data_7HHK
# 
_entry.id   7HHK 
# 
_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   7HHK         pdb_00007hhk 10.2210/pdb7hhk/pdb 
WWPDB D_1001407482 ?            ?                   
# 
_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                        7HHK 
_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    1   ? ?    ? ? 
4 non-polymer syn '1-(methanesulfonyl)piperidin-4-ol'                179.237   3   ? ?    ? ? 
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 '1-(methanesulfonyl)piperidin-4-ol' LPU 
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 
LPU non-polymer         . '1-(methanesulfonyl)piperidin-4-ol' ?                 'C6 H13 N O3 S'  179.237 
LYS 'L-peptide linking' y LYSINE                              ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                          ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                       ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                             ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                              ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                       ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                           ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                          ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                            ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                              ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        LPU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LPU 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4 1   101 95  SO4 SO4 A . 
E 2 SO4 1   102 96  SO4 SO4 A . 
F 3 EDO 1   103 97  EDO EDO A . 
G 4 LPU 1   104 101 LPU LIG A . 
H 2 SO4 1   105 4   SO4 SO4 A . 
I 2 SO4 1   101 1   SO4 SO4 B . 
J 2 SO4 1   102 3   SO4 SO4 B . 
K 4 LPU 1   103 101 LPU LIG B . 
L 2 SO4 1   101 5   SO4 SO4 C . 
M 4 LPU 1   102 101 LPU LIG C . 
N 5 HOH 1   201 84  HOH HOH A . 
N 5 HOH 2   202 307 HOH HOH A . 
N 5 HOH 3   203 333 HOH HOH A . 
N 5 HOH 4   204 334 HOH HOH A . 
N 5 HOH 5   205 259 HOH HOH A . 
N 5 HOH 6   206 66  HOH HOH A . 
N 5 HOH 7   207 202 HOH HOH A . 
N 5 HOH 8   208 335 HOH HOH A . 
N 5 HOH 9   209 208 HOH HOH A . 
N 5 HOH 10  210 94  HOH HOH A . 
N 5 HOH 11  211 289 HOH HOH A . 
N 5 HOH 12  212 167 HOH HOH A . 
N 5 HOH 13  213 23  HOH HOH A . 
N 5 HOH 14  214 87  HOH HOH A . 
N 5 HOH 15  215 139 HOH HOH A . 
N 5 HOH 16  216 32  HOH HOH A . 
N 5 HOH 17  217 93  HOH HOH A . 
N 5 HOH 18  218 85  HOH HOH A . 
N 5 HOH 19  219 292 HOH HOH A . 
N 5 HOH 20  220 86  HOH HOH A . 
N 5 HOH 21  221 97  HOH HOH A . 
N 5 HOH 22  222 26  HOH HOH A . 
N 5 HOH 23  223 304 HOH HOH A . 
N 5 HOH 24  224 260 HOH HOH A . 
N 5 HOH 25  225 8   HOH HOH A . 
N 5 HOH 26  226 27  HOH HOH A . 
N 5 HOH 27  227 151 HOH HOH A . 
N 5 HOH 28  228 91  HOH HOH A . 
N 5 HOH 29  229 38  HOH HOH A . 
N 5 HOH 30  230 199 HOH HOH A . 
N 5 HOH 31  231 7   HOH HOH A . 
N 5 HOH 32  232 299 HOH HOH A . 
N 5 HOH 33  233 188 HOH HOH A . 
N 5 HOH 34  234 35  HOH HOH A . 
N 5 HOH 35  235 12  HOH HOH A . 
N 5 HOH 36  236 42  HOH HOH A . 
N 5 HOH 37  237 78  HOH HOH A . 
N 5 HOH 38  238 350 HOH HOH A . 
N 5 HOH 39  239 41  HOH HOH A . 
N 5 HOH 40  240 28  HOH HOH A . 
N 5 HOH 41  241 143 HOH HOH A . 
N 5 HOH 42  242 190 HOH HOH A . 
N 5 HOH 43  243 1   HOH HOH A . 
N 5 HOH 44  244 2   HOH HOH A . 
N 5 HOH 45  245 340 HOH HOH A . 
N 5 HOH 46  246 60  HOH HOH A . 
N 5 HOH 47  247 18  HOH HOH A . 
N 5 HOH 48  248 267 HOH HOH A . 
N 5 HOH 49  249 293 HOH HOH A . 
N 5 HOH 50  250 290 HOH HOH A . 
N 5 HOH 51  251 55  HOH HOH A . 
N 5 HOH 52  252 111 HOH HOH A . 
N 5 HOH 53  253 352 HOH HOH A . 
N 5 HOH 54  254 287 HOH HOH A . 
N 5 HOH 55  255 300 HOH HOH A . 
N 5 HOH 56  256 37  HOH HOH A . 
N 5 HOH 57  257 274 HOH HOH A . 
N 5 HOH 58  258 58  HOH HOH A . 
N 5 HOH 59  259 34  HOH HOH A . 
N 5 HOH 60  260 71  HOH HOH A . 
N 5 HOH 61  261 145 HOH HOH A . 
N 5 HOH 62  262 109 HOH HOH A . 
N 5 HOH 63  263 222 HOH HOH A . 
N 5 HOH 64  264 99  HOH HOH A . 
N 5 HOH 65  265 297 HOH HOH A . 
N 5 HOH 66  266 203 HOH HOH A . 
N 5 HOH 67  267 116 HOH HOH A . 
N 5 HOH 68  268 218 HOH HOH A . 
N 5 HOH 69  269 20  HOH HOH A . 
N 5 HOH 70  270 9   HOH HOH A . 
N 5 HOH 71  271 77  HOH HOH A . 
N 5 HOH 72  272 164 HOH HOH A . 
N 5 HOH 73  273 301 HOH HOH A . 
N 5 HOH 74  274 47  HOH HOH A . 
N 5 HOH 75  275 288 HOH HOH A . 
N 5 HOH 76  276 14  HOH HOH A . 
N 5 HOH 77  277 115 HOH HOH A . 
N 5 HOH 78  278 179 HOH HOH A . 
N 5 HOH 79  279 21  HOH HOH A . 
N 5 HOH 80  280 365 HOH HOH A . 
N 5 HOH 81  281 357 HOH HOH A . 
N 5 HOH 82  282 364 HOH HOH A . 
N 5 HOH 83  283 281 HOH HOH A . 
N 5 HOH 84  284 73  HOH HOH A . 
N 5 HOH 85  285 95  HOH HOH A . 
N 5 HOH 86  286 16  HOH HOH A . 
N 5 HOH 87  287 19  HOH HOH A . 
N 5 HOH 88  288 165 HOH HOH A . 
N 5 HOH 89  289 338 HOH HOH A . 
N 5 HOH 90  290 296 HOH HOH A . 
N 5 HOH 91  291 318 HOH HOH A . 
N 5 HOH 92  292 83  HOH HOH A . 
N 5 HOH 93  293 131 HOH HOH A . 
N 5 HOH 94  294 348 HOH HOH A . 
N 5 HOH 95  295 211 HOH HOH A . 
N 5 HOH 96  296 31  HOH HOH A . 
N 5 HOH 97  297 152 HOH HOH A . 
N 5 HOH 98  298 210 HOH HOH A . 
N 5 HOH 99  299 22  HOH HOH A . 
N 5 HOH 100 300 113 HOH HOH A . 
N 5 HOH 101 301 219 HOH HOH A . 
N 5 HOH 102 302 327 HOH HOH A . 
N 5 HOH 103 303 342 HOH HOH A . 
N 5 HOH 104 304 64  HOH HOH A . 
N 5 HOH 105 305 363 HOH HOH A . 
N 5 HOH 106 306 185 HOH HOH A . 
N 5 HOH 107 307 63  HOH HOH A . 
N 5 HOH 108 308 156 HOH HOH A . 
N 5 HOH 109 309 283 HOH HOH A . 
N 5 HOH 110 310 205 HOH HOH A . 
N 5 HOH 111 311 75  HOH HOH A . 
N 5 HOH 112 312 57  HOH HOH A . 
N 5 HOH 113 313 125 HOH HOH A . 
N 5 HOH 114 314 313 HOH HOH A . 
N 5 HOH 115 315 356 HOH HOH A . 
N 5 HOH 116 316 332 HOH HOH A . 
N 5 HOH 117 317 347 HOH HOH A . 
O 5 HOH 1   201 344 HOH HOH B . 
O 5 HOH 2   202 247 HOH HOH B . 
O 5 HOH 3   203 123 HOH HOH B . 
O 5 HOH 4   204 341 HOH HOH B . 
O 5 HOH 5   205 258 HOH HOH B . 
O 5 HOH 6   206 249 HOH HOH B . 
O 5 HOH 7   207 329 HOH HOH B . 
O 5 HOH 8   208 117 HOH HOH B . 
O 5 HOH 9   209 89  HOH HOH B . 
O 5 HOH 10  210 339 HOH HOH B . 
O 5 HOH 11  211 242 HOH HOH B . 
O 5 HOH 12  212 98  HOH HOH B . 
O 5 HOH 13  213 331 HOH HOH B . 
O 5 HOH 14  214 272 HOH HOH B . 
O 5 HOH 15  215 150 HOH HOH B . 
O 5 HOH 16  216 59  HOH HOH B . 
O 5 HOH 17  217 17  HOH HOH B . 
O 5 HOH 18  218 54  HOH HOH B . 
O 5 HOH 19  219 172 HOH HOH B . 
O 5 HOH 20  220 169 HOH HOH B . 
O 5 HOH 21  221 6   HOH HOH B . 
O 5 HOH 22  222 215 HOH HOH B . 
O 5 HOH 23  223 168 HOH HOH B . 
O 5 HOH 24  224 68  HOH HOH B . 
O 5 HOH 25  225 69  HOH HOH B . 
O 5 HOH 26  226 184 HOH HOH B . 
O 5 HOH 27  227 153 HOH HOH B . 
O 5 HOH 28  228 25  HOH HOH B . 
O 5 HOH 29  229 157 HOH HOH B . 
O 5 HOH 30  230 5   HOH HOH B . 
O 5 HOH 31  231 10  HOH HOH B . 
O 5 HOH 32  232 61  HOH HOH B . 
O 5 HOH 33  233 24  HOH HOH B . 
O 5 HOH 34  234 79  HOH HOH B . 
O 5 HOH 35  235 96  HOH HOH B . 
O 5 HOH 36  236 137 HOH HOH B . 
O 5 HOH 37  237 119 HOH HOH B . 
O 5 HOH 38  238 72  HOH HOH B . 
O 5 HOH 39  239 320 HOH HOH B . 
O 5 HOH 40  240 223 HOH HOH B . 
O 5 HOH 41  241 224 HOH HOH B . 
O 5 HOH 42  242 175 HOH HOH B . 
O 5 HOH 43  243 279 HOH HOH B . 
O 5 HOH 44  244 101 HOH HOH B . 
O 5 HOH 45  245 337 HOH HOH B . 
O 5 HOH 46  246 354 HOH HOH B . 
O 5 HOH 47  247 74  HOH HOH B . 
O 5 HOH 48  248 261 HOH HOH B . 
O 5 HOH 49  249 182 HOH HOH B . 
O 5 HOH 50  250 280 HOH HOH B . 
O 5 HOH 51  251 214 HOH HOH B . 
O 5 HOH 52  252 36  HOH HOH B . 
O 5 HOH 53  253 76  HOH HOH B . 
O 5 HOH 54  254 44  HOH HOH B . 
O 5 HOH 55  255 13  HOH HOH B . 
O 5 HOH 56  256 315 HOH HOH B . 
O 5 HOH 57  257 120 HOH HOH B . 
O 5 HOH 58  258 217 HOH HOH B . 
O 5 HOH 59  259 197 HOH HOH B . 
O 5 HOH 60  260 303 HOH HOH B . 
O 5 HOH 61  261 160 HOH HOH B . 
O 5 HOH 62  262 316 HOH HOH B . 
O 5 HOH 63  263 177 HOH HOH B . 
O 5 HOH 64  264 46  HOH HOH B . 
O 5 HOH 65  265 104 HOH HOH B . 
O 5 HOH 66  266 170 HOH HOH B . 
O 5 HOH 67  267 163 HOH HOH B . 
O 5 HOH 68  268 319 HOH HOH B . 
O 5 HOH 69  269 201 HOH HOH B . 
O 5 HOH 70  270 346 HOH HOH B . 
O 5 HOH 71  271 322 HOH HOH B . 
O 5 HOH 72  272 291 HOH HOH B . 
O 5 HOH 73  273 70  HOH HOH B . 
O 5 HOH 74  274 351 HOH HOH B . 
O 5 HOH 75  275 355 HOH HOH B . 
O 5 HOH 76  276 107 HOH HOH B . 
O 5 HOH 77  277 314 HOH HOH B . 
O 5 HOH 78  278 92  HOH HOH B . 
O 5 HOH 79  279 312 HOH HOH B . 
O 5 HOH 80  280 360 HOH HOH B . 
P 5 HOH 1   201 349 HOH HOH C . 
P 5 HOH 2   202 323 HOH HOH C . 
P 5 HOH 3   203 161 HOH HOH C . 
P 5 HOH 4   204 226 HOH HOH C . 
P 5 HOH 5   205 359 HOH HOH C . 
P 5 HOH 6   206 336 HOH HOH C . 
P 5 HOH 7   207 209 HOH HOH C . 
P 5 HOH 8   208 15  HOH HOH C . 
P 5 HOH 9   209 321 HOH HOH C . 
P 5 HOH 10  210 173 HOH HOH C . 
P 5 HOH 11  211 254 HOH HOH C . 
P 5 HOH 12  212 317 HOH HOH C . 
P 5 HOH 13  213 102 HOH HOH C . 
P 5 HOH 14  214 142 HOH HOH C . 
P 5 HOH 15  215 134 HOH HOH C . 
P 5 HOH 16  216 295 HOH HOH C . 
P 5 HOH 17  217 309 HOH HOH C . 
P 5 HOH 18  218 4   HOH HOH C . 
P 5 HOH 19  219 298 HOH HOH C . 
P 5 HOH 20  220 118 HOH HOH C . 
P 5 HOH 21  221 271 HOH HOH C . 
P 5 HOH 22  222 45  HOH HOH C . 
P 5 HOH 23  223 122 HOH HOH C . 
P 5 HOH 24  224 189 HOH HOH C . 
P 5 HOH 25  225 43  HOH HOH C . 
P 5 HOH 26  226 90  HOH HOH C . 
P 5 HOH 27  227 82  HOH HOH C . 
P 5 HOH 28  228 275 HOH HOH C . 
P 5 HOH 29  229 135 HOH HOH C . 
P 5 HOH 30  230 149 HOH HOH C . 
P 5 HOH 31  231 126 HOH HOH C . 
P 5 HOH 32  232 49  HOH HOH C . 
P 5 HOH 33  233 56  HOH HOH C . 
P 5 HOH 34  234 269 HOH HOH C . 
P 5 HOH 35  235 343 HOH HOH C . 
P 5 HOH 36  236 148 HOH HOH C . 
P 5 HOH 37  237 67  HOH HOH C . 
P 5 HOH 38  238 294 HOH HOH C . 
P 5 HOH 39  239 40  HOH HOH C . 
P 5 HOH 40  240 132 HOH HOH C . 
P 5 HOH 41  241 284 HOH HOH C . 
P 5 HOH 42  242 302 HOH HOH C . 
P 5 HOH 43  243 362 HOH HOH C . 
P 5 HOH 44  244 358 HOH HOH C . 
P 5 HOH 45  245 48  HOH HOH C . 
P 5 HOH 46  246 305 HOH HOH C . 
P 5 HOH 47  247 330 HOH HOH C . 
P 5 HOH 48  248 62  HOH HOH C . 
P 5 HOH 49  249 65  HOH HOH C . 
P 5 HOH 50  250 171 HOH HOH C . 
P 5 HOH 51  251 130 HOH HOH C . 
P 5 HOH 52  252 53  HOH HOH C . 
P 5 HOH 53  253 146 HOH HOH C . 
P 5 HOH 54  254 246 HOH HOH C . 
P 5 HOH 55  255 198 HOH HOH C . 
P 5 HOH 56  256 328 HOH HOH C . 
P 5 HOH 57  257 241 HOH HOH C . 
P 5 HOH 58  258 270 HOH HOH C . 
P 5 HOH 59  259 108 HOH HOH C . 
P 5 HOH 60  260 324 HOH HOH C . 
P 5 HOH 61  261 353 HOH HOH C . 
P 5 HOH 62  262 103 HOH HOH C . 
P 5 HOH 63  263 361 HOH HOH C . 
P 5 HOH 64  264 345 HOH HOH C . 
P 5 HOH 65  265 206 HOH HOH C . 
P 5 HOH 66  266 310 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 TYR 18 ? CD1 ? A TYR 19 CD1 
2  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
3  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
4  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
5  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
6  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
7  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
8  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
9  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
10 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
11 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
12 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
13 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
14 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
15 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
16 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
17 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
18 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
19 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
20 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
21 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
22 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
23 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
24 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
25 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
26 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
27 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
28 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
29 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
30 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
31 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
32 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
33 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
34 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
35 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
36 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
37 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
38 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
39 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
40 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
41 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
42 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
43 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
44 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
45 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
46 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
47 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
48 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
49 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
50 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
51 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
52 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
53 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
54 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
55 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           7HHK 
_cell.length_a           41.350 
_cell.length_b           42.020 
_cell.length_c           158.280 
_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                         7HHK 
_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          7HHK 
_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                     7HHK 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.14 
_reflns.d_resolution_high            1.94 
_reflns.number_obs                   21315 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.144 
_reflns.pdbx_netI_over_sigmaI        7.7 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.157 
_reflns.pdbx_Rpim_I_all              0.062 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     133905 
_reflns.pdbx_chi_squared             0.98 
_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                  1.94 
_reflns_shell.d_res_low                   1.99 
_reflns_shell.number_measured_all         9790 
_reflns_shell.number_unique_obs           1552 
_reflns_shell.Rmerge_I_obs                2.400 
_reflns_shell.pdbx_chi_squared            0.89 
_reflns_shell.pdbx_redundancy             6.3 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.615 
_reflns_shell.pdbx_Rpim_I_all             1.028 
_reflns_shell.pdbx_CC_half                0.364 
_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                                 7HHK 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     20129 
_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                             79.14 
_refine.ls_d_res_high                            1.94 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_R_factor_obs                          0.19672 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19306 
_refine.ls_R_factor_R_free                       0.26046 
_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                  1123 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.B_iso_mean                               44.537 
_refine.aniso_B[1][1]                            1.15 
_refine.aniso_B[2][2]                            -0.78 
_refine.aniso_B[3][3]                            -0.37 
_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                       0.188 
_refine.pdbx_overall_ESU_R_Free                  0.181 
_refine.overall_SU_ML                            0.179 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             6.826 
_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        2140 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.number_atoms_solvent             263 
_refine_hist.number_atoms_total               2470 
_refine_hist.d_res_high                       1.94 
_refine_hist.d_res_low                        79.14 
# 
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  ? 2310 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.816  1.826  ? 3147 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.315  5.000  ? 266  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       5.934  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.293 10.000 ? 302  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.142  0.200  ? 295  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1871 '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                  4.567  4.283  ? 1073 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 6.087  7.647  ? 1345 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  5.515  4.510  ? 1237 '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       11.004 66.06  ? 3640 '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                       1.940 
_refine_ls_shell.d_res_low                        1.990 
_refine_ls_shell.number_reflns_R_work             1462 
_refine_ls_shell.R_factor_R_work                  0.368 
_refine_ls_shell.percent_reflns_obs               99.74 
_refine_ls_shell.R_factor_R_free                  0.358 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             84 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHK 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1247413608' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHK 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 4 ? 
L N N 2 ? 
M N N 4 ? 
N N N 5 ? 
O N N 5 ? 
P 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 7HHK A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHK B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHK 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 7HHK GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHK SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHK GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHK SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHK GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHK SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,H,N 
2 1 B,I,J,K,O     
3 1 C,L,M,P       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O TRP B 22 ? O TRP B 21 N ALA B 14 ? N ALA B 13 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHK 
_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   A HOH 232 ? ? O  C HOH 206 ? ? 1.71 
2  1 O   B HOH 250 ? ? O  B HOH 271 ? ? 1.88 
3  1 O   A HOH 233 ? ? O  A HOH 289 ? ? 1.94 
4  1 OD1 C ASP 26  ? ? O  C HOH 201 ? ? 1.99 
5  1 O   C HOH 253 ? ? O  C HOH 260 ? ? 2.05 
6  1 O   C HOH 205 ? ? O  C HOH 258 ? ? 2.05 
7  1 O   A PRO 37  ? ? O  A HOH 201 ? ? 2.07 
8  1 O2  A SO4 105 ? ? O  A HOH 202 ? ? 2.08 
9  1 OD1 C ASP 9   ? ? O  C HOH 202 ? ? 2.12 
10 1 O   A HOH 208 ? ? O  A HOH 299 ? ? 2.14 
11 1 O   B ASP 66  ? ? NZ B LYS 70  ? ? 2.17 
12 1 OE1 A GLN 85  ? ? O  A HOH 203 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   B HOH 268 ? ? 1_555 O  C HOH 238 ? ? 4_435 2.01 
2 1 O   A HOH 219 ? ? 1_555 O  A HOH 263 ? ? 4_545 2.06 
3 1 NH2 C ARG 74  ? ? 1_555 O3 A LPU 104 ? ? 4_535 2.18 
4 1 O   A HOH 303 ? ? 1_555 O  C HOH 209 ? ? 4_435 2.18 
5 1 O   A HOH 269 ? ? 1_555 O  A HOH 309 ? ? 4_545 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A TYR 18 ? ? CG A TYR 18 ? ? CD2 A TYR 18 ? ? 116.62 121.00 -4.38  0.60 N 
2 1 CB A LEU 53 ? ? CG A LEU 53 ? ? CD1 A LEU 53 ? ? 99.37  111.00 -11.63 1.70 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 ? ? -151.72 64.37  
2 1 ASN B 38 ? ? 77.64   -10.79 
3 1 ASN B 87 ? ? -162.97 54.61  
4 1 ASN C 87 ? ? -166.02 50.87  
# 
_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            148.43 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 316 ? 6.22 . 
2 1 O ? A HOH 317 ? 8.23 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C ALA 29 ? C ALA 30 
11 1 Y 1 C ASP 30 ? C ASP 31 
12 1 Y 1 C GLY 31 ? C GLY 32 
13 1 Y 1 C ALA 32 ? C ALA 33 
14 1 Y 1 C VAL 33 ? C VAL 34 
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 
LPU N1   N N N 215 
LPU C4   C N N 216 
LPU C5   C N N 217 
LPU C6   C N N 218 
LPU C1   C N N 219 
LPU S1   S N N 220 
LPU O1   O N N 221 
LPU O2   O N N 222 
LPU C2   C N N 223 
LPU C3   C N N 224 
LPU O3   O N N 225 
LPU H1   H N N 226 
LPU H2   H N N 227 
LPU H3   H N N 228 
LPU H4   H N N 229 
LPU H5   H N N 230 
LPU H6   H N N 231 
LPU H7   H N N 232 
LPU H8   H N N 233 
LPU H9   H N N 234 
LPU H10  H N N 235 
LPU H11  H N N 236 
LPU H12  H N N 237 
LPU H13  H N N 238 
LYS N    N N N 239 
LYS CA   C N S 240 
LYS C    C N N 241 
LYS O    O N N 242 
LYS CB   C N N 243 
LYS CG   C N N 244 
LYS CD   C N N 245 
LYS CE   C N N 246 
LYS NZ   N N N 247 
LYS OXT  O N N 248 
LYS H    H N N 249 
LYS H2   H N N 250 
LYS HA   H N N 251 
LYS HB2  H N N 252 
LYS HB3  H N N 253 
LYS HG2  H N N 254 
LYS HG3  H N N 255 
LYS HD2  H N N 256 
LYS HD3  H N N 257 
LYS HE2  H N N 258 
LYS HE3  H N N 259 
LYS HZ1  H N N 260 
LYS HZ2  H N N 261 
LYS HZ3  H N N 262 
LYS HXT  H N N 263 
MET N    N N N 264 
MET CA   C N S 265 
MET C    C N N 266 
MET O    O N N 267 
MET CB   C N N 268 
MET CG   C N N 269 
MET SD   S N N 270 
MET CE   C N N 271 
MET OXT  O N N 272 
MET H    H N N 273 
MET H2   H N N 274 
MET HA   H N N 275 
MET HB2  H N N 276 
MET HB3  H N N 277 
MET HG2  H N N 278 
MET HG3  H N N 279 
MET HE1  H N N 280 
MET HE2  H N N 281 
MET HE3  H N N 282 
MET HXT  H N N 283 
PHE N    N N N 284 
PHE CA   C N S 285 
PHE C    C N N 286 
PHE O    O N N 287 
PHE CB   C N N 288 
PHE CG   C Y N 289 
PHE CD1  C Y N 290 
PHE CD2  C Y N 291 
PHE CE1  C Y N 292 
PHE CE2  C Y N 293 
PHE CZ   C Y N 294 
PHE OXT  O N N 295 
PHE H    H N N 296 
PHE H2   H N N 297 
PHE HA   H N N 298 
PHE HB2  H N N 299 
PHE HB3  H N N 300 
PHE HD1  H N N 301 
PHE HD2  H N N 302 
PHE HE1  H N N 303 
PHE HE2  H N N 304 
PHE HZ   H N N 305 
PHE HXT  H N N 306 
PRO N    N N N 307 
PRO CA   C N S 308 
PRO C    C N N 309 
PRO O    O N N 310 
PRO CB   C N N 311 
PRO CG   C N N 312 
PRO CD   C N N 313 
PRO OXT  O N N 314 
PRO H    H N N 315 
PRO HA   H N N 316 
PRO HB2  H N N 317 
PRO HB3  H N N 318 
PRO HG2  H N N 319 
PRO HG3  H N N 320 
PRO HD2  H N N 321 
PRO HD3  H N N 322 
PRO HXT  H N N 323 
SER N    N N N 324 
SER CA   C N S 325 
SER C    C N N 326 
SER O    O N N 327 
SER CB   C N N 328 
SER OG   O N N 329 
SER OXT  O N N 330 
SER H    H N N 331 
SER H2   H N N 332 
SER HA   H N N 333 
SER HB2  H N N 334 
SER HB3  H N N 335 
SER HG   H N N 336 
SER HXT  H N N 337 
SO4 S    S N N 338 
SO4 O1   O N N 339 
SO4 O2   O N N 340 
SO4 O3   O N N 341 
SO4 O4   O N N 342 
THR N    N N N 343 
THR CA   C N S 344 
THR C    C N N 345 
THR O    O N N 346 
THR CB   C N R 347 
THR OG1  O N N 348 
THR CG2  C N N 349 
THR OXT  O N N 350 
THR H    H N N 351 
THR H2   H N N 352 
THR HA   H N N 353 
THR HB   H N N 354 
THR HG1  H N N 355 
THR HG21 H N N 356 
THR HG22 H N N 357 
THR HG23 H N N 358 
THR HXT  H N N 359 
TRP N    N N N 360 
TRP CA   C N S 361 
TRP C    C N N 362 
TRP O    O N N 363 
TRP CB   C N N 364 
TRP CG   C Y N 365 
TRP CD1  C Y N 366 
TRP CD2  C Y N 367 
TRP NE1  N Y N 368 
TRP CE2  C Y N 369 
TRP CE3  C Y N 370 
TRP CZ2  C Y N 371 
TRP CZ3  C Y N 372 
TRP CH2  C Y N 373 
TRP OXT  O N N 374 
TRP H    H N N 375 
TRP H2   H N N 376 
TRP HA   H N N 377 
TRP HB2  H N N 378 
TRP HB3  H N N 379 
TRP HD1  H N N 380 
TRP HE1  H N N 381 
TRP HE3  H N N 382 
TRP HZ2  H N N 383 
TRP HZ3  H N N 384 
TRP HH2  H N N 385 
TRP HXT  H N N 386 
TYR N    N N N 387 
TYR CA   C N S 388 
TYR C    C N N 389 
TYR O    O N N 390 
TYR CB   C N N 391 
TYR CG   C Y N 392 
TYR CD1  C Y N 393 
TYR CD2  C Y N 394 
TYR CE1  C Y N 395 
TYR CE2  C Y N 396 
TYR CZ   C Y N 397 
TYR OH   O N N 398 
TYR OXT  O N N 399 
TYR H    H N N 400 
TYR H2   H N N 401 
TYR HA   H N N 402 
TYR HB2  H N N 403 
TYR HB3  H N N 404 
TYR HD1  H N N 405 
TYR HD2  H N N 406 
TYR HE1  H N N 407 
TYR HE2  H N N 408 
TYR HH   H N N 409 
TYR HXT  H N N 410 
VAL N    N N N 411 
VAL CA   C N S 412 
VAL C    C N N 413 
VAL O    O N N 414 
VAL CB   C N N 415 
VAL CG1  C N N 416 
VAL CG2  C N N 417 
VAL OXT  O N N 418 
VAL H    H N N 419 
VAL H2   H N N 420 
VAL HA   H N N 421 
VAL HB   H N N 422 
VAL HG11 H N N 423 
VAL HG12 H N N 424 
VAL HG13 H N N 425 
VAL HG21 H N N 426 
VAL HG22 H N N 427 
VAL HG23 H N N 428 
VAL HXT  H N N 429 
# 
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 
LPU O2  S1   doub N N 203 
LPU C6  N1   sing N N 204 
LPU C6  C5   sing N N 205 
LPU S1  N1   sing N N 206 
LPU S1  O1   doub N N 207 
LPU S1  C1   sing N N 208 
LPU N1  C2   sing N N 209 
LPU C5  C4   sing N N 210 
LPU O3  C4   sing N N 211 
LPU C4  C3   sing N N 212 
LPU C2  C3   sing N N 213 
LPU C4  H1   sing N N 214 
LPU C5  H2   sing N N 215 
LPU C5  H3   sing N N 216 
LPU C6  H4   sing N N 217 
LPU C6  H5   sing N N 218 
LPU C1  H6   sing N N 219 
LPU C1  H7   sing N N 220 
LPU C1  H8   sing N N 221 
LPU C2  H9   sing N N 222 
LPU C2  H10  sing N N 223 
LPU C3  H11  sing N N 224 
LPU C3  H12  sing N N 225 
LPU O3  H13  sing N N 226 
LYS N   CA   sing N N 227 
LYS N   H    sing N N 228 
LYS N   H2   sing N N 229 
LYS CA  C    sing N N 230 
LYS CA  CB   sing N N 231 
LYS CA  HA   sing N N 232 
LYS C   O    doub N N 233 
LYS C   OXT  sing N N 234 
LYS CB  CG   sing N N 235 
LYS CB  HB2  sing N N 236 
LYS CB  HB3  sing N N 237 
LYS CG  CD   sing N N 238 
LYS CG  HG2  sing N N 239 
LYS CG  HG3  sing N N 240 
LYS CD  CE   sing N N 241 
LYS CD  HD2  sing N N 242 
LYS CD  HD3  sing N N 243 
LYS CE  NZ   sing N N 244 
LYS CE  HE2  sing N N 245 
LYS CE  HE3  sing N N 246 
LYS NZ  HZ1  sing N N 247 
LYS NZ  HZ2  sing N N 248 
LYS NZ  HZ3  sing N N 249 
LYS OXT HXT  sing N N 250 
MET N   CA   sing N N 251 
MET N   H    sing N N 252 
MET N   H2   sing N N 253 
MET CA  C    sing N N 254 
MET CA  CB   sing N N 255 
MET CA  HA   sing N N 256 
MET C   O    doub N N 257 
MET C   OXT  sing N N 258 
MET CB  CG   sing N N 259 
MET CB  HB2  sing N N 260 
MET CB  HB3  sing N N 261 
MET CG  SD   sing N N 262 
MET CG  HG2  sing N N 263 
MET CG  HG3  sing N N 264 
MET SD  CE   sing N N 265 
MET CE  HE1  sing N N 266 
MET CE  HE2  sing N N 267 
MET CE  HE3  sing N N 268 
MET OXT HXT  sing N N 269 
PHE N   CA   sing N N 270 
PHE N   H    sing N N 271 
PHE N   H2   sing N N 272 
PHE CA  C    sing N N 273 
PHE CA  CB   sing N N 274 
PHE CA  HA   sing N N 275 
PHE C   O    doub N N 276 
PHE C   OXT  sing N N 277 
PHE CB  CG   sing N N 278 
PHE CB  HB2  sing N N 279 
PHE CB  HB3  sing N N 280 
PHE CG  CD1  doub Y N 281 
PHE CG  CD2  sing Y N 282 
PHE CD1 CE1  sing Y N 283 
PHE CD1 HD1  sing N N 284 
PHE CD2 CE2  doub Y N 285 
PHE CD2 HD2  sing N N 286 
PHE CE1 CZ   doub Y N 287 
PHE CE1 HE1  sing N N 288 
PHE CE2 CZ   sing Y N 289 
PHE CE2 HE2  sing N N 290 
PHE CZ  HZ   sing N N 291 
PHE OXT HXT  sing N N 292 
PRO N   CA   sing N N 293 
PRO N   CD   sing N N 294 
PRO N   H    sing N N 295 
PRO CA  C    sing N N 296 
PRO CA  CB   sing N N 297 
PRO CA  HA   sing N N 298 
PRO C   O    doub N N 299 
PRO C   OXT  sing N N 300 
PRO CB  CG   sing N N 301 
PRO CB  HB2  sing N N 302 
PRO CB  HB3  sing N N 303 
PRO CG  CD   sing N N 304 
PRO CG  HG2  sing N N 305 
PRO CG  HG3  sing N N 306 
PRO CD  HD2  sing N N 307 
PRO CD  HD3  sing N N 308 
PRO OXT HXT  sing N N 309 
SER N   CA   sing N N 310 
SER N   H    sing N N 311 
SER N   H2   sing N N 312 
SER CA  C    sing N N 313 
SER CA  CB   sing N N 314 
SER CA  HA   sing N N 315 
SER C   O    doub N N 316 
SER C   OXT  sing N N 317 
SER CB  OG   sing N N 318 
SER CB  HB2  sing N N 319 
SER CB  HB3  sing N N 320 
SER OG  HG   sing N N 321 
SER OXT HXT  sing N N 322 
SO4 S   O1   doub N N 323 
SO4 S   O2   doub N N 324 
SO4 S   O3   sing N N 325 
SO4 S   O4   sing N N 326 
THR N   CA   sing N N 327 
THR N   H    sing N N 328 
THR N   H2   sing N N 329 
THR CA  C    sing N N 330 
THR CA  CB   sing N N 331 
THR CA  HA   sing N N 332 
THR C   O    doub N N 333 
THR C   OXT  sing N N 334 
THR CB  OG1  sing N N 335 
THR CB  CG2  sing N N 336 
THR CB  HB   sing N N 337 
THR OG1 HG1  sing N N 338 
THR CG2 HG21 sing N N 339 
THR CG2 HG22 sing N N 340 
THR CG2 HG23 sing N N 341 
THR OXT HXT  sing N N 342 
TRP N   CA   sing N N 343 
TRP N   H    sing N N 344 
TRP N   H2   sing N N 345 
TRP CA  C    sing N N 346 
TRP CA  CB   sing N N 347 
TRP CA  HA   sing N N 348 
TRP C   O    doub N N 349 
TRP C   OXT  sing N N 350 
TRP CB  CG   sing N N 351 
TRP CB  HB2  sing N N 352 
TRP CB  HB3  sing N N 353 
TRP CG  CD1  doub Y N 354 
TRP CG  CD2  sing Y N 355 
TRP CD1 NE1  sing Y N 356 
TRP CD1 HD1  sing N N 357 
TRP CD2 CE2  doub Y N 358 
TRP CD2 CE3  sing Y N 359 
TRP NE1 CE2  sing Y N 360 
TRP NE1 HE1  sing N N 361 
TRP CE2 CZ2  sing Y N 362 
TRP CE3 CZ3  doub Y N 363 
TRP CE3 HE3  sing N N 364 
TRP CZ2 CH2  doub Y N 365 
TRP CZ2 HZ2  sing N N 366 
TRP CZ3 CH2  sing Y N 367 
TRP CZ3 HZ3  sing N N 368 
TRP CH2 HH2  sing N N 369 
TRP OXT HXT  sing N N 370 
TYR N   CA   sing N N 371 
TYR N   H    sing N N 372 
TYR N   H2   sing N N 373 
TYR CA  C    sing N N 374 
TYR CA  CB   sing N N 375 
TYR CA  HA   sing N N 376 
TYR C   O    doub N N 377 
TYR C   OXT  sing N N 378 
TYR CB  CG   sing N N 379 
TYR CB  HB2  sing N N 380 
TYR CB  HB3  sing N N 381 
TYR CG  CD1  doub Y N 382 
TYR CG  CD2  sing Y N 383 
TYR CD1 CE1  sing Y N 384 
TYR CD1 HD1  sing N N 385 
TYR CD2 CE2  doub Y N 386 
TYR CD2 HD2  sing N N 387 
TYR CE1 CZ   doub Y N 388 
TYR CE1 HE1  sing N N 389 
TYR CE2 CZ   sing Y N 390 
TYR CE2 HE2  sing N N 391 
TYR CZ  OH   sing N N 392 
TYR OH  HH   sing N N 393 
TYR OXT HXT  sing N N 394 
VAL N   CA   sing N N 395 
VAL N   H    sing N N 396 
VAL N   H2   sing N N 397 
VAL CA  C    sing N N 398 
VAL CA  CB   sing N N 399 
VAL CA  HA   sing N N 400 
VAL C   O    doub N N 401 
VAL C   OXT  sing N N 402 
VAL CB  CG1  sing N N 403 
VAL CB  CG2  sing N N 404 
VAL CB  HB   sing N N 405 
VAL CG1 HG11 sing N N 406 
VAL CG1 HG12 sing N N 407 
VAL CG1 HG13 sing N N 408 
VAL CG2 HG21 sing N N 409 
VAL CG2 HG22 sing N N 410 
VAL CG2 HG23 sing N N 411 
VAL OXT HXT  sing N N 412 
# 
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                    7HHK 
_atom_sites.fract_transf_matrix[1][1]   0.024184 
_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]   0.023798 
_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]   0.006318 
