE1 . PHE C 1 45 ? 19.254  -33.306 20.046  1.00 31.57  ? 44  PHE C CE1 1 
ATOM   1725 C CE2 . PHE C 1 45 ? 18.269  -34.614 21.802  1.00 33.64  ? 44  PHE C CE2 1 
ATOM   1726 C CZ  . PHE C 1 45 ? 19.384  -34.215 21.093  1.00 33.87  ? 44  PHE C CZ  1 
ATOM   1727 N N   . PHE C 1 46 ? 14.084  -29.508 19.696  1.00 29.17  ? 45  PHE C N   1 
ATOM   1728 C CA  . PHE C 1 46 ? 12.931  -28.879 19.066  1.00 28.61  ? 45  PHE C CA  1 
ATOM   1729 C C   . PHE C 1 46 ? 12.420  -29.729 17.907  1.00 30.13  ? 45  PHE C C   1 
ATOM   1730 O O   . PHE C 1 46 ? 13.169  -30.491 17.298  1.00 31.99  ? 45  PHE C O   1 
ATOM   1731 C CB  . PHE C 1 46 ? 13.221  -27.423 18.673  1.00 28.05  ? 45  PHE C CB  1 
ATOM   1732 C CG  . PHE C 1 46 ? 13.534  -26.438 19.791  1.00 28.98  ? 45  PHE C CG  1 
ATOM   1733 C CD1 . PHE C 1 46 ? 12.523  -25.942 20.613  1.00 32.67  ? 45  PHE C CD1 1 
ATOM   1734 C CD2 . PHE C 1 46 ? 14.832  -25.973 20.006  1.00 26.53  ? 45  PHE C CD2 1 
ATOM   1735 C CE1 . PHE C 1 46 ? 12.826  -25.022 21.614  1.00 31.21  ? 45  PHE C CE1 1 
ATOM   1736 C CE2 . PHE C 1 46 ? 15.120  -25.046 21.007  1.00 30.50  ? 45  PHE C CE2 1 
ATOM   1737 C CZ  . PHE C 1 46 ? 14.121  -24.572 21.813  1.00 31.26  ? 45  PHE C CZ  1 
ATOM   1738 N N   . GLY C 1 47 ? 11.137  -29.568 17.579  1.00 30.62  ? 46  GLY C N   1 
ATOM   1739 C CA  . GLY C 1 47 ? 10.583  -30.305 16.453  1.00 34.03  ? 46  GLY C CA  1 
ATOM   1740 C C   . GLY C 1 47 ? 10.174  -31.721 16.838  1.00 39.19  ? 46  GLY C C   1 
ATOM   1741 O O   . GLY C 1 47 ? 8.987   -32.049 16.795  1.00 42.10  ? 46  GLY C O   1 
ATOM   1742 N N   . THR C 1 48 ? 11.147  -32.566 17.207  1.00 37.02  ? 47  THR C N   1 
ATOM   1743 C CA  . THR C 1 48 ? 10.781  -33.916 17.626  1.00 36.22  ? 47  THR C CA  1 
ATOM   1744 C C   . THR C 1 48 ? 10.264  -33.878 19.064  1.00 35.72  ? 47  THR C C   1 
ATOM   1745 O O   . THR C 1 48 ? 9.518   -34.771 19.473  1.00 42.36  ? 47  THR C O   1 
ATOM   1746 C CB  . THR C 1 48 ? 11.971  -34.866 17.548  1.00 34.75  ? 47  THR C CB  1 
ATOM   1747 O OG1 . THR C 1 48 ? 12.818  -34.314 18.558  1.00 36.52  ? 47  THR C OG1 1 
ATOM   1748 C CG2 . THR C 1 48 ? 12.551  -35.014 16.151  1.00 32.54  ? 47  THR C CG2 1 
ATOM   1749 N N   . HIS C 1 49 ? 10.693  -32.872 19.833  1.00 33.50  ? 48  HIS C N   1 
ATOM   1750 C CA  . HIS C 1 49 ? 10.371  -32.738 21.250  1.00 39.68  ? 48  HIS C CA  1 
ATOM   1751 C C   . HIS C 1 49 ? 10.835  -33.938 22.087  1.00 37.40  ? 48  HIS C C   1 
ATOM   1752 O O   . HIS C 1 49 ? 10.200  -34.255 23.086  1.00 41.20  ? 48  HIS C O   1 
ATOM   1753 C CB  . HIS C 1 49 ? 8.877   -32.463 21.467  1.00 42.64  ? 48  HIS C CB  1 
ATOM   1754 C CG  . HIS C 1 49 ? 8.352   -31.379 20.582  1.00 44.08  ? 48  HIS C CG  1 
ATOM   1755 N ND1 . HIS C 1 49 ? 7.235   -31.553 19.794  1.00 49.84  ? 48  HIS C ND1 1 
ATOM   1756 C CD2 . HIS C 1 49 ? 8.811   -30.158 20.316  1.00 39.21  ? 48  HIS C CD2 1 
ATOM   1757 C CE1 . HIS C 1 49 ? 7.031   -30.451 19.082  1.00 49.98  ? 48  HIS C CE1 1 
ATOM   1758 N NE2 . HIS C 1 49 ? 7.976   -29.589 19.396  1.00 47.54  ? 48  HIS C NE2 1 
ATOM   1759 N N   . GLU C 1 50 ? 11.946  -34.574 21.706  1.00 34.72  ? 49  GLU C N   1 
ATOM   1760 C CA  . GLU C 1 50 ? 12.500  -35.650 22.512  1.00 36.97  ? 49  GLU C CA  1 
ATOM   1761 C C   . GLU C 1 50 ? 13.631  -35.138 23.400  1.00 37.00  ? 49  GLU C C   1 
ATOM   1762 O O   . GLU C 1 50 ? 14.017  -33.968 23.334  1.00 37.13  ? 49  GLU C O   1 
ATOM   1763 C CB  . GLU C 1 50 ? 12.905  -36.762 21.559  1.00 35.83  ? 49  GLU C CB  1 
ATOM   1764 C CG  . GLU C 1 50 ? 11.708  -37.273 20.765  1.00 43.87  ? 49  GLU C CG  1 
ATOM   1765 C CD  . GLU C 1 50 ? 12.169  -38.291 19.747  1.00 51.66  ? 49  GLU C CD  1 
ATOM   1766 O OE1 . GLU C 1 50 ? 13.401  -38.494 19.594  1.00 56.26  ? 49  GLU C OE1 1 
ATOM   1767 O OE2 . GLU C 1 50 ? 11.276  -38.879 19.109  1.00 62.58  ? 49  GLU C OE2 1 
ATOM   1768 N N   . THR C 1 51 ? 14.131  -36.018 24.281  1.00 40.78  ? 50  THR C N   1 
ATOM   1769 C CA  . THR C 1 51 ? 15.197  -35.641 25.200  1.00 38.64  ? 50  THR C CA  1 
ATOM   1770 C C   . THR C 1 51 ? 16.335  -36.658 25.126  1.00 34.11  ? 50  THR C C   1 
ATOM   1771 O O   . THR C 1 51 ? 16.175  -37.778 24.646  1.00 36.60  ? 50  THR C O   1 
ATOM   1772 C CB  . THR C 1 51 ? 14.696  -35.471 26.637  1.00 43.16  ? 50  THR C CB  1 
ATOM   1773 O OG1 . THR C 1 51 ? 14.138  -36.747 26.955  1.00 45.15  ? 50  THR C OG1 1 
ATOM   1774 C CG2 . THR C 1 51 ? 13.764  -34.286 26.831  1.00 40.04  ? 50  THR C CG2 1 
ATOM   1775 N N   . ALA C 1 52 ? 17.515  -36.216 25.552  1.00 37.08  ? 51  ALA C N   1 
ATOM   1776 C CA  . ALA C 1 52 ? 18.696  -37.060 25.674  1.00 39.19  ? 51  ALA C CA  1 
ATOM   1777 C C   . ALA C 1 52 ? 19.700  -36.362 26.585  1.00 39.22  ? 51  ALA C C   1 
ATOM   1778 O O   . ALA C 1 52 ? 19.502  -35.208 26.961  1.00 39.84  ? 51  ALA C O   1 
ATOM   1779 C CB  . ALA C 1 52 ? 19.284  -37.365 24.314  1.00 35.94  ? 51  ALA C CB  1 
ATOM   1780 N N   . PHE C 1 53 ? 20.765  -37.085 26.967  1.00 39.92  ? 52  PHE C N   1 
ATOM   1781 C CA  . PHE C 1 53 ? 21.876  -36.494 27.698  1.00 36.48  ? 52  PHE C CA  1 
ATOM   1782 C C   . PHE C 1 53 ? 23.032  -36.350 26.724  1.00 35.15  ? 52  PHE C C   1 
ATOM   1783 O O   . PHE C 1 53 ? 23.399  -37.305 26.039  1.00 35.12  ? 52  PHE C O   1 
ATOM   1784 C CB  . PHE C 1 53 ? 22.286  -37.407 28.860  1.00 35.69  ? 52  PHE C CB  1 
ATOM   1785 C CG  . PHE C 1 53 ? 21.307  -37.318 30.012  1.00 37.56  ? 52  PHE C CG  1 
ATOM   1786 C CD1 . PHE C 1 53 ? 21.023  -36.095 30.613  1.00 40.88  ? 52  PHE C CD1 1 
ATOM   1787 C CD2 . PHE C 1 53 ? 20.604  -38.437 30.438  1.00 48.04  ? 52  PHE C CD2 1 
ATOM   1788 C CE1 . PHE C 1 53 ? 20.104  -35.999 31.651  1.00 41.21  ? 52  PHE C CE1 1 
ATOM   1789 C CE2 . PHE C 1 53 ? 19.694  -38.341 31.488  1.00 46.83  ? 52  PHE C CE2 1 
ATOM   1790 C CZ  . PHE C 1 53 ? 19.431  -37.122 32.079  1.00 44.50  ? 52  PHE C CZ  1 
ATOM   1791 N N   . LEU C 1 54 ? 23.623  -35.156 26.684  1.00 31.08  ? 53  LEU C N   1 
ATOM   1792 C CA  . LEU C 1 54 ? 24.774  -34.950 25.823  1.00 30.19  ? 53  LEU C CA  1 
ATOM   1793 C C   . LEU C 1 54 ? 25.851  -34.217 26.607  1.00 31.82  ? 53  LEU C C   1 
ATOM   1794 O O   . LEU C 1 54 ? 25.541  -33.434 27.503  1.00 34.96  ? 53  LEU C O   1 
ATOM   1795 C CB  . LEU C 1 54 ? 24.451  -34.207 24.518  1.00 33.40  ? 53  LEU C CB  1 
ATOM   1796 C CG  . LEU C 1 54 ? 23.586  -34.957 23.494  1.00 35.87  ? 53  LEU C CG  1 
ATOM   1797 C CD1 . LEU C 1 54 ? 23.165  -34.027 22.357  1.00 33.11  ? 53  LEU C CD1 1 
ATOM   1798 C CD2 . LEU C 1 54 ? 24.341  -36.158 22.935  1.00 40.79  ? 53  LEU C CD2 1 
ATOM   1799 N N   . GLY C 1 55 ? 27.103  -34.470 26.213  1.00 33.65  ? 54  GLY C N   1 
ATOM   1800 C CA  . GLY C 1 55 ? 28.273  -33.781 26.736  1.00 35.30  ? 54  GLY C CA  1 
ATOM   1801 C C   . GLY C 1 55 ? 28.494  -32.449 26.027  1.00 39.47  ? 54  GLY C C   1 
ATOM   1802 O O   . GLY C 1 55 ? 27.984  -32.213 24.910  1.00 34.50  ? 54  GLY C O   1 
ATOM   1803 N N   . PRO C 1 56 ? 29.288  -31.544 26.647  1.00 38.70  ? 55  PRO C N   1 
ATOM   1804 C CA  . PRO C 1 56 ? 29.354  -30.162 26.185  1.00 40.53  ? 55  PRO C CA  1 
ATOM   1805 C C   . PRO C 1 56 ? 30.045  -30.105 24.827  1.00 39.76  ? 55  PRO C C   1 
ATOM   1806 O O   . PRO C 1 56 ? 29.786  -29.193 24.042  1.00 47.33  ? 55  PRO C O   1 
ATOM   1807 C CB  . PRO C 1 56 ? 30.089  -29.383 27.319  1.00 43.00  ? 55  PRO C CB  1 
ATOM   1808 C CG  . PRO C 1 56 ? 30.836  -30.460 28.105  1.00 36.48  ? 55  PRO C CG  1 
