data_9DON
# 
_entry.id   9DON 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9DON         pdb_00009don 10.2210/pdb9don/pdb 
WWPDB D_1000288556 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DON 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-19 
_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 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jass@umich.edu 
_pdbx_contact_author.name_first         Jeanne 
_pdbx_contact_author.name_last          Stuckey 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4192-8900 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Meagher, J.L.' 1 0000-0003-1250-4575 
'Stuckey, J.A.' 2 0000-0002-4192-8900 
# 
_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 Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                96 
_citation.page_last                 100 
_citation.title                     
'Second-Generation Cap Analogue Prodrugs for Targeting Aberrant Eukaryotic Translation Initiation Factor 4E Activity in Cancer.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00466 
_citation.pdbx_database_id_PubMed   39811141 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cardenas, E.L.'     1 ?                   
primary 
;O'Rourke, R.L.
;
2 ?                   
primary 'Menon, A.'          3 ?                   
primary 'Vega-Hernandez, G.' 4 ?                   
primary 'Meagher, J.'        5 ?                   
primary 'Stuckey, J.'        6 ?                   
primary 'Garner, A.L.'       7 0000-0002-0870-3347 
# 
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 'Eukaryotic translation initiation factor 4E' 22290.334 2   ? ? ? ? 
2 non-polymer syn "7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE" 458.235   1   ? ? ? ? 
3 non-polymer syn 
'2-[3-[[2-azanyl-7-[(5-chloranyl-1-benzofuran-2-yl)methyl]-6-oxidanylidene-1~{H}-purin-9-yl]methyl]phenyl]ethylphosphonic acid' 
514.878   1   ? ? ? ? 
4 water       nat water 18.015    151 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'eIF4E,eIF-4F 25 kDa subunit,mRNA cap-binding protein' 
# 
_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       
;MVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEK
NKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKER
LGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEK
NKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKER
LGLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE"                                                                                     
M7G   
3 '2-[3-[[2-azanyl-7-[(5-chloranyl-1-benzofuran-2-yl)methyl]-6-oxidanylidene-1~{H}-purin-9-yl]methyl]phenyl]ethylphosphonic acid' 
A1A8P 
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   VAL n 
1 3   ALA n 
1 4   ASN n 
1 5   PRO n 
1 6   GLU n 
1 7   HIS n 
1 8   TYR n 
1 9   ILE n 
1 10  LYS n 
1 11  HIS n 
1 12  PRO n 
1 13  LEU n 
1 14  GLN n 
1 15  ASN n 
1 16  ARG n 
1 17  TRP n 
1 18  ALA n 
1 19  LEU n 
1 20  TRP n 
1 21  PHE n 
1 22  PHE n 
1 23  LYS n 
1 24  ASN n 
1 25  ASP n 
1 26  LYS n 
1 27  SER n 
1 28  LYS n 
1 29  THR n 
1 30  TRP n 
1 31  GLN n 
1 32  ALA n 
1 33  ASN n 
1 34  LEU n 
1 35  ARG n 
1 36  LEU n 
1 37  ILE n 
1 38  SER n 
1 39  LYS n 
1 40  PHE n 
1 41  ASP n 
1 42  THR n 
1 43  VAL n 
1 44  GLU n 
1 45  ASP n 
1 46  PHE n 
1 47  TRP n 
1 48  ALA n 
1 49  LEU n 
1 50  TYR n 
1 51  ASN n 
1 52  HIS n 
1 53  ILE n 
1 54  GLN n 
1 55  LEU n 
1 56  SER n 
1 57  SER n 
1 58  ASN n 
1 59  LEU n 
1 60  MET n 
1 61  PRO n 
1 62  GLY n 
1 63  CYS n 
1 64  ASP n 
1 65  TYR n 
1 66  SER n 
1 67  LEU n 
1 68  PHE n 
1 69  LYS n 
1 70  ASP n 
1 71  GLY n 
1 72  ILE n 
1 73  GLU n 
1 74  PRO n 
1 75  MET n 
1 76  TRP n 
1 77  GLU n 
1 78  ASP n 
1 79  GLU n 
1 80  LYS n 
1 81  ASN n 
1 82  LYS n 
1 83  ARG n 
1 84  GLY n 
1 85  GLY n 
1 86  ARG n 
1 87  TRP n 
1 88  LEU n 
1 89  ILE n 
1 90  THR n 
1 91  LEU n 
1 92  ASN n 
1 93  LYS n 
1 94  GLN n 
1 95  GLN n 
1 96  ARG n 
1 97  ARG n 
1 98  SER n 
1 99  ASP n 
1 100 LEU n 
1 101 ASP n 
1 102 ARG n 
1 103 PHE n 
1 104 TRP n 
1 105 LEU n 
1 106 GLU n 
1 107 THR n 
1 108 LEU n 
1 109 LEU n 
1 110 CYS n 
1 111 LEU n 
1 112 ILE n 
1 113 GLY n 
1 114 GLU n 
1 115 SER n 
1 116 PHE n 
1 117 ASP n 
1 118 ASP n 
1 119 TYR n 
1 120 SER n 
1 121 ASP n 
1 122 ASP n 
1 123 VAL n 
1 124 CYS n 
1 125 GLY n 
1 126 ALA n 
1 127 VAL n 
1 128 VAL n 
1 129 ASN n 
1 130 VAL n 
1 131 ARG n 
1 132 ALA n 
1 133 LYS n 
1 134 GLY n 
1 135 ASP n 
1 136 LYS n 
1 137 ILE n 
1 138 ALA n 
1 139 ILE n 
1 140 TRP n 
1 141 THR n 
1 142 THR n 
1 143 GLU n 
1 144 CYS n 
1 145 GLU n 
1 146 ASN n 
1 147 ARG n 
1 148 GLU n 
1 149 ALA n 
1 150 VAL n 
1 151 THR n 
1 152 HIS n 
1 153 ILE n 
1 154 GLY n 
1 155 ARG n 
1 156 VAL n 
1 157 TYR n 
1 158 LYS n 
1 159 GLU n 
1 160 ARG n 
1 161 LEU n 
1 162 GLY n 
1 163 LEU n 
1 164 PRO n 
1 165 PRO n 
1 166 LYS n 
1 167 ILE n 
1 168 VAL n 
1 169 ILE n 
1 170 GLY n 
1 171 TYR n 
1 172 GLN n 
1 173 SER n 
1 174 HIS n 
1 175 ALA n 
1 176 ASP n 
1 177 THR n 
1 178 ALA n 
1 179 THR n 
1 180 LYS n 
1 181 SER n 
1 182 GLY n 
1 183 SER n 
1 184 THR n 
1 185 THR n 
1 186 LYS n 
1 187 ASN n 
1 188 ARG n 
1 189 PHE n 
1 190 VAL n 
1 191 VAL 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                   191 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'EIF4E, EIF4EL1, EIF4F' 
_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 
A1A8P non-polymer         . 
'2-[3-[[2-azanyl-7-[(5-chloranyl-1-benzofuran-2-yl)methyl]-6-oxidanylidene-1~{H}-purin-9-yl]methyl]phenyl]ethylphosphonic acid' ? 
'C23 H22 Cl N5 O5 P 1' 514.878 
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 
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 
M7G   non-polymer         . "7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE" ? 'C11 H18 N5 O11 P2 1'  458.235 
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   27  27  MET MET A . n 
A 1 2   VAL 2   28  28  VAL VAL A . n 
A 1 3   ALA 3   29  29  ALA ALA A . n 
A 1 4   ASN 4   30  30  ASN ASN A . n 
A 1 5   PRO 5   31  31  PRO PRO A . n 
A 1 6   GLU 6   32  32  GLU GLU A . n 
A 1 7   HIS 7   33  33  HIS HIS A . n 
A 1 8   TYR 8   34  34  TYR TYR A . n 
A 1 9   ILE 9   35  35  ILE ILE A . n 
A 1 10  LYS 10  36  36  LYS LYS A . n 
A 1 11  HIS 11  37  37  HIS HIS A . n 
A 1 12  PRO 12  38  38  PRO PRO A . n 
A 1 13  LEU 13  39  39  LEU LEU A . n 
A 1 14  GLN 14  40  40  GLN GLN A . n 
A 1 15  ASN 15  41  41  ASN ASN A . n 
A 1 16  ARG 16  42  42  ARG ARG A . n 
A 1 17  TRP 17  43  43  TRP TRP A . n 
A 1 18  ALA 18  44  44  ALA ALA A . n 
A 1 19  LEU 19  45  45  LEU LEU A . n 
A 1 20  TRP 20  46  46  TRP TRP A . n 
A 1 21  PHE 21  47  47  PHE PHE A . n 
A 1 22  PHE 22  48  48  PHE PHE A . n 
A 1 23  LYS 23  49  49  LYS LYS A . n 
A 1 24  ASN 24  50  50  ASN ASN A . n 
A 1 25  ASP 25  51  51  ASP ASP A . n 
A 1 26  LYS 26  52  52  LYS LYS A . n 
A 1 27  SER 27  53  53  SER SER A . n 
A 1 28  LYS 28  54  54  LYS LYS A . n 
A 1 29  THR 29  55  55  THR THR A . n 
A 1 30  TRP 30  56  56  TRP TRP A . n 
A 1 31  GLN 31  57  57  GLN GLN A . n 
A 1 32  ALA 32  58  58  ALA ALA A . n 
A 1 33  ASN 33  59  59  ASN ASN A . n 
A 1 34  LEU 34  60  60  LEU LEU A . n 
A 1 35  ARG 35  61  61  ARG ARG A . n 
A 1 36  LEU 36  62  62  LEU LEU A . n 
A 1 37  ILE 37  63  63  ILE ILE A . n 
A 1 38  SER 38  64  64  SER SER A . n 
A 1 39  LYS 39  65  65  LYS LYS A . n 
A 1 40  PHE 40  66  66  PHE PHE A . n 
A 1 41  ASP 41  67  67  ASP ASP A . n 
A 1 42  THR 42  68  68  THR THR A . n 
A 1 43  VAL 43  69  69  VAL VAL A . n 
A 1 44  GLU 44  70  70  GLU GLU A . n 
A 1 45  ASP 45  71  71  ASP ASP A . n 
A 1 46  PHE 46  72  72  PHE PHE A . n 
A 1 47  TRP 47  73  73  TRP TRP A . n 
A 1 48  ALA 48  74  74  ALA ALA A . n 
A 1 49  LEU 49  75  75  LEU LEU A . n 
A 1 50  TYR 50  76  76  TYR TYR A . n 
A 1 51  ASN 51  77  77  ASN ASN A . n 
A 1 52  HIS 52  78  78  HIS HIS A . n 
A 1 53  ILE 53  79  79  ILE ILE A . n 
A 1 54  GLN 54  80  80  GLN GLN A . n 
A 1 55  LEU 55  81  81  LEU LEU A . n 
A 1 56  SER 56  82  82  SER SER A . n 
A 1 57  SER 57  83  83  SER SER A . n 
A 1 58  ASN 58  84  84  ASN ASN A . n 
A 1 59  LEU 59  85  85  LEU LEU A . n 
A 1 60  MET 60  86  86  MET MET A . n 
A 1 61  PRO 61  87  87  PRO PRO A . n 
A 1 62  GLY 62  88  88  GLY GLY A . n 
A 1 63  CYS 63  89  89  CYS CYS A . n 
A 1 64  ASP 64  90  90  ASP ASP A . n 
A 1 65  TYR 65  91  91  TYR TYR A . n 
A 1 66  SER 66  92  92  SER SER A . n 
A 1 67  LEU 67  93  93  LEU LEU A . n 
A 1 68  PHE 68  94  94  PHE PHE A . n 
A 1 69  LYS 69  95  95  LYS LYS A . n 
A 1 70  ASP 70  96  96  ASP ASP A . n 
A 1 71  GLY 71  97  97  GLY GLY A . n 
A 1 72  ILE 72  98  98  ILE ILE A . n 
A 1 73  GLU 73  99  99  GLU GLU A . n 
A 1 74  PRO 74  100 100 PRO PRO A . n 
A 1 75  MET 75  101 101 MET MET A . n 
A 1 76  TRP 76  102 102 TRP TRP A . n 
A 1 77  GLU 77  103 103 GLU GLU A . n 
A 1 78  ASP 78  104 104 ASP ASP A . n 
A 1 79  GLU 79  105 105 GLU GLU A . n 
A 1 80  LYS 80  106 106 LYS LYS A . n 
A 1 81  ASN 81  107 107 ASN ASN A . n 
A 1 82  LYS 82  108 108 LYS LYS A . n 
A 1 83  ARG 83  109 109 ARG ARG A . n 
A 1 84  GLY 84  110 110 GLY GLY A . n 
A 1 85  GLY 85  111 111 GLY GLY A . n 
A 1 86  ARG 86  112 112 ARG ARG A . n 
A 1 87  TRP 87  113 113 TRP TRP A . n 
A 1 88  LEU 88  114 114 LEU LEU A . n 
A 1 89  ILE 89  115 115 ILE ILE A . n 
A 1 90  THR 90  116 116 THR THR A . n 
A 1 91  LEU 91  117 117 LEU LEU A . n 
A 1 92  ASN 92  118 118 ASN ASN A . n 
A 1 93  LYS 93  119 119 LYS LYS A . n 
A 1 94  GLN 94  120 120 GLN GLN A . n 
A 1 95  GLN 95  121 121 GLN GLN A . n 
A 1 96  ARG 96  122 122 ARG ARG A . n 
A 1 97  ARG 97  123 123 ARG ARG A . n 
A 1 98  SER 98  124 124 SER SER A . n 
A 1 99  ASP 99  125 125 ASP ASP A . n 
A 1 100 LEU 100 126 126 LEU LEU A . n 
A 1 101 ASP 101 127 127 ASP ASP A . n 
A 1 102 ARG 102 128 128 ARG ARG A . n 
A 1 103 PHE 103 129 129 PHE PHE A . n 
A 1 104 TRP 104 130 130 TRP TRP A . n 
A 1 105 LEU 105 131 131 LEU LEU A . n 
A 1 106 GLU 106 132 132 GLU GLU A . n 
A 1 107 THR 107 133 133 THR THR A . n 
A 1 108 LEU 108 134 134 LEU LEU A . n 
A 1 109 LEU 109 135 135 LEU LEU A . n 
A 1 110 CYS 110 136 136 CYS CYS A . n 
A 1 111 LEU 111 137 137 LEU LEU A . n 
A 1 112 ILE 112 138 138 ILE ILE A . n 
A 1 113 GLY 113 139 139 GLY GLY A . n 
A 1 114 GLU 114 140 140 GLU GLU A . n 
A 1 115 SER 115 141 141 SER SER A . n 
A 1 116 PHE 116 142 142 PHE PHE A . n 
A 1 117 ASP 117 143 143 ASP ASP A . n 
A 1 118 ASP 118 144 144 ASP ASP A . n 
A 1 119 TYR 119 145 145 TYR TYR A . n 
