data_7HH6
# 
_entry.id   7HH6 
# 
_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   7HH6         pdb_00007hh6 10.2210/pdb7hh6/pdb 
WWPDB D_1001407468 ?            ?                   
# 
_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                        7HH6 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '2-[methyl(pyridin-2-yl)amino]ethan-1-ol'          152.194   1   ? ?    ? ? 
5 water       nat water                                              18.015    263 ? ?    ? ? 
# 
_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 '2-[methyl(pyridin-2-yl)amino]ethan-1-ol' UUY 
5 water                                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                   ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                  ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                           ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                  ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                            'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                                 ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                           ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                   ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                 ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                     ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                   ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                    ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                             ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                   ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                    ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                             ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                 ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                  ?                 'C9 H11 N O3'    181.189 
UUY non-polymer         . '2-[methyl(pyridin-2-yl)amino]ethan-1-ol' ?                 'C8 H12 N2 O'    152.194 
VAL 'L-peptide linking' y VALINE                                    ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 ?  ?   ?   B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 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        UUY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UUY 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 2 SO4 1   104 4   SO4 SO4 A . 
H 2 SO4 1   101 1   SO4 SO4 B . 
I 2 SO4 1   102 3   SO4 SO4 B . 
J 4 UUY 1   103 101 UUY LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 307 HOH HOH A . 
M 5 HOH 2   202 84  HOH HOH A . 
M 5 HOH 3   203 345 HOH HOH A . 
M 5 HOH 4   204 202 HOH HOH A . 
M 5 HOH 5   205 66  HOH HOH A . 
M 5 HOH 6   206 360 HOH HOH A . 
M 5 HOH 7   207 293 HOH HOH A . 
M 5 HOH 8   208 304 HOH HOH A . 
M 5 HOH 9   209 94  HOH HOH A . 
M 5 HOH 10  210 363 HOH HOH A . 
M 5 HOH 11  211 87  HOH HOH A . 
M 5 HOH 12  212 364 HOH HOH A . 
M 5 HOH 13  213 289 HOH HOH A . 
M 5 HOH 14  214 37  HOH HOH A . 
M 5 HOH 15  215 55  HOH HOH A . 
M 5 HOH 16  216 139 HOH HOH A . 
M 5 HOH 17  217 28  HOH HOH A . 
M 5 HOH 18  218 91  HOH HOH A . 
M 5 HOH 19  219 38  HOH HOH A . 
M 5 HOH 20  220 188 HOH HOH A . 
M 5 HOH 21  221 179 HOH HOH A . 
M 5 HOH 22  222 95  HOH HOH A . 
M 5 HOH 23  223 199 HOH HOH A . 
M 5 HOH 24  224 71  HOH HOH A . 
M 5 HOH 25  225 259 HOH HOH A . 
M 5 HOH 26  226 292 HOH HOH A . 
M 5 HOH 27  227 116 HOH HOH A . 
M 5 HOH 28  228 352 HOH HOH A . 
M 5 HOH 29  229 86  HOH HOH A . 
M 5 HOH 30  230 290 HOH HOH A . 
M 5 HOH 31  231 340 HOH HOH A . 
M 5 HOH 32  232 111 HOH HOH A . 
M 5 HOH 33  233 32  HOH HOH A . 
M 5 HOH 34  234 347 HOH HOH A . 
M 5 HOH 35  235 26  HOH HOH A . 
M 5 HOH 36  236 7   HOH HOH A . 
M 5 HOH 37  237 337 HOH HOH A . 
M 5 HOH 38  238 8   HOH HOH A . 
M 5 HOH 39  239 167 HOH HOH A . 
M 5 HOH 40  240 34  HOH HOH A . 
M 5 HOH 41  241 12  HOH HOH A . 
M 5 HOH 42  242 85  HOH HOH A . 
M 5 HOH 43  243 99  HOH HOH A . 
M 5 HOH 44  244 41  HOH HOH A . 
M 5 HOH 45  245 260 HOH HOH A . 
M 5 HOH 46  246 165 HOH HOH A . 
M 5 HOH 47  247 274 HOH HOH A . 
M 5 HOH 48  248 362 HOH HOH A . 
M 5 HOH 49  249 23  HOH HOH A . 
M 5 HOH 50  250 278 HOH HOH A . 
M 5 HOH 51  251 97  HOH HOH A . 
M 5 HOH 52  252 60  HOH HOH A . 
M 5 HOH 53  253 190 HOH HOH A . 
M 5 HOH 54  254 42  HOH HOH A . 
M 5 HOH 55  255 203 HOH HOH A . 
M 5 HOH 56  256 1   HOH HOH A . 
M 5 HOH 57  257 2   HOH HOH A . 
M 5 HOH 58  258 27  HOH HOH A . 
M 5 HOH 59  259 77  HOH HOH A . 
M 5 HOH 60  260 351 HOH HOH A . 
M 5 HOH 61  261 145 HOH HOH A . 
M 5 HOH 62  262 267 HOH HOH A . 
M 5 HOH 63  263 20  HOH HOH A . 
M 5 HOH 64  264 58  HOH HOH A . 
M 5 HOH 65  265 18  HOH HOH A . 
M 5 HOH 66  266 78  HOH HOH A . 
M 5 HOH 67  267 47  HOH HOH A . 
M 5 HOH 68  268 288 HOH HOH A . 
M 5 HOH 69  269 109 HOH HOH A . 
M 5 HOH 70  270 164 HOH HOH A . 
M 5 HOH 71  271 21  HOH HOH A . 
M 5 HOH 72  272 93  HOH HOH A . 
M 5 HOH 73  273 14  HOH HOH A . 
M 5 HOH 74  274 287 HOH HOH A . 
M 5 HOH 75  275 301 HOH HOH A . 
M 5 HOH 76  276 152 HOH HOH A . 
M 5 HOH 77  277 19  HOH HOH A . 
M 5 HOH 78  278 222 HOH HOH A . 
M 5 HOH 79  279 281 HOH HOH A . 
M 5 HOH 80  280 327 HOH HOH A . 
M 5 HOH 81  281 300 HOH HOH A . 
M 5 HOH 82  282 64  HOH HOH A . 
M 5 HOH 83  283 143 HOH HOH A . 
M 5 HOH 84  284 9   HOH HOH A . 
M 5 HOH 85  285 113 HOH HOH A . 
M 5 HOH 86  286 115 HOH HOH A . 
M 5 HOH 87  287 218 HOH HOH A . 
M 5 HOH 88  288 73  HOH HOH A . 
M 5 HOH 89  289 208 HOH HOH A . 
M 5 HOH 90  290 16  HOH HOH A . 
M 5 HOH 91  291 343 HOH HOH A . 
M 5 HOH 92  292 31  HOH HOH A . 
M 5 HOH 93  293 63  HOH HOH A . 
M 5 HOH 94  294 185 HOH HOH A . 
M 5 HOH 95  295 318 HOH HOH A . 
M 5 HOH 96  296 22  HOH HOH A . 
M 5 HOH 97  297 210 HOH HOH A . 
M 5 HOH 98  298 296 HOH HOH A . 
M 5 HOH 99  299 83  HOH HOH A . 
M 5 HOH 100 300 270 HOH HOH A . 
M 5 HOH 101 301 211 HOH HOH A . 
M 5 HOH 102 302 349 HOH HOH A . 
M 5 HOH 103 303 35  HOH HOH A . 
M 5 HOH 104 304 338 HOH HOH A . 
M 5 HOH 105 305 219 HOH HOH A . 
M 5 HOH 106 306 75  HOH HOH A . 
M 5 HOH 107 307 156 HOH HOH A . 
M 5 HOH 108 308 205 HOH HOH A . 
M 5 HOH 109 309 283 HOH HOH A . 
M 5 HOH 110 310 57  HOH HOH A . 
M 5 HOH 111 311 313 HOH HOH A . 
M 5 HOH 112 312 125 HOH HOH A . 
M 5 HOH 113 313 332 HOH HOH A . 
N 5 HOH 1   201 329 HOH HOH B . 
N 5 HOH 2   202 123 HOH HOH B . 
N 5 HOH 3   203 272 HOH HOH B . 
N 5 HOH 4   204 89  HOH HOH B . 
N 5 HOH 5   205 247 HOH HOH B . 
N 5 HOH 6   206 331 HOH HOH B . 
N 5 HOH 7   207 157 HOH HOH B . 
N 5 HOH 8   208 184 HOH HOH B . 
N 5 HOH 9   209 98  HOH HOH B . 
N 5 HOH 10  210 69  HOH HOH B . 
N 5 HOH 11  211 249 HOH HOH B . 
N 5 HOH 12  212 333 HOH HOH B . 
N 5 HOH 13  213 153 HOH HOH B . 
N 5 HOH 14  214 258 HOH HOH B . 
N 5 HOH 15  215 17  HOH HOH B . 
N 5 HOH 16  216 334 HOH HOH B . 
N 5 HOH 17  217 346 HOH HOH B . 
N 5 HOH 18  218 137 HOH HOH B . 
N 5 HOH 19  219 150 HOH HOH B . 
N 5 HOH 20  220 101 HOH HOH B . 
N 5 HOH 21  221 215 HOH HOH B . 
N 5 HOH 22  222 54  HOH HOH B . 
N 5 HOH 23  223 6   HOH HOH B . 
N 5 HOH 24  224 117 HOH HOH B . 
N 5 HOH 25  225 242 HOH HOH B . 
N 5 HOH 26  226 339 HOH HOH B . 
N 5 HOH 27  227 5   HOH HOH B . 
N 5 HOH 28  228 119 HOH HOH B . 
N 5 HOH 29  229 168 HOH HOH B . 
N 5 HOH 30  230 96  HOH HOH B . 
N 5 HOH 31  231 172 HOH HOH B . 
N 5 HOH 32  232 170 HOH HOH B . 
N 5 HOH 33  233 280 HOH HOH B . 
N 5 HOH 34  234 224 HOH HOH B . 
N 5 HOH 35  235 10  HOH HOH B . 
N 5 HOH 36  236 68  HOH HOH B . 
N 5 HOH 37  237 320 HOH HOH B . 
N 5 HOH 38  238 223 HOH HOH B . 
N 5 HOH 39  239 76  HOH HOH B . 
N 5 HOH 40  240 74  HOH HOH B . 
N 5 HOH 41  241 261 HOH HOH B . 
N 5 HOH 42  242 361 HOH HOH B . 
N 5 HOH 43  243 315 HOH HOH B . 
N 5 HOH 44  244 13  HOH HOH B . 
N 5 HOH 45  245 59  HOH HOH B . 
N 5 HOH 46  246 175 HOH HOH B . 
N 5 HOH 47  247 217 HOH HOH B . 
N 5 HOH 48  248 61  HOH HOH B . 
N 5 HOH 49  249 79  HOH HOH B . 
N 5 HOH 50  250 169 HOH HOH B . 
N 5 HOH 51  251 24  HOH HOH B . 
N 5 HOH 52  252 182 HOH HOH B . 
N 5 HOH 53  253 25  HOH HOH B . 
N 5 HOH 54  254 36  HOH HOH B . 
N 5 HOH 55  255 197 HOH HOH B . 
N 5 HOH 56  256 46  HOH HOH B . 
N 5 HOH 57  257 303 HOH HOH B . 
N 5 HOH 58  258 104 HOH HOH B . 
N 5 HOH 59  259 72  HOH HOH B . 
N 5 HOH 60  260 214 HOH HOH B . 
N 5 HOH 61  261 177 HOH HOH B . 
N 5 HOH 62  262 319 HOH HOH B . 
N 5 HOH 63  263 335 HOH HOH B . 
N 5 HOH 64  264 120 HOH HOH B . 
N 5 HOH 65  265 44  HOH HOH B . 
N 5 HOH 66  266 279 HOH HOH B . 
N 5 HOH 67  267 163 HOH HOH B . 
N 5 HOH 68  268 291 HOH HOH B . 
N 5 HOH 69  269 322 HOH HOH B . 
N 5 HOH 70  270 201 HOH HOH B . 
N 5 HOH 71  271 316 HOH HOH B . 
N 5 HOH 72  272 314 HOH HOH B . 
N 5 HOH 73  273 160 HOH HOH B . 
N 5 HOH 74  274 103 HOH HOH B . 
N 5 HOH 75  275 341 HOH HOH B . 
N 5 HOH 76  276 357 HOH HOH B . 
N 5 HOH 77  277 348 HOH HOH B . 
N 5 HOH 78  278 107 HOH HOH B . 
N 5 HOH 79  279 312 HOH HOH B . 
N 5 HOH 80  280 355 HOH HOH B . 
O 5 HOH 1   201 336 HOH HOH C . 
O 5 HOH 2   202 323 HOH HOH C . 
O 5 HOH 3   203 254 HOH HOH C . 
O 5 HOH 4   204 302 HOH HOH C . 
O 5 HOH 5   205 321 HOH HOH C . 
O 5 HOH 6   206 271 HOH HOH C . 
O 5 HOH 7   207 359 HOH HOH C . 
O 5 HOH 8   208 317 HOH HOH C . 
O 5 HOH 9   209 309 HOH HOH C . 
O 5 HOH 10  210 226 HOH HOH C . 
O 5 HOH 11  211 126 HOH HOH C . 
O 5 HOH 12  212 269 HOH HOH C . 
O 5 HOH 13  213 132 HOH HOH C . 
O 5 HOH 14  214 118 HOH HOH C . 
O 5 HOH 15  215 134 HOH HOH C . 
O 5 HOH 16  216 173 HOH HOH C . 
O 5 HOH 17  217 161 HOH HOH C . 
O 5 HOH 18  218 325 HOH HOH C . 
O 5 HOH 19  219 142 HOH HOH C . 
O 5 HOH 20  220 82  HOH HOH C . 
O 5 HOH 21  221 15  HOH HOH C . 
O 5 HOH 22  222 49  HOH HOH C . 
O 5 HOH 23  223 40  HOH HOH C . 
O 5 HOH 24  224 353 HOH HOH C . 
O 5 HOH 25  225 90  HOH HOH C . 
O 5 HOH 26  226 189 HOH HOH C . 
O 5 HOH 27  227 275 HOH HOH C . 
O 5 HOH 28  228 354 HOH HOH C . 
O 5 HOH 29  229 209 HOH HOH C . 
O 5 HOH 30  230 48  HOH HOH C . 
O 5 HOH 31  231 45  HOH HOH C . 
O 5 HOH 32  232 122 HOH HOH C . 
O 5 HOH 33  233 4   HOH HOH C . 
O 5 HOH 34  234 43  HOH HOH C . 
O 5 HOH 35  235 102 HOH HOH C . 
O 5 HOH 36  236 358 HOH HOH C . 
O 5 HOH 37  237 198 HOH HOH C . 
O 5 HOH 38  238 62  HOH HOH C . 
O 5 HOH 39  239 326 HOH HOH C . 
O 5 HOH 40  240 148 HOH HOH C . 
O 5 HOH 41  241 299 HOH HOH C . 
O 5 HOH 42  242 294 HOH HOH C . 
O 5 HOH 43  243 284 HOH HOH C . 
O 5 HOH 44  244 56  HOH HOH C . 
O 5 HOH 45  245 53  HOH HOH C . 
O 5 HOH 46  246 135 HOH HOH C . 
O 5 HOH 47  247 350 HOH HOH C . 
O 5 HOH 48  248 67  HOH HOH C . 
O 5 HOH 49  249 328 HOH HOH C . 
O 5 HOH 50  250 149 HOH HOH C . 
O 5 HOH 51  251 298 HOH HOH C . 
O 5 HOH 52  252 295 HOH HOH C . 
O 5 HOH 53  253 130 HOH HOH C . 
O 5 HOH 54  254 171 HOH HOH C . 
O 5 HOH 55  255 151 HOH HOH C . 
O 5 HOH 56  256 65  HOH HOH C . 
O 5 HOH 57  257 305 HOH HOH C . 
O 5 HOH 58  258 241 HOH HOH C . 
O 5 HOH 59  259 146 HOH HOH C . 
O 5 HOH 60  260 131 HOH HOH C . 
O 5 HOH 61  261 70  HOH HOH C . 
O 5 HOH 62  262 356 HOH HOH C . 
O 5 HOH 63  263 108 HOH HOH C . 
O 5 HOH 64  264 324 HOH HOH C . 
O 5 HOH 65  265 330 HOH HOH C . 
O 5 HOH 66  266 310 HOH HOH C . 
O 5 HOH 67  267 246 HOH HOH C . 
O 5 HOH 68  268 344 HOH HOH C . 
O 5 HOH 69  269 92  HOH HOH C . 
O 5 HOH 70  270 206 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
2  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
3  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
8  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
9  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
17 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
18 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
19 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
20 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
21 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
22 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
23 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
24 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
25 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
26 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
27 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
28 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
29 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
30 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
31 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
32 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
33 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
34 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
35 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
36 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
37 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
38 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
39 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
40 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
41 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
42 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
43 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
44 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
45 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
46 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
47 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
48 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
49 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
50 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
51 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
52 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
53 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HH6 
_cell.length_a           41.700 
_cell.length_b           42.180 
_cell.length_c           159.110 
_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                         7HH6 
_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          7HH6 
_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                     7HH6 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.04 
_reflns.d_resolution_high            1.71 
_reflns.number_obs                   31342 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.094 
_reflns.pdbx_netI_over_sigmaI        9.6 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.103 
_reflns.pdbx_Rpim_I_all              0.041 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     198200 
_reflns.pdbx_chi_squared             0.99 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.71 
_reflns_shell.d_res_low                   1.75 
_reflns_shell.number_measured_all         14818 
_reflns_shell.number_unique_obs           2298 
_reflns_shell.Rmerge_I_obs                2.024 
_reflns_shell.pdbx_chi_squared            0.78 
_reflns_shell.pdbx_redundancy             6.4 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             2.203 
_reflns_shell.pdbx_Rpim_I_all             0.862 
_reflns_shell.pdbx_CC_half                0.323 
_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                                 7HH6 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29625 
_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                             40.80 
_refine.ls_d_res_high                            1.71 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_R_factor_obs                          0.20668 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20440 
_refine.ls_R_factor_R_free                       0.24704 
_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                  1650 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               38.686 
_refine.aniso_B[1][1]                            0.07 
_refine.aniso_B[2][2]                            0.17 
_refine.aniso_B[3][3]                            -0.25 
_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                       0.126 
_refine.pdbx_overall_ESU_R_Free                  0.124 
_refine.overall_SU_ML                            0.109 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.531 
_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        2139 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             263 
_refine_hist.number_atoms_total               2451 
_refine_hist.d_res_high                       1.71 
_refine_hist.d_res_low                        40.80 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.009  0.012  ? 2282 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.734  1.836  ? 3102 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.058  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       3.430  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.001 10.000 ? 301  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.128  0.200  ? 285  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1888 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.454  3.601  ? 1069 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.723  6.430  ? 1328 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.805  3.944  ? 1213 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.343  53.44  ? 3560 '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                       1.710 
_refine_ls_shell.d_res_low                        1.754 
_refine_ls_shell.number_reflns_R_work             2142 
_refine_ls_shell.R_factor_R_work                  0.339 
_refine_ls_shell.percent_reflns_obs               99.96 
_refine_ls_shell.R_factor_R_free                  0.340 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             149 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH6 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z54633859' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH6 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HH6 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH6 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH6 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 7HH6 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH6 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH6 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH6 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH6 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH6 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HH6 
_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 233 ? ? O B HOH 269 ? ? 1.51 
2 1 O   C HOH 259 ? ? O C HOH 264 ? ? 2.00 
3 1 CE  A LYS 39  ? ? O A HOH 260 ? ? 2.07 
4 1 O2  A SO4 104 ? ? O A HOH 201 ? ? 2.09 
5 1 OD1 C ASP 26  ? ? O C HOH 201 ? ? 2.13 
6 1 O   A HOH 258 ? ? O A HOH 304 ? ? 2.13 
7 1 O   B HOH 209 ? ? O B HOH 277 ? ? 2.15 
8 1 O   A HOH 209 ? ? O A HOH 285 ? ? 2.16 
9 1 O   A HOH 231 ? ? O A HOH 272 ? ? 2.19 
# 
_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     226 
_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    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     278 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_545 
_pdbx_validate_symm_contact.dist              2.17 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              66 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              66 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              66 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                122.42 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            12.02 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -151.40 62.07  
2 1 ASN B 38 ? ? 80.68   -2.97  
3 1 ASN B 87 ? ? -158.71 62.71  
4 1 ASN C 87 ? ? -156.68 50.77  
5 1 SER C 91 ? ? -73.32  -70.03 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.93 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 B VAL 33 ? B VAL 34 
8  1 Y 1 C GLY 0  ? C GLY 1  
9  1 Y 1 C MET 1  ? C MET 2  
10 1 Y 1 C PRO 2  ? C PRO 3  
11 1 Y 1 C ILE 28 ? C ILE 29 
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
UUY N1   N Y N 387 
UUY C4   C Y N 388 
UUY C5   C Y N 389 
UUY C6   C Y N 390 
UUY C7   C Y N 391 
UUY N    N N N 392 
UUY C    C N N 393 
UUY O    O N N 394 
UUY C1   C N N 395 
UUY C2   C N N 396 
UUY C3   C Y N 397 
UUY H1   H N N 398 
UUY H2   H N N 399 
UUY H3   H N N 400 
UUY H4   H N N 401 
UUY H5   H N N 402 
UUY H6   H N N 403 
UUY H7   H N N 404 
UUY H8   H N N 405 
UUY H9   H N N 406 
UUY H10  H N N 407 
UUY H11  H N N 408 
UUY H12  H N N 409 
VAL N    N N N 410 
VAL CA   C N S 411 
VAL C    C N N 412 
VAL O    O N N 413 
VAL CB   C N N 414 
VAL CG1  C N N 415 
VAL CG2  C N N 416 
VAL OXT  O N N 417 
VAL H    H N N 418 
VAL H2   H N N 419 
VAL HA   H N N 420 
VAL HB   H N N 421 
VAL HG11 H N N 422 
VAL HG12 H N N 423 
VAL HG13 H N N 424 
VAL HG21 H N N 425 
VAL HG22 H N N 426 
VAL HG23 H N N 427 
VAL HXT  H N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
UUY O   C2   sing N N 371 
UUY C1  C2   sing N N 372 
UUY C1  N    sing N N 373 
UUY N1  C7   doub Y N 374 
UUY N1  C3   sing Y N 375 
UUY C7  C6   sing Y N 376 
UUY N   C3   sing N N 377 
UUY N   C    sing N N 378 
UUY C3  C4   doub Y N 379 
UUY C6  C5   doub Y N 380 
UUY C4  C5   sing Y N 381 
UUY C4  H1   sing N N 382 
UUY C5  H2   sing N N 383 
UUY C6  H3   sing N N 384 
UUY C7  H4   sing N N 385 
UUY C   H5   sing N N 386 
UUY C   H6   sing N N 387 
UUY C   H7   sing N N 388 
UUY O   H8   sing N N 389 
UUY C1  H9   sing N N 390 
UUY C1  H10  sing N N 391 
UUY C2  H11  sing N N 392 
UUY C2  H12  sing N N 393 
VAL N   CA   sing N N 394 
VAL N   H    sing N N 395 
VAL N   H2   sing N N 396 
VAL CA  C    sing N N 397 
VAL CA  CB   sing N N 398 
VAL CA  HA   sing N N 399 
VAL C   O    doub N N 400 
VAL C   OXT  sing N N 401 
VAL CB  CG1  sing N N 402 
VAL CB  CG2  sing N N 403 
VAL CB  HB   sing N N 404 
VAL CG1 HG11 sing N N 405 
VAL CG1 HG12 sing N N 406 
VAL CG1 HG13 sing N N 407 
VAL CG2 HG21 sing N N 408 
VAL CG2 HG22 sing N N 409 
VAL CG2 HG23 sing N N 410 
VAL OXT HXT  sing N N 411 
# 
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                    7HH6 
_atom_sites.fract_transf_matrix[1][1]   0.023981 
_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]   0.023708 
_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]   0.006285 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 2  ? 0.702   4.357   2.320   1.00 50.66  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.346  3.532   1.659   1.00 58.20  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.279   2.458   0.761   1.00 53.87  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.382   2.618   0.242   1.00 52.20  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.347  4.411   0.901   1.00 63.61  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.267  5.214   1.814   1.00 75.25  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.569  4.335   2.711   1.00 76.71  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -3.874  5.515   4.033   1.00 78.81  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.397  1.296   0.601   1.00 44.23  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.062   0.215   -0.283  1.00 42.94  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.321   0.577   -1.748  1.00 39.95  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.437  1.331   -2.366  1.00 40.25  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.155  -0.788  -0.162  1.00 45.94  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.665  -0.564  1.257   1.00 47.14  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.621  0.942   1.346   1.00 45.09  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.348   -0.041  -2.339  1.00 36.18  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.499   0.048   -3.779  1.00 37.04  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.961   -1.260  -4.359  1.00 36.91  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.537   -2.135  -3.602  1.00 38.80  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.971   0.271   -4.161  1.00 45.27  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.583   1.554   -3.668  1.00 62.24  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.456   2.027   -2.374  1.00 70.68  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.370   2.443   -4.304  1.00 71.78  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.118   3.171   -2.253  1.00 71.55  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.684   3.442   -3.410  1.00 68.20  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 1.005   -1.404  -5.685  1.00 31.26  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.789   -2.706  -6.298  1.00 30.86  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.908   -3.689  -5.953  1.00 30.64  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 3.015   -3.304  -5.549  1.00 28.72  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.603   -2.560  -7.790  1.00 36.47  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.610   -4.974  -6.126  1.00 29.40  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.631   -5.994  -5.961  1.00 31.05  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.797   -5.779  -6.935  1.00 29.71  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.602   -5.419  -8.097  1.00 28.07  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 2.050   -7.406  -6.039  1.00 29.62  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.297   -7.753  -4.759  1.00 30.81  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 2.002   -7.941  -3.555  1.00 28.75  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.108  -7.918  -4.762  1.00 26.24  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.350   -8.245  -2.367  1.00 26.78  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.756  -8.268  -3.570  1.00 24.62  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.062  -8.398  -2.390  1.00 27.46  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 5.014   -6.059  -6.452  1.00 26.35  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.184   -6.042  -7.326  1.00 27.20  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 7.111   -7.224  -6.990  1.00 22.86  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 7.117   -7.761  -5.883  1.00 22.76  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.935   -4.724  -7.097  1.00 27.56  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.515   -4.585  -5.704  1.00 32.25  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.244   -3.254  -5.490  1.00 38.65  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.880   -3.150  -4.120  1.00 39.37  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.865   -3.189  -3.055  1.00 37.86  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.978   -7.634  -7.938  1.00 27.94  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.941   -8.717  -7.692  1.00 28.66  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.723   -8.432  -6.409  1.00 24.54  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.139  -7.296  -6.159  1.00 27.57  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.822   -8.632  -8.999  1.00 26.67  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.866   -8.066  -10.066 1.00 28.62  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.126   -6.994  -9.267  1.00 30.75  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.867   -9.454  -5.552  1.00 23.01  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.621  -9.344  -4.317  1.00 23.68  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.681   -9.214  -3.123  1.00 24.34  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 10.048  -9.519  -1.979  1.00 23.43  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.431   -8.783  -3.383  1.00 18.65  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.499   -8.734  -2.259  1.00 20.70  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.283   -10.119 -1.631  1.00 20.24  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 7.157   -11.115 -2.348  1.00 22.19  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.141   -8.138  -2.646  1.00 23.07  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.153   -6.629  -2.876  1.00 26.06  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.164   -5.968  -2.474  1.00 26.23  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.181   -6.114  -3.471  1.00 24.06  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.169   -10.150 -0.292  1.00 19.48  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.995   -11.399 0.459   1.00 20.26  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.519   -11.516 0.835   1.00 22.23  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.923   -10.512 1.270   1.00 23.42  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.889   -11.453 1.694   1.00 21.85  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.384   -11.258 1.387   1.00 22.54  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.293  -11.403 2.625   1.00 25.36  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.788   -12.266 0.273   1.00 24.06  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.984   -12.728 0.694   1.00 20.57  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.543   -12.920 0.924   1.00 20.75  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.294   -14.285 1.553   1.00 23.86  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 4.179   -15.149 1.630   1.00 21.05  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.708   -12.793 -0.348  1.00 20.69  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.783   -11.375 -0.929  1.00 22.33  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 3.106   -13.879 -1.369  1.00 22.02  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 2.067   -14.461 2.048   1.00 22.62  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.511   -15.786 2.097   1.00 23.86  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.536   -15.853 0.930   1.00 25.45  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.285  -14.937 0.782   1.00 24.75  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.743   -16.161 3.384   1.00 21.80  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.656   -16.299 4.601   1.00 23.47  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 2.010   -15.159 5.327   1.00 27.48  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.148   -17.541 5.012   1.00 26.00  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.896   -15.257 6.399   1.00 34.63  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 3.034   -17.638 6.083   1.00 30.04  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.382   -16.508 6.788   1.00 29.77  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.626   -16.954 0.157   1.00 22.59  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.177  -17.129 -1.051  1.00 24.25  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.154  -18.296 -0.854  1.00 28.88  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.796  -19.359 -0.310  1.00 26.34  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.731   -17.294 -2.289  1.00 22.11  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.420  -18.060 -1.240  1.00 25.82  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.451  -19.067 -1.035  1.00 26.19  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.822  -19.777 -2.348  1.00 29.31  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.161  -19.148 -3.343  1.00 30.69  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.672  -18.409 -0.393  1.00 28.83  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.771  -19.407 0.049   1.00 35.98  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.290  -20.374 1.138   1.00 35.71  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.429  -21.107 1.825   1.00 32.24  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.931  -22.153 0.916   1.00 32.29  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.790  -21.109 -2.302  1.00 29.38  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.262  -22.003 -3.353  1.00 30.01  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.301  -22.924 -2.718  1.00 33.99  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.150  -23.294 -1.559  1.00 29.42  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.138  -22.978 -3.736  1.00 34.63  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.808  -22.340 -4.100  1.00 41.70  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.876  -21.858 -5.835  1.00 38.51  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.384  -23.363 -6.652  1.00 33.34  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.293  -23.351 -3.503  1.00 38.00  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.362  -24.216 -3.019  1.00 40.04  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.751  -25.523 -2.536  1.00 36.92  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.814  -26.042 -3.145  1.00 36.80  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.375  -24.411 -4.155  1.00 48.36  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.694  -25.026 -3.713  1.00 59.49  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.956 -24.627 -4.474  1.00 69.08  ? 16  LYS A CD  1 