ATOM   1809 C CD  . PRO C 1 56 ? 30.182  -31.811 27.794  1.00 39.21  ? 55  PRO C CD  1 
ATOM   1810 N N   . LYS C 1 57 ? 30.857  -31.128 24.540  1.00 38.78  ? 56  LYS C N   1 
ATOM   1811 C CA  . LYS C 1 57 ? 31.483  -31.337 23.243  1.00 41.26  ? 56  LYS C CA  1 
ATOM   1812 C C   . LYS C 1 57 ? 30.432  -31.280 22.128  1.00 48.00  ? 56  LYS C C   1 
ATOM   1813 O O   . LYS C 1 57 ? 30.723  -30.870 21.002  1.00 41.70  ? 56  LYS C O   1 
ATOM   1814 C CB  . LYS C 1 57 ? 32.043  -32.767 23.164  1.00 38.07  ? 56  LYS C CB  1 
ATOM   1815 N N   . ASP C 1 58 ? 29.214  -31.738 22.438  1.00 43.72  ? 57  ASP C N   1 
ATOM   1816 C CA  . ASP C 1 58 ? 28.241  -32.032 21.401  1.00 38.74  ? 57  ASP C CA  1 
ATOM   1817 C C   . ASP C 1 58 ? 27.278  -30.866 21.216  1.00 37.04  ? 57  ASP C C   1 
ATOM   1818 O O   . ASP C 1 58 ? 26.272  -31.019 20.513  1.00 33.30  ? 57  ASP C O   1 
ATOM   1819 C CB  . ASP C 1 58 ? 27.500  -33.319 21.702  1.00 41.56  ? 57  ASP C CB  1 
ATOM   1820 C CG  . ASP C 1 58 ? 28.378  -34.553 21.708  1.00 44.37  ? 57  ASP C CG  1 
ATOM   1821 O OD1 . ASP C 1 58 ? 29.202  -34.676 20.789  1.00 48.22  ? 57  ASP C OD1 1 
ATOM   1822 O OD2 . ASP C 1 58 ? 28.185  -35.400 22.588  1.00 47.10  ? 57  ASP C OD2 1 
ATOM   1823 N N   . LEU C 1 59 ? 27.580  -29.728 21.862  1.00 33.16  ? 58  LEU C N   1 
ATOM   1824 C CA  . LEU C 1 59 ? 26.643  -28.617 21.986  1.00 37.57  ? 58  LEU C CA  1 
ATOM   1825 C C   . LEU C 1 59 ? 27.260  -27.328 21.458  1.00 40.22  ? 58  LEU C C   1 
ATOM   1826 O O   . LEU C 1 59 ? 28.436  -27.068 21.715  1.00 41.95  ? 58  LEU C O   1 
ATOM   1827 C CB  . LEU C 1 59 ? 26.251  -28.438 23.451  1.00 35.16  ? 58  LEU C CB  1 
ATOM   1828 C CG  . LEU C 1 59 ? 25.701  -29.696 24.135  1.00 33.34  ? 58  LEU C CG  1 
ATOM   1829 C CD1 . LEU C 1 59 ? 25.528  -29.415 25.603  1.00 35.04  ? 58  LEU C CD1 1 
ATOM   1830 C CD2 . LEU C 1 59 ? 24.361  -30.123 23.496  1.00 26.97  ? 58  LEU C CD2 1 
ATOM   1831 N N   . PHE C 1 60 ? 26.430  -26.521 20.774  1.00 40.05  ? 59  PHE C N   1 
ATOM   1832 C CA  . PHE C 1 60 ? 26.870  -25.275 20.145  1.00 39.57  ? 59  PHE C CA  1 
ATOM   1833 C C   . PHE C 1 60 ? 25.852  -24.181 20.438  1.00 38.54  ? 59  PHE C C   1 
ATOM   1834 O O   . PHE C 1 60 ? 24.664  -24.356 20.179  1.00 40.81  ? 59  PHE C O   1 
ATOM   1835 C CB  . PHE C 1 60 ? 27.151  -25.437 18.647  1.00 42.15  ? 59  PHE C CB  1 
ATOM   1836 C CG  . PHE C 1 60 ? 28.070  -26.609 18.327  1.00 41.09  ? 59  PHE C CG  1 
ATOM   1837 C CD1 . PHE C 1 60 ? 27.584  -27.918 18.310  1.00 37.76  ? 59  PHE C CD1 1 
ATOM   1838 C CD2 . PHE C 1 60 ? 29.428  -26.408 18.072  1.00 44.90  ? 59  PHE C CD2 1 
ATOM   1839 C CE1 . PHE C 1 60 ? 28.423  -29.000 18.078  1.00 32.76  ? 59  PHE C CE1 1 
ATOM   1840 C CE2 . PHE C 1 60 ? 30.266  -27.491 17.812  1.00 42.21  ? 59  PHE C CE2 1 
ATOM   1841 C CZ  . PHE C 1 60 ? 29.760  -28.780 17.805  1.00 42.04  ? 59  PHE C CZ  1 
ATOM   1842 N N   . PRO C 1 61 ? 26.258  -23.024 21.019  1.00 40.11  ? 60  PRO C N   1 
ATOM   1843 C CA  . PRO C 1 61 ? 25.310  -21.931 21.271  1.00 38.11  ? 60  PRO C CA  1 
ATOM   1844 C C   . PRO C 1 61 ? 24.661  -21.494 19.960  1.00 36.35  ? 60  PRO C C   1 
ATOM   1845 O O   . PRO C 1 61 ? 25.337  -21.390 18.938  1.00 41.13  ? 60  PRO C O   1 
ATOM   1846 C CB  . PRO C 1 61 ? 26.106  -20.800 21.994  1.00 38.03  ? 60  PRO C CB  1 
ATOM   1847 C CG  . PRO C 1 61 ? 27.517  -21.380 22.199  1.00 39.88  ? 60  PRO C CG  1 
ATOM   1848 C CD  . PRO C 1 61 ? 27.630  -22.713 21.464  1.00 42.93  ? 60  PRO C CD  1 
ATOM   1849 N N   . TYR C 1 62 ? 23.325  -21.370 20.009  1.00 39.74  ? 61  TYR C N   1 
ATOM   1850 C CA  . TYR C 1 62 ? 22.453  -21.126 18.873  1.00 41.15  ? 61  TYR C CA  1 
ATOM   1851 C C   . TYR C 1 62 ? 22.920  -19.892 18.098  1.00 48.84  ? 61  TYR C C   1 
ATOM   1852 O O   . TYR C 1 62 ? 23.106  -19.962 16.884  1.00 50.14  ? 61  TYR C O   1 
ATOM   1853 C CB  . TYR C 1 62 ? 21.038  -20.897 19.404  1.00 42.35  ? 61  TYR C CB  1 
ATOM   1854 C CG  . TYR C 1 62 ? 20.051  -20.577 18.296  1.00 46.32  ? 61  TYR C CG  1 
ATOM   1855 C CD1 . TYR C 1 62 ? 19.913  -21.427 17.195  1.00 44.42  ? 61  TYR C CD1 1 
ATOM   1856 C CD2 . TYR C 1 62 ? 19.307  -19.400 18.325  1.00 45.48  ? 61  TYR C CD2 1 
ATOM   1857 C CE1 . TYR C 1 62 ? 19.021  -21.126 16.176  1.00 43.30  ? 61  TYR C CE1 1 
ATOM   1858 C CE2 . TYR C 1 62 ? 18.419  -19.088 17.310  1.00 49.03  ? 61  TYR C CE2 1 
ATOM   1859 C CZ  . TYR C 1 62 ? 18.281  -19.954 16.235  1.00 41.12  ? 61  TYR C CZ  1 
ATOM   1860 O OH  . TYR C 1 62 ? 17.401  -19.647 15.247  1.00 41.63  ? 61  TYR C OH  1 
ATOM   1861 N N   . ASP C 1 63 ? 23.174  -18.796 18.825  1.00 51.19  ? 62  ASP C N   1 
ATOM   1862 C CA  . ASP C 1 63 ? 23.495  -17.516 18.204  1.00 56.62  ? 62  ASP C CA  1 
ATOM   1863 C C   . ASP C 1 63 ? 24.845  -17.557 17.506  1.00 46.38  ? 62  ASP C C   1 
ATOM   1864 O O   . ASP C 1 63 ? 25.001  -16.974 16.439  1.00 56.27  ? 62  ASP C O   1 
ATOM   1865 C CB  . ASP C 1 63 ? 23.330  -16.343 19.154  1.00 59.46  ? 62  ASP C CB  1 
ATOM   1866 C CG  . ASP C 1 63 ? 21.949  -15.715 19.075  1.00 72.98  ? 62  ASP C CG  1 
ATOM   1867 O OD1 . ASP C 1 63 ? 21.199  -15.812 20.069  1.00 70.09  ? 62  ASP C OD1 1 
ATOM   1868 O OD2 . ASP C 1 63 ? 21.629  -15.162 17.998  1.00 82.19  ? 62  ASP C OD2 1 
ATOM   1869 N N   . LYS C 1 64 ? 25.801  -18.268 18.091  1.00 42.09  ? 63  LYS C N   1 
ATOM   1870 C CA  . LYS C 1 64 ? 27.134  -18.357 17.518  1.00 42.24  ? 63  LYS C CA  1 
ATOM   1871 C C   . LYS C 1 64 ? 27.121  -19.253 16.282  1.00 41.56  ? 63  LYS C C   1 
ATOM   1872 O O   . LYS C 1 64 ? 27.911  -19.045 15.363  1.00 39.46  ? 63  LYS C O   1 
ATOM   1873 C CB  . LYS C 1 64 ? 28.157  -18.876 18.537  1.00 44.34  ? 63  LYS C CB  1 
ATOM   1874 N N   . SER C 1 65 ? 26.229  -20.264 16.241  1.00 39.46  ? 64  SER C N   1 
ATOM   1875 C CA  . SER C 1 65 ? 26.448  -21.300 15.235  1.00 34.55  ? 64  SER C CA  1 
ATOM   1876 C C   . SER C 1 65 ? 25.294  -21.388 14.223  1.00 35.36  ? 64  SER C C   1 
ATOM   1877 O O   . SER C 1 65 ? 25.327  -22.217 13.316  1.00 35.26  ? 64  SER C O   1 
ATOM   1878 C CB  . SER C 1 65 ? 26.771  -22.634 15.879  1.00 39.05  ? 64  SER C CB  1 
ATOM   1879 O OG  . SER C 1 65 ? 25.639  -23.138 16.583  1.00 38.58  ? 64  SER C OG  1 
ATOM   1880 N N   . LYS C 1 66 ? 24.262  -20.558 14.390  1.00 33.30  ? 65  LYS C N   1 
ATOM   1881 C CA  . LYS C 1 66 ? 23.078  -20.718 13.545  1.00 40.28  ? 65  LYS C CA  1 
ATOM   1882 C C   . LYS C 1 66 ? 23.399  -20.483 12.074  1.00 40.87  ? 65  LYS C C   1 
ATOM   1883 O O   . LYS C 1 66 ? 22.845  -21.172 11.218  1.00 37.55  ? 65  LYS C O   1 
ATOM   1884 C CB  . LYS C 1 66 ? 21.862  -19.872 13.919  1.00 36.94  ? 65  LYS C CB  1 
ATOM   1885 C CG  . LYS C 1 66 ? 22.119  -18.382 13.975  1.00 40.08  ? 65  LYS C CG  1 
ATOM   1886 C CD  . LYS C 1 66 ? 20.797  -17.707 14.307  1.00 48.85  ? 65  LYS C CD  1 
ATOM   1887 C CE  . LYS C 1 66 ? 20.858  -16.223 14.422  1.00 52.91  ? 65  LYS C CE  1 
ATOM   1888 N NZ  . LYS C 1 66 ? 19.699  -15.888 15.245  1.00 59.81  ? 65  LYS C NZ  1 
ATOM   1889 N N   . ASP C 1 67 ? 24.301  -19.533 11.789  1.00 42.80  ? 66  ASP C N   1 
ATOM   1890 C CA  . ASP C 1 67 ? 24.716  -19.278 10.410  1.00 45.06  ? 66  ASP C CA  1 
ATOM   1891 C C   . ASP C 1 67 ? 25.176  -20.595 9.781   1.00 42.60  ? 66  ASP C C   1 
ATOM   1892 O O   . ASP C 1 67 ? 24.912  -20.852 8.606   1.00 43.09  ? 66  ASP C O   1 
