data_9NX6
# 
_entry.id   9NX6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9NX6         pdb_00009nx6 10.2210/pdb9nx6/pdb 
WWPDB D_1000294408 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ISSN'         
4  2 'Structure model' '_citation.page_first'              
5  2 'Structure model' '_citation.page_last'               
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation_author.identifier_ORCID' 
10 2 'Structure model' '_citation_author.name'             
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2025-04-02 
_pdbx_database_PDB_obs_spr.pdb_id           9NX6 
_pdbx_database_PDB_obs_spr.replace_pdb_id   8FDZ 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NX6 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'GARFTase in complex with AGF271 and GAR' 8FDX unspecified 
PDB 'GARFTase in complex with AGF305 and GAR' 8FE0 unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              cedann@iu.edu 
_pdbx_contact_author.name_first         Charles 
_pdbx_contact_author.name_last          Dann 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0117-9474 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wong-Roushar, J.' 1 0000-0002-3278-3711 
'Dann III, C.E.'   2 0000-0002-0117-9474 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Pharmacol Transl Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2575-910 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            6 
_citation.language                  ? 
_citation.page_first                748 
_citation.page_last                 770 
_citation.title                     
;Multitargeted 6-Substituted Thieno[2,3- d ]pyrimidines as Folate Receptor-Selective Anticancer Agents that Inhibit Cytosolic and Mitochondrial One-Carbon Metabolism.
;
_citation.year                      2023 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsptsci.3c00020 
_citation.pdbx_database_id_PubMed   37200803 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Tong, N.'           1  0000-0002-2934-999X 
primary 'Wong-Roushar, J.'   2  ?                   
primary 'Wallace-Povirk, A.' 3  ?                   
primary 'Shah, Y.'           4  0009-0000-5271-5567 
primary 'Nyman, M.C.'        5  ?                   
primary 'Katinas, J.M.'      6  ?                   
primary 'Schneider, M.'      7  ?                   
primary 
;O'Connor, C.
;
8  ?                   
primary 'Bao, X.'            9  ?                   
primary 'Kim, S.'            10 ?                   
primary 'Li, J.'             11 ?                   
primary 'Hou, Z.'            12 ?                   
primary 'Matherly, L.H.'     13 ?                   
primary 'Dann 3rd, C.E.'     14 ?                   
primary 'Gangjee, A.'        15 0000-0002-5513-7616 
# 
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 'Trifunctional purine biosynthetic protein adenosine-3' 22810.139 1  6.3.4.13,6.3.3.1,2.1.2.2 ? 
'UNP residues 808-1010' 'Full length GARFTase with 6-His tag on C-terminus' 
2 non-polymer syn 'GLYCINAMIDE RIBONUCLEOTIDE' 284.160   1  ?                        ? ?                       ? 
3 non-polymer syn 
'N-{4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]-3-fluorothiophene-2-carbonyl}-L-glutamic acid' 496.532   1  
?                        ? ?                       ?                                                   
4 water       nat water 18.015    53 ?                        ? ?                       ? 
# 
_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       
;MARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFS
IDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRG
DTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFS
IDIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRG
DTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'GLYCINAMIDE RIBONUCLEOTIDE'                                                                                         GAR   
3 'N-{4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]-3-fluorothiophene-2-carbonyl}-L-glutamic acid' A1B62 
4 water                                                                                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ARG n 
1 4   VAL n 
1 5   ALA n 
1 6   VAL n 
1 7   LEU n 
1 8   ILE n 
1 9   SER n 
1 10  GLY n 
1 11  THR n 
1 12  GLY n 
1 13  SER n 
1 14  ASN n 
1 15  LEU n 
1 16  GLN n 
1 17  ALA n 
1 18  LEU n 
1 19  ILE n 
1 20  ASP n 
1 21  SER n 
1 22  THR n 
1 23  ARG n 
1 24  GLU n 
1 25  PRO n 
1 26  ASN n 
1 27  SER n 
1 28  SER n 
1 29  ALA n 
1 30  GLN n 
1 31  ILE n 
1 32  ASP n 
1 33  ILE n 
1 34  VAL n 
1 35  ILE n 
1 36  SER n 
1 37  ASN n 
1 38  LYS n 
1 39  ALA n 
1 40  ALA n 
1 41  VAL n 
1 42  ALA n 
1 43  GLY n 
1 44  LEU n 
1 45  ASP n 
1 46  LYS n 
1 47  ALA n 
1 48  GLU n 
1 49  ARG n 
1 50  ALA n 
1 51  GLY n 
1 52  ILE n 
1 53  PRO n 
1 54  THR n 
1 55  ARG n 
1 56  VAL n 
1 57  ILE n 
1 58  ASN n 
1 59  HIS n 
1 60  LYS n 
1 61  LEU n 
1 62  TYR n 
1 63  LYS n 
1 64  ASN n 
1 65  ARG n 
1 66  VAL n 
1 67  GLU n 
1 68  PHE n 
1 69  ASP n 
1 70  SER n 
1 71  ALA n 
1 72  ILE n 
1 73  ASP n 
1 74  LEU n 
1 75  VAL n 
1 76  LEU n 
1 77  GLU n 
1 78  GLU n 
1 79  PHE n 
1 80  SER n 
1 81  ILE n 
1 82  ASP n 
1 83  ILE n 
1 84  VAL n 
1 85  CYS n 
1 86  LEU n 
1 87  ALA n 
1 88  GLY n 
1 89  PHE n 
1 90  MET n 
1 91  ARG n 
1 92  ILE n 
1 93  LEU n 
1 94  SER n 
1 95  GLY n 
1 96  PRO n 
1 97  PHE n 
1 98  VAL n 
1 99  GLN n 
1 100 LYS n 
1 101 TRP n 
1 102 ASN n 
1 103 GLY n 
1 104 LYS n 
1 105 MET n 
1 106 LEU n 
1 107 ASN n 
1 108 ILE n 
1 109 HIS n 
1 110 PRO n 
1 111 SER n 
1 112 LEU n 
1 113 LEU n 
1 114 PRO n 
1 115 SER n 
1 116 PHE n 
1 117 LYS n 
1 118 GLY n 
1 119 SER n 
1 120 ASN n 
1 121 ALA n 
1 122 HIS n 
1 123 GLU n 
1 124 GLN n 
1 125 ALA n 
1 126 LEU n 
1 127 GLU n 
1 128 THR n 
1 129 GLY n 
1 130 VAL n 
1 131 THR n 
1 132 VAL n 
1 133 THR n 
1 134 GLY n 
1 135 CYS n 
1 136 THR n 
1 137 VAL n 
1 138 HIS n 
1 139 PHE n 
1 140 VAL n 
1 141 ALA n 
1 142 GLU n 
1 143 ASP n 
1 144 VAL n 
1 145 ASP n 
1 146 ALA n 
1 147 GLY n 
1 148 GLN n 
1 149 ILE n 
1 150 ILE n 
1 151 LEU n 
1 152 GLN n 
1 153 GLU n 
1 154 ALA n 
1 155 VAL n 
1 156 PRO n 
1 157 VAL n 
1 158 LYS n 
1 159 ARG n 
1 160 GLY n 
1 161 ASP n 
1 162 THR n 
1 163 VAL n 
1 164 ALA n 
1 165 THR n 
1 166 LEU n 
1 167 SER n 
1 168 GLU n 
1 169 ARG n 
1 170 VAL n 
1 171 LYS n 
1 172 LEU n 
1 173 ALA n 
1 174 GLU n 
1 175 HIS n 
1 176 LYS n 
1 177 ILE n 
1 178 PHE n 
1 179 PRO n 
1 180 ALA n 
1 181 ALA n 
1 182 LEU n 
1 183 GLN n 
1 184 LEU n 
1 185 VAL n 
1 186 ALA n 
1 187 SER n 
1 188 GLY n 
1 189 THR n 
1 190 VAL n 
1 191 GLN n 
1 192 LEU n 
1 193 GLY n 
1 194 GLU n 
1 195 ASN n 
1 196 GLY n 
1 197 LYS n 
1 198 ILE n 
1 199 CYS n 
1 200 TRP n 
1 201 VAL n 
1 202 LYS n 
1 203 GLU n 
1 204 GLU n 
1 205 HIS n 
1 206 HIS n 
1 207 HIS n 
1 208 HIS n 
1 209 HIS n 
1 210 HIS 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                   210 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'GART, PGFT, PRGS' 
_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          ? 
_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 
A1B62 non-polymer         . 
'N-{4-[4-(2-amino-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidin-6-yl)butyl]-3-fluorothiophene-2-carbonyl}-L-glutamic acid' ? 
'C20 H21 F N4 O6 S2' 496.532 
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 
GAR   non-polymer         . 'GLYCINAMIDE RIBONUCLEOTIDE' ? 'C7 H13 N2 O8 P -2'  284.160 
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 
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   MET 1   807  ?    ?   ?   A . n 
A 1 2   ALA 2   808  808  ALA ALA A . n 
A 1 3   ARG 3   809  809  ARG ARG A . n 
A 1 4   VAL 4   810  810  VAL VAL A . n 
A 1 5   ALA 5   811  811  ALA ALA A . n 
A 1 6   VAL 6   812  812  VAL VAL A . n 
A 1 7   LEU 7   813  813  LEU LEU A . n 
A 1 8   ILE 8   814  814  ILE ILE A . n 
A 1 9   SER 9   815  815  SER SER A . n 
A 1 10  GLY 10  816  816  GLY GLY A . n 
A 1 11  THR 11  817  817  THR THR A . n 
A 1 12  GLY 12  818  818  GLY GLY A . n 
A 1 13  SER 13  819  819  SER SER A . n 
A 1 14  ASN 14  820  820  ASN ASN A . n 
A 1 15  LEU 15  821  821  LEU LEU A . n 
A 1 16  GLN 16  822  822  GLN GLN A . n 
A 1 17  ALA 17  823  823  ALA ALA A . n 
A 1 18  LEU 18  824  824  LEU LEU A . n 
A 1 19  ILE 19  825  825  ILE ILE A . n 
A 1 20  ASP 20  826  826  ASP ASP A . n 
A 1 21  SER 21  827  827  SER SER A . n 
A 1 22  THR 22  828  828  THR THR A . n 
A 1 23  ARG 23  829  829  ARG ARG A . n 
A 1 24  GLU 24  830  830  GLU GLU A . n 
A 1 25  PRO 25  831  831  PRO PRO A . n 
A 1 26  ASN 26  832  832  ASN ASN A . n 
A 1 27  SER 27  833  833  SER SER A . n 
A 1 28  SER 28  834  834  SER SER A . n 
A 1 29  ALA 29  835  835  ALA ALA A . n 
A 1 30  GLN 30  836  836  GLN GLN A . n 
A 1 31  ILE 31  837  837  ILE ILE A . n 
A 1 32  ASP 32  838  838  ASP ASP A . n 
A 1 33  ILE 33  839  839  ILE ILE A . n 
A 1 34  VAL 34  840  840  VAL VAL A . n 
A 1 35  ILE 35  841  841  ILE ILE A . n 
A 1 36  SER 36  842  842  SER SER A . n 
A 1 37  ASN 37  843  843  ASN ASN A . n 
A 1 38  LYS 38  844  844  LYS LYS A . n 
A 1 39  ALA 39  845  845  ALA ALA A . n 
A 1 40  ALA 40  846  846  ALA ALA A . n 
A 1 41  VAL 41  847  847  VAL VAL A . n 
A 1 42  ALA 42  848  848  ALA ALA A . n 
A 1 43  GLY 43  849  849  GLY GLY A . n 
A 1 44  LEU 44  850  850  LEU LEU A . n 
A 1 45  ASP 45  851  851  ASP ASP A . n 
A 1 46  LYS 46  852  852  LYS LYS A . n 
A 1 47  ALA 47  853  853  ALA ALA A . n 
A 1 48  GLU 48  854  854  GLU GLU A . n 
A 1 49  ARG 49  855  855  ARG ARG A . n 
A 1 50  ALA 50  856  856  ALA ALA A . n 
A 1 51  GLY 51  857  857  GLY GLY A . n 
A 1 52  ILE 52  858  858  ILE ILE A . n 
A 1 53  PRO 53  859  859  PRO PRO A . n 
A 1 54  THR 54  860  860  THR THR A . n 
A 1 55  ARG 55  861  861  ARG ARG A . n 
A 1 56  VAL 56  862  862  VAL VAL A . n 
A 1 57  ILE 57  863  863  ILE ILE A . n 
A 1 58  ASN 58  864  864  ASN ASN A . n 
A 1 59  HIS 59  865  865  HIS HIS A . n 
A 1 60  LYS 60  866  866  LYS LYS A . n 
A 1 61  LEU 61  867  867  LEU LEU A . n 
A 1 62  TYR 62  868  868  TYR TYR A . n 
A 1 63  LYS 63  869  869  LYS LYS A . n 
A 1 64  ASN 64  870  870  ASN ASN A . n 
A 1 65  ARG 65  871  871  ARG ARG A . n 
A 1 66  VAL 66  872  872  VAL VAL A . n 
A 1 67  GLU 67  873  873  GLU GLU A . n 
A 1 68  PHE 68  874  874  PHE PHE A . n 
A 1 69  ASP 69  875  875  ASP ASP A . n 
A 1 70  SER 70  876  876  SER SER A . n 
A 1 71  ALA 71  877  877  ALA ALA A . n 
A 1 72  ILE 72  878  878  ILE ILE A . n 
A 1 73  ASP 73  879  879  ASP ASP A . n 
A 1 74  LEU 74  880  880  LEU LEU A . n 
A 1 75  VAL 75  881  881  VAL VAL A . n 
A 1 76  LEU 76  882  882  LEU LEU A . n 
A 1 77  GLU 77  883  883  GLU GLU A . n 
A 1 78  GLU 78  884  884  GLU GLU A . n 
A 1 79  PHE 79  885  885  PHE PHE A . n 
A 1 80  SER 80  886  886  SER SER A . n 
A 1 81  ILE 81  887  887  ILE ILE A . n 
A 1 82  ASP 82  888  888  ASP ASP A . n 
A 1 83  ILE 83  889  889  ILE ILE A . n 
A 1 84  VAL 84  890  890  VAL VAL A . n 
A 1 85  CYS 85  891  891  CYS CYS A . n 
A 1 86  LEU 86  892  892  LEU LEU A . n 
A 1 87  ALA 87  893  893  ALA ALA A . n 
A 1 88  GLY 88  894  894  GLY GLY A . n 
A 1 89  PHE 89  895  895  PHE PHE A . n 
A 1 90  MET 90  896  896  MET MET A . n 
A 1 91  ARG 91  897  897  ARG ARG A . n 
A 1 92  ILE 92  898  898  ILE ILE A . n 
A 1 93  LEU 93  899  899  LEU LEU A . n 
A 1 94  SER 94  900  900  SER SER A . n 
A 1 95  GLY 95  901  901  GLY GLY A . n 
A 1 96  PRO 96  902  902  PRO PRO A . n 
A 1 97  PHE 97  903  903  PHE PHE A . n 
A 1 98  VAL 98  904  904  VAL VAL A . n 
A 1 99  GLN 99  905  905  GLN ALA A . n 
A 1 100 LYS 100 906  906  LYS LYS A . n 
A 1 101 TRP 101 907  907  TRP TRP A . n 
A 1 102 ASN 102 908  908  ASN ASN A . n 
A 1 103 GLY 103 909  909  GLY GLY A . n 
A 1 104 LYS 104 910  910  LYS LYS A . n 
A 1 105 MET 105 911  911  MET MET A . n 
A 1 106 LEU 106 912  912  LEU LEU A . n 
A 1 107 ASN 107 913  913  ASN ASN A . n 
A 1 108 ILE 108 914  914  ILE ILE A . n 
A 1 109 HIS 109 915  915  HIS HIS A . n 
A 1 110 PRO 110 916  916  PRO PRO A . n 
A 1 111 SER 111 917  917  SER SER A . n 
A 1 112 LEU 112 918  918  LEU LEU A . n 
A 1 113 LEU 113 919  919  LEU LEU A . n 
A 1 114 PRO 114 920  920  PRO PRO A . n 
A 1 115 SER 115 921  921  SER SER A . n 
A 1 116 PHE 116 922  922  PHE PHE A . n 
A 1 117 LYS 117 923  923  LYS LYS A . n 
A 1 118 GLY 118 924  924  GLY GLY A . n 
A 1 119 SER 119 925  925  SER SER A . n 
A 1 120 ASN 120 926  926  ASN ASN A . n 
A 1 121 ALA 121 927  927  ALA ALA A . n 
A 1 122 HIS 122 928  928  HIS HIS A . n 
A 1 123 GLU 123 929  929  GLU GLU A . n 
A 1 124 GLN 124 930  930  GLN GLN A . n 
A 1 125 ALA 125 931  931  ALA ALA A . n 
A 1 126 LEU 126 932  932  LEU LEU A . n 
A 1 127 GLU 127 933  933  GLU GLU A . n 
A 1 128 THR 128 934  934  THR THR A . n 
A 1 129 GLY 129 935  935  GLY GLY A . n 
A 1 130 VAL 130 936  936  VAL VAL A . n 
A 1 131 THR 131 937  937  THR THR A . n 
A 1 132 VAL 132 938  938  VAL VAL A . n 
A 1 133 THR 133 939  939  THR THR A . n 
A 1 134 GLY 134 940  940  GLY GLY A . n 
A 1 135 CYS 135 941  941  CYS CYS A . n 
A 1 136 THR 136 942  942  THR THR A . n 
A 1 137 VAL 137 943  943  VAL VAL A . n 
A 1 138 HIS 138 944  944  HIS HIS A . n 
A 1 139 PHE 139 945  945  PHE PHE A . n 
A 1 140 VAL 140 946  946  VAL VAL A . n 
A 1 141 ALA 141 947  947  ALA ALA A . n 
A 1 142 GLU 142 948  948  GLU GLU A . n 
A 1 143 ASP 143 949  949  ASP ASP A . n 
A 1 144 VAL 144 950  950  VAL VAL A . n 
A 1 145 ASP 145 951  951  ASP ASP A . n 
A 1 146 ALA 146 952  952  ALA ALA A . n 
A 1 147 GLY 147 953  953  GLY GLY A . n 
A 1 148 GLN 148 954  954  GLN GLN A . n 
A 1 149 ILE 149 955  955  ILE ILE A . n 
A 1 150 ILE 150 956  956  ILE ILE A . n 
A 1 151 LEU 151 957  957  LEU LEU A . n 
A 1 152 GLN 152 958  958  GLN GLN A . n 
A 1 153 GLU 153 959  959  GLU GLU A . n 
A 1 154 ALA 154 960  960  ALA ALA A . n 
A 1 155 VAL 155 961  961  VAL VAL A . n 
A 1 156 PRO 156 962  962  PRO PRO A . n 
A 1 157 VAL 157 963  963  VAL VAL A . n 
A 1 158 LYS 158 964  964  LYS LYS A . n 
A 1 159 ARG 159 965  965  ARG ARG A . n 
A 1 160 GLY 160 966  966  GLY GLY A . n 
A 1 161 ASP 161 967  967  ASP ASP A . n 
A 1 162 THR 162 968  968  THR THR A . n 
A 1 163 VAL 163 969  969  VAL VAL A . n 
A 1 164 ALA 164 970  970  ALA ALA A . n 
A 1 165 THR 165 971  971  THR THR A . n 
A 1 166 LEU 166 972  972  LEU LEU A . n 
A 1 167 SER 167 973  973  SER SER A . n 
A 1 168 GLU 168 974  974  GLU GLU A . n 
A 1 169 ARG 169 975  975  ARG ARG A . n 
A 1 170 VAL 170 976  976  VAL VAL A . n 
A 1 171 LYS 171 977  977  LYS LYS A . n 
A 1 172 LEU 172 978  978  LEU LEU A . n 
A 1 173 ALA 173 979  979  ALA ALA A . n 
A 1 174 GLU 174 980  980  GLU GLU A . n 
A 1 175 HIS 175 981  981  HIS HIS A . n 
A 1 176 LYS 176 982  982  LYS LYS A . n 
A 1 177 ILE 177 983  983  ILE ILE A . n 
A 1 178 PHE 178 984  984  PHE PHE A . n 
A 1 179 PRO 179 985  985  PRO PRO A . n 
A 1 180 ALA 180 986  986  ALA ALA A . n 
A 1 181 ALA 181 987  987  ALA ALA A . n 
A 1 182 LEU 182 988  988  LEU LEU A . n 
A 1 183 GLN 183 989  989  GLN GLN A . n 
A 1 184 LEU 184 990  990  LEU LEU A . n 
A 1 185 VAL 185 991  991  VAL VAL A . n 
A 1 186 ALA 186 992  992  ALA ALA A . n 
A 1 187 SER 187 993  993  SER SER A . n 
A 1 188 GLY 188 994  994  GLY GLY A . n 
A 1 189 THR 189 995  995  THR THR A . n 
A 1 190 VAL 190 996  996  VAL VAL A . n 
A 1 191 GLN 191 997  997  GLN GLN A . n 
A 1 192 LEU 192 998  998  LEU LEU A . n 
A 1 193 GLY 193 999  999  GLY GLY A . n 
A 1 194 GLU 194 1000 1000 GLU GLU A . n 
A 1 195 ASN 195 1001 1001 ASN ASN A . n 
A 1 196 GLY 196 1002 1002 GLY GLY A . n 
A 1 197 LYS 197 1003 1003 LYS LYS A . n 
A 1 198 ILE 198 1004 1004 ILE ILE A . n 
A 1 199 CYS 199 1005 1005 CYS CYS A . n 
A 1 200 TRP 200 1006 1006 TRP TRP A . n 
A 1 201 VAL 201 1007 1007 VAL VAL A . n 
A 1 202 LYS 202 1008 ?    ?   ?   A . n 
A 1 203 GLU 203 1009 ?    ?   ?   A . n 
A 1 204 GLU 204 1010 ?    ?   ?   A . n 
A 1 205 HIS 205 1011 ?    ?   ?   A . n 
A 1 206 HIS 206 1012 ?    ?   ?   A . n 
A 1 207 HIS 207 1013 ?    ?   ?   A . n 
A 1 208 HIS 208 1014 ?    ?   ?   A . n 
A 1 209 HIS 209 1015 ?    ?   ?   A . n 
A 1 210 HIS 210 1016 ?    ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1B62 ? ? A1B62 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GAR   ? ? GAR   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
B 2 GAR   1  1101 1101 GAR   GAR A . 
C 3 A1B62 1  1102 1201 A1B62 F32 A . 
D 4 HOH   1  1201 44   HOH   HOH A . 
D 4 HOH   2  1202 40   HOH   HOH A . 
D 4 HOH   3  1203 25   HOH   HOH A . 
D 4 HOH   4  1204 24   HOH   HOH A . 
D 4 HOH   5  1205 45   HOH   HOH A . 
D 4 HOH   6  1206 16   HOH   HOH A . 
D 4 HOH   7  1207 22   HOH   HOH A . 
D 4 HOH   8  1208 38   HOH   HOH A . 
D 4 HOH   9  1209 4    HOH   HOH A . 
D 4 HOH   10 1210 13   HOH   HOH A . 
D 4 HOH   11 1211 36   HOH   HOH A . 
D 4 HOH   12 1212 35   HOH   HOH A . 
D 4 HOH   13 1213 10   HOH   HOH A . 
D 4 HOH   14 1214 11   HOH   HOH A . 
D 4 HOH   15 1215 3    HOH   HOH A . 
D 4 HOH   16 1216 8    HOH   HOH A . 
D 4 HOH   17 1217 7    HOH   HOH A . 
D 4 HOH   18 1218 9    HOH   HOH A . 
D 4 HOH   19 1219 1    HOH   HOH A . 
D 4 HOH   20 1220 21   HOH   HOH A . 
D 4 HOH   21 1221 19   HOH   HOH A . 
D 4 HOH   22 1222 39   HOH   HOH A . 
D 4 HOH   23 1223 43   HOH   HOH A . 
D 4 HOH   24 1224 34   HOH   HOH A . 
D 4 HOH   25 1225 18   HOH   HOH A . 
D 4 HOH   26 1226 23   HOH   HOH A . 
D 4 HOH   27 1227 26   HOH   HOH A . 
D 4 HOH   28 1228 49   HOH   HOH A . 
D 4 HOH   29 1229 47   HOH   HOH A . 
D 4 HOH   30 1230 6    HOH   HOH A . 
D 4 HOH   31 1231 51   HOH   HOH A . 
D 4 HOH   32 1232 48   HOH   HOH A . 
D 4 HOH   33 1233 2    HOH   HOH A . 
D 4 HOH   34 1234 12   HOH   HOH A . 
D 4 HOH   35 1235 37   HOH   HOH A . 
D 4 HOH   36 1236 5    HOH   HOH A . 
D 4 HOH   37 1237 15   HOH   HOH A . 
D 4 HOH   38 1238 31   HOH   HOH A . 
D 4 HOH   39 1239 28   HOH   HOH A . 
D 4 HOH   40 1240 20   HOH   HOH A . 
D 4 HOH   41 1241 33   HOH   HOH A . 
D 4 HOH   42 1242 53   HOH   HOH A . 
D 4 HOH   43 1243 14   HOH   HOH A . 
D 4 HOH   44 1244 46   HOH   HOH A . 
D 4 HOH   45 1245 27   HOH   HOH A . 
D 4 HOH   46 1246 42   HOH   HOH A . 
D 4 HOH   47 1247 32   HOH   HOH A . 
D 4 HOH   48 1248 41   HOH   HOH A . 
D 4 HOH   49 1249 17   HOH   HOH A . 
D 4 HOH   50 1250 30   HOH   HOH A . 
D 4 HOH   51 1251 29   HOH   HOH A . 
D 4 HOH   52 1252 50   HOH   HOH A . 
D 4 HOH   53 1253 52   HOH   HOH A . 
# 
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 866  ? CG  ? A LYS 60  CG  
2  1 Y 1 A LYS 866  ? CD  ? A LYS 60  CD  
3  1 Y 1 A LYS 866  ? CE  ? A LYS 60  CE  
4  1 Y 1 A LYS 866  ? NZ  ? A LYS 60  NZ  
5  1 Y 1 A GLN 905  ? CG  ? A GLN 99  CG  
6  1 Y 1 A GLN 905  ? CD  ? A GLN 99  CD  
7  1 Y 1 A GLN 905  ? OE1 ? A GLN 99  OE1 
8  1 Y 1 A GLN 905  ? NE2 ? A GLN 99  NE2 
9  1 Y 1 A GLU 1000 ? CG  ? A GLU 194 CG  
10 1 Y 1 A GLU 1000 ? CD  ? A GLU 194 CD  
11 1 Y 1 A GLU 1000 ? OE1 ? A GLU 194 OE1 
12 1 Y 1 A GLU 1000 ? OE2 ? A GLU 194 OE2 
13 1 Y 1 A LYS 1003 ? CG  ? A LYS 197 CG  
14 1 Y 1 A LYS 1003 ? CD  ? A LYS 197 CD  
15 1 Y 1 A LYS 1003 ? CE  ? A LYS 197 CE  
16 1 Y 1 A LYS 1003 ? NZ  ? A LYS 197 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.18.2_3874 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NX6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.977 
_cell.length_a_esd                 ? 
_cell.length_b                     74.977 
_cell.length_b_esd                 ? 
_cell.length_c                     99.732 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9NX6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9NX6 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.57 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          65.54 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris-HCl pH 7.5, 0.33 M NaCl, 16-21% PEG 4000, and 2% PEG 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CMOS 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RDI CMOS_8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-06-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NX6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.48 
_reflns.d_resolution_low                               39.55 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     11884 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.48 
_reflns_shell.d_res_low                                     2.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             11949 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.365 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NX6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.48 
_refine.ls_d_res_low                             39.55 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     11884 
_refine.ls_number_reflns_R_free                  597 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.63 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2073 
_refine.ls_R_factor_R_free                       0.2492 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2051 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.03 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.48 
_refine_hist.d_res_low                        39.55 
_refine_hist.number_atoms_solvent             53 
_refine_hist.number_atoms_total               1595 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1491 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 1567 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.072  ? 2133 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.264 ? 227  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059  ? 256  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 271  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.48 2.73  . . 147 2735 99.00  . . . . 0.2874 . . . . . . . . . . . . . . . 0.3397 
'X-RAY DIFFRACTION' 2.73 3.12  . . 160 2790 100.00 . . . . 0.2290 . . . . . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 3.13 3.94  . . 138 2808 100.00 . . . . 0.2045 . . . . . . . . . . . . . . . 0.2547 
'X-RAY DIFFRACTION' 3.94 39.55 . . 152 2954 100.00 . . . . 0.1755 . . . . . . . . . . . . . . . 0.2091 
# 
_struct.entry_id                     9NX6 
_struct.title                        'Human GAR transformylase in complex with GAR substrate and AGF302 inhibitor' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9NX6 
_struct_keywords.text            'GARFTase, ligase, purine biosynthesis, monomer' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PUR2_HUMAN 
_struct_ref.pdbx_db_accession          P22102 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ARVAVLISGTGSNLQALIDSTREPNSSAQIDIVISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSI
DIVCLAGFMRILSGPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEAVPVKRGD
TVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
;
_struct_ref.pdbx_align_begin           808 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9NX6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 204 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P22102 
_struct_ref_seq.db_align_beg                  808 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1010 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       808 
_struct_ref_seq.pdbx_auth_seq_align_end       1010 
# 
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 9NX6 MET A 1   ? UNP P22102 ? ? 'initiating methionine' 807  1 
1 9NX6 HIS A 205 ? UNP P22102 ? ? 'expression tag'        1011 2 
1 9NX6 HIS A 206 ? UNP P22102 ? ? 'expression tag'        1012 3 
1 9NX6 HIS A 207 ? UNP P22102 ? ? 'expression tag'        1013 4 
1 9NX6 HIS A 208 ? UNP P22102 ? ? 'expression tag'        1014 5 
1 9NX6 HIS A 209 ? UNP P22102 ? ? 'expression tag'        1015 6 
1 9NX6 HIS A 210 ? UNP P22102 ? ? 'expression tag'        1016 7 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 12  ? ARG A 23  ? GLY A 818 ARG A 829 1 ? 12 
HELX_P HELX_P2 AA2 VAL A 41  ? ALA A 50  ? VAL A 847 ALA A 856 1 ? 10 
HELX_P HELX_P3 AA3 ASN A 64  ? PHE A 79  ? ASN A 870 PHE A 885 1 ? 16 
HELX_P HELX_P4 AA4 SER A 94  ? TRP A 101 ? SER A 900 TRP A 907 1 ? 8  
HELX_P HELX_P5 AA5 ASN A 120 ? GLY A 129 ? ASN A 926 GLY A 935 1 ? 10 
HELX_P HELX_P6 AA6 THR A 162 ? SER A 187 ? THR A 968 SER A 993 1 ? 26 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          LEU 
_struct_mon_prot_cis.label_seq_id           113 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           LEU 
_struct_mon_prot_cis.auth_seq_id            919 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    114 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     920 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       7.68 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? 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 54  ? VAL A 56  ? THR A 860  VAL A 862  
AA1 2 GLN A 30  ? SER A 36  ? GLN A 836  SER A 842  
AA1 3 ARG A 3   ? ILE A 8   ? ARG A 809  ILE A 814  
AA1 4 ILE A 83  ? LEU A 86  ? ILE A 889  LEU A 892  
AA1 5 MET A 105 ? HIS A 109 ? MET A 911  HIS A 915  
AA1 6 VAL A 132 ? PHE A 139 ? VAL A 938  PHE A 945  
AA1 7 ILE A 149 ? PRO A 156 ? ILE A 955  PRO A 962  
AA2 1 VAL A 190 ? LEU A 192 ? VAL A 996  LEU A 998  
AA2 2 ILE A 198 ? TRP A 200 ? ILE A 1004 TRP A 1006 
# 
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 ARG A 55  ? O ARG A 861 N SER A 36  ? N SER A 842  
AA1 2 3 O GLN A 30  ? O GLN A 836 N VAL A 4   ? N VAL A 810  
AA1 3 4 N ALA A 5   ? N ALA A 811 O CYS A 85  ? O CYS A 891  
AA1 4 5 N LEU A 86  ? N LEU A 892 O LEU A 106 ? O LEU A 912  
AA1 5 6 N HIS A 109 ? N HIS A 915 O THR A 136 ? O THR A 942  
AA1 6 7 N VAL A 137 ? N VAL A 943 O ILE A 150 ? O ILE A 956  
AA2 1 2 N GLN A 191 ? N GLN A 997 O CYS A 199 ? O CYS A 1005 
# 
_pdbx_entry_details.entry_id                   9NX6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 865 ? ? -79.19  26.11   
2 1 ALA A 893 ? ? -119.83 76.32   
3 1 MET A 896 ? ? -102.34 52.20   
4 1 PRO A 916 ? ? -89.60  48.84   
5 1 ASN A 926 ? ? -111.72 55.83   
6 1 THR A 939 ? ? -132.39 -150.85 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -31.9845 
_pdbx_refine_tls.origin_y         18.9075 
_pdbx_refine_tls.origin_z         27.9145 
_pdbx_refine_tls.T[1][1]          0.2568 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0062 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0035 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2252 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0161 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3152 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.8916 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.7605 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          1.2539 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.4760 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          1.2267 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.9887 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.1517 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0033 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.3757 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0709 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0262 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0661 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.3441 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0244 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.1645 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 MET 807  ? A MET 1   
2  1 Y 1 A LYS 1008 ? A LYS 202 
3  1 Y 1 A GLU 1009 ? A GLU 203 
4  1 Y 1 A GLU 1010 ? A GLU 204 
5  1 Y 1 A HIS 1011 ? A HIS 205 
6  1 Y 1 A HIS 1012 ? A HIS 206 
7  1 Y 1 A HIS 1013 ? A HIS 207 
8  1 Y 1 A HIS 1014 ? A HIS 208 
9  1 Y 1 A HIS 1015 ? A HIS 209 
10 1 Y 1 A HIS 1016 ? A HIS 210 
# 
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 
A1B62 C12  C Y N 1   
A1B62 C13  C Y N 2   
A1B62 C15  C Y N 3   
A1B62 C16  C Y N 4   
A1B62 C21  C N N 5   
A1B62 C22  C N N 6   
A1B62 C17  C N N 7   
A1B62 C23  C N N 8   
A1B62 N11  N N N 9   
A1B62 C20  C N S 10  
A1B62 C02  C N N 11  
A1B62 C04  C N N 12  
A1B62 C05  C Y N 13  
A1B62 C06  C Y N 14  
A1B62 C08  C Y N 15  
A1B62 C09  C Y N 16  
A1B62 C26  C N N 17  
A1B62 C29  C N N 18  
A1B62 C30  C N N 19  
A1B62 C31  C N N 20  
A1B62 C32  C N N 21  
A1B62 F33  F N N 22  
A1B62 N01  N N N 23  
A1B62 N03  N N N 24  
A1B62 N19  N N N 25  
A1B62 O10  O N N 26  
A1B62 O18  O N N 27  
A1B62 O24  O N N 28  
A1B62 O25  O N N 29  
A1B62 O27  O N N 30  
A1B62 O28  O N N 31  
A1B62 S07  S Y N 32  
A1B62 S14  S Y N 33  
A1B62 H1   H N N 34  
A1B62 H2   H N N 35  
A1B62 H3   H N N 36  
A1B62 H4   H N N 37  
A1B62 H5   H N N 38  
A1B62 H6   H N N 39  
A1B62 H7   H N N 40  
A1B62 H8   H N N 41  
A1B62 H9   H N N 42  
A1B62 H10  H N N 43  
A1B62 H11  H N N 44  
A1B62 H12  H N N 45  
A1B62 H13  H N N 46  
A1B62 H14  H N N 47  
A1B62 H15  H N N 48  
A1B62 H16  H N N 49  
A1B62 H17  H N N 50  
A1B62 H18  H N N 51  
A1B62 H19  H N N 52  
A1B62 H20  H N N 53  
A1B62 H21  H N N 54  
ALA   N    N N N 55  
ALA   CA   C N S 56  
ALA   C    C N N 57  
ALA   O    O N N 58  
ALA   CB   C N N 59  
ALA   OXT  O N N 60  
ALA   H    H N N 61  
ALA   H2   H N N 62  
ALA   HA   H N N 63  
ALA   HB1  H N N 64  
ALA   HB2  H N N 65  
ALA   HB3  H N N 66  
ALA   HXT  H N N 67  
ARG   N    N N N 68  
ARG   CA   C N S 69  
ARG   C    C N N 70  
ARG   O    O N N 71  
ARG   CB   C N N 72  
ARG   CG   C N N 73  
ARG   CD   C N N 74  
ARG   NE   N N N 75  
ARG   CZ   C N N 76  
ARG   NH1  N N N 77  
ARG   NH2  N N N 78  
ARG   OXT  O N N 79  
ARG   H    H N N 80  
ARG   H2   H N N 81  
ARG   HA   H N N 82  
ARG   HB2  H N N 83  
ARG   HB3  H N N 84  
ARG   HG2  H N N 85  
ARG   HG3  H N N 86  
ARG   HD2  H N N 87  
ARG   HD3  H N N 88  
ARG   HE   H N N 89  
ARG   HH11 H N N 90  
ARG   HH12 H N N 91  
ARG   HH21 H N N 92  
ARG   HH22 H N N 93  
ARG   HXT  H N N 94  
ASN   N    N N N 95  
ASN   CA   C N S 96  
ASN   C    C N N 97  
ASN   O    O N N 98  
ASN   CB   C N N 99  
ASN   CG   C N N 100 
ASN   OD1  O N N 101 
ASN   ND2  N N N 102 
ASN   OXT  O N N 103 
ASN   H    H N N 104 
ASN   H2   H N N 105 
ASN   HA   H N N 106 
ASN   HB2  H N N 107 
ASN   HB3  H N N 108 
ASN   HD21 H N N 109 
ASN   HD22 H N N 110 
ASN   HXT  H N N 111 
ASP   N    N N N 112 
ASP   CA   C N S 113 
ASP   C    C N N 114 
ASP   O    O N N 115 
ASP   CB   C N N 116 
ASP   CG   C N N 117 
ASP   OD1  O N N 118 
ASP   OD2  O N N 119 
ASP   OXT  O N N 120 
ASP   H    H N N 121 
ASP   H2   H N N 122 
ASP   HA   H N N 123 
ASP   HB2  H N N 124 
ASP   HB3  H N N 125 
ASP   HD2  H N N 126 
ASP   HXT  H N N 127 
CYS   N    N N N 128 
CYS   CA   C N R 129 
CYS   C    C N N 130 
CYS   O    O N N 131 
CYS   CB   C N N 132 
CYS   SG   S N N 133 
CYS   OXT  O N N 134 
CYS   H    H N N 135 
CYS   H2   H N N 136 
CYS   HA   H N N 137 
CYS   HB2  H N N 138 
CYS   HB3  H N N 139 
CYS   HG   H N N 140 
CYS   HXT  H N N 141 
GAR   C1   C N S 142 
GAR   O6   O N N 143 
GAR   C2   C N R 144 
GAR   O8   O N N 145 
GAR   C3   C N R 146 
GAR   O4   O N N 147 
GAR   C5   C N R 148 
GAR   C10  C N N 149 
GAR   O12  O N N 150 
GAR   N19  N N N 151 
GAR   C21  C N N 152 
GAR   O22  O N N 153 
GAR   C23  C N N 154 
GAR   N24  N N N 155 
GAR   P15  P N N 156 
GAR   O16  O N N 157 
GAR   O17  O N N 158 
GAR   O18  O N N 159 
GAR   H1   H N N 160 
GAR   HO6  H N N 161 
GAR   H2   H N N 162 
GAR   HO8  H N N 163 
GAR   H3   H N N 164 
GAR   H5   H N N 165 
GAR   H101 H N N 166 
GAR   H102 H N N 167 
GAR   H19  H N N 168 
GAR   H231 H N N 169 
GAR   H232 H N N 170 
GAR   H241 H N N 171 
GAR   H242 H N N 172 
GLN   N    N N N 173 
GLN   CA   C N S 174 
GLN   C    C N N 175 
GLN   O    O N N 176 
GLN   CB   C N N 177 
GLN   CG   C N N 178 
GLN   CD   C N N 179 
GLN   OE1  O N N 180 
GLN   NE2  N N N 181 
GLN   OXT  O N N 182 
GLN   H    H N N 183 
GLN   H2   H N N 184 
GLN   HA   H N N 185 
GLN   HB2  H N N 186 
GLN   HB3  H N N 187 
GLN   HG2  H N N 188 
GLN   HG3  H N N 189 
GLN   HE21 H N N 190 
GLN   HE22 H N N 191 
GLN   HXT  H N N 192 
GLU   N    N N N 193 
GLU   CA   C N S 194 
GLU   C    C N N 195 
GLU   O    O N N 196 
GLU   CB   C N N 197 
GLU   CG   C N N 198 
GLU   CD   C N N 199 
GLU   OE1  O N N 200 
GLU   OE2  O N N 201 
GLU   OXT  O N N 202 
GLU   H    H N N 203 
GLU   H2   H N N 204 
GLU   HA   H N N 205 
GLU   HB2  H N N 206 
GLU   HB3  H N N 207 
GLU   HG2  H N N 208 
GLU   HG3  H N N 209 
GLU   HE2  H N N 210 
GLU   HXT  H N N 211 
GLY   N    N N N 212 
GLY   CA   C N N 213 
GLY   C    C N N 214 
GLY   O    O N N 215 
GLY   OXT  O N N 216 
GLY   H    H N N 217 
GLY   H2   H N N 218 
GLY   HA2  H N N 219 
GLY   HA3  H N N 220 
GLY   HXT  H N N 221 
HIS   N    N N N 222 
HIS   CA   C N S 223 
HIS   C    C N N 224 
HIS   O    O N N 225 
HIS   CB   C N N 226 
HIS   CG   C Y N 227 
HIS   ND1  N Y N 228 
HIS   CD2  C Y N 229 
HIS   CE1  C Y N 230 
HIS   NE2  N Y N 231 
HIS   OXT  O N N 232 
HIS   H    H N N 233 
HIS   H2   H N N 234 
HIS   HA   H N N 235 
HIS   HB2  H N N 236 
HIS   HB3  H N N 237 
HIS   HD1  H N N 238 
HIS   HD2  H N N 239 
HIS   HE1  H N N 240 
HIS   HE2  H N N 241 
HIS   HXT  H N N 242 
HOH   O    O N N 243 
HOH   H1   H N N 244 
HOH   H2   H N N 245 
ILE   N    N N N 246 
ILE   CA   C N S 247 
ILE   C    C N N 248 
ILE   O    O N N 249 
ILE   CB   C N S 250 
ILE   CG1  C N N 251 
ILE   CG2  C N N 252 
ILE   CD1  C N N 253 
ILE   OXT  O N N 254 
ILE   H    H N N 255 
ILE   H2   H N N 256 
ILE   HA   H N N 257 
ILE   HB   H N N 258 
ILE   HG12 H N N 259 
ILE   HG13 H N N 260 
ILE   HG21 H N N 261 
ILE   HG22 H N N 262 
ILE   HG23 H N N 263 
ILE   HD11 H N N 264 
ILE   HD12 H N N 265 
ILE   HD13 H N N 266 
ILE   HXT  H N N 267 
LEU   N    N N N 268 
LEU   CA   C N S 269 
LEU   C    C N N 270 
LEU   O    O N N 271 
LEU   CB   C N N 272 
LEU   CG   C N N 273 
LEU   CD1  C N N 274 
LEU   CD2  C N N 275 
LEU   OXT  O N N 276 
LEU   H    H N N 277 
LEU   H2   H N N 278 
LEU   HA   H N N 279 
LEU   HB2  H N N 280 
LEU   HB3  H N N 281 
LEU   HG   H N N 282 
LEU   HD11 H N N 283 
LEU   HD12 H N N 284 
LEU   HD13 H N N 285 
LEU   HD21 H N N 286 
LEU   HD22 H N N 287 
LEU   HD23 H N N 288 
LEU   HXT  H N N 289 
LYS   N    N N N 290 
LYS   CA   C N S 291 
LYS   C    C N N 292 
LYS   O    O N N 293 
LYS   CB   C N N 294 
LYS   CG   C N N 295 
LYS   CD   C N N 296 
LYS   CE   C N N 297 
LYS   NZ   N N N 298 
LYS   OXT  O N N 299 
LYS   H    H N N 300 
LYS   H2   H N N 301 
LYS   HA   H N N 302 
LYS   HB2  H N N 303 
LYS   HB3  H N N 304 
LYS   HG2  H N N 305 
LYS   HG3  H N N 306 
LYS   HD2  H N N 307 
LYS   HD3  H N N 308 
LYS   HE2  H N N 309 
LYS   HE3  H N N 310 
LYS   HZ1  H N N 311 
LYS   HZ2  H N N 312 
LYS   HZ3  H N N 313 
LYS   HXT  H N N 314 
MET   N    N N N 315 
MET   CA   C N S 316 
MET   C    C N N 317 
MET   O    O N N 318 
MET   CB   C N N 319 
MET   CG   C N N 320 
MET   SD   S N N 321 
MET   CE   C N N 322 
MET   OXT  O N N 323 
MET   H    H N N 324 
MET   H2   H N N 325 
MET   HA   H N N 326 
MET   HB2  H N N 327 
MET   HB3  H N N 328 
MET   HG2  H N N 329 
MET   HG3  H N N 330 
MET   HE1  H N N 331 
MET   HE2  H N N 332 
MET   HE3  H N N 333 
MET   HXT  H N N 334 
PHE   N    N N N 335 
PHE   CA   C N S 336 
PHE   C    C N N 337 
PHE   O    O N N 338 
PHE   CB   C N N 339 
PHE   CG   C Y N 340 
PHE   CD1  C Y N 341 
PHE   CD2  C Y N 342 
PHE   CE1  C Y N 343 
PHE   CE2  C Y N 344 
PHE   CZ   C Y N 345 
PHE   OXT  O N N 346 
PHE   H    H N N 347 
PHE   H2   H N N 348 
PHE   HA   H N N 349 
PHE   HB2  H N N 350 
PHE   HB3  H N N 351 
PHE   HD1  H N N 352 
PHE   HD2  H N N 353 
PHE   HE1  H N N 354 
PHE   HE2  H N N 355 
PHE   HZ   H N N 356 
PHE   HXT  H N N 357 
PRO   N    N N N 358 
PRO   CA   C N S 359 
PRO   C    C N N 360 
PRO   O    O N N 361 
PRO   CB   C N N 362 
PRO   CG   C N N 363 
PRO   CD   C N N 364 
PRO   OXT  O N N 365 
PRO   H    H N N 366 
PRO   HA   H N N 367 
PRO   HB2  H N N 368 
PRO   HB3  H N N 369 
PRO   HG2  H N N 370 
PRO   HG3  H N N 371 
PRO   HD2  H N N 372 
PRO   HD3  H N N 373 
PRO   HXT  H N N 374 
SER   N    N N N 375 
SER   CA   C N S 376 
SER   C    C N N 377 
SER   O    O N N 378 
SER   CB   C N N 379 
SER   OG   O N N 380 
SER   OXT  O N N 381 
SER   H    H N N 382 
SER   H2   H N N 383 
SER   HA   H N N 384 
SER   HB2  H N N 385 
SER   HB3  H N N 386 
SER   HG   H N N 387 
SER   HXT  H N N 388 
THR   N    N N N 389 
THR   CA   C N S 390 
THR   C    C N N 391 
THR   O    O N N 392 
THR   CB   C N R 393 
THR   OG1  O N N 394 
THR   CG2  C N N 395 
THR   OXT  O N N 396 
THR   H    H N N 397 
THR   H2   H N N 398 
THR   HA   H N N 399 
THR   HB   H N N 400 
THR   HG1  H N N 401 
THR   HG21 H N N 402 
THR   HG22 H N N 403 
THR   HG23 H N N 404 
THR   HXT  H N N 405 
TRP   N    N N N 406 
TRP   CA   C N S 407 
TRP   C    C N N 408 
TRP   O    O N N 409 
TRP   CB   C N N 410 
TRP   CG   C Y N 411 
TRP   CD1  C Y N 412 
TRP   CD2  C Y N 413 
TRP   NE1  N Y N 414 
TRP   CE2  C Y N 415 
TRP   CE3  C Y N 416 
TRP   CZ2  C Y N 417 
TRP   CZ3  C Y N 418 
TRP   CH2  C Y N 419 
TRP   OXT  O N N 420 
TRP   H    H N N 421 
TRP   H2   H N N 422 
TRP   HA   H N N 423 
TRP   HB2  H N N 424 
TRP   HB3  H N N 425 
TRP   HD1  H N N 426 
TRP   HE1  H N N 427 
TRP   HE3  H N N 428 
TRP   HZ2  H N N 429 
TRP   HZ3  H N N 430 
TRP   HH2  H N N 431 
TRP   HXT  H N N 432 
TYR   N    N N N 433 
TYR   CA   C N S 434 
TYR   C    C N N 435 
TYR   O    O N N 436 
TYR   CB   C N N 437 
TYR   CG   C Y N 438 
TYR   CD1  C Y N 439 
TYR   CD2  C Y N 440 
TYR   CE1  C Y N 441 
TYR   CE2  C Y N 442 
TYR   CZ   C Y N 443 
TYR   OH   O N N 444 
TYR   OXT  O N N 445 
TYR   H    H N N 446 
TYR   H2   H N N 447 
TYR   HA   H N N 448 
TYR   HB2  H N N 449 
TYR   HB3  H N N 450 
TYR   HD1  H N N 451 
TYR   HD2  H N N 452 
TYR   HE1  H N N 453 
TYR   HE2  H N N 454 
TYR   HH   H N N 455 
TYR   HXT  H N N 456 
VAL   N    N N N 457 
VAL   CA   C N S 458 
VAL   C    C N N 459 
VAL   O    O N N 460 
VAL   CB   C N N 461 
VAL   CG1  C N N 462 
VAL   CG2  C N N 463 
VAL   OXT  O N N 464 
VAL   H    H N N 465 
VAL   H2   H N N 466 
VAL   HA   H N N 467 
VAL   HB   H N N 468 
VAL   HG11 H N N 469 
VAL   HG12 H N N 470 
VAL   HG13 H N N 471 
VAL   HG21 H N N 472 
VAL   HG22 H N N 473 
VAL   HG23 H N N 474 
VAL   HXT  H N N 475 
# 
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 
A1B62 N11 C02  sing N N 1   
A1B62 N03 C02  sing N N 2   
A1B62 N03 C04  sing N N 3   
A1B62 C02 N01  doub N N 4   
A1B62 O10 C04  doub N N 5   
A1B62 C04 C08  sing N N 6   
A1B62 N01 C09  sing N N 7   
A1B62 C08 C09  doub Y N 8   
A1B62 C08 C05  sing Y N 9   
A1B62 C09 S07  sing Y N 10  
A1B62 C05 C06  doub Y N 11  
A1B62 S07 C06  sing Y N 12  
A1B62 C06 C29  sing N N 13  
A1B62 C29 C30  sing N N 14  
A1B62 C30 C31  sing N N 15  
A1B62 C31 C32  sing N N 16  
A1B62 O28 C26  doub N N 17  
A1B62 C32 C16  sing N N 18  
A1B62 F33 C12  sing N N 19  
A1B62 C16 C12  sing Y N 20  
A1B62 C16 C15  doub Y N 21  
A1B62 C26 O27  sing N N 22  
A1B62 C26 C20  sing N N 23  
A1B62 C12 C13  doub Y N 24  
A1B62 C15 S14  sing Y N 25  
A1B62 C13 S14  sing Y N 26  
A1B62 C13 C17  sing N N 27  
A1B62 N19 C17  sing N N 28  
A1B62 N19 C20  sing N N 29  
A1B62 C17 O18  doub N N 30  
A1B62 C20 C21  sing N N 31  
A1B62 C21 C22  sing N N 32  
A1B62 O25 C23  doub N N 33  
A1B62 C22 C23  sing N N 34  
A1B62 C23 O24  sing N N 35  
A1B62 C15 H1   sing N N 36  
A1B62 C21 H2   sing N N 37  
A1B62 C21 H3   sing N N 38  
A1B62 C22 H4   sing N N 39  
A1B62 C22 H5   sing N N 40  
A1B62 N11 H6   sing N N 41  
A1B62 N11 H7   sing N N 42  
A1B62 C20 H8   sing N N 43  
A1B62 C05 H9   sing N N 44  
A1B62 C29 H10  sing N N 45  
A1B62 C29 H11  sing N N 46  
A1B62 C30 H12  sing N N 47  
A1B62 C30 H13  sing N N 48  
A1B62 C31 H14  sing N N 49  
A1B62 C31 H15  sing N N 50  
A1B62 C32 H16  sing N N 51  
A1B62 C32 H17  sing N N 52  
A1B62 N03 H18  sing N N 53  
A1B62 N19 H19  sing N N 54  
A1B62 O24 H20  sing N N 55  
A1B62 O27 H21  sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
GAR   C1  O6   sing N N 139 
GAR   C1  C2   sing N N 140 
GAR   C1  C5   sing N N 141 
GAR   C1  H1   sing N N 142 
GAR   O6  HO6  sing N N 143 
GAR   C2  O8   sing N N 144 
GAR   C2  C3   sing N N 145 
GAR   C2  H2   sing N N 146 
GAR   O8  HO8  sing N N 147 
GAR   C3  O4   sing N N 148 
GAR   C3  N19  sing N N 149 
GAR   C3  H3   sing N N 150 
GAR   O4  C5   sing N N 151 
GAR   C5  C10  sing N N 152 
GAR   C5  H5   sing N N 153 
GAR   C10 O12  sing N N 154 
GAR   C10 H101 sing N N 155 
GAR   C10 H102 sing N N 156 
GAR   O12 P15  sing N N 157 
GAR   N19 C21  sing N N 158 
GAR   N19 H19  sing N N 159 
GAR   C21 O22  doub N N 160 
GAR   C21 C23  sing N N 161 
GAR   C23 N24  sing N N 162 
GAR   C23 H231 sing N N 163 
GAR   C23 H232 sing N N 164 
GAR   N24 H241 sing N N 165 
GAR   N24 H242 sing N N 166 
GAR   P15 O16  doub N N 167 
GAR   P15 O17  sing N N 168 
GAR   P15 O18  sing N N 169 
GLN   N   CA   sing N N 170 
GLN   N   H    sing N N 171 
GLN   N   H2   sing N N 172 
GLN   CA  C    sing N N 173 
GLN   CA  CB   sing N N 174 
GLN   CA  HA   sing N N 175 
GLN   C   O    doub N N 176 
GLN   C   OXT  sing N N 177 
GLN   CB  CG   sing N N 178 
GLN   CB  HB2  sing N N 179 
GLN   CB  HB3  sing N N 180 
GLN   CG  CD   sing N N 181 
GLN   CG  HG2  sing N N 182 
GLN   CG  HG3  sing N N 183 
GLN   CD  OE1  doub N N 184 
GLN   CD  NE2  sing N N 185 
GLN   NE2 HE21 sing N N 186 
GLN   NE2 HE22 sing N N 187 
GLN   OXT HXT  sing N N 188 
GLU   N   CA   sing N N 189 
GLU   N   H    sing N N 190 
GLU   N   H2   sing N N 191 
GLU   CA  C    sing N N 192 
GLU   CA  CB   sing N N 193 
GLU   CA  HA   sing N N 194 
GLU   C   O    doub N N 195 
GLU   C   OXT  sing N N 196 
GLU   CB  CG   sing N N 197 
GLU   CB  HB2  sing N N 198 
GLU   CB  HB3  sing N N 199 
GLU   CG  CD   sing N N 200 
GLU   CG  HG2  sing N N 201 
GLU   CG  HG3  sing N N 202 
GLU   CD  OE1  doub N N 203 
GLU   CD  OE2  sing N N 204 
GLU   OE2 HE2  sing N N 205 
GLU   OXT HXT  sing N N 206 
GLY   N   CA   sing N N 207 
GLY   N   H    sing N N 208 
GLY   N   H2   sing N N 209 
GLY   CA  C    sing N N 210 
GLY   CA  HA2  sing N N 211 
GLY   CA  HA3  sing N N 212 
GLY   C   O    doub N N 213 
GLY   C   OXT  sing N N 214 
GLY   OXT HXT  sing N N 215 
HIS   N   CA   sing N N 216 
HIS   N   H    sing N N 217 
HIS   N   H2   sing N N 218 
HIS   CA  C    sing N N 219 
HIS   CA  CB   sing N N 220 
HIS   CA  HA   sing N N 221 
HIS   C   O    doub N N 222 
HIS   C   OXT  sing N N 223 
HIS   CB  CG   sing N N 224 
HIS   CB  HB2  sing N N 225 
HIS   CB  HB3  sing N N 226 
HIS   CG  ND1  sing Y N 227 
HIS   CG  CD2  doub Y N 228 
HIS   ND1 CE1  doub Y N 229 
HIS   ND1 HD1  sing N N 230 
HIS   CD2 NE2  sing Y N 231 
HIS   CD2 HD2  sing N N 232 
HIS   CE1 NE2  sing Y N 233 
HIS   CE1 HE1  sing N N 234 
HIS   NE2 HE2  sing N N 235 
HIS   OXT HXT  sing N N 236 
HOH   O   H1   sing N N 237 
HOH   O   H2   sing N N 238 
ILE   N   CA   sing N N 239 
ILE   N   H    sing N N 240 
ILE   N   H2   sing N N 241 
ILE   CA  C    sing N N 242 
ILE   CA  CB   sing N N 243 
ILE   CA  HA   sing N N 244 
