data_7HH0
# 
_entry.id   7HH0 
# 
_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   7HH0         pdb_00007hh0 10.2210/pdb7hh0/pdb 
WWPDB D_1001407462 ?            ?                   
# 
_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                        7HH0 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '~{N}-methyl-1-pyridin-4-yl-methanamine'           122.168   1   ? ?    ? ? 
5 water       nat water                                              18.015    238 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                            SO4 
3 1,2-ETHANEDIOL                           EDO 
4 '~{N}-methyl-1-pyridin-4-yl-methanamine' RYP 
5 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                 ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                 ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                           'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                                ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                          ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                  ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                    ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                               ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                  ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                   ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                               ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                            ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                  ?                 'C5 H9 N O2'     115.130 
RYP non-polymer         . '~{N}-methyl-1-pyridin-4-yl-methanamine' ?                 'C7 H10 N2'      122.168 
SER 'L-peptide linking' y SERINE                                   ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                            ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                               ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                 ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                   ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP 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        RYP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RYP 
_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 RYP 1   103 101 RYP 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 84  HOH HOH A . 
M 5 HOH 3   203 202 HOH HOH A . 
M 5 HOH 4   204 139 HOH HOH A . 
M 5 HOH 5   205 334 HOH HOH A . 
M 5 HOH 6   206 333 HOH HOH A . 
M 5 HOH 7   207 66  HOH HOH A . 
M 5 HOH 8   208 55  HOH HOH A . 
M 5 HOH 9   209 304 HOH HOH A . 
M 5 HOH 10  210 208 HOH HOH A . 
M 5 HOH 11  211 87  HOH HOH A . 
M 5 HOH 12  212 26  HOH HOH A . 
M 5 HOH 13  213 293 HOH HOH A . 
M 5 HOH 14  214 259 HOH HOH A . 
M 5 HOH 15  215 37  HOH HOH A . 
M 5 HOH 16  216 97  HOH HOH A . 
M 5 HOH 17  217 179 HOH HOH A . 
M 5 HOH 18  218 289 HOH HOH A . 
M 5 HOH 19  219 91  HOH HOH A . 
M 5 HOH 20  220 165 HOH HOH A . 
M 5 HOH 21  221 32  HOH HOH A . 
M 5 HOH 22  222 8   HOH HOH A . 
M 5 HOH 23  223 94  HOH HOH A . 
M 5 HOH 24  224 86  HOH HOH A . 
M 5 HOH 25  225 28  HOH HOH A . 
M 5 HOH 26  226 260 HOH HOH A . 
M 5 HOH 27  227 188 HOH HOH A . 
M 5 HOH 28  228 111 HOH HOH A . 
M 5 HOH 29  229 34  HOH HOH A . 
M 5 HOH 30  230 95  HOH HOH A . 
M 5 HOH 31  231 23  HOH HOH A . 
M 5 HOH 32  232 71  HOH HOH A . 
M 5 HOH 33  233 199 HOH HOH A . 
M 5 HOH 34  234 167 HOH HOH A . 
M 5 HOH 35  235 7   HOH HOH A . 
M 5 HOH 36  236 2   HOH HOH A . 
M 5 HOH 37  237 93  HOH HOH A . 
M 5 HOH 38  238 278 HOH HOH A . 
M 5 HOH 39  239 1   HOH HOH A . 
M 5 HOH 40  240 58  HOH HOH A . 
M 5 HOH 41  241 267 HOH HOH A . 
M 5 HOH 42  242 27  HOH HOH A . 
M 5 HOH 43  243 60  HOH HOH A . 
M 5 HOH 44  244 292 HOH HOH A . 
M 5 HOH 45  245 12  HOH HOH A . 
M 5 HOH 46  246 38  HOH HOH A . 
M 5 HOH 47  247 77  HOH HOH A . 
M 5 HOH 48  248 203 HOH HOH A . 
M 5 HOH 49  249 99  HOH HOH A . 
M 5 HOH 50  250 274 HOH HOH A . 
M 5 HOH 51  251 109 HOH HOH A . 
M 5 HOH 52  252 47  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 78  HOH HOH A . 
M 5 HOH 56  256 297 HOH HOH A . 
M 5 HOH 57  257 18  HOH HOH A . 
M 5 HOH 58  258 20  HOH HOH A . 
M 5 HOH 59  259 164 HOH HOH A . 
M 5 HOH 60  260 300 HOH HOH A . 
M 5 HOH 61  261 287 HOH HOH A . 
M 5 HOH 62  262 21  HOH HOH A . 
M 5 HOH 63  263 145 HOH HOH A . 
M 5 HOH 64  264 116 HOH HOH A . 
M 5 HOH 65  265 222 HOH HOH A . 
M 5 HOH 66  266 42  HOH HOH A . 
M 5 HOH 67  267 143 HOH HOH A . 
M 5 HOH 68  268 115 HOH HOH A . 
M 5 HOH 69  269 14  HOH HOH A . 
M 5 HOH 70  270 218 HOH HOH A . 
M 5 HOH 71  271 9   HOH HOH A . 
M 5 HOH 72  272 75  HOH HOH A . 
M 5 HOH 73  273 16  HOH HOH A . 
M 5 HOH 74  274 152 HOH HOH A . 
M 5 HOH 75  275 281 HOH HOH A . 
M 5 HOH 76  276 318 HOH HOH A . 
M 5 HOH 77  277 19  HOH HOH A . 
M 5 HOH 78  278 211 HOH HOH A . 
M 5 HOH 79  279 73  HOH HOH A . 
M 5 HOH 80  280 301 HOH HOH A . 
M 5 HOH 81  281 31  HOH HOH A . 
M 5 HOH 82  282 327 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 63  HOH HOH A . 
M 5 HOH 88  288 210 HOH HOH A . 
M 5 HOH 89  289 296 HOH HOH A . 
M 5 HOH 90  290 83  HOH HOH A . 
M 5 HOH 91  291 185 HOH HOH A . 
M 5 HOH 92  292 108 HOH HOH A . 
M 5 HOH 93  293 219 HOH HOH A . 
M 5 HOH 94  294 57  HOH HOH A . 
M 5 HOH 95  295 205 HOH HOH A . 
M 5 HOH 96  296 283 HOH HOH A . 
M 5 HOH 97  297 35  HOH HOH A . 
M 5 HOH 98  298 156 HOH HOH A . 
M 5 HOH 99  299 125 HOH HOH A . 
M 5 HOH 100 300 332 HOH HOH A . 
N 5 HOH 1   201 247 HOH HOH B . 
N 5 HOH 2   202 272 HOH HOH B . 
N 5 HOH 3   203 98  HOH HOH B . 
N 5 HOH 4   204 331 HOH HOH B . 
N 5 HOH 5   205 249 HOH HOH B . 
N 5 HOH 6   206 258 HOH HOH B . 
N 5 HOH 7   207 184 HOH HOH B . 
N 5 HOH 8   208 69  HOH HOH B . 
N 5 HOH 9   209 172 HOH HOH B . 
N 5 HOH 10  210 224 HOH HOH B . 
N 5 HOH 11  211 329 HOH HOH B . 
N 5 HOH 12  212 89  HOH HOH B . 
N 5 HOH 13  213 54  HOH HOH B . 
N 5 HOH 14  214 17  HOH HOH B . 
N 5 HOH 15  215 320 HOH HOH B . 
N 5 HOH 16  216 242 HOH HOH B . 
N 5 HOH 17  217 117 HOH HOH B . 
N 5 HOH 18  218 123 HOH HOH B . 
N 5 HOH 19  219 119 HOH HOH B . 
N 5 HOH 20  220 137 HOH HOH B . 
N 5 HOH 21  221 215 HOH HOH B . 
N 5 HOH 22  222 10  HOH HOH B . 
N 5 HOH 23  223 6   HOH HOH B . 
N 5 HOH 24  224 169 HOH HOH B . 
N 5 HOH 25  225 157 HOH HOH B . 
N 5 HOH 26  226 68  HOH HOH B . 
N 5 HOH 27  227 223 HOH HOH B . 
N 5 HOH 28  228 280 HOH HOH B . 
N 5 HOH 29  229 13  HOH HOH B . 
N 5 HOH 30  230 5   HOH HOH B . 
N 5 HOH 31  231 150 HOH HOH B . 
N 5 HOH 32  232 261 HOH HOH B . 
N 5 HOH 33  233 279 HOH HOH B . 
N 5 HOH 34  234 59  HOH HOH B . 
N 5 HOH 35  235 24  HOH HOH B . 
N 5 HOH 36  236 79  HOH HOH B . 
N 5 HOH 37  237 25  HOH HOH B . 
N 5 HOH 38  238 175 HOH HOH B . 
N 5 HOH 39  239 153 HOH HOH B . 
N 5 HOH 40  240 61  HOH HOH B . 
N 5 HOH 41  241 315 HOH HOH B . 
N 5 HOH 42  242 74  HOH HOH B . 
N 5 HOH 43  243 44  HOH HOH B . 
N 5 HOH 44  244 170 HOH HOH B . 
N 5 HOH 45  245 101 HOH HOH B . 
N 5 HOH 46  246 96  HOH HOH B . 
N 5 HOH 47  247 168 HOH HOH B . 
N 5 HOH 48  248 335 HOH HOH B . 
N 5 HOH 49  249 214 HOH HOH B . 
N 5 HOH 50  250 197 HOH HOH B . 
N 5 HOH 51  251 76  HOH HOH B . 
N 5 HOH 52  252 217 HOH HOH B . 
N 5 HOH 53  253 36  HOH HOH B . 
N 5 HOH 54  254 177 HOH HOH B . 
N 5 HOH 55  255 72  HOH HOH B . 
N 5 HOH 56  256 104 HOH HOH B . 
N 5 HOH 57  257 46  HOH HOH B . 
N 5 HOH 58  258 120 HOH HOH B . 
N 5 HOH 59  259 316 HOH HOH B . 
N 5 HOH 60  260 322 HOH HOH B . 
N 5 HOH 61  261 182 HOH HOH B . 
N 5 HOH 62  262 336 HOH HOH B . 
N 5 HOH 63  263 319 HOH HOH B . 
N 5 HOH 64  264 303 HOH HOH B . 
N 5 HOH 65  265 291 HOH HOH B . 
N 5 HOH 66  266 163 HOH HOH B . 
N 5 HOH 67  267 201 HOH HOH B . 
N 5 HOH 68  268 160 HOH HOH B . 
N 5 HOH 69  269 103 HOH HOH B . 
N 5 HOH 70  270 314 HOH HOH B . 
N 5 HOH 71  271 337 HOH HOH B . 
N 5 HOH 72  272 107 HOH HOH B . 
N 5 HOH 73  273 312 HOH HOH B . 
O 5 HOH 1   201 321 HOH HOH C . 
O 5 HOH 2   202 254 HOH HOH C . 
O 5 HOH 3   203 323 HOH HOH C . 
O 5 HOH 4   204 161 HOH HOH C . 
O 5 HOH 5   205 325 HOH HOH C . 
O 5 HOH 6   206 226 HOH HOH C . 
O 5 HOH 7   207 317 HOH HOH C . 
O 5 HOH 8   208 118 HOH HOH C . 
O 5 HOH 9   209 271 HOH HOH C . 
O 5 HOH 10  210 134 HOH HOH C . 
O 5 HOH 11  211 302 HOH HOH C . 
O 5 HOH 12  212 82  HOH HOH C . 
O 5 HOH 13  213 148 HOH HOH C . 
O 5 HOH 14  214 269 HOH HOH C . 
O 5 HOH 15  215 132 HOH HOH C . 
O 5 HOH 16  216 90  HOH HOH C . 
O 5 HOH 17  217 15  HOH HOH C . 
O 5 HOH 18  218 49  HOH HOH C . 
O 5 HOH 19  219 85  HOH HOH C . 
O 5 HOH 20  220 142 HOH HOH C . 
O 5 HOH 21  221 126 HOH HOH C . 
O 5 HOH 22  222 284 HOH HOH C . 
O 5 HOH 23  223 189 HOH HOH C . 
O 5 HOH 24  224 41  HOH HOH C . 
O 5 HOH 25  225 53  HOH HOH C . 
O 5 HOH 26  226 173 HOH HOH C . 
O 5 HOH 27  227 45  HOH HOH C . 
O 5 HOH 28  228 275 HOH HOH C . 
O 5 HOH 29  229 294 HOH HOH C . 
O 5 HOH 30  230 102 HOH HOH C . 
O 5 HOH 31  231 309 HOH HOH C . 
O 5 HOH 32  232 290 HOH HOH C . 
O 5 HOH 33  233 135 HOH HOH C . 
O 5 HOH 34  234 295 HOH HOH C . 
O 5 HOH 35  235 4   HOH HOH C . 
O 5 HOH 36  236 48  HOH HOH C . 
O 5 HOH 37  237 56  HOH HOH C . 
O 5 HOH 38  238 40  HOH HOH C . 
O 5 HOH 39  239 209 HOH HOH C . 
O 5 HOH 40  240 151 HOH HOH C . 
O 5 HOH 41  241 43  HOH HOH C . 
O 5 HOH 42  242 149 HOH HOH C . 
O 5 HOH 43  243 62  HOH HOH C . 
O 5 HOH 44  244 122 HOH HOH C . 
O 5 HOH 45  245 326 HOH HOH C . 
O 5 HOH 46  246 198 HOH HOH C . 
O 5 HOH 47  247 299 HOH HOH C . 
O 5 HOH 48  248 130 HOH HOH C . 
O 5 HOH 49  249 171 HOH HOH C . 
O 5 HOH 50  250 328 HOH HOH C . 
O 5 HOH 51  251 298 HOH HOH C . 
O 5 HOH 52  252 67  HOH HOH C . 
O 5 HOH 53  253 65  HOH HOH C . 
O 5 HOH 54  254 246 HOH HOH C . 
O 5 HOH 55  255 305 HOH HOH C . 
O 5 HOH 56  256 146 HOH HOH C . 
O 5 HOH 57  257 324 HOH HOH C . 
O 5 HOH 58  258 70  HOH HOH C . 
O 5 HOH 59  259 241 HOH HOH C . 
O 5 HOH 60  260 270 HOH HOH C . 
O 5 HOH 61  261 330 HOH HOH C . 
O 5 HOH 62  262 310 HOH HOH C . 
O 5 HOH 63  263 92  HOH HOH C . 
O 5 HOH 64  264 206 HOH HOH C . 
O 5 HOH 65  265 313 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 34 ? CG  ? B LYS 35 CG  
18 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
19 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
20 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
21 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
22 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
23 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
24 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
25 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
26 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
27 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
28 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
29 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
30 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
31 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
32 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
33 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
34 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
35 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
36 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
37 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
38 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
39 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
40 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
41 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
42 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
43 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
44 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
45 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
46 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
47 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
48 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
49 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
50 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
51 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
52 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
53 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
54 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
55 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
56 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
57 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
58 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
59 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
60 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
61 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
62 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
63 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
64 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
65 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           7HH0 
_cell.length_a           41.650 
_cell.length_b           42.300 
_cell.length_c           159.240 
_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                         7HH0 
_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          7HH0 
_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                     7HH0 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.08 
_reflns.d_resolution_high            1.60 
_reflns.number_obs                   38191 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.080 
_reflns.pdbx_netI_over_sigmaI        10.6 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.088 
_reflns.pdbx_Rpim_I_all              0.035 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     234935 
_reflns.pdbx_chi_squared             0.97 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.60 
_reflns_shell.d_res_low                   1.64 
_reflns_shell.number_measured_all         14956 
_reflns_shell.number_unique_obs           2753 
_reflns_shell.Rmerge_I_obs                1.556 
_reflns_shell.pdbx_chi_squared            0.74 
_reflns_shell.pdbx_redundancy             5.4 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.723 
_reflns_shell.pdbx_Rpim_I_all             0.732 
_reflns_shell.pdbx_CC_half                0.418 
_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                                 7HH0 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     36124 
_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                             40.92 
_refine.ls_d_res_high                            1.60 
_refine.ls_percent_reflns_obs                    99.89 
_refine.ls_R_factor_obs                          0.20949 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20757 
_refine.ls_R_factor_R_free                       0.24357 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1994 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               35.225 
_refine.aniso_B[1][1]                            0.85 
_refine.aniso_B[2][2]                            -0.90 
_refine.aniso_B[3][3]                            0.05 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.102 
_refine.pdbx_overall_ESU_R_Free                  0.103 
_refine.overall_SU_ML                            0.092 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.781 
_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        2122 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         47 
_refine_hist.number_atoms_solvent             238 
_refine_hist.number_atoms_total               2407 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        40.92 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.009  0.012  ? 2262 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.843  1.833  ? 3076 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.063  5.000  ? 263  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.913  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.251 10.000 ? 295  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.128  0.200  ? 284  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1874 '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                  3.221  3.303  ? 1065 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.486  5.906  ? 1323 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.478  3.596  ? 1197 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.479  47.67  ? 3435 '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                       1.600 
_refine_ls_shell.d_res_low                        1.641 
_refine_ls_shell.number_reflns_R_work             2617 
_refine_ls_shell.R_factor_R_work                  0.352 
_refine_ls_shell.percent_reflns_obs               99.78 
_refine_ls_shell.R_factor_R_free                  0.383 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             126 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH0 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z57390007' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH0 
_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 7HH0 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH0 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH0 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 7HH0 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH0 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH0 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH0 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH0 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH0 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O 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                   7HH0 
_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 228 ? ? O B HOH 260 ? ? 1.64 
2 1 O2  C SO4 102 ? ? O C HOH 201 ? ? 1.99 
3 1 O   C HOH 256 ? ? O C HOH 257 ? ? 2.00 
4 1 O2  C SO4 102 ? ? O C HOH 202 ? ? 2.00 
5 1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.05 
6 1 OD1 C ASP 9   ? ? O C HOH 203 ? ? 2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 263 ? ? 1_555 O C HOH 229 ? ? 4_435 2.14 
2 1 O A HOH 244 ? ? 1_555 O A HOH 265 ? ? 4_545 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -154.06 62.24 
2 1 ASN B 38 ? ? 77.80   -3.04 
3 1 ASN B 87 ? ? -162.55 58.62 
4 1 ASN C 87 ? ? -159.15 49.52 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.37 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       300 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.87 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ILE 28 ? C ILE 29 
11 1 Y 1 C ALA 29 ? C ALA 30 
12 1 Y 1 C ASP 30 ? C ASP 31 
13 1 Y 1 C GLY 31 ? C GLY 32 
14 1 Y 1 C ALA 32 ? C ALA 33 
15 1 Y 1 C VAL 33 ? C VAL 34 
16 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
RYP C01  C N N 300 
RYP C03  C N N 301 
RYP C04  C Y N 302 
RYP C05  C Y N 303 
RYP C06  C Y N 304 
RYP C08  C Y N 305 
RYP C09  C Y N 306 
RYP N02  N N N 307 
RYP N07  N Y N 308 
RYP H1   H N N 309 
RYP H2   H N N 310 
RYP H3   H N N 311 
RYP H4   H N N 312 
RYP H5   H N N 313 
RYP H6   H N N 314 
RYP H7   H N N 315 
RYP H8   H N N 316 
RYP H9   H N N 317 
RYP H10  H N N 318 
SER N    N N N 319 
SER CA   C N S 320 
SER C    C N N 321 
SER O    O N N 322 
SER CB   C N N 323 
SER OG   O N N 324 
SER OXT  O N N 325 
SER H    H N N 326 
SER H2   H N N 327 
SER HA   H N N 328 
SER HB2  H N N 329 
SER HB3  H N N 330 
SER HG   H N N 331 
SER HXT  H N N 332 
SO4 S    S N N 333 
SO4 O1   O N N 334 
SO4 O2   O N N 335 
SO4 O3   O N N 336 
SO4 O4   O N N 337 
THR N    N N N 338 
THR CA   C N S 339 
THR C    C N N 340 
THR O    O N N 341 
THR CB   C N R 342 
THR OG1  O N N 343 
THR CG2  C N N 344 
THR OXT  O N N 345 
THR H    H N N 346 
THR H2   H N N 347 
THR HA   H N N 348 
THR HB   H N N 349 
THR HG1  H N N 350 
THR HG21 H N N 351 
THR HG22 H N N 352 
THR HG23 H N N 353 
THR HXT  H N N 354 
TRP N    N N N 355 
TRP CA   C N S 356 
TRP C    C N N 357 
TRP O    O N N 358 
TRP CB   C N N 359 
TRP CG   C Y N 360 
TRP CD1  C Y N 361 
TRP CD2  C Y N 362 
TRP NE1  N Y N 363 
TRP CE2  C Y N 364 
TRP CE3  C Y N 365 
TRP CZ2  C Y N 366 
TRP CZ3  C Y N 367 
TRP CH2  C Y N 368 
TRP OXT  O N N 369 
TRP H    H N N 370 
TRP H2   H N N 371 
TRP HA   H N N 372 
TRP HB2  H N N 373 
TRP HB3  H N N 374 
TRP HD1  H N N 375 
TRP HE1  H N N 376 
TRP HE3  H N N 377 
TRP HZ2  H N N 378 
TRP HZ3  H N N 379 
TRP HH2  H N N 380 
TRP HXT  H N N 381 
TYR N    N N N 382 
TYR CA   C N S 383 
TYR C    C N N 384 
TYR O    O N N 385 
TYR CB   C N N 386 
TYR CG   C Y N 387 
TYR CD1  C Y N 388 
TYR CD2  C Y N 389 
TYR CE1  C Y N 390 
TYR CE2  C Y N 391 
TYR CZ   C Y N 392 
TYR OH   O N N 393 
TYR OXT  O N N 394 
TYR H    H N N 395 
TYR H2   H N N 396 
TYR HA   H N N 397 
TYR HB2  H N N 398 
TYR HB3  H N N 399 
TYR HD1  H N N 400 
TYR HD2  H N N 401 
TYR HE1  H N N 402 
TYR HE2  H N N 403 
TYR HH   H N N 404 
TYR HXT  H N N 405 
VAL N    N N N 406 
VAL CA   C N S 407 
VAL C    C N N 408 
VAL O    O N N 409 
VAL CB   C N N 410 
VAL CG1  C N N 411 
VAL CG2  C N N 412 
VAL OXT  O N N 413 
VAL H    H N N 414 
VAL H2   H N N 415 
VAL HA   H N N 416 
VAL HB   H N N 417 
VAL HG11 H N N 418 
VAL HG12 H N N 419 
VAL HG13 H N N 420 
VAL HG21 H N N 421 
VAL HG22 H N N 422 
VAL HG23 H N N 423 
VAL HXT  H N N 424 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
RYP C01 N02  sing N N 286 
RYP N02 C03  sing N N 287 
RYP C03 C04  sing N N 288 
RYP C04 C09  doub Y N 289 
RYP C04 C05  sing Y N 290 
RYP C09 C08  sing Y N 291 
RYP C05 C06  doub Y N 292 
RYP C08 N07  doub Y N 293 
RYP C06 N07  sing Y N 294 
RYP C01 H1   sing N N 295 
RYP C01 H2   sing N N 296 
RYP C01 H3   sing N N 297 
RYP C03 H4   sing N N 298 
RYP C03 H5   sing N N 299 
RYP C05 H6   sing N N 300 
RYP C06 H7   sing N N 301 
RYP C08 H8   sing N N 302 
RYP C09 H9   sing N N 303 
RYP N02 H10  sing N N 304 
SER N   CA   sing N N 305 
SER N   H    sing N N 306 
SER N   H2   sing N N 307 
SER CA  C    sing N N 308 
SER CA  CB   sing N N 309 
SER CA  HA   sing N N 310 
SER C   O    doub N N 311 
SER C   OXT  sing N N 312 
SER CB  OG   sing N N 313 
SER CB  HB2  sing N N 314 
SER CB  HB3  sing N N 315 
SER OG  HG   sing N N 316 
SER OXT HXT  sing N N 317 
SO4 S   O1   doub N N 318 
SO4 S   O2   doub N N 319 
SO4 S   O3   sing N N 320 
SO4 S   O4   sing N N 321 
THR N   CA   sing N N 322 
THR N   H    sing N N 323 
THR N   H2   sing N N 324 
THR CA  C    sing N N 325 
THR CA  CB   sing N N 326 
THR CA  HA   sing N N 327 
THR C   O    doub N N 328 
THR C   OXT  sing N N 329 
THR CB  OG1  sing N N 330 
THR CB  CG2  sing N N 331 
THR CB  HB   sing N N 332 
THR OG1 HG1  sing N N 333 
THR CG2 HG21 sing N N 334 
THR CG2 HG22 sing N N 335 
THR CG2 HG23 sing N N 336 
THR OXT HXT  sing N N 337 
TRP N   CA   sing N N 338 
TRP N   H    sing N N 339 
TRP N   H2   sing N N 340 
TRP CA  C    sing N N 341 
TRP CA  CB   sing N N 342 
TRP CA  HA   sing N N 343 
TRP C   O    doub N N 344 
TRP C   OXT  sing N N 345 
TRP CB  CG   sing N N 346 
TRP CB  HB2  sing N N 347 
TRP CB  HB3  sing N N 348 
TRP CG  CD1  doub Y N 349 
TRP CG  CD2  sing Y N 350 
TRP CD1 NE1  sing Y N 351 
TRP CD1 HD1  sing N N 352 
TRP CD2 CE2  doub Y N 353 
TRP CD2 CE3  sing Y N 354 
TRP NE1 CE2  sing Y N 355 
TRP NE1 HE1  sing N N 356 
TRP CE2 CZ2  sing Y N 357 
TRP CE3 CZ3  doub Y N 358 
TRP CE3 HE3  sing N N 359 
TRP CZ2 CH2  doub Y N 360 
TRP CZ2 HZ2  sing N N 361 
TRP CZ3 CH2  sing Y N 362 
TRP CZ3 HZ3  sing N N 363 
TRP CH2 HH2  sing N N 364 
TRP OXT HXT  sing N N 365 
TYR N   CA   sing N N 366 
TYR N   H    sing N N 367 
TYR N   H2   sing N N 368 
TYR CA  C    sing N N 369 
TYR CA  CB   sing N N 370 
TYR CA  HA   sing N N 371 
TYR C   O    doub N N 372 
TYR C   OXT  sing N N 373 
TYR CB  CG   sing N N 374 
TYR CB  HB2  sing N N 375 
TYR CB  HB3  sing N N 376 
TYR CG  CD1  doub Y N 377 
TYR CG  CD2  sing Y N 378 
TYR CD1 CE1  sing Y N 379 
TYR CD1 HD1  sing N N 380 
TYR CD2 CE2  doub Y N 381 
TYR CD2 HD2  sing N N 382 
TYR CE1 CZ   doub Y N 383 
TYR CE1 HE1  sing N N 384 
TYR CE2 CZ   sing Y N 385 
TYR CE2 HE2  sing N N 386 
TYR CZ  OH   sing N N 387 
TYR OH  HH   sing N N 388 
TYR OXT HXT  sing N N 389 
VAL N   CA   sing N N 390 
VAL N   H    sing N N 391 
VAL N   H2   sing N N 392 
VAL CA  C    sing N N 393 
VAL CA  CB   sing N N 394 
VAL CA  HA   sing N N 395 
VAL C   O    doub N N 396 
VAL C   OXT  sing N N 397 
VAL CB  CG1  sing N N 398 
VAL CB  CG2  sing N N 399 
VAL CB  HB   sing N N 400 
VAL CG1 HG11 sing N N 401 
VAL CG1 HG12 sing N N 402 
VAL CG1 HG13 sing N N 403 
VAL CG2 HG21 sing N N 404 
VAL CG2 HG22 sing N N 405 
VAL CG2 HG23 sing N N 406 
VAL OXT HXT  sing N N 407 
# 
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                    7HH0 
_atom_sites.fract_transf_matrix[1][1]   0.024010 
_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]   0.023641 
_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]   0.006280 
_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  ? 1.049   4.096   2.440   1.00 47.22  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.084  3.466   1.708   1.00 49.95  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.441   2.397   0.743   1.00 47.05  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.512   2.553   0.167   1.00 44.99  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -0.940  4.520   0.996   1.00 54.70  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -1.970  5.204   1.898   1.00 67.55  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.397  4.273   2.513   1.00 72.50  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.198  5.476   3.585   1.00 74.77  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.282  1.261   0.576   1.00 41.54  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.147   0.151   -0.287  1.00 41.46  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.397   0.504   -1.753  1.00 40.49  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.335  1.290   -2.353  1.00 41.73  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.102  -0.805  -0.150  1.00 39.39  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.610  -0.522  1.252   1.00 44.57  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.559  0.985   1.262   1.00 41.92  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.396   -0.134  -2.359  1.00 34.80  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.549   0.008   -3.790  1.00 35.03  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.964   -1.259  -4.411  1.00 34.63  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.435   -2.105  -3.689  1.00 34.05  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 3.033   0.229   -4.131  1.00 42.75  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.602   1.529   -3.626  1.00 56.59  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.874   1.791   -2.298  1.00 62.74  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 3.949   2.649   -4.288  1.00 64.62  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.355   3.023   -2.172  1.00 64.83  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.413   3.562   -3.367  1.00 59.91  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.032   -1.392  -5.731  1.00 28.10  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.792   -2.689  -6.347  1.00 25.23  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.907   -3.651  -5.955  1.00 26.52  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.003   -3.247  -5.515  1.00 26.66  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.707   -2.555  -7.858  1.00 32.39  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.601   -4.934  -6.129  1.00 25.47  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.601   -5.973  -5.971  1.00 25.04  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.760   -5.768  -6.962  1.00 26.26  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.564   -5.356  -8.110  1.00 27.72  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.057   -7.402  -6.039  1.00 24.83  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.295   -7.755  -4.768  1.00 26.53  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.980   -7.970  -3.562  1.00 21.75  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.102  -7.923  -4.798  1.00 23.36  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.312   -8.318  -2.386  1.00 23.04  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.757  -8.296  -3.614  1.00 20.87  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.066  -8.494  -2.431  1.00 23.10  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.992   -6.048  -6.477  1.00 21.10  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.152   -6.011  -7.372  1.00 22.94  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.070   -7.202  -7.061  1.00 22.18  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.035   -7.775  -5.983  1.00 21.74  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.864   -4.666  -7.151  1.00 26.15  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.510   -4.566  -5.794  1.00 26.16  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.240   -3.235  -5.540  1.00 33.94  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.887   -3.224  -4.163  1.00 35.27  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.885   -3.232  -3.085  1.00 32.94  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.970   -7.600  -7.992  1.00 24.38  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.900   -8.693  -7.724  1.00 24.17  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.680   -8.414  -6.445  1.00 20.47  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.144  -7.286  -6.206  1.00 22.58  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.820   -8.668  -8.992  1.00 24.37  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.907   -8.085  -10.081 1.00 25.74  