_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  ? 0.300   4.432   2.374   1.00 55.05  ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.674  3.585   1.636   1.00 60.38  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.064   2.526   0.813   1.00 53.19  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.229   2.685   0.479   1.00 52.60  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.625  4.411   0.752   1.00 66.24  ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.755  5.178   1.469   1.00 67.91  ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.780  4.421   2.757   1.00 66.06  ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -2.863  4.925   4.225   1.00 68.58  ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.602  1.382   0.530   1.00 52.47  ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? -0.087  0.333   -0.361  1.00 45.16  ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.216   0.754   -1.805  1.00 47.76  ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.461  1.601   -2.392  1.00 47.74  ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.311  -0.668  -0.302  1.00 44.34  ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.860  -0.491  1.086   1.00 45.84  ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.887  1.018   1.159   1.00 48.31  ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.246   0.142   -2.384  1.00 46.18  ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.446   0.214   -3.819  1.00 44.51  ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.890   -1.100  -4.338  1.00 43.91  ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.431   -1.902  -3.533  1.00 40.58  ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.933   0.407   -4.152  1.00 51.41  ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.534   1.689   -3.657  1.00 64.31  ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.269   2.253   -2.424  1.00 72.58  ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.410   2.511   -4.253  1.00 71.46  ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 3.958   3.376   -2.291  1.00 66.68  ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.659   3.551   -3.391  1.00 67.53  ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.883   -1.270  -5.664  1.00 35.39  ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.608   -2.516  -6.343  1.00 35.73  ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.700   -3.528  -5.983  1.00 35.08  ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.779   -3.168  -5.519  1.00 35.02  ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.565   -2.228  -7.849  1.00 38.44  ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.426   -4.808  -6.193  1.00 36.64  ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.434   -5.821  -5.940  1.00 38.03  ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.606   -5.687  -6.922  1.00 41.08  ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.414   -5.389  -8.100  1.00 39.71  ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.800   -7.216  -5.998  1.00 31.36  ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.118   -7.621  -4.699  1.00 36.88  ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.847   -7.760  -3.513  1.00 31.25  ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.268  -7.836  -4.668  1.00 32.76  ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.205   -8.114  -2.321  1.00 33.79  ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.884  -8.231  -3.495  1.00 31.15  ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.159  -8.350  -2.320  1.00 30.91  ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.824   -6.012  -6.464  1.00 38.17  ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 5.946   -5.982  -7.393  1.00 34.86  ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.895   -7.144  -7.094  1.00 35.29  ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.848   -7.715  -6.019  1.00 30.05  ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.667   -4.633  -7.274  1.00 33.63  ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.220   -4.486  -5.863  1.00 40.69  ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 7.894   -3.139  -5.646  1.00 48.53  ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.675   -3.096  -4.375  1.00 51.09  ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.816   -3.302  -3.214  1.00 42.34  ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.767   -7.570  -8.045  1.00 30.65  ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.658   -8.693  -7.780  1.00 34.52  ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.434   -8.393  -6.482  1.00 28.68  ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 9.811   -7.251  -6.231  1.00 29.95  ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.528   -8.803  -9.091  1.00 32.11  ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.688   -8.083  -10.168 1.00 33.09  ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 7.903   -7.004  -9.408  1.00 30.78  ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.609   -9.432  -5.648  1.00 28.46  ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.351  -9.397  -4.391  1.00 24.48  ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.424   -9.265  -3.169  1.00 28.77  ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.876   -9.427  -2.026  1.00 33.77  ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.168   -8.834  -3.382  1.00 26.77  ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.188   -8.742  -2.298  1.00 32.34  ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 6.940   -10.117 -1.682  1.00 30.02  ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.813   -11.118 -2.388  1.00 29.76  ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 5.873   -8.108  -2.747  1.00 34.45  ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 5.916   -6.605  -2.971  1.00 34.61  ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 6.877   -5.950  -2.487  1.00 30.46  ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.019   -6.101  -3.661  1.00 38.02  ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 6.825   -10.164 -0.353  1.00 28.34  ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.710   -11.439 0.342   1.00 25.49  ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.264   -11.562 0.796   1.00 31.30  ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.700   -10.580 1.301   1.00 34.03  ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.662   -11.469 1.541   1.00 26.65  ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.137   -11.228 1.203   1.00 28.06  ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 9.992   -11.289 2.463   1.00 26.25  ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.527   -12.294 0.153   1.00 28.96  ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.687   -12.771 0.665   1.00 26.20  ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.258   -12.881 0.911   1.00 27.59  ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 2.941   -14.226 1.564   1.00 29.71  ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.804   -15.112 1.646   1.00 28.72  ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.454   -12.682 -0.384  1.00 24.91  ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.705   -11.290 -0.978  1.00 26.08  ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.752   -13.807 -1.381  1.00 23.97  ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.696   -14.374 2.024   1.00 28.00  ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.120   -15.712 2.164   1.00 25.46  ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.171   -15.832 0.985   1.00 32.19  ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.618  -14.921 0.768   1.00 27.51  ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.377   -16.062 3.467   1.00 30.08  ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.325   -16.181 4.657   1.00 29.36  ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.723   -15.069 5.379   1.00 32.91  ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 1.885   -17.394 4.993   1.00 32.44  ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.627   -15.179 6.421   1.00 39.53  ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.788   -17.516 6.042   1.00 39.17  ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.161   -16.409 6.759   1.00 40.65  ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.365   -16.876 0.161   1.00 35.05  ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.448  -17.085 -1.031  1.00 36.86  ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.426  -18.223 -0.741  1.00 31.45  ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -1.055  -19.275 -0.174  1.00 35.89  ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.408   -17.351 -2.278  1.00 28.21  ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.685  -17.983 -1.118  1.00 31.28  ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.768  -18.904 -0.843  1.00 31.68  ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -4.220  -19.533 -2.155  1.00 34.31  ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.642  -18.834 -3.076  1.00 35.19  ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.976  -18.190 -0.225  1.00 32.59  ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -6.104  -19.151 0.083   1.00 37.22  ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.713  -20.125 1.198   1.00 42.45  ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.863  -20.952 1.773   1.00 40.35  ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -7.196  -22.082 0.895   1.00 39.02  ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -4.140  -20.862 -2.204  1.00 33.34  ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.855  -21.609 -3.230  1.00 39.72  ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.864  -22.561 -2.603  1.00 41.16  ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.654  -23.039 -1.485  1.00 35.22  ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.879  -22.385 -4.106  1.00 36.61  ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -2.995  -21.406 -4.874  1.00 44.54  ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.873  -22.197 -6.026  1.00 45.11  ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -3.059  -22.794 -7.237  1.00 53.96  ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.948  -22.810 -3.356  1.00 45.27  ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -8.013  -23.729 -2.978  1.00 44.34  ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -7.394  -25.028 -2.484  1.00 45.23  ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -6.543  -25.622 -3.156  1.00 40.79  ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.824  -24.127 -4.223  1.00 57.15  ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -10.131 -24.877 -3.983  1.00 65.03  ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -11.220 -24.071 -3.265  1.00 75.83  ? 16  LYS A CD  1 
ATOM   125  C CE  . LYS A 1 17 ? -12.553 -24.767 -3.090  1.00 76.42  ? 16  LYS A CE  1 
ATOM   126  N NZ  . LYS A 1 17 ? -13.143 -25.172 -4.374  1.00 74.18  ? 16  LYS A NZ  1 
ATOM   127  N N   . GLY A 1 18 ? -7.809  -25.453 -1.290  1.00 37.03  ? 17  GLY A N   1 
ATOM   128  C CA  . GLY A 1 18 ? -7.381  -26.759 -0.832  1.00 38.09  ? 17  GLY A CA  1 
ATOM   129  C C   . GLY A 1 18 ? -6.014  -26.723 -0.155  1.00 48.90  ? 17  GLY A C   1 
ATOM   130  O O   . GLY A 1 18 ? -5.544  -27.754 0.289   1.00 47.17  ? 17  GLY A O   1 
ATOM   131  N N   . TYR A 1 19 ? -5.369  -25.554 -0.054  1.00 39.85  ? 18  TYR A N   1 
ATOM   132  C CA  . TYR A 1 19 ? -4.109  -25.540 0.667   1.00 36.48  ? 18  TYR A CA  1 
ATOM   133  C C   . TYR A 1 19 ? -4.159  -24.424 1.699   1.00 35.58  ? 18  TYR A C   1 
ATOM   134  O O   . TYR A 1 19 ? -4.813  -23.406 1.494   1.00 34.70  ? 18  TYR A O   1 
ATOM   135  C CB  . TYR A 1 19 ? -2.826  -25.345 -0.144  1.00 41.61  ? 18  TYR A CB  1 
ATOM   136  C CG  . TYR A 1 19 ? -2.499  -26.406 -1.199  1.00 34.57  ? 18  TYR A CG  1 
ATOM   137  C CD2 . TYR A 1 19 ? -3.051  -26.219 -2.464  1.00 41.33  ? 18  TYR A CD2 1 
ATOM   138  C CE1 . TYR A 1 19 ? -1.502  -28.419 -2.061  1.00 61.68  ? 18  TYR A CE1 1 
ATOM   139  C CE2 . TYR A 1 19 ? -2.841  -27.088 -3.523  1.00 46.29  ? 18  TYR A CE2 1 
ATOM   140  C CZ  . TYR A 1 19 ? -2.054  -28.208 -3.318  1.00 68.11  ? 18  TYR A CZ  1 
ATOM   141  O OH  . TYR A 1 19 ? -1.848  -29.078 -4.364  1.00 67.11  ? 18  TYR A OH  1 
ATOM   142  N N   . PRO A 1 20 ? -3.408  -24.544 2.806   1.00 33.58  ? 19  PRO A N   1 
ATOM   143  C CA  . PRO A 1 20 ? -3.352  -23.452 3.772   1.00 39.18  ? 19  PRO A CA  1 
ATOM   144  C C   . PRO A 1 20 ? -2.609  -22.282 3.098   1.00 38.07  ? 19  PRO A C   1 
ATOM   145  O O   . PRO A 1 20 ? -1.889  -22.458 2.104   1.00 36.51  ? 19  PRO A O   1 
ATOM   146  C CB  . PRO A 1 20 ? -2.625  -24.165 4.952   1.00 32.66  ? 19  PRO A CB  1 
ATOM   147  C CG  . PRO A 1 20 ? -1.623  -25.113 4.274   1.00 35.56  ? 19  PRO A CG  1 
ATOM   148  C CD  . PRO A 1 20 ? -2.458  -25.638 3.100   1.00 40.97  ? 19  PRO A CD  1 
ATOM   149  N N   . HIS A 1 21 ? -2.885  -21.068 3.572   1.00 29.85  ? 20  HIS A N   1 
ATOM   150  C CA  . HIS A 1 21 ? -2.131  -19.876 3.229   1.00 29.01  ? 20  HIS A CA  1 
ATOM   151  C C   . HIS A 1 21 ? -0.637  -20.225 3.296   1.00 34.58  ? 20  HIS A C   1 
ATOM   152  O O   . HIS A 1 21 ? -0.173  -20.702 4.339   1.00 32.37  ? 20  HIS A O   1 
ATOM   153  C CB  . HIS A 1 21 ? -2.573  -18.719 4.147   1.00 28.12  ? 20  HIS A CB  1 
ATOM   154  C CG  . HIS A 1 21 ? -4.030  -18.344 4.056   1.00 34.73  ? 20  HIS A CG  1 
ATOM   155  N ND1 . HIS A 1 21 ? -5.045  -19.054 4.695   1.00 33.64  ? 20  HIS A ND1 1 
ATOM   156  C CD2 . HIS A 1 21 ? -4.645  -17.308 3.409   1.00 31.35  ? 20  HIS A CD2 1 
ATOM   157  C CE1 . HIS A 1 21 ? -6.228  -18.492 4.417   1.00 29.90  ? 20  HIS A CE1 1 
ATOM   158  N NE2 . HIS A 1 21 ? -6.009  -17.422 3.639   1.00 35.18  ? 20  HIS A NE2 1 
ATOM   159  N N   . TRP A 1 22 ? 0.127   -19.931 2.218   1.00 30.34  ? 21  TRP A N   1 
ATOM   160  C CA  . TRP A 1 22 ? 1.449   -20.537 2.053   1.00 29.51  ? 21  TRP A CA  1 
ATOM   161  C C   . TRP A 1 22 ? 2.539   -19.470 1.879   1.00 31.36  ? 21  TRP A C   1 
ATOM   162  O O   . TRP A 1 22 ? 2.379   -18.557 1.066   1.00 29.07  ? 21  TRP A O   1 
ATOM   163  C CB  . TRP A 1 22 ? 1.438   -21.506 0.853   1.00 32.42  ? 21  TRP A CB  1 
ATOM   164  C CG  . TRP A 1 22 ? 2.511   -22.569 0.920   1.00 35.63  ? 21  TRP A CG  1 
ATOM   165  C CD1 . TRP A 1 22 ? 3.858   -22.398 0.731   1.00 32.10  ? 21  TRP A CD1 1 
ATOM   166  C CD2 . TRP A 1 22 ? 2.327   -23.976 1.211   1.00 33.84  ? 21  TRP A CD2 1 
ATOM   167  N NE1 . TRP A 1 22 ? 4.523   -23.598 0.851   1.00 34.40  ? 21  TRP A NE1 1 
ATOM   168  C CE2 . TRP A 1 22 ? 3.609   -24.589 1.136   1.00 34.58  ? 21  TRP A CE2 1 
ATOM   169  C CE3 . TRP A 1 22 ? 1.207   -24.779 1.479   1.00 36.74  ? 21  TRP A CE3 1 
ATOM   170  C CZ2 . TRP A 1 22 ? 3.806   -25.960 1.366   1.00 37.02  ? 21  TRP A CZ2 1 
ATOM   171  C CZ3 . TRP A 1 22 ? 1.402   -26.135 1.678   1.00 38.66  ? 21  TRP A CZ3 1 
ATOM   172  C CH2 . TRP A 1 22 ? 2.687   -26.714 1.658   1.00 40.17  ? 21  TRP A CH2 1 
ATOM   173  N N   . PRO A 1 23 ? 3.694   -19.537 2.598   1.00 27.77  ? 22  PRO A N   1 
ATOM   174  C CA  . PRO A 1 23 ? 4.737   -18.514 2.448   1.00 29.57  ? 22  PRO A CA  1 
ATOM   175  C C   . PRO A 1 23 ? 5.232   -18.508 1.002   1.00 28.63  ? 22  PRO A C   1 
ATOM   176  O O   . PRO A 1 23 ? 5.469   -19.575 0.398   1.00 29.43  ? 22  PRO A O   1 
ATOM   177  C CB  . PRO A 1 23 ? 5.842   -18.888 3.470   1.00 28.70  ? 22  PRO A CB  1 
ATOM   178  C CG  . PRO A 1 23 ? 5.602   -20.387 3.715   1.00 28.44  ? 22  PRO A CG  1 
ATOM   179  C CD  . PRO A 1 23 ? 4.060   -20.555 3.589   1.00 29.83  ? 22  PRO A CD  1 
ATOM   180  N N   . ALA A 1 24 ? 5.286   -17.300 0.441   1.00 26.33  ? 23  ALA A N   1 
ATOM   181  C CA  . ALA A 1 24 ? 5.552   -17.151 -0.986  1.00 25.40  ? 23  ALA A CA  1 
ATOM   182  C C   . ALA A 1 24 ? 6.125   -15.782 -1.338  1.00 27.30  ? 23  ALA A C   1 
ATOM   183  O O   . ALA A 1 24 ? 6.250   -14.894 -0.501  1.00 23.84  ? 23  ALA A O   1 
ATOM   184  C CB  . ALA A 1 24 ? 4.316   -17.504 -1.814  1.00 27.87  ? 23  ALA A CB  1 
ATOM   185  N N   . ARG A 1 25 ? 6.602   -15.644 -2.596  1.00 26.98  ? 24  ARG A N   1 
ATOM   186  C CA  . ARG A 1 25 ? 7.103   -14.359 -3.026  1.00 27.82  ? 24  ARG A CA  1 
ATOM   187  C C   . ARG A 1 25 ? 6.532   -14.038 -4.404  1.00 26.58  ? 24  ARG A C   1 
ATOM   188  O O   . ARG A 1 25 ? 6.207   -14.940 -5.197  1.00 26.24  ? 24  ARG A O   1 
ATOM   189  C CB  . ARG A 1 25 ? 8.623   -14.167 -2.923  1.00 25.79  ? 24  ARG A CB  1 
ATOM   190  C CG  . ARG A 1 25 ? 9.323   -15.040 -3.976  1.00 29.10  ? 24  ARG A CG  1 
ATOM   191  C CD  . ARG A 1 25 ? 10.880  -14.819 -3.957  1.00 26.37  ? 24  ARG A CD  1 
ATOM   192  N NE  . ARG A 1 25 ? 11.571  -15.715 -4.894  1.00 23.04  ? 24  ARG A NE  1 
ATOM   193  C CZ  . ARG A 1 25 ? 12.801  -16.202 -4.754  1.00 26.63  ? 24  ARG A CZ  1 
ATOM   194  N NH1 . ARG A 1 25 ? 13.498  -16.042 -3.654  1.00 24.26  ? 24  ARG A NH1 1 
ATOM   195  N NH2 . ARG A 1 25 ? 13.356  -16.862 -5.751  1.00 29.26  ? 24  ARG A NH2 1 
ATOM   196  N N   . ILE A 1 26 ? 6.474   -12.748 -4.721  1.00 29.96  ? 25  ILE A N   1 
ATOM   197  C CA  . ILE A 1 26 ? 6.231   -12.389 -6.123  1.00 29.84  ? 25  ILE A CA  1 
ATOM   198  C C   . ILE A 1 26 ? 7.533   -12.579 -6.898  1.00 30.01  ? 25  ILE A C   1 
ATOM   199  O O   . ILE A 1 26 ? 8.555   -11.992 -6.578  1.00 31.51  ? 25  ILE A O   1 
ATOM   200  C CB  . ILE A 1 26 ? 5.711   -10.950 -6.309  1.00 32.00  ? 25  ILE A CB  1 
ATOM   201  C CG1 . ILE A 1 26 ? 4.505   -10.565 -5.400  1.00 33.78  ? 25  ILE A CG1 1 
ATOM   202  C CG2 . ILE A 1 26 ? 5.519   -10.578 -7.798  1.00 25.01  ? 25  ILE A CG2 1 
ATOM   203  C CD1 . ILE A 1 26 ? 3.219   -11.322 -5.574  1.00 34.38  ? 25  ILE A CD1 1 
ATOM   204  N N   . ASP A 1 27 ? 7.511   -13.429 -7.915  1.00 33.29  ? 26  ASP A N   1 
ATOM   205  C CA  . ASP A 1 27 ? 8.741   -13.649 -8.653  1.00 34.85  ? 26  ASP A CA  1 
ATOM   206  C C   . ASP A 1 27 ? 8.920   -12.621 -9.772  1.00 35.50  ? 26  ASP A C   1 
ATOM   207  O O   . ASP A 1 27 ? 7.996   -11.912 -10.183 1.00 29.36  ? 26  ASP A O   1 
ATOM   208  C CB  . ASP A 1 27 ? 8.862   -15.069 -9.171  1.00 36.47  ? 26  ASP A CB  1 
ATOM   209  C CG  . ASP A 1 27 ? 9.882   -15.926 -8.454  1.00 38.82  ? 26  ASP A CG  1 
ATOM   210  O OD1 . ASP A 1 27 ? 10.438  -15.452 -7.440  1.00 42.87  ? 26  ASP A OD1 1 
ATOM   211  O OD2 . ASP A 1 27 ? 10.133  -17.027 -8.944  1.00 38.99  ? 26  ASP A OD2 1 
ATOM   212  N N   . ASP A 1 28 ? 10.183  -12.477 -10.171 1.00 35.23  ? 27  ASP A N   1 
ATOM   213  C CA  . ASP A 1 28 ? 10.531  -11.873 -11.439 1.00 39.86  ? 27  ASP A CA  1 
ATOM   214  C C   . ASP A 1 28 ? 10.265  -12.891 -12.544 1.00 36.26  ? 27  ASP A C   1 
ATOM   215  O O   . ASP A 1 28 ? 10.268  -14.092 -12.305 1.00 38.95  ? 27  ASP A O   1 
ATOM   216  C CB  . ASP A 1 28 ? 12.022  -11.573 -11.463 1.00 46.33  ? 27  ASP A CB  1 
ATOM   217  C CG  . ASP A 1 28 ? 12.453  -10.297 -10.752 1.00 53.72  ? 27  ASP A CG  1 
ATOM   218  O OD1 . ASP A 1 28 ? 12.047  -9.191  -11.205 1.00 53.07  ? 27  ASP A OD1 1 
ATOM   219  O OD2 . ASP A 1 28 ? 13.195  -10.417 -9.750  1.00 62.89  ? 27  ASP A OD2 1 
ATOM   220  N N   . ILE A 1 29 ? 10.094  -12.406 -13.765 1.00 38.69  ? 28  ILE A N   1 
ATOM   221  C CA  . ILE A 1 29 ? 10.157  -13.250 -14.946 1.00 36.63  ? 28  ILE A CA  1 
ATOM   222  C C   . ILE A 1 29 ? 11.533  -13.048 -15.595 1.00 43.51  ? 28  ILE A C   1 
ATOM   223  O O   . ILE A 1 29 ? 11.868  -11.909 -15.919 1.00 39.52  ? 28  ILE A O   1 
ATOM   224  C CB  . ILE A 1 29 ? 9.048   -12.769 -15.886 1.00 39.89  ? 28  ILE A CB  1 
ATOM   225  C CG1 . ILE A 1 29 ? 7.651   -12.832 -15.205 1.00 44.53  ? 28  ILE A CG1 1 
ATOM   226  C CG2 . ILE A 1 29 ? 9.098   -13.504 -17.235 1.00 29.17  ? 28  ILE A CG2 1 
ATOM   227  C CD1 . ILE A 1 29 ? 6.757   -11.645 -15.531 1.00 40.14  ? 28  ILE A CD1 1 
ATOM   228  N N   . ALA A 1 30 ? 12.327  -14.127 -15.764 1.00 40.43  ? 29  ALA A N   1 
ATOM   229  C CA  . ALA A 1 30 ? 13.602  -14.072 -16.484 1.00 40.79  ? 29  ALA A CA  1 
ATOM   230  C C   . ALA A 1 30 ? 13.370  -13.804 -17.982 1.00 40.23  ? 29  ALA A C   1 
ATOM   231  O O   . ALA A 1 30 ? 12.346  -14.189 -18.575 1.00 31.91  ? 29  ALA A O   1 
ATOM   232  C CB  . ALA A 1 30 ? 14.406  -15.352 -16.273 1.00 36.39  ? 29  ALA A CB  1 
ATOM   233  N N   . ASP A 1 31 ? 14.320  -13.077 -18.575 1.00 37.75  ? 30  ASP A N   1 
ATOM   234  C CA  . ASP A 1 31 ? 14.328  -12.837 -20.010 1.00 39.33  ? 30  ASP A CA  1 
ATOM   235  C C   . ASP A 1 31 ? 14.126  -14.178 -20.689 1.00 28.72  ? 30  ASP A C   1 
ATOM   236  O O   . ASP A 1 31 ? 14.697  -15.141 -20.240 1.00 35.22  ? 30  ASP A O   1 
ATOM   237  C CB  . ASP A 1 31 ? 15.679  -12.298 -20.468 1.00 39.82  ? 30  ASP A CB  1 
ATOM   238  C CG  . ASP A 1 31 ? 15.880  -10.811 -20.253 1.00 35.86  ? 30  ASP A CG  1 
ATOM   239  O OD1 . ASP A 1 31 ? 14.905  -10.111 -20.121 1.00 38.99  ? 30  ASP A OD1 1 
ATOM   240  O OD2 . ASP A 1 31 ? 17.017  -10.380 -20.187 1.00 40.54  ? 30  ASP A OD2 1 
ATOM   241  N N   . GLY A 1 32 ? 13.193  -14.255 -21.635 1.00 36.37  ? 31  GLY A N   1 
ATOM   242  C CA  . GLY A 1 32 ? 12.997  -15.450 -22.435 1.00 33.08  ? 31  GLY A CA  1 
ATOM   243  C C   . GLY A 1 32 ? 12.059  -16.460 -21.766 1.00 44.54  ? 31  GLY A C   1 
ATOM   244  O O   . GLY A 1 32 ? 11.771  -17.488 -22.359 1.00 37.73  ? 31  GLY A O   1 
ATOM   245  N N   . ALA A 1 33 ? 11.649  -16.202 -20.514 1.00 36.77  ? 32  ALA A N   1 
ATOM   246  C CA  . ALA A 1 33 ? 10.814  -17.134 -19.767 1.00 36.63  ? 32  ALA A CA  1 
ATOM   247  C C   . ALA A 1 33 ? 9.328   -16.857 -20.028 1.00 35.09  ? 32  ALA A C   1 
ATOM   248  O O   . ALA A 1 33 ? 8.933   -15.798 -20.521 1.00 34.91  ? 32  ALA A O   1 
ATOM   249  C CB  . ALA A 1 33 ? 11.168  -17.059 -18.288 1.00 40.30  ? 32  ALA A CB  1 
ATOM   250  N N   . VAL A 1 34 ? 8.489   -17.829 -19.675 1.00 41.44  ? 33  VAL A N   1 
ATOM   251  C CA  . VAL A 1 34 ? 7.048   -17.723 -19.857 1.00 37.03  ? 33  VAL A CA  1 
ATOM   252  C C   . VAL A 1 34 ? 6.462   -16.683 -18.908 1.00 35.41  ? 33  VAL A C   1 
ATOM   253  O O   . VAL A 1 34 ? 6.703   -16.712 -17.710 1.00 37.37  ? 33  VAL A O   1 
ATOM   254  C CB  . VAL A 1 34 ? 6.440   -19.119 -19.614 1.00 41.12  ? 33  VAL A CB  1 
ATOM   255  C CG1 . VAL A 1 34 ? 4.912   -19.093 -19.641 1.00 45.19  ? 33  VAL A CG1 1 
ATOM   256  C CG2 . VAL A 1 34 ? 6.978   -20.123 -20.634 1.00 39.29  ? 33  VAL A CG2 1 
ATOM   257  N N   . LYS A 1 35 ? 5.699   -15.766 -19.488 1.00 34.84  ? 34  LYS A N   1 
ATOM   258  C CA  . LYS A 1 35 ? 5.028   -14.700 -18.783 1.00 38.20  ? 34  LYS A CA  1 
ATOM   259  C C   . LYS A 1 35 ? 3.712   -15.255 -18.237 1.00 46.21  ? 34  LYS A C   1 
ATOM   260  O O   . LYS A 1 35 ? 3.161   -16.218 -18.778 1.00 38.16  ? 34  LYS A O   1 
ATOM   261  C CB  . LYS A 1 35 ? 4.659   -13.532 -19.706 1.00 37.84  ? 34  LYS A CB  1 
ATOM   262  C CG  . LYS A 1 35 ? 5.833   -12.650 -20.130 1.00 39.39  ? 34  LYS A CG  1 
ATOM   263  C CD  . LYS A 1 35 ? 5.459   -11.511 -21.074 1.00 37.50  ? 34  LYS A CD  1 
ATOM   264  C CE  . LYS A 1 35 ? 5.274   -11.953 -22.497 1.00 41.92  ? 34  LYS A CE  1 
ATOM   265  N NZ  . LYS A 1 35 ? 4.978   -10.875 -23.435 1.00 42.32  ? 34  LYS A NZ  1 
ATOM   266  N N   . PRO A 1 36 ? 3.184   -14.663 -17.144 1.00 43.66  ? 35  PRO A N   1 
ATOM   267  C CA  . PRO A 1 36 ? 1.917   -15.101 -16.571 1.00 46.27  ? 35  PRO A CA  1 
ATOM   268  C C   . PRO A 1 36 ? 0.821   -14.557 -17.474 1.00 42.91  ? 35  PRO A C   1 
ATOM   269  O O   . PRO A 1 36 ? 1.069   -13.648 -18.249 1.00 42.27  ? 35  PRO A O   1 
ATOM   270  C CB  . PRO A 1 36 ? 1.837   -14.439 -15.184 1.00 38.39  ? 35  PRO A CB  1 
ATOM   271  C CG  . PRO A 1 36 ? 3.063   -13.542 -15.058 1.00 43.20  ? 35  PRO A CG  1 
ATOM   272  C CD  . PRO A 1 36 ? 3.768   -13.534 -16.405 1.00 44.33  ? 35  PRO A CD  1 
ATOM   273  N N   . PRO A 1 37 ? -0.431  -15.044 -17.330 1.00 44.76  ? 36  PRO A N   1 
ATOM   274  C CA  . PRO A 1 37 ? -1.588  -14.379 -17.923 1.00 43.62  ? 36  PRO A CA  1 
ATOM   275  C C   . PRO A 1 37 ? -1.739  -12.938 -17.465 1.00 45.37  ? 36  PRO A C   1 
ATOM   276  O O   . PRO A 1 37 ? -1.089  -12.515 -16.491 1.00 42.81  ? 36  PRO A O   1 
ATOM   277  C CB  . PRO A 1 37 ? -2.816  -15.217 -17.516 1.00 42.08  ? 36  PRO A CB  1 
ATOM   278  C CG  . PRO A 1 37 ? -2.261  -16.507 -16.985 1.00 38.17  ? 36  PRO A CG  1 
ATOM   279  C CD  . PRO A 1 37 ? -0.794  -16.277 -16.616 1.00 41.10  ? 36  PRO A CD  1 
ATOM   280  N N   . PRO A 1 38 ? -2.600  -12.179 -18.189 1.00 46.90  ? 37  PRO A N   1 
ATOM   281  C CA  . PRO A 1 38 ? -3.071  -10.859 -17.760 1.00 50.27  ? 37  PRO A CA  1 
ATOM   282  C C   . PRO A 1 38 ? -3.598  -10.866 -16.329 1.00 43.12  ? 37  PRO A C   1 
ATOM   283  O O   . PRO A 1 38 ? -4.333  -11.761 -15.924 1.00 52.70  ? 37  PRO A O   1 
ATOM   284  C CB  . PRO A 1 38 ? -4.222  -10.500 -18.747 1.00 50.76  ? 37  PRO A CB  1 
ATOM   285  C CG  . PRO A 1 38 ? -4.094  -11.461 -19.911 1.00 53.78  ? 37  PRO A CG  1 
ATOM   286  C CD  . PRO A 1 38 ? -3.162  -12.592 -19.494 1.00 52.49  ? 37  PRO A CD  1 
ATOM   287  N N   . ASN A 1 39 ? -3.205  -9.864  -15.552 1.00 45.67  ? 38  ASN A N   1 
ATOM   288  C CA  . ASN A 1 39 ? -3.792  -9.656  -14.237 1.00 50.19  ? 38  ASN A CA  1 
ATOM   289  C C   . ASN A 1 39 ? -3.300  -10.689 -13.224 1.00 47.50  ? 38  ASN A C   1 
ATOM   290  O O   . ASN A 1 39 ? -3.757  -10.661 -12.089 1.00 45.47  ? 38  ASN A O   1 
ATOM   291  C CB  . ASN A 1 39 ? -5.315  -9.571  -14.294 1.00 54.62  ? 38  ASN A CB  1 
ATOM   292  C CG  . ASN A 1 39 ? -5.764  -8.337  -15.044 1.00 56.23  ? 38  ASN A CG  1 
ATOM   293  O OD1 . ASN A 1 39 ? -5.712  -7.216  -14.516 1.00 56.62  ? 38  ASN A OD1 1 
ATOM   294  N ND2 . ASN A 1 39 ? -6.170  -8.531  -16.287 1.00 53.92  ? 38  ASN A ND2 1 
ATOM   295  N N   . LYS A 1 40 ? -2.340  -11.544 -13.614 1.00 44.47  ? 39  LYS A N   1 
ATOM   296  C CA  . LYS A 1 40 ? -1.784  -12.542 -12.705 1.00 39.88  ? 39  LYS A CA  1 
ATOM   297  C C   . LYS A 1 40 ? -0.300  -12.260 -12.472 1.00 36.46  ? 39  LYS A C   1 
ATOM   298  O O   . LYS A 1 40 ? 0.350   -11.644 -13.326 1.00 32.88  ? 39  LYS A O   1 
ATOM   299  C CB  . LYS A 1 40 ? -2.041  -13.969 -13.214 1.00 42.06  ? 39  LYS A CB  1 
ATOM   300  C CG  . LYS A 1 40 ? -3.507  -14.365 -13.380 1.00 44.69  ? 39  LYS A CG  1 
ATOM   301  C CD  . LYS A 1 40 ? -4.374  -14.013 -12.174 1.00 50.68  ? 39  LYS A CD  1 
ATOM   302  C CE  . LYS A 1 40 ? -5.866  -14.161 -12.388 1.00 51.07  ? 39  LYS A CE  1 
ATOM   303  N NZ  . LYS A 1 40 ? -6.151  -15.588 -12.508 1.00 46.28  ? 39  LYS A NZ  1 
ATOM   304  N N   . TYR A 1 41 ? 0.214   -12.732 -11.324 1.00 29.25  ? 40  TYR A N   1 
ATOM   305  C CA  . TYR A 1 41 ? 1.632   -12.600 -10.965 1.00 30.04  ? 40  TYR A CA  1 
ATOM   306  C C   . TYR A 1 41 ? 2.235   -13.982 -10.847 1.00 29.67  ? 40  TYR A C   1 
ATOM   307  O O   . TYR A 1 41 ? 1.521   -14.893 -10.418 1.00 33.28  ? 40  TYR A O   1 
ATOM   308  C CB  . TYR A 1 41 ? 1.801   -11.996 -9.552  1.00 28.94  ? 40  TYR A CB  1 
ATOM   309  C CG  . TYR A 1 41 ? 1.322   -10.561 -9.513  1.00 32.96  ? 40  TYR A CG  1 
ATOM   310  C CD1 . TYR A 1 41 ? -0.039  -10.258 -9.438  1.00 43.76  ? 40  TYR A CD1 1 
ATOM   311  C CD2 . TYR A 1 41 ? 2.215   -9.501  -9.630  1.00 37.00  ? 40  TYR A CD2 1 
ATOM   312  C CE1 . TYR A 1 41 ? -0.491  -8.945  -9.461  1.00 38.67  ? 40  TYR A CE1 1 
ATOM   313  C CE2 . TYR A 1 41 ? 1.785   -8.185  -9.616  1.00 39.35  ? 40  TYR A CE2 1 
ATOM   314  C CZ  . TYR A 1 41 ? 0.426   -7.912  -9.547  1.00 45.52  ? 40  TYR A CZ  1 
ATOM   315  O OH  . TYR A 1 41 ? -0.015  -6.617  -9.589  1.00 44.17  ? 40  TYR A OH  1 
ATOM   316  N N   . PRO A 1 42 ? 3.564   -14.169 -11.090 1.00 28.80  ? 41  PRO A N   1 
ATOM   317  C CA  . PRO A 1 42 ? 4.210   -15.463 -10.891 1.00 25.66  ? 41  PRO A CA  1 
ATOM   318  C C   . PRO A 1 42 ? 4.511   -15.636 -9.402  1.00 26.98  ? 41  PRO A C   1 
ATOM   319  O O   . PRO A 1 42 ? 5.191   -14.807 -8.797  1.00 31.42  ? 41  PRO A O   1 
ATOM   320  C CB  . PRO A 1 42 ? 5.501   -15.411 -11.740 1.00 27.87  ? 41  PRO A CB  1 
ATOM   321  C CG  . PRO A 1 42 ? 5.695   -13.968 -12.060 1.00 28.47  ? 41  PRO A CG  1 
ATOM   322  C CD  . PRO A 1 42 ? 4.519   -13.125 -11.507 1.00 32.63  ? 41  PRO A CD  1 
ATOM   323  N N   . ILE A 1 43 ? 3.967   -16.679 -8.766  1.00 28.40  ? 42  ILE A N   1 
ATOM   324  C CA  . ILE A 1 43 ? 4.118   -16.789 -7.310  1.00 25.86  ? 42  ILE A CA  1 
ATOM   325  C C   . ILE A 1 43 ? 5.036   -17.972 -7.031  1.00 29.27  ? 42  ILE A C   1 
ATOM   326  O O   . ILE A 1 43 ? 4.787   -19.089 -7.487  1.00 29.16  ? 42  ILE A O   1 
ATOM   327  C CB  . ILE A 1 43 ? 2.759   -16.926 -6.580  1.00 29.85  ? 42  ILE A CB  1 
ATOM   328  C CG1 . ILE A 1 43 ? 1.743   -15.773 -6.940  1.00 28.89  ? 42  ILE A CG1 1 
ATOM   329  C CG2 . ILE A 1 43 ? 2.936   -17.138 -5.053  1.00 25.98  ? 42  ILE A CG2 1 
ATOM   330  C CD1 . ILE A 1 43 ? 2.200   -14.337 -6.624  1.00 29.28  ? 42  ILE A CD1 1 
ATOM   331  N N   . PHE A 1 44 ? 6.179   -17.696 -6.392  1.00 26.27  ? 43  PHE A N   1 
ATOM   332  C CA  . PHE A 1 44 ? 7.090   -18.748 -6.016  1.00 24.99  ? 43  PHE A CA  1 
ATOM   333  C C   . PHE A 1 44 ? 6.736   -19.135 -4.575  1.00 28.46  ? 43  PHE A C   1 
ATOM   334  O O   . PHE A 1 44 ? 6.751   -18.278 -3.677  1.00 28.71  ? 43  PHE A O   1 
ATOM   335  C CB  . PHE A 1 44 ? 8.546   -18.270 -6.153  1.00 26.40  ? 43  PHE A CB  1 
ATOM   336  C CG  . PHE A 1 44 ? 9.583   -19.307 -5.706  1.00 31.25  ? 43  PHE A CG  1 
ATOM   337  C CD1 . PHE A 1 44 ? 9.966   -20.368 -6.547  1.00 31.33  ? 43  PHE A CD1 1 
ATOM   338  C CD2 . PHE A 1 44 ? 10.141  -19.245 -4.430  1.00 30.95  ? 43  PHE A CD2 1 
ATOM   339  C CE1 . PHE A 1 44 ? 10.908  -21.302 -6.123  1.00 33.26  ? 43  PHE A CE1 1 
ATOM   340  C CE2 . PHE A 1 44 ? 11.101  -20.171 -4.021  1.00 37.42  ? 43  PHE A CE2 1 
ATOM   341  C CZ  . PHE A 1 44 ? 11.499  -21.184 -4.880  1.00 31.52  ? 43  PHE A CZ  1 
ATOM   342  N N   . PHE A 1 45 ? 6.371   -20.401 -4.363  1.00 32.04  ? 44  PHE A N   1 
ATOM   343  C CA  . PHE A 1 45 ? 6.015   -20.838 -3.016  1.00 28.52  ? 44  PHE A CA  1 
ATOM   344  C C   . PHE A 1 45 ? 7.274   -21.422 -2.377  1.00 33.34  ? 44  PHE A C   1 
ATOM   345  O O   . PHE A 1 45 ? 7.911   -22.355 -2.938  1.00 28.64  ? 44  PHE A O   1 
ATOM   346  C CB  . PHE A 1 45 ? 5.012   -21.994 -3.223  1.00 33.47  ? 44  PHE A CB  1 
ATOM   347  C CG  . PHE A 1 45 ? 3.624   -21.527 -3.654  1.00 35.86  ? 44  PHE A CG  1 
ATOM   348  C CD1 . PHE A 1 45 ? 3.315   -21.330 -5.014  1.00 36.44  ? 44  PHE A CD1 1 
ATOM   349  C CD2 . PHE A 1 45 ? 2.638   -21.270 -2.703  1.00 34.03  ? 44  PHE A CD2 1 
ATOM   350  C CE1 . PHE A 1 45 ? 2.062   -20.863 -5.412  1.00 34.06  ? 44  PHE A CE1 1 
ATOM   351  C CE2 . PHE A 1 45 ? 1.385   -20.803 -3.098  1.00 31.10  ? 44  PHE A CE2 1 
ATOM   352  C CZ  . PHE A 1 45 ? 1.107   -20.579 -4.446  1.00 34.04  ? 44  PHE A CZ  1 
ATOM   353  N N   . PHE A 1 46 ? 7.641   -20.858 -1.221  1.00 29.13  ? 45  PHE A N   1 
ATOM   354  C CA  . PHE A 1 46 ? 8.761   -21.348 -0.435  1.00 31.57  ? 45  PHE A CA  1 
ATOM   355  C C   . PHE A 1 46 ? 8.453   -22.780 0.002   1.00 29.67  ? 45  PHE A C   1 
ATOM   356  O O   . PHE A 1 46 ? 7.283   -23.172 0.178   1.00 30.06  ? 45  PHE A O   1 
ATOM   357  C CB  . PHE A 1 46 ? 9.104   -20.456 0.783   1.00 31.16  ? 45  PHE A CB  1 
ATOM   358  C CG  . PHE A 1 46 ? 9.543   -19.051 0.367   1.00 29.66  ? 45  PHE A CG  1 
