data_7HH3
# 
_entry.id   7HH3 
# 
_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   7HH3         pdb_00007hh3 10.2210/pdb7hh3/pdb 
WWPDB D_1001407465 ?            ?                   
# 
_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                        7HH3 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn '2-[(2S)-2-methylpiperidin-1-yl]ethan-1-amine'     142.242   1   ? ?    ? ? 
5 water       nat water                                              18.015    273 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                  SO4   
3 1,2-ETHANEDIOL                                 EDO   
4 '2-[(2S)-2-methylpiperidin-1-yl]ethan-1-amine' A1A3X 
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 
A1A3X non-polymer         . '2-[(2S)-2-methylpiperidin-1-yl]ethan-1-amine' ?                 'C8 H18 N2'      142.242 
ALA   'L-peptide linking' y ALANINE                                        ?                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                       ?                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                     ?                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                ?                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                       ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                 'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE                                      ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                        ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                      ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                          ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                     ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                        ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                         ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                     ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                  ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                        ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                         ?                 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                  ?                 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                      ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                     ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                       ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                         ?                 'C5 H11 N O2'    117.146 
# 
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        A1A3X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3X 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 2 SO4   1   104 4   SO4   SO4 A . 
H 2 SO4   1   101 1   SO4   SO4 B . 
I 2 SO4   1   102 3   SO4   SO4 B . 
J 4 A1A3X 1   103 101 A1A3X LIG B . 
K 3 EDO   1   101 101 EDO   EDO C . 
L 2 SO4   1   102 5   SO4   SO4 C . 
M 5 HOH   1   201 202 HOH   HOH A . 
M 5 HOH   2   202 307 HOH   HOH A . 
M 5 HOH   3   203 356 HOH   HOH A . 
M 5 HOH   4   204 26  HOH   HOH A . 
M 5 HOH   5   205 165 HOH   HOH A . 
M 5 HOH   6   206 111 HOH   HOH A . 
M 5 HOH   7   207 41  HOH   HOH A . 
M 5 HOH   8   208 71  HOH   HOH A . 
M 5 HOH   9   209 293 HOH   HOH A . 
M 5 HOH   10  210 289 HOH   HOH A . 
M 5 HOH   11  211 259 HOH   HOH A . 
M 5 HOH   12  212 188 HOH   HOH A . 
M 5 HOH   13  213 179 HOH   HOH A . 
M 5 HOH   14  214 55  HOH   HOH A . 
M 5 HOH   15  215 86  HOH   HOH A . 
M 5 HOH   16  216 93  HOH   HOH A . 
M 5 HOH   17  217 66  HOH   HOH A . 
M 5 HOH   18  218 299 HOH   HOH A . 
M 5 HOH   19  219 139 HOH   HOH A . 
M 5 HOH   20  220 190 HOH   HOH A . 
M 5 HOH   21  221 37  HOH   HOH A . 
M 5 HOH   22  222 349 HOH   HOH A . 
M 5 HOH   23  223 260 HOH   HOH A . 
M 5 HOH   24  224 28  HOH   HOH A . 
M 5 HOH   25  225 167 HOH   HOH A . 
M 5 HOH   26  226 87  HOH   HOH A . 
M 5 HOH   27  227 91  HOH   HOH A . 
M 5 HOH   28  228 38  HOH   HOH A . 
M 5 HOH   29  229 116 HOH   HOH A . 
M 5 HOH   30  230 145 HOH   HOH A . 
M 5 HOH   31  231 60  HOH   HOH A . 
M 5 HOH   32  232 8   HOH   HOH A . 
M 5 HOH   33  233 337 HOH   HOH A . 
M 5 HOH   34  234 12  HOH   HOH A . 
M 5 HOH   35  235 97  HOH   HOH A . 
M 5 HOH   36  236 32  HOH   HOH A . 
M 5 HOH   37  237 27  HOH   HOH A . 
M 5 HOH   38  238 34  HOH   HOH A . 
M 5 HOH   39  239 2   HOH   HOH A . 
M 5 HOH   40  240 109 HOH   HOH A . 
M 5 HOH   41  241 203 HOH   HOH A . 
M 5 HOH   42  242 267 HOH   HOH A . 
M 5 HOH   43  243 290 HOH   HOH A . 
M 5 HOH   44  244 94  HOH   HOH A . 
M 5 HOH   45  245 1   HOH   HOH A . 
M 5 HOH   46  246 7   HOH   HOH A . 
M 5 HOH   47  247 95  HOH   HOH A . 
M 5 HOH   48  248 288 HOH   HOH A . 
M 5 HOH   49  249 366 HOH   HOH A . 
M 5 HOH   50  250 199 HOH   HOH A . 
M 5 HOH   51  251 344 HOH   HOH A . 
M 5 HOH   52  252 143 HOH   HOH A . 
M 5 HOH   53  253 274 HOH   HOH A . 
M 5 HOH   54  254 23  HOH   HOH A . 
M 5 HOH   55  255 355 HOH   HOH A . 
M 5 HOH   56  256 99  HOH   HOH A . 
M 5 HOH   57  257 20  HOH   HOH A . 
M 5 HOH   58  258 300 HOH   HOH A . 
M 5 HOH   59  259 164 HOH   HOH A . 
M 5 HOH   60  260 42  HOH   HOH A . 
M 5 HOH   61  261 364 HOH   HOH A . 
M 5 HOH   62  262 369 HOH   HOH A . 
M 5 HOH   63  263 222 HOH   HOH A . 
M 5 HOH   64  264 78  HOH   HOH A . 
M 5 HOH   65  265 21  HOH   HOH A . 
M 5 HOH   66  266 18  HOH   HOH A . 
M 5 HOH   67  267 58  HOH   HOH A . 
M 5 HOH   68  268 31  HOH   HOH A . 
M 5 HOH   69  269 19  HOH   HOH A . 
M 5 HOH   70  270 362 HOH   HOH A . 
M 5 HOH   71  271 115 HOH   HOH A . 
M 5 HOH   72  272 14  HOH   HOH A . 
M 5 HOH   73  273 301 HOH   HOH A . 
M 5 HOH   74  274 47  HOH   HOH A . 
M 5 HOH   75  275 292 HOH   HOH A . 
M 5 HOH   76  276 208 HOH   HOH A . 
M 5 HOH   77  277 9   HOH   HOH A . 
M 5 HOH   78  278 327 HOH   HOH A . 
M 5 HOH   79  279 218 HOH   HOH A . 
M 5 HOH   80  280 77  HOH   HOH A . 
M 5 HOH   81  281 336 HOH   HOH A . 
M 5 HOH   82  282 211 HOH   HOH A . 
M 5 HOH   83  283 281 HOH   HOH A . 
M 5 HOH   84  284 84  HOH   HOH A . 
M 5 HOH   85  285 16  HOH   HOH A . 
M 5 HOH   86  286 318 HOH   HOH A . 
M 5 HOH   87  287 352 HOH   HOH A . 
M 5 HOH   88  288 152 HOH   HOH A . 
M 5 HOH   89  289 131 HOH   HOH A . 
M 5 HOH   90  290 358 HOH   HOH A . 
M 5 HOH   91  291 113 HOH   HOH A . 
M 5 HOH   92  292 73  HOH   HOH A . 
M 5 HOH   93  293 210 HOH   HOH A . 
M 5 HOH   94  294 64  HOH   HOH A . 
M 5 HOH   95  295 35  HOH   HOH A . 
M 5 HOH   96  296 185 HOH   HOH A . 
M 5 HOH   97  297 22  HOH   HOH A . 
M 5 HOH   98  298 83  HOH   HOH A . 
M 5 HOH   99  299 278 HOH   HOH A . 
M 5 HOH   100 300 343 HOH   HOH A . 
M 5 HOH   101 301 334 HOH   HOH A . 
M 5 HOH   102 302 63  HOH   HOH A . 
M 5 HOH   103 303 108 HOH   HOH A . 
M 5 HOH   104 304 296 HOH   HOH A . 
M 5 HOH   105 305 219 HOH   HOH A . 
M 5 HOH   106 306 357 HOH   HOH A . 
M 5 HOH   107 307 370 HOH   HOH A . 
M 5 HOH   108 308 75  HOH   HOH A . 
M 5 HOH   109 309 57  HOH   HOH A . 
M 5 HOH   110 310 156 HOH   HOH A . 
M 5 HOH   111 311 283 HOH   HOH A . 
M 5 HOH   112 312 365 HOH   HOH A . 
M 5 HOH   113 313 205 HOH   HOH A . 
M 5 HOH   114 314 360 HOH   HOH A . 
M 5 HOH   115 315 125 HOH   HOH A . 
M 5 HOH   116 316 332 HOH   HOH A . 
N 5 HOH   1   201 184 HOH   HOH B . 
N 5 HOH   2   202 247 HOH   HOH B . 
N 5 HOH   3   203 329 HOH   HOH B . 
N 5 HOH   4   204 223 HOH   HOH B . 
N 5 HOH   5   205 258 HOH   HOH B . 
N 5 HOH   6   206 89  HOH   HOH B . 
N 5 HOH   7   207 215 HOH   HOH B . 
N 5 HOH   8   208 54  HOH   HOH B . 
N 5 HOH   9   209 123 HOH   HOH B . 
N 5 HOH   10  210 153 HOH   HOH B . 
N 5 HOH   11  211 69  HOH   HOH B . 
N 5 HOH   12  212 98  HOH   HOH B . 
N 5 HOH   13  213 272 HOH   HOH B . 
N 5 HOH   14  214 249 HOH   HOH B . 
N 5 HOH   15  215 345 HOH   HOH B . 
N 5 HOH   16  216 101 HOH   HOH B . 
N 5 HOH   17  217 331 HOH   HOH B . 
N 5 HOH   18  218 157 HOH   HOH B . 
N 5 HOH   19  219 320 HOH   HOH B . 
N 5 HOH   20  220 168 HOH   HOH B . 
N 5 HOH   21  221 172 HOH   HOH B . 
N 5 HOH   22  222 315 HOH   HOH B . 
N 5 HOH   23  223 361 HOH   HOH B . 
N 5 HOH   24  224 17  HOH   HOH B . 
N 5 HOH   25  225 6   HOH   HOH B . 
N 5 HOH   26  226 25  HOH   HOH B . 
N 5 HOH   27  227 137 HOH   HOH B . 
N 5 HOH   28  228 10  HOH   HOH B . 
N 5 HOH   29  229 119 HOH   HOH B . 
N 5 HOH   30  230 76  HOH   HOH B . 
N 5 HOH   31  231 79  HOH   HOH B . 
N 5 HOH   32  232 342 HOH   HOH B . 
N 5 HOH   33  233 117 HOH   HOH B . 
N 5 HOH   34  234 61  HOH   HOH B . 
N 5 HOH   35  235 5   HOH   HOH B . 
N 5 HOH   36  236 338 HOH   HOH B . 
N 5 HOH   37  237 24  HOH   HOH B . 
N 5 HOH   38  238 371 HOH   HOH B . 
N 5 HOH   39  239 319 HOH   HOH B . 
N 5 HOH   40  240 150 HOH   HOH B . 
N 5 HOH   41  241 169 HOH   HOH B . 
N 5 HOH   42  242 175 HOH   HOH B . 
N 5 HOH   43  243 261 HOH   HOH B . 
N 5 HOH   44  244 13  HOH   HOH B . 
N 5 HOH   45  245 96  HOH   HOH B . 
N 5 HOH   46  246 170 HOH   HOH B . 
N 5 HOH   47  247 120 HOH   HOH B . 
N 5 HOH   48  248 36  HOH   HOH B . 
N 5 HOH   49  249 280 HOH   HOH B . 
N 5 HOH   50  250 46  HOH   HOH B . 
N 5 HOH   51  251 182 HOH   HOH B . 
N 5 HOH   52  252 72  HOH   HOH B . 
N 5 HOH   53  253 217 HOH   HOH B . 
N 5 HOH   54  254 68  HOH   HOH B . 
N 5 HOH   55  255 335 HOH   HOH B . 
N 5 HOH   56  256 74  HOH   HOH B . 
N 5 HOH   57  257 373 HOH   HOH B . 
N 5 HOH   58  258 59  HOH   HOH B . 
N 5 HOH   59  259 372 HOH   HOH B . 
N 5 HOH   60  260 224 HOH   HOH B . 
N 5 HOH   61  261 104 HOH   HOH B . 
N 5 HOH   62  262 197 HOH   HOH B . 
N 5 HOH   63  263 242 HOH   HOH B . 
N 5 HOH   64  264 303 HOH   HOH B . 
N 5 HOH   65  265 177 HOH   HOH B . 
N 5 HOH   66  266 279 HOH   HOH B . 
N 5 HOH   67  267 214 HOH   HOH B . 
N 5 HOH   68  268 44  HOH   HOH B . 
N 5 HOH   69  269 160 HOH   HOH B . 
N 5 HOH   70  270 291 HOH   HOH B . 
N 5 HOH   71  271 163 HOH   HOH B . 
N 5 HOH   72  272 368 HOH   HOH B . 
N 5 HOH   73  273 70  HOH   HOH B . 
N 5 HOH   74  274 322 HOH   HOH B . 
N 5 HOH   75  275 201 HOH   HOH B . 
N 5 HOH   76  276 314 HOH   HOH B . 
N 5 HOH   77  277 354 HOH   HOH B . 
N 5 HOH   78  278 367 HOH   HOH B . 
N 5 HOH   79  279 316 HOH   HOH B . 
N 5 HOH   80  280 350 HOH   HOH B . 
N 5 HOH   81  281 340 HOH   HOH B . 
N 5 HOH   82  282 107 HOH   HOH B . 
N 5 HOH   83  283 312 HOH   HOH B . 
N 5 HOH   84  284 310 HOH   HOH B . 
O 5 HOH   1   201 333 HOH   HOH C . 
O 5 HOH   2   202 323 HOH   HOH C . 
O 5 HOH   3   203 317 HOH   HOH C . 
O 5 HOH   4   204 226 HOH   HOH C . 
O 5 HOH   5   205 325 HOH   HOH C . 
O 5 HOH   6   206 309 HOH   HOH C . 
O 5 HOH   7   207 254 HOH   HOH C . 
O 5 HOH   8   208 347 HOH   HOH C . 
O 5 HOH   9   209 118 HOH   HOH C . 
O 5 HOH   10  210 148 HOH   HOH C . 
O 5 HOH   11  211 142 HOH   HOH C . 
O 5 HOH   12  212 321 HOH   HOH C . 
O 5 HOH   13  213 271 HOH   HOH C . 
O 5 HOH   14  214 173 HOH   HOH C . 
O 5 HOH   15  215 134 HOH   HOH C . 
O 5 HOH   16  216 339 HOH   HOH C . 
O 5 HOH   17  217 353 HOH   HOH C . 
O 5 HOH   18  218 209 HOH   HOH C . 
O 5 HOH   19  219 90  HOH   HOH C . 
O 5 HOH   20  220 45  HOH   HOH C . 
O 5 HOH   21  221 269 HOH   HOH C . 
O 5 HOH   22  222 284 HOH   HOH C . 
O 5 HOH   23  223 189 HOH   HOH C . 
O 5 HOH   24  224 126 HOH   HOH C . 
O 5 HOH   25  225 53  HOH   HOH C . 
O 5 HOH   26  226 82  HOH   HOH C . 
O 5 HOH   27  227 85  HOH   HOH C . 
O 5 HOH   28  228 48  HOH   HOH C . 
O 5 HOH   29  229 4   HOH   HOH C . 
O 5 HOH   30  230 132 HOH   HOH C . 
O 5 HOH   31  231 15  HOH   HOH C . 
O 5 HOH   32  232 287 HOH   HOH C . 
O 5 HOH   33  233 295 HOH   HOH C . 
O 5 HOH   34  234 326 HOH   HOH C . 
O 5 HOH   35  235 305 HOH   HOH C . 
O 5 HOH   36  236 149 HOH   HOH C . 
O 5 HOH   37  237 348 HOH   HOH C . 
O 5 HOH   38  238 49  HOH   HOH C . 
O 5 HOH   39  239 161 HOH   HOH C . 
O 5 HOH   40  240 302 HOH   HOH C . 
O 5 HOH   41  241 130 HOH   HOH C . 
O 5 HOH   42  242 122 HOH   HOH C . 
O 5 HOH   43  243 102 HOH   HOH C . 
O 5 HOH   44  244 298 HOH   HOH C . 
O 5 HOH   45  245 43  HOH   HOH C . 
O 5 HOH   46  246 135 HOH   HOH C . 
O 5 HOH   47  247 56  HOH   HOH C . 
O 5 HOH   48  248 62  HOH   HOH C . 
O 5 HOH   49  249 275 HOH   HOH C . 
O 5 HOH   50  250 67  HOH   HOH C . 
O 5 HOH   51  251 304 HOH   HOH C . 
O 5 HOH   52  252 40  HOH   HOH C . 
O 5 HOH   53  253 151 HOH   HOH C . 
O 5 HOH   54  254 198 HOH   HOH C . 
O 5 HOH   55  255 328 HOH   HOH C . 
O 5 HOH   56  256 294 HOH   HOH C . 
O 5 HOH   57  257 65  HOH   HOH C . 
O 5 HOH   58  258 341 HOH   HOH C . 
O 5 HOH   59  259 146 HOH   HOH C . 
O 5 HOH   60  260 171 HOH   HOH C . 
O 5 HOH   61  261 359 HOH   HOH C . 
O 5 HOH   62  262 346 HOH   HOH C . 
O 5 HOH   63  263 324 HOH   HOH C . 
O 5 HOH   64  264 270 HOH   HOH C . 
O 5 HOH   65  265 241 HOH   HOH C . 
O 5 HOH   66  266 103 HOH   HOH C . 
O 5 HOH   67  267 330 HOH   HOH C . 
O 5 HOH   68  268 363 HOH   HOH C . 
O 5 HOH   69  269 246 HOH   HOH C . 
O 5 HOH   70  270 92  HOH   HOH C . 
O 5 HOH   71  271 313 HOH   HOH C . 
O 5 HOH   72  272 206 HOH   HOH C . 
O 5 HOH   73  273 351 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
2  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
3  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
4  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
5  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
6  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
7  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
8  1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
9  1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
10 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
11 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
12 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
13 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
14 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
15 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
16 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
17 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
18 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
19 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
20 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
21 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
22 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
23 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
24 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
25 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
26 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
27 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
28 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
29 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
30 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
31 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
32 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
33 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
34 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
35 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
36 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
37 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
38 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
39 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
40 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
41 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
42 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
43 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
44 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
45 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
46 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
47 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
48 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
49 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
50 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
51 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
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           7HH3 
_cell.length_a           41.860 
_cell.length_b           42.150 
_cell.length_c           159.590 
_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                         7HH3 
_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          7HH3 
_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                     7HH3 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             53.20 
_reflns.d_resolution_high            1.64 
_reflns.number_obs                   35301 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            0.084 
_reflns.pdbx_netI_over_sigmaI        9.6 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.093 
_reflns.pdbx_Rpim_I_all              0.038 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     186966 
_reflns.pdbx_chi_squared             0.97 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.64 
_reflns_shell.d_res_low                   1.68 
_reflns_shell.number_measured_all         10567 
_reflns_shell.number_unique_obs           2418 
_reflns_shell.Rmerge_I_obs                1.309 
_reflns_shell.pdbx_chi_squared            0.61 
_reflns_shell.pdbx_redundancy             4.4 
_reflns_shell.percent_possible_obs        92.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.488 
_reflns_shell.pdbx_Rpim_I_all             0.694 
_reflns_shell.pdbx_CC_half                0.309 
_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                                 7HH3 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     33381 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.79 
_refine.ls_d_res_high                            1.64 
_refine.ls_percent_reflns_obs                    98.91 
_refine.ls_R_factor_obs                          0.21043 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20792 
_refine.ls_R_factor_R_free                       0.25542 
_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                  1851 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.B_iso_mean                               37.798 
_refine.aniso_B[1][1]                            0.58 
_refine.aniso_B[2][2]                            -0.40 
_refine.aniso_B[3][3]                            -0.18 
_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                       0.113 
_refine.pdbx_overall_ESU_R_Free                  0.116 
_refine.overall_SU_ML                            0.109 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.404 
_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         48 
_refine_hist.number_atoms_solvent             273 
_refine_hist.number_atoms_total               2461 
_refine_hist.d_res_high                       1.64 
_refine_hist.d_res_low                        40.79 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.012  ? 2281 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.741  1.836  ? 3100 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.999  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.486  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.299 10.000 ? 306  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.127  0.200  ? 287  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 1858 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.410  3.510  ? 1068 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.675  6.274  ? 1329 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.418  3.837  ? 1213 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.534  50.98  ? 3486 '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                       1.640 
_refine_ls_shell.d_res_low                        1.682 
_refine_ls_shell.number_reflns_R_work             2274 
_refine_ls_shell.R_factor_R_work                  0.346 
_refine_ls_shell.percent_reflns_obs               92.19 
_refine_ls_shell.R_factor_R_free                  0.363 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             133 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH3 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1245580425' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH3 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HH3 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH3 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH3 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 7HH3 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH3 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH3 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH3 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH3 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH3 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HH3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B HOH 249 ? ? O B HOH 274 ? ? 1.42 
2 1 O   A HOH 218 ? ? O C HOH 208 ? ? 1.47 
3 1 O   A HOH 221 ? ? O A HOH 281 ? ? 1.63 
4 1 O   C HOH 259 ? ? O C HOH 263 ? ? 1.82 
5 1 OD1 C ASP 26  ? ? O C HOH 201 ? ? 1.98 
6 1 O   B HOH 264 ? ? O B HOH 274 ? ? 2.05 
7 1 O   C HOH 255 ? ? O C HOH 268 ? ? 2.06 
8 1 O4  A SO4 104 ? ? O A HOH 201 ? ? 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 A HOH 247 ? ? 1_555 O A HOH 285 ? ? 4_545 1.94 
2 1 O A HOH 263 ? ? 1_555 O A HOH 275 ? ? 4_445 2.02 
# 
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 ? ? -155.12 67.19   
2 1 ASN B 38 ? ? 78.64   -2.89   
3 1 ASN B 87 ? ? -159.76 61.90   
4 1 ASN C 87 ? ? -152.27 52.36   
5 1 ALA C 90 ? ? -74.76  -136.88 
6 1 SER C 91 ? ? -125.77 -70.30  
# 
_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            149.65 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.087 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       316 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.94 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 0  ? A GLY 1  
2  1 Y 1 B GLY 0  ? B GLY 1  
3  1 Y 1 B ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C 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 
A1A3X N1   N N N 1   
A1A3X C4   C N N 2   
A1A3X C5   C N N 3   
A1A3X C6   C N N 4   
A1A3X C7   C N N 5   
A1A3X N    N N N 6   
A1A3X C1   C N S 7   
A1A3X C    C N N 8   
A1A3X C3   C N N 9   
A1A3X C2   C N N 10  
A1A3X H16  H N N 11  
A1A3X H18  H N N 12  
A1A3X H9   H N N 13  
A1A3X H8   H N N 14  
A1A3X H11  H N N 15  
A1A3X H10  H N N 16  
A1A3X H13  H N N 17  
A1A3X H12  H N N 18  
A1A3X H14  H N N 19  
A1A3X H15  H N N 20  
A1A3X H3   H N N 21  
A1A3X H    H N N 22  
A1A3X H2   H N N 23  
A1A3X H1   H N N 24  
A1A3X H7   H N N 25  
A1A3X H6   H N N 26  
A1A3X H5   H N N 27  
A1A3X H4   H N N 28  
ALA   N    N N N 29  
ALA   CA   C N S 30  
ALA   C    C N N 31  
ALA   O    O N N 32  
ALA   CB   C N N 33  
ALA   OXT  O N N 34  
ALA   H    H N N 35  
ALA   H2   H N N 36  
ALA   HA   H N N 37  
ALA   HB1  H N N 38  
ALA   HB2  H N N 39  
ALA   HB3  H N N 40  
ALA   HXT  H N N 41  
ARG   N    N N N 42  
ARG   CA   C N S 43  
ARG   C    C N N 44  
ARG   O    O N N 45  
ARG   CB   C N N 46  
ARG   CG   C N N 47  
ARG   CD   C N N 48  
ARG   NE   N N N 49  
ARG   CZ   C N N 50  
ARG   NH1  N N N 51  
ARG   NH2  N N N 52  
ARG   OXT  O N N 53  
ARG   H    H N N 54  
ARG   H2   H N N 55  
ARG   HA   H N N 56  
ARG   HB2  H N N 57  
ARG   HB3  H N N 58  
ARG   HG2  H N N 59  
ARG   HG3  H N N 60  
ARG   HD2  H N N 61  
ARG   HD3  H N N 62  
ARG   HE   H N N 63  
ARG   HH11 H N N 64  
ARG   HH12 H N N 65  
ARG   HH21 H N N 66  
ARG   HH22 H N N 67  
ARG   HXT  H N N 68  
ASN   N    N N N 69  
ASN   CA   C N S 70  
ASN   C    C N N 71  
ASN   O    O N N 72  
ASN   CB   C N N 73  
ASN   CG   C N N 74  
ASN   OD1  O N N 75  
ASN   ND2  N N N 76  
ASN   OXT  O N N 77  
ASN   H    H N N 78  
ASN   H2   H N N 79  
ASN   HA   H N N 80  
ASN   HB2  H N N 81  
ASN   HB3  H N N 82  
ASN   HD21 H N N 83  
ASN   HD22 H N N 84  
ASN   HXT  H N N 85  
ASP   N    N N N 86  
ASP   CA   C N S 87  
ASP   C    C N N 88  
ASP   O    O N N 89  
ASP   CB   C N N 90  
ASP   CG   C N N 91  
ASP   OD1  O N N 92  
ASP   OD2  O N N 93  
ASP   OXT  O N N 94  
ASP   H    H N N 95  
ASP   H2   H N N 96  
ASP   HA   H N N 97  
ASP   HB2  H N N 98  
ASP   HB3  H N N 99  
ASP   HD2  H N N 100 
ASP   HXT  H N N 101 
CYS   N    N N N 102 
CYS   CA   C N R 103 
CYS   C    C N N 104 
CYS   O    O N N 105 
CYS   CB   C N N 106 
CYS   SG   S N N 107 
CYS   OXT  O N N 108 
CYS   H    H N N 109 
CYS   H2   H N N 110 
CYS   HA   H N N 111 
CYS   HB2  H N N 112 
CYS   HB3  H N N 113 
CYS   HG   H N N 114 
CYS   HXT  H N N 115 
EDO   C1   C N N 116 
EDO   O1   O N N 117 
EDO   C2   C N N 118 
EDO   O2   O N N 119 
EDO   H11  H N N 120 
EDO   H12  H N N 121 
EDO   HO1  H N N 122 
EDO   H21  H N N 123 
EDO   H22  H N N 124 
EDO   HO2  H N N 125 
GLN   N    N N N 126 
GLN   CA   C N S 127 
GLN   C    C N N 128 
GLN   O    O N N 129 
GLN   CB   C N N 130 
GLN   CG   C N N 131 
GLN   CD   C N N 132 
GLN   OE1  O N N 133 
GLN   NE2  N N N 134 
GLN   OXT  O N N 135 
GLN   H    H N N 136 
GLN   H2   H N N 137 
GLN   HA   H N N 138 
GLN   HB2  H N N 139 
GLN   HB3  H N N 140 
GLN   HG2  H N N 141 
GLN   HG3  H N N 142 
GLN   HE21 H N N 143 
GLN   HE22 H N N 144 
GLN   HXT  H N N 145 
GLU   N    N N N 146 
GLU   CA   C N S 147 
GLU   C    C N N 148 
GLU   O    O N N 149 
GLU   CB   C N N 150 
GLU   CG   C N N 151 
GLU   CD   C N N 152 
GLU   OE1  O N N 153 
GLU   OE2  O N N 154 
GLU   OXT  O N N 155 
GLU   H    H N N 156 
GLU   H2   H N N 157 
GLU   HA   H N N 158 
GLU   HB2  H N N 159 
GLU   HB3  H N N 160 
GLU   HG2  H N N 161 
GLU   HG3  H N N 162 
GLU   HE2  H N N 163 
GLU   HXT  H N N 164 
GLY   N    N N N 165 
GLY   CA   C N N 166 
GLY   C    C N N 167 
GLY   O    O N N 168 
GLY   OXT  O N N 169 
GLY   H    H N N 170 
GLY   H2   H N N 171 
GLY   HA2  H N N 172 
GLY   HA3  H N N 173 
GLY   HXT  H N N 174 
HIS   N    N N N 175 
HIS   CA   C N S 176 
HIS   C    C N N 177 
HIS   O    O N N 178 
HIS   CB   C N N 179 
HIS   CG   C Y N 180 
HIS   ND1  N Y N 181 
HIS   CD2  C Y N 182 
HIS   CE1  C Y N 183 
HIS   NE2  N Y N 184 
HIS   OXT  O N N 185 
HIS   H    H N N 186 
HIS   H2   H N N 187 
HIS   HA   H N N 188 
HIS   HB2  H N N 189 
HIS   HB3  H N N 190 
HIS   HD1  H N N 191 
HIS   HD2  H N N 192 
HIS   HE1  H N N 193 
HIS   HE2  H N N 194 
HIS   HXT  H N N 195 
HOH   O    O N N 196 
HOH   H1   H N N 197 
HOH   H2   H N N 198 
ILE   N    N N N 199 
ILE   CA   C N S 200 
ILE   C    C N N 201 
ILE   O    O N N 202 
ILE   CB   C N S 203 
ILE   CG1  C N N 204 
ILE   CG2  C N N 205 
ILE   CD1  C N N 206 
ILE   OXT  O N N 207 
ILE   H    H N N 208 
ILE   H2   H N N 209 
ILE   HA   H N N 210 
ILE   HB   H N N 211 
ILE   HG12 H N N 212 
ILE   HG13 H N N 213 
ILE   HG21 H N N 214 
ILE   HG22 H N N 215 
ILE   HG23 H N N 216 
ILE   HD11 H N N 217 
ILE   HD12 H N N 218 
ILE   HD13 H N N 219 
ILE   HXT  H N N 220 
LEU   N    N N N 221 
LEU   CA   C N S 222 
LEU   C    C N N 223 
LEU   O    O N N 224 
LEU   CB   C N N 225 
LEU   CG   C N N 226 
LEU   CD1  C N N 227 
LEU   CD2  C N N 228 
LEU   OXT  O N N 229 
LEU   H    H N N 230 
LEU   H2   H N N 231 
LEU   HA   H N N 232 
LEU   HB2  H N N 233 
LEU   HB3  H N N 234 
LEU   HG   H N N 235 
LEU   HD11 H N N 236 
LEU   HD12 H N N 237 
LEU   HD13 H N N 238 
LEU   HD21 H N N 239 
LEU   HD22 H N N 240 
LEU   HD23 H N N 241 
LEU   HXT  H N N 242 
LYS   N    N N N 243 
LYS   CA   C N S 244 
LYS   C    C N N 245 
LYS   O    O N N 246 
LYS   CB   C N N 247 
LYS   CG   C N N 248 
LYS   CD   C N N 249 
LYS   CE   C N N 250 
LYS   NZ   N N N 251 
LYS   OXT  O N N 252 
LYS   H    H N N 253 
LYS   H2   H N N 254 
LYS   HA   H N N 255 
LYS   HB2  H N N 256 
LYS   HB3  H N N 257 
LYS   HG2  H N N 258 
LYS   HG3  H N N 259 
LYS   HD2  H N N 260 
LYS   HD3  H N N 261 
LYS   HE2  H N N 262 
LYS   HE3  H N N 263 
LYS   HZ1  H N N 264 
LYS   HZ2  H N N 265 
LYS   HZ3  H N N 266 
LYS   HXT  H N N 267 
MET   N    N N N 268 
MET   CA   C N S 269 
MET   C    C N N 270 
MET   O    O N N 271 
MET   CB   C N N 272 
MET   CG   C N N 273 
MET   SD   S N N 274 
MET   CE   C N N 275 
MET   OXT  O N N 276 
MET   H    H N N 277 
MET   H2   H N N 278 
MET   HA   H N N 279 
MET   HB2  H N N 280 
MET   HB3  H N N 281 
MET   HG2  H N N 282 
MET   HG3  H N N 283 
MET   HE1  H N N 284 
MET   HE2  H N N 285 
MET   HE3  H N N 286 
MET   HXT  H N N 287 
PHE   N    N N N 288 
PHE   CA   C N S 289 
PHE   C    C N N 290 
PHE   O    O N N 291 
PHE   CB   C N N 292 
PHE   CG   C Y N 293 
PHE   CD1  C Y N 294 
PHE   CD2  C Y N 295 
PHE   CE1  C Y N 296 
PHE   CE2  C Y N 297 
PHE   CZ   C Y N 298 
PHE   OXT  O N N 299 
PHE   H    H N N 300 
PHE   H2   H N N 301 
PHE   HA   H N N 302 
PHE   HB2  H N N 303 
PHE   HB3  H N N 304 
PHE   HD1  H N N 305 
PHE   HD2  H N N 306 
PHE   HE1  H N N 307 
PHE   HE2  H N N 308 
PHE   HZ   H N N 309 
PHE   HXT  H N N 310 
PRO   N    N N N 311 
PRO   CA   C N S 312 
PRO   C    C N N 313 
PRO   O    O N N 314 
PRO   CB   C N N 315 
PRO   CG   C N N 316 
PRO   CD   C N N 317 
PRO   OXT  O N N 318 
PRO   H    H N N 319 
PRO   HA   H N N 320 
PRO   HB2  H N N 321 
PRO   HB3  H N N 322 
PRO   HG2  H N N 323 
PRO   HG3  H N N 324 
PRO   HD2  H N N 325 
PRO   HD3  H N N 326 
PRO   HXT  H N N 327 
SER   N    N N N 328 
SER   CA   C N S 329 
SER   C    C N N 330 
SER   O    O N N 331 
SER   CB   C N N 332 
SER   OG   O N N 333 
SER   OXT  O N N 334 
SER   H    H N N 335 
SER   H2   H N N 336 
SER   HA   H N N 337 
SER   HB2  H N N 338 
SER   HB3  H N N 339 
SER   HG   H N N 340 
SER   HXT  H N N 341 
SO4   S    S N N 342 
SO4   O1   O N N 343 
SO4   O2   O N N 344 
SO4   O3   O N N 345 
SO4   O4   O N N 346 
THR   N    N N N 347 
THR   CA   C N S 348 
THR   C    C N N 349 
THR   O    O N N 350 
THR   CB   C N R 351 
THR   OG1  O N N 352 
THR   CG2  C N N 353 
THR   OXT  O N N 354 
THR   H    H N N 355 
THR   H2   H N N 356 
THR   HA   H N N 357 
THR   HB   H N N 358 
THR   HG1  H N N 359 
THR   HG21 H N N 360 
THR   HG22 H N N 361 
THR   HG23 H N N 362 
THR   HXT  H N N 363 
TRP   N    N N N 364 
TRP   CA   C N S 365 
TRP   C    C N N 366 
TRP   O    O N N 367 
TRP   CB   C N N 368 
TRP   CG   C Y N 369 
TRP   CD1  C Y N 370 
TRP   CD2  C Y N 371 
TRP   NE1  N Y N 372 
TRP   CE2  C Y N 373 
TRP   CE3  C Y N 374 
TRP   CZ2  C Y N 375 
TRP   CZ3  C Y N 376 
TRP   CH2  C Y N 377 
TRP   OXT  O N N 378 
TRP   H    H N N 379 
TRP   H2   H N N 380 
TRP   HA   H N N 381 
TRP   HB2  H N N 382 
TRP   HB3  H N N 383 
TRP   HD1  H N N 384 
TRP   HE1  H N N 385 
TRP   HE3  H N N 386 
TRP   HZ2  H N N 387 
TRP   HZ3  H N N 388 
TRP   HH2  H N N 389 
TRP   HXT  H N N 390 
TYR   N    N N N 391 
TYR   CA   C N S 392 
TYR   C    C N N 393 
TYR   O    O N N 394 
TYR   CB   C N N 395 
TYR   CG   C Y N 396 
TYR   CD1  C Y N 397 
TYR   CD2  C Y N 398 
TYR   CE1  C Y N 399 
TYR   CE2  C Y N 400 
TYR   CZ   C Y N 401 
TYR   OH   O N N 402 
TYR   OXT  O N N 403 
TYR   H    H N N 404 
TYR   H2   H N N 405 
TYR   HA   H N N 406 
TYR   HB2  H N N 407 
TYR   HB3  H N N 408 
TYR   HD1  H N N 409 
TYR   HD2  H N N 410 
TYR   HE1  H N N 411 
TYR   HE2  H N N 412 
TYR   HH   H N N 413 
TYR   HXT  H N N 414 
VAL   N    N N N 415 
VAL   CA   C N S 416 
VAL   C    C N N 417 
VAL   O    O N N 418 
VAL   CB   C N N 419 
VAL   CG1  C N N 420 
VAL   CG2  C N N 421 
VAL   OXT  O N N 422 
VAL   H    H N N 423 
VAL   H2   H N N 424 
VAL   HA   H N N 425 
VAL   HB   H N N 426 
VAL   HG11 H N N 427 
VAL   HG12 H N N 428 
VAL   HG13 H N N 429 
VAL   HG21 H N N 430 
VAL   HG22 H N N 431 
VAL   HG23 H N N 432 
VAL   HXT  H N N 433 
# 
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 
A1A3X C   C1   sing N N 1   
A1A3X C1  C2   sing N N 2   
A1A3X C2  C3   sing N N 3   
A1A3X C3  C4   sing N N 4   
A1A3X C4  C5   sing N N 5   
A1A3X C5  N    sing N N 6   
A1A3X C1  N    sing N N 7   
A1A3X N   C6   sing N N 8   
A1A3X C6  C7   sing N N 9   
A1A3X C7  N1   sing N N 10  
A1A3X N1  H16  sing N N 11  
A1A3X N1  H18  sing N N 12  
A1A3X C4  H9   sing N N 13  
A1A3X C4  H8   sing N N 14  
A1A3X C5  H11  sing N N 15  
A1A3X C5  H10  sing N N 16  
A1A3X C6  H13  sing N N 17  
A1A3X C6  H12  sing N N 18  
A1A3X C7  H14  sing N N 19  
A1A3X C7  H15  sing N N 20  
A1A3X C1  H3   sing N N 21  
A1A3X C   H    sing N N 22  
A1A3X C   H2   sing N N 23  
A1A3X C   H1   sing N N 24  
A1A3X C3  H7   sing N N 25  
A1A3X C3  H6   sing N N 26  
A1A3X C2  H5   sing N N 27  
A1A3X C2  H4   sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
EDO   C1  O1   sing N N 111 
EDO   C1  C2   sing N N 112 
EDO   C1  H11  sing N N 113 
EDO   C1  H12  sing N N 114 
EDO   O1  HO1  sing N N 115 
EDO   C2  O2   sing N N 116 
EDO   C2  H21  sing N N 117 
EDO   C2  H22  sing N N 118 
EDO   O2  HO2  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