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.163   -6.969  -9.327  1.00 27.16  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.868   -9.465  -5.635  1.00 21.02  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.607  -9.377  -4.386  1.00 18.21  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.672   -9.226  -3.181  1.00 20.08  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.029  -9.544  -2.047  1.00 21.25  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.424   -8.822  -3.421  1.00 16.73  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.497   -8.782  -2.280  1.00 17.15  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.240   -10.168 -1.664  1.00 16.25  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.092   -11.166 -2.371  1.00 18.36  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.148   -8.174  -2.696  1.00 20.02  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.169   -6.668  -2.901  1.00 23.13  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.128   -5.989  -2.429  1.00 23.44  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.232   -6.172  -3.549  1.00 22.15  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.132   -10.199 -0.320  1.00 18.18  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.967   -11.455 0.411   1.00 16.49  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.484   -11.540 0.800   1.00 19.33  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.915   -10.511 1.238   1.00 20.53  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.872   -11.504 1.645   1.00 17.96  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.354   -11.325 1.282   1.00 17.70  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.278  -11.405 2.534   1.00 19.80  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.806   -12.280 0.172   1.00 21.29  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.934   -12.764 0.674   1.00 19.08  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.500   -12.985 0.895   1.00 17.76  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.245   -14.360 1.519   1.00 18.49  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.111   -15.253 1.602   1.00 19.50  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.686   -12.852 -0.407  1.00 16.50  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.827   -11.431 -1.017  1.00 20.17  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.051   -13.941 -1.423  1.00 19.35  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.025   -14.521 2.064   1.00 17.90  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.466   -15.846 2.101   1.00 18.26  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.509   -15.922 0.904   1.00 20.21  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.282  -15.001 0.698   1.00 20.10  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.658   -16.238 3.379   1.00 17.99  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.578   -16.331 4.594   1.00 19.19  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.897   -15.159 5.281   1.00 21.46  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.105   -17.555 5.004   1.00 22.31  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.817   -15.214 6.331   1.00 27.54  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.032   -17.609 6.053   1.00 25.45  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.361   -16.438 6.713   1.00 24.60  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.608   -17.025 0.133   1.00 18.83  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.186  -17.204 -1.083  1.00 19.79  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.186  -18.349 -0.878  1.00 23.12  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.830  -19.424 -0.377  1.00 23.78  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.722   -17.425 -2.310  1.00 18.97  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.457  -18.118 -1.297  1.00 20.63  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.467  -19.135 -1.052  1.00 23.42  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.837  -19.842 -2.353  1.00 25.30  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.209  -19.213 -3.348  1.00 26.83  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.677  -18.467 -0.392  1.00 23.19  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.838  -19.441 -0.023  1.00 29.50  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.426  -20.350 1.146   1.00 32.89  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.542  -21.191 1.726   1.00 35.59  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.896  -22.315 0.856   1.00 34.25  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.750  -21.177 -2.303  1.00 24.73  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.400  -21.966 -3.329  1.00 29.44  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.382  -22.970 -2.745  1.00 31.42  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.230  -23.375 -1.612  1.00 27.45  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.383  -22.778 -4.099  1.00 35.08  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -3.500  -22.288 -5.511  1.00 48.67  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.791  -21.924 -5.886  1.00 37.31  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.328  -23.466 -6.652  1.00 34.94  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.338  -23.383 -3.585  1.00 34.86  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.377  -24.335 -3.224  1.00 38.55  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.752  -25.576 -2.619  1.00 33.47  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.839  -26.154 -3.208  1.00 34.97  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.047  -24.789 -4.525  1.00 44.41  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.364  -25.535 -4.317  1.00 49.70  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.371 -24.705 -3.521  1.00 57.33  ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.247  -25.999 -1.441  1.00 34.05  ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.794  -27.255 -0.879  1.00 34.53  ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.512  -27.102 -0.079  1.00 38.47  ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.033  -28.063 0.511   1.00 42.23  ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -4.939  -25.891 -0.050  1.00 33.34  ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.695  -25.786 0.679   1.00 32.03  ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.764  -24.656 1.682   1.00 28.56  ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.472  -23.683 1.465   1.00 28.60  ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.531  -25.421 -0.253  1.00 34.00  ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.025  -26.452 -1.252  1.00 35.46  ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -0.906  -27.219 -0.967  1.00 49.39  ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.614  -26.592 -2.504  1.00 39.59  ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.413  -28.131 -1.885  1.00 45.77  ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.117  -27.482 -3.451  1.00 41.49  ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.012  -28.255 -3.128  1.00 49.82  ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.496  -29.167 -4.011  1.00 63.32  ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -2.976  -24.720 2.780   1.00 27.87  ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -2.917  -23.631 3.764   1.00 29.20  ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.228  -22.451 3.075   1.00 24.81  ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.491  -22.701 2.115   1.00 25.81  ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.050  -24.209 4.908   1.00 31.06  ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.265  -25.334 4.240   1.00 30.16  ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.135  -25.887 3.139   1.00 30.33  ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.510  -21.247 3.560   1.00 24.06  ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.815  -20.014 3.183   1.00 22.69  ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.304  -20.276 3.283   1.00 23.68  ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.157   -20.702 4.348   1.00 23.06  ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.273  -18.822 4.041   1.00 24.39  ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.710  -18.438 3.853   1.00 25.06  ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.691  -19.106 4.568   1.00 28.94  ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.335  -17.488 3.113   1.00 24.59  ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.893  -18.596 4.243   1.00 29.56  ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.713  -17.578 3.401   1.00 27.51  ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.448   -20.072 2.166   1.00 23.60  ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.764   -20.694 2.000   1.00 23.40  ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.847   -19.618 1.903   1.00 21.11  ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.691   -18.676 1.140   1.00 21.79  ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.806   -21.578 0.751   1.00 22.67  ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.903   -22.617 0.839   1.00 24.18  ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.259   -22.477 0.656   1.00 23.56  ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.683   -24.005 1.176   1.00 24.74  ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.890   -23.708 0.810   1.00 23.73  ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.942   -24.653 1.126   1.00 28.81  ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.538   -24.762 1.489   1.00 26.56  ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.096   -26.015 1.423   1.00 30.32  ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.691   -26.117 1.734   1.00 29.99  ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.955   -26.732 1.701   1.00 33.03  ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.973   -19.686 2.656   1.00 20.56  ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 5.026   -18.674 2.450   1.00 18.10  ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.538   -18.612 1.005   1.00 18.24  ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.863   -19.656 0.400   1.00 19.75  ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 6.115   -19.094 3.482   1.00 19.13  ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.938   -20.576 3.649   1.00 18.38  ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.362   -20.730 3.608   1.00 21.91  ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.622   -17.397 0.443   1.00 17.23  ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.956   -17.269 -0.977  1.00 16.44  ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.461   -15.873 -1.324  1.00 16.45  ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.498   -14.986 -0.482  1.00 18.43  ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.701   -17.612 -1.845  1.00 19.69  ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 7.024   -15.749 -2.540  1.00 16.19  ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.410   -14.408 -2.984  1.00 18.07  ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.865   -14.127 -4.378  1.00 18.89  ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.583   -15.057 -5.146  1.00 19.27  ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.928   -14.269 -2.955  1.00 19.58  ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.618   -15.146 -3.983  1.00 19.98  ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.181  -14.980 -3.811  1.00 21.15  ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.865  -15.766 -4.857  1.00 21.01  ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 13.128  -16.188 -4.753  1.00 21.95  ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.801  -16.045 -3.606  1.00 21.13  ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.702  -16.810 -5.787  1.00 24.30  ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.776   -12.844 -4.727  1.00 18.46  ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.522   -12.497 -6.123  1.00 19.72  ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.846   -12.602 -6.872  1.00 22.75  ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.813   -12.011 -6.423  1.00 20.84  ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 6.033   -11.040 -6.218  1.00 21.00  ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.868   -10.752 -5.243  1.00 25.27  ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.667   -10.696 -7.679  1.00 22.65  ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.540   -11.343 -5.649  1.00 29.26  ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.902   -13.466 -7.873  1.00 20.65  ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 9.129   -13.631 -8.644  1.00 21.89  ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.247   -12.598 -9.766  1.00 25.42  ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.293   -11.987 -10.226 1.00 25.30  ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.250   -15.025 -9.218  1.00 22.01  ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.219  -15.947 -8.502  1.00 25.46  ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.830  -15.512 -7.489  1.00 29.42  ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.359  -17.064 -8.944  1.00 26.09  ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.493  -12.425 -10.264 1.00 28.09  ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.707  -11.742 -11.521 1.00 31.05  ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.477  -12.779 -12.629 1.00 29.75  ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.388  -13.973 -12.384 1.00 28.13  ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.171  -11.324 -11.643 1.00 37.14  ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.631  -10.058 -10.924 1.00 45.85  ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.309  -8.939  -11.398 1.00 48.62  ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.360  -10.198 -9.920  1.00 50.40  ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.389  -12.314 -13.860 1.00 31.38  ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.321  -13.228 -14.996 1.00 29.45  ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.655  -13.027 -15.713 1.00 29.84  ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.993  -11.880 -16.006 1.00 30.27  ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.154   -12.784 -15.893 1.00 32.18  ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.779   -12.761 -15.137 1.00 32.22  ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.103   -13.595 -17.190 1.00 29.21  ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.747   -11.843 -15.777 1.00 32.25  ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.407  -14.119 -15.905 1.00 32.23  ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.699  -14.046 -16.583 1.00 30.79  ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.495  -13.665 -18.054 1.00 29.02  ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.450  -13.929 -18.648 1.00 29.96  ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.398  -15.381 -16.453 1.00 33.21  ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.497  -12.996 -18.640 1.00 29.67  ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.508  -12.823 -20.089 1.00 31.18  ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.294  -14.190 -20.730 1.00 25.50  ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.923  -15.167 -20.353 1.00 29.85  ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.831  -12.224 -20.574 1.00 32.13  ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 16.045  -10.742 -20.307 1.00 37.18  ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 15.067  -10.056 -20.051 1.00 33.09  ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.214  -10.284 -20.325 1.00 38.64  ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.359  -14.245 -21.675 1.00 25.10  ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.113  -15.403 -22.514 1.00 27.66  ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.206  -16.440 -21.860 1.00 32.41  ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.859  -17.428 -22.498 1.00 33.38  ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.803  -16.181 -20.607 1.00 30.39  ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.967  -17.120 -19.862 1.00 33.13  ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.476   -16.862 -20.127 1.00 27.85  ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.040   -15.770 -20.510 1.00 28.80  ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.313  -17.019 -18.373 1.00 30.63  ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.665   -17.906 -19.879 1.00 32.81  ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.211   -17.825 -20.022 1.00 34.58  ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.615   -16.800 -19.057 1.00 32.32  ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.864   -16.879 -17.853 1.00 33.74  ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.600   -19.213 -19.731 1.00 36.58  ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.081   -19.140 -19.747 1.00 35.74  ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.106   -20.245 -20.734 1.00 36.41  ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.806   -15.885 -19.604 1.00 31.31  ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.167   -14.824 -18.841 1.00 35.02  ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.866   -15.346 -18.239 1.00 34.19  ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.274   -16.280 -18.774 1.00 37.39  ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.828   -13.600 -19.692 1.00 32.18  ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.035   -12.878 -20.328 1.00 32.43  ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.727   -11.594 -21.100 1.00 42.58  ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.237   -11.905 -22.487 1.00 40.61  ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.116   -10.698 -23.299 1.00 41.03  ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.346   -14.703 -17.166 1.00 33.56  ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.058   -15.106 -16.594 1.00 33.45  ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.914   -14.584 -17.461 1.00 34.40  ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.077   -13.639 -18.222 1.00 34.22  ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 2.038   -14.472 -15.201 1.00 33.99  ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.956   -13.259 -15.309 1.00 37.40  ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.925   -13.535 -16.486 1.00 34.80  ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.312  -15.115 -17.298 1.00 38.68  ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.486  -14.518 -17.943 1.00 40.49  ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.659  -13.092 -17.442 1.00 43.24  ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.121  -12.750 -16.389 1.00 33.90  ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.642  -15.399 -17.445 1.00 34.93  ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -1.993  -16.701 -17.057 1.00 33.83  ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.630  -16.307 -16.488 1.00 37.92  ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.444  -12.244 -18.148 1.00 39.13  ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.809  -10.915 -17.659 1.00 42.59  ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.439  -10.957 -16.272 1.00 35.78  ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.175  -11.878 -15.953 1.00 37.37  ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.795  -10.335 -18.705 1.00 47.21  ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.113  -11.493 -19.605 1.00 38.25  ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.026  -12.542 -19.477 1.00 45.47  ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.102  -9.942  -15.467 1.00 37.98  ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.605  -9.740  -14.126 1.00 36.47  ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.043  -10.767 -13.139 1.00 31.88  ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.482  -10.750 -11.985 1.00 30.91  ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.126  -9.640  -14.110 1.00 45.97  ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.570  -8.446  -14.922 1.00 50.40  ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.492  -7.306  -14.448 1.00 51.14  ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -5.985  -8.684  -16.153 1.00 49.68  ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.113  -11.648 -13.578 1.00 27.54  ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.557  -12.656 -12.666 1.00 23.58  ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.073  -12.363 -12.435 1.00 23.35  ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.583   -11.655 -13.242 1.00 26.19  ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.678  -14.109 -13.129 1.00 27.73  ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.067  -14.598 -13.546 1.00 31.25  ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.013  -14.441 -12.360 1.00 35.05  ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.506  -14.547 -12.622 1.00 45.39  ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.857  -15.960 -12.766 1.00 43.44  ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.394   -12.863 -11.289 1.00 21.29  ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.790   -12.723 -10.896 1.00 22.77  ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.430   -14.095 -10.818 1.00 22.28  ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.816   -15.077 -10.429 1.00 21.76  ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.855   -12.087 -9.493  1.00 22.83  ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.372   -10.650 -9.491  1.00 24.11  ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? 0.003   -10.380 -9.416  1.00 30.91  ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.241   -9.589  -9.659  1.00 27.23  ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.474  -9.079  -9.520  1.00 32.09  ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.781   -8.274  -9.706  1.00 26.60  ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.417   -8.029  -9.640  1.00 34.26  ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.054  -6.749  -9.755  1.00 32.62  ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.752   -14.206 -11.085 1.00 20.31  ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.426   -15.486 -10.871 1.00 20.23  ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.802   -15.614 -9.411  1.00 19.54  ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.455   -14.711 -8.879  1.00 22.39  ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.672   -15.342 -11.779 1.00 21.78  ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.880   -13.892 -11.939 1.00 21.76  ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.573   -13.127 -11.657 1.00 23.20  ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.243   -16.641 -8.761  1.00 20.90  ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.457   -16.801 -7.332  1.00 19.69  ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.403   -17.972 -7.107  1.00 21.25  ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 5.114   -19.110 -7.527  1.00 22.76  ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 3.109   -17.074 -6.630  1.00 20.58  ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 2.088   -15.965 -6.951  1.00 21.88  ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.350   -17.209 -5.113  1.00 20.25  ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.564   -14.554 -6.619  1.00 24.08  ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.512   -17.725 -6.381  1.00 18.73  ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.410   -18.802 -6.044  1.00 21.45  ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 7.103   -19.206 -4.603  1.00 21.50  ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.146   -18.373 -3.696  1.00 20.63  ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.854   -18.279 -6.196  1.00 21.03  ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.863   -19.311 -5.730  1.00 23.66  ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.245  -20.342 -6.614  1.00 23.97  ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.456  -19.223 -4.462  1.00 26.44  ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.186  -21.284 -6.197  1.00 25.74  ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.383  -20.191 -4.055  1.00 28.57  ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.763  -21.190 -4.943  1.00 26.38  ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.816   -20.490 -4.401  1.00 21.12  ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.426   -21.002 -3.090  1.00 20.91  ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.686   -21.525 -2.402  1.00 22.98  ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.414   -22.400 -2.944  1.00 22.34  ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.425   -22.153 -3.324  1.00 24.97  ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 4.053   -21.652 -3.746  1.00 21.34  ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.700   -21.480 -5.084  1.00 25.79  ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 3.089   -21.391 -2.766  1.00 24.85  ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.434   -21.005 -5.446  1.00 27.06  ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.832   -20.897 -3.127  1.00 25.69  ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.518   -20.699 -4.452  1.00 26.42  ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.941   -20.968 -1.218  1.00 21.18  ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.106   -21.427 -0.461  1.00 22.91  ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.893   -22.887 -0.020  1.00 22.67  ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.763   -23.361 0.134   1.00 25.63  ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.370   -20.501 0.736   1.00 22.92  ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.835   -19.116 0.329   1.00 20.42  ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 11.089  -18.921 -0.273  1.00 19.98  ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 9.098   -17.963 0.662   1.00 20.88  ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.511  -17.638 -0.628  1.00 19.01  ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.531   -16.686 0.304   1.00 18.92  ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.759  -16.511 -0.334  1.00 19.30  ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 10.017  -23.584 0.188   1.00 23.71  ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.969   -24.959 0.682   1.00 22.58  ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.708   -25.940 -0.471  1.00 28.78  ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.565  -26.765 -0.801  1.00 28.68  ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.550   -25.842 -1.150  1.00 29.20  ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.297   -26.693 -2.301  1.00 29.67  ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.092   -26.242 -3.521  1.00 30.39  ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.359   -27.031 -4.437  1.00 29.01  ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.807   -26.779 -2.641  1.00 29.48  ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.456   -25.471 -3.093  1.00 27.77  ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.943   -27.252 -1.494  1.00 30.33  ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.372   -24.929 -3.584  1.00 24.28  ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 10.079  -24.321 -4.700  1.00 25.98  ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.265   -24.447 -5.985  1.00 25.55  ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.830   -24.410 -7.063  1.00 29.20  ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.515  -24.849 -4.854  1.00 25.49  ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.239  -24.898 -3.540  1.00 26.63  ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 13.005  -25.973 -3.161  1.00 28.66  ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.365  -23.974 -2.557  1.00 25.53  ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.517  -25.733 -1.953  1.00 32.40  ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.180  -24.496 -1.584  1.00 29.67  ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.943   -24.545 -5.858  1.00 27.25  ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 7.098   -24.560 -7.044  1.00 27.38  ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.654   -23.142 -7.417  1.00 28.01  ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.833   -22.197 -6.636  1.00 26.75  ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.854   -25.401 -6.798  1.00 29.50  ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.187   -26.879 -6.600  1.00 40.06  ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.065   -27.740 -6.050  1.00 47.67  ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.884   -27.330 -5.973  1.00 48.57  ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.442   -28.859 -5.643  1.00 55.06  ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.167   -22.999 -8.658  1.00 24.82  ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.700   -21.712 -9.162  1.00 23.66  ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.258   -21.890 -9.628  1.00 28.17  ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.931   -22.881 -10.288 1.00 30.58  ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.557   -21.193 -10.326 1.00 27.84  ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.849   -20.801 -9.866  1.00 28.11  ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.993   -19.919 -10.944 1.00 31.97  ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.371   -20.975 -9.208  1.00 24.13  ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 2.038   -20.873 -9.789  1.00 23.21  ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.732   -19.429 -10.139 1.00 23.20  ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.388   -18.500 -9.656  1.00 24.90  ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 1.006   -21.418 -8.828  1.00 26.54  ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.676   -19.218 -10.949 1.00 22.55  ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.286   -17.860 -11.284 1.00 24.51  ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -0.977  -17.496 -10.516 1.00 27.12  ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -1.963  -18.226 -10.543 1.00 29.79  ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.072  -17.860 -12.764 1.00 26.76  ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.091   -18.220 -13.661 1.00 27.57  ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.307   -17.540 -13.574 1.00 33.92  ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.949   -19.232 -14.602 1.00 32.44  ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.374   -17.871 -14.411 1.00 41.79  ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.019   -19.558 -15.426 1.00 38.83  ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.221   -18.881 -15.343 1.00 37.14  ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -0.911  -16.392 -9.758  1.00 21.26  ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.041  -16.043 -8.902  1.00 21.61  ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.329  -14.550 -9.036  1.00 24.00  ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.465  -13.731 -9.389  1.00 22.76  ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.653  -16.336 -7.449  1.00 23.41  ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.662  -17.806 -7.042  1.00 24.44  ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.266  -17.885 -5.547  1.00 24.37  ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.067  -18.412 -7.236  1.00 27.87  ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.580  -14.184 -8.723  1.00 20.37  ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.940  -12.773 -8.679  1.00 22.13  ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -3.978  -12.270 -7.219  1.00 19.24  ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -3.868  -13.088 -6.272  1.00 19.38  ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.053  -10.935 -7.022  1.00 21.13  ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -3.978  -10.306 -5.692  1.00 20.89  ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -4.956  -10.820 -4.647  1.00 20.50  ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.657  -10.752 -3.469  1.00 20.53  ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.258  -8.827  -5.970  1.00 21.01  ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.701  -8.625  -7.378  1.00 24.54  ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.019  -9.935  -8.111  1.00 22.53  ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.084  -11.374 -5.120  1.00 22.29  ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.057  -11.905 -4.161  1.00 21.24  ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.502  -13.049 -3.307  1.00 20.13  ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -6.973  -13.284 -2.194  1.00 21.05  ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.338  -12.412 -4.843  1.00 25.15  ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.218  -13.723 -5.586  1.00 27.67  ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.526  -14.022 -6.327  1.00 33.45  ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.447  -15.272 -7.122  1.00 36.97  ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.376  -16.435 -6.231  1.00 39.88  ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.439  -13.736 -3.794  1.00 19.88  ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -4.870  -14.870 -3.120  1.00 21.34  ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.528  -14.499 -2.482  1.00 19.32  ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.836  -15.402 -2.016  1.00 21.46  ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.794  -16.039 -4.100  1.00 22.98  ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.175  -16.623 -4.380  1.00 25.89  ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -6.984  -16.680 -3.406  1.00 26.64  ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.450  -17.006 -5.533  1.00 27.69  ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.188  -13.203 -2.481  1.00 19.47  ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.870  -12.796 -1.969  1.00 19.29  ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.013  -11.933 -0.704  1.00 16.75  ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.567  -10.830 -0.731  1.00 19.34  ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.083  -12.072 -3.086  1.00 18.86  ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -0.974  -12.850 -4.394  1.00 18.91  ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.222  -11.982 -5.404  1.00 20.80  ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.199  -14.121 -4.230  1.00 19.36  ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.385  -12.389 0.396   1.00 18.28  ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.511  -11.706 1.687   1.00 20.02  ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.136  -11.190 2.098   1.00 21.34  ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.753   -12.016 2.283   1.00 22.98  ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -1.969  -12.759 2.699   1.00 19.82  ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.416  -13.172 2.446   1.00 20.27  ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.733  -14.127 1.481   1.00 20.65  ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.422  -12.646 3.263   1.00 21.63  ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.053  -14.471 1.209   1.00 25.57  ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.752  -12.985 2.966   1.00 21.41  ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.045  -13.916 1.995   1.00 23.28  ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? 0.103   -9.871  2.227   1.00 24.17  ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.460   -9.394  2.576   1.00 21.71  ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 2.005   -10.088 3.818   1.00 22.18  ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.323   -10.275 4.818   1.00 23.03  ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.211   -7.885  2.754   1.00 22.80  ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.171   -7.603  1.628   1.00 25.65  ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.801  -8.752  1.906   1.00 24.17  ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.302   -10.465 3.791   1.00 23.60  ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.860   -11.340 4.809   1.00 23.02  ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.912   -10.669 6.199   1.00 21.60  ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.542   -11.325 7.176   1.00 26.29  ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.279   -11.751 4.360   1.00 24.19  ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 6.025   -12.547 5.427   1.00 22.73  ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.746   -13.900 5.660   1.00 22.99  ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 7.067   -11.954 6.137   1.00 27.44  ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.431   -14.656 6.614   1.00 24.02  ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.759   -12.704 7.070   1.00 26.55  ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.431   -14.017 7.337   1.00 28.29  ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.178   -14.704 8.278   1.00 29.83  ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.308   -9.401  6.248   1.00 22.79  ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.486   -8.711  7.529   1.00 27.45  ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 3.155   -8.693  8.288   1.00 27.69  ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 3.073   -9.238  9.388   1.00 35.10  ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.205   -7.378  7.392   1.00 26.24  ? 62  ASP A CB  1 
ATOM   495  N N   . LYS A 1 64 ? 2.097   -8.212  7.617   1.00 29.19  ? 63  LYS A N   1 
ATOM   496  C CA  . LYS A 1 64 ? 0.771   -8.152  8.243   1.00 29.10  ? 63  LYS A CA  1 
ATOM   497  C C   . LYS A 1 64 ? 0.220   -9.528  8.654   1.00 27.98  ? 63  LYS A C   1 
ATOM   498  O O   . LYS A 1 64 ? -0.553  -9.630  9.633   1.00 27.41  ? 63  LYS A O   1 
ATOM   499  C CB  . LYS A 1 64 ? -0.157  -7.515  7.203   1.00 31.11  ? 63  LYS A CB  1 
ATOM   500  C CG  . LYS A 1 64 ? -1.614  -7.276  7.656   1.00 37.35  ? 63  LYS A CG  1 
ATOM   501  C CD  . LYS A 1 64 ? -2.429  -6.643  6.535   1.00 37.10  ? 63  LYS A CD  1 
ATOM   502  C CE  . LYS A 1 64 ? -3.592  -5.831  7.028   1.00 42.44  ? 63  LYS A CE  1 
ATOM   503  N NZ  . LYS A 1 64 ? -4.523  -6.521  7.911   1.00 49.16  ? 63  LYS A NZ  1 
ATOM   504  N N   . SER A 1 65 ? 0.549   -10.607 7.916   1.00 27.19  ? 64  SER A N   1 
ATOM   505  C CA  . SER A 1 65 ? -0.155  -11.876 8.032   1.00 26.46  ? 64  SER A CA  1 
ATOM   506  C C   . SER A 1 65 ? 0.603   -12.951 8.819   1.00 28.48  ? 64  SER A C   1 
ATOM   507  O O   . SER A 1 65 ? 0.059   -14.047 9.003   1.00 27.98  ? 64  SER A O   1 
ATOM   508  C CB  . SER A 1 65 ? -0.503  -12.465 6.668   1.00 29.58  ? 64  SER A CB  1 
ATOM   509  O OG  . SER A 1 65 ? -1.277  -11.506 5.964   1.00 37.67  ? 64  SER A OG  1 
ATOM   510  N N   . LYS A 1 66 ? 1.884   -12.709 9.148   1.00 28.63  ? 65  LYS A N   1 
ATOM   511  C CA  . LYS A 1 66 ? 2.711   -13.797 9.656   1.00 30.42  ? 65  LYS A CA  1 
ATOM   512  C C   . LYS A 1 66 ? 2.241   -14.318 11.015  1.00 30.37  ? 65  LYS A C   1 
ATOM   513  O O   . LYS A 1 66 ? 2.372   -15.508 11.296  1.00 32.59  ? 65  LYS A O   1 
ATOM   514  C CB  . LYS A 1 66 ? 4.213   -13.471 9.637   1.00 28.72  ? 65  LYS A CB  1 
ATOM   515  C CG  . LYS A 1 66 ? 4.593   -12.242 10.440  1.00 30.61  ? 65  LYS A CG  1 
ATOM   516  C CD  . LYS A 1 66 ? 6.107   -12.109 10.264  1.00 42.82  ? 65  LYS A CD  1 
ATOM   517  C CE  . LYS A 1 66 ? 6.684   -11.039 11.153  1.00 49.92  ? 65  LYS A CE  1 
ATOM   518  N NZ  . LYS A 1 66 ? 6.223   -9.701  10.763  1.00 59.56  ? 65  LYS A NZ  1 
ATOM   519  N N   A ASP A 1 67 ? 1.677   -13.432 11.841  0.50 33.51  ? 66  ASP A N   1 
ATOM   520  N N   B ASP A 1 67 ? 1.701   -13.425 11.853  0.50 33.13  ? 66  ASP A N   1 
ATOM   521  C CA  A ASP A 1 67 ? 1.181   -13.850 13.145  0.50 35.40  ? 66  ASP A CA  1 
ATOM   522  C CA  B ASP A 1 67 ? 1.151   -13.842 13.137  0.50 34.75  ? 66  ASP A CA  1 
ATOM   523  C C   A ASP A 1 67 ? 0.066   -14.887 12.986  0.50 34.67  ? 66  ASP A C   1 
ATOM   524  C C   B ASP A 1 67 ? 0.134   -14.959 12.915  0.50 34.06  ? 66  ASP A C   1 
ATOM   525  O O   A ASP A 1 67 ? -0.040  -15.820 13.769  0.50 37.38  ? 66  ASP A O   1 
ATOM   526  O O   B ASP A 1 67 ? 0.164   -15.997 13.565  0.50 34.88  ? 66  ASP A O   1 
ATOM   527  C CB  A ASP A 1 67 ? 0.886   -12.650 14.033  0.50 38.98  ? 66  ASP A CB  1 
ATOM   528  C CB  B ASP A 1 67 ? 0.542   -12.667 13.883  0.50 38.19  ? 66  ASP A CB  1 
ATOM   529  C CG  A ASP A 1 67 ? 2.105   -11.923 14.589  0.50 41.80  ? 66  ASP A CG  1 
ATOM   530  C CG  B ASP A 1 67 ? 0.020   -12.973 15.280  0.50 40.88  ? 66  ASP A CG  1 
ATOM   531  O OD1 A ASP A 1 67 ? 3.203   -12.527 14.627  0.50 41.77  ? 66  ASP A OD1 1 
ATOM   532  O OD1 B ASP A 1 67 ? 0.854   -13.255 16.167  0.50 41.51  ? 66  ASP A OD1 1 
ATOM   533  O OD2 A ASP A 1 67 ? 1.958   -10.748 14.972  0.50 45.27  ? 66  ASP A OD2 1 
ATOM   534  O OD2 B ASP A 1 67 ? -1.214  -12.925 15.470  0.50 47.28  ? 66  ASP A OD2 1 
ATOM   535  N N   . LYS A 1 68 ? -0.739  -14.763 11.927  1.00 32.03  ? 67  LYS A N   1 
ATOM   536  C CA  . LYS A 1 68 ? -1.819  -15.692 11.707  1.00 29.36  ? 67  LYS A CA  1 
ATOM   537  C C   . LYS A 1 68 ? -1.389  -16.932 10.944  1.00 30.49  ? 67  LYS A C   1 
ATOM   538  O O   . LYS A 1 68 ? -1.901  -18.021 11.210  1.00 32.52  ? 67  LYS A O   1 
ATOM   539  C CB  . LYS A 1 68 ? -2.863  -14.923 10.910  1.00 30.55  ? 67  LYS A CB  1 
ATOM   540  C CG  . LYS A 1 68 ? -4.119  -15.739 10.722  1.00 32.10  ? 67  LYS A CG  1 
ATOM   541  C CD  . LYS A 1 68 ? -5.185  -14.806 10.136  1.00 36.32  ? 67  LYS A CD  1 
ATOM   542  C CE  . LYS A 1 68 ? -6.553  -15.350 9.839   1.00 43.34  ? 67  LYS A CE  1 
ATOM   543  N NZ  . LYS A 1 68 ? -7.399  -14.302 9.236   1.00 41.26  ? 67  LYS A NZ  1 
ATOM   544  N N   . TYR A 1 69 ? -0.513  -16.778 9.929   1.00 28.70  ? 68  TYR A N   1 
ATOM   545  C CA  . TYR A 1 69 ? -0.296  -17.875 8.985   1.00 28.22  ? 68  TYR A CA  1 
ATOM   546  C C   . TYR A 1 69 ? 1.087   -18.522 9.130   1.00 25.72  ? 68  TYR A C   1 
ATOM   547  O O   . TYR A 1 69 ? 1.327   -19.588 8.577   1.00 29.09  ? 68  TYR A O   1 
ATOM   548  C CB  . TYR A 1 69 ? -0.450  -17.374 7.535   1.00 26.12  ? 68  TYR A CB  1 
ATOM   549  C CG  . TYR A 1 69 ? -1.851  -16.940 7.122   1.00 28.79  ? 68  TYR A CG  1 
ATOM   550  C CD1 . TYR A 1 69 ? -2.977  -17.679 7.505   1.00 27.67  ? 68  TYR A CD1 1 
ATOM   551  C CD2 . TYR A 1 69 ? -2.045  -15.747 6.423   1.00 27.71  ? 68  TYR A CD2 1 
ATOM   552  C CE1 . TYR A 1 69 ? -4.253  -17.295 7.106   1.00 28.62  ? 68  TYR A CE1 1 
ATOM   553  C CE2 . TYR A 1 69 ? -3.317  -15.332 6.051   1.00 30.84  ? 68  TYR A CE2 1 
ATOM   554  C CZ  . TYR A 1 69 ? -4.418  -16.099 6.418   1.00 29.17  ? 68  TYR A CZ  1 
ATOM   555  O OH  . TYR A 1 69 ? -5.645  -15.667 6.002   1.00 29.40  ? 68  TYR A OH  1 
ATOM   556  N N   . GLY A 1 70 ? 1.963   -17.917 9.917   1.00 26.75  ? 69  GLY A N   1 
ATOM   557  C CA  . GLY A 1 70 ? 3.342   -18.384 9.975   1.00 28.20  ? 69  GLY A CA  1 
ATOM   558  C C   . GLY A 1 70 ? 3.554   -19.366 11.134  1.00 30.45  ? 69  GLY A C   1 
ATOM   559  O O   . GLY A 1 70 ? 4.351   -19.104 12.005  1.00 37.82  ? 69  GLY A O   1 
ATOM   560  N N   . LYS A 1 71 ? 2.783   -20.449 11.149  1.00 33.62  ? 70  LYS A N   1 
ATOM   561  C CA  . LYS A 1 71 ? 2.893   -21.488 12.156  1.00 37.55  ? 70  LYS A CA  1 
ATOM   562  C C   . LYS A 1 71 ? 3.195   -22.794 11.434  1.00 32.49  ? 70  LYS A C   1 
ATOM   563  O O   . LYS A 1 71 ? 2.852   -22.964 10.269  1.00 36.59  ? 70  LYS A O   1 
ATOM   564  C CB  . LYS A 1 71 ? 1.621   -21.490 13.015  1.00 39.81  ? 70  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 71 ? 1.502   -20.189 13.816  1.00 40.68  ? 70  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 71 ? 0.680   -20.212 15.099  1.00 48.09  ? 70  LYS A CD  1 
ATOM   567  N N   . PRO A 1 72 ? 3.851   -23.774 12.095  1.00 37.65  ? 71  PRO A N   1 
ATOM   568  C CA  . PRO A 1 72 ? 4.187   -25.035 11.430  1.00 31.86  ? 71  PRO A CA  1 
ATOM   569  C C   . PRO A 1 72 ? 2.985   -25.822 10.937  1.00 33.58  ? 71  PRO A C   1 
ATOM   570  O O   . PRO A 1 72 ? 1.913   -25.749 11.519  1.00 37.54  ? 71  PRO A O   1 
ATOM   571  C CB  . PRO A 1 72 ? 5.010   -25.817 12.479  1.00 39.22  ? 71  PRO A CB  1 
ATOM   572  C CG  . PRO A 1 72 ? 5.473   -24.746 13.444  1.00 41.86  ? 71  PRO A CG  1 
ATOM   573  C CD  . PRO A 1 72 ? 4.376   -23.664 13.459  1.00 39.12  ? 71  PRO A CD  1 
ATOM   574  N N   . ASN A 1 73 ? 3.187   -26.588 9.870   1.00 36.04  ? 72  ASN A N   1 
ATOM   575  C CA  . ASN A 1 73 ? 2.096   -27.276 9.214   1.00 41.94  ? 72  ASN A CA  1 
ATOM   576  C C   . ASN A 1 73 ? 2.656   -28.618 8.781   1.00 48.88  ? 72  ASN A C   1 
ATOM   577  O O   . ASN A 1 73 ? 3.844   -28.731 8.481   1.00 48.37  ? 72  ASN A O   1 
ATOM   578  C CB  . ASN A 1 73 ? 1.529   -26.417 8.080   1.00 42.58  ? 72  ASN A CB  1 
ATOM   579  C CG  . ASN A 1 73 ? 0.214   -26.907 7.515   1.00 50.51  ? 72  ASN A CG  1 
ATOM   580  O OD1 . ASN A 1 73 ? 0.191   -27.790 6.651   1.00 47.25  ? 72  ASN A OD1 1 
ATOM   581  N ND2 . ASN A 1 73 ? -0.893  -26.304 7.933   1.00 50.88  ? 72  ASN A ND2 1 
ATOM   582  N N   . LYS A 1 74 ? 1.783   -29.624 8.764   1.00 50.71  ? 73  LYS A N   1 
ATOM   583  C CA  . LYS A 1 74 ? 2.174   -30.986 8.455   1.00 49.59  ? 73  LYS A CA  1 
ATOM   584  C C   . LYS A 1 74 ? 2.596   -31.120 6.989   1.00 46.93  ? 73  LYS A C   1 
ATOM   585  O O   . LYS A 1 74 ? 3.325   -32.045 6.629   1.00 47.44  ? 73  LYS A O   1 
ATOM   586  C CB  . LYS A 1 74 ? 1.005   -31.881 8.907   1.00 52.89  ? 73  LYS A CB  1 
ATOM   587  C CG  . LYS A 1 74 ? -0.216  -31.968 7.984   1.00 53.66  ? 73  LYS A CG  1 
ATOM   588  N N   . ARG A 1 75 ? 2.147   -30.196 6.129   1.00 43.61  ? 74  ARG A N   1 
ATOM   589  C CA  . ARG A 1 75 ? 2.225   -30.394 4.691   1.00 40.36  ? 74  ARG A CA  1 
ATOM   590  C C   . ARG A 1 75 ? 3.669   -30.377 4.191   1.00 37.50  ? 74  ARG A C   1 
ATOM   591  O O   . ARG A 1 75 ? 4.488   -29.604 4.700   1.00 33.27  ? 74  ARG A O   1 
ATOM   592  C CB  . ARG A 1 75 ? 1.382   -29.319 3.995   1.00 44.68  ? 74  ARG A CB  1 
ATOM   593  C CG  . ARG A 1 75 ? -0.081  -29.584 4.312   1.00 50.34  ? 74  ARG A CG  1 
ATOM   594  C CD  . ARG A 1 75 ? -0.611  -30.749 3.494   1.00 45.08  ? 74  ARG A CD  1 
ATOM   595  N NE  . ARG A 1 75 ? -1.391  -30.287 2.343   1.00 60.81  ? 74  ARG A NE  1 
ATOM   596  C CZ  . ARG A 1 75 ? -2.554  -29.637 2.438   1.00 58.86  ? 74  ARG A CZ  1 
ATOM   597  N NH1 . ARG A 1 75 ? -3.227  -29.361 1.340   1.00 61.83  ? 74  ARG A NH1 1 
ATOM   598  N NH2 . ARG A 1 75 ? -3.058  -29.308 3.620   1.00 62.57  ? 74  ARG A NH2 1 
ATOM   599  N N   . LYS A 1 76 ? 3.924   -31.174 3.139   1.00 32.81  ? 75  LYS A N   1 
ATOM   600  C CA  . LYS A 1 76 ? 5.259   -31.349 2.574   1.00 32.96  ? 75  LYS A CA  1 
ATOM   601  C C   . LYS A 1 76 ? 5.836   -29.991 2.174   1.00 32.52  ? 75  LYS A C   1 
ATOM   602  O O   . LYS A 1 76 ? 5.289   -29.310 1.316   1.00 28.40  ? 75  LYS A O   1 
ATOM   603  C CB  . LYS A 1 76 ? 5.269   -32.292 1.366   1.00 36.67  ? 75  LYS A CB  1 
ATOM   604  C CG  . LYS A 1 76 ? 6.617   -32.592 0.710   1.00 39.99  ? 75  LYS A CG  1 
ATOM   605  C CD  . LYS A 1 76 ? 6.603   -33.733 -0.311  1.00 45.08  ? 75  LYS A CD  1 
ATOM   606  C CE  . LYS A 1 76 ? 8.004   -34.153 -0.658  1.00 52.27  ? 75  LYS A CE  1 
ATOM   607  N N   . GLY A 1 77 ? 6.959   -29.620 2.794   1.00 32.26  ? 76  GLY A N   1 
ATOM   608  C CA  . GLY A 1 77 ? 7.698   -28.448 2.340   1.00 30.59  ? 76  GLY A CA  1 
ATOM   609  C C   . GLY A 1 77 ? 7.360   -27.196 3.141   1.00 28.09  ? 76  GLY A C   1 
ATOM   610  O O   . GLY A 1 77 ? 8.072   -26.207 3.027   1.00 28.59  ? 76  GLY A O   1 
ATOM   611  N N   . PHE A 1 78 ? 6.323   -27.239 3.975   1.00 27.76  ? 77  PHE A N   1 
ATOM   612  C CA  . PHE A 1 78 ? 5.845   -26.023 4.598   1.00 28.65  ? 77  PHE A CA  1 
ATOM   613  C C   . PHE A 1 78 ? 6.859   -25.435 5.589   1.00 32.94  ? 77  PHE A C   1 
ATOM   614  O O   . PHE A 1 78 ? 7.144   -24.234 5.573   1.00 29.41  ? 77  PHE A O   1 
ATOM   615  C CB  . PHE A 1 78 ? 4.466   -26.295 5.208   1.00 29.58  ? 77  PHE A CB  1 
ATOM   616  C CG  . PHE A 1 78 ? 3.740   -25.014 5.594   1.00 30.08  ? 77  PHE A CG  1 
ATOM   617  C CD1 . PHE A 1 78 ? 4.016   -24.345 6.784   1.00 30.19  ? 77  PHE A CD1 1 
ATOM   618  C CD2 . PHE A 1 78 ? 2.812   -24.448 4.720   1.00 29.61  ? 77  PHE A CD2 1 
ATOM   619  C CE1 . PHE A 1 78 ? 3.387   -23.159 7.114   1.00 29.98  ? 77  PHE A CE1 1 
ATOM   620  C CE2 . PHE A 1 78 ? 2.171   -23.262 5.060   1.00 26.99  ? 77  PHE A CE2 1 
ATOM   621  C CZ  . PHE A 1 78 ? 2.434   -22.627 6.253   1.00 25.37  ? 77  PHE A CZ  1 
ATOM   622  N N   . ASN A 1 79 ? 7.369   -26.258 6.514   1.00 28.42  ? 78  ASN A N   1 
ATOM   623  C CA  . ASN A 1 79 ? 8.278   -25.753 7.541   1.00 28.69  ? 78  ASN A CA  1 
ATOM   624  C C   . ASN A 1 79 ? 9.625   -25.299 6.945   1.00 23.91  ? 78  ASN A C   1 
ATOM   625  O O   . ASN A 1 79 ? 10.239  -24.343 7.458   1.00 28.74  ? 78  ASN A O   1 
ATOM   626  C CB  . ASN A 1 79 ? 8.447   -26.815 8.630   1.00 29.54  ? 78  ASN A CB  1 
ATOM   627  C CG  . ASN A 1 79 ? 7.096   -27.123 9.243   1.00 35.61  ? 78  ASN A CG  1 
ATOM   628  O OD1 . ASN A 1 79 ? 6.182   -26.290 9.170   1.00 30.32  ? 78  ASN A OD1 1 
ATOM   629  N ND2 . ASN A 1 79 ? 6.964   -28.281 9.885   1.00 31.62  ? 78  ASN A ND2 1 
ATOM   630  N N   . GLU A 1 80 ? 10.097  -25.989 5.902   1.00 24.60  ? 79  GLU A N   1 
ATOM   631  C CA  . GLU A 1 80 ? 11.239  -25.513 5.144   1.00 24.78  ? 79  GLU A CA  1 
ATOM   632  C C   . GLU A 1 80 ? 10.909  -24.114 4.623   1.00 23.89  ? 79  GLU A C   1 
ATOM   633  O O   . GLU A 1 80 ? 11.765  -23.229 4.645   1.00 24.08  ? 79  GLU A O   1 
ATOM   634  C CB  . GLU A 1 80 ? 11.636  -26.410 3.973   1.00 25.98  ? 79  GLU A CB  1 
ATOM   635  C CG  . GLU A 1 80 ? 12.951  -26.001 3.303   1.00 27.23  ? 79  GLU A CG  1 
ATOM   636  C CD  . GLU A 1 80 ? 13.506  -27.057 2.339   1.00 38.63  ? 79  GLU A CD  1 
ATOM   637  O OE1 . GLU A 1 80 ? 12.858  -28.095 2.090   1.00 39.84  ? 79  GLU A OE1 1 
ATOM   638  O OE2 . GLU A 1 80 ? 14.608  -26.841 1.811   1.00 38.77  ? 79  GLU A OE2 1 
ATOM   639  N N   . GLY A 1 81 ? 9.691   -23.976 4.078   1.00 24.15  ? 80  GLY A N   1 
ATOM   640  C CA  . GLY A 1 81 ? 9.283   -22.686 3.533   1.00 26.01  ? 80  GLY A CA  1 
ATOM   641  C C   . GLY A 1 81 ? 9.299   -21.574 4.584   1.00 23.06  ? 80  GLY A C   1 
ATOM   642  O O   . GLY A 1 81 ? 9.634   -20.428 4.245   1.00 23.00  ? 80  GLY A O   1 
ATOM   643  N N   . LEU A 1 82 ? 8.851   -21.864 5.824   1.00 21.90  ? 81  LEU A N   1 
ATOM   644  C CA  . LEU A 1 82 ? 8.878   -20.864 6.882   1.00 23.42  ? 81  LEU A CA  1 
ATOM   645  C C   . LEU A 1 82 ? 10.314  -20.415 7.151   1.00 23.03  ? 81  LEU A C   1 
ATOM   646  O O   . LEU A 1 82 ? 10.541  -19.209 7.388   1.00 22.34  ? 81  LEU A O   1 
ATOM   647  C CB  . LEU A 1 82 ? 8.203   -21.333 8.176   1.00 25.63  ? 81  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 82 ? 6.708   -21.646 8.049   1.00 28.25  ? 81  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 82 ? 6.356   -22.298 9.374   1.00 28.66  ? 81  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 82 ? 5.826   -20.421 7.771   1.00 26.41  ? 81  LEU A CD2 1 
ATOM   651  N N   . TRP A 1 83 ? 11.282  -21.357 6.993   1.00 23.19  ? 82  TRP A N   1 
ATOM   652  C CA  . TRP A 1 83 ? 12.649  -20.971 7.323   1.00 23.52  ? 82  TRP A CA  1 
ATOM   653  C C   . TRP A 1 83 ? 13.141  -20.020 6.236   1.00 22.89  ? 82  TRP A C   1 
ATOM   654  O O   . TRP A 1 83 ? 13.830  -19.047 6.524   1.00 23.48  ? 82  TRP A O   1 
ATOM   655  C CB  . TRP A 1 83 ? 13.585  -22.198 7.478   1.00 26.44  ? 82  TRP A CB  1 
ATOM   656  C CG  . TRP A 1 83 ? 15.034  -21.840 7.753   1.00 25.20  ? 82  TRP A CG  1 
ATOM   657  C CD1 . TRP A 1 83 ? 15.677  -21.758 8.961   1.00 26.77  ? 82  TRP A CD1 1 
ATOM   658  C CD2 . TRP A 1 83 ? 16.019  -21.505 6.754   1.00 24.04  ? 82  TRP A CD2 1 
ATOM   659  N NE1 . TRP A 1 83 ? 16.986  -21.383 8.771   1.00 27.13  ? 82  TRP A NE1 1 
ATOM   660  C CE2 . TRP A 1 83 ? 17.224  -21.230 7.434   1.00 24.60  ? 82  TRP A CE2 1 
ATOM   661  C CE3 . TRP A 1 83 ? 15.992  -21.427 5.356   1.00 25.05  ? 82  TRP A CE3 1 
ATOM   662  C CZ2 . TRP A 1 83 ? 18.386  -20.868 6.749   1.00 24.84  ? 82  TRP A CZ2 1 
ATOM   663  C CZ3 . TRP A 1 83 ? 17.139  -21.061 4.674   1.00 26.89  ? 82  TRP A CZ3 1 
ATOM   664  C CH2 . TRP A 1 83 ? 18.336  -20.810 5.372   1.00 27.00  ? 82  TRP A CH2 1 
ATOM   665  N N   . GLU A 1 84 ? 12.828  -20.356 4.979   1.00 21.35  ? 83  GLU A N   1 
ATOM   666  C CA  . GLU A 1 84 ? 13.340  -19.646 3.826   1.00 20.06  ? 83  GLU A CA  1 
ATOM   667  C C   . GLU A 1 84 ? 12.812  -18.214 3.866   1.00 22.17  ? 83  GLU A C   1 
ATOM   668  O O   . GLU A 1 84 ? 13.552  -17.259 3.669   1.00 20.71  ? 83  GLU A O   1 
ATOM   669  C CB  . GLU A 1 84 ? 12.898  -20.325 2.540   1.00 20.25  ? 83  GLU A CB  1 
ATOM   670  C CG  . GLU A 1 84 ? 13.581  -21.676 2.388   1.00 20.58  ? 83  GLU A CG  1 
ATOM   671  C CD  . GLU A 1 84 ? 13.198  -22.411 1.106   1.00 25.95  ? 83  GLU A CD  1 
ATOM   672  O OE1 . GLU A 1 84 ? 12.301  -21.981 0.361   1.00 25.87  ? 83  GLU A OE1 1 
ATOM   673  O OE2 . GLU A 1 84 ? 13.861  -23.473 0.796   1.00 26.65  ? 83  GLU A OE2 1 
ATOM   674  N N   . ILE A 1 85 ? 11.490  -18.051 4.084   1.00 19.29  ? 84  ILE A N   1 
ATOM   675  C CA  . ILE A 1 85 ? 10.922  -16.707 4.012   1.00 20.39  ? 84  ILE A CA  1 
ATOM   676  C C   . ILE A 1 85 ? 11.454  -15.785 5.129   1.00 21.38  ? 84  ILE A C   1 
ATOM   677  O O   . ILE A 1 85 ? 11.601  -14.570 4.933   1.00 22.01  ? 84  ILE A O   1 
ATOM   678  C CB  . ILE A 1 85 ? 9.375   -16.746 4.027   1.00 18.56  ? 84  ILE A CB  1 
ATOM   679  C CG1 . ILE A 1 85 ? 8.830   -15.363 3.584   1.00 17.44  ? 84  ILE A CG1 1 
ATOM   680  C CG2 . ILE A 1 85 ? 8.834   -17.067 5.422   1.00 19.38  ? 84  ILE A CG2 1 
ATOM   681  C CD1 . ILE A 1 85 ? 7.385   -15.433 3.021   1.00 18.29  ? 84  ILE A CD1 1 
ATOM   682  N N   . GLN A 1 86 ? 11.807  -16.376 6.287   1.00 21.61  ? 85  GLN A N   1 
ATOM   683  C CA  . GLN A 1 86 ? 12.338  -15.629 7.437   1.00 23.65  ? 85  GLN A CA  1 
ATOM   684  C C   . GLN A 1 86 ? 13.842  -15.366 7.294   1.00 25.42  ? 85  GLN A C   1 
ATOM   685  O O   . GLN A 1 86 ? 14.311  -14.271 7.690   1.00 27.19  ? 85  GLN A O   1 
ATOM   686  C CB  . GLN A 1 86 ? 11.922  -16.361 8.725   1.00 26.27  ? 85  GLN A CB  1 
ATOM   687  C CG  . GLN A 1 86 ? 12.456  -15.741 10.007  1.00 29.18  ? 85  GLN A CG  1 
ATOM   688  C CD  . GLN A 1 86 ? 11.775  -16.292 11.255  1.00 38.31  ? 85  GLN A CD  1 
ATOM   689  O OE1 . GLN A 1 86 ? 11.597  -17.510 11.411  1.00 37.40  ? 85  GLN A OE1 1 
ATOM   690  N NE2 . GLN A 1 86 ? 11.365  -15.396 12.146  1.00 43.69  ? 85  GLN A NE2 1 
ATOM   691  N N   . ASN A 1 87 ? 14.581  -16.330 6.713   1.00 21.65  ? 86  ASN A N   1 
ATOM   692  C CA  . ASN A 1 87 ? 16.039  -16.308 6.831   1.00 18.97  ? 86  ASN A CA  1 
ATOM   693  C C   . ASN A 1 87 ? 16.774  -15.958 5.537   1.00 20.80  ? 86  ASN A C   1 
ATOM   694  O O   . ASN A 1 87 ? 17.874  -15.379 5.624   1.00 22.49  ? 86  ASN A O   1 
ATOM   695  C CB  . ASN A 1 87 ? 16.591  -17.574 7.498   1.00 21.19  ? 86  ASN A CB  1 
ATOM   696  C CG  . ASN A 1 87 ? 16.077  -17.658 8.922   1.00 26.42  ? 86  ASN A CG  1 
ATOM   697  O OD1 . ASN A 1 87 ? 16.383  -16.780 9.747   1.00 30.51  ? 86  ASN A OD1 1 
ATOM   698  N ND2 . ASN A 1 87 ? 15.117  -18.530 9.187   1.00 24.76  ? 86  ASN A ND2 1 
ATOM   699  N N   . ASN A 1 88 ? 16.229  -16.310 4.353   1.00 19.83  ? 87  ASN A N   1 
ATOM   700  C CA  . ASN A 1 88 ? 16.890  -15.952 3.106   1.00 19.05  ? 87  ASN A CA  1 
ATOM   701  C C   . ASN A 1 88 ? 15.840  -15.863 1.989   1.00 20.81  ? 87  ASN A C   1 
ATOM   702  O O   . ASN A 1 88 ? 15.857  -16.616 1.009   1.00 21.18  ? 87  ASN A O   1 
ATOM   703  C CB  . ASN A 1 88 ? 18.076  -16.870 2.793   1.00 21.33  ? 87  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 88 ? 19.108  -16.230 1.893   1.00 25.63  ? 87  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 88 ? 18.843  -15.250 1.188   1.00 22.57  ? 87  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 88 ? 20.335  -16.751 1.921   1.00 27.11  ? 87  ASN A ND2 1 
ATOM   707  N N   . PRO A 1 89 ? 14.870  -14.933 2.121   1.00 19.99  ? 88  PRO A N   1 
ATOM   708  C CA  . PRO A 1 89 ? 13.744  -14.890 1.179   1.00 19.92  ? 88  PRO A CA  1 
ATOM   709  C C   . PRO A 1 89 ? 14.095  -14.458 -0.240  1.00 22.13  ? 88  PRO A C   1 
ATOM   710  O O   . PRO A 1 89 ? 13.283  -14.674 -1.135  1.00 19.31  ? 88  PRO A O   1 
ATOM   711  C CB  . PRO A 1 89 ? 12.799  -13.906 1.851   1.00 19.23  ? 88  PRO A CB  1 
ATOM   712  C CG  . PRO A 1 89 ? 13.711  -12.979 2.620   1.00 19.42  ? 88  PRO A CG  1 
ATOM   713  C CD  . PRO A 1 89 ? 14.805  -13.869 3.135   1.00 18.70  ? 88  PRO A CD  1 
ATOM   714  N N   . HIS A 1 90 ? 15.296  -13.903 -0.465  1.00 19.05  ? 89  HIS A N   1 
ATOM   715  C CA  . HIS A 1 90 ? 15.662  -13.354 -1.775  1.00 18.51  ? 89  HIS A CA  1 
ATOM   716  C C   . HIS A 1 90 ? 16.753  -14.184 -2.465  1.00 19.75  ? 89  HIS A C   1 
ATOM   717  O O   . HIS A 1 90 ? 17.238  -13.780 -3.524  1.00 21.84  ? 89  HIS A O   1 
ATOM   718  C CB  . HIS A 1 90 ? 16.042  -11.865 -1.618  1.00 18.55  ? 89  HIS A CB  1 
ATOM   719  C CG  . HIS A 1 90 ? 14.931  -11.022 -1.078  1.00 18.42  ? 89  HIS A CG  1 
ATOM   720  N ND1 . HIS A 1 90 ? 13.682  -10.907 -1.689  1.00 18.24  ? 89  HIS A ND1 1 
ATOM   721  C CD2 . HIS A 1 90 ? 14.904  -10.273 0.018   1.00 19.19  ? 89  HIS A CD2 1 
ATOM   722  C CE1 . HIS A 1 90 ? 12.946  -10.070 -0.952  1.00 19.58  ? 89  HIS A CE1 1 
ATOM   723  N NE2 . HIS A 1 90 ? 13.664  -9.680  0.084   1.00 21.83  ? 89  HIS A NE2 1 
ATOM   724  N N   . ALA A 1 91 ? 17.011  -15.374 -1.908  1.00 20.14  ? 90  ALA A N   1 
ATOM   725  C CA  . ALA A 1 91 ? 18.074  -16.222 -2.432  1.00 22.31  ? 90  ALA A CA  1 
ATOM   726  C C   . ALA A 1 91 ? 17.634  -16.937 -3.704  1.00 26.76  ? 90  ALA A C   1 
ATOM   727  O O   . ALA A 1 91 ? 16.458  -17.088 -3.995  1.00 23.40  ? 90  ALA A O   1 
ATOM   728  C CB  . ALA A 1 91 ? 18.503  -17.232 -1.405  1.00 23.64  ? 90  ALA A CB  1 
ATOM   729  N N   . SER A 1 92 ? 18.622  -17.437 -4.455  1.00 24.81  ? 91  SER A N   1 
ATOM   730  C CA  . SER A 1 92 ? 18.352  -18.373 -5.529  1.00 27.98  ? 91  SER A CA  1 
ATOM   731  C C   . SER A 1 92 ? 18.066  -19.762 -4.966  1.00 28.59  ? 91  SER A C   1 
ATOM   732  O O   . SER A 1 92 ? 18.879  -20.299 -4.198  1.00 30.86  ? 91  SER A O   1 
ATOM   733  C CB  . SER A 1 92 ? 19.510  -18.390 -6.494  1.00 32.38  ? 91  SER A CB  1 
ATOM   734  O OG  . SER A 1 92 ? 19.344  -19.512 -7.332  1.00 39.53  ? 91  SER A OG  1 