ATOM   359  C CD1 . PHE A 1 46 ? 10.776  -18.829 -0.268  1.00 25.11  ? 45  PHE A CD1 1 
ATOM   360  C CD2 . PHE A 1 46 ? 8.729   -17.948 0.609   1.00 26.90  ? 45  PHE A CD2 1 
ATOM   361  C CE1 . PHE A 1 46 ? 11.152  -17.550 -0.690  1.00 24.57  ? 45  PHE A CE1 1 
ATOM   362  C CE2 . PHE A 1 46 ? 9.100   -16.676 0.165   1.00 30.43  ? 45  PHE A CE2 1 
ATOM   363  C CZ  . PHE A 1 46 ? 10.344  -16.447 -0.429  1.00 27.05  ? 45  PHE A CZ  1 
ATOM   364  N N   . GLY A 1 47 ? 9.533   -23.549 0.162   1.00 27.29  ? 46  GLY A N   1 
ATOM   365  C CA  . GLY A 1 47 ? 9.469   -24.912 0.656   1.00 32.38  ? 46  GLY A CA  1 
ATOM   366  C C   . GLY A 1 47 ? 9.246   -25.923 -0.475  1.00 37.39  ? 46  GLY A C   1 
ATOM   367  O O   . GLY A 1 47 ? 10.037  -26.844 -0.634  1.00 36.31  ? 46  GLY A O   1 
ATOM   368  N N   . THR A 1 48 ? 8.179   -25.753 -1.269  1.00 33.27  ? 47  THR A N   1 
ATOM   369  C CA  . THR A 1 48 ? 7.906   -26.708 -2.336  1.00 37.08  ? 47  THR A CA  1 
ATOM   370  C C   . THR A 1 48 ? 8.658   -26.281 -3.591  1.00 37.11  ? 47  THR A C   1 
ATOM   371  O O   . THR A 1 48 ? 8.908   -27.091 -4.503  1.00 35.96  ? 47  THR A O   1 
ATOM   372  C CB  . THR A 1 48 ? 6.412   -26.774 -2.625  1.00 36.12  ? 47  THR A CB  1 
ATOM   373  O OG1 . THR A 1 48 ? 6.049   -25.416 -2.844  1.00 33.27  ? 47  THR A OG1 1 
ATOM   374  C CG2 . THR A 1 48 ? 5.625   -27.347 -1.464  1.00 34.52  ? 47  THR A CG2 1 
ATOM   375  N N   . HIS A 1 49 ? 8.957   -24.974 -3.637  1.00 31.85  ? 48  HIS A N   1 
ATOM   376  C CA  . HIS A 1 49 ? 9.637   -24.345 -4.763  1.00 36.84  ? 48  HIS A CA  1 
ATOM   377  C C   . HIS A 1 49 ? 8.812   -24.409 -6.044  1.00 35.07  ? 48  HIS A C   1 
ATOM   378  O O   . HIS A 1 49 ? 9.369   -24.287 -7.147  1.00 35.67  ? 48  HIS A O   1 
ATOM   379  C CB  . HIS A 1 49 ? 11.072  -24.877 -4.936  1.00 33.95  ? 48  HIS A CB  1 
ATOM   380  C CG  . HIS A 1 49 ? 11.817  -24.889 -3.661  1.00 33.67  ? 48  HIS A CG  1 
ATOM   381  N ND1 . HIS A 1 49 ? 12.710  -25.878 -3.327  1.00 38.04  ? 48  HIS A ND1 1 
ATOM   382  C CD2 . HIS A 1 49 ? 11.771  -24.030 -2.599  1.00 31.64  ? 48  HIS A CD2 1 
ATOM   383  C CE1 . HIS A 1 49 ? 13.212  -25.614 -2.110  1.00 40.87  ? 48  HIS A CE1 1 
ATOM   384  N NE2 . HIS A 1 49 ? 12.675  -24.492 -1.671  1.00 36.18  ? 48  HIS A NE2 1 
ATOM   385  N N   . GLU A 1 50 ? 7.482   -24.472 -5.919  1.00 39.81  ? 49  GLU A N   1 
ATOM   386  C CA  . GLU A 1 50 ? 6.664   -24.484 -7.128  1.00 39.71  ? 49  GLU A CA  1 
ATOM   387  C C   . GLU A 1 50 ? 6.187   -23.080 -7.449  1.00 36.70  ? 49  GLU A C   1 
ATOM   388  O O   . GLU A 1 50 ? 6.169   -22.208 -6.571  1.00 34.41  ? 49  GLU A O   1 
ATOM   389  C CB  . GLU A 1 50 ? 5.468   -25.409 -6.920  1.00 38.94  ? 49  GLU A CB  1 
ATOM   390  C CG  . GLU A 1 50 ? 5.923   -26.808 -6.535  1.00 43.09  ? 49  GLU A CG  1 
ATOM   391  C CD  . GLU A 1 50 ? 4.732   -27.664 -6.167  1.00 53.73  ? 49  GLU A CD  1 
ATOM   392  O OE1 . GLU A 1 50 ? 3.573   -27.239 -6.370  1.00 54.33  ? 49  GLU A OE1 1 
ATOM   393  O OE2 . GLU A 1 50 ? 4.988   -28.737 -5.587  1.00 59.89  ? 49  GLU A OE2 1 
ATOM   394  N N   . THR A 1 51 ? 5.847   -22.868 -8.726  1.00 29.92  ? 50  THR A N   1 
ATOM   395  C CA  . THR A 1 51 ? 5.249   -21.610 -9.147  1.00 32.00  ? 50  THR A CA  1 
ATOM   396  C C   . THR A 1 51 ? 3.781   -21.821 -9.533  1.00 32.81  ? 50  THR A C   1 
ATOM   397  O O   . THR A 1 51 ? 3.473   -22.781 -10.246 1.00 37.69  ? 50  THR A O   1 
ATOM   398  C CB  . THR A 1 51 ? 6.057   -21.068 -10.329 1.00 38.37  ? 50  THR A CB  1 
ATOM   399  O OG1 . THR A 1 51 ? 7.361   -20.695 -9.875  1.00 30.97  ? 50  THR A OG1 1 
ATOM   400  C CG2 . THR A 1 51 ? 5.387   -19.860 -10.970 1.00 35.50  ? 50  THR A CG2 1 
ATOM   401  N N   . ALA A 1 52 ? 2.885   -20.900 -9.125  1.00 32.58  ? 51  ALA A N   1 
ATOM   402  C CA  . ALA A 1 52 ? 1.597   -20.750 -9.804  1.00 33.34  ? 51  ALA A CA  1 
ATOM   403  C C   . ALA A 1 52 ? 1.331   -19.279 -10.105 1.00 34.56  ? 51  ALA A C   1 
ATOM   404  O O   . ALA A 1 52 ? 2.060   -18.397 -9.652  1.00 31.98  ? 51  ALA A O   1 
ATOM   405  C CB  . ALA A 1 52 ? 0.434   -21.397 -9.041  1.00 32.71  ? 51  ALA A CB  1 
ATOM   406  N N   . PHE A 1 53 ? 0.277   -19.037 -10.891 1.00 31.06  ? 52  PHE A N   1 
ATOM   407  C CA  . PHE A 1 53 ? -0.082  -17.705 -11.317 1.00 32.01  ? 52  PHE A CA  1 
ATOM   408  C C   . PHE A 1 53 ? -1.326  -17.322 -10.530 1.00 38.19  ? 52  PHE A C   1 
ATOM   409  O O   . PHE A 1 53 ? -2.354  -17.993 -10.626 1.00 38.71  ? 52  PHE A O   1 
ATOM   410  C CB  . PHE A 1 53 ? -0.376  -17.703 -12.824 1.00 36.76  ? 52  PHE A CB  1 
ATOM   411  C CG  . PHE A 1 53 ? 0.813   -18.082 -13.697 1.00 38.67  ? 52  PHE A CG  1 
ATOM   412  C CD1 . PHE A 1 53 ? 2.060   -17.502 -13.500 1.00 37.53  ? 52  PHE A CD1 1 
ATOM   413  C CD2 . PHE A 1 53 ? 0.667   -18.992 -14.743 1.00 41.77  ? 52  PHE A CD2 1 
ATOM   414  C CE1 . PHE A 1 53 ? 3.147   -17.863 -14.289 1.00 48.74  ? 52  PHE A CE1 1 
ATOM   415  C CE2 . PHE A 1 53 ? 1.755   -19.334 -15.538 1.00 42.39  ? 52  PHE A CE2 1 
ATOM   416  C CZ  . PHE A 1 53 ? 2.995   -18.785 -15.314 1.00 40.24  ? 52  PHE A CZ  1 
ATOM   417  N N   . LEU A 1 54 ? -1.231  -16.231 -9.771  1.00 36.74  ? 53  LEU A N   1 
ATOM   418  C CA  . LEU A 1 54 ? -2.343  -15.828 -8.923  1.00 34.94  ? 53  LEU A CA  1 
ATOM   419  C C   . LEU A 1 54 ? -2.583  -14.328 -9.011  1.00 35.10  ? 53  LEU A C   1 
ATOM   420  O O   . LEU A 1 54 ? -1.666  -13.565 -9.322  1.00 33.51  ? 53  LEU A O   1 
ATOM   421  C CB  . LEU A 1 54 ? -2.009  -16.172 -7.472  1.00 30.06  ? 53  LEU A CB  1 
ATOM   422  C CG  . LEU A 1 54 ? -1.826  -17.644 -7.125  1.00 29.11  ? 53  LEU A CG  1 
ATOM   423  C CD1 . LEU A 1 54 ? -1.530  -17.512 -5.623  1.00 29.65  ? 53  LEU A CD1 1 
ATOM   424  C CD2 . LEU A 1 54 ? -3.134  -18.362 -7.354  1.00 33.34  ? 53  LEU A CD2 1 
ATOM   425  N N   . GLY A 1 55 ? -3.845  -13.935 -8.733  1.00 31.53  ? 54  GLY A N   1 
ATOM   426  C CA  . GLY A 1 55 ? -4.229  -12.546 -8.657  1.00 26.69  ? 54  GLY A CA  1 
ATOM   427  C C   . GLY A 1 55 ? -4.179  -12.085 -7.191  1.00 30.12  ? 54  GLY A C   1 
ATOM   428  O O   . GLY A 1 55 ? -4.102  -12.905 -6.263  1.00 30.42  ? 54  GLY A O   1 
ATOM   429  N N   . PRO A 1 56 ? -4.207  -10.754 -6.995  1.00 29.25  ? 55  PRO A N   1 
ATOM   430  C CA  . PRO A 1 56 ? -4.171  -10.114 -5.670  1.00 26.07  ? 55  PRO A CA  1 
ATOM   431  C C   . PRO A 1 56 ? -5.130  -10.683 -4.627  1.00 28.99  ? 55  PRO A C   1 
ATOM   432  O O   . PRO A 1 56 ? -4.805  -10.772 -3.429  1.00 27.31  ? 55  PRO A O   1 
ATOM   433  C CB  . PRO A 1 56 ? -4.486  -8.655  -5.995  1.00 30.80  ? 55  PRO A CB  1 
ATOM   434  C CG  . PRO A 1 56 ? -3.957  -8.475  -7.406  1.00 34.04  ? 55  PRO A CG  1 
ATOM   435  C CD  . PRO A 1 56 ? -4.217  -9.798  -8.117  1.00 25.42  ? 55  PRO A CD  1 
ATOM   436  N N   . LYS A 1 57 ? -6.318  -11.092 -5.075  1.00 27.69  ? 56  LYS A N   1 
ATOM   437  C CA  . LYS A 1 57 ? -7.283  -11.631 -4.121  1.00 31.58  ? 56  LYS A CA  1 
ATOM   438  C C   . LYS A 1 57 ? -6.698  -12.788 -3.309  1.00 34.06  ? 56  LYS A C   1 
ATOM   439  O O   . LYS A 1 57 ? -7.134  -13.055 -2.195  1.00 30.51  ? 56  LYS A O   1 
ATOM   440  C CB  . LYS A 1 57 ? -8.575  -12.169 -4.749  1.00 37.05  ? 56  LYS A CB  1 
ATOM   441  C CG  . LYS A 1 57 ? -8.405  -13.423 -5.602  1.00 38.40  ? 56  LYS A CG  1 
ATOM   442  C CD  . LYS A 1 57 ? -9.756  -13.865 -6.184  1.00 45.68  ? 56  LYS A CD  1 
ATOM   443  C CE  . LYS A 1 57 ? -9.641  -15.069 -7.065  1.00 40.39  ? 56  LYS A CE  1 
ATOM   444  N NZ  . LYS A 1 57 ? -9.370  -16.279 -6.260  1.00 52.66  ? 56  LYS A NZ  1 
ATOM   445  N N   . ASP A 1 58 ? -5.705  -13.494 -3.848  1.00 31.36  ? 57  ASP A N   1 
ATOM   446  C CA  . ASP A 1 58 ? -5.186  -14.625 -3.129  1.00 26.68  ? 57  ASP A CA  1 
ATOM   447  C C   . ASP A 1 58 ? -3.847  -14.328 -2.440  1.00 29.41  ? 57  ASP A C   1 
ATOM   448  O O   . ASP A 1 58 ? -3.203  -15.272 -1.971  1.00 35.28  ? 57  ASP A O   1 
ATOM   449  C CB  . ASP A 1 58 ? -5.085  -15.804 -4.079  1.00 30.23  ? 57  ASP A CB  1 
ATOM   450  C CG  . ASP A 1 58 ? -6.455  -16.343 -4.451  1.00 37.71  ? 57  ASP A CG  1 
ATOM   451  O OD1 . ASP A 1 58 ? -7.347  -16.290 -3.566  1.00 38.08  ? 57  ASP A OD1 1 
ATOM   452  O OD2 . ASP A 1 58 ? -6.638  -16.723 -5.618  1.00 32.20  ? 57  ASP A OD2 1 
ATOM   453  N N   . LEU A 1 59 ? -3.447  -13.056 -2.371  1.00 25.90  ? 58  LEU A N   1 
ATOM   454  C CA  . LEU A 1 59 ? -2.112  -12.626 -1.951  1.00 24.82  ? 58  LEU A CA  1 
ATOM   455  C C   . LEU A 1 59 ? -2.210  -11.763 -0.692  1.00 24.72  ? 58  LEU A C   1 
ATOM   456  O O   . LEU A 1 59 ? -2.798  -10.682 -0.731  1.00 29.89  ? 58  LEU A O   1 
ATOM   457  C CB  . LEU A 1 59 ? -1.470  -11.834 -3.096  1.00 22.92  ? 58  LEU A CB  1 
ATOM   458  C CG  . LEU A 1 59 ? -1.267  -12.582 -4.419  1.00 23.61  ? 58  LEU A CG  1 
ATOM   459  C CD1 . LEU A 1 59 ? -0.532  -11.786 -5.430  1.00 27.53  ? 58  LEU A CD1 1 
ATOM   460  C CD2 . LEU A 1 59 ? -0.512  -13.889 -4.194  1.00 25.73  ? 58  LEU A CD2 1 
ATOM   461  N N   . PHE A 1 60 ? -1.636  -12.255 0.406   1.00 27.56  ? 59  PHE A N   1 
ATOM   462  C CA  . PHE A 1 60 ? -1.687  -11.571 1.702   1.00 28.70  ? 59  PHE A CA  1 
ATOM   463  C C   . PHE A 1 60 ? -0.288  -11.136 2.110   1.00 27.67  ? 59  PHE A C   1 
ATOM   464  O O   . PHE A 1 60 ? 0.576   -11.964 2.431   1.00 32.78  ? 59  PHE A O   1 
ATOM   465  C CB  . PHE A 1 60 ? -2.172  -12.584 2.743   1.00 26.65  ? 59  PHE A CB  1 
ATOM   466  C CG  . PHE A 1 60 ? -3.620  -13.016 2.494   1.00 31.36  ? 59  PHE A CG  1 
ATOM   467  C CD1 . PHE A 1 60 ? -3.929  -14.032 1.587   1.00 30.99  ? 59  PHE A CD1 1 
ATOM   468  C CD2 . PHE A 1 60 ? -4.670  -12.406 3.177   1.00 31.29  ? 59  PHE A CD2 1 
ATOM   469  C CE1 . PHE A 1 60 ? -5.247  -14.414 1.366   1.00 40.56  ? 59  PHE A CE1 1 
ATOM   470  C CE2 . PHE A 1 60 ? -5.993  -12.812 2.965   1.00 32.57  ? 59  PHE A CE2 1 
ATOM   471  C CZ  . PHE A 1 60 ? -6.284  -13.803 2.056   1.00 30.76  ? 59  PHE A CZ  1 
ATOM   472  N N   . PRO A 1 61 ? -0.027  -9.823  2.127   1.00 33.01  ? 60  PRO A N   1 
ATOM   473  C CA  . PRO A 1 61 ? 1.278   -9.306  2.584   1.00 31.31  ? 60  PRO A CA  1 
ATOM   474  C C   . PRO A 1 61 ? 1.799   -9.935  3.876   1.00 31.37  ? 60  PRO A C   1 
ATOM   475  O O   . PRO A 1 61 ? 1.099   -9.977  4.875   1.00 27.99  ? 60  PRO A O   1 
ATOM   476  C CB  . PRO A 1 61 ? 0.925   -7.827  2.777   1.00 36.83  ? 60  PRO A CB  1 
ATOM   477  C CG  . PRO A 1 61 ? -0.044  -7.556  1.608   1.00 36.88  ? 60  PRO A CG  1 
ATOM   478  C CD  . PRO A 1 61 ? -0.935  -8.788  1.592   1.00 32.75  ? 60  PRO A CD  1 
ATOM   479  N N   . TYR A 1 62 ? 3.077   -10.341 3.851   1.00 30.35  ? 61  TYR A N   1 
ATOM   480  C CA  . TYR A 1 62 ? 3.681   -11.215 4.843   1.00 31.80  ? 61  TYR A CA  1 
ATOM   481  C C   . TYR A 1 62 ? 3.738   -10.529 6.212   1.00 28.16  ? 61  TYR A C   1 
ATOM   482  O O   . TYR A 1 62 ? 3.329   -11.138 7.200   1.00 36.32  ? 61  TYR A O   1 
ATOM   483  C CB  . TYR A 1 62 ? 5.086   -11.570 4.335   1.00 34.13  ? 61  TYR A CB  1 
ATOM   484  C CG  . TYR A 1 62 ? 5.888   -12.321 5.397   1.00 32.83  ? 61  TYR A CG  1 
ATOM   485  C CD1 . TYR A 1 62 ? 5.572   -13.642 5.726   1.00 33.63  ? 61  TYR A CD1 1 
ATOM   486  C CD2 . TYR A 1 62 ? 6.921   -11.701 6.111   1.00 36.43  ? 61  TYR A CD2 1 
ATOM   487  C CE1 . TYR A 1 62 ? 6.265   -14.349 6.702   1.00 32.20  ? 61  TYR A CE1 1 
ATOM   488  C CE2 . TYR A 1 62 ? 7.642   -12.408 7.074   1.00 31.88  ? 61  TYR A CE2 1 
ATOM   489  C CZ  . TYR A 1 62 ? 7.307   -13.719 7.373   1.00 36.63  ? 61  TYR A CZ  1 
ATOM   490  O OH  . TYR A 1 62 ? 8.001   -14.425 8.327   1.00 50.43  ? 61  TYR A OH  1 
ATOM   491  N N   . ASP A 1 63 ? 4.222   -9.285  6.244   1.00 29.70  ? 62  ASP A N   1 
ATOM   492  C CA  . ASP A 1 63 ? 4.324   -8.556  7.507   1.00 40.95  ? 62  ASP A CA  1 
ATOM   493  C C   . ASP A 1 63 ? 3.002   -8.605  8.269   1.00 41.08  ? 62  ASP A C   1 
ATOM   494  O O   . ASP A 1 63 ? 2.905   -9.227  9.328   1.00 41.97  ? 62  ASP A O   1 
ATOM   495  C CB  . ASP A 1 63 ? 5.018   -7.213  7.352   1.00 45.30  ? 62  ASP A CB  1 
ATOM   496  C CG  . ASP A 1 63 ? 6.519   -7.292  7.640   1.00 71.07  ? 62  ASP A CG  1 
ATOM   497  O OD1 . ASP A 1 63 ? 7.226   -8.031  6.930   1.00 63.61  ? 62  ASP A OD1 1 
ATOM   498  O OD2 . ASP A 1 63 ? 6.983   -6.681  8.628   1.00 89.38  ? 62  ASP A OD2 1 
ATOM   499  N N   . LYS A 1 64 ? 1.966   -8.033  7.649   1.00 40.60  ? 63  LYS A N   1 
ATOM   500  C CA  . LYS A 1 64 ? 0.623   -7.982  8.211   1.00 43.63  ? 63  LYS A CA  1 
ATOM   501  C C   . LYS A 1 64 ? 0.074   -9.351  8.630   1.00 38.80  ? 63  LYS A C   1 
ATOM   502  O O   . LYS A 1 64 ? -0.654  -9.410  9.620   1.00 41.71  ? 63  LYS A O   1 
ATOM   503  C CB  . LYS A 1 64 ? -0.293  -7.223  7.235   1.00 40.21  ? 63  LYS A CB  1 
ATOM   504  C CG  . LYS A 1 64 ? -1.791  -7.454  7.470   1.00 48.24  ? 63  LYS A CG  1 
ATOM   505  C CD  . LYS A 1 64 ? -2.632  -6.515  6.625   1.00 45.59  ? 63  LYS A CD  1 
ATOM   506  C CE  . LYS A 1 64 ? -3.401  -5.636  7.553   1.00 49.84  ? 63  LYS A CE  1 
ATOM   507  N NZ  . LYS A 1 64 ? -4.681  -6.295  7.806   1.00 43.93  ? 63  LYS A NZ  1 
ATOM   508  N N   . SER A 1 65 ? 0.405   -10.433 7.887   1.00 37.85  ? 64  SER A N   1 
ATOM   509  C CA  . SER A 1 65 ? -0.303  -11.707 7.986   1.00 35.17  ? 64  SER A CA  1 
ATOM   510  C C   . SER A 1 65 ? 0.483   -12.746 8.778   1.00 36.14  ? 64  SER A C   1 
ATOM   511  O O   . SER A 1 65 ? -0.039  -13.830 9.037   1.00 31.74  ? 64  SER A O   1 
ATOM   512  C CB  . SER A 1 65 ? -0.638  -12.274 6.596   1.00 40.98  ? 64  SER A CB  1 
ATOM   513  O OG  . SER A 1 65 ? -1.240  -11.284 5.775   1.00 54.07  ? 64  SER A OG  1 
ATOM   514  N N   . LYS A 1 66 ? 1.751   -12.453 9.115   1.00 42.35  ? 65  LYS A N   1 
ATOM   515  C CA  . LYS A 1 66 ? 2.612   -13.507 9.645   1.00 39.47  ? 65  LYS A CA  1 
ATOM   516  C C   . LYS A 1 66 ? 2.107   -14.090 10.974  1.00 39.65  ? 65  LYS A C   1 
ATOM   517  O O   . LYS A 1 66 ? 2.217   -15.299 11.180  1.00 37.61  ? 65  LYS A O   1 
ATOM   518  C CB  . LYS A 1 66 ? 4.105   -13.152 9.687   1.00 40.97  ? 65  LYS A CB  1 
ATOM   519  C CG  . LYS A 1 66 ? 4.495   -11.965 10.526  1.00 46.91  ? 65  LYS A CG  1 
ATOM   520  C CD  . LYS A 1 66 ? 5.958   -12.180 10.903  1.00 59.64  ? 65  LYS A CD  1 
ATOM   521  C CE  . LYS A 1 66 ? 6.598   -10.909 11.373  1.00 57.56  ? 65  LYS A CE  1 
ATOM   522  N NZ  . LYS A 1 66 ? 6.766   -9.990  10.240  1.00 75.45  ? 65  LYS A NZ  1 
ATOM   523  N N   A ASP A 1 67 ? 1.563   -13.237 11.857  0.50 39.98  ? 66  ASP A N   1 
ATOM   524  N N   B ASP A 1 67 ? 1.594   -13.234 11.870  0.50 39.42  ? 66  ASP A N   1 
ATOM   525  C CA  A ASP A 1 67 ? 1.082   -13.677 13.165  0.50 42.36  ? 66  ASP A CA  1 
ATOM   526  C CA  B ASP A 1 67 ? 1.079   -13.717 13.145  0.50 41.35  ? 66  ASP A CA  1 
ATOM   527  C C   A ASP A 1 67 ? -0.078  -14.672 13.026  0.50 42.58  ? 66  ASP A C   1 
ATOM   528  C C   B ASP A 1 67 ? 0.016   -14.791 12.916  0.50 41.86  ? 66  ASP A C   1 
ATOM   529  O O   A ASP A 1 67 ? -0.203  -15.599 13.820  0.50 43.77  ? 66  ASP A O   1 
ATOM   530  O O   B ASP A 1 67 ? 0.033   -15.846 13.549  0.50 40.09  ? 66  ASP A O   1 
ATOM   531  C CB  A ASP A 1 67 ? 0.903   -12.514 14.135  0.50 40.75  ? 66  ASP A CB  1 
ATOM   532  C CB  B ASP A 1 67 ? 0.496   -12.617 14.015  0.50 39.15  ? 66  ASP A CB  1 
ATOM   533  C CG  A ASP A 1 67 ? 2.183   -11.760 14.486  0.50 44.51  ? 66  ASP A CG  1 
ATOM   534  C CG  B ASP A 1 67 ? 0.045   -13.111 15.378  0.50 44.61  ? 66  ASP A CG  1 
ATOM   535  O OD1 A ASP A 1 67 ? 3.273   -12.218 14.074  0.50 46.05  ? 66  ASP A OD1 1 
ATOM   536  O OD1 B ASP A 1 67 ? 0.934   -13.294 16.251  0.50 38.44  ? 66  ASP A OD1 1 
ATOM   537  O OD2 A ASP A 1 67 ? 2.089   -10.707 15.152  0.50 44.81  ? 66  ASP A OD2 1 
ATOM   538  O OD2 B ASP A 1 67 ? -1.174  -13.382 15.527  0.50 46.88  ? 66  ASP A OD2 1 
ATOM   539  N N   . LYS A 1 68 ? -0.900  -14.532 11.983  1.00 43.20  ? 67  LYS A N   1 
ATOM   540  C CA  . LYS A 1 68 ? -1.971  -15.485 11.747  1.00 44.54  ? 67  LYS A CA  1 
ATOM   541  C C   . LYS A 1 68 ? -1.478  -16.746 11.026  1.00 41.51  ? 67  LYS A C   1 
ATOM   542  O O   . LYS A 1 68 ? -1.879  -17.854 11.363  1.00 42.45  ? 67  LYS A O   1 
ATOM   543  C CB  . LYS A 1 68 ? -3.085  -14.791 10.964  1.00 44.05  ? 67  LYS A CB  1 
ATOM   544  C CG  . LYS A 1 68 ? -4.317  -15.627 10.732  1.00 48.14  ? 67  LYS A CG  1 
ATOM   545  C CD  . LYS A 1 68 ? -5.280  -14.629 10.089  1.00 56.07  ? 67  LYS A CD  1 
ATOM   546  C CE  . LYS A 1 68 ? -6.737  -14.952 10.224  1.00 60.55  ? 67  LYS A CE  1 
ATOM   547  N NZ  . LYS A 1 68 ? -7.588  -13.979 9.520   1.00 59.97  ? 67  LYS A NZ  1 
ATOM   548  N N   . TYR A 1 69 ? -0.659  -16.591 9.987   1.00 40.39  ? 68  TYR A N   1 
ATOM   549  C CA  . TYR A 1 69 ? -0.508  -17.671 9.010   1.00 35.04  ? 68  TYR A CA  1 
ATOM   550  C C   . TYR A 1 69 ? 0.833   -18.381 9.189   1.00 36.28  ? 68  TYR A C   1 
ATOM   551  O O   . TYR A 1 69 ? 0.995   -19.502 8.701   1.00 41.50  ? 68  TYR A O   1 
ATOM   552  C CB  . TYR A 1 69 ? -0.678  -17.199 7.558   1.00 32.25  ? 68  TYR A CB  1 
ATOM   553  C CG  . TYR A 1 69 ? -2.103  -16.769 7.216   1.00 36.10  ? 68  TYR A CG  1 
ATOM   554  C CD1 . TYR A 1 69 ? -3.226  -17.532 7.595   1.00 38.92  ? 68  TYR A CD1 1 
ATOM   555  C CD2 . TYR A 1 69 ? -2.332  -15.607 6.475   1.00 35.91  ? 68  TYR A CD2 1 
ATOM   556  C CE1 . TYR A 1 69 ? -4.523  -17.144 7.250   1.00 38.22  ? 68  TYR A CE1 1 
ATOM   557  C CE2 . TYR A 1 69 ? -3.625  -15.214 6.127   1.00 35.43  ? 68  TYR A CE2 1 
ATOM   558  C CZ  . TYR A 1 69 ? -4.721  -15.974 6.520   1.00 41.03  ? 68  TYR A CZ  1 
ATOM   559  O OH  . TYR A 1 69 ? -5.975  -15.531 6.154   1.00 40.58  ? 68  TYR A OH  1 
ATOM   560  N N   . GLY A 1 70 ? 1.758   -17.743 9.909   1.00 31.62  ? 69  GLY A N   1 
ATOM   561  C CA  . GLY A 1 70 ? 3.127   -18.239 10.002  1.00 36.18  ? 69  GLY A CA  1 
ATOM   562  C C   . GLY A 1 70 ? 3.312   -19.178 11.203  1.00 36.33  ? 69  GLY A C   1 
ATOM   563  O O   . GLY A 1 70 ? 4.008   -18.853 12.132  1.00 40.23  ? 69  GLY A O   1 
ATOM   564  N N   . LYS A 1 71 ? 2.626   -20.317 11.188  1.00 38.26  ? 70  LYS A N   1 
ATOM   565  C CA  . LYS A 1 71 ? 2.695   -21.342 12.212  1.00 43.14  ? 70  LYS A CA  1 
ATOM   566  C C   . LYS A 1 71 ? 2.943   -22.649 11.467  1.00 46.84  ? 70  LYS A C   1 
ATOM   567  O O   . LYS A 1 71 ? 2.605   -22.746 10.275  1.00 35.60  ? 70  LYS A O   1 
ATOM   568  C CB  . LYS A 1 71 ? 1.425   -21.327 13.076  1.00 45.59  ? 70  LYS A CB  1 
ATOM   569  C CG  . LYS A 1 71 ? 1.252   -19.997 13.823  1.00 52.67  ? 70  LYS A CG  1 
ATOM   570  C CD  . LYS A 1 71 ? -0.058  -19.715 14.563  1.00 59.35  ? 70  LYS A CD  1 
ATOM   571  N N   . PRO A 1 72 ? 3.633   -23.624 12.107  1.00 38.63  ? 71  PRO A N   1 
ATOM   572  C CA  . PRO A 1 72 ? 3.902   -24.928 11.495  1.00 39.99  ? 71  PRO A CA  1 
ATOM   573  C C   . PRO A 1 72 ? 2.668   -25.622 10.949  1.00 39.49  ? 71  PRO A C   1 
ATOM   574  O O   . PRO A 1 72 ? 1.583   -25.450 11.461  1.00 40.93  ? 71  PRO A O   1 
ATOM   575  C CB  . PRO A 1 72 ? 4.591   -25.766 12.611  1.00 45.63  ? 71  PRO A CB  1 
ATOM   576  C CG  . PRO A 1 72 ? 5.151   -24.726 13.564  1.00 44.18  ? 71  PRO A CG  1 
ATOM   577  C CD  . PRO A 1 72 ? 4.329   -23.445 13.398  1.00 39.75  ? 71  PRO A CD  1 
ATOM   578  N N   . ASN A 1 73 ? 2.865   -26.398 9.890   1.00 38.36  ? 72  ASN A N   1 
ATOM   579  C CA  . ASN A 1 73 ? 1.774   -27.083 9.236   1.00 47.45  ? 72  ASN A CA  1 
ATOM   580  C C   . ASN A 1 73 ? 2.312   -28.445 8.811   1.00 55.49  ? 72  ASN A C   1 
ATOM   581  O O   . ASN A 1 73 ? 3.505   -28.580 8.542   1.00 56.47  ? 72  ASN A O   1 
ATOM   582  C CB  . ASN A 1 73 ? 1.233   -26.200 8.113   1.00 52.20  ? 72  ASN A CB  1 
ATOM   583  C CG  . ASN A 1 73 ? -0.045  -26.723 7.510   1.00 50.80  ? 72  ASN A CG  1 
ATOM   584  O OD1 . ASN A 1 73 ? -0.008  -27.640 6.690   1.00 61.26  ? 72  ASN A OD1 1 
ATOM   585  N ND2 . ASN A 1 73 ? -1.178  -26.142 7.869   1.00 52.55  ? 72  ASN A ND2 1 
ATOM   586  N N   . LYS A 1 74 ? 1.423   -29.438 8.755   1.00 56.32  ? 73  LYS A N   1 
ATOM   587  C CA  . LYS A 1 74 ? 1.794   -30.801 8.430   1.00 59.60  ? 73  LYS A CA  1 
ATOM   588  C C   . LYS A 1 74 ? 2.167   -30.914 6.951   1.00 56.99  ? 73  LYS A C   1 
ATOM   589  O O   . LYS A 1 74 ? 2.946   -31.785 6.582   1.00 57.54  ? 73  LYS A O   1 
ATOM   590  C CB  . LYS A 1 74 ? 0.701   -31.779 8.898   1.00 65.18  ? 73  LYS A CB  1 
ATOM   591  C CG  . LYS A 1 74 ? -0.590  -31.850 8.076   1.00 72.63  ? 73  LYS A CG  1 
ATOM   592  N N   . ARG A 1 75 ? 1.634   -30.031 6.099   1.00 50.25  ? 74  ARG A N   1 
ATOM   593  C CA  . ARG A 1 75 ? 1.741   -30.223 4.657   1.00 47.84  ? 74  ARG A CA  1 
ATOM   594  C C   . ARG A 1 75 ? 3.200   -30.210 4.194   1.00 47.14  ? 74  ARG A C   1 
ATOM   595  O O   . ARG A 1 75 ? 4.039   -29.518 4.758   1.00 41.17  ? 74  ARG A O   1 
ATOM   596  C CB  . ARG A 1 75 ? 0.831   -29.234 3.919   1.00 50.93  ? 74  ARG A CB  1 
ATOM   597  C CG  . ARG A 1 75 ? -0.616  -29.589 4.212   1.00 52.54  ? 74  ARG A CG  1 
ATOM   598  C CD  . ARG A 1 75 ? -1.038  -30.704 3.276   1.00 47.31  ? 74  ARG A CD  1 
ATOM   599  N NE  . ARG A 1 75 ? -1.897  -30.176 2.209   1.00 66.52  ? 74  ARG A NE  1 
ATOM   600  C CZ  . ARG A 1 75 ? -3.024  -29.478 2.431   1.00 70.70  ? 74  ARG A CZ  1 
ATOM   601  N NH1 . ARG A 1 75 ? -3.786  -29.143 1.403   1.00 65.69  ? 74  ARG A NH1 1 
ATOM   602  N NH2 . ARG A 1 75 ? -3.399  -29.150 3.668   1.00 69.92  ? 74  ARG A NH2 1 
ATOM   603  N N   . LYS A 1 76 ? 3.476   -30.993 3.150   1.00 45.58  ? 75  LYS A N   1 
ATOM   604  C CA  . LYS A 1 76 ? 4.817   -31.165 2.629   1.00 47.89  ? 75  LYS A CA  1 
ATOM   605  C C   . LYS A 1 76 ? 5.410   -29.822 2.212   1.00 41.11  ? 75  LYS A C   1 
ATOM   606  O O   . LYS A 1 76 ? 4.879   -29.134 1.348   1.00 39.40  ? 75  LYS A O   1 
ATOM   607  C CB  . LYS A 1 76 ? 4.738   -32.087 1.413   1.00 43.03  ? 75  LYS A CB  1 
ATOM   608  C CG  . LYS A 1 76 ? 6.057   -32.370 0.729   1.00 43.20  ? 75  LYS A CG  1 
ATOM   609  C CD  . LYS A 1 76 ? 5.952   -33.710 -0.007  1.00 50.29  ? 75  LYS A CD  1 
ATOM   610  C CE  . LYS A 1 76 ? 7.272   -34.087 -0.613  1.00 56.56  ? 75  LYS A CE  1 
ATOM   611  N N   . GLY A 1 77 ? 6.564   -29.499 2.787   1.00 43.44  ? 76  GLY A N   1 
ATOM   612  C CA  . GLY A 1 77 ? 7.365   -28.376 2.329   1.00 35.47  ? 76  GLY A CA  1 
ATOM   613  C C   . GLY A 1 77 ? 7.060   -27.098 3.115   1.00 38.38  ? 76  GLY A C   1 
ATOM   614  O O   . GLY A 1 77 ? 7.808   -26.126 3.030   1.00 39.18  ? 76  GLY A O   1 
ATOM   615  N N   . PHE A 1 78 ? 5.967   -27.104 3.883   1.00 30.59  ? 77  PHE A N   1 
ATOM   616  C CA  . PHE A 1 78 ? 5.473   -25.890 4.512   1.00 32.80  ? 77  PHE A CA  1 
ATOM   617  C C   . PHE A 1 78 ? 6.493   -25.328 5.504   1.00 35.97  ? 77  PHE A C   1 
ATOM   618  O O   . PHE A 1 78 ? 6.781   -24.119 5.517   1.00 32.87  ? 77  PHE A O   1 
ATOM   619  C CB  . PHE A 1 78 ? 4.117   -26.132 5.185   1.00 32.81  ? 77  PHE A CB  1 
ATOM   620  C CG  . PHE A 1 78 ? 3.372   -24.857 5.569   1.00 33.87  ? 77  PHE A CG  1 
ATOM   621  C CD1 . PHE A 1 78 ? 3.643   -24.199 6.764   1.00 32.08  ? 77  PHE A CD1 1 
ATOM   622  C CD2 . PHE A 1 78 ? 2.409   -24.313 4.725   1.00 33.12  ? 77  PHE A CD2 1 
ATOM   623  C CE1 . PHE A 1 78 ? 2.985   -23.031 7.113   1.00 32.60  ? 77  PHE A CE1 1 
ATOM   624  C CE2 . PHE A 1 78 ? 1.751   -23.145 5.077   1.00 32.18  ? 77  PHE A CE2 1 
ATOM   625  C CZ  . PHE A 1 78 ? 2.020   -22.512 6.277   1.00 33.08  ? 77  PHE A CZ  1 
ATOM   626  N N   . ASN A 1 79 ? 6.986   -26.188 6.391   1.00 33.18  ? 78  ASN A N   1 
ATOM   627  C CA  . ASN A 1 79 ? 7.870   -25.698 7.435   1.00 33.58  ? 78  ASN A CA  1 
ATOM   628  C C   . ASN A 1 79 ? 9.229   -25.272 6.870   1.00 36.33  ? 78  ASN A C   1 
ATOM   629  O O   . ASN A 1 79 ? 9.826   -24.297 7.358   1.00 31.55  ? 78  ASN A O   1 
ATOM   630  C CB  . ASN A 1 79 ? 8.060   -26.737 8.533   1.00 38.54  ? 78  ASN A CB  1 
ATOM   631  C CG  . ASN A 1 79 ? 6.744   -26.987 9.236   1.00 47.34  ? 78  ASN A CG  1 
ATOM   632  O OD1 . ASN A 1 79 ? 5.868   -26.120 9.224   1.00 39.07  ? 78  ASN A OD1 1 
ATOM   633  N ND2 . ASN A 1 79 ? 6.585   -28.147 9.857   1.00 44.15  ? 78  ASN A ND2 1 
ATOM   634  N N   . GLU A 1 80 ? 9.737   -26.020 5.870   1.00 31.09  ? 79  GLU A N   1 
ATOM   635  C CA  . GLU A 1 80 ? 10.889  -25.512 5.135   1.00 36.69  ? 79  GLU A CA  1 
ATOM   636  C C   . GLU A 1 80 ? 10.564  -24.113 4.608   1.00 33.51  ? 79  GLU A C   1 
ATOM   637  O O   . GLU A 1 80 ? 11.431  -23.230 4.615   1.00 31.96  ? 79  GLU A O   1 
ATOM   638  C CB  . GLU A 1 80 ? 11.295  -26.381 3.939   1.00 34.00  ? 79  GLU A CB  1 
ATOM   639  C CG  . GLU A 1 80 ? 12.571  -25.923 3.240   1.00 34.77  ? 79  GLU A CG  1 
ATOM   640  C CD  . GLU A 1 80 ? 13.177  -26.962 2.303   1.00 47.32  ? 79  GLU A CD  1 
ATOM   641  O OE1 . GLU A 1 80 ? 12.593  -28.048 2.158   1.00 53.02  ? 79  GLU A OE1 1 
ATOM   642  O OE2 . GLU A 1 80 ? 14.246  -26.715 1.727   1.00 54.31  ? 79  GLU A OE2 1 
ATOM   643  N N   . GLY A 1 81 ? 9.335   -23.956 4.091   1.00 37.91  ? 80  GLY A N   1 
ATOM   644  C CA  . GLY A 1 81 ? 8.877   -22.694 3.515   1.00 37.04  ? 80  GLY A CA  1 
ATOM   645  C C   . GLY A 1 81 ? 8.941   -21.550 4.531   1.00 31.45  ? 80  GLY A C   1 
ATOM   646  O O   . GLY A 1 81 ? 9.329   -20.414 4.209   1.00 28.49  ? 80  GLY A O   1 
ATOM   647  N N   . LEU A 1 82 ? 8.564   -21.859 5.770   1.00 23.45  ? 81  LEU A N   1 
ATOM   648  C CA  . LEU A 1 82 ? 8.556   -20.827 6.808   1.00 30.06  ? 81  LEU A CA  1 
ATOM   649  C C   . LEU A 1 82 ? 9.986   -20.333 7.049   1.00 31.53  ? 81  LEU A C   1 
ATOM   650  O O   . LEU A 1 82 ? 10.195  -19.147 7.315   1.00 27.42  ? 81  LEU A O   1 
ATOM   651  C CB  . LEU A 1 82 ? 7.927   -21.270 8.134   1.00 31.33  ? 81  LEU A CB  1 
ATOM   652  C CG  . LEU A 1 82 ? 6.418   -21.557 8.111   1.00 36.67  ? 81  LEU A CG  1 
ATOM   653  C CD1 . LEU A 1 82 ? 6.045   -22.214 9.452   1.00 33.34  ? 81  LEU A CD1 1 
ATOM   654  C CD2 . LEU A 1 82 ? 5.551   -20.305 7.864   1.00 34.58  ? 81  LEU A CD2 1 
ATOM   655  N N   . TRP A 1 83 ? 10.963  -21.242 6.982   1.00 31.24  ? 82  TRP A N   1 
ATOM   656  C CA  . TRP A 1 83 ? 12.346  -20.898 7.299   1.00 32.48  ? 82  TRP A CA  1 
ATOM   657  C C   . TRP A 1 83 ? 12.847  -19.997 6.173   1.00 32.35  ? 82  TRP A C   1 
ATOM   658  O O   . TRP A 1 83 ? 13.468  -18.963 6.409   1.00 33.76  ? 82  TRP A O   1 
ATOM   659  C CB  . TRP A 1 83 ? 13.206  -22.173 7.456   1.00 30.92  ? 82  TRP A CB  1 
ATOM   660  C CG  . TRP A 1 83 ? 14.667  -21.881 7.677   1.00 31.64  ? 82  TRP A CG  1 
ATOM   661  C CD1 . TRP A 1 83 ? 15.295  -21.756 8.888   1.00 35.49  ? 82  TRP A CD1 1 
ATOM   662  C CD2 . TRP A 1 83 ? 15.652  -21.589 6.669   1.00 25.05  ? 82  TRP A CD2 1 
ATOM   663  N NE1 . TRP A 1 83 ? 16.607  -21.431 8.700   1.00 30.86  ? 82  TRP A NE1 1 
ATOM   664  C CE2 . TRP A 1 83 ? 16.844  -21.299 7.350   1.00 30.77  ? 82  TRP A CE2 1 
ATOM   665  C CE3 . TRP A 1 83 ? 15.618  -21.519 5.267   1.00 29.39  ? 82  TRP A CE3 1 
ATOM   666  C CZ2 . TRP A 1 83 ? 18.016  -20.958 6.669   1.00 32.37  ? 82  TRP A CZ2 1 
ATOM   667  C CZ3 . TRP A 1 83 ? 16.770  -21.188 4.586   1.00 32.08  ? 82  TRP A CZ3 1 
ATOM   668  C CH2 . TRP A 1 83 ? 17.944  -20.873 5.295   1.00 33.16  ? 82  TRP A CH2 1 
ATOM   669  N N   . GLU A 1 84 ? 12.485  -20.346 4.927   1.00 30.19  ? 83  GLU A N   1 
ATOM   670  C CA  . GLU A 1 84 ? 12.995  -19.591 3.788   1.00 26.64  ? 83  GLU A CA  1 
ATOM   671  C C   . GLU A 1 84 ? 12.515  -18.142 3.792   1.00 28.93  ? 83  GLU A C   1 
ATOM   672  O O   . GLU A 1 84 ? 13.294  -17.218 3.540   1.00 28.65  ? 83  GLU A O   1 
ATOM   673  C CB  . GLU A 1 84 ? 12.584  -20.310 2.507   1.00 24.29  ? 83  GLU A CB  1 
ATOM   674  C CG  . GLU A 1 84 ? 13.307  -21.631 2.289   1.00 24.68  ? 83  GLU A CG  1 
ATOM   675  C CD  . GLU A 1 84 ? 12.865  -22.442 1.064   1.00 32.98  ? 83  GLU A CD  1 
ATOM   676  O OE1 . GLU A 1 84 ? 11.896  -21.967 0.438   1.00 32.23  ? 83  GLU A OE1 1 
ATOM   677  O OE2 . GLU A 1 84 ? 13.414  -23.567 0.738   1.00 28.03  ? 83  GLU A OE2 1 
ATOM   678  N N   . ILE A 1 85 ? 11.209  -17.946 4.029   1.00 30.02  ? 84  ILE A N   1 
ATOM   679  C CA  . ILE A 1 85 ? 10.632  -16.622 3.916   1.00 27.46  ? 84  ILE A CA  1 
ATOM   680  C C   . ILE A 1 85 ? 11.179  -15.749 5.056   1.00 29.98  ? 84  ILE A C   1 
ATOM   681  O O   . ILE A 1 85 ? 11.330  -14.522 4.915   1.00 28.26  ? 84  ILE A O   1 
ATOM   682  C CB  . ILE A 1 85 ? 9.089   -16.645 3.944   1.00 28.65  ? 84  ILE A CB  1 
ATOM   683  C CG1 . ILE A 1 85 ? 8.494   -15.239 3.599   1.00 29.17  ? 84  ILE A CG1 1 
ATOM   684  C CG2 . ILE A 1 85 ? 8.537   -17.170 5.296   1.00 28.23  ? 84  ILE A CG2 1 
ATOM   685  C CD1 . ILE A 1 85 ? 7.087   -15.281 2.996   1.00 25.11  ? 84  ILE A CD1 1 
ATOM   686  N N   . GLN A 1 86 ? 11.463  -16.383 6.205   1.00 30.89  ? 85  GLN A N   1 
ATOM   687  C CA  . GLN A 1 86 ? 11.946  -15.611 7.350   1.00 28.19  ? 85  GLN A CA  1 
ATOM   688  C C   . GLN A 1 86 ? 13.452  -15.335 7.204   1.00 32.97  ? 85  GLN A C   1 
ATOM   689  O O   . GLN A 1 86 ? 13.892  -14.264 7.613   1.00 35.25  ? 85  GLN A O   1 
ATOM   690  C CB  . GLN A 1 86 ? 11.634  -16.373 8.647   1.00 28.92  ? 85  GLN A CB  1 
ATOM   691  C CG  . GLN A 1 86 ? 11.996  -15.628 9.941   1.00 36.37  ? 85  GLN A CG  1 
ATOM   692  C CD  . GLN A 1 86 ? 11.391  -16.257 11.203  1.00 46.90  ? 85  GLN A CD  1 
ATOM   693  O OE1 . GLN A 1 86 ? 11.279  -17.491 11.348  1.00 43.11  ? 85  GLN A OE1 1 
ATOM   694  N NE2 . GLN A 1 86 ? 10.979  -15.416 12.149  1.00 37.12  ? 85  GLN A NE2 1 
ATOM   695  N N   . ASN A 1 87 ? 14.234  -16.318 6.690   1.00 26.96  ? 86  ASN A N   1 
ATOM   696  C CA  . ASN A 1 87 ? 15.695  -16.354 6.781   1.00 30.60  ? 86  ASN A CA  1 
ATOM   697  C C   . ASN A 1 87 ? 16.427  -16.031 5.464   1.00 33.62  ? 86  ASN A C   1 
ATOM   698  O O   . ASN A 1 87 ? 17.515  -15.436 5.542   1.00 30.89  ? 86  ASN A O   1 
ATOM   699  C CB  . ASN A 1 87 ? 16.187  -17.621 7.484   1.00 34.69  ? 86  ASN A CB  1 
ATOM   700  C CG  . ASN A 1 87 ? 15.681  -17.649 8.913   1.00 36.01  ? 86  ASN A CG  1 
ATOM   701  O OD1 . ASN A 1 87 ? 16.087  -16.810 9.719   1.00 39.74  ? 86  ASN A OD1 1 
ATOM   702  N ND2 . ASN A 1 87 ? 14.730  -18.506 9.240   1.00 32.36  ? 86  ASN A ND2 1 
ATOM   703  N N   . ASN A 1 88 ? 15.903  -16.414 4.271   1.00 31.62  ? 87  ASN A N   1 
ATOM   704  C CA  . ASN A 1 88 ? 16.548  -15.990 3.018   1.00 30.87  ? 87  ASN A CA  1 
ATOM   705  C C   . ASN A 1 88 ? 15.525  -15.894 1.887   1.00 32.02  ? 87  ASN A C   1 
ATOM   706  O O   . ASN A 1 88 ? 15.563  -16.666 0.917   1.00 30.49  ? 87  ASN A O   1 
ATOM   707  C CB  . ASN A 1 88 ? 17.698  -16.917 2.626   1.00 32.33  ? 87  ASN A CB  1 
ATOM   708  C CG  . ASN A 1 88 ? 18.780  -16.246 1.808   1.00 37.06  ? 87  ASN A CG  1 
ATOM   709  O OD1 . ASN A 1 88 ? 18.554  -15.189 1.181   1.00 33.46  ? 87  ASN A OD1 1 
ATOM   710  N ND2 . ASN A 1 88 ? 19.963  -16.871 1.776   1.00 33.96  ? 87  ASN A ND2 1 
ATOM   711  N N   . PRO A 1 89 ? 14.543  -14.966 2.004   1.00 29.75  ? 88  PRO A N   1 
ATOM   712  C CA  . PRO A 1 89 ? 13.394  -14.989 1.115   1.00 26.72  ? 88  PRO A CA  1 
ATOM   713  C C   . PRO A 1 89 ? 13.761  -14.528 -0.295  1.00 30.12  ? 88  PRO A C   1 