SO4   S   O1   doub N N 327 
SO4   S   O2   doub N N 328 
SO4   S   O3   sing N N 329 
SO4   S   O4   sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TRP   N   CA   sing N N 347 
TRP   N   H    sing N N 348 
TRP   N   H2   sing N N 349 
TRP   CA  C    sing N N 350 
TRP   CA  CB   sing N N 351 
TRP   CA  HA   sing N N 352 
TRP   C   O    doub N N 353 
TRP   C   OXT  sing N N 354 
TRP   CB  CG   sing N N 355 
TRP   CB  HB2  sing N N 356 
TRP   CB  HB3  sing N N 357 
TRP   CG  CD1  doub Y N 358 
TRP   CG  CD2  sing Y N 359 
TRP   CD1 NE1  sing Y N 360 
TRP   CD1 HD1  sing N N 361 
TRP   CD2 CE2  doub Y N 362 
TRP   CD2 CE3  sing Y N 363 
TRP   NE1 CE2  sing Y N 364 
TRP   NE1 HE1  sing N N 365 
TRP   CE2 CZ2  sing Y N 366 
TRP   CE3 CZ3  doub Y N 367 
TRP   CE3 HE3  sing N N 368 
TRP   CZ2 CH2  doub Y N 369 
TRP   CZ2 HZ2  sing N N 370 
TRP   CZ3 CH2  sing Y N 371 
TRP   CZ3 HZ3  sing N N 372 
TRP   CH2 HH2  sing N N 373 
TRP   OXT HXT  sing N N 374 
TYR   N   CA   sing N N 375 
TYR   N   H    sing N N 376 
TYR   N   H2   sing N N 377 
TYR   CA  C    sing N N 378 
TYR   CA  CB   sing N N 379 
TYR   CA  HA   sing N N 380 
TYR   C   O    doub N N 381 
TYR   C   OXT  sing N N 382 
TYR   CB  CG   sing N N 383 
TYR   CB  HB2  sing N N 384 
TYR   CB  HB3  sing N N 385 
TYR   CG  CD1  doub Y N 386 
TYR   CG  CD2  sing Y N 387 
TYR   CD1 CE1  sing Y N 388 
TYR   CD1 HD1  sing N N 389 
TYR   CD2 CE2  doub Y N 390 
TYR   CD2 HD2  sing N N 391 
TYR   CE1 CZ   doub Y N 392 
TYR   CE1 HE1  sing N N 393 
TYR   CE2 CZ   sing Y N 394 
TYR   CE2 HE2  sing N N 395 
TYR   CZ  OH   sing N N 396 
TYR   OH  HH   sing N N 397 
TYR   OXT HXT  sing N N 398 
VAL   N   CA   sing N N 399 
VAL   N   H    sing N N 400 
VAL   N   H2   sing N N 401 
VAL   CA  C    sing N N 402 
VAL   CA  CB   sing N N 403 
VAL   CA  HA   sing N N 404 
VAL   C   O    doub N N 405 
VAL   C   OXT  sing N N 406 
VAL   CB  CG1  sing N N 407 
VAL   CB  CG2  sing N N 408 
VAL   CB  HB   sing N N 409 
VAL   CG1 HG11 sing N N 410 
VAL   CG1 HG12 sing N N 411 
VAL   CG1 HG13 sing N N 412 
VAL   CG2 HG21 sing N N 413 
VAL   CG2 HG22 sing N N 414 
VAL   CG2 HG23 sing N N 415 
VAL   OXT HXT  sing N N 416 
# 
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                    7HH3 
_atom_sites.fract_transf_matrix[1][1]   0.023889 
_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]   0.023725 
_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]   0.006266 
_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  ? 0.694   4.134   2.320   1.00 55.68  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.440  3.470   1.618   1.00 59.19  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.094   2.425   0.639   1.00 55.74  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.112   2.654   -0.008  1.00 55.18  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.356  4.485   0.922   1.00 62.82  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.307  5.198   1.872   1.00 70.85  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.677  4.250   2.573   1.00 67.08  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.207  5.335   3.906   1.00 76.07  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.556  1.234   0.553   1.00 51.63  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.134  0.140   -0.339  1.00 47.49  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.131   0.521   -1.795  1.00 41.29  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.606  1.305   -2.392  1.00 43.56  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.383  -0.797  -0.242  1.00 45.68  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.828  -0.624  1.183   1.00 49.83  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.743  0.874   1.355   1.00 48.69  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.160   -0.083  -2.386  1.00 36.79  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.329   0.041   -3.818  1.00 37.34  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.847   -1.277  -4.403  1.00 33.66  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.382   -2.142  -3.659  1.00 35.84  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.811   0.238   -4.168  1.00 45.66  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.435   1.529   -3.743  1.00 61.64  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.126   2.209   -2.583  1.00 67.71  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.389   2.248   -4.349  1.00 61.06  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.867   3.304   -2.504  1.00 67.29  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.644   3.345   -3.565  1.00 65.64  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.941   -1.432  -5.726  1.00 27.82  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.674   -2.731  -6.323  1.00 26.39  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.815   -3.689  -5.986  1.00 27.57  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.927   -3.260  -5.615  1.00 26.63  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.467   -2.593  -7.824  1.00 31.26  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.532   -4.990  -6.080  1.00 27.11  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.577   -5.997  -5.911  1.00 29.60  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.716   -5.789  -6.920  1.00 31.34  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.483   -5.439  -8.078  1.00 30.32  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.963   -7.393  -6.026  1.00 26.80  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.209   -7.760  -4.756  1.00 27.73  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.908   -7.985  -3.568  1.00 26.92  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.182  -7.925  -4.757  1.00 24.83  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.251   -8.306  -2.384  1.00 27.24  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.833  -8.300  -3.564  1.00 25.63  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.130  -8.482  -2.397  1.00 28.22  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.960   -6.035  -6.462  1.00 24.91  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.127   -5.983  -7.325  1.00 25.28  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.004   -7.190  -7.010  1.00 24.31  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.994   -7.705  -5.894  1.00 23.11  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.895   -4.687  -7.033  1.00 27.47  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.272   -4.440  -5.593  1.00 32.01  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.104   -3.179  -5.336  1.00 39.30  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.686   -3.135  -3.935  1.00 37.43  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.698   -3.228  -2.857  1.00 34.82  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.838   -7.644  -7.960  1.00 25.47  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.803   -8.715  -7.681  1.00 26.20  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.601   -8.420  -6.408  1.00 25.35  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.018  -7.277  -6.175  1.00 26.38  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.711   -8.708  -8.934  1.00 28.69  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.859   -8.069  -10.004 1.00 28.20  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.888   -7.109  -9.336  1.00 30.58  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.778   -9.457  -5.576  1.00 22.30  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.547  -9.326  -4.340  1.00 22.38  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.627   -9.199  -3.132  1.00 23.45  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.995   -9.539  -1.992  1.00 22.54  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.362   -8.825  -3.393  1.00 20.58  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.438   -8.762  -2.262  1.00 21.10  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.214   -10.134 -1.629  1.00 19.82  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.084   -11.133 -2.339  1.00 21.16  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.084   -8.165  -2.648  1.00 21.65  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.053   -6.664  -2.879  1.00 25.82  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.009   -5.967  -2.409  1.00 25.84  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.057   -6.197  -3.471  1.00 24.58  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.112   -10.142 -0.280  1.00 18.83  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.917   -11.401 0.455   1.00 19.20  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.451   -11.518 0.880   1.00 18.91  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.871   -10.524 1.349   1.00 22.46  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.824   -11.501 1.683   1.00 20.59  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.319   -11.271 1.387   1.00 20.98  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.176  -11.350 2.653   1.00 22.82  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.831   -12.216 0.319   1.00 23.04  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.906   -12.738 0.738   1.00 18.70  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.465   -12.910 0.958   1.00 19.26  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.201   -14.273 1.584   1.00 22.15  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.063   -15.153 1.668   1.00 21.74  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.654   -12.759 -0.353  1.00 18.51  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.823   -11.349 -0.940  1.00 20.60  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.041   -13.832 -1.376  1.00 20.94  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.969   -14.442 2.082   1.00 20.57  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.445   -15.786 2.157   1.00 23.45  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.484   -15.895 0.974   1.00 22.86  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.315  -14.983 0.759   1.00 22.85  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.669   -16.105 3.447   1.00 22.61  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.584   -16.175 4.659   1.00 24.09  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.899   -15.016 5.369   1.00 26.59  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.081   -17.393 5.099   1.00 24.11  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.781   -15.080 6.454   1.00 30.60  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.980   -17.460 6.172   1.00 29.74  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.312   -16.306 6.852   1.00 30.77  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.600   -16.982 0.186   1.00 20.77  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.196  -17.158 -1.017  1.00 21.99  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.192  -18.311 -0.810  1.00 25.63  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.827  -19.372 -0.279  1.00 25.31  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.715   -17.402 -2.227  1.00 21.94  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.460  -18.106 -1.228  1.00 23.79  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.496  -19.102 -0.980  1.00 25.89  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.873  -19.861 -2.263  1.00 28.94  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.271  -19.277 -3.264  1.00 29.59  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.701  -18.376 -0.367  1.00 27.03  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.789  -19.323 0.178   1.00 30.64  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.274  -20.303 1.242   1.00 31.81  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.373  -21.070 1.957   1.00 31.72  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.988  -22.045 1.058   1.00 31.50  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.775  -21.189 -2.198  1.00 29.84  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.265  -22.073 -3.243  1.00 31.71  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.368  -22.921 -2.600  1.00 34.36  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.241  -23.295 -1.440  1.00 30.42  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.156  -23.069 -3.618  1.00 34.76  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.848  -22.460 -4.102  1.00 33.35  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.941  -21.924 -5.828  1.00 36.06  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.599  -23.476 -6.647  1.00 38.67  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.394  -23.271 -3.373  1.00 38.85  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.446  -24.179 -2.921  1.00 42.18  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.845  -25.480 -2.393  1.00 39.38  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.957  -26.053 -3.018  1.00 40.99  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.327  -24.466 -4.141  1.00 43.54  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.592  -25.255 -3.862  1.00 49.89  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.788 -24.709 -4.637  1.00 55.33  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -12.035 -25.487 -4.340  1.00 61.13  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -13.168 -24.987 -5.120  1.00 68.53  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -7.300  -25.922 -1.206  1.00 37.00  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -6.849  -27.185 -0.644  1.00 39.70  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -5.512  -27.098 0.088   1.00 44.78  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -5.036  -28.106 0.614   1.00 46.69  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -4.913  -25.898 0.142   1.00 35.23  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -3.663  -25.753 0.844   1.00 34.63  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -3.767  -24.609 1.832   1.00 28.90  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -4.488  -23.648 1.594   1.00 30.24  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -2.532  -25.418 -0.128  1.00 40.03  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -2.169  -26.515 -1.117  1.00 50.09  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -1.372  -27.589 -0.736  1.00 60.43  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -2.581  -26.438 -2.444  1.00 58.10  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? -1.019  -28.572 -1.645  1.00 72.58  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -2.224  -27.409 -3.366  1.00 68.22  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -1.446  -28.482 -2.961  1.00 79.59  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? -1.109  -29.451 -3.865  1.00 96.87  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -3.024  -24.661 2.951   1.00 31.14  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -3.004  -23.549 3.909   1.00 31.52  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -2.294  -22.366 3.224   1.00 30.37  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -1.548  -22.578 2.272   1.00 28.94  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -2.242  -24.122 5.117   1.00 35.16  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -1.400  -25.227 4.520   1.00 37.68  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -2.140  -25.782 3.321   1.00 35.82  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -2.574  -21.140 3.681   1.00 27.79  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -1.824  -19.942 3.283   1.00 23.51  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? -0.325  -20.232 3.386   1.00 24.90  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? 0.147   -20.654 4.445   1.00 25.10  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -2.223  -18.750 4.164   1.00 24.83  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -3.690  -18.380 4.041   1.00 25.39  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -4.732  -18.978 4.733   1.00 28.61  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -4.249  -17.425 3.252   1.00 25.60  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -5.896  -18.427 4.350   1.00 28.67  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -5.627  -17.465 3.446   1.00 28.43  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? 0.428   -19.985 2.293   1.00 24.97  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 1.742   -20.611 2.191   1.00 24.85  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 2.815   -19.549 2.019   1.00 23.51  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 2.675   -18.724 1.129   1.00 25.01  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 1.765   -21.514 0.952   1.00 25.24  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 2.867   -22.545 1.011   1.00 23.30  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 4.210   -22.360 0.810   1.00 26.48  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 2.689   -23.914 1.398   1.00 24.62  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 4.875   -23.558 0.971   1.00 24.33  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 3.967   -24.525 1.344   1.00 28.27  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 1.573   -24.691 1.747   1.00 31.55  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 4.154   -25.874 1.663   1.00 32.05  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 1.760   -26.027 2.054   1.00 34.09  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 3.042   -26.608 2.026   1.00 38.10  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 3.959   -19.594 2.746   1.00 21.91  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 5.020   -18.599 2.522   1.00 22.59  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 5.542   -18.563 1.076   1.00 20.64  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 5.849   -19.611 0.486   1.00 21.74  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 6.100   -19.036 3.553   1.00 23.28  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 5.856   -20.511 3.749   1.00 22.06  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 4.311   -20.605 3.750   1.00 20.98  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 5.618   -17.363 0.495   1.00 19.34  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 5.892   -17.235 -0.938  1.00 21.30  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 6.488   -15.865 -1.265  1.00 19.82  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 6.481   -14.945 -0.432  1.00 19.73  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 4.609   -17.486 -1.745  1.00 21.54  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 6.940   -15.686 -2.505  1.00 20.41  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 7.324   -14.342 -2.908  1.00 20.99  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 6.791   -14.065 -4.317  1.00 18.56  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 6.527   -15.023 -5.063  1.00 20.27  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 8.856   -14.262 -2.828  1.00 19.95  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 9.576   -15.056 -3.910  1.00 19.24  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 11.166  -14.833 -3.758  1.00 20.12  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 11.796  -15.679 -4.798  1.00 22.90  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 13.053  -16.121 -4.739  1.00 23.86  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 13.764  -15.955 -3.620  1.00 23.88  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 13.571  -16.767 -5.778  1.00 25.99  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 6.702   -12.780 -4.693  1.00 22.55  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 6.433   -12.424 -6.087  1.00 21.38  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 7.750   -12.540 -6.838  1.00 23.27  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 8.713   -11.918 -6.421  1.00 21.99  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 5.909   -10.981 -6.203  1.00 25.46  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 4.671   -10.734 -5.278  1.00 29.57  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 5.630   -10.637 -7.687  1.00 23.21  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 3.378   -11.371 -5.725  1.00 33.80  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 7.798   -13.364 -7.885  1.00 23.11  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 9.050   -13.635 -8.588  1.00 26.19  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 9.249   -12.651 -9.739  1.00 29.68  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 8.316   -12.004 -10.182 1.00 25.75  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 9.091   -15.051 -9.152  1.00 23.12  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 10.153  -15.945 -8.530  1.00 26.77  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 10.772  -15.518 -7.529  1.00 28.71  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 10.337  -17.062 -9.004  1.00 30.67  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 10.501  -12.544 -10.220 1.00 30.29  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 10.767  -11.886 -11.482 1.00 35.11  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 10.488  -12.892 -12.598 1.00 29.35  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 10.470  -14.095 -12.375 1.00 35.28  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 12.247  -11.499 -11.588 1.00 37.22  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 12.725  -10.354 -10.703 1.00 47.65  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 12.432  -9.179  -11.045 1.00 52.90  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 13.413  -10.646 -9.696  1.00 50.10  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 10.255  -12.405 -13.806 1.00 36.59  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 10.237  -13.296 -14.958 1.00 32.29  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 11.593  -13.142 -15.643 1.00 35.42  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 11.980  -12.010 -15.948 1.00 34.33  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 9.118   -12.822 -15.892 1.00 35.10  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 7.751   -12.751 -15.157 1.00 36.68  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 9.068   -13.676 -17.161 1.00 32.25  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.799   -11.703 -15.710 1.00 35.06  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 12.296  -14.259 -15.874 1.00 31.48  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 13.612  -14.203 -16.508 1.00 31.98  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 13.454  -13.825 -17.988 1.00 31.32  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 12.422  -14.094 -18.598 1.00 30.94  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 14.287  -15.543 -16.356 1.00 34.98  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 14.479  -13.165 -18.551 1.00 31.78  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 14.530  -12.997 -20.004 1.00 33.33  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 14.278  -14.355 -20.655 1.00 28.04  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 14.910  -15.347 -20.294 1.00 31.55  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.882  -12.456 -20.454 1.00 34.61  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 16.123  -10.976 -20.196 1.00 38.97  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 15.138  -10.246 -20.068 1.00 39.20  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 17.307  -10.576 -20.099 1.00 42.63  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 13.353  -14.374 -21.629 1.00 31.93  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 13.108  -15.565 -22.433 1.00 30.60  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 12.177  -16.572 -21.756 1.00 34.76  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 11.788  -17.561 -22.377 1.00 32.64  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.805  -16.300 -20.493 1.00 30.86  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 10.917  -17.196 -19.757 1.00 36.27  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 9.447   -16.890 -20.048 1.00 33.19  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 9.057   -15.768 -20.413 1.00 32.15  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 11.183  -17.087 -18.259 1.00 34.85  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 8.612   -17.904 -19.780 1.00 35.91  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 7.169   -17.827 -19.995 1.00 33.94  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 6.549   -16.762 -19.101 1.00 34.72  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 6.764   -16.766 -17.894 1.00 38.30  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 6.545   -19.203 -19.687 1.00 35.30  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 5.020   -19.128 -19.681 1.00 37.25  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 7.021   -20.232 -20.704 1.00 39.86  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 5.737   -15.897 -19.714 1.00 36.11  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 5.059   -14.803 -19.027 1.00 39.28  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 3.759   -15.295 -18.391 1.00 37.72  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 3.116   -16.209 -18.906 1.00 35.18  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 4.777   -13.638 -19.979 1.00 38.39  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 6.003   -12.837 -20.441 1.00 41.94  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 5.682   -11.633 -21.320 1.00 47.81  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 5.468   -11.964 -22.766 1.00 46.98  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 5.085   -10.749 -23.487 1.00 47.12  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 3.295   -14.691 -17.267 1.00 36.51  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 2.055   -15.146 -16.633 1.00 35.77  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 0.874   -14.643 -17.454 1.00 34.24  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 1.011   -13.702 -18.227 1.00 38.05  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 2.035   -14.502 -15.239 1.00 33.67  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 3.035   -13.357 -15.318 1.00 39.46  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 3.861   -13.509 -16.606 1.00 35.28  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -0.345  -15.171 -17.223 1.00 37.21  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -1.552  -14.581 -17.813 1.00 43.81  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -1.760  -13.132 -17.387 1.00 43.94  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -1.281  -12.720 -16.326 1.00 35.98  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -2.699  -15.466 -17.308 1.00 40.24  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -2.025  -16.756 -16.880 1.00 40.67  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -0.612  -16.381 -16.427 1.00 38.75  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -2.497  -12.327 -18.186 1.00 41.86  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -3.034  -11.045 -17.723 1.00 43.46  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -3.573  -11.125 -16.298 1.00 34.20  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -4.176  -12.121 -15.923 1.00 38.96  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -4.173  -10.732 -18.712 1.00 40.06  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -3.818  -11.506 -19.937 1.00 40.33  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -2.846  -12.613 -19.591 1.00 40.98  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -3.268  -10.082 -15.525 1.00 36.73  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -3.725  -9.856  -14.164 1.00 38.67  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -3.166  -10.868 -13.159 1.00 34.63  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -3.619  -10.852 -12.019 1.00 34.17  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -5.237  -9.659  -14.107 1.00 48.75  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -5.655  -8.476  -14.950 1.00 51.72  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.518  -7.323  -14.522 1.00 54.27  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -6.136  -8.742  -16.154 1.00 56.45  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -2.165  -11.688 -13.545 1.00 30.42  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -1.594  -12.684 -12.637 1.00 25.47  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? -0.112  -12.384 -12.394 1.00 22.82  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? 0.561   -11.673 -13.163 1.00 28.04  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -1.759  -14.145 -13.083 1.00 30.25  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -3.163  -14.648 -13.466 1.00 36.28  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -4.083  -14.429 -12.282 1.00 37.75  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -5.555  -14.635 -12.528 1.00 45.70  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -5.856  -16.039 -12.780 1.00 41.87  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? 0.354   -12.841 -11.236 1.00 20.87  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 1.754   -12.653 -10.861 1.00 21.80  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 2.410   -14.023 -10.815 1.00 21.30  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 1.794   -14.989 -10.443 1.00 22.47  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 1.842   -12.029 -9.450  1.00 22.98  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 1.288   -10.616 -9.417  1.00 25.45  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? -0.087  -10.386 -9.359  1.00 30.46  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 2.115   -9.519  -9.590  1.00 27.85  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -0.596  -9.096  -9.462  1.00 31.25  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 1.621   -8.217  -9.614  1.00 26.70  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? 