data_7HH4
# 
_entry.id   7HH4 
# 
_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   7HH4         pdb_00007hh4 10.2210/pdb7hh4/pdb 
WWPDB D_1001407466 ?            ?                   
# 
_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                        7HH4 
_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           N 
_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    1   ? ?    ? ? 
4 non-polymer syn '(3R)-N-methyl-1-(pyridazin-3-yl)piperidin-3-amine' 192.261   1   ? ?    ? ? 
5 non-polymer syn '(3R)-N-methyl-1-(pyridazin-3-yl)piperidin-3-amine' 192.261   2   ? ?    ? ? 
6 water       nat water                                               18.015    232 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                       SO4   
3 1,2-ETHANEDIOL                                      EDO   
4 '(3R)-N-methyl-1-(pyridazin-3-yl)piperidin-3-amine' A1A39 
5 '(3R)-N-methyl-1-(pyridazin-3-yl)piperidin-3-amine' W0J   
6 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 
A1A39 non-polymer         . '(3R)-N-methyl-1-(pyridazin-3-yl)piperidin-3-amine' ?                 'C10 H16 N4'     192.261 
ALA   'L-peptide linking' y ALANINE                                             ?                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                            ?                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                          ?                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                     ?                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                            ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                      'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE                                           ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                     ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                             ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                           ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                               ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                          ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                             ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                              ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                          ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                       ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                             ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                              ?                 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                       ?                 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                           ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                          ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                            ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                              ?                 'C5 H11 N O2'    117.146 
W0J   non-polymer         . '(3R)-N-methyl-1-(pyridazin-3-yl)piperidin-3-amine' ?                 'C10 H16 N4'     192.261 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 29 ALA ALA B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A39 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A39 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 4 A1A39 1   104 101 A1A39 LIG A . 
H 2 SO4   1   105 4   SO4   SO4 A . 
I 2 SO4   1   101 1   SO4   SO4 B . 
J 2 SO4   1   102 3   SO4   SO4 B . 
K 5 W0J   1   103 101 W0J   LIG B . 
L 2 SO4   1   101 5   SO4   SO4 C . 
M 5 W0J   1   102 101 W0J   LIG C . 
N 6 HOH   1   201 307 HOH   HOH A . 
N 6 HOH   2   202 304 HOH   HOH A . 
N 6 HOH   3   203 202 HOH   HOH A . 
N 6 HOH   4   204 71  HOH   HOH A . 
N 6 HOH   5   205 84  HOH   HOH A . 
N 6 HOH   6   206 66  HOH   HOH A . 
N 6 HOH   7   207 95  HOH   HOH A . 
N 6 HOH   8   208 55  HOH   HOH A . 
N 6 HOH   9   209 139 HOH   HOH A . 
N 6 HOH   10  210 26  HOH   HOH A . 
N 6 HOH   11  211 28  HOH   HOH A . 
N 6 HOH   12  212 91  HOH   HOH A . 
N 6 HOH   13  213 260 HOH   HOH A . 
N 6 HOH   14  214 259 HOH   HOH A . 
N 6 HOH   15  215 37  HOH   HOH A . 
N 6 HOH   16  216 199 HOH   HOH A . 
N 6 HOH   17  217 86  HOH   HOH A . 
N 6 HOH   18  218 87  HOH   HOH A . 
N 6 HOH   19  219 289 HOH   HOH A . 
N 6 HOH   20  220 27  HOH   HOH A . 
N 6 HOH   21  221 164 HOH   HOH A . 
N 6 HOH   22  222 94  HOH   HOH A . 
N 6 HOH   23  223 188 HOH   HOH A . 
N 6 HOH   24  224 34  HOH   HOH A . 
N 6 HOH   25  225 32  HOH   HOH A . 
N 6 HOH   26  226 208 HOH   HOH A . 
N 6 HOH   27  227 7   HOH   HOH A . 
N 6 HOH   28  228 12  HOH   HOH A . 
N 6 HOH   29  229 8   HOH   HOH A . 
N 6 HOH   30  230 97  HOH   HOH A . 
N 6 HOH   31  231 23  HOH   HOH A . 
N 6 HOH   32  232 293 HOH   HOH A . 
N 6 HOH   33  233 267 HOH   HOH A . 
N 6 HOH   34  234 203 HOH   HOH A . 
N 6 HOH   35  235 292 HOH   HOH A . 
N 6 HOH   36  236 99  HOH   HOH A . 
N 6 HOH   37  237 288 HOH   HOH A . 
N 6 HOH   38  238 41  HOH   HOH A . 
N 6 HOH   39  239 301 HOH   HOH A . 
N 6 HOH   40  240 1   HOH   HOH A . 
N 6 HOH   41  241 179 HOH   HOH A . 
N 6 HOH   42  242 218 HOH   HOH A . 
N 6 HOH   43  243 109 HOH   HOH A . 
N 6 HOH   44  244 274 HOH   HOH A . 
N 6 HOH   45  245 2   HOH   HOH A . 
N 6 HOH   46  246 300 HOH   HOH A . 
N 6 HOH   47  247 18  HOH   HOH A . 
N 6 HOH   48  248 111 HOH   HOH A . 
N 6 HOH   49  249 77  HOH   HOH A . 
N 6 HOH   50  250 21  HOH   HOH A . 
N 6 HOH   51  251 297 HOH   HOH A . 
N 6 HOH   52  252 60  HOH   HOH A . 
N 6 HOH   53  253 287 HOH   HOH A . 
N 6 HOH   54  254 145 HOH   HOH A . 
N 6 HOH   55  255 58  HOH   HOH A . 
N 6 HOH   56  256 299 HOH   HOH A . 
N 6 HOH   57  257 190 HOH   HOH A . 
N 6 HOH   58  258 116 HOH   HOH A . 
N 6 HOH   59  259 167 HOH   HOH A . 
N 6 HOH   60  260 115 HOH   HOH A . 
N 6 HOH   61  261 78  HOH   HOH A . 
N 6 HOH   62  262 20  HOH   HOH A . 
N 6 HOH   63  263 143 HOH   HOH A . 
N 6 HOH   64  264 222 HOH   HOH A . 
N 6 HOH   65  265 113 HOH   HOH A . 
N 6 HOH   66  266 42  HOH   HOH A . 
N 6 HOH   67  267 14  HOH   HOH A . 
N 6 HOH   68  268 131 HOH   HOH A . 
N 6 HOH   69  269 93  HOH   HOH A . 
N 6 HOH   70  270 38  HOH   HOH A . 
N 6 HOH   71  271 47  HOH   HOH A . 
N 6 HOH   72  272 9   HOH   HOH A . 
N 6 HOH   73  273 318 HOH   HOH A . 
N 6 HOH   74  274 16  HOH   HOH A . 
N 6 HOH   75  275 64  HOH   HOH A . 
N 6 HOH   76  276 211 HOH   HOH A . 
N 6 HOH   77  277 31  HOH   HOH A . 
N 6 HOH   78  278 19  HOH   HOH A . 
N 6 HOH   79  279 73  HOH   HOH A . 
N 6 HOH   80  280 281 HOH   HOH A . 
N 6 HOH   81  281 296 HOH   HOH A . 
N 6 HOH   82  282 152 HOH   HOH A . 
N 6 HOH   83  283 63  HOH   HOH A . 
N 6 HOH   84  284 22  HOH   HOH A . 
N 6 HOH   85  285 165 HOH   HOH A . 
N 6 HOH   86  286 327 HOH   HOH A . 
N 6 HOH   87  287 75  HOH   HOH A . 
N 6 HOH   88  288 210 HOH   HOH A . 
N 6 HOH   89  289 146 HOH   HOH A . 
N 6 HOH   90  290 83  HOH   HOH A . 
N 6 HOH   91  291 270 HOH   HOH A . 
N 6 HOH   92  292 185 HOH   HOH A . 
N 6 HOH   93  293 219 HOH   HOH A . 
N 6 HOH   94  294 57  HOH   HOH A . 
N 6 HOH   95  295 283 HOH   HOH A . 
N 6 HOH   96  296 35  HOH   HOH A . 
N 6 HOH   97  297 205 HOH   HOH A . 
N 6 HOH   98  298 156 HOH   HOH A . 
N 6 HOH   99  299 125 HOH   HOH A . 
N 6 HOH   100 300 332 HOH   HOH A . 
O 6 HOH   1   201 272 HOH   HOH B . 
O 6 HOH   2   202 247 HOH   HOH B . 
O 6 HOH   3   203 123 HOH   HOH B . 
O 6 HOH   4   204 184 HOH   HOH B . 
O 6 HOH   5   205 69  HOH   HOH B . 
O 6 HOH   6   206 331 HOH   HOH B . 
O 6 HOH   7   207 17  HOH   HOH B . 
O 6 HOH   8   208 89  HOH   HOH B . 
O 6 HOH   9   209 329 HOH   HOH B . 
O 6 HOH   10  210 137 HOH   HOH B . 
O 6 HOH   11  211 98  HOH   HOH B . 
O 6 HOH   12  212 68  HOH   HOH B . 
O 6 HOH   13  213 172 HOH   HOH B . 
O 6 HOH   14  214 177 HOH   HOH B . 
O 6 HOH   15  215 249 HOH   HOH B . 
O 6 HOH   16  216 223 HOH   HOH B . 
O 6 HOH   17  217 54  HOH   HOH B . 
O 6 HOH   18  218 242 HOH   HOH B . 
O 6 HOH   19  219 153 HOH   HOH B . 
O 6 HOH   20  220 150 HOH   HOH B . 
O 6 HOH   21  221 10  HOH   HOH B . 
O 6 HOH   22  222 280 HOH   HOH B . 
O 6 HOH   23  223 117 HOH   HOH B . 
O 6 HOH   24  224 59  HOH   HOH B . 
O 6 HOH   25  225 168 HOH   HOH B . 
O 6 HOH   26  226 258 HOH   HOH B . 
O 6 HOH   27  227 13  HOH   HOH B . 
O 6 HOH   28  228 320 HOH   HOH B . 
O 6 HOH   29  229 6   HOH   HOH B . 
O 6 HOH   30  230 5   HOH   HOH B . 
O 6 HOH   31  231 72  HOH   HOH B . 
O 6 HOH   32  232 215 HOH   HOH B . 
O 6 HOH   33  233 217 HOH   HOH B . 
O 6 HOH   34  234 169 HOH   HOH B . 
O 6 HOH   35  235 261 HOH   HOH B . 
O 6 HOH   36  236 25  HOH   HOH B . 
O 6 HOH   37  237 315 HOH   HOH B . 
O 6 HOH   38  238 24  HOH   HOH B . 
O 6 HOH   39  239 120 HOH   HOH B . 
O 6 HOH   40  240 96  HOH   HOH B . 
O 6 HOH   41  241 101 HOH   HOH B . 
O 6 HOH   42  242 224 HOH   HOH B . 
O 6 HOH   43  243 79  HOH   HOH B . 
O 6 HOH   44  244 61  HOH   HOH B . 
O 6 HOH   45  245 319 HOH   HOH B . 
O 6 HOH   46  246 175 HOH   HOH B . 
O 6 HOH   47  247 76  HOH   HOH B . 
O 6 HOH   48  248 119 HOH   HOH B . 
O 6 HOH   49  249 104 HOH   HOH B . 
O 6 HOH   50  250 214 HOH   HOH B . 
O 6 HOH   51  251 74  HOH   HOH B . 
O 6 HOH   52  252 197 HOH   HOH B . 
O 6 HOH   53  253 36  HOH   HOH B . 
O 6 HOH   54  254 279 HOH   HOH B . 
O 6 HOH   55  255 182 HOH   HOH B . 
O 6 HOH   56  256 157 HOH   HOH B . 
O 6 HOH   57  257 46  HOH   HOH B . 
O 6 HOH   58  258 303 HOH   HOH B . 
O 6 HOH   59  259 44  HOH   HOH B . 
O 6 HOH   60  260 316 HOH   HOH B . 
O 6 HOH   61  261 160 HOH   HOH B . 
O 6 HOH   62  262 322 HOH   HOH B . 
O 6 HOH   63  263 170 HOH   HOH B . 
O 6 HOH   64  264 291 HOH   HOH B . 
O 6 HOH   65  265 163 HOH   HOH B . 
O 6 HOH   66  266 201 HOH   HOH B . 
O 6 HOH   67  267 103 HOH   HOH B . 
O 6 HOH   68  268 314 HOH   HOH B . 
O 6 HOH   69  269 107 HOH   HOH B . 
O 6 HOH   70  270 312 HOH   HOH B . 
P 6 HOH   1   201 323 HOH   HOH C . 
P 6 HOH   2   202 254 HOH   HOH C . 
P 6 HOH   3   203 321 HOH   HOH C . 
P 6 HOH   4   204 161 HOH   HOH C . 
P 6 HOH   5   205 118 HOH   HOH C . 
P 6 HOH   6   206 302 HOH   HOH C . 
P 6 HOH   7   207 271 HOH   HOH C . 
P 6 HOH   8   208 85  HOH   HOH C . 
P 6 HOH   9   209 209 HOH   HOH C . 
P 6 HOH   10  210 90  HOH   HOH C . 
P 6 HOH   11  211 142 HOH   HOH C . 
P 6 HOH   12  212 309 HOH   HOH C . 
P 6 HOH   13  213 148 HOH   HOH C . 
P 6 HOH   14  214 134 HOH   HOH C . 
P 6 HOH   15  215 15  HOH   HOH C . 
P 6 HOH   16  216 173 HOH   HOH C . 
P 6 HOH   17  217 82  HOH   HOH C . 
P 6 HOH   18  218 317 HOH   HOH C . 
P 6 HOH   19  219 294 HOH   HOH C . 
P 6 HOH   20  220 226 HOH   HOH C . 
P 6 HOH   21  221 132 HOH   HOH C . 
P 6 HOH   22  222 49  HOH   HOH C . 
P 6 HOH   23  223 284 HOH   HOH C . 
P 6 HOH   24  224 53  HOH   HOH C . 
P 6 HOH   25  225 269 HOH   HOH C . 
P 6 HOH   26  226 126 HOH   HOH C . 
P 6 HOH   27  227 333 HOH   HOH C . 
P 6 HOH   28  228 130 HOH   HOH C . 
P 6 HOH   29  229 45  HOH   HOH C . 
P 6 HOH   30  230 4   HOH   HOH C . 
P 6 HOH   31  231 67  HOH   HOH C . 
P 6 HOH   32  232 135 HOH   HOH C . 
P 6 HOH   33  233 40  HOH   HOH C . 
P 6 HOH   34  234 48  HOH   HOH C . 
P 6 HOH   35  235 102 HOH   HOH C . 
P 6 HOH   36  236 43  HOH   HOH C . 
P 6 HOH   37  237 122 HOH   HOH C . 
P 6 HOH   38  238 56  HOH   HOH C . 
P 6 HOH   39  239 275 HOH   HOH C . 
P 6 HOH   40  240 62  HOH   HOH C . 
P 6 HOH   41  241 336 HOH   HOH C . 
P 6 HOH   42  242 298 HOH   HOH C . 
P 6 HOH   43  243 151 HOH   HOH C . 
P 6 HOH   44  244 328 HOH   HOH C . 
P 6 HOH   45  245 198 HOH   HOH C . 
P 6 HOH   46  246 171 HOH   HOH C . 
P 6 HOH   47  247 335 HOH   HOH C . 
P 6 HOH   48  248 65  HOH   HOH C . 
P 6 HOH   49  249 295 HOH   HOH C . 
P 6 HOH   50  250 149 HOH   HOH C . 
P 6 HOH   51  251 305 HOH   HOH C . 
P 6 HOH   52  252 241 HOH   HOH C . 
P 6 HOH   53  253 70  HOH   HOH C . 
P 6 HOH   54  254 330 HOH   HOH C . 
P 6 HOH   55  255 108 HOH   HOH C . 
P 6 HOH   56  256 324 HOH   HOH C . 
P 6 HOH   57  257 334 HOH   HOH C . 
P 6 HOH   58  258 310 HOH   HOH C . 
P 6 HOH   59  259 92  HOH   HOH C . 
P 6 HOH   60  260 206 HOH   HOH C . 
P 6 HOH   61  261 313 HOH   HOH C . 
P 6 HOH   62  262 246 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 ILE 28 ? CG1 ? C ILE 29 CG1 
48 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
49 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
50 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
51 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
52 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
53 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
54 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
55 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
56 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
57 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
58 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
59 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
60 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
61 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
62 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
63 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
64 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
65 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
66 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
67 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
68 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           7HH4 
_cell.length_a           41.710 
_cell.length_b           42.310 
_cell.length_c           159.310 
_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                         7HH4 
_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          7HH4 
_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                     7HH4 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             42.31 
_reflns.d_resolution_high            1.49 
_reflns.number_obs                   47184 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.052 
_reflns.pdbx_netI_over_sigmaI        13.6 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.057 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     288434 
_reflns.pdbx_chi_squared             0.95 
_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                  1.49 
_reflns_shell.d_res_low                   1.53 
_reflns_shell.number_measured_all         16015 
_reflns_shell.number_unique_obs           3418 
_reflns_shell.Rmerge_I_obs                1.632 
_reflns_shell.pdbx_chi_squared            0.81 
_reflns_shell.pdbx_redundancy             4.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.842 
_reflns_shell.pdbx_Rpim_I_all             0.842 
_reflns_shell.pdbx_CC_half                0.398 
_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                                 7HH4 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     44594 
_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                             40.93 
_refine.ls_d_res_high                            1.49 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_R_factor_obs                          0.21128 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20979 
_refine.ls_R_factor_R_free                       0.23776 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2499 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_refine.B_iso_mean                               35.507 
_refine.aniso_B[1][1]                            0.79 
_refine.aniso_B[2][2]                            -0.15 
_refine.aniso_B[3][3]                            -0.64 
_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                       0.085 
_refine.pdbx_overall_ESU_R_Free                  0.085 
_refine.overall_SU_ML                            0.074 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.096 
_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        2149 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         76 
_refine_hist.number_atoms_solvent             232 
_refine_hist.number_atoms_total               2457 
_refine_hist.d_res_high                       1.49 
_refine_hist.d_res_low                        40.93 
# 
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             0.010  0.012  ? 2331 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          2.095  1.825  ? 3173 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.101  5.000  ? 270  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.591  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.140 10.000 ? 297  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.141  0.200  ? 294  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 1962 '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                  3.310  3.330  ? 1092 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.533  5.950  ? 1356 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.179  3.636  ? 1239 '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       8.719  49.06  ? 3539 '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                       1.490 
_refine_ls_shell.d_res_low                        1.529 
_refine_ls_shell.number_reflns_R_work             3221 
_refine_ls_shell.R_factor_R_work                  0.354 
_refine_ls_shell.percent_reflns_obs               99.50 
_refine_ls_shell.R_factor_R_free                  0.399 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             174 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH4 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1139246057' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH4 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 5 ? 
L N N 2 ? 
M N N 5 ? 
N N N 6 ? 
O N N 6 ? 
P N N 6 ? 
# 
_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 7HH4 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH4 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH4 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 7HH4 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH4 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH4 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH4 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH4 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH4 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O 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                   7HH4 
_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 222 ? ? O  B HOH   262 ? ? 1.26 
2 1 OD1 C ASP 9   ? ? O  C HOH   201 ? ? 2.09 
3 1 O2  C SO4 101 ? ? O  C HOH   202 ? ? 2.09 
4 1 OE1 A GLU 49  ? ? C5 A A1A39 104 ? ? 2.11 
5 1 O2  C SO4 101 ? ? O  C HOH   203 ? ? 2.14 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     289 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     256 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_445 
_pdbx_validate_symm_contact.dist              2.17 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CG A MET 15 ? ? SD A MET 15 ? ? CE A MET 15 ? ? 76.61 100.20 -23.59 1.60 N 
2 1 CG C MET 15 ? ? SD C MET 15 ? ? CE C MET 15 ? ? 71.30 100.20 -28.90 1.60 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -152.82 67.16 
2 1 ASN B 38 ? ? 77.42   -2.62 
3 1 ASN B 87 ? ? -159.32 61.32 
4 1 ASN C 87 ? ? -157.97 49.18 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.69 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ASP 30 ? B ASP 31 
4  1 Y 1 B GLY 31 ? B GLY 32 
5  1 Y 1 B ALA 32 ? B ALA 33 
6  1 Y 1 C GLY 0  ? C GLY 1  
7  1 Y 1 C MET 1  ? C MET 2  
8  1 Y 1 C PRO 2  ? C PRO 3  
9  1 Y 1 C ASP 30 ? C ASP 31 
10 1 Y 1 C GLY 31 ? C GLY 32 
11 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 
A1A39 N1   N N N 1   
A1A39 N3   N Y N 2   
A1A39 C4   C N N 3   
A1A39 C5   C N N 4   
A1A39 C6   C Y N 5   
A1A39 C7   C Y N 6   
A1A39 C8   C Y N 7   
A1A39 C    C N N 8   
A1A39 N    N N N 9   
A1A39 C1   C N S 10  
A1A39 C3   C N N 11  
A1A39 C2   C N N 12  
A1A39 N2   N Y N 13  
A1A39 C9   C Y N 14  
A1A39 H10  H N N 15  
A1A39 H9   H N N 16  
A1A39 H11  H N N 17  
A1A39 H12  H N N 18  
A1A39 H13  H N N 19  
A1A39 H14  H N N 20  
A1A39 H2   H N N 21  
A1A39 H    H N N 22  
A1A39 H1   H N N 23  
A1A39 H3   H N N 24  
A1A39 H4   H N N 25  
A1A39 H7   H N N 26  
A1A39 H8   H N N 27  
A1A39 H5   H N N 28  
A1A39 H6   H N N 29  
A1A39 H15  H N N 30  
ALA   N    N N N 31  
ALA   CA   C N S 32  
ALA   C    C N N 33  
ALA   O    O N N 34  
ALA   CB   C N N 35  
ALA   OXT  O N N 36  
ALA   H    H N N 37  
ALA   H2   H N N 38  
ALA   HA   H N N 39  
ALA   HB1  H N N 40  
ALA   HB2  H N N 41  
ALA   HB3  H N N 42  
ALA   HXT  H N N 43  
ARG   N    N N N 44  
ARG   CA   C N S 45  
ARG   C    C N N 46  
ARG   O    O N N 47  
ARG   CB   C N N 48  
ARG   CG   C N N 49  
ARG   CD   C N N 50  
ARG   NE   N N N 51  
ARG   CZ   C N N 52  
ARG   NH1  N N N 53  
ARG   NH2  N N N 54  
ARG   OXT  O N N 55  
ARG   H    H N N 56  
ARG   H2   H N N 57  
ARG   HA   H N N 58  
ARG   HB2  H N N 59  
ARG   HB3  H N N 60  
ARG   HG2  H N N 61  
ARG   HG3  H N N 62  
ARG   HD2  H N N 63  
ARG   HD3  H N N 64  
ARG   HE   H N N 65  
ARG   HH11 H N N 66  
ARG   HH12 H N N 67  
ARG   HH21 H N N 68  
ARG   HH22 H N N 69  
ARG   HXT  H N N 70  
ASN   N    N N N 71  
ASN   CA   C N S 72  
ASN   C    C N N 73  
ASN   O    O N N 74  
ASN   CB   C N N 75  
ASN   CG   C N N 76  
ASN   OD1  O N N 77  
ASN   ND2  N N N 78  
ASN   OXT  O N N 79  
ASN   H    H N N 80  
ASN   H2   H N N 81  
ASN   HA   H N N 82  
ASN   HB2  H N N 83  
ASN   HB3  H N N 84  
ASN   HD21 H N N 85  
ASN   HD22 H N N 86  
ASN   HXT  H N N 87  
ASP   N    N N N 88  
ASP   CA   C N S 89  
ASP   C    C N N 90  
ASP   O    O N N 91  
ASP   CB   C N N 92  
ASP   CG   C N N 93  
ASP   OD1  O N N 94  
ASP   OD2  O N N 95  
ASP   OXT  O N N 96  
ASP   H    H N N 97  
ASP   H2   H N N 98  
ASP   HA   H N N 99  
ASP   HB2  H N N 100 
ASP   HB3  H N N 101 
ASP   HD2  H N N 102 
ASP   HXT  H N N 103 
CYS   N    N N N 104 
CYS   CA   C N R 105 
CYS   C    C N N 106 
CYS   O    O N N 107 
CYS   CB   C N N 108 
CYS   SG   S N N 109 
CYS   OXT  O N N 110 
CYS   H    H N N 111 
CYS   H2   H N N 112 
CYS   HA   H N N 113 
CYS   HB2  H N N 114 
CYS   HB3  H N N 115 
CYS   HG   H N N 116 
CYS   HXT  H N N 117 
EDO   C1   C N N 118 
EDO   O1   O N N 119 
EDO   C2   C N N 120 
EDO   O2   O N N 121 
EDO   H11  H N N 122 
EDO   H12  H N N 123 
EDO   HO1  H N N 124 
EDO   H21  H N N 125 
EDO   H22  H N N 126 
EDO   HO2  H N N 127 
GLN   N    N N N 128 
GLN   CA   C N S 129 
GLN   C    C N N 130 
GLN   O    O N N 131 
GLN   CB   C N N 132 
GLN   CG   C N N 133 
GLN   CD   C N N 134 
GLN   OE1  O N N 135 
GLN   NE2  N N N 136 
GLN   OXT  O N N 137 
GLN   H    H N N 138 
GLN   H2   H N N 139 
GLN   HA   H N N 140 
GLN   HB2  H N N 141 
GLN   HB3  H N N 142 
GLN   HG2  H N N 143 
GLN   HG3  H N N 144 
GLN   HE21 H N N 145 
GLN   HE22 H N N 146 
GLN   HXT  H N N 147 
GLU   N    N N N 148 
GLU   CA   C N S 149 
GLU   C    C N N 150 
GLU   O    O N N 151 
GLU   CB   C N N 152 
GLU   CG   C N N 153 
GLU   CD   C N N 154 
GLU   OE1  O N N 155 
GLU   OE2  O N N 156 
GLU   OXT  O N N 157 
GLU   H    H N N 158 
GLU   H2   H N N 159 
GLU   HA   H N N 160 
GLU   HB2  H N N 161 
GLU   HB3  H N N 162 
GLU   HG2  H N N 163 
GLU   HG3  H N N 164 
GLU   HE2  H N N 165 
GLU   HXT  H N N 166 
GLY   N    N N N 167 
GLY   CA   C N N 168 
GLY   C    C N N 169 
GLY   O    O N N 170 
GLY   OXT  O N N 171 
GLY   H    H N N 172 
GLY   H2   H N N 173 
GLY   HA2  H N N 174 
GLY   HA3  H N N 175 
GLY   HXT  H N N 176 
HIS   N    N N N 177 
HIS   CA   C N S 178 
HIS   C    C N N 179 
HIS   O    O N N 180 
HIS   CB   C N N 181 
HIS   CG   C Y N 182 
HIS   ND1  N Y N 183 
HIS   CD2  C Y N 184 
HIS   CE1  C Y N 185 
HIS   NE2  N Y N 186 
HIS   OXT  O N N 187 
HIS   H    H N N 188 
HIS   H2   H N N 189 
HIS   HA   H N N 190 
HIS   HB2  H N N 191 
HIS   HB3  H N N 192 
HIS   HD1  H N N 193 
HIS   HD2  H N N 194 
HIS   HE1  H N N 195 
HIS   HE2  H N N 196 
HIS   HXT  H N N 197 
HOH   O    O N N 198 
HOH   H1   H N N 199 
HOH   H2   H N N 200 
ILE   N    N N N 201 
ILE   CA   C N S 202 
ILE   C    C N N 203 
ILE   O    O N N 204 
ILE   CB   C N S 205 
ILE   CG1  C N N 206 
ILE   CG2  C N N 207 
ILE   CD1  C N N 208 
ILE   OXT  O N N 209 
ILE   H    H N N 210 
ILE   H2   H N N 211 
ILE   HA   H N N 212 
ILE   HB   H N N 213 
ILE   HG12 H N N 214 
ILE   HG13 H N N 215 
ILE   HG21 H N N 216 
ILE   HG22 H N N 217 
ILE   HG23 H N N 218 
ILE   HD11 H N N 219 
ILE   HD12 H N N 220 
ILE   HD13 H N N 221 
ILE   HXT  H N N 222 
LEU   N    N N N 223 
LEU   CA   C N S 224 
LEU   C    C N N 225 
LEU   O    O N N 226 
LEU   CB   C N N 227 
LEU   CG   C N N 228 
LEU   CD1  C N N 229 
LEU   CD2  C N N 230 
LEU   OXT  O N N 231 
LEU   H    H N N 232 
LEU   H2   H N N 233 
LEU   HA   H N N 234 
LEU   HB2  H N N 235 
LEU   HB3  H N N 236 
LEU   HG   H N N 237 
LEU   HD11 H N N 238 
LEU   HD12 H N N 239 
LEU   HD13 H N N 240 
LEU   HD21 H N N 241 
LEU   HD22 H N N 242 
LEU   HD23 H N N 243 
LEU   HXT  H N N 244 
LYS   N    N N N 245 
LYS   CA   C N S 246 
LYS   C    C N N 247 
LYS   O    O N N 248 
LYS   CB   C N N 249 
LYS   CG   C N N 250 
LYS   CD   C N N 251 
LYS   CE   C N N 252 
LYS   NZ   N N N 253 
LYS   OXT  O N N 254 
LYS   H    H N N 255 
LYS   H2   H N N 256 
LYS   HA   H N N 257 
LYS   HB2  H N N 258 
LYS   HB3  H N N 259 
LYS   HG2  H N N 260 
LYS   HG3  H N N 261 
LYS   HD2  H N N 262 
LYS   HD3  H N N 263 
LYS   HE2  H N N 264 
LYS   HE3  H N N 265 
LYS   HZ1  H N N 266 
LYS   HZ2  H N N 267 
LYS   HZ3  H N N 268 
LYS   HXT  H N N 269 
MET   N    N N N 270 
MET   CA   C N S 271 
MET   C    C N N 272 
MET   O    O N N 273 
MET   CB   C N N 274 
MET   CG   C N N 275 
MET   SD   S N N 276 
MET   CE   C N N 277 
MET   OXT  O N N 278 
MET   H    H N N 279 
MET   H2   H N N 280 
MET   HA   H N N 281 
MET   HB2  H N N 282 
MET   HB3  H N N 283 
MET   HG2  H N N 284 
MET   HG3  H N N 285 
MET   HE1  H N N 286 
MET   HE2  H N N 287 
MET   HE3  H N N 288 
MET   HXT  H N N 289 
PHE   N    N N N 290 
PHE   CA   C N S 291 
PHE   C    C N N 292 
PHE   O    O N N 293 
PHE   CB   C N N 294 
PHE   CG   C Y N 295 
PHE   CD1  C Y N 296 
PHE   CD2  C Y N 297 
PHE   CE1  C Y N 298 
PHE   CE2  C Y N 299 
PHE   CZ   C Y N 300 
PHE   OXT  O N N 301 
PHE   H    H N N 302 
PHE   H2   H N N 303 
PHE   HA   H N N 304 
PHE   HB2  H N N 305 
PHE   HB3  H N N 306 
PHE   HD1  H N N 307 
PHE   HD2  H N N 308 
PHE   HE1  H N N 309 
PHE   HE2  H N N 310 
PHE   HZ   H N N 311 
PHE   HXT  H N N 312 
PRO   N    N N N 313 
PRO   CA   C N S 314 
PRO   C    C N N 315 
PRO   O    O N N 316 
PRO   CB   C N N 317 
PRO   CG   C N N 318 
PRO   CD   C N N 319 
PRO   OXT  O N N 320 
PRO   H    H N N 321 
PRO   HA   H N N 322 
PRO   HB2  H N N 323 
PRO   HB3  H N N 324 
PRO   HG2  H N N 325 
PRO   HG3  H N N 326 
PRO   HD2  H N N 327 
PRO   HD3  H N N 328 
PRO   HXT  H N N 329 
SER   N    N N N 330 
SER   CA   C N S 331 
SER   C    C N N 332 
SER   O    O N N 333 
SER   CB   C N N 334 
SER   OG   O N N 335 
SER   OXT  O N N 336 
SER   H    H N N 337 
SER   H2   H N N 338 
SER   HA   H N N 339 
SER   HB2  H N N 340 
SER   HB3  H N N 341 
SER   HG   H N N 342 
SER   HXT  H N N 343 
SO4   S    S N N 344 
SO4   O1   O N N 345 
SO4   O2   O N N 346 
SO4   O3   O N N 347 
SO4   O4   O N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TRP   N    N N N 366 
TRP   CA   C N S 367 
TRP   C    C N N 368 
TRP   O    O N N 369 
TRP   CB   C N N 370 
TRP   CG   C Y N 371 
TRP   CD1  C Y N 372 
TRP   CD2  C Y N 373 
TRP   NE1  N Y N 374 
TRP   CE2  C Y N 375 
TRP   CE3  C Y N 376 
TRP   CZ2  C Y N 377 
TRP   CZ3  C Y N 378 
TRP   CH2  C Y N 379 
TRP   OXT  O N N 380 
TRP   H    H N N 381 
TRP   H2   H N N 382 
TRP   HA   H N N 383 
TRP   HB2  H N N 384 
TRP   HB3  H N N 385 
TRP   HD1  H N N 386 
TRP   HE1  H N N 387 
TRP   HE3  H N N 388 
TRP   HZ2  H N N 389 
TRP   HZ3  H N N 390 
TRP   HH2  H N N 391 
TRP   HXT  H N N 392 
TYR   N    N N N 393 
TYR   CA   C N S 394 
TYR   C    C N N 395 
TYR   O    O N N 396 
TYR   CB   C N N 397 
TYR   CG   C Y N 398 
TYR   CD1  C Y N 399 
TYR   CD2  C Y N 400 
TYR   CE1  C Y N 401 
TYR   CE2  C Y N 402 
TYR   CZ   C Y N 403 
TYR   OH   O N N 404 
TYR   OXT  O N N 405 
TYR   H    H N N 406 
TYR   H2   H N N 407 
TYR   HA   H N N 408 
TYR   HB2  H N N 409 
TYR   HB3  H N N 410 
TYR   HD1  H N N 411 
TYR   HD2  H N N 412 
TYR   HE1  H N N 413 
TYR   HE2  H N N 414 
TYR   HH   H N N 415 
TYR   HXT  H N N 416 
VAL   N    N N N 417 
VAL   CA   C N S 418 
VAL   C    C N N 419 
VAL   O    O N N 420 
VAL   CB   C N N 421 
VAL   CG1  C N N 422 
VAL   CG2  C N N 423 
VAL   OXT  O N N 424 
VAL   H    H N N 425 
VAL   H2   H N N 426 
VAL   HA   H N N 427 
VAL   HB   H N N 428 
VAL   HG11 H N N 429 
VAL   HG12 H N N 430 
VAL   HG13 H N N 431 
VAL   HG21 H N N 432 
VAL   HG22 H N N 433 
VAL   HG23 H N N 434 
VAL   HXT  H N N 435 
W0J   N1   N N N 436 
W0J   N3   N Y N 437 
W0J   C4   C N N 438 
W0J   C5   C N N 439 
W0J   C6   C Y N 440 
W0J   C7   C Y N 441 
W0J   C8   C Y N 442 
W0J   C    C N N 443 
W0J   N    N N N 444 
W0J   C1   C N R 445 
W0J   C3   C N N 446 
W0J   C2   C N N 447 
W0J   N2   N Y N 448 
W0J   C9   C Y N 449 
W0J   H1   H N N 450 
W0J   H2   H N N 451 
W0J   H3   H N N 452 
W0J   H4   H N N 453 
W0J   H5   H N N 454 
W0J   H6   H N N 455 
W0J   H7   H N N 456 
W0J   H8   H N N 457 
W0J   H9   H N N 458 
W0J   H10  H N N 459 
W0J   H12  H N N 460 
W0J   H13  H N N 461 
W0J   H14  H N N 462 
W0J   H15  H N N 463 
W0J   H16  H N N 464 
W0J   H17  H N N 465 
# 
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 
A1A39 N   C    sing N N 1   
A1A39 C1  N    sing N N 2   
A1A39 C1  C2   sing N N 3   
A1A39 C2  C3   sing N N 4   
A1A39 C3  C4   sing N N 5   
A1A39 C4  N1   sing N N 6   
A1A39 N1  C5   sing N N 7   
A1A39 C5  C1   sing N N 8   
A1A39 C6  N1   sing N N 9   
A1A39 C6  C7   sing Y N 10  
A1A39 C7  C8   doub Y N 11  
A1A39 C8  C9   sing Y N 12  
A1A39 C9  N2   doub Y N 13  
A1A39 N2  N3   sing Y N 14  
A1A39 N3  C6   doub Y N 15  
A1A39 C4  H10  sing N N 16  
A1A39 C4  H9   sing N N 17  
A1A39 C5  H11  sing N N 18  
A1A39 C5  H12  sing N N 19  
A1A39 C7  H13  sing N N 20  
A1A39 C8  H14  sing N N 21  
A1A39 C   H2   sing N N 22  
A1A39 C   H    sing N N 23  
A1A39 C   H1   sing N N 24  
A1A39 N   H3   sing N N 25  
A1A39 C1  H4   sing N N 26  
A1A39 C3  H7   sing N N 27  
A1A39 C3  H8   sing N N 28  
A1A39 C2  H5   sing N N 29  
A1A39 C2  H6   sing N N 30  
A1A39 C9  H15  sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
EDO   C1  O1   sing N N 114 
EDO   C1  C2   sing N N 115 
EDO   C1  H11  sing N N 116 
EDO   C1  H12  sing N N 117 
EDO   O1  HO1  sing N N 118 
EDO   C2  O2   sing N N 119 
EDO   C2  H21  sing N N 120 
EDO   C2  H22  sing N N 121 
EDO   O2  HO2  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
SO4   S   O1   doub N N 330 
SO4   S   O2   doub N N 331 
SO4   S   O3   sing N N 332 
SO4   S   O4   sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
W0J   C8  C9   doub Y N 420 
W0J   C8  C7   sing Y N 421 
W0J   C2  C1   sing N N 422 
W0J   C2  C3   sing N N 423 
W0J   C9  N2   sing Y N 424 
W0J   C7  C6   doub Y N 425 
W0J   C1  C5   sing N N 426 
W0J   C1  N    sing N N 427 
W0J   N2  N3   doub Y N 428 
W0J   C6  N3   sing Y N 429 
W0J   C6  N1   sing N N 430 
W0J   C5  N1   sing N N 431 
W0J   N1  C4   sing N N 432 
W0J   C   N    sing N N 433 
W0J   C3  C4   sing N N 434 
W0J   C4  H1   sing N N 435 
W0J   C4  H2   sing N N 436 
W0J   C5  H3   sing N N 437 
W0J   C5  H4   sing N N 438 
W0J   C7  H5   sing N N 439 
W0J   C8  H6   sing N N 440 
W0J   C   H7   sing N N 441 
W0J   C   H8   sing N N 442 
W0J   C   H9   sing N N 443 
W0J   N   H10  sing N N 444 
W0J   C1  H12  sing N N 445 
W0J   C3  H13  sing N N 446 
W0J   C3  H14  sing N N 447 
W0J   C2  H15  sing N N 448 
W0J   C2  H16  sing N N 449 
W0J   C9  H17  sing N N 450 
# 
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                    7HH4 
_atom_sites.fract_transf_matrix[1][1]   0.023975 
_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]   0.023635 