A 1 120 SER 120 146 146 SER SER A . n 
A 1 121 ASP 121 147 147 ASP ASP A . n 
A 1 122 ASP 122 148 148 ASP ASP A . n 
A 1 123 VAL 123 149 149 VAL VAL A . n 
A 1 124 CYS 124 150 150 CYS CYS A . n 
A 1 125 GLY 125 151 151 GLY GLY A . n 
A 1 126 ALA 126 152 152 ALA ALA A . n 
A 1 127 VAL 127 153 153 VAL VAL A . n 
A 1 128 VAL 128 154 154 VAL VAL A . n 
A 1 129 ASN 129 155 155 ASN ASN A . n 
A 1 130 VAL 130 156 156 VAL VAL A . n 
A 1 131 ARG 131 157 157 ARG ARG A . n 
A 1 132 ALA 132 158 158 ALA ALA A . n 
A 1 133 LYS 133 159 159 LYS LYS A . n 
A 1 134 GLY 134 160 160 GLY GLY A . n 
A 1 135 ASP 135 161 161 ASP ASP A . n 
A 1 136 LYS 136 162 162 LYS LYS A . n 
A 1 137 ILE 137 163 163 ILE ILE A . n 
A 1 138 ALA 138 164 164 ALA ALA A . n 
A 1 139 ILE 139 165 165 ILE ILE A . n 
A 1 140 TRP 140 166 166 TRP TRP A . n 
A 1 141 THR 141 167 167 THR THR A . n 
A 1 142 THR 142 168 168 THR THR A . n 
A 1 143 GLU 143 169 169 GLU GLU A . n 
A 1 144 CYS 144 170 170 CYS CYS A . n 
A 1 145 GLU 145 171 171 GLU GLU A . n 
A 1 146 ASN 146 172 172 ASN ASN A . n 
A 1 147 ARG 147 173 173 ARG ARG A . n 
A 1 148 GLU 148 174 174 GLU GLU A . n 
A 1 149 ALA 149 175 175 ALA ALA A . n 
A 1 150 VAL 150 176 176 VAL VAL A . n 
A 1 151 THR 151 177 177 THR THR A . n 
A 1 152 HIS 152 178 178 HIS HIS A . n 
A 1 153 ILE 153 179 179 ILE ILE A . n 
A 1 154 GLY 154 180 180 GLY GLY A . n 
A 1 155 ARG 155 181 181 ARG ARG A . n 
A 1 156 VAL 156 182 182 VAL VAL A . n 
A 1 157 TYR 157 183 183 TYR TYR A . n 
A 1 158 LYS 158 184 184 LYS LYS A . n 
A 1 159 GLU 159 185 185 GLU GLU A . n 
A 1 160 ARG 160 186 186 ARG ARG A . n 
A 1 161 LEU 161 187 187 LEU LEU A . n 
A 1 162 GLY 162 188 188 GLY GLY A . n 
A 1 163 LEU 163 189 189 LEU LEU A . n 
A 1 164 PRO 164 190 190 PRO PRO A . n 
A 1 165 PRO 165 191 191 PRO PRO A . n 
A 1 166 LYS 166 192 192 LYS LYS A . n 
A 1 167 ILE 167 193 193 ILE ILE A . n 
A 1 168 VAL 168 194 194 VAL VAL A . n 
A 1 169 ILE 169 195 195 ILE ILE A . n 
A 1 170 GLY 170 196 196 GLY GLY A . n 
A 1 171 TYR 171 197 197 TYR TYR A . n 
A 1 172 GLN 172 198 198 GLN GLN A . n 
A 1 173 SER 173 199 199 SER SER A . n 
A 1 174 HIS 174 200 200 HIS HIS A . n 
A 1 175 ALA 175 201 201 ALA ALA A . n 
A 1 176 ASP 176 202 202 ASP ASP A . n 
A 1 177 THR 177 203 203 THR THR A . n 
A 1 178 ALA 178 204 204 ALA ALA A . n 
A 1 179 THR 179 205 205 THR THR A . n 
A 1 180 LYS 180 206 206 LYS LYS A . n 
A 1 181 SER 181 207 207 SER SER A . n 
A 1 182 GLY 182 208 ?   ?   ?   A . n 
A 1 183 SER 183 209 ?   ?   ?   A . n 
A 1 184 THR 184 210 ?   ?   ?   A . n 
A 1 185 THR 185 211 ?   ?   ?   A . n 
A 1 186 LYS 186 212 212 LYS LYS A . n 
A 1 187 ASN 187 213 213 ASN ASN A . n 
A 1 188 ARG 188 214 214 ARG ARG A . n 
A 1 189 PHE 189 215 215 PHE PHE A . n 
A 1 190 VAL 190 216 216 VAL VAL A . n 
A 1 191 VAL 191 217 217 VAL VAL A . n 
B 1 1   MET 1   27  ?   ?   ?   B . n 
B 1 2   VAL 2   28  ?   ?   ?   B . n 
B 1 3   ALA 3   29  29  ALA ALA B . n 
B 1 4   ASN 4   30  30  ASN ASN B . n 
B 1 5   PRO 5   31  31  PRO PRO B . n 
B 1 6   GLU 6   32  32  GLU GLU B . n 
B 1 7   HIS 7   33  33  HIS HIS B . n 
B 1 8   TYR 8   34  34  TYR TYR B . n 
B 1 9   ILE 9   35  35  ILE ILE B . n 
B 1 10  LYS 10  36  36  LYS LYS B . n 
B 1 11  HIS 11  37  37  HIS HIS B . n 
B 1 12  PRO 12  38  38  PRO PRO B . n 
B 1 13  LEU 13  39  39  LEU LEU B . n 
B 1 14  GLN 14  40  40  GLN GLN B . n 
B 1 15  ASN 15  41  41  ASN ASN B . n 
B 1 16  ARG 16  42  42  ARG ARG B . n 
B 1 17  TRP 17  43  43  TRP TRP B . n 
B 1 18  ALA 18  44  44  ALA ALA B . n 
B 1 19  LEU 19  45  45  LEU LEU B . n 
B 1 20  TRP 20  46  46  TRP TRP B . n 
B 1 21  PHE 21  47  47  PHE PHE B . n 
B 1 22  PHE 22  48  48  PHE PHE B . n 
B 1 23  LYS 23  49  49  LYS LYS B . n 
B 1 24  ASN 24  50  50  ASN ASN B . n 
B 1 25  ASP 25  51  51  ASP ASP B . n 
B 1 26  LYS 26  52  52  LYS LYS B . n 
B 1 27  SER 27  53  53  SER SER B . n 
B 1 28  LYS 28  54  54  LYS LYS B . n 
B 1 29  THR 29  55  55  THR THR B . n 
B 1 30  TRP 30  56  56  TRP TRP B . n 
B 1 31  GLN 31  57  57  GLN GLN B . n 
B 1 32  ALA 32  58  58  ALA ALA B . n 
B 1 33  ASN 33  59  59  ASN ASN B . n 
B 1 34  LEU 34  60  60  LEU LEU B . n 
B 1 35  ARG 35  61  61  ARG ARG B . n 
B 1 36  LEU 36  62  62  LEU LEU B . n 
B 1 37  ILE 37  63  63  ILE ILE B . n 
B 1 38  SER 38  64  64  SER SER B . n 
B 1 39  LYS 39  65  65  LYS LYS B . n 
B 1 40  PHE 40  66  66  PHE PHE B . n 
B 1 41  ASP 41  67  67  ASP ASP B . n 
B 1 42  THR 42  68  68  THR THR B . n 
B 1 43  VAL 43  69  69  VAL VAL B . n 
B 1 44  GLU 44  70  70  GLU GLU B . n 
B 1 45  ASP 45  71  71  ASP ASP B . n 
B 1 46  PHE 46  72  72  PHE PHE B . n 
B 1 47  TRP 47  73  73  TRP TRP B . n 
B 1 48  ALA 48  74  74  ALA ALA B . n 
B 1 49  LEU 49  75  75  LEU LEU B . n 
B 1 50  TYR 50  76  76  TYR TYR B . n 
B 1 51  ASN 51  77  77  ASN ASN B . n 
B 1 52  HIS 52  78  78  HIS HIS B . n 
B 1 53  ILE 53  79  79  ILE ILE B . n 
B 1 54  GLN 54  80  80  GLN GLN B . n 
B 1 55  LEU 55  81  81  LEU LEU B . n 
B 1 56  SER 56  82  82  SER SER B . n 
B 1 57  SER 57  83  ?   ?   ?   B . n 
B 1 58  ASN 58  84  ?   ?   ?   B . n 
B 1 59  LEU 59  85  ?   ?   ?   B . n 
B 1 60  MET 60  86  ?   ?   ?   B . n 
B 1 61  PRO 61  87  ?   ?   ?   B . n 
B 1 62  GLY 62  88  ?   ?   ?   B . n 
B 1 63  CYS 63  89  89  CYS CYS B . n 
B 1 64  ASP 64  90  90  ASP ASP B . n 
B 1 65  TYR 65  91  91  TYR TYR B . n 
B 1 66  SER 66  92  92  SER SER B . n 
B 1 67  LEU 67  93  93  LEU LEU B . n 
B 1 68  PHE 68  94  94  PHE PHE B . n 
B 1 69  LYS 69  95  95  LYS LYS B . n 
B 1 70  ASP 70  96  96  ASP ASP B . n 
B 1 71  GLY 71  97  97  GLY GLY B . n 
B 1 72  ILE 72  98  98  ILE ILE B . n 
B 1 73  GLU 73  99  99  GLU GLU B . n 
B 1 74  PRO 74  100 100 PRO PRO B . n 
B 1 75  MET 75  101 101 MET MET B . n 
B 1 76  TRP 76  102 102 TRP TRP B . n 
B 1 77  GLU 77  103 103 GLU GLU B . n 
B 1 78  ASP 78  104 104 ASP ASP B . n 
B 1 79  GLU 79  105 105 GLU GLU B . n 
B 1 80  LYS 80  106 106 LYS LYS B . n 
B 1 81  ASN 81  107 107 ASN ASN B . n 
B 1 82  LYS 82  108 108 LYS LYS B . n 
B 1 83  ARG 83  109 109 ARG ARG B . n 
B 1 84  GLY 84  110 110 GLY GLY B . n 
B 1 85  GLY 85  111 111 GLY GLY B . n 
B 1 86  ARG 86  112 112 ARG ARG B . n 
B 1 87  TRP 87  113 113 TRP TRP B . n 
B 1 88  LEU 88  114 114 LEU LEU B . n 
B 1 89  ILE 89  115 115 ILE ILE B . n 
B 1 90  THR 90  116 116 THR THR B . n 
B 1 91  LEU 91  117 117 LEU LEU B . n 
B 1 92  ASN 92  118 118 ASN ASN B . n 
B 1 93  LYS 93  119 119 LYS LYS B . n 
B 1 94  GLN 94  120 ?   ?   ?   B . n 
B 1 95  GLN 95  121 ?   ?   ?   B . n 
B 1 96  ARG 96  122 ?   ?   ?   B . n 
B 1 97  ARG 97  123 ?   ?   ?   B . n 
B 1 98  SER 98  124 ?   ?   ?   B . n 
B 1 99  ASP 99  125 125 ASP ASP B . n 
B 1 100 LEU 100 126 126 LEU LEU B . n 
B 1 101 ASP 101 127 127 ASP ASP B . n 
B 1 102 ARG 102 128 128 ARG ARG B . n 
B 1 103 PHE 103 129 129 PHE PHE B . n 
B 1 104 TRP 104 130 130 TRP TRP B . n 
B 1 105 LEU 105 131 131 LEU LEU B . n 
B 1 106 GLU 106 132 132 GLU GLU B . n 
B 1 107 THR 107 133 133 THR THR B . n 
B 1 108 LEU 108 134 134 LEU LEU B . n 
B 1 109 LEU 109 135 135 LEU LEU B . n 
B 1 110 CYS 110 136 136 CYS CYS B . n 
B 1 111 LEU 111 137 137 LEU LEU B . n 
B 1 112 ILE 112 138 138 ILE ILE B . n 
B 1 113 GLY 113 139 139 GLY GLY B . n 
B 1 114 GLU 114 140 140 GLU GLU B . n 
B 1 115 SER 115 141 141 SER SER B . n 
B 1 116 PHE 116 142 142 PHE PHE B . n 
B 1 117 ASP 117 143 143 ASP ASP B . n 
B 1 118 ASP 118 144 144 ASP ASP B . n 
B 1 119 TYR 119 145 145 TYR TYR B . n 
B 1 120 SER 120 146 146 SER SER B . n 
B 1 121 ASP 121 147 147 ASP ASP B . n 
B 1 122 ASP 122 148 148 ASP ASP B . n 
B 1 123 VAL 123 149 149 VAL VAL B . n 
B 1 124 CYS 124 150 150 CYS CYS B . n 
B 1 125 GLY 125 151 151 GLY GLY B . n 
B 1 126 ALA 126 152 152 ALA ALA B . n 
B 1 127 VAL 127 153 153 VAL VAL B . n 
B 1 128 VAL 128 154 154 VAL VAL B . n 
B 1 129 ASN 129 155 155 ASN ASN B . n 
B 1 130 VAL 130 156 156 VAL VAL B . n 
B 1 131 ARG 131 157 157 ARG ARG B . n 
B 1 132 ALA 132 158 158 ALA ALA B . n 
B 1 133 LYS 133 159 159 LYS LYS B . n 
B 1 134 GLY 134 160 160 GLY GLY B . n 
B 1 135 ASP 135 161 161 ASP ASP B . n 
B 1 136 LYS 136 162 162 LYS LYS B . n 
B 1 137 ILE 137 163 163 ILE ILE B . n 
B 1 138 ALA 138 164 164 ALA ALA B . n 
B 1 139 ILE 139 165 165 ILE ILE B . n 
B 1 140 TRP 140 166 166 TRP TRP B . n 
B 1 141 THR 141 167 167 THR THR B . n 
B 1 142 THR 142 168 168 THR THR B . n 
B 1 143 GLU 143 169 169 GLU GLU B . n 
B 1 144 CYS 144 170 170 CYS CYS B . n 
B 1 145 GLU 145 171 171 GLU GLU B . n 
B 1 146 ASN 146 172 172 ASN ASN B . n 
B 1 147 ARG 147 173 173 ARG ARG B . n 
B 1 148 GLU 148 174 174 GLU GLU B . n 
B 1 149 ALA 149 175 175 ALA ALA B . n 
B 1 150 VAL 150 176 176 VAL VAL B . n 
B 1 151 THR 151 177 177 THR THR B . n 
B 1 152 HIS 152 178 178 HIS HIS B . n 
B 1 153 ILE 153 179 179 ILE ILE B . n 
B 1 154 GLY 154 180 180 GLY GLY B . n 
B 1 155 ARG 155 181 181 ARG ARG B . n 
B 1 156 VAL 156 182 182 VAL VAL B . n 
B 1 157 TYR 157 183 183 TYR TYR B . n 
B 1 158 LYS 158 184 184 LYS LYS B . n 
B 1 159 GLU 159 185 185 GLU GLU B . n 
B 1 160 ARG 160 186 186 ARG ARG B . n 
B 1 161 LEU 161 187 187 LEU LEU B . n 
B 1 162 GLY 162 188 188 GLY GLY B . n 
B 1 163 LEU 163 189 189 LEU LEU B . n 
B 1 164 PRO 164 190 190 PRO PRO B . n 
B 1 165 PRO 165 191 191 PRO PRO B . n 
B 1 166 LYS 166 192 192 LYS LYS B . n 
B 1 167 ILE 167 193 193 ILE ILE B . n 
B 1 168 VAL 168 194 194 VAL VAL B . n 
B 1 169 ILE 169 195 195 ILE ILE B . n 
B 1 170 GLY 170 196 196 GLY GLY B . n 
B 1 171 TYR 171 197 197 TYR TYR B . n 
B 1 172 GLN 172 198 198 GLN GLN B . n 
B 1 173 SER 173 199 199 SER SER B . n 
B 1 174 HIS 174 200 200 HIS HIS B . n 
B 1 175 ALA 175 201 201 ALA ALA B . n 
B 1 176 ASP 176 202 202 ASP ASP B . n 
B 1 177 THR 177 203 203 THR THR B . n 
B 1 178 ALA 178 204 204 ALA ALA B . n 
B 1 179 THR 179 205 205 THR THR B . n 
B 1 180 LYS 180 206 206 LYS LYS B . n 
B 1 181 SER 181 207 207 SER SER B . n 
B 1 182 GLY 182 208 208 GLY GLY B . n 
B 1 183 SER 183 209 ?   ?   ?   B . n 
B 1 184 THR 184 210 ?   ?   ?   B . n 
B 1 185 THR 185 211 211 THR THR B . n 
B 1 186 LYS 186 212 212 LYS LYS B . n 
B 1 187 ASN 187 213 213 ASN ASN B . n 
B 1 188 ARG 188 214 214 ARG ARG B . n 
B 1 189 PHE 189 215 215 PHE PHE B . n 
B 1 190 VAL 190 216 216 VAL VAL B . n 
B 1 191 VAL 191 217 217 VAL VAL B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A8P 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A8P 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 M7G   1  301 301 M7G   M7G A . 