ATOM   735  N N   . TYR A 1 93 ? 16.924  -20.344 -5.379  1.00 25.77  ? 92  TYR A N   1 
ATOM   736  C CA  . TYR A 1 93 ? 16.494  -21.660 -4.929  1.00 27.57  ? 92  TYR A CA  1 
ATOM   737  C C   . TYR A 1 93 ? 16.433  -22.639 -6.105  1.00 34.24  ? 92  TYR A C   1 
ATOM   738  O O   . TYR A 1 93 ? 16.066  -23.787 -5.905  1.00 42.20  ? 92  TYR A O   1 
ATOM   739  C CB  . TYR A 1 93 ? 15.163  -21.601 -4.152  1.00 25.65  ? 92  TYR A CB  1 
ATOM   740  C CG  . TYR A 1 93 ? 15.319  -21.034 -2.748  1.00 25.91  ? 92  TYR A CG  1 
ATOM   741  C CD1 . TYR A 1 93 ? 15.797  -21.807 -1.688  1.00 28.79  ? 92  TYR A CD1 1 
ATOM   742  C CD2 . TYR A 1 93 ? 15.006  -19.701 -2.493  1.00 24.56  ? 92  TYR A CD2 1 
ATOM   743  C CE1 . TYR A 1 93 ? 15.988  -21.265 -0.424  1.00 28.91  ? 92  TYR A CE1 1 
ATOM   744  C CE2 . TYR A 1 93 ? 15.155  -19.164 -1.229  1.00 25.66  ? 92  TYR A CE2 1 
ATOM   745  C CZ  . TYR A 1 93 ? 15.640  -19.941 -0.196  1.00 27.31  ? 92  TYR A CZ  1 
ATOM   746  O OH  . TYR A 1 93 ? 15.916  -19.409 1.023   1.00 25.73  ? 92  TYR A OH  1 
ATOM   747  N N   . SER A 1 94 ? 16.841  -22.191 -7.295  1.00 41.58  ? 93  SER A N   1 
ATOM   748  C CA  . SER A 1 94 ? 16.968  -23.011 -8.495  1.00 55.26  ? 93  SER A CA  1 
ATOM   749  C C   . SER A 1 94 ? 17.974  -24.161 -8.299  1.00 68.46  ? 93  SER A C   1 
ATOM   750  O O   . SER A 1 94 ? 18.801  -24.074 -7.357  1.00 68.56  ? 93  SER A O   1 
ATOM   751  C CB  . SER A 1 94 ? 17.367  -22.162 -9.672  1.00 55.56  ? 93  SER A CB  1 
ATOM   752  O OG  . SER A 1 94 ? 16.266  -21.369 -10.094 1.00 63.85  ? 93  SER A OG  1 
ATOM   753  O OXT . SER A 1 94 ? 17.918  -25.102 -9.126  1.00 85.09  ? 93  SER A OXT 1 
ATOM   754  N N   . MET B 1 2  ? 38.786  -10.957 -42.236 1.00 68.41  ? 1   MET B N   1 
ATOM   755  C CA  . MET B 1 2  ? 38.515  -11.922 -43.335 1.00 66.09  ? 1   MET B CA  1 
ATOM   756  C C   . MET B 1 2  ? 37.013  -12.211 -43.367 1.00 55.46  ? 1   MET B C   1 
ATOM   757  O O   . MET B 1 2  ? 36.460  -12.617 -42.345 1.00 60.69  ? 1   MET B O   1 
ATOM   758  C CB  . MET B 1 2  ? 39.329  -13.206 -43.121 1.00 73.51  ? 1   MET B CB  1 
ATOM   759  C CG  . MET B 1 2  ? 39.411  -14.134 -44.328 1.00 95.33  ? 1   MET B CG  1 
ATOM   760  S SD  . MET B 1 2  ? 40.406  -13.544 -45.717 1.00 101.68 ? 1   MET B SD  1 
ATOM   761  C CE  . MET B 1 2  ? 41.904  -12.985 -44.893 1.00 91.89  ? 1   MET B CE  1 
ATOM   762  N N   . PRO B 1 3  ? 36.299  -12.001 -44.509 1.00 48.88  ? 2   PRO B N   1 
ATOM   763  C CA  . PRO B 1 3  ? 34.852  -12.240 -44.565 1.00 47.49  ? 2   PRO B CA  1 
ATOM   764  C C   . PRO B 1 3  ? 34.540  -13.666 -44.119 1.00 47.18  ? 2   PRO B C   1 
ATOM   765  O O   . PRO B 1 3  ? 35.388  -14.543 -44.242 1.00 44.35  ? 2   PRO B O   1 
ATOM   766  C CB  . PRO B 1 3  ? 34.456  -11.968 -46.018 1.00 48.92  ? 2   PRO B CB  1 
ATOM   767  C CG  . PRO B 1 3  ? 35.566  -11.056 -46.516 1.00 47.10  ? 2   PRO B CG  1 
ATOM   768  C CD  . PRO B 1 3  ? 36.832  -11.503 -45.789 1.00 44.10  ? 2   PRO B CD  1 
ATOM   769  N N   . HIS B 1 4  ? 33.356  -13.850 -43.518 1.00 44.41  ? 3   HIS B N   1 
ATOM   770  C CA  . HIS B 1 4  ? 32.907  -15.171 -43.097 1.00 45.84  ? 3   HIS B CA  1 
ATOM   771  C C   . HIS B 1 4  ? 31.552  -15.479 -43.728 1.00 42.27  ? 3   HIS B C   1 
ATOM   772  O O   . HIS B 1 4  ? 30.951  -14.624 -44.396 1.00 40.05  ? 3   HIS B O   1 
ATOM   773  C CB  . HIS B 1 4  ? 32.989  -15.324 -41.578 1.00 50.30  ? 3   HIS B CB  1 
ATOM   774  C CG  . HIS B 1 4  ? 34.401  -15.410 -41.090 1.00 60.57  ? 3   HIS B CG  1 
ATOM   775  N ND1 . HIS B 1 4  ? 35.337  -16.252 -41.664 1.00 59.79  ? 3   HIS B ND1 1 
ATOM   776  C CD2 . HIS B 1 4  ? 35.033  -14.774 -40.082 1.00 57.23  ? 3   HIS B CD2 1 
ATOM   777  C CE1 . HIS B 1 4  ? 36.492  -16.119 -41.016 1.00 55.84  ? 3   HIS B CE1 1 
ATOM   778  N NE2 . HIS B 1 4  ? 36.330  -15.225 -40.057 1.00 61.28  ? 3   HIS B NE2 1 
ATOM   779  N N   . ALA B 1 5  ? 31.064  -16.714 -43.527 1.00 39.26  ? 4   ALA B N   1 
ATOM   780  C CA  . ALA B 1 5  ? 29.751  -17.044 -44.062 1.00 40.35  ? 4   ALA B CA  1 
ATOM   781  C C   . ALA B 1 5  ? 28.741  -16.014 -43.561 1.00 40.93  ? 4   ALA B C   1 
ATOM   782  O O   . ALA B 1 5  ? 27.866  -15.561 -44.311 1.00 39.98  ? 4   ALA B O   1 
ATOM   783  C CB  . ALA B 1 5  ? 29.365  -18.426 -43.602 1.00 40.84  ? 4   ALA B CB  1 
ATOM   784  N N   . PHE B 1 6  ? 28.881  -15.678 -42.274 1.00 42.62  ? 5   PHE B N   1 
ATOM   785  C CA  . PHE B 1 6  ? 28.083  -14.659 -41.604 1.00 43.76  ? 5   PHE B CA  1 
ATOM   786  C C   . PHE B 1 6  ? 28.956  -13.428 -41.354 1.00 37.68  ? 5   PHE B C   1 
ATOM   787  O O   . PHE B 1 6  ? 30.067  -13.539 -40.831 1.00 41.61  ? 5   PHE B O   1 
ATOM   788  C CB  . PHE B 1 6  ? 27.499  -15.140 -40.267 1.00 41.95  ? 5   PHE B CB  1 
ATOM   789  C CG  . PHE B 1 6  ? 26.406  -16.194 -40.389 1.00 37.55  ? 5   PHE B CG  1 
ATOM   790  C CD1 . PHE B 1 6  ? 25.081  -15.827 -40.610 1.00 32.03  ? 5   PHE B CD1 1 
ATOM   791  C CD2 . PHE B 1 6  ? 26.703  -17.550 -40.286 1.00 39.07  ? 5   PHE B CD2 1 
ATOM   792  C CE1 . PHE B 1 6  ? 24.084  -16.769 -40.738 1.00 32.60  ? 5   PHE B CE1 1 
ATOM   793  C CE2 . PHE B 1 6  ? 25.691  -18.495 -40.422 1.00 31.05  ? 5   PHE B CE2 1 
ATOM   794  C CZ  . PHE B 1 6  ? 24.387  -18.106 -40.617 1.00 30.48  ? 5   PHE B CZ  1 
ATOM   795  N N   . LYS B 1 7  ? 28.425  -12.264 -41.730 1.00 43.87  ? 6   LYS B N   1 
ATOM   796  C CA  . LYS B 1 7  ? 29.103  -11.000 -41.495 1.00 37.53  ? 6   LYS B CA  1 
ATOM   797  C C   . LYS B 1 7  ? 28.267  -10.170 -40.516 1.00 39.82  ? 6   LYS B C   1 
ATOM   798  O O   . LYS B 1 7  ? 27.021  -10.215 -40.542 1.00 35.16  ? 6   LYS B O   1 
ATOM   799  C CB  . LYS B 1 7  ? 29.225  -10.287 -42.843 1.00 43.55  ? 6   LYS B CB  1 
ATOM   800  C CG  . LYS B 1 7  ? 27.899  -9.941  -43.504 1.00 42.26  ? 6   LYS B CG  1 
ATOM   801  C CD  . LYS B 1 7  ? 28.079  -9.364  -44.910 1.00 49.34  ? 6   LYS B CD  1 
ATOM   802  C CE  . LYS B 1 7  ? 26.840  -8.818  -45.548 1.00 51.60  ? 6   LYS B CE  1 
ATOM   803  N NZ  . LYS B 1 7  ? 25.858  -9.837  -45.947 1.00 57.16  ? 6   LYS B NZ  1 
ATOM   804  N N   . PRO B 1 8  ? 28.934  -9.307  -39.712 1.00 40.71  ? 7   PRO B N   1 
ATOM   805  C CA  . PRO B 1 8  ? 28.257  -8.330  -38.846 1.00 34.88  ? 7   PRO B CA  1 
ATOM   806  C C   . PRO B 1 8  ? 27.116  -7.612  -39.539 1.00 33.27  ? 7   PRO B C   1 
ATOM   807  O O   . PRO B 1 8  ? 27.266  -7.133  -40.672 1.00 37.51  ? 7   PRO B O   1 
ATOM   808  C CB  . PRO B 1 8  ? 29.448  -7.404  -38.590 1.00 42.06  ? 7   PRO B CB  1 
ATOM   809  C CG  . PRO B 1 8  ? 30.599  -8.380  -38.402 1.00 42.92  ? 7   PRO B CG  1 
ATOM   810  C CD  . PRO B 1 8  ? 30.402  -9.167  -39.663 1.00 45.61  ? 7   PRO B CD  1 
ATOM   811  N N   . GLY B 1 9  ? 25.966  -7.550  -38.852 1.00 28.54  ? 8   GLY B N   1 
ATOM   812  C CA  . GLY B 1 9  ? 24.742  -6.923  -39.332 1.00 30.17  ? 8   GLY B CA  1 
ATOM   813  C C   . GLY B 1 9  ? 23.776  -7.887  -40.020 1.00 26.68  ? 8   GLY B C   1 
ATOM   814  O O   . GLY B 1 9  ? 22.636  -7.520  -40.322 1.00 30.71  ? 8   GLY B O   1 
ATOM   815  N N   . ASP B 1 10 ? 24.232  -9.118  -40.323 1.00 28.16  ? 9   ASP B N   1 
ATOM   816  C CA  . ASP B 1 10 ? 23.315  -10.112 -40.852 1.00 29.16  ? 9   ASP B CA  1 
ATOM   817  C C   . ASP B 1 10 ? 22.246  -10.457 -39.798 1.00 22.75  ? 9   ASP B C   1 
ATOM   818  O O   . ASP B 1 10 ? 22.542  -10.508 -38.606 1.00 28.03  ? 9   ASP B O   1 
ATOM   819  C CB  . ASP B 1 10 ? 24.030  -11.421 -41.145 1.00 29.16  ? 9   ASP B CB  1 
ATOM   820  C CG  . ASP B 1 10 ? 24.764  -11.515 -42.482 1.00 42.18  ? 9   ASP B CG  1 
ATOM   821  O OD1 . ASP B 1 10 ? 24.428  -10.726 -43.397 1.00 38.43  ? 9   ASP B OD1 1 
ATOM   822  O OD2 . ASP B 1 10 ? 25.639  -12.412 -42.591 1.00 36.61  ? 9   ASP B OD2 1 
ATOM   823  N N   . LEU B 1 11 ? 21.017  -10.606 -40.266 1.00 25.19  ? 10  LEU B N   1 
ATOM   824  C CA  . LEU B 1 11 ? 19.915  -10.845 -39.340 1.00 25.20  ? 10  LEU B CA  1 
ATOM   825  C C   . LEU B 1 11 ? 19.646  -12.343 -39.353 1.00 28.05  ? 10  LEU B C   1 
ATOM   826  O O   . LEU B 1 11 ? 19.709  -12.924 -40.443 1.00 28.93  ? 10  LEU B O   1 
ATOM   827  C CB  . LEU B 1 11 ? 18.707  -10.056 -39.812 1.00 27.16  ? 10  LEU B CB  1 
ATOM   828  C CG  . LEU B 1 11 ? 18.955  -8.547  -39.927 1.00 26.67  ? 10  LEU B CG  1 
ATOM   829  C CD1 . LEU B 1 11 ? 17.611  -7.890  -40.241 1.00 28.17  ? 10  LEU B CD1 1 
ATOM   830  C CD2 . LEU B 1 11 ? 19.650  -8.074  -38.656 1.00 25.44  ? 10  LEU B CD2 1 
ATOM   831  N N   . VAL B 1 12 ? 19.233  -12.912 -38.200 1.00 23.94  ? 11  VAL B N   1 
ATOM   832  C CA  . VAL B 1 12 ? 19.062  -14.368 -38.086 1.00 21.92  ? 11  VAL B CA  1 
ATOM   833  C C   . VAL B 1 12 ? 17.945  -14.646 -37.078 1.00 25.71  ? 11  VAL B C   1 
ATOM   834  O O   . VAL B 1 12 ? 17.545  -13.751 -36.332 1.00 23.79  ? 11  VAL B O   1 
ATOM   835  C CB  . VAL B 1 12 ? 20.378  -15.036 -37.622 1.00 23.35  ? 11  VAL B CB  1 
ATOM   836  C CG1 . VAL B 1 12 ? 21.521  -14.931 -38.666 1.00 25.06  ? 11  VAL B CG1 1 
ATOM   837  C CG2 . VAL B 1 12 ? 20.856  -14.610 -36.223 1.00 24.23  ? 11  VAL B CG2 1 
ATOM   838  N N   . PHE B 1 13 ? 17.476  -15.904 -37.022 1.00 23.58  ? 12  PHE B N   1 
ATOM   839  C CA  . PHE B 1 13 ? 16.995  -16.408 -35.752 1.00 25.47  ? 12  PHE B CA  1 
ATOM   840  C C   . PHE B 1 13 ? 18.071  -17.297 -35.156 1.00 24.36  ? 12  PHE B C   1 
ATOM   841  O O   . PHE B 1 13 ? 18.709  -18.075 -35.901 1.00 25.68  ? 12  PHE B O   1 
ATOM   842  C CB  . PHE B 1 13 ? 15.727  -17.226 -35.951 1.00 24.64  ? 12  PHE B CB  1 
ATOM   843  C CG  . PHE B 1 13 ? 14.532  -16.402 -36.389 1.00 27.41  ? 12  PHE B CG  1 
ATOM   844  C CD1 . PHE B 1 13 ? 14.336  -16.128 -37.738 1.00 28.23  ? 12  PHE B CD1 1 
ATOM   845  C CD2 . PHE B 1 13 ? 13.617  -15.913 -35.460 1.00 28.45  ? 12  PHE B CD2 1 
ATOM   846  C CE1 . PHE B 1 13 ? 13.242  -15.392 -38.154 1.00 30.79  ? 12  PHE B CE1 1 
ATOM   847  C CE2 . PHE B 1 13 ? 12.513  -15.177 -35.878 1.00 29.09  ? 12  PHE B CE2 1 
ATOM   848  C CZ  . PHE B 1 13 ? 12.333  -14.915 -37.230 1.00 32.99  ? 12  PHE B CZ  1 
ATOM   849  N N   . ALA B 1 14 ? 18.320  -17.122 -33.841 1.00 21.73  ? 13  ALA B N   1 
ATOM   850  C CA  . ALA B 1 14 ? 19.344  -17.864 -33.136 1.00 24.36  ? 13  ALA B CA  1 
ATOM   851  C C   . ALA B 1 14 ? 18.711  -18.807 -32.114 1.00 23.60  ? 13  ALA B C   1 
ATOM   852  O O   . ALA B 1 14 ? 17.812  -18.421 -31.369 1.00 24.13  ? 13  ALA B O   1 
ATOM   853  C CB  . ALA B 1 14 ? 20.345  -16.926 -32.474 1.00 23.84  ? 13  ALA B CB  1 
ATOM   854  N N   . LYS B 1 15 ? 19.241  -20.025 -32.043 1.00 23.50  ? 14  LYS B N   1 
ATOM   855  C CA  . LYS B 1 15 ? 18.621  -21.070 -31.224 1.00 25.20  ? 14  LYS B CA  1 
ATOM   856  C C   . LYS B 1 15 ? 19.508  -21.383 -30.029 1.00 26.68  ? 14  LYS B C   1 
ATOM   857  O O   . LYS B 1 15 ? 20.695  -21.693 -30.176 1.00 28.94  ? 14  LYS B O   1 
ATOM   858  C CB  . LYS B 1 15 ? 18.394  -22.333 -32.075 1.00 26.48  ? 14  LYS B CB  1 
ATOM   859  C CG  . LYS B 1 15 ? 17.700  -23.482 -31.273 1.00 24.20  ? 14  LYS B CG  1 
ATOM   860  C CD  . LYS B 1 15 ? 16.215  -23.173 -31.069 1.00 28.73  ? 14  LYS B CD  1 
ATOM   861  C CE  . LYS B 1 15 ? 15.336  -24.251 -30.354 1.00 28.13  ? 14  LYS B CE  1 
ATOM   862  N NZ  . LYS B 1 15 ? 15.897  -24.440 -29.021 1.00 26.86  ? 14  LYS B NZ  1 
ATOM   863  N N   . MET B 1 16 ? 18.896  -21.289 -28.838 1.00 28.25  ? 15  MET B N   1 
ATOM   864  C CA  . MET B 1 16 ? 19.524  -21.663 -27.575 1.00 29.72  ? 15  MET B CA  1 
ATOM   865  C C   . MET B 1 16 ? 18.673  -22.756 -26.922 1.00 29.99  ? 15  MET B C   1 
ATOM   866  O O   . MET B 1 16 ? 17.445  -22.747 -27.034 1.00 26.39  ? 15  MET B O   1 
ATOM   867  C CB  . MET B 1 16 ? 19.567  -20.487 -26.588 1.00 33.82  ? 15  MET B CB  1 
ATOM   868  C CG  . MET B 1 16 ? 20.170  -19.210 -27.112 1.00 43.71  ? 15  MET B CG  1 
ATOM   869  S SD  . MET B 1 16 ? 21.935  -19.063 -26.778 1.00 51.40  ? 15  MET B SD  1 
ATOM   870  C CE  . MET B 1 16 ? 22.028  -18.985 -24.985 1.00 49.12  ? 15  MET B CE  1 
ATOM   871  N N   . LYS B 1 17 ? 19.330  -23.719 -26.263 1.00 32.87  ? 16  LYS B N   1 
ATOM   872  C CA  . LYS B 1 17 ? 18.581  -24.767 -25.575 1.00 31.77  ? 16  LYS B CA  1 
ATOM   873  C C   . LYS B 1 17 ? 17.596  -24.133 -24.584 1.00 29.74  ? 16  LYS B C   1 
ATOM   874  O O   . LYS B 1 17 ? 17.983  -23.247 -23.833 1.00 31.17  ? 16  LYS B O   1 
ATOM   875  C CB  . LYS B 1 17 ? 19.609  -25.613 -24.806 1.00 38.35  ? 16  LYS B CB  1 
ATOM   876  C CG  . LYS B 1 17 ? 19.038  -26.910 -24.189 1.00 43.07  ? 16  LYS B CG  1 
ATOM   877  C CD  . LYS B 1 17 ? 20.073  -27.763 -23.461 1.00 46.33  ? 16  LYS B CD  1 
ATOM   878  N N   . GLY B 1 18 ? 16.325  -24.558 -24.635 1.00 33.03  ? 17  GLY B N   1 
ATOM   879  C CA  . GLY B 1 18 ? 15.279  -24.103 -23.721 1.00 32.90  ? 17  GLY B CA  1 
ATOM   880  C C   . GLY B 1 18 ? 14.475  -22.898 -24.233 1.00 33.80  ? 17  GLY B C   1 
ATOM   881  O O   . GLY B 1 18 ? 13.538  -22.433 -23.567 1.00 30.33  ? 17  GLY B O   1 
ATOM   882  N N   . TYR B 1 19 ? 14.825  -22.372 -25.420 1.00 31.06  ? 18  TYR B N   1 
ATOM   883  C CA  . TYR B 1 19 ? 14.119  -21.193 -25.910 1.00 26.50  ? 18  TYR B CA  1 
ATOM   884  C C   . TYR B 1 19 ? 13.759  -21.385 -27.383 1.00 27.98  ? 18  TYR B C   1 
ATOM   885  O O   . TYR B 1 19 ? 14.466  -22.104 -28.093 1.00 28.35  ? 18  TYR B O   1 
ATOM   886  C CB  . TYR B 1 19 ? 15.053  -19.977 -25.886 1.00 29.31  ? 18  TYR B CB  1 
ATOM   887  C CG  . TYR B 1 19 ? 15.577  -19.642 -24.495 1.00 28.93  ? 18  TYR B CG  1 
ATOM   888  C CD1 . TYR B 1 19 ? 14.819  -18.893 -23.595 1.00 30.38  ? 18  TYR B CD1 1 
ATOM   889  C CD2 . TYR B 1 19 ? 16.768  -20.191 -24.037 1.00 29.32  ? 18  TYR B CD2 1 
ATOM   890  C CE1 . TYR B 1 19 ? 15.296  -18.627 -22.311 1.00 30.70  ? 18  TYR B CE1 1 
ATOM   891  C CE2 . TYR B 1 19 ? 17.262  -19.910 -22.769 1.00 31.07  ? 18  TYR B CE2 1 
ATOM   892  C CZ  . TYR B 1 19 ? 16.502  -19.156 -21.889 1.00 31.92  ? 18  TYR B CZ  1 
ATOM   893  O OH  . TYR B 1 19 ? 17.027  -18.912 -20.645 1.00 36.85  ? 18  TYR B OH  1 
ATOM   894  N N   . PRO B 1 20 ? 12.710  -20.705 -27.895 1.00 27.20  ? 19  PRO B N   1 
ATOM   895  C CA  . PRO B 1 20 ? 12.357  -20.764 -29.319 1.00 26.48  ? 19  PRO B CA  1 
ATOM   896  C C   . PRO B 1 20 ? 13.439  -20.043 -30.131 1.00 24.67  ? 19  PRO B C   1 
ATOM   897  O O   . PRO B 1 20 ? 14.153  -19.210 -29.575 1.00 25.58  ? 19  PRO B O   1 
ATOM   898  C CB  . PRO B 1 20 ? 11.021  -20.065 -29.392 1.00 25.99  ? 19  PRO B CB  1 
ATOM   899  C CG  . PRO B 1 20 ? 11.011  -19.115 -28.197 1.00 28.15  ? 19  PRO B CG  1 
ATOM   900  C CD  . PRO B 1 20 ? 11.825  -19.824 -27.104 1.00 25.28  ? 19  PRO B CD  1 
ATOM   901  N N   . HIS B 1 21 ? 13.588  -20.431 -31.409 1.00 24.62  ? 20  HIS B N   1 
ATOM   902  C CA  . HIS B 1 21 ? 14.415  -19.666 -32.372 1.00 23.57  ? 20  HIS B CA  1 
ATOM   903  C C   . HIS B 1 21 ? 14.158  -18.159 -32.199 1.00 22.81  ? 20  HIS B C   1 
ATOM   904  O O   . HIS B 1 21 ? 13.014  -17.718 -32.290 1.00 23.88  ? 20  HIS B O   1 
ATOM   905  C CB  . HIS B 1 21 ? 14.054  -20.113 -33.796 1.00 24.99  ? 20  HIS B CB  1 
ATOM   906  C CG  . HIS B 1 21 ? 14.294  -21.589 -33.987 1.00 25.88  ? 20  HIS B CG  1 
ATOM   907  N ND1 . HIS B 1 21 ? 13.413  -22.573 -33.529 1.00 25.49  ? 20  HIS B ND1 1 
ATOM   908  C CD2 . HIS B 1 21 ? 15.333  -22.246 -34.550 1.00 26.81  ? 20  HIS B CD2 1 
ATOM   909  C CE1 . HIS B 1 21 ? 13.910  -23.764 -33.820 1.00 26.18  ? 20  HIS B CE1 1 
ATOM   910  N NE2 . HIS B 1 21 ? 15.074  -23.608 -34.451 1.00 23.83  ? 20  HIS B NE2 1 
ATOM   911  N N   . TRP B 1 22 ? 15.219  -17.381 -31.950 1.00 23.16  ? 21  TRP B N   1 
ATOM   912  C CA  . TRP B 1 22 ? 15.013  -16.048 -31.375 1.00 21.44  ? 21  TRP B CA  1 
ATOM   913  C C   . TRP B 1 22 ? 15.510  -14.964 -32.345 1.00 23.73  ? 21  TRP B C   1 
ATOM   914  O O   . TRP B 1 22 ? 16.622  -15.095 -32.830 1.00 24.39  ? 21  TRP B O   1 
ATOM   915  C CB  . TRP B 1 22 ? 15.789  -15.946 -30.060 1.00 21.93  ? 21  TRP B CB  1 
ATOM   916  C CG  . TRP B 1 22 ? 15.278  -14.797 -29.223 1.00 22.15  ? 21  TRP B CG  1 
ATOM   917  C CD1 . TRP B 1 22 ? 15.532  -13.451 -29.375 1.00 23.41  ? 21  TRP B CD1 1 
ATOM   918  C CD2 . TRP B 1 22 ? 14.352  -14.913 -28.110 1.00 24.14  ? 21  TRP B CD2 1 
ATOM   919  N NE1 . TRP B 1 22 ? 14.802  -12.729 -28.444 1.00 25.73  ? 21  TRP B NE1 1 
ATOM   920  C CE2 . TRP B 1 22 ? 14.089  -13.595 -27.650 1.00 22.79  ? 21  TRP B CE2 1 
ATOM   921  C CE3 . TRP B 1 22 ? 13.738  -16.006 -27.461 1.00 26.25  ? 21  TRP B CE3 1 
ATOM   922  C CZ2 . TRP B 1 22 ? 13.235  -13.325 -26.572 1.00 23.31  ? 21  TRP B CZ2 1 
ATOM   923  C CZ3 . TRP B 1 22 ? 12.896  -15.728 -26.398 1.00 25.38  ? 21  TRP B CZ3 1 
ATOM   924  C CH2 . TRP B 1 22 ? 12.641  -14.416 -25.978 1.00 23.79  ? 21  TRP B CH2 1 
ATOM   925  N N   . PRO B 1 23 ? 14.747  -13.883 -32.661 1.00 24.12  ? 22  PRO B N   1 
ATOM   926  C CA  . PRO B 1 23 ? 15.231  -12.860 -33.609 1.00 22.42  ? 22  PRO B CA  1 
ATOM   927  C C   . PRO B 1 23 ? 16.524  -12.239 -33.091 1.00 23.88  ? 22  PRO B C   1 
ATOM   928  O O   . PRO B 1 23 ? 16.628  -11.835 -31.931 1.00 23.32  ? 22  PRO B O   1 
ATOM   929  C CB  . PRO B 1 23 ? 14.080  -11.825 -33.672 1.00 22.09  ? 22  PRO B CB  1 
ATOM   930  C CG  . PRO B 1 23 ? 13.371  -12.020 -32.340 1.00 23.12  ? 22  PRO B CG  1 
ATOM   931  C CD  . PRO B 1 23 ? 13.428  -13.546 -32.108 1.00 21.94  ? 22  PRO B CD  1 
ATOM   932  N N   . ALA B 1 24 ? 17.557  -12.171 -33.942 1.00 21.48  ? 23  ALA B N   1 
ATOM   933  C CA  . ALA B 1 24 ? 18.877  -11.800 -33.462 1.00 21.85  ? 23  ALA B CA  1 
ATOM   934  C C   . ALA B 1 24 ? 19.709  -11.244 -34.630 1.00 22.22  ? 23  ALA B C   1 
ATOM   935  O O   . ALA B 1 24 ? 19.235  -11.236 -35.760 1.00 24.44  ? 23  ALA B O   1 
ATOM   936  C CB  . ALA B 1 24 ? 19.588  -12.958 -32.795 1.00 24.37  ? 23  ALA B CB  1 
ATOM   937  N N   . ARG B 1 25 ? 20.882  -10.693 -34.298 1.00 24.64  ? 24  ARG B N   1 
ATOM   938  C CA  . ARG B 1 25 ? 21.837  -10.226 -35.313 1.00 24.57  ? 24  ARG B CA  1 
ATOM   939  C C   . ARG B 1 25 ? 23.245  -10.707 -34.978 1.00 24.53  ? 24  ARG B C   1 
ATOM   940  O O   . ARG B 1 25 ? 23.623  -10.967 -33.840 1.00 24.63  ? 24  ARG B O   1 
ATOM   941  C CB  . ARG B 1 25 ? 21.828  -8.702  -35.491 1.00 25.29  ? 24  ARG B CB  1 
ATOM   942  C CG  . ARG B 1 25 ? 22.413  -7.940  -34.305 1.00 24.83  ? 24  ARG B CG  1 
ATOM   943  C CD  . ARG B 1 25 ? 22.153  -6.420  -34.418 1.00 24.19  ? 24  ARG B CD  1 
ATOM   944  N NE  . ARG B 1 25 ? 22.828  -5.737  -33.319 1.00 27.74  ? 24  ARG B NE  1 
ATOM   945  C CZ  . ARG B 1 25 ? 22.535  -4.484  -32.917 1.00 27.71  ? 24  ARG B CZ  1 
ATOM   946  N NH1 . ARG B 1 25 ? 21.564  -3.811  -33.521 1.00 27.57  ? 24  ARG B NH1 1 
ATOM   947  N NH2 . ARG B 1 25 ? 23.219  -3.943  -31.931 1.00 25.04  ? 24  ARG B NH2 1 
ATOM   948  N N   . ILE B 1 26 ? 24.094  -10.778 -36.032 1.00 24.58  ? 25  ILE B N   1 
ATOM   949  C CA  . ILE B 1 26 ? 25.502  -10.966 -35.791 1.00 27.53  ? 25  ILE B CA  1 
ATOM   950  C C   . ILE B 1 26 ? 26.070  -9.599  -35.441 1.00 31.58  ? 25  ILE B C   1 
ATOM   951  O O   . ILE B 1 26 ? 25.834  -8.649  -36.183 1.00 35.37  ? 25  ILE B O   1 
ATOM   952  C CB  . ILE B 1 26 ? 26.148  -11.449 -37.106 1.00 31.96  ? 25  ILE B CB  1 
ATOM   953  C CG1 . ILE B 1 26 ? 25.405  -12.655 -37.706 1.00 31.65  ? 25  ILE B CG1 1 
ATOM   954  C CG2 . ILE B 1 26 ? 27.647  -11.679 -36.943 1.00 35.38  ? 25  ILE B CG2 1 
ATOM   955  C CD1 . ILE B 1 26 ? 25.377  -13.903 -36.833 1.00 30.04  ? 25  ILE B CD1 1 
ATOM   956  N N   . ASP B 1 27 ? 26.862  -9.564  -34.373 1.00 30.50  ? 26  ASP B N   1 
ATOM   957  C CA  . ASP B 1 27 ? 27.542  -8.337  -33.948 1.00 39.56  ? 26  ASP B CA  1 
ATOM   958  C C   . ASP B 1 27 ? 29.017  -8.337  -34.385 1.00 43.02  ? 26  ASP B C   1 
ATOM   959  O O   . ASP B 1 27 ? 29.557  -9.389  -34.708 1.00 43.97  ? 26  ASP B O   1 
ATOM   960  C CB  . ASP B 1 27 ? 27.439  -8.180  -32.442 1.00 34.32  ? 26  ASP B CB  1 
ATOM   961  C CG  . ASP B 1 27 ? 26.232  -7.430  -31.892 1.00 38.41  ? 26  ASP B CG  1 
ATOM   962  O OD1 . ASP B 1 27 ? 25.409  -6.927  -32.701 1.00 36.63  ? 26  ASP B OD1 1 
ATOM   963  O OD2 . ASP B 1 27 ? 26.147  -7.339  -30.637 1.00 36.24  ? 26  ASP B OD2 1 
ATOM   964  N N   . ASP B 1 28 ? 29.682  -7.161  -34.345 1.00 51.54  ? 27  ASP B N   1 
ATOM   965  C CA  . ASP B 1 28 ? 31.141  -7.050  -34.436 1.00 60.08  ? 27  ASP B CA  1 
ATOM   966  C C   . ASP B 1 28 ? 31.793  -7.445  -33.110 1.00 56.70  ? 27  ASP B C   1 
ATOM   967  O O   . ASP B 1 28 ? 31.100  -7.625  -32.108 1.00 61.32  ? 27  ASP B O   1 
ATOM   968  C CB  . ASP B 1 28 ? 31.595  -5.616  -34.660 1.00 60.53  ? 27  ASP B CB  1 
ATOM   969  C CG  . ASP B 1 28 ? 31.086  -4.948  -35.925 1.00 69.10  ? 27  ASP B CG  1 
ATOM   970  O OD1 . ASP B 1 28 ? 31.677  -5.200  -37.007 1.00 66.09  ? 27  ASP B OD1 1 
ATOM   971  O OD2 . ASP B 1 28 ? 30.102  -4.184  -35.813 1.00 71.23  ? 27  ASP B OD2 1 
ATOM   972  N N   . ILE B 1 29 ? 33.134  -7.522  -33.093 1.00 64.56  ? 28  ILE B N   1 
ATOM   973  C CA  . ILE B 1 29 ? 33.867  -7.982  -31.917 1.00 69.63  ? 28  ILE B CA  1 
ATOM   974  C C   . ILE B 1 29 ? 34.207  -6.791  -30.998 1.00 72.77  ? 28  ILE B C   1 
ATOM   975  O O   . ILE B 1 29 ? 34.863  -5.840  -31.484 1.00 76.92  ? 28  ILE B O   1 
ATOM   976  C CB  . ILE B 1 29 ? 35.112  -8.807  -32.301 1.00 62.56  ? 28  ILE B CB  1 
ATOM   977  N N   . VAL B 1 34 ? 36.876  -9.785  -25.207 1.00 62.46  ? 33  VAL B N   1 
ATOM   978  C CA  . VAL B 1 34 ? 36.703  -11.253 -25.431 1.00 66.86  ? 33  VAL B CA  1 
ATOM   979  C C   . VAL B 1 34 ? 36.547  -11.456 -26.932 1.00 70.62  ? 33  VAL B C   1 
ATOM   980  O O   . VAL B 1 34 ? 35.980  -10.602 -27.613 1.00 83.80  ? 33  VAL B O   1 
ATOM   981  C CB  . VAL B 1 34 ? 35.481  -11.767 -24.637 1.00 65.30  ? 33  VAL B CB  1 
ATOM   982  C CG1 . VAL B 1 34 ? 34.197  -11.019 -24.991 1.00 67.11  ? 33  VAL B CG1 1 
ATOM   983  C CG2 . VAL B 1 34 ? 35.285  -13.278 -24.752 1.00 53.50  ? 33  VAL B CG2 1 
ATOM   984  N N   . LYS B 1 35 ? 37.101  -12.554 -27.453 1.00 69.87  ? 34  LYS B N   1 
ATOM   985  C CA  . LYS B 1 35 ? 36.814  -12.952 -28.825 1.00 61.35  ? 34  LYS B CA  1 
ATOM   986  C C   . LYS B 1 35 ? 35.943  -14.211 -28.795 1.00 62.48  ? 34  LYS B C   1 
ATOM   987  O O   . LYS B 1 35 ? 36.048  -15.018 -27.864 1.00 56.96  ? 34  LYS B O   1 
ATOM   988  C CB  . LYS B 1 35 ? 38.105  -13.075 -29.643 1.00 61.68  ? 34  LYS B CB  1 
ATOM   989  N N   . PRO B 1 36 ? 35.034  -14.426 -29.785 1.00 59.74  ? 35  PRO B N   1 
ATOM   990  C CA  . PRO B 1 36 ? 34.230  -15.653 -29.810 1.00 51.65  ? 35  PRO B CA  1 
ATOM   991  C C   . PRO B 1 36 ? 35.167  -16.852 -29.749 1.00 47.12  ? 35  PRO B C   1 
ATOM   992  O O   . PRO B 1 36 ? 36.291  -16.769 -30.232 1.00 50.77  ? 35  PRO B O   1 
ATOM   993  C CB  . PRO B 1 36 ? 33.452  -15.580 -31.139 1.00 52.15  ? 35  PRO B CB  1 
ATOM   994  C CG  . PRO B 1 36 ? 34.136  -14.472 -31.938 1.00 57.44  ? 35  PRO B CG  1 
ATOM   995  C CD  . PRO B 1 36 ? 34.740  -13.519 -30.912 1.00 51.76  ? 35  PRO B CD  1 
ATOM   996  N N   . PRO B 1 37 ? 34.778  -17.987 -29.127 1.00 48.02  ? 36  PRO B N   1 
ATOM   997  C CA  . PRO B 1 37 ? 35.557  -19.212 -29.270 1.00 49.41  ? 36  PRO B CA  1 
ATOM   998  C C   . PRO B 1 37 ? 35.596  -19.552 -30.759 1.00 56.48  ? 36  PRO B C   1 
ATOM   999  O O   . PRO B 1 37 ? 34.777  -19.053 -31.542 1.00 52.54  ? 36  PRO B O   1 
ATOM   1000 C CB  . PRO B 1 37 ? 34.833  -20.290 -28.435 1.00 50.94  ? 36  PRO B CB  1 
ATOM   1001 C CG  . PRO B 1 37 ? 33.659  -19.585 -27.764 1.00 51.56  ? 36  PRO B CG  1 
ATOM   1002 C CD  . PRO B 1 37 ? 33.599  -18.145 -28.258 1.00 50.19  ? 36  PRO B CD  1 
ATOM   1003 N N   . PRO B 1 38 ? 36.551  -20.405 -31.203 1.00 59.15  ? 37  PRO B N   1 
ATOM   1004 C CA  . PRO B 1 38 ? 36.607  -20.835 -32.610 1.00 57.69  ? 37  PRO B CA  1 
ATOM   1005 C C   . PRO B 1 38 ? 35.265  -21.306 -33.186 1.00 50.04  ? 37  PRO B C   1 
ATOM   1006 O O   . PRO B 1 38 ? 34.502  -21.991 -32.506 1.00 47.05  ? 37  PRO B O   1 
ATOM   1007 C CB  . PRO B 1 38 ? 37.656  -21.974 -32.583 1.00 60.73  ? 37  PRO B CB  1 
ATOM   1008 C CG  . PRO B 1 38 ? 38.523  -21.685 -31.362 1.00 54.69  ? 37  PRO B CG  1 
ATOM   1009 C CD  . PRO B 1 38 ? 37.614  -20.991 -30.362 1.00 60.60  ? 37  PRO B CD  1 
ATOM   1010 N N   . ASN B 1 39 ? 34.984  -20.909 -34.437 1.00 50.52  ? 38  ASN B N   1 
ATOM   1011 C CA  . ASN B 1 39 ? 33.815  -21.355 -35.195 1.00 52.47  ? 38  ASN B CA  1 
ATOM   1012 C C   . ASN B 1 39 ? 32.517  -20.649 -34.779 1.00 45.86  ? 38  ASN B C   1 
ATOM   1013 O O   . ASN B 1 39 ? 31.476  -20.907 -35.374 1.00 42.63  ? 38  ASN B O   1 
ATOM   1014 C CB  . ASN B 1 39 ? 33.575  -22.860 -35.082 1.00 54.33  ? 38  ASN B CB  1 
ATOM   1015 C CG  . ASN B 1 39 ? 34.786  -23.697 -35.431 1.00 63.38  ? 38  ASN B CG  1 
ATOM   1016 O OD1 . ASN B 1 39 ? 35.066  -24.686 -34.744 1.00 68.55  ? 38  ASN B OD1 1 
ATOM   1017 N ND2 . ASN B 1 39 ? 35.494  -23.350 -36.499 1.00 58.77  ? 38  ASN B ND2 1 
ATOM   1018 N N   . LYS B 1 40 ? 32.553  -19.772 -33.760 1.00 43.97  ? 39  LYS B N   1 
ATOM   1019 C CA  . LYS B 1 40 ? 31.337  -19.148 -33.257 1.00 39.25  ? 39  LYS B CA  1 
ATOM   1020 C C   . LYS B 1 40 ? 31.344  -17.651 -33.535 1.00 36.37  ? 39  LYS B C   1 
ATOM   1021 O O   . LYS B 1 40 ? 32.386  -17.086 -33.828 1.00 40.47  ? 39  LYS B O   1 
ATOM   1022 C CB  . LYS B 1 40 ? 31.263  -19.422 -31.755 1.00 41.43  ? 39  LYS B CB  1 
ATOM   1023 C CG  . LYS B 1 40 ? 31.046  -20.887 -31.404 1.00 43.66  ? 39  LYS B CG  1 
ATOM   1024 C CD  . LYS B 1 40 ? 30.888  -21.027 -29.893 1.00 53.40  ? 39  LYS B CD  1 
ATOM   1025 C CE  . LYS B 1 40 ? 29.770  -21.896 -29.400 1.00 61.20  ? 39  LYS B CE  1 
ATOM   1026 N NZ  . LYS B 1 40 ? 30.036  -23.329 -29.516 1.00 59.22  ? 39  LYS B NZ  1 
ATOM   1027 N N   . TYR B 1 41 ? 30.166  -17.030 -33.416 1.00 33.56  ? 40  TYR B N   1 
ATOM   1028 C CA  . TYR B 1 41 ? 29.932  -15.626 -33.744 1.00 31.27  ? 40  TYR B CA  1 
ATOM   1029 C C   . TYR B 1 41 ? 29.354  -14.929 -32.516 1.00 34.58  ? 40  TYR B C   1 
ATOM   1030 O O   . TYR B 1 41 ? 28.623  -15.544 -31.746 1.00 31.04  ? 40  TYR B O   1 
ATOM   1031 C CB  . TYR B 1 41 ? 28.863  -15.501 -34.837 1.00 31.18  ? 40  TYR B CB  1 
ATOM   1032 C CG  . TYR B 1 41 ? 29.353  -15.946 -36.208 1.00 33.17  ? 40  TYR B CG  1 
ATOM   1033 C CD1 . TYR B 1 41 ? 30.033  -15.080 -37.062 1.00 31.28  ? 40  TYR B CD1 1 
ATOM   1034 C CD2 . TYR B 1 41 ? 29.153  -17.252 -36.632 1.00 33.79  ? 40  TYR B CD2 1 
ATOM   1035 C CE1 . TYR B 1 41 ? 30.498  -15.516 -38.300 1.00 37.47  ? 40  TYR B CE1 1 
ATOM   1036 C CE2 . TYR B 1 41 ? 29.609  -17.698 -37.862 1.00 38.70  ? 40  TYR B CE2 1 
ATOM   1037 C CZ  . TYR B 1 41 ? 30.296  -16.829 -38.699 1.00 39.34  ? 40  TYR B CZ  1 
ATOM   1038 O OH  . TYR B 1 41 ? 30.723  -17.301 -39.921 1.00 37.54  ? 40  TYR B OH  1 
ATOM   1039 N N   . PRO B 1 42 ? 29.584  -13.605 -32.337 1.00 35.59  ? 41  PRO B N   1 
ATOM   1040 C CA  . PRO B 1 42 ? 28.860  -12.853 -31.312 1.00 30.72  ? 41  PRO B CA  1 
ATOM   1041 C C   . PRO B 1 42 ? 27.442  -12.567 -31.781 1.00 29.42  ? 41  PRO B C   1 
ATOM   1042 O O   . PRO B 1 42 ? 27.220  -11.914 -32.821 1.00 30.76  ? 41  PRO B O   1 
ATOM   1043 C CB  . PRO B 1 42 ? 29.661  -11.541 -31.148 1.00 36.07  ? 41  PRO B CB  1 
ATOM   1044 C CG  . PRO B 1 42 ? 30.665  -11.500 -32.297 1.00 35.24  ? 41  PRO B CG  1 
ATOM   1045 C CD  . PRO B 1 42 ? 30.472  -12.751 -33.154 1.00 35.75  ? 41  PRO B CD  1 
ATOM   1046 N N   . ILE B 1 43 ? 26.469  -13.038 -30.971 1.00 27.79  ? 42  ILE B N   1 
ATOM   1047 C CA  . ILE B 1 43 ? 25.051  -12.826 -31.246 1.00 27.07  ? 42  ILE B CA  1 
ATOM   1048 C C   . ILE B 1 43 ? 24.443  -11.794 -30.295 1.00 25.02  ? 42  ILE B C   1 
ATOM   1049 O O   . ILE B 1 43 ? 24.695  -11.850 -29.109 1.00 28.50  ? 42  ILE B O   1 
ATOM   1050 C CB  . ILE B 1 43 ? 24.308  -14.162 -31.109 1.00 25.30  ? 42  ILE B CB  1 
ATOM   1051 C CG1 . ILE B 1 43 ? 25.020  -15.253 -31.963 1.00 28.68  ? 42  ILE B CG1 1 
ATOM   1052 C CG2 . ILE B 1 43 ? 22.841  -13.977 -31.514 1.00 27.58  ? 42  ILE B CG2 1 
ATOM   1053 C CD1 . ILE B 1 43 ? 25.194  -14.875 -33.421 1.00 27.93  ? 42  ILE B CD1 1 
ATOM   1054 N N   . PHE B 1 44 ? 23.640  -10.887 -30.857 1.00 27.07  ? 43  PHE B N   1 
ATOM   1055 C CA  . PHE B 1 44 ? 22.800  -9.978  -30.080 1.00 27.48  ? 43  PHE B CA  1 
ATOM   1056 C C   . PHE B 1 44 ? 21.349  -10.395 -30.285 1.00 25.14  ? 43  PHE B C   1 
ATOM   1057 O O   . PHE B 1 44 ? 20.858  -10.451 -31.399 1.00 26.58  ? 43  PHE B O   1 
ATOM   1058 C CB  . PHE B 1 44 ? 23.053  -8.518  -30.479 1.00 27.45  ? 43  PHE B CB  1 
ATOM   1059 C CG  . PHE B 1 44 ? 22.099  -7.519  -29.825 1.00 27.67  ? 43  PHE B CG  1 
ATOM   1060 C CD1 . PHE B 1 44 ? 20.920  -7.120  -30.465 1.00 25.15  ? 43  PHE B CD1 1 
ATOM   1061 C CD2 . PHE B 1 44 ? 22.392  -6.976  -28.584 1.00 33.06  ? 43  PHE B CD2 1 
ATOM   1062 C CE1 . PHE B 1 44 ? 20.079  -6.170  -29.875 1.00 29.38  ? 43  PHE B CE1 1 
ATOM   1063 C CE2 . PHE B 1 44 ? 21.542  -6.036  -27.991 1.00 28.47  ? 43  PHE B CE2 1 
ATOM   1064 C CZ  . PHE B 1 44 ? 20.398  -5.642  -28.641 1.00 32.92  ? 43  PHE B CZ  1 
ATOM   1065 N N   . PHE B 1 45 ? 20.629  -10.688 -29.185 1.00 24.60  ? 44  PHE B N   1 
ATOM   1066 C CA  . PHE B 1 45 ? 19.241  -11.090 -29.240 1.00 25.85  ? 44  PHE B CA  1 
ATOM   1067 C C   . PHE B 1 45 ? 18.359  -9.874  -29.042 1.00 23.51  ? 44  PHE B C   1 
ATOM   1068 O O   . PHE B 1 45 ? 18.475  -9.155  -28.024 1.00 26.87  ? 44  PHE B O   1 
ATOM   1069 C CB  . PHE B 1 45 ? 18.985  -12.068 -28.076 1.00 24.66  ? 44  PHE B CB  1 
ATOM   1070 C CG  . PHE B 1 45 ? 19.718  -13.401 -28.175 1.00 24.46  ? 44  PHE B CG  1 
ATOM   1071 C CD1 . PHE B 1 45 ? 21.022  -13.556 -27.738 1.00 29.08  ? 44  PHE B CD1 1 
ATOM   1072 C CD2 . PHE B 1 45 ? 19.110  -14.486 -28.809 1.00 24.26  ? 44  PHE B CD2 1 
ATOM   1073 C CE1 . PHE B 1 45 ? 21.685  -14.764 -27.884 1.00 28.96  ? 44  PHE B CE1 1 