ATOM   1893 C CB  . ASP C 1 67 ? 25.617  -18.046 10.262  1.00 47.78  ? 66  ASP C CB  1 
ATOM   1894 C CG  . ASP C 1 67 ? 27.050  -18.131 10.787  1.00 60.06  ? 66  ASP C CG  1 
ATOM   1895 O OD1 . ASP C 1 67 ? 27.489  -19.238 11.187  1.00 56.13  ? 66  ASP C OD1 1 
ATOM   1896 O OD2 . ASP C 1 67 ? 27.732  -17.072 10.815  1.00 64.97  ? 66  ASP C OD2 1 
ATOM   1897 N N   . LYS C 1 68 ? 25.773  -21.477 10.600  1.00 38.23  ? 67  LYS C N   1 
ATOM   1898 C CA  . LYS C 1 68 ? 26.307  -22.738 10.105  1.00 38.50  ? 67  LYS C CA  1 
ATOM   1899 C C   . LYS C 1 68 ? 25.273  -23.884 10.134  1.00 36.85  ? 67  LYS C C   1 
ATOM   1900 O O   . LYS C 1 68 ? 25.199  -24.645 9.186   1.00 37.06  ? 67  LYS C O   1 
ATOM   1901 C CB  . LYS C 1 68 ? 27.624  -23.029 10.837  1.00 42.95  ? 67  LYS C CB  1 
ATOM   1902 C CG  . LYS C 1 68 ? 28.368  -24.295 10.438  1.00 50.49  ? 67  LYS C CG  1 
ATOM   1903 C CD  . LYS C 1 68 ? 29.586  -24.511 11.339  1.00 55.64  ? 67  LYS C CD  1 
ATOM   1904 C CE  . LYS C 1 68 ? 30.171  -25.896 11.296  1.00 62.01  ? 67  LYS C CE  1 
ATOM   1905 N NZ  . LYS C 1 68 ? 30.652  -26.300 9.971   1.00 66.12  ? 67  LYS C NZ  1 
ATOM   1906 N N   . TYR C 1 69 ? 24.507  -24.062 11.226  1.00 30.68  ? 68  TYR C N   1 
ATOM   1907 C CA  . TYR C 1 69 ? 23.680  -25.261 11.323  1.00 32.79  ? 68  TYR C CA  1 
ATOM   1908 C C   . TYR C 1 69 ? 22.208  -24.931 11.104  1.00 34.94  ? 68  TYR C C   1 
ATOM   1909 O O   . TYR C 1 69 ? 21.389  -25.842 11.000  1.00 33.46  ? 68  TYR C O   1 
ATOM   1910 C CB  . TYR C 1 69 ? 23.796  -25.880 12.721  1.00 31.33  ? 68  TYR C CB  1 
ATOM   1911 C CG  . TYR C 1 69 ? 25.206  -26.329 13.041  1.00 30.75  ? 68  TYR C CG  1 
ATOM   1912 C CD1 . TYR C 1 69 ? 25.933  -27.134 12.166  1.00 33.44  ? 68  TYR C CD1 1 
ATOM   1913 C CD2 . TYR C 1 69 ? 25.834  -25.881 14.198  1.00 34.26  ? 68  TYR C CD2 1 
ATOM   1914 C CE1 . TYR C 1 69 ? 27.228  -27.541 12.462  1.00 32.81  ? 68  TYR C CE1 1 
ATOM   1915 C CE2 . TYR C 1 69 ? 27.114  -26.306 14.522  1.00 36.13  ? 68  TYR C CE2 1 
ATOM   1916 C CZ  . TYR C 1 69 ? 27.813  -27.120 13.648  1.00 36.11  ? 68  TYR C CZ  1 
ATOM   1917 O OH  . TYR C 1 69 ? 29.087  -27.446 14.016  1.00 37.84  ? 68  TYR C OH  1 
ATOM   1918 N N   . GLY C 1 70 ? 21.875  -23.633 11.110  1.00 27.40  ? 69  GLY C N   1 
ATOM   1919 C CA  . GLY C 1 70 ? 20.467  -23.256 11.031  1.00 35.25  ? 69  GLY C CA  1 
ATOM   1920 C C   . GLY C 1 70 ? 20.051  -23.162 9.568   1.00 33.44  ? 69  GLY C C   1 
ATOM   1921 O O   . GLY C 1 70 ? 19.998  -22.073 8.994   1.00 34.24  ? 69  GLY C O   1 
ATOM   1922 N N   . LYS C 1 71 ? 19.886  -24.329 8.952   1.00 34.27  ? 70  LYS C N   1 
ATOM   1923 C CA  . LYS C 1 71 ? 19.556  -24.414 7.537   1.00 37.32  ? 70  LYS C CA  1 
ATOM   1924 C C   . LYS C 1 71 ? 18.677  -25.640 7.397   1.00 35.48  ? 70  LYS C C   1 
ATOM   1925 O O   . LYS C 1 71 ? 18.881  -26.620 8.115   1.00 34.98  ? 70  LYS C O   1 
ATOM   1926 C CB  . LYS C 1 71 ? 20.799  -24.559 6.653   1.00 41.32  ? 70  LYS C CB  1 
ATOM   1927 C CG  . LYS C 1 71 ? 21.839  -25.545 7.190   1.00 45.91  ? 70  LYS C CG  1 
ATOM   1928 C CD  . LYS C 1 71 ? 23.060  -25.960 6.375   1.00 49.64  ? 70  LYS C CD  1 
ATOM   1929 C CE  . LYS C 1 71 ? 24.011  -26.777 7.219   1.00 52.75  ? 70  LYS C CE  1 
ATOM   1930 N N   . PRO C 1 72 ? 17.638  -25.606 6.537   1.00 31.82  ? 71  PRO C N   1 
ATOM   1931 C CA  . PRO C 1 72 ? 16.692  -26.711 6.486   1.00 27.43  ? 71  PRO C CA  1 
ATOM   1932 C C   . PRO C 1 72 ? 17.352  -28.042 6.155   1.00 33.28  ? 71  PRO C C   1 
ATOM   1933 O O   . PRO C 1 72 ? 18.404  -28.083 5.530   1.00 32.70  ? 71  PRO C O   1 
ATOM   1934 C CB  . PRO C 1 72 ? 15.786  -26.241 5.335   1.00 31.66  ? 71  PRO C CB  1 
ATOM   1935 C CG  . PRO C 1 72 ? 15.769  -24.751 5.561   1.00 29.69  ? 71  PRO C CG  1 
ATOM   1936 C CD  . PRO C 1 72 ? 17.262  -24.474 5.671   1.00 29.92  ? 71  PRO C CD  1 
ATOM   1937 N N   . ASN C 1 73 ? 16.694  -29.119 6.561   1.00 30.83  ? 72  ASN C N   1 
ATOM   1938 C CA  . ASN C 1 73 ? 17.016  -30.403 5.978   1.00 37.50  ? 72  ASN C CA  1 
ATOM   1939 C C   . ASN C 1 73 ? 15.787  -31.277 6.155   1.00 31.04  ? 72  ASN C C   1 
ATOM   1940 O O   . ASN C 1 73 ? 14.828  -30.870 6.816   1.00 30.36  ? 72  ASN C O   1 
ATOM   1941 C CB  . ASN C 1 73 ? 18.354  -30.971 6.443   1.00 41.22  ? 72  ASN C CB  1 
ATOM   1942 C CG  . ASN C 1 73 ? 18.254  -31.545 7.832   1.00 41.12  ? 72  ASN C CG  1 
ATOM   1943 O OD1 . ASN C 1 73 ? 17.554  -32.545 8.058   1.00 39.34  ? 72  ASN C OD1 1 
ATOM   1944 N ND2 . ASN C 1 73 ? 18.946  -30.914 8.760   1.00 48.05  ? 72  ASN C ND2 1 
ATOM   1945 N N   . LYS C 1 74 ? 15.814  -32.455 5.528   1.00 33.80  ? 73  LYS C N   1 
ATOM   1946 C CA  . LYS C 1 74 ? 14.575  -33.201 5.338   1.00 32.18  ? 73  LYS C CA  1 
ATOM   1947 C C   . LYS C 1 74 ? 14.376  -34.217 6.451   1.00 33.50  ? 73  LYS C C   1 
ATOM   1948 O O   . LYS C 1 74 ? 13.481  -35.053 6.361   1.00 36.93  ? 73  LYS C O   1 
ATOM   1949 C CB  . LYS C 1 74 ? 14.601  -33.938 3.989   1.00 34.39  ? 73  LYS C CB  1 
ATOM   1950 N N   . ARG C 1 75 ? 15.226  -34.191 7.487   1.00 32.01  ? 74  ARG C N   1 
ATOM   1951 C CA  . ARG C 1 75 ? 15.054  -35.164 8.561   1.00 30.19  ? 74  ARG C CA  1 
ATOM   1952 C C   . ARG C 1 75 ? 13.790  -34.841 9.343   1.00 33.64  ? 74  ARG C C   1 
ATOM   1953 O O   . ARG C 1 75 ? 13.438  -33.662 9.528   1.00 29.74  ? 74  ARG C O   1 
ATOM   1954 C CB  . ARG C 1 75 ? 16.249  -35.300 9.523   1.00 32.32  ? 74  ARG C CB  1 
ATOM   1955 C CG  . ARG C 1 75 ? 17.591  -35.547 8.832   1.00 38.25  ? 74  ARG C CG  1 
ATOM   1956 C CD  . ARG C 1 75 ? 17.856  -36.974 8.322   1.00 38.10  ? 74  ARG C CD  1 
ATOM   1957 N NE  . ARG C 1 75 ? 17.722  -37.898 9.457   1.00 35.17  ? 74  ARG C NE  1 
ATOM   1958 C CZ  . ARG C 1 75 ? 18.804  -38.392 10.087  1.00 36.15  ? 74  ARG C CZ  1 
ATOM   1959 N NH1 . ARG C 1 75 ? 18.680  -38.994 11.252  1.00 36.43  ? 74  ARG C NH1 1 
ATOM   1960 N NH2 . ARG C 1 75 ? 19.999  -38.175 9.584   1.00 34.11  ? 74  ARG C NH2 1 
ATOM   1961 N N   . LYS C 1 76 ? 13.154  -35.919 9.832   1.00 33.17  ? 75  LYS C N   1 
ATOM   1962 C CA  . LYS C 1 76 ? 11.872  -35.840 10.515  1.00 35.63  ? 75  LYS C CA  1 
ATOM   1963 C C   . LYS C 1 76 ? 11.911  -34.829 11.657  1.00 34.72  ? 75  LYS C C   1 
ATOM   1964 O O   . LYS C 1 76 ? 12.609  -35.001 12.668  1.00 32.21  ? 75  LYS C O   1 
ATOM   1965 C CB  . LYS C 1 76 ? 11.286  -37.211 10.887  1.00 39.56  ? 75  LYS C CB  1 
ATOM   1966 C CG  . LYS C 1 76 ? 9.787   -37.370 10.612  1.00 45.90  ? 75  LYS C CG  1 
ATOM   1967 C CD  . LYS C 1 76 ? 9.001   -37.730 11.872  1.00 49.44  ? 75  LYS C CD  1 
ATOM   1968 N N   . GLY C 1 77 ? 11.085  -33.788 11.517  1.00 33.43  ? 76  GLY C N   1 
ATOM   1969 C CA  . GLY C 1 77 ? 10.887  -32.894 12.642  1.00 31.37  ? 76  GLY C CA  1 
ATOM   1970 C C   . GLY C 1 77 ? 11.847  -31.707 12.595  1.00 27.29  ? 76  GLY C C   1 
ATOM   1971 O O   . GLY C 1 77 ? 11.688  -30.753 13.352  1.00 32.92  ? 76  GLY C O   1 
ATOM   1972 N N   . PHE C 1 78 ? 12.834  -31.755 11.691  1.00 28.16  ? 77  PHE C N   1 
ATOM   1973 C CA  . PHE C 1 78 ? 13.911  -30.780 11.718  1.00 27.47  ? 77  PHE C CA  1 
ATOM   1974 C C   . PHE C 1 78 ? 13.403  -29.345 11.478  1.00 31.12  ? 77  PHE C C   1 
ATOM   1975 O O   . PHE C 1 78 ? 13.765  -28.404 12.198  1.00 30.68  ? 77  PHE C O   1 
ATOM   1976 C CB  . PHE C 1 78 ? 14.989  -31.176 10.703  1.00 31.20  ? 77  PHE C CB  1 
ATOM   1977 C CG  . PHE C 1 78 ? 16.275  -30.411 10.983  1.00 30.93  ? 77  PHE C CG  1 