D 3 A1A8P 1  301 301 A1A8P 121 B . 
E 4 HOH   1  401 103 HOH   HOH A . 
E 4 HOH   2  402 123 HOH   HOH A . 
E 4 HOH   3  403 111 HOH   HOH A . 
E 4 HOH   4  404 155 HOH   HOH A . 
E 4 HOH   5  405 75  HOH   HOH A . 
E 4 HOH   6  406 163 HOH   HOH A . 
E 4 HOH   7  407 5   HOH   HOH A . 
E 4 HOH   8  408 36  HOH   HOH A . 
E 4 HOH   9  409 13  HOH   HOH A . 
E 4 HOH   10 410 117 HOH   HOH A . 
E 4 HOH   11 411 64  HOH   HOH A . 
E 4 HOH   12 412 45  HOH   HOH A . 
E 4 HOH   13 413 94  HOH   HOH A . 
E 4 HOH   14 414 121 HOH   HOH A . 
E 4 HOH   15 415 29  HOH   HOH A . 
E 4 HOH   16 416 73  HOH   HOH A . 
E 4 HOH   17 417 136 HOH   HOH A . 
E 4 HOH   18 418 3   HOH   HOH A . 
E 4 HOH   19 419 71  HOH   HOH A . 
E 4 HOH   20 420 10  HOH   HOH A . 
E 4 HOH   21 421 127 HOH   HOH A . 
E 4 HOH   22 422 159 HOH   HOH A . 
E 4 HOH   23 423 51  HOH   HOH A . 
E 4 HOH   24 424 12  HOH   HOH A . 
E 4 HOH   25 425 39  HOH   HOH A . 
E 4 HOH   26 426 41  HOH   HOH A . 
E 4 HOH   27 427 37  HOH   HOH A . 
E 4 HOH   28 428 153 HOH   HOH A . 
E 4 HOH   29 429 48  HOH   HOH A . 
E 4 HOH   30 430 108 HOH   HOH A . 
E 4 HOH   31 431 44  HOH   HOH A . 
E 4 HOH   32 432 20  HOH   HOH A . 
E 4 HOH   33 433 68  HOH   HOH A . 
E 4 HOH   34 434 47  HOH   HOH A . 
E 4 HOH   35 435 8   HOH   HOH A . 
E 4 HOH   36 436 38  HOH   HOH A . 
E 4 HOH   37 437 27  HOH   HOH A . 
E 4 HOH   38 438 148 HOH   HOH A . 
E 4 HOH   39 439 83  HOH   HOH A . 
E 4 HOH   40 440 42  HOH   HOH A . 
E 4 HOH   41 441 50  HOH   HOH A . 
E 4 HOH   42 442 17  HOH   HOH A . 
E 4 HOH   43 443 156 HOH   HOH A . 
E 4 HOH   44 444 105 HOH   HOH A . 
E 4 HOH   45 445 31  HOH   HOH A . 
E 4 HOH   46 446 114 HOH   HOH A . 
E 4 HOH   47 447 98  HOH   HOH A . 
E 4 HOH   48 448 145 HOH   HOH A . 
E 4 HOH   49 449 18  HOH   HOH A . 
E 4 HOH   50 450 102 HOH   HOH A . 
E 4 HOH   51 451 151 HOH   HOH A . 
E 4 HOH   52 452 28  HOH   HOH A . 
E 4 HOH   53 453 46  HOH   HOH A . 
E 4 HOH   54 454 138 HOH   HOH A . 
E 4 HOH   55 455 25  HOH   HOH A . 
E 4 HOH   56 456 76  HOH   HOH A . 
E 4 HOH   57 457 43  HOH   HOH A . 
E 4 HOH   58 458 61  HOH   HOH A . 
E 4 HOH   59 459 122 HOH   HOH A . 
E 4 HOH   60 460 80  HOH   HOH A . 
E 4 HOH   61 461 95  HOH   HOH A . 
E 4 HOH   62 462 152 HOH   HOH A . 
E 4 HOH   63 463 6   HOH   HOH A . 
E 4 HOH   64 464 35  HOH   HOH A . 
E 4 HOH   65 465 84  HOH   HOH A . 
E 4 HOH   66 466 70  HOH   HOH A . 
E 4 HOH   67 467 62  HOH   HOH A . 
E 4 HOH   68 468 78  HOH   HOH A . 
E 4 HOH   69 469 72  HOH   HOH A . 
E 4 HOH   70 470 162 HOH   HOH A . 
E 4 HOH   71 471 160 HOH   HOH A . 
E 4 HOH   72 472 99  HOH   HOH A . 
E 4 HOH   73 473 157 HOH   HOH A . 
E 4 HOH   74 474 154 HOH   HOH A . 
F 4 HOH   1  401 139 HOH   HOH B . 
F 4 HOH   2  402 14  HOH   HOH B . 
F 4 HOH   3  403 90  HOH   HOH B . 
F 4 HOH   4  404 91  HOH   HOH B . 
F 4 HOH   5  405 2   HOH   HOH B . 
F 4 HOH   6  406 118 HOH   HOH B . 
F 4 HOH   7  407 54  HOH   HOH B . 
F 4 HOH   8  408 52  HOH   HOH B . 
F 4 HOH   9  409 88  HOH   HOH B . 
F 4 HOH   10 410 9   HOH   HOH B . 
F 4 HOH   11 411 21  HOH   HOH B . 
F 4 HOH   12 412 110 HOH   HOH B . 
F 4 HOH   13 413 137 HOH   HOH B . 
F 4 HOH   14 414 66  HOH   HOH B . 
F 4 HOH   15 415 92  HOH   HOH B . 
F 4 HOH   16 416 59  HOH   HOH B . 
F 4 HOH   17 417 60  HOH   HOH B . 
F 4 HOH   18 418 115 HOH   HOH B . 
F 4 HOH   19 419 144 HOH   HOH B . 
F 4 HOH   20 420 7   HOH   HOH B . 
F 4 HOH   21 421 128 HOH   HOH B . 
F 4 HOH   22 422 23  HOH   HOH B . 
F 4 HOH   23 423 116 HOH   HOH B . 
F 4 HOH   24 424 77  HOH   HOH B . 
F 4 HOH   25 425 149 HOH   HOH B . 
F 4 HOH   26 426 124 HOH   HOH B . 
F 4 HOH   27 427 11  HOH   HOH B . 
F 4 HOH   28 428 56  HOH   HOH B . 
F 4 HOH   29 429 146 HOH   HOH B . 
F 4 HOH   30 430 93  HOH   HOH B . 
F 4 HOH   31 431 40  HOH   HOH B . 
F 4 HOH   32 432 85  HOH   HOH B . 
F 4 HOH   33 433 67  HOH   HOH B . 
F 4 HOH   34 434 34  HOH   HOH B . 
F 4 HOH   35 435 22  HOH   HOH B . 
F 4 HOH   36 436 55  HOH   HOH B . 
F 4 HOH   37 437 24  HOH   HOH B . 
F 4 HOH   38 438 53  HOH   HOH B . 
F 4 HOH   39 439 65  HOH   HOH B . 
F 4 HOH   40 440 33  HOH   HOH B . 
F 4 HOH   41 441 82  HOH   HOH B . 
F 4 HOH   42 442 15  HOH   HOH B . 
F 4 HOH   43 443 16  HOH   HOH B . 
F 4 HOH   44 444 104 HOH   HOH B . 
F 4 HOH   45 445 143 HOH   HOH B . 
F 4 HOH   46 446 141 HOH   HOH B . 
F 4 HOH   47 447 87  HOH   HOH B . 
F 4 HOH   48 448 57  HOH   HOH B . 
F 4 HOH   49 449 147 HOH   HOH B . 
F 4 HOH   50 450 74  HOH   HOH B . 
F 4 HOH   51 451 63  HOH   HOH B . 
F 4 HOH   52 452 81  HOH   HOH B . 
F 4 HOH   53 453 89  HOH   HOH B . 
F 4 HOH   54 454 133 HOH   HOH B . 
F 4 HOH   55 455 69  HOH   HOH B . 
F 4 HOH   56 456 106 HOH   HOH B . 
F 4 HOH   57 457 107 HOH   HOH B . 
F 4 HOH   58 458 101 HOH   HOH B . 
F 4 HOH   59 459 125 HOH   HOH B . 
F 4 HOH   60 460 32  HOH   HOH B . 
F 4 HOH   61 461 130 HOH   HOH B . 
F 4 HOH   62 462 120 HOH   HOH B . 
F 4 HOH   63 463 119 HOH   HOH B . 
F 4 HOH   64 464 161 HOH   HOH B . 
F 4 HOH   65 465 26  HOH   HOH B . 
F 4 HOH   66 466 112 HOH   HOH B . 
F 4 HOH   67 467 142 HOH   HOH B . 
F 4 HOH   68 468 126 HOH   HOH B . 
F 4 HOH   69 469 150 HOH   HOH B . 
F 4 HOH   70 470 97  HOH   HOH B . 
F 4 HOH   71 471 140 HOH   HOH B . 
F 4 HOH   72 472 158 HOH   HOH B . 
F 4 HOH   73 473 109 HOH   HOH B . 
F 4 HOH   74 474 96  HOH   HOH B . 
F 4 HOH   75 475 134 HOH   HOH B . 
F 4 HOH   76 476 113 HOH   HOH B . 
F 4 HOH   77 477 132 HOH   HOH B . 
# 
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 GLU 32  ? CG  ? A GLU 6   CG  
2  1 Y 1 A GLU 32  ? CD  ? A GLU 6   CD  
3  1 Y 1 A GLU 32  ? OE1 ? A GLU 6   OE1 
4  1 Y 1 A GLU 32  ? OE2 ? A GLU 6   OE2 
5  1 Y 1 A LYS 206 ? CG  ? A LYS 180 CG  
6  1 Y 1 A LYS 206 ? CD  ? A LYS 180 CD  
7  1 Y 1 A LYS 206 ? CE  ? A LYS 180 CE  
8  1 Y 1 A LYS 206 ? NZ  ? A LYS 180 NZ  
9  1 Y 1 A LYS 212 ? CG  ? A LYS 186 CG  
10 1 Y 1 A LYS 212 ? CD  ? A LYS 186 CD  
11 1 Y 1 A LYS 212 ? CE  ? A LYS 186 CE  
12 1 Y 1 A LYS 212 ? NZ  ? A LYS 186 NZ  
13 1 Y 1 B CYS 89  ? SG  ? B CYS 63  SG  
14 1 Y 1 B LYS 119 ? CG  ? B LYS 93  CG  
15 1 Y 1 B LYS 119 ? CD  ? B LYS 93  CD  
16 1 Y 1 B LYS 119 ? CE  ? B LYS 93  CE  
17 1 Y 1 B LYS 119 ? NZ  ? B LYS 93  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       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? '2.10.4 (10-JUL-2024)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                      4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.38 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DON 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.194 
_cell.length_a_esd                 ? 
_cell.length_b                     74.397 
_cell.length_b_esd                 ? 
_cell.length_c                     52.454 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9DON 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9DON 
_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             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.40 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '26% Peg 3350, 0.1 M MES pH 6.0, 10% isopropanol and 2 mM CaCl2' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-14 
_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   1.1271 
_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                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.1271 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DON 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.091 
_reflns.d_resolution_low                               50.00 
_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                                     21714 
_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                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.883 
_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                                0.114 
_reflns.pdbx_Rpim_I_all                                0.049 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_reflns.pdbx_CC_star                                   1.00 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.102 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
2.10 2.14  ? ? ? ? ? ? 1051 ? ? ? ? ? ? ? ? ? ? ? 5.2 0.899 ? ? 0.353 0.154 ? 1  1 0.910 0.976 ? 95.8 ? 0.316 ? ? ? ? ? ? ? ? ? 
2.14 2.18  ? ? ? ? ? ? 1090 ? ? ? ? ? ? ? ? ? ? ? 5.4 0.903 ? ? 0.330 0.140 ? 2  1 0.939 0.984 ? 99.2 ? 0.298 ? ? ? ? ? ? ? ? ? 
2.18 2.22  ? ? ? ? ? ? 1078 ? ? ? ? ? ? ? ? ? ? ? 5.6 0.948 ? ? 0.302 0.128 ? 3  1 0.938 0.984 ? 98.6 ? 0.272 ? ? ? ? ? ? ? ? ? 
2.22 2.26  ? ? ? ? ? ? 1096 ? ? ? ? ? ? ? ? ? ? ? 5.7 0.976 ? ? 0.297 0.124 ? 4  1 0.949 0.987 ? 99.3 ? 0.269 ? ? ? ? ? ? ? ? ? 
2.26 2.31  ? ? ? ? ? ? 1076 ? ? ? ? ? ? ? ? ? ? ? 5.7 0.932 ? ? 0.244 0.102 ? 5  1 0.955 0.988 ? 99.4 ? 0.220 ? ? ? ? ? ? ? ? ? 
2.31 2.37  ? ? ? ? ? ? 1112 ? ? ? ? ? ? ? ? ? ? ? 5.9 0.989 ? ? 0.235 0.097 ? 6  1 0.964 0.991 ? 99.5 ? 0.214 ? ? ? ? ? ? ? ? ? 