ATOM   125  C CE  . LYS A 1 17 ? -12.137 -25.415 -3.959  1.00 77.79  ? 16  LYS A CE  1 
ATOM   126  N NZ  . LYS A 1 17 ? -13.440 -25.018 -4.503  1.00 77.10  ? 16  LYS A NZ  1 
ATOM   127  N N   . GLY A 1 18 ? -7.227  -26.003 -1.379  1.00 38.59  ? 17  GLY A N   1 
ATOM   128  C CA  . GLY A 1 18 ? -6.722  -27.240 -0.808  1.00 36.85  ? 17  GLY A CA  1 
ATOM   129  C C   . GLY A 1 18 ? -5.417  -27.090 -0.027  1.00 42.89  ? 17  GLY A C   1 
ATOM   130  O O   . GLY A 1 18 ? -4.921  -28.074 0.513   1.00 46.27  ? 17  GLY A O   1 
ATOM   131  N N   . TYR A 1 19 ? -4.850  -25.873 0.044   1.00 34.85  ? 18  TYR A N   1 
ATOM   132  C CA  . TYR A 1 19 ? -3.619  -25.727 0.780   1.00 35.55  ? 18  TYR A CA  1 
ATOM   133  C C   . TYR A 1 19 ? -3.730  -24.589 1.770   1.00 32.03  ? 18  TYR A C   1 
ATOM   134  O O   . TYR A 1 19 ? -4.430  -23.617 1.519   1.00 32.42  ? 18  TYR A O   1 
ATOM   135  C CB  . TYR A 1 19 ? -2.532  -25.276 -0.195  1.00 40.95  ? 18  TYR A CB  1 
ATOM   136  C CG  . TYR A 1 19 ? -2.006  -26.332 -1.154  1.00 44.32  ? 18  TYR A CG  1 
ATOM   137  C CD1 . TYR A 1 19 ? -0.869  -27.062 -0.831  1.00 56.46  ? 18  TYR A CD1 1 
ATOM   138  C CD2 . TYR A 1 19 ? -2.588  -26.535 -2.403  1.00 45.00  ? 18  TYR A CD2 1 
ATOM   139  C CE1 . TYR A 1 19 ? -0.342  -27.998 -1.706  1.00 57.42  ? 18  TYR A CE1 1 
ATOM   140  C CE2 . TYR A 1 19 ? -2.066  -27.468 -3.292  1.00 51.69  ? 18  TYR A CE2 1 
ATOM   141  C CZ  . TYR A 1 19 ? -0.937  -28.199 -2.939  1.00 55.30  ? 18  TYR A CZ  1 
ATOM   142  O OH  . TYR A 1 19 ? -0.374  -29.135 -3.769  1.00 61.88  ? 18  TYR A OH  1 
ATOM   143  N N   . PRO A 1 20 ? -2.962  -24.648 2.874   1.00 32.49  ? 19  PRO A N   1 
ATOM   144  C CA  . PRO A 1 20 ? -2.926  -23.544 3.842   1.00 33.17  ? 19  PRO A CA  1 
ATOM   145  C C   . PRO A 1 20 ? -2.229  -22.362 3.155   1.00 30.10  ? 19  PRO A C   1 
ATOM   146  O O   . PRO A 1 20 ? -1.483  -22.575 2.218   1.00 28.66  ? 19  PRO A O   1 
ATOM   147  C CB  . PRO A 1 20 ? -2.106  -24.121 5.015   1.00 32.98  ? 19  PRO A CB  1 
ATOM   148  C CG  . PRO A 1 20 ? -1.266  -25.212 4.363   1.00 33.40  ? 19  PRO A CG  1 
ATOM   149  C CD  . PRO A 1 20 ? -2.070  -25.776 3.215   1.00 33.02  ? 19  PRO A CD  1 
ATOM   150  N N   . HIS A 1 21 ? -2.513  -21.145 3.597   1.00 27.32  ? 20  HIS A N   1 
ATOM   151  C CA  . HIS A 1 21 ? -1.754  -19.963 3.198   1.00 26.52  ? 20  HIS A CA  1 
ATOM   152  C C   . HIS A 1 21 ? -0.256  -20.243 3.350   1.00 27.18  ? 20  HIS A C   1 
ATOM   153  O O   . HIS A 1 21 ? 0.189   -20.649 4.437   1.00 27.10  ? 20  HIS A O   1 
ATOM   154  C CB  . HIS A 1 21 ? -2.179  -18.770 4.066   1.00 27.12  ? 20  HIS A CB  1 
ATOM   155  C CG  . HIS A 1 21 ? -3.634  -18.437 3.895   1.00 26.95  ? 20  HIS A CG  1 
ATOM   156  N ND1 . HIS A 1 21 ? -4.615  -19.117 4.592   1.00 30.11  ? 20  HIS A ND1 1 
ATOM   157  C CD2 . HIS A 1 21 ? -4.270  -17.474 3.174   1.00 28.52  ? 20  HIS A CD2 1 
ATOM   158  C CE1 . HIS A 1 21 ? -5.815  -18.598 4.289   1.00 31.52  ? 20  HIS A CE1 1 
ATOM   159  N NE2 . HIS A 1 21 ? -5.633  -17.597 3.441   1.00 29.63  ? 20  HIS A NE2 1 
ATOM   160  N N   . TRP A 1 22 ? 0.505   -20.017 2.251   1.00 26.51  ? 21  TRP A N   1 
ATOM   161  C CA  . TRP A 1 22 ? 1.833   -20.602 2.076   1.00 23.67  ? 21  TRP A CA  1 
ATOM   162  C C   . TRP A 1 22 ? 2.908   -19.527 1.936   1.00 24.12  ? 21  TRP A C   1 
ATOM   163  O O   . TRP A 1 22 ? 2.775   -18.641 1.104   1.00 24.16  ? 21  TRP A O   1 
ATOM   164  C CB  . TRP A 1 22 ? 1.844   -21.521 0.848   1.00 24.67  ? 21  TRP A CB  1 
ATOM   165  C CG  . TRP A 1 22 ? 2.932   -22.570 0.907   1.00 25.43  ? 21  TRP A CG  1 
ATOM   166  C CD1 . TRP A 1 22 ? 4.281   -22.433 0.686   1.00 26.63  ? 21  TRP A CD1 1 
ATOM   167  C CD2 . TRP A 1 22 ? 2.723   -23.955 1.249   1.00 27.78  ? 21  TRP A CD2 1 
ATOM   168  N NE1 . TRP A 1 22 ? 4.907   -23.656 0.801   1.00 26.68  ? 21  TRP A NE1 1 
ATOM   169  C CE2 . TRP A 1 22 ? 3.982   -24.599 1.165   1.00 30.77  ? 21  TRP A CE2 1 
ATOM   170  C CE3 . TRP A 1 22 ? 1.590   -24.715 1.581   1.00 31.26  ? 21  TRP A CE3 1 
ATOM   171  C CZ2 . TRP A 1 22 ? 4.152   -25.963 1.446   1.00 31.99  ? 21  TRP A CZ2 1 
ATOM   172  C CZ3 . TRP A 1 22 ? 1.760   -26.065 1.847   1.00 33.82  ? 21  TRP A CZ3 1 
ATOM   173  C CH2 . TRP A 1 22 ? 3.024   -26.673 1.784   1.00 37.53  ? 21  TRP A CH2 1 
ATOM   174  N N   . PRO A 1 23 ? 4.047   -19.585 2.682   1.00 24.72  ? 22  PRO A N   1 
ATOM   175  C CA  . PRO A 1 23 ? 5.112   -18.582 2.499   1.00 23.79  ? 22  PRO A CA  1 
ATOM   176  C C   . PRO A 1 23 ? 5.582   -18.562 1.032   1.00 22.09  ? 22  PRO A C   1 
ATOM   177  O O   . PRO A 1 23 ? 5.866   -19.613 0.423   1.00 23.71  ? 22  PRO A O   1 
ATOM   178  C CB  . PRO A 1 23 ? 6.215   -19.097 3.517   1.00 23.35  ? 22  PRO A CB  1 
ATOM   179  C CG  . PRO A 1 23 ? 5.966   -20.628 3.619   1.00 21.24  ? 22  PRO A CG  1 
ATOM   180  C CD  . PRO A 1 23 ? 4.408   -20.621 3.669   1.00 23.15  ? 22  PRO A CD  1 
ATOM   181  N N   . ALA A 1 24 ? 5.659   -17.368 0.447   1.00 19.03  ? 23  ALA A N   1 
ATOM   182  C CA  . ALA A 1 24 ? 5.956   -17.265 -0.980  1.00 19.68  ? 23  ALA A CA  1 
ATOM   183  C C   . ALA A 1 24 ? 6.512   -15.877 -1.303  1.00 20.53  ? 23  ALA A C   1 
ATOM   184  O O   . ALA A 1 24 ? 6.501   -14.978 -0.470  1.00 21.22  ? 23  ALA A O   1 
ATOM   185  C CB  . ALA A 1 24 ? 4.693   -17.523 -1.781  1.00 22.25  ? 23  ALA A CB  1 
ATOM   186  N N   . ARG A 1 25 ? 6.995   -15.701 -2.530  1.00 21.86  ? 24  ARG A N   1 
ATOM   187  C CA  . ARG A 1 25 ? 7.396   -14.364 -2.927  1.00 21.62  ? 24  ARG A CA  1 
ATOM   188  C C   . ARG A 1 25 ? 6.863   -14.093 -4.327  1.00 22.32  ? 24  ARG A C   1 
ATOM   189  O O   . ARG A 1 25 ? 6.598   -15.042 -5.097  1.00 23.48  ? 24  ARG A O   1 
ATOM   190  C CB  . ARG A 1 25 ? 8.914   -14.253 -2.885  1.00 20.11  ? 24  ARG A CB  1 
ATOM   191  C CG  . ARG A 1 25 ? 9.605   -15.120 -3.918  1.00 19.85  ? 24  ARG A CG  1 
ATOM   192  C CD  . ARG A 1 25 ? 11.179  -14.904 -3.809  1.00 20.61  ? 24  ARG A CD  1 
ATOM   193  N NE  . ARG A 1 25 ? 11.862  -15.707 -4.853  1.00 23.43  ? 24  ARG A NE  1 
ATOM   194  C CZ  . ARG A 1 25 ? 13.112  -16.170 -4.761  1.00 25.10  ? 24  ARG A CZ  1 
ATOM   195  N NH1 . ARG A 1 25 ? 13.815  -16.078 -3.634  1.00 24.27  ? 24  ARG A NH1 1 
ATOM   196  N NH2 . ARG A 1 25 ? 13.638  -16.827 -5.791  1.00 26.97  ? 24  ARG A NH2 1 
ATOM   197  N N   . ILE A 1 26 ? 6.714   -12.804 -4.651  1.00 21.90  ? 25  ILE A N   1 
ATOM   198  C CA  . ILE A 1 26 ? 6.526   -12.433 -6.060  1.00 22.58  ? 25  ILE A CA  1 
ATOM   199  C C   . ILE A 1 26 ? 7.852   -12.572 -6.797  1.00 24.74  ? 25  ILE A C   1 
ATOM   200  O O   . ILE A 1 26 ? 8.828   -11.955 -6.393  1.00 25.44  ? 25  ILE A O   1 
ATOM   201  C CB  . ILE A 1 26 ? 6.016   -10.985 -6.222  1.00 25.19  ? 25  ILE A CB  1 
ATOM   202  C CG1 . ILE A 1 26 ? 4.869   -10.659 -5.278  1.00 29.92  ? 25  ILE A CG1 1 
ATOM   203  C CG2 . ILE A 1 26 ? 5.704   -10.656 -7.711  1.00 21.03  ? 25  ILE A CG2 1 
ATOM   204  C CD1 . ILE A 1 26 ? 3.550   -11.313 -5.626  1.00 31.01  ? 25  ILE A CD1 1 
ATOM   205  N N   . ASP A 1 27 ? 7.874   -13.378 -7.864  1.00 25.74  ? 26  ASP A N   1 
ATOM   206  C CA  . ASP A 1 27 ? 9.121   -13.603 -8.590  1.00 27.23  ? 26  ASP A CA  1 
ATOM   207  C C   . ASP A 1 27 ? 9.299   -12.597 -9.723  1.00 28.10  ? 26  ASP A C   1 
ATOM   208  O O   . ASP A 1 27 ? 8.358   -11.969 -10.191 1.00 26.98  ? 26  ASP A O   1 
ATOM   209  C CB  . ASP A 1 27 ? 9.223   -15.001 -9.176  1.00 24.77  ? 26  ASP A CB  1 
ATOM   210  C CG  . ASP A 1 27 ? 10.241  -15.925 -8.535  1.00 27.19  ? 26  ASP A CG  1 
ATOM   211  O OD1 . ASP A 1 27 ? 10.833  -15.514 -7.525  1.00 31.78  ? 26  ASP A OD1 1 
ATOM   212  O OD2 . ASP A 1 27 ? 10.438  -17.032 -9.054  1.00 30.54  ? 26  ASP A OD2 1 
ATOM   213  N N   . ASP A 1 28 ? 10.567  -12.448 -10.155 1.00 28.97  ? 27  ASP A N   1 
ATOM   214  C CA  . ASP A 1 28 ? 10.870  -11.772 -11.399 1.00 30.90  ? 27  ASP A CA  1 
ATOM   215  C C   . ASP A 1 28 ? 10.557  -12.760 -12.534 1.00 30.09  ? 27  ASP A C   1 
ATOM   216  O O   . ASP A 1 28 ? 10.435  -13.967 -12.332 1.00 33.95  ? 27  ASP A O   1 
ATOM   217  C CB  . ASP A 1 28 ? 12.362  -11.418 -11.440 1.00 34.96  ? 27  ASP A CB  1 
ATOM   218  C CG  . ASP A 1 28 ? 12.844  -10.184 -10.668 1.00 43.61  ? 27  ASP A CG  1 
ATOM   219  O OD1 . ASP A 1 28 ? 12.582  -9.031  -11.112 1.00 42.85  ? 27  ASP A OD1 1 
ATOM   220  O OD2 . ASP A 1 28 ? 13.532  -10.386 -9.636  1.00 50.80  ? 27  ASP A OD2 1 
ATOM   221  N N   . ILE A 1 29 ? 10.392  -12.257 -13.748 1.00 33.83  ? 28  ILE A N   1 
ATOM   222  C CA  . ILE A 1 29 ? 10.340  -13.162 -14.892 1.00 31.95  ? 28  ILE A CA  1 
ATOM   223  C C   . ILE A 1 29 ? 11.666  -12.946 -15.616 1.00 35.48  ? 28  ILE A C   1 
ATOM   224  O O   . ILE A 1 29 ? 12.004  -11.794 -15.889 1.00 33.10  ? 28  ILE A O   1 
ATOM   225  C CB  . ILE A 1 29 ? 9.173   -12.729 -15.794 1.00 33.54  ? 28  ILE A CB  1 
ATOM   226  C CG1 . ILE A 1 29 ? 7.819   -12.767 -15.056 1.00 37.01  ? 28  ILE A CG1 1 
ATOM   227  C CG2 . ILE A 1 29 ? 9.131   -13.544 -17.078 1.00 29.71  ? 28  ILE A CG2 1 
ATOM   228  C CD1 . ILE A 1 29 ? 6.856   -11.690 -15.523 1.00 34.82  ? 28  ILE A CD1 1 
ATOM   229  N N   . ALA A 1 30 ? 12.427  -14.022 -15.848 1.00 37.28  ? 29  ALA A N   1 
ATOM   230  C CA  . ALA A 1 30 ? 13.699  -13.892 -16.556 1.00 31.61  ? 29  ALA A CA  1 
ATOM   231  C C   . ALA A 1 30 ? 13.461  -13.541 -18.031 1.00 31.00  ? 29  ALA A C   1 
ATOM   232  O O   . ALA A 1 30 ? 12.445  -13.885 -18.627 1.00 30.83  ? 29  ALA A O   1 
ATOM   233  C CB  . ALA A 1 30 ? 14.495  -15.177 -16.418 1.00 34.93  ? 29  ALA A CB  1 
ATOM   234  N N   . ASP A 1 31 ? 14.424  -12.851 -18.640 1.00 33.01  ? 30  ASP A N   1 
ATOM   235  C CA  . ASP A 1 31 ? 14.432  -12.740 -20.095 1.00 31.51  ? 30  ASP A CA  1 
ATOM   236  C C   . ASP A 1 31 ? 14.327  -14.153 -20.679 1.00 26.65  ? 30  ASP A C   1 
ATOM   237  O O   . ASP A 1 31 ? 14.995  -15.067 -20.193 1.00 30.15  ? 30  ASP A O   1 
ATOM   238  C CB  . ASP A 1 31 ? 15.697  -12.003 -20.523 1.00 32.69  ? 30  ASP A CB  1 
ATOM   239  C CG  . ASP A 1 31 ? 15.647  -10.489 -20.349 1.00 37.27  ? 30  ASP A CG  1 
ATOM   240  O OD1 . ASP A 1 31 ? 14.538  -9.928  -20.381 1.00 43.38  ? 30  ASP A OD1 1 
ATOM   241  O OD2 . ASP A 1 31 ? 16.726  -9.894  -20.189 1.00 42.82  ? 30  ASP A OD2 1 
ATOM   242  N N   . GLY A 1 32 ? 13.435  -14.303 -21.669 1.00 27.82  ? 31  GLY A N   1 
ATOM   243  C CA  . GLY A 1 32 ? 13.237  -15.519 -22.449 1.00 29.19  ? 31  GLY A CA  1 
ATOM   244  C C   . GLY A 1 32 ? 12.231  -16.456 -21.778 1.00 34.63  ? 31  GLY A C   1 
ATOM   245  O O   . GLY A 1 32 ? 11.827  -17.443 -22.374 1.00 34.45  ? 31  GLY A O   1 
ATOM   246  N N   . ALA A 1 33 ? 11.833  -16.133 -20.539 1.00 30.59  ? 32  ALA A N   1 
ATOM   247  C CA  . ALA A 1 33 ? 10.978  -17.039 -19.781 1.00 33.67  ? 32  ALA A CA  1 
ATOM   248  C C   . ALA A 1 33 ? 9.487   -16.766 -20.052 1.00 28.78  ? 32  ALA A C   1 
ATOM   249  O O   . ALA A 1 33 ? 9.086   -15.679 -20.491 1.00 31.07  ? 32  ALA A O   1 
ATOM   250  C CB  . ALA A 1 33 ? 11.345  -16.922 -18.295 1.00 34.51  ? 32  ALA A CB  1 
ATOM   251  N N   . VAL A 1 34 ? 8.650   -17.792 -19.796 1.00 33.39  ? 33  VAL A N   1 
ATOM   252  C CA  . VAL A 1 34 ? 7.204   -17.742 -20.027 1.00 34.62  ? 33  VAL A CA  1 
ATOM   253  C C   . VAL A 1 34 ? 6.582   -16.681 -19.127 1.00 33.01  ? 33  VAL A C   1 
ATOM   254  O O   . VAL A 1 34 ? 6.814   -16.724 -17.931 1.00 33.14  ? 33  VAL A O   1 
ATOM   255  C CB  . VAL A 1 34 ? 6.605   -19.129 -19.674 1.00 35.37  ? 33  VAL A CB  1 
ATOM   256  C CG1 . VAL A 1 34 ? 5.078   -19.122 -19.687 1.00 34.72  ? 33  VAL A CG1 1 
ATOM   257  C CG2 . VAL A 1 34 ? 7.135   -20.210 -20.618 1.00 37.19  ? 33  VAL A CG2 1 
ATOM   258  N N   . LYS A 1 35 ? 5.807   -15.753 -19.707 1.00 33.46  ? 34  LYS A N   1 
ATOM   259  C CA  . LYS A 1 35 ? 5.145   -14.690 -18.949 1.00 35.66  ? 34  LYS A CA  1 
ATOM   260  C C   . LYS A 1 35 ? 3.841   -15.176 -18.317 1.00 38.23  ? 34  LYS A C   1 
ATOM   261  O O   . LYS A 1 35 ? 3.172   -16.032 -18.881 1.00 36.24  ? 34  LYS A O   1 
ATOM   262  C CB  . LYS A 1 35 ? 4.842   -13.471 -19.824 1.00 38.28  ? 34  LYS A CB  1 
ATOM   263  C CG  . LYS A 1 35 ? 6.067   -12.673 -20.271 1.00 38.58  ? 34  LYS A CG  1 
ATOM   264  C CD  . LYS A 1 35 ? 5.756   -11.479 -21.175 1.00 42.62  ? 34  LYS A CD  1 
ATOM   265  C CE  . LYS A 1 35 ? 5.438   -11.945 -22.569 1.00 41.41  ? 34  LYS A CE  1 
ATOM   266  N NZ  . LYS A 1 35 ? 5.197   -10.801 -23.448 1.00 38.51  ? 34  LYS A NZ  1 
ATOM   267  N N   . PRO A 1 36 ? 3.386   -14.594 -17.175 1.00 37.51  ? 35  PRO A N   1 
ATOM   268  C CA  . PRO A 1 36 ? 2.112   -15.010 -16.578 1.00 37.71  ? 35  PRO A CA  1 
ATOM   269  C C   . PRO A 1 36 ? 0.963   -14.476 -17.430 1.00 35.42  ? 35  PRO A C   1 
ATOM   270  O O   . PRO A 1 36 ? 1.111   -13.489 -18.144 1.00 37.00  ? 35  PRO A O   1 
ATOM   271  C CB  . PRO A 1 36 ? 2.102   -14.387 -15.157 1.00 35.51  ? 35  PRO A CB  1 
ATOM   272  C CG  . PRO A 1 36 ? 3.087   -13.217 -15.225 1.00 42.06  ? 35  PRO A CG  1 
ATOM   273  C CD  . PRO A 1 36 ? 4.000   -13.476 -16.443 1.00 39.75  ? 35  PRO A CD  1 
ATOM   274  N N   . PRO A 1 37 ? -0.255  -15.028 -17.266 1.00 35.94  ? 36  PRO A N   1 
ATOM   275  C CA  . PRO A 1 37 ? -1.448  -14.468 -17.900 1.00 40.42  ? 36  PRO A CA  1 
ATOM   276  C C   . PRO A 1 37 ? -1.643  -13.047 -17.398 1.00 41.67  ? 36  PRO A C   1 
ATOM   277  O O   . PRO A 1 37 ? -1.113  -12.699 -16.330 1.00 34.87  ? 36  PRO A O   1 
ATOM   278  C CB  . PRO A 1 37 ? -2.617  -15.351 -17.433 1.00 37.45  ? 36  PRO A CB  1 
ATOM   279  C CG  . PRO A 1 37 ? -1.981  -16.583 -16.819 1.00 36.79  ? 36  PRO A CG  1 
ATOM   280  C CD  . PRO A 1 37 ? -0.541  -16.215 -16.441 1.00 38.43  ? 36  PRO A CD  1 
ATOM   281  N N   . PRO A 1 38 ? -2.444  -12.213 -18.106 1.00 40.46  ? 37  PRO A N   1 
ATOM   282  C CA  . PRO A 1 38 ? -2.821  -10.885 -17.606 1.00 43.29  ? 37  PRO A CA  1 
ATOM   283  C C   . PRO A 1 38 ? -3.455  -10.953 -16.218 1.00 34.90  ? 37  PRO A C   1 
ATOM   284  O O   . PRO A 1 38 ? -4.123  -11.931 -15.894 1.00 38.19  ? 37  PRO A O   1 
ATOM   285  C CB  . PRO A 1 38 ? -3.797  -10.278 -18.654 1.00 43.12  ? 37  PRO A CB  1 
ATOM   286  C CG  . PRO A 1 38 ? -4.076  -11.412 -19.608 1.00 38.87  ? 37  PRO A CG  1 
ATOM   287  C CD  . PRO A 1 38 ? -3.035  -12.506 -19.430 1.00 43.32  ? 37  PRO A CD  1 
ATOM   288  N N   . ASN A 1 39 ? -3.135  -9.934  -15.414 1.00 37.03  ? 38  ASN A N   1 
ATOM   289  C CA  . ASN A 1 39 ? -3.617  -9.706  -14.066 1.00 40.86  ? 38  ASN A CA  1 
ATOM   290  C C   . ASN A 1 39 ? -3.052  -10.733 -13.083 1.00 36.90  ? 38  ASN A C   1 
ATOM   291  O O   . ASN A 1 39 ? -3.462  -10.700 -11.918 1.00 35.49  ? 38  ASN A O   1 
ATOM   292  C CB  . ASN A 1 39 ? -5.140  -9.558  -14.033 1.00 47.89  ? 38  ASN A CB  1 
ATOM   293  C CG  . ASN A 1 39 ? -5.576  -8.409  -14.912 1.00 51.26  ? 38  ASN A CG  1 
ATOM   294  O OD1 . ASN A 1 39 ? -5.397  -7.242  -14.541 1.00 52.11  ? 38  ASN A OD1 1 
ATOM   295  N ND2 . ASN A 1 39 ? -6.083  -8.720  -16.095 1.00 50.61  ? 38  ASN A ND2 1 
ATOM   296  N N   . LYS A 1 40 ? -2.133  -11.616 -13.545 1.00 30.70  ? 39  LYS A N   1 
ATOM   297  C CA  . LYS A 1 40 ? -1.523  -12.635 -12.684 1.00 25.82  ? 39  LYS A CA  1 
ATOM   298  C C   . LYS A 1 40 ? -0.044  -12.316 -12.414 1.00 24.82  ? 39  LYS A C   1 
ATOM   299  O O   . LYS A 1 40 ? 0.623   -11.572 -13.159 1.00 29.62  ? 39  LYS A O   1 
ATOM   300  C CB  . LYS A 1 40 ? -1.622  -14.082 -13.174 1.00 31.38  ? 39  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 40 ? -3.014  -14.602 -13.568 1.00 35.97  ? 39  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 40 ? -3.948  -14.361 -12.396 1.00 38.14  ? 39  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 40 ? -5.409  -14.536 -12.690 1.00 45.16  ? 39  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 40 ? -5.770  -15.952 -12.666 1.00 43.63  ? 39  LYS A NZ  1 
ATOM   305  N N   . TYR A 1 41 ? 0.412   -12.849 -11.283 1.00 22.85  ? 40  TYR A N   1 
ATOM   306  C CA  . TYR A 1 41 ? 1.791   -12.700 -10.849 1.00 23.42  ? 40  TYR A CA  1 
ATOM   307  C C   . TYR A 1 41 ? 2.438   -14.073 -10.810 1.00 23.74  ? 40  TYR A C   1 
ATOM   308  O O   . TYR A 1 41 ? 1.838   -15.068 -10.394 1.00 24.71  ? 40  TYR A O   1 
ATOM   309  C CB  . TYR A 1 41 ? 1.871   -12.056 -9.448  1.00 24.50  ? 40  TYR A CB  1 
ATOM   310  C CG  . TYR A 1 41 ? 1.390   -10.619 -9.449  1.00 27.07  ? 40  TYR A CG  1 
ATOM   311  C CD1 . TYR A 1 41 ? 0.039   -10.320 -9.283  1.00 31.50  ? 40  TYR A CD1 1 
ATOM   312  C CD2 . TYR A 1 41 ? 2.272   -9.559  -9.637  1.00 30.91  ? 40  TYR A CD2 1 
ATOM   313  C CE1 . TYR A 1 41 ? -0.421  -9.020  -9.384  1.00 36.28  ? 40  TYR A CE1 1 
ATOM   314  C CE2 . TYR A 1 41 ? 1.822   -8.244  -9.689  1.00 33.82  ? 40  TYR A CE2 1 
ATOM   315  C CZ  . TYR A 1 41 ? 0.470   -7.981  -9.560  1.00 36.07  ? 40  TYR A CZ  1 
ATOM   316  O OH  . TYR A 1 41 ? -0.026  -6.712  -9.652  1.00 36.35  ? 40  TYR A OH  1 
ATOM   317  N N   . PRO A 1 42 ? 3.761   -14.165 -11.069 1.00 23.13  ? 41  PRO A N   1 
ATOM   318  C CA  . PRO A 1 42 ? 4.464   -15.426 -10.801 1.00 22.14  ? 41  PRO A CA  1 
ATOM   319  C C   . PRO A 1 42 ? 4.771   -15.555 -9.321  1.00 24.07  ? 41  PRO A C   1 
ATOM   320  O O   . PRO A 1 42 ? 5.452   -14.680 -8.774  1.00 25.92  ? 41  PRO A O   1 
ATOM   321  C CB  . PRO A 1 42 ? 5.747   -15.313 -11.636 1.00 25.09  ? 41  PRO A CB  1 
ATOM   322  C CG  . PRO A 1 42 ? 5.955   -13.849 -11.861 1.00 24.81  ? 41  PRO A CG  1 
ATOM   323  C CD  . PRO A 1 42 ? 4.606   -13.109 -11.649 1.00 25.12  ? 41  PRO A CD  1 
ATOM   324  N N   . ILE A 1 43 ? 4.242   -16.609 -8.690  1.00 22.52  ? 42  ILE A N   1 
ATOM   325  C CA  . ILE A 1 43 ? 4.434   -16.760 -7.257  1.00 23.19  ? 42  ILE A CA  1 
ATOM   326  C C   . ILE A 1 43 ? 5.403   -17.918 -7.052  1.00 25.66  ? 42  ILE A C   1 
ATOM   327  O O   . ILE A 1 43 ? 5.115   -19.041 -7.485  1.00 27.98  ? 42  ILE A O   1 
ATOM   328  C CB  . ILE A 1 43 ? 3.097   -17.027 -6.544  1.00 23.06  ? 42  ILE A CB  1 
ATOM   329  C CG1 . ILE A 1 43 ? 2.055   -15.909 -6.854  1.00 24.56  ? 42  ILE A CG1 1 
ATOM   330  C CG2 . ILE A 1 43 ? 3.316   -17.199 -5.022  1.00 20.65  ? 42  ILE A CG2 1 
ATOM   331  C CD1 . ILE A 1 43 ? 2.514   -14.490 -6.534  1.00 25.18  ? 42  ILE A CD1 1 
ATOM   332  N N   . PHE A 1 44 ? 6.531   -17.647 -6.373  1.00 22.60  ? 43  PHE A N   1 
ATOM   333  C CA  . PHE A 1 44 ? 7.416   -18.744 -6.018  1.00 22.58  ? 43  PHE A CA  1 
ATOM   334  C C   . PHE A 1 44 ? 7.149   -19.145 -4.565  1.00 23.12  ? 43  PHE A C   1 
ATOM   335  O O   . PHE A 1 44 ? 7.199   -18.288 -3.674  1.00 23.80  ? 43  PHE A O   1 
ATOM   336  C CB  . PHE A 1 44 ? 8.840   -18.190 -6.183  1.00 22.82  ? 43  PHE A CB  1 
ATOM   337  C CG  . PHE A 1 44 ? 9.855   -19.236 -5.749  1.00 26.58  ? 43  PHE A CG  1 
ATOM   338  C CD1 . PHE A 1 44 ? 10.248  -20.247 -6.641  1.00 26.42  ? 43  PHE A CD1 1 
ATOM   339  C CD2 . PHE A 1 44 ? 10.409  -19.207 -4.460  1.00 29.42  ? 43  PHE A CD2 1 
ATOM   340  C CE1 . PHE A 1 44 ? 11.189  -21.193 -6.255  1.00 27.63  ? 43  PHE A CE1 1 
ATOM   341  C CE2 . PHE A 1 44 ? 11.351  -20.179 -4.082  1.00 29.83  ? 43  PHE A CE2 1 
ATOM   342  C CZ  . PHE A 1 44 ? 11.752  -21.146 -4.982  1.00 28.29  ? 43  PHE A CZ  1 
ATOM   343  N N   . PHE A 1 45 ? 6.839   -20.438 -4.347  1.00 23.14  ? 44  PHE A N   1 
ATOM   344  C CA  . PHE A 1 45 ? 6.425   -20.965 -3.050  1.00 21.09  ? 44  PHE A CA  1 
ATOM   345  C C   . PHE A 1 45 ? 7.699   -21.460 -2.376  1.00 27.44  ? 44  PHE A C   1 
ATOM   346  O O   . PHE A 1 45 ? 8.430   -22.307 -2.930  1.00 24.53  ? 44  PHE A O   1 
ATOM   347  C CB  . PHE A 1 45 ? 5.423   -22.137 -3.231  1.00 27.01  ? 44  PHE A CB  1 
ATOM   348  C CG  . PHE A 1 45 ? 4.050   -21.641 -3.669  1.00 26.47  ? 44  PHE A CG  1 
ATOM   349  C CD1 . PHE A 1 45 ? 3.751   -21.480 -5.020  1.00 29.73  ? 44  PHE A CD1 1 
ATOM   350  C CD2 . PHE A 1 45 ? 3.060   -21.343 -2.741  1.00 29.73  ? 44  PHE A CD2 1 
ATOM   351  C CE1 . PHE A 1 45 ? 2.513   -20.985 -5.436  1.00 31.66  ? 44  PHE A CE1 1 
ATOM   352  C CE2 . PHE A 1 45 ? 1.802   -20.880 -3.170  1.00 27.12  ? 44  PHE A CE2 1 
ATOM   353  C CZ  . PHE A 1 45 ? 1.550   -20.677 -4.496  1.00 30.23  ? 44  PHE A CZ  1 
ATOM   354  N N   . PHE A 1 46 ? 7.970   -20.901 -1.192  1.00 23.80  ? 45  PHE A N   1 
ATOM   355  C CA  . PHE A 1 46 ? 9.126   -21.365 -0.445  1.00 24.86  ? 45  PHE A CA  1 
ATOM   356  C C   . PHE A 1 46 ? 8.879   -22.804 0.023   1.00 25.84  ? 45  PHE A C   1 
ATOM   357  O O   . PHE A 1 46 ? 7.727   -23.250 0.175   1.00 26.59  ? 45  PHE A O   1 
ATOM   358  C CB  . PHE A 1 46 ? 9.393   -20.426 0.740   1.00 25.82  ? 45  PHE A CB  1 
ATOM   359  C CG  . PHE A 1 46 ? 9.859   -19.037 0.325   1.00 24.24  ? 45  PHE A CG  1 
ATOM   360  C CD1 . PHE A 1 46 ? 11.142  -18.848 -0.204  1.00 23.11  ? 45  PHE A CD1 1 
ATOM   361  C CD2 . PHE A 1 46 ? 9.092   -17.900 0.599   1.00 25.23  ? 45  PHE A CD2 1 
ATOM   362  C CE1 . PHE A 1 46 ? 11.566  -17.570 -0.587  1.00 20.80  ? 45  PHE A CE1 1 
ATOM   363  C CE2 . PHE A 1 46 ? 9.553   -16.616 0.257   1.00 21.10  ? 45  PHE A CE2 1 
ATOM   364  C CZ  . PHE A 1 46 ? 10.801  -16.448 -0.314  1.00 22.65  ? 45  PHE A CZ  1 
ATOM   365  N N   . GLY A 1 47 ? 9.994   -23.525 0.208   1.00 25.93  ? 46  GLY A N   1 
ATOM   366  C CA  . GLY A 1 47 ? 9.979   -24.915 0.646   1.00 27.86  ? 46  GLY A CA  1 
ATOM   367  C C   . GLY A 1 47 ? 9.764   -25.901 -0.513  1.00 33.35  ? 46  GLY A C   1 
ATOM   368  O O   . GLY A 1 47 ? 10.656  -26.692 -0.859  1.00 32.45  ? 46  GLY A O   1 
ATOM   369  N N   . THR A 1 48 ? 8.583   -25.845 -1.143  1.00 32.63  ? 47  THR A N   1 
ATOM   370  C CA  . THR A 1 48 ? 8.322   -26.662 -2.322  1.00 34.36  ? 47  THR A CA  1 
ATOM   371  C C   . THR A 1 48 ? 9.119   -26.166 -3.523  1.00 36.37  ? 47  THR A C   1 
ATOM   372  O O   . THR A 1 48 ? 9.373   -26.916 -4.480  1.00 30.37  ? 47  THR A O   1 
ATOM   373  C CB  . THR A 1 48 ? 6.829   -26.676 -2.666  1.00 34.43  ? 47  THR A CB  1 
ATOM   374  O OG1 . THR A 1 48 ? 6.499   -25.358 -3.080  1.00 32.51  ? 47  THR A OG1 1 
ATOM   375  C CG2 . THR A 1 48 ? 5.916   -27.129 -1.549  1.00 33.32  ? 47  THR A CG2 1 
ATOM   376  N N   . HIS A 1 49 ? 9.360   -24.852 -3.572  1.00 28.29  ? 48  HIS A N   1 
ATOM   377  C CA  . HIS A 1 49 ? 10.050  -24.270 -4.717  1.00 29.83  ? 48  HIS A CA  1 
ATOM   378  C C   . HIS A 1 49 ? 9.237   -24.392 -6.007  1.00 30.56  ? 48  HIS A C   1 
ATOM   379  O O   . HIS A 1 49 ? 9.807   -24.372 -7.099  1.00 30.74  ? 48  HIS A O   1 
ATOM   380  C CB  . HIS A 1 49 ? 11.514  -24.753 -4.837  1.00 27.96  ? 48  HIS A CB  1 
ATOM   381  C CG  . HIS A 1 49 ? 12.257  -24.787 -3.554  1.00 30.33  ? 48  HIS A CG  1 
ATOM   382  N ND1 . HIS A 1 49 ? 13.111  -25.812 -3.231  1.00 29.92  ? 48  HIS A ND1 1 
ATOM   383  C CD2 . HIS A 1 49 ? 12.292  -23.925 -2.513  1.00 28.37  ? 48  HIS A CD2 1 
ATOM   384  C CE1 . HIS A 1 49 ? 13.605  -25.605 -2.018  1.00 37.01  ? 48  HIS A CE1 1 
ATOM   385  N NE2 . HIS A 1 49 ? 13.158  -24.438 -1.578  1.00 33.83  ? 48  HIS A NE2 1 
ATOM   386  N N   . GLU A 1 50 ? 7.906   -24.501 -5.896  1.00 31.70  ? 49  GLU A N   1 
ATOM   387  C CA  . GLU A 1 50 ? 7.030   -24.503 -7.060  1.00 31.89  ? 49  GLU A CA  1 
ATOM   388  C C   . GLU A 1 50 ? 6.599   -23.077 -7.400  1.00 33.04  ? 49  GLU A C   1 
ATOM   389  O O   . GLU A 1 50 ? 6.712   -22.174 -6.558  1.00 29.48  ? 49  GLU A O   1 
ATOM   390  C CB  . GLU A 1 50 ? 5.793   -25.376 -6.856  1.00 36.29  ? 49  GLU A CB  1 
ATOM   391  C CG  . GLU A 1 50 ? 6.165   -26.822 -6.543  1.00 42.73  ? 49  GLU A CG  1 
ATOM   392  C CD  . GLU A 1 50 ? 5.012   -27.721 -6.155  1.00 46.89  ? 49  GLU A CD  1 
ATOM   393  O OE1 . GLU A 1 50 ? 3.833   -27.305 -6.219  1.00 47.53  ? 49  GLU A OE1 1 
ATOM   394  O OE2 . GLU A 1 50 ? 5.338   -28.852 -5.741  1.00 52.59  ? 49  GLU A OE2 1 
ATOM   395  N N   . THR A 1 51 ? 6.205   -22.888 -8.669  1.00 26.62  ? 50  THR A N   1 
ATOM   396  C CA  . THR A 1 51 ? 5.702   -21.611 -9.174  1.00 28.58  ? 50  THR A CA  1 
ATOM   397  C C   . THR A 1 51 ? 4.255   -21.798 -9.601  1.00 28.01  ? 50  THR A C   1 
ATOM   398  O O   . THR A 1 51 ? 3.910   -22.807 -10.223 1.00 31.74  ? 50  THR A O   1 
ATOM   399  C CB  . THR A 1 51 ? 6.555   -21.034 -10.310 1.00 31.15  ? 50  THR A CB  1 
ATOM   400  O OG1 . THR A 1 51 ? 7.879   -20.760 -9.848  1.00 31.47  ? 50  THR A OG1 1 
ATOM   401  C CG2 . THR A 1 51 ? 6.004   -19.731 -10.877 1.00 34.69  ? 50  THR A CG2 1 
ATOM   402  N N   . ALA A 1 52 ? 3.390   -20.851 -9.225  1.00 28.36  ? 51  ALA A N   1 
ATOM   403  C CA  . ALA A 1 52 ? 2.043   -20.800 -9.780  1.00 26.99  ? 51  ALA A CA  1 
ATOM   404  C C   . ALA A 1 52 ? 1.718   -19.350 -10.106 1.00 28.47  ? 51  ALA A C   1 
ATOM   405  O O   . ALA A 1 52 ? 2.370   -18.434 -9.623  1.00 27.97  ? 51  ALA A O   1 
ATOM   406  C CB  . ALA A 1 52 ? 1.037   -21.361 -8.808  1.00 29.89  ? 51  ALA A CB  1 
ATOM   407  N N   . PHE A 1 53 ? 0.681   -19.144 -10.921 1.00 26.89  ? 52  PHE A N   1 
ATOM   408  C CA  . PHE A 1 53 ? 0.285   -17.797 -11.280 1.00 26.91  ? 52  PHE A CA  1 
ATOM   409  C C   . PHE A 1 53 ? -0.967  -17.432 -10.505 1.00 30.52  ? 52  PHE A C   1 
ATOM   410  O O   . PHE A 1 53 ? -1.979  -18.131 -10.599 1.00 32.94  ? 52  PHE A O   1 
ATOM   411  C CB  . PHE A 1 53 ? -0.006  -17.693 -12.786 1.00 26.84  ? 52  PHE A CB  1 
ATOM   412  C CG  . PHE A 1 53 ? 1.167   -18.098 -13.648 1.00 30.61  ? 52  PHE A CG  1 
ATOM   413  C CD1 . PHE A 1 53 ? 2.350   -17.364 -13.593 1.00 34.74  ? 52  PHE A CD1 1 
ATOM   414  C CD2 . PHE A 1 53 ? 1.043   -19.113 -14.603 1.00 33.83  ? 52  PHE A CD2 1 
ATOM   415  C CE1 . PHE A 1 53 ? 3.441   -17.708 -14.396 1.00 45.16  ? 52  PHE A CE1 1 
ATOM   416  C CE2 . PHE A 1 53 ? 2.134   -19.449 -15.393 1.00 39.66  ? 52  PHE A CE2 1 
ATOM   417  C CZ  . PHE A 1 53 ? 3.325   -18.747 -15.306 1.00 37.45  ? 52  PHE A CZ  1 
ATOM   418  N N   . LEU A 1 54 ? -0.881  -16.330 -9.739  1.00 24.67  ? 53  LEU A N   1 
ATOM   419  C CA  . LEU A 1 54 ? -1.989  -15.981 -8.855  1.00 24.79  ? 53  LEU A CA  1 
ATOM   420  C C   . LEU A 1 54 ? -2.300  -14.495 -9.004  1.00 27.95  ? 53  LEU A C   1 
ATOM   421  O O   . LEU A 1 54 ? -1.413  -13.666 -9.296  1.00 27.06  ? 53  LEU A O   1 
ATOM   422  C CB  . LEU A 1 54 ? -1.628  -16.276 -7.397  1.00 28.09  ? 53  LEU A CB  1 
ATOM   423  C CG  . LEU A 1 54 ? -1.578  -17.747 -7.006  1.00 28.17  ? 53  LEU A CG  1 
ATOM   424  C CD1 . LEU A 1 54 ? -1.221  -17.796 -5.528  1.00 25.79  ? 53  LEU A CD1 1 
ATOM   425  C CD2 . LEU A 1 54 ? -2.954  -18.400 -7.282  1.00 32.00  ? 53  LEU A CD2 1 
ATOM   426  N N   . GLY A 1 55 ? -3.568  -14.160 -8.734  1.00 25.27  ? 54  GLY A N   1 
ATOM   427  C CA  . GLY A 1 55 ? -3.935  -12.759 -8.647  1.00 24.17  ? 54  GLY A CA  1 
ATOM   428  C C   . GLY A 1 55 ? -3.921  -12.264 -7.197  1.00 20.96  ? 54  GLY A C   1 
ATOM   429  O O   . GLY A 1 55 ? -3.866  -13.080 -6.250  1.00 22.16  ? 54  GLY A O   1 
ATOM   430  N N   . PRO A 1 56 ? -4.005  -10.928 -7.004  1.00 20.97  ? 55  PRO A N   1 
ATOM   431  C CA  . PRO A 1 56 ? -3.935  -10.289 -5.662  1.00 23.99  ? 55  PRO A CA  1 