ATOM   1978 C CD1 . PHE C 1 78 ? 16.472  -29.141 10.458  1.00 28.15  ? 77  PHE C CD1 1 
ATOM   1979 C CD2 . PHE C 1 78 ? 17.269  -30.956 11.792  1.00 27.83  ? 77  PHE C CD2 1 
ATOM   1980 C CE1 . PHE C 1 78 ? 17.633  -28.423 10.742  1.00 30.24  ? 77  PHE C CE1 1 
ATOM   1981 C CE2 . PHE C 1 78 ? 18.436  -30.236 12.063  1.00 28.52  ? 77  PHE C CE2 1 
ATOM   1982 C CZ  . PHE C 1 78 ? 18.622  -28.982 11.530  1.00 28.14  ? 77  PHE C CZ  1 
ATOM   1983 N N   . ASN C 1 79 ? 12.630  -29.172 10.397  1.00 27.43  ? 78  ASN C N   1 
ATOM   1984 C CA  . ASN C 1 79 ? 12.247  -27.849 9.939   1.00 29.72  ? 78  ASN C CA  1 
ATOM   1985 C C   . ASN C 1 79 ? 11.287  -27.241 10.950  1.00 27.86  ? 78  ASN C C   1 
ATOM   1986 O O   . ASN C 1 79 ? 11.353  -26.050 11.256  1.00 26.86  ? 78  ASN C O   1 
ATOM   1987 C CB  . ASN C 1 79 ? 11.745  -27.882 8.498   1.00 28.85  ? 78  ASN C CB  1 
ATOM   1988 C CG  . ASN C 1 79 ? 12.876  -28.284 7.577   1.00 30.35  ? 78  ASN C CG  1 
ATOM   1989 O OD1 . ASN C 1 79 ? 14.044  -28.024 7.893   1.00 29.12  ? 78  ASN C OD1 1 
ATOM   1990 N ND2 . ASN C 1 79 ? 12.557  -28.847 6.424   1.00 28.20  ? 78  ASN C ND2 1 
ATOM   1991 N N   . GLU C 1 80 ? 10.407  -28.065 11.501  1.00 32.76  ? 79  GLU C N   1 
ATOM   1992 C CA  . GLU C 1 80 ? 9.547   -27.553 12.557  1.00 29.96  ? 79  GLU C CA  1 
ATOM   1993 C C   . GLU C 1 80 ? 10.390  -27.156 13.766  1.00 35.03  ? 79  GLU C C   1 
ATOM   1994 O O   . GLU C 1 80 ? 10.089  -26.176 14.455  1.00 31.81  ? 79  GLU C O   1 
ATOM   1995 C CB  . GLU C 1 80 ? 8.528   -28.627 12.926  1.00 35.61  ? 79  GLU C CB  1 
ATOM   1996 C CG  . GLU C 1 80 ? 7.562   -28.133 13.998  1.00 31.28  ? 79  GLU C CG  1 
ATOM   1997 C CD  . GLU C 1 80 ? 6.358   -29.024 14.197  1.00 44.08  ? 79  GLU C CD  1 
ATOM   1998 O OE1 . GLU C 1 80 ? 6.378   -30.161 13.674  1.00 45.53  ? 79  GLU C OE1 1 
ATOM   1999 O OE2 . GLU C 1 80 ? 5.392   -28.571 14.850  1.00 44.93  ? 79  GLU C OE2 1 
ATOM   2000 N N   . GLY C 1 81 ? 11.456  -27.942 14.033  1.00 31.60  ? 80  GLY C N   1 
ATOM   2001 C CA  . GLY C 1 81 ? 12.400  -27.579 15.079  1.00 29.23  ? 80  GLY C CA  1 
ATOM   2002 C C   . GLY C 1 81 ? 13.032  -26.210 14.844  1.00 31.26  ? 80  GLY C C   1 
ATOM   2003 O O   . GLY C 1 81 ? 13.231  -25.448 15.785  1.00 29.56  ? 80  GLY C O   1 
ATOM   2004 N N   . LEU C 1 82 ? 13.459  -25.938 13.606  1.00 30.22  ? 81  LEU C N   1 
ATOM   2005 C CA  . LEU C 1 82 ? 14.033  -24.628 13.302  1.00 30.13  ? 81  LEU C CA  1 
ATOM   2006 C C   . LEU C 1 82 ? 13.016  -23.508 13.575  1.00 29.12  ? 81  LEU C C   1 
ATOM   2007 O O   . LEU C 1 82 ? 13.400  -22.427 14.048  1.00 29.44  ? 81  LEU C O   1 
ATOM   2008 C CB  . LEU C 1 82 ? 14.530  -24.568 11.857  1.00 32.02  ? 81  LEU C CB  1 
ATOM   2009 C CG  . LEU C 1 82 ? 15.756  -25.409 11.500  1.00 30.77  ? 81  LEU C CG  1 
ATOM   2010 C CD1 . LEU C 1 82 ? 15.940  -25.316 9.987   1.00 30.16  ? 81  LEU C CD1 1 
ATOM   2011 C CD2 . LEU C 1 82 ? 16.989  -24.859 12.161  1.00 26.77  ? 81  LEU C CD2 1 
ATOM   2012 N N   . TRP C 1 83 ? 11.732  -23.745 13.260  1.00 27.72  ? 82  TRP C N   1 
ATOM   2013 C CA  . TRP C 1 83 ? 10.718  -22.721 13.500  1.00 35.49  ? 82  TRP C CA  1 
ATOM   2014 C C   . TRP C 1 83 ? 10.631  -22.417 15.005  1.00 38.30  ? 82  TRP C C   1 
ATOM   2015 O O   . TRP C 1 83 ? 10.706  -21.246 15.421  1.00 35.21  ? 82  TRP C O   1 
ATOM   2016 C CB  . TRP C 1 83 ? 9.353   -23.084 12.892  1.00 33.88  ? 82  TRP C CB  1 
ATOM   2017 C CG  . TRP C 1 83 ? 8.352   -21.961 13.026  1.00 40.98  ? 82  TRP C CG  1 
ATOM   2018 C CD1 . TRP C 1 83 ? 8.122   -20.942 12.140  1.00 38.34  ? 82  TRP C CD1 1 
ATOM   2019 C CD2 . TRP C 1 83 ? 7.488   -21.707 14.158  1.00 40.32  ? 82  TRP C CD2 1 
ATOM   2020 N NE1 . TRP C 1 83 ? 7.168   -20.095 12.625  1.00 36.93  ? 82  TRP C NE1 1 
ATOM   2021 C CE2 . TRP C 1 83 ? 6.760   -20.530 13.858  1.00 39.08  ? 82  TRP C CE2 1 
ATOM   2022 C CE3 . TRP C 1 83 ? 7.252   -22.368 15.377  1.00 35.67  ? 82  TRP C CE3 1 
ATOM   2023 C CZ2 . TRP C 1 83 ? 5.828   -19.996 14.745  1.00 43.12  ? 82  TRP C CZ2 1 
ATOM   2024 C CZ3 . TRP C 1 83 ? 6.334   -21.836 16.259  1.00 41.98  ? 82  TRP C CZ3 1 
ATOM   2025 C CH2 . TRP C 1 83 ? 5.638   -20.661 15.944  1.00 45.65  ? 82  TRP C CH2 1 
ATOM   2026 N N   . GLU C 1 84 ? 10.596  -23.494 15.813  1.00 35.26  ? 83  GLU C N   1 
ATOM   2027 C CA  . GLU C 1 84 ? 10.448  -23.374 17.261  1.00 36.07  ? 83  GLU C CA  1 
ATOM   2028 C C   . GLU C 1 84 ? 11.602  -22.583 17.869  1.00 35.52  ? 83  GLU C C   1 
ATOM   2029 O O   . GLU C 1 84 ? 11.378  -21.696 18.711  1.00 38.63  ? 83  GLU C O   1 
ATOM   2030 C CB  . GLU C 1 84 ? 10.282  -24.720 17.974  1.00 29.50  ? 83  GLU C CB  1 
ATOM   2031 C CG  . GLU C 1 84 ? 9.035   -25.448 17.481  1.00 34.27  ? 83  GLU C CG  1 
ATOM   2032 C CD  . GLU C 1 84 ? 8.895   -26.822 18.083  1.00 37.94  ? 83  GLU C CD  1 
ATOM   2033 O OE1 . GLU C 1 84 ? 9.904   -27.288 18.672  1.00 35.72  ? 83  GLU C OE1 1 
ATOM   2034 O OE2 . GLU C 1 84 ? 7.802   -27.425 17.934  1.00 38.35  ? 83  GLU C OE2 1 
ATOM   2035 N N   . ILE C 1 85 ? 12.837  -22.898 17.465  1.00 33.46  ? 84  ILE C N   1 
ATOM   2036 C CA  . ILE C 1 85 ? 13.987  -22.293 18.128  1.00 34.38  ? 84  ILE C CA  1 
ATOM   2037 C C   . ILE C 1 85 ? 14.092  -20.785 17.869  1.00 36.25  ? 84  ILE C C   1 
ATOM   2038 O O   . ILE C 1 85 ? 14.674  -20.062 18.676  1.00 32.68  ? 84  ILE C O   1 
ATOM   2039 C CB  . ILE C 1 85 ? 15.304  -23.024 17.822  1.00 30.49  ? 84  ILE C CB  1 
ATOM   2040 C CG1 . ILE C 1 85 ? 16.404  -22.549 18.787  1.00 31.29  ? 84  ILE C CG1 1 
ATOM   2041 C CG2 . ILE C 1 85 ? 15.739  -22.886 16.360  1.00 31.13  ? 84  ILE C CG2 1 
ATOM   2042 C CD1 . ILE C 1 85 ? 17.619  -23.463 18.858  1.00 34.98  ? 84  ILE C CD1 1 
ATOM   2043 N N   . GLN C 1 86 ? 13.558  -20.341 16.724  1.00 35.14  ? 85  GLN C N   1 
ATOM   2044 C CA  . GLN C 1 86 ? 13.581  -18.945 16.304  1.00 36.96  ? 85  GLN C CA  1 
ATOM   2045 C C   . GLN C 1 86 ? 12.365  -18.184 16.838  1.00 33.50  ? 85  GLN C C   1 
ATOM   2046 O O   . GLN C 1 86 ? 12.514  -17.038 17.256  1.00 42.60  ? 85  GLN C O   1 
ATOM   2047 C CB  . GLN C 1 86 ? 13.675  -18.869 14.772  1.00 34.39  ? 85  GLN C CB  1 
ATOM   2048 C CG  . GLN C 1 86 ? 13.936  -17.460 14.233  1.00 34.65  ? 85  GLN C CG  1 
ATOM   2049 C CD  . GLN C 1 86 ? 14.390  -17.457 12.782  1.00 35.51  ? 85  GLN C CD  1 
ATOM   2050 O OE1 . GLN C 1 86 ? 14.343  -18.474 12.075  1.00 39.01  ? 85  GLN C OE1 1 
ATOM   2051 N NE2 . GLN C 1 86 ? 14.891  -16.315 12.337  1.00 35.66  ? 85  GLN C NE2 1 
ATOM   2052 N N   . ASN C 1 87 ? 11.204  -18.844 16.867  1.00 36.20  ? 86  ASN C N   1 
ATOM   2053 C CA  . ASN C 1 87 ? 9.890   -18.228 17.030  1.00 45.32  ? 86  ASN C CA  1 
ATOM   2054 C C   . ASN C 1 87 ? 9.211   -18.548 18.369  1.00 47.07  ? 86  ASN C C   1 
ATOM   2055 O O   . ASN C 1 87 ? 8.333   -17.805 18.776  1.00 47.39  ? 86  ASN C O   1 
ATOM   2056 C CB  . ASN C 1 87 ? 8.963   -18.523 15.851  1.00 39.86  ? 86  ASN C CB  1 
ATOM   2057 C CG  . ASN C 1 87 ? 9.549   -17.941 14.586  1.00 44.08  ? 86  ASN C CG  1 
ATOM   2058 O OD1 . ASN C 1 87 ? 9.722   -16.720 14.503  1.00 39.43  ? 86  ASN C OD1 1 
ATOM   2059 N ND2 . ASN C 1 87 ? 9.967   -18.788 13.654  1.00 38.05  ? 86  ASN C ND2 1 
ATOM   2060 N N   . ASN C 1 88 ? 9.554   -19.658 19.038  1.00 46.12  ? 87  ASN C N   1 
ATOM   2061 C CA  . ASN C 1 88 ? 8.834   -20.034 20.257  1.00 41.89  ? 87  ASN C CA  1 
ATOM   2062 C C   . ASN C 1 88 ? 9.752   -20.875 21.146  1.00 40.11  ? 87  ASN C C   1 