2.37 2.42  ? ? ? ? ? ? 1082 ? ? ? ? ? ? ? ? ? ? ? 6.0 0.958 ? ? 0.228 0.093 ? 7  1 0.967 0.992 ? 99.5 ? 0.207 ? ? ? ? ? ? ? ? ? 
2.42 2.49  ? ? ? ? ? ? 1121 ? ? ? ? ? ? ? ? ? ? ? 6.1 0.909 ? ? 0.203 0.082 ? 8  1 0.973 0.993 ? 99.6 ? 0.185 ? ? ? ? ? ? ? ? ? 
2.49 2.56  ? ? ? ? ? ? 1085 ? ? ? ? ? ? ? ? ? ? ? 6.1 0.911 ? ? 0.190 0.077 ? 9  1 0.971 0.993 ? 99.7 ? 0.173 ? ? ? ? ? ? ? ? ? 
2.56 2.65  ? ? ? ? ? ? 1112 ? ? ? ? ? ? ? ? ? ? ? 6.0 0.971 ? ? 0.173 0.071 ? 10 1 0.976 0.994 ? 99.8 ? 0.157 ? ? ? ? ? ? ? ? ? 
2.65 2.74  ? ? ? ? ? ? 1103 ? ? ? ? ? ? ? ? ? ? ? 5.9 0.934 ? ? 0.151 0.063 ? 11 1 0.978 0.994 ? 99.2 ? 0.137 ? ? ? ? ? ? ? ? ? 
2.74 2.85  ? ? ? ? ? ? 1052 ? ? ? ? ? ? ? ? ? ? ? 5.4 0.971 ? ? 0.137 0.059 ? 12 1 0.981 0.995 ? 97.0 ? 0.123 ? ? ? ? ? ? ? ? ? 
2.85 2.98  ? ? ? ? ? ? 1036 ? ? ? ? ? ? ? ? ? ? ? 5.2 0.914 ? ? 0.118 0.052 ? 13 1 0.977 0.994 ? 93.3 ? 0.106 ? ? ? ? ? ? ? ? ? 
2.98 3.14  ? ? ? ? ? ? 1100 ? ? ? ? ? ? ? ? ? ? ? 6.0 0.820 ? ? 0.102 0.043 ? 14 1 0.988 0.997 ? 98.9 ? 0.092 ? ? ? ? ? ? ? ? ? 
3.14 3.33  ? ? ? ? ? ? 1109 ? ? ? ? ? ? ? ? ? ? ? 5.8 0.834 ? ? 0.089 0.039 ? 15 1 0.987 0.997 ? 99.4 ? 0.079 ? ? ? ? ? ? ? ? ? 
3.33 3.59  ? ? ? ? ? ? 1084 ? ? ? ? ? ? ? ? ? ? ? 5.5 0.785 ? ? 0.078 0.035 ? 16 1 0.988 0.997 ? 98.0 ? 0.069 ? ? ? ? ? ? ? ? ? 
3.59 3.95  ? ? ? ? ? ? 1081 ? ? ? ? ? ? ? ? ? ? ? 5.3 0.716 ? ? 0.070 0.032 ? 17 1 0.989 0.997 ? 97.3 ? 0.062 ? ? ? ? ? ? ? ? ? 
3.95 4.52  ? ? ? ? ? ? 1083 ? ? ? ? ? ? ? ? ? ? ? 4.9 0.626 ? ? 0.062 0.029 ? 18 1 0.991 0.998 ? 96.8 ? 0.054 ? ? ? ? ? ? ? ? ? 
4.52 5.70  ? ? ? ? ? ? 1028 ? ? ? ? ? ? ? ? ? ? ? 4.5 0.648 ? ? 0.062 0.030 ? 19 1 0.989 0.997 ? 92.2 ? 0.054 ? ? ? ? ? ? ? ? ? 
5.70 50.00 ? ? ? ? ? ? 1135 ? ? ? ? ? ? ? ? ? ? ? 5.6 0.876 ? ? 0.077 0.034 ? 20 1 0.992 0.998 ? 98.2 ? 0.069 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            2.91940 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.90810 
_refine.aniso_B[2][2]                            0.11620 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -3.03560 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.91 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.927 
_refine.correlation_coeff_Fo_to_Fc_free          0.905 
_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                                 9DON 
_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                            2.091 
_refine.ls_d_res_low                             33.50 
_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                     21660 
_refine.ls_number_reflns_R_free                  1050 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.3 
_refine.ls_percent_reflns_R_free                 4.850 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2005 
_refine.ls_R_factor_R_free                       0.2470 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1982 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                          0.000 
_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       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.200 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.197 
_refine.pdbx_overall_SU_R_Blow_DPI               0.249 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.251 
_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_analyze.entry_id                        9DON 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.091 
_refine_hist.d_res_low                        33.50 
_refine_hist.number_atoms_solvent             151 
_refine_hist.number_atoms_total               3201 
_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        2986 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_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 ? 3131 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 0.88  ? 4251 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1083 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 564  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 3131 ? t_it                      10.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.23  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 16.41 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 388  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 2512 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.091 
_refine_ls_shell.d_res_low                        2.11 
_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             417 
_refine_ls_shell.percent_reflns_obs               73.30 
_refine_ls_shell.percent_reflns_R_free            3.92 
_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                  0.1992 
_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.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                  0.2597 
# 
_struct.entry_id                     9DON 
_struct.title                        'Crystal structure of eIF4e in complex with Compound 5-PA' 
_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        9DON 
_struct_keywords.text            'EIF4E, TRANSLATION INITIATION INHIBITOR, TRANSLATION' 
_struct_keywords.pdbx_keywords   TRANSLATION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IF4E_HUMAN 
_struct_ref.pdbx_db_accession          P06730 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKN
KRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERL
GLPPKIVIGYQSHADTATKSGSTTKNRFVV
;
_struct_ref.pdbx_align_begin           28 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DON A 2 ? 191 ? P06730 28 ? 217 ? 28 217 
2 1 9DON B 2 ? 191 ? P06730 28 ? 217 ? 28 217 
# 
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 9DON MET A 1 ? UNP P06730 ? ? 'initiating methionine' 27 1 
2 9DON MET B 1 ? UNP P06730 ? ? 'initiating methionine' 27 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_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 VAL A 43  ? ASN A 51  ? VAL A 69  ASN A 77  1 ? 9  
HELX_P HELX_P2  AA2 LEU A 55  ? LEU A 59  ? LEU A 81  LEU A 85  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 94  ? ASP A 99  ? GLN A 120 ASP A 125 1 ? 6  
HELX_P HELX_P4  AA4 ASP A 99  ? GLY A 113 ? ASP A 125 GLY A 139 1 ? 15 
HELX_P HELX_P5  AA5 PHE A 116 ? ASP A 121 ? PHE A 142 ASP A 147 5 ? 6  
HELX_P HELX_P6  AA6 ASN A 146 ? GLY A 162 ? ASN A 172 GLY A 188 1 ? 17 
HELX_P HELX_P7  AA7 HIS A 174 ? ALA A 178 ? HIS A 200 ALA A 204 1 ? 5  
HELX_P HELX_P8  AA8 TRP B 30  ? ALA B 32  ? TRP B 56  ALA B 58  5 ? 3  
HELX_P HELX_P9  AA9 VAL B 43  ? LEU B 55  ? VAL B 69  LEU B 81  1 ? 13 
HELX_P HELX_P10 AB1 LEU B 100 ? GLY B 113 ? LEU B 126 GLY B 139 1 ? 14 
HELX_P HELX_P11 AB2 PHE B 116 ? ASP B 121 ? PHE B 142 ASP B 147 5 ? 6  
HELX_P HELX_P12 AB3 ASN B 146 ? GLY B 162 ? ASN B 172 GLY B 188 1 ? 17 
HELX_P HELX_P13 AB4 HIS B 174 ? THR B 179 ? HIS B 200 THR B 205 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? 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 LEU A 34  ? THR A 42  ? LEU A 60  THR A 68  
AA1 2 PRO A 12  ? PHE A 22  ? PRO A 38  PHE A 48  
AA1 3 ASP A 64  ? LYS A 69  ? ASP A 90  LYS A 95  
AA1 4 VAL A 123 ? ASN A 129 ? VAL A 149 ASN A 155 
AA1 5 LYS A 136 ? THR A 141 ? LYS A 162 THR A 167 
AA1 6 GLY A 85  ? THR A 90  ? GLY A 111 THR A 116 
AA1 7 GLY A 170 ? SER A 173 ? GLY A 196 SER A 199 
AA1 8 PHE A 189 ? VAL A 190 ? PHE A 215 VAL A 216 
AA2 1 LEU B 34  ? THR B 42  ? LEU B 60  THR B 68  
AA2 2 PRO B 12  ? PHE B 22  ? PRO B 38  PHE B 48  
AA2 3 ASP B 64  ? LYS B 69  ? ASP B 90  LYS B 95  
AA2 4 VAL B 123 ? ASN B 129 ? VAL B 149 ASN B 155 
AA2 5 LYS B 136 ? THR B 141 ? LYS B 162 THR B 167 
AA2 6 GLY B 85  ? THR B 90  ? GLY B 111 THR B 116 
AA2 7 GLY B 170 ? SER B 173 ? GLY B 196 SER B 199 
AA2 8 PHE B 189 ? VAL B 190 ? PHE B 215 VAL B 216 
# 
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 35  ? O ARG A 61  N PHE A 21  ? N PHE A 47  
AA1 2 3 N TRP A 20  ? N TRP A 46  O SER A 66  ? O SER A 92  
AA1 3 4 N TYR A 65  ? N TYR A 91  O VAL A 128 ? O VAL A 154 
AA1 4 5 N CYS A 124 ? N CYS A 150 O TRP A 140 ? O TRP A 166 
AA1 5 6 O ILE A 137 ? O ILE A 163 N ILE A 89  ? N ILE A 115 
AA1 6 7 N LEU A 88  ? N LEU A 114 O GLY A 170 ? O GLY A 196 
AA1 7 8 N TYR A 171 ? N TYR A 197 O PHE A 189 ? O PHE A 215 
AA2 1 2 O PHE B 40  ? O PHE B 66  N TRP B 17  ? N TRP B 43  
AA2 2 3 N ALA B 18  ? N ALA B 44  O PHE B 68  ? O PHE B 94  
AA2 3 4 N TYR B 65  ? N TYR B 91  O VAL B 128 ? O VAL B 154 
AA2 4 5 N GLY B 125 ? N GLY B 151 O TRP B 140 ? O TRP B 166 
AA2 5 6 O ILE B 137 ? O ILE B 163 N ILE B 89  ? N ILE B 115 
AA2 6 7 N ARG B 86  ? N ARG B 112 O GLN B 172 ? O GLN B 198 
AA2 7 8 N TYR B 171 ? N TYR B 197 O PHE B 189 ? O PHE B 215 
# 
_pdbx_entry_details.entry_id                   9DON 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ASP A 143 ? ? 45.52   -118.91 
2 1 ASP B 67  ? ? -142.18 22.24   
3 1 ASP B 143 ? ? 54.21   -134.18 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 1.8263  -12.6791 25.4752 -0.0024 ? 0.0092 ? -0.0023 ? -0.0203 ? 0.0234 ? -0.0593 ? 1.2422 ? 0.0100 
? 0.4674 ? 0.6409 ? 0.2682 ? 0.9392 ? -0.0775 ? -0.0301 ? -0.0011 ? -0.0047 ? 0.0671 ? 0.0409  ? 0.0287  ? -0.0648 ? 0.0104  ? 