ATOM   432  C C   . PRO A 1 56 ? -4.901  -10.787 -4.583  1.00 22.73  ? 55  PRO A C   1 
ATOM   433  O O   . PRO A 1 56 ? -4.598  -10.736 -3.376  1.00 22.72  ? 55  PRO A O   1 
ATOM   434  C CB  . PRO A 1 56 ? -4.190  -8.810  -5.981  1.00 25.85  ? 55  PRO A CB  1 
ATOM   435  C CG  . PRO A 1 56 ? -3.689  -8.646  -7.414  1.00 28.12  ? 55  PRO A CG  1 
ATOM   436  C CD  . PRO A 1 56 ? -4.025  -9.939  -8.102  1.00 26.37  ? 55  PRO A CD  1 
ATOM   437  N N   . LYS A 1 57 ? -6.061  -11.300 -5.030  1.00 23.52  ? 56  LYS A N   1 
ATOM   438  C CA  . LYS A 1 57 ? -7.035  -11.838 -4.086  1.00 26.44  ? 56  LYS A CA  1 
ATOM   439  C C   . LYS A 1 57 ? -6.464  -12.996 -3.263  1.00 25.54  ? 56  LYS A C   1 
ATOM   440  O O   . LYS A 1 57 ? -6.937  -13.257 -2.160  1.00 24.53  ? 56  LYS A O   1 
ATOM   441  C CB  . LYS A 1 57 ? -8.347  -12.291 -4.746  1.00 28.55  ? 56  LYS A CB  1 
ATOM   442  C CG  . LYS A 1 57 ? -8.171  -13.542 -5.582  1.00 30.80  ? 56  LYS A CG  1 
ATOM   443  C CD  . LYS A 1 57 ? -9.498  -14.050 -6.152  1.00 37.47  ? 56  LYS A CD  1 
ATOM   444  C CE  . LYS A 1 57 ? -9.371  -15.312 -6.946  1.00 37.70  ? 56  LYS A CE  1 
ATOM   445  N NZ  . LYS A 1 57 ? -9.197  -16.487 -6.084  1.00 47.10  ? 56  LYS A NZ  1 
ATOM   446  N N   . ASP A 1 58 ? -5.415  -13.674 -3.764  1.00 25.98  ? 57  ASP A N   1 
ATOM   447  C CA  . ASP A 1 58 ? -4.858  -14.819 -3.073  1.00 24.23  ? 57  ASP A CA  1 
ATOM   448  C C   . ASP A 1 58 ? -3.498  -14.473 -2.425  1.00 27.17  ? 57  ASP A C   1 
ATOM   449  O O   . ASP A 1 58 ? -2.757  -15.374 -2.003  1.00 24.25  ? 57  ASP A O   1 
ATOM   450  C CB  . ASP A 1 58 ? -4.811  -16.006 -4.034  1.00 26.52  ? 57  ASP A CB  1 
ATOM   451  C CG  . ASP A 1 58 ? -6.194  -16.546 -4.390  1.00 28.91  ? 57  ASP A CG  1 
ATOM   452  O OD1 . ASP A 1 58 ? -7.039  -16.532 -3.477  1.00 31.07  ? 57  ASP A OD1 1 
ATOM   453  O OD2 . ASP A 1 58 ? -6.397  -16.976 -5.555  1.00 28.80  ? 57  ASP A OD2 1 
ATOM   454  N N   . LEU A 1 59 ? -3.163  -13.169 -2.376  1.00 24.95  ? 58  LEU A N   1 
ATOM   455  C CA  . LEU A 1 59 ? -1.840  -12.719 -1.933  1.00 21.89  ? 58  LEU A CA  1 
ATOM   456  C C   . LEU A 1 59 ? -1.978  -11.887 -0.662  1.00 20.27  ? 58  LEU A C   1 
ATOM   457  O O   . LEU A 1 59 ? -2.539  -10.786 -0.692  1.00 22.35  ? 58  LEU A O   1 
ATOM   458  C CB  . LEU A 1 59 ? -1.070  -11.955 -3.027  1.00 20.31  ? 58  LEU A CB  1 
ATOM   459  C CG  . LEU A 1 59 ? -1.000  -12.707 -4.364  1.00 22.85  ? 58  LEU A CG  1 
ATOM   460  C CD1 . LEU A 1 59 ? -0.218  -11.948 -5.399  1.00 22.46  ? 58  LEU A CD1 1 
ATOM   461  C CD2 . LEU A 1 59 ? -0.343  -14.046 -4.228  1.00 22.59  ? 58  LEU A CD2 1 
ATOM   462  N N   . PHE A 1 60 ? -1.384  -12.393 0.427   1.00 20.67  ? 59  PHE A N   1 
ATOM   463  C CA  . PHE A 1 60 ? -1.488  -11.668 1.701   1.00 21.43  ? 59  PHE A CA  1 
ATOM   464  C C   . PHE A 1 60 ? -0.109  -11.173 2.114   1.00 24.40  ? 59  PHE A C   1 
ATOM   465  O O   . PHE A 1 60 ? 0.790   -12.000 2.306   1.00 26.48  ? 59  PHE A O   1 
ATOM   466  C CB  . PHE A 1 60 ? -1.948  -12.679 2.744   1.00 19.25  ? 59  PHE A CB  1 
ATOM   467  C CG  . PHE A 1 60 ? -3.393  -13.103 2.494   1.00 21.78  ? 59  PHE A CG  1 
ATOM   468  C CD1 . PHE A 1 60 ? -3.706  -14.049 1.516   1.00 24.37  ? 59  PHE A CD1 1 
ATOM   469  C CD2 . PHE A 1 60 ? -4.412  -12.554 3.257   1.00 24.97  ? 59  PHE A CD2 1 
ATOM   470  C CE1 . PHE A 1 60 ? -5.034  -14.406 1.274   1.00 29.11  ? 59  PHE A CE1 1 
ATOM   471  C CE2 . PHE A 1 60 ? -5.740  -12.945 3.033   1.00 24.99  ? 59  PHE A CE2 1 
ATOM   472  C CZ  . PHE A 1 60 ? -6.026  -13.892 2.063   1.00 26.47  ? 59  PHE A CZ  1 
ATOM   473  N N   . PRO A 1 61 ? 0.124   -9.848  2.264   1.00 26.69  ? 60  PRO A N   1 
ATOM   474  C CA  . PRO A 1 61 ? 1.476   -9.370  2.636   1.00 26.94  ? 60  PRO A CA  1 
ATOM   475  C C   . PRO A 1 61 ? 2.040   -10.066 3.874   1.00 26.65  ? 60  PRO A C   1 
ATOM   476  O O   . PRO A 1 61 ? 1.354   -10.250 4.859   1.00 25.26  ? 60  PRO A O   1 
ATOM   477  C CB  . PRO A 1 61 ? 1.203   -7.857  2.818   1.00 30.54  ? 60  PRO A CB  1 
ATOM   478  C CG  . PRO A 1 61 ? 0.190   -7.582  1.683   1.00 28.63  ? 60  PRO A CG  1 
ATOM   479  C CD  . PRO A 1 61 ? -0.791  -8.743  1.970   1.00 29.49  ? 60  PRO A CD  1 
ATOM   480  N N   . TYR A 1 62 ? 3.331   -10.463 3.826   1.00 25.57  ? 61  TYR A N   1 
ATOM   481  C CA  . TYR A 1 62 ? 3.893   -11.350 4.823   1.00 24.04  ? 61  TYR A CA  1 
ATOM   482  C C   . TYR A 1 62 ? 3.933   -10.682 6.211   1.00 24.60  ? 61  TYR A C   1 
ATOM   483  O O   . TYR A 1 62 ? 3.552   -11.316 7.187   1.00 26.98  ? 61  TYR A O   1 
ATOM   484  C CB  . TYR A 1 62 ? 5.326   -11.674 4.382   1.00 24.44  ? 61  TYR A CB  1 
ATOM   485  C CG  . TYR A 1 62 ? 6.082   -12.479 5.416   1.00 25.10  ? 61  TYR A CG  1 
ATOM   486  C CD1 . TYR A 1 62 ? 5.805   -13.829 5.664   1.00 27.10  ? 61  TYR A CD1 1 
ATOM   487  C CD2 . TYR A 1 62 ? 7.076   -11.858 6.173   1.00 32.21  ? 61  TYR A CD2 1 
ATOM   488  C CE1 . TYR A 1 62 ? 6.516   -14.562 6.608   1.00 27.69  ? 61  TYR A CE1 1 
ATOM   489  C CE2 . TYR A 1 62 ? 7.802   -12.589 7.098   1.00 31.57  ? 61  TYR A CE2 1 
ATOM   490  C CZ  . TYR A 1 62 ? 7.508   -13.918 7.329   1.00 30.59  ? 61  TYR A CZ  1 
ATOM   491  O OH  . TYR A 1 62 ? 8.251   -14.550 8.296   1.00 32.92  ? 61  TYR A OH  1 
ATOM   492  N N   . ASP A 1 63 ? 4.352   -9.419  6.270   1.00 27.82  ? 62  ASP A N   1 
ATOM   493  C CA  . ASP A 1 63 ? 4.538   -8.768  7.560   1.00 34.46  ? 62  ASP A CA  1 
ATOM   494  C C   . ASP A 1 63 ? 3.196   -8.706  8.294   1.00 33.89  ? 62  ASP A C   1 
ATOM   495  O O   . ASP A 1 63 ? 3.094   -9.185  9.430   1.00 38.70  ? 62  ASP A O   1 
ATOM   496  C CB  . ASP A 1 63 ? 5.281   -7.445  7.444   1.00 36.70  ? 62  ASP A CB  1 
ATOM   497  C CG  . ASP A 1 63 ? 6.326   -7.249  8.532   1.00 63.98  ? 62  ASP A CG  1 
ATOM   498  O OD1 . ASP A 1 63 ? 5.919   -7.133  9.718   1.00 63.56  ? 62  ASP A OD1 1 
ATOM   499  O OD2 . ASP A 1 63 ? 7.539   -7.273  8.195   1.00 74.76  ? 62  ASP A OD2 1 
ATOM   500  N N   . LYS A 1 64 ? 2.159   -8.201  7.612   1.00 34.80  ? 63  LYS A N   1 
ATOM   501  C CA  . LYS A 1 64 ? 0.824   -8.129  8.217   1.00 35.75  ? 63  LYS A CA  1 
ATOM   502  C C   . LYS A 1 64 ? 0.287   -9.500  8.650   1.00 34.43  ? 63  LYS A C   1 
ATOM   503  O O   . LYS A 1 64 ? -0.462  -9.563  9.623   1.00 30.64  ? 63  LYS A O   1 
ATOM   504  C CB  . LYS A 1 64 ? -0.164  -7.431  7.268   1.00 37.01  ? 63  LYS A CB  1 
ATOM   505  C CG  . LYS A 1 64 ? -1.646  -7.372  7.703   1.00 39.43  ? 63  LYS A CG  1 
ATOM   506  C CD  . LYS A 1 64 ? -2.473  -6.472  6.784   1.00 39.42  ? 63  LYS A CD  1 
ATOM   507  C CE  . LYS A 1 64 ? -3.663  -5.864  7.471   1.00 42.66  ? 63  LYS A CE  1 
ATOM   508  N NZ  . LYS A 1 64 ? -4.746  -6.839  7.418   1.00 55.91  ? 63  LYS A NZ  1 
ATOM   509  N N   . SER A 1 65 ? 0.639   -10.604 7.952   1.00 30.08  ? 64  SER A N   1 
ATOM   510  C CA  . SER A 1 65 ? -0.110  -11.856 8.069   1.00 28.62  ? 64  SER A CA  1 
ATOM   511  C C   . SER A 1 65 ? 0.630   -12.942 8.854   1.00 29.86  ? 64  SER A C   1 
ATOM   512  O O   . SER A 1 65 ? 0.071   -14.032 9.016   1.00 31.80  ? 64  SER A O   1 
ATOM   513  C CB  . SER A 1 65 ? -0.446  -12.443 6.684   1.00 30.81  ? 64  SER A CB  1 
ATOM   514  O OG  . SER A 1 65 ? -1.372  -11.598 6.016   1.00 38.32  ? 64  SER A OG  1 
ATOM   515  N N   . LYS A 1 66 ? 1.911   -12.710 9.187   1.00 30.28  ? 65  LYS A N   1 
ATOM   516  C CA  . LYS A 1 66 ? 2.751   -13.807 9.688   1.00 31.75  ? 65  LYS A CA  1 
ATOM   517  C C   . LYS A 1 66 ? 2.277   -14.328 11.049  1.00 33.13  ? 65  LYS A C   1 
ATOM   518  O O   . LYS A 1 66 ? 2.430   -15.525 11.362  1.00 32.94  ? 65  LYS A O   1 
ATOM   519  C CB  . LYS A 1 66 ? 4.264   -13.523 9.686   1.00 33.58  ? 65  LYS A CB  1 
ATOM   520  C CG  . LYS A 1 66 ? 4.651   -12.281 10.437  1.00 32.86  ? 65  LYS A CG  1 
ATOM   521  C CD  . LYS A 1 66 ? 6.163   -12.104 10.452  1.00 48.93  ? 65  LYS A CD  1 
ATOM   522  C CE  . LYS A 1 66 ? 6.546   -10.899 11.266  1.00 50.68  ? 65  LYS A CE  1 
ATOM   523  N NZ  . LYS A 1 66 ? 6.395   -9.651  10.504  1.00 55.89  ? 65  LYS A NZ  1 
ATOM   524  N N   A ASP A 1 67 ? 1.678   -13.439 11.854  0.50 34.11  ? 66  ASP A N   1 
ATOM   525  N N   B ASP A 1 67 ? 1.717   -13.428 11.867  0.50 33.65  ? 66  ASP A N   1 
ATOM   526  C CA  A ASP A 1 67 ? 1.210   -13.825 13.178  0.50 36.15  ? 66  ASP A CA  1 
ATOM   527  C CA  B ASP A 1 67 ? 1.220   -13.852 13.165  0.50 34.87  ? 66  ASP A CA  1 
ATOM   528  C C   A ASP A 1 67 ? 0.061   -14.827 13.060  0.50 37.47  ? 66  ASP A C   1 
ATOM   529  C C   B ASP A 1 67 ? 0.194   -14.962 12.951  0.50 36.50  ? 66  ASP A C   1 
ATOM   530  O O   A ASP A 1 67 ? -0.139  -15.662 13.929  0.50 38.95  ? 66  ASP A O   1 
ATOM   531  O O   B ASP A 1 67 ? 0.242   -15.994 13.612  0.50 34.56  ? 66  ASP A O   1 
ATOM   532  C CB  A ASP A 1 67 ? 0.879   -12.615 14.039  0.50 38.29  ? 66  ASP A CB  1 
ATOM   533  C CB  B ASP A 1 67 ? 0.651   -12.697 13.975  0.50 36.72  ? 66  ASP A CB  1 
ATOM   534  C CG  A ASP A 1 67 ? 2.075   -11.903 14.655  0.50 42.51  ? 66  ASP A CG  1 
ATOM   535  C CG  B ASP A 1 67 ? 0.121   -13.076 15.351  0.50 38.69  ? 66  ASP A CG  1 
ATOM   536  O OD1 A ASP A 1 67 ? 3.171   -12.503 14.667  0.50 43.94  ? 66  ASP A OD1 1 
ATOM   537  O OD1 B ASP A 1 67 ? 0.957   -13.289 16.254  0.50 40.23  ? 66  ASP A OD1 1 
ATOM   538  O OD2 A ASP A 1 67 ? 1.911   -10.749 15.095  0.50 43.09  ? 66  ASP A OD2 1 
ATOM   539  O OD2 B ASP A 1 67 ? -1.122  -13.198 15.496  0.50 42.18  ? 66  ASP A OD2 1 
ATOM   540  N N   . LYS A 1 68 ? -0.673  -14.766 11.950  1.00 32.95  ? 67  LYS A N   1 
ATOM   541  C CA  . LYS A 1 68 ? -1.800  -15.647 11.713  1.00 33.55  ? 67  LYS A CA  1 
ATOM   542  C C   . LYS A 1 68 ? -1.376  -16.891 10.951  1.00 34.80  ? 67  LYS A C   1 
ATOM   543  O O   . LYS A 1 68 ? -1.930  -17.961 11.199  1.00 37.84  ? 67  LYS A O   1 
ATOM   544  C CB  . LYS A 1 68 ? -2.852  -14.903 10.893  1.00 32.71  ? 67  LYS A CB  1 
ATOM   545  C CG  . LYS A 1 68 ? -4.159  -15.670 10.735  1.00 35.24  ? 67  LYS A CG  1 
ATOM   546  C CD  . LYS A 1 68 ? -5.188  -14.752 10.069  1.00 41.85  ? 67  LYS A CD  1 
ATOM   547  C CE  . LYS A 1 68 ? -6.555  -15.342 9.902   1.00 47.82  ? 67  LYS A CE  1 
ATOM   548  N NZ  . LYS A 1 68 ? -7.502  -14.314 9.446   1.00 48.42  ? 67  LYS A NZ  1 
ATOM   549  N N   . TYR A 1 69 ? -0.475  -16.750 9.966   1.00 31.82  ? 68  TYR A N   1 
ATOM   550  C CA  . TYR A 1 69 ? -0.285  -17.849 9.024   1.00 28.43  ? 68  TYR A CA  1 
ATOM   551  C C   . TYR A 1 69 ? 1.094   -18.496 9.183   1.00 28.97  ? 68  TYR A C   1 
ATOM   552  O O   . TYR A 1 69 ? 1.343   -19.565 8.633   1.00 31.54  ? 68  TYR A O   1 
ATOM   553  C CB  . TYR A 1 69 ? -0.411  -17.365 7.570   1.00 28.03  ? 68  TYR A CB  1 
ATOM   554  C CG  . TYR A 1 69 ? -1.804  -16.904 7.163   1.00 29.02  ? 68  TYR A CG  1 
ATOM   555  C CD1 . TYR A 1 69 ? -2.944  -17.617 7.557   1.00 28.56  ? 68  TYR A CD1 1 
ATOM   556  C CD2 . TYR A 1 69 ? -1.972  -15.733 6.414   1.00 29.98  ? 68  TYR A CD2 1 
ATOM   557  C CE1 . TYR A 1 69 ? -4.213  -17.185 7.198   1.00 28.74  ? 68  TYR A CE1 1 
ATOM   558  C CE2 . TYR A 1 69 ? -3.237  -15.299 6.044   1.00 30.38  ? 68  TYR A CE2 1 
ATOM   559  C CZ  . TYR A 1 69 ? -4.348  -16.023 6.456   1.00 28.14  ? 68  TYR A CZ  1 
ATOM   560  O OH  . TYR A 1 69 ? -5.577  -15.605 6.063   1.00 30.78  ? 68  TYR A OH  1 
ATOM   561  N N   . GLY A 1 70 ? 1.972   -17.854 9.931   1.00 29.23  ? 69  GLY A N   1 
ATOM   562  C CA  . GLY A 1 70 ? 3.349   -18.334 9.989   1.00 31.39  ? 69  GLY A CA  1 
ATOM   563  C C   . GLY A 1 70 ? 3.575   -19.287 11.171  1.00 33.17  ? 69  GLY A C   1 
ATOM   564  O O   . GLY A 1 70 ? 4.408   -19.019 12.008  1.00 37.16  ? 69  GLY A O   1 
ATOM   565  N N   . LYS A 1 71 ? 2.850   -20.399 11.205  1.00 35.37  ? 70  LYS A N   1 
ATOM   566  C CA  . LYS A 1 71 ? 2.985   -21.402 12.250  1.00 41.23  ? 70  LYS A CA  1 
ATOM   567  C C   . LYS A 1 71 ? 3.312   -22.711 11.547  1.00 39.59  ? 70  LYS A C   1 
ATOM   568  O O   . LYS A 1 71 ? 2.955   -22.883 10.381  1.00 37.71  ? 70  LYS A O   1 
ATOM   569  C CB  . LYS A 1 71 ? 1.708   -21.508 13.095  1.00 39.70  ? 70  LYS A CB  1 
ATOM   570  C CG  . LYS A 1 71 ? 1.474   -20.215 13.894  1.00 44.09  ? 70  LYS A CG  1 
ATOM   571  C CD  . LYS A 1 71 ? 0.666   -20.362 15.176  1.00 48.28  ? 70  LYS A CD  1 
ATOM   572  N N   . PRO A 1 72 ? 4.046   -23.651 12.180  1.00 40.36  ? 71  PRO A N   1 
ATOM   573  C CA  . PRO A 1 72 ? 4.335   -24.933 11.528  1.00 38.08  ? 71  PRO A CA  1 
ATOM   574  C C   . PRO A 1 72 ? 3.082   -25.673 11.083  1.00 37.47  ? 71  PRO A C   1 
ATOM   575  O O   . PRO A 1 72 ? 2.027   -25.535 11.687  1.00 43.80  ? 71  PRO A O   1 
ATOM   576  C CB  . PRO A 1 72 ? 5.157   -25.732 12.565  1.00 41.92  ? 71  PRO A CB  1 
ATOM   577  C CG  . PRO A 1 72 ? 5.698   -24.669 13.505  1.00 45.08  ? 71  PRO A CG  1 
ATOM   578  C CD  . PRO A 1 72 ? 4.693   -23.498 13.493  1.00 42.74  ? 71  PRO A CD  1 
ATOM   579  N N   . ASN A 1 73 ? 3.219   -26.460 10.021  1.00 39.35  ? 72  ASN A N   1 
ATOM   580  C CA  . ASN A 1 73 ? 2.114   -27.148 9.382   1.00 46.26  ? 72  ASN A CA  1 
ATOM   581  C C   . ASN A 1 73 ? 2.689   -28.486 8.947   1.00 51.86  ? 72  ASN A C   1 
ATOM   582  O O   . ASN A 1 73 ? 3.885   -28.585 8.691   1.00 55.09  ? 72  ASN A O   1 
ATOM   583  C CB  . ASN A 1 73 ? 1.553   -26.284 8.248   1.00 47.63  ? 72  ASN A CB  1 
ATOM   584  C CG  . ASN A 1 73 ? 0.247   -26.776 7.660   1.00 58.55  ? 72  ASN A CG  1 
ATOM   585  O OD1 . ASN A 1 73 ? 0.240   -27.608 6.749   1.00 56.30  ? 72  ASN A OD1 1 
ATOM   586  N ND2 . ASN A 1 73 ? -0.872  -26.222 8.105   1.00 61.94  ? 72  ASN A ND2 1 
ATOM   587  N N   . LYS A 1 74 ? 1.836   -29.506 8.877   1.00 50.86  ? 73  LYS A N   1 
ATOM   588  C CA  . LYS A 1 74 ? 2.262   -30.864 8.583   1.00 50.60  ? 73  LYS A CA  1 
ATOM   589  C C   . LYS A 1 74 ? 2.669   -31.016 7.111   1.00 48.69  ? 73  LYS A C   1 
ATOM   590  O O   . LYS A 1 74 ? 3.413   -31.933 6.753   1.00 49.03  ? 73  LYS A O   1 
ATOM   591  C CB  . LYS A 1 74 ? 1.105   -31.759 9.064   1.00 50.94  ? 73  LYS A CB  1 
ATOM   592  C CG  . LYS A 1 74 ? -0.056  -31.960 8.081   1.00 55.38  ? 73  LYS A CG  1 
ATOM   593  N N   . ARG A 1 75 ? 2.204   -30.101 6.248   1.00 45.89  ? 74  ARG A N   1 
ATOM   594  C CA  . ARG A 1 75 ? 2.277   -30.292 4.807   1.00 43.31  ? 74  ARG A CA  1 
ATOM   595  C C   . ARG A 1 75 ? 3.719   -30.272 4.293   1.00 38.59  ? 74  ARG A C   1 
ATOM   596  O O   . ARG A 1 75 ? 4.543   -29.493 4.782   1.00 35.77  ? 74  ARG A O   1 
ATOM   597  C CB  . ARG A 1 75 ? 1.392   -29.249 4.113   1.00 43.50  ? 74  ARG A CB  1 
ATOM   598  C CG  . ARG A 1 75 ? -0.071  -29.550 4.404   1.00 53.61  ? 74  ARG A CG  1 
ATOM   599  C CD  . ARG A 1 75 ? -0.633  -30.694 3.561   1.00 45.76  ? 74  ARG A CD  1 
ATOM   600  N NE  . ARG A 1 75 ? -1.588  -30.195 2.569   1.00 64.27  ? 74  ARG A NE  1 
ATOM   601  C CZ  . ARG A 1 75 ? -2.692  -29.500 2.884   1.00 64.25  ? 74  ARG A CZ  1 
ATOM   602  N NH1 . ARG A 1 75 ? -3.493  -29.081 1.923   1.00 60.14  ? 74  ARG A NH1 1 
ATOM   603  N NH2 . ARG A 1 75 ? -2.994  -29.229 4.150   1.00 67.42  ? 74  ARG A NH2 1 
ATOM   604  N N   . LYS A 1 76 ? 3.986   -31.105 3.273   1.00 39.17  ? 75  LYS A N   1 
ATOM   605  C CA  . LYS A 1 76 ? 5.318   -31.253 2.700   1.00 38.10  ? 75  LYS A CA  1 
ATOM   606  C C   . LYS A 1 76 ? 5.851   -29.879 2.284   1.00 37.49  ? 75  LYS A C   1 
ATOM   607  O O   . LYS A 1 76 ? 5.274   -29.221 1.417   1.00 33.13  ? 75  LYS A O   1 
ATOM   608  C CB  . LYS A 1 76 ? 5.323   -32.173 1.474   1.00 37.79  ? 75  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 76 ? 6.693   -32.551 0.927   1.00 45.41  ? 75  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 76 ? 6.698   -33.601 -0.187  1.00 49.23  ? 75  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 76 ? 8.120   -33.976 -0.525  1.00 50.17  ? 75  LYS A CE  1 
ATOM   612  N N   . GLY A 1 77 ? 6.977   -29.473 2.881   1.00 35.92  ? 76  GLY A N   1 
ATOM   613  C CA  . GLY A 1 77 ? 7.720   -28.328 2.367   1.00 32.22  ? 76  GLY A CA  1 
ATOM   614  C C   . GLY A 1 77 ? 7.434   -27.067 3.173   1.00 32.35  ? 76  GLY A C   1 
ATOM   615  O O   . GLY A 1 77 ? 8.198   -26.105 3.094   1.00 33.23  ? 76  GLY A O   1 
ATOM   616  N N   . PHE A 1 78 ? 6.380   -27.109 3.986   1.00 30.94  ? 77  PHE A N   1 
ATOM   617  C CA  . PHE A 1 78 ? 5.863   -25.924 4.643   1.00 33.38  ? 77  PHE A CA  1 
ATOM   618  C C   . PHE A 1 78 ? 6.873   -25.305 5.618   1.00 37.33  ? 77  PHE A C   1 
ATOM   619  O O   . PHE A 1 78 ? 7.111   -24.094 5.612   1.00 32.86  ? 77  PHE A O   1 
ATOM   620  C CB  . PHE A 1 78 ? 4.477   -26.195 5.232   1.00 32.88  ? 77  PHE A CB  1 
ATOM   621  C CG  . PHE A 1 78 ? 3.760   -24.913 5.623   1.00 32.83  ? 77  PHE A CG  1 
ATOM   622  C CD1 . PHE A 1 78 ? 4.063   -24.260 6.813   1.00 34.76  ? 77  PHE A CD1 1 
ATOM   623  C CD2 . PHE A 1 78 ? 2.792   -24.359 4.781   1.00 32.60  ? 77  PHE A CD2 1 
ATOM   624  C CE1 . PHE A 1 78 ? 3.425   -23.079 7.151   1.00 35.85  ? 77  PHE A CE1 1 
ATOM   625  C CE2 . PHE A 1 78 ? 2.159   -23.166 5.121   1.00 29.84  ? 77  PHE A CE2 1 
ATOM   626  C CZ  . PHE A 1 78 ? 2.462   -22.544 6.317   1.00 28.25  ? 77  PHE A CZ  1 
ATOM   627  N N   . ASN A 1 79 ? 7.411   -26.134 6.517   1.00 31.59  ? 78  ASN A N   1 
ATOM   628  C CA  . ASN A 1 79 ? 8.319   -25.674 7.559   1.00 34.08  ? 78  ASN A CA  1 
ATOM   629  C C   . ASN A 1 79 ? 9.644   -25.191 6.954   1.00 27.67  ? 78  ASN A C   1 
ATOM   630  O O   . ASN A 1 79 ? 10.231  -24.212 7.437   1.00 28.71  ? 78  ASN A O   1 
ATOM   631  C CB  . ASN A 1 79 ? 8.439   -26.771 8.620   1.00 33.22  ? 78  ASN A CB  1 
ATOM   632  C CG  . ASN A 1 79 ? 7.092   -27.006 9.278   1.00 40.78  ? 78  ASN A CG  1 
ATOM   633  O OD1 . ASN A 1 79 ? 6.180   -26.181 9.132   1.00 35.50  ? 78  ASN A OD1 1 
ATOM   634  N ND2 . ASN A 1 79 ? 6.944   -28.096 10.031  1.00 34.51  ? 78  ASN A ND2 1 
ATOM   635  N N   . GLU A 1 80 ? 10.127  -25.900 5.926   1.00 26.82  ? 79  GLU A N   1 
ATOM   636  C CA  . GLU A 1 80 ? 11.294  -25.430 5.198   1.00 29.17  ? 79  GLU A CA  1 
ATOM   637  C C   . GLU A 1 80 ? 10.966  -24.047 4.643   1.00 28.55  ? 79  GLU A C   1 
ATOM   638  O O   . GLU A 1 80 ? 11.794  -23.129 4.670   1.00 25.97  ? 79  GLU A O   1 
ATOM   639  C CB  . GLU A 1 80 ? 11.678  -26.323 4.009   1.00 30.46  ? 79  GLU A CB  1 
ATOM   640  C CG  . GLU A 1 80 ? 12.996  -25.924 3.342   1.00 32.85  ? 79  GLU A CG  1 
ATOM   641  C CD  . GLU A 1 80 ? 13.516  -26.946 2.325   1.00 44.72  ? 79  GLU A CD  1 
ATOM   642  O OE1 . GLU A 1 80 ? 12.858  -27.975 2.074   1.00 45.74  ? 79  GLU A OE1 1 
ATOM   643  O OE2 . GLU A 1 80 ? 14.595  -26.724 1.765   1.00 42.38  ? 79  GLU A OE2 1 
ATOM   644  N N   . GLY A 1 81 ? 9.738   -23.927 4.129   1.00 27.25  ? 80  GLY A N   1 
ATOM   645  C CA  . GLY A 1 81 ? 9.326   -22.654 3.551   1.00 28.92  ? 80  GLY A CA  1 
ATOM   646  C C   . GLY A 1 81 ? 9.336   -21.532 4.589   1.00 25.46  ? 80  GLY A C   1 
ATOM   647  O O   . GLY A 1 81 ? 9.652   -20.393 4.243   1.00 26.25  ? 80  GLY A O   1 
ATOM   648  N N   . LEU A 1 82 ? 8.942   -21.820 5.847   1.00 23.40  ? 81  LEU A N   1 
ATOM   649  C CA  . LEU A 1 82 ? 8.954   -20.780 6.861   1.00 24.18  ? 81  LEU A CA  1 
ATOM   650  C C   . LEU A 1 82 ? 10.384  -20.301 7.131   1.00 26.91  ? 81  LEU A C   1 
ATOM   651  O O   . LEU A 1 82 ? 10.601  -19.118 7.440   1.00 24.18  ? 81  LEU A O   1 
ATOM   652  C CB  . LEU A 1 82 ? 8.299   -21.266 8.159   1.00 26.72  ? 81  LEU A CB  1 
ATOM   653  C CG  . LEU A 1 82 ? 6.809   -21.615 8.050   1.00 29.31  ? 81  LEU A CG  1 
ATOM   654  C CD1 . LEU A 1 82 ? 6.453   -22.231 9.398   1.00 34.10  ? 81  LEU A CD1 1 
ATOM   655  C CD2 . LEU A 1 82 ? 5.812   -20.481 7.750   1.00 28.44  ? 81  LEU A CD2 1 
ATOM   656  N N   . TRP A 1 83 ? 11.352  -21.236 7.012   1.00 25.91  ? 82  TRP A N   1 
ATOM   657  C CA  . TRP A 1 83 ? 12.722  -20.876 7.342   1.00 26.00  ? 82  TRP A CA  1 
ATOM   658  C C   . TRP A 1 83 ? 13.210  -19.948 6.233   1.00 23.65  ? 82  TRP A C   1 
ATOM   659  O O   . TRP A 1 83 ? 13.885  -18.962 6.491   1.00 26.93  ? 82  TRP A O   1 
ATOM   660  C CB  . TRP A 1 83 ? 13.618  -22.130 7.523   1.00 26.73  ? 82  TRP A CB  1 
ATOM   661  C CG  . TRP A 1 83 ? 15.081  -21.805 7.771   1.00 29.00  ? 82  TRP A CG  1 
ATOM   662  C CD1 . TRP A 1 83 ? 15.727  -21.672 8.969   1.00 27.30  ? 82  TRP A CD1 1 
ATOM   663  C CD2 . TRP A 1 83 ? 16.052  -21.486 6.765   1.00 26.92  ? 82  TRP A CD2 1 
ATOM   664  N NE1 . TRP A 1 83 ? 17.032  -21.316 8.772   1.00 28.67  ? 82  TRP A NE1 1 
ATOM   665  C CE2 . TRP A 1 83 ? 17.250  -21.168 7.429   1.00 29.32  ? 82  TRP A CE2 1 
ATOM   666  C CE3 . TRP A 1 83 ? 16.003  -21.428 5.363   1.00 28.22  ? 82  TRP A CE3 1 
ATOM   667  C CZ2 . TRP A 1 83 ? 18.408  -20.817 6.738   1.00 27.99  ? 82  TRP A CZ2 1 
ATOM   668  C CZ3 . TRP A 1 83 ? 17.137  -21.055 4.682   1.00 31.10  ? 82  TRP A CZ3 1 
ATOM   669  C CH2 . TRP A 1 83 ? 18.326  -20.774 5.365   1.00 30.91  ? 82  TRP A CH2 1 
ATOM   670  N N   . GLU A 1 84 ? 12.873  -20.320 4.986   1.00 23.38  ? 83  GLU A N   1 
ATOM   671  C CA  . GLU A 1 84 ? 13.327  -19.589 3.821   1.00 22.50  ? 83  GLU A CA  1 
ATOM   672  C C   . GLU A 1 84 ? 12.814  -18.155 3.881   1.00 24.40  ? 83  GLU A C   1 
ATOM   673  O O   . GLU A 1 84 ? 13.575  -17.214 3.712   1.00 21.84  ? 83  GLU A O   1 
ATOM   674  C CB  . GLU A 1 84 ? 12.924  -20.287 2.521   1.00 23.47  ? 83  GLU A CB  1 
ATOM   675  C CG  . GLU A 1 84 ? 13.617  -21.644 2.383   1.00 25.37  ? 83  GLU A CG  1 
ATOM   676  C CD  . GLU A 1 84 ? 13.228  -22.395 1.114   1.00 30.26  ? 83  GLU A CD  1 
ATOM   677  O OE1 . GLU A 1 84 ? 12.287  -21.932 0.455   1.00 28.71  ? 83  GLU A OE1 1 
ATOM   678  O OE2 . GLU A 1 84 ? 13.877  -23.430 0.760   1.00 31.16  ? 83  GLU A OE2 1 
ATOM   679  N N   . ILE A 1 85 ? 11.505  -17.997 4.117   1.00 21.95  ? 84  ILE A N   1 
ATOM   680  C CA  . ILE A 1 85 ? 10.956  -16.656 4.011   1.00 22.92  ? 84  ILE A CA  1 
ATOM   681  C C   . ILE A 1 85 ? 11.526  -15.763 5.125   1.00 24.72  ? 84  ILE A C   1 
ATOM   682  O O   . ILE A 1 85 ? 11.696  -14.557 4.942   1.00 23.86  ? 84  ILE A O   1 
ATOM   683  C CB  . ILE A 1 85 ? 9.408   -16.697 4.033   1.00 19.51  ? 84  ILE A CB  1 
ATOM   684  C CG1 . ILE A 1 85 ? 8.850   -15.313 3.574   1.00 21.90  ? 84  ILE A CG1 1 
ATOM   685  C CG2 . ILE A 1 85 ? 8.861   -17.068 5.414   1.00 21.73  ? 84  ILE A CG2 1 
ATOM   686  C CD1 . ILE A 1 85 ? 7.365   -15.358 3.119   1.00 21.48  ? 84  ILE A CD1 1 
ATOM   687  N N   . GLN A 1 86 ? 11.891  -16.368 6.274   1.00 24.29  ? 85  GLN A N   1 
ATOM   688  C CA  . GLN A 1 86 ? 12.381  -15.585 7.409   1.00 26.77  ? 85  GLN A CA  1 
ATOM   689  C C   . GLN A 1 86 ? 13.876  -15.295 7.255   1.00 26.51  ? 85  GLN A C   1 
ATOM   690  O O   . GLN A 1 86 ? 14.312  -14.198 7.623   1.00 29.45  ? 85  GLN A O   1 
ATOM   691  C CB  . GLN A 1 86 ? 12.106  -16.343 8.719   1.00 27.75  ? 85  GLN A CB  1 
ATOM   692  C CG  . GLN A 1 86 ? 12.475  -15.581 9.988   1.00 35.04  ? 85  GLN A CG  1 
ATOM   693  C CD  . GLN A 1 86 ? 11.863  -16.197 11.239  1.00 46.00  ? 85  GLN A CD  1 
ATOM   694  O OE1 . GLN A 1 86 ? 11.708  -17.426 11.370  1.00 37.53  ? 85  GLN A OE1 1 
ATOM   695  N NE2 . GLN A 1 86 ? 11.484  -15.324 12.168  1.00 48.35  ? 85  GLN A NE2 1 
ATOM   696  N N   . ASN A 1 87 ? 14.625  -16.242 6.672   1.00 23.16  ? 86  ASN A N   1 
ATOM   697  C CA  . ASN A 1 87 ? 16.083  -16.252 6.765   1.00 23.56  ? 86  ASN A CA  1 
ATOM   698  C C   . ASN A 1 87 ? 16.811  -15.881 5.472   1.00 25.46  ? 86  ASN A C   1 
ATOM   699  O O   . ASN A 1 87 ? 17.943  -15.369 5.546   1.00 28.11  ? 86  ASN A O   1 
ATOM   700  C CB  . ASN A 1 87 ? 16.606  -17.529 7.438   1.00 25.30  ? 86  ASN A CB  1 
ATOM   701  C CG  . ASN A 1 87 ? 16.129  -17.636 8.872   1.00 27.55  ? 86  ASN A CG  1 
ATOM   702  O OD1 . ASN A 1 87 ? 16.466  -16.780 9.704   1.00 31.16  ? 86  ASN A OD1 1 
ATOM   703  N ND2 . ASN A 1 87 ? 15.216  -18.561 9.163   1.00 27.52  ? 86  ASN A ND2 1 
ATOM   704  N N   . ASN A 1 88 ? 16.287  -16.263 4.288   1.00 24.71  ? 87  ASN A N   1 
ATOM   705  C CA  . ASN A 1 88 ? 16.917  -15.901 3.025   1.00 25.83  ? 87  ASN A CA  1 
ATOM   706  C C   . ASN A 1 88 ? 15.836  -15.811 1.938   1.00 25.44  ? 87  ASN A C   1 
ATOM   707  O O   . ASN A 1 88 ? 15.847  -16.577 0.963   1.00 23.96  ? 87  ASN A O   1 
ATOM   708  C CB  . ASN A 1 88 ? 18.120  -16.811 2.700   1.00 26.60  ? 87  ASN A CB  1 
ATOM   709  C CG  . ASN A 1 88 ? 19.147  -16.175 1.796   1.00 31.02  ? 87  ASN A CG  1 
ATOM   710  O OD1 . ASN A 1 88 ? 18.863  -15.200 1.088   1.00 26.18  ? 87  ASN A OD1 1 
ATOM   711  N ND2 . ASN A 1 88 ? 20.375  -16.707 1.779   1.00 28.82  ? 87  ASN A ND2 1 
ATOM   712  N N   . PRO A 1 89 ? 14.852  -14.886 2.083   1.00 23.67  ? 88  PRO A N   1 
ATOM   713  C CA  . PRO A 1 89 ? 13.732  -14.826 1.140   1.00 22.74  ? 88  PRO A CA  1 
ATOM   714  C C   . PRO A 1 89 ? 14.102  -14.398 -0.285  1.00 25.74  ? 88  PRO A C   1 
ATOM   715  O O   . PRO A 1 89 ? 13.336  -14.610 -1.202  1.00 22.52  ? 88  PRO A O   1 
ATOM   716  C CB  . PRO A 1 89 ? 12.779  -13.847 1.834   1.00 22.90  ? 88  PRO A CB  1 
ATOM   717  C CG  . PRO A 1 89 ? 13.696  -12.901 2.611   1.00 22.34  ? 88  PRO A CG  1 
ATOM   718  C CD  . PRO A 1 89 ? 14.784  -13.852 3.147   1.00 19.93  ? 88  PRO A CD  1 
ATOM   719  N N   . HIS A 1 90 ? 15.286  -13.825 -0.508  1.00 22.17  ? 89  HIS A N   1 
ATOM   720  C CA  . HIS A 1 90 ? 15.621  -13.306 -1.825  1.00 21.94  ? 89  HIS A CA  1 
ATOM   721  C C   . HIS A 1 90 ? 16.748  -14.114 -2.493  1.00 24.47  ? 89  HIS A C   1 
ATOM   722  O O   . HIS A 1 90 ? 17.298  -13.651 -3.495  1.00 23.62  ? 89  HIS A O   1 
ATOM   723  C CB  . HIS A 1 90 ? 16.029  -11.833 -1.680  1.00 23.18  ? 89  HIS A CB  1 
ATOM   724  C CG  . HIS A 1 90 ? 14.970  -10.985 -1.046  1.00 23.77  ? 89  HIS A CG  1 
ATOM   725  N ND1 . HIS A 1 90 ? 13.708  -10.890 -1.600  1.00 24.00  ? 89  HIS A ND1 1 
ATOM   726  C CD2 . HIS A 1 90 ? 14.949  -10.229 0.045   1.00 21.75  ? 89  HIS A CD2 1 
ATOM   727  C CE1 . HIS A 1 90 ? 12.980  -10.033 -0.898  1.00 23.44  ? 89  HIS A CE1 1 
ATOM   728  N NE2 . HIS A 1 90 ? 13.712  -9.622  0.113   1.00 25.47  ? 89  HIS A NE2 1 
ATOM   729  N N   . ALA A 1 91 ? 16.999  -15.337 -1.991  1.00 22.74  ? 90  ALA A N   1 
ATOM   730  C CA  . ALA A 1 91 ? 18.114  -16.128 -2.487  1.00 27.40  ? 90  ALA A CA  1 
ATOM   731  C C   . ALA A 1 91 ? 17.659  -16.875 -3.733  1.00 31.10  ? 90  ALA A C   1 
ATOM   732  O O   . ALA A 1 91 ? 16.459  -17.004 -3.997  1.00 26.22  ? 90  ALA A O   1 
ATOM   733  C CB  . ALA A 1 91 ? 18.603  -17.100 -1.449  1.00 25.86  ? 90  ALA A CB  1 
ATOM   734  N N   . SER A 1 92 ? 18.651  -17.385 -4.476  1.00 28.42  ? 91  SER A N   1 
ATOM   735  C CA  . SER A 1 92 ? 18.363  -18.284 -5.584  1.00 32.54  ? 91  SER A CA  1 
ATOM   736  C C   . SER A 1 92 ? 18.048  -19.663 -5.020  1.00 32.54  ? 91  SER A C   1 
ATOM   737  O O   . SER A 1 92 ? 18.825  -20.197 -4.210  1.00 34.04  ? 91  SER A O   1 
ATOM   738  C CB  . SER A 1 92 ? 19.534  -18.325 -6.533  1.00 38.65  ? 91  SER A CB  1 
ATOM   739  O OG  . SER A 1 92 ? 19.287  -19.312 -7.522  1.00 43.02  ? 91  SER A OG  1 
ATOM   740  N N   . TYR A 1 93 ? 16.885  -20.219 -5.404  1.00 29.67  ? 92  TYR A N   1 
ATOM   741  C CA  . TYR A 1 93 ? 16.521  -21.544 -4.932  1.00 32.04  ? 92  TYR A CA  1 
ATOM   742  C C   . TYR A 1 93 ? 16.452  -22.516 -6.111  1.00 37.78  ? 92  TYR A C   1 
ATOM   743  O O   . TYR A 1 93 ? 16.004  -23.639 -5.934  1.00 49.03  ? 92  TYR A O   1 
ATOM   744  C CB  . TYR A 1 93 ? 15.194  -21.562 -4.162  1.00 30.73  ? 92  TYR A CB  1 
ATOM   745  C CG  . TYR A 1 93 ? 15.320  -20.980 -2.763  1.00 29.46  ? 92  TYR A CG  1 
ATOM   746  C CD1 . TYR A 1 93 ? 15.777  -21.757 -1.695  1.00 31.18  ? 92  TYR A CD1 1 
ATOM   747  C CD2 . TYR A 1 93 ? 15.017  -19.641 -2.526  1.00 28.95  ? 92  TYR A CD2 1 
ATOM   748  C CE1 . TYR A 1 93 ? 15.943  -21.214 -0.426  1.00 33.90  ? 92  TYR A CE1 1 
ATOM   749  C CE2 . TYR A 1 93 ? 15.161  -19.106 -1.266  1.00 26.72  ? 92  TYR A CE2 1 
ATOM   750  C CZ  . TYR A 1 93 ? 15.620  -19.881 -0.219  1.00 29.97  ? 92  TYR A CZ  1 
ATOM   751  O OH  . TYR A 1 93 ? 15.799  -19.330 1.015   1.00 30.67  ? 92  TYR A OH  1 
ATOM   752  N N   . SER A 1 94 ? 16.906  -22.076 -7.288  1.00 49.72  ? 93  SER A N   1 
ATOM   753  C CA  . SER A 1 94 ? 17.148  -22.945 -8.435  1.00 64.53  ? 93  SER A CA  1 
ATOM   754  C C   . SER A 1 94 ? 17.947  -24.185 -7.990  1.00 72.26  ? 93  SER A C   1 
ATOM   755  O O   . SER A 1 94 ? 19.148  -24.009 -7.652  1.00 68.66  ? 93  SER A O   1 
ATOM   756  C CB  . SER A 1 94 ? 17.887  -22.195 -9.530  1.00 65.38  ? 93  SER A CB  1 
ATOM   757  O OG  . SER A 1 94 ? 17.307  -20.922 -9.777  1.00 74.26  ? 93  SER A OG  1 
ATOM   758  O OXT . SER A 1 94 ? 17.345  -25.288 -7.974  1.00 77.13  ? 93  SER A OXT 1 
ATOM   759  N N   . MET B 1 2  ? 38.873  -11.167 -42.234 1.00 58.31  ? 1   MET B N   1 
ATOM   760  C CA  . MET B 1 2  ? 38.456  -12.180 -43.238 1.00 57.54  ? 1   MET B CA  1 
ATOM   761  C C   . MET B 1 2  ? 36.929  -12.245 -43.259 1.00 53.84  ? 1   MET B C   1 
ATOM   762  O O   . MET B 1 2  ? 36.315  -12.434 -42.208 1.00 57.69  ? 1   MET B O   1 
ATOM   763  C CB  . MET B 1 2  ? 39.080  -13.547 -42.920 1.00 68.72  ? 1   MET B CB  1 
ATOM   764  C CG  . MET B 1 2  ? 39.102  -14.542 -44.078 1.00 86.08  ? 1   MET B CG  1 
ATOM   765  S SD  . MET B 1 2  ? 39.868  -13.969 -45.613 1.00 99.00  ? 1   MET B SD  1 
ATOM   766  C CE  . MET B 1 2  ? 41.280  -12.995 -45.065 1.00 69.77  ? 1   MET B CE  1 
ATOM   767  N N   . PRO B 1 3  ? 36.265  -12.043 -44.429 1.00 49.13  ? 2   PRO B N   1 
ATOM   768  C CA  . PRO B 1 3  ? 34.811  -12.205 -44.518 1.00 47.34  ? 2   PRO B CA  1 
ATOM   769  C C   . PRO B 1 3  ? 34.478  -13.644 -44.133 1.00 48.52  ? 2   PRO B C   1 
ATOM   770  O O   . PRO B 1 3  ? 35.253  -14.543 -44.422 1.00 43.74  ? 2   PRO B O   1 
ATOM   771  C CB  . PRO B 1 3  ? 34.485  -11.882 -45.977 1.00 50.13  ? 2   PRO B CB  1 
ATOM   772  C CG  . PRO B 1 3  ? 35.661  -11.032 -46.436 1.00 46.17  ? 2   PRO B CG  1 