ILE   C   O    doub N N 245 
ILE   C   OXT  sing N N 246 
ILE   CB  CG1  sing N N 247 
ILE   CB  CG2  sing N N 248 
ILE   CB  HB   sing N N 249 
ILE   CG1 CD1  sing N N 250 
ILE   CG1 HG12 sing N N 251 
ILE   CG1 HG13 sing N N 252 
ILE   CG2 HG21 sing N N 253 
ILE   CG2 HG22 sing N N 254 
ILE   CG2 HG23 sing N N 255 
ILE   CD1 HD11 sing N N 256 
ILE   CD1 HD12 sing N N 257 
ILE   CD1 HD13 sing N N 258 
ILE   OXT HXT  sing N N 259 
LEU   N   CA   sing N N 260 
LEU   N   H    sing N N 261 
LEU   N   H2   sing N N 262 
LEU   CA  C    sing N N 263 
LEU   CA  CB   sing N N 264 
LEU   CA  HA   sing N N 265 
LEU   C   O    doub N N 266 
LEU   C   OXT  sing N N 267 
LEU   CB  CG   sing N N 268 
LEU   CB  HB2  sing N N 269 
LEU   CB  HB3  sing N N 270 
LEU   CG  CD1  sing N N 271 
LEU   CG  CD2  sing N N 272 
LEU   CG  HG   sing N N 273 
LEU   CD1 HD11 sing N N 274 
LEU   CD1 HD12 sing N N 275 
LEU   CD1 HD13 sing N N 276 
LEU   CD2 HD21 sing N N 277 
LEU   CD2 HD22 sing N N 278 
LEU   CD2 HD23 sing N N 279 
LEU   OXT HXT  sing N N 280 
LYS   N   CA   sing N N 281 
LYS   N   H    sing N N 282 
LYS   N   H2   sing N N 283 
LYS   CA  C    sing N N 284 
LYS   CA  CB   sing N N 285 
LYS   CA  HA   sing N N 286 
LYS   C   O    doub N N 287 
LYS   C   OXT  sing N N 288 
LYS   CB  CG   sing N N 289 
LYS   CB  HB2  sing N N 290 
LYS   CB  HB3  sing N N 291 
LYS   CG  CD   sing N N 292 
LYS   CG  HG2  sing N N 293 
LYS   CG  HG3  sing N N 294 
LYS   CD  CE   sing N N 295 
LYS   CD  HD2  sing N N 296 
LYS   CD  HD3  sing N N 297 
LYS   CE  NZ   sing N N 298 
LYS   CE  HE2  sing N N 299 
LYS   CE  HE3  sing N N 300 
LYS   NZ  HZ1  sing N N 301 
LYS   NZ  HZ2  sing N N 302 
LYS   NZ  HZ3  sing N N 303 
LYS   OXT HXT  sing N N 304 
MET   N   CA   sing N N 305 
MET   N   H    sing N N 306 
MET   N   H2   sing N N 307 
MET   CA  C    sing N N 308 
MET   CA  CB   sing N N 309 
MET   CA  HA   sing N N 310 
MET   C   O    doub N N 311 
MET   C   OXT  sing N N 312 
MET   CB  CG   sing N N 313 
MET   CB  HB2  sing N N 314 
MET   CB  HB3  sing N N 315 
MET   CG  SD   sing N N 316 
MET   CG  HG2  sing N N 317 
MET   CG  HG3  sing N N 318 
MET   SD  CE   sing N N 319 
MET   CE  HE1  sing N N 320 
MET   CE  HE2  sing N N 321 
MET   CE  HE3  sing N N 322 
MET   OXT HXT  sing N N 323 
PHE   N   CA   sing N N 324 
PHE   N   H    sing N N 325 
PHE   N   H2   sing N N 326 
PHE   CA  C    sing N N 327 
PHE   CA  CB   sing N N 328 
PHE   CA  HA   sing N N 329 
PHE   C   O    doub N N 330 
PHE   C   OXT  sing N N 331 
PHE   CB  CG   sing N N 332 
PHE   CB  HB2  sing N N 333 
PHE   CB  HB3  sing N N 334 
PHE   CG  CD1  doub Y N 335 
PHE   CG  CD2  sing Y N 336 
PHE   CD1 CE1  sing Y N 337 
PHE   CD1 HD1  sing N N 338 
PHE   CD2 CE2  doub Y N 339 
PHE   CD2 HD2  sing N N 340 
PHE   CE1 CZ   doub Y N 341 
PHE   CE1 HE1  sing N N 342 
PHE   CE2 CZ   sing Y N 343 
PHE   CE2 HE2  sing N N 344 
PHE   CZ  HZ   sing N N 345 
PHE   OXT HXT  sing N N 346 
PRO   N   CA   sing N N 347 
PRO   N   CD   sing N N 348 
PRO   N   H    sing N N 349 
PRO   CA  C    sing N N 350 
PRO   CA  CB   sing N N 351 
PRO   CA  HA   sing N N 352 
PRO   C   O    doub N N 353 
PRO   C   OXT  sing N N 354 
PRO   CB  CG   sing N N 355 
PRO   CB  HB2  sing N N 356 
PRO   CB  HB3  sing N N 357 
PRO   CG  CD   sing N N 358 
PRO   CG  HG2  sing N N 359 
PRO   CG  HG3  sing N N 360 
PRO   CD  HD2  sing N N 361 
PRO   CD  HD3  sing N N 362 
PRO   OXT HXT  sing N N 363 
SER   N   CA   sing N N 364 
SER   N   H    sing N N 365 
SER   N   H2   sing N N 366 
SER   CA  C    sing N N 367 
SER   CA  CB   sing N N 368 
SER   CA  HA   sing N N 369 
SER   C   O    doub N N 370 
SER   C   OXT  sing N N 371 
SER   CB  OG   sing N N 372 
SER   CB  HB2  sing N N 373 
SER   CB  HB3  sing N N 374 
SER   OG  HG   sing N N 375 
SER   OXT HXT  sing N N 376 
THR   N   CA   sing N N 377 
THR   N   H    sing N N 378 
THR   N   H2   sing N N 379 
THR   CA  C    sing N N 380 
THR   CA  CB   sing N N 381 
THR   CA  HA   sing N N 382 
THR   C   O    doub N N 383 
THR   C   OXT  sing N N 384 
THR   CB  OG1  sing N N 385 
THR   CB  CG2  sing N N 386 
THR   CB  HB   sing N N 387 
THR   OG1 HG1  sing N N 388 
THR   CG2 HG21 sing N N 389 
THR   CG2 HG22 sing N N 390 
THR   CG2 HG23 sing N N 391 
THR   OXT HXT  sing N N 392 
TRP   N   CA   sing N N 393 
TRP   N   H    sing N N 394 
TRP   N   H2   sing N N 395 
TRP   CA  C    sing N N 396 
TRP   CA  CB   sing N N 397 
TRP   CA  HA   sing N N 398 
TRP   C   O    doub N N 399 
TRP   C   OXT  sing N N 400 
TRP   CB  CG   sing N N 401 
TRP   CB  HB2  sing N N 402 
TRP   CB  HB3  sing N N 403 
TRP   CG  CD1  doub Y N 404 
TRP   CG  CD2  sing Y N 405 
TRP   CD1 NE1  sing Y N 406 
TRP   CD1 HD1  sing N N 407 
TRP   CD2 CE2  doub Y N 408 
TRP   CD2 CE3  sing Y N 409 
TRP   NE1 CE2  sing Y N 410 
TRP   NE1 HE1  sing N N 411 
TRP   CE2 CZ2  sing Y N 412 
TRP   CE3 CZ3  doub Y N 413 
TRP   CE3 HE3  sing N N 414 
TRP   CZ2 CH2  doub Y N 415 
TRP   CZ2 HZ2  sing N N 416 
TRP   CZ3 CH2  sing Y N 417 
TRP   CZ3 HZ3  sing N N 418 
TRP   CH2 HH2  sing N N 419 
TRP   OXT HXT  sing N N 420 
TYR   N   CA   sing N N 421 
TYR   N   H    sing N N 422 
TYR   N   H2   sing N N 423 
TYR   CA  C    sing N N 424 
TYR   CA  CB   sing N N 425 
TYR   CA  HA   sing N N 426 
TYR   C   O    doub N N 427 
TYR   C   OXT  sing N N 428 
TYR   CB  CG   sing N N 429 
TYR   CB  HB2  sing N N 430 
TYR   CB  HB3  sing N N 431 
TYR   CG  CD1  doub Y N 432 
TYR   CG  CD2  sing Y N 433 
TYR   CD1 CE1  sing Y N 434 
TYR   CD1 HD1  sing N N 435 
TYR   CD2 CE2  doub Y N 436 
TYR   CD2 HD2  sing N N 437 
TYR   CE1 CZ   doub Y N 438 
TYR   CE1 HE1  sing N N 439 
TYR   CE2 CZ   sing Y N 440 
TYR   CE2 HE2  sing N N 441 
TYR   CZ  OH   sing N N 442 
TYR   OH  HH   sing N N 443 
TYR   OXT HXT  sing N N 444 
VAL   N   CA   sing N N 445 
VAL   N   H    sing N N 446 
VAL   N   H2   sing N N 447 
VAL   CA  C    sing N N 448 
VAL   CA  CB   sing N N 449 
VAL   CA  HA   sing N N 450 
VAL   C   O    doub N N 451 
VAL   C   OXT  sing N N 452 
VAL   CB  CG1  sing N N 453 
VAL   CB  CG2  sing N N 454 
VAL   CB  HB   sing N N 455 
VAL   CG1 HG11 sing N N 456 
VAL   CG1 HG12 sing N N 457 
VAL   CG1 HG13 sing N N 458 
VAL   CG2 HG21 sing N N 459 
VAL   CG2 HG22 sing N N 460 
VAL   CG2 HG23 sing N N 461 
VAL   OXT HXT  sing N N 462 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' 'R01 CA166711' 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' 'R01 CA250469' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5J9F 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NX6 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013337 
_atom_sites.fract_transf_matrix[1][2]   0.007700 
_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]   0.015401 
_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]   0.010027 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
F 
H 
N 
O 
P 
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    . ALA   A 1 2   ? -40.178 23.080 13.122 1.00 29.21  ? 808  ALA   A N    1 
ATOM   2    C CA   . ALA   A 1 2   ? -39.422 21.928 13.595 1.00 33.51  ? 808  ALA   A CA   1 
ATOM   3    C C    . ALA   A 1 2   ? -40.192 21.247 14.701 1.00 33.29  ? 808  ALA   A C    1 
ATOM   4    O O    . ALA   A 1 2   ? -40.609 21.895 15.669 1.00 36.80  ? 808  ALA   A O    1 
ATOM   5    C CB   . ALA   A 1 2   ? -38.046 22.342 14.088 1.00 32.22  ? 808  ALA   A CB   1 
ATOM   6    N N    . ARG   A 1 3   ? -40.381 19.945 14.549 1.00 31.14  ? 809  ARG   A N    1 
ATOM   7    C CA   . ARG   A 1 3   ? -41.114 19.145 15.514 1.00 34.97  ? 809  ARG   A CA   1 
ATOM   8    C C    . ARG   A 1 3   ? -40.169 18.665 16.616 1.00 34.87  ? 809  ARG   A C    1 
ATOM   9    O O    . ARG   A 1 3   ? -39.113 18.088 16.339 1.00 33.76  ? 809  ARG   A O    1 
ATOM   10   C CB   . ARG   A 1 3   ? -41.795 17.981 14.796 1.00 35.01  ? 809  ARG   A CB   1 
ATOM   11   C CG   . ARG   A 1 3   ? -42.679 18.467 13.647 1.00 36.08  ? 809  ARG   A CG   1 
ATOM   12   C CD   . ARG   A 1 3   ? -43.325 17.325 12.917 1.00 35.04  ? 809  ARG   A CD   1 
ATOM   13   N NE   . ARG   A 1 3   ? -44.059 16.455 13.839 1.00 39.89  ? 809  ARG   A NE   1 
ATOM   14   C CZ   . ARG   A 1 3   ? -45.264 16.738 14.329 1.00 38.46  ? 809  ARG   A CZ   1 
ATOM   15   N NH1  . ARG   A 1 3   ? -45.869 17.872 13.986 1.00 37.35  ? 809  ARG   A NH1  1 
ATOM   16   N NH2  . ARG   A 1 3   ? -45.864 15.894 15.157 1.00 34.91  ? 809  ARG   A NH2  1 
ATOM   17   N N    . VAL   A 1 4   ? -40.546 18.908 17.867 1.00 32.49  ? 810  VAL   A N    1 
ATOM   18   C CA   . VAL   A 1 4   ? -39.619 18.784 18.983 1.00 36.75  ? 810  VAL   A CA   1 
ATOM   19   C C    . VAL   A 1 4   ? -40.152 17.820 20.041 1.00 33.40  ? 810  VAL   A C    1 
ATOM   20   O O    . VAL   A 1 4   ? -41.342 17.825 20.376 1.00 29.22  ? 810  VAL   A O    1 
ATOM   21   C CB   . VAL   A 1 4   ? -39.324 20.165 19.597 1.00 34.25  ? 810  VAL   A CB   1 
ATOM   22   C CG1  . VAL   A 1 4   ? -38.634 19.995 20.958 1.00 28.18  ? 810  VAL   A CG1  1 
ATOM   23   C CG2  . VAL   A 1 4   ? -38.503 21.014 18.603 1.00 26.63  ? 810  VAL   A CG2  1 
ATOM   24   N N    . ALA   A 1 5   ? -39.261 16.976 20.547 1.00 32.05  ? 811  ALA   A N    1 
ATOM   25   C CA   . ALA   A 1 5   ? -39.537 16.129 21.698 1.00 35.26  ? 811  ALA   A CA   1 
ATOM   26   C C    . ALA   A 1 5   ? -38.703 16.612 22.881 1.00 32.40  ? 811  ALA   A C    1 
ATOM   27   O O    . ALA   A 1 5   ? -37.526 16.971 22.728 1.00 30.30  ? 811  ALA   A O    1 
ATOM   28   C CB   . ALA   A 1 5   ? -39.232 14.654 21.409 1.00 28.21  ? 811  ALA   A CB   1 
ATOM   29   N N    . VAL   A 1 6   ? -39.316 16.638 24.058 1.00 29.19  ? 812  VAL   A N    1 
ATOM   30   C CA   . VAL   A 1 6   ? -38.612 16.978 25.285 1.00 33.93  ? 812  VAL   A CA   1 
ATOM   31   C C    . VAL   A 1 6   ? -38.582 15.733 26.162 1.00 32.98  ? 812  VAL   A C    1 
ATOM   32   O O    . VAL   A 1 6   ? -39.636 15.179 26.496 1.00 36.55  ? 812  VAL   A O    1 
ATOM   33   C CB   . VAL   A 1 6   ? -39.274 18.166 25.994 1.00 32.30  ? 812  VAL   A CB   1 
ATOM   34   C CG1  . VAL   A 1 6   ? -38.469 18.567 27.216 1.00 27.45  ? 812  VAL   A CG1  1 
ATOM   35   C CG2  . VAL   A 1 6   ? -39.392 19.312 25.020 1.00 26.18  ? 812  VAL   A CG2  1 
ATOM   36   N N    . LEU   A 1 7   ? -37.384 15.275 26.517 1.00 30.01  ? 813  LEU   A N    1 
ATOM   37   C CA   . LEU   A 1 7   ? -37.233 14.164 27.452 1.00 34.36  ? 813  LEU   A CA   1 
ATOM   38   C C    . LEU   A 1 7   ? -36.982 14.730 28.838 1.00 33.71  ? 813  LEU   A C    1 
ATOM   39   O O    . LEU   A 1 7   ? -36.121 15.602 29.012 1.00 33.77  ? 813  LEU   A O    1 
ATOM   40   C CB   . LEU   A 1 7   ? -36.091 13.230 27.042 1.00 32.59  ? 813  LEU   A CB   1 
ATOM   41   C CG   . LEU   A 1 7   ? -36.453 12.256 25.922 1.00 35.86  ? 813  LEU   A CG   1 
ATOM   42   C CD1  . LEU   A 1 7   ? -37.169 12.985 24.776 1.00 33.95  ? 813  LEU   A CD1  1 
ATOM   43   C CD2  . LEU   A 1 7   ? -35.223 11.522 25.416 1.00 33.21  ? 813  LEU   A CD2  1 
ATOM   44   N N    . ILE   A 1 8   ? -37.753 14.259 29.817 1.00 37.37  ? 814  ILE   A N    1 
ATOM   45   C CA   . ILE   A 1 8   ? -37.646 14.751 31.183 1.00 38.70  ? 814  ILE   A CA   1 
ATOM   46   C C    . ILE   A 1 8   ? -37.505 13.587 32.142 1.00 40.21  ? 814  ILE   A C    1 
ATOM   47   O O    . ILE   A 1 8   ? -37.880 12.446 31.847 1.00 38.60  ? 814  ILE   A O    1 
ATOM   48   C CB   . ILE   A 1 8   ? -38.856 15.595 31.614 1.00 37.05  ? 814  ILE   A CB   1 
ATOM   49   C CG1  . ILE   A 1 8   ? -40.092 14.696 31.680 1.00 38.31  ? 814  ILE   A CG1  1 
ATOM   50   C CG2  . ILE   A 1 8   ? -39.003 16.803 30.703 1.00 33.14  ? 814  ILE   A CG2  1 
ATOM   51   C CD1  . ILE   A 1 8   ? -41.267 15.314 32.360 1.00 39.53  ? 814  ILE   A CD1  1 
ATOM   52   N N    . SER   A 1 9   ? -36.995 13.914 33.335 1.00 41.36  ? 815  SER   A N    1 
ATOM   53   C CA   . SER   A 1 9   ? -37.006 12.981 34.442 1.00 38.30  ? 815  SER   A CA   1 
ATOM   54   C C    . SER   A 1 9   ? -37.659 13.517 35.704 1.00 41.63  ? 815  SER   A C    1 
ATOM   55   O O    . SER   A 1 9   ? -37.929 12.723 36.614 1.00 45.52  ? 815  SER   A O    1 
ATOM   56   C CB   . SER   A 1 9   ? -35.582 12.523 34.756 1.00 40.77  ? 815  SER   A CB   1 
ATOM   57   O OG   . SER   A 1 9   ? -35.130 11.693 33.700 1.00 44.93  ? 815  SER   A OG   1 
ATOM   58   N N    . GLY   A 1 10  ? -37.954 14.811 35.784 1.00 40.91  ? 816  GLY   A N    1 
ATOM   59   C CA   . GLY   A 1 10  ? -38.409 15.365 37.043 1.00 38.72  ? 816  GLY   A CA   1 
ATOM   60   C C    . GLY   A 1 10  ? -39.345 16.550 36.953 1.00 40.46  ? 816  GLY   A C    1 
ATOM   61   O O    . GLY   A 1 10  ? -40.343 16.509 36.226 1.00 40.02  ? 816  GLY   A O    1 
ATOM   62   N N    . THR   A 1 11  ? -39.008 17.612 37.699 1.00 38.75  ? 817  THR   A N    1 
ATOM   63   C CA   . THR   A 1 11  ? -39.902 18.751 37.915 1.00 40.28  ? 817  THR   A CA   1 
ATOM   64   C C    . THR   A 1 11  ? -40.343 19.409 36.609 1.00 40.86  ? 817  THR   A C    1 
ATOM   65   O O    . THR   A 1 11  ? -41.471 19.915 36.519 1.00 39.45  ? 817  THR   A O    1 
ATOM   66   C CB   . THR   A 1 11  ? -39.203 19.788 38.802 1.00 39.38  ? 817  THR   A CB   1 
ATOM   67   O OG1  . THR   A 1 11  ? -38.891 19.201 40.073 1.00 42.83  ? 817  THR   A OG1  1 
ATOM   68   C CG2  . THR   A 1 11  ? -40.095 20.996 39.008 1.00 34.54  ? 817  THR   A CG2  1 
ATOM   69   N N    . GLY   A 1 12  ? -39.463 19.455 35.610 1.00 35.88  ? 818  GLY   A N    1 
ATOM   70   C CA   . GLY   A 1 12  ? -39.857 19.967 34.317 1.00 36.27  ? 818  GLY   A CA   1 
ATOM   71   C C    . GLY   A 1 12  ? -39.924 21.475 34.194 1.00 37.66  ? 818  GLY   A C    1 
ATOM   72   O O    . GLY   A 1 12  ? -40.708 21.985 33.387 1.00 39.01  ? 818  GLY   A O    1 
ATOM   73   N N    . SER   A 1 13  ? -39.121 22.216 34.961 1.00 32.73  ? 819  SER   A N    1 
ATOM   74   C CA   . SER   A 1 13  ? -39.155 23.665 34.828 1.00 30.83  ? 819  SER   A CA   1 
ATOM   75   C C    . SER   A 1 13  ? -38.488 24.127 33.535 1.00 34.78  ? 819  SER   A C    1 
ATOM   76   O O    . SER   A 1 13  ? -38.890 25.153 32.967 1.00 34.56  ? 819  SER   A O    1 
ATOM   77   C CB   . SER   A 1 13  ? -38.519 24.322 36.054 1.00 31.13  ? 819  SER   A CB   1 
ATOM   78   O OG   . SER   A 1 13  ? -37.111 24.281 36.033 1.00 31.61  ? 819  SER   A OG   1 
ATOM   79   N N    . ASN   A 1 14  ? -37.487 23.392 33.040 1.00 31.52  ? 820  ASN   A N    1 
ATOM   80   C CA   . ASN   A 1 14  ? -36.981 23.699 31.706 1.00 32.92  ? 820  ASN   A CA   1 
ATOM   81   C C    . ASN   A 1 14  ? -38.026 23.373 30.652 1.00 32.04  ? 820  ASN   A C    1 
ATOM   82   O O    . ASN   A 1 14  ? -38.267 24.173 29.740 1.00 27.29  ? 820  ASN   A O    1 
ATOM   83   C CB   . ASN   A 1 14  ? -35.679 22.948 31.433 1.00 29.61  ? 820  ASN   A CB   1 
ATOM   84   C CG   . ASN   A 1 14  ? -34.495 23.623 32.058 1.00 30.75  ? 820  ASN   A CG   1 
ATOM   85   O OD1  . ASN   A 1 14  ? -34.057 24.670 31.601 1.00 30.28  ? 820  ASN   A OD1  1 
ATOM   86   N ND2  . ASN   A 1 14  ? -33.978 23.040 33.119 1.00 31.99  ? 820  ASN   A ND2  1 
ATOM   87   N N    . LEU   A 1 15  ? -38.687 22.218 30.790 1.00 37.12  ? 821  LEU   A N    1 
ATOM   88   C CA   . LEU   A 1 15  ? -39.824 21.904 29.935 1.00 31.34  ? 821  LEU   A CA   1 
ATOM   89   C C    . LEU   A 1 15  ? -40.800 23.070 29.889 1.00 34.32  ? 821  LEU   A C    1 
ATOM   90   O O    . LEU   A 1 15  ? -41.219 23.503 28.809 1.00 35.50  ? 821  LEU   A O    1 
ATOM   91   C CB   . LEU   A 1 15  ? -40.525 20.646 30.427 1.00 32.52  ? 821  LEU   A CB   1 
ATOM   92   C CG   . LEU   A 1 15  ? -41.810 20.362 29.636 1.00 37.31  ? 821  LEU   A CG   1 
ATOM   93   C CD1  . LEU   A 1 15  ? -41.470 20.204 28.160 1.00 33.25  ? 821  LEU   A CD1  1 
ATOM   94   C CD2  . LEU   A 1 15  ? -42.541 19.136 30.162 1.00 34.83  ? 821  LEU   A CD2  1 
ATOM   95   N N    . GLN   A 1 16  ? -41.159 23.601 31.063 1.00 33.04  ? 822  GLN   A N    1 
ATOM   96   C CA   . GLN   A 1 16  ? -42.090 24.727 31.137 1.00 34.51  ? 822  GLN   A CA   1 
ATOM   97   C C    . GLN   A 1 16  ? -41.548 25.944 30.388 1.00 36.44  ? 822  GLN   A C    1 
ATOM   98   O O    . GLN   A 1 16  ? -42.269 26.582 29.609 1.00 34.20  ? 822  GLN   A O    1 
ATOM   99   C CB   . GLN   A 1 16  ? -42.366 25.072 32.605 1.00 34.80  ? 822  GLN   A CB   1 
ATOM   100  C CG   . GLN   A 1 16  ? -43.545 26.025 32.857 1.00 32.79  ? 822  GLN   A CG   1 
ATOM   101  C CD   . GLN   A 1 16  ? -44.764 25.728 31.986 1.00 39.07  ? 822  GLN   A CD   1 
ATOM   102  O OE1  . GLN   A 1 16  ? -45.167 26.559 31.163 1.00 40.56  ? 822  GLN   A OE1  1 
ATOM   103  N NE2  . GLN   A 1 16  ? -45.351 24.545 32.155 1.00 37.21  ? 822  GLN   A NE2  1 
ATOM   104  N N    . ALA   A 1 17  ? -40.275 26.286 30.622 1.00 34.93  ? 823  ALA   A N    1 
ATOM   105  C CA   . ALA   A 1 17  ? -39.659 27.402 29.910 1.00 34.46  ? 823  ALA   A CA   1 
ATOM   106  C C    . ALA   A 1 17  ? -39.683 27.179 28.397 1.00 35.77  ? 823  ALA   A C    1 
ATOM   107  O O    . ALA   A 1 17  ? -39.896 28.124 27.630 1.00 33.86  ? 823  ALA   A O    1 
ATOM   108  C CB   . ALA   A 1 17  ? -38.223 27.612 30.404 1.00 31.81  ? 823  ALA   A CB   1 
ATOM   109  N N    . LEU   A 1 18  ? -39.461 25.934 27.953 1.00 35.36  ? 824  LEU   A N    1 
ATOM   110  C CA   . LEU   A 1 18  ? -39.512 25.617 26.524 1.00 33.50  ? 824  LEU   A CA   1 
ATOM   111  C C    . LEU   A 1 18  ? -40.929 25.737 25.984 1.00 33.76  ? 824  LEU   A C    1 
ATOM   112  O O    . LEU   A 1 18  ? -41.147 26.310 24.912 1.00 34.14  ? 824  LEU   A O    1 
ATOM   113  C CB   . LEU   A 1 18  ? -38.960 24.210 26.268 1.00 29.55  ? 824  LEU   A CB   1 
ATOM   114  C CG   . LEU   A 1 18  ? -37.449 24.108 26.478 1.00 31.45  ? 824  LEU   A CG   1 
ATOM   115  C CD1  . LEU   A 1 18  ? -36.991 22.650 26.486 1.00 28.48  ? 824  LEU   A CD1  1 
ATOM   116  C CD2  . LEU   A 1 18  ? -36.699 24.954 25.431 1.00 27.09  ? 824  LEU   A CD2  1 
ATOM   117  N N    . ILE   A 1 19  ? -41.906 25.179 26.700 1.00 31.74  ? 825  ILE   A N    1 
ATOM   118  C CA   . ILE   A 1 19  ? -43.298 25.345 26.299 1.00 33.08  ? 825  ILE   A CA   1 
ATOM   119  C C    . ILE   A 1 19  ? -43.609 26.822 26.130 1.00 37.98  ? 825  ILE   A C    1 
ATOM   120  O O    . ILE   A 1 19  ? -44.231 27.248 25.149 1.00 41.74  ? 825  ILE   A O    1 
ATOM   121  C CB   . ILE   A 1 19  ? -44.239 24.706 27.336 1.00 37.92  ? 825  ILE   A CB   1 
ATOM   122  C CG1  . ILE   A 1 19  ? -44.049 23.190 27.391 1.00 36.86  ? 825  ILE   A CG1  1 
ATOM   123  C CG2  . ILE   A 1 19  ? -45.703 25.124 27.089 1.00 36.07  ? 825  ILE   A CG2  1 
ATOM   124  C CD1  . ILE   A 1 19  ? -44.474 22.592 28.703 1.00 36.33  ? 825  ILE   A CD1  1 
ATOM   125  N N    . ASP   A 1 20  ? -43.180 27.629 27.095 1.00 35.61  ? 826  ASP   A N    1 
ATOM   126  C CA   . ASP   A 1 20  ? -43.572 29.029 27.082 1.00 37.59  ? 826  ASP   A CA   1 
ATOM   127  C C    . ASP   A 1 20  ? -43.032 29.734 25.847 1.00 37.80  ? 826  ASP   A C    1 
ATOM   128  O O    . ASP   A 1 20  ? -43.750 30.509 25.207 1.00 37.96  ? 826  ASP   A O    1 
ATOM   129  C CB   . ASP   A 1 20  ? -43.096 29.723 28.358 1.00 37.98  ? 826  ASP   A CB   1 
ATOM   130  C CG   . ASP   A 1 20  ? -43.959 29.386 29.578 1.00 41.05  ? 826  ASP   A CG   1 
ATOM   131  O OD1  . ASP   A 1 20  ? -45.003 28.700 29.444 1.00 41.88  ? 826  ASP   A OD1  1 
ATOM   132  O OD2  . ASP   A 1 20  ? -43.575 29.814 30.684 1.00 39.49  ? 826  ASP   A OD2  1 
ATOM   133  N N    . SER   A 1 21  ? -41.774 29.469 25.484 1.00 35.48  ? 827  SER   A N    1 
ATOM   134  C CA   . SER   A 1 21  ? -41.211 30.131 24.314 1.00 38.10  ? 827  SER   A CA   1 
ATOM   135  C C    . SER   A 1 21  ? -41.816 29.597 23.021 1.00 37.62  ? 827  SER   A C    1 
ATOM   136  O O    . SER   A 1 21  ? -42.022 30.363 22.077 1.00 38.34  ? 827  SER   A O    1 
ATOM   137  C CB   . SER   A 1 21  ? -39.692 29.984 24.287 1.00 31.11  ? 827  SER   A CB   1 
ATOM   138  O OG   . SER   A 1 21  ? -39.359 28.624 24.230 1.00 31.21  ? 827  SER   A OG   1 
ATOM   139  N N    . THR   A 1 22  ? -42.111 28.299 22.950 1.00 37.31  ? 828  THR   A N    1 
ATOM   140  C CA   . THR   A 1 22  ? -42.552 27.740 21.674 1.00 37.63  ? 828  THR   A CA   1 
ATOM   141  C C    . THR   A 1 22  ? -44.004 28.056 21.359 1.00 42.47  ? 828  THR   A C    1 
ATOM   142  O O    . THR   A 1 22  ? -44.473 27.744 20.254 1.00 42.52  ? 828  THR   A O    1 
ATOM   143  C CB   . THR   A 1 22  ? -42.370 26.219 21.619 1.00 32.26  ? 828  THR   A CB   1 
ATOM   144  O OG1  . THR   A 1 22  ? -43.247 25.607 22.561 1.00 37.35  ? 828  THR   A OG1  1 
ATOM   145  C CG2  . THR   A 1 22  ? -40.936 25.801 21.870 1.00 28.33  ? 828  THR   A CG2  1 
ATOM   146  N N    . ARG   A 1 23  ? -44.736 28.638 22.293 1.00 47.54  ? 829  ARG   A N    1 
ATOM   147  C CA   . ARG   A 1 23  ? -46.065 29.113 21.968 1.00 51.08  ? 829  ARG   A CA   1 
ATOM   148  C C    . ARG   A 1 23  ? -46.063 30.569 21.545 1.00 52.00  ? 829  ARG   A C    1 
ATOM   149  O O    . ARG   A 1 23  ? -47.105 31.074 21.117 1.00 53.79  ? 829  ARG   A O    1 
ATOM   150  C CB   . ARG   A 1 23  ? -47.011 28.902 23.152 1.00 57.10  ? 829  ARG   A CB   1 
ATOM   151  C CG   . ARG   A 1 23  ? -47.303 27.432 23.442 1.00 59.85  ? 829  ARG   A CG   1 
ATOM   152  C CD   . ARG   A 1 23  ? -48.264 27.329 24.610 1.00 66.76  ? 829  ARG   A CD   1 
ATOM   153  N NE   . ARG   A 1 23  ? -47.859 28.262 25.658 1.00 70.78  ? 829  ARG   A NE   1 
ATOM   154  C CZ   . ARG   A 1 23  ? -48.104 28.100 26.959 1.00 71.20  ? 829  ARG   A CZ   1 
ATOM   155  N NH1  . ARG   A 1 23  ? -48.782 27.037 27.385 1.00 67.15  ? 829  ARG   A NH1  1 
ATOM   156  N NH2  . ARG   A 1 23  ? -47.673 29.010 27.834 1.00 62.87  ? 829  ARG   A NH2  1 
ATOM   157  N N    . GLU   A 1 24  ? -44.922 31.243 21.644 1.00 41.98  ? 830  GLU   A N    1 
ATOM   158  C CA   . GLU   A 1 24  ? -44.794 32.565 21.062 1.00 40.95  ? 830  GLU   A CA   1 
ATOM   159  C C    . GLU   A 1 24  ? -44.929 32.455 19.545 1.00 40.44  ? 830  GLU   A C    1 
ATOM   160  O O    . GLU   A 1 24  ? -44.418 31.509 18.940 1.00 38.88  ? 830  GLU   A O    1 
ATOM   161  C CB   . GLU   A 1 24  ? -43.457 33.201 21.435 1.00 41.41  ? 830  GLU   A CB   1 
ATOM   162  C CG   . GLU   A 1 24  ? -43.348 33.512 22.924 1.00 51.74  ? 830  GLU   A CG   1 
ATOM   163  C CD   . GLU   A 1 24  ? -44.077 34.800 23.361 1.00 63.99  ? 830  GLU   A CD   1 
ATOM   164  O OE1  . GLU   A 1 24  ? -43.379 35.809 23.636 1.00 70.10  ? 830  GLU   A OE1  1 
ATOM   165  O OE2  . GLU   A 1 24  ? -45.338 34.808 23.430 1.00 63.55  ? 830  GLU   A OE2  1 
ATOM   166  N N    . PRO   A 1 25  ? -45.621 33.392 18.913 1.00 39.20  ? 831  PRO   A N    1 
ATOM   167  C CA   . PRO   A 1 25  ? -45.939 33.220 17.485 1.00 40.33  ? 831  PRO   A CA   1 
ATOM   168  C C    . PRO   A 1 25  ? -44.714 33.075 16.595 1.00 37.29  ? 831  PRO   A C    1 
ATOM   169  O O    . PRO   A 1 25  ? -44.771 32.349 15.590 1.00 37.19  ? 831  PRO   A O    1 
ATOM   170  C CB   . PRO   A 1 25  ? -46.740 34.486 17.155 1.00 35.99  ? 831  PRO   A CB   1 
ATOM   171  C CG   . PRO   A 1 25  ? -47.177 35.029 18.528 1.00 34.97  ? 831  PRO   A CG   1 
ATOM   172  C CD   . PRO   A 1 25  ? -46.100 34.667 19.457 1.00 38.56  ? 831  PRO   A CD   1 
ATOM   173  N N    . ASN   A 1 26  ? -43.607 33.724 16.931 1.00 37.09  ? 832  ASN   A N    1 
ATOM   174  C CA   . ASN   A 1 26  ? -42.406 33.630 16.113 1.00 37.99  ? 832  ASN   A CA   1 
ATOM   175  C C    . ASN   A 1 26  ? -41.623 32.346 16.358 1.00 37.05  ? 832  ASN   A C    1 
ATOM   176  O O    . ASN   A 1 26  ? -40.627 32.111 15.669 1.00 38.66  ? 832  ASN   A O    1 
ATOM   177  C CB   . ASN   A 1 26  ? -41.512 34.849 16.355 1.00 35.97  ? 832  ASN   A CB   1 
ATOM   178  C CG   . ASN   A 1 26  ? -41.918 36.034 15.513 1.00 40.56  ? 832  ASN   A CG   1 
ATOM   179  O OD1  . ASN   A 1 26  ? -42.654 35.883 14.546 1.00 47.29  ? 832  ASN   A OD1  1 
ATOM   180  N ND2  . ASN   A 1 26  ? -41.453 37.225 15.878 1.00 44.68  ? 832  ASN   A ND2  1 
ATOM   181  N N    . SER   A 1 27  ? -42.051 31.507 17.296 1.00 35.07  ? 833  SER   A N    1 
ATOM   182  C CA   . SER   A 1 27  ? -41.331 30.274 17.577 1.00 32.77  ? 833  SER   A CA   1 
ATOM   183  C C    . SER   A 1 27  ? -41.203 29.415 16.325 1.00 35.41  ? 833  SER   A C    1 
ATOM   184  O O    . SER   A 1 27  ? -42.178 29.199 15.596 1.00 34.78  ? 833  SER   A O    1 
ATOM   185  C CB   . SER   A 1 27  ? -42.041 29.490 18.674 1.00 32.24  ? 833  SER   A CB   1 
ATOM   186  O OG   . SER   A 1 27  ? -41.448 28.209 18.833 1.00 33.24  ? 833  SER   A OG   1 
ATOM   187  N N    . SER   A 1 28  ? -39.997 28.909 16.087 1.00 34.27  ? 834  SER   A N    1 
ATOM   188  C CA   . SER   A 1 28  ? -39.748 27.965 15.011 1.00 34.74  ? 834  SER   A CA   1 
ATOM   189  C C    . SER   A 1 28  ? -39.805 26.527 15.490 1.00 33.63  ? 834  SER   A C    1 
ATOM   190  O O    . SER   A 1 28  ? -39.525 25.602 14.711 1.00 35.75  ? 834  SER   A O    1 
ATOM   191  C CB   . SER   A 1 28  ? -38.395 28.258 14.356 1.00 40.08  ? 834  SER   A CB   1 
ATOM   192  O OG   . SER   A 1 28  ? -38.448 29.466 13.601 1.00 35.75  ? 834  SER   A OG   1 
ATOM   193  N N    . ALA   A 1 29  ? -40.188 26.321 16.738 1.00 31.63  ? 835  ALA   A N    1 
ATOM   194  C CA   . ALA   A 1 29  ? -40.264 25.002 17.340 1.00 33.23  ? 835  ALA   A CA   1 
ATOM   195  C C    . ALA   A 1 29  ? -41.680 24.752 17.823 1.00 37.32  ? 835  ALA   A C    1 
ATOM   196  O O    . ALA   A 1 29  ? -42.372 25.673 18.276 1.00 35.37  ? 835  ALA   A O    1 
ATOM   197  C CB   . ALA   A 1 29  ? -39.294 24.871 18.512 1.00 34.08  ? 835  ALA   A CB   1 
ATOM   198  N N    . GLN   A 1 30  ? -42.111 23.507 17.701 1.00 36.04  ? 836  GLN   A N    1 
ATOM   199  C CA   . GLN   A 1 30  ? -43.366 23.066 18.280 1.00 34.52  ? 836  GLN   A CA   1 
ATOM   200  C C    . GLN   A 1 30  ? -43.078 21.810 19.092 1.00 36.74  ? 836  GLN   A C    1 
ATOM   201  O O    . GLN   A 1 30  ? -42.396 20.893 18.610 1.00 35.17  ? 836  GLN   A O    1 
ATOM   202  C CB   . GLN   A 1 30  ? -44.409 22.812 17.182 1.00 33.03  ? 836  GLN   A CB   1 
ATOM   203  C CG   . GLN   A 1 30  ? -44.109 21.616 16.316 1.00 32.60  ? 836  GLN   A CG   1 
ATOM   204  C CD   . GLN   A 1 30  ? -45.220 21.323 15.359 1.00 34.63  ? 836  GLN   A CD   1 
ATOM   205  O OE1  . GLN   A 1 30  ? -45.088 21.554 14.156 1.00 37.84  ? 836  GLN   A OE1  1 
ATOM   206  N NE2  . GLN   A 1 30  ? -46.335 20.824 15.874 1.00 30.83  ? 836  GLN   A NE2  1 
ATOM   207  N N    . ILE   A 1 31  ? -43.550 21.782 20.331 1.00 30.76  ? 837  ILE   A N    1 
ATOM   208  C CA   . ILE   A 1 31  ? -43.333 20.636 21.196 1.00 32.76  ? 837  ILE   A CA   1 
ATOM   209  C C    . ILE   A 1 31  ? -44.471 19.656 20.965 1.00 33.74  ? 837  ILE   A C    1 
ATOM   210  O O    . ILE   A 1 31  ? -45.604 19.914 21.371 1.00 40.37  ? 837  ILE   A O    1 
ATOM   211  C CB   . ILE   A 1 31  ? -43.256 21.048 22.667 1.00 34.35  ? 837  ILE   A CB   1 
ATOM   212  C CG1  . ILE   A 1 31  ? -41.981 21.848 22.917 1.00 31.23  ? 837  ILE   A CG1  1 
ATOM   213  C CG2  . ILE   A 1 31  ? -43.316 19.810 23.531 1.00 30.03  ? 837  ILE   A CG2  1 
ATOM   214  C CD1  . ILE   A 1 31  ? -42.010 22.676 24.151 1.00 28.92  ? 837  ILE   A CD1  1 
ATOM   215  N N    . ASP   A 1 32  ? -44.168 18.508 20.360 1.00 33.68  ? 838  ASP   A N    1 
ATOM   216  C CA   . ASP   A 1 32  ? -45.199 17.578 19.920 1.00 37.42  ? 838  ASP   A CA   1 
ATOM   217  C C    . ASP   A 1 32  ? -45.313 16.342 20.796 1.00 39.09  ? 838  ASP   A C    1 
ATOM   218  O O    . ASP   A 1 32  ? -46.266 15.558 20.635 1.00 38.19  ? 838  ASP   A O    1 
ATOM   219  C CB   . ASP   A 1 32  ? -44.941 17.172 18.461 1.00 30.27  ? 838  ASP   A CB   1 
ATOM   220  C CG   . ASP   A 1 32  ? -44.989 18.360 17.534 1.00 34.99  ? 838  ASP   A CG   1 
ATOM   221  O OD1  . ASP   A 1 32  ? -44.036 18.588 16.754 1.00 38.69  ? 838  ASP   A OD1  1 
ATOM   222  O OD2  . ASP   A 1 32  ? -45.987 19.098 17.606 1.00 34.43  ? 838  ASP   A OD2  1 
ATOM   223  N N    . ILE   A 1 33  ? -44.385 16.160 21.727 1.00 36.83  ? 839  ILE   A N    1 
ATOM   224  C CA   . ILE   A 1 33  ? -44.382 14.998 22.597 1.00 35.43  ? 839  ILE   A CA   1 
ATOM   225  C C    . ILE   A 1 33  ? -43.464 15.316 23.760 1.00 36.66  ? 839  ILE   A C    1 
ATOM   226  O O    . ILE   A 1 33  ? -42.443 15.987 23.590 1.00 32.07  ? 839  ILE   A O    1 
ATOM   227  C CB   . ILE   A 1 33  ? -43.933 13.731 21.834 1.00 33.82  ? 839  ILE   A CB   1 
ATOM   228  C CG1  . ILE   A 1 33  ? -43.898 12.522 22.771 1.00 37.42  ? 839  ILE   A CG1  1 
ATOM   229  C CG2  . ILE   A 1 33  ? -42.575 13.968 21.198 1.00 34.94  ? 839  ILE   A CG2  1 
ATOM   230  C CD1  . ILE   A 1 33  ? -45.204 12.245 23.455 1.00 36.01  ? 839  ILE   A CD1  1 
ATOM   231  N N    . VAL   A 1 34  ? -43.847 14.850 24.947 1.00 36.40  ? 840  VAL   A N    1 
ATOM   232  C CA   . VAL   A 1 34  ? -42.997 14.899 26.124 1.00 31.78  ? 840  VAL   A CA   1 
ATOM   233  C C    . VAL   A 1 34  ? -42.837 13.474 26.640 1.00 37.21  ? 840  VAL   A C    1 
ATOM   234  O O    . VAL   A 1 34  ? -43.836 12.781 26.888 1.00 40.98  ? 840  VAL   A O    1 
ATOM   235  C CB   . VAL   A 1 34  ? -43.581 15.824 27.196 1.00 37.22  ? 840  VAL   A CB   1 
ATOM   236  C CG1  . VAL   A 1 34  ? -42.917 15.553 28.560 1.00 38.50  ? 840  VAL   A CG1  1 
ATOM   237  C CG2  . VAL   A 1 34  ? -43.399 17.280 26.768 1.00 32.20  ? 840  VAL   A CG2  1 
ATOM   238  N N    . ILE   A 1 35  ? -41.588 13.030 26.791 1.00 35.46  ? 841  ILE   A N    1 
ATOM   239  C CA   . ILE   A 1 35  ? -41.263 11.650 27.160 1.00 40.04  ? 841  ILE   A CA   1 
ATOM   240  C C    . ILE   A 1 35  ? -40.477 11.657 28.470 1.00 41.61  ? 841  ILE   A C    1 
ATOM   241  O O    . ILE   A 1 35  ? -39.403 12.270 28.556 1.00 37.80  ? 841  ILE   A O    1 
ATOM   242  C CB   . ILE   A 1 35  ? -40.460 10.932 26.058 1.00 38.76  ? 841  ILE   A CB   1 
ATOM   243  C CG1  . ILE   A 1 35  ? -41.210 10.951 24.727 1.00 37.93  ? 841  ILE   A CG1  1 
ATOM   244  C CG2  . ILE   A 1 35  ? -40.165 9.496  26.452 1.00 40.73  ? 841  ILE   A CG2  1 
ATOM   245  C CD1  . ILE   A 1 35  ? -40.440 10.279 23.576 1.00 40.13  ? 841  ILE   A CD1  1 
ATOM   246  N N    . SER   A 1 36  ? -40.994 10.955 29.479 1.00 43.01  ? 842  SER   A N    1 
ATOM   247  C CA   . SER   A 1 36  ? -40.337 10.843 30.774 1.00 45.38  ? 842  SER   A CA   1 
ATOM   248  C C    . SER   A 1 36  ? -40.041 9.388  31.084 1.00 44.92  ? 842  SER   A C    1 
ATOM   249  O O    . SER   A 1 36  ? -40.858 8.507  30.804 1.00 46.44  ? 842  SER   A O    1 
ATOM   250  C CB   . SER   A 1 36  ? -41.194 11.428 31.897 1.00 48.05  ? 842  SER   A CB   1 
ATOM   251  O OG   . SER   A 1 36  ? -40.700 11.021 33.167 1.00 48.63  ? 842  SER   A OG   1 
ATOM   252  N N    . ASN   A 1 37  ? -38.881 9.138  31.686 1.00 50.27  ? 843  ASN   A N    1 
ATOM   253  C CA   . ASN   A 1 37  ? -38.545 7.773  32.064 1.00 51.31  ? 843  ASN   A CA   1 
ATOM   254  C C    . ASN   A 1 37  ? -39.013 7.426  33.461 1.00 55.18  ? 843  ASN   A C    1 
ATOM   255  O O    . ASN   A 1 37  ? -38.884 6.264  33.866 1.00 62.16  ? 843  ASN   A O    1 
ATOM   256  C CB   . ASN   A 1 37  ? -37.037 7.526  31.950 1.00 51.54  ? 843  ASN   A CB   1 
ATOM   257  C CG   . ASN   A 1 37  ? -36.231 8.276  32.992 1.00 50.87  ? 843  ASN   A CG   1 
ATOM   258  O OD1  . ASN   A 1 37  ? -36.520 9.429  33.313 1.00 47.43  ? 843  ASN   A OD1  1 
ATOM   259  N ND2  . ASN   A 1 37  ? -35.193 7.627  33.506 1.00 55.31  ? 843  ASN   A ND2  1 
ATOM   260  N N    . LYS   A 1 38  ? -39.544 8.403  34.193 1.00 52.00  ? 844  LYS   A N    1 
ATOM   261  C CA   . LYS   A 1 38  ? -40.044 8.230  35.552 1.00 55.07  ? 844  LYS   A CA   1 
ATOM   262  C C    . LYS   A 1 38  ? -41.477 8.740  35.605 1.00 51.72  ? 844  LYS   A C    1 
ATOM   263  O O    . LYS   A 1 38  ? -41.775 9.814  35.077 1.00 51.56  ? 844  LYS   A O    1 
ATOM   264  C CB   . LYS   A 1 38  ? -39.134 8.924  36.603 1.00 56.27  ? 844  LYS   A CB   1 
ATOM   265  C CG   . LYS   A 1 38  ? -37.766 8.243  36.797 1.00 60.51  ? 844  LYS   A CG   1 
ATOM   266  C CD   . LYS   A 1 38  ? -38.033 6.887  37.480 1.00 66.38  ? 844  LYS   A CD   1 
ATOM   267  C CE   . LYS   A 1 38  ? -38.284 5.784  36.435 1.00 67.91  ? 844  LYS   A CE   1 
ATOM   268  N NZ   . LYS   A 1 38  ? -38.393 4.416  37.018 1.00 72.12  ? 844  LYS   A NZ   1 
ATOM   269  N N    . ALA   A 1 39  ? -42.373 7.939  36.172 1.00 53.36  ? 845  ALA   A N    1 
ATOM   270  C CA   . ALA   A 1 39  ? -43.776 8.318  36.248 1.00 51.79  ? 845  ALA   A CA   1 
ATOM   271  C C    . ALA   A 1 39  ? -44.029 9.208  37.461 1.00 55.22  ? 845  ALA   A C    1 
ATOM   272  O O    . ALA   A 1 39  ? -43.210 9.304  38.379 1.00 55.51  ? 845  ALA   A O    1 
ATOM   273  C CB   . ALA   A 1 39  ? -44.670 7.086  36.315 1.00 45.52  ? 845  ALA   A CB   1 
ATOM   274  N N    . ALA   A 1 40  ? -45.181 9.875  37.449 1.00 53.13  ? 846  ALA   A N    1 
ATOM   275  C CA   . ALA   A 1 40  ? -45.634 10.727 38.543 1.00 49.86  ? 846  ALA   A CA   1 
ATOM   276  C C    . ALA   A 1 40  ? -44.752 11.950 38.764 1.00 50.70  ? 846  ALA   A C    1 
ATOM   277  O O    . ALA   A 1 40  ? -44.928 12.651 39.766 1.00 50.47  ? 846  ALA   A O    1 
ATOM   278  C CB   . ALA   A 1 40  ? -45.740 9.943  39.856 1.00 49.27  ? 846  ALA   A CB   1 
ATOM   279  N N    . VAL   A 1 41  ? -43.805 12.233 37.869 1.00 48.53  ? 847  VAL   A N    1 
ATOM   280  C CA   . VAL   A 1 41  ? -42.998 13.437 38.020 1.00 45.64  ? 847  VAL   A CA   1 
ATOM   281  C C    . VAL   A 1 41  ? -43.783 14.648 37.526 1.00 44.23  ? 847  VAL   A C    1 
ATOM   282  O O    . VAL   A 1 41  ? -44.688 14.544 36.694 1.00 47.37  ? 847  VAL   A O    1 
ATOM   283  C CB   . VAL   A 1 41  ? -41.649 13.302 37.296 1.00 45.64  ? 847  VAL   A CB   1 
ATOM   284  C CG1  . VAL   A 1 41  ? -40.997 11.991 37.685 1.00 50.46  ? 847  VAL   A CG1  1 
ATOM   285  C CG2  . VAL   A 1 41  ? -41.830 13.377 35.804 1.00 42.13  ? 847  VAL   A CG2  1 
ATOM   286  N N    . ALA   A 1 42  ? -43.428 15.818 38.064 1.00 41.66  ? 848  ALA   A N    1 
ATOM   287  C CA   . ALA   A 1 42  ? -44.182 17.042 37.813 1.00 40.23  ? 848  ALA   A CA   1 
ATOM   288  C C    . ALA   A 1 42  ? -44.076 17.526 36.375 1.00 44.82  ? 848  ALA   A C    1 
ATOM   289  O O    . ALA   A 1 42  ? -44.956 18.272 35.925 1.00 44.34  ? 848  ALA   A O    1 
ATOM   290  C CB   . ALA   A 1 42  ? -43.707 18.149 38.753 1.00 38.38  ? 848  ALA   A CB   1 
ATOM   291  N N    . GLY   A 1 43  ? -43.009 17.160 35.659 1.00 40.76  ? 849  GLY   A N    1 
ATOM   292  C CA   . GLY   A 1 43  ? -42.914 17.530 34.259 1.00 41.49  ? 849  GLY   A CA   1 
ATOM   293  C C    . GLY   A 1 43  ? -44.033 16.948 33.421 1.00 42.42  ? 849  GLY   A C    1 
ATOM   294  O O    . GLY   A 1 43  ? -44.457 17.552 32.436 1.00 41.04  ? 849  GLY   A O    1 
ATOM   295  N N    . LEU   A 1 44  ? -44.536 15.773 33.799 1.00 44.77  ? 850  LEU   A N    1 
ATOM   296  C CA   . LEU   A 1 44  ? -45.651 15.203 33.054 1.00 44.68  ? 850  LEU   A CA   1 
ATOM   297  C C    . LEU   A 1 44  ? -46.916 16.032 33.241 1.00 48.17  ? 850  LEU   A C    1 
ATOM   298  O O    . LEU   A 1 44  ? -47.701 16.177 32.298 1.00 51.82  ? 850  LEU   A O    1 
ATOM   299  C CB   . LEU   A 1 44  ? -45.883 13.749 33.474 1.00 40.62  ? 850  LEU   A CB   1 
ATOM   300  C CG   . LEU   A 1 44  ? -44.842 12.680 33.099 1.00 44.25  ? 850  LEU   A CG   1 
ATOM   301  C CD1  . LEU   A 1 44  ? -45.098 11.351 33.796 1.00 43.34  ? 850  LEU   A CD1  1 
ATOM   302  C CD2  . LEU   A 1 44  ? -44.771 12.471 31.599 1.00 40.74  ? 850  LEU   A CD2  1 
ATOM   303  N N    . ASP   A 1 45  ? -47.121 16.598 34.434 1.00 45.38  ? 851  ASP   A N    1 
ATOM   304  C CA   . ASP   A 1 45  ? -48.291 17.442 34.667 1.00 47.69  ? 851  ASP   A CA   1 
ATOM   305  C C    . ASP   A 1 45  ? -48.242 18.700 33.818 1.00 47.56  ? 851  ASP   A C    1 
ATOM   306  O O    . ASP   A 1 45  ? -49.231 19.067 33.175 1.00 47.16  ? 851  ASP   A O    1 
ATOM   307  C CB   . ASP   A 1 45  ? -48.375 17.828 36.138 1.00 47.63  ? 851  ASP   A CB   1 
ATOM   308  C CG   . ASP   A 1 45  ? -48.932 16.734 36.975 1.00 54.80  ? 851  ASP   A CG   1 
ATOM   309  O OD1  . ASP   A 1 45  ? -48.503 16.629 38.148 1.00 65.27  ? 851  ASP   A OD1  1 
ATOM   310  O OD2  . ASP   A 1 45  ? -49.780 15.963 36.457 1.00 57.36  ? 851  ASP   A OD2  1 
ATOM   311  N N    . LYS   A 1 46  ? -47.108 19.401 33.856 1.00 50.48  ? 852  LYS   A N    1 
ATOM   312  C CA   . LYS   A 1 46  ? -46.923 20.585 33.033 1.00 47.67  ? 852  LYS   A CA   1 
ATOM   313  C C    . LYS   A 1 46  ? -47.214 20.278 31.578 1.00 45.43  ? 852  LYS   A C    1 
ATOM   314  O O    . LYS   A 1 46  ? -47.901 21.048 30.899 1.00 45.99  ? 852  LYS   A O    1 
ATOM   315  C CB   . LYS   A 1 46  ? -45.497 21.116 33.186 1.00 41.88  ? 852  LYS   A CB   1 
ATOM   316  C CG   . LYS   A 1 46  ? -45.213 21.839 34.498 1.00 46.84  ? 852  LYS   A CG   1 
ATOM   317  C CD   . LYS   A 1 46  ? -43.695 21.960 34.707 1.00 44.31  ? 852  LYS   A CD   1 
ATOM   318  C CE   . LYS   A 1 46  ? -43.342 22.434 36.101 1.00 36.66  ? 852  LYS   A CE   1 
ATOM   319  N NZ   . LYS   A 1 46  ? -43.972 21.545 37.084 1.00 39.30  ? 852  LYS   A NZ   1 
ATOM   320  N N    . ALA   A 1 47  ? -46.705 19.152 31.080 1.00 43.55  ? 853  ALA   A N    1 
ATOM   321  C CA   . ALA   A 1 47  ? -46.939 18.811 29.682 1.00 43.08  ? 853  ALA   A CA   1 
ATOM   322  C C    . ALA   A 1 47  ? -48.420 18.566 29.424 1.00 46.07  ? 853  ALA   A C    1 
ATOM   323  O O    . ALA   A 1 47  ? -48.971 19.046 28.426 1.00 45.85  ? 853  ALA   A O    1 
ATOM   324  C CB   . ALA   A 1 47  ? -46.106 17.593 29.280 1.00 42.21  ? 853  ALA   A CB   1 
ATOM   325  N N    . GLU   A 1 48  ? -49.091 17.840 30.321 1.00 47.49  ? 854  GLU   A N    1 
ATOM   326  C CA   . GLU   A 1 48  ? -50.523 17.616 30.140 1.00 50.15  ? 854  GLU   A CA   1 
ATOM   327  C C    . GLU   A 1 48  ? -51.312 18.904 30.345 1.00 49.61  ? 854  GLU   A C    1 
ATOM   328  O O    . GLU   A 1 48  ? -52.306 19.146 29.652 1.00 46.96  ? 854  GLU   A O    1 
ATOM   329  C CB   . GLU   A 1 48  ? -51.005 16.512 31.077 1.00 49.20  ? 854  GLU   A CB   1 
ATOM   330  C CG   . GLU   A 1 48  ? -50.197 15.235 30.878 1.00 56.67  ? 854  GLU   A CG   1 
ATOM   331  C CD   . GLU   A 1 48  ? -50.621 14.076 31.770 1.00 66.87  ? 854  GLU   A CD   1 
ATOM   332  O OE1  . GLU   A 1 48  ? -51.407 14.287 32.730 1.00 68.89  ? 854  GLU   A OE1  1 
ATOM   333  O OE2  . GLU   A 1 48  ? -50.135 12.952 31.507 1.00 65.82  ? 854  GLU   A OE2  1 
ATOM   334  N N    . ARG   A 1 49  ? -50.874 19.761 31.270 1.00 50.30  ? 855  ARG   A N    1 
ATOM   335  C CA   . ARG   A 1 49  ? -51.553 21.042 31.420 1.00 53.48  ? 855  ARG   A CA   1 
ATOM   336  C C    . ARG   A 1 49  ? -51.413 21.882 30.155 1.00 48.48  ? 855  ARG   A C    1 
ATOM   337  O O    . ARG   A 1 49  ? -52.300 22.677 29.829 1.00 49.71  ? 855  ARG   A O    1 
ATOM   338  C CB   . ARG   A 1 49  ? -51.013 21.777 32.654 1.00 56.80  ? 855  ARG   A CB   1 
ATOM   339  C CG   . ARG   A 1 49  ? -51.751 23.061 33.027 1.00 64.24  ? 855  ARG   A CG   1 
ATOM   340  C CD   . ARG   A 1 49  ? -51.665 23.375 34.538 1.00 71.73  ? 855  ARG   A CD   1 
ATOM   341  N NE   . ARG   A 1 49  ? -50.460 22.833 35.165 1.00 69.88  ? 855  ARG   A NE   1 
ATOM   342  C CZ   . ARG   A 1 49  ? -49.249 23.389 35.083 1.00 70.96  ? 855  ARG   A CZ   1 
ATOM   343  N NH1  . ARG   A 1 49  ? -49.068 24.517 34.395 1.00 73.14  ? 855  ARG   A NH1  1 
ATOM   344  N NH2  . ARG   A 1 49  ? -48.210 22.810 35.684 1.00 62.65  ? 855  ARG   A NH2  1 
ATOM   345  N N    . ALA   A 1 50  ? -50.327 21.697 29.417 1.00 48.03  ? 856  ALA   A N    1 
ATOM   346  C CA   . ALA   A 1 50  ? -50.084 22.441 28.191 1.00 46.38  ? 856  ALA   A CA   1 
ATOM   347  C C    . ALA   A 1 50  ? -50.736 21.805 26.977 1.00 46.00  ? 856  ALA   A C    1 
ATOM   348  O O    . ALA   A 1 50  ? -50.712 22.399 25.894 1.00 45.81  ? 856  ALA   A O    1 
ATOM   349  C CB   . ALA   A 1 50  ? -48.575 22.578 27.937 1.00 38.38  ? 856  ALA   A CB   1 
ATOM   350  N N    . GLY   A 1 51  ? -51.315 20.624 27.127 1.00 44.66  ? 857  GLY   A N    1 
ATOM   351  C CA   . GLY   A 1 51  ? -51.953 19.960 26.018 1.00 42.27  ? 857  GLY   A CA   1 
ATOM   352  C C    . GLY   A 1 51  ? -51.041 19.055 25.241 1.00 40.29  ? 857  GLY   A C    1 
ATOM   353  O O    . GLY   A 1 51  ? -51.439 18.553 24.193 1.00 46.21  ? 857  GLY   A O    1 
ATOM   354  N N    . ILE   A 1 52  ? -49.838 18.816 25.728 1.00 38.98  ? 858  ILE   A N    1 
ATOM   355  C CA   . ILE   A 1 52  ? -48.839 18.098 24.960 1.00 39.01  ? 858  ILE   A CA   1 
ATOM   356  C C    . ILE   A 1 52  ? -48.933 16.616 25.289 1.00 40.90  ? 858  ILE   A C    1 
ATOM   357  O O    . ILE   A 1 52  ? -48.860 16.243 26.469 1.00 43.78  ? 858  ILE   A O    1 
ATOM   358  C CB   . ILE   A 1 52  ? -47.444 18.670 25.250 1.00 37.83  ? 858  ILE   A CB   1 
ATOM   359  C CG1  . ILE   A 1 52  ? -47.463 20.194 25.058 1.00 35.87  ? 858  ILE   A CG1  1 
ATOM   360  C CG2  . ILE   A 1 52  ? -46.390 18.015 24.366 1.00 36.98  ? 858  ILE   A CG2  1 
ATOM   361  C CD1  . ILE   A 1 52  ? -46.118 20.862 25.297 1.00 40.47  ? 858  ILE   A CD1  1 
ATOM   362  N N    . PRO   A 1 53  ? -49.069 15.743 24.292 1.00 36.88  ? 859  PRO   A N    1 
ATOM   363  C CA   . PRO   A 1 53  ? -49.019 14.301 24.559 1.00 38.11  ? 859  PRO   A CA   1 
ATOM   364  C C    . PRO   A 1 53  ? -47.781 13.934 25.367 1.00 42.19  ? 859  PRO   A C    1 
ATOM   365  O O    . PRO   A 1 53  ? -46.724 14.569 25.252 1.00 40.91  ? 859  PRO   A O    1 
ATOM   366  C CB   . PRO   A 1 53  ? -48.960 13.669 23.161 1.00 37.95  ? 859  PRO   A CB   1 
ATOM   367  C CG   . PRO   A 1 53  ? -49.223 14.754 22.197 1.00 39.86  ? 859  PRO   A CG   1 
ATOM   368  C CD   . PRO   A 1 53  ? -48.882 16.047 22.869 1.00 40.15  ? 859  PRO   A CD   1 
ATOM   369  N N    . THR   A 1 54  ? -47.918 12.867 26.158 1.00 41.84  ? 860  THR   A N    1 
ATOM   370  C CA   . THR   A 1 54  ? -46.873 12.389 27.048 1.00 39.21  ? 860  THR   A CA   1 
ATOM   371  C C    . THR   A 1 54  ? -46.748 10.876 26.901 1.00 42.27  ? 860  THR   A C    1 
ATOM   372  O O    . THR   A 1 54  ? -47.735 10.186 26.640 1.00 45.16  ? 860  THR   A O    1 
ATOM   373  C CB   . THR   A 1 54  ? -47.188 12.762 28.523 1.00 42.56  ? 860  THR   A CB   1 
ATOM   374  O OG1  . THR   A 1 54  ? -48.536 12.389 28.839 1.00 51.58  ? 860  THR   A OG1  1 
ATOM   375  C CG2  . THR   A 1 54  ? -47.039 14.253 28.760 1.00 40.37  ? 860  THR   A CG2  1 
ATOM   376  N N    . ARG   A 1 55  ? -45.524 10.363 27.042 1.00 39.92  ? 861  ARG   A N    1 
ATOM   377  C CA   . ARG   A 1 55  ? -45.293 8.926  27.174 1.00 38.81  ? 861  ARG   A CA   1 
ATOM   378  C C    . ARG   A 1 55  ? -44.281 8.702  28.287 1.00 43.60  ? 861  ARG   A C    1 
ATOM   379  O O    . ARG   A 1 55  ? -43.325 9.475  28.421 1.00 43.65  ? 861  ARG   A O    1 
ATOM   380  C CB   . ARG   A 1 55  ? -44.755 8.280  25.888 1.00 39.71  ? 861  ARG   A CB   1 
ATOM   381  C CG   . ARG   A 1 55  ? -45.584 8.504  24.630 1.00 40.20  ? 861  ARG   A CG   1 
ATOM   382  C CD   . ARG   A 1 55  ? -46.971 7.897  24.735 1.00 44.08  ? 861  ARG   A CD   1 
ATOM   383  N NE   . ARG   A 1 55  ? -47.506 7.504  23.434 1.00 52.14  ? 861  ARG   A NE   1 
ATOM   384  C CZ   . ARG   A 1 55  ? -48.501 8.136  22.813 1.00 56.46  ? 861  ARG   A CZ   1 
ATOM   385  N NH1  . ARG   A 1 55  ? -49.078 9.208  23.370 1.00 47.35  ? 861  ARG   A NH1  1 