2 'X-RAY DIFFRACTION' ? refined 20.3635 -9.2263  47.9548 -0.0140 ? 0.0144 ? 0.0038  ? 0.0006  ? 0.0058 ? -0.0632 ? 0.9571 ? 0.3896 
? 0.6338 ? 1.2746 ? 0.0704 ? 1.0117 ? -0.0092 ? -0.1430 ? -0.0265 ? 0.0732  ? 0.0158 ? -0.0159 ? -0.0128 ? -0.0933 ? -0.0067 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ A|27 - 217 }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|29 - 217 }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 208 ? A GLY 182 
2  1 Y 1 A SER 209 ? A SER 183 
3  1 Y 1 A THR 210 ? A THR 184 
4  1 Y 1 A THR 211 ? A THR 185 
5  1 Y 1 B MET 27  ? B MET 1   
6  1 Y 1 B VAL 28  ? B VAL 2   
7  1 Y 1 B SER 83  ? B SER 57  
8  1 Y 1 B ASN 84  ? B ASN 58  
9  1 Y 1 B LEU 85  ? B LEU 59  
10 1 Y 1 B MET 86  ? B MET 60  
11 1 Y 1 B PRO 87  ? B PRO 61  
12 1 Y 1 B GLY 88  ? B GLY 62  
13 1 Y 1 B GLN 120 ? B GLN 94  
14 1 Y 1 B GLN 121 ? B GLN 95  
15 1 Y 1 B ARG 122 ? B ARG 96  
16 1 Y 1 B ARG 123 ? B ARG 97  
17 1 Y 1 B SER 124 ? B SER 98  
18 1 Y 1 B SER 209 ? B SER 183 
19 1 Y 1 B THR 210 ? B THR 184 
# 
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 
A1A8P C1     C  N N 1   
A1A8P C2     C  Y N 2   
A1A8P C3     C  Y N 3   
A1A8P C4     C  N N 4   
A1A8P C5     C  Y N 5   
A1A8P C6     C  Y N 6   
A1A8P C7     C  Y N 7   
A1A8P N1     N  N N 8   
A1A8P N2     N  N N 9   
A1A8P N3     N  Y N 10  
A1A8P N4     N  Y N 11  
A1A8P C8     C  Y N 12  
A1A8P CL     CL N N 13  
A1A8P C19    C  Y N 14  
A1A8P C18    C  Y N 15  
A1A8P C20    C  Y N 16  
A1A8P C21    C  Y N 17  
A1A8P C22    C  Y N 18  
A1A8P C17    C  Y N 19  
A1A8P C16    C  Y N 20  
A1A8P O4     O  Y N 21  
A1A8P C15    C  Y N 22  
A1A8P C14    C  N N 23  
A1A8P C      C  N N 24  
A1A8P O      O  N N 25  
A1A8P C13    C  Y N 26  
A1A8P N      N  N N 27  
A1A8P C12    C  Y N 28  
A1A8P C9     C  Y N 29  
A1A8P C10    C  N N 30  
A1A8P C11    C  N N 31  
A1A8P P      P  N N 32  
A1A8P O3     O  N N 33  
A1A8P O2     O  N N 34  
A1A8P O1     O  N N 35  
A1A8P H1     H  N N 36  
A1A8P H2     H  N N 37  
A1A8P H3     H  N N 38  
A1A8P H4     H  N N 39  
A1A8P H5     H  N N 40  
A1A8P H6     H  N N 41  
A1A8P H7     H  N N 42  
A1A8P H8     H  N N 43  
A1A8P H9     H  N N 44  
A1A8P H10    H  N N 45  
A1A8P H11    H  N N 46  
A1A8P H12    H  N N 47  
A1A8P H13    H  N N 48  
A1A8P H14    H  N N 49  
A1A8P H15    H  N N 50  
A1A8P H16    H  N N 51  
A1A8P H17    H  N N 52  
A1A8P H18    H  N N 53  
A1A8P H19    H  N N 54  
A1A8P H20    H  N N 55  
A1A8P H21    H  N N 56  
A1A8P H22    H  N N 57  
ALA   N      N  N N 58  
ALA   CA     C  N S 59  
ALA   C      C  N N 60  
ALA   O      O  N N 61  
ALA   CB     C  N N 62  
ALA   OXT    O  N N 63  
ALA   H      H  N N 64  
ALA   H2     H  N N 65  
ALA   HA     H  N N 66  
ALA   HB1    H  N N 67  
ALA   HB2    H  N N 68  
ALA   HB3    H  N N 69  
ALA   HXT    H  N N 70  
ARG   N      N  N N 71  
ARG   CA     C  N S 72  
ARG   C      C  N N 73  
ARG   O      O  N N 74  
ARG   CB     C  N N 75  
ARG   CG     C  N N 76  
ARG   CD     C  N N 77  
ARG   NE     N  N N 78  
ARG   CZ     C  N N 79  
ARG   NH1    N  N N 80  
ARG   NH2    N  N N 81  
ARG   OXT    O  N N 82  
ARG   H      H  N N 83  
ARG   H2     H  N N 84  
ARG   HA     H  N N 85  
ARG   HB2    H  N N 86  
ARG   HB3    H  N N 87  
ARG   HG2    H  N N 88  
ARG   HG3    H  N N 89  
ARG   HD2    H  N N 90  
ARG   HD3    H  N N 91  
ARG   HE     H  N N 92  
ARG   HH11   H  N N 93  
ARG   HH12   H  N N 94  
ARG   HH21   H  N N 95  
ARG   HH22   H  N N 96  
ARG   HXT    H  N N 97  
ASN   N      N  N N 98  
ASN   CA     C  N S 99  
ASN   C      C  N N 100 
ASN   O      O  N N 101 
ASN   CB     C  N N 102 
ASN   CG     C  N N 103 
ASN   OD1    O  N N 104 
ASN   ND2    N  N N 105 
ASN   OXT    O  N N 106 
ASN   H      H  N N 107 
ASN   H2     H  N N 108 
ASN   HA     H  N N 109 
ASN   HB2    H  N N 110 
ASN   HB3    H  N N 111 
ASN   HD21   H  N N 112 
ASN   HD22   H  N N 113 
ASN   HXT    H  N N 114 
ASP   N      N  N N 115 
ASP   CA     C  N S 116 
ASP   C      C  N N 117 
ASP   O      O  N N 118 
ASP   CB     C  N N 119 
ASP   CG     C  N N 120 
ASP   OD1    O  N N 121 
ASP   OD2    O  N N 122 
ASP   OXT    O  N N 123 
ASP   H      H  N N 124 
ASP   H2     H  N N 125 
ASP   HA     H  N N 126 
ASP   HB2    H  N N 127 
ASP   HB3    H  N N 128 
ASP   HD2    H  N N 129 
ASP   HXT    H  N N 130 
CYS   N      N  N N 131 
CYS   CA     C  N R 132 
CYS   C      C  N N 133 
CYS   O      O  N N 134 
CYS   CB     C  N N 135 
CYS   SG     S  N N 136 
CYS   OXT    O  N N 137 
CYS   H      H  N N 138 
CYS   H2     H  N N 139 
CYS   HA     H  N N 140 
CYS   HB2    H  N N 141 
CYS   HB3    H  N N 142 
CYS   HG     H  N N 143 
CYS   HXT    H  N N 144 
GLN   N      N  N N 145 
GLN   CA     C  N S 146 
GLN   C      C  N N 147 
GLN   O      O  N N 148 
GLN   CB     C  N N 149 
GLN   CG     C  N N 150 
GLN   CD     C  N N 151 
GLN   OE1    O  N N 152 
GLN   NE2    N  N N 153 
GLN   OXT    O  N N 154 
GLN   H      H  N N 155 
GLN   H2     H  N N 156 
GLN   HA     H  N N 157 
GLN   HB2    H  N N 158 
GLN   HB3    H  N N 159 
GLN   HG2    H  N N 160 
GLN   HG3    H  N N 161 
GLN   HE21   H  N N 162 
GLN   HE22   H  N N 163 
GLN   HXT    H  N N 164 
GLU   N      N  N N 165 
GLU   CA     C  N S 166 
GLU   C      C  N N 167 
GLU   O      O  N N 168 
GLU   CB     C  N N 169 
GLU   CG     C  N N 170 
GLU   CD     C  N N 171 
GLU   OE1    O  N N 172 
GLU   OE2    O  N N 173 
GLU   OXT    O  N N 174 
GLU   H      H  N N 175 
GLU   H2     H  N N 176 
GLU   HA     H  N N 177 
GLU   HB2    H  N N 178 
GLU   HB3    H  N N 179 
GLU   HG2    H  N N 180 
GLU   HG3    H  N N 181 
GLU   HE2    H  N N 182 
GLU   HXT    H  N N 183 
GLY   N      N  N N 184 
GLY   CA     C  N N 185 
GLY   C      C  N N 186 
GLY   O      O  N N 187 
GLY   OXT    O  N N 188 
GLY   H      H  N N 189 
GLY   H2     H  N N 190 
GLY   HA2    H  N N 191 
GLY   HA3    H  N N 192 
GLY   HXT    H  N N 193 
HIS   N      N  N N 194 
HIS   CA     C  N S 195 
HIS   C      C  N N 196 
HIS   O      O  N N 197 
HIS   CB     C  N N 198 
HIS   CG     C  Y N 199 
HIS   ND1    N  Y N 200 
HIS   CD2    C  Y N 201 
HIS   CE1    C  Y N 202 
HIS   NE2    N  Y N 203 
HIS   OXT    O  N N 204 
HIS   H      H  N N 205 
HIS   H2     H  N N 206 
HIS   HA     H  N N 207 
HIS   HB2    H  N N 208 
HIS   HB3    H  N N 209 
HIS   HD1    H  N N 210 
HIS   HD2    H  N N 211 
HIS   HE1    H  N N 212 
HIS   HE2    H  N N 213 
HIS   HXT    H  N N 214 
HOH   O      O  N N 215 
HOH   H1     H  N N 216 
HOH   H2     H  N N 217 
ILE   N      N  N N 218 
ILE   CA     C  N S 219 
ILE   C      C  N N 220 
ILE   O      O  N N 221 
ILE   CB     C  N S 222 
ILE   CG1    C  N N 223 
ILE   CG2    C  N N 224 
ILE   CD1    C  N N 225 
ILE   OXT    O  N N 226 
ILE   H      H  N N 227 
ILE   H2     H  N N 228 
ILE   HA     H  N N 229 
ILE   HB     H  N N 230 
ILE   HG12   H  N N 231 
ILE   HG13   H  N N 232 
ILE   HG21   H  N N 233 
ILE   HG22   H  N N 234 
ILE   HG23   H  N N 235 
ILE   HD11   H  N N 236 
ILE   HD12   H  N N 237 
ILE   HD13   H  N N 238 
ILE   HXT    H  N N 239 
LEU   N      N  N N 240 
LEU   CA     C  N S 241 
LEU   C      C  N N 242 
LEU   O      O  N N 243 
LEU   CB     C  N N 244 
LEU   CG     C  N N 245 
LEU   CD1    C  N N 246 
LEU   CD2    C  N N 247 
LEU   OXT    O  N N 248 
LEU   H      H  N N 249 
LEU   H2     H  N N 250 
LEU   HA     H  N N 251 
LEU   HB2    H  N N 252 
LEU   HB3    H  N N 253 
LEU   HG     H  N N 254 
LEU   HD11   H  N N 255 
LEU   HD12   H  N N 256 
LEU   HD13   H  N N 257 
LEU   HD21   H  N N 258 
LEU   HD22   H  N N 259 
LEU   HD23   H  N N 260 
LEU   HXT    H  N N 261 
LYS   N      N  N N 262 
LYS   CA     C  N S 263 
LYS   C      C  N N 264 
LYS   O      O  N N 265 
LYS   CB     C  N N 266 
LYS   CG     C  N N 267 
LYS   CD     C  N N 268 
LYS   CE     C  N N 269 
LYS   NZ     N  N N 270 
LYS   OXT    O  N N 271 
LYS   H      H  N N 272 
LYS   H2     H  N N 273 
LYS   HA     H  N N 274 
LYS   HB2    H  N N 275 
LYS   HB3    H  N N 276 
LYS   HG2    H  N N 277 
LYS   HG3    H  N N 278 
LYS   HD2    H  N N 279 
LYS   HD3    H  N N 280 
LYS   HE2    H  N N 281 
LYS   HE3    H  N N 282 
LYS   HZ1    H  N N 283 
LYS   HZ2    H  N N 284 
LYS   HZ3    H  N N 285 
LYS   HXT    H  N N 286 
M7G   PA     P  N N 287 
M7G   O1A    O  N N 288 
M7G   O2A    O  N N 289 
M7G   O3A    O  N N 290 
M7G   "O5'"  O  N N 291 
M7G   PB     P  N N 292 
M7G   O1B    O  N N 293 
M7G   O2B    O  N N 294 
M7G   O3B    O  N N 295 
M7G   "C5'"  C  N N 296 
M7G   "C4'"  C  N R 297 
M7G   "O4'"  O  N N 298 
M7G   "C3'"  C  N S 299 
M7G   "O3'"  O  N N 300 
M7G   "C2'"  C  N R 301 
M7G   "O2'"  O  N N 302 
M7G   "C1'"  C  N R 303 
M7G   N9     N  Y N 304 
M7G   C8     C  Y N 305 
M7G   N7     N  Y N 306 
M7G   CM7    C  N N 307 
M7G   C5     C  Y N 308 
M7G   C6     C  N N 309 
M7G   O6     O  N N 310 
M7G   N1     N  N N 311 
M7G   C2     C  N N 312 
M7G   N2     N  N N 313 
M7G   N3     N  N N 314 
M7G   C4     C  Y N 315 
M7G   HOA2   H  N N 316 
M7G   HOB2   H  N N 317 
M7G   HOB3   H  N N 318 
M7G   "H5'1" H  N N 319 
M7G   "H5'2" H  N N 320 
M7G   "H4'"  H  N N 321 
M7G   "H3'"  H  N N 322 
M7G   "HO3'" H  N N 323 
M7G   "H2'"  H  N N 324 
M7G   "HO2'" H  N N 325 
M7G   "H1'"  H  N N 326 
M7G   H81    H  N N 327 
M7G   HM71   H  N N 328 
M7G   HM72   H  N N 329 
M7G   HM73   H  N N 330 
M7G   HN1    H  N N 331 
M7G   HN21   H  N N 332 
M7G   HN22   H  N N 333 
MET   N      N  N N 334 
MET   CA     C  N S 335 
MET   C      C  N N 336 
MET   O      O  N N 337 
MET   CB     C  N N 338 
MET   CG     C  N N 339 
MET   SD     S  N N 340 
MET   CE     C  N N 341 
MET   OXT    O  N N 342 
MET   H      H  N N 343 
MET   H2     H  N N 344 
MET   HA     H  N N 345 
MET   HB2    H  N N 346 
MET   HB3    H  N N 347 
MET   HG2    H  N N 348 
MET   HG3    H  N N 349 
MET   HE1    H  N N 350 
MET   HE2    H  N N 351 
MET   HE3    H  N N 352 
MET   HXT    H  N N 353 
PHE   N      N  N N 354 
PHE   CA     C  N S 355 
PHE   C      C  N N 356 
PHE   O      O  N N 357 
PHE   CB     C  N N 358 
PHE   CG     C  Y N 359 
PHE   CD1    C  Y N 360 
PHE   CD2    C  Y N 361 
PHE   CE1    C  Y N 362 
PHE   CE2    C  Y N 363 
PHE   CZ     C  Y N 364 
PHE   OXT    O  N N 365 
PHE   H      H  N N 366 
PHE   H2     H  N N 367 
PHE   HA     H  N N 368 
PHE   HB2    H  N N 369 
PHE   HB3    H  N N 370 
PHE   HD1    H  N N 371 
PHE   HD2    H  N N 372 
PHE   HE1    H  N N 373 
PHE   HE2    H  N N 374 
PHE   HZ     H  N N 375 
PHE   HXT    H  N N 376 
PRO   N      N  N N 377 
PRO   CA     C  N S 378 
PRO   C      C  N N 379 
PRO   O      O  N N 380 
PRO   CB     C  N N 381 
PRO   CG     C  N N 382 
PRO   CD     C  N N 383 
PRO   OXT    O  N N 384 
PRO   H      H  N N 385 
PRO   HA     H  N N 386 
PRO   HB2    H  N N 387 
PRO   HB3    H  N N 388 
PRO   HG2    H  N N 389 
PRO   HG3    H  N N 390 
PRO   HD2    H  N N 391 
PRO   HD3    H  N N 392 