_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]   0.006277 
_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  ? 1.008   4.232   2.411   1.00 49.70  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.094  3.502   1.726   1.00 51.25  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.486   2.442   0.789   1.00 47.89  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.575   2.615   0.248   1.00 48.66  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.029  4.454   0.969   1.00 56.99  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.048  5.175   1.852   1.00 70.22  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.409  4.239   2.596   1.00 72.47  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.093  5.497   3.685   1.00 77.23  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.209  1.297   0.605   1.00 42.33  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.257   0.205   -0.262  1.00 41.58  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.454   0.542   -1.738  1.00 38.65  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.276  1.337   -2.320  1.00 41.95  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -0.924  -0.806  -0.088  1.00 41.39  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.402  -0.537  1.331   1.00 44.68  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.479  0.974   1.284   1.00 42.17  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.417   -0.132  -2.357  1.00 34.21  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.594   -0.015  -3.785  1.00 35.02  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.064   -1.310  -4.384  1.00 32.27  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.576   -2.170  -3.650  1.00 31.65  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.095   0.100   -4.083  1.00 43.82  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.725   1.361   -3.578  1.00 57.63  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 4.013   1.601   -2.251  1.00 62.12  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.112   2.461   -4.241  1.00 62.93  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.542   2.810   -2.130  1.00 66.35  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.613   3.352   -3.326  1.00 61.16  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.099   -1.443  -5.705  1.00 28.92  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.908   -2.752  -6.306  1.00 26.42  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 2.062   -3.683  -5.948  1.00 26.35  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.142   -3.229  -5.520  1.00 27.40  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.801   -2.617  -7.814  1.00 32.55  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.759   -4.974  -6.067  1.00 25.03  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.765   -6.020  -5.934  1.00 25.88  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.908   -5.759  -6.918  1.00 28.57  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.694   -5.307  -8.050  1.00 29.14  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.217   -7.455  -6.001  1.00 25.55  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.419   -7.788  -4.745  1.00 26.34  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.074   -8.006  -3.542  1.00 23.17  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.023   -7.943  -4.782  1.00 24.36  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.406   -8.311  -2.360  1.00 23.16  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.645  -8.298  -3.606  1.00 22.77  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.025   -8.473  -2.416  1.00 24.73  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.129   -6.041  -6.437  1.00 22.84  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.293   -5.978  -7.319  1.00 24.45  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.208   -7.172  -7.015  1.00 23.22  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.188   -7.764  -5.930  1.00 22.09  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 7.042   -4.664  -7.065  1.00 27.91  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.680   -4.552  -5.720  1.00 29.19  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.421   -3.231  -5.439  1.00 36.64  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 9.004   -3.194  -4.031  1.00 36.20  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 8.000   -3.231  -2.945  1.00 35.67  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.119   -7.555  -7.932  1.00 23.35  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 9.060   -8.647  -7.689  1.00 23.75  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.863   -8.387  -6.424  1.00 20.91  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.320  -7.266  -6.169  1.00 22.75  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.982   -8.559  -8.968  1.00 24.62  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 9.011   -8.010  -10.018 1.00 26.81  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.271   -6.926  -9.274  1.00 26.19  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.021  -9.442  -5.617  1.00 20.74  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.727  -9.352  -4.357  1.00 21.05  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.796   -9.218  -3.161  1.00 21.94  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.199  -9.473  -2.026  1.00 22.92  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.548   -8.796  -3.409  1.00 18.68  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.637   -8.775  -2.272  1.00 17.92  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.395   -10.168 -1.666  1.00 17.80  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.276   -11.154 -2.365  1.00 18.78  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.301   -8.172  -2.685  1.00 20.23  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.315   -6.670  -2.900  1.00 23.72  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.246   -5.987  -2.417  1.00 24.79  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.330   -6.138  -3.506  1.00 23.49  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.275   -10.215 -0.314  1.00 19.38  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.115   -11.465 0.417   1.00 17.27  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.650   -11.548 0.833   1.00 18.85  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.097   -10.521 1.271   1.00 21.22  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.046   -11.467 1.650   1.00 19.02  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.534   -11.287 1.291   1.00 19.52  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.375  -11.383 2.571   1.00 21.00  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.997   -12.273 0.232   1.00 23.20  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 5.101   -12.750 0.679   1.00 18.77  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.656   -12.968 0.912   1.00 18.62  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.425   -14.335 1.546   1.00 19.62  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.286   -15.206 1.620   1.00 20.11  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.826   -12.882 -0.376  1.00 18.58  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.961   -11.511 -1.031  1.00 20.74  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.303   -13.927 -1.391  1.00 20.36  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.173   -14.537 2.052   1.00 18.67  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.599   -15.860 2.074   1.00 19.89  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.622   -15.927 0.901   1.00 20.18  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.147  -14.973 0.686   1.00 21.17  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.831   -16.254 3.373   1.00 20.82  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.771   -16.330 4.556   1.00 20.65  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.086   -15.147 5.220   1.00 22.12  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.299   -17.568 4.974   1.00 22.60  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.996   -15.202 6.299   1.00 28.21  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.230   -17.605 6.029   1.00 23.70  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.521   -16.441 6.679   1.00 24.43  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.731   -17.020 0.132   1.00 19.33  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.037  -17.196 -1.095  1.00 21.37  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.022  -18.341 -0.887  1.00 22.92  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.640  -19.390 -0.372  1.00 23.34  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.872   -17.439 -2.297  1.00 21.52  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.297  -18.122 -1.276  1.00 21.92  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.304  -19.159 -1.056  1.00 24.33  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.626  -19.878 -2.365  1.00 25.37  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.006  -19.244 -3.340  1.00 26.99  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.543  -18.485 -0.433  1.00 23.87  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.669  -19.498 -0.058  1.00 27.64  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.213  -20.386 1.106   1.00 31.89  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.304  -21.201 1.752   1.00 33.42  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.626  -22.337 0.884   1.00 36.44  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.591  -21.223 -2.300  1.00 26.57  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.080  -22.069 -3.371  1.00 29.24  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.150  -22.988 -2.769  1.00 32.26  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.095  -23.290 -1.592  1.00 27.46  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -2.937  -22.993 -3.781  1.00 35.12  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.851  -23.106 -5.265  1.00 55.01  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.686  -21.880 -5.892  1.00 34.76  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.273  -23.340 -6.801  1.00 34.25  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.079  -23.419 -3.623  1.00 35.89  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.122  -24.366 -3.251  1.00 39.23  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.522  -25.592 -2.581  1.00 33.70  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.576  -26.199 -3.084  1.00 36.50  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -7.707  -24.854 -4.581  1.00 40.00  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.059  -25.564 -4.410  1.00 46.96  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.128 -24.611 -3.877  1.00 57.01  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.052  -25.965 -1.406  1.00 38.66  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -6.646  -27.230 -0.836  1.00 32.51  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.341  -27.119 -0.052  1.00 39.35  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -4.883  -28.083 0.548   1.00 43.48  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -4.724  -25.928 -0.047  1.00 33.57  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.480  -25.792 0.683   1.00 32.24  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.572  -24.641 1.673   1.00 28.25  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.327  -23.689 1.456   1.00 28.02  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.365  -25.383 -0.281  1.00 36.09  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -1.942  -26.431 -1.298  1.00 42.40  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -0.929  -27.330 -1.010  1.00 56.42  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.532  -26.481 -2.559  1.00 47.90  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.526  -28.269 -1.947  1.00 57.41  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -2.124  -27.403 -3.515  1.00 53.62  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -1.109  -28.294 -3.204  1.00 60.11  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.685  -29.221 -4.121  1.00 73.45  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -2.800  -24.703 2.776   1.00 28.10  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -2.747  -23.630 3.783   1.00 28.18  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.067  -22.428 3.108   1.00 25.44  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.298  -22.647 2.182   1.00 27.42  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -1.868  -24.231 4.924   1.00 32.87  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.061  -25.331 4.243   1.00 32.79  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -1.918  -25.852 3.099   1.00 32.54  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.363  -21.225 3.581   1.00 24.70  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.657  -19.999 3.173   1.00 22.53  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.155  -20.252 3.294   1.00 26.44  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? 0.278   -20.699 4.347   1.00 25.15  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.097  -18.825 4.056   1.00 24.49  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.534  -18.423 3.835   1.00 25.09  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.555  -19.070 4.507   1.00 29.73  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.111  -17.447 3.086   1.00 26.37  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -5.715  -18.524 4.154   1.00 31.19  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.492  -17.522 3.323   1.00 30.91  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.604   -20.044 2.183   1.00 22.59  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.919   -20.669 2.058   1.00 22.16  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.989   -19.584 1.919   1.00 21.35  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.834   -18.701 1.082   1.00 20.94  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.955   -21.541 0.808   1.00 22.92  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 3.053   -22.576 0.857   1.00 22.90  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.409   -22.415 0.684   1.00 24.63  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.852   -23.969 1.186   1.00 25.84  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 5.043   -23.645 0.817   1.00 24.88  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 4.119   -24.599 1.157   1.00 27.32  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.736   -24.747 1.516   1.00 31.23  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 4.296   -25.964 1.429   1.00 32.82  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.914   -26.094 1.781   1.00 31.92  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 3.178   -26.695 1.737   1.00 34.33  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 4.147   -19.658 2.624   1.00 21.23  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 5.196   -18.639 2.458   1.00 20.16  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.726   -18.582 1.009   1.00 19.93  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 6.036   -19.625 0.425   1.00 20.41  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 6.272   -19.120 3.470   1.00 21.28  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 6.111   -20.620 3.554   1.00 19.14  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.542   -20.736 3.564   1.00 21.82  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.771   -17.380 0.425   1.00 18.12  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 6.112   -17.279 -0.989  1.00 18.81  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.632   -15.875 -1.294  1.00 18.68  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.607   -14.978 -0.475  1.00 18.35  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.855   -17.598 -1.844  1.00 20.43  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 7.117   -15.698 -2.520  1.00 18.94  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.562   -14.380 -2.962  1.00 18.83  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 7.050   -14.108 -4.385  1.00 18.03  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.757   -15.085 -5.116  1.00 19.65  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 9.090   -14.235 -2.920  1.00 20.02  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.776   -15.095 -3.966  1.00 19.48  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 11.340  -14.911 -3.778  1.00 19.03  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.976  -15.739 -4.835  1.00 20.87  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 13.258  -16.150 -4.715  1.00 22.02  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.948  -16.003 -3.576  1.00 23.16  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.829  -16.775 -5.756  1.00 24.46  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.889   -12.822 -4.722  1.00 18.54  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.669   -12.456 -6.132  1.00 18.73  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.995   -12.580 -6.855  1.00 21.46  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.942   -11.937 -6.441  1.00 21.78  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 6.193   -11.003 -6.233  1.00 20.21  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 5.058   -10.691 -5.245  1.00 26.60  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.826   -10.657 -7.703  1.00 22.23  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.707   -11.264 -5.582  1.00 29.61  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 8.041   -13.424 -7.865  1.00 21.23  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 9.278   -13.607 -8.631  1.00 22.19  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.398   -12.582 -9.754  1.00 25.13  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.465   -11.937 -10.192 1.00 24.55  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.395   -14.996 -9.211  1.00 22.16  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.386  -15.938 -8.526  1.00 23.98  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.966  -15.531 -7.472  1.00 29.14  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.534  -17.067 -8.947  1.00 26.97  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.642  -12.430 -10.247 1.00 26.92  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.859  -11.744 -11.504 1.00 32.81  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.586  -12.737 -12.641 1.00 29.87  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.426  -13.932 -12.426 1.00 31.38  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.328  -11.332 -11.627 1.00 34.29  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.789  -10.074 -10.891 1.00 43.24  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.462  -8.958  -11.344 1.00 46.12  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.513  -10.211 -9.881  1.00 50.82  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 10.521  -12.242 -13.873 1.00 32.64  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 10.446  -13.157 -15.011 1.00 30.91  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.769  -12.927 -15.736 1.00 27.51  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 12.094  -11.783 -15.981 1.00 31.33  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 9.258   -12.714 -15.884 1.00 32.94  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.924   -12.764 -15.098 1.00 32.12  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 9.202   -13.507 -17.187 1.00 32.03  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.884   -11.807 -15.631 1.00 36.79  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.539  -14.007 -15.916 1.00 31.25  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.828  -13.956 -16.611 1.00 29.17  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.616  -13.594 -18.089 1.00 29.53  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.581  -13.897 -18.684 1.00 31.31  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.502  -15.305 -16.478 1.00 32.69  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.575  -12.864 -18.669 1.00 30.17  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.580  -12.725 -20.129 1.00 29.62  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.405  -14.105 -20.751 1.00 27.02  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 15.026  -15.083 -20.352 1.00 32.04  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.904  -12.101 -20.559 1.00 31.02  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 16.059  -10.616 -20.326 1.00 37.09  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 15.040  -9.961  -20.170 1.00 37.31  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 17.229  -10.128 -20.319 1.00 35.90  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.493  -14.165 -21.728 1.00 28.32  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 13.268  -15.357 -22.515 1.00 28.92  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 12.338  -16.380 -21.884 1.00 31.28  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 12.029  -17.376 -22.517 1.00 35.49  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.935  -16.149 -20.624 1.00 29.02  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 11.095  -17.110 -19.916 1.00 31.16  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.606   -16.812 -20.145 1.00 28.59  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 9.171   -15.726 -20.545 1.00 30.10  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 11.450  -17.013 -18.439 1.00 32.16  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.788   -17.843 -19.863 1.00 33.54  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 7.342   -17.741 -20.035 1.00 33.26  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.749   -16.720 -19.058 1.00 32.88  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 7.032   -16.785 -17.863 1.00 32.30  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.787   -19.142 -19.683 1.00 36.02  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 5.264   -19.108 -19.554 1.00 37.21  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 7.223   -20.194 -20.694 1.00 39.72  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.933   -15.810 -19.591 1.00 32.14  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 5.282   -14.737 -18.846 1.00 34.04  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.967   -15.232 -18.266 1.00 36.18  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 3.324   -16.131 -18.799 1.00 37.97  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.936   -13.518 -19.700 1.00 34.66  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 6.174   -12.782 -20.224 1.00 38.90  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.940   -11.492 -21.007 1.00 46.05  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.385   -11.813 -22.364 1.00 47.77  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 5.374   -10.623 -23.204 1.00 46.07  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.495   -14.604 -17.170 1.00 35.54  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 2.231   -15.025 -16.571 1.00 34.20  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 1.081   -14.564 -17.455 1.00 34.05  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 1.209   -13.623 -18.221 1.00 35.04  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 2.186   -14.337 -15.187 1.00 35.30  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 3.170   -13.173 -15.292 1.00 38.84  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 4.088   -13.423 -16.524 1.00 33.52  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.136  -15.096 -17.240 1.00 33.92  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.322  -14.475 -17.840 1.00 39.38  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.521  -13.034 -17.377 1.00 41.71  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.041  -12.670 -16.306 1.00 32.85  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.479  -15.371 -17.351 1.00 36.52  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -1.843  -16.661 -16.872 1.00 35.21  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.413  -16.317 -16.460 1.00 37.03  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.287  -12.170 -18.097 1.00 36.33  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -2.689  -10.859 -17.572 1.00 39.30  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.281  -10.915 -16.167 1.00 31.76  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -3.999  -11.855 -15.829 1.00 37.49  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -3.719  -10.283 -18.588 1.00 43.63  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -3.997  -11.446 -19.485 1.00 37.99  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -2.820  -12.416 -19.459 1.00 46.12  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -2.959  -9.865  -15.396 1.00 33.56  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.408  -9.627  -14.048 1.00 36.89  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -2.896  -10.698 -13.091 1.00 32.13  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.400  -10.750 -11.971 1.00 32.31  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -4.933  -9.580  -14.000 1.00 42.76  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.424  -8.460  -14.889 1.00 52.21  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.196  -7.282  -14.576 1.00 50.90  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.036  -8.807  -16.010 1.00 53.41  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -1.965  -11.564 -13.540 1.00 28.93  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.425  -12.598 -12.645 1.00 23.74  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? 0.078   -12.354 -12.433 1.00 24.65  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.748   -11.671 -13.228 1.00 27.08  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.542  -14.041 -13.135 1.00 26.63  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -2.955  -14.547 -13.538 1.00 30.72  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -3.839  -14.214 -12.345 1.00 32.88  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.315  -14.432 -12.675 1.00 45.44  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.575  -15.874 -12.697 1.00 46.18  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.563   -12.822 -11.274 1.00 21.77  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.953   -12.681 -10.883 1.00 23.18  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.581   -14.061 -10.794 1.00 21.23  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.972   -15.049 -10.411 1.00 21.38  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 2.072   -12.066 -9.458  1.00 22.35  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.571   -10.630 -9.471  1.00 24.23  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? 0.211   -10.366 -9.316  1.00 28.33  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.418   -9.552  -9.645  1.00 25.96  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.303  -9.083  -9.445  1.00 30.33  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.924   -8.246  -9.702  1.00 29.37  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.561   -8.017  -9.590  1.00 32.39  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.000  -6.770  -9.756  1.00 31.09  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.909   -14.203 -11.069 1.00 20.62  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.585   -15.478 -10.847 1.00 21.15  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.955   -15.595 -9.371  1.00 21.03  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.627   -14.689 -8.865  1.00 22.46  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.845   -15.331 -11.749 1.00 23.02  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 6.054   -13.875 -11.906 1.00 23.34  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.756   -13.116 -11.590 1.00 23.48  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.387   -16.609 -8.714  1.00 20.95  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.595   -16.781 -7.275  1.00 20.28  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.526   -17.974 -7.077  1.00 21.86  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 5.249   -19.134 -7.518  1.00 22.99  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 3.237   -17.029 -6.599  1.00 19.86  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 2.260   -15.893 -6.887  1.00 22.68  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.528   -17.218 -5.094  1.00 20.73  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.796   -14.513 -6.508  1.00 23.00  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.660   -17.719 -6.382  1.00 18.88  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.558   -18.782 -6.032  1.00 21.00  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 7.285   -19.185 -4.587  1.00 20.90  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 7.346   -18.336 -3.676  1.00 21.00  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 9.013   -18.285 -6.216  1.00 21.69  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 10.016  -19.332 -5.776  1.00 22.62  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.408  -20.350 -6.663  1.00 24.85  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.623  -19.267 -4.504  1.00 24.50  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 11.336  -21.305 -6.242  1.00 25.84  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.541  -20.246 -4.106  1.00 26.88  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.903  -21.237 -4.992  1.00 27.07  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.961   -20.463 -4.404  1.00 21.17  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.593   -21.005 -3.112  1.00 21.44  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.830   -21.514 -2.387  1.00 23.11  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.524   -22.405 -2.914  1.00 22.63  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.574   -22.139 -3.327  1.00 24.78  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 4.203   -21.609 -3.727  1.00 21.62  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.864   -21.430 -5.055  1.00 26.54  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 3.236   -21.350 -2.753  1.00 25.60  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.597   -20.931 -5.403  1.00 26.53  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.988   -20.864 -3.104  1.00 24.69  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.683   -20.651 -4.419  1.00 26.48  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 8.101   -20.921 -1.227  1.00 21.22  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 9.260   -21.390 -0.450  1.00 21.17  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 9.053   -22.843 -0.001  1.00 23.46  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.929   -23.330 0.134   1.00 23.99  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.521   -20.451 0.736   1.00 22.05  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.987   -19.079 0.299   1.00 19.58  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 11.276  -18.902 -0.238  1.00 18.97  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 9.255   -17.923 0.589   1.00 20.82  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.678  -17.621 -0.584  1.00 18.88  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.682   -16.644 0.264   1.00 18.20  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.928  -16.494 -0.332  1.00 19.87  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 10.164  -23.556 0.207   1.00 23.05  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 10.064  -24.929 0.712   1.00 23.92  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.835   -25.922 -0.443  1.00 29.25  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.701  -26.740 -0.752  1.00 31.41  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.696   -25.846 -1.141  1.00 28.25  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.457   -26.697 -2.302  1.00 27.77  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 9.250   -26.218 -3.528  1.00 28.15  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.537   -26.966 -4.471  1.00 28.34  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.958   -26.747 -2.623  1.00 31.26  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.536   -25.463 -3.081  1.00 29.74  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 6.100   -27.224 -1.479  1.00 31.51  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.569   -24.920 -3.588  1.00 24.21  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 10.243  -24.323 -4.722  1.00 25.13  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.421   -24.429 -6.006  1.00 25.63  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.984   -24.402 -7.085  1.00 28.92  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.699  -24.808 -4.885  1.00 24.62  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.388  -24.845 -3.558  1.00 27.03  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 13.246  -25.872 -3.199  1.00 30.15  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.452  -23.943 -2.545  1.00 26.05  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.717  -25.639 -1.980  1.00 36.56  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 13.295  -24.451 -1.572  1.00 29.05  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 8.089   -24.497 -5.858  1.00 27.21  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 7.230   -24.524 -7.036  1.00 27.01  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.795   -23.118 -7.453  1.00 26.05  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.946   -22.145 -6.695  1.00 25.45  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.989   -25.356 -6.758  1.00 31.37  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 6.327   -26.807 -6.419  1.00 42.30  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 5.150   -27.608 -5.892  1.00 55.85  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 4.366   -27.116 -5.057  1.00 61.01  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 5.064   -28.779 -6.283  1.00 71.53  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 6.342   -22.973 -8.705  1.00 25.68  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.836   -21.690 -9.168  1.00 24.29  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.387   -21.890 -9.593  1.00 26.21  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 4.071   -22.889 -10.262 1.00 28.81  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.632   -21.157 -10.368 1.00 29.30  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.926   -20.760 -9.919  1.00 28.40  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 6.071   -19.875 -10.973 1.00 30.01  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.499   -20.956 -9.222  1.00 25.55  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 2.162   -20.870 -9.790  1.00 24.21  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.836   -19.417 -10.097 1.00 24.35  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.501   -18.475 -9.641  1.00 25.51  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 1.141   -21.456 -8.846  1.00 26.40  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.820   -19.170 -10.938 1.00 24.12  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.457   -17.811 -11.285 1.00 24.16  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -0.812  -17.450 -10.524 1.00 27.51  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -1.812  -18.172 -10.562 1.00 30.94  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? 