0.256   -8.011  -9.570  1.00 31.36  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? -0.204  -6.725  -9.694  1.00 33.63  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 3.731   -14.186 -11.067 1.00 21.61  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 4.370   -15.481 -10.805 1.00 21.93  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 4.721   -15.583 -9.324  1.00 22.07  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 5.414   -14.716 -8.796  1.00 25.27  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 5.639   -15.422 -11.645 1.00 23.52  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 5.949   -13.946 -11.771 1.00 23.40  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 4.631   -13.159 -11.595 1.00 24.67  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 4.160   -16.587 -8.655  1.00 24.06  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 4.396   -16.763 -7.228  1.00 21.56  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 5.373   -17.914 -7.025  1.00 23.13  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 5.092   -19.056 -7.440  1.00 23.56  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 3.053   -17.042 -6.542  1.00 20.48  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 2.050   -15.911 -6.847  1.00 22.65  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 3.255   -17.233 -5.016  1.00 21.01  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 2.536   -14.498 -6.575  1.00 23.77  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 6.491   -17.634 -6.329  1.00 21.64  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 7.321   -18.776 -5.990  1.00 22.43  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 7.047   -19.166 -4.537  1.00 20.55  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 7.099   -18.309 -3.648  1.00 23.43  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 8.763   -18.269 -6.163  1.00 22.03  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 9.818   -19.259 -5.684  1.00 25.59  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 10.258  -20.264 -6.546  1.00 27.39  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 10.369  -19.168 -4.397  1.00 27.05  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 11.223  -21.174 -6.137  1.00 28.05  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 11.339  -20.092 -3.996  1.00 28.82  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 11.752  -21.084 -4.863  1.00 30.84  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 6.785   -20.454 -4.303  1.00 19.93  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 6.389   -20.970 -3.002  1.00 20.40  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 7.659   -21.469 -2.323  1.00 25.44  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 8.354   -22.352 -2.864  1.00 23.27  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 5.396   -22.134 -3.235  1.00 25.86  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 3.995   -21.668 -3.630  1.00 26.03  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 3.671   -21.425 -4.966  1.00 27.24  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 3.008   -21.482 -2.673  1.00 25.30  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 2.412   -20.973 -5.333  1.00 26.23  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 1.759   -20.984 -3.039  1.00 25.16  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 1.470   -20.758 -4.365  1.00 25.67  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 7.961   -20.879 -1.164  1.00 23.52  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 9.119   -21.342 -0.399  1.00 23.66  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 8.868   -22.786 0.061   1.00 24.75  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 7.730   -23.211 0.276   1.00 26.60  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 9.377   -20.399 0.791   1.00 21.38  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 9.810   -18.997 0.390   1.00 20.29  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 11.091  -18.784 -0.151  1.00 22.71  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 9.083   -17.850 0.710   1.00 23.24  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 11.498  -17.502 -0.563  1.00 21.49  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 9.525   -16.561 0.338   1.00 20.98  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 10.783  -16.383 -0.241  1.00 22.60  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 9.962   -23.506 0.313   1.00 23.61  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 9.860   -24.866 0.825   1.00 26.36  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 9.648   -25.868 -0.315  1.00 34.43  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 10.515  -26.701 -0.573  1.00 35.71  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 8.520   -25.759 -1.034  1.00 32.25  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 8.267   -26.631 -2.178  1.00 32.10  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 9.075   -26.207 -3.410  1.00 31.37  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 9.370   -27.011 -4.306  1.00 30.29  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 6.769   -26.671 -2.500  1.00 31.83  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 6.369   -25.407 -3.020  1.00 34.24  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 5.904   -27.108 -1.339  1.00 35.37  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 9.353   -24.902 -3.494  1.00 27.50  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 10.029  -24.252 -4.608  1.00 30.17  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 9.214   -24.365 -5.894  1.00 29.71  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 9.794   -24.351 -6.974  1.00 30.27  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 11.497  -24.709 -4.774  1.00 26.97  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 12.230  -24.760 -3.481  1.00 30.86  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 13.014  -25.841 -3.143  1.00 31.89  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 12.309  -23.895 -2.441  1.00 29.29  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 13.514  -25.666 -1.928  1.00 36.11  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 13.130  -24.479 -1.490  1.00 33.00  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 7.884   -24.494 -5.772  1.00 28.85  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 6.967   -24.543 -6.910  1.00 29.78  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 6.581   -23.126 -7.348  1.00 31.45  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 6.770   -22.184 -6.576  1.00 26.83  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 5.679   -25.257 -6.503  1.00 35.17  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 5.812   -26.777 -6.428  1.00 46.95  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 4.718   -27.488 -5.646  1.00 54.88  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 3.961   -26.840 -4.890  1.00 59.79  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 4.648   -28.720 -5.775  1.00 68.53  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 6.183   -22.978 -8.624  1.00 25.53  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 5.689   -21.727 -9.170  1.00 26.46  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 4.228   -21.911 -9.595  1.00 28.56  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 3.838   -22.929 -10.180 1.00 31.87  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 6.541   -21.173 -10.319 1.00 32.31  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 7.768   -20.691 -9.776  1.00 30.82  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 5.907   -19.951 -10.965 1.00 33.08  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 3.404   -20.930 -9.240  1.00 24.87  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 2.044   -20.825 -9.754  1.00 25.17  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 1.710   -19.373 -10.060 1.00 28.72  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 2.363   -18.462 -9.549  1.00 26.83  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 1.065   -21.397 -8.743  1.00 31.03  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? 0.636   -19.166 -10.850 1.00 26.08  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? 0.229   -17.837 -11.238 1.00 26.40  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -1.026  -17.449 -10.460 1.00 29.33  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -2.056  -18.089 -10.571 1.00 31.09  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? -0.087  -17.800 -12.732 1.00 26.42  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 1.091   -18.186 -13.600 1.00 26.57  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 2.244   -17.406 -13.598 1.00 32.61  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 0.992   -19.251 -14.499 1.00 32.56  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 3.329   -17.742 -14.407 1.00 44.30  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 2.075   -19.574 -15.312 1.00 39.48  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 3.235   -18.820 -15.275 1.00 37.28  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -0.920  -16.405 -9.634  1.00 26.65  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -2.054  -16.028 -8.801  1.00 24.64  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -2.359  -14.541 -8.964  1.00 23.25  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -1.495  -13.726 -9.317  1.00 25.57  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -1.726  -16.331 -7.335  1.00 25.70  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -1.677  -17.802 -6.960  1.00 28.26  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -1.376  -17.792 -5.474  1.00 25.18  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -3.034  -18.444 -7.213  1.00 32.57  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -3.634  -14.176 -8.716  1.00 22.33  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -3.990  -12.764 -8.640  1.00 24.16  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -4.003  -12.286 -7.178  1.00 21.66  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -3.931  -13.120 -6.255  1.00 21.95  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -4.103  -10.958 -6.964  1.00 21.37  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -4.047  -10.320 -5.630  1.00 23.27  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -5.037  -10.828 -4.587  1.00 23.80  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -4.746  -10.807 -3.396  1.00 22.07  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -4.240  -8.836  -5.931  1.00 26.37  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -3.721  -8.703  -7.324  1.00 27.32  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -4.152  -9.962  -8.052  1.00 24.25  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -6.167  -11.376 -5.047  1.00 24.95  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -7.133  -11.924 -4.100  1.00 24.95  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -6.579  -13.075 -3.252  1.00 23.23  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -7.046  -13.331 -2.130  1.00 21.98  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -8.398  -12.428 -4.815  1.00 30.65  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -8.205  -13.738 -5.542  1.00 28.56  ? 56  LYS   A CG  1 
ATOM   443  C CD  . LYS   A 1 57 ? -9.542  -14.315 -5.999  1.00 37.64  ? 56  LYS   A CD  1 
ATOM   444  C CE  . LYS   A 1 57 ? -9.435  -15.552 -6.832  1.00 39.09  ? 56  LYS   A CE  1 
ATOM   445  N NZ  . LYS   A 1 57 ? -8.903  -16.678 -6.065  1.00 50.37  ? 56  LYS   A NZ  1 
ATOM   446  N N   . ASP   A 1 58 ? -5.492  -13.716 -3.745  1.00 23.28  ? 57  ASP   A N   1 
ATOM   447  C CA  . ASP   A 1 58 ? -4.933  -14.858 -3.061  1.00 22.55  ? 57  ASP   A CA  1 
ATOM   448  C C   . ASP   A 1 58 ? -3.583  -14.496 -2.417  1.00 23.02  ? 57  ASP   A C   1 
ATOM   449  O O   . ASP   A 1 58 ? -2.876  -15.408 -1.987  1.00 23.70  ? 57  ASP   A O   1 
ATOM   450  C CB  . ASP   A 1 58 ? -4.832  -15.998 -4.072  1.00 25.47  ? 57  ASP   A CB  1 
ATOM   451  C CG  . ASP   A 1 58 ? -6.183  -16.644 -4.372  1.00 31.21  ? 57  ASP   A CG  1 
ATOM   452  O OD1 . ASP   A 1 58 ? -6.968  -16.758 -3.400  1.00 32.56  ? 57  ASP   A OD1 1 
ATOM   453  O OD2 . ASP   A 1 58 ? -6.427  -17.058 -5.546  1.00 31.80  ? 57  ASP   A OD2 1 
ATOM   454  N N   . LEU   A 1 59 ? -3.224  -13.193 -2.392  1.00 21.71  ? 58  LEU   A N   1 
ATOM   455  C CA  . LEU   A 1 59 ? -1.896  -12.786 -1.911  1.00 19.79  ? 58  LEU   A CA  1 
ATOM   456  C C   . LEU   A 1 59 ? -2.051  -11.927 -0.644  1.00 19.83  ? 58  LEU   A C   1 
ATOM   457  O O   . LEU   A 1 59 ? -2.664  -10.854 -0.667  1.00 23.38  ? 58  LEU   A O   1 
ATOM   458  C CB  . LEU   A 1 59 ? -1.163  -12.035 -3.036  1.00 21.06  ? 58  LEU   A CB  1 
ATOM   459  C CG  . LEU   A 1 59 ? -1.085  -12.781 -4.370  1.00 22.75  ? 58  LEU   A CG  1 
ATOM   460  C CD1 . LEU   A 1 59 ? -0.345  -11.891 -5.346  1.00 22.42  ? 58  LEU   A CD1 1 
ATOM   461  C CD2 . LEU   A 1 59 ? -0.313  -14.097 -4.210  1.00 21.86  ? 58  LEU   A CD2 1 
ATOM   462  N N   . PHE   A 1 60 ? -1.490  -12.409 0.470   1.00 21.03  ? 59  PHE   A N   1 
ATOM   463  C CA  . PHE   A 1 60 ? -1.552  -11.708 1.755   1.00 22.06  ? 59  PHE   A CA  1 
ATOM   464  C C   . PHE   A 1 60 ? -0.158  -11.227 2.145   1.00 23.87  ? 59  PHE   A C   1 
ATOM   465  O O   . PHE   A 1 60 ? 0.755   -12.051 2.293   1.00 24.21  ? 59  PHE   A O   1 
ATOM   466  C CB  . PHE   A 1 60 ? -1.995  -12.745 2.780   1.00 22.44  ? 59  PHE   A CB  1 
ATOM   467  C CG  . PHE   A 1 60 ? -3.437  -13.156 2.507   1.00 21.63  ? 59  PHE   A CG  1 
ATOM   468  C CD1 . PHE   A 1 60 ? -3.746  -14.038 1.477   1.00 22.45  ? 59  PHE   A CD1 1 
ATOM   469  C CD2 . PHE   A 1 60 ? -4.442  -12.640 3.301   1.00 24.52  ? 59  PHE   A CD2 1 
ATOM   470  C CE1 . PHE   A 1 60 ? -5.065  -14.375 1.210   1.00 25.90  ? 59  PHE   A CE1 1 
ATOM   471  C CE2 . PHE   A 1 60 ? -5.759  -13.009 3.041   1.00 22.06  ? 59  PHE   A CE2 1 
ATOM   472  C CZ  . PHE   A 1 60 ? -6.046  -13.887 2.033   1.00 23.81  ? 59  PHE   A CZ  1 
ATOM   473  N N   . PRO   A 1 61 ? 0.056   -9.908  2.314   1.00 27.18  ? 60  PRO   A N   1 
ATOM   474  C CA  . PRO   A 1 61 ? 1.396   -9.407  2.672   1.00 26.09  ? 60  PRO   A CA  1 
ATOM   475  C C   . PRO   A 1 61 ? 1.969   -10.069 3.925   1.00 24.90  ? 60  PRO   A C   1 
ATOM   476  O O   . PRO   A 1 61 ? 1.295   -10.249 4.921   1.00 23.77  ? 60  PRO   A O   1 
ATOM   477  C CB  . PRO   A 1 61 ? 1.165   -7.890  2.765   1.00 27.00  ? 60  PRO   A CB  1 
ATOM   478  C CG  . PRO   A 1 61 ? 0.022   -7.669  1.723   1.00 32.51  ? 60  PRO   A CG  1 
ATOM   479  C CD  . PRO   A 1 61 ? -0.909  -8.822  2.070   1.00 31.15  ? 60  PRO   A CD  1 
ATOM   480  N N   . TYR   A 1 62 ? 3.261   -10.467 3.879   1.00 24.83  ? 61  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 62 ? 3.815   -11.373 4.871   1.00 24.46  ? 61  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 62 ? 3.836   -10.709 6.264   1.00 25.29  ? 61  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 62 ? 3.539   -11.377 7.254   1.00 27.99  ? 61  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 62 ? 5.253   -11.708 4.431   1.00 25.20  ? 61  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 62 ? 6.032   -12.494 5.479   1.00 24.08  ? 61  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 62 ? 5.747   -13.828 5.773   1.00 24.94  ? 61  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 62 ? 7.080   -11.871 6.155   1.00 29.06  ? 61  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 62 ? 6.482   -14.542 6.722   1.00 27.39  ? 61  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 62 ? 7.804   -12.572 7.098   1.00 29.70  ? 61  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 62 ? 7.511   -13.886 7.381   1.00 30.45  ? 61  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 62 ? 8.296   -14.476 8.345   1.00 30.08  ? 61  TYR   A OH  1 
ATOM   492  N N   . ASP   A 1 63 ? 4.251   -9.435  6.337   1.00 26.91  ? 62  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 63 ? 4.450   -8.806  7.637   1.00 33.74  ? 62  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 63 ? 3.123   -8.697  8.384   1.00 29.59  ? 62  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 63 ? 3.051   -9.101  9.538   1.00 40.02  ? 62  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 63 ? 5.343   -7.573  7.584   1.00 38.37  ? 62  ASP   A CB  1 
ATOM   497  C CG  . ASP   A 1 63 ? 6.462   -7.667  8.610   1.00 57.36  ? 62  ASP   A CG  1 
ATOM   498  O OD1 . ASP   A 1 63 ? 6.139   -7.655  9.823   1.00 54.97  ? 62  ASP   A OD1 1 
ATOM   499  O OD2 . ASP   A 1 63 ? 7.632   -7.855  8.191   1.00 64.93  ? 62  ASP   A OD2 1 
ATOM   500  N N   . LYS   A 1 64 ? 2.068   -8.258  7.693   1.00 36.14  ? 63  LYS   A N   1 
ATOM   501  C CA  . LYS   A 1 64 ? 0.749   -8.126  8.304   1.00 37.01  ? 63  LYS   A CA  1 
ATOM   502  C C   . LYS   A 1 64 ? 0.212   -9.475  8.780   1.00 36.43  ? 63  LYS   A C   1 
ATOM   503  O O   . LYS   A 1 64 ? -0.510  -9.519  9.782   1.00 32.77  ? 63  LYS   A O   1 
ATOM   504  C CB  . LYS   A 1 64 ? -0.259  -7.517  7.312   1.00 35.98  ? 63  LYS   A CB  1 
ATOM   505  C CG  . LYS   A 1 64 ? -1.683  -7.144  7.806   1.00 43.73  ? 63  LYS   A CG  1 
ATOM   506  C CD  . LYS   A 1 64 ? -2.642  -6.712  6.695   1.00 41.84  ? 63  LYS   A CD  1 
ATOM   507  C CE  . LYS   A 1 64 ? -3.769  -5.744  6.978   1.00 47.70  ? 63  LYS   A CE  1 
ATOM   508  N NZ  . LYS   A 1 64 ? -4.457  -5.751  8.270   1.00 47.22  ? 63  LYS   A NZ  1 
ATOM   509  N N   . SER   A 1 65 ? 0.516   -10.561 8.045   1.00 31.08  ? 64  SER   A N   1 
ATOM   510  C CA  . SER   A 1 65 ? -0.211  -11.821 8.138   1.00 28.46  ? 64  SER   A CA  1 
ATOM   511  C C   . SER   A 1 65 ? 0.569   -12.898 8.897   1.00 26.80  ? 64  SER   A C   1 
ATOM   512  O O   . SER   A 1 65 ? 0.044   -13.981 9.108   1.00 29.63  ? 64  SER   A O   1 
ATOM   513  C CB  . SER   A 1 65 ? -0.559  -12.352 6.750   1.00 28.60  ? 64  SER   A CB  1 
ATOM   514  O OG  . SER   A 1 65 ? -1.294  -11.340 6.055   1.00 39.86  ? 64  SER   A OG  1 
ATOM   515  N N   . LYS   A 1 66 ? 1.847   -12.656 9.201   1.00 28.02  ? 65  LYS   A N   1 
ATOM   516  C CA  . LYS   A 1 66 ? 2.675   -13.742 9.720   1.00 30.22  ? 65  LYS   A CA  1 
ATOM   517  C C   . LYS   A 1 66 ? 2.244   -14.252 11.103  1.00 30.48  ? 65  LYS   A C   1 
ATOM   518  O O   . LYS   A 1 66 ? 2.442   -15.429 11.421  1.00 32.59  ? 65  LYS   A O   1 
ATOM   519  C CB  . LYS   A 1 66 ? 4.157   -13.353 9.648   1.00 33.93  ? 65  LYS   A CB  1 
ATOM   520  C CG  . LYS   A 1 66 ? 4.612   -12.279 10.598  1.00 35.32  ? 65  LYS   A CG  1 
ATOM   521  C CD  . LYS   A 1 66 ? 6.129   -12.208 10.460  1.00 46.20  ? 65  LYS   A CD  1 
ATOM   522  C CE  . LYS   A 1 66 ? 6.739   -11.269 11.459  1.00 54.34  ? 65  LYS   A CE  1 
ATOM   523  N NZ  . LYS   A 1 66 ? 6.269   -9.892  11.279  1.00 59.43  ? 65  LYS   A NZ  1 
ATOM   524  N N   A ASP   A 1 67 ? 1.665   -13.373 11.931  0.50 33.22  ? 66  ASP   A N   1 
ATOM   525  N N   B ASP   A 1 67 ? 1.706   -13.353 11.936  0.50 33.00  ? 66  ASP   A N   1 
ATOM   526  C CA  A ASP   A 1 67 ? 1.199   -13.783 13.248  0.50 35.48  ? 66  ASP   A CA  1 
ATOM   527  C CA  B ASP   A 1 67 ? 1.194   -13.769 13.231  0.50 34.90  ? 66  ASP   A CA  1 
ATOM   528  C C   A ASP   A 1 67 ? 0.036   -14.765 13.122  0.50 36.38  ? 66  ASP   A C   1 
ATOM   529  C C   B ASP   A 1 67 ? 0.161   -14.872 13.019  0.50 35.12  ? 66  ASP   A C   1 
ATOM   530  O O   A ASP   A 1 67 ? -0.185  -15.589 14.000  0.50 39.73  ? 66  ASP   A O   1 
ATOM   531  O O   B ASP   A 1 67 ? 0.200   -15.898 13.692  0.50 35.02  ? 66  ASP   A O   1 
ATOM   532  C CB  A ASP   A 1 67 ? 0.807   -12.600 14.117  0.50 38.82  ? 66  ASP   A CB  1 
ATOM   533  C CB  B ASP   A 1 67 ? 0.649   -12.598 14.036  0.50 39.04  ? 66  ASP   A CB  1 
ATOM   534  C CG  A ASP   A 1 67 ? 1.949   -11.811 14.739  0.50 41.45  ? 66  ASP   A CG  1 
ATOM   535  C CG  B ASP   A 1 67 ? 0.066   -12.957 15.396  0.50 40.84  ? 66  ASP   A CG  1 
ATOM   536  O OD1 A ASP   A 1 67 ? 3.118   -12.262 14.640  0.50 42.28  ? 66  ASP   A OD1 1 
ATOM   537  O OD1 B ASP   A 1 67 ? 0.863   -13.233 16.320  0.50 43.67  ? 66  ASP   A OD1 1 
ATOM   538  O OD2 A ASP   A 1 67 ? 1.658   -10.749 15.317  0.50 43.03  ? 66  ASP   A OD2 1 
ATOM   539  O OD2 B ASP   A 1 67 ? -1.177  -12.970 15.513  0.50 44.28  ? 66  ASP   A OD2 1 
ATOM   540  N N   . LYS   A 1 68 ? -0.711  -14.686 12.021  1.00 31.63  ? 67  LYS   A N   1 
ATOM   541  C CA  . LYS   A 1 68 ? -1.831  -15.588 11.826  1.00 32.01  ? 67  LYS   A CA  1 
ATOM   542  C C   . LYS   A 1 68 ? -1.416  -16.842 11.066  1.00 30.99  ? 67  LYS   A C   1 
ATOM   543  O O   . LYS   A 1 68 ? -1.939  -17.931 11.316  1.00 35.36  ? 67  LYS   A O   1 
ATOM   544  C CB  . LYS   A 1 68 ? -2.874  -14.812 11.019  1.00 32.95  ? 67  LYS   A CB  1 
ATOM   545  C CG  . LYS   A 1 68 ? -4.165  -15.583 10.777  1.00 36.28  ? 67  LYS   A CG  1 
ATOM   546  C CD  . LYS   A 1 68 ? -5.197  -14.734 10.035  1.00 41.12  ? 67  LYS   A CD  1 
ATOM   547  C CE  . LYS   A 1 68 ? -6.543  -15.388 9.973   1.00 40.85  ? 67  LYS   A CE  1 
ATOM   548  N NZ  . LYS   A 1 68 ? -7.484  -14.597 9.171   1.00 40.41  ? 67  LYS   A NZ  1 
ATOM   549  N N   . TYR   A 1 69 ? -0.554  -16.682 10.049  1.00 27.75  ? 68  TYR   A N   1 
ATOM   550  C CA  . TYR   A 1 69 ? -0.331  -17.784 9.113   1.00 26.09  ? 68  TYR   A CA  1 
ATOM   551  C C   . TYR   A 1 69 ? 1.062   -18.411 9.275   1.00 27.03  ? 68  TYR   A C   1 
ATOM   552  O O   . TYR   A 1 69 ? 1.342   -19.429 8.658   1.00 27.98  ? 68  TYR   A O   1 
ATOM   553  C CB  . TYR   A 1 69 ? -0.483  -17.293 7.658   1.00 25.59  ? 68  TYR   A CB  1 
ATOM   554  C CG  . TYR   A 1 69 ? -1.885  -16.830 7.268   1.00 29.07  ? 68  TYR   A CG  1 
ATOM   555  C CD1 . TYR   A 1 69 ? -3.023  -17.544 7.636   1.00 29.40  ? 68  TYR   A CD1 1 
ATOM   556  C CD2 . TYR   A 1 69 ? -2.062  -15.681 6.496   1.00 29.86  ? 68  TYR   A CD2 1 
ATOM   557  C CE1 . TYR   A 1 69 ? -4.292  -17.139 7.240   1.00 29.69  ? 68  TYR   A CE1 1 
ATOM   558  C CE2 . TYR   A 1 69 ? -3.327  -15.242 6.122   1.00 31.41  ? 68  TYR   A CE2 1 
ATOM   559  C CZ  . TYR   A 1 69 ? -4.442  -15.968 6.507   1.00 31.81  ? 68  TYR   A CZ  1 
ATOM   560  O OH  . TYR   A 1 69 ? -5.682  -15.530 6.118   1.00 29.62  ? 68  TYR   A OH  1 
ATOM   561  N N   . GLY   A 1 70 ? 1.906   -17.811 10.100  1.00 32.09  ? 69  GLY   A N   1 
ATOM   562  C CA  . GLY   A 1 70 ? 3.317   -18.176 10.173  1.00 29.17  ? 69  GLY   A CA  1 
ATOM   563  C C   . GLY   A 1 70 ? 3.625   -19.191 11.279  1.00 31.91  ? 69  GLY   A C   1 
ATOM   564  O O   . GLY   A 1 70 ? 4.629   -19.054 11.954  1.00 43.10  ? 69  GLY   A O   1 
ATOM   565  N N   . LYS   A 1 71 ? 2.809   -20.241 11.380  1.00 35.66  ? 70  LYS   A N   1 
ATOM   566  C CA  . LYS   A 1 71 ? 2.965   -21.280 12.388  1.00 40.70  ? 70  LYS   A CA  1 
ATOM   567  C C   . LYS   A 1 71 ? 3.245   -22.610 11.693  1.00 34.91  ? 70  LYS   A C   1 
ATOM   568  O O   . LYS   A 1 71 ? 2.809   -22.839 10.567  1.00 35.49  ? 70  LYS   A O   1 
ATOM   569  C CB  . LYS   A 1 71 ? 1.687   -21.420 13.229  1.00 40.18  ? 70  LYS   A CB  1 
ATOM   570  C CG  . LYS   A 1 71 ? 1.450   -20.231 14.142  1.00 42.96  ? 70  LYS   A CG  1 
ATOM   571  C CD  . LYS   A 1 71 ? 0.469   -20.556 15.258  1.00 51.49  ? 70  LYS   A CD  1 
ATOM   572  N N   . PRO   A 1 72 ? 3.984   -23.548 12.333  1.00 38.23  ? 71  PRO   A N   1 
ATOM   573  C CA  . PRO   A 1 72 ? 4.270   -24.834 11.696  1.00 37.87  ? 71  PRO   A CA  1 
ATOM   574  C C   . PRO   A 1 72 ? 2.994   -25.543 11.277  1.00 41.77  ? 71  PRO   A C   1 
ATOM   575  O O   . PRO   A 1 72 ? 1.946   -25.328 11.877  1.00 50.94  ? 71  PRO   A O   1 
ATOM   576  C CB  . PRO   A 1 72 ? 5.011   -25.605 12.811  1.00 39.45  ? 71  PRO   A CB  1 
ATOM   577  C CG  . PRO   A 1 72 ? 5.662   -24.498 13.623  1.00 48.16  ? 71  PRO   A CG  1 
ATOM   578  C CD  . PRO   A 1 72 ? 4.624   -23.380 13.647  1.00 45.00  ? 71  PRO   A CD  1 
ATOM   579  N N   . ASN   A 1 73 ? 3.125   -26.370 10.240  1.00 42.93  ? 72  ASN   A N   1 
ATOM   580  C CA  . ASN   A 1 73 ? 2.057   -27.070 9.552   1.00 48.90  ? 72  ASN   A CA  1 
ATOM   581  C C   . ASN   A 1 73 ? 2.634   -28.420 9.151   1.00 57.53  ? 72  ASN   A C   1 
ATOM   582  O O   . ASN   A 1 73 ? 3.832   -28.519 8.880   1.00 57.40  ? 72  ASN   A O   1 
ATOM   583  C CB  . ASN   A 1 73 ? 1.675   -26.326 8.274   1.00 47.60  ? 72  ASN   A CB  1 
ATOM   584  C CG  . ASN   A 1 73 ? 0.326   -26.716 7.723   1.00 56.19  ? 72  ASN   A CG  1 
ATOM   585  O OD1 . ASN   A 1 73 ? 0.240   -27.374 6.682   1.00 53.37  ? 72  ASN   A OD1 1 
ATOM   586  N ND2 . ASN   A 1 73 ? -0.742  -26.302 8.389   1.00 68.45  ? 72  ASN   A ND2 1 
ATOM   587  N N   . LYS   A 1 74 ? 1.777   -29.442 9.100   1.00 53.24  ? 73  LYS   A N   1 
ATOM   588  C CA  . LYS   A 1 74 ? 2.192   -30.798 8.790   1.00 51.31  ? 73  LYS   A CA  1 
ATOM   589  C C   . LYS   A 1 74 ? 2.569   -30.922 7.311   1.00 47.48  ? 73  LYS   A C   1 
ATOM   590  O O   . LYS   A 1 74 ? 3.330   -31.810 6.933   1.00 43.89  ? 73  LYS   A O   1 
ATOM   591  C CB  . LYS   A 1 74 ? 1.086   -31.748 9.286   1.00 48.57  ? 73  LYS   A CB  1 
ATOM   592  C CG  . LYS   A 1 74 ? -0.040  -32.054 8.301   1.00 49.86  ? 73  LYS   A CG  1 
ATOM   593  N N   . ARG   A 1 75 ? 2.063   -30.021 6.458   1.00 42.99  ? 74  ARG   A N   1 
ATOM   594  C CA  . ARG   A 1 75 ? 2.193   -30.208 5.019   1.00 42.86  ? 74  ARG   A CA  1 
ATOM   595  C C   . ARG   A 1 75 ? 3.656   -30.169 4.565   1.00 40.64  ? 74  ARG   A C   1 
ATOM   596  O O   . ARG   A 1 75 ? 4.465   -29.406 5.102   1.00 38.39  ? 74  ARG   A O   1 
ATOM   597  C CB  . ARG   A 1 75 ? 1.326   -29.219 4.230   1.00 41.86  ? 74  ARG   A CB  1 
ATOM   598  C CG  . ARG   A 1 75 ? -0.128  -29.372 4.647   1.00 53.23  ? 74  ARG   A CG  1 
ATOM   599  C CD  . ARG   A 1 75 ? -0.789  -30.612 4.055   1.00 57.23  ? 74  ARG   A CD  1 
ATOM   600  N NE  . ARG   A 1 75 ? -1.691  -30.240 2.960   1.00 64.40  ? 74  ARG   A NE  1 
ATOM   601  C CZ  . ARG   A 1 75 ? -2.807  -29.532 3.142   1.00 66.39  ? 74  ARG   A CZ  1 
ATOM   602  N NH1 . ARG   A 1 75 ? -3.501  -29.120 2.095   1.00 68.35  ? 74  ARG   A NH1 1 
ATOM   603  N NH2 . ARG   A 1 75 ? -3.212  -29.223 4.365   1.00 63.91  ? 74  ARG   A NH2 1 
ATOM   604  N N   . LYS   A 1 76 ? 3.943   -30.981 3.535   1.00 39.26  ? 75  LYS   A N   1 
ATOM   605  C CA  . LYS   A 1 76 ? 5.272   -31.190 2.982   1.00 38.38  ? 75  LYS   A CA  1 
ATOM   606  C C   . LYS   A 1 76 ? 5.853   -29.866 2.484   1.00 35.62  ? 75  LYS   A C   1 
ATOM   607  O O   . LYS   A 1 76 ? 5.308   -29.255 1.558   1.00 31.31  ? 75  LYS   A O   1 
ATOM   608  C CB  . LYS   A 1 76 ? 5.157   -32.054 1.723   1.00 41.57  ? 75  LYS   A CB  1 
ATOM   609  C CG  . LYS   A 1 76 ? 6.461   -32.533 1.112   1.00 46.91  ? 75  LYS   A CG  1 
ATOM   610  C CD  . LYS   A 1 76 ? 6.271   -33.439 -0.099  1.00 49.25  ? 75  LYS   A CD  1 
ATOM   611  C CE  . LYS   A 1 76 ? 7.574   -34.011 -0.582  1.00 58.43  ? 75  LYS   A CE  1 
ATOM   612  N N   . GLY   A 1 77 ? 6.998   -29.463 3.060   1.00 36.14  ? 76  GLY   A N   1 
ATOM   613  C CA  . GLY   A 1 77 ? 7.681   -28.279 2.562   1.00 32.99  ? 76  GLY   A CA  1 
ATOM   614  C C   . GLY   A 1 77 ? 7.336   -27.010 3.352   1.00 30.00  ? 76  GLY   A C   1 
ATOM   615  O O   . GLY   A 1 77 ? 8.051   -26.026 3.242   1.00 30.93  ? 76  GLY   A O   1 
ATOM   616  N N   . PHE   A 1 78 ? 6.259   -27.023 4.136   1.00 29.96  ? 77  PHE   A N   1 
ATOM   617  C CA  . PHE   A 1 78 ? 5.810   -25.820 4.818   1.00 32.32  ? 77  PHE   A CA  1 
ATOM   618  C C   . PHE   A 1 78 ? 6.851   -25.243 5.790   1.00 34.08  ? 77  PHE   A C   1 
ATOM   619  O O   . PHE   A 1 78 ? 7.155   -24.046 5.764   1.00 29.36  ? 77  PHE   A O   1 
ATOM   620  C CB  . PHE   A 1 78 ? 4.436   -26.089 5.447   1.00 30.49  ? 77  PHE   A CB  1 
ATOM   621  C CG  . PHE   A 1 78 ? 3.722   -24.808 5.844   1.00 33.36  ? 77  PHE   A CG  1 
ATOM   622  C CD1 . PHE   A 1 78 ? 4.025   -24.145 7.032   1.00 34.06  ? 77  PHE   A CD1 1 
ATOM   623  C CD2 . PHE   A 1 78 ? 2.774   -24.245 4.979   1.00 31.64  ? 77  PHE   A CD2 1 
ATOM   624  C CE1 . PHE   A 1 78 ? 3.384   -22.954 7.374   1.00 34.09  ? 77  PHE   A CE1 1 
ATOM   625  C CE2 . PHE   A 1 78 ? 2.126   -23.066 5.328   1.00 28.83  ? 77  PHE   A CE2 1 
ATOM   626  C CZ  . PHE   A 1 78 ? 2.438   -22.419 6.512   1.00 27.94  ? 77  PHE   A CZ  1 
ATOM   627  N N   . ASN   A 1 79 ? 7.368   -26.060 6.714   1.00 29.68  ? 78  ASN   A N   1 
ATOM   628  C CA  . ASN   A 1 79 ? 8.293   -25.556 7.727   1.00 30.57  ? 78  ASN   A CA  1 
ATOM   629  C C   . ASN   A 1 79 ? 9.616   -25.077 7.107   1.00 28.53  ? 78  ASN   A C   1 
ATOM   630  O O   . ASN   A 1 79 ? 10.215  -24.093 7.577   1.00 28.09  ? 78  ASN   A O   1 
ATOM   631  C CB  . ASN   A 1 79 ? 8.480   -26.585 8.838   1.00 31.70  ? 78  ASN   A CB  1 
ATOM   632  C CG  . ASN   A 1 79 ? 7.164   -26.874 9.531   1.00 39.12  ? 78  ASN   A CG  1 
ATOM   633  O OD1 . ASN   A 1 79 ? 6.256   -26.030 9.529   1.00 33.35  ? 78  ASN   A OD1 1 
ATOM   634  N ND2 . ASN   A 1 79 ? 7.045   -28.050 10.139  1.00 31.20  ? 78  ASN   A ND2 1 
ATOM   635  N N   . GLU   A 1 80 ? 10.088  -25.821 6.092   1.00 28.72  ? 79  GLU   A N   1 
ATOM   636  C CA  . GLU   A 1 80 ? 11.245  -25.387 5.320   1.00 28.24  ? 79  GLU   A CA  1 
ATOM   637  C C   . GLU   A 1 80 ? 10.914  -24.016 4.743   1.00 26.07  ? 79  GLU   A C   1 
ATOM   638  O O   . GLU   A 1 80 ? 11.722  -23.075 4.789   1.00 24.79  ? 79  GLU   A O   1 
ATOM   639  C CB  . GLU   A 1 80 ? 11.691  -26.345 4.217   1.00 29.99  ? 79  GLU   A CB  1 
ATOM   640  C CG  . GLU   A 1 80 ? 12.969  -25.879 3.517   1.00 35.12  ? 79  GLU   A CG  1 
ATOM   641  C CD  . GLU   A 1 80 ? 13.568  -26.944 2.610   1.00 42.76  ? 79  GLU   A CD  1 
ATOM   642  O OE1 . GLU   A 1 80 ? 12.980  -28.043 2.521   1.00 47.57  ? 79  GLU   A OE1 1 
ATOM   643  O OE2 . GLU   A 1 80 ? 14.606  -26.683 1.989   1.00 37.24  ? 79  GLU   A OE2 1 
ATOM   644  N N   . GLY   A 1 81 ? 9.688   -23.897 4.221   1.00 24.71  ? 80  GLY   A N   1 
ATOM   645  C CA  . GLY   A 1 81 ? 9.261   -22.621 3.650   1.00 28.46  ? 80  GLY   A CA  1 
ATOM   646  C C   . GLY   A 1 81 ? 9.294   -21.474 4.668   1.00 23.02  ? 80  GLY   A C   1 
ATOM   647  O O   . GLY   A 1 81 ? 9.598   -20.318 4.326   1.00 22.85  ? 80  GLY   A O   1 
ATOM   648  N N   . LEU   A 1 82 ? 8.887   -21.760 5.919   1.00 22.10  ? 81  LEU   A N   1 
ATOM   649  C CA  . LEU   A 1 82 ? 8.926   -20.744 6.961   1.00 24.49  ? 81  LEU   A CA  1 
ATOM   650  C C   . LEU   A 1 82 ? 10.352  -20.253 7.224   1.00 24.46  ? 81  LEU   A C   1 
ATOM   651  O O   . LEU   A 1 82 ? 10.540  -19.073 7.469   1.00 22.07  ? 81  LEU   A O   1 
ATOM   652  C CB  . LEU   A 1 82 ? 8.235   -21.136 8.269   1.00 26.37  ? 81  LEU   A CB  1 
ATOM   653  C CG  . LEU   A 1 82 ? 6.744   -21.484 8.139   1.00 30.74  ? 81  LEU   A CG  1 
ATOM   654  C CD1 . LEU   A 1 82 ? 6.326   -22.077 9.471   1.00 31.55  ? 81  LEU   A CD1 1 
ATOM   655  C CD2 . LEU   A 1 82 ? 5.859   -20.292 7.843   1.00 32.36  ? 81  LEU   A CD2 1 
ATOM   656  N N   . TRP   A 1 83 ? 11.337  -21.163 7.177   1.00 24.70  ? 82  TRP   A N   1 
ATOM   657  C CA  . TRP   A 1 83 ? 12.708  -20.747 7.443   1.00 25.05  ? 82  TRP   A CA  1 
ATOM   658  C C   . TRP   A 1 83 ? 13.161  -19.839 6.304   1.00 22.59  ? 82  TRP   A C   1 
ATOM   659  O O   . TRP   A 1 83 ? 13.772  -18.808 6.526   1.00 24.26  ? 82  TRP   A O   1 
ATOM   660  C CB  . TRP   A 1 83 ? 13.615  -21.989 7.590   1.00 23.18  ? 82  TRP   A CB  1 
ATOM   661  C CG  . TRP   A 1 83 ? 15.066  -21.669 7.857   1.00 24.67  ? 82  TRP   A CG  1 
ATOM   662  C CD1 . TRP   A 1 83 ? 15.704  -21.553 9.063   1.00 27.74  ? 82  TRP   A CD1 1 
ATOM   663  C CD2 . TRP   A 1 83 ? 16.040  -21.376 6.844   1.00 25.37  ? 82  TRP   A CD2 1 
ATOM   664  N NE1 . TRP   A 1 83 ? 17.018  -21.224 8.857   1.00 28.41  ? 82  TRP   A NE1 1 
ATOM   665  C CE2 . TRP   A 1 83 ? 17.241  -21.087 7.509   1.00 28.49  ? 82  TRP   A CE2 1 
ATOM   666  C CE3 . TRP   A 1 83 ? 15.979  -21.321 5.446   1.00 27.25  ? 82  TRP   A CE3 1 
ATOM   667  C CZ2 . TRP   A 1 83 ? 18.401  -20.783 6.802   1.00 25.39  ? 82  TRP   A CZ2 1 
ATOM   668  C CZ3 . TRP   A 1 83 ? 17.119  -20.972 4.752   1.00 30.69  ? 82  TRP   A CZ3 1 
ATOM   669  C CH2 . TRP   A 1 83 ? 18.315  -20.715 5.432   1.00 27.63  ? 82  TRP   A CH2 1 
ATOM   670  N N   . GLU   A 1 84 ? 12.836  -20.216 5.067   1.00 22.12  ? 83  GLU   A N   1 
ATOM   671  C CA  . GLU   A 1 84 ? 13.337  -19.493 3.923   1.00 20.03  ? 83  GLU   A CA  1 
ATOM   672  C C   . GLU   A 1 84 ? 12.818  -18.056 3.947   1.00 24.02  ? 83  GLU   A C   1 
ATOM   673  O O   . GLU   A 1 84 ? 13.549  -17.098 3.734   1.00 21.73  ? 83  GLU   A O   1 
ATOM   674  C CB  . GLU   A 1 84 ? 12.907  -20.200 2.640   1.00 20.37  ? 83  GLU   A CB  1 
ATOM   675  C CG  . GLU   A 1 84 ? 13.581  -21.560 2.483   1.00 21.20  ? 83  GLU   A CG  1 
ATOM   676  C CD  . GLU   A 1 84 ? 13.202  -22.316 1.192   1.00 26.68  ? 83  GLU   A CD  1 
ATOM   677  O OE1 . GLU   A 1 84 ? 12.278  -21.895 0.473   1.00 28.67  ? 83  GLU   A OE1 1 
ATOM   678  O OE2 . GLU   A 1 84 ? 13.833  -23.355 0.872   1.00 29.36  ? 83  GLU   A OE2 1 
ATOM   679  N N   . ILE   A 1 85 ? 11.500  -17.897 4.145   1.00 21.29  ? 84  ILE   A N   1 
ATOM   680  C CA  . ILE   A 1 85 ? 10.950  -16.556 4.033   1.00 22.84  ? 84  ILE   A CA  1 
ATOM   681  C C   . ILE   A 1 85 ? 11.479  -15.657 5.150   1.00 21.24  ? 84  ILE   A C   1 
ATOM   682  O O   . ILE   A 1 85 ? 11.612  -14.459 4.918   1.00 22.33  ? 84  ILE   A O   1 
ATOM   683  C CB  . ILE   A 1 85 ? 9.409   -16.591 4.032   1.00 19.63  ? 84  ILE   A CB  1 
ATOM   684  C CG1 . ILE   A 1 85 ? 8.830   -15.262 3.507   1.00 18.65  ? 84  ILE   A CG1 1 
ATOM   685  C CG2 . ILE   A 1 85 ? 8.884   -16.935 5.436   1.00 22.48  ? 84  ILE   A CG2 1 
ATOM   686  C CD1 . ILE   A 1 85 ? 7.332   -15.350 3.091   1.00 18.94  ? 84  ILE   A CD1 1 
ATOM   687  N N   . GLN   A 1 86 ? 11.776  -16.221 6.344   1.00 22.16  ? 85  GLN   A N   1 
ATOM   688  C CA  . GLN   A 1 86 ? 12.342  -15.448 7.463   1.00 22.87  ? 85  GLN   A CA  1 
ATOM   689  C C   . GLN   A 1 86 ? 13.835  -15.185 7.295   1.00 26.02  ? 85  GLN   A C   1 
ATOM   690  O O   . GLN   A 1 86 ? 14.281  -14.090 7.665   1.00 27.67  ? 85  GLN   A O   1 
ATOM   691  C CB  . GLN   A 1 86 ? 12.050  -16.155 8.797   1.00 26.53  ? 85  GLN   A CB  1 
ATOM   692  C CG  . GLN   A 1 86 ? 12.435  -15.350 10.035  1.00 36.38  ? 85  GLN   A CG  1 
ATOM   693  C CD  . GLN   A 1 86 ? 11.901  -15.949 11.321  1.00 40.92  ? 85  GLN   A CD  1 
ATOM   694  O OE1 . GLN   A 1 86 ? 11.774  -17.178 11.461  1.00 39.60  ? 85  GLN   A OE1 1 
ATOM   695  N NE2 . GLN   A 1 86 ? 11.605  -15.077 12.282  1.00 43.90  ? 85  GLN   A NE2 1 
ATOM   696  N N   . ASN   A 1 87 ? 14.578  -16.179 6.789   1.00 21.77  ? 86  ASN   A N   1 
ATOM   697  C CA  . ASN   A 1 87 ? 16.044  -16.206 6.836   1.00 23.05  ? 86  ASN   A CA  1 
ATOM   698  C C   . ASN   A 1 87 ? 16.761  -15.825 5.540   1.00 25.38  ? 86  ASN   A C   1 