PRO   HXT    H  N N 393 
SER   N      N  N N 394 
SER   CA     C  N S 395 
SER   C      C  N N 396 
SER   O      O  N N 397 
SER   CB     C  N N 398 
SER   OG     O  N N 399 
SER   OXT    O  N N 400 
SER   H      H  N N 401 
SER   H2     H  N N 402 
SER   HA     H  N N 403 
SER   HB2    H  N N 404 
SER   HB3    H  N N 405 
SER   HG     H  N N 406 
SER   HXT    H  N N 407 
THR   N      N  N N 408 
THR   CA     C  N S 409 
THR   C      C  N N 410 
THR   O      O  N N 411 
THR   CB     C  N R 412 
THR   OG1    O  N N 413 
THR   CG2    C  N N 414 
THR   OXT    O  N N 415 
THR   H      H  N N 416 
THR   H2     H  N N 417 
THR   HA     H  N N 418 
THR   HB     H  N N 419 
THR   HG1    H  N N 420 
THR   HG21   H  N N 421 
THR   HG22   H  N N 422 
THR   HG23   H  N N 423 
THR   HXT    H  N N 424 
TRP   N      N  N N 425 
TRP   CA     C  N S 426 
TRP   C      C  N N 427 
TRP   O      O  N N 428 
TRP   CB     C  N N 429 
TRP   CG     C  Y N 430 
TRP   CD1    C  Y N 431 
TRP   CD2    C  Y N 432 
TRP   NE1    N  Y N 433 
TRP   CE2    C  Y N 434 
TRP   CE3    C  Y N 435 
TRP   CZ2    C  Y N 436 
TRP   CZ3    C  Y N 437 
TRP   CH2    C  Y N 438 
TRP   OXT    O  N N 439 
TRP   H      H  N N 440 
TRP   H2     H  N N 441 
TRP   HA     H  N N 442 
TRP   HB2    H  N N 443 
TRP   HB3    H  N N 444 
TRP   HD1    H  N N 445 
TRP   HE1    H  N N 446 
TRP   HE3    H  N N 447 
TRP   HZ2    H  N N 448 
TRP   HZ3    H  N N 449 
TRP   HH2    H  N N 450 
TRP   HXT    H  N N 451 
TYR   N      N  N N 452 
TYR   CA     C  N S 453 
TYR   C      C  N N 454 
TYR   O      O  N N 455 
TYR   CB     C  N N 456 
TYR   CG     C  Y N 457 
TYR   CD1    C  Y N 458 
TYR   CD2    C  Y N 459 
TYR   CE1    C  Y N 460 
TYR   CE2    C  Y N 461 
TYR   CZ     C  Y N 462 
TYR   OH     O  N N 463 
TYR   OXT    O  N N 464 
TYR   H      H  N N 465 
TYR   H2     H  N N 466 
TYR   HA     H  N N 467 
TYR   HB2    H  N N 468 
TYR   HB3    H  N N 469 
TYR   HD1    H  N N 470 
TYR   HD2    H  N N 471 
TYR   HE1    H  N N 472 
TYR   HE2    H  N N 473 
TYR   HH     H  N N 474 
TYR   HXT    H  N N 475 
VAL   N      N  N N 476 
VAL   CA     C  N S 477 
VAL   C      C  N N 478 
VAL   O      O  N N 479 
VAL   CB     C  N N 480 
VAL   CG1    C  N N 481 
VAL   CG2    C  N N 482 
VAL   OXT    O  N N 483 
VAL   H      H  N N 484 
VAL   H2     H  N N 485 
VAL   HA     H  N N 486 
VAL   HB     H  N N 487 
VAL   HG11   H  N N 488 
VAL   HG12   H  N N 489 
VAL   HG13   H  N N 490 
VAL   HG21   H  N N 491 
VAL   HG22   H  N N 492 
VAL   HG23   H  N N 493 
VAL   HXT    H  N N 494 
# 
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 
A1A8P CL    C19    sing N N 1   
A1A8P C19   C18    doub Y N 2   
A1A8P C19   C20    sing Y N 3   
A1A8P C18   C17    sing Y N 4   
A1A8P C20   C21    doub Y N 5   
A1A8P C17   C16    sing Y N 6   
A1A8P C17   C22    doub Y N 7   
A1A8P C16   C15    doub Y N 8   
A1A8P C21   C22    sing Y N 9   
A1A8P C22   O4     sing Y N 10  
A1A8P C15   O4     sing Y N 11  
A1A8P C15   C14    sing N N 12  
A1A8P C14   N4     sing N N 13  
A1A8P O     C      doub N N 14  
A1A8P C     C2     sing N N 15  
A1A8P C     N      sing N N 16  
A1A8P N4    C2     sing Y N 17  
A1A8P N4    C13    doub Y N 18  
A1A8P C2    C3     doub Y N 19  
A1A8P N     C1     sing N N 20  
A1A8P C13   N3     sing Y N 21  
A1A8P O1    P      doub N N 22  
A1A8P O2    P      sing N N 23  
A1A8P C3    N3     sing Y N 24  
A1A8P C3    N2     sing N N 25  
A1A8P P     O3     sing N N 26  
A1A8P P     C11    sing N N 27  
A1A8P N3    C4     sing N N 28  
A1A8P C1    N2     doub N N 29  
A1A8P C1    N1     sing N N 30  
A1A8P C4    C5     sing N N 31  
A1A8P C10   C11    sing N N 32  
A1A8P C10   C9     sing N N 33  
A1A8P C12   C5     doub Y N 34  
A1A8P C12   C9     sing Y N 35  
A1A8P C5    C6     sing Y N 36  
A1A8P C9    C8     doub Y N 37  
A1A8P C6    C7     doub Y N 38  
A1A8P C8    C7     sing Y N 39  
A1A8P C4    H1     sing N N 40  
A1A8P C4    H2     sing N N 41  
A1A8P C6    H3     sing N N 42  
A1A8P C7    H4     sing N N 43  
A1A8P N1    H5     sing N N 44  
A1A8P N1    H6     sing N N 45  
A1A8P C8    H7     sing N N 46  
A1A8P C18   H8     sing N N 47  
A1A8P C20   H9     sing N N 48  
A1A8P C21   H10    sing N N 49  
A1A8P C16   H11    sing N N 50  
A1A8P C14   H12    sing N N 51  
A1A8P C14   H13    sing N N 52  
A1A8P C13   H14    sing N N 53  
A1A8P N     H15    sing N N 54  
A1A8P C12   H16    sing N N 55  
A1A8P C10   H17    sing N N 56  
A1A8P C10   H18    sing N N 57  
A1A8P C11   H19    sing N N 58  
A1A8P C11   H20    sing N N 59  
A1A8P O3    H21    sing N N 60  
A1A8P O2    H22    sing N N 61  
ALA   N     CA     sing N N 62  
ALA   N     H      sing N N 63  
ALA   N     H2     sing N N 64  
ALA   CA    C      sing N N 65  
ALA   CA    CB     sing N N 66  
ALA   CA    HA     sing N N 67  
ALA   C     O      doub N N 68  
ALA   C     OXT    sing N N 69  
ALA   CB    HB1    sing N N 70  
ALA   CB    HB2    sing N N 71  
ALA   CB    HB3    sing N N 72  
ALA   OXT   HXT    sing N N 73  
ARG   N     CA     sing N N 74  
ARG   N     H      sing N N 75  
ARG   N     H2     sing N N 76  
ARG   CA    C      sing N N 77  
ARG   CA    CB     sing N N 78  
ARG   CA    HA     sing N N 79  
ARG   C     O      doub N N 80  
ARG   C     OXT    sing N N 81  
ARG   CB    CG     sing N N 82  
ARG   CB    HB2    sing N N 83  
ARG   CB    HB3    sing N N 84  
ARG   CG    CD     sing N N 85  
ARG   CG    HG2    sing N N 86  
ARG   CG    HG3    sing N N 87  
ARG   CD    NE     sing N N 88  
ARG   CD    HD2    sing N N 89  
ARG   CD    HD3    sing N N 90  
ARG   NE    CZ     sing N N 91  
ARG   NE    HE     sing N N 92  
ARG   CZ    NH1    sing N N 93  
ARG   CZ    NH2    doub N N 94  
ARG   NH1   HH11   sing N N 95  
ARG   NH1   HH12   sing N N 96  
ARG   NH2   HH21   sing N N 97  
ARG   NH2   HH22   sing N N 98  
ARG   OXT   HXT    sing N N 99  
ASN   N     CA     sing N N 100 
ASN   N     H      sing N N 101 
ASN   N     H2     sing N N 102 
ASN   CA    C      sing N N 103 
ASN   CA    CB     sing N N 104 
ASN   CA    HA     sing N N 105 
ASN   C     O      doub N N 106 
ASN   C     OXT    sing N N 107 
ASN   CB    CG     sing N N 108 
ASN   CB    HB2    sing N N 109 
ASN   CB    HB3    sing N N 110 
ASN   CG    OD1    doub N N 111 
ASN   CG    ND2    sing N N 112 
ASN   ND2   HD21   sing N N 113 
ASN   ND2   HD22   sing N N 114 
ASN   OXT   HXT    sing N N 115 
ASP   N     CA     sing N N 116 
ASP   N     H      sing N N 117 
ASP   N     H2     sing N N 118 
ASP   CA    C      sing N N 119 
ASP   CA    CB     sing N N 120 
ASP   CA    HA     sing N N 121 
ASP   C     O      doub N N 122 
ASP   C     OXT    sing N N 123 
ASP   CB    CG     sing N N 124 
ASP   CB    HB2    sing N N 125 
ASP   CB    HB3    sing N N 126 
ASP   CG    OD1    doub N N 127 
ASP   CG    OD2    sing N N 128 
ASP   OD2   HD2    sing N N 129 
ASP   OXT   HXT    sing N N 130 
CYS   N     CA     sing N N 131 
CYS   N     H      sing N N 132 
CYS   N     H2     sing N N 133 
CYS   CA    C      sing N N 134 
CYS   CA    CB     sing N N 135 
CYS   CA    HA     sing N N 136 
CYS   C     O      doub N N 137 
CYS   C     OXT    sing N N 138 
CYS   CB    SG     sing N N 139 
CYS   CB    HB2    sing N N 140 
CYS   CB    HB3    sing N N 141 
CYS   SG    HG     sing N N 142 
CYS   OXT   HXT    sing N N 143 
GLN   N     CA     sing N N 144 
GLN   N     H      sing N N 145 
GLN   N     H2     sing N N 146 
GLN   CA    C      sing N N 147 
GLN   CA    CB     sing N N 148 
GLN   CA    HA     sing N N 149 
GLN   C     O      doub N N 150 
GLN   C     OXT    sing N N 151 
GLN   CB    CG     sing N N 152 
GLN   CB    HB2    sing N N 153 
GLN   CB    HB3    sing N N 154 
GLN   CG    CD     sing N N 155 
GLN   CG    HG2    sing N N 156 
GLN   CG    HG3    sing N N 157 
GLN   CD    OE1    doub N N 158 
GLN   CD    NE2    sing N N 159 
GLN   NE2   HE21   sing N N 160 
GLN   NE2   HE22   sing N N 161 
GLN   OXT   HXT    sing N N 162 
GLU   N     CA     sing N N 163 
GLU   N     H      sing N N 164 
GLU   N     H2     sing N N 165 
GLU   CA    C      sing N N 166 
GLU   CA    CB     sing N N 167 
GLU   CA    HA     sing N N 168 
GLU   C     O      doub N N 169 
GLU   C     OXT    sing N N 170 
GLU   CB    CG     sing N N 171 
GLU   CB    HB2    sing N N 172 
GLU   CB    HB3    sing N N 173 
GLU   CG    CD     sing N N 174 
GLU   CG    HG2    sing N N 175 
GLU   CG    HG3    sing N N 176 
GLU   CD    OE1    doub N N 177 
GLU   CD    OE2    sing N N 178 
GLU   OE2   HE2    sing N N 179 
GLU   OXT   HXT    sing N N 180 
GLY   N     CA     sing N N 181 
GLY   N     H      sing N N 182 
GLY   N     H2     sing N N 183 
GLY   CA    C      sing N N 184 
GLY   CA    HA2    sing N N 185 
GLY   CA    HA3    sing N N 186 
GLY   C     O      doub N N 187 
GLY   C     OXT    sing N N 188 
GLY   OXT   HXT    sing N N 189 
HIS   N     CA     sing N N 190 
HIS   N     H      sing N N 191 
HIS   N     H2     sing N N 192 
HIS   CA    C      sing N N 193 
HIS   CA    CB     sing N N 194 
HIS   CA    HA     sing N N 195 
HIS   C     O      doub N N 196 
HIS   C     OXT    sing N N 197 
HIS   CB    CG     sing N N 198 
HIS   CB    HB2    sing N N 199 
HIS   CB    HB3    sing N N 200 
HIS   CG    ND1    sing Y N 201 
HIS   CG    CD2    doub Y N 202 
HIS   ND1   CE1    doub Y N 203 
HIS   ND1   HD1    sing N N 204 
HIS   CD2   NE2    sing Y N 205 
HIS   CD2   HD2    sing N N 206 
HIS   CE1   NE2    sing Y N 207 
HIS   CE1   HE1    sing N N 208 
HIS   NE2   HE2    sing N N 209 
HIS   OXT   HXT    sing N N 210 
HOH   O     H1     sing N N 211 
HOH   O     H2     sing N N 212 
ILE   N     CA     sing N N 213 
ILE   N     H      sing N N 214 
ILE   N     H2     sing N N 215 
ILE   CA    C      sing N N 216 
ILE   CA    CB     sing N N 217 
ILE   CA    HA     sing N N 218 
ILE   C     O      doub N N 219 
ILE   C     OXT    sing N N 220 
ILE   CB    CG1    sing N N 221 
ILE   CB    CG2    sing N N 222 
ILE   CB    HB     sing N N 223 
ILE   CG1   CD1    sing N N 224 
ILE   CG1   HG12   sing N N 225 
ILE   CG1   HG13   sing N N 226 
ILE   CG2   HG21   sing N N 227 
ILE   CG2   HG22   sing N N 228 
ILE   CG2   HG23   sing N N 229 
ILE   CD1   HD11   sing N N 230 
ILE   CD1   HD12   sing N N 231 
ILE   CD1   HD13   sing N N 232 
ILE   OXT   HXT    sing N N 233 
LEU   N     CA     sing N N 234 
LEU   N     H      sing N N 235 
LEU   N     H2     sing N N 236 
LEU   CA    C      sing N N 237 
LEU   CA    CB     sing N N 238 
LEU   CA    HA     sing N N 239 
LEU   C     O      doub N N 240 
LEU   C     OXT    sing N N 241 
LEU   CB    CG     sing N N 242 
LEU   CB    HB2    sing N N 243 
LEU   CB    HB3    sing N N 244 
LEU   CG    CD1    sing N N 245 
LEU   CG    CD2    sing N N 246 
LEU   CG    HG     sing N N 247 
LEU   CD1   HD11   sing N N 248 
LEU   CD1   HD12   sing N N 249 
LEU   CD1   HD13   sing N N 250 
LEU   CD2   HD21   sing N N 251 