0.140   -17.783 -12.786 1.00 27.01  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 1.327   -18.170 -13.631 1.00 28.21  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.518   -17.448 -13.551 1.00 35.08  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 1.220   -19.208 -14.546 1.00 35.77  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.613   -17.780 -14.354 1.00 41.93  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 2.318   -19.547 -15.320 1.00 36.09  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.494   -18.825 -15.252 1.00 35.19  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -0.766  -16.360 -9.753  1.00 22.62  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -1.882  -16.012 -8.877  1.00 21.68  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.168  -14.523 -8.985  1.00 22.72  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.302  -13.718 -9.346  1.00 23.01  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.507  -16.300 -7.421  1.00 23.35  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.467  -17.784 -7.069  1.00 25.23  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.110  -17.882 -5.577  1.00 25.27  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -2.883  -18.380 -7.361  1.00 29.07  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.441  -14.161 -8.690  1.00 21.49  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -3.774  -12.745 -8.639  1.00 21.40  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -3.780  -12.246 -7.176  1.00 19.15  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -3.727  -13.070 -6.237  1.00 19.42  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -3.884  -10.926 -6.986  1.00 21.08  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -3.804  -10.317 -5.652  1.00 20.82  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -4.790  -10.844 -4.614  1.00 21.99  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.515  -10.791 -3.422  1.00 21.43  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.073  -8.833  -5.954  1.00 22.57  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.459  -8.624  -7.343  1.00 23.41  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -3.801  -9.911  -8.057  1.00 22.52  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -5.944  -11.372 -5.092  1.00 22.43  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -6.895  -11.892 -4.107  1.00 21.49  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.361  -13.064 -3.271  1.00 22.40  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -6.805  -13.322 -2.151  1.00 22.24  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.175  -12.422 -4.770  1.00 25.57  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -7.989  -13.657 -5.612  1.00 29.98  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.329  -14.023 -6.261  1.00 34.67  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.224  -15.271 -7.069  1.00 38.24  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.021  -16.454 -6.224  1.00 42.03  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.285  -13.743 -3.773  1.00 19.27  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -4.731  -14.883 -3.079  1.00 22.33  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.368  -14.517 -2.464  1.00 20.57  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -2.689  -15.429 -2.011  1.00 22.31  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.625  -16.078 -4.025  1.00 23.62  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.004  -16.647 -4.376  1.00 24.80  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -6.833  -16.733 -3.412  1.00 27.83  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.202  -16.989 -5.533  1.00 28.81  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.021  -13.223 -2.449  1.00 19.77  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -1.708  -12.769 -1.953  1.00 19.12  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -1.876  -11.910 -0.701  1.00 16.67  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.446  -10.808 -0.736  1.00 19.85  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -0.968  -12.030 -3.067  1.00 21.24  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -0.847  -12.826 -4.356  1.00 20.61  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.173  -11.948 -5.415  1.00 22.13  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.041  -14.092 -4.194  1.00 21.07  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.261  -12.381 0.391   1.00 18.97  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.339  -11.717 1.707   1.00 20.04  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? 0.039   -11.211 2.093   1.00 22.22  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.936   -12.030 2.305   1.00 23.77  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -1.836  -12.742 2.735   1.00 20.00  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.272  -13.192 2.472   1.00 21.03  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.552  -14.140 1.497   1.00 21.89  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.277  -12.621 3.252   1.00 23.17  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -4.880  -14.452 1.175   1.00 25.09  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.587  -12.982 2.949   1.00 23.44  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -5.850  -13.905 1.969   1.00 24.52  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? 0.268   -9.900  2.229   1.00 24.30  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.621   -9.407  2.550   1.00 22.56  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 2.156   -10.046 3.825   1.00 22.13  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.452   -10.257 4.832   1.00 23.22  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.368   -7.896  2.701   1.00 24.95  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? 0.264   -7.607  1.641   1.00 26.47  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -0.656  -8.804  1.876   1.00 25.11  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.462   -10.440 3.806   1.00 22.55  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 4.012   -11.322 4.830   1.00 20.74  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 4.092   -10.688 6.238   1.00 21.20  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.664   -11.368 7.187   1.00 26.01  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.412   -11.745 4.322   1.00 22.91  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 6.217   -12.536 5.344   1.00 22.03  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.925   -13.868 5.653   1.00 23.21  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 7.245   -11.904 6.031   1.00 27.41  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.618   -14.589 6.629   1.00 24.76  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.964   -12.628 6.968   1.00 27.29  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.667   -13.942 7.264   1.00 26.53  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.394   -14.677 8.224   1.00 28.39  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.426   -9.409  6.264   1.00 25.08  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.605   -8.712  7.553   1.00 28.48  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 3.278   -8.693  8.310   1.00 26.88  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 3.236   -9.201  9.429   1.00 35.00  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.298   -7.372  7.410   1.00 28.96  ? 62  ASP   A CB  1 
ATOM   495  N N   . LYS   A 1 64 ? 2.215   -8.251  7.614   1.00 30.33  ? 63  LYS   A N   1 
ATOM   496  C CA  . LYS   A 1 64 ? 0.887   -8.153  8.234   1.00 30.11  ? 63  LYS   A CA  1 
ATOM   497  C C   . LYS   A 1 64 ? 0.389   -9.533  8.665   1.00 30.57  ? 63  LYS   A C   1 
ATOM   498  O O   . LYS   A 1 64 ? -0.306  -9.670  9.675   1.00 29.37  ? 63  LYS   A O   1 
ATOM   499  C CB  . LYS   A 1 64 ? -0.043  -7.547  7.176   1.00 29.96  ? 63  LYS   A CB  1 
ATOM   500  C CG  . LYS   A 1 64 ? -1.494  -7.366  7.653   1.00 33.99  ? 63  LYS   A CG  1 
ATOM   501  C CD  . LYS   A 1 64 ? -2.279  -6.652  6.554   1.00 34.42  ? 63  LYS   A CD  1 
ATOM   502  C CE  . LYS   A 1 64 ? -3.489  -5.962  7.076   1.00 39.57  ? 63  LYS   A CE  1 
ATOM   503  N NZ  . LYS   A 1 64 ? -4.397  -6.947  7.647   1.00 48.53  ? 63  LYS   A NZ  1 
ATOM   504  N N   . SER   A 1 65 ? 0.702   -10.587 7.891   1.00 26.46  ? 64  SER   A N   1 
ATOM   505  C CA  . SER   A 1 65 ? 0.042   -11.876 7.980   1.00 25.74  ? 64  SER   A CA  1 
ATOM   506  C C   . SER   A 1 65 ? 0.797   -12.949 8.776   1.00 27.53  ? 64  SER   A C   1 
ATOM   507  O O   . SER   A 1 65 ? 0.246   -14.037 8.963   1.00 29.17  ? 64  SER   A O   1 
ATOM   508  C CB  . SER   A 1 65 ? -0.273  -12.451 6.584   1.00 28.11  ? 64  SER   A CB  1 
ATOM   509  O OG  . SER   A 1 65 ? -1.042  -11.485 5.873   1.00 35.36  ? 64  SER   A OG  1 
ATOM   510  N N   . LYS   A 1 66 ? 2.073   -12.711 9.132   1.00 27.97  ? 65  LYS   A N   1 
ATOM   511  C CA  . LYS   A 1 66 ? 2.861   -13.836 9.625   1.00 28.98  ? 65  LYS   A CA  1 
ATOM   512  C C   . LYS   A 1 66 ? 2.405   -14.346 10.990  1.00 30.39  ? 65  LYS   A C   1 
ATOM   513  O O   . LYS   A 1 66 ? 2.527   -15.539 11.270  1.00 31.74  ? 65  LYS   A O   1 
ATOM   514  C CB  . LYS   A 1 66 ? 4.356   -13.521 9.599   1.00 30.36  ? 65  LYS   A CB  1 
ATOM   515  C CG  . LYS   A 1 66 ? 4.719   -12.360 10.482  1.00 30.86  ? 65  LYS   A CG  1 
ATOM   516  C CD  . LYS   A 1 66 ? 6.207   -12.151 10.193  1.00 41.08  ? 65  LYS   A CD  1 
ATOM   517  C CE  . LYS   A 1 66 ? 6.796   -11.320 11.294  1.00 45.56  ? 65  LYS   A CE  1 
ATOM   518  N NZ  . LYS   A 1 66 ? 6.444   -9.915  11.071  1.00 57.53  ? 65  LYS   A NZ  1 
ATOM   519  N N   A ASP   A 1 67 ? 1.851   -13.447 11.810  0.50 33.87  ? 66  ASP   A N   1 
ATOM   520  N N   B ASP   A 1 67 ? 1.876   -13.442 11.817  0.50 33.11  ? 66  ASP   A N   1 
ATOM   521  C CA  A ASP   A 1 67 ? 1.344   -13.849 13.113  0.50 36.58  ? 66  ASP   A CA  1 
ATOM   522  C CA  B ASP   A 1 67 ? 1.335   -13.856 13.101  0.50 35.30  ? 66  ASP   A CA  1 
ATOM   523  C C   A ASP   A 1 67 ? 0.239   -14.894 12.963  0.50 35.21  ? 66  ASP   A C   1 
ATOM   524  C C   B ASP   A 1 67 ? 0.315   -14.971 12.890  0.50 34.74  ? 66  ASP   A C   1 
ATOM   525  O O   A ASP   A 1 67 ? 0.111   -15.789 13.785  0.50 34.26  ? 66  ASP   A O   1 
ATOM   526  O O   B ASP   A 1 67 ? 0.334   -15.988 13.575  0.50 36.05  ? 66  ASP   A O   1 
ATOM   527  C CB  A ASP   A 1 67 ? 0.941   -12.642 13.943  0.50 39.40  ? 66  ASP   A CB  1 
ATOM   528  C CB  B ASP   A 1 67 ? 0.734   -12.668 13.828  0.50 35.59  ? 66  ASP   A CB  1 
ATOM   529  C CG  A ASP   A 1 67 ? 2.090   -11.876 14.584  0.50 42.63  ? 66  ASP   A CG  1 
ATOM   530  C CG  B ASP   A 1 67 ? 0.200   -12.948 15.224  0.50 38.95  ? 66  ASP   A CG  1 
ATOM   531  O OD1 A ASP   A 1 67 ? 3.229   -12.389 14.568  0.50 45.12  ? 66  ASP   A OD1 1 
ATOM   532  O OD1 B ASP   A 1 67 ? 1.012   -13.323 16.105  0.50 40.94  ? 66  ASP   A OD1 1 
ATOM   533  O OD2 A ASP   A 1 67 ? 1.844   -10.767 15.092  0.50 44.97  ? 66  ASP   A OD2 1 
ATOM   534  O OD2 B ASP   A 1 67 ? -1.024  -12.769 15.415  0.50 42.19  ? 66  ASP   A OD2 1 
ATOM   535  N N   . LYS   A 1 68 ? -0.570  -14.784 11.905  1.00 30.64  ? 67  LYS   A N   1 
ATOM   536  C CA  . LYS   A 1 68 ? -1.650  -15.719 11.697  1.00 28.85  ? 67  LYS   A CA  1 
ATOM   537  C C   . LYS   A 1 68 ? -1.185  -16.961 10.961  1.00 30.05  ? 67  LYS   A C   1 
ATOM   538  O O   . LYS   A 1 68 ? -1.671  -18.068 11.217  1.00 35.08  ? 67  LYS   A O   1 
ATOM   539  C CB  . LYS   A 1 68 ? -2.693  -14.947 10.887  1.00 30.52  ? 67  LYS   A CB  1 
ATOM   540  C CG  . LYS   A 1 68 ? -3.967  -15.689 10.713  1.00 31.09  ? 67  LYS   A CG  1 
ATOM   541  C CD  . LYS   A 1 68 ? -4.980  -14.780 10.009  1.00 35.04  ? 67  LYS   A CD  1 
ATOM   542  C CE  . LYS   A 1 68 ? -6.371  -15.345 9.883   1.00 41.74  ? 67  LYS   A CE  1 
ATOM   543  N NZ  . LYS   A 1 68 ? -7.180  -14.330 9.181   1.00 41.47  ? 67  LYS   A NZ  1 
ATOM   544  N N   . TYR   A 1 69 ? -0.361  -16.774 9.908   1.00 28.30  ? 68  TYR   A N   1 
ATOM   545  C CA  . TYR   A 1 69 ? -0.151  -17.876 8.976   1.00 27.30  ? 68  TYR   A CA  1 
ATOM   546  C C   . TYR   A 1 69 ? 1.241   -18.531 9.107   1.00 25.60  ? 68  TYR   A C   1 
ATOM   547  O O   . TYR   A 1 69 ? 1.472   -19.594 8.548   1.00 29.48  ? 68  TYR   A O   1 
ATOM   548  C CB  . TYR   A 1 69 ? -0.274  -17.324 7.543   1.00 23.65  ? 68  TYR   A CB  1 
ATOM   549  C CG  . TYR   A 1 69 ? -1.674  -16.908 7.111   1.00 27.13  ? 68  TYR   A CG  1 
ATOM   550  C CD1 . TYR   A 1 69 ? -2.797  -17.669 7.485   1.00 27.65  ? 68  TYR   A CD1 1 
ATOM   551  C CD2 . TYR   A 1 69 ? -1.858  -15.704 6.424   1.00 25.75  ? 68  TYR   A CD2 1 
ATOM   552  C CE1 . TYR   A 1 69 ? -4.070  -17.246 7.140   1.00 30.92  ? 68  TYR   A CE1 1 
ATOM   553  C CE2 . TYR   A 1 69 ? -3.137  -15.294 6.066   1.00 28.94  ? 68  TYR   A CE2 1 
ATOM   554  C CZ  . TYR   A 1 69 ? -4.231  -16.064 6.432   1.00 29.58  ? 68  TYR   A CZ  1 
ATOM   555  O OH  . TYR   A 1 69 ? -5.485  -15.655 6.047   1.00 29.76  ? 68  TYR   A OH  1 
ATOM   556  N N   . GLY   A 1 70 ? 2.127   -17.929 9.902   1.00 27.47  ? 69  GLY   A N   1 
ATOM   557  C CA  . GLY   A 1 70 ? 3.524   -18.359 9.968   1.00 26.89  ? 69  GLY   A CA  1 
ATOM   558  C C   . GLY   A 1 70 ? 3.784   -19.326 11.135  1.00 30.51  ? 69  GLY   A C   1 
ATOM   559  O O   . GLY   A 1 70 ? 4.588   -19.048 11.990  1.00 39.00  ? 69  GLY   A O   1 
ATOM   560  N N   . LYS   A 1 71 ? 3.024   -20.399 11.206  1.00 33.60  ? 70  LYS   A N   1 
ATOM   561  C CA  . LYS   A 1 71 ? 3.216   -21.402 12.239  1.00 36.37  ? 70  LYS   A CA  1 
ATOM   562  C C   . LYS   A 1 71 ? 3.484   -22.727 11.542  1.00 32.16  ? 70  LYS   A C   1 
ATOM   563  O O   . LYS   A 1 71 ? 3.032   -22.974 10.427  1.00 34.24  ? 70  LYS   A O   1 
ATOM   564  C CB  . LYS   A 1 71 ? 1.968   -21.460 13.131  1.00 41.24  ? 70  LYS   A CB  1 
ATOM   565  C CG  . LYS   A 1 71 ? 1.731   -20.160 13.893  1.00 43.27  ? 70  LYS   A CG  1 
ATOM   566  C CD  . LYS   A 1 71 ? 1.032   -20.362 15.231  1.00 45.65  ? 70  LYS   A CD  1 
ATOM   567  N N   . PRO   A 1 72 ? 4.252   -23.668 12.153  1.00 34.99  ? 71  PRO   A N   1 
ATOM   568  C CA  . PRO   A 1 72 ? 4.489   -24.951 11.490  1.00 33.93  ? 71  PRO   A CA  1 
ATOM   569  C C   . PRO   A 1 72 ? 3.272   -25.720 10.999  1.00 32.95  ? 71  PRO   A C   1 
ATOM   570  O O   . PRO   A 1 72 ? 2.218   -25.698 11.637  1.00 41.15  ? 71  PRO   A O   1 
ATOM   571  C CB  . PRO   A 1 72 ? 5.328   -25.748 12.534  1.00 37.02  ? 71  PRO   A CB  1 
ATOM   572  C CG  . PRO   A 1 72 ? 5.970   -24.675 13.386  1.00 41.46  ? 71  PRO   A CG  1 
ATOM   573  C CD  . PRO   A 1 72 ? 4.990   -23.490 13.418  1.00 42.29  ? 71  PRO   A CD  1 
ATOM   574  N N   . ASN   A 1 73 ? 3.415   -26.397 9.868   1.00 37.15  ? 72  ASN   A N   1 
ATOM   575  C CA  . ASN   A 1 73 ? 2.351   -27.156 9.249   1.00 41.21  ? 72  ASN   A CA  1 
ATOM   576  C C   . ASN   A 1 73 ? 2.957   -28.505 8.933   1.00 46.26  ? 72  ASN   A C   1 
ATOM   577  O O   . ASN   A 1 73 ? 4.154   -28.636 8.718   1.00 47.69  ? 72  ASN   A O   1 
ATOM   578  C CB  . ASN   A 1 73 ? 1.835   -26.461 7.983   1.00 38.17  ? 72  ASN   A CB  1 
ATOM   579  C CG  . ASN   A 1 73 ? 0.462   -26.906 7.523   1.00 47.35  ? 72  ASN   A CG  1 
ATOM   580  O OD1 . ASN   A 1 73 ? 0.325   -27.783 6.663   1.00 45.06  ? 72  ASN   A OD1 1 
ATOM   581  N ND2 . ASN   A 1 73 ? -0.582  -26.231 7.982   1.00 47.20  ? 72  ASN   A ND2 1 
ATOM   582  N N   . LYS   A 1 74 ? 2.106   -29.514 8.911   1.00 47.77  ? 73  LYS   A N   1 
ATOM   583  C CA  . LYS   A 1 74 ? 2.542   -30.858 8.625   1.00 42.84  ? 73  LYS   A CA  1 
ATOM   584  C C   . LYS   A 1 74 ? 2.846   -31.030 7.135   1.00 44.62  ? 73  LYS   A C   1 
ATOM   585  O O   . LYS   A 1 74 ? 3.483   -32.009 6.742   1.00 45.00  ? 73  LYS   A O   1 
ATOM   586  C CB  . LYS   A 1 74 ? 1.379   -31.677 9.224   1.00 47.28  ? 73  LYS   A CB  1 
ATOM   587  C CG  . LYS   A 1 74 ? 0.122   -31.799 8.352   1.00 50.07  ? 73  LYS   A CG  1 
ATOM   588  N N   . ARG   A 1 75 ? 2.403   -30.095 6.278   1.00 40.75  ? 74  ARG   A N   1 
ATOM   589  C CA  . ARG   A 1 75 ? 2.457   -30.364 4.847   1.00 36.95  ? 74  ARG   A CA  1 
ATOM   590  C C   . ARG   A 1 75 ? 3.890   -30.302 4.294   1.00 36.24  ? 74  ARG   A C   1 
ATOM   591  O O   . ARG   A 1 75 ? 4.694   -29.504 4.760   1.00 34.42  ? 74  ARG   A O   1 
ATOM   592  C CB  . ARG   A 1 75 ? 1.519   -29.425 4.075   1.00 39.78  ? 74  ARG   A CB  1 
ATOM   593  C CG  . ARG   A 1 75 ? 0.063   -29.676 4.440   1.00 47.22  ? 74  ARG   A CG  1 
ATOM   594  C CD  . ARG   A 1 75 ? -0.544  -30.793 3.626   1.00 44.33  ? 74  ARG   A CD  1 
ATOM   595  N NE  . ARG   A 1 75 ? -1.277  -30.265 2.478   1.00 55.98  ? 74  ARG   A NE  1 
ATOM   596  C CZ  . ARG   A 1 75 ? -2.398  -29.552 2.623   1.00 56.45  ? 74  ARG   A CZ  1 
ATOM   597  N NH1 . ARG   A 1 75 ? -3.122  -29.268 1.562   1.00 54.85  ? 74  ARG   A NH1 1 
ATOM   598  N NH2 . ARG   A 1 75 ? -2.829  -29.192 3.828   1.00 64.10  ? 74  ARG   A NH2 1 
ATOM   599  N N   . LYS   A 1 76 ? 4.165   -31.144 3.287   1.00 36.28  ? 75  LYS   A N   1 
ATOM   600  C CA  . LYS   A 1 76 ? 5.489   -31.305 2.702   1.00 37.83  ? 75  LYS   A CA  1 
ATOM   601  C C   . LYS   A 1 76 ? 6.039   -29.941 2.285   1.00 33.92  ? 75  LYS   A C   1 
ATOM   602  O O   . LYS   A 1 76 ? 5.448   -29.261 1.434   1.00 32.40  ? 75  LYS   A O   1 
ATOM   603  C CB  . LYS   A 1 76 ? 5.442   -32.209 1.467   1.00 38.57  ? 75  LYS   A CB  1 
ATOM   604  C CG  . LYS   A 1 76 ? 6.809   -32.587 0.929   1.00 43.62  ? 75  LYS   A CG  1 
ATOM   605  C CD  . LYS   A 1 76 ? 6.853   -33.576 -0.234  1.00 45.26  ? 75  LYS   A CD  1 
ATOM   606  C CE  . LYS   A 1 76 ? 8.283   -33.780 -0.652  1.00 48.62  ? 75  LYS   A CE  1 
ATOM   607  N N   . GLY   A 1 77 ? 7.209   -29.600 2.838   1.00 33.33  ? 76  GLY   A N   1 
ATOM   608  C CA  . GLY   A 1 77 ? 7.924   -28.408 2.394   1.00 29.19  ? 76  GLY   A CA  1 
ATOM   609  C C   . GLY   A 1 77 ? 7.574   -27.166 3.208   1.00 27.65  ? 76  GLY   A C   1 
ATOM   610  O O   . GLY   A 1 77 ? 8.285   -26.172 3.118   1.00 29.03  ? 76  GLY   A O   1 
ATOM   611  N N   . PHE   A 1 78 ? 6.490   -27.198 3.971   1.00 28.32  ? 77  PHE   A N   1 
ATOM   612  C CA  . PHE   A 1 78 ? 6.033   -25.982 4.605   1.00 26.48  ? 77  PHE   A CA  1 
ATOM   613  C C   . PHE   A 1 78 ? 7.057   -25.407 5.596   1.00 29.59  ? 77  PHE   A C   1 
ATOM   614  O O   . PHE   A 1 78 ? 7.347   -24.211 5.623   1.00 27.44  ? 77  PHE   A O   1 
ATOM   615  C CB  . PHE   A 1 78 ? 4.648   -26.262 5.210   1.00 30.58  ? 77  PHE   A CB  1 
ATOM   616  C CG  . PHE   A 1 78 ? 3.939   -24.975 5.608   1.00 32.14  ? 77  PHE   A CG  1 
ATOM   617  C CD1 . PHE   A 1 78 ? 4.213   -24.326 6.807   1.00 30.03  ? 77  PHE   A CD1 1 
ATOM   618  C CD2 . PHE   A 1 78 ? 2.977   -24.409 4.757   1.00 31.59  ? 77  PHE   A CD2 1 
ATOM   619  C CE1 . PHE   A 1 78 ? 3.590   -23.140 7.151   1.00 29.48  ? 77  PHE   A CE1 1 
ATOM   620  C CE2 . PHE   A 1 78 ? 2.334   -23.224 5.115   1.00 27.15  ? 77  PHE   A CE2 1 
ATOM   621  C CZ  . PHE   A 1 78 ? 2.623   -22.591 6.307   1.00 26.55  ? 77  PHE   A CZ  1 
ATOM   622  N N   . ASN   A 1 79 ? 7.577   -26.240 6.511   1.00 28.96  ? 78  ASN   A N   1 
ATOM   623  C CA  . ASN   A 1 79 ? 8.454   -25.712 7.549   1.00 26.60  ? 78  ASN   A CA  1 
ATOM   624  C C   . ASN   A 1 79 ? 9.812   -25.301 6.931   1.00 23.17  ? 78  ASN   A C   1 
ATOM   625  O O   . ASN   A 1 79 ? 10.414  -24.332 7.430   1.00 26.87  ? 78  ASN   A O   1 
ATOM   626  C CB  . ASN   A 1 79 ? 8.604   -26.760 8.665   1.00 28.09  ? 78  ASN   A CB  1 
ATOM   627  C CG  . ASN   A 1 79 ? 7.262   -27.035 9.306   1.00 31.38  ? 78  ASN   A CG  1 
ATOM   628  O OD1 . ASN   A 1 79 ? 6.368   -26.176 9.316   1.00 32.08  ? 78  ASN   A OD1 1 
ATOM   629  N ND2 . ASN   A 1 79 ? 7.121   -28.205 9.931   1.00 30.16  ? 78  ASN   A ND2 1 
ATOM   630  N N   . GLU   A 1 80 ? 10.307  -25.988 5.882   1.00 24.91  ? 79  GLU   A N   1 
ATOM   631  C CA  . GLU   A 1 80 ? 11.462  -25.465 5.176   1.00 24.88  ? 79  GLU   A CA  1 
ATOM   632  C C   . GLU   A 1 80 ? 11.113  -24.073 4.635   1.00 24.41  ? 79  GLU   A C   1 
ATOM   633  O O   . GLU   A 1 80 ? 11.940  -23.154 4.643   1.00 24.30  ? 79  GLU   A O   1 
ATOM   634  C CB  . GLU   A 1 80 ? 11.840  -26.354 3.992   1.00 26.95  ? 79  GLU   A CB  1 
ATOM   635  C CG  . GLU   A 1 80 ? 13.175  -25.985 3.344   1.00 27.11  ? 79  GLU   A CG  1 
ATOM   636  C CD  . GLU   A 1 80 ? 13.651  -27.066 2.373   1.00 41.99  ? 79  GLU   A CD  1 
ATOM   637  O OE1 . GLU   A 1 80 ? 12.998  -28.119 2.224   1.00 45.21  ? 79  GLU   A OE1 1 
ATOM   638  O OE2 . GLU   A 1 80 ? 14.700  -26.854 1.754   1.00 37.98  ? 79  GLU   A OE2 1 
ATOM   639  N N   . GLY   A 1 81 ? 9.883   -23.964 4.091   1.00 25.75  ? 80  GLY   A N   1 
ATOM   640  C CA  . GLY   A 1 81 ? 9.443   -22.686 3.545   1.00 26.48  ? 80  GLY   A CA  1 
ATOM   641  C C   . GLY   A 1 81 ? 9.470   -21.574 4.585   1.00 22.71  ? 80  GLY   A C   1 
ATOM   642  O O   . GLY   A 1 81 ? 9.817   -20.445 4.254   1.00 22.45  ? 80  GLY   A O   1 
ATOM   643  N N   . LEU   A 1 82 ? 9.001   -21.847 5.813   1.00 22.60  ? 81  LEU   A N   1 
ATOM   644  C CA  . LEU   A 1 82 ? 9.027   -20.856 6.860   1.00 22.35  ? 81  LEU   A CA  1 
ATOM   645  C C   . LEU   A 1 82 ? 10.470  -20.414 7.142   1.00 23.39  ? 81  LEU   A C   1 
ATOM   646  O O   . LEU   A 1 82 ? 10.695  -19.205 7.382   1.00 22.80  ? 81  LEU   A O   1 
ATOM   647  C CB  . LEU   A 1 82 ? 8.336   -21.324 8.141   1.00 24.66  ? 81  LEU   A CB  1 
ATOM   648  C CG  . LEU   A 1 82 ? 6.831   -21.609 8.019   1.00 25.49  ? 81  LEU   A CG  1 
ATOM   649  C CD1 . LEU   A 1 82 ? 6.500   -22.159 9.410   1.00 28.32  ? 81  LEU   A CD1 1 
ATOM   650  C CD2 . LEU   A 1 82 ? 6.075   -20.309 7.845   1.00 25.75  ? 81  LEU   A CD2 1 
ATOM   651  N N   . TRP   A 1 83 ? 11.439  -21.355 7.007   1.00 22.90  ? 82  TRP   A N   1 
ATOM   652  C CA  . TRP   A 1 83 ? 12.789  -20.946 7.319   1.00 24.57  ? 82  TRP   A CA  1 
ATOM   653  C C   . TRP   A 1 83 ? 13.295  -20.015 6.223   1.00 21.25  ? 82  TRP   A C   1 
ATOM   654  O O   . TRP   A 1 83 ? 13.976  -19.041 6.507   1.00 22.56  ? 82  TRP   A O   1 
ATOM   655  C CB  . TRP   A 1 83 ? 13.712  -22.182 7.454   1.00 24.84  ? 82  TRP   A CB  1 
ATOM   656  C CG  . TRP   A 1 83 ? 15.147  -21.827 7.743   1.00 24.05  ? 82  TRP   A CG  1 
ATOM   657  C CD1 . TRP   A 1 83 ? 15.775  -21.762 8.958   1.00 28.17  ? 82  TRP   A CD1 1 
ATOM   658  C CD2 . TRP   A 1 83 ? 16.145  -21.505 6.749   1.00 24.24  ? 82  TRP   A CD2 1 
ATOM   659  N NE1 . TRP   A 1 83 ? 17.092  -21.416 8.775   1.00 26.83  ? 82  TRP   A NE1 1 
ATOM   660  C CE2 . TRP   A 1 83 ? 17.340  -21.246 7.446   1.00 24.73  ? 82  TRP   A CE2 1 
ATOM   661  C CE3 . TRP   A 1 83 ? 16.154  -21.425 5.349   1.00 26.62  ? 82  TRP   A CE3 1 
ATOM   662  C CZ2 . TRP   A 1 83 ? 18.526  -20.917 6.792   1.00 25.70  ? 82  TRP   A CZ2 1 
ATOM   663  C CZ3 . TRP   A 1 83 ? 17.324  -21.079 4.702   1.00 26.82  ? 82  TRP   A CZ3 1 
ATOM   664  C CH2 . TRP   A 1 83 ? 18.499  -20.830 5.421   1.00 29.57  ? 82  TRP   A CH2 1 
ATOM   665  N N   . GLU   A 1 84 ? 12.984  -20.373 4.968   1.00 20.14  ? 83  GLU   A N   1 
ATOM   666  C CA  . GLU   A 1 84 ? 13.495  -19.636 3.831   1.00 19.45  ? 83  GLU   A CA  1 
ATOM   667  C C   . GLU   A 1 84 ? 12.967  -18.203 3.862   1.00 21.78  ? 83  GLU   A C   1 
ATOM   668  O O   . GLU   A 1 84 ? 13.710  -17.254 3.656   1.00 20.53  ? 83  GLU   A O   1 
ATOM   669  C CB  . GLU   A 1 84 ? 13.059  -20.309 2.540   1.00 20.97  ? 83  GLU   A CB  1 
ATOM   670  C CG  . GLU   A 1 84 ? 13.825  -21.620 2.395   1.00 21.72  ? 83  GLU   A CG  1 
ATOM   671  C CD  . GLU   A 1 84 ? 13.412  -22.370 1.118   1.00 24.90  ? 83  GLU   A CD  1 
ATOM   672  O OE1 . GLU   A 1 84 ? 12.480  -21.959 0.394   1.00 23.98  ? 83  GLU   A OE1 1 
ATOM   673  O OE2 . GLU   A 1 84 ? 14.001  -23.453 0.833   1.00 25.26  ? 83  GLU   A OE2 1 
ATOM   674  N N   . ILE   A 1 85 ? 11.641  -18.037 4.090   1.00 19.99  ? 84  ILE   A N   1 
ATOM   675  C CA  . ILE   A 1 85 ? 11.093  -16.688 4.002   1.00 19.72  ? 84  ILE   A CA  1 
ATOM   676  C C   . ILE   A 1 85 ? 11.653  -15.779 5.129   1.00 19.22  ? 84  ILE   A C   1 
ATOM   677  O O   . ILE   A 1 85 ? 11.839  -14.566 4.949   1.00 21.23  ? 84  ILE   A O   1 
ATOM   678  C CB  . ILE   A 1 85 ? 9.533   -16.738 3.979   1.00 18.89  ? 84  ILE   A CB  1 
ATOM   679  C CG1 . ILE   A 1 85 ? 8.954   -15.363 3.596   1.00 20.56  ? 84  ILE   A CG1 1 
ATOM   680  C CG2 . ILE   A 1 85 ? 9.004   -17.110 5.370   1.00 21.87  ? 84  ILE   A CG2 1 
ATOM   681  C CD1 . ILE   A 1 85 ? 7.522   -15.450 3.043   1.00 19.44  ? 84  ILE   A CD1 1 
ATOM   682  N N   . GLN   A 1 86 ? 11.927  -16.384 6.295   1.00 20.64  ? 85  GLN   A N   1 
ATOM   683  C CA  . GLN   A 1 86 ? 12.468  -15.626 7.439   1.00 23.31  ? 85  GLN   A CA  1 
ATOM   684  C C   . GLN   A 1 86 ? 13.969  -15.347 7.292   1.00 23.58  ? 85  GLN   A C   1 
ATOM   685  O O   . GLN   A 1 86 ? 14.439  -14.246 7.710   1.00 26.76  ? 85  GLN   A O   1 
ATOM   686  C CB  . GLN   A 1 86 ? 12.175  -16.404 8.731   1.00 25.89  ? 85  GLN   A CB  1 
ATOM   687  C CG  . GLN   A 1 86 ? 12.537  -15.619 9.984   1.00 31.21  ? 85  GLN   A CG  1 
ATOM   688  C CD  . GLN   A 1 86 ? 11.994  -16.277 11.251  1.00 35.70  ? 85  GLN   A CD  1 
ATOM   689  O OE1 . GLN   A 1 86 ? 11.728  -17.491 11.305  1.00 36.30  ? 85  GLN   A OE1 1 
ATOM   690  N NE2 . GLN   A 1 86 ? 11.856  -15.462 12.289  1.00 43.61  ? 85  GLN   A NE2 1 
ATOM   691  N N   . ASN   A 1 87 ? 14.718  -16.312 6.732   1.00 21.70  ? 86  ASN   A N   1 
ATOM   692  C CA  . ASN   A 1 87 ? 16.176  -16.275 6.823   1.00 21.88  ? 86  ASN   A CA  1 
ATOM   693  C C   . ASN   A 1 87 ? 16.909  -15.932 5.542   1.00 22.80  ? 86  ASN   A C   1 
ATOM   694  O O   . ASN   A 1 87 ? 18.010  -15.390 5.600   1.00 24.36  ? 86  ASN   A O   1 
ATOM   695  C CB  . ASN   A 1 87 ? 16.723  -17.547 7.467   1.00 22.26  ? 86  ASN   A CB  1 
ATOM   696  C CG  . ASN   A 1 87 ? 16.248  -17.647 8.897   1.00 28.37  ? 86  ASN   A CG  1 
ATOM   697  O OD1 . ASN   A 1 87 ? 16.538  -16.753 9.717   1.00 30.39  ? 86  ASN   A OD1 1 
ATOM   698  N ND2 . ASN   A 1 87 ? 15.322  -18.555 9.156   1.00 26.40  ? 86  ASN   A ND2 1 
ATOM   699  N N   . ASN   A 1 88 ? 16.366  -16.310 4.388   1.00 21.85  ? 87  ASN   A N   1 
ATOM   700  C CA  . ASN   A 1 88 ? 17.000  -15.939 3.139   1.00 20.63  ? 87  ASN   A CA  1 
ATOM   701  C C   . ASN   A 1 88 ? 15.960  -15.856 2.022   1.00 21.20  ? 87  ASN   A C   1 
ATOM   702  O O   . ASN   A 1 88 ? 15.982  -16.600 1.025   1.00 20.94  ? 87  ASN   A O   1 
ATOM   703  C CB  . ASN   A 1 88 ? 18.185  -16.865 2.830   1.00 21.50  ? 87  ASN   A CB  1 
ATOM   704  C CG  . ASN   A 1 88 ? 19.212  -16.226 1.914   1.00 24.97  ? 87  ASN   A CG  1 
ATOM   705  O OD1 . ASN   A 1 88 ? 18.987  -15.222 1.222   1.00 23.02  ? 87  ASN   A OD1 1 
ATOM   706  N ND2 . ASN   A 1 88 ? 20.418  -16.788 1.916   1.00 27.76  ? 87  ASN   A ND2 1 
ATOM   707  N N   . PRO   A 1 89 ? 15.042  -14.869 2.112   1.00 20.78  ? 88  PRO   A N   1 
ATOM   708  C CA  . PRO   A 1 89 ? 13.909  -14.868 1.177   1.00 19.44  ? 88  PRO   A CA  1 
ATOM   709  C C   . PRO   A 1 89 ? 14.243  -14.423 -0.228  1.00 22.94  ? 88  PRO   A C   1 
ATOM   710  O O   . PRO   A 1 89 ? 13.454  -14.670 -1.134  1.00 20.45  ? 88  PRO   A O   1 
ATOM   711  C CB  . PRO   A 1 89 ? 12.953  -13.899 1.860   1.00 20.49  ? 88  PRO   A CB  1 
ATOM   712  C CG  . PRO   A 1 89 ? 13.878  -12.936 2.566   1.00 20.34  ? 88  PRO   A CG  1 
ATOM   713  C CD  . PRO   A 1 89 ? 14.905  -13.887 3.190   1.00 19.67  ? 88  PRO   A CD  1 
ATOM   714  N N   . HIS   A 1 90 ? 15.457  -13.866 -0.436  1.00 19.20  ? 89  HIS   A N   1 
ATOM   715  C CA  . HIS   A 1 90 ? 15.813  -13.358 -1.758  1.00 19.27  ? 89  HIS   A CA  1 
ATOM   716  C C   . HIS   A 1 90 ? 16.919  -14.165 -2.447  1.00 20.64  ? 89  HIS   A C   1 
ATOM   717  O O   . HIS   A 1 90 ? 17.385  -13.756 -3.516  1.00 22.54  ? 89  HIS   A O   1 
ATOM   718  C CB  . HIS   A 1 90 ? 16.192  -11.861 -1.653  1.00 19.57  ? 89  HIS   A CB  1 
ATOM   719  C CG  . HIS   A 1 90 ? 15.115  -11.023 -1.060  1.00 20.04  ? 89  HIS   A CG  1 
ATOM   720  N ND1 . HIS   A 1 90 ? 13.866  -10.927 -1.691  1.00 19.90  ? 89  HIS   A ND1 1 