ATOM   1074 C CE2 . PHE B 1 45 ? 19.755  -15.708 -28.907 1.00 25.11  ? 44  PHE B CE2 1 
ATOM   1075 C CZ  . PHE B 1 45 ? 21.067  -15.833 -28.497 1.00 27.54  ? 44  PHE B CZ  1 
ATOM   1076 N N   . PHE B 1 46 ? 17.480  -9.646  -30.029 1.00 24.78  ? 45  PHE B N   1 
ATOM   1077 C CA  . PHE B 1 46 ? 16.611  -8.496  -29.985 1.00 23.77  ? 45  PHE B CA  1 
ATOM   1078 C C   . PHE B 1 46 ? 15.564  -8.693  -28.875 1.00 28.66  ? 45  PHE B C   1 
ATOM   1079 O O   . PHE B 1 46 ? 15.256  -9.817  -28.468 1.00 26.64  ? 45  PHE B O   1 
ATOM   1080 C CB  . PHE B 1 46 ? 15.851  -8.359  -31.297 1.00 21.90  ? 45  PHE B CB  1 
ATOM   1081 C CG  . PHE B 1 46 ? 16.786  -7.905  -32.410 1.00 24.52  ? 45  PHE B CG  1 
ATOM   1082 C CD1 . PHE B 1 46 ? 17.279  -6.593  -32.398 1.00 28.62  ? 45  PHE B CD1 1 
ATOM   1083 C CD2 . PHE B 1 46 ? 17.093  -8.737  -33.499 1.00 25.28  ? 45  PHE B CD2 1 
ATOM   1084 C CE1 . PHE B 1 46 ? 18.157  -6.167  -33.402 1.00 28.81  ? 45  PHE B CE1 1 
ATOM   1085 C CE2 . PHE B 1 46 ? 17.922  -8.282  -34.537 1.00 25.24  ? 45  PHE B CE2 1 
ATOM   1086 C CZ  . PHE B 1 46 ? 18.438  -6.984  -34.479 1.00 27.54  ? 45  PHE B CZ  1 
ATOM   1087 N N   . GLY B 1 47 ? 15.033  -7.580  -28.369 1.00 25.50  ? 46  GLY B N   1 
ATOM   1088 C CA  . GLY B 1 47 ? 13.972  -7.647  -27.360 1.00 25.09  ? 46  GLY B CA  1 
ATOM   1089 C C   . GLY B 1 47 ? 14.585  -7.718  -25.964 1.00 27.24  ? 46  GLY B C   1 
ATOM   1090 O O   . GLY B 1 47 ? 14.465  -6.784  -25.168 1.00 30.26  ? 46  GLY B O   1 
ATOM   1091 N N   . THR B 1 48 ? 15.284  -8.811  -25.668 1.00 27.05  ? 47  THR B N   1 
ATOM   1092 C CA  . THR B 1 48 ? 15.975  -9.003  -24.405 1.00 28.07  ? 47  THR B CA  1 
ATOM   1093 C C   . THR B 1 48 ? 17.272  -8.213  -24.344 1.00 31.36  ? 47  THR B C   1 
ATOM   1094 O O   . THR B 1 48 ? 17.727  -7.864  -23.255 1.00 32.36  ? 47  THR B O   1 
ATOM   1095 C CB  . THR B 1 48 ? 16.249  -10.487 -24.145 1.00 29.50  ? 47  THR B CB  1 
ATOM   1096 O OG1 . THR B 1 48 ? 17.187  -10.972 -25.111 1.00 30.14  ? 47  THR B OG1 1 
ATOM   1097 C CG2 . THR B 1 48 ? 14.981  -11.325 -24.053 1.00 28.69  ? 47  THR B CG2 1 
ATOM   1098 N N   . HIS B 1 49 ? 17.890  -8.011  -25.510 1.00 28.32  ? 48  HIS B N   1 
ATOM   1099 C CA  . HIS B 1 49 ? 19.221  -7.445  -25.648 1.00 32.28  ? 48  HIS B CA  1 
ATOM   1100 C C   . HIS B 1 49 ? 20.259  -8.281  -24.919 1.00 31.32  ? 48  HIS B C   1 
ATOM   1101 O O   . HIS B 1 49 ? 21.268  -7.733  -24.484 1.00 36.59  ? 48  HIS B O   1 
ATOM   1102 C CB  . HIS B 1 49 ? 19.260  -5.979  -25.191 1.00 29.86  ? 48  HIS B CB  1 
ATOM   1103 C CG  . HIS B 1 49 ? 18.121  -5.230  -25.759 1.00 30.56  ? 48  HIS B CG  1 
ATOM   1104 N ND1 . HIS B 1 49 ? 17.414  -4.331  -24.992 1.00 33.53  ? 48  HIS B ND1 1 
ATOM   1105 C CD2 . HIS B 1 49 ? 17.512  -5.247  -26.964 1.00 29.28  ? 48  HIS B CD2 1 
ATOM   1106 C CE1 . HIS B 1 49 ? 16.419  -3.832  -25.721 1.00 38.47  ? 48  HIS B CE1 1 
ATOM   1107 N NE2 . HIS B 1 49 ? 16.454  -4.377  -26.925 1.00 34.90  ? 48  HIS B NE2 1 
ATOM   1108 N N   . GLU B 1 50 ? 20.061  -9.605  -24.830 1.00 29.88  ? 49  GLU B N   1 
ATOM   1109 C CA  . GLU B 1 50 ? 21.090  -10.483 -24.296 1.00 30.10  ? 49  GLU B CA  1 
ATOM   1110 C C   . GLU B 1 50 ? 22.133  -10.739 -25.395 1.00 28.26  ? 49  GLU B C   1 
ATOM   1111 O O   . GLU B 1 50 ? 21.888  -10.439 -26.572 1.00 29.51  ? 49  GLU B O   1 
ATOM   1112 C CB  . GLU B 1 50 ? 20.450  -11.837 -23.996 1.00 31.19  ? 49  GLU B CB  1 
ATOM   1113 C CG  . GLU B 1 50 ? 19.392  -11.733 -22.900 1.00 34.49  ? 49  GLU B CG  1 
ATOM   1114 C CD  . GLU B 1 50 ? 19.870  -12.279 -21.579 1.00 43.59  ? 49  GLU B CD  1 
ATOM   1115 O OE1 . GLU B 1 50 ? 19.306  -11.924 -20.528 1.00 47.52  ? 49  GLU B OE1 1 
ATOM   1116 O OE2 . GLU B 1 50 ? 20.800  -13.088 -21.605 1.00 48.97  ? 49  GLU B OE2 1 
ATOM   1117 N N   . THR B 1 51 ? 23.262  -11.303 -24.978 1.00 26.94  ? 50  THR B N   1 
ATOM   1118 C CA  . THR B 1 51 ? 24.309  -11.732 -25.908 1.00 31.96  ? 50  THR B CA  1 
ATOM   1119 C C   . THR B 1 51 ? 24.738  -13.169 -25.603 1.00 36.33  ? 50  THR B C   1 
ATOM   1120 O O   . THR B 1 51 ? 24.523  -13.714 -24.511 1.00 34.11  ? 50  THR B O   1 
ATOM   1121 C CB  . THR B 1 51 ? 25.476  -10.741 -26.011 1.00 36.78  ? 50  THR B CB  1 
ATOM   1122 O OG1 . THR B 1 51 ? 26.088  -10.666 -24.734 1.00 37.40  ? 50  THR B OG1 1 
ATOM   1123 C CG2 . THR B 1 51 ? 25.057  -9.330  -26.384 1.00 32.93  ? 50  THR B CG2 1 
ATOM   1124 N N   . ALA B 1 52 ? 25.321  -13.813 -26.622 1.00 37.29  ? 51  ALA B N   1 
ATOM   1125 C CA  . ALA B 1 52 ? 25.935  -15.118 -26.482 1.00 36.35  ? 51  ALA B CA  1 
ATOM   1126 C C   . ALA B 1 52 ? 26.829  -15.373 -27.695 1.00 30.90  ? 51  ALA B C   1 
ATOM   1127 O O   . ALA B 1 52 ? 26.749  -14.642 -28.695 1.00 32.62  ? 51  ALA B O   1 
ATOM   1128 C CB  . ALA B 1 52 ? 24.879  -16.191 -26.329 1.00 31.70  ? 51  ALA B CB  1 
ATOM   1129 N N   . PHE B 1 53 ? 27.663  -16.411 -27.580 1.00 33.32  ? 52  PHE B N   1 
ATOM   1130 C CA  . PHE B 1 53 ? 28.421  -16.925 -28.712 1.00 34.93  ? 52  PHE B CA  1 
ATOM   1131 C C   . PHE B 1 53 ? 27.746  -18.200 -29.241 1.00 35.09  ? 52  PHE B C   1 
ATOM   1132 O O   . PHE B 1 53 ? 27.531  -19.163 -28.486 1.00 35.01  ? 52  PHE B O   1 
ATOM   1133 C CB  . PHE B 1 53 ? 29.897  -17.154 -28.346 1.00 34.37  ? 52  PHE B CB  1 
ATOM   1134 C CG  . PHE B 1 53 ? 30.671  -15.932 -27.864 1.00 39.89  ? 52  PHE B CG  1 
ATOM   1135 C CD1 . PHE B 1 53 ? 30.971  -14.893 -28.736 1.00 41.34  ? 52  PHE B CD1 1 
ATOM   1136 C CD2 . PHE B 1 53 ? 31.114  -15.840 -26.546 1.00 42.27  ? 52  PHE B CD2 1 
ATOM   1137 C CE1 . PHE B 1 53 ? 31.686  -13.784 -28.299 1.00 44.47  ? 52  PHE B CE1 1 
ATOM   1138 C CE2 . PHE B 1 53 ? 31.801  -14.716 -26.098 1.00 42.95  ? 52  PHE B CE2 1 
ATOM   1139 C CZ  . PHE B 1 53 ? 32.096  -13.698 -26.978 1.00 40.08  ? 52  PHE B CZ  1 
ATOM   1140 N N   . LEU B 1 54 ? 27.425  -18.212 -30.550 1.00 33.18  ? 53  LEU B N   1 
ATOM   1141 C CA  . LEU B 1 54 ? 26.810  -19.376 -31.177 1.00 30.23  ? 53  LEU B CA  1 
ATOM   1142 C C   . LEU B 1 54 ? 27.532  -19.725 -32.476 1.00 31.61  ? 53  LEU B C   1 
ATOM   1143 O O   . LEU B 1 54 ? 28.010  -18.836 -33.197 1.00 32.23  ? 53  LEU B O   1 
ATOM   1144 C CB  . LEU B 1 54 ? 25.322  -19.192 -31.502 1.00 28.69  ? 53  LEU B CB  1 
ATOM   1145 C CG  . LEU B 1 54 ? 24.355  -19.085 -30.318 1.00 29.61  ? 53  LEU B CG  1 
ATOM   1146 C CD1 . LEU B 1 54 ? 22.969  -18.707 -30.776 1.00 28.15  ? 53  LEU B CD1 1 
ATOM   1147 C CD2 . LEU B 1 54 ? 24.335  -20.431 -29.594 1.00 34.00  ? 53  LEU B CD2 1 
ATOM   1148 N N   . GLY B 1 55 ? 27.484  -21.023 -32.815 1.00 30.74  ? 54  GLY B N   1 
ATOM   1149 C CA  . GLY B 1 55 ? 28.001  -21.537 -34.079 1.00 30.26  ? 54  GLY B CA  1 
ATOM   1150 C C   . GLY B 1 55 ? 26.904  -21.589 -35.149 1.00 30.63  ? 54  GLY B C   1 
ATOM   1151 O O   . GLY B 1 55 ? 25.706  -21.506 -34.839 1.00 27.87  ? 54  GLY B O   1 
ATOM   1152 N N   . PRO B 1 56 ? 27.271  -21.758 -36.437 1.00 27.98  ? 55  PRO B N   1 
ATOM   1153 C CA  . PRO B 1 56 ? 26.300  -21.837 -37.524 1.00 27.63  ? 55  PRO B CA  1 
ATOM   1154 C C   . PRO B 1 56 ? 25.129  -22.801 -37.394 1.00 26.29  ? 55  PRO B C   1 
ATOM   1155 O O   . PRO B 1 56 ? 24.079  -22.554 -37.953 1.00 26.37  ? 55  PRO B O   1 
ATOM   1156 C CB  . PRO B 1 56 ? 27.119  -22.135 -38.791 1.00 32.58  ? 55  PRO B CB  1 
ATOM   1157 C CG  . PRO B 1 56 ? 28.552  -22.116 -38.383 1.00 34.26  ? 55  PRO B CG  1 
ATOM   1158 C CD  . PRO B 1 56 ? 28.660  -21.863 -36.909 1.00 31.82  ? 55  PRO B CD  1 
ATOM   1159 N N   . LYS B 1 57 ? 25.312  -23.902 -36.661 1.00 29.80  ? 56  LYS B N   1 
ATOM   1160 C CA  . LYS B 1 57 ? 24.252  -24.900 -36.594 1.00 28.30  ? 56  LYS B CA  1 
ATOM   1161 C C   . LYS B 1 57 ? 23.011  -24.320 -35.914 1.00 27.68  ? 56  LYS B C   1 
ATOM   1162 O O   . LYS B 1 57 ? 21.910  -24.773 -36.167 1.00 27.26  ? 56  LYS B O   1 
ATOM   1163 C CB  . LYS B 1 57 ? 24.719  -26.189 -35.893 1.00 34.14  ? 56  LYS B CB  1 
ATOM   1164 C CG  . LYS B 1 57 ? 24.844  -26.114 -34.383 1.00 38.49  ? 56  LYS B CG  1 
ATOM   1165 C CD  . LYS B 1 57 ? 24.808  -27.499 -33.740 1.00 40.01  ? 56  LYS B CD  1 
ATOM   1166 C CE  . LYS B 1 57 ? 25.148  -27.477 -32.271 1.00 40.28  ? 56  LYS B CE  1 
ATOM   1167 N NZ  . LYS B 1 57 ? 24.120  -26.880 -31.419 1.00 42.59  ? 56  LYS B NZ  1 
ATOM   1168 N N   . ASP B 1 58 ? 23.207  -23.243 -35.136 1.00 25.45  ? 57  ASP B N   1 
ATOM   1169 C CA  . ASP B 1 58 ? 22.151  -22.608 -34.367 1.00 25.44  ? 57  ASP B CA  1 
ATOM   1170 C C   . ASP B 1 58 ? 21.739  -21.262 -34.980 1.00 25.74  ? 57  ASP B C   1 
ATOM   1171 O O   . ASP B 1 58 ? 21.008  -20.515 -34.323 1.00 24.90  ? 57  ASP B O   1 
ATOM   1172 C CB  . ASP B 1 58 ? 22.626  -22.471 -32.932 1.00 28.64  ? 57  ASP B CB  1 
ATOM   1173 C CG  . ASP B 1 58 ? 22.776  -23.797 -32.189 1.00 33.40  ? 57  ASP B CG  1 
ATOM   1174 O OD1 . ASP B 1 58 ? 21.870  -24.637 -32.334 1.00 32.40  ? 57  ASP B OD1 1 
ATOM   1175 O OD2 . ASP B 1 58 ? 23.770  -23.945 -31.448 1.00 34.71  ? 57  ASP B OD2 1 
ATOM   1176 N N   . LEU B 1 59 ? 22.220  -20.964 -36.204 1.00 26.41  ? 58  LEU B N   1 
ATOM   1177 C CA  . LEU B 1 59 ? 21.941  -19.668 -36.835 1.00 25.62  ? 58  LEU B CA  1 
ATOM   1178 C C   . LEU B 1 59 ? 21.197  -19.847 -38.151 1.00 24.20  ? 58  LEU B C   1 
ATOM   1179 O O   . LEU B 1 59 ? 21.695  -20.525 -39.073 1.00 25.39  ? 58  LEU B O   1 
ATOM   1180 C CB  . LEU B 1 59 ? 23.256  -18.929 -37.030 1.00 25.67  ? 58  LEU B CB  1 
ATOM   1181 C CG  . LEU B 1 59 ? 24.063  -18.669 -35.758 1.00 25.39  ? 58  LEU B CG  1 
ATOM   1182 C CD1 . LEU B 1 59 ? 25.338  -17.955 -36.122 1.00 28.31  ? 58  LEU B CD1 1 
ATOM   1183 C CD2 . LEU B 1 59 ? 23.239  -17.774 -34.815 1.00 28.42  ? 58  LEU B CD2 1 
ATOM   1184 N N   . PHE B 1 60 ? 20.015  -19.235 -38.221 1.00 23.11  ? 59  PHE B N   1 
ATOM   1185 C CA  . PHE B 1 60 ? 19.062  -19.413 -39.300 1.00 23.42  ? 59  PHE B CA  1 
ATOM   1186 C C   . PHE B 1 60 ? 18.873  -18.058 -39.985 1.00 24.29  ? 59  PHE B C   1 
ATOM   1187 O O   . PHE B 1 60 ? 18.274  -17.149 -39.413 1.00 24.71  ? 59  PHE B O   1 
ATOM   1188 C CB  . PHE B 1 60 ? 17.739  -19.981 -38.778 1.00 22.36  ? 59  PHE B CB  1 
ATOM   1189 C CG  . PHE B 1 60 ? 17.841  -21.382 -38.176 1.00 22.65  ? 59  PHE B CG  1 
ATOM   1190 C CD1 . PHE B 1 60 ? 18.397  -21.544 -36.906 1.00 24.08  ? 59  PHE B CD1 1 
ATOM   1191 C CD2 . PHE B 1 60 ? 17.430  -22.508 -38.893 1.00 27.82  ? 59  PHE B CD2 1 
ATOM   1192 C CE1 . PHE B 1 60 ? 18.531  -22.817 -36.351 1.00 28.80  ? 59  PHE B CE1 1 
ATOM   1193 C CE2 . PHE B 1 60 ? 17.525  -23.772 -38.319 1.00 28.83  ? 59  PHE B CE2 1 
ATOM   1194 C CZ  . PHE B 1 60 ? 18.124  -23.920 -37.081 1.00 28.36  ? 59  PHE B CZ  1 
ATOM   1195 N N   . PRO B 1 61 ? 19.401  -17.855 -41.208 1.00 27.49  ? 60  PRO B N   1 
ATOM   1196 C CA  . PRO B 1 61 ? 19.199  -16.557 -41.889 1.00 28.91  ? 60  PRO B CA  1 
ATOM   1197 C C   . PRO B 1 61 ? 17.745  -16.067 -41.876 1.00 28.11  ? 60  PRO B C   1 
ATOM   1198 O O   . PRO B 1 61 ? 16.818  -16.819 -42.147 1.00 29.10  ? 60  PRO B O   1 
ATOM   1199 C CB  . PRO B 1 61 ? 19.775  -16.802 -43.310 1.00 29.26  ? 60  PRO B CB  1 
ATOM   1200 C CG  . PRO B 1 61 ? 20.755  -17.941 -43.145 1.00 36.10  ? 60  PRO B CG  1 
ATOM   1201 C CD  . PRO B 1 61 ? 20.201  -18.819 -41.992 1.00 31.66  ? 60  PRO B CD  1 
ATOM   1202 N N   . TYR B 1 62 ? 17.527  -14.773 -41.523 1.00 28.54  ? 61  TYR B N   1 
ATOM   1203 C CA  . TYR B 1 62 ? 16.221  -14.255 -41.156 1.00 30.16  ? 61  TYR B CA  1 
ATOM   1204 C C   . TYR B 1 62 ? 15.226  -14.282 -42.305 1.00 27.59  ? 61  TYR B C   1 
ATOM   1205 O O   . TYR B 1 62 ? 14.079  -14.686 -42.124 1.00 31.39  ? 61  TYR B O   1 
ATOM   1206 C CB  . TYR B 1 62 ? 16.420  -12.783 -40.755 1.00 30.17  ? 61  TYR B CB  1 
ATOM   1207 C CG  . TYR B 1 62 ? 15.111  -12.065 -40.474 1.00 33.13  ? 61  TYR B CG  1 
ATOM   1208 C CD1 . TYR B 1 62 ? 14.401  -12.302 -39.305 1.00 35.70  ? 61  TYR B CD1 1 
ATOM   1209 C CD2 . TYR B 1 62 ? 14.630  -11.089 -41.352 1.00 38.91  ? 61  TYR B CD2 1 
ATOM   1210 C CE1 . TYR B 1 62 ? 13.227  -11.627 -39.031 1.00 34.11  ? 61  TYR B CE1 1 
ATOM   1211 C CE2 . TYR B 1 62 ? 13.456  -10.399 -41.085 1.00 39.83  ? 61  TYR B CE2 1 
ATOM   1212 C CZ  . TYR B 1 62 ? 12.752  -10.683 -39.926 1.00 38.35  ? 61  TYR B CZ  1 
ATOM   1213 O OH  . TYR B 1 62 ? 11.593  -10.024 -39.675 1.00 39.30  ? 61  TYR B OH  1 
ATOM   1214 N N   . ASP B 1 63 ? 15.684  -13.860 -43.501 1.00 35.78  ? 62  ASP B N   1 
ATOM   1215 C CA  . ASP B 1 63 ? 14.849  -13.828 -44.700 1.00 40.51  ? 62  ASP B CA  1 
ATOM   1216 C C   . ASP B 1 63 ? 14.286  -15.209 -45.024 1.00 34.62  ? 62  ASP B C   1 
ATOM   1217 O O   . ASP B 1 63 ? 13.073  -15.365 -45.120 1.00 43.31  ? 62  ASP B O   1 
ATOM   1218 C CB  . ASP B 1 63 ? 15.560  -13.220 -45.896 1.00 44.78  ? 62  ASP B CB  1 
ATOM   1219 C CG  . ASP B 1 63 ? 15.197  -11.774 -46.180 1.00 57.83  ? 62  ASP B CG  1 
ATOM   1220 O OD1 . ASP B 1 63 ? 14.735  -11.078 -45.236 1.00 60.04  ? 62  ASP B OD1 1 
ATOM   1221 O OD2 . ASP B 1 63 ? 15.329  -11.372 -47.357 1.00 63.93  ? 62  ASP B OD2 1 
ATOM   1222 N N   . LYS B 1 64 ? 15.169  -16.196 -45.127 1.00 40.16  ? 63  LYS B N   1 
ATOM   1223 C CA  . LYS B 1 64 ? 14.749  -17.567 -45.359 1.00 39.56  ? 63  LYS B CA  1 
ATOM   1224 C C   . LYS B 1 64 ? 13.789  -18.052 -44.268 1.00 37.20  ? 63  LYS B C   1 
ATOM   1225 O O   . LYS B 1 64 ? 12.843  -18.777 -44.571 1.00 40.27  ? 63  LYS B O   1 
ATOM   1226 C CB  . LYS B 1 64 ? 15.949  -18.515 -45.381 1.00 45.08  ? 63  LYS B CB  1 
ATOM   1227 C CG  . LYS B 1 64 ? 15.574  -19.927 -45.814 1.00 41.56  ? 63  LYS B CG  1 
ATOM   1228 C CD  . LYS B 1 64 ? 16.792  -20.831 -45.900 1.00 48.13  ? 63  LYS B CD  1 
ATOM   1229 C CE  . LYS B 1 64 ? 16.569  -22.116 -46.666 1.00 46.83  ? 63  LYS B CE  1 
ATOM   1230 N NZ  . LYS B 1 64 ? 15.444  -22.889 -46.146 1.00 42.41  ? 63  LYS B NZ  1 
ATOM   1231 N N   . SER B 1 65 ? 14.007  -17.664 -43.003 1.00 34.67  ? 64  SER B N   1 
ATOM   1232 C CA  . SER B 1 65 ? 13.330  -18.425 -41.941 1.00 34.70  ? 64  SER B CA  1 
ATOM   1233 C C   . SER B 1 65 ? 12.214  -17.652 -41.225 1.00 35.22  ? 64  SER B C   1 
ATOM   1234 O O   . SER B 1 65 ? 11.535  -18.189 -40.345 1.00 35.38  ? 64  SER B O   1 
ATOM   1235 C CB  . SER B 1 65 ? 14.322  -19.065 -41.010 1.00 35.42  ? 64  SER B CB  1 
ATOM   1236 O OG  . SER B 1 65 ? 15.104  -18.044 -40.414 1.00 48.11  ? 64  SER B OG  1 
ATOM   1237 N N   . LYS B 1 66 ? 11.922  -16.421 -41.668 1.00 34.42  ? 65  LYS B N   1 
ATOM   1238 C CA  . LYS B 1 66 ? 11.013  -15.592 -40.884 1.00 34.30  ? 65  LYS B CA  1 
ATOM   1239 C C   . LYS B 1 66 ? 9.564   -16.091 -40.870 1.00 38.35  ? 65  LYS B C   1 
ATOM   1240 O O   . LYS B 1 66 ? 8.860   -15.869 -39.892 1.00 38.07  ? 65  LYS B O   1 
ATOM   1241 C CB  . LYS B 1 66 ? 11.093  -14.104 -41.261 1.00 35.14  ? 65  LYS B CB  1 
ATOM   1242 C CG  . LYS B 1 66 ? 10.474  -13.785 -42.619 1.00 39.01  ? 65  LYS B CG  1 
ATOM   1243 N N   . ASP B 1 67 ? 9.053   -16.718 -41.934 1.00 39.65  ? 66  ASP B N   1 
ATOM   1244 C CA  . ASP B 1 67 ? 7.642   -17.070 -41.831 1.00 45.64  ? 66  ASP B CA  1 
ATOM   1245 C C   . ASP B 1 67 ? 7.450   -18.296 -40.933 1.00 44.24  ? 66  ASP B C   1 
ATOM   1246 O O   . ASP B 1 67 ? 6.373   -18.487 -40.346 1.00 46.71  ? 66  ASP B O   1 
ATOM   1247 C CB  . ASP B 1 67 ? 6.898   -16.986 -43.153 1.00 60.63  ? 66  ASP B CB  1 
ATOM   1248 C CG  . ASP B 1 67 ? 7.675   -17.488 -44.357 1.00 72.23  ? 66  ASP B CG  1 
ATOM   1249 O OD1 . ASP B 1 67 ? 7.712   -16.762 -45.381 1.00 77.02  ? 66  ASP B OD1 1 
ATOM   1250 O OD2 . ASP B 1 67 ? 8.261   -18.581 -44.238 1.00 74.12  ? 66  ASP B OD2 1 
ATOM   1251 N N   . LYS B 1 68 ? 8.518   -19.090 -40.793 1.00 39.09  ? 67  LYS B N   1 
ATOM   1252 C CA  . LYS B 1 68 ? 8.502   -20.249 -39.907 1.00 35.53  ? 67  LYS B CA  1 
ATOM   1253 C C   . LYS B 1 68 ? 8.692   -19.839 -38.445 1.00 33.59  ? 67  LYS B C   1 
ATOM   1254 O O   . LYS B 1 68 ? 7.893   -20.235 -37.589 1.00 34.97  ? 67  LYS B O   1 
ATOM   1255 C CB  . LYS B 1 68 ? 9.554   -21.254 -40.379 1.00 38.71  ? 67  LYS B CB  1 
ATOM   1256 C CG  . LYS B 1 68 ? 9.742   -22.476 -39.502 1.00 42.60  ? 67  LYS B CG  1 
ATOM   1257 C CD  . LYS B 1 68 ? 10.653  -23.417 -40.287 1.00 52.65  ? 67  LYS B CD  1 
ATOM   1258 C CE  . LYS B 1 68 ? 10.996  -24.680 -39.559 1.00 58.67  ? 67  LYS B CE  1 
ATOM   1259 N NZ  . LYS B 1 68 ? 9.827   -25.552 -39.400 1.00 57.64  ? 67  LYS B NZ  1 
ATOM   1260 N N   . TYR B 1 69 ? 9.692   -18.992 -38.156 1.00 29.05  ? 68  TYR B N   1 
ATOM   1261 C CA  . TYR B 1 69 ? 10.107  -18.732 -36.778 1.00 26.16  ? 68  TYR B CA  1 
ATOM   1262 C C   . TYR B 1 69 ? 9.596   -17.392 -36.247 1.00 28.87  ? 68  TYR B C   1 
ATOM   1263 O O   . TYR B 1 69 ? 9.768   -17.123 -35.060 1.00 31.37  ? 68  TYR B O   1 
ATOM   1264 C CB  . TYR B 1 69 ? 11.629  -18.788 -36.609 1.00 28.19  ? 68  TYR B CB  1 
ATOM   1265 C CG  . TYR B 1 69 ? 12.234  -20.161 -36.883 1.00 29.06  ? 68  TYR B CG  1 
ATOM   1266 C CD1 . TYR B 1 69 ? 11.667  -21.321 -36.354 1.00 31.85  ? 68  TYR B CD1 1 
ATOM   1267 C CD2 . TYR B 1 69 ? 13.342  -20.302 -37.713 1.00 31.61  ? 68  TYR B CD2 1 
ATOM   1268 C CE1 . TYR B 1 69 ? 12.213  -22.574 -36.620 1.00 32.57  ? 68  TYR B CE1 1 
ATOM   1269 C CE2 . TYR B 1 69 ? 13.880  -21.548 -38.008 1.00 32.94  ? 68  TYR B CE2 1 
ATOM   1270 C CZ  . TYR B 1 69 ? 13.330  -22.684 -37.433 1.00 34.81  ? 68  TYR B CZ  1 
ATOM   1271 O OH  . TYR B 1 69 ? 13.850  -23.911 -37.729 1.00 33.30  ? 68  TYR B OH  1 
ATOM   1272 N N   . GLY B 1 70 ? 9.066   -16.532 -37.134 1.00 31.19  ? 69  GLY B N   1 
ATOM   1273 C CA  . GLY B 1 70 ? 8.814   -15.154 -36.753 1.00 33.74  ? 69  GLY B CA  1 
ATOM   1274 C C   . GLY B 1 70 ? 7.380   -14.911 -36.273 1.00 38.93  ? 69  GLY B C   1 
ATOM   1275 O O   . GLY B 1 70 ? 6.820   -13.858 -36.578 1.00 39.56  ? 69  GLY B O   1 
ATOM   1276 N N   . LYS B 1 71 ? 6.806   -15.876 -35.535 1.00 38.27  ? 70  LYS B N   1 
ATOM   1277 C CA  . LYS B 1 71 ? 5.463   -15.747 -35.000 1.00 39.66  ? 70  LYS B CA  1 
ATOM   1278 C C   . LYS B 1 71 ? 5.554   -15.295 -33.550 1.00 42.14  ? 70  LYS B C   1 
ATOM   1279 O O   . LYS B 1 71 ? 6.450   -15.725 -32.816 1.00 37.81  ? 70  LYS B O   1 
ATOM   1280 C CB  . LYS B 1 71 ? 4.756   -17.102 -34.890 1.00 43.60  ? 70  LYS B CB  1 
ATOM   1281 C CG  . LYS B 1 71 ? 3.858   -17.495 -36.056 1.00 60.27  ? 70  LYS B CG  1 
ATOM   1282 C CD  . LYS B 1 71 ? 4.559   -17.784 -37.376 1.00 60.26  ? 70  LYS B CD  1 
ATOM   1283 C CE  . LYS B 1 71 ? 3.592   -18.248 -38.424 1.00 63.38  ? 70  LYS B CE  1 
ATOM   1284 N NZ  . LYS B 1 71 ? 4.042   -17.793 -39.746 1.00 72.41  ? 70  LYS B NZ  1 
ATOM   1285 N N   . PRO B 1 72 ? 4.614   -14.450 -33.068 1.00 42.71  ? 71  PRO B N   1 
ATOM   1286 C CA  . PRO B 1 72 ? 4.613   -14.076 -31.653 1.00 40.70  ? 71  PRO B CA  1 
ATOM   1287 C C   . PRO B 1 72 ? 4.436   -15.273 -30.718 1.00 40.01  ? 71  PRO B C   1 
ATOM   1288 O O   . PRO B 1 72 ? 3.861   -16.296 -31.104 1.00 38.48  ? 71  PRO B O   1 
ATOM   1289 C CB  . PRO B 1 72 ? 3.488   -13.037 -31.524 1.00 38.93  ? 71  PRO B CB  1 
ATOM   1290 C CG  . PRO B 1 72 ? 3.299   -12.547 -32.934 1.00 43.78  ? 71  PRO B CG  1 
ATOM   1291 C CD  . PRO B 1 72 ? 3.588   -13.744 -33.853 1.00 42.01  ? 71  PRO B CD  1 
ATOM   1292 N N   . ASN B 1 73 ? 4.969   -15.132 -29.496 1.00 36.62  ? 72  ASN B N   1 
ATOM   1293 C CA  . ASN B 1 73 ? 4.779   -16.113 -28.436 1.00 35.85  ? 72  ASN B CA  1 
ATOM   1294 C C   . ASN B 1 73 ? 4.710   -15.377 -27.089 1.00 39.71  ? 72  ASN B C   1 
ATOM   1295 O O   . ASN B 1 73 ? 4.753   -14.141 -27.034 1.00 40.58  ? 72  ASN B O   1 
ATOM   1296 C CB  . ASN B 1 73 ? 5.801   -17.251 -28.484 1.00 35.74  ? 72  ASN B CB  1 
ATOM   1297 C CG  . ASN B 1 73 ? 7.223   -16.813 -28.218 1.00 34.35  ? 72  ASN B CG  1 
ATOM   1298 O OD1 . ASN B 1 73 ? 7.473   -16.051 -27.274 1.00 34.23  ? 72  ASN B OD1 1 
ATOM   1299 N ND2 . ASN B 1 73 ? 8.169   -17.265 -29.044 1.00 29.39  ? 72  ASN B ND2 1 
ATOM   1300 N N   . LYS B 1 74 ? 4.626   -16.142 -25.999 1.00 38.54  ? 73  LYS B N   1 
ATOM   1301 C CA  . LYS B 1 74 ? 4.515   -15.554 -24.667 1.00 40.91  ? 73  LYS B CA  1 
ATOM   1302 C C   . LYS B 1 74 ? 5.853   -15.575 -23.899 1.00 39.69  ? 73  LYS B C   1 
ATOM   1303 O O   . LYS B 1 74 ? 5.851   -15.404 -22.678 1.00 38.57  ? 73  LYS B O   1 
ATOM   1304 C CB  . LYS B 1 74 ? 3.345   -16.229 -23.923 1.00 38.08  ? 73  LYS B CB  1 
ATOM   1305 N N   . ARG B 1 75 ? 7.000   -15.791 -24.580 1.00 29.56  ? 74  ARG B N   1 
ATOM   1306 C CA  . ARG B 1 75 ? 8.307   -15.636 -23.941 1.00 29.39  ? 74  ARG B CA  1 
ATOM   1307 C C   . ARG B 1 75 ? 8.625   -14.143 -23.761 1.00 32.63  ? 74  ARG B C   1 
ATOM   1308 O O   . ARG B 1 75 ? 8.467   -13.335 -24.679 1.00 32.51  ? 74  ARG B O   1 
ATOM   1309 C CB  . ARG B 1 75 ? 9.457   -16.365 -24.668 1.00 28.37  ? 74  ARG B CB  1 
ATOM   1310 C CG  . ARG B 1 75 ? 9.293   -17.877 -24.811 1.00 28.76  ? 74  ARG B CG  1 
ATOM   1311 C CD  . ARG B 1 75 ? 9.193   -18.666 -23.505 1.00 29.88  ? 74  ARG B CD  1 
ATOM   1312 N NE  . ARG B 1 75 ? 9.402   -20.101 -23.750 1.00 29.21  ? 74  ARG B NE  1 
ATOM   1313 C CZ  . ARG B 1 75 ? 10.530  -20.751 -23.559 1.00 30.12  ? 74  ARG B CZ  1 
ATOM   1314 N NH1 . ARG B 1 75 ? 11.581  -20.124 -23.058 1.00 33.94  ? 74  ARG B NH1 1 
ATOM   1315 N NH2 . ARG B 1 75 ? 10.627  -22.029 -23.921 1.00 34.50  ? 74  ARG B NH2 1 
ATOM   1316 N N   . LYS B 1 76 ? 9.073   -13.766 -22.555 1.00 29.85  ? 75  LYS B N   1 
ATOM   1317 C CA  . LYS B 1 76 ? 9.427   -12.387 -22.247 1.00 24.97  ? 75  LYS B CA  1 
ATOM   1318 C C   . LYS B 1 76 ? 10.521  -11.845 -23.201 1.00 24.85  ? 75  LYS B C   1 
ATOM   1319 O O   . LYS B 1 76 ? 11.628  -12.409 -23.269 1.00 27.57  ? 75  LYS B O   1 
ATOM   1320 C CB  . LYS B 1 76 ? 9.977   -12.299 -20.811 1.00 27.88  ? 75  LYS B CB  1 
ATOM   1321 C CG  . LYS B 1 76 ? 10.238  -10.862 -20.361 1.00 28.14  ? 75  LYS B CG  1 
ATOM   1322 C CD  . LYS B 1 76 ? 10.914  -10.757 -18.996 1.00 30.91  ? 75  LYS B CD  1 
ATOM   1323 C CE  . LYS B 1 76 ? 11.041  -9.333  -18.515 1.00 37.41  ? 75  LYS B CE  1 
ATOM   1324 N NZ  . LYS B 1 76 ? 11.556  -9.293  -17.135 1.00 44.10  ? 75  LYS B NZ  1 
ATOM   1325 N N   . GLY B 1 77 ? 10.186  -10.732 -23.870 1.00 24.45  ? 76  GLY B N   1 
ATOM   1326 C CA  . GLY B 1 77 ? 11.109  -10.003 -24.760 1.00 25.36  ? 76  GLY B CA  1 
ATOM   1327 C C   . GLY B 1 77 ? 10.965  -10.452 -26.225 1.00 29.11  ? 76  GLY B C   1 
ATOM   1328 O O   . GLY B 1 77 ? 11.460  -9.796  -27.144 1.00 29.11  ? 76  GLY B O   1 
ATOM   1329 N N   . PHE B 1 78 ? 10.309  -11.595 -26.468 1.00 25.29  ? 77  PHE B N   1 
ATOM   1330 C CA  . PHE B 1 78 ? 10.206  -12.086 -27.849 1.00 24.99  ? 77  PHE B CA  1 
ATOM   1331 C C   . PHE B 1 78 ? 9.445   -11.138 -28.778 1.00 27.27  ? 77  PHE B C   1 
ATOM   1332 O O   . PHE B 1 78 ? 9.925   -10.818 -29.871 1.00 26.49  ? 77  PHE B O   1 
ATOM   1333 C CB  . PHE B 1 78 ? 9.478   -13.426 -27.885 1.00 24.93  ? 77  PHE B CB  1 
ATOM   1334 C CG  . PHE B 1 78 ? 9.728   -14.153 -29.194 1.00 25.07  ? 77  PHE B CG  1 
ATOM   1335 C CD1 . PHE B 1 78 ? 10.812  -15.006 -29.319 1.00 25.47  ? 77  PHE B CD1 1 
ATOM   1336 C CD2 . PHE B 1 78 ? 8.810   -14.052 -30.232 1.00 27.59  ? 77  PHE B CD2 1 
ATOM   1337 C CE1 . PHE B 1 78 ? 11.057  -15.672 -30.522 1.00 24.99  ? 77  PHE B CE1 1 
ATOM   1338 C CE2 . PHE B 1 78 ? 9.027   -14.759 -31.416 1.00 28.55  ? 77  PHE B CE2 1 
ATOM   1339 C CZ  . PHE B 1 78 ? 10.155  -15.578 -31.539 1.00 27.14  ? 77  PHE B CZ  1 
ATOM   1340 N N   . ASN B 1 79 ? 8.240   -10.680 -28.414 1.00 27.13  ? 78  ASN B N   1 
ATOM   1341 C CA  . ASN B 1 79 ? 7.477   -9.838  -29.331 1.00 29.56  ? 78  ASN B CA  1 
ATOM   1342 C C   . ASN B 1 79 ? 8.167   -8.477  -29.519 1.00 30.26  ? 78  ASN B C   1 
ATOM   1343 O O   . ASN B 1 79 ? 8.108   -7.905  -30.613 1.00 30.11  ? 78  ASN B O   1 
ATOM   1344 C CB  . ASN B 1 79 ? 6.004   -9.727  -28.944 1.00 33.36  ? 78  ASN B CB  1 
ATOM   1345 C CG  . ASN B 1 79 ? 5.257   -11.044 -29.005 1.00 36.88  ? 78  ASN B CG  1 
ATOM   1346 O OD1 . ASN B 1 79 ? 5.744   -12.015 -29.595 1.00 34.08  ? 78  ASN B OD1 1 
ATOM   1347 N ND2 . ASN B 1 79 ? 4.093   -11.111 -28.364 1.00 37.29  ? 78  ASN B ND2 1 
ATOM   1348 N N   . GLU B 1 80 ? 8.891   -8.008  -28.500 1.00 29.54  ? 79  GLU B N   1 
ATOM   1349 C CA  . GLU B 1 80 ? 9.624   -6.767  -28.628 1.00 31.14  ? 79  GLU B CA  1 
ATOM   1350 C C   . GLU B 1 80 ? 10.750  -6.999  -29.632 1.00 28.92  ? 79  GLU B C   1 
ATOM   1351 O O   . GLU B 1 80 ? 11.038  -6.113  -30.439 1.00 28.93  ? 79  GLU B O   1 
ATOM   1352 C CB  . GLU B 1 80 ? 10.254  -6.240  -27.344 1.00 29.42  ? 79  GLU B CB  1 
ATOM   1353 C CG  . GLU B 1 80 ? 9.209   -5.543  -26.479 1.00 38.58  ? 79  GLU B CG  1 
ATOM   1354 N N   . GLY B 1 81 ? 11.335  -8.202  -29.573 1.00 26.49  ? 80  GLY B N   1 
ATOM   1355 C CA  . GLY B 1 81 ? 12.431  -8.598  -30.462 1.00 28.69  ? 80  GLY B CA  1 
ATOM   1356 C C   . GLY B 1 81 ? 11.965  -8.669  -31.916 1.00 29.07  ? 80  GLY B C   1 
ATOM   1357 O O   . GLY B 1 81 ? 12.719  -8.294  -32.837 1.00 27.59  ? 80  GLY B O   1 
ATOM   1358 N N   . LEU B 1 82 ? 10.739  -9.133  -32.127 1.00 25.77  ? 81  LEU B N   1 
ATOM   1359 C CA  . LEU B 1 82 ? 10.149  -9.164  -33.457 1.00 28.12  ? 81  LEU B CA  1 
ATOM   1360 C C   . LEU B 1 82 ? 10.017  -7.733  -33.973 1.00 29.22  ? 81  LEU B C   1 
ATOM   1361 O O   . LEU B 1 82 ? 10.243  -7.484  -35.152 1.00 29.98  ? 81  LEU B O   1 
ATOM   1362 C CB  . LEU B 1 82 ? 8.817   -9.913  -33.565 1.00 28.80  ? 81  LEU B CB  1 
ATOM   1363 C CG  . LEU B 1 82 ? 8.869   -11.431 -33.334 1.00 26.28  ? 81  LEU B CG  1 
ATOM   1364 C CD1 . LEU B 1 82 ? 7.452   -12.046 -33.307 1.00 29.17  ? 81  LEU B CD1 1 
ATOM   1365 C CD2 . LEU B 1 82 ? 9.809   -12.165 -34.317 1.00 26.09  ? 81  LEU B CD2 1 
ATOM   1366 N N   . TRP B 1 83 ? 9.657   -6.809  -33.073 1.00 27.57  ? 82  TRP B N   1 
ATOM   1367 C CA  . TRP B 1 83 ? 9.492   -5.417  -33.460 1.00 28.62  ? 82  TRP B CA  1 
ATOM   1368 C C   . TRP B 1 83 ? 10.839  -4.830  -33.891 1.00 27.77  ? 82  TRP B C   1 
ATOM   1369 O O   . TRP B 1 83 ? 10.910  -4.150  -34.914 1.00 28.99  ? 82  TRP B O   1 
ATOM   1370 C CB  . TRP B 1 83 ? 8.838   -4.584  -32.344 1.00 29.48  ? 82  TRP B CB  1 
ATOM   1371 C CG  . TRP B 1 83 ? 8.589   -3.174  -32.814 1.00 29.63  ? 82  TRP B CG  1 
ATOM   1372 C CD1 . TRP B 1 83 ? 7.482   -2.711  -33.458 1.00 36.50  ? 82  TRP B CD1 1 
ATOM   1373 C CD2 . TRP B 1 83 ? 9.534   -2.085  -32.809 1.00 34.19  ? 82  TRP B CD2 1 
ATOM   1374 N NE1 . TRP B 1 83 ? 7.660   -1.399  -33.819 1.00 38.93  ? 82  TRP B NE1 1 
ATOM   1375 C CE2 . TRP B 1 83 ? 8.908   -0.992  -33.442 1.00 36.35  ? 82  TRP B CE2 1 
ATOM   1376 C CE3 . TRP B 1 83 ? 10.842  -1.922  -32.332 1.00 32.53  ? 82  TRP B CE3 1 
ATOM   1377 C CZ2 . TRP B 1 83 ? 9.542   0.247   -33.588 1.00 34.32  ? 82  TRP B CZ2 1 
ATOM   1378 C CZ3 . TRP B 1 83 ? 11.467  -0.700  -32.476 1.00 36.59  ? 82  TRP B CZ3 1 
ATOM   1379 C CH2 . TRP B 1 83 ? 10.830  0.362   -33.116 1.00 33.39  ? 82  TRP B CH2 1 
ATOM   1380 N N   . GLU B 1 84 ? 11.891  -5.118  -33.113 1.00 24.26  ? 83  GLU B N   1 
ATOM   1381 C CA  . GLU B 1 84 ? 13.224  -4.574  -33.325 1.00 27.39  ? 83  GLU B CA  1 
ATOM   1382 C C   . GLU B 1 84 ? 13.807  -5.075  -34.648 1.00 28.13  ? 83  GLU B C   1 
ATOM   1383 O O   . GLU B 1 84 ? 14.387  -4.293  -35.412 1.00 28.01  ? 83  GLU B O   1 
ATOM   1384 C CB  . GLU B 1 84 ? 14.157  -4.801  -32.147 1.00 27.09  ? 83  GLU B CB  1 
ATOM   1385 C CG  . GLU B 1 84 ? 13.681  -4.156  -30.838 1.00 28.54  ? 83  GLU B CG  1 
ATOM   1386 C CD  . GLU B 1 84 ? 14.637  -4.455  -29.707 1.00 32.84  ? 83  GLU B CD  1 
ATOM   1387 O OE1 . GLU B 1 84 ? 15.541  -5.308  -29.885 1.00 30.46  ? 83  GLU B OE1 1 
ATOM   1388 O OE2 . GLU B 1 84 ? 14.536  -3.831  -28.610 1.00 33.43  ? 83  GLU B OE2 1 
ATOM   1389 N N   . ILE B 1 85 ? 13.659  -6.372  -34.932 1.00 26.12  ? 84  ILE B N   1 
ATOM   1390 C CA  . ILE B 1 85 ? 14.375  -6.915  -36.092 1.00 25.04  ? 84  ILE B CA  1 
ATOM   1391 C C   . ILE B 1 85 ? 13.749  -6.380  -37.383 1.00 27.55  ? 84  ILE B C   1 
ATOM   1392 O O   . ILE B 1 85 ? 14.452  -6.153  -38.386 1.00 25.00  ? 84  ILE B O   1 
ATOM   1393 C CB  . ILE B 1 85 ? 14.481  -8.451  -36.037 1.00 25.26  ? 84  ILE B CB  1 
ATOM   1394 C CG1 . ILE B 1 85 ? 15.524  -8.971  -37.043 1.00 25.95  ? 84  ILE B CG1 1 
ATOM   1395 C CG2 . ILE B 1 85 ? 13.129  -9.113  -36.266 1.00 25.10  ? 84  ILE B CG2 1 
ATOM   1396 C CD1 . ILE B 1 85 ? 15.980  -10.390 -36.739 1.00 24.34  ? 84  ILE B CD1 1 
ATOM   1397 N N   . GLN B 1 86 ? 12.460  -6.084  -37.278 1.00 26.67  ? 85  GLN B N   1 
ATOM   1398 C CA  . GLN B 1 86 ? 11.636  -5.546  -38.350 1.00 26.91  ? 85  GLN B CA  1 
ATOM   1399 C C   . GLN B 1 86 ? 11.898  -4.054  -38.554 1.00 32.95  ? 85  GLN B C   1 
ATOM   1400 O O   . GLN B 1 86 ? 12.013  -3.600  -39.695 1.00 34.32  ? 85  GLN B O   1 
ATOM   1401 C CB  . GLN B 1 86 ? 10.173  -5.834  -38.008 1.00 33.31  ? 85  GLN B CB  1 
ATOM   1402 N N   . ASN B 1 87 ? 11.980  -3.289  -37.463 1.00 27.98  ? 86  ASN B N   1 
ATOM   1403 C CA  . ASN B 1 87 ? 11.862  -1.834  -37.602 1.00 29.31  ? 86  ASN B CA  1 
ATOM   1404 C C   . ASN B 1 87 ? 13.171  -1.086  -37.416 1.00 29.34  ? 86  ASN B C   1 
ATOM   1405 O O   . ASN B 1 87 ? 13.290  0.066   -37.867 1.00 31.03  ? 86  ASN B O   1 
ATOM   1406 C CB  . ASN B 1 87 ? 10.875  -1.281  -36.574 1.00 32.52  ? 86  ASN B CB  1 
ATOM   1407 C CG  . ASN B 1 87 ? 9.486   -1.761  -36.901 1.00 38.70  ? 86  ASN B CG  1 
ATOM   1408 O OD1 . ASN B 1 87 ? 8.888   -1.282  -37.864 1.00 46.15  ? 86  ASN B OD1 1 
ATOM   1409 N ND2 . ASN B 1 87 ? 9.003   -2.767  -36.192 1.00 42.58  ? 86  ASN B ND2 1 
ATOM   1410 N N   . ASN B 1 88 ? 14.137  -1.679  -36.715 1.00 27.88  ? 87  ASN B N   1 
ATOM   1411 C CA  . ASN B 1 88 ? 15.392  -0.984  -36.455 1.00 29.32  ? 87  ASN B CA  1 
ATOM   1412 C C   . ASN B 1 88 ? 16.459  -1.990  -36.035 1.00 26.43  ? 87  ASN B C   1 