ATOM   2063 O O   . ASN C 1 88 ? 9.407   -22.013 21.484  1.00 43.81  ? 87  ASN C O   1 
ATOM   2064 C CB  . ASN C 1 88 ? 7.608   -20.885 19.922  1.00 43.30  ? 87  ASN C CB  1 
ATOM   2065 C CG  . ASN C 1 88 ? 6.545   -20.885 20.996  1.00 51.27  ? 87  ASN C CG  1 
ATOM   2066 O OD1 . ASN C 1 88 ? 6.579   -20.053 21.908  1.00 55.11  ? 87  ASN C OD1 1 
ATOM   2067 N ND2 . ASN C 1 88 ? 5.590   -21.801 20.902  1.00 49.26  ? 87  ASN C ND2 1 
ATOM   2068 N N   . PRO C 1 89 ? 10.960  -20.375 21.494  1.00 39.95  ? 88  PRO C N   1 
ATOM   2069 C CA  . PRO C 1 89 ? 11.993  -21.217 22.100  1.00 42.81  ? 88  PRO C CA  1 
ATOM   2070 C C   . PRO C 1 89 ? 11.747  -21.740 23.513  1.00 48.42  ? 88  PRO C C   1 
ATOM   2071 O O   . PRO C 1 89 ? 12.504  -22.598 23.981  1.00 45.19  ? 88  PRO C O   1 
ATOM   2072 C CB  . PRO C 1 89 ? 13.281  -20.402 22.026  1.00 39.26  ? 88  PRO C CB  1 
ATOM   2073 C CG  . PRO C 1 89 ? 12.826  -18.965 21.856  1.00 39.60  ? 88  PRO C CG  1 
ATOM   2074 C CD  . PRO C 1 89 ? 11.425  -19.002 21.252  1.00 40.32  ? 88  PRO C CD  1 
ATOM   2075 N N   . HIS C 1 90 ? 10.703  -21.211 24.172  1.00 50.18  ? 89  HIS C N   1 
ATOM   2076 C CA  . HIS C 1 90 ? 10.455  -21.521 25.574  1.00 47.51  ? 89  HIS C CA  1 
ATOM   2077 C C   . HIS C 1 90 ? 9.006   -21.942 25.822  1.00 47.96  ? 89  HIS C C   1 
ATOM   2078 O O   . HIS C 1 90 ? 8.568   -22.026 26.967  1.00 52.04  ? 89  HIS C O   1 
ATOM   2079 C CB  . HIS C 1 90 ? 11.054  -20.461 26.508  1.00 45.66  ? 89  HIS C CB  1 
ATOM   2080 C CG  . HIS C 1 90 ? 12.496  -20.082 26.270  1.00 45.24  ? 89  HIS C CG  1 
ATOM   2081 N ND1 . HIS C 1 90 ? 12.849  -18.852 25.755  1.00 45.96  ? 89  HIS C ND1 1 
ATOM   2082 C CD2 . HIS C 1 90 ? 13.664  -20.699 26.527  1.00 45.93  ? 89  HIS C CD2 1 
ATOM   2083 C CE1 . HIS C 1 90 ? 14.176  -18.740 25.682  1.00 42.06  ? 89  HIS C CE1 1 
ATOM   2084 N NE2 . HIS C 1 90 ? 14.693  -19.852 26.155  1.00 46.29  ? 89  HIS C NE2 1 
ATOM   2085 N N   . ALA C 1 91 ? 8.265   -22.283 24.764  1.00 55.39  ? 90  ALA C N   1 
ATOM   2086 C CA  . ALA C 1 91 ? 6.999   -22.987 24.946  1.00 63.86  ? 90  ALA C CA  1 
ATOM   2087 C C   . ALA C 1 91 ? 7.250   -24.334 25.634  1.00 72.51  ? 90  ALA C C   1 
ATOM   2088 O O   . ALA C 1 91 ? 8.395   -24.663 25.943  1.00 74.33  ? 90  ALA C O   1 
ATOM   2089 C CB  . ALA C 1 91 ? 6.266   -23.132 23.624  1.00 61.74  ? 90  ALA C CB  1 
ATOM   2090 N N   . SER C 1 92 ? 6.180   -25.114 25.863  1.00 78.78  ? 91  SER C N   1 
ATOM   2091 C CA  . SER C 1 92 ? 6.238   -26.290 26.725  1.00 77.44  ? 91  SER C CA  1 
ATOM   2092 C C   . SER C 1 92 ? 6.340   -27.595 25.936  1.00 73.57  ? 91  SER C C   1 
ATOM   2093 O O   . SER C 1 92 ? 6.966   -28.546 26.401  1.00 66.94  ? 91  SER C O   1 
ATOM   2094 C CB  . SER C 1 92 ? 5.053   -26.334 27.664  1.00 79.85  ? 91  SER C CB  1 
ATOM   2095 O OG  . SER C 1 92 ? 5.143   -25.302 28.634  1.00 83.41  ? 91  SER C OG  1 
ATOM   2096 N N   . TYR C 1 93 ? 5.665   -27.643 24.780  1.00 78.98  ? 92  TYR C N   1 
ATOM   2097 C CA  . TYR C 1 93 ? 5.533   -28.832 23.946  1.00 78.49  ? 92  TYR C CA  1 
ATOM   2098 C C   . TYR C 1 93 ? 5.517   -30.093 24.825  1.00 81.00  ? 92  TYR C C   1 
ATOM   2099 O O   . TYR C 1 93 ? 4.554   -30.893 24.728  1.00 88.49  ? 92  TYR C O   1 
ATOM   2100 C CB  . TYR C 1 93 ? 6.651   -28.914 22.902  1.00 76.22  ? 92  TYR C CB  1 
ATOM   2101 C CG  . TYR C 1 93 ? 7.037   -27.606 22.216  1.00 70.15  ? 92  TYR C CG  1 
ATOM   2102 C CD1 . TYR C 1 93 ? 6.358   -27.153 21.084  1.00 60.72  ? 92  TYR C CD1 1 
ATOM   2103 C CD2 . TYR C 1 93 ? 8.094   -26.831 22.697  1.00 62.39  ? 92  TYR C CD2 1 
ATOM   2104 C CE1 . TYR C 1 93 ? 6.706   -25.963 20.465  1.00 55.89  ? 92  TYR C CE1 1 
ATOM   2105 C CE2 . TYR C 1 93 ? 8.461   -25.649 22.071  1.00 59.04  ? 92  TYR C CE2 1 
ATOM   2106 C CZ  . TYR C 1 93 ? 7.768   -25.215 20.953  1.00 60.59  ? 92  TYR C CZ  1 
ATOM   2107 O OH  . TYR C 1 93 ? 8.135   -24.035 20.357  1.00 61.50  ? 92  TYR C OH  1 
HETATM 2108 S S   . SO4 D 2 .  ? 1.023   -33.630 1.735   1.00 98.95  ? 101 SO4 A S   1 
HETATM 2109 O O1  . SO4 D 2 .  ? 1.576   -34.374 0.629   1.00 79.50  ? 101 SO4 A O1  1 
HETATM 2110 O O2  . SO4 D 2 .  ? 1.038   -32.223 1.426   1.00 100.07 ? 101 SO4 A O2  1 
HETATM 2111 O O3  . SO4 D 2 .  ? -0.336  -34.055 1.971   1.00 106.06 ? 101 SO4 A O3  1 
HETATM 2112 O O4  . SO4 D 2 .  ? 1.810   -33.864 2.914   1.00 92.50  ? 101 SO4 A O4  1 
HETATM 2113 S S   . SO4 E 2 .  ? -9.554  -24.618 1.317   1.00 96.29  ? 102 SO4 A S   1 
HETATM 2114 O O1  . SO4 E 2 .  ? -9.572  -24.229 -0.067  1.00 92.66  ? 102 SO4 A O1  1 
HETATM 2115 O O2  . SO4 E 2 .  ? -9.669  -23.446 2.144   1.00 93.93  ? 102 SO4 A O2  1 
HETATM 2116 O O3  . SO4 E 2 .  ? -10.654 -25.517 1.567   1.00 105.76 ? 102 SO4 A O3  1 
HETATM 2117 O O4  . SO4 E 2 .  ? -8.319  -25.289 1.626   1.00 99.06  ? 102 SO4 A O4  1 
HETATM 2118 C C1  . EDO F 3 .  ? 13.792  -19.527 -7.404  1.00 41.38  ? 103 EDO A C1  1 
HETATM 2119 O O1  . EDO F 3 .  ? 15.014  -18.788 -7.286  1.00 33.96  ? 103 EDO A O1  1 
HETATM 2120 C C2  . EDO F 3 .  ? 12.866  -19.052 -8.497  1.00 39.22  ? 103 EDO A C2  1 
HETATM 2121 O O2  . EDO F 3 .  ? 12.491  -17.696 -8.328  1.00 33.45  ? 103 EDO A O2  1 
HETATM 2122 S S   . SO4 G 2 .  ? 8.897   -29.457 5.819   1.00 58.82  ? 104 SO4 A S   1 
HETATM 2123 O O1  . SO4 G 2 .  ? 9.698   -28.579 5.031   1.00 54.87  ? 104 SO4 A O1  1 
HETATM 2124 O O2  . SO4 G 2 .  ? 8.529   -30.607 5.013   1.00 65.21  ? 104 SO4 A O2  1 
HETATM 2125 O O3  . SO4 G 2 .  ? 9.646   -29.899 6.976   1.00 64.50  ? 104 SO4 A O3  1 
HETATM 2126 O O4  . SO4 G 2 .  ? 7.700   -28.775 6.239   1.00 68.91  ? 104 SO4 A O4  1 
HETATM 2127 S S   . SO4 H 2 .  ? 7.316   -8.601  -24.802 1.00 70.70  ? 101 SO4 B S   1 
HETATM 2128 O O1  . SO4 H 2 .  ? 8.475   -8.722  -25.654 1.00 48.90  ? 101 SO4 B O1  1 
HETATM 2129 O O2  . SO4 H 2 .  ? 6.160   -9.178  -25.447 1.00 50.68  ? 101 SO4 B O2  1 
HETATM 2130 O O3  . SO4 H 2 .  ? 7.492   -9.303  -23.534 1.00 45.41  ? 101 SO4 B O3  1 
HETATM 2131 O O4  . SO4 H 2 .  ? 7.138   -7.180  -24.563 1.00 61.60  ? 101 SO4 B O4  1 
HETATM 2132 S S   . SO4 I 2 .  ? 14.349  -27.061 -26.336 1.00 59.28  ? 102 SO4 B S   1 
HETATM 2133 O O1  . SO4 I 2 .  ? 15.740  -26.840 -26.103 1.00 52.60  ? 102 SO4 B O1  1 
HETATM 2134 O O2  . SO4 I 2 .  ? 14.178  -28.337 -26.979 1.00 65.79  ? 102 SO4 B O2  1 
HETATM 2135 O O3  . SO4 I 2 .  ? 13.644  -27.063 -25.080 1.00 64.90  ? 102 SO4 B O3  1 
HETATM 2136 O O4  . SO4 I 2 .  ? 13.813  -26.021 -27.183 1.00 60.62  ? 102 SO4 B O4  1 
HETATM 2137 N N1  . LJR J 4 .  ? 17.000  -15.535 -25.968 0.66 44.49  ? 103 LJR B N1  1 
HETATM 2138 C C4  . LJR J 4 .  ? 18.437  -15.963 -21.160 0.66 48.93  ? 103 LJR B C4  1 
HETATM 2139 C C5  . LJR J 4 .  ? 19.313  -16.744 -20.186 0.66 46.19  ? 103 LJR B C5  1 
HETATM 2140 C C6  . LJR J 4 .  ? 20.733  -16.211 -20.163 0.66 50.14  ? 103 LJR B C6  1 
HETATM 2141 C C7  . LJR J 4 .  ? 21.345  -16.239 -21.551 0.66 48.88  ? 103 LJR B C7  1 
HETATM 2142 C C8  . LJR J 4 .  ? 20.331  -16.710 -22.580 0.66 49.87  ? 103 LJR B C8  1 
HETATM 2143 C C1  . LJR J 4 .  ? 17.404  -16.897 -26.296 0.66 42.81  ? 103 LJR B C1  1 
HETATM 2144 S S1  . LJR J 4 .  ? 17.063  -15.072 -24.433 0.66 51.21  ? 103 LJR B S1  1 
HETATM 2145 O O1  . LJR J 4 .  ? 17.708  -13.792 -24.403 0.66 39.27  ? 103 LJR B O1  1 
HETATM 2146 O O2  . LJR J 4 .  ? 15.751  -15.201 -23.893 0.66 42.48  ? 103 LJR B O2  1 