ATOM   721  C CD2 . HIS   A 1 90 ? 15.081  -10.291 0.039   1.00 20.38  ? 89  HIS   A CD2 1 
ATOM   722  C CE1 . HIS   A 1 90 ? 13.109  -10.096 -0.967  1.00 20.17  ? 89  HIS   A CE1 1 
ATOM   723  N NE2 . HIS   A 1 90 ? 13.826  -9.700  0.107   1.00 21.50  ? 89  HIS   A NE2 1 
ATOM   724  N N   . ALA   A 1 91 ? 17.168  -15.360 -1.922  1.00 21.43  ? 90  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 91 ? 18.232  -16.189 -2.489  1.00 21.59  ? 90  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 91 ? 17.772  -16.916 -3.743  1.00 26.66  ? 90  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 91 ? 16.584  -17.041 -4.041  1.00 24.19  ? 90  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 91 ? 18.711  -17.159 -1.442  1.00 22.86  ? 90  ALA   A CB  1 
ATOM   729  N N   . SER   A 1 92 ? 18.755  -17.426 -4.502  1.00 25.71  ? 91  SER   A N   1 
ATOM   730  C CA  . SER   A 1 92 ? 18.476  -18.358 -5.571  1.00 28.31  ? 91  SER   A CA  1 
ATOM   731  C C   . SER   A 1 92 ? 18.207  -19.744 -4.994  1.00 29.08  ? 91  SER   A C   1 
ATOM   732  O O   . SER   A 1 92 ? 19.036  -20.287 -4.251  1.00 31.10  ? 91  SER   A O   1 
ATOM   733  C CB  . SER   A 1 92 ? 19.645  -18.365 -6.523  1.00 33.57  ? 91  SER   A CB  1 
ATOM   734  O OG  . SER   A 1 92 ? 19.515  -19.536 -7.305  1.00 36.82  ? 91  SER   A OG  1 
ATOM   735  N N   . TYR   A 1 93 ? 17.046  -20.313 -5.343  1.00 27.13  ? 92  TYR   A N   1 
ATOM   736  C CA  . TYR   A 1 93 ? 16.695  -21.647 -4.897  1.00 28.40  ? 92  TYR   A CA  1 
ATOM   737  C C   . TYR   A 1 93 ? 16.604  -22.575 -6.098  1.00 36.17  ? 92  TYR   A C   1 
ATOM   738  O O   . TYR   A 1 93 ? 16.093  -23.678 -5.959  1.00 43.59  ? 92  TYR   A O   1 
ATOM   739  C CB  . TYR   A 1 93 ? 15.343  -21.579 -4.161  1.00 27.17  ? 92  TYR   A CB  1 
ATOM   740  C CG  . TYR   A 1 93 ? 15.503  -20.999 -2.766  1.00 25.69  ? 92  TYR   A CG  1 
ATOM   741  C CD1 . TYR   A 1 93 ? 15.923  -21.786 -1.673  1.00 28.06  ? 92  TYR   A CD1 1 
ATOM   742  C CD2 . TYR   A 1 93 ? 15.212  -19.647 -2.528  1.00 24.75  ? 92  TYR   A CD2 1 
ATOM   743  C CE1 . TYR   A 1 93 ? 16.091  -21.229 -0.401  1.00 29.31  ? 92  TYR   A CE1 1 
ATOM   744  C CE2 . TYR   A 1 93 ? 15.343  -19.105 -1.261  1.00 26.25  ? 92  TYR   A CE2 1 
ATOM   745  C CZ  . TYR   A 1 93 ? 15.795  -19.883 -0.201  1.00 26.33  ? 92  TYR   A CZ  1 
ATOM   746  O OH  . TYR   A 1 93 ? 16.003  -19.363 1.048   1.00 27.26  ? 92  TYR   A OH  1 
ATOM   747  N N   . SER   A 1 94 ? 17.150  -22.122 -7.228  1.00 46.09  ? 93  SER   A N   1 
ATOM   748  C CA  . SER   A 1 94 ? 17.439  -22.991 -8.355  1.00 61.04  ? 93  SER   A CA  1 
ATOM   749  C C   . SER   A 1 94 ? 18.324  -24.135 -7.842  1.00 67.83  ? 93  SER   A C   1 
ATOM   750  O O   . SER   A 1 94 ? 19.544  -23.892 -7.711  1.00 67.16  ? 93  SER   A O   1 
ATOM   751  C CB  . SER   A 1 94 ? 18.124  -22.218 -9.456  1.00 61.05  ? 93  SER   A CB  1 
ATOM   752  O OG  . SER   A 1 94 ? 17.306  -21.148 -9.902  1.00 65.27  ? 93  SER   A OG  1 
ATOM   753  O OXT . SER   A 1 94 ? 17.753  -25.209 -7.530  1.00 80.86  ? 93  SER   A OXT 1 
ATOM   754  N N   . MET   B 1 2  ? 38.866  -11.466 -42.066 1.00 54.60  ? 1   MET   B N   1 
ATOM   755  C CA  . MET   B 1 2  ? 38.457  -12.123 -43.334 1.00 52.28  ? 1   MET   B CA  1 
ATOM   756  C C   . MET   B 1 2  ? 36.928  -12.188 -43.372 1.00 50.01  ? 1   MET   B C   1 
ATOM   757  O O   . MET   B 1 2  ? 36.311  -12.348 -42.317 1.00 55.98  ? 1   MET   B O   1 
ATOM   758  C CB  . MET   B 1 2  ? 39.080  -13.527 -43.421 1.00 56.49  ? 1   MET   B CB  1 
ATOM   759  C CG  . MET   B 1 2  ? 38.913  -14.214 -44.782 1.00 71.31  ? 1   MET   B CG  1 
ATOM   760  S SD  . MET   B 1 2  ? 40.284  -14.096 -45.958 1.00 73.52  ? 1   MET   B SD  1 
ATOM   761  C CE  . MET   B 1 2  ? 41.154  -12.648 -45.336 1.00 45.02  ? 1   MET   B CE  1 
ATOM   762  N N   . PRO   B 1 3  ? 36.258  -12.012 -44.547 1.00 43.41  ? 2   PRO   B N   1 
ATOM   763  C CA  . PRO   B 1 3  ? 34.823  -12.289 -44.656 1.00 44.65  ? 2   PRO   B CA  1 
ATOM   764  C C   . PRO   B 1 3  ? 34.533  -13.720 -44.208 1.00 44.17  ? 2   PRO   B C   1 
ATOM   765  O O   . PRO   B 1 3  ? 35.378  -14.586 -44.396 1.00 43.69  ? 2   PRO   B O   1 
ATOM   766  C CB  . PRO   B 1 3  ? 34.506  -12.073 -46.131 1.00 44.69  ? 2   PRO   B CB  1 
ATOM   767  C CG  . PRO   B 1 3  ? 35.579  -11.082 -46.582 1.00 39.16  ? 2   PRO   B CG  1 
ATOM   768  C CD  . PRO   B 1 3  ? 36.822  -11.482 -45.802 1.00 37.46  ? 2   PRO   B CD  1 
ATOM   769  N N   . HIS   B 1 4  ? 33.381  -13.918 -43.541 1.00 39.34  ? 3   HIS   B N   1 
ATOM   770  C CA  . HIS   B 1 4  ? 32.902  -15.238 -43.147 1.00 40.08  ? 3   HIS   B CA  1 
ATOM   771  C C   . HIS   B 1 4  ? 31.537  -15.491 -43.779 1.00 37.79  ? 3   HIS   B C   1 
ATOM   772  O O   . HIS   B 1 4  ? 30.989  -14.609 -44.442 1.00 39.08  ? 3   HIS   B O   1 
ATOM   773  C CB  . HIS   B 1 4  ? 32.923  -15.389 -41.624 1.00 44.29  ? 3   HIS   B CB  1 
ATOM   774  C CG  . HIS   B 1 4  ? 34.325  -15.421 -41.128 1.00 52.66  ? 3   HIS   B CG  1 
ATOM   775  N ND1 . HIS   B 1 4  ? 35.266  -16.268 -41.688 1.00 57.98  ? 3   HIS   B ND1 1 
ATOM   776  C CD2 . HIS   B 1 4  ? 34.965  -14.728 -40.162 1.00 55.53  ? 3   HIS   B CD2 1 
ATOM   777  C CE1 . HIS   B 1 4  ? 36.434  -16.086 -41.079 1.00 48.42  ? 3   HIS   B CE1 1 
ATOM   778  N NE2 . HIS   B 1 4  ? 36.276  -15.157 -40.150 1.00 57.77  ? 3   HIS   B NE2 1 
ATOM   779  N N   . ALA   B 1 5  ? 30.995  -16.707 -43.587 1.00 35.52  ? 4   ALA   B N   1 
ATOM   780  C CA  . ALA   B 1 5  ? 29.681  -17.022 -44.127 1.00 36.27  ? 4   ALA   B CA  1 
ATOM   781  C C   . ALA   B 1 5  ? 28.668  -16.011 -43.606 1.00 37.62  ? 4   ALA   B C   1 
ATOM   782  O O   . ALA   B 1 5  ? 27.721  -15.634 -44.299 1.00 36.12  ? 4   ALA   B O   1 
ATOM   783  C CB  . ALA   B 1 5  ? 29.321  -18.402 -43.654 1.00 36.83  ? 4   ALA   B CB  1 
ATOM   784  N N   . PHE   B 1 6  ? 28.857  -15.629 -42.347 1.00 39.75  ? 5   PHE   B N   1 
ATOM   785  C CA  . PHE   B 1 6  ? 28.013  -14.611 -41.744 1.00 41.00  ? 5   PHE   B CA  1 
ATOM   786  C C   . PHE   B 1 6  ? 28.859  -13.373 -41.466 1.00 36.68  ? 5   PHE   B C   1 
ATOM   787  O O   . PHE   B 1 6  ? 29.978  -13.488 -40.970 1.00 41.45  ? 5   PHE   B O   1 
ATOM   788  C CB  . PHE   B 1 6  ? 27.458  -15.024 -40.376 1.00 39.62  ? 5   PHE   B CB  1 
ATOM   789  C CG  . PHE   B 1 6  ? 26.413  -16.127 -40.426 1.00 37.67  ? 5   PHE   B CG  1 
ATOM   790  C CD1 . PHE   B 1 6  ? 25.064  -15.811 -40.597 1.00 32.04  ? 5   PHE   B CD1 1 
ATOM   791  C CD2 . PHE   B 1 6  ? 26.776  -17.465 -40.336 1.00 35.59  ? 5   PHE   B CD2 1 
ATOM   792  C CE1 . PHE   B 1 6  ? 24.098  -16.791 -40.669 1.00 34.96  ? 5   PHE   B CE1 1 
ATOM   793  C CE2 . PHE   B 1 6  ? 25.781  -18.443 -40.388 1.00 31.14  ? 5   PHE   B CE2 1 
ATOM   794  C CZ  . PHE   B 1 6  ? 24.464  -18.115 -40.540 1.00 29.87  ? 5   PHE   B CZ  1 
ATOM   795  N N   . LYS   B 1 7  ? 28.285  -12.215 -41.802 1.00 42.62  ? 6   LYS   B N   1 
ATOM   796  C CA  . LYS   B 1 7  ? 28.986  -10.956 -41.602 1.00 38.82  ? 6   LYS   B CA  1 
ATOM   797  C C   . LYS   B 1 7  ? 28.234  -10.134 -40.552 1.00 38.72  ? 6   LYS   B C   1 
ATOM   798  O O   . LYS   B 1 7  ? 27.000  -10.231 -40.443 1.00 33.68  ? 6   LYS   B O   1 
ATOM   799  C CB  . LYS   B 1 7  ? 29.079  -10.215 -42.937 1.00 42.46  ? 6   LYS   B CB  1 
ATOM   800  C CG  . LYS   B 1 7  ? 27.781  -9.947  -43.662 1.00 45.83  ? 6   LYS   B CG  1 
ATOM   801  C CD  . LYS   B 1 7  ? 27.974  -9.284  -45.029 1.00 49.51  ? 6   LYS   B CD  1 
ATOM   802  C CE  . LYS   B 1 7  ? 26.693  -8.815  -45.662 1.00 50.57  ? 6   LYS   B CE  1 
ATOM   803  N NZ  . LYS   B 1 7  ? 25.888  -9.947  -46.124 1.00 51.31  ? 6   LYS   B NZ  1 
ATOM   804  N N   . PRO   B 1 8  ? 28.934  -9.252  -39.791 1.00 42.63  ? 7   PRO   B N   1 
ATOM   805  C CA  . PRO   B 1 8  ? 28.280  -8.249  -38.935 1.00 34.15  ? 7   PRO   B CA  1 
ATOM   806  C C   . PRO   B 1 8  ? 27.097  -7.596  -39.615 1.00 33.77  ? 7   PRO   B C   1 
ATOM   807  O O   . PRO   B 1 8  ? 27.196  -7.139  -40.773 1.00 37.25  ? 7   PRO   B O   1 
ATOM   808  C CB  . PRO   B 1 8  ? 29.452  -7.262  -38.789 1.00 36.57  ? 7   PRO   B CB  1 
ATOM   809  C CG  . PRO   B 1 8  ? 30.643  -8.184  -38.621 1.00 44.27  ? 7   PRO   B CG  1 
ATOM   810  C CD  . PRO   B 1 8  ? 30.407  -9.129  -39.757 1.00 42.97  ? 7   PRO   B CD  1 
ATOM   811  N N   . GLY   B 1 9  ? 25.971  -7.535  -38.892 1.00 31.64  ? 8   GLY   B N   1 
ATOM   812  C CA  . GLY   B 1 9  ? 24.766  -6.894  -39.397 1.00 30.00  ? 8   GLY   B CA  1 
ATOM   813  C C   . GLY   B 1 9  ? 23.778  -7.864  -40.050 1.00 26.87  ? 8   GLY   B C   1 
ATOM   814  O O   . GLY   B 1 9  ? 22.631  -7.503  -40.309 1.00 29.69  ? 8   GLY   B O   1 
ATOM   815  N N   . ASP   B 1 10 ? 24.230  -9.100  -40.358 1.00 28.52  ? 9   ASP   B N   1 
ATOM   816  C CA  . ASP   B 1 10 ? 23.319  -10.109 -40.879 1.00 29.14  ? 9   ASP   B CA  1 
ATOM   817  C C   . ASP   B 1 10 ? 22.257  -10.458 -39.811 1.00 24.03  ? 9   ASP   B C   1 
ATOM   818  O O   . ASP   B 1 10 ? 22.577  -10.501 -38.617 1.00 28.28  ? 9   ASP   B O   1 
ATOM   819  C CB  . ASP   B 1 10 ? 24.031  -11.409 -41.226 1.00 29.32  ? 9   ASP   B CB  1 
ATOM   820  C CG  . ASP   B 1 10 ? 24.804  -11.479 -42.542 1.00 39.50  ? 9   ASP   B CG  1 
ATOM   821  O OD1 . ASP   B 1 10 ? 24.552  -10.628 -43.410 1.00 36.17  ? 9   ASP   B OD1 1 
ATOM   822  O OD2 . ASP   B 1 10 ? 25.613  -12.444 -42.695 1.00 36.83  ? 9   ASP   B OD2 1 
ATOM   823  N N   . LEU   B 1 11 ? 21.047  -10.603 -40.287 1.00 25.94  ? 10  LEU   B N   1 
ATOM   824  C CA  . LEU   B 1 11 ? 19.906  -10.824 -39.394 1.00 25.46  ? 10  LEU   B CA  1 
ATOM   825  C C   . LEU   B 1 11 ? 19.664  -12.331 -39.396 1.00 26.90  ? 10  LEU   B C   1 
ATOM   826  O O   . LEU   B 1 11 ? 19.742  -12.942 -40.472 1.00 29.60  ? 10  LEU   B O   1 
ATOM   827  C CB  . LEU   B 1 11 ? 18.710  -10.012 -39.883 1.00 27.82  ? 10  LEU   B CB  1 
ATOM   828  C CG  . LEU   B 1 11 ? 18.973  -8.490  -39.967 1.00 25.16  ? 10  LEU   B CG  1 
ATOM   829  C CD1 . LEU   B 1 11 ? 17.684  -7.780  -40.341 1.00 27.54  ? 10  LEU   B CD1 1 
ATOM   830  C CD2 . LEU   B 1 11 ? 19.605  -7.992  -38.679 1.00 27.10  ? 10  LEU   B CD2 1 
ATOM   831  N N   . VAL   B 1 12 ? 19.279  -12.903 -38.225 1.00 25.12  ? 11  VAL   B N   1 
ATOM   832  C CA  . VAL   B 1 12 ? 19.071  -14.350 -38.133 1.00 24.16  ? 11  VAL   B CA  1 
ATOM   833  C C   . VAL   B 1 12 ? 17.979  -14.612 -37.109 1.00 25.82  ? 11  VAL   B C   1 
ATOM   834  O O   . VAL   B 1 12 ? 17.612  -13.703 -36.367 1.00 24.91  ? 11  VAL   B O   1 
ATOM   835  C CB  . VAL   B 1 12 ? 20.371  -15.026 -37.649 1.00 24.30  ? 11  VAL   B CB  1 
ATOM   836  C CG1 . VAL   B 1 12 ? 21.515  -14.840 -38.669 1.00 24.44  ? 11  VAL   B CG1 1 
ATOM   837  C CG2 . VAL   B 1 12 ? 20.821  -14.591 -36.234 1.00 27.11  ? 11  VAL   B CG2 1 
ATOM   838  N N   . PHE   B 1 13 ? 17.519  -15.865 -37.041 1.00 23.87  ? 12  PHE   B N   1 
ATOM   839  C CA  . PHE   B 1 13 ? 17.012  -16.381 -35.770 1.00 23.18  ? 12  PHE   B CA  1 
ATOM   840  C C   . PHE   B 1 13 ? 18.094  -17.271 -35.174 1.00 23.27  ? 12  PHE   B C   1 
ATOM   841  O O   . PHE   B 1 13 ? 18.708  -18.068 -35.928 1.00 25.12  ? 12  PHE   B O   1 
ATOM   842  C CB  . PHE   B 1 13 ? 15.768  -17.227 -36.010 1.00 23.57  ? 12  PHE   B CB  1 
ATOM   843  C CG  . PHE   B 1 13 ? 14.550  -16.430 -36.444 1.00 24.70  ? 12  PHE   B CG  1 
ATOM   844  C CD1 . PHE   B 1 13 ? 14.359  -16.120 -37.796 1.00 26.92  ? 12  PHE   B CD1 1 
ATOM   845  C CD2 . PHE   B 1 13 ? 13.651  -15.943 -35.492 1.00 26.28  ? 12  PHE   B CD2 1 
ATOM   846  C CE1 . PHE   B 1 13 ? 13.273  -15.365 -38.164 1.00 28.54  ? 12  PHE   B CE1 1 
ATOM   847  C CE2 . PHE   B 1 13 ? 12.554  -15.179 -35.885 1.00 28.18  ? 12  PHE   B CE2 1 
ATOM   848  C CZ  . PHE   B 1 13 ? 12.362  -14.909 -37.224 1.00 32.94  ? 12  PHE   B CZ  1 
ATOM   849  N N   . ALA   B 1 14 ? 18.365  -17.102 -33.860 1.00 21.60  ? 13  ALA   B N   1 
ATOM   850  C CA  . ALA   B 1 14 ? 19.412  -17.824 -33.178 1.00 22.34  ? 13  ALA   B CA  1 
ATOM   851  C C   . ALA   B 1 14 ? 18.794  -18.780 -32.153 1.00 24.36  ? 13  ALA   B C   1 
ATOM   852  O O   . ALA   B 1 14 ? 17.841  -18.411 -31.448 1.00 26.13  ? 13  ALA   B O   1 
ATOM   853  C CB  . ALA   B 1 14 ? 20.386  -16.867 -32.523 1.00 24.03  ? 13  ALA   B CB  1 
ATOM   854  N N   . LYS   B 1 15 ? 19.320  -20.002 -32.115 1.00 22.45  ? 14  LYS   B N   1 
ATOM   855  C CA  . LYS   B 1 15 ? 18.668  -21.022 -31.278 1.00 25.58  ? 14  LYS   B CA  1 
ATOM   856  C C   . LYS   B 1 15 ? 19.545  -21.353 -30.072 1.00 27.30  ? 14  LYS   B C   1 
ATOM   857  O O   . LYS   B 1 15 ? 20.724  -21.687 -30.198 1.00 28.26  ? 14  LYS   B O   1 
ATOM   858  C CB  . LYS   B 1 15 ? 18.359  -22.250 -32.159 1.00 26.94  ? 14  LYS   B CB  1 
ATOM   859  C CG  . LYS   B 1 15 ? 17.681  -23.408 -31.320 1.00 26.75  ? 14  LYS   B CG  1 
ATOM   860  C CD  . LYS   B 1 15 ? 16.211  -23.066 -31.099 1.00 29.02  ? 14  LYS   B CD  1 
ATOM   861  C CE  . LYS   B 1 15 ? 15.326  -24.146 -30.345 1.00 30.95  ? 14  LYS   B CE  1 
ATOM   862  N NZ  . LYS   B 1 15 ? 15.915  -24.399 -29.035 1.00 28.19  ? 14  LYS   B NZ  1 
ATOM   863  N N   . MET   B 1 16 ? 18.940  -21.248 -28.875 1.00 27.57  ? 15  MET   B N   1 
ATOM   864  C CA  . MET   B 1 16 ? 19.549  -21.656 -27.613 1.00 29.92  ? 15  MET   B CA  1 
ATOM   865  C C   . MET   B 1 16 ? 18.678  -22.739 -26.974 1.00 29.58  ? 15  MET   B C   1 
ATOM   866  O O   . MET   B 1 16 ? 17.452  -22.684 -27.054 1.00 29.63  ? 15  MET   B O   1 
ATOM   867  C CB  . MET   B 1 16 ? 19.617  -20.497 -26.613 1.00 33.65  ? 15  MET   B CB  1 
ATOM   868  C CG  . MET   B 1 16 ? 20.240  -19.240 -27.147 1.00 42.04  ? 15  MET   B CG  1 
ATOM   869  S SD  . MET   B 1 16 ? 21.971  -18.989 -26.730 1.00 50.18  ? 15  MET   B SD  1 
ATOM   870  C CE  . MET   B 1 16 ? 21.976  -18.855 -24.942 1.00 46.43  ? 15  MET   B CE  1 
ATOM   871  N N   . LYS   B 1 17 ? 19.329  -23.709 -26.310 1.00 32.89  ? 16  LYS   B N   1 
ATOM   872  C CA  . LYS   B 1 17 ? 18.582  -24.742 -25.601 1.00 33.17  ? 16  LYS   B CA  1 
ATOM   873  C C   . LYS   B 1 17 ? 17.630  -24.079 -24.589 1.00 29.23  ? 16  LYS   B C   1 
ATOM   874  O O   . LYS   B 1 17 ? 18.035  -23.203 -23.834 1.00 33.89  ? 16  LYS   B O   1 
ATOM   875  C CB  . LYS   B 1 17 ? 19.622  -25.647 -24.923 1.00 41.25  ? 16  LYS   B CB  1 
ATOM   876  C CG  . LYS   B 1 17 ? 19.070  -26.878 -24.177 1.00 44.31  ? 16  LYS   B CG  1 
ATOM   877  C CD  . LYS   B 1 17 ? 20.058  -27.494 -23.190 1.00 51.19  ? 16  LYS   B CD  1 
ATOM   878  N N   . GLY   B 1 18 ? 16.371  -24.513 -24.624 1.00 32.99  ? 17  GLY   B N   1 
ATOM   879  C CA  . GLY   B 1 18 ? 15.340  -24.017 -23.723 1.00 35.35  ? 17  GLY   B CA  1 
ATOM   880  C C   . GLY   B 1 18 ? 14.566  -22.817 -24.270 1.00 34.63  ? 17  GLY   B C   1 
ATOM   881  O O   . GLY   B 1 18 ? 13.645  -22.344 -23.610 1.00 32.63  ? 17  GLY   B O   1 
ATOM   882  N N   . TYR   B 1 19 ? 14.927  -22.316 -25.476 1.00 29.56  ? 18  TYR   B N   1 
ATOM   883  C CA  . TYR   B 1 19 ? 14.278  -21.100 -25.965 1.00 28.06  ? 18  TYR   B CA  1 
ATOM   884  C C   . TYR   B 1 19 ? 13.842  -21.318 -27.411 1.00 26.57  ? 18  TYR   B C   1 
ATOM   885  O O   . TYR   B 1 19 ? 14.502  -22.085 -28.123 1.00 28.59  ? 18  TYR   B O   1 
ATOM   886  C CB  . TYR   B 1 19 ? 15.233  -19.896 -25.998 1.00 28.38  ? 18  TYR   B CB  1 
ATOM   887  C CG  . TYR   B 1 19 ? 15.687  -19.583 -24.580 1.00 30.93  ? 18  TYR   B CG  1 
ATOM   888  C CD1 . TYR   B 1 19 ? 14.932  -18.758 -23.752 1.00 33.59  ? 18  TYR   B CD1 1 
ATOM   889  C CD2 . TYR   B 1 19 ? 16.753  -20.274 -24.035 1.00 29.63  ? 18  TYR   B CD2 1 
ATOM   890  C CE1 . TYR   B 1 19 ? 15.285  -18.569 -22.417 1.00 35.27  ? 18  TYR   B CE1 1 
ATOM   891  C CE2 . TYR   B 1 19 ? 17.123  -20.085 -22.711 1.00 33.30  ? 18  TYR   B CE2 1 
ATOM   892  C CZ  . TYR   B 1 19 ? 16.385  -19.228 -21.910 1.00 32.79  ? 18  TYR   B CZ  1 
ATOM   893  O OH  . TYR   B 1 19 ? 16.785  -19.049 -20.603 1.00 40.95  ? 18  TYR   B OH  1 
ATOM   894  N N   . PRO   B 1 20 ? 12.799  -20.630 -27.897 1.00 26.63  ? 19  PRO   B N   1 
ATOM   895  C CA  . PRO   B 1 20 ? 12.418  -20.691 -29.313 1.00 25.21  ? 19  PRO   B CA  1 
ATOM   896  C C   . PRO   B 1 20 ? 13.498  -19.984 -30.146 1.00 23.03  ? 19  PRO   B C   1 
ATOM   897  O O   . PRO   B 1 20 ? 14.208  -19.150 -29.624 1.00 25.51  ? 19  PRO   B O   1 
ATOM   898  C CB  . PRO   B 1 20 ? 11.115  -19.968 -29.416 1.00 26.85  ? 19  PRO   B CB  1 
ATOM   899  C CG  . PRO   B 1 20 ? 11.111  -19.047 -28.210 1.00 28.30  ? 19  PRO   B CG  1 
ATOM   900  C CD  . PRO   B 1 20 ? 11.946  -19.727 -27.123 1.00 26.79  ? 19  PRO   B CD  1 
ATOM   901  N N   . HIS   B 1 21 ? 13.632  -20.398 -31.417 1.00 24.68  ? 20  HIS   B N   1 
ATOM   902  C CA  . HIS   B 1 21 ? 14.446  -19.633 -32.378 1.00 24.69  ? 20  HIS   B CA  1 
ATOM   903  C C   . HIS   B 1 21 ? 14.178  -18.126 -32.202 1.00 22.07  ? 20  HIS   B C   1 
ATOM   904  O O   . HIS   B 1 21 ? 13.043  -17.675 -32.307 1.00 24.39  ? 20  HIS   B O   1 
ATOM   905  C CB  . HIS   B 1 21 ? 14.138  -20.101 -33.808 1.00 25.51  ? 20  HIS   B CB  1 
ATOM   906  C CG  . HIS   B 1 21 ? 14.336  -21.581 -34.014 1.00 24.84  ? 20  HIS   B CG  1 
ATOM   907  N ND1 . HIS   B 1 21 ? 13.445  -22.556 -33.551 1.00 27.82  ? 20  HIS   B ND1 1 
ATOM   908  C CD2 . HIS   B 1 21 ? 15.356  -22.248 -34.573 1.00 27.45  ? 20  HIS   B CD2 1 
ATOM   909  C CE1 . HIS   B 1 21 ? 13.927  -23.758 -33.863 1.00 28.84  ? 20  HIS   B CE1 1 
ATOM   910  N NE2 . HIS   B 1 21 ? 15.081  -23.602 -34.490 1.00 27.55  ? 20  HIS   B NE2 1 
ATOM   911  N N   . TRP   B 1 22 ? 15.251  -17.328 -32.044 1.00 23.13  ? 21  TRP   B N   1 
ATOM   912  C CA  . TRP   B 1 22 ? 15.027  -16.006 -31.453 1.00 22.22  ? 21  TRP   B CA  1 
ATOM   913  C C   . TRP   B 1 22 ? 15.536  -14.944 -32.426 1.00 23.46  ? 21  TRP   B C   1 
ATOM   914  O O   . TRP   B 1 22 ? 16.683  -15.068 -32.857 1.00 23.55  ? 21  TRP   B O   1 
ATOM   915  C CB  . TRP   B 1 22 ? 15.810  -15.911 -30.127 1.00 24.64  ? 21  TRP   B CB  1 
ATOM   916  C CG  . TRP   B 1 22 ? 15.286  -14.788 -29.255 1.00 24.96  ? 21  TRP   B CG  1 
ATOM   917  C CD1 . TRP   B 1 22 ? 15.510  -13.440 -29.396 1.00 24.86  ? 21  TRP   B CD1 1 
ATOM   918  C CD2 . TRP   B 1 22 ? 14.351  -14.910 -28.138 1.00 25.81  ? 21  TRP   B CD2 1 
ATOM   919  N NE1 . TRP   B 1 22 ? 14.778  -12.719 -28.453 1.00 25.41  ? 21  TRP   B NE1 1 
ATOM   920  C CE2 . TRP   B 1 22 ? 14.102  -13.606 -27.649 1.00 22.97  ? 21  TRP   B CE2 1 
ATOM   921  C CE3 . TRP   B 1 22 ? 13.756  -16.013 -27.500 1.00 28.05  ? 21  TRP   B CE3 1 
ATOM   922  C CZ2 . TRP   B 1 22 ? 13.220  -13.332 -26.584 1.00 25.25  ? 21  TRP   B CZ2 1 
ATOM   923  C CZ3 . TRP   B 1 22 ? 12.931  -15.748 -26.417 1.00 24.98  ? 21  TRP   B CZ3 1 
ATOM   924  C CH2 . TRP   B 1 22 ? 12.647  -14.439 -25.992 1.00 26.46  ? 21  TRP   B CH2 1 
ATOM   925  N N   . PRO   B 1 23 ? 14.775  -13.848 -32.697 1.00 23.03  ? 22  PRO   B N   1 
ATOM   926  C CA  . PRO   B 1 23 ? 15.254  -12.811 -33.633 1.00 21.76  ? 22  PRO   B CA  1 
ATOM   927  C C   . PRO   B 1 23 ? 16.550  -12.199 -33.122 1.00 24.42  ? 22  PRO   B C   1 
ATOM   928  O O   . PRO   B 1 23 ? 16.664  -11.811 -31.948 1.00 24.18  ? 22  PRO   B O   1 
ATOM   929  C CB  . PRO   B 1 23 ? 14.103  -11.763 -33.726 1.00 21.81  ? 22  PRO   B CB  1 
ATOM   930  C CG  . PRO   B 1 23 ? 13.418  -11.979 -32.361 1.00 22.51  ? 22  PRO   B CG  1 
ATOM   931  C CD  . PRO   B 1 23 ? 13.467  -13.504 -32.112 1.00 23.09  ? 22  PRO   B CD  1 
ATOM   932  N N   . ALA   B 1 24 ? 17.568  -12.082 -33.994 1.00 23.10  ? 23  ALA   B N   1 
ATOM   933  C CA  . ALA   B 1 24 ? 18.889  -11.730 -33.518 1.00 22.14  ? 23  ALA   B CA  1 
ATOM   934  C C   . ALA   B 1 24 ? 19.732  -11.204 -34.700 1.00 22.11  ? 23  ALA   B C   1 
ATOM   935  O O   . ALA   B 1 24 ? 19.276  -11.244 -35.838 1.00 24.36  ? 23  ALA   B O   1 
ATOM   936  C CB  . ALA   B 1 24 ? 19.578  -12.922 -32.836 1.00 25.61  ? 23  ALA   B CB  1 
ATOM   937  N N   . ARG   B 1 25 ? 20.883  -10.661 -34.331 1.00 24.04  ? 24  ARG   B N   1 
ATOM   938  C CA  . ARG   B 1 25 ? 21.820  -10.176 -35.353 1.00 24.50  ? 24  ARG   B CA  1 
ATOM   939  C C   . ARG   B 1 25 ? 23.214  -10.661 -35.017 1.00 24.03  ? 24  ARG   B C   1 
ATOM   940  O O   . ARG   B 1 25 ? 23.603  -10.921 -33.877 1.00 25.31  ? 24  ARG   B O   1 
ATOM   941  C CB  . ARG   B 1 25 ? 21.749  -8.651  -35.505 1.00 27.49  ? 24  ARG   B CB  1 
ATOM   942  C CG  . ARG   B 1 25 ? 22.370  -7.907  -34.326 1.00 27.49  ? 24  ARG   B CG  1 
ATOM   943  C CD  . ARG   B 1 25 ? 22.169  -6.375  -34.445 1.00 26.43  ? 24  ARG   B CD  1 
ATOM   944  N NE  . ARG   B 1 25 ? 22.831  -5.739  -33.299 1.00 28.67  ? 24  ARG   B NE  1 
ATOM   945  C CZ  . ARG   B 1 25 ? 22.549  -4.486  -32.917 1.00 29.32  ? 24  ARG   B CZ  1 
ATOM   946  N NH1 . ARG   B 1 25 ? 21.602  -3.826  -33.550 1.00 28.34  ? 24  ARG   B NH1 1 
ATOM   947  N NH2 . ARG   B 1 25 ? 23.178  -3.946  -31.884 1.00 28.32  ? 24  ARG   B NH2 1 
ATOM   948  N N   . ILE   B 1 26 ? 24.023  -10.725 -36.086 1.00 25.58  ? 25  ILE   B N   1 
ATOM   949  C CA  . ILE   B 1 26 ? 25.442  -10.918 -35.883 1.00 25.47  ? 25  ILE   B CA  1 
ATOM   950  C C   . ILE   B 1 26 ? 26.055  -9.556  -35.555 1.00 29.99  ? 25  ILE   B C   1 
ATOM   951  O O   . ILE   B 1 26 ? 25.858  -8.623  -36.331 1.00 32.68  ? 25  ILE   B O   1 
ATOM   952  C CB  . ILE   B 1 26 ? 26.075  -11.394 -37.205 1.00 29.71  ? 25  ILE   B CB  1 
ATOM   953  C CG1 . ILE   B 1 26 ? 25.373  -12.635 -37.792 1.00 29.50  ? 25  ILE   B CG1 1 
ATOM   954  C CG2 . ILE   B 1 26 ? 27.576  -11.624 -37.034 1.00 34.70  ? 25  ILE   B CG2 1 
ATOM   955  C CD1 . ILE   B 1 26 ? 25.415  -13.870 -36.895 1.00 30.29  ? 25  ILE   B CD1 1 
ATOM   956  N N   . ASP   B 1 27 ? 26.829  -9.514  -34.471 1.00 30.28  ? 26  ASP   B N   1 
ATOM   957  C CA  . ASP   B 1 27 ? 27.510  -8.285  -34.055 1.00 35.75  ? 26  ASP   B CA  1 
ATOM   958  C C   . ASP   B 1 27 ? 28.972  -8.247  -34.509 1.00 41.18  ? 26  ASP   B C   1 
ATOM   959  O O   . ASP   B 1 27 ? 29.550  -9.284  -34.827 1.00 42.28  ? 26  ASP   B O   1 
ATOM   960  C CB  . ASP   B 1 27 ? 27.434  -8.130  -32.552 1.00 31.91  ? 26  ASP   B CB  1 
ATOM   961  C CG  . ASP   B 1 27 ? 26.234  -7.380  -31.997 1.00 38.85  ? 26  ASP   B CG  1 
ATOM   962  O OD1 . ASP   B 1 27 ? 25.452  -6.817  -32.817 1.00 39.93  ? 26  ASP   B OD1 1 
ATOM   963  O OD2 . ASP   B 1 27 ? 26.117  -7.345  -30.735 1.00 36.80  ? 26  ASP   B OD2 1 
ATOM   964  N N   A ASP   B 1 28 ? 29.543  -7.030  -34.495 0.50 48.05  ? 27  ASP   B N   1 
ATOM   965  N N   B ASP   B 1 28 ? 29.570  -7.045  -34.546 0.50 47.42  ? 27  ASP   B N   1 
ATOM   966  C CA  A ASP   B 1 28 ? 30.962  -6.757  -34.679 0.50 55.66  ? 27  ASP   B CA  1 
ATOM   967  C CA  B ASP   B 1 28 ? 30.998  -6.914  -34.807 0.50 54.94  ? 27  ASP   B CA  1 
ATOM   968  C C   A ASP   B 1 28 ? 31.742  -7.252  -33.460 0.50 58.69  ? 27  ASP   B C   1 
ATOM   969  C C   B ASP   B 1 28 ? 31.754  -7.085  -33.486 0.50 60.13  ? 27  ASP   B C   1 
ATOM   970  O O   A ASP   B 1 28 ? 31.149  -7.585  -32.433 0.50 56.01  ? 27  ASP   B O   1 
ATOM   971  O O   B ASP   B 1 28 ? 31.147  -7.033  -32.416 0.50 62.50  ? 27  ASP   B O   1 
ATOM   972  C CB  A ASP   B 1 28 ? 31.198  -5.263  -34.846 0.50 51.73  ? 27  ASP   B CB  1 
ATOM   973  C CB  B ASP   B 1 28 ? 31.327  -5.627  -35.553 0.50 50.13  ? 27  ASP   B CB  1 
ATOM   974  C CG  A ASP   B 1 28 ? 30.352  -4.580  -35.911 0.50 52.84  ? 27  ASP   B CG  1 
ATOM   975  C CG  B ASP   B 1 28 ? 32.373  -5.750  -36.656 0.50 47.67  ? 27  ASP   B CG  1 
ATOM   976  O OD1 A ASP   B 1 28 ? 30.693  -4.706  -37.112 0.50 50.71  ? 27  ASP   B OD1 1 
ATOM   977  O OD1 B ASP   B 1 28 ? 33.299  -6.577  -36.505 0.50 51.91  ? 27  ASP   B OD1 1 
ATOM   978  O OD2 A ASP   B 1 28 ? 29.341  -3.952  -35.530 0.50 50.68  ? 27  ASP   B OD2 1 
ATOM   979  O OD2 B ASP   B 1 28 ? 32.276  -4.990  -37.643 0.50 43.56  ? 27  ASP   B OD2 1 
ATOM   980  N N   . ILE   B 1 29 ? 33.077  -7.290  -33.572 1.00 64.40  ? 28  ILE   B N   1 
ATOM   981  C CA  . ILE   B 1 29 ? 33.898  -7.683  -32.433 1.00 71.21  ? 28  ILE   B CA  1 
ATOM   982  C C   . ILE   B 1 29 ? 34.204  -6.461  -31.570 1.00 86.03  ? 28  ILE   B C   1 
ATOM   983  O O   . ILE   B 1 29 ? 34.524  -6.603  -30.390 1.00 95.16  ? 28  ILE   B O   1 
ATOM   984  C CB  . ILE   B 1 29 ? 35.171  -8.447  -32.853 1.00 66.57  ? 28  ILE   B CB  1 
ATOM   985  N N   . ALA   B 1 30 ? 34.072  -5.266  -32.162 1.00 82.14  ? 29  ALA   B N   1 
ATOM   986  C CA  . ALA   B 1 30 ? 34.387  -4.005  -31.508 1.00 86.62  ? 29  ALA   B CA  1 
ATOM   987  C C   . ALA   B 1 30 ? 35.878  -3.957  -31.151 1.00 79.81  ? 29  ALA   B C   1 
ATOM   988  O O   . ALA   B 1 30 ? 36.551  -2.990  -31.585 1.00 83.95  ? 29  ALA   B O   1 
ATOM   989  C CB  . ALA   B 1 30 ? 33.502  -3.787  -30.291 1.00 89.19  ? 29  ALA   B CB  1 
ATOM   990  N N   . VAL   B 1 34 ? 37.071  -9.851  -25.728 1.00 60.98  ? 33  VAL   B N   1 
ATOM   991  C CA  . VAL   B 1 34 ? 36.859  -11.332 -25.668 1.00 67.13  ? 33  VAL   B CA  1 
ATOM   992  C C   . VAL   B 1 34 ? 36.394  -11.777 -27.047 1.00 71.41  ? 33  VAL   B C   1 
ATOM   993  O O   . VAL   B 1 34 ? 35.235  -11.558 -27.397 1.00 76.02  ? 33  VAL   B O   1 
ATOM   994  C CB  . VAL   B 1 34 ? 35.832  -11.746 -24.591 1.00 68.09  ? 33  VAL   B CB  1 
ATOM   995  C CG1 . VAL   B 1 34 ? 34.570  -10.886 -24.634 1.00 72.70  ? 33  VAL   B CG1 1 
ATOM   996  C CG2 . VAL   B 1 34 ? 35.477  -13.233 -24.668 1.00 59.22  ? 33  VAL   B CG2 1 
ATOM   997  N N   . LYS   B 1 35 ? 37.307  -12.379 -27.823 1.00 66.19  ? 34  LYS   B N   1 
ATOM   998  C CA  . LYS   B 1 35 ? 36.960  -12.893 -29.140 1.00 55.44  ? 34  LYS   B CA  1 
ATOM   999  C C   . LYS   B 1 35 ? 36.087  -14.144 -28.974 1.00 58.62  ? 34  LYS   B C   1 
ATOM   1000 O O   . LYS   B 1 35 ? 36.223  -14.882 -27.994 1.00 57.99  ? 34  LYS   B O   1 
ATOM   1001 C CB  . LYS   B 1 35 ? 38.243  -13.030 -29.966 1.00 52.49  ? 34  LYS   B CB  1 
ATOM   1002 N N   . PRO   B 1 36 ? 35.130  -14.420 -29.897 1.00 52.55  ? 35  PRO   B N   1 
ATOM   1003 C CA  . PRO   B 1 36 ? 34.303  -15.630 -29.796 1.00 47.40  ? 35  PRO   B CA  1 
ATOM   1004 C C   . PRO   B 1 36 ? 35.216  -16.846 -29.740 1.00 42.63  ? 35  PRO   B C   1 
ATOM   1005 O O   . PRO   B 1 36 ? 36.346  -16.769 -30.208 1.00 49.11  ? 35  PRO   B O   1 
ATOM   1006 C CB  . PRO   B 1 36 ? 33.481  -15.620 -31.090 1.00 48.05  ? 35  PRO   B CB  1 
ATOM   1007 C CG  . PRO   B 1 36 ? 34.185  -14.616 -31.989 1.00 56.62  ? 35  PRO   B CG  1 
ATOM   1008 C CD  . PRO   B 1 36 ? 34.810  -13.587 -31.065 1.00 48.34  ? 35  PRO   B CD  1 
ATOM   1009 N N   . PRO   B 1 37 ? 34.773  -17.991 -29.168 1.00 43.52  ? 36  PRO   B N   1 
ATOM   1010 C CA  . PRO   B 1 37 ? 35.520  -19.238 -29.300 1.00 44.75  ? 36  PRO   B CA  1 
ATOM   1011 C C   . PRO   B 1 37 ? 35.574  -19.573 -30.786 1.00 51.01  ? 36  PRO   B C   1 
ATOM   1012 O O   . PRO   B 1 37 ? 34.774  -19.045 -31.575 1.00 46.26  ? 36  PRO   B O   1 
ATOM   1013 C CB  . PRO   B 1 37 ? 34.708  -20.283 -28.509 1.00 47.41  ? 36  PRO   B CB  1 
ATOM   1014 C CG  . PRO   B 1 37 ? 33.736  -19.473 -27.653 1.00 46.77  ? 36  PRO   B CG  1 
ATOM   1015 C CD  . PRO   B 1 37 ? 33.556  -18.133 -28.346 1.00 44.78  ? 36  PRO   B CD  1 
ATOM   1016 N N   . PRO   B 1 38 ? 36.491  -20.480 -31.212 1.00 53.93  ? 37  PRO   B N   1 
ATOM   1017 C CA  . PRO   B 1 38 ? 36.604  -20.863 -32.627 1.00 52.06  ? 37  PRO   B CA  1 
ATOM   1018 C C   . PRO   B 1 38 ? 35.239  -21.239 -33.209 1.00 42.15  ? 37  PRO   B C   1 
ATOM   1019 O O   . PRO   B 1 38 ? 34.429  -21.849 -32.514 1.00 45.45  ? 37  PRO   B O   1 
ATOM   1020 C CB  . PRO   B 1 38 ? 37.567  -22.080 -32.556 1.00 49.65  ? 37  PRO   B CB  1 
ATOM   1021 C CG  . PRO   B 1 38 ? 38.448  -21.773 -31.355 1.00 50.16  ? 37  PRO   B CG  1 
ATOM   1022 C CD  . PRO   B 1 38 ? 37.457  -21.192 -30.348 1.00 56.14  ? 37  PRO   B CD  1 
ATOM   1023 N N   . ASN   B 1 39 ? 34.995  -20.845 -34.467 1.00 44.26  ? 38  ASN   B N   1 
ATOM   1024 C CA  . ASN   B 1 39 ? 33.830  -21.303 -35.227 1.00 45.88  ? 38  ASN   B CA  1 
ATOM   1025 C C   . ASN   B 1 39 ? 32.531  -20.597 -34.827 1.00 41.68  ? 38  ASN   B C   1 
ATOM   1026 O O   . ASN   B 1 39 ? 31.495  -20.841 -35.433 1.00 39.62  ? 38  ASN   B O   1 
ATOM   1027 C CB  . ASN   B 1 39 ? 33.594  -22.807 -35.103 1.00 44.10  ? 38  ASN   B CB  1 
ATOM   1028 C CG  . ASN   B 1 39 ? 34.801  -23.633 -35.490 1.00 56.60  ? 38  ASN   B CG  1 
ATOM   1029 O OD1 . ASN   B 1 39 ? 35.191  -24.536 -34.739 1.00 60.46  ? 38  ASN   B OD1 1 
ATOM   1030 N ND2 . ASN   B 1 39 ? 35.398  -23.352 -36.642 1.00 50.33  ? 38  ASN   B ND2 1 
ATOM   1031 N N   . LYS   B 1 40 ? 32.568  -19.705 -33.825 1.00 43.54  ? 39  LYS   B N   1 
ATOM   1032 C CA  . LYS   B 1 40 ? 31.340  -19.080 -33.361 1.00 38.25  ? 39  LYS   B CA  1 
ATOM   1033 C C   . LYS   B 1 40 ? 31.363  -17.588 -33.641 1.00 35.72  ? 39  LYS   B C   1 
ATOM   1034 O O   . LYS   B 1 40 ? 32.412  -17.052 -33.983 1.00 39.81  ? 39  LYS   B O   1 
ATOM   1035 C CB  . LYS   B 1 40 ? 31.222  -19.297 -31.855 1.00 39.19  ? 39  LYS   B CB  1 
ATOM   1036 C CG  . LYS   B 1 40 ? 31.146  -20.775 -31.525 1.00 38.26  ? 39  LYS   B CG  1 
ATOM   1037 C CD  . LYS   B 1 40 ? 30.899  -20.904 -30.030 1.00 48.70  ? 39  LYS   B CD  1 
ATOM   1038 C CE  . LYS   B 1 40 ? 29.963  -21.977 -29.601 1.00 58.12  ? 39  LYS   B CE  1 
ATOM   1039 N NZ  . LYS   B 1 40 ? 30.426  -23.300 -30.010 1.00 55.73  ? 39  LYS   B NZ  1 
ATOM   1040 N N   . TYR   B 1 41 ? 30.198  -16.951 -33.444 1.00 32.72  ? 40  TYR   B N   1 
ATOM   1041 C CA  . TYR   B 1 41 ? 29.895  -15.573 -33.823 1.00 29.18  ? 40  TYR   B CA  1 
ATOM   1042 C C   . TYR   B 1 41 ? 29.329  -14.863 -32.600 1.00 33.61  ? 40  TYR   B C   1 
ATOM   1043 O O   . TYR   B 1 41 ? 28.591  -15.461 -31.808 1.00 31.15  ? 40  TYR   B O   1 
ATOM   1044 C CB  . TYR   B 1 41 ? 28.853  -15.482 -34.946 1.00 30.12  ? 40  TYR   B CB  1 
ATOM   1045 C CG  . TYR   B 1 41 ? 29.334  -15.952 -36.312 1.00 30.67  ? 40  TYR   B CG  1 
ATOM   1046 C CD1 . TYR   B 1 41 ? 29.953  -15.080 -37.200 1.00 30.98  ? 40  TYR   B CD1 1 
ATOM   1047 C CD2 . TYR   B 1 41 ? 29.171  -17.273 -36.700 1.00 30.16  ? 40  TYR   B CD2 1 
ATOM   1048 C CE1 . TYR   B 1 41 ? 30.386  -15.530 -38.445 1.00 37.59  ? 40  TYR   B CE1 1 
ATOM   1049 C CE2 . TYR   B 1 41 ? 29.589  -17.734 -37.933 1.00 35.08  ? 40  TYR   B CE2 1 
ATOM   1050 C CZ  . TYR   B 1 41 ? 30.193  -16.852 -38.814 1.00 36.40  ? 40  TYR   B CZ  1 
ATOM   1051 O OH  . TYR   B 1 41 ? 30.588  -17.305 -40.048 1.00 33.57  ? 40  TYR   B OH  1 
ATOM   1052 N N   . PRO   B 1 42 ? 29.546  -13.537 -32.454 1.00 33.05  ? 41  PRO   B N   1 
ATOM   1053 C CA  . PRO   B 1 42 ? 28.842  -12.805 -31.402 1.00 29.63  ? 41  PRO   B CA  1 
ATOM   1054 C C   . PRO   B 1 42 ? 27.428  -12.493 -31.871 1.00 30.34  ? 41  PRO   B C   1 
ATOM   1055 O O   . PRO   B 1 42 ? 27.217  -11.853 -32.914 1.00 30.25  ? 41  PRO   B O   1 
ATOM   1056 C CB  . PRO   B 1 42 ? 29.681  -11.529 -31.200 1.00 34.45  ? 41  PRO   B CB  1 
ATOM   1057 C CG  . PRO   B 1 42 ? 30.611  -11.466 -32.392 1.00 35.66  ? 41  PRO   B CG  1 
ATOM   1058 C CD  . PRO   B 1 42 ? 30.411  -12.679 -33.295 1.00 33.32  ? 41  PRO   B CD  1 
ATOM   1059 N N   . ILE   B 1 43 ? 26.465  -12.984 -31.062 1.00 29.85  ? 42  ILE   B N   1 
ATOM   1060 C CA  . ILE   B 1 43 ? 25.037  -12.794 -31.310 1.00 27.80  ? 42  ILE   B CA  1 
ATOM   1061 C C   . ILE   B 1 43 ? 24.462  -11.743 -30.364 1.00 27.25  ? 42  ILE   B C   1 
ATOM   1062 O O   . ILE   B 1 43 ? 24.745  -11.791 -29.194 1.00 30.47  ? 42  ILE   B O   1 
ATOM   1063 C CB  . ILE   B 1 43 ? 24.324  -14.140 -31.133 1.00 27.62  ? 42  ILE   B CB  1 
ATOM   1064 C CG1 . ILE   B 1 43 ? 25.083  -15.202 -31.992 1.00 29.78  ? 42  ILE   B CG1 1 
ATOM   1065 C CG2 . ILE   B 1 43 ? 22.846  -14.012 -31.558 1.00 28.34  ? 42  ILE   B CG2 1 
ATOM   1066 C CD1 . ILE   B 1 43 ? 25.214  -14.859 -33.458 1.00 29.28  ? 42  ILE   B CD1 1 
ATOM   1067 N N   . PHE   B 1 44 ? 23.624  -10.867 -30.903 1.00 27.48  ? 43  PHE   B N   1 
ATOM   1068 C CA  . PHE   B 1 44 ? 22.777  -9.976  -30.110 1.00 27.58  ? 43  PHE   B CA  1 
ATOM   1069 C C   . PHE   B 1 44 ? 21.330  -10.388 -30.329 1.00 26.11  ? 43  PHE   B C   1 
ATOM   1070 O O   . PHE   B 1 44 ? 20.825  -10.391 -31.447 1.00 26.70  ? 43  PHE   B O   1 