ATOM   699  O O   . ASN   A 1 87 ? 17.882  -15.253 5.587   1.00 26.43  ? 86  ASN   A O   1 
ATOM   700  C CB  . ASN   A 1 87 ? 16.535  -17.509 7.465   1.00 26.29  ? 86  ASN   A CB  1 
ATOM   701  C CG  . ASN   A 1 87 ? 16.043  -17.570 8.892   1.00 25.93  ? 86  ASN   A CG  1 
ATOM   702  O OD1 . ASN   A 1 87 ? 16.411  -16.692 9.687   1.00 29.67  ? 86  ASN   A OD1 1 
ATOM   703  N ND2 . ASN   A 1 87 ? 15.120  -18.479 9.211   1.00 26.22  ? 86  ASN   A ND2 1 
ATOM   704  N N   . ASN   A 1 88 ? 16.209  -16.181 4.372   1.00 24.02  ? 87  ASN   A N   1 
ATOM   705  C CA  . ASN   A 1 88 ? 16.853  -15.817 3.118   1.00 25.09  ? 87  ASN   A CA  1 
ATOM   706  C C   . ASN   A 1 88 ? 15.783  -15.767 2.010   1.00 22.94  ? 87  ASN   A C   1 
ATOM   707  O O   . ASN   A 1 88 ? 15.819  -16.531 1.043   1.00 24.20  ? 87  ASN   A O   1 
ATOM   708  C CB  . ASN   A 1 88 ? 17.991  -16.791 2.782   1.00 26.70  ? 87  ASN   A CB  1 
ATOM   709  C CG  . ASN   A 1 88 ? 19.040  -16.190 1.876   1.00 28.98  ? 87  ASN   A CG  1 
ATOM   710  O OD1 . ASN   A 1 88 ? 18.782  -15.224 1.158   1.00 24.16  ? 87  ASN   A OD1 1 
ATOM   711  N ND2 . ASN   A 1 88 ? 20.247  -16.753 1.867   1.00 29.37  ? 87  ASN   A ND2 1 
ATOM   712  N N   . PRO   A 1 89 ? 14.847  -14.799 2.087   1.00 22.74  ? 88  PRO   A N   1 
ATOM   713  C CA  . PRO   A 1 89 ? 13.701  -14.744 1.170   1.00 22.41  ? 88  PRO   A CA  1 
ATOM   714  C C   . PRO   A 1 89 ? 14.030  -14.338 -0.263  1.00 25.57  ? 88  PRO   A C   1 
ATOM   715  O O   . PRO   A 1 89 ? 13.271  -14.637 -1.162  1.00 21.42  ? 88  PRO   A O   1 
ATOM   716  C CB  . PRO   A 1 89 ? 12.764  -13.754 1.842   1.00 21.07  ? 88  PRO   A CB  1 
ATOM   717  C CG  . PRO   A 1 89 ? 13.650  -12.844 2.612   1.00 20.54  ? 88  PRO   A CG  1 
ATOM   718  C CD  . PRO   A 1 89 ? 14.782  -13.765 3.134   1.00 20.06  ? 88  PRO   A CD  1 
ATOM   719  N N   . HIS   A 1 90 ? 15.230  -13.788 -0.514  1.00 19.57  ? 89  HIS   A N   1 
ATOM   720  C CA  . HIS   A 1 90 ? 15.548  -13.293 -1.850  1.00 19.54  ? 89  HIS   A CA  1 
ATOM   721  C C   . HIS   A 1 90 ? 16.698  -14.110 -2.489  1.00 23.29  ? 89  HIS   A C   1 
ATOM   722  O O   . HIS   A 1 90 ? 17.239  -13.677 -3.527  1.00 23.62  ? 89  HIS   A O   1 
ATOM   723  C CB  . HIS   A 1 90 ? 16.035  -11.836 -1.690  1.00 21.53  ? 89  HIS   A CB  1 
ATOM   724  C CG  . HIS   A 1 90 ? 15.000  -10.935 -1.087  1.00 21.41  ? 89  HIS   A CG  1 
ATOM   725  N ND1 . HIS   A 1 90 ? 13.754  -10.875 -1.702  1.00 21.87  ? 89  HIS   A ND1 1 
ATOM   726  C CD2 . HIS   A 1 90 ? 14.914  -10.172 0.043   1.00 21.26  ? 89  HIS   A CD2 1 
ATOM   727  C CE1 . HIS   A 1 90 ? 12.984  -10.039 -1.012  1.00 21.61  ? 89  HIS   A CE1 1 
ATOM   728  N NE2 . HIS   A 1 90 ? 13.666  -9.585  0.036   1.00 24.15  ? 89  HIS   A NE2 1 
ATOM   729  N N   . ALA   A 1 91 ? 16.966  -15.311 -1.936  1.00 23.42  ? 90  ALA   A N   1 
ATOM   730  C CA  . ALA   A 1 91 ? 18.041  -16.172 -2.429  1.00 24.74  ? 90  ALA   A CA  1 
ATOM   731  C C   . ALA   A 1 91 ? 17.604  -16.903 -3.690  1.00 28.72  ? 90  ALA   A C   1 
ATOM   732  O O   . ALA   A 1 91 ? 16.420  -17.066 -3.957  1.00 25.99  ? 90  ALA   A O   1 
ATOM   733  C CB  . ALA   A 1 91 ? 18.486  -17.159 -1.384  1.00 26.03  ? 90  ALA   A CB  1 
ATOM   734  N N   . SER   A 1 92 ? 18.604  -17.345 -4.459  1.00 25.30  ? 91  SER   A N   1 
ATOM   735  C CA  . SER   A 1 92 ? 18.325  -18.267 -5.550  1.00 31.33  ? 91  SER   A CA  1 
ATOM   736  C C   . SER   A 1 92 ? 18.043  -19.661 -4.983  1.00 30.56  ? 91  SER   A C   1 
ATOM   737  O O   . SER   A 1 92 ? 18.864  -20.209 -4.250  1.00 35.49  ? 91  SER   A O   1 
ATOM   738  C CB  . SER   A 1 92 ? 19.462  -18.286 -6.527  1.00 37.71  ? 91  SER   A CB  1 
ATOM   739  O OG  . SER   A 1 92 ? 19.307  -19.397 -7.392  1.00 44.08  ? 91  SER   A OG  1 
ATOM   740  N N   . TYR   A 1 93 ? 16.873  -20.222 -5.312  1.00 26.98  ? 92  TYR   A N   1 
ATOM   741  C CA  . TYR   A 1 93 ? 16.476  -21.545 -4.850  1.00 32.21  ? 92  TYR   A CA  1 
ATOM   742  C C   . TYR   A 1 93 ? 16.355  -22.530 -6.019  1.00 38.36  ? 92  TYR   A C   1 
ATOM   743  O O   . TYR   A 1 93 ? 15.870  -23.643 -5.828  1.00 44.70  ? 92  TYR   A O   1 
ATOM   744  C CB  . TYR   A 1 93 ? 15.153  -21.580 -4.070  1.00 28.73  ? 92  TYR   A CB  1 
ATOM   745  C CG  . TYR   A 1 93 ? 15.279  -20.955 -2.690  1.00 26.52  ? 92  TYR   A CG  1 
ATOM   746  C CD1 . TYR   A 1 93 ? 15.739  -21.713 -1.603  1.00 29.88  ? 92  TYR   A CD1 1 
ATOM   747  C CD2 . TYR   A 1 93 ? 14.957  -19.618 -2.477  1.00 28.00  ? 92  TYR   A CD2 1 
ATOM   748  C CE1 . TYR   A 1 93 ? 15.882  -21.139 -0.346  1.00 32.93  ? 92  TYR   A CE1 1 
ATOM   749  C CE2 . TYR   A 1 93 ? 15.112  -19.043 -1.230  1.00 28.61  ? 92  TYR   A CE2 1 
ATOM   750  C CZ  . TYR   A 1 93 ? 15.545  -19.808 -0.166  1.00 28.30  ? 92  TYR   A CZ  1 
ATOM   751  O OH  . TYR   A 1 93 ? 15.751  -19.257 1.056   1.00 28.70  ? 92  TYR   A OH  1 
ATOM   752  N N   . SER   A 1 94 ? 16.775  -22.119 -7.211  1.00 46.45  ? 93  SER   A N   1 
ATOM   753  C CA  . SER   A 1 94 ? 16.996  -23.041 -8.314  1.00 58.66  ? 93  SER   A CA  1 
ATOM   754  C C   . SER   A 1 94 ? 17.803  -24.248 -7.805  1.00 69.67  ? 93  SER   A C   1 
ATOM   755  O O   . SER   A 1 94 ? 19.031  -24.074 -7.627  1.00 77.84  ? 93  SER   A O   1 
ATOM   756  C CB  . SER   A 1 94 ? 17.724  -22.343 -9.435  1.00 56.74  ? 93  SER   A CB  1 
ATOM   757  O OG  . SER   A 1 94 ? 17.041  -21.155 -9.805  1.00 72.78  ? 93  SER   A OG  1 
ATOM   758  O OXT . SER   A 1 94 ? 17.177  -25.312 -7.571  1.00 73.09  ? 93  SER   A OXT 1 
ATOM   759  N N   . MET   B 1 2  ? 38.934  -11.490 -42.251 1.00 60.75  ? 1   MET   B N   1 
ATOM   760  C CA  . MET   B 1 2  ? 38.513  -12.309 -43.419 1.00 61.21  ? 1   MET   B CA  1 
ATOM   761  C C   . MET   B 1 2  ? 36.985  -12.377 -43.452 1.00 52.84  ? 1   MET   B C   1 
ATOM   762  O O   . MET   B 1 2  ? 36.360  -12.576 -42.406 1.00 54.07  ? 1   MET   B O   1 
ATOM   763  C CB  . MET   B 1 2  ? 39.118  -13.718 -43.334 1.00 62.40  ? 1   MET   B CB  1 
ATOM   764  C CG  . MET   B 1 2  ? 39.144  -14.500 -44.645 1.00 75.00  ? 1   MET   B CG  1 
ATOM   765  S SD  . MET   B 1 2  ? 40.085  -13.768 -46.005 1.00 77.97  ? 1   MET   B SD  1 
ATOM   766  C CE  . MET   B 1 2  ? 41.381  -12.846 -45.163 1.00 54.00  ? 1   MET   B CE  1 
ATOM   767  N N   . PRO   B 1 3  ? 36.339  -12.147 -44.626 1.00 50.88  ? 2   PRO   B N   1 
ATOM   768  C CA  . PRO   B 1 3  ? 34.899  -12.381 -44.773 1.00 51.27  ? 2   PRO   B CA  1 
ATOM   769  C C   . PRO   B 1 3  ? 34.540  -13.823 -44.423 1.00 50.89  ? 2   PRO   B C   1 
ATOM   770  O O   . PRO   B 1 3  ? 35.250  -14.751 -44.808 1.00 49.95  ? 2   PRO   B O   1 
ATOM   771  C CB  . PRO   B 1 3  ? 34.602  -12.039 -46.246 1.00 49.91  ? 2   PRO   B CB  1 
ATOM   772  C CG  . PRO   B 1 3  ? 35.715  -11.089 -46.621 1.00 49.25  ? 2   PRO   B CG  1 
ATOM   773  C CD  . PRO   B 1 3  ? 36.941  -11.577 -45.848 1.00 48.36  ? 2   PRO   B CD  1 
ATOM   774  N N   . HIS   B 1 4  ? 33.442  -13.993 -43.673 1.00 48.89  ? 3   HIS   B N   1 
ATOM   775  C CA  . HIS   B 1 4  ? 32.984  -15.325 -43.292 1.00 50.06  ? 3   HIS   B CA  1 
ATOM   776  C C   . HIS   B 1 4  ? 31.612  -15.601 -43.898 1.00 44.89  ? 3   HIS   B C   1 
ATOM   777  O O   . HIS   B 1 4  ? 31.033  -14.723 -44.558 1.00 37.02  ? 3   HIS   B O   1 
ATOM   778  C CB  . HIS   B 1 4  ? 33.064  -15.507 -41.774 1.00 56.11  ? 3   HIS   B CB  1 
ATOM   779  C CG  . HIS   B 1 4  ? 34.479  -15.606 -41.311 1.00 64.95  ? 3   HIS   B CG  1 
ATOM   780  N ND1 . HIS   B 1 4  ? 35.376  -16.471 -41.903 1.00 65.25  ? 3   HIS   B ND1 1 
ATOM   781  C CD2 . HIS   B 1 4  ? 35.153  -14.972 -40.328 1.00 64.80  ? 3   HIS   B CD2 1 
ATOM   782  C CE1 . HIS   B 1 4  ? 36.553  -16.355 -41.297 1.00 62.23  ? 3   HIS   B CE1 1 
ATOM   783  N NE2 . HIS   B 1 4  ? 36.439  -15.447 -40.341 1.00 63.39  ? 3   HIS   B NE2 1 
ATOM   784  N N   . ALA   B 1 5  ? 31.110  -16.830 -43.678 1.00 41.14  ? 4   ALA   B N   1 
ATOM   785  C CA  . ALA   B 1 5  ? 29.799  -17.201 -44.190 1.00 40.83  ? 4   ALA   B CA  1 
ATOM   786  C C   . ALA   B 1 5  ? 28.768  -16.201 -43.684 1.00 39.82  ? 4   ALA   B C   1 
ATOM   787  O O   . ALA   B 1 5  ? 27.859  -15.825 -44.425 1.00 40.49  ? 4   ALA   B O   1 
ATOM   788  C CB  . ALA   B 1 5  ? 29.438  -18.611 -43.787 1.00 37.44  ? 4   ALA   B CB  1 
ATOM   789  N N   . PHE   B 1 6  ? 28.918  -15.800 -42.415 1.00 40.59  ? 5   PHE   B N   1 
ATOM   790  C CA  . PHE   B 1 6  ? 28.066  -14.787 -41.809 1.00 40.39  ? 5   PHE   B CA  1 
ATOM   791  C C   . PHE   B 1 6  ? 28.860  -13.494 -41.630 1.00 40.89  ? 5   PHE   B C   1 
ATOM   792  O O   . PHE   B 1 6  ? 29.987  -13.525 -41.147 1.00 39.93  ? 5   PHE   B O   1 
ATOM   793  C CB  . PHE   B 1 6  ? 27.554  -15.238 -40.438 1.00 38.09  ? 5   PHE   B CB  1 
ATOM   794  C CG  . PHE   B 1 6  ? 26.465  -16.302 -40.519 1.00 43.58  ? 5   PHE   B CG  1 
ATOM   795  C CD1 . PHE   B 1 6  ? 25.130  -15.947 -40.696 1.00 37.56  ? 5   PHE   B CD1 1 
ATOM   796  C CD2 . PHE   B 1 6  ? 26.777  -17.655 -40.450 1.00 41.91  ? 5   PHE   B CD2 1 
ATOM   797  C CE1 . PHE   B 1 6  ? 24.139  -16.914 -40.795 1.00 38.46  ? 5   PHE   B CE1 1 
ATOM   798  C CE2 . PHE   B 1 6  ? 25.777  -18.614 -40.541 1.00 33.44  ? 5   PHE   B CE2 1 
ATOM   799  C CZ  . PHE   B 1 6  ? 24.459  -18.246 -40.698 1.00 36.63  ? 5   PHE   B CZ  1 
ATOM   800  N N   . LYS   B 1 7  ? 28.245  -12.362 -41.999 1.00 42.10  ? 6   LYS   B N   1 
ATOM   801  C CA  . LYS   B 1 7  ? 28.911  -11.078 -41.847 1.00 34.86  ? 6   LYS   B CA  1 
ATOM   802  C C   . LYS   B 1 7  ? 28.197  -10.265 -40.770 1.00 36.73  ? 6   LYS   B C   1 
ATOM   803  O O   . LYS   B 1 7  ? 26.980  -10.404 -40.579 1.00 32.84  ? 6   LYS   B O   1 
ATOM   804  C CB  . LYS   B 1 7  ? 28.954  -10.338 -43.185 1.00 36.22  ? 6   LYS   B CB  1 
ATOM   805  C CG  . LYS   B 1 7  ? 27.631  -10.174 -43.892 1.00 44.71  ? 6   LYS   B CG  1 
ATOM   806  C CD  . LYS   B 1 7  ? 27.781  -9.745  -45.353 1.00 44.40  ? 6   LYS   B CD  1 
ATOM   807  C CE  . LYS   B 1 7  ? 26.458  -9.440  -45.998 1.00 46.80  ? 6   LYS   B CE  1 
ATOM   808  N NZ  . LYS   B 1 7  ? 25.582  -10.615 -46.048 1.00 43.14  ? 6   LYS   B NZ  1 
ATOM   809  N N   . PRO   B 1 8  ? 28.928  -9.371  -40.058 1.00 38.21  ? 7   PRO   B N   1 
ATOM   810  C CA  . PRO   B 1 8  ? 28.324  -8.492  -39.053 1.00 32.43  ? 7   PRO   B CA  1 
ATOM   811  C C   . PRO   B 1 8  ? 27.182  -7.723  -39.703 1.00 39.74  ? 7   PRO   B C   1 
ATOM   812  O O   . PRO   B 1 8  ? 27.295  -7.240  -40.843 1.00 38.56  ? 7   PRO   B O   1 
ATOM   813  C CB  . PRO   B 1 8  ? 29.511  -7.590  -38.702 1.00 37.76  ? 7   PRO   B CB  1 
ATOM   814  C CG  . PRO   B 1 8  ? 30.710  -8.491  -38.873 1.00 35.10  ? 7   PRO   B CG  1 
ATOM   815  C CD  . PRO   B 1 8  ? 30.379  -9.134  -40.206 1.00 37.13  ? 7   PRO   B CD  1 
ATOM   816  N N   . GLY   B 1 9  ? 26.051  -7.706  -38.996 1.00 34.08  ? 8   GLY   B N   1 
ATOM   817  C CA  . GLY   B 1 9  ? 24.842  -7.078  -39.488 1.00 31.92  ? 8   GLY   B CA  1 
ATOM   818  C C   . GLY   B 1 9  ? 23.895  -8.060  -40.160 1.00 28.81  ? 8   GLY   B C   1 
ATOM   819  O O   . GLY   B 1 9  ? 22.765  -7.685  -40.395 1.00 29.60  ? 8   GLY   B O   1 
ATOM   820  N N   . ASP   B 1 10 ? 24.328  -9.298  -40.490 1.00 31.27  ? 9   ASP   B N   1 
ATOM   821  C CA  . ASP   B 1 10 ? 23.366  -10.282 -40.981 1.00 33.57  ? 9   ASP   B CA  1 
ATOM   822  C C   . ASP   B 1 10 ? 22.301  -10.595 -39.912 1.00 25.15  ? 9   ASP   B C   1 
ATOM   823  O O   . ASP   B 1 10 ? 22.583  -10.614 -38.718 1.00 29.41  ? 9   ASP   B O   1 
ATOM   824  C CB  . ASP   B 1 10 ? 24.017  -11.599 -41.358 1.00 33.51  ? 9   ASP   B CB  1 
ATOM   825  C CG  . ASP   B 1 10 ? 24.753  -11.654 -42.693 1.00 39.62  ? 9   ASP   B CG  1 
ATOM   826  O OD1 . ASP   B 1 10 ? 24.533  -10.751 -43.523 1.00 34.34  ? 9   ASP   B OD1 1 
ATOM   827  O OD2 . ASP   B 1 10 ? 25.578  -12.589 -42.861 1.00 37.52  ? 9   ASP   B OD2 1 
ATOM   828  N N   . LEU   B 1 11 ? 21.066  -10.789 -40.362 1.00 25.39  ? 10  LEU   B N   1 
ATOM   829  C CA  . LEU   B 1 11 ? 19.986  -11.002 -39.413 1.00 25.70  ? 10  LEU   B CA  1 
ATOM   830  C C   . LEU   B 1 11 ? 19.644  -12.479 -39.439 1.00 26.47  ? 10  LEU   B C   1 
ATOM   831  O O   . LEU   B 1 11 ? 19.698  -13.102 -40.506 1.00 31.23  ? 10  LEU   B O   1 
ATOM   832  C CB  . LEU   B 1 11 ? 18.803  -10.161 -39.865 1.00 27.36  ? 10  LEU   B CB  1 
ATOM   833  C CG  . LEU   B 1 11 ? 19.077  -8.654  -39.993 1.00 26.71  ? 10  LEU   B CG  1 
ATOM   834  C CD1 . LEU   B 1 11 ? 17.724  -8.026  -40.270 1.00 30.24  ? 10  LEU   B CD1 1 
ATOM   835  C CD2 . LEU   B 1 11 ? 19.785  -8.132  -38.730 1.00 28.75  ? 10  LEU   B CD2 1 
ATOM   836  N N   . VAL   B 1 12 ? 19.266  -13.030 -38.269 1.00 25.27  ? 11  VAL   B N   1 
ATOM   837  C CA  . VAL   B 1 12 ? 19.158  -14.479 -38.156 1.00 24.88  ? 11  VAL   B CA  1 
ATOM   838  C C   . VAL   B 1 12 ? 18.060  -14.753 -37.130 1.00 27.50  ? 11  VAL   B C   1 
ATOM   839  O O   . VAL   B 1 12 ? 17.658  -13.839 -36.403 1.00 26.46  ? 11  VAL   B O   1 
ATOM   840  C CB  . VAL   B 1 12 ? 20.470  -15.198 -37.731 1.00 25.18  ? 11  VAL   B CB  1 
ATOM   841  C CG1 . VAL   B 1 12 ? 21.613  -15.041 -38.750 1.00 27.26  ? 11  VAL   B CG1 1 
ATOM   842  C CG2 . VAL   B 1 12 ? 20.961  -14.861 -36.316 1.00 27.61  ? 11  VAL   B CG2 1 
ATOM   843  N N   . PHE   B 1 13 ? 17.587  -16.011 -37.083 1.00 27.25  ? 12  PHE   B N   1 
ATOM   844  C CA  . PHE   B 1 13 ? 17.091  -16.553 -35.828 1.00 26.14  ? 12  PHE   B CA  1 
ATOM   845  C C   . PHE   B 1 13 ? 18.199  -17.401 -35.233 1.00 28.34  ? 12  PHE   B C   1 
ATOM   846  O O   . PHE   B 1 13 ? 18.813  -18.184 -35.978 1.00 30.01  ? 12  PHE   B O   1 
ATOM   847  C CB  . PHE   B 1 13 ? 15.795  -17.339 -36.048 1.00 24.54  ? 12  PHE   B CB  1 
ATOM   848  C CG  . PHE   B 1 13 ? 14.599  -16.486 -36.471 1.00 28.62  ? 12  PHE   B CG  1 
ATOM   849  C CD1 . PHE   B 1 13 ? 14.378  -16.199 -37.813 1.00 26.54  ? 12  PHE   B CD1 1 
ATOM   850  C CD2 . PHE   B 1 13 ? 13.726  -15.942 -35.529 1.00 30.41  ? 12  PHE   B CD2 1 
ATOM   851  C CE1 . PHE   B 1 13 ? 13.276  -15.457 -38.228 1.00 31.38  ? 12  PHE   B CE1 1 
ATOM   852  C CE2 . PHE   B 1 13 ? 12.627  -15.181 -35.939 1.00 28.52  ? 12  PHE   B CE2 1 
ATOM   853  C CZ  . PHE   B 1 13 ? 12.413  -14.938 -37.290 1.00 29.91  ? 12  PHE   B CZ  1 
ATOM   854  N N   . ALA   B 1 14 ? 18.403  -17.299 -33.895 1.00 24.84  ? 13  ALA   B N   1 
ATOM   855  C CA  . ALA   B 1 14 ? 19.464  -18.019 -33.214 1.00 26.64  ? 13  ALA   B CA  1 
ATOM   856  C C   . ALA   B 1 14 ? 18.860  -18.956 -32.162 1.00 25.30  ? 13  ALA   B C   1 
ATOM   857  O O   . ALA   B 1 14 ? 17.986  -18.552 -31.397 1.00 25.19  ? 13  ALA   B O   1 
ATOM   858  C CB  . ALA   B 1 14 ? 20.440  -17.075 -32.561 1.00 25.04  ? 13  ALA   B CB  1 
ATOM   859  N N   . LYS   B 1 15 ? 19.354  -20.191 -32.127 1.00 25.96  ? 14  LYS   B N   1 
ATOM   860  C CA  . LYS   B 1 15 ? 18.720  -21.209 -31.293 1.00 28.54  ? 14  LYS   B CA  1 
ATOM   861  C C   . LYS   B 1 15 ? 19.616  -21.506 -30.096 1.00 30.19  ? 14  LYS   B C   1 
ATOM   862  O O   . LYS   B 1 15 ? 20.819  -21.741 -30.247 1.00 30.35  ? 14  LYS   B O   1 
ATOM   863  C CB  . LYS   B 1 15 ? 18.531  -22.504 -32.091 1.00 30.62  ? 14  LYS   B CB  1 
ATOM   864  C CG  . LYS   B 1 15 ? 17.822  -23.624 -31.275 1.00 27.54  ? 14  LYS   B CG  1 
ATOM   865  C CD  . LYS   B 1 15 ? 16.318  -23.344 -31.158 1.00 32.17  ? 14  LYS   B CD  1 
ATOM   866  C CE  . LYS   B 1 15 ? 15.535  -24.475 -30.439 1.00 29.16  ? 14  LYS   B CE  1 
ATOM   867  N NZ  . LYS   B 1 15 ? 15.993  -24.515 -29.052 1.00 28.04  ? 14  LYS   B NZ  1 
ATOM   868  N N   . MET   B 1 16 ? 19.002  -21.529 -28.912 1.00 31.17  ? 15  MET   B N   1 
ATOM   869  C CA  . MET   B 1 16 ? 19.662  -21.862 -27.654 1.00 32.75  ? 15  MET   B CA  1 
ATOM   870  C C   . MET   B 1 16 ? 18.789  -22.898 -26.954 1.00 30.70  ? 15  MET   B C   1 
ATOM   871  O O   . MET   B 1 16 ? 17.558  -22.817 -27.010 1.00 27.86  ? 15  MET   B O   1 
ATOM   872  C CB  . MET   B 1 16 ? 19.697  -20.678 -26.671 1.00 35.80  ? 15  MET   B CB  1 
ATOM   873  C CG  . MET   B 1 16 ? 20.318  -19.379 -27.143 1.00 40.61  ? 15  MET   B CG  1 
ATOM   874  S SD  . MET   B 1 16 ? 22.039  -19.054 -26.697 1.00 45.52  ? 15  MET   B SD  1 
ATOM   875  C CE  . MET   B 1 16 ? 22.220  -19.440 -24.952 1.00 43.30  ? 15  MET   B CE  1 
ATOM   876  N N   . LYS   B 1 17 ? 19.430  -23.853 -26.289 1.00 29.91  ? 16  LYS   B N   1 
ATOM   877  C CA  . LYS   B 1 17 ? 18.678  -24.843 -25.530 1.00 32.24  ? 16  LYS   B CA  1 
ATOM   878  C C   . LYS   B 1 17 ? 17.692  -24.156 -24.572 1.00 31.86  ? 16  LYS   B C   1 
ATOM   879  O O   . LYS   B 1 17 ? 18.073  -23.246 -23.835 1.00 33.69  ? 16  LYS   B O   1 
ATOM   880  C CB  . LYS   B 1 17 ? 19.685  -25.670 -24.725 1.00 40.42  ? 16  LYS   B CB  1 
ATOM   881  C CG  . LYS   B 1 17 ? 19.106  -26.949 -24.115 1.00 48.35  ? 16  LYS   B CG  1 
ATOM   882  C CD  . LYS   B 1 17 ? 20.099  -27.789 -23.308 1.00 56.91  ? 16  LYS   B CD  1 
ATOM   883  C CE  . LYS   B 1 17 ? 19.646  -29.213 -23.026 1.00 54.78  ? 16  LYS   B CE  1 
ATOM   884  N NZ  . LYS   B 1 17 ? 18.546  -29.379 -22.069 1.00 52.81  ? 16  LYS   B NZ  1 
ATOM   885  N N   . GLY   B 1 18 ? 16.429  -24.592 -24.616 1.00 32.98  ? 17  GLY   B N   1 
ATOM   886  C CA  . GLY   B 1 18 ? 15.369  -24.140 -23.722 1.00 35.42  ? 17  GLY   B CA  1 
ATOM   887  C C   . GLY   B 1 18 ? 14.526  -22.986 -24.263 1.00 36.93  ? 17  GLY   B C   1 
ATOM   888  O O   . GLY   B 1 18 ? 13.572  -22.552 -23.609 1.00 33.61  ? 17  GLY   B O   1 
ATOM   889  N N   . TYR   B 1 19 ? 14.839  -22.502 -25.476 1.00 33.60  ? 18  TYR   B N   1 
ATOM   890  C CA  . TYR   B 1 19 ? 14.172  -21.299 -25.972 1.00 30.23  ? 18  TYR   B CA  1 
ATOM   891  C C   . TYR   B 1 19 ? 13.851  -21.460 -27.458 1.00 26.96  ? 18  TYR   B C   1 
ATOM   892  O O   . TYR   B 1 19 ? 14.553  -22.179 -28.160 1.00 31.11  ? 18  TYR   B O   1 
ATOM   893  C CB  . TYR   B 1 19 ? 15.155  -20.134 -25.824 1.00 27.76  ? 18  TYR   B CB  1 
ATOM   894  C CG  . TYR   B 1 19 ? 15.532  -19.857 -24.376 1.00 28.12  ? 18  TYR   B CG  1 
ATOM   895  C CD1 . TYR   B 1 19 ? 14.655  -19.182 -23.529 1.00 30.32  ? 18  TYR   B CD1 1 
ATOM   896  C CD2 . TYR   B 1 19 ? 16.713  -20.352 -23.846 1.00 28.59  ? 18  TYR   B CD2 1 
ATOM   897  C CE1 . TYR   B 1 19 ? 14.960  -18.985 -22.184 1.00 29.35  ? 18  TYR   B CE1 1 
ATOM   898  C CE2 . TYR   B 1 19 ? 17.022  -20.155 -22.508 1.00 34.15  ? 18  TYR   B CE2 1 
ATOM   899  C CZ  . TYR   B 1 19 ? 16.146  -19.475 -21.677 1.00 32.89  ? 18  TYR   B CZ  1 
ATOM   900  O OH  . TYR   B 1 19 ? 16.508  -19.306 -20.368 1.00 37.84  ? 18  TYR   B OH  1 
ATOM   901  N N   . PRO   B 1 20 ? 12.797  -20.798 -27.973 1.00 29.39  ? 19  PRO   B N   1 
ATOM   902  C CA  . PRO   B 1 20 ? 12.469  -20.856 -29.403 1.00 26.42  ? 19  PRO   B CA  1 
ATOM   903  C C   . PRO   B 1 20 ? 13.581  -20.165 -30.192 1.00 25.72  ? 19  PRO   B C   1 
ATOM   904  O O   . PRO   B 1 20 ? 14.244  -19.302 -29.637 1.00 26.12  ? 19  PRO   B O   1 
ATOM   905  C CB  . PRO   B 1 20 ? 11.182  -20.085 -29.537 1.00 25.90  ? 19  PRO   B CB  1 
ATOM   906  C CG  . PRO   B 1 20 ? 11.116  -19.198 -28.288 1.00 29.92  ? 19  PRO   B CG  1 
ATOM   907  C CD  . PRO   B 1 20 ? 11.909  -19.912 -27.205 1.00 29.09  ? 19  PRO   B CD  1 
ATOM   908  N N   . HIS   B 1 21 ? 13.743  -20.556 -31.476 1.00 26.01  ? 20  HIS   B N   1 
ATOM   909  C CA  . HIS   B 1 21 ? 14.595  -19.813 -32.408 1.00 28.31  ? 20  HIS   B CA  1 
ATOM   910  C C   . HIS   B 1 21 ? 14.332  -18.320 -32.237 1.00 26.70  ? 20  HIS   B C   1 
ATOM   911  O O   . HIS   B 1 21 ? 13.189  -17.887 -32.363 1.00 26.84  ? 20  HIS   B O   1 
ATOM   912  C CB  . HIS   B 1 21 ? 14.292  -20.258 -33.851 1.00 25.59  ? 20  HIS   B CB  1 
ATOM   913  C CG  . HIS   B 1 21 ? 14.512  -21.730 -34.047 1.00 26.99  ? 20  HIS   B CG  1 
ATOM   914  N ND1 . HIS   B 1 21 ? 13.553  -22.649 -33.631 1.00 25.50  ? 20  HIS   B ND1 1 
ATOM   915  C CD2 . HIS   B 1 21 ? 15.555  -22.464 -34.495 1.00 28.86  ? 20  HIS   B CD2 1 
ATOM   916  C CE1 . HIS   B 1 21 ? 13.977  -23.885 -33.910 1.00 29.74  ? 20  HIS   B CE1 1 
ATOM   917  N NE2 . HIS   B 1 21 ? 15.197  -23.803 -34.426 1.00 28.23  ? 20  HIS   B NE2 1 
ATOM   918  N N   . TRP   B 1 22 ? 15.391  -17.526 -32.046 1.00 25.84  ? 21  TRP   B N   1 
ATOM   919  C CA  . TRP   B 1 22 ? 15.186  -16.216 -31.425 1.00 24.78  ? 21  TRP   B CA  1 
ATOM   920  C C   . TRP   B 1 22 ? 15.674  -15.113 -32.363 1.00 25.36  ? 21  TRP   B C   1 
ATOM   921  O O   . TRP   B 1 22 ? 16.776  -15.261 -32.872 1.00 24.90  ? 21  TRP   B O   1 
ATOM   922  C CB  . TRP   B 1 22 ? 15.898  -16.158 -30.063 1.00 24.15  ? 21  TRP   B CB  1 
ATOM   923  C CG  . TRP   B 1 22 ? 15.395  -15.013 -29.212 1.00 26.61  ? 21  TRP   B CG  1 
ATOM   924  C CD1 . TRP   B 1 22 ? 15.686  -13.679 -29.341 1.00 26.18  ? 21  TRP   B CD1 1 
ATOM   925  C CD2 . TRP   B 1 22 ? 14.470  -15.100 -28.090 1.00 27.46  ? 21  TRP   B CD2 1 
ATOM   926  N NE1 . TRP   B 1 22 ? 14.982  -12.932 -28.406 1.00 27.42  ? 21  TRP   B NE1 1 
ATOM   927  C CE2 . TRP   B 1 22 ? 14.228  -13.782 -27.628 1.00 27.34  ? 21  TRP   B CE2 1 
ATOM   928  C CE3 . TRP   B 1 22 ? 13.809  -16.164 -27.453 1.00 28.99  ? 21  TRP   B CE3 1 
ATOM   929  C CZ2 . TRP   B 1 22 ? 13.362  -13.492 -26.556 1.00 26.27  ? 21  TRP   B CZ2 1 
ATOM   930  C CZ3 . TRP   B 1 22 ? 12.969  -15.876 -26.391 1.00 27.58  ? 21  TRP   B CZ3 1 
ATOM   931  C CH2 . TRP   B 1 22 ? 12.718  -14.561 -25.967 1.00 27.87  ? 21  TRP   B CH2 1 
ATOM   932  N N   . PRO   B 1 23 ? 14.907  -14.023 -32.645 1.00 25.18  ? 22  PRO   B N   1 
ATOM   933  C CA  . PRO   B 1 23 ? 15.342  -12.985 -33.597 1.00 25.66  ? 22  PRO   B CA  1 
ATOM   934  C C   . PRO   B 1 23 ? 16.670  -12.391 -33.117 1.00 28.30  ? 22  PRO   B C   1 
ATOM   935  O O   . PRO   B 1 23 ? 16.832  -11.997 -31.959 1.00 25.22  ? 22  PRO   B O   1 
ATOM   936  C CB  . PRO   B 1 23 ? 14.191  -11.936 -33.657 1.00 25.81  ? 22  PRO   B CB  1 
ATOM   937  C CG  . PRO   B 1 23 ? 13.418  -12.201 -32.351 1.00 26.01  ? 22  PRO   B CG  1 
ATOM   938  C CD  . PRO   B 1 23 ? 13.581  -13.704 -32.096 1.00 24.76  ? 22  PRO   B CD  1 
ATOM   939  N N   . ALA   B 1 24 ? 17.662  -12.341 -34.008 1.00 26.50  ? 23  ALA   B N   1 
ATOM   940  C CA  . ALA   B 1 24 ? 18.984  -11.930 -33.554 1.00 23.88  ? 23  ALA   B CA  1 
ATOM   941  C C   . ALA   B 1 24 ? 19.804  -11.374 -34.716 1.00 23.99  ? 23  ALA   B C   1 
ATOM   942  O O   . ALA   B 1 24 ? 19.349  -11.418 -35.869 1.00 26.80  ? 23  ALA   B O   1 
ATOM   943  C CB  . ALA   B 1 24 ? 19.679  -13.086 -32.872 1.00 26.22  ? 23  ALA   B CB  1 
ATOM   944  N N   . ARG   B 1 25 ? 21.006  -10.887 -34.380 1.00 27.32  ? 24  ARG   B N   1 
ATOM   945  C CA  . ARG   B 1 25 ? 21.919  -10.411 -35.421 1.00 27.24  ? 24  ARG   B CA  1 
ATOM   946  C C   . ARG   B 1 25 ? 23.340  -10.853 -35.094 1.00 26.22  ? 24  ARG   B C   1 
ATOM   947  O O   . ARG   B 1 25 ? 23.666  -11.154 -33.950 1.00 25.87  ? 24  ARG   B O   1 
ATOM   948  C CB  . ARG   B 1 25 ? 21.923  -8.889  -35.539 1.00 27.66  ? 24  ARG   B CB  1 
ATOM   949  C CG  . ARG   B 1 25 ? 22.603  -8.154  -34.393 1.00 31.36  ? 24  ARG   B CG  1 
ATOM   950  C CD  . ARG   B 1 25 ? 22.395  -6.628  -34.505 1.00 30.51  ? 24  ARG   B CD  1 
ATOM   951  N NE  . ARG   B 1 25 ? 22.991  -5.904  -33.375 1.00 31.42  ? 24  ARG   B NE  1 
ATOM   952  C CZ  . ARG   B 1 25 ? 22.659  -4.668  -33.001 1.00 29.37  ? 24  ARG   B CZ  1 
ATOM   953  N NH1 . ARG   B 1 25 ? 21.662  -4.028  -33.612 1.00 30.97  ? 24  ARG   B NH1 1 
ATOM   954  N NH2 . ARG   B 1 25 ? 23.311  -4.107  -31.995 1.00 29.59  ? 24  ARG   B NH2 1 
ATOM   955  N N   . ILE   B 1 26 ? 24.182  -10.921 -36.152 1.00 26.88  ? 25  ILE   B N   1 
ATOM   956  C CA  . ILE   B 1 26 ? 25.605  -11.137 -35.974 1.00 30.68  ? 25  ILE   B CA  1 
ATOM   957  C C   . ILE   B 1 26 ? 26.200  -9.765  -35.663 1.00 34.02  ? 25  ILE   B C   1 
ATOM   958  O O   . ILE   B 1 26 ? 25.931  -8.812  -36.388 1.00 31.77  ? 25  ILE   B O   1 
ATOM   959  C CB  . ILE   B 1 26 ? 26.190  -11.692 -37.295 1.00 35.88  ? 25  ILE   B CB  1 
ATOM   960  C CG1 . ILE   B 1 26 ? 25.371  -12.851 -37.850 1.00 33.15  ? 25  ILE   B CG1 1 
ATOM   961  C CG2 . ILE   B 1 26 ? 27.687  -12.011 -37.178 1.00 38.35  ? 25  ILE   B CG2 1 
ATOM   962  C CD1 . ILE   B 1 26 ? 25.363  -14.097 -36.974 1.00 31.36  ? 25  ILE   B CD1 1 
ATOM   963  N N   . ASP   B 1 27 ? 26.989  -9.687  -34.590 1.00 31.39  ? 26  ASP   B N   1 
ATOM   964  C CA  . ASP   B 1 27 ? 27.627  -8.446  -34.168 1.00 38.60  ? 26  ASP   B CA  1 
ATOM   965  C C   . ASP   B 1 27 ? 29.076  -8.389  -34.669 1.00 43.06  ? 26  ASP   B C   1 
ATOM   966  O O   . ASP   B 1 27 ? 29.645  -9.414  -35.024 1.00 42.41  ? 26  ASP   B O   1 
ATOM   967  C CB  . ASP   B 1 27 ? 27.577  -8.323  -32.657 1.00 32.59  ? 26  ASP   B CB  1 
ATOM   968  C CG  . ASP   B 1 27 ? 26.376  -7.608  -32.061 1.00 43.35  ? 26  ASP   B CG  1 
ATOM   969  O OD1 . ASP   B 1 27 ? 25.506  -7.148  -32.841 1.00 42.57  ? 26  ASP   B OD1 1 
ATOM   970  O OD2 . ASP   B 1 27 ? 26.325  -7.508  -30.809 1.00 41.04  ? 26  ASP   B OD2 1 
ATOM   971  N N   . ASP   B 1 28 ? 29.689  -7.191  -34.656 1.00 51.18  ? 27  ASP   B N   1 
ATOM   972  C CA  . ASP   B 1 28 ? 31.115  -7.063  -34.927 1.00 55.24  ? 27  ASP   B CA  1 
ATOM   973  C C   . ASP   B 1 28 ? 31.877  -7.472  -33.661 1.00 57.02  ? 27  ASP   B C   1 
ATOM   974  O O   . ASP   B 1 28 ? 31.272  -7.609  -32.599 1.00 58.86  ? 27  ASP   B O   1 
ATOM   975  C CB  . ASP   B 1 28 ? 31.454  -5.690  -35.496 1.00 54.54  ? 27  ASP   B CB  1 
ATOM   976  C CG  . ASP   B 1 28 ? 32.203  -5.713  -36.826 1.00 53.13  ? 27  ASP   B CG  1 
ATOM   977  O OD1 . ASP   B 1 28 ? 33.203  -6.451  -36.938 1.00 56.05  ? 27  ASP   B OD1 1 
ATOM   978  O OD2 . ASP   B 1 28 ? 31.782  -4.998  -37.756 1.00 55.48  ? 27  ASP   B OD2 1 
ATOM   979  N N   . ILE   B 1 29 ? 33.191  -7.708  -33.778 1.00 70.12  ? 28  ILE   B N   1 
ATOM   980  C CA  . ILE   B 1 29 ? 33.989  -8.202  -32.661 1.00 79.01  ? 28  ILE   B CA  1 
ATOM   981  C C   . ILE   B 1 29 ? 34.702  -7.024  -31.970 1.00 88.72  ? 28  ILE   B C   1 
ATOM   982  O O   . ILE   B 1 29 ? 35.302  -6.198  -32.698 1.00 93.14  ? 28  ILE   B O   1 
ATOM   983  C CB  . ILE   B 1 29 ? 34.979  -9.296  -33.109 1.00 66.52  ? 28  ILE   B CB  1 
ATOM   984  N N   . VAL   B 1 34 ? 37.490  -9.947  -25.735 1.00 69.92  ? 33  VAL   B N   1 
ATOM   985  C CA  . VAL   B 1 34 ? 37.004  -11.358 -25.825 1.00 66.21  ? 33  VAL   B CA  1 
ATOM   986  C C   . VAL   B 1 34 ? 36.590  -11.592 -27.274 1.00 78.31  ? 33  VAL   B C   1 
ATOM   987  O O   . VAL   B 1 34 ? 35.550  -11.104 -27.711 1.00 87.54  ? 33  VAL   B O   1 
ATOM   988  C CB  . VAL   B 1 34 ? 35.863  -11.641 -24.818 1.00 64.10  ? 33  VAL   B CB  1 
ATOM   989  C CG1 . VAL   B 1 34 ? 34.673  -10.694 -24.975 1.00 65.78  ? 33  VAL   B CG1 1 
ATOM   990  C CG2 . VAL   B 1 34 ? 35.395  -13.093 -24.834 1.00 53.00  ? 33  VAL   B CG2 1 
ATOM   991  N N   . LYS   B 1 35 ? 37.449  -12.277 -28.036 1.00 75.22  ? 34  LYS   B N   1 
ATOM   992  C CA  . LYS   B 1 35 ? 37.075  -12.736 -29.364 1.00 65.50  ? 34  LYS   B CA  1 
ATOM   993  C C   . LYS   B 1 35 ? 36.187  -13.974 -29.210 1.00 66.43  ? 34  LYS   B C   1 
ATOM   994  O O   . LYS   B 1 35 ? 36.190  -14.616 -28.155 1.00 64.19  ? 34  LYS   B O   1 
ATOM   995  C CB  . LYS   B 1 35 ? 38.334  -12.950 -30.212 1.00 63.34  ? 34  LYS   B CB  1 
ATOM   996  N N   . PRO   B 1 36 ? 35.359  -14.336 -30.222 1.00 62.21  ? 35  PRO   B N   1 
ATOM   997  C CA  . PRO   B 1 36 ? 34.560  -15.565 -30.135 1.00 58.10  ? 35  PRO   B CA  1 
ATOM   998  C C   . PRO   B 1 36 ? 35.432  -16.815 -30.034 1.00 44.83  ? 35  PRO   B C   1 
ATOM   999  O O   . PRO   B 1 36 ? 36.528  -16.831 -30.577 1.00 49.75  ? 35  PRO   B O   1 
ATOM   1000 C CB  . PRO   B 1 36 ? 33.732  -15.532 -31.433 1.00 57.86  ? 35  PRO   B CB  1 
ATOM   1001 C CG  . PRO   B 1 36 ? 34.498  -14.604 -32.364 1.00 64.23  ? 35  PRO   B CG  1 
ATOM   1002 C CD  . PRO   B 1 36 ? 35.125  -13.569 -31.459 1.00 59.13  ? 35  PRO   B CD  1 
ATOM   1003 N N   . PRO   B 1 37 ? 35.004  -17.903 -29.356 1.00 45.28  ? 36  PRO   B N   1 
ATOM   1004 C CA  . PRO   B 1 37 ? 35.729  -19.171 -29.444 1.00 43.44  ? 36  PRO   B CA  1 
ATOM   1005 C C   . PRO   B 1 37 ? 35.794  -19.594 -30.908 1.00 47.09  ? 36  PRO   B C   1 
ATOM   1006 O O   . PRO   B 1 37 ? 35.015  -19.089 -31.728 1.00 47.79  ? 36  PRO   B O   1 
ATOM   1007 C CB  . PRO   B 1 37 ? 34.939  -20.184 -28.581 1.00 47.32  ? 36  PRO   B CB  1 
ATOM   1008 C CG  . PRO   B 1 37 ? 33.970  -19.340 -27.771 1.00 47.88  ? 36  PRO   B CG  1 
ATOM   1009 C CD  . PRO   B 1 37 ? 33.850  -17.968 -28.447 1.00 47.28  ? 36  PRO   B CD  1 
ATOM   1010 N N   . PRO   B 1 38 ? 36.711  -20.522 -31.282 1.00 48.68  ? 37  PRO   B N   1 
ATOM   1011 C CA  . PRO   B 1 38 ? 36.765  -21.064 -32.650 1.00 48.06  ? 37  PRO   B CA  1 
ATOM   1012 C C   . PRO   B 1 38 ? 35.416  -21.486 -33.239 1.00 45.39  ? 37  PRO   B C   1 
ATOM   1013 O O   . PRO   B 1 38 ? 34.653  -22.201 -32.592 1.00 46.05  ? 37  PRO   B O   1 
ATOM   1014 C CB  . PRO   B 1 38 ? 37.735  -22.270 -32.525 1.00 48.67  ? 37  PRO   B CB  1 
ATOM   1015 C CG  . PRO   B 1 38 ? 38.632  -21.930 -31.336 1.00 48.63  ? 37  PRO   B CG  1 
ATOM   1016 C CD  . PRO   B 1 38 ? 37.772  -21.068 -30.409 1.00 54.43  ? 37  PRO   B CD  1 
ATOM   1017 N N   . ASN   B 1 39 ? 35.145  -21.031 -34.472 1.00 46.48  ? 38  ASN   B N   1 
ATOM   1018 C CA  . ASN   B 1 39 ? 33.980  -21.434 -35.263 1.00 48.56  ? 38  ASN   B CA  1 
ATOM   1019 C C   . ASN   B 1 39 ? 32.693  -20.726 -34.837 1.00 38.69  ? 38  ASN   B C   1 
ATOM   1020 O O   . ASN   B 1 39 ? 31.653  -20.961 -35.433 1.00 40.52  ? 38  ASN   B O   1 
ATOM   1021 C CB  . ASN   B 1 39 ? 33.664  -22.921 -35.142 1.00 44.19  ? 38  ASN   B CB  1 
ATOM   1022 C CG  . ASN   B 1 39 ? 34.847  -23.784 -35.504 1.00 52.75  ? 38  ASN   B CG  1 
ATOM   1023 O OD1 . ASN   B 1 39 ? 35.171  -24.732 -34.775 1.00 57.92  ? 38  ASN   B OD1 1 
ATOM   1024 N ND2 . ASN   B 1 39 ? 35.485  -23.477 -36.623 1.00 46.92  ? 38  ASN   B ND2 1 
ATOM   1025 N N   . LYS   B 1 40 ? 32.743  -19.894 -33.794 1.00 42.19  ? 39  LYS   B N   1 
ATOM   1026 C CA  . LYS   B 1 40 ? 31.542  -19.251 -33.270 1.00 37.99  ? 39  LYS   B CA  1 
ATOM   1027 C C   . LYS   B 1 40 ? 31.513  -17.767 -33.646 1.00 36.14  ? 39  LYS   B C   1 
ATOM   1028 O O   . LYS   B 1 40 ? 32.531  -17.183 -34.003 1.00 38.87  ? 39  LYS   B O   1 
ATOM   1029 C CB  . LYS   B 1 40 ? 31.504  -19.582 -31.774 1.00 36.52  ? 39  LYS   B CB  1 
ATOM   1030 C CG  . LYS   B 1 40 ? 31.260  -21.064 -31.503 1.00 36.59  ? 39  LYS   B CG  1 
ATOM   1031 C CD  . LYS   B 1 40 ? 31.317  -21.356 -30.008 1.00 47.24  ? 39  LYS   B CD  1 
ATOM   1032 C CE  . LYS   B 1 40 ? 30.343  -22.403 -29.537 1.00 57.69  ? 39  LYS   B CE  1 
ATOM   1033 N NZ  . LYS   B 1 40 ? 30.426  -23.683 -30.252 1.00 61.18  ? 39  LYS   B NZ  1 
ATOM   1034 N N   . TYR   B 1 41 ? 30.322  -17.164 -33.582 1.00 36.88  ? 40  TYR   B N   1 
ATOM   1035 C CA  . TYR   B 1 41 ? 30.111  -15.756 -33.901 1.00 36.29  ? 40  TYR   B CA  1 
ATOM   1036 C C   . TYR   B 1 41 ? 29.532  -15.005 -32.700 1.00 36.77  ? 40  TYR   B C   1 
ATOM   1037 O O   . TYR   B 1 41 ? 28.762  -15.581 -31.923 1.00 35.03  ? 40  TYR   B O   1 
ATOM   1038 C CB  . TYR   B 1 41 ? 29.021  -15.713 -34.973 1.00 34.89  ? 40  TYR   B CB  1 
ATOM   1039 C CG  . TYR   B 1 41 ? 29.457  -16.129 -36.375 1.00 34.09  ? 40  TYR   B CG  1 
ATOM   1040 C CD1 . TYR   B 1 41 ? 30.112  -15.240 -37.229 1.00 30.59  ? 40  TYR   B CD1 1 
ATOM   1041 C CD2 . TYR   B 1 41 ? 29.180  -17.406 -36.845 1.00 31.82  ? 40  TYR   B CD2 1 
ATOM   1042 C CE1 . TYR   B 1 41 ? 30.489  -15.640 -38.514 1.00 35.23  ? 40  TYR   B CE1 1 
ATOM   1043 C CE2 . TYR   B 1 41 ? 29.549  -17.812 -38.119 1.00 35.80  ? 40  TYR   B CE2 1 
ATOM   1044 C CZ  . TYR   B 1 41 ? 30.215  -16.928 -38.957 1.00 36.67  ? 40  TYR   B CZ  1 
ATOM   1045 O OH  . TYR   B 1 41 ? 30.545  -17.347 -40.230 1.00 35.71  ? 40  TYR   B OH  1 
ATOM   1046 N N   . PRO   B 1 42 ? 29.770  -13.674 -32.573 1.00 35.47  ? 41  PRO   B N   1 
ATOM   1047 C CA  . PRO   B 1 42 ? 29.071  -12.881 -31.558 1.00 31.44  ? 41  PRO   B CA  1 
ATOM   1048 C C   . PRO   B 1 42 ? 27.630  -12.607 -31.977 1.00 29.68  ? 41  PRO   B C   1 
ATOM   1049 O O   . PRO   B 1 42 ? 27.378  -11.987 -33.035 1.00 33.01  ? 41  PRO   B O   1 
ATOM   1050 C CB  . PRO   B 1 42 ? 29.909  -11.570 -31.411 1.00 34.87  ? 41  PRO   B CB  1 
ATOM   1051 C CG  . PRO   B 1 42 ? 30.995  -11.662 -32.491 1.00 37.47  ? 41  PRO   B CG  1 
ATOM   1052 C CD  . PRO   B 1 42 ? 30.677  -12.849 -33.406 1.00 34.85  ? 41  PRO   B CD  1 
ATOM   1053 N N   . ILE   B 1 43 ? 26.689  -13.078 -31.141 1.00 30.09  ? 42  ILE   B N   1 
ATOM   1054 C CA  . ILE   B 1 43 ? 25.257  -12.926 -31.405 1.00 26.96  ? 42  ILE   B CA  1 
ATOM   1055 C C   . ILE   B 1 43 ? 24.658  -11.900 -30.443 1.00 27.53  ? 42  ILE   B C   1 