ATOM   1413 O O   . ASN B 1 88 ? 17.090  -1.886  -34.968 1.00 25.30  ? 87  ASN B O   1 
ATOM   1414 C CB  . ASN B 1 88 ? 15.219  0.205   -35.506 1.00 33.44  ? 87  ASN B CB  1 
ATOM   1415 C CG  . ASN B 1 88 ? 16.291  1.256   -35.689 1.00 34.61  ? 87  ASN B CG  1 
ATOM   1416 O OD1 . ASN B 1 88 ? 17.329  1.026   -36.337 1.00 30.98  ? 87  ASN B OD1 1 
ATOM   1417 N ND2 . ASN B 1 88 ? 16.066  2.422   -35.097 1.00 34.08  ? 87  ASN B ND2 1 
ATOM   1418 N N   . PRO B 1 89 ? 16.736  -2.986  -36.924 1.00 26.91  ? 88  PRO B N   1 
ATOM   1419 C CA  . PRO B 1 89 ? 17.675  -4.059  -36.609 1.00 24.43  ? 88  PRO B CA  1 
ATOM   1420 C C   . PRO B 1 89 ? 19.109  -3.603  -36.347 1.00 24.34  ? 88  PRO B C   1 
ATOM   1421 O O   . PRO B 1 89 ? 19.891  -4.349  -35.777 1.00 24.39  ? 88  PRO B O   1 
ATOM   1422 C CB  . PRO B 1 89 ? 17.624  -4.967  -37.905 1.00 24.79  ? 88  PRO B CB  1 
ATOM   1423 C CG  . PRO B 1 89 ? 17.126  -4.047  -39.013 1.00 24.22  ? 88  PRO B CG  1 
ATOM   1424 C CD  . PRO B 1 89 ? 16.146  -3.106  -38.273 1.00 25.45  ? 88  PRO B CD  1 
ATOM   1425 N N   . HIS B 1 90 ? 19.493  -2.398  -36.865 1.00 26.04  ? 89  HIS B N   1 
ATOM   1426 C CA  . HIS B 1 90 ? 20.886  -1.984  -36.792 1.00 25.29  ? 89  HIS B CA  1 
ATOM   1427 C C   . HIS B 1 90 ? 21.139  -0.884  -35.744 1.00 26.96  ? 89  HIS B C   1 
ATOM   1428 O O   . HIS B 1 90 ? 22.281  -0.419  -35.607 1.00 27.88  ? 89  HIS B O   1 
ATOM   1429 C CB  . HIS B 1 90 ? 21.442  -1.592  -38.178 1.00 25.51  ? 89  HIS B CB  1 
ATOM   1430 C CG  . HIS B 1 90 ? 21.265  -2.677  -39.194 1.00 27.43  ? 89  HIS B CG  1 
ATOM   1431 N ND1 . HIS B 1 90 ? 21.845  -3.917  -39.091 1.00 25.83  ? 89  HIS B ND1 1 
ATOM   1432 C CD2 . HIS B 1 90 ? 20.571  -2.695  -40.331 1.00 26.93  ? 89  HIS B CD2 1 
ATOM   1433 C CE1 . HIS B 1 90 ? 21.503  -4.652  -40.145 1.00 23.44  ? 89  HIS B CE1 1 
ATOM   1434 N NE2 . HIS B 1 90 ? 20.744  -3.924  -40.895 1.00 26.71  ? 89  HIS B NE2 1 
ATOM   1435 N N   . ALA B 1 91 ? 20.127  -0.595  -34.921 1.00 27.96  ? 90  ALA B N   1 
ATOM   1436 C CA  . ALA B 1 91 ? 20.286  0.402   -33.867 1.00 27.94  ? 90  ALA B CA  1 
ATOM   1437 C C   . ALA B 1 91 ? 21.281  -0.013  -32.775 1.00 31.67  ? 90  ALA B C   1 
ATOM   1438 O O   . ALA B 1 91 ? 21.569  -1.190  -32.522 1.00 28.71  ? 90  ALA B O   1 
ATOM   1439 C CB  . ALA B 1 91 ? 18.933  0.730   -33.269 1.00 28.38  ? 90  ALA B CB  1 
ATOM   1440 N N   . SER B 1 92 ? 21.773  1.001   -32.037 1.00 30.99  ? 91  SER B N   1 
ATOM   1441 C CA  . SER B 1 92 ? 22.434  0.771   -30.772 1.00 35.07  ? 91  SER B CA  1 
ATOM   1442 C C   . SER B 1 92 ? 21.355  0.574   -29.710 1.00 37.53  ? 91  SER B C   1 
ATOM   1443 O O   . SER B 1 92 ? 20.451  1.419   -29.592 1.00 38.57  ? 91  SER B O   1 
ATOM   1444 C CB  . SER B 1 92 ? 23.282  1.997   -30.435 1.00 39.13  ? 91  SER B CB  1 
ATOM   1445 O OG  . SER B 1 92 ? 23.549  2.032   -29.049 1.00 43.84  ? 91  SER B OG  1 
ATOM   1446 N N   . TYR B 1 93 ? 21.464  -0.551  -28.983 1.00 38.39  ? 92  TYR B N   1 
ATOM   1447 C CA  . TYR B 1 93 ? 20.592  -0.955  -27.893 1.00 39.48  ? 92  TYR B CA  1 
ATOM   1448 C C   . TYR B 1 93 ? 21.423  -0.921  -26.612 1.00 47.51  ? 92  TYR B C   1 
ATOM   1449 O O   . TYR B 1 93 ? 21.085  -1.562  -25.622 1.00 51.91  ? 92  TYR B O   1 
ATOM   1450 C CB  . TYR B 1 93 ? 19.917  -2.313  -28.167 1.00 34.43  ? 92  TYR B CB  1 
ATOM   1451 C CG  . TYR B 1 93 ? 18.900  -2.229  -29.294 1.00 27.64  ? 92  TYR B CG  1 
ATOM   1452 C CD1 . TYR B 1 93 ? 17.608  -1.778  -29.061 1.00 29.29  ? 92  TYR B CD1 1 
ATOM   1453 C CD2 . TYR B 1 93 ? 19.228  -2.605  -30.603 1.00 31.25  ? 92  TYR B CD2 1 
ATOM   1454 C CE1 . TYR B 1 93 ? 16.686  -1.631  -30.086 1.00 28.29  ? 92  TYR B CE1 1 
ATOM   1455 C CE2 . TYR B 1 93 ? 18.310  -2.453  -31.638 1.00 27.88  ? 92  TYR B CE2 1 
ATOM   1456 C CZ  . TYR B 1 93 ? 17.024  -2.006  -31.376 1.00 29.97  ? 92  TYR B CZ  1 
ATOM   1457 O OH  . TYR B 1 93 ? 16.066  -1.900  -32.351 1.00 32.46  ? 92  TYR B OH  1 
ATOM   1458 N N   . SER B 1 94 ? 22.512  -0.138  -26.667 1.00 58.76  ? 93  SER B N   1 
ATOM   1459 C CA  . SER B 1 94 ? 23.462  0.090   -25.588 1.00 65.26  ? 93  SER B CA  1 
ATOM   1460 C C   . SER B 1 94 ? 22.745  0.677   -24.366 1.00 78.49  ? 93  SER B C   1 
ATOM   1461 O O   . SER B 1 94 ? 21.687  1.329   -24.571 1.00 75.25  ? 93  SER B O   1 
ATOM   1462 C CB  . SER B 1 94 ? 24.556  1.037   -26.026 1.00 67.77  ? 93  SER B CB  1 
ATOM   1463 O OG  . SER B 1 94 ? 25.484  0.407   -26.896 1.00 74.18  ? 93  SER B OG  1 
ATOM   1464 O OXT . SER B 1 94 ? 23.294  0.494   -23.250 1.00 90.54  ? 93  SER B OXT 1 
ATOM   1465 N N   . HIS C 1 4  ? 32.772  -23.839 26.909  1.00 68.70  ? 3   HIS C N   1 
ATOM   1466 C CA  . HIS C 1 4  ? 31.720  -22.878 27.341  1.00 74.47  ? 3   HIS C CA  1 
ATOM   1467 C C   . HIS C 1 4  ? 31.181  -23.312 28.706  1.00 77.23  ? 3   HIS C C   1 
ATOM   1468 O O   . HIS C 1 4  ? 31.885  -23.978 29.469  1.00 74.54  ? 3   HIS C O   1 
ATOM   1469 C CB  . HIS C 1 4  ? 30.665  -22.721 26.234  1.00 70.99  ? 3   HIS C CB  1 
ATOM   1470 N N   . ALA C 1 5  ? 29.945  -22.890 29.011  1.00 78.66  ? 4   ALA C N   1 
ATOM   1471 C CA  . ALA C 1 5  ? 29.139  -23.419 30.102  1.00 70.02  ? 4   ALA C CA  1 
ATOM   1472 C C   . ALA C 1 5  ? 27.661  -23.260 29.768  1.00 74.70  ? 4   ALA C C   1 
ATOM   1473 O O   . ALA C 1 5  ? 27.254  -22.283 29.136  1.00 72.31  ? 4   ALA C O   1 
ATOM   1474 C CB  . ALA C 1 5  ? 29.444  -22.693 31.372  1.00 73.80  ? 4   ALA C CB  1 
ATOM   1475 N N   . PHE C 1 6  ? 26.858  -24.217 30.234  1.00 61.15  ? 5   PHE C N   1 
ATOM   1476 C CA  . PHE C 1 6  ? 25.481  -24.286 29.792  1.00 55.44  ? 5   PHE C CA  1 
ATOM   1477 C C   . PHE C 1 6  ? 24.581  -24.387 31.016  1.00 62.57  ? 5   PHE C C   1 
ATOM   1478 O O   . PHE C 1 6  ? 24.658  -25.363 31.760  1.00 76.83  ? 5   PHE C O   1 
ATOM   1479 C CB  . PHE C 1 6  ? 25.335  -25.470 28.820  1.00 49.52  ? 5   PHE C CB  1 
ATOM   1480 C CG  . PHE C 1 6  ? 26.139  -25.408 27.522  1.00 44.35  ? 5   PHE C CG  1 
ATOM   1481 C CD1 . PHE C 1 6  ? 27.270  -26.193 27.326  1.00 45.67  ? 5   PHE C CD1 1 
ATOM   1482 C CD2 . PHE C 1 6  ? 25.764  -24.556 26.486  1.00 48.52  ? 5   PHE C CD2 1 
ATOM   1483 C CE1 . PHE C 1 6  ? 27.988  -26.144 26.131  1.00 49.45  ? 5   PHE C CE1 1 
ATOM   1484 C CE2 . PHE C 1 6  ? 26.481  -24.512 25.294  1.00 45.20  ? 5   PHE C CE2 1 
ATOM   1485 C CZ  . PHE C 1 6  ? 27.589  -25.301 25.110  1.00 43.73  ? 5   PHE C CZ  1 
ATOM   1486 N N   . LYS C 1 7  ? 23.746  -23.365 31.222  1.00 57.30  ? 6   LYS C N   1 
ATOM   1487 C CA  . LYS C 1 7  ? 22.743  -23.388 32.279  1.00 57.45  ? 6   LYS C CA  1 
ATOM   1488 C C   . LYS C 1 7  ? 21.454  -23.870 31.627  1.00 47.99  ? 6   LYS C C   1 
ATOM   1489 O O   . LYS C 1 7  ? 21.362  -23.837 30.400  1.00 50.43  ? 6   LYS C O   1 
ATOM   1490 C CB  . LYS C 1 7  ? 22.582  -22.012 32.948  1.00 55.99  ? 6   LYS C CB  1 
ATOM   1491 N N   . PRO C 1 8  ? 20.434  -24.354 32.374  1.00 52.35  ? 7   PRO C N   1 
ATOM   1492 C CA  . PRO C 1 8  ? 19.151  -24.700 31.757  1.00 52.48  ? 7   PRO C CA  1 
ATOM   1493 C C   . PRO C 1 8  ? 18.588  -23.534 30.942  1.00 60.94  ? 7   PRO C C   1 
ATOM   1494 O O   . PRO C 1 8  ? 18.889  -22.371 31.222  1.00 66.68  ? 7   PRO C O   1 
ATOM   1495 C CB  . PRO C 1 8  ? 18.273  -25.087 32.951  1.00 55.23  ? 7   PRO C CB  1 
ATOM   1496 C CG  . PRO C 1 8  ? 19.270  -25.601 33.962  1.00 51.31  ? 7   PRO C CG  1 
ATOM   1497 C CD  . PRO C 1 8  ? 20.473  -24.668 33.816  1.00 48.96  ? 7   PRO C CD  1 
ATOM   1498 N N   . GLY C 1 9  ? 17.812  -23.867 29.902  1.00 58.40  ? 8   GLY C N   1 
ATOM   1499 C CA  . GLY C 1 9  ? 17.132  -22.882 29.074  1.00 53.25  ? 8   GLY C CA  1 
ATOM   1500 C C   . GLY C 1 9  ? 17.975  -22.390 27.898  1.00 50.09  ? 8   GLY C C   1 
ATOM   1501 O O   . GLY C 1 9  ? 17.416  -21.887 26.923  1.00 51.31  ? 8   GLY C O   1 
ATOM   1502 N N   . ASP C 1 10 ? 19.304  -22.546 27.994  1.00 46.65  ? 9   ASP C N   1 
ATOM   1503 C CA  . ASP C 1 10 ? 20.253  -22.168 26.960  1.00 37.72  ? 9   ASP C CA  1 
ATOM   1504 C C   . ASP C 1 10 ? 19.961  -22.899 25.643  1.00 42.71  ? 9   ASP C C   1 
ATOM   1505 O O   . ASP C 1 10 ? 19.707  -24.102 25.627  1.00 39.05  ? 9   ASP C O   1 
ATOM   1506 C CB  . ASP C 1 10 ? 21.687  -22.437 27.388  1.00 41.21  ? 9   ASP C CB  1 
ATOM   1507 C CG  . ASP C 1 10 ? 22.324  -21.509 28.426  1.00 53.85  ? 9   ASP C CG  1 
ATOM   1508 O OD1 . ASP C 1 10 ? 21.644  -20.586 28.896  1.00 58.01  ? 9   ASP C OD1 1 
ATOM   1509 O OD2 . ASP C 1 10 ? 23.506  -21.725 28.774  1.00 54.29  ? 9   ASP C OD2 1 
ATOM   1510 N N   . LEU C 1 11 ? 20.021  -22.154 24.530  1.00 42.58  ? 10  LEU C N   1 
ATOM   1511 C CA  . LEU C 1 11 ? 19.698  -22.664 23.203  1.00 41.12  ? 10  LEU C CA  1 
ATOM   1512 C C   . LEU C 1 11 ? 20.958  -23.128 22.495  1.00 34.20  ? 10  LEU C C   1 
ATOM   1513 O O   . LEU C 1 11 ? 21.943  -22.406 22.470  1.00 36.20  ? 10  LEU C O   1 
ATOM   1514 C CB  . LEU C 1 11 ? 19.042  -21.540 22.402  1.00 38.53  ? 10  LEU C CB  1 
ATOM   1515 C CG  . LEU C 1 11 ? 17.734  -21.017 22.979  1.00 36.61  ? 10  LEU C CG  1 
ATOM   1516 C CD1 . LEU C 1 11 ? 17.129  -20.074 21.946  1.00 38.54  ? 10  LEU C CD1 1 
ATOM   1517 C CD2 . LEU C 1 11 ? 16.837  -22.201 23.297  1.00 37.61  ? 10  LEU C CD2 1 
ATOM   1518 N N   . VAL C 1 12 ? 20.910  -24.315 21.857  1.00 33.72  ? 11  VAL C N   1 
ATOM   1519 C CA  . VAL C 1 12 ? 22.111  -24.930 21.309  1.00 30.77  ? 11  VAL C CA  1 
ATOM   1520 C C   . VAL C 1 12 ? 21.739  -25.685 20.018  1.00 30.32  ? 11  VAL C C   1 
ATOM   1521 O O   . VAL C 1 12 ? 20.542  -25.871 19.753  1.00 29.16  ? 11  VAL C O   1 
ATOM   1522 C CB  . VAL C 1 12 ? 22.742  -25.918 22.323  1.00 32.35  ? 11  VAL C CB  1 
ATOM   1523 C CG1 . VAL C 1 12 ? 23.085  -25.253 23.668  1.00 34.73  ? 11  VAL C CG1 1 
ATOM   1524 C CG2 . VAL C 1 12 ? 21.866  -27.145 22.537  1.00 32.00  ? 11  VAL C CG2 1 
ATOM   1525 N N   . PHE C 1 13 ? 22.774  -26.067 19.247  1.00 28.84  ? 12  PHE C N   1 
ATOM   1526 C CA  . PHE C 1 13 ? 22.761  -27.233 18.367  1.00 31.18  ? 12  PHE C CA  1 
ATOM   1527 C C   . PHE C 1 13 ? 23.452  -28.406 19.074  1.00 31.15  ? 12  PHE C C   1 
ATOM   1528 O O   . PHE C 1 13 ? 24.534  -28.269 19.665  1.00 31.44  ? 12  PHE C O   1 
ATOM   1529 C CB  . PHE C 1 13 ? 23.419  -26.963 17.005  1.00 30.91  ? 12  PHE C CB  1 
ATOM   1530 C CG  . PHE C 1 13 ? 22.635  -25.973 16.158  1.00 35.08  ? 12  PHE C CG  1 
ATOM   1531 C CD1 . PHE C 1 13 ? 21.641  -26.413 15.282  1.00 33.75  ? 12  PHE C CD1 1 
ATOM   1532 C CD2 . PHE C 1 13 ? 22.899  -24.602 16.219  1.00 36.30  ? 12  PHE C CD2 1 
ATOM   1533 C CE1 . PHE C 1 13 ? 20.916  -25.511 14.514  1.00 36.11  ? 12  PHE C CE1 1 
ATOM   1534 C CE2 . PHE C 1 13 ? 22.164  -23.712 15.450  1.00 39.20  ? 12  PHE C CE2 1 
ATOM   1535 C CZ  . PHE C 1 13 ? 21.183  -24.167 14.595  1.00 38.83  ? 12  PHE C CZ  1 
ATOM   1536 N N   . ALA C 1 14 ? 22.808  -29.579 19.029  1.00 28.03  ? 13  ALA C N   1 
ATOM   1537 C CA  . ALA C 1 14 ? 23.292  -30.747 19.746  1.00 24.65  ? 13  ALA C CA  1 
ATOM   1538 C C   . ALA C 1 14 ? 23.574  -31.873 18.763  1.00 31.08  ? 13  ALA C C   1 
ATOM   1539 O O   . ALA C 1 14 ? 22.707  -32.172 17.942  1.00 26.42  ? 13  ALA C O   1 
ATOM   1540 C CB  . ALA C 1 14 ? 22.240  -31.177 20.733  1.00 22.34  ? 13  ALA C CB  1 
ATOM   1541 N N   . LYS C 1 15 ? 24.784  -32.447 18.848  1.00 29.67  ? 14  LYS C N   1 
ATOM   1542 C CA  . LYS C 1 15 ? 25.211  -33.461 17.887  1.00 28.99  ? 14  LYS C CA  1 
ATOM   1543 C C   . LYS C 1 15 ? 25.182  -34.844 18.524  1.00 27.86  ? 14  LYS C C   1 
ATOM   1544 O O   . LYS C 1 15 ? 25.919  -35.141 19.469  1.00 29.21  ? 14  LYS C O   1 
ATOM   1545 C CB  . LYS C 1 15 ? 26.601  -33.168 17.294  1.00 30.02  ? 14  LYS C CB  1 
ATOM   1546 C CG  . LYS C 1 15 ? 27.009  -34.189 16.198  1.00 30.29  ? 14  LYS C CG  1 
ATOM   1547 C CD  . LYS C 1 15 ? 26.228  -33.959 14.903  1.00 31.04  ? 14  LYS C CD  1 
ATOM   1548 C CE  . LYS C 1 15 ? 26.762  -34.763 13.723  1.00 31.94  ? 14  LYS C CE  1 
ATOM   1549 N NZ  . LYS C 1 15 ? 26.684  -36.183 14.037  1.00 31.46  ? 14  LYS C NZ  1 
ATOM   1550 N N   . MET C 1 16 ? 24.373  -35.734 17.949  1.00 26.06  ? 15  MET C N   1 
ATOM   1551 C CA  . MET C 1 16 ? 24.406  -37.159 18.283  1.00 26.24  ? 15  MET C CA  1 
ATOM   1552 C C   . MET C 1 16 ? 24.895  -37.953 17.071  1.00 30.58  ? 15  MET C C   1 
ATOM   1553 O O   . MET C 1 16 ? 24.674  -37.581 15.918  1.00 25.54  ? 15  MET C O   1 
ATOM   1554 C CB  . MET C 1 16 ? 22.993  -37.656 18.613  1.00 31.12  ? 15  MET C CB  1 
ATOM   1555 C CG  . MET C 1 16 ? 22.397  -36.970 19.808  1.00 35.29  ? 15  MET C CG  1 
ATOM   1556 S SD  . MET C 1 16 ? 20.808  -37.688 20.264  1.00 37.51  ? 15  MET C SD  1 
ATOM   1557 C CE  . MET C 1 16 ? 19.809  -37.108 18.881  1.00 37.74  ? 15  MET C CE  1 
ATOM   1558 N N   . LYS C 1 17 ? 25.550  -39.088 17.337  1.00 29.97  ? 16  LYS C N   1 
ATOM   1559 C CA  . LYS C 1 17 ? 25.939  -39.979 16.250  1.00 32.95  ? 16  LYS C CA  1 
ATOM   1560 C C   . LYS C 1 17 ? 24.675  -40.401 15.499  1.00 25.76  ? 16  LYS C C   1 
ATOM   1561 O O   . LYS C 1 17 ? 23.699  -40.839 16.102  1.00 30.68  ? 16  LYS C O   1 
ATOM   1562 C CB  . LYS C 1 17 ? 26.695  -41.174 16.849  1.00 30.49  ? 16  LYS C CB  1 
ATOM   1563 C CG  . LYS C 1 17 ? 27.201  -42.257 15.884  1.00 35.03  ? 16  LYS C CG  1 
ATOM   1564 C CD  . LYS C 1 17 ? 28.292  -41.565 15.074  1.00 37.88  ? 16  LYS C CD  1 
ATOM   1565 C CE  . LYS C 1 17 ? 29.186  -42.556 14.371  1.00 51.45  ? 16  LYS C CE  1 
ATOM   1566 N NZ  . LYS C 1 17 ? 30.377  -41.883 13.842  1.00 48.54  ? 16  LYS C NZ  1 
ATOM   1567 N N   . GLY C 1 18 ? 24.722  -40.243 14.180  1.00 33.13  ? 17  GLY C N   1 
ATOM   1568 C CA  . GLY C 1 18 ? 23.619  -40.751 13.373  1.00 31.49  ? 17  GLY C CA  1 
ATOM   1569 C C   . GLY C 1 18 ? 22.691  -39.622 12.933  1.00 31.35  ? 17  GLY C C   1 
ATOM   1570 O O   . GLY C 1 18 ? 21.716  -39.880 12.237  1.00 29.68  ? 17  GLY C O   1 
ATOM   1571 N N   . TYR C 1 19 ? 22.949  -38.391 13.397  1.00 28.29  ? 18  TYR C N   1 
ATOM   1572 C CA  . TYR C 1 19 ? 22.043  -37.266 13.145  1.00 27.87  ? 18  TYR C CA  1 
ATOM   1573 C C   . TYR C 1 19 ? 22.815  -35.983 12.891  1.00 27.78  ? 18  TYR C C   1 
ATOM   1574 O O   . TYR C 1 19 ? 23.929  -35.802 13.407  1.00 26.50  ? 18  TYR C O   1 
ATOM   1575 C CB  . TYR C 1 19 ? 21.225  -37.002 14.406  1.00 24.00  ? 18  TYR C CB  1 
ATOM   1576 C CG  . TYR C 1 19 ? 20.388  -38.201 14.811  1.00 27.76  ? 18  TYR C CG  1 
ATOM   1577 C CD1 . TYR C 1 19 ? 20.901  -39.202 15.629  1.00 28.61  ? 18  TYR C CD1 1 
ATOM   1578 C CD2 . TYR C 1 19 ? 19.094  -38.326 14.330  1.00 27.83  ? 18  TYR C CD2 1 
ATOM   1579 C CE1 . TYR C 1 19 ? 20.127  -40.283 16.009  1.00 30.09  ? 18  TYR C CE1 1 
ATOM   1580 C CE2 . TYR C 1 19 ? 18.319  -39.412 14.693  1.00 32.72  ? 18  TYR C CE2 1 
ATOM   1581 C CZ  . TYR C 1 19 ? 18.838  -40.387 15.521  1.00 32.50  ? 18  TYR C CZ  1 
ATOM   1582 O OH  . TYR C 1 19 ? 18.044  -41.455 15.834  1.00 40.98  ? 18  TYR C OH  1 
ATOM   1583 N N   . PRO C 1 20 ? 22.245  -35.044 12.104  1.00 27.23  ? 19  PRO C N   1 
ATOM   1584 C CA  . PRO C 1 20 ? 22.884  -33.751 11.871  1.00 27.78  ? 19  PRO C CA  1 
ATOM   1585 C C   . PRO C 1 20 ? 22.845  -32.925 13.162  1.00 27.59  ? 19  PRO C C   1 
ATOM   1586 O O   . PRO C 1 20 ? 22.043  -33.187 14.070  1.00 24.71  ? 19  PRO C O   1 
ATOM   1587 C CB  . PRO C 1 20 ? 21.988  -33.131 10.759  1.00 30.79  ? 19  PRO C CB  1 
ATOM   1588 C CG  . PRO C 1 20 ? 20.631  -33.732 11.023  1.00 30.62  ? 19  PRO C CG  1 
ATOM   1589 C CD  . PRO C 1 20 ? 20.931  -35.171 11.432  1.00 26.55  ? 19  PRO C CD  1 
ATOM   1590 N N   . HIS C 1 21 ? 23.676  -31.878 13.210  1.00 27.66  ? 20  HIS C N   1 
ATOM   1591 C CA  . HIS C 1 21 ? 23.600  -30.960 14.348  1.00 27.45  ? 20  HIS C CA  1 
ATOM   1592 C C   . HIS C 1 21 ? 22.172  -30.439 14.479  1.00 29.88  ? 20  HIS C C   1 
ATOM   1593 O O   . HIS C 1 21 ? 21.619  -29.898 13.515  1.00 29.97  ? 20  HIS C O   1 
ATOM   1594 C CB  . HIS C 1 21 ? 24.567  -29.798 14.151  1.00 32.37  ? 20  HIS C CB  1 
ATOM   1595 C CG  . HIS C 1 21 ? 25.994  -30.236 14.191  1.00 30.34  ? 20  HIS C CG  1 
ATOM   1596 N ND1 . HIS C 1 21 ? 26.645  -30.909 13.179  1.00 32.91  ? 20  HIS C ND1 1 
ATOM   1597 C CD2 . HIS C 1 21 ? 26.897  -30.046 15.176  1.00 33.69  ? 20  HIS C CD2 1 
ATOM   1598 C CE1 . HIS C 1 21 ? 27.907  -31.135 13.553  1.00 36.97  ? 20  HIS C CE1 1 
ATOM   1599 N NE2 . HIS C 1 21 ? 28.090  -30.582 14.747  1.00 33.64  ? 20  HIS C NE2 1 
ATOM   1600 N N   . TRP C 1 22 ? 21.584  -30.612 15.673  1.00 24.42  ? 21  TRP C N   1 
ATOM   1601 C CA  . TRP C 1 22 ? 20.134  -30.493 15.817  1.00 24.68  ? 21  TRP C CA  1 
ATOM   1602 C C   . TRP C 1 22 ? 19.746  -29.338 16.748  1.00 26.30  ? 21  TRP C C   1 
ATOM   1603 O O   . TRP C 1 22 ? 20.316  -29.189 17.838  1.00 25.06  ? 21  TRP C O   1 
ATOM   1604 C CB  . TRP C 1 22 ? 19.564  -31.806 16.381  1.00 24.25  ? 21  TRP C CB  1 
ATOM   1605 C CG  . TRP C 1 22 ? 18.104  -31.977 16.043  1.00 24.19  ? 21  TRP C CG  1 
ATOM   1606 C CD1 . TRP C 1 22 ? 17.004  -31.413 16.639  1.00 26.22  ? 21  TRP C CD1 1 
ATOM   1607 C CD2 . TRP C 1 22 ? 17.611  -32.864 15.006  1.00 26.00  ? 21  TRP C CD2 1 
ATOM   1608 N NE1 . TRP C 1 22 ? 15.867  -31.847 15.987  1.00 26.78  ? 21  TRP C NE1 1 
ATOM   1609 C CE2 . TRP C 1 22 ? 16.202  -32.752 15.010  1.00 26.97  ? 21  TRP C CE2 1 
ATOM   1610 C CE3 . TRP C 1 22 ? 18.233  -33.731 14.094  1.00 24.67  ? 21  TRP C CE3 1 
ATOM   1611 C CZ2 . TRP C 1 22 ? 15.410  -33.492 14.114  1.00 27.72  ? 21  TRP C CZ2 1 
ATOM   1612 C CZ3 . TRP C 1 22 ? 17.461  -34.434 13.184  1.00 27.03  ? 21  TRP C CZ3 1 
ATOM   1613 C CH2 . TRP C 1 22 ? 16.062  -34.356 13.247  1.00 25.41  ? 21  TRP C CH2 1 
ATOM   1614 N N   . PRO C 1 23 ? 18.719  -28.512 16.418  1.00 26.81  ? 22  PRO C N   1 
ATOM   1615 C CA  . PRO C 1 23 ? 18.321  -27.412 17.297  1.00 24.89  ? 22  PRO C CA  1 
ATOM   1616 C C   . PRO C 1 23 ? 17.712  -27.958 18.581  1.00 25.17  ? 22  PRO C C   1 
ATOM   1617 O O   . PRO C 1 23 ? 16.883  -28.853 18.539  1.00 27.16  ? 22  PRO C O   1 
ATOM   1618 C CB  . PRO C 1 23 ? 17.293  -26.659 16.420  1.00 27.14  ? 22  PRO C CB  1 
ATOM   1619 C CG  . PRO C 1 23 ? 16.698  -27.738 15.532  1.00 24.96  ? 22  PRO C CG  1 
ATOM   1620 C CD  . PRO C 1 23 ? 17.948  -28.518 15.149  1.00 24.79  ? 22  PRO C CD  1 
ATOM   1621 N N   . ALA C 1 24 ? 18.193  -27.439 19.718  1.00 28.11  ? 23  ALA C N   1 
ATOM   1622 C CA  . ALA C 1 24 ? 17.886  -27.998 21.029  1.00 32.72  ? 23  ALA C CA  1 
ATOM   1623 C C   . ALA C 1 24 ? 18.012  -26.928 22.120  1.00 34.31  ? 23  ALA C C   1 
ATOM   1624 O O   . ALA C 1 24 ? 18.447  -25.804 21.859  1.00 31.51  ? 23  ALA C O   1 
ATOM   1625 C CB  . ALA C 1 24 ? 18.848  -29.148 21.298  1.00 30.13  ? 23  ALA C CB  1 
ATOM   1626 N N   . ARG C 1 25 ? 17.622  -27.289 23.350  1.00 32.72  ? 24  ARG C N   1 
ATOM   1627 C CA  . ARG C 1 25 ? 17.989  -26.484 24.509  1.00 34.06  ? 24  ARG C CA  1 
ATOM   1628 C C   . ARG C 1 25 ? 18.431  -27.400 25.654  1.00 33.07  ? 24  ARG C C   1 
ATOM   1629 O O   . ARG C 1 25 ? 18.105  -28.587 25.652  1.00 34.35  ? 24  ARG C O   1 
ATOM   1630 C CB  . ARG C 1 25 ? 16.757  -25.707 24.972  1.00 34.77  ? 24  ARG C CB  1 
ATOM   1631 C CG  . ARG C 1 25 ? 15.492  -26.460 25.345  1.00 40.45  ? 24  ARG C CG  1 
ATOM   1632 C CD  . ARG C 1 25 ? 14.451  -25.550 26.017  1.00 41.86  ? 24  ARG C CD  1 
ATOM   1633 N NE  . ARG C 1 25 ? 13.274  -26.375 26.332  1.00 49.63  ? 24  ARG C NE  1 
ATOM   1634 C CZ  . ARG C 1 25 ? 11.995  -26.229 25.988  1.00 51.33  ? 24  ARG C CZ  1 
ATOM   1635 N NH1 . ARG C 1 25 ? 11.594  -25.193 25.269  1.00 52.33  ? 24  ARG C NH1 1 
ATOM   1636 N NH2 . ARG C 1 25 ? 11.106  -27.128 26.387  1.00 49.99  ? 24  ARG C NH2 1 
ATOM   1637 N N   . ILE C 1 26 ? 19.139  -26.809 26.618  1.00 36.07  ? 25  ILE C N   1 
ATOM   1638 C CA  . ILE C 1 26 ? 19.488  -27.442 27.885  1.00 34.15  ? 25  ILE C CA  1 
ATOM   1639 C C   . ILE C 1 26 ? 18.259  -27.470 28.782  1.00 42.01  ? 25  ILE C C   1 
ATOM   1640 O O   . ILE C 1 26 ? 17.659  -26.433 29.036  1.00 47.56  ? 25  ILE C O   1 
ATOM   1641 C CB  . ILE C 1 26 ? 20.648  -26.680 28.559  1.00 35.80  ? 25  ILE C CB  1 
ATOM   1642 C CG1 . ILE C 1 26 ? 21.806  -26.383 27.619  1.00 36.08  ? 25  ILE C CG1 1 
ATOM   1643 C CG2 . ILE C 1 26 ? 21.118  -27.409 29.822  1.00 38.47  ? 25  ILE C CG2 1 
ATOM   1644 C CD1 . ILE C 1 26 ? 22.618  -27.575 27.144  1.00 39.13  ? 25  ILE C CD1 1 
ATOM   1645 N N   . ASP C 1 27 ? 17.904  -28.662 29.261  1.00 44.95  ? 26  ASP C N   1 
ATOM   1646 C CA  . ASP C 1 27 ? 16.817  -28.853 30.208  1.00 52.13  ? 26  ASP C CA  1 
ATOM   1647 C C   . ASP C 1 27 ? 17.301  -28.746 31.652  1.00 57.12  ? 26  ASP C C   1 
ATOM   1648 O O   . ASP C 1 27 ? 18.504  -28.774 31.911  1.00 58.00  ? 26  ASP C O   1 
ATOM   1649 C CB  . ASP C 1 27 ? 16.138  -30.193 30.004  1.00 55.35  ? 26  ASP C CB  1 
ATOM   1650 C CG  . ASP C 1 27 ? 14.783  -30.105 29.327  1.00 62.31  ? 26  ASP C CG  1 
ATOM   1651 O OD1 . ASP C 1 27 ? 14.518  -29.033 28.727  1.00 60.16  ? 26  ASP C OD1 1 
ATOM   1652 O OD2 . ASP C 1 27 ? 13.998  -31.081 29.475  1.00 55.53  ? 26  ASP C OD2 1 
ATOM   1653 N N   . ASP C 1 28 ? 16.324  -28.649 32.572  1.00 71.21  ? 27  ASP C N   1 
ATOM   1654 C CA  . ASP C 1 28 ? 16.513  -28.530 34.012  1.00 68.86  ? 27  ASP C CA  1 
ATOM   1655 C C   . ASP C 1 28 ? 17.176  -29.803 34.549  1.00 73.67  ? 27  ASP C C   1 
ATOM   1656 O O   . ASP C 1 28 ? 16.507  -30.855 34.486  1.00 73.20  ? 27  ASP C O   1 
ATOM   1657 C CB  . ASP C 1 28 ? 15.185  -28.304 34.720  1.00 68.32  ? 27  ASP C CB  1 
ATOM   1658 N N   . LYS C 1 35 ? 19.830  -38.988 37.934  1.00 52.68  ? 34  LYS C N   1 
ATOM   1659 C CA  . LYS C 1 35 ? 20.829  -37.931 37.623  1.00 56.08  ? 34  LYS C CA  1 
ATOM   1660 C C   . LYS C 1 35 ? 21.480  -38.261 36.279  1.00 55.32  ? 34  LYS C C   1 
ATOM   1661 O O   . LYS C 1 35 ? 21.476  -39.420 35.855  1.00 52.45  ? 34  LYS C O   1 
ATOM   1662 C CB  . LYS C 1 35 ? 21.837  -37.787 38.773  1.00 56.94  ? 34  LYS C CB  1 
ATOM   1663 N N   . PRO C 1 36 ? 22.038  -37.261 35.555  1.00 53.58  ? 35  PRO C N   1 
ATOM   1664 C CA  . PRO C 1 36 ? 22.712  -37.529 34.285  1.00 53.09  ? 35  PRO C CA  1 
ATOM   1665 C C   . PRO C 1 36 ? 23.883  -38.482 34.517  1.00 53.66  ? 35  PRO C C   1 
ATOM   1666 O O   . PRO C 1 36 ? 24.359  -38.643 35.649  1.00 48.64  ? 35  PRO C O   1 
ATOM   1667 C CB  . PRO C 1 36 ? 23.182  -36.136 33.791  1.00 56.15  ? 35  PRO C CB  1 
ATOM   1668 C CG  . PRO C 1 36 ? 22.405  -35.138 34.620  1.00 52.18  ? 35  PRO C CG  1 
ATOM   1669 C CD  . PRO C 1 36 ? 22.054  -35.834 35.930  1.00 55.40  ? 35  PRO C CD  1 
ATOM   1670 N N   . PRO C 1 37 ? 24.382  -39.176 33.472  1.00 50.43  ? 36  PRO C N   1 
ATOM   1671 C CA  . PRO C 1 37 ? 25.727  -39.738 33.546  1.00 48.72  ? 36  PRO C CA  1 
ATOM   1672 C C   . PRO C 1 37 ? 26.682  -38.604 33.910  1.00 44.60  ? 36  PRO C C   1 
ATOM   1673 O O   . PRO C 1 37 ? 26.378  -37.421 33.713  1.00 37.17  ? 36  PRO C O   1 
ATOM   1674 C CB  . PRO C 1 37 ? 25.971  -40.321 32.142  1.00 44.88  ? 36  PRO C CB  1 
ATOM   1675 C CG  . PRO C 1 37 ? 24.568  -40.629 31.657  1.00 42.03  ? 36  PRO C CG  1 
ATOM   1676 C CD  . PRO C 1 37 ? 23.687  -39.530 32.226  1.00 45.78  ? 36  PRO C CD  1 
ATOM   1677 N N   . PRO C 1 38 ? 27.855  -38.941 34.487  1.00 42.98  ? 37  PRO C N   1 
ATOM   1678 C CA  . PRO C 1 38 ? 28.867  -37.939 34.810  1.00 38.93  ? 37  PRO C CA  1 
ATOM   1679 C C   . PRO C 1 38 ? 29.145  -37.010 33.639  1.00 36.92  ? 37  PRO C C   1 
ATOM   1680 O O   . PRO C 1 38 ? 29.419  -37.473 32.535  1.00 38.02  ? 37  PRO C O   1 
ATOM   1681 C CB  . PRO C 1 38 ? 30.079  -38.833 35.109  1.00 40.33  ? 37  PRO C CB  1 
ATOM   1682 C CG  . PRO C 1 38 ? 29.455  -40.064 35.723  1.00 42.24  ? 37  PRO C CG  1 
ATOM   1683 C CD  . PRO C 1 38 ? 28.251  -40.314 34.853  1.00 46.14  ? 37  PRO C CD  1 
ATOM   1684 N N   . ASN C 1 39 ? 29.033  -35.701 33.904  1.00 36.15  ? 38  ASN C N   1 
ATOM   1685 C CA  . ASN C 1 39 ? 29.454  -34.657 32.990  1.00 35.49  ? 38  ASN C CA  1 
ATOM   1686 C C   . ASN C 1 39 ? 28.563  -34.599 31.747  1.00 39.30  ? 38  ASN C C   1 
ATOM   1687 O O   . ASN C 1 39 ? 29.010  -34.145 30.691  1.00 45.89  ? 38  ASN C O   1 
ATOM   1688 C CB  . ASN C 1 39 ? 30.933  -34.778 32.645  1.00 39.50  ? 38  ASN C CB  1 
ATOM   1689 C CG  . ASN C 1 39 ? 31.532  -33.543 32.012  1.00 51.15  ? 38  ASN C CG  1 
ATOM   1690 O OD1 . ASN C 1 39 ? 31.179  -32.412 32.368  1.00 61.13  ? 38  ASN C OD1 1 
ATOM   1691 N ND2 . ASN C 1 39 ? 32.446  -33.733 31.071  1.00 52.50  ? 38  ASN C ND2 1 
ATOM   1692 N N   . LYS C 1 40 ? 27.306  -35.027 31.873  1.00 33.89  ? 39  LYS C N   1 
ATOM   1693 C CA  . LYS C 1 40 ? 26.392  -34.897 30.747  1.00 32.54  ? 39  LYS C CA  1 
ATOM   1694 C C   . LYS C 1 40 ? 25.251  -33.953 31.106  1.00 33.07  ? 39  LYS C C   1 
ATOM   1695 O O   . LYS C 1 40 ? 24.826  -33.878 32.253  1.00 35.31  ? 39  LYS C O   1 
ATOM   1696 C CB  . LYS C 1 40 ? 25.740  -36.239 30.397  1.00 30.22  ? 39  LYS C CB  1 
ATOM   1697 C CG  . LYS C 1 40 ? 26.739  -37.334 30.127  1.00 36.15  ? 39  LYS C CG  1 
ATOM   1698 C CD  . LYS C 1 40 ? 27.564  -37.133 28.870  1.00 41.63  ? 39  LYS C CD  1 
ATOM   1699 C CE  . LYS C 1 40 ? 28.237  -38.428 28.528  1.00 43.33  ? 39  LYS C CE  1 
ATOM   1700 N NZ  . LYS C 1 40 ? 29.184  -38.226 27.427  1.00 47.96  ? 39  LYS C NZ  1 
ATOM   1701 N N   . TYR C 1 41 ? 24.765  -33.239 30.086  1.00 32.41  ? 40  TYR C N   1 
ATOM   1702 C CA  . TYR C 1 41 ? 23.628  -32.335 30.190  1.00 30.98  ? 40  TYR C CA  1 
ATOM   1703 C C   . TYR C 1 41 ? 22.371  -33.012 29.648  1.00 33.03  ? 40  TYR C C   1 
ATOM   1704 O O   . TYR C 1 41 ? 22.424  -33.782 28.686  1.00 32.26  ? 40  TYR C O   1 
ATOM   1705 C CB  . TYR C 1 41 ? 23.832  -31.098 29.300  1.00 29.32  ? 40  TYR C CB  1 
ATOM   1706 C CG  . TYR C 1 41 ? 24.977  -30.192 29.731  1.00 30.93  ? 40  TYR C CG  1 
ATOM   1707 C CD1 . TYR C 1 41 ? 26.271  -30.393 29.250  1.00 31.96  ? 40  TYR C CD1 1 
ATOM   1708 C CD2 . TYR C 1 41 ? 24.773  -29.135 30.628  1.00 36.38  ? 40  TYR C CD2 1 
ATOM   1709 C CE1 . TYR C 1 41 ? 27.335  -29.602 29.651  1.00 39.39  ? 40  TYR C CE1 1 
ATOM   1710 C CE2 . TYR C 1 41 ? 25.831  -28.315 31.004  1.00 35.52  ? 40  TYR C CE2 1 
ATOM   1711 C CZ  . TYR C 1 41 ? 27.113  -28.562 30.537  1.00 39.32  ? 40  TYR C CZ  1 
ATOM   1712 O OH  . TYR C 1 41 ? 28.181  -27.798 30.913  1.00 51.03  ? 40  TYR C OH  1 
ATOM   1713 N N   . PRO C 1 42 ? 21.202  -32.698 30.255  1.00 31.07  ? 41  PRO C N   1 
ATOM   1714 C CA  . PRO C 1 42 ? 19.898  -33.123 29.736  1.00 31.84  ? 41  PRO C CA  1 
ATOM   1715 C C   . PRO C 1 42 ? 19.546  -32.191 28.577  1.00 32.74  ? 41  PRO C C   1 
ATOM   1716 O O   . PRO C 1 42 ? 19.532  -30.964 28.738  1.00 34.54  ? 41  PRO C O   1 
ATOM   1717 C CB  . PRO C 1 42 ? 18.933  -32.949 30.934  1.00 33.41  ? 41  PRO C CB  1 
ATOM   1718 C CG  . PRO C 1 42 ? 19.651  -31.998 31.856  1.00 33.04  ? 41  PRO C CG  1 
ATOM   1719 C CD  . PRO C 1 42 ? 21.108  -31.834 31.445  1.00 37.76  ? 41  PRO C CD  1 
ATOM   1720 N N   . ILE C 1 43 ? 19.326  -32.800 27.406  1.00 31.00  ? 42  ILE C N   1 
ATOM   1721 C CA  . ILE C 1 43 ? 19.006  -32.038 26.201  1.00 28.47  ? 42  ILE C CA  1 
ATOM   1722 C C   . ILE C 1 43 ? 17.556  -32.307 25.821  1.00 27.84  ? 42  ILE C C   1 
ATOM   1723 O O   . ILE C 1 43 ? 17.048  -33.437 25.879  1.00 32.13  ? 42  ILE C O   1 
ATOM   1724 C CB  . ILE C 1 43 ? 19.987  -32.418 25.072  1.00 28.16  ? 42  ILE C CB  1 
ATOM   1725 C CG1 . ILE C 1 43 ? 21.442  -32.223 25.527  1.00 28.12  ? 42  ILE C CG1 1 
ATOM   1726 C CG2 . ILE C 1 43 ? 19.667  -31.682 23.764  1.00 31.91  ? 42  ILE C CG2 1 
ATOM   1727 C CD1 . ILE C 1 43 ? 21.815  -30.780 25.833  1.00 27.94  ? 42  ILE C CD1 1 
ATOM   1728 N N   . PHE C 1 44 ? 16.874  -31.239 25.368  1.00 29.83  ? 43  PHE C N   1 
ATOM   1729 C CA  . PHE C 1 44 ? 15.604  -31.422 24.696  1.00 28.75  ? 43  PHE C CA  1 
ATOM   1730 C C   . PHE C 1 44 ? 15.760  -30.947 23.248  1.00 28.06  ? 43  PHE C C   1 
ATOM   1731 O O   . PHE C 1 44 ? 16.306  -29.861 23.006  1.00 29.66  ? 43  PHE C O   1 
ATOM   1732 C CB  . PHE C 1 44 ? 14.615  -30.499 25.420  1.00 34.56  ? 43  PHE C CB  1 
ATOM   1733 C CG  . PHE C 1 44 ? 13.234  -30.394 24.779  1.00 33.82  ? 43  PHE C CG  1 
ATOM   1734 C CD1 . PHE C 1 44 ? 12.246  -31.349 25.046  1.00 34.77  ? 43  PHE C CD1 1 
ATOM   1735 C CD2 . PHE C 1 44 ? 12.942  -29.351 23.891  1.00 33.14  ? 43  PHE C CD2 1 
ATOM   1736 C CE1 . PHE C 1 44 ? 10.987  -31.266 24.454  1.00 38.12  ? 43  PHE C CE1 1 
ATOM   1737 C CE2 . PHE C 1 44 ? 11.683  -29.274 23.287  1.00 34.53  ? 43  PHE C CE2 1 
ATOM   1738 C CZ  . PHE C 1 44 ? 10.710  -30.217 23.592  1.00 39.80  ? 43  PHE C CZ  1 
ATOM   1739 N N   . PHE C 1 45 ? 15.224  -31.744 22.318  1.00 29.47  ? 44  PHE C N   1 
ATOM   1740 C CA  . PHE C 1 45 ? 15.440  -31.515 20.901  1.00 30.94  ? 44  PHE C CA  1 
ATOM   1741 C C   . PHE C 1 45 ? 14.174  -30.889 20.333  1.00 30.49  ? 44  PHE C C   1 
ATOM   1742 O O   . PHE C 1 45 ? 13.091  -31.452 20.482  1.00 34.44  ? 44  PHE C O   1 
ATOM   1743 C CB  . PHE C 1 45 ? 15.780  -32.812 20.162  1.00 29.42  ? 44  PHE C CB  1 
ATOM   1744 C CG  . PHE C 1 45 ? 17.146  -33.373 20.518  1.00 27.47  ? 44  PHE C CG  1 
ATOM   1745 C CD1 . PHE C 1 45 ? 18.276  -33.000 19.786  1.00 25.27  ? 44  PHE C CD1 1 
ATOM   1746 C CD2 . PHE C 1 45 ? 17.288  -34.315 21.541  1.00 28.14  ? 44  PHE C CD2 1 
ATOM   1747 C CE1 . PHE C 1 45 ? 19.536  -33.540 20.082  1.00 30.66  ? 44  PHE C CE1 1 
ATOM   1748 C CE2 . PHE C 1 45 ? 18.538  -34.848 21.846  1.00 29.58  ? 44  PHE C CE2 1 
ATOM   1749 C CZ  . PHE C 1 45 ? 19.661  -34.455 21.118  1.00 29.46  ? 44  PHE C CZ  1 
ATOM   1750 N N   . PHE C 1 46 ? 14.321  -29.704 19.714  1.00 30.58  ? 45  PHE C N   1 
ATOM   1751 C CA  . PHE C 1 46 ? 13.160  -29.101 19.067  1.00 26.30  ? 45  PHE C CA  1 