ATOM   714  O O   . PRO A 1 89 ? 12.978  -14.793 -1.189  1.00 27.82  ? 88  PRO A O   1 
ATOM   715  C CB  . PRO A 1 89 ? 12.371  -14.083 1.785   1.00 24.28  ? 88  PRO A CB  1 
ATOM   716  C CG  . PRO A 1 89 ? 13.246  -13.104 2.569   1.00 24.91  ? 88  PRO A CG  1 
ATOM   717  C CD  . PRO A 1 89 ? 14.479  -13.873 2.997   1.00 26.78  ? 88  PRO A CD  1 
ATOM   718  N N   . HIS A 1 90 ? 14.962  -13.930 -0.509  1.00 29.62  ? 89  HIS A N   1 
ATOM   719  C CA  . HIS A 1 90 ? 15.295  -13.369 -1.820  1.00 30.15  ? 89  HIS A CA  1 
ATOM   720  C C   . HIS A 1 90 ? 16.379  -14.179 -2.551  1.00 30.87  ? 89  HIS A C   1 
ATOM   721  O O   . HIS A 1 90 ? 16.882  -13.712 -3.581  1.00 31.83  ? 89  HIS A O   1 
ATOM   722  C CB  . HIS A 1 90 ? 15.688  -11.881 -1.696  1.00 27.86  ? 89  HIS A CB  1 
ATOM   723  C CG  . HIS A 1 90 ? 14.600  -11.047 -1.131  1.00 30.28  ? 89  HIS A CG  1 
ATOM   724  N ND1 . HIS A 1 90 ? 13.339  -10.959 -1.705  1.00 29.64  ? 89  HIS A ND1 1 
ATOM   725  C CD2 . HIS A 1 90 ? 14.589  -10.246 -0.042  1.00 29.25  ? 89  HIS A CD2 1 
ATOM   726  C CE1 . HIS A 1 90 ? 12.595  -10.114 -0.982  1.00 30.73  ? 89  HIS A CE1 1 
ATOM   727  N NE2 . HIS A 1 90 ? 13.341  -9.659  0.033   1.00 31.27  ? 89  HIS A NE2 1 
ATOM   728  N N   . ALA A 1 91 ? 16.760  -15.344 -1.989  1.00 29.01  ? 90  ALA A N   1 
ATOM   729  C CA  . ALA A 1 91 ? 17.769  -16.259 -2.498  1.00 28.26  ? 90  ALA A CA  1 
ATOM   730  C C   . ALA A 1 91 ? 17.305  -16.977 -3.758  1.00 29.65  ? 90  ALA A C   1 
ATOM   731  O O   . ALA A 1 91 ? 16.121  -17.122 -4.025  1.00 32.31  ? 90  ALA A O   1 
ATOM   732  C CB  . ALA A 1 91 ? 18.137  -17.274 -1.435  1.00 28.93  ? 90  ALA A CB  1 
ATOM   733  N N   . SER A 1 92 ? 18.276  -17.446 -4.535  1.00 33.42  ? 91  SER A N   1 
ATOM   734  C CA  . SER A 1 92 ? 17.972  -18.315 -5.660  1.00 36.01  ? 91  SER A CA  1 
ATOM   735  C C   . SER A 1 92 ? 17.687  -19.719 -5.124  1.00 37.71  ? 91  SER A C   1 
ATOM   736  O O   . SER A 1 92 ? 18.496  -20.269 -4.369  1.00 43.61  ? 91  SER A O   1 
ATOM   737  C CB  . SER A 1 92 ? 19.133  -18.299 -6.613  1.00 37.72  ? 91  SER A CB  1 
ATOM   738  O OG  . SER A 1 92 ? 19.059  -19.480 -7.381  1.00 45.10  ? 91  SER A OG  1 
ATOM   739  N N   . TYR A 1 93 ? 16.480  -20.242 -5.388  1.00 31.27  ? 92  TYR A N   1 
ATOM   740  C CA  . TYR A 1 93 ? 16.147  -21.611 -5.008  1.00 38.01  ? 92  TYR A CA  1 
ATOM   741  C C   . TYR A 1 93 ? 16.076  -22.523 -6.244  1.00 43.79  ? 92  TYR A C   1 
ATOM   742  O O   . TYR A 1 93 ? 15.470  -23.590 -6.177  1.00 49.95  ? 92  TYR A O   1 
ATOM   743  C CB  . TYR A 1 93 ? 14.837  -21.731 -4.205  1.00 32.34  ? 92  TYR A CB  1 
ATOM   744  C CG  . TYR A 1 93 ? 14.934  -21.097 -2.826  1.00 30.54  ? 92  TYR A CG  1 
ATOM   745  C CD1 . TYR A 1 93 ? 15.359  -21.848 -1.718  1.00 32.14  ? 92  TYR A CD1 1 
ATOM   746  C CD2 . TYR A 1 93 ? 14.660  -19.747 -2.637  1.00 33.17  ? 92  TYR A CD2 1 
ATOM   747  C CE1 . TYR A 1 93 ? 15.520  -21.244 -0.474  1.00 36.44  ? 92  TYR A CE1 1 
ATOM   748  C CE2 . TYR A 1 93 ? 14.752  -19.152 -1.385  1.00 33.46  ? 92  TYR A CE2 1 
ATOM   749  C CZ  . TYR A 1 93 ? 15.218  -19.898 -0.309  1.00 29.80  ? 92  TYR A CZ  1 
ATOM   750  O OH  . TYR A 1 93 ? 15.366  -19.303 0.912   1.00 31.10  ? 92  TYR A OH  1 
ATOM   751  N N   . SER A 1 94 ? 16.700  -22.122 -7.355  1.00 54.31  ? 93  SER A N   1 
ATOM   752  C CA  . SER A 1 94 ? 16.877  -23.014 -8.496  1.00 71.88  ? 93  SER A CA  1 
ATOM   753  C C   . SER A 1 94 ? 17.468  -24.345 -7.995  1.00 88.28  ? 93  SER A C   1 
ATOM   754  O O   . SER A 1 94 ? 18.709  -24.383 -7.774  1.00 91.96  ? 93  SER A O   1 
ATOM   755  C CB  . SER A 1 94 ? 17.785  -22.411 -9.562  1.00 69.56  ? 93  SER A CB  1 
ATOM   756  O OG  . SER A 1 94 ? 17.500  -21.046 -9.821  1.00 69.92  ? 93  SER A OG  1 
ATOM   757  O OXT . SER A 1 94 ? 16.672  -25.296 -7.823  1.00 102.21 ? 93  SER A OXT 1 
ATOM   758  N N   . MET B 1 2  ? 38.944  -11.189 -41.744 1.00 85.30  ? 1   MET B N   1 
ATOM   759  C CA  . MET B 1 2  ? 38.517  -12.048 -42.880 1.00 80.97  ? 1   MET B CA  1 
ATOM   760  C C   . MET B 1 2  ? 36.985  -12.090 -42.947 1.00 76.06  ? 1   MET B C   1 
ATOM   761  O O   . MET B 1 2  ? 36.323  -12.347 -41.938 1.00 61.05  ? 1   MET B O   1 
ATOM   762  C CB  . MET B 1 2  ? 39.100  -13.458 -42.723 1.00 91.13  ? 1   MET B CB  1 
ATOM   763  C CG  . MET B 1 2  ? 39.422  -14.154 -44.038 1.00 108.05 ? 1   MET B CG  1 
ATOM   764  S SD  . MET B 1 2  ? 40.754  -13.370 -44.974 1.00 103.20 ? 1   MET B SD  1 
ATOM   765  C CE  . MET B 1 2  ? 42.081  -13.346 -43.760 1.00 110.55 ? 1   MET B CE  1 
ATOM   766  N N   . PRO B 1 3  ? 36.367  -11.854 -44.136 1.00 72.39  ? 2   PRO B N   1 
ATOM   767  C CA  . PRO B 1 3  ? 34.918  -11.997 -44.292 1.00 63.42  ? 2   PRO B CA  1 
ATOM   768  C C   . PRO B 1 3  ? 34.500  -13.413 -43.898 1.00 66.32  ? 2   PRO B C   1 
ATOM   769  O O   . PRO B 1 3  ? 35.313  -14.346 -43.909 1.00 57.82  ? 2   PRO B O   1 
ATOM   770  C CB  . PRO B 1 3  ? 34.625  -11.675 -45.767 1.00 62.69  ? 2   PRO B CB  1 
ATOM   771  C CG  . PRO B 1 3  ? 35.858  -10.929 -46.223 1.00 62.54  ? 2   PRO B CG  1 
ATOM   772  C CD  . PRO B 1 3  ? 37.028  -11.461 -45.395 1.00 66.71  ? 2   PRO B CD  1 
ATOM   773  N N   . HIS B 1 4  ? 33.233  -13.534 -43.485 1.00 63.12  ? 3   HIS B N   1 
ATOM   774  C CA  . HIS B 1 4  ? 32.722  -14.777 -42.931 1.00 67.69  ? 3   HIS B CA  1 
ATOM   775  C C   . HIS B 1 4  ? 31.344  -15.097 -43.519 1.00 66.85  ? 3   HIS B C   1 
ATOM   776  O O   . HIS B 1 4  ? 30.703  -14.229 -44.138 1.00 58.37  ? 3   HIS B O   1 
ATOM   777  C CB  . HIS B 1 4  ? 32.814  -14.743 -41.404 1.00 63.84  ? 3   HIS B CB  1 
ATOM   778  C CG  . HIS B 1 4  ? 34.179  -15.028 -40.845 1.00 82.12  ? 3   HIS B CG  1 
ATOM   779  N ND1 . HIS B 1 4  ? 35.001  -16.043 -41.308 1.00 76.30  ? 3   HIS B ND1 1 
ATOM   780  C CD2 . HIS B 1 4  ? 34.840  -14.442 -39.811 1.00 66.25  ? 3   HIS B CD2 1 
ATOM   781  C CE1 . HIS B 1 4  ? 36.113  -16.065 -40.577 1.00 75.77  ? 3   HIS B CE1 1 
ATOM   782  N NE2 . HIS B 1 4  ? 36.034  -15.101 -39.667 1.00 74.82  ? 3   HIS B NE2 1 
ATOM   783  N N   . ALA B 1 5  ? 30.932  -16.369 -43.346 1.00 58.18  ? 4   ALA B N   1 
ATOM   784  C CA  . ALA B 1 5  ? 29.626  -16.845 -43.770 1.00 53.43  ? 4   ALA B CA  1 
ATOM   785  C C   . ALA B 1 5  ? 28.589  -15.845 -43.291 1.00 53.67  ? 4   ALA B C   1 
ATOM   786  O O   . ALA B 1 5  ? 27.783  -15.355 -44.078 1.00 48.70  ? 4   ALA B O   1 
ATOM   787  C CB  . ALA B 1 5  ? 29.350  -18.193 -43.163 1.00 60.17  ? 4   ALA B CB  1 
ATOM   788  N N   . PHE B 1 6  ? 28.668  -15.542 -41.989 1.00 50.27  ? 5   PHE B N   1 
ATOM   789  C CA  . PHE B 1 6  ? 27.838  -14.526 -41.356 1.00 55.32  ? 5   PHE B CA  1 
ATOM   790  C C   . PHE B 1 6  ? 28.719  -13.311 -41.053 1.00 51.81  ? 5   PHE B C   1 
ATOM   791  O O   . PHE B 1 6  ? 29.812  -13.447 -40.512 1.00 52.78  ? 5   PHE B O   1 
ATOM   792  C CB  . PHE B 1 6  ? 27.209  -15.070 -40.063 1.00 48.39  ? 5   PHE B CB  1 
ATOM   793  C CG  . PHE B 1 6  ? 26.168  -16.183 -40.157 1.00 43.12  ? 5   PHE B CG  1 
ATOM   794  C CD1 . PHE B 1 6  ? 24.823  -15.886 -40.366 1.00 41.03  ? 5   PHE B CD1 1 
ATOM   795  C CD2 . PHE B 1 6  ? 26.521  -17.513 -39.967 1.00 42.70  ? 5   PHE B CD2 1 
ATOM   796  C CE1 . PHE B 1 6  ? 23.862  -16.879 -40.422 1.00 44.59  ? 5   PHE B CE1 1 
ATOM   797  C CE2 . PHE B 1 6  ? 25.560  -18.516 -40.013 1.00 45.54  ? 5   PHE B CE2 1 
ATOM   798  C CZ  . PHE B 1 6  ? 24.227  -18.201 -40.217 1.00 45.98  ? 5   PHE B CZ  1 
ATOM   799  N N   . LYS B 1 7  ? 28.231  -12.118 -41.389 1.00 52.06  ? 6   LYS B N   1 
ATOM   800  C CA  . LYS B 1 7  ? 28.970  -10.889 -41.136 1.00 53.87  ? 6   LYS B CA  1 
ATOM   801  C C   . LYS B 1 7  ? 28.183  -9.995  -40.164 1.00 52.85  ? 6   LYS B C   1 
ATOM   802  O O   . LYS B 1 7  ? 26.950  -10.085 -40.063 1.00 48.29  ? 6   LYS B O   1 
ATOM   803  C CB  . LYS B 1 7  ? 29.208  -10.253 -42.511 1.00 55.50  ? 6   LYS B CB  1 
ATOM   804  C CG  . LYS B 1 7  ? 27.917  -9.950  -43.258 1.00 53.92  ? 6   LYS B CG  1 
ATOM   805  C CD  . LYS B 1 7  ? 28.160  -9.512  -44.698 1.00 65.99  ? 6   LYS B CD  1 
ATOM   806  C CE  . LYS B 1 7  ? 26.924  -9.058  -45.416 1.00 63.60  ? 6   LYS B CE  1 
ATOM   807  N NZ  . LYS B 1 7  ? 25.914  -10.113 -45.578 1.00 66.10  ? 6   LYS B NZ  1 
ATOM   808  N N   . PRO B 1 8  ? 28.861  -9.077  -39.433 1.00 51.77  ? 7   PRO B N   1 
ATOM   809  C CA  . PRO B 1 8  ? 28.191  -8.217  -38.456 1.00 45.15  ? 7   PRO B CA  1 
ATOM   810  C C   . PRO B 1 8  ? 27.042  -7.511  -39.139 1.00 43.65  ? 7   PRO B C   1 
ATOM   811  O O   . PRO B 1 8  ? 27.186  -7.032  -40.264 1.00 53.86  ? 7   PRO B O   1 
ATOM   812  C CB  . PRO B 1 8  ? 29.339  -7.295  -38.118 1.00 48.21  ? 7   PRO B CB  1 
ATOM   813  C CG  . PRO B 1 8  ? 30.509  -8.266  -38.068 1.00 49.23  ? 7   PRO B CG  1 
ATOM   814  C CD  . PRO B 1 8  ? 30.316  -8.836  -39.466 1.00 51.79  ? 7   PRO B CD  1 
ATOM   815  N N   . GLY B 1 9  ? 25.876  -7.558  -38.493 1.00 41.05  ? 8   GLY B N   1 
ATOM   816  C CA  . GLY B 1 9  ? 24.709  -6.854  -38.990 1.00 34.88  ? 8   GLY B CA  1 
ATOM   817  C C   . GLY B 1 9  ? 23.717  -7.810  -39.631 1.00 34.69  ? 8   GLY B C   1 
ATOM   818  O O   . GLY B 1 9  ? 22.607  -7.400  -39.954 1.00 40.82  ? 8   GLY B O   1 
ATOM   819  N N   . ASP B 1 10 ? 24.148  -9.055  -39.877 1.00 42.00  ? 9   ASP B N   1 
ATOM   820  C CA  . ASP B 1 10 ? 23.280  -10.068 -40.471 1.00 37.04  ? 9   ASP B CA  1 
ATOM   821  C C   . ASP B 1 10 ? 22.161  -10.374 -39.480 1.00 38.78  ? 9   ASP B C   1 
ATOM   822  O O   . ASP B 1 10 ? 22.367  -10.382 -38.255 1.00 33.66  ? 9   ASP B O   1 
ATOM   823  C CB  . ASP B 1 10 ? 24.056  -11.334 -40.789 1.00 40.27  ? 9   ASP B CB  1 
ATOM   824  C CG  . ASP B 1 10 ? 24.845  -11.363 -42.095 1.00 51.04  ? 9   ASP B CG  1 
ATOM   825  O OD1 . ASP B 1 10 ? 24.570  -10.534 -43.004 1.00 44.37  ? 9   ASP B OD1 1 
ATOM   826  O OD2 . ASP B 1 10 ? 25.745  -12.218 -42.191 1.00 47.02  ? 9   ASP B OD2 1 
ATOM   827  N N   . LEU B 1 11 ? 20.950  -10.520 -40.005 1.00 33.90  ? 10  LEU B N   1 
ATOM   828  C CA  . LEU B 1 11 ? 19.846  -10.798 -39.105 1.00 36.75  ? 10  LEU B CA  1 
ATOM   829  C C   . LEU B 1 11 ? 19.535  -12.288 -39.139 1.00 38.39  ? 10  LEU B C   1 
ATOM   830  O O   . LEU B 1 11 ? 19.531  -12.877 -40.214 1.00 39.20  ? 10  LEU B O   1 
ATOM   831  C CB  . LEU B 1 11 ? 18.633  -9.960  -39.502 1.00 29.96  ? 10  LEU B CB  1 
ATOM   832  C CG  . LEU B 1 11 ? 18.914  -8.464  -39.645 1.00 36.63  ? 10  LEU B CG  1 
ATOM   833  C CD1 . LEU B 1 11 ? 17.654  -7.822  -40.179 1.00 30.92  ? 10  LEU B CD1 1 
ATOM   834  C CD2 . LEU B 1 11 ? 19.356  -7.891  -38.274 1.00 34.91  ? 10  LEU B CD2 1 
ATOM   835  N N   . VAL B 1 12 ? 19.191  -12.861 -37.974 1.00 37.05  ? 11  VAL B N   1 
ATOM   836  C CA  . VAL B 1 12 ? 18.942  -14.295 -37.840 1.00 33.51  ? 11  VAL B CA  1 
ATOM   837  C C   . VAL B 1 12 ? 17.807  -14.530 -36.847 1.00 38.65  ? 11  VAL B C   1 
ATOM   838  O O   . VAL B 1 12 ? 17.396  -13.617 -36.141 1.00 32.83  ? 11  VAL B O   1 
ATOM   839  C CB  . VAL B 1 12 ? 20.215  -14.982 -37.308 1.00 38.96  ? 11  VAL B CB  1 
ATOM   840  C CG1 . VAL B 1 12 ? 21.340  -14.915 -38.350 1.00 40.36  ? 11  VAL B CG1 1 
ATOM   841  C CG2 . VAL B 1 12 ? 20.636  -14.423 -35.937 1.00 34.36  ? 11  VAL B CG2 1 
ATOM   842  N N   . PHE B 1 13 ? 17.296  -15.764 -36.809 1.00 37.05  ? 12  PHE B N   1 
ATOM   843  C CA  . PHE B 1 13 ? 16.774  -16.281 -35.555 1.00 37.03  ? 12  PHE B CA  1 
ATOM   844  C C   . PHE B 1 13 ? 17.866  -17.155 -34.958 1.00 40.58  ? 12  PHE B C   1 
ATOM   845  O O   . PHE B 1 13 ? 18.478  -17.928 -35.708 1.00 35.62  ? 12  PHE B O   1 
ATOM   846  C CB  . PHE B 1 13 ? 15.545  -17.149 -35.796 1.00 34.16  ? 12  PHE B CB  1 
ATOM   847  C CG  . PHE B 1 13 ? 14.334  -16.338 -36.225 1.00 38.01  ? 12  PHE B CG  1 
ATOM   848  C CD1 . PHE B 1 13 ? 14.126  -16.051 -37.573 1.00 38.10  ? 12  PHE B CD1 1 
ATOM   849  C CD2 . PHE B 1 13 ? 13.415  -15.871 -35.293 1.00 36.23  ? 12  PHE B CD2 1 
ATOM   850  C CE1 . PHE B 1 13 ? 13.025  -15.334 -37.990 1.00 42.29  ? 12  PHE B CE1 1 
ATOM   851  C CE2 . PHE B 1 13 ? 12.308  -15.138 -35.708 1.00 36.22  ? 12  PHE B CE2 1 
ATOM   852  C CZ  . PHE B 1 13 ? 12.130  -14.852 -37.060 1.00 39.23  ? 12  PHE B CZ  1 
ATOM   853  N N   . ALA B 1 14 ? 18.098  -17.000 -33.635 1.00 32.76  ? 13  ALA B N   1 
ATOM   854  C CA  . ALA B 1 14 ? 19.105  -17.766 -32.927 1.00 33.13  ? 13  ALA B CA  1 
ATOM   855  C C   . ALA B 1 14 ? 18.458  -18.728 -31.929 1.00 33.89  ? 13  ALA B C   1 
ATOM   856  O O   . ALA B 1 14 ? 17.444  -18.408 -31.294 1.00 37.63  ? 13  ALA B O   1 
ATOM   857  C CB  . ALA B 1 14 ? 20.139  -16.851 -32.285 1.00 30.28  ? 13  ALA B CB  1 
ATOM   858  N N   . LYS B 1 15 ? 19.050  -19.919 -31.815 1.00 35.18  ? 14  LYS B N   1 
ATOM   859  C CA  . LYS B 1 15 ? 18.392  -21.025 -31.119 1.00 40.31  ? 14  LYS B CA  1 
ATOM   860  C C   . LYS B 1 15 ? 19.258  -21.439 -29.947 1.00 36.93  ? 14  LYS B C   1 
ATOM   861  O O   . LYS B 1 15 ? 20.448  -21.700 -30.121 1.00 42.41  ? 14  LYS B O   1 
ATOM   862  C CB  . LYS B 1 15 ? 18.161  -22.310 -31.925 1.00 39.96  ? 14  LYS B CB  1 
ATOM   863  C CG  . LYS B 1 15 ? 17.426  -23.435 -31.135 1.00 40.01  ? 14  LYS B CG  1 
ATOM   864  C CD  . LYS B 1 15 ? 15.949  -23.076 -30.875 1.00 35.08  ? 14  LYS B CD  1 
ATOM   865  C CE  . LYS B 1 15 ? 15.052  -24.140 -30.224 1.00 35.64  ? 14  LYS B CE  1 
ATOM   866  N NZ  . LYS B 1 15 ? 15.544  -24.417 -28.887 1.00 34.23  ? 14  LYS B NZ  1 
ATOM   867  N N   . MET B 1 16 ? 18.671  -21.375 -28.747 1.00 38.21  ? 15  MET B N   1 
ATOM   868  C CA  . MET B 1 16 ? 19.335  -21.851 -27.552 1.00 37.81  ? 15  MET B CA  1 
ATOM   869  C C   . MET B 1 16 ? 18.395  -22.828 -26.851 1.00 37.88  ? 15  MET B C   1 
ATOM   870  O O   . MET B 1 16 ? 17.160  -22.693 -26.934 1.00 38.33  ? 15  MET B O   1 
ATOM   871  C CB  . MET B 1 16 ? 19.733  -20.698 -26.626 1.00 38.61  ? 15  MET B CB  1 
ATOM   872  C CG  . MET B 1 16 ? 20.941  -19.920 -27.137 1.00 49.14  ? 15  MET B CG  1 
ATOM   873  S SD  . MET B 1 16 ? 21.529  -18.583 -26.078 1.00 50.53  ? 15  MET B SD  1 
ATOM   874  C CE  . MET B 1 16 ? 22.173  -19.519 -24.682 1.00 42.53  ? 15  MET B CE  1 
ATOM   875  N N   . LYS B 1 17 ? 18.997  -23.804 -26.160 1.00 36.74  ? 16  LYS B N   1 
ATOM   876  C CA  . LYS B 1 17 ? 18.240  -24.795 -25.388 1.00 39.02  ? 16  LYS B CA  1 
ATOM   877  C C   . LYS B 1 17 ? 17.375  -24.070 -24.355 1.00 36.47  ? 16  LYS B C   1 
ATOM   878  O O   . LYS B 1 17 ? 17.861  -23.172 -23.669 1.00 38.40  ? 16  LYS B O   1 
ATOM   879  C CB  . LYS B 1 17 ? 19.212  -25.855 -24.838 1.00 43.49  ? 16  LYS B CB  1 
ATOM   880  C CG  . LYS B 1 17 ? 18.531  -26.982 -24.037 1.00 49.83  ? 16  LYS B CG  1 
ATOM   881  C CD  . LYS B 1 17 ? 19.471  -27.753 -23.117 1.00 50.01  ? 16  LYS B CD  1 
ATOM   882  N N   . GLY B 1 18 ? 16.073  -24.393 -24.332 1.00 39.29  ? 17  GLY B N   1 
ATOM   883  C CA  . GLY B 1 18 ? 15.132  -23.819 -23.386 1.00 36.35  ? 17  GLY B CA  1 
ATOM   884  C C   . GLY B 1 18 ? 14.281  -22.692 -23.968 1.00 37.42  ? 17  GLY B C   1 
ATOM   885  O O   . GLY B 1 18 ? 13.374  -22.172 -23.302 1.00 40.15  ? 17  GLY B O   1 
ATOM   886  N N   . TYR B 1 19 ? 14.588  -22.295 -25.206 1.00 35.29  ? 18  TYR B N   1 
ATOM   887  C CA  . TYR B 1 19 ? 13.935  -21.136 -25.783 1.00 35.58  ? 18  TYR B CA  1 
ATOM   888  C C   . TYR B 1 19 ? 13.569  -21.397 -27.242 1.00 34.19  ? 18  TYR B C   1 
ATOM   889  O O   . TYR B 1 19 ? 14.265  -22.121 -27.946 1.00 38.83  ? 18  TYR B O   1 
ATOM   890  C CB  . TYR B 1 19 ? 14.912  -19.959 -25.686 1.00 33.69  ? 18  TYR B CB  1 
ATOM   891  C CG  . TYR B 1 19 ? 15.413  -19.684 -24.275 1.00 37.27  ? 18  TYR B CG  1 
ATOM   892  C CD1 . TYR B 1 19 ? 14.700  -18.878 -23.378 1.00 40.99  ? 18  TYR B CD1 1 
ATOM   893  C CD2 . TYR B 1 19 ? 16.619  -20.229 -23.842 1.00 40.37  ? 18  TYR B CD2 1 
ATOM   894  C CE1 . TYR B 1 19 ? 15.170  -18.659 -22.082 1.00 44.71  ? 18  TYR B CE1 1 
ATOM   895  C CE2 . TYR B 1 19 ? 17.085  -20.038 -22.551 1.00 38.42  ? 18  TYR B CE2 1 
ATOM   896  C CZ  . TYR B 1 19 ? 16.379  -19.216 -21.684 1.00 40.52  ? 18  TYR B CZ  1 
ATOM   897  O OH  . TYR B 1 19 ? 16.934  -19.035 -20.457 1.00 43.68  ? 18  TYR B OH  1 
ATOM   898  N N   . PRO B 1 20 ? 12.508  -20.734 -27.744 1.00 30.06  ? 19  PRO B N   1 
ATOM   899  C CA  . PRO B 1 20 ? 12.214  -20.723 -29.173 1.00 28.93  ? 19  PRO B CA  1 
ATOM   900  C C   . PRO B 1 20 ? 13.283  -19.975 -29.977 1.00 35.75  ? 19  PRO B C   1 
ATOM   901  O O   . PRO B 1 20 ? 13.946  -19.070 -29.455 1.00 32.22  ? 19  PRO B O   1 
ATOM   902  C CB  . PRO B 1 20 ? 10.883  -20.018 -29.215 1.00 28.38  ? 19  PRO B CB  1 
ATOM   903  C CG  . PRO B 1 20 ? 10.963  -19.003 -28.025 1.00 33.23  ? 19  PRO B CG  1 
ATOM   904  C CD  . PRO B 1 20 ? 11.607  -19.877 -26.941 1.00 30.57  ? 19  PRO B CD  1 
ATOM   905  N N   . HIS B 1 21 ? 13.493  -20.409 -31.229 1.00 33.77  ? 20  HIS B N   1 
ATOM   906  C CA  . HIS B 1 21 ? 14.318  -19.658 -32.193 1.00 32.19  ? 20  HIS B CA  1 
ATOM   907  C C   . HIS B 1 21 ? 13.980  -18.184 -32.060 1.00 30.64  ? 20  HIS B C   1 
ATOM   908  O O   . HIS B 1 21 ? 12.814  -17.802 -32.153 1.00 29.00  ? 20  HIS B O   1 
ATOM   909  C CB  . HIS B 1 21 ? 14.000  -20.080 -33.637 1.00 32.07  ? 20  HIS B CB  1 
ATOM   910  C CG  . HIS B 1 21 ? 14.118  -21.552 -33.819 1.00 31.41  ? 20  HIS B CG  1 
ATOM   911  N ND1 . HIS B 1 21 ? 13.110  -22.421 -33.472 1.00 34.78  ? 20  HIS B ND1 1 
ATOM   912  C CD2 . HIS B 1 21 ? 15.148  -22.315 -34.226 1.00 33.48  ? 20  HIS B CD2 1 
ATOM   913  C CE1 . HIS B 1 21 ? 13.517  -23.661 -33.694 1.00 36.63  ? 20  HIS B CE1 1 
ATOM   914  N NE2 . HIS B 1 21 ? 14.748  -23.621 -34.150 1.00 35.35  ? 20  HIS B NE2 1 
ATOM   915  N N   . TRP B 1 22 ? 15.011  -17.363 -31.826 1.00 31.64  ? 21  TRP B N   1 
ATOM   916  C CA  . TRP B 1 22 ? 14.770  -16.038 -31.278 1.00 31.19  ? 21  TRP B CA  1 
ATOM   917  C C   . TRP B 1 22 ? 15.318  -14.960 -32.220 1.00 31.57  ? 21  TRP B C   1 
ATOM   918  O O   . TRP B 1 22 ? 16.472  -15.093 -32.675 1.00 32.96  ? 21  TRP B O   1 
ATOM   919  C CB  . TRP B 1 22 ? 15.497  -15.969 -29.937 1.00 28.87  ? 21  TRP B CB  1 
ATOM   920  C CG  . TRP B 1 22 ? 14.998  -14.812 -29.120 1.00 34.64  ? 21  TRP B CG  1 
ATOM   921  C CD1 . TRP B 1 22 ? 15.292  -13.490 -29.289 1.00 34.12  ? 21  TRP B CD1 1 
ATOM   922  C CD2 . TRP B 1 22 ? 14.074  -14.892 -28.006 1.00 37.64  ? 21  TRP B CD2 1 
ATOM   923  N NE1 . TRP B 1 22 ? 14.627  -12.739 -28.350 1.00 39.87  ? 21  TRP B NE1 1 
ATOM   924  C CE2 . TRP B 1 22 ? 13.866  -13.568 -27.552 1.00 36.77  ? 21  TRP B CE2 1 
ATOM   925  C CE3 . TRP B 1 22 ? 13.422  -15.944 -27.347 1.00 38.19  ? 21  TRP B CE3 1 
ATOM   926  C CZ2 . TRP B 1 22 ? 13.047  -13.282 -26.458 1.00 33.13  ? 21  TRP B CZ2 1 
ATOM   927  C CZ3 . TRP B 1 22 ? 12.606  -15.667 -26.260 1.00 34.48  ? 21  TRP B CZ3 1 
ATOM   928  C CH2 . TRP B 1 22 ? 12.404  -14.343 -25.849 1.00 33.07  ? 21  TRP B CH2 1 
ATOM   929  N N   . PRO B 1 23 ? 14.552  -13.878 -32.525 1.00 30.37  ? 22  PRO B N   1 
ATOM   930  C CA  . PRO B 1 23 ? 15.033  -12.780 -33.384 1.00 33.23  ? 22  PRO B CA  1 
ATOM   931  C C   . PRO B 1 23 ? 16.339  -12.230 -32.842 1.00 36.47  ? 22  PRO B C   1 
ATOM   932  O O   . PRO B 1 23 ? 16.450  -11.897 -31.662 1.00 36.10  ? 22  PRO B O   1 
ATOM   933  C CB  . PRO B 1 23 ? 13.873  -11.755 -33.407 1.00 29.85  ? 22  PRO B CB  1 
ATOM   934  C CG  . PRO B 1 23 ? 13.094  -12.135 -32.141 1.00 29.32  ? 22  PRO B CG  1 
ATOM   935  C CD  . PRO B 1 23 ? 13.132  -13.673 -32.185 1.00 28.65  ? 22  PRO B CD  1 
ATOM   936  N N   . ALA B 1 24 ? 17.369  -12.212 -33.699 1.00 34.52  ? 23  ALA B N   1 
ATOM   937  C CA  . ALA B 1 24 ? 18.657  -11.745 -33.221 1.00 30.25  ? 23  ALA B CA  1 
ATOM   938  C C   . ALA B 1 24 ? 19.496  -11.176 -34.364 1.00 35.61  ? 23  ALA B C   1 
ATOM   939  O O   . ALA B 1 24 ? 19.077  -11.192 -35.530 1.00 40.57  ? 23  ALA B O   1 
ATOM   940  C CB  . ALA B 1 24 ? 19.392  -12.860 -32.536 1.00 28.12  ? 23  ALA B CB  1 
ATOM   941  N N   . ARG B 1 25 ? 20.718  -10.742 -33.993 1.00 34.26  ? 24  ARG B N   1 
ATOM   942  C CA  . ARG B 1 25 ? 21.660  -10.194 -34.954 1.00 36.35  ? 24  ARG B CA  1 
ATOM   943  C C   . ARG B 1 25 ? 23.055  -10.703 -34.624 1.00 35.48  ? 24  ARG B C   1 
ATOM   944  O O   . ARG B 1 25 ? 23.335  -11.065 -33.475 1.00 35.16  ? 24  ARG B O   1 
ATOM   945  C CB  . ARG B 1 25 ? 21.606  -8.669  -35.052 1.00 31.66  ? 24  ARG B CB  1 
ATOM   946  C CG  . ARG B 1 25 ? 22.387  -7.891  -34.005 1.00 36.37  ? 24  ARG B CG  1 
ATOM   947  C CD  . ARG B 1 25 ? 21.980  -6.429  -34.036 1.00 33.22  ? 24  ARG B CD  1 
ATOM   948  N NE  . ARG B 1 25 ? 22.677  -5.707  -32.968 1.00 32.71  ? 24  ARG B NE  1 
ATOM   949  C CZ  . ARG B 1 25 ? 22.389  -4.474  -32.562 1.00 35.36  ? 24  ARG B CZ  1 
ATOM   950  N NH1 . ARG B 1 25 ? 21.418  -3.772  -33.152 1.00 33.82  ? 24  ARG B NH1 1 
ATOM   951  N NH2 . ARG B 1 25 ? 23.122  -3.952  -31.600 1.00 28.03  ? 24  ARG B NH2 1 
ATOM   952  N N   . ILE B 1 26 ? 23.881  -10.780 -35.681 1.00 32.86  ? 25  ILE B N   1 
ATOM   953  C CA  . ILE B 1 26 ? 25.327  -10.901 -35.551 1.00 36.78  ? 25  ILE B CA  1 
ATOM   954  C C   . ILE B 1 26 ? 25.914  -9.520  -35.237 1.00 35.86  ? 25  ILE B C   1 
ATOM   955  O O   . ILE B 1 26 ? 25.797  -8.566  -36.027 1.00 40.92  ? 25  ILE B O   1 
ATOM   956  C CB  . ILE B 1 26 ? 25.965  -11.503 -36.822 1.00 39.25  ? 25  ILE B CB  1 
ATOM   957  C CG1 . ILE B 1 26 ? 25.240  -12.765 -37.322 1.00 36.53  ? 25  ILE B CG1 1 
ATOM   958  C CG2 . ILE B 1 26 ? 27.474  -11.706 -36.648 1.00 42.93  ? 25  ILE B CG2 1 
ATOM   959  C CD1 . ILE B 1 26 ? 25.336  -13.970 -36.415 1.00 39.61  ? 25  ILE B CD1 1 
ATOM   960  N N   . ASP B 1 27 ? 26.591  -9.465  -34.097 1.00 37.78  ? 26  ASP B N   1 
ATOM   961  C CA  . ASP B 1 27 ? 27.295  -8.292  -33.602 1.00 50.40  ? 26  ASP B CA  1 
ATOM   962  C C   . ASP B 1 27 ? 28.796  -8.321  -33.917 1.00 58.48  ? 26  ASP B C   1 
ATOM   963  O O   . ASP B 1 27 ? 29.381  -9.391  -34.114 1.00 53.46  ? 26  ASP B O   1 
ATOM   964  C CB  . ASP B 1 27 ? 27.167  -8.217  -32.090 1.00 45.61  ? 26  ASP B CB  1 
ATOM   965  C CG  . ASP B 1 27 ? 26.020  -7.367  -31.564 1.00 46.65  ? 26  ASP B CG  1 
ATOM   966  O OD1 . ASP B 1 27 ? 25.296  -6.769  -32.395 1.00 43.19  ? 26  ASP B OD1 1 
ATOM   967  O OD2 . ASP B 1 27 ? 25.903  -7.252  -30.328 1.00 41.47  ? 26  ASP B OD2 1 
ATOM   968  N N   A ASP B 1 28 ? 29.402  -7.123  -33.904 0.50 62.37  ? 27  ASP B N   1 
ATOM   969  N N   B ASP B 1 28 ? 29.410  -7.126  -33.939 0.50 62.40  ? 27  ASP B N   1 
ATOM   970  C CA  A ASP B 1 28 ? 30.836  -6.894  -34.007 0.50 63.76  ? 27  ASP B CA  1 
ATOM   971  C CA  B ASP B 1 28 ? 30.852  -6.946  -34.051 0.50 63.79  ? 27  ASP B CA  1 
ATOM   972  C C   A ASP B 1 28 ? 31.523  -7.360  -32.726 0.50 67.51  ? 27  ASP B C   1 
ATOM   973  C C   B ASP B 1 28 ? 31.528  -7.323  -32.735 0.50 67.31  ? 27  ASP B C   1 
ATOM   974  O O   A ASP B 1 28 ? 30.860  -7.513  -31.697 0.50 63.86  ? 27  ASP B O   1 
ATOM   975  O O   B ASP B 1 28 ? 30.864  -7.380  -31.697 0.50 63.07  ? 27  ASP B O   1 
ATOM   976  C CB  A ASP B 1 28 ? 31.115  -5.413  -34.197 0.50 60.68  ? 27  ASP B CB  1 
ATOM   977  C CB  B ASP B 1 28 ? 31.202  -5.522  -34.455 0.50 61.68  ? 27  ASP B CB  1 
ATOM   978  C CG  A ASP B 1 28 ? 30.439  -4.796  -35.406 0.50 63.13  ? 27  ASP B CG  1 
ATOM   979  C CG  B ASP B 1 28 ? 31.306  -5.286  -35.952 0.50 67.02  ? 27  ASP B CG  1 
ATOM   980  O OD1 A ASP B 1 28 ? 30.925  -5.049  -36.530 0.50 71.56  ? 27  ASP B OD1 1 
ATOM   981  O OD1 B ASP B 1 28 ? 32.298  -5.755  -36.553 0.50 59.51  ? 27  ASP B OD1 1 
ATOM   982  O OD2 A ASP B 1 28 ? 29.418  -4.103  -35.215 0.50 61.71  ? 27  ASP B OD2 1 
ATOM   983  O OD2 B ASP B 1 28 ? 30.389  -4.645  -36.502 0.50 78.54  ? 27  ASP B OD2 1 
ATOM   984  N N   . ILE B 1 29 ? 32.854  -7.543  -32.798 1.00 68.47  ? 28  ILE B N   1 
ATOM   985  C CA  . ILE B 1 29 ? 33.633  -8.113  -31.700 1.00 66.36  ? 28  ILE B CA  1 
ATOM   986  C C   . ILE B 1 29 ? 34.395  -7.023  -30.918 1.00 67.37  ? 28  ILE B C   1 
ATOM   987  O O   . ILE B 1 29 ? 34.328  -5.837  -31.320 1.00 78.97  ? 28  ILE B O   1 
ATOM   988  C CB  . ILE B 1 29 ? 34.572  -9.225  -32.205 1.00 63.74  ? 28  ILE B CB  1 
ATOM   989  N N   . VAL B 1 34 ? 36.575  -9.722  -25.044 1.00 88.63  ? 33  VAL B N   1 
ATOM   990  C CA  . VAL B 1 34 ? 36.524  -11.215 -25.064 1.00 77.15  ? 33  VAL B CA  1 
ATOM   991  C C   . VAL B 1 34 ? 35.968  -11.620 -26.417 1.00 80.68  ? 33  VAL B C   1 
ATOM   992  O O   . VAL B 1 34 ? 34.761  -11.521 -26.625 1.00 93.44  ? 33  VAL B O   1 
ATOM   993  C CB  . VAL B 1 34 ? 35.643  -11.721 -23.905 1.00 70.51  ? 33  VAL B CB  1 
ATOM   994  C CG1 . VAL B 1 34 ? 34.646  -10.654 -23.482 1.00 70.81  ? 33  VAL B CG1 1 
ATOM   995  C CG2 . VAL B 1 34 ? 34.971  -13.068 -24.191 1.00 63.49  ? 33  VAL B CG2 1 
ATOM   996  N N   . LYS B 1 35 ? 36.869  -12.038 -27.319 1.00 82.83  ? 34  LYS B N   1 
ATOM   997  C CA  . LYS B 1 35 ? 36.538  -12.489 -28.668 1.00 76.65  ? 34  LYS B CA  1 
ATOM   998  C C   . LYS B 1 35 ? 35.843  -13.858 -28.622 1.00 73.60  ? 34  LYS B C   1 
ATOM   999  O O   . LYS B 1 35 ? 36.138  -14.682 -27.754 1.00 65.94  ? 34  LYS B O   1 
ATOM   1000 C CB  . LYS B 1 35 ? 37.805  -12.490 -29.534 1.00 67.37  ? 34  LYS B CB  1 
ATOM   1001 N N   . PRO B 1 36 ? 34.908  -14.167 -29.559 1.00 72.04  ? 35  PRO B N   1 
ATOM   1002 C CA  . PRO B 1 36 ? 34.124  -15.411 -29.497 1.00 60.30  ? 35  PRO B CA  1 
ATOM   1003 C C   . PRO B 1 36 ? 35.002  -16.657 -29.525 1.00 49.11  ? 35  PRO B C   1 
ATOM   1004 O O   . PRO B 1 36 ? 36.112  -16.576 -30.032 1.00 53.55  ? 35  PRO B O   1 
ATOM   1005 C CB  . PRO B 1 36 ? 33.214  -15.295 -30.736 1.00 61.21  ? 35  PRO B CB  1 
ATOM   1006 C CG  . PRO B 1 36 ? 33.963  -14.367 -31.667 1.00 67.62  ? 35  PRO B CG  1 
ATOM   1007 C CD  . PRO B 1 36 ? 34.571  -13.341 -30.733 1.00 64.54  ? 35  PRO B CD  1 
ATOM   1008 N N   . PRO B 1 37 ? 34.587  -17.809 -28.935 1.00 55.08  ? 36  PRO B N   1 
ATOM   1009 C CA  . PRO B 1 37 ? 35.321  -19.067 -29.106 1.00 53.00  ? 36  PRO B CA  1 
ATOM   1010 C C   . PRO B 1 37 ? 35.407  -19.382 -30.603 1.00 66.73  ? 36  PRO B C   1 
ATOM   1011 O O   . PRO B 1 37 ? 34.606  -18.870 -31.386 1.00 62.66  ? 36  PRO B O   1 
ATOM   1012 C CB  . PRO B 1 37 ? 34.503  -20.128 -28.325 1.00 52.17  ? 36  PRO B CB  1 
ATOM   1013 C CG  . PRO B 1 37 ? 33.582  -19.332 -27.402 1.00 49.87  ? 36  PRO B CG  1 
ATOM   1014 C CD  . PRO B 1 37 ? 33.418  -17.959 -28.041 1.00 51.18  ? 36  PRO B CD  1 
ATOM   1015 N N   . PRO B 1 38 ? 36.374  -20.216 -31.066 1.00 74.91  ? 37  PRO B N   1 
ATOM   1016 C CA  . PRO B 1 38 ? 36.449  -20.588 -32.489 1.00 75.03  ? 37  PRO B CA  1 
ATOM   1017 C C   . PRO B 1 38 ? 35.133  -21.148 -33.046 1.00 65.86  ? 37  PRO B C   1 
ATOM   1018 O O   . PRO B 1 38 ? 34.412  -21.861 -32.341 1.00 58.58  ? 37  PRO B O   1 
ATOM   1019 C CB  . PRO B 1 38 ? 37.610  -21.614 -32.602 1.00 71.37  ? 37  PRO B CB  1 
ATOM   1020 C CG  . PRO B 1 38 ? 38.324  -21.558 -31.255 1.00 74.06  ? 37  PRO B CG  1 
ATOM   1021 C CD  . PRO B 1 38 ? 37.427  -20.844 -30.244 1.00 77.66  ? 37  PRO B CD  1 
ATOM   1022 N N   . ASN B 1 39 ? 34.820  -20.787 -34.303 1.00 57.87  ? 38  ASN B N   1 
ATOM   1023 C CA  . ASN B 1 39 ? 33.620  -21.223 -35.019 1.00 57.56  ? 38  ASN B CA  1 
ATOM   1024 C C   . ASN B 1 39 ? 32.357  -20.466 -34.583 1.00 53.91  ? 38  ASN B C   1 
ATOM   1025 O O   . ASN B 1 39 ? 31.334  -20.576 -35.236 1.00 47.73  ? 38  ASN B O   1 
ATOM   1026 C CB  . ASN B 1 39 ? 33.334  -22.716 -34.850 1.00 59.49  ? 38  ASN B CB  1 
ATOM   1027 C CG  . ASN B 1 39 ? 34.540  -23.608 -35.049 1.00 75.28  ? 38  ASN B CG  1 
ATOM   1028 O OD1 . ASN B 1 39 ? 34.800  -24.474 -34.205 1.00 81.01  ? 38  ASN B OD1 1 
ATOM   1029 N ND2 . ASN B 1 39 ? 35.279  -23.428 -36.139 1.00 70.22  ? 38  ASN B ND2 1 
ATOM   1030 N N   . LYS B 1 40 ? 32.407  -19.685 -33.496 1.00 57.55  ? 39  LYS B N   1 
ATOM   1031 C CA  . LYS B 1 40 ? 31.202  -19.099 -32.928 1.00 53.60  ? 39  LYS B CA  1 
ATOM   1032 C C   . LYS B 1 40 ? 31.191  -17.592 -33.151 1.00 53.67  ? 39  LYS B C   1 
ATOM   1033 O O   . LYS B 1 40 ? 32.216  -16.990 -33.435 1.00 53.08  ? 39  LYS B O   1 
ATOM   1034 C CB  . LYS B 1 40 ? 31.063  -19.482 -31.452 1.00 50.85  ? 39  LYS B CB  1 
ATOM   1035 C CG  . LYS B 1 40 ? 31.024  -20.985 -31.208 1.00 50.17  ? 39  LYS B CG  1 
ATOM   1036 C CD  . LYS B 1 40 ? 31.114  -21.317 -29.725 1.00 51.74  ? 39  LYS B CD  1 
ATOM   1037 C CE  . LYS B 1 40 ? 29.836  -21.339 -28.963 1.00 64.98  ? 39  LYS B CE  1 
ATOM   1038 N NZ  . LYS B 1 40 ? 29.311  -22.705 -28.851 1.00 65.43  ? 39  LYS B NZ  1 
ATOM   1039 N N   . TYR B 1 41 ? 30.005  -16.997 -33.049 1.00 49.40  ? 40  TYR B N   1 
ATOM   1040 C CA  . TYR B 1 41 ? 29.876  -15.575 -33.298 1.00 42.90  ? 40  TYR B CA  1 
ATOM   1041 C C   . TYR B 1 41 ? 29.234  -14.917 -32.084 1.00 41.71  ? 40  TYR B C   1 
ATOM   1042 O O   . TYR B 1 41 ? 28.459  -15.555 -31.368 1.00 39.54  ? 40  TYR B O   1 
ATOM   1043 C CB  . TYR B 1 41 ? 28.922  -15.401 -34.475 1.00 40.28  ? 40  TYR B CB  1 
ATOM   1044 C CG  . TYR B 1 41 ? 29.398  -15.880 -35.842 1.00 43.85  ? 40  TYR B CG  1 
ATOM   1045 C CD1 . TYR B 1 41 ? 29.935  -14.976 -36.751 1.00 43.06  ? 40  TYR B CD1 1 
ATOM   1046 C CD2 . TYR B 1 41 ? 29.251  -17.203 -36.252 1.00 44.48  ? 40  TYR B CD2 1 
ATOM   1047 C CE1 . TYR B 1 41 ? 30.400  -15.371 -37.997 1.00 42.55  ? 40  TYR B CE1 1 
ATOM   1048 C CE2 . TYR B 1 41 ? 29.691  -17.613 -37.509 1.00 43.28  ? 40  TYR B CE2 1 
ATOM   1049 C CZ  . TYR B 1 41 ? 30.281  -16.695 -38.378 1.00 45.62  ? 40  TYR B CZ  1 
ATOM   1050 O OH  . TYR B 1 41 ? 30.697  -17.013 -39.647 1.00 49.87  ? 40  TYR B OH  1 
ATOM   1051 N N   . PRO B 1 42 ? 29.446  -13.592 -31.904 1.00 45.39  ? 41  PRO B N   1 
ATOM   1052 C CA  . PRO B 1 42 ? 28.690  -12.824 -30.922 1.00 38.87  ? 41  PRO B CA  1 
ATOM   1053 C C   . PRO B 1 42 ? 27.259  -12.549 -31.400 1.00 40.96  ? 41  PRO B C   1 
ATOM   1054 O O   . PRO B 1 42 ? 27.030  -11.845 -32.407 1.00 40.19  ? 41  PRO B O   1 
ATOM   1055 C CB  . PRO B 1 42 ? 29.552  -11.541 -30.811 1.00 37.14  ? 41  PRO B CB  1 
ATOM   1056 C CG  . PRO B 1 42 ? 30.131  -11.337 -32.203 1.00 41.67  ? 41  PRO B CG  1 
ATOM   1057 C CD  . PRO B 1 42 ? 30.362  -12.750 -32.711 1.00 46.74  ? 41  PRO B CD  1 
ATOM   1058 N N   . ILE B 1 43 ? 26.300  -13.099 -30.632 1.00 33.78  ? 42  ILE B N   1 
ATOM   1059 C CA  . ILE B 1 43 ? 24.875  -12.907 -30.890 1.00 33.13  ? 42  ILE B CA  1 
ATOM   1060 C C   . ILE B 1 43 ? 24.266  -11.812 -29.995 1.00 35.35  ? 42  ILE B C   1 
ATOM   1061 O O   . ILE B 1 43 ? 24.565  -11.732 -28.814 1.00 43.25  ? 42  ILE B O   1 
ATOM   1062 C CB  . ILE B 1 43 ? 24.130  -14.247 -30.786 1.00 29.26  ? 42  ILE B CB  1 
ATOM   1063 C CG1 . ILE B 1 43 ? 24.852  -15.350 -31.617 1.00 32.89  ? 42  ILE B CG1 1 
ATOM   1064 C CG2 . ILE B 1 43 ? 22.675  -14.065 -31.266 1.00 35.39  ? 42  ILE B CG2 1 
ATOM   1065 C CD1 . ILE B 1 43 ? 25.155  -14.928 -33.053 1.00 30.23  ? 42  ILE B CD1 1 
ATOM   1066 N N   . PHE B 1 44 ? 23.371  -10.994 -30.577 1.00 39.05  ? 43  PHE B N   1 
ATOM   1067 C CA  . PHE B 1 44 ? 22.546  -10.041 -29.841 1.00 38.93  ? 43  PHE B CA  1 