ATOM   1071 C CB  . PHE   B 1 44 ? 22.999  -8.527  -30.556 1.00 27.05  ? 43  PHE   B CB  1 
ATOM   1072 C CG  . PHE   B 1 44 ? 22.047  -7.525  -29.905 1.00 26.46  ? 43  PHE   B CG  1 
ATOM   1073 C CD1 . PHE   B 1 44 ? 20.896  -7.100  -30.565 1.00 27.33  ? 43  PHE   B CD1 1 
ATOM   1074 C CD2 . PHE   B 1 44 ? 22.362  -6.944  -28.690 1.00 33.92  ? 43  PHE   B CD2 1 
ATOM   1075 C CE1 . PHE   B 1 44 ? 20.024  -6.182  -29.991 1.00 31.39  ? 43  PHE   B CE1 1 
ATOM   1076 C CE2 . PHE   B 1 44 ? 21.504  -6.001  -28.128 1.00 29.93  ? 43  PHE   B CE2 1 
ATOM   1077 C CZ  . PHE   B 1 44 ? 20.347  -5.633  -28.777 1.00 32.04  ? 43  PHE   B CZ  1 
ATOM   1078 N N   . PHE   B 1 45 ? 20.609  -10.642 -29.219 1.00 25.50  ? 44  PHE   B N   1 
ATOM   1079 C CA  . PHE   B 1 45 ? 19.225  -11.048 -29.265 1.00 25.28  ? 44  PHE   B CA  1 
ATOM   1080 C C   . PHE   B 1 45 ? 18.366  -9.816  -29.103 1.00 25.67  ? 44  PHE   B C   1 
ATOM   1081 O O   . PHE   B 1 45 ? 18.491  -9.085  -28.100 1.00 27.09  ? 44  PHE   B O   1 
ATOM   1082 C CB  . PHE   B 1 45 ? 18.982  -12.035 -28.097 1.00 24.27  ? 44  PHE   B CB  1 
ATOM   1083 C CG  . PHE   B 1 45 ? 19.693  -13.385 -28.207 1.00 25.46  ? 44  PHE   B CG  1 
ATOM   1084 C CD1 . PHE   B 1 45 ? 20.925  -13.597 -27.636 1.00 29.86  ? 44  PHE   B CD1 1 
ATOM   1085 C CD2 . PHE   B 1 45 ? 19.100  -14.434 -28.918 1.00 23.73  ? 44  PHE   B CD2 1 
ATOM   1086 C CE1 . PHE   B 1 45 ? 21.576  -14.817 -27.780 1.00 36.74  ? 44  PHE   B CE1 1 
ATOM   1087 C CE2 . PHE   B 1 45 ? 19.710  -15.663 -29.004 1.00 25.99  ? 44  PHE   B CE2 1 
ATOM   1088 C CZ  . PHE   B 1 45 ? 20.968  -15.841 -28.481 1.00 28.59  ? 44  PHE   B CZ  1 
ATOM   1089 N N   . PHE   B 1 46 ? 17.528  -9.585  -30.118 1.00 24.97  ? 45  PHE   B N   1 
ATOM   1090 C CA  . PHE   B 1 46 ? 16.563  -8.506  -30.102 1.00 24.18  ? 45  PHE   B CA  1 
ATOM   1091 C C   . PHE   B 1 46 ? 15.572  -8.711  -28.941 1.00 25.85  ? 45  PHE   B C   1 
ATOM   1092 O O   . PHE   B 1 46 ? 15.262  -9.836  -28.536 1.00 25.90  ? 45  PHE   B O   1 
ATOM   1093 C CB  . PHE   B 1 46 ? 15.819  -8.308  -31.420 1.00 23.24  ? 45  PHE   B CB  1 
ATOM   1094 C CG  . PHE   B 1 46 ? 16.776  -7.866  -32.518 1.00 25.82  ? 45  PHE   B CG  1 
ATOM   1095 C CD1 . PHE   B 1 46 ? 17.274  -6.544  -32.492 1.00 27.39  ? 45  PHE   B CD1 1 
ATOM   1096 C CD2 . PHE   B 1 46 ? 17.070  -8.720  -33.598 1.00 25.16  ? 45  PHE   B CD2 1 
ATOM   1097 C CE1 . PHE   B 1 46 ? 18.147  -6.137  -33.501 1.00 26.47  ? 45  PHE   B CE1 1 
ATOM   1098 C CE2 . PHE   B 1 46 ? 17.903  -8.269  -34.639 1.00 26.21  ? 45  PHE   B CE2 1 
ATOM   1099 C CZ  . PHE   B 1 46 ? 18.423  -6.982  -34.562 1.00 26.37  ? 45  PHE   B CZ  1 
ATOM   1100 N N   . GLY   B 1 47 ? 15.082  -7.586  -28.433 1.00 26.40  ? 46  GLY   B N   1 
ATOM   1101 C CA  . GLY   B 1 47 ? 14.036  -7.675  -27.408 1.00 26.08  ? 46  GLY   B CA  1 
ATOM   1102 C C   . GLY   B 1 47 ? 14.657  -7.767  -26.014 1.00 27.00  ? 46  GLY   B C   1 
ATOM   1103 O O   . GLY   B 1 47 ? 14.426  -6.891  -25.173 1.00 32.08  ? 46  GLY   B O   1 
ATOM   1104 N N   . THR   B 1 48 ? 15.381  -8.844  -25.732 1.00 26.85  ? 47  THR   B N   1 
ATOM   1105 C CA  . THR   B 1 48 ? 16.075  -9.079  -24.476 1.00 28.21  ? 47  THR   B CA  1 
ATOM   1106 C C   . THR   B 1 48 ? 17.344  -8.232  -24.401 1.00 27.35  ? 47  THR   B C   1 
ATOM   1107 O O   . THR   B 1 48 ? 17.786  -7.835  -23.307 1.00 30.97  ? 47  THR   B O   1 
ATOM   1108 C CB  . THR   B 1 48 ? 16.378  -10.565 -24.214 1.00 32.66  ? 47  THR   B CB  1 
ATOM   1109 O OG1 . THR   B 1 48 ? 17.400  -11.044 -25.109 1.00 30.36  ? 47  THR   B OG1 1 
ATOM   1110 C CG2 . THR   B 1 48 ? 15.115  -11.416 -24.197 1.00 27.88  ? 47  THR   B CG2 1 
ATOM   1111 N N   . HIS   B 1 49 ? 17.946  -7.974  -25.568 1.00 28.25  ? 48  HIS   B N   1 
ATOM   1112 C CA  . HIS   B 1 49 ? 19.243  -7.338  -25.699 1.00 31.50  ? 48  HIS   B CA  1 
ATOM   1113 C C   . HIS   B 1 49 ? 20.317  -8.148  -25.001 1.00 31.81  ? 48  HIS   B C   1 
ATOM   1114 O O   . HIS   B 1 49 ? 21.339  -7.579  -24.611 1.00 36.90  ? 48  HIS   B O   1 
ATOM   1115 C CB  . HIS   B 1 49 ? 19.247  -5.855  -25.273 1.00 30.37  ? 48  HIS   B CB  1 
ATOM   1116 C CG  . HIS   B 1 49 ? 18.066  -5.131  -25.814 1.00 31.59  ? 48  HIS   B CG  1 
ATOM   1117 N ND1 . HIS   B 1 49 ? 17.287  -4.303  -25.035 1.00 33.12  ? 48  HIS   B ND1 1 
ATOM   1118 C CD2 . HIS   B 1 49 ? 17.450  -5.181  -27.005 1.00 28.70  ? 48  HIS   B CD2 1 
ATOM   1119 C CE1 . HIS   B 1 49 ? 16.252  -3.871  -25.745 1.00 37.26  ? 48  HIS   B CE1 1 
ATOM   1120 N NE2 . HIS   B 1 49 ? 16.342  -4.392  -26.965 1.00 32.25  ? 48  HIS   B NE2 1 
ATOM   1121 N N   . GLU   B 1 50 ? 20.121  -9.467  -24.862 1.00 30.05  ? 49  GLU   B N   1 
ATOM   1122 C CA  . GLU   B 1 50 ? 21.162  -10.347 -24.359 1.00 30.20  ? 49  GLU   B CA  1 
ATOM   1123 C C   . GLU   B 1 50 ? 22.173  -10.686 -25.477 1.00 29.46  ? 49  GLU   B C   1 
ATOM   1124 O O   . GLU   B 1 50 ? 21.905  -10.492 -26.680 1.00 30.62  ? 49  GLU   B O   1 
ATOM   1125 C CB  . GLU   B 1 50 ? 20.523  -11.640 -23.840 1.00 35.04  ? 49  GLU   B CB  1 
ATOM   1126 C CG  . GLU   B 1 50 ? 19.739  -11.455 -22.539 1.00 41.81  ? 49  GLU   B CG  1 
ATOM   1127 C CD  . GLU   B 1 50 ? 20.673  -11.360 -21.339 1.00 54.33  ? 49  GLU   B CD  1 
ATOM   1128 O OE1 . GLU   B 1 50 ? 21.377  -12.339 -21.028 1.00 61.25  ? 49  GLU   B OE1 1 
ATOM   1129 O OE2 . GLU   B 1 50 ? 20.739  -10.284 -20.720 1.00 67.97  ? 49  GLU   B OE2 1 
ATOM   1130 N N   . THR   B 1 51 ? 23.311  -11.224 -25.056 1.00 28.95  ? 50  THR   B N   1 
ATOM   1131 C CA  . THR   B 1 51 ? 24.375  -11.629 -25.982 1.00 31.43  ? 50  THR   B CA  1 
ATOM   1132 C C   . THR   B 1 51 ? 24.853  -13.041 -25.656 1.00 35.32  ? 50  THR   B C   1 
ATOM   1133 O O   . THR   B 1 51 ? 24.711  -13.539 -24.535 1.00 36.88  ? 50  THR   B O   1 
ATOM   1134 C CB  . THR   B 1 51 ? 25.518  -10.601 -26.076 1.00 35.54  ? 50  THR   B CB  1 
ATOM   1135 O OG1 . THR   B 1 51 ? 26.126  -10.544 -24.796 1.00 37.65  ? 50  THR   B OG1 1 
ATOM   1136 C CG2 . THR   B 1 51 ? 25.078  -9.212  -26.506 1.00 30.87  ? 50  THR   B CG2 1 
ATOM   1137 N N   . ALA   B 1 52 ? 25.341  -13.749 -26.686 1.00 34.60  ? 51  ALA   B N   1 
ATOM   1138 C CA  . ALA   B 1 52 ? 25.964  -15.050 -26.544 1.00 35.95  ? 51  ALA   B CA  1 
ATOM   1139 C C   . ALA   B 1 52 ? 26.859  -15.303 -27.758 1.00 31.53  ? 51  ALA   B C   1 
ATOM   1140 O O   . ALA   B 1 52 ? 26.800  -14.550 -28.741 1.00 31.05  ? 51  ALA   B O   1 
ATOM   1141 C CB  . ALA   B 1 52 ? 24.933  -16.152 -26.365 1.00 34.83  ? 51  ALA   B CB  1 
ATOM   1142 N N   . PHE   B 1 53 ? 27.701  -16.343 -27.644 1.00 33.49  ? 52  PHE   B N   1 
ATOM   1143 C CA  . PHE   B 1 53 ? 28.444  -16.844 -28.789 1.00 32.95  ? 52  PHE   B CA  1 
ATOM   1144 C C   . PHE   B 1 53 ? 27.768  -18.114 -29.310 1.00 32.21  ? 52  PHE   B C   1 
ATOM   1145 O O   . PHE   B 1 53 ? 27.555  -19.085 -28.565 1.00 35.37  ? 52  PHE   B O   1 
ATOM   1146 C CB  . PHE   B 1 53 ? 29.896  -17.126 -28.382 1.00 33.31  ? 52  PHE   B CB  1 
ATOM   1147 C CG  . PHE   B 1 53 ? 30.683  -15.924 -27.880 1.00 35.82  ? 52  PHE   B CG  1 
ATOM   1148 C CD1 . PHE   B 1 53 ? 30.998  -14.878 -28.739 1.00 37.21  ? 52  PHE   B CD1 1 
ATOM   1149 C CD2 . PHE   B 1 53 ? 31.109  -15.853 -26.559 1.00 41.55  ? 52  PHE   B CD2 1 
ATOM   1150 C CE1 . PHE   B 1 53 ? 31.721  -13.781 -28.309 1.00 43.39  ? 52  PHE   B CE1 1 
ATOM   1151 C CE2 . PHE   B 1 53 ? 31.829  -14.747 -26.122 1.00 44.27  ? 52  PHE   B CE2 1 
ATOM   1152 C CZ  . PHE   B 1 53 ? 32.136  -13.725 -26.992 1.00 42.08  ? 52  PHE   B CZ  1 
ATOM   1153 N N   . LEU   B 1 54 ? 27.443  -18.126 -30.613 1.00 31.31  ? 53  LEU   B N   1 
ATOM   1154 C CA  . LEU   B 1 54 ? 26.830  -19.302 -31.200 1.00 27.74  ? 53  LEU   B CA  1 
ATOM   1155 C C   . LEU   B 1 54 ? 27.562  -19.672 -32.490 1.00 29.49  ? 53  LEU   B C   1 
ATOM   1156 O O   . LEU   B 1 54 ? 28.044  -18.790 -33.209 1.00 31.63  ? 53  LEU   B O   1 
ATOM   1157 C CB  . LEU   B 1 54 ? 25.336  -19.139 -31.512 1.00 28.91  ? 53  LEU   B CB  1 
ATOM   1158 C CG  . LEU   B 1 54 ? 24.405  -18.998 -30.306 1.00 30.07  ? 53  LEU   B CG  1 
ATOM   1159 C CD1 . LEU   B 1 54 ? 22.993  -18.671 -30.775 1.00 30.56  ? 53  LEU   B CD1 1 
ATOM   1160 C CD2 . LEU   B 1 54 ? 24.494  -20.356 -29.615 1.00 36.64  ? 53  LEU   B CD2 1 
ATOM   1161 N N   . GLY   B 1 55 ? 27.507  -20.974 -32.809 1.00 31.91  ? 54  GLY   B N   1 
ATOM   1162 C CA  . GLY   B 1 55 ? 28.044  -21.543 -34.038 1.00 30.45  ? 54  GLY   B CA  1 
ATOM   1163 C C   . GLY   B 1 55 ? 26.969  -21.546 -35.124 1.00 28.83  ? 54  GLY   B C   1 
ATOM   1164 O O   . GLY   B 1 55 ? 25.770  -21.412 -34.853 1.00 28.64  ? 54  GLY   B O   1 
ATOM   1165 N N   . PRO   B 1 56 ? 27.333  -21.736 -36.409 1.00 27.93  ? 55  PRO   B N   1 
ATOM   1166 C CA  . PRO   B 1 56 ? 26.335  -21.811 -37.464 1.00 26.38  ? 55  PRO   B CA  1 
ATOM   1167 C C   . PRO   B 1 56 ? 25.183  -22.799 -37.363 1.00 25.32  ? 55  PRO   B C   1 
ATOM   1168 O O   . PRO   B 1 56 ? 24.158  -22.557 -37.972 1.00 26.81  ? 55  PRO   B O   1 
ATOM   1169 C CB  . PRO   B 1 56 ? 27.167  -22.079 -38.757 1.00 29.29  ? 55  PRO   B CB  1 
ATOM   1170 C CG  . PRO   B 1 56 ? 28.600  -22.053 -38.371 1.00 32.29  ? 55  PRO   B CG  1 
ATOM   1171 C CD  . PRO   B 1 56 ? 28.724  -21.795 -36.896 1.00 31.54  ? 55  PRO   B CD  1 
ATOM   1172 N N   . LYS   B 1 57 ? 25.372  -23.918 -36.649 1.00 26.17  ? 56  LYS   B N   1 
ATOM   1173 C CA  . LYS   B 1 57 ? 24.281  -24.891 -36.562 1.00 25.88  ? 56  LYS   B CA  1 
ATOM   1174 C C   . LYS   B 1 57 ? 23.044  -24.292 -35.901 1.00 28.79  ? 56  LYS   B C   1 
ATOM   1175 O O   . LYS   B 1 57 ? 21.929  -24.776 -36.128 1.00 27.87  ? 56  LYS   B O   1 
ATOM   1176 C CB  . LYS   B 1 57 ? 24.714  -26.176 -35.837 1.00 33.28  ? 56  LYS   B CB  1 
ATOM   1177 C CG  . LYS   B 1 57 ? 24.835  -26.069 -34.331 1.00 38.04  ? 56  LYS   B CG  1 
ATOM   1178 C CD  . LYS   B 1 57 ? 24.878  -27.464 -33.697 1.00 41.98  ? 56  LYS   B CD  1 
ATOM   1179 C CE  . LYS   B 1 57 ? 25.170  -27.462 -32.211 1.00 43.77  ? 56  LYS   B CE  1 
ATOM   1180 N NZ  . LYS   B 1 57 ? 24.139  -26.840 -31.373 1.00 50.18  ? 56  LYS   B NZ  1 
ATOM   1181 N N   . ASP   B 1 58 ? 23.266  -23.191 -35.156 1.00 26.08  ? 57  ASP   B N   1 
ATOM   1182 C CA  . ASP   B 1 58 ? 22.192  -22.576 -34.390 1.00 26.34  ? 57  ASP   B CA  1 
ATOM   1183 C C   . ASP   B 1 58 ? 21.760  -21.253 -35.018 1.00 26.31  ? 57  ASP   B C   1 
ATOM   1184 O O   . ASP   B 1 58 ? 21.048  -20.489 -34.348 1.00 25.91  ? 57  ASP   B O   1 
ATOM   1185 C CB  . ASP   B 1 58 ? 22.682  -22.412 -32.966 1.00 27.33  ? 57  ASP   B CB  1 
ATOM   1186 C CG  . ASP   B 1 58 ? 22.822  -23.738 -32.220 1.00 31.75  ? 57  ASP   B CG  1 
ATOM   1187 O OD1 . ASP   B 1 58 ? 21.862  -24.574 -32.346 1.00 32.88  ? 57  ASP   B OD1 1 
ATOM   1188 O OD2 . ASP   B 1 58 ? 23.828  -23.886 -31.486 1.00 36.50  ? 57  ASP   B OD2 1 
ATOM   1189 N N   . LEU   B 1 59 ? 22.271  -20.920 -36.229 1.00 24.93  ? 58  LEU   B N   1 
ATOM   1190 C CA  . LEU   B 1 59 ? 21.975  -19.623 -36.839 1.00 24.80  ? 58  LEU   B CA  1 
ATOM   1191 C C   . LEU   B 1 59 ? 21.221  -19.828 -38.137 1.00 23.48  ? 58  LEU   B C   1 
ATOM   1192 O O   . LEU   B 1 59 ? 21.702  -20.514 -39.058 1.00 26.03  ? 58  LEU   B O   1 
ATOM   1193 C CB  . LEU   B 1 59 ? 23.306  -18.908 -37.063 1.00 25.74  ? 58  LEU   B CB  1 
ATOM   1194 C CG  . LEU   B 1 59 ? 24.134  -18.649 -35.808 1.00 24.44  ? 58  LEU   B CG  1 
ATOM   1195 C CD1 . LEU   B 1 59 ? 25.443  -17.920 -36.125 1.00 27.77  ? 58  LEU   B CD1 1 
ATOM   1196 C CD2 . LEU   B 1 59 ? 23.350  -17.750 -34.826 1.00 27.54  ? 58  LEU   B CD2 1 
ATOM   1197 N N   . PHE   B 1 60 ? 20.051  -19.223 -38.224 1.00 22.75  ? 59  PHE   B N   1 
ATOM   1198 C CA  . PHE   B 1 60 ? 19.115  -19.407 -39.320 1.00 24.88  ? 59  PHE   B CA  1 
ATOM   1199 C C   . PHE   B 1 60 ? 18.920  -18.057 -40.015 1.00 24.56  ? 59  PHE   B C   1 
ATOM   1200 O O   . PHE   B 1 60 ? 18.345  -17.133 -39.442 1.00 25.04  ? 59  PHE   B O   1 
ATOM   1201 C CB  . PHE   B 1 60 ? 17.780  -19.943 -38.765 1.00 23.22  ? 59  PHE   B CB  1 
ATOM   1202 C CG  . PHE   B 1 60 ? 17.896  -21.340 -38.143 1.00 23.28  ? 59  PHE   B CG  1 
ATOM   1203 C CD1 . PHE   B 1 60 ? 18.455  -21.492 -36.877 1.00 25.97  ? 59  PHE   B CD1 1 
ATOM   1204 C CD2 . PHE   B 1 60 ? 17.437  -22.451 -38.847 1.00 26.98  ? 59  PHE   B CD2 1 
ATOM   1205 C CE1 . PHE   B 1 60 ? 18.584  -22.749 -36.311 1.00 28.73  ? 59  PHE   B CE1 1 
ATOM   1206 C CE2 . PHE   B 1 60 ? 17.569  -23.720 -38.278 1.00 26.66  ? 59  PHE   B CE2 1 
ATOM   1207 C CZ  . PHE   B 1 60 ? 18.155  -23.852 -37.025 1.00 28.16  ? 59  PHE   B CZ  1 
ATOM   1208 N N   . PRO   B 1 61 ? 19.447  -17.829 -41.244 1.00 27.84  ? 60  PRO   B N   1 
ATOM   1209 C CA  . PRO   B 1 61 ? 19.223  -16.539 -41.922 1.00 27.12  ? 60  PRO   B CA  1 
ATOM   1210 C C   . PRO   B 1 61 ? 17.760  -16.070 -41.890 1.00 24.79  ? 60  PRO   B C   1 
ATOM   1211 O O   . PRO   B 1 61 ? 16.816  -16.812 -42.160 1.00 29.03  ? 60  PRO   B O   1 
ATOM   1212 C CB  . PRO   B 1 61 ? 19.731  -16.862 -43.345 1.00 29.49  ? 60  PRO   B CB  1 
ATOM   1213 C CG  . PRO   B 1 61 ? 20.852  -17.852 -43.120 1.00 36.43  ? 60  PRO   B CG  1 
ATOM   1214 C CD  . PRO   B 1 61 ? 20.305  -18.778 -41.996 1.00 33.16  ? 60  PRO   B CD  1 
ATOM   1215 N N   . TYR   B 1 62 ? 17.553  -14.757 -41.553 1.00 27.17  ? 61  TYR   B N   1 
ATOM   1216 C CA  . TYR   B 1 62 ? 16.245  -14.234 -41.220 1.00 27.42  ? 61  TYR   B CA  1 
ATOM   1217 C C   . TYR   B 1 62 ? 15.259  -14.274 -42.370 1.00 29.44  ? 61  TYR   B C   1 
ATOM   1218 O O   . TYR   B 1 62 ? 14.125  -14.695 -42.165 1.00 31.49  ? 61  TYR   B O   1 
ATOM   1219 C CB  . TYR   B 1 62 ? 16.432  -12.789 -40.724 1.00 29.90  ? 61  TYR   B CB  1 
ATOM   1220 C CG  . TYR   B 1 62 ? 15.108  -12.076 -40.484 1.00 31.61  ? 61  TYR   B CG  1 
ATOM   1221 C CD1 . TYR   B 1 62 ? 14.362  -12.311 -39.344 1.00 33.53  ? 61  TYR   B CD1 1 
ATOM   1222 C CD2 . TYR   B 1 62 ? 14.673  -11.076 -41.351 1.00 38.78  ? 61  TYR   B CD2 1 
ATOM   1223 C CE1 . TYR   B 1 62 ? 13.172  -11.644 -39.115 1.00 33.97  ? 61  TYR   B CE1 1 
ATOM   1224 C CE2 . TYR   B 1 62 ? 13.502  -10.366 -41.118 1.00 38.78  ? 61  TYR   B CE2 1 
ATOM   1225 C CZ  . TYR   B 1 62 ? 12.749  -10.658 -39.992 1.00 41.32  ? 61  TYR   B CZ  1 
ATOM   1226 O OH  . TYR   B 1 62 ? 11.593  -9.989  -39.769 1.00 39.61  ? 61  TYR   B OH  1 
ATOM   1227 N N   . ASP   B 1 63 ? 15.696  -13.832 -43.572 1.00 33.64  ? 62  ASP   B N   1 
ATOM   1228 C CA  . ASP   B 1 63 ? 14.867  -13.851 -44.777 1.00 39.38  ? 62  ASP   B CA  1 
ATOM   1229 C C   . ASP   B 1 63 ? 14.288  -15.238 -45.053 1.00 30.96  ? 62  ASP   B C   1 
ATOM   1230 O O   . ASP   B 1 63 ? 13.075  -15.389 -45.151 1.00 41.78  ? 62  ASP   B O   1 
ATOM   1231 C CB  . ASP   B 1 63 ? 15.578  -13.232 -45.969 1.00 45.08  ? 62  ASP   B CB  1 
ATOM   1232 C CG  . ASP   B 1 63 ? 15.419  -11.726 -46.094 1.00 61.58  ? 62  ASP   B CG  1 
ATOM   1233 O OD1 . ASP   B 1 63 ? 14.619  -11.150 -45.316 1.00 65.56  ? 62  ASP   B OD1 1 
ATOM   1234 O OD2 . ASP   B 1 63 ? 16.103  -11.139 -46.964 1.00 72.73  ? 62  ASP   B OD2 1 
ATOM   1235 N N   . LYS   B 1 64 ? 15.158  -16.233 -45.134 1.00 36.89  ? 63  LYS   B N   1 
ATOM   1236 C CA  . LYS   B 1 64 ? 14.768  -17.612 -45.356 1.00 37.93  ? 63  LYS   B CA  1 
ATOM   1237 C C   . LYS   B 1 64 ? 13.776  -18.096 -44.293 1.00 34.58  ? 63  LYS   B C   1 
ATOM   1238 O O   . LYS   B 1 64 ? 12.854  -18.845 -44.615 1.00 38.49  ? 63  LYS   B O   1 
ATOM   1239 C CB  . LYS   B 1 64 ? 16.028  -18.487 -45.339 1.00 41.96  ? 63  LYS   B CB  1 
ATOM   1240 C CG  . LYS   B 1 64 ? 15.749  -19.950 -45.651 1.00 40.79  ? 63  LYS   B CG  1 
ATOM   1241 C CD  . LYS   B 1 64 ? 17.002  -20.765 -45.904 1.00 47.21  ? 63  LYS   B CD  1 
ATOM   1242 C CE  . LYS   B 1 64 ? 16.712  -21.968 -46.765 1.00 51.38  ? 63  LYS   B CE  1 
ATOM   1243 N NZ  . LYS   B 1 64 ? 15.787  -22.898 -46.127 1.00 42.80  ? 63  LYS   B NZ  1 
ATOM   1244 N N   . SER   B 1 65 ? 13.943  -17.648 -43.045 1.00 34.01  ? 64  SER   B N   1 
ATOM   1245 C CA  . SER   B 1 65 ? 13.331  -18.379 -41.925 1.00 35.45  ? 64  SER   B CA  1 
ATOM   1246 C C   . SER   B 1 65 ? 12.195  -17.631 -41.210 1.00 34.49  ? 64  SER   B C   1 
ATOM   1247 O O   . SER   B 1 65 ? 11.568  -18.165 -40.302 1.00 36.18  ? 64  SER   B O   1 
ATOM   1248 C CB  . SER   B 1 65 ? 14.404  -18.883 -41.002 1.00 38.78  ? 64  SER   B CB  1 
ATOM   1249 O OG  . SER   B 1 65 ? 15.206  -17.816 -40.520 1.00 56.35  ? 64  SER   B OG  1 
ATOM   1250 N N   . LYS   B 1 66 ? 11.855  -16.411 -41.647 1.00 35.29  ? 65  LYS   B N   1 
ATOM   1251 C CA  . LYS   B 1 66 ? 10.953  -15.600 -40.835 1.00 32.99  ? 65  LYS   B CA  1 
ATOM   1252 C C   . LYS   B 1 66 ? 9.514   -16.109 -40.838 1.00 38.86  ? 65  LYS   B C   1 
ATOM   1253 O O   . LYS   B 1 66 ? 8.787   -15.951 -39.847 1.00 37.24  ? 65  LYS   B O   1 
ATOM   1254 C CB  . LYS   B 1 66 ? 11.042  -14.113 -41.203 1.00 31.85  ? 65  LYS   B CB  1 
ATOM   1255 C CG  . LYS   B 1 66 ? 10.504  -13.805 -42.603 1.00 35.27  ? 65  LYS   B CG  1 
ATOM   1256 N N   . ASP   B 1 67 ? 9.052   -16.677 -41.946 1.00 38.31  ? 66  ASP   B N   1 
ATOM   1257 C CA  . ASP   B 1 67 ? 7.659   -17.080 -41.920 1.00 42.91  ? 66  ASP   B CA  1 
ATOM   1258 C C   . ASP   B 1 67 ? 7.497   -18.247 -40.940 1.00 42.95  ? 66  ASP   B C   1 
ATOM   1259 O O   . ASP   B 1 67 ? 6.450   -18.383 -40.292 1.00 47.32  ? 66  ASP   B O   1 
ATOM   1260 C CB  . ASP   B 1 67 ? 7.041   -17.130 -43.310 1.00 51.87  ? 66  ASP   B CB  1 
ATOM   1261 C CG  . ASP   B 1 67 ? 7.670   -18.104 -44.290 1.00 69.67  ? 66  ASP   B CG  1 
ATOM   1262 O OD1 . ASP   B 1 67 ? 7.999   -17.665 -45.420 1.00 81.61  ? 66  ASP   B OD1 1 
ATOM   1263 O OD2 . ASP   B 1 67 ? 7.804   -19.292 -43.924 1.00 82.21  ? 66  ASP   B OD2 1 
ATOM   1264 N N   . LYS   B 1 68 ? 8.553   -19.059 -40.809 1.00 38.72  ? 67  LYS   B N   1 
ATOM   1265 C CA  . LYS   B 1 68 ? 8.525   -20.220 -39.934 1.00 33.18  ? 67  LYS   B CA  1 
ATOM   1266 C C   . LYS   B 1 68 ? 8.707   -19.840 -38.461 1.00 33.81  ? 67  LYS   B C   1 
ATOM   1267 O O   . LYS   B 1 68 ? 7.969   -20.339 -37.612 1.00 34.50  ? 67  LYS   B O   1 
ATOM   1268 C CB  . LYS   B 1 68 ? 9.618   -21.219 -40.326 1.00 33.71  ? 67  LYS   B CB  1 
ATOM   1269 C CG  . LYS   B 1 68 ? 9.713   -22.491 -39.485 1.00 40.16  ? 67  LYS   B CG  1 
ATOM   1270 C CD  . LYS   B 1 68 ? 10.616  -23.518 -40.171 1.00 47.82  ? 67  LYS   B CD  1 
ATOM   1271 C CE  . LYS   B 1 68 ? 10.802  -24.794 -39.417 1.00 50.24  ? 67  LYS   B CE  1 
ATOM   1272 N NZ  . LYS   B 1 68 ? 9.526   -25.469 -39.154 1.00 60.11  ? 67  LYS   B NZ  1 
ATOM   1273 N N   . TYR   B 1 69 ? 9.704   -19.006 -38.147 1.00 30.11  ? 68  TYR   B N   1 
ATOM   1274 C CA  . TYR   B 1 69 ? 10.101  -18.716 -36.768 1.00 26.89  ? 68  TYR   B CA  1 
ATOM   1275 C C   . TYR   B 1 69 ? 9.624   -17.342 -36.286 1.00 29.61  ? 68  TYR   B C   1 
ATOM   1276 O O   . TYR   B 1 69 ? 9.698   -17.065 -35.083 1.00 33.19  ? 68  TYR   B O   1 
ATOM   1277 C CB  . TYR   B 1 69 ? 11.620  -18.782 -36.626 1.00 27.48  ? 68  TYR   B CB  1 
ATOM   1278 C CG  . TYR   B 1 69 ? 12.242  -20.148 -36.897 1.00 31.50  ? 68  TYR   B CG  1 
ATOM   1279 C CD1 . TYR   B 1 69 ? 11.724  -21.298 -36.310 1.00 30.50  ? 68  TYR   B CD1 1 
ATOM   1280 C CD2 . TYR   B 1 69 ? 13.335  -20.288 -37.745 1.00 32.80  ? 68  TYR   B CD2 1 
ATOM   1281 C CE1 . TYR   B 1 69 ? 12.275  -22.553 -36.560 1.00 32.09  ? 68  TYR   B CE1 1 
ATOM   1282 C CE2 . TYR   B 1 69 ? 13.867  -21.538 -38.040 1.00 34.33  ? 68  TYR   B CE2 1 
ATOM   1283 C CZ  . TYR   B 1 69 ? 13.360  -22.667 -37.410 1.00 34.13  ? 68  TYR   B CZ  1 
ATOM   1284 O OH  . TYR   B 1 69 ? 13.879  -23.900 -37.682 1.00 34.30  ? 68  TYR   B OH  1 
ATOM   1285 N N   . GLY   B 1 70 ? 9.192   -16.449 -37.190 1.00 31.02  ? 69  GLY   B N   1 
ATOM   1286 C CA  . GLY   B 1 70 ? 8.867   -15.085 -36.786 1.00 35.38  ? 69  GLY   B CA  1 
ATOM   1287 C C   . GLY   B 1 70 ? 7.441   -14.884 -36.250 1.00 37.88  ? 69  GLY   B C   1 
ATOM   1288 O O   . GLY   B 1 70 ? 6.817   -13.863 -36.534 1.00 39.00  ? 69  GLY   B O   1 
ATOM   1289 N N   . LYS   B 1 71 ? 6.906   -15.855 -35.491 1.00 37.24  ? 70  LYS   B N   1 
ATOM   1290 C CA  . LYS   B 1 71 ? 5.542   -15.721 -34.995 1.00 40.90  ? 70  LYS   B CA  1 
ATOM   1291 C C   . LYS   B 1 71 ? 5.604   -15.277 -33.541 1.00 41.49  ? 70  LYS   B C   1 
ATOM   1292 O O   . LYS   B 1 71 ? 6.505   -15.673 -32.790 1.00 35.52  ? 70  LYS   B O   1 
ATOM   1293 C CB  . LYS   B 1 71 ? 4.705   -17.006 -35.049 1.00 44.66  ? 70  LYS   B CB  1 
ATOM   1294 C CG  . LYS   B 1 71 ? 4.033   -17.283 -36.397 1.00 56.84  ? 70  LYS   B CG  1 
ATOM   1295 C CD  . LYS   B 1 71 ? 4.832   -18.260 -37.249 1.00 63.59  ? 70  LYS   B CD  1 
ATOM   1296 C CE  . LYS   B 1 71 ? 4.020   -18.933 -38.315 1.00 68.08  ? 70  LYS   B CE  1 
ATOM   1297 N NZ  . LYS   B 1 71 ? 3.793   -18.031 -39.447 1.00 77.12  ? 70  LYS   B NZ  1 
ATOM   1298 N N   . PRO   B 1 72 ? 4.653   -14.437 -33.086 1.00 41.94  ? 71  PRO   B N   1 
ATOM   1299 C CA  . PRO   B 1 72 ? 4.620   -14.066 -31.670 1.00 37.60  ? 71  PRO   B CA  1 
ATOM   1300 C C   . PRO   B 1 72 ? 4.461   -15.250 -30.722 1.00 34.03  ? 71  PRO   B C   1 
ATOM   1301 O O   . PRO   B 1 72 ? 3.884   -16.296 -31.066 1.00 37.58  ? 71  PRO   B O   1 
ATOM   1302 C CB  . PRO   B 1 72 ? 3.475   -13.053 -31.563 1.00 39.57  ? 71  PRO   B CB  1 
ATOM   1303 C CG  . PRO   B 1 72 ? 3.342   -12.537 -32.973 1.00 44.03  ? 71  PRO   B CG  1 
ATOM   1304 C CD  . PRO   B 1 72 ? 3.670   -13.708 -33.905 1.00 37.81  ? 71  PRO   B CD  1 
ATOM   1305 N N   . ASN   B 1 73 ? 4.996   -15.060 -29.516 1.00 36.52  ? 72  ASN   B N   1 
ATOM   1306 C CA  . ASN   B 1 73 ? 4.821   -16.028 -28.448 1.00 33.95  ? 72  ASN   B CA  1 
ATOM   1307 C C   . ASN   B 1 73 ? 4.785   -15.290 -27.099 1.00 37.84  ? 72  ASN   B C   1 
ATOM   1308 O O   . ASN   B 1 73 ? 4.851   -14.052 -27.042 1.00 39.64  ? 72  ASN   B O   1 
ATOM   1309 C CB  . ASN   B 1 73 ? 5.848   -17.159 -28.508 1.00 33.73  ? 72  ASN   B CB  1 
ATOM   1310 C CG  . ASN   B 1 73 ? 7.283   -16.750 -28.246 1.00 32.65  ? 72  ASN   B CG  1 
ATOM   1311 O OD1 . ASN   B 1 73 ? 7.583   -16.055 -27.261 1.00 31.80  ? 72  ASN   B OD1 1 
ATOM   1312 N ND2 . ASN   B 1 73 ? 8.190   -17.186 -29.121 1.00 30.22  ? 72  ASN   B ND2 1 
ATOM   1313 N N   . LYS   B 1 74 ? 4.738   -16.067 -26.013 1.00 38.41  ? 73  LYS   B N   1 
ATOM   1314 C CA  . LYS   B 1 74 ? 4.596   -15.527 -24.663 1.00 41.35  ? 73  LYS   B CA  1 
ATOM   1315 C C   . LYS   B 1 74 ? 5.937   -15.474 -23.906 1.00 37.65  ? 73  LYS   B C   1 
ATOM   1316 O O   . LYS   B 1 74 ? 5.953   -15.226 -22.689 1.00 37.07  ? 73  LYS   B O   1 
ATOM   1317 C CB  . LYS   B 1 74 ? 3.450   -16.279 -23.943 1.00 38.06  ? 73  LYS   B CB  1 
ATOM   1318 N N   . ARG   B 1 75 ? 7.083   -15.713 -24.585 1.00 31.19  ? 74  ARG   B N   1 
ATOM   1319 C CA  . ARG   B 1 75 ? 8.369   -15.536 -23.920 1.00 29.93  ? 74  ARG   B CA  1 
ATOM   1320 C C   . ARG   B 1 75 ? 8.695   -14.038 -23.752 1.00 31.44  ? 74  ARG   B C   1 
ATOM   1321 O O   . ARG   B 1 75 ? 8.504   -13.197 -24.636 1.00 30.33  ? 74  ARG   B O   1 
ATOM   1322 C CB  . ARG   B 1 75 ? 9.512   -16.321 -24.594 1.00 28.42  ? 74  ARG   B CB  1 
ATOM   1323 C CG  . ARG   B 1 75 ? 9.379   -17.830 -24.821 1.00 29.65  ? 74  ARG   B CG  1 
ATOM   1324 C CD  . ARG   B 1 75 ? 9.280   -18.630 -23.517 1.00 32.99  ? 74  ARG   B CD  1 
ATOM   1325 N NE  . ARG   B 1 75 ? 9.478   -20.077 -23.737 1.00 29.54  ? 74  ARG   B NE  1 
ATOM   1326 C CZ  . ARG   B 1 75 ? 10.638  -20.707 -23.570 1.00 32.50  ? 74  ARG   B CZ  1 
ATOM   1327 N NH1 . ARG   B 1 75 ? 11.702  -20.056 -23.098 1.00 34.68  ? 74  ARG   B NH1 1 
ATOM   1328 N NH2 . ARG   B 1 75 ? 10.743  -21.992 -23.911 1.00 35.57  ? 74  ARG   B NH2 1 
ATOM   1329 N N   . LYS   B 1 76 ? 9.180   -13.670 -22.564 1.00 29.60  ? 75  LYS   B N   1 
ATOM   1330 C CA  . LYS   B 1 76 ? 9.582   -12.311 -22.258 1.00 26.18  ? 75  LYS   B CA  1 
ATOM   1331 C C   . LYS   B 1 76 ? 10.645  -11.793 -23.242 1.00 26.09  ? 75  LYS   B C   1 
ATOM   1332 O O   . LYS   B 1 76 ? 11.729  -12.398 -23.325 1.00 28.34  ? 75  LYS   B O   1 
ATOM   1333 C CB  . LYS   B 1 76 ? 10.127  -12.213 -20.823 1.00 28.94  ? 75  LYS   B CB  1 
ATOM   1334 C CG  . LYS   B 1 76 ? 10.450  -10.786 -20.440 1.00 31.41  ? 75  LYS   B CG  1 
ATOM   1335 C CD  . LYS   B 1 76 ? 10.987  -10.693 -19.012 1.00 34.58  ? 75  LYS   B CD  1 
ATOM   1336 C CE  . LYS   B 1 76 ? 11.237  -9.249  -18.645 1.00 39.36  ? 75  LYS   B CE  1 
ATOM   1337 N NZ  . LYS   B 1 76 ? 11.535  -9.080  -17.215 1.00 45.93  ? 75  LYS   B NZ  1 
ATOM   1338 N N   . GLY   B 1 77 ? 10.262  -10.702 -23.919 1.00 26.05  ? 76  GLY   B N   1 
ATOM   1339 C CA  . GLY   B 1 77 ? 11.204  -10.008 -24.820 1.00 26.19  ? 76  GLY   B CA  1 
ATOM   1340 C C   . GLY   B 1 77 ? 11.022  -10.441 -26.271 1.00 31.87  ? 76  GLY   B C   1 
ATOM   1341 O O   . GLY   B 1 77 ? 11.564  -9.808  -27.180 1.00 29.68  ? 76  GLY   B O   1 
ATOM   1342 N N   . PHE   B 1 78 ? 10.299  -11.530 -26.509 1.00 27.00  ? 77  PHE   B N   1 
ATOM   1343 C CA  . PHE   B 1 78 ? 10.241  -12.048 -27.883 1.00 25.23  ? 77  PHE   B CA  1 
ATOM   1344 C C   . PHE   B 1 78 ? 9.483   -11.117 -28.830 1.00 28.90  ? 77  PHE   B C   1 
ATOM   1345 O O   . PHE   B 1 78 ? 9.956   -10.797 -29.939 1.00 28.16  ? 77  PHE   B O   1 
ATOM   1346 C CB  . PHE   B 1 78 ? 9.510   -13.389 -27.920 1.00 25.27  ? 77  PHE   B CB  1 
ATOM   1347 C CG  . PHE   B 1 78 ? 9.747   -14.114 -29.228 1.00 24.37  ? 77  PHE   B CG  1 
ATOM   1348 C CD1 . PHE   B 1 78 ? 10.816  -14.989 -29.314 1.00 24.02  ? 77  PHE   B CD1 1 
ATOM   1349 C CD2 . PHE   B 1 78 ? 8.845   -13.987 -30.291 1.00 27.01  ? 77  PHE   B CD2 1 
ATOM   1350 C CE1 . PHE   B 1 78 ? 11.067  -15.658 -30.534 1.00 24.26  ? 77  PHE   B CE1 1 
ATOM   1351 C CE2 . PHE   B 1 78 ? 9.086   -14.689 -31.483 1.00 28.25  ? 77  PHE   B CE2 1 
ATOM   1352 C CZ  . PHE   B 1 78 ? 10.185  -15.539 -31.567 1.00 27.25  ? 77  PHE   B CZ  1 
ATOM   1353 N N   . ASN   B 1 79 ? 8.295   -10.647 -28.452 1.00 28.32  ? 78  ASN   B N   1 
ATOM   1354 C CA  . ASN   B 1 79 ? 7.525   -9.819  -29.377 1.00 30.40  ? 78  ASN   B CA  1 
ATOM   1355 C C   . ASN   B 1 79 ? 8.219   -8.462  -29.583 1.00 30.49  ? 78  ASN   B C   1 
ATOM   1356 O O   . ASN   B 1 79 ? 8.158   -7.907  -30.692 1.00 30.52  ? 78  ASN   B O   1 
ATOM   1357 C CB  . ASN   B 1 79 ? 6.046   -9.732  -28.993 1.00 34.18  ? 78  ASN   B CB  1 
ATOM   1358 C CG  . ASN   B 1 79 ? 5.313   -11.057 -28.993 1.00 38.87  ? 78  ASN   B CG  1 
ATOM   1359 O OD1 . ASN   B 1 79 ? 5.777   -12.050 -29.566 1.00 35.93  ? 78  ASN   B OD1 1 
ATOM   1360 N ND2 . ASN   B 1 79 ? 4.144   -11.098 -28.368 1.00 39.05  ? 78  ASN   B ND2 1 
ATOM   1361 N N   . GLU   B 1 80 ? 8.886   -7.951  -28.548 1.00 29.68  ? 79  GLU   B N   1 
ATOM   1362 C CA  . GLU   B 1 80 ? 9.648   -6.724  -28.701 1.00 31.60  ? 79  GLU   B CA  1 
ATOM   1363 C C   . GLU   B 1 80 ? 10.778  -6.991  -29.704 1.00 29.75  ? 79  GLU   B C   1 
ATOM   1364 O O   . GLU   B 1 80 ? 11.096  -6.102  -30.521 1.00 27.14  ? 79  GLU   B O   1 
ATOM   1365 C CB  . GLU   B 1 80 ? 10.270  -6.284  -27.380 1.00 32.32  ? 79  GLU   B CB  1 
ATOM   1366 C CG  . GLU   B 1 80 ? 9.248   -5.746  -26.377 1.00 43.26  ? 79  GLU   B CG  1 
ATOM   1367 N N   . GLY   B 1 81 ? 11.377  -8.200  -29.612 1.00 28.33  ? 80  GLY   B N   1 
ATOM   1368 C CA  . GLY   B 1 81 ? 12.482  -8.584  -30.502 1.00 29.52  ? 80  GLY   B CA  1 
ATOM   1369 C C   . GLY   B 1 81 ? 12.024  -8.653  -31.960 1.00 28.82  ? 80  GLY   B C   1 
ATOM   1370 O O   . GLY   B 1 81 ? 12.771  -8.246  -32.882 1.00 26.60  ? 80  GLY   B O   1 
ATOM   1371 N N   . LEU   B 1 82 ? 10.799  -9.109  -32.180 1.00 26.66  ? 81  LEU   B N   1 
ATOM   1372 C CA  . LEU   B 1 82 ? 10.192  -9.162  -33.506 1.00 28.31  ? 81  LEU   B CA  1 
ATOM   1373 C C   . LEU   B 1 82 ? 10.074  -7.735  -34.034 1.00 28.90  ? 81  LEU   B C   1 
ATOM   1374 O O   . LEU   B 1 82 ? 10.358  -7.477  -35.209 1.00 29.14  ? 81  LEU   B O   1 
ATOM   1375 C CB  . LEU   B 1 82 ? 8.850   -9.904  -33.556 1.00 30.24  ? 81  LEU   B CB  1 
ATOM   1376 C CG  . LEU   B 1 82 ? 8.893   -11.422 -33.321 1.00 28.08  ? 81  LEU   B CG  1 
ATOM   1377 C CD1 . LEU   B 1 82 ? 7.468   -11.981 -33.358 1.00 29.11  ? 81  LEU   B CD1 1 
ATOM   1378 C CD2 . LEU   B 1 82 ? 9.836   -12.104 -34.335 1.00 27.33  ? 81  LEU   B CD2 1 
ATOM   1379 N N   . TRP   B 1 83 ? 9.643   -6.826  -33.157 1.00 29.28  ? 82  TRP   B N   1 
ATOM   1380 C CA  . TRP   B 1 83 ? 9.482   -5.427  -33.516 1.00 32.81  ? 82  TRP   B CA  1 
ATOM   1381 C C   . TRP   B 1 83 ? 10.819  -4.843  -33.965 1.00 29.83  ? 82  TRP   B C   1 
ATOM   1382 O O   . TRP   B 1 83 ? 10.892  -4.236  -35.045 1.00 30.27  ? 82  TRP   B O   1 
ATOM   1383 C CB  . TRP   B 1 83 ? 8.874   -4.594  -32.379 1.00 34.90  ? 82  TRP   B CB  1 
ATOM   1384 C CG  . TRP   B 1 83 ? 8.568   -3.205  -32.877 1.00 33.18  ? 82  TRP   B CG  1 
ATOM   1385 C CD1 . TRP   B 1 83 ? 7.412   -2.788  -33.471 1.00 40.63  ? 82  TRP   B CD1 1 
ATOM   1386 C CD2 . TRP   B 1 83 ? 9.481   -2.094  -32.934 1.00 38.02  ? 82  TRP   B CD2 1 
ATOM   1387 N NE1 . TRP   B 1 83 ? 7.525   -1.477  -33.859 1.00 42.25  ? 82  TRP   B NE1 1 
ATOM   1388 C CE2 . TRP   B 1 83 ? 8.785   -1.032  -33.556 1.00 35.94  ? 82  TRP   B CE2 1 
ATOM   1389 C CE3 . TRP   B 1 83 ? 10.808  -1.898  -32.524 1.00 33.02  ? 82  TRP   B CE3 1 
ATOM   1390 C CZ2 . TRP   B 1 83 ? 9.378   0.221   -33.752 1.00 36.16  ? 82  TRP   B CZ2 1 
ATOM   1391 C CZ3 . TRP   B 1 83 ? 11.384  -0.659  -32.703 1.00 39.08  ? 82  TRP   B CZ3 1 
ATOM   1392 C CH2 . TRP   B 1 83 ? 10.673  0.383   -33.317 1.00 33.03  ? 82  TRP   B CH2 1 
ATOM   1393 N N   . GLU   B 1 84 ? 11.875  -5.112  -33.182 1.00 25.62  ? 83  GLU   B N   1 
ATOM   1394 C CA  . GLU   B 1 84 ? 13.193  -4.552  -33.403 1.00 27.91  ? 83  GLU   B CA  1 
ATOM   1395 C C   . GLU   B 1 84 ? 13.807  -5.059  -34.712 1.00 28.19  ? 83  GLU   B C   1 
ATOM   1396 O O   . GLU   B 1 84 ? 14.407  -4.274  -35.456 1.00 28.59  ? 83  GLU   B O   1 
ATOM   1397 C CB  . GLU   B 1 84 ? 14.132  -4.808  -32.238 1.00 25.88  ? 83  GLU   B CB  1 
ATOM   1398 C CG  . GLU   B 1 84 ? 13.700  -4.072  -30.963 1.00 29.30  ? 83  GLU   B CG  1 
ATOM   1399 C CD  . GLU   B 1 84 ? 14.569  -4.421  -29.788 1.00 31.16  ? 83  GLU   B CD  1 
ATOM   1400 O OE1 . GLU   B 1 84 ? 15.512  -5.258  -29.877 1.00 28.11  ? 83  GLU   B OE1 1 
ATOM   1401 O OE2 . GLU   B 1 84 ? 14.337  -3.800  -28.693 1.00 32.61  ? 83  GLU   B OE2 1 
ATOM   1402 N N   . ILE   B 1 85 ? 13.733  -6.372  -34.940 1.00 26.56  ? 84  ILE   B N   1 
ATOM   1403 C CA  . ILE   B 1 85 ? 14.409  -6.926  -36.127 1.00 24.70  ? 84  ILE   B CA  1 
ATOM   1404 C C   . ILE   B 1 85 ? 13.760  -6.375  -37.409 1.00 25.16  ? 84  ILE   B C   1 
ATOM   1405 O O   . ILE   B 1 85 ? 14.466  -6.147  -38.416 1.00 26.61  ? 84  ILE   B O   1 
ATOM   1406 C CB  . ILE   B 1 85 ? 14.482  -8.462  -36.095 1.00 23.59  ? 84  ILE   B CB  1 
ATOM   1407 C CG1 . ILE   B 1 85 ? 15.538  -8.992  -37.132 1.00 25.61  ? 84  ILE   B CG1 1 
ATOM   1408 C CG2 . ILE   B 1 85 ? 13.105  -9.073  -36.320 1.00 25.92  ? 84  ILE   B CG2 1 
ATOM   1409 C CD1 . ILE   B 1 85 ? 15.991  -10.403 -36.792 1.00 24.90  ? 84  ILE   B CD1 1 
ATOM   1410 N N   . GLN   B 1 86 ? 12.442  -6.144  -37.367 1.00 25.56  ? 85  GLN   B N   1 
ATOM   1411 C CA  . GLN   B 1 86 ? 11.644  -5.569  -38.447 1.00 28.13  ? 85  GLN   B CA  1 
ATOM   1412 C C   . GLN   B 1 86 ? 11.909  -4.071  -38.642 1.00 33.84  ? 85  GLN   B C   1 
ATOM   1413 O O   . GLN   B 1 86 ? 11.990  -3.602  -39.779 1.00 36.02  ? 85  GLN   B O   1 
ATOM   1414 C CB  . GLN   B 1 86 ? 10.162  -5.858  -38.198 1.00 33.24  ? 85  GLN   B CB  1 
ATOM   1415 N N   . ASN   B 1 87 ? 12.011  -3.307  -37.551 1.00 27.50  ? 86  ASN   B N   1 
ATOM   1416 C CA  . ASN   B 1 87 ? 11.874  -1.849  -37.681 1.00 26.98  ? 86  ASN   B CA  1 
ATOM   1417 C C   . ASN   B 1 87 ? 13.182  -1.110  -37.474 1.00 27.51  ? 86  ASN   B C   1 
ATOM   1418 O O   . ASN   B 1 87 ? 13.342  0.026   -37.964 1.00 29.61  ? 86  ASN   B O   1 
ATOM   1419 C CB  . ASN   B 1 87 ? 10.869  -1.304  -36.658 1.00 30.67  ? 86  ASN   B CB  1 
ATOM   1420 C CG  . ASN   B 1 87 ? 9.478   -1.717  -37.056 1.00 38.15  ? 86  ASN   B CG  1 
ATOM   1421 O OD1 . ASN   B 1 87 ? 8.917   -1.169  -38.012 1.00 44.87  ? 86  ASN   B OD1 1 