HETATM 2147 C C2  . LJR J 4 .  ? 18.094  -16.289 -23.644 0.66 43.06  ? 103 LJR B C2  1 
HETATM 2148 C C3  . LJR J 4 .  ? 19.064  -15.869 -22.544 0.66 49.50  ? 103 LJR B C3  1 
HETATM 2149 C C1  . EDO K 3 .  ? 16.660  -36.281 16.489  1.00 37.88  ? 101 EDO C C1  1 
HETATM 2150 O O1  . EDO K 3 .  ? 15.616  -36.901 15.762  1.00 47.98  ? 101 EDO C O1  1 
HETATM 2151 C C2  . EDO K 3 .  ? 16.217  -35.274 17.482  1.00 35.22  ? 101 EDO C C2  1 
HETATM 2152 O O2  . EDO K 3 .  ? 15.227  -35.779 18.328  1.00 29.59  ? 101 EDO C O2  1 
HETATM 2153 S S   . SO4 L 2 .  ? 28.969  -38.334 12.283  1.00 86.16  ? 102 SO4 C S   1 
HETATM 2154 O O1  . SO4 L 2 .  ? 29.987  -37.338 12.052  1.00 91.38  ? 102 SO4 C O1  1 
HETATM 2155 O O2  . SO4 L 2 .  ? 27.818  -38.049 11.468  1.00 70.59  ? 102 SO4 C O2  1 
HETATM 2156 O O3  . SO4 L 2 .  ? 29.473  -39.636 11.944  1.00 73.85  ? 102 SO4 C O3  1 
HETATM 2157 O O4  . SO4 L 2 .  ? 28.602  -38.318 13.673  1.00 95.14  ? 102 SO4 C O4  1 
HETATM 2158 O O   . HOH M 5 .  ? 8.350   -32.365 4.052   1.00 56.66  ? 201 HOH A O   1 
HETATM 2159 O O   . HOH M 5 .  ? -2.504  -30.919 -3.757  1.00 65.35  ? 202 HOH A O   1 
HETATM 2160 O O   . HOH M 5 .  ? 5.516   -29.022 6.889   1.00 53.62  ? 203 HOH A O   1 
HETATM 2161 O O   . HOH M 5 .  ? -5.680  -13.402 -16.411 1.00 48.51  ? 204 HOH A O   1 
HETATM 2162 O O   . HOH M 5 .  ? 3.700   -34.685 4.073   1.00 56.66  ? 205 HOH A O   1 
HETATM 2163 O O   . HOH M 5 .  ? 0.161   -33.658 4.613   1.00 49.34  ? 206 HOH A O   1 
HETATM 2164 O O   . HOH M 5 .  ? 1.071   -24.625 13.699  1.00 61.36  ? 207 HOH A O   1 
HETATM 2165 O O   . HOH M 5 .  ? 10.834  -29.628 3.039   1.00 48.46  ? 208 HOH A O   1 
HETATM 2166 O O   . HOH M 5 .  ? -3.809  -10.881 6.826   1.00 40.95  ? 209 HOH A O   1 
HETATM 2167 O O   . HOH M 5 .  ? 12.749  -9.480  -7.312  1.00 46.26  ? 210 HOH A O   1 
HETATM 2168 O O   . HOH M 5 .  ? 7.690   -1.918  -0.711  1.00 66.55  ? 211 HOH A O   1 
HETATM 2169 O O   . HOH M 5 .  ? 8.834   -18.031 -11.038 1.00 32.78  ? 212 HOH A O   1 
HETATM 2170 O O   . HOH M 5 .  ? 13.870  -15.677 -9.180  1.00 34.50  ? 213 HOH A O   1 
HETATM 2171 O O   . HOH M 5 .  ? 12.917  -11.877 7.903   1.00 59.65  ? 214 HOH A O   1 
HETATM 2172 O O   . HOH M 5 .  ? 0.574   -10.685 -15.602 1.00 52.88  ? 215 HOH A O   1 
HETATM 2173 O O   . HOH M 5 .  ? 15.739  -24.477 1.941   1.00 43.14  ? 216 HOH A O   1 
HETATM 2174 O O   . HOH M 5 .  ? 16.907  -18.154 -9.631  1.00 44.21  ? 217 HOH A O   1 
HETATM 2175 O O   . HOH M 5 .  ? -0.879  -29.406 9.749   1.00 57.19  ? 218 HOH A O   1 
HETATM 2176 O O   . HOH M 5 .  ? -8.697  -21.097 -1.164  1.00 47.06  ? 219 HOH A O   1 
HETATM 2177 O O   . HOH M 5 .  ? 2.477   -10.012 -13.227 1.00 55.68  ? 220 HOH A O   1 
HETATM 2178 O O   . HOH M 5 .  ? 10.618  -5.190  -7.696  1.00 31.57  ? 221 HOH A O   1 
HETATM 2179 O O   . HOH M 5 .  ? -4.440  -21.090 6.197   1.00 41.06  ? 222 HOH A O   1 
HETATM 2180 O O   . HOH M 5 .  ? 19.600  -15.530 7.249   1.00 30.49  ? 223 HOH A O   1 
HETATM 2181 O O   . HOH M 5 .  ? 6.877   -10.515 -12.109 1.00 44.54  ? 224 HOH A O   1 
HETATM 2182 O O   . HOH M 5 .  ? -2.463  3.215   -1.931  1.00 40.47  ? 225 HOH A O   1 
HETATM 2183 O O   . HOH M 5 .  ? 2.321   -25.100 -10.091 1.00 41.96  ? 226 HOH A O   1 
HETATM 2184 O O   . HOH M 5 .  ? -7.592  -21.238 -5.078  1.00 73.31  ? 227 HOH A O   1 
HETATM 2185 O O   . HOH M 5 .  ? 11.222  -12.018 5.862   1.00 33.87  ? 228 HOH A O   1 
HETATM 2186 O O   . HOH M 5 .  ? 4.720   -1.478  -6.315  1.00 35.42  ? 229 HOH A O   1 
HETATM 2187 O O   . HOH M 5 .  ? 8.045   -17.799 -15.723 1.00 46.69  ? 230 HOH A O   1 
HETATM 2188 O O   . HOH M 5 .  ? -8.124  -15.697 -1.041  1.00 32.95  ? 231 HOH A O   1 
HETATM 2189 O O   . HOH M 5 .  ? 9.474   -6.095  -1.663  1.00 37.78  ? 232 HOH A O   1 
HETATM 2190 O O   . HOH M 5 .  ? 4.338   -3.451  -3.257  1.00 33.14  ? 233 HOH A O   1 
HETATM 2191 O O   . HOH M 5 .  ? 4.432   -7.861  1.044   1.00 34.20  ? 234 HOH A O   1 
HETATM 2192 O O   . HOH M 5 .  ? 10.875  -23.599 9.876   1.00 38.49  ? 235 HOH A O   1 
HETATM 2193 O O   . HOH M 5 .  ? -0.836  -20.940 6.939   1.00 31.37  ? 236 HOH A O   1 
HETATM 2194 O O   . HOH M 5 .  ? 17.083  -12.891 1.348   1.00 20.94  ? 237 HOH A O   1 
HETATM 2195 O O   . HOH M 5 .  ? -7.940  -17.267 6.673   1.00 45.61  ? 238 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? 1.673   0.660   -7.428  1.00 43.33  ? 239 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? -5.322  -25.672 -5.705  1.00 53.76  ? 240 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? 8.443   -17.795 8.880   1.00 44.67  ? 241 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? 11.324  -12.247 -6.172  1.00 26.54  ? 242 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? 3.173   -29.655 -0.520  1.00 37.91  ? 243 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? -1.918  -21.970 -0.654  1.00 25.33  ? 244 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 1.613   -10.542 11.699  1.00 36.17  ? 245 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? -5.920  -19.547 -5.702  1.00 39.42  ? 246 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 2.021   -25.092 -6.413  1.00 58.81  ? 247 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? -6.280  -11.351 -11.349 1.00 37.21  ? 248 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? -5.813  -15.802 -8.099  1.00 29.85  ? 249 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 16.387  -11.743 -17.191 1.00 48.96  ? 250 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? -8.233  -16.639 2.149   1.00 45.62  ? 251 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 0.855   -17.872 -18.865 1.00 55.65  ? 252 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 15.609  -11.979 -5.317  1.00 32.61  ? 253 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 9.920   -13.050 9.706   1.00 44.78  ? 254 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 13.109  -11.966 -4.258  1.00 21.47  ? 255 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 1.847   -4.710  -10.336 1.00 41.36  ? 256 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 0.108   -23.344 9.157   1.00 44.03  ? 257 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? -1.302  -11.803 11.295  1.00 40.22  ? 258 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 9.380   -30.484 9.789   1.00 35.23  ? 259 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 7.665   -7.863  1.320   1.00 29.90  ? 260 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 14.299  -29.355 4.050   1.00 45.89  ? 261 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? -11.351 -16.089 -3.777  1.00 49.79  ? 262 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 12.697  -28.420 -4.599  1.00 59.52  ? 263 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -6.203  -12.801 6.739   1.00 39.68  ? 264 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 11.235  -5.886  -3.944  1.00 43.16  ? 265 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 2.328   -6.169  5.438   1.00 36.41  ? 266 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 4.956   -7.556  4.013   1.00 35.14  ? 267 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 12.714  -15.337 -11.974 1.00 53.26  ? 268 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 6.450   -15.901 -14.860 1.00 57.65  ? 269 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 8.648   -16.258 -13.240 1.00 37.83  ? 270 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 22.023  -16.650 -0.458  1.00 41.99  ? 