ATOM   1068 C C   . PHE B 1 44 ? 21.080  -10.404 -30.060 1.00 37.48  ? 43  PHE B C   1 
ATOM   1069 O O   . PHE B 1 44 ? 20.607  -10.462 -31.213 1.00 32.64  ? 43  PHE B O   1 
ATOM   1070 C CB  . PHE B 1 44 ? 22.788  -8.560  -30.176 1.00 38.09  ? 43  PHE B CB  1 
ATOM   1071 C CG  . PHE B 1 44 ? 21.891  -7.535  -29.476 1.00 38.05  ? 43  PHE B CG  1 
ATOM   1072 C CD1 . PHE B 1 44 ? 20.709  -7.088  -30.066 1.00 33.67  ? 43  PHE B CD1 1 
ATOM   1073 C CD2 . PHE B 1 44 ? 22.242  -6.992  -28.233 1.00 42.40  ? 43  PHE B CD2 1 
ATOM   1074 C CE1 . PHE B 1 44 ? 19.912  -6.119  -29.446 1.00 34.63  ? 43  PHE B CE1 1 
ATOM   1075 C CE2 . PHE B 1 44 ? 21.456  -6.003  -27.620 1.00 35.50  ? 43  PHE B CE2 1 
ATOM   1076 C CZ  . PHE B 1 44 ? 20.288  -5.586  -28.226 1.00 38.76  ? 43  PHE B CZ  1 
ATOM   1077 N N   . PHE B 1 45 ? 20.391  -10.701 -28.937 1.00 33.53  ? 44  PHE B N   1 
ATOM   1078 C CA  . PHE B 1 45 ? 18.969  -11.069 -28.928 1.00 30.39  ? 44  PHE B CA  1 
ATOM   1079 C C   . PHE B 1 45 ? 18.103  -9.819  -28.823 1.00 31.40  ? 44  PHE B C   1 
ATOM   1080 O O   . PHE B 1 45 ? 18.146  -9.105  -27.822 1.00 33.97  ? 44  PHE B O   1 
ATOM   1081 C CB  . PHE B 1 45 ? 18.694  -12.002 -27.732 1.00 28.77  ? 44  PHE B CB  1 
ATOM   1082 C CG  . PHE B 1 45 ? 19.419  -13.331 -27.870 1.00 29.10  ? 44  PHE B CG  1 
ATOM   1083 C CD1 . PHE B 1 45 ? 20.761  -13.445 -27.563 1.00 32.56  ? 44  PHE B CD1 1 
ATOM   1084 C CD2 . PHE B 1 45 ? 18.766  -14.451 -28.359 1.00 30.17  ? 44  PHE B CD2 1 
ATOM   1085 C CE1 . PHE B 1 45 ? 21.432  -14.646 -27.726 1.00 37.28  ? 44  PHE B CE1 1 
ATOM   1086 C CE2 . PHE B 1 45 ? 19.431  -15.656 -28.492 1.00 34.85  ? 44  PHE B CE2 1 
ATOM   1087 C CZ  . PHE B 1 45 ? 20.770  -15.745 -28.211 1.00 34.62  ? 44  PHE B CZ  1 
ATOM   1088 N N   . PHE B 1 46 ? 17.266  -9.551  -29.836 1.00 31.23  ? 45  PHE B N   1 
ATOM   1089 C CA  . PHE B 1 46 ? 16.426  -8.378  -29.724 1.00 36.06  ? 45  PHE B CA  1 
ATOM   1090 C C   . PHE B 1 46 ? 15.395  -8.558  -28.592 1.00 40.91  ? 45  PHE B C   1 
ATOM   1091 O O   . PHE B 1 46 ? 15.122  -9.677  -28.166 1.00 35.30  ? 45  PHE B O   1 
ATOM   1092 C CB  . PHE B 1 46 ? 15.716  -8.183  -31.047 1.00 30.85  ? 45  PHE B CB  1 
ATOM   1093 C CG  . PHE B 1 46 ? 16.645  -7.737  -32.161 1.00 40.84  ? 45  PHE B CG  1 
ATOM   1094 C CD1 . PHE B 1 46 ? 17.116  -6.417  -32.204 1.00 36.94  ? 45  PHE B CD1 1 
ATOM   1095 C CD2 . PHE B 1 46 ? 16.970  -8.607  -33.203 1.00 34.59  ? 45  PHE B CD2 1 
ATOM   1096 C CE1 . PHE B 1 46 ? 17.944  -6.004  -33.243 1.00 35.86  ? 45  PHE B CE1 1 
ATOM   1097 C CE2 . PHE B 1 46 ? 17.815  -8.186  -34.228 1.00 37.93  ? 45  PHE B CE2 1 
ATOM   1098 C CZ  . PHE B 1 46 ? 18.274  -6.891  -34.262 1.00 30.80  ? 45  PHE B CZ  1 
ATOM   1099 N N   . GLY B 1 47 ? 14.778  -7.444  -28.158 1.00 37.67  ? 46  GLY B N   1 
ATOM   1100 C CA  . GLY B 1 47 ? 13.762  -7.451  -27.117 1.00 35.79  ? 46  GLY B CA  1 
ATOM   1101 C C   . GLY B 1 47 ? 14.369  -7.650  -25.722 1.00 37.63  ? 46  GLY B C   1 
ATOM   1102 O O   . GLY B 1 47 ? 14.222  -6.783  -24.882 1.00 40.52  ? 46  GLY B O   1 
ATOM   1103 N N   . THR B 1 48 ? 14.988  -8.806  -25.448 1.00 36.93  ? 47  THR B N   1 
ATOM   1104 C CA  . THR B 1 48 ? 15.676  -9.020  -24.187 1.00 38.23  ? 47  THR B CA  1 
ATOM   1105 C C   . THR B 1 48 ? 16.981  -8.234  -24.154 1.00 39.53  ? 47  THR B C   1 
ATOM   1106 O O   . THR B 1 48 ? 17.448  -7.860  -23.080 1.00 33.50  ? 47  THR B O   1 
ATOM   1107 C CB  . THR B 1 48 ? 15.979  -10.505 -23.959 1.00 40.55  ? 47  THR B CB  1 
ATOM   1108 O OG1 . THR B 1 48 ? 16.878  -10.905 -24.994 1.00 33.64  ? 47  THR B OG1 1 
ATOM   1109 C CG2 . THR B 1 48 ? 14.726  -11.361 -23.902 1.00 35.81  ? 47  THR B CG2 1 
ATOM   1110 N N   . HIS B 1 49 ? 17.628  -8.075  -25.314 1.00 36.03  ? 48  HIS B N   1 
ATOM   1111 C CA  . HIS B 1 49 ? 18.942  -7.437  -25.380 1.00 39.02  ? 48  HIS B CA  1 
ATOM   1112 C C   . HIS B 1 49 ? 20.030  -8.251  -24.685 1.00 37.95  ? 48  HIS B C   1 
ATOM   1113 O O   . HIS B 1 49 ? 21.061  -7.670  -24.336 1.00 48.90  ? 48  HIS B O   1 
ATOM   1114 C CB  . HIS B 1 49 ? 18.934  -5.971  -24.879 1.00 40.05  ? 48  HIS B CB  1 
ATOM   1115 C CG  . HIS B 1 49 ? 17.826  -5.196  -25.523 1.00 42.46  ? 48  HIS B CG  1 
ATOM   1116 N ND1 . HIS B 1 49 ? 17.050  -4.274  -24.861 1.00 42.86  ? 48  HIS B ND1 1 
ATOM   1117 C CD2 . HIS B 1 49 ? 17.292  -5.295  -26.767 1.00 35.80  ? 48  HIS B CD2 1 
ATOM   1118 C CE1 . HIS B 1 49 ? 16.113  -3.801  -25.690 1.00 42.49  ? 48  HIS B CE1 1 
ATOM   1119 N NE2 . HIS B 1 49 ? 16.226  -4.418  -26.861 1.00 39.86  ? 48  HIS B NE2 1 
ATOM   1120 N N   . GLU B 1 50 ? 19.855  -9.567  -24.540 1.00 35.63  ? 49  GLU B N   1 
ATOM   1121 C CA  . GLU B 1 50 ? 20.902  -10.453 -24.020 1.00 40.84  ? 49  GLU B CA  1 
ATOM   1122 C C   . GLU B 1 50 ? 21.930  -10.732 -25.121 1.00 39.11  ? 49  GLU B C   1 
ATOM   1123 O O   . GLU B 1 50 ? 21.683  -10.413 -26.280 1.00 36.83  ? 49  GLU B O   1 
ATOM   1124 C CB  . GLU B 1 50 ? 20.325  -11.832 -23.698 1.00 40.09  ? 49  GLU B CB  1 
ATOM   1125 C CG  . GLU B 1 50 ? 19.216  -11.800 -22.642 1.00 39.02  ? 49  GLU B CG  1 
ATOM   1126 C CD  . GLU B 1 50 ? 19.762  -12.109 -21.252 1.00 43.32  ? 49  GLU B CD  1 
ATOM   1127 O OE1 . GLU B 1 50 ? 19.123  -11.821 -20.227 1.00 42.73  ? 49  GLU B OE1 1 
ATOM   1128 O OE2 . GLU B 1 50 ? 20.845  -12.671 -21.179 1.00 40.18  ? 49  GLU B OE2 1 
ATOM   1129 N N   . THR B 1 51 ? 23.078  -11.326 -24.770 1.00 38.49  ? 50  THR B N   1 
ATOM   1130 C CA  . THR B 1 51 ? 24.107  -11.691 -25.745 1.00 39.33  ? 50  THR B CA  1 
ATOM   1131 C C   . THR B 1 51 ? 24.527  -13.124 -25.434 1.00 43.44  ? 50  THR B C   1 
ATOM   1132 O O   . THR B 1 51 ? 24.419  -13.547 -24.296 1.00 42.59  ? 50  THR B O   1 
ATOM   1133 C CB  . THR B 1 51 ? 25.319  -10.741 -25.699 1.00 42.10  ? 50  THR B CB  1 
ATOM   1134 O OG1 . THR B 1 51 ? 25.857  -10.935 -24.397 1.00 45.96  ? 50  THR B OG1 1 
ATOM   1135 C CG2 . THR B 1 51 ? 25.012  -9.257  -25.856 1.00 39.11  ? 50  THR B CG2 1 
ATOM   1136 N N   . ALA B 1 52 ? 24.959  -13.889 -26.446 1.00 42.21  ? 51  ALA B N   1 
ATOM   1137 C CA  . ALA B 1 52 ? 25.654  -15.148 -26.210 1.00 40.90  ? 51  ALA B CA  1 
ATOM   1138 C C   . ALA B 1 52 ? 26.600  -15.396 -27.387 1.00 42.51  ? 51  ALA B C   1 
ATOM   1139 O O   . ALA B 1 52 ? 26.594  -14.625 -28.356 1.00 41.62  ? 51  ALA B O   1 
ATOM   1140 C CB  . ALA B 1 52 ? 24.671  -16.287 -25.999 1.00 36.84  ? 51  ALA B CB  1 
ATOM   1141 N N   . PHE B 1 53 ? 27.418  -16.448 -27.281 1.00 37.94  ? 52  PHE B N   1 
ATOM   1142 C CA  . PHE B 1 53 ? 28.200  -16.939 -28.412 1.00 48.73  ? 52  PHE B CA  1 
ATOM   1143 C C   . PHE B 1 53 ? 27.540  -18.217 -28.959 1.00 48.63  ? 52  PHE B C   1 
ATOM   1144 O O   . PHE B 1 53 ? 27.278  -19.158 -28.208 1.00 45.76  ? 52  PHE B O   1 
ATOM   1145 C CB  . PHE B 1 53 ? 29.657  -17.144 -27.966 1.00 43.54  ? 52  PHE B CB  1 
ATOM   1146 C CG  . PHE B 1 53 ? 30.425  -15.903 -27.525 1.00 48.87  ? 52  PHE B CG  1 
ATOM   1147 C CD1 . PHE B 1 53 ? 30.606  -14.828 -28.387 1.00 51.46  ? 52  PHE B CD1 1 
ATOM   1148 C CD2 . PHE B 1 53 ? 30.944  -15.807 -26.233 1.00 51.11  ? 52  PHE B CD2 1 
ATOM   1149 C CE1 . PHE B 1 53 ? 31.297  -13.698 -27.975 1.00 50.19  ? 52  PHE B CE1 1 
ATOM   1150 C CE2 . PHE B 1 53 ? 31.628  -14.671 -25.818 1.00 49.97  ? 52  PHE B CE2 1 
ATOM   1151 C CZ  . PHE B 1 53 ? 31.793  -13.618 -26.682 1.00 45.46  ? 52  PHE B CZ  1 
ATOM   1152 N N   . LEU B 1 54 ? 27.257  -18.239 -30.275 1.00 42.89  ? 53  LEU B N   1 
ATOM   1153 C CA  . LEU B 1 54 ? 26.591  -19.356 -30.936 1.00 37.85  ? 53  LEU B CA  1 
ATOM   1154 C C   . LEU B 1 54 ? 27.307  -19.704 -32.239 1.00 40.87  ? 53  LEU B C   1 
ATOM   1155 O O   . LEU B 1 54 ? 27.876  -18.815 -32.890 1.00 41.80  ? 53  LEU B O   1 
ATOM   1156 C CB  . LEU B 1 54 ? 25.110  -19.092 -31.211 1.00 33.28  ? 53  LEU B CB  1 
ATOM   1157 C CG  . LEU B 1 54 ? 24.235  -18.928 -29.966 1.00 37.85  ? 53  LEU B CG  1 
ATOM   1158 C CD1 . LEU B 1 54 ? 22.876  -18.385 -30.364 1.00 34.43  ? 53  LEU B CD1 1 
ATOM   1159 C CD2 . LEU B 1 54 ? 24.105  -20.318 -29.305 1.00 35.09  ? 53  LEU B CD2 1 
ATOM   1160 N N   . GLY B 1 55 ? 27.266  -21.000 -32.585 1.00 40.38  ? 54  GLY B N   1 
ATOM   1161 C CA  . GLY B 1 55 ? 27.843  -21.492 -33.830 1.00 38.12  ? 54  GLY B CA  1 
ATOM   1162 C C   . GLY B 1 55 ? 26.765  -21.513 -34.917 1.00 39.04  ? 54  GLY B C   1 
ATOM   1163 O O   . GLY B 1 55 ? 25.572  -21.454 -34.612 1.00 40.51  ? 54  GLY B O   1 
ATOM   1164 N N   . PRO B 1 56 ? 27.121  -21.668 -36.212 1.00 38.81  ? 55  PRO B N   1 
ATOM   1165 C CA  . PRO B 1 56 ? 26.132  -21.663 -37.288 1.00 35.24  ? 55  PRO B CA  1 
ATOM   1166 C C   . PRO B 1 56 ? 24.962  -22.635 -37.197 1.00 35.05  ? 55  PRO B C   1 
ATOM   1167 O O   . PRO B 1 56 ? 23.907  -22.335 -37.742 1.00 36.87  ? 55  PRO B O   1 
ATOM   1168 C CB  . PRO B 1 56 ? 26.934  -21.888 -38.571 1.00 39.41  ? 55  PRO B CB  1 
ATOM   1169 C CG  . PRO B 1 56 ? 28.341  -21.582 -38.195 1.00 43.74  ? 55  PRO B CG  1 
ATOM   1170 C CD  . PRO B 1 56 ? 28.488  -21.849 -36.705 1.00 39.69  ? 55  PRO B CD  1 
ATOM   1171 N N   . LYS B 1 57 ? 25.115  -23.750 -36.467 1.00 37.46  ? 56  LYS B N   1 
ATOM   1172 C CA  . LYS B 1 57 ? 24.053  -24.751 -36.411 1.00 37.46  ? 56  LYS B CA  1 
ATOM   1173 C C   . LYS B 1 57 ? 22.805  -24.176 -35.740 1.00 37.49  ? 56  LYS B C   1 
ATOM   1174 O O   . LYS B 1 57 ? 21.686  -24.676 -35.948 1.00 35.78  ? 56  LYS B O   1 
ATOM   1175 C CB  . LYS B 1 57 ? 24.435  -26.101 -35.776 1.00 39.61  ? 56  LYS B CB  1 
ATOM   1176 C CG  . LYS B 1 57 ? 24.753  -26.076 -34.304 1.00 37.89  ? 56  LYS B CG  1 
ATOM   1177 C CD  . LYS B 1 57 ? 24.467  -27.413 -33.635 1.00 43.72  ? 56  LYS B CD  1 
ATOM   1178 C CE  . LYS B 1 57 ? 24.969  -27.427 -32.228 1.00 48.13  ? 56  LYS B CE  1 
ATOM   1179 N NZ  . LYS B 1 57 ? 24.170  -26.603 -31.316 1.00 53.62  ? 56  LYS B NZ  1 
ATOM   1180 N N   . ASP B 1 58 ? 23.008  -23.091 -34.989 1.00 37.95  ? 57  ASP B N   1 
ATOM   1181 C CA  . ASP B 1 58 ? 21.932  -22.503 -34.216 1.00 37.59  ? 57  ASP B CA  1 
ATOM   1182 C C   . ASP B 1 58 ? 21.538  -21.143 -34.774 1.00 41.46  ? 57  ASP B C   1 
ATOM   1183 O O   . ASP B 1 58 ? 20.726  -20.441 -34.128 1.00 36.08  ? 57  ASP B O   1 
ATOM   1184 C CB  . ASP B 1 58 ? 22.302  -22.385 -32.747 1.00 37.75  ? 57  ASP B CB  1 
ATOM   1185 C CG  . ASP B 1 58 ? 22.529  -23.693 -32.012 1.00 42.52  ? 57  ASP B CG  1 
ATOM   1186 O OD1 . ASP B 1 58 ? 21.614  -24.547 -32.054 1.00 42.24  ? 57  ASP B OD1 1 
ATOM   1187 O OD2 . ASP B 1 58 ? 23.585  -23.806 -31.350 1.00 41.71  ? 57  ASP B OD2 1 
ATOM   1188 N N   . LEU B 1 59 ? 22.104  -20.793 -35.951 1.00 33.28  ? 58  LEU B N   1 
ATOM   1189 C CA  . LEU B 1 59 ? 21.823  -19.498 -36.559 1.00 36.33  ? 58  LEU B CA  1 
ATOM   1190 C C   . LEU B 1 59 ? 21.076  -19.687 -37.867 1.00 35.68  ? 58  LEU B C   1 
ATOM   1191 O O   . LEU B 1 59 ? 21.558  -20.382 -38.747 1.00 37.87  ? 58  LEU B O   1 
ATOM   1192 C CB  . LEU B 1 59 ? 23.127  -18.720 -36.756 1.00 38.17  ? 58  LEU B CB  1 
ATOM   1193 C CG  . LEU B 1 59 ? 23.905  -18.436 -35.469 1.00 35.19  ? 58  LEU B CG  1 
ATOM   1194 C CD1 . LEU B 1 59 ? 25.276  -17.843 -35.754 1.00 34.28  ? 58  LEU B CD1 1 
ATOM   1195 C CD2 . LEU B 1 59 ? 23.069  -17.482 -34.605 1.00 29.51  ? 58  LEU B CD2 1 
ATOM   1196 N N   . PHE B 1 60 ? 19.910  -19.048 -37.976 1.00 33.87  ? 59  PHE B N   1 
ATOM   1197 C CA  . PHE B 1 60 ? 18.999  -19.238 -39.083 1.00 36.34  ? 59  PHE B CA  1 
ATOM   1198 C C   . PHE B 1 60 ? 18.802  -17.883 -39.778 1.00 40.72  ? 59  PHE B C   1 
ATOM   1199 O O   . PHE B 1 60 ? 18.185  -16.981 -39.215 1.00 32.89  ? 59  PHE B O   1 
ATOM   1200 C CB  . PHE B 1 60 ? 17.687  -19.831 -38.550 1.00 37.23  ? 59  PHE B CB  1 
ATOM   1201 C CG  . PHE B 1 60 ? 17.748  -21.244 -37.975 1.00 35.40  ? 59  PHE B CG  1 
ATOM   1202 C CD1 . PHE B 1 60 ? 18.158  -21.459 -36.662 1.00 39.11  ? 59  PHE B CD1 1 
ATOM   1203 C CD2 . PHE B 1 60 ? 17.387  -22.351 -38.746 1.00 31.15  ? 59  PHE B CD2 1 
ATOM   1204 C CE1 . PHE B 1 60 ? 18.260  -22.744 -36.146 1.00 35.71  ? 59  PHE B CE1 1 
ATOM   1205 C CE2 . PHE B 1 60 ? 17.420  -23.628 -38.200 1.00 32.74  ? 59  PHE B CE2 1 
ATOM   1206 C CZ  . PHE B 1 60 ? 17.881  -23.827 -36.914 1.00 32.85  ? 59  PHE B CZ  1 
ATOM   1207 N N   . PRO B 1 61 ? 19.316  -17.684 -41.019 1.00 45.16  ? 60  PRO B N   1 
ATOM   1208 C CA  . PRO B 1 61 ? 19.109  -16.421 -41.748 1.00 41.00  ? 60  PRO B CA  1 
ATOM   1209 C C   . PRO B 1 61 ? 17.659  -15.948 -41.680 1.00 39.32  ? 60  PRO B C   1 
ATOM   1210 O O   . PRO B 1 61 ? 16.733  -16.690 -42.011 1.00 36.79  ? 60  PRO B O   1 
ATOM   1211 C CB  . PRO B 1 61 ? 19.573  -16.770 -43.181 1.00 41.98  ? 60  PRO B CB  1 
ATOM   1212 C CG  . PRO B 1 61 ? 20.696  -17.767 -42.932 1.00 48.06  ? 60  PRO B CG  1 
ATOM   1213 C CD  . PRO B 1 61 ? 20.164  -18.631 -41.776 1.00 44.96  ? 60  PRO B CD  1 
ATOM   1214 N N   . TYR B 1 62 ? 17.474  -14.691 -41.233 1.00 38.66  ? 61  TYR B N   1 
ATOM   1215 C CA  . TYR B 1 62 ? 16.159  -14.213 -40.844 1.00 42.33  ? 61  TYR B CA  1 
ATOM   1216 C C   . TYR B 1 62 ? 15.193  -14.234 -42.012 1.00 41.98  ? 61  TYR B C   1 
ATOM   1217 O O   . TYR B 1 62 ? 14.043  -14.627 -41.842 1.00 48.86  ? 61  TYR B O   1 
ATOM   1218 C CB  . TYR B 1 62 ? 16.235  -12.786 -40.309 1.00 46.24  ? 61  TYR B CB  1 
ATOM   1219 C CG  . TYR B 1 62 ? 14.921  -12.047 -40.149 1.00 46.62  ? 61  TYR B CG  1 
ATOM   1220 C CD1 . TYR B 1 62 ? 14.111  -12.255 -39.034 1.00 50.00  ? 61  TYR B CD1 1 
ATOM   1221 C CD2 . TYR B 1 62 ? 14.536  -11.072 -41.066 1.00 53.82  ? 61  TYR B CD2 1 
ATOM   1222 C CE1 . TYR B 1 62 ? 12.925  -11.558 -38.867 1.00 48.16  ? 61  TYR B CE1 1 
ATOM   1223 C CE2 . TYR B 1 62 ? 13.356  -10.362 -40.904 1.00 54.95  ? 61  TYR B CE2 1 
ATOM   1224 C CZ  . TYR B 1 62 ? 12.555  -10.605 -39.800 1.00 52.83  ? 61  TYR B CZ  1 
ATOM   1225 O OH  . TYR B 1 62 ? 11.411  -9.884  -39.650 1.00 54.31  ? 61  TYR B OH  1 
ATOM   1226 N N   . ASP B 1 63 ? 15.678  -13.841 -43.194 1.00 51.34  ? 62  ASP B N   1 
ATOM   1227 C CA  . ASP B 1 63 ? 14.791  -13.616 -44.325 1.00 53.79  ? 62  ASP B CA  1 
ATOM   1228 C C   . ASP B 1 63 ? 14.179  -14.938 -44.762 1.00 47.24  ? 62  ASP B C   1 
ATOM   1229 O O   . ASP B 1 63 ? 12.966  -15.043 -44.874 1.00 46.57  ? 62  ASP B O   1 
ATOM   1230 C CB  . ASP B 1 63 ? 15.467  -12.820 -45.429 1.00 59.95  ? 62  ASP B CB  1 
ATOM   1231 C CG  . ASP B 1 63 ? 14.560  -11.737 -45.986 1.00 79.09  ? 62  ASP B CG  1 
ATOM   1232 O OD1 . ASP B 1 63 ? 14.113  -10.875 -45.176 1.00 80.19  ? 62  ASP B OD1 1 
ATOM   1233 O OD2 . ASP B 1 63 ? 14.268  -11.795 -47.198 1.00 84.99  ? 62  ASP B OD2 1 
ATOM   1234 N N   . LYS B 1 64 ? 15.034  -15.957 -44.910 1.00 49.62  ? 63  LYS B N   1 
ATOM   1235 C CA  . LYS B 1 64 ? 14.613  -17.328 -45.172 1.00 49.68  ? 63  LYS B CA  1 
ATOM   1236 C C   . LYS B 1 64 ? 13.637  -17.862 -44.116 1.00 44.70  ? 63  LYS B C   1 
ATOM   1237 O O   . LYS B 1 64 ? 12.767  -18.656 -44.441 1.00 46.64  ? 63  LYS B O   1 
ATOM   1238 C CB  . LYS B 1 64 ? 15.843  -18.249 -45.185 1.00 56.63  ? 63  LYS B CB  1 
ATOM   1239 C CG  . LYS B 1 64 ? 15.536  -19.713 -45.525 1.00 52.74  ? 63  LYS B CG  1 
ATOM   1240 C CD  . LYS B 1 64 ? 16.717  -20.619 -45.823 1.00 57.78  ? 63  LYS B CD  1 
ATOM   1241 C CE  . LYS B 1 64 ? 16.369  -21.858 -46.620 1.00 56.85  ? 63  LYS B CE  1 
ATOM   1242 N NZ  . LYS B 1 64 ? 15.266  -22.633 -46.061 1.00 57.75  ? 63  LYS B NZ  1 
ATOM   1243 N N   . SER B 1 65 ? 13.774  -17.477 -42.846 1.00 46.36  ? 64  SER B N   1 
ATOM   1244 C CA  . SER B 1 65 ? 13.125  -18.297 -41.827 1.00 45.49  ? 64  SER B CA  1 
ATOM   1245 C C   . SER B 1 65 ? 12.006  -17.572 -41.077 1.00 43.48  ? 64  SER B C   1 
ATOM   1246 O O   . SER B 1 65 ? 11.353  -18.157 -40.197 1.00 43.65  ? 64  SER B O   1 
ATOM   1247 C CB  . SER B 1 65 ? 14.138  -18.927 -40.927 1.00 43.38  ? 64  SER B CB  1 
ATOM   1248 O OG  . SER B 1 65 ? 15.136  -17.980 -40.600 1.00 63.22  ? 64  SER B OG  1 
ATOM   1249 N N   . LYS B 1 66 ? 11.724  -16.326 -41.488 1.00 42.88  ? 65  LYS B N   1 
ATOM   1250 C CA  . LYS B 1 66 ? 10.810  -15.461 -40.750 1.00 46.92  ? 65  LYS B CA  1 
ATOM   1251 C C   . LYS B 1 66 ? 9.387   -16.018 -40.708 1.00 47.22  ? 65  LYS B C   1 
ATOM   1252 O O   . LYS B 1 66 ? 8.704   -15.886 -39.683 1.00 53.33  ? 65  LYS B O   1 
ATOM   1253 C CB  . LYS B 1 66 ? 10.963  -13.969 -41.085 1.00 42.66  ? 65  LYS B CB  1 
ATOM   1254 C CG  . LYS B 1 66 ? 10.467  -13.475 -42.426 1.00 44.09  ? 65  LYS B CG  1 
ATOM   1255 N N   . ASP B 1 67 ? 8.921   -16.688 -41.772 1.00 50.22  ? 66  ASP B N   1 
ATOM   1256 C CA  . ASP B 1 67 ? 7.541   -17.154 -41.684 1.00 54.91  ? 66  ASP B CA  1 
ATOM   1257 C C   . ASP B 1 67 ? 7.426   -18.402 -40.802 1.00 55.23  ? 66  ASP B C   1 
ATOM   1258 O O   . ASP B 1 67 ? 6.365   -18.665 -40.219 1.00 50.28  ? 66  ASP B O   1 
ATOM   1259 C CB  . ASP B 1 67 ? 6.739   -17.057 -42.976 1.00 76.69  ? 66  ASP B CB  1 
ATOM   1260 C CG  . ASP B 1 67 ? 7.462   -17.359 -44.279 1.00 89.93  ? 66  ASP B CG  1 
ATOM   1261 O OD1 . ASP B 1 67 ? 6.843   -17.151 -45.354 1.00 80.95  ? 66  ASP B OD1 1 
ATOM   1262 O OD2 . ASP B 1 67 ? 8.629   -17.790 -44.208 1.00 97.68  ? 66  ASP B OD2 1 
ATOM   1263 N N   . LYS B 1 68 ? 8.525   -19.149 -40.654 1.00 45.59  ? 67  LYS B N   1 
ATOM   1264 C CA  . LYS B 1 68 ? 8.476   -20.295 -39.755 1.00 42.92  ? 67  LYS B CA  1 
ATOM   1265 C C   . LYS B 1 68 ? 8.550   -19.834 -38.297 1.00 42.07  ? 67  LYS B C   1 
ATOM   1266 O O   . LYS B 1 68 ? 7.685   -20.206 -37.500 1.00 43.53  ? 67  LYS B O   1 
ATOM   1267 C CB  . LYS B 1 68 ? 9.484   -21.349 -40.213 1.00 47.08  ? 67  LYS B CB  1 
ATOM   1268 C CG  . LYS B 1 68 ? 9.465   -22.652 -39.421 1.00 55.71  ? 67  LYS B CG  1 
ATOM   1269 C CD  . LYS B 1 68 ? 9.964   -23.793 -40.304 1.00 63.81  ? 67  LYS B CD  1 
ATOM   1270 C CE  . LYS B 1 68 ? 10.642  -24.909 -39.541 1.00 77.32  ? 67  LYS B CE  1 
ATOM   1271 N NZ  . LYS B 1 68 ? 9.844   -25.600 -38.520 1.00 67.78  ? 67  LYS B NZ  1 
ATOM   1272 N N   . TYR B 1 69 ? 9.539   -18.983 -37.970 1.00 43.64  ? 68  TYR B N   1 
ATOM   1273 C CA  . TYR B 1 69 ? 9.932   -18.723 -36.585 1.00 41.03  ? 68  TYR B CA  1 
ATOM   1274 C C   . TYR B 1 69 ? 9.401   -17.394 -36.070 1.00 46.36  ? 68  TYR B C   1 
ATOM   1275 O O   . TYR B 1 69 ? 9.484   -17.131 -34.864 1.00 40.79  ? 68  TYR B O   1 
ATOM   1276 C CB  . TYR B 1 69 ? 11.460  -18.702 -36.465 1.00 40.79  ? 68  TYR B CB  1 
ATOM   1277 C CG  . TYR B 1 69 ? 12.069  -20.070 -36.774 1.00 38.41  ? 68  TYR B CG  1 
ATOM   1278 C CD1 . TYR B 1 69 ? 11.524  -21.232 -36.233 1.00 40.18  ? 68  TYR B CD1 1 
ATOM   1279 C CD2 . TYR B 1 69 ? 13.179  -20.197 -37.612 1.00 41.84  ? 68  TYR B CD2 1 
ATOM   1280 C CE1 . TYR B 1 69 ? 12.086  -22.476 -36.493 1.00 44.73  ? 68  TYR B CE1 1 
ATOM   1281 C CE2 . TYR B 1 69 ? 13.723  -21.439 -37.916 1.00 44.08  ? 68  TYR B CE2 1 
ATOM   1282 C CZ  . TYR B 1 69 ? 13.173  -22.577 -37.345 1.00 41.52  ? 68  TYR B CZ  1 
ATOM   1283 O OH  . TYR B 1 69 ? 13.705  -23.789 -37.610 1.00 37.71  ? 68  TYR B OH  1 
ATOM   1284 N N   . GLY B 1 70 ? 8.874   -16.557 -36.975 1.00 39.10  ? 69  GLY B N   1 
ATOM   1285 C CA  . GLY B 1 70 ? 8.606   -15.174 -36.614 1.00 42.35  ? 69  GLY B CA  1 
ATOM   1286 C C   . GLY B 1 70 ? 7.189   -14.955 -36.079 1.00 49.55  ? 69  GLY B C   1 
ATOM   1287 O O   . GLY B 1 70 ? 6.583   -13.917 -36.356 1.00 49.22  ? 69  GLY B O   1 
ATOM   1288 N N   . LYS B 1 71 ? 6.680   -15.926 -35.310 1.00 48.63  ? 70  LYS B N   1 
ATOM   1289 C CA  . LYS B 1 71 ? 5.337   -15.857 -34.778 1.00 52.56  ? 70  LYS B CA  1 
ATOM   1290 C C   . LYS B 1 71 ? 5.420   -15.453 -33.318 1.00 59.77  ? 70  LYS B C   1 
ATOM   1291 O O   . LYS B 1 71 ? 6.249   -16.003 -32.584 1.00 58.13  ? 70  LYS B O   1 
ATOM   1292 C CB  . LYS B 1 71 ? 4.624   -17.209 -34.693 1.00 52.81  ? 70  LYS B CB  1 
ATOM   1293 C CG  . LYS B 1 71 ? 3.770   -17.622 -35.886 1.00 67.32  ? 70  LYS B CG  1 
ATOM   1294 C CD  . LYS B 1 71 ? 4.586   -18.047 -37.096 1.00 61.07  ? 70  LYS B CD  1 
ATOM   1295 C CE  . LYS B 1 71 ? 3.729   -18.595 -38.189 1.00 67.37  ? 70  LYS B CE  1 
ATOM   1296 N NZ  . LYS B 1 71 ? 4.368   -18.280 -39.472 1.00 67.90  ? 70  LYS B NZ  1 
ATOM   1297 N N   . PRO B 1 72 ? 4.532   -14.533 -32.866 1.00 61.41  ? 71  PRO B N   1 
ATOM   1298 C CA  . PRO B 1 72 ? 4.491   -14.118 -31.458 1.00 57.26  ? 71  PRO B CA  1 
ATOM   1299 C C   . PRO B 1 72 ? 4.227   -15.297 -30.520 1.00 57.47  ? 71  PRO B C   1 
ATOM   1300 O O   . PRO B 1 72 ? 3.545   -16.239 -30.912 1.00 48.21  ? 71  PRO B O   1 
ATOM   1301 C CB  . PRO B 1 72 ? 3.396   -13.018 -31.384 1.00 52.18  ? 71  PRO B CB  1 
ATOM   1302 C CG  . PRO B 1 72 ? 3.117   -12.666 -32.824 1.00 60.21  ? 71  PRO B CG  1 
ATOM   1303 C CD  . PRO B 1 72 ? 3.542   -13.834 -33.706 1.00 54.77  ? 71  PRO B CD  1 
ATOM   1304 N N   . ASN B 1 73 ? 4.802   -15.256 -29.303 1.00 47.84  ? 72  ASN B N   1 
ATOM   1305 C CA  . ASN B 1 73 ? 4.521   -16.256 -28.276 1.00 44.31  ? 72  ASN B CA  1 
ATOM   1306 C C   . ASN B 1 73 ? 4.502   -15.587 -26.890 1.00 51.15  ? 72  ASN B C   1 
ATOM   1307 O O   . ASN B 1 73 ? 4.464   -14.361 -26.803 1.00 46.02  ? 72  ASN B O   1 
ATOM   1308 C CB  . ASN B 1 73 ? 5.505   -17.414 -28.359 1.00 41.13  ? 72  ASN B CB  1 
ATOM   1309 C CG  . ASN B 1 73 ? 6.921   -16.940 -28.159 1.00 41.71  ? 72  ASN B CG  1 
ATOM   1310 O OD1 . ASN B 1 73 ? 7.152   -16.136 -27.252 1.00 37.12  ? 72  ASN B OD1 1 
ATOM   1311 N ND2 . ASN B 1 73 ? 7.862   -17.372 -28.995 1.00 39.65  ? 72  ASN B ND2 1 
ATOM   1312 N N   . LYS B 1 74 ? 4.571   -16.387 -25.810 1.00 49.62  ? 73  LYS B N   1 
ATOM   1313 C CA  . LYS B 1 74 ? 4.440   -15.858 -24.451 1.00 56.92  ? 73  LYS B CA  1 
ATOM   1314 C C   . LYS B 1 74 ? 5.800   -15.684 -23.739 1.00 46.21  ? 73  LYS B C   1 
ATOM   1315 O O   . LYS B 1 74 ? 5.838   -15.545 -22.516 1.00 40.53  ? 73  LYS B O   1 
ATOM   1316 C CB  . LYS B 1 74 ? 3.419   -16.669 -23.629 1.00 39.23  ? 73  LYS B CB  1 
ATOM   1317 N N   . ARG B 1 75 ? 6.922   -15.701 -24.472 1.00 37.35  ? 74  ARG B N   1 
ATOM   1318 C CA  . ARG B 1 75 ? 8.218   -15.591 -23.808 1.00 33.98  ? 74  ARG B CA  1 
ATOM   1319 C C   . ARG B 1 75 ? 8.569   -14.113 -23.679 1.00 39.04  ? 74  ARG B C   1 
ATOM   1320 O O   . ARG B 1 75 ? 8.378   -13.338 -24.633 1.00 42.57  ? 74  ARG B O   1 
ATOM   1321 C CB  . ARG B 1 75 ? 9.328   -16.446 -24.444 1.00 35.58  ? 74  ARG B CB  1 
ATOM   1322 C CG  . ARG B 1 75 ? 8.941   -17.892 -24.730 1.00 35.11  ? 74  ARG B CG  1 
ATOM   1323 C CD  . ARG B 1 75 ? 9.022   -18.672 -23.422 1.00 38.30  ? 74  ARG B CD  1 
ATOM   1324 N NE  . ARG B 1 75 ? 9.138   -20.114 -23.643 1.00 35.85  ? 74  ARG B NE  1 
ATOM   1325 C CZ  . ARG B 1 75 ? 10.257  -20.759 -23.470 1.00 35.01  ? 74  ARG B CZ  1 
ATOM   1326 N NH1 . ARG B 1 75 ? 11.360  -20.132 -23.087 1.00 39.61  ? 74  ARG B NH1 1 
ATOM   1327 N NH2 . ARG B 1 75 ? 10.289  -22.042 -23.726 1.00 36.11  ? 74  ARG B NH2 1 
ATOM   1328 N N   . LYS B 1 76 ? 9.041   -13.723 -22.480 1.00 34.41  ? 75  LYS B N   1 
ATOM   1329 C CA  . LYS B 1 76 ? 9.297   -12.326 -22.178 1.00 31.35  ? 75  LYS B CA  1 
ATOM   1330 C C   . LYS B 1 76 ? 10.372  -11.770 -23.113 1.00 31.96  ? 75  LYS B C   1 
ATOM   1331 O O   . LYS B 1 76 ? 11.496  -12.289 -23.177 1.00 33.29  ? 75  LYS B O   1 
ATOM   1332 C CB  . LYS B 1 76 ? 9.755   -12.175 -20.719 1.00 34.70  ? 75  LYS B CB  1 
ATOM   1333 C CG  . LYS B 1 76 ? 10.232  -10.747 -20.382 1.00 40.24  ? 75  LYS B CG  1 
ATOM   1334 C CD  . LYS B 1 76 ? 10.795  -10.644 -18.967 1.00 42.68  ? 75  LYS B CD  1 
ATOM   1335 C CE  . LYS B 1 76 ? 11.178  -9.277  -18.487 1.00 48.17  ? 75  LYS B CE  1 
ATOM   1336 N NZ  . LYS B 1 76 ? 11.116  -9.250  -17.013 1.00 48.99  ? 75  LYS B NZ  1 
ATOM   1337 N N   . GLY B 1 77 ? 10.016  -10.696 -23.813 1.00 32.37  ? 76  GLY B N   1 
ATOM   1338 C CA  . GLY B 1 77 ? 10.973  -9.986  -24.645 1.00 33.98  ? 76  GLY B CA  1 
ATOM   1339 C C   . GLY B 1 77 ? 10.822  -10.346 -26.131 1.00 36.04  ? 76  GLY B C   1 
ATOM   1340 O O   . GLY B 1 77 ? 11.377  -9.675  -26.977 1.00 37.93  ? 76  GLY B O   1 
ATOM   1341 N N   . PHE B 1 78 ? 9.988   -11.337 -26.457 1.00 39.95  ? 77  PHE B N   1 
ATOM   1342 C CA  . PHE B 1 78 ? 9.951   -11.933 -27.793 1.00 32.24  ? 77  PHE B CA  1 
ATOM   1343 C C   . PHE B 1 78 ? 9.207   -11.032 -28.754 1.00 32.10  ? 77  PHE B C   1 
ATOM   1344 O O   . PHE B 1 78 ? 9.657   -10.795 -29.857 1.00 32.91  ? 77  PHE B O   1 
ATOM   1345 C CB  . PHE B 1 78 ? 9.236   -13.285 -27.804 1.00 32.11  ? 77  PHE B CB  1 
ATOM   1346 C CG  . PHE B 1 78 ? 9.478   -14.064 -29.092 1.00 34.36  ? 77  PHE B CG  1 
ATOM   1347 C CD1 . PHE B 1 78 ? 10.589  -14.902 -29.216 1.00 32.85  ? 77  PHE B CD1 1 
ATOM   1348 C CD2 . PHE B 1 78 ? 8.607   -13.933 -30.173 1.00 38.20  ? 77  PHE B CD2 1 
ATOM   1349 C CE1 . PHE B 1 78 ? 10.814  -15.591 -30.397 1.00 36.84  ? 77  PHE B CE1 1 
ATOM   1350 C CE2 . PHE B 1 78 ? 8.830   -14.642 -31.349 1.00 38.37  ? 77  PHE B CE2 1 
ATOM   1351 C CZ  . PHE B 1 78 ? 9.938   -15.465 -31.456 1.00 37.97  ? 77  PHE B CZ  1 
ATOM   1352 N N   . ASN B 1 79 ? 8.035   -10.563 -28.339 1.00 35.43  ? 78  ASN B N   1 
ATOM   1353 C CA  . ASN B 1 79 ? 7.289   -9.676  -29.194 1.00 34.87  ? 78  ASN B CA  1 
ATOM   1354 C C   . ASN B 1 79 ? 8.042   -8.349  -29.312 1.00 35.27  ? 78  ASN B C   1 
ATOM   1355 O O   . ASN B 1 79 ? 8.013   -7.713  -30.353 1.00 40.93  ? 78  ASN B O   1 
ATOM   1356 C CB  . ASN B 1 79 ? 5.832   -9.543  -28.745 1.00 41.39  ? 78  ASN B CB  1 
ATOM   1357 C CG  . ASN B 1 79 ? 5.065   -10.854 -28.741 1.00 49.48  ? 78  ASN B CG  1 
ATOM   1358 O OD1 . ASN B 1 79 ? 5.507   -11.891 -29.269 1.00 44.61  ? 78  ASN B OD1 1 
ATOM   1359 N ND2 . ASN B 1 79 ? 3.891   -10.831 -28.130 1.00 48.19  ? 78  ASN B ND2 1 
ATOM   1360 N N   . GLU B 1 80 ? 8.699   -7.893  -28.251 1.00 37.08  ? 79  GLU B N   1 
ATOM   1361 C CA  . GLU B 1 80 ? 9.520   -6.696  -28.417 1.00 44.49  ? 79  GLU B CA  1 
ATOM   1362 C C   . GLU B 1 80 ? 10.641  -6.941  -29.440 1.00 39.36  ? 79  GLU B C   1 
ATOM   1363 O O   . GLU B 1 80 ? 10.953  -6.047  -30.223 1.00 37.48  ? 79  GLU B O   1 
ATOM   1364 C CB  . GLU B 1 80 ? 10.000  -6.111  -27.092 1.00 39.77  ? 79  GLU B CB  1 
ATOM   1365 C CG  . GLU B 1 80 ? 8.874   -5.353  -26.390 1.00 50.50  ? 79  GLU B CG  1 
ATOM   1366 N N   . GLY B 1 81 ? 11.193  -8.164  -29.429 1.00 35.07  ? 80  GLY B N   1 
ATOM   1367 C CA  . GLY B 1 81 ? 12.261  -8.628  -30.299 1.00 35.41  ? 80  GLY B CA  1 
ATOM   1368 C C   . GLY B 1 81 ? 11.799  -8.623  -31.749 1.00 39.07  ? 80  GLY B C   1 
ATOM   1369 O O   . GLY B 1 81 ? 12.540  -8.184  -32.630 1.00 39.66  ? 80  GLY B O   1 
ATOM   1370 N N   . LEU B 1 82 ? 10.572  -9.103  -31.973 1.00 33.77  ? 81  LEU B N   1 
ATOM   1371 C CA  . LEU B 1 82 ? 10.008  -9.132  -33.317 1.00 40.72  ? 81  LEU B CA  1 
ATOM   1372 C C   . LEU B 1 82 ? 9.873   -7.698  -33.799 1.00 39.02  ? 81  LEU B C   1 
ATOM   1373 O O   . LEU B 1 82 ? 10.154  -7.424  -34.954 1.00 38.23  ? 81  LEU B O   1 
ATOM   1374 C CB  . LEU B 1 82 ? 8.672   -9.865  -33.441 1.00 32.95  ? 81  LEU B CB  1 
ATOM   1375 C CG  . LEU B 1 82 ? 8.716   -11.349 -33.079 1.00 34.92  ? 81  LEU B CG  1 
ATOM   1376 C CD1 . LEU B 1 82 ? 7.331   -11.983 -33.158 1.00 38.93  ? 81  LEU B CD1 1 
ATOM   1377 C CD2 . LEU B 1 82 ? 9.669   -12.054 -34.024 1.00 33.88  ? 81  LEU B CD2 1 
ATOM   1378 N N   . TRP B 1 83 ? 9.469   -6.793  -32.893 1.00 33.69  ? 82  TRP B N   1 
ATOM   1379 C CA  . TRP B 1 83 ? 9.357   -5.388  -33.243 1.00 35.59  ? 82  TRP B CA  1 
ATOM   1380 C C   . TRP B 1 83 ? 10.719  -4.824  -33.661 1.00 35.89  ? 82  TRP B C   1 
ATOM   1381 O O   . TRP B 1 83 ? 10.816  -4.105  -34.651 1.00 43.22  ? 82  TRP B O   1 
ATOM   1382 C CB  . TRP B 1 83 ? 8.748   -4.554  -32.096 1.00 34.66  ? 82  TRP B CB  1 
ATOM   1383 C CG  . TRP B 1 83 ? 8.460   -3.155  -32.564 1.00 39.67  ? 82  TRP B CG  1 
ATOM   1384 C CD1 . TRP B 1 83 ? 7.304   -2.724  -33.145 1.00 40.95  ? 82  TRP B CD1 1 
ATOM   1385 C CD2 . TRP B 1 83 ? 9.386   -2.043  -32.611 1.00 42.74  ? 82  TRP B CD2 1 
ATOM   1386 N NE1 . TRP B 1 83 ? 7.431   -1.414  -33.505 1.00 43.24  ? 82  TRP B NE1 1 
ATOM   1387 C CE2 . TRP B 1 83 ? 8.698   -0.972  -33.216 1.00 39.30  ? 82  TRP B CE2 1 
ATOM   1388 C CE3 . TRP B 1 83 ? 10.717  -1.843  -32.198 1.00 44.34  ? 82  TRP B CE3 1 
ATOM   1389 C CZ2 . TRP B 1 83 ? 9.288   0.281   -33.409 1.00 38.91  ? 82  TRP B CZ2 1 
ATOM   1390 C CZ3 . TRP B 1 83 ? 11.309  -0.605  -32.390 1.00 42.37  ? 82  TRP B CZ3 1 
ATOM   1391 C CH2 . TRP B 1 83 ? 10.600  0.435   -33.004 1.00 48.04  ? 82  TRP B CH2 1 
ATOM   1392 N N   . GLU B 1 84 ? 11.761  -5.126  -32.880 1.00 33.84  ? 83  GLU B N   1 
ATOM   1393 C CA  . GLU B 1 84 ? 13.058  -4.498  -33.078 1.00 35.41  ? 83  GLU B CA  1 
ATOM   1394 C C   . GLU B 1 84 ? 13.693  -4.972  -34.388 1.00 35.68  ? 83  GLU B C   1 
ATOM   1395 O O   . GLU B 1 84 ? 14.354  -4.188  -35.097 1.00 35.37  ? 83  GLU B O   1 
ATOM   1396 C CB  . GLU B 1 84 ? 14.027  -4.771  -31.931 1.00 33.00  ? 83  GLU B CB  1 
ATOM   1397 C CG  . GLU B 1 84 ? 13.533  -4.181  -30.615 1.00 37.81  ? 83  GLU B CG  1 
ATOM   1398 C CD  . GLU B 1 84 ? 14.439  -4.448  -29.444 1.00 31.53  ? 83  GLU B CD  1 
ATOM   1399 O OE1 . GLU B 1 84 ? 15.411  -5.224  -29.563 1.00 32.27  ? 83  GLU B OE1 1 
ATOM   1400 O OE2 . GLU B 1 84 ? 14.185  -3.839  -28.378 1.00 42.10  ? 83  GLU B OE2 1 
ATOM   1401 N N   . ILE B 1 85 ? 13.518  -6.254  -34.687 1.00 32.48  ? 84  ILE B N   1 
ATOM   1402 C CA  . ILE B 1 85 ? 14.243  -6.791  -35.834 1.00 36.72  ? 84  ILE B CA  1 
ATOM   1403 C C   . ILE B 1 85 ? 13.600  -6.256  -37.116 1.00 38.92  ? 84  ILE B C   1 
ATOM   1404 O O   . ILE B 1 85 ? 14.256  -6.119  -38.144 1.00 38.70  ? 84  ILE B O   1 
ATOM   1405 C CB  . ILE B 1 85 ? 14.297  -8.324  -35.797 1.00 34.38  ? 84  ILE B CB  1 
ATOM   1406 C CG1 . ILE B 1 85 ? 15.346  -8.856  -36.785 1.00 34.85  ? 84  ILE B CG1 1 
ATOM   1407 C CG2 . ILE B 1 85 ? 12.927  -8.941  -36.069 1.00 33.06  ? 84  ILE B CG2 1 
ATOM   1408 C CD1 . ILE B 1 85 ? 15.619  -10.350 -36.674 1.00 34.65  ? 84  ILE B CD1 1 
ATOM   1409 N N   . GLN B 1 86 ? 12.296  -5.980  -37.041 1.00 39.47  ? 85  GLN B N   1 
ATOM   1410 C CA  . GLN B 1 86 ? 11.528  -5.475  -38.163 1.00 37.93  ? 85  GLN B CA  1 
ATOM   1411 C C   . GLN B 1 86 ? 11.689  -3.954  -38.314 1.00 41.94  ? 85  GLN B C   1 
ATOM   1412 O O   . GLN B 1 86 ? 11.644  -3.444  -39.429 1.00 41.68  ? 85  GLN B O   1 
ATOM   1413 C CB  . GLN B 1 86 ? 10.065  -5.891  -37.986 1.00 44.13  ? 85  GLN B CB  1 
ATOM   1414 N N   . ASN B 1 87 ? 11.855  -3.200  -37.219 1.00 35.50  ? 86  ASN B N   1 
ATOM   1415 C CA  . ASN B 1 87 ? 11.745  -1.749  -37.356 1.00 36.62  ? 86  ASN B CA  1 
ATOM   1416 C C   . ASN B 1 87 ? 13.087  -1.040  -37.205 1.00 37.27  ? 86  ASN B C   1 
ATOM   1417 O O   . ASN B 1 87 ? 13.239  0.084   -37.683 1.00 39.35  ? 86  ASN B O   1 
ATOM   1418 C CB  . ASN B 1 87 ? 10.718  -1.172  -36.383 1.00 45.75  ? 86  ASN B CB  1 
ATOM   1419 C CG  . ASN B 1 87 ? 9.344   -1.703  -36.697 1.00 47.46  ? 86  ASN B CG  1 
ATOM   1420 O OD1 . ASN B 1 87 ? 8.805   -1.374  -37.749 1.00 58.17  ? 86  ASN B OD1 1 
ATOM   1421 N ND2 . ASN B 1 87 ? 8.824   -2.606  -35.882 1.00 44.12  ? 86  ASN B ND2 1 
ATOM   1422 N N   . ASN B 1 88 ? 14.058  -1.669  -36.518 1.00 36.41  ? 87  ASN B N   1 