ATOM   1422 N ND2 . ASN   B 1 87 ? 8.944   -2.738  -36.415 1.00 42.68  ? 86  ASN   B ND2 1 
ATOM   1423 N N   . ASN   B 1 88 ? 14.128  -1.676  -36.729 1.00 29.04  ? 87  ASN   B N   1 
ATOM   1424 C CA  . ASN   B 1 88 ? 15.388  -0.974  -36.524 1.00 28.30  ? 87  ASN   B CA  1 
ATOM   1425 C C   . ASN   B 1 88 ? 16.468  -1.969  -36.108 1.00 28.92  ? 87  ASN   B C   1 
ATOM   1426 O O   . ASN   B 1 88 ? 17.096  -1.899  -35.037 1.00 27.19  ? 87  ASN   B O   1 
ATOM   1427 C CB  . ASN   B 1 88 ? 15.241  0.256   -35.622 1.00 32.74  ? 87  ASN   B CB  1 
ATOM   1428 C CG  . ASN   B 1 88 ? 16.382  1.245   -35.727 1.00 31.51  ? 87  ASN   B CG  1 
ATOM   1429 O OD1 . ASN   B 1 88 ? 17.405  1.010   -36.384 1.00 32.98  ? 87  ASN   B OD1 1 
ATOM   1430 N ND2 . ASN   B 1 88 ? 16.207  2.390   -35.071 1.00 34.73  ? 87  ASN   B ND2 1 
ATOM   1431 N N   . PRO   B 1 89 ? 16.755  -2.954  -37.010 1.00 27.09  ? 88  PRO   B N   1 
ATOM   1432 C CA  . PRO   B 1 89 ? 17.704  -4.014  -36.655 1.00 25.54  ? 88  PRO   B CA  1 
ATOM   1433 C C   . PRO   B 1 89 ? 19.144  -3.591  -36.371 1.00 23.57  ? 88  PRO   B C   1 
ATOM   1434 O O   . PRO   B 1 89 ? 19.934  -4.338  -35.801 1.00 25.21  ? 88  PRO   B O   1 
ATOM   1435 C CB  . PRO   B 1 89 ? 17.617  -4.951  -37.894 1.00 26.46  ? 88  PRO   B CB  1 
ATOM   1436 C CG  . PRO   B 1 89 ? 17.136  -4.056  -39.055 1.00 25.31  ? 88  PRO   B CG  1 
ATOM   1437 C CD  . PRO   B 1 89 ? 16.186  -3.071  -38.372 1.00 27.26  ? 88  PRO   B CD  1 
ATOM   1438 N N   . HIS   B 1 90 ? 19.559  -2.399  -36.912 1.00 24.46  ? 89  HIS   B N   1 
ATOM   1439 C CA  . HIS   B 1 90 ? 20.946  -1.986  -36.836 1.00 25.38  ? 89  HIS   B CA  1 
ATOM   1440 C C   . HIS   B 1 90 ? 21.186  -0.901  -35.779 1.00 27.71  ? 89  HIS   B C   1 
ATOM   1441 O O   . HIS   B 1 90 ? 22.314  -0.429  -35.655 1.00 28.36  ? 89  HIS   B O   1 
ATOM   1442 C CB  . HIS   B 1 90 ? 21.465  -1.538  -38.222 1.00 25.10  ? 89  HIS   B CB  1 
ATOM   1443 C CG  . HIS   B 1 90 ? 21.302  -2.611  -39.246 1.00 26.97  ? 89  HIS   B CG  1 
ATOM   1444 N ND1 . HIS   B 1 90 ? 21.902  -3.837  -39.092 1.00 24.71  ? 89  HIS   B ND1 1 
ATOM   1445 C CD2 . HIS   B 1 90 ? 20.644  -2.659  -40.412 1.00 25.44  ? 89  HIS   B CD2 1 
ATOM   1446 C CE1 . HIS   B 1 90 ? 21.584  -4.595  -40.130 1.00 24.41  ? 89  HIS   B CE1 1 
ATOM   1447 N NE2 . HIS   B 1 90 ? 20.812  -3.923  -40.926 1.00 26.95  ? 89  HIS   B NE2 1 
ATOM   1448 N N   . ALA   B 1 91 ? 20.161  -0.639  -34.954 1.00 27.65  ? 90  ALA   B N   1 
ATOM   1449 C CA  . ALA   B 1 91 ? 20.326  0.363   -33.898 1.00 29.53  ? 90  ALA   B CA  1 
ATOM   1450 C C   . ALA   B 1 91 ? 21.290  -0.041  -32.785 1.00 33.33  ? 90  ALA   B C   1 
ATOM   1451 O O   . ALA   B 1 91 ? 21.614  -1.206  -32.529 1.00 29.41  ? 90  ALA   B O   1 
ATOM   1452 C CB  . ALA   B 1 91 ? 18.983  0.807   -33.369 1.00 28.51  ? 90  ALA   B CB  1 
ATOM   1453 N N   . SER   B 1 92 ? 21.785  0.997   -32.078 1.00 33.92  ? 91  SER   B N   1 
ATOM   1454 C CA  . SER   B 1 92 ? 22.445  0.824   -30.812 1.00 36.41  ? 91  SER   B CA  1 
ATOM   1455 C C   . SER   B 1 92 ? 21.369  0.609   -29.748 1.00 39.71  ? 91  SER   B C   1 
ATOM   1456 O O   . SER   B 1 92 ? 20.429  1.419   -29.620 1.00 39.85  ? 91  SER   B O   1 
ATOM   1457 C CB  . SER   B 1 92 ? 23.253  2.081   -30.492 1.00 41.56  ? 91  SER   B CB  1 
ATOM   1458 O OG  . SER   B 1 92 ? 23.608  2.043   -29.126 1.00 46.00  ? 91  SER   B OG  1 
ATOM   1459 N N   . TYR   B 1 93 ? 21.523  -0.504  -29.025 1.00 38.99  ? 92  TYR   B N   1 
ATOM   1460 C CA  . TYR   B 1 93 ? 20.646  -0.926  -27.949 1.00 40.66  ? 92  TYR   B CA  1 
ATOM   1461 C C   . TYR   B 1 93 ? 21.438  -0.823  -26.651 1.00 51.06  ? 92  TYR   B C   1 
ATOM   1462 O O   . TYR   B 1 93 ? 21.037  -1.373  -25.632 1.00 53.83  ? 92  TYR   B O   1 
ATOM   1463 C CB  . TYR   B 1 93 ? 20.032  -2.308  -28.227 1.00 35.26  ? 92  TYR   B CB  1 
ATOM   1464 C CG  . TYR   B 1 93 ? 19.027  -2.230  -29.362 1.00 29.13  ? 92  TYR   B CG  1 
ATOM   1465 C CD1 . TYR   B 1 93 ? 17.725  -1.809  -29.130 1.00 31.76  ? 92  TYR   B CD1 1 
ATOM   1466 C CD2 . TYR   B 1 93 ? 19.348  -2.589  -30.683 1.00 31.40  ? 92  TYR   B CD2 1 
ATOM   1467 C CE1 . TYR   B 1 93 ? 16.789  -1.658  -30.136 1.00 31.60  ? 92  TYR   B CE1 1 
ATOM   1468 C CE2 . TYR   B 1 93 ? 18.403  -2.439  -31.693 1.00 28.67  ? 92  TYR   B CE2 1 
ATOM   1469 C CZ  . TYR   B 1 93 ? 17.113  -2.012  -31.432 1.00 32.12  ? 92  TYR   B CZ  1 
ATOM   1470 O OH  . TYR   B 1 93 ? 16.107  -1.906  -32.357 1.00 32.03  ? 92  TYR   B OH  1 
ATOM   1471 N N   . SER   B 1 94 ? 22.555  -0.084  -26.731 1.00 58.99  ? 93  SER   B N   1 
ATOM   1472 C CA  . SER   B 1 94 ? 23.349  0.335   -25.584 1.00 72.58  ? 93  SER   B CA  1 
ATOM   1473 C C   . SER   B 1 94 ? 22.485  1.191   -24.644 1.00 80.03  ? 93  SER   B C   1 
ATOM   1474 O O   . SER   B 1 94 ? 21.838  2.136   -25.156 1.00 82.60  ? 93  SER   B O   1 
ATOM   1475 C CB  . SER   B 1 94 ? 24.586  1.099   -26.014 1.00 67.34  ? 93  SER   B CB  1 
ATOM   1476 O OG  . SER   B 1 94 ? 25.586  0.223   -26.513 1.00 68.51  ? 93  SER   B OG  1 
ATOM   1477 O OXT . SER   B 1 94 ? 22.479  0.875   -23.434 1.00 94.81  ? 93  SER   B OXT 1 
ATOM   1478 N N   . HIS   C 1 4  ? 32.923  -24.220 26.958  1.00 66.10  ? 3   HIS   C N   1 
ATOM   1479 C CA  . HIS   C 1 4  ? 32.088  -23.076 27.416  1.00 75.41  ? 3   HIS   C CA  1 
ATOM   1480 C C   . HIS   C 1 4  ? 31.441  -23.471 28.744  1.00 79.19  ? 3   HIS   C C   1 
ATOM   1481 O O   . HIS   C 1 4  ? 32.068  -24.158 29.553  1.00 76.22  ? 3   HIS   C O   1 
ATOM   1482 C CB  . HIS   C 1 4  ? 31.133  -22.627 26.299  1.00 72.64  ? 3   HIS   C CB  1 
ATOM   1483 N N   . ALA   C 1 5  ? 30.196  -23.025 28.963  1.00 77.66  ? 4   ALA   C N   1 
ATOM   1484 C CA  . ALA   C 1 5  ? 29.392  -23.471 30.090  1.00 69.21  ? 4   ALA   C CA  1 
ATOM   1485 C C   . ALA   C 1 5  ? 27.914  -23.236 29.810  1.00 75.10  ? 4   ALA   C C   1 
ATOM   1486 O O   . ALA   C 1 5  ? 27.511  -22.166 29.353  1.00 74.58  ? 4   ALA   C O   1 
ATOM   1487 C CB  . ALA   C 1 5  ? 29.799  -22.744 31.330  1.00 76.89  ? 4   ALA   C CB  1 
ATOM   1488 N N   . PHE   C 1 6  ? 27.115  -24.254 30.120  1.00 65.15  ? 5   PHE   C N   1 
ATOM   1489 C CA  . PHE   C 1 6  ? 25.721  -24.257 29.736  1.00 53.70  ? 5   PHE   C CA  1 
ATOM   1490 C C   . PHE   C 1 6  ? 24.898  -24.355 31.011  1.00 56.96  ? 5   PHE   C C   1 
ATOM   1491 O O   . PHE   C 1 6  ? 25.302  -25.071 31.922  1.00 69.36  ? 5   PHE   C O   1 
ATOM   1492 C CB  . PHE   C 1 6  ? 25.536  -25.462 28.796  1.00 49.34  ? 5   PHE   C CB  1 
ATOM   1493 C CG  . PHE   C 1 6  ? 26.328  -25.424 27.492  1.00 45.46  ? 5   PHE   C CG  1 
ATOM   1494 C CD1 . PHE   C 1 6  ? 27.485  -26.176 27.319  1.00 46.41  ? 5   PHE   C CD1 1 
ATOM   1495 C CD2 . PHE   C 1 6  ? 25.923  -24.621 26.426  1.00 52.34  ? 5   PHE   C CD2 1 
ATOM   1496 C CE1 . PHE   C 1 6  ? 28.216  -26.140 26.128  1.00 49.33  ? 5   PHE   C CE1 1 
ATOM   1497 C CE2 . PHE   C 1 6  ? 26.634  -24.607 25.227  1.00 46.45  ? 5   PHE   C CE2 1 
ATOM   1498 C CZ  . PHE   C 1 6  ? 27.783  -25.352 25.073  1.00 42.32  ? 5   PHE   C CZ  1 
ATOM   1499 N N   . LYS   C 1 7  ? 23.777  -23.623 31.074  1.00 51.41  ? 6   LYS   C N   1 
ATOM   1500 C CA  . LYS   C 1 7  ? 22.838  -23.664 32.194  1.00 54.14  ? 6   LYS   C CA  1 
ATOM   1501 C C   . LYS   C 1 7  ? 21.482  -23.991 31.586  1.00 43.06  ? 6   LYS   C C   1 
ATOM   1502 O O   . LYS   C 1 7  ? 21.357  -23.883 30.360  1.00 44.98  ? 6   LYS   C O   1 
ATOM   1503 C CB  . LYS   C 1 7  ? 22.811  -22.371 33.029  1.00 52.76  ? 6   LYS   C CB  1 
ATOM   1504 N N   . PRO   C 1 8  ? 20.449  -24.443 32.344  1.00 48.13  ? 7   PRO   C N   1 
ATOM   1505 C CA  . PRO   C 1 8  ? 19.161  -24.757 31.730  1.00 49.85  ? 7   PRO   C CA  1 
ATOM   1506 C C   . PRO   C 1 8  ? 18.644  -23.553 30.941  1.00 58.29  ? 7   PRO   C C   1 
ATOM   1507 O O   . PRO   C 1 8  ? 18.939  -22.402 31.278  1.00 65.52  ? 7   PRO   C O   1 
ATOM   1508 C CB  . PRO   C 1 8  ? 18.269  -25.141 32.913  1.00 52.85  ? 7   PRO   C CB  1 
ATOM   1509 C CG  . PRO   C 1 8  ? 19.250  -25.648 33.940  1.00 51.54  ? 7   PRO   C CG  1 
ATOM   1510 C CD  . PRO   C 1 8  ? 20.465  -24.725 33.799  1.00 43.67  ? 7   PRO   C CD  1 
ATOM   1511 N N   . GLY   C 1 9  ? 17.929  -23.833 29.845  1.00 51.92  ? 8   GLY   C N   1 
ATOM   1512 C CA  . GLY   C 1 9  ? 17.307  -22.788 29.047  1.00 48.76  ? 8   GLY   C CA  1 
ATOM   1513 C C   . GLY   C 1 9  ? 18.171  -22.307 27.880  1.00 47.64  ? 8   GLY   C C   1 
ATOM   1514 O O   . GLY   C 1 9  ? 17.617  -21.810 26.904  1.00 48.12  ? 8   GLY   C O   1 
ATOM   1515 N N   . ASP   C 1 10 ? 19.498  -22.479 27.976  1.00 44.29  ? 9   ASP   C N   1 
ATOM   1516 C CA  . ASP   C 1 10 ? 20.463  -22.168 26.940  1.00 36.13  ? 9   ASP   C CA  1 
ATOM   1517 C C   . ASP   C 1 10 ? 20.145  -22.898 25.623  1.00 39.49  ? 9   ASP   C C   1 
ATOM   1518 O O   . ASP   C 1 10 ? 19.912  -24.114 25.604  1.00 37.30  ? 9   ASP   C O   1 
ATOM   1519 C CB  . ASP   C 1 10 ? 21.881  -22.514 27.366  1.00 40.79  ? 9   ASP   C CB  1 
ATOM   1520 C CG  . ASP   C 1 10 ? 22.573  -21.570 28.351  1.00 50.67  ? 9   ASP   C CG  1 
ATOM   1521 O OD1 . ASP   C 1 10 ? 21.948  -20.588 28.759  1.00 53.57  ? 9   ASP   C OD1 1 
ATOM   1522 O OD2 . ASP   C 1 10 ? 23.749  -21.823 28.704  1.00 55.29  ? 9   ASP   C OD2 1 
ATOM   1523 N N   . LEU   C 1 11 ? 20.166  -22.137 24.519  1.00 39.02  ? 10  LEU   C N   1 
ATOM   1524 C CA  . LEU   C 1 11 ? 19.866  -22.669 23.193  1.00 36.81  ? 10  LEU   C CA  1 
ATOM   1525 C C   . LEU   C 1 11 ? 21.134  -23.127 22.489  1.00 32.64  ? 10  LEU   C C   1 
ATOM   1526 O O   . LEU   C 1 11 ? 22.142  -22.428 22.468  1.00 38.73  ? 10  LEU   C O   1 
ATOM   1527 C CB  . LEU   C 1 11 ? 19.150  -21.590 22.377  1.00 36.00  ? 10  LEU   C CB  1 
ATOM   1528 C CG  . LEU   C 1 11 ? 17.892  -21.029 23.033  1.00 35.24  ? 10  LEU   C CG  1 
ATOM   1529 C CD1 . LEU   C 1 11 ? 17.311  -20.040 22.030  1.00 36.55  ? 10  LEU   C CD1 1 
ATOM   1530 C CD2 . LEU   C 1 11 ? 16.907  -22.152 23.382  1.00 36.44  ? 10  LEU   C CD2 1 
ATOM   1531 N N   . VAL   C 1 12 ? 21.072  -24.304 21.811  1.00 33.92  ? 11  VAL   C N   1 
ATOM   1532 C CA  . VAL   C 1 12 ? 22.289  -24.934 21.317  1.00 31.81  ? 11  VAL   C CA  1 
ATOM   1533 C C   . VAL   C 1 12 ? 21.974  -25.671 19.997  1.00 29.61  ? 11  VAL   C C   1 
ATOM   1534 O O   . VAL   C 1 12 ? 20.781  -25.863 19.728  1.00 31.17  ? 11  VAL   C O   1 
ATOM   1535 C CB  . VAL   C 1 12 ? 22.914  -25.942 22.316  1.00 32.55  ? 11  VAL   C CB  1 
ATOM   1536 C CG1 . VAL   C 1 12 ? 23.410  -25.295 23.638  1.00 33.89  ? 11  VAL   C CG1 1 
ATOM   1537 C CG2 . VAL   C 1 12 ? 22.013  -27.147 22.558  1.00 35.03  ? 11  VAL   C CG2 1 
ATOM   1538 N N   . PHE   C 1 13 ? 23.038  -26.063 19.262  1.00 29.97  ? 12  PHE   C N   1 
ATOM   1539 C CA  . PHE   C 1 13 ? 22.992  -27.212 18.347  1.00 29.24  ? 12  PHE   C CA  1 
ATOM   1540 C C   . PHE   C 1 13 ? 23.653  -28.402 19.038  1.00 28.24  ? 12  PHE   C C   1 
ATOM   1541 O O   . PHE   C 1 13 ? 24.751  -28.297 19.618  1.00 30.12  ? 12  PHE   C O   1 
ATOM   1542 C CB  . PHE   C 1 13 ? 23.588  -27.044 16.934  1.00 31.95  ? 12  PHE   C CB  1 
ATOM   1543 C CG  . PHE   C 1 13 ? 22.824  -26.024 16.116  1.00 37.15  ? 12  PHE   C CG  1 
ATOM   1544 C CD1 . PHE   C 1 13 ? 21.785  -26.407 15.259  1.00 33.03  ? 12  PHE   C CD1 1 
ATOM   1545 C CD2 . PHE   C 1 13 ? 23.143  -24.670 16.222  1.00 36.00  ? 12  PHE   C CD2 1 
ATOM   1546 C CE1 . PHE   C 1 13 ? 21.093  -25.444 14.540  1.00 34.34  ? 12  PHE   C CE1 1 
ATOM   1547 C CE2 . PHE   C 1 13 ? 22.411  -23.727 15.542  1.00 36.40  ? 12  PHE   C CE2 1 
ATOM   1548 C CZ  . PHE   C 1 13 ? 21.402  -24.113 14.687  1.00 37.88  ? 12  PHE   C CZ  1 
ATOM   1549 N N   . ALA   C 1 14 ? 22.971  -29.563 19.028  1.00 28.39  ? 13  ALA   C N   1 
ATOM   1550 C CA  . ALA   C 1 14 ? 23.424  -30.735 19.764  1.00 25.93  ? 13  ALA   C CA  1 
ATOM   1551 C C   . ALA   C 1 14 ? 23.702  -31.837 18.756  1.00 32.55  ? 13  ALA   C C   1 
ATOM   1552 O O   . ALA   C 1 14 ? 22.829  -32.089 17.914  1.00 27.69  ? 13  ALA   C O   1 
ATOM   1553 C CB  . ALA   C 1 14 ? 22.347  -31.175 20.720  1.00 26.38  ? 13  ALA   C CB  1 
ATOM   1554 N N   . LYS   C 1 15 ? 24.895  -32.449 18.863  1.00 29.07  ? 14  LYS   C N   1 
ATOM   1555 C CA  . LYS   C 1 15 ? 25.319  -33.440 17.882  1.00 29.29  ? 14  LYS   C CA  1 
ATOM   1556 C C   . LYS   C 1 15 ? 25.334  -34.817 18.517  1.00 28.23  ? 14  LYS   C C   1 
ATOM   1557 O O   . LYS   C 1 15 ? 26.100  -35.091 19.453  1.00 32.17  ? 14  LYS   C O   1 
ATOM   1558 C CB  . LYS   C 1 15 ? 26.712  -33.096 17.337  1.00 30.97  ? 14  LYS   C CB  1 
ATOM   1559 C CG  . LYS   C 1 15 ? 27.203  -34.088 16.257  1.00 29.88  ? 14  LYS   C CG  1 
ATOM   1560 C CD  . LYS   C 1 15 ? 26.311  -34.004 15.024  1.00 29.82  ? 14  LYS   C CD  1 
ATOM   1561 C CE  . LYS   C 1 15 ? 26.789  -34.792 13.805  1.00 30.38  ? 14  LYS   C CE  1 
ATOM   1562 N NZ  . LYS   C 1 15 ? 26.792  -36.229 14.038  1.00 31.45  ? 14  LYS   C NZ  1 
ATOM   1563 N N   . MET   C 1 16 ? 24.523  -35.728 17.976  1.00 26.04  ? 15  MET   C N   1 
ATOM   1564 C CA  . MET   C 1 16 ? 24.574  -37.157 18.280  1.00 28.03  ? 15  MET   C CA  1 
ATOM   1565 C C   . MET   C 1 16 ? 25.026  -37.939 17.043  1.00 31.11  ? 15  MET   C C   1 
ATOM   1566 O O   . MET   C 1 16 ? 24.712  -37.578 15.896  1.00 27.08  ? 15  MET   C O   1 
ATOM   1567 C CB  . MET   C 1 16 ? 23.206  -37.707 18.693  1.00 33.93  ? 15  MET   C CB  1 
ATOM   1568 C CG  . MET   C 1 16 ? 22.933  -37.421 20.158  1.00 49.88  ? 15  MET   C CG  1 
ATOM   1569 S SD  . MET   C 1 16 ? 22.064  -38.716 21.069  1.00 73.47  ? 15  MET   C SD  1 
ATOM   1570 C CE  . MET   C 1 16 ? 20.867  -37.598 20.389  1.00 27.59  ? 15  MET   C CE  1 
ATOM   1571 N N   . LYS   C 1 17 ? 25.696  -39.084 17.292  1.00 31.11  ? 16  LYS   C N   1 
ATOM   1572 C CA  . LYS   C 1 17 ? 26.020  -39.986 16.194  1.00 33.94  ? 16  LYS   C CA  1 
ATOM   1573 C C   . LYS   C 1 17 ? 24.738  -40.388 15.453  1.00 27.70  ? 16  LYS   C C   1 
ATOM   1574 O O   . LYS   C 1 17 ? 23.775  -40.867 16.048  1.00 30.69  ? 16  LYS   C O   1 
ATOM   1575 C CB  . LYS   C 1 17 ? 26.665  -41.251 16.784  1.00 32.31  ? 16  LYS   C CB  1 
ATOM   1576 C CG  . LYS   C 1 17 ? 27.218  -42.278 15.784  1.00 36.49  ? 16  LYS   C CG  1 
ATOM   1577 C CD  . LYS   C 1 17 ? 28.434  -41.595 15.166  1.00 37.04  ? 16  LYS   C CD  1 
ATOM   1578 C CE  . LYS   C 1 17 ? 29.238  -42.584 14.354  1.00 49.41  ? 16  LYS   C CE  1 
ATOM   1579 N NZ  . LYS   C 1 17 ? 30.513  -41.968 13.968  1.00 46.77  ? 16  LYS   C NZ  1 
ATOM   1580 N N   . GLY   C 1 18 ? 24.821  -40.253 14.133  1.00 31.97  ? 17  GLY   C N   1 
ATOM   1581 C CA  . GLY   C 1 18 ? 23.755  -40.717 13.257  1.00 31.13  ? 17  GLY   C CA  1 
ATOM   1582 C C   . GLY   C 1 18 ? 22.774  -39.605 12.904  1.00 31.36  ? 17  GLY   C C   1 
ATOM   1583 O O   . GLY   C 1 18 ? 21.773  -39.907 12.253  1.00 29.78  ? 17  GLY   C O   1 
ATOM   1584 N N   . TYR   C 1 19 ? 23.015  -38.381 13.406  1.00 28.00  ? 18  TYR   C N   1 
ATOM   1585 C CA  . TYR   C 1 19 ? 22.088  -37.257 13.163  1.00 27.34  ? 18  TYR   C CA  1 
ATOM   1586 C C   . TYR   C 1 19 ? 22.871  -35.977 12.912  1.00 25.88  ? 18  TYR   C C   1 
ATOM   1587 O O   . TYR   C 1 19 ? 23.991  -35.795 13.412  1.00 26.10  ? 18  TYR   C O   1 
ATOM   1588 C CB  . TYR   C 1 19 ? 21.281  -36.943 14.426  1.00 24.73  ? 18  TYR   C CB  1 
ATOM   1589 C CG  . TYR   C 1 19 ? 20.442  -38.119 14.833  1.00 28.89  ? 18  TYR   C CG  1 
ATOM   1590 C CD1 . TYR   C 1 19 ? 20.961  -39.115 15.654  1.00 31.53  ? 18  TYR   C CD1 1 
ATOM   1591 C CD2 . TYR   C 1 19 ? 19.148  -38.214 14.360  1.00 30.59  ? 18  TYR   C CD2 1 
ATOM   1592 C CE1 . TYR   C 1 19 ? 20.174  -40.190 16.027  1.00 33.15  ? 18  TYR   C CE1 1 
ATOM   1593 C CE2 . TYR   C 1 19 ? 18.355  -39.281 14.739  1.00 40.61  ? 18  TYR   C CE2 1 
ATOM   1594 C CZ  . TYR   C 1 19 ? 18.870  -40.258 15.567  1.00 39.32  ? 18  TYR   C CZ  1 
ATOM   1595 O OH  . TYR   C 1 19 ? 18.040  -41.302 15.886  1.00 48.72  ? 18  TYR   C OH  1 
ATOM   1596 N N   . PRO   C 1 20 ? 22.320  -35.030 12.126  1.00 26.30  ? 19  PRO   C N   1 
ATOM   1597 C CA  . PRO   C 1 20 ? 22.980  -33.747 11.889  1.00 27.16  ? 19  PRO   C CA  1 
ATOM   1598 C C   . PRO   C 1 20 ? 22.960  -32.944 13.185  1.00 28.72  ? 19  PRO   C C   1 
ATOM   1599 O O   . PRO   C 1 20 ? 22.184  -33.230 14.114  1.00 25.78  ? 19  PRO   C O   1 
ATOM   1600 C CB  . PRO   C 1 20 ? 22.083  -33.078 10.808  1.00 31.78  ? 19  PRO   C CB  1 
ATOM   1601 C CG  . PRO   C 1 20 ? 20.740  -33.718 11.031  1.00 28.09  ? 19  PRO   C CG  1 
ATOM   1602 C CD  . PRO   C 1 20 ? 20.990  -35.126 11.486  1.00 26.69  ? 19  PRO   C CD  1 
ATOM   1603 N N   . HIS   C 1 21 ? 23.780  -31.907 13.211  1.00 27.81  ? 20  HIS   C N   1 
ATOM   1604 C CA  . HIS   C 1 21 ? 23.711  -31.005 14.366  1.00 27.09  ? 20  HIS   C CA  1 
ATOM   1605 C C   . HIS   C 1 21 ? 22.294  -30.458 14.506  1.00 29.19  ? 20  HIS   C C   1 
ATOM   1606 O O   . HIS   C 1 21 ? 21.769  -29.871 13.567  1.00 28.15  ? 20  HIS   C O   1 
ATOM   1607 C CB  . HIS   C 1 21 ? 24.660  -29.828 14.151  1.00 31.51  ? 20  HIS   C CB  1 
ATOM   1608 C CG  . HIS   C 1 21 ? 26.098  -30.227 14.191  1.00 33.27  ? 20  HIS   C CG  1 
ATOM   1609 N ND1 . HIS   C 1 21 ? 26.782  -30.849 13.166  1.00 33.81  ? 20  HIS   C ND1 1 
ATOM   1610 C CD2 . HIS   C 1 21 ? 26.978  -30.058 15.198  1.00 38.27  ? 20  HIS   C CD2 1 
ATOM   1611 C CE1 . HIS   C 1 21 ? 28.033  -31.067 13.556  1.00 39.90  ? 20  HIS   C CE1 1 
ATOM   1612 N NE2 . HIS   C 1 21 ? 28.179  -30.575 14.780  1.00 36.90  ? 20  HIS   C NE2 1 
ATOM   1613 N N   . TRP   C 1 22 ? 21.701  -30.563 15.713  1.00 25.54  ? 21  TRP   C N   1 
ATOM   1614 C CA  . TRP   C 1 22 ? 20.251  -30.465 15.804  1.00 26.18  ? 21  TRP   C CA  1 
ATOM   1615 C C   . TRP   C 1 22 ? 19.850  -29.295 16.700  1.00 25.93  ? 21  TRP   C C   1 
ATOM   1616 O O   . TRP   C 1 22 ? 20.373  -29.173 17.823  1.00 25.86  ? 21  TRP   C O   1 
ATOM   1617 C CB  . TRP   C 1 22 ? 19.697  -31.787 16.393  1.00 24.54  ? 21  TRP   C CB  1 
ATOM   1618 C CG  . TRP   C 1 22 ? 18.235  -31.973 16.040  1.00 23.49  ? 21  TRP   C CG  1 
ATOM   1619 C CD1 . TRP   C 1 22 ? 17.167  -31.372 16.628  1.00 27.14  ? 21  TRP   C CD1 1 
ATOM   1620 C CD2 . TRP   C 1 22 ? 17.721  -32.848 15.007  1.00 24.00  ? 21  TRP   C CD2 1 
ATOM   1621 N NE1 . TRP   C 1 22 ? 16.014  -31.780 16.002  1.00 26.66  ? 21  TRP   C NE1 1 
ATOM   1622 C CE2 . TRP   C 1 22 ? 16.315  -32.690 15.028  1.00 25.93  ? 21  TRP   C CE2 1 
ATOM   1623 C CE3 . TRP   C 1 22 ? 18.321  -33.750 14.112  1.00 24.74  ? 21  TRP   C CE3 1 
ATOM   1624 C CZ2 . TRP   C 1 22 ? 15.502  -33.417 14.147  1.00 25.61  ? 21  TRP   C CZ2 1 
ATOM   1625 C CZ3 . TRP   C 1 22 ? 17.529  -34.462 13.225  1.00 26.88  ? 21  TRP   C CZ3 1 
ATOM   1626 C CH2 . TRP   C 1 22 ? 16.132  -34.298 13.301  1.00 24.73  ? 21  TRP   C CH2 1 
ATOM   1627 N N   . PRO   C 1 23 ? 18.835  -28.469 16.368  1.00 29.53  ? 22  PRO   C N   1 
ATOM   1628 C CA  . PRO   C 1 23 ? 18.425  -27.398 17.291  1.00 26.92  ? 22  PRO   C CA  1 
ATOM   1629 C C   . PRO   C 1 23 ? 17.891  -27.940 18.610  1.00 25.72  ? 22  PRO   C C   1 
ATOM   1630 O O   . PRO   C 1 23 ? 17.068  -28.832 18.600  1.00 25.10  ? 22  PRO   C O   1 
ATOM   1631 C CB  . PRO   C 1 23 ? 17.352  -26.640 16.451  1.00 28.19  ? 22  PRO   C CB  1 
ATOM   1632 C CG  . PRO   C 1 23 ? 16.834  -27.674 15.480  1.00 26.15  ? 22  PRO   C CG  1 
ATOM   1633 C CD  . PRO   C 1 23 ? 18.098  -28.436 15.073  1.00 27.17  ? 22  PRO   C CD  1 
ATOM   1634 N N   . ALA   C 1 24 ? 18.425  -27.414 19.728  1.00 28.34  ? 23  ALA   C N   1 
ATOM   1635 C CA  . ALA   C 1 24 ? 18.121  -28.014 21.030  1.00 32.14  ? 23  ALA   C CA  1 
ATOM   1636 C C   . ALA   C 1 24 ? 18.234  -26.961 22.130  1.00 31.62  ? 23  ALA   C C   1 
ATOM   1637 O O   . ALA   C 1 24 ? 18.717  -25.852 21.885  1.00 32.42  ? 23  ALA   C O   1 
ATOM   1638 C CB  . ALA   C 1 24 ? 19.119  -29.150 21.291  1.00 29.80  ? 23  ALA   C CB  1 
ATOM   1639 N N   . ARG   C 1 25 ? 17.803  -27.327 23.352  1.00 33.49  ? 24  ARG   C N   1 
ATOM   1640 C CA  . ARG   C 1 25 ? 18.106  -26.501 24.508  1.00 34.31  ? 24  ARG   C CA  1 
ATOM   1641 C C   . ARG   C 1 25 ? 18.595  -27.401 25.648  1.00 34.03  ? 24  ARG   C C   1 
ATOM   1642 O O   . ARG   C 1 25 ? 18.273  -28.590 25.642  1.00 34.16  ? 24  ARG   C O   1 
ATOM   1643 C CB  . ARG   C 1 25 ? 16.881  -25.713 24.978  1.00 34.20  ? 24  ARG   C CB  1 
ATOM   1644 C CG  . ARG   C 1 25 ? 15.621  -26.475 25.358  1.00 38.70  ? 24  ARG   C CG  1 
ATOM   1645 C CD  . ARG   C 1 25 ? 14.584  -25.566 26.056  1.00 40.23  ? 24  ARG   C CD  1 
ATOM   1646 N NE  . ARG   C 1 25 ? 13.403  -26.398 26.338  1.00 50.84  ? 24  ARG   C NE  1 
ATOM   1647 C CZ  . ARG   C 1 25 ? 12.137  -26.154 26.027  1.00 51.73  ? 24  ARG   C CZ  1 
ATOM   1648 N NH1 . ARG   C 1 25 ? 11.802  -25.015 25.441  1.00 46.06  ? 24  ARG   C NH1 1 
ATOM   1649 N NH2 . ARG   C 1 25 ? 11.198  -27.044 26.329  1.00 55.96  ? 24  ARG   C NH2 1 
ATOM   1650 N N   . ILE   C 1 26 ? 19.359  -26.791 26.567  1.00 35.83  ? 25  ILE   C N   1 
ATOM   1651 C CA  . ILE   C 1 26 ? 19.683  -27.378 27.867  1.00 35.79  ? 25  ILE   C CA  1 
ATOM   1652 C C   . ILE   C 1 26 ? 18.457  -27.333 28.770  1.00 41.56  ? 25  ILE   C C   1 
ATOM   1653 O O   . ILE   C 1 26 ? 17.871  -26.273 28.984  1.00 43.35  ? 25  ILE   C O   1 
ATOM   1654 C CB  . ILE   C 1 26 ? 20.856  -26.645 28.546  1.00 37.16  ? 25  ILE   C CB  1 
ATOM   1655 C CG1 . ILE   C 1 26 ? 22.045  -26.378 27.638  1.00 37.18  ? 25  ILE   C CG1 1 
ATOM   1656 C CG2 . ILE   C 1 26 ? 21.272  -27.416 29.810  1.00 37.26  ? 25  ILE   C CG2 1 
ATOM   1657 C CD1 . ILE   C 1 26 ? 22.775  -27.600 27.107  1.00 40.11  ? 25  ILE   C CD1 1 
ATOM   1658 N N   . ASP   C 1 27 ? 18.089  -28.492 29.312  1.00 41.25  ? 26  ASP   C N   1 
ATOM   1659 C CA  . ASP   C 1 27 ? 17.030  -28.603 30.304  1.00 48.35  ? 26  ASP   C CA  1 
ATOM   1660 C C   . ASP   C 1 27 ? 17.633  -28.658 31.708  1.00 51.90  ? 26  ASP   C C   1 
ATOM   1661 O O   . ASP   C 1 27 ? 18.831  -28.906 31.866  1.00 53.09  ? 26  ASP   C O   1 
ATOM   1662 C CB  . ASP   C 1 27 ? 16.240  -29.877 30.079  1.00 46.49  ? 26  ASP   C CB  1 
ATOM   1663 C CG  . ASP   C 1 27 ? 15.013  -29.747 29.192  1.00 57.75  ? 26  ASP   C CG  1 
ATOM   1664 O OD1 . ASP   C 1 27 ? 14.848  -28.665 28.584  1.00 58.10  ? 26  ASP   C OD1 1 
ATOM   1665 O OD2 . ASP   C 1 27 ? 14.211  -30.709 29.181  1.00 58.79  ? 26  ASP   C OD2 1 
ATOM   1666 N N   . ASP   C 1 28 ? 16.795  -28.409 32.726  1.00 62.98  ? 27  ASP   C N   1 
ATOM   1667 C CA  . ASP   C 1 28 ? 17.167  -28.694 34.107  1.00 64.94  ? 27  ASP   C CA  1 
ATOM   1668 C C   . ASP   C 1 28 ? 16.822  -30.154 34.384  1.00 64.08  ? 27  ASP   C C   1 
ATOM   1669 O O   . ASP   C 1 28 ? 16.095  -30.768 33.609  1.00 58.13  ? 27  ASP   C O   1 
ATOM   1670 C CB  . ASP   C 1 28 ? 16.541  -27.718 35.097  1.00 68.07  ? 27  ASP   C CB  1 
ATOM   1671 N N   . ILE   C 1 29 ? 17.382  -30.709 35.465  1.00 60.51  ? 28  ILE   C N   1 
ATOM   1672 C CA  . ILE   C 1 29 ? 16.953  -32.005 35.965  1.00 57.12  ? 28  ILE   C CA  1 
ATOM   1673 C C   . ILE   C 1 29 ? 16.131  -31.740 37.222  1.00 57.71  ? 28  ILE   C C   1 
ATOM   1674 O O   . ILE   C 1 29 ? 16.529  -30.886 38.014  1.00 50.68  ? 28  ILE   C O   1 
ATOM   1675 C CB  . ILE   C 1 29 ? 18.179  -32.886 36.271  1.00 58.32  ? 28  ILE   C CB  1 
ATOM   1676 N N   . ALA   C 1 30 ? 14.989  -32.436 37.382  1.00 60.91  ? 29  ALA   C N   1 
ATOM   1677 C CA  . ALA   C 1 30 ? 14.192  -32.355 38.606  1.00 52.03  ? 29  ALA   C CA  1 
ATOM   1678 C C   . ALA   C 1 30 ? 15.019  -32.862 39.795  1.00 54.01  ? 29  ALA   C C   1 
ATOM   1679 O O   . ALA   C 1 30 ? 15.612  -33.973 39.640  1.00 46.41  ? 29  ALA   C O   1 
ATOM   1680 C CB  . ALA   C 1 30 ? 12.910  -33.150 38.464  1.00 49.44  ? 29  ALA   C CB  1 
ATOM   1681 N N   . ALA   C 1 33 ? 15.082  -36.552 40.375  1.00 49.74  ? 32  ALA   C N   1 
ATOM   1682 C CA  . ALA   C 1 33 ? 15.187  -37.416 39.174  1.00 48.10  ? 32  ALA   C CA  1 
ATOM   1683 C C   . ALA   C 1 33 ? 16.492  -38.211 39.164  1.00 53.15  ? 32  ALA   C C   1 
ATOM   1684 O O   . ALA   C 1 33 ? 17.311  -38.132 40.085  1.00 46.26  ? 32  ALA   C O   1 
ATOM   1685 C CB  . ALA   C 1 33 ? 15.049  -36.600 37.908  1.00 44.95  ? 32  ALA   C CB  1 
ATOM   1686 N N   . VAL   C 1 34 ? 16.659  -39.015 38.106  1.00 57.09  ? 33  VAL   C N   1 
ATOM   1687 C CA  . VAL   C 1 34 ? 17.901  -39.751 37.937  1.00 64.40  ? 33  VAL   C CA  1 
ATOM   1688 C C   . VAL   C 1 34 ? 18.909  -38.840 37.238  1.00 62.00  ? 33  VAL   C C   1 
ATOM   1689 O O   . VAL   C 1 34 ? 18.576  -38.128 36.280  1.00 50.04  ? 33  VAL   C O   1 
ATOM   1690 C CB  . VAL   C 1 34 ? 17.880  -41.200 37.406  1.00 67.34  ? 33  VAL   C CB  1 
ATOM   1691 C CG1 . VAL   C 1 34 ? 18.946  -41.467 36.343  1.00 71.77  ? 33  VAL   C CG1 1 
ATOM   1692 C CG2 . VAL   C 1 34 ? 17.989  -42.190 38.561  1.00 66.87  ? 33  VAL   C CG2 1 
ATOM   1693 N N   . LYS   C 1 35 ? 20.127  -38.849 37.800  1.00 53.82  ? 34  LYS   C N   1 
ATOM   1694 C CA  . LYS   C 1 35 ? 21.159  -37.899 37.432  1.00 54.87  ? 34  LYS   C CA  1 
ATOM   1695 C C   . LYS   C 1 35 ? 21.690  -38.278 36.053  1.00 44.89  ? 34  LYS   C C   1 
ATOM   1696 O O   . LYS   C 1 35 ? 21.622  -39.438 35.643  1.00 46.51  ? 34  LYS   C O   1 
ATOM   1697 C CB  . LYS   C 1 35 ? 22.223  -37.812 38.534  1.00 52.82  ? 34  LYS   C CB  1 
ATOM   1698 N N   . PRO   C 1 36 ? 22.203  -37.298 35.280  1.00 45.83  ? 35  PRO   C N   1 
ATOM   1699 C CA  . PRO   C 1 36 ? 22.888  -37.611 34.031  1.00 47.59  ? 35  PRO   C CA  1 
ATOM   1700 C C   . PRO   C 1 36 ? 24.021  -38.581 34.349  1.00 47.28  ? 35  PRO   C C   1 
ATOM   1701 O O   . PRO   C 1 36 ? 24.430  -38.753 35.515  1.00 46.40  ? 35  PRO   C O   1 
ATOM   1702 C CB  . PRO   C 1 36 ? 23.411  -36.242 33.531  1.00 50.03  ? 35  PRO   C CB  1 
ATOM   1703 C CG  . PRO   C 1 36 ? 22.580  -35.201 34.272  1.00 48.91  ? 35  PRO   C CG  1 
ATOM   1704 C CD  . PRO   C 1 36 ? 22.119  -35.852 35.565  1.00 48.55  ? 35  PRO   C CD  1 
ATOM   1705 N N   . PRO   C 1 37 ? 24.565  -39.255 33.322  1.00 48.28  ? 36  PRO   C N   1 
ATOM   1706 C CA  . PRO   C 1 37 ? 25.894  -39.830 33.457  1.00 44.07  ? 36  PRO   C CA  1 
ATOM   1707 C C   . PRO   C 1 37 ? 26.799  -38.667 33.851  1.00 44.01  ? 36  PRO   C C   1 
ATOM   1708 O O   . PRO   C 1 37 ? 26.488  -37.482 33.648  1.00 39.46  ? 36  PRO   C O   1 
ATOM   1709 C CB  . PRO   C 1 37 ? 26.175  -40.352 32.049  1.00 42.07  ? 36  PRO   C CB  1 
ATOM   1710 C CG  . PRO   C 1 37 ? 24.785  -40.656 31.532  1.00 44.55  ? 36  PRO   C CG  1 
ATOM   1711 C CD  . PRO   C 1 37 ? 23.957  -39.492 32.002  1.00 40.71  ? 36  PRO   C CD  1 
ATOM   1712 N N   . PRO   C 1 38 ? 27.976  -38.985 34.423  1.00 39.69  ? 37  PRO   C N   1 
ATOM   1713 C CA  . PRO   C 1 38 ? 28.930  -37.951 34.813  1.00 36.86  ? 37  PRO   C CA  1 
ATOM   1714 C C   . PRO   C 1 38 ? 29.223  -37.022 33.641  1.00 35.63  ? 37  PRO   C C   1 
ATOM   1715 O O   . PRO   C 1 38 ? 29.524  -37.480 32.536  1.00 39.75  ? 37  PRO   C O   1 
ATOM   1716 C CB  . PRO   C 1 38 ? 30.136  -38.858 35.143  1.00 39.22  ? 37  PRO   C CB  1 
ATOM   1717 C CG  . PRO   C 1 38 ? 29.469  -40.083 35.725  1.00 37.65  ? 37  PRO   C CG  1 
ATOM   1718 C CD  . PRO   C 1 38 ? 28.463  -40.360 34.645  1.00 41.62  ? 37  PRO   C CD  1 
ATOM   1719 N N   . ASN   C 1 39 ? 29.069  -35.711 33.905  1.00 35.87  ? 38  ASN   C N   1 
ATOM   1720 C CA  . ASN   C 1 39 ? 29.532  -34.641 33.048  1.00 35.56  ? 38  ASN   C CA  1 
ATOM   1721 C C   . ASN   C 1 39 ? 28.660  -34.547 31.808  1.00 39.76  ? 38  ASN   C C   1 
ATOM   1722 O O   . ASN   C 1 39 ? 29.131  -34.040 30.791  1.00 43.51  ? 38  ASN   C O   1 
ATOM   1723 C CB  . ASN   C 1 39 ? 30.987  -34.815 32.642  1.00 37.82  ? 38  ASN   C CB  1 
ATOM   1724 C CG  . ASN   C 1 39 ? 31.632  -33.590 32.036  1.00 48.55  ? 38  ASN   C CG  1 
ATOM   1725 O OD1 . ASN   C 1 39 ? 31.453  -32.470 32.531  1.00 59.32  ? 38  ASN   C OD1 1 
ATOM   1726 N ND2 . ASN   C 1 39 ? 32.411  -33.777 30.980  1.00 48.74  ? 38  ASN   C ND2 1 
ATOM   1727 N N   . LYS   C 1 40 ? 27.421  -35.048 31.915  1.00 32.47  ? 39  LYS   C N   1 
ATOM   1728 C CA  . LYS   C 1 40 ? 26.506  -34.878 30.797  1.00 31.69  ? 39  LYS   C CA  1 
ATOM   1729 C C   . LYS   C 1 40 ? 25.373  -33.923 31.154  1.00 32.23  ? 39  LYS   C C   1 
ATOM   1730 O O   . LYS   C 1 40 ? 24.970  -33.785 32.301  1.00 34.65  ? 39  LYS   C O   1 
ATOM   1731 C CB  . LYS   C 1 40 ? 25.876  -36.217 30.393  1.00 31.02  ? 39  LYS   C CB  1 
ATOM   1732 C CG  . LYS   C 1 40 ? 26.843  -37.301 30.011  1.00 35.25  ? 39  LYS   C CG  1 
ATOM   1733 C CD  . LYS   C 1 40 ? 27.646  -37.157 28.735  1.00 42.10  ? 39  LYS   C CD  1 
ATOM   1734 C CE  . LYS   C 1 40 ? 28.561  -38.358 28.539  1.00 41.41  ? 39  LYS   C CE  1 
ATOM   1735 N NZ  . LYS   C 1 40 ? 29.311  -38.361 27.282  1.00 50.99  ? 39  LYS   C NZ  1 
ATOM   1736 N N   . TYR   C 1 41 ? 24.838  -33.269 30.108  1.00 30.14  ? 40  TYR   C N   1 
ATOM   1737 C CA  . TYR   C 1 41 ? 23.748  -32.309 30.211  1.00 32.48  ? 40  TYR   C CA  1 
ATOM   1738 C C   . TYR   C 1 41 ? 22.480  -32.962 29.686  1.00 30.85  ? 40  TYR   C C   1 
ATOM   1739 O O   . TYR   C 1 41 ? 22.538  -33.719 28.722  1.00 30.78  ? 40  TYR   C O   1 
ATOM   1740 C CB  . TYR   C 1 41 ? 23.925  -31.121 29.257  1.00 28.10  ? 40  TYR   C CB  1 
ATOM   1741 C CG  . TYR   C 1 41 ? 25.054  -30.200 29.686  1.00 28.40  ? 40  TYR   C CG  1 
ATOM   1742 C CD1 . TYR   C 1 41 ? 26.356  -30.426 29.254  1.00 30.57  ? 40  TYR   C CD1 1 
ATOM   1743 C CD2 . TYR   C 1 41 ? 24.821  -29.157 30.585  1.00 34.34  ? 40  TYR   C CD2 1 
ATOM   1744 C CE1 . TYR   C 1 41 ? 27.405  -29.630 29.672  1.00 40.26  ? 40  TYR   C CE1 1 
ATOM   1745 C CE2 . TYR   C 1 41 ? 25.865  -28.339 30.983  1.00 33.56  ? 40  TYR   C CE2 1 
ATOM   1746 C CZ  . TYR   C 1 41 ? 27.151  -28.587 30.546  1.00 37.97  ? 40  TYR   C CZ  1 
ATOM   1747 O OH  . TYR   C 1 41 ? 28.206  -27.835 30.958  1.00 47.41  ? 40  TYR   C OH  1 
ATOM   1748 N N   . PRO   C 1 42 ? 21.315  -32.648 30.302  1.00 33.16  ? 41  PRO   C N   1 
ATOM   1749 C CA  . PRO   C 1 42 ? 20.007  -33.065 29.784  1.00 29.85  ? 41  PRO   C CA  1 
ATOM   1750 C C   . PRO   C 1 42 ? 19.665  -32.156 28.600  1.00 31.44  ? 41  PRO   C C   1 
ATOM   1751 O O   . PRO   C 1 42 ? 19.717  -30.930 28.728  1.00 32.45  ? 41  PRO   C O   1 
ATOM   1752 C CB  . PRO   C 1 42 ? 19.023  -32.861 30.941  1.00 34.18  ? 41  PRO   C CB  1 
ATOM   1753 C CG  . PRO   C 1 42 ? 19.782  -32.004 31.921  1.00 36.65  ? 41  PRO   C CG  1 
ATOM   1754 C CD  . PRO   C 1 42 ? 21.232  -31.813 31.515  1.00 38.88  ? 41  PRO   C CD  1 
ATOM   1755 N N   . ILE   C 1 43 ? 19.382  -32.799 27.458  1.00 30.32  ? 42  ILE   C N   1 
ATOM   1756 C CA  . ILE   C 1 43 ? 19.099  -32.026 26.245  1.00 30.20  ? 42  ILE   C CA  1 
ATOM   1757 C C   . ILE   C 1 43 ? 17.658  -32.260 25.829  1.00 28.75  ? 42  ILE   C C   1 
ATOM   1758 O O   . ILE   C 1 43 ? 17.131  -33.380 25.892  1.00 33.12  ? 42  ILE   C O   1 
ATOM   1759 C CB  . ILE   C 1 43 ? 20.079  -32.422 25.131  1.00 27.95  ? 42  ILE   C CB  1 
ATOM   1760 C CG1 . ILE   C 1 43 ? 21.544  -32.261 25.567  1.00 31.35  ? 42  ILE   C CG1 1 
ATOM   1761 C CG2 . ILE   C 1 43 ? 19.749  -31.675 23.819  1.00 31.09  ? 42  ILE   C CG2 1 
ATOM   1762 C CD1 . ILE   C 1 43 ? 22.004  -30.843 25.870  1.00 32.95  ? 42  ILE   C CD1 1 
ATOM   1763 N N   . PHE   C 1 44 ? 17.009  -31.189 25.321  1.00 31.88  ? 43  PHE   C N   1 
ATOM   1764 C CA  . PHE   C 1 44 ? 15.712  -31.375 24.690  1.00 28.63  ? 43  PHE   C CA  1 
ATOM   1765 C C   . PHE   C 1 44 ? 15.857  -30.929 23.234  1.00 27.15  ? 43  PHE   C C   1 
ATOM   1766 O O   . PHE   C 1 44 ? 16.446  -29.864 22.975  1.00 30.12  ? 43  PHE   C O   1 
ATOM   1767 C CB  . PHE   C 1 44 ? 14.772  -30.357 25.350  1.00 33.13  ? 43  PHE   C CB  1 
ATOM   1768 C CG  . PHE   C 1 44 ? 13.370  -30.339 24.742  1.00 34.38  ? 43  PHE   C CG  1 
ATOM   1769 C CD1 . PHE   C 1 44 ? 12.446  -31.336 25.049  1.00 35.88  ? 43  PHE   C CD1 1 
ATOM   1770 C CD2 . PHE   C 1 44 ? 13.004  -29.331 23.832  1.00 37.25  ? 43  PHE   C CD2 1 
ATOM   1771 C CE1 . PHE   C 1 44 ? 11.181  -31.353 24.452  1.00 39.83  ? 43  PHE   C CE1 1 
ATOM   1772 C CE2 . PHE   C 1 44 ? 11.728  -29.338 23.250  1.00 34.71  ? 43  PHE   C CE2 1 