ATOM   773  C CD  . PRO B 1 3  ? 36.862  -11.600 -45.699 1.00 45.59  ? 2   PRO B CD  1 
ATOM   774  N N   . HIS B 1 4  ? 33.364  -13.839 -43.412 1.00 48.69  ? 3   HIS B N   1 
ATOM   775  C CA  . HIS B 1 4  ? 32.918  -15.180 -43.051 1.00 48.38  ? 3   HIS B CA  1 
ATOM   776  C C   . HIS B 1 4  ? 31.569  -15.473 -43.700 1.00 39.39  ? 3   HIS B C   1 
ATOM   777  O O   . HIS B 1 4  ? 30.992  -14.606 -44.369 1.00 38.42  ? 3   HIS B O   1 
ATOM   778  C CB  . HIS B 1 4  ? 32.979  -15.390 -41.536 1.00 49.30  ? 3   HIS B CB  1 
ATOM   779  C CG  . HIS B 1 4  ? 34.396  -15.447 -41.065 1.00 64.11  ? 3   HIS B CG  1 
ATOM   780  N ND1 . HIS B 1 4  ? 35.339  -16.260 -41.668 1.00 67.31  ? 3   HIS B ND1 1 
ATOM   781  C CD2 . HIS B 1 4  ? 35.035  -14.804 -40.066 1.00 61.06  ? 3   HIS B CD2 1 
ATOM   782  C CE1 . HIS B 1 4  ? 36.505  -16.112 -41.047 1.00 58.04  ? 3   HIS B CE1 1 
ATOM   783  N NE2 . HIS B 1 4  ? 36.346  -15.228 -40.077 1.00 65.70  ? 3   HIS B NE2 1 
ATOM   784  N N   . ALA B 1 5  ? 31.078  -16.711 -43.521 1.00 40.91  ? 4   ALA B N   1 
ATOM   785  C CA  . ALA B 1 5  ? 29.755  -17.048 -44.032 1.00 41.35  ? 4   ALA B CA  1 
ATOM   786  C C   . ALA B 1 5  ? 28.741  -16.016 -43.537 1.00 44.88  ? 4   ALA B C   1 
ATOM   787  O O   . ALA B 1 5  ? 27.879  -15.553 -44.298 1.00 39.83  ? 4   ALA B O   1 
ATOM   788  C CB  . ALA B 1 5  ? 29.365  -18.439 -43.567 1.00 39.60  ? 4   ALA B CB  1 
ATOM   789  N N   . PHE B 1 6  ? 28.840  -15.709 -42.236 1.00 44.13  ? 5   PHE B N   1 
ATOM   790  C CA  . PHE B 1 6  ? 28.041  -14.668 -41.599 1.00 44.72  ? 5   PHE B CA  1 
ATOM   791  C C   . PHE B 1 6  ? 28.917  -13.435 -41.373 1.00 42.73  ? 5   PHE B C   1 
ATOM   792  O O   . PHE B 1 6  ? 30.042  -13.551 -40.886 1.00 43.16  ? 5   PHE B O   1 
ATOM   793  C CB  . PHE B 1 6  ? 27.459  -15.091 -40.245 1.00 41.99  ? 5   PHE B CB  1 
ATOM   794  C CG  . PHE B 1 6  ? 26.402  -16.182 -40.337 1.00 38.40  ? 5   PHE B CG  1 
ATOM   795  C CD1 . PHE B 1 6  ? 25.057  -15.865 -40.529 1.00 32.94  ? 5   PHE B CD1 1 
ATOM   796  C CD2 . PHE B 1 6  ? 26.755  -17.523 -40.250 1.00 39.26  ? 5   PHE B CD2 1 
ATOM   797  C CE1 . PHE B 1 6  ? 24.101  -16.863 -40.647 1.00 36.53  ? 5   PHE B CE1 1 
ATOM   798  C CE2 . PHE B 1 6  ? 25.794  -18.516 -40.380 1.00 34.96  ? 5   PHE B CE2 1 
ATOM   799  C CZ  . PHE B 1 6  ? 24.470  -18.188 -40.546 1.00 36.36  ? 5   PHE B CZ  1 
ATOM   800  N N   . LYS B 1 7  ? 28.365  -12.269 -41.721 1.00 43.97  ? 6   LYS B N   1 
ATOM   801  C CA  . LYS B 1 7  ? 29.043  -10.998 -41.527 1.00 38.05  ? 6   LYS B CA  1 
ATOM   802  C C   . LYS B 1 7  ? 28.259  -10.139 -40.531 1.00 40.70  ? 6   LYS B C   1 
ATOM   803  O O   . LYS B 1 7  ? 27.016  -10.231 -40.416 1.00 35.51  ? 6   LYS B O   1 
ATOM   804  C CB  . LYS B 1 7  ? 29.152  -10.314 -42.889 1.00 42.55  ? 6   LYS B CB  1 
ATOM   805  C CG  . LYS B 1 7  ? 27.836  -10.002 -43.574 1.00 45.43  ? 6   LYS B CG  1 
ATOM   806  C CD  . LYS B 1 7  ? 28.008  -9.352  -44.948 1.00 51.96  ? 6   LYS B CD  1 
ATOM   807  C CE  . LYS B 1 7  ? 26.730  -8.924  -45.603 1.00 52.24  ? 6   LYS B CE  1 
ATOM   808  N NZ  . LYS B 1 7  ? 25.897  -10.062 -46.011 1.00 53.98  ? 6   LYS B NZ  1 
ATOM   809  N N   . PRO B 1 8  ? 28.961  -9.210  -39.838 1.00 41.65  ? 7   PRO B N   1 
ATOM   810  C CA  . PRO B 1 8  ? 28.321  -8.307  -38.874 1.00 34.81  ? 7   PRO B CA  1 
ATOM   811  C C   . PRO B 1 8  ? 27.144  -7.575  -39.501 1.00 37.50  ? 7   PRO B C   1 
ATOM   812  O O   . PRO B 1 8  ? 27.226  -7.098  -40.638 1.00 42.27  ? 7   PRO B O   1 
ATOM   813  C CB  . PRO B 1 8  ? 29.505  -7.390  -38.579 1.00 40.72  ? 7   PRO B CB  1 
ATOM   814  C CG  . PRO B 1 8  ? 30.691  -8.325  -38.640 1.00 41.55  ? 7   PRO B CG  1 
ATOM   815  C CD  . PRO B 1 8  ? 30.412  -8.966  -39.971 1.00 41.09  ? 7   PRO B CD  1 
ATOM   816  N N   . GLY B 1 9  ? 26.015  -7.573  -38.786 1.00 32.10  ? 8   GLY B N   1 
ATOM   817  C CA  . GLY B 1 9  ? 24.782  -6.965  -39.257 1.00 32.38  ? 8   GLY B CA  1 
ATOM   818  C C   . GLY B 1 9  ? 23.839  -7.934  -39.960 1.00 30.50  ? 8   GLY B C   1 
ATOM   819  O O   . GLY B 1 9  ? 22.716  -7.568  -40.278 1.00 31.34  ? 8   GLY B O   1 
ATOM   820  N N   . ASP B 1 10 ? 24.304  -9.155  -40.274 1.00 33.86  ? 9   ASP B N   1 
ATOM   821  C CA  . ASP B 1 10 ? 23.381  -10.139 -40.823 1.00 31.80  ? 9   ASP B CA  1 
ATOM   822  C C   . ASP B 1 10 ? 22.279  -10.455 -39.788 1.00 26.75  ? 9   ASP B C   1 
ATOM   823  O O   . ASP B 1 10 ? 22.545  -10.525 -38.597 1.00 29.66  ? 9   ASP B O   1 
ATOM   824  C CB  . ASP B 1 10 ? 24.102  -11.431 -41.163 1.00 34.79  ? 9   ASP B CB  1 
ATOM   825  C CG  . ASP B 1 10 ? 24.823  -11.512 -42.509 1.00 45.55  ? 9   ASP B CG  1 
ATOM   826  O OD1 . ASP B 1 10 ? 24.569  -10.652 -43.375 1.00 39.31  ? 9   ASP B OD1 1 
ATOM   827  O OD2 . ASP B 1 10 ? 25.653  -12.447 -42.670 1.00 39.78  ? 9   ASP B OD2 1 
ATOM   828  N N   . LEU B 1 11 ? 21.046  -10.613 -40.251 1.00 28.12  ? 10  LEU B N   1 
ATOM   829  C CA  . LEU B 1 11 ? 19.911  -10.858 -39.366 1.00 26.43  ? 10  LEU B CA  1 
ATOM   830  C C   . LEU B 1 11 ? 19.619  -12.348 -39.389 1.00 29.42  ? 10  LEU B C   1 
ATOM   831  O O   . LEU B 1 11 ? 19.718  -12.959 -40.454 1.00 31.20  ? 10  LEU B O   1 
ATOM   832  C CB  . LEU B 1 11 ? 18.726  -10.039 -39.861 1.00 28.42  ? 10  LEU B CB  1 
ATOM   833  C CG  . LEU B 1 11 ? 19.005  -8.530  -39.926 1.00 27.71  ? 10  LEU B CG  1 
ATOM   834  C CD1 . LEU B 1 11 ? 17.671  -7.845  -40.291 1.00 32.28  ? 10  LEU B CD1 1 
ATOM   835  C CD2 . LEU B 1 11 ? 19.636  -8.089  -38.596 1.00 25.96  ? 10  LEU B CD2 1 
ATOM   836  N N   . VAL B 1 12 ? 19.254  -12.907 -38.230 1.00 26.85  ? 11  VAL B N   1 
ATOM   837  C CA  . VAL B 1 12 ? 19.075  -14.355 -38.113 1.00 24.30  ? 11  VAL B CA  1 
ATOM   838  C C   . VAL B 1 12 ? 17.971  -14.630 -37.101 1.00 29.66  ? 11  VAL B C   1 
ATOM   839  O O   . VAL B 1 12 ? 17.587  -13.737 -36.348 1.00 26.62  ? 11  VAL B O   1 
ATOM   840  C CB  . VAL B 1 12 ? 20.367  -15.041 -37.612 1.00 25.79  ? 11  VAL B CB  1 
ATOM   841  C CG1 . VAL B 1 12 ? 21.533  -14.919 -38.607 1.00 26.05  ? 11  VAL B CG1 1 
ATOM   842  C CG2 . VAL B 1 12 ? 20.798  -14.593 -36.203 1.00 27.65  ? 11  VAL B CG2 1 
ATOM   843  N N   . PHE B 1 13 ? 17.564  -15.905 -37.007 1.00 28.47  ? 12  PHE B N   1 
ATOM   844  C CA  . PHE B 1 13 ? 17.084  -16.406 -35.732 1.00 27.87  ? 12  PHE B CA  1 
ATOM   845  C C   . PHE B 1 13 ? 18.160  -17.293 -35.125 1.00 27.24  ? 12  PHE B C   1 
ATOM   846  O O   . PHE B 1 13 ? 18.779  -18.076 -35.870 1.00 27.42  ? 12  PHE B O   1 
ATOM   847  C CB  . PHE B 1 13 ? 15.831  -17.261 -35.930 1.00 25.79  ? 12  PHE B CB  1 
ATOM   848  C CG  . PHE B 1 13 ? 14.643  -16.434 -36.374 1.00 27.68  ? 12  PHE B CG  1 
ATOM   849  C CD1 . PHE B 1 13 ? 14.424  -16.177 -37.728 1.00 27.66  ? 12  PHE B CD1 1 
ATOM   850  C CD2 . PHE B 1 13 ? 13.752  -15.922 -35.443 1.00 27.65  ? 12  PHE B CD2 1 
ATOM   851  C CE1 . PHE B 1 13 ? 13.322  -15.448 -38.148 1.00 34.84  ? 12  PHE B CE1 1 
ATOM   852  C CE2 . PHE B 1 13 ? 12.635  -15.200 -35.862 1.00 28.14  ? 12  PHE B CE2 1 
ATOM   853  C CZ  . PHE B 1 13 ? 12.431  -14.958 -37.212 1.00 32.66  ? 12  PHE B CZ  1 
ATOM   854  N N   . ALA B 1 14 ? 18.369  -17.159 -33.788 1.00 22.98  ? 13  ALA B N   1 
ATOM   855  C CA  . ALA B 1 14 ? 19.400  -17.879 -33.088 1.00 26.01  ? 13  ALA B CA  1 
ATOM   856  C C   . ALA B 1 14 ? 18.764  -18.821 -32.070 1.00 24.28  ? 13  ALA B C   1 
ATOM   857  O O   . ALA B 1 14 ? 17.835  -18.440 -31.361 1.00 27.70  ? 13  ALA B O   1 
ATOM   858  C CB  . ALA B 1 14 ? 20.390  -16.914 -32.428 1.00 25.69  ? 13  ALA B CB  1 
ATOM   859  N N   . LYS B 1 15 ? 19.306  -20.033 -31.984 1.00 25.56  ? 14  LYS B N   1 
ATOM   860  C CA  . LYS B 1 15 ? 18.661  -21.067 -31.178 1.00 26.37  ? 14  LYS B CA  1 
ATOM   861  C C   . LYS B 1 15 ? 19.516  -21.344 -29.951 1.00 26.46  ? 14  LYS B C   1 
ATOM   862  O O   . LYS B 1 15 ? 20.712  -21.644 -30.060 1.00 29.94  ? 14  LYS B O   1 
ATOM   863  C CB  . LYS B 1 15 ? 18.452  -22.333 -32.033 1.00 26.96  ? 14  LYS B CB  1 
ATOM   864  C CG  . LYS B 1 15 ? 17.726  -23.450 -31.232 1.00 28.06  ? 14  LYS B CG  1 
ATOM   865  C CD  . LYS B 1 15 ? 16.235  -23.096 -31.099 1.00 30.77  ? 14  LYS B CD  1 
ATOM   866  C CE  . LYS B 1 15 ? 15.345  -24.216 -30.459 1.00 29.74  ? 14  LYS B CE  1 
ATOM   867  N NZ  . LYS B 1 15 ? 15.802  -24.442 -29.090 1.00 27.95  ? 14  LYS B NZ  1 
ATOM   868  N N   . MET B 1 16 ? 18.904  -21.167 -28.777 1.00 29.62  ? 15  MET B N   1 
ATOM   869  C CA  . MET B 1 16 ? 19.487  -21.537 -27.493 1.00 27.84  ? 15  MET B CA  1 
ATOM   870  C C   . MET B 1 16 ? 18.664  -22.688 -26.905 1.00 31.81  ? 15  MET B C   1 
ATOM   871  O O   . MET B 1 16 ? 17.433  -22.660 -26.945 1.00 29.01  ? 15  MET B O   1 
ATOM   872  C CB  . MET B 1 16 ? 19.436  -20.362 -26.506 1.00 30.78  ? 15  MET B CB  1 
ATOM   873  C CG  . MET B 1 16 ? 20.096  -19.093 -26.978 1.00 35.89  ? 15  MET B CG  1 
ATOM   874  S SD  . MET B 1 16 ? 21.889  -19.038 -26.777 1.00 45.21  ? 15  MET B SD  1 
ATOM   875  C CE  . MET B 1 16 ? 22.050  -19.051 -24.985 1.00 37.74  ? 15  MET B CE  1 
ATOM   876  N N   . LYS B 1 17 ? 19.343  -23.673 -26.312 1.00 33.65  ? 16  LYS B N   1 
ATOM   877  C CA  . LYS B 1 17 ? 18.636  -24.719 -25.577 1.00 33.46  ? 16  LYS B CA  1 
ATOM   878  C C   . LYS B 1 17 ? 17.595  -24.109 -24.622 1.00 32.58  ? 16  LYS B C   1 
ATOM   879  O O   . LYS B 1 17 ? 17.890  -23.181 -23.864 1.00 33.10  ? 16  LYS B O   1 
ATOM   880  C CB  . LYS B 1 17 ? 19.682  -25.554 -24.822 1.00 39.64  ? 16  LYS B CB  1 
ATOM   881  C CG  . LYS B 1 17 ? 19.112  -26.833 -24.184 1.00 47.04  ? 16  LYS B CG  1 
ATOM   882  C CD  . LYS B 1 17 ? 20.122  -27.661 -23.394 1.00 51.45  ? 16  LYS B CD  1 
ATOM   883  N N   . GLY B 1 18 ? 16.374  -24.641 -24.669 1.00 34.11  ? 17  GLY B N   1 
ATOM   884  C CA  . GLY B 1 18 ? 15.316  -24.201 -23.774 1.00 35.64  ? 17  GLY B CA  1 
ATOM   885  C C   . GLY B 1 18 ? 14.495  -23.025 -24.310 1.00 36.51  ? 17  GLY B C   1 
ATOM   886  O O   . GLY B 1 18 ? 13.537  -22.620 -23.661 1.00 32.93  ? 17  GLY B O   1 
ATOM   887  N N   . TYR B 1 19 ? 14.857  -22.453 -25.476 1.00 33.25  ? 18  TYR B N   1 
ATOM   888  C CA  . TYR B 1 19 ? 14.137  -21.267 -25.944 1.00 30.88  ? 18  TYR B CA  1 
ATOM   889  C C   . TYR B 1 19 ? 13.760  -21.430 -27.420 1.00 29.52  ? 18  TYR B C   1 
ATOM   890  O O   . TYR B 1 19 ? 14.423  -22.166 -28.145 1.00 32.06  ? 18  TYR B O   1 
ATOM   891  C CB  . TYR B 1 19 ? 15.074  -20.052 -25.832 1.00 28.06  ? 18  TYR B CB  1 
ATOM   892  C CG  . TYR B 1 19 ? 15.437  -19.784 -24.381 1.00 31.69  ? 18  TYR B CG  1 
ATOM   893  C CD1 . TYR B 1 19 ? 14.579  -19.054 -23.560 1.00 33.77  ? 18  TYR B CD1 1 
ATOM   894  C CD2 . TYR B 1 19 ? 16.550  -20.397 -23.801 1.00 32.91  ? 18  TYR B CD2 1 
ATOM   895  C CE1 . TYR B 1 19 ? 14.854  -18.881 -22.207 1.00 34.65  ? 18  TYR B CE1 1 
ATOM   896  C CE2 . TYR B 1 19 ? 16.828  -20.229 -22.446 1.00 36.95  ? 18  TYR B CE2 1 
ATOM   897  C CZ  . TYR B 1 19 ? 15.982  -19.469 -21.653 1.00 33.88  ? 18  TYR B CZ  1 
ATOM   898  O OH  . TYR B 1 19 ? 16.283  -19.331 -20.327 1.00 34.91  ? 18  TYR B OH  1 
ATOM   899  N N   . PRO B 1 20 ? 12.704  -20.743 -27.917 1.00 28.72  ? 19  PRO B N   1 
ATOM   900  C CA  . PRO B 1 20 ? 12.366  -20.774 -29.343 1.00 25.81  ? 19  PRO B CA  1 
ATOM   901  C C   . PRO B 1 20 ? 13.443  -20.029 -30.135 1.00 27.29  ? 19  PRO B C   1 
ATOM   902  O O   . PRO B 1 20 ? 14.071  -19.141 -29.572 1.00 25.17  ? 19  PRO B O   1 
ATOM   903  C CB  . PRO B 1 20 ? 11.048  -20.051 -29.405 1.00 26.45  ? 19  PRO B CB  1 
ATOM   904  C CG  . PRO B 1 20 ? 11.086  -19.083 -28.230 1.00 30.69  ? 19  PRO B CG  1 
ATOM   905  C CD  . PRO B 1 20 ? 11.840  -19.839 -27.133 1.00 26.21  ? 19  PRO B CD  1 
ATOM   906  N N   . HIS B 1 21 ? 13.651  -20.428 -31.401 1.00 26.04  ? 20  HIS B N   1 
ATOM   907  C CA  . HIS B 1 21 ? 14.472  -19.659 -32.358 1.00 28.84  ? 20  HIS B CA  1 
ATOM   908  C C   . HIS B 1 21 ? 14.208  -18.161 -32.204 1.00 25.41  ? 20  HIS B C   1 
ATOM   909  O O   . HIS B 1 21 ? 13.057  -17.734 -32.322 1.00 25.54  ? 20  HIS B O   1 
ATOM   910  C CB  . HIS B 1 21 ? 14.149  -20.103 -33.790 1.00 25.53  ? 20  HIS B CB  1 
ATOM   911  C CG  . HIS B 1 21 ? 14.386  -21.587 -33.985 1.00 29.48  ? 20  HIS B CG  1 
ATOM   912  N ND1 . HIS B 1 21 ? 13.471  -22.552 -33.573 1.00 30.79  ? 20  HIS B ND1 1 
ATOM   913  C CD2 . HIS B 1 21 ? 15.450  -22.272 -34.461 1.00 30.92  ? 20  HIS B CD2 1 
ATOM   914  C CE1 . HIS B 1 21 ? 13.944  -23.762 -33.857 1.00 30.20  ? 20  HIS B CE1 1 
ATOM   915  N NE2 . HIS B 1 21 ? 15.153  -23.623 -34.381 1.00 28.84  ? 20  HIS B NE2 1 
ATOM   916  N N   . TRP B 1 22 ? 15.275  -17.381 -31.959 1.00 26.20  ? 21  TRP B N   1 
ATOM   917  C CA  . TRP B 1 22 ? 15.078  -16.058 -31.370 1.00 25.69  ? 21  TRP B CA  1 
ATOM   918  C C   . TRP B 1 22 ? 15.535  -14.973 -32.357 1.00 26.05  ? 21  TRP B C   1 
ATOM   919  O O   . TRP B 1 22 ? 16.656  -15.062 -32.823 1.00 25.33  ? 21  TRP B O   1 
ATOM   920  C CB  . TRP B 1 22 ? 15.854  -15.947 -30.053 1.00 25.99  ? 21  TRP B CB  1 
ATOM   921  C CG  . TRP B 1 22 ? 15.320  -14.824 -29.186 1.00 27.80  ? 21  TRP B CG  1 
ATOM   922  C CD1 . TRP B 1 22 ? 15.537  -13.477 -29.331 1.00 27.32  ? 21  TRP B CD1 1 
ATOM   923  C CD2 . TRP B 1 22 ? 14.416  -14.960 -28.058 1.00 28.57  ? 21  TRP B CD2 1 
ATOM   924  N NE1 . TRP B 1 22 ? 14.813  -12.765 -28.383 1.00 26.31  ? 21  TRP B NE1 1 
ATOM   925  C CE2 . TRP B 1 22 ? 14.130  -13.651 -27.582 1.00 26.89  ? 21  TRP B CE2 1 
ATOM   926  C CE3 . TRP B 1 22 ? 13.834  -16.064 -27.405 1.00 27.21  ? 21  TRP B CE3 1 
ATOM   927  C CZ2 . TRP B 1 22 ? 13.285  -13.415 -26.484 1.00 24.80  ? 21  TRP B CZ2 1 
ATOM   928  C CZ3 . TRP B 1 22 ? 13.009  -15.830 -26.321 1.00 26.82  ? 21  TRP B CZ3 1 
ATOM   929  C CH2 . TRP B 1 22 ? 12.699  -14.520 -25.901 1.00 24.29  ? 21  TRP B CH2 1 
ATOM   930  N N   . PRO B 1 23 ? 14.769  -13.890 -32.663 1.00 25.66  ? 22  PRO B N   1 
ATOM   931  C CA  . PRO B 1 23 ? 15.260  -12.881 -33.622 1.00 24.81  ? 22  PRO B CA  1 
ATOM   932  C C   . PRO B 1 23 ? 16.567  -12.289 -33.100 1.00 24.67  ? 22  PRO B C   1 
ATOM   933  O O   . PRO B 1 23 ? 16.679  -11.911 -31.935 1.00 26.26  ? 22  PRO B O   1 
ATOM   934  C CB  . PRO B 1 23 ? 14.101  -11.820 -33.678 1.00 24.56  ? 22  PRO B CB  1 
ATOM   935  C CG  . PRO B 1 23 ? 13.395  -12.015 -32.338 1.00 27.31  ? 22  PRO B CG  1 
ATOM   936  C CD  . PRO B 1 23 ? 13.464  -13.545 -32.104 1.00 25.11  ? 22  PRO B CD  1 
ATOM   937  N N   . ALA B 1 24 ? 17.587  -12.202 -33.947 1.00 25.81  ? 23  ALA B N   1 
ATOM   938  C CA  . ALA B 1 24 ? 18.909  -11.811 -33.473 1.00 25.15  ? 23  ALA B CA  1 
ATOM   939  C C   . ALA B 1 24 ? 19.726  -11.220 -34.627 1.00 26.27  ? 23  ALA B C   1 
ATOM   940  O O   . ALA B 1 24 ? 19.292  -11.242 -35.786 1.00 27.60  ? 23  ALA B O   1 
ATOM   941  C CB  . ALA B 1 24 ? 19.623  -12.998 -32.830 1.00 27.23  ? 23  ALA B CB  1 
ATOM   942  N N   . ARG B 1 25 ? 20.911  -10.711 -34.271 1.00 28.68  ? 24  ARG B N   1 
ATOM   943  C CA  . ARG B 1 25 ? 21.842  -10.231 -35.286 1.00 29.86  ? 24  ARG B CA  1 
ATOM   944  C C   . ARG B 1 25 ? 23.253  -10.726 -34.982 1.00 28.23  ? 24  ARG B C   1 
ATOM   945  O O   . ARG B 1 25 ? 23.611  -11.014 -33.838 1.00 25.96  ? 24  ARG B O   1 
ATOM   946  C CB  . ARG B 1 25 ? 21.808  -8.705  -35.400 1.00 30.00  ? 24  ARG B CB  1 
ATOM   947  C CG  . ARG B 1 25 ? 22.447  -8.021  -34.204 1.00 30.74  ? 24  ARG B CG  1 
ATOM   948  C CD  . ARG B 1 25 ? 22.330  -6.499  -34.371 1.00 26.02  ? 24  ARG B CD  1 
ATOM   949  N NE  . ARG B 1 25 ? 22.939  -5.792  -33.246 1.00 28.85  ? 24  ARG B NE  1 
ATOM   950  C CZ  . ARG B 1 25 ? 22.613  -4.546  -32.877 1.00 30.91  ? 24  ARG B CZ  1 
ATOM   951  N NH1 . ARG B 1 25 ? 21.635  -3.892  -33.492 1.00 31.52  ? 24  ARG B NH1 1 
ATOM   952  N NH2 . ARG B 1 25 ? 23.260  -3.987  -31.868 1.00 29.04  ? 24  ARG B NH2 1 
ATOM   953  N N   . ILE B 1 26 ? 24.081  -10.806 -36.038 1.00 28.75  ? 25  ILE B N   1 
ATOM   954  C CA  . ILE B 1 26 ? 25.501  -10.964 -35.824 1.00 29.68  ? 25  ILE B CA  1 
ATOM   955  C C   . ILE B 1 26 ? 26.060  -9.578  -35.509 1.00 32.96  ? 25  ILE B C   1 
ATOM   956  O O   . ILE B 1 26 ? 25.814  -8.653  -36.288 1.00 34.01  ? 25  ILE B O   1 
ATOM   957  C CB  . ILE B 1 26 ? 26.166  -11.475 -37.114 1.00 34.83  ? 25  ILE B CB  1 
ATOM   958  C CG1 . ILE B 1 26 ? 25.427  -12.669 -37.711 1.00 32.50  ? 25  ILE B CG1 1 
ATOM   959  C CG2 . ILE B 1 26 ? 27.663  -11.713 -36.891 1.00 39.64  ? 25  ILE B CG2 1 
ATOM   960  C CD1 . ILE B 1 26 ? 25.373  -13.889 -36.803 1.00 31.61  ? 25  ILE B CD1 1 
ATOM   961  N N   . ASP B 1 27 ? 26.865  -9.502  -34.443 1.00 34.78  ? 26  ASP B N   1 
ATOM   962  C CA  . ASP B 1 27 ? 27.536  -8.286  -33.990 1.00 43.26  ? 26  ASP B CA  1 
ATOM   963  C C   . ASP B 1 27 ? 29.008  -8.267  -34.421 1.00 43.97  ? 26  ASP B C   1 
ATOM   964  O O   . ASP B 1 27 ? 29.572  -9.305  -34.750 1.00 41.23  ? 26  ASP B O   1 
ATOM   965  C CB  . ASP B 1 27 ? 27.455  -8.176  -32.478 1.00 37.10  ? 26  ASP B CB  1 
ATOM   966  C CG  . ASP B 1 27 ? 26.269  -7.415  -31.899 1.00 42.02  ? 26  ASP B CG  1 
ATOM   967  O OD1 . ASP B 1 27 ? 25.487  -6.845  -32.686 1.00 40.96  ? 26  ASP B OD1 1 
ATOM   968  O OD2 . ASP B 1 27 ? 26.165  -7.374  -30.647 1.00 37.60  ? 26  ASP B OD2 1 
ATOM   969  N N   . ASP B 1 28 ? 29.631  -7.075  -34.379 1.00 54.48  ? 27  ASP B N   1 
ATOM   970  C CA  . ASP B 1 28 ? 31.071  -6.886  -34.529 1.00 60.22  ? 27  ASP B CA  1 
ATOM   971  C C   . ASP B 1 28 ? 31.817  -7.334  -33.271 1.00 59.34  ? 27  ASP B C   1 
ATOM   972  O O   . ASP B 1 28 ? 31.201  -7.774  -32.300 1.00 66.92  ? 27  ASP B O   1 
ATOM   973  C CB  . ASP B 1 28 ? 31.414  -5.434  -34.825 1.00 57.04  ? 27  ASP B CB  1 
ATOM   974  C CG  . ASP B 1 28 ? 31.418  -5.064  -36.299 1.00 65.77  ? 27  ASP B CG  1 
ATOM   975  O OD1 . ASP B 1 28 ? 32.365  -5.488  -37.017 1.00 55.00  ? 27  ASP B OD1 1 
ATOM   976  O OD2 . ASP B 1 28 ? 30.467  -4.366  -36.720 1.00 76.22  ? 27  ASP B OD2 1 
ATOM   977  N N   . ILE B 1 29 ? 33.152  -7.202  -33.293 1.00 65.56  ? 28  ILE B N   1 
ATOM   978  C CA  . ILE B 1 29 ? 33.989  -7.496  -32.136 1.00 70.90  ? 28  ILE B CA  1 
ATOM   979  C C   . ILE B 1 29 ? 34.862  -6.266  -31.832 1.00 77.74  ? 28  ILE B C   1 
ATOM   980  O O   . ILE B 1 29 ? 34.277  -5.164  -31.746 1.00 79.97  ? 28  ILE B O   1 
ATOM   981  C CB  . ILE B 1 29 ? 34.844  -8.757  -32.364 1.00 69.20  ? 28  ILE B CB  1 
ATOM   982  N N   . LYS B 1 35 ? 36.979  -12.159 -27.506 1.00 72.12  ? 34  LYS B N   1 
ATOM   983  C CA  . LYS B 1 35 ? 36.791  -12.723 -28.874 1.00 63.51  ? 34  LYS B CA  1 
ATOM   984  C C   . LYS B 1 35 ? 36.029  -14.058 -28.799 1.00 64.27  ? 34  LYS B C   1 
ATOM   985  O O   . LYS B 1 35 ? 36.170  -14.804 -27.825 1.00 59.95  ? 34  LYS B O   1 
ATOM   986  C CB  . LYS B 1 35 ? 38.155  -12.753 -29.573 1.00 60.93  ? 34  LYS B CB  1 
ATOM   987  N N   . PRO B 1 36 ? 35.167  -14.403 -29.796 1.00 58.41  ? 35  PRO B N   1 
ATOM   988  C CA  . PRO B 1 36 ? 34.387  -15.650 -29.749 1.00 53.59  ? 35  PRO B CA  1 
ATOM   989  C C   . PRO B 1 36 ? 35.277  -16.885 -29.711 1.00 48.12  ? 35  PRO B C   1 
ATOM   990  O O   . PRO B 1 36 ? 36.402  -16.832 -30.185 1.00 51.85  ? 35  PRO B O   1 
ATOM   991  C CB  . PRO B 1 36 ? 33.533  -15.608 -31.028 1.00 50.20  ? 35  PRO B CB  1 
ATOM   992  C CG  . PRO B 1 36 ? 34.231  -14.610 -31.927 1.00 56.82  ? 35  PRO B CG  1 
ATOM   993  C CD  . PRO B 1 36 ? 34.887  -13.604 -31.001 1.00 50.06  ? 35  PRO B CD  1 
ATOM   994  N N   . PRO B 1 37 ? 34.845  -18.022 -29.117 1.00 48.45  ? 36  PRO B N   1 
ATOM   995  C CA  . PRO B 1 37 ? 35.592  -19.270 -29.259 1.00 48.50  ? 36  PRO B CA  1 
ATOM   996  C C   . PRO B 1 37 ? 35.665  -19.585 -30.753 1.00 52.82  ? 36  PRO B C   1 
ATOM   997  O O   . PRO B 1 37 ? 34.866  -19.064 -31.536 1.00 49.86  ? 36  PRO B O   1 
ATOM   998  C CB  . PRO B 1 37 ? 34.750  -20.322 -28.489 1.00 50.66  ? 36  PRO B CB  1 
ATOM   999  C CG  . PRO B 1 37 ? 33.825  -19.517 -27.597 1.00 49.18  ? 36  PRO B CG  1 
ATOM   1000 C CD  . PRO B 1 37 ? 33.653  -18.157 -28.261 1.00 52.95  ? 36  PRO B CD  1 
ATOM   1001 N N   . PRO B 1 38 ? 36.596  -20.459 -31.206 1.00 53.75  ? 37  PRO B N   1 
ATOM   1002 C CA  . PRO B 1 38 ? 36.662  -20.837 -32.627 1.00 53.69  ? 37  PRO B CA  1 
ATOM   1003 C C   . PRO B 1 38 ? 35.319  -21.309 -33.202 1.00 51.48  ? 37  PRO B C   1 
ATOM   1004 O O   . PRO B 1 38 ? 34.575  -22.017 -32.524 1.00 51.49  ? 37  PRO B O   1 
ATOM   1005 C CB  . PRO B 1 38 ? 37.743  -21.953 -32.634 1.00 55.19  ? 37  PRO B CB  1 
ATOM   1006 C CG  . PRO B 1 38 ? 38.623  -21.654 -31.415 1.00 49.92  ? 37  PRO B CG  1 
ATOM   1007 C CD  . PRO B 1 38 ? 37.640  -21.104 -30.383 1.00 60.20  ? 37  PRO B CD  1 
ATOM   1008 N N   . ASN B 1 39 ? 35.009  -20.897 -34.443 1.00 51.13  ? 38  ASN B N   1 
ATOM   1009 C CA  . ASN B 1 39 ? 33.828  -21.355 -35.179 1.00 48.96  ? 38  ASN B CA  1 
ATOM   1010 C C   . ASN B 1 39 ? 32.546  -20.621 -34.767 1.00 44.40  ? 38  ASN B C   1 
ATOM   1011 O O   . ASN B 1 39 ? 31.492  -20.859 -35.339 1.00 39.20  ? 38  ASN B O   1 
ATOM   1012 C CB  . ASN B 1 39 ? 33.581  -22.852 -35.007 1.00 49.15  ? 38  ASN B CB  1 
ATOM   1013 C CG  . ASN B 1 39 ? 34.794  -23.680 -35.374 1.00 57.93  ? 38  ASN B CG  1 
ATOM   1014 O OD1 . ASN B 1 39 ? 35.120  -24.650 -34.680 1.00 63.53  ? 38  ASN B OD1 1 
ATOM   1015 N ND2 . ASN B 1 39 ? 35.462  -23.331 -36.464 1.00 52.81  ? 38  ASN B ND2 1 
ATOM   1016 N N   . LYS B 1 40 ? 32.620  -19.721 -33.777 1.00 44.87  ? 39  LYS B N   1 
ATOM   1017 C CA  . LYS B 1 40 ? 31.420  -19.123 -33.221 1.00 40.93  ? 39  LYS B CA  1 
ATOM   1018 C C   . LYS B 1 40 ? 31.416  -17.623 -33.494 1.00 41.27  ? 39  LYS B C   1 
ATOM   1019 O O   . LYS B 1 40 ? 32.458  -17.037 -33.766 1.00 40.29  ? 39  LYS B O   1 
ATOM   1020 C CB  . LYS B 1 40 ? 31.389  -19.491 -31.736 1.00 42.63  ? 39  LYS B CB  1 
ATOM   1021 C CG  . LYS B 1 40 ? 31.116  -20.948 -31.445 1.00 43.91  ? 39  LYS B CG  1 
ATOM   1022 C CD  . LYS B 1 40 ? 31.197  -21.176 -29.940 1.00 59.50  ? 39  LYS B CD  1 
ATOM   1023 C CE  . LYS B 1 40 ? 30.098  -21.997 -29.338 1.00 68.01  ? 39  LYS B CE  1 
ATOM   1024 N NZ  . LYS B 1 40 ? 30.290  -23.443 -29.461 1.00 63.13  ? 39  LYS B NZ  1 
ATOM   1025 N N   . TYR B 1 41 ? 30.222  -17.029 -33.429 1.00 37.10  ? 40  TYR B N   1 
ATOM   1026 C CA  . TYR B 1 41 ? 29.988  -15.620 -33.702 1.00 34.63  ? 40  TYR B CA  1 
ATOM   1027 C C   . TYR B 1 41 ? 29.363  -14.932 -32.493 1.00 35.97  ? 40  TYR B C   1 
ATOM   1028 O O   . TYR B 1 41 ? 28.643  -15.561 -31.719 1.00 34.29  ? 40  TYR B O   1 
ATOM   1029 C CB  . TYR B 1 41 ? 28.930  -15.536 -34.793 1.00 31.97  ? 40  TYR B CB  1 
ATOM   1030 C CG  . TYR B 1 41 ? 29.396  -15.974 -36.174 1.00 34.21  ? 40  TYR B CG  1 
ATOM   1031 C CD1 . TYR B 1 41 ? 30.114  -15.111 -37.000 1.00 31.40  ? 40  TYR B CD1 1 
ATOM   1032 C CD2 . TYR B 1 41 ? 29.090  -17.244 -36.651 1.00 33.88  ? 40  TYR B CD2 1 
ATOM   1033 C CE1 . TYR B 1 41 ? 30.546  -15.528 -38.256 1.00 37.77  ? 40  TYR B CE1 1 
ATOM   1034 C CE2 . TYR B 1 41 ? 29.499  -17.662 -37.907 1.00 34.96  ? 40  TYR B CE2 1 
ATOM   1035 C CZ  . TYR B 1 41 ? 30.251  -16.809 -38.703 1.00 38.38  ? 40  TYR B CZ  1 
ATOM   1036 O OH  . TYR B 1 41 ? 30.618  -17.238 -39.956 1.00 36.90  ? 40  TYR B OH  1 
ATOM   1037 N N   . PRO B 1 42 ? 29.602  -13.603 -32.332 1.00 35.94  ? 41  PRO B N   1 
ATOM   1038 C CA  . PRO B 1 42 ? 28.917  -12.813 -31.310 1.00 33.03  ? 41  PRO B CA  1 
ATOM   1039 C C   . PRO B 1 42 ? 27.494  -12.569 -31.782 1.00 33.30  ? 41  PRO B C   1 
ATOM   1040 O O   . PRO B 1 42 ? 27.275  -11.921 -32.820 1.00 34.96  ? 41  PRO B O   1 
ATOM   1041 C CB  . PRO B 1 42 ? 29.723  -11.485 -31.187 1.00 33.53  ? 41  PRO B CB  1 
ATOM   1042 C CG  . PRO B 1 42 ? 30.701  -11.480 -32.366 1.00 36.01  ? 41  PRO B CG  1 
ATOM   1043 C CD  . PRO B 1 42 ? 30.536  -12.798 -33.142 1.00 36.43  ? 41  PRO B CD  1 
ATOM   1044 N N   . ILE B 1 43 ? 26.535  -13.049 -30.970 1.00 28.59  ? 42  ILE B N   1 
ATOM   1045 C CA  . ILE B 1 43 ? 25.117  -12.859 -31.245 1.00 29.19  ? 42  ILE B CA  1 
ATOM   1046 C C   . ILE B 1 43 ? 24.503  -11.828 -30.302 1.00 25.98  ? 42  ILE B C   1 
ATOM   1047 O O   . ILE B 1 43 ? 24.752  -11.875 -29.114 1.00 29.50  ? 42  ILE B O   1 
ATOM   1048 C CB  . ILE B 1 43 ? 24.374  -14.200 -31.143 1.00 27.25  ? 42  ILE B CB  1 
ATOM   1049 C CG1 . ILE B 1 43 ? 25.117  -15.267 -32.021 1.00 29.46  ? 42  ILE B CG1 1 
ATOM   1050 C CG2 . ILE B 1 43 ? 22.918  -14.021 -31.584 1.00 30.09  ? 42  ILE B CG2 1 
ATOM   1051 C CD1 . ILE B 1 43 ? 25.193  -14.904 -33.495 1.00 27.66  ? 42  ILE B CD1 1 
ATOM   1052 N N   . PHE B 1 44 ? 23.623  -10.985 -30.855 1.00 27.94  ? 43  PHE B N   1 
ATOM   1053 C CA  . PHE B 1 44 ? 22.828  -10.039 -30.077 1.00 29.95  ? 43  PHE B CA  1 
ATOM   1054 C C   . PHE B 1 44 ? 21.357  -10.409 -30.276 1.00 28.30  ? 43  PHE B C   1 
ATOM   1055 O O   . PHE B 1 44 ? 20.856  -10.430 -31.392 1.00 29.12  ? 43  PHE B O   1 
ATOM   1056 C CB  . PHE B 1 44 ? 23.135  -8.605  -30.532 1.00 28.09  ? 43  PHE B CB  1 
ATOM   1057 C CG  . PHE B 1 44 ? 22.198  -7.580  -29.894 1.00 29.35  ? 43  PHE B CG  1 
ATOM   1058 C CD1 . PHE B 1 44 ? 20.983  -7.218  -30.500 1.00 27.79  ? 43  PHE B CD1 1 
ATOM   1059 C CD2 . PHE B 1 44 ? 22.531  -6.997  -28.681 1.00 33.64  ? 43  PHE B CD2 1 
ATOM   1060 C CE1 . PHE B 1 44 ? 20.136  -6.290  -29.891 1.00 32.14  ? 43  PHE B CE1 1 
ATOM   1061 C CE2 . PHE B 1 44 ? 21.678  -6.073  -28.076 1.00 33.33  ? 43  PHE B CE2 1 
ATOM   1062 C CZ  . PHE B 1 44 ? 20.503  -5.715  -28.683 1.00 33.09  ? 43  PHE B CZ  1 
ATOM   1063 N N   . PHE B 1 45 ? 20.645  -10.687 -29.176 1.00 27.85  ? 44  PHE B N   1 
ATOM   1064 C CA  . PHE B 1 45 ? 19.263  -11.126 -29.209 1.00 27.56  ? 44  PHE B CA  1 
ATOM   1065 C C   . PHE B 1 45 ? 18.381  -9.903  -29.028 1.00 27.36  ? 44  PHE B C   1 
ATOM   1066 O O   . PHE B 1 45 ? 18.491  -9.189  -28.026 1.00 27.83  ? 44  PHE B O   1 
ATOM   1067 C CB  . PHE B 1 45 ? 19.154  -12.076 -28.008 1.00 25.71  ? 44  PHE B CB  1 
ATOM   1068 C CG  . PHE B 1 45 ? 19.831  -13.431 -28.207 1.00 24.94  ? 44  PHE B CG  1 
ATOM   1069 C CD1 . PHE B 1 45 ? 21.192  -13.601 -28.011 1.00 26.21  ? 44  PHE B CD1 1 
ATOM   1070 C CD2 . PHE B 1 45 ? 19.100  -14.523 -28.669 1.00 27.13  ? 44  PHE B CD2 1 
ATOM   1071 C CE1 . PHE B 1 45 ? 21.798  -14.824 -28.249 1.00 28.40  ? 44  PHE B CE1 1 
ATOM   1072 C CE2 . PHE B 1 45 ? 19.706  -15.755 -28.877 1.00 28.38  ? 44  PHE B CE2 1 
ATOM   1073 C CZ  . PHE B 1 45 ? 21.067  -15.902 -28.683 1.00 28.28  ? 44  PHE B CZ  1 
ATOM   1074 N N   . PHE B 1 46 ? 17.544  -9.654  -30.036 1.00 27.09  ? 45  PHE B N   1 
ATOM   1075 C CA  . PHE B 1 46 ? 16.643  -8.517  -29.993 1.00 30.13  ? 45  PHE B CA  1 
ATOM   1076 C C   . PHE B 1 46 ? 15.625  -8.723  -28.870 1.00 31.68  ? 45  PHE B C   1 
ATOM   1077 O O   . PHE B 1 46 ? 15.314  -9.859  -28.465 1.00 28.23  ? 45  PHE B O   1 
ATOM   1078 C CB  . PHE B 1 46 ? 15.905  -8.357  -31.311 1.00 26.34  ? 45  PHE B CB  1 
ATOM   1079 C CG  . PHE B 1 46 ? 16.813  -7.943  -32.456 1.00 30.92  ? 45  PHE B CG  1 
ATOM   1080 C CD1 . PHE B 1 46 ? 17.368  -6.648  -32.486 1.00 33.22  ? 45  PHE B CD1 1 
ATOM   1081 C CD2 . PHE B 1 46 ? 17.086  -8.827  -33.505 1.00 27.94  ? 45  PHE B CD2 1 
ATOM   1082 C CE1 . PHE B 1 46 ? 18.187  -6.254  -33.544 1.00 31.50  ? 45  PHE B CE1 1 
ATOM   1083 C CE2 . PHE B 1 46 ? 17.895  -8.414  -34.567 1.00 28.91  ? 45  PHE B CE2 1 
ATOM   1084 C CZ  . PHE B 1 46 ? 18.460  -7.133  -34.566 1.00 30.31  ? 45  PHE B CZ  1 
ATOM   1085 N N   . GLY B 1 47 ? 15.109  -7.596  -28.364 1.00 32.51  ? 46  GLY B N   1 
ATOM   1086 C CA  . GLY B 1 47 ? 14.045  -7.677  -27.376 1.00 29.43  ? 46  GLY B CA  1 
ATOM   1087 C C   . GLY B 1 47 ? 14.669  -7.801  -25.987 1.00 30.28  ? 46  GLY B C   1 
ATOM   1088 O O   . GLY B 1 47 ? 14.536  -6.889  -25.176 1.00 33.58  ? 46  GLY B O   1 
ATOM   1089 N N   . THR B 1 48 ? 15.347  -8.925  -25.725 1.00 31.54  ? 47  THR B N   1 
ATOM   1090 C CA  . THR B 1 48 ? 16.066  -9.151  -24.483 1.00 30.89  ? 47  THR B CA  1 
ATOM   1091 C C   . THR B 1 48 ? 17.329  -8.302  -24.409 1.00 32.76  ? 47  THR B C   1 
ATOM   1092 O O   . THR B 1 48 ? 17.743  -7.931  -23.302 1.00 33.35  ? 47  THR B O   1 
ATOM   1093 C CB  . THR B 1 48 ? 16.385  -10.630 -24.243 1.00 31.57  ? 47  THR B CB  1 
ATOM   1094 O OG1 . THR B 1 48 ? 17.378  -11.046 -25.191 1.00 32.07  ? 47  THR B OG1 1 
ATOM   1095 C CG2 . THR B 1 48 ? 15.136  -11.491 -24.201 1.00 28.40  ? 47  THR B CG2 1 
ATOM   1096 N N   . HIS B 1 49 ? 17.929  -8.037  -25.575 1.00 30.91  ? 48  HIS B N   1 
ATOM   1097 C CA  . HIS B 1 49 ? 19.246  -7.416  -25.687 1.00 34.02  ? 48  HIS B CA  1 
ATOM   1098 C C   . HIS B 1 49 ? 20.319  -8.232  -24.980 1.00 35.11  ? 48  HIS B C   1 
ATOM   1099 O O   . HIS B 1 49 ? 21.353  -7.683  -24.601 1.00 39.06  ? 48  HIS B O   1 
ATOM   1100 C CB  . HIS B 1 49 ? 19.257  -5.943  -25.227 1.00 30.21  ? 48  HIS B CB  1 
ATOM   1101 C CG  . HIS B 1 49 ? 18.094  -5.214  -25.771 1.00 32.43  ? 48  HIS B CG  1 
ATOM   1102 N ND1 . HIS B 1 49 ? 17.368  -4.351  -24.981 1.00 34.71  ? 48  HIS B ND1 1 
ATOM   1103 C CD2 . HIS B 1 49 ? 17.477  -5.248  -26.971 1.00 31.51  ? 48  HIS B CD2 1 
ATOM   1104 C CE1 . HIS B 1 49 ? 16.356  -3.869  -25.703 1.00 42.29  ? 48  HIS B CE1 1 
ATOM   1105 N NE2 . HIS B 1 49 ? 16.405  -4.403  -26.918 1.00 38.21  ? 48  HIS B NE2 1 
ATOM   1106 N N   . GLU B 1 50 ? 20.124  -9.547  -24.873 1.00 30.19  ? 49  GLU B N   1 
ATOM   1107 C CA  . GLU B 1 50 ? 21.164  -10.416 -24.336 1.00 33.98  ? 49  GLU B CA  1 
ATOM   1108 C C   . GLU B 1 50 ? 22.200  -10.744 -25.426 1.00 32.01  ? 49  GLU B C   1 
ATOM   1109 O O   . GLU B 1 50 ? 21.955  -10.491 -26.613 1.00 31.27  ? 49  GLU B O   1 
ATOM   1110 C CB  . GLU B 1 50 ? 20.532  -11.708 -23.822 1.00 33.71  ? 49  GLU B CB  1 
ATOM   1111 C CG  . GLU B 1 50 ? 19.825  -11.488 -22.487 1.00 34.79  ? 49  GLU B CG  1 
ATOM   1112 C CD  . GLU B 1 50 ? 19.182  -12.719 -21.873 1.00 38.93  ? 49  GLU B CD  1 
ATOM   1113 O OE1 . GLU B 1 50 ? 18.380  -13.349 -22.563 1.00 36.42  ? 49  GLU B OE1 1 
ATOM   1114 O OE2 . GLU B 1 50 ? 19.425  -13.034 -20.698 1.00 36.91  ? 49  GLU B OE2 1 