ATOM   1423 C CA  . ASN B 1 88 ? 15.293  -0.946  -36.233 1.00 39.37  ? 87  ASN B CA  1 
ATOM   1424 C C   . ASN B 1 88 ? 16.376  -1.940  -35.844 1.00 36.78  ? 87  ASN B C   1 
ATOM   1425 O O   . ASN B 1 88 ? 16.998  -1.842  -34.775 1.00 35.74  ? 87  ASN B O   1 
ATOM   1426 C CB  . ASN B 1 88 ? 15.091  0.224   -35.269 1.00 40.93  ? 87  ASN B CB  1 
ATOM   1427 C CG  . ASN B 1 88 ? 16.175  1.277   -35.412 1.00 41.19  ? 87  ASN B CG  1 
ATOM   1428 O OD1 . ASN B 1 88 ? 17.253  1.073   -35.999 1.00 35.99  ? 87  ASN B OD1 1 
ATOM   1429 N ND2 . ASN B 1 88 ? 15.922  2.424   -34.830 1.00 39.68  ? 87  ASN B ND2 1 
ATOM   1430 N N   . PRO B 1 89 ? 16.608  -2.939  -36.728 1.00 36.72  ? 88  PRO B N   1 
ATOM   1431 C CA  . PRO B 1 89 ? 17.517  -4.034  -36.431 1.00 32.08  ? 88  PRO B CA  1 
ATOM   1432 C C   . PRO B 1 89 ? 18.920  -3.575  -36.082 1.00 35.28  ? 88  PRO B C   1 
ATOM   1433 O O   . PRO B 1 89 ? 19.658  -4.351  -35.478 1.00 32.24  ? 88  PRO B O   1 
ATOM   1434 C CB  . PRO B 1 89 ? 17.514  -4.860  -37.761 1.00 32.94  ? 88  PRO B CB  1 
ATOM   1435 C CG  . PRO B 1 89 ? 17.063  -3.864  -38.843 1.00 34.35  ? 88  PRO B CG  1 
ATOM   1436 C CD  . PRO B 1 89 ? 15.996  -3.064  -38.069 1.00 36.53  ? 88  PRO B CD  1 
ATOM   1437 N N   . HIS B 1 90 ? 19.310  -2.369  -36.558 1.00 33.84  ? 89  HIS B N   1 
ATOM   1438 C CA  . HIS B 1 90 ? 20.710  -1.953  -36.486 1.00 34.12  ? 89  HIS B CA  1 
ATOM   1439 C C   . HIS B 1 90 ? 20.921  -0.867  -35.422 1.00 33.15  ? 89  HIS B C   1 
ATOM   1440 O O   . HIS B 1 90 ? 22.024  -0.341  -35.288 1.00 32.95  ? 89  HIS B O   1 
ATOM   1441 C CB  . HIS B 1 90 ? 21.252  -1.536  -37.865 1.00 32.95  ? 89  HIS B CB  1 
ATOM   1442 C CG  . HIS B 1 90 ? 21.139  -2.667  -38.857 1.00 34.29  ? 89  HIS B CG  1 
ATOM   1443 N ND1 . HIS B 1 90 ? 21.760  -3.897  -38.711 1.00 32.51  ? 89  HIS B ND1 1 
ATOM   1444 C CD2 . HIS B 1 90 ? 20.408  -2.747  -39.978 1.00 30.95  ? 89  HIS B CD2 1 
ATOM   1445 C CE1 . HIS B 1 90 ? 21.422  -4.673  -39.739 1.00 32.48  ? 89  HIS B CE1 1 
ATOM   1446 N NE2 . HIS B 1 90 ? 20.616  -3.975  -40.530 1.00 31.00  ? 89  HIS B NE2 1 
ATOM   1447 N N   . ALA B 1 91 ? 19.904  -0.594  -34.610 1.00 34.11  ? 90  ALA B N   1 
ATOM   1448 C CA  . ALA B 1 91 ? 20.053  0.451   -33.591 1.00 40.93  ? 90  ALA B CA  1 
ATOM   1449 C C   . ALA B 1 91 ? 21.033  0.025   -32.497 1.00 40.92  ? 90  ALA B C   1 
ATOM   1450 O O   . ALA B 1 91 ? 21.377  -1.130  -32.361 1.00 37.20  ? 90  ALA B O   1 
ATOM   1451 C CB  . ALA B 1 91 ? 18.696  0.819   -32.968 1.00 30.72  ? 90  ALA B CB  1 
ATOM   1452 N N   . SER B 1 92 ? 21.492  1.000   -31.714 1.00 44.53  ? 91  SER B N   1 
ATOM   1453 C CA  . SER B 1 92 ? 22.177  0.746   -30.470 1.00 52.34  ? 91  SER B CA  1 
ATOM   1454 C C   . SER B 1 92 ? 21.108  0.517   -29.406 1.00 51.34  ? 91  SER B C   1 
ATOM   1455 O O   . SER B 1 92 ? 20.164  1.306   -29.320 1.00 48.31  ? 91  SER B O   1 
ATOM   1456 C CB  . SER B 1 92 ? 23.029  1.930   -30.108 1.00 52.75  ? 91  SER B CB  1 
ATOM   1457 O OG  . SER B 1 92 ? 23.669  1.634   -28.883 1.00 52.75  ? 91  SER B OG  1 
ATOM   1458 N N   . TYR B 1 93 ? 21.238  -0.591  -28.661 1.00 43.27  ? 92  TYR B N   1 
ATOM   1459 C CA  . TYR B 1 93 ? 20.316  -0.957  -27.594 1.00 47.33  ? 92  TYR B CA  1 
ATOM   1460 C C   . TYR B 1 93 ? 21.107  -0.937  -26.285 1.00 53.70  ? 92  TYR B C   1 
ATOM   1461 O O   . TYR B 1 93 ? 20.660  -1.457  -25.268 1.00 48.53  ? 92  TYR B O   1 
ATOM   1462 C CB  . TYR B 1 93 ? 19.603  -2.284  -27.890 1.00 38.53  ? 92  TYR B CB  1 
ATOM   1463 C CG  . TYR B 1 93 ? 18.616  -2.203  -29.053 1.00 35.60  ? 92  TYR B CG  1 
ATOM   1464 C CD1 . TYR B 1 93 ? 17.344  -1.690  -28.860 1.00 33.90  ? 92  TYR B CD1 1 
ATOM   1465 C CD2 . TYR B 1 93 ? 18.966  -2.583  -30.353 1.00 36.22  ? 92  TYR B CD2 1 
ATOM   1466 C CE1 . TYR B 1 93 ? 16.431  -1.569  -29.894 1.00 35.55  ? 92  TYR B CE1 1 
ATOM   1467 C CE2 . TYR B 1 93 ? 18.049  -2.496  -31.394 1.00 30.89  ? 92  TYR B CE2 1 
ATOM   1468 C CZ  . TYR B 1 93 ? 16.773  -2.014  -31.157 1.00 31.30  ? 92  TYR B CZ  1 
ATOM   1469 O OH  . TYR B 1 93 ? 15.826  -1.864  -32.127 1.00 33.25  ? 92  TYR B OH  1 
ATOM   1470 N N   . SER B 1 94 ? 22.287  -0.306  -26.375 1.00 68.49  ? 93  SER B N   1 
ATOM   1471 C CA  . SER B 1 94 ? 23.171  0.107   -25.294 1.00 78.15  ? 93  SER B CA  1 
ATOM   1472 C C   . SER B 1 94 ? 22.370  0.378   -24.016 1.00 84.09  ? 93  SER B C   1 
ATOM   1473 O O   . SER B 1 94 ? 21.579  1.356   -24.031 1.00 68.79  ? 93  SER B O   1 
ATOM   1474 C CB  . SER B 1 94 ? 23.924  1.352   -25.684 1.00 71.17  ? 93  SER B CB  1 
ATOM   1475 O OG  . SER B 1 94 ? 24.773  1.102   -26.792 1.00 66.18  ? 93  SER B OG  1 
ATOM   1476 O OXT . SER B 1 94 ? 22.574  -0.390  -23.057 1.00 96.55  ? 93  SER B OXT 1 
ATOM   1477 N N   . HIS C 1 4  ? 32.965  -23.910 27.653  1.00 97.48  ? 3   HIS C N   1 
ATOM   1478 C CA  . HIS C 1 4  ? 31.773  -23.018 27.602  1.00 101.91 ? 3   HIS C CA  1 
ATOM   1479 C C   . HIS C 1 4  ? 30.936  -23.256 28.863  1.00 94.11  ? 3   HIS C C   1 
ATOM   1480 O O   . HIS C 1 4  ? 31.413  -23.895 29.801  1.00 86.38  ? 3   HIS C O   1 
ATOM   1481 C CB  . HIS C 1 4  ? 31.039  -23.215 26.267  1.00 111.50 ? 3   HIS C CB  1 
ATOM   1482 C CG  . HIS C 1 4  ? 30.181  -22.060 25.853  1.00 120.41 ? 3   HIS C CG  1 
ATOM   1483 N ND1 . HIS C 1 4  ? 30.622  -21.072 24.997  1.00 127.95 ? 3   HIS C ND1 1 
ATOM   1484 C CD2 . HIS C 1 4  ? 28.919  -21.736 26.168  1.00 117.05 ? 3   HIS C CD2 1 
ATOM   1485 C CE1 . HIS C 1 4  ? 29.656  -20.182 24.818  1.00 118.44 ? 3   HIS C CE1 1 
ATOM   1486 N NE2 . HIS C 1 4  ? 28.612  -20.567 25.521  1.00 118.44 ? 3   HIS C NE2 1 
ATOM   1487 N N   . ALA C 1 5  ? 29.693  -22.744 28.862  1.00 83.90  ? 4   ALA C N   1 
ATOM   1488 C CA  . ALA C 1 5  ? 28.768  -22.804 29.984  1.00 74.55  ? 4   ALA C CA  1 
ATOM   1489 C C   . ALA C 1 5  ? 27.335  -22.960 29.482  1.00 85.76  ? 4   ALA C C   1 
ATOM   1490 O O   . ALA C 1 5  ? 26.944  -22.260 28.546  1.00 89.54  ? 4   ALA C O   1 
ATOM   1491 C CB  . ALA C 1 5  ? 28.866  -21.499 30.707  1.00 81.68  ? 4   ALA C CB  1 
ATOM   1492 N N   . PHE C 1 6  ? 26.533  -23.812 30.145  1.00 67.97  ? 5   PHE C N   1 
ATOM   1493 C CA  . PHE C 1 6  ? 25.154  -23.993 29.709  1.00 68.52  ? 5   PHE C CA  1 
ATOM   1494 C C   . PHE C 1 6  ? 24.235  -24.148 30.919  1.00 74.46  ? 5   PHE C C   1 
ATOM   1495 O O   . PHE C 1 6  ? 24.470  -25.013 31.760  1.00 93.69  ? 5   PHE C O   1 
ATOM   1496 C CB  . PHE C 1 6  ? 25.042  -25.207 28.772  1.00 54.91  ? 5   PHE C CB  1 
ATOM   1497 C CG  . PHE C 1 6  ? 25.854  -25.196 27.477  1.00 48.99  ? 5   PHE C CG  1 
ATOM   1498 C CD1 . PHE C 1 6  ? 26.959  -26.024 27.315  1.00 54.36  ? 5   PHE C CD1 1 
ATOM   1499 C CD2 . PHE C 1 6  ? 25.511  -24.374 26.411  1.00 50.51  ? 5   PHE C CD2 1 
ATOM   1500 C CE1 . PHE C 1 6  ? 27.699  -26.024 26.126  1.00 58.21  ? 5   PHE C CE1 1 
ATOM   1501 C CE2 . PHE C 1 6  ? 26.240  -24.391 25.216  1.00 46.85  ? 5   PHE C CE2 1 
ATOM   1502 C CZ  . PHE C 1 6  ? 27.334  -25.206 25.076  1.00 50.30  ? 5   PHE C CZ  1 
ATOM   1503 N N   . LYS C 1 7  ? 23.179  -23.327 30.995  1.00 67.84  ? 6   LYS C N   1 
ATOM   1504 C CA  . LYS C 1 7  ? 22.195  -23.455 32.069  1.00 65.87  ? 6   LYS C CA  1 
ATOM   1505 C C   . LYS C 1 7  ? 20.834  -23.765 31.450  1.00 59.19  ? 6   LYS C C   1 
ATOM   1506 O O   . LYS C 1 7  ? 20.674  -23.646 30.240  1.00 62.60  ? 6   LYS C O   1 
ATOM   1507 C CB  . LYS C 1 7  ? 22.214  -22.282 33.064  1.00 72.99  ? 6   LYS C CB  1 
ATOM   1508 C CG  . LYS C 1 7  ? 21.493  -20.990 32.664  1.00 73.18  ? 6   LYS C CG  1 
ATOM   1509 C CD  . LYS C 1 7  ? 22.382  -19.752 32.712  1.00 65.19  ? 6   LYS C CD  1 
ATOM   1510 N N   . PRO C 1 8  ? 19.809  -24.210 32.216  1.00 65.09  ? 7   PRO C N   1 
ATOM   1511 C CA  . PRO C 1 8  ? 18.522  -24.559 31.604  1.00 69.93  ? 7   PRO C CA  1 
ATOM   1512 C C   . PRO C 1 8  ? 17.952  -23.403 30.779  1.00 77.06  ? 7   PRO C C   1 
ATOM   1513 O O   . PRO C 1 8  ? 18.146  -22.239 31.129  1.00 79.68  ? 7   PRO C O   1 
ATOM   1514 C CB  . PRO C 1 8  ? 17.640  -24.961 32.795  1.00 74.26  ? 7   PRO C CB  1 
ATOM   1515 C CG  . PRO C 1 8  ? 18.643  -25.373 33.859  1.00 66.12  ? 7   PRO C CG  1 
ATOM   1516 C CD  . PRO C 1 8  ? 19.824  -24.428 33.673  1.00 66.39  ? 7   PRO C CD  1 
ATOM   1517 N N   . GLY C 1 9  ? 17.313  -23.742 29.648  1.00 74.81  ? 8   GLY C N   1 
ATOM   1518 C CA  . GLY C 1 9  ? 16.655  -22.775 28.783  1.00 65.36  ? 8   GLY C CA  1 
ATOM   1519 C C   . GLY C 1 9  ? 17.525  -22.315 27.607  1.00 66.03  ? 8   GLY C C   1 
ATOM   1520 O O   . GLY C 1 9  ? 16.985  -21.962 26.559  1.00 72.93  ? 8   GLY C O   1 
ATOM   1521 N N   . ASP C 1 10 ? 18.857  -22.305 27.796  1.00 47.93  ? 9   ASP C N   1 
ATOM   1522 C CA  . ASP C 1 10 ? 19.837  -21.931 26.794  1.00 42.73  ? 9   ASP C CA  1 
ATOM   1523 C C   . ASP C 1 10 ? 19.599  -22.698 25.491  1.00 43.15  ? 9   ASP C C   1 
ATOM   1524 O O   . ASP C 1 10 ? 19.396  -23.900 25.491  1.00 45.94  ? 9   ASP C O   1 
ATOM   1525 C CB  . ASP C 1 10 ? 21.257  -22.235 27.255  1.00 44.37  ? 9   ASP C CB  1 
ATOM   1526 C CG  . ASP C 1 10 ? 21.885  -21.287 28.273  1.00 62.69  ? 9   ASP C CG  1 
ATOM   1527 O OD1 . ASP C 1 10 ? 21.118  -20.588 28.976  1.00 66.74  ? 9   ASP C OD1 1 
ATOM   1528 O OD2 . ASP C 1 10 ? 23.147  -21.221 28.339  1.00 64.54  ? 9   ASP C OD2 1 
ATOM   1529 N N   . LEU C 1 11 ? 19.662  -22.001 24.359  1.00 45.23  ? 10  LEU C N   1 
ATOM   1530 C CA  . LEU C 1 11 ? 19.320  -22.620 23.092  1.00 46.64  ? 10  LEU C CA  1 
ATOM   1531 C C   . LEU C 1 11 ? 20.607  -23.025 22.371  1.00 43.41  ? 10  LEU C C   1 
ATOM   1532 O O   . LEU C 1 11 ? 21.582  -22.282 22.345  1.00 44.41  ? 10  LEU C O   1 
ATOM   1533 C CB  . LEU C 1 11 ? 18.468  -21.640 22.286  1.00 50.14  ? 10  LEU C CB  1 
ATOM   1534 C CG  . LEU C 1 11 ? 17.243  -21.046 22.984  1.00 46.92  ? 10  LEU C CG  1 
ATOM   1535 C CD1 . LEU C 1 11 ? 16.727  -19.970 22.059  1.00 52.37  ? 10  LEU C CD1 1 
ATOM   1536 C CD2 . LEU C 1 11 ? 16.125  -22.062 23.266  1.00 49.20  ? 10  LEU C CD2 1 
ATOM   1537 N N   . VAL C 1 12 ? 20.600  -24.215 21.764  1.00 43.34  ? 11  VAL C N   1 
ATOM   1538 C CA  . VAL C 1 12 ? 21.799  -24.742 21.133  1.00 41.10  ? 11  VAL C CA  1 
ATOM   1539 C C   . VAL C 1 12 ? 21.383  -25.511 19.862  1.00 42.29  ? 11  VAL C C   1 
ATOM   1540 O O   . VAL C 1 12 ? 20.197  -25.710 19.598  1.00 39.91  ? 11  VAL C O   1 
ATOM   1541 C CB  . VAL C 1 12 ? 22.493  -25.683 22.154  1.00 40.39  ? 11  VAL C CB  1 
ATOM   1542 C CG1 . VAL C 1 12 ? 22.906  -25.000 23.457  1.00 45.50  ? 11  VAL C CG1 1 
ATOM   1543 C CG2 . VAL C 1 12 ? 21.610  -26.862 22.515  1.00 36.93  ? 11  VAL C CG2 1 
ATOM   1544 N N   . PHE C 1 13 ? 22.380  -25.941 19.082  1.00 38.74  ? 12  PHE C N   1 
ATOM   1545 C CA  . PHE C 1 13 ? 22.314  -27.131 18.243  1.00 36.28  ? 12  PHE C CA  1 
ATOM   1546 C C   . PHE C 1 13 ? 23.026  -28.282 18.948  1.00 35.38  ? 12  PHE C C   1 
ATOM   1547 O O   . PHE C 1 13 ? 24.132  -28.111 19.473  1.00 37.38  ? 12  PHE C O   1 
ATOM   1548 C CB  . PHE C 1 13 ? 23.042  -26.772 16.947  1.00 40.75  ? 12  PHE C CB  1 
ATOM   1549 C CG  . PHE C 1 13 ? 22.227  -25.819 16.093  1.00 37.69  ? 12  PHE C CG  1 
ATOM   1550 C CD1 . PHE C 1 13 ? 21.271  -26.303 15.208  1.00 35.89  ? 12  PHE C CD1 1 
ATOM   1551 C CD2 . PHE C 1 13 ? 22.444  -24.438 16.154  1.00 39.66  ? 12  PHE C CD2 1 
ATOM   1552 C CE1 . PHE C 1 13 ? 20.555  -25.415 14.401  1.00 32.82  ? 12  PHE C CE1 1 
ATOM   1553 C CE2 . PHE C 1 13 ? 21.681  -23.555 15.395  1.00 42.42  ? 12  PHE C CE2 1 
ATOM   1554 C CZ  . PHE C 1 13 ? 20.745  -24.053 14.509  1.00 38.32  ? 12  PHE C CZ  1 
ATOM   1555 N N   . ALA C 1 14 ? 22.346  -29.428 19.022  1.00 32.09  ? 13  ALA C N   1 
ATOM   1556 C CA  . ALA C 1 14 ? 22.825  -30.595 19.725  1.00 33.24  ? 13  ALA C CA  1 
ATOM   1557 C C   . ALA C 1 14 ? 23.094  -31.658 18.668  1.00 38.47  ? 13  ALA C C   1 
ATOM   1558 O O   . ALA C 1 14 ? 22.224  -31.923 17.855  1.00 32.06  ? 13  ALA C O   1 
ATOM   1559 C CB  . ALA C 1 14 ? 21.762  -31.098 20.687  1.00 35.61  ? 13  ALA C CB  1 
ATOM   1560 N N   . LYS C 1 15 ? 24.282  -32.256 18.715  1.00 37.48  ? 14  LYS C N   1 
ATOM   1561 C CA  . LYS C 1 15 ? 24.712  -33.242 17.737  1.00 40.67  ? 14  LYS C CA  1 
ATOM   1562 C C   . LYS C 1 15 ? 24.747  -34.576 18.449  1.00 40.17  ? 14  LYS C C   1 
ATOM   1563 O O   . LYS C 1 15 ? 25.409  -34.706 19.478  1.00 37.23  ? 14  LYS C O   1 
ATOM   1564 C CB  . LYS C 1 15 ? 26.150  -33.065 17.224  1.00 43.83  ? 14  LYS C CB  1 
ATOM   1565 C CG  . LYS C 1 15 ? 26.569  -34.114 16.187  1.00 36.77  ? 14  LYS C CG  1 
ATOM   1566 C CD  . LYS C 1 15 ? 25.753  -34.030 14.900  1.00 35.02  ? 14  LYS C CD  1 
ATOM   1567 C CE  . LYS C 1 15 ? 26.235  -34.949 13.758  1.00 32.47  ? 14  LYS C CE  1 
ATOM   1568 N NZ  . LYS C 1 15 ? 26.056  -36.359 14.144  1.00 28.97  ? 14  LYS C NZ  1 
ATOM   1569 N N   . MET C 1 16 ? 24.026  -35.526 17.864  1.00 34.29  ? 15  MET C N   1 
ATOM   1570 C CA  . MET C 1 16 ? 23.991  -36.906 18.307  1.00 34.62  ? 15  MET C CA  1 
ATOM   1571 C C   . MET C 1 16 ? 24.417  -37.741 17.105  1.00 41.77  ? 15  MET C C   1 
ATOM   1572 O O   . MET C 1 16 ? 24.193  -37.327 15.965  1.00 35.40  ? 15  MET C O   1 
ATOM   1573 C CB  . MET C 1 16 ? 22.546  -37.319 18.590  1.00 34.22  ? 15  MET C CB  1 
ATOM   1574 C CG  . MET C 1 16 ? 22.024  -36.739 19.869  1.00 46.14  ? 15  MET C CG  1 
ATOM   1575 S SD  . MET C 1 16 ? 20.464  -37.454 20.430  1.00 50.27  ? 15  MET C SD  1 
ATOM   1576 C CE  . MET C 1 16 ? 20.953  -39.128 20.878  1.00 47.90  ? 15  MET C CE  1 
ATOM   1577 N N   . LYS C 1 17 ? 24.955  -38.937 17.365  1.00 45.37  ? 16  LYS C N   1 
ATOM   1578 C CA  . LYS C 1 17 ? 25.444  -39.764 16.270  1.00 46.03  ? 16  LYS C CA  1 
ATOM   1579 C C   . LYS C 1 17 ? 24.220  -40.248 15.503  1.00 39.97  ? 16  LYS C C   1 
ATOM   1580 O O   . LYS C 1 17 ? 23.264  -40.703 16.114  1.00 37.23  ? 16  LYS C O   1 
ATOM   1581 C CB  . LYS C 1 17 ? 26.214  -40.959 16.849  1.00 44.29  ? 16  LYS C CB  1 
ATOM   1582 C CG  . LYS C 1 17 ? 26.917  -41.900 15.880  1.00 46.93  ? 16  LYS C CG  1 
ATOM   1583 C CD  . LYS C 1 17 ? 28.088  -41.238 15.170  1.00 56.45  ? 16  LYS C CD  1 
ATOM   1584 C CE  . LYS C 1 17 ? 28.799  -42.249 14.328  1.00 65.14  ? 16  LYS C CE  1 
ATOM   1585 N NZ  . LYS C 1 17 ? 30.025  -41.656 13.796  1.00 61.95  ? 16  LYS C NZ  1 
ATOM   1586 N N   . GLY C 1 18 ? 24.268  -40.146 14.172  1.00 39.41  ? 17  GLY C N   1 
ATOM   1587 C CA  . GLY C 1 18 ? 23.167  -40.595 13.338  1.00 38.50  ? 17  GLY C CA  1 
ATOM   1588 C C   . GLY C 1 18 ? 22.188  -39.467 12.976  1.00 41.82  ? 17  GLY C C   1 
ATOM   1589 O O   . GLY C 1 18 ? 21.127  -39.736 12.422  1.00 39.30  ? 17  GLY C O   1 
ATOM   1590 N N   . TYR C 1 19 ? 22.516  -38.219 13.342  1.00 39.56  ? 18  TYR C N   1 
ATOM   1591 C CA  . TYR C 1 19 ? 21.586  -37.099 13.198  1.00 37.05  ? 18  TYR C CA  1 
ATOM   1592 C C   . TYR C 1 19 ? 22.369  -35.838 12.865  1.00 32.76  ? 18  TYR C C   1 
ATOM   1593 O O   . TYR C 1 19 ? 23.500  -35.650 13.325  1.00 31.83  ? 18  TYR C O   1 
ATOM   1594 C CB  . TYR C 1 19 ? 20.811  -36.835 14.496  1.00 35.72  ? 18  TYR C CB  1 
ATOM   1595 C CG  . TYR C 1 19 ? 19.960  -38.033 14.876  1.00 32.03  ? 18  TYR C CG  1 
ATOM   1596 C CD1 . TYR C 1 19 ? 20.471  -39.036 15.684  1.00 30.04  ? 18  TYR C CD1 1 
ATOM   1597 C CD2 . TYR C 1 19 ? 18.654  -38.147 14.434  1.00 36.06  ? 18  TYR C CD2 1 
ATOM   1598 C CE1 . TYR C 1 19 ? 19.711  -40.134 16.031  1.00 37.37  ? 18  TYR C CE1 1 
ATOM   1599 C CE2 . TYR C 1 19 ? 17.881  -39.244 14.772  1.00 40.70  ? 18  TYR C CE2 1 
ATOM   1600 C CZ  . TYR C 1 19 ? 18.420  -40.245 15.559  1.00 37.43  ? 18  TYR C CZ  1 
ATOM   1601 O OH  . TYR C 1 19 ? 17.665  -41.322 15.919  1.00 48.26  ? 18  TYR C OH  1 
ATOM   1602 N N   . PRO C 1 20 ? 21.810  -34.960 12.016  1.00 33.17  ? 19  PRO C N   1 
ATOM   1603 C CA  . PRO C 1 20 ? 22.413  -33.636 11.797  1.00 31.05  ? 19  PRO C CA  1 
ATOM   1604 C C   . PRO C 1 20 ? 22.357  -32.853 13.127  1.00 34.40  ? 19  PRO C C   1 
ATOM   1605 O O   . PRO C 1 20 ? 21.660  -33.256 14.083  1.00 30.66  ? 19  PRO C O   1 
ATOM   1606 C CB  . PRO C 1 20 ? 21.493  -33.038 10.684  1.00 31.96  ? 19  PRO C CB  1 
ATOM   1607 C CG  . PRO C 1 20 ? 20.160  -33.698 10.973  1.00 32.68  ? 19  PRO C CG  1 
ATOM   1608 C CD  . PRO C 1 20 ? 20.507  -35.154 11.355  1.00 34.20  ? 19  PRO C CD  1 
ATOM   1609 N N   . HIS C 1 21 ? 23.188  -31.809 13.223  1.00 34.37  ? 20  HIS C N   1 
ATOM   1610 C CA  . HIS C 1 21 ? 23.193  -30.910 14.379  1.00 41.92  ? 20  HIS C CA  1 
ATOM   1611 C C   . HIS C 1 21 ? 21.806  -30.283 14.534  1.00 40.61  ? 20  HIS C C   1 
ATOM   1612 O O   . HIS C 1 21 ? 21.334  -29.624 13.597  1.00 37.44  ? 20  HIS C O   1 
ATOM   1613 C CB  . HIS C 1 21 ? 24.124  -29.720 14.134  1.00 33.94  ? 20  HIS C CB  1 
ATOM   1614 C CG  . HIS C 1 21 ? 25.566  -30.073 14.114  1.00 38.92  ? 20  HIS C CG  1 
ATOM   1615 N ND1 . HIS C 1 21 ? 26.168  -30.678 13.033  1.00 42.73  ? 20  HIS C ND1 1 
ATOM   1616 C CD2 . HIS C 1 21 ? 26.512  -29.947 15.058  1.00 43.34  ? 20  HIS C CD2 1 
ATOM   1617 C CE1 . HIS C 1 21 ? 27.450  -30.887 13.317  1.00 48.59  ? 20  HIS C CE1 1 
ATOM   1618 N NE2 . HIS C 1 21 ? 27.678  -30.442 14.546  1.00 51.58  ? 20  HIS C NE2 1 
ATOM   1619 N N   . TRP C 1 22 ? 21.175  -30.485 15.710  1.00 34.51  ? 21  TRP C N   1 
ATOM   1620 C CA  . TRP C 1 22 ? 19.724  -30.376 15.830  1.00 33.75  ? 21  TRP C CA  1 
ATOM   1621 C C   . TRP C 1 22 ? 19.417  -29.177 16.720  1.00 34.54  ? 21  TRP C C   1 
ATOM   1622 O O   . TRP C 1 22 ? 20.005  -29.029 17.785  1.00 35.46  ? 21  TRP C O   1 
ATOM   1623 C CB  . TRP C 1 22 ? 19.084  -31.666 16.410  1.00 34.56  ? 21  TRP C CB  1 
ATOM   1624 C CG  . TRP C 1 22 ? 17.621  -31.891 16.039  1.00 40.33  ? 21  TRP C CG  1 
ATOM   1625 C CD1 . TRP C 1 22 ? 16.495  -31.326 16.588  1.00 32.49  ? 21  TRP C CD1 1 
ATOM   1626 C CD2 . TRP C 1 22 ? 17.127  -32.784 15.001  1.00 33.36  ? 21  TRP C CD2 1 
ATOM   1627 N NE1 . TRP C 1 22 ? 15.350  -31.784 15.965  1.00 33.71  ? 21  TRP C NE1 1 
ATOM   1628 C CE2 . TRP C 1 22 ? 15.708  -32.679 14.989  1.00 34.93  ? 21  TRP C CE2 1 
ATOM   1629 C CE3 . TRP C 1 22 ? 17.740  -33.660 14.094  1.00 32.66  ? 21  TRP C CE3 1 
ATOM   1630 C CZ2 . TRP C 1 22 ? 14.928  -33.420 14.099  1.00 32.31  ? 21  TRP C CZ2 1 
ATOM   1631 C CZ3 . TRP C 1 22 ? 16.967  -34.378 13.193  1.00 31.97  ? 21  TRP C CZ3 1 
ATOM   1632 C CH2 . TRP C 1 22 ? 15.579  -34.274 13.221  1.00 32.81  ? 21  TRP C CH2 1 
ATOM   1633 N N   . PRO C 1 23 ? 18.429  -28.324 16.364  1.00 33.46  ? 22  PRO C N   1 
ATOM   1634 C CA  . PRO C 1 23 ? 18.063  -27.212 17.236  1.00 31.89  ? 22  PRO C CA  1 
ATOM   1635 C C   . PRO C 1 23 ? 17.441  -27.783 18.499  1.00 33.22  ? 22  PRO C C   1 
ATOM   1636 O O   . PRO C 1 23 ? 16.560  -28.636 18.413  1.00 30.20  ? 22  PRO C O   1 
ATOM   1637 C CB  . PRO C 1 23 ? 17.002  -26.486 16.398  1.00 34.42  ? 22  PRO C CB  1 
ATOM   1638 C CG  . PRO C 1 23 ? 16.372  -27.595 15.551  1.00 34.45  ? 22  PRO C CG  1 
ATOM   1639 C CD  . PRO C 1 23 ? 17.601  -28.409 15.146  1.00 33.21  ? 22  PRO C CD  1 
ATOM   1640 N N   . ALA C 1 24 ? 17.814  -27.211 19.651  1.00 34.40  ? 23  ALA C N   1 
ATOM   1641 C CA  . ALA C 1 24 ? 17.458  -27.805 20.927  1.00 34.81  ? 23  ALA C CA  1 
ATOM   1642 C C   . ALA C 1 24 ? 17.639  -26.757 22.039  1.00 39.98  ? 23  ALA C C   1 
ATOM   1643 O O   . ALA C 1 24 ? 18.090  -25.628 21.796  1.00 39.01  ? 23  ALA C O   1 
ATOM   1644 C CB  . ALA C 1 24 ? 18.325  -29.054 21.147  1.00 31.91  ? 23  ALA C CB  1 
ATOM   1645 N N   . ARG C 1 25 ? 17.343  -27.146 23.282  1.00 42.29  ? 24  ARG C N   1 
ATOM   1646 C CA  . ARG C 1 25 ? 17.743  -26.332 24.419  1.00 36.69  ? 24  ARG C CA  1 
ATOM   1647 C C   . ARG C 1 25 ? 18.092  -27.226 25.614  1.00 37.03  ? 24  ARG C C   1 
ATOM   1648 O O   . ARG C 1 25 ? 17.641  -28.370 25.668  1.00 39.03  ? 24  ARG C O   1 
ATOM   1649 C CB  . ARG C 1 25 ? 16.527  -25.489 24.811  1.00 37.86  ? 24  ARG C CB  1 
ATOM   1650 C CG  . ARG C 1 25 ? 15.252  -26.248 25.138  1.00 40.13  ? 24  ARG C CG  1 
ATOM   1651 C CD  . ARG C 1 25 ? 14.243  -25.295 25.820  1.00 46.23  ? 24  ARG C CD  1 
ATOM   1652 N NE  . ARG C 1 25 ? 13.071  -26.058 26.271  1.00 47.85  ? 24  ARG C NE  1 
ATOM   1653 C CZ  . ARG C 1 25 ? 11.779  -25.868 25.976  1.00 61.49  ? 24  ARG C CZ  1 
ATOM   1654 N NH1 . ARG C 1 25 ? 11.371  -24.773 25.350  1.00 57.39  ? 24  ARG C NH1 1 
ATOM   1655 N NH2 . ARG C 1 25 ? 10.883  -26.767 26.351  1.00 59.07  ? 24  ARG C NH2 1 
ATOM   1656 N N   . ILE C 1 26 ? 18.842  -26.660 26.573  1.00 45.65  ? 25  ILE C N   1 
ATOM   1657 C CA  . ILE C 1 26 ? 19.194  -27.262 27.859  1.00 53.61  ? 25  ILE C CA  1 
ATOM   1658 C C   . ILE C 1 26 ? 17.929  -27.383 28.705  1.00 52.61  ? 25  ILE C C   1 
ATOM   1659 O O   . ILE C 1 26 ? 17.310  -26.379 29.050  1.00 56.84  ? 25  ILE C O   1 
ATOM   1660 C CB  . ILE C 1 26 ? 20.245  -26.395 28.591  1.00 54.47  ? 25  ILE C CB  1 
ATOM   1661 C CG1 . ILE C 1 26 ? 21.307  -25.881 27.647  1.00 52.47  ? 25  ILE C CG1 1 
ATOM   1662 C CG2 . ILE C 1 26 ? 20.871  -27.108 29.800  1.00 48.78  ? 25  ILE C CG2 1 
ATOM   1663 C CD1 . ILE C 1 26 ? 22.363  -26.905 27.279  1.00 49.54  ? 25  ILE C CD1 1 
ATOM   1664 N N   . ASP C 1 27 ? 17.528  -28.614 29.023  1.00 55.67  ? 26  ASP C N   1 
ATOM   1665 C CA  . ASP C 1 27 ? 16.453  -28.809 29.991  1.00 59.59  ? 26  ASP C CA  1 
ATOM   1666 C C   . ASP C 1 27 ? 16.937  -28.558 31.420  1.00 64.58  ? 26  ASP C C   1 
ATOM   1667 O O   . ASP C 1 27 ? 18.132  -28.358 31.661  1.00 58.94  ? 26  ASP C O   1 
ATOM   1668 C CB  . ASP C 1 27 ? 15.862  -30.208 29.928  1.00 68.49  ? 26  ASP C CB  1 
ATOM   1669 C CG  . ASP C 1 27 ? 14.422  -30.276 29.447  1.00 75.08  ? 26  ASP C CG  1 
ATOM   1670 O OD1 . ASP C 1 27 ? 13.923  -29.227 28.988  1.00 77.19  ? 26  ASP C OD1 1 
ATOM   1671 O OD2 . ASP C 1 27 ? 13.809  -31.364 29.572  1.00 64.46  ? 26  ASP C OD2 1 
ATOM   1672 N N   . ASP C 1 28 ? 15.969  -28.559 32.352  1.00 79.37  ? 27  ASP C N   1 
ATOM   1673 C CA  . ASP C 1 28 ? 16.190  -28.551 33.789  1.00 78.23  ? 27  ASP C CA  1 
ATOM   1674 C C   . ASP C 1 28 ? 16.248  -29.999 34.252  1.00 84.24  ? 27  ASP C C   1 
ATOM   1675 O O   . ASP C 1 28 ? 15.751  -30.872 33.545  1.00 94.70  ? 27  ASP C O   1 
ATOM   1676 C CB  . ASP C 1 28 ? 15.026  -27.899 34.517  1.00 83.44  ? 27  ASP C CB  1 
ATOM   1677 N N   . ILE C 1 29 ? 16.854  -30.240 35.426  1.00 88.14  ? 28  ILE C N   1 
ATOM   1678 C CA  . ILE C 1 29 ? 16.800  -31.537 36.084  1.00 82.75  ? 28  ILE C CA  1 
ATOM   1679 C C   . ILE C 1 29 ? 15.701  -31.484 37.161  1.00 82.94  ? 28  ILE C C   1 
ATOM   1680 O O   . ILE C 1 29 ? 15.391  -32.553 37.748  1.00 94.58  ? 28  ILE C O   1 
ATOM   1681 C CB  . ILE C 1 29 ? 18.170  -31.935 36.665  1.00 82.33  ? 28  ILE C CB  1 
ATOM   1682 N N   . LYS C 1 35 ? 19.478  -39.169 38.025  1.00 86.96  ? 34  LYS C N   1 
ATOM   1683 C CA  . LYS C 1 35 ? 20.469  -38.092 37.744  1.00 81.80  ? 34  LYS C CA  1 
ATOM   1684 C C   . LYS C 1 35 ? 21.096  -38.346 36.371  1.00 80.60  ? 34  LYS C C   1 
ATOM   1685 O O   . LYS C 1 35 ? 21.086  -39.483 35.887  1.00 64.04  ? 34  LYS C O   1 
ATOM   1686 C CB  . LYS C 1 35 ? 21.502  -37.944 38.872  1.00 80.06  ? 34  LYS C CB  1 
ATOM   1687 N N   . PRO C 1 36 ? 21.628  -37.295 35.691  1.00 75.67  ? 35  PRO C N   1 
ATOM   1688 C CA  . PRO C 1 36 ? 22.347  -37.477 34.424  1.00 73.03  ? 35  PRO C CA  1 
ATOM   1689 C C   . PRO C 1 36 ? 23.579  -38.369 34.591  1.00 75.14  ? 35  PRO C C   1 
ATOM   1690 O O   . PRO C 1 36 ? 24.119  -38.507 35.693  1.00 59.46  ? 35  PRO C O   1 
ATOM   1691 C CB  . PRO C 1 36 ? 22.745  -36.051 33.951  1.00 73.93  ? 35  PRO C CB  1 
ATOM   1692 C CG  . PRO C 1 36 ? 22.051  -35.091 34.903  1.00 74.24  ? 35  PRO C CG  1 
ATOM   1693 C CD  . PRO C 1 36 ? 21.553  -35.882 36.113  1.00 75.07  ? 35  PRO C CD  1 
ATOM   1694 N N   . PRO C 1 37 ? 24.087  -39.013 33.517  1.00 61.32  ? 36  PRO C N   1 
ATOM   1695 C CA  . PRO C 1 37 ? 25.451  -39.535 33.559  1.00 69.17  ? 36  PRO C CA  1 
ATOM   1696 C C   . PRO C 1 37 ? 26.399  -38.362 33.826  1.00 63.22  ? 36  PRO C C   1 
ATOM   1697 O O   . PRO C 1 37 ? 26.054  -37.212 33.539  1.00 54.57  ? 36  PRO C O   1 
ATOM   1698 C CB  . PRO C 1 37 ? 25.630  -40.197 32.176  1.00 57.83  ? 36  PRO C CB  1 
ATOM   1699 C CG  . PRO C 1 37 ? 24.217  -40.509 31.768  1.00 53.79  ? 36  PRO C CG  1 
ATOM   1700 C CD  . PRO C 1 37 ? 23.390  -39.323 32.262  1.00 64.70  ? 36  PRO C CD  1 
ATOM   1701 N N   . PRO C 1 38 ? 27.578  -38.605 34.454  1.00 56.30  ? 37  PRO C N   1 
ATOM   1702 C CA  . PRO C 1 38 ? 28.510  -37.531 34.801  1.00 56.77  ? 37  PRO C CA  1 
ATOM   1703 C C   . PRO C 1 38 ? 28.793  -36.683 33.575  1.00 52.78  ? 37  PRO C C   1 
ATOM   1704 O O   . PRO C 1 38 ? 28.934  -37.225 32.482  1.00 47.68  ? 37  PRO C O   1 
ATOM   1705 C CB  . PRO C 1 38 ? 29.778  -38.273 35.242  1.00 60.96  ? 37  PRO C CB  1 
ATOM   1706 C CG  . PRO C 1 38 ? 29.267  -39.609 35.741  1.00 57.30  ? 37  PRO C CG  1 
ATOM   1707 C CD  . PRO C 1 38 ? 28.064  -39.930 34.875  1.00 58.80  ? 37  PRO C CD  1 
ATOM   1708 N N   . ASN C 1 39 ? 28.837  -35.362 33.790  1.00 52.36  ? 38  ASN C N   1 
ATOM   1709 C CA  . ASN C 1 39 ? 29.225  -34.375 32.800  1.00 52.65  ? 38  ASN C CA  1 
ATOM   1710 C C   . ASN C 1 39 ? 28.277  -34.366 31.596  1.00 53.67  ? 38  ASN C C   1 
ATOM   1711 O O   . ASN C 1 39 ? 28.686  -33.923 30.520  1.00 60.25  ? 38  ASN C O   1 
ATOM   1712 C CB  . ASN C 1 39 ? 30.673  -34.568 32.369  1.00 58.43  ? 38  ASN C CB  1 
ATOM   1713 C CG  . ASN C 1 39 ? 31.262  -33.319 31.752  1.00 64.93  ? 38  ASN C CG  1 
ATOM   1714 O OD1 . ASN C 1 39 ? 30.649  -32.242 31.775  1.00 77.66  ? 38  ASN C OD1 1 
ATOM   1715 N ND2 . ASN C 1 39 ? 32.456  -33.441 31.196  1.00 62.89  ? 38  ASN C ND2 1 
ATOM   1716 N N   . LYS C 1 40 ? 27.019  -34.806 31.779  1.00 43.94  ? 39  LYS C N   1 
ATOM   1717 C CA  . LYS C 1 40 ? 26.038  -34.758 30.698  1.00 48.65  ? 39  LYS C CA  1 
ATOM   1718 C C   . LYS C 1 40 ? 24.891  -33.809 31.037  1.00 46.32  ? 39  LYS C C   1 
ATOM   1719 O O   . LYS C 1 40 ? 24.367  -33.827 32.142  1.00 48.05  ? 39  LYS C O   1 
ATOM   1720 C CB  . LYS C 1 40 ? 25.440  -36.125 30.337  1.00 44.32  ? 39  LYS C CB  1 
ATOM   1721 C CG  . LYS C 1 40 ? 26.442  -37.221 30.003  1.00 44.93  ? 39  LYS C CG  1 
ATOM   1722 C CD  . LYS C 1 40 ? 27.060  -37.086 28.625  1.00 47.55  ? 39  LYS C CD  1 
ATOM   1723 C CE  . LYS C 1 40 ? 28.302  -37.934 28.528  1.00 50.86  ? 39  LYS C CE  1 
ATOM   1724 N NZ  . LYS C 1 40 ? 29.074  -37.691 27.288  1.00 44.67  ? 39  LYS C NZ  1 
ATOM   1725 N N   . TYR C 1 41 ? 24.485  -33.011 30.044  1.00 47.98  ? 40  TYR C N   1 
ATOM   1726 C CA  . TYR C 1 41 ? 23.356  -32.099 30.144  1.00 46.59  ? 40  TYR C CA  1 
ATOM   1727 C C   . TYR C 1 41 ? 22.085  -32.771 29.622  1.00 47.01  ? 40  TYR C C   1 
ATOM   1728 O O   . TYR C 1 41 ? 22.113  -33.566 28.669  1.00 46.03  ? 40  TYR C O   1 
ATOM   1729 C CB  . TYR C 1 41 ? 23.568  -30.874 29.250  1.00 37.55  ? 40  TYR C CB  1 
ATOM   1730 C CG  . TYR C 1 41 ? 24.665  -29.934 29.705  1.00 47.26  ? 40  TYR C CG  1 
ATOM   1731 C CD1 . TYR C 1 41 ? 25.984  -30.135 29.301  1.00 44.72  ? 40  TYR C CD1 1 
ATOM   1732 C CD2 . TYR C 1 41 ? 24.382  -28.837 30.530  1.00 45.12  ? 40  TYR C CD2 1 
ATOM   1733 C CE1 . TYR C 1 41 ? 26.998  -29.290 29.724  1.00 54.71  ? 40  TYR C CE1 1 
ATOM   1734 C CE2 . TYR C 1 41 ? 25.388  -27.959 30.911  1.00 52.15  ? 40  TYR C CE2 1 
ATOM   1735 C CZ  . TYR C 1 41 ? 26.694  -28.194 30.516  1.00 46.80  ? 40  TYR C CZ  1 
ATOM   1736 O OH  . TYR C 1 41 ? 27.717  -27.381 30.892  1.00 69.69  ? 40  TYR C OH  1 
ATOM   1737 N N   . PRO C 1 42 ? 20.913  -32.458 30.217  1.00 50.63  ? 41  PRO C N   1 
ATOM   1738 C CA  . PRO C 1 42 ? 19.650  -32.979 29.698  1.00 39.66  ? 41  PRO C CA  1 
ATOM   1739 C C   . PRO C 1 42 ? 19.263  -32.016 28.565  1.00 40.59  ? 41  PRO C C   1 
ATOM   1740 O O   . PRO C 1 42 ? 19.279  -30.809 28.766  1.00 37.19  ? 41  PRO C O   1 
ATOM   1741 C CB  . PRO C 1 42 ? 18.757  -32.918 30.952  1.00 40.98  ? 41  PRO C CB  1 
ATOM   1742 C CG  . PRO C 1 42 ? 19.233  -31.672 31.667  1.00 47.51  ? 41  PRO C CG  1 
ATOM   1743 C CD  . PRO C 1 42 ? 20.742  -31.566 31.385  1.00 49.62  ? 41  PRO C CD  1 
ATOM   1744 N N   . ILE C 1 43 ? 18.986  -32.564 27.362  1.00 39.24  ? 42  ILE C N   1 
ATOM   1745 C CA  . ILE C 1 43 ? 18.646  -31.799 26.162  1.00 39.50  ? 42  ILE C CA  1 
ATOM   1746 C C   . ILE C 1 43 ? 17.224  -32.155 25.710  1.00 42.38  ? 42  ILE C C   1 
ATOM   1747 O O   . ILE C 1 43 ? 16.818  -33.328 25.722  1.00 45.93  ? 42  ILE C O   1 
ATOM   1748 C CB  . ILE C 1 43 ? 19.682  -32.057 25.037  1.00 39.99  ? 42  ILE C CB  1 
ATOM   1749 C CG1 . ILE C 1 43 ? 21.150  -31.838 25.517  1.00 39.16  ? 42  ILE C CG1 1 
ATOM   1750 C CG2 . ILE C 1 43 ? 19.368  -31.308 23.723  1.00 36.33  ? 42  ILE C CG2 1 
ATOM   1751 C CD1 . ILE C 1 43 ? 21.510  -30.434 25.964  1.00 40.71  ? 42  ILE C CD1 1 
ATOM   1752 N N   . PHE C 1 44 ? 16.474  -31.115 25.307  1.00 41.40  ? 43  PHE C N   1 
ATOM   1753 C CA  . PHE C 1 44 ? 15.169  -31.209 24.660  1.00 33.77  ? 43  PHE C CA  1 
ATOM   1754 C C   . PHE C 1 44 ? 15.392  -30.832 23.194  1.00 35.03  ? 43  PHE C C   1 
ATOM   1755 O O   . PHE C 1 44 ? 15.998  -29.806 22.894  1.00 38.94  ? 43  PHE C O   1 
ATOM   1756 C CB  . PHE C 1 44 ? 14.207  -30.214 25.336  1.00 36.19  ? 43  PHE C CB  1 
ATOM   1757 C CG  . PHE C 1 44 ? 12.826  -30.091 24.691  1.00 44.53  ? 43  PHE C CG  1 
ATOM   1758 C CD1 . PHE C 1 44 ? 11.821  -31.035 24.949  1.00 46.04  ? 43  PHE C CD1 1 
ATOM   1759 C CD2 . PHE C 1 44 ? 12.527  -29.026 23.828  1.00 47.14  ? 43  PHE C CD2 1 
ATOM   1760 C CE1 . PHE C 1 44 ? 10.562  -30.946 24.356  1.00 50.13  ? 43  PHE C CE1 1 
ATOM   1761 C CE2 . PHE C 1 44 ? 11.272  -28.936 23.217  1.00 47.86  ? 43  PHE C CE2 1 
ATOM   1762 C CZ  . PHE C 1 44 ? 10.290  -29.890 23.492  1.00 49.83  ? 43  PHE C CZ  1 
ATOM   1763 N N   . PHE C 1 45 ? 14.871  -31.647 22.284  1.00 36.59  ? 44  PHE C N   1 
ATOM   1764 C CA  . PHE C 1 45 ? 15.030  -31.401 20.872  1.00 37.24  ? 44  PHE C CA  1 
ATOM   1765 C C   . PHE C 1 45 ? 13.761  -30.751 20.323  1.00 37.25  ? 44  PHE C C   1 
ATOM   1766 O O   . PHE C 1 45 ? 12.663  -31.307 20.427  1.00 37.79  ? 44  PHE C O   1 
ATOM   1767 C CB  . PHE C 1 45 ? 15.402  -32.687 20.144  1.00 34.99  ? 44  PHE C CB  1 
ATOM   1768 C CG  . PHE C 1 45 ? 16.795  -33.209 20.464  1.00 34.05  ? 44  PHE C CG  1 
ATOM   1769 C CD1 . PHE C 1 45 ? 17.877  -32.878 19.656  1.00 32.58  ? 44  PHE C CD1 1 
ATOM   1770 C CD2 . PHE C 1 45 ? 17.016  -34.009 21.596  1.00 34.00  ? 44  PHE C CD2 1 
ATOM   1771 C CE1 . PHE C 1 45 ? 19.150  -33.388 19.953  1.00 39.26  ? 44  PHE C CE1 1 
ATOM   1772 C CE2 . PHE C 1 45 ? 18.290  -34.510 21.896  1.00 41.54  ? 44  PHE C CE2 1 
ATOM   1773 C CZ  . PHE C 1 45 ? 19.351  -34.196 21.078  1.00 38.28  ? 44  PHE C CZ  1 
ATOM   1774 N N   . PHE C 1 46 ? 13.935  -29.582 19.700  1.00 38.11  ? 45  PHE C N   1 
ATOM   1775 C CA  . PHE C 1 46 ? 12.807  -28.936 19.033  1.00 38.52  ? 45  PHE C CA  1 
ATOM   1776 C C   . PHE C 1 46 ? 12.335  -29.811 17.872  1.00 39.66  ? 45  PHE C C   1 
ATOM   1777 O O   . PHE C 1 46 ? 13.117  -30.593 17.295  1.00 34.30  ? 45  PHE C O   1 