ATOM   386  N NH2  . ARG   A 1 55  ? -48.912 7.693  21.629 1.00 56.38  ? 861  ARG   A NH2  1 
ATOM   387  N N    . VAL   A 1 56  ? -44.491 7.652  29.082 1.00 43.38  ? 862  VAL   A N    1 
ATOM   388  C CA   . VAL   A 1 56  ? -43.568 7.268  30.143 1.00 46.32  ? 862  VAL   A CA   1 
ATOM   389  C C    . VAL   A 1 56  ? -42.937 5.952  29.744 1.00 49.00  ? 862  VAL   A C    1 
ATOM   390  O O    . VAL   A 1 56  ? -43.637 4.947  29.598 1.00 46.21  ? 862  VAL   A O    1 
ATOM   391  C CB   . VAL   A 1 56  ? -44.260 7.142  31.509 1.00 45.36  ? 862  VAL   A CB   1 
ATOM   392  C CG1  . VAL   A 1 56  ? -43.398 6.315  32.455 1.00 46.78  ? 862  VAL   A CG1  1 
ATOM   393  C CG2  . VAL   A 1 56  ? -44.479 8.510  32.118 1.00 48.84  ? 862  VAL   A CG2  1 
ATOM   394  N N    . ILE   A 1 57  ? -41.620 5.946  29.580 1.00 48.93  ? 863  ILE   A N    1 
ATOM   395  C CA   . ILE   A 1 57  ? -40.895 4.733  29.237 1.00 55.52  ? 863  ILE   A CA   1 
ATOM   396  C C    . ILE   A 1 57  ? -40.103 4.313  30.464 1.00 64.18  ? 863  ILE   A C    1 
ATOM   397  O O    . ILE   A 1 57  ? -39.127 4.973  30.843 1.00 66.83  ? 863  ILE   A O    1 
ATOM   398  C CB   . ILE   A 1 57  ? -39.979 4.929  28.026 1.00 54.11  ? 863  ILE   A CB   1 
ATOM   399  C CG1  . ILE   A 1 57  ? -40.809 5.238  26.783 1.00 50.51  ? 863  ILE   A CG1  1 
ATOM   400  C CG2  . ILE   A 1 57  ? -39.144 3.673  27.801 1.00 54.99  ? 863  ILE   A CG2  1 
ATOM   401  C CD1  . ILE   A 1 57  ? -39.973 5.743  25.620 1.00 49.32  ? 863  ILE   A CD1  1 
ATOM   402  N N    . ASN   A 1 58  ? -40.513 3.206  31.077 1.00 75.66  ? 864  ASN   A N    1 
ATOM   403  C CA   . ASN   A 1 58  ? -39.852 2.684  32.264 1.00 81.52  ? 864  ASN   A CA   1 
ATOM   404  C C    . ASN   A 1 58  ? -38.583 1.934  31.879 1.00 83.19  ? 864  ASN   A C    1 
ATOM   405  O O    . ASN   A 1 58  ? -38.656 0.888  31.222 1.00 82.75  ? 864  ASN   A O    1 
ATOM   406  C CB   . ASN   A 1 58  ? -40.795 1.753  33.016 1.00 85.58  ? 864  ASN   A CB   1 
ATOM   407  C CG   . ASN   A 1 58  ? -40.464 1.660  34.475 1.00 86.32  ? 864  ASN   A CG   1 
ATOM   408  O OD1  . ASN   A 1 58  ? -39.304 1.795  34.868 1.00 89.07  ? 864  ASN   A OD1  1 
ATOM   409  N ND2  . ASN   A 1 58  ? -41.475 1.396  35.293 1.00 92.16  ? 864  ASN   A ND2  1 
ATOM   410  N N    . HIS   A 1 59  ? -37.426 2.433  32.323 1.00 85.89  ? 865  HIS   A N    1 
ATOM   411  C CA   . HIS   A 1 59  ? -36.174 1.743  32.028 1.00 86.23  ? 865  HIS   A CA   1 
ATOM   412  C C    . HIS   A 1 59  ? -35.973 0.557  32.960 1.00 89.08  ? 865  HIS   A C    1 
ATOM   413  O O    . HIS   A 1 59  ? -34.839 0.148  33.220 1.00 90.15  ? 865  HIS   A O    1 
ATOM   414  C CB   . HIS   A 1 59  ? -34.976 2.693  32.109 1.00 86.63  ? 865  HIS   A CB   1 
ATOM   415  C CG   . HIS   A 1 59  ? -34.815 3.370  33.435 1.00 90.92  ? 865  HIS   A CG   1 
ATOM   416  N ND1  . HIS   A 1 59  ? -35.400 4.584  33.730 1.00 85.00  ? 865  HIS   A ND1  1 
ATOM   417  C CD2  . HIS   A 1 59  ? -34.125 3.006  34.542 1.00 94.22  ? 865  HIS   A CD2  1 
ATOM   418  C CE1  . HIS   A 1 59  ? -35.078 4.936  34.962 1.00 87.53  ? 865  HIS   A CE1  1 
ATOM   419  N NE2  . HIS   A 1 59  ? -34.303 3.997  35.476 1.00 93.20  ? 865  HIS   A NE2  1 
ATOM   420  N N    . LYS   A 1 60  ? -37.068 0.002  33.469 1.00 87.83  ? 866  LYS   A N    1 
ATOM   421  C CA   . LYS   A 1 60  ? -37.045 -1.270 34.173 1.00 84.07  ? 866  LYS   A CA   1 
ATOM   422  C C    . LYS   A 1 60  ? -38.004 -2.252 33.522 1.00 82.31  ? 866  LYS   A C    1 
ATOM   423  O O    . LYS   A 1 60  ? -38.547 -3.133 34.182 1.00 88.53  ? 866  LYS   A O    1 
ATOM   424  C CB   . LYS   A 1 60  ? -37.381 -1.091 35.653 1.00 84.43  ? 866  LYS   A CB   1 
ATOM   425  N N    . LEU   A 1 61  ? -38.242 -2.085 32.229 1.00 79.08  ? 867  LEU   A N    1 
ATOM   426  C CA   . LEU   A 1 61  ? -39.067 -3.006 31.466 1.00 76.45  ? 867  LEU   A CA   1 
ATOM   427  C C    . LEU   A 1 61  ? -38.339 -3.465 30.215 1.00 76.81  ? 867  LEU   A C    1 
ATOM   428  O O    . LEU   A 1 61  ? -38.872 -4.290 29.462 1.00 78.60  ? 867  LEU   A O    1 
ATOM   429  C CB   . LEU   A 1 61  ? -40.403 -2.349 31.083 1.00 82.33  ? 867  LEU   A CB   1 
ATOM   430  C CG   . LEU   A 1 61  ? -41.453 -2.167 32.182 1.00 85.95  ? 867  LEU   A CG   1 
ATOM   431  C CD1  . LEU   A 1 61  ? -40.950 -1.238 33.269 1.00 87.31  ? 867  LEU   A CD1  1 
ATOM   432  C CD2  . LEU   A 1 61  ? -42.731 -1.607 31.600 1.00 85.79  ? 867  LEU   A CD2  1 
ATOM   433  N N    . TYR   A 1 62  ? -37.140 -2.941 29.975 1.00 79.04  ? 868  TYR   A N    1 
ATOM   434  C CA   . TYR   A 1 62  ? -36.300 -3.276 28.839 1.00 74.47  ? 868  TYR   A CA   1 
ATOM   435  C C    . TYR   A 1 62  ? -35.006 -3.874 29.367 1.00 74.32  ? 868  TYR   A C    1 
ATOM   436  O O    . TYR   A 1 62  ? -34.561 -3.548 30.470 1.00 75.48  ? 868  TYR   A O    1 
ATOM   437  C CB   . TYR   A 1 62  ? -36.005 -2.026 27.987 1.00 69.55  ? 868  TYR   A CB   1 
ATOM   438  C CG   . TYR   A 1 62  ? -37.256 -1.318 27.508 1.00 65.46  ? 868  TYR   A CG   1 
ATOM   439  C CD1  . TYR   A 1 62  ? -37.782 -1.569 26.251 1.00 61.28  ? 868  TYR   A CD1  1 
ATOM   440  C CD2  . TYR   A 1 62  ? -37.930 -0.427 28.330 1.00 62.34  ? 868  TYR   A CD2  1 
ATOM   441  C CE1  . TYR   A 1 62  ? -38.929 -0.936 25.822 1.00 55.70  ? 868  TYR   A CE1  1 
ATOM   442  C CE2  . TYR   A 1 62  ? -39.076 0.204  27.908 1.00 60.36  ? 868  TYR   A CE2  1 
ATOM   443  C CZ   . TYR   A 1 62  ? -39.571 -0.056 26.656 1.00 55.89  ? 868  TYR   A CZ   1 
ATOM   444  O OH   . TYR   A 1 62  ? -40.713 0.574  26.236 1.00 55.90  ? 868  TYR   A OH   1 
ATOM   445  N N    . LYS   A 1 63  ? -34.403 -4.761 28.585 1.00 77.38  ? 869  LYS   A N    1 
ATOM   446  C CA   . LYS   A 1 63  ? -33.169 -5.369 29.062 1.00 78.87  ? 869  LYS   A CA   1 
ATOM   447  C C    . LYS   A 1 63  ? -31.985 -4.426 28.902 1.00 80.08  ? 869  LYS   A C    1 
ATOM   448  O O    . LYS   A 1 63  ? -31.210 -4.224 29.842 1.00 82.42  ? 869  LYS   A O    1 
ATOM   449  C CB   . LYS   A 1 63  ? -32.877 -6.672 28.326 1.00 78.65  ? 869  LYS   A CB   1 
ATOM   450  C CG   . LYS   A 1 63  ? -31.664 -7.338 28.928 1.00 82.09  ? 869  LYS   A CG   1 
ATOM   451  C CD   . LYS   A 1 63  ? -30.839 -8.134 27.937 1.00 84.50  ? 869  LYS   A CD   1 
ATOM   452  C CE   . LYS   A 1 63  ? -29.441 -8.351 28.516 1.00 81.88  ? 869  LYS   A CE   1 
ATOM   453  N NZ   . LYS   A 1 63  ? -29.516 -8.889 29.916 1.00 77.79  ? 869  LYS   A NZ   1 
ATOM   454  N N    . ASN   A 1 64  ? -31.826 -3.848 27.720 1.00 83.38  ? 870  ASN   A N    1 
ATOM   455  C CA   . ASN   A 1 64  ? -30.631 -3.103 27.362 1.00 78.92  ? 870  ASN   A CA   1 
ATOM   456  C C    . ASN   A 1 64  ? -30.890 -1.615 27.428 1.00 78.32  ? 870  ASN   A C    1 
ATOM   457  O O    . ASN   A 1 64  ? -32.014 -1.148 27.232 1.00 80.64  ? 870  ASN   A O    1 
ATOM   458  C CB   . ASN   A 1 64  ? -30.184 -3.438 25.945 1.00 77.21  ? 870  ASN   A CB   1 
ATOM   459  C CG   . ASN   A 1 64  ? -30.067 -4.905 25.728 1.00 88.50  ? 870  ASN   A CG   1 
ATOM   460  O OD1  . ASN   A 1 64  ? -30.786 -5.477 24.905 1.00 97.36  ? 870  ASN   A OD1  1 
ATOM   461  N ND2  . ASN   A 1 64  ? -29.178 -5.548 26.484 1.00 94.87  ? 870  ASN   A ND2  1 
ATOM   462  N N    . ARG   A 1 65  ? -29.823 -0.861 27.656 1.00 68.15  ? 871  ARG   A N    1 
ATOM   463  C CA   . ARG   A 1 65  ? -29.884 0.544  27.301 1.00 62.61  ? 871  ARG   A CA   1 
ATOM   464  C C    . ARG   A 1 65  ? -30.312 0.690  25.845 1.00 61.91  ? 871  ARG   A C    1 
ATOM   465  O O    . ARG   A 1 65  ? -31.082 1.591  25.496 1.00 60.93  ? 871  ARG   A O    1 
ATOM   466  C CB   . ARG   A 1 65  ? -28.531 1.202  27.550 1.00 58.74  ? 871  ARG   A CB   1 
ATOM   467  C CG   . ARG   A 1 65  ? -28.637 2.574  28.147 1.00 59.62  ? 871  ARG   A CG   1 
ATOM   468  C CD   . ARG   A 1 65  ? -27.269 3.204  28.289 1.00 59.00  ? 871  ARG   A CD   1 
ATOM   469  N NE   . ARG   A 1 65  ? -26.641 2.854  29.567 1.00 59.93  ? 871  ARG   A NE   1 
ATOM   470  C CZ   . ARG   A 1 65  ? -27.020 3.317  30.760 1.00 58.07  ? 871  ARG   A CZ   1 
ATOM   471  N NH1  . ARG   A 1 65  ? -28.022 4.183  30.870 1.00 56.54  ? 871  ARG   A NH1  1 
ATOM   472  N NH2  . ARG   A 1 65  ? -26.373 2.929  31.850 1.00 61.73  ? 871  ARG   A NH2  1 
ATOM   473  N N    . VAL   A 1 66  ? -29.853 -0.219 24.985 1.00 62.21  ? 872  VAL   A N    1 
ATOM   474  C CA   . VAL   A 1 66  ? -30.175 -0.115 23.569 1.00 58.60  ? 872  VAL   A CA   1 
ATOM   475  C C    . VAL   A 1 66  ? -31.646 -0.437 23.320 1.00 63.60  ? 872  VAL   A C    1 
ATOM   476  O O    . VAL   A 1 66  ? -32.313 0.249  22.538 1.00 61.41  ? 872  VAL   A O    1 
ATOM   477  C CB   . VAL   A 1 66  ? -29.240 -1.015 22.752 1.00 53.77  ? 872  VAL   A CB   1 
ATOM   478  C CG1  . VAL   A 1 66  ? -29.772 -1.187 21.364 1.00 56.80  ? 872  VAL   A CG1  1 
ATOM   479  C CG2  . VAL   A 1 66  ? -27.870 -0.390 22.704 1.00 52.99  ? 872  VAL   A CG2  1 
ATOM   480  N N    . GLU   A 1 67  ? -32.179 -1.482 23.966 1.00 67.89  ? 873  GLU   A N    1 
ATOM   481  C CA   . GLU   A 1 67  ? -33.619 -1.728 23.878 1.00 67.53  ? 873  GLU   A CA   1 
ATOM   482  C C    . GLU   A 1 67  ? -34.403 -0.531 24.406 1.00 64.12  ? 873  GLU   A C    1 
ATOM   483  O O    . GLU   A 1 67  ? -35.462 -0.181 23.872 1.00 63.36  ? 873  GLU   A O    1 
ATOM   484  C CB   . GLU   A 1 67  ? -34.011 -2.994 24.649 1.00 70.66  ? 873  GLU   A CB   1 
ATOM   485  C CG   . GLU   A 1 67  ? -33.698 -4.322 23.961 1.00 78.13  ? 873  GLU   A CG   1 
ATOM   486  C CD   . GLU   A 1 67  ? -34.104 -4.359 22.483 1.00 83.62  ? 873  GLU   A CD   1 
ATOM   487  O OE1  . GLU   A 1 67  ? -35.283 -4.072 22.168 1.00 85.78  ? 873  GLU   A OE1  1 
ATOM   488  O OE2  . GLU   A 1 67  ? -33.250 -4.703 21.632 1.00 83.09  ? 873  GLU   A OE2  1 
ATOM   489  N N    . PHE   A 1 68  ? -33.893 0.115  25.451 1.00 57.93  ? 874  PHE   A N    1 
ATOM   490  C CA   . PHE   A 1 68  ? -34.605 1.240  26.036 1.00 56.25  ? 874  PHE   A CA   1 
ATOM   491  C C    . PHE   A 1 68  ? -34.643 2.434  25.084 1.00 54.83  ? 874  PHE   A C    1 
ATOM   492  O O    . PHE   A 1 68  ? -35.708 3.012  24.834 1.00 53.71  ? 874  PHE   A O    1 
ATOM   493  C CB   . PHE   A 1 68  ? -33.948 1.618  27.358 1.00 57.97  ? 874  PHE   A CB   1 
ATOM   494  C CG   . PHE   A 1 68  ? -34.490 2.869  27.966 1.00 55.12  ? 874  PHE   A CG   1 
ATOM   495  C CD1  . PHE   A 1 68  ? -35.609 2.833  28.770 1.00 59.77  ? 874  PHE   A CD1  1 
ATOM   496  C CD2  . PHE   A 1 68  ? -33.885 4.084  27.726 1.00 54.40  ? 874  PHE   A CD2  1 
ATOM   497  C CE1  . PHE   A 1 68  ? -36.109 3.984  29.334 1.00 62.34  ? 874  PHE   A CE1  1 
ATOM   498  C CE2  . PHE   A 1 68  ? -34.376 5.235  28.288 1.00 54.70  ? 874  PHE   A CE2  1 
ATOM   499  C CZ   . PHE   A 1 68  ? -35.492 5.187  29.091 1.00 57.71  ? 874  PHE   A CZ   1 
ATOM   500  N N    . ASP   A 1 69  ? -33.487 2.841  24.559 1.00 50.68  ? 875  ASP   A N    1 
ATOM   501  C CA   . ASP   A 1 69  ? -33.491 3.964  23.631 1.00 50.16  ? 875  ASP   A CA   1 
ATOM   502  C C    . ASP   A 1 69  ? -34.306 3.640  22.377 1.00 49.99  ? 875  ASP   A C    1 
ATOM   503  O O    . ASP   A 1 69  ? -34.942 4.530  21.801 1.00 45.83  ? 875  ASP   A O    1 
ATOM   504  C CB   . ASP   A 1 69  ? -32.054 4.363  23.267 1.00 47.90  ? 875  ASP   A CB   1 
ATOM   505  C CG   . ASP   A 1 69  ? -31.167 4.634  24.499 1.00 54.36  ? 875  ASP   A CG   1 
ATOM   506  O OD1  . ASP   A 1 69  ? -31.683 4.851  25.628 1.00 56.87  ? 875  ASP   A OD1  1 
ATOM   507  O OD2  . ASP   A 1 69  ? -29.925 4.640  24.329 1.00 52.67  ? 875  ASP   A OD2  1 
ATOM   508  N N    . SER   A 1 70  ? -34.303 2.375  21.945 1.00 50.33  ? 876  SER   A N    1 
ATOM   509  C CA   . SER   A 1 70  ? -35.150 1.966  20.830 1.00 48.64  ? 876  SER   A CA   1 
ATOM   510  C C    . SER   A 1 70  ? -36.599 2.341  21.079 1.00 47.06  ? 876  SER   A C    1 
ATOM   511  O O    . SER   A 1 70  ? -37.315 2.757  20.163 1.00 46.92  ? 876  SER   A O    1 
ATOM   512  C CB   . SER   A 1 70  ? -35.046 0.457  20.602 1.00 56.31  ? 876  SER   A CB   1 
ATOM   513  O OG   . SER   A 1 70  ? -33.719 0.046  20.325 1.00 64.41  ? 876  SER   A OG   1 
ATOM   514  N N    . ALA   A 1 71  ? -37.060 2.160  22.308 1.00 47.27  ? 877  ALA   A N    1 
ATOM   515  C CA   . ALA   A 1 71  ? -38.428 2.519  22.621 1.00 45.13  ? 877  ALA   A CA   1 
ATOM   516  C C    . ALA   A 1 71  ? -38.624 4.019  22.482 1.00 46.31  ? 877  ALA   A C    1 
ATOM   517  O O    . ALA   A 1 71  ? -39.638 4.468  21.942 1.00 45.16  ? 877  ALA   A O    1 
ATOM   518  C CB   . ALA   A 1 71  ? -38.784 2.032  24.027 1.00 46.00  ? 877  ALA   A CB   1 
ATOM   519  N N    . ILE   A 1 72  ? -37.647 4.810  22.935 1.00 46.28  ? 878  ILE   A N    1 
ATOM   520  C CA   . ILE   A 1 72  ? -37.727 6.262  22.769 1.00 43.69  ? 878  ILE   A CA   1 
ATOM   521  C C    . ILE   A 1 72  ? -37.742 6.627  21.291 1.00 44.10  ? 878  ILE   A C    1 
ATOM   522  O O    . ILE   A 1 72  ? -38.634 7.341  20.819 1.00 44.26  ? 878  ILE   A O    1 
ATOM   523  C CB   . ILE   A 1 72  ? -36.561 6.955  23.496 1.00 42.20  ? 878  ILE   A CB   1 
ATOM   524  C CG1  . ILE   A 1 72  ? -36.514 6.565  24.964 1.00 45.62  ? 878  ILE   A CG1  1 
ATOM   525  C CG2  . ILE   A 1 72  ? -36.668 8.431  23.384 1.00 39.13  ? 878  ILE   A CG2  1 
ATOM   526  C CD1  . ILE   A 1 72  ? -35.174 6.854  25.567 1.00 44.41  ? 878  ILE   A CD1  1 
ATOM   527  N N    . ASP   A 1 73  ? -36.739 6.153  20.542 1.00 43.59  ? 879  ASP   A N    1 
ATOM   528  C CA   . ASP   A 1 73  ? -36.680 6.378  19.101 1.00 44.62  ? 879  ASP   A CA   1 
ATOM   529  C C    . ASP   A 1 73  ? -37.995 6.013  18.410 1.00 45.89  ? 879  ASP   A C    1 
ATOM   530  O O    . ASP   A 1 73  ? -38.466 6.731  17.517 1.00 45.65  ? 879  ASP   A O    1 
ATOM   531  C CB   . ASP   A 1 73  ? -35.523 5.574  18.511 1.00 43.27  ? 879  ASP   A CB   1 
ATOM   532  C CG   . ASP   A 1 73  ? -35.062 6.107  17.174 1.00 45.39  ? 879  ASP   A CG   1 
ATOM   533  O OD1  . ASP   A 1 73  ? -34.847 7.334  17.052 1.00 47.56  ? 879  ASP   A OD1  1 
ATOM   534  O OD2  . ASP   A 1 73  ? -34.907 5.296  16.245 1.00 49.28  ? 879  ASP   A OD2  1 
ATOM   535  N N    . LEU   A 1 74  ? -38.606 4.900  18.807 1.00 43.33  ? 880  LEU   A N    1 
ATOM   536  C CA   . LEU   A 1 74  ? -39.894 4.536  18.235 1.00 42.30  ? 880  LEU   A CA   1 
ATOM   537  C C    . LEU   A 1 74  ? -40.901 5.665  18.386 1.00 43.12  ? 880  LEU   A C    1 
ATOM   538  O O    . LEU   A 1 74  ? -41.602 6.023  17.433 1.00 41.39  ? 880  LEU   A O    1 
ATOM   539  C CB   . LEU   A 1 74  ? -40.414 3.277  18.907 1.00 46.74  ? 880  LEU   A CB   1 
ATOM   540  C CG   . LEU   A 1 74  ? -41.264 2.362  18.039 1.00 45.68  ? 880  LEU   A CG   1 
ATOM   541  C CD1  . LEU   A 1 74  ? -40.383 1.694  17.017 1.00 44.94  ? 880  LEU   A CD1  1 
ATOM   542  C CD2  . LEU   A 1 74  ? -41.937 1.330  18.914 1.00 47.45  ? 880  LEU   A CD2  1 
ATOM   543  N N    . VAL   A 1 75  ? -40.993 6.235  19.589 1.00 41.71  ? 881  VAL   A N    1 
ATOM   544  C CA   . VAL   A 1 75  ? -41.951 7.309  19.821 1.00 41.78  ? 881  VAL   A CA   1 
ATOM   545  C C    . VAL   A 1 75  ? -41.561 8.553  19.024 1.00 46.17  ? 881  VAL   A C    1 
ATOM   546  O O    . VAL   A 1 75  ? -42.422 9.242  18.461 1.00 45.70  ? 881  VAL   A O    1 
ATOM   547  C CB   . VAL   A 1 75  ? -42.064 7.590  21.329 1.00 40.49  ? 881  VAL   A CB   1 
ATOM   548  C CG1  . VAL   A 1 75  ? -42.920 8.823  21.595 1.00 40.76  ? 881  VAL   A CG1  1 
ATOM   549  C CG2  . VAL   A 1 75  ? -42.643 6.385  22.040 1.00 37.61  ? 881  VAL   A CG2  1 
ATOM   550  N N    . LEU   A 1 76  ? -40.257 8.845  18.944 1.00 42.55  ? 882  LEU   A N    1 
ATOM   551  C CA   . LEU   A 1 76  ? -39.789 9.991  18.176 1.00 42.08  ? 882  LEU   A CA   1 
ATOM   552  C C    . LEU   A 1 76  ? -40.144 9.846  16.710 1.00 46.11  ? 882  LEU   A C    1 
ATOM   553  O O    . LEU   A 1 76  ? -40.548 10.816 16.056 1.00 44.63  ? 882  LEU   A O    1 
ATOM   554  C CB   . LEU   A 1 76  ? -38.279 10.151 18.324 1.00 39.33  ? 882  LEU   A CB   1 
ATOM   555  C CG   . LEU   A 1 76  ? -37.821 10.360 19.753 1.00 37.69  ? 882  LEU   A CG   1 
ATOM   556  C CD1  . LEU   A 1 76  ? -36.333 10.562 19.807 1.00 40.76  ? 882  LEU   A CD1  1 
ATOM   557  C CD2  . LEU   A 1 76  ? -38.535 11.553 20.280 1.00 35.58  ? 882  LEU   A CD2  1 
ATOM   558  N N    . GLU   A 1 77  ? -39.962 8.651  16.165 1.00 46.04  ? 883  GLU   A N    1 
ATOM   559  C CA   . GLU   A 1 77  ? -40.406 8.435  14.805 1.00 47.62  ? 883  GLU   A CA   1 
ATOM   560  C C    . GLU   A 1 77  ? -41.917 8.484  14.725 1.00 47.23  ? 883  GLU   A C    1 
ATOM   561  O O    . GLU   A 1 77  ? -42.460 9.039  13.765 1.00 49.45  ? 883  GLU   A O    1 
ATOM   562  C CB   . GLU   A 1 77  ? -39.888 7.102  14.285 1.00 48.81  ? 883  GLU   A CB   1 
ATOM   563  C CG   . GLU   A 1 77  ? -38.391 6.995  14.345 1.00 53.95  ? 883  GLU   A CG   1 
ATOM   564  C CD   . GLU   A 1 77  ? -37.732 7.573  13.129 1.00 62.71  ? 883  GLU   A CD   1 
ATOM   565  O OE1  . GLU   A 1 77  ? -38.433 8.268  12.362 1.00 69.34  ? 883  GLU   A OE1  1 
ATOM   566  O OE2  . GLU   A 1 77  ? -36.516 7.335  12.950 1.00 66.70  ? 883  GLU   A OE2  1 
ATOM   567  N N    . GLU   A 1 78  ? -42.620 7.921  15.708 1.00 49.79  ? 884  GLU   A N    1 
ATOM   568  C CA   . GLU   A 1 78  ? -44.075 7.939  15.623 1.00 52.19  ? 884  GLU   A CA   1 
ATOM   569  C C    . GLU   A 1 78  ? -44.589 9.367  15.514 1.00 51.05  ? 884  GLU   A C    1 
ATOM   570  O O    . GLU   A 1 78  ? -45.528 9.634  14.760 1.00 49.72  ? 884  GLU   A O    1 
ATOM   571  C CB   . GLU   A 1 78  ? -44.716 7.205  16.813 1.00 56.97  ? 884  GLU   A CB   1 
ATOM   572  C CG   . GLU   A 1 78  ? -46.180 7.395  16.862 1.00 64.69  ? 884  GLU   A CG   1 
ATOM   573  C CD   . GLU   A 1 78  ? -46.933 6.791  18.088 1.00 72.75  ? 884  GLU   A CD   1 
ATOM   574  O OE1  . GLU   A 1 78  ? -46.283 6.189  18.969 1.00 72.85  ? 884  GLU   A OE1  1 
ATOM   575  O OE2  . GLU   A 1 78  ? -48.194 6.875  18.105 1.00 78.81  ? 884  GLU   A OE2  1 
ATOM   576  N N    . PHE   A 1 79  ? -43.966 10.310 16.234 1.00 48.17  ? 885  PHE   A N    1 
ATOM   577  C CA   . PHE   A 1 79  ? -44.357 11.722 16.224 1.00 39.29  ? 885  PHE   A CA   1 
ATOM   578  C C    . PHE   A 1 79  ? -43.565 12.574 15.231 1.00 41.06  ? 885  PHE   A C    1 
ATOM   579  O O    . PHE   A 1 79  ? -43.600 13.812 15.324 1.00 38.66  ? 885  PHE   A O    1 
ATOM   580  C CB   . PHE   A 1 79  ? -44.214 12.317 17.628 1.00 40.73  ? 885  PHE   A CB   1 
ATOM   581  C CG   . PHE   A 1 79  ? -45.308 11.908 18.564 1.00 42.88  ? 885  PHE   A CG   1 
ATOM   582  C CD1  . PHE   A 1 79  ? -45.370 10.622 19.048 1.00 44.89  ? 885  PHE   A CD1  1 
ATOM   583  C CD2  . PHE   A 1 79  ? -46.285 12.813 18.956 1.00 41.85  ? 885  PHE   A CD2  1 
ATOM   584  C CE1  . PHE   A 1 79  ? -46.385 10.234 19.897 1.00 47.89  ? 885  PHE   A CE1  1 
ATOM   585  C CE2  . PHE   A 1 79  ? -47.308 12.426 19.811 1.00 36.97  ? 885  PHE   A CE2  1 
ATOM   586  C CZ   . PHE   A 1 79  ? -47.351 11.134 20.281 1.00 42.31  ? 885  PHE   A CZ   1 
ATOM   587  N N    . SER   A 1 80  ? -42.846 11.948 14.300 1.00 38.18  ? 886  SER   A N    1 
ATOM   588  C CA   . SER   A 1 80  ? -42.093 12.659 13.269 1.00 36.62  ? 886  SER   A CA   1 
ATOM   589  C C    . SER   A 1 80  ? -41.270 13.797 13.862 1.00 40.22  ? 886  SER   A C    1 
ATOM   590  O O    . SER   A 1 80  ? -41.276 14.925 13.361 1.00 41.86  ? 886  SER   A O    1 
ATOM   591  C CB   . SER   A 1 80  ? -43.026 13.190 12.190 1.00 34.02  ? 886  SER   A CB   1 
ATOM   592  O OG   . SER   A 1 80  ? -43.963 12.200 11.823 1.00 38.04  ? 886  SER   A OG   1 
ATOM   593  N N    . ILE   A 1 81  ? -40.543 13.489 14.937 1.00 35.18  ? 887  ILE   A N    1 
ATOM   594  C CA   . ILE   A 1 81  ? -39.789 14.512 15.644 1.00 34.83  ? 887  ILE   A CA   1 
ATOM   595  C C    . ILE   A 1 81  ? -38.586 14.961 14.822 1.00 33.25  ? 887  ILE   A C    1 
ATOM   596  O O    . ILE   A 1 81  ? -37.951 14.172 14.116 1.00 32.25  ? 887  ILE   A O    1 
ATOM   597  C CB   . ILE   A 1 81  ? -39.362 13.980 17.020 1.00 35.28  ? 887  ILE   A CB   1 
ATOM   598  C CG1  . ILE   A 1 81  ? -40.586 13.805 17.926 1.00 37.78  ? 887  ILE   A CG1  1 
ATOM   599  C CG2  . ILE   A 1 81  ? -38.319 14.864 17.621 1.00 34.23  ? 887  ILE   A CG2  1 
ATOM   600  C CD1  . ILE   A 1 81  ? -41.621 14.917 17.821 1.00 36.84  ? 887  ILE   A CD1  1 
ATOM   601  N N    . ASP   A 1 82  ? -38.261 16.242 14.904 1.00 36.15  ? 888  ASP   A N    1 
ATOM   602  C CA   . ASP   A 1 82  ? -37.083 16.765 14.226 1.00 34.46  ? 888  ASP   A CA   1 
ATOM   603  C C    . ASP   A 1 82  ? -35.943 17.081 15.179 1.00 37.47  ? 888  ASP   A C    1 
ATOM   604  O O    . ASP   A 1 82  ? -34.774 16.855 14.833 1.00 37.04  ? 888  ASP   A O    1 
ATOM   605  C CB   . ASP   A 1 82  ? -37.444 18.024 13.426 1.00 31.07  ? 888  ASP   A CB   1 
ATOM   606  C CG   . ASP   A 1 82  ? -38.449 17.745 12.319 1.00 36.42  ? 888  ASP   A CG   1 
ATOM   607  O OD1  . ASP   A 1 82  ? -38.249 16.765 11.564 1.00 35.01  ? 888  ASP   A OD1  1 
ATOM   608  O OD2  . ASP   A 1 82  ? -39.446 18.501 12.204 1.00 37.14  ? 888  ASP   A OD2  1 
ATOM   609  N N    . ILE   A 1 83  ? -36.261 17.583 16.377 1.00 33.45  ? 889  ILE   A N    1 
ATOM   610  C CA   . ILE   A 1 83  ? -35.271 17.969 17.371 1.00 32.87  ? 889  ILE   A CA   1 
ATOM   611  C C    . ILE   A 1 83  ? -35.631 17.352 18.714 1.00 31.62  ? 889  ILE   A C    1 
ATOM   612  O O    . ILE   A 1 83  ? -36.798 17.360 19.123 1.00 29.17  ? 889  ILE   A O    1 
ATOM   613  C CB   . ILE   A 1 83  ? -35.164 19.495 17.511 1.00 34.68  ? 889  ILE   A CB   1 
ATOM   614  C CG1  . ILE   A 1 83  ? -34.645 20.096 16.206 1.00 30.34  ? 889  ILE   A CG1  1 
ATOM   615  C CG2  . ILE   A 1 83  ? -34.270 19.830 18.726 1.00 33.38  ? 889  ILE   A CG2  1 
ATOM   616  C CD1  . ILE   A 1 83  ? -34.638 21.582 16.203 1.00 28.42  ? 889  ILE   A CD1  1 
ATOM   617  N N    . VAL   A 1 84  ? -34.622 16.828 19.404 1.00 31.34  ? 890  VAL   A N    1 
ATOM   618  C CA   . VAL   A 1 84  ? -34.788 16.229 20.723 1.00 32.33  ? 890  VAL   A CA   1 
ATOM   619  C C    . VAL   A 1 84  ? -34.104 17.123 21.745 1.00 31.40  ? 890  VAL   A C    1 
ATOM   620  O O    . VAL   A 1 84  ? -32.898 17.388 21.639 1.00 32.15  ? 890  VAL   A O    1 
ATOM   621  C CB   . VAL   A 1 84  ? -34.211 14.810 20.785 1.00 35.35  ? 890  VAL   A CB   1 
ATOM   622  C CG1  . VAL   A 1 84  ? -34.198 14.328 22.242 1.00 32.84  ? 890  VAL   A CG1  1 
ATOM   623  C CG2  . VAL   A 1 84  ? -34.996 13.874 19.883 1.00 32.60  ? 890  VAL   A CG2  1 
ATOM   624  N N    . CYS   A 1 85  ? -34.876 17.582 22.733 1.00 31.00  ? 891  CYS   A N    1 
ATOM   625  C CA   . CYS   A 1 85  ? -34.370 18.358 23.862 1.00 30.88  ? 891  CYS   A CA   1 
ATOM   626  C C    . CYS   A 1 85  ? -34.377 17.503 25.124 1.00 31.51  ? 891  CYS   A C    1 
ATOM   627  O O    . CYS   A 1 85  ? -35.439 17.043 25.557 1.00 31.72  ? 891  CYS   A O    1 
ATOM   628  C CB   . CYS   A 1 85  ? -35.209 19.614 24.070 1.00 29.34  ? 891  CYS   A CB   1 
ATOM   629  S SG   . CYS   A 1 85  ? -34.955 20.792 22.757 1.00 35.91  ? 891  CYS   A SG   1 
ATOM   630  N N    . LEU   A 1 86  ? -33.194 17.283 25.704 1.00 32.74  ? 892  LEU   A N    1 
ATOM   631  C CA   . LEU   A 1 86  ? -33.076 16.678 27.033 1.00 32.96  ? 892  LEU   A CA   1 
ATOM   632  C C    . LEU   A 1 86  ? -33.186 17.793 28.075 1.00 34.41  ? 892  LEU   A C    1 
ATOM   633  O O    . LEU   A 1 86  ? -32.297 18.649 28.183 1.00 34.10  ? 892  LEU   A O    1 
ATOM   634  C CB   . LEU   A 1 86  ? -31.761 15.913 27.171 1.00 30.58  ? 892  LEU   A CB   1 
ATOM   635  C CG   . LEU   A 1 86  ? -31.327 14.949 26.053 1.00 33.40  ? 892  LEU   A CG   1 
ATOM   636  C CD1  . LEU   A 1 86  ? -30.094 14.166 26.461 1.00 32.25  ? 892  LEU   A CD1  1 
ATOM   637  C CD2  . LEU   A 1 86  ? -32.436 13.983 25.680 1.00 33.10  ? 892  LEU   A CD2  1 
ATOM   638  N N    . ALA   A 1 87  ? -34.282 17.802 28.832 1.00 34.56  ? 893  ALA   A N    1 
ATOM   639  C CA   . ALA   A 1 87  ? -34.550 18.855 29.817 1.00 33.69  ? 893  ALA   A CA   1 
ATOM   640  C C    . ALA   A 1 87  ? -34.658 18.220 31.201 1.00 36.47  ? 893  ALA   A C    1 
ATOM   641  O O    . ALA   A 1 87  ? -35.746 18.070 31.754 1.00 39.19  ? 893  ALA   A O    1 
ATOM   642  C CB   . ALA   A 1 87  ? -35.823 19.625 29.447 1.00 27.88  ? 893  ALA   A CB   1 
ATOM   643  N N    . GLY   A 1 88  ? -33.522 17.867 31.776 1.00 37.44  ? 894  GLY   A N    1 
ATOM   644  C CA   . GLY   A 1 88  ? -33.547 17.163 33.033 1.00 36.02  ? 894  GLY   A CA   1 
ATOM   645  C C    . GLY   A 1 88  ? -33.696 15.676 32.880 1.00 39.62  ? 894  GLY   A C    1 
ATOM   646  O O    . GLY   A 1 88  ? -34.138 15.012 33.820 1.00 42.89  ? 894  GLY   A O    1 
ATOM   647  N N    . PHE   A 1 89  ? -33.354 15.132 31.719 1.00 40.27  ? 895  PHE   A N    1 
ATOM   648  C CA   . PHE   A 1 89  ? -33.365 13.695 31.502 1.00 39.62  ? 895  PHE   A CA   1 
ATOM   649  C C    . PHE   A 1 89  ? -32.185 13.070 32.227 1.00 44.02  ? 895  PHE   A C    1 
ATOM   650  O O    . PHE   A 1 89  ? -31.033 13.353 31.898 1.00 45.88  ? 895  PHE   A O    1 
ATOM   651  C CB   . PHE   A 1 89  ? -33.285 13.424 30.004 1.00 39.31  ? 895  PHE   A CB   1 
ATOM   652  C CG   . PHE   A 1 89  ? -33.626 12.026 29.622 1.00 37.43  ? 895  PHE   A CG   1 
ATOM   653  C CD1  . PHE   A 1 89  ? -34.873 11.511 29.911 1.00 35.14  ? 895  PHE   A CD1  1 
ATOM   654  C CD2  . PHE   A 1 89  ? -32.694 11.220 28.979 1.00 37.77  ? 895  PHE   A CD2  1 
ATOM   655  C CE1  . PHE   A 1 89  ? -35.194 10.206 29.569 1.00 38.95  ? 895  PHE   A CE1  1 
ATOM   656  C CE2  . PHE   A 1 89  ? -33.005 9.908  28.636 1.00 41.84  ? 895  PHE   A CE2  1 
ATOM   657  C CZ   . PHE   A 1 89  ? -34.260 9.399  28.933 1.00 40.25  ? 895  PHE   A CZ   1 
ATOM   658  N N    . MET   A 1 90  ? -32.449 12.226 33.211 1.00 46.84  ? 896  MET   A N    1 
ATOM   659  C CA   . MET   A 1 90  ? -31.363 11.655 34.012 1.00 49.13  ? 896  MET   A CA   1 
ATOM   660  C C    . MET   A 1 90  ? -31.054 10.225 33.601 1.00 51.68  ? 896  MET   A C    1 
ATOM   661  O O    . MET   A 1 90  ? -31.040 9.291  34.408 1.00 54.25  ? 896  MET   A O    1 
ATOM   662  C CB   . MET   A 1 90  ? -31.711 11.727 35.487 1.00 50.14  ? 896  MET   A CB   1 
ATOM   663  C CG   . MET   A 1 90  ? -31.863 13.124 35.995 1.00 50.78  ? 896  MET   A CG   1 
ATOM   664  S SD   . MET   A 1 90  ? -30.248 13.890 35.842 1.00 60.45  ? 896  MET   A SD   1 
ATOM   665  C CE   . MET   A 1 90  ? -30.605 15.577 36.330 1.00 52.18  ? 896  MET   A CE   1 
ATOM   666  N N    . ARG   A 1 91  ? -30.831 10.024 32.311 1.00 48.95  ? 897  ARG   A N    1 
ATOM   667  C CA   . ARG   A 1 91  ? -30.405 8.714  31.868 1.00 49.84  ? 897  ARG   A CA   1 
ATOM   668  C C    . ARG   A 1 91  ? -29.480 8.875  30.669 1.00 50.25  ? 897  ARG   A C    1 
ATOM   669  O O    . ARG   A 1 91  ? -29.698 9.739  29.821 1.00 49.14  ? 897  ARG   A O    1 
ATOM   670  C CB   . ARG   A 1 91  ? -31.618 7.848  31.559 1.00 48.76  ? 897  ARG   A CB   1 
ATOM   671  C CG   . ARG   A 1 91  ? -31.240 6.438  31.324 1.00 57.83  ? 897  ARG   A CG   1 
ATOM   672  C CD   . ARG   A 1 91  ? -32.334 5.481  31.722 1.00 68.51  ? 897  ARG   A CD   1 
ATOM   673  N NE   . ARG   A 1 91  ? -31.941 4.096  31.453 1.00 69.88  ? 897  ARG   A NE   1 
ATOM   674  C CZ   . ARG   A 1 91  ? -31.564 3.638  30.256 1.00 63.18  ? 897  ARG   A CZ   1 
ATOM   675  N NH1  . ARG   A 1 91  ? -31.501 4.451  29.199 1.00 62.65  ? 897  ARG   A NH1  1 
ATOM   676  N NH2  . ARG   A 1 91  ? -31.226 2.361  30.116 1.00 67.32  ? 897  ARG   A NH2  1 
ATOM   677  N N    . ILE   A 1 92  ? -28.430 8.070  30.622 1.00 53.52  ? 898  ILE   A N    1 
ATOM   678  C CA   . ILE   A 1 92  ? -27.404 8.212  29.600 1.00 50.44  ? 898  ILE   A CA   1 
ATOM   679  C C    . ILE   A 1 92  ? -27.792 7.404  28.378 1.00 49.02  ? 898  ILE   A C    1 
ATOM   680  O O    . ILE   A 1 92  ? -28.189 6.235  28.486 1.00 48.76  ? 898  ILE   A O    1 
ATOM   681  C CB   . ILE   A 1 92  ? -26.036 7.776  30.130 1.00 51.06  ? 898  ILE   A CB   1 
ATOM   682  C CG1  . ILE   A 1 92  ? -25.493 8.852  31.064 1.00 52.70  ? 898  ILE   A CG1  1 
ATOM   683  C CG2  . ILE   A 1 92  ? -25.097 7.514  28.978 1.00 45.33  ? 898  ILE   A CG2  1 
ATOM   684  C CD1  . ILE   A 1 92  ? -24.450 8.338  31.989 1.00 53.80  ? 898  ILE   A CD1  1 
ATOM   685  N N    . LEU   A 1 93  ? -27.649 8.018  27.211 1.00 47.53  ? 899  LEU   A N    1 
ATOM   686  C CA   . LEU   A 1 93  ? -28.197 7.463  25.986 1.00 47.48  ? 899  LEU   A CA   1 
ATOM   687  C C    . LEU   A 1 93  ? -27.157 6.615  25.274 1.00 46.83  ? 899  LEU   A C    1 
ATOM   688  O O    . LEU   A 1 93  ? -25.964 6.918  25.290 1.00 45.90  ? 899  LEU   A O    1 
ATOM   689  C CB   . LEU   A 1 93  ? -28.700 8.578  25.073 1.00 43.64  ? 899  LEU   A CB   1 
ATOM   690  C CG   . LEU   A 1 93  ? -29.959 9.267  25.614 1.00 44.91  ? 899  LEU   A CG   1 
ATOM   691  C CD1  . LEU   A 1 93  ? -29.984 10.744 25.298 1.00 41.97  ? 899  LEU   A CD1  1 
ATOM   692  C CD2  . LEU   A 1 93  ? -31.202 8.605  25.055 1.00 46.98  ? 899  LEU   A CD2  1 
ATOM   693  N N    . SER   A 1 94  ? -27.622 5.547  24.650 1.00 49.06  ? 900  SER   A N    1 
ATOM   694  C CA   . SER   A 1 94  ? -26.718 4.637  23.978 1.00 49.52  ? 900  SER   A CA   1 
ATOM   695  C C    . SER   A 1 94  ? -26.059 5.308  22.772 1.00 47.65  ? 900  SER   A C    1 
ATOM   696  O O    . SER   A 1 94  ? -26.565 6.273  22.199 1.00 46.20  ? 900  SER   A O    1 
ATOM   697  C CB   . SER   A 1 94  ? -27.467 3.382  23.546 1.00 52.35  ? 900  SER   A CB   1 
ATOM   698  O OG   . SER   A 1 94  ? -28.359 3.691  22.494 1.00 54.08  ? 900  SER   A OG   1 
ATOM   699  N N    . GLY   A 1 95  ? -24.917 4.755  22.378 1.00 52.73  ? 901  GLY   A N    1 
ATOM   700  C CA   . GLY   A 1 95  ? -24.118 5.298  21.307 1.00 53.22  ? 901  GLY   A CA   1 
ATOM   701  C C    . GLY   A 1 95  ? -24.830 5.327  19.974 1.00 47.10  ? 901  GLY   A C    1 
ATOM   702  O O    . GLY   A 1 95  ? -24.773 6.315  19.242 1.00 50.79  ? 901  GLY   A O    1 
ATOM   703  N N    . PRO   A 1 96  ? -25.490 4.235  19.605 1.00 48.67  ? 902  PRO   A N    1 
ATOM   704  C CA   . PRO   A 1 96  ? -26.246 4.281  18.345 1.00 46.66  ? 902  PRO   A CA   1 
ATOM   705  C C    . PRO   A 1 96  ? -27.392 5.268  18.410 1.00 46.50  ? 902  PRO   A C    1 
ATOM   706  O O    . PRO   A 1 96  ? -27.586 6.038  17.463 1.00 47.57  ? 902  PRO   A O    1 
ATOM   707  C CB   . PRO   A 1 96  ? -26.711 2.830  18.132 1.00 45.10  ? 902  PRO   A CB   1 
ATOM   708  C CG   . PRO   A 1 96  ? -26.427 2.108  19.388 1.00 49.04  ? 902  PRO   A CG   1 
ATOM   709  C CD   . PRO   A 1 96  ? -25.368 2.869  20.143 1.00 50.76  ? 902  PRO   A CD   1 
ATOM   710  N N    . PHE   A 1 97  ? -28.138 5.317  19.513 1.00 45.01  ? 903  PHE   A N    1 
ATOM   711  C CA   . PHE   A 1 97  ? -29.165 6.347  19.613 1.00 42.28  ? 903  PHE   A CA   1 
ATOM   712  C C    . PHE   A 1 97  ? -28.569 7.735  19.400 1.00 43.68  ? 903  PHE   A C    1 
ATOM   713  O O    . PHE   A 1 97  ? -29.110 8.545  18.644 1.00 43.94  ? 903  PHE   A O    1 
ATOM   714  C CB   . PHE   A 1 97  ? -29.874 6.276  20.954 1.00 42.30  ? 903  PHE   A CB   1 
ATOM   715  C CG   . PHE   A 1 97  ? -31.025 7.224  21.069 1.00 43.91  ? 903  PHE   A CG   1 
ATOM   716  C CD1  . PHE   A 1 97  ? -32.294 6.845  20.657 1.00 47.78  ? 903  PHE   A CD1  1 
ATOM   717  C CD2  . PHE   A 1 97  ? -30.845 8.500  21.571 1.00 44.28  ? 903  PHE   A CD2  1 
ATOM   718  C CE1  . PHE   A 1 97  ? -33.370 7.720  20.759 1.00 44.88  ? 903  PHE   A CE1  1 
ATOM   719  C CE2  . PHE   A 1 97  ? -31.912 9.384  21.678 1.00 41.27  ? 903  PHE   A CE2  1 
ATOM   720  C CZ   . PHE   A 1 97  ? -33.178 8.989  21.279 1.00 41.22  ? 903  PHE   A CZ   1 
ATOM   721  N N    . VAL   A 1 98  ? -27.448 8.027  20.055 1.00 43.52  ? 904  VAL   A N    1 
ATOM   722  C CA   . VAL   A 1 98  ? -26.844 9.349  19.911 1.00 46.22  ? 904  VAL   A CA   1 
ATOM   723  C C    . VAL   A 1 98  ? -26.391 9.571  18.476 1.00 44.23  ? 904  VAL   A C    1 
ATOM   724  O O    . VAL   A 1 98  ? -26.540 10.664 17.918 1.00 40.99  ? 904  VAL   A O    1 
ATOM   725  C CB   . VAL   A 1 98  ? -25.680 9.517  20.904 1.00 44.82  ? 904  VAL   A CB   1 
ATOM   726  C CG1  . VAL   A 1 98  ? -24.988 10.834 20.671 1.00 43.35  ? 904  VAL   A CG1  1 
ATOM   727  C CG2  . VAL   A 1 98  ? -26.185 9.422  22.331 1.00 44.12  ? 904  VAL   A CG2  1 
ATOM   728  N N    . GLN   A 1 99  ? -25.827 8.538  17.858 1.00 45.56  ? 905  GLN   A N    1 
ATOM   729  C CA   . GLN   A 1 99  ? -25.406 8.645  16.467 1.00 44.11  ? 905  GLN   A CA   1 
ATOM   730  C C    . GLN   A 1 99  ? -26.585 9.020  15.569 1.00 45.94  ? 905  GLN   A C    1 
ATOM   731  O O    . GLN   A 1 99  ? -26.476 9.925  14.733 1.00 44.95  ? 905  GLN   A O    1 
ATOM   732  C CB   . GLN   A 1 99  ? -24.757 7.330  16.021 1.00 43.44  ? 905  GLN   A CB   1 
ATOM   733  N N    . LYS   A 1 100 ? -27.737 8.355  15.753 1.00 44.68  ? 906  LYS   A N    1 
ATOM   734  C CA   . LYS   A 1 100 ? -28.887 8.597  14.880 1.00 42.97  ? 906  LYS   A CA   1 
ATOM   735  C C    . LYS   A 1 100 ? -29.384 10.028 14.993 1.00 45.14  ? 906  LYS   A C    1 
ATOM   736  O O    . LYS   A 1 100 ? -29.857 10.611 14.008 1.00 47.90  ? 906  LYS   A O    1 
ATOM   737  C CB   . LYS   A 1 100 ? -30.028 7.632  15.200 1.00 42.18  ? 906  LYS   A CB   1 
ATOM   738  C CG   . LYS   A 1 100 ? -31.317 7.979  14.482 1.00 39.18  ? 906  LYS   A CG   1 
ATOM   739  C CD   . LYS   A 1 100 ? -32.391 6.903  14.634 1.00 44.34  ? 906  LYS   A CD   1 
ATOM   740  C CE   . LYS   A 1 100 ? -33.666 7.311  13.901 1.00 49.41  ? 906  LYS   A CE   1 
ATOM   741  N NZ   . LYS   A 1 100 ? -34.677 6.230  13.790 1.00 55.15  ? 906  LYS   A NZ   1 
ATOM   742  N N    . TRP   A 1 101 ? -29.309 10.603 16.184 1.00 41.68  ? 907  TRP   A N    1 
ATOM   743  C CA   . TRP   A 1 101 ? -29.794 11.950 16.413 1.00 41.00  ? 907  TRP   A CA   1 
ATOM   744  C C    . TRP   A 1 101 ? -28.668 12.962 16.460 1.00 42.75  ? 907  TRP   A C    1 
ATOM   745  O O    . TRP   A 1 101 ? -28.899 14.116 16.836 1.00 41.51  ? 907  TRP   A O    1 
ATOM   746  C CB   . TRP   A 1 101 ? -30.627 11.980 17.688 1.00 36.15  ? 907  TRP   A CB   1 
ATOM   747  C CG   . TRP   A 1 101 ? -31.851 11.172 17.469 1.00 37.80  ? 907  TRP   A CG   1 
ATOM   748  C CD1  . TRP   A 1 101 ? -31.998 9.835  17.663 1.00 40.46  ? 907  TRP   A CD1  1 
ATOM   749  C CD2  . TRP   A 1 101 ? -33.087 11.637 16.931 1.00 39.42  ? 907  TRP   A CD2  1 
ATOM   750  N NE1  . TRP   A 1 101 ? -33.261 9.439  17.305 1.00 40.63  ? 907  TRP   A NE1  1 
ATOM   751  C CE2  . TRP   A 1 101 ? -33.951 10.532 16.856 1.00 39.31  ? 907  TRP   A CE2  1 
ATOM   752  C CE3  . TRP   A 1 101 ? -33.554 12.893 16.520 1.00 39.17  ? 907  TRP   A CE3  1 
ATOM   753  C CZ2  . TRP   A 1 101 ? -35.254 10.638 16.386 1.00 41.61  ? 907  TRP   A CZ2  1 
ATOM   754  C CZ3  . TRP   A 1 101 ? -34.851 13.000 16.055 1.00 39.45  ? 907  TRP   A CZ3  1 
ATOM   755  C CH2  . TRP   A 1 101 ? -35.683 11.878 15.982 1.00 40.83  ? 907  TRP   A CH2  1 
ATOM   756  N N    . ASN   A 1 102 ? -27.461 12.569 16.058 1.00 43.45  ? 908  ASN   A N    1 
ATOM   757  C CA   . ASN   A 1 102 ? -26.359 13.514 16.065 1.00 43.97  ? 908  ASN   A CA   1 
ATOM   758  C C    . ASN   A 1 102 ? -26.774 14.773 15.332 1.00 42.10  ? 908  ASN   A C    1 
ATOM   759  O O    . ASN   A 1 102 ? -27.304 14.713 14.223 1.00 40.55  ? 908  ASN   A O    1 
ATOM   760  C CB   . ASN   A 1 102 ? -25.121 12.917 15.413 1.00 39.62  ? 908  ASN   A CB   1 
ATOM   761  C CG   . ASN   A 1 102 ? -23.928 13.832 15.528 1.00 41.70  ? 908  ASN   A CG   1 
ATOM   762  O OD1  . ASN   A 1 102 ? -23.357 14.237 14.530 1.00 48.53  ? 908  ASN   A OD1  1 
ATOM   763  N ND2  . ASN   A 1 102 ? -23.555 14.180 16.757 1.00 47.96  ? 908  ASN   A ND2  1 
ATOM   764  N N    . GLY   A 1 103 ? -26.572 15.912 15.979 1.00 42.89  ? 909  GLY   A N    1 
ATOM   765  C CA   . GLY   A 1 103 ? -26.956 17.166 15.387 1.00 38.84  ? 909  GLY   A CA   1 
ATOM   766  C C    . GLY   A 1 103 ? -28.415 17.515 15.529 1.00 38.79  ? 909  GLY   A C    1 
ATOM   767  O O    . GLY   A 1 103 ? -28.829 18.562 15.024 1.00 36.67  ? 909  GLY   A O    1 
ATOM   768  N N    . LYS   A 1 104 ? -29.212 16.689 16.208 1.00 38.29  ? 910  LYS   A N    1 
ATOM   769  C CA   . LYS   A 1 104 ? -30.621 17.004 16.393 1.00 36.65  ? 910  LYS   A CA   1 
ATOM   770  C C    . LYS   A 1 104 ? -31.049 16.902 17.850 1.00 35.58  ? 910  LYS   A C    1 
ATOM   771  O O    . LYS   A 1 104 ? -32.255 16.927 18.140 1.00 34.78  ? 910  LYS   A O    1 
ATOM   772  C CB   . LYS   A 1 104 ? -31.496 16.087 15.530 1.00 37.57  ? 910  LYS   A CB   1 
ATOM   773  C CG   . LYS   A 1 104 ? -31.182 16.135 14.069 1.00 38.58  ? 910  LYS   A CG   1 
ATOM   774  C CD   . LYS   A 1 104 ? -31.976 15.088 13.297 1.00 41.33  ? 910  LYS   A CD   1 
ATOM   775  C CE   . LYS   A 1 104 ? -31.932 15.364 11.799 1.00 36.38  ? 910  LYS   A CE   1 
ATOM   776  N NZ   . LYS   A 1 104 ? -32.112 14.095 11.033 1.00 49.80  ? 910  LYS   A NZ   1 
ATOM   777  N N    . MET   A 1 105 ? -30.110 16.788 18.776 1.00 36.75  ? 911  MET   A N    1 
ATOM   778  C CA   . MET   A 1 105 ? -30.439 16.533 20.170 1.00 33.16  ? 911  MET   A CA   1 
ATOM   779  C C    . MET   A 1 105 ? -29.660 17.502 21.041 1.00 35.34  ? 911  MET   A C    1 
ATOM   780  O O    . MET   A 1 105 ? -28.423 17.490 21.031 1.00 35.72  ? 911  MET   A O    1 
ATOM   781  C CB   . MET   A 1 105 ? -30.111 15.091 20.540 1.00 34.06  ? 911  MET   A CB   1 
ATOM   782  C CG   . MET   A 1 105 ? -30.413 14.756 21.997 1.00 38.93  ? 911  MET   A CG   1 
ATOM   783  S SD   . MET   A 1 105 ? -30.775 13.016 22.259 1.00 42.63  ? 911  MET   A SD   1 
ATOM   784  C CE   . MET   A 1 105 ? -29.329 12.248 21.529 1.00 36.99  ? 911  MET   A CE   1 
ATOM   785  N N    . LEU   A 1 106 ? -30.382 18.324 21.796 1.00 35.80  ? 912  LEU   A N    1 
ATOM   786  C CA   . LEU   A 1 106 ? -29.813 19.325 22.692 1.00 32.75  ? 912  LEU   A CA   1 
ATOM   787  C C    . LEU   A 1 106 ? -29.941 18.881 24.146 1.00 33.87  ? 912  LEU   A C    1 
ATOM   788  O O    . LEU   A 1 106 ? -30.907 18.209 24.528 1.00 32.75  ? 912  LEU   A O    1 
ATOM   789  C CB   . LEU   A 1 106 ? -30.513 20.680 22.530 1.00 28.57  ? 912  LEU   A CB   1 
ATOM   790  C CG   . LEU   A 1 106 ? -30.256 21.499 21.270 1.00 31.52  ? 912  LEU   A CG   1 
ATOM   791  C CD1  . LEU   A 1 106 ? -30.549 20.684 20.032 1.00 29.88  ? 912  LEU   A CD1  1 
ATOM   792  C CD2  . LEU   A 1 106 ? -31.113 22.752 21.301 1.00 29.02  ? 912  LEU   A CD2  1 
ATOM   793  N N    . ASN   A 1 107 ? -28.964 19.276 24.959 1.00 33.16  ? 913  ASN   A N    1 
ATOM   794  C CA   . ASN   A 1 107 ? -28.985 19.020 26.388 1.00 32.44  ? 913  ASN   A CA   1 
ATOM   795  C C    . ASN   A 1 107 ? -28.691 20.305 27.141 1.00 33.49  ? 913  ASN   A C    1 
ATOM   796  O O    . ASN   A 1 107 ? -27.867 21.109 26.701 1.00 34.63  ? 913  ASN   A O    1 
ATOM   797  C CB   . ASN   A 1 107 ? -27.971 17.969 26.752 1.00 37.12  ? 913  ASN   A CB   1 
ATOM   798  C CG   . ASN   A 1 107 ? -27.951 17.676 28.223 1.00 37.73  ? 913  ASN   A CG   1 
ATOM   799  O OD1  . ASN   A 1 107 ? -28.983 17.367 28.811 1.00 39.16  ? 913  ASN   A OD1  1 
ATOM   800  N ND2  . ASN   A 1 107 ? -26.770 17.756 28.830 1.00 36.41  ? 913  ASN   A ND2  1 
ATOM   801  N N    . ILE   A 1 108 ? -29.375 20.504 28.266 1.00 35.13  ? 914  ILE   A N    1 
ATOM   802  C CA   . ILE   A 1 108 ? -29.078 21.595 29.196 1.00 31.42  ? 914  ILE   A CA   1 
ATOM   803  C C    . ILE   A 1 108 ? -28.309 21.015 30.376 1.00 35.63  ? 914  ILE   A C    1 
ATOM   804  O O    . ILE   A 1 108 ? -28.821 20.147 31.099 1.00 38.91  ? 914  ILE   A O    1 
ATOM   805  C CB   . ILE   A 1 108 ? -30.354 22.302 29.667 1.00 30.83  ? 914  ILE   A CB   1 
ATOM   806  C CG1  . ILE   A 1 108 ? -29.994 23.422 30.641 1.00 33.37  ? 914  ILE   A CG1  1 
ATOM   807  C CG2  . ILE   A 1 108 ? -31.284 21.312 30.337 1.00 30.14  ? 914  ILE   A CG2  1 
ATOM   808  C CD1  . ILE   A 1 108 ? -29.080 24.462 30.085 1.00 26.47  ? 914  ILE   A CD1  1 
ATOM   809  N N    . HIS   A 1 109 ? -27.074 21.475 30.553 1.00 35.25  ? 915  HIS   A N    1 
ATOM   810  C CA   . HIS   A 1 109 ? -26.219 21.050 31.641 1.00 34.66  ? 915  HIS   A CA   1 
ATOM   811  C C    . HIS   A 1 109 ? -25.910 22.240 32.547 1.00 35.55  ? 915  HIS   A C    1 
ATOM   812  O O    . HIS   A 1 109 ? -25.578 23.326 32.049 1.00 32.04  ? 915  HIS   A O    1 
ATOM   813  C CB   . HIS   A 1 109 ? -24.926 20.447 31.104 1.00 32.80  ? 915  HIS   A CB   1 
ATOM   814  C CG   . HIS   A 1 109 ? -23.949 20.066 32.171 1.00 36.75  ? 915  HIS   A CG   1 
ATOM   815  N ND1  . HIS   A 1 109 ? -24.068 18.908 32.910 1.00 39.10  ? 915  HIS   A ND1  1 
ATOM   816  C CD2  . HIS   A 1 109 ? -22.844 20.699 32.634 1.00 33.16  ? 915  HIS   A CD2  1 
ATOM   817  C CE1  . HIS   A 1 109 ? -23.071 18.840 33.774 1.00 39.24  ? 915  HIS   A CE1  1 
ATOM   818  N NE2  . HIS   A 1 109 ? -22.315 19.915 33.628 1.00 33.22  ? 915  HIS   A NE2  1 
ATOM   819  N N    . PRO   A 1 110 ? -25.992 22.084 33.871 1.00 35.52  ? 916  PRO   A N    1 
ATOM   820  C CA   . PRO   A 1 110 ? -25.946 23.240 34.772 1.00 36.82  ? 916  PRO   A CA   1 
ATOM   821  C C    . PRO   A 1 110 ? -24.528 23.593 35.196 1.00 35.07  ? 916  PRO   A C    1 
ATOM   822  O O    . PRO   A 1 110 ? -24.239 23.774 36.383 1.00 33.75  ? 916  PRO   A O    1 
ATOM   823  C CB   . PRO   A 1 110 ? -26.806 22.775 35.955 1.00 35.54  ? 916  PRO   A CB   1 
ATOM   824  C CG   . PRO   A 1 110 ? -26.595 21.251 35.990 1.00 38.18  ? 916  PRO   A CG   1 
ATOM   825  C CD   . PRO   A 1 110 ? -26.010 20.828 34.634 1.00 37.28  ? 916  PRO   A CD   1 
ATOM   826  N N    . SER   A 1 111 ? -23.619 23.685 34.220 1.00 34.68  ? 917  SER   A N    1 
ATOM   827  C CA   . SER   A 1 111 ? -22.316 24.283 34.470 1.00 30.31  ? 917  SER   A CA   1 
ATOM   828  C C    . SER   A 1 111 ? -21.814 24.945 33.198 1.00 33.22  ? 917  SER   A C    1 
ATOM   829  O O    . SER   A 1 111 ? -22.388 24.794 32.117 1.00 33.24  ? 917  SER   A O    1 
ATOM   830  C CB   . SER   A 1 111 ? -21.300 23.264 34.996 1.00 29.70  ? 917  SER   A CB   1 
ATOM   831  O OG   . SER   A 1 111 ? -20.769 22.434 33.989 1.00 30.91  ? 917  SER   A OG   1 
ATOM   832  N N    . LEU   A 1 112 ? -20.733 25.707 33.352 1.00 33.83  ? 918  LEU   A N    1 
ATOM   833  C CA   . LEU   A 1 112 ? -20.002 26.258 32.219 1.00 30.19  ? 918  LEU   A CA   1 
ATOM   834  C C    . LEU   A 1 112 ? -19.026 25.185 31.758 1.00 30.62  ? 918  LEU   A C    1 
ATOM   835  O O    . LEU   A 1 112 ? -17.879 25.121 32.200 1.00 32.10  ? 918  LEU   A O    1 
ATOM   836  C CB   . LEU   A 1 112 ? -19.316 27.560 32.609 1.00 29.88  ? 918  LEU   A CB   1 
ATOM   837  C CG   . LEU   A 1 112 ? -20.309 28.703 32.832 1.00 29.71  ? 918  LEU   A CG   1 
ATOM   838  C CD1  . LEU   A 1 112 ? -19.585 29.941 33.223 1.00 30.86  ? 918  LEU   A CD1  1 
ATOM   839  C CD2  . LEU   A 1 112 ? -21.115 28.954 31.580 1.00 25.13  ? 918  LEU   A CD2  1 
ATOM   840  N N    . LEU   A 1 113 ? -19.501 24.305 30.879 1.00 29.96  ? 919  LEU   A N    1 
ATOM   841  C CA   . LEU   A 1 113 ? -18.637 23.283 30.323 1.00 30.90  ? 919  LEU   A CA   1 
ATOM   842  C C    . LEU   A 1 113 ? -17.453 23.936 29.615 1.00 30.08  ? 919  LEU   A C    1 
ATOM   843  O O    . LEU   A 1 113 ? -17.590 25.008 29.023 1.00 30.25  ? 919  LEU   A O    1 