ATOM   1115 N N   . THR B 1 51 ? 23.345  -11.295 -25.003 1.00 29.45  ? 50  THR B N   1 
ATOM   1116 C CA  . THR B 1 51 ? 24.393  -11.727 -25.923 1.00 32.37  ? 50  THR B CA  1 
ATOM   1117 C C   . THR B 1 51 ? 24.838  -13.153 -25.606 1.00 34.65  ? 50  THR B C   1 
ATOM   1118 O O   . THR B 1 51 ? 24.738  -13.637 -24.472 1.00 34.85  ? 50  THR B O   1 
ATOM   1119 C CB  . THR B 1 51 ? 25.565  -10.741 -26.029 1.00 36.74  ? 50  THR B CB  1 
ATOM   1120 O OG1 . THR B 1 51 ? 26.151  -10.665 -24.745 1.00 35.33  ? 50  THR B OG1 1 
ATOM   1121 C CG2 . THR B 1 51 ? 25.132  -9.328  -26.374 1.00 30.75  ? 50  THR B CG2 1 
ATOM   1122 N N   . ALA B 1 52 ? 25.281  -13.862 -26.655 1.00 36.92  ? 51  ALA B N   1 
ATOM   1123 C CA  . ALA B 1 52 ? 25.981  -15.118 -26.475 1.00 36.22  ? 51  ALA B CA  1 
ATOM   1124 C C   . ALA B 1 52 ? 26.848  -15.398 -27.700 1.00 34.18  ? 51  ALA B C   1 
ATOM   1125 O O   . ALA B 1 52 ? 26.759  -14.683 -28.703 1.00 34.43  ? 51  ALA B O   1 
ATOM   1126 C CB  . ALA B 1 52 ? 25.029  -16.258 -26.163 1.00 32.35  ? 51  ALA B CB  1 
ATOM   1127 N N   . PHE B 1 53 ? 27.706  -16.415 -27.573 1.00 33.70  ? 52  PHE B N   1 
ATOM   1128 C CA  . PHE B 1 53 ? 28.480  -16.891 -28.709 1.00 37.44  ? 52  PHE B CA  1 
ATOM   1129 C C   . PHE B 1 53 ? 27.810  -18.144 -29.271 1.00 35.02  ? 52  PHE B C   1 
ATOM   1130 O O   . PHE B 1 53 ? 27.629  -19.123 -28.547 1.00 37.68  ? 52  PHE B O   1 
ATOM   1131 C CB  . PHE B 1 53 ? 29.933  -17.199 -28.321 1.00 35.42  ? 52  PHE B CB  1 
ATOM   1132 C CG  . PHE B 1 53 ? 30.729  -15.971 -27.920 1.00 40.22  ? 52  PHE B CG  1 
ATOM   1133 C CD1 . PHE B 1 53 ? 30.986  -14.958 -28.837 1.00 43.33  ? 52  PHE B CD1 1 
ATOM   1134 C CD2 . PHE B 1 53 ? 31.199  -15.831 -26.620 1.00 42.53  ? 52  PHE B CD2 1 
ATOM   1135 C CE1 . PHE B 1 53 ? 31.704  -13.829 -28.466 1.00 43.95  ? 52  PHE B CE1 1 
ATOM   1136 C CE2 . PHE B 1 53 ? 31.904  -14.700 -26.242 1.00 48.29  ? 52  PHE B CE2 1 
ATOM   1137 C CZ  . PHE B 1 53 ? 32.160  -13.711 -27.161 1.00 38.79  ? 52  PHE B CZ  1 
ATOM   1138 N N   . LEU B 1 54 ? 27.499  -18.137 -30.575 1.00 33.29  ? 53  LEU B N   1 
ATOM   1139 C CA  . LEU B 1 54 ? 26.892  -19.305 -31.191 1.00 29.75  ? 53  LEU B CA  1 
ATOM   1140 C C   . LEU B 1 54 ? 27.638  -19.688 -32.473 1.00 30.56  ? 53  LEU B C   1 
ATOM   1141 O O   . LEU B 1 54 ? 28.136  -18.812 -33.204 1.00 31.99  ? 53  LEU B O   1 
ATOM   1142 C CB  . LEU B 1 54 ? 25.403  -19.121 -31.519 1.00 31.45  ? 53  LEU B CB  1 
ATOM   1143 C CG  . LEU B 1 54 ? 24.414  -19.020 -30.361 1.00 31.37  ? 53  LEU B CG  1 
ATOM   1144 C CD1 . LEU B 1 54 ? 23.014  -18.725 -30.884 1.00 30.21  ? 53  LEU B CD1 1 
ATOM   1145 C CD2 . LEU B 1 54 ? 24.473  -20.415 -29.710 1.00 34.55  ? 53  LEU B CD2 1 
ATOM   1146 N N   . GLY B 1 55 ? 27.587  -21.003 -32.761 1.00 31.30  ? 54  GLY B N   1 
ATOM   1147 C CA  . GLY B 1 55 ? 28.050  -21.606 -34.007 1.00 29.26  ? 54  GLY B CA  1 
ATOM   1148 C C   . GLY B 1 55 ? 26.951  -21.640 -35.070 1.00 31.93  ? 54  GLY B C   1 
ATOM   1149 O O   . GLY B 1 55 ? 25.736  -21.542 -34.778 1.00 29.63  ? 54  GLY B O   1 
ATOM   1150 N N   . PRO B 1 56 ? 27.334  -21.768 -36.360 1.00 29.44  ? 55  PRO B N   1 
ATOM   1151 C CA  . PRO B 1 56 ? 26.362  -21.841 -37.444 1.00 30.06  ? 55  PRO B CA  1 
ATOM   1152 C C   . PRO B 1 56 ? 25.189  -22.808 -37.287 1.00 28.31  ? 55  PRO B C   1 
ATOM   1153 O O   . PRO B 1 56 ? 24.139  -22.550 -37.847 1.00 26.96  ? 55  PRO B O   1 
ATOM   1154 C CB  . PRO B 1 56 ? 27.186  -22.160 -38.703 1.00 34.83  ? 55  PRO B CB  1 
ATOM   1155 C CG  . PRO B 1 56 ? 28.636  -22.127 -38.287 1.00 34.84  ? 55  PRO B CG  1 
ATOM   1156 C CD  . PRO B 1 56 ? 28.736  -21.786 -36.826 1.00 31.32  ? 55  PRO B CD  1 
ATOM   1157 N N   . LYS B 1 57 ? 25.345  -23.911 -36.544 1.00 31.48  ? 56  LYS B N   1 
ATOM   1158 C CA  . LYS B 1 57 ? 24.273  -24.902 -36.530 1.00 30.82  ? 56  LYS B CA  1 
ATOM   1159 C C   . LYS B 1 57 ? 23.023  -24.284 -35.898 1.00 29.12  ? 56  LYS B C   1 
ATOM   1160 O O   . LYS B 1 57 ? 21.912  -24.772 -36.096 1.00 29.23  ? 56  LYS B O   1 
ATOM   1161 C CB  . LYS B 1 57 ? 24.722  -26.196 -35.832 1.00 36.30  ? 56  LYS B CB  1 
ATOM   1162 C CG  . LYS B 1 57 ? 24.875  -26.112 -34.319 1.00 37.96  ? 56  LYS B CG  1 
ATOM   1163 C CD  . LYS B 1 57 ? 24.977  -27.479 -33.637 1.00 43.32  ? 56  LYS B CD  1 
ATOM   1164 C CE  . LYS B 1 57 ? 25.268  -27.450 -32.150 1.00 42.81  ? 56  LYS B CE  1 
ATOM   1165 N NZ  . LYS B 1 57 ? 24.223  -26.833 -31.323 1.00 45.19  ? 56  LYS B NZ  1 
ATOM   1166 N N   . ASP B 1 58 ? 23.245  -23.213 -35.118 1.00 27.87  ? 57  ASP B N   1 
ATOM   1167 C CA  . ASP B 1 58 ? 22.212  -22.587 -34.315 1.00 28.88  ? 57  ASP B CA  1 
ATOM   1168 C C   . ASP B 1 58 ? 21.814  -21.240 -34.908 1.00 29.28  ? 57  ASP B C   1 
ATOM   1169 O O   . ASP B 1 58 ? 21.064  -20.493 -34.256 1.00 29.04  ? 57  ASP B O   1 
ATOM   1170 C CB  . ASP B 1 58 ? 22.660  -22.461 -32.871 1.00 28.85  ? 57  ASP B CB  1 
ATOM   1171 C CG  . ASP B 1 58 ? 22.758  -23.785 -32.118 1.00 36.66  ? 57  ASP B CG  1 
ATOM   1172 O OD1 . ASP B 1 58 ? 21.807  -24.594 -32.265 1.00 33.84  ? 57  ASP B OD1 1 
ATOM   1173 O OD2 . ASP B 1 58 ? 23.776  -23.977 -31.403 1.00 37.59  ? 57  ASP B OD2 1 
ATOM   1174 N N   . LEU B 1 59 ? 22.257  -20.986 -36.152 1.00 30.69  ? 58  LEU B N   1 
ATOM   1175 C CA  . LEU B 1 59 ? 22.038  -19.683 -36.776 1.00 29.57  ? 58  LEU B CA  1 
ATOM   1176 C C   . LEU B 1 59 ? 21.254  -19.821 -38.067 1.00 26.42  ? 58  LEU B C   1 
ATOM   1177 O O   . LEU B 1 59 ? 21.675  -20.510 -38.994 1.00 26.75  ? 58  LEU B O   1 
ATOM   1178 C CB  . LEU B 1 59 ? 23.362  -18.959 -37.012 1.00 30.61  ? 58  LEU B CB  1 
ATOM   1179 C CG  . LEU B 1 59 ? 24.171  -18.664 -35.748 1.00 27.69  ? 58  LEU B CG  1 
ATOM   1180 C CD1 . LEU B 1 59 ? 25.418  -17.910 -36.143 1.00 31.24  ? 58  LEU B CD1 1 
ATOM   1181 C CD2 . LEU B 1 59 ? 23.379  -17.849 -34.692 1.00 29.45  ? 58  LEU B CD2 1 
ATOM   1182 N N   . PHE B 1 60 ? 20.079  -19.194 -38.108 1.00 24.14  ? 59  PHE B N   1 
ATOM   1183 C CA  . PHE B 1 60 ? 19.167  -19.390 -39.220 1.00 26.60  ? 59  PHE B CA  1 
ATOM   1184 C C   . PHE B 1 60 ? 19.004  -18.045 -39.927 1.00 28.81  ? 59  PHE B C   1 
ATOM   1185 O O   . PHE B 1 60 ? 18.370  -17.156 -39.372 1.00 29.56  ? 59  PHE B O   1 
ATOM   1186 C CB  . PHE B 1 60 ? 17.811  -19.897 -38.704 1.00 22.80  ? 59  PHE B CB  1 
ATOM   1187 C CG  . PHE B 1 60 ? 17.891  -21.320 -38.128 1.00 24.15  ? 59  PHE B CG  1 
ATOM   1188 C CD1 . PHE B 1 60 ? 18.400  -21.543 -36.856 1.00 25.19  ? 59  PHE B CD1 1 
ATOM   1189 C CD2 . PHE B 1 60 ? 17.496  -22.414 -38.902 1.00 26.55  ? 59  PHE B CD2 1 
ATOM   1190 C CE1 . PHE B 1 60 ? 18.517  -22.836 -36.351 1.00 28.86  ? 59  PHE B CE1 1 
ATOM   1191 C CE2 . PHE B 1 60 ? 17.600  -23.710 -38.398 1.00 30.97  ? 59  PHE B CE2 1 
ATOM   1192 C CZ  . PHE B 1 60 ? 18.130  -23.921 -37.143 1.00 28.26  ? 59  PHE B CZ  1 
ATOM   1193 N N   . PRO B 1 61 ? 19.503  -17.861 -41.174 1.00 31.47  ? 60  PRO B N   1 
ATOM   1194 C CA  . PRO B 1 61 ? 19.254  -16.607 -41.904 1.00 31.21  ? 60  PRO B CA  1 
ATOM   1195 C C   . PRO B 1 61 ? 17.803  -16.131 -41.833 1.00 30.55  ? 60  PRO B C   1 
ATOM   1196 O O   . PRO B 1 61 ? 16.886  -16.892 -42.120 1.00 29.35  ? 60  PRO B O   1 
ATOM   1197 C CB  . PRO B 1 61 ? 19.728  -16.958 -43.325 1.00 30.15  ? 60  PRO B CB  1 
ATOM   1198 C CG  . PRO B 1 61 ? 20.909  -17.859 -43.059 1.00 34.75  ? 60  PRO B CG  1 
ATOM   1199 C CD  . PRO B 1 61 ? 20.354  -18.807 -41.941 1.00 32.26  ? 60  PRO B CD  1 
ATOM   1200 N N   . TYR B 1 62 ? 17.612  -14.840 -41.486 1.00 31.28  ? 61  TYR B N   1 
ATOM   1201 C CA  . TYR B 1 62 ? 16.316  -14.292 -41.143 1.00 33.41  ? 61  TYR B CA  1 
ATOM   1202 C C   . TYR B 1 62 ? 15.302  -14.367 -42.275 1.00 30.76  ? 61  TYR B C   1 
ATOM   1203 O O   . TYR B 1 62 ? 14.153  -14.757 -42.056 1.00 34.87  ? 61  TYR B O   1 
ATOM   1204 C CB  . TYR B 1 62 ? 16.470  -12.832 -40.705 1.00 35.86  ? 61  TYR B CB  1 
ATOM   1205 C CG  . TYR B 1 62 ? 15.137  -12.154 -40.434 1.00 35.34  ? 61  TYR B CG  1 
ATOM   1206 C CD1 . TYR B 1 62 ? 14.430  -12.395 -39.261 1.00 35.27  ? 61  TYR B CD1 1 
ATOM   1207 C CD2 . TYR B 1 62 ? 14.636  -11.207 -41.323 1.00 41.86  ? 61  TYR B CD2 1 
ATOM   1208 C CE1 . TYR B 1 62 ? 13.233  -11.740 -39.006 1.00 36.99  ? 61  TYR B CE1 1 
ATOM   1209 C CE2 . TYR B 1 62 ? 13.451  -10.534 -41.074 1.00 43.07  ? 61  TYR B CE2 1 
ATOM   1210 C CZ  . TYR B 1 62 ? 12.751  -10.806 -39.911 1.00 43.73  ? 61  TYR B CZ  1 
ATOM   1211 O OH  . TYR B 1 62 ? 11.583  -10.141 -39.687 1.00 43.17  ? 61  TYR B OH  1 
ATOM   1212 N N   . ASP B 1 63 ? 15.736  -13.986 -43.491 1.00 38.94  ? 62  ASP B N   1 
ATOM   1213 C CA  . ASP B 1 63 ? 14.880  -13.988 -44.672 1.00 41.21  ? 62  ASP B CA  1 
ATOM   1214 C C   . ASP B 1 63 ? 14.334  -15.376 -44.994 1.00 36.89  ? 62  ASP B C   1 
ATOM   1215 O O   . ASP B 1 63 ? 13.123  -15.540 -45.124 1.00 41.06  ? 62  ASP B O   1 
ATOM   1216 C CB  . ASP B 1 63 ? 15.543  -13.325 -45.862 1.00 48.99  ? 62  ASP B CB  1 
ATOM   1217 C CG  . ASP B 1 63 ? 14.971  -11.954 -46.171 1.00 60.63  ? 62  ASP B CG  1 
ATOM   1218 O OD1 . ASP B 1 63 ? 14.835  -11.144 -45.220 1.00 61.75  ? 62  ASP B OD1 1 
ATOM   1219 O OD2 . ASP B 1 63 ? 14.641  -11.728 -47.355 1.00 73.01  ? 62  ASP B OD2 1 
ATOM   1220 N N   . LYS B 1 64 ? 15.218  -16.362 -45.099 1.00 37.76  ? 63  LYS B N   1 
ATOM   1221 C CA  . LYS B 1 64 ? 14.794  -17.726 -45.352 1.00 42.10  ? 63  LYS B CA  1 
ATOM   1222 C C   . LYS B 1 64 ? 13.783  -18.189 -44.305 1.00 37.82  ? 63  LYS B C   1 
ATOM   1223 O O   . LYS B 1 64 ? 12.872  -18.958 -44.618 1.00 41.47  ? 63  LYS B O   1 
ATOM   1224 C CB  . LYS B 1 64 ? 16.001  -18.670 -45.345 1.00 49.33  ? 63  LYS B CB  1 
ATOM   1225 C CG  . LYS B 1 64 ? 15.682  -20.068 -45.849 1.00 45.32  ? 63  LYS B CG  1 
ATOM   1226 C CD  . LYS B 1 64 ? 16.870  -21.011 -45.719 1.00 51.13  ? 63  LYS B CD  1 
ATOM   1227 C CE  . LYS B 1 64 ? 16.671  -22.364 -46.362 1.00 44.08  ? 63  LYS B CE  1 
ATOM   1228 N NZ  . LYS B 1 64 ? 15.350  -22.960 -46.148 1.00 43.03  ? 63  LYS B NZ  1 
ATOM   1229 N N   . SER B 1 65 ? 13.925  -17.736 -43.058 1.00 38.92  ? 64  SER B N   1 
ATOM   1230 C CA  . SER B 1 65 ? 13.238  -18.474 -41.994 1.00 41.05  ? 64  SER B CA  1 
ATOM   1231 C C   . SER B 1 65 ? 12.160  -17.682 -41.245 1.00 37.08  ? 64  SER B C   1 
ATOM   1232 O O   . SER B 1 65 ? 11.541  -18.217 -40.327 1.00 38.91  ? 64  SER B O   1 
ATOM   1233 C CB  . SER B 1 65 ? 14.215  -19.142 -41.081 1.00 40.72  ? 64  SER B CB  1 
ATOM   1234 O OG  . SER B 1 65 ? 15.131  -18.173 -40.607 1.00 55.79  ? 64  SER B OG  1 
ATOM   1235 N N   . LYS B 1 66 ? 11.843  -16.453 -41.687 1.00 37.06  ? 65  LYS B N   1 
ATOM   1236 C CA  . LYS B 1 66 ? 10.976  -15.596 -40.886 1.00 33.60  ? 65  LYS B CA  1 
ATOM   1237 C C   . LYS B 1 66 ? 9.535   -16.111 -40.840 1.00 37.20  ? 65  LYS B C   1 
ATOM   1238 O O   . LYS B 1 66 ? 8.829   -15.897 -39.871 1.00 38.88  ? 65  LYS B O   1 
ATOM   1239 C CB  . LYS B 1 66 ? 10.982  -14.113 -41.285 1.00 35.44  ? 65  LYS B CB  1 
ATOM   1240 C CG  . LYS B 1 66 ? 10.572  -13.837 -42.741 1.00 36.41  ? 65  LYS B CG  1 
ATOM   1241 N N   . ASP B 1 67 ? 9.059   -16.786 -41.875 1.00 38.47  ? 66  ASP B N   1 
ATOM   1242 C CA  . ASP B 1 67 ? 7.651   -17.117 -41.769 1.00 45.62  ? 66  ASP B CA  1 
ATOM   1243 C C   . ASP B 1 67 ? 7.477   -18.341 -40.863 1.00 45.17  ? 66  ASP B C   1 
ATOM   1244 O O   . ASP B 1 67 ? 6.409   -18.540 -40.276 1.00 45.17  ? 66  ASP B O   1 
ATOM   1245 C CB  . ASP B 1 67 ? 6.940   -16.985 -43.106 1.00 60.20  ? 66  ASP B CB  1 
ATOM   1246 C CG  . ASP B 1 67 ? 7.537   -17.809 -44.230 1.00 72.05  ? 66  ASP B CG  1 
ATOM   1247 O OD1 . ASP B 1 67 ? 7.226   -17.520 -45.413 1.00 76.82  ? 66  ASP B OD1 1 
ATOM   1248 O OD2 . ASP B 1 67 ? 8.300   -18.738 -43.903 1.00 75.26  ? 66  ASP B OD2 1 
ATOM   1249 N N   . LYS B 1 68 ? 8.556   -19.120 -40.707 1.00 38.99  ? 67  LYS B N   1 
ATOM   1250 C CA  . LYS B 1 68 ? 8.535   -20.280 -39.827 1.00 36.22  ? 67  LYS B CA  1 
ATOM   1251 C C   . LYS B 1 68 ? 8.726   -19.864 -38.369 1.00 33.80  ? 67  LYS B C   1 
ATOM   1252 O O   . LYS B 1 68 ? 7.944   -20.284 -37.509 1.00 35.59  ? 67  LYS B O   1 
ATOM   1253 C CB  . LYS B 1 68 ? 9.564   -21.296 -40.334 1.00 39.57  ? 67  LYS B CB  1 
ATOM   1254 C CG  . LYS B 1 68 ? 9.777   -22.518 -39.452 1.00 44.69  ? 67  LYS B CG  1 
ATOM   1255 C CD  . LYS B 1 68 ? 10.478  -23.595 -40.273 1.00 55.03  ? 67  LYS B CD  1 
ATOM   1256 C CE  . LYS B 1 68 ? 10.923  -24.808 -39.510 1.00 62.75  ? 67  LYS B CE  1 
ATOM   1257 N NZ  . LYS B 1 68 ? 9.808   -25.678 -39.126 1.00 61.43  ? 67  LYS B NZ  1 
ATOM   1258 N N   . TYR B 1 69 ? 9.738   -19.021 -38.088 1.00 30.24  ? 68  TYR B N   1 
ATOM   1259 C CA  . TYR B 1 69 ? 10.179  -18.750 -36.720 1.00 28.09  ? 68  TYR B CA  1 
ATOM   1260 C C   . TYR B 1 69 ? 9.696   -17.391 -36.225 1.00 29.30  ? 68  TYR B C   1 
ATOM   1261 O O   . TYR B 1 69 ? 9.830   -17.103 -35.026 1.00 33.10  ? 68  TYR B O   1 
ATOM   1262 C CB  . TYR B 1 69 ? 11.702  -18.840 -36.529 1.00 27.49  ? 68  TYR B CB  1 
ATOM   1263 C CG  . TYR B 1 69 ? 12.305  -20.210 -36.820 1.00 32.65  ? 68  TYR B CG  1 
ATOM   1264 C CD1 . TYR B 1 69 ? 11.763  -21.377 -36.279 1.00 35.99  ? 68  TYR B CD1 1 
ATOM   1265 C CD2 . TYR B 1 69 ? 13.403  -20.343 -37.665 1.00 35.77  ? 68  TYR B CD2 1 
ATOM   1266 C CE1 . TYR B 1 69 ? 12.310  -22.629 -36.550 1.00 34.35  ? 68  TYR B CE1 1 
ATOM   1267 C CE2 . TYR B 1 69 ? 13.956  -21.584 -37.948 1.00 36.99  ? 68  TYR B CE2 1 
ATOM   1268 C CZ  . TYR B 1 69 ? 13.416  -22.726 -37.373 1.00 38.38  ? 68  TYR B CZ  1 
ATOM   1269 O OH  . TYR B 1 69 ? 13.950  -23.942 -37.677 1.00 33.90  ? 68  TYR B OH  1 
ATOM   1270 N N   . GLY B 1 70 ? 9.163   -16.547 -37.122 1.00 29.90  ? 69  GLY B N   1 
ATOM   1271 C CA  . GLY B 1 70 ? 8.898   -15.178 -36.706 1.00 34.50  ? 69  GLY B CA  1 
ATOM   1272 C C   . GLY B 1 70 ? 7.465   -14.942 -36.212 1.00 38.19  ? 69  GLY B C   1 
ATOM   1273 O O   . GLY B 1 70 ? 6.888   -13.909 -36.543 1.00 36.30  ? 69  GLY B O   1 
ATOM   1274 N N   . LYS B 1 71 ? 6.902   -15.885 -35.437 1.00 39.34  ? 70  LYS B N   1 
ATOM   1275 C CA  . LYS B 1 71 ? 5.547   -15.775 -34.915 1.00 42.68  ? 70  LYS B CA  1 
ATOM   1276 C C   . LYS B 1 71 ? 5.603   -15.337 -33.461 1.00 40.80  ? 70  LYS B C   1 
ATOM   1277 O O   . LYS B 1 71 ? 6.474   -15.802 -32.721 1.00 40.43  ? 70  LYS B O   1 
ATOM   1278 C CB  . LYS B 1 71 ? 4.804   -17.107 -34.773 1.00 48.27  ? 70  LYS B CB  1 
ATOM   1279 C CG  . LYS B 1 71 ? 3.800   -17.467 -35.854 1.00 61.46  ? 70  LYS B CG  1 
ATOM   1280 C CD  . LYS B 1 71 ? 4.445   -17.878 -37.169 1.00 63.02  ? 70  LYS B CD  1 
ATOM   1281 C CE  . LYS B 1 71 ? 3.436   -18.369 -38.157 1.00 68.74  ? 70  LYS B CE  1 
ATOM   1282 N NZ  . LYS B 1 71 ? 3.978   -18.268 -39.514 1.00 73.21  ? 70  LYS B NZ  1 
ATOM   1283 N N   . PRO B 1 72 ? 4.675   -14.465 -32.997 1.00 39.59  ? 71  PRO B N   1 
ATOM   1284 C CA  . PRO B 1 72 ? 4.647   -14.069 -31.586 1.00 35.90  ? 71  PRO B CA  1 
ATOM   1285 C C   . PRO B 1 72 ? 4.453   -15.277 -30.666 1.00 34.81  ? 71  PRO B C   1 
ATOM   1286 O O   . PRO B 1 72 ? 3.919   -16.308 -31.080 1.00 36.50  ? 71  PRO B O   1 
ATOM   1287 C CB  . PRO B 1 72 ? 3.536   -13.009 -31.509 1.00 38.16  ? 71  PRO B CB  1 
ATOM   1288 C CG  . PRO B 1 72 ? 3.498   -12.473 -32.926 1.00 41.71  ? 71  PRO B CG  1 
ATOM   1289 C CD  . PRO B 1 72 ? 3.698   -13.722 -33.813 1.00 40.39  ? 71  PRO B CD  1 
ATOM   1290 N N   . ASN B 1 73 ? 5.004   -15.167 -29.453 1.00 36.84  ? 72  ASN B N   1 
ATOM   1291 C CA  . ASN B 1 73 ? 4.800   -16.153 -28.402 1.00 34.58  ? 72  ASN B CA  1 
ATOM   1292 C C   . ASN B 1 73 ? 4.753   -15.407 -27.061 1.00 40.47  ? 72  ASN B C   1 
ATOM   1293 O O   . ASN B 1 73 ? 4.791   -14.169 -27.016 1.00 43.82  ? 72  ASN B O   1 
ATOM   1294 C CB  . ASN B 1 73 ? 5.817   -17.293 -28.477 1.00 35.01  ? 72  ASN B CB  1 
ATOM   1295 C CG  . ASN B 1 73 ? 7.234   -16.836 -28.208 1.00 36.68  ? 72  ASN B CG  1 
ATOM   1296 O OD1 . ASN B 1 73 ? 7.469   -16.087 -27.255 1.00 35.92  ? 72  ASN B OD1 1 
ATOM   1297 N ND2 . ASN B 1 73 ? 8.191   -17.236 -29.047 1.00 32.44  ? 72  ASN B ND2 1 
ATOM   1298 N N   . LYS B 1 74 ? 4.709   -16.164 -25.961 1.00 42.42  ? 73  LYS B N   1 
ATOM   1299 C CA  . LYS B 1 74 ? 4.560   -15.565 -24.637 1.00 46.18  ? 73  LYS B CA  1 
ATOM   1300 C C   . LYS B 1 74 ? 5.895   -15.466 -23.888 1.00 42.20  ? 73  LYS B C   1 
ATOM   1301 O O   . LYS B 1 74 ? 5.887   -15.268 -22.675 1.00 43.25  ? 73  LYS B O   1 
ATOM   1302 C CB  . LYS B 1 74 ? 3.592   -16.375 -23.761 1.00 46.75  ? 73  LYS B CB  1 
ATOM   1303 C CG  . LYS B 1 74 ? 2.217   -16.704 -24.316 1.00 53.19  ? 73  LYS B CG  1 
ATOM   1304 C CD  . LYS B 1 74 ? 1.624   -17.942 -23.640 1.00 59.97  ? 73  LYS B CD  1 
ATOM   1305 N N   . ARG B 1 75 ? 7.038   -15.631 -24.571 1.00 33.15  ? 74  ARG B N   1 
ATOM   1306 C CA  . ARG B 1 75 ? 8.315   -15.495 -23.882 1.00 30.08  ? 74  ARG B CA  1 
ATOM   1307 C C   . ARG B 1 75 ? 8.686   -14.015 -23.747 1.00 35.12  ? 74  ARG B C   1 
ATOM   1308 O O   . ARG B 1 75 ? 8.558   -13.229 -24.696 1.00 36.61  ? 74  ARG B O   1 
ATOM   1309 C CB  . ARG B 1 75 ? 9.457   -16.304 -24.516 1.00 29.80  ? 74  ARG B CB  1 
ATOM   1310 C CG  . ARG B 1 75 ? 9.319   -17.808 -24.743 1.00 30.80  ? 74  ARG B CG  1 
ATOM   1311 C CD  . ARG B 1 75 ? 9.115   -18.605 -23.475 1.00 33.20  ? 74  ARG B CD  1 
ATOM   1312 N NE  . ARG B 1 75 ? 9.351   -20.019 -23.779 1.00 34.60  ? 74  ARG B NE  1 
ATOM   1313 C CZ  . ARG B 1 75 ? 10.428  -20.706 -23.498 1.00 38.46  ? 74  ARG B CZ  1 
ATOM   1314 N NH1 . ARG B 1 75 ? 11.478  -20.116 -22.947 1.00 40.37  ? 74  ARG B NH1 1 
ATOM   1315 N NH2 . ARG B 1 75 ? 10.487  -21.966 -23.882 1.00 41.43  ? 74  ARG B NH2 1 
ATOM   1316 N N   . LYS B 1 76 ? 9.133   -13.639 -22.538 1.00 32.44  ? 75  LYS B N   1 
ATOM   1317 C CA  . LYS B 1 76 ? 9.507   -12.272 -22.216 1.00 30.72  ? 75  LYS B CA  1 
ATOM   1318 C C   . LYS B 1 76 ? 10.606  -11.781 -23.164 1.00 27.15  ? 75  LYS B C   1 
ATOM   1319 O O   . LYS B 1 76 ? 11.707  -12.380 -23.225 1.00 27.44  ? 75  LYS B O   1 
ATOM   1320 C CB  . LYS B 1 76 ? 10.085  -12.177 -20.792 1.00 34.27  ? 75  LYS B CB  1 
ATOM   1321 C CG  . LYS B 1 76 ? 10.442  -10.729 -20.391 1.00 30.50  ? 75  LYS B CG  1 
ATOM   1322 C CD  . LYS B 1 76 ? 10.884  -10.610 -18.938 1.00 36.29  ? 75  LYS B CD  1 
ATOM   1323 C CE  . LYS B 1 76 ? 11.017  -9.203  -18.401 1.00 38.55  ? 75  LYS B CE  1 
ATOM   1324 N NZ  . LYS B 1 76 ? 11.593  -9.190  -17.041 1.00 44.90  ? 75  LYS B NZ  1 
ATOM   1325 N N   . GLY B 1 77 ? 10.284  -10.678 -23.845 1.00 26.70  ? 76  GLY B N   1 
ATOM   1326 C CA  . GLY B 1 77 ? 11.232  -10.021 -24.742 1.00 28.71  ? 76  GLY B CA  1 
ATOM   1327 C C   . GLY B 1 77 ? 11.112  -10.499 -26.194 1.00 30.84  ? 76  GLY B C   1 
ATOM   1328 O O   . GLY B 1 77 ? 11.672  -9.864  -27.082 1.00 32.35  ? 76  GLY B O   1 
ATOM   1329 N N   . PHE B 1 78 ? 10.405  -11.618 -26.446 1.00 27.29  ? 77  PHE B N   1 
ATOM   1330 C CA  . PHE B 1 78 ? 10.313  -12.131 -27.818 1.00 25.49  ? 77  PHE B CA  1 
ATOM   1331 C C   . PHE B 1 78 ? 9.536   -11.202 -28.752 1.00 28.07  ? 77  PHE B C   1 
ATOM   1332 O O   . PHE B 1 78 ? 9.964   -10.922 -29.869 1.00 26.95  ? 77  PHE B O   1 
ATOM   1333 C CB  . PHE B 1 78 ? 9.584   -13.478 -27.803 1.00 27.58  ? 77  PHE B CB  1 
ATOM   1334 C CG  . PHE B 1 78 ? 9.808   -14.216 -29.109 1.00 26.71  ? 77  PHE B CG  1 
ATOM   1335 C CD1 . PHE B 1 78 ? 10.880  -15.094 -29.235 1.00 26.92  ? 77  PHE B CD1 1 
ATOM   1336 C CD2 . PHE B 1 78 ? 8.935   -14.058 -30.177 1.00 28.99  ? 77  PHE B CD2 1 
ATOM   1337 C CE1 . PHE B 1 78 ? 11.117  -15.765 -30.433 1.00 28.15  ? 77  PHE B CE1 1 
ATOM   1338 C CE2 . PHE B 1 78 ? 9.159   -14.750 -31.367 1.00 28.51  ? 77  PHE B CE2 1 
ATOM   1339 C CZ  . PHE B 1 78 ? 10.261  -15.588 -31.488 1.00 29.57  ? 77  PHE B CZ  1 
ATOM   1340 N N   . ASN B 1 79 ? 8.340   -10.754 -28.374 1.00 28.23  ? 78  ASN B N   1 
ATOM   1341 C CA  . ASN B 1 79 ? 7.597   -9.920  -29.318 1.00 32.83  ? 78  ASN B CA  1 
ATOM   1342 C C   . ASN B 1 79 ? 8.278   -8.551  -29.495 1.00 30.86  ? 78  ASN B C   1 
ATOM   1343 O O   . ASN B 1 79 ? 8.241   -7.964  -30.579 1.00 31.98  ? 78  ASN B O   1 
ATOM   1344 C CB  . ASN B 1 79 ? 6.122   -9.783  -28.949 1.00 31.44  ? 78  ASN B CB  1 
ATOM   1345 C CG  . ASN B 1 79 ? 5.374   -11.099 -28.940 1.00 38.92  ? 78  ASN B CG  1 
ATOM   1346 O OD1 . ASN B 1 79 ? 5.858   -12.096 -29.487 1.00 39.65  ? 78  ASN B OD1 1 
ATOM   1347 N ND2 . ASN B 1 79 ? 4.190   -11.128 -28.334 1.00 37.45  ? 78  ASN B ND2 1 
ATOM   1348 N N   . GLU B 1 80 ? 8.940   -8.053  -28.455 1.00 33.97  ? 79  GLU B N   1 
ATOM   1349 C CA  . GLU B 1 80 ? 9.708   -6.830  -28.622 1.00 34.90  ? 79  GLU B CA  1 
ATOM   1350 C C   . GLU B 1 80 ? 10.830  -7.075  -29.629 1.00 34.53  ? 79  GLU B C   1 
ATOM   1351 O O   . GLU B 1 80 ? 11.136  -6.185  -30.427 1.00 33.12  ? 79  GLU B O   1 
ATOM   1352 C CB  . GLU B 1 80 ? 10.376  -6.308  -27.356 1.00 33.14  ? 79  GLU B CB  1 
ATOM   1353 C CG  . GLU B 1 80 ? 9.367   -5.656  -26.417 1.00 42.28  ? 79  GLU B CG  1 
ATOM   1354 N N   . GLY B 1 81 ? 11.417  -8.282  -29.572 1.00 29.84  ? 80  GLY B N   1 
ATOM   1355 C CA  . GLY B 1 81 ? 12.504  -8.680  -30.459 1.00 30.99  ? 80  GLY B CA  1 
ATOM   1356 C C   . GLY B 1 81 ? 12.026  -8.740  -31.907 1.00 31.97  ? 80  GLY B C   1 
ATOM   1357 O O   . GLY B 1 81 ? 12.742  -8.349  -32.839 1.00 30.88  ? 80  GLY B O   1 
ATOM   1358 N N   . LEU B 1 82 ? 10.797  -9.212  -32.095 1.00 28.86  ? 81  LEU B N   1 
ATOM   1359 C CA  . LEU B 1 82 ? 10.224  -9.226  -33.434 1.00 33.07  ? 81  LEU B CA  1 
ATOM   1360 C C   . LEU B 1 82 ? 10.082  -7.788  -33.929 1.00 31.19  ? 81  LEU B C   1 
ATOM   1361 O O   . LEU B 1 82 ? 10.269  -7.540  -35.120 1.00 32.19  ? 81  LEU B O   1 
ATOM   1362 C CB  . LEU B 1 82 ? 8.875   -9.956  -33.496 1.00 30.37  ? 81  LEU B CB  1 
ATOM   1363 C CG  . LEU B 1 82 ? 8.925   -11.471 -33.263 1.00 29.86  ? 81  LEU B CG  1 
ATOM   1364 C CD1 . LEU B 1 82 ? 7.533   -12.092 -33.234 1.00 29.65  ? 81  LEU B CD1 1 
ATOM   1365 C CD2 . LEU B 1 82 ? 9.803   -12.165 -34.276 1.00 28.20  ? 81  LEU B CD2 1 
ATOM   1366 N N   . TRP B 1 83 ? 9.696   -6.868  -33.033 1.00 30.76  ? 82  TRP B N   1 
ATOM   1367 C CA  . TRP B 1 83 ? 9.529   -5.461  -33.379 1.00 32.43  ? 82  TRP B CA  1 
ATOM   1368 C C   . TRP B 1 83 ? 10.853  -4.879  -33.863 1.00 31.38  ? 82  TRP B C   1 
ATOM   1369 O O   . TRP B 1 83 ? 10.885  -4.241  -34.923 1.00 32.42  ? 82  TRP B O   1 
ATOM   1370 C CB  . TRP B 1 83 ? 8.932   -4.601  -32.244 1.00 34.02  ? 82  TRP B CB  1 
ATOM   1371 C CG  . TRP B 1 83 ? 8.656   -3.199  -32.734 1.00 34.18  ? 82  TRP B CG  1 
ATOM   1372 C CD1 . TRP B 1 83 ? 7.521   -2.724  -33.316 1.00 38.57  ? 82  TRP B CD1 1 
ATOM   1373 C CD2 . TRP B 1 83 ? 9.606   -2.107  -32.754 1.00 38.44  ? 82  TRP B CD2 1 
ATOM   1374 N NE1 . TRP B 1 83 ? 7.699   -1.414  -33.695 1.00 40.46  ? 82  TRP B NE1 1 
ATOM   1375 C CE2 . TRP B 1 83 ? 8.966   -1.009  -33.358 1.00 39.06  ? 82  TRP B CE2 1 
ATOM   1376 C CE3 . TRP B 1 83 ? 10.932  -1.952  -32.311 1.00 38.08  ? 82  TRP B CE3 1 
ATOM   1377 C CZ2 . TRP B 1 83 ? 9.607   0.225   -33.517 1.00 37.49  ? 82  TRP B CZ2 1 
ATOM   1378 C CZ3 . TRP B 1 83 ? 11.564  -0.737  -32.470 1.00 41.08  ? 82  TRP B CZ3 1 
ATOM   1379 C CH2 . TRP B 1 83 ? 10.912  0.331   -33.085 1.00 35.23  ? 82  TRP B CH2 1 
ATOM   1380 N N   . GLU B 1 84 ? 11.926  -5.163  -33.110 1.00 31.21  ? 83  GLU B N   1 
ATOM   1381 C CA  . GLU B 1 84 ? 13.242  -4.590  -33.353 1.00 31.83  ? 83  GLU B CA  1 
ATOM   1382 C C   . GLU B 1 84 ? 13.826  -5.107  -34.665 1.00 34.00  ? 83  GLU B C   1 
ATOM   1383 O O   . GLU B 1 84 ? 14.396  -4.324  -35.432 1.00 34.13  ? 83  GLU B O   1 
ATOM   1384 C CB  . GLU B 1 84 ? 14.194  -4.855  -32.190 1.00 28.51  ? 83  GLU B CB  1 
ATOM   1385 C CG  . GLU B 1 84 ? 13.741  -4.187  -30.885 1.00 30.17  ? 83  GLU B CG  1 
ATOM   1386 C CD  . GLU B 1 84 ? 14.629  -4.523  -29.714 1.00 32.46  ? 83  GLU B CD  1 
ATOM   1387 O OE1 . GLU B 1 84 ? 15.517  -5.389  -29.887 1.00 31.16  ? 83  GLU B OE1 1 
ATOM   1388 O OE2 . GLU B 1 84 ? 14.501  -3.893  -28.627 1.00 34.11  ? 83  GLU B OE2 1 
ATOM   1389 N N   . ILE B 1 85 ? 13.727  -6.421  -34.900 1.00 31.82  ? 84  ILE B N   1 
ATOM   1390 C CA  . ILE B 1 85 ? 14.391  -6.986  -36.073 1.00 30.68  ? 84  ILE B CA  1 
ATOM   1391 C C   . ILE B 1 85 ? 13.717  -6.447  -37.325 1.00 27.00  ? 84  ILE B C   1 
ATOM   1392 O O   . ILE B 1 85 ? 14.361  -6.245  -38.357 1.00 28.41  ? 84  ILE B O   1 
ATOM   1393 C CB  . ILE B 1 85 ? 14.481  -8.521  -36.067 1.00 29.37  ? 84  ILE B CB  1 
ATOM   1394 C CG1 . ILE B 1 85 ? 15.557  -9.014  -37.051 1.00 29.85  ? 84  ILE B CG1 1 
ATOM   1395 C CG2 . ILE B 1 85 ? 13.125  -9.169  -36.332 1.00 29.67  ? 84  ILE B CG2 1 
ATOM   1396 C CD1 . ILE B 1 85 ? 16.000  -10.450 -36.817 1.00 28.91  ? 84  ILE B CD1 1 
ATOM   1397 N N   . GLN B 1 86 ? 12.416  -6.182  -37.209 1.00 30.71  ? 85  GLN B N   1 
ATOM   1398 C CA  . GLN B 1 86 ? 11.640  -5.601  -38.292 1.00 31.31  ? 85  GLN B CA  1 
ATOM   1399 C C   . GLN B 1 86 ? 11.931  -4.111  -38.480 1.00 30.92  ? 85  GLN B C   1 
ATOM   1400 O O   . GLN B 1 86 ? 12.020  -3.637  -39.607 1.00 33.80  ? 85  GLN B O   1 
ATOM   1401 C CB  . GLN B 1 86 ? 10.152  -5.883  -38.052 1.00 34.69  ? 85  GLN B CB  1 
ATOM   1402 N N   . ASN B 1 87 ? 12.034  -3.338  -37.405 1.00 30.29  ? 86  ASN B N   1 
ATOM   1403 C CA  . ASN B 1 87 ? 11.864  -1.893  -37.579 1.00 32.91  ? 86  ASN B CA  1 
ATOM   1404 C C   . ASN B 1 87 ? 13.166  -1.125  -37.409 1.00 32.97  ? 86  ASN B C   1 
ATOM   1405 O O   . ASN B 1 87 ? 13.305  -0.009  -37.938 1.00 36.21  ? 86  ASN B O   1 
ATOM   1406 C CB  . ASN B 1 87 ? 10.835  -1.361  -36.586 1.00 37.22  ? 86  ASN B CB  1 
ATOM   1407 C CG  . ASN B 1 87 ? 9.475   -1.875  -36.973 1.00 40.23  ? 86  ASN B CG  1 
ATOM   1408 O OD1 . ASN B 1 87 ? 8.888   -1.371  -37.930 1.00 46.37  ? 86  ASN B OD1 1 
ATOM   1409 N ND2 . ASN B 1 87 ? 8.993   -2.917  -36.309 1.00 43.98  ? 86  ASN B ND2 1 
ATOM   1410 N N   . ASN B 1 88 ? 14.107  -1.705  -36.659 1.00 29.21  ? 87  ASN B N   1 
ATOM   1411 C CA  . ASN B 1 88 ? 15.392  -1.046  -36.433 1.00 31.88  ? 87  ASN B CA  1 
ATOM   1412 C C   . ASN B 1 88 ? 16.461  -2.056  -36.024 1.00 29.59  ? 87  ASN B C   1 
ATOM   1413 O O   . ASN B 1 88 ? 17.120  -1.934  -34.978 1.00 28.65  ? 87  ASN B O   1 
ATOM   1414 C CB  . ASN B 1 88 ? 15.278  0.129   -35.461 1.00 36.33  ? 87  ASN B CB  1 
ATOM   1415 C CG  . ASN B 1 88 ? 16.354  1.173   -35.668 1.00 38.11  ? 87  ASN B CG  1 
ATOM   1416 O OD1 . ASN B 1 88 ? 17.402  0.933   -36.289 1.00 33.97  ? 87  ASN B OD1 1 
ATOM   1417 N ND2 . ASN B 1 88 ? 16.115  2.352   -35.119 1.00 37.94  ? 87  ASN B ND2 1 
ATOM   1418 N N   . PRO B 1 89 ? 16.775  -3.018  -36.928 1.00 28.65  ? 88  PRO B N   1 
ATOM   1419 C CA  . PRO B 1 89 ? 17.700  -4.101  -36.605 1.00 27.49  ? 88  PRO B CA  1 
ATOM   1420 C C   . PRO B 1 89 ? 19.141  -3.676  -36.345 1.00 26.69  ? 88  PRO B C   1 
ATOM   1421 O O   . PRO B 1 89 ? 19.922  -4.418  -35.742 1.00 26.55  ? 88  PRO B O   1 
ATOM   1422 C CB  . PRO B 1 89 ? 17.575  -5.024  -37.868 1.00 25.23  ? 88  PRO B CB  1 
ATOM   1423 C CG  . PRO B 1 89 ? 17.194  -4.085  -38.997 1.00 26.20  ? 88  PRO B CG  1 
ATOM   1424 C CD  . PRO B 1 89 ? 16.281  -3.074  -38.313 1.00 26.42  ? 88  PRO B CD  1 
ATOM   1425 N N   . HIS B 1 90 ? 19.515  -2.481  -36.861 1.00 28.00  ? 89  HIS B N   1 
ATOM   1426 C CA  . HIS B 1 90 ? 20.912  -2.075  -36.817 1.00 26.00  ? 89  HIS B CA  1 
ATOM   1427 C C   . HIS B 1 90 ? 21.174  -1.000  -35.755 1.00 30.81  ? 89  HIS B C   1 
ATOM   1428 O O   . HIS B 1 90 ? 22.300  -0.495  -35.676 1.00 29.94  ? 89  HIS B O   1 
ATOM   1429 C CB  . HIS B 1 90 ? 21.387  -1.623  -38.210 1.00 25.95  ? 89  HIS B CB  1 
ATOM   1430 C CG  . HIS B 1 90 ? 21.220  -2.707  -39.235 1.00 27.70  ? 89  HIS B CG  1 
ATOM   1431 N ND1 . HIS B 1 90 ? 21.785  -3.952  -39.094 1.00 26.38  ? 89  HIS B ND1 1 
ATOM   1432 C CD2 . HIS B 1 90 ? 20.585  -2.736  -40.396 1.00 28.15  ? 89  HIS B CD2 1 
ATOM   1433 C CE1 . HIS B 1 90 ? 21.472  -4.697  -40.130 1.00 25.89  ? 89  HIS B CE1 1 
ATOM   1434 N NE2 . HIS B 1 90 ? 20.772  -3.967  -40.932 1.00 26.97  ? 89  HIS B NE2 1 
ATOM   1435 N N   . ALA B 1 91 ? 20.172  -0.704  -34.912 1.00 31.37  ? 90  ALA B N   1 
ATOM   1436 C CA  . ALA B 1 91 ? 20.297  0.323   -33.875 1.00 29.75  ? 90  ALA B CA  1 
ATOM   1437 C C   . ALA B 1 91 ? 21.267  -0.060  -32.754 1.00 34.75  ? 90  ALA B C   1 
ATOM   1438 O O   . ALA B 1 91 ? 21.564  -1.226  -32.497 1.00 31.51  ? 90  ALA B O   1 
ATOM   1439 C CB  . ALA B 1 91 ? 18.927  0.676   -33.322 1.00 26.59  ? 90  ALA B CB  1 
ATOM   1440 N N   . SER B 1 92 ? 21.757  0.966   -32.034 1.00 33.83  ? 91  SER B N   1 
ATOM   1441 C CA  . SER B 1 92 ? 22.396  0.768   -30.751 1.00 36.58  ? 91  SER B CA  1 
ATOM   1442 C C   . SER B 1 92 ? 21.326  0.522   -29.682 1.00 41.33  ? 91  SER B C   1 
ATOM   1443 O O   . SER B 1 92 ? 20.419  1.343   -29.511 1.00 42.42  ? 91  SER B O   1 
ATOM   1444 C CB  . SER B 1 92 ? 23.209  2.020   -30.406 1.00 40.57  ? 91  SER B CB  1 
ATOM   1445 O OG  . SER B 1 92 ? 23.728  1.894   -29.100 1.00 45.31  ? 91  SER B OG  1 
ATOM   1446 N N   . TYR B 1 93 ? 21.463  -0.604  -28.966 1.00 38.80  ? 92  TYR B N   1 
ATOM   1447 C CA  . TYR B 1 93 ? 20.603  -1.038  -27.879 1.00 45.11  ? 92  TYR B CA  1 
ATOM   1448 C C   . TYR B 1 93 ? 21.371  -0.919  -26.565 1.00 53.92  ? 92  TYR B C   1 
ATOM   1449 O O   . TYR B 1 93 ? 20.948  -1.454  -25.548 1.00 54.78  ? 92  TYR B O   1 
ATOM   1450 C CB  . TYR B 1 93 ? 20.042  -2.438  -28.185 1.00 38.30  ? 92  TYR B CB  1 
ATOM   1451 C CG  . TYR B 1 93 ? 19.010  -2.351  -29.295 1.00 33.74  ? 92  TYR B CG  1 
ATOM   1452 C CD1 . TYR B 1 93 ? 17.736  -1.864  -29.036 1.00 32.98  ? 92  TYR B CD1 1 
ATOM   1453 C CD2 . TYR B 1 93 ? 19.310  -2.726  -30.608 1.00 33.34  ? 92  TYR B CD2 1 
ATOM   1454 C CE1 . TYR B 1 93 ? 16.794  -1.703  -30.032 1.00 32.19  ? 92  TYR B CE1 1 
ATOM   1455 C CE2 . TYR B 1 93 ? 18.372  -2.559  -31.621 1.00 31.33  ? 92  TYR B CE2 1 
ATOM   1456 C CZ  . TYR B 1 93 ? 17.111  -2.073  -31.326 1.00 32.01  ? 92  TYR B CZ  1 