ATOM   1778 C CB  . PHE C 1 46 ? 13.074  -27.475 18.633  1.00 39.03  ? 45  PHE C CB  1 
ATOM   1779 C CG  . PHE C 1 46 ? 13.364  -26.505 19.772  1.00 37.98  ? 45  PHE C CG  1 
ATOM   1780 C CD1 . PHE C 1 46 ? 12.335  -26.084 20.613  1.00 40.07  ? 45  PHE C CD1 1 
ATOM   1781 C CD2 . PHE C 1 46 ? 14.657  -26.016 19.994  1.00 35.37  ? 45  PHE C CD2 1 
ATOM   1782 C CE1 . PHE C 1 46 ? 12.589  -25.201 21.658  1.00 41.07  ? 45  PHE C CE1 1 
ATOM   1783 C CE2 . PHE C 1 46 ? 14.910  -25.131 21.039  1.00 37.00  ? 45  PHE C CE2 1 
ATOM   1784 C CZ  . PHE C 1 46 ? 13.877  -24.717 21.861  1.00 42.05  ? 45  PHE C CZ  1 
ATOM   1785 N N   . GLY C 1 47 ? 11.040  -29.686 17.564  1.00 38.85  ? 46  GLY C N   1 
ATOM   1786 C CA  . GLY C 1 47 ? 10.501  -30.365 16.401  1.00 43.27  ? 46  GLY C CA  1 
ATOM   1787 C C   . GLY C 1 47 ? 10.028  -31.759 16.784  1.00 51.11  ? 46  GLY C C   1 
ATOM   1788 O O   . GLY C 1 47 ? 8.828   -32.017 16.750  1.00 50.42  ? 46  GLY C O   1 
ATOM   1789 N N   . THR C 1 48 ? 10.975  -32.635 17.157  1.00 47.20  ? 47  THR C N   1 
ATOM   1790 C CA  . THR C 1 48 ? 10.629  -33.967 17.644  1.00 44.91  ? 47  THR C CA  1 
ATOM   1791 C C   . THR C 1 48 ? 10.104  -33.898 19.078  1.00 43.60  ? 47  THR C C   1 
ATOM   1792 O O   . THR C 1 48 ? 9.305   -34.746 19.458  1.00 52.64  ? 47  THR C O   1 
ATOM   1793 C CB  . THR C 1 48 ? 11.825  -34.913 17.582  1.00 43.67  ? 47  THR C CB  1 
ATOM   1794 O OG1 . THR C 1 48 ? 12.718  -34.388 18.577  1.00 38.06  ? 47  THR C OG1 1 
ATOM   1795 C CG2 . THR C 1 48 ? 12.374  -35.051 16.171  1.00 37.23  ? 47  THR C CG2 1 
ATOM   1796 N N   . HIS C 1 49 ? 10.584  -32.923 19.871  1.00 37.35  ? 48  HIS C N   1 
ATOM   1797 C CA  . HIS C 1 49 ? 10.218  -32.776 21.284  1.00 49.72  ? 48  HIS C CA  1 
ATOM   1798 C C   . HIS C 1 49 ? 10.703  -33.953 22.129  1.00 45.34  ? 48  HIS C C   1 
ATOM   1799 O O   . HIS C 1 49 ? 10.093  -34.252 23.142  1.00 47.70  ? 48  HIS C O   1 
ATOM   1800 C CB  . HIS C 1 49 ? 8.719   -32.497 21.506  1.00 49.33  ? 48  HIS C CB  1 
ATOM   1801 C CG  . HIS C 1 49 ? 8.182   -31.428 20.607  1.00 51.19  ? 48  HIS C CG  1 
ATOM   1802 N ND1 . HIS C 1 49 ? 7.158   -31.666 19.717  1.00 53.89  ? 48  HIS C ND1 1 
ATOM   1803 C CD2 . HIS C 1 49 ? 8.592   -30.169 20.382  1.00 41.70  ? 48  HIS C CD2 1 
ATOM   1804 C CE1 . HIS C 1 49 ? 6.936   -30.563 19.007  1.00 56.59  ? 48  HIS C CE1 1 
ATOM   1805 N NE2 . HIS C 1 49 ? 7.789   -29.640 19.402  1.00 52.87  ? 48  HIS C NE2 1 
ATOM   1806 N N   . GLU C 1 50 ? 11.809  -34.594 21.729  1.00 41.97  ? 49  GLU C N   1 
ATOM   1807 C CA  . GLU C 1 50 ? 12.348  -35.711 22.500  1.00 47.39  ? 49  GLU C CA  1 
ATOM   1808 C C   . GLU C 1 50 ? 13.500  -35.257 23.378  1.00 43.16  ? 49  GLU C C   1 
ATOM   1809 O O   . GLU C 1 50 ? 13.895  -34.101 23.312  1.00 46.79  ? 49  GLU C O   1 
ATOM   1810 C CB  . GLU C 1 50 ? 12.670  -36.856 21.560  1.00 44.73  ? 49  GLU C CB  1 
ATOM   1811 C CG  . GLU C 1 50 ? 11.339  -37.443 21.113  1.00 51.31  ? 49  GLU C CG  1 
ATOM   1812 C CD  . GLU C 1 50 ? 11.501  -38.472 20.037  1.00 54.49  ? 49  GLU C CD  1 
ATOM   1813 O OE1 . GLU C 1 50 ? 12.648  -38.866 19.702  1.00 59.01  ? 49  GLU C OE1 1 
ATOM   1814 O OE2 . GLU C 1 50 ? 10.422  -38.837 19.538  1.00 60.80  ? 49  GLU C OE2 1 
ATOM   1815 N N   . THR C 1 51 ? 13.982  -36.146 24.255  1.00 46.08  ? 50  THR C N   1 
ATOM   1816 C CA  . THR C 1 51 ? 15.015  -35.758 25.210  1.00 46.12  ? 50  THR C CA  1 
ATOM   1817 C C   . THR C 1 51 ? 16.184  -36.741 25.136  1.00 42.45  ? 50  THR C C   1 
ATOM   1818 O O   . THR C 1 51 ? 16.037  -37.850 24.624  1.00 37.00  ? 50  THR C O   1 
ATOM   1819 C CB  . THR C 1 51 ? 14.483  -35.603 26.640  1.00 48.09  ? 50  THR C CB  1 
ATOM   1820 O OG1 . THR C 1 51 ? 13.863  -36.861 26.879  1.00 53.59  ? 50  THR C OG1 1 
ATOM   1821 C CG2 . THR C 1 51 ? 13.514  -34.450 26.856  1.00 41.93  ? 50  THR C CG2 1 
ATOM   1822 N N   . ALA C 1 52 ? 17.346  -36.317 25.647  1.00 37.28  ? 51  ALA C N   1 
ATOM   1823 C CA  . ALA C 1 52 ? 18.559  -37.121 25.630  1.00 42.56  ? 51  ALA C CA  1 
ATOM   1824 C C   . ALA C 1 52 ? 19.589  -36.454 26.519  1.00 47.76  ? 51  ALA C C   1 
ATOM   1825 O O   . ALA C 1 52 ? 19.422  -35.294 26.871  1.00 47.55  ? 51  ALA C O   1 
ATOM   1826 C CB  . ALA C 1 52 ? 19.106  -37.320 24.227  1.00 44.51  ? 51  ALA C CB  1 
ATOM   1827 N N   . PHE C 1 53 ? 20.633  -37.214 26.874  1.00 47.27  ? 52  PHE C N   1 
ATOM   1828 C CA  . PHE C 1 53 ? 21.745  -36.702 27.646  1.00 47.16  ? 52  PHE C CA  1 
ATOM   1829 C C   . PHE C 1 53 ? 22.921  -36.545 26.697  1.00 46.18  ? 52  PHE C C   1 
ATOM   1830 O O   . PHE C 1 53 ? 23.259  -37.473 25.972  1.00 49.44  ? 52  PHE C O   1 
ATOM   1831 C CB  . PHE C 1 53 ? 22.049  -37.740 28.728  1.00 44.85  ? 52  PHE C CB  1 
ATOM   1832 C CG  . PHE C 1 53 ? 21.157  -37.532 29.935  1.00 47.10  ? 52  PHE C CG  1 
ATOM   1833 C CD1 . PHE C 1 53 ? 21.019  -36.270 30.504  1.00 52.03  ? 52  PHE C CD1 1 
ATOM   1834 C CD2 . PHE C 1 53 ? 20.435  -38.587 30.486  1.00 61.89  ? 52  PHE C CD2 1 
ATOM   1835 C CE1 . PHE C 1 53 ? 20.202  -36.072 31.617  1.00 55.13  ? 52  PHE C CE1 1 
ATOM   1836 C CE2 . PHE C 1 53 ? 19.631  -38.389 31.608  1.00 63.25  ? 52  PHE C CE2 1 
ATOM   1837 C CZ  . PHE C 1 53 ? 19.510  -37.132 32.172  1.00 51.89  ? 52  PHE C CZ  1 
ATOM   1838 N N   . LEU C 1 54 ? 23.500  -35.351 26.684  1.00 43.72  ? 53  LEU C N   1 
ATOM   1839 C CA  . LEU C 1 54 ? 24.607  -35.052 25.791  1.00 43.45  ? 53  LEU C CA  1 
ATOM   1840 C C   . LEU C 1 54 ? 25.664  -34.330 26.605  1.00 36.08  ? 53  LEU C C   1 
ATOM   1841 O O   . LEU C 1 54 ? 25.346  -33.638 27.570  1.00 37.90  ? 53  LEU C O   1 
ATOM   1842 C CB  . LEU C 1 54 ? 24.202  -34.225 24.567  1.00 42.11  ? 53  LEU C CB  1 
ATOM   1843 C CG  . LEU C 1 54 ? 23.389  -34.953 23.497  1.00 45.03  ? 53  LEU C CG  1 
ATOM   1844 C CD1 . LEU C 1 54 ? 23.182  -34.004 22.334  1.00 39.93  ? 53  LEU C CD1 1 
ATOM   1845 C CD2 . LEU C 1 54 ? 24.061  -36.234 22.995  1.00 48.89  ? 53  LEU C CD2 1 
ATOM   1846 N N   . GLY C 1 55 ? 26.919  -34.593 26.250  1.00 36.86  ? 54  GLY C N   1 
ATOM   1847 C CA  . GLY C 1 55 ? 28.052  -33.926 26.851  1.00 38.66  ? 54  GLY C CA  1 
ATOM   1848 C C   . GLY C 1 55 ? 28.357  -32.643 26.086  1.00 50.58  ? 54  GLY C C   1 
ATOM   1849 O O   . GLY C 1 55 ? 27.930  -32.484 24.925  1.00 45.40  ? 54  GLY C O   1 
ATOM   1850 N N   . PRO C 1 56 ? 29.108  -31.707 26.716  1.00 49.98  ? 55  PRO C N   1 
ATOM   1851 C CA  . PRO C 1 56 ? 29.209  -30.338 26.208  1.00 57.19  ? 55  PRO C CA  1 
ATOM   1852 C C   . PRO C 1 56 ? 29.846  -30.248 24.826  1.00 47.96  ? 55  PRO C C   1 
ATOM   1853 O O   . PRO C 1 56 ? 29.584  -29.314 24.080  1.00 55.92  ? 55  PRO C O   1 
ATOM   1854 C CB  . PRO C 1 56 ? 29.998  -29.590 27.306  1.00 57.64  ? 55  PRO C CB  1 
ATOM   1855 C CG  . PRO C 1 56 ? 30.809  -30.690 27.961  1.00 48.64  ? 55  PRO C CG  1 
ATOM   1856 C CD  . PRO C 1 56 ? 29.853  -31.893 27.976  1.00 53.54  ? 55  PRO C CD  1 
ATOM   1857 N N   . LYS C 1 57 ? 30.637  -31.253 24.478  1.00 45.13  ? 56  LYS C N   1 
ATOM   1858 C CA  . LYS C 1 57 ? 31.288  -31.298 23.179  1.00 48.49  ? 56  LYS C CA  1 
ATOM   1859 C C   . LYS C 1 57 ? 30.244  -31.328 22.063  1.00 53.19  ? 56  LYS C C   1 
ATOM   1860 O O   . LYS C 1 57 ? 30.551  -30.982 20.914  1.00 51.94  ? 56  LYS C O   1 
ATOM   1861 C CB  . LYS C 1 57 ? 32.186  -32.539 23.111  1.00 53.03  ? 56  LYS C CB  1 
ATOM   1862 N N   . ASP C 1 58 ? 29.012  -31.729 22.420  1.00 53.35  ? 57  ASP C N   1 
ATOM   1863 C CA  . ASP C 1 58 ? 27.982  -32.049 21.447  1.00 51.15  ? 57  ASP C CA  1 
ATOM   1864 C C   . ASP C 1 58 ? 27.065  -30.867 21.191  1.00 47.31  ? 57  ASP C C   1 
ATOM   1865 O O   . ASP C 1 58 ? 26.104  -30.999 20.433  1.00 43.14  ? 57  ASP C O   1 
ATOM   1866 C CB  . ASP C 1 58 ? 27.098  -33.186 21.918  1.00 50.40  ? 57  ASP C CB  1 
ATOM   1867 C CG  . ASP C 1 58 ? 27.826  -34.514 21.940  1.00 53.32  ? 57  ASP C CG  1 
ATOM   1868 O OD1 . ASP C 1 58 ? 28.795  -34.626 21.160  1.00 49.36  ? 57  ASP C OD1 1 
ATOM   1869 O OD2 . ASP C 1 58 ? 27.432  -35.383 22.753  1.00 51.14  ? 57  ASP C OD2 1 
ATOM   1870 N N   . LEU C 1 59 ? 27.368  -29.745 21.844  1.00 43.67  ? 58  LEU C N   1 
ATOM   1871 C CA  . LEU C 1 59 ? 26.436  -28.646 22.028  1.00 44.73  ? 58  LEU C CA  1 
ATOM   1872 C C   . LEU C 1 59 ? 27.069  -27.369 21.492  1.00 45.43  ? 58  LEU C C   1 
ATOM   1873 O O   . LEU C 1 59 ? 28.276  -27.180 21.646  1.00 51.71  ? 58  LEU C O   1 
ATOM   1874 C CB  . LEU C 1 59 ? 26.159  -28.550 23.526  1.00 43.09  ? 58  LEU C CB  1 
ATOM   1875 C CG  . LEU C 1 59 ? 25.537  -29.783 24.194  1.00 35.99  ? 58  LEU C CG  1 
ATOM   1876 C CD1 . LEU C 1 59 ? 25.393  -29.443 25.693  1.00 34.33  ? 58  LEU C CD1 1 
ATOM   1877 C CD2 . LEU C 1 59 ? 24.179  -30.179 23.556  1.00 31.17  ? 58  LEU C CD2 1 
ATOM   1878 N N   . PHE C 1 60 ? 26.254  -26.536 20.833  1.00 45.19  ? 59  PHE C N   1 
ATOM   1879 C CA  . PHE C 1 60 ? 26.720  -25.340 20.133  1.00 47.87  ? 59  PHE C CA  1 
ATOM   1880 C C   . PHE C 1 60 ? 25.756  -24.189 20.424  1.00 47.77  ? 59  PHE C C   1 
ATOM   1881 O O   . PHE C 1 60 ? 24.560  -24.328 20.197  1.00 47.14  ? 59  PHE C O   1 
ATOM   1882 C CB  . PHE C 1 60 ? 26.973  -25.540 18.632  1.00 47.87  ? 59  PHE C CB  1 
ATOM   1883 C CG  . PHE C 1 60 ? 27.944  -26.672 18.329  1.00 47.52  ? 59  PHE C CG  1 
ATOM   1884 C CD1 . PHE C 1 60 ? 27.506  -27.996 18.338  1.00 43.68  ? 59  PHE C CD1 1 
ATOM   1885 C CD2 . PHE C 1 60 ? 29.285  -26.418 18.032  1.00 52.16  ? 59  PHE C CD2 1 
ATOM   1886 C CE1 . PHE C 1 60 ? 28.381  -29.043 18.105  1.00 35.21  ? 59  PHE C CE1 1 
ATOM   1887 C CE2 . PHE C 1 60 ? 30.169  -27.469 17.777  1.00 48.52  ? 59  PHE C CE2 1 
ATOM   1888 C CZ  . PHE C 1 60 ? 29.717  -28.777 17.824  1.00 46.99  ? 59  PHE C CZ  1 
ATOM   1889 N N   . PRO C 1 61 ? 26.222  -23.054 21.011  1.00 48.12  ? 60  PRO C N   1 
ATOM   1890 C CA  . PRO C 1 61 ? 25.333  -21.927 21.301  1.00 48.29  ? 60  PRO C CA  1 
ATOM   1891 C C   . PRO C 1 61 ? 24.636  -21.511 20.009  1.00 53.69  ? 60  PRO C C   1 
ATOM   1892 O O   . PRO C 1 61 ? 25.294  -21.364 18.977  1.00 47.19  ? 60  PRO C O   1 
ATOM   1893 C CB  . PRO C 1 61 ? 26.233  -20.815 21.874  1.00 52.47  ? 60  PRO C CB  1 
ATOM   1894 C CG  . PRO C 1 61 ? 27.549  -21.503 22.188  1.00 41.42  ? 60  PRO C CG  1 
ATOM   1895 C CD  . PRO C 1 61 ? 27.614  -22.825 21.447  1.00 46.55  ? 60  PRO C CD  1 
ATOM   1896 N N   . TYR C 1 62 ? 23.302  -21.365 20.116  1.00 58.51  ? 61  TYR C N   1 
ATOM   1897 C CA  . TYR C 1 62 ? 22.351  -21.192 19.029  1.00 53.54  ? 61  TYR C CA  1 
ATOM   1898 C C   . TYR C 1 62 ? 22.751  -19.988 18.177  1.00 61.02  ? 61  TYR C C   1 
ATOM   1899 O O   . TYR C 1 62 ? 22.972  -20.126 16.970  1.00 55.02  ? 61  TYR C O   1 
ATOM   1900 C CB  . TYR C 1 62 ? 20.908  -21.059 19.537  1.00 52.20  ? 61  TYR C CB  1 
ATOM   1901 C CG  . TYR C 1 62 ? 19.918  -20.702 18.436  1.00 57.86  ? 61  TYR C CG  1 
ATOM   1902 C CD1 . TYR C 1 62 ? 19.782  -21.512 17.309  1.00 57.46  ? 61  TYR C CD1 1 
ATOM   1903 C CD2 . TYR C 1 62 ? 19.196  -19.509 18.475  1.00 57.13  ? 61  TYR C CD2 1 
ATOM   1904 C CE1 . TYR C 1 62 ? 18.902  -21.183 16.289  1.00 55.51  ? 61  TYR C CE1 1 
ATOM   1905 C CE2 . TYR C 1 62 ? 18.329  -19.155 17.452  1.00 55.50  ? 61  TYR C CE2 1 
ATOM   1906 C CZ  . TYR C 1 62 ? 18.192  -19.994 16.354  1.00 52.56  ? 61  TYR C CZ  1 
ATOM   1907 O OH  . TYR C 1 62 ? 17.352  -19.682 15.335  1.00 46.69  ? 61  TYR C OH  1 
ATOM   1908 N N   . ASP C 1 63 ? 22.887  -18.832 18.834  1.00 58.22  ? 62  ASP C N   1 
ATOM   1909 C CA  . ASP C 1 63 ? 23.184  -17.572 18.171  1.00 64.38  ? 62  ASP C CA  1 
ATOM   1910 C C   . ASP C 1 63 ? 24.559  -17.597 17.520  1.00 56.29  ? 62  ASP C C   1 
ATOM   1911 O O   . ASP C 1 63 ? 24.718  -17.075 16.420  1.00 62.08  ? 62  ASP C O   1 
ATOM   1912 C CB  . ASP C 1 63 ? 22.949  -16.379 19.080  1.00 79.94  ? 62  ASP C CB  1 
ATOM   1913 C CG  . ASP C 1 63 ? 21.502  -15.917 19.108  1.00 85.14  ? 62  ASP C CG  1 
ATOM   1914 O OD1 . ASP C 1 63 ? 21.106  -15.312 20.123  1.00 87.58  ? 62  ASP C OD1 1 
ATOM   1915 O OD2 . ASP C 1 63 ? 20.793  -16.148 18.098  1.00 87.09  ? 62  ASP C OD2 1 
ATOM   1916 N N   . LYS C 1 64 ? 25.531  -18.237 18.171  1.00 46.48  ? 63  LYS C N   1 
ATOM   1917 C CA  . LYS C 1 64 ? 26.869  -18.341 17.601  1.00 46.99  ? 63  LYS C CA  1 
ATOM   1918 C C   . LYS C 1 64 ? 26.886  -19.183 16.322  1.00 53.84  ? 63  LYS C C   1 
ATOM   1919 O O   . LYS C 1 64 ? 27.684  -18.889 15.428  1.00 48.66  ? 63  LYS C O   1 
ATOM   1920 C CB  . LYS C 1 64 ? 27.918  -18.887 18.575  1.00 43.35  ? 63  LYS C CB  1 
ATOM   1921 N N   . SER C 1 65 ? 26.027  -20.226 16.239  1.00 51.56  ? 64  SER C N   1 
ATOM   1922 C CA  . SER C 1 65 ? 26.232  -21.297 15.261  1.00 47.19  ? 64  SER C CA  1 
ATOM   1923 C C   . SER C 1 65 ? 25.084  -21.399 14.240  1.00 47.48  ? 64  SER C C   1 
ATOM   1924 O O   . SER C 1 65 ? 25.130  -22.190 13.294  1.00 41.72  ? 64  SER C O   1 
ATOM   1925 C CB  . SER C 1 65 ? 26.499  -22.613 15.978  1.00 47.89  ? 64  SER C CB  1 
ATOM   1926 O OG  . SER C 1 65 ? 25.321  -22.993 16.686  1.00 46.31  ? 64  SER C OG  1 
ATOM   1927 N N   . LYS C 1 66 ? 24.036  -20.586 14.408  1.00 41.13  ? 65  LYS C N   1 
ATOM   1928 C CA  . LYS C 1 66 ? 22.883  -20.733 13.537  1.00 45.60  ? 65  LYS C CA  1 
ATOM   1929 C C   . LYS C 1 66 ? 23.259  -20.518 12.072  1.00 48.28  ? 65  LYS C C   1 
ATOM   1930 O O   . LYS C 1 66 ? 22.754  -21.233 11.215  1.00 52.70  ? 65  LYS C O   1 
ATOM   1931 C CB  . LYS C 1 66 ? 21.649  -19.968 14.013  1.00 40.52  ? 65  LYS C CB  1 
ATOM   1932 C CG  . LYS C 1 66 ? 21.685  -18.478 13.811  1.00 45.45  ? 65  LYS C CG  1 
ATOM   1933 C CD  . LYS C 1 66 ? 20.520  -17.802 14.513  1.00 54.45  ? 65  LYS C CD  1 
ATOM   1934 C CE  . LYS C 1 66 ? 20.562  -16.316 14.419  1.00 57.32  ? 65  LYS C CE  1 
ATOM   1935 N NZ  . LYS C 1 66 ? 19.485  -15.778 15.254  1.00 68.07  ? 65  LYS C NZ  1 
ATOM   1936 N N   . ASP C 1 67 ? 24.168  -19.577 11.785  1.00 51.55  ? 66  ASP C N   1 
ATOM   1937 C CA  . ASP C 1 67 ? 24.570  -19.309 10.402  1.00 49.97  ? 66  ASP C CA  1 
ATOM   1938 C C   . ASP C 1 67 ? 25.066  -20.604 9.764   1.00 47.87  ? 66  ASP C C   1 
ATOM   1939 O O   . ASP C 1 67 ? 24.913  -20.811 8.570   1.00 46.86  ? 66  ASP C O   1 
ATOM   1940 C CB  . ASP C 1 67 ? 25.445  -18.067 10.235  1.00 50.58  ? 66  ASP C CB  1 
ATOM   1941 C CG  . ASP C 1 67 ? 26.829  -18.069 10.883  1.00 58.68  ? 66  ASP C CG  1 
ATOM   1942 O OD1 . ASP C 1 67 ? 27.310  -19.150 11.284  1.00 63.25  ? 66  ASP C OD1 1 
ATOM   1943 O OD2 . ASP C 1 67 ? 27.422  -16.969 11.004  1.00 65.28  ? 66  ASP C OD2 1 
ATOM   1944 N N   . LYS C 1 68 ? 25.574  -21.520 10.594  1.00 44.65  ? 67  LYS C N   1 
ATOM   1945 C CA  . LYS C 1 68 ? 26.133  -22.769 10.093  1.00 44.26  ? 67  LYS C CA  1 
ATOM   1946 C C   . LYS C 1 68 ? 25.101  -23.906 10.174  1.00 43.13  ? 67  LYS C C   1 
ATOM   1947 O O   . LYS C 1 68 ? 24.972  -24.664 9.224   1.00 41.07  ? 67  LYS C O   1 
ATOM   1948 C CB  . LYS C 1 68 ? 27.471  -23.057 10.794  1.00 44.13  ? 67  LYS C CB  1 
ATOM   1949 C CG  . LYS C 1 68 ? 28.179  -24.372 10.490  1.00 56.32  ? 67  LYS C CG  1 
ATOM   1950 C CD  . LYS C 1 68 ? 29.392  -24.495 11.415  1.00 64.23  ? 67  LYS C CD  1 
ATOM   1951 C CE  . LYS C 1 68 ? 30.085  -25.823 11.360  1.00 71.42  ? 67  LYS C CE  1 
ATOM   1952 N NZ  . LYS C 1 68 ? 30.297  -26.282 9.984   1.00 75.83  ? 67  LYS C NZ  1 
ATOM   1953 N N   . TYR C 1 69 ? 24.385  -24.067 11.305  1.00 37.02  ? 68  TYR C N   1 
ATOM   1954 C CA  . TYR C 1 69 ? 23.571  -25.272 11.419  1.00 39.61  ? 68  TYR C CA  1 
ATOM   1955 C C   . TYR C 1 69 ? 22.094  -24.968 11.161  1.00 41.32  ? 68  TYR C C   1 
ATOM   1956 O O   . TYR C 1 69 ? 21.309  -25.888 10.975  1.00 39.27  ? 68  TYR C O   1 
ATOM   1957 C CB  . TYR C 1 69 ? 23.705  -25.872 12.826  1.00 38.14  ? 68  TYR C CB  1 
ATOM   1958 C CG  . TYR C 1 69 ? 25.116  -26.310 13.170  1.00 40.11  ? 68  TYR C CG  1 
ATOM   1959 C CD1 . TYR C 1 69 ? 25.859  -27.110 12.302  1.00 40.53  ? 68  TYR C CD1 1 
ATOM   1960 C CD2 . TYR C 1 69 ? 25.723  -25.872 14.341  1.00 45.57  ? 68  TYR C CD2 1 
ATOM   1961 C CE1 . TYR C 1 69 ? 27.154  -27.502 12.601  1.00 39.02  ? 68  TYR C CE1 1 
ATOM   1962 C CE2 . TYR C 1 69 ? 27.010  -26.276 14.664  1.00 45.86  ? 68  TYR C CE2 1 
ATOM   1963 C CZ  . TYR C 1 69 ? 27.731  -27.070 13.785  1.00 43.56  ? 68  TYR C CZ  1 
ATOM   1964 O OH  . TYR C 1 69 ? 29.007  -27.436 14.133  1.00 45.04  ? 68  TYR C OH  1 
ATOM   1965 N N   . GLY C 1 70 ? 21.705  -23.684 11.245  1.00 34.78  ? 69  GLY C N   1 
ATOM   1966 C CA  . GLY C 1 70 ? 20.306  -23.318 11.086  1.00 45.11  ? 69  GLY C CA  1 
ATOM   1967 C C   . GLY C 1 70 ? 19.972  -23.190 9.604   1.00 46.36  ? 69  GLY C C   1 
ATOM   1968 O O   . GLY C 1 70 ? 19.935  -22.092 9.056   1.00 50.28  ? 69  GLY C O   1 
ATOM   1969 N N   . LYS C 1 71 ? 19.841  -24.338 8.948   1.00 42.75  ? 70  LYS C N   1 
ATOM   1970 C CA  . LYS C 1 71 ? 19.472  -24.418 7.544   1.00 42.91  ? 70  LYS C CA  1 
ATOM   1971 C C   . LYS C 1 71 ? 18.599  -25.654 7.441   1.00 43.40  ? 70  LYS C C   1 
ATOM   1972 O O   . LYS C 1 71 ? 18.774  -26.592 8.209   1.00 45.39  ? 70  LYS C O   1 
ATOM   1973 C CB  . LYS C 1 71 ? 20.663  -24.607 6.596   1.00 38.84  ? 70  LYS C CB  1 
ATOM   1974 C CG  . LYS C 1 71 ? 21.732  -25.489 7.218   1.00 50.27  ? 70  LYS C CG  1 
ATOM   1975 C CD  . LYS C 1 71 ? 22.746  -26.234 6.353   1.00 61.73  ? 70  LYS C CD  1 
ATOM   1976 C CE  . LYS C 1 71 ? 23.675  -27.072 7.210   1.00 55.97  ? 70  LYS C CE  1 
ATOM   1977 N N   . PRO C 1 72 ? 17.596  -25.674 6.550   1.00 37.24  ? 71  PRO C N   1 
ATOM   1978 C CA  . PRO C 1 72 ? 16.701  -26.828 6.468   1.00 38.42  ? 71  PRO C CA  1 
ATOM   1979 C C   . PRO C 1 72 ? 17.347  -28.151 6.065   1.00 41.62  ? 71  PRO C C   1 
ATOM   1980 O O   . PRO C 1 72 ? 18.332  -28.195 5.329   1.00 42.13  ? 71  PRO C O   1 
ATOM   1981 C CB  . PRO C 1 72 ? 15.698  -26.333 5.410   1.00 37.02  ? 71  PRO C CB  1 
ATOM   1982 C CG  . PRO C 1 72 ? 15.722  -24.836 5.613   1.00 36.15  ? 71  PRO C CG  1 
ATOM   1983 C CD  . PRO C 1 72 ? 17.215  -24.560 5.664   1.00 37.93  ? 71  PRO C CD  1 
ATOM   1984 N N   . ASN C 1 73 ? 16.747  -29.243 6.530   1.00 39.85  ? 72  ASN C N   1 
ATOM   1985 C CA  . ASN C 1 73 ? 17.002  -30.528 5.909   1.00 46.28  ? 72  ASN C CA  1 
ATOM   1986 C C   . ASN C 1 73 ? 15.716  -31.321 6.058   1.00 37.95  ? 72  ASN C C   1 
ATOM   1987 O O   . ASN C 1 73 ? 14.786  -30.826 6.690   1.00 31.72  ? 72  ASN C O   1 
ATOM   1988 C CB  . ASN C 1 73 ? 18.241  -31.247 6.439   1.00 45.49  ? 72  ASN C CB  1 
ATOM   1989 C CG  . ASN C 1 73 ? 18.050  -31.622 7.884   1.00 44.17  ? 72  ASN C CG  1 
ATOM   1990 O OD1 . ASN C 1 73 ? 17.099  -32.348 8.232   1.00 40.63  ? 72  ASN C OD1 1 
ATOM   1991 N ND2 . ASN C 1 73 ? 18.888  -31.044 8.726   1.00 45.10  ? 72  ASN C ND2 1 
ATOM   1992 N N   . LYS C 1 74 ? 15.717  -32.542 5.509   1.00 39.05  ? 73  LYS C N   1 
ATOM   1993 C CA  . LYS C 1 74 ? 14.480  -33.278 5.342   1.00 45.52  ? 73  LYS C CA  1 
ATOM   1994 C C   . LYS C 1 74 ? 14.263  -34.244 6.496   1.00 42.92  ? 73  LYS C C   1 
ATOM   1995 O O   . LYS C 1 74 ? 13.276  -34.959 6.481   1.00 43.51  ? 73  LYS C O   1 
ATOM   1996 C CB  . LYS C 1 74 ? 14.427  -33.960 3.971   1.00 51.76  ? 73  LYS C CB  1 
ATOM   1997 C CG  . LYS C 1 74 ? 13.518  -33.185 2.982   1.00 54.10  ? 73  LYS C CG  1 
ATOM   1998 C CD  . LYS C 1 74 ? 14.339  -32.250 2.115   1.00 59.21  ? 73  LYS C CD  1 
ATOM   1999 N N   . ARG C 1 75 ? 15.150  -34.244 7.500   1.00 37.04  ? 74  ARG C N   1 
ATOM   2000 C CA  . ARG C 1 75 ? 14.973  -35.185 8.609   1.00 44.68  ? 74  ARG C CA  1 
ATOM   2001 C C   . ARG C 1 75 ? 13.697  -34.833 9.375   1.00 43.98  ? 74  ARG C C   1 
ATOM   2002 O O   . ARG C 1 75 ? 13.406  -33.651 9.598   1.00 41.34  ? 74  ARG C O   1 
ATOM   2003 C CB  . ARG C 1 75 ? 16.155  -35.265 9.595   1.00 39.02  ? 74  ARG C CB  1 
ATOM   2004 C CG  . ARG C 1 75 ? 17.497  -35.614 8.944   1.00 45.52  ? 74  ARG C CG  1 
ATOM   2005 C CD  . ARG C 1 75 ? 17.580  -37.024 8.322   1.00 44.78  ? 74  ARG C CD  1 
ATOM   2006 N NE  . ARG C 1 75 ? 17.409  -38.047 9.366   1.00 48.20  ? 74  ARG C NE  1 
ATOM   2007 C CZ  . ARG C 1 75 ? 18.346  -38.573 10.165  1.00 41.95  ? 74  ARG C CZ  1 
ATOM   2008 N NH1 . ARG C 1 75 ? 17.995  -39.381 11.148  1.00 49.48  ? 74  ARG C NH1 1 
ATOM   2009 N NH2 . ARG C 1 75 ? 19.614  -38.285 9.977   1.00 39.32  ? 74  ARG C NH2 1 
ATOM   2010 N N   . LYS C 1 76 ? 13.011  -35.882 9.850   1.00 43.19  ? 75  LYS C N   1 
ATOM   2011 C CA  . LYS C 1 76 ? 11.721  -35.775 10.524  1.00 44.36  ? 75  LYS C CA  1 
ATOM   2012 C C   . LYS C 1 76 ? 11.763  -34.786 11.689  1.00 40.14  ? 75  LYS C C   1 
ATOM   2013 O O   . LYS C 1 76 ? 12.517  -34.974 12.646  1.00 37.72  ? 75  LYS C O   1 
ATOM   2014 C CB  . LYS C 1 76 ? 11.132  -37.133 10.937  1.00 46.05  ? 75  LYS C CB  1 
ATOM   2015 C CG  . LYS C 1 76 ? 9.595   -37.176 10.848  1.00 52.65  ? 75  LYS C CG  1 
ATOM   2016 C CD  . LYS C 1 76 ? 8.879   -38.009 11.916  1.00 62.73  ? 75  LYS C CD  1 
ATOM   2017 N N   . GLY C 1 77 ? 10.887  -33.775 11.614  1.00 40.38  ? 76  GLY C N   1 
ATOM   2018 C CA  . GLY C 1 77 ? 10.678  -32.841 12.709  1.00 38.90  ? 76  GLY C CA  1 
ATOM   2019 C C   . GLY C 1 77 ? 11.672  -31.676 12.645  1.00 37.12  ? 76  GLY C C   1 
ATOM   2020 O O   . GLY C 1 77 ? 11.527  -30.683 13.363  1.00 50.27  ? 76  GLY C O   1 
ATOM   2021 N N   . PHE C 1 78 ? 12.695  -31.801 11.787  1.00 39.06  ? 77  PHE C N   1 
ATOM   2022 C CA  . PHE C 1 78 ? 13.784  -30.833 11.756  1.00 37.61  ? 77  PHE C CA  1 
ATOM   2023 C C   . PHE C 1 78 ? 13.282  -29.407 11.491  1.00 40.41  ? 77  PHE C C   1 
ATOM   2024 O O   . PHE C 1 78 ? 13.618  -28.496 12.253  1.00 36.04  ? 77  PHE C O   1 
ATOM   2025 C CB  . PHE C 1 78 ? 14.908  -31.217 10.783  1.00 37.06  ? 77  PHE C CB  1 
ATOM   2026 C CG  . PHE C 1 78 ? 16.182  -30.411 11.030  1.00 36.00  ? 77  PHE C CG  1 
ATOM   2027 C CD1 . PHE C 1 78 ? 16.399  -29.207 10.370  1.00 33.83  ? 77  PHE C CD1 1 
ATOM   2028 C CD2 . PHE C 1 78 ? 17.197  -30.889 11.855  1.00 33.86  ? 77  PHE C CD2 1 
ATOM   2029 C CE1 . PHE C 1 78 ? 17.546  -28.466 10.601  1.00 34.50  ? 77  PHE C CE1 1 
ATOM   2030 C CE2 . PHE C 1 78 ? 18.356  -30.140 12.068  1.00 30.58  ? 77  PHE C CE2 1 
ATOM   2031 C CZ  . PHE C 1 78 ? 18.528  -28.935 11.436  1.00 31.70  ? 77  PHE C CZ  1 
ATOM   2032 N N   . ASN C 1 79 ? 12.536  -29.211 10.386  1.00 34.17  ? 78  ASN C N   1 
ATOM   2033 C CA  . ASN C 1 79 ? 12.170  -27.869 9.962   1.00 34.91  ? 78  ASN C CA  1 
ATOM   2034 C C   . ASN C 1 79 ? 11.185  -27.224 10.943  1.00 30.87  ? 78  ASN C C   1 
ATOM   2035 O O   . ASN C 1 79 ? 11.333  -26.061 11.314  1.00 35.51  ? 78  ASN C O   1 
ATOM   2036 C CB  . ASN C 1 79 ? 11.753  -27.822 8.495   1.00 34.13  ? 78  ASN C CB  1 
ATOM   2037 C CG  . ASN C 1 79 ? 12.860  -28.287 7.576   1.00 32.11  ? 78  ASN C CG  1 
ATOM   2038 O OD1 . ASN C 1 79 ? 14.048  -28.101 7.852   1.00 38.73  ? 78  ASN C OD1 1 
ATOM   2039 N ND2 . ASN C 1 79 ? 12.490  -28.826 6.431   1.00 34.05  ? 78  ASN C ND2 1 
ATOM   2040 N N   . GLU C 1 80 ? 10.215  -27.978 11.431  1.00 35.57  ? 79  GLU C N   1 
ATOM   2041 C CA  . GLU C 1 80 ? 9.439   -27.523 12.584  1.00 39.48  ? 79  GLU C CA  1 
ATOM   2042 C C   . GLU C 1 80 ? 10.336  -27.107 13.753  1.00 40.74  ? 79  GLU C C   1 
ATOM   2043 O O   . GLU C 1 80 ? 10.099  -26.066 14.381  1.00 44.21  ? 79  GLU C O   1 
ATOM   2044 C CB  . GLU C 1 80 ? 8.410   -28.570 13.024  1.00 37.92  ? 79  GLU C CB  1 
ATOM   2045 C CG  . GLU C 1 80 ? 7.534   -28.055 14.160  1.00 40.87  ? 79  GLU C CG  1 
ATOM   2046 C CD  . GLU C 1 80 ? 6.239   -28.846 14.258  1.00 54.90  ? 79  GLU C CD  1 
ATOM   2047 O OE1 . GLU C 1 80 ? 6.114   -29.873 13.562  1.00 56.66  ? 79  GLU C OE1 1 
ATOM   2048 O OE2 . GLU C 1 80 ? 5.341   -28.435 15.019  1.00 56.09  ? 79  GLU C OE2 1 
ATOM   2049 N N   . GLY C 1 81 ? 11.370  -27.920 14.055  1.00 41.22  ? 80  GLY C N   1 
ATOM   2050 C CA  . GLY C 1 81 ? 12.326  -27.566 15.102  1.00 36.86  ? 80  GLY C CA  1 
ATOM   2051 C C   . GLY C 1 81 ? 12.970  -26.196 14.873  1.00 34.13  ? 80  GLY C C   1 
ATOM   2052 O O   . GLY C 1 81 ? 13.217  -25.436 15.811  1.00 34.16  ? 80  GLY C O   1 
ATOM   2053 N N   . LEU C 1 82 ? 13.341  -25.923 13.619  1.00 34.18  ? 81  LEU C N   1 
ATOM   2054 C CA  . LEU C 1 82 ? 13.950  -24.647 13.257  1.00 39.13  ? 81  LEU C CA  1 
ATOM   2055 C C   . LEU C 1 82 ? 12.970  -23.497 13.515  1.00 37.69  ? 81  LEU C C   1 
ATOM   2056 O O   . LEU C 1 82 ? 13.382  -22.412 13.960  1.00 39.53  ? 81  LEU C O   1 
ATOM   2057 C CB  . LEU C 1 82 ? 14.372  -24.675 11.786  1.00 38.95  ? 81  LEU C CB  1 
ATOM   2058 C CG  . LEU C 1 82 ? 15.604  -25.502 11.416  1.00 29.82  ? 81  LEU C CG  1 
ATOM   2059 C CD1 . LEU C 1 82 ? 15.809  -25.262 9.908   1.00 33.76  ? 81  LEU C CD1 1 
ATOM   2060 C CD2 . LEU C 1 82 ? 16.787  -25.002 12.204  1.00 34.02  ? 81  LEU C CD2 1 
ATOM   2061 N N   . TRP C 1 83 ? 11.675  -23.751 13.243  1.00 37.64  ? 82  TRP C N   1 
ATOM   2062 C CA  . TRP C 1 83 ? 10.636  -22.759 13.514  1.00 42.92  ? 82  TRP C CA  1 
ATOM   2063 C C   . TRP C 1 83 ? 10.538  -22.431 15.017  1.00 45.70  ? 82  TRP C C   1 
ATOM   2064 O O   . TRP C 1 83 ? 10.590  -21.257 15.405  1.00 38.78  ? 82  TRP C O   1 
ATOM   2065 C CB  . TRP C 1 83 ? 9.276   -23.143 12.916  1.00 40.25  ? 82  TRP C CB  1 
ATOM   2066 C CG  . TRP C 1 83 ? 8.272   -22.011 13.039  1.00 54.40  ? 82  TRP C CG  1 
ATOM   2067 C CD1 . TRP C 1 83 ? 8.047   -20.991 12.151  1.00 46.72  ? 82  TRP C CD1 1 
ATOM   2068 C CD2 . TRP C 1 83 ? 7.409   -21.740 14.173  1.00 52.10  ? 82  TRP C CD2 1 
ATOM   2069 N NE1 . TRP C 1 83 ? 7.082   -20.145 12.626  1.00 47.04  ? 82  TRP C NE1 1 
ATOM   2070 C CE2 . TRP C 1 83 ? 6.670   -20.577 13.857  1.00 45.73  ? 82  TRP C CE2 1 
ATOM   2071 C CE3 . TRP C 1 83 ? 7.182   -22.379 15.407  1.00 50.47  ? 82  TRP C CE3 1 
ATOM   2072 C CZ2 . TRP C 1 83 ? 5.742   -20.030 14.741  1.00 53.37  ? 82  TRP C CZ2 1 
ATOM   2073 C CZ3 . TRP C 1 83 ? 6.250   -21.843 16.277  1.00 52.32  ? 82  TRP C CZ3 1 
ATOM   2074 C CH2 . TRP C 1 83 ? 5.560   -20.667 15.953  1.00 54.98  ? 82  TRP C CH2 1 
ATOM   2075 N N   . GLU C 1 84 ? 10.412  -23.479 15.843  1.00 43.35  ? 83  GLU C N   1 
ATOM   2076 C CA  . GLU C 1 84 ? 10.317  -23.372 17.294  1.00 48.50  ? 83  GLU C CA  1 
ATOM   2077 C C   . GLU C 1 84 ? 11.496  -22.614 17.885  1.00 46.17  ? 83  GLU C C   1 
ATOM   2078 O O   . GLU C 1 84 ? 11.283  -21.741 18.726  1.00 47.91  ? 83  GLU C O   1 
ATOM   2079 C CB  . GLU C 1 84 ? 10.187  -24.736 17.965  1.00 41.61  ? 83  GLU C CB  1 
ATOM   2080 C CG  . GLU C 1 84 ? 8.923   -25.441 17.502  1.00 40.39  ? 83  GLU C CG  1 
ATOM   2081 C CD  . GLU C 1 84 ? 8.805   -26.829 18.076  1.00 43.73  ? 83  GLU C CD  1 
ATOM   2082 O OE1 . GLU C 1 84 ? 9.805   -27.296 18.652  1.00 42.51  ? 83  GLU C OE1 1 
ATOM   2083 O OE2 . GLU C 1 84 ? 7.721   -27.439 17.951  1.00 47.04  ? 83  GLU C OE2 1 
ATOM   2084 N N   . ILE C 1 85 ? 12.727  -22.924 17.451  1.00 45.50  ? 84  ILE C N   1 
ATOM   2085 C CA  . ILE C 1 85 ? 13.894  -22.307 18.087  1.00 43.57  ? 84  ILE C CA  1 
ATOM   2086 C C   . ILE C 1 85 ? 13.956  -20.797 17.803  1.00 48.32  ? 84  ILE C C   1 
ATOM   2087 O O   . ILE C 1 85 ? 14.326  -20.034 18.687  1.00 43.78  ? 84  ILE C O   1 
ATOM   2088 C CB  . ILE C 1 85 ? 15.202  -23.070 17.798  1.00 38.72  ? 84  ILE C CB  1 
ATOM   2089 C CG1 . ILE C 1 85 ? 16.347  -22.659 18.763  1.00 38.65  ? 84  ILE C CG1 1 
ATOM   2090 C CG2 . ILE C 1 85 ? 15.608  -23.014 16.318  1.00 38.39  ? 84  ILE C CG2 1 
ATOM   2091 C CD1 . ILE C 1 85 ? 17.566  -23.586 18.762  1.00 37.87  ? 84  ILE C CD1 1 
ATOM   2092 N N   . GLN C 1 86 ? 13.499  -20.362 16.616  1.00 48.43  ? 85  GLN C N   1 
ATOM   2093 C CA  . GLN C 1 86 ? 13.481  -18.951 16.223  1.00 46.42  ? 85  GLN C CA  1 
ATOM   2094 C C   . GLN C 1 86 ? 12.278  -18.225 16.828  1.00 43.09  ? 85  GLN C C   1 
ATOM   2095 O O   . GLN C 1 86 ? 12.445  -17.101 17.285  1.00 44.72  ? 85  GLN C O   1 
ATOM   2096 C CB  . GLN C 1 86 ? 13.531  -18.787 14.695  1.00 45.27  ? 85  GLN C CB  1 
ATOM   2097 C CG  . GLN C 1 86 ? 13.864  -17.406 14.124  1.00 43.00  ? 85  GLN C CG  1 
ATOM   2098 C CD  . GLN C 1 86 ? 14.349  -17.463 12.673  1.00 44.71  ? 85  GLN C CD  1 
ATOM   2099 O OE1 . GLN C 1 86 ? 14.253  -18.480 11.975  1.00 43.37  ? 85  GLN C OE1 1 
ATOM   2100 N NE2 . GLN C 1 86 ? 14.941  -16.381 12.187  1.00 40.85  ? 85  GLN C NE2 1 
ATOM   2101 N N   . ASN C 1 87 ? 11.103  -18.875 16.847  1.00 44.93  ? 86  ASN C N   1 
ATOM   2102 C CA  . ASN C 1 87 ? 9.798   -18.245 17.039  1.00 54.33  ? 86  ASN C CA  1 
ATOM   2103 C C   . ASN C 1 87 ? 9.088   -18.632 18.347  1.00 54.04  ? 86  ASN C C   1 
ATOM   2104 O O   . ASN C 1 87 ? 8.035   -18.075 18.641  1.00 50.82  ? 86  ASN C O   1 
ATOM   2105 C CB  . ASN C 1 87 ? 8.861   -18.508 15.860  1.00 44.72  ? 86  ASN C CB  1 
ATOM   2106 C CG  . ASN C 1 87 ? 9.460   -17.948 14.592  1.00 48.82  ? 86  ASN C CG  1 
ATOM   2107 O OD1 . ASN C 1 87 ? 9.646   -16.732 14.507  1.00 47.32  ? 86  ASN C OD1 1 
ATOM   2108 N ND2 . ASN C 1 87 ? 9.829   -18.788 13.632  1.00 39.18  ? 86  ASN C ND2 1 
ATOM   2109 N N   . ASN C 1 88 ? 9.581   -19.624 19.103  1.00 50.94  ? 87  ASN C N   1 
ATOM   2110 C CA  . ASN C 1 88 ? 8.852   -20.044 20.304  1.00 46.10  ? 87  ASN C CA  1 
ATOM   2111 C C   . ASN C 1 88 ? 9.743   -20.921 21.183  1.00 45.50  ? 87  ASN C C   1 
ATOM   2112 O O   . ASN C 1 88 ? 9.353   -22.027 21.583  1.00 48.27  ? 87  ASN C O   1 
ATOM   2113 C CB  . ASN C 1 88 ? 7.545   -20.762 19.961  1.00 51.45  ? 87  ASN C CB  1 
ATOM   2114 C CG  . ASN C 1 88 ? 6.540   -20.729 21.091  1.00 56.91  ? 87  ASN C CG  1 
ATOM   2115 O OD1 . ASN C 1 88 ? 6.788   -20.083 22.112  1.00 61.14  ? 87  ASN C OD1 1 
ATOM   2116 N ND2 . ASN C 1 88 ? 5.413   -21.409 20.938  1.00 58.35  ? 87  ASN C ND2 1 
ATOM   2117 N N   . PRO C 1 89 ? 10.977  -20.479 21.507  1.00 42.71  ? 88  PRO C N   1 
ATOM   2118 C CA  . PRO C 1 89 ? 11.953  -21.381 22.098  1.00 44.85  ? 88  PRO C CA  1 
ATOM   2119 C C   . PRO C 1 89 ? 11.706  -21.771 23.547  1.00 52.49  ? 88  PRO C C   1 
ATOM   2120 O O   . PRO C 1 89 ? 12.471  -22.589 24.066  1.00 55.61  ? 88  PRO C O   1 
ATOM   2121 C CB  . PRO C 1 89 ? 13.286  -20.624 21.889  1.00 45.38  ? 88  PRO C CB  1 
ATOM   2122 C CG  . PRO C 1 89 ? 12.885  -19.158 21.988  1.00 43.84  ? 88  PRO C CG  1 
ATOM   2123 C CD  . PRO C 1 89 ? 11.525  -19.135 21.278  1.00 41.09  ? 88  PRO C CD  1 
ATOM   2124 N N   . HIS C 1 90 ? 10.645  -21.222 24.171  1.00 55.45  ? 89  HIS C N   1 
ATOM   2125 C CA  . HIS C 1 90 ? 10.367  -21.528 25.575  1.00 50.57  ? 89  HIS C CA  1 
ATOM   2126 C C   . HIS C 1 90 ? 8.925   -21.982 25.828  1.00 56.90  ? 89  HIS C C   1 
ATOM   2127 O O   . HIS C 1 90 ? 8.458   -21.906 26.960  1.00 63.71  ? 89  HIS C O   1 
ATOM   2128 C CB  . HIS C 1 90 ? 10.932  -20.466 26.524  1.00 44.00  ? 89  HIS C CB  1 
ATOM   2129 C CG  . HIS C 1 90 ? 12.377  -20.101 26.303  1.00 46.66  ? 89  HIS C CG  1 
ATOM   2130 N ND1 . HIS C 1 90 ? 12.793  -18.927 25.692  1.00 49.66  ? 89  HIS C ND1 1 
ATOM   2131 C CD2 . HIS C 1 90 ? 13.510  -20.733 26.660  1.00 44.26  ? 89  HIS C CD2 1 