ATOM   844  C CB   . LEU   A 1 113 ? -19.413 22.408 29.343 1.00 35.54  ? 919  LEU   A CB   1 
ATOM   845  C CG   . LEU   A 1 113 ? -20.492 21.508 29.940 1.00 35.88  ? 919  LEU   A CG   1 
ATOM   846  C CD1  . LEU   A 1 113 ? -21.317 20.930 28.810 1.00 32.38  ? 919  LEU   A CD1  1 
ATOM   847  C CD2  . LEU   A 1 113 ? -19.893 20.404 30.843 1.00 32.16  ? 919  LEU   A CD2  1 
ATOM   848  N N    . PRO   A 1 114 ? -16.286 23.291 29.618 1.00 30.06  ? 920  PRO   A N    1 
ATOM   849  C CA   . PRO   A 1 114 ? -16.087 21.923 30.113 1.00 33.67  ? 920  PRO   A CA   1 
ATOM   850  C C    . PRO   A 1 114 ? -15.985 21.746 31.631 1.00 34.71  ? 920  PRO   A C    1 
ATOM   851  O O    . PRO   A 1 114 ? -15.779 20.616 32.047 1.00 40.14  ? 920  PRO   A O    1 
ATOM   852  C CB   . PRO   A 1 114 ? -14.753 21.513 29.459 1.00 32.98  ? 920  PRO   A CB   1 
ATOM   853  C CG   . PRO   A 1 114 ? -14.000 22.785 29.277 1.00 33.38  ? 920  PRO   A CG   1 
ATOM   854  C CD   . PRO   A 1 114 ? -15.056 23.857 29.028 1.00 33.02  ? 920  PRO   A CD   1 
ATOM   855  N N    . SER   A 1 115 ? -16.094 22.791 32.446 1.00 34.84  ? 921  SER   A N    1 
ATOM   856  C CA   . SER   A 1 115 ? -16.034 22.578 33.893 1.00 35.45  ? 921  SER   A CA   1 
ATOM   857  C C    . SER   A 1 115 ? -17.199 21.701 34.350 1.00 33.71  ? 921  SER   A C    1 
ATOM   858  O O    . SER   A 1 115 ? -18.323 21.828 33.854 1.00 30.78  ? 921  SER   A O    1 
ATOM   859  C CB   . SER   A 1 115 ? -16.076 23.913 34.650 1.00 30.92  ? 921  SER   A CB   1 
ATOM   860  O OG   . SER   A 1 115 ? -14.895 24.678 34.472 1.00 34.66  ? 921  SER   A OG   1 
ATOM   861  N N    . PHE   A 1 116 ? -16.927 20.809 35.310 1.00 35.45  ? 922  PHE   A N    1 
ATOM   862  C CA   . PHE   A 1 116 ? -17.978 20.099 36.060 1.00 32.07  ? 922  PHE   A CA   1 
ATOM   863  C C    . PHE   A 1 116 ? -18.905 19.303 35.151 1.00 33.22  ? 922  PHE   A C    1 
ATOM   864  O O    . PHE   A 1 116 ? -20.125 19.397 35.232 1.00 34.04  ? 922  PHE   A O    1 
ATOM   865  C CB   . PHE   A 1 116 ? -18.773 21.077 36.922 1.00 33.20  ? 922  PHE   A CB   1 
ATOM   866  C CG   . PHE   A 1 116 ? -17.900 22.032 37.657 1.00 30.82  ? 922  PHE   A CG   1 
ATOM   867  C CD1  . PHE   A 1 116 ? -16.771 21.564 38.323 1.00 32.36  ? 922  PHE   A CD1  1 
ATOM   868  C CD2  . PHE   A 1 116 ? -18.174 23.385 37.666 1.00 27.93  ? 922  PHE   A CD2  1 
ATOM   869  C CE1  . PHE   A 1 116 ? -15.945 22.427 39.002 1.00 33.49  ? 922  PHE   A CE1  1 
ATOM   870  C CE2  . PHE   A 1 116 ? -17.350 24.264 38.334 1.00 28.97  ? 922  PHE   A CE2  1 
ATOM   871  C CZ   . PHE   A 1 116 ? -16.228 23.790 38.999 1.00 32.63  ? 922  PHE   A CZ   1 
ATOM   872  N N    . LYS   A 1 117 ? -18.310 18.525 34.258 1.00 39.04  ? 923  LYS   A N    1 
ATOM   873  C CA   . LYS   A 1 117 ? -19.057 17.472 33.606 1.00 34.39  ? 923  LYS   A CA   1 
ATOM   874  C C    . LYS   A 1 117 ? -19.663 16.549 34.660 1.00 39.48  ? 923  LYS   A C    1 
ATOM   875  O O    . LYS   A 1 117 ? -19.176 16.436 35.786 1.00 43.41  ? 923  LYS   A O    1 
ATOM   876  C CB   . LYS   A 1 117 ? -18.139 16.682 32.684 1.00 36.97  ? 923  LYS   A CB   1 
ATOM   877  C CG   . LYS   A 1 117 ? -17.463 17.500 31.605 1.00 39.24  ? 923  LYS   A CG   1 
ATOM   878  C CD   . LYS   A 1 117 ? -16.739 16.585 30.634 1.00 42.69  ? 923  LYS   A CD   1 
ATOM   879  C CE   . LYS   A 1 117 ? -15.806 17.348 29.718 1.00 49.15  ? 923  LYS   A CE   1 
ATOM   880  N NZ   . LYS   A 1 117 ? -16.606 18.074 28.687 1.00 52.85  ? 923  LYS   A NZ   1 
ATOM   881  N N    . GLY   A 1 118 ? -20.725 15.867 34.295 1.00 43.52  ? 924  GLY   A N    1 
ATOM   882  C CA   . GLY   A 1 118 ? -21.265 14.868 35.192 1.00 44.44  ? 924  GLY   A CA   1 
ATOM   883  C C    . GLY   A 1 118 ? -22.513 15.347 35.895 1.00 47.72  ? 924  GLY   A C    1 
ATOM   884  O O    . GLY   A 1 118 ? -23.066 16.415 35.612 1.00 47.98  ? 924  GLY   A O    1 
ATOM   885  N N    . SER   A 1 119 ? -22.962 14.531 36.842 1.00 47.67  ? 925  SER   A N    1 
ATOM   886  C CA   . SER   A 1 119 ? -24.330 14.668 37.314 1.00 52.19  ? 925  SER   A CA   1 
ATOM   887  C C    . SER   A 1 119 ? -24.479 15.594 38.514 1.00 51.12  ? 925  SER   A C    1 
ATOM   888  O O    . SER   A 1 119 ? -25.574 16.124 38.733 1.00 50.48  ? 925  SER   A O    1 
ATOM   889  C CB   . SER   A 1 119 ? -24.901 13.292 37.647 1.00 48.92  ? 925  SER   A CB   1 
ATOM   890  O OG   . SER   A 1 119 ? -24.012 12.597 38.498 1.00 54.28  ? 925  SER   A OG   1 
ATOM   891  N N    . ASN   A 1 120 ? -23.424 15.820 39.289 1.00 43.64  ? 926  ASN   A N    1 
ATOM   892  C CA   . ASN   A 1 120 ? -23.587 16.676 40.459 1.00 46.63  ? 926  ASN   A CA   1 
ATOM   893  C C    . ASN   A 1 120 ? -22.825 17.974 40.264 1.00 41.41  ? 926  ASN   A C    1 
ATOM   894  O O    . ASN   A 1 120 ? -21.978 18.324 41.095 1.00 39.57  ? 926  ASN   A O    1 
ATOM   895  C CB   . ASN   A 1 120 ? -23.081 15.964 41.703 1.00 52.39  ? 926  ASN   A CB   1 
ATOM   896  C CG   . ASN   A 1 120 ? -21.738 15.337 41.460 1.00 55.49  ? 926  ASN   A CG   1 
ATOM   897  O OD1  . ASN   A 1 120 ? -21.328 15.209 40.296 1.00 53.22  ? 926  ASN   A OD1  1 
ATOM   898  N ND2  . ASN   A 1 120 ? -21.034 14.953 42.530 1.00 56.79  ? 926  ASN   A ND2  1 
ATOM   899  N N    . ALA   A 1 121 ? -23.122 18.685 39.173 1.00 37.23  ? 927  ALA   A N    1 
ATOM   900  C CA   . ALA   A 1 121 ? -22.305 19.829 38.776 1.00 39.95  ? 927  ALA   A CA   1 
ATOM   901  C C    . ALA   A 1 121 ? -22.273 20.901 39.864 1.00 38.60  ? 927  ALA   A C    1 
ATOM   902  O O    . ALA   A 1 121 ? -21.203 21.429 40.201 1.00 39.70  ? 927  ALA   A O    1 
ATOM   903  C CB   . ALA   A 1 121 ? -22.812 20.405 37.446 1.00 35.75  ? 927  ALA   A CB   1 
ATOM   904  N N    . HIS   A 1 122 ? -23.437 21.236 40.433 1.00 36.60  ? 928  HIS   A N    1 
ATOM   905  C CA   . HIS   A 1 122 ? -23.481 22.248 41.484 1.00 31.04  ? 928  HIS   A CA   1 
ATOM   906  C C    . HIS   A 1 122 ? -22.614 21.853 42.678 1.00 38.71  ? 928  HIS   A C    1 
ATOM   907  O O    . HIS   A 1 122 ? -21.927 22.701 43.269 1.00 35.89  ? 928  HIS   A O    1 
ATOM   908  C CB   . HIS   A 1 122 ? -24.923 22.480 41.921 1.00 31.89  ? 928  HIS   A CB   1 
ATOM   909  C CG   . HIS   A 1 122 ? -25.780 23.106 40.871 1.00 30.93  ? 928  HIS   A CG   1 
ATOM   910  N ND1  . HIS   A 1 122 ? -25.406 24.239 40.183 1.00 32.03  ? 928  HIS   A ND1  1 
ATOM   911  C CD2  . HIS   A 1 122 ? -26.992 22.753 40.383 1.00 32.49  ? 928  HIS   A CD2  1 
ATOM   912  C CE1  . HIS   A 1 122 ? -26.353 24.562 39.320 1.00 33.45  ? 928  HIS   A CE1  1 
ATOM   913  N NE2  . HIS   A 1 122 ? -27.326 23.673 39.418 1.00 34.90  ? 928  HIS   A NE2  1 
ATOM   914  N N    . GLU   A 1 123 ? -22.643 20.576 43.067 1.00 38.98  ? 929  GLU   A N    1 
ATOM   915  C CA   . GLU   A 1 123 ? -21.789 20.156 44.169 1.00 37.04  ? 929  GLU   A CA   1 
ATOM   916  C C    . GLU   A 1 123 ? -20.328 20.320 43.792 1.00 36.97  ? 929  GLU   A C    1 
ATOM   917  O O    . GLU   A 1 123 ? -19.515 20.797 44.598 1.00 38.86  ? 929  GLU   A O    1 
ATOM   918  C CB   . GLU   A 1 123 ? -22.080 18.706 44.556 1.00 41.77  ? 929  GLU   A CB   1 
ATOM   919  C CG   . GLU   A 1 123 ? -23.532 18.420 44.819 1.00 44.88  ? 929  GLU   A CG   1 
ATOM   920  C CD   . GLU   A 1 123 ? -23.778 16.991 45.265 1.00 56.72  ? 929  GLU   A CD   1 
ATOM   921  O OE1  . GLU   A 1 123 ? -23.010 16.095 44.842 1.00 61.71  ? 929  GLU   A OE1  1 
ATOM   922  O OE2  . GLU   A 1 123 ? -24.734 16.764 46.051 1.00 60.57  ? 929  GLU   A OE2  1 
ATOM   923  N N    . GLN   A 1 124 ? -19.977 19.929 42.567 1.00 36.99  ? 930  GLN   A N    1 
ATOM   924  C CA   . GLN   A 1 124 ? -18.616 20.142 42.084 1.00 39.11  ? 930  GLN   A CA   1 
ATOM   925  C C    . GLN   A 1 124 ? -18.231 21.615 42.155 1.00 35.42  ? 930  GLN   A C    1 
ATOM   926  O O    . GLN   A 1 124 ? -17.149 21.963 42.641 1.00 36.69  ? 930  GLN   A O    1 
ATOM   927  C CB   . GLN   A 1 124 ? -18.493 19.631 40.655 1.00 38.18  ? 930  GLN   A CB   1 
ATOM   928  C CG   . GLN   A 1 124 ? -18.494 18.139 40.518 1.00 38.50  ? 930  GLN   A CG   1 
ATOM   929  C CD   . GLN   A 1 124 ? -18.383 17.752 39.062 1.00 39.89  ? 930  GLN   A CD   1 
ATOM   930  O OE1  . GLN   A 1 124 ? -17.332 17.943 38.455 1.00 41.52  ? 930  GLN   A OE1  1 
ATOM   931  N NE2  . GLN   A 1 124 ? -19.475 17.251 38.479 1.00 36.00  ? 930  GLN   A NE2  1 
ATOM   932  N N    . ALA   A 1 125 ? -19.110 22.490 41.662 1.00 31.90  ? 931  ALA   A N    1 
ATOM   933  C CA   . ALA   A 1 125 ? -18.832 23.922 41.645 1.00 32.66  ? 931  ALA   A CA   1 
ATOM   934  C C    . ALA   A 1 125 ? -18.601 24.470 43.050 1.00 40.50  ? 931  ALA   A C    1 
ATOM   935  O O    . ALA   A 1 125 ? -17.713 25.310 43.269 1.00 36.91  ? 931  ALA   A O    1 
ATOM   936  C CB   . ALA   A 1 125 ? -19.987 24.659 40.974 1.00 27.59  ? 931  ALA   A CB   1 
ATOM   937  N N    . LEU   A 1 126 ? -19.408 24.033 44.015 1.00 39.45  ? 932  LEU   A N    1 
ATOM   938  C CA   . LEU   A 1 126 ? -19.261 24.564 45.356 1.00 33.76  ? 932  LEU   A CA   1 
ATOM   939  C C    . LEU   A 1 126 ? -18.026 23.988 46.024 1.00 34.93  ? 932  LEU   A C    1 
ATOM   940  O O    . LEU   A 1 126 ? -17.279 24.716 46.678 1.00 36.19  ? 932  LEU   A O    1 
ATOM   941  C CB   . LEU   A 1 126 ? -20.530 24.295 46.162 1.00 33.39  ? 932  LEU   A CB   1 
ATOM   942  C CG   . LEU   A 1 126 ? -21.778 25.027 45.641 1.00 36.33  ? 932  LEU   A CG   1 
ATOM   943  C CD1  . LEU   A 1 126 ? -23.084 24.355 46.078 1.00 34.13  ? 932  LEU   A CD1  1 
ATOM   944  C CD2  . LEU   A 1 126 ? -21.777 26.509 46.022 1.00 30.67  ? 932  LEU   A CD2  1 
ATOM   945  N N    . GLU   A 1 127 ? -17.773 22.690 45.842 1.00 42.27  ? 933  GLU   A N    1 
ATOM   946  C CA   . GLU   A 1 127 ? -16.562 22.078 46.394 1.00 43.46  ? 933  GLU   A CA   1 
ATOM   947  C C    . GLU   A 1 127 ? -15.306 22.761 45.858 1.00 44.81  ? 933  GLU   A C    1 
ATOM   948  O O    . GLU   A 1 127 ? -14.363 23.021 46.618 1.00 41.71  ? 933  GLU   A O    1 
ATOM   949  C CB   . GLU   A 1 127 ? -16.547 20.577 46.074 1.00 43.24  ? 933  GLU   A CB   1 
ATOM   950  C CG   . GLU   A 1 127 ? -15.229 19.836 46.314 1.00 51.81  ? 933  GLU   A CG   1 
ATOM   951  C CD   . GLU   A 1 127 ? -14.695 19.950 47.759 1.00 67.89  ? 933  GLU   A CD   1 
ATOM   952  O OE1  . GLU   A 1 127 ? -13.509 19.609 48.004 1.00 69.23  ? 933  GLU   A OE1  1 
ATOM   953  O OE2  . GLU   A 1 127 ? -15.449 20.392 48.654 1.00 71.77  ? 933  GLU   A OE2  1 
ATOM   954  N N    . THR   A 1 128 ? -15.297 23.086 44.548 1.00 43.32  ? 934  THR   A N    1 
ATOM   955  C CA   . THR   A 1 128 ? -14.149 23.726 43.900 1.00 40.83  ? 934  THR   A CA   1 
ATOM   956  C C    . THR   A 1 128 ? -13.963 25.161 44.368 1.00 35.56  ? 934  THR   A C    1 
ATOM   957  O O    . THR   A 1 128 ? -12.835 25.645 44.470 1.00 41.67  ? 934  THR   A O    1 
ATOM   958  C CB   . THR   A 1 128 ? -14.322 23.701 42.377 1.00 43.34  ? 934  THR   A CB   1 
ATOM   959  O OG1  . THR   A 1 128 ? -14.434 22.351 41.937 1.00 44.80  ? 934  THR   A OG1  1 
ATOM   960  C CG2  . THR   A 1 128 ? -13.145 24.347 41.669 1.00 37.89  ? 934  THR   A CG2  1 
ATOM   961  N N    . GLY   A 1 129 ? -15.053 25.866 44.631 1.00 39.68  ? 935  GLY   A N    1 
ATOM   962  C CA   . GLY   A 1 129 ? -14.962 27.219 45.134 1.00 38.12  ? 935  GLY   A CA   1 
ATOM   963  C C    . GLY   A 1 129 ? -14.936 28.299 44.079 1.00 36.89  ? 935  GLY   A C    1 
ATOM   964  O O    . GLY   A 1 129 ? -14.275 29.323 44.282 1.00 37.52  ? 935  GLY   A O    1 
ATOM   965  N N    . VAL   A 1 130 ? -15.632 28.110 42.964 1.00 32.48  ? 936  VAL   A N    1 
ATOM   966  C CA   . VAL   A 1 130 ? -15.643 29.105 41.900 1.00 34.01  ? 936  VAL   A CA   1 
ATOM   967  C C    . VAL   A 1 130 ? -16.579 30.236 42.283 1.00 30.39  ? 936  VAL   A C    1 
ATOM   968  O O    . VAL   A 1 130 ? -17.566 30.042 42.988 1.00 30.41  ? 936  VAL   A O    1 
ATOM   969  C CB   . VAL   A 1 130 ? -16.050 28.481 40.548 1.00 31.49  ? 936  VAL   A CB   1 
ATOM   970  C CG1  . VAL   A 1 130 ? -15.119 27.334 40.199 1.00 30.16  ? 936  VAL   A CG1  1 
ATOM   971  C CG2  . VAL   A 1 130 ? -17.523 28.039 40.564 1.00 27.40  ? 936  VAL   A CG2  1 
ATOM   972  N N    . THR   A 1 131 ? -16.290 31.432 41.801 1.00 32.37  ? 937  THR   A N    1 
ATOM   973  C CA   . THR   A 1 131 ? -17.204 32.528 42.049 1.00 29.95  ? 937  THR   A CA   1 
ATOM   974  C C    . THR   A 1 131 ? -18.123 32.771 40.872 1.00 31.02  ? 937  THR   A C    1 
ATOM   975  O O    . THR   A 1 131 ? -19.063 33.562 40.982 1.00 36.23  ? 937  THR   A O    1 
ATOM   976  C CB   . THR   A 1 131 ? -16.428 33.792 42.405 1.00 31.46  ? 937  THR   A CB   1 
ATOM   977  O OG1  . THR   A 1 131 ? -15.777 34.311 41.245 1.00 32.10  ? 937  THR   A OG1  1 
ATOM   978  C CG2  . THR   A 1 131 ? -15.393 33.462 43.450 1.00 32.08  ? 937  THR   A CG2  1 
ATOM   979  N N    . VAL   A 1 132 ? -17.910 32.059 39.779 1.00 29.37  ? 938  VAL   A N    1 
ATOM   980  C CA   . VAL   A 1 132 ? -18.760 32.133 38.603 1.00 29.14  ? 938  VAL   A CA   1 
ATOM   981  C C    . VAL   A 1 132 ? -19.028 30.713 38.120 1.00 29.00  ? 938  VAL   A C    1 
ATOM   982  O O    . VAL   A 1 132 ? -18.095 29.921 37.947 1.00 31.07  ? 938  VAL   A O    1 
ATOM   983  C CB   . VAL   A 1 132 ? -18.088 32.970 37.495 1.00 28.52  ? 938  VAL   A CB   1 
ATOM   984  C CG1  . VAL   A 1 132 ? -18.775 32.748 36.153 1.00 26.62  ? 938  VAL   A CG1  1 
ATOM   985  C CG2  . VAL   A 1 132 ? -18.074 34.421 37.892 1.00 28.61  ? 938  VAL   A CG2  1 
ATOM   986  N N    . THR   A 1 133 ? -20.295 30.387 37.916 1.00 24.31  ? 939  THR   A N    1 
ATOM   987  C CA   . THR   A 1 133 ? -20.646 29.146 37.247 1.00 24.77  ? 939  THR   A CA   1 
ATOM   988  C C    . THR   A 1 133 ? -21.680 29.504 36.193 1.00 24.82  ? 939  THR   A C    1 
ATOM   989  O O    . THR   A 1 133 ? -21.674 30.625 35.690 1.00 25.53  ? 939  THR   A O    1 
ATOM   990  C CB   . THR   A 1 133 ? -21.135 28.084 38.262 1.00 28.04  ? 939  THR   A CB   1 
ATOM   991  O OG1  . THR   A 1 133 ? -21.405 26.855 37.588 1.00 25.82  ? 939  THR   A OG1  1 
ATOM   992  C CG2  . THR   A 1 133 ? -22.373 28.522 39.042 1.00 23.92  ? 939  THR   A CG2  1 
ATOM   993  N N    . GLY   A 1 134 ? -22.579 28.601 35.845 1.00 28.21  ? 940  GLY   A N    1 
ATOM   994  C CA   . GLY   A 1 134 ? -23.529 28.935 34.802 1.00 28.32  ? 940  GLY   A CA   1 
ATOM   995  C C    . GLY   A 1 134 ? -24.141 27.670 34.240 1.00 29.87  ? 940  GLY   A C    1 
ATOM   996  O O    . GLY   A 1 134 ? -24.141 26.630 34.888 1.00 30.16  ? 940  GLY   A O    1 
ATOM   997  N N    . CYS   A 1 135 ? -24.655 27.784 33.025 1.00 29.92  ? 941  CYS   A N    1 
ATOM   998  C CA   . CYS   A 1 135 ? -25.210 26.621 32.362 1.00 30.65  ? 941  CYS   A CA   1 
ATOM   999  C C    . CYS   A 1 135 ? -24.811 26.626 30.887 1.00 31.34  ? 941  CYS   A C    1 
ATOM   1000 O O    . CYS   A 1 135 ? -24.364 27.635 30.332 1.00 28.65  ? 941  CYS   A O    1 
ATOM   1001 C CB   . CYS   A 1 135 ? -26.726 26.578 32.526 1.00 28.06  ? 941  CYS   A CB   1 
ATOM   1002 S SG   . CYS   A 1 135 ? -27.482 28.137 32.080 1.00 29.48  ? 941  CYS   A SG   1 
ATOM   1003 N N    . THR   A 1 136 ? -24.992 25.472 30.264 1.00 29.80  ? 942  THR   A N    1 
ATOM   1004 C CA   . THR   A 1 136 ? -24.621 25.243 28.882 1.00 32.61  ? 942  THR   A CA   1 
ATOM   1005 C C    . THR   A 1 136 ? -25.739 24.498 28.160 1.00 33.59  ? 942  THR   A C    1 
ATOM   1006 O O    . THR   A 1 136 ? -26.313 23.544 28.698 1.00 33.26  ? 942  THR   A O    1 
ATOM   1007 C CB   . THR   A 1 136 ? -23.320 24.430 28.806 1.00 31.41  ? 942  THR   A CB   1 
ATOM   1008 O OG1  . THR   A 1 136 ? -22.302 25.095 29.566 1.00 31.00  ? 942  THR   A OG1  1 
ATOM   1009 C CG2  . THR   A 1 136 ? -22.860 24.298 27.356 1.00 30.65  ? 942  THR   A CG2  1 
ATOM   1010 N N    . VAL   A 1 137 ? -26.055 24.935 26.945 1.00 28.59  ? 943  VAL   A N    1 
ATOM   1011 C CA   . VAL   A 1 137 ? -26.815 24.124 26.005 1.00 30.05  ? 943  VAL   A CA   1 
ATOM   1012 C C    . VAL   A 1 137 ? -25.830 23.641 24.959 1.00 32.69  ? 943  VAL   A C    1 
ATOM   1013 O O    . VAL   A 1 137 ? -25.035 24.429 24.433 1.00 31.10  ? 943  VAL   A O    1 
ATOM   1014 C CB   . VAL   A 1 137 ? -27.995 24.881 25.363 1.00 30.76  ? 943  VAL   A CB   1 
ATOM   1015 C CG1  . VAL   A 1 137 ? -28.717 23.977 24.357 1.00 27.58  ? 943  VAL   A CG1  1 
ATOM   1016 C CG2  . VAL   A 1 137 ? -28.974 25.351 26.422 1.00 26.34  ? 943  VAL   A CG2  1 
ATOM   1017 N N    . HIS   A 1 138 ? -25.861 22.343 24.684 1.00 32.47  ? 944  HIS   A N    1 
ATOM   1018 C CA   . HIS   A 1 138 ? -24.908 21.733 23.784 1.00 31.71  ? 944  HIS   A CA   1 
ATOM   1019 C C    . HIS   A 1 138 ? -25.614 20.613 23.050 1.00 35.60  ? 944  HIS   A C    1 
ATOM   1020 O O    . HIS   A 1 138 ? -26.615 20.069 23.523 1.00 35.23  ? 944  HIS   A O    1 
ATOM   1021 C CB   . HIS   A 1 138 ? -23.679 21.193 24.534 1.00 36.75  ? 944  HIS   A CB   1 
ATOM   1022 C CG   . HIS   A 1 138 ? -23.973 20.033 25.442 1.00 37.95  ? 944  HIS   A CG   1 
ATOM   1023 N ND1  . HIS   A 1 138 ? -23.695 18.728 25.098 1.00 37.68  ? 944  HIS   A ND1  1 
ATOM   1024 C CD2  . HIS   A 1 138 ? -24.507 19.985 26.687 1.00 38.02  ? 944  HIS   A CD2  1 
ATOM   1025 C CE1  . HIS   A 1 138 ? -24.055 17.925 26.083 1.00 38.13  ? 944  HIS   A CE1  1 
ATOM   1026 N NE2  . HIS   A 1 138 ? -24.554 18.662 27.058 1.00 38.51  ? 944  HIS   A NE2  1 
ATOM   1027 N N    . PHE   A 1 139 ? -25.087 20.287 21.877 1.00 35.43  ? 945  PHE   A N    1 
ATOM   1028 C CA   . PHE   A 1 139 ? -25.516 19.089 21.178 1.00 35.60  ? 945  PHE   A CA   1 
ATOM   1029 C C    . PHE   A 1 139 ? -25.019 17.852 21.919 1.00 36.94  ? 945  PHE   A C    1 
ATOM   1030 O O    . PHE   A 1 139 ? -23.921 17.843 22.475 1.00 39.54  ? 945  PHE   A O    1 
ATOM   1031 C CB   . PHE   A 1 139 ? -24.976 19.103 19.750 1.00 38.20  ? 945  PHE   A CB   1 
ATOM   1032 C CG   . PHE   A 1 139 ? -25.712 20.019 18.824 1.00 35.24  ? 945  PHE   A CG   1 
ATOM   1033 C CD1  . PHE   A 1 139 ? -27.005 19.729 18.422 1.00 38.65  ? 945  PHE   A CD1  1 
ATOM   1034 C CD2  . PHE   A 1 139 ? -25.101 21.153 18.323 1.00 36.95  ? 945  PHE   A CD2  1 
ATOM   1035 C CE1  . PHE   A 1 139 ? -27.680 20.567 17.545 1.00 37.34  ? 945  PHE   A CE1  1 
ATOM   1036 C CE2  . PHE   A 1 139 ? -25.775 22.003 17.458 1.00 37.23  ? 945  PHE   A CE2  1 
ATOM   1037 C CZ   . PHE   A 1 139 ? -27.056 21.712 17.068 1.00 36.25  ? 945  PHE   A CZ   1 
ATOM   1038 N N    . VAL   A 1 140 ? -25.817 16.794 21.920 1.00 38.20  ? 946  VAL   A N    1 
ATOM   1039 C CA   . VAL   A 1 140 ? -25.398 15.558 22.568 1.00 39.21  ? 946  VAL   A CA   1 
ATOM   1040 C C    . VAL   A 1 140 ? -24.479 14.778 21.633 1.00 42.57  ? 946  VAL   A C    1 
ATOM   1041 O O    . VAL   A 1 140 ? -24.868 14.391 20.528 1.00 43.59  ? 946  VAL   A O    1 
ATOM   1042 C CB   . VAL   A 1 140 ? -26.607 14.719 22.985 1.00 40.37  ? 946  VAL   A CB   1 
ATOM   1043 C CG1  . VAL   A 1 140 ? -26.142 13.402 23.560 1.00 38.43  ? 946  VAL   A CG1  1 
ATOM   1044 C CG2  . VAL   A 1 140 ? -27.464 15.502 23.982 1.00 37.58  ? 946  VAL   A CG2  1 
ATOM   1045 N N    . ALA   A 1 141 ? -23.250 14.566 22.067 1.00 48.05  ? 947  ALA   A N    1 
ATOM   1046 C CA   . ALA   A 1 141 ? -22.307 13.656 21.441 1.00 45.54  ? 947  ALA   A CA   1 
ATOM   1047 C C    . ALA   A 1 141 ? -22.174 12.406 22.319 1.00 49.09  ? 947  ALA   A C    1 
ATOM   1048 O O    . ALA   A 1 141 ? -22.759 12.310 23.399 1.00 50.60  ? 947  ALA   A O    1 
ATOM   1049 C CB   . ALA   A 1 141 ? -20.973 14.363 21.228 1.00 47.16  ? 947  ALA   A CB   1 
ATOM   1050 N N    . GLU   A 1 142 ? -21.411 11.419 21.854 1.00 53.05  ? 948  GLU   A N    1 
ATOM   1051 C CA   . GLU   A 1 142 ? -21.323 10.179 22.622 1.00 57.67  ? 948  GLU   A CA   1 
ATOM   1052 C C    . GLU   A 1 142 ? -20.672 10.416 23.985 1.00 61.79  ? 948  GLU   A C    1 
ATOM   1053 O O    . GLU   A 1 142 ? -21.205 9.994  25.020 1.00 58.76  ? 948  GLU   A O    1 
ATOM   1054 C CB   . GLU   A 1 142 ? -20.589 9.108  21.820 1.00 58.29  ? 948  GLU   A CB   1 
ATOM   1055 C CG   . GLU   A 1 142 ? -21.548 8.303  20.975 1.00 61.43  ? 948  GLU   A CG   1 
ATOM   1056 C CD   . GLU   A 1 142 ? -20.888 7.153  20.225 1.00 76.75  ? 948  GLU   A CD   1 
ATOM   1057 O OE1  . GLU   A 1 142 ? -20.949 7.132  18.967 1.00 78.23  ? 948  GLU   A OE1  1 
ATOM   1058 O OE2  . GLU   A 1 142 ? -20.308 6.269  20.896 1.00 80.89  ? 948  GLU   A OE2  1 
ATOM   1059 N N    . ASP   A 1 143 ? -19.539 11.115 24.015 1.00 65.42  ? 949  ASP   A N    1 
ATOM   1060 C CA   . ASP   A 1 143 ? -18.914 11.471 25.288 1.00 67.50  ? 949  ASP   A CA   1 
ATOM   1061 C C    . ASP   A 1 143 ? -19.784 12.477 26.039 1.00 62.78  ? 949  ASP   A C    1 
ATOM   1062 O O    . ASP   A 1 143 ? -20.084 13.555 25.518 1.00 62.46  ? 949  ASP   A O    1 
ATOM   1063 C CB   . ASP   A 1 143 ? -17.519 12.038 25.049 1.00 74.36  ? 949  ASP   A CB   1 
ATOM   1064 C CG   . ASP   A 1 143 ? -16.571 11.002 24.488 1.00 83.12  ? 949  ASP   A CG   1 
ATOM   1065 O OD1  . ASP   A 1 143 ? -16.368 9.968  25.161 1.00 82.52  ? 949  ASP   A OD1  1 
ATOM   1066 O OD2  . ASP   A 1 143 ? -16.047 11.208 23.368 1.00 90.88  ? 949  ASP   A OD2  1 
ATOM   1067 N N    . VAL   A 1 144 ? -20.165 12.134 27.273 1.00 55.36  ? 950  VAL   A N    1 
ATOM   1068 C CA   . VAL   A 1 144 ? -21.196 12.884 27.987 1.00 57.05  ? 950  VAL   A CA   1 
ATOM   1069 C C    . VAL   A 1 144 ? -20.717 14.307 28.274 1.00 59.44  ? 950  VAL   A C    1 
ATOM   1070 O O    . VAL   A 1 144 ? -19.537 14.539 28.580 1.00 58.97  ? 950  VAL   A O    1 
ATOM   1071 C CB   . VAL   A 1 144 ? -21.598 12.139 29.277 1.00 55.87  ? 950  VAL   A CB   1 
ATOM   1072 C CG1  . VAL   A 1 144 ? -22.613 12.939 30.094 1.00 52.96  ? 950  VAL   A CG1  1 
ATOM   1073 C CG2  . VAL   A 1 144 ? -22.171 10.773 28.938 1.00 52.44  ? 950  VAL   A CG2  1 
ATOM   1074 N N    . ASP   A 1 145 ? -21.642 15.273 28.172 1.00 54.01  ? 951  ASP   A N    1 
ATOM   1075 C CA   . ASP   A 1 145 ? -21.342 16.704 28.321 1.00 51.83  ? 951  ASP   A CA   1 
ATOM   1076 C C    . ASP   A 1 145 ? -20.095 17.107 27.534 1.00 52.56  ? 951  ASP   A C    1 
ATOM   1077 O O    . ASP   A 1 145 ? -19.227 17.830 28.030 1.00 51.83  ? 951  ASP   A O    1 
ATOM   1078 C CB   . ASP   A 1 145 ? -21.195 17.088 29.793 1.00 47.16  ? 951  ASP   A CB   1 
ATOM   1079 C CG   . ASP   A 1 145 ? -22.310 16.536 30.655 1.00 50.62  ? 951  ASP   A CG   1 
ATOM   1080 O OD1  . ASP   A 1 145 ? -23.493 16.604 30.230 1.00 49.63  ? 951  ASP   A OD1  1 
ATOM   1081 O OD2  . ASP   A 1 145 ? -21.996 16.033 31.762 1.00 49.19  ? 951  ASP   A OD2  1 
ATOM   1082 N N    . ALA   A 1 146 ? -20.008 16.644 26.283 1.00 61.92  ? 952  ALA   A N    1 
ATOM   1083 C CA   . ALA   A 1 146 ? -18.819 16.895 25.475 1.00 63.37  ? 952  ALA   A CA   1 
ATOM   1084 C C    . ALA   A 1 146 ? -19.151 17.258 24.030 1.00 62.11  ? 952  ALA   A C    1 
ATOM   1085 O O    . ALA   A 1 146 ? -18.227 17.394 23.215 1.00 64.22  ? 952  ALA   A O    1 
ATOM   1086 C CB   . ALA   A 1 146 ? -17.873 15.680 25.517 1.00 61.21  ? 952  ALA   A CB   1 
ATOM   1087 N N    . GLY   A 1 147 ? -20.426 17.439 23.685 1.00 50.62  ? 953  GLY   A N    1 
ATOM   1088 C CA   . GLY   A 1 147 ? -20.794 17.839 22.343 1.00 48.72  ? 953  GLY   A CA   1 
ATOM   1089 C C    . GLY   A 1 147 ? -20.543 19.311 22.088 1.00 42.11  ? 953  GLY   A C    1 
ATOM   1090 O O    . GLY   A 1 147 ? -20.102 20.055 22.958 1.00 47.68  ? 953  GLY   A O    1 
ATOM   1091 N N    . GLN   A 1 148 ? -20.848 19.739 20.861 1.00 44.37  ? 954  GLN   A N    1 
ATOM   1092 C CA   . GLN   A 1 148 ? -20.665 21.138 20.492 1.00 40.29  ? 954  GLN   A CA   1 
ATOM   1093 C C    . GLN   A 1 148 ? -21.579 22.059 21.303 1.00 39.34  ? 954  GLN   A C    1 
ATOM   1094 O O    . GLN   A 1 148 ? -22.791 21.833 21.421 1.00 36.30  ? 954  GLN   A O    1 
ATOM   1095 C CB   . GLN   A 1 148 ? -20.901 21.329 18.999 1.00 44.55  ? 954  GLN   A CB   1 
ATOM   1096 C CG   . GLN   A 1 148 ? -19.697 20.969 18.146 1.00 55.00  ? 954  GLN   A CG   1 
ATOM   1097 C CD   . GLN   A 1 148 ? -18.452 21.794 18.499 1.00 60.78  ? 954  GLN   A CD   1 
ATOM   1098 O OE1  . GLN   A 1 148 ? -17.337 21.272 18.519 1.00 57.46  ? 954  GLN   A OE1  1 
ATOM   1099 N NE2  . GLN   A 1 148 ? -18.644 23.083 18.787 1.00 61.13  ? 954  GLN   A NE2  1 
ATOM   1100 N N    . ILE   A 1 149 ? -20.985 23.106 21.856 1.00 39.34  ? 955  ILE   A N    1 
ATOM   1101 C CA   . ILE   A 1 149 ? -21.692 24.035 22.725 1.00 33.44  ? 955  ILE   A CA   1 
ATOM   1102 C C    . ILE   A 1 149 ? -22.497 24.996 21.867 1.00 30.63  ? 955  ILE   A C    1 
ATOM   1103 O O    . ILE   A 1 149 ? -21.977 25.567 20.904 1.00 35.72  ? 955  ILE   A O    1 
ATOM   1104 C CB   . ILE   A 1 149 ? -20.697 24.793 23.625 1.00 35.24  ? 955  ILE   A CB   1 
ATOM   1105 C CG1  . ILE   A 1 149 ? -20.127 23.870 24.705 1.00 33.76  ? 955  ILE   A CG1  1 
ATOM   1106 C CG2  . ILE   A 1 149 ? -21.326 26.071 24.226 1.00 30.80  ? 955  ILE   A CG2  1 
ATOM   1107 C CD1  . ILE   A 1 149 ? -18.693 24.181 25.088 1.00 31.13  ? 955  ILE   A CD1  1 
ATOM   1108 N N    . ILE   A 1 150 ? -23.753 25.216 22.243 1.00 33.94  ? 956  ILE   A N    1 
ATOM   1109 C CA   . ILE   A 1 150 ? -24.624 26.143 21.528 1.00 30.07  ? 956  ILE   A CA   1 
ATOM   1110 C C    . ILE   A 1 150 ? -24.706 27.487 22.252 1.00 31.13  ? 956  ILE   A C    1 
ATOM   1111 O O    . ILE   A 1 150 ? -24.406 28.530 21.663 1.00 33.17  ? 956  ILE   A O    1 
ATOM   1112 C CB   . ILE   A 1 150 ? -26.012 25.512 21.324 1.00 31.20  ? 956  ILE   A CB   1 
ATOM   1113 C CG1  . ILE   A 1 150 ? -25.863 24.213 20.525 1.00 32.41  ? 956  ILE   A CG1  1 
ATOM   1114 C CG2  . ILE   A 1 150 ? -26.944 26.475 20.591 1.00 31.77  ? 956  ILE   A CG2  1 
ATOM   1115 C CD1  . ILE   A 1 150 ? -27.096 23.340 20.483 1.00 33.98  ? 956  ILE   A CD1  1 
ATOM   1116 N N    . LEU   A 1 151 ? -25.102 27.489 23.523 1.00 29.76  ? 957  LEU   A N    1 
ATOM   1117 C CA   . LEU   A 1 151 ? -25.126 28.720 24.314 1.00 32.37  ? 957  LEU   A CA   1 
ATOM   1118 C C    . LEU   A 1 151 ? -24.685 28.423 25.736 1.00 29.77  ? 957  LEU   A C    1 
ATOM   1119 O O    . LEU   A 1 151 ? -24.740 27.287 26.211 1.00 30.75  ? 957  LEU   A O    1 
ATOM   1120 C CB   . LEU   A 1 151 ? -26.515 29.394 24.388 1.00 31.37  ? 957  LEU   A CB   1 
ATOM   1121 C CG   . LEU   A 1 151 ? -27.286 29.822 23.142 1.00 30.19  ? 957  LEU   A CG   1 
ATOM   1122 C CD1  . LEU   A 1 151 ? -28.496 30.632 23.535 1.00 27.26  ? 957  LEU   A CD1  1 
ATOM   1123 C CD2  . LEU   A 1 151 ? -26.409 30.606 22.201 1.00 26.35  ? 957  LEU   A CD2  1 
ATOM   1124 N N    . GLN   A 1 152 ? -24.260 29.477 26.416 1.00 29.69  ? 958  GLN   A N    1 
ATOM   1125 C CA   . GLN   A 1 152 ? -23.893 29.411 27.819 1.00 29.38  ? 958  GLN   A CA   1 
ATOM   1126 C C    . GLN   A 1 152 ? -24.290 30.730 28.460 1.00 31.89  ? 958  GLN   A C    1 
ATOM   1127 O O    . GLN   A 1 152 ? -24.302 31.771 27.791 1.00 30.44  ? 958  GLN   A O    1 
ATOM   1128 C CB   . GLN   A 1 152 ? -22.396 29.157 27.993 1.00 29.01  ? 958  GLN   A CB   1 
ATOM   1129 C CG   . GLN   A 1 152 ? -21.936 27.861 27.422 1.00 26.86  ? 958  GLN   A CG   1 
ATOM   1130 C CD   . GLN   A 1 152 ? -20.435 27.703 27.503 1.00 31.31  ? 958  GLN   A CD   1 
ATOM   1131 O OE1  . GLN   A 1 152 ? -19.684 28.459 26.863 1.00 31.99  ? 958  GLN   A OE1  1 
ATOM   1132 N NE2  . GLN   A 1 152 ? -19.977 26.708 28.286 1.00 27.61  ? 958  GLN   A NE2  1 
ATOM   1133 N N    . GLU   A 1 153 ? -24.628 30.686 29.750 1.00 28.57  ? 959  GLU   A N    1 
ATOM   1134 C CA   . GLU   A 1 153 ? -24.800 31.927 30.497 1.00 29.17  ? 959  GLU   A CA   1 
ATOM   1135 C C    . GLU   A 1 153 ? -24.129 31.834 31.862 1.00 29.74  ? 959  GLU   A C    1 
ATOM   1136 O O    . GLU   A 1 153 ? -24.342 30.883 32.621 1.00 28.00  ? 959  GLU   A O    1 
ATOM   1137 C CB   . GLU   A 1 153 ? -26.273 32.294 30.659 1.00 29.73  ? 959  GLU   A CB   1 
ATOM   1138 C CG   . GLU   A 1 153 ? -26.478 33.592 31.430 1.00 30.84  ? 959  GLU   A CG   1 
ATOM   1139 C CD   . GLU   A 1 153 ? -27.959 33.980 31.552 1.00 41.66  ? 959  GLU   A CD   1 
ATOM   1140 O OE1  . GLU   A 1 153 ? -28.788 33.511 30.725 1.00 43.70  ? 959  GLU   A OE1  1 
ATOM   1141 O OE2  . GLU   A 1 153 ? -28.296 34.767 32.466 1.00 44.29  ? 959  GLU   A OE2  1 
ATOM   1142 N N    . ALA   A 1 154 ? -23.302 32.825 32.157 1.00 33.15  ? 960  ALA   A N    1 
ATOM   1143 C CA   . ALA   A 1 154 ? -22.606 32.848 33.427 1.00 28.17  ? 960  ALA   A CA   1 
ATOM   1144 C C    . ALA   A 1 154 ? -23.581 33.227 34.533 1.00 29.46  ? 960  ALA   A C    1 
ATOM   1145 O O    . ALA   A 1 154 ? -24.478 34.053 34.330 1.00 25.95  ? 960  ALA   A O    1 
ATOM   1146 C CB   . ALA   A 1 154 ? -21.441 33.826 33.365 1.00 22.90  ? 960  ALA   A CB   1 
ATOM   1147 N N    . VAL   A 1 155 ? -23.405 32.606 35.701 1.00 27.24  ? 961  VAL   A N    1 
ATOM   1148 C CA   . VAL   A 1 155 ? -24.223 32.886 36.874 1.00 26.60  ? 961  VAL   A CA   1 
ATOM   1149 C C    . VAL   A 1 155 ? -23.313 32.986 38.093 1.00 29.32  ? 961  VAL   A C    1 
ATOM   1150 O O    . VAL   A 1 155 ? -22.471 32.099 38.310 1.00 29.51  ? 961  VAL   A O    1 
ATOM   1151 C CB   . VAL   A 1 155 ? -25.303 31.807 37.057 1.00 30.00  ? 961  VAL   A CB   1 
ATOM   1152 C CG1  . VAL   A 1 155 ? -26.054 32.021 38.357 1.00 28.42  ? 961  VAL   A CG1  1 
ATOM   1153 C CG2  . VAL   A 1 155 ? -26.255 31.830 35.875 1.00 28.42  ? 961  VAL   A CG2  1 
ATOM   1154 N N    . PRO   A 1 156 ? -23.437 34.032 38.911 1.00 29.10  ? 962  PRO   A N    1 
ATOM   1155 C CA   . PRO   A 1 156 ? -22.539 34.172 40.070 1.00 29.10  ? 962  PRO   A CA   1 
ATOM   1156 C C    . PRO   A 1 156 ? -22.821 33.133 41.138 1.00 30.51  ? 962  PRO   A C    1 
ATOM   1157 O O    . PRO   A 1 156 ? -23.975 32.787 41.409 1.00 30.74  ? 962  PRO   A O    1 
ATOM   1158 C CB   . PRO   A 1 156 ? -22.854 35.572 40.598 1.00 26.72  ? 962  PRO   A CB   1 
ATOM   1159 C CG   . PRO   A 1 156 ? -24.270 35.786 40.206 1.00 25.83  ? 962  PRO   A CG   1 
ATOM   1160 C CD   . PRO   A 1 156 ? -24.438 35.107 38.859 1.00 23.49  ? 962  PRO   A CD   1 
ATOM   1161 N N    . VAL   A 1 157 ? -21.757 32.663 41.771 1.00 30.29  ? 963  VAL   A N    1 
ATOM   1162 C CA   . VAL   A 1 157 ? -21.881 31.921 43.015 1.00 34.79  ? 963  VAL   A CA   1 
ATOM   1163 C C    . VAL   A 1 157 ? -21.824 32.920 44.162 1.00 33.32  ? 963  VAL   A C    1 
ATOM   1164 O O    . VAL   A 1 157 ? -20.896 33.731 44.245 1.00 33.51  ? 963  VAL   A O    1 
ATOM   1165 C CB   . VAL   A 1 157 ? -20.773 30.866 43.144 1.00 32.33  ? 963  VAL   A CB   1 
ATOM   1166 C CG1  . VAL   A 1 157 ? -20.873 30.174 44.506 1.00 26.59  ? 963  VAL   A CG1  1 
ATOM   1167 C CG2  . VAL   A 1 157 ? -20.861 29.878 42.005 1.00 26.29  ? 963  VAL   A CG2  1 
ATOM   1168 N N    . LYS   A 1 158 ? -22.805 32.867 45.048 1.00 32.85  ? 964  LYS   A N    1 
ATOM   1169 C CA   . LYS   A 1 158 ? -22.847 33.792 46.168 1.00 34.25  ? 964  LYS   A CA   1 
ATOM   1170 C C    . LYS   A 1 158 ? -22.435 33.087 47.453 1.00 37.93  ? 964  LYS   A C    1 
ATOM   1171 O O    . LYS   A 1 158 ? -22.607 31.874 47.598 1.00 37.49  ? 964  LYS   A O    1 
ATOM   1172 C CB   . LYS   A 1 158 ? -24.235 34.433 46.279 1.00 32.44  ? 964  LYS   A CB   1 
ATOM   1173 C CG   . LYS   A 1 158 ? -24.581 35.175 44.962 1.00 34.97  ? 964  LYS   A CG   1 
ATOM   1174 C CD   . LYS   A 1 158 ? -25.650 36.242 45.108 1.00 37.81  ? 964  LYS   A CD   1 
ATOM   1175 C CE   . LYS   A 1 158 ? -25.791 37.071 43.832 1.00 39.64  ? 964  LYS   A CE   1 
ATOM   1176 N NZ   . LYS   A 1 158 ? -27.117 37.768 43.766 1.00 44.35  ? 964  LYS   A NZ   1 
ATOM   1177 N N    . ARG   A 1 159 ? -21.832 33.859 48.361 1.00 46.73  ? 965  ARG   A N    1 
ATOM   1178 C CA   . ARG   A 1 159 ? -21.366 33.330 49.641 1.00 45.95  ? 965  ARG   A CA   1 
ATOM   1179 C C    . ARG   A 1 159 ? -22.494 32.605 50.356 1.00 42.12  ? 965  ARG   A C    1 
ATOM   1180 O O    . ARG   A 1 159 ? -23.636 33.080 50.387 1.00 39.09  ? 965  ARG   A O    1 
ATOM   1181 C CB   . ARG   A 1 159 ? -20.831 34.459 50.525 1.00 46.86  ? 965  ARG   A CB   1 
ATOM   1182 C CG   . ARG   A 1 159 ? -19.379 34.850 50.227 1.00 58.04  ? 965  ARG   A CG   1 
ATOM   1183 C CD   . ARG   A 1 159 ? -18.632 35.194 51.522 1.00 70.00  ? 965  ARG   A CD   1 
ATOM   1184 N NE   . ARG   A 1 159 ? -18.771 36.605 51.905 1.00 74.61  ? 965  ARG   A NE   1 
ATOM   1185 C CZ   . ARG   A 1 159 ? -18.939 37.039 53.156 1.00 74.53  ? 965  ARG   A CZ   1 
ATOM   1186 N NH1  . ARG   A 1 159 ? -18.991 36.179 54.168 1.00 75.92  ? 965  ARG   A NH1  1 
ATOM   1187 N NH2  . ARG   A 1 159 ? -19.058 38.339 53.396 1.00 76.69  ? 965  ARG   A NH2  1 
ATOM   1188 N N    . GLY   A 1 160 ? -22.164 31.444 50.925 1.00 35.49  ? 966  GLY   A N    1 
ATOM   1189 C CA   . GLY   A 1 160 ? -23.158 30.638 51.600 1.00 35.29  ? 966  GLY   A CA   1 
ATOM   1190 C C    . GLY   A 1 160 ? -24.103 29.887 50.689 1.00 41.77  ? 966  GLY   A C    1 
ATOM   1191 O O    . GLY   A 1 160 ? -25.007 29.209 51.195 1.00 40.43  ? 966  GLY   A O    1 
ATOM   1192 N N    . ASP   A 1 161 ? -23.933 29.993 49.365 1.00 34.73  ? 967  ASP   A N    1 
ATOM   1193 C CA   . ASP   A 1 161 ? -24.721 29.200 48.432 1.00 34.51  ? 967  ASP   A CA   1 
ATOM   1194 C C    . ASP   A 1 161 ? -24.695 27.727 48.816 1.00 33.77  ? 967  ASP   A C    1 
ATOM   1195 O O    . ASP   A 1 161 ? -23.708 27.211 49.339 1.00 35.06  ? 967  ASP   A O    1 
ATOM   1196 C CB   . ASP   A 1 161 ? -24.206 29.369 46.993 1.00 31.84  ? 967  ASP   A CB   1 
ATOM   1197 C CG   . ASP   A 1 161 ? -24.997 30.414 46.191 1.00 33.88  ? 967  ASP   A CG   1 
ATOM   1198 O OD1  . ASP   A 1 161 ? -26.166 30.681 46.560 1.00 32.82  ? 967  ASP   A OD1  1 
ATOM   1199 O OD2  . ASP   A 1 161 ? -24.489 30.908 45.149 1.00 34.14  ? 967  ASP   A OD2  1 
ATOM   1200 N N    . THR   A 1 162 ? -25.804 27.049 48.572 1.00 32.61  ? 968  THR   A N    1 
ATOM   1201 C CA   . THR   A 1 162 ? -25.842 25.597 48.606 1.00 33.56  ? 968  THR   A CA   1 
ATOM   1202 C C    . THR   A 1 162 ? -26.389 25.131 47.274 1.00 34.57  ? 968  THR   A C    1 
ATOM   1203 O O    . THR   A 1 162 ? -26.822 25.936 46.455 1.00 35.51  ? 968  THR   A O    1 
ATOM   1204 C CB   . THR   A 1 162 ? -26.704 25.063 49.754 1.00 34.25  ? 968  THR   A CB   1 
ATOM   1205 O OG1  . THR   A 1 162 ? -28.083 25.375 49.512 1.00 34.98  ? 968  THR   A OG1  1 
ATOM   1206 C CG2  . THR   A 1 162 ? -26.271 25.646 51.064 1.00 34.21  ? 968  THR   A CG2  1 
ATOM   1207 N N    . VAL   A 1 163 ? -26.395 23.816 47.065 1.00 34.03  ? 969  VAL   A N    1 
ATOM   1208 C CA   . VAL   A 1 163 ? -27.006 23.286 45.851 1.00 35.85  ? 969  VAL   A CA   1 
ATOM   1209 C C    . VAL   A 1 163 ? -28.400 23.873 45.649 1.00 33.45  ? 969  VAL   A C    1 
ATOM   1210 O O    . VAL   A 1 163 ? -28.799 24.200 44.525 1.00 33.28  ? 969  VAL   A O    1 
ATOM   1211 C CB   . VAL   A 1 163 ? -27.041 21.748 45.901 1.00 37.09  ? 969  VAL   A CB   1 
ATOM   1212 C CG1  . VAL   A 1 163 ? -27.919 21.207 44.781 1.00 29.48  ? 969  VAL   A CG1  1 
ATOM   1213 C CG2  . VAL   A 1 163 ? -25.625 21.194 45.847 1.00 33.94  ? 969  VAL   A CG2  1 
ATOM   1214 N N    . ALA   A 1 164 ? -29.161 24.014 46.735 1.00 35.96  ? 970  ALA   A N    1 
ATOM   1215 C CA   . ALA   A 1 164 ? -30.499 24.583 46.634 1.00 34.00  ? 970  ALA   A CA   1 
ATOM   1216 C C    . ALA   A 1 164 ? -30.450 25.968 46.001 1.00 34.57  ? 970  ALA   A C    1 
ATOM   1217 O O    . ALA   A 1 164 ? -31.107 26.234 44.983 1.00 32.65  ? 970  ALA   A O    1 
ATOM   1218 C CB   . ALA   A 1 164 ? -31.150 24.641 48.017 1.00 31.34  ? 970  ALA   A CB   1 
ATOM   1219 N N    . THR   A 1 165 ? -29.664 26.866 46.588 1.00 30.35  ? 971  THR   A N    1 
ATOM   1220 C CA   . THR   A 1 165 ? -29.698 28.252 46.141 1.00 30.81  ? 971  THR   A CA   1 
ATOM   1221 C C    . THR   A 1 165 ? -28.930 28.435 44.834 1.00 33.94  ? 971  THR   A C    1 
ATOM   1222 O O    . THR   A 1 165 ? -29.391 29.155 43.935 1.00 31.03  ? 971  THR   A O    1 
ATOM   1223 C CB   . THR   A 1 165 ? -29.166 29.167 47.251 1.00 33.09  ? 971  THR   A CB   1 
ATOM   1224 O OG1  . THR   A 1 165 ? -27.787 28.870 47.535 1.00 28.95  ? 971  THR   A OG1  1 
ATOM   1225 C CG2  . THR   A 1 165 ? -29.988 28.957 48.513 1.00 29.62  ? 971  THR   A CG2  1 
ATOM   1226 N N    . LEU   A 1 166 ? -27.782 27.769 44.684 1.00 33.30  ? 972  LEU   A N    1 
ATOM   1227 C CA   . LEU   A 1 166 ? -27.064 27.850 43.417 1.00 31.57  ? 972  LEU   A CA   1 
ATOM   1228 C C    . LEU   A 1 166 ? -27.946 27.387 42.265 1.00 31.51  ? 972  LEU   A C    1 
ATOM   1229 O O    . LEU   A 1 166 ? -28.089 28.093 41.258 1.00 34.69  ? 972  LEU   A O    1 
ATOM   1230 C CB   . LEU   A 1 166 ? -25.763 27.038 43.471 1.00 31.76  ? 972  LEU   A CB   1 
ATOM   1231 C CG   . LEU   A 1 166 ? -24.806 27.282 42.281 1.00 29.39  ? 972  LEU   A CG   1 
ATOM   1232 C CD1  . LEU   A 1 166 ? -24.627 28.760 42.016 1.00 26.86  ? 972  LEU   A CD1  1 
ATOM   1233 C CD2  . LEU   A 1 166 ? -23.439 26.651 42.500 1.00 29.28  ? 972  LEU   A CD2  1 
ATOM   1234 N N    . SER   A 1 167 ? -28.552 26.204 42.386 1.00 28.64  ? 973  SER   A N    1 
ATOM   1235 C CA   . SER   A 1 167 ? -29.319 25.699 41.253 1.00 32.11  ? 973  SER   A CA   1 
ATOM   1236 C C    . SER   A 1 167 ? -30.592 26.485 41.023 1.00 32.65  ? 973  SER   A C    1 
ATOM   1237 O O    . SER   A 1 167 ? -31.133 26.437 39.924 1.00 33.74  ? 973  SER   A O    1 
ATOM   1238 C CB   . SER   A 1 167 ? -29.673 24.231 41.427 1.00 30.77  ? 973  SER   A CB   1 
ATOM   1239 O OG   . SER   A 1 167 ? -30.230 24.029 42.695 1.00 34.01  ? 973  SER   A OG   1 
ATOM   1240 N N    . GLU   A 1 168 ? -31.112 27.168 42.038 1.00 35.71  ? 974  GLU   A N    1 
ATOM   1241 C CA   . GLU   A 1 168 ? -32.205 28.098 41.795 1.00 31.90  ? 974  GLU   A CA   1 
ATOM   1242 C C    . GLU   A 1 168 ? -31.735 29.224 40.885 1.00 37.30  ? 974  GLU   A C    1 
ATOM   1243 O O    . GLU   A 1 168 ? -32.385 29.552 39.882 1.00 35.28  ? 974  GLU   A O    1 
ATOM   1244 C CB   . GLU   A 1 168 ? -32.720 28.635 43.126 1.00 30.11  ? 974  GLU   A CB   1 
ATOM   1245 C CG   . GLU   A 1 168 ? -33.772 29.679 43.043 1.00 30.46  ? 974  GLU   A CG   1 
ATOM   1246 C CD   . GLU   A 1 168 ? -34.469 29.919 44.380 1.00 38.84  ? 974  GLU   A CD   1 
ATOM   1247 O OE1  . GLU   A 1 168 ? -33.868 30.561 45.280 1.00 33.60  ? 974  GLU   A OE1  1 
ATOM   1248 O OE2  . GLU   A 1 168 ? -35.630 29.463 44.529 1.00 46.55  ? 974  GLU   A OE2  1 
ATOM   1249 N N    . ARG   A 1 169 ? -30.563 29.791 41.193 1.00 35.28  ? 975  ARG   A N    1 
ATOM   1250 C CA   . ARG   A 1 169 ? -30.058 30.897 40.398 1.00 33.89  ? 975  ARG   A CA   1 
ATOM   1251 C C    . ARG   A 1 169 ? -29.713 30.443 38.985 1.00 33.96  ? 975  ARG   A C    1 
ATOM   1252 O O    . ARG   A 1 169 ? -30.058 31.116 38.007 1.00 33.09  ? 975  ARG   A O    1 
ATOM   1253 C CB   . ARG   A 1 169 ? -28.853 31.526 41.086 1.00 29.49  ? 975  ARG   A CB   1 
ATOM   1254 C CG   . ARG   A 1 169 ? -28.478 32.873 40.511 1.00 26.98  ? 975  ARG   A CG   1 
ATOM   1255 C CD   . ARG   A 1 169 ? -27.325 33.483 41.279 1.00 33.48  ? 975  ARG   A CD   1 
ATOM   1256 N NE   . ARG   A 1 169 ? -27.603 33.490 42.714 1.00 31.01  ? 975  ARG   A NE   1 
ATOM   1257 C CZ   . ARG   A 1 169 ? -27.018 32.675 43.585 1.00 29.97  ? 975  ARG   A CZ   1 
ATOM   1258 N NH1  . ARG   A 1 169 ? -26.111 31.799 43.183 1.00 31.10  ? 975  ARG   A NH1  1 
ATOM   1259 N NH2  . ARG   A 1 169 ? -27.342 32.735 44.864 1.00 32.27  ? 975  ARG   A NH2  1 
ATOM   1260 N N    . VAL   A 1 170 ? -29.024 29.305 38.854 1.00 32.72  ? 976  VAL   A N    1 
ATOM   1261 C CA   . VAL   A 1 170 ? -28.647 28.832 37.523 1.00 33.38  ? 976  VAL   A CA   1 
ATOM   1262 C C    . VAL   A 1 170 ? -29.890 28.564 36.671 1.00 34.11  ? 976  VAL   A C    1 
ATOM   1263 O O    . VAL   A 1 170 ? -29.921 28.867 35.469 1.00 32.74  ? 976  VAL   A O    1 
ATOM   1264 C CB   . VAL   A 1 170 ? -27.750 27.583 37.617 1.00 30.24  ? 976  VAL   A CB   1 
ATOM   1265 C CG1  . VAL   A 1 170 ? -27.419 27.133 36.237 1.00 30.83  ? 976  VAL   A CG1  1 
ATOM   1266 C CG2  . VAL   A 1 170 ? -26.474 27.883 38.361 1.00 28.44  ? 976  VAL   A CG2  1 
ATOM   1267 N N    . LYS   A 1 171 ? -30.939 28.010 37.278 1.00 31.47  ? 977  LYS   A N    1 
ATOM   1268 C CA   . LYS   A 1 171 ? -32.110 27.615 36.503 1.00 31.97  ? 977  LYS   A CA   1 
ATOM   1269 C C    . LYS   A 1 171 ? -32.784 28.801 35.821 1.00 33.93  ? 977  LYS   A C    1 
ATOM   1270 O O    . LYS   A 1 171 ? -33.397 28.632 34.767 1.00 36.22  ? 977  LYS   A O    1 
ATOM   1271 C CB   . LYS   A 1 171 ? -33.109 26.891 37.396 1.00 35.59  ? 977  LYS   A CB   1 
ATOM   1272 C CG   . LYS   A 1 171 ? -32.901 25.388 37.490 1.00 35.39  ? 977  LYS   A CG   1 
ATOM   1273 C CD   . LYS   A 1 171 ? -33.843 24.819 38.527 1.00 32.12  ? 977  LYS   A CD   1 
ATOM   1274 C CE   . LYS   A 1 171 ? -33.454 23.416 38.965 1.00 38.89  ? 977  LYS   A CE   1 
ATOM   1275 N NZ   . LYS   A 1 171 ? -34.309 22.347 38.368 1.00 44.40  ? 977  LYS   A NZ   1 
ATOM   1276 N N    . LEU   A 1 172 ? -32.718 29.997 36.406 1.00 32.73  ? 978  LEU   A N    1 
ATOM   1277 C CA   . LEU   A 1 172 ? -33.234 31.165 35.702 1.00 33.70  ? 978  LEU   A CA   1 
ATOM   1278 C C    . LEU   A 1 172 ? -32.467 31.397 34.415 1.00 34.22  ? 978  LEU   A C    1 
ATOM   1279 O O    . LEU   A 1 172 ? -33.030 31.844 33.409 1.00 35.83  ? 978  LEU   A O    1 
ATOM   1280 C CB   . LEU   A 1 172 ? -33.138 32.403 36.583 1.00 35.63  ? 978  LEU   A CB   1 
ATOM   1281 C CG   . LEU   A 1 172 ? -33.944 32.316 37.867 1.00 40.24  ? 978  LEU   A CG   1 
ATOM   1282 C CD1  . LEU   A 1 172 ? -33.614 33.518 38.731 1.00 35.07  ? 978  LEU   A CD1  1 
ATOM   1283 C CD2  . LEU   A 1 172 ? -35.441 32.233 37.546 1.00 36.17  ? 978  LEU   A CD2  1 
ATOM   1284 N N    . ALA   A 1 173 ? -31.165 31.142 34.449 1.00 34.83  ? 979  ALA   A N    1 
ATOM   1285 C CA   . ALA   A 1 173 ? -30.361 31.239 33.247 1.00 31.38  ? 979  ALA   A CA   1 
ATOM   1286 C C    . ALA   A 1 173 ? -30.722 30.123 32.279 1.00 32.49  ? 979  ALA   A C    1 
ATOM   1287 O O    . ALA   A 1 173 ? -30.804 30.336 31.066 1.00 32.08  ? 979  ALA   A O    1 
ATOM   1288 C CB   . ALA   A 1 173 ? -28.884 31.185 33.632 1.00 32.57  ? 979  ALA   A CB   1 
ATOM   1289 N N    . GLU   A 1 174 ? -30.968 28.927 32.804 1.00 32.42  ? 980  GLU   A N    1 
ATOM   1290 C CA   . GLU   A 1 174 ? -31.339 27.817 31.941 1.00 31.43  ? 980  GLU   A CA   1 
ATOM   1291 C C    . GLU   A 1 174 ? -32.624 28.110 31.185 1.00 32.03  ? 980  GLU   A C    1 
ATOM   1292 O O    . GLU   A 1 174 ? -32.718 27.827 29.990 1.00 31.84  ? 980  GLU   A O    1 
ATOM   1293 C CB   . GLU   A 1 174 ? -31.473 26.542 32.763 1.00 29.82  ? 980  GLU   A CB   1 
ATOM   1294 C CG   . GLU   A 1 174 ? -30.198 26.159 33.453 1.00 29.76  ? 980  GLU   A CG   1 
ATOM   1295 C CD   . GLU   A 1 174 ? -30.373 24.907 34.287 1.00 37.24  ? 980  GLU   A CD   1 
ATOM   1296 O OE1  . GLU   A 1 174 ? -29.437 24.539 35.029 1.00 41.65  ? 980  GLU   A OE1  1 
ATOM   1297 O OE2  . GLU   A 1 174 ? -31.446 24.277 34.186 1.00 37.94  ? 980  GLU   A OE2  1 
ATOM   1298 N N    . HIS   A 1 175 ? -33.622 28.681 31.862 1.00 29.45  ? 981  HIS   A N    1 
ATOM   1299 C CA   . HIS   A 1 175 ? -34.876 29.032 31.214 1.00 31.12  ? 981  HIS   A CA   1 
ATOM   1300 C C    . HIS   A 1 175 ? -34.726 30.138 30.181 1.00 34.11  ? 981  HIS   A C    1 
ATOM   1301 O O    . HIS   A 1 175 ? -35.681 30.406 29.440 1.00 35.21  ? 981  HIS   A O    1 
ATOM   1302 C CB   . HIS   A 1 175 ? -35.890 29.439 32.275 1.00 30.03  ? 981  HIS   A CB   1 