271 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 6.208   -5.810  0.530   1.00 49.21  ? 272 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -3.972  -7.911  10.483  1.00 46.61  ? 273 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 15.137  -28.223 -0.792  1.00 55.64  ? 274 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -6.294  -26.654 3.453   1.00 48.08  ? 275 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 10.948  -7.864  0.365   1.00 25.61  ? 276 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 12.606  -13.374 -8.501  1.00 38.08  ? 277 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? -1.699  -7.228  11.352  1.00 60.02  ? 278 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 21.209  -16.610 -3.538  1.00 29.93  ? 279 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 9.603   -20.281 -18.372 1.00 40.72  ? 280 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? -0.720  -20.774 10.942  1.00 90.22  ? 281 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? -7.388  -11.479 -8.061  1.00 29.54  ? 282 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 10.687  -27.903 -7.168  1.00 51.70  ? 283 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 14.776  -13.365 10.724  1.00 47.25  ? 284 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -8.293  -19.581 -3.400  1.00 40.47  ? 285 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 8.616   -9.046  -13.703 1.00 43.94  ? 286 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -4.186  -26.900 6.928   1.00 53.34  ? 287 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? -0.125  -27.796 -7.272  1.00 66.47  ? 288 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 16.617  -9.769  -9.723  1.00 48.22  ? 289 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -7.281  -14.022 -9.182  1.00 44.95  ? 290 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 11.726  -21.003 10.709  1.00 38.31  ? 291 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? -5.874  -23.389 -7.219  1.00 49.11  ? 292 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? 10.746  -2.002  -0.957  1.00 55.83  ? 293 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? -10.394 -28.185 -2.056  1.00 56.51  ? 294 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 1.089   -7.672  -13.101 1.00 48.39  ? 295 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -11.072 -13.329 -2.700  1.00 59.21  ? 296 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -6.391  -22.891 5.525   1.00 53.28  ? 297 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 8.003   -8.320  4.479   1.00 39.53  ? 298 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 4.507   -9.674  -11.505 1.00 47.77  ? 299 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 5.997   -3.215  1.124   1.00 51.08  ? 300 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 7.344   -30.744 -2.209  1.00 65.81  ? 301 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? -7.178  -19.162 8.564   1.00 51.52  ? 302 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 8.815   -22.371 -19.210 1.00 51.14  ? 303 HOH A O   1 
HETATM 2261 O O   . HOH N 5 .  ? 30.750  -8.541  -29.782 1.00 64.21  ? 201 HOH B O   1 
HETATM 2262 O O   . HOH N 5 .  ? 6.541   -12.391 -25.912 1.00 40.87  ? 202 HOH B O   1 
HETATM 2263 O O   . HOH N 5 .  ? 29.912  -12.811 -45.193 1.00 58.98  ? 203 HOH B O   1 
HETATM 2264 O O   . HOH N 5 .  ? 19.825  -22.147 -22.996 1.00 58.00  ? 204 HOH B O   1 
HETATM 2265 O O   . HOH N 5 .  ? 27.711  -8.220  -28.767 1.00 42.04  ? 205 HOH B O   1 
HETATM 2266 O O   . HOH N 5 .  ? 24.825  -5.382  -29.617 1.00 37.28  ? 206 HOH B O   1 
HETATM 2267 O O   . HOH N 5 .  ? 24.230  -1.808  -36.040 1.00 57.45  ? 207 HOH B O   1 
HETATM 2268 O O   . HOH N 5 .  ? 9.931   -11.442 -37.877 1.00 59.78  ? 208 HOH B O   1 
HETATM 2269 O O   . HOH N 5 .  ? 25.840  -4.826  -33.364 1.00 49.42  ? 209 HOH B O   1 
HETATM 2270 O O   . HOH N 5 .  ? 30.269  -19.690 -40.103 1.00 40.39  ? 210 HOH B O   1 
HETATM 2271 O O   . HOH N 5 .  ? 25.920  -0.600  -28.996 1.00 47.74  ? 211 HOH B O   1 
HETATM 2272 O O   . HOH N 5 .  ? 17.554  -15.633 -45.540 1.00 42.45  ? 212 HOH B O   1 
HETATM 2273 O O   . HOH N 5 .  ? 13.028  -4.782  -41.667 1.00 63.28  ? 213 HOH B O   1 
HETATM 2274 O O   . HOH N 5 .  ? 25.310  -6.130  -35.675 1.00 44.02  ? 214 HOH B O   1 
HETATM 2275 O O   . HOH N 5 .  ? 10.190  -19.644 -42.900 1.00 56.15  ? 215 HOH B O   1 
HETATM 2276 O O   . HOH N 5 .  ? 27.578  -17.837 -24.964 1.00 45.87  ? 216 HOH B O   1 
HETATM 2277 O O   . HOH N 5 .  ? 20.689  -3.214  -23.094 1.00 67.39  ? 217 HOH B O   1 
HETATM 2278 O O   . HOH N 5 .  ? 22.414  -23.393 -28.754 1.00 39.98  ? 218 HOH B O   1 
HETATM 2279 O O   . HOH N 5 .  ? 34.610  -23.168 -30.010 1.00 59.54  ? 219 HOH B O   1 
HETATM 2280 O O   . HOH N 5 .  ? 10.314  -16.889 -44.034 1.00 53.97  ? 220 HOH B O   1 
HETATM 2281 O O   . HOH N 5 .  ? 23.354  -2.497  -28.892 1.00 39.23  ? 221 HOH B O   1 
HETATM 2282 O O   . HOH N 5 .  ? 32.572  -18.534 -41.891 1.00 54.60  ? 222 HOH B O   1 
HETATM 2283 O O   . HOH N 5 .  ? 18.171  -0.533  -38.217 1.00 28.91  ? 223 HOH B O   1 
HETATM 2284 O O   . HOH N 5 .  ? 10.551  -18.993 -32.842 1.00 29.77  ? 224 HOH B O   1 
HETATM 2285 O O   . HOH N 5 .  ? 12.774  -22.223 -20.624 1.00 63.51  ? 225 HOH B O   1 
HETATM 2286 O O   . HOH N 5 .  ? 16.664  -19.303 -28.653 1.00 25.22  ? 226 HOH B O   1 
HETATM 2287 O O   . HOH N 5 .  ? 21.410  -6.567  -42.273 1.00 45.24  ? 227 HOH B O   1 
HETATM 2288 O O   . HOH N 5 .  ? 21.078  -13.621 -42.369 1.00 38.84  ? 228 HOH B O   1 
HETATM 2289 O O   . HOH N 5 .  ? 8.437   -27.960 -38.198 1.00 57.97  ? 229 HOH B O   1 
HETATM 2290 O O   . HOH N 5 .  ? 26.084  -23.124 -30.913 1.00 36.73  ? 230 HOH B O   1 
HETATM 2291 O O   . HOH N 5 .  ? 8.548   -8.755  -16.531 1.00 43.51  ? 231 HOH B O   1 
HETATM 2292 O O   . HOH N 5 .  ? 20.779  -26.773 -30.386 1.00 60.63  ? 232 HOH B O   1 
HETATM 2293 O O   . HOH N 5 .  ? 27.059  -10.574 -28.630 1.00 46.19  ? 233 HOH B O   1 
HETATM 2294 O O   . HOH N 5 .  ? 7.620   -18.627 -31.482 1.00 44.17  ? 234 HOH B O   1 
HETATM 2295 O O   . HOH N 5 .  ? 5.989   -7.290  -32.453 1.00 47.41  ? 235 HOH B O   1 
HETATM 2296 O O   . HOH N 5 .  ? 23.793  -4.306  -36.578 1.00 28.40  ? 236 HOH B O   1 
HETATM 2297 O O   . HOH N 5 .  ? 19.679  -25.637 -34.015 1.00 40.66  ? 237 HOH B O   1 
HETATM 2298 O O   . HOH N 5 .  ? 14.426  -6.540  -41.099 1.00 43.87  ? 238 HOH B O   1 
HETATM 2299 O O   . HOH N 5 .  ? 21.694  3.653   -32.489 1.00 41.47  ? 239 HOH B O   1 
HETATM 2300 O O   . HOH N 5 .  ? 20.591  -10.171 -42.728 1.00 34.10  ? 240 HOH B O   1 
HETATM 2301 O O   . HOH N 5 .  ? 17.318  -19.723 -41.964 1.00 71.18  ? 241 HOH B O   1 
HETATM 2302 O O   . HOH N 5 .  ? 1.642   -12.737 -28.472 1.00 47.01  ? 242 HOH B O   1 
HETATM 2303 O O   . HOH N 5 .  ? 7.622   -12.674 -38.889 1.00 61.27  ? 243 HOH B O   1 