ATOM   1457 O OH  . TYR B 1 93 ? 16.130  -1.953  -32.262 1.00 32.05  ? 92  TYR B OH  1 
ATOM   1458 N N   . SER B 1 94 ? 22.492  -0.184  -26.611 1.00 73.52  ? 93  SER B N   1 
ATOM   1459 C CA  . SER B 1 94 ? 23.324  0.103   -25.451 1.00 82.30  ? 93  SER B CA  1 
ATOM   1460 C C   . SER B 1 94 ? 22.438  0.376   -24.227 1.00 90.54  ? 93  SER B C   1 
ATOM   1461 O O   . SER B 1 94 ? 21.608  1.314   -24.317 1.00 87.17  ? 93  SER B O   1 
ATOM   1462 C CB  . SER B 1 94 ? 24.252  1.263   -25.712 1.00 82.14  ? 93  SER B CB  1 
ATOM   1463 O OG  . SER B 1 94 ? 25.312  0.871   -26.571 1.00 81.98  ? 93  SER B OG  1 
ATOM   1464 O OXT . SER B 1 94 ? 22.596  -0.369  -23.238 1.00 99.89  ? 93  SER B OXT 1 
ATOM   1465 N N   . HIS C 1 4  ? 33.200  -23.876 27.010  1.00 84.52  ? 3   HIS C N   1 
ATOM   1466 C CA  . HIS C 1 4  ? 32.050  -22.954 27.225  1.00 92.50  ? 3   HIS C CA  1 
ATOM   1467 C C   . HIS C 1 4  ? 31.407  -23.279 28.577  1.00 92.74  ? 3   HIS C C   1 
ATOM   1468 O O   . HIS C 1 4  ? 32.048  -23.890 29.429  1.00 95.27  ? 3   HIS C O   1 
ATOM   1469 C CB  . HIS C 1 4  ? 31.124  -23.007 26.001  1.00 102.61 ? 3   HIS C CB  1 
ATOM   1470 C CG  . HIS C 1 4  ? 30.304  -21.775 25.792  1.00 113.27 ? 3   HIS C CG  1 
ATOM   1471 N ND1 . HIS C 1 4  ? 29.011  -21.638 26.254  1.00 118.65 ? 3   HIS C ND1 1 
ATOM   1472 C CD2 . HIS C 1 4  ? 30.596  -20.626 25.166  1.00 110.76 ? 3   HIS C CD2 1 
ATOM   1473 C CE1 . HIS C 1 4  ? 28.550  -20.441 25.920  1.00 118.32 ? 3   HIS C CE1 1 
ATOM   1474 N NE2 . HIS C 1 4  ? 29.498  -19.809 25.261  1.00 115.95 ? 3   HIS C NE2 1 
ATOM   1475 N N   . ALA C 1 5  ? 30.152  -22.848 28.772  1.00 85.24  ? 4   ALA C N   1 
ATOM   1476 C CA  . ALA C 1 5  ? 29.357  -23.185 29.944  1.00 76.63  ? 4   ALA C CA  1 
ATOM   1477 C C   . ALA C 1 5  ? 27.874  -23.072 29.619  1.00 78.62  ? 4   ALA C C   1 
ATOM   1478 O O   . ALA C 1 5  ? 27.450  -22.123 28.960  1.00 85.62  ? 4   ALA C O   1 
ATOM   1479 C CB  . ALA C 1 5  ? 29.679  -22.241 31.056  1.00 84.75  ? 4   ALA C CB  1 
ATOM   1480 N N   . PHE C 1 6  ? 27.090  -24.021 30.134  1.00 66.58  ? 5   PHE C N   1 
ATOM   1481 C CA  . PHE C 1 6  ? 25.695  -24.111 29.748  1.00 58.41  ? 5   PHE C CA  1 
ATOM   1482 C C   . PHE C 1 6  ? 24.838  -24.176 31.005  1.00 63.13  ? 5   PHE C C   1 
ATOM   1483 O O   . PHE C 1 6  ? 25.035  -25.058 31.833  1.00 79.22  ? 5   PHE C O   1 
ATOM   1484 C CB  . PHE C 1 6  ? 25.497  -25.334 28.836  1.00 53.62  ? 5   PHE C CB  1 
ATOM   1485 C CG  . PHE C 1 6  ? 26.193  -25.263 27.482  1.00 45.83  ? 5   PHE C CG  1 
ATOM   1486 C CD1 . PHE C 1 6  ? 27.278  -26.077 27.183  1.00 44.21  ? 5   PHE C CD1 1 
ATOM   1487 C CD2 . PHE C 1 6  ? 25.783  -24.352 26.512  1.00 49.03  ? 5   PHE C CD2 1 
ATOM   1488 C CE1 . PHE C 1 6  ? 27.911  -26.013 25.944  1.00 53.73  ? 5   PHE C CE1 1 
ATOM   1489 C CE2 . PHE C 1 6  ? 26.415  -24.294 25.272  1.00 50.43  ? 5   PHE C CE2 1 
ATOM   1490 C CZ  . PHE C 1 6  ? 27.473  -25.126 24.983  1.00 47.52  ? 5   PHE C CZ  1 
ATOM   1491 N N   . LYS C 1 7  ? 23.908  -23.227 31.145  1.00 62.05  ? 6   LYS C N   1 
ATOM   1492 C CA  . LYS C 1 7  ? 22.919  -23.254 32.217  1.00 63.96  ? 6   LYS C CA  1 
ATOM   1493 C C   . LYS C 1 7  ? 21.610  -23.714 31.586  1.00 51.30  ? 6   LYS C C   1 
ATOM   1494 O O   . LYS C 1 7  ? 21.499  -23.686 30.364  1.00 51.13  ? 6   LYS C O   1 
ATOM   1495 C CB  . LYS C 1 7  ? 22.790  -21.879 32.893  1.00 59.44  ? 6   LYS C CB  1 
ATOM   1496 N N   . PRO C 1 8  ? 20.587  -24.160 32.351  1.00 60.89  ? 7   PRO C N   1 
ATOM   1497 C CA  . PRO C 1 8  ? 19.284  -24.480 31.761  1.00 57.35  ? 7   PRO C CA  1 
ATOM   1498 C C   . PRO C 1 8  ? 18.691  -23.318 30.963  1.00 62.00  ? 7   PRO C C   1 
ATOM   1499 O O   . PRO C 1 8  ? 18.819  -22.163 31.364  1.00 62.66  ? 7   PRO C O   1 
ATOM   1500 C CB  . PRO C 1 8  ? 18.432  -24.854 32.981  1.00 63.52  ? 7   PRO C CB  1 
ATOM   1501 C CG  . PRO C 1 8  ? 19.443  -25.369 33.975  1.00 62.64  ? 7   PRO C CG  1 
ATOM   1502 C CD  . PRO C 1 8  ? 20.638  -24.437 33.798  1.00 61.42  ? 7   PRO C CD  1 
ATOM   1503 N N   . GLY C 1 9  ? 18.089  -23.635 29.806  1.00 59.22  ? 8   GLY C N   1 
ATOM   1504 C CA  . GLY C 1 9  ? 17.388  -22.661 28.978  1.00 52.36  ? 8   GLY C CA  1 
ATOM   1505 C C   . GLY C 1 9  ? 18.218  -22.186 27.784  1.00 52.41  ? 8   GLY C C   1 
ATOM   1506 O O   . GLY C 1 9  ? 17.654  -21.706 26.801  1.00 57.96  ? 8   GLY C O   1 
ATOM   1507 N N   . ASP C 1 10 ? 19.551  -22.326 27.887  1.00 46.70  ? 9   ASP C N   1 
ATOM   1508 C CA  . ASP C 1 10 ? 20.509  -21.996 26.851  1.00 41.92  ? 9   ASP C CA  1 
ATOM   1509 C C   . ASP C 1 10 ? 20.187  -22.772 25.576  1.00 43.93  ? 9   ASP C C   1 
ATOM   1510 O O   . ASP C 1 10 ? 20.021  -23.986 25.611  1.00 41.91  ? 9   ASP C O   1 
ATOM   1511 C CB  . ASP C 1 10 ? 21.937  -22.296 27.292  1.00 48.62  ? 9   ASP C CB  1 
ATOM   1512 C CG  . ASP C 1 10 ? 22.554  -21.379 28.347  1.00 57.93  ? 9   ASP C CG  1 
ATOM   1513 O OD1 . ASP C 1 10 ? 21.898  -20.398 28.733  1.00 57.78  ? 9   ASP C OD1 1 
ATOM   1514 O OD2 . ASP C 1 10 ? 23.702  -21.650 28.771  1.00 61.46  ? 9   ASP C OD2 1 
ATOM   1515 N N   . LEU C 1 11 ? 20.116  -22.053 24.452  1.00 46.63  ? 10  LEU C N   1 
ATOM   1516 C CA  . LEU C 1 11 ? 19.764  -22.634 23.166  1.00 43.42  ? 10  LEU C CA  1 
ATOM   1517 C C   . LEU C 1 11 ? 21.034  -23.057 22.449  1.00 36.29  ? 10  LEU C C   1 
ATOM   1518 O O   . LEU C 1 11 ? 22.012  -22.309 22.432  1.00 38.92  ? 10  LEU C O   1 
ATOM   1519 C CB  . LEU C 1 11 ? 18.987  -21.615 22.335  1.00 41.62  ? 10  LEU C CB  1 
ATOM   1520 C CG  . LEU C 1 11 ? 17.753  -21.027 23.012  1.00 42.47  ? 10  LEU C CG  1 
ATOM   1521 C CD1 . LEU C 1 11 ? 17.140  -20.030 22.055  1.00 45.77  ? 10  LEU C CD1 1 
ATOM   1522 C CD2 . LEU C 1 11 ? 16.762  -22.123 23.386  1.00 41.74  ? 10  LEU C CD2 1 
ATOM   1523 N N   . VAL C 1 12 ? 20.995  -24.252 21.820  1.00 36.73  ? 11  VAL C N   1 
ATOM   1524 C CA  . VAL C 1 12 ? 22.191  -24.819 21.227  1.00 33.88  ? 11  VAL C CA  1 
ATOM   1525 C C   . VAL C 1 12 ? 21.806  -25.575 19.940  1.00 35.96  ? 11  VAL C C   1 
ATOM   1526 O O   . VAL C 1 12 ? 20.615  -25.746 19.654  1.00 33.64  ? 11  VAL C O   1 
ATOM   1527 C CB  . VAL C 1 12 ? 22.856  -25.804 22.225  1.00 35.84  ? 11  VAL C CB  1 
ATOM   1528 C CG1 . VAL C 1 12 ? 23.262  -25.133 23.546  1.00 39.26  ? 11  VAL C CG1 1 
ATOM   1529 C CG2 . VAL C 1 12 ? 21.961  -27.005 22.517  1.00 35.07  ? 11  VAL C CG2 1 
ATOM   1530 N N   . PHE C 1 13 ? 22.838  -26.014 19.203  1.00 32.76  ? 12  PHE C N   1 
ATOM   1531 C CA  . PHE C 1 13 ? 22.765  -27.191 18.349  1.00 34.08  ? 12  PHE C CA  1 
ATOM   1532 C C   . PHE C 1 13 ? 23.497  -28.345 19.038  1.00 30.57  ? 12  PHE C C   1 
ATOM   1533 O O   . PHE C 1 13 ? 24.615  -28.188 19.542  1.00 36.12  ? 12  PHE C O   1 
ATOM   1534 C CB  . PHE C 1 13 ? 23.426  -26.948 16.988  1.00 36.15  ? 12  PHE C CB  1 
ATOM   1535 C CG  . PHE C 1 13 ? 22.675  -25.942 16.125  1.00 39.43  ? 12  PHE C CG  1 
ATOM   1536 C CD1 . PHE C 1 13 ? 21.669  -26.356 15.252  1.00 35.89  ? 12  PHE C CD1 1 
ATOM   1537 C CD2 . PHE C 1 13 ? 22.971  -24.584 16.195  1.00 39.24  ? 12  PHE C CD2 1 
ATOM   1538 C CE1 . PHE C 1 13 ? 20.967  -25.434 14.486  1.00 41.17  ? 12  PHE C CE1 1 
ATOM   1539 C CE2 . PHE C 1 13 ? 22.274  -23.668 15.416  1.00 41.19  ? 12  PHE C CE2 1 
ATOM   1540 C CZ  . PHE C 1 13 ? 21.284  -24.100 14.559  1.00 42.60  ? 12  PHE C CZ  1 
ATOM   1541 N N   . ALA C 1 14 ? 22.857  -29.523 19.032  1.00 31.96  ? 13  ALA C N   1 
ATOM   1542 C CA  . ALA C 1 14 ? 23.319  -30.692 19.763  1.00 29.42  ? 13  ALA C CA  1 
ATOM   1543 C C   . ALA C 1 14 ? 23.601  -31.807 18.759  1.00 34.55  ? 13  ALA C C   1 
ATOM   1544 O O   . ALA C 1 14 ? 22.719  -32.117 17.952  1.00 28.40  ? 13  ALA C O   1 
ATOM   1545 C CB  . ALA C 1 14 ? 22.232  -31.124 20.715  1.00 27.80  ? 13  ALA C CB  1 
ATOM   1546 N N   . LYS C 1 15 ? 24.820  -32.381 18.806  1.00 30.47  ? 14  LYS C N   1 
ATOM   1547 C CA  . LYS C 1 15 ? 25.198  -33.400 17.830  1.00 33.74  ? 14  LYS C CA  1 
ATOM   1548 C C   . LYS C 1 15 ? 25.157  -34.774 18.489  1.00 32.62  ? 14  LYS C C   1 
ATOM   1549 O O   . LYS C 1 15 ? 25.869  -35.027 19.453  1.00 33.96  ? 14  LYS C O   1 
ATOM   1550 C CB  . LYS C 1 15 ? 26.598  -33.170 17.244  1.00 36.61  ? 14  LYS C CB  1 
ATOM   1551 C CG  . LYS C 1 15 ? 26.990  -34.236 16.184  1.00 35.03  ? 14  LYS C CG  1 
ATOM   1552 C CD  . LYS C 1 15 ? 26.271  -33.987 14.858  1.00 33.51  ? 14  LYS C CD  1 
ATOM   1553 C CE  . LYS C 1 15 ? 26.702  -34.868 13.683  1.00 31.58  ? 14  LYS C CE  1 
ATOM   1554 N NZ  . LYS C 1 15 ? 26.620  -36.282 14.055  1.00 32.61  ? 14  LYS C NZ  1 
ATOM   1555 N N   . MET C 1 16 ? 24.332  -35.672 17.951  1.00 28.35  ? 15  MET C N   1 
ATOM   1556 C CA  . MET C 1 16 ? 24.385  -37.091 18.307  1.00 30.29  ? 15  MET C CA  1 
ATOM   1557 C C   . MET C 1 16 ? 24.876  -37.904 17.109  1.00 35.28  ? 15  MET C C   1 
ATOM   1558 O O   . MET C 1 16 ? 24.697  -37.502 15.957  1.00 30.56  ? 15  MET C O   1 
ATOM   1559 C CB  . MET C 1 16 ? 22.991  -37.609 18.681  1.00 32.02  ? 15  MET C CB  1 
ATOM   1560 C CG  . MET C 1 16 ? 22.425  -36.971 19.945  1.00 38.23  ? 15  MET C CG  1 
ATOM   1561 S SD  . MET C 1 16 ? 20.787  -37.629 20.310  1.00 41.88  ? 15  MET C SD  1 
ATOM   1562 C CE  . MET C 1 16 ? 19.911  -37.074 18.840  1.00 37.60  ? 15  MET C CE  1 
ATOM   1563 N N   . LYS C 1 17 ? 25.469  -39.077 17.386  1.00 32.45  ? 16  LYS C N   1 
ATOM   1564 C CA  . LYS C 1 17 ? 25.865  -39.967 16.302  1.00 36.73  ? 16  LYS C CA  1 
ATOM   1565 C C   . LYS C 1 17 ? 24.613  -40.374 15.512  1.00 30.08  ? 16  LYS C C   1 
ATOM   1566 O O   . LYS C 1 17 ? 23.611  -40.811 16.072  1.00 36.97  ? 16  LYS C O   1 
ATOM   1567 C CB  . LYS C 1 17 ? 26.651  -41.165 16.860  1.00 36.23  ? 16  LYS C CB  1 
ATOM   1568 C CG  . LYS C 1 17 ? 27.246  -42.101 15.805  1.00 39.26  ? 16  LYS C CG  1 
ATOM   1569 C CD  . LYS C 1 17 ? 28.382  -41.341 15.126  1.00 40.72  ? 16  LYS C CD  1 
ATOM   1570 C CE  . LYS C 1 17 ? 29.171  -42.198 14.177  1.00 55.59  ? 16  LYS C CE  1 
ATOM   1571 N NZ  . LYS C 1 17 ? 30.431  -41.551 13.797  1.00 51.22  ? 16  LYS C NZ  1 
ATOM   1572 N N   . GLY C 1 18 ? 24.690  -40.222 14.193  1.00 35.48  ? 17  GLY C N   1 
ATOM   1573 C CA  . GLY C 1 18 ? 23.591  -40.677 13.353  1.00 33.25  ? 17  GLY C CA  1 
ATOM   1574 C C   . GLY C 1 18 ? 22.683  -39.538 12.891  1.00 33.27  ? 17  GLY C C   1 
ATOM   1575 O O   . GLY C 1 18 ? 21.684  -39.795 12.232  1.00 36.73  ? 17  GLY C O   1 
ATOM   1576 N N   . TYR C 1 19 ? 22.970  -38.297 13.321  1.00 31.76  ? 18  TYR C N   1 
ATOM   1577 C CA  . TYR C 1 19 ? 22.038  -37.180 13.139  1.00 33.37  ? 18  TYR C CA  1 
ATOM   1578 C C   . TYR C 1 19 ? 22.824  -35.902 12.897  1.00 31.50  ? 18  TYR C C   1 
ATOM   1579 O O   . TYR C 1 19 ? 23.928  -35.725 13.440  1.00 31.23  ? 18  TYR C O   1 
ATOM   1580 C CB  . TYR C 1 19 ? 21.197  -36.916 14.396  1.00 29.81  ? 18  TYR C CB  1 
ATOM   1581 C CG  . TYR C 1 19 ? 20.320  -38.092 14.781  1.00 34.76  ? 18  TYR C CG  1 
ATOM   1582 C CD1 . TYR C 1 19 ? 20.813  -39.154 15.548  1.00 32.56  ? 18  TYR C CD1 1 
ATOM   1583 C CD2 . TYR C 1 19 ? 19.017  -38.155 14.327  1.00 32.20  ? 18  TYR C CD2 1 
ATOM   1584 C CE1 . TYR C 1 19 ? 20.003  -40.226 15.869  1.00 34.30  ? 18  TYR C CE1 1 
ATOM   1585 C CE2 . TYR C 1 19 ? 18.203  -39.224 14.649  1.00 39.01  ? 18  TYR C CE2 1 
ATOM   1586 C CZ  . TYR C 1 19 ? 18.692  -40.252 15.428  1.00 39.02  ? 18  TYR C CZ  1 
ATOM   1587 O OH  . TYR C 1 19 ? 17.836  -41.290 15.689  1.00 45.36  ? 18  TYR C OH  1 
ATOM   1588 N N   . PRO C 1 20 ? 22.270  -34.972 12.083  1.00 31.35  ? 19  PRO C N   1 
ATOM   1589 C CA  . PRO C 1 20 ? 22.923  -33.687 11.840  1.00 29.35  ? 19  PRO C CA  1 
ATOM   1590 C C   . PRO C 1 20 ? 22.863  -32.878 13.141  1.00 30.42  ? 19  PRO C C   1 
ATOM   1591 O O   . PRO C 1 20 ? 22.072  -33.175 14.036  1.00 27.20  ? 19  PRO C O   1 
ATOM   1592 C CB  . PRO C 1 20 ? 22.041  -33.058 10.713  1.00 31.56  ? 19  PRO C CB  1 
ATOM   1593 C CG  . PRO C 1 20 ? 20.658  -33.637 10.952  1.00 30.61  ? 19  PRO C CG  1 
ATOM   1594 C CD  . PRO C 1 20 ? 20.922  -35.066 11.472  1.00 28.44  ? 19  PRO C CD  1 
ATOM   1595 N N   . HIS C 1 21 ? 23.743  -31.882 13.256  1.00 29.99  ? 20  HIS C N   1 
ATOM   1596 C CA  . HIS C 1 21 ? 23.650  -30.940 14.369  1.00 29.61  ? 20  HIS C CA  1 
ATOM   1597 C C   . HIS C 1 21 ? 22.221  -30.411 14.472  1.00 31.71  ? 20  HIS C C   1 
ATOM   1598 O O   . HIS C 1 21 ? 21.687  -29.885 13.490  1.00 33.73  ? 20  HIS C O   1 
ATOM   1599 C CB  . HIS C 1 21 ? 24.617  -29.779 14.146  1.00 35.35  ? 20  HIS C CB  1 
ATOM   1600 C CG  . HIS C 1 21 ? 26.040  -30.227 14.199  1.00 37.55  ? 20  HIS C CG  1 
ATOM   1601 N ND1 . HIS C 1 21 ? 26.696  -30.896 13.188  1.00 40.03  ? 20  HIS C ND1 1 
ATOM   1602 C CD2 . HIS C 1 21 ? 26.905  -30.127 15.211  1.00 39.95  ? 20  HIS C CD2 1 
ATOM   1603 C CE1 . HIS C 1 21 ? 27.938  -31.165 13.580  1.00 41.38  ? 20  HIS C CE1 1 
ATOM   1604 N NE2 . HIS C 1 21 ? 28.085  -30.690 14.811  1.00 38.85  ? 20  HIS C NE2 1 
ATOM   1605 N N   . TRP C 1 22 ? 21.615  -30.526 15.668  1.00 29.33  ? 21  TRP C N   1 
ATOM   1606 C CA  . TRP C 1 22 ? 20.165  -30.409 15.785  1.00 26.62  ? 21  TRP C CA  1 
ATOM   1607 C C   . TRP C 1 22 ? 19.790  -29.260 16.719  1.00 28.42  ? 21  TRP C C   1 
ATOM   1608 O O   . TRP C 1 22 ? 20.348  -29.161 17.811  1.00 29.00  ? 21  TRP C O   1 
ATOM   1609 C CB  . TRP C 1 22 ? 19.594  -31.724 16.334  1.00 28.71  ? 21  TRP C CB  1 
ATOM   1610 C CG  . TRP C 1 22 ? 18.131  -31.897 16.024  1.00 28.72  ? 21  TRP C CG  1 
ATOM   1611 C CD1 . TRP C 1 22 ? 17.041  -31.295 16.593  1.00 30.87  ? 21  TRP C CD1 1 
ATOM   1612 C CD2 . TRP C 1 22 ? 17.617  -32.793 15.010  1.00 28.20  ? 21  TRP C CD2 1 
ATOM   1613 N NE1 . TRP C 1 22 ? 15.888  -31.737 15.987  1.00 29.19  ? 21  TRP C NE1 1 
ATOM   1614 C CE2 . TRP C 1 22 ? 16.203  -32.657 15.025  1.00 28.85  ? 21  TRP C CE2 1 
ATOM   1615 C CE3 . TRP C 1 22 ? 18.218  -33.681 14.104  1.00 27.16  ? 21  TRP C CE3 1 
ATOM   1616 C CZ2 . TRP C 1 22 ? 15.383  -33.394 14.172  1.00 29.79  ? 21  TRP C CZ2 1 
ATOM   1617 C CZ3 . TRP C 1 22 ? 17.402  -34.399 13.249  1.00 33.30  ? 21  TRP C CZ3 1 
ATOM   1618 C CH2 . TRP C 1 22 ? 16.006  -34.272 13.305  1.00 31.22  ? 21  TRP C CH2 1 
ATOM   1619 N N   . PRO C 1 23 ? 18.780  -28.413 16.389  1.00 31.74  ? 22  PRO C N   1 
ATOM   1620 C CA  . PRO C 1 23 ? 18.392  -27.305 17.265  1.00 29.68  ? 22  PRO C CA  1 
ATOM   1621 C C   . PRO C 1 23 ? 17.817  -27.846 18.569  1.00 26.43  ? 22  PRO C C   1 
ATOM   1622 O O   . PRO C 1 23 ? 16.989  -28.750 18.574  1.00 30.60  ? 22  PRO C O   1 
ATOM   1623 C CB  . PRO C 1 23 ? 17.342  -26.549 16.416  1.00 33.74  ? 22  PRO C CB  1 
ATOM   1624 C CG  . PRO C 1 23 ? 16.724  -27.626 15.514  1.00 29.03  ? 22  PRO C CG  1 
ATOM   1625 C CD  . PRO C 1 23 ? 17.958  -28.446 15.161  1.00 30.77  ? 22  PRO C CD  1 
ATOM   1626 N N   . ALA C 1 24 ? 18.271  -27.272 19.690  1.00 31.74  ? 23  ALA C N   1 
ATOM   1627 C CA  . ALA C 1 24 ? 18.001  -27.867 20.996  1.00 33.15  ? 23  ALA C CA  1 
ATOM   1628 C C   . ALA C 1 24 ? 18.156  -26.805 22.088  1.00 36.40  ? 23  ALA C C   1 
ATOM   1629 O O   . ALA C 1 24 ? 18.662  -25.717 21.821  1.00 34.64  ? 23  ALA C O   1 
ATOM   1630 C CB  . ALA C 1 24 ? 18.953  -29.050 21.218  1.00 31.14  ? 23  ALA C CB  1 
ATOM   1631 N N   . ARG C 1 25 ? 17.752  -27.144 23.319  1.00 36.29  ? 24  ARG C N   1 
ATOM   1632 C CA  . ARG C 1 25 ? 18.105  -26.337 24.480  1.00 33.00  ? 24  ARG C CA  1 
ATOM   1633 C C   . ARG C 1 25 ? 18.598  -27.231 25.632  1.00 36.87  ? 24  ARG C C   1 
ATOM   1634 O O   . ARG C 1 25 ? 18.316  -28.432 25.640  1.00 35.92  ? 24  ARG C O   1 
ATOM   1635 C CB  . ARG C 1 25 ? 16.878  -25.560 24.959  1.00 34.38  ? 24  ARG C CB  1 
ATOM   1636 C CG  . ARG C 1 25 ? 15.630  -26.365 25.290  1.00 40.88  ? 24  ARG C CG  1 
ATOM   1637 C CD  . ARG C 1 25 ? 14.596  -25.491 26.017  1.00 42.01  ? 24  ARG C CD  1 
ATOM   1638 N NE  . ARG C 1 25 ? 13.399  -26.283 26.336  1.00 44.81  ? 24  ARG C NE  1 
ATOM   1639 C CZ  . ARG C 1 25 ? 12.131  -26.010 26.064  1.00 50.46  ? 24  ARG C CZ  1 
ATOM   1640 N NH1 . ARG C 1 25 ? 11.814  -24.917 25.387  1.00 46.91  ? 24  ARG C NH1 1 
ATOM   1641 N NH2 . ARG C 1 25 ? 11.181  -26.840 26.484  1.00 48.74  ? 24  ARG C NH2 1 
ATOM   1642 N N   . ILE C 1 26 ? 19.325  -26.622 26.584  1.00 38.38  ? 25  ILE C N   1 
ATOM   1643 C CA  . ILE C 1 26 ? 19.668  -27.240 27.867  1.00 40.73  ? 25  ILE C CA  1 
ATOM   1644 C C   . ILE C 1 26 ? 18.439  -27.215 28.768  1.00 48.17  ? 25  ILE C C   1 
ATOM   1645 O O   . ILE C 1 26 ? 17.855  -26.147 28.978  1.00 43.64  ? 25  ILE C O   1 
ATOM   1646 C CB  . ILE C 1 26 ? 20.842  -26.529 28.568  1.00 43.47  ? 25  ILE C CB  1 
ATOM   1647 C CG1 . ILE C 1 26 ? 21.989  -26.183 27.640  1.00 43.79  ? 25  ILE C CG1 1 
ATOM   1648 C CG2 . ILE C 1 26 ? 21.304  -27.308 29.806  1.00 40.18  ? 25  ILE C CG2 1 
ATOM   1649 C CD1 . ILE C 1 26 ? 22.755  -27.359 27.066  1.00 46.83  ? 25  ILE C CD1 1 
ATOM   1650 N N   . ASP C 1 27 ? 18.066  -28.400 29.274  1.00 48.25  ? 26  ASP C N   1 
ATOM   1651 C CA  . ASP C 1 27 ? 17.019  -28.605 30.269  1.00 55.86  ? 26  ASP C CA  1 
ATOM   1652 C C   . ASP C 1 27 ? 17.604  -28.513 31.683  1.00 59.85  ? 26  ASP C C   1 
ATOM   1653 O O   . ASP C 1 27 ? 18.813  -28.656 31.872  1.00 59.97  ? 26  ASP C O   1 
ATOM   1654 C CB  . ASP C 1 27 ? 16.309  -29.938 30.056  1.00 55.87  ? 26  ASP C CB  1 
ATOM   1655 C CG  . ASP C 1 27 ? 14.936  -29.892 29.396  1.00 61.14  ? 26  ASP C CG  1 
ATOM   1656 O OD1 . ASP C 1 27 ? 14.568  -28.811 28.873  1.00 56.48  ? 26  ASP C OD1 1 
ATOM   1657 O OD2 . ASP C 1 27 ? 14.227  -30.932 29.451  1.00 57.27  ? 26  ASP C OD2 1 
ATOM   1658 N N   . ASP C 1 28 ? 16.730  -28.272 32.675  1.00 69.07  ? 27  ASP C N   1 
ATOM   1659 C CA  . ASP C 1 28 ? 17.099  -28.292 34.085  1.00 71.75  ? 27  ASP C CA  1 
ATOM   1660 C C   . ASP C 1 28 ? 16.964  -29.725 34.607  1.00 69.34  ? 27  ASP C C   1 
ATOM   1661 O O   . ASP C 1 28 ? 16.329  -30.507 33.873  1.00 58.39  ? 27  ASP C O   1 
ATOM   1662 C CB  . ASP C 1 28 ? 16.264  -27.325 34.909  1.00 73.58  ? 27  ASP C CB  1 
ATOM   1663 N N   . ALA C 1 33 ? 14.942  -36.688 40.488  1.00 55.29  ? 32  ALA C N   1 
ATOM   1664 C CA  . ALA C 1 33 ? 15.104  -37.390 39.193  1.00 58.67  ? 32  ALA C CA  1 
ATOM   1665 C C   . ALA C 1 33 ? 16.447  -38.118 39.162  1.00 61.65  ? 32  ALA C C   1 
ATOM   1666 O O   . ALA C 1 33 ? 17.300  -37.890 40.024  1.00 62.87  ? 32  ALA C O   1 
ATOM   1667 C CB  . ALA C 1 33 ? 14.967  -36.415 38.041  1.00 54.24  ? 32  ALA C CB  1 
ATOM   1668 N N   . VAL C 1 34 ? 16.615  -39.009 38.173  1.00 60.80  ? 33  VAL C N   1 
ATOM   1669 C CA  . VAL C 1 34 ? 17.882  -39.694 37.950  1.00 67.88  ? 33  VAL C CA  1 
ATOM   1670 C C   . VAL C 1 34 ? 18.862  -38.689 37.344  1.00 68.30  ? 33  VAL C C   1 
ATOM   1671 O O   . VAL C 1 34 ? 18.535  -37.993 36.377  1.00 57.74  ? 33  VAL C O   1 
ATOM   1672 C CB  . VAL C 1 34 ? 17.797  -41.004 37.139  1.00 77.10  ? 33  VAL C CB  1 
ATOM   1673 C CG1 . VAL C 1 34 ? 19.051  -41.269 36.306  1.00 80.52  ? 33  VAL C CG1 1 
ATOM   1674 C CG2 . VAL C 1 34 ? 17.473  -42.192 38.038  1.00 81.87  ? 33  VAL C CG2 1 
ATOM   1675 N N   . LYS C 1 35 ? 20.048  -38.602 37.964  1.00 61.27  ? 34  LYS C N   1 
ATOM   1676 C CA  . LYS C 1 35 ? 21.037  -37.603 37.600  1.00 62.52  ? 34  LYS C CA  1 
ATOM   1677 C C   . LYS C 1 35 ? 21.617  -37.962 36.232  1.00 58.63  ? 34  LYS C C   1 
ATOM   1678 O O   . LYS C 1 35 ? 21.591  -39.125 35.813  1.00 50.43  ? 34  LYS C O   1 
ATOM   1679 C CB  . LYS C 1 35 ? 22.086  -37.458 38.709  1.00 63.40  ? 34  LYS C CB  1 
ATOM   1680 N N   . PRO C 1 36 ? 22.133  -36.964 35.479  1.00 58.77  ? 35  PRO C N   1 
ATOM   1681 C CA  . PRO C 1 36 ? 22.839  -37.254 34.233  1.00 58.02  ? 35  PRO C CA  1 
ATOM   1682 C C   . PRO C 1 36 ? 23.951  -38.272 34.488  1.00 60.41  ? 35  PRO C C   1 
ATOM   1683 O O   . PRO C 1 36 ? 24.396  -38.487 35.625  1.00 51.54  ? 35  PRO C O   1 
ATOM   1684 C CB  . PRO C 1 36 ? 23.395  -35.871 33.818  1.00 63.38  ? 35  PRO C CB  1 
ATOM   1685 C CG  . PRO C 1 36 ? 22.469  -34.870 34.483  1.00 59.38  ? 35  PRO C CG  1 
ATOM   1686 C CD  . PRO C 1 36 ? 22.057  -35.525 35.796  1.00 59.75  ? 35  PRO C CD  1 
ATOM   1687 N N   . PRO C 1 37 ? 24.456  -38.949 33.441  1.00 51.65  ? 36  PRO C N   1 
ATOM   1688 C CA  . PRO C 1 37 ? 25.760  -39.592 33.566  1.00 48.34  ? 36  PRO C CA  1 
ATOM   1689 C C   . PRO C 1 37 ? 26.705  -38.445 33.922  1.00 46.91  ? 36  PRO C C   1 
ATOM   1690 O O   . PRO C 1 37 ? 26.373  -37.269 33.741  1.00 43.07  ? 36  PRO C O   1 
ATOM   1691 C CB  . PRO C 1 37 ? 25.969  -40.179 32.159  1.00 46.54  ? 36  PRO C CB  1 
ATOM   1692 C CG  . PRO C 1 37 ? 24.546  -40.412 31.693  1.00 45.07  ? 36  PRO C CG  1 
ATOM   1693 C CD  . PRO C 1 37 ? 23.825  -39.150 32.128  1.00 49.44  ? 36  PRO C CD  1 
ATOM   1694 N N   . PRO C 1 38 ? 27.883  -38.743 34.510  1.00 45.35  ? 37  PRO C N   1 
ATOM   1695 C CA  . PRO C 1 38 ? 28.854  -37.706 34.850  1.00 43.57  ? 37  PRO C CA  1 
ATOM   1696 C C   . PRO C 1 38 ? 29.171  -36.826 33.650  1.00 40.48  ? 37  PRO C C   1 
ATOM   1697 O O   . PRO C 1 38 ? 29.403  -37.336 32.554  1.00 41.75  ? 37  PRO C O   1 
ATOM   1698 C CB  . PRO C 1 38 ? 30.067  -38.570 35.255  1.00 47.07  ? 37  PRO C CB  1 
ATOM   1699 C CG  . PRO C 1 38 ? 29.411  -39.778 35.876  1.00 42.46  ? 37  PRO C CG  1 
ATOM   1700 C CD  . PRO C 1 38 ? 28.340  -40.102 34.857  1.00 47.46  ? 37  PRO C CD  1 
ATOM   1701 N N   . ASN C 1 39 ? 29.130  -35.508 33.889  1.00 37.45  ? 38  ASN C N   1 
ATOM   1702 C CA  . ASN C 1 39 ? 29.573  -34.460 32.979  1.00 37.10  ? 38  ASN C CA  1 
ATOM   1703 C C   . ASN C 1 39 ? 28.648  -34.340 31.768  1.00 42.13  ? 38  ASN C C   1 
ATOM   1704 O O   . ASN C 1 39 ? 29.055  -33.778 30.742  1.00 44.75  ? 38  ASN C O   1 
ATOM   1705 C CB  . ASN C 1 39 ? 31.061  -34.549 32.660  1.00 38.83  ? 38  ASN C CB  1 
ATOM   1706 C CG  . ASN C 1 39 ? 31.620  -33.334 31.952  1.00 48.16  ? 38  ASN C CG  1 
ATOM   1707 O OD1 . ASN C 1 39 ? 31.257  -32.193 32.256  1.00 57.39  ? 38  ASN C OD1 1 
ATOM   1708 N ND2 . ASN C 1 39 ? 32.505  -33.547 30.990  1.00 53.14  ? 38  ASN C ND2 1 
ATOM   1709 N N   . LYS C 1 40 ? 27.403  -34.830 31.891  1.00 36.55  ? 39  LYS C N   1 
ATOM   1710 C CA  . LYS C 1 40 ? 26.485  -34.679 30.770  1.00 36.03  ? 39  LYS C CA  1 
ATOM   1711 C C   . LYS C 1 40 ? 25.348  -33.724 31.120  1.00 36.74  ? 39  LYS C C   1 
ATOM   1712 O O   . LYS C 1 40 ? 24.904  -33.687 32.252  1.00 37.62  ? 39  LYS C O   1 
ATOM   1713 C CB  . LYS C 1 40 ? 25.780  -36.002 30.457  1.00 35.27  ? 39  LYS C CB  1 
ATOM   1714 C CG  . LYS C 1 40 ? 26.691  -37.166 30.172  1.00 39.02  ? 39  LYS C CG  1 
ATOM   1715 C CD  . LYS C 1 40 ? 27.535  -37.021 28.929  1.00 45.74  ? 39  LYS C CD  1 
ATOM   1716 C CE  . LYS C 1 40 ? 28.093  -38.357 28.553  1.00 53.10  ? 39  LYS C CE  1 
ATOM   1717 N NZ  . LYS C 1 40 ? 29.136  -38.181 27.542  1.00 56.45  ? 39  LYS C NZ  1 
ATOM   1718 N N   . TYR C 1 41 ? 24.842  -33.013 30.106  1.00 34.51  ? 40  TYR C N   1 
ATOM   1719 C CA  . TYR C 1 41 ? 23.697  -32.126 30.243  1.00 35.04  ? 40  TYR C CA  1 
ATOM   1720 C C   . TYR C 1 41 ? 22.434  -32.793 29.716  1.00 33.92  ? 40  TYR C C   1 
ATOM   1721 O O   . TYR C 1 41 ? 22.490  -33.574 28.756  1.00 36.10  ? 40  TYR C O   1 
ATOM   1722 C CB  . TYR C 1 41 ? 23.848  -30.904 29.335  1.00 32.74  ? 40  TYR C CB  1 
ATOM   1723 C CG  . TYR C 1 41 ? 25.015  -30.027 29.744  1.00 35.35  ? 40  TYR C CG  1 
ATOM   1724 C CD1 . TYR C 1 41 ? 26.300  -30.272 29.255  1.00 34.82  ? 40  TYR C CD1 1 
ATOM   1725 C CD2 . TYR C 1 41 ? 24.830  -28.956 30.622  1.00 37.54  ? 40  TYR C CD2 1 
ATOM   1726 C CE1 . TYR C 1 41 ? 27.382  -29.500 29.637  1.00 40.16  ? 40  TYR C CE1 1 
ATOM   1727 C CE2 . TYR C 1 41 ? 25.905  -28.153 30.975  1.00 37.44  ? 40  TYR C CE2 1 
ATOM   1728 C CZ  . TYR C 1 41 ? 27.176  -28.437 30.502  1.00 39.97  ? 40  TYR C CZ  1 
ATOM   1729 O OH  . TYR C 1 41 ? 28.252  -27.679 30.841  1.00 46.54  ? 40  TYR C OH  1 
ATOM   1730 N N   . PRO C 1 42 ? 21.265  -32.437 30.306  1.00 36.59  ? 41  PRO C N   1 
ATOM   1731 C CA  . PRO C 1 42 ? 19.959  -32.880 29.805  1.00 35.25  ? 41  PRO C CA  1 
ATOM   1732 C C   . PRO C 1 42 ? 19.667  -31.964 28.622  1.00 36.13  ? 41  PRO C C   1 
ATOM   1733 O O   . PRO C 1 42 ? 19.713  -30.733 28.769  1.00 35.17  ? 41  PRO C O   1 
ATOM   1734 C CB  . PRO C 1 42 ? 18.972  -32.669 30.974  1.00 33.57  ? 41  PRO C CB  1 
ATOM   1735 C CG  . PRO C 1 42 ? 19.730  -31.788 31.943  1.00 35.72  ? 41  PRO C CG  1 
ATOM   1736 C CD  . PRO C 1 42 ? 21.156  -31.540 31.468  1.00 37.62  ? 41  PRO C CD  1 
ATOM   1737 N N   . ILE C 1 43 ? 19.383  -32.599 27.469  1.00 33.87  ? 42  ILE C N   1 
ATOM   1738 C CA  . ILE C 1 43 ? 19.112  -31.860 26.240  1.00 33.67  ? 42  ILE C CA  1 
ATOM   1739 C C   . ILE C 1 43 ? 17.660  -32.113 25.837  1.00 31.29  ? 42  ILE C C   1 
ATOM   1740 O O   . ILE C 1 43 ? 17.141  -33.234 25.914  1.00 35.72  ? 42  ILE C O   1 
ATOM   1741 C CB  . ILE C 1 43 ? 20.113  -32.237 25.122  1.00 31.16  ? 42  ILE C CB  1 
ATOM   1742 C CG1 . ILE C 1 43 ? 21.585  -32.025 25.549  1.00 30.30  ? 42  ILE C CG1 1 
ATOM   1743 C CG2 . ILE C 1 43 ? 19.795  -31.493 23.817  1.00 33.52  ? 42  ILE C CG2 1 
ATOM   1744 C CD1 . ILE C 1 43 ? 21.957  -30.574 25.847  1.00 32.37  ? 42  ILE C CD1 1 
ATOM   1745 N N   . PHE C 1 44 ? 17.003  -31.047 25.368  1.00 33.63  ? 43  PHE C N   1 
ATOM   1746 C CA  . PHE C 1 44 ? 15.702  -31.179 24.739  1.00 30.17  ? 43  PHE C CA  1 
ATOM   1747 C C   . PHE C 1 44 ? 15.868  -30.732 23.287  1.00 31.38  ? 43  PHE C C   1 
ATOM   1748 O O   . PHE C 1 44 ? 16.471  -29.686 23.046  1.00 30.49  ? 43  PHE C O   1 
ATOM   1749 C CB  . PHE C 1 44 ? 14.777  -30.166 25.427  1.00 35.77  ? 43  PHE C CB  1 
ATOM   1750 C CG  . PHE C 1 44 ? 13.375  -30.111 24.828  1.00 33.99  ? 43  PHE C CG  1 
ATOM   1751 C CD1 . PHE C 1 44 ? 12.446  -31.115 25.104  1.00 39.73  ? 43  PHE C CD1 1 
ATOM   1752 C CD2 . PHE C 1 44 ? 13.011  -29.086 23.946  1.00 36.74  ? 43  PHE C CD2 1 
ATOM   1753 C CE1 . PHE C 1 44 ? 11.173  -31.093 24.538  1.00 41.91  ? 43  PHE C CE1 1 
ATOM   1754 C CE2 . PHE C 1 44 ? 11.732  -29.064 23.381  1.00 37.16  ? 43  PHE C CE2 1 
ATOM   1755 C CZ  . PHE C 1 44 ? 10.824  -30.059 23.686  1.00 43.41  ? 43  PHE C CZ  1 
ATOM   1756 N N   . PHE C 1 45 ? 15.404  -31.577 22.363  1.00 31.63  ? 44  PHE C N   1 
ATOM   1757 C CA  . PHE C 1 45 ? 15.517  -31.389 20.925  1.00 33.67  ? 44  PHE C CA  1 
ATOM   1758 C C   . PHE C 1 45 ? 14.223  -30.765 20.416  1.00 32.91  ? 44  PHE C C   1 
ATOM   1759 O O   . PHE C 1 45 ? 13.148  -31.346 20.536  1.00 35.85  ? 44  PHE C O   1 
ATOM   1760 C CB  . PHE C 1 45 ? 15.813  -32.694 20.178  1.00 29.25  ? 44  PHE C CB  1 
ATOM   1761 C CG  . PHE C 1 45 ? 17.192  -33.263 20.481  1.00 32.19  ? 44  PHE C CG  1 
ATOM   1762 C CD1 . PHE C 1 45 ? 18.302  -32.860 19.745  1.00 29.44  ? 44  PHE C CD1 1 
ATOM   1763 C CD2 . PHE C 1 45 ? 17.372  -34.167 21.530  1.00 30.53  ? 44  PHE C CD2 1 
ATOM   1764 C CE1 . PHE C 1 45 ? 19.567  -33.383 20.034  1.00 35.77  ? 44  PHE C CE1 1 
ATOM   1765 C CE2 . PHE C 1 45 ? 18.630  -34.692 21.811  1.00 34.71  ? 44  PHE C CE2 1 
ATOM   1766 C CZ  . PHE C 1 45 ? 19.718  -34.300 21.060  1.00 33.20  ? 44  PHE C CZ  1 
ATOM   1767 N N   . PHE C 1 46 ? 14.349  -29.591 19.788  1.00 33.56  ? 45  PHE C N   1 
ATOM   1768 C CA  . PHE C 1 46 ? 13.183  -28.992 19.147  1.00 31.29  ? 45  PHE C CA  1 
ATOM   1769 C C   . PHE C 1 46 ? 12.719  -29.831 17.961  1.00 33.59  ? 45  PHE C C   1 
ATOM   1770 O O   . PHE C 1 46 ? 13.501  -30.581 17.360  1.00 32.29  ? 45  PHE C O   1 
ATOM   1771 C CB  . PHE C 1 46 ? 13.535  -27.565 18.728  1.00 31.73  ? 45  PHE C CB  1 
ATOM   1772 C CG  . PHE C 1 46 ? 13.831  -26.587 19.858  1.00 33.38  ? 45  PHE C CG  1 
ATOM   1773 C CD1 . PHE C 1 46 ? 12.808  -26.122 20.690  1.00 33.80  ? 45  PHE C CD1 1 
ATOM   1774 C CD2 . PHE C 1 46 ? 15.115  -26.056 20.003  1.00 31.85  ? 45  PHE C CD2 1 
ATOM   1775 C CE1 . PHE C 1 46 ? 13.096  -25.193 21.682  1.00 35.99  ? 45  PHE C CE1 1 
ATOM   1776 C CE2 . PHE C 1 46 ? 15.394  -25.123 20.987  1.00 35.01  ? 45  PHE C CE2 1 
ATOM   1777 C CZ  . PHE C 1 46 ? 14.386  -24.695 21.820  1.00 35.39  ? 45  PHE C CZ  1 
ATOM   1778 N N   . GLY C 1 47 ? 11.428  -29.683 17.620  1.00 29.73  ? 46  GLY C N   1 
ATOM   1779 C CA  . GLY C 1 47 ? 10.895  -30.375 16.472  1.00 36.06  ? 46  GLY C CA  1 
ATOM   1780 C C   . GLY C 1 47 ? 10.466  -31.780 16.868  1.00 39.20  ? 46  GLY C C   1 
ATOM   1781 O O   . GLY C 1 47 ? 9.281   -32.103 16.816  1.00 39.58  ? 46  GLY C O   1 
ATOM   1782 N N   . THR C 1 48 ? 11.440  -32.615 17.246  1.00 32.90  ? 47  THR C N   1 
ATOM   1783 C CA  . THR C 1 48 ? 11.071  -33.965 17.662  1.00 37.89  ? 47  THR C CA  1 
ATOM   1784 C C   . THR C 1 48 ? 10.542  -33.930 19.092  1.00 35.37  ? 47  THR C C   1 
ATOM   1785 O O   . THR C 1 48 ? 9.740   -34.789 19.468  1.00 39.34  ? 47  THR C O   1 
ATOM   1786 C CB  . THR C 1 48 ? 12.246  -34.931 17.553  1.00 36.69  ? 47  THR C CB  1 
ATOM   1787 O OG1 . THR C 1 48 ? 13.158  -34.418 18.535  1.00 36.21  ? 47  THR C OG1 1 
ATOM   1788 C CG2 . THR C 1 48 ? 12.785  -35.043 16.135  1.00 33.18  ? 47  THR C CG2 1 
ATOM   1789 N N   . HIS C 1 49 ? 11.019  -32.963 19.886  1.00 35.28  ? 48  HIS C N   1 
ATOM   1790 C CA  . HIS C 1 49 ? 10.658  -32.847 21.295  1.00 44.94  ? 48  HIS C CA  1 
ATOM   1791 C C   . HIS C 1 49 ? 11.105  -34.063 22.116  1.00 41.58  ? 48  HIS C C   1 
ATOM   1792 O O   . HIS C 1 49 ? 10.468  -34.400 23.115  1.00 46.54  ? 48  HIS C O   1 
ATOM   1793 C CB  . HIS C 1 49 ? 9.149   -32.622 21.462  1.00 40.44  ? 48  HIS C CB  1 
ATOM   1794 C CG  . HIS C 1 49 ? 8.601   -31.512 20.623  1.00 43.72  ? 48  HIS C CG  1 
ATOM   1795 N ND1 . HIS C 1 49 ? 7.469   -31.675 19.849  1.00 48.47  ? 48  HIS C ND1 1 
ATOM   1796 C CD2 . HIS C 1 49 ? 9.032   -30.266 20.401  1.00 44.82  ? 48  HIS C CD2 1 
ATOM   1797 C CE1 . HIS C 1 49 ? 7.226   -30.548 19.192  1.00 50.95  ? 48  HIS C CE1 1 
ATOM   1798 N NE2 . HIS C 1 49 ? 8.160   -29.676 19.516  1.00 47.69  ? 48  HIS C NE2 1 