ATOM   1303 C CG   . HIS   A 1 175 ? -36.098 28.393 33.318 1.00 33.34  ? 981  HIS   A CG   1 
ATOM   1304 N ND1  . HIS   A 1 175 ? -36.591 28.677 34.573 1.00 31.29  ? 981  HIS   A ND1  1 
ATOM   1305 C CD2  . HIS   A 1 175 ? -35.855 27.058 33.300 1.00 32.49  ? 981  HIS   A CD2  1 
ATOM   1306 C CE1  . HIS   A 1 175 ? -36.649 27.562 35.280 1.00 31.30  ? 981  HIS   A CE1  1 
ATOM   1307 N NE2  . HIS   A 1 175 ? -36.217 26.564 34.529 1.00 31.38  ? 981  HIS   A NE2  1 
ATOM   1308 N N    . LYS   A 1 176 ? -33.574 30.800 30.133 1.00 33.89  ? 982  LYS   A N    1 
ATOM   1309 C CA   . LYS   A 1 176 ? -33.271 31.775 29.095 1.00 31.21  ? 982  LYS   A CA   1 
ATOM   1310 C C    . LYS   A 1 176 ? -32.563 31.115 27.907 1.00 32.06  ? 982  LYS   A C    1 
ATOM   1311 O O    . LYS   A 1 176 ? -33.050 31.177 26.773 1.00 32.80  ? 982  LYS   A O    1 
ATOM   1312 C CB   . LYS   A 1 176 ? -32.419 32.901 29.690 1.00 34.52  ? 982  LYS   A CB   1 
ATOM   1313 C CG   . LYS   A 1 176 ? -33.225 34.050 30.274 1.00 41.33  ? 982  LYS   A CG   1 
ATOM   1314 C CD   . LYS   A 1 176 ? -32.541 34.698 31.507 1.00 40.92  ? 982  LYS   A CD   1 
ATOM   1315 C CE   . LYS   A 1 176 ? -31.466 35.710 31.085 1.00 52.86  ? 982  LYS   A CE   1 
ATOM   1316 N NZ   . LYS   A 1 176 ? -30.753 36.367 32.249 1.00 53.32  ? 982  LYS   A NZ   1 
ATOM   1317 N N    . ILE   A 1 177 ? -31.423 30.462 28.153 1.00 31.53  ? 983  ILE   A N    1 
ATOM   1318 C CA   . ILE   A 1 177 ? -30.601 29.972 27.047 1.00 31.01  ? 983  ILE   A CA   1 
ATOM   1319 C C    . ILE   A 1 177 ? -31.145 28.691 26.419 1.00 31.17  ? 983  ILE   A C    1 
ATOM   1320 O O    . ILE   A 1 177 ? -30.848 28.406 25.253 1.00 32.43  ? 983  ILE   A O    1 
ATOM   1321 C CB   . ILE   A 1 177 ? -29.135 29.763 27.478 1.00 28.98  ? 983  ILE   A CB   1 
ATOM   1322 C CG1  . ILE   A 1 177 ? -28.997 28.598 28.461 1.00 29.24  ? 983  ILE   A CG1  1 
ATOM   1323 C CG2  . ILE   A 1 177 ? -28.570 31.031 28.061 1.00 28.20  ? 983  ILE   A CG2  1 
ATOM   1324 C CD1  . ILE   A 1 177 ? -27.583 28.070 28.583 1.00 26.32  ? 983  ILE   A CD1  1 
ATOM   1325 N N    . PHE   A 1 178 ? -31.947 27.924 27.124 1.00 31.57  ? 984  PHE   A N    1 
ATOM   1326 C CA   . PHE   A 1 178 ? -32.402 26.681 26.508 1.00 30.40  ? 984  PHE   A CA   1 
ATOM   1327 C C    . PHE   A 1 178 ? -33.504 26.951 25.488 1.00 30.54  ? 984  PHE   A C    1 
ATOM   1328 O O    . PHE   A 1 178 ? -33.501 26.351 24.410 1.00 33.75  ? 984  PHE   A O    1 
ATOM   1329 C CB   . PHE   A 1 178 ? -32.867 25.704 27.585 1.00 25.35  ? 984  PHE   A CB   1 
ATOM   1330 C CG   . PHE   A 1 178 ? -32.963 24.291 27.125 1.00 28.16  ? 984  PHE   A CG   1 
ATOM   1331 C CD1  . PHE   A 1 178 ? -32.326 23.872 25.969 1.00 30.11  ? 984  PHE   A CD1  1 
ATOM   1332 C CD2  . PHE   A 1 178 ? -33.504 23.338 27.948 1.00 27.10  ? 984  PHE   A CD2  1 
ATOM   1333 C CE1  . PHE   A 1 178 ? -32.362 22.536 25.583 1.00 28.23  ? 984  PHE   A CE1  1 
ATOM   1334 C CE2  . PHE   A 1 178 ? -33.540 21.998 27.568 1.00 30.01  ? 984  PHE   A CE2  1 
ATOM   1335 C CZ   . PHE   A 1 178 ? -32.965 21.595 26.393 1.00 25.90  ? 984  PHE   A CZ   1 
ATOM   1336 N N    . PRO   A 1 179 ? -34.454 27.842 25.769 1.00 32.21  ? 985  PRO   A N    1 
ATOM   1337 C CA   . PRO   A 1 179 ? -35.385 28.243 24.702 1.00 32.30  ? 985  PRO   A CA   1 
ATOM   1338 C C    . PRO   A 1 179 ? -34.693 28.961 23.565 1.00 30.40  ? 985  PRO   A C    1 
ATOM   1339 O O    . PRO   A 1 179 ? -35.042 28.754 22.398 1.00 35.10  ? 985  PRO   A O    1 
ATOM   1340 C CB   . PRO   A 1 179 ? -36.390 29.156 25.428 1.00 30.14  ? 985  PRO   A CB   1 
ATOM   1341 C CG   . PRO   A 1 179 ? -36.330 28.757 26.826 1.00 31.36  ? 985  PRO   A CG   1 
ATOM   1342 C CD   . PRO   A 1 179 ? -34.909 28.306 27.091 1.00 31.98  ? 985  PRO   A CD   1 
ATOM   1343 N N    . ALA   A 1 180 ? -33.723 29.818 23.859 1.00 29.93  ? 986  ALA   A N    1 
ATOM   1344 C CA   . ALA   A 1 180 ? -33.030 30.498 22.774 1.00 28.57  ? 986  ALA   A CA   1 
ATOM   1345 C C    . ALA   A 1 180 ? -32.286 29.498 21.902 1.00 29.83  ? 986  ALA   A C    1 
ATOM   1346 O O    . ALA   A 1 180 ? -32.343 29.572 20.670 1.00 31.46  ? 986  ALA   A O    1 
ATOM   1347 C CB   . ALA   A 1 180 ? -32.080 31.551 23.331 1.00 26.28  ? 986  ALA   A CB   1 
ATOM   1348 N N    . ALA   A 1 181 ? -31.570 28.557 22.537 1.00 33.19  ? 987  ALA   A N    1 
ATOM   1349 C CA   . ALA   A 1 181 ? -30.814 27.531 21.818 1.00 29.20  ? 987  ALA   A CA   1 
ATOM   1350 C C    . ALA   A 1 181 ? -31.720 26.693 20.929 1.00 33.90  ? 987  ALA   A C    1 
ATOM   1351 O O    . ALA   A 1 181 ? -31.410 26.452 19.753 1.00 33.18  ? 987  ALA   A O    1 
ATOM   1352 C CB   . ALA   A 1 181 ? -30.084 26.628 22.807 1.00 27.86  ? 987  ALA   A CB   1 
ATOM   1353 N N    . LEU   A 1 182 ? -32.836 26.210 21.483 1.00 30.35  ? 988  LEU   A N    1 
ATOM   1354 C CA   . LEU   A 1 182 ? -33.796 25.494 20.655 1.00 31.78  ? 988  LEU   A CA   1 
ATOM   1355 C C    . LEU   A 1 182 ? -34.174 26.337 19.435 1.00 32.01  ? 988  LEU   A C    1 
ATOM   1356 O O    . LEU   A 1 182 ? -34.149 25.858 18.294 1.00 30.74  ? 988  LEU   A O    1 
ATOM   1357 C CB   . LEU   A 1 182 ? -35.018 25.124 21.499 1.00 27.64  ? 988  LEU   A CB   1 
ATOM   1358 C CG   . LEU   A 1 182 ? -36.228 24.507 20.799 1.00 29.83  ? 988  LEU   A CG   1 
ATOM   1359 C CD1  . LEU   A 1 182 ? -35.829 23.248 20.142 1.00 27.38  ? 988  LEU   A CD1  1 
ATOM   1360 C CD2  . LEU   A 1 182 ? -37.395 24.236 21.737 1.00 25.75  ? 988  LEU   A CD2  1 
ATOM   1361 N N    . GLN   A 1 183 ? -34.463 27.619 19.655 1.00 33.59  ? 989  GLN   A N    1 
ATOM   1362 C CA   . GLN   A 1 183 ? -34.936 28.469 18.571 1.00 32.30  ? 989  GLN   A CA   1 
ATOM   1363 C C    . GLN   A 1 183 ? -33.857 28.688 17.513 1.00 34.58  ? 989  GLN   A C    1 
ATOM   1364 O O    . GLN   A 1 183 ? -34.165 28.756 16.319 1.00 38.07  ? 989  GLN   A O    1 
ATOM   1365 C CB   . GLN   A 1 183 ? -35.438 29.795 19.135 1.00 32.29  ? 989  GLN   A CB   1 
ATOM   1366 C CG   . GLN   A 1 183 ? -35.740 30.842 18.042 1.00 34.26  ? 989  GLN   A CG   1 
ATOM   1367 C CD   . GLN   A 1 183 ? -36.943 30.481 17.186 1.00 38.18  ? 989  GLN   A CD   1 
ATOM   1368 O OE1  . GLN   A 1 183 ? -37.724 29.590 17.530 1.00 40.21  ? 989  GLN   A OE1  1 
ATOM   1369 N NE2  . GLN   A 1 183 ? -37.104 31.181 16.066 1.00 40.03  ? 989  GLN   A NE2  1 
ATOM   1370 N N    . LEU   A 1 184 ? -32.588 28.780 17.922 1.00 33.19  ? 990  LEU   A N    1 
ATOM   1371 C CA   . LEU   A 1 184 ? -31.492 28.856 16.955 1.00 35.47  ? 990  LEU   A CA   1 
ATOM   1372 C C    . LEU   A 1 184 ? -31.410 27.610 16.085 1.00 38.29  ? 990  LEU   A C    1 
ATOM   1373 O O    . LEU   A 1 184 ? -31.163 27.703 14.875 1.00 38.76  ? 990  LEU   A O    1 
ATOM   1374 C CB   . LEU   A 1 184 ? -30.167 29.035 17.676 1.00 35.91  ? 990  LEU   A CB   1 
ATOM   1375 C CG   . LEU   A 1 184 ? -29.993 30.396 18.310 1.00 38.63  ? 990  LEU   A CG   1 
ATOM   1376 C CD1  . LEU   A 1 184 ? -28.841 30.332 19.279 1.00 35.89  ? 990  LEU   A CD1  1 
ATOM   1377 C CD2  . LEU   A 1 184 ? -29.745 31.414 17.215 1.00 35.20  ? 990  LEU   A CD2  1 
ATOM   1378 N N    . VAL   A 1 185 ? -31.542 26.430 16.698 1.00 37.15  ? 991  VAL   A N    1 
ATOM   1379 C CA   . VAL   A 1 185 ? -31.414 25.191 15.944 1.00 37.40  ? 991  VAL   A CA   1 
ATOM   1380 C C    . VAL   A 1 185 ? -32.660 24.954 15.105 1.00 37.72  ? 991  VAL   A C    1 
ATOM   1381 O O    . VAL   A 1 185 ? -32.570 24.518 13.955 1.00 40.86  ? 991  VAL   A O    1 
ATOM   1382 C CB   . VAL   A 1 185 ? -31.143 24.003 16.885 1.00 34.27  ? 991  VAL   A CB   1 
ATOM   1383 C CG1  . VAL   A 1 185 ? -31.286 22.685 16.110 1.00 30.76  ? 991  VAL   A CG1  1 
ATOM   1384 C CG2  . VAL   A 1 185 ? -29.782 24.118 17.500 1.00 29.48  ? 991  VAL   A CG2  1 
ATOM   1385 N N    . ALA   A 1 186 ? -33.841 25.218 15.667 1.00 39.94  ? 992  ALA   A N    1 
ATOM   1386 C CA   . ALA   A 1 186 ? -35.072 24.987 14.918 1.00 35.29  ? 992  ALA   A CA   1 
ATOM   1387 C C    . ALA   A 1 186 ? -35.216 25.942 13.754 1.00 37.69  ? 992  ALA   A C    1 
ATOM   1388 O O    . ALA   A 1 186 ? -35.924 25.618 12.804 1.00 42.25  ? 992  ALA   A O    1 
ATOM   1389 C CB   . ALA   A 1 186 ? -36.308 25.105 15.814 1.00 31.88  ? 992  ALA   A CB   1 
ATOM   1390 N N    . SER   A 1 187 ? -34.575 27.102 13.787 1.00 37.93  ? 993  SER   A N    1 
ATOM   1391 C CA   . SER   A 1 187 ? -34.698 28.016 12.663 1.00 36.64  ? 993  SER   A CA   1 
ATOM   1392 C C    . SER   A 1 187 ? -33.614 27.800 11.609 1.00 44.32  ? 993  SER   A C    1 
ATOM   1393 O O    . SER   A 1 187 ? -33.594 28.505 10.590 1.00 41.30  ? 993  SER   A O    1 
ATOM   1394 C CB   . SER   A 1 187 ? -34.679 29.463 13.160 1.00 35.64  ? 993  SER   A CB   1 
ATOM   1395 O OG   . SER   A 1 187 ? -33.546 29.717 13.964 1.00 38.63  ? 993  SER   A OG   1 
ATOM   1396 N N    . GLY   A 1 188 ? -32.722 26.836 11.813 1.00 42.80  ? 994  GLY   A N    1 
ATOM   1397 C CA   . GLY   A 1 188 ? -31.627 26.699 10.882 1.00 39.27  ? 994  GLY   A CA   1 
ATOM   1398 C C    . GLY   A 1 188 ? -30.556 27.758 10.980 1.00 42.26  ? 994  GLY   A C    1 
ATOM   1399 O O    . GLY   A 1 188 ? -29.729 27.860 10.073 1.00 53.18  ? 994  GLY   A O    1 
ATOM   1400 N N    . THR   A 1 189 ? -30.541 28.556 12.046 1.00 43.22  ? 995  THR   A N    1 
ATOM   1401 C CA   . THR   A 1 189 ? -29.456 29.507 12.251 1.00 43.24  ? 995  THR   A CA   1 
ATOM   1402 C C    . THR   A 1 189 ? -28.184 28.823 12.704 1.00 44.39  ? 995  THR   A C    1 
ATOM   1403 O O    . THR   A 1 189 ? -27.089 29.286 12.385 1.00 49.51  ? 995  THR   A O    1 
ATOM   1404 C CB   . THR   A 1 189 ? -29.856 30.533 13.298 1.00 42.92  ? 995  THR   A CB   1 
ATOM   1405 O OG1  . THR   A 1 189 ? -31.154 31.030 12.973 1.00 43.91  ? 995  THR   A OG1  1 
ATOM   1406 C CG2  . THR   A 1 189 ? -28.850 31.660 13.342 1.00 41.28  ? 995  THR   A CG2  1 
ATOM   1407 N N    . VAL   A 1 190 ? -28.323 27.768 13.492 1.00 43.65  ? 996  VAL   A N    1 
ATOM   1408 C CA   . VAL   A 1 190 ? -27.219 26.988 14.022 1.00 43.36  ? 996  VAL   A CA   1 
ATOM   1409 C C    . VAL   A 1 190 ? -27.420 25.559 13.553 1.00 47.65  ? 996  VAL   A C    1 
ATOM   1410 O O    . VAL   A 1 190 ? -28.551 25.055 13.528 1.00 47.70  ? 996  VAL   A O    1 
ATOM   1411 C CB   . VAL   A 1 190 ? -27.152 27.057 15.565 1.00 43.24  ? 996  VAL   A CB   1 
ATOM   1412 C CG1  . VAL   A 1 190 ? -26.304 25.919 16.121 1.00 45.15  ? 996  VAL   A CG1  1 
ATOM   1413 C CG2  . VAL   A 1 190 ? -26.612 28.418 16.022 1.00 43.57  ? 996  VAL   A CG2  1 
ATOM   1414 N N    . GLN   A 1 191 ? -26.333 24.928 13.137 1.00 47.34  ? 997  GLN   A N    1 
ATOM   1415 C CA   . GLN   A 1 191 ? -26.340 23.514 12.822 1.00 46.47  ? 997  GLN   A CA   1 
ATOM   1416 C C    . GLN   A 1 191 ? -24.985 22.964 13.223 1.00 52.58  ? 997  GLN   A C    1 
ATOM   1417 O O    . GLN   A 1 191 ? -24.094 23.699 13.651 1.00 57.32  ? 997  GLN   A O    1 
ATOM   1418 C CB   . GLN   A 1 191 ? -26.634 23.258 11.343 1.00 40.57  ? 997  GLN   A CB   1 
ATOM   1419 C CG   . GLN   A 1 191 ? -25.598 23.849 10.435 1.00 50.79  ? 997  GLN   A CG   1 
ATOM   1420 C CD   . GLN   A 1 191 ? -25.646 23.288 9.045  1.00 52.82  ? 997  GLN   A CD   1 
ATOM   1421 O OE1  . GLN   A 1 191 ? -26.715 23.159 8.448  1.00 52.79  ? 997  GLN   A OE1  1 
ATOM   1422 N NE2  . GLN   A 1 191 ? -24.481 22.946 8.512  1.00 56.74  ? 997  GLN   A NE2  1 
ATOM   1423 N N    . LEU   A 1 192 ? -24.846 21.660 13.098 1.00 53.31  ? 998  LEU   A N    1 
ATOM   1424 C CA   . LEU   A 1 192 ? -23.585 20.974 13.294 1.00 53.53  ? 998  LEU   A CA   1 
ATOM   1425 C C    . LEU   A 1 192 ? -22.928 20.856 11.920 1.00 59.89  ? 998  LEU   A C    1 
ATOM   1426 O O    . LEU   A 1 192 ? -23.496 20.246 11.007 1.00 63.85  ? 998  LEU   A O    1 
ATOM   1427 C CB   . LEU   A 1 192 ? -23.852 19.614 13.939 1.00 51.00  ? 998  LEU   A CB   1 
ATOM   1428 C CG   . LEU   A 1 192 ? -22.866 19.090 14.968 1.00 49.30  ? 998  LEU   A CG   1 
ATOM   1429 C CD1  . LEU   A 1 192 ? -22.935 19.986 16.171 1.00 49.78  ? 998  LEU   A CD1  1 
ATOM   1430 C CD2  . LEU   A 1 192 ? -23.255 17.699 15.372 1.00 43.05  ? 998  LEU   A CD2  1 
ATOM   1431 N N    . GLY   A 1 193 ? -21.771 21.479 11.749 1.00 66.73  ? 999  GLY   A N    1 
ATOM   1432 C CA   . GLY   A 1 193 ? -21.161 21.510 10.434 1.00 65.34  ? 999  GLY   A CA   1 
ATOM   1433 C C    . GLY   A 1 193 ? -20.648 20.150 9.992  1.00 71.86  ? 999  GLY   A C    1 
ATOM   1434 O O    . GLY   A 1 193 ? -20.615 19.175 10.744 1.00 75.38  ? 999  GLY   A O    1 
ATOM   1435 N N    . GLU   A 1 194 ? -20.228 20.090 8.726  1.00 78.08  ? 1000 GLU   A N    1 
ATOM   1436 C CA   . GLU   A 1 194 ? -19.570 18.887 8.221  1.00 79.11  ? 1000 GLU   A CA   1 
ATOM   1437 C C    . GLU   A 1 194 ? -18.347 18.526 9.060  1.00 86.08  ? 1000 GLU   A C    1 
ATOM   1438 O O    . GLU   A 1 194 ? -18.049 17.340 9.252  1.00 82.91  ? 1000 GLU   A O    1 
ATOM   1439 C CB   . GLU   A 1 194 ? -19.175 19.083 6.757  1.00 71.28  ? 1000 GLU   A CB   1 
ATOM   1440 N N    . ASN   A 1 195 ? -17.629 19.531 9.563  1.00 97.35  ? 1001 ASN   A N    1 
ATOM   1441 C CA   . ASN   A 1 195 ? -16.483 19.331 10.440 1.00 95.79  ? 1001 ASN   A CA   1 
ATOM   1442 C C    . ASN   A 1 195 ? -16.883 19.095 11.886 1.00 96.33  ? 1001 ASN   A C    1 
ATOM   1443 O O    . ASN   A 1 195 ? -15.997 18.980 12.740 1.00 95.97  ? 1001 ASN   A O    1 
ATOM   1444 C CB   . ASN   A 1 195 ? -15.551 20.542 10.375 1.00 98.13  ? 1001 ASN   A CB   1 
ATOM   1445 C CG   . ASN   A 1 195 ? -16.182 21.787 10.970 1.00 98.87  ? 1001 ASN   A CG   1 
ATOM   1446 O OD1  . ASN   A 1 195 ? -17.395 21.838 11.179 1.00 97.35  ? 1001 ASN   A OD1  1 
ATOM   1447 N ND2  . ASN   A 1 195 ? -15.360 22.790 11.264 1.00 104.56 ? 1001 ASN   A ND2  1 
ATOM   1448 N N    . GLY   A 1 196 ? -18.181 19.053 12.185 1.00 85.48  ? 1002 GLY   A N    1 
ATOM   1449 C CA   . GLY   A 1 196 ? -18.651 18.771 13.520 1.00 77.68  ? 1002 GLY   A CA   1 
ATOM   1450 C C    . GLY   A 1 196 ? -18.528 19.903 14.515 1.00 77.19  ? 1002 GLY   A C    1 
ATOM   1451 O O    . GLY   A 1 196 ? -18.930 19.729 15.675 1.00 68.96  ? 1002 GLY   A O    1 
ATOM   1452 N N    . LYS   A 1 197 ? -17.969 21.046 14.123 1.00 84.30  ? 1003 LYS   A N    1 
ATOM   1453 C CA   . LYS   A 1 197 ? -18.044 22.214 14.988 1.00 83.13  ? 1003 LYS   A CA   1 
ATOM   1454 C C    . LYS   A 1 197 ? -19.387 22.921 14.774 1.00 77.15  ? 1003 LYS   A C    1 
ATOM   1455 O O    . LYS   A 1 197 ? -20.166 22.570 13.876 1.00 75.98  ? 1003 LYS   A O    1 
ATOM   1456 C CB   . LYS   A 1 197 ? -16.856 23.150 14.738 1.00 79.04  ? 1003 LYS   A CB   1 
ATOM   1457 N N    . ILE   A 1 198 ? -19.666 23.914 15.623 1.00 65.70  ? 1004 ILE   A N    1 
ATOM   1458 C CA   . ILE   A 1 198 ? -20.960 24.591 15.591 1.00 60.44  ? 1004 ILE   A CA   1 
ATOM   1459 C C    . ILE   A 1 198 ? -20.972 25.495 14.361 1.00 59.48  ? 1004 ILE   A C    1 
ATOM   1460 O O    . ILE   A 1 198 ? -19.996 26.204 14.087 1.00 62.57  ? 1004 ILE   A O    1 
ATOM   1461 C CB   . ILE   A 1 198 ? -21.171 25.407 16.875 1.00 53.72  ? 1004 ILE   A CB   1 
ATOM   1462 C CG1  . ILE   A 1 198 ? -22.637 25.524 17.222 1.00 50.36  ? 1004 ILE   A CG1  1 
ATOM   1463 C CG2  . ILE   A 1 198 ? -20.701 26.827 16.674 1.00 55.66  ? 1004 ILE   A CG2  1 
ATOM   1464 C CD1  . ILE   A 1 198 ? -23.197 24.183 17.658 1.00 48.04  ? 1004 ILE   A CD1  1 
ATOM   1465 N N    . CYS   A 1 199 ? -22.054 25.464 13.598 1.00 56.77  ? 1005 CYS   A N    1 
ATOM   1466 C CA   . CYS   A 1 199 ? -22.124 26.148 12.309 1.00 57.00  ? 1005 CYS   A CA   1 
ATOM   1467 C C    . CYS   A 1 199 ? -23.208 27.219 12.365 1.00 55.29  ? 1005 CYS   A C    1 
ATOM   1468 O O    . CYS   A 1 199 ? -24.395 26.885 12.419 1.00 51.89  ? 1005 CYS   A O    1 
ATOM   1469 C CB   . CYS   A 1 199 ? -22.410 25.135 11.197 1.00 55.07  ? 1005 CYS   A CB   1 
ATOM   1470 S SG   . CYS   A 1 199 ? -21.967 25.634 9.537  1.00 62.16  ? 1005 CYS   A SG   1 
ATOM   1471 N N    . TRP   A 1 200 ? -22.810 28.500 12.344 1.00 55.41  ? 1006 TRP   A N    1 
ATOM   1472 C CA   . TRP   A 1 200 ? -23.758 29.612 12.263 1.00 56.51  ? 1006 TRP   A CA   1 
ATOM   1473 C C    . TRP   A 1 200 ? -24.133 29.906 10.814 1.00 60.91  ? 1006 TRP   A C    1 
ATOM   1474 O O    . TRP   A 1 200 ? -23.284 29.876 9.921  1.00 62.96  ? 1006 TRP   A O    1 
ATOM   1475 C CB   . TRP   A 1 200 ? -23.188 30.875 12.907 1.00 57.48  ? 1006 TRP   A CB   1 
ATOM   1476 C CG   . TRP   A 1 200 ? -23.211 30.805 14.402 1.00 63.23  ? 1006 TRP   A CG   1 
ATOM   1477 C CD1  . TRP   A 1 200 ? -22.306 30.163 15.212 1.00 61.99  ? 1006 TRP   A CD1  1 
ATOM   1478 C CD2  . TRP   A 1 200 ? -24.201 31.372 15.279 1.00 61.34  ? 1006 TRP   A CD2  1 
ATOM   1479 N NE1  . TRP   A 1 200 ? -22.665 30.308 16.537 1.00 59.02  ? 1006 TRP   A NE1  1 
ATOM   1480 C CE2  . TRP   A 1 200 ? -23.824 31.040 16.607 1.00 62.75  ? 1006 TRP   A CE2  1 
ATOM   1481 C CE3  . TRP   A 1 200 ? -25.365 32.131 15.074 1.00 56.05  ? 1006 TRP   A CE3  1 
ATOM   1482 C CZ2  . TRP   A 1 200 ? -24.574 31.447 17.730 1.00 61.48  ? 1006 TRP   A CZ2  1 
ATOM   1483 C CZ3  . TRP   A 1 200 ? -26.104 32.538 16.187 1.00 51.94  ? 1006 TRP   A CZ3  1 
ATOM   1484 C CH2  . TRP   A 1 200 ? -25.704 32.191 17.498 1.00 55.46  ? 1006 TRP   A CH2  1 
ATOM   1485 N N    . VAL   A 1 201 ? -25.408 30.212 10.586 1.00 63.04  ? 1007 VAL   A N    1 
ATOM   1486 C CA   . VAL   A 1 201 ? -25.866 30.438 9.226  1.00 64.77  ? 1007 VAL   A CA   1 
ATOM   1487 C C    . VAL   A 1 201 ? -26.785 31.670 9.189  1.00 66.84  ? 1007 VAL   A C    1 
ATOM   1488 O O    . VAL   A 1 201 ? -26.506 32.681 8.539  1.00 71.68  ? 1007 VAL   A O    1 
ATOM   1489 C CB   . VAL   A 1 201 ? -26.606 29.214 8.699  1.00 57.38  ? 1007 VAL   A CB   1 
ATOM   1490 C CG1  . VAL   A 1 201 ? -26.980 29.424 7.237  1.00 55.60  ? 1007 VAL   A CG1  1 
ATOM   1491 C CG2  . VAL   A 1 201 ? -25.848 27.891 9.017  1.00 52.45  ? 1007 VAL   A CG2  1 
HETATM 1492 C C1   . GAR   B 2 .   ? -31.701 21.301 35.370 1.00 40.83  ? 1101 GAR   A C1   1 
HETATM 1493 O O6   . GAR   B 2 .   ? -31.306 22.163 36.429 1.00 46.92  ? 1101 GAR   A O6   1 
HETATM 1494 C C2   . GAR   B 2 .   ? -30.469 20.842 34.586 1.00 42.97  ? 1101 GAR   A C2   1 
HETATM 1495 O O8   . GAR   B 2 .   ? -29.387 21.775 34.595 1.00 46.48  ? 1101 GAR   A O8   1 
HETATM 1496 C C3   . GAR   B 2 .   ? -30.148 19.538 35.303 1.00 41.18  ? 1101 GAR   A C3   1 
HETATM 1497 O O4   . GAR   B 2 .   ? -31.374 19.061 35.893 1.00 44.83  ? 1101 GAR   A O4   1 
HETATM 1498 C C5   . GAR   B 2 .   ? -32.356 20.089 36.039 1.00 40.63  ? 1101 GAR   A C5   1 
HETATM 1499 C C10  . GAR   B 2 .   ? -33.731 19.714 35.518 1.00 41.26  ? 1101 GAR   A C10  1 
HETATM 1500 O O12  . GAR   B 2 .   ? -34.616 20.636 36.152 1.00 38.97  ? 1101 GAR   A O12  1 
HETATM 1501 N N19  . GAR   B 2 .   ? -29.590 18.446 34.535 1.00 54.84  ? 1101 GAR   A N19  1 
HETATM 1502 C C21  . GAR   B 2 .   ? -28.469 17.853 35.000 1.00 56.37  ? 1101 GAR   A C21  1 
HETATM 1503 O O22  . GAR   B 2 .   ? -27.993 18.052 36.144 1.00 49.69  ? 1101 GAR   A O22  1 
HETATM 1504 C C23  . GAR   B 2 .   ? -27.831 16.915 33.984 1.00 50.51  ? 1101 GAR   A C23  1 
HETATM 1505 N N24  . GAR   B 2 .   ? -26.546 16.372 34.406 1.00 54.75  ? 1101 GAR   A N24  1 
HETATM 1506 P P15  . GAR   B 2 .   ? -36.120 20.748 35.632 1.00 38.59  ? 1101 GAR   A P15  1 
HETATM 1507 O O16  . GAR   B 2 .   ? -36.816 21.661 36.611 1.00 33.64  ? 1101 GAR   A O16  1 
HETATM 1508 O O17  . GAR   B 2 .   ? -35.942 21.319 34.225 1.00 34.04  ? 1101 GAR   A O17  1 
HETATM 1509 O O18  . GAR   B 2 .   ? -36.600 19.316 35.705 1.00 38.61  ? 1101 GAR   A O18  1 
HETATM 1510 H H1   . GAR   B 2 .   ? -32.384 21.810 34.675 1.00 49.00  ? 1101 GAR   A H1   1 
HETATM 1511 H HO6  . GAR   B 2 .   ? -30.481 22.608 36.191 1.00 56.31  ? 1101 GAR   A HO6  1 
HETATM 1512 H H2   . GAR   B 2 .   ? -30.644 20.741 33.506 1.00 51.56  ? 1101 GAR   A H2   1 
HETATM 1513 H HO8  . GAR   B 2 .   ? -28.806 21.602 33.841 1.00 55.78  ? 1101 GAR   A HO8  1 
HETATM 1514 H H3   . GAR   B 2 .   ? -29.344 19.813 35.999 1.00 49.41  ? 1101 GAR   A H3   1 
HETATM 1515 H H5   . GAR   B 2 .   ? -32.601 20.294 37.090 1.00 48.75  ? 1101 GAR   A H5   1 
HETATM 1516 H H101 . GAR   B 2 .   ? -33.778 19.807 34.431 1.00 49.51  ? 1101 GAR   A H101 1 
HETATM 1517 H H102 . GAR   B 2 .   ? -33.982 18.684 35.778 1.00 49.51  ? 1101 GAR   A H102 1 
HETATM 1518 H H19  . GAR   B 2 .   ? -30.033 18.146 33.679 1.00 65.80  ? 1101 GAR   A H19  1 
HETATM 1519 H H231 . GAR   B 2 .   ? -27.692 17.456 33.046 1.00 60.62  ? 1101 GAR   A H231 1 
HETATM 1520 H H232 . GAR   B 2 .   ? -28.516 16.085 33.794 1.00 60.62  ? 1101 GAR   A H232 1 
HETATM 1521 H H241 . GAR   B 2 .   ? -26.159 16.629 35.303 1.00 65.70  ? 1101 GAR   A H241 1 
HETATM 1522 H H242 . GAR   B 2 .   ? -26.042 15.739 33.801 1.00 65.70  ? 1101 GAR   A H242 1 
HETATM 1523 C C12  . A1B62 C 3 .   ? -26.937 10.995 33.973 0.90 54.65  ? 1102 A1B62 A C12  1 
HETATM 1524 C C13  . A1B62 C 3 .   ? -26.102 10.033 34.570 0.90 56.28  ? 1102 A1B62 A C13  1 
HETATM 1525 C C15  . A1B62 C 3 .   ? -24.970 12.320 34.138 0.90 53.15  ? 1102 A1B62 A C15  1 
HETATM 1526 C C16  . A1B62 C 3 .   ? -26.311 12.252 33.733 0.90 53.37  ? 1102 A1B62 A C16  1 
HETATM 1527 C C21  . A1B62 C 3 .   ? -29.549 6.716  35.607 0.90 62.72  ? 1102 A1B62 A C21  1 
HETATM 1528 C C22  . A1B62 C 3 .   ? -29.678 7.237  37.040 0.90 68.19  ? 1102 A1B62 A C22  1 
HETATM 1529 C C17  . A1B62 C 3 .   ? -26.445 8.591  34.940 0.90 57.02  ? 1102 A1B62 A C17  1 
HETATM 1530 C C23  . A1B62 C 3 .   ? -31.082 6.948  37.585 0.90 75.09  ? 1102 A1B62 A C23  1 
HETATM 1531 N N11  . A1B62 C 3 .   ? -24.290 9.641  25.301 0.90 45.99  ? 1102 A1B62 A N11  1 
HETATM 1532 C C20  . A1B62 C 3 .   ? -28.128 6.726  35.058 0.90 58.05  ? 1102 A1B62 A C20  1 
HETATM 1533 C C02  . A1B62 C 3 .   ? -24.794 10.784 26.013 0.90 45.34  ? 1102 A1B62 A C02  1 
HETATM 1534 C C04  . A1B62 C 3 .   ? -24.586 13.008 26.582 0.90 48.50  ? 1102 A1B62 A C04  1 
HETATM 1535 C C05  . A1B62 C 3 .   ? -26.426 13.957 28.143 0.90 42.18  ? 1102 A1B62 A C05  1 
HETATM 1536 C C06  . A1B62 C 3 .   ? -27.603 13.551 28.798 0.90 41.26  ? 1102 A1B62 A C06  1 
HETATM 1537 C C08  . A1B62 C 3 .   ? -25.772 12.912 27.357 0.90 44.73  ? 1102 A1B62 A C08  1 
HETATM 1538 C C09  . A1B62 C 3 .   ? -26.428 11.677 27.399 0.90 44.27  ? 1102 A1B62 A C09  1 
HETATM 1539 C C26  . A1B62 C 3 .   ? -28.118 5.909  33.765 0.90 58.69  ? 1102 A1B62 A C26  1 
HETATM 1540 C C29  . A1B62 C 3 .   ? -28.521 14.379 29.685 0.90 44.80  ? 1102 A1B62 A C29  1 
HETATM 1541 C C30  . A1B62 C 3 .   ? -27.894 14.591 31.062 0.90 46.48  ? 1102 A1B62 A C30  1 
HETATM 1542 C C31  . A1B62 C 3 .   ? -27.272 13.311 31.610 0.90 46.87  ? 1102 A1B62 A C31  1 
HETATM 1543 C C32  . A1B62 C 3 .   ? -27.066 13.424 33.112 0.90 50.56  ? 1102 A1B62 A C32  1 
HETATM 1544 F F33  . A1B62 C 3 .   ? -28.235 10.764 33.648 0.90 56.37  ? 1102 A1B62 A F33  1 
HETATM 1545 N N01  . A1B62 C 3 .   ? -25.914 10.635 26.723 0.90 45.72  ? 1102 A1B62 A N01  1 
HETATM 1546 N N03  . A1B62 C 3 .   ? -24.123 11.937 25.933 0.90 47.45  ? 1102 A1B62 A N03  1 
HETATM 1547 N N19  . A1B62 C 3 .   ? -27.790 8.093  34.735 0.90 60.37  ? 1102 A1B62 A N19  1 
HETATM 1548 O O10  . A1B62 C 3 .   ? -24.016 14.047 26.526 0.90 47.36  ? 1102 A1B62 A O10  1 
HETATM 1549 O O18  . A1B62 C 3 .   ? -25.614 7.876  35.376 0.90 56.69  ? 1102 A1B62 A O18  1 
HETATM 1550 O O24  . A1B62 C 3 .   ? -31.253 6.759  38.820 0.90 76.95  ? 1102 A1B62 A O24  1 
HETATM 1551 O O25  . A1B62 C 3 .   ? -32.066 6.896  36.789 0.90 80.16  ? 1102 A1B62 A O25  1 
HETATM 1552 O O27  . A1B62 C 3 .   ? -28.232 4.655  33.830 0.90 58.78  ? 1102 A1B62 A O27  1 
HETATM 1553 O O28  . A1B62 C 3 .   ? -28.016 6.477  32.635 0.90 57.19  ? 1102 A1B62 A O28  1 
HETATM 1554 S S07  . A1B62 C 3 .   ? -27.807 11.927 28.391 0.90 45.52  ? 1102 A1B62 A S07  1 
HETATM 1555 S S14  . A1B62 C 3 .   ? -24.615 10.794 34.776 0.90 61.14  ? 1102 A1B62 A S14  1 
HETATM 1556 O O    . HOH   D 4 .   ? -36.363 18.279 37.899 1.00 40.14  ? 1201 HOH   A O    1 
HETATM 1557 O O    . HOH   D 4 .   ? -40.820 18.207 10.174 1.00 37.13  ? 1202 HOH   A O    1 
HETATM 1558 O O    . HOH   D 4 .   ? -46.278 21.730 37.950 1.00 45.12  ? 1203 HOH   A O    1 
HETATM 1559 O O    . HOH   D 4 .   ? -37.575 28.422 22.479 1.00 32.60  ? 1204 HOH   A O    1 
HETATM 1560 O O    . HOH   D 4 .   ? -36.900 20.400 41.115 1.00 40.02  ? 1205 HOH   A O    1 
HETATM 1561 O O    . HOH   D 4 .   ? -50.568 11.830 27.389 1.00 48.09  ? 1206 HOH   A O    1 
HETATM 1562 O O    . HOH   D 4 .   ? -19.748 26.056 35.810 1.00 31.67  ? 1207 HOH   A O    1 
HETATM 1563 O O    . HOH   D 4 .   ? -27.034 13.451 19.543 1.00 41.93  ? 1208 HOH   A O    1 
HETATM 1564 O O    . HOH   D 4 .   ? -30.013 21.796 38.624 1.00 40.79  ? 1209 HOH   A O    1 
HETATM 1565 O O    . HOH   D 4 .   ? -29.055 12.855 12.944 1.00 42.05  ? 1210 HOH   A O    1 
HETATM 1566 O O    . HOH   D 4 .   ? -37.015 16.886 34.478 1.00 39.69  ? 1211 HOH   A O    1 
HETATM 1567 O O    . HOH   D 4 .   ? -25.697 17.027 31.598 1.00 42.52  ? 1212 HOH   A O    1 
HETATM 1568 O O    . HOH   D 4 .   ? -46.821 8.840  35.662 1.00 52.88  ? 1213 HOH   A O    1 
HETATM 1569 O O    . HOH   D 4 .   ? -45.372 25.931 18.556 1.00 40.98  ? 1214 HOH   A O    1 
HETATM 1570 O O    . HOH   D 4 .   ? -40.006 27.447 33.677 1.00 41.26  ? 1215 HOH   A O    1 
HETATM 1571 O O    . HOH   D 4 .   ? -44.871 23.972 21.223 1.00 32.36  ? 1216 HOH   A O    1 
HETATM 1572 O O    . HOH   D 4 .   ? -23.298 35.000 30.552 1.00 32.11  ? 1217 HOH   A O    1 
HETATM 1573 O O    . HOH   D 4 .   ? -35.432 33.022 33.813 1.00 35.53  ? 1218 HOH   A O    1 
HETATM 1574 O O    . HOH   D 4 .   ? -22.413 15.113 24.617 1.00 47.52  ? 1219 HOH   A O    1 
HETATM 1575 O O    . HOH   D 4 .   ? -48.593 15.923 19.286 1.00 43.18  ? 1220 HOH   A O    1 
HETATM 1576 O O    . HOH   D 4 .   ? -37.292 31.262 35.020 1.00 33.17  ? 1221 HOH   A O    1 
HETATM 1577 O O    . HOH   D 4 .   ? -30.838 16.833 30.725 1.00 37.85  ? 1222 HOH   A O    1 
HETATM 1578 O O    . HOH   D 4 .   ? -23.145 24.909 38.797 1.00 33.79  ? 1223 HOH   A O    1 
HETATM 1579 O O    . HOH   D 4 .   ? -25.044 17.983 36.782 1.00 47.09  ? 1224 HOH   A O    1 
HETATM 1580 O O    . HOH   D 4 .   ? -31.174 35.326 34.758 1.00 40.29  ? 1225 HOH   A O    1 
HETATM 1581 O O    . HOH   D 4 .   ? -31.155 31.172 44.683 1.00 30.66  ? 1226 HOH   A O    1 
HETATM 1582 O O    . HOH   D 4 .   ? -27.110 15.983 18.735 1.00 40.00  ? 1227 HOH   A O    1 
HETATM 1583 O O    . HOH   D 4 .   ? -22.056 29.363 19.112 1.00 50.30  ? 1228 HOH   A O    1 
HETATM 1584 O O    . HOH   D 4 .   ? -39.614 30.909 27.911 1.00 36.21  ? 1229 HOH   A O    1 
HETATM 1585 O O    . HOH   D 4 .   ? -18.257 27.744 44.583 1.00 38.09  ? 1230 HOH   A O    1 
HETATM 1586 O O    . HOH   D 4 .   ? -40.629 15.550 10.661 1.00 46.41  ? 1231 HOH   A O    1 
HETATM 1587 O O    . HOH   D 4 .   ? -45.108 37.082 25.466 1.00 50.59  ? 1232 HOH   A O    1 
HETATM 1588 O O    . HOH   D 4 .   ? -41.453 16.111 40.061 1.00 42.34  ? 1233 HOH   A O    1 
HETATM 1589 O O    . HOH   D 4 .   ? -21.550 36.619 47.764 1.00 40.52  ? 1234 HOH   A O    1 
HETATM 1590 O O    . HOH   D 4 .   ? -14.203 20.373 36.011 1.00 34.78  ? 1235 HOH   A O    1 
HETATM 1591 O O    . HOH   D 4 .   ? -20.060 36.187 43.049 1.00 38.18  ? 1236 HOH   A O    1 
HETATM 1592 O O    . HOH   D 4 .   ? -29.347 35.616 43.518 1.00 39.27  ? 1237 HOH   A O    1 
HETATM 1593 O O    . HOH   D 4 .   ? -29.771 24.296 38.049 1.00 43.06  ? 1238 HOH   A O    1 
HETATM 1594 O O    . HOH   D 4 .   ? -19.237 25.917 20.095 1.00 45.82  ? 1239 HOH   A O    1 
HETATM 1595 O O    . HOH   D 4 .   ? -35.183 28.845 39.480 1.00 40.20  ? 1240 HOH   A O    1 
HETATM 1596 O O    . HOH   D 4 .   ? -35.642 25.880 29.457 1.00 31.32  ? 1241 HOH   A O    1 
HETATM 1597 O O    . HOH   D 4 .   ? -24.381 14.504 32.540 1.00 70.15  ? 1242 HOH   A O    1 
HETATM 1598 O O    . HOH   D 4 .   ? -34.814 16.037 36.523 1.00 38.52  ? 1243 HOH   A O    1 
HETATM 1599 O O    . HOH   D 4 .   ? -41.094 18.257 41.877 1.00 37.25  ? 1244 HOH   A O    1 
HETATM 1600 O O    . HOH   D 4 .   ? -21.964 17.636 18.888 1.00 44.07  ? 1245 HOH   A O    1 
HETATM 1601 O O    . HOH   D 4 .   ? -27.268 -1.802 26.102 1.00 71.62  ? 1246 HOH   A O    1 
HETATM 1602 O O    . HOH   D 4 .   ? -34.212 25.864 45.623 1.00 32.73  ? 1247 HOH   A O    1 
HETATM 1603 O O    . HOH   D 4 .   ? -22.775 5.506  16.779 1.00 58.62  ? 1248 HOH   A O    1 
HETATM 1604 O O    . HOH   D 4 .   ? -14.988 19.149 42.683 1.00 49.01  ? 1249 HOH   A O    1 
HETATM 1605 O O    . HOH   D 4 .   ? -33.224 11.309 12.643 1.00 39.44  ? 1250 HOH   A O    1 
HETATM 1606 O O    . HOH   D 4 .   ? -31.954 32.920 42.530 1.00 51.14  ? 1251 HOH   A O    1 
HETATM 1607 O O    . HOH   D 4 .   ? -34.152 11.831 38.014 1.00 51.33  ? 1252 HOH   A O    1 
HETATM 1608 O O    . HOH   D 4 .   ? -19.226 28.870 19.151 1.00 49.63  ? 1253 HOH   A O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA   A 2   ? 0.4238 0.3414 0.3448 -0.0102 -0.0704 -0.0260 808  ALA   A N   
2    C CA  . ALA   A 2   ? 0.4701 0.3975 0.4055 -0.0122 -0.0556 -0.0308 808  ALA   A CA  
3    C C   . ALA   A 2   ? 0.4497 0.3928 0.4224 -0.0094 -0.0558 -0.0308 808  ALA   A C   
4    O O   . ALA   A 2   ? 0.4848 0.4384 0.4750 -0.0058 -0.0556 -0.0254 808  ALA   A O   
5    C CB  . ALA   A 2   ? 0.4554 0.3849 0.3840 -0.0135 -0.0397 -0.0277 808  ALA   A CB  
6    N N   . ARG   A 3   ? 0.4189 0.3626 0.4016 -0.0122 -0.0562 -0.0373 809  ARG   A N   
7    C CA  . ARG   A 3   ? 0.4532 0.4087 0.4667 -0.0140 -0.0564 -0.0368 809  ARG   A CA  
8    C C   . ARG   A 3   ? 0.4481 0.4056 0.4712 -0.0139 -0.0431 -0.0333 809  ARG   A C   
9    O O   . ARG   A 3   ? 0.4405 0.3889 0.4534 -0.0128 -0.0371 -0.0376 809  ARG   A O   
10   C CB  . ARG   A 3   ? 0.4545 0.4044 0.4711 -0.0190 -0.0657 -0.0448 809  ARG   A CB  
11   C CG  . ARG   A 3   ? 0.4731 0.4200 0.4778 -0.0186 -0.0812 -0.0486 809  ARG   A CG  
12   C CD  . ARG   A 3   ? 0.4611 0.4023 0.4681 -0.0242 -0.0913 -0.0575 809  ARG   A CD  
13   N NE  . ARG   A 3   ? 0.5079 0.4610 0.5466 -0.0306 -0.0908 -0.0571 809  ARG   A NE  
14   C CZ  . ARG   A 3   ? 0.4743 0.4482 0.5390 -0.0332 -0.0971 -0.0559 809  ARG   A CZ  
15   N NH1 . ARG   A 3   ? 0.4570 0.4403 0.5218 -0.0265 -0.1067 -0.0559 809  ARG   A NH1 
16   N NH2 . ARG   A 3   ? 0.4171 0.4022 0.5072 -0.0429 -0.0944 -0.0555 809  ARG   A NH2 
17   N N   . VAL   A 4   ? 0.4072 0.3775 0.4499 -0.0144 -0.0392 -0.0268 810  VAL   A N   
18   C CA  . VAL   A 4   ? 0.4593 0.4305 0.5065 -0.0135 -0.0283 -0.0216 810  VAL   A CA  
19   C C   . VAL   A 4   ? 0.4095 0.3843 0.4752 -0.0203 -0.0272 -0.0181 810  VAL   A C   
20   O O   . VAL   A 4   ? 0.3472 0.3350 0.4281 -0.0259 -0.0304 -0.0173 810  VAL   A O   
21   C CB  . VAL   A 4   ? 0.4255 0.4052 0.4706 -0.0090 -0.0231 -0.0158 810  VAL   A CB  
22   C CG1 . VAL   A 4   ? 0.3446 0.3281 0.3979 -0.0092 -0.0137 -0.0100 810  VAL   A CG1 
23   C CG2 . VAL   A 4   ? 0.3401 0.3106 0.3610 -0.0058 -0.0227 -0.0174 810  VAL   A CG2 
24   N N   . ALA   A 5   ? 0.3970 0.3600 0.4609 -0.0204 -0.0234 -0.0166 811  ALA   A N   
25   C CA  . ALA   A 5   ? 0.4353 0.3951 0.5092 -0.0283 -0.0224 -0.0103 811  ALA   A CA  
26   C C   . ALA   A 5   ? 0.3985 0.3613 0.4711 -0.0250 -0.0146 -0.0030 811  ALA   A C   
27   O O   . ALA   A 5   ? 0.3757 0.3350 0.4405 -0.0163 -0.0115 -0.0048 811  ALA   A O   
28   C CB  . ALA   A 5   ? 0.3549 0.2915 0.4255 -0.0309 -0.0290 -0.0139 811  ALA   A CB  
29   N N   . VAL   A 6   ? 0.3525 0.3240 0.4325 -0.0331 -0.0110 0.0045  812  VAL   A N   
30   C CA  . VAL   A 6   ? 0.4135 0.3858 0.4898 -0.0318 -0.0049 0.0119  812  VAL   A CA  
31   C C   . VAL   A 6   ? 0.4086 0.3631 0.4813 -0.0416 -0.0080 0.0191  812  VAL   A C   
32   O O   . VAL   A 6   ? 0.4517 0.4085 0.5288 -0.0554 -0.0084 0.0223  812  VAL   A O   
33   C CB  . VAL   A 6   ? 0.3829 0.3788 0.4657 -0.0331 0.0021  0.0140  812  VAL   A CB  
34   C CG1 . VAL   A 6   ? 0.3238 0.3193 0.3999 -0.0314 0.0078  0.0206  812  VAL   A CG1 
35   C CG2 . VAL   A 6   ? 0.3018 0.3074 0.3854 -0.0238 0.0007  0.0075  812  VAL   A CG2 
36   N N   . LEU   A 7   ? 0.3800 0.3160 0.4442 -0.0352 -0.0113 0.0213  813  LEU   A N   
37   C CA  . LEU   A 7   ? 0.4457 0.3583 0.5016 -0.0432 -0.0173 0.0299  813  LEU   A CA  
38   C C   . LEU   A 7   ? 0.4376 0.3565 0.4866 -0.0465 -0.0117 0.0395  813  LEU   A C   
39   O O   . LEU   A 7   ? 0.4351 0.3637 0.4842 -0.0354 -0.0081 0.0377  813  LEU   A O   
40   C CB  . LEU   A 7   ? 0.4336 0.3194 0.4852 -0.0323 -0.0282 0.0252  813  LEU   A CB  
41   C CG  . LEU   A 7   ? 0.4795 0.3497 0.5333 -0.0330 -0.0363 0.0168  813  LEU   A CG  
42   C CD1 . LEU   A 7   ? 0.4451 0.3384 0.5066 -0.0326 -0.0304 0.0083  813  LEU   A CD1 
43   C CD2 . LEU   A 7   ? 0.4530 0.3029 0.5060 -0.0178 -0.0458 0.0072  813  LEU   A CD2 
44   N N   . ILE   A 8   ? 0.4879 0.4024 0.5295 -0.0634 -0.0103 0.0492  814  ILE   A N   
45   C CA  . ILE   A 8   ? 0.5062 0.4270 0.5374 -0.0692 -0.0041 0.0580  814  ILE   A CA  
46   C C   . ILE   A 8   ? 0.5428 0.4315 0.5535 -0.0821 -0.0126 0.0705  814  ILE   A C   
47   O O   . ILE   A 8   ? 0.5317 0.3970 0.5379 -0.0917 -0.0210 0.0733  814  ILE   A O   
48   C CB  . ILE   A 8   ? 0.4716 0.4257 0.5106 -0.0798 0.0094  0.0568  814  ILE   A CB  
49   C CG1 . ILE   A 8   ? 0.4872 0.4411 0.5275 -0.1008 0.0103  0.0599  814  ILE   A CG1 
50   C CG2 . ILE   A 8   ? 0.4076 0.3876 0.4638 -0.0660 0.0141  0.0453  814  ILE   A CG2 
51   C CD1 . ILE   A 8   ? 0.4884 0.4770 0.5367 -0.1142 0.0242  0.0582  814  ILE   A CD1 
52   N N   . SER   A 9   ? 0.5634 0.4491 0.5590 -0.0837 -0.0112 0.0786  815  SER   A N   
53   C CA  . SER   A 9   ? 0.5434 0.3990 0.5130 -0.0997 -0.0184 0.0930  815  SER   A CA  
54   C C   . SER   A 9   ? 0.5845 0.4576 0.5397 -0.1171 -0.0055 0.1006  815  SER   A C   
55   O O   . SER   A 9   ? 0.6501 0.4999 0.5796 -0.1368 -0.0091 0.1138  815  SER   A O   
56   C CB  . SER   A 9   ? 0.5893 0.4128 0.5471 -0.0853 -0.0352 0.0968  815  SER   A CB  
57   O OG  . SER   A 9   ? 0.6456 0.4481 0.6135 -0.0734 -0.0481 0.0896  815  SER   A OG  
58   N N   . GLY   A 10  ? 0.5580 0.4697 0.5268 -0.1116 0.0090  0.0924  816  GLY   A N   
59   C CA  . GLY   A 10  ? 0.5294 0.4581 0.4837 -0.1252 0.0210  0.0969  816  GLY   A CA  
60   C C   . GLY   A 10  ? 0.5290 0.5041 0.5041 -0.1245 0.0383  0.0846  816  GLY   A C   
61   O O   . GLY   A 10  ? 0.5099 0.5051 0.5056 -0.1290 0.0436  0.0771  816  GLY   A O   
62   N N   . THR   A 11  ? 0.5037 0.4946 0.4739 -0.1178 0.0451  0.0816  817  THR   A N   
63   C CA  . THR   A 11  ? 0.5042 0.5366 0.4898 -0.1177 0.0607  0.0694  817  THR   A CA  
64   C C   . THR   A 11  ? 0.4938 0.5473 0.5116 -0.1024 0.0609  0.0558  817  THR   A C   
65   O O   . THR   A 11  ? 0.4584 0.5453 0.4952 -0.1057 0.0707  0.0451  817  THR   A O   
66   C CB  . THR   A 11  ? 0.4950 0.5325 0.4686 -0.1087 0.0638  0.0676  817  THR   A CB  
67   O OG1 . THR   A 11  ? 0.5563 0.5748 0.4964 -0.1245 0.0631  0.0803  817  THR   A OG1 
68   C CG2 . THR   A 11  ? 0.4146 0.4926 0.4051 -0.1056 0.0780  0.0526  817  THR   A CG2 
69   N N   . GLY   A 12  ? 0.4344 0.4704 0.4584 -0.0857 0.0498  0.0550  818  GLY   A N   
70   C CA  . GLY   A 12  ? 0.4270 0.4765 0.4746 -0.0737 0.0480  0.0442  818  GLY   A CA  
71   C C   . GLY   A 12  ? 0.4337 0.5045 0.4925 -0.0594 0.0521  0.0335  818  GLY   A C   
72   O O   . GLY   A 12  ? 0.4387 0.5269 0.5167 -0.0534 0.0520  0.0237  818  GLY   A O   
73   N N   . SER   A 13  ? 0.3766 0.4438 0.4231 -0.0534 0.0536  0.0347  819  SER   A N   
74   C CA  . SER   A 13  ? 0.3448 0.4265 0.3999 -0.0400 0.0554  0.0245  819  SER   A CA  
75   C C   . SER   A 13  ? 0.3974 0.4664 0.4578 -0.0263 0.0464  0.0222  819  SER   A C   
76   O O   . SER   A 13  ? 0.3883 0.4664 0.4586 -0.0166 0.0448  0.0136  819  SER   A O   
77   C CB  . SER   A 13  ? 0.3544 0.4352 0.3934 -0.0393 0.0593  0.0258  819  SER   A CB  
78   O OG  . SER   A 13  ? 0.3722 0.4301 0.3986 -0.0337 0.0516  0.0327  819  SER   A OG  
79   N N   . ASN   A 14  ? 0.3656 0.4133 0.4186 -0.0254 0.0399  0.0290  820  ASN   A N   
80   C CA  . ASN   A 14  ? 0.3847 0.4240 0.4419 -0.0158 0.0337  0.0257  820  ASN   A CA  
81   C C   . ASN   A 14  ? 0.3675 0.4129 0.4371 -0.0167 0.0311  0.0210  820  ASN   A C   
82   O O   . ASN   A 14  ? 0.3050 0.3527 0.3791 -0.0090 0.0274  0.0151  820  ASN   A O   
83   C CB  . ASN   A 14  ? 0.3516 0.3722 0.4013 -0.0141 0.0286  0.0305  820  ASN   A CB  
84   C CG  . ASN   A 14  ? 0.3699 0.3871 0.4115 -0.0096 0.0284  0.0319  820  ASN   A CG  
85   O OD1 . ASN   A 14  ? 0.3632 0.3825 0.4046 -0.0038 0.0285  0.0278  820  ASN   A OD1 
86   N ND2 . ASN   A 14  ? 0.3907 0.4009 0.4238 -0.0134 0.0270  0.0381  820  ASN   A ND2 
87   N N   . LEU   A 15  ? 0.4301 0.4765 0.5037 -0.0270 0.0318  0.0238  821  LEU   A N   
88   C CA  . LEU   A 15  ? 0.3489 0.4051 0.4366 -0.0297 0.0293  0.0183  821  LEU   A CA  
89   C C   . LEU   A 15  ? 0.3742 0.4538 0.4758 -0.0237 0.0308  0.0088  821  LEU   A C   
90   O O   . LEU   A 15  ? 0.3862 0.4673 0.4954 -0.0162 0.0236  0.0027  821  LEU   A O   
91   C CB  . LEU   A 15  ? 0.3626 0.4204 0.4526 -0.0456 0.0317  0.0226  821  LEU   A CB  
92   C CG  . LEU   A 15  ? 0.4120 0.4854 0.5203 -0.0502 0.0293  0.0155  821  LEU   A CG  
93   C CD1 . LEU   A 15  ? 0.3660 0.4237 0.4736 -0.0414 0.0190  0.0125  821  LEU   A CD1 
94   C CD2 . LEU   A 15  ? 0.3793 0.4547 0.4893 -0.0699 0.0324  0.0200  821  LEU   A CD2 
95   N N   . GLN   A 16  ? 0.3515 0.4483 0.4554 -0.0260 0.0390  0.0065  822  GLN   A N   
96   C CA  . GLN   A 16  ? 0.3569 0.4775 0.4767 -0.0179 0.0398  -0.0055 822  GLN   A CA  
97   C C   . GLN   A 16  ? 0.3878 0.4944 0.5023 -0.0020 0.0308  -0.0086 822  GLN   A C   
98   O O   . GLN   A 16  ? 0.3535 0.4662 0.4798 0.0071  0.0226  -0.0170 822  GLN   A O   
99   C CB  . GLN   A 16  ? 0.3543 0.4942 0.4736 -0.0230 0.0514  -0.0085 822  GLN   A CB  
100  C CG  . GLN   A 16  ? 0.3107 0.4831 0.4522 -0.0157 0.0542  -0.0248 822  GLN   A CG  
101  C CD  . GLN   A 16  ? 0.3747 0.5676 0.5423 -0.0157 0.0492  -0.0337 822  GLN   A CD  
102  O OE1 . GLN   A 16  ? 0.3886 0.5837 0.5690 -0.0005 0.0381  -0.0430 822  GLN   A OE1 
103  N NE2 . GLN   A 16  ? 0.3447 0.5502 0.5189 -0.0334 0.0556  -0.0307 822  GLN   A NE2 
104  N N   . ALA   A 17  ? 0.3816 0.4683 0.4774 0.0006  0.0310  -0.0020 823  ALA   A N   
105  C CA  . ALA   A 17  ? 0.3841 0.4545 0.4707 0.0113  0.0231  -0.0033 823  ALA   A CA  
106  C C   . ALA   A 17  ? 0.4058 0.4632 0.4902 0.0135  0.0139  -0.0025 823  ALA   A C   
107  O O   . ALA   A 17  ? 0.3854 0.4345 0.4667 0.0216  0.0047  -0.0063 823  ALA   A O   
108  C CB  . ALA   A 17  ? 0.3617 0.4164 0.4307 0.0101  0.0260  0.0037  823  ALA   A CB  
109  N N   . LEU   A 18  ? 0.4024 0.4551 0.4859 0.0061  0.0149  0.0022  824  LEU   A N   
110  C CA  . LEU   A 18  ? 0.3838 0.4254 0.4636 0.0071  0.0069  0.0015  824  LEU   A CA  
111  C C   . LEU   A 18  ? 0.3776 0.4322 0.4731 0.0100  -0.0006 -0.0060 824  LEU   A C   
112  O O   . LEU   A 18  ? 0.3877 0.4324 0.4773 0.0161  -0.0113 -0.0087 824  LEU   A O   
113  C CB  . LEU   A 18  ? 0.3376 0.3710 0.4140 -0.0003 0.0093  0.0058  824  LEU   A CB  
114  C CG  . LEU   A 18  ? 0.3704 0.3910 0.4335 -0.0002 0.0133  0.0105  824  LEU   A CG  
115  C CD1 . LEU   A 18  ? 0.3351 0.3482 0.3987 -0.0051 0.0139  0.0129  824  LEU   A CD1 
116  C CD2 . LEU   A 18  ? 0.3237 0.3329 0.3726 0.0039  0.0101  0.0091  824  LEU   A CD2 
117  N N   . ILE   A 19  ? 0.3380 0.4151 0.4527 0.0045  0.0042  -0.0096 825  ILE   A N   
118  C CA  . ILE   A 19  ? 0.3414 0.4383 0.4773 0.0076  -0.0028 -0.0193 825  ILE   A CA  
119  C C   . ILE   A 19  ? 0.4026 0.4999 0.5405 0.0223  -0.0117 -0.0265 825  ILE   A C   
120  O O   . ILE   A 19  ? 0.4500 0.5441 0.5920 0.0302  -0.0258 -0.0319 825  ILE   A O   
121  C CB  . ILE   A 19  ? 0.3854 0.5127 0.5428 -0.0026 0.0072  -0.0234 825  ILE   A CB  
122  C CG1 . ILE   A 19  ? 0.3758 0.4961 0.5287 -0.0184 0.0121  -0.0155 825  ILE   A CG1 
123  C CG2 . ILE   A 19  ? 0.3424 0.4995 0.5285 0.0027  0.0009  -0.0375 825  ILE   A CG2 
124  C CD1 . ILE   A 19  ? 0.3604 0.4997 0.5201 -0.0329 0.0250  -0.0139 825  ILE   A CD1 
125  N N   . ASP   A 20  ? 0.3737 0.4719 0.5072 0.0265  -0.0056 -0.0268 826  ASP   A N   
126  C CA  . ASP   A 20  ? 0.3979 0.4954 0.5350 0.0411  -0.0151 -0.0354 826  ASP   A CA  
127  C C   . ASP   A 20  ? 0.4193 0.4832 0.5337 0.0477  -0.0300 -0.0306 826  ASP   A C   
128  O O   . ASP   A 20  ? 0.4214 0.4806 0.5403 0.0590  -0.0458 -0.0375 826  ASP   A O   
129  C CB  . ASP   A 20  ? 0.4031 0.5041 0.5360 0.0433  -0.0058 -0.0368 826  ASP   A CB  
130  C CG  . ASP   A 20  ? 0.4220 0.5601 0.5776 0.0390  0.0069  -0.0459 826  ASP   A CG  
131  O OD1 . ASP   A 20  ? 0.4164 0.5804 0.5944 0.0343  0.0084  -0.0522 826  ASP   A OD1 
132  O OD2 . ASP   A 20  ? 0.4028 0.5450 0.5526 0.0387  0.0159  -0.0472 826  ASP   A OD2 
133  N N   . SER   A 21  ? 0.4060 0.4466 0.4955 0.0401  -0.0259 -0.0194 827  SER   A N   
134  C CA  . SER   A 21  ? 0.4581 0.4677 0.5218 0.0422  -0.0376 -0.0144 827  SER   A CA  
135  C C   . SER   A 21  ? 0.4540 0.4590 0.5163 0.0415  -0.0485 -0.0154 827  SER   A C   
136  O O   . SER   A 21  ? 0.4753 0.4594 0.5221 0.0470  -0.0642 -0.0153 827  SER   A O   
137  C CB  . SER   A 21  ? 0.3827 0.3757 0.4235 0.0329  -0.0282 -0.0048 827  SER   A CB  
138  O OG  . SER   A 21  ? 0.3794 0.3815 0.4249 0.0244  -0.0188 -0.0020 827  SER   A OG  
139  N N   . THR   A 22  ? 0.4405 0.4614 0.5159 0.0341  -0.0421 -0.0160 828  THR   A N   
140  C CA  . THR   A 22  ? 0.4484 0.4623 0.5190 0.0322  -0.0526 -0.0171 828  THR   A CA  
141  C C   . THR   A 22  ? 0.4981 0.5259 0.5896 0.0412  -0.0678 -0.0268 828  THR   A C   
142  O O   . THR   A 22  ? 0.5028 0.5234 0.5894 0.0410  -0.0802 -0.0284 828  THR   A O   
143  C CB  . THR   A 22  ? 0.3758 0.3977 0.4522 0.0213  -0.0431 -0.0154 828  THR   A CB  
144  O OG1 . THR   A 22  ? 0.4212 0.4711 0.5267 0.0183  -0.0369 -0.0201 828  THR   A OG1 
145  C CG2 . THR   A 22  ? 0.3356 0.3456 0.3951 0.0148  -0.0304 -0.0083 828  THR   A CG2 
146  N N   . ARG   A 23  ? 0.5469 0.5965 0.6629 0.0493  -0.0675 -0.0348 829  ARG   A N   
147  C CA  . ARG   A 23  ? 0.5792 0.6437 0.7178 0.0611  -0.0842 -0.0468 829  ARG   A CA  
148  C C   . ARG   A 23  ? 0.6049 0.6433 0.7277 0.0758  -0.1027 -0.0481 829  ARG   A C   
149  O O   . ARG   A 23  ? 0.6204 0.6646 0.7589 0.0887  -0.1219 -0.0582 829  ARG   A O   
150  C CB  . ARG   A 23  ? 0.6276 0.7360 0.8059 0.0622  -0.0742 -0.0588 829  ARG   A CB  
151  C CG  . ARG   A 23  ? 0.6491 0.7816 0.8434 0.0457  -0.0604 -0.0579 829  ARG   A CG  
152  C CD  . ARG   A 23  ? 0.7097 0.8869 0.9401 0.0439  -0.0494 -0.0700 829  ARG   A CD  
153  N NE  . ARG   A 23  ? 0.7611 0.9400 0.9882 0.0512  -0.0412 -0.0721 829  ARG   A NE  
154  C CZ  . ARG   A 23  ? 0.7513 0.9600 0.9938 0.0447  -0.0238 -0.0773 829  ARG   A CZ  
155  N NH1 . ARG   A 23  ? 0.6830 0.9228 0.9456 0.0290  -0.0123 -0.0802 829  ARG   A NH1 
156  N NH2 . ARG   A 23  ? 0.6489 0.8552 0.8845 0.0523  -0.0182 -0.0798 829  ARG   A NH2 
157  N N   . GLU   A 24  ? 0.4980 0.5069 0.5903 0.0739  -0.0991 -0.0384 830  GLU   A N   
158  C CA  . GLU   A 24  ? 0.5048 0.4783 0.5727 0.0839  -0.1186 -0.0363 830  GLU   A CA  
159  C C   . GLU   A 24  ? 0.5154 0.4627 0.5584 0.0816  -0.1365 -0.0311 830  GLU   A C   