ATOM   1752 C C   . PHE C 1 46 ? 12.684  -29.938 17.887  1.00 30.25  ? 45  PHE C C   1 
ATOM   1753 O O   . PHE C 1 46 ? 13.459  -30.689 17.271  1.00 29.76  ? 45  PHE C O   1 
ATOM   1754 C CB  . PHE C 1 46 ? 13.413  -27.646 18.665  1.00 28.95  ? 45  PHE C CB  1 
ATOM   1755 C CG  . PHE C 1 46 ? 13.709  -26.680 19.797  1.00 28.98  ? 45  PHE C CG  1 
ATOM   1756 C CD1 . PHE C 1 46 ? 12.684  -26.205 20.618  1.00 29.82  ? 45  PHE C CD1 1 
ATOM   1757 C CD2 . PHE C 1 46 ? 15.015  -26.225 20.005  1.00 26.64  ? 45  PHE C CD2 1 
ATOM   1758 C CE1 . PHE C 1 46 ? 12.988  -25.298 21.651  1.00 32.11  ? 45  PHE C CE1 1 
ATOM   1759 C CE2 . PHE C 1 46 ? 15.302  -25.323 21.020  1.00 32.69  ? 45  PHE C CE2 1 
ATOM   1760 C CZ  . PHE C 1 46 ? 14.299  -24.864 21.845  1.00 31.41  ? 45  PHE C CZ  1 
ATOM   1761 N N   . GLY C 1 47 ? 11.401  -29.766 17.537  1.00 27.54  ? 46  GLY C N   1 
ATOM   1762 C CA  . GLY C 1 47 ? 10.841  -30.491 16.414  1.00 31.83  ? 46  GLY C CA  1 
ATOM   1763 C C   . GLY C 1 47 ? 10.414  -31.904 16.809  1.00 34.19  ? 46  GLY C C   1 
ATOM   1764 O O   . GLY C 1 47 ? 9.231   -32.235 16.755  1.00 38.22  ? 46  GLY C O   1 
ATOM   1765 N N   . THR C 1 48 ? 11.384  -32.767 17.148  1.00 31.68  ? 47  THR C N   1 
ATOM   1766 C CA  . THR C 1 48 ? 11.026  -34.117 17.574  1.00 34.23  ? 47  THR C CA  1 
ATOM   1767 C C   . THR C 1 48 ? 10.531  -34.108 19.021  1.00 31.77  ? 47  THR C C   1 
ATOM   1768 O O   . THR C 1 48 ? 9.812   -35.022 19.414  1.00 36.81  ? 47  THR C O   1 
ATOM   1769 C CB  . THR C 1 48 ? 12.207  -35.073 17.444  1.00 32.69  ? 47  THR C CB  1 
ATOM   1770 O OG1 . THR C 1 48 ? 13.075  -34.489 18.418  1.00 34.59  ? 47  THR C OG1 1 
ATOM   1771 C CG2 . THR C 1 48 ? 12.769  -35.171 16.034  1.00 29.28  ? 47  THR C CG2 1 
ATOM   1772 N N   . HIS C 1 49 ? 10.959  -33.129 19.823  1.00 31.87  ? 48  HIS C N   1 
ATOM   1773 C CA  . HIS C 1 49 ? 10.611  -33.053 21.239  1.00 36.68  ? 48  HIS C CA  1 
ATOM   1774 C C   . HIS C 1 49 ? 11.079  -34.283 22.027  1.00 34.09  ? 48  HIS C C   1 
ATOM   1775 O O   . HIS C 1 49 ? 10.437  -34.645 23.015  1.00 42.18  ? 48  HIS C O   1 
ATOM   1776 C CB  . HIS C 1 49 ? 9.103   -32.828 21.426  1.00 33.74  ? 48  HIS C CB  1 
ATOM   1777 C CG  . HIS C 1 49 ? 8.555   -31.717 20.594  1.00 39.23  ? 48  HIS C CG  1 
ATOM   1778 N ND1 . HIS C 1 49 ? 7.377   -31.847 19.884  1.00 42.94  ? 48  HIS C ND1 1 
ATOM   1779 C CD2 . HIS C 1 49 ? 9.038   -30.509 20.307  1.00 39.92  ? 48  HIS C CD2 1 
ATOM   1780 C CE1 . HIS C 1 49 ? 7.169   -30.739 19.189  1.00 46.61  ? 48  HIS C CE1 1 
ATOM   1781 N NE2 . HIS C 1 49 ? 8.166   -29.913 19.429  1.00 42.93  ? 48  HIS C NE2 1 
ATOM   1782 N N   . GLU C 1 50 ? 12.205  -34.888 21.620  1.00 34.79  ? 49  GLU C N   1 
ATOM   1783 C CA  . GLU C 1 50 ? 12.799  -36.000 22.348  1.00 34.84  ? 49  GLU C CA  1 
ATOM   1784 C C   . GLU C 1 50 ? 13.893  -35.479 23.279  1.00 33.64  ? 49  GLU C C   1 
ATOM   1785 O O   . GLU C 1 50 ? 14.215  -34.294 23.279  1.00 32.27  ? 49  GLU C O   1 
ATOM   1786 C CB  . GLU C 1 50 ? 13.325  -37.055 21.386  1.00 39.82  ? 49  GLU C CB  1 
ATOM   1787 C CG  . GLU C 1 50 ? 12.214  -37.748 20.598  1.00 49.88  ? 49  GLU C CG  1 
ATOM   1788 C CD  . GLU C 1 50 ? 12.920  -38.531 19.513  1.00 57.80  ? 49  GLU C CD  1 
ATOM   1789 O OE1 . GLU C 1 50 ? 14.169  -38.616 19.606  1.00 60.92  ? 49  GLU C OE1 1 
ATOM   1790 O OE2 . GLU C 1 50 ? 12.257  -39.015 18.572  1.00 63.69  ? 49  GLU C OE2 1 
ATOM   1791 N N   . THR C 1 51 ? 14.404  -36.376 24.132  1.00 36.79  ? 50  THR C N   1 
ATOM   1792 C CA  . THR C 1 51 ? 15.380  -36.009 25.159  1.00 34.13  ? 50  THR C CA  1 
ATOM   1793 C C   . THR C 1 51 ? 16.522  -37.016 25.098  1.00 30.98  ? 50  THR C C   1 
ATOM   1794 O O   . THR C 1 51 ? 16.355  -38.127 24.611  1.00 34.48  ? 50  THR C O   1 
ATOM   1795 C CB  . THR C 1 51 ? 14.767  -35.975 26.562  1.00 38.51  ? 50  THR C CB  1 
ATOM   1796 O OG1 . THR C 1 51 ? 14.280  -37.300 26.768  1.00 37.77  ? 50  THR C OG1 1 
ATOM   1797 C CG2 . THR C 1 51 ? 13.665  -34.940 26.724  1.00 40.46  ? 50  THR C CG2 1 
ATOM   1798 N N   . ALA C 1 52 ? 17.712  -36.557 25.491  1.00 31.32  ? 51  ALA C N   1 
ATOM   1799 C CA  . ALA C 1 52 ? 18.910  -37.368 25.607  1.00 34.77  ? 51  ALA C CA  1 
ATOM   1800 C C   . ALA C 1 52 ? 19.864  -36.665 26.565  1.00 36.40  ? 51  ALA C C   1 
ATOM   1801 O O   . ALA C 1 52 ? 19.602  -35.541 26.989  1.00 36.57  ? 51  ALA C O   1 
ATOM   1802 C CB  . ALA C 1 52 ? 19.563  -37.594 24.265  1.00 31.08  ? 51  ALA C CB  1 
ATOM   1803 N N   . PHE C 1 53 ? 20.970  -37.343 26.910  1.00 36.91  ? 52  PHE C N   1 
ATOM   1804 C CA  . PHE C 1 53 ? 22.038  -36.772 27.718  1.00 35.45  ? 52  PHE C CA  1 
ATOM   1805 C C   . PHE C 1 53 ? 23.249  -36.627 26.812  1.00 32.74  ? 52  PHE C C   1 
ATOM   1806 O O   . PHE C 1 53 ? 23.651  -37.593 26.175  1.00 34.84  ? 52  PHE C O   1 
ATOM   1807 C CB  . PHE C 1 53 ? 22.394  -37.770 28.836  1.00 35.47  ? 52  PHE C CB  1 
ATOM   1808 C CG  . PHE C 1 53 ? 21.417  -37.702 29.998  1.00 34.81  ? 52  PHE C CG  1 
ATOM   1809 C CD1 . PHE C 1 53 ? 21.137  -36.495 30.630  1.00 37.94  ? 52  PHE C CD1 1 
ATOM   1810 C CD2 . PHE C 1 53 ? 20.744  -38.843 30.430  1.00 48.30  ? 52  PHE C CD2 1 
ATOM   1811 C CE1 . PHE C 1 53 ? 20.219  -36.432 31.678  1.00 42.79  ? 52  PHE C CE1 1 
ATOM   1812 C CE2 . PHE C 1 53 ? 19.828  -38.773 31.481  1.00 49.44  ? 52  PHE C CE2 1 
ATOM   1813 C CZ  . PHE C 1 53 ? 19.557  -37.562 32.089  1.00 43.53  ? 52  PHE C CZ  1 
ATOM   1814 N N   . LEU C 1 54 ? 23.859  -35.440 26.780  1.00 29.04  ? 53  LEU C N   1 
ATOM   1815 C CA  . LEU C 1 54 ? 25.027  -35.230 25.930  1.00 27.88  ? 53  LEU C CA  1 
ATOM   1816 C C   . LEU C 1 54 ? 26.101  -34.467 26.695  1.00 29.10  ? 53  LEU C C   1 
ATOM   1817 O O   . LEU C 1 54 ? 25.782  -33.712 27.597  1.00 31.04  ? 53  LEU C O   1 
ATOM   1818 C CB  . LEU C 1 54 ? 24.681  -34.487 24.635  1.00 31.47  ? 53  LEU C CB  1 
ATOM   1819 C CG  . LEU C 1 54 ? 23.775  -35.213 23.634  1.00 39.17  ? 53  LEU C CG  1 
ATOM   1820 C CD1 . LEU C 1 54 ? 23.391  -34.249 22.526  1.00 35.62  ? 53  LEU C CD1 1 
ATOM   1821 C CD2 . LEU C 1 54 ? 24.447  -36.456 23.027  1.00 42.01  ? 53  LEU C CD2 1 
ATOM   1822 N N   . GLY C 1 55 ? 27.358  -34.675 26.298  1.00 31.85  ? 54  GLY C N   1 
ATOM   1823 C CA  . GLY C 1 55 ? 28.490  -33.967 26.871  1.00 33.26  ? 54  GLY C CA  1 
ATOM   1824 C C   . GLY C 1 55 ? 28.765  -32.644 26.156  1.00 38.28  ? 54  GLY C C   1 
ATOM   1825 O O   . GLY C 1 55 ? 28.287  -32.379 25.043  1.00 34.97  ? 54  GLY C O   1 
ATOM   1826 N N   . PRO C 1 56 ? 29.531  -31.734 26.796  1.00 38.88  ? 55  PRO C N   1 
ATOM   1827 C CA  . PRO C 1 56 ? 29.673  -30.368 26.297  1.00 41.87  ? 55  PRO C CA  1 
ATOM   1828 C C   . PRO C 1 56 ? 30.246  -30.270 24.887  1.00 41.55  ? 55  PRO C C   1 
ATOM   1829 O O   . PRO C 1 56 ? 29.936  -29.336 24.147  1.00 50.84  ? 55  PRO C O   1 
ATOM   1830 C CB  . PRO C 1 56 ? 30.553  -29.645 27.365  1.00 44.24  ? 55  PRO C CB  1 
ATOM   1831 C CG  . PRO C 1 56 ? 31.196  -30.772 28.148  1.00 41.05  ? 55  PRO C CG  1 
ATOM   1832 C CD  . PRO C 1 56 ? 30.259  -31.962 28.058  1.00 41.56  ? 55  PRO C CD  1 
ATOM   1833 N N   . LYS C 1 57 ? 31.054  -31.268 24.526  1.00 40.39  ? 56  LYS C N   1 
ATOM   1834 C CA  . LYS C 1 57 ? 31.726  -31.317 23.237  1.00 42.67  ? 56  LYS C CA  1 
ATOM   1835 C C   . LYS C 1 57 ? 30.689  -31.467 22.128  1.00 45.12  ? 56  LYS C C   1 
ATOM   1836 O O   . LYS C 1 57 ? 30.973  -31.158 20.966  1.00 40.35  ? 56  LYS C O   1 
ATOM   1837 C CB  . LYS C 1 57 ? 32.537  -32.614 23.138  1.00 41.80  ? 56  LYS C CB  1 
ATOM   1838 N N   . ASP C 1 58 ? 29.513  -31.985 22.508  1.00 38.42  ? 57  ASP C N   1 
ATOM   1839 C CA  . ASP C 1 58 ? 28.460  -32.276 21.537  1.00 39.91  ? 57  ASP C CA  1 
ATOM   1840 C C   . ASP C 1 58 ? 27.514  -31.096 21.363  1.00 37.59  ? 57  ASP C C   1 
ATOM   1841 O O   . ASP C 1 58 ? 26.507  -31.211 20.648  1.00 35.00  ? 57  ASP C O   1 
ATOM   1842 C CB  . ASP C 1 58 ? 27.655  -33.494 21.952  1.00 41.60  ? 57  ASP C CB  1 
ATOM   1843 C CG  . ASP C 1 58 ? 28.436  -34.794 21.959  1.00 45.69  ? 57  ASP C CG  1 
ATOM   1844 O OD1 . ASP C 1 58 ? 29.427  -34.858 21.222  1.00 42.09  ? 57  ASP C OD1 1 
ATOM   1845 O OD2 . ASP C 1 58 ? 28.049  -35.711 22.711  1.00 49.49  ? 57  ASP C OD2 1 
ATOM   1846 N N   . LEU C 1 59 ? 27.807  -29.973 22.032  1.00 33.41  ? 58  LEU C N   1 
ATOM   1847 C CA  . LEU C 1 59 ? 26.855  -28.877 22.130  1.00 34.68  ? 58  LEU C CA  1 
ATOM   1848 C C   . LEU C 1 59 ? 27.478  -27.577 21.619  1.00 38.85  ? 58  LEU C C   1 
ATOM   1849 O O   . LEU C 1 59 ? 28.649  -27.322 21.911  1.00 43.87  ? 58  LEU C O   1 
ATOM   1850 C CB  . LEU C 1 59 ? 26.429  -28.696 23.587  1.00 32.78  ? 58  LEU C CB  1 
ATOM   1851 C CG  . LEU C 1 59 ? 25.913  -29.946 24.306  1.00 30.87  ? 58  LEU C CG  1 
ATOM   1852 C CD1 . LEU C 1 59 ? 25.588  -29.645 25.755  1.00 33.02  ? 58  LEU C CD1 1 
ATOM   1853 C CD2 . LEU C 1 59 ? 24.624  -30.399 23.589  1.00 28.64  ? 58  LEU C CD2 1 
ATOM   1854 N N   . PHE C 1 60 ? 26.670  -26.759 20.920  1.00 37.84  ? 59  PHE C N   1 
ATOM   1855 C CA  . PHE C 1 60 ? 27.127  -25.531 20.264  1.00 39.74  ? 59  PHE C CA  1 
ATOM   1856 C C   . PHE C 1 60 ? 26.138  -24.405 20.556  1.00 40.07  ? 59  PHE C C   1 
ATOM   1857 O O   . PHE C 1 60 ? 24.958  -24.520 20.242  1.00 39.43  ? 59  PHE C O   1 
ATOM   1858 C CB  . PHE C 1 60 ? 27.318  -25.771 18.756  1.00 38.74  ? 59  PHE C CB  1 
ATOM   1859 C CG  . PHE C 1 60 ? 28.284  -26.906 18.435  1.00 36.24  ? 59  PHE C CG  1 
ATOM   1860 C CD1 . PHE C 1 60 ? 27.865  -28.233 18.448  1.00 36.02  ? 59  PHE C CD1 1 
ATOM   1861 C CD2 . PHE C 1 60 ? 29.630  -26.653 18.165  1.00 44.90  ? 59  PHE C CD2 1 
ATOM   1862 C CE1 . PHE C 1 60 ? 28.747  -29.275 18.217  1.00 36.22  ? 59  PHE C CE1 1 
ATOM   1863 C CE2 . PHE C 1 60 ? 30.516  -27.696 17.906  1.00 43.08  ? 59  PHE C CE2 1 
ATOM   1864 C CZ  . PHE C 1 60 ? 30.076  -29.006 17.925  1.00 47.03  ? 59  PHE C CZ  1 
ATOM   1865 N N   . PRO C 1 61 ? 26.539  -23.262 21.174  1.00 40.93  ? 60  PRO C N   1 
ATOM   1866 C CA  . PRO C 1 61 ? 25.571  -22.198 21.464  1.00 41.72  ? 60  PRO C CA  1 
ATOM   1867 C C   . PRO C 1 61 ? 24.925  -21.711 20.170  1.00 37.12  ? 60  PRO C C   1 
ATOM   1868 O O   . PRO C 1 61 ? 25.583  -21.640 19.136  1.00 41.26  ? 60  PRO C O   1 
ATOM   1869 C CB  . PRO C 1 61 ? 26.335  -21.072 22.225  1.00 44.30  ? 60  PRO C CB  1 
ATOM   1870 C CG  . PRO C 1 61 ? 27.763  -21.585 22.321  1.00 41.93  ? 60  PRO C CG  1 
ATOM   1871 C CD  . PRO C 1 61 ? 27.912  -22.918 21.587  1.00 48.23  ? 60  PRO C CD  1 
ATOM   1872 N N   . TYR C 1 62 ? 23.614  -21.429 20.266  1.00 45.14  ? 61  TYR C N   1 
ATOM   1873 C CA  . TYR C 1 62 ? 22.706  -21.253 19.144  1.00 43.17  ? 61  TYR C CA  1 
ATOM   1874 C C   . TYR C 1 62 ? 23.048  -19.996 18.350  1.00 52.25  ? 61  TYR C C   1 
ATOM   1875 O O   . TYR C 1 62 ? 23.152  -20.054 17.124  1.00 52.92  ? 61  TYR C O   1 
ATOM   1876 C CB  . TYR C 1 62 ? 21.253  -21.160 19.607  1.00 42.81  ? 61  TYR C CB  1 
ATOM   1877 C CG  . TYR C 1 62 ? 20.294  -20.772 18.491  1.00 42.72  ? 61  TYR C CG  1 
ATOM   1878 C CD1 . TYR C 1 62 ? 20.086  -21.618 17.397  1.00 43.13  ? 61  TYR C CD1 1 
ATOM   1879 C CD2 . TYR C 1 62 ? 19.560  -19.588 18.562  1.00 44.08  ? 61  TYR C CD2 1 
ATOM   1880 C CE1 . TYR C 1 62 ? 19.194  -21.275 16.385  1.00 43.67  ? 61  TYR C CE1 1 
ATOM   1881 C CE2 . TYR C 1 62 ? 18.664  -19.241 17.560  1.00 47.52  ? 61  TYR C CE2 1 
ATOM   1882 C CZ  . TYR C 1 62 ? 18.493  -20.078 16.466  1.00 43.91  ? 61  TYR C CZ  1 
ATOM   1883 O OH  . TYR C 1 62 ? 17.616  -19.707 15.485  1.00 45.28  ? 61  TYR C OH  1 
ATOM   1884 N N   . ASP C 1 63 ? 23.225  -18.872 19.056  1.00 50.52  ? 62  ASP C N   1 
ATOM   1885 C CA  . ASP C 1 63 ? 23.506  -17.619 18.373  1.00 55.22  ? 62  ASP C CA  1 
ATOM   1886 C C   . ASP C 1 63 ? 24.854  -17.695 17.668  1.00 52.64  ? 62  ASP C C   1 
ATOM   1887 O O   . ASP C 1 63 ? 25.017  -17.138 16.585  1.00 59.22  ? 62  ASP C O   1 
ATOM   1888 C CB  . ASP C 1 63 ? 23.262  -16.408 19.257  1.00 59.37  ? 62  ASP C CB  1 
ATOM   1889 C CG  . ASP C 1 63 ? 21.860  -15.835 19.104  1.00 74.64  ? 62  ASP C CG  1 
ATOM   1890 O OD1 . ASP C 1 63 ? 21.012  -16.120 19.977  1.00 68.71  ? 62  ASP C OD1 1 
ATOM   1891 O OD2 . ASP C 1 63 ? 21.623  -15.124 18.095  1.00 81.03  ? 62  ASP C OD2 1 
ATOM   1892 N N   . LYS C 1 64 ? 25.788  -18.429 18.270  1.00 43.73  ? 63  LYS C N   1 
ATOM   1893 C CA  . LYS C 1 64 ? 27.148  -18.481 17.769  1.00 44.58  ? 63  LYS C CA  1 
ATOM   1894 C C   . LYS C 1 64 ? 27.237  -19.384 16.541  1.00 45.55  ? 63  LYS C C   1 
ATOM   1895 O O   . LYS C 1 64 ? 28.096  -19.167 15.693  1.00 38.95  ? 63  LYS C O   1 
ATOM   1896 C CB  . LYS C 1 64 ? 28.128  -18.944 18.855  1.00 48.68  ? 63  LYS C CB  1 
ATOM   1897 N N   . SER C 1 65 ? 26.340  -20.385 16.413  1.00 38.74  ? 64  SER C N   1 
ATOM   1898 C CA  . SER C 1 65 ? 26.603  -21.374 15.376  1.00 36.38  ? 64  SER C CA  1 
ATOM   1899 C C   . SER C 1 65 ? 25.446  -21.508 14.376  1.00 33.86  ? 64  SER C C   1 
ATOM   1900 O O   . SER C 1 65 ? 25.535  -22.293 13.438  1.00 37.67  ? 64  SER C O   1 
ATOM   1901 C CB  . SER C 1 65 ? 27.008  -22.718 15.963  1.00 41.96  ? 64  SER C CB  1 
ATOM   1902 O OG  . SER C 1 65 ? 25.913  -23.242 16.704  1.00 40.22  ? 64  SER C OG  1 
ATOM   1903 N N   . LYS C 1 66 ? 24.372  -20.744 14.564  1.00 34.38  ? 65  LYS C N   1 
ATOM   1904 C CA  . LYS C 1 66 ? 23.235  -20.894 13.662  1.00 35.61  ? 65  LYS C CA  1 
ATOM   1905 C C   . LYS C 1 66 ? 23.613  -20.596 12.207  1.00 40.14  ? 65  LYS C C   1 
ATOM   1906 O O   . LYS C 1 66 ? 23.074  -21.227 11.303  1.00 39.22  ? 65  LYS C O   1 
ATOM   1907 C CB  . LYS C 1 66 ? 22.012  -20.069 14.056  1.00 39.12  ? 65  LYS C CB  1 
ATOM   1908 C CG  . LYS C 1 66 ? 22.269  -18.576 14.008  1.00 38.44  ? 65  LYS C CG  1 
ATOM   1909 C CD  . LYS C 1 66 ? 20.938  -17.869 14.210  1.00 48.51  ? 65  LYS C CD  1 
ATOM   1910 C CE  . LYS C 1 66 ? 21.181  -16.436 14.551  1.00 47.93  ? 65  LYS C CE  1 
ATOM   1911 N NZ  . LYS C 1 66 ? 19.987  -15.942 15.219  1.00 48.04  ? 65  LYS C NZ  1 
ATOM   1912 N N   . ASP C 1 67 ? 24.542  -19.655 11.958  1.00 38.07  ? 66  ASP C N   1 
ATOM   1913 C CA  . ASP C 1 67 ? 24.921  -19.378 10.569  1.00 40.57  ? 66  ASP C CA  1 
ATOM   1914 C C   . ASP C 1 67 ? 25.329  -20.670 9.848   1.00 40.09  ? 66  ASP C C   1 
ATOM   1915 O O   . ASP C 1 67 ? 25.010  -20.863 8.677   1.00 39.91  ? 66  ASP C O   1 
ATOM   1916 C CB  . ASP C 1 67 ? 25.831  -18.152 10.430  1.00 40.93  ? 66  ASP C CB  1 
ATOM   1917 C CG  . ASP C 1 67 ? 27.223  -18.224 11.052  1.00 58.64  ? 66  ASP C CG  1 
ATOM   1918 O OD1 . ASP C 1 67 ? 27.548  -19.267 11.687  1.00 58.18  ? 66  ASP C OD1 1 
ATOM   1919 O OD2 . ASP C 1 67 ? 27.980  -17.223 10.911  1.00 55.19  ? 66  ASP C OD2 1 
ATOM   1920 N N   . LYS C 1 68 ? 25.969  -21.598 10.580  1.00 35.88  ? 67  LYS C N   1 
ATOM   1921 C CA  . LYS C 1 68 ? 26.494  -22.835 10.024  1.00 35.23  ? 67  LYS C CA  1 
ATOM   1922 C C   . LYS C 1 68 ? 25.508  -24.013 10.149  1.00 33.63  ? 67  LYS C C   1 
ATOM   1923 O O   . LYS C 1 68 ? 25.365  -24.814 9.220   1.00 37.29  ? 67  LYS C O   1 
ATOM   1924 C CB  . LYS C 1 68 ? 27.809  -23.071 10.770  1.00 33.41  ? 67  LYS C CB  1 
ATOM   1925 C CG  . LYS C 1 68 ? 28.546  -24.349 10.514  1.00 40.67  ? 67  LYS C CG  1 
ATOM   1926 C CD  . LYS C 1 68 ? 29.762  -24.318 11.444  1.00 47.72  ? 67  LYS C CD  1 
ATOM   1927 C CE  . LYS C 1 68 ? 30.521  -25.596 11.554  1.00 57.24  ? 67  LYS C CE  1 
ATOM   1928 N NZ  . LYS C 1 68 ? 31.056  -26.067 10.273  1.00 72.77  ? 67  LYS C NZ  1 
ATOM   1929 N N   . TYR C 1 69 ? 24.812  -24.130 11.292  1.00 31.79  ? 68  TYR C N   1 
ATOM   1930 C CA  . TYR C 1 69 ? 23.976  -25.316 11.477  1.00 29.82  ? 68  TYR C CA  1 
ATOM   1931 C C   . TYR C 1 69 ? 22.494  -25.007 11.265  1.00 32.58  ? 68  TYR C C   1 
ATOM   1932 O O   . TYR C 1 69 ? 21.693  -25.929 11.106  1.00 31.71  ? 68  TYR C O   1 
ATOM   1933 C CB  . TYR C 1 69 ? 24.136  -25.950 12.870  1.00 29.93  ? 68  TYR C CB  1 
ATOM   1934 C CG  . TYR C 1 69 ? 25.556  -26.398 13.163  1.00 30.14  ? 68  TYR C CG  1 
ATOM   1935 C CD1 . TYR C 1 69 ? 26.271  -27.186 12.269  1.00 34.25  ? 68  TYR C CD1 1 
ATOM   1936 C CD2 . TYR C 1 69 ? 26.184  -26.000 14.339  1.00 35.66  ? 68  TYR C CD2 1 
ATOM   1937 C CE1 . TYR C 1 69 ? 27.556  -27.623 12.558  1.00 33.42  ? 68  TYR C CE1 1 
ATOM   1938 C CE2 . TYR C 1 69 ? 27.471  -26.422 14.633  1.00 36.26  ? 68  TYR C CE2 1 
ATOM   1939 C CZ  . TYR C 1 69 ? 28.160  -27.214 13.733  1.00 36.28  ? 68  TYR C CZ  1 
ATOM   1940 O OH  . TYR C 1 69 ? 29.439  -27.594 14.061  1.00 40.51  ? 68  TYR C OH  1 
ATOM   1941 N N   . GLY C 1 70 ? 22.111  -23.723 11.295  1.00 28.40  ? 69  GLY C N   1 
ATOM   1942 C CA  . GLY C 1 70 ? 20.692  -23.421 11.180  1.00 28.36  ? 69  GLY C CA  1 
ATOM   1943 C C   . GLY C 1 70 ? 20.308  -23.279 9.718   1.00 32.20  ? 69  GLY C C   1 
ATOM   1944 O O   . GLY C 1 70 ? 20.226  -22.171 9.202   1.00 32.55  ? 69  GLY C O   1 
ATOM   1945 N N   . LYS C 1 71 ? 20.214  -24.420 9.039   1.00 29.97  ? 70  LYS C N   1 
ATOM   1946 C CA  . LYS C 1 71 ? 19.791  -24.448 7.645   1.00 33.44  ? 70  LYS C CA  1 
ATOM   1947 C C   . LYS C 1 71 ? 18.928  -25.682 7.498   1.00 32.06  ? 70  LYS C C   1 
ATOM   1948 O O   . LYS C 1 71 ? 19.113  -26.649 8.236   1.00 35.19  ? 70  LYS C O   1 
ATOM   1949 C CB  . LYS C 1 71 ? 20.975  -24.593 6.684   1.00 32.65  ? 70  LYS C CB  1 
ATOM   1950 C CG  . LYS C 1 71 ? 22.010  -25.579 7.178   1.00 33.25  ? 70  LYS C CG  1 
ATOM   1951 C CD  . LYS C 1 71 ? 23.227  -26.043 6.377   1.00 41.09  ? 70  LYS C CD  1 
ATOM   1952 C CE  . LYS C 1 71 ? 23.997  -27.034 7.221   1.00 42.76  ? 70  LYS C CE  1 
ATOM   1953 N N   . PRO C 1 72 ? 17.928  -25.683 6.594   1.00 28.36  ? 71  PRO C N   1 
ATOM   1954 C CA  . PRO C 1 72 ? 17.010  -26.810 6.526   1.00 26.34  ? 71  PRO C CA  1 
ATOM   1955 C C   . PRO C 1 72 ? 17.692  -28.127 6.195   1.00 29.22  ? 71  PRO C C   1 
ATOM   1956 O O   . PRO C 1 72 ? 18.727  -28.171 5.519   1.00 31.90  ? 71  PRO C O   1 
ATOM   1957 C CB  . PRO C 1 72 ? 16.014  -26.428 5.434   1.00 26.03  ? 71  PRO C CB  1 
ATOM   1958 C CG  . PRO C 1 72 ? 16.105  -24.914 5.440   1.00 28.02  ? 71  PRO C CG  1 
ATOM   1959 C CD  . PRO C 1 72 ? 17.567  -24.566 5.695   1.00 28.05  ? 71  PRO C CD  1 
ATOM   1960 N N   . ASN C 1 73 ? 17.007  -29.179 6.612   1.00 31.64  ? 72  ASN C N   1 
ATOM   1961 C CA  . ASN C 1 73 ? 17.292  -30.475 6.033   1.00 37.85  ? 72  ASN C CA  1 
ATOM   1962 C C   . ASN C 1 73 ? 16.069  -31.375 6.171   1.00 30.91  ? 72  ASN C C   1 
ATOM   1963 O O   . ASN C 1 73 ? 15.093  -31.055 6.847   1.00 30.57  ? 72  ASN C O   1 
ATOM   1964 C CB  . ASN C 1 73 ? 18.666  -31.032 6.420   1.00 43.50  ? 72  ASN C CB  1 
ATOM   1965 C CG  . ASN C 1 73 ? 18.650  -31.759 7.739   1.00 42.73  ? 72  ASN C CG  1 
ATOM   1966 O OD1 . ASN C 1 73 ? 18.108  -32.870 7.845   1.00 40.04  ? 72  ASN C OD1 1 
ATOM   1967 N ND2 . ASN C 1 73 ? 19.276  -31.158 8.730   1.00 45.75  ? 72  ASN C ND2 1 
ATOM   1968 N N   . LYS C 1 74 ? 16.182  -32.548 5.556   1.00 32.25  ? 73  LYS C N   1 
ATOM   1969 C CA  . LYS C 1 74 ? 14.978  -33.330 5.294   1.00 29.13  ? 73  LYS C CA  1 
ATOM   1970 C C   . LYS C 1 74 ? 14.702  -34.298 6.437   1.00 31.14  ? 73  LYS C C   1 
ATOM   1971 O O   . LYS C 1 74 ? 13.660  -34.949 6.442   1.00 33.72  ? 73  LYS C O   1 
ATOM   1972 C CB  . LYS C 1 74 ? 15.123  -34.043 3.939   1.00 34.28  ? 73  LYS C CB  1 
ATOM   1973 N N   . ARG C 1 75 ? 15.588  -34.346 7.451   1.00 28.25  ? 74  ARG C N   1 
ATOM   1974 C CA  . ARG C 1 75 ? 15.334  -35.318 8.516   1.00 28.73  ? 74  ARG C CA  1 
ATOM   1975 C C   . ARG C 1 75 ? 14.041  -34.985 9.267   1.00 30.89  ? 74  ARG C C   1 
ATOM   1976 O O   . ARG C 1 75 ? 13.697  -33.813 9.502   1.00 30.36  ? 74  ARG C O   1 
ATOM   1977 C CB  . ARG C 1 75 ? 16.528  -35.431 9.489   1.00 31.69  ? 74  ARG C CB  1 
ATOM   1978 C CG  . ARG C 1 75 ? 17.909  -35.557 8.848   1.00 33.69  ? 74  ARG C CG  1 
ATOM   1979 C CD  . ARG C 1 75 ? 18.315  -36.879 8.182   1.00 42.00  ? 74  ARG C CD  1 
ATOM   1980 N NE  . ARG C 1 75 ? 18.332  -37.910 9.219   1.00 38.16  ? 74  ARG C NE  1 
ATOM   1981 C CZ  . ARG C 1 75 ? 19.453  -38.382 9.782   1.00 34.69  ? 74  ARG C CZ  1 
ATOM   1982 N NH1 . ARG C 1 75 ? 19.360  -39.034 10.907  1.00 36.60  ? 74  ARG C NH1 1 
ATOM   1983 N NH2 . ARG C 1 75 ? 20.631  -38.097 9.255   1.00 33.06  ? 74  ARG C NH2 1 
ATOM   1984 N N   . LYS C 1 76 ? 13.332  -36.049 9.661   1.00 32.96  ? 75  LYS C N   1 
ATOM   1985 C CA  . LYS C 1 76 ? 12.052  -35.963 10.349  1.00 35.96  ? 75  LYS C CA  1 
ATOM   1986 C C   . LYS C 1 76 ? 12.104  -34.999 11.537  1.00 32.52  ? 75  LYS C C   1 
ATOM   1987 O O   . LYS C 1 76 ? 12.861  -35.186 12.511  1.00 30.58  ? 75  LYS C O   1 
ATOM   1988 C CB  . LYS C 1 76 ? 11.475  -37.326 10.761  1.00 34.86  ? 75  LYS C CB  1 
ATOM   1989 C CG  . LYS C 1 76 ? 9.953   -37.319 10.807  1.00 41.82  ? 75  LYS C CG  1 
ATOM   1990 C CD  . LYS C 1 76 ? 9.321   -38.407 11.673  1.00 52.03  ? 75  LYS C CD  1 
ATOM   1991 N N   . GLY C 1 77 ? 11.274  -33.956 11.447  1.00 33.53  ? 76  GLY C N   1 
ATOM   1992 C CA  . GLY C 1 77 ? 11.056  -33.056 12.574  1.00 29.55  ? 76  GLY C CA  1 
ATOM   1993 C C   . GLY C 1 77 ? 12.043  -31.882 12.598  1.00 26.40  ? 76  GLY C C   1 
ATOM   1994 O O   . GLY C 1 77 ? 11.866  -30.957 13.377  1.00 32.62  ? 76  GLY C O   1 
ATOM   1995 N N   . PHE C 1 78 ? 13.032  -31.870 11.691  1.00 25.95  ? 77  PHE C N   1 
ATOM   1996 C CA  . PHE C 1 78 ? 14.140  -30.936 11.781  1.00 26.22  ? 77  PHE C CA  1 
ATOM   1997 C C   . PHE C 1 78 ? 13.651  -29.506 11.521  1.00 28.18  ? 77  PHE C C   1 
ATOM   1998 O O   . PHE C 1 78 ? 14.018  -28.561 12.225  1.00 27.28  ? 77  PHE C O   1 
ATOM   1999 C CB  . PHE C 1 78 ? 15.215  -31.300 10.754  1.00 28.42  ? 77  PHE C CB  1 
ATOM   2000 C CG  . PHE C 1 78 ? 16.499  -30.533 11.043  1.00 27.75  ? 77  PHE C CG  1 
ATOM   2001 C CD1 . PHE C 1 78 ? 16.701  -29.249 10.541  1.00 27.75  ? 77  PHE C CD1 1 
ATOM   2002 C CD2 . PHE C 1 78 ? 17.515  -31.097 11.807  1.00 25.52  ? 77  PHE C CD2 1 
ATOM   2003 C CE1 . PHE C 1 78 ? 17.887  -28.566 10.778  1.00 28.13  ? 77  PHE C CE1 1 
ATOM   2004 C CE2 . PHE C 1 78 ? 18.698  -30.398 12.063  1.00 26.76  ? 77  PHE C CE2 1 
ATOM   2005 C CZ  . PHE C 1 78 ? 18.879  -29.127 11.568  1.00 28.86  ? 77  PHE C CZ  1 
ATOM   2006 N N   . ASN C 1 79 ? 12.827  -29.357 10.474  1.00 28.74  ? 78  ASN C N   1 
ATOM   2007 C CA  . ASN C 1 79 ? 12.530  -28.000 10.037  1.00 30.64  ? 78  ASN C CA  1 
ATOM   2008 C C   . ASN C 1 79 ? 11.510  -27.357 10.971  1.00 30.65  ? 78  ASN C C   1 
ATOM   2009 O O   . ASN C 1 79 ? 11.571  -26.146 11.232  1.00 28.69  ? 78  ASN C O   1 
ATOM   2010 C CB  . ASN C 1 79 ? 12.111  -27.929 8.577   1.00 27.60  ? 78  ASN C CB  1 
ATOM   2011 C CG  . ASN C 1 79 ? 13.230  -28.300 7.631   1.00 28.34  ? 78  ASN C CG  1 
ATOM   2012 O OD1 . ASN C 1 79 ? 14.397  -28.017 7.917   1.00 25.23  ? 78  ASN C OD1 1 
ATOM   2013 N ND2 . ASN C 1 79 ? 12.906  -28.958 6.526   1.00 27.66  ? 78  ASN C ND2 1 
ATOM   2014 N N   . GLU C 1 80 ? 10.627  -28.180 11.526  1.00 31.37  ? 79  GLU C N   1 
ATOM   2015 C CA  . GLU C 1 80 ? 9.766   -27.694 12.596  1.00 28.72  ? 79  GLU C CA  1 
ATOM   2016 C C   . GLU C 1 80 ? 10.608  -27.278 13.803  1.00 35.53  ? 79  GLU C C   1 
ATOM   2017 O O   . GLU C 1 80 ? 10.285  -26.291 14.466  1.00 33.72  ? 79  GLU C O   1 
ATOM   2018 C CB  . GLU C 1 80 ? 8.734   -28.767 12.938  1.00 34.50  ? 79  GLU C CB  1 
ATOM   2019 C CG  . GLU C 1 80 ? 7.786   -28.325 14.046  1.00 34.65  ? 79  GLU C CG  1 
ATOM   2020 C CD  . GLU C 1 80 ? 6.538   -29.173 14.143  1.00 44.66  ? 79  GLU C CD  1 
ATOM   2021 O OE1 . GLU C 1 80 ? 6.470   -30.286 13.562  1.00 46.81  ? 79  GLU C OE1 1 
ATOM   2022 O OE2 . GLU C 1 80 ? 5.597   -28.688 14.793  1.00 42.09  ? 79  GLU C OE2 1 
ATOM   2023 N N   . GLY C 1 81 ? 11.681  -28.050 14.091  1.00 31.45  ? 80  GLY C N   1 
ATOM   2024 C CA  . GLY C 1 81 ? 12.615  -27.677 15.149  1.00 28.89  ? 80  GLY C CA  1 
ATOM   2025 C C   . GLY C 1 81 ? 13.273  -26.317 14.904  1.00 30.72  ? 80  GLY C C   1 
ATOM   2026 O O   . GLY C 1 81 ? 13.476  -25.551 15.844  1.00 28.67  ? 80  GLY C O   1 
ATOM   2027 N N   . LEU C 1 82 ? 13.730  -26.084 13.655  1.00 31.65  ? 81  LEU C N   1 
ATOM   2028 C CA  . LEU C 1 82 ? 14.290  -24.790 13.273  1.00 32.33  ? 81  LEU C CA  1 
ATOM   2029 C C   . LEU C 1 82 ? 13.280  -23.683 13.554  1.00 29.64  ? 81  LEU C C   1 
ATOM   2030 O O   . LEU C 1 82 ? 13.674  -22.607 14.016  1.00 31.83  ? 81  LEU C O   1 
ATOM   2031 C CB  . LEU C 1 82 ? 14.772  -24.722 11.824  1.00 31.58  ? 81  LEU C CB  1 
ATOM   2032 C CG  . LEU C 1 82 ? 16.045  -25.500 11.465  1.00 28.80  ? 81  LEU C CG  1 
ATOM   2033 C CD1 . LEU C 1 82 ? 16.332  -25.407 9.980   1.00 26.72  ? 81  LEU C CD1 1 
ATOM   2034 C CD2 . LEU C 1 82 ? 17.289  -25.078 12.216  1.00 25.30  ? 81  LEU C CD2 1 
ATOM   2035 N N   . TRP C 1 83 ? 11.998  -23.939 13.265  1.00 30.06  ? 82  TRP C N   1 
ATOM   2036 C CA  . TRP C 1 83 ? 10.986  -22.913 13.511  1.00 36.26  ? 82  TRP C CA  1 
ATOM   2037 C C   . TRP C 1 83 ? 10.858  -22.659 15.022  1.00 37.71  ? 82  TRP C C   1 
ATOM   2038 O O   . TRP C 1 83 ? 10.821  -21.510 15.455  1.00 37.08  ? 82  TRP C O   1 
ATOM   2039 C CB  . TRP C 1 83 ? 9.625   -23.239 12.865  1.00 37.23  ? 82  TRP C CB  1 
ATOM   2040 C CG  . TRP C 1 83 ? 8.636   -22.102 12.994  1.00 39.51  ? 82  TRP C CG  1 
ATOM   2041 C CD1 . TRP C 1 83 ? 8.445   -21.072 12.111  1.00 42.92  ? 82  TRP C CD1 1 
ATOM   2042 C CD2 . TRP C 1 83 ? 7.726   -21.847 14.096  1.00 40.86  ? 82  TRP C CD2 1 
ATOM   2043 N NE1 . TRP C 1 83 ? 7.479   -20.213 12.569  1.00 36.31  ? 82  TRP C NE1 1 
ATOM   2044 C CE2 . TRP C 1 83 ? 7.018   -20.660 13.777  1.00 39.93  ? 82  TRP C CE2 1 
ATOM   2045 C CE3 . TRP C 1 83 ? 7.441   -22.509 15.301  1.00 38.89  ? 82  TRP C CE3 1 
ATOM   2046 C CZ2 . TRP C 1 83 ? 6.055   -20.126 14.627  1.00 42.98  ? 82  TRP C CZ2 1 
ATOM   2047 C CZ3 . TRP C 1 83 ? 6.484   -21.982 16.146  1.00 44.37  ? 82  TRP C CZ3 1 
ATOM   2048 C CH2 . TRP C 1 83 ? 5.822   -20.795 15.815  1.00 46.20  ? 82  TRP C CH2 1 
ATOM   2049 N N   . GLU C 1 84 ? 10.872  -23.730 15.834  1.00 32.25  ? 83  GLU C N   1 
ATOM   2050 C CA  . GLU C 1 84 ? 10.716  -23.564 17.278  1.00 34.58  ? 83  GLU C CA  1 
ATOM   2051 C C   . GLU C 1 84 ? 11.864  -22.782 17.917  1.00 35.66  ? 83  GLU C C   1 
ATOM   2052 O O   . GLU C 1 84 ? 11.626  -21.925 18.781  1.00 39.70  ? 83  GLU C O   1 
ATOM   2053 C CB  . GLU C 1 84 ? 10.522  -24.914 17.962  1.00 31.01  ? 83  GLU C CB  1 
ATOM   2054 C CG  . GLU C 1 84 ? 9.201   -25.572 17.596  1.00 35.63  ? 83  GLU C CG  1 
ATOM   2055 C CD  . GLU C 1 84 ? 9.153   -26.986 18.108  1.00 39.36  ? 83  GLU C CD  1 
ATOM   2056 O OE1 . GLU C 1 84 ? 10.149  -27.418 18.744  1.00 34.89  ? 83  GLU C OE1 1 
ATOM   2057 O OE2 . GLU C 1 84 ? 8.138   -27.654 17.825  1.00 41.06  ? 83  GLU C OE2 1 
ATOM   2058 N N   . ILE C 1 85 ? 13.113  -23.044 17.497  1.00 33.42  ? 84  ILE C N   1 
ATOM   2059 C CA  . ILE C 1 85 ? 14.273  -22.469 18.169  1.00 35.31  ? 84  ILE C CA  1 
ATOM   2060 C C   . ILE C 1 85 ? 14.370  -20.959 17.908  1.00 35.40  ? 84  ILE C C   1 
ATOM   2061 O O   . ILE C 1 85 ? 14.828  -20.210 18.760  1.00 36.43  ? 84  ILE C O   1 
ATOM   2062 C CB  . ILE C 1 85 ? 15.569  -23.222 17.841  1.00 34.65  ? 84  ILE C CB  1 
ATOM   2063 C CG1 . ILE C 1 85 ? 16.658  -22.880 18.875  1.00 32.87  ? 84  ILE C CG1 1 
ATOM   2064 C CG2 . ILE C 1 85 ? 16.031  -22.991 16.390  1.00 32.14  ? 84  ILE C CG2 1 
ATOM   2065 C CD1 . ILE C 1 85 ? 17.871  -23.797 18.902  1.00 33.15  ? 84  ILE C CD1 1 
ATOM   2066 N N   . GLN C 1 86 ? 13.926  -20.533 16.722  1.00 33.52  ? 85  GLN C N   1 
ATOM   2067 C CA  . GLN C 1 86 ? 13.868  -19.115 16.366  1.00 36.23  ? 85  GLN C CA  1 
ATOM   2068 C C   . GLN C 1 86 ? 12.629  -18.390 16.917  1.00 37.87  ? 85  GLN C C   1 
ATOM   2069 O O   . GLN C 1 86 ? 12.725  -17.211 17.258  1.00 43.05  ? 85  GLN C O   1 
ATOM   2070 C CB  . GLN C 1 86 ? 13.962  -19.017 14.839  1.00 35.56  ? 85  GLN C CB  1 
ATOM   2071 C CG  . GLN C 1 86 ? 14.172  -17.593 14.315  1.00 34.30  ? 85  GLN C CG  1 
ATOM   2072 C CD  . GLN C 1 86 ? 14.568  -17.570 12.848  1.00 34.81  ? 85  GLN C CD  1 
ATOM   2073 O OE1 . GLN C 1 86 ? 14.510  -18.588 12.140  1.00 34.02  ? 85  GLN C OE1 1 
ATOM   2074 N NE2 . GLN C 1 86 ? 15.040  -16.416 12.386  1.00 34.98  ? 85  GLN C NE2 1 
ATOM   2075 N N   . ASN C 1 87 ? 11.484  -19.066 17.009  1.00 40.24  ? 86  ASN C N   1 
ATOM   2076 C CA  . ASN C 1 87 ? 10.195  -18.395 17.131  1.00 45.08  ? 86  ASN C CA  1 
ATOM   2077 C C   . ASN C 1 87 ? 9.426   -18.775 18.399  1.00 50.12  ? 86  ASN C C   1 
ATOM   2078 O O   . ASN C 1 87 ? 8.431   -18.126 18.709  1.00 48.74  ? 86  ASN C O   1 
ATOM   2079 C CB  . ASN C 1 87 ? 9.282   -18.636 15.930  1.00 41.86  ? 86  ASN C CB  1 
ATOM   2080 C CG  . ASN C 1 87 ? 9.879   -18.047 14.676  1.00 44.00  ? 86  ASN C CG  1 
ATOM   2081 O OD1 . ASN C 1 87 ? 9.936   -16.819 14.549  1.00 42.52  ? 86  ASN C OD1 1 
ATOM   2082 N ND2 . ASN C 1 87 ? 10.349  -18.892 13.764  1.00 33.93  ? 86  ASN C ND2 1 
ATOM   2083 N N   . ASN C 1 88 ? 9.831   -19.837 19.107  1.00 49.02  ? 87  ASN C N   1 
ATOM   2084 C CA  . ASN C 1 88 ? 9.082   -20.230 20.299  1.00 46.96  ? 87  ASN C CA  1 
ATOM   2085 C C   . ASN C 1 88 ? 9.959   -21.085 21.212  1.00 42.16  ? 87  ASN C C   1 
ATOM   2086 O O   . ASN C 1 88 ? 9.535   -22.174 21.618  1.00 46.49  ? 87  ASN C O   1 
ATOM   2087 C CB  . ASN C 1 88 ? 7.777   -20.950 19.959  1.00 52.14  ? 87  ASN C CB  1 
ATOM   2088 C CG  . ASN C 1 88 ? 6.782   -20.881 21.098  1.00 55.06  ? 87  ASN C CG  1 
ATOM   2089 O OD1 . ASN C 1 88 ? 7.022   -20.194 22.099  1.00 57.39  ? 87  ASN C OD1 1 
ATOM   2090 N ND2 . ASN C 1 88 ? 5.662   -21.571 20.965  1.00 51.25  ? 87  ASN C ND2 1 