HETATM 2304 O O   . HOH N 5 .  ? 18.469  -3.659  -22.056 1.00 55.76  ? 244 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 7.340   -8.139  -20.737 1.00 50.61  ? 245 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 18.310  -25.999 -28.740 1.00 41.48  ? 246 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 3.099   -8.341  -27.035 1.00 57.54  ? 247 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 17.046  -9.691  -43.617 1.00 55.71  ? 248 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 7.240   -19.185 -34.567 1.00 50.94  ? 249 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 18.234  4.457   -34.315 1.00 39.97  ? 250 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 23.791  -11.649 -21.646 1.00 47.45  ? 251 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 14.374  -24.733 -40.468 1.00 53.92  ? 252 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 7.523   -23.309 -24.014 1.00 52.28  ? 253 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 24.749  -7.481  -42.520 1.00 60.11  ? 254 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 31.965  -21.292 -38.121 1.00 42.89  ? 255 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 10.319  -21.770 -32.649 1.00 36.64  ? 256 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 6.240   -20.444 -24.986 1.00 46.10  ? 257 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 27.801  -24.858 -34.949 1.00 35.56  ? 258 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 39.338  -13.209 -39.359 1.00 77.14  ? 259 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 15.153  -8.261  -42.963 1.00 46.64  ? 260 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 9.898   -6.065  -40.920 1.00 53.16  ? 261 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 31.589  -11.983 -37.948 1.00 62.29  ? 262 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 20.082  3.772   -32.939 1.00 37.85  ? 263 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 12.896  -20.368 -19.688 1.00 51.92  ? 264 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 16.724  -25.702 -20.858 1.00 72.31  ? 265 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 17.339  -0.446  -25.339 1.00 52.10  ? 266 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 15.535  -22.023 -41.772 1.00 56.80  ? 267 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 7.541   -21.572 -29.826 1.00 42.21  ? 268 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 7.214   -9.828  -18.513 1.00 48.60  ? 269 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 19.345  -8.495  -43.625 1.00 44.13  ? 270 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 16.792  3.448   -26.442 1.00 68.63  ? 271 HOH B O   1 
HETATM 2332 O O   . HOH O 5 .  ? 19.985  -19.739 29.737  1.00 58.94  ? 201 HOH C O   1 
HETATM 2333 O O   . HOH O 5 .  ? 26.297  -37.424 9.956   1.00 52.91  ? 202 HOH C O   1 
HETATM 2334 O O   . HOH O 5 .  ? 26.276  -39.172 12.705  1.00 36.73  ? 203 HOH C O   1 
HETATM 2335 O O   . HOH O 5 .  ? 7.378   -31.514 12.117  1.00 47.08  ? 204 HOH C O   1 
HETATM 2336 O O   . HOH O 5 .  ? 9.016   -36.843 18.464  1.00 54.11  ? 205 HOH C O   1 
HETATM 2337 O O   . HOH O 5 .  ? 12.289  -28.199 28.142  1.00 50.40  ? 206 HOH C O   1 
HETATM 2338 O O   . HOH O 5 .  ? 5.555   -26.716 16.548  1.00 40.58  ? 207 HOH C O   1 
HETATM 2339 O O   . HOH O 5 .  ? 19.049  -20.300 10.517  1.00 45.48  ? 208 HOH C O   1 
HETATM 2340 O O   . HOH O 5 .  ? 29.922  -40.419 9.534   1.00 39.34  ? 209 HOH C O   1 
HETATM 2341 O O   . HOH O 5 .  ? 22.773  -41.467 18.492  1.00 41.93  ? 210 HOH C O   1 
HETATM 2342 O O   . HOH O 5 .  ? 17.332  -17.047 14.937  1.00 49.21  ? 211 HOH C O   1 
HETATM 2343 O O   . HOH O 5 .  ? 13.933  -37.077 13.582  1.00 45.01  ? 212 HOH C O   1 
HETATM 2344 O O   . HOH O 5 .  ? 30.040  -31.232 15.743  1.00 51.41  ? 213 HOH C O   1 
HETATM 2345 O O   . HOH O 5 .  ? 19.870  -41.902 12.190  1.00 29.86  ? 214 HOH C O   1 
HETATM 2346 O O   . HOH O 5 .  ? 25.118  -31.262 10.780  1.00 35.71  ? 215 HOH C O   1 
HETATM 2347 O O   . HOH O 5 .  ? 14.951  -21.139 12.333  1.00 38.72  ? 216 HOH C O   1 
HETATM 2348 O O   . HOH O 5 .  ? 27.961  -37.205 15.993  1.00 42.16  ? 217 HOH C O   1 
HETATM 2349 O O   . HOH O 5 .  ? 12.637  -31.509 8.201   1.00 34.05  ? 218 HOH C O   1 
HETATM 2350 O O   . HOH O 5 .  ? 30.368  -35.717 28.511  1.00 49.97  ? 219 HOH C O   1 
HETATM 2351 O O   . HOH O 5 .  ? 15.353  -17.510 19.260  1.00 41.81  ? 220 HOH C O   1 
HETATM 2352 O O   . HOH O 5 .  ? 21.903  -34.311 16.577  1.00 25.90  ? 221 HOH C O   1 
HETATM 2353 O O   . HOH O 5 .  ? 20.753  -28.580 8.460   1.00 35.71  ? 222 HOH C O   1 
HETATM 2354 O O   . HOH O 5 .  ? 14.491  -39.094 16.964  1.00 56.41  ? 223 HOH C O   1 
HETATM 2355 O O   . HOH O 5 .  ? 6.773   -17.939 10.965  1.00 36.81  ? 224 HOH C O   1 
HETATM 2356 O O   . HOH O 5 .  ? 25.499  -33.514 34.720  1.00 52.99  ? 225 HOH C O   1 
HETATM 2357 O O   . HOH O 5 .  ? 31.632  -43.122 12.078  1.00 53.64  ? 226 HOH C O   1 
HETATM 2358 O O   . HOH O 5 .  ? 22.109  -28.523 11.014  1.00 31.68  ? 227 HOH C O   1 
HETATM 2359 O O   . HOH O 5 .  ? 18.066  -40.884 38.048  1.00 58.07  ? 228 HOH C O   1 
HETATM 2360 O O   . HOH O 5 .  ? 27.581  -15.127 12.807  1.00 50.46  ? 229 HOH C O   1 
HETATM 2361 O O   . HOH O 5 .  ? 31.768  -33.468 25.776  1.00 48.37  ? 230 HOH C O   1 
HETATM 2362 O O   . HOH O 5 .  ? 31.088  -39.758 27.136  1.00 45.17  ? 231 HOH C O   1 
HETATM 2363 O O   . HOH O 5 .  ? 25.776  -17.590 13.799  1.00 53.40  ? 232 HOH C O   1 
HETATM 2364 O O   . HOH O 5 .  ? 29.751  -39.655 31.336  1.00 37.92  ? 233 HOH C O   1 
HETATM 2365 O O   . HOH O 5 .  ? 20.590  -39.841 26.251  1.00 40.91  ? 234 HOH C O   1 
HETATM 2366 O O   . HOH O 5 .  ? 25.337  -39.630 20.095  1.00 33.46  ? 235 HOH C O   1 
HETATM 2367 O O   . HOH O 5 .  ? 22.713  -18.468 21.637  1.00 60.58  ? 236 HOH C O   1 
HETATM 2368 O O   . HOH O 5 .  ? 16.245  -37.736 20.233  1.00 52.35  ? 237 HOH C O   1 
HETATM 2369 O O   . HOH O 5 .  ? 30.353  -17.492 9.607   1.00 47.65  ? 238 HOH C O   1 
HETATM 2370 O O   . HOH O 5 .  ? 9.144   -18.788 23.626  1.00 50.35  ? 239 HOH C O   1 
HETATM 2371 O O   . HOH O 5 .  ? 18.921  -26.776 2.941   1.00 48.98  ? 240 HOH C O   1 
HETATM 2372 O O   . HOH O 5 .  ? 19.735  -18.962 24.855  1.00 47.66  ? 241 HOH C O   1 
HETATM 2373 O O   . HOH O 5 .  ? 20.907  -29.439 4.472   1.00 59.80  ? 242 HOH C O   1 
HETATM 2374 O O   . HOH O 5 .  ? 14.169  -38.838 9.597   1.00 57.22  ? 243 HOH C O   1 
HETATM 2375 O O   . HOH O 5 .  ? 25.336  -17.712 21.113  1.00 72.31  ? 244 HOH C O   1 
HETATM 2376 O O   . HOH O 5 .  ? 27.154  -38.103 24.974  1.00 55.55  ? 245 HOH C O   1 
HETATM 2377 O O   . HOH O 5 .  ? 29.429  -25.413 32.796  1.00 58.49  ? 246 HOH C O   1 
HETATM 2378 O O   . HOH O 5 .  ? 31.083  -43.642 15.968  1.00 56.18  ? 247 HOH C O   1 
HETATM 2379 O O   . HOH O 5 .  ? 4.893   -23.984 18.511  1.00 55.77  ? 248 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 16.814  -38.005 28.526  1.00 60.95  ? 249 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 30.028  -32.601 18.194  1.00 50.83  ? 250 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 20.006  -13.033 13.453  1.00 50.50  ? 251 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 12.878  -22.871 27.847  1.00 69.58  ? 252 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 2.289   -28.933 13.192  1.00 55.47  ? 253 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 25.678  -14.004 11.032  1.00 50.72  ? 254 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 28.954  -41.645 27.103  1.00 40.37  ? 255 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 32.020  -39.194 29.762  1.00 60.36  ? 256 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 33.199  -24.272 31.437  1.00 55.69  ? 257 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 33.396  -44.463 15.244  1.00 43.43  ? 258 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 15.610  -42.042 8.216   1.00 56.86  ? 259 HOH C O   1 
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