160  O O   . GLU   A 24  ? 0.5013 0.4458 0.5302 0.0683  -0.1278 -0.0244 830  GLU   A O   
161  C CB  . GLU   A 24  ? 0.5292 0.4767 0.5675 0.0774  -0.1094 -0.0260 830  GLU   A CB  
162  C CG  . GLU   A 24  ? 0.6465 0.6148 0.7047 0.0814  -0.0958 -0.0319 830  GLU   A CG  
163  C CD  . GLU   A 24  ? 0.7993 0.7635 0.8687 0.0999  -0.1114 -0.0434 830  GLU   A CD  
164  O OE1 . GLU   A 24  ? 0.8931 0.8295 0.9410 0.1016  -0.1148 -0.0395 830  GLU   A OE1 
165  O OE2 . GLU   A 24  ? 0.7748 0.7640 0.8759 0.1129  -0.1209 -0.0576 830  GLU   A OE2 
166  N N   . PRO   A 25  ? 0.5088 0.4356 0.5452 0.0950  -0.1626 -0.0349 831  PRO   A N   
167  C CA  . PRO   A 25  ? 0.5383 0.4424 0.5518 0.0931  -0.1821 -0.0311 831  PRO   A CA  
168  C C   . PRO   A 25  ? 0.5280 0.3972 0.4916 0.0756  -0.1760 -0.0157 831  PRO   A C   
169  O O   . PRO   A 25  ? 0.5334 0.3975 0.4822 0.0676  -0.1796 -0.0132 831  PRO   A O   
170  C CB  . PRO   A 25  ? 0.4919 0.3729 0.5027 0.1123  -0.2133 -0.0368 831  PRO   A CB  
171  C CG  . PRO   A 25  ? 0.4565 0.3658 0.5065 0.1267  -0.2075 -0.0500 831  PRO   A CG  
172  C CD  . PRO   A 25  ? 0.4998 0.4192 0.5460 0.1129  -0.1775 -0.0432 831  PRO   A CD  
173  N N   . ASN   A 26  ? 0.5412 0.3887 0.4793 0.0685  -0.1664 -0.0066 832  ASN   A N   
174  C CA  . ASN   A 26  ? 0.5768 0.3967 0.4698 0.0502  -0.1584 0.0061  832  ASN   A CA  
175  C C   . ASN   A 26  ? 0.5527 0.3996 0.4556 0.0372  -0.1313 0.0065  832  ASN   A C   
176  O O   . ASN   A 26  ? 0.5885 0.4208 0.4597 0.0224  -0.1222 0.0135  832  ASN   A O   
177  C CB  . ASN   A 26  ? 0.5721 0.3595 0.4350 0.0456  -0.1592 0.0149  832  ASN   A CB  
178  C CG  . ASN   A 26  ? 0.6576 0.3980 0.4854 0.0506  -0.1891 0.0202  832  ASN   A CG  
179  O OD1 . ASN   A 26  ? 0.7502 0.4790 0.5674 0.0543  -0.2081 0.0195  832  ASN   A OD1 
180  N ND2 . ASN   A 26  ? 0.7265 0.4366 0.5344 0.0506  -0.1955 0.0256  832  ASN   A ND2 
181  N N   . SER   A 27  ? 0.5010 0.3857 0.4457 0.0418  -0.1189 -0.0014 833  SER   A N   
182  C CA  . SER   A 27  ? 0.4622 0.3673 0.4157 0.0311  -0.0967 -0.0009 833  SER   A CA  
183  C C   . SER   A 27  ? 0.5047 0.4019 0.4388 0.0222  -0.0984 -0.0003 833  SER   A C   
184  O O   . SER   A 27  ? 0.4964 0.3922 0.4328 0.0264  -0.1142 -0.0046 833  SER   A O   
185  C CB  . SER   A 27  ? 0.4287 0.3705 0.4258 0.0360  -0.0878 -0.0087 833  SER   A CB  
186  O OG  . SER   A 27  ? 0.4351 0.3900 0.4380 0.0262  -0.0711 -0.0077 833  SER   A OG  
187  N N   . SER   A 28  ? 0.4972 0.3913 0.4136 0.0105  -0.0824 0.0031  834  SER   A N   
188  C CA  . SER   A 28  ? 0.5097 0.4005 0.4099 0.0022  -0.0801 0.0008  834  SER   A CA  
189  C C   . SER   A 28  ? 0.4774 0.3933 0.4073 0.0018  -0.0683 -0.0057 834  SER   A C   
190  O O   . SER   A 28  ? 0.5079 0.4224 0.4280 -0.0040 -0.0649 -0.0098 834  SER   A O   
191  C CB  . SER   A 28  ? 0.5951 0.4695 0.4581 -0.0105 -0.0698 0.0055  834  SER   A CB  
192  O OG  . SER   A 28  ? 0.5632 0.4065 0.3889 -0.0142 -0.0841 0.0127  834  SER   A OG  
193  N N   . ALA   A 29  ? 0.4339 0.3705 0.3974 0.0073  -0.0628 -0.0070 835  ALA   A N   
194  C CA  . ALA   A 29  ? 0.4394 0.3950 0.4283 0.0052  -0.0530 -0.0109 835  ALA   A CA  
195  C C   . ALA   A 29  ? 0.4748 0.4489 0.4943 0.0096  -0.0609 -0.0154 835  ALA   A C   
196  O O   . ALA   A 29  ? 0.4442 0.4249 0.4749 0.0170  -0.0679 -0.0161 835  ALA   A O   
197  C CB  . ALA   A 29  ? 0.4441 0.4085 0.4424 0.0038  -0.0370 -0.0076 835  ALA   A CB  
198  N N   . GLN   A 30  ? 0.4510 0.4340 0.4843 0.0047  -0.0601 -0.0197 836  GLN   A N   
199  C CA  . GLN   A 30  ? 0.4136 0.4192 0.4789 0.0044  -0.0636 -0.0243 836  GLN   A CA  
200  C C   . GLN   A 30  ? 0.4347 0.4480 0.5132 -0.0043 -0.0509 -0.0230 836  GLN   A C   
201  O O   . GLN   A 30  ? 0.4236 0.4230 0.4897 -0.0089 -0.0480 -0.0231 836  GLN   A O   
202  C CB  . GLN   A 30  ? 0.3940 0.3995 0.4616 0.0047  -0.0805 -0.0310 836  GLN   A CB  
203  C CG  . GLN   A 30  ? 0.3969 0.3899 0.4517 -0.0031 -0.0809 -0.0334 836  GLN   A CG  
204  C CD  . GLN   A 30  ? 0.4203 0.4155 0.4800 -0.0037 -0.0982 -0.0407 836  GLN   A CD  
205  O OE1 . GLN   A 30  ? 0.4764 0.4525 0.5090 -0.0023 -0.1092 -0.0420 836  GLN   A OE1 
206  N NE2 . GLN   A 30  ? 0.3529 0.3725 0.4462 -0.0072 -0.1011 -0.0458 836  GLN   A NE2 
207  N N   . ILE   A 31  ? 0.3447 0.3782 0.4459 -0.0065 -0.0437 -0.0221 837  ILE   A N   
208  C CA  . ILE   A 31  ? 0.3662 0.4028 0.4757 -0.0165 -0.0334 -0.0187 837  ILE   A CA  
209  C C   . ILE   A 31  ? 0.3690 0.4165 0.4964 -0.0261 -0.0390 -0.0237 837  ILE   A C   
210  O O   . ILE   A 31  ? 0.4366 0.5098 0.5873 -0.0283 -0.0405 -0.0284 837  ILE   A O   
211  C CB  . ILE   A 31  ? 0.3782 0.4294 0.4976 -0.0175 -0.0221 -0.0146 837  ILE   A CB  
212  C CG1 . ILE   A 31  ? 0.3494 0.3871 0.4501 -0.0101 -0.0168 -0.0095 837  ILE   A CG1 
213  C CG2 . ILE   A 31  ? 0.3208 0.3736 0.4468 -0.0307 -0.0147 -0.0104 837  ILE   A CG2 
214  C CD1 . ILE   A 31  ? 0.3131 0.3647 0.4208 -0.0076 -0.0093 -0.0078 837  ILE   A CD1 
215  N N   . ASP   A 32  ? 0.3772 0.4069 0.4955 -0.0324 -0.0419 -0.0241 838  ASP   A N   
216  C CA  . ASP   A 32  ? 0.4182 0.4534 0.5501 -0.0423 -0.0499 -0.0296 838  ASP   A CA  
217  C C   . ASP   A 32  ? 0.4377 0.4703 0.5772 -0.0576 -0.0436 -0.0252 838  ASP   A C   
218  O O   . ASP   A 32  ? 0.4193 0.4591 0.5727 -0.0699 -0.0488 -0.0289 838  ASP   A O   
219  C CB  . ASP   A 32  ? 0.3408 0.3548 0.4547 -0.0393 -0.0608 -0.0351 838  ASP   A CB  
220  C CG  . ASP   A 32  ? 0.4048 0.4181 0.5066 -0.0278 -0.0695 -0.0382 838  ASP   A CG  
221  O OD1 . ASP   A 32  ? 0.4673 0.4605 0.5424 -0.0223 -0.0697 -0.0379 838  ASP   A OD1 
222  O OD2 . ASP   A 32  ? 0.3853 0.4187 0.5042 -0.0244 -0.0765 -0.0414 838  ASP   A OD2 
223  N N   . ILE   A 33  ? 0.4162 0.4375 0.5458 -0.0583 -0.0339 -0.0170 839  ILE   A N   
224  C CA  . ILE   A 33  ? 0.4019 0.4128 0.5317 -0.0730 -0.0301 -0.0105 839  ILE   A CA  
225  C C   . ILE   A 33  ? 0.4222 0.4284 0.5424 -0.0701 -0.0202 -0.0016 839  ILE   A C   
226  O O   . ILE   A 33  ? 0.3701 0.3692 0.4792 -0.0563 -0.0184 -0.0012 839  ILE   A O   
227  C CB  . ILE   A 33  ? 0.3963 0.3752 0.5136 -0.0757 -0.0391 -0.0126 839  ILE   A CB  
228  C CG1 . ILE   A 33  ? 0.4494 0.4094 0.5628 -0.0913 -0.0383 -0.0043 839  ILE   A CG1 
229  C CG2 . ILE   A 33  ? 0.4229 0.3827 0.5219 -0.0594 -0.0398 -0.0151 839  ILE   A CG2 
230  C CD1 . ILE   A 33  ? 0.4192 0.4003 0.5489 -0.1120 -0.0349 -0.0016 839  ILE   A CD1 
231  N N   . VAL   A 34  ? 0.4161 0.4271 0.5397 -0.0849 -0.0138 0.0056  840  VAL   A N   
232  C CA  . VAL   A 34  ? 0.3653 0.3664 0.4757 -0.0851 -0.0067 0.0153  840  VAL   A CA  
233  C C   . VAL   A 34  ? 0.4479 0.4198 0.5460 -0.1001 -0.0109 0.0238  840  VAL   A C   
234  O O   . VAL   A 34  ? 0.4923 0.4686 0.5963 -0.1195 -0.0108 0.0256  840  VAL   A O   
235  C CB  . VAL   A 34  ? 0.4206 0.4530 0.5404 -0.0893 0.0049  0.0165  840  VAL   A CB  
236  C CG1 . VAL   A 34  ? 0.4469 0.4663 0.5496 -0.0964 0.0112  0.0280  840  VAL   A CG1 
237  C CG2 . VAL   A 34  ? 0.3493 0.3988 0.4752 -0.0708 0.0061  0.0095  840  VAL   A CG2 
238  N N   . ILE   A 35  ? 0.4415 0.3831 0.5228 -0.0916 -0.0158 0.0283  841  ILE   A N   
239  C CA  . ILE   A 35  ? 0.5167 0.4211 0.5834 -0.1015 -0.0248 0.0358  841  ILE   A CA  
240  C C   . ILE   A 35  ? 0.5465 0.4375 0.5970 -0.1024 -0.0227 0.0473  841  ILE   A C   
241  O O   . ILE   A 35  ? 0.4991 0.3903 0.5467 -0.0853 -0.0220 0.0459  841  ILE   A O   
242  C CB  . ILE   A 35  ? 0.5113 0.3875 0.5737 -0.0880 -0.0372 0.0277  841  ILE   A CB  
243  C CG1 . ILE   A 35  ? 0.4931 0.3809 0.5672 -0.0873 -0.0402 0.0160  841  ILE   A CG1 
244  C CG2 . ILE   A 35  ? 0.5556 0.3889 0.6030 -0.0966 -0.0497 0.0343  841  ILE   A CG2 
245  C CD1 . ILE   A 35  ? 0.5313 0.3941 0.5995 -0.0742 -0.0508 0.0053  841  ILE   A CD1 
246  N N   . SER   A 36  ? 0.5725 0.4511 0.6108 -0.1238 -0.0225 0.0589  842  SER   A N   
247  C CA  . SER   A 36  ? 0.6153 0.4762 0.6325 -0.1277 -0.0228 0.0715  842  SER   A CA  
248  C C   . SER   A 36  ? 0.6335 0.4443 0.6290 -0.1383 -0.0386 0.0815  842  SER   A C   
249  O O   . SER   A 36  ? 0.6577 0.4551 0.6517 -0.1560 -0.0431 0.0832  842  SER   A O   
250  C CB  . SER   A 36  ? 0.6404 0.5301 0.6551 -0.1461 -0.0076 0.0778  842  SER   A CB  
251  O OG  . SER   A 36  ? 0.6655 0.5298 0.6524 -0.1562 -0.0102 0.0922  842  SER   A OG  
252  N N   . ASN   A 37  ? 0.7167 0.4983 0.6951 -0.1277 -0.0487 0.0879  843  ASN   A N   
253  C CA  . ASN   A 37  ? 0.7556 0.4835 0.7105 -0.1358 -0.0674 0.0981  843  ASN   A CA  
254  C C   . ASN   A 37  ? 0.8196 0.5314 0.7457 -0.1627 -0.0658 0.1168  843  ASN   A C   
255  O O   . ASN   A 37  ? 0.9330 0.5950 0.8339 -0.1746 -0.0825 0.1283  843  ASN   A O   
256  C CB  . ASN   A 37  ? 0.7685 0.4692 0.7205 -0.1094 -0.0836 0.0940  843  ASN   A CB  
257  C CG  . ASN   A 37  ? 0.7604 0.4694 0.7033 -0.1016 -0.0808 0.1005  843  ASN   A CG  
258  O OD1 . ASN   A 37  ? 0.7009 0.4499 0.6513 -0.1034 -0.0633 0.0996  843  ASN   A OD1 
259  N ND2 . ASN   A 37  ? 0.8347 0.5049 0.7620 -0.0915 -0.1000 0.1057  843  ASN   A ND2 
260  N N   . LYS   A 38  ? 0.7657 0.5168 0.6932 -0.1728 -0.0467 0.1195  844  LYS   A N   
261  C CA  . LYS   A 38  ? 0.8163 0.5609 0.7151 -0.2004 -0.0406 0.1355  844  LYS   A CA  
262  C C   . LYS   A 38  ? 0.7526 0.5457 0.6670 -0.2220 -0.0186 0.1310  844  LYS   A C   
263  O O   . LYS   A 38  ? 0.7250 0.5650 0.6691 -0.2084 -0.0054 0.1168  844  LYS   A O   
264  C CB  . LYS   A 38  ? 0.8371 0.5820 0.7189 -0.1903 -0.0397 0.1417  844  LYS   A CB  
265  C CG  . LYS   A 38  ? 0.9141 0.6078 0.7773 -0.1732 -0.0645 0.1480  844  LYS   A CG  
266  C CD  . LYS   A 38  ? 1.0180 0.6598 0.8445 -0.1968 -0.0794 0.1648  844  LYS   A CD  
267  C CE  . LYS   A 38  ? 1.0429 0.6583 0.8792 -0.1955 -0.0925 0.1589  844  LYS   A CE  
268  N NZ  . LYS   A 38  ? 1.1201 0.6937 0.9265 -0.2075 -0.1080 0.1681  844  LYS   A NZ  
269  N N   . ALA   A 39  ? 0.7838 0.5647 0.6791 -0.2558 -0.0159 0.1421  845  ALA   A N   
270  C CA  . ALA   A 39  ? 0.7405 0.5726 0.6547 -0.2764 0.0051  0.1349  845  ALA   A CA  
271  C C   . ALA   A 39  ? 0.7746 0.6431 0.6805 -0.2829 0.0243  0.1354  845  ALA   A C   
272  O O   . ALA   A 39  ? 0.7949 0.6416 0.6724 -0.2779 0.0201  0.1448  845  ALA   A O   
273  C CB  . ALA   A 39  ? 0.6694 0.4863 0.5740 -0.2988 0.0018  0.1384  845  ALA   A CB  
274  N N   . ALA   A 40  ? 0.7202 0.6458 0.6526 -0.2923 0.0444  0.1231  846  ALA   A N   
275  C CA  . ALA   A 40  ? 0.6660 0.6328 0.5956 -0.2980 0.0642  0.1186  846  ALA   A CA  
276  C C   . ALA   A 40  ? 0.6722 0.6511 0.6031 -0.2776 0.0680  0.1158  846  ALA   A C   
277  O O   . ALA   A 40  ? 0.6633 0.6683 0.5860 -0.2798 0.0819  0.1124  846  ALA   A O   
278  C CB  . ALA   A 40  ? 0.6803 0.6227 0.5690 -0.3178 0.0642  0.1313  846  ALA   A CB  
279  N N   . VAL   A 41  ? 0.6462 0.6079 0.5896 -0.2479 0.0541  0.1120  847  VAL   A N   
280  C CA  . VAL   A 41  ? 0.6030 0.5789 0.5522 -0.2210 0.0563  0.1050  847  VAL   A CA  
281  C C   . VAL   A 41  ? 0.5537 0.5858 0.5411 -0.2091 0.0704  0.0853  847  VAL   A C   
282  O O   . VAL   A 41  ? 0.5767 0.6316 0.5918 -0.2121 0.0727  0.0757  847  VAL   A O   
283  C CB  . VAL   A 41  ? 0.6155 0.5548 0.5637 -0.1937 0.0369  0.1067  847  VAL   A CB  
284  C CG1 . VAL   A 41  ? 0.7065 0.5891 0.6215 -0.2040 0.0194  0.1238  847  VAL   A CG1 
285  C CG2 . VAL   A 41  ? 0.5570 0.5063 0.5374 -0.1775 0.0319  0.0942  847  VAL   A CG2 
286  N N   . ALA   A 42  ? 0.5139 0.5666 0.5022 -0.1949 0.0781  0.0789  848  ALA   A N   
287  C CA  . ALA   A 42  ? 0.4682 0.5715 0.4888 -0.1835 0.0904  0.0601  848  ALA   A CA  
288  C C   . ALA   A 42  ? 0.5150 0.6227 0.5653 -0.1588 0.0807  0.0493  848  ALA   A C   
289  O O   . ALA   A 42  ? 0.4863 0.6323 0.5664 -0.1521 0.0868  0.0339  848  ALA   A O   
290  C CB  . ALA   A 42  ? 0.4442 0.5600 0.4541 -0.1735 0.0982  0.0562  848  ALA   A CB  
291  N N   . GLY   A 43  ? 0.4788 0.5491 0.5209 -0.1447 0.0655  0.0560  849  GLY   A N   
292  C CA  . GLY   A 43  ? 0.4798 0.5522 0.5443 -0.1250 0.0570  0.0466  849  GLY   A CA  
293  C C   . GLY   A 43  ? 0.4799 0.5662 0.5654 -0.1348 0.0557  0.0406  849  GLY   A C   
294  O O   . GLY   A 43  ? 0.4487 0.5533 0.5575 -0.1216 0.0527  0.0288  849  GLY   A O   
295  N N   . LEU   A 44  ? 0.5165 0.5924 0.5923 -0.1592 0.0566  0.0488  850  LEU   A N   
296  C CA  . LEU   A 44  ? 0.5032 0.5944 0.6001 -0.1713 0.0554  0.0425  850  LEU   A CA  
297  C C   . LEU   A 44  ? 0.5189 0.6660 0.6455 -0.1751 0.0686  0.0275  850  LEU   A C   
298  O O   . LEU   A 44  ? 0.5483 0.7175 0.7031 -0.1705 0.0646  0.0156  850  LEU   A O   
299  C CB  . LEU   A 44  ? 0.4675 0.5314 0.5446 -0.1995 0.0529  0.0555  850  LEU   A CB  
300  C CG  . LEU   A 44  ? 0.5406 0.5471 0.5936 -0.1961 0.0355  0.0674  850  LEU   A CG  
301  C CD1 . LEU   A 44  ? 0.5480 0.5234 0.5753 -0.2262 0.0326  0.0822  850  LEU   A CD1 
302  C CD2 . LEU   A 44  ? 0.4934 0.4911 0.5636 -0.1806 0.0231  0.0585  850  LEU   A CD2 
303  N N   . ASP   A 45  ? 0.4772 0.6484 0.5986 -0.1823 0.0834  0.0261  851  ASP   A N   
304  C CA  . ASP   A 45  ? 0.4770 0.7052 0.6297 -0.1831 0.0964  0.0083  851  ASP   A CA  
305  C C   . ASP   A 45  ? 0.4621 0.7057 0.6392 -0.1517 0.0890  -0.0064 851  ASP   A C   
306  O O   . ASP   A 45  ? 0.4343 0.7122 0.6451 -0.1464 0.0873  -0.0217 851  ASP   A O   
307  C CB  . ASP   A 45  ? 0.4746 0.7226 0.6124 -0.1953 0.1139  0.0085  851  ASP   A CB  
308  C CG  . ASP   A 45  ? 0.5706 0.8202 0.6912 -0.2320 0.1248  0.0182  851  ASP   A CG  
309  O OD1 . ASP   A 45  ? 0.7186 0.9552 0.8062 -0.2443 0.1329  0.0285  851  ASP   A OD1 
310  O OD2 . ASP   A 45  ? 0.5939 0.8544 0.7312 -0.2490 0.1238  0.0162  851  ASP   A OD2 
311  N N   . LYS   A 46  ? 0.5132 0.7319 0.6729 -0.1317 0.0838  -0.0019 852  LYS   A N   
312  C CA  . LYS   A 46  ? 0.4710 0.6943 0.6460 -0.1040 0.0750  -0.0127 852  LYS   A CA  
313  C C   . LYS   A 46  ? 0.4400 0.6559 0.6303 -0.0969 0.0608  -0.0161 852  LYS   A C   
314  O O   . LYS   A 46  ? 0.4311 0.6700 0.6464 -0.0832 0.0549  -0.0299 852  LYS   A O   
315  C CB  . LYS   A 46  ? 0.4173 0.6071 0.5667 -0.0889 0.0703  -0.0040 852  LYS   A CB  
316  C CG  . LYS   A 46  ? 0.4808 0.6809 0.6180 -0.0888 0.0816  -0.0050 852  LYS   A CG  
317  C CD  . LYS   A 46  ? 0.4710 0.6329 0.5798 -0.0802 0.0756  0.0072  852  LYS   A CD  
318  C CE  . LYS   A 46  ? 0.3785 0.5452 0.4693 -0.0842 0.0855  0.0087  852  LYS   A CE  
319  N NZ  . LYS   A 46  ? 0.4117 0.5894 0.4922 -0.1095 0.0970  0.0139  852  LYS   A NZ  
320  N N   . ALA   A 47  ? 0.4327 0.6150 0.6071 -0.1054 0.0535  -0.0043 853  ALA   A N   
321  C CA  . ALA   A 47  ? 0.4262 0.5993 0.6114 -0.0994 0.0399  -0.0081 853  ALA   A CA  
322  C C   . ALA   A 47  ? 0.4413 0.6517 0.6574 -0.1108 0.0408  -0.0198 853  ALA   A C   
323  O O   . ALA   A 47  ? 0.4274 0.6510 0.6637 -0.0981 0.0304  -0.0309 853  ALA   A O   
324  C CB  . ALA   A 47  ? 0.4371 0.5672 0.5995 -0.1063 0.0323  0.0044  853  ALA   A CB  
325  N N   . GLU   A 48  ? 0.4520 0.6807 0.6718 -0.1357 0.0526  -0.0177 854  GLU   A N   
326  C CA  . GLU   A 48  ? 0.4603 0.7316 0.7135 -0.1489 0.0552  -0.0306 854  GLU   A CA  
327  C C   . GLU   A 48  ? 0.4264 0.7470 0.7114 -0.1342 0.0601  -0.0496 854  GLU   A C   
328  O O   . GLU   A 48  ? 0.3711 0.7233 0.6898 -0.1291 0.0530  -0.0647 854  GLU   A O   
329  C CB  . GLU   A 48  ? 0.4485 0.7264 0.6944 -0.1831 0.0681  -0.0229 854  GLU   A CB  
330  C CG  . GLU   A 48  ? 0.5726 0.7950 0.7856 -0.1954 0.0596  -0.0045 854  GLU   A CG  
331  C CD  . GLU   A 48  ? 0.7082 0.9260 0.9067 -0.2315 0.0690  0.0061  854  GLU   A CD  
332  O OE1 . GLU   A 48  ? 0.7168 0.9755 0.9253 -0.2495 0.0862  0.0010  854  GLU   A OE1 
333  O OE2 . GLU   A 48  ? 0.7182 0.8895 0.8932 -0.2421 0.0587  0.0193  854  GLU   A OE2 
334  N N   . ARG   A 49  ? 0.4363 0.7629 0.7118 -0.1255 0.0701  -0.0504 855  ARG   A N   
335  C CA  . ARG   A 49  ? 0.4527 0.8214 0.7579 -0.1075 0.0721  -0.0704 855  ARG   A CA  
336  C C   . ARG   A 49  ? 0.3909 0.7457 0.7054 -0.0789 0.0515  -0.0769 855  ARG   A C   
337  O O   . ARG   A 49  ? 0.3842 0.7730 0.7315 -0.0645 0.0451  -0.0955 855  ARG   A O   
338  C CB  . ARG   A 49  ? 0.4993 0.8710 0.7878 -0.1037 0.0857  -0.0698 855  ARG   A CB  
339  C CG  . ARG   A 49  ? 0.5685 0.9852 0.8872 -0.0864 0.0899  -0.0928 855  ARG   A CG  
340  C CD  . ARG   A 49  ? 0.6607 1.0972 0.9676 -0.0959 0.1106  -0.0957 855  ARG   A CD  
341  N NE  . ARG   A 49  ? 0.6673 1.0594 0.9284 -0.1076 0.1153  -0.0731 855  ARG   A NE  
342  C CZ  . ARG   A 49  ? 0.7032 1.0546 0.9382 -0.0905 0.1066  -0.0633 855  ARG   A CZ  
343  N NH1 . ARG   A 49  ? 0.7290 1.0748 0.9753 -0.0629 0.0936  -0.0725 855  ARG   A NH1 
344  N NH2 . ARG   A 49  ? 0.6226 0.9380 0.8199 -0.1018 0.1097  -0.0442 855  ARG   A NH2 
345  N N   . ALA   A 50  ? 0.4113 0.7168 0.6969 -0.0711 0.0402  -0.0627 856  ALA   A N   
346  C CA  . ALA   A 50  ? 0.3970 0.6831 0.6822 -0.0479 0.0213  -0.0660 856  ALA   A CA  
347  C C   . ALA   A 50  ? 0.3873 0.6739 0.6865 -0.0508 0.0071  -0.0696 856  ALA   A C   
348  O O   . ALA   A 50  ? 0.3896 0.6625 0.6883 -0.0333 -0.0101 -0.0735 856  ALA   A O   
349  C CB  . ALA   A 50  ? 0.3246 0.5616 0.5720 -0.0397 0.0176  -0.0507 856  ALA   A CB  
350  N N   . GLY   A 51  ? 0.3629 0.6623 0.6715 -0.0737 0.0129  -0.0682 857  GLY   A N   
351  C CA  . GLY   A 51  ? 0.3281 0.6281 0.6499 -0.0783 -0.0008 -0.0723 857  GLY   A CA  
352  C C   . GLY   A 51  ? 0.3298 0.5809 0.6202 -0.0827 -0.0085 -0.0583 857  GLY   A C   
353  O O   . GLY   A 51  ? 0.4049 0.6499 0.7008 -0.0843 -0.0219 -0.0619 857  GLY   A O   
354  N N   . ILE   A 52  ? 0.3349 0.5524 0.5938 -0.0841 -0.0012 -0.0442 858  ILE   A N   
355  C CA  . ILE   A 52  ? 0.3598 0.5321 0.5905 -0.0831 -0.0090 -0.0341 858  ILE   A CA  
356  C C   . ILE   A 52  ? 0.3901 0.5494 0.6146 -0.1069 -0.0053 -0.0266 858  ILE   A C   
357  O O   . ILE   A 52  ? 0.4273 0.5898 0.6462 -0.1217 0.0073  -0.0193 858  ILE   A O   
358  C CB  . ILE   A 52  ? 0.3631 0.5077 0.5664 -0.0700 -0.0052 -0.0251 858  ILE   A CB  
359  C CG1 . ILE   A 52  ? 0.3325 0.4893 0.5413 -0.0497 -0.0089 -0.0322 858  ILE   A CG1 
360  C CG2 . ILE   A 52  ? 0.3744 0.4783 0.5525 -0.0665 -0.0130 -0.0186 858  ILE   A CG2 
361  C CD1 . ILE   A 52  ? 0.4076 0.5394 0.5909 -0.0383 -0.0056 -0.0243 858  ILE   A CD1 
362  N N   . PRO   A 53  ? 0.3461 0.4870 0.5680 -0.1119 -0.0170 -0.0277 859  PRO   A N   
363  C CA  . PRO   A 53  ? 0.3729 0.4910 0.5839 -0.1336 -0.0163 -0.0197 859  PRO   A CA  
364  C C   . PRO   A 53  ? 0.4457 0.5298 0.6276 -0.1341 -0.0101 -0.0059 859  PRO   A C   
365  O O   . PRO   A 53  ? 0.4395 0.5083 0.6065 -0.1154 -0.0103 -0.0035 859  PRO   A O   
366  C CB  . PRO   A 53  ? 0.3810 0.4747 0.5863 -0.1296 -0.0325 -0.0243 859  PRO   A CB  
367  C CG  . PRO   A 53  ? 0.3962 0.5064 0.6118 -0.1099 -0.0411 -0.0348 859  PRO   A CG  
368  C CD  . PRO   A 53  ? 0.3940 0.5205 0.6109 -0.0955 -0.0322 -0.0338 859  PRO   A CD  
369  N N   . THR   A 54  ? 0.4486 0.5194 0.6216 -0.1569 -0.0061 0.0032  860  THR   A N   
370  C CA  . THR   A 54  ? 0.4359 0.4730 0.5809 -0.1601 -0.0029 0.0170  860  THR   A CA  
371  C C   . THR   A 54  ? 0.4936 0.4898 0.6225 -0.1763 -0.0130 0.0241  860  THR   A C   
372  O O   . THR   A 54  ? 0.5243 0.5272 0.6643 -0.1956 -0.0160 0.0213  860  THR   A O   
373  C CB  . THR   A 54  ? 0.4709 0.5313 0.6149 -0.1739 0.0129  0.0232  860  THR   A CB  
374  O OG1 . THR   A 54  ? 0.5686 0.6601 0.7310 -0.1989 0.0197  0.0195  860  THR   A OG1 
375  C CG2 . THR   A 54  ? 0.4295 0.5203 0.5840 -0.1543 0.0210  0.0163  860  THR   A CG2 
376  N N   . ARG   A 55  ? 0.4864 0.4398 0.5904 -0.1678 -0.0197 0.0322  861  ARG   A N   
377  C CA  . ARG   A 55  ? 0.4942 0.4018 0.5786 -0.1824 -0.0307 0.0406  861  ARG   A CA  
378  C C   . ARG   A 55  ? 0.5734 0.4513 0.6319 -0.1816 -0.0307 0.0543  861  ARG   A C   
379  O O   . ARG   A 55  ? 0.5741 0.4551 0.6294 -0.1604 -0.0281 0.0534  861  ARG   A O   
380  C CB  . ARG   A 55  ? 0.5171 0.3935 0.5981 -0.1682 -0.0464 0.0321  861  ARG   A CB  
381  C CG  . ARG   A 55  ? 0.5087 0.4084 0.6105 -0.1654 -0.0499 0.0179  861  ARG   A CG  
382  C CD  . ARG   A 55  ? 0.5487 0.4625 0.6635 -0.1935 -0.0501 0.0179  861  ARG   A CD  
383  N NE  . ARG   A 55  ? 0.6478 0.5601 0.7733 -0.1926 -0.0618 0.0056  861  ARG   A NE  
384  C CZ  . ARG   A 55  ? 0.6805 0.6335 0.8313 -0.1928 -0.0608 -0.0053 861  ARG   A CZ  
385  N NH1 . ARG   A 55  ? 0.5431 0.5425 0.7135 -0.1922 -0.0482 -0.0067 861  ARG   A NH1 
386  N NH2 . ARG   A 55  ? 0.6799 0.6263 0.8362 -0.1922 -0.0738 -0.0160 861  ARG   A NH2 
387  N N   . VAL   A 56  ? 0.5873 0.4351 0.6259 -0.2056 -0.0349 0.0671  862  VAL   A N   
388  C CA  . VAL   A 56  ? 0.6464 0.4577 0.6558 -0.2067 -0.0396 0.0816  862  VAL   A CA  
389  C C   . VAL   A 56  ? 0.7061 0.4582 0.6974 -0.2046 -0.0610 0.0847  862  VAL   A C   
390  O O   . VAL   A 56  ? 0.6805 0.4101 0.6654 -0.2266 -0.0686 0.0882  862  VAL   A O   
391  C CB  . VAL   A 56  ? 0.6373 0.4557 0.6306 -0.2375 -0.0285 0.0957  862  VAL   A CB  
392  C CG1 . VAL   A 56  ? 0.6864 0.4496 0.6415 -0.2437 -0.0410 0.1129  862  VAL   A CG1 
393  C CG2 . VAL   A 56  ? 0.6598 0.5299 0.6659 -0.2323 -0.0089 0.0918  862  VAL   A CG2 
394  N N   . ILE   A 57  ? 0.7159 0.4433 0.7000 -0.1784 -0.0714 0.0823  863  ILE   A N   
395  C CA  . ILE   A 57  ? 0.8230 0.4943 0.7922 -0.1711 -0.0935 0.0823  863  ILE   A CA  
396  C C   . ILE   A 57  ? 0.9552 0.5878 0.8956 -0.1732 -0.1034 0.0981  863  ILE   A C   
397  O O   . ILE   A 57  ? 0.9859 0.6270 0.9265 -0.1532 -0.1018 0.0975  863  ILE   A O   
398  C CB  . ILE   A 57  ? 0.7993 0.4725 0.7843 -0.1388 -0.0997 0.0639  863  ILE   A CB  
399  C CG1 . ILE   A 57  ? 0.7360 0.4402 0.7429 -0.1390 -0.0931 0.0497  863  ILE   A CG1 
400  C CG2 . ILE   A 57  ? 0.8342 0.4500 0.8050 -0.1284 -0.1232 0.0616  863  ILE   A CG2 
401  C CD1 . ILE   A 57  ? 0.7121 0.4296 0.7324 -0.1097 -0.0934 0.0319  863  ILE   A CD1 
402  N N   . ASN   A 58  ? 1.1232 0.7137 1.0377 -0.1973 -0.1144 0.1119  864  ASN   A N   
403  C CA  . ASN   A 58  ? 1.2177 0.7775 1.1020 -0.1963 -0.1239 0.1251  864  ASN   A CA  
404  C C   . ASN   A 58  ? 1.2544 0.7718 1.1345 -0.1677 -0.1479 0.1179  864  ASN   A C   
405  O O   . ASN   A 58  ? 1.2587 0.7480 1.1376 -0.1649 -0.1618 0.1112  864  ASN   A O   
406  C CB  . ASN   A 58  ? 1.2817 0.8280 1.1418 -0.2260 -0.1231 0.1374  864  ASN   A CB  
407  C CG  . ASN   A 58  ? 1.3064 0.8390 1.1346 -0.2341 -0.1243 0.1531  864  ASN   A CG  
408  O OD1 . ASN   A 58  ? 1.3504 0.8644 1.1695 -0.2134 -0.1359 0.1549  864  ASN   A OD1 
409  N ND2 . ASN   A 58  ? 1.3829 0.9251 1.1936 -0.2644 -0.1133 0.1635  864  ASN   A ND2 
410  N N   . HIS   A 59  ? 1.2900 0.8046 1.1686 -0.1462 -0.1531 0.1181  865  HIS   A N   
411  C CA  . HIS   A 59  ? 1.3049 0.7872 1.1842 -0.1172 -0.1755 0.1085  865  HIS   A CA  
412  C C   . HIS   A 59  ? 1.3657 0.8056 1.2132 -0.1242 -0.1941 0.1204  865  HIS   A C   
413  O O   . HIS   A 59  ? 1.3885 0.8054 1.2316 -0.1023 -0.2129 0.1168  865  HIS   A O   
414  C CB  . HIS   A 59  ? 1.2995 0.7986 1.1935 -0.0905 -0.1752 0.1018  865  HIS   A CB  
415  C CG  . HIS   A 59  ? 1.3564 0.8654 1.2327 -0.0993 -0.1686 0.1177  865  HIS   A CG  
416  N ND1 . HIS   A 59  ? 1.2663 0.8155 1.1480 -0.1126 -0.1457 0.1232  865  HIS   A ND1 
417  C CD2 . HIS   A 59  ? 1.4133 0.9001 1.2666 -0.0960 -0.1819 0.1273  865  HIS   A CD2 
418  C CE1 . HIS   A 59  ? 1.3059 0.8532 1.1667 -0.1179 -0.1453 0.1364  865  HIS   A CE1 
419  N NE2 . HIS   A 59  ? 1.3958 0.9065 1.2390 -0.1080 -0.1670 0.1389  865  HIS   A NE2 
420  N N   . LYS   A 60  ? 1.3601 0.7909 1.1861 -0.1551 -0.1897 0.1336  866  LYS   A N   
421  C CA  . LYS   A 60  ? 1.3384 0.7235 1.1322 -0.1654 -0.2090 0.1443  866  LYS   A CA  
422  C C   . LYS   A 60  ? 1.3227 0.6908 1.1139 -0.1826 -0.2123 0.1427  866  LYS   A C   
423  O O   . LYS   A 60  ? 1.4204 0.7607 1.1826 -0.2054 -0.2195 0.1556  866  LYS   A O   
424  C CB  . LYS   A 60  ? 1.3534 0.7389 1.1155 -0.1891 -0.2023 0.1639  866  LYS   A CB  
425  N N   . LEU   A 61  ? 1.2666 0.6513 1.0867 -0.1733 -0.2072 0.1266  867  LEU   A N   
426  C CA  . LEU   A 61  ? 1.2383 0.6071 1.0591 -0.1863 -0.2120 0.1221  867  LEU   A CA  
427  C C   . LEU   A 61  ? 1.2418 0.5950 1.0816 -0.1570 -0.2271 0.1013  867  LEU   A C   
428  O O   . LEU   A 61  ? 1.2698 0.6061 1.1107 -0.1631 -0.2342 0.0946  867  LEU   A O   
429  C CB  . LEU   A 61  ? 1.2929 0.7047 1.1306 -0.2107 -0.1880 0.1216  867  LEU   A CB  
430  C CG  . LEU   A 61  ? 1.3381 0.7686 1.1588 -0.2456 -0.1715 0.1388  867  LEU   A CG  
431  C CD1 . LEU   A 61  ? 1.3523 0.8011 1.1638 -0.2427 -0.1618 0.1484  867  LEU   A CD1 
432  C CD2 . LEU   A 61  ? 1.3124 0.7891 1.1581 -0.2651 -0.1506 0.1329  867  LEU   A CD2 
433  N N   . TYR   A 62  ? 1.2622 0.6235 1.1176 -0.1255 -0.2314 0.0896  868  TYR   A N   
434  C CA  . TYR   A 62  ? 1.2000 0.5542 1.0754 -0.0947 -0.2434 0.0668  868  TYR   A CA  
435  C C   . TYR   A 62  ? 1.2105 0.5360 1.0773 -0.0709 -0.2656 0.0646  868  TYR   A C   
436  O O   . TYR   A 62  ? 1.2301 0.5542 1.0837 -0.0719 -0.2673 0.0774  868  TYR   A O   
437  C CB  . TYR   A 62  ? 1.1126 0.5108 1.0191 -0.0777 -0.2266 0.0510  868  TYR   A CB  
438  C CG  . TYR   A 62  ? 1.0470 0.4764 0.9636 -0.1004 -0.2065 0.0528  868  TYR   A CG  
439  C CD1 . TYR   A 62  ? 0.9881 0.4221 0.9182 -0.1003 -0.2058 0.0373  868  TYR   A CD1 
440  C CD2 . TYR   A 62  ? 1.0000 0.4559 0.9126 -0.1224 -0.1890 0.0690  868  TYR   A CD2 
441  C CE1 . TYR   A 62  ? 0.9037 0.3680 0.8448 -0.1209 -0.1900 0.0380  868  TYR   A CE1 
442  C CE2 . TYR   A 62  ? 0.9598 0.4484 0.8852 -0.1426 -0.1720 0.0690  868  TYR   A CE2 
443  C CZ  . TYR   A 62  ? 0.8970 0.3895 0.8373 -0.1417 -0.1736 0.0536  868  TYR   A CZ  
444  O OH  . TYR   A 62  ? 0.8804 0.4079 0.8356 -0.1612 -0.1591 0.0525  868  TYR   A OH  
445  N N   . LYS   A 63  ? 1.2539 0.5578 1.1284 -0.0496 -0.2833 0.0471  869  LYS   A N   
446  C CA  . LYS   A 63  ? 1.2826 0.5618 1.1524 -0.0262 -0.3063 0.0426  869  LYS   A CA  
447  C C   . LYS   A 63  ? 1.2768 0.5917 1.1740 0.0031  -0.3005 0.0277  869  LYS   A C   
448  O O   . LYS   A 63  ? 1.3092 0.6218 1.2006 0.0113  -0.3084 0.0344  869  LYS   A O   
449  C CB  . LYS   A 63  ? 1.2911 0.5362 1.1610 -0.0122 -0.3286 0.0275  869  LYS   A CB  
450  C CG  . LYS   A 63  ? 1.3453 0.5639 1.2097 0.0099  -0.3548 0.0238  869  LYS   A CG  
451  C CD  . LYS   A 63  ? 1.3725 0.5820 1.2562 0.0398  -0.3719 -0.0032 869  LYS   A CD  
452  C CE  . LYS   A 63  ? 1.3392 0.5425 1.2295 0.0667  -0.3925 -0.0112 869  LYS   A CE  
453  N NZ  . LYS   A 63  ? 1.3139 0.4744 1.1676 0.0505  -0.4120 0.0133  869  LYS   A NZ  
454  N N   . ASN   A 64  ? 1.2978 0.6463 1.2240 0.0183  -0.2869 0.0069  870  ASN   A N   
455  C CA  . ASN   A 64  ? 1.2201 0.6036 1.1748 0.0478  -0.2820 -0.0121 870  ASN   A CA  
456  C C   . ASN   A 64  ? 1.1952 0.6198 1.1610 0.0410  -0.2572 -0.0070 870  ASN   A C   
457  O O   . ASN   A 64  ? 1.2234 0.6566 1.1839 0.0185  -0.2418 0.0023  870  ASN   A O   
458  C CB  . ASN   A 64  ? 1.1861 0.5826 1.1647 0.0700  -0.2825 -0.0415 870  ASN   A CB  
459  C CG  . ASN   A 64  ? 1.3461 0.7018 1.3147 0.0758  -0.3064 -0.0480 870  ASN   A CG  
460  O OD1 . ASN   A 64  ? 1.4640 0.8064 1.4286 0.0678  -0.3066 -0.0540 870  ASN   A OD1 
461  N ND2 . ASN   A 64  ? 1.4361 0.7693 1.3992 0.0892  -0.3285 -0.0470 870  ASN   A ND2 
462  N N   . ARG   A 65  ? 1.0513 0.5034 1.0348 0.0612  -0.2539 -0.0149 871  ARG   A N   
463  C CA  . ARG   A 65  ? 0.9608 0.4558 0.9623 0.0621  -0.2308 -0.0189 871  ARG   A CA  
464  C C   . ARG   A 65  ? 0.9408 0.4538 0.9577 0.0650  -0.2188 -0.0380 871  ARG   A C   
465  O O   . ARG   A 65  ? 0.9207 0.4538 0.9407 0.0517  -0.2014 -0.0346 871  ARG   A O   
466  C CB  . ARG   A 65  ? 0.8949 0.4194 0.9176 0.0867  -0.2304 -0.0302 871  ARG   A CB  
467  C CG  . ARG   A 65  ? 0.8964 0.4477 0.9211 0.0790  -0.2140 -0.0178 871  ARG   A CG  
468  C CD  . ARG   A 65  ? 0.8696 0.4537 0.9183 0.1033  -0.2133 -0.0315 871  ARG   A CD  
469  N NE  . ARG   A 65  ? 0.8920 0.4573 0.9277 0.1057  -0.2308 -0.0190 871  ARG   A NE  
470  C CZ  . ARG   A 65  ? 0.8794 0.4345 0.8926 0.0887  -0.2300 0.0052  871  ARG   A CZ  
471  N NH1 . ARG   A 65  ? 0.8601 0.4243 0.8638 0.0681  -0.2119 0.0199  871  ARG   A NH1 
472  N NH2 . ARG   A 65  ? 0.9361 0.4732 0.9362 0.0922  -0.2476 0.0137  871  ARG   A NH2 
473  N N   . VAL   A 66  ? 0.9445 0.4495 0.9699 0.0813  -0.2291 -0.0587 872  VAL   A N   
474  C CA  . VAL   A 66  ? 0.8888 0.4115 0.9262 0.0849  -0.2182 -0.0790 872  VAL   A CA  
475  C C   . VAL   A 66  ? 0.9653 0.4665 0.9849 0.0578  -0.2165 -0.0668 872  VAL   A C   
476  O O   . VAL   A 66  ? 0.9287 0.4508 0.9539 0.0495  -0.2017 -0.0724 872  VAL   A O   
477  C CB  . VAL   A 66  ? 0.8233 0.3457 0.8740 0.1097  -0.2291 -0.1054 872  VAL   A CB  
478  C CG1 . VAL   A 66  ? 0.8583 0.3879 0.9118 0.1084  -0.2212 -0.1233 872  VAL   A CG1 
479  C CG2 . VAL   A 66  ? 0.7918 0.3538 0.8677 0.1341  -0.2230 -0.1226 872  VAL   A CG2 
480  N N   . GLU   A 67  ? 1.0403 0.5009 1.0384 0.0427  -0.2320 -0.0507 873  GLU   A N   
481  C CA  . GLU   A 67  ? 1.0457 0.4916 1.0284 0.0130  -0.2286 -0.0372 873  GLU   A CA  
482  C C   . GLU   A 67  ? 0.9948 0.4650 0.9765 -0.0083 -0.2105 -0.0200 873  GLU   A C   
483  O O   . GLU   A 67  ? 0.9803 0.4632 0.9641 -0.0265 -0.2001 -0.0190 873  GLU   A O   
484  C CB  . GLU   A 67  ? 1.1090 0.5092 1.0667 -0.0020 -0.2471 -0.0209 873  GLU   A CB  
485  C CG  . GLU   A 67  ? 1.2143 0.5841 1.1700 0.0111  -0.2662 -0.0364 873  GLU   A CG  
486  C CD  . GLU   A 67  ? 1.2751 0.6587 1.2435 0.0148  -0.2592 -0.0576 873  GLU   A CD  
487  O OE1 . GLU   A 67  ? 1.3012 0.6922 1.2658 -0.0086 -0.2486 -0.0510 873  GLU   A OE1 
488  O OE2 . GLU   A 67  ? 1.2622 0.6508 1.2440 0.0405  -0.2646 -0.0819 873  GLU   A OE2 
489  N N   . PHE   A 68  ? 0.9142 0.3930 0.8938 -0.0062 -0.2073 -0.0073 874  PHE   A N   
490  C CA  . PHE   A 68  ? 0.8858 0.3877 0.8638 -0.0263 -0.1905 0.0092  874  PHE   A CA  
491  C C   . PHE   A 68  ? 0.8400 0.4027 0.8406 -0.0177 -0.1668 -0.0050 874  PHE   A C   
492  O O   . PHE   A 68  ? 0.8156 0.4066 0.8186 -0.0357 -0.1514 0.0001  874  PHE   A O   
493  C CB  . PHE   A 68  ? 0.9109 0.4119 0.8797 -0.0238 -0.1921 0.0245  874  PHE   A CB  
494  C CG  . PHE   A 68  ? 0.8600 0.4046 0.8297 -0.0391 -0.1690 0.0378  874  PHE   A CG  
495  C CD1 . PHE   A 68  ? 0.9270 0.4657 0.8784 -0.0702 -0.1632 0.0582  874  PHE   A CD1 
496  C CD2 . PHE   A 68  ? 0.8279 0.4222 0.8170 -0.0229 -0.1522 0.0286  874  PHE   A CD2 
497  C CE1 . PHE   A 68  ? 0.9438 0.5268 0.8982 -0.0821 -0.1414 0.0672  874  PHE   A CE1 
498  C CE2 . PHE   A 68  ? 0.8185 0.4516 0.8083 -0.0353 -0.1323 0.0393  874  PHE   A CE2 
499  C CZ  . PHE   A 68  ? 0.8637 0.4920 0.8372 -0.0634 -0.1270 0.0576  874  PHE   A CZ  
500  N N   . ASP   A 69  ? 0.7747 0.3591 0.7917 0.0093  -0.1641 -0.0231 875  ASP   A N   
501  C CA  . ASP   A 69  ? 0.7453 0.3825 0.7780 0.0150  -0.1425 -0.0352 875  ASP   A CA  
502  C C   . ASP   A 69  ? 0.7426 0.3807 0.7760 0.0086  -0.1409 -0.0471 875  ASP   A C   
503  O O   . ASP   A 69  ? 0.6764 0.3505 0.7143 0.0009  -0.1248 -0.0478 875  ASP   A O   
504  C CB  . ASP   A 69  ? 0.7038 0.3634 0.7527 0.0422  -0.1397 -0.0535 875  ASP   A CB  
505  C CG  . ASP   A 69  ? 0.7858 0.4440 0.8357 0.0502  -0.1444 -0.0435 875  ASP   A CG  
506  O OD1 . ASP   A 69  ? 0.8249 0.4745 0.8613 0.0337  -0.1442 -0.0212 875  ASP   A OD1 
507  O OD2 . ASP   A 69  ? 0.7559 0.4242 0.8210 0.0730  -0.1483 -0.0596 875  ASP   A OD2 
508  N N   . SER   A 70  ? 0.7627 0.3590 0.7907 0.0121  -0.1595 -0.0568 876  SER   A N   
509  C CA  . SER   A 70  ? 0.7434 0.3355 0.7693 0.0037  -0.1605 -0.0673 876  SER   A CA  
510  C C   . SER   A 70  ? 0.7207 0.3257 0.7419 -0.0249 -0.1520 -0.0500 876  SER   A C   
511  O O   . SER   A 70  ? 0.7091 0.3388 0.7348 -0.0310 -0.1435 -0.0570 876  SER   A O   
512  C CB  . SER   A 70  ? 0.8620 0.3980 0.8794 0.0078  -0.1849 -0.0765 876  SER   A CB  
513  O OG  . SER   A 70  ? 0.9639 0.4940 0.9895 0.0366  -0.1929 -0.0958 876  SER   A OG  
514  N N   . ALA   A 71  ? 0.7319 0.3203 0.7437 -0.0431 -0.1551 -0.0283 877  ALA   A N   
515  C CA  . ALA   A 71  ? 0.6989 0.3058 0.7099 -0.0707 -0.1454 -0.0139 877  ALA   A CA  
516  C C   . ALA   A 71  ? 0.6904 0.3544 0.7149 -0.0679 -0.1238 -0.0138 877  ALA   A C   
517  O O   . ALA   A 71  ? 0.6643 0.3550 0.6966 -0.0794 -0.1160 -0.0155 877  ALA   A O   
518  C CB  . ALA   A 71  ? 0.7246 0.3036 0.7197 -0.0920 -0.1513 0.0087  877  ALA   A CB  
519  N N   . ILE   A 72  ? 0.6828 0.3648 0.7106 -0.0520 -0.1159 -0.0127 878  ILE   A N   
520  C CA  . ILE   A 72  ? 0.6303 0.3611 0.6686 -0.0480 -0.0973 -0.0132 878  ILE   A CA  
521  C C   . ILE   A 72  ? 0.6271 0.3770 0.6717 -0.0378 -0.0934 -0.0310 878  ILE   A C   
522  O O   . ILE   A 72  ? 0.6183 0.3954 0.6681 -0.0460 -0.0855 -0.0310 878  ILE   A O   
523  C CB  . ILE   A 72  ? 0.6074 0.3494 0.6468 -0.0331 -0.0916 -0.0100 878  ILE   A CB  
524  C CG1 . ILE   A 72  ? 0.6620 0.3814 0.6902 -0.0433 -0.0974 0.0079  878  ILE   A CG1 
525  C CG2 . ILE   A 72  ? 0.5510 0.3371 0.5986 -0.0309 -0.0743 -0.0095 878  ILE   A CG2 
526  C CD1 . ILE   A 72  ? 0.6468 0.3652 0.6752 -0.0254 -0.0994 0.0076  878  ILE   A CD1 
527  N N   . ASP   A 73  ? 0.6253 0.3620 0.6690 -0.0196 -0.0996 -0.0474 879  ASP   A N   
528  C CA  . ASP   A 73  ? 0.6334 0.3845 0.6775 -0.0113 -0.0962 -0.0655 879  ASP   A CA  
529  C C   . ASP   A 73  ? 0.6518 0.3983 0.6933 -0.0269 -0.1015 -0.0669 879  ASP   A C   
530  O O   . ASP   A 73  ? 0.6408 0.4116 0.6820 -0.0281 -0.0951 -0.0726 879  ASP   A O   
531  C CB  . ASP   A 73  ? 0.6230 0.3547 0.6664 0.0081  -0.1043 -0.0850 879  ASP   A CB  
532  C CG  . ASP   A 73  ? 0.6422 0.3985 0.6841 0.0190  -0.0948 -0.1042 879  ASP   A CG  
533  O OD1 . ASP   A 73  ? 0.6582 0.4481 0.7007 0.0199  -0.0801 -0.1013 879  ASP   A OD1 
534  O OD2 . ASP   A 73  ? 0.6982 0.4384 0.7358 0.0257  -0.1025 -0.1225 879  ASP   A OD2 
535  N N   . LEU   A 74  ? 0.6313 0.3453 0.6697 -0.0400 -0.1146 -0.0614 880  LEU   A N   
536  C CA  . LEU   A 74  ? 0.6188 0.3308 0.6576 -0.0574 -0.1201 -0.0625 880  LEU   A CA  
537  C C   . LEU   A 74  ? 0.6124 0.3649 0.6610 -0.0694 -0.1083 -0.0531 880  LEU   A C   
538  O O   . LEU   A 74  ? 0.5838 0.3539 0.6351 -0.0721 -0.1084 -0.0609 880  LEU   A O   
539  C CB  . LEU   A 74  ? 0.6902 0.3622 0.7236 -0.0746 -0.1343 -0.0537 880  LEU   A CB  
540  C CG  . LEU   A 74  ? 0.6846 0.3359 0.7151 -0.0866 -0.1472 -0.0631 880  LEU   A CG  
541  C CD1 . LEU   A 74  ? 0.6860 0.3124 0.7089 -0.0663 -0.1573 -0.0845 880  LEU   A CD1 
542  C CD2 . LEU   A 74  ? 0.7206 0.3370 0.7452 -0.1105 -0.1584 -0.0491 880  LEU   A CD2 
543  N N   . VAL   A 75  ? 0.5881 0.3552 0.6416 -0.0759 -0.0994 -0.0373 881  VAL   A N   
544  C CA  . VAL   A 75  ? 0.5718 0.3783 0.6372 -0.0854 -0.0888 -0.0306 881  VAL   A CA  
545  C C   . VAL   A 75  ? 0.6178 0.4524 0.6842 -0.0690 -0.0807 -0.0384 881  VAL   A C   
546  O O   . VAL   A 75  ? 0.6013 0.4604 0.6748 -0.0724 -0.0795 -0.0413 881  VAL   A O   
547  C CB  . VAL   A 75  ? 0.5521 0.3663 0.6200 -0.0957 -0.0806 -0.0138 881  VAL   A CB  
548  C CG1 . VAL   A 75  ? 0.5359 0.3943 0.6185 -0.1008 -0.0686 -0.0103 881  VAL   A CG1 
549  C CG2 . VAL   A 75  ? 0.5269 0.3128 0.5895 -0.1176 -0.0887 -0.0046 881  VAL   A CG2 
550  N N   . LEU   A 76  ? 0.5759 0.4063 0.6345 -0.0518 -0.0764 -0.0425 882  LEU   A N   
551  C CA  . LEU   A 76  ? 0.5637 0.4167 0.6186 -0.0393 -0.0684 -0.0491 882  LEU   A CA  
552  C C   . LEU   A 76  ? 0.6179 0.4692 0.6649 -0.0379 -0.0747 -0.0628 882  LEU   A C   
553  O O   . LEU   A 76  ? 0.5936 0.4645 0.6375 -0.0369 -0.0722 -0.0644 882  LEU   A O   
554  C CB  . LEU   A 76  ? 0.5319 0.3812 0.5813 -0.0237 -0.0628 -0.0531 882  LEU   A CB  
555  C CG  . LEU   A 76  ? 0.5090 0.3594 0.5637 -0.0237 -0.0580 -0.0400 882  LEU   A CG  
556  C CD1 . LEU   A 76  ? 0.5482 0.3995 0.6010 -0.0078 -0.0537 -0.0461 882  LEU   A CD1 
557  C CD2 . LEU   A 76  ? 0.4713 0.3488 0.5316 -0.0305 -0.0492 -0.0295 882  LEU   A CD2 
558  N N   . GLU   A 77  ? 0.6277 0.4527 0.6690 -0.0370 -0.0844 -0.0734 883  GLU   A N   
559  C CA  . GLU   A 77  ? 0.6519 0.4737 0.6838 -0.0376 -0.0916 -0.0869 883  GLU   A CA  
560  C C   . GLU   A 77  ? 0.6405 0.4721 0.6818 -0.0532 -0.0987 -0.0818 883  GLU   A C   
561  O O   . GLU   A 77  ? 0.6663 0.5107 0.7021 -0.0533 -0.1020 -0.0876 883  GLU   A O   
562  C CB  . GLU   A 77  ? 0.6800 0.4702 0.7044 -0.0326 -0.1012 -0.1013 883  GLU   A CB  
563  C CG  . GLU   A 77  ? 0.7482 0.5331 0.7687 -0.0154 -0.0952 -0.1100 883  GLU   A CG  
564  C CD  . GLU   A 77  ? 0.8586 0.6589 0.8650 -0.0053 -0.0875 -0.1254 883  GLU   A CD  
565  O OE1 . GLU   A 77  ? 0.9411 0.7554 0.9379 -0.0118 -0.0867 -0.1250 883  GLU   A OE1 
566  O OE2 . GLU   A 77  ? 0.9102 0.7091 0.9149 0.0086  -0.0827 -0.1383 883  GLU   A OE2 
567  N N   . GLU   A 78  ? 0.6701 0.4968 0.7250 -0.0674 -0.1017 -0.0716 884  GLU   A N   
568  C CA  . GLU   A 78  ? 0.6908 0.5330 0.7593 -0.0835 -0.1077 -0.0693 884  GLU   A CA  
569  C C   . GLU   A 78  ? 0.6614 0.5401 0.7381 -0.0798 -0.1017 -0.0663 884  GLU   A C   
570  O O   . GLU   A 78  ? 0.6382 0.5308 0.7202 -0.0836 -0.1099 -0.0721 884  GLU   A O   
571  C CB  . GLU   A 78  ? 0.7492 0.5852 0.8303 -0.1027 -0.1084 -0.0578 884  GLU   A CB  
572  C CG  . GLU   A 78  ? 0.8315 0.6945 0.9321 -0.1198 -0.1108 -0.0564 884  GLU   A CG  
573  C CD  . GLU   A 78  ? 0.9286 0.7936 1.0419 -0.1438 -0.1079 -0.0447 884  GLU   A CD  
574  O OE1 . GLU   A 78  ? 0.9424 0.7811 1.0446 -0.1475 -0.1056 -0.0353 884  GLU   A OE1 
575  O OE2 . GLU   A 78  ? 0.9894 0.8820 1.1230 -0.1599 -0.1093 -0.0461 884  GLU   A OE2 
576  N N   . PHE   A 79  ? 0.6201 0.5127 0.6973 -0.0712 -0.0896 -0.0581 885  PHE   A N   
577  C CA  . PHE   A 79  ? 0.4958 0.4180 0.5792 -0.0659 -0.0851 -0.0551 885  PHE   A CA  
578  C C   . PHE   A 79  ? 0.5258 0.4460 0.5884 -0.0513 -0.0840 -0.0606 885  PHE   A C   
579  O O   . PHE   A 79  ? 0.4897 0.4269 0.5522 -0.0453 -0.0801 -0.0563 885  PHE   A O   
580  C CB  . PHE   A 79  ? 0.5050 0.4429 0.5998 -0.0669 -0.0730 -0.0432 885  PHE   A CB  
581  C CG  . PHE   A 79  ? 0.5204 0.4728 0.6362 -0.0840 -0.0721 -0.0378 885  PHE   A CG  
582  C CD1 . PHE   A 79  ? 0.5530 0.4844 0.6681 -0.0980 -0.0746 -0.0343 885  PHE   A CD1 
583  C CD2 . PHE   A 79  ? 0.4889 0.4763 0.6250 -0.0867 -0.0691 -0.0370 885  PHE   A CD2 
584  C CE1 . PHE   A 79  ? 0.5809 0.5264 0.7124 -0.1179 -0.0723 -0.0288 885  PHE   A CE1 
585  C CE2 . PHE   A 79  ? 0.4137 0.4205 0.5707 -0.1045 -0.0659 -0.0342 885  PHE   A CE2 
586  C CZ  . PHE   A 79  ? 0.4893 0.4755 0.6427 -0.1218 -0.0665 -0.0293 885  PHE   A CZ  
587  N N   . SER   A 80  ? 0.5026 0.4017 0.5462 -0.0466 -0.0872 -0.0705 886  SER   A N   
588  C CA  . SER   A 80  ? 0.4915 0.3888 0.5111 -0.0367 -0.0848 -0.0768 886  SER   A CA  
589  C C   . SER   A 80  ? 0.5341 0.4433 0.5506 -0.0294 -0.0722 -0.0686 886  SER   A C   
590  O O   . SER   A 80  ? 0.5567 0.4736 0.5603 -0.0261 -0.0719 -0.0667 886  SER   A O   
591  C CB  . SER   A 80  ? 0.4597 0.3626 0.4703 -0.0388 -0.0966 -0.0811 886  SER   A CB  
592  O OG  . SER   A 80  ? 0.5098 0.4062 0.5292 -0.0475 -0.1092 -0.0876 886  SER   A OG  
593  N N   . ILE   A 81  ? 0.4677 0.3751 0.4939 -0.0273 -0.0634 -0.0633 887  ILE   A N   
594  C CA  . ILE   A 81  ? 0.4594 0.3785 0.4854 -0.0216 -0.0522 -0.0554 887  ILE   A CA  
595  C C   . ILE   A 81  ? 0.4471 0.3641 0.4520 -0.0145 -0.0453 -0.0626 887  ILE   A C   
596  O O   . ILE   A 81  ? 0.4412 0.3475 0.4367 -0.0115 -0.0454 -0.0745 887  ILE   A O   
597  C CB  . ILE   A 81  ? 0.4613 0.3775 0.5018 -0.0222 -0.0470 -0.0482 887  ILE   A CB  
598  C CG1 . ILE   A 81  ? 0.4843 0.4084 0.5429 -0.0329 -0.0502 -0.0394 887  ILE   A CG1 
599  C CG2 . ILE   A 81  ? 0.4459 0.3711 0.4837 -0.0152 -0.0362 -0.0432 887  ILE   A CG2 
600  C CD1 . ILE   A 81  ? 0.4626 0.4088 0.5283 -0.0347 -0.0516 -0.0367 887  ILE   A CD1 
601  N N   . ASP   A 82  ? 0.4830 0.4106 0.4799 -0.0125 -0.0390 -0.0564 888  ASP   A N   
602  C CA  . ASP   A 82  ? 0.4680 0.3966 0.4445 -0.0096 -0.0302 -0.0619 888  ASP   A CA  
603  C C   . ASP   A 82  ? 0.5004 0.4378 0.4856 -0.0053 -0.0186 -0.0583 888  ASP   A C   
604  O O   . ASP   A 82  ? 0.4959 0.4362 0.4753 -0.0020 -0.0105 -0.0676 888  ASP   A O   
605  C CB  . ASP   A 82  ? 0.4325 0.3615 0.3864 -0.0130 -0.0333 -0.0579 888  ASP   A CB  
606  C CG  . ASP   A 82  ? 0.5077 0.4272 0.4488 -0.0166 -0.0467 -0.0631 888  ASP   A CG  
607  O OD1 . ASP   A 82  ? 0.4951 0.4068 0.4283 -0.0172 -0.0480 -0.0750 888  ASP   A OD1 
608  O OD2 . ASP   A 82  ? 0.5172 0.4369 0.4569 -0.0177 -0.0573 -0.0566 888  ASP   A OD2 
609  N N   . ILE   A 83  ? 0.4423 0.3862 0.4425 -0.0054 -0.0177 -0.0465 889  ILE   A N   
610  C CA  . ILE   A 83  ? 0.4297 0.3816 0.4377 -0.0019 -0.0087 -0.0420 889  ILE   A CA  
611  C C   . ILE   A 83  ? 0.4077 0.3581 0.4357 -0.0017 -0.0111 -0.0346 889  ILE   A C   
612  O O   . ILE   A 83  ? 0.3736 0.3252 0.4095 -0.0065 -0.0162 -0.0284 889  ILE   A O   
613  C CB  . ILE   A 83  ? 0.4532 0.4128 0.4516 -0.0037 -0.0043 -0.0341 889  ILE   A CB  
614  C CG1 . ILE   A 83  ? 0.4076 0.3650 0.3801 -0.0072 -0.0013 -0.0398 889  ILE   A CG1 
615  C CG2 . ILE   A 83  ? 0.4303 0.3983 0.4398 -0.0008 0.0034  -0.0290 889  ILE   A CG2 
616  C CD1 . ILE   A 83  ? 0.3884 0.3454 0.3461 -0.0109 -0.0004 -0.0312 889  ILE   A CD1 
617  N N   . VAL   A 84  ? 0.4021 0.3509 0.4376 0.0033  -0.0078 -0.0360 890  VAL   A N   
618  C CA  . VAL   A 84  ? 0.4125 0.3554 0.4606 0.0023  -0.0108 -0.0278 890  VAL   A CA  
619  C C   . VAL   A 84  ? 0.3961 0.3500 0.4470 0.0046  -0.0041 -0.0205 890  VAL   A C   
620  O O   . VAL   A 84  ? 0.4038 0.3638 0.4539 0.0105  0.0007  -0.0259 890  VAL   A O   
621  C CB  . VAL   A 84  ? 0.4548 0.3805 0.5077 0.0072  -0.0173 -0.0345 890  VAL   A CB  
622  C CG1 . VAL   A 84  ? 0.4242 0.3400 0.4838 0.0052  -0.0212 -0.0235 890  VAL   A CG1 
623  C CG2 . VAL   A 84  ? 0.4256 0.3373 0.4755 0.0036  -0.0253 -0.0415 890  VAL   A CG2 
624  N N   . CYS   A 85  ? 0.3882 0.3466 0.4430 -0.0007 -0.0035 -0.0098 891  CYS   A N   
625  C CA  . CYS   A 85  ? 0.3834 0.3500 0.4398 0.0005  0.0016  -0.0027 891  CYS   A CA  
626  C C   . CYS   A 85  ? 0.3933 0.3500 0.4538 -0.0023 -0.0020 0.0046  891  CYS   A C   
627  O O   . CYS   A 85  ? 0.3967 0.3497 0.4590 -0.0110 -0.0042 0.0101  891  CYS   A O   
628  C CB  . CYS   A 85  ? 0.3602 0.3393 0.4155 -0.0028 0.0050  0.0021  891  CYS   A CB  
629  S SG  . CYS   A 85  ? 0.4461 0.4292 0.4891 -0.0002 0.0067  -0.0034 891  CYS   A SG  
630  N N   . LEU   A 86  ? 0.4101 0.3625 0.4713 0.0039  -0.0032 0.0045  892  LEU   A N   
631  C CA  . LEU   A 86  ? 0.4176 0.3578 0.4771 0.0012  -0.0082 0.0136  892  LEU   A CA  
632  C C   . LEU   A 86  ? 0.4324 0.3862 0.4888 -0.0023 -0.0015 0.0214  892  LEU   A C   
633  O O   . LEU   A 86  ? 0.4247 0.3891 0.4819 0.0037  0.0022  0.0189  892  LEU   A O   
634  C CB  . LEU   A 86  ? 0.3904 0.3186 0.4531 0.0117  -0.0161 0.0086  892  LEU   A CB  
635  C CG  . LEU   A 86  ? 0.4276 0.3459 0.4957 0.0198  -0.0222 -0.0044 892  LEU   A CG  
636  C CD1 . LEU   A 86  ? 0.4147 0.3213 0.4892 0.0320  -0.0327 -0.0099 892  LEU   A CD1 
637  C CD2 . LEU   A 86  ? 0.4315 0.3309 0.4953 0.0119  -0.0283 -0.0026 892  LEU   A CD2 