ATOM   1773 C CZ  . PHE   C 1 44 ? 10.821  -30.332 23.590  1.00 39.19  ? 43  PHE   C CZ  1 
ATOM   1774 N N   . PHE   C 1 45 ? 15.414  -31.793 22.320  1.00 27.76  ? 44  PHE   C N   1 
ATOM   1775 C CA  . PHE   C 1 45 ? 15.597  -31.522 20.901  1.00 29.58  ? 44  PHE   C CA  1 
ATOM   1776 C C   . PHE   C 1 45 ? 14.344  -30.850 20.365  1.00 27.65  ? 44  PHE   C C   1 
ATOM   1777 O O   . PHE   C 1 45 ? 13.249  -31.381 20.501  1.00 31.04  ? 44  PHE   C O   1 
ATOM   1778 C CB  . PHE   C 1 45 ? 15.893  -32.804 20.139  1.00 27.54  ? 44  PHE   C CB  1 
ATOM   1779 C CG  . PHE   C 1 45 ? 17.257  -33.404 20.439  1.00 26.30  ? 44  PHE   C CG  1 
ATOM   1780 C CD1 . PHE   C 1 45 ? 18.397  -32.967 19.765  1.00 27.44  ? 44  PHE   C CD1 1 
ATOM   1781 C CD2 . PHE   C 1 45 ? 17.385  -34.408 21.406  1.00 29.26  ? 44  PHE   C CD2 1 
ATOM   1782 C CE1 . PHE   C 1 45 ? 19.645  -33.542 20.014  1.00 32.39  ? 44  PHE   C CE1 1 
ATOM   1783 C CE2 . PHE   C 1 45 ? 18.630  -34.968 21.663  1.00 34.27  ? 44  PHE   C CE2 1 
ATOM   1784 C CZ  . PHE   C 1 45 ? 19.751  -34.526 20.979  1.00 30.38  ? 44  PHE   C CZ  1 
ATOM   1785 N N   . PHE   C 1 46 ? 14.524  -29.673 19.729  1.00 28.43  ? 45  PHE   C N   1 
ATOM   1786 C CA  . PHE   C 1 46 ? 13.338  -29.099 19.104  1.00 27.26  ? 45  PHE   C CA  1 
ATOM   1787 C C   . PHE   C 1 46 ? 12.880  -29.926 17.904  1.00 30.67  ? 45  PHE   C C   1 
ATOM   1788 O O   . PHE   C 1 46 ? 13.640  -30.668 17.265  1.00 27.81  ? 45  PHE   C O   1 
ATOM   1789 C CB  . PHE   C 1 46 ? 13.624  -27.664 18.671  1.00 27.42  ? 45  PHE   C CB  1 
ATOM   1790 C CG  . PHE   C 1 46 ? 13.864  -26.672 19.789  1.00 28.95  ? 45  PHE   C CG  1 
ATOM   1791 C CD1 . PHE   C 1 46 ? 12.806  -26.210 20.572  1.00 32.77  ? 45  PHE   C CD1 1 
ATOM   1792 C CD2 . PHE   C 1 46 ? 15.155  -26.188 20.014  1.00 28.39  ? 45  PHE   C CD2 1 
ATOM   1793 C CE1 . PHE   C 1 46 ? 13.066  -25.303 21.601  1.00 36.38  ? 45  PHE   C CE1 1 
ATOM   1794 C CE2 . PHE   C 1 46 ? 15.406  -25.309 21.061  1.00 35.68  ? 45  PHE   C CE2 1 
ATOM   1795 C CZ  . PHE   C 1 46 ? 14.358  -24.850 21.826  1.00 32.68  ? 45  PHE   C CZ  1 
ATOM   1796 N N   . GLY   C 1 47 ? 11.593  -29.790 17.564  1.00 27.42  ? 46  GLY   C N   1 
ATOM   1797 C CA  . GLY   C 1 47 ? 11.093  -30.477 16.387  1.00 30.28  ? 46  GLY   C CA  1 
ATOM   1798 C C   . GLY   C 1 47 ? 10.606  -31.885 16.737  1.00 35.66  ? 46  GLY   C C   1 
ATOM   1799 O O   . GLY   C 1 47 ? 9.422   -32.185 16.630  1.00 38.78  ? 46  GLY   C O   1 
ATOM   1800 N N   . THR   C 1 48 ? 11.525  -32.752 17.181  1.00 30.17  ? 47  THR   C N   1 
ATOM   1801 C CA  . THR   C 1 48 ? 11.185  -34.111 17.585  1.00 33.51  ? 47  THR   C CA  1 
ATOM   1802 C C   . THR   C 1 48 ? 10.664  -34.117 19.024  1.00 32.08  ? 47  THR   C C   1 
ATOM   1803 O O   . THR   C 1 48 ? 9.928   -35.046 19.373  1.00 35.55  ? 47  THR   C O   1 
ATOM   1804 C CB  . THR   C 1 48 ? 12.435  -34.989 17.472  1.00 31.88  ? 47  THR   C CB  1 
ATOM   1805 O OG1 . THR   C 1 48 ? 13.312  -34.502 18.492  1.00 33.35  ? 47  THR   C OG1 1 
ATOM   1806 C CG2 . THR   C 1 48 ? 12.961  -35.088 16.055  1.00 31.94  ? 47  THR   C CG2 1 
ATOM   1807 N N   . HIS   C 1 49 ? 11.062  -33.129 19.837  1.00 32.14  ? 48  HIS   C N   1 
ATOM   1808 C CA  . HIS   C 1 49 ? 10.730  -33.016 21.257  1.00 36.33  ? 48  HIS   C CA  1 
ATOM   1809 C C   . HIS   C 1 49 ? 11.219  -34.233 22.055  1.00 35.21  ? 48  HIS   C C   1 
ATOM   1810 O O   . HIS   C 1 49 ? 10.635  -34.577 23.087  1.00 41.23  ? 48  HIS   C O   1 
ATOM   1811 C CB  . HIS   C 1 49 ? 9.227   -32.773 21.455  1.00 34.23  ? 48  HIS   C CB  1 
ATOM   1812 C CG  . HIS   C 1 49 ? 8.696   -31.667 20.590  1.00 41.14  ? 48  HIS   C CG  1 
ATOM   1813 N ND1 . HIS   C 1 49 ? 7.506   -31.816 19.908  1.00 49.87  ? 48  HIS   C ND1 1 
ATOM   1814 C CD2 . HIS   C 1 49 ? 9.152   -30.442 20.274  1.00 43.03  ? 48  HIS   C CD2 1 
ATOM   1815 C CE1 . HIS   C 1 49 ? 7.267   -30.726 19.185  1.00 48.57  ? 48  HIS   C CE1 1 
ATOM   1816 N NE2 . HIS   C 1 49 ? 8.249   -29.878 19.389  1.00 43.63  ? 48  HIS   C NE2 1 
ATOM   1817 N N   . GLU   C 1 50 ? 12.300  -34.861 21.603  1.00 32.54  ? 49  GLU   C N   1 
ATOM   1818 C CA  . GLU   C 1 50 ? 12.938  -35.949 22.337  1.00 34.78  ? 49  GLU   C CA  1 
ATOM   1819 C C   . GLU   C 1 50 ? 14.039  -35.425 23.261  1.00 35.22  ? 49  GLU   C C   1 
ATOM   1820 O O   . GLU   C 1 50 ? 14.361  -34.242 23.297  1.00 33.29  ? 49  GLU   C O   1 
ATOM   1821 C CB  . GLU   C 1 50 ? 13.437  -36.966 21.322  1.00 39.52  ? 49  GLU   C CB  1 
ATOM   1822 C CG  . GLU   C 1 50 ? 12.304  -37.554 20.487  1.00 44.44  ? 49  GLU   C CG  1 
ATOM   1823 C CD  . GLU   C 1 50 ? 12.790  -38.636 19.552  1.00 61.08  ? 49  GLU   C CD  1 
ATOM   1824 O OE1 . GLU   C 1 50 ? 13.998  -38.960 19.617  1.00 70.86  ? 49  GLU   C OE1 1 
ATOM   1825 O OE2 . GLU   C 1 50 ? 11.967  -39.155 18.765  1.00 75.85  ? 49  GLU   C OE2 1 
ATOM   1826 N N   . THR   C 1 51 ? 14.539  -36.317 24.125  1.00 38.06  ? 50  THR   C N   1 
ATOM   1827 C CA  . THR   C 1 51 ? 15.525  -35.949 25.142  1.00 33.66  ? 50  THR   C CA  1 
ATOM   1828 C C   . THR   C 1 51 ? 16.644  -36.974 25.092  1.00 31.74  ? 50  THR   C C   1 
ATOM   1829 O O   . THR   C 1 51 ? 16.451  -38.111 24.639  1.00 36.19  ? 50  THR   C O   1 
ATOM   1830 C CB  . THR   C 1 51 ? 14.899  -35.903 26.539  1.00 36.83  ? 50  THR   C CB  1 
ATOM   1831 O OG1 . THR   C 1 51 ? 14.475  -37.236 26.826  1.00 37.33  ? 50  THR   C OG1 1 
ATOM   1832 C CG2 . THR   C 1 51 ? 13.792  -34.870 26.670  1.00 41.04  ? 50  THR   C CG2 1 
ATOM   1833 N N   . ALA   C 1 52 ? 17.835  -36.505 25.460  1.00 31.85  ? 51  ALA   C N   1 
ATOM   1834 C CA  . ALA   C 1 52 ? 19.033  -37.323 25.576  1.00 33.44  ? 51  ALA   C CA  1 
ATOM   1835 C C   . ALA   C 1 52 ? 19.991  -36.642 26.549  1.00 35.66  ? 51  ALA   C C   1 
ATOM   1836 O O   . ALA   C 1 52 ? 19.769  -35.517 26.985  1.00 34.86  ? 51  ALA   C O   1 
ATOM   1837 C CB  . ALA   C 1 52 ? 19.688  -37.508 24.234  1.00 35.28  ? 51  ALA   C CB  1 
ATOM   1838 N N   . PHE   C 1 53 ? 21.071  -37.351 26.915  1.00 36.20  ? 52  PHE   C N   1 
ATOM   1839 C CA  . PHE   C 1 53 ? 22.146  -36.764 27.707  1.00 34.81  ? 52  PHE   C CA  1 
ATOM   1840 C C   . PHE   C 1 53 ? 23.360  -36.613 26.812  1.00 33.09  ? 52  PHE   C C   1 
ATOM   1841 O O   . PHE   C 1 53 ? 23.755  -37.564 26.142  1.00 34.51  ? 52  PHE   C O   1 
ATOM   1842 C CB  . PHE   C 1 53 ? 22.495  -37.766 28.817  1.00 35.86  ? 52  PHE   C CB  1 
ATOM   1843 C CG  . PHE   C 1 53 ? 21.506  -37.691 29.965  1.00 33.82  ? 52  PHE   C CG  1 
ATOM   1844 C CD1 . PHE   C 1 53 ? 21.279  -36.502 30.639  1.00 36.93  ? 52  PHE   C CD1 1 
ATOM   1845 C CD2 . PHE   C 1 53 ? 20.774  -38.811 30.355  1.00 49.62  ? 52  PHE   C CD2 1 
ATOM   1846 C CE1 . PHE   C 1 53 ? 20.381  -36.423 31.700  1.00 41.14  ? 52  PHE   C CE1 1 
ATOM   1847 C CE2 . PHE   C 1 53 ? 19.865  -38.721 31.412  1.00 41.92  ? 52  PHE   C CE2 1 
ATOM   1848 C CZ  . PHE   C 1 53 ? 19.666  -37.524 32.076  1.00 42.09  ? 52  PHE   C CZ  1 
ATOM   1849 N N   . LEU   C 1 54 ? 23.973  -35.425 26.809  1.00 29.33  ? 53  LEU   C N   1 
ATOM   1850 C CA  . LEU   C 1 54 ? 25.139  -35.233 25.959  1.00 28.11  ? 53  LEU   C CA  1 
ATOM   1851 C C   . LEU   C 1 54 ? 26.227  -34.466 26.704  1.00 30.43  ? 53  LEU   C C   1 
ATOM   1852 O O   . LEU   C 1 54 ? 25.941  -33.677 27.598  1.00 33.14  ? 53  LEU   C O   1 
ATOM   1853 C CB  . LEU   C 1 54 ? 24.770  -34.470 24.679  1.00 29.88  ? 53  LEU   C CB  1 
ATOM   1854 C CG  . LEU   C 1 54 ? 23.916  -35.229 23.669  1.00 34.70  ? 53  LEU   C CG  1 
ATOM   1855 C CD1 . LEU   C 1 54 ? 23.633  -34.290 22.515  1.00 34.65  ? 53  LEU   C CD1 1 
ATOM   1856 C CD2 . LEU   C 1 54 ? 24.675  -36.468 23.123  1.00 42.22  ? 53  LEU   C CD2 1 
ATOM   1857 N N   . GLY   C 1 55 ? 27.471  -34.685 26.287  1.00 31.79  ? 54  GLY   C N   1 
ATOM   1858 C CA  . GLY   C 1 55 ? 28.578  -33.967 26.898  1.00 32.50  ? 54  GLY   C CA  1 
ATOM   1859 C C   . GLY   C 1 55 ? 28.900  -32.674 26.153  1.00 39.86  ? 54  GLY   C C   1 
ATOM   1860 O O   . GLY   C 1 55 ? 28.438  -32.416 25.033  1.00 35.43  ? 54  GLY   C O   1 
ATOM   1861 N N   . PRO   C 1 56 ? 29.718  -31.787 26.763  1.00 37.78  ? 55  PRO   C N   1 
ATOM   1862 C CA  . PRO   C 1 56 ? 29.942  -30.448 26.226  1.00 39.69  ? 55  PRO   C CA  1 
ATOM   1863 C C   . PRO   C 1 56 ? 30.573  -30.384 24.843  1.00 38.23  ? 55  PRO   C C   1 
ATOM   1864 O O   . PRO   C 1 56 ? 30.361  -29.412 24.121  1.00 52.56  ? 55  PRO   C O   1 
ATOM   1865 C CB  . PRO   C 1 56 ? 30.800  -29.733 27.324  1.00 41.74  ? 55  PRO   C CB  1 
ATOM   1866 C CG  . PRO   C 1 56 ? 31.435  -30.870 28.077  1.00 37.90  ? 55  PRO   C CG  1 
ATOM   1867 C CD  . PRO   C 1 56 ? 30.413  -32.007 28.047  1.00 37.36  ? 55  PRO   C CD  1 
ATOM   1868 N N   . LYS   C 1 57 ? 31.284  -31.438 24.458  1.00 38.29  ? 56  LYS   C N   1 
ATOM   1869 C CA  . LYS   C 1 57 ? 31.947  -31.423 23.166  1.00 41.32  ? 56  LYS   C CA  1 
ATOM   1870 C C   . LYS   C 1 57 ? 30.897  -31.540 22.063  1.00 45.77  ? 56  LYS   C C   1 
ATOM   1871 O O   . LYS   C 1 57 ? 31.182  -31.257 20.895  1.00 39.25  ? 56  LYS   C O   1 
ATOM   1872 C CB  . LYS   C 1 57 ? 32.810  -32.678 23.014  1.00 42.70  ? 56  LYS   C CB  1 
ATOM   1873 N N   . ASP   C 1 58 ? 29.699  -31.992 22.454  1.00 40.35  ? 57  ASP   C N   1 
ATOM   1874 C CA  . ASP   C 1 58 ? 28.656  -32.289 21.478  1.00 38.83  ? 57  ASP   C CA  1 
ATOM   1875 C C   . ASP   C 1 58 ? 27.713  -31.109 21.316  1.00 37.31  ? 57  ASP   C C   1 
ATOM   1876 O O   . ASP   C 1 58 ? 26.693  -31.232 20.638  1.00 35.53  ? 57  ASP   C O   1 
ATOM   1877 C CB  . ASP   C 1 58 ? 27.876  -33.524 21.888  1.00 38.76  ? 57  ASP   C CB  1 
ATOM   1878 C CG  . ASP   C 1 58 ? 28.702  -34.793 21.898  1.00 44.47  ? 57  ASP   C CG  1 
ATOM   1879 O OD1 . ASP   C 1 58 ? 29.654  -34.839 21.116  1.00 46.60  ? 57  ASP   C OD1 1 
ATOM   1880 O OD2 . ASP   C 1 58 ? 28.390  -35.693 22.695  1.00 50.45  ? 57  ASP   C OD2 1 
ATOM   1881 N N   . LEU   C 1 59 ? 27.993  -29.996 21.993  1.00 33.43  ? 58  LEU   C N   1 
ATOM   1882 C CA  . LEU   C 1 59 ? 27.060  -28.897 22.129  1.00 33.78  ? 58  LEU   C CA  1 
ATOM   1883 C C   . LEU   C 1 59 ? 27.676  -27.614 21.577  1.00 36.94  ? 58  LEU   C C   1 
ATOM   1884 O O   . LEU   C 1 59 ? 28.857  -27.361 21.834  1.00 46.50  ? 58  LEU   C O   1 
ATOM   1885 C CB  . LEU   C 1 59 ? 26.699  -28.715 23.601  1.00 32.93  ? 58  LEU   C CB  1 
ATOM   1886 C CG  . LEU   C 1 59 ? 26.113  -29.966 24.271  1.00 30.90  ? 58  LEU   C CG  1 
ATOM   1887 C CD1 . LEU   C 1 59 ? 25.853  -29.822 25.753  1.00 32.86  ? 58  LEU   C CD1 1 
ATOM   1888 C CD2 . LEU   C 1 59 ? 24.811  -30.411 23.584  1.00 29.44  ? 58  LEU   C CD2 1 
ATOM   1889 N N   . PHE   C 1 60 ? 26.865  -26.809 20.876  1.00 40.91  ? 59  PHE   C N   1 
ATOM   1890 C CA  . PHE   C 1 60 ? 27.355  -25.614 20.182  1.00 36.97  ? 59  PHE   C CA  1 
ATOM   1891 C C   . PHE   C 1 60 ? 26.394  -24.470 20.483  1.00 40.77  ? 59  PHE   C C   1 
ATOM   1892 O O   . PHE   C 1 60 ? 25.190  -24.580 20.255  1.00 36.16  ? 59  PHE   C O   1 
ATOM   1893 C CB  . PHE   C 1 60 ? 27.538  -25.904 18.680  1.00 34.76  ? 59  PHE   C CB  1 
ATOM   1894 C CG  . PHE   C 1 60 ? 28.535  -27.022 18.393  1.00 34.60  ? 59  PHE   C CG  1 
ATOM   1895 C CD1 . PHE   C 1 60 ? 28.149  -28.362 18.383  1.00 34.55  ? 59  PHE   C CD1 1 
ATOM   1896 C CD2 . PHE   C 1 60 ? 29.891  -26.752 18.189  1.00 40.21  ? 59  PHE   C CD2 1 
ATOM   1897 C CE1 . PHE   C 1 60 ? 29.068  -29.383 18.171  1.00 37.56  ? 59  PHE   C CE1 1 
ATOM   1898 C CE2 . PHE   C 1 60 ? 30.802  -27.776 17.957  1.00 40.33  ? 59  PHE   C CE2 1 
ATOM   1899 C CZ  . PHE   C 1 60 ? 30.400  -29.092 17.931  1.00 40.74  ? 59  PHE   C CZ  1 
ATOM   1900 N N   . PRO   C 1 61 ? 26.835  -23.324 21.056  1.00 41.59  ? 60  PRO   C N   1 
ATOM   1901 C CA  . PRO   C 1 61 ? 25.871  -22.271 21.385  1.00 42.28  ? 60  PRO   C CA  1 
ATOM   1902 C C   . PRO   C 1 61 ? 25.166  -21.792 20.112  1.00 34.37  ? 60  PRO   C C   1 
ATOM   1903 O O   . PRO   C 1 61 ? 25.777  -21.686 19.052  1.00 38.41  ? 60  PRO   C O   1 
ATOM   1904 C CB  . PRO   C 1 61 ? 26.675  -21.166 22.130  1.00 43.36  ? 60  PRO   C CB  1 
ATOM   1905 C CG  . PRO   C 1 61 ? 28.078  -21.744 22.259  1.00 44.42  ? 60  PRO   C CG  1 
ATOM   1906 C CD  . PRO   C 1 61 ? 28.231  -22.988 21.388  1.00 46.66  ? 60  PRO   C CD  1 
ATOM   1907 N N   . TYR   C 1 62 ? 23.853  -21.540 20.248  1.00 40.38  ? 61  TYR   C N   1 
ATOM   1908 C CA  . TYR   C 1 62 ? 22.940  -21.339 19.132  1.00 44.00  ? 61  TYR   C CA  1 
ATOM   1909 C C   . TYR   C 1 62 ? 23.327  -20.092 18.343  1.00 51.70  ? 61  TYR   C C   1 
ATOM   1910 O O   . TYR   C 1 62 ? 23.553  -20.174 17.131  1.00 52.31  ? 61  TYR   C O   1 
ATOM   1911 C CB  . TYR   C 1 62 ? 21.500  -21.138 19.606  1.00 40.07  ? 61  TYR   C CB  1 
ATOM   1912 C CG  . TYR   C 1 62 ? 20.539  -20.795 18.471  1.00 41.55  ? 61  TYR   C CG  1 
ATOM   1913 C CD1 . TYR   C 1 62 ? 20.414  -21.624 17.352  1.00 42.87  ? 61  TYR   C CD1 1 
ATOM   1914 C CD2 . TYR   C 1 62 ? 19.796  -19.618 18.503  1.00 43.16  ? 61  TYR   C CD2 1 
ATOM   1915 C CE1 . TYR   C 1 62 ? 19.529  -21.309 16.322  1.00 43.71  ? 61  TYR   C CE1 1 
ATOM   1916 C CE2 . TYR   C 1 62 ? 18.929  -19.286 17.476  1.00 48.56  ? 61  TYR   C CE2 1 
ATOM   1917 C CZ  . TYR   C 1 62 ? 18.788  -20.133 16.388  1.00 42.97  ? 61  TYR   C CZ  1 
ATOM   1918 O OH  . TYR   C 1 62 ? 17.925  -19.711 15.404  1.00 43.70  ? 61  TYR   C OH  1 
ATOM   1919 N N   . ASP   C 1 63 ? 23.398  -18.949 19.048  1.00 46.90  ? 62  ASP   C N   1 
ATOM   1920 C CA  . ASP   C 1 63 ? 23.636  -17.677 18.378  1.00 51.04  ? 62  ASP   C CA  1 
ATOM   1921 C C   . ASP   C 1 63 ? 24.977  -17.701 17.663  1.00 47.44  ? 62  ASP   C C   1 
ATOM   1922 O O   . ASP   C 1 63 ? 25.110  -17.105 16.589  1.00 48.83  ? 62  ASP   C O   1 
ATOM   1923 C CB  . ASP   C 1 63 ? 23.400  -16.478 19.285  1.00 52.92  ? 62  ASP   C CB  1 
ATOM   1924 C CG  . ASP   C 1 63 ? 21.931  -16.098 19.410  1.00 64.89  ? 62  ASP   C CG  1 
ATOM   1925 O OD1 . ASP   C 1 63 ? 21.482  -15.851 20.546  1.00 67.59  ? 62  ASP   C OD1 1 
ATOM   1926 O OD2 . ASP   C 1 63 ? 21.238  -16.072 18.362  1.00 71.82  ? 62  ASP   C OD2 1 
ATOM   1927 N N   . LYS   C 1 64 ? 25.933  -18.424 18.244  1.00 41.34  ? 63  LYS   C N   1 
ATOM   1928 C CA  . LYS   C 1 64 ? 27.292  -18.444 17.740  1.00 44.79  ? 63  LYS   C CA  1 
ATOM   1929 C C   . LYS   C 1 64 ? 27.406  -19.379 16.538  1.00 45.42  ? 63  LYS   C C   1 
ATOM   1930 O O   . LYS   C 1 64 ? 28.215  -19.125 15.652  1.00 38.94  ? 63  LYS   C O   1 
ATOM   1931 C CB  . LYS   C 1 64 ? 28.312  -18.761 18.843  1.00 50.66  ? 63  LYS   C CB  1 
ATOM   1932 N N   . SER   C 1 65 ? 26.555  -20.428 16.458  1.00 41.14  ? 64  SER   C N   1 
ATOM   1933 C CA  . SER   C 1 65 ? 26.794  -21.391 15.391  1.00 36.12  ? 64  SER   C CA  1 
ATOM   1934 C C   . SER   C 1 65 ? 25.613  -21.512 14.419  1.00 34.22  ? 64  SER   C C   1 
ATOM   1935 O O   . SER   C 1 65 ? 25.701  -22.286 13.477  1.00 34.72  ? 64  SER   C O   1 
ATOM   1936 C CB  . SER   C 1 65 ? 27.208  -22.730 15.929  1.00 42.03  ? 64  SER   C CB  1 
ATOM   1937 O OG  . SER   C 1 65 ? 26.121  -23.307 16.627  1.00 41.30  ? 64  SER   C OG  1 
ATOM   1938 N N   . LYS   C 1 66 ? 24.566  -20.702 14.576  1.00 33.70  ? 65  LYS   C N   1 
ATOM   1939 C CA  . LYS   C 1 66 ? 23.422  -20.849 13.676  1.00 36.91  ? 65  LYS   C CA  1 
ATOM   1940 C C   . LYS   C 1 66 ? 23.788  -20.549 12.225  1.00 39.92  ? 65  LYS   C C   1 
ATOM   1941 O O   . LYS   C 1 66 ? 23.254  -21.177 11.313  1.00 35.82  ? 65  LYS   C O   1 
ATOM   1942 C CB  . LYS   C 1 66 ? 22.212  -20.006 14.073  1.00 39.57  ? 65  LYS   C CB  1 
ATOM   1943 C CG  . LYS   C 1 66 ? 22.488  -18.522 14.199  1.00 31.77  ? 65  LYS   C CG  1 
ATOM   1944 C CD  . LYS   C 1 66 ? 21.179  -17.867 14.610  1.00 43.51  ? 65  LYS   C CD  1 
ATOM   1945 C CE  . LYS   C 1 66 ? 21.299  -16.402 14.844  1.00 45.92  ? 65  LYS   C CE  1 
ATOM   1946 N NZ  . LYS   C 1 66 ? 19.980  -15.936 15.262  1.00 50.24  ? 65  LYS   C NZ  1 
ATOM   1947 N N   . ASP   C 1 67 ? 24.731  -19.628 11.998  1.00 38.48  ? 66  ASP   C N   1 
ATOM   1948 C CA  . ASP   C 1 67 ? 25.140  -19.347 10.624  1.00 40.78  ? 66  ASP   C CA  1 
ATOM   1949 C C   . ASP   C 1 67 ? 25.537  -20.640 9.888   1.00 41.28  ? 66  ASP   C C   1 
ATOM   1950 O O   . ASP   C 1 67 ? 25.240  -20.804 8.706   1.00 39.23  ? 66  ASP   C O   1 
ATOM   1951 C CB  . ASP   C 1 67 ? 25.988  -18.071 10.549  1.00 40.36  ? 66  ASP   C CB  1 
ATOM   1952 C CG  . ASP   C 1 67 ? 27.506  -18.160 10.698  1.00 57.23  ? 66  ASP   C CG  1 
ATOM   1953 O OD1 . ASP   C 1 67 ? 28.094  -19.238 10.409  1.00 59.04  ? 66  ASP   C OD1 1 
ATOM   1954 O OD2 . ASP   C 1 67 ? 28.106  -17.123 11.086  1.00 59.74  ? 66  ASP   C OD2 1 
ATOM   1955 N N   . LYS   C 1 68 ? 26.163  -21.590 10.607  1.00 36.20  ? 67  LYS   C N   1 
ATOM   1956 C CA  . LYS   C 1 68 ? 26.651  -22.840 10.055  1.00 35.73  ? 67  LYS   C CA  1 
ATOM   1957 C C   . LYS   C 1 68 ? 25.652  -24.011 10.163  1.00 33.47  ? 67  LYS   C C   1 
ATOM   1958 O O   . LYS   C 1 68 ? 25.527  -24.814 9.236   1.00 37.01  ? 67  LYS   C O   1 
ATOM   1959 C CB  . LYS   C 1 68 ? 27.881  -23.157 10.904  1.00 34.61  ? 67  LYS   C CB  1 
ATOM   1960 C CG  . LYS   C 1 68 ? 28.659  -24.333 10.398  1.00 37.47  ? 67  LYS   C CG  1 
ATOM   1961 C CD  . LYS   C 1 68 ? 29.939  -24.423 11.244  1.00 47.77  ? 67  LYS   C CD  1 
ATOM   1962 C CE  . LYS   C 1 68 ? 30.759  -25.672 11.121  1.00 57.95  ? 67  LYS   C CE  1 
ATOM   1963 N NZ  . LYS   C 1 68 ? 31.111  -26.064 9.750   1.00 68.39  ? 67  LYS   C NZ  1 
ATOM   1964 N N   . TYR   C 1 69 ? 24.954  -24.152 11.300  1.00 31.26  ? 68  TYR   C N   1 
ATOM   1965 C CA  . TYR   C 1 69 ? 24.108  -25.340 11.425  1.00 30.41  ? 68  TYR   C CA  1 
ATOM   1966 C C   . TYR   C 1 69 ? 22.633  -25.009 11.237  1.00 31.74  ? 68  TYR   C C   1 
ATOM   1967 O O   . TYR   C 1 69 ? 21.834  -25.932 11.067  1.00 30.67  ? 68  TYR   C O   1 
ATOM   1968 C CB  . TYR   C 1 69 ? 24.249  -25.923 12.845  1.00 29.49  ? 68  TYR   C CB  1 
ATOM   1969 C CG  . TYR   C 1 69 ? 25.678  -26.370 13.123  1.00 28.06  ? 68  TYR   C CG  1 
ATOM   1970 C CD1 . TYR   C 1 69 ? 26.379  -27.159 12.219  1.00 32.43  ? 68  TYR   C CD1 1 
ATOM   1971 C CD2 . TYR   C 1 69 ? 26.306  -25.981 14.309  1.00 34.34  ? 68  TYR   C CD2 1 
ATOM   1972 C CE1 . TYR   C 1 69 ? 27.670  -27.600 12.486  1.00 34.33  ? 68  TYR   C CE1 1 
ATOM   1973 C CE2 . TYR   C 1 69 ? 27.598  -26.406 14.579  1.00 36.93  ? 68  TYR   C CE2 1 
ATOM   1974 C CZ  . TYR   C 1 69 ? 28.271  -27.190 13.664  1.00 35.00  ? 68  TYR   C CZ  1 
ATOM   1975 O OH  . TYR   C 1 69 ? 29.542  -27.560 14.011  1.00 39.40  ? 68  TYR   C OH  1 
ATOM   1976 N N   . GLY   C 1 70 ? 22.261  -23.717 11.247  1.00 30.30  ? 69  GLY   C N   1 
ATOM   1977 C CA  . GLY   C 1 70 ? 20.838  -23.400 11.206  1.00 27.46  ? 69  GLY   C CA  1 
ATOM   1978 C C   . GLY   C 1 70 ? 20.428  -23.272 9.741   1.00 30.40  ? 69  GLY   C C   1 
ATOM   1979 O O   . GLY   C 1 70 ? 20.402  -22.159 9.210   1.00 32.96  ? 69  GLY   C O   1 
ATOM   1980 N N   . LYS   C 1 71 ? 20.303  -24.427 9.079   1.00 30.46  ? 70  LYS   C N   1 
ATOM   1981 C CA  . LYS   C 1 71 ? 19.919  -24.481 7.676   1.00 31.80  ? 70  LYS   C CA  1 
ATOM   1982 C C   . LYS   C 1 71 ? 19.054  -25.714 7.524   1.00 32.39  ? 70  LYS   C C   1 
ATOM   1983 O O   . LYS   C 1 71 ? 19.173  -26.683 8.288   1.00 31.85  ? 70  LYS   C O   1 
ATOM   1984 C CB  . LYS   C 1 71 ? 21.127  -24.621 6.743   1.00 32.73  ? 70  LYS   C CB  1 
ATOM   1985 C CG  . LYS   C 1 71 ? 22.088  -25.657 7.223   1.00 35.38  ? 70  LYS   C CG  1 
ATOM   1986 C CD  . LYS   C 1 71 ? 23.372  -25.916 6.446   1.00 41.88  ? 70  LYS   C CD  1 
ATOM   1987 C CE  . LYS   C 1 71 ? 24.090  -26.992 7.205   1.00 43.92  ? 70  LYS   C CE  1 
ATOM   1988 N N   . PRO   C 1 72 ? 18.089  -25.711 6.595   1.00 27.43  ? 71  PRO   C N   1 
ATOM   1989 C CA  . PRO   C 1 72 ? 17.154  -26.830 6.530   1.00 26.73  ? 71  PRO   C CA  1 
ATOM   1990 C C   . PRO   C 1 72 ? 17.813  -28.163 6.199   1.00 28.27  ? 71  PRO   C C   1 
ATOM   1991 O O   . PRO   C 1 72 ? 18.862  -28.247 5.532   1.00 31.83  ? 71  PRO   C O   1 
ATOM   1992 C CB  . PRO   C 1 72 ? 16.152  -26.396 5.436   1.00 28.99  ? 71  PRO   C CB  1 
ATOM   1993 C CG  . PRO   C 1 72 ? 16.253  -24.878 5.498   1.00 28.31  ? 71  PRO   C CG  1 
ATOM   1994 C CD  . PRO   C 1 72 ? 17.726  -24.559 5.743   1.00 28.69  ? 71  PRO   C CD  1 
ATOM   1995 N N   . ASN   C 1 73 ? 17.113  -29.191 6.640   1.00 29.10  ? 72  ASN   C N   1 
ATOM   1996 C CA  . ASN   C 1 73 ? 17.410  -30.478 6.057   1.00 36.00  ? 72  ASN   C CA  1 
ATOM   1997 C C   . ASN   C 1 73 ? 16.192  -31.377 6.160   1.00 31.81  ? 72  ASN   C C   1 
ATOM   1998 O O   . ASN   C 1 73 ? 15.185  -31.066 6.792   1.00 33.86  ? 72  ASN   C O   1 
ATOM   1999 C CB  . ASN   C 1 73 ? 18.770  -31.054 6.424   1.00 40.42  ? 72  ASN   C CB  1 
ATOM   2000 C CG  . ASN   C 1 73 ? 18.749  -31.738 7.763   1.00 41.09  ? 72  ASN   C CG  1 
ATOM   2001 O OD1 . ASN   C 1 73 ? 18.321  -32.896 7.859   1.00 38.59  ? 72  ASN   C OD1 1 
ATOM   2002 N ND2 . ASN   C 1 73 ? 19.325  -31.091 8.752   1.00 46.28  ? 72  ASN   C ND2 1 
ATOM   2003 N N   . LYS   C 1 74 ? 16.306  -32.513 5.492   1.00 32.97  ? 73  LYS   C N   1 
ATOM   2004 C CA  . LYS   C 1 74 ? 15.113  -33.313 5.271   1.00 28.76  ? 73  LYS   C CA  1 
ATOM   2005 C C   . LYS   C 1 74 ? 14.828  -34.256 6.432   1.00 31.70  ? 73  LYS   C C   1 
ATOM   2006 O O   . LYS   C 1 74 ? 13.760  -34.879 6.476   1.00 33.59  ? 73  LYS   C O   1 
ATOM   2007 C CB  . LYS   C 1 74 ? 15.353  -34.064 3.956   1.00 34.28  ? 73  LYS   C CB  1 
ATOM   2008 N N   . ARG   C 1 75 ? 15.725  -34.324 7.439   1.00 26.93  ? 74  ARG   C N   1 
ATOM   2009 C CA  . ARG   C 1 75 ? 15.479  -35.305 8.495   1.00 26.96  ? 74  ARG   C CA  1 
ATOM   2010 C C   . ARG   C 1 75 ? 14.209  -34.968 9.277   1.00 28.22  ? 74  ARG   C C   1 
ATOM   2011 O O   . ARG   C 1 75 ? 13.839  -33.798 9.470   1.00 30.03  ? 74  ARG   C O   1 
ATOM   2012 C CB  . ARG   C 1 75 ? 16.722  -35.358 9.409   1.00 30.21  ? 74  ARG   C CB  1 
ATOM   2013 C CG  . ARG   C 1 75 ? 18.055  -35.619 8.697   1.00 34.92  ? 74  ARG   C CG  1 
ATOM   2014 C CD  . ARG   C 1 75 ? 18.398  -37.015 8.154   1.00 40.39  ? 74  ARG   C CD  1 
ATOM   2015 N NE  . ARG   C 1 75 ? 18.357  -37.946 9.280   1.00 38.41  ? 74  ARG   C NE  1 
ATOM   2016 C CZ  . ARG   C 1 75 ? 19.479  -38.388 9.894   1.00 34.25  ? 74  ARG   C CZ  1 
ATOM   2017 N NH1 . ARG   C 1 75 ? 19.373  -38.999 11.049  1.00 39.66  ? 74  ARG   C NH1 1 
ATOM   2018 N NH2 . ARG   C 1 75 ? 20.646  -38.084 9.353   1.00 32.26  ? 74  ARG   C NH2 1 
ATOM   2019 N N   . LYS   C 1 76 ? 13.492  -36.021 9.685   1.00 32.86  ? 75  LYS   C N   1 
ATOM   2020 C CA  . LYS   C 1 76 ? 12.206  -35.910 10.366  1.00 37.12  ? 75  LYS   C CA  1 
ATOM   2021 C C   . LYS   C 1 76 ? 12.282  -34.983 11.584  1.00 32.31  ? 75  LYS   C C   1 
ATOM   2022 O O   . LYS   C 1 76 ? 13.086  -35.163 12.502  1.00 32.89  ? 75  LYS   C O   1 
ATOM   2023 C CB  . LYS   C 1 76 ? 11.617  -37.289 10.706  1.00 37.64  ? 75  LYS   C CB  1 
ATOM   2024 C CG  . LYS   C 1 76 ? 10.135  -37.260 11.035  1.00 43.86  ? 75  LYS   C CG  1 
ATOM   2025 C CD  . LYS   C 1 76 ? 9.615   -38.509 11.748  1.00 52.77  ? 75  LYS   C CD  1 
ATOM   2026 N N   . GLY   C 1 77 ? 11.520  -33.886 11.491  1.00 33.24  ? 76  GLY   C N   1 
ATOM   2027 C CA  . GLY   C 1 77 ? 11.279  -32.997 12.620  1.00 29.62  ? 76  GLY   C CA  1 
ATOM   2028 C C   . GLY   C 1 77 ? 12.253  -31.802 12.627  1.00 26.44  ? 76  GLY   C C   1 
ATOM   2029 O O   . GLY   C 1 77 ? 12.129  -30.881 13.429  1.00 32.62  ? 76  GLY   C O   1 
ATOM   2030 N N   . PHE   C 1 78 ? 13.217  -31.808 11.712  1.00 27.12  ? 77  PHE   C N   1 
ATOM   2031 C CA  . PHE   C 1 78 ? 14.321  -30.871 11.804  1.00 27.55  ? 77  PHE   C CA  1 
ATOM   2032 C C   . PHE   C 1 78 ? 13.819  -29.451 11.520  1.00 28.65  ? 77  PHE   C C   1 
ATOM   2033 O O   . PHE   C 1 78 ? 14.144  -28.511 12.238  1.00 27.30  ? 77  PHE   C O   1 
ATOM   2034 C CB  . PHE   C 1 78 ? 15.415  -31.290 10.830  1.00 30.63  ? 77  PHE   C CB  1 
ATOM   2035 C CG  . PHE   C 1 78 ? 16.687  -30.515 11.093  1.00 28.43  ? 77  PHE   C CG  1 
ATOM   2036 C CD1 . PHE   C 1 78 ? 16.865  -29.229 10.578  1.00 28.54  ? 77  PHE   C CD1 1 
ATOM   2037 C CD2 . PHE   C 1 78 ? 17.720  -31.069 11.852  1.00 26.55  ? 77  PHE   C CD2 1 
ATOM   2038 C CE1 . PHE   C 1 78 ? 18.040  -28.521 10.814  1.00 28.13  ? 77  PHE   C CE1 1 
ATOM   2039 C CE2 . PHE   C 1 78 ? 18.890  -30.347 12.095  1.00 26.77  ? 77  PHE   C CE2 1 
ATOM   2040 C CZ  . PHE   C 1 78 ? 19.076  -29.085 11.557  1.00 27.57  ? 77  PHE   C CZ  1 
ATOM   2041 N N   . ASN   C 1 79 ? 13.037  -29.306 10.432  1.00 28.77  ? 78  ASN   C N   1 
ATOM   2042 C CA  . ASN   C 1 79 ? 12.710  -27.938 10.053  1.00 30.85  ? 78  ASN   C CA  1 
ATOM   2043 C C   . ASN   C 1 79 ? 11.719  -27.319 11.028  1.00 31.39  ? 78  ASN   C C   1 
ATOM   2044 O O   . ASN   C 1 79 ? 11.777  -26.111 11.318  1.00 30.14  ? 78  ASN   C O   1 
ATOM   2045 C CB  . ASN   C 1 79 ? 12.257  -27.856 8.604   1.00 28.12  ? 78  ASN   C CB  1 
ATOM   2046 C CG  . ASN   C 1 79 ? 13.347  -28.301 7.661   1.00 30.54  ? 78  ASN   C CG  1 
ATOM   2047 O OD1 . ASN   C 1 79 ? 14.521  -28.045 7.918   1.00 27.11  ? 78  ASN   C OD1 1 
ATOM   2048 N ND2 . ASN   C 1 79 ? 12.991  -28.931 6.543   1.00 29.91  ? 78  ASN   C ND2 1 
ATOM   2049 N N   . GLU   C 1 80 ? 10.812  -28.149 11.541  1.00 31.85  ? 79  GLU   C N   1 
ATOM   2050 C CA  . GLU   C 1 80 ? 9.969   -27.657 12.624  1.00 30.60  ? 79  GLU   C CA  1 
ATOM   2051 C C   . GLU   C 1 80 ? 10.839  -27.243 13.813  1.00 34.63  ? 79  GLU   C C   1 
ATOM   2052 O O   . GLU   C 1 80 ? 10.576  -26.240 14.479  1.00 30.94  ? 79  GLU   C O   1 
ATOM   2053 C CB  . GLU   C 1 80 ? 8.859   -28.654 12.939  1.00 37.51  ? 79  GLU   C CB  1 
ATOM   2054 C CG  . GLU   C 1 80 ? 8.005   -28.217 14.119  1.00 34.64  ? 79  GLU   C CG  1 
ATOM   2055 C CD  . GLU   C 1 80 ? 6.752   -29.045 14.293  1.00 45.23  ? 79  GLU   C CD  1 
ATOM   2056 O OE1 . GLU   C 1 80 ? 6.664   -30.180 13.782  1.00 54.50  ? 79  GLU   C OE1 1 
ATOM   2057 O OE2 . GLU   C 1 80 ? 5.834   -28.518 14.936  1.00 43.65  ? 79  GLU   C OE2 1 
ATOM   2058 N N   . GLY   C 1 81 ? 11.897  -28.032 14.080  1.00 30.41  ? 80  GLY   C N   1 
ATOM   2059 C CA  . GLY   C 1 81 ? 12.826  -27.668 15.138  1.00 31.19  ? 80  GLY   C CA  1 
ATOM   2060 C C   . GLY   C 1 81 ? 13.492  -26.309 14.919  1.00 31.25  ? 80  GLY   C C   1 
ATOM   2061 O O   . GLY   C 1 81 ? 13.637  -25.551 15.862  1.00 30.16  ? 80  GLY   C O   1 
ATOM   2062 N N   . LEU   C 1 82 ? 13.948  -26.036 13.678  1.00 29.59  ? 81  LEU   C N   1 
ATOM   2063 C CA  . LEU   C 1 82 ? 14.492  -24.733 13.319  1.00 31.53  ? 81  LEU   C CA  1 
ATOM   2064 C C   . LEU   C 1 82 ? 13.462  -23.638 13.608  1.00 27.22  ? 81  LEU   C C   1 
ATOM   2065 O O   . LEU   C 1 82 ? 13.854  -22.549 14.069  1.00 29.58  ? 81  LEU   C O   1 
ATOM   2066 C CB  . LEU   C 1 82 ? 14.913  -24.681 11.851  1.00 28.95  ? 81  LEU   C CB  1 
ATOM   2067 C CG  . LEU   C 1 82 ? 16.168  -25.462 11.452  1.00 27.50  ? 81  LEU   C CG  1 
ATOM   2068 C CD1 . LEU   C 1 82 ? 16.463  -25.315 9.975   1.00 27.34  ? 81  LEU   C CD1 1 
ATOM   2069 C CD2 . LEU   C 1 82 ? 17.393  -25.074 12.227  1.00 24.88  ? 81  LEU   C CD2 1 
ATOM   2070 N N   . TRP   C 1 83 ? 12.181  -23.901 13.326  1.00 28.45  ? 82  TRP   C N   1 
ATOM   2071 C CA  . TRP   C 1 83 ? 11.197  -22.847 13.534  1.00 34.56  ? 82  TRP   C CA  1 
ATOM   2072 C C   . TRP   C 1 83 ? 11.085  -22.575 15.040  1.00 34.54  ? 82  TRP   C C   1 
ATOM   2073 O O   . TRP   C 1 83 ? 11.087  -21.420 15.484  1.00 34.65  ? 82  TRP   C O   1 
ATOM   2074 C CB  . TRP   C 1 83 ? 9.831   -23.201 12.926  1.00 35.22  ? 82  TRP   C CB  1 
ATOM   2075 C CG  . TRP   C 1 83 ? 8.876   -22.042 13.064  1.00 38.24  ? 82  TRP   C CG  1 
ATOM   2076 C CD1 . TRP   C 1 83 ? 8.736   -21.008 12.179  1.00 38.55  ? 82  TRP   C CD1 1 
ATOM   2077 C CD2 . TRP   C 1 83 ? 7.992   -21.743 14.171  1.00 41.03  ? 82  TRP   C CD2 1 
ATOM   2078 N NE1 . TRP   C 1 83 ? 7.790   -20.117 12.627  1.00 34.31  ? 82  TRP   C NE1 1 
ATOM   2079 C CE2 . TRP   C 1 83 ? 7.322   -20.534 13.846  1.00 38.74  ? 82  TRP   C CE2 1 
ATOM   2080 C CE3 . TRP   C 1 83 ? 7.711   -22.374 15.394  1.00 36.41  ? 82  TRP   C CE3 1 
ATOM   2081 C CZ2 . TRP   C 1 83 ? 6.392   -19.951 14.703  1.00 42.54  ? 82  TRP   C CZ2 1 
ATOM   2082 C CZ3 . TRP   C 1 83 ? 6.783   -21.799 16.240  1.00 46.85  ? 82  TRP   C CZ3 1 
ATOM   2083 C CH2 . TRP   C 1 83 ? 6.152   -20.597 15.901  1.00 44.54  ? 82  TRP   C CH2 1 
ATOM   2084 N N   . GLU   C 1 84 ? 11.073  -23.660 15.831  1.00 30.80  ? 83  GLU   C N   1 
ATOM   2085 C CA  . GLU   C 1 84 ? 10.939  -23.539 17.283  1.00 34.93  ? 83  GLU   C CA  1 
ATOM   2086 C C   . GLU   C 1 84 ? 12.107  -22.791 17.934  1.00 35.47  ? 83  GLU   C C   1 
ATOM   2087 O O   . GLU   C 1 84 ? 11.890  -21.921 18.799  1.00 37.92  ? 83  GLU   C O   1 
ATOM   2088 C CB  . GLU   C 1 84 ? 10.736  -24.920 17.892  1.00 32.27  ? 83  GLU   C CB  1 
ATOM   2089 C CG  . GLU   C 1 84 ? 9.415   -25.565 17.493  1.00 34.54  ? 83  GLU   C CG  1 
ATOM   2090 C CD  . GLU   C 1 84 ? 9.323   -26.969 18.024  1.00 37.32  ? 83  GLU   C CD  1 
ATOM   2091 O OE1 . GLU   C 1 84 ? 10.327  -27.421 18.647  1.00 36.87  ? 83  GLU   C OE1 1 
ATOM   2092 O OE2 . GLU   C 1 84 ? 8.263   -27.592 17.816  1.00 38.26  ? 83  GLU   C OE2 1 
ATOM   2093 N N   . ILE   C 1 85 ? 13.354  -23.096 17.545  1.00 33.04  ? 84  ILE   C N   1 
ATOM   2094 C CA  . ILE   C 1 85 ? 14.507  -22.496 18.188  1.00 35.91  ? 84  ILE   C CA  1 
ATOM   2095 C C   . ILE   C 1 85 ? 14.561  -20.989 17.923  1.00 36.03  ? 84  ILE   C C   1 
ATOM   2096 O O   . ILE   C 1 85 ? 15.063  -20.240 18.747  1.00 35.55  ? 84  ILE   C O   1 
ATOM   2097 C CB  . ILE   C 1 85 ? 15.811  -23.216 17.826  1.00 34.54  ? 84  ILE   C CB  1 
ATOM   2098 C CG1 . ILE   C 1 85 ? 16.905  -22.880 18.858  1.00 34.25  ? 84  ILE   C CG1 1 
ATOM   2099 C CG2 . ILE   C 1 85 ? 16.226  -22.916 16.363  1.00 31.95  ? 84  ILE   C CG2 1 
ATOM   2100 C CD1 . ILE   C 1 85 ? 18.097  -23.832 18.926  1.00 30.02  ? 84  ILE   C CD1 1 
ATOM   2101 N N   . GLN   C 1 86 ? 14.040  -20.570 16.763  1.00 32.03  ? 85  GLN   C N   1 
ATOM   2102 C CA  . GLN   C 1 86 ? 14.124  -19.159 16.384  1.00 38.85  ? 85  GLN   C CA  1 
ATOM   2103 C C   . GLN   C 1 86 ? 12.918  -18.363 16.887  1.00 35.93  ? 85  GLN   C C   1 
ATOM   2104 O O   . GLN   C 1 86 ? 13.062  -17.176 17.180  1.00 40.65  ? 85  GLN   C O   1 
ATOM   2105 C CB  . GLN   C 1 86 ? 14.344  -19.012 14.870  1.00 34.51  ? 85  GLN   C CB  1 
ATOM   2106 C CG  . GLN   C 1 86 ? 14.444  -17.571 14.369  1.00 33.71  ? 85  GLN   C CG  1 
ATOM   2107 C CD  . GLN   C 1 86 ? 14.826  -17.523 12.899  1.00 36.39  ? 85  GLN   C CD  1 
ATOM   2108 O OE1 . GLN   C 1 86 ? 14.741  -18.526 12.171  1.00 35.99  ? 85  GLN   C OE1 1 
ATOM   2109 N NE2 . GLN   C 1 86 ? 15.339  -16.381 12.462  1.00 37.23  ? 85  GLN   C NE2 1 
ATOM   2110 N N   . ASN   C 1 87 ? 11.750  -18.989 16.966  1.00 37.00  ? 86  ASN   C N   1 
ATOM   2111 C CA  . ASN   C 1 87 ? 10.499  -18.265 17.125  1.00 40.38  ? 86  ASN   C CA  1 
ATOM   2112 C C   . ASN   C 1 87 ? 9.827   -18.579 18.461  1.00 43.25  ? 86  ASN   C C   1 
ATOM   2113 O O   . ASN   C 1 87 ? 8.905   -17.875 18.849  1.00 43.97  ? 86  ASN   C O   1 
ATOM   2114 C CB  . ASN   C 1 87 ? 9.517   -18.557 15.994  1.00 39.31  ? 86  ASN   C CB  1 
ATOM   2115 C CG  . ASN   C 1 87 ? 10.067  -18.005 14.706  1.00 42.89  ? 86  ASN   C CG  1 
ATOM   2116 O OD1 . ASN   C 1 87 ? 10.113  -16.783 14.545  1.00 45.94  ? 86  ASN   C OD1 1 
ATOM   2117 N ND2 . ASN   C 1 87 ? 10.570  -18.867 13.837  1.00 35.15  ? 86  ASN   C ND2 1 
ATOM   2118 N N   . ASN   C 1 88 ? 10.221  -19.671 19.126  1.00 43.46  ? 87  ASN   C N   1 
ATOM   2119 C CA  . ASN   C 1 88 ? 9.475   -20.070 20.314  1.00 41.40  ? 87  ASN   C CA  1 
ATOM   2120 C C   . ASN   C 1 88 ? 10.339  -20.947 21.212  1.00 40.84  ? 87  ASN   C C   1 
ATOM   2121 O O   . ASN   C 1 88 ? 9.886   -22.017 21.639  1.00 48.46  ? 87  ASN   C O   1 
ATOM   2122 C CB  . ASN   C 1 88 ? 8.152   -20.745 19.964  1.00 47.13  ? 87  ASN   C CB  1 