ATOM   1056 O O   . ILE   B 1 43 ? 24.941  -11.972 -29.253 1.00 30.60  ? 42  ILE   B O   1 
ATOM   1057 C CB  . ILE   B 1 43 ? 24.516  -14.267 -31.256 1.00 28.01  ? 42  ILE   B CB  1 
ATOM   1058 C CG1 . ILE   B 1 43 ? 25.215  -15.390 -32.059 1.00 29.38  ? 42  ILE   B CG1 1 
ATOM   1059 C CG2 . ILE   B 1 43 ? 23.045  -14.115 -31.664 1.00 26.09  ? 42  ILE   B CG2 1 
ATOM   1060 C CD1 . ILE   B 1 43 ? 25.331  -15.106 -33.549 1.00 29.04  ? 42  ILE   B CD1 1 
ATOM   1061 N N   . PHE   B 1 44 ? 23.795  -11.018 -30.985 1.00 27.50  ? 43  PHE   B N   1 
ATOM   1062 C CA  . PHE   B 1 44 ? 22.957  -10.124 -30.204 1.00 28.14  ? 43  PHE   B CA  1 
ATOM   1063 C C   . PHE   B 1 44 ? 21.497  -10.517 -30.406 1.00 26.47  ? 43  PHE   B C   1 
ATOM   1064 O O   . PHE   B 1 44 ? 21.005  -10.544 -31.529 1.00 27.15  ? 43  PHE   B O   1 
ATOM   1065 C CB  . PHE   B 1 44 ? 23.223  -8.670  -30.618 1.00 27.47  ? 43  PHE   B CB  1 
ATOM   1066 C CG  . PHE   B 1 44 ? 22.264  -7.687  -29.961 1.00 29.25  ? 43  PHE   B CG  1 
ATOM   1067 C CD1 . PHE   B 1 44 ? 21.071  -7.309  -30.588 1.00 27.10  ? 43  PHE   B CD1 1 
ATOM   1068 C CD2 . PHE   B 1 44 ? 22.560  -7.147  -28.712 1.00 35.43  ? 43  PHE   B CD2 1 
ATOM   1069 C CE1 . PHE   B 1 44 ? 20.219  -6.375  -29.996 1.00 30.73  ? 43  PHE   B CE1 1 
ATOM   1070 C CE2 . PHE   B 1 44 ? 21.683  -6.238  -28.113 1.00 32.64  ? 43  PHE   B CE2 1 
ATOM   1071 C CZ  . PHE   B 1 44 ? 20.534  -5.856  -28.759 1.00 32.16  ? 43  PHE   B CZ  1 
ATOM   1072 N N   . PHE   B 1 45 ? 20.816  -10.849 -29.304 1.00 26.53  ? 44  PHE   B N   1 
ATOM   1073 C CA  . PHE   B 1 45 ? 19.406  -11.199 -29.336 1.00 26.51  ? 44  PHE   B CA  1 
ATOM   1074 C C   . PHE   B 1 45 ? 18.551  -9.961  -29.117 1.00 26.10  ? 44  PHE   B C   1 
ATOM   1075 O O   . PHE   B 1 45 ? 18.676  -9.276  -28.091 1.00 29.12  ? 44  PHE   B O   1 
ATOM   1076 C CB  . PHE   B 1 45 ? 19.211  -12.139 -28.142 1.00 26.20  ? 44  PHE   B CB  1 
ATOM   1077 C CG  . PHE   B 1 45 ? 19.924  -13.475 -28.297 1.00 26.13  ? 44  PHE   B CG  1 
ATOM   1078 C CD1 . PHE   B 1 45 ? 21.236  -13.632 -27.877 1.00 28.65  ? 44  PHE   B CD1 1 
ATOM   1079 C CD2 . PHE   B 1 45 ? 19.301  -14.552 -28.931 1.00 24.31  ? 44  PHE   B CD2 1 
ATOM   1080 C CE1 . PHE   B 1 45 ? 21.882  -14.847 -28.045 1.00 32.67  ? 44  PHE   B CE1 1 
ATOM   1081 C CE2 . PHE   B 1 45 ? 19.956  -15.774 -29.070 1.00 26.87  ? 44  PHE   B CE2 1 
ATOM   1082 C CZ  . PHE   B 1 45 ? 21.265  -15.893 -28.680 1.00 25.05  ? 44  PHE   B CZ  1 
ATOM   1083 N N   . PHE   B 1 46 ? 17.680  -9.708  -30.094 1.00 26.18  ? 45  PHE   B N   1 
ATOM   1084 C CA  . PHE   B 1 46 ? 16.726  -8.622  -30.042 1.00 26.59  ? 45  PHE   B CA  1 
ATOM   1085 C C   . PHE   B 1 46 ? 15.737  -8.892  -28.899 1.00 29.52  ? 45  PHE   B C   1 
ATOM   1086 O O   . PHE   B 1 46 ? 15.401  -10.043 -28.575 1.00 29.17  ? 45  PHE   B O   1 
ATOM   1087 C CB  . PHE   B 1 46 ? 15.974  -8.481  -31.367 1.00 26.13  ? 45  PHE   B CB  1 
ATOM   1088 C CG  . PHE   B 1 46 ? 16.893  -8.034  -32.503 1.00 28.52  ? 45  PHE   B CG  1 
ATOM   1089 C CD1 . PHE   B 1 46 ? 17.436  -6.748  -32.493 1.00 30.85  ? 45  PHE   B CD1 1 
ATOM   1090 C CD2 . PHE   B 1 46 ? 17.167  -8.873  -33.598 1.00 27.46  ? 45  PHE   B CD2 1 
ATOM   1091 C CE1 . PHE   B 1 46 ? 18.260  -6.318  -33.535 1.00 33.80  ? 45  PHE   B CE1 1 
ATOM   1092 C CE2 . PHE   B 1 46 ? 17.993  -8.444  -34.638 1.00 30.30  ? 45  PHE   B CE2 1 
ATOM   1093 C CZ  . PHE   B 1 46 ? 18.532  -7.165  -34.598 1.00 28.09  ? 45  PHE   B CZ  1 
ATOM   1094 N N   . GLY   B 1 47 ? 15.261  -7.800  -28.294 1.00 29.51  ? 46  GLY   B N   1 
ATOM   1095 C CA  . GLY   B 1 47 ? 14.201  -7.929  -27.308 1.00 27.66  ? 46  GLY   B CA  1 
ATOM   1096 C C   . GLY   B 1 47 ? 14.825  -7.996  -25.919 1.00 31.21  ? 46  GLY   B C   1 
ATOM   1097 O O   . GLY   B 1 47 ? 14.630  -7.080  -25.128 1.00 34.38  ? 46  GLY   B O   1 
ATOM   1098 N N   . THR   B 1 48 ? 15.628  -9.038  -25.652 1.00 29.32  ? 47  THR   B N   1 
ATOM   1099 C CA  . THR   B 1 48 ? 16.278  -9.229  -24.369 1.00 33.30  ? 47  THR   B CA  1 
ATOM   1100 C C   . THR   B 1 48 ? 17.595  -8.459  -24.331 1.00 35.63  ? 47  THR   B C   1 
ATOM   1101 O O   . THR   B 1 48 ? 18.117  -8.153  -23.253 1.00 34.33  ? 47  THR   B O   1 
ATOM   1102 C CB  . THR   B 1 48 ? 16.495  -10.711 -24.048 1.00 35.48  ? 47  THR   B CB  1 
ATOM   1103 O OG1 . THR   B 1 48 ? 17.501  -11.261 -24.905 1.00 31.67  ? 47  THR   B OG1 1 
ATOM   1104 C CG2 . THR   B 1 48 ? 15.188  -11.481 -24.078 1.00 30.77  ? 47  THR   B CG2 1 
ATOM   1105 N N   . HIS   B 1 49 ? 18.103  -8.165  -25.529 1.00 32.25  ? 48  HIS   B N   1 
ATOM   1106 C CA  . HIS   B 1 49 ? 19.354  -7.450  -25.722 1.00 37.32  ? 48  HIS   B CA  1 
ATOM   1107 C C   . HIS   B 1 49 ? 20.482  -8.204  -25.043 1.00 34.89  ? 48  HIS   B C   1 
ATOM   1108 O O   . HIS   B 1 49 ? 21.452  -7.581  -24.625 1.00 41.22  ? 48  HIS   B O   1 
ATOM   1109 C CB  . HIS   B 1 49 ? 19.265  -5.970  -25.310 1.00 34.58  ? 48  HIS   B CB  1 
ATOM   1110 C CG  . HIS   B 1 49 ? 18.050  -5.302  -25.850 1.00 34.95  ? 48  HIS   B CG  1 
ATOM   1111 N ND1 . HIS   B 1 49 ? 17.347  -4.382  -25.112 1.00 36.11  ? 48  HIS   B ND1 1 
ATOM   1112 C CD2 . HIS   B 1 49 ? 17.376  -5.433  -27.021 1.00 32.90  ? 48  HIS   B CD2 1 
ATOM   1113 C CE1 . HIS   B 1 49 ? 16.279  -3.997  -25.814 1.00 42.09  ? 48  HIS   B CE1 1 
ATOM   1114 N NE2 . HIS   B 1 49 ? 16.293  -4.599  -26.990 1.00 35.28  ? 48  HIS   B NE2 1 
ATOM   1115 N N   . GLU   B 1 50 ? 20.370  -9.535  -24.973 1.00 33.38  ? 49  GLU   B N   1 
ATOM   1116 C CA  . GLU   B 1 50 ? 21.460  -10.350 -24.462 1.00 34.50  ? 49  GLU   B CA  1 
ATOM   1117 C C   . GLU   B 1 50 ? 22.454  -10.667 -25.588 1.00 35.51  ? 49  GLU   B C   1 
ATOM   1118 O O   . GLU   B 1 50 ? 22.155  -10.485 -26.770 1.00 33.58  ? 49  GLU   B O   1 
ATOM   1119 C CB  . GLU   B 1 50 ? 20.894  -11.675 -23.962 1.00 35.36  ? 49  GLU   B CB  1 
ATOM   1120 C CG  . GLU   B 1 50 ? 20.068  -11.499 -22.687 1.00 34.77  ? 49  GLU   B CG  1 
ATOM   1121 C CD  . GLU   B 1 50 ? 19.338  -12.787 -22.359 1.00 36.00  ? 49  GLU   B CD  1 
ATOM   1122 O OE1 . GLU   B 1 50 ? 18.428  -13.145 -23.130 1.00 39.13  ? 49  GLU   B OE1 1 
ATOM   1123 O OE2 . GLU   B 1 50 ? 19.693  -13.450 -21.375 1.00 35.34  ? 49  GLU   B OE2 1 
ATOM   1124 N N   . THR   B 1 51 ? 23.626  -11.166 -25.205 1.00 30.88  ? 50  THR   B N   1 
ATOM   1125 C CA  . THR   B 1 51 ? 24.618  -11.635 -26.168 1.00 34.52  ? 50  THR   B CA  1 
ATOM   1126 C C   . THR   B 1 51 ? 25.038  -13.059 -25.807 1.00 37.36  ? 50  THR   B C   1 
ATOM   1127 O O   . THR   B 1 51 ? 24.920  -13.465 -24.647 1.00 36.76  ? 50  THR   B O   1 
ATOM   1128 C CB  . THR   B 1 51 ? 25.815  -10.685 -26.280 1.00 37.30  ? 50  THR   B CB  1 
ATOM   1129 O OG1 . THR   B 1 51 ? 26.392  -10.731 -24.983 1.00 38.65  ? 50  THR   B OG1 1 
ATOM   1130 C CG2 . THR   B 1 51 ? 25.427  -9.257  -26.635 1.00 32.74  ? 50  THR   B CG2 1 
ATOM   1131 N N   . ALA   B 1 52 ? 25.547  -13.798 -26.811 1.00 33.46  ? 51  ALA   B N   1 
ATOM   1132 C CA  . ALA   B 1 52 ? 26.196  -15.082 -26.587 1.00 35.67  ? 51  ALA   B CA  1 
ATOM   1133 C C   . ALA   B 1 52 ? 27.075  -15.418 -27.786 1.00 34.14  ? 51  ALA   B C   1 
ATOM   1134 O O   . ALA   B 1 52 ? 27.031  -14.713 -28.794 1.00 35.04  ? 51  ALA   B O   1 
ATOM   1135 C CB  . ALA   B 1 52 ? 25.163  -16.152 -26.324 1.00 33.50  ? 51  ALA   B CB  1 
ATOM   1136 N N   . PHE   B 1 53 ? 27.852  -16.498 -27.671 1.00 33.31  ? 52  PHE   B N   1 
ATOM   1137 C CA  . PHE   B 1 53 ? 28.595  -16.964 -28.832 1.00 36.68  ? 52  PHE   B CA  1 
ATOM   1138 C C   . PHE   B 1 53 ? 27.918  -18.221 -29.373 1.00 35.22  ? 52  PHE   B C   1 
ATOM   1139 O O   . PHE   B 1 53 ? 27.707  -19.180 -28.623 1.00 38.91  ? 52  PHE   B O   1 
ATOM   1140 C CB  . PHE   B 1 53 ? 30.079  -17.230 -28.545 1.00 34.88  ? 52  PHE   B CB  1 
ATOM   1141 C CG  . PHE   B 1 53 ? 30.873  -16.003 -28.121 1.00 41.17  ? 52  PHE   B CG  1 
ATOM   1142 C CD1 . PHE   B 1 53 ? 31.105  -14.961 -29.015 1.00 43.10  ? 52  PHE   B CD1 1 
ATOM   1143 C CD2 . PHE   B 1 53 ? 31.405  -15.907 -26.841 1.00 44.32  ? 52  PHE   B CD2 1 
ATOM   1144 C CE1 . PHE   B 1 53 ? 31.825  -13.835 -28.637 1.00 40.75  ? 52  PHE   B CE1 1 
ATOM   1145 C CE2 . PHE   B 1 53 ? 32.133  -14.782 -26.458 1.00 42.23  ? 52  PHE   B CE2 1 
ATOM   1146 C CZ  . PHE   B 1 53 ? 32.343  -13.756 -27.350 1.00 39.16  ? 52  PHE   B CZ  1 
ATOM   1147 N N   . LEU   B 1 54 ? 27.636  -18.243 -30.689 1.00 31.42  ? 53  LEU   B N   1 
ATOM   1148 C CA  . LEU   B 1 54 ? 27.065  -19.449 -31.283 1.00 29.73  ? 53  LEU   B CA  1 
ATOM   1149 C C   . LEU   B 1 54 ? 27.753  -19.808 -32.603 1.00 30.42  ? 53  LEU   B C   1 
ATOM   1150 O O   . LEU   B 1 54 ? 28.220  -18.921 -33.328 1.00 32.76  ? 53  LEU   B O   1 
ATOM   1151 C CB  . LEU   B 1 54 ? 25.571  -19.267 -31.538 1.00 29.31  ? 53  LEU   B CB  1 
ATOM   1152 C CG  . LEU   B 1 54 ? 24.652  -19.199 -30.318 1.00 32.58  ? 53  LEU   B CG  1 
ATOM   1153 C CD1 . LEU   B 1 54 ? 23.315  -18.706 -30.848 1.00 30.76  ? 53  LEU   B CD1 1 
ATOM   1154 C CD2 . LEU   B 1 54 ? 24.577  -20.566 -29.622 1.00 32.75  ? 53  LEU   B CD2 1 
ATOM   1155 N N   . GLY   B 1 55 ? 27.728  -21.115 -32.913 1.00 33.20  ? 54  GLY   B N   1 
ATOM   1156 C CA  . GLY   B 1 55 ? 28.239  -21.677 -34.158 1.00 29.11  ? 54  GLY   B CA  1 
ATOM   1157 C C   . GLY   B 1 55 ? 27.144  -21.716 -35.223 1.00 31.90  ? 54  GLY   B C   1 
ATOM   1158 O O   . GLY   B 1 55 ? 25.947  -21.581 -34.896 1.00 29.96  ? 54  GLY   B O   1 
ATOM   1159 N N   . PRO   B 1 56 ? 27.497  -21.904 -36.521 1.00 31.55  ? 55  PRO   B N   1 
ATOM   1160 C CA  . PRO   B 1 56 ? 26.500  -21.940 -37.591 1.00 31.40  ? 55  PRO   B CA  1 
ATOM   1161 C C   . PRO   B 1 56 ? 25.339  -22.924 -37.470 1.00 28.57  ? 55  PRO   B C   1 
ATOM   1162 O O   . PRO   B 1 56 ? 24.273  -22.681 -38.017 1.00 28.22  ? 55  PRO   B O   1 
ATOM   1163 C CB  . PRO   B 1 56 ? 27.312  -22.177 -38.876 1.00 32.19  ? 55  PRO   B CB  1 
ATOM   1164 C CG  . PRO   B 1 56 ? 28.749  -22.044 -38.499 1.00 33.37  ? 55  PRO   B CG  1 
ATOM   1165 C CD  . PRO   B 1 56 ? 28.870  -22.119 -37.007 1.00 30.77  ? 55  PRO   B CD  1 
ATOM   1166 N N   . LYS   B 1 57 ? 25.510  -24.029 -36.731 1.00 30.35  ? 56  LYS   B N   1 
ATOM   1167 C CA  . LYS   B 1 57 ? 24.438  -25.012 -36.648 1.00 30.83  ? 56  LYS   B CA  1 
ATOM   1168 C C   . LYS   B 1 57 ? 23.182  -24.401 -36.003 1.00 28.59  ? 56  LYS   B C   1 
ATOM   1169 O O   . LYS   B 1 57 ? 22.069  -24.876 -36.228 1.00 29.06  ? 56  LYS   B O   1 
ATOM   1170 C CB  . LYS   B 1 57 ? 24.924  -26.252 -35.889 1.00 32.82  ? 56  LYS   B CB  1 
ATOM   1171 C CG  . LYS   B 1 57 ? 25.044  -26.164 -34.377 1.00 38.01  ? 56  LYS   B CG  1 
ATOM   1172 C CD  . LYS   B 1 57 ? 25.109  -27.564 -33.768 1.00 40.97  ? 56  LYS   B CD  1 
ATOM   1173 C CE  . LYS   B 1 57 ? 25.345  -27.605 -32.268 1.00 41.79  ? 56  LYS   B CE  1 
ATOM   1174 N NZ  . LYS   B 1 57 ? 24.256  -27.041 -31.469 1.00 40.91  ? 56  LYS   B NZ  1 
ATOM   1175 N N   . ASP   B 1 58 ? 23.371  -23.318 -35.236 1.00 27.26  ? 57  ASP   B N   1 
ATOM   1176 C CA  . ASP   B 1 58 ? 22.302  -22.737 -34.438 1.00 28.22  ? 57  ASP   B CA  1 
ATOM   1177 C C   . ASP   B 1 58 ? 21.852  -21.400 -35.012 1.00 27.80  ? 57  ASP   B C   1 
ATOM   1178 O O   . ASP   B 1 58 ? 21.112  -20.670 -34.346 1.00 27.43  ? 57  ASP   B O   1 
ATOM   1179 C CB  . ASP   B 1 58 ? 22.695  -22.650 -32.971 1.00 29.32  ? 57  ASP   B CB  1 
ATOM   1180 C CG  . ASP   B 1 58 ? 22.830  -23.983 -32.257 1.00 33.79  ? 57  ASP   B CG  1 
ATOM   1181 O OD1 . ASP   B 1 58 ? 21.912  -24.811 -32.394 1.00 34.08  ? 57  ASP   B OD1 1 
ATOM   1182 O OD2 . ASP   B 1 58 ? 23.852  -24.157 -31.570 1.00 38.28  ? 57  ASP   B OD2 1 
ATOM   1183 N N   . LEU   B 1 59 ? 22.234  -21.136 -36.270 1.00 27.52  ? 58  LEU   B N   1 
ATOM   1184 C CA  . LEU   B 1 59 ? 22.071  -19.819 -36.877 1.00 25.27  ? 58  LEU   B CA  1 
ATOM   1185 C C   . LEU   B 1 59 ? 21.346  -19.939 -38.209 1.00 26.45  ? 58  LEU   B C   1 
ATOM   1186 O O   . LEU   B 1 59 ? 21.816  -20.601 -39.139 1.00 27.71  ? 58  LEU   B O   1 
ATOM   1187 C CB  . LEU   B 1 59 ? 23.412  -19.117 -37.076 1.00 28.95  ? 58  LEU   B CB  1 
ATOM   1188 C CG  . LEU   B 1 59 ? 24.213  -18.730 -35.830 1.00 27.50  ? 58  LEU   B CG  1 
ATOM   1189 C CD1 . LEU   B 1 59 ? 25.489  -17.975 -36.219 1.00 30.87  ? 58  LEU   B CD1 1 
ATOM   1190 C CD2 . LEU   B 1 59 ? 23.477  -17.877 -34.819 1.00 26.77  ? 58  LEU   B CD2 1 
ATOM   1191 N N   . PHE   B 1 60 ? 20.163  -19.340 -38.256 1.00 22.88  ? 59  PHE   B N   1 
ATOM   1192 C CA  . PHE   B 1 60 ? 19.212  -19.516 -39.329 1.00 25.76  ? 59  PHE   B CA  1 
ATOM   1193 C C   . PHE   B 1 60 ? 18.991  -18.172 -40.021 1.00 26.50  ? 59  PHE   B C   1 
ATOM   1194 O O   . PHE   B 1 60 ? 18.332  -17.272 -39.481 1.00 28.28  ? 59  PHE   B O   1 
ATOM   1195 C CB  . PHE   B 1 60 ? 17.881  -20.022 -38.759 1.00 25.15  ? 59  PHE   B CB  1 
ATOM   1196 C CG  . PHE   B 1 60 ? 17.961  -21.441 -38.209 1.00 24.24  ? 59  PHE   B CG  1 
ATOM   1197 C CD1 . PHE   B 1 60 ? 18.473  -21.666 -36.929 1.00 27.77  ? 59  PHE   B CD1 1 
ATOM   1198 C CD2 . PHE   B 1 60 ? 17.553  -22.523 -38.969 1.00 29.42  ? 59  PHE   B CD2 1 
ATOM   1199 C CE1 . PHE   B 1 60 ? 18.606  -22.957 -36.422 1.00 28.51  ? 59  PHE   B CE1 1 
ATOM   1200 C CE2 . PHE   B 1 60 ? 17.668  -23.821 -38.454 1.00 30.99  ? 59  PHE   B CE2 1 
ATOM   1201 C CZ  . PHE   B 1 60 ? 18.201  -24.030 -37.198 1.00 28.84  ? 59  PHE   B CZ  1 
ATOM   1202 N N   . PRO   B 1 61 ? 19.509  -17.984 -41.259 1.00 31.24  ? 60  PRO   B N   1 
ATOM   1203 C CA  . PRO   B 1 61 ? 19.242  -16.731 -41.987 1.00 27.53  ? 60  PRO   B CA  1 
ATOM   1204 C C   . PRO   B 1 61 ? 17.789  -16.249 -41.923 1.00 27.00  ? 60  PRO   B C   1 
ATOM   1205 O O   . PRO   B 1 61 ? 16.841  -17.028 -42.118 1.00 28.52  ? 60  PRO   B O   1 
ATOM   1206 C CB  . PRO   B 1 61 ? 19.695  -17.087 -43.431 1.00 29.13  ? 60  PRO   B CB  1 
ATOM   1207 C CG  . PRO   B 1 61 ? 20.797  -18.089 -43.229 1.00 34.12  ? 60  PRO   B CG  1 
ATOM   1208 C CD  . PRO   B 1 61 ? 20.356  -18.946 -42.007 1.00 30.65  ? 60  PRO   B CD  1 
ATOM   1209 N N   . TYR   B 1 62 ? 17.605  -14.944 -41.626 1.00 29.80  ? 61  TYR   B N   1 
ATOM   1210 C CA  . TYR   B 1 62 ? 16.305  -14.382 -41.285 1.00 30.33  ? 61  TYR   B CA  1 
ATOM   1211 C C   . TYR   B 1 62 ? 15.312  -14.440 -42.437 1.00 29.58  ? 61  TYR   B C   1 
ATOM   1212 O O   . TYR   B 1 62 ? 14.151  -14.816 -42.228 1.00 34.27  ? 61  TYR   B O   1 
ATOM   1213 C CB  . TYR   B 1 62 ? 16.446  -12.946 -40.762 1.00 33.10  ? 61  TYR   B CB  1 
ATOM   1214 C CG  . TYR   B 1 62 ? 15.132  -12.216 -40.515 1.00 34.35  ? 61  TYR   B CG  1 
ATOM   1215 C CD1 . TYR   B 1 62 ? 14.414  -12.404 -39.345 1.00 35.02  ? 61  TYR   B CD1 1 
ATOM   1216 C CD2 . TYR   B 1 62 ? 14.664  -11.278 -41.428 1.00 40.30  ? 61  TYR   B CD2 1 
ATOM   1217 C CE1 . TYR   B 1 62 ? 13.244  -11.700 -39.105 1.00 39.40  ? 61  TYR   B CE1 1 
ATOM   1218 C CE2 . TYR   B 1 62 ? 13.495  -10.571 -41.205 1.00 43.66  ? 61  TYR   B CE2 1 
ATOM   1219 C CZ  . TYR   B 1 62 ? 12.784  -10.794 -40.041 1.00 40.93  ? 61  TYR   B CZ  1 
ATOM   1220 O OH  . TYR   B 1 62 ? 11.648  -10.085 -39.830 1.00 43.03  ? 61  TYR   B OH  1 
ATOM   1221 N N   . ASP   B 1 63 ? 15.767  -14.080 -43.656 1.00 37.06  ? 62  ASP   B N   1 
ATOM   1222 C CA  . ASP   B 1 63 ? 14.886  -14.067 -44.822 1.00 38.90  ? 62  ASP   B CA  1 
ATOM   1223 C C   . ASP   B 1 63 ? 14.302  -15.440 -45.120 1.00 34.23  ? 62  ASP   B C   1 
ATOM   1224 O O   . ASP   B 1 63 ? 13.098  -15.557 -45.336 1.00 40.72  ? 62  ASP   B O   1 
ATOM   1225 C CB  . ASP   B 1 63 ? 15.557  -13.544 -46.078 1.00 47.32  ? 62  ASP   B CB  1 
ATOM   1226 C CG  . ASP   B 1 63 ? 15.288  -12.076 -46.343 1.00 55.34  ? 62  ASP   B CG  1 
ATOM   1227 O OD1 . ASP   B 1 63 ? 14.899  -11.388 -45.374 1.00 48.44  ? 62  ASP   B OD1 1 
ATOM   1228 O OD2 . ASP   B 1 63 ? 15.420  -11.659 -47.518 1.00 59.99  ? 62  ASP   B OD2 1 
ATOM   1229 N N   . LYS   B 1 64 ? 15.170  -16.449 -45.145 1.00 36.53  ? 63  LYS   B N   1 
ATOM   1230 C CA  . LYS   B 1 64 ? 14.792  -17.823 -45.400 1.00 41.22  ? 63  LYS   B CA  1 
ATOM   1231 C C   . LYS   B 1 64 ? 13.807  -18.321 -44.343 1.00 39.06  ? 63  LYS   B C   1 
ATOM   1232 O O   . LYS   B 1 64 ? 12.846  -19.010 -44.679 1.00 37.93  ? 63  LYS   B O   1 
ATOM   1233 C CB  . LYS   B 1 64 ? 16.037  -18.716 -45.433 1.00 40.58  ? 63  LYS   B CB  1 
ATOM   1234 C CG  . LYS   B 1 64 ? 15.756  -20.124 -45.916 1.00 39.68  ? 63  LYS   B CG  1 
ATOM   1235 C CD  . LYS   B 1 64 ? 16.950  -21.059 -45.773 1.00 47.45  ? 63  LYS   B CD  1 
ATOM   1236 C CE  . LYS   B 1 64 ? 16.795  -22.371 -46.506 1.00 43.52  ? 63  LYS   B CE  1 
ATOM   1237 N NZ  . LYS   B 1 64 ? 15.430  -22.889 -46.472 1.00 37.16  ? 63  LYS   B NZ  1 
ATOM   1238 N N   . SER   B 1 65 ? 14.021  -17.950 -43.077 1.00 38.38  ? 64  SER   B N   1 
ATOM   1239 C CA  . SER   B 1 65 ? 13.306  -18.648 -42.009 1.00 35.99  ? 64  SER   B CA  1 
ATOM   1240 C C   . SER   B 1 65 ? 12.204  -17.842 -41.293 1.00 35.42  ? 64  SER   B C   1 
ATOM   1241 O O   . SER   B 1 65 ? 11.575  -18.366 -40.384 1.00 36.62  ? 64  SER   B O   1 
ATOM   1242 C CB  . SER   B 1 65 ? 14.276  -19.282 -41.056 1.00 38.56  ? 64  SER   B CB  1 
ATOM   1243 O OG  . SER   B 1 65 ? 15.151  -18.301 -40.539 1.00 49.71  ? 64  SER   B OG  1 
ATOM   1244 N N   . LYS   B 1 66 ? 11.900  -16.606 -41.707 1.00 36.15  ? 65  LYS   B N   1 
ATOM   1245 C CA  . LYS   B 1 66 ? 11.034  -15.758 -40.886 1.00 37.00  ? 65  LYS   B CA  1 
ATOM   1246 C C   . LYS   B 1 66 ? 9.582   -16.245 -40.817 1.00 38.87  ? 65  LYS   B C   1 
ATOM   1247 O O   . LYS   B 1 66 ? 8.896   -15.994 -39.826 1.00 39.58  ? 65  LYS   B O   1 
ATOM   1248 C CB  . LYS   B 1 66 ? 11.065  -14.263 -41.238 1.00 35.60  ? 65  LYS   B CB  1 
ATOM   1249 C CG  . LYS   B 1 66 ? 10.570  -13.893 -42.642 1.00 38.39  ? 65  LYS   B CG  1 
ATOM   1250 N N   . ASP   B 1 67 ? 9.081   -16.913 -41.853 1.00 36.54  ? 66  ASP   B N   1 
ATOM   1251 C CA  . ASP   B 1 67 ? 7.669   -17.259 -41.779 1.00 46.75  ? 66  ASP   B CA  1 
ATOM   1252 C C   . ASP   B 1 67 ? 7.481   -18.510 -40.917 1.00 43.63  ? 66  ASP   B C   1 
ATOM   1253 O O   . ASP   B 1 67 ? 6.396   -18.728 -40.371 1.00 44.48  ? 66  ASP   B O   1 
ATOM   1254 C CB  . ASP   B 1 67 ? 6.969   -17.129 -43.122 1.00 57.08  ? 66  ASP   B CB  1 
ATOM   1255 C CG  . ASP   B 1 67 ? 7.519   -18.019 -44.218 1.00 62.72  ? 66  ASP   B CG  1 
ATOM   1256 O OD1 . ASP   B 1 67 ? 7.203   -17.761 -45.407 1.00 72.57  ? 66  ASP   B OD1 1 
ATOM   1257 O OD2 . ASP   B 1 67 ? 8.243   -18.967 -43.868 1.00 66.74  ? 66  ASP   B OD2 1 
ATOM   1258 N N   . LYS   B 1 68 ? 8.569   -19.276 -40.758 1.00 40.87  ? 67  LYS   B N   1 
ATOM   1259 C CA  . LYS   B 1 68 ? 8.618   -20.410 -39.849 1.00 35.72  ? 67  LYS   B CA  1 
ATOM   1260 C C   . LYS   B 1 68 ? 8.843   -19.958 -38.402 1.00 38.18  ? 67  LYS   B C   1 
ATOM   1261 O O   . LYS   B 1 68 ? 8.131   -20.430 -37.519 1.00 41.12  ? 67  LYS   B O   1 
ATOM   1262 C CB  . LYS   B 1 68 ? 9.703   -21.377 -40.332 1.00 38.05  ? 67  LYS   B CB  1 
ATOM   1263 C CG  . LYS   B 1 68 ? 9.788   -22.684 -39.561 1.00 42.77  ? 67  LYS   B CG  1 
ATOM   1264 C CD  . LYS   B 1 68 ? 10.919  -23.550 -40.105 1.00 50.89  ? 67  LYS   B CD  1 
ATOM   1265 C CE  . LYS   B 1 68 ? 11.136  -24.817 -39.325 1.00 62.61  ? 67  LYS   B CE  1 
ATOM   1266 N NZ  . LYS   B 1 68 ? 9.992   -25.730 -39.403 1.00 64.10  ? 67  LYS   B NZ  1 
ATOM   1267 N N   . TYR   B 1 69 ? 9.830   -19.076 -38.135 1.00 30.89  ? 68  TYR   B N   1 
ATOM   1268 C CA  . TYR   B 1 69 ? 10.231  -18.808 -36.751 1.00 26.85  ? 68  TYR   B CA  1 
ATOM   1269 C C   . TYR   B 1 69 ? 9.745   -17.452 -36.241 1.00 30.81  ? 68  TYR   B C   1 
ATOM   1270 O O   . TYR   B 1 69 ? 9.903   -17.148 -35.050 1.00 31.84  ? 68  TYR   B O   1 
ATOM   1271 C CB  . TYR   B 1 69 ? 11.759  -18.887 -36.620 1.00 26.67  ? 68  TYR   B CB  1 
ATOM   1272 C CG  . TYR   B 1 69 ? 12.353  -20.259 -36.913 1.00 31.28  ? 68  TYR   B CG  1 
ATOM   1273 C CD1 . TYR   B 1 69 ? 11.818  -21.420 -36.353 1.00 33.71  ? 68  TYR   B CD1 1 
ATOM   1274 C CD2 . TYR   B 1 69 ? 13.453  -20.406 -37.755 1.00 35.48  ? 68  TYR   B CD2 1 
ATOM   1275 C CE1 . TYR   B 1 69 ? 12.354  -22.677 -36.613 1.00 33.99  ? 68  TYR   B CE1 1 
ATOM   1276 C CE2 . TYR   B 1 69 ? 13.989  -21.655 -38.029 1.00 35.81  ? 68  TYR   B CE2 1 
ATOM   1277 C CZ  . TYR   B 1 69 ? 13.446  -22.793 -37.451 1.00 33.05  ? 68  TYR   B CZ  1 
ATOM   1278 O OH  . TYR   B 1 69 ? 13.959  -24.020 -37.745 1.00 34.14  ? 68  TYR   B OH  1 
ATOM   1279 N N   . GLY   B 1 70 ? 9.194   -16.626 -37.142 1.00 31.51  ? 69  GLY   B N   1 
ATOM   1280 C CA  . GLY   B 1 70 ? 8.896   -15.231 -36.858 1.00 33.15  ? 69  GLY   B CA  1 
ATOM   1281 C C   . GLY   B 1 70 ? 7.485   -15.016 -36.305 1.00 37.75  ? 69  GLY   B C   1 
ATOM   1282 O O   . GLY   B 1 70 ? 6.902   -13.977 -36.557 1.00 36.71  ? 69  GLY   B O   1 
ATOM   1283 N N   . LYS   B 1 71 ? 6.935   -15.992 -35.570 1.00 39.44  ? 70  LYS   B N   1 
ATOM   1284 C CA  . LYS   B 1 71 ? 5.569   -15.902 -35.075 1.00 41.26  ? 70  LYS   B CA  1 
ATOM   1285 C C   . LYS   B 1 71 ? 5.619   -15.483 -33.618 1.00 41.23  ? 70  LYS   B C   1 
ATOM   1286 O O   . LYS   B 1 71 ? 6.503   -15.921 -32.883 1.00 38.43  ? 70  LYS   B O   1 
ATOM   1287 C CB  . LYS   B 1 71 ? 4.821   -17.241 -35.076 1.00 45.33  ? 70  LYS   B CB  1 
ATOM   1288 C CG  . LYS   B 1 71 ? 3.867   -17.542 -36.232 1.00 51.82  ? 70  LYS   B CG  1 
ATOM   1289 C CD  . LYS   B 1 71 ? 4.519   -17.797 -37.580 1.00 51.71  ? 70  LYS   B CD  1 
ATOM   1290 C CE  . LYS   B 1 71 ? 3.495   -18.150 -38.624 1.00 51.53  ? 70  LYS   B CE  1 
ATOM   1291 N NZ  . LYS   B 1 71 ? 4.040   -17.929 -39.968 1.00 57.33  ? 70  LYS   B NZ  1 
ATOM   1292 N N   . PRO   B 1 72 ? 4.674   -14.640 -33.141 1.00 40.16  ? 71  PRO   B N   1 
ATOM   1293 C CA  . PRO   B 1 72 ? 4.697   -14.231 -31.737 1.00 39.42  ? 71  PRO   B CA  1 
ATOM   1294 C C   . PRO   B 1 72 ? 4.480   -15.410 -30.789 1.00 38.43  ? 71  PRO   B C   1 
ATOM   1295 O O   . PRO   B 1 72 ? 3.890   -16.419 -31.179 1.00 37.42  ? 71  PRO   B O   1 
ATOM   1296 C CB  . PRO   B 1 72 ? 3.654   -13.101 -31.610 1.00 39.73  ? 71  PRO   B CB  1 
ATOM   1297 C CG  . PRO   B 1 72 ? 3.274   -12.784 -33.045 1.00 46.60  ? 71  PRO   B CG  1 
ATOM   1298 C CD  . PRO   B 1 72 ? 3.596   -14.005 -33.919 1.00 41.53  ? 71  PRO   B CD  1 
ATOM   1299 N N   . ASN   B 1 73 ? 5.009   -15.282 -29.564 1.00 37.79  ? 72  ASN   B N   1 
ATOM   1300 C CA  . ASN   B 1 73 ? 4.803   -16.250 -28.497 1.00 37.61  ? 72  ASN   B CA  1 
ATOM   1301 C C   . ASN   B 1 73 ? 4.771   -15.528 -27.146 1.00 39.18  ? 72  ASN   B C   1 
ATOM   1302 O O   . ASN   B 1 73 ? 4.832   -14.293 -27.095 1.00 44.67  ? 72  ASN   B O   1 
ATOM   1303 C CB  . ASN   B 1 73 ? 5.813   -17.395 -28.564 1.00 37.58  ? 72  ASN   B CB  1 
ATOM   1304 C CG  . ASN   B 1 73 ? 7.230   -16.952 -28.311 1.00 37.65  ? 72  ASN   B CG  1 
ATOM   1305 O OD1 . ASN   B 1 73 ? 7.482   -16.172 -27.388 1.00 36.62  ? 72  ASN   B OD1 1 
ATOM   1306 N ND2 . ASN   B 1 73 ? 8.164   -17.441 -29.118 1.00 34.57  ? 72  ASN   B ND2 1 
ATOM   1307 N N   . LYS   B 1 74 ? 4.736   -16.304 -26.054 1.00 40.71  ? 73  LYS   B N   1 
ATOM   1308 C CA  . LYS   B 1 74 ? 4.576   -15.759 -24.705 1.00 45.98  ? 73  LYS   B CA  1 
ATOM   1309 C C   . LYS   B 1 74 ? 5.912   -15.707 -23.940 1.00 41.65  ? 73  LYS   B C   1 
ATOM   1310 O O   . LYS   B 1 74 ? 5.944   -15.581 -22.711 1.00 39.61  ? 73  LYS   B O   1 
ATOM   1311 C CB  . LYS   B 1 74 ? 3.458   -16.535 -23.991 1.00 45.77  ? 73  LYS   B CB  1 
ATOM   1312 N N   . ARG   B 1 75 ? 7.043   -15.788 -24.653 1.00 31.05  ? 74  ARG   B N   1 
ATOM   1313 C CA  . ARG   B 1 75 ? 8.329   -15.637 -23.979 1.00 32.20  ? 74  ARG   B CA  1 
ATOM   1314 C C   . ARG   B 1 75 ? 8.653   -14.145 -23.812 1.00 31.28  ? 74  ARG   B C   1 
ATOM   1315 O O   . ARG   B 1 75 ? 8.555   -13.357 -24.754 1.00 33.96  ? 74  ARG   B O   1 
ATOM   1316 C CB  . ARG   B 1 75 ? 9.474   -16.449 -24.604 1.00 35.31  ? 74  ARG   B CB  1 
ATOM   1317 C CG  . ARG   B 1 75 ? 9.358   -17.952 -24.811 1.00 36.36  ? 74  ARG   B CG  1 
ATOM   1318 C CD  . ARG   B 1 75 ? 9.194   -18.717 -23.508 1.00 37.58  ? 74  ARG   B CD  1 
ATOM   1319 N NE  . ARG   B 1 75 ? 9.341   -20.142 -23.815 1.00 38.21  ? 74  ARG   B NE  1 
ATOM   1320 C CZ  . ARG   B 1 75 ? 10.410  -20.879 -23.624 1.00 37.48  ? 74  ARG   B CZ  1 
ATOM   1321 N NH1 . ARG   B 1 75 ? 11.532  -20.354 -23.155 1.00 38.72  ? 74  ARG   B NH1 1 
ATOM   1322 N NH2 . ARG   B 1 75 ? 10.377  -22.146 -24.003 1.00 43.99  ? 74  ARG   B NH2 1 
ATOM   1323 N N   . LYS   B 1 76 ? 9.034   -13.765 -22.589 1.00 32.09  ? 75  LYS   B N   1 
ATOM   1324 C CA  . LYS   B 1 76 ? 9.454   -12.412 -22.259 1.00 31.34  ? 75  LYS   B CA  1 
ATOM   1325 C C   . LYS   B 1 76 ? 10.562  -11.918 -23.196 1.00 28.54  ? 75  LYS   B C   1 
ATOM   1326 O O   . LYS   B 1 76 ? 11.668  -12.494 -23.227 1.00 30.21  ? 75  LYS   B O   1 
ATOM   1327 C CB  . LYS   B 1 76 ? 10.097  -12.385 -20.865 1.00 36.89  ? 75  LYS   B CB  1 
ATOM   1328 C CG  . LYS   B 1 76 ? 10.434  -10.960 -20.401 1.00 37.55  ? 75  LYS   B CG  1 
ATOM   1329 C CD  . LYS   B 1 76 ? 10.843  -10.853 -18.940 1.00 40.78  ? 75  LYS   B CD  1 
ATOM   1330 C CE  . LYS   B 1 76 ? 11.174  -9.456  -18.494 1.00 43.02  ? 75  LYS   B CE  1 
ATOM   1331 N NZ  . LYS   B 1 76 ? 11.645  -9.491  -17.102 1.00 49.12  ? 75  LYS   B NZ  1 
ATOM   1332 N N   . GLY   B 1 77 ? 10.244  -10.823 -23.896 1.00 28.69  ? 76  GLY   B N   1 
ATOM   1333 C CA  . GLY   B 1 77 ? 11.222  -10.178 -24.780 1.00 29.87  ? 76  GLY   B CA  1 
ATOM   1334 C C   . GLY   B 1 77 ? 11.097  -10.643 -26.239 1.00 29.30  ? 76  GLY   B C   1 
ATOM   1335 O O   . GLY   B 1 77 ? 11.625  -9.997  -27.149 1.00 30.15  ? 76  GLY   B O   1 
ATOM   1336 N N   . PHE   B 1 78 ? 10.406  -11.759 -26.485 1.00 28.34  ? 77  PHE   B N   1 
ATOM   1337 C CA  . PHE   B 1 78 ? 10.308  -12.261 -27.860 1.00 28.18  ? 77  PHE   B CA  1 
ATOM   1338 C C   . PHE   B 1 78 ? 9.588   -11.297 -28.810 1.00 30.76  ? 77  PHE   B C   1 
ATOM   1339 O O   . PHE   B 1 78 ? 10.083  -11.000 -29.912 1.00 27.55  ? 77  PHE   B O   1 
ATOM   1340 C CB  . PHE   B 1 78 ? 9.556   -13.586 -27.920 1.00 28.31  ? 77  PHE   B CB  1 
ATOM   1341 C CG  . PHE   B 1 78 ? 9.845   -14.335 -29.216 1.00 29.16  ? 77  PHE   B CG  1 
ATOM   1342 C CD1 . PHE   B 1 78 ? 10.949  -15.172 -29.299 1.00 26.65  ? 77  PHE   B CD1 1 
ATOM   1343 C CD2 . PHE   B 1 78 ? 8.994   -14.223 -30.310 1.00 30.06  ? 77  PHE   B CD2 1 
ATOM   1344 C CE1 . PHE   B 1 78 ? 11.203  -15.889 -30.477 1.00 28.76  ? 77  PHE   B CE1 1 
ATOM   1345 C CE2 . PHE   B 1 78 ? 9.248   -14.930 -31.478 1.00 30.23  ? 77  PHE   B CE2 1 
ATOM   1346 C CZ  . PHE   B 1 78 ? 10.358  -15.762 -31.553 1.00 30.15  ? 77  PHE   B CZ  1 
ATOM   1347 N N   . ASN   B 1 79 ? 8.367   -10.871 -28.454 1.00 28.87  ? 78  ASN   B N   1 
ATOM   1348 C CA  . ASN   B 1 79 ? 7.607   -10.042 -29.371 1.00 33.09  ? 78  ASN   B CA  1 
ATOM   1349 C C   . ASN   B 1 79 ? 8.311   -8.696  -29.548 1.00 32.58  ? 78  ASN   B C   1 
ATOM   1350 O O   . ASN   B 1 79 ? 8.292   -8.130  -30.645 1.00 34.16  ? 78  ASN   B O   1 
ATOM   1351 C CB  . ASN   B 1 79 ? 6.136   -9.900  -28.984 1.00 35.23  ? 78  ASN   B CB  1 
ATOM   1352 C CG  . ASN   B 1 79 ? 5.362   -11.203 -29.034 1.00 40.06  ? 78  ASN   B CG  1 
ATOM   1353 O OD1 . ASN   B 1 79 ? 5.886   -12.228 -29.480 1.00 38.05  ? 78  ASN   B OD1 1 
ATOM   1354 N ND2 . ASN   B 1 79 ? 4.121   -11.199 -28.552 1.00 37.27  ? 78  ASN   B ND2 1 
ATOM   1355 N N   . GLU   B 1 80 ? 8.972   -8.226  -28.492 1.00 30.43  ? 79  GLU   B N   1 
ATOM   1356 C CA  . GLU   B 1 80 ? 9.770   -7.015  -28.592 1.00 31.33  ? 79  GLU   B CA  1 
ATOM   1357 C C   . GLU   B 1 80 ? 10.862  -7.234  -29.644 1.00 31.66  ? 79  GLU   B C   1 
ATOM   1358 O O   . GLU   B 1 80 ? 11.094  -6.358  -30.480 1.00 29.34  ? 79  GLU   B O   1 
ATOM   1359 C CB  . GLU   B 1 80 ? 10.431  -6.612  -27.282 1.00 35.30  ? 79  GLU   B CB  1 
ATOM   1360 C CG  . GLU   B 1 80 ? 9.513   -5.745  -26.423 1.00 45.57  ? 79  GLU   B CG  1 
ATOM   1361 N N   . GLY   B 1 81 ? 11.524  -8.405  -29.570 1.00 31.75  ? 80  GLY   B N   1 
ATOM   1362 C CA  . GLY   B 1 81 ? 12.603  -8.784  -30.480 1.00 29.37  ? 80  GLY   B CA  1 
ATOM   1363 C C   . GLY   B 1 81 ? 12.135  -8.841  -31.930 1.00 30.62  ? 80  GLY   B C   1 
ATOM   1364 O O   . GLY   B 1 81 ? 12.877  -8.450  -32.852 1.00 30.11  ? 80  GLY   B O   1 
ATOM   1365 N N   . LEU   B 1 82 ? 10.908  -9.311  -32.131 1.00 26.34  ? 81  LEU   B N   1 
ATOM   1366 C CA  . LEU   B 1 82 ? 10.299  -9.383  -33.446 1.00 30.57  ? 81  LEU   B CA  1 
ATOM   1367 C C   . LEU   B 1 82 ? 10.126  -7.978  -33.997 1.00 32.36  ? 81  LEU   B C   1 
ATOM   1368 O O   . LEU   B 1 82 ? 10.318  -7.775  -35.197 1.00 31.87  ? 81  LEU   B O   1 
ATOM   1369 C CB  . LEU   B 1 82 ? 8.964   -10.140 -33.426 1.00 31.85  ? 81  LEU   B CB  1 
ATOM   1370 C CG  . LEU   B 1 82 ? 9.041   -11.662 -33.263 1.00 28.74  ? 81  LEU   B CG  1 
ATOM   1371 C CD1 . LEU   B 1 82 ? 7.647   -12.273 -33.358 1.00 26.95  ? 81  LEU   B CD1 1 
ATOM   1372 C CD2 . LEU   B 1 82 ? 9.965   -12.329 -34.274 1.00 29.11  ? 81  LEU   B CD2 1 
ATOM   1373 N N   . TRP   B 1 83 ? 9.750   -7.025  -33.124 1.00 28.84  ? 82  TRP   B N   1 
ATOM   1374 C CA  . TRP   B 1 83 ? 9.602   -5.637  -33.540 1.00 32.06  ? 82  TRP   B CA  1 
ATOM   1375 C C   . TRP   B 1 83 ? 10.940  -5.035  -33.981 1.00 34.35  ? 82  TRP   B C   1 
ATOM   1376 O O   . TRP   B 1 83 ? 10.997  -4.334  -34.999 1.00 32.74  ? 82  TRP   B O   1 
ATOM   1377 C CB  . TRP   B 1 83 ? 8.920   -4.766  -32.470 1.00 34.23  ? 82  TRP   B CB  1 
ATOM   1378 C CG  . TRP   B 1 83 ? 8.666   -3.363  -32.961 1.00 37.52  ? 82  TRP   B CG  1 
ATOM   1379 C CD1 . TRP   B 1 83 ? 7.539   -2.896  -33.570 1.00 41.15  ? 82  TRP   B CD1 1 
ATOM   1380 C CD2 . TRP   B 1 83 ? 9.601   -2.263  -32.952 1.00 38.41  ? 82  TRP   B CD2 1 
ATOM   1381 N NE1 . TRP   B 1 83 ? 7.704   -1.582  -33.928 1.00 41.39  ? 82  TRP   B NE1 1 
ATOM   1382 C CE2 . TRP   B 1 83 ? 8.959   -1.171  -33.572 1.00 39.04  ? 82  TRP   B CE2 1 
ATOM   1383 C CE3 . TRP   B 1 83 ? 10.915  -2.097  -32.493 1.00 36.08  ? 82  TRP   B CE3 1 
ATOM   1384 C CZ2 . TRP   B 1 83 ? 9.579   0.072   -33.715 1.00 37.56  ? 82  TRP   B CZ2 1 
ATOM   1385 C CZ3 . TRP   B 1 83 ? 11.535  -0.871  -32.644 1.00 39.87  ? 82  TRP   B CZ3 1 
ATOM   1386 C CH2 . TRP   B 1 83 ? 10.879  0.192   -33.265 1.00 39.02  ? 82  TRP   B CH2 1 
ATOM   1387 N N   . GLU   B 1 84 ? 12.003  -5.359  -33.238 1.00 28.40  ? 83  GLU   B N   1 
ATOM   1388 C CA  . GLU   B 1 84 ? 13.319  -4.787  -33.447 1.00 31.38  ? 83  GLU   B CA  1 
ATOM   1389 C C   . GLU   B 1 84 ? 13.906  -5.304  -34.761 1.00 29.03  ? 83  GLU   B C   1 
ATOM   1390 O O   . GLU   B 1 84 ? 14.419  -4.503  -35.542 1.00 28.64  ? 83  GLU   B O   1 
ATOM   1391 C CB  . GLU   B 1 84 ? 14.268  -4.975  -32.272 1.00 27.26  ? 83  GLU   B CB  1 
ATOM   1392 C CG  . GLU   B 1 84 ? 13.727  -4.401  -30.965 1.00 31.35  ? 83  GLU   B CG  1 
ATOM   1393 C CD  . GLU   B 1 84 ? 14.625  -4.638  -29.781 1.00 33.55  ? 83  GLU   B CD  1 
ATOM   1394 O OE1 . GLU   B 1 84 ? 15.536  -5.484  -29.904 1.00 32.11  ? 83  GLU   B OE1 1 
ATOM   1395 O OE2 . GLU   B 1 84 ? 14.443  -3.951  -28.725 1.00 33.64  ? 83  GLU   B OE2 1 
ATOM   1396 N N   . ILE   B 1 85 ? 13.821  -6.617  -35.009 1.00 28.69  ? 84  ILE   B N   1 
ATOM   1397 C CA  . ILE   B 1 85 ? 14.516  -7.159  -36.178 1.00 27.05  ? 84  ILE   B CA  1 
ATOM   1398 C C   . ILE   B 1 85 ? 13.847  -6.603  -37.435 1.00 29.04  ? 84  ILE   B C   1 
ATOM   1399 O O   . ILE   B 1 85 ? 14.503  -6.370  -38.457 1.00 27.65  ? 84  ILE   B O   1 
ATOM   1400 C CB  . ILE   B 1 85 ? 14.565  -8.703  -36.178 1.00 28.96  ? 84  ILE   B CB  1 
ATOM   1401 C CG1 . ILE   B 1 85 ? 15.585  -9.260  -37.232 1.00 27.92  ? 84  ILE   B CG1 1 
ATOM   1402 C CG2 . ILE   B 1 85 ? 13.178  -9.303  -36.373 1.00 28.11  ? 84  ILE   B CG2 1 
ATOM   1403 C CD1 . ILE   B 1 85 ? 16.206  -10.594 -36.845 1.00 31.48  ? 84  ILE   B CD1 1 
ATOM   1404 N N   . GLN   B 1 86 ? 12.533  -6.356  -37.326 1.00 28.82  ? 85  GLN   B N   1 
ATOM   1405 C CA  . GLN   B 1 86 ? 11.752  -5.788  -38.414 1.00 32.62  ? 85  GLN   B CA  1 
ATOM   1406 C C   . GLN   B 1 86 ? 12.031  -4.290  -38.600 1.00 32.77  ? 85  GLN   B C   1 
ATOM   1407 O O   . GLN   B 1 86 ? 12.161  -3.822  -39.739 1.00 34.07  ? 85  GLN   B O   1 
ATOM   1408 C CB  . GLN   B 1 86 ? 10.278  -6.095  -38.127 1.00 34.46  ? 85  GLN   B CB  1 
ATOM   1409 N N   . ASN   B 1 87 ? 12.073  -3.515  -37.508 1.00 29.90  ? 86  ASN   B N   1 
ATOM   1410 C CA  . ASN   B 1 87 ? 11.928  -2.064  -37.640 1.00 31.48  ? 86  ASN   B CA  1 
ATOM   1411 C C   . ASN   B 1 87 ? 13.232  -1.291  -37.441 1.00 32.23  ? 86  ASN   B C   1 