638  N N   . ALA   A 87  ? 0.4349 0.3902 0.4880 -0.0128 0.0008  0.0293  893  ALA   A N   
639  C CA  . ALA   A 87  ? 0.4201 0.3898 0.4700 -0.0162 0.0079  0.0342  893  ALA   A CA  
640  C C   . ALA   A 87  ? 0.4625 0.4211 0.5019 -0.0251 0.0057  0.0444  893  ALA   A C   
641  O O   . ALA   A 87  ? 0.4963 0.4598 0.5330 -0.0373 0.0100  0.0490  893  ALA   A O   
642  C CB  . ALA   A 87  ? 0.3384 0.3261 0.3947 -0.0203 0.0141  0.0313  893  ALA   A CB  
643  N N   . GLY   A 88  ? 0.4816 0.4263 0.5145 -0.0197 -0.0013 0.0475  894  GLY   A N   
644  C CA  . GLY   A 88  ? 0.4748 0.4019 0.4920 -0.0286 -0.0067 0.0585  894  GLY   A CA  
645  C C   . GLY   A 88  ? 0.5318 0.4304 0.5431 -0.0336 -0.0179 0.0628  894  GLY   A C   
646  O O   . GLY   A 88  ? 0.5847 0.4659 0.5789 -0.0473 -0.0214 0.0740  894  GLY   A O   
647  N N   . PHE   A 89  ? 0.5387 0.4302 0.5613 -0.0242 -0.0238 0.0540  895  PHE   A N   
648  C CA  . PHE   A 89  ? 0.5426 0.4025 0.5601 -0.0263 -0.0372 0.0558  895  PHE   A CA  
649  C C   . PHE   A 89  ? 0.6097 0.4442 0.6187 -0.0173 -0.0525 0.0594  895  PHE   A C   
650  O O   . PHE   A 89  ? 0.6264 0.4691 0.6476 -0.0003 -0.0559 0.0497  895  PHE   A O   
651  C CB  . PHE   A 89  ? 0.5328 0.3957 0.5651 -0.0167 -0.0382 0.0421  895  PHE   A CB  
652  C CG  . PHE   A 89  ? 0.5206 0.3528 0.5486 -0.0210 -0.0505 0.0421  895  PHE   A CG  
653  C CD1 . PHE   A 89  ? 0.4980 0.3204 0.5170 -0.0405 -0.0497 0.0512  895  PHE   A CD1 
654  C CD2 . PHE   A 89  ? 0.5292 0.3429 0.5630 -0.0058 -0.0629 0.0315  895  PHE   A CD2 
655  C CE1 . PHE   A 89  ? 0.5589 0.3491 0.5721 -0.0465 -0.0623 0.0517  895  PHE   A CE1 
656  C CE2 . PHE   A 89  ? 0.5936 0.3740 0.6220 -0.0089 -0.0763 0.0306  895  PHE   A CE2 
657  C CZ  . PHE   A 89  ? 0.5820 0.3485 0.5988 -0.0302 -0.0765 0.0417  895  PHE   A CZ  
658  N N   . MET   A 90  ? 0.6626 0.4667 0.6504 -0.0291 -0.0627 0.0730  896  MET   A N   
659  C CA  . MET   A 90  ? 0.7048 0.4807 0.6812 -0.0203 -0.0809 0.0779  896  MET   A CA  
660  C C   . MET   A 90  ? 0.7513 0.4870 0.7253 -0.0140 -0.1014 0.0758  896  MET   A C   
661  O O   . MET   A 90  ? 0.8053 0.5000 0.7560 -0.0213 -0.1183 0.0883  896  MET   A O   
662  C CB  . MET   A 90  ? 0.7311 0.4947 0.6792 -0.0372 -0.0814 0.0953  896  MET   A CB  
663  C CG  . MET   A 90  ? 0.7263 0.5267 0.6764 -0.0403 -0.0638 0.0951  896  MET   A CG  
664  S SD  . MET   A 90  ? 0.8368 0.6543 0.8059 -0.0153 -0.0691 0.0832  896  MET   A SD  
665  C CE  . MET   A 90  ? 0.7186 0.5756 0.6885 -0.0211 -0.0482 0.0825  896  MET   A CE  
666  N N   . ARG   A 91  ? 0.7067 0.4509 0.7023 -0.0009 -0.1009 0.0595  897  ARG   A N   
667  C CA  . ARG   A 91  ? 0.7302 0.4373 0.7264 0.0093  -0.1214 0.0533  897  ARG   A CA  
668  C C   . ARG   A 91  ? 0.7183 0.4480 0.7431 0.0326  -0.1199 0.0302  897  ARG   A C   
669  O O   . ARG   A 91  ? 0.6873 0.4538 0.7261 0.0329  -0.1015 0.0210  897  ARG   A O   
670  C CB  . ARG   A 91  ? 0.7292 0.4109 0.7126 -0.0092 -0.1233 0.0599  897  ARG   A CB  
671  C CG  . ARG   A 91  ? 0.8620 0.4956 0.8396 -0.0010 -0.1477 0.0564  897  ARG   A CG  
672  C CD  . ARG   A 91  ? 1.0195 0.6127 0.9710 -0.0262 -0.1556 0.0724  897  ARG   A CD  
673  N NE  . ARG   A 91  ? 1.0569 0.5970 1.0013 -0.0173 -0.1821 0.0682  897  ARG   A NE  
674  C CZ  . ARG   A 91  ? 0.9657 0.5045 0.9305 0.0014  -0.1880 0.0473  897  ARG   A CZ  
675  N NH1 . ARG   A 91  ? 0.9342 0.5214 0.9250 0.0116  -0.1689 0.0300  897  ARG   A NH1 
676  N NH2 . ARG   A 91  ? 1.0328 0.5342 0.9907 0.0096  -0.2092 0.0418  897  ARG   A NH2 
677  N N   . ILE   A 92  ? 0.7642 0.4725 0.7968 0.0520  -0.1397 0.0202  898  ILE   A N   
678  C CA  . ILE   A 92  ? 0.7068 0.4415 0.7682 0.0745  -0.1376 -0.0042 898  ILE   A CA  
679  C C   . ILE   A 92  ? 0.6910 0.4137 0.7578 0.0778  -0.1396 -0.0180 898  ILE   A C   
680  O O   . ILE   A 92  ? 0.7071 0.3849 0.7607 0.0749  -0.1573 -0.0135 898  ILE   A O   
681  C CB  . ILE   A 92  ? 0.7144 0.4385 0.7871 0.0965  -0.1582 -0.0125 898  ILE   A CB  
682  C CG1 . ILE   A 92  ? 0.7262 0.4764 0.7999 0.0952  -0.1518 -0.0047 898  ILE   A CG1 
683  C CG2 . ILE   A 92  ? 0.6248 0.3697 0.7279 0.1194  -0.1590 -0.0412 898  ILE   A CG2 
684  C CD1 . ILE   A 92  ? 0.7468 0.4755 0.8218 0.1107  -0.1769 -0.0044 898  ILE   A CD1 
685  N N   . LEU   A 93  ? 0.6538 0.4141 0.7378 0.0831  -0.1225 -0.0348 899  LEU   A N   
686  C CA  . LEU   A 93  ? 0.6547 0.4091 0.7401 0.0823  -0.1204 -0.0471 899  LEU   A CA  
687  C C   . LEU   A 93  ? 0.6427 0.3909 0.7459 0.1062  -0.1329 -0.0722 899  LEU   A C   
688  O O   . LEU   A 93  ? 0.6160 0.3889 0.7391 0.1234  -0.1325 -0.0862 899  LEU   A O   
689  C CB  . LEU   A 93  ? 0.5916 0.3865 0.6801 0.0733  -0.0963 -0.0509 899  LEU   A CB  
690  C CG  . LEU   A 93  ? 0.6115 0.4102 0.6846 0.0508  -0.0859 -0.0297 899  LEU   A CG  
691  C CD1 . LEU   A 93  ? 0.5589 0.3995 0.6365 0.0469  -0.0655 -0.0300 899  LEU   A CD1 
692  C CD2 . LEU   A 93  ? 0.6476 0.4266 0.7109 0.0374  -0.0884 -0.0269 899  LEU   A CD2 
693  N N   . SER   A 94  ? 0.6834 0.3999 0.7809 0.1072  -0.1441 -0.0795 900  SER   A N   
694  C CA  . SER   A 94  ? 0.6869 0.3936 0.8009 0.1311  -0.1577 -0.1056 900  SER   A CA  
695  C C   . SER   A 94  ? 0.6394 0.3973 0.7736 0.1414  -0.1377 -0.1308 900  SER   A C   
696  O O   . SER   A 94  ? 0.6123 0.4017 0.7412 0.1274  -0.1157 -0.1274 900  SER   A O   
697  C CB  . SER   A 94  ? 0.7433 0.4019 0.8437 0.1275  -0.1740 -0.1076 900  SER   A CB  
698  O OG  . SER   A 94  ? 0.7616 0.4371 0.8562 0.1139  -0.1574 -0.1114 900  SER   A OG  
699  N N   . GLY   A 95  ? 0.6940 0.4590 0.8506 0.1661  -0.1465 -0.1573 901  GLY   A N   
700  C CA  . GLY   A 95  ? 0.6767 0.4923 0.8533 0.1760  -0.1276 -0.1840 901  GLY   A CA  
701  C C   . GLY   A 95  ? 0.6005 0.4239 0.7651 0.1662  -0.1132 -0.1938 901  GLY   A C   
702  O O   . GLY   A 95  ? 0.6338 0.4986 0.7974 0.1575  -0.0898 -0.1988 901  GLY   A O   
703  N N   . PRO   A 96  ? 0.6381 0.4198 0.7913 0.1668  -0.1282 -0.1973 902  PRO   A N   
704  C CA  . PRO   A 96  ? 0.6152 0.4031 0.7544 0.1560  -0.1159 -0.2057 902  PRO   A CA  
705  C C   . PRO   A 96  ? 0.6168 0.4140 0.7359 0.1297  -0.1012 -0.1800 902  PRO   A C   
706  O O   . PRO   A 96  ? 0.6224 0.4502 0.7347 0.1214  -0.0825 -0.1859 902  PRO   A O   
707  C CB  . PRO   A 96  ? 0.6146 0.3546 0.7446 0.1593  -0.1375 -0.2098 902  PRO   A CB  
708  C CG  . PRO   A 96  ? 0.6745 0.3832 0.8055 0.1638  -0.1590 -0.1937 902  PRO   A CG  
709  C CD  . PRO   A 96  ? 0.6795 0.4201 0.8290 0.1739  -0.1538 -0.1929 902  PRO   A CD  
710  N N   . PHE   A 97  ? 0.6094 0.3825 0.7182 0.1163  -0.1090 -0.1523 903  PHE   A N   
711  C CA  . PHE   A 97  ? 0.5743 0.3629 0.6692 0.0940  -0.0943 -0.1312 903  PHE   A CA  
712  C C   . PHE   A 97  ? 0.5740 0.4107 0.6749 0.0935  -0.0731 -0.1331 903  PHE   A C   
713  O O   . PHE   A 97  ? 0.5740 0.4311 0.6646 0.0821  -0.0587 -0.1316 903  PHE   A O   
714  C CB  . PHE   A 97  ? 0.5858 0.3495 0.6718 0.0806  -0.1032 -0.1037 903  PHE   A CB  
715  C CG  . PHE   A 97  ? 0.6045 0.3842 0.6797 0.0594  -0.0898 -0.0852 903  PHE   A CG  
716  C CD1 . PHE   A 97  ? 0.6623 0.4264 0.7267 0.0440  -0.0927 -0.0797 903  PHE   A CD1 
717  C CD2 . PHE   A 97  ? 0.5979 0.4091 0.6754 0.0554  -0.0755 -0.0749 903  PHE   A CD2 
718  C CE1 . PHE   A 97  ? 0.6213 0.4037 0.6802 0.0266  -0.0818 -0.0652 903  PHE   A CE1 
719  C CE2 . PHE   A 97  ? 0.5577 0.3832 0.6273 0.0385  -0.0649 -0.0603 903  PHE   A CE2 
720  C CZ  . PHE   A 97  ? 0.5640 0.3765 0.6257 0.0249  -0.0683 -0.0559 903  PHE   A CZ  
721  N N   . VAL   A 98  ? 0.5613 0.4144 0.6778 0.1053  -0.0726 -0.1363 904  VAL   A N   
722  C CA  . VAL   A 98  ? 0.5792 0.4761 0.7009 0.1024  -0.0531 -0.1375 904  VAL   A CA  
723  C C   . VAL   A 98  ? 0.5445 0.4695 0.6668 0.1053  -0.0388 -0.1610 904  VAL   A C   
724  O O   . VAL   A 98  ? 0.4984 0.4489 0.6099 0.0932  -0.0217 -0.1577 904  VAL   A O   
725  C CB  . VAL   A 98  ? 0.5509 0.4603 0.6917 0.1146  -0.0574 -0.1386 904  VAL   A CB  
726  C CG1 . VAL   A 98  ? 0.5152 0.4698 0.6621 0.1102  -0.0374 -0.1421 904  VAL   A CG1 
727  C CG2 . VAL   A 98  ? 0.5540 0.4354 0.6869 0.1083  -0.0700 -0.1134 904  VAL   A CG2 
728  N N   . GLN   A 99  ? 0.5597 0.4788 0.6926 0.1210  -0.0462 -0.1854 905  GLN   A N   
729  C CA  . GLN   A 99  ? 0.5331 0.4790 0.6640 0.1230  -0.0319 -0.2101 905  GLN   A CA  
730  C C   . GLN   A 99  ? 0.5680 0.5068 0.6706 0.1049  -0.0245 -0.2018 905  GLN   A C   
731  O O   . GLN   A 99  ? 0.5504 0.5170 0.6404 0.0949  -0.0069 -0.2058 905  GLN   A O   
732  C CB  . GLN   A 99  ? 0.5228 0.4581 0.6697 0.1445  -0.0440 -0.2391 905  GLN   A CB  
733  N N   . LYS   A 100 ? 0.5684 0.4694 0.6599 0.0991  -0.0390 -0.1892 906  LYS   A N   
734  C CA  . LYS   A 100 ? 0.5569 0.4509 0.6249 0.0837  -0.0355 -0.1836 906  LYS   A CA  
735  C C   . LYS   A 100 ? 0.5821 0.4957 0.6376 0.0675  -0.0227 -0.1637 906  LYS   A C   
736  O O   . LYS   A 100 ? 0.6205 0.5431 0.6564 0.0573  -0.0146 -0.1650 906  LYS   A O   
737  C CB  . LYS   A 100 ? 0.5624 0.4152 0.6251 0.0787  -0.0539 -0.1732 906  LYS   A CB  
738  C CG  . LYS   A 100 ? 0.5324 0.3811 0.5751 0.0618  -0.0522 -0.1647 906  LYS   A CG  
739  C CD  . LYS   A 100 ? 0.6115 0.4224 0.6509 0.0556  -0.0701 -0.1591 906  LYS   A CD  
740  C CE  . LYS   A 100 ? 0.6803 0.4930 0.7038 0.0394  -0.0691 -0.1523 906  LYS   A CE  
741  N NZ  . LYS   A 100 ? 0.7650 0.5450 0.7854 0.0317  -0.0856 -0.1518 906  LYS   A NZ  
742  N N   . TRP   A 101 ? 0.5339 0.4513 0.5984 0.0653  -0.0224 -0.1454 907  TRP   A N   
743  C CA  . TRP   A 101 ? 0.5238 0.4561 0.5779 0.0519  -0.0126 -0.1271 907  TRP   A CA  
744  C C   . TRP   A 101 ? 0.5339 0.4979 0.5925 0.0531  0.0020  -0.1309 907  TRP   A C   
745  O O   . TRP   A 101 ? 0.5172 0.4911 0.5689 0.0436  0.0087  -0.1156 907  TRP   A O   
746  C CB  . TRP   A 101 ? 0.4665 0.3823 0.5248 0.0459  -0.0212 -0.1046 907  TRP   A CB  
747  C CG  . TRP   A 101 ? 0.4981 0.3884 0.5498 0.0392  -0.0325 -0.1006 907  TRP   A CG  
748  C CD1 . TRP   A 101 ? 0.5397 0.4015 0.5961 0.0436  -0.0468 -0.1052 907  TRP   A CD1 
749  C CD2 . TRP   A 101 ? 0.5226 0.4132 0.5619 0.0265  -0.0321 -0.0931 907  TRP   A CD2 
750  N NE1 . TRP   A 101 ? 0.5500 0.3957 0.5980 0.0322  -0.0538 -0.1003 907  TRP   A NE1 
751  C CE2 . TRP   A 101 ? 0.5297 0.3950 0.5690 0.0224  -0.0450 -0.0934 907  TRP   A CE2 
752  C CE3 . TRP   A 101 ? 0.5173 0.4255 0.5456 0.0185  -0.0239 -0.0861 907  TRP   A CE3 
753  C CZ2 . TRP   A 101 ? 0.5621 0.4246 0.5943 0.0104  -0.0491 -0.0882 907  TRP   A CZ2 
754  C CZ3 . TRP   A 101 ? 0.5251 0.4280 0.5458 0.0089  -0.0296 -0.0809 907  TRP   A CZ3 
755  C CH2 . TRP   A 101 ? 0.5481 0.4310 0.5723 0.0050  -0.0416 -0.0827 907  TRP   A CH2 
756  N N   . ASN   A 102 ? 0.5330 0.5141 0.6037 0.0642  0.0069  -0.1525 908  ASN   A N   
757  C CA  . ASN   A 102 ? 0.5262 0.5414 0.6029 0.0628  0.0218  -0.1577 908  ASN   A CA  
758  C C   . ASN   A 102 ? 0.5078 0.5336 0.5582 0.0451  0.0347  -0.1488 908  ASN   A C   
759  O O   . ASN   A 102 ? 0.4973 0.5173 0.5263 0.0385  0.0370  -0.1543 908  ASN   A O   
760  C CB  . ASN   A 102 ? 0.4580 0.4967 0.5506 0.0751  0.0280  -0.1871 908  ASN   A CB  
761  C CG  . ASN   A 102 ? 0.4675 0.5455 0.5713 0.0723  0.0434  -0.1934 908  ASN   A CG  
762  O OD1 . ASN   A 102 ? 0.5476 0.6529 0.6433 0.0652  0.0596  -0.2087 908  ASN   A OD1 
763  N ND2 . ASN   A 102 ? 0.5400 0.6212 0.6608 0.0757  0.0385  -0.1814 908  ASN   A ND2 
764  N N   . GLY   A 103 ? 0.5143 0.5515 0.5639 0.0374  0.0409  -0.1344 909  GLY   A N   
765  C CA  . GLY   A 103 ? 0.4705 0.5116 0.4935 0.0210  0.0499  -0.1241 909  GLY   A CA  
766  C C   . GLY   A 103 ? 0.4834 0.4995 0.4907 0.0144  0.0401  -0.1048 909  GLY   A C   
767  O O   . GLY   A 103 ? 0.4650 0.4792 0.4490 0.0025  0.0438  -0.0959 909  GLY   A O   
768  N N   . LYS   A 104 ? 0.4796 0.4765 0.4989 0.0211  0.0272  -0.0984 910  LYS   A N   
769  C CA  . LYS   A 104 ? 0.4676 0.4473 0.4774 0.0146  0.0188  -0.0824 910  LYS   A CA  
770  C C   . LYS   A 104 ? 0.4509 0.4235 0.4774 0.0171  0.0120  -0.0682 910  LYS   A C   
771  O O   . LYS   A 104 ? 0.4449 0.4066 0.4700 0.0126  0.0049  -0.0576 910  LYS   A O   
772  C CB  . LYS   A 104 ? 0.4874 0.4509 0.4893 0.0143  0.0101  -0.0892 910  LYS   A CB  
773  C CG  . LYS   A 104 ? 0.5056 0.4739 0.4862 0.0106  0.0161  -0.1035 910  LYS   A CG  
774  C CD  . LYS   A 104 ? 0.5483 0.4993 0.5228 0.0117  0.0059  -0.1123 910  LYS   A CD  
775  C CE  . LYS   A 104 ? 0.4946 0.4479 0.4396 0.0048  0.0107  -0.1232 910  LYS   A CE  
776  N NZ  . LYS   A 104 ? 0.6692 0.6108 0.6122 0.0097  0.0041  -0.1405 910  LYS   A NZ  
777  N N   . MET   A 105 ? 0.4581 0.4381 0.5003 0.0236  0.0138  -0.0686 911  MET   A N   
778  C CA  . MET   A 105 ? 0.4118 0.3824 0.4657 0.0255  0.0067  -0.0560 911  MET   A CA  
779  C C   . MET   A 105 ? 0.4328 0.4183 0.4917 0.0256  0.0128  -0.0499 911  MET   A C   
780  O O   . MET   A 105 ? 0.4299 0.4295 0.4979 0.0315  0.0170  -0.0598 911  MET   A O   
781  C CB  . MET   A 105 ? 0.4242 0.3794 0.4905 0.0347  -0.0035 -0.0627 911  MET   A CB  
782  C CG  . MET   A 105 ? 0.4886 0.4296 0.5609 0.0341  -0.0118 -0.0483 911  MET   A CG  
783  S SD  . MET   A 105 ? 0.5456 0.4531 0.6209 0.0376  -0.0284 -0.0497 911  MET   A SD  
784  C CE  . MET   A 105 ? 0.4690 0.3798 0.5565 0.0555  -0.0316 -0.0735 911  MET   A CE  
785  N N   . LEU   A 106 ? 0.4405 0.4247 0.4951 0.0194  0.0130  -0.0355 912  LEU   A N   
786  C CA  . LEU   A 106 ? 0.3974 0.3926 0.4542 0.0183  0.0176  -0.0287 912  LEU   A CA  
787  C C   . LEU   A 106 ? 0.4117 0.3986 0.4767 0.0207  0.0110  -0.0194 912  LEU   A C   
788  O O   . LEU   A 106 ? 0.4024 0.3753 0.4667 0.0180  0.0049  -0.0130 912  LEU   A O   
789  C CB  . LEU   A 106 ? 0.3481 0.3459 0.3916 0.0104  0.0217  -0.0205 912  LEU   A CB  
790  C CG  . LEU   A 106 ? 0.3889 0.3919 0.4167 0.0049  0.0277  -0.0257 912  LEU   A CG  
791  C CD1 . LEU   A 106 ? 0.3722 0.3698 0.3935 0.0050  0.0261  -0.0350 912  LEU   A CD1 
792  C CD2 . LEU   A 106 ? 0.3635 0.3608 0.3781 -0.0008 0.0263  -0.0159 912  LEU   A CD2 
793  N N   . ASN   A 107 ? 0.3976 0.3934 0.4688 0.0239  0.0122  -0.0185 913  ASN   A N   
794  C CA  . ASN   A 107 ? 0.3905 0.3779 0.4642 0.0249  0.0058  -0.0088 913  ASN   A CA  
795  C C   . ASN   A 107 ? 0.4009 0.4001 0.4715 0.0214  0.0110  -0.0029 913  ASN   A C   
796  O O   . ASN   A 107 ? 0.4098 0.4239 0.4821 0.0212  0.0172  -0.0089 913  ASN   A O   
797  C CB  . ASN   A 107 ? 0.4479 0.4295 0.5329 0.0350  -0.0035 -0.0151 913  ASN   A CB  
798  C CG  . ASN   A 107 ? 0.4611 0.4295 0.5431 0.0351  -0.0124 -0.0038 913  ASN   A CG  
799  O OD1 . ASN   A 107 ? 0.4879 0.4409 0.5592 0.0274  -0.0151 0.0074  913  ASN   A OD1 
800  N ND2 . ASN   A 107 ? 0.4390 0.4146 0.5298 0.0427  -0.0172 -0.0073 913  ASN   A ND2 
801  N N   . ILE   A 108 ? 0.4259 0.4184 0.4904 0.0172  0.0091  0.0081  914  ILE   A N   
802  C CA  . ILE   A 108 ? 0.3776 0.3780 0.4382 0.0149  0.0121  0.0130  914  ILE   A CA  
803  C C   . ILE   A 108 ? 0.4321 0.4268 0.4950 0.0189  0.0038  0.0162  914  ILE   A C   
804  O O   . ILE   A 108 ? 0.4809 0.4598 0.5379 0.0171  -0.0027 0.0236  914  ILE   A O   
805  C CB  . ILE   A 108 ? 0.3733 0.3730 0.4251 0.0083  0.0159  0.0203  914  ILE   A CB  
806  C CG1 . ILE   A 108 ? 0.4050 0.4111 0.4519 0.0071  0.0182  0.0232  914  ILE   A CG1 
807  C CG2 . ILE   A 108 ? 0.3691 0.3579 0.4181 0.0040  0.0122  0.0271  914  ILE   A CG2 
808  C CD1 . ILE   A 108 ? 0.3143 0.3293 0.3620 0.0077  0.0217  0.0178  914  ILE   A CD1 
809  N N   . HIS   A 109 ? 0.4208 0.4273 0.4911 0.0232  0.0032  0.0109  915  HIS   A N   
810  C CA  . HIS   A 109 ? 0.4136 0.4162 0.4870 0.0284  -0.0071 0.0127  915  HIS   A CA  
811  C C   . HIS   A 109 ? 0.4240 0.4354 0.4914 0.0241  -0.0045 0.0166  915  HIS   A C   
812  O O   . HIS   A 109 ? 0.3737 0.3999 0.4438 0.0209  0.0036  0.0117  915  HIS   A O   
813  C CB  . HIS   A 109 ? 0.3803 0.3928 0.4731 0.0390  -0.0127 -0.0002 915  HIS   A CB  
814  C CG  . HIS   A 109 ? 0.4290 0.4391 0.5281 0.0466  -0.0264 -0.0001 915  HIS   A CG  
815  N ND1 . HIS   A 109 ? 0.4694 0.4541 0.5622 0.0518  -0.0419 0.0063  915  HIS   A ND1 
816  C CD2 . HIS   A 109 ? 0.3740 0.4020 0.4837 0.0493  -0.0286 -0.0053 915  HIS   A CD2 
817  C CE1 . HIS   A 109 ? 0.4688 0.4549 0.5674 0.0589  -0.0544 0.0051  915  HIS   A CE1 
818  N NE2 . HIS   A 109 ? 0.3790 0.3935 0.4898 0.0577  -0.0463 -0.0026 915  HIS   A NE2 
819  N N   . PRO   A 110 ? 0.4310 0.4313 0.4872 0.0228  -0.0118 0.0252  916  PRO   A N   
820  C CA  . PRO   A 110 ? 0.4487 0.4549 0.4952 0.0177  -0.0087 0.0286  916  PRO   A CA  
821  C C   . PRO   A 110 ? 0.4196 0.4370 0.4760 0.0223  -0.0155 0.0230  916  PRO   A C   
822  O O   . PRO   A 110 ? 0.4078 0.4203 0.4543 0.0214  -0.0227 0.0277  916  PRO   A O   
823  C CB  . PRO   A 110 ? 0.4449 0.4341 0.4715 0.0123  -0.0123 0.0399  916  PRO   A CB  
824  C CG  . PRO   A 110 ? 0.4841 0.4551 0.5116 0.0168  -0.0248 0.0431  916  PRO   A CG  
825  C CD  . PRO   A 110 ? 0.4626 0.4419 0.5120 0.0256  -0.0250 0.0318  916  PRO   A CD  
826  N N   . SER   A 111 ? 0.4024 0.4371 0.4784 0.0262  -0.0132 0.0118  917  SER   A N   
827  C CA  . SER   A 111 ? 0.3363 0.3896 0.4256 0.0275  -0.0163 0.0042  917  SER   A CA  
828  C C   . SER   A 111 ? 0.3617 0.4364 0.4640 0.0230  -0.0046 -0.0063 917  SER   A C   
829  O O   . SER   A 111 ? 0.3630 0.4363 0.4636 0.0211  0.0038  -0.0080 917  SER   A O   
830  C CB  . SER   A 111 ? 0.3233 0.3778 0.4275 0.0391  -0.0326 -0.0004 917  SER   A CB  
831  O OG  . SER   A 111 ? 0.3277 0.3929 0.4536 0.0478  -0.0335 -0.0123 917  SER   A OG  
832  N N   . LEU   A 112 ? 0.3592 0.4536 0.4725 0.0195  -0.0042 -0.0132 918  LEU   A N   
833  C CA  . LEU   A 112 ? 0.3008 0.4190 0.4272 0.0125  0.0067  -0.0243 918  LEU   A CA  
834  C C   . LEU   A 112 ? 0.2899 0.4292 0.4445 0.0233  0.0025  -0.0386 918  LEU   A C   
835  O O   . LEU   A 112 ? 0.2944 0.4548 0.4705 0.0276  -0.0046 -0.0479 918  LEU   A O   
836  C CB  . LEU   A 112 ? 0.2932 0.4232 0.4187 0.0012  0.0091  -0.0255 918  LEU   A CB  
837  C CG  . LEU   A 112 ? 0.3077 0.4155 0.4056 -0.0085 0.0137  -0.0144 918  LEU   A CG  
838  C CD1 . LEU   A 112 ? 0.3203 0.4357 0.4164 -0.0198 0.0141  -0.0164 918  LEU   A CD1 
839  C CD2 . LEU   A 112 ? 0.2567 0.3559 0.3422 -0.0144 0.0244  -0.0125 918  LEU   A CD2 
840  N N   . LEU   A 113 ? 0.2829 0.4166 0.4388 0.0289  0.0055  -0.0418 919  LEU   A N   
841  C CA  . LEU   A 113 ? 0.2794 0.4325 0.4622 0.0407  0.0021  -0.0583 919  LEU   A CA  
842  C C   . LEU   A 113 ? 0.2489 0.4419 0.4522 0.0329  0.0135  -0.0745 919  LEU   A C   
843  O O   . LEU   A 113 ? 0.2538 0.4523 0.4432 0.0159  0.0276  -0.0717 919  LEU   A O   
844  C CB  . LEU   A 113 ? 0.3446 0.4844 0.5215 0.0452  0.0058  -0.0601 919  LEU   A CB  
845  C CG  . LEU   A 113 ? 0.3660 0.4697 0.5274 0.0522  -0.0058 -0.0470 919  LEU   A CG  
846  C CD1 . LEU   A 113 ? 0.3278 0.4211 0.4816 0.0519  0.0006  -0.0491 919  LEU   A CD1 
847  C CD2 . LEU   A 113 ? 0.3172 0.4121 0.4925 0.0682  -0.0260 -0.0498 919  LEU   A CD2 
848  N N   . PRO   A 114 ? 0.2281 0.4496 0.4646 0.0444  0.0073  -0.0923 920  PRO   A N   
849  C CA  . PRO   A 114 ? 0.2715 0.4832 0.5245 0.0664  -0.0117 -0.0978 920  PRO   A CA  
850  C C   . PRO   A 114 ? 0.2922 0.4844 0.5420 0.0746  -0.0328 -0.0870 920  PRO   A C   
851  O O   . PRO   A 114 ? 0.3617 0.5413 0.6221 0.0923  -0.0511 -0.0906 920  PRO   A O   
852  C CB  . PRO   A 114 ? 0.2343 0.4911 0.5279 0.0752  -0.0096 -0.1250 920  PRO   A CB  
853  C CG  . PRO   A 114 ? 0.2247 0.5172 0.5262 0.0568  0.0051  -0.1304 920  PRO   A CG  
854  C CD  . PRO   A 114 ? 0.2419 0.5094 0.5035 0.0359  0.0188  -0.1105 920  PRO   A CD  
855  N N   . SER   A 115 ? 0.3007 0.4882 0.5348 0.0627  -0.0320 -0.0749 921  SER   A N   
856  C CA  . SER   A 115 ? 0.3179 0.4850 0.5440 0.0698  -0.0521 -0.0646 921  SER   A CA  
857  C C   . SER   A 115 ? 0.3196 0.4428 0.5185 0.0749  -0.0613 -0.0485 921  SER   A C   
858  O O   . SER   A 115 ? 0.2950 0.4016 0.4728 0.0664  -0.0490 -0.0392 921  SER   A O   
859  C CB  . SER   A 115 ? 0.2659 0.4334 0.4754 0.0548  -0.0480 -0.0549 921  SER   A CB  
860  O OG  . SER   A 115 ? 0.2922 0.4981 0.5267 0.0486  -0.0436 -0.0688 921  SER   A OG  
861  N N   . PHE   A 116 ? 0.3482 0.4520 0.5467 0.0879  -0.0841 -0.0451 922  PHE   A N   
862  C CA  . PHE   A 116 ? 0.3311 0.3902 0.4973 0.0877  -0.0945 -0.0265 922  PHE   A CA  
863  C C   . PHE   A 116 ? 0.3537 0.3954 0.5132 0.0884  -0.0876 -0.0247 922  PHE   A C   
864  O O   . PHE   A 116 ? 0.3801 0.4003 0.5129 0.0773  -0.0793 -0.0105 922  PHE   A O   
865  C CB  . PHE   A 116 ? 0.3603 0.4066 0.4947 0.0719  -0.0871 -0.0098 922  PHE   A CB  
866  C CG  . PHE   A 116 ? 0.3217 0.3872 0.4622 0.0690  -0.0909 -0.0131 922  PHE   A CG  
867  C CD1 . PHE   A 116 ? 0.3337 0.4047 0.4910 0.0815  -0.1127 -0.0200 922  PHE   A CD1 
868  C CD2 . PHE   A 116 ? 0.2845 0.3614 0.4151 0.0546  -0.0751 -0.0106 922  PHE   A CD2 
869  C CE1 . PHE   A 116 ? 0.3393 0.4293 0.5036 0.0782  -0.1176 -0.0240 922  PHE   A CE1 
870  C CE2 . PHE   A 116 ? 0.2906 0.3836 0.4266 0.0508  -0.0795 -0.0144 922  PHE   A CE2 
871  C CZ  . PHE   A 116 ? 0.3284 0.4296 0.4817 0.0619  -0.1002 -0.0212 922  PHE   A CZ  
872  N N   . LYS   A 117 ? 0.4145 0.4684 0.6004 0.1015  -0.0909 -0.0415 923  LYS   A N   
873  C CA  . LYS   A 117 ? 0.3659 0.3956 0.5451 0.1057  -0.0924 -0.0405 923  LYS   A CA  
874  C C   . LYS   A 117 ? 0.4549 0.4377 0.6076 0.1073  -0.1124 -0.0231 923  LYS   A C   
875  O O   . LYS   A 117 ? 0.5109 0.4814 0.6572 0.1116  -0.1303 -0.0169 923  LYS   A O   
876  C CB  . LYS   A 117 ? 0.3810 0.4297 0.5941 0.1233  -0.0976 -0.0641 923  LYS   A CB  
877  C CG  . LYS   A 117 ? 0.3852 0.4825 0.6233 0.1194  -0.0768 -0.0827 923  LYS   A CG  
878  C CD  . LYS   A 117 ? 0.4125 0.5280 0.6815 0.1364  -0.0799 -0.1077 923  LYS   A CD  
879  C CE  . LYS   A 117 ? 0.4669 0.6369 0.7637 0.1321  -0.0606 -0.1289 923  LYS   A CE  
880  N NZ  . LYS   A 117 ? 0.5192 0.6937 0.7952 0.1129  -0.0354 -0.1239 923  LYS   A NZ  
881  N N   . GLY   A 118 ? 0.5210 0.4764 0.6562 0.1023  -0.1103 -0.0150 924  GLY   A N   
882  C CA  . GLY   A 118 ? 0.5569 0.4658 0.6658 0.1014  -0.1294 0.0009  924  GLY   A CA  
883  C C   . GLY   A 118 ? 0.6153 0.5082 0.6895 0.0804  -0.1189 0.0219  924  GLY   A C   
884  O O   . GLY   A 118 ? 0.6119 0.5274 0.6837 0.0688  -0.0976 0.0234  924  GLY   A O   
885  N N   . SER   A 119 ? 0.6378 0.4899 0.6837 0.0754  -0.1350 0.0379  925  SER   A N   
886  C CA  . SER   A 119 ? 0.7108 0.5470 0.7251 0.0541  -0.1237 0.0555  925  SER   A CA  
887  C C   . SER   A 119 ? 0.7027 0.5445 0.6952 0.0424  -0.1187 0.0667  925  SER   A C   
888  O O   . SER   A 119 ? 0.6988 0.5452 0.6742 0.0257  -0.1018 0.0752  925  SER   A O   
889  C CB  . SER   A 119 ? 0.6934 0.4818 0.6837 0.0490  -0.1403 0.0678  925  SER   A CB  
890  O OG  . SER   A 119 ? 0.7740 0.5333 0.7551 0.0594  -0.1680 0.0718  925  SER   A OG  
891  N N   . ASN   A 120 ? 0.6068 0.4504 0.6008 0.0511  -0.1330 0.0653  926  ASN   A N   
892  C CA  . ASN   A 120 ? 0.6518 0.4984 0.6216 0.0394  -0.1290 0.0753  926  ASN   A CA  
893  C C   . ASN   A 120 ? 0.5645 0.4510 0.5579 0.0449  -0.1189 0.0626  926  ASN   A C   
894  O O   . ASN   A 120 ? 0.5411 0.4303 0.5320 0.0491  -0.1310 0.0621  926  ASN   A O   
895  C CB  . ASN   A 120 ? 0.7453 0.5565 0.6887 0.0409  -0.1554 0.0868  926  ASN   A CB  
896  C CG  . ASN   A 120 ? 0.7767 0.5850 0.7465 0.0638  -0.1797 0.0750  926  ASN   A CG  
897  O OD1 . ASN   A 120 ? 0.7288 0.5585 0.7348 0.0768  -0.1753 0.0585  926  ASN   A OD1 
898  N ND2 . ASN   A 120 ? 0.8071 0.5909 0.7599 0.0693  -0.2059 0.0817  926  ASN   A ND2 
899  N N   . ALA   A 121 ? 0.4952 0.4101 0.5091 0.0436  -0.0983 0.0527  927  ALA   A N   
900  C CA  . ALA   A 121 ? 0.5100 0.4603 0.5476 0.0478  -0.0897 0.0398  927  ALA   A CA  
901  C C   . ALA   A 121 ? 0.4970 0.4527 0.5170 0.0393  -0.0871 0.0452  927  ALA   A C   
902  O O   . ALA   A 121 ? 0.5016 0.4728 0.5340 0.0446  -0.0945 0.0381  927  ALA   A O   
903  C CB  . ALA   A 121 ? 0.4446 0.4164 0.4974 0.0443  -0.0686 0.0318  927  ALA   A CB  
904  N N   . HIS   A 122 ? 0.4845 0.4295 0.4767 0.0258  -0.0767 0.0561  928  HIS   A N   
905  C CA  . HIS   A 122 ? 0.4190 0.3682 0.3924 0.0180  -0.0736 0.0594  928  HIS   A CA  
906  C C   . HIS   A 122 ? 0.5261 0.4597 0.4850 0.0216  -0.0954 0.0644  928  HIS   A C   
907  O O   . HIS   A 122 ? 0.4864 0.4318 0.4454 0.0220  -0.0991 0.0601  928  HIS   A O   
908  C CB  . HIS   A 122 ? 0.4409 0.3827 0.3881 0.0041  -0.0593 0.0680  928  HIS   A CB  
909  C CG  . HIS   A 122 ? 0.4183 0.3773 0.3795 0.0015  -0.0400 0.0620  928  HIS   A CG  
910  N ND1 . HIS   A 122 ? 0.4190 0.3993 0.3986 0.0049  -0.0316 0.0516  928  HIS   A ND1 
911  C CD2 . HIS   A 122 ? 0.4399 0.3963 0.3983 -0.0047 -0.0292 0.0651  928  HIS   A CD2 
912  C CE1 . HIS   A 122 ? 0.4327 0.4201 0.4182 0.0021  -0.0179 0.0491  928  HIS   A CE1 
913  N NE2 . HIS   A 122 ? 0.4585 0.4339 0.4336 -0.0029 -0.0162 0.0564  928  HIS   A NE2 
914  N N   . GLU   A 123 ? 0.5443 0.4483 0.4883 0.0236  -0.1121 0.0738  929  GLU   A N   
915  C CA  . GLU   A 123 ? 0.5315 0.4162 0.4597 0.0282  -0.1368 0.0791  929  GLU   A CA  
916  C C   . GLU   A 123 ? 0.5109 0.4175 0.4762 0.0452  -0.1501 0.0642  929  GLU   A C   
917  O O   . GLU   A 123 ? 0.5340 0.4459 0.4966 0.0476  -0.1625 0.0621  929  GLU   A O   
918  C CB  . GLU   A 123 ? 0.6135 0.4564 0.5173 0.0273  -0.1549 0.0926  929  GLU   A CB  
919  C CG  . GLU   A 123 ? 0.6700 0.4946 0.5406 0.0079  -0.1406 0.1063  929  GLU   A CG  
920  C CD  . GLU   A 123 ? 0.8451 0.6233 0.6866 0.0034  -0.1601 0.1214  929  GLU   A CD  
921  O OE1 . GLU   A 123 ? 0.9082 0.6701 0.7666 0.0194  -0.1814 0.1178  929  GLU   A OE1 
922  O OE2 . GLU   A 123 ? 0.9143 0.6718 0.7151 -0.0168 -0.1545 0.1363  929  GLU   A OE2 
923  N N   . GLN   A 124 ? 0.4943 0.4161 0.4950 0.0563  -0.1474 0.0524  930  GLN   A N   
924  C CA  . GLN   A 124 ? 0.4977 0.4496 0.5388 0.0708  -0.1555 0.0347  930  GLN   A CA  
925  C C   . GLN   A 124 ? 0.4369 0.4213 0.4877 0.0635  -0.1420 0.0273  930  GLN   A C   
926  O O   . GLN   A 124 ? 0.4432 0.4428 0.5080 0.0691  -0.1552 0.0197  930  GLN   A O   
927  C CB  . GLN   A 124 ? 0.4697 0.4372 0.5439 0.0803  -0.1478 0.0218  930  GLN   A CB  
928  C CG  . GLN   A 124 ? 0.4837 0.4215 0.5578 0.0924  -0.1667 0.0236  930  GLN   A CG  
929  C CD  . GLN   A 124 ? 0.4841 0.4409 0.5905 0.1012  -0.1566 0.0081  930  GLN   A CD  
930  O OE1 . GLN   A 124 ? 0.4807 0.4720 0.6247 0.1125  -0.1568 -0.0111 930  GLN   A OE1 
931  N NE2 . GLN   A 124 ? 0.4459 0.3838 0.5383 0.0946  -0.1462 0.0150  930  GLN   A NE2 
932  N N   . ALA   A 125 ? 0.3914 0.3854 0.4351 0.0511  -0.1174 0.0288  931  ALA   A N   
933  C CA  . ALA   A 125 ? 0.3907 0.4095 0.4407 0.0430  -0.1050 0.0222  931  ALA   A CA  
934  C C   . ALA   A 125 ? 0.5010 0.5108 0.5271 0.0381  -0.1158 0.0279  931  ALA   A C   
935  O O   . ALA   A 125 ? 0.4443 0.4742 0.4838 0.0372  -0.1190 0.0192  931  ALA   A O   
936  C CB  . ALA   A 125 ? 0.3289 0.3499 0.3694 0.0321  -0.0809 0.0249  931  ALA   A CB  
937  N N   . LEU   A 126 ? 0.5101 0.4900 0.4988 0.0327  -0.1207 0.0420  932  LEU   A N   
938  C CA  . LEU   A 126 ? 0.4505 0.4208 0.4112 0.0266  -0.1297 0.0470  932  LEU   A CA  
939  C C   . LEU   A 126 ? 0.4649 0.4304 0.4319 0.0373  -0.1581 0.0452  932  LEU   A C   
940  O O   . LEU   A 126 ? 0.4770 0.4533 0.4447 0.0363  -0.1668 0.0400  932  LEU   A O   
941  C CB  . LEU   A 126 ? 0.4696 0.4128 0.3864 0.0151  -0.1236 0.0615  932  LEU   A CB  
942  C CG  . LEU   A 126 ? 0.5052 0.4575 0.4177 0.0055  -0.0967 0.0606  932  LEU   A CG  
943  C CD1 . LEU   A 126 ? 0.4951 0.4262 0.3755 -0.0048 -0.0894 0.0731  932  LEU   A CD1 
944  C CD2 . LEU   A 126 ? 0.4302 0.3973 0.3379 -0.0004 -0.0869 0.0531  932  LEU   A CD2 
945  N N   . GLU   A 127 ? 0.5611 0.5102 0.5346 0.0484  -0.1748 0.0482  933  GLU   A N   
946  C CA  . GLU   A 127 ? 0.5741 0.5185 0.5585 0.0622  -0.2056 0.0445  933  GLU   A CA  
947  C C   . GLU   A 127 ? 0.5608 0.5487 0.5929 0.0706  -0.2070 0.0246  933  GLU   A C   
948  O O   . GLU   A 127 ? 0.5177 0.5128 0.5545 0.0748  -0.2263 0.0198  933  GLU   A O   
949  C CB  . GLU   A 127 ? 0.5787 0.4975 0.5667 0.0749  -0.2228 0.0485  933  GLU   A CB  
950  C CG  . GLU   A 127 ? 0.6795 0.5975 0.6917 0.0953  -0.2562 0.0397  933  GLU   A CG  
951  C CD  . GLU   A 127 ? 0.8993 0.7979 0.8825 0.0946  -0.2824 0.0474  933  GLU   A CD  
952  O OE1 . GLU   A 127 ? 0.9055 0.8115 0.9135 0.1116  -0.3105 0.0373  933  GLU   A OE1 
953  O OE2 . GLU   A 127 ? 0.9709 0.8488 0.9072 0.0774  -0.2755 0.0621  933  GLU   A OE2 
954  N N   . THR   A 128 ? 0.5205 0.5385 0.5868 0.0709  -0.1862 0.0128  934  THR   A N   
955  C CA  . THR   A 128 ? 0.4589 0.5217 0.5707 0.0748  -0.1832 -0.0068 934  THR   A CA  
956  C C   . THR   A 128 ? 0.3892 0.4678 0.4940 0.0605  -0.1744 -0.0088 934  THR   A C   
957  O O   . THR   A 128 ? 0.4477 0.5553 0.5802 0.0622  -0.1829 -0.0218 934  THR   A O   
958  C CB  . THR   A 128 ? 0.4734 0.5595 0.6139 0.0749  -0.1612 -0.0168 934  THR   A CB  
959  O OG1 . THR   A 128 ? 0.4942 0.5653 0.6427 0.0892  -0.1709 -0.0171 934  THR   A OG1 
960  C CG2 . THR   A 128 ? 0.3733 0.5079 0.5587 0.0752  -0.1555 -0.0371 934  THR   A CG2 
961  N N   . GLY   A 129 ? 0.4589 0.5198 0.5289 0.0465  -0.1577 0.0022  935  GLY   A N   
962  C CA  . GLY   A 129 ? 0.4399 0.5092 0.4991 0.0339  -0.1511 0.0000  935  GLY   A CA  
963  C C   . GLY   A 129 ? 0.4093 0.5038 0.4886 0.0238  -0.1288 -0.0092 935  GLY   A C   
964  O O   . GLY   A 129 ? 0.4090 0.5202 0.4964 0.0157  -0.1290 -0.0169 935  GLY   A O   
965  N N   . VAL   A 130 ? 0.3512 0.4467 0.4363 0.0229  -0.1108 -0.0082 936  VAL   A N   
966  C CA  . VAL   A 130 ? 0.3597 0.4739 0.4585 0.0122  -0.0910 -0.0152 936  VAL   A CA  
967  C C   . VAL   A 130 ? 0.3307 0.4261 0.3978 0.0006  -0.0800 -0.0085 936  VAL   A C   
968  O O   . VAL   A 130 ? 0.3492 0.4199 0.3863 0.0016  -0.0801 0.0014  936  VAL   A O   
969  C CB  . VAL   A 130 ? 0.3209 0.4410 0.4344 0.0157  -0.0775 -0.0170 936  VAL   A CB  
970  C CG1 . VAL   A 130 ? 0.2871 0.4258 0.4332 0.0296  -0.0894 -0.0266 936  VAL   A CG1 
971  C CG2 . VAL   A 130 ? 0.2887 0.3789 0.3734 0.0166  -0.0702 -0.0039 936  VAL   A CG2 
972  N N   . THR   A 131 ? 0.3499 0.4567 0.4231 -0.0111 -0.0704 -0.0148 937  THR   A N   
973  C CA  . THR   A 131 ? 0.3354 0.4221 0.3806 -0.0198 -0.0613 -0.0104 937  THR   A CA  
974  C C   . THR   A 131 ? 0.3520 0.4323 0.3943 -0.0230 -0.0443 -0.0079 937  THR   A C   
975  O O   . THR   A 131 ? 0.4315 0.4933 0.4519 -0.0268 -0.0375 -0.0047 937  THR   A O   
976  C CB  . THR   A 131 ? 0.3521 0.4452 0.3981 -0.0313 -0.0650 -0.0175 937  THR   A CB  
977  O OG1 . THR   A 131 ? 0.3462 0.4588 0.4147 -0.0415 -0.0560 -0.0244 937  THR   A OG1 
978  C CG2 . THR   A 131 ? 0.3536 0.4576 0.4077 -0.0275 -0.0839 -0.0215 937  THR   A CG2 
979  N N   . VAL   A 132 ? 0.3194 0.4139 0.3827 -0.0200 -0.0386 -0.0101 938  VAL   A N   
980  C CA  . VAL   A 132 ? 0.3198 0.4079 0.3795 -0.0223 -0.0244 -0.0075 938  VAL   A CA  
981  C C   . VAL   A 132 ? 0.3133 0.4046 0.3840 -0.0113 -0.0243 -0.0056 938  VAL   A C   
982  O O   . VAL   A 132 ? 0.3254 0.4353 0.4196 -0.0054 -0.0306 -0.0120 938  VAL   A O   
983  C CB  . VAL   A 132 ? 0.3031 0.4058 0.3748 -0.0353 -0.0156 -0.0141 938  VAL   A CB  
984  C CG1 . VAL   A 132 ? 0.2807 0.3798 0.3509 -0.0364 -0.0032 -0.0120 938  VAL   A CG1 
985  C CG2 . VAL   A 132 ? 0.3142 0.4039 0.3690 -0.0473 -0.0161 -0.0141 938  VAL   A CG2 
986  N N   . THR   A 133 ? 0.2651 0.3385 0.3202 -0.0082 -0.0182 0.0018  939  THR   A N   
987  C CA  . THR   A 133 ? 0.2679 0.3415 0.3319 -0.0003 -0.0167 0.0032  939  THR   A CA  
988  C C   . THR   A 133 ? 0.2738 0.3395 0.3296 -0.0045 -0.0039 0.0055  939  THR   A C   
989  O O   . THR   A 133 ? 0.2845 0.3501 0.3353 -0.0131 0.0025  0.0035  939  THR   A O   
990  C CB  . THR   A 133 ? 0.3184 0.3762 0.3709 0.0076  -0.0267 0.0111  939  THR   A CB  
991  O OG1 . THR   A 133 ? 0.2883 0.3432 0.3497 0.0145  -0.0271 0.0120  939  THR   A OG1 
992  C CG2 . THR   A 133 ? 0.2815 0.3210 0.3065 0.0035  -0.0226 0.0192  939  THR   A CG2 
993  N N   . GLY   A 134 ? 0.3208 0.3774 0.3737 0.0008  -0.0018 0.0099  940  GLY   A N   
994  C CA  . GLY   A 134 ? 0.3263 0.3768 0.3730 -0.0024 0.0081  0.0110  940  GLY   A CA  
995  C C   . GLY   A 134 ? 0.3458 0.3922 0.3971 0.0036  0.0087  0.0129  940  GLY   A C   
996  O O   . GLY   A 134 ? 0.3506 0.3920 0.4034 0.0093  0.0013  0.0161  940  GLY   A O   
997  N N   . CYS   A 135 ? 0.3465 0.3924 0.3977 0.0013  0.0161  0.0113  941  CYS   A N   
998  C CA  . CYS   A 135 ? 0.3556 0.3976 0.4114 0.0061  0.0164  0.0116  941  CYS   A CA  
999  C C   . CYS   A 135 ? 0.3588 0.4103 0.4217 0.0038  0.0228  0.0041  941  CYS   A C   
1000 O O   . CYS   A 135 ? 0.3239 0.3815 0.3832 -0.0040 0.0283  0.0011  941  CYS   A O   
1001 C CB  . CYS   A 135 ? 0.3313 0.3601 0.3749 0.0053  0.0183  0.0183  941  CYS   A CB  
1002 S SG  . CYS   A 135 ? 0.3547 0.3792 0.3862 0.0000  0.0240  0.0184  941  CYS   A SG  
1003 N N   . THR   A 136 ? 0.3372 0.3876 0.4073 0.0092  0.0218  0.0011  942  THR   A N   
1004 C CA  . THR   A 136 ? 0.3677 0.4278 0.4435 0.0079  0.0279  -0.0078 942  THR   A CA  
1005 C C   . THR   A 136 ? 0.3865 0.4336 0.4563 0.0101  0.0279  -0.0059 942  THR   A C   
1006 O O   . THR   A 136 ? 0.3854 0.4213 0.4570 0.0155  0.0214  -0.0018 942  THR   A O   
1007 C CB  . THR   A 136 ? 0.3393 0.4174 0.4368 0.0150  0.0251  -0.0195 942  THR   A CB  
1008 O OG1 . THR   A 136 ? 0.3267 0.4188 0.4322 0.0128  0.0233  -0.0216 942  THR   A OG1 
1009 C CG2 . THR   A 136 ? 0.3228 0.4162 0.4255 0.0120  0.0343  -0.0316 942  THR   A CG2 
1010 N N   . VAL   A 137 ? 0.3262 0.3734 0.3868 0.0042  0.0344  -0.0085 943  VAL   A N   
1011 C CA  . VAL   A 137 ? 0.3481 0.3876 0.4058 0.0063  0.0342  -0.0108 943  VAL   A CA  
1012 C C   . VAL   A 137 ? 0.3742 0.4283 0.4394 0.0069  0.0394  -0.0242 943  VAL   A C   
1013 O O   . VAL   A 137 ? 0.3507 0.4185 0.4126 -0.0009 0.0472  -0.0291 943  VAL   A O   
1014 C CB  . VAL   A 137 ? 0.3670 0.3945 0.4071 0.0004  0.0353  -0.0050 943  VAL   A CB  
1015 C CG1 . VAL   A 137 ? 0.3297 0.3505 0.3677 0.0022  0.0337  -0.0086 943  VAL   A CG1 
1016 C CG2 . VAL   A 137 ? 0.3150 0.3336 0.3521 0.0013  0.0311  0.0044  943  VAL   A CG2 
1017 N N   . HIS   A 138 ? 0.3690 0.4207 0.4442 0.0154  0.0351  -0.0309 944  HIS   A N   
1018 C CA  . HIS   A 138 ? 0.3502 0.4182 0.4363 0.0190  0.0395  -0.0472 944  HIS   A CA  
1019 C C   . HIS   A 138 ? 0.4047 0.4593 0.4886 0.0243  0.0355  -0.0518 944  HIS   A C   
1020 O O   . HIS   A 138 ? 0.4081 0.4422 0.4885 0.0267  0.0270  -0.0427 944  HIS   A O   
1021 C CB  . HIS   A 138 ? 0.4008 0.4843 0.5114 0.0291  0.0348  -0.0561 944  HIS   A CB  
1022 C CG  . HIS   A 138 ? 0.4196 0.4840 0.5385 0.0412  0.0201  -0.0522 944  HIS   A CG  
1023 N ND1 . HIS   A 138 ? 0.4133 0.4733 0.5450 0.0532  0.0126  -0.0639 944  HIS   A ND1 
1024 C CD2 . HIS   A 138 ? 0.4282 0.4747 0.5416 0.0417  0.0111  -0.0378 944  HIS   A CD2 
1025 C CE1 . HIS   A 138 ? 0.4269 0.4632 0.5587 0.0598  -0.0017 -0.0551 944  HIS   A CE1 
1026 N NE2 . HIS   A 138 ? 0.4380 0.4671 0.5580 0.0520  -0.0020 -0.0390 944  HIS   A NE2 
1027 N N   . PHE   A 139 ? 0.3980 0.4652 0.4829 0.0244  0.0422  -0.0670 945  PHE   A N   
1028 C CA  . PHE   A 139 ? 0.4037 0.4596 0.4894 0.0314  0.0373  -0.0757 945  PHE   A CA  
1029 C C   . PHE   A 139 ? 0.4150 0.4657 0.5228 0.0468  0.0255  -0.0824 945  PHE   A C   
1030 O O   . PHE   A 139 ? 0.4362 0.5036 0.5625 0.0538  0.0245  -0.0895 945  PHE   A O   
1031 C CB  . PHE   A 139 ? 0.4329 0.5062 0.5125 0.0274  0.0487  -0.0926 945  PHE   A CB  
1032 C CG  . PHE   A 139 ? 0.4074 0.4741 0.4577 0.0126  0.0554  -0.0853 945  PHE   A CG  
1033 C CD1 . PHE   A 139 ? 0.4632 0.5066 0.4985 0.0113  0.0482  -0.0780 945  PHE   A CD1 
1034 C CD2 . PHE   A 139 ? 0.4281 0.5108 0.4651 -0.0007 0.0677  -0.0859 945  PHE   A CD2 
1035 C CE1 . PHE   A 139 ? 0.4584 0.4938 0.4664 -0.0006 0.0510  -0.0718 945  PHE   A CE1 
1036 C CE2 . PHE   A 139 ? 0.4463 0.5166 0.4518 -0.0144 0.0707  -0.0779 945  PHE   A CE2 
1037 C CZ  . PHE   A 139 ? 0.4464 0.4930 0.4378 -0.0131 0.0615  -0.0711 945  PHE   A CZ  
1038 N N   . VAL   A 140 ? 0.4401 0.4659 0.5456 0.0518  0.0149  -0.0804 946  VAL   A N   
1039 C CA  . VAL   A 140 ? 0.4521 0.4642 0.5736 0.0660  0.0005  -0.0858 946  VAL   A CA  
1040 C C   . VAL   A 140 ? 0.4851 0.5108 0.6217 0.0782  0.0012  -0.1109 946  VAL   A C   
1041 O O   . VAL   A 140 ? 0.5019 0.5242 0.6300 0.0768  0.0048  -0.1206 946  VAL   A O   
1042 C CB  . VAL   A 140 ? 0.4818 0.4591 0.5930 0.0639  -0.0119 -0.0731 946  VAL   A CB  
1043 C CG1 . VAL   A 140 ? 0.4604 0.4164 0.5833 0.0777  -0.0292 -0.0784 946  VAL   A CG1 
1044 C CG2 . VAL   A 140 ? 0.4526 0.4231 0.5520 0.0523  -0.0108 -0.0514 946  VAL   A CG2 
1045 N N   . ALA   A 141 ? 0.5409 0.5840 0.7007 0.0905  -0.0025 -0.1231 947  ALA   A N   
1046 C CA  . ALA   A 141 ? 0.4976 0.5539 0.6789 0.1069  -0.0056 -0.1497 947  ALA   A CA  
1047 C C   . ALA   A 141 ? 0.5485 0.5744 0.7422 0.1243  -0.0297 -0.1500 947  ALA   A C   
1048 O O   . ALA   A 141 ? 0.5809 0.5780 0.7638 0.1208  -0.0417 -0.1287 947  ALA   A O   
1049 C CB  . ALA   A 141 ? 0.4955 0.5987 0.6976 0.1082  0.0075  -0.1663 947  ALA   A CB  
1050 N N   . GLU   A 142 ? 0.5903 0.6206 0.8049 0.1431  -0.0378 -0.1748 948  GLU   A N   
1051 C CA  . GLU   A 142 ? 0.6585 0.6517 0.8811 0.1603  -0.0644 -0.1748 948  GLU   A CA  
1052 C C   . GLU   A 142 ? 0.7068 0.7001 0.9407 0.1664  -0.0770 -0.1645 948  GLU   A C   
1053 O O   . GLU   A 142 ? 0.6869 0.6400 0.9058 0.1648  -0.0945 -0.1441 948  GLU   A O   
1054 C CB  . GLU   A 142 ? 0.6572 0.6554 0.9021 0.1821  -0.0721 -0.2067 948  GLU   A CB  
1055 C CG  . GLU   A 142 ? 0.7139 0.6804 0.9398 0.1792  -0.0750 -0.2094 948  GLU   A CG  
1056 C CD  . GLU   A 142 ? 0.9029 0.8700 1.1434 0.1969  -0.0840 -0.2366 948  GLU   A CD  
1057 O OE1 . GLU   A 142 ? 0.9165 0.9024 1.1533 0.1939  -0.0692 -0.2542 948  GLU   A OE1 
1058 O OE2 . GLU   A 142 ? 0.9580 0.9073 1.2083 0.2098  -0.1058 -0.2370 948  GLU   A OE2 
1059 N N   . ASP   A 143 ? 0.7297 0.7681 0.9878 0.1710  -0.0680 -0.1780 949  ASP   A N   
1060 C CA  . ASP   A 143 ? 0.7516 0.7934 1.0196 0.1751  -0.0794 -0.1683 949  ASP   A CA  
1061 C C   . ASP   A 143 ? 0.7053 0.7355 0.9447 0.1530  -0.0715 -0.1379 949  ASP   A C   
1062 O O   . ASP   A 143 ? 0.6965 0.7502 0.9263 0.1361  -0.0495 -0.1336 949  ASP   A O   
1063 C CB  . ASP   A 143 ? 0.8080 0.9061 1.1111 0.1829  -0.0699 -0.1917 949  ASP   A CB  
1064 C CG  . ASP   A 143 ? 0.9077 1.0175 1.2329 0.1999  -0.0788 -0.2179 949  ASP   A CG  
1065 O OD1 . ASP   A 143 ? 0.9110 0.9878 1.2365 0.2134  -0.1048 -0.2156 949  ASP   A OD1 
1066 O OD2 . ASP   A 143 ? 0.9892 1.1384 1.3253 0.1962  -0.0599 -0.2386 949  ASP   A OD2 
1067 N N   . VAL   A 144 ? 0.6284 0.6216 0.8532 0.1531  -0.0900 -0.1177 950  VAL   A N   
1068 C CA  . VAL   A 144 ? 0.6650 0.6421 0.8603 0.1327  -0.0834 -0.0901 950  VAL   A CA  
1069 C C   . VAL   A 144 ? 0.6816 0.6954 0.8815 0.1231  -0.0682 -0.0873 950  VAL   A C   
1070 O O   . VAL   A 144 ? 0.6591 0.6990 0.8826 0.1327  -0.0723 -0.0993 950  VAL   A O   
1071 C CB  . VAL   A 144 ? 0.6717 0.6026 0.8485 0.1338  -0.1064 -0.0710 950  VAL   A CB  
1072 C CG1 . VAL   A 144 ? 0.6479 0.5683 0.7960 0.1127  -0.0978 -0.0453 950  VAL   A CG1 
1073 C CG2 . VAL   A 144 ? 0.6449 0.5347 0.8129 0.1394  -0.1212 -0.0720 950  VAL   A CG2 
1074 N N   . ASP   A 145 ? 0.6193 0.6349 0.7979 0.1041  -0.0518 -0.0725 951  ASP   A N   
1075 C CA  . ASP   A 145 ? 0.5821 0.6268 0.7604 0.0927  -0.0369 -0.0691 951  ASP   A CA  
1076 C C   . ASP   A 145 ? 0.5682 0.6559 0.7729 0.0972  -0.0268 -0.0913 951  ASP   A C   
1077 O O   . ASP   A 145 ? 0.5466 0.6586 0.7640 0.0960  -0.0253 -0.0944 951  ASP   A O   
1078 C CB  . ASP   A 145 ? 0.5285 0.5637 0.6997 0.0910  -0.0471 -0.0545 951  ASP   A CB  
1079 C CG  . ASP   A 145 ? 0.5943 0.5891 0.7397 0.0859  -0.0575 -0.0344 951  ASP   A CG  
1080 O OD1 . ASP   A 145 ? 0.5915 0.5744 0.7200 0.0750  -0.0483 -0.0259 951  ASP   A OD1 
1081 O OD2 . ASP   A 145 ? 0.5840 0.5595 0.7255 0.0918  -0.0752 -0.0274 951  ASP   A OD2 
1082 N N   . ALA   A 146 ? 0.6805 0.7793 0.8929 0.1008  -0.0189 -0.1081 952  ALA   A N   
1083 C CA  . ALA   A 146 ? 0.6756 0.8187 0.9135 0.1041  -0.0076 -0.1321 952  ALA   A CA  
1084 C C   . ALA   A 146 ? 0.6588 0.8161 0.8848 0.0921  0.0128  -0.1401 952  ALA   A C   
1085 O O   . ALA   A 146 ? 0.6670 0.8622 0.9108 0.0922  0.0250  -0.1616 952  ALA   A O   
1086 C CB  . ALA   A 146 ? 0.6353 0.7856 0.9050 0.1280  -0.0234 -0.1542 952  ALA   A CB  
1087 N N   . GLY   A 147 ? 0.5324 0.6625 0.7286 0.0809  0.0168  -0.1243 953  GLY   A N   
1088 C CA  . GLY   A 147 ? 0.5107 0.6498 0.6906 0.0687  0.0335  -0.1296 953  GLY   A CA  
1089 C C   . GLY   A 147 ? 0.4239 0.5842 0.5918 0.0496  0.0498  -0.1241 953  GLY   A C   
1090 O O   . GLY   A 147 ? 0.4897 0.6586 0.6634 0.0456  0.0488  -0.1166 953  GLY   A O   
1091 N N   . GLN   A 148 ? 0.4576 0.6228 0.6054 0.0366  0.0637  -0.1274 954  GLN   A N   
1092 C CA  . GLN   A 148 ? 0.4076 0.5859 0.5374 0.0160  0.0780  -0.1210 954  GLN   A CA  
1093 C C   . GLN   A 148 ? 0.4113 0.5624 0.5212 0.0082  0.0719  -0.0960 954  GLN   A C   
1094 O O   . GLN   A 148 ? 0.3877 0.5090 0.4826 0.0106  0.0639  -0.0833 954  GLN   A O   
1095 C CB  . GLN   A 148 ? 0.4684 0.6502 0.5740 0.0032  0.0913  -0.1278 954  GLN   A CB  
1096 C CG  . GLN   A 148 ? 0.5818 0.8040 0.7041 0.0028  0.1052  -0.1546 954  GLN   A CG  
1097 C CD  . GLN   A 148 ? 0.6367 0.8961 0.7765 -0.0072 0.1155  -0.1611 954  GLN   A CD  
1098 O OE1 . GLN   A 148 ? 0.5709 0.8676 0.7445 0.0018  0.1193  -0.1836 954  GLN   A OE1 
1099 N NE2 . GLN   A 148 ? 0.6516 0.9011 0.7701 -0.0255 0.1187  -0.1425 954  GLN   A NE2 
1100 N N   . ILE   A 149 ? 0.4067 0.5701 0.5181 -0.0014 0.0759  -0.0910 955  ILE   A N   
1101 C CA  . ILE   A 149 ? 0.3447 0.4856 0.4405 -0.0072 0.0701  -0.0708 955  ILE   A CA  
1102 C C   . ILE   A 149 ? 0.3261 0.4494 0.3883 -0.0227 0.0759  -0.0607 955  ILE   A C   
1103 O O   . ILE   A 149 ? 0.3906 0.5265 0.4400 -0.0373 0.0876  -0.0665 955  ILE   A O   
1104 C CB  . ILE   A 149 ? 0.3567 0.5158 0.4663 -0.0116 0.0706  -0.0708 955  ILE   A CB  
1105 C CG1 . ILE   A 149 ? 0.3254 0.4928 0.4645 0.0061  0.0587  -0.0766 955  ILE   A CG1 
1106 C CG2 . ILE   A 149 ? 0.3150 0.4527 0.4024 -0.0222 0.0683  -0.0529 955  ILE   A CG2 
1107 C CD1 . ILE   A 149 ? 0.2721 0.4742 0.4367 0.0046  0.0611  -0.0889 955  ILE   A CD1 
1108 N N   . ILE   A 150 ? 0.3826 0.4772 0.4299 -0.0205 0.0673  -0.0458 956  ILE   A N   
1109 C CA  . ILE   A 150 ? 0.3507 0.4246 0.3673 -0.0318 0.0681  -0.0358 956  ILE   A CA  
1110 C C   . ILE   A 150 ? 0.3713 0.4344 0.3770 -0.0396 0.0655  -0.0240 956  ILE   A C   
1111 O O   . ILE   A 150 ? 0.4055 0.4644 0.3904 -0.0548 0.0704  -0.0213 956  ILE   A O   
1112 C CB  . ILE   A 150 ? 0.3743 0.4268 0.3843 -0.0236 0.0594  -0.0303 956  ILE   A CB  
1113 C CG1 . ILE   A 150 ? 0.3842 0.4447 0.4025 -0.0172 0.0614  -0.0434 956  ILE   A CG1 
1114 C CG2 . ILE   A 150 ? 0.3987 0.4295 0.3790 -0.0328 0.0566  -0.0210 956  ILE   A CG2 
1115 C CD1 . ILE   A 150 ? 0.4101 0.4524 0.4285 -0.0087 0.0519  -0.0399 956  ILE   A CD1 
1116 N N   . LEU   A 151 ? 0.3525 0.4088 0.3693 -0.0304 0.0574  -0.0172 957  LEU   A N   