ATOM   1799 N N   . GLU C 1 50 ? 12.211  -34.697 21.724  1.00 37.27  ? 49  GLU C N   1 
ATOM   1800 C CA  . GLU C 1 50 ? 12.769  -35.778 22.522  1.00 37.73  ? 49  GLU C CA  1 
ATOM   1801 C C   . GLU C 1 50 ? 13.917  -35.273 23.401  1.00 37.17  ? 49  GLU C C   1 
ATOM   1802 O O   . GLU C 1 50 ? 14.273  -34.102 23.366  1.00 32.23  ? 49  GLU C O   1 
ATOM   1803 C CB  . GLU C 1 50 ? 13.184  -36.894 21.581  1.00 36.74  ? 49  GLU C CB  1 
ATOM   1804 C CG  . GLU C 1 50 ? 12.006  -37.471 20.803  1.00 48.21  ? 49  GLU C CG  1 
ATOM   1805 C CD  . GLU C 1 50 ? 12.565  -38.396 19.743  1.00 53.80  ? 49  GLU C CD  1 
ATOM   1806 O OE1 . GLU C 1 50 ? 13.790  -38.682 19.777  1.00 58.21  ? 49  GLU C OE1 1 
ATOM   1807 O OE2 . GLU C 1 50 ? 11.780  -38.809 18.866  1.00 65.07  ? 49  GLU C OE2 1 
ATOM   1808 N N   . THR C 1 51 ? 14.437  -36.159 24.263  1.00 40.39  ? 50  THR C N   1 
ATOM   1809 C CA  . THR C 1 51 ? 15.466  -35.804 25.241  1.00 38.69  ? 50  THR C CA  1 
ATOM   1810 C C   . THR C 1 51 ? 16.600  -36.829 25.179  1.00 36.90  ? 50  THR C C   1 
ATOM   1811 O O   . THR C 1 51 ? 16.414  -37.968 24.758  1.00 36.18  ? 50  THR C O   1 
ATOM   1812 C CB  . THR C 1 51 ? 14.895  -35.729 26.663  1.00 41.57  ? 50  THR C CB  1 
ATOM   1813 O OG1 . THR C 1 51 ? 14.336  -37.023 26.875  1.00 40.93  ? 50  THR C OG1 1 
ATOM   1814 C CG2 . THR C 1 51 ? 13.869  -34.628 26.871  1.00 45.25  ? 50  THR C CG2 1 
ATOM   1815 N N   . ALA C 1 52 ? 17.799  -36.369 25.537  1.00 34.48  ? 51  ALA C N   1 
ATOM   1816 C CA  . ALA C 1 52 ? 18.986  -37.190 25.704  1.00 38.24  ? 51  ALA C CA  1 
ATOM   1817 C C   . ALA C 1 52 ? 19.941  -36.442 26.624  1.00 39.44  ? 51  ALA C C   1 
ATOM   1818 O O   . ALA C 1 52 ? 19.711  -35.285 26.951  1.00 39.95  ? 51  ALA C O   1 
ATOM   1819 C CB  . ALA C 1 52 ? 19.629  -37.501 24.369  1.00 32.91  ? 51  ALA C CB  1 
ATOM   1820 N N   . PHE C 1 53 ? 20.998  -37.141 27.053  1.00 41.58  ? 52  PHE C N   1 
ATOM   1821 C CA  . PHE C 1 53 ? 22.086  -36.583 27.831  1.00 39.74  ? 52  PHE C CA  1 
ATOM   1822 C C   . PHE C 1 53 ? 23.280  -36.473 26.895  1.00 37.20  ? 52  PHE C C   1 
ATOM   1823 O O   . PHE C 1 53 ? 23.624  -37.446 26.229  1.00 35.90  ? 52  PHE C O   1 
ATOM   1824 C CB  . PHE C 1 53 ? 22.354  -37.591 28.959  1.00 37.94  ? 52  PHE C CB  1 
ATOM   1825 C CG  . PHE C 1 53 ? 21.371  -37.492 30.117  1.00 37.93  ? 52  PHE C CG  1 
ATOM   1826 C CD1 . PHE C 1 53 ? 21.139  -36.279 30.760  1.00 39.38  ? 52  PHE C CD1 1 
ATOM   1827 C CD2 . PHE C 1 53 ? 20.678  -38.617 30.561  1.00 49.06  ? 52  PHE C CD2 1 
ATOM   1828 C CE1 . PHE C 1 53 ? 20.241  -36.189 31.819  1.00 43.28  ? 52  PHE C CE1 1 
ATOM   1829 C CE2 . PHE C 1 53 ? 19.776  -38.522 31.619  1.00 48.30  ? 52  PHE C CE2 1 
ATOM   1830 C CZ  . PHE C 1 53 ? 19.544  -37.306 32.230  1.00 41.67  ? 52  PHE C CZ  1 
ATOM   1831 N N   . LEU C 1 54 ? 23.926  -35.303 26.870  1.00 32.28  ? 53  LEU C N   1 
ATOM   1832 C CA  . LEU C 1 54 ? 25.065  -35.084 25.992  1.00 29.81  ? 53  LEU C CA  1 
ATOM   1833 C C   . LEU C 1 54 ? 26.134  -34.306 26.746  1.00 29.91  ? 53  LEU C C   1 
ATOM   1834 O O   . LEU C 1 54 ? 25.823  -33.470 27.590  1.00 35.63  ? 53  LEU C O   1 
ATOM   1835 C CB  . LEU C 1 54 ? 24.686  -34.315 24.716  1.00 31.43  ? 53  LEU C CB  1 
ATOM   1836 C CG  . LEU C 1 54 ? 23.797  -35.032 23.694  1.00 38.56  ? 53  LEU C CG  1 
ATOM   1837 C CD1 . LEU C 1 54 ? 23.414  -34.091 22.559  1.00 30.93  ? 53  LEU C CD1 1 
ATOM   1838 C CD2 . LEU C 1 54 ? 24.449  -36.317 23.142  1.00 45.20  ? 53  LEU C CD2 1 
ATOM   1839 N N   . GLY C 1 55 ? 27.388  -34.572 26.370  1.00 32.05  ? 54  GLY C N   1 
ATOM   1840 C CA  . GLY C 1 55 ? 28.550  -33.883 26.903  1.00 33.54  ? 54  GLY C CA  1 
ATOM   1841 C C   . GLY C 1 55 ? 28.831  -32.580 26.158  1.00 41.29  ? 54  GLY C C   1 
ATOM   1842 O O   . GLY C 1 55 ? 28.317  -32.321 25.052  1.00 38.02  ? 54  GLY C O   1 
ATOM   1843 N N   . PRO C 1 56 ? 29.638  -31.684 26.767  1.00 42.83  ? 55  PRO C N   1 
ATOM   1844 C CA  . PRO C 1 56 ? 29.837  -30.342 26.222  1.00 44.07  ? 55  PRO C CA  1 
ATOM   1845 C C   . PRO C 1 56 ? 30.420  -30.324 24.811  1.00 42.35  ? 55  PRO C C   1 
ATOM   1846 O O   . PRO C 1 56 ? 30.107  -29.434 24.020  1.00 55.72  ? 55  PRO C O   1 
ATOM   1847 C CB  . PRO C 1 56 ? 30.740  -29.639 27.278  1.00 47.07  ? 55  PRO C CB  1 
ATOM   1848 C CG  . PRO C 1 56 ? 31.401  -30.779 28.016  1.00 42.74  ? 55  PRO C CG  1 
ATOM   1849 C CD  . PRO C 1 56 ? 30.368  -31.903 28.028  1.00 44.89  ? 55  PRO C CD  1 
ATOM   1850 N N   . LYS C 1 57 ? 31.203  -31.352 24.486  1.00 42.95  ? 56  LYS C N   1 
ATOM   1851 C CA  . LYS C 1 57 ? 31.835  -31.456 23.182  1.00 49.24  ? 56  LYS C CA  1 
ATOM   1852 C C   . LYS C 1 57 ? 30.768  -31.544 22.089  1.00 48.80  ? 56  LYS C C   1 
ATOM   1853 O O   . LYS C 1 57 ? 31.046  -31.180 20.947  1.00 44.41  ? 56  LYS C O   1 
ATOM   1854 C CB  . LYS C 1 57 ? 32.735  -32.693 23.088  1.00 52.43  ? 56  LYS C CB  1 
ATOM   1855 N N   . ASP C 1 58 ? 29.564  -32.028 22.448  1.00 45.03  ? 57  ASP C N   1 
ATOM   1856 C CA  . ASP C 1 58 ? 28.529  -32.311 21.457  1.00 43.56  ? 57  ASP C CA  1 
ATOM   1857 C C   . ASP C 1 58 ? 27.604  -31.115 21.281  1.00 40.83  ? 57  ASP C C   1 
ATOM   1858 O O   . ASP C 1 58 ? 26.590  -31.215 20.586  1.00 39.92  ? 57  ASP C O   1 
ATOM   1859 C CB  . ASP C 1 58 ? 27.695  -33.529 21.820  1.00 41.62  ? 57  ASP C CB  1 
ATOM   1860 C CG  . ASP C 1 58 ? 28.479  -34.823 21.935  1.00 44.55  ? 57  ASP C CG  1 
ATOM   1861 O OD1 . ASP C 1 58 ? 29.357  -35.029 21.104  1.00 46.77  ? 57  ASP C OD1 1 
ATOM   1862 O OD2 . ASP C 1 58 ? 28.170  -35.631 22.825  1.00 56.53  ? 57  ASP C OD2 1 
ATOM   1863 N N   . LEU C 1 59 ? 27.931  -29.994 21.934  1.00 35.91  ? 58  LEU C N   1 
ATOM   1864 C CA  . LEU C 1 59 ? 26.984  -28.895 22.057  1.00 35.88  ? 58  LEU C CA  1 
ATOM   1865 C C   . LEU C 1 59 ? 27.584  -27.613 21.494  1.00 41.58  ? 58  LEU C C   1 
ATOM   1866 O O   . LEU C 1 59 ? 28.793  -27.418 21.619  1.00 46.42  ? 58  LEU C O   1 
ATOM   1867 C CB  . LEU C 1 59 ? 26.635  -28.702 23.531  1.00 36.95  ? 58  LEU C CB  1 
ATOM   1868 C CG  . LEU C 1 59 ? 25.993  -29.908 24.219  1.00 35.00  ? 58  LEU C CG  1 
ATOM   1869 C CD1 . LEU C 1 59 ? 25.837  -29.692 25.712  1.00 34.11  ? 58  LEU C CD1 1 
ATOM   1870 C CD2 . LEU C 1 59 ? 24.637  -30.199 23.557  1.00 28.91  ? 58  LEU C CD2 1 
ATOM   1871 N N   . PHE C 1 60 ? 26.727  -26.743 20.930  1.00 43.23  ? 59  PHE C N   1 
ATOM   1872 C CA  . PHE C 1 60 ? 27.168  -25.534 20.230  1.00 43.75  ? 59  PHE C CA  1 
ATOM   1873 C C   . PHE C 1 60 ? 26.212  -24.370 20.511  1.00 44.14  ? 59  PHE C C   1 
ATOM   1874 O O   . PHE C 1 60 ? 25.023  -24.423 20.202  1.00 39.31  ? 59  PHE C O   1 
ATOM   1875 C CB  . PHE C 1 60 ? 27.467  -25.775 18.742  1.00 42.74  ? 59  PHE C CB  1 
ATOM   1876 C CG  . PHE C 1 60 ? 28.430  -26.916 18.430  1.00 40.53  ? 59  PHE C CG  1 
ATOM   1877 C CD1 . PHE C 1 60 ? 27.980  -28.231 18.316  1.00 38.01  ? 59  PHE C CD1 1 
ATOM   1878 C CD2 . PHE C 1 60 ? 29.792  -26.680 18.235  1.00 46.06  ? 59  PHE C CD2 1 
ATOM   1879 C CE1 . PHE C 1 60 ? 28.853  -29.280 18.076  1.00 39.81  ? 59  PHE C CE1 1 
ATOM   1880 C CE2 . PHE C 1 60 ? 30.668  -27.731 17.954  1.00 43.47  ? 59  PHE C CE2 1 
ATOM   1881 C CZ  . PHE C 1 60 ? 30.202  -29.029 17.879  1.00 47.70  ? 59  PHE C CZ  1 
ATOM   1882 N N   . PRO C 1 61 ? 26.680  -23.249 21.115  1.00 47.67  ? 60  PRO C N   1 
ATOM   1883 C CA  . PRO C 1 61 ? 25.791  -22.111 21.375  1.00 49.52  ? 60  PRO C CA  1 
ATOM   1884 C C   . PRO C 1 61 ? 25.108  -21.693 20.074  1.00 42.20  ? 60  PRO C C   1 
ATOM   1885 O O   . PRO C 1 61 ? 25.751  -21.598 19.034  1.00 48.07  ? 60  PRO C O   1 
ATOM   1886 C CB  . PRO C 1 61 ? 26.686  -21.004 21.988  1.00 47.20  ? 60  PRO C CB  1 
ATOM   1887 C CG  . PRO C 1 61 ? 28.001  -21.699 22.300  1.00 48.55  ? 60  PRO C CG  1 
ATOM   1888 C CD  . PRO C 1 61 ? 28.076  -23.012 21.535  1.00 54.57  ? 60  PRO C CD  1 
ATOM   1889 N N   . TYR C 1 62 ? 23.780  -21.512 20.144  1.00 52.81  ? 61  TYR C N   1 
ATOM   1890 C CA  . TYR C 1 62 ? 22.921  -21.309 18.986  1.00 50.48  ? 61  TYR C CA  1 
ATOM   1891 C C   . TYR C 1 62 ? 23.350  -20.075 18.194  1.00 60.48  ? 61  TYR C C   1 
ATOM   1892 O O   . TYR C 1 62 ? 23.732  -20.191 17.026  1.00 57.89  ? 61  TYR C O   1 
ATOM   1893 C CB  . TYR C 1 62 ? 21.458  -21.224 19.421  1.00 51.71  ? 61  TYR C CB  1 
ATOM   1894 C CG  . TYR C 1 62 ? 20.470  -20.800 18.341  1.00 49.67  ? 61  TYR C CG  1 
ATOM   1895 C CD1 . TYR C 1 62 ? 20.166  -21.646 17.275  1.00 46.67  ? 61  TYR C CD1 1 
ATOM   1896 C CD2 . TYR C 1 62 ? 19.811  -19.575 18.411  1.00 51.20  ? 61  TYR C CD2 1 
ATOM   1897 C CE1 . TYR C 1 62 ? 19.240  -21.280 16.303  1.00 46.05  ? 61  TYR C CE1 1 
ATOM   1898 C CE2 . TYR C 1 62 ? 18.896  -19.195 17.439  1.00 53.43  ? 61  TYR C CE2 1 
ATOM   1899 C CZ  . TYR C 1 62 ? 18.612  -20.045 16.379  1.00 46.07  ? 61  TYR C CZ  1 
ATOM   1900 O OH  . TYR C 1 62 ? 17.699  -19.677 15.425  1.00 46.03  ? 61  TYR C OH  1 
ATOM   1901 N N   . ASP C 1 63 ? 23.314  -18.908 18.854  1.00 57.97  ? 62  ASP C N   1 
ATOM   1902 C CA  . ASP C 1 63 ? 23.682  -17.654 18.215  1.00 57.64  ? 62  ASP C CA  1 
ATOM   1903 C C   . ASP C 1 63 ? 25.052  -17.737 17.554  1.00 52.52  ? 62  ASP C C   1 
ATOM   1904 O O   . ASP C 1 63 ? 25.221  -17.218 16.451  1.00 64.17  ? 62  ASP C O   1 
ATOM   1905 C CB  . ASP C 1 63 ? 23.446  -16.447 19.108  1.00 64.79  ? 62  ASP C CB  1 
ATOM   1906 C CG  . ASP C 1 63 ? 21.974  -16.086 19.256  1.00 80.18  ? 62  ASP C CG  1 
ATOM   1907 O OD1 . ASP C 1 63 ? 21.563  -15.781 20.393  1.00 78.90  ? 62  ASP C OD1 1 
ATOM   1908 O OD2 . ASP C 1 63 ? 21.234  -16.156 18.237  1.00 78.22  ? 62  ASP C OD2 1 
ATOM   1909 N N   . LYS C 1 64 ? 26.009  -18.402 18.205  1.00 41.94  ? 63  LYS C N   1 
ATOM   1910 C CA  . LYS C 1 64 ? 27.363  -18.496 17.680  1.00 44.89  ? 63  LYS C CA  1 
ATOM   1911 C C   . LYS C 1 64 ? 27.405  -19.385 16.435  1.00 47.29  ? 63  LYS C C   1 
ATOM   1912 O O   . LYS C 1 64 ? 28.210  -19.131 15.537  1.00 41.05  ? 63  LYS C O   1 
ATOM   1913 C CB  . LYS C 1 64 ? 28.389  -18.902 18.751  1.00 48.72  ? 63  LYS C CB  1 
ATOM   1914 N N   . SER C 1 65 ? 26.524  -20.412 16.357  1.00 42.42  ? 64  SER C N   1 
ATOM   1915 C CA  . SER C 1 65 ? 26.744  -21.426 15.332  1.00 38.87  ? 64  SER C CA  1 
ATOM   1916 C C   . SER C 1 65 ? 25.597  -21.531 14.316  1.00 40.17  ? 64  SER C C   1 
ATOM   1917 O O   . SER C 1 65 ? 25.686  -22.332 13.390  1.00 40.74  ? 64  SER C O   1 
ATOM   1918 C CB  . SER C 1 65 ? 27.095  -22.773 15.950  1.00 41.00  ? 64  SER C CB  1 
ATOM   1919 O OG  . SER C 1 65 ? 25.960  -23.268 16.654  1.00 38.05  ? 64  SER C OG  1 
ATOM   1920 N N   . LYS C 1 66 ? 24.527  -20.736 14.475  1.00 39.62  ? 65  LYS C N   1 
ATOM   1921 C CA  . LYS C 1 66 ? 23.368  -20.877 13.596  1.00 42.72  ? 65  LYS C CA  1 
ATOM   1922 C C   . LYS C 1 66 ? 23.724  -20.626 12.127  1.00 47.72  ? 65  LYS C C   1 
ATOM   1923 O O   . LYS C 1 66 ? 23.167  -21.293 11.257  1.00 46.34  ? 65  LYS C O   1 
ATOM   1924 C CB  . LYS C 1 66 ? 22.109  -20.086 13.971  1.00 42.97  ? 65  LYS C CB  1 
ATOM   1925 C CG  . LYS C 1 66 ? 22.266  -18.580 14.040  1.00 37.32  ? 65  LYS C CG  1 
ATOM   1926 C CD  . LYS C 1 66 ? 20.907  -17.900 14.139  1.00 46.38  ? 65  LYS C CD  1 
ATOM   1927 C CE  . LYS C 1 66 ? 21.127  -16.432 14.282  1.00 52.67  ? 65  LYS C CE  1 
ATOM   1928 N NZ  . LYS C 1 66 ? 20.043  -15.908 15.098  1.00 46.36  ? 65  LYS C NZ  1 
ATOM   1929 N N   . ASP C 1 67 ? 24.658  -19.701 11.847  1.00 45.04  ? 66  ASP C N   1 
ATOM   1930 C CA  . ASP C 1 67 ? 25.033  -19.429 10.457  1.00 44.01  ? 66  ASP C CA  1 
ATOM   1931 C C   . ASP C 1 67 ? 25.478  -20.727 9.778   1.00 43.99  ? 66  ASP C C   1 
ATOM   1932 O O   . ASP C 1 67 ? 25.174  -20.949 8.609   1.00 41.65  ? 66  ASP C O   1 
ATOM   1933 C CB  . ASP C 1 67 ? 25.859  -18.154 10.265  1.00 45.89  ? 66  ASP C CB  1 
ATOM   1934 C CG  . ASP C 1 67 ? 27.312  -18.131 10.733  1.00 56.45  ? 66  ASP C CG  1 
ATOM   1935 O OD1 . ASP C 1 67 ? 27.996  -19.171 10.617  1.00 58.34  ? 66  ASP C OD1 1 
ATOM   1936 O OD2 . ASP C 1 67 ? 27.785  -17.041 11.138  1.00 60.46  ? 66  ASP C OD2 1 
ATOM   1937 N N   . LYS C 1 68 ? 26.081  -21.635 10.562  1.00 38.90  ? 67  LYS C N   1 
ATOM   1938 C CA  . LYS C 1 68 ? 26.592  -22.901 10.059  1.00 40.11  ? 67  LYS C CA  1 
ATOM   1939 C C   . LYS C 1 68 ? 25.543  -24.028 10.145  1.00 38.87  ? 67  LYS C C   1 
ATOM   1940 O O   . LYS C 1 68 ? 25.372  -24.780 9.187   1.00 43.42  ? 67  LYS C O   1 
ATOM   1941 C CB  . LYS C 1 68 ? 27.901  -23.168 10.810  1.00 37.71  ? 67  LYS C CB  1 
ATOM   1942 C CG  . LYS C 1 68 ? 28.628  -24.451 10.457  1.00 47.07  ? 67  LYS C CG  1 
ATOM   1943 C CD  . LYS C 1 68 ? 29.960  -24.600 11.194  1.00 50.71  ? 67  LYS C CD  1 
ATOM   1944 C CE  . LYS C 1 68 ? 30.606  -25.946 11.022  1.00 60.18  ? 67  LYS C CE  1 
ATOM   1945 N NZ  . LYS C 1 68 ? 30.755  -26.311 9.607   1.00 65.42  ? 67  LYS C NZ  1 
ATOM   1946 N N   . TYR C 1 69 ? 24.806  -24.145 11.260  1.00 36.65  ? 68  TYR C N   1 
ATOM   1947 C CA  . TYR C 1 69 ? 23.955  -25.321 11.428  1.00 34.26  ? 68  TYR C CA  1 
ATOM   1948 C C   . TYR C 1 69 ? 22.473  -25.010 11.203  1.00 33.34  ? 68  TYR C C   1 
ATOM   1949 O O   . TYR C 1 69 ? 21.680  -25.933 11.046  1.00 32.17  ? 68  TYR C O   1 
ATOM   1950 C CB  . TYR C 1 69 ? 24.134  -25.887 12.845  1.00 31.58  ? 68  TYR C CB  1 
ATOM   1951 C CG  . TYR C 1 69 ? 25.552  -26.361 13.140  1.00 32.78  ? 68  TYR C CG  1 
ATOM   1952 C CD1 . TYR C 1 69 ? 26.252  -27.181 12.254  1.00 35.31  ? 68  TYR C CD1 1 
ATOM   1953 C CD2 . TYR C 1 69 ? 26.194  -25.955 14.305  1.00 38.84  ? 68  TYR C CD2 1 
ATOM   1954 C CE1 . TYR C 1 69 ? 27.536  -27.632 12.543  1.00 38.03  ? 68  TYR C CE1 1 
ATOM   1955 C CE2 . TYR C 1 69 ? 27.474  -26.398 14.599  1.00 39.73  ? 68  TYR C CE2 1 
ATOM   1956 C CZ  . TYR C 1 69 ? 28.142  -27.234 13.724  1.00 37.38  ? 68  TYR C CZ  1 
ATOM   1957 O OH  . TYR C 1 69 ? 29.431  -27.596 14.041  1.00 43.93  ? 68  TYR C OH  1 
ATOM   1958 N N   . GLY C 1 70 ? 22.086  -23.727 11.262  1.00 34.39  ? 69  GLY C N   1 
ATOM   1959 C CA  . GLY C 1 70 ? 20.676  -23.382 11.153  1.00 35.39  ? 69  GLY C CA  1 
ATOM   1960 C C   . GLY C 1 70 ? 20.312  -23.233 9.686   1.00 38.14  ? 69  GLY C C   1 
ATOM   1961 O O   . GLY C 1 70 ? 20.286  -22.120 9.164   1.00 37.12  ? 69  GLY C O   1 
ATOM   1962 N N   . LYS C 1 71 ? 20.178  -24.380 9.022   1.00 34.32  ? 70  LYS C N   1 
ATOM   1963 C CA  . LYS C 1 71 ? 19.842  -24.456 7.611   1.00 36.99  ? 70  LYS C CA  1 
ATOM   1964 C C   . LYS C 1 71 ? 18.963  -25.688 7.483   1.00 37.78  ? 70  LYS C C   1 
ATOM   1965 O O   . LYS C 1 71 ? 19.127  -26.635 8.252   1.00 41.12  ? 70  LYS C O   1 
ATOM   1966 C CB  . LYS C 1 71 ? 21.054  -24.636 6.685   1.00 39.07  ? 70  LYS C CB  1 
ATOM   1967 C CG  . LYS C 1 71 ? 22.116  -25.560 7.240   1.00 41.33  ? 70  LYS C CG  1 
ATOM   1968 C CD  . LYS C 1 71 ? 23.194  -26.213 6.382   1.00 48.27  ? 70  LYS C CD  1 
ATOM   1969 C CE  . LYS C 1 71 ? 24.027  -27.099 7.275   1.00 47.89  ? 70  LYS C CE  1 
ATOM   1970 N N   . PRO C 1 72 ? 17.943  -25.667 6.598   1.00 35.51  ? 71  PRO C N   1 
ATOM   1971 C CA  . PRO C 1 72 ? 16.985  -26.764 6.539   1.00 28.37  ? 71  PRO C CA  1 
ATOM   1972 C C   . PRO C 1 72 ? 17.658  -28.083 6.177   1.00 31.74  ? 71  PRO C C   1 
ATOM   1973 O O   . PRO C 1 72 ? 18.671  -28.121 5.487   1.00 35.54  ? 71  PRO C O   1 
ATOM   1974 C CB  . PRO C 1 72 ? 16.044  -26.320 5.409   1.00 29.16  ? 71  PRO C CB  1 
ATOM   1975 C CG  . PRO C 1 72 ? 16.124  -24.801 5.498   1.00 31.59  ? 71  PRO C CG  1 
ATOM   1976 C CD  . PRO C 1 72 ? 17.602  -24.538 5.708   1.00 31.86  ? 71  PRO C CD  1 
ATOM   1977 N N   . ASN C 1 73 ? 17.006  -29.156 6.579   1.00 34.28  ? 72  ASN C N   1 
ATOM   1978 C CA  . ASN C 1 73 ? 17.298  -30.436 5.966   1.00 41.51  ? 72  ASN C CA  1 
ATOM   1979 C C   . ASN C 1 73 ? 16.074  -31.323 6.145   1.00 35.16  ? 72  ASN C C   1 
ATOM   1980 O O   . ASN C 1 73 ? 15.122  -30.943 6.810   1.00 32.95  ? 72  ASN C O   1 
ATOM   1981 C CB  . ASN C 1 73 ? 18.637  -31.021 6.409   1.00 47.19  ? 72  ASN C CB  1 
ATOM   1982 C CG  . ASN C 1 73 ? 18.541  -31.651 7.772   1.00 45.24  ? 72  ASN C CG  1 
ATOM   1983 O OD1 . ASN C 1 73 ? 18.034  -32.772 7.928   1.00 41.24  ? 72  ASN C OD1 1 
ATOM   1984 N ND2 . ASN C 1 73 ? 19.034  -30.932 8.755   1.00 48.07  ? 72  ASN C ND2 1 
ATOM   1985 N N   . LYS C 1 74 ? 16.128  -32.512 5.543   1.00 37.44  ? 73  LYS C N   1 
ATOM   1986 C CA  . LYS C 1 74 ? 14.902  -33.270 5.344   1.00 34.13  ? 73  LYS C CA  1 
ATOM   1987 C C   . LYS C 1 74 ? 14.661  -34.243 6.496   1.00 37.89  ? 73  LYS C C   1 
ATOM   1988 O O   . LYS C 1 74 ? 13.624  -34.913 6.522   1.00 40.26  ? 73  LYS C O   1 
ATOM   1989 C CB  . LYS C 1 74 ? 14.955  -33.951 3.968   1.00 37.77  ? 73  LYS C CB  1 
ATOM   1990 N N   . ARG C 1 75 ? 15.589  -34.303 7.469   1.00 35.72  ? 74  ARG C N   1 
ATOM   1991 C CA  . ARG C 1 75 ? 15.422  -35.245 8.579   1.00 34.27  ? 74  ARG C CA  1 
ATOM   1992 C C   . ARG C 1 75 ? 14.165  -34.908 9.378   1.00 36.99  ? 74  ARG C C   1 
ATOM   1993 O O   . ARG C 1 75 ? 13.810  -33.728 9.539   1.00 36.35  ? 74  ARG C O   1 
ATOM   1994 C CB  . ARG C 1 75 ? 16.672  -35.327 9.480   1.00 36.67  ? 74  ARG C CB  1 
ATOM   1995 C CG  . ARG C 1 75 ? 17.986  -35.608 8.749   1.00 41.20  ? 74  ARG C CG  1 
ATOM   1996 C CD  . ARG C 1 75 ? 18.248  -37.025 8.203   1.00 40.69  ? 74  ARG C CD  1 
ATOM   1997 N NE  . ARG C 1 75 ? 18.098  -37.955 9.324   1.00 36.26  ? 74  ARG C NE  1 
ATOM   1998 C CZ  . ARG C 1 75 ? 19.176  -38.437 9.949   1.00 37.57  ? 74  ARG C CZ  1 
ATOM   1999 N NH1 . ARG C 1 75 ? 19.020  -39.097 11.082  1.00 40.50  ? 74  ARG C NH1 1 
ATOM   2000 N NH2 . ARG C 1 75 ? 20.373  -38.162 9.446   1.00 33.74  ? 74  ARG C NH2 1 
ATOM   2001 N N   . LYS C 1 76 ? 13.488  -35.957 9.879   1.00 37.33  ? 75  LYS C N   1 
ATOM   2002 C CA  . LYS C 1 76 ? 12.173  -35.822 10.495  1.00 41.89  ? 75  LYS C CA  1 
ATOM   2003 C C   . LYS C 1 76 ? 12.199  -34.838 11.664  1.00 39.23  ? 75  LYS C C   1 
ATOM   2004 O O   . LYS C 1 76 ? 12.983  -34.997 12.604  1.00 34.03  ? 75  LYS C O   1 
ATOM   2005 C CB  . LYS C 1 76 ? 11.539  -37.162 10.909  1.00 42.27  ? 75  LYS C CB  1 
ATOM   2006 C CG  . LYS C 1 76 ? 10.013  -37.145 10.949  1.00 45.45  ? 75  LYS C CG  1 
ATOM   2007 C CD  . LYS C 1 76 ? 9.363   -38.425 11.474  1.00 51.19  ? 75  LYS C CD  1 
ATOM   2008 N N   . GLY C 1 77 ? 11.293  -33.849 11.611  1.00 36.40  ? 76  GLY C N   1 
ATOM   2009 C CA  . GLY C 1 77 ? 11.108  -32.906 12.708  1.00 33.16  ? 76  GLY C CA  1 
ATOM   2010 C C   . GLY C 1 77 ? 12.114  -31.747 12.668  1.00 30.56  ? 76  GLY C C   1 
ATOM   2011 O O   . GLY C 1 77 ? 12.009  -30.823 13.473  1.00 37.88  ? 76  GLY C O   1 
ATOM   2012 N N   . PHE C 1 78 ? 13.066  -31.761 11.728  1.00 32.26  ? 77  PHE C N   1 
ATOM   2013 C CA  . PHE C 1 78 ? 14.192  -30.839 11.791  1.00 31.52  ? 77  PHE C CA  1 
ATOM   2014 C C   . PHE C 1 78 ? 13.725  -29.395 11.543  1.00 35.02  ? 77  PHE C C   1 
ATOM   2015 O O   . PHE C 1 78 ? 14.122  -28.467 12.244  1.00 30.09  ? 77  PHE C O   1 
ATOM   2016 C CB  . PHE C 1 78 ? 15.292  -31.187 10.789  1.00 34.67  ? 77  PHE C CB  1 
ATOM   2017 C CG  . PHE C 1 78 ? 16.580  -30.416 11.065  1.00 33.24  ? 77  PHE C CG  1 
ATOM   2018 C CD1 . PHE C 1 78 ? 16.775  -29.149 10.529  1.00 34.17  ? 77  PHE C CD1 1 
ATOM   2019 C CD2 . PHE C 1 78 ? 17.604  -30.973 11.827  1.00 30.14  ? 77  PHE C CD2 1 
ATOM   2020 C CE1 . PHE C 1 78 ? 17.950  -28.450 10.762  1.00 31.76  ? 77  PHE C CE1 1 
ATOM   2021 C CE2 . PHE C 1 78 ? 18.792  -30.274 12.052  1.00 29.84  ? 77  PHE C CE2 1 
ATOM   2022 C CZ  . PHE C 1 78 ? 18.956  -29.011 11.534  1.00 33.92  ? 77  PHE C CZ  1 
ATOM   2023 N N   . ASN C 1 79 ? 12.908  -29.214 10.498  1.00 33.82  ? 78  ASN C N   1 
ATOM   2024 C CA  . ASN C 1 79 ? 12.534  -27.877 10.059  1.00 37.65  ? 78  ASN C CA  1 
ATOM   2025 C C   . ASN C 1 79 ? 11.552  -27.251 11.041  1.00 33.78  ? 78  ASN C C   1 
ATOM   2026 O O   . ASN C 1 79 ? 11.642  -26.059 11.339  1.00 32.79  ? 78  ASN C O   1 
ATOM   2027 C CB  . ASN C 1 79 ? 12.072  -27.854 8.606   1.00 34.54  ? 78  ASN C CB  1 
ATOM   2028 C CG  . ASN C 1 79 ? 13.176  -28.278 7.670   1.00 33.29  ? 78  ASN C CG  1 
ATOM   2029 O OD1 . ASN C 1 79 ? 14.360  -28.001 7.915   1.00 31.15  ? 78  ASN C OD1 1 
ATOM   2030 N ND2 . ASN C 1 79 ? 12.814  -28.955 6.590   1.00 30.27  ? 78  ASN C ND2 1 
ATOM   2031 N N   . GLU C 1 80 ? 10.685  -28.068 11.631  1.00 36.35  ? 79  GLU C N   1 
ATOM   2032 C CA  . GLU C 1 80 ? 9.861   -27.543 12.714  1.00 36.43  ? 79  GLU C CA  1 
ATOM   2033 C C   . GLU C 1 80 ? 10.757  -27.167 13.894  1.00 39.81  ? 79  GLU C C   1 
ATOM   2034 O O   . GLU C 1 80 ? 10.546  -26.140 14.536  1.00 34.62  ? 79  GLU C O   1 
ATOM   2035 C CB  . GLU C 1 80 ? 8.781   -28.561 13.079  1.00 39.82  ? 79  GLU C CB  1 
ATOM   2036 C CG  . GLU C 1 80 ? 7.854   -28.057 14.178  1.00 42.69  ? 79  GLU C CG  1 
ATOM   2037 C CD  . GLU C 1 80 ? 6.610   -28.900 14.346  1.00 45.41  ? 79  GLU C CD  1 
ATOM   2038 O OE1 . GLU C 1 80 ? 6.486   -29.983 13.740  1.00 50.33  ? 79  GLU C OE1 1 
ATOM   2039 O OE2 . GLU C 1 80 ? 5.752   -28.454 15.116  1.00 51.85  ? 79  GLU C OE2 1 
ATOM   2040 N N   . GLY C 1 81 ? 11.783  -27.999 14.169  1.00 32.97  ? 80  GLY C N   1 
ATOM   2041 C CA  . GLY C 1 81 ? 12.759  -27.625 15.185  1.00 33.35  ? 80  GLY C CA  1 
ATOM   2042 C C   . GLY C 1 81 ? 13.394  -26.257 14.921  1.00 35.11  ? 80  GLY C C   1 
ATOM   2043 O O   . GLY C 1 81 ? 13.599  -25.488 15.857  1.00 32.43  ? 80  GLY C O   1 
ATOM   2044 N N   . LEU C 1 82 ? 13.788  -25.999 13.659  1.00 33.59  ? 81  LEU C N   1 
ATOM   2045 C CA  . LEU C 1 82 ? 14.364  -24.702 13.291  1.00 34.69  ? 81  LEU C CA  1 
ATOM   2046 C C   . LEU C 1 82 ? 13.367  -23.570 13.568  1.00 33.09  ? 81  LEU C C   1 
ATOM   2047 O O   . LEU C 1 82 ? 13.767  -22.488 14.001  1.00 36.04  ? 81  LEU C O   1 
ATOM   2048 C CB  . LEU C 1 82 ? 14.883  -24.616 11.856  1.00 34.13  ? 81  LEU C CB  1 
ATOM   2049 C CG  . LEU C 1 82 ? 16.117  -25.457 11.495  1.00 29.81  ? 81  LEU C CG  1 
ATOM   2050 C CD1 . LEU C 1 82 ? 16.356  -25.319 10.003  1.00 31.60  ? 81  LEU C CD1 1 
ATOM   2051 C CD2 . LEU C 1 82 ? 17.345  -24.988 12.216  1.00 28.17  ? 81  LEU C CD2 1 
ATOM   2052 N N   . TRP C 1 83 ? 12.080  -23.818 13.323  1.00 33.12  ? 82  TRP C N   1 
ATOM   2053 C CA  . TRP C 1 83 ? 11.072  -22.794 13.597  1.00 40.84  ? 82  TRP C CA  1 
ATOM   2054 C C   . TRP C 1 83 ? 11.008  -22.471 15.102  1.00 43.02  ? 82  TRP C C   1 
ATOM   2055 O O   . TRP C 1 83 ? 11.098  -21.300 15.498  1.00 40.66  ? 82  TRP C O   1 
ATOM   2056 C CB  . TRP C 1 83 ? 9.698   -23.179 13.017  1.00 38.94  ? 82  TRP C CB  1 
ATOM   2057 C CG  . TRP C 1 83 ? 8.718   -22.033 13.060  1.00 43.02  ? 82  TRP C CG  1 
ATOM   2058 C CD1 . TRP C 1 83 ? 8.532   -21.051 12.127  1.00 44.22  ? 82  TRP C CD1 1 
ATOM   2059 C CD2 . TRP C 1 83 ? 7.840   -21.702 14.158  1.00 44.38  ? 82  TRP C CD2 1 
ATOM   2060 N NE1 . TRP C 1 83 ? 7.569   -20.164 12.540  1.00 40.89  ? 82  TRP C NE1 1 
ATOM   2061 C CE2 . TRP C 1 83 ? 7.131   -20.533 13.783  1.00 39.69  ? 82  TRP C CE2 1 
ATOM   2062 C CE3 . TRP C 1 83 ? 7.586   -22.290 15.406  1.00 41.83  ? 82  TRP C CE3 1 
ATOM   2063 C CZ2 . TRP C 1 83 ? 6.195   -19.940 14.621  1.00 45.13  ? 82  TRP C CZ2 1 
ATOM   2064 C CZ3 . TRP C 1 83 ? 6.650   -21.703 16.234  1.00 45.08  ? 82  TRP C CZ3 1 
ATOM   2065 C CH2 . TRP C 1 83 ? 5.988   -20.534 15.852  1.00 47.54  ? 82  TRP C CH2 1 
ATOM   2066 N N   . GLU C 1 84 ? 10.910  -23.524 15.929  1.00 36.90  ? 83  GLU C N   1 
ATOM   2067 C CA  . GLU C 1 84 ? 10.857  -23.406 17.383  1.00 37.01  ? 83  GLU C CA  1 
ATOM   2068 C C   . GLU C 1 84 ? 12.055  -22.655 17.974  1.00 38.22  ? 83  GLU C C   1 
ATOM   2069 O O   . GLU C 1 84 ? 11.848  -21.767 18.810  1.00 41.07  ? 83  GLU C O   1 
ATOM   2070 C CB  . GLU C 1 84 ? 10.645  -24.769 18.046  1.00 35.93  ? 83  GLU C CB  1 
ATOM   2071 C CG  . GLU C 1 84 ? 9.318   -25.429 17.693  1.00 39.35  ? 83  GLU C CG  1 
ATOM   2072 C CD  . GLU C 1 84 ? 9.204   -26.853 18.192  1.00 43.53  ? 83  GLU C CD  1 
ATOM   2073 O OE1 . GLU C 1 84 ? 10.230  -27.426 18.638  1.00 41.36  ? 83  GLU C OE1 1 
ATOM   2074 O OE2 . GLU C 1 84 ? 8.092   -27.411 18.096  1.00 44.05  ? 83  GLU C OE2 1 
ATOM   2075 N N   . ILE C 1 85 ? 13.297  -22.991 17.568  1.00 36.20  ? 84  ILE C N   1 
ATOM   2076 C CA  . ILE C 1 85 ? 14.483  -22.398 18.178  1.00 36.40  ? 84  ILE C CA  1 
ATOM   2077 C C   . ILE C 1 85 ? 14.576  -20.888 17.908  1.00 39.55  ? 84  ILE C C   1 
ATOM   2078 O O   . ILE C 1 85 ? 15.185  -20.159 18.680  1.00 37.52  ? 84  ILE C O   1 
ATOM   2079 C CB  . ILE C 1 85 ? 15.784  -23.145 17.831  1.00 37.37  ? 84  ILE C CB  1 
ATOM   2080 C CG1 . ILE C 1 85 ? 16.900  -22.785 18.828  1.00 34.45  ? 84  ILE C CG1 1 
ATOM   2081 C CG2 . ILE C 1 85 ? 16.221  -22.934 16.371  1.00 32.53  ? 84  ILE C CG2 1 
ATOM   2082 C CD1 . ILE C 1 85 ? 18.103  -23.715 18.844  1.00 36.03  ? 84  ILE C CD1 1 
ATOM   2083 N N   . GLN C 1 86 ? 13.993  -20.430 16.796  1.00 35.80  ? 85  GLN C N   1 
ATOM   2084 C CA  . GLN C 1 86 ? 14.048  -19.032 16.392  1.00 39.28  ? 85  GLN C CA  1 
ATOM   2085 C C   . GLN C 1 86 ? 12.828  -18.262 16.898  1.00 38.23  ? 85  GLN C C   1 
ATOM   2086 O O   . GLN C 1 86 ? 12.935  -17.075 17.201  1.00 42.78  ? 85  GLN C O   1 
ATOM   2087 C CB  . GLN C 1 86 ? 14.103  -18.949 14.864  1.00 37.61  ? 85  GLN C CB  1 
ATOM   2088 C CG  . GLN C 1 86 ? 14.287  -17.531 14.315  1.00 37.98  ? 85  GLN C CG  1 
ATOM   2089 C CD  . GLN C 1 86 ? 14.701  -17.509 12.856  1.00 39.23  ? 85  GLN C CD  1 
ATOM   2090 O OE1 . GLN C 1 86 ? 14.726  -18.529 12.145  1.00 41.38  ? 85  GLN C OE1 1 
ATOM   2091 N NE2 . GLN C 1 86 ? 15.119  -16.335 12.411  1.00 34.18  ? 85  GLN C NE2 1 
ATOM   2092 N N   . ASN C 1 87 ? 11.687  -18.938 16.991  1.00 38.48  ? 86  ASN C N   1 
ATOM   2093 C CA  . ASN C 1 87 ? 10.414  -18.249 17.144  1.00 44.62  ? 86  ASN C CA  1 
ATOM   2094 C C   . ASN C 1 87 ? 9.760   -18.525 18.499  1.00 48.18  ? 86  ASN C C   1 
ATOM   2095 O O   . ASN C 1 87 ? 8.907   -17.754 18.918  1.00 49.21  ? 86  ASN C O   1 
ATOM   2096 C CB  . ASN C 1 87 ? 9.463   -18.539 15.985  1.00 42.29  ? 86  ASN C CB  1 
ATOM   2097 C CG  . ASN C 1 87 ? 10.024  -17.985 14.702  1.00 50.11  ? 86  ASN C CG  1 
ATOM   2098 O OD1 . ASN C 1 87 ? 10.143  -16.760 14.566  1.00 46.89  ? 86  ASN C OD1 1 
ATOM   2099 N ND2 . ASN C 1 87 ? 10.433  -18.857 13.788  1.00 39.64  ? 86  ASN C ND2 1 
ATOM   2100 N N   . ASN C 1 88 ? 10.101  -19.635 19.167  1.00 46.13  ? 87  ASN C N   1 
ATOM   2101 C CA  . ASN C 1 88 ? 9.354   -20.009 20.364  1.00 45.97  ? 87  ASN C CA  1 
ATOM   2102 C C   . ASN C 1 88 ? 10.211  -20.904 21.258  1.00 41.48  ? 87  ASN C C   1 
ATOM   2103 O O   . ASN C 1 88 ? 9.769   -21.985 21.659  1.00 49.10  ? 87  ASN C O   1 
ATOM   2104 C CB  . ASN C 1 88 ? 8.048   -20.714 20.002  1.00 49.57  ? 87  ASN C CB  1 
ATOM   2105 C CG  . ASN C 1 88 ? 7.047   -20.702 21.137  1.00 57.21  ? 87  ASN C CG  1 
ATOM   2106 O OD1 . ASN C 1 88 ? 7.214   -19.951 22.107  1.00 59.17  ? 87  ASN C OD1 1 
ATOM   2107 N ND2 . ASN C 1 88 ? 6.005   -21.511 21.032  1.00 52.57  ? 87  ASN C ND2 1 
ATOM   2108 N N   . PRO C 1 89 ? 11.459  -20.502 21.579  1.00 42.98  ? 88  PRO C N   1 
ATOM   2109 C CA  . PRO C 1 89 ? 12.431  -21.443 22.140  1.00 45.18  ? 88  PRO C CA  1 
ATOM   2110 C C   . PRO C 1 89 ? 12.150  -21.887 23.577  1.00 50.56  ? 88  PRO C C   1 
ATOM   2111 O O   . PRO C 1 89 ? 12.690  -22.904 24.028  1.00 43.76  ? 88  PRO C O   1 
ATOM   2112 C CB  . PRO C 1 89 ? 13.763  -20.705 21.988  1.00 45.37  ? 88  PRO C CB  1 
ATOM   2113 C CG  . PRO C 1 89 ? 13.373  -19.241 22.060  1.00 53.30  ? 88  PRO C CG  1 
ATOM   2114 C CD  . PRO C 1 89 ? 12.002  -19.149 21.409  1.00 42.23  ? 88  PRO C CD  1 
ATOM   2115 N N   . HIS C 1 90 ? 11.277  -21.147 24.277  1.00 50.87  ? 89  HIS C N   1 
ATOM   2116 C CA  . HIS C 1 90 ? 11.059  -21.416 25.694  1.00 50.11  ? 89  HIS C CA  1 
ATOM   2117 C C   . HIS C 1 90 ? 9.609   -21.799 25.998  1.00 55.66  ? 89  HIS C C   1 
ATOM   2118 O O   . HIS C 1 90 ? 9.189   -21.741 27.146  1.00 62.52  ? 89  HIS C O   1 
ATOM   2119 C CB  . HIS C 1 90 ? 11.611  -20.283 26.559  1.00 39.86  ? 89  HIS C CB  1 
ATOM   2120 C CG  . HIS C 1 90 ? 13.042  -19.948 26.301  1.00 38.85  ? 89  HIS C CG  1 
ATOM   2121 N ND1 . HIS C 1 90 ? 13.425  -18.747 25.741  1.00 42.31  ? 89  HIS C ND1 1 
ATOM   2122 C CD2 . HIS C 1 90 ? 14.186  -20.617 26.555  1.00 37.63  ? 89  HIS C CD2 1 
ATOM   2123 C CE1 . HIS C 1 90 ? 14.757  -18.695 25.634  1.00 39.22  ? 89  HIS C CE1 1 
ATOM   2124 N NE2 . HIS C 1 90 ? 15.244  -19.827 26.135  1.00 43.34  ? 89  HIS C NE2 1 
ATOM   2125 N N   . ALA C 1 91 ? 8.848   -22.223 24.985  1.00 57.75  ? 90  ALA C N   1 
ATOM   2126 C CA  . ALA C 1 91 ? 7.525   -22.785 25.226  1.00 62.56  ? 90  ALA C CA  1 
ATOM   2127 C C   . ALA C 1 91 ? 7.621   -24.214 25.776  1.00 70.45  ? 90  ALA C C   1 
ATOM   2128 O O   . ALA C 1 91 ? 8.705   -24.792 25.858  1.00 66.06  ? 90  ALA C O   1 
ATOM   2129 C CB  . ALA C 1 91 ? 6.684   -22.720 23.967  1.00 59.06  ? 90  ALA C CB  1 
ATOM   2130 N N   . SER C 1 92 ? 6.454   -24.787 26.107  1.00 75.64  ? 91  SER C N   1 
ATOM   2131 C CA  . SER C 1 92 ? 6.320   -26.026 26.862  1.00 80.61  ? 91  SER C CA  1 
ATOM   2132 C C   . SER C 1 92 ? 6.689   -27.255 26.034  1.00 77.21  ? 91  SER C C   1 
ATOM   2133 O O   . SER C 1 92 ? 7.685   -27.909 26.324  1.00 81.55  ? 91  SER C O   1 
ATOM   2134 C CB  . SER C 1 92 ? 4.928   -26.170 27.431  1.00 80.95  ? 91  SER C CB  1 
ATOM   2135 O OG  . SER C 1 92 ? 4.749   -25.283 28.522  1.00 85.48  ? 91  SER C OG  1 
ATOM   2136 N N   . TYR C 1 93 ? 5.841   -27.583 25.049  1.00 77.34  ? 92  TYR C N   1 
ATOM   2137 C CA  . TYR C 1 93 ? 5.971   -28.779 24.227  1.00 80.80  ? 92  TYR C CA  1 
ATOM   2138 C C   . TYR C 1 93 ? 5.902   -30.027 25.122  1.00 87.79  ? 92  TYR C C   1 
ATOM   2139 O O   . TYR C 1 93 ? 4.786   -30.520 25.413  1.00 88.21  ? 92  TYR C O   1 
ATOM   2140 C CB  . TYR C 1 93 ? 7.267   -28.774 23.406  1.00 79.75  ? 92  TYR C CB  1 