ATOM   2091 N N   . PRO C 1 89 ? 11.198  -20.639 21.522  1.00 38.88  ? 88  PRO C N   1 
ATOM   2092 C CA  . PRO C 1 89 ? 12.200  -21.515 22.137  1.00 40.74  ? 88  PRO C CA  1 
ATOM   2093 C C   . PRO C 1 89 ? 11.953  -21.991 23.564  1.00 46.54  ? 88  PRO C C   1 
ATOM   2094 O O   . PRO C 1 89 ? 12.599  -22.944 24.006  1.00 40.83  ? 88  PRO C O   1 
ATOM   2095 C CB  . PRO C 1 89 ? 13.497  -20.730 22.013  1.00 42.04  ? 88  PRO C CB  1 
ATOM   2096 C CG  . PRO C 1 89 ? 13.023  -19.277 22.022  1.00 44.45  ? 88  PRO C CG  1 
ATOM   2097 C CD  . PRO C 1 89 ? 11.748  -19.310 21.204  1.00 41.63  ? 88  PRO C CD  1 
ATOM   2098 N N   . HIS C 1 90 ? 11.013  -21.334 24.260  1.00 49.25  ? 89  HIS C N   1 
ATOM   2099 C CA  . HIS C 1 90 ? 10.759  -21.651 25.657  1.00 48.92  ? 89  HIS C CA  1 
ATOM   2100 C C   . HIS C 1 90 ? 9.299   -22.037 25.890  1.00 51.97  ? 89  HIS C C   1 
ATOM   2101 O O   . HIS C 1 90 ? 8.831   -22.030 27.025  1.00 61.77  ? 89  HIS C O   1 
ATOM   2102 C CB  . HIS C 1 90 ? 11.288  -20.548 26.577  1.00 40.38  ? 89  HIS C CB  1 
ATOM   2103 C CG  . HIS C 1 90 ? 12.712  -20.141 26.340  1.00 39.38  ? 89  HIS C CG  1 
ATOM   2104 N ND1 . HIS C 1 90 ? 13.066  -18.917 25.807  1.00 45.38  ? 89  HIS C ND1 1 
ATOM   2105 C CD2 . HIS C 1 90 ? 13.873  -20.764 26.620  1.00 41.89  ? 89  HIS C CD2 1 
ATOM   2106 C CE1 . HIS C 1 90 ? 14.396  -18.823 25.729  1.00 43.27  ? 89  HIS C CE1 1 
ATOM   2107 N NE2 . HIS C 1 90 ? 14.912  -19.935 26.232  1.00 46.38  ? 89  HIS C NE2 1 
ATOM   2108 N N   . ALA C 1 91 ? 8.579   -22.408 24.828  1.00 58.76  ? 90  ALA C N   1 
ATOM   2109 C CA  . ALA C 1 91 ? 7.283   -23.052 24.991  1.00 60.32  ? 90  ALA C CA  1 
ATOM   2110 C C   . ALA C 1 91 ? 7.468   -24.436 25.628  1.00 69.98  ? 90  ALA C C   1 
ATOM   2111 O O   . ALA C 1 91 ? 8.600   -24.889 25.816  1.00 69.67  ? 90  ALA C O   1 
ATOM   2112 C CB  . ALA C 1 91 ? 6.540   -23.116 23.666  1.00 56.64  ? 90  ALA C CB  1 
ATOM   2113 N N   . SER C 1 92 ? 6.344   -25.113 25.917  1.00 72.65  ? 91  SER C N   1 
ATOM   2114 C CA  . SER C 1 92 ? 6.299   -26.297 26.769  1.00 73.93  ? 91  SER C CA  1 
ATOM   2115 C C   . SER C 1 92 ? 6.587   -27.592 26.010  1.00 73.83  ? 91  SER C C   1 
ATOM   2116 O O   . SER C 1 92 ? 7.463   -28.357 26.411  1.00 77.37  ? 91  SER C O   1 
ATOM   2117 C CB  . SER C 1 92 ? 4.982   -26.375 27.505  1.00 71.17  ? 91  SER C CB  1 
ATOM   2118 O OG  . SER C 1 92 ? 4.943   -25.373 28.508  1.00 64.81  ? 91  SER C OG  1 
ATOM   2119 N N   . TYR C 1 93 ? 5.795   -27.855 24.960  1.00 77.25  ? 92  TYR C N   1 
ATOM   2120 C CA  . TYR C 1 93 ? 5.939   -29.021 24.097  1.00 73.30  ? 92  TYR C CA  1 
ATOM   2121 C C   . TYR C 1 93 ? 5.836   -30.312 24.926  1.00 77.25  ? 92  TYR C C   1 
ATOM   2122 O O   . TYR C 1 93 ? 4.738   -30.623 25.446  1.00 83.26  ? 92  TYR C O   1 
ATOM   2123 C CB  . TYR C 1 93 ? 7.249   -28.953 23.301  1.00 65.56  ? 92  TYR C CB  1 
ATOM   2124 C CG  . TYR C 1 93 ? 7.460   -27.685 22.476  1.00 57.68  ? 92  TYR C CG  1 
ATOM   2125 C CD1 . TYR C 1 93 ? 6.642   -27.400 21.385  1.00 51.72  ? 92  TYR C CD1 1 
ATOM   2126 C CD2 . TYR C 1 93 ? 8.490   -26.792 22.767  1.00 52.46  ? 92  TYR C CD2 1 
ATOM   2127 C CE1 . TYR C 1 93 ? 6.817   -26.254 20.628  1.00 50.58  ? 92  TYR C CE1 1 
ATOM   2128 C CE2 . TYR C 1 93 ? 8.686   -25.649 22.002  1.00 47.52  ? 92  TYR C CE2 1 
ATOM   2129 C CZ  . TYR C 1 93 ? 7.847   -25.379 20.933  1.00 48.92  ? 92  TYR C CZ  1 
ATOM   2130 O OH  . TYR C 1 93 ? 8.023   -24.247 20.182  1.00 47.63  ? 92  TYR C OH  1 
HETATM 2131 S S   . SO4 D 2 .  ? 1.146   -33.605 1.684   1.00 102.35 ? 101 SO4 A S   1 
HETATM 2132 O O1  . SO4 D 2 .  ? 1.881   -34.524 0.849   1.00 79.71  ? 101 SO4 A O1  1 
HETATM 2133 O O2  . SO4 D 2 .  ? 0.918   -32.372 0.968   1.00 99.59  ? 101 SO4 A O2  1 
HETATM 2134 O O3  . SO4 D 2 .  ? -0.120  -34.194 2.044   1.00 111.38 ? 101 SO4 A O3  1 
HETATM 2135 O O4  . SO4 D 2 .  ? 1.898   -33.329 2.877   1.00 96.98  ? 101 SO4 A O4  1 
HETATM 2136 S S   . SO4 E 2 .  ? -9.444  -24.856 1.153   1.00 90.23  ? 102 SO4 A S   1 
HETATM 2137 O O1  . SO4 E 2 .  ? -9.024  -24.608 -0.204  1.00 85.37  ? 102 SO4 A O1  1 
HETATM 2138 O O2  . SO4 E 2 .  ? -9.254  -23.669 1.948   1.00 84.28  ? 102 SO4 A O2  1 
HETATM 2139 O O3  . SO4 E 2 .  ? -10.838 -25.221 1.152   1.00 99.39  ? 102 SO4 A O3  1 
HETATM 2140 O O4  . SO4 E 2 .  ? -8.666  -25.932 1.721   1.00 83.85  ? 102 SO4 A O4  1 
HETATM 2141 C C1  . EDO F 3 .  ? 14.058  -19.581 -7.345  1.00 33.73  ? 103 EDO A C1  1 
HETATM 2142 O O1  . EDO F 3 .  ? 15.292  -18.884 -7.206  1.00 29.62  ? 103 EDO A O1  1 
HETATM 2143 C C2  . EDO F 3 .  ? 13.197  -19.100 -8.472  1.00 32.92  ? 103 EDO A C2  1 
HETATM 2144 O O2  . EDO F 3 .  ? 12.712  -17.791 -8.297  1.00 33.47  ? 103 EDO A O2  1 
HETATM 2145 S S   . SO4 G 2 .  ? 9.122   -29.576 5.860   1.00 56.55  ? 104 SO4 A S   1 
HETATM 2146 O O1  . SO4 G 2 .  ? 9.944   -28.762 5.050   1.00 47.37  ? 104 SO4 A O1  1 
HETATM 2147 O O2  . SO4 G 2 .  ? 8.554   -30.640 5.043   1.00 58.87  ? 104 SO4 A O2  1 
HETATM 2148 O O3  . SO4 G 2 .  ? 9.928   -30.148 6.928   1.00 58.03  ? 104 SO4 A O3  1 
HETATM 2149 O O4  . SO4 G 2 .  ? 8.043   -28.796 6.408   1.00 65.76  ? 104 SO4 A O4  1 
HETATM 2150 S S   . SO4 H 2 .  ? 7.484   -8.461  -24.887 1.00 78.24  ? 101 SO4 B S   1 
HETATM 2151 O O1  . SO4 H 2 .  ? 8.612   -8.569  -25.784 1.00 39.73  ? 101 SO4 B O1  1 
HETATM 2152 O O2  . SO4 H 2 .  ? 6.288   -8.934  -25.552 1.00 60.09  ? 101 SO4 B O2  1 
HETATM 2153 O O3  . SO4 H 2 .  ? 7.655   -9.260  -23.665 1.00 48.64  ? 101 SO4 B O3  1 
HETATM 2154 O O4  . SO4 H 2 .  ? 7.380   -7.052  -24.555 1.00 61.41  ? 101 SO4 B O4  1 
HETATM 2155 S S   . SO4 I 2 .  ? 14.587  -27.099 -26.604 1.00 53.21  ? 102 SO4 B S   1 
HETATM 2156 O O1  . SO4 I 2 .  ? 15.778  -26.447 -26.149 1.00 58.37  ? 102 SO4 B O1  1 
HETATM 2157 O O2  . SO4 I 2 .  ? 14.961  -28.339 -27.249 1.00 63.18  ? 102 SO4 B O2  1 
HETATM 2158 O O3  . SO4 I 2 .  ? 13.733  -27.379 -25.485 1.00 61.32  ? 102 SO4 B O3  1 
HETATM 2159 O O4  . SO4 I 2 .  ? 13.880  -26.262 -27.528 1.00 51.20  ? 102 SO4 B O4  1 
HETATM 2160 C C01 . RYP J 4 .  ? 17.274  -16.833 -26.396 0.62 23.15  ? 103 RYP B C01 1 
HETATM 2161 C C03 . RYP J 4 .  ? 17.600  -16.227 -24.067 0.62 23.69  ? 103 RYP B C03 1 
HETATM 2162 C C04 . RYP J 4 .  ? 19.092  -16.253 -23.845 0.62 31.04  ? 103 RYP B C04 1 
HETATM 2163 C C05 . RYP J 4 .  ? 19.643  -17.026 -22.832 0.62 32.56  ? 103 RYP B C05 1 
HETATM 2164 C C06 . RYP J 4 .  ? 20.978  -16.864 -22.506 0.62 33.55  ? 103 RYP B C06 1 
HETATM 2165 C C08 . RYP J 4 .  ? 21.266  -15.300 -24.143 0.62 31.82  ? 103 RYP B C08 1 
HETATM 2166 C C09 . RYP J 4 .  ? 19.942  -15.398 -24.536 0.62 30.05  ? 103 RYP B C09 1 
HETATM 2167 N N02 . RYP J 4 .  ? 17.243  -15.755 -25.399 0.62 25.25  ? 103 RYP B N02 1 
HETATM 2168 N N07 . RYP J 4 .  ? 21.798  -16.008 -23.137 0.62 34.69  ? 103 RYP B N07 1 
HETATM 2169 C C1  . EDO K 3 .  ? 16.929  -36.414 16.384  1.00 43.44  ? 101 EDO C C1  1 
HETATM 2170 O O1  . EDO K 3 .  ? 15.824  -37.095 15.783  1.00 48.88  ? 101 EDO C O1  1 
HETATM 2171 C C2  . EDO K 3 .  ? 16.497  -35.418 17.394  1.00 35.52  ? 101 EDO C C2  1 
HETATM 2172 O O2  . EDO K 3 .  ? 15.436  -35.945 18.125  1.00 33.81  ? 101 EDO C O2  1 
HETATM 2173 S S   . SO4 L 2 .  ? 29.246  -38.737 12.353  1.00 92.34  ? 102 SO4 C S   1 
HETATM 2174 O O1  . SO4 L 2 .  ? 30.353  -37.915 11.924  1.00 95.41  ? 102 SO4 C O1  1 
HETATM 2175 O O2  . SO4 L 2 .  ? 28.030  -38.254 11.761  1.00 70.89  ? 102 SO4 C O2  1 
HETATM 2176 O O3  . SO4 L 2 .  ? 29.463  -40.100 11.945  1.00 84.31  ? 102 SO4 C O3  1 
HETATM 2177 O O4  . SO4 L 2 .  ? 29.136  -38.681 13.789  1.00 97.28  ? 102 SO4 C O4  1 
HETATM 2178 O O   . HOH M 5 .  ? 8.622   -32.446 4.075   1.00 52.62  ? 201 HOH A O   1 
HETATM 2179 O O   . HOH M 5 .  ? -5.704  -13.479 -16.542 1.00 51.65  ? 202 HOH A O   1 
HETATM 2180 O O   . HOH M 5 .  ? 5.693   -28.977 6.772   1.00 51.49  ? 203 HOH A O   1 
HETATM 2181 O O   . HOH M 5 .  ? 0.574   -10.553 -15.430 1.00 41.45  ? 204 HOH A O   1 
HETATM 2182 O O   . HOH M 5 .  ? -2.529  -11.650 13.821  1.00 48.47  ? 205 HOH A O   1 
HETATM 2183 O O   . HOH M 5 .  ? 15.486  -17.285 -19.135 1.00 43.22  ? 206 HOH A O   1 
HETATM 2184 O O   . HOH M 5 .  ? 11.079  -29.813 3.054   1.00 44.92  ? 207 HOH A O   1 
HETATM 2185 O O   . HOH M 5 .  ? 9.270   -18.215 -10.937 1.00 31.41  ? 208 HOH A O   1 
HETATM 2186 O O   . HOH M 5 .  ? -2.342  -30.931 -3.906  1.00 48.75  ? 209 HOH A O   1 
HETATM 2187 O O   . HOH M 5 .  ? 1.181   -24.790 13.791  1.00 53.24  ? 210 HOH A O   1 
HETATM 2188 O O   . HOH M 5 .  ? 7.179   -10.637 -12.138 1.00 36.26  ? 211 HOH A O   1 
HETATM 2189 O O   . HOH M 5 .  ? 11.128  -23.764 9.848   1.00 39.91  ? 212 HOH A O   1 
HETATM 2190 O O   . HOH M 5 .  ? -3.656  -10.760 6.766   1.00 34.58  ? 213 HOH A O   1 
HETATM 2191 O O   . HOH M 5 .  ? 3.752   -34.668 4.157   1.00 52.15  ? 214 HOH A O   1 
HETATM 2192 O O   . HOH M 5 .  ? 4.735   -7.896  1.140   1.00 32.52  ? 215 HOH A O   1 
HETATM 2193 O O   . HOH M 5 .  ? 10.910  -5.298  -7.757  1.00 32.45  ? 216 HOH A O   1 
HETATM 2194 O O   . HOH M 5 .  ? 13.482  -27.987 -4.804  1.00 50.23  ? 217 HOH A O   1 
HETATM 2195 O O   . HOH M 5 .  ? 14.132  -15.781 -9.279  1.00 32.49  ? 218 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? -2.232  3.127   -2.046  1.00 38.37  ? 219 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? 12.329  -15.778 -12.136 1.00 59.44  ? 220 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? -7.995  -15.822 -1.088  1.00 36.49  ? 221 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? 19.937  -15.580 7.324   1.00 30.75  ? 222 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? -7.624  -21.634 -5.163  1.00 74.71  ? 223 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 16.066  -24.582 1.927   1.00 39.33  ? 224 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 4.504   -3.593  -3.286  1.00 30.81  ? 225 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? -7.764  -17.225 6.603   1.00 43.71  ? 226 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? -4.240  -21.256 6.149   1.00 39.02  ? 227 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 3.284   -29.649 -0.478  1.00 39.36  ? 228 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 9.728   -6.110  -1.661  1.00 31.77  ? 229 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 12.880  -12.032 8.302   1.00 51.27  ? 230 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 11.652  -12.007 5.865   1.00 35.25  ? 231 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 0.243   -33.853 4.983   1.00 58.82  ? 232 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 8.423   -18.048 -15.941 1.00 52.66  ? 233 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? -0.638  -29.504 10.072  1.00 52.14  ? 234 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? -0.587  -20.959 6.999   1.00 36.49  ? 235 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? -1.637  -22.121 -0.591  1.00 27.05  ? 236 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? -4.397  -25.958 -5.567  1.00 42.81  ? 237 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 2.421   -25.033 -6.512  1.00 53.66  ? 238 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? 17.286  -12.956 1.381   1.00 19.19  ? 239 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 8.275   -17.465 8.645   1.00 41.10  ? 240 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 13.411  -12.050 -4.224  1.00 20.75  ? 241 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 1.903   -4.726  -10.273 1.00 36.28  ? 242 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? -5.769  -19.831 -5.603  1.00 34.68  ? 243 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 12.923  -9.539  -7.215  1.00 37.25  ? 244 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? -5.692  -15.949 -8.093  1.00 26.27  ? 245 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? -8.490  -21.206 -1.202  1.00 34.21  ? 246 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 16.768  -12.428 -17.049 1.00 41.68  ? 247 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 0.284   -23.599 9.240   1.00 44.32  ? 248 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 1.042   -18.035 -18.809 1.00 47.86  ? 249 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 11.605  -12.456 -6.142  1.00 25.12  ? 250 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 11.495  -5.961  -4.084  1.00 44.56  ? 251 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 9.421   -20.284 -18.505 1.00 48.53  ? 252 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 15.841  -12.059 -5.326  1.00 32.51  ? 253 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 10.069  -13.076 9.674   1.00 38.67  ? 254 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -7.936  -16.796 1.723   1.00 38.12  ? 255 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 2.626   -6.376  5.444   1.00 34.60  ? 256 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 1.803   -10.536 11.650  1.00 36.17  ? 257 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? 8.137   -7.933  1.184   1.00 29.58  ? 258 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 12.731  -13.329 -8.646  1.00 40.66  ? 259 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? -1.382  -11.881 11.279  1.00 35.39  ? 260 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 14.587  -29.532 3.941   1.00 42.04  ? 261 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 8.971   -16.404 -13.166 1.00 35.94  ? 262 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? -1.343  -7.529  11.502  1.00 48.85  ? 263 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 2.947   -9.922  -13.173 1.00 48.25  ? 264 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? -6.157  -12.815 6.698   1.00 40.00  ? 265 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? -6.240  -11.709 -11.389 1.00 37.00  ? 266 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 6.499   -6.064  0.501   1.00 51.74  ? 267 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 6.361   -16.282 -14.956 1.00 45.31  ? 268 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 5.223   -7.633  3.974   1.00 34.94  ? 269 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? -0.265  -20.754 11.009  1.00 59.69  ? 270 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 11.084  -7.934  0.378   1.00 25.26  ? 271 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 7.797   -30.003 -3.987  1.00 50.12  ? 272 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -7.196  -11.549 -8.011  1.00 28.58  ? 273 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 9.241   -2.135  -0.517  1.00 63.97  ? 274 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 22.326  -16.704 -0.476  1.00 40.99  ? 275 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -3.800  -7.787  10.669  1.00 42.49  ? 276 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 21.531  -16.792 -3.450  1.00 29.24  ? 277 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 15.403  -28.293 -0.883  1.00 56.78  ? 278 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -11.129 -16.117 -3.592  1.00 54.55  ? 279 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 17.250  -18.217 -9.643  1.00 47.19  ? 280 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? -5.973  -26.689 3.307   1.00 44.64  ? 281 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? -4.048  -26.707 7.408   1.00 50.47  ? 282 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 10.492  -27.700 -7.402  1.00 49.66  ? 283 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 15.469  -13.412 10.609  1.00 45.16  ? 284 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -8.027  -19.898 -3.537  1.00 51.65  ? 285 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 8.845   -9.181  -13.797 1.00 36.38  ? 286 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -5.587  -23.616 -6.989  1.00 40.83  ? 287 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? -3.798  -10.982 9.826   1.00 56.46  ? 288 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 1.163   -29.305 -7.264  1.00 58.98  ? 289 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? -7.255  -14.187 -9.258  1.00 41.08  ? 290 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -9.986  -28.481 -1.864  1.00 54.23  ? 291 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 5.052   -7.136  -11.087 1.00 41.11  ? 292 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 11.485  -1.950  -1.798  1.00 43.24  ? 293 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 4.900   -9.732  -11.322 1.00 44.04  ? 294 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? -6.301  -22.799 5.840   1.00 60.36  ? 295 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? -11.249 -13.542 -2.883  1.00 42.36  ? 296 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 8.146   -8.253  4.535   1.00 36.13  ? 297 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? -6.990  -19.185 8.432   1.00 51.67  ? 298 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -4.993  -21.173 -8.219  1.00 46.63  ? 299 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? 4.201   -3.253  1.859   1.00 63.10  ? 300 HOH A O   1 
HETATM 2278 O O   . HOH N 5 .  ? 30.767  -8.134  -29.894 1.00 52.08  ? 201 HOH B O   1 
HETATM 2279 O O   . HOH N 5 .  ? 10.125  -11.294 -38.191 1.00 47.90  ? 202 HOH B O   1 
HETATM 2280 O O   . HOH N 5 .  ? 25.292  -5.139  -29.961 1.00 36.14  ? 203 HOH B O   1 
HETATM 2281 O O   . HOH N 5 .  ? 20.165  -22.195 -23.406 1.00 54.13  ? 204 HOH B O   1 
HETATM 2282 O O   . HOH N 5 .  ? 24.351  -1.610  -36.348 1.00 52.47  ? 205 HOH B O   1 
HETATM 2283 O O   . HOH N 5 .  ? 27.801  -8.196  -28.918 1.00 43.26  ? 206 HOH B O   1 
HETATM 2284 O O   . HOH N 5 .  ? 29.885  -12.631 -45.575 1.00 73.26  ? 207 HOH B O   1 
HETATM 2285 O O   . HOH N 5 .  ? 30.357  -19.772 -40.448 1.00 37.02  ? 208 HOH B O   1 
HETATM 2286 O O   . HOH N 5 .  ? 12.998  -4.639  -41.822 1.00 51.70  ? 209 HOH B O   1 
HETATM 2287 O O   . HOH N 5 .  ? 21.903  -3.753  -24.508 1.00 58.94  ? 210 HOH B O   1 
HETATM 2288 O O   . HOH N 5 .  ? 10.398  -19.732 -43.276 1.00 48.03  ? 211 HOH B O   1 
HETATM 2289 O O   . HOH N 5 .  ? 6.644   -12.224 -26.220 1.00 35.04  ? 212 HOH B O   1 
HETATM 2290 O O   . HOH N 5 .  ? 25.616  -6.014  -35.964 1.00 44.53  ? 213 HOH B O   1 
HETATM 2291 O O   . HOH N 5 .  ? 26.270  -23.063 -31.325 1.00 37.08  ? 214 HOH B O   1 
HETATM 2292 O O   . HOH N 5 .  ? 17.780  -19.705 -42.213 1.00 46.09  ? 215 HOH B O   1 
HETATM 2293 O O   . HOH N 5 .  ? 6.190   -7.242  -32.330 1.00 59.97  ? 216 HOH B O   1 
HETATM 2294 O O   . HOH N 5 .  ? 27.794  -17.746 -25.285 1.00 46.70  ? 217 HOH B O   1 
HETATM 2295 O O   . HOH N 5 .  ? 25.887  -4.509  -33.736 1.00 48.05  ? 218 HOH B O   1 
HETATM 2296 O O   . HOH N 5 .  ? 32.607  -18.631 -42.412 1.00 51.20  ? 219 HOH B O   1 
HETATM 2297 O O   . HOH N 5 .  ? 20.968  -13.332 -42.805 1.00 37.58  ? 220 HOH B O   1 
HETATM 2298 O O   . HOH N 5 .  ? 34.728  -23.222 -30.077 1.00 59.11  ? 221 HOH B O   1 
HETATM 2299 O O   . HOH N 5 .  ? 16.820  -19.203 -28.945 1.00 23.72  ? 222 HOH B O   1 
HETATM 2300 O O   . HOH N 5 .  ? 10.620  -18.881 -33.120 1.00 26.51  ? 223 HOH B O   1 
HETATM 2301 O O   . HOH N 5 .  ? 13.286  -22.347 -20.782 1.00 60.87  ? 224 HOH B O   1 
HETATM 2302 O O   . HOH N 5 .  ? 7.662   -12.574 -38.933 1.00 44.78  ? 225 HOH B O   1 
HETATM 2303 O O   . HOH N 5 .  ? 10.516  -16.906 -44.426 1.00 45.11  ? 226 HOH B O   1 
HETATM 2304 O O   . HOH N 5 .  ? 3.176   -8.719  -27.189 1.00 54.52  ? 227 HOH B O   1 
HETATM 2305 O O   . HOH N 5 .  ? 22.082  3.741   -32.626 1.00 46.94  ? 228 HOH B O   1 
HETATM 2306 O O   . HOH N 5 .  ? 10.734  -21.880 -32.914 1.00 37.54  ? 229 HOH B O   1 
HETATM 2307 O O   . HOH N 5 .  ? 18.196  -0.491  -38.572 1.00 28.44  ? 230 HOH B O   1 
HETATM 2308 O O   . HOH N 5 .  ? 23.706  -2.283  -29.178 1.00 41.52  ? 231 HOH B O   1 
HETATM 2309 O O   . HOH N 5 .  ? 22.734  -23.214 -28.905 1.00 39.72  ? 232 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 26.277  -0.336  -29.524 1.00 49.55  ? 233 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 8.787   -8.782  -16.612 1.00 38.53  ? 234 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 14.458  -6.414  -41.243 1.00 40.23  ? 235 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 18.091  -3.486  -22.335 1.00 54.93  ? 236 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 23.765  -4.160  -36.968 1.00 30.72  ? 237 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 27.299  -10.636 -28.963 1.00 49.43  ? 238 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 21.070  -26.418 -30.216 1.00 58.72  ? 239 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 20.533  -10.105 -43.071 1.00 38.66  ? 240 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 7.072   -19.114 -35.039 1.00 44.51  ? 241 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 14.750  -24.531 -40.439 1.00 41.09  ? 242 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 25.088  -6.499  -42.534 1.00 55.43  ? 243 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 31.698  -12.360 -38.680 1.00 56.08  ? 244 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 7.586   -18.267 -31.844 1.00 42.06  ? 245 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 19.811  -25.741 -34.308 1.00 40.74  ? 246 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 8.405   -27.962 -38.405 1.00 55.30  ? 247 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 19.979  -7.943  -21.292 1.00 52.37  ? 248 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 18.034  -15.940 -45.944 1.00 40.80  ? 249 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 1.793   -13.023 -28.466 1.00 48.31  ? 250 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 7.510   -8.097  -20.908 1.00 48.27  ? 251 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 31.982  -21.302 -38.314 1.00 38.96  ? 252 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 21.161  -6.379  -42.725 1.00 36.71  ? 253 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 18.303  -0.272  -25.649 1.00 59.66  ? 254 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 23.547  -11.444 -21.921 1.00 40.97  ? 255 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 27.868  -24.850 -35.232 1.00 36.68  ? 256 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 17.125  -9.570  -43.969 1.00 44.61  ? 257 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 18.608  -26.015 -28.943 1.00 40.57  ? 258 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 39.035  -13.115 -39.739 1.00 65.85  ? 259 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 20.530  3.880   -33.130 1.00 34.34  ? 260 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 6.389   -20.637 -25.072 1.00 40.99  ? 261 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 25.074  -8.259  -22.660 1.00 49.48  ? 262 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 7.681   -23.629 -24.301 1.00 61.62  ? 263 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 18.537  4.586   -34.324 1.00 41.18  ? 264 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 9.856   -5.949  -41.139 1.00 52.18  ? 265 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 12.869  -20.271 -19.765 1.00 55.93  ? 266 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 15.141  -8.055  -43.147 1.00 40.91  ? 267 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 16.999  -25.659 -20.887 1.00 63.33  ? 268 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 11.465  -24.112 -30.003 1.00 45.24  ? 269 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 15.418  -21.867 -42.035 1.00 48.42  ? 270 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 13.662  -5.750  -18.139 1.00 62.25  ? 271 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 7.482   -9.998  -18.628 1.00 39.03  ? 272 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 22.305  -29.195 -35.601 1.00 45.03  ? 273 HOH B O   1 
HETATM 2351 O O   . HOH O 5 .  ? 26.942  -37.864 10.143  1.00 39.18  ? 201 HOH C O   1 
HETATM 2352 O O   . HOH O 5 .  ? 26.705  -39.419 12.710  1.00 40.09  ? 202 HOH C O   1 
HETATM 2353 O O   . HOH O 5 .  ? 19.871  -20.100 29.982  1.00 60.52  ? 203 HOH C O   1 
HETATM 2354 O O   . HOH O 5 .  ? 8.095   -36.078 18.074  1.00 66.50  ? 204 HOH C O   1 
HETATM 2355 O O   . HOH O 5 .  ? 15.183  -39.209 16.803  1.00 60.32  ? 205 HOH C O   1 
HETATM 2356 O O   . HOH O 5 .  ? 7.893   -31.726 12.185  1.00 49.91  ? 206 HOH C O   1 
HETATM 2357 O O   . HOH O 5 .  ? 12.159  -28.681 28.042  1.00 54.95  ? 207 HOH C O   1 
HETATM 2358 O O   . HOH O 5 .  ? 17.487  -17.215 15.031  1.00 41.15  ? 208 HOH C O   1 
HETATM 2359 O O   . HOH O 5 .  ? 19.234  -20.280 10.578  1.00 39.45  ? 209 HOH C O   1 
HETATM 2360 O O   . HOH O 5 .  ? 22.999  -41.699 18.493  1.00 40.89  ? 210 HOH C O   1 
HETATM 2361 O O   . HOH O 5 .  ? 31.824  -33.404 25.894  1.00 45.52  ? 211 HOH C O   1 
HETATM 2362 O O   . HOH O 5 .  ? 25.555  -33.922 34.803  1.00 52.48  ? 212 HOH C O   1 
HETATM 2363 O O   . HOH O 5 .  ? 8.954   -19.076 23.534  1.00 50.46  ? 213 HOH C O   1 
HETATM 2364 O O   . HOH O 5 .  ? 15.373  -21.240 12.501  1.00 39.56  ? 214 HOH C O   1 
HETATM 2365 O O   . HOH O 5 .  ? 19.433  -26.753 3.381   1.00 51.59  ? 215 HOH C O   1 
HETATM 2366 O O   . HOH O 5 .  ? 12.866  -31.652 8.181   1.00 31.23  ? 216 HOH C O   1 
HETATM 2367 O O   . HOH O 5 .  ? 20.080  -41.986 12.213  1.00 28.04  ? 217 HOH C O   1 
HETATM 2368 O O   . HOH O 5 .  ? 28.407  -37.294 15.952  1.00 41.09  ? 218 HOH C O   1 
HETATM 2369 O O   . HOH O 5 .  ? 30.403  -40.630 9.492   1.00 35.95  ? 219 HOH C O   1 
HETATM 2370 O O   . HOH O 5 .  ? 25.768  -19.618 6.426   1.00 35.67  ? 220 HOH C O   1 
HETATM 2371 O O   . HOH O 5 .  ? 15.638  -17.741 19.429  1.00 41.15  ? 221 HOH C O   1 
HETATM 2372 O O   . HOH O 5 .  ? 30.465  -31.283 15.784  1.00 45.31  ? 222 HOH C O   1 
HETATM 2373 O O   . HOH O 5 .  ? 13.812  -37.422 13.711  1.00 47.05  ? 223 HOH C O   1 
HETATM 2374 O O   . HOH O 5 .  ? 22.719  -21.733 7.473   1.00 39.07  ? 224 HOH C O   1 
HETATM 2375 O O   . HOH O 5 .  ? 22.924  -18.632 21.763  1.00 53.38  ? 225 HOH C O   1 
HETATM 2376 O O   . HOH O 5 .  ? 5.667   -26.755 16.737  1.00 51.39  ? 226 HOH C O   1 
HETATM 2377 O O   . HOH O 5 .  ? 22.314  -28.601 11.118  1.00 31.81  ? 227 HOH C O   1 
HETATM 2378 O O   . HOH O 5 .  ? 25.850  -17.591 14.007  1.00 45.97  ? 228 HOH C O   1 
HETATM 2379 O O   . HOH O 5 .  ? 27.860  -37.912 25.032  1.00 46.09  ? 229 HOH C O   1 
HETATM 2380 O O   . HOH O 5 .  ? 25.341  -31.517 10.830  1.00 35.64  ? 230 HOH C O   1 
HETATM 2381 O O   . HOH O 5 .  ? 33.558  -24.491 31.601  1.00 45.07  ? 231 HOH C O   1 
HETATM 2382 O O   . HOH O 5 .  ? 23.247  -38.250 10.126  1.00 35.65  ? 232 HOH C O   1 
HETATM 2383 O O   . HOH O 5 .  ? 31.558  -43.455 15.785  1.00 54.13  ? 233 HOH C O   1 
HETATM 2384 O O   . HOH O 5 .  ? 20.294  -41.264 39.475  1.00 63.18  ? 234 HOH C O   1 
HETATM 2385 O O   . HOH O 5 .  ? 22.164  -34.540 16.566  1.00 26.08  ? 235 HOH C O   1 
HETATM 2386 O O   . HOH O 5 .  ? 29.817  -40.036 31.493  1.00 36.57  ? 236 HOH C O   1 
HETATM 2387 O O   . HOH O 5 .  ? 31.344  -40.010 27.294  1.00 50.90  ? 237 HOH C O   1 
HETATM 2388 O O   . HOH O 5 .  ? 6.979   -18.083 10.800  1.00 41.08  ? 238 HOH C O   1 
HETATM 2389 O O   . HOH O 5 .  ? 27.940  -15.192 12.868  1.00 49.90  ? 239 HOH C O   1 
HETATM 2390 O O   . HOH O 5 .  ? 30.591  -17.344 9.829   1.00 44.53  ? 240 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 20.719  -40.155 26.403  1.00 37.96  ? 241 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 31.883  -43.437 11.934  1.00 46.20  ? 242 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 25.676  -39.791 20.139  1.00 34.44  ? 243 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 21.018  -28.844 8.502   1.00 35.85  ? 244 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 17.058  -38.274 19.485  1.00 56.01  ? 245 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 19.859  -19.289 25.095  1.00 50.24  ? 246 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 9.731   -30.472 9.904   1.00 32.73  ? 247 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 21.215  -29.655 4.976   1.00 58.59  ? 248 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 2.716   -28.869 14.042  1.00 61.23  ? 249 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 14.389  -38.876 9.456   1.00 54.92  ? 250 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 30.686  -35.754 28.721  1.00 50.43  ? 251 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 25.304  -17.910 21.237  1.00 56.30  ? 252 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 30.424  -32.862 18.278  1.00 46.29  ? 253 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 5.075   -24.364 18.580  1.00 66.28  ? 254 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 29.068  -25.377 33.095  1.00 60.09  ? 255 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 20.648  -13.039 13.379  1.00 47.28  ? 256 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 22.378  -14.039 13.366  1.00 46.93  ? 257 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 29.297  -41.874 27.288  1.00 41.07  ? 258 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 17.089  -36.801 29.353  1.00 54.27  ? 259 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 12.103  -21.212 10.679  1.00 39.08  ? 260 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 13.332  -22.992 28.012  1.00 72.00  ? 261 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 36.886  -24.529 26.531  1.00 68.24  ? 262 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 28.402  -41.754 29.942  1.00 44.16  ? 263 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 33.694  -44.647 15.392  1.00 36.32  ? 264 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 29.395  -40.820 19.469  1.00 55.35  ? 265 HOH C O   1 
# 