ATOM   1412 O O   . ASN   B 1 87 ? 13.356  -0.151  -37.927 1.00 33.49  ? 86  ASN   B O   1 
ATOM   1413 C CB  . ASN   B 1 87 ? 10.850  -1.539  -36.689 1.00 35.40  ? 86  ASN   B CB  1 
ATOM   1414 C CG  . ASN   B 1 87 ? 9.500   -2.049  -37.126 1.00 39.15  ? 86  ASN   B CG  1 
ATOM   1415 O OD1 . ASN   B 1 87 ? 8.992   -1.600  -38.153 1.00 42.69  ? 86  ASN   B OD1 1 
ATOM   1416 N ND2 . ASN   B 1 87 ? 8.953   -3.043  -36.440 1.00 38.85  ? 86  ASN   B ND2 1 
ATOM   1417 N N   . ASN   B 1 88 ? 14.192  -1.886  -36.722 1.00 30.68  ? 87  ASN   B N   1 
ATOM   1418 C CA  . ASN   B 1 88 ? 15.481  -1.241  -36.482 1.00 32.56  ? 87  ASN   B CA  1 
ATOM   1419 C C   . ASN   B 1 88 ? 16.556  -2.251  -36.093 1.00 30.97  ? 87  ASN   B C   1 
ATOM   1420 O O   . ASN   B 1 88 ? 17.190  -2.149  -35.028 1.00 29.63  ? 87  ASN   B O   1 
ATOM   1421 C CB  . ASN   B 1 88 ? 15.380  -0.084  -35.487 1.00 35.38  ? 87  ASN   B CB  1 
ATOM   1422 C CG  . ASN   B 1 88 ? 16.438  0.972   -35.724 1.00 36.61  ? 87  ASN   B CG  1 
ATOM   1423 O OD1 . ASN   B 1 88 ? 17.459  0.737   -36.386 1.00 35.36  ? 87  ASN   B OD1 1 
ATOM   1424 N ND2 . ASN   B 1 88 ? 16.234  2.151   -35.152 1.00 38.67  ? 87  ASN   B ND2 1 
ATOM   1425 N N   . PRO   B 1 89 ? 16.865  -3.206  -37.005 1.00 29.33  ? 88  PRO   B N   1 
ATOM   1426 C CA  . PRO   B 1 89 ? 17.839  -4.261  -36.724 1.00 28.83  ? 88  PRO   B CA  1 
ATOM   1427 C C   . PRO   B 1 89 ? 19.278  -3.851  -36.437 1.00 25.30  ? 88  PRO   B C   1 
ATOM   1428 O O   . PRO   B 1 89 ? 20.007  -4.587  -35.792 1.00 29.56  ? 88  PRO   B O   1 
ATOM   1429 C CB  . PRO   B 1 89 ? 17.743  -5.140  -38.009 1.00 25.68  ? 88  PRO   B CB  1 
ATOM   1430 C CG  . PRO   B 1 89 ? 17.219  -4.231  -39.109 1.00 27.29  ? 88  PRO   B CG  1 
ATOM   1431 C CD  . PRO   B 1 89 ? 16.282  -3.286  -38.362 1.00 28.10  ? 88  PRO   B CD  1 
ATOM   1432 N N   . HIS   B 1 90 ? 19.675  -2.651  -36.907 1.00 29.10  ? 89  HIS   B N   1 
ATOM   1433 C CA  . HIS   B 1 90 ? 21.064  -2.215  -36.886 1.00 26.33  ? 89  HIS   B CA  1 
ATOM   1434 C C   . HIS   B 1 90 ? 21.322  -1.115  -35.839 1.00 30.34  ? 89  HIS   B C   1 
ATOM   1435 O O   . HIS   B 1 90 ? 22.435  -0.572  -35.777 1.00 27.02  ? 89  HIS   B O   1 
ATOM   1436 C CB  . HIS   B 1 90 ? 21.439  -1.742  -38.306 1.00 27.46  ? 89  HIS   B CB  1 
ATOM   1437 C CG  . HIS   B 1 90 ? 21.298  -2.847  -39.309 1.00 28.21  ? 89  HIS   B CG  1 
ATOM   1438 N ND1 . HIS   B 1 90 ? 21.947  -4.044  -39.141 1.00 26.89  ? 89  HIS   B ND1 1 
ATOM   1439 C CD2 . HIS   B 1 90 ? 20.660  -2.922  -40.498 1.00 28.39  ? 89  HIS   B CD2 1 
ATOM   1440 C CE1 . HIS   B 1 90 ? 21.689  -4.819  -40.195 1.00 28.79  ? 89  HIS   B CE1 1 
ATOM   1441 N NE2 . HIS   B 1 90 ? 20.903  -4.160  -41.006 1.00 28.73  ? 89  HIS   B NE2 1 
ATOM   1442 N N   . ALA   B 1 91 ? 20.317  -0.830  -34.998 1.00 31.36  ? 90  ALA   B N   1 
ATOM   1443 C CA  . ALA   B 1 91 ? 20.420  0.188   -33.955 1.00 32.99  ? 90  ALA   B CA  1 
ATOM   1444 C C   . ALA   B 1 91 ? 21.385  -0.205  -32.828 1.00 35.82  ? 90  ALA   B C   1 
ATOM   1445 O O   . ALA   B 1 91 ? 21.685  -1.379  -32.579 1.00 31.02  ? 90  ALA   B O   1 
ATOM   1446 C CB  . ALA   B 1 91 ? 19.026  0.522   -33.438 1.00 29.10  ? 90  ALA   B CB  1 
ATOM   1447 N N   . SER   B 1 92 ? 21.877  0.815   -32.113 1.00 34.78  ? 91  SER   B N   1 
ATOM   1448 C CA  . SER   B 1 92 ? 22.521  0.598   -30.834 1.00 38.30  ? 91  SER   B CA  1 
ATOM   1449 C C   . SER   B 1 92 ? 21.461  0.375   -29.761 1.00 42.00  ? 91  SER   B C   1 
ATOM   1450 O O   . SER   B 1 92 ? 20.562  1.205   -29.605 1.00 45.38  ? 91  SER   B O   1 
ATOM   1451 C CB  . SER   B 1 92 ? 23.375  1.773   -30.455 1.00 38.79  ? 91  SER   B CB  1 
ATOM   1452 O OG  . SER   B 1 92 ? 23.872  1.519   -29.152 1.00 47.05  ? 91  SER   B OG  1 
ATOM   1453 N N   . TYR   B 1 93 ? 21.594  -0.748  -29.036 1.00 42.24  ? 92  TYR   B N   1 
ATOM   1454 C CA  . TYR   B 1 93 ? 20.694  -1.140  -27.966 1.00 41.78  ? 92  TYR   B CA  1 
ATOM   1455 C C   . TYR   B 1 93 ? 21.441  -1.081  -26.636 1.00 51.49  ? 92  TYR   B C   1 
ATOM   1456 O O   . TYR   B 1 93 ? 20.977  -1.622  -25.633 1.00 54.96  ? 92  TYR   B O   1 
ATOM   1457 C CB  . TYR   B 1 93 ? 20.069  -2.507  -28.271 1.00 36.00  ? 92  TYR   B CB  1 
ATOM   1458 C CG  . TYR   B 1 93 ? 19.064  -2.418  -29.405 1.00 34.05  ? 92  TYR   B CG  1 
ATOM   1459 C CD1 . TYR   B 1 93 ? 17.782  -1.941  -29.171 1.00 31.39  ? 92  TYR   B CD1 1 
ATOM   1460 C CD2 . TYR   B 1 93 ? 19.376  -2.858  -30.695 1.00 30.20  ? 92  TYR   B CD2 1 
ATOM   1461 C CE1 . TYR   B 1 93 ? 16.845  -1.814  -30.178 1.00 31.80  ? 92  TYR   B CE1 1 
ATOM   1462 C CE2 . TYR   B 1 93 ? 18.447  -2.720  -31.716 1.00 31.55  ? 92  TYR   B CE2 1 
ATOM   1463 C CZ  . TYR   B 1 93 ? 17.180  -2.230  -31.453 1.00 31.62  ? 92  TYR   B CZ  1 
ATOM   1464 O OH  . TYR   B 1 93 ? 16.224  -2.133  -32.402 1.00 31.53  ? 92  TYR   B OH  1 
ATOM   1465 N N   . SER   B 1 94 ? 22.606  -0.419  -26.658 1.00 59.26  ? 93  SER   B N   1 
ATOM   1466 C CA  . SER   B 1 94 ? 23.321  -0.036  -25.453 1.00 63.25  ? 93  SER   B CA  1 
ATOM   1467 C C   . SER   B 1 94 ? 22.317  0.601   -24.480 1.00 75.41  ? 93  SER   B C   1 
ATOM   1468 O O   . SER   B 1 94 ? 21.728  1.647   -24.860 1.00 75.44  ? 93  SER   B O   1 
ATOM   1469 C CB  . SER   B 1 94 ? 24.458  0.914   -25.773 1.00 63.80  ? 93  SER   B CB  1 
ATOM   1470 O OG  . SER   B 1 94 ? 25.477  0.276   -26.533 1.00 72.35  ? 93  SER   B OG  1 
ATOM   1471 O OXT . SER   B 1 94 ? 22.115  0.003   -23.397 1.00 84.15  ? 93  SER   B OXT 1 
ATOM   1472 N N   . HIS   C 1 4  ? 32.227  -23.223 26.861  1.00 70.30  ? 3   HIS   C N   1 
ATOM   1473 C CA  . HIS   C 1 4  ? 32.398  -24.210 27.963  1.00 80.22  ? 3   HIS   C CA  1 
ATOM   1474 C C   . HIS   C 1 4  ? 31.496  -23.840 29.145  1.00 87.38  ? 3   HIS   C C   1 
ATOM   1475 O O   . HIS   C 1 4  ? 31.684  -24.334 30.255  1.00 91.27  ? 3   HIS   C O   1 
ATOM   1476 C CB  . HIS   C 1 4  ? 33.882  -24.329 28.337  1.00 70.66  ? 3   HIS   C CB  1 
ATOM   1477 N N   . ALA   C 1 5  ? 30.491  -22.994 28.895  1.00 83.30  ? 4   ALA   C N   1 
ATOM   1478 C CA  . ALA   C 1 5  ? 29.671  -22.445 29.962  1.00 80.71  ? 4   ALA   C CA  1 
ATOM   1479 C C   . ALA   C 1 5  ? 28.183  -22.599 29.647  1.00 82.37  ? 4   ALA   C C   1 
ATOM   1480 O O   . ALA   C 1 5  ? 27.528  -21.619 29.288  1.00 87.41  ? 4   ALA   C O   1 
ATOM   1481 C CB  . ALA   C 1 5  ? 30.031  -20.987 30.137  1.00 80.19  ? 4   ALA   C CB  1 
ATOM   1482 N N   . PHE   C 1 6  ? 27.645  -23.819 29.794  1.00 68.36  ? 5   PHE   C N   1 
ATOM   1483 C CA  . PHE   C 1 6  ? 26.234  -24.035 29.505  1.00 58.58  ? 5   PHE   C CA  1 
ATOM   1484 C C   . PHE   C 1 6  ? 25.465  -24.054 30.817  1.00 59.45  ? 5   PHE   C C   1 
ATOM   1485 O O   . PHE   C 1 6  ? 25.852  -24.764 31.744  1.00 62.96  ? 5   PHE   C O   1 
ATOM   1486 C CB  . PHE   C 1 6  ? 25.885  -25.259 28.642  1.00 50.83  ? 5   PHE   C CB  1 
ATOM   1487 C CG  . PHE   C 1 6  ? 26.614  -25.291 27.306  1.00 45.53  ? 5   PHE   C CG  1 
ATOM   1488 C CD1 . PHE   C 1 6  ? 27.764  -26.051 27.137  1.00 47.67  ? 5   PHE   C CD1 1 
ATOM   1489 C CD2 . PHE   C 1 6  ? 26.179  -24.522 26.235  1.00 46.35  ? 5   PHE   C CD2 1 
ATOM   1490 C CE1 . PHE   C 1 6  ? 28.442  -26.069 25.922  1.00 52.19  ? 5   PHE   C CE1 1 
ATOM   1491 C CE2 . PHE   C 1 6  ? 26.854  -24.541 25.026  1.00 42.71  ? 5   PHE   C CE2 1 
ATOM   1492 C CZ  . PHE   C 1 6  ? 27.987  -25.306 24.866  1.00 45.73  ? 5   PHE   C CZ  1 
ATOM   1493 N N   . LYS   C 1 7  ? 24.382  -23.267 30.857  1.00 57.00  ? 6   LYS   C N   1 
ATOM   1494 C CA  . LYS   C 1 7  ? 23.464  -23.174 31.982  1.00 58.35  ? 6   LYS   C CA  1 
ATOM   1495 C C   . LYS   C 1 7  ? 22.059  -23.521 31.490  1.00 50.55  ? 6   LYS   C C   1 
ATOM   1496 O O   . LYS   C 1 7  ? 21.816  -23.509 30.285  1.00 53.59  ? 6   LYS   C O   1 
ATOM   1497 C CB  . LYS   C 1 7  ? 23.504  -21.749 32.557  1.00 60.35  ? 6   LYS   C CB  1 
ATOM   1498 N N   . PRO   C 1 8  ? 21.075  -23.823 32.368  1.00 51.57  ? 7   PRO   C N   1 
ATOM   1499 C CA  . PRO   C 1 8  ? 19.741  -24.221 31.900  1.00 50.40  ? 7   PRO   C CA  1 
ATOM   1500 C C   . PRO   C 1 8  ? 19.143  -23.091 31.065  1.00 55.12  ? 7   PRO   C C   1 
ATOM   1501 O O   . PRO   C 1 8  ? 19.367  -21.919 31.375  1.00 58.70  ? 7   PRO   C O   1 
ATOM   1502 C CB  . PRO   C 1 8  ? 18.953  -24.481 33.184  1.00 53.63  ? 7   PRO   C CB  1 
ATOM   1503 C CG  . PRO   C 1 8  ? 20.025  -24.684 34.235  1.00 54.04  ? 7   PRO   C CG  1 
ATOM   1504 C CD  . PRO   C 1 8  ? 21.171  -23.770 33.837  1.00 53.37  ? 7   PRO   C CD  1 
ATOM   1505 N N   . GLY   C 1 9  ? 18.447  -23.451 29.976  1.00 51.33  ? 8   GLY   C N   1 
ATOM   1506 C CA  . GLY   C 1 9  ? 17.801  -22.482 29.099  1.00 47.87  ? 8   GLY   C CA  1 
ATOM   1507 C C   . GLY   C 1 9  ? 18.673  -22.019 27.931  1.00 49.23  ? 8   GLY   C C   1 
ATOM   1508 O O   . GLY   C 1 9  ? 18.135  -21.495 26.958  1.00 56.97  ? 8   GLY   C O   1 
ATOM   1509 N N   . ASP   C 1 10 ? 20.002  -22.205 28.010  1.00 43.28  ? 9   ASP   C N   1 
ATOM   1510 C CA  . ASP   C 1 10 ? 20.891  -21.830 26.925  1.00 42.85  ? 9   ASP   C CA  1 
ATOM   1511 C C   . ASP   C 1 10 ? 20.481  -22.548 25.642  1.00 43.04  ? 9   ASP   C C   1 
ATOM   1512 O O   . ASP   C 1 10 ? 20.106  -23.716 25.673  1.00 41.46  ? 9   ASP   C O   1 
ATOM   1513 C CB  . ASP   C 1 10 ? 22.363  -22.045 27.244  1.00 48.08  ? 9   ASP   C CB  1 
ATOM   1514 C CG  . ASP   C 1 10 ? 22.950  -21.133 28.315  1.00 53.19  ? 9   ASP   C CG  1 
ATOM   1515 O OD1 . ASP   C 1 10 ? 22.212  -20.255 28.803  1.00 59.24  ? 9   ASP   C OD1 1 
ATOM   1516 O OD2 . ASP   C 1 10 ? 24.144  -21.301 28.650  1.00 59.25  ? 9   ASP   C OD2 1 
ATOM   1517 N N   . LEU   C 1 11 ? 20.547  -21.817 24.524  1.00 41.19  ? 10  LEU   C N   1 
ATOM   1518 C CA  . LEU   C 1 11 ? 20.102  -22.349 23.243  1.00 40.74  ? 10  LEU   C CA  1 
ATOM   1519 C C   . LEU   C 1 11 ? 21.309  -22.841 22.468  1.00 35.92  ? 10  LEU   C C   1 
ATOM   1520 O O   . LEU   C 1 11 ? 22.346  -22.165 22.422  1.00 42.57  ? 10  LEU   C O   1 
ATOM   1521 C CB  . LEU   C 1 11 ? 19.336  -21.301 22.447  1.00 38.39  ? 10  LEU   C CB  1 
ATOM   1522 C CG  . LEU   C 1 11 ? 18.023  -20.836 23.060  1.00 37.53  ? 10  LEU   C CG  1 
ATOM   1523 C CD1 . LEU   C 1 11 ? 17.524  -19.856 22.016  1.00 40.55  ? 10  LEU   C CD1 1 
ATOM   1524 C CD2 . LEU   C 1 11 ? 17.026  -21.957 23.350  1.00 38.49  ? 10  LEU   C CD2 1 
ATOM   1525 N N   . VAL   C 1 12 ? 21.162  -24.026 21.842  1.00 38.22  ? 11  VAL   C N   1 
ATOM   1526 C CA  . VAL   C 1 12 ? 22.304  -24.739 21.301  1.00 34.23  ? 11  VAL   C CA  1 
ATOM   1527 C C   . VAL   C 1 12 ? 21.896  -25.485 20.022  1.00 30.66  ? 11  VAL   C C   1 
ATOM   1528 O O   . VAL   C 1 12 ? 20.699  -25.634 19.742  1.00 31.11  ? 11  VAL   C O   1 
ATOM   1529 C CB  . VAL   C 1 12 ? 22.891  -25.713 22.352  1.00 36.10  ? 11  VAL   C CB  1 
ATOM   1530 C CG1 . VAL   C 1 12 ? 23.258  -25.025 23.675  1.00 38.49  ? 11  VAL   C CG1 1 
ATOM   1531 C CG2 . VAL   C 1 12 ? 21.984  -26.893 22.641  1.00 36.16  ? 11  VAL   C CG2 1 
ATOM   1532 N N   . PHE   C 1 13 ? 22.915  -25.882 19.247  1.00 32.84  ? 12  PHE   C N   1 
ATOM   1533 C CA  . PHE   C 1 13 ? 22.857  -27.046 18.366  1.00 31.86  ? 12  PHE   C CA  1 
ATOM   1534 C C   . PHE   C 1 13 ? 23.576  -28.191 19.066  1.00 29.30  ? 12  PHE   C C   1 
ATOM   1535 O O   . PHE   C 1 13 ? 24.681  -28.017 19.591  1.00 36.94  ? 12  PHE   C O   1 
ATOM   1536 C CB  . PHE   C 1 13 ? 23.485  -26.901 16.966  1.00 33.96  ? 12  PHE   C CB  1 
ATOM   1537 C CG  . PHE   C 1 13 ? 22.699  -25.903 16.128  1.00 38.05  ? 12  PHE   C CG  1 
ATOM   1538 C CD1 . PHE   C 1 13 ? 21.651  -26.325 15.292  1.00 33.47  ? 12  PHE   C CD1 1 
ATOM   1539 C CD2 . PHE   C 1 13 ? 22.991  -24.544 16.201  1.00 35.88  ? 12  PHE   C CD2 1 
ATOM   1540 C CE1 . PHE   C 1 13 ? 20.923  -25.401 14.558  1.00 38.94  ? 12  PHE   C CE1 1 
ATOM   1541 C CE2 . PHE   C 1 13 ? 22.254  -23.625 15.459  1.00 41.16  ? 12  PHE   C CE2 1 
ATOM   1542 C CZ  . PHE   C 1 13 ? 21.234  -24.057 14.639  1.00 36.95  ? 12  PHE   C CZ  1 
ATOM   1543 N N   . ALA   C 1 14 ? 22.925  -29.369 19.061  1.00 30.31  ? 13  ALA   C N   1 
ATOM   1544 C CA  . ALA   C 1 14 ? 23.400  -30.534 19.786  1.00 25.96  ? 13  ALA   C CA  1 
ATOM   1545 C C   . ALA   C 1 14 ? 23.668  -31.673 18.803  1.00 31.48  ? 13  ALA   C C   1 
ATOM   1546 O O   . ALA   C 1 14 ? 22.796  -31.992 18.004  1.00 26.65  ? 13  ALA   C O   1 
ATOM   1547 C CB  . ALA   C 1 14 ? 22.339  -30.958 20.774  1.00 26.61  ? 13  ALA   C CB  1 
ATOM   1548 N N   . LYS   C 1 15 ? 24.845  -32.299 18.901  1.00 28.58  ? 14  LYS   C N   1 
ATOM   1549 C CA  . LYS   C 1 15 ? 25.239  -33.294 17.907  1.00 29.66  ? 14  LYS   C CA  1 
ATOM   1550 C C   . LYS   C 1 15 ? 25.233  -34.668 18.546  1.00 31.38  ? 14  LYS   C C   1 
ATOM   1551 O O   . LYS   C 1 15 ? 25.936  -34.911 19.519  1.00 30.44  ? 14  LYS   C O   1 
ATOM   1552 C CB  . LYS   C 1 15 ? 26.648  -33.042 17.347  1.00 30.92  ? 14  LYS   C CB  1 
ATOM   1553 C CG  . LYS   C 1 15 ? 27.086  -34.064 16.306  1.00 30.98  ? 14  LYS   C CG  1 
ATOM   1554 C CD  . LYS   C 1 15 ? 26.329  -33.824 15.001  1.00 29.63  ? 14  LYS   C CD  1 
ATOM   1555 C CE  . LYS   C 1 15 ? 26.748  -34.731 13.850  1.00 33.81  ? 14  LYS   C CE  1 
ATOM   1556 N NZ  . LYS   C 1 15 ? 26.528  -36.131 14.179  1.00 30.97  ? 14  LYS   C NZ  1 
ATOM   1557 N N   . MET   C 1 16 ? 24.440  -35.571 17.964  1.00 31.20  ? 15  MET   C N   1 
ATOM   1558 C CA  . MET   C 1 16 ? 24.443  -36.988 18.285  1.00 29.82  ? 15  MET   C CA  1 
ATOM   1559 C C   . MET   C 1 16 ? 24.906  -37.779 17.070  1.00 35.18  ? 15  MET   C C   1 
ATOM   1560 O O   . MET   C 1 16 ? 24.591  -37.413 15.940  1.00 28.32  ? 15  MET   C O   1 
ATOM   1561 C CB  . MET   C 1 16 ? 23.020  -37.444 18.624  1.00 30.81  ? 15  MET   C CB  1 
ATOM   1562 C CG  . MET   C 1 16 ? 22.523  -36.794 19.902  1.00 41.10  ? 15  MET   C CG  1 
ATOM   1563 S SD  . MET   C 1 16 ? 21.024  -37.562 20.532  1.00 47.40  ? 15  MET   C SD  1 
ATOM   1564 C CE  . MET   C 1 16 ? 19.929  -37.149 19.164  1.00 48.75  ? 15  MET   C CE  1 
ATOM   1565 N N   . LYS   C 1 17 ? 25.596  -38.902 17.308  1.00 31.69  ? 16  LYS   C N   1 
ATOM   1566 C CA  . LYS   C 1 17 ? 25.949  -39.788 16.209  1.00 31.60  ? 16  LYS   C CA  1 
ATOM   1567 C C   . LYS   C 1 17 ? 24.688  -40.224 15.449  1.00 30.35  ? 16  LYS   C C   1 
ATOM   1568 O O   . LYS   C 1 17 ? 23.707  -40.658 16.064  1.00 33.06  ? 16  LYS   C O   1 
ATOM   1569 C CB  . LYS   C 1 17 ? 26.650  -41.005 16.832  1.00 33.51  ? 16  LYS   C CB  1 
ATOM   1570 C CG  . LYS   C 1 17 ? 27.331  -41.964 15.851  1.00 37.68  ? 16  LYS   C CG  1 
ATOM   1571 C CD  . LYS   C 1 17 ? 28.482  -41.289 15.126  1.00 40.08  ? 16  LYS   C CD  1 
ATOM   1572 C CE  . LYS   C 1 17 ? 29.153  -42.184 14.140  1.00 49.55  ? 16  LYS   C CE  1 
ATOM   1573 N NZ  . LYS   C 1 17 ? 30.418  -41.612 13.671  1.00 47.91  ? 16  LYS   C NZ  1 
ATOM   1574 N N   . GLY   C 1 18 ? 24.757  -40.149 14.102  1.00 32.18  ? 17  GLY   C N   1 
ATOM   1575 C CA  . GLY   C 1 18 ? 23.664  -40.574 13.235  1.00 30.03  ? 17  GLY   C CA  1 
ATOM   1576 C C   . GLY   C 1 18 ? 22.712  -39.420 12.865  1.00 33.64  ? 17  GLY   C C   1 
ATOM   1577 O O   . GLY   C 1 18 ? 21.696  -39.651 12.219  1.00 33.85  ? 17  GLY   C O   1 
ATOM   1578 N N   . TYR   C 1 19 ? 22.983  -38.198 13.339  1.00 30.67  ? 18  TYR   C N   1 
ATOM   1579 C CA  . TYR   C 1 19 ? 22.050  -37.071 13.201  1.00 31.02  ? 18  TYR   C CA  1 
ATOM   1580 C C   . TYR   C 1 19 ? 22.826  -35.799 12.914  1.00 29.77  ? 18  TYR   C C   1 
ATOM   1581 O O   . TYR   C 1 19 ? 23.951  -35.623 13.403  1.00 29.08  ? 18  TYR   C O   1 
ATOM   1582 C CB  . TYR   C 1 19 ? 21.251  -36.792 14.484  1.00 28.33  ? 18  TYR   C CB  1 
ATOM   1583 C CG  . TYR   C 1 19 ? 20.382  -37.985 14.823  1.00 32.77  ? 18  TYR   C CG  1 
ATOM   1584 C CD1 . TYR   C 1 19 ? 20.865  -39.051 15.589  1.00 36.81  ? 18  TYR   C CD1 1 
ATOM   1585 C CD2 . TYR   C 1 19 ? 19.098  -38.066 14.310  1.00 35.02  ? 18  TYR   C CD2 1 
ATOM   1586 C CE1 . TYR   C 1 19 ? 20.055  -40.142 15.865  1.00 36.25  ? 18  TYR   C CE1 1 
ATOM   1587 C CE2 . TYR   C 1 19 ? 18.282  -39.145 14.595  1.00 46.73  ? 18  TYR   C CE2 1 
ATOM   1588 C CZ  . TYR   C 1 19 ? 18.763  -40.182 15.369  1.00 44.60  ? 18  TYR   C CZ  1 
ATOM   1589 O OH  . TYR   C 1 19 ? 17.900  -41.216 15.602  1.00 58.05  ? 18  TYR   C OH  1 
ATOM   1590 N N   . PRO   C 1 20 ? 22.239  -34.867 12.124  1.00 27.57  ? 19  PRO   C N   1 
ATOM   1591 C CA  . PRO   C 1 20 ? 22.859  -33.559 11.907  1.00 26.99  ? 19  PRO   C CA  1 
ATOM   1592 C C   . PRO   C 1 20 ? 22.824  -32.760 13.216  1.00 27.81  ? 19  PRO   C C   1 
ATOM   1593 O O   . PRO   C 1 20 ? 22.062  -33.082 14.143  1.00 26.05  ? 19  PRO   C O   1 
ATOM   1594 C CB  . PRO   C 1 20 ? 21.901  -32.973 10.828  1.00 30.36  ? 19  PRO   C CB  1 
ATOM   1595 C CG  . PRO   C 1 20 ? 20.551  -33.528 11.193  1.00 30.71  ? 19  PRO   C CG  1 
ATOM   1596 C CD  . PRO   C 1 20 ? 20.891  -34.990 11.515  1.00 28.43  ? 19  PRO   C CD  1 
ATOM   1597 N N   . HIS   C 1 21 ? 23.668  -31.727 13.300  1.00 30.31  ? 20  HIS   C N   1 
ATOM   1598 C CA  . HIS   C 1 21 ? 23.598  -30.776 14.411  1.00 28.56  ? 20  HIS   C CA  1 
ATOM   1599 C C   . HIS   C 1 21 ? 22.162  -30.261 14.572  1.00 31.01  ? 20  HIS   C C   1 
ATOM   1600 O O   . HIS   C 1 21 ? 21.583  -29.695 13.638  1.00 30.91  ? 20  HIS   C O   1 
ATOM   1601 C CB  . HIS   C 1 21 ? 24.612  -29.642 14.207  1.00 32.72  ? 20  HIS   C CB  1 
ATOM   1602 C CG  . HIS   C 1 21 ? 26.041  -30.112 14.221  1.00 36.72  ? 20  HIS   C CG  1 
ATOM   1603 N ND1 . HIS   C 1 21 ? 26.702  -30.744 13.180  1.00 36.32  ? 20  HIS   C ND1 1 
ATOM   1604 C CD2 . HIS   C 1 21 ? 26.950  -29.995 15.214  1.00 38.48  ? 20  HIS   C CD2 1 
ATOM   1605 C CE1 . HIS   C 1 21 ? 27.945  -31.024 13.548  1.00 36.15  ? 20  HIS   C CE1 1 
ATOM   1606 N NE2 . HIS   C 1 21 ? 28.121  -30.582 14.783  1.00 34.60  ? 20  HIS   C NE2 1 
ATOM   1607 N N   . TRP   C 1 22 ? 21.598  -30.446 15.780  1.00 25.97  ? 21  TRP   C N   1 
ATOM   1608 C CA  . TRP   C 1 22 ? 20.151  -30.352 15.932  1.00 24.00  ? 21  TRP   C CA  1 
ATOM   1609 C C   . TRP   C 1 22 ? 19.801  -29.161 16.821  1.00 26.48  ? 21  TRP   C C   1 
ATOM   1610 O O   . TRP   C 1 22 ? 20.417  -29.000 17.877  1.00 28.53  ? 21  TRP   C O   1 
ATOM   1611 C CB  . TRP   C 1 22 ? 19.570  -31.643 16.521  1.00 26.56  ? 21  TRP   C CB  1 
ATOM   1612 C CG  . TRP   C 1 22 ? 18.110  -31.821 16.183  1.00 27.09  ? 21  TRP   C CG  1 
ATOM   1613 C CD1 . TRP   C 1 22 ? 17.015  -31.226 16.759  1.00 28.81  ? 21  TRP   C CD1 1 
ATOM   1614 C CD2 . TRP   C 1 22 ? 17.609  -32.700 15.151  1.00 26.43  ? 21  TRP   C CD2 1 
ATOM   1615 N NE1 . TRP   C 1 22 ? 15.863  -31.691 16.158  1.00 27.35  ? 21  TRP   C NE1 1 
ATOM   1616 C CE2 . TRP   C 1 22 ? 16.199  -32.596 15.177  1.00 27.84  ? 21  TRP   C CE2 1 
ATOM   1617 C CE3 . TRP   C 1 22 ? 18.219  -33.574 14.226  1.00 27.60  ? 21  TRP   C CE3 1 
ATOM   1618 C CZ2 . TRP   C 1 22 ? 15.403  -33.329 14.293  1.00 27.31  ? 21  TRP   C CZ2 1 
ATOM   1619 C CZ3 . TRP   C 1 22 ? 17.429  -34.291 13.356  1.00 30.46  ? 21  TRP   C CZ3 1 
ATOM   1620 C CH2 . TRP   C 1 22 ? 16.035  -34.187 13.418  1.00 26.89  ? 21  TRP   C CH2 1 
ATOM   1621 N N   . PRO   C 1 23 ? 18.794  -28.312 16.475  1.00 30.98  ? 22  PRO   C N   1 
ATOM   1622 C CA  . PRO   C 1 23 ? 18.395  -27.213 17.374  1.00 27.12  ? 22  PRO   C CA  1 
ATOM   1623 C C   . PRO   C 1 23 ? 17.824  -27.706 18.702  1.00 24.65  ? 22  PRO   C C   1 
ATOM   1624 O O   . PRO   C 1 23 ? 16.938  -28.552 18.726  1.00 29.16  ? 22  PRO   C O   1 
ATOM   1625 C CB  . PRO   C 1 23 ? 17.358  -26.431 16.550  1.00 31.47  ? 22  PRO   C CB  1 
ATOM   1626 C CG  . PRO   C 1 23 ? 16.782  -27.483 15.603  1.00 27.57  ? 22  PRO   C CG  1 
ATOM   1627 C CD  . PRO   C 1 23 ? 18.014  -28.312 15.217  1.00 28.46  ? 22  PRO   C CD  1 
ATOM   1628 N N   . ALA   C 1 24 ? 18.363  -27.171 19.814  1.00 27.82  ? 23  ALA   C N   1 
ATOM   1629 C CA  . ALA   C 1 24 ? 18.048  -27.726 21.124  1.00 33.47  ? 23  ALA   C CA  1 
ATOM   1630 C C   . ALA   C 1 24 ? 18.260  -26.672 22.211  1.00 32.47  ? 23  ALA   C C   1 
ATOM   1631 O O   . ALA   C 1 24 ? 18.737  -25.565 21.939  1.00 32.67  ? 23  ALA   C O   1 
ATOM   1632 C CB  . ALA   C 1 24 ? 18.902  -28.989 21.374  1.00 31.51  ? 23  ALA   C CB  1 
ATOM   1633 N N   . ARG   C 1 25 ? 17.948  -27.056 23.460  1.00 36.21  ? 24  ARG   C N   1 
ATOM   1634 C CA  . ARG   C 1 25 ? 18.275  -26.228 24.609  1.00 33.34  ? 24  ARG   C CA  1 
ATOM   1635 C C   . ARG   C 1 25 ? 18.702  -27.102 25.793  1.00 35.45  ? 24  ARG   C C   1 
ATOM   1636 O O   . ARG   C 1 25 ? 18.388  -28.289 25.828  1.00 37.01  ? 24  ARG   C O   1 
ATOM   1637 C CB  . ARG   C 1 25 ? 17.073  -25.413 25.081  1.00 35.50  ? 24  ARG   C CB  1 
ATOM   1638 C CG  . ARG   C 1 25 ? 15.848  -26.173 25.556  1.00 42.00  ? 24  ARG   C CG  1 
ATOM   1639 C CD  . ARG   C 1 25 ? 14.766  -25.241 26.088  1.00 44.57  ? 24  ARG   C CD  1 
ATOM   1640 N NE  . ARG   C 1 25 ? 13.611  -26.019 26.547  1.00 47.35  ? 24  ARG   C NE  1 
ATOM   1641 C CZ  . ARG   C 1 25 ? 12.329  -25.818 26.259  1.00 49.67  ? 24  ARG   C CZ  1 
ATOM   1642 N NH1 . ARG   C 1 25 ? 11.940  -24.749 25.582  1.00 48.47  ? 24  ARG   C NH1 1 
ATOM   1643 N NH2 . ARG   C 1 25 ? 11.423  -26.691 26.671  1.00 52.00  ? 24  ARG   C NH2 1 
ATOM   1644 N N   . ILE   C 1 26 ? 19.379  -26.465 26.754  1.00 37.05  ? 25  ILE   C N   1 
ATOM   1645 C CA  . ILE   C 1 26 ? 19.752  -27.091 28.021  1.00 38.67  ? 25  ILE   C CA  1 
ATOM   1646 C C   . ILE   C 1 26 ? 18.530  -27.116 28.929  1.00 43.08  ? 25  ILE   C C   1 
ATOM   1647 O O   . ILE   C 1 26 ? 17.891  -26.086 29.131  1.00 46.34  ? 25  ILE   C O   1 
ATOM   1648 C CB  . ILE   C 1 26 ? 20.905  -26.343 28.707  1.00 41.43  ? 25  ILE   C CB  1 
ATOM   1649 C CG1 . ILE   C 1 26 ? 21.996  -25.887 27.755  1.00 44.00  ? 25  ILE   C CG1 1 
ATOM   1650 C CG2 . ILE   C 1 26 ? 21.465  -27.173 29.862  1.00 45.69  ? 25  ILE   C CG2 1 
ATOM   1651 C CD1 . ILE   C 1 26 ? 22.836  -26.985 27.129  1.00 43.96  ? 25  ILE   C CD1 1 
ATOM   1652 N N   . ASP   C 1 27 ? 18.191  -28.308 29.434  1.00 47.52  ? 26  ASP   C N   1 
ATOM   1653 C CA  . ASP   C 1 27 ? 17.156  -28.464 30.446  1.00 51.55  ? 26  ASP   C CA  1 
ATOM   1654 C C   . ASP   C 1 27 ? 17.803  -28.301 31.819  1.00 57.03  ? 26  ASP   C C   1 
ATOM   1655 O O   . ASP   C 1 27 ? 19.025  -28.440 31.946  1.00 57.93  ? 26  ASP   C O   1 
ATOM   1656 C CB  . ASP   C 1 27 ? 16.455  -29.816 30.340  1.00 52.62  ? 26  ASP   C CB  1 
ATOM   1657 C CG  . ASP   C 1 27 ? 15.118  -29.871 29.604  1.00 58.38  ? 26  ASP   C CG  1 
ATOM   1658 O OD1 . ASP   C 1 27 ? 14.742  -28.854 28.974  1.00 51.18  ? 26  ASP   C OD1 1 
ATOM   1659 O OD2 . ASP   C 1 27 ? 14.430  -30.929 29.692  1.00 54.08  ? 26  ASP   C OD2 1 
ATOM   1660 N N   . ASP   C 1 28 ? 16.989  -27.991 32.837  1.00 58.17  ? 27  ASP   C N   1 
ATOM   1661 C CA  . ASP   C 1 28 ? 17.402  -28.205 34.220  1.00 66.37  ? 27  ASP   C CA  1 
ATOM   1662 C C   . ASP   C 1 28 ? 16.769  -29.516 34.689  1.00 65.38  ? 27  ASP   C C   1 
ATOM   1663 O O   . ASP   C 1 28 ? 15.657  -29.834 34.276  1.00 67.39  ? 27  ASP   C O   1 
ATOM   1664 C CB  . ASP   C 1 28 ? 17.135  -26.988 35.098  1.00 66.10  ? 27  ASP   C CB  1 
ATOM   1665 C CG  . ASP   C 1 28 ? 17.943  -26.866 36.389  1.00 68.91  ? 27  ASP   C CG  1 
ATOM   1666 O OD1 . ASP   C 1 28 ? 18.846  -27.696 36.630  1.00 64.64  ? 27  ASP   C OD1 1 
ATOM   1667 O OD2 . ASP   C 1 28 ? 17.671  -25.921 37.157  1.00 65.22  ? 27  ASP   C OD2 1 
ATOM   1668 N N   . ILE   C 1 29 ? 17.495  -30.270 35.532  1.00 63.75  ? 28  ILE   C N   1 
ATOM   1669 C CA  . ILE   C 1 29 ? 17.090  -31.609 35.937  1.00 64.81  ? 28  ILE   C CA  1 
ATOM   1670 C C   . ILE   C 1 29 ? 16.126  -31.499 37.127  1.00 58.84  ? 28  ILE   C C   1 
ATOM   1671 O O   . ILE   C 1 29 ? 16.614  -31.072 38.191  1.00 58.46  ? 28  ILE   C O   1 
ATOM   1672 C CB  . ILE   C 1 29 ? 18.315  -32.487 36.271  1.00 59.71  ? 28  ILE   C CB  1 
ATOM   1673 N N   . LYS   C 1 35 ? 19.894  -38.699 37.678  1.00 53.65  ? 34  LYS   C N   1 
ATOM   1674 C CA  . LYS   C 1 35 ? 21.026  -37.748 37.500  1.00 58.91  ? 34  LYS   C CA  1 
ATOM   1675 C C   . LYS   C 1 35 ? 21.698  -38.001 36.150  1.00 52.94  ? 34  LYS   C C   1 
ATOM   1676 O O   . LYS   C 1 35 ? 21.751  -39.140 35.685  1.00 45.41  ? 34  LYS   C O   1 
ATOM   1677 C CB  . LYS   C 1 35 ? 22.020  -37.905 38.659  1.00 66.45  ? 34  LYS   C CB  1 
ATOM   1678 C CG  . LYS   C 1 35 ? 21.601  -37.259 39.981  1.00 72.86  ? 34  LYS   C CG  1 
ATOM   1679 C CD  . LYS   C 1 35 ? 21.712  -35.738 39.980  1.00 75.77  ? 34  LYS   C CD  1 
ATOM   1680 N N   . PRO   C 1 36 ? 22.241  -36.955 35.477  1.00 48.70  ? 35  PRO   C N   1 
ATOM   1681 C CA  . PRO   C 1 36 ? 22.997  -37.163 34.238  1.00 46.28  ? 35  PRO   C CA  1 
ATOM   1682 C C   . PRO   C 1 36 ? 24.165  -38.111 34.517  1.00 48.96  ? 35  PRO   C C   1 
ATOM   1683 O O   . PRO   C 1 36 ? 24.619  -38.217 35.667  1.00 44.04  ? 35  PRO   C O   1 
ATOM   1684 C CB  . PRO   C 1 36 ? 23.484  -35.742 33.877  1.00 57.41  ? 35  PRO   C CB  1 
ATOM   1685 C CG  . PRO   C 1 36 ? 22.562  -34.798 34.634  1.00 54.74  ? 35  PRO   C CG  1 
ATOM   1686 C CD  . PRO   C 1 36 ? 22.163  -35.544 35.896  1.00 52.80  ? 35  PRO   C CD  1 
ATOM   1687 N N   . PRO   C 1 37 ? 24.687  -38.847 33.508  1.00 44.77  ? 36  PRO   C N   1 
ATOM   1688 C CA  . PRO   C 1 37 ? 25.988  -39.495 33.659  1.00 45.08  ? 36  PRO   C CA  1 
ATOM   1689 C C   . PRO   C 1 37 ? 26.944  -38.347 33.951  1.00 45.41  ? 36  PRO   C C   1 
ATOM   1690 O O   . PRO   C 1 37 ? 26.599  -37.185 33.730  1.00 40.80  ? 36  PRO   C O   1 
ATOM   1691 C CB  . PRO   C 1 37 ? 26.228  -40.147 32.288  1.00 43.37  ? 36  PRO   C CB  1 
ATOM   1692 C CG  . PRO   C 1 37 ? 24.812  -40.397 31.799  1.00 44.17  ? 36  PRO   C CG  1 
ATOM   1693 C CD  . PRO   C 1 37 ? 24.079  -39.119 32.194  1.00 44.17  ? 36  PRO   C CD  1 
ATOM   1694 N N   . PRO   C 1 38 ? 28.157  -38.635 34.474  1.00 44.24  ? 37  PRO   C N   1 
ATOM   1695 C CA  . PRO   C 1 38 ? 29.085  -37.578 34.860  1.00 39.25  ? 37  PRO   C CA  1 
ATOM   1696 C C   . PRO   C 1 38 ? 29.402  -36.680 33.677  1.00 37.67  ? 37  PRO   C C   1 
ATOM   1697 O O   . PRO   C 1 38 ? 29.665  -37.163 32.581  1.00 39.99  ? 37  PRO   C O   1 
ATOM   1698 C CB  . PRO   C 1 38 ? 30.310  -38.386 35.360  1.00 42.45  ? 37  PRO   C CB  1 
ATOM   1699 C CG  . PRO   C 1 38 ? 29.686  -39.690 35.830  1.00 39.13  ? 37  PRO   C CG  1 
ATOM   1700 C CD  . PRO   C 1 38 ? 28.686  -39.987 34.734  1.00 42.55  ? 37  PRO   C CD  1 
ATOM   1701 N N   . ASN   C 1 39 ? 29.343  -35.367 33.943  1.00 40.11  ? 38  ASN   C N   1 
ATOM   1702 C CA  . ASN   C 1 39 ? 29.750  -34.311 33.038  1.00 39.30  ? 38  ASN   C CA  1 
ATOM   1703 C C   . ASN   C 1 39 ? 28.807  -34.160 31.842  1.00 40.96  ? 38  ASN   C C   1 
ATOM   1704 O O   . ASN   C 1 39 ? 29.232  -33.571 30.850  1.00 41.07  ? 38  ASN   C O   1 
ATOM   1705 C CB  . ASN   C 1 39 ? 31.211  -34.413 32.604  1.00 41.06  ? 38  ASN   C CB  1 
ATOM   1706 C CG  . ASN   C 1 39 ? 31.772  -33.063 32.213  1.00 55.51  ? 38  ASN   C CG  1 
ATOM   1707 O OD1 . ASN   C 1 39 ? 31.511  -32.058 32.889  1.00 68.59  ? 38  ASN   C OD1 1 
ATOM   1708 N ND2 . ASN   C 1 39 ? 32.529  -33.005 31.125  1.00 57.91  ? 38  ASN   C ND2 1 
ATOM   1709 N N   . LYS   C 1 40 ? 27.552  -34.647 31.943  1.00 38.50  ? 39  LYS   C N   1 
ATOM   1710 C CA  . LYS   C 1 40 ? 26.600  -34.556 30.838  1.00 32.50  ? 39  LYS   C CA  1 
ATOM   1711 C C   . LYS   C 1 40 ? 25.459  -33.609 31.199  1.00 38.39  ? 39  LYS   C C   1 
ATOM   1712 O O   . LYS   C 1 40 ? 25.078  -33.496 32.362  1.00 36.08  ? 39  LYS   C O   1 
ATOM   1713 C CB  . LYS   C 1 40 ? 25.899  -35.881 30.519  1.00 32.59  ? 39  LYS   C CB  1 
ATOM   1714 C CG  . LYS   C 1 40 ? 26.819  -37.015 30.160  1.00 37.30  ? 39  LYS   C CG  1 
ATOM   1715 C CD  . LYS   C 1 40 ? 27.688  -36.832 28.932  1.00 40.92  ? 39  LYS   C CD  1 
ATOM   1716 C CE  . LYS   C 1 40 ? 28.479  -38.080 28.642  1.00 50.24  ? 39  LYS   C CE  1 
ATOM   1717 N NZ  . LYS   C 1 40 ? 29.668  -37.741 27.856  1.00 58.94  ? 39  LYS   C NZ  1 
ATOM   1718 N N   . TYR   C 1 41 ? 24.960  -32.890 30.184  1.00 32.11  ? 40  TYR   C N   1 
ATOM   1719 C CA  . TYR   C 1 41 ? 23.785  -32.037 30.305  1.00 34.50  ? 40  TYR   C CA  1 
ATOM   1720 C C   . TYR   C 1 41 ? 22.536  -32.734 29.788  1.00 34.75  ? 40  TYR   C C   1 
ATOM   1721 O O   . TYR   C 1 41 ? 22.592  -33.498 28.815  1.00 35.28  ? 40  TYR   C O   1 
ATOM   1722 C CB  . TYR   C 1 41 ? 23.912  -30.785 29.430  1.00 34.07  ? 40  TYR   C CB  1 
ATOM   1723 C CG  . TYR   C 1 41 ? 25.114  -29.934 29.807  1.00 32.41  ? 40  TYR   C CG  1 
ATOM   1724 C CD1 . TYR   C 1 41 ? 26.378  -30.202 29.282  1.00 35.47  ? 40  TYR   C CD1 1 
ATOM   1725 C CD2 . TYR   C 1 41 ? 24.989  -28.875 30.712  1.00 37.80  ? 40  TYR   C CD2 1 
ATOM   1726 C CE1 . TYR   C 1 41 ? 27.488  -29.451 29.628  1.00 42.72  ? 40  TYR   C CE1 1 
ATOM   1727 C CE2 . TYR   C 1 41 ? 26.095  -28.108 31.043  1.00 36.58  ? 40  TYR   C CE2 1 
ATOM   1728 C CZ  . TYR   C 1 41 ? 27.339  -28.400 30.517  1.00 45.01  ? 40  TYR   C CZ  1 
ATOM   1729 O OH  . TYR   C 1 41 ? 28.446  -27.663 30.843  1.00 53.06  ? 40  TYR   C OH  1 
ATOM   1730 N N   . PRO   C 1 42 ? 21.375  -32.436 30.422  1.00 35.89  ? 41  PRO   C N   1 
ATOM   1731 C CA  . PRO   C 1 42 ? 20.060  -32.789 29.886  1.00 38.02  ? 41  PRO   C CA  1 
ATOM   1732 C C   . PRO   C 1 42 ? 19.751  -31.803 28.766  1.00 36.83  ? 41  PRO   C C   1 
ATOM   1733 O O   . PRO   C 1 42 ? 19.834  -30.576 28.940  1.00 33.96  ? 41  PRO   C O   1 
ATOM   1734 C CB  . PRO   C 1 42 ? 19.076  -32.677 31.054  1.00 35.75  ? 41  PRO   C CB  1 
ATOM   1735 C CG  . PRO   C 1 42 ? 19.801  -31.818 32.058  1.00 35.50  ? 41  PRO   C CG  1 
ATOM   1736 C CD  . PRO   C 1 42 ? 21.270  -31.684 31.688  1.00 40.65  ? 41  PRO   C CD  1 
ATOM   1737 N N   . ILE   C 1 43 ? 19.494  -32.401 27.603  1.00 34.01  ? 42  ILE   C N   1 
ATOM   1738 C CA  . ILE   C 1 43 ? 19.222  -31.674 26.372  1.00 30.38  ? 42  ILE   C CA  1 
ATOM   1739 C C   . ILE   C 1 43 ? 17.774  -31.933 25.974  1.00 30.62  ? 42  ILE   C C   1 
ATOM   1740 O O   . ILE   C 1 43 ? 17.284  -33.067 26.021  1.00 32.08  ? 42  ILE   C O   1 
ATOM   1741 C CB  . ILE   C 1 43 ? 20.202  -32.086 25.257  1.00 29.63  ? 42  ILE   C CB  1 
ATOM   1742 C CG1 . ILE   C 1 43 ? 21.685  -31.782 25.615  1.00 30.81  ? 42  ILE   C CG1 1 
ATOM   1743 C CG2 . ILE   C 1 43 ? 19.782  -31.487 23.902  1.00 32.52  ? 42  ILE   C CG2 1 
ATOM   1744 C CD1 . ILE   C 1 43 ? 21.973  -30.350 26.057  1.00 32.70  ? 42  ILE   C CD1 1 
ATOM   1745 N N   . PHE   C 1 44 ? 17.092  -30.859 25.547  1.00 33.88  ? 43  PHE   C N   1 
ATOM   1746 C CA  . PHE   C 1 44 ? 15.793  -31.020 24.926  1.00 32.04  ? 43  PHE   C CA  1 
ATOM   1747 C C   . PHE   C 1 44 ? 15.909  -30.602 23.463  1.00 30.62  ? 43  PHE   C C   1 
ATOM   1748 O O   . PHE   C 1 44 ? 16.489  -29.560 23.172  1.00 30.65  ? 43  PHE   C O   1 
ATOM   1749 C CB  . PHE   C 1 44 ? 14.776  -30.133 25.657  1.00 36.56  ? 43  PHE   C CB  1 
ATOM   1750 C CG  . PHE   C 1 44 ? 13.416  -29.987 24.991  1.00 35.46  ? 43  PHE   C CG  1 
ATOM   1751 C CD1 . PHE   C 1 44 ? 12.405  -30.930 25.212  1.00 44.09  ? 43  PHE   C CD1 1 
ATOM   1752 C CD2 . PHE   C 1 44 ? 13.154  -28.923 24.123  1.00 40.92  ? 43  PHE   C CD2 1 
ATOM   1753 C CE1 . PHE   C 1 44 ? 11.162  -30.806 24.593  1.00 46.30  ? 43  PHE   C CE1 1 
ATOM   1754 C CE2 . PHE   C 1 44 ? 11.912  -28.802 23.501  1.00 42.99  ? 43  PHE   C CE2 1 
ATOM   1755 C CZ  . PHE   C 1 44 ? 10.919  -29.736 23.741  1.00 44.79  ? 43  PHE   C CZ  1 
ATOM   1756 N N   . PHE   C 1 45 ? 15.389  -31.449 22.566  1.00 31.11  ? 44  PHE   C N   1 
ATOM   1757 C CA  . PHE   C 1 45 ? 15.548  -31.257 21.129  1.00 33.80  ? 44  PHE   C CA  1 
ATOM   1758 C C   . PHE   C 1 45 ? 14.274  -30.614 20.594  1.00 32.18  ? 44  PHE   C C   1 
ATOM   1759 O O   . PHE   C 1 45 ? 13.189  -31.162 20.769  1.00 34.67  ? 44  PHE   C O   1 
ATOM   1760 C CB  . PHE   C 1 45 ? 15.839  -32.569 20.390  1.00 28.87  ? 44  PHE   C CB  1 
ATOM   1761 C CG  . PHE   C 1 45 ? 17.198  -33.195 20.692  1.00 30.34  ? 44  PHE   C CG  1 
ATOM   1762 C CD1 . PHE   C 1 45 ? 18.328  -32.810 19.982  1.00 28.49  ? 44  PHE   C CD1 1 
ATOM   1763 C CD2 . PHE   C 1 45 ? 17.346  -34.119 21.718  1.00 29.84  ? 44  PHE   C CD2 1 
ATOM   1764 C CE1 . PHE   C 1 45 ? 19.575  -33.352 20.265  1.00 32.52  ? 44  PHE   C CE1 1 
ATOM   1765 C CE2 . PHE   C 1 45 ? 18.590  -34.677 21.999  1.00 33.49  ? 44  PHE   C CE2 1 
ATOM   1766 C CZ  . PHE   C 1 45 ? 19.704  -34.298 21.272  1.00 32.43  ? 44  PHE   C CZ  1 
ATOM   1767 N N   . PHE   C 1 46 ? 14.417  -29.473 19.900  1.00 33.17  ? 45  PHE   C N   1 
ATOM   1768 C CA  . PHE   C 1 46 ? 13.243  -28.846 19.300  1.00 31.41  ? 45  PHE   C CA  1 