LEU   CD2   HD22   sing N N 252 
LEU   CD2   HD23   sing N N 253 
LEU   OXT   HXT    sing N N 254 
LYS   N     CA     sing N N 255 
LYS   N     H      sing N N 256 
LYS   N     H2     sing N N 257 
LYS   CA    C      sing N N 258 
LYS   CA    CB     sing N N 259 
LYS   CA    HA     sing N N 260 
LYS   C     O      doub N N 261 
LYS   C     OXT    sing N N 262 
LYS   CB    CG     sing N N 263 
LYS   CB    HB2    sing N N 264 
LYS   CB    HB3    sing N N 265 
LYS   CG    CD     sing N N 266 
LYS   CG    HG2    sing N N 267 
LYS   CG    HG3    sing N N 268 
LYS   CD    CE     sing N N 269 
LYS   CD    HD2    sing N N 270 
LYS   CD    HD3    sing N N 271 
LYS   CE    NZ     sing N N 272 
LYS   CE    HE2    sing N N 273 
LYS   CE    HE3    sing N N 274 
LYS   NZ    HZ1    sing N N 275 
LYS   NZ    HZ2    sing N N 276 
LYS   NZ    HZ3    sing N N 277 
LYS   OXT   HXT    sing N N 278 
M7G   PA    O1A    doub N N 279 
M7G   PA    O2A    sing N N 280 
M7G   PA    O3A    sing N N 281 
M7G   PA    "O5'"  sing N N 282 
M7G   O2A   HOA2   sing N N 283 
M7G   O3A   PB     sing N N 284 
M7G   "O5'" "C5'"  sing N N 285 
M7G   PB    O1B    doub N N 286 
M7G   PB    O2B    sing N N 287 
M7G   PB    O3B    sing N N 288 
M7G   O2B   HOB2   sing N N 289 
M7G   O3B   HOB3   sing N N 290 
M7G   "C5'" "C4'"  sing N N 291 
M7G   "C5'" "H5'1" sing N N 292 
M7G   "C5'" "H5'2" sing N N 293 
M7G   "C4'" "O4'"  sing N N 294 
M7G   "C4'" "C3'"  sing N N 295 
M7G   "C4'" "H4'"  sing N N 296 
M7G   "O4'" "C1'"  sing N N 297 
M7G   "C3'" "O3'"  sing N N 298 
M7G   "C3'" "C2'"  sing N N 299 
M7G   "C3'" "H3'"  sing N N 300 
M7G   "O3'" "HO3'" sing N N 301 
M7G   "C2'" "O2'"  sing N N 302 
M7G   "C2'" "C1'"  sing N N 303 
M7G   "C2'" "H2'"  sing N N 304 
M7G   "O2'" "HO2'" sing N N 305 
M7G   "C1'" N9     sing N N 306 
M7G   "C1'" "H1'"  sing N N 307 
M7G   N9    C8     sing Y N 308 
M7G   N9    C4     sing Y N 309 
M7G   C8    N7     doub Y N 310 
M7G   C8    H81    sing N N 311 
M7G   N7    CM7    sing N N 312 
M7G   N7    C5     sing Y N 313 
M7G   CM7   HM71   sing N N 314 
M7G   CM7   HM72   sing N N 315 
M7G   CM7   HM73   sing N N 316 
M7G   C5    C6     sing N N 317 
M7G   C5    C4     doub Y N 318 
M7G   C6    O6     doub N N 319 
M7G   C6    N1     sing N N 320 
M7G   N1    C2     sing N N 321 
M7G   N1    HN1    sing N N 322 
M7G   C2    N2     sing N N 323 
M7G   C2    N3     doub N N 324 
M7G   N2    HN21   sing N N 325 
M7G   N2    HN22   sing N N 326 
M7G   N3    C4     sing N N 327 
MET   N     CA     sing N N 328 
MET   N     H      sing N N 329 
MET   N     H2     sing N N 330 
MET   CA    C      sing N N 331 
MET   CA    CB     sing N N 332 
MET   CA    HA     sing N N 333 
MET   C     O      doub N N 334 
MET   C     OXT    sing N N 335 
MET   CB    CG     sing N N 336 
MET   CB    HB2    sing N N 337 
MET   CB    HB3    sing N N 338 
MET   CG    SD     sing N N 339 
MET   CG    HG2    sing N N 340 
MET   CG    HG3    sing N N 341 
MET   SD    CE     sing N N 342 
MET   CE    HE1    sing N N 343 
MET   CE    HE2    sing N N 344 
MET   CE    HE3    sing N N 345 
MET   OXT   HXT    sing N N 346 
PHE   N     CA     sing N N 347 
PHE   N     H      sing N N 348 
PHE   N     H2     sing N N 349 
PHE   CA    C      sing N N 350 
PHE   CA    CB     sing N N 351 
PHE   CA    HA     sing N N 352 
PHE   C     O      doub N N 353 
PHE   C     OXT    sing N N 354 
PHE   CB    CG     sing N N 355 
PHE   CB    HB2    sing N N 356 
PHE   CB    HB3    sing N N 357 
PHE   CG    CD1    doub Y N 358 
PHE   CG    CD2    sing Y N 359 
PHE   CD1   CE1    sing Y N 360 
PHE   CD1   HD1    sing N N 361 
PHE   CD2   CE2    doub Y N 362 
PHE   CD2   HD2    sing N N 363 
PHE   CE1   CZ     doub Y N 364 
PHE   CE1   HE1    sing N N 365 
PHE   CE2   CZ     sing Y N 366 
PHE   CE2   HE2    sing N N 367 
PHE   CZ    HZ     sing N N 368 
PHE   OXT   HXT    sing N N 369 
PRO   N     CA     sing N N 370 
PRO   N     CD     sing N N 371 
PRO   N     H      sing N N 372 
PRO   CA    C      sing N N 373 
PRO   CA    CB     sing N N 374 
PRO   CA    HA     sing N N 375 
PRO   C     O      doub N N 376 
PRO   C     OXT    sing N N 377 
PRO   CB    CG     sing N N 378 
PRO   CB    HB2    sing N N 379 
PRO   CB    HB3    sing N N 380 
PRO   CG    CD     sing N N 381 
PRO   CG    HG2    sing N N 382 
PRO   CG    HG3    sing N N 383 
PRO   CD    HD2    sing N N 384 
PRO   CD    HD3    sing N N 385 
PRO   OXT   HXT    sing N N 386 
SER   N     CA     sing N N 387 
SER   N     H      sing N N 388 
SER   N     H2     sing N N 389 
SER   CA    C      sing N N 390 
SER   CA    CB     sing N N 391 
SER   CA    HA     sing N N 392 
SER   C     O      doub N N 393 
SER   C     OXT    sing N N 394 
SER   CB    OG     sing N N 395 
SER   CB    HB2    sing N N 396 
SER   CB    HB3    sing N N 397 
SER   OG    HG     sing N N 398 
SER   OXT   HXT    sing N N 399 
THR   N     CA     sing N N 400 
THR   N     H      sing N N 401 
THR   N     H2     sing N N 402 
THR   CA    C      sing N N 403 
THR   CA    CB     sing N N 404 
THR   CA    HA     sing N N 405 
THR   C     O      doub N N 406 
THR   C     OXT    sing N N 407 
THR   CB    OG1    sing N N 408 
THR   CB    CG2    sing N N 409 
THR   CB    HB     sing N N 410 
THR   OG1   HG1    sing N N 411 
THR   CG2   HG21   sing N N 412 
THR   CG2   HG22   sing N N 413 
THR   CG2   HG23   sing N N 414 
THR   OXT   HXT    sing N N 415 
TRP   N     CA     sing N N 416 
TRP   N     H      sing N N 417 
TRP   N     H2     sing N N 418 
TRP   CA    C      sing N N 419 
TRP   CA    CB     sing N N 420 
TRP   CA    HA     sing N N 421 
TRP   C     O      doub N N 422 
TRP   C     OXT    sing N N 423 
TRP   CB    CG     sing N N 424 
TRP   CB    HB2    sing N N 425 
TRP   CB    HB3    sing N N 426 
TRP   CG    CD1    doub Y N 427 
TRP   CG    CD2    sing Y N 428 
TRP   CD1   NE1    sing Y N 429 
TRP   CD1   HD1    sing N N 430 
TRP   CD2   CE2    doub Y N 431 
TRP   CD2   CE3    sing Y N 432 
TRP   NE1   CE2    sing Y N 433 
TRP   NE1   HE1    sing N N 434 
TRP   CE2   CZ2    sing Y N 435 
TRP   CE3   CZ3    doub Y N 436 
TRP   CE3   HE3    sing N N 437 
TRP   CZ2   CH2    doub Y N 438 
TRP   CZ2   HZ2    sing N N 439 
TRP   CZ3   CH2    sing Y N 440 
TRP   CZ3   HZ3    sing N N 441 
TRP   CH2   HH2    sing N N 442 
TRP   OXT   HXT    sing N N 443 
TYR   N     CA     sing N N 444 
TYR   N     H      sing N N 445 
TYR   N     H2     sing N N 446 
TYR   CA    C      sing N N 447 
TYR   CA    CB     sing N N 448 
TYR   CA    HA     sing N N 449 
TYR   C     O      doub N N 450 
TYR   C     OXT    sing N N 451 
TYR   CB    CG     sing N N 452 
TYR   CB    HB2    sing N N 453 
TYR   CB    HB3    sing N N 454 
TYR   CG    CD1    doub Y N 455 
TYR   CG    CD2    sing Y N 456 
TYR   CD1   CE1    sing Y N 457 
TYR   CD1   HD1    sing N N 458 
TYR   CD2   CE2    doub Y N 459 
TYR   CD2   HD2    sing N N 460 
TYR   CE1   CZ     doub Y N 461 
TYR   CE1   HE1    sing N N 462 
TYR   CE2   CZ     sing Y N 463 
TYR   CE2   HE2    sing N N 464 
TYR   CZ    OH     sing N N 465 
TYR   OH    HH     sing N N 466 
TYR   OXT   HXT    sing N N 467 
VAL   N     CA     sing N N 468 
VAL   N     H      sing N N 469 
VAL   N     H2     sing N N 470 
VAL   CA    C      sing N N 471 
VAL   CA    CB     sing N N 472 
VAL   CA    HA     sing N N 473 
VAL   C     O      doub N N 474 
VAL   C     OXT    sing N N 475 
VAL   CB    CG1    sing N N 476 
VAL   CB    CG2    sing N N 477 
VAL   CB    HB     sing N N 478 
VAL   CG1   HG11   sing N N 479 
VAL   CG1   HG12   sing N N 480 
VAL   CG1   HG13   sing N N 481 
VAL   CG2   HG21   sing N N 482 
VAL   CG2   HG22   sing N N 483 
VAL   CG2   HG23   sing N N 484 
VAL   OXT   HXT    sing N N 485 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM132341 
_pdbx_audit_support.ordinal                1 
# 
_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   4TQC 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DON 
_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]   0.020328 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002633 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013441 
_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]   0.019224 
_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  
CL 
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     . MET   A 1 1   ? 43.045  1.928   36.631 1.00 50.78 ? 27  MET   A N     1 
ATOM   2    C  CA    . MET   A 1 1   ? 43.265  3.110   35.817 1.00 50.87 ? 27  MET   A CA    1 
ATOM   3    C  C     . MET   A 1 1   ? 42.840  2.892   34.367 1.00 50.26 ? 27  MET   A C     1 
ATOM   4    O  O     . MET   A 1 1   ? 42.309  3.813   33.752 1.00 50.35 ? 27  MET   A O     1 
ATOM   5    C  CB    . MET   A 1 1   ? 44.727  3.572   35.907 1.00 52.06 ? 27  MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 1   ? 45.729  2.582   35.377 1.00 55.22 ? 27  MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 1   ? 46.986  3.445   34.398 1.00 64.93 ? 27  MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 1   ? 46.036  3.825   32.916 1.00 63.49 ? 27  MET   A CE    1 
ATOM   9    N  N     . VAL   A 1 2   ? 43.033  1.677   33.831 1.00 49.31 ? 28  VAL   A N     1 
ATOM   10   C  CA    . VAL   A 1 2   ? 42.665  1.406   32.444 1.00 49.26 ? 28  VAL   A CA    1 
ATOM   11   C  C     . VAL   A 1 2   ? 41.204  0.963   32.377 1.00 49.13 ? 28  VAL   A C     1 
ATOM   12   O  O     . VAL   A 1 2   ? 40.434  1.464   31.558 1.00 49.43 ? 28  VAL   A O     1 
ATOM   13   C  CB    . VAL   A 1 2   ? 43.581  0.376   31.721 1.00 49.98 ? 28  VAL   A CB    1 
ATOM   14   C  CG1   . VAL   A 1 2   ? 43.558  0.610   30.220 1.00 50.59 ? 28  VAL   A CG1   1 
ATOM   15   C  CG2   . VAL   A 1 2   ? 45.025  0.419   32.235 1.00 50.77 ? 28  VAL   A CG2   1 
ATOM   16   N  N     . ALA   A 1 3   ? 40.826  0.035   33.247 1.00 48.48 ? 29  ALA   A N     1 
ATOM   17   C  CA    . ALA   A 1 3   ? 39.496  -0.524  33.279 1.00 48.35 ? 29  ALA   A CA    1 
ATOM   18   C  C     . ALA   A 1 3   ? 38.495  0.338   34.054 1.00 48.00 ? 29  ALA   A C     1 
ATOM   19   O  O     . ALA   A 1 3   ? 38.133  0.008   35.190 1.00 48.41 ? 29  ALA   A O     1 
ATOM   20   C  CB    . ALA   A 1 3   ? 39.548  -1.932  33.848 1.00 48.78 ? 29  ALA   A CB    1 
ATOM   21   N  N     . ASN   A 1 4   ? 38.058  1.450   33.445 1.00 46.73 ? 30  ASN   A N     1 
ATOM   22   C  CA    . ASN   A 1 4   ? 37.073  2.320   34.088 1.00 45.63 ? 30  ASN   A CA    1 
ATOM   23   C  C     . ASN   A 1 4   ? 35.751  1.629   34.018 1.00 42.96 ? 30  ASN   A C     1 
ATOM   24   O  O     . ASN   A 1 4   ? 35.377  1.140   32.957 1.00 43.05 ? 30  ASN   A O     1 
ATOM   25   C  CB    . ASN   A 1 4   ? 36.909  3.635   33.344 1.00 47.78 ? 30  ASN   A CB    1 
ATOM   26   C  CG    . ASN   A 1 4   ? 38.158  4.420   33.243 1.00 53.16 ? 30  ASN   A CG    1 
ATOM   27   O  OD1   . ASN   A 1 4   ? 39.043  4.338   34.111 1.00 54.47 ? 30  ASN   A OD1   1 