ATOM   2123 C CG  . ASN   C 1 88 ? 7.195   -20.712 21.137  1.00 52.94  ? 87  ASN   C CG  1 
ATOM   2124 O OD1 . ASN   C 1 88 ? 7.443   -20.000 22.123  1.00 52.12  ? 87  ASN   C OD1 1 
ATOM   2125 N ND2 . ASN   C 1 88 ? 6.106   -21.457 21.039  1.00 48.63  ? 87  ASN   C ND2 1 
ATOM   2126 N N   . PRO   C 1 89 ? 11.582  -20.527 21.517  1.00 41.27  ? 88  PRO   C N   1 
ATOM   2127 C CA  . PRO   C 1 89 ? 12.567  -21.437 22.111  1.00 41.97  ? 88  PRO   C CA  1 
ATOM   2128 C C   . PRO   C 1 89 ? 12.276  -21.906 23.538  1.00 49.21  ? 88  PRO   C C   1 
ATOM   2129 O O   . PRO   C 1 89 ? 12.882  -22.870 24.007  1.00 44.51  ? 88  PRO   C O   1 
ATOM   2130 C CB  . PRO   C 1 89 ? 13.894  -20.687 22.024  1.00 40.85  ? 88  PRO   C CB  1 
ATOM   2131 C CG  . PRO   C 1 89 ? 13.472  -19.216 21.958  1.00 46.84  ? 88  PRO   C CG  1 
ATOM   2132 C CD  . PRO   C 1 89 ? 12.141  -19.196 21.221  1.00 42.40  ? 88  PRO   C CD  1 
ATOM   2133 N N   . HIS   C 1 90 ? 11.341  -21.233 24.221  1.00 52.12  ? 89  HIS   C N   1 
ATOM   2134 C CA  . HIS   C 1 90 ? 11.184  -21.495 25.645  1.00 50.41  ? 89  HIS   C CA  1 
ATOM   2135 C C   . HIS   C 1 90 ? 9.754   -21.903 25.987  1.00 51.90  ? 89  HIS   C C   1 
ATOM   2136 O O   . HIS   C 1 90 ? 9.400   -21.922 27.158  1.00 58.97  ? 89  HIS   C O   1 
ATOM   2137 C CB  . HIS   C 1 90 ? 11.740  -20.339 26.476  1.00 40.23  ? 89  HIS   C CB  1 
ATOM   2138 C CG  . HIS   C 1 90 ? 13.192  -20.030 26.280  1.00 37.59  ? 89  HIS   C CG  1 
ATOM   2139 N ND1 . HIS   C 1 90 ? 13.662  -18.858 25.725  1.00 43.12  ? 89  HIS   C ND1 1 
ATOM   2140 C CD2 . HIS   C 1 90 ? 14.285  -20.714 26.652  1.00 40.74  ? 89  HIS   C CD2 1 
ATOM   2141 C CE1 . HIS   C 1 90 ? 14.993  -18.849 25.727  1.00 42.32  ? 89  HIS   C CE1 1 
ATOM   2142 N NE2 . HIS   C 1 90 ? 15.397  -19.977 26.291  1.00 43.61  ? 89  HIS   C NE2 1 
ATOM   2143 N N   . ALA   C 1 91 ? 8.944   -22.250 24.981  1.00 52.94  ? 90  ALA   C N   1 
ATOM   2144 C CA  . ALA   C 1 91 ? 7.608   -22.792 25.206  1.00 54.52  ? 90  ALA   C CA  1 
ATOM   2145 C C   . ALA   C 1 91 ? 7.660   -24.239 25.717  1.00 61.74  ? 90  ALA   C C   1 
ATOM   2146 O O   . ALA   C 1 91 ? 8.730   -24.842 25.814  1.00 63.49  ? 90  ALA   C O   1 
ATOM   2147 C CB  . ALA   C 1 91 ? 6.764   -22.665 23.952  1.00 54.91  ? 90  ALA   C CB  1 
ATOM   2148 N N   . SER   C 1 92 ? 6.466   -24.801 25.981  1.00 67.83  ? 91  SER   C N   1 
ATOM   2149 C CA  . SER   C 1 92 ? 6.256   -26.026 26.748  1.00 72.83  ? 91  SER   C CA  1 
ATOM   2150 C C   . SER   C 1 92 ? 6.707   -27.267 25.988  1.00 69.06  ? 91  SER   C C   1 
ATOM   2151 O O   . SER   C 1 92 ? 7.577   -28.000 26.451  1.00 71.08  ? 91  SER   C O   1 
ATOM   2152 C CB  . SER   C 1 92 ? 4.799   -26.186 27.140  1.00 67.34  ? 91  SER   C CB  1 
ATOM   2153 O OG  . SER   C 1 92 ? 4.454   -25.306 28.195  1.00 82.04  ? 91  SER   C OG  1 
ATOM   2154 N N   . TYR   C 1 93 ? 6.034   -27.520 24.860  1.00 72.25  ? 92  TYR   C N   1 
ATOM   2155 C CA  . TYR   C 1 93 ? 6.140   -28.761 24.109  1.00 72.38  ? 92  TYR   C CA  1 
ATOM   2156 C C   . TYR   C 1 93 ? 5.910   -29.945 25.061  1.00 75.96  ? 92  TYR   C C   1 
ATOM   2157 O O   . TYR   C 1 93 ? 6.024   -31.097 24.591  1.00 86.40  ? 92  TYR   C O   1 
ATOM   2158 C CB  . TYR   C 1 93 ? 7.461   -28.783 23.328  1.00 63.13  ? 92  TYR   C CB  1 
ATOM   2159 C CG  . TYR   C 1 93 ? 7.726   -27.517 22.518  1.00 53.82  ? 92  TYR   C CG  1 
ATOM   2160 C CD1 . TYR   C 1 93 ? 6.967   -27.214 21.389  1.00 49.99  ? 92  TYR   C CD1 1 
ATOM   2161 C CD2 . TYR   C 1 93 ? 8.738   -26.630 22.879  1.00 50.87  ? 92  TYR   C CD2 1 
ATOM   2162 C CE1 . TYR   C 1 93 ? 7.187   -26.062 20.653  1.00 50.09  ? 92  TYR   C CE1 1 
ATOM   2163 C CE2 . TYR   C 1 93 ? 8.976   -25.480 22.136  1.00 53.39  ? 92  TYR   C CE2 1 
ATOM   2164 C CZ  . TYR   C 1 93 ? 8.204   -25.198 21.022  1.00 53.61  ? 92  TYR   C CZ  1 
ATOM   2165 O OH  . TYR   C 1 93 ? 8.422   -24.057 20.291  1.00 56.20  ? 92  TYR   C OH  1 
HETATM 2166 S S   . SO4   D 2 .  ? 1.500   -33.545 2.179   1.00 96.08  ? 101 SO4   A S   1 
HETATM 2167 O O1  . SO4   D 2 .  ? 2.095   -34.333 1.119   1.00 72.59  ? 101 SO4   A O1  1 
HETATM 2168 O O2  . SO4   D 2 .  ? 1.576   -32.143 1.853   1.00 82.49  ? 101 SO4   A O2  1 
HETATM 2169 O O3  . SO4   D 2 .  ? 0.115   -33.914 2.347   1.00 100.46 ? 101 SO4   A O3  1 
HETATM 2170 O O4  . SO4   D 2 .  ? 2.209   -33.799 3.406   1.00 91.10  ? 101 SO4   A O4  1 
HETATM 2171 S S   . SO4   E 2 .  ? -8.883  -24.780 1.510   1.00 91.39  ? 102 SO4   A S   1 
HETATM 2172 O O1  . SO4   E 2 .  ? -9.522  -24.385 0.277   1.00 75.61  ? 102 SO4   A O1  1 
HETATM 2173 O O2  . SO4   E 2 .  ? -9.062  -23.749 2.506   1.00 78.50  ? 102 SO4   A O2  1 
HETATM 2174 O O3  . SO4   E 2 .  ? -9.453  -26.024 1.977   1.00 83.37  ? 102 SO4   A O3  1 
HETATM 2175 O O4  . SO4   E 2 .  ? -7.478  -24.967 1.280   1.00 99.45  ? 102 SO4   A O4  1 
HETATM 2176 C C1  . EDO   F 3 .  ? 14.220  -19.599 -7.270  1.00 36.25  ? 103 EDO   A C1  1 
HETATM 2177 O O1  . EDO   F 3 .  ? 15.402  -18.841 -7.194  1.00 33.98  ? 103 EDO   A O1  1 
HETATM 2178 C C2  . EDO   F 3 .  ? 13.270  -19.153 -8.346  1.00 33.40  ? 103 EDO   A C2  1 
HETATM 2179 O O2  . EDO   F 3 .  ? 12.806  -17.825 -8.236  1.00 32.33  ? 103 EDO   A O2  1 
HETATM 2180 N N1  . A1A39 G 4 .  ? 1.998   -25.577 -6.399  0.60 52.36  ? 104 A1A39 A N1  1 
HETATM 2181 N N3  . A1A39 G 4 .  ? 3.072   -26.974 -7.914  0.60 52.30  ? 104 A1A39 A N3  1 
HETATM 2182 C C4  . A1A39 G 4 .  ? 1.991   -24.194 -5.932  0.60 54.12  ? 104 A1A39 A C4  1 
HETATM 2183 C C5  . A1A39 G 4 .  ? 2.364   -26.495 -5.317  0.60 62.27  ? 104 A1A39 A C5  1 
HETATM 2184 C C6  . A1A39 G 4 .  ? 2.427   -25.823 -7.697  0.60 51.86  ? 104 A1A39 A C6  1 
HETATM 2185 C C7  . A1A39 G 4 .  ? 2.189   -24.902 -8.738  0.60 44.48  ? 104 A1A39 A C7  1 
HETATM 2186 C C8  . A1A39 G 4 .  ? 2.653   -25.235 -10.000 0.60 25.85  ? 104 A1A39 A C8  1 
HETATM 2187 C C   . A1A39 G 4 .  ? 2.669   -25.879 -2.027  0.60 54.88  ? 104 A1A39 A C   1 
HETATM 2188 N N   . A1A39 G 4 .  ? 2.095   -26.910 -2.907  0.60 63.84  ? 104 A1A39 A N   1 
HETATM 2189 C C1  . A1A39 G 4 .  ? 1.432   -26.362 -4.112  0.60 61.98  ? 104 A1A39 A C1  1 
HETATM 2190 C C3  . A1A39 G 4 .  ? 0.953   -24.014 -4.854  0.60 62.56  ? 104 A1A39 A C3  1 
HETATM 2191 C C2  . A1A39 G 4 .  ? 1.251   -24.920 -3.671  0.60 60.62  ? 104 A1A39 A C2  1 
HETATM 2192 N N2  . A1A39 G 4 .  ? 3.533   -27.271 -9.155  0.60 38.59  ? 104 A1A39 A N2  1 
HETATM 2193 C C9  . A1A39 G 4 .  ? 3.330   -26.422 -10.150 0.60 39.13  ? 104 A1A39 A C9  1 
HETATM 2194 S S   . SO4   H 2 .  ? 9.286   -29.511 5.928   1.00 52.62  ? 105 SO4   A S   1 
HETATM 2195 O O1  . SO4   H 2 .  ? 10.152  -28.754 5.105   1.00 46.58  ? 105 SO4   A O1  1 
HETATM 2196 O O2  . SO4   H 2 .  ? 8.697   -30.596 5.122   1.00 50.01  ? 105 SO4   A O2  1 
HETATM 2197 O O3  . SO4   H 2 .  ? 10.028  -30.081 7.043   1.00 57.04  ? 105 SO4   A O3  1 
HETATM 2198 O O4  . SO4   H 2 .  ? 8.223   -28.669 6.420   1.00 63.82  ? 105 SO4   A O4  1 
HETATM 2199 S S   . SO4   I 2 .  ? 7.646   -8.407  -24.849 1.00 79.62  ? 101 SO4   B S   1 
HETATM 2200 O O1  . SO4   I 2 .  ? 8.760   -8.435  -25.760 1.00 42.39  ? 101 SO4   B O1  1 
HETATM 2201 O O2  . SO4   I 2 .  ? 6.481   -8.972  -25.511 1.00 55.44  ? 101 SO4   B O2  1 
HETATM 2202 O O3  . SO4   I 2 .  ? 7.870   -9.191  -23.605 1.00 43.47  ? 101 SO4   B O3  1 
HETATM 2203 O O4  . SO4   I 2 .  ? 7.470   -6.998  -24.545 1.00 60.66  ? 101 SO4   B O4  1 
HETATM 2204 S S   . SO4   J 2 .  ? 14.569  -26.974 -26.603 1.00 51.55  ? 102 SO4   B S   1 
HETATM 2205 O O1  . SO4   J 2 .  ? 15.878  -26.532 -26.208 1.00 57.41  ? 102 SO4   B O1  1 
HETATM 2206 O O2  . SO4   J 2 .  ? 14.693  -28.275 -27.224 1.00 62.92  ? 102 SO4   B O2  1 
HETATM 2207 O O3  . SO4   J 2 .  ? 13.727  -27.081 -25.441 1.00 63.33  ? 102 SO4   B O3  1 
HETATM 2208 O O4  . SO4   J 2 .  ? 13.970  -26.053 -27.542 1.00 53.35  ? 102 SO4   B O4  1 
HETATM 2209 N N1  . W0J   K 5 .  ? 18.927  -15.903 -22.601 0.64 44.32  ? 103 W0J   B N1  1 
HETATM 2210 N N3  . W0J   K 5 .  ? 18.108  -14.208 -23.963 0.64 33.53  ? 103 W0J   B N3  1 
HETATM 2211 C C4  . W0J   K 5 .  ? 19.854  -17.044 -22.676 0.64 45.82  ? 103 W0J   B C4  1 
HETATM 2212 C C5  . W0J   K 5 .  ? 18.215  -15.860 -21.322 0.64 52.14  ? 103 W0J   B C5  1 
HETATM 2213 C C6  . W0J   K 5 .  ? 18.248  -15.523 -23.751 0.64 38.32  ? 103 W0J   B C6  1 
HETATM 2214 C C7  . W0J   K 5 .  ? 17.760  -16.470 -24.648 0.64 33.88  ? 103 W0J   B C7  1 
HETATM 2215 C C8  . W0J   K 5 .  ? 17.104  -15.999 -25.771 0.64 30.10  ? 103 W0J   B C8  1 
HETATM 2216 C C   . W0J   K 5 .  ? 19.347  -13.646 -18.629 0.64 63.35  ? 103 W0J   B C   1 
HETATM 2217 N N   . W0J   K 5 .  ? 19.307  -14.084 -20.025 0.64 62.86  ? 103 W0J   B N   1 
HETATM 2218 C C1  . W0J   K 5 .  ? 19.181  -15.547 -20.185 0.64 57.58  ? 103 W0J   B C1  1 
HETATM 2219 C C3  . W0J   K 5 .  ? 20.379  -17.447 -21.304 0.64 48.49  ? 103 W0J   B C3  1 
HETATM 2220 C C2  . W0J   K 5 .  ? 20.521  -16.233 -20.395 0.64 50.18  ? 103 W0J   B C2  1 
HETATM 2221 N N2  . W0J   K 5 .  ? 17.474  -13.767 -25.069 0.64 28.37  ? 103 W0J   B N2  1 
HETATM 2222 C C9  . W0J   K 5 .  ? 16.973  -14.634 -25.924 0.64 26.06  ? 103 W0J   B C9  1 
HETATM 2223 S S   . SO4   L 2 .  ? 29.711  -38.784 12.287  1.00 102.56 ? 101 SO4   C S   1 
HETATM 2224 O O1  . SO4   L 2 .  ? 30.796  -37.940 11.844  1.00 97.41  ? 101 SO4   C O1  1 
HETATM 2225 O O2  . SO4   L 2 .  ? 28.508  -38.418 11.590  1.00 88.41  ? 101 SO4   C O2  1 
HETATM 2226 O O3  . SO4   L 2 .  ? 30.010  -40.163 12.010  1.00 90.84  ? 101 SO4   C O3  1 
HETATM 2227 O O4  . SO4   L 2 .  ? 29.525  -38.619 13.705  1.00 102.94 ? 101 SO4   C O4  1 
HETATM 2228 N N1  . W0J   M 5 .  ? 17.137  -37.728 18.544  0.50 36.22  ? 102 W0J   C N1  1 
HETATM 2229 N N3  . W0J   M 5 .  ? 17.134  -38.176 20.772  0.50 45.94  ? 102 W0J   C N3  1 
HETATM 2230 C C4  . W0J   M 5 .  ? 18.320  -37.008 18.081  0.50 34.13  ? 102 W0J   C C4  1 
HETATM 2231 C C5  . W0J   M 5 .  ? 15.928  -36.911 18.425  0.50 34.87  ? 102 W0J   C C5  1 
HETATM 2232 C C6  . W0J   M 5 .  ? 17.212  -38.661 19.541  0.50 38.91  ? 102 W0J   C C6  1 
HETATM 2233 C C7  . W0J   M 5 .  ? 17.265  -40.011 19.271  0.50 43.70  ? 102 W0J   C C7  1 
HETATM 2234 C C8  . W0J   M 5 .  ? 17.208  -40.874 20.352  0.50 40.09  ? 102 W0J   C C8  1 
HETATM 2235 C C   . W0J   M 5 .  ? 14.457  -38.715 16.638  0.50 36.71  ? 102 W0J   C C   1 
HETATM 2236 N N   . W0J   M 5 .  ? 15.541  -37.839 16.185  0.50 39.81  ? 102 W0J   C N   1 
HETATM 2237 C C1  . W0J   M 5 .  ? 15.684  -36.592 16.969  0.50 42.86  ? 102 W0J   C C1  1 
HETATM 2238 C C3  . W0J   M 5 .  ? 17.932  -35.665 17.496  0.50 38.06  ? 102 W0J   C C3  1 
HETATM 2239 C C2  . W0J   M 5 .  ? 16.874  -35.852 16.421  0.50 40.26  ? 102 W0J   C C2  1 
HETATM 2240 N N2  . W0J   M 5 .  ? 17.080  -39.026 21.820  0.50 49.30  ? 102 W0J   C N2  1 
HETATM 2241 C C9  . W0J   M 5 .  ? 17.110  -40.330 21.605  0.50 40.79  ? 102 W0J   C C9  1 
HETATM 2242 O O   . HOH   N 6 .  ? 9.555   -32.256 3.901   1.00 51.98  ? 201 HOH   A O   1 
HETATM 2243 O O   . HOH   N 6 .  ? -1.892  -31.126 -3.981  1.00 45.52  ? 202 HOH   A O   1 
HETATM 2244 O O   . HOH   N 6 .  ? 5.998   -28.895 7.018   1.00 47.30  ? 203 HOH   A O   1 
HETATM 2245 O O   . HOH   N 6 .  ? 0.619   -33.678 5.244   1.00 53.10  ? 204 HOH   A O   1 
HETATM 2246 O O   . HOH   N 6 .  ? -5.635  -13.508 -16.767 1.00 47.46  ? 205 HOH   A O   1 
HETATM 2247 O O   . HOH   N 6 .  ? 11.319  -29.822 3.156   1.00 44.27  ? 206 HOH   A O   1 
HETATM 2248 O O   . HOH   N 6 .  ? 13.314  -12.009 8.059   1.00 52.18  ? 207 HOH   A O   1 
HETATM 2249 O O   . HOH   N 6 .  ? 9.399   -18.270 -10.888 1.00 34.02  ? 208 HOH   A O   1 
HETATM 2250 O O   . HOH   N 6 .  ? 0.783   -10.584 -15.545 1.00 44.28  ? 209 HOH   A O   1 
HETATM 2251 O O   . HOH   N 6 .  ? 11.395  -23.799 9.751   1.00 35.87  ? 210 HOH   A O   1 
HETATM 2252 O O   . HOH   N 6 .  ? 4.676   -3.627  -3.287  1.00 32.04  ? 211 HOH   A O   1 
HETATM 2253 O O   . HOH   N 6 .  ? -2.086  3.205   -2.136  1.00 41.79  ? 212 HOH   A O   1 
HETATM 2254 O O   . HOH   N 6 .  ? -7.542  -17.128 6.730   1.00 44.29  ? 213 HOH   A O   1 
HETATM 2255 O O   . HOH   N 6 .  ? 4.243   -34.894 4.645   1.00 58.46  ? 214 HOH   A O   1 
HETATM 2256 O O   . HOH   N 6 .  ? 4.850   -7.912  1.192   1.00 32.70  ? 215 HOH   A O   1 
HETATM 2257 O O   . HOH   N 6 .  ? 8.485   -17.925 -15.960 1.00 53.00  ? 216 HOH   A O   1 
HETATM 2258 O O   . HOH   N 6 .  ? 16.139  -24.596 1.930   1.00 38.00  ? 217 HOH   A O   1 
HETATM 2259 O O   . HOH   N 6 .  ? 7.257   -10.558 -12.143 1.00 35.09  ? 218 HOH   A O   1 
HETATM 2260 O O   . HOH   N 6 .  ? 14.193  -15.741 -9.244  1.00 37.09  ? 219 HOH   A O   1 
HETATM 2261 O O   . HOH   N 6 .  ? 2.073   -4.680  -10.122 1.00 33.93  ? 220 HOH   A O   1 
HETATM 2262 O O   . HOH   N 6 .  ? 12.792  -13.277 -8.810  1.00 42.83  ? 221 HOH   A O   1 
HETATM 2263 O O   . HOH   N 6 .  ? -6.900  -21.760 -5.636  1.00 61.64  ? 222 HOH   A O   1 
HETATM 2264 O O   . HOH   N 6 .  ? -3.947  -21.211 6.103   1.00 39.21  ? 223 HOH   A O   1 
HETATM 2265 O O   . HOH   N 6 .  ? 9.869   -6.037  -1.629  1.00 32.44  ? 224 HOH   A O   1 
HETATM 2266 O O   . HOH   N 6 .  ? -7.838  -15.782 -1.042  1.00 36.57  ? 225 HOH   A O   1 
HETATM 2267 O O   . HOH   N 6 .  ? 1.990   -24.942 14.267  1.00 51.59  ? 226 HOH   A O   1 
HETATM 2268 O O   . HOH   N 6 .  ? -0.456  -20.931 6.988   1.00 34.11  ? 227 HOH   A O   1 
HETATM 2269 O O   . HOH   N 6 .  ? -5.483  -16.010 -8.013  1.00 28.31  ? 228 HOH   A O   1 
HETATM 2270 O O   . HOH   N 6 .  ? 20.178  -15.589 7.299   1.00 28.69  ? 229 HOH   A O   1 
HETATM 2271 O O   . HOH   N 6 .  ? 11.161  -5.220  -7.823  1.00 33.39  ? 230 HOH   A O   1 
HETATM 2272 O O   . HOH   N 6 .  ? 11.699  -11.977 5.932   1.00 33.15  ? 231 HOH   A O   1 
HETATM 2273 O O   . HOH   N 6 .  ? -3.593  -10.824 6.742   1.00 36.32  ? 232 HOH   A O   1 
HETATM 2274 O O   . HOH   N 6 .  ? 13.539  -12.028 -4.220  1.00 21.77  ? 233 HOH   A O   1 
HETATM 2275 O O   . HOH   N 6 .  ? 0.504   -23.397 9.344   1.00 46.55  ? 234 HOH   A O   1 
HETATM 2276 O O   . HOH   N 6 .  ? 13.176  -9.533  -7.201  1.00 41.07  ? 235 HOH   A O   1 
HETATM 2277 O O   . HOH   N 6 .  ? 1.521   -18.267 -18.797 1.00 52.37  ? 236 HOH   A O   1 
HETATM 2278 O O   . HOH   N 6 .  ? 15.953  -12.145 -5.297  1.00 33.10  ? 237 HOH   A O   1 
HETATM 2279 O O   . HOH   N 6 .  ? 1.996   0.534   -7.468  1.00 38.13  ? 238 HOH   A O   1 
HETATM 2280 O O   . HOH   N 6 .  ? 17.342  -18.365 -9.628  1.00 48.39  ? 239 HOH   A O   1 
HETATM 2281 O O   . HOH   N 6 .  ? 17.411  -12.912 1.394   1.00 20.66  ? 240 HOH   A O   1 
HETATM 2282 O O   . HOH   N 6 .  ? 13.528  -28.149 -4.816  1.00 48.82  ? 241 HOH   A O   1 
HETATM 2283 O O   . HOH   N 6 .  ? -0.368  -20.581 11.355  1.00 54.83  ? 242 HOH   A O   1 
HETATM 2284 O O   . HOH   N 6 .  ? 11.551  -6.037  -3.912  1.00 49.17  ? 243 HOH   A O   1 
HETATM 2285 O O   . HOH   N 6 .  ? 11.742  -12.396 -6.136  1.00 27.19  ? 244 HOH   A O   1 
HETATM 2286 O O   . HOH   N 6 .  ? -1.459  -22.150 -0.637  1.00 26.53  ? 245 HOH   A O   1 
HETATM 2287 O O   . HOH   N 6 .  ? -1.272  -11.834 11.278  1.00 36.45  ? 246 HOH   A O   1 
HETATM 2288 O O   . HOH   N 6 .  ? 1.899   -10.585 11.664  1.00 37.79  ? 247 HOH   A O   1 
HETATM 2289 O O   . HOH   N 6 .  ? 3.413   -29.671 -0.544  1.00 42.39  ? 248 HOH   A O   1 
HETATM 2290 O O   . HOH   N 6 .  ? 16.833  -12.075 -17.075 1.00 39.44  ? 249 HOH   A O   1 
HETATM 2291 O O   . HOH   N 6 .  ? 9.053   -16.360 -13.129 1.00 37.70  ? 250 HOH   A O   1 
HETATM 2292 O O   . HOH   N 6 .  ? 2.705   -6.406  5.461   1.00 35.73  ? 251 HOH   A O   1 
HETATM 2293 O O   . HOH   N 6 .  ? -5.529  -19.813 -5.715  1.00 37.43  ? 252 HOH   A O   1 
HETATM 2294 O O   . HOH   N 6 .  ? 14.736  -29.509 4.053   1.00 39.50  ? 253 HOH   A O   1 
HETATM 2295 O O   . HOH   N 6 .  ? -1.266  -7.584  11.423  1.00 46.75  ? 254 HOH   A O   1 
HETATM 2296 O O   . HOH   N 6 .  ? 8.367   -17.550 8.573   1.00 38.09  ? 255 HOH   A O   1 
HETATM 2297 O O   . HOH   N 6 .  ? 9.912   -30.447 9.919   1.00 32.20  ? 256 HOH   A O   1 
HETATM 2298 O O   . HOH   N 6 .  ? 10.320  -13.001 9.614   1.00 37.65  ? 257 HOH   A O   1 
HETATM 2299 O O   . HOH   N 6 .  ? 3.036   -9.867  -13.163 1.00 46.57  ? 258 HOH   A O   1 
HETATM 2300 O O   . HOH   N 6 .  ? -0.457  -29.485 10.302  1.00 52.07  ? 259 HOH   A O   1 
HETATM 2301 O O   . HOH   N 6 .  ? 6.527   -16.173 -15.050 1.00 46.48  ? 260 HOH   A O   1 
HETATM 2302 O O   . HOH   N 6 .  ? -7.688  -16.714 1.552   1.00 37.59  ? 261 HOH   A O   1 
HETATM 2303 O O   . HOH   N 6 .  ? 8.172   -7.896  1.249   1.00 31.15  ? 262 HOH   A O   1 
HETATM 2304 O O   . HOH   N 6 .  ? 6.719   -5.865  0.476   1.00 43.88  ? 263 HOH   A O   1 
HETATM 2305 O O   . HOH   N 6 .  ? -5.848  -12.811 6.725   1.00 39.05  ? 264 HOH   A O   1 
HETATM 2306 O O   . HOH   N 6 .  ? -8.185  -19.363 -3.285  1.00 48.83  ? 265 HOH   A O   1 
HETATM 2307 O O   . HOH   N 6 .  ? -6.101  -11.798 -11.343 1.00 42.19  ? 266 HOH   A O   1 
HETATM 2308 O O   . HOH   N 6 .  ? 5.353   -7.685  4.029   1.00 33.96  ? 267 HOH   A O   1 
HETATM 2309 O O   . HOH   N 6 .  ? 15.309  -13.446 10.452  1.00 46.97  ? 268 HOH   A O   1 
HETATM 2310 O O   . HOH   N 6 .  ? -4.060  -25.979 -5.656  1.00 38.57  ? 269 HOH   A O   1 
HETATM 2311 O O   . HOH   N 6 .  ? -8.433  -21.224 -1.258  1.00 40.01  ? 270 HOH   A O   1 
HETATM 2312 O O   . HOH   N 6 .  ? 9.946   -20.318 -18.558 1.00 43.01  ? 271 HOH   A O   1 
HETATM 2313 O O   . HOH   N 6 .  ? 11.275  -7.879  0.355   1.00 26.79  ? 272 HOH   A O   1 
HETATM 2314 O O   . HOH   N 6 .  ? -3.752  -7.758  10.538  1.00 45.27  ? 273 HOH   A O   1 
HETATM 2315 O O   . HOH   N 6 .  ? -7.061  -11.547 -7.962  1.00 27.57  ? 274 HOH   A O   1 
HETATM 2316 O O   . HOH   N 6 .  ? 10.989  -27.775 -7.092  1.00 53.52  ? 275 HOH   A O   1 
HETATM 2317 O O   . HOH   N 6 .  ? 15.562  -28.295 -0.857  1.00 54.84  ? 276 HOH   A O   1 
HETATM 2318 O O   . HOH   N 6 .  ? -5.868  -26.806 3.231   1.00 51.21  ? 277 HOH   A O   1 
HETATM 2319 O O   . HOH   N 6 .  ? 21.640  -16.755 -3.415  1.00 31.13  ? 278 HOH   A O   1 
HETATM 2320 O O   . HOH   N 6 .  ? -10.997 -16.140 -3.762  1.00 56.19  ? 279 HOH   A O   1 
HETATM 2321 O O   . HOH   N 6 .  ? 22.563  -16.648 -0.431  1.00 42.29  ? 280 HOH   A O   1 
HETATM 2322 O O   . HOH   N 6 .  ? 0.874   -29.109 -7.014  1.00 70.02  ? 281 HOH   A O   1 
HETATM 2323 O O   . HOH   N 6 .  ? 9.893   -2.960  -0.363  1.00 61.07  ? 282 HOH   A O   1 
HETATM 2324 O O   . HOH   N 6 .  ? -5.311  -23.648 -6.839  1.00 39.09  ? 283 HOH   A O   1 
HETATM 2325 O O   . HOH   N 6 .  ? 9.014   -9.274  -13.803 1.00 37.24  ? 284 HOH   A O   1 
HETATM 2326 O O   . HOH   N 6 .  ? 13.503  -15.356 -12.238 1.00 55.04  ? 285 HOH   A O   1 
HETATM 2327 O O   . HOH   N 6 .  ? -4.012  -26.697 7.498   1.00 57.48  ? 286 HOH   A O   1 
HETATM 2328 O O   . HOH   N 6 .  ? 8.107   -30.082 -3.690  1.00 54.35  ? 287 HOH   A O   1 
HETATM 2329 O O   . HOH   N 6 .  ? -3.566  -10.997 9.353   1.00 45.93  ? 288 HOH   A O   1 
HETATM 2330 O O   . HOH   N 6 .  ? 0.275   -8.067  -13.088 1.00 46.84  ? 289 HOH   A O   1 
HETATM 2331 O O   . HOH   N 6 .  ? -7.098  -14.091 -9.294  1.00 38.63  ? 290 HOH   A O   1 
HETATM 2332 O O   . HOH   N 6 .  ? 12.229  -21.234 10.660  1.00 41.42  ? 291 HOH   A O   1 
HETATM 2333 O O   . HOH   N 6 .  ? -9.914  -28.521 -1.624  1.00 53.88  ? 292 HOH   A O   1 
HETATM 2334 O O   . HOH   N 6 .  ? 11.650  -1.933  -1.594  1.00 43.55  ? 293 HOH   A O   1 
HETATM 2335 O O   . HOH   N 6 .  ? 4.969   -9.650  -11.344 1.00 43.11  ? 294 HOH   A O   1 
HETATM 2336 O O   . HOH   N 6 .  ? -11.082 -13.632 -2.867  1.00 39.99  ? 295 HOH   A O   1 
HETATM 2337 O O   . HOH   N 6 .  ? 8.310   -8.306  4.570   1.00 36.75  ? 296 HOH   A O   1 
HETATM 2338 O O   . HOH   N 6 .  ? -5.727  -23.115 5.764   1.00 56.73  ? 297 HOH   A O   1 
HETATM 2339 O O   . HOH   N 6 .  ? -6.774  -19.138 8.636   1.00 49.09  ? 298 HOH   A O   1 
HETATM 2340 O O   . HOH   N 6 .  ? -4.748  -21.180 -8.182  1.00 52.18  ? 299 HOH   A O   1 
HETATM 2341 O O   . HOH   N 6 .  ? 4.453   -3.421  1.793   1.00 53.73  ? 300 HOH   A O   1 
HETATM 2342 O O   . HOH   O 6 .  ? 10.147  -11.199 -38.252 1.00 46.32  ? 201 HOH   B O   1 
HETATM 2343 O O   . HOH   O 6 .  ? 30.570  -7.996  -30.107 1.00 49.36  ? 202 HOH   B O   1 
HETATM 2344 O O   . HOH   O 6 .  ? 25.787  -4.529  -33.702 1.00 52.68  ? 203 HOH   B O   1 
HETATM 2345 O O   . HOH   O 6 .  ? 29.896  -12.643 -45.518 1.00 76.59  ? 204 HOH   B O   1 
HETATM 2346 O O   . HOH   O 6 .  ? 30.468  -19.804 -40.421 1.00 36.63  ? 205 HOH   B O   1 
HETATM 2347 O O   . HOH   O 6 .  ? 20.310  -22.060 -23.529 1.00 48.74  ? 206 HOH   B O   1 
HETATM 2348 O O   . HOH   O 6 .  ? 26.257  -23.001 -31.291 1.00 36.46  ? 207 HOH   B O   1 
HETATM 2349 O O   . HOH   O 6 .  ? 6.755   -12.113 -26.269 1.00 35.92  ? 208 HOH   B O   1 
HETATM 2350 O O   . HOH   O 6 .  ? 10.346  -19.624 -43.216 1.00 46.81  ? 209 HOH   B O   1 
HETATM 2351 O O   . HOH   O 6 .  ? 20.697  -13.342 -42.930 1.00 36.92  ? 210 HOH   B O   1 
HETATM 2352 O O   . HOH   O 6 .  ? 25.151  -4.985  -29.953 1.00 39.81  ? 211 HOH   B O   1 
HETATM 2353 O O   . HOH   O 6 .  ? 10.318  -16.792 -44.431 1.00 42.54  ? 212 HOH   B O   1 
HETATM 2354 O O   . HOH   O 6 .  ? 13.023  -4.566  -42.043 1.00 42.82  ? 213 HOH   B O   1 
HETATM 2355 O O   . HOH   O 6 .  ? 18.710  -0.065  -25.665 1.00 55.06  ? 214 HOH   B O   1 
HETATM 2356 O O   . HOH   O 6 .  ? 24.519  -1.754  -36.398 1.00 48.08  ? 215 HOH   B O   1 
HETATM 2357 O O   . HOH   O 6 .  ? 3.380   -8.795  -27.232 1.00 54.81  ? 216 HOH   B O   1 
HETATM 2358 O O   . HOH   O 6 .  ? 25.429  -6.001  -35.976 1.00 44.03  ? 217 HOH   B O   1 
HETATM 2359 O O   . HOH   O 6 .  ? 6.047   -7.315  -32.238 1.00 52.57  ? 218 HOH   B O   1 
HETATM 2360 O O   . HOH   O 6 .  ? 21.150  -25.216 -29.809 1.00 63.35  ? 219 HOH   B O   1 
HETATM 2361 O O   . HOH   O 6 .  ? 23.577  -2.257  -29.279 1.00 42.13  ? 220 HOH   B O   1 
HETATM 2362 O O   . HOH   O 6 .  ? 16.848  -19.220 -28.951 1.00 25.82  ? 221 HOH   B O   1 
HETATM 2363 O O   . HOH   O 6 .  ? 21.464  3.630   -32.732 1.00 40.45  ? 222 HOH   B O   1 
HETATM 2364 O O   . HOH   O 6 .  ? 27.918  -17.546 -25.175 1.00 46.23  ? 223 HOH   B O   1 
HETATM 2365 O O   . HOH   O 6 .  ? 8.888   -8.616  -16.551 1.00 43.59  ? 224 HOH   B O   1 
HETATM 2366 O O   . HOH   O 6 .  ? 8.326   -27.899 -38.562 1.00 63.44  ? 225 HOH   B O   1 
HETATM 2367 O O   . HOH   O 6 .  ? 27.929  -8.295  -28.848 1.00 44.89  ? 226 HOH   B O   1 
HETATM 2368 O O   . HOH   O 6 .  ? 10.855  -21.867 -32.783 1.00 36.06  ? 227 HOH   B O   1 
HETATM 2369 O O   . HOH   O 6 .  ? 17.725  -19.801 -42.214 1.00 46.95  ? 228 HOH   B O   1 
HETATM 2370 O O   . HOH   O 6 .  ? 10.621  -18.865 -33.140 1.00 29.66  ? 229 HOH   B O   1 
HETATM 2371 O O   . HOH   O 6 .  ? 18.168  -0.520  -38.632 1.00 29.42  ? 230 HOH   B O   1 
HETATM 2372 O O   . HOH   O 6 .  ? 23.745  -11.153 -22.042 1.00 39.77  ? 231 HOH   B O   1 
HETATM 2373 O O   . HOH   O 6 .  ? 34.622  -23.351 -30.096 1.00 58.40  ? 232 HOH   B O   1 
HETATM 2374 O O   . HOH   O 6 .  ? 31.996  -21.264 -38.215 1.00 41.97  ? 233 HOH   B O   1 
HETATM 2375 O O   . HOH   O 6 .  ? 13.412  -22.364 -20.761 1.00 48.91  ? 234 HOH   B O   1 
HETATM 2376 O O   . HOH   O 6 .  ? 22.789  -23.186 -28.900 1.00 40.66  ? 235 HOH   B O   1 
HETATM 2377 O O   . HOH   O 6 .  ? 23.810  -4.125  -36.970 1.00 31.29  ? 236 HOH   B O   1 
HETATM 2378 O O   . HOH   O 6 .  ? 7.235   -19.101 -35.102 1.00 47.04  ? 237 HOH   B O   1 
HETATM 2379 O O   . HOH   O 6 .  ? 14.338  -6.378  -41.299 1.00 38.26  ? 238 HOH   B O   1 
HETATM 2380 O O   . HOH   O 6 .  ? 18.394  -25.911 -29.003 1.00 40.17  ? 239 HOH   B O   1 
HETATM 2381 O O   . HOH   O 6 .  ? 19.853  -25.606 -34.267 1.00 41.47  ? 240 HOH   B O   1 
HETATM 2382 O O   . HOH   O 6 .  ? 7.592   -18.242 -31.868 1.00 41.34  ? 241 HOH   B O   1 
HETATM 2383 O O   . HOH   O 6 .  ? 22.226  -3.743  -24.337 1.00 58.03  ? 242 HOH   B O   1 
HETATM 2384 O O   . HOH   O 6 .  ? 17.826  -3.670  -22.182 1.00 55.73  ? 243 HOH   B O   1 
HETATM 2385 O O   . HOH   O 6 .  ? 20.352  -10.156 -43.156 1.00 38.56  ? 244 HOH   B O   1 
HETATM 2386 O O   . HOH   O 6 .  ? 8.277   -23.582 -24.468 1.00 60.15  ? 245 HOH   B O   1 
HETATM 2387 O O   . HOH   O 6 .  ? 27.505  -10.700 -28.820 1.00 53.28  ? 246 HOH   B O   1 
HETATM 2388 O O   . HOH   O 6 .  ? 7.764   -7.992  -20.861 1.00 49.30  ? 247 HOH   B O   1 
HETATM 2389 O O   . HOH   O 6 .  ? 32.735  -18.919 -42.485 1.00 43.80  ? 248 HOH   B O   1 
HETATM 2390 O O   . HOH   O 6 .  ? 27.871  -24.814 -35.197 1.00 37.40  ? 249 HOH   B O   1 
HETATM 2391 O O   . HOH   O 6 .  ? 18.080  -15.983 -45.948 1.00 44.71  ? 250 HOH   B O   1 
HETATM 2392 O O   . HOH   O 6 .  ? 14.841  -24.533 -40.506 1.00 41.95  ? 251 HOH   B O   1 
HETATM 2393 O O   . HOH   O 6 .  ? 1.792   -13.051 -28.480 1.00 47.75  ? 252 HOH   B O   1 
HETATM 2394 O O   . HOH   O 6 .  ? 21.011  -6.384  -42.768 1.00 36.49  ? 253 HOH   B O   1 
HETATM 2395 O O   . HOH   O 6 .  ? 26.273  -0.293  -29.487 1.00 52.19  ? 254 HOH   B O   1 
HETATM 2396 O O   . HOH   O 6 .  ? 6.695   -20.624 -25.072 1.00 42.75  ? 255 HOH   B O   1 
HETATM 2397 O O   . HOH   O 6 .  ? 7.564   -12.357 -39.181 1.00 46.37  ? 256 HOH   B O   1 
HETATM 2398 O O   . HOH   O 6 .  ? 17.065  -9.550  -44.170 1.00 46.12  ? 257 HOH   B O   1 
HETATM 2399 O O   . HOH   O 6 .  ? 18.404  4.651   -34.439 1.00 37.39  ? 258 HOH   B O   1 
HETATM 2400 O O   . HOH   O 6 .  ? 24.852  -6.503  -42.890 1.00 49.35  ? 259 HOH   B O   1 
HETATM 2401 O O   . HOH   O 6 .  ? 39.380  -13.066 -39.298 1.00 59.02  ? 260 HOH   B O   1 
HETATM 2402 O O   . HOH   O 6 .  ? 17.519  -25.212 -21.169 1.00 65.33  ? 261 HOH   B O   1 
HETATM 2403 O O   . HOH   O 6 .  ? 20.362  3.937   -33.262 1.00 42.51  ? 262 HOH   B O   1 
HETATM 2404 O O   . HOH   O 6 .  ? 31.691  -12.116 -38.118 1.00 65.26  ? 263 HOH   B O   1 
HETATM 2405 O O   . HOH   O 6 .  ? 9.625   -6.180  -41.131 1.00 48.45  ? 264 HOH   B O   1 
HETATM 2406 O O   . HOH   O 6 .  ? 13.147  -20.222 -19.620 1.00 57.47  ? 265 HOH   B O   1 
HETATM 2407 O O   . HOH   O 6 .  ? 15.044  -8.001  -43.257 1.00 41.91  ? 266 HOH   B O   1 
HETATM 2408 O O   . HOH   O 6 .  ? 11.544  -24.142 -29.966 1.00 46.13  ? 267 HOH   B O   1 
HETATM 2409 O O   . HOH   O 6 .  ? 15.033  -21.772 -42.143 1.00 49.77  ? 268 HOH   B O   1 
HETATM 2410 O O   . HOH   O 6 .  ? 7.557   -9.970  -18.598 1.00 42.07  ? 269 HOH   B O   1 
HETATM 2411 O O   . HOH   O 6 .  ? 22.789  -29.339 -35.713 1.00 41.40  ? 270 HOH   B O   1 
HETATM 2412 O O   . HOH   P 6 .  ? 20.282  -20.065 29.911  1.00 57.89  ? 201 HOH   C O   1 
HETATM 2413 O O   . HOH   P 6 .  ? 26.847  -39.146 12.635  1.00 39.94  ? 202 HOH   C O   1 
HETATM 2414 O O   . HOH   P 6 .  ? 27.009  -37.911 10.151  1.00 41.95  ? 203 HOH   C O   1 
HETATM 2415 O O   . HOH   P 6 .  ? 9.009   -37.024 18.174  1.00 56.63  ? 204 HOH   C O   1 
HETATM 2416 O O   . HOH   P 6 .  ? 17.658  -17.251 15.030  1.00 42.52  ? 205 HOH   C O   1 
HETATM 2417 O O   . HOH   P 6 .  ? 31.969  -33.393 25.867  1.00 47.42  ? 206 HOH   C O   1 
HETATM 2418 O O   . HOH   P 6 .  ? 19.452  -20.271 10.600  1.00 36.43  ? 207 HOH   C O   1 
HETATM 2419 O O   . HOH   P 6 .  ? 30.549  -40.452 9.508   1.00 36.94  ? 208 HOH   C O   1 
HETATM 2420 O O   . HOH   P 6 .  ? 28.317  -15.186 12.814  1.00 59.33  ? 209 HOH   C O   1 
HETATM 2421 O O   . HOH   P 6 .  ? 13.051  -31.618 8.264   1.00 31.00  ? 210 HOH   C O   1 
HETATM 2422 O O   . HOH   P 6 .  ? 25.840  -19.621 6.435   1.00 37.46  ? 211 HOH   C O   1 
HETATM 2423 O O   . HOH   P 6 .  ? 33.416  -24.603 31.768  1.00 52.01  ? 212 HOH   C O   1 
HETATM 2424 O O   . HOH   P 6 .  ? 9.301   -18.968 23.683  1.00 52.26  ? 213 HOH   C O   1 
HETATM 2425 O O   . HOH   P 6 .  ? 23.301  -41.728 18.498  1.00 41.72  ? 214 HOH   C O   1 
HETATM 2426 O O   . HOH   P 6 .  ? 20.231  -42.048 12.146  1.00 27.81  ? 215 HOH   C O   1 
HETATM 2427 O O   . HOH   P 6 .  ? 5.991   -26.531 16.972  1.00 53.04  ? 216 HOH   C O   1 
HETATM 2428 O O   . HOH   P 6 .  ? 25.657  -34.044 34.851  1.00 49.22  ? 217 HOH   C O   1 
HETATM 2429 O O   . HOH   P 6 .  ? 12.033  -29.007 27.913  1.00 58.58  ? 218 HOH   C O   1 
HETATM 2430 O O   . HOH   P 6 .  ? 28.031  -37.684 25.048  1.00 51.61  ? 219 HOH   C O   1 
HETATM 2431 O O   . HOH   P 6 .  ? 8.078   -31.702 12.105  1.00 53.05  ? 220 HOH   C O   1 
HETATM 2432 O O   . HOH   P 6 .  ? 19.901  -26.767 3.542   1.00 54.08  ? 221 HOH   C O   1 
HETATM 2433 O O   . HOH   P 6 .  ? 28.322  -37.402 15.916  1.00 43.02  ? 222 HOH   C O   1 
HETATM 2434 O O   . HOH   P 6 .  ? 30.617  -31.322 15.676  1.00 44.88  ? 223 HOH   C O   1 
HETATM 2435 O O   . HOH   P 6 .  ? 23.703  -18.667 21.730  1.00 57.19  ? 224 HOH   C O   1 
HETATM 2436 O O   . HOH   P 6 .  ? 15.419  -21.216 12.277  1.00 37.88  ? 225 HOH   C O   1 
HETATM 2437 O O   . HOH   P 6 .  ? 15.984  -17.761 19.454  1.00 43.47  ? 226 HOH   C O   1 
HETATM 2438 O O   . HOH   P 6 .  ? 14.120  -37.421 13.660  1.00 53.30  ? 227 HOH   C O   1 
HETATM 2439 O O   . HOH   P 6 .  ? 21.033  -29.856 5.016   1.00 52.12  ? 228 HOH   C O   1 
HETATM 2440 O O   . HOH   P 6 .  ? 22.456  -28.631 11.085  1.00 31.54  ? 229 HOH   C O   1 
HETATM 2441 O O   . HOH   P 6 .  ? 22.310  -34.543 16.568  1.00 26.44  ? 230 HOH   C O   1 
HETATM 2442 O O   . HOH   P 6 .  ? 26.045  -18.128 21.022  1.00 62.23  ? 231 HOH   C O   1 
HETATM 2443 O O   . HOH   P 6 .  ? 31.756  -43.443 15.995  1.00 50.78  ? 232 HOH   C O   1 
HETATM 2444 O O   . HOH   P 6 .  ? 7.173   -18.046 10.847  1.00 42.16  ? 233 HOH   C O   1 
HETATM 2445 O O   . HOH   P 6 .  ? 30.050  -40.000 31.396  1.00 39.07  ? 234 HOH   C O   1 
HETATM 2446 O O   . HOH   P 6 .  ? 25.482  -31.543 10.754  1.00 36.96  ? 235 HOH   C O   1 
HETATM 2447 O O   . HOH   P 6 .  ? 20.937  -40.171 26.438  1.00 38.28  ? 236 HOH   C O   1 
HETATM 2448 O O   . HOH   P 6 .  ? 21.176  -28.866 8.480   1.00 35.19  ? 237 HOH   C O   1 
HETATM 2449 O O   . HOH   P 6 .  ? 31.652  -40.078 27.131  1.00 45.48  ? 238 HOH   C O   1 
HETATM 2450 O O   . HOH   P 6 .  ? 26.056  -17.600 13.870  1.00 43.64  ? 239 HOH   C O   1 
HETATM 2451 O O   . HOH   P 6 .  ? 25.918  -39.823 20.176  1.00 38.38  ? 240 HOH   C O   1 
HETATM 2452 O O   . HOH   P 6 .  ? 13.029  -38.908 24.069  1.00 49.82  ? 241 HOH   C O   1 
HETATM 2453 O O   . HOH   P 6 .  ? 30.606  -35.809 28.848  1.00 59.54  ? 242 HOH   C O   1 
HETATM 2454 O O   . HOH   P 6 .  ? 30.737  -17.462 9.655   1.00 42.14  ? 243 HOH   C O   1 
HETATM 2455 O O   . HOH   P 6 .  ? 14.028  -38.949 9.161   1.00 64.15  ? 244 HOH   C O   1 
HETATM 2456 O O   . HOH   P 6 .  ? 20.368  -19.139 24.940  1.00 55.02  ? 245 HOH   C O   1 
HETATM 2457 O O   . HOH   P 6 .  ? 2.806   -28.413 14.617  1.00 55.77  ? 246 HOH   C O   1 
HETATM 2458 O O   . HOH   P 6 .  ? 16.426  -38.421 11.816  1.00 47.40  ? 247 HOH   C O   1 
HETATM 2459 O O   . HOH   P 6 .  ? 30.521  -32.815 18.214  1.00 47.00  ? 248 HOH   C O   1 
HETATM 2460 O O   . HOH   P 6 .  ? 20.564  -41.345 39.707  1.00 69.11  ? 249 HOH   C O   1 
HETATM 2461 O O   . HOH   P 6 .  ? 32.174  -43.601 11.805  1.00 48.73  ? 250 HOH   C O   1 
HETATM 2462 O O   . HOH   P 6 .  ? 29.811  -25.482 32.666  1.00 58.85  ? 251 HOH   C O   1 
HETATM 2463 O O   . HOH   P 6 .  ? 17.405  -36.610 29.292  1.00 51.59  ? 252 HOH   C O   1 
HETATM 2464 O O   . HOH   P 6 .  ? 29.471  -41.921 27.306  1.00 42.59  ? 253 HOH   C O   1 
HETATM 2465 O O   . HOH   P 6 .  ? 13.832  -23.043 27.860  1.00 61.43  ? 254 HOH   C O   1 
HETATM 2466 O O   . HOH   P 6 .  ? 26.081  -13.983 11.164  1.00 48.51  ? 255 HOH   C O   1 
HETATM 2467 O O   . HOH   P 6 .  ? 23.003  -14.039 13.645  1.00 49.29  ? 256 HOH   C O   1 
HETATM 2468 O O   . HOH   P 6 .  ? 9.132   -35.678 14.366  1.00 50.79  ? 257 HOH   C O   1 
HETATM 2469 O O   . HOH   P 6 .  ? 37.247  -24.386 26.796  1.00 65.57  ? 258 HOH   C O   1 
HETATM 2470 O O   . HOH   P 6 .  ? 28.475  -41.896 29.827  1.00 41.35  ? 259 HOH   C O   1 
HETATM 2471 O O   . HOH   P 6 .  ? 33.729  -44.731 15.369  1.00 36.83  ? 260 HOH   C O   1 
HETATM 2472 O O   . HOH   P 6 .  ? 29.368  -40.804 19.579  1.00 61.57  ? 261 HOH   C O   1 
HETATM 2473 O O   . HOH   P 6 .  ? 4.288   -24.757 17.871  1.00 62.53  ? 262 HOH   C O   1 
# 