ATOM   1769 C C   . PHE   C 1 46 ? 12.729  -29.713 18.153  1.00 34.56  ? 45  PHE   C C   1 
ATOM   1770 O O   . PHE   C 1 46 ? 13.475  -30.497 17.562  1.00 33.27  ? 45  PHE   C O   1 
ATOM   1771 C CB  . PHE   C 1 46 ? 13.509  -27.401 18.842  1.00 32.08  ? 45  PHE   C CB  1 
ATOM   1772 C CG  . PHE   C 1 46 ? 13.839  -26.422 19.958  1.00 32.71  ? 45  PHE   C CG  1 
ATOM   1773 C CD1 . PHE   C 1 46 ? 12.838  -25.983 20.821  1.00 32.53  ? 45  PHE   C CD1 1 
ATOM   1774 C CD2 . PHE   C 1 46 ? 15.144  -25.951 20.145  1.00 29.31  ? 45  PHE   C CD2 1 
ATOM   1775 C CE1 . PHE   C 1 46 ? 13.152  -25.112 21.854  1.00 35.35  ? 45  PHE   C CE1 1 
ATOM   1776 C CE2 . PHE   C 1 46 ? 15.440  -25.068 21.170  1.00 35.07  ? 45  PHE   C CE2 1 
ATOM   1777 C CZ  . PHE   C 1 46 ? 14.449  -24.647 22.021  1.00 34.66  ? 45  PHE   C CZ  1 
ATOM   1778 N N   . GLY   C 1 47 ? 11.441  -29.558 17.806  1.00 30.93  ? 46  GLY   C N   1 
ATOM   1779 C CA  . GLY   C 1 47 ? 10.952  -30.273 16.650  1.00 32.66  ? 46  GLY   C CA  1 
ATOM   1780 C C   . GLY   C 1 47 ? 10.495  -31.668 17.058  1.00 37.79  ? 46  GLY   C C   1 
ATOM   1781 O O   . GLY   C 1 47 ? 9.300   -31.949 17.072  1.00 39.33  ? 46  GLY   C O   1 
ATOM   1782 N N   . THR   C 1 48 ? 11.453  -32.535 17.421  1.00 32.67  ? 47  THR   C N   1 
ATOM   1783 C CA  . THR   C 1 48 ? 11.087  -33.884 17.836  1.00 32.66  ? 47  THR   C CA  1 
ATOM   1784 C C   . THR   C 1 48 ? 10.603  -33.858 19.285  1.00 32.53  ? 47  THR   C C   1 
ATOM   1785 O O   . THR   C 1 48 ? 9.872   -34.755 19.699  1.00 36.56  ? 47  THR   C O   1 
ATOM   1786 C CB  . THR   C 1 48 ? 12.233  -34.885 17.688  1.00 33.24  ? 47  THR   C CB  1 
ATOM   1787 O OG1 . THR   C 1 48 ? 13.177  -34.380 18.637  1.00 34.01  ? 47  THR   C OG1 1 
ATOM   1788 C CG2 . THR   C 1 48 ? 12.753  -35.057 16.268  1.00 31.61  ? 47  THR   C CG2 1 
ATOM   1789 N N   . HIS   C 1 49 ? 11.072  -32.889 20.077  1.00 32.04  ? 48  HIS   C N   1 
ATOM   1790 C CA  . HIS   C 1 49 ? 10.728  -32.750 21.494  1.00 35.78  ? 48  HIS   C CA  1 
ATOM   1791 C C   . HIS   C 1 49 ? 11.180  -33.939 22.344  1.00 38.49  ? 48  HIS   C C   1 
ATOM   1792 O O   . HIS   C 1 49 ? 10.566  -34.212 23.379  1.00 43.48  ? 48  HIS   C O   1 
ATOM   1793 C CB  . HIS   C 1 49 ? 9.233   -32.475 21.731  1.00 41.71  ? 48  HIS   C CB  1 
ATOM   1794 C CG  . HIS   C 1 49 ? 8.656   -31.409 20.861  1.00 44.55  ? 48  HIS   C CG  1 
ATOM   1795 N ND1 . HIS   C 1 49 ? 7.513   -31.609 20.114  1.00 49.08  ? 48  HIS   C ND1 1 
ATOM   1796 C CD2 . HIS   C 1 49 ? 9.084   -30.187 20.566  1.00 41.83  ? 48  HIS   C CD2 1 
ATOM   1797 C CE1 . HIS   C 1 49 ? 7.249   -30.514 19.416  1.00 46.63  ? 48  HIS   C CE1 1 
ATOM   1798 N NE2 . HIS   C 1 49 ? 8.188   -29.637 19.685  1.00 48.87  ? 48  HIS   C NE2 1 
ATOM   1799 N N   . GLU   C 1 50 ? 12.276  -34.587 21.940  1.00 36.78  ? 49  GLU   C N   1 
ATOM   1800 C CA  . GLU   C 1 50 ? 12.873  -35.676 22.699  1.00 35.26  ? 49  GLU   C CA  1 
ATOM   1801 C C   . GLU   C 1 50 ? 13.969  -35.142 23.630  1.00 35.94  ? 49  GLU   C C   1 
ATOM   1802 O O   . GLU   C 1 50 ? 14.308  -33.956 23.632  1.00 32.42  ? 49  GLU   C O   1 
ATOM   1803 C CB  . GLU   C 1 50 ? 13.405  -36.737 21.733  1.00 39.94  ? 49  GLU   C CB  1 
ATOM   1804 C CG  . GLU   C 1 50 ? 12.346  -37.365 20.828  1.00 41.50  ? 49  GLU   C CG  1 
ATOM   1805 C CD  . GLU   C 1 50 ? 12.994  -38.252 19.769  1.00 52.24  ? 49  GLU   C CD  1 
ATOM   1806 O OE1 . GLU   C 1 50 ? 14.220  -38.450 19.856  1.00 54.09  ? 49  GLU   C OE1 1 
ATOM   1807 O OE2 . GLU   C 1 50 ? 12.298  -38.738 18.844  1.00 60.29  ? 49  GLU   C OE2 1 
ATOM   1808 N N   . THR   C 1 51 ? 14.492  -36.042 24.483  1.00 39.40  ? 50  THR   C N   1 
ATOM   1809 C CA  . THR   C 1 51 ? 15.494  -35.687 25.482  1.00 38.84  ? 50  THR   C CA  1 
ATOM   1810 C C   . THR   C 1 51 ? 16.638  -36.700 25.414  1.00 32.68  ? 50  THR   C C   1 
ATOM   1811 O O   . THR   C 1 51 ? 16.460  -37.819 24.942  1.00 32.56  ? 50  THR   C O   1 
ATOM   1812 C CB  . THR   C 1 51 ? 14.891  -35.583 26.887  1.00 40.10  ? 50  THR   C CB  1 
ATOM   1813 O OG1 . THR   C 1 51 ? 14.332  -36.876 27.094  1.00 40.05  ? 50  THR   C OG1 1 
ATOM   1814 C CG2 . THR   C 1 51 ? 13.909  -34.435 27.052  1.00 40.58  ? 50  THR   C CG2 1 
ATOM   1815 N N   . ALA   C 1 52 ? 17.835  -36.234 25.781  1.00 34.37  ? 51  ALA   C N   1 
ATOM   1816 C CA  . ALA   C 1 52 ? 19.054  -37.027 25.844  1.00 32.14  ? 51  ALA   C CA  1 
ATOM   1817 C C   . ALA   C 1 52 ? 20.046  -36.330 26.769  1.00 32.71  ? 51  ALA   C C   1 
ATOM   1818 O O   . ALA   C 1 52 ? 19.854  -35.179 27.149  1.00 40.33  ? 51  ALA   C O   1 
ATOM   1819 C CB  . ALA   C 1 52 ? 19.652  -37.257 24.471  1.00 31.87  ? 51  ALA   C CB  1 
ATOM   1820 N N   . PHE   C 1 53 ? 21.112  -37.051 27.156  1.00 35.36  ? 52  PHE   C N   1 
ATOM   1821 C CA  . PHE   C 1 53 ? 22.213  -36.495 27.924  1.00 36.16  ? 52  PHE   C CA  1 
ATOM   1822 C C   . PHE   C 1 53 ? 23.400  -36.361 26.988  1.00 33.68  ? 52  PHE   C C   1 
ATOM   1823 O O   . PHE   C 1 53 ? 23.713  -37.313 26.283  1.00 36.11  ? 52  PHE   C O   1 
ATOM   1824 C CB  . PHE   C 1 53 ? 22.591  -37.501 29.023  1.00 36.74  ? 52  PHE   C CB  1 
ATOM   1825 C CG  . PHE   C 1 53 ? 21.598  -37.434 30.168  1.00 37.41  ? 52  PHE   C CG  1 
ATOM   1826 C CD1 . PHE   C 1 53 ? 21.334  -36.222 30.797  1.00 39.28  ? 52  PHE   C CD1 1 
ATOM   1827 C CD2 . PHE   C 1 53 ? 20.880  -38.563 30.558  1.00 44.98  ? 52  PHE   C CD2 1 
ATOM   1828 C CE1 . PHE   C 1 53 ? 20.416  -36.147 31.838  1.00 46.74  ? 52  PHE   C CE1 1 
ATOM   1829 C CE2 . PHE   C 1 53 ? 19.960  -38.480 31.597  1.00 49.89  ? 52  PHE   C CE2 1 
ATOM   1830 C CZ  . PHE   C 1 53 ? 19.717  -37.272 32.221  1.00 45.46  ? 52  PHE   C CZ  1 
ATOM   1831 N N   . LEU   C 1 54 ? 24.053  -35.187 26.974  1.00 29.77  ? 53  LEU   C N   1 
ATOM   1832 C CA  . LEU   C 1 54 ? 25.189  -34.984 26.087  1.00 30.06  ? 53  LEU   C CA  1 
ATOM   1833 C C   . LEU   C 1 54 ? 26.273  -34.206 26.816  1.00 29.89  ? 53  LEU   C C   1 
ATOM   1834 O O   . LEU   C 1 54 ? 25.976  -33.419 27.694  1.00 33.05  ? 53  LEU   C O   1 
ATOM   1835 C CB  . LEU   C 1 54 ? 24.813  -34.229 24.811  1.00 30.49  ? 53  LEU   C CB  1 
ATOM   1836 C CG  . LEU   C 1 54 ? 24.014  -35.000 23.757  1.00 33.86  ? 53  LEU   C CG  1 
ATOM   1837 C CD1 . LEU   C 1 54 ? 23.658  -34.056 22.626  1.00 33.16  ? 53  LEU   C CD1 1 
ATOM   1838 C CD2 . LEU   C 1 54 ? 24.772  -36.190 23.175  1.00 43.73  ? 53  LEU   C CD2 1 
ATOM   1839 N N   . GLY   C 1 55 ? 27.512  -34.402 26.364  1.00 34.03  ? 54  GLY   C N   1 
ATOM   1840 C CA  . GLY   C 1 55 ? 28.659  -33.710 26.918  1.00 34.33  ? 54  GLY   C CA  1 
ATOM   1841 C C   . GLY   C 1 55 ? 28.951  -32.428 26.149  1.00 40.93  ? 54  GLY   C C   1 
ATOM   1842 O O   . GLY   C 1 55 ? 28.491  -32.255 25.011  1.00 39.38  ? 54  GLY   C O   1 
ATOM   1843 N N   . PRO   C 1 56 ? 29.744  -31.503 26.743  1.00 37.21  ? 55  PRO   C N   1 
ATOM   1844 C CA  . PRO   C 1 56 ? 29.927  -30.166 26.183  1.00 42.44  ? 55  PRO   C CA  1 
ATOM   1845 C C   . PRO   C 1 56 ? 30.586  -30.215 24.807  1.00 40.83  ? 55  PRO   C C   1 
ATOM   1846 O O   . PRO   C 1 56 ? 30.464  -29.268 24.028  1.00 52.99  ? 55  PRO   C O   1 
ATOM   1847 C CB  . PRO   C 1 56 ? 30.766  -29.399 27.254  1.00 42.13  ? 55  PRO   C CB  1 
ATOM   1848 C CG  . PRO   C 1 56 ? 31.499  -30.496 27.994  1.00 38.54  ? 55  PRO   C CG  1 
ATOM   1849 C CD  . PRO   C 1 56 ? 30.578  -31.724 27.940  1.00 38.62  ? 55  PRO   C CD  1 
ATOM   1850 N N   . LYS   C 1 57 ? 31.255  -31.331 24.501  1.00 44.05  ? 56  LYS   C N   1 
ATOM   1851 C CA  . LYS   C 1 57 ? 31.908  -31.502 23.210  1.00 45.89  ? 56  LYS   C CA  1 
ATOM   1852 C C   . LYS   C 1 57 ? 30.858  -31.538 22.099  1.00 42.91  ? 56  LYS   C C   1 
ATOM   1853 O O   . LYS   C 1 57 ? 31.185  -31.308 20.924  1.00 39.27  ? 56  LYS   C O   1 
ATOM   1854 C CB  . LYS   C 1 57 ? 32.737  -32.793 23.128  1.00 40.18  ? 56  LYS   C CB  1 
ATOM   1855 N N   . ASP   C 1 58 ? 29.609  -31.826 22.485  1.00 41.66  ? 57  ASP   C N   1 
ATOM   1856 C CA  . ASP   C 1 58 ? 28.571  -32.120 21.502  1.00 39.55  ? 57  ASP   C CA  1 
ATOM   1857 C C   . ASP   C 1 58 ? 27.616  -30.946 21.348  1.00 40.69  ? 57  ASP   C C   1 
ATOM   1858 O O   . ASP   C 1 58 ? 26.589  -31.082 20.683  1.00 39.45  ? 57  ASP   C O   1 
ATOM   1859 C CB  . ASP   C 1 58 ? 27.815  -33.394 21.837  1.00 38.69  ? 57  ASP   C CB  1 
ATOM   1860 C CG  . ASP   C 1 58 ? 28.680  -34.647 21.851  1.00 45.12  ? 57  ASP   C CG  1 
ATOM   1861 O OD1 . ASP   C 1 58 ? 29.562  -34.737 20.982  1.00 47.87  ? 57  ASP   C OD1 1 
ATOM   1862 O OD2 . ASP   C 1 58 ? 28.434  -35.542 22.692  1.00 50.00  ? 57  ASP   C OD2 1 
ATOM   1863 N N   . LEU   C 1 59 ? 27.944  -29.806 21.967  1.00 34.14  ? 58  LEU   C N   1 
ATOM   1864 C CA  . LEU   C 1 59 ? 26.997  -28.711 22.105  1.00 39.23  ? 58  LEU   C CA  1 
ATOM   1865 C C   . LEU   C 1 59 ? 27.606  -27.427 21.558  1.00 43.40  ? 58  LEU   C C   1 
ATOM   1866 O O   . LEU   C 1 59 ? 28.798  -27.196 21.756  1.00 44.65  ? 58  LEU   C O   1 
ATOM   1867 C CB  . LEU   C 1 59 ? 26.690  -28.538 23.589  1.00 32.47  ? 58  LEU   C CB  1 
ATOM   1868 C CG  . LEU   C 1 59 ? 26.132  -29.771 24.297  1.00 31.35  ? 58  LEU   C CG  1 
ATOM   1869 C CD1 . LEU   C 1 59 ? 25.848  -29.407 25.746  1.00 35.34  ? 58  LEU   C CD1 1 
ATOM   1870 C CD2 . LEU   C 1 59 ? 24.841  -30.222 23.597  1.00 27.26  ? 58  LEU   C CD2 1 
ATOM   1871 N N   . PHE   C 1 60 ? 26.771  -26.593 20.916  1.00 42.11  ? 59  PHE   C N   1 
ATOM   1872 C CA  . PHE   C 1 60 ? 27.257  -25.396 20.233  1.00 43.70  ? 59  PHE   C CA  1 
ATOM   1873 C C   . PHE   C 1 60 ? 26.291  -24.232 20.472  1.00 44.92  ? 59  PHE   C C   1 
ATOM   1874 O O   . PHE   C 1 60 ? 25.109  -24.316 20.147  1.00 40.62  ? 59  PHE   C O   1 
ATOM   1875 C CB  . PHE   C 1 60 ? 27.510  -25.695 18.747  1.00 44.19  ? 59  PHE   C CB  1 
ATOM   1876 C CG  . PHE   C 1 60 ? 28.452  -26.857 18.463  1.00 39.53  ? 59  PHE   C CG  1 
ATOM   1877 C CD1 . PHE   C 1 60 ? 27.987  -28.169 18.459  1.00 37.45  ? 59  PHE   C CD1 1 
ATOM   1878 C CD2 . PHE   C 1 60 ? 29.804  -26.643 18.196  1.00 41.42  ? 59  PHE   C CD2 1 
ATOM   1879 C CE1 . PHE   C 1 60 ? 28.841  -29.229 18.225  1.00 35.58  ? 59  PHE   C CE1 1 
ATOM   1880 C CE2 . PHE   C 1 60 ? 30.658  -27.711 17.938  1.00 41.32  ? 59  PHE   C CE2 1 
ATOM   1881 C CZ  . PHE   C 1 60 ? 30.178  -29.001 17.945  1.00 42.60  ? 59  PHE   C CZ  1 
ATOM   1882 N N   . PRO   C 1 61 ? 26.712  -23.090 21.077  1.00 47.68  ? 60  PRO   C N   1 
ATOM   1883 C CA  . PRO   C 1 61 ? 25.734  -22.062 21.438  1.00 45.29  ? 60  PRO   C CA  1 
ATOM   1884 C C   . PRO   C 1 61 ? 25.077  -21.603 20.140  1.00 40.13  ? 60  PRO   C C   1 
ATOM   1885 O O   . PRO   C 1 61 ? 25.727  -21.547 19.097  1.00 41.97  ? 60  PRO   C O   1 
ATOM   1886 C CB  . PRO   C 1 61 ? 26.501  -20.951 22.188  1.00 42.52  ? 60  PRO   C CB  1 
ATOM   1887 C CG  . PRO   C 1 61 ? 27.962  -21.351 22.052  1.00 45.36  ? 60  PRO   C CG  1 
ATOM   1888 C CD  . PRO   C 1 61 ? 28.097  -22.734 21.436  1.00 48.61  ? 60  PRO   C CD  1 
ATOM   1889 N N   . TYR   C 1 62 ? 23.763  -21.356 20.223  1.00 46.89  ? 61  TYR   C N   1 
ATOM   1890 C CA  . TYR   C 1 62 ? 22.891  -21.168 19.078  1.00 46.67  ? 61  TYR   C CA  1 
ATOM   1891 C C   . TYR   C 1 62 ? 23.311  -19.928 18.295  1.00 54.29  ? 61  TYR   C C   1 
ATOM   1892 O O   . TYR   C 1 62 ? 23.571  -20.021 17.095  1.00 52.24  ? 61  TYR   C O   1 
ATOM   1893 C CB  . TYR   C 1 62 ? 21.445  -21.029 19.560  1.00 53.00  ? 61  TYR   C CB  1 
ATOM   1894 C CG  . TYR   C 1 62 ? 20.456  -20.662 18.466  1.00 48.54  ? 61  TYR   C CG  1 
ATOM   1895 C CD1 . TYR   C 1 62 ? 20.387  -21.388 17.276  1.00 49.06  ? 61  TYR   C CD1 1 
ATOM   1896 C CD2 . TYR   C 1 62 ? 19.609  -19.566 18.616  1.00 52.02  ? 61  TYR   C CD2 1 
ATOM   1897 C CE1 . TYR   C 1 62 ? 19.484  -21.031 16.279  1.00 51.79  ? 61  TYR   C CE1 1 
ATOM   1898 C CE2 . TYR   C 1 62 ? 18.704  -19.206 17.629  1.00 49.20  ? 61  TYR   C CE2 1 
ATOM   1899 C CZ  . TYR   C 1 62 ? 18.651  -19.931 16.451  1.00 50.36  ? 61  TYR   C CZ  1 
ATOM   1900 O OH  . TYR   C 1 62 ? 17.759  -19.550 15.485  1.00 45.30  ? 61  TYR   C OH  1 
ATOM   1901 N N   . ASP   C 1 63 ? 23.406  -18.786 18.993  1.00 55.75  ? 62  ASP   C N   1 
ATOM   1902 C CA  . ASP   C 1 63 ? 23.684  -17.514 18.341  1.00 56.26  ? 62  ASP   C CA  1 
ATOM   1903 C C   . ASP   C 1 63 ? 25.045  -17.531 17.655  1.00 52.25  ? 62  ASP   C C   1 
ATOM   1904 O O   . ASP   C 1 63 ? 25.193  -16.919 16.597  1.00 59.97  ? 62  ASP   C O   1 
ATOM   1905 C CB  . ASP   C 1 63 ? 23.314  -16.326 19.213  1.00 61.12  ? 62  ASP   C CB  1 
ATOM   1906 C CG  . ASP   C 1 63 ? 21.813  -16.062 19.270  1.00 73.77  ? 62  ASP   C CG  1 
ATOM   1907 O OD1 . ASP   C 1 63 ? 21.203  -16.331 20.329  1.00 72.85  ? 62  ASP   C OD1 1 
ATOM   1908 O OD2 . ASP   C 1 63 ? 21.256  -15.606 18.242  1.00 78.38  ? 62  ASP   C OD2 1 
ATOM   1909 N N   . LYS   C 1 64 ? 25.997  -18.287 18.216  1.00 42.68  ? 63  LYS   C N   1 
ATOM   1910 C CA  . LYS   C 1 64 ? 27.338  -18.370 17.662  1.00 44.51  ? 63  LYS   C CA  1 
ATOM   1911 C C   . LYS   C 1 64 ? 27.366  -19.234 16.402  1.00 46.45  ? 63  LYS   C C   1 
ATOM   1912 O O   . LYS   C 1 64 ? 28.146  -18.953 15.499  1.00 44.59  ? 63  LYS   C O   1 
ATOM   1913 C CB  . LYS   C 1 64 ? 28.358  -18.923 18.667  1.00 47.66  ? 63  LYS   C CB  1 
ATOM   1914 N N   . SER   C 1 65 ? 26.533  -20.290 16.331  1.00 41.06  ? 64  SER   C N   1 
ATOM   1915 C CA  . SER   C 1 65 ? 26.796  -21.326 15.334  1.00 42.50  ? 64  SER   C CA  1 
ATOM   1916 C C   . SER   C 1 65 ? 25.668  -21.451 14.302  1.00 39.58  ? 64  SER   C C   1 
ATOM   1917 O O   . SER   C 1 65 ? 25.754  -22.302 13.420  1.00 40.64  ? 64  SER   C O   1 
ATOM   1918 C CB  . SER   C 1 65 ? 27.109  -22.668 15.981  1.00 41.39  ? 64  SER   C CB  1 
ATOM   1919 O OG  . SER   C 1 65 ? 25.939  -23.150 16.632  1.00 39.73  ? 64  SER   C OG  1 
ATOM   1920 N N   . LYS   C 1 66 ? 24.632  -20.612 14.413  1.00 40.10  ? 65  LYS   C N   1 
ATOM   1921 C CA  . LYS   C 1 66 ? 23.437  -20.764 13.588  1.00 42.78  ? 65  LYS   C CA  1 
ATOM   1922 C C   . LYS   C 1 66 ? 23.736  -20.530 12.110  1.00 43.32  ? 65  LYS   C C   1 
ATOM   1923 O O   . LYS   C 1 66 ? 23.108  -21.158 11.264  1.00 40.90  ? 65  LYS   C O   1 
ATOM   1924 C CB  . LYS   C 1 66 ? 22.222  -19.945 14.033  1.00 44.41  ? 65  LYS   C CB  1 
ATOM   1925 C CG  . LYS   C 1 66 ? 22.452  -18.456 14.105  1.00 43.47  ? 65  LYS   C CG  1 
ATOM   1926 C CD  . LYS   C 1 66 ? 21.164  -17.776 14.545  1.00 51.52  ? 65  LYS   C CD  1 
ATOM   1927 C CE  . LYS   C 1 66 ? 21.435  -16.344 14.900  1.00 48.32  ? 65  LYS   C CE  1 
ATOM   1928 N NZ  . LYS   C 1 66 ? 20.145  -15.703 15.150  1.00 46.38  ? 65  LYS   C NZ  1 
ATOM   1929 N N   . ASP   C 1 67 ? 24.718  -19.672 11.796  1.00 45.88  ? 66  ASP   C N   1 
ATOM   1930 C CA  . ASP   C 1 67 ? 25.077  -19.425 10.401  1.00 45.13  ? 66  ASP   C CA  1 
ATOM   1931 C C   . ASP   C 1 67 ? 25.555  -20.718 9.730   1.00 43.90  ? 66  ASP   C C   1 
ATOM   1932 O O   . ASP   C 1 67 ? 25.318  -20.920 8.542   1.00 40.82  ? 66  ASP   C O   1 
ATOM   1933 C CB  . ASP   C 1 67 ? 25.911  -18.158 10.209  1.00 44.42  ? 66  ASP   C CB  1 
ATOM   1934 C CG  . ASP   C 1 67 ? 27.418  -18.232 10.432  1.00 54.78  ? 66  ASP   C CG  1 
ATOM   1935 O OD1 . ASP   C 1 67 ? 28.054  -19.223 9.985   1.00 58.01  ? 66  ASP   C OD1 1 
ATOM   1936 O OD2 . ASP   C 1 67 ? 27.971  -17.252 10.988  1.00 57.53  ? 66  ASP   C OD2 1 
ATOM   1937 N N   . LYS   C 1 68 ? 26.144  -21.633 10.515  1.00 37.65  ? 67  LYS   C N   1 
ATOM   1938 C CA  . LYS   C 1 68 ? 26.602  -22.923 10.017  1.00 36.93  ? 67  LYS   C CA  1 
ATOM   1939 C C   . LYS   C 1 68 ? 25.508  -23.998 10.100  1.00 34.76  ? 67  LYS   C C   1 
ATOM   1940 O O   . LYS   C 1 68 ? 25.241  -24.682 9.110   1.00 39.11  ? 67  LYS   C O   1 
ATOM   1941 C CB  . LYS   C 1 68 ? 27.888  -23.304 10.763  1.00 35.99  ? 67  LYS   C CB  1 
ATOM   1942 C CG  . LYS   C 1 68 ? 28.593  -24.597 10.378  1.00 44.76  ? 67  LYS   C CG  1 
ATOM   1943 C CD  . LYS   C 1 68 ? 30.008  -24.681 10.958  1.00 50.86  ? 67  LYS   C CD  1 
ATOM   1944 C CE  . LYS   C 1 68 ? 30.579  -26.059 11.154  1.00 60.13  ? 67  LYS   C CE  1 
ATOM   1945 N NZ  . LYS   C 1 68 ? 30.707  -26.904 9.959   1.00 68.08  ? 67  LYS   C NZ  1 
ATOM   1946 N N   . TYR   C 1 69 ? 24.851  -24.140 11.260  1.00 33.47  ? 68  TYR   C N   1 
ATOM   1947 C CA  . TYR   C 1 69 ? 23.996  -25.306 11.476  1.00 30.73  ? 68  TYR   C CA  1 
ATOM   1948 C C   . TYR   C 1 69 ? 22.528  -24.967 11.231  1.00 30.37  ? 68  TYR   C C   1 
ATOM   1949 O O   . TYR   C 1 69 ? 21.733  -25.883 11.043  1.00 31.64  ? 68  TYR   C O   1 
ATOM   1950 C CB  . TYR   C 1 69 ? 24.151  -25.932 12.872  1.00 31.30  ? 68  TYR   C CB  1 
ATOM   1951 C CG  . TYR   C 1 69 ? 25.593  -26.350 13.152  1.00 32.04  ? 68  TYR   C CG  1 
ATOM   1952 C CD1 . TYR   C 1 69 ? 26.358  -27.022 12.203  1.00 35.44  ? 68  TYR   C CD1 1 
ATOM   1953 C CD2 . TYR   C 1 69 ? 26.186  -26.046 14.366  1.00 38.03  ? 68  TYR   C CD2 1 
ATOM   1954 C CE1 . TYR   C 1 69 ? 27.666  -27.411 12.459  1.00 35.78  ? 68  TYR   C CE1 1 
ATOM   1955 C CE2 . TYR   C 1 69 ? 27.494  -26.421 14.629  1.00 34.11  ? 68  TYR   C CE2 1 
ATOM   1956 C CZ  . TYR   C 1 69 ? 28.242  -27.083 13.677  1.00 35.46  ? 68  TYR   C CZ  1 
ATOM   1957 O OH  . TYR   C 1 69 ? 29.547  -27.373 14.011  1.00 39.31  ? 68  TYR   C OH  1 
ATOM   1958 N N   . GLY   C 1 70 ? 22.172  -23.676 11.287  1.00 29.75  ? 69  GLY   C N   1 
ATOM   1959 C CA  . GLY   C 1 70 ? 20.763  -23.298 11.218  1.00 31.34  ? 69  GLY   C CA  1 
ATOM   1960 C C   . GLY   C 1 70 ? 20.345  -23.134 9.762   1.00 33.32  ? 69  GLY   C C   1 
ATOM   1961 O O   . GLY   C 1 70 ? 20.278  -22.009 9.257   1.00 32.81  ? 69  GLY   C O   1 
ATOM   1962 N N   . LYS   C 1 71 ? 20.169  -24.281 9.104   1.00 36.68  ? 70  LYS   C N   1 
ATOM   1963 C CA  . LYS   C 1 71 ? 19.771  -24.384 7.707   1.00 35.32  ? 70  LYS   C CA  1 
ATOM   1964 C C   . LYS   C 1 71 ? 18.885  -25.616 7.603   1.00 33.26  ? 70  LYS   C C   1 
ATOM   1965 O O   . LYS   C 1 71 ? 19.028  -26.555 8.380   1.00 36.99  ? 70  LYS   C O   1 
ATOM   1966 C CB  . LYS   C 1 71 ? 20.933  -24.480 6.712   1.00 38.41  ? 70  LYS   C CB  1 
ATOM   1967 C CG  . LYS   C 1 71 ? 22.010  -25.501 7.037   1.00 44.60  ? 70  LYS   C CG  1 
ATOM   1968 C CD  . LYS   C 1 71 ? 22.978  -25.816 5.903   1.00 57.69  ? 70  LYS   C CD  1 
ATOM   1969 C CE  . LYS   C 1 71 ? 23.740  -27.076 6.166   1.00 59.53  ? 70  LYS   C CE  1 
ATOM   1970 N NZ  . LYS   C 1 71 ? 24.357  -27.049 7.494   1.00 62.21  ? 70  LYS   C NZ  1 
ATOM   1971 N N   . PRO   C 1 72 ? 17.896  -25.620 6.686   1.00 28.78  ? 71  PRO   C N   1 
ATOM   1972 C CA  . PRO   C 1 72 ? 16.928  -26.710 6.643   1.00 28.30  ? 71  PRO   C CA  1 
ATOM   1973 C C   . PRO   C 1 72 ? 17.558  -28.037 6.262   1.00 29.89  ? 71  PRO   C C   1 
ATOM   1974 O O   . PRO   C 1 72 ? 18.585  -28.060 5.601   1.00 33.19  ? 71  PRO   C O   1 
ATOM   1975 C CB  . PRO   C 1 72 ? 15.957  -26.227 5.559   1.00 29.07  ? 71  PRO   C CB  1 
ATOM   1976 C CG  . PRO   C 1 72 ? 16.100  -24.718 5.626   1.00 29.45  ? 71  PRO   C CG  1 
ATOM   1977 C CD  . PRO   C 1 72 ? 17.602  -24.519 5.740   1.00 28.82  ? 71  PRO   C CD  1 
ATOM   1978 N N   . ASN   C 1 73 ? 16.882  -29.122 6.636   1.00 32.01  ? 72  ASN   C N   1 
ATOM   1979 C CA  . ASN   C 1 73 ? 17.155  -30.411 6.024   1.00 37.80  ? 72  ASN   C CA  1 
ATOM   1980 C C   . ASN   C 1 73 ? 15.887  -31.244 6.143   1.00 35.58  ? 72  ASN   C C   1 
ATOM   1981 O O   . ASN   C 1 73 ? 14.905  -30.791 6.717   1.00 34.93  ? 72  ASN   C O   1 
ATOM   1982 C CB  . ASN   C 1 73 ? 18.391  -31.097 6.592   1.00 37.70  ? 72  ASN   C CB  1 
ATOM   1983 C CG  . ASN   C 1 73 ? 18.170  -31.472 8.034   1.00 37.88  ? 72  ASN   C CG  1 
ATOM   1984 O OD1 . ASN   C 1 73 ? 17.231  -32.212 8.377   1.00 39.41  ? 72  ASN   C OD1 1 
ATOM   1985 N ND2 . ASN   C 1 73 ? 19.008  -30.924 8.887   1.00 38.49  ? 72  ASN   C ND2 1 
ATOM   1986 N N   . LYS   C 1 74 ? 15.931  -32.460 5.594   1.00 37.85  ? 73  LYS   C N   1 
ATOM   1987 C CA  . LYS   C 1 74 ? 14.707  -33.232 5.439   1.00 32.83  ? 73  LYS   C CA  1 
ATOM   1988 C C   . LYS   C 1 74 ? 14.543  -34.229 6.584   1.00 35.17  ? 73  LYS   C C   1 
ATOM   1989 O O   . LYS   C 1 74 ? 13.606  -35.030 6.561   1.00 35.79  ? 73  LYS   C O   1 
ATOM   1990 C CB  . LYS   C 1 74 ? 14.708  -33.996 4.101   1.00 34.40  ? 73  LYS   C CB  1 
ATOM   1991 N N   . ARG   C 1 75 ? 15.454  -34.207 7.575   1.00 33.64  ? 74  ARG   C N   1 
ATOM   1992 C CA  . ARG   C 1 75 ? 15.281  -35.144 8.684   1.00 28.60  ? 74  ARG   C CA  1 
ATOM   1993 C C   . ARG   C 1 75 ? 14.020  -34.788 9.469   1.00 31.78  ? 74  ARG   C C   1 
ATOM   1994 O O   . ARG   C 1 75 ? 13.657  -33.611 9.622   1.00 32.81  ? 74  ARG   C O   1 
ATOM   1995 C CB  . ARG   C 1 75 ? 16.506  -35.254 9.614   1.00 33.13  ? 74  ARG   C CB  1 
ATOM   1996 C CG  . ARG   C 1 75 ? 17.885  -35.365 8.967   1.00 34.48  ? 74  ARG   C CG  1 
ATOM   1997 C CD  . ARG   C 1 75 ? 18.198  -36.702 8.276   1.00 39.36  ? 74  ARG   C CD  1 
ATOM   1998 N NE  . ARG   C 1 75 ? 18.150  -37.789 9.261   1.00 40.32  ? 74  ARG   C NE  1 
ATOM   1999 C CZ  . ARG   C 1 75 ? 19.241  -38.276 9.865   1.00 39.95  ? 74  ARG   C CZ  1 
ATOM   2000 N NH1 . ARG   C 1 75 ? 19.090  -38.970 10.973  1.00 42.56  ? 74  ARG   C NH1 1 
ATOM   2001 N NH2 . ARG   C 1 75 ? 20.450  -37.945 9.427   1.00 35.93  ? 74  ARG   C NH2 1 
ATOM   2002 N N   . LYS   C 1 76 ? 13.340  -35.844 9.948   1.00 33.41  ? 75  LYS   C N   1 
ATOM   2003 C CA  . LYS   C 1 76 ? 12.065  -35.756 10.647  1.00 36.12  ? 75  LYS   C CA  1 
ATOM   2004 C C   . LYS   C 1 76 ? 12.145  -34.787 11.824  1.00 35.57  ? 75  LYS   C C   1 
ATOM   2005 O O   . LYS   C 1 76 ? 12.966  -34.929 12.740  1.00 32.17  ? 75  LYS   C O   1 
ATOM   2006 C CB  . LYS   C 1 76 ? 11.424  -37.108 11.009  1.00 41.20  ? 75  LYS   C CB  1 
ATOM   2007 C CG  . LYS   C 1 76 ? 10.136  -37.008 11.826  1.00 46.97  ? 75  LYS   C CG  1 
ATOM   2008 C CD  . LYS   C 1 76 ? 9.105   -38.123 11.664  1.00 53.58  ? 75  LYS   C CD  1 
ATOM   2009 N N   . GLY   C 1 77 ? 11.247  -33.792 11.793  1.00 33.16  ? 76  GLY   C N   1 
ATOM   2010 C CA  . GLY   C 1 77 ? 11.093  -32.881 12.911  1.00 30.80  ? 76  GLY   C CA  1 
ATOM   2011 C C   . GLY   C 1 77 ? 12.078  -31.709 12.846  1.00 31.70  ? 76  GLY   C C   1 
ATOM   2012 O O   . GLY   C 1 77 ? 11.951  -30.771 13.623  1.00 33.41  ? 76  GLY   C O   1 
ATOM   2013 N N   . PHE   C 1 78 ? 13.025  -31.719 11.896  1.00 29.41  ? 77  PHE   C N   1 
ATOM   2014 C CA  . PHE   C 1 78 ? 14.114  -30.738 11.913  1.00 29.64  ? 77  PHE   C CA  1 
ATOM   2015 C C   . PHE   C 1 78 ? 13.619  -29.295 11.703  1.00 34.24  ? 77  PHE   C C   1 
ATOM   2016 O O   . PHE   C 1 78 ? 13.990  -28.342 12.419  1.00 28.59  ? 77  PHE   C O   1 
ATOM   2017 C CB  . PHE   C 1 78 ? 15.193  -31.065 10.874  1.00 32.38  ? 77  PHE   C CB  1 
ATOM   2018 C CG  . PHE   C 1 78 ? 16.499  -30.325 11.142  1.00 29.41  ? 77  PHE   C CG  1 
ATOM   2019 C CD1 . PHE   C 1 78 ? 16.731  -29.065 10.603  1.00 29.68  ? 77  PHE   C CD1 1 
ATOM   2020 C CD2 . PHE   C 1 78 ? 17.491  -30.882 11.941  1.00 29.19  ? 77  PHE   C CD2 1 
ATOM   2021 C CE1 . PHE   C 1 78 ? 17.920  -28.400 10.842  1.00 28.38  ? 77  PHE   C CE1 1 
ATOM   2022 C CE2 . PHE   C 1 78 ? 18.678  -30.199 12.205  1.00 26.59  ? 77  PHE   C CE2 1 
ATOM   2023 C CZ  . PHE   C 1 78 ? 18.890  -28.960 11.659  1.00 28.51  ? 77  PHE   C CZ  1 
ATOM   2024 N N   . ASN   C 1 79 ? 12.815  -29.127 10.652  1.00 33.13  ? 78  ASN   C N   1 
ATOM   2025 C CA  . ASN   C 1 79 ? 12.495  -27.784 10.201  1.00 34.78  ? 78  ASN   C CA  1 
ATOM   2026 C C   . ASN   C 1 79 ? 11.542  -27.143 11.204  1.00 32.16  ? 78  ASN   C C   1 
ATOM   2027 O O   . ASN   C 1 79 ? 11.608  -25.950 11.489  1.00 29.35  ? 78  ASN   C O   1 
ATOM   2028 C CB  . ASN   C 1 79 ? 12.018  -27.790 8.755   1.00 32.21  ? 78  ASN   C CB  1 
ATOM   2029 C CG  . ASN   C 1 79 ? 13.111  -28.160 7.784   1.00 30.24  ? 78  ASN   C CG  1 
ATOM   2030 O OD1 . ASN   C 1 79 ? 14.306  -27.951 8.062   1.00 30.35  ? 78  ASN   C OD1 1 
ATOM   2031 N ND2 . ASN   C 1 79 ? 12.720  -28.643 6.611   1.00 31.95  ? 78  ASN   C ND2 1 
ATOM   2032 N N   . GLU   C 1 80 ? 10.669  -27.958 11.791  1.00 33.48  ? 79  GLU   C N   1 
ATOM   2033 C CA  . GLU   C 1 80 ? 9.825   -27.446 12.853  1.00 30.48  ? 79  GLU   C CA  1 
ATOM   2034 C C   . GLU   C 1 80 ? 10.687  -27.051 14.048  1.00 37.22  ? 79  GLU   C C   1 
ATOM   2035 O O   . GLU   C 1 80 ? 10.383  -26.068 14.718  1.00 33.62  ? 79  GLU   C O   1 
ATOM   2036 C CB  . GLU   C 1 80 ? 8.735   -28.471 13.162  1.00 33.82  ? 79  GLU   C CB  1 
ATOM   2037 C CG  . GLU   C 1 80 ? 8.049   -28.219 14.494  1.00 42.30  ? 79  GLU   C CG  1 
ATOM   2038 C CD  . GLU   C 1 80 ? 6.716   -28.925 14.516  1.00 48.98  ? 79  GLU   C CD  1 
ATOM   2039 O OE1 . GLU   C 1 80 ? 6.602   -30.048 13.986  1.00 54.09  ? 79  GLU   C OE1 1 
ATOM   2040 O OE2 . GLU   C 1 80 ? 5.786   -28.338 15.081  1.00 51.74  ? 79  GLU   C OE2 1 
ATOM   2041 N N   . GLY   C 1 81 ? 11.764  -27.826 14.307  1.00 32.20  ? 80  GLY   C N   1 
ATOM   2042 C CA  . GLY   C 1 81 ? 12.734  -27.456 15.330  1.00 33.25  ? 80  GLY   C CA  1 
ATOM   2043 C C   . GLY   C 1 81 ? 13.400  -26.101 15.071  1.00 34.44  ? 80  GLY   C C   1 
ATOM   2044 O O   . GLY   C 1 81 ? 13.632  -25.335 15.998  1.00 30.97  ? 80  GLY   C O   1 
ATOM   2045 N N   . LEU   C 1 82 ? 13.771  -25.829 13.810  1.00 33.25  ? 81  LEU   C N   1 
ATOM   2046 C CA  . LEU   C 1 82 ? 14.395  -24.561 13.471  1.00 32.86  ? 81  LEU   C CA  1 
ATOM   2047 C C   . LEU   C 1 82 ? 13.395  -23.422 13.696  1.00 30.43  ? 81  LEU   C C   1 
ATOM   2048 O O   . LEU   C 1 82 ? 13.775  -22.334 14.122  1.00 34.04  ? 81  LEU   C O   1 
ATOM   2049 C CB  . LEU   C 1 82 ? 14.870  -24.569 12.022  1.00 35.86  ? 81  LEU   C CB  1 
ATOM   2050 C CG  . LEU   C 1 82 ? 16.112  -25.390 11.670  1.00 31.45  ? 81  LEU   C CG  1 
ATOM   2051 C CD1 . LEU   C 1 82 ? 16.287  -25.269 10.146  1.00 31.72  ? 81  LEU   C CD1 1 
ATOM   2052 C CD2 . LEU   C 1 82 ? 17.378  -24.892 12.320  1.00 29.68  ? 81  LEU   C CD2 1 
ATOM   2053 N N   . TRP   C 1 83 ? 12.117  -23.685 13.436  1.00 30.24  ? 82  TRP   C N   1 
ATOM   2054 C CA  . TRP   C 1 83 ? 11.099  -22.667 13.704  1.00 37.76  ? 82  TRP   C CA  1 
ATOM   2055 C C   . TRP   C 1 83 ? 11.040  -22.340 15.202  1.00 39.28  ? 82  TRP   C C   1 
ATOM   2056 O O   . TRP   C 1 83 ? 11.117  -21.170 15.605  1.00 38.97  ? 82  TRP   C O   1 
ATOM   2057 C CB  . TRP   C 1 83 ? 9.728   -23.102 13.173  1.00 38.55  ? 82  TRP   C CB  1 
ATOM   2058 C CG  . TRP   C 1 83 ? 8.717   -21.991 13.250  1.00 42.72  ? 82  TRP   C CG  1 
ATOM   2059 C CD1 . TRP   C 1 83 ? 8.468   -21.042 12.302  1.00 48.34  ? 82  TRP   C CD1 1 
ATOM   2060 C CD2 . TRP   C 1 83 ? 7.837   -21.692 14.355  1.00 47.88  ? 82  TRP   C CD2 1 
ATOM   2061 N NE1 . TRP   C 1 83 ? 7.494   -20.180 12.733  1.00 45.19  ? 82  TRP   C NE1 1 
ATOM   2062 C CE2 . TRP   C 1 83 ? 7.084   -20.554 13.982  1.00 48.74  ? 82  TRP   C CE2 1 
ATOM   2063 C CE3 . TRP   C 1 83 ? 7.614   -22.271 15.610  1.00 48.33  ? 82  TRP   C CE3 1 
ATOM   2064 C CZ2 . TRP   C 1 83 ? 6.130   -19.990 14.825  1.00 52.81  ? 82  TRP   C CZ2 1 
ATOM   2065 C CZ3 . TRP   C 1 83 ? 6.669   -21.712 16.445  1.00 51.21  ? 82  TRP   C CZ3 1 
ATOM   2066 C CH2 . TRP   C 1 83 ? 5.948   -20.581 16.058  1.00 52.31  ? 82  TRP   C CH2 1 
ATOM   2067 N N   . GLU   C 1 84 ? 10.979  -23.391 16.021  1.00 36.69  ? 83  GLU   C N   1 
ATOM   2068 C CA  . GLU   C 1 84 ? 10.858  -23.248 17.467  1.00 35.17  ? 83  GLU   C CA  1 
ATOM   2069 C C   . GLU   C 1 84 ? 12.036  -22.505 18.096  1.00 39.06  ? 83  GLU   C C   1 
ATOM   2070 O O   . GLU   C 1 84 ? 11.817  -21.678 18.984  1.00 43.05  ? 83  GLU   C O   1 
ATOM   2071 C CB  . GLU   C 1 84 ? 10.669  -24.602 18.149  1.00 33.94  ? 83  GLU   C CB  1 
ATOM   2072 C CG  . GLU   C 1 84 ? 9.338   -25.265 17.811  1.00 36.47  ? 83  GLU   C CG  1 
ATOM   2073 C CD  . GLU   C 1 84 ? 9.232   -26.672 18.349  1.00 43.99  ? 83  GLU   C CD  1 
ATOM   2074 O OE1 . GLU   C 1 84 ? 10.276  -27.153 18.849  1.00 39.56  ? 83  GLU   C OE1 1 
ATOM   2075 O OE2 . GLU   C 1 84 ? 8.140   -27.282 18.245  1.00 43.47  ? 83  GLU   C OE2 1 
ATOM   2076 N N   . ILE   C 1 85 ? 13.276  -22.802 17.670  1.00 36.83  ? 84  ILE   C N   1 
ATOM   2077 C CA  . ILE   C 1 85 ? 14.457  -22.242 18.312  1.00 35.45  ? 84  ILE   C CA  1 
ATOM   2078 C C   . ILE   C 1 85 ? 14.586  -20.741 18.029  1.00 37.54  ? 84  ILE   C C   1 
ATOM   2079 O O   . ILE   C 1 85 ? 15.101  -20.000 18.864  1.00 36.11  ? 84  ILE   C O   1 
ATOM   2080 C CB  . ILE   C 1 85 ? 15.747  -23.017 17.996  1.00 34.12  ? 84  ILE   C CB  1 
ATOM   2081 C CG1 . ILE   C 1 85 ? 16.851  -22.658 19.014  1.00 35.09  ? 84  ILE   C CG1 1 
ATOM   2082 C CG2 . ILE   C 1 85 ? 16.187  -22.817 16.536  1.00 36.50  ? 84  ILE   C CG2 1 
ATOM   2083 C CD1 . ILE   C 1 85 ? 18.080  -23.555 19.012  1.00 36.21  ? 84  ILE   C CD1 1 
ATOM   2084 N N   . GLN   C 1 86 ? 14.098  -20.310 16.858  1.00 35.89  ? 85  GLN   C N   1 
ATOM   2085 C CA  . GLN   C 1 86 ? 14.122  -18.906 16.476  1.00 37.15  ? 85  GLN   C CA  1 
ATOM   2086 C C   . GLN   C 1 86 ? 12.871  -18.169 16.952  1.00 36.35  ? 85  GLN   C C   1 
ATOM   2087 O O   . GLN   C 1 86 ? 12.933  -16.967 17.227  1.00 44.10  ? 85  GLN   C O   1 
ATOM   2088 C CB  . GLN   C 1 86 ? 14.260  -18.813 14.953  1.00 32.49  ? 85  GLN   C CB  1 
ATOM   2089 C CG  . GLN   C 1 86 ? 14.374  -17.392 14.406  1.00 34.56  ? 85  GLN   C CG  1 
ATOM   2090 C CD  . GLN   C 1 86 ? 14.732  -17.342 12.934  1.00 38.28  ? 85  GLN   C CD  1 
ATOM   2091 O OE1 . GLN   C 1 86 ? 14.688  -18.343 12.206  1.00 38.45  ? 85  GLN   C OE1 1 
ATOM   2092 N NE2 . GLN   C 1 86 ? 15.179  -16.174 12.491  1.00 37.22  ? 85  GLN   C NE2 1 
ATOM   2093 N N   . ASN   C 1 87 ? 11.734  -18.858 17.024  1.00 40.08  ? 86  ASN   C N   1 
ATOM   2094 C CA  . ASN   C 1 87 ? 10.482  -18.138 17.209  1.00 50.08  ? 86  ASN   C CA  1 
ATOM   2095 C C   . ASN   C 1 87 ? 9.875   -18.373 18.592  1.00 51.30  ? 86  ASN   C C   1 
ATOM   2096 O O   . ASN   C 1 87 ? 9.099   -17.544 19.055  1.00 54.20  ? 86  ASN   C O   1 
ATOM   2097 C CB  . ASN   C 1 87 ? 9.504   -18.353 16.057  1.00 49.02  ? 86  ASN   C CB  1 
ATOM   2098 C CG  . ASN   C 1 87 ? 10.084  -17.806 14.777  1.00 51.42  ? 86  ASN   C CG  1 
ATOM   2099 O OD1 . ASN   C 1 87 ? 10.180  -16.583 14.618  1.00 49.16  ? 86  ASN   C OD1 1 
ATOM   2100 N ND2 . ASN   C 1 87 ? 10.529  -18.688 13.891  1.00 46.46  ? 86  ASN   C ND2 1 
ATOM   2101 N N   . ASN   C 1 88 ? 10.209  -19.493 19.247  1.00 45.56  ? 87  ASN   C N   1 
ATOM   2102 C CA  . ASN   C 1 88 ? 9.529   -19.809 20.499  1.00 45.53  ? 87  ASN   C CA  1 
ATOM   2103 C C   . ASN   C 1 88 ? 10.422  -20.648 21.413  1.00 41.75  ? 87  ASN   C C   1 
ATOM   2104 O O   . ASN   C 1 88 ? 9.986   -21.690 21.894  1.00 52.64  ? 87  ASN   C O   1 
ATOM   2105 C CB  . ASN   C 1 88 ? 8.215   -20.545 20.266  1.00 45.39  ? 87  ASN   C CB  1 
ATOM   2106 C CG  . ASN   C 1 88 ? 7.271   -20.363 21.433  1.00 53.03  ? 87  ASN   C CG  1 
ATOM   2107 O OD1 . ASN   C 1 88 ? 7.558   -19.554 22.324  1.00 57.10  ? 87  ASN   C OD1 1 
ATOM   2108 N ND2 . ASN   C 1 88 ? 6.150   -21.073 21.444  1.00 54.21  ? 87  ASN   C ND2 1 
ATOM   2109 N N   . PRO   C 1 89 ? 11.675  -20.225 21.702  1.00 42.80  ? 88  PRO   C N   1 
ATOM   2110 C CA  . PRO   C 1 89 ? 12.676  -21.145 22.241  1.00 39.62  ? 88  PRO   C CA  1 
ATOM   2111 C C   . PRO   C 1 89 ? 12.406  -21.595 23.679  1.00 49.01  ? 88  PRO   C C   1 
ATOM   2112 O O   . PRO   C 1 89 ? 12.796  -22.702 24.061  1.00 46.19  ? 88  PRO   C O   1 
ATOM   2113 C CB  . PRO   C 1 89 ? 14.004  -20.387 22.089  1.00 42.43  ? 88  PRO   C CB  1 
ATOM   2114 C CG  . PRO   C 1 89 ? 13.602  -18.918 22.136  1.00 47.12  ? 88  PRO   C CG  1 
ATOM   2115 C CD  . PRO   C 1 89 ? 12.176  -18.851 21.593  1.00 43.93  ? 88  PRO   C CD  1 
ATOM   2116 N N   . HIS   C 1 90 ? 11.707  -20.761 24.465  1.00 52.81  ? 89  HIS   C N   1 
ATOM   2117 C CA  . HIS   C 1 90 ? 11.570  -21.048 25.893  1.00 50.82  ? 89  HIS   C CA  1 
ATOM   2118 C C   . HIS   C 1 90 ? 10.135  -21.397 26.273  1.00 56.17  ? 89  HIS   C C   1 
ATOM   2119 O O   . HIS   C 1 90 ? 9.722   -21.127 27.393  1.00 61.28  ? 89  HIS   C O   1 
ATOM   2120 C CB  . HIS   C 1 90 ? 12.091  -19.894 26.747  1.00 46.70  ? 89  HIS   C CB  1 
ATOM   2121 C CG  . HIS   C 1 90 ? 13.506  -19.580 26.452  1.00 45.76  ? 89  HIS   C CG  1 
ATOM   2122 N ND1 . HIS   C 1 90 ? 13.896  -18.423 25.822  1.00 50.76  ? 89  HIS   C ND1 1 
ATOM   2123 C CD2 . HIS   C 1 90 ? 14.624  -20.260 26.711  1.00 47.70  ? 89  HIS   C CD2 1 
ATOM   2124 C CE1 . HIS   C 1 90 ? 15.216  -18.414 25.702  1.00 46.80  ? 89  HIS   C CE1 1 