ATOM   2141 C CG  . TYR C 1 93 ? 7.596   -27.483 22.661  1.00 70.88  ? 92  TYR C CG  1 
ATOM   2142 C CD1 . TYR C 1 93 ? 6.902   -27.118 21.509  1.00 62.37  ? 92  TYR C CD1 1 
ATOM   2143 C CD2 . TYR C 1 93 ? 8.617   -26.644 23.099  1.00 66.72  ? 92  TYR C CD2 1 
ATOM   2144 C CE1 . TYR C 1 93 ? 7.202   -25.953 20.822  1.00 63.20  ? 92  TYR C CE1 1 
ATOM   2145 C CE2 . TYR C 1 93 ? 8.926   -25.477 22.419  1.00 68.84  ? 92  TYR C CE2 1 
ATOM   2146 C CZ  . TYR C 1 93 ? 8.222   -25.133 21.275  1.00 64.25  ? 92  TYR C CZ  1 
ATOM   2147 O OH  . TYR C 1 93 ? 8.522   -23.972 20.611  1.00 63.41  ? 92  TYR C OH  1 
HETATM 2148 S S   . SO4 D 2 .  ? 1.048   -33.760 1.747   1.00 117.86 ? 101 SO4 A S   1 
HETATM 2149 O O1  . SO4 D 2 .  ? 1.623   -34.517 0.665   1.00 100.88 ? 101 SO4 A O1  1 
HETATM 2150 O O2  . SO4 D 2 .  ? 0.908   -32.382 1.353   1.00 113.30 ? 101 SO4 A O2  1 
HETATM 2151 O O3  . SO4 D 2 .  ? -0.247  -34.303 2.070   1.00 121.75 ? 101 SO4 A O3  1 
HETATM 2152 O O4  . SO4 D 2 .  ? 1.907   -33.841 2.897   1.00 109.60 ? 101 SO4 A O4  1 
HETATM 2153 S S   . SO4 E 2 .  ? -9.394  -24.732 1.170   1.00 105.62 ? 102 SO4 A S   1 
HETATM 2154 O O1  . SO4 E 2 .  ? -8.866  -24.437 -0.134  1.00 98.97  ? 102 SO4 A O1  1 
HETATM 2155 O O2  . SO4 E 2 .  ? -9.269  -23.573 2.014   1.00 98.23  ? 102 SO4 A O2  1 
HETATM 2156 O O3  . SO4 E 2 .  ? -10.782 -25.103 1.042   1.00 111.47 ? 102 SO4 A O3  1 
HETATM 2157 O O4  . SO4 E 2 .  ? -8.659  -25.824 1.757   1.00 102.46 ? 102 SO4 A O4  1 
HETATM 2158 C C1  . EDO F 3 .  ? 14.044  -19.497 -7.357  1.00 43.10  ? 103 EDO A C1  1 
HETATM 2159 O O1  . EDO F 3 .  ? 15.240  -18.740 -7.291  1.00 35.46  ? 103 EDO A O1  1 
HETATM 2160 C C2  . EDO F 3 .  ? 13.146  -19.078 -8.470  1.00 42.22  ? 103 EDO A C2  1 
HETATM 2161 O O2  . EDO F 3 .  ? 12.756  -17.737 -8.366  1.00 38.02  ? 103 EDO A O2  1 
HETATM 2162 S S   . SO4 G 2 .  ? 9.154   -29.340 5.840   1.00 67.40  ? 104 SO4 A S   1 
HETATM 2163 O O1  . SO4 G 2 .  ? 10.137  -28.672 5.054   1.00 59.22  ? 104 SO4 A O1  1 
HETATM 2164 O O2  . SO4 G 2 .  ? 8.645   -30.492 5.124   1.00 72.33  ? 104 SO4 A O2  1 
HETATM 2165 O O3  . SO4 G 2 .  ? 9.758   -29.771 7.080   1.00 75.91  ? 104 SO4 A O3  1 
HETATM 2166 O O4  . SO4 G 2 .  ? 8.060   -28.443 6.093   1.00 77.62  ? 104 SO4 A O4  1 
HETATM 2167 S S   . SO4 H 2 .  ? 7.617   -8.445  -24.869 1.00 84.17  ? 101 SO4 B S   1 
HETATM 2168 O O1  . SO4 H 2 .  ? 8.783   -8.619  -25.704 1.00 43.99  ? 101 SO4 B O1  1 
HETATM 2169 O O2  . SO4 H 2 .  ? 6.443   -8.966  -25.555 1.00 60.47  ? 101 SO4 B O2  1 
HETATM 2170 O O3  . SO4 H 2 .  ? 7.736   -9.166  -23.584 1.00 45.83  ? 101 SO4 B O3  1 
HETATM 2171 O O4  . SO4 H 2 .  ? 7.517   -7.005  -24.642 1.00 54.36  ? 101 SO4 B O4  1 
HETATM 2172 S S   . SO4 I 2 .  ? 14.674  -27.085 -26.625 1.00 57.83  ? 102 SO4 B S   1 
HETATM 2173 O O1  . SO4 I 2 .  ? 15.876  -26.422 -26.223 1.00 61.30  ? 102 SO4 B O1  1 
HETATM 2174 O O2  . SO4 I 2 .  ? 15.029  -28.296 -27.327 1.00 67.40  ? 102 SO4 B O2  1 
HETATM 2175 O O3  . SO4 I 2 .  ? 13.901  -27.418 -25.462 1.00 68.55  ? 102 SO4 B O3  1 
HETATM 2176 O O4  . SO4 I 2 .  ? 13.894  -26.231 -27.474 1.00 58.06  ? 102 SO4 B O4  1 
HETATM 2177 N N1  . UUY J 4 .  ? 20.012  -16.309 -22.697 0.86 39.49  ? 103 UUY B N1  1 
HETATM 2178 C C4  . UUY J 4 .  ? 20.390  -15.349 -24.890 0.86 33.15  ? 103 UUY B C4  1 
HETATM 2179 C C5  . UUY J 4 .  ? 21.683  -15.010 -24.512 0.86 36.04  ? 103 UUY B C5  1 
HETATM 2180 C C6  . UUY J 4 .  ? 22.136  -15.309 -23.246 0.86 35.43  ? 103 UUY B C6  1 
HETATM 2181 C C7  . UUY J 4 .  ? 21.267  -15.949 -22.371 0.86 32.70  ? 103 UUY B C7  1 
HETATM 2182 N N   . UUY J 4 .  ? 18.222  -16.394 -24.236 0.86 30.86  ? 103 UUY B N   1 
HETATM 2183 C C   . UUY J 4 .  ? 17.301  -16.538 -23.118 0.86 34.74  ? 103 UUY B C   1 
HETATM 2184 O O   . UUY J 4 .  ? 17.779  -13.658 -25.121 0.86 30.51  ? 103 UUY B O   1 
HETATM 2185 C C1  . UUY J 4 .  ? 17.570  -16.043 -25.487 0.86 29.89  ? 103 UUY B C1  1 
HETATM 2186 C C2  . UUY J 4 .  ? 16.854  -14.701 -25.404 0.86 31.43  ? 103 UUY B C2  1 
HETATM 2187 C C3  . UUY J 4 .  ? 19.587  -16.004 -23.941 0.86 38.37  ? 103 UUY B C3  1 
HETATM 2188 C C1  . EDO K 3 .  ? 16.928  -36.368 16.517  1.00 41.39  ? 101 EDO C C1  1 
HETATM 2189 O O1  . EDO K 3 .  ? 15.844  -36.982 15.857  1.00 49.29  ? 101 EDO C O1  1 
HETATM 2190 C C2  . EDO K 3 .  ? 16.470  -35.279 17.407  1.00 34.75  ? 101 EDO C C2  1 
HETATM 2191 O O2  . EDO K 3 .  ? 15.516  -35.731 18.332  1.00 28.34  ? 101 EDO C O2  1 
HETATM 2192 S S   . SO4 L 2 .  ? 29.432  -38.349 12.302  1.00 106.18 ? 102 SO4 C S   1 
HETATM 2193 O O1  . SO4 L 2 .  ? 30.528  -37.668 11.661  1.00 103.41 ? 102 SO4 C O1  1 
HETATM 2194 O O2  . SO4 L 2 .  ? 28.240  -37.554 12.183  1.00 98.46  ? 102 SO4 C O2  1 
HETATM 2195 O O3  . SO4 L 2 .  ? 29.219  -39.624 11.673  1.00 96.14  ? 102 SO4 C O3  1 
HETATM 2196 O O4  . SO4 L 2 .  ? 29.741  -38.548 13.693  1.00 107.02 ? 102 SO4 C O4  1 
HETATM 2197 O O   . HOH M 5 .  ? 8.704   -32.400 4.261   1.00 56.28  ? 201 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? -5.848  -13.383 -16.537 1.00 43.27  ? 202 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? 4.375   -10.624 13.829  1.00 60.33  ? 203 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? 5.875   -29.079 7.076   1.00 56.57  ? 204 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? 11.165  -29.613 2.936   1.00 45.60  ? 205 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? 1.389   2.600   4.024   1.00 66.43  ? 206 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? -3.672  -10.701 6.649   1.00 40.38  ? 207 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? -2.265  -30.844 -3.699  1.00 50.15  ? 208 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? -7.447  -21.195 -4.228  1.00 74.75  ? 209 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? 1.971   -2.017  -0.850  1.00 63.53  ? 210 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 7.226   -10.615 -12.039 1.00 35.18  ? 211 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? -2.439  -11.822 13.776  1.00 48.98  ? 212 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 14.176  -15.769 -9.243  1.00 33.72  ? 213 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? 4.672   -7.933  1.194   1.00 38.18  ? 214 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? 9.214   -18.212 -11.014 1.00 33.73  ? 215 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 0.610   -10.588 -15.563 1.00 42.81  ? 216 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 4.479   -3.620  -3.221  1.00 33.95  ? 217 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? -2.294  3.151   -2.033  1.00 42.49  ? 218 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? -8.297  -21.295 -1.151  1.00 42.92  ? 219 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? -4.220  -21.236 6.092   1.00 41.25  ? 220 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 13.420  -28.012 -4.645  1.00 56.32  ? 221 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 13.167  -11.884 8.171   1.00 66.16  ? 222 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 8.266   -17.894 -16.058 1.00 54.54  ? 223 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? -0.025  -33.758 4.710   1.00 56.94  ? 224 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? 4.030   -34.874 4.110   1.00 62.81  ? 225 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 13.010  -9.495  -7.187  1.00 42.44  ? 226 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? 2.659   -9.860  -13.186 1.00 57.75  ? 227 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 10.955  -9.440  -13.183 1.00 58.20  ? 228 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 16.109  -24.529 1.867   1.00 44.96  ? 229 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? 2.535   -25.082 -9.955  1.00 40.47  ? 230 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? -6.382  -25.659 -5.737  1.00 63.51  ? 231 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 3.374   -29.649 -0.435  1.00 39.35  ? 232 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? -7.959  -15.793 -1.053  1.00 35.45  ? 233 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? 4.757   5.824   -4.671  1.00 65.63  ? 234 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? 11.263  -23.728 9.881   1.00 38.65  ? 235 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? -0.475  -20.917 7.042   1.00 36.18  ? 236 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 11.886  -16.488 -14.871 1.00 46.58  ? 237 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 20.003  -15.510 7.299   1.00 34.18  ? 238 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? -0.603  -29.389 10.050  1.00 56.25  ? 239 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 9.720   -6.015  -1.541  1.00 37.19  ? 240 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? -5.626  -15.884 -7.926  1.00 28.26  ? 241 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 9.611   -22.802 -9.357  1.00 41.57  ? 242 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 1.314   -18.026 -18.802 1.00 50.41  ? 243 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 1.728   0.558   -7.436  1.00 50.75  ? 244 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? -7.621  -17.220 6.881   1.00 48.54  ? 245 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 12.518  -15.740 -12.110 1.00 52.99  ? 246 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 11.552  -12.293 -6.223  1.00 27.00  ? 247 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? 18.684  -11.177 -18.741 1.00 48.91  ? 248 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 11.685  -11.956 5.855   1.00 39.18  ? 249 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 2.259   -25.051 -6.530  1.00 57.88  ? 250 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 10.867  -5.176  -7.803  1.00 34.87  ? 251 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? -5.672  -19.662 -5.663  1.00 39.66  ? 252 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 10.132  -13.044 9.715   1.00 43.48  ? 253 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -6.110  -11.471 -11.438 1.00 42.90  ? 254 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 0.306   -23.164 9.515   1.00 48.47  ? 255 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? 17.290  -12.882 1.420   1.00 22.02  ? 256 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -1.639  -22.054 -0.554  1.00 31.60  ? 257 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? 1.803   -4.695  -10.421 1.00 39.98  ? 258 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 16.527  -11.716 -17.117 1.00 45.73  ? 259 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? -6.924  -13.545 -11.680 1.00 56.78  ? 260 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? -1.388  -7.692  11.563  1.00 57.87  ? 261 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? 13.383  -11.993 -4.214  1.00 22.90  ? 262 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? 8.085   -7.873  1.179   1.00 36.57  ? 263 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? 8.341   -17.389 8.655   1.00 50.25  ? 264 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 1.813   -10.562 11.762  1.00 37.17  ? 265 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -7.881  -16.719 1.887   1.00 44.64  ? 266 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 9.491   -20.222 -18.476 1.00 48.13  ? 267 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? 15.860  -12.034 -5.425  1.00 36.30  ? 268 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 11.200  -6.200  -3.693  1.00 54.13  ? 269 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 12.849  -13.560 -8.398  1.00 43.82  ? 270 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 8.891   -16.312 -13.208 1.00 38.94  ? 271 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? -4.204  -25.792 -5.621  1.00 48.83  ? 272 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? 5.381   -7.642  4.093   1.00 33.24  ? 273 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 14.631  -29.443 3.987   1.00 40.04  ? 274 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? 16.790  -17.898 -9.719  1.00 50.61  ? 275 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 8.648   -1.936  -0.441  1.00 77.35  ? 276 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 21.433  -16.662 -3.588  1.00 33.90  ? 277 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? -6.034  -12.696 6.714   1.00 36.45  ? 278 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 22.480  -16.662 -0.392  1.00 43.28  ? 279 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? -3.860  -26.321 7.595   1.00 56.14  ? 280 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -1.452  -11.902 11.319  1.00 35.04  ? 281 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? 10.137  -27.709 -7.310  1.00 58.82  ? 282 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 6.522   -5.901  0.520   1.00 45.21  ? 283 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? 11.115  -7.855  0.393   1.00 28.56  ? 284 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? -8.199  -19.410 -3.271  1.00 47.10  ? 285 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 6.563   -15.925 -14.926 1.00 51.53  ? 286 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -0.279  -20.609 11.241  1.00 57.26  ? 287 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? -10.923 -16.140 -3.443  1.00 57.49  ? 288 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? 2.132   -24.901 14.820  1.00 59.65  ? 289 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -7.231  -11.509 -8.019  1.00 31.65  ? 290 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 16.686  -29.229 2.244   1.00 65.18  ? 291 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? -5.906  -26.748 3.368   1.00 53.47  ? 292 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? -5.594  -23.538 -6.822  1.00 44.63  ? 293 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? -10.568 -27.578 -1.399  1.00 74.54  ? 294 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -3.744  -7.857  10.641  1.00 46.21  ? 295 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 8.797   -9.096  -13.786 1.00 36.75  ? 296 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -3.689  -11.006 10.031  1.00 57.97  ? 297 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 0.967   -29.202 -7.190  1.00 62.07  ? 298 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? -7.162  -14.028 -9.090  1.00 45.14  ? 299 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? 11.770  -21.231 10.662  1.00 45.88  ? 300 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? 15.319  -28.369 -1.782  1.00 62.32  ? 301 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -0.501  -3.290  -11.046 1.00 59.59  ? 302 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 8.167   -8.181  4.585   1.00 37.70  ? 303 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? 3.213   -5.212  -11.927 1.00 45.28  ? 304 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? -9.314  -19.129 1.651   1.00 44.35  ? 305 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? 7.227   -30.786 -2.491  1.00 56.13  ? 306 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? -6.889  -19.257 8.225   1.00 52.55  ? 307 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? -6.008  -22.867 6.188   1.00 54.60  ? 308 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? -11.181 -13.646 -2.874  1.00 41.22  ? 309 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? 4.742   -9.797  -11.372 1.00 42.75  ? 310 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? 8.844   -22.428 -19.200 1.00 59.83  ? 311 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? -5.151  -21.001 -8.225  1.00 54.25  ? 312 HOH A O   1 
HETATM 2309 O O   . HOH M 5 .  ? 4.396   -3.423  1.663   1.00 56.06  ? 313 HOH A O   1 
HETATM 2310 O O   . HOH N 5 .  ? 10.302  -19.690 -43.222 1.00 53.67  ? 201 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 25.945  -4.668  -33.700 1.00 45.58  ? 202 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 10.019  -11.363 -38.252 1.00 53.27  ? 203 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 6.809   -12.314 -26.146 1.00 38.06  ? 204 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 30.801  -8.293  -29.903 1.00 57.72  ? 205 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 19.986  -21.974 -23.260 1.00 50.17  ? 206 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 7.470   -12.544 -38.610 1.00 47.38  ? 207 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 30.236  -12.744 -45.959 1.00 63.65  ? 208 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 25.232  -5.087  -29.957 1.00 39.02  ? 209 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 30.381  -19.759 -40.401 1.00 36.13  ? 210 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 24.375  -1.833  -36.505 1.00 55.38  ? 211 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 19.179  -16.780 -20.255 1.00 48.12  ? 212 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 21.278  -26.038 -30.135 1.00 60.59  ? 213 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 27.802  -8.293  -28.804 1.00 45.22  ? 214 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 26.270  -23.122 -31.301 1.00 39.09  ? 215 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 17.694  -14.658 -19.516 1.00 41.01  ? 216 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 32.126  -11.927 -42.049 1.00 41.03  ? 217 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 20.908  -13.393 -42.792 1.00 40.55  ? 218 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 23.582  -2.195  -29.231 1.00 41.02  ? 219 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 7.571   -18.121 -31.931 1.00 49.33  ? 220 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 34.697  -23.241 -30.119 1.00 54.95  ? 221 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 25.452  -5.973  -36.040 1.00 45.21  ? 222 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 10.673  -18.829 -33.081 1.00 26.62  ? 223 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 28.071  -17.582 -25.128 1.00 42.74  ? 224 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 6.123   -7.464  -32.252 1.00 56.25  ? 225 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 4.536   -18.900 -25.729 1.00 46.35  ? 226 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 18.088  -0.508  -38.538 1.00 31.90  ? 227 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 32.543  -18.810 -42.463 1.00 49.18  ? 228 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 8.352   -27.913 -38.370 1.00 55.95  ? 229 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 20.011  -25.597 -34.142 1.00 43.43  ? 230 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 12.825  -4.615  -42.091 1.00 45.00  ? 231 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 31.681  -12.282 -39.019 1.00 59.83  ? 232 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 21.420  3.634   -32.821 1.00 37.35  ? 233 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 22.201  -3.729  -24.488 1.00 61.14  ? 234 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 16.787  -19.291 -28.864 1.00 25.47  ? 235 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 10.551  -17.089 -44.267 1.00 46.67  ? 236 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 17.673  -19.815 -42.062 1.00 50.86  ? 237 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 3.347   -8.748  -27.072 1.00 50.71  ? 238 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 7.698   -8.101  -20.941 1.00 54.76  ? 239 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 14.679  -24.494 -40.380 1.00 49.48  ? 240 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 22.862  -23.085 -28.849 1.00 41.03  ? 241 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 12.708  -4.676  -25.031 1.00 52.31  ? 242 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 7.280   -19.065 -34.992 1.00 49.37  ? 243 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 10.734  -21.855 -33.009 1.00 42.07  ? 244 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 8.816   -8.649  -16.501 1.00 39.06  ? 245 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 27.323  -10.552 -29.034 1.00 48.78  ? 246 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 31.943  -21.158 -38.192 1.00 38.68  ? 247 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 20.405  -10.160 -43.054 1.00 39.93  ? 248 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 18.235  -3.621  -22.286 1.00 53.42  ? 249 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 13.110  -22.419 -20.766 1.00 56.00  ? 250 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 14.363  -6.399  -41.323 1.00 47.59  ? 251 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 6.704   -20.696 -24.948 1.00 49.18  ? 252 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 23.896  -4.237  -36.902 1.00 34.63  ? 253 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 21.163  -6.430  -42.751 1.00 43.19  ? 254 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 1.735   -13.012 -28.437 1.00 50.66  ? 255 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 17.144  -9.576  -43.847 1.00 51.99  ? 256 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 18.172  4.584   -34.412 1.00 40.04  ? 257 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 27.959  -24.875 -35.142 1.00 34.06  ? 258 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 23.579  -11.491 -21.894 1.00 36.62  ? 259 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 18.250  -15.979 -45.921 1.00 44.50  ? 260 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 18.028  -0.226  -25.582 1.00 62.19  ? 261 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 7.879   -23.656 -24.549 1.00 57.85  ? 262 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 20.166  -7.792  -21.244 1.00 51.73  ? 263 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 18.675  -25.880 -28.789 1.00 42.31  ? 264 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 24.800  -6.608  -42.783 1.00 54.27  ? 265 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 26.116  -0.420  -29.554 1.00 47.23  ? 266 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 12.992  -20.455 -19.531 1.00 57.98  ? 267 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 9.772   -6.150  -41.000 1.00 46.83  ? 268 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 20.012  3.911   -33.304 1.00 44.11  ? 269 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 15.213  -8.016  -43.187 1.00 47.46  ? 270 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 39.890  -13.943 -39.545 1.00 76.82  ? 271 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 15.455  -21.767 -41.897 1.00 56.31  ? 272 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 17.203  -25.765 -21.079 1.00 69.18  ? 273 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 11.750  -24.151 -30.116 1.00 54.86  ? 274 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 7.769   -13.746 -44.549 1.00 68.05  ? 275 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 13.858  -6.178  -18.173 1.00 62.60  ? 276 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 24.737  -4.299  -28.014 1.00 58.74  ? 277 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 7.495   -9.881  -18.483 1.00 44.30  ? 278 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 22.438  -29.342 -35.635 1.00 49.48  ? 279 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 12.853  -24.934 -19.624 1.00 64.08  ? 280 HOH B O   1 
HETATM 2390 O O   . HOH O 5 .  ? 15.753  -27.080 28.533  1.00 51.86  ? 201 HOH C O   1 
HETATM 2391 O O   . HOH O 5 .  ? 20.030  -19.943 29.925  1.00 62.92  ? 202 HOH C O   1 
HETATM 2392 O O   . HOH O 5 .  ? 26.723  -39.251 12.704  1.00 40.55  ? 203 HOH C O   1 
HETATM 2393 O O   . HOH O 5 .  ? 31.935  -33.114 25.838  1.00 46.34  ? 204 HOH C O   1 
HETATM 2394 O O   . HOH O 5 .  ? 27.021  -37.853 10.195  1.00 42.70  ? 205 HOH C O   1 
HETATM 2395 O O   . HOH O 5 .  ? 19.423  -20.322 10.570  1.00 42.99  ? 206 HOH C O   1 
HETATM 2396 O O   . HOH O 5 .  ? 2.459   -31.073 26.073  1.00 63.75  ? 207 HOH C O   1 
HETATM 2397 O O   . HOH O 5 .  ? 12.202  -28.546 28.163  1.00 58.61  ? 208 HOH C O   1 
HETATM 2398 O O   . HOH O 5 .  ? 33.483  -24.282 31.433  1.00 50.19  ? 209 HOH C O   1 
HETATM 2399 O O   . HOH O 5 .  ? 7.861   -31.605 12.426  1.00 52.07  ? 210 HOH C O   1 
HETATM 2400 O O   . HOH O 5 .  ? 15.548  -17.734 19.397  1.00 46.16  ? 211 HOH C O   1 
HETATM 2401 O O   . HOH O 5 .  ? 15.316  -21.176 12.423  1.00 44.75  ? 212 HOH C O   1 
HETATM 2402 O O   . HOH O 5 .  ? 19.111  -27.026 3.201   1.00 52.10  ? 213 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 17.703  -17.154 14.907  1.00 44.97  ? 214 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 23.005  -41.611 18.450  1.00 44.30  ? 215 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 5.870   -26.507 17.127  1.00 52.95  ? 216 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 9.229   -37.010 18.234  1.00 62.89  ? 217 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 15.787  -39.281 17.126  1.00 66.71  ? 218 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 25.746  -19.616 6.415   1.00 38.87  ? 219 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 25.570  -33.762 34.802  1.00 50.50  ? 220 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 20.125  -41.941 12.150  1.00 32.10  ? 221 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 28.106  -37.444 15.943  1.00 44.94  ? 222 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 7.165   -18.122 10.836  1.00 38.26  ? 223 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 30.700  -29.104 12.210  1.00 55.59  ? 224 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 12.876  -31.566 8.215   1.00 38.09  ? 225 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 14.212  -37.189 13.630  1.00 44.41  ? 226 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 25.992  -17.638 13.874  1.00 52.91  ? 227 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 25.832  -20.281 30.167  1.00 74.11  ? 228 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 28.370  -15.103 12.992  1.00 54.03  ? 229 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 29.910  -39.815 31.469  1.00 39.01  ? 230 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 22.361  -28.645 11.126  1.00 34.44  ? 231 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 20.940  -28.711 8.401   1.00 39.60  ? 232 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 22.196  -34.482 16.615  1.00 29.57  ? 233 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 20.812  -39.918 26.477  1.00 41.44  ? 234 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 25.417  -31.482 10.711  1.00 34.67  ? 235 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 16.572  -33.750 28.664  1.00 53.11  ? 236 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 20.759  -19.279 24.746  1.00 60.63  ? 237 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 25.618  -39.736 20.169  1.00 37.24  ? 238 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 16.583  -37.355 20.439  1.00 56.40  ? 239 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 9.341   -18.960 23.766  1.00 56.43  ? 240 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 9.897   -30.364 10.067  1.00 38.26  ? 241 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 27.765  -37.393 25.121  1.00 49.90  ? 242 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 30.483  -32.046 15.721  1.00 72.17  ? 243 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 31.510  -39.902 27.237  1.00 52.26  ? 244 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 21.907  -18.303 21.942  1.00 55.91  ? 245 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 31.443  -43.489 15.827  1.00 51.37  ? 246 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 17.826  -21.196 12.855  1.00 53.22  ? 247 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 24.538  -18.293 21.517  1.00 56.22  ? 248 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 14.387  -38.867 9.745   1.00 60.47  ? 249 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 32.021  -43.352 11.919  1.00 45.66  ? 250 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 30.599  -35.708 28.627  1.00 48.05  ? 251 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 20.258  -41.353 39.394  1.00 62.54  ? 252 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 21.267  -29.618 4.645   1.00 56.84  ? 253 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 2.880   -28.758 13.913  1.00 66.58  ? 254 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 30.605  -17.390 9.681   1.00 48.16  ? 255 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 30.353  -32.879 18.167  1.00 48.96  ? 256 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 29.912  -25.308 32.589  1.00 57.83  ? 257 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 17.505  -36.433 29.248  1.00 68.33  ? 258 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 20.578  -12.967 13.377  1.00 48.67  ? 259 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 15.818  -13.361 10.746  1.00 58.39  ? 260 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 29.231  -41.683 27.195  1.00 50.17  ? 261 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 22.686  -40.195 39.697  1.00 72.68  ? 262 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 25.891  -13.974 11.057  1.00 41.75  ? 263 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 22.375  -13.839 13.275  1.00 56.75  ? 264 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 13.716  -22.984 27.893  1.00 82.59  ? 265 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 36.997  -23.729 27.464  1.00 83.21  ? 266 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 5.316   -24.279 18.462  1.00 54.76  ? 267 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 28.518  -17.840 28.693  1.00 61.64  ? 268 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 28.653  -41.625 29.951  1.00 50.11  ? 269 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 33.729  -44.550 15.301  1.00 37.68  ? 270 HOH C O   1 
# 