ATOM   28   N  ND2   . ASN   A 1 4   ? 38.279  5.168   32.151 1.00 54.78 ? 30  ASN   A ND2   1 
ATOM   29   N  N     . PRO   A 1 5   ? 34.998  1.616   35.120 1.00 41.05 ? 31  PRO   A N     1 
ATOM   30   C  CA    . PRO   A 1 5   ? 33.687  0.960   35.090 1.00 40.12 ? 31  PRO   A CA    1 
ATOM   31   C  C     . PRO   A 1 5   ? 32.741  1.697   34.153 1.00 38.88 ? 31  PRO   A C     1 
ATOM   32   O  O     . PRO   A 1 5   ? 32.565  2.905   34.270 1.00 39.31 ? 31  PRO   A O     1 
ATOM   33   C  CB    . PRO   A 1 5   ? 33.217  1.039   36.549 1.00 40.91 ? 31  PRO   A CB    1 
ATOM   34   C  CG    . PRO   A 1 5   ? 34.450  1.294   37.346 1.00 41.74 ? 31  PRO   A CG    1 
ATOM   35   C  CD    . PRO   A 1 5   ? 35.306  2.140   36.461 1.00 40.25 ? 31  PRO   A CD    1 
ATOM   36   N  N     . GLU   A 1 6   ? 32.217  0.990   33.175 1.00 37.43 ? 32  GLU   A N     1 
ATOM   37   C  CA    . GLU   A 1 6   ? 31.285  1.561   32.216 1.00 36.70 ? 32  GLU   A CA    1 
ATOM   38   C  C     . GLU   A 1 6   ? 29.837  1.277   32.621 1.00 35.59 ? 32  GLU   A C     1 
ATOM   39   O  O     . GLU   A 1 6   ? 29.534  0.232   33.208 1.00 36.02 ? 32  GLU   A O     1 
ATOM   40   C  CB    . GLU   A 1 6   ? 31.545  0.978   30.825 1.00 38.81 ? 32  GLU   A CB    1 
ATOM   41   N  N     . HIS   A 1 7   ? 28.951  2.194   32.278 1.00 33.70 ? 33  HIS   A N     1 
ATOM   42   C  CA    . HIS   A 1 7   ? 27.525  2.090   32.547 1.00 32.92 ? 33  HIS   A CA    1 
ATOM   43   C  C     . HIS   A 1 7   ? 26.753  2.750   31.410 1.00 31.35 ? 33  HIS   A C     1 
ATOM   44   O  O     . HIS   A 1 7   ? 27.304  3.592   30.700 1.00 31.81 ? 33  HIS   A O     1 
ATOM   45   C  CB    . HIS   A 1 7   ? 27.156  2.701   33.911 1.00 34.19 ? 33  HIS   A CB    1 
ATOM   46   C  CG    . HIS   A 1 7   ? 27.829  4.007   34.209 1.00 37.06 ? 33  HIS   A CG    1 
ATOM   47   N  ND1   . HIS   A 1 7   ? 29.196  4.079   34.453 1.00 39.07 ? 33  HIS   A ND1   1 
ATOM   48   C  CD2   . HIS   A 1 7   ? 27.296  5.243   34.342 1.00 38.31 ? 33  HIS   A CD2   1 
ATOM   49   C  CE1   . HIS   A 1 7   ? 29.451  5.355   34.691 1.00 39.57 ? 33  HIS   A CE1   1 
ATOM   50   N  NE2   . HIS   A 1 7   ? 28.340  6.092   34.655 1.00 39.42 ? 33  HIS   A NE2   1 
ATOM   51   N  N     . TYR   A 1 8   ? 25.493  2.366   31.218 1.00 29.29 ? 34  TYR   A N     1 
ATOM   52   C  CA    . TYR   A 1 8   ? 24.700  2.856   30.099 1.00 28.71 ? 34  TYR   A CA    1 
ATOM   53   C  C     . TYR   A 1 8   ? 23.391  3.469   30.595 1.00 28.95 ? 34  TYR   A C     1 
ATOM   54   O  O     . TYR   A 1 8   ? 22.775  2.934   31.509 1.00 29.04 ? 34  TYR   A O     1 
ATOM   55   C  CB    . TYR   A 1 8   ? 24.457  1.719   29.069 1.00 28.36 ? 34  TYR   A CB    1 
ATOM   56   C  CG    . TYR   A 1 8   ? 25.721  0.926   28.788 1.00 29.30 ? 34  TYR   A CG    1 
ATOM   57   C  CD1   . TYR   A 1 8   ? 26.759  1.476   28.044 1.00 30.06 ? 34  TYR   A CD1   1 
ATOM   58   C  CD2   . TYR   A 1 8   ? 25.945  -0.301  29.404 1.00 30.29 ? 34  TYR   A CD2   1 
ATOM   59   C  CE1   . TYR   A 1 8   ? 27.967  0.807   27.881 1.00 30.96 ? 34  TYR   A CE1   1 
ATOM   60   C  CE2   . TYR   A 1 8   ? 27.143  -0.986  29.238 1.00 31.27 ? 34  TYR   A CE2   1 
ATOM   61   C  CZ    . TYR   A 1 8   ? 28.149  -0.432  28.467 1.00 32.19 ? 34  TYR   A CZ    1 
ATOM   62   O  OH    . TYR   A 1 8   ? 29.339  -1.095  28.320 1.00 33.77 ? 34  TYR   A OH    1 
ATOM   63   N  N     . ILE   A 1 9   ? 22.986  4.603   30.009 1.00 28.69 ? 35  ILE   A N     1 
ATOM   64   C  CA    . ILE   A 1 9   ? 21.774  5.329   30.392 1.00 28.91 ? 35  ILE   A CA    1 
ATOM   65   C  C     . ILE   A 1 9   ? 20.504  4.538   29.994 1.00 27.72 ? 35  ILE   A C     1 
ATOM   66   O  O     . ILE   A 1 9   ? 19.505  4.583   30.702 1.00 27.46 ? 35  ILE   A O     1 
ATOM   67   C  CB    . ILE   A 1 9   ? 21.823  6.750   29.761 1.00 30.50 ? 35  ILE   A CB    1 
ATOM   68   C  CG1   . ILE   A 1 9   ? 20.823  7.714   30.422 1.00 32.47 ? 35  ILE   A CG1   1 
ATOM   69   C  CG2   . ILE   A 1 9   ? 21.646  6.701   28.241 1.00 31.02 ? 35  ILE   A CG2   1 
ATOM   70   C  CD1   . ILE   A 1 9   ? 21.241  8.127   31.843 1.00 34.47 ? 35  ILE   A CD1   1 
ATOM   71   N  N     . LYS   A 1 10  ? 20.570  3.792   28.879 1.00 26.78 ? 36  LYS   A N     1 
ATOM   72   C  CA    . LYS   A 1 10  ? 19.486  2.976   28.356 1.00 26.35 ? 36  LYS   A CA    1 
ATOM   73   C  C     . LYS   A 1 10  ? 20.019  1.641   27.847 1.00 24.44 ? 36  LYS   A C     1 
ATOM   74   O  O     . LYS   A 1 10  ? 21.141  1.557   27.338 1.00 24.09 ? 36  LYS   A O     1 
ATOM   75   C  CB    . LYS   A 1 10  ? 18.752  3.708   27.222 1.00 30.02 ? 36  LYS   A CB    1 
ATOM   76   C  CG    . LYS   A 1 10  ? 17.699  4.722   27.699 1.00 36.34 ? 36  LYS   A CG    1 
ATOM   77   C  CD    . LYS   A 1 10  ? 16.616  4.067   28.569 1.00 42.29 ? 36  LYS   A CD    1 
ATOM   78   C  CE    . LYS   A 1 10  ? 15.355  4.885   28.684 1.00 46.46 ? 36  LYS   A CE    1 
ATOM   79   N  NZ    . LYS   A 1 10  ? 14.417  4.582   27.579 1.00 49.27 ? 36  LYS   A NZ    1 
ATOM   80   N  N     . HIS   A 1 11  ? 19.223  0.592   28.013 1.00 23.02 ? 37  HIS   A N     1 
ATOM   81   C  CA    . HIS   A 1 11  ? 19.587  -0.748  27.582 1.00 22.12 ? 37  HIS   A CA    1 
ATOM   82   C  C     . HIS   A 1 11  ? 18.533  -1.197  26.605 1.00 22.28 ? 37  HIS   A C     1 
ATOM   83   O  O     . HIS   A 1 11  ? 17.446  -1.627  27.014 1.00 22.22 ? 37  HIS   A O     1 
ATOM   84   C  CB    . HIS   A 1 11  ? 19.639  -1.706  28.773 1.00 22.10 ? 37  HIS   A CB    1 
ATOM   85   C  CG    . HIS   A 1 11  ? 20.689  -1.358  29.782 1.00 23.17 ? 37  HIS   A CG    1 
ATOM   86   N  ND1   . HIS   A 1 11  ? 20.494  -0.356  30.711 1.00 24.27 ? 37  HIS   A ND1   1 
ATOM   87   C  CD2   . HIS   A 1 11  ? 21.907  -1.910  29.987 1.00 23.63 ? 37  HIS   A CD2   1 
ATOM   88   C  CE1   . HIS   A 1 11  ? 21.601  -0.314  31.434 1.00 23.75 ? 37  HIS   A CE1   1 
ATOM   89   N  NE2   . HIS   A 1 11  ? 22.468  -1.245  31.051 1.00 23.75 ? 37  HIS   A NE2   1 
ATOM   90   N  N     . PRO   A 1 12  ? 18.816  -1.080  25.297 1.00 22.18 ? 38  PRO   A N     1 
ATOM   91   C  CA    . PRO   A 1 12  ? 17.800  -1.479  24.310 1.00 21.77 ? 38  PRO   A CA    1 
ATOM   92   C  C     . PRO   A 1 12  ? 17.442  -2.958  24.311 1.00 21.07 ? 38  PRO   A C     1 
ATOM   93   O  O     . PRO   A 1 12  ? 18.277  -3.817  24.609 1.00 21.56 ? 38  PRO   A O     1 
ATOM   94   C  CB    . PRO   A 1 12  ? 18.388  -1.046  22.961 1.00 22.90 ? 38  PRO   A CB    1 
ATOM   95   C  CG    . PRO   A 1 12  ? 19.596  -0.152  23.287 1.00 23.72 ? 38  PRO   A CG    1 
ATOM   96   C  CD    . PRO   A 1 12  ? 20.053  -0.562  24.662 1.00 21.92 ? 38  PRO   A CD    1 
ATOM   97   N  N     . LEU   A 1 13  ? 16.188  -3.248  23.943 1.00 19.15 ? 39  LEU   A N     1 
ATOM   98   C  CA    . LEU   A 1 13  ? 15.670  -4.598  23.743 1.00 18.70 ? 39  LEU   A CA    1 
ATOM   99   C  C     . LEU   A 1 13  ? 15.931  -4.952  22.261 1.00 20.59 ? 39  LEU   A C     1 
ATOM   100  O  O     . LEU   A 1 13  ? 16.107  -4.039  21.424 1.00 21.10 ? 39  LEU   A O     1 
ATOM   101  C  CB    . LEU   A 1 13  ? 14.141  -4.636  24.028 1.00 17.16 ? 39  LEU   A CB    1 
ATOM   102  C  CG    . LEU   A 1 13  ? 13.709  -4.216  25.439 1.00 16.64 ? 39  LEU   A CG    1 
ATOM   103  C  CD1   . LEU   A 1 13  ? 12.197  -4.056  25.528 1.00 16.29 ? 39  LEU   A CD1   1 
ATOM   104  C  CD2   . LEU   A 1 13  ? 14.239  -5.193  26.508 1.00 16.47 ? 39  LEU   A CD2   1 
ATOM   105  N  N     . GLN   A 1 14  ? 15.956  -6.254  21.920 1.00 20.63 ? 40  GLN   A N     1 
ATOM   106  C  CA    . GLN   A 1 14  ? 16.182  -6.638  20.526 1.00 21.75 ? 40  GLN   A CA    1 
ATOM   107  C  C     . GLN   A 1 14  ? 15.010  -6.234  19.607 1.00 21.01 ? 40  GLN   A C     1 
ATOM   108  O  O     . GLN   A 1 14  ? 15.219  -6.043  18.423 1.00 21.68 ? 40  GLN   A O     1 
ATOM   109  C  CB    . GLN   A 1 14  ? 16.485  -8.130  20.405 1.00 25.97 ? 40  GLN   A CB    1 
ATOM   110  C  CG    . GLN   A 1 14  ? 17.672  -8.552  21.265 1.00 33.15 ? 40  GLN   A CG    1 
ATOM   111  C  CD    . GLN   A 1 14  ? 18.168  -9.891  20.811 1.00 42.78 ? 40  GLN   A CD    1 
ATOM   112  O  OE1   . GLN   A 1 14  ? 18.358  -10.123 19.613 1.00 46.35 ? 40  GLN   A OE1   1 
ATOM   113  N  NE2   . GLN   A 1 14  ? 18.372  -10.807 21.752 1.00 44.60 ? 40  GLN   A NE2   1 
ATOM   114  N  N     . ASN   A 1 15  ? 13.800  -6.082  20.158 1.00 19.52 ? 41  ASN   A N     1 
ATOM   115  C  CA    . ASN   A 1 15  ? 12.620  -5.689  19.399 1.00 19.13 ? 41  ASN   A CA    1 
ATOM   116  C  C     . ASN   A 1 15  ? 11.877  -4.568  20.114 1.00 18.01 ? 41  ASN   A C     1 
ATOM   117  O  O     . ASN   A 1 15  ? 11.987  -4.414  21.345 1.00 17.50 ? 41  ASN   A O     1 
ATOM   118  C  CB    . ASN   A 1 15  ? 11.664  -6.877  19.276 1.00 20.95 ? 41  ASN   A CB    1 
ATOM   119  C  CG    . ASN   A 1 15  ? 11.996  -7.836  18.173 1.00 25.84 ? 41  ASN   A CG    1 
ATOM   120  O  OD1   . ASN   A 1 15  ? 11.977  -7.482  16.997 1.00 28.03 ? 41  ASN   A OD1   1 
ATOM   121  N  ND2   . ASN   A 1 15  ? 12.308  -9.066  18.533 1.00 26.54 ? 41  ASN   A ND2   1 
ATOM   122  N  N     . ARG   A 1 16  ? 11.058  -3.844  19.363 1.00 17.19 ? 42  ARG   A N     1 
ATOM   123  C  CA    . ARG   A 1 16  ? 10.182  -2.835  19.939 1.00 17.60 ? 42  ARG   A CA    1 
ATOM   124  C  C     . ARG   A 1 16  ? 8.837   -3.522  20.190 1.00 17.10 ? 42  ARG   A C     1 
ATOM   125  O  O     . ARG   A 1 16  ? 8.381   -4.302  19.355 1.00 17.52 ? 42  ARG   A O     1 
ATOM   126  C  CB    . ARG   A 1 16  ? 10.014  -1.642  18.996 1.00 19.35 ? 42  ARG   A CB    1 
ATOM   127  C  CG    . ARG   A 1 16  ? 9.130   -0.550  19.586 1.00 24.38 ? 42  ARG   A CG    1 
ATOM   128  C  CD    . ARG   A 1 16  ? 8.862   0.568   18.597 1.00 31.09 ? 42  ARG   A CD    1 
ATOM   129  N  NE    . ARG   A 1 16  ? 9.838   1.642   18.752 1.00 38.06 ? 42  ARG   A NE    1 
ATOM   130  C  CZ    . ARG   A 1 16  ? 10.899  1.812   17.968 1.00 44.20 ? 42  ARG   A CZ    1 
ATOM   131  N  NH1   . ARG   A 1 16  ? 11.121  0.988   16.948 1.00 44.65 ? 42  ARG   A NH1   1 
ATOM   132  N  NH2   . ARG   A 1 16  ? 11.746  2.812   18.192 1.00 45.38 ? 42  ARG   A NH2   1 
ATOM   133  N  N     . TRP   A 1 17  ? 8.214   -3.252  21.339 1.00 15.86 ? 43  TRP   A N     1 
ATOM   134  C  CA    . TRP   A 1 17  ? 6.981   -3.911  21.730 1.00 15.65 ? 43  TRP   A CA    1 
ATOM   135  C  C     . TRP   A 1 17  ? 5.904   -2.913  22.028 1.00 16.58 ? 43  TRP   A C     1 
ATOM   136  O  O     . TRP   A 1 17  ? 6.201   -1.769  22.380 1.00 17.26 ? 43  TRP   A O     1 
ATOM   137  C  CB    . TRP   A 1 17  ? 7.222   -4.766  22.988 1.00 15.00 ? 43  TRP   A CB    1 
ATOM   138  C  CG    . TRP   A 1 17  ? 8.226   -5.852  22.773 1.00 14.15 ? 43  TRP   A CG    1 
ATOM   139  C  CD1   . TRP   A 1 17  ? 9.581   -5.765  22.914 1.00 14.37 ? 43  TRP   A CD1   1 
ATOM   140  C  CD2   . TRP   A 1 17  ? 7.950   -7.188  22.354 1.00 13.43 ? 43  TRP   A CD2   1 
ATOM   141  N  NE1   . TRP   A 