ATOM   2125 N NE2 . HIS   C 1 90 ? 15.677  -19.524 26.229  1.00 48.37  ? 89  HIS   C NE2 1 
ATOM   2126 N N   . ALA   C 1 91 ? 9.399   -22.033 25.356  1.00 58.65  ? 90  ALA   C N   1 
ATOM   2127 C CA  . ALA   C 1 91 ? 8.017   -22.411 25.606  1.00 65.11  ? 90  ALA   C CA  1 
ATOM   2128 C C   . ALA   C 1 91 ? 7.960   -23.613 26.544  1.00 73.86  ? 90  ALA   C C   1 
ATOM   2129 O O   . ALA   C 1 91 ? 8.676   -23.653 27.541  1.00 75.19  ? 90  ALA   C O   1 
ATOM   2130 C CB  . ALA   C 1 91 ? 7.292   -22.679 24.304  1.00 61.58  ? 90  ALA   C CB  1 
ATOM   2131 N N   . SER   C 1 92 ? 7.080   -24.573 26.219  1.00 83.89  ? 91  SER   C N   1 
ATOM   2132 C CA  . SER   C 1 92 ? 6.804   -25.725 27.064  1.00 82.64  ? 91  SER   C CA  1 
ATOM   2133 C C   . SER   C 1 92 ? 6.996   -27.016 26.274  1.00 88.33  ? 91  SER   C C   1 
ATOM   2134 O O   . SER   C 1 92 ? 7.948   -27.755 26.516  1.00 94.80  ? 91  SER   C O   1 
ATOM   2135 C CB  . SER   C 1 92 ? 5.418   -25.652 27.668  1.00 80.54  ? 91  SER   C CB  1 
ATOM   2136 O OG  . SER   C 1 92 ? 5.406   -24.816 28.815  1.00 79.28  ? 91  SER   C OG  1 
ATOM   2137 N N   . TYR   C 1 93 ? 6.079   -27.262 25.328  1.00 83.56  ? 92  TYR   C N   1 
ATOM   2138 C CA  . TYR   C 1 93 ? 6.049   -28.470 24.515  1.00 83.63  ? 92  TYR   C CA  1 
ATOM   2139 C C   . TYR   C 1 93 ? 5.873   -29.679 25.445  1.00 80.88  ? 92  TYR   C C   1 
ATOM   2140 O O   . TYR   C 1 93 ? 6.111   -30.808 24.965  1.00 89.12  ? 92  TYR   C O   1 
ATOM   2141 C CB  . TYR   C 1 93 ? 7.255   -28.585 23.568  1.00 74.91  ? 92  TYR   C CB  1 
ATOM   2142 C CG  . TYR   C 1 93 ? 7.629   -27.309 22.817  1.00 64.29  ? 92  TYR   C CG  1 
ATOM   2143 C CD1 . TYR   C 1 93 ? 6.996   -26.954 21.627  1.00 53.18  ? 92  TYR   C CD1 1 
ATOM   2144 C CD2 . TYR   C 1 93 ? 8.616   -26.454 23.307  1.00 66.91  ? 92  TYR   C CD2 1 
ATOM   2145 C CE1 . TYR   C 1 93 ? 7.332   -25.789 20.953  1.00 62.48  ? 92  TYR   C CE1 1 
ATOM   2146 C CE2 . TYR   C 1 93 ? 8.959   -25.286 22.641  1.00 63.36  ? 92  TYR   C CE2 1 
ATOM   2147 C CZ  . TYR   C 1 93 ? 8.317   -24.951 21.458  1.00 65.48  ? 92  TYR   C CZ  1 
ATOM   2148 O OH  . TYR   C 1 93 ? 8.656   -23.786 20.815  1.00 59.88  ? 92  TYR   C OH  1 
HETATM 2149 S S   . SO4   D 2 .  ? 0.828   -33.444 2.087   1.00 107.96 ? 101 SO4   A S   1 
HETATM 2150 O O1  . SO4   D 2 .  ? 1.026   -34.252 0.910   1.00 105.92 ? 101 SO4   A O1  1 
HETATM 2151 O O2  . SO4   D 2 .  ? 1.027   -32.057 1.760   1.00 97.24  ? 101 SO4   A O2  1 
HETATM 2152 O O3  . SO4   D 2 .  ? -0.512  -33.639 2.579   1.00 109.12 ? 101 SO4   A O3  1 
HETATM 2153 O O4  . SO4   D 2 .  ? 1.767   -33.831 3.101   1.00 97.42  ? 101 SO4   A O4  1 
HETATM 2154 S S   . SO4   E 2 .  ? -9.489  -24.751 1.406   1.00 87.46  ? 102 SO4   A S   1 
HETATM 2155 O O1  . SO4   E 2 .  ? -9.215  -24.504 0.019   1.00 75.06  ? 102 SO4   A O1  1 
HETATM 2156 O O2  . SO4   E 2 .  ? -9.275  -23.545 2.167   1.00 87.91  ? 102 SO4   A O2  1 
HETATM 2157 O O3  . SO4   E 2 .  ? -10.857 -25.181 1.544   1.00 94.64  ? 102 SO4   A O3  1 
HETATM 2158 O O4  . SO4   E 2 .  ? -8.609  -25.778 1.903   1.00 87.28  ? 102 SO4   A O4  1 
HETATM 2159 C C1  . EDO   F 3 .  ? 14.065  -19.551 -7.477  1.00 41.79  ? 103 EDO   A C1  1 
HETATM 2160 O O1  . EDO   F 3 .  ? 15.271  -18.798 -7.307  1.00 32.14  ? 103 EDO   A O1  1 
HETATM 2161 C C2  . EDO   F 3 .  ? 13.113  -19.035 -8.502  1.00 39.47  ? 103 EDO   A C2  1 
HETATM 2162 O O2  . EDO   F 3 .  ? 12.679  -17.705 -8.277  1.00 36.89  ? 103 EDO   A O2  1 
HETATM 2163 S S   . SO4   G 2 .  ? 8.823   -29.386 6.140   1.00 78.37  ? 104 SO4   A S   1 
HETATM 2164 O O1  . SO4   G 2 .  ? 9.946   -28.653 5.676   1.00 55.77  ? 104 SO4   A O1  1 
HETATM 2165 O O2  . SO4   G 2 .  ? 8.571   -30.487 5.241   1.00 79.63  ? 104 SO4   A O2  1 
HETATM 2166 O O3  . SO4   G 2 .  ? 9.097   -29.882 7.471   1.00 84.60  ? 104 SO4   A O3  1 
HETATM 2167 O O4  . SO4   G 2 .  ? 7.673   -28.526 6.170   1.00 83.06  ? 104 SO4   A O4  1 
HETATM 2168 S S   . SO4   H 2 .  ? 7.646   -8.462  -24.884 1.00 73.63  ? 101 SO4   B S   1 
HETATM 2169 O O1  . SO4   H 2 .  ? 8.743   -8.670  -25.794 1.00 42.63  ? 101 SO4   B O1  1 
HETATM 2170 O O2  . SO4   H 2 .  ? 6.404   -8.836  -25.528 1.00 60.80  ? 101 SO4   B O2  1 
HETATM 2171 O O3  . SO4   H 2 .  ? 7.805   -9.263  -23.665 1.00 49.99  ? 101 SO4   B O3  1 
HETATM 2172 O O4  . SO4   H 2 .  ? 7.634   -7.052  -24.560 1.00 52.54  ? 101 SO4   B O4  1 
HETATM 2173 S S   . SO4   I 2 .  ? 14.711  -27.148 -26.602 1.00 50.72  ? 102 SO4   B S   1 
HETATM 2174 O O1  . SO4   I 2 .  ? 16.116  -26.942 -26.389 1.00 47.96  ? 102 SO4   B O1  1 
HETATM 2175 O O2  . SO4   I 2 .  ? 14.529  -28.410 -27.276 1.00 60.81  ? 102 SO4   B O2  1 
HETATM 2176 O O3  . SO4   I 2 .  ? 14.045  -27.179 -25.325 1.00 58.40  ? 102 SO4   B O3  1 
HETATM 2177 O O4  . SO4   I 2 .  ? 14.159  -26.100 -27.409 1.00 50.23  ? 102 SO4   B O4  1 
HETATM 2178 N N1  . A1A3X J 4 .  ? 18.453  -16.797 -19.512 0.84 39.85  ? 103 A1A3X B N1  1 
HETATM 2179 C C4  . A1A3X J 4 .  ? 16.505  -15.692 -24.764 0.84 29.79  ? 103 A1A3X B C4  1 
HETATM 2180 C C5  . A1A3X J 4 .  ? 17.003  -16.406 -23.525 0.84 27.74  ? 103 A1A3X B C5  1 
HETATM 2181 C C6  . A1A3X J 4 .  ? 18.831  -16.662 -21.938 0.84 34.81  ? 103 A1A3X B C6  1 
HETATM 2182 C C7  . A1A3X J 4 .  ? 18.171  -16.035 -20.721 0.84 37.74  ? 103 A1A3X B C7  1 
HETATM 2183 N N   . A1A3X J 4 .  ? 18.405  -16.067 -23.223 0.84 31.41  ? 103 A1A3X B N   1 
HETATM 2184 C C1  . A1A3X J 4 .  ? 19.318  -16.374 -24.346 0.84 34.28  ? 103 A1A3X B C1  1 
HETATM 2185 C C   . A1A3X J 4 .  ? 20.770  -16.032 -24.023 0.84 34.83  ? 103 A1A3X B C   1 
HETATM 2186 C C3  . A1A3X J 4 .  ? 17.398  -16.011 -25.952 0.84 31.86  ? 103 A1A3X B C3  1 
HETATM 2187 C C2  . A1A3X J 4 .  ? 18.854  -15.702 -25.633 0.84 30.69  ? 103 A1A3X B C2  1 
HETATM 2188 C C1  . EDO   K 3 .  ? 17.011  -36.171 16.629  1.00 42.55  ? 101 EDO   C C1  1 
HETATM 2189 O O1  . EDO   K 3 .  ? 16.043  -37.066 16.142  1.00 48.08  ? 101 EDO   C O1  1 
HETATM 2190 C C2  . EDO   K 3 .  ? 16.445  -35.208 17.603  1.00 47.47  ? 101 EDO   C C2  1 
HETATM 2191 O O2  . EDO   K 3 .  ? 15.476  -35.843 18.402  1.00 46.36  ? 101 EDO   C O2  1 
HETATM 2192 S S   . SO4   L 2 .  ? 29.465  -38.115 12.287  1.00 105.42 ? 102 SO4   C S   1 
HETATM 2193 O O1  . SO4   L 2 .  ? 30.644  -37.544 11.689  1.00 100.84 ? 102 SO4   C O1  1 
HETATM 2194 O O2  . SO4   L 2 .  ? 28.367  -37.196 12.138  1.00 105.22 ? 102 SO4   C O2  1 
HETATM 2195 O O3  . SO4   L 2 .  ? 29.140  -39.358 11.639  1.00 99.52  ? 102 SO4   C O3  1 
HETATM 2196 O O4  . SO4   L 2 .  ? 29.707  -38.358 13.685  1.00 106.50 ? 102 SO4   C O4  1 
HETATM 2197 O O   . HOH   M 5 .  ? 6.011   -28.735 7.546   1.00 48.43  ? 201 HOH   A O   1 
HETATM 2198 O O   . HOH   M 5 .  ? 8.418   -32.531 4.319   1.00 56.78  ? 202 HOH   A O   1 
HETATM 2199 O O   . HOH   M 5 .  ? 1.772   -9.561  17.230  1.00 59.08  ? 203 HOH   A O   1 
HETATM 2200 O O   . HOH   M 5 .  ? 10.998  -23.605 9.870   1.00 47.46  ? 204 HOH   A O   1 
HETATM 2201 O O   . HOH   M 5 .  ? 12.423  -15.619 -12.348 1.00 55.78  ? 205 HOH   A O   1 
HETATM 2202 O O   . HOH   M 5 .  ? 3.587   -29.568 -0.248  1.00 41.48  ? 206 HOH   A O   1 
HETATM 2203 O O   . HOH   M 5 .  ? 1.564   0.304   -7.436  1.00 46.08  ? 207 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? 0.055   -33.954 5.017   1.00 57.44  ? 208 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? -3.603  -10.533 6.773   1.00 44.26  ? 209 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? -6.838  -5.373  9.107   1.00 34.23  ? 210 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 3.769   -34.619 4.480   1.00 57.99  ? 211 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? -4.374  -21.065 6.172   1.00 40.30  ? 212 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 13.722  -27.394 -5.056  1.00 47.55  ? 213 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 9.180   -18.225 -10.981 1.00 38.39  ? 214 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? 16.030  -24.545 1.908   1.00 42.64  ? 215 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? -5.669  -25.542 -5.532  1.00 58.66  ? 216 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 11.048  -29.602 3.258   1.00 43.41  ? 217 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? 9.748   -30.476 9.914   1.00 36.92  ? 218 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? 0.744   -10.588 -15.521 1.00 40.55  ? 219 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 10.001  -13.000 9.650   1.00 40.88  ? 220 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? 4.758   -7.908  1.460   1.00 38.56  ? 221 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? -2.555  -11.587 13.733  1.00 44.91  ? 222 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? -7.630  -17.215 6.785   1.00 43.62  ? 223 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 4.471   -3.611  -3.242  1.00 31.95  ? 224 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? -0.630  -29.333 10.235  1.00 53.47  ? 225 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 7.132   -10.537 -12.067 1.00 37.37  ? 226 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? -2.560  3.098   -2.098  1.00 44.07  ? 227 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? -8.389  -21.307 -1.094  1.00 37.45  ? 228 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 2.925   -10.520 -13.674 1.00 56.37  ? 229 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? -1.248  -7.635  11.551  1.00 52.15  ? 230 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? -5.619  -19.811 -5.536  1.00 38.02  ? 231 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 20.005  -15.316 7.265   1.00 30.96  ? 232 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 10.867  -9.825  -13.240 1.00 67.66  ? 233 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -5.680  -15.990 -7.949  1.00 29.92  ? 234 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? 10.848  -5.197  -7.754  1.00 34.70  ? 235 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? -8.078  -15.971 -1.004  1.00 37.47  ? 236 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 1.734   -4.850  -10.281 1.00 43.27  ? 237 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 9.666   -5.940  -1.630  1.00 35.52  ? 238 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? -1.722  -21.993 -0.429  1.00 29.42  ? 239 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? 11.157  -6.143  -3.920  1.00 55.78  ? 240 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 0.276   -23.145 9.480   1.00 45.94  ? 241 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 13.424  -11.954 -4.240  1.00 23.43  ? 242 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 2.381   -25.301 -10.015 1.00 38.74  ? 243 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? -7.090  -21.828 -5.658  1.00 46.72  ? 244 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 17.267  -12.882 1.388   1.00 18.43  ? 245 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? -0.687  -20.949 7.103   1.00 32.25  ? 246 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 13.509  -11.412 7.969   1.00 56.40  ? 247 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 15.789  -12.087 -5.353  1.00 35.13  ? 248 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 11.209  -16.649 -14.822 1.00 47.56  ? 249 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 8.335   -17.956 -15.845 1.00 49.35  ? 250 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 10.879  -32.084 7.192   1.00 44.41  ? 251 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 6.354   -5.815  0.376   1.00 51.38  ? 252 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 11.533  -12.341 -6.142  1.00 26.55  ? 253 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 11.609  -11.775 5.926   1.00 34.40  ? 254 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 2.694   -6.420  5.576   1.00 42.89  ? 255 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 0.908   -18.052 -18.834 1.00 55.06  ? 256 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 8.097   -7.864  1.176   1.00 37.31  ? 257 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? -1.409  -11.962 11.395  1.00 37.11  ? 258 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 12.779  -13.644 -8.417  1.00 39.34  ? 259 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? -6.358  -11.657 -11.473 1.00 41.56  ? 260 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 16.525  -28.862 2.264   1.00 59.08  ? 261 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 1.954   -27.285 -2.803  1.00 48.98  ? 262 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? -5.938  -12.682 6.768   1.00 35.68  ? 263 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -7.979  -16.622 1.903   1.00 44.64  ? 264 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 8.964   -16.528 -13.055 1.00 41.89  ? 265 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 1.818   -10.411 11.904  1.00 39.53  ? 266 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? 8.145   -17.417 8.645   1.00 37.67  ? 267 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? -6.291  -26.546 3.617   1.00 57.40  ? 268 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 21.343  -16.516 -3.603  1.00 35.11  ? 269 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 15.565  -9.229  -17.270 1.00 54.59  ? 270 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 6.832   -16.291 -14.909 1.00 52.72  ? 271 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 5.348   -7.768  4.044   1.00 35.21  ? 272 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 16.995  -17.994 -9.698  1.00 56.30  ? 273 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 9.463   -20.507 -18.422 1.00 45.13  ? 274 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 13.170  -9.239  -6.993  1.00 45.31  ? 275 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 2.314   -24.739 14.865  1.00 54.17  ? 276 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 11.035  -7.800  0.345   1.00 27.17  ? 277 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -3.708  -26.568 7.541   1.00 58.86  ? 278 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? -0.325  -20.575 11.398  1.00 52.92  ? 279 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 17.135  -12.880 -16.949 1.00 47.33  ? 280 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 4.014   -7.838  0.014   1.00 48.21  ? 281 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 15.347  -27.998 -0.751  1.00 54.99  ? 282 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 22.471  -16.585 -0.335  1.00 42.65  ? 283 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? -6.142  -14.534 -16.540 1.00 49.48  ? 284 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? -7.321  -11.600 -8.002  1.00 28.92  ? 285 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -3.654  -7.994  10.425  1.00 70.83  ? 286 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 9.341   -9.649  6.129   1.00 42.98  ? 287 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 9.252   -3.369  -0.018  1.00 56.32  ? 288 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -4.776  -7.964  -10.830 1.00 51.24  ? 289 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 2.834   -24.915 -2.400  1.00 54.54  ? 290 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -7.971  -19.994 -3.373  1.00 46.44  ? 291 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -11.443 -15.999 -3.722  1.00 48.52  ? 292 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 16.946  -10.288 -9.642  1.00 54.90  ? 293 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 9.047   -28.057 -7.722  1.00 57.42  ? 294 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? 8.300   -8.200  4.671   1.00 35.93  ? 295 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -9.869  -28.467 -1.333  1.00 58.91  ? 296 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? 8.785   -9.093  -13.825 1.00 40.54  ? 297 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? -7.236  -14.185 -9.339  1.00 46.00  ? 298 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 2.122   -24.379 -6.922  1.00 88.49  ? 299 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -0.669  -3.265  -10.953 1.00 53.59  ? 300 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 3.757   -27.414 -9.255  1.00 48.57  ? 301 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -5.466  -23.666 -7.061  1.00 51.83  ? 302 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 5.133   -7.140  -11.085 1.00 52.38  ? 303 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 0.967   -29.281 -7.152  1.00 61.13  ? 304 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? -9.615  -19.147 1.287   1.00 46.00  ? 305 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 4.848   7.429   -3.707  1.00 57.69  ? 306 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 4.491   -30.880 -2.235  1.00 48.19  ? 307 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 6.755   -30.660 -2.703  1.00 53.86  ? 308 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 4.781   -9.877  -11.341 1.00 45.25  ? 309 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? -7.030  -19.167 8.367   1.00 45.45  ? 310 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -11.309 -13.629 -2.792  1.00 39.56  ? 311 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? -3.195  -21.330 8.045   1.00 47.46  ? 312 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? -6.130  -23.300 5.755   1.00 47.17  ? 313 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -9.582  -21.440 -5.994  1.00 53.81  ? 314 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -5.505  -20.564 -8.379  1.00 63.88  ? 315 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? 3.864   -3.815  2.153   1.00 53.34  ? 316 HOH   A O   1 
HETATM 2313 O O   . HOH   N 5 .  ? 30.094  -13.051 -45.914 1.00 54.05  ? 201 HOH   B O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 30.971  -8.155  -30.312 1.00 52.31  ? 202 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 10.445  -19.821 -43.370 1.00 51.13  ? 203 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 3.095   -9.265  -27.424 1.00 53.65  ? 204 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 28.025  -8.158  -29.111 1.00 47.27  ? 205 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 6.846   -12.314 -26.247 1.00 34.92  ? 206 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 34.828  -23.325 -30.343 1.00 50.36  ? 207 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 25.710  -6.308  -36.124 1.00 39.05  ? 208 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 26.246  -4.887  -33.699 1.00 53.18  ? 209 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 21.275  -25.832 -30.141 1.00 59.06  ? 210 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 30.545  -19.897 -40.536 1.00 34.91  ? 211 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 25.260  -5.242  -30.176 1.00 40.57  ? 212 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 10.287  -11.581 -38.209 1.00 58.18  ? 213 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 24.576  -1.790  -36.626 1.00 47.71  ? 214 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 11.166  -8.294  -41.673 1.00 51.20  ? 215 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 7.626   -18.265 -32.222 1.00 54.88  ? 216 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 20.411  -21.967 -23.337 1.00 45.97  ? 217 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 7.555   -12.736 -38.878 1.00 49.83  ? 218 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 17.620  -19.653 -42.290 1.00 58.56  ? 219 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 8.804   -27.638 -37.863 1.00 64.47  ? 220 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 12.863  -4.854  -42.164 1.00 52.22  ? 221 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 7.222   -19.213 -35.246 1.00 51.99  ? 222 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 17.399  -7.727  -20.648 1.00 47.05  ? 223 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 26.410  -23.207 -31.308 1.00 35.08  ? 224 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 10.738  -18.910 -33.123 1.00 27.93  ? 225 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 23.774  -4.358  -37.101 1.00 32.75  ? 226 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 20.786  -13.553 -43.002 1.00 38.46  ? 227 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 16.916  -19.414 -28.955 1.00 26.36  ? 228 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 32.586  -18.924 -42.642 1.00 53.17  ? 229 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 7.579   -8.335  -21.011 1.00 45.65  ? 230 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 17.827  -3.619  -22.439 1.00 54.25  ? 231 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 16.061  -26.465 -34.810 1.00 42.71  ? 232 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 28.154  -17.689 -25.127 1.00 44.17  ? 233 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 20.633  -10.142 -43.084 1.00 38.73  ? 234 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 18.237  -0.753  -38.681 1.00 30.17  ? 235 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 4.709   -19.150 -25.872 1.00 49.16  ? 236 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 14.299  -6.344  -41.308 1.00 47.71  ? 237 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 18.350  -28.318 -27.552 1.00 53.50  ? 238 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 7.926   -23.541 -24.542 1.00 62.73  ? 239 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 23.735  -2.641  -29.342 1.00 41.10  ? 240 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 13.369  -22.628 -20.737 1.00 54.77  ? 241 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 27.555  -10.728 -29.199 1.00 52.67  ? 242 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 22.865  -23.230 -28.838 1.00 44.30  ? 243 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 10.806  -21.907 -33.002 1.00 40.27  ? 244 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 19.983  -25.787 -34.401 1.00 50.20  ? 245 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 31.832  -12.514 -39.122 1.00 56.22  ? 246 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 18.572  -25.902 -28.875 1.00 39.68  ? 247 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 21.320  -6.660  -42.748 1.00 40.89  ? 248 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 21.227  3.594   -32.914 1.00 34.07  ? 249 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 17.185  -9.942  -44.146 1.00 47.33  ? 250 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 6.651   -20.626 -25.034 1.00 57.05  ? 251 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 24.026  -11.302 -22.228 1.00 37.70  ? 252 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 32.214  -21.296 -38.384 1.00 42.30  ? 253 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 10.483  -16.932 -44.534 1.00 46.25  ? 254 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 4.308   -19.413 -31.312 1.00 44.66  ? 255 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 14.722  -24.392 -40.660 1.00 40.48  ? 256 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 19.385  -19.841 -19.548 1.00 51.83  ? 257 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 8.727   -8.737  -16.527 1.00 43.52  ? 258 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 21.424  -16.416 -20.212 1.00 60.26  ? 259 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 22.298  -4.024  -24.227 1.00 57.28  ? 260 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 28.048  -24.844 -35.165 1.00 39.76  ? 261 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 1.844   -13.307 -28.591 1.00 48.40  ? 262 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 6.858   -7.493  -34.318 1.00 77.55  ? 263 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 18.301  4.465   -34.533 1.00 40.15  ? 264 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 17.934  -0.625  -25.602 1.00 58.26  ? 265 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 26.356  -0.702  -29.491 1.00 45.16  ? 266 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 18.293  -16.211 -46.052 1.00 45.82  ? 267 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 24.868  -6.509  -42.982 1.00 42.53  ? 268 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 17.197  -25.388 -21.115 1.00 67.63  ? 269 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 9.758   -6.117  -41.169 1.00 43.56  ? 270 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 12.804  -20.483 -19.612 1.00 56.01  ? 271 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 5.589   -5.698  -29.611 1.00 59.37  ? 272 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 8.416   -21.519 -27.222 1.00 44.31  ? 273 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 19.968  3.773   -33.551 1.00 47.85  ? 274 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 15.316  -8.068  -43.207 1.00 46.26  ? 275 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 15.500  -22.085 -42.030 1.00 47.40  ? 276 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 26.701  -23.156 -28.574 1.00 52.15  ? 277 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 7.484   -4.347  -28.317 1.00 63.29  ? 278 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 40.392  -14.529 -39.361 1.00 62.96  ? 279 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 20.736  -19.573 -22.126 1.00 50.66  ? 280 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 35.948  -29.004 -35.316 1.00 52.36  ? 281 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 7.432   -9.919  -18.658 1.00 46.91  ? 282 HOH   B O   1 
HETATM 2395 O O   . HOH   N 5 .  ? 19.330  -8.497  -43.983 1.00 52.26  ? 283 HOH   B O   1 
HETATM 2396 O O   . HOH   N 5 .  ? 16.582  3.847   -26.778 1.00 66.83  ? 284 HOH   B O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 15.509  -27.085 28.515  1.00 48.86  ? 201 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 20.538  -19.885 30.244  1.00 60.76  ? 202 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 12.709  -28.089 28.401  1.00 59.84  ? 203 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 7.750   -31.393 12.420  1.00 41.90  ? 204 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 15.659  -39.159 17.187  1.00 55.34  ? 205 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 33.632  -24.105 31.614  1.00 43.87  ? 206 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 26.764  -38.937 12.651  1.00 37.03  ? 207 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 9.791   -30.174 11.350  1.00 50.79  ? 208 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 17.877  -17.178 14.911  1.00 51.70  ? 209 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 9.287   -19.180 24.068  1.00 65.63  ? 210 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 25.649  -19.610 6.359   1.00 36.76  ? 211 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 26.970  -37.729 10.051  1.00 38.72  ? 212 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 19.399  -19.986 10.593  1.00 40.78  ? 213 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 5.785   -26.607 17.000  1.00 55.31  ? 214 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 23.109  -41.428 18.463  1.00 41.95  ? 215 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 25.819  -19.849 30.152  1.00 58.97  ? 216 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 28.075  -19.444 12.597  1.00 60.78  ? 217 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 27.985  -15.124 12.577  1.00 70.42  ? 218 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 12.832  -31.414 8.377   1.00 37.75  ? 219 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 22.310  -28.496 11.163  1.00 28.91  ? 220 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 15.384  -20.939 12.493  1.00 39.30  ? 221 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 30.398  -31.745 15.619  1.00 50.21  ? 222 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 14.065  -37.114 13.880  1.00 39.46  ? 223 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 16.032  -17.534 19.463  1.00 52.07  ? 224 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 23.532  -18.339 21.665  1.00 54.78  ? 225 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 25.765  -33.709 34.995  1.00 53.32  ? 226 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 30.441  -40.400 9.465   1.00 34.39  ? 227 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 30.114  -39.638 31.492  1.00 38.63  ? 228 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 22.246  -34.365 16.561  1.00 27.96  ? 229 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 19.341  -26.576 3.420   1.00 56.11  ? 230 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 20.132  -41.905 12.095  1.00 29.15  ? 231 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 14.586  -29.565 4.262   1.00 43.66  ? 232 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 20.115  -41.053 39.135  1.00 82.45  ? 233 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 16.946  -37.911 19.860  1.00 60.39  ? 234 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 30.341  -25.017 32.592  1.00 59.63  ? 235 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 31.940  -43.174 11.904  1.00 49.08  ? 236 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 3.792   -21.972 22.674  1.00 63.79  ? 237 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 28.293  -37.393 15.964  1.00 52.86  ? 238 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 9.767   -37.245 18.373  1.00 61.93  ? 239 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 32.139  -33.633 25.877  1.00 46.93  ? 240 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 20.832  -29.569 4.707   1.00 55.13  ? 241 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 20.873  -28.720 8.583   1.00 34.36  ? 242 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 25.402  -31.415 10.713  1.00 32.68  ? 243 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 30.923  -35.334 28.792  1.00 44.81  ? 244 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 21.098  -39.865 26.568  1.00 36.31  ? 245 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 31.597  -43.350 15.639  1.00 54.78  ? 246 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 31.725  -39.639 27.145  1.00 47.67  ? 247 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 25.714  -39.520 20.157  1.00 38.15  ? 248 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 26.235  -17.700 13.676  1.00 47.23  ? 249 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 26.171  -17.615 21.070  1.00 66.73  ? 250 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 16.861  -33.160 2.882   1.00 88.70  ? 251 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 7.174   -17.913 10.840  1.00 42.30  ? 252 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 30.646  -17.885 9.402   1.00 46.26  ? 253 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 19.999  -18.937 25.041  1.00 49.10  ? 254 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 14.629  -38.594 9.755   1.00 48.62  ? 255 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 27.825  -37.446 25.107  1.00 54.37  ? 256 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 30.382  -32.693 18.174  1.00 43.78  ? 257 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 31.223  -33.512 35.728  1.00 56.42  ? 258 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 20.299  -12.942 13.453  1.00 50.95  ? 259 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 2.827   -28.767 13.648  1.00 54.18  ? 260 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 30.347  -21.922 24.426  1.00 75.77  ? 261 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 5.822   -33.928 23.503  1.00 58.33  ? 262 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 21.987  -13.534 13.137  1.00 47.10  ? 263 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 12.012  -21.442 10.742  1.00 42.08  ? 264 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 17.272  -36.988 29.324  1.00 64.32  ? 265 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 32.568  -39.121 30.022  1.00 48.95  ? 266 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 13.930  -22.460 28.090  1.00 79.74  ? 267 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 14.713  -39.103 11.747  1.00 48.25  ? 268 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 5.176   -24.202 18.666  1.00 57.11  ? 269 HOH   C O   1 
HETATM 2466 O O   . HOH   O 5 .  ? 28.812  -41.403 29.970  1.00 42.04  ? 270 HOH   C O   1 
HETATM 2467 O O   . HOH   O 5 .  ? 29.230  -40.338 19.636  1.00 68.37  ? 271 HOH   C O   1 
HETATM 2468 O O   . HOH   O 5 .  ? 33.731  -44.405 15.176  1.00 36.63  ? 272 HOH   C O   1 
HETATM 2469 O O   . HOH   O 5 .  ? 35.478  -22.693 22.847  1.00 58.25  ? 273 HOH   C O   1 
# 