1117 C CA  . LEU   A 151 ? 0.3916 0.4384 0.3998 -0.0359 0.0544  -0.0087 957  LEU   A CA  
1118 C C   . LEU   A 151 ? 0.3486 0.4051 0.3774 -0.0274 0.0503  -0.0088 957  LEU   A C   
1119 O O   . LEU   A 151 ? 0.3538 0.4156 0.3990 -0.0161 0.0466  -0.0115 957  LEU   A O   
1120 C CB  . LEU   A 151 ? 0.3937 0.4139 0.3841 -0.0341 0.0466  0.0016  957  LEU   A CB  
1121 C CG  . LEU   A 151 ? 0.3932 0.3949 0.3592 -0.0400 0.0445  0.0048  957  LEU   A CG  
1122 C CD1 . LEU   A 151 ? 0.3669 0.3463 0.3227 -0.0352 0.0341  0.0127  957  LEU   A CD1 
1123 C CD2 . LEU   A 151 ? 0.3517 0.3524 0.2971 -0.0572 0.0511  0.0038  957  LEU   A CD2 
1124 N N   . GLN   A 152 ? 0.3495 0.4046 0.3741 -0.0338 0.0494  -0.0053 958  GLN   A N   
1125 C CA  . GLN   A 152 ? 0.3391 0.3999 0.3772 -0.0275 0.0440  -0.0044 958  GLN   A CA  
1126 C C   . GLN   A 152 ? 0.3819 0.4257 0.4041 -0.0327 0.0403  0.0028  958  GLN   A C   
1127 O O   . GLN   A 152 ? 0.3732 0.4056 0.3777 -0.0438 0.0422  0.0050  958  GLN   A O   
1128 C CB  . GLN   A 152 ? 0.3188 0.4064 0.3772 -0.0296 0.0467  -0.0141 958  GLN   A CB  
1129 C CG  . GLN   A 152 ? 0.2794 0.3846 0.3566 -0.0217 0.0489  -0.0244 958  GLN   A CG  
1130 C CD  . GLN   A 152 ? 0.3172 0.4541 0.4184 -0.0230 0.0515  -0.0373 958  GLN   A CD  
1131 O OE1 . GLN   A 152 ? 0.3209 0.4741 0.4206 -0.0376 0.0609  -0.0430 958  GLN   A OE1 
1132 N NE2 . GLN   A 152 ? 0.2598 0.4058 0.3835 -0.0084 0.0422  -0.0426 958  GLN   A NE2 
1133 N N   . GLU   A 153 ? 0.3400 0.3797 0.3658 -0.0250 0.0343  0.0061  959  GLU   A N   
1134 C CA  . GLU   A 153 ? 0.3562 0.3829 0.3695 -0.0288 0.0305  0.0095  959  GLU   A CA  
1135 C C   . GLU   A 153 ? 0.3572 0.3931 0.3797 -0.0257 0.0262  0.0082  959  GLU   A C   
1136 O O   . GLU   A 153 ? 0.3312 0.3711 0.3615 -0.0168 0.0229  0.0094  959  GLU   A O   
1137 C CB  . GLU   A 153 ? 0.3736 0.3813 0.3747 -0.0227 0.0271  0.0140  959  GLU   A CB  
1138 C CG  . GLU   A 153 ? 0.3966 0.3899 0.3854 -0.0242 0.0223  0.0146  959  GLU   A CG  
1139 C CD  . GLU   A 153 ? 0.5409 0.5198 0.5222 -0.0159 0.0186  0.0154  959  GLU   A CD  
1140 O OE1 . GLU   A 153 ? 0.5671 0.5439 0.5494 -0.0123 0.0190  0.0164  959  GLU   A OE1 
1141 O OE2 . GLU   A 153 ? 0.5787 0.5498 0.5543 -0.0126 0.0148  0.0132  959  GLU   A OE2 
1142 N N   . ALA   A 154 ? 0.4011 0.4382 0.4204 -0.0347 0.0250  0.0062  960  ALA   A N   
1143 C CA  . ALA   A 154 ? 0.3329 0.3782 0.3593 -0.0329 0.0192  0.0044  960  ALA   A CA  
1144 C C   . ALA   A 154 ? 0.3594 0.3880 0.3718 -0.0266 0.0145  0.0082  960  ALA   A C   
1145 O O   . ALA   A 154 ? 0.3257 0.3368 0.3236 -0.0271 0.0150  0.0098  960  ALA   A O   
1146 C CB  . ALA   A 154 ? 0.2632 0.3159 0.2910 -0.0463 0.0193  0.0001  960  ALA   A CB  
1147 N N   . VAL   A 155 ? 0.3282 0.3624 0.3444 -0.0205 0.0093  0.0087  961  VAL   A N   
1148 C CA  . VAL   A 155 ? 0.3288 0.3516 0.3304 -0.0163 0.0065  0.0108  961  VAL   A CA  
1149 C C   . VAL   A 155 ? 0.3619 0.3897 0.3625 -0.0174 -0.0014 0.0091  961  VAL   A C   
1150 O O   . VAL   A 155 ? 0.3561 0.3958 0.3691 -0.0150 -0.0068 0.0091  961  VAL   A O   
1151 C CB  . VAL   A 155 ? 0.3728 0.3939 0.3730 -0.0091 0.0088  0.0154  961  VAL   A CB  
1152 C CG1 . VAL   A 155 ? 0.3600 0.3750 0.3449 -0.0073 0.0080  0.0162  961  VAL   A CG1 
1153 C CG2 . VAL   A 155 ? 0.3540 0.3705 0.3554 -0.0081 0.0149  0.0159  961  VAL   A CG2 
1154 N N   . PRO   A 156 ? 0.3672 0.3853 0.3532 -0.0200 -0.0042 0.0066  962  PRO   A N   
1155 C CA  . PRO   A 156 ? 0.3669 0.3889 0.3500 -0.0219 -0.0131 0.0044  962  PRO   A CA  
1156 C C   . PRO   A 156 ? 0.3873 0.4093 0.3625 -0.0158 -0.0177 0.0090  962  PRO   A C   
1157 O O   . PRO   A 156 ? 0.3965 0.4115 0.3598 -0.0126 -0.0123 0.0124  962  PRO   A O   
1158 C CB  . PRO   A 156 ? 0.3473 0.3547 0.3132 -0.0256 -0.0142 -0.0003 962  PRO   A CB  
1159 C CG  . PRO   A 156 ? 0.3424 0.3388 0.3000 -0.0204 -0.0067 0.0001  962  PRO   A CG  
1160 C CD  . PRO   A 156 ? 0.3063 0.3084 0.2779 -0.0198 -0.0010 0.0043  962  PRO   A CD  
1161 N N   . VAL   A 157 ? 0.3803 0.4097 0.3609 -0.0154 -0.0284 0.0089  963  VAL   A N   
1162 C CA  . VAL   A 157 ? 0.4450 0.4676 0.4093 -0.0122 -0.0367 0.0140  963  VAL   A CA  
1163 C C   . VAL   A 157 ? 0.4357 0.4512 0.3792 -0.0165 -0.0408 0.0101  963  VAL   A C   
1164 O O   . VAL   A 157 ? 0.4342 0.4548 0.3844 -0.0206 -0.0468 0.0038  963  VAL   A O   
1165 C CB  . VAL   A 157 ? 0.4060 0.4368 0.3855 -0.0073 -0.0503 0.0155  963  VAL   A CB  
1166 C CG1 . VAL   A 157 ? 0.3460 0.3630 0.3014 -0.0057 -0.0620 0.0226  963  VAL   A CG1 
1167 C CG2 . VAL   A 157 ? 0.3209 0.3576 0.3203 -0.0020 -0.0462 0.0171  963  VAL   A CG2 
1168 N N   . LYS   A 158 ? 0.4416 0.4467 0.3598 -0.0167 -0.0371 0.0126  964  LYS   A N   
1169 C CA  . LYS   A 158 ? 0.4691 0.4675 0.3647 -0.0201 -0.0399 0.0069  964  LYS   A CA  
1170 C C   . LYS   A 158 ? 0.5247 0.5174 0.3991 -0.0214 -0.0520 0.0122  964  LYS   A C   
1171 O O   . LYS   A 158 ? 0.5220 0.5109 0.3914 -0.0201 -0.0551 0.0217  964  LYS   A O   
1172 C CB  . LYS   A 158 ? 0.4526 0.4461 0.3340 -0.0197 -0.0264 0.0020  964  LYS   A CB  
1173 C CG  . LYS   A 158 ? 0.4780 0.4721 0.3785 -0.0175 -0.0188 -0.0026 964  LYS   A CG  
1174 C CD  . LYS   A 158 ? 0.5198 0.5071 0.4099 -0.0147 -0.0113 -0.0123 964  LYS   A CD  
1175 C CE  . LYS   A 158 ? 0.5402 0.5210 0.4450 -0.0130 -0.0094 -0.0157 964  LYS   A CE  
1176 N NZ  . LYS   A 158 ? 0.6032 0.5787 0.5031 -0.0061 -0.0028 -0.0244 964  LYS   A NZ  
1177 N N   . ARG   A 159 ? 0.6418 0.6312 0.5024 -0.0247 -0.0610 0.0062  965  ARG   A N   
1178 C CA  . ARG   A 159 ? 0.6428 0.6244 0.4787 -0.0266 -0.0754 0.0108  965  ARG   A CA  
1179 C C   . ARG   A 159 ? 0.6081 0.5795 0.4126 -0.0298 -0.0678 0.0184  965  ARG   A C   
1180 O O   . ARG   A 159 ? 0.5727 0.5456 0.3668 -0.0319 -0.0514 0.0136  965  ARG   A O   
1181 C CB  . ARG   A 159 ? 0.6604 0.6387 0.4813 -0.0308 -0.0832 0.0011  965  ARG   A CB  
1182 C CG  . ARG   A 159 ? 0.7900 0.7784 0.6368 -0.0311 -0.0978 -0.0041 965  ARG   A CG  
1183 C CD  . ARG   A 159 ? 0.9508 0.9332 0.7757 -0.0347 -0.1153 -0.0079 965  ARG   A CD  
1184 N NE  . ARG   A 159 ? 1.0155 0.9920 0.8273 -0.0401 -0.1117 -0.0198 965  ARG   A NE  
1185 C CZ  . ARG   A 159 ? 1.0302 0.9948 0.8066 -0.0435 -0.1170 -0.0245 965  ARG   A CZ  
1186 N NH1 . ARG   A 159 ? 1.0604 1.0170 0.8074 -0.0439 -0.1258 -0.0167 965  ARG   A NH1 
1187 N NH2 . ARG   A 159 ? 1.0628 1.0207 0.8303 -0.0471 -0.1142 -0.0373 965  ARG   A NH2 
1188 N N   . GLY   A 160 ? 0.5325 0.4937 0.3222 -0.0307 -0.0807 0.0298  966  GLY   A N   
1189 C CA  . GLY   A 160 ? 0.5451 0.4942 0.3016 -0.0376 -0.0744 0.0394  966  GLY   A CA  
1190 C C   . GLY   A 160 ? 0.6216 0.5738 0.3918 -0.0374 -0.0605 0.0453  966  GLY   A C   
1191 O O   . GLY   A 160 ? 0.6160 0.5602 0.3599 -0.0460 -0.0534 0.0531  966  GLY   A O   
1192 N N   . ASP   A 161 ? 0.5156 0.4795 0.3244 -0.0296 -0.0562 0.0415  967  ASP   A N   
1193 C CA  . ASP   A 161 ? 0.5075 0.4732 0.3306 -0.0287 -0.0459 0.0470  967  ASP   A CA  
1194 C C   . ASP   A 161 ? 0.5097 0.4573 0.3161 -0.0319 -0.0568 0.0614  967  ASP   A C   
1195 O O   . ASP   A 161 ? 0.5328 0.4678 0.3316 -0.0293 -0.0769 0.0668  967  ASP   A O   
1196 C CB  . ASP   A 161 ? 0.4562 0.4339 0.3197 -0.0200 -0.0450 0.0419  967  ASP   A CB  
1197 C CG  . ASP   A 161 ? 0.4737 0.4629 0.3508 -0.0193 -0.0282 0.0325  967  ASP   A CG  
1198 O OD1 . ASP   A 161 ? 0.4649 0.4553 0.3269 -0.0232 -0.0158 0.0304  967  ASP   A OD1 
1199 O OD2 . ASP   A 161 ? 0.4657 0.4630 0.3686 -0.0151 -0.0275 0.0272  967  ASP   A OD2 
1200 N N   . THR   A 162 ? 0.4983 0.4428 0.2980 -0.0381 -0.0450 0.0676  968  THR   A N   
1201 C CA  . THR   A 162 ? 0.5207 0.4449 0.3097 -0.0413 -0.0550 0.0815  968  THR   A CA  
1202 C C   . THR   A 162 ? 0.5211 0.4527 0.3395 -0.0373 -0.0455 0.0807  968  THR   A C   
1203 O O   . THR   A 162 ? 0.5187 0.4703 0.3603 -0.0335 -0.0311 0.0706  968  THR   A O   
1204 C CB  . THR   A 162 ? 0.5497 0.4583 0.2935 -0.0582 -0.0510 0.0920  968  THR   A CB  
1205 O OG1 . THR   A 162 ? 0.5525 0.4788 0.2977 -0.0666 -0.0268 0.0871  968  THR   A OG1 
1206 C CG2 . THR   A 162 ? 0.5621 0.4649 0.2730 -0.0633 -0.0581 0.0911  968  THR   A CG2 
1207 N N   . VAL   A 163 ? 0.5219 0.4342 0.3369 -0.0383 -0.0552 0.0914  969  VAL   A N   
1208 C CA  . VAL   A 163 ? 0.5354 0.4525 0.3743 -0.0361 -0.0465 0.0907  969  VAL   A CA  
1209 C C   . VAL   A 163 ? 0.4987 0.4344 0.3378 -0.0449 -0.0231 0.0858  969  VAL   A C   
1210 O O   . VAL   A 163 ? 0.4820 0.4335 0.3489 -0.0392 -0.0131 0.0782  969  VAL   A O   
1211 C CB  . VAL   A 163 ? 0.5653 0.4530 0.3909 -0.0397 -0.0601 0.1039  969  VAL   A CB  
1212 C CG1 . VAL   A 163 ? 0.4613 0.3533 0.3056 -0.0413 -0.0490 0.1032  969  VAL   A CG1 
1213 C CG2 . VAL   A 163 ? 0.5266 0.3998 0.3629 -0.0253 -0.0850 0.1043  969  VAL   A CG2 
1214 N N   . ALA   A 164 ? 0.5411 0.4762 0.3491 -0.0589 -0.0147 0.0891  970  ALA   A N   
1215 C CA  . ALA   A 164 ? 0.5075 0.4653 0.3188 -0.0662 0.0072  0.0814  970  ALA   A CA  
1216 C C   . ALA   A 164 ? 0.4983 0.4788 0.3365 -0.0537 0.0150  0.0657  970  ALA   A C   
1217 O O   . ALA   A 164 ? 0.4607 0.4556 0.3241 -0.0490 0.0245  0.0588  970  ALA   A O   
1218 C CB  . ALA   A 164 ? 0.4866 0.4446 0.2595 -0.0829 0.0155  0.0843  970  ALA   A CB  
1219 N N   . THR   A 165 ? 0.4471 0.4278 0.2782 -0.0488 0.0093  0.0601  971  THR   A N   
1220 C CA  . THR   A 165 ? 0.4413 0.4383 0.2911 -0.0397 0.0161  0.0457  971  THR   A CA  
1221 C C   . THR   A 165 ? 0.4705 0.4680 0.3513 -0.0285 0.0096  0.0434  971  THR   A C   
1222 O O   . THR   A 165 ? 0.4237 0.4316 0.3239 -0.0231 0.0173  0.0351  971  THR   A O   
1223 C CB  . THR   A 165 ? 0.4774 0.4728 0.3068 -0.0404 0.0122  0.0398  971  THR   A CB  
1224 O OG1 . THR   A 165 ? 0.4313 0.4125 0.2563 -0.0376 -0.0061 0.0462  971  THR   A OG1 
1225 C CG2 . THR   A 165 ? 0.4443 0.4412 0.2399 -0.0533 0.0209  0.0410  971  THR   A CG2 
1226 N N   . LEU   A 166 ? 0.4643 0.4510 0.3499 -0.0250 -0.0049 0.0499  972  LEU   A N   
1227 C CA  . LEU   A 166 ? 0.4309 0.4225 0.3459 -0.0163 -0.0085 0.0462  972  LEU   A CA  
1228 C C   . LEU   A 166 ? 0.4235 0.4195 0.3544 -0.0153 0.0006  0.0465  972  LEU   A C   
1229 O O   . LEU   A 166 ? 0.4551 0.4598 0.4033 -0.0111 0.0065  0.0396  972  LEU   A O   
1230 C CB  . LEU   A 166 ? 0.4341 0.4177 0.3551 -0.0116 -0.0254 0.0508  972  LEU   A CB  
1231 C CG  . LEU   A 166 ? 0.3898 0.3852 0.3418 -0.0038 -0.0280 0.0434  972  LEU   A CG  
1232 C CD1 . LEU   A 166 ? 0.3519 0.3585 0.3102 -0.0049 -0.0212 0.0343  972  LEU   A CD1 
1233 C CD2 . LEU   A 166 ? 0.3856 0.3797 0.3474 0.0025  -0.0454 0.0435  972  LEU   A CD2 
1234 N N   . SER   A 167 ? 0.3926 0.3801 0.3155 -0.0204 0.0006  0.0550  973  SER   A N   
1235 C CA  . SER   A 167 ? 0.4299 0.4210 0.3691 -0.0197 0.0072  0.0547  973  SER   A CA  
1236 C C   . SER   A 167 ? 0.4306 0.4365 0.3735 -0.0220 0.0215  0.0478  973  SER   A C   
1237 O O   . SER   A 167 ? 0.4369 0.4485 0.3966 -0.0191 0.0259  0.0446  973  SER   A O   
1238 C CB  . SER   A 167 ? 0.4213 0.3971 0.3507 -0.0261 0.0026  0.0652  973  SER   A CB  
1239 O OG  . SER   A 167 ? 0.4736 0.4435 0.3750 -0.0380 0.0051  0.0717  973  SER   A OG  
1240 N N   . GLU   A 168 ? 0.4723 0.4849 0.3998 -0.0266 0.0280  0.0441  974  GLU   A N   
1241 C CA  . GLU   A 168 ? 0.4155 0.4447 0.3517 -0.0246 0.0395  0.0334  974  GLU   A CA  
1242 C C   . GLU   A 168 ? 0.4785 0.5082 0.4304 -0.0141 0.0365  0.0254  974  GLU   A C   
1243 O O   . GLU   A 168 ? 0.4458 0.4811 0.4134 -0.0094 0.0397  0.0204  974  GLU   A O   
1244 C CB  . GLU   A 168 ? 0.3966 0.4341 0.3131 -0.0304 0.0467  0.0282  974  GLU   A CB  
1245 C CG  . GLU   A 168 ? 0.3916 0.4476 0.3183 -0.0256 0.0569  0.0135  974  GLU   A CG  
1246 C CD  . GLU   A 168 ? 0.4996 0.5692 0.4072 -0.0334 0.0673  0.0068  974  GLU   A CD  
1247 O OE1 . GLU   A 168 ? 0.4410 0.5050 0.3305 -0.0329 0.0643  0.0034  974  GLU   A OE1 
1248 O OE2 . GLU   A 168 ? 0.5900 0.6779 0.5007 -0.0411 0.0790  0.0038  974  GLU   A OE2 
1249 N N   . ARG   A 169 ? 0.4572 0.4793 0.4038 -0.0117 0.0288  0.0249  975  ARG   A N   
1250 C CA  . ARG   A 169 ? 0.4369 0.4569 0.3940 -0.0056 0.0260  0.0185  975  ARG   A CA  
1251 C C   . ARG   A 169 ? 0.4328 0.4510 0.4066 -0.0034 0.0239  0.0215  975  ARG   A C   
1252 O O   . ARG   A 169 ? 0.4194 0.4368 0.4012 -0.0002 0.0255  0.0172  975  ARG   A O   
1253 C CB  . ARG   A 169 ? 0.3859 0.4003 0.3343 -0.0065 0.0184  0.0172  975  ARG   A CB  
1254 C CG  . ARG   A 169 ? 0.3541 0.3637 0.3072 -0.0039 0.0162  0.0099  975  ARG   A CG  
1255 C CD  . ARG   A 169 ? 0.4407 0.4461 0.3854 -0.0068 0.0086  0.0079  975  ARG   A CD  
1256 N NE  . ARG   A 169 ? 0.4156 0.4212 0.3413 -0.0084 0.0086  0.0062  975  ARG   A NE  
1257 C CZ  . ARG   A 169 ? 0.4059 0.4113 0.3214 -0.0118 0.0029  0.0125  975  ARG   A CZ  
1258 N NH1 . ARG   A 169 ? 0.4163 0.4222 0.3429 -0.0117 -0.0044 0.0194  975  ARG   A NH1 
1259 N NH2 . ARG   A 169 ? 0.4431 0.4471 0.3361 -0.0150 0.0037  0.0111  975  ARG   A NH2 
1260 N N   . VAL   A 170 ? 0.4166 0.4326 0.3942 -0.0046 0.0192  0.0283  976  VAL   A N   
1261 C CA  . VAL   A 170 ? 0.4195 0.4359 0.4127 -0.0022 0.0181  0.0287  976  VAL   A CA  
1262 C C   . VAL   A 170 ? 0.4263 0.4444 0.4253 -0.0015 0.0241  0.0282  976  VAL   A C   
1263 O O   . VAL   A 170 ? 0.4062 0.4242 0.4134 0.0004  0.0250  0.0253  976  VAL   A O   
1264 C CB  . VAL   A 170 ? 0.3792 0.3929 0.3770 -0.0011 0.0105  0.0334  976  VAL   A CB  
1265 C CG1 . VAL   A 170 ? 0.3803 0.3970 0.3942 0.0020  0.0110  0.0307  976  VAL   A CG1 
1266 C CG2 . VAL   A 170 ? 0.3565 0.3713 0.3527 -0.0004 0.0023  0.0323  976  VAL   A CG2 
1267 N N   . LYS   A 171 ? 0.3937 0.4143 0.3876 -0.0047 0.0281  0.0306  977  LYS   A N   
1268 C CA  . LYS   A 171 ? 0.3956 0.4208 0.3983 -0.0050 0.0326  0.0295  977  LYS   A CA  
1269 C C   . LYS   A 171 ? 0.4169 0.4466 0.4257 0.0001  0.0348  0.0215  977  LYS   A C   
1270 O O   . LYS   A 171 ? 0.4424 0.4732 0.4605 0.0020  0.0348  0.0199  977  LYS   A O   
1271 C CB  . LYS   A 171 ? 0.4419 0.4725 0.4380 -0.0124 0.0378  0.0327  977  LYS   A CB  
1272 C CG  . LYS   A 171 ? 0.4443 0.4642 0.4363 -0.0184 0.0336  0.0421  977  LYS   A CG  
1273 C CD  . LYS   A 171 ? 0.4058 0.4294 0.3851 -0.0302 0.0395  0.0464  977  LYS   A CD  
1274 C CE  . LYS   A 171 ? 0.5026 0.5067 0.4684 -0.0380 0.0321  0.0582  977  LYS   A CE  
1275 N NZ  . LYS   A 171 ? 0.5715 0.5724 0.5432 -0.0455 0.0333  0.0616  977  LYS   A NZ  
1276 N N   . LEU   A 172 ? 0.4038 0.4336 0.4063 0.0028  0.0349  0.0160  978  LEU   A N   
1277 C CA  . LEU   A 172 ? 0.4156 0.4426 0.4220 0.0091  0.0329  0.0086  978  LEU   A CA  
1278 C C   . LEU   A 172 ? 0.4261 0.4410 0.4332 0.0093  0.0278  0.0112  978  LEU   A C   
1279 O O   . LEU   A 172 ? 0.4474 0.4568 0.4570 0.0127  0.0247  0.0087  978  LEU   A O   
1280 C CB  . LEU   A 172 ? 0.4441 0.4683 0.4416 0.0123  0.0318  0.0016  978  LEU   A CB  
1281 C CG  . LEU   A 172 ? 0.4985 0.5373 0.4930 0.0116  0.0387  -0.0038 978  LEU   A CG  
1282 C CD1 . LEU   A 172 ? 0.4386 0.4719 0.4219 0.0149  0.0366  -0.0116 978  LEU   A CD1 
1283 C CD2 . LEU   A 172 ? 0.4369 0.4916 0.4458 0.0157  0.0431  -0.0114 978  LEU   A CD2 
1284 N N   . ALA   A 173 ? 0.4360 0.4475 0.4400 0.0051  0.0264  0.0154  979  ALA   A N   
1285 C CA  . ALA   A 173 ? 0.3940 0.3995 0.3989 0.0026  0.0244  0.0167  979  ALA   A CA  
1286 C C   . ALA   A 173 ? 0.4042 0.4131 0.4172 0.0029  0.0259  0.0187  979  ALA   A C   
1287 O O   . ALA   A 173 ? 0.4015 0.4047 0.4128 0.0021  0.0249  0.0179  979  ALA   A O   
1288 C CB  . ALA   A 173 ? 0.4081 0.4164 0.4130 -0.0017 0.0233  0.0178  979  ALA   A CB  
1289 N N   . GLU   A 174 ? 0.3993 0.4144 0.4180 0.0031  0.0273  0.0215  980  GLU   A N   
1290 C CA  . GLU   A 174 ? 0.3842 0.3998 0.4100 0.0032  0.0275  0.0226  980  GLU   A CA  
1291 C C   . GLU   A 174 ? 0.3912 0.4066 0.4191 0.0049  0.0275  0.0201  980  GLU   A C   
1292 O O   . GLU   A 174 ? 0.3895 0.4014 0.4187 0.0049  0.0260  0.0191  980  GLU   A O   
1293 C CB  . GLU   A 174 ? 0.3627 0.3795 0.3908 0.0015  0.0271  0.0271  980  GLU   A CB  
1294 C CG  . GLU   A 174 ? 0.3632 0.3779 0.3897 0.0019  0.0232  0.0293  980  GLU   A CG  
1295 C CD  . GLU   A 174 ? 0.4611 0.4696 0.4843 -0.0004 0.0197  0.0355  980  GLU   A CD  
1296 O OE1 . GLU   A 174 ? 0.5196 0.5235 0.5395 0.0008  0.0134  0.0381  980  GLU   A OE1 
1297 O OE2 . GLU   A 174 ? 0.4706 0.4774 0.4936 -0.0042 0.0218  0.0379  980  GLU   A OE2 
1298 N N   . HIS   A 175 ? 0.3565 0.3772 0.3852 0.0068  0.0286  0.0175  981  HIS   A N   
1299 C CA  . HIS   A 175 ? 0.3747 0.3983 0.4094 0.0106  0.0264  0.0128  981  HIS   A CA  
1300 C C   . HIS   A 175 ? 0.4196 0.4296 0.4467 0.0142  0.0198  0.0107  981  HIS   A C   
1301 O O   . HIS   A 175 ? 0.4329 0.4414 0.4635 0.0185  0.0144  0.0071  981  HIS   A O   
1302 C CB  . HIS   A 175 ? 0.3544 0.3916 0.3949 0.0129  0.0297  0.0073  981  HIS   A CB  
1303 C CG  . HIS   A 175 ? 0.3921 0.4406 0.4342 0.0057  0.0366  0.0108  981  HIS   A CG  
1304 N ND1 . HIS   A 175 ? 0.3623 0.4235 0.4030 0.0039  0.0427  0.0070  981  HIS   A ND1 
1305 C CD2 . HIS   A 175 ? 0.3823 0.4281 0.4241 -0.0013 0.0377  0.0179  981  HIS   A CD2 
1306 C CE1 . HIS   A 175 ? 0.3625 0.4277 0.3992 -0.0059 0.0476  0.0132  981  HIS   A CE1 
1307 N NE2 . HIS   A 175 ? 0.3669 0.4209 0.4045 -0.0087 0.0435  0.0202  981  HIS   A NE2 
1308 N N   . LYS   A 176 ? 0.4243 0.4236 0.4398 0.0116  0.0190  0.0128  982  LYS   A N   
1309 C CA  . LYS   A 176 ? 0.4006 0.3825 0.4028 0.0104  0.0130  0.0131  982  LYS   A CA  
1310 C C   . LYS   A 176 ? 0.4139 0.3930 0.4111 0.0039  0.0149  0.0160  982  LYS   A C   
1311 O O   . LYS   A 176 ? 0.4286 0.3988 0.4190 0.0038  0.0102  0.0160  982  LYS   A O   
1312 C CB  . LYS   A 176 ? 0.4495 0.4215 0.4408 0.0078  0.0118  0.0132  982  LYS   A CB  
1313 C CG  . LYS   A 176 ? 0.5393 0.5030 0.5280 0.0155  0.0053  0.0078  982  LYS   A CG  
1314 C CD  . LYS   A 176 ? 0.5357 0.4989 0.5201 0.0142  0.0070  0.0059  982  LYS   A CD  
1315 C CE  . LYS   A 176 ? 0.6996 0.6420 0.6669 0.0059  0.0024  0.0089  982  LYS   A CE  
1316 N NZ  . LYS   A 176 ? 0.7074 0.6483 0.6703 0.0037  0.0025  0.0064  982  LYS   A NZ  
1317 N N   . ILE   A 177 ? 0.4031 0.3909 0.4041 -0.0007 0.0210  0.0171  983  ILE   A N   
1318 C CA  . ILE   A 177 ? 0.3975 0.3861 0.3947 -0.0065 0.0241  0.0165  983  ILE   A CA  
1319 C C   . ILE   A 177 ? 0.3951 0.3888 0.4005 -0.0037 0.0246  0.0148  983  ILE   A C   
1320 O O   . ILE   A 177 ? 0.4139 0.4055 0.4126 -0.0074 0.0258  0.0126  983  ILE   A O   
1321 C CB  . ILE   A 177 ? 0.3661 0.3660 0.3690 -0.0108 0.0293  0.0149  983  ILE   A CB  
1322 C CG1 . ILE   A 177 ? 0.3603 0.3716 0.3793 -0.0050 0.0299  0.0146  983  ILE   A CG1 
1323 C CG2 . ILE   A 177 ? 0.3609 0.3553 0.3553 -0.0156 0.0282  0.0161  983  ILE   A CG2 
1324 C CD1 . ILE   A 177 ? 0.3158 0.3397 0.3447 -0.0061 0.0322  0.0106  983  ILE   A CD1 
1325 N N   . PHE   A 178 ? 0.3943 0.3937 0.4117 0.0011  0.0237  0.0155  984  PHE   A N   
1326 C CA  . PHE   A 178 ? 0.3766 0.3779 0.4007 0.0020  0.0231  0.0139  984  PHE   A CA  
1327 C C   . PHE   A 178 ? 0.3822 0.3770 0.4010 0.0027  0.0179  0.0126  984  PHE   A C   
1328 O O   . PHE   A 178 ? 0.4253 0.4168 0.4404 0.0011  0.0168  0.0100  984  PHE   A O   
1329 C CB  . PHE   A 178 ? 0.3068 0.3137 0.3426 0.0034  0.0235  0.0162  984  PHE   A CB  
1330 C CG  . PHE   A 178 ? 0.3410 0.3459 0.3830 0.0031  0.0220  0.0149  984  PHE   A CG  
1331 C CD1 . PHE   A 178 ? 0.3674 0.3695 0.4070 0.0035  0.0220  0.0098  984  PHE   A CD1 
1332 C CD2 . PHE   A 178 ? 0.3256 0.3302 0.3739 0.0013  0.0209  0.0184  984  PHE   A CD2 
1333 C CE1 . PHE   A 178 ? 0.3432 0.3411 0.3884 0.0046  0.0194  0.0068  984  PHE   A CE1 
1334 C CE2 . PHE   A 178 ? 0.3636 0.3610 0.4158 0.0004  0.0175  0.0175  984  PHE   A CE2 
1335 C CZ  . PHE   A 178 ? 0.3130 0.3065 0.3647 0.0034  0.0161  0.0111  984  PHE   A CZ  
1336 N N   . PRO   A 179 ? 0.4042 0.3971 0.4227 0.0060  0.0133  0.0129  985  PRO   A N   
1337 C CA  . PRO   A 179 ? 0.4101 0.3947 0.4224 0.0080  0.0048  0.0110  985  PRO   A CA  
1338 C C   . PRO   A 179 ? 0.3993 0.3671 0.3886 0.0033  0.0019  0.0125  985  PRO   A C   
1339 O O   . PRO   A 179 ? 0.4649 0.4246 0.4441 0.0016  -0.0033 0.0116  985  PRO   A O   
1340 C CB  . PRO   A 179 ? 0.3792 0.3670 0.3990 0.0149  -0.0003 0.0088  985  PRO   A CB  
1341 C CG  . PRO   A 179 ? 0.3852 0.3881 0.4182 0.0147  0.0077  0.0088  985  PRO   A CG  
1342 C CD  . PRO   A 179 ? 0.3960 0.3966 0.4227 0.0093  0.0145  0.0129  985  PRO   A CD  
1343 N N   . ALA   A 180 ? 0.3991 0.3606 0.3773 -0.0008 0.0050  0.0150  986  ALA   A N   
1344 C CA  . ALA   A 180 ? 0.3956 0.3411 0.3487 -0.0096 0.0037  0.0173  986  ALA   A CA  
1345 C C   . ALA   A 180 ? 0.4099 0.3635 0.3601 -0.0161 0.0116  0.0142  986  ALA   A C   
1346 O O   . ALA   A 180 ? 0.4409 0.3834 0.3712 -0.0218 0.0089  0.0141  986  ALA   A O   
1347 C CB  . ALA   A 180 ? 0.3719 0.3111 0.3155 -0.0154 0.0064  0.0201  986  ALA   A CB  
1348 N N   . ALA   A 181 ? 0.4402 0.4120 0.4088 -0.0146 0.0203  0.0107  987  ALA   A N   
1349 C CA  . ALA   A 181 ? 0.3856 0.3675 0.3565 -0.0176 0.0273  0.0044  987  ALA   A CA  
1350 C C   . ALA   A 181 ? 0.4472 0.4244 0.4163 -0.0149 0.0225  0.0014  987  ALA   A C   
1351 O O   . ALA   A 181 ? 0.4437 0.4186 0.3983 -0.0203 0.0248  -0.0031 987  ALA   A O   
1352 C CB  . ALA   A 181 ? 0.3555 0.3539 0.3493 -0.0126 0.0324  0.0010  987  ALA   A CB  
1353 N N   . LEU   A 182 ? 0.3973 0.3749 0.3809 -0.0077 0.0163  0.0030  988  LEU   A N   
1354 C CA  . LEU   A 182 ? 0.4172 0.3903 0.4001 -0.0063 0.0100  0.0001  988  LEU   A CA  
1355 C C   . LEU   A 182 ? 0.4336 0.3914 0.3911 -0.0105 0.0030  0.0013  988  LEU   A C   
1356 O O   . LEU   A 182 ? 0.4236 0.3765 0.3677 -0.0142 0.0020  -0.0031 988  LEU   A O   
1357 C CB  . LEU   A 182 ? 0.3565 0.3348 0.3588 -0.0009 0.0047  0.0020  988  LEU   A CB  
1358 C CG  . LEU   A 182 ? 0.3835 0.3601 0.3898 -0.0001 -0.0037 -0.0010 988  LEU   A CG  
1359 C CD1 . LEU   A 182 ? 0.3532 0.3281 0.3590 -0.0022 -0.0016 -0.0065 988  LEU   A CD1 
1360 C CD2 . LEU   A 182 ? 0.3209 0.3086 0.3488 0.0023  -0.0064 -0.0001 988  LEU   A CD2 
1361 N N   . GLN   A 183 ? 0.4605 0.4078 0.4081 -0.0103 -0.0029 0.0069  989  GLN   A N   
1362 C CA  . GLN   A 183 ? 0.4600 0.3864 0.3807 -0.0135 -0.0140 0.0097  989  GLN   A CA  
1363 C C   . GLN   A 183 ? 0.5020 0.4192 0.3926 -0.0264 -0.0075 0.0099  989  GLN   A C   
1364 O O   . GLN   A 183 ? 0.5595 0.4619 0.4251 -0.0315 -0.0143 0.0100  989  GLN   A O   
1365 C CB  . GLN   A 183 ? 0.4653 0.3790 0.3827 -0.0087 -0.0238 0.0147  989  GLN   A CB  
1366 C CG  . GLN   A 183 ? 0.5116 0.3952 0.3948 -0.0127 -0.0382 0.0195  989  GLN   A CG  
1367 C CD  . GLN   A 183 ? 0.5639 0.4414 0.4454 -0.0070 -0.0529 0.0168  989  GLN   A CD  
1368 O OE1 . GLN   A 183 ? 0.5736 0.4708 0.4835 0.0007  -0.0531 0.0110  989  GLN   A OE1 
1369 N NE2 . GLN   A 183 ? 0.6085 0.4575 0.4549 -0.0120 -0.0663 0.0214  989  GLN   A NE2 
1370 N N   . LEU   A 184 ? 0.4803 0.4082 0.3726 -0.0329 0.0057  0.0091  990  LEU   A N   
1371 C CA  . LEU   A 184 ? 0.5171 0.4452 0.3856 -0.0470 0.0156  0.0064  990  LEU   A CA  
1372 C C   . LEU   A 184 ? 0.5488 0.4877 0.4184 -0.0470 0.0207  -0.0035 990  LEU   A C   
1373 O O   . LEU   A 184 ? 0.5671 0.4981 0.4074 -0.0578 0.0228  -0.0058 990  LEU   A O   
1374 C CB  . LEU   A 184 ? 0.5128 0.4587 0.3928 -0.0524 0.0291  0.0043  990  LEU   A CB  
1375 C CG  . LEU   A 184 ? 0.5550 0.4872 0.4254 -0.0572 0.0252  0.0131  990  LEU   A CG  
1376 C CD1 . LEU   A 184 ? 0.5058 0.4604 0.3975 -0.0587 0.0365  0.0095  990  LEU   A CD1 
1377 C CD2 . LEU   A 184 ? 0.5335 0.4419 0.3620 -0.0743 0.0228  0.0190  990  LEU   A CD2 
1378 N N   . VAL   A 185 ? 0.5186 0.4738 0.4192 -0.0360 0.0230  -0.0100 991  VAL   A N   
1379 C CA  . VAL   A 185 ? 0.5181 0.4813 0.4216 -0.0346 0.0268  -0.0211 991  VAL   A CA  
1380 C C   . VAL   A 185 ? 0.5319 0.4790 0.4222 -0.0330 0.0140  -0.0203 991  VAL   A C   
1381 O O   . VAL   A 185 ? 0.5792 0.5229 0.4504 -0.0381 0.0151  -0.0274 991  VAL   A O   
1382 C CB  . VAL   A 185 ? 0.4616 0.4410 0.3997 -0.0238 0.0302  -0.0274 991  VAL   A CB  
1383 C CG1 . VAL   A 185 ? 0.4156 0.3963 0.3567 -0.0202 0.0294  -0.0390 991  VAL   A CG1 
1384 C CG2 . VAL   A 185 ? 0.3907 0.3880 0.3412 -0.0249 0.0414  -0.0312 991  VAL   A CG2 
1385 N N   . ALA   A 186 ? 0.5590 0.4984 0.4603 -0.0259 0.0016  -0.0132 992  ALA   A N   
1386 C CA  . ALA   A 186 ? 0.5063 0.4341 0.4002 -0.0237 -0.0124 -0.0137 992  ALA   A CA  
1387 C C   . ALA   A 186 ? 0.5571 0.4634 0.4116 -0.0319 -0.0207 -0.0095 992  ALA   A C   
1388 O O   . ALA   A 186 ? 0.6230 0.5191 0.4633 -0.0325 -0.0310 -0.0123 992  ALA   A O   
1389 C CB  . ALA   A 186 ? 0.4540 0.3845 0.3728 -0.0145 -0.0230 -0.0094 992  ALA   A CB  
1390 N N   . SER   A 187 ? 0.5703 0.4666 0.4041 -0.0394 -0.0178 -0.0023 993  SER   A N   
1391 C CA  . SER   A 187 ? 0.5776 0.4470 0.3674 -0.0496 -0.0274 0.0037  993  SER   A CA  
1392 C C   . SER   A 187 ? 0.6849 0.5554 0.4435 -0.0655 -0.0137 -0.0014 993  SER   A C   
1393 O O   . SER   A 187 ? 0.6693 0.5161 0.3840 -0.0782 -0.0198 0.0041  993  SER   A O   
1394 C CB  . SER   A 187 ? 0.5752 0.4260 0.3531 -0.0513 -0.0346 0.0149  993  SER   A CB  
1395 O OG  . SER   A 187 ? 0.6048 0.4697 0.3933 -0.0564 -0.0186 0.0154  993  SER   A OG  
1396 N N   . GLY   A 188 ? 0.6499 0.5473 0.4289 -0.0654 0.0039  -0.0126 994  GLY   A N   
1397 C CA  . GLY   A 188 ? 0.6112 0.5164 0.3645 -0.0804 0.0193  -0.0204 994  GLY   A CA  
1398 C C   . GLY   A 188 ? 0.6549 0.5608 0.3900 -0.0961 0.0305  -0.0147 994  GLY   A C   
1399 O O   . GLY   A 188 ? 0.8012 0.7118 0.5074 -0.1132 0.0431  -0.0199 994  GLY   A O   
1400 N N   . THR   A 189 ? 0.6633 0.5654 0.4134 -0.0925 0.0270  -0.0051 995  THR   A N   
1401 C CA  . THR   A 189 ? 0.6671 0.5717 0.4042 -0.1083 0.0380  -0.0007 995  THR   A CA  
1402 C C   . THR   A 189 ? 0.6584 0.6025 0.4257 -0.1090 0.0586  -0.0141 995  THR   A C   
1403 O O   . THR   A 189 ? 0.7241 0.6801 0.4770 -0.1269 0.0729  -0.0169 995  THR   A O   
1404 C CB  . THR   A 189 ? 0.6660 0.5536 0.4113 -0.1025 0.0263  0.0118  995  THR   A CB  
1405 O OG1 . THR   A 189 ? 0.6956 0.5503 0.4225 -0.0960 0.0045  0.0209  995  THR   A OG1 
1406 C CG2 . THR   A 189 ? 0.6547 0.5358 0.3778 -0.1221 0.0340  0.0182  995  THR   A CG2 
1407 N N   . VAL   A 190 ? 0.6284 0.5924 0.4377 -0.0903 0.0590  -0.0223 996  VAL   A N   
1408 C CA  . VAL   A 190 ? 0.6018 0.6009 0.4447 -0.0856 0.0735  -0.0360 996  VAL   A CA  
1409 C C   . VAL   A 190 ? 0.6477 0.6578 0.5048 -0.0742 0.0745  -0.0503 996  VAL   A C   
1410 O O   . VAL   A 190 ? 0.6531 0.6468 0.5126 -0.0637 0.0615  -0.0470 996  VAL   A O   
1411 C CB  . VAL   A 190 ? 0.5861 0.5926 0.4642 -0.0731 0.0697  -0.0312 996  VAL   A CB  
1412 C CG1 . VAL   A 190 ? 0.5875 0.6248 0.5032 -0.0619 0.0779  -0.0458 996  VAL   A CG1 
1413 C CG2 . VAL   A 190 ? 0.5959 0.5970 0.4624 -0.0859 0.0718  -0.0214 996  VAL   A CG2 
1414 N N   . GLN   A 191 ? 0.6312 0.6697 0.4977 -0.0768 0.0895  -0.0676 997  GLN   A N   
1415 C CA  . GLN   A 191 ? 0.6102 0.6602 0.4951 -0.0636 0.0902  -0.0844 997  GLN   A CA  
1416 C C   . GLN   A 191 ? 0.6647 0.7511 0.5821 -0.0584 0.1032  -0.1019 997  GLN   A C   
1417 O O   . GLN   A 191 ? 0.7167 0.8208 0.6406 -0.0669 0.1122  -0.1008 997  GLN   A O   
1418 C CB  . GLN   A 191 ? 0.5497 0.5917 0.4002 -0.0727 0.0927  -0.0922 997  GLN   A CB  
1419 C CG  . GLN   A 191 ? 0.6820 0.7418 0.5060 -0.0935 0.1109  -0.1003 997  GLN   A CG  
1420 C CD  . GLN   A 191 ? 0.7169 0.7776 0.5126 -0.1003 0.1168  -0.1145 997  GLN   A CD  
1421 O OE1 . GLN   A 191 ? 0.7341 0.7665 0.5051 -0.0995 0.1036  -0.1080 997  GLN   A OE1 
1422 N NE2 . GLN   A 191 ? 0.7535 0.8492 0.5533 -0.1071 0.1366  -0.1357 997  GLN   A NE2 
1423 N N   . LEU   A 192 ? 0.6632 0.7599 0.6025 -0.0435 0.1024  -0.1189 998  LEU   A N   
1424 C CA  . LEU   A 192 ? 0.6434 0.7753 0.6151 -0.0350 0.1124  -0.1404 998  LEU   A CA  
1425 C C   . LEU   A 192 ? 0.7229 0.8770 0.6759 -0.0466 0.1291  -0.1605 998  LEU   A C   
1426 O O   . LEU   A 192 ? 0.7834 0.9248 0.7178 -0.0452 0.1268  -0.1677 998  LEU   A O   
1427 C CB  . LEU   A 192 ? 0.6033 0.7278 0.6067 -0.0114 0.0990  -0.1477 998  LEU   A CB  
1428 C CG  . LEU   A 192 ? 0.5606 0.7069 0.6057 0.0039  0.0973  -0.1577 998  LEU   A CG  
1429 C CD1 . LEU   A 192 ? 0.5669 0.7071 0.6175 0.0004  0.0925  -0.1373 998  LEU   A CD1 
1430 C CD2 . LEU   A 192 ? 0.4804 0.6093 0.5459 0.0246  0.0818  -0.1640 998  LEU   A CD2 
1431 N N   . GLY   A 193 ? 0.7976 0.9850 0.7529 -0.0602 0.1465  -0.1694 999  GLY   A N   
1432 C CA  . GLY   A 193 ? 0.7798 0.9906 0.7122 -0.0761 0.1654  -0.1876 999  GLY   A CA  
1433 C C   . GLY   A 193 ? 0.8451 1.0816 0.8037 -0.0586 0.1701  -0.2187 999  GLY   A C   
1434 O O   . GLY   A 193 ? 0.8767 1.1135 0.8739 -0.0338 0.1581  -0.2267 999  GLY   A O   
1435 N N   . GLU   A 194 ? 0.9259 1.1787 0.8621 -0.0718 0.1840  -0.2332 1000 GLU   A N   
1436 C CA  . GLU   A 194 ? 0.9220 1.1982 0.8857 -0.0556 0.1854  -0.2598 1000 GLU   A CA  
1437 C C   . GLU   A 194 ? 0.9798 1.2923 0.9984 -0.0408 0.1852  -0.2732 1000 GLU   A C   
1438 O O   . GLU   A 194 ? 0.9256 1.2461 0.9784 -0.0166 0.1767  -0.2920 1000 GLU   A O   
1439 C CB  . GLU   A 194 ? 0.8292 1.1174 0.7615 -0.0754 0.1989  -0.2674 1000 GLU   A CB  
1440 N N   . ASN   A 195 ? 1.1138 1.4453 1.1399 -0.0552 0.1921  -0.2636 1001 ASN   A N   
1441 C CA  . ASN   A 195 ? 1.0664 1.4310 1.1421 -0.0431 0.1898  -0.2745 1001 ASN   A CA  
1442 C C   . ASN   A 195 ? 1.0696 1.4181 1.1725 -0.0226 0.1739  -0.2653 1001 ASN   A C   
1443 O O   . ASN   A 195 ? 1.0446 1.4157 1.1863 -0.0121 0.1687  -0.2714 1001 ASN   A O   
1444 C CB  . ASN   A 195 ? 1.0893 1.4792 1.1600 -0.0689 0.2027  -0.2685 1001 ASN   A CB  
1445 C CG  . ASN   A 195 ? 1.1162 1.4799 1.1603 -0.0855 0.2015  -0.2403 1001 ASN   A CG  
1446 O OD1 . ASN   A 195 ? 1.1169 1.4442 1.1378 -0.0820 0.1939  -0.2251 1001 ASN   A OD1 
1447 N ND2 . ASN   A 195 ? 1.1813 1.5628 1.2287 -0.1036 0.2079  -0.2342 1001 ASN   A ND2 
1448 N N   . GLY   A 196 ? 0.9516 1.2621 1.0340 -0.0179 0.1656  -0.2509 1002 GLY   A N   
1449 C CA  . GLY   A 196 ? 0.8526 1.1412 0.9577 0.0006  0.1474  -0.2386 1002 GLY   A CA  
1450 C C   . GLY   A 196 ? 0.8468 1.1332 0.9530 -0.0103 0.1456  -0.2163 1002 GLY   A C   
1451 O O   . GLY   A 196 ? 0.7453 1.0089 0.8661 0.0030  0.1281  -0.2015 1002 GLY   A O   
1452 N N   . LYS   A 197 ? 0.9349 1.2432 1.0247 -0.0352 0.1628  -0.2139 1003 LYS   A N   
1453 C CA  . LYS   A 197 ? 0.9265 1.2230 1.0090 -0.0475 0.1593  -0.1903 1003 LYS   A CA  
1454 C C   . LYS   A 197 ? 0.8823 1.1298 0.9191 -0.0591 0.1516  -0.1627 1003 LYS   A C   
1455 O O   . LYS   A 197 ? 0.8832 1.1103 0.8934 -0.0603 0.1504  -0.1623 1003 LYS   A O   
1456 C CB  . LYS   A 197 ? 0.8616 1.1954 0.9461 -0.0699 0.1763  -0.1968 1003 LYS   A CB  
1457 N N   . ILE   A 198 ? 0.7459 0.9750 0.7752 -0.0663 0.1447  -0.1409 1004 ILE   A N   
1458 C CA  . ILE   A 198 ? 0.7066 0.8903 0.6997 -0.0728 0.1341  -0.1163 1004 ILE   A CA  
1459 C C   . ILE   A 198 ? 0.7113 0.8889 0.6596 -0.0993 0.1459  -0.1124 1004 ILE   A C   
1460 O O   . ILE   A 198 ? 0.7443 0.9461 0.6871 -0.1190 0.1606  -0.1175 1004 ILE   A O   
1461 C CB  . ILE   A 198 ? 0.6245 0.7927 0.6240 -0.0717 0.1238  -0.0976 1004 ILE   A CB  
1462 C CG1 . ILE   A 198 ? 0.6014 0.7278 0.5841 -0.0642 0.1077  -0.0784 1004 ILE   A CG1 
1463 C CG2 . ILE   A 198 ? 0.6568 0.8258 0.6322 -0.0968 0.1326  -0.0889 1004 ILE   A CG2 
1464 C CD1 . ILE   A 198 ? 0.5662 0.6868 0.5722 -0.0417 0.0970  -0.0830 1004 ILE   A CD1 
1465 N N   . CYS   A 199 ? 0.6990 0.8444 0.6136 -0.1013 0.1389  -0.1036 1005 CYS   A N   
1466 C CA  . CYS   A 199 ? 0.7214 0.8563 0.5879 -0.1256 0.1475  -0.1006 1005 CYS   A CA  
1467 C C   . CYS   A 199 ? 0.7276 0.8155 0.5578 -0.1334 0.1323  -0.0747 1005 CYS   A C   
1468 O O   . CYS   A 199 ? 0.6951 0.7552 0.5213 -0.1196 0.1163  -0.0665 1005 CYS   A O   
1469 C CB  . CYS   A 199 ? 0.7000 0.8376 0.5550 -0.1209 0.1509  -0.1159 1005 CYS   A CB  
1470 S SG  . CYS   A 199 ? 0.8054 0.9491 0.6072 -0.1519 0.1691  -0.1229 1005 CYS   A SG  
1471 N N   . TRP   A 200 ? 0.7404 0.8195 0.5455 -0.1554 0.1362  -0.0630 1006 TRP   A N   
1472 C CA  . TRP   A 200 ? 0.7831 0.8146 0.5495 -0.1637 0.1204  -0.0402 1006 TRP   A CA  
1473 C C   . TRP   A 200 ? 0.8650 0.8725 0.5767 -0.1823 0.1206  -0.0362 1006 TRP   A C   
1474 O O   . TRP   A 200 ? 0.8907 0.9188 0.5826 -0.2026 0.1387  -0.0467 1006 TRP   A O   
1475 C CB  . TRP   A 200 ? 0.7994 0.8246 0.5598 -0.1791 0.1214  -0.0288 1006 TRP   A CB  
1476 C CG  . TRP   A 200 ? 0.8553 0.8883 0.6589 -0.1596 0.1138  -0.0268 1006 TRP   A CG  
1477 C CD1 . TRP   A 200 ? 0.8110 0.8841 0.6601 -0.1498 0.1229  -0.0405 1006 TRP   A CD1 
1478 C CD2 . TRP   A 200 ? 0.8420 0.8422 0.6466 -0.1469 0.0948  -0.0114 1006 TRP   A CD2 
1479 N NE1 . TRP   A 200 ? 0.7680 0.8326 0.6418 -0.1336 0.1107  -0.0328 1006 TRP   A NE1 
1480 C CE2 . TRP   A 200 ? 0.8380 0.8602 0.6860 -0.1318 0.0948  -0.0158 1006 TRP   A CE2 
1481 C CE3 . TRP   A 200 ? 0.8001 0.7557 0.5738 -0.1461 0.0769  0.0043  1006 TRP   A CE3 
1482 C CZ2 . TRP   A 200 ? 0.8248 0.8272 0.6839 -0.1179 0.0802  -0.0053 1006 TRP   A CZ2 
1483 C CZ3 . TRP   A 200 ? 0.7484 0.6870 0.5381 -0.1303 0.0622  0.0128  1006 TRP   A CZ3 
1484 C CH2 . TRP   A 200 ? 0.7712 0.7341 0.6021 -0.1173 0.0652  0.0079  1006 TRP   A CH2 
1485 N N   . VAL   A 201 ? 0.9146 0.8795 0.6012 -0.1758 0.0999  -0.0216 1007 VAL   A N   
1486 C CA  . VAL   A 201 ? 0.9635 0.9013 0.5962 -0.1912 0.0957  -0.0170 1007 VAL   A CA  
1487 C C   . VAL   A 201 ? 1.0201 0.9045 0.6150 -0.1963 0.0728  0.0059  1007 VAL   A C   
1488 O O   . VAL   A 201 ? 1.1066 0.9648 0.6521 -0.2216 0.0723  0.0171  1007 VAL   A O   
1489 C CB  . VAL   A 201 ? 0.8658 0.8073 0.5070 -0.1741 0.0905  -0.0280 1007 VAL   A CB  
1490 C CG1 . VAL   A 201 ? 0.8717 0.7869 0.4539 -0.1916 0.0868  -0.0247 1007 VAL   A CG1 
1491 C CG2 . VAL   A 201 ? 0.7713 0.7609 0.4605 -0.1605 0.1073  -0.0512 1007 VAL   A CG2 
1492 C C1  . GAR   B .   ? 0.5231 0.4979 0.5303 -0.0153 0.0089  0.0545  1101 GAR   A C1  
1493 O O6  . GAR   B .   ? 0.6018 0.5821 0.5990 -0.0158 0.0104  0.0557  1101 GAR   A O6  
1494 C C2  . GAR   B .   ? 0.5486 0.5169 0.5670 -0.0044 0.0001  0.0497  1101 GAR   A C2  
1495 O O8  . GAR   B .   ? 0.5875 0.5670 0.6117 0.0026  0.0001  0.0441  1101 GAR   A O8  
1496 C C3  . GAR   B .   ? 0.5374 0.4819 0.5452 -0.0061 -0.0125 0.0576  1101 GAR   A C3  
1497 O O4  . GAR   B .   ? 0.5914 0.5277 0.5844 -0.0202 -0.0089 0.0665  1101 GAR   A O4  
1498 C C5  . GAR   B .   ? 0.5308 0.4887 0.5242 -0.0267 0.0052  0.0643  1101 GAR   A C5  
1499 C C10 . GAR   B .   ? 0.5352 0.4988 0.5336 -0.0360 0.0122  0.0639  1101 GAR   A C10 
1500 O O12 . GAR   B .   ? 0.5001 0.4845 0.4960 -0.0426 0.0240  0.0620  1101 GAR   A O12 
1501 N N19 . GAR   B .   ? 0.7118 0.6424 0.7293 0.0019  -0.0229 0.0538  1101 GAR   A N19 
1502 C C21 . GAR   B .   ? 0.7358 0.6529 0.7531 0.0104  -0.0374 0.0540  1101 GAR   A C21 
1503 O O22 . GAR   B .   ? 0.6570 0.5687 0.6622 0.0095  -0.0438 0.0602  1101 GAR   A O22 
1504 C C23 . GAR   B .   ? 0.6586 0.5682 0.6925 0.0225  -0.0465 0.0441  1101 GAR   A C23 
1505 N N24 . GAR   B .   ? 0.7133 0.6134 0.7535 0.0354  -0.0633 0.0404  1101 GAR   A N24 
1506 P P15 . GAR   B .   ? 0.4845 0.4884 0.4932 -0.0497 0.0336  0.0566  1101 GAR   A P15 
1507 O O16 . GAR   B .   ? 0.4158 0.4416 0.4206 -0.0550 0.0447  0.0531  1101 GAR   A O16 
1508 O O17 . GAR   B .   ? 0.4190 0.4290 0.4456 -0.0365 0.0316  0.0476  1101 GAR   A O17 
1509 O O18 . GAR   B .   ? 0.4926 0.4802 0.4942 -0.0633 0.0297  0.0648  1101 GAR   A O18 
1523 C C12 . A1B62 C .   ? 0.7657 0.5281 0.7827 0.0476  -0.1282 0.0473  1102 A1B62 A C12 
1524 C C13 . A1B62 C .   ? 0.7997 0.5272 0.8114 0.0601  -0.1553 0.0485  1102 A1B62 A C13 
1525 C C15 . A1B62 C .   ? 0.7184 0.5320 0.7690 0.0712  -0.1265 0.0292  1102 A1B62 A C15 
1526 C C16 . A1B62 C .   ? 0.7280 0.5351 0.7649 0.0544  -0.1134 0.0371  1102 A1B62 A C16 
1527 C C21 . A1B62 C .   ? 0.9639 0.5432 0.8762 -0.0063 -0.1822 0.1019  1102 A1B62 A C21 
1528 C C22 . A1B62 C .   ? 1.0438 0.6208 0.9264 -0.0226 -0.1796 0.1210  1102 A1B62 A C22 
1529 C C17 . A1B62 C .   ? 0.8364 0.5058 0.8242 0.0559  -0.1789 0.0593  1102 A1B62 A C17 
1530 C C23 . A1B62 C .   ? 1.1471 0.7084 0.9977 -0.0572 -0.1696 0.1398  1102 A1B62 A C23 
1531 N N11 . A1B62 C .   ? 0.5713 0.4498 0.7261 0.1271  -0.0949 -0.0970 1102 A1B62 A N11 
1532 C C20 . A1B62 C .   ? 0.8908 0.4810 0.8337 0.0269  -0.1947 0.0815  1102 A1B62 A C20 
1533 C C02 . A1B62 C .   ? 0.5637 0.4539 0.7052 0.1101  -0.0830 -0.0762 1102 A1B62 A C02 
1534 C C04 . A1B62 C .   ? 0.5882 0.5268 0.7279 0.0947  -0.0584 -0.0633 1102 A1B62 A C04 
1535 C C05 . A1B62 C .   ? 0.5274 0.4445 0.6305 0.0663  -0.0530 -0.0236 1102 A1B62 A C05 
1536 C C06 . A1B62 C .   ? 0.5312 0.4215 0.6151 0.0537  -0.0575 -0.0066 1102 A1B62 A C06 
1537 C C08 . A1B62 C .   ? 0.5571 0.4678 0.6745 0.0811  -0.0623 -0.0415 1102 A1B62 A C08 
1538 C C09 . A1B62 C .   ? 0.5671 0.4403 0.6747 0.0806  -0.0763 -0.0372 1102 A1B62 A C09 
1539 C C26 . A1B62 C .   ? 0.8957 0.4757 0.8583 0.0394  -0.2008 0.0642  1102 A1B62 A C26 
1540 C C29 . A1B62 C .   ? 0.5802 0.4737 0.6484 0.0378  -0.0490 0.0106  1102 A1B62 A C29 
1541 C C30 . A1B62 C .   ? 0.6053 0.4938 0.6671 0.0391  -0.0566 0.0197  1102 A1B62 A C30 
1542 C C31 . A1B62 C .   ? 0.6219 0.4781 0.6810 0.0482  -0.0785 0.0207  1102 A1B62 A C31 
1543 C C32 . A1B62 C .   ? 0.6790 0.5213 0.7209 0.0436  -0.0875 0.0353  1102 A1B62 A C32 
1544 F F33 . A1B62 C .   ? 0.7943 0.5485 0.7991 0.0300  -0.1183 0.0548  1102 A1B62 A F33 
1545 N N01 . A1B62 C .   ? 0.5856 0.4469 0.7046 0.0952  -0.0874 -0.0542 1102 A1B62 A N01 
1546 N N03 . A1B62 C .   ? 0.5736 0.5037 0.7258 0.1092  -0.0681 -0.0809 1102 A1B62 A N03 
1547 N N19 . A1B62 C .   ? 0.8923 0.5410 0.8604 0.0341  -0.1720 0.0704  1102 A1B62 A N19 
1548 O O10 . A1B62 C .   ? 0.5608 0.5307 0.7080 0.0924  -0.0463 -0.0667 1102 A1B62 A O10 
1549 O O18 . A1B62 C .   ? 0.8425 0.4830 0.8283 0.0702  -0.2041 0.0581  1102 A1B62 A O18 
1550 O O24 . A1B62 C .   ? 1.1877 0.7319 1.0041 -0.0740 -0.1733 0.1554  1102 A1B62 A O24 
1551 O O25 . A1B62 C .   ? 1.2025 0.7791 1.0642 -0.0687 -0.1546 0.1355  1102 A1B62 A O25 
1552 O O27 . A1B62 C .   ? 0.9160 0.4540 0.8633 0.0373  -0.2196 0.0668  1102 A1B62 A O27 
1553 O O28 . A1B62 C .   ? 0.8530 0.4748 0.8450 0.0493  -0.1835 0.0456  1102 A1B62 A O28 
1554 S S07 . A1B62 C .   ? 0.5976 0.4520 0.6799 0.0592  -0.0741 -0.0114 1102 A1B62 A S07 
1555 S S14 . A1B62 C .   ? 0.8419 0.6023 0.8789 0.0800  -0.1587 0.0350  1102 A1B62 A S14 
1556 O O   . HOH   D .   ? 0.5361 0.4955 0.4936 -0.0860 0.0262  0.0845  1201 HOH   A O   
1557 O O   . HOH   D .   ? 0.5326 0.4352 0.4430 -0.0229 -0.0823 -0.0665 1202 HOH   A O   
1558 O O   . HOH   D .   ? 0.4486 0.7044 0.5614 -0.1322 0.1225  -0.0084 1203 HOH   A O   
1559 O O   . HOH   D .   ? 0.4208 0.3917 0.4263 0.0137  -0.0179 0.0057  1204 HOH   A O   
1560 O O   . HOH   D .   ? 0.5342 0.5354 0.4511 -0.1033 0.0529  0.0820  1205 HOH   A O   
1561 O O   . HOH   D .   ? 0.4947 0.6278 0.7047 -0.2160 0.0099  -0.0003 1206 HOH   A O   
1562 O O   . HOH   D .   ? 0.3341 0.4254 0.4438 0.0229  -0.0262 -0.0080 1207 HOH   A O   
1563 O O   . HOH   D .   ? 0.5057 0.4830 0.6046 0.0669  -0.0040 -0.1122 1208 HOH   A O   
1564 O O   . HOH   D .   ? 0.5409 0.5005 0.5083 -0.0187 -0.0045 0.0672  1209 HOH   A O   
1565 O O   . HOH   D .   ? 0.5382 0.5111 0.5483 0.0416  0.0158  -0.1652 1210 HOH   A O   
1566 O O   . HOH   D .   ? 0.5183 0.4681 0.5217 -0.0742 0.0146  0.0713  1211 HOH   A O   
1567 O O   . HOH   D .   ? 0.5273 0.4765 0.6119 0.0503  -0.0442 0.0078  1212 HOH   A O   
1568 O O   . HOH   D .   ? 0.6962 0.6396 0.6735 -0.3086 0.0400  0.1090  1213 HOH   A O   
1569 O O   . HOH   D .   ? 0.4812 0.5047 0.5712 0.0303  -0.0924 -0.0332 1214 HOH   A O   
1570 O O   . HOH   D .   ? 0.4587 0.5663 0.5426 -0.0020 0.0487  -0.0064 1215 HOH   A O   
1571 O O   . HOH   D .   ? 0.3459 0.4102 0.4733 0.0096  -0.0507 -0.0291 1216 HOH   A O   
1572 O O   . HOH   D .   ? 0.4085 0.4167 0.3947 -0.0584 0.0282  0.0094  1217 HOH   A O   
1573 O O   . HOH   D .   ? 0.4360 0.4568 0.4572 0.0270  0.0225  -0.0079 1218 HOH   A O   
1574 O O   . HOH   D .   ? 0.5297 0.5711 0.7048 0.0960  -0.0187 -0.1025 1219 HOH   A O   
1575 O O   . HOH   D .   ? 0.4568 0.5371 0.6467 -0.0724 -0.0701 -0.0473 1220 HOH   A O   
1576 O O   . HOH   D .   ? 0.3837 0.4497 0.4268 0.0210  0.0389  -0.0126 1221 HOH   A O   
1577 O O   . HOH   D .   ? 0.4884 0.4147 0.5351 0.0071  -0.0194 0.0330  1222 HOH   A O   
1578 O O   . HOH   D .   ? 0.4148 0.4272 0.4419 0.0181  -0.0368 0.0320  1223 HOH   A O   
1579 O O   . HOH   D .   ? 0.6153 0.5315 0.6424 0.0363  -0.0717 0.0479  1224 HOH   A O   
1580 O O   . HOH   D .   ? 0.5259 0.5011 0.5040 0.0111  0.0129  0.0004  1225 HOH   A O   
1581 O O   . HOH   D .   ? 0.4143 0.4440 0.3067 -0.0214 0.0372  0.0121  1226 HOH   A O   
1582 O O   . HOH   D .   ? 0.4772 0.4916 0.5510 0.0438  0.0226  -0.1018 1227 HOH   A O   
1583 O O   . HOH   D .   ? 0.6191 0.7188 0.5732 -0.0996 0.1032  -0.0408 1228 HOH   A O   
1584 O O   . HOH   D .   ? 0.4274 0.4553 0.4931 0.0386  -0.0073 -0.0128 1229 HOH   A O   
1585 O O   . HOH   D .   ? 0.4728 0.5022 0.4723 0.0153  -0.1048 0.0210  1230 HOH   A O   
1586 O O   . HOH   D .   ? 0.6403 0.5399 0.5831 -0.0240 -0.0777 -0.0821 1231 HOH   A O   
1587 O O   . HOH   D .   ? 0.6122 0.5913 0.7186 0.1358  -0.1227 -0.0746 1232 HOH   A O   
1588 O O   . HOH   D .   ? 0.5591 0.5651 0.4847 -0.1903 0.0709  0.0988  1233 HOH   A O   
1589 O O   . HOH   D .   ? 0.5607 0.5472 0.4318 -0.0300 -0.0560 -0.0146 1234 HOH   A O   
1590 O O   . HOH   D .   ? 0.3018 0.4551 0.5647 0.1140  -0.1163 -0.0758 1235 HOH   A O   
1591 O O   . HOH   D .   ? 0.4885 0.5098 0.4526 -0.0360 -0.0419 -0.0095 1236 HOH   A O   
1592 O O   . HOH   D .   ? 0.5263 0.5294 0.4365 -0.0008 0.0176  -0.0165 1237 HOH   A O   
1593 O O   . HOH   D .   ? 0.5532 0.5454 0.5375 -0.0104 0.0092  0.0514  1238 HOH   A O   
1594 O O   . HOH   D .   ? 0.4842 0.6955 0.5613 -0.0568 0.1142  -0.0983 1239 HOH   A O   
1595 O O   . HOH   D .   ? 0.4922 0.5571 0.4781 -0.0145 0.0562  0.0131  1240 HOH   A O   
1596 O O   . HOH   D .   ? 0.3715 0.3965 0.4219 0.0026  0.0250  0.0174  1241 HOH   A O   
1597 O O   . HOH   D .   ? 0.8918 0.7909 0.9825 0.0745  -0.0877 0.0045  1242 HOH   A O   
1598 O O   . HOH   D .   ? 0.5363 0.4323 0.4952 -0.0715 -0.0069 0.0911  1243 HOH   A O   
1599 O O   . HOH   D .   ? 0.4862 0.5337 0.3956 -0.1804 0.0908  0.0870  1244 HOH   A O   
1600 O O   . HOH   D .   ? 0.4675 0.6058 0.6011 0.0500  0.0597  -0.1489 1245 HOH   A O   
1601 O O   . HOH   D .   ? 1.0690 0.5479 1.1045 0.1260  -0.2736 -0.0739 1246 HOH   A O   
1602 O O   . HOH   D .   ? 0.4534 0.4845 0.3055 -0.0751 0.0599  0.0526  1247 HOH   A O   
1603 O O   . HOH   D .   ? 0.7007 0.6304 0.8963 0.1873  -0.0736 -0.2704 1248 HOH   A O   
1604 O O   . HOH   D .   ? 0.5882 0.5708 0.7031 0.1167  -0.2202 0.0021  1249 HOH   A O   
1605 O O   . HOH   D .   ? 0.5377 0.4330 0.5278 0.0242  -0.0269 -0.1396 1250 HOH   A O   
1606 O O   . HOH   D .   ? 0.6585 0.6933 0.5915 -0.0031 0.0395  -0.0052 1251 HOH   A O   
1607 O O   . HOH   D .   ? 0.7685 0.5278 0.6541 -0.0990 -0.0596 0.1298  1252 HOH   A O   
1608 O O   . HOH   D .   ? 0.5645 0.7505 0.5706 -0.1109 0.1288  -0.0741 1253 HOH   A O   
# 