ATOM   2132 C CE1 . HIS C 1 90 ? 14.129  -18.860 25.667  1.00 42.59  ? 89  HIS C CE1 1 
ATOM   2133 N NE2 . HIS C 1 90 ? 14.585  -19.960 26.245  1.00 45.53  ? 89  HIS C NE2 1 
ATOM   2134 N N   . ALA C 1 91 ? 8.235   -22.509 24.803  1.00 62.30  ? 90  ALA C N   1 
ATOM   2135 C CA  . ALA C 1 91 ? 6.944   -23.172 24.989  1.00 68.61  ? 90  ALA C CA  1 
ATOM   2136 C C   . ALA C 1 91 ? 7.117   -24.518 25.702  1.00 81.01  ? 90  ALA C C   1 
ATOM   2137 O O   . ALA C 1 91 ? 8.222   -24.858 26.122  1.00 84.24  ? 90  ALA C O   1 
ATOM   2138 C CB  . ALA C 1 91 ? 6.202   -23.295 23.667  1.00 65.40  ? 90  ALA C CB  1 
ATOM   2139 N N   . SER C 1 92 ? 6.020   -25.287 25.826  1.00 92.09  ? 91  SER C N   1 
ATOM   2140 C CA  . SER C 1 92 ? 5.951   -26.441 26.717  1.00 93.20  ? 91  SER C CA  1 
ATOM   2141 C C   . SER C 1 92 ? 6.048   -27.776 25.977  1.00 83.04  ? 91  SER C C   1 
ATOM   2142 O O   . SER C 1 92 ? 6.680   -28.702 26.478  1.00 73.83  ? 91  SER C O   1 
ATOM   2143 C CB  . SER C 1 92 ? 4.709   -26.401 27.588  1.00 92.59  ? 91  SER C CB  1 
ATOM   2144 O OG  . SER C 1 92 ? 4.901   -25.544 28.704  1.00 90.84  ? 91  SER C OG  1 
ATOM   2145 N N   . TYR C 1 93 ? 5.355   -27.875 24.834  1.00 81.97  ? 92  TYR C N   1 
ATOM   2146 C CA  . TYR C 1 93 ? 5.217   -29.090 24.038  1.00 85.06  ? 92  TYR C CA  1 
ATOM   2147 C C   . TYR C 1 93 ? 5.062   -30.328 24.957  1.00 94.45  ? 92  TYR C C   1 
ATOM   2148 O O   . TYR C 1 93 ? 3.930   -30.716 25.374  1.00 93.04  ? 92  TYR C O   1 
ATOM   2149 C CB  . TYR C 1 93 ? 6.357   -29.209 23.016  1.00 84.77  ? 92  TYR C CB  1 
ATOM   2150 C CG  . TYR C 1 93 ? 6.749   -27.922 22.290  1.00 73.92  ? 92  TYR C CG  1 
ATOM   2151 C CD1 . TYR C 1 93 ? 6.083   -27.505 21.135  1.00 66.91  ? 92  TYR C CD1 1 
ATOM   2152 C CD2 . TYR C 1 93 ? 7.786   -27.119 22.762  1.00 65.74  ? 92  TYR C CD2 1 
ATOM   2153 C CE1 . TYR C 1 93 ? 6.420   -26.327 20.483  1.00 61.99  ? 92  TYR C CE1 1 
ATOM   2154 C CE2 . TYR C 1 93 ? 8.150   -25.954 22.102  1.00 54.87  ? 92  TYR C CE2 1 
ATOM   2155 C CZ  . TYR C 1 93 ? 7.470   -25.558 20.962  1.00 63.41  ? 92  TYR C CZ  1 
ATOM   2156 O OH  . TYR C 1 93 ? 7.839   -24.392 20.341  1.00 67.10  ? 92  TYR C OH  1 
HETATM 2157 S S   . SO4 D 2 .  ? 0.934   -33.888 1.693   1.00 88.58  ? 101 SO4 A S   1 
HETATM 2158 O O1  . SO4 D 2 .  ? 1.367   -34.531 0.470   1.00 71.30  ? 101 SO4 A O1  1 
HETATM 2159 O O2  . SO4 D 2 .  ? 1.084   -32.462 1.561   1.00 88.40  ? 101 SO4 A O2  1 
HETATM 2160 O O3  . SO4 D 2 .  ? -0.451  -34.197 1.960   1.00 100.51 ? 101 SO4 A O3  1 
HETATM 2161 O O4  . SO4 D 2 .  ? 1.731   -34.343 2.793   1.00 79.86  ? 101 SO4 A O4  1 
HETATM 2162 S S   . SO4 E 2 .  ? -9.813  -24.620 1.420   1.00 90.35  ? 102 SO4 A S   1 
HETATM 2163 O O1  . SO4 E 2 .  ? -9.748  -24.219 0.038   1.00 82.16  ? 102 SO4 A O1  1 
HETATM 2164 O O2  . SO4 E 2 .  ? -9.276  -23.579 2.257   1.00 79.26  ? 102 SO4 A O2  1 
HETATM 2165 O O3  . SO4 E 2 .  ? -11.185 -24.879 1.779   1.00 111.10 ? 102 SO4 A O3  1 
HETATM 2166 O O4  . SO4 E 2 .  ? -9.047  -25.822 1.621   1.00 102.43 ? 102 SO4 A O4  1 
HETATM 2167 C C1  . EDO F 3 .  ? 13.691  -19.535 -7.379  1.00 46.69  ? 103 EDO A C1  1 
HETATM 2168 O O1  . EDO F 3 .  ? 14.941  -18.843 -7.205  1.00 41.91  ? 103 EDO A O1  1 
HETATM 2169 C C2  . EDO F 3 .  ? 12.898  -19.105 -8.582  1.00 41.15  ? 103 EDO A C2  1 
HETATM 2170 O O2  . EDO F 3 .  ? 12.472  -17.777 -8.491  1.00 37.97  ? 103 EDO A O2  1 
HETATM 2171 N N1  . LPU G 4 .  ? 1.271   -25.461 -4.272  0.88 56.78  ? 104 LPU A N1  1 
HETATM 2172 C C4  . LPU G 4 .  ? 0.291   -25.339 -6.930  0.88 52.93  ? 104 LPU A C4  1 
HETATM 2173 C C5  . LPU G 4 .  ? -0.172  -26.450 -6.014  0.88 48.67  ? 104 LPU A C5  1 
HETATM 2174 C C6  . LPU G 4 .  ? 0.848   -26.726 -4.903  0.88 58.63  ? 104 LPU A C6  1 
HETATM 2175 C C1  . LPU G 4 .  ? 0.852   -24.432 -1.782  0.88 51.15  ? 104 LPU A C1  1 
HETATM 2176 S S1  . LPU G 4 .  ? 1.847   -25.521 -2.731  0.88 56.45  ? 104 LPU A S1  1 
HETATM 2177 O O1  . LPU G 4 .  ? 3.185   -25.017 -2.765  0.88 43.37  ? 104 LPU A O1  1 
HETATM 2178 O O2  . LPU G 4 .  ? 1.632   -26.852 -2.249  0.88 52.46  ? 104 LPU A O2  1 
HETATM 2179 C C2  . LPU G 4 .  ? 1.945   -24.552 -5.222  0.88 56.65  ? 104 LPU A C2  1 
HETATM 2180 C C3  . LPU G 4 .  ? 1.747   -24.994 -6.667  0.88 45.04  ? 104 LPU A C3  1 
HETATM 2181 O O3  . LPU G 4 .  ? 0.013   -25.663 -8.318  0.88 50.67  ? 104 LPU A O3  1 
HETATM 2182 S S   . SO4 H 2 .  ? 8.595   -29.470 5.800   1.00 64.19  ? 105 SO4 A S   1 
HETATM 2183 O O1  . SO4 H 2 .  ? 9.468   -28.793 4.909   1.00 57.80  ? 105 SO4 A O1  1 
HETATM 2184 O O2  . SO4 H 2 .  ? 8.113   -30.675 5.163   1.00 74.88  ? 105 SO4 A O2  1 
HETATM 2185 O O3  . SO4 H 2 .  ? 9.322   -29.776 7.013   1.00 64.62  ? 105 SO4 A O3  1 
HETATM 2186 O O4  . SO4 H 2 .  ? 7.455   -28.626 6.093   1.00 88.45  ? 105 SO4 A O4  1 
HETATM 2187 S S   . SO4 I 2 .  ? 7.336   -8.559  -24.723 1.00 83.04  ? 101 SO4 B S   1 
HETATM 2188 O O1  . SO4 I 2 .  ? 8.364   -8.811  -25.718 1.00 54.10  ? 101 SO4 B O1  1 
HETATM 2189 O O2  . SO4 I 2 .  ? 6.047   -8.920  -25.259 1.00 60.68  ? 101 SO4 B O2  1 
HETATM 2190 O O3  . SO4 I 2 .  ? 7.531   -9.353  -23.507 1.00 54.73  ? 101 SO4 B O3  1 
HETATM 2191 O O4  . SO4 I 2 .  ? 7.398   -7.148  -24.405 1.00 66.98  ? 101 SO4 B O4  1 
HETATM 2192 S S   . SO4 J 2 .  ? 14.232  -27.056 -26.530 1.00 63.33  ? 102 SO4 B S   1 
HETATM 2193 O O1  . SO4 J 2 .  ? 15.346  -26.563 -25.777 1.00 58.27  ? 102 SO4 B O1  1 
HETATM 2194 O O2  . SO4 J 2 .  ? 14.645  -28.215 -27.289 1.00 76.69  ? 102 SO4 B O2  1 
HETATM 2195 O O3  . SO4 J 2 .  ? 13.173  -27.431 -25.632 1.00 76.63  ? 102 SO4 B O3  1 
HETATM 2196 O O4  . SO4 J 2 .  ? 13.740  -26.041 -27.427 1.00 55.96  ? 102 SO4 B O4  1 
HETATM 2197 N N1  . LPU K 4 .  ? 18.283  -15.216 -23.673 0.92 36.43  ? 103 LPU B N1  1 
HETATM 2198 C C4  . LPU K 4 .  ? 20.422  -16.855 -22.644 0.92 39.25  ? 103 LPU B C4  1 
HETATM 2199 C C5  . LPU K 4 .  ? 19.308  -16.329 -21.769 0.92 37.03  ? 103 LPU B C5  1 
HETATM 2200 C C6  . LPU K 4 .  ? 18.042  -16.184 -22.588 0.92 37.80  ? 103 LPU B C6  1 
HETATM 2201 C C1  . LPU K 4 .  ? 16.298  -15.919 -25.368 0.92 44.31  ? 103 LPU B C1  1 
HETATM 2202 S S1  . LPU K 4 .  ? 16.944  -14.642 -24.357 0.92 38.56  ? 103 LPU B S1  1 
HETATM 2203 O O1  . LPU K 4 .  ? 17.342  -13.554 -25.193 0.92 44.22  ? 103 LPU B O1  1 
HETATM 2204 O O2  . LPU K 4 .  ? 16.004  -14.404 -23.311 0.92 41.14  ? 103 LPU B O2  1 
HETATM 2205 C C2  . LPU K 4 .  ? 19.344  -15.657 -24.607 0.92 37.48  ? 103 LPU B C2  1 
HETATM 2206 C C3  . LPU K 4 .  ? 20.657  -15.956 -23.853 0.92 40.72  ? 103 LPU B C3  1 
HETATM 2207 O O3  . LPU K 4 .  ? 21.607  -16.861 -21.874 0.92 49.36  ? 103 LPU B O3  1 
HETATM 2208 S S   . SO4 L 2 .  ? 29.078  -38.307 12.457  1.00 115.19 ? 101 SO4 C S   1 
HETATM 2209 O O1  . SO4 L 2 .  ? 30.402  -37.937 12.025  1.00 121.72 ? 101 SO4 C O1  1 
HETATM 2210 O O2  . SO4 L 2 .  ? 28.136  -37.329 11.978  1.00 127.81 ? 101 SO4 C O2  1 
HETATM 2211 O O3  . SO4 L 2 .  ? 28.732  -39.602 11.934  1.00 92.67  ? 101 SO4 C O3  1 
HETATM 2212 O O4  . SO4 L 2 .  ? 29.043  -38.347 13.894  1.00 125.05 ? 101 SO4 C O4  1 
HETATM 2213 N N1  . LPU M 4 .  ? 16.488  -37.416 18.441  0.66 43.80  ? 102 LPU C N1  1 
HETATM 2214 C C4  . LPU M 4 .  ? 16.938  -39.300 20.488  0.66 43.44  ? 102 LPU C C4  1 
HETATM 2215 C C5  . LPU M 4 .  ? 16.790  -39.806 19.069  0.66 45.65  ? 102 LPU C C5  1 
HETATM 2216 C C6  . LPU M 4 .  ? 16.036  -38.799 18.190  0.66 44.63  ? 102 LPU C C6  1 
HETATM 2217 C C1  . LPU M 4 .  ? 17.459  -35.367 16.944  0.66 42.16  ? 102 LPU C C1  1 
HETATM 2218 S S1  . LPU M 4 .  ? 16.030  -36.278 17.373  0.66 39.32  ? 102 LPU C S1  1 
HETATM 2219 O O1  . LPU M 4 .  ? 15.144  -35.414 18.080  0.66 28.51  ? 102 LPU C O1  1 
HETATM 2220 O O2  . LPU M 4 .  ? 15.576  -36.954 16.199  0.66 38.29  ? 102 LPU C O2  1 
HETATM 2221 C C2  . LPU M 4 .  ? 16.331  -36.997 19.849  0.66 43.87  ? 102 LPU C C2  1 
HETATM 2222 C C3  . LPU M 4 .  ? 15.986  -38.163 20.738  0.66 43.84  ? 102 LPU C C3  1 
HETATM 2223 O O3  . LPU M 4 .  ? 16.646  -40.318 21.426  0.66 43.04  ? 102 LPU C O3  1 
HETATM 2224 O O   . HOH N 5 .  ? -5.698  -13.242 -16.410 1.00 51.68  ? 201 HOH A O   1 
HETATM 2225 O O   . HOH N 5 .  ? 8.076   -32.501 4.172   1.00 65.25  ? 202 HOH A O   1 
HETATM 2226 O O   . HOH N 5 .  ? 10.431  -19.114 10.187  1.00 58.61  ? 203 HOH A O   1 
HETATM 2227 O O   . HOH N 5 .  ? 0.971   2.907   3.806   1.00 60.30  ? 204 HOH A O   1 
HETATM 2228 O O   . HOH N 5 .  ? 3.715   -34.311 3.763   1.00 63.45  ? 205 HOH A O   1 
HETATM 2229 O O   . HOH N 5 .  ? 10.698  -29.545 3.108   1.00 41.66  ? 206 HOH A O   1 
HETATM 2230 O O   . HOH N 5 .  ? 5.160   -29.417 6.774   1.00 51.76  ? 207 HOH A O   1 
HETATM 2231 O O   . HOH N 5 .  ? 10.675  -9.535  -13.078 1.00 71.55  ? 208 HOH A O   1 
HETATM 2232 O O   . HOH N 5 .  ? 1.098   -24.624 13.676  1.00 72.18  ? 209 HOH A O   1 
HETATM 2233 O O   . HOH N 5 .  ? -7.717  -21.331 -5.214  1.00 78.16  ? 210 HOH A O   1 
HETATM 2234 O O   . HOH N 5 .  ? 13.711  -15.729 -9.201  1.00 38.48  ? 211 HOH A O   1 
HETATM 2235 O O   . HOH N 5 .  ? -0.870  -29.157 9.748   1.00 57.82  ? 212 HOH A O   1 
HETATM 2236 O O   . HOH N 5 .  ? 11.232  -12.196 5.874   1.00 44.55  ? 213 HOH A O   1 
HETATM 2237 O O   . HOH N 5 .  ? 6.928   -10.697 -12.124 1.00 40.49  ? 214 HOH A O   1 
HETATM 2238 O O   . HOH N 5 .  ? 0.693   -10.653 -15.663 1.00 52.41  ? 215 HOH A O   1 
HETATM 2239 O O   . HOH N 5 .  ? -7.949  -15.736 -1.130  1.00 39.29  ? 216 HOH A O   1 
HETATM 2240 O O   . HOH N 5 .  ? -5.744  -25.436 -5.593  1.00 55.79  ? 217 HOH A O   1 
HETATM 2241 O O   . HOH N 5 .  ? 8.954   -22.683 -9.487  1.00 39.60  ? 218 HOH A O   1 
HETATM 2242 O O   . HOH N 5 .  ? 12.825  -9.464  -7.376  1.00 46.25  ? 219 HOH A O   1 
HETATM 2243 O O   . HOH N 5 .  ? 15.578  -24.513 1.969   1.00 46.38  ? 220 HOH A O   1 
HETATM 2244 O O   . HOH N 5 .  ? 10.435  -5.270  -7.785  1.00 34.01  ? 221 HOH A O   1 
HETATM 2245 O O   . HOH N 5 .  ? 10.754  -23.739 9.716   1.00 45.89  ? 222 HOH A O   1 
HETATM 2246 O O   . HOH N 5 .  ? -3.341  -30.797 -3.119  1.00 96.19  ? 223 HOH A O   1 
HETATM 2247 O O   . HOH N 5 .  ? -7.899  -17.238 6.565   1.00 50.44  ? 224 HOH A O   1 
HETATM 2248 O O   . HOH N 5 .  ? 19.487  -15.317 7.263   1.00 40.05  ? 225 HOH A O   1 
HETATM 2249 O O   . HOH N 5 .  ? 1.734   -4.893  -10.512 1.00 53.10  ? 226 HOH A O   1 
HETATM 2250 O O   . HOH N 5 .  ? -9.366  -15.618 10.646  1.00 53.59  ? 227 HOH A O   1 
HETATM 2251 O O   . HOH N 5 .  ? -2.519  3.255   -1.977  1.00 38.57  ? 228 HOH A O   1 
HETATM 2252 O O   . HOH N 5 .  ? -8.709  -20.929 -0.988  1.00 45.61  ? 229 HOH A O   1 
HETATM 2253 O O   . HOH N 5 .  ? 8.299   -17.658 -15.779 1.00 52.59  ? 230 HOH A O   1 
HETATM 2254 O O   . HOH N 5 .  ? -0.708  -20.809 7.097   1.00 36.62  ? 231 HOH A O   1 
HETATM 2255 O O   . HOH N 5 .  ? 9.300   -30.497 9.594   1.00 37.46  ? 232 HOH A O   1 
HETATM 2256 O O   . HOH N 5 .  ? -4.771  -21.272 6.179   1.00 46.07  ? 233 HOH A O   1 
HETATM 2257 O O   . HOH N 5 .  ? 7.875   -8.386  4.351   1.00 49.53  ? 234 HOH A O   1 
HETATM 2258 O O   . HOH N 5 .  ? -5.871  -15.712 -7.992  1.00 34.49  ? 235 HOH A O   1 
HETATM 2259 O O   . HOH N 5 .  ? -6.252  -11.265 -11.276 1.00 44.39  ? 236 HOH A O   1 
HETATM 2260 O O   . HOH N 5 .  ? -8.205  -16.639 2.284   1.00 48.78  ? 237 HOH A O   1 
HETATM 2261 O O   . HOH N 5 .  ? -10.791 -27.883 1.638   1.00 74.87  ? 238 HOH A O   1 
HETATM 2262 O O   . HOH N 5 .  ? 1.724   0.700   -7.317  1.00 54.31  ? 239 HOH A O   1 
HETATM 2263 O O   . HOH N 5 .  ? 4.270   -3.441  -3.264  1.00 39.09  ? 240 HOH A O   1 
HETATM 2264 O O   . HOH N 5 .  ? 6.045   -6.109  0.095   1.00 98.97  ? 241 HOH A O   1 
HETATM 2265 O O   . HOH N 5 .  ? 9.853   -13.050 9.775   1.00 50.86  ? 242 HOH A O   1 
HETATM 2266 O O   . HOH N 5 .  ? 17.064  -12.895 1.446   1.00 24.37  ? 243 HOH A O   1 
HETATM 2267 O O   . HOH N 5 .  ? -2.070  -21.898 -0.721  1.00 32.14  ? 244 HOH A O   1 
HETATM 2268 O O   . HOH N 5 .  ? 11.394  -16.569 -14.904 1.00 52.18  ? 245 HOH A O   1 
HETATM 2269 O O   . HOH N 5 .  ? -5.679  -19.301 -5.772  1.00 57.49  ? 246 HOH A O   1 
HETATM 2270 O O   . HOH N 5 .  ? 1.808   -10.386 11.582  1.00 51.53  ? 247 HOH A O   1 
HETATM 2271 O O   . HOH N 5 .  ? 13.064  -11.993 -4.253  1.00 27.11  ? 248 HOH A O   1 
HETATM 2272 O O   . HOH N 5 .  ? -3.687  -10.655 6.925   1.00 55.42  ? 249 HOH A O   1 
HETATM 2273 O O   . HOH N 5 .  ? 2.172   -25.232 -10.124 1.00 43.17  ? 250 HOH A O   1 
HETATM 2274 O O   . HOH N 5 .  ? 8.715   -18.143 -11.059 1.00 39.62  ? 251 HOH A O   1 
HETATM 2275 O O   . HOH N 5 .  ? 2.813   -29.622 -0.449  1.00 44.58  ? 252 HOH A O   1 
HETATM 2276 O O   . HOH N 5 .  ? -2.661  -11.638 13.938  1.00 48.35  ? 253 HOH A O   1 
HETATM 2277 O O   . HOH N 5 .  ? 14.020  -29.675 3.952   1.00 52.73  ? 254 HOH A O   1 
HETATM 2278 O O   . HOH N 5 .  ? -1.240  -11.793 11.368  1.00 43.30  ? 255 HOH A O   1 
HETATM 2279 O O   . HOH N 5 .  ? 4.192   -7.843  0.793   1.00 37.00  ? 256 HOH A O   1 
HETATM 2280 O O   . HOH N 5 .  ? 11.305  -12.529 -6.131  1.00 31.46  ? 257 HOH A O   1 
HETATM 2281 O O   . HOH N 5 .  ? 8.359   -17.931 9.121   1.00 49.54  ? 258 HOH A O   1 
HETATM 2282 O O   . HOH N 5 .  ? 9.588   -6.057  -1.601  1.00 43.06  ? 259 HOH A O   1 
HETATM 2283 O O   . HOH N 5 .  ? -0.167  -33.701 4.829   1.00 57.13  ? 260 HOH A O   1 
HETATM 2284 O O   . HOH N 5 .  ? -1.665  -7.472  11.462  1.00 54.18  ? 261 HOH A O   1 
HETATM 2285 O O   . HOH N 5 .  ? 11.055  -6.018  -3.971  1.00 49.43  ? 262 HOH A O   1 
HETATM 2286 O O   . HOH N 5 .  ? -6.293  -12.759 6.790   1.00 44.99  ? 263 HOH A O   1 
HETATM 2287 O O   . HOH N 5 .  ? 0.802   -17.807 -19.155 1.00 54.73  ? 264 HOH A O   1 
HETATM 2288 O O   . HOH N 5 .  ? 2.583   -6.285  5.442   1.00 50.26  ? 265 HOH A O   1 
HETATM 2289 O O   . HOH N 5 .  ? 0.019   -23.441 9.149   1.00 47.42  ? 266 HOH A O   1 
HETATM 2290 O O   . HOH N 5 .  ? 2.787   -10.046 -13.207 1.00 64.45  ? 267 HOH A O   1 
HETATM 2291 O O   . HOH N 5 .  ? -0.349  -21.277 10.610  1.00 78.76  ? 268 HOH A O   1 
HETATM 2292 O O   . HOH N 5 .  ? 7.667   -7.754  1.096   1.00 41.63  ? 269 HOH A O   1 
HETATM 2293 O O   . HOH N 5 .  ? 10.897  -7.974  0.330   1.00 30.88  ? 270 HOH A O   1 
HETATM 2294 O O   . HOH N 5 .  ? 16.826  -12.395 -17.164 1.00 53.09  ? 271 HOH A O   1 
HETATM 2295 O O   . HOH N 5 .  ? 12.442  -13.516 -8.567  1.00 40.59  ? 272 HOH A O   1 
HETATM 2296 O O   . HOH N 5 .  ? 16.837  -18.168 -9.633  1.00 50.98  ? 273 HOH A O   1 
HETATM 2297 O O   . HOH N 5 .  ? 9.496   -20.350 -18.458 1.00 45.35  ? 274 HOH A O   1 
HETATM 2298 O O   . HOH N 5 .  ? 15.589  -11.844 -5.506  1.00 43.86  ? 275 HOH A O   1 
HETATM 2299 O O   . HOH N 5 .  ? 5.014   -7.579  3.900   1.00 46.64  ? 276 HOH A O   1 
HETATM 2300 O O   . HOH N 5 .  ? 6.226   -16.496 -14.742 1.00 66.42  ? 277 HOH A O   1 
HETATM 2301 O O   . HOH N 5 .  ? 12.650  -28.614 -4.614  1.00 55.43  ? 278 HOH A O   1 
HETATM 2302 O O   . HOH N 5 .  ? 8.592   -16.495 -13.116 1.00 42.07  ? 279 HOH A O   1 
HETATM 2303 O O   . HOH N 5 .  ? -0.581  -31.629 -3.268  1.00 56.21  ? 280 HOH A O   1 
HETATM 2304 O O   . HOH N 5 .  ? 4.294   6.226   -4.840  1.00 76.25  ? 281 HOH A O   1 
HETATM 2305 O O   . HOH N 5 .  ? 2.198   -29.162 -4.389  1.00 62.91  ? 282 HOH A O   1 
HETATM 2306 O O   . HOH N 5 .  ? 22.063  -16.666 -0.467  1.00 45.14  ? 283 HOH A O   1 
HETATM 2307 O O   . HOH N 5 .  ? -11.383 -16.363 -3.868  1.00 60.56  ? 284 HOH A O   1 
HETATM 2308 O O   . HOH N 5 .  ? 14.368  -13.353 10.579  1.00 55.09  ? 285 HOH A O   1 
HETATM 2309 O O   . HOH N 5 .  ? -7.386  -11.207 -8.027  1.00 37.87  ? 286 HOH A O   1 
HETATM 2310 O O   . HOH N 5 .  ? 21.292  -16.772 -3.500  1.00 35.58  ? 287 HOH A O   1 
HETATM 2311 O O   . HOH N 5 .  ? 13.389  -15.090 -12.180 1.00 64.28  ? 288 HOH A O   1 
HETATM 2312 O O   . HOH N 5 .  ? -2.957  -21.109 6.852   1.00 59.64  ? 289 HOH A O   1 
HETATM 2313 O O   . HOH N 5 .  ? 1.721   -29.848 -7.166  1.00 51.98  ? 290 HOH A O   1 
HETATM 2314 O O   . HOH N 5 .  ? -3.672  -7.905  10.547  1.00 55.14  ? 291 HOH A O   1 
HETATM 2315 O O   . HOH N 5 .  ? -7.195  -13.972 -9.055  1.00 46.74  ? 292 HOH A O   1 
HETATM 2316 O O   . HOH N 5 .  ? 16.669  -13.724 10.931  1.00 55.68  ? 293 HOH A O   1 
HETATM 2317 O O   . HOH N 5 .  ? 12.412  -12.367 11.864  1.00 57.73  ? 294 HOH A O   1 
HETATM 2318 O O   . HOH N 5 .  ? 14.971  -28.229 -1.229  1.00 62.59  ? 295 HOH A O   1 
HETATM 2319 O O   . HOH N 5 .  ? -6.154  -26.517 3.406   1.00 48.66  ? 296 HOH A O   1 
HETATM 2320 O O   . HOH N 5 .  ? 6.727   -1.473  -0.535  1.00 90.88  ? 297 HOH A O   1 
HETATM 2321 O O   . HOH N 5 .  ? -3.811  -10.914 9.865   1.00 55.67  ? 298 HOH A O   1 
HETATM 2322 O O   . HOH N 5 .  ? 8.653   -9.199  -13.703 1.00 40.32  ? 299 HOH A O   1 
HETATM 2323 O O   . HOH N 5 .  ? -8.501  -19.604 -3.296  1.00 44.72  ? 300 HOH A O   1 
HETATM 2324 O O   . HOH N 5 .  ? 10.682  -1.668  -1.870  1.00 70.40  ? 301 HOH A O   1 
HETATM 2325 O O   . HOH N 5 .  ? -4.469  -26.970 6.639   1.00 62.11  ? 302 HOH A O   1 
HETATM 2326 O O   . HOH N 5 .  ? 4.337   -27.055 -9.899  1.00 45.85  ? 303 HOH A O   1 
HETATM 2327 O O   . HOH N 5 .  ? 11.096  -27.803 -7.310  1.00 64.43  ? 304 HOH A O   1 
HETATM 2328 O O   . HOH N 5 .  ? 4.397   -30.878 -2.685  1.00 51.62  ? 305 HOH A O   1 
HETATM 2329 O O   . HOH N 5 .  ? -10.587 -28.043 -1.552  1.00 65.28  ? 306 HOH A O   1 
HETATM 2330 O O   . HOH N 5 .  ? -6.107  -23.171 -7.233  1.00 54.27  ? 307 HOH A O   1 
HETATM 2331 O O   . HOH N 5 .  ? -7.289  -19.417 8.032   1.00 53.78  ? 308 HOH A O   1 
HETATM 2332 O O   . HOH N 5 .  ? -11.348 -12.964 -2.499  1.00 97.58  ? 309 HOH A O   1 
HETATM 2333 O O   . HOH N 5 .  ? -6.568  -22.888 5.727   1.00 53.12  ? 310 HOH A O   1 
HETATM 2334 O O   . HOH N 5 .  ? 7.193   -30.711 -2.291  1.00 55.75  ? 311 HOH A O   1 
HETATM 2335 O O   . HOH N 5 .  ? 4.471   -9.724  -11.740 1.00 60.85  ? 312 HOH A O   1 
HETATM 2336 O O   . HOH N 5 .  ? -5.342  -20.740 -8.638  1.00 77.16  ? 313 HOH A O   1 
HETATM 2337 O O   . HOH N 5 .  ? 8.765   -22.547 -19.213 1.00 55.74  ? 314 HOH A O   1 
HETATM 2338 O O   . HOH N 5 .  ? -9.393  -10.441 -13.158 1.00 61.54  ? 315 HOH A O   1 
HETATM 2339 O O   . HOH N 5 .  ? 4.352   -2.245  2.637   1.00 86.80  ? 316 HOH A O   1 
HETATM 2340 O O   . HOH N 5 .  ? -5.483  -20.331 18.335  1.00 71.89  ? 317 HOH A O   1 
HETATM 2341 O O   . HOH O 5 .  ? 35.310  -15.915 -26.132 1.00 65.00  ? 201 HOH B O   1 
HETATM 2342 O O   . HOH O 5 .  ? 30.923  -8.265  -29.577 1.00 60.20  ? 202 HOH B O   1 
HETATM 2343 O O   . HOH O 5 .  ? 25.816  -4.811  -33.449 1.00 50.30  ? 203 HOH B O   1 
HETATM 2344 O O   . HOH O 5 .  ? 12.573  -25.675 -36.949 1.00 50.10  ? 204 HOH B O   1 
HETATM 2345 O O   . HOH O 5 .  ? 27.456  -8.053  -28.777 1.00 43.31  ? 205 HOH B O   1 
HETATM 2346 O O   . HOH O 5 .  ? 23.898  -1.687  -35.679 1.00 64.16  ? 206 HOH B O   1 
HETATM 2347 O O   . HOH O 5 .  ? 10.102  -19.343 -43.147 1.00 71.92  ? 207 HOH B O   1 
HETATM 2348 O O   . HOH O 5 .  ? 27.555  -17.655 -25.215 1.00 54.38  ? 208 HOH B O   1 
HETATM 2349 O O   . HOH O 5 .  ? 6.461   -12.374 -25.838 1.00 38.97  ? 209 HOH B O   1 
HETATM 2350 O O   . HOH O 5 .  ? 1.642   -16.288 -32.478 1.00 64.32  ? 210 HOH B O   1 
HETATM 2351 O O   . HOH O 5 .  ? 6.300   -7.159  -32.083 1.00 66.49  ? 211 HOH B O   1 
HETATM 2352 O O   . HOH O 5 .  ? 24.665  -5.132  -29.688 1.00 51.76  ? 212 HOH B O   1 
HETATM 2353 O O   . HOH O 5 .  ? 20.268  -22.340 -23.381 1.00 60.58  ? 213 HOH B O   1 
HETATM 2354 O O   . HOH O 5 .  ? 10.252  -11.558 -38.089 1.00 76.02  ? 214 HOH B O   1 
HETATM 2355 O O   . HOH O 5 .  ? 23.163  -2.273  -28.962 1.00 44.55  ? 215 HOH B O   1 
HETATM 2356 O O   . HOH O 5 .  ? 8.647   -8.871  -16.341 1.00 40.71  ? 216 HOH B O   1 
HETATM 2357 O O   . HOH O 5 .  ? 26.033  -23.015 -30.965 1.00 36.92  ? 217 HOH B O   1 
HETATM 2358 O O   . HOH O 5 .  ? 25.164  -6.041  -35.790 1.00 52.46  ? 218 HOH B O   1 
HETATM 2359 O O   . HOH O 5 .  ? 12.871  -4.435  -41.514 1.00 58.49  ? 219 HOH B O   1 
HETATM 2360 O O   . HOH O 5 .  ? 13.300  -22.364 -20.688 1.00 60.56  ? 220 HOH B O   1 
HETATM 2361 O O   . HOH O 5 .  ? 10.473  -18.704 -32.933 1.00 33.56  ? 221 HOH B O   1 
HETATM 2362 O O   . HOH O 5 .  ? 34.898  -23.001 -30.020 1.00 66.32  ? 222 HOH B O   1 
HETATM 2363 O O   . HOH O 5 .  ? 8.192   -27.644 -38.302 1.00 53.77  ? 223 HOH B O   1 
HETATM 2364 O O   . HOH O 5 .  ? 10.753  -16.218 -44.049 1.00 73.57  ? 224 HOH B O   1 
HETATM 2365 O O   . HOH O 5 .  ? 11.233  1.416   -38.805 1.00 46.90  ? 225 HOH B O   1 
HETATM 2366 O O   . HOH O 5 .  ? 30.834  -12.540 -46.201 1.00 63.44  ? 226 HOH B O   1 
HETATM 2367 O O   . HOH O 5 .  ? 21.728  -26.971 -30.261 1.00 69.98  ? 227 HOH B O   1 
HETATM 2368 O O   . HOH O 5 .  ? 23.521  -4.215  -36.648 1.00 33.58  ? 228 HOH B O   1 
HETATM 2369 O O   . HOH O 5 .  ? 7.645   -12.803 -38.616 1.00 73.78  ? 229 HOH B O   1 
HETATM 2370 O O   . HOH O 5 .  ? 17.942  -0.512  -38.122 1.00 34.01  ? 230 HOH B O   1 
HETATM 2371 O O   . HOH O 5 .  ? 16.646  -19.190 -28.791 1.00 27.45  ? 231 HOH B O   1 
HETATM 2372 O O   . HOH O 5 .  ? 20.542  -9.803  -42.632 1.00 41.92  ? 232 HOH B O   1 
HETATM 2373 O O   . HOH O 5 .  ? 14.170  -6.352  -40.928 1.00 50.65  ? 233 HOH B O   1 
HETATM 2374 O O   . HOH O 5 .  ? 18.303  -3.473  -22.453 1.00 61.12  ? 234 HOH B O   1 
HETATM 2375 O O   . HOH O 5 .  ? 19.849  -25.720 -34.036 1.00 48.51  ? 235 HOH B O   1 
HETATM 2376 O O   . HOH O 5 .  ? 21.197  -13.532 -42.437 1.00 49.03  ? 236 HOH B O   1 
HETATM 2377 O O   . HOH O 5 .  ? 32.511  -18.289 -41.925 1.00 64.31  ? 237 HOH B O   1 
HETATM 2378 O O   . HOH O 5 .  ? 23.413  -11.570 -21.811 1.00 53.12  ? 238 HOH B O   1 
HETATM 2379 O O   . HOH O 5 .  ? 17.539  -19.659 -42.103 1.00 83.62  ? 239 HOH B O   1 
HETATM 2380 O O   . HOH O 5 .  ? 3.056   -8.370  -26.910 1.00 64.85  ? 240 HOH B O   1 
HETATM 2381 O O   . HOH O 5 .  ? 20.864  -3.359  -23.119 1.00 62.27  ? 241 HOH B O   1 
HETATM 2382 O O   . HOH O 5 .  ? 27.025  -10.249 -28.601 1.00 58.48  ? 242 HOH B O   1 
HETATM 2383 O O   . HOH O 5 .  ? 25.898  -0.489  -28.938 1.00 50.20  ? 243 HOH B O   1 
HETATM 2384 O O   . HOH O 5 .  ? 7.306   -18.584 -31.581 1.00 62.98  ? 244 HOH B O   1 
HETATM 2385 O O   . HOH O 5 .  ? 4.992   -19.279 -25.869 1.00 55.80  ? 245 HOH B O   1 
HETATM 2386 O O   . HOH O 5 .  ? 19.607  -8.329  -21.164 1.00 53.62  ? 246 HOH B O   1 
HETATM 2387 O O   . HOH O 5 .  ? 14.182  -24.338 -40.454 1.00 55.31  ? 247 HOH B O   1 
HETATM 2388 O O   . HOH O 5 .  ? 22.501  -23.255 -28.676 1.00 51.80  ? 248 HOH B O   1 
HETATM 2389 O O   . HOH O 5 .  ? 6.601   -20.680 -25.023 1.00 52.64  ? 249 HOH B O   1 
HETATM 2390 O O   . HOH O 5 .  ? 21.647  3.838   -32.501 1.00 45.53  ? 250 HOH B O   1 
HETATM 2391 O O   . HOH O 5 .  ? 17.864  -15.598 -45.678 1.00 45.75  ? 251 HOH B O   1 
HETATM 2392 O O   . HOH O 5 .  ? 21.249  -6.323  -42.396 1.00 53.75  ? 252 HOH B O   1 
HETATM 2393 O O   . HOH O 5 .  ? 7.498   -8.261  -20.707 1.00 49.50  ? 253 HOH B O   1 
HETATM 2394 O O   . HOH O 5 .  ? 25.018  -7.286  -42.332 1.00 56.40  ? 254 HOH B O   1 
HETATM 2395 O O   . HOH O 5 .  ? 10.269  -21.575 -32.830 1.00 45.92  ? 255 HOH B O   1 
HETATM 2396 O O   . HOH O 5 .  ? 7.103   -19.017 -34.761 1.00 65.35  ? 256 HOH B O   1 
HETATM 2397 O O   . HOH O 5 .  ? 18.110  -26.072 -28.906 1.00 54.09  ? 257 HOH B O   1 
HETATM 2398 O O   . HOH O 5 .  ? 31.988  -21.671 -38.030 1.00 54.90  ? 258 HOH B O   1 
HETATM 2399 O O   . HOH O 5 .  ? 1.680   -12.981 -28.215 1.00 64.74  ? 259 HOH B O   1 
HETATM 2400 O O   . HOH O 5 .  ? 18.063  4.587   -34.254 1.00 47.86  ? 260 HOH B O   1 
HETATM 2401 O O   . HOH O 5 .  ? 16.863  -23.821 -20.742 1.00 80.37  ? 261 HOH B O   1 
HETATM 2402 O O   . HOH O 5 .  ? 39.222  -13.254 -39.301 1.00 74.96  ? 262 HOH B O   1 
HETATM 2403 O O   . HOH O 5 .  ? 17.638  -0.332  -25.237 1.00 56.88  ? 263 HOH B O   1 
HETATM 2404 O O   . HOH O 5 .  ? 16.831  -9.558  -43.788 1.00 60.05  ? 264 HOH B O   1 
HETATM 2405 O O   . HOH O 5 .  ? 28.082  -24.618 -34.904 1.00 40.31  ? 265 HOH B O   1 
HETATM 2406 O O   . HOH O 5 .  ? 31.539  -11.913 -37.997 1.00 52.54  ? 266 HOH B O   1 
HETATM 2407 O O   . HOH O 5 .  ? 12.640  -20.258 -19.778 1.00 47.81  ? 267 HOH B O   1 
HETATM 2408 O O   . HOH O 5 .  ? 6.883   -23.439 -24.061 1.00 58.13  ? 268 HOH B O   1 
HETATM 2409 O O   . HOH O 5 .  ? 14.493  -8.025  -42.846 1.00 58.22  ? 269 HOH B O   1 
HETATM 2410 O O   . HOH O 5 .  ? 17.223  3.472   -31.467 1.00 54.43  ? 270 HOH B O   1 
HETATM 2411 O O   . HOH O 5 .  ? 19.876  4.191   -33.017 1.00 44.76  ? 271 HOH B O   1 
HETATM 2412 O O   . HOH O 5 .  ? 9.518   -6.264  -40.864 1.00 49.56  ? 272 HOH B O   1 
HETATM 2413 O O   . HOH O 5 .  ? 8.195   -21.236 -27.249 1.00 46.80  ? 273 HOH B O   1 
HETATM 2414 O O   . HOH O 5 .  ? 13.111  -5.885  -17.766 1.00 68.84  ? 274 HOH B O   1 
HETATM 2415 O O   . HOH O 5 .  ? 8.806   -13.512 -44.960 1.00 66.53  ? 275 HOH B O   1 
HETATM 2416 O O   . HOH O 5 .  ? 7.256   -9.978  -18.461 1.00 43.44  ? 276 HOH B O   1 
HETATM 2417 O O   . HOH O 5 .  ? 15.285  -22.040 -41.854 1.00 59.59  ? 277 HOH B O   1 
HETATM 2418 O O   . HOH O 5 .  ? 7.416   -21.510 -30.048 1.00 42.57  ? 278 HOH B O   1 
HETATM 2419 O O   . HOH O 5 .  ? 21.919  -29.055 -35.631 1.00 58.36  ? 279 HOH B O   1 
HETATM 2420 O O   . HOH O 5 .  ? 22.807  -23.683 -23.911 1.00 55.81  ? 280 HOH B O   1 
HETATM 2421 O O   . HOH P 5 .  ? 13.480  -27.291 28.808  1.00 57.29  ? 201 HOH C O   1 
HETATM 2422 O O   . HOH P 5 .  ? 19.477  -19.799 30.067  1.00 60.50  ? 202 HOH C O   1 
HETATM 2423 O O   . HOH P 5 .  ? 8.904   -36.685 18.438  1.00 63.50  ? 203 HOH C O   1 
HETATM 2424 O O   . HOH P 5 .  ? 7.122   -31.499 12.213  1.00 62.28  ? 204 HOH C O   1 
HETATM 2425 O O   . HOH P 5 .  ? 13.209  -20.516 11.402  1.00 68.32  ? 205 HOH C O   1 
HETATM 2426 O O   . HOH P 5 .  ? 9.062   -30.087 11.237  1.00 59.69  ? 206 HOH C O   1 
HETATM 2427 O O   . HOH P 5 .  ? 27.357  -15.298 12.767  1.00 48.08  ? 207 HOH C O   1 
HETATM 2428 O O   . HOH P 5 .  ? 19.567  -41.679 12.167  1.00 35.27  ? 208 HOH C O   1 
HETATM 2429 O O   . HOH P 5 .  ? 26.414  -37.627 10.166  1.00 44.64  ? 209 HOH C O   1 
HETATM 2430 O O   . HOH P 5 .  ? 5.587   -26.598 16.740  1.00 58.21  ? 210 HOH C O   1 
HETATM 2431 O O   . HOH P 5 .  ? 26.305  -39.000 12.582  1.00 44.94  ? 211 HOH C O   1 
HETATM 2432 O O   . HOH P 5 .  ? 11.724  -29.682 27.766  1.00 51.29  ? 212 HOH C O   1 
HETATM 2433 O O   . HOH P 5 .  ? 25.082  -31.241 10.765  1.00 45.71  ? 213 HOH C O   1 
HETATM 2434 O O   . HOH P 5 .  ? 25.339  -19.574 6.324   1.00 45.27  ? 214 HOH C O   1 
HETATM 2435 O O   . HOH P 5 .  ? 22.741  -41.272 18.599  1.00 44.27  ? 215 HOH C O   1 
HETATM 2436 O O   . HOH P 5 .  ? 20.837  -40.774 39.605  1.00 75.67  ? 216 HOH C O   1 
HETATM 2437 O O   . HOH P 5 .  ? 33.309  -24.354 31.572  1.00 59.27  ? 217 HOH C O   1 
HETATM 2438 O O   . HOH P 5 .  ? 21.797  -34.244 16.544  1.00 32.21  ? 218 HOH C O   1 
HETATM 2439 O O   . HOH P 5 .  ? 30.434  -35.755 28.511  1.00 52.31  ? 219 HOH C O   1 
HETATM 2440 O O   . HOH P 5 .  ? 17.211  -17.055 14.606  1.00 45.05  ? 220 HOH C O   1 
HETATM 2441 O O   . HOH P 5 .  ? 18.800  -20.113 10.490  1.00 52.65  ? 221 HOH C O   1 
HETATM 2442 O O   . HOH P 5 .  ? 21.998  -28.496 11.002  1.00 41.75  ? 222 HOH C O   1 
HETATM 2443 O O   . HOH P 5 .  ? 20.570  -28.636 8.405   1.00 44.07  ? 223 HOH C O   1 
HETATM 2444 O O   . HOH P 5 .  ? 13.596  -37.241 13.736  1.00 55.46  ? 224 HOH C O   1 
HETATM 2445 O O   . HOH P 5 .  ? 20.394  -39.890 26.347  1.00 54.58  ? 225 HOH C O   1 
HETATM 2446 O O   . HOH P 5 .  ? 12.504  -31.502 8.160   1.00 38.51  ? 226 HOH C O   1 
HETATM 2447 O O   . HOH P 5 .  ? 25.213  -33.829 34.775  1.00 65.19  ? 227 HOH C O   1 
HETATM 2448 O O   . HOH P 5 .  ? 25.759  -17.661 13.854  1.00 50.67  ? 228 HOH C O   1 
HETATM 2449 O O   . HOH P 5 .  ? 31.243  -43.118 15.816  1.00 54.72  ? 229 HOH C O   1 
HETATM 2450 O O   . HOH P 5 .  ? 31.471  -43.218 12.009  1.00 60.81  ? 230 HOH C O   1 
HETATM 2451 O O   . HOH P 5 .  ? 15.656  -17.659 19.252  1.00 50.06  ? 231 HOH C O   1 
HETATM 2452 O O   . HOH P 5 .  ? 27.853  -37.102 16.149  1.00 53.57  ? 232 HOH C O   1 
HETATM 2453 O O   . HOH P 5 .  ? 30.935  -39.756 27.737  1.00 56.88  ? 233 HOH C O   1 
HETATM 2454 O O   . HOH P 5 .  ? 15.315  -21.142 12.317  1.00 45.41  ? 234 HOH C O   1 
HETATM 2455 O O   . HOH P 5 .  ? 30.481  -28.899 12.194  1.00 58.49  ? 235 HOH C O   1 
HETATM 2456 O O   . HOH P 5 .  ? 8.842   -18.994 23.760  1.00 51.93  ? 236 HOH C O   1 
HETATM 2457 O O   . HOH P 5 .  ? 25.025  -17.794 20.972  1.00 59.62  ? 237 HOH C O   1 
HETATM 2458 O O   . HOH P 5 .  ? 27.484  -37.765 24.887  1.00 55.65  ? 238 HOH C O   1 
HETATM 2459 O O   . HOH P 5 .  ? 6.810   -17.727 11.047  1.00 49.77  ? 239 HOH C O   1 
HETATM 2460 O O   . HOH P 5 .  ? 18.752  -26.646 2.901   1.00 54.38  ? 240 HOH C O   1 
HETATM 2461 O O   . HOH P 5 .  ? 30.043  -31.720 15.708  1.00 58.13  ? 241 HOH C O   1 
HETATM 2462 O O   . HOH P 5 .  ? 31.545  -33.701 25.809  1.00 57.37  ? 242 HOH C O   1 
HETATM 2463 O O   . HOH P 5 .  ? 13.194  -39.499 16.886  1.00 59.04  ? 243 HOH C O   1 
HETATM 2464 O O   . HOH P 5 .  ? 17.453  -27.614 36.620  1.00 78.27  ? 244 HOH C O   1 
HETATM 2465 O O   . HOH P 5 .  ? 29.553  -39.973 31.591  1.00 42.44  ? 245 HOH C O   1 
HETATM 2466 O O   . HOH P 5 .  ? 28.084  -24.802 32.465  1.00 73.43  ? 246 HOH C O   1 
HETATM 2467 O O   . HOH P 5 .  ? 14.659  -20.648 29.134  1.00 66.22  ? 247 HOH C O   1 
HETATM 2468 O O   . HOH P 5 .  ? 25.022  -39.694 20.250  1.00 39.12  ? 248 HOH C O   1 
HETATM 2469 O O   . HOH P 5 .  ? 29.955  -32.421 18.369  1.00 59.91  ? 249 HOH C O   1 
HETATM 2470 O O   . HOH P 5 .  ? 2.566   -29.341 14.219  1.00 72.15  ? 250 HOH C O   1 
HETATM 2471 O O   . HOH P 5 .  ? 21.108  -29.424 4.694   1.00 57.54  ? 251 HOH C O   1 
HETATM 2472 O O   . HOH P 5 .  ? 21.869  -18.232 21.710  1.00 67.39  ? 252 HOH C O   1 
HETATM 2473 O O   . HOH P 5 .  ? 19.563  -13.170 13.386  1.00 52.24  ? 253 HOH C O   1 
HETATM 2474 O O   . HOH P 5 .  ? 4.780   -23.677 18.580  1.00 70.90  ? 254 HOH C O   1 
HETATM 2475 O O   . HOH P 5 .  ? 19.187  -18.840 25.306  1.00 54.18  ? 255 HOH C O   1 
HETATM 2476 O O   . HOH P 5 .  ? 14.093  -39.082 9.689   1.00 51.72  ? 256 HOH C O   1 
HETATM 2477 O O   . HOH P 5 .  ? 16.538  -37.722 28.812  1.00 64.83  ? 257 HOH C O   1 
HETATM 2478 O O   . HOH P 5 .  ? 11.486  -21.341 10.656  1.00 58.99  ? 258 HOH C O   1 
HETATM 2479 O O   . HOH P 5 .  ? 25.377  -13.988 11.088  1.00 58.25  ? 259 HOH C O   1 
HETATM 2480 O O   . HOH P 5 .  ? 21.584  -13.498 13.371  1.00 47.83  ? 260 HOH C O   1 
HETATM 2481 O O   . HOH P 5 .  ? 30.048  -33.458 13.801  1.00 64.10  ? 261 HOH C O   1 
HETATM 2482 O O   . HOH P 5 .  ? 31.629  -39.177 30.200  1.00 65.13  ? 262 HOH C O   1 
HETATM 2483 O O   . HOH P 5 .  ? 10.342  -38.289 24.071  1.00 68.73  ? 263 HOH C O   1 
HETATM 2484 O O   . HOH P 5 .  ? 17.455  -16.942 25.054  1.00 68.53  ? 264 HOH C O   1 
HETATM 2485 O O   . HOH P 5 .  ? 33.337  -44.229 15.328  1.00 46.50  ? 265 HOH C O   1 
HETATM 2486 O O   . HOH P 5 .  ? 37.729  -25.673 26.490  1.00 75.06  ? 266 HOH C O   1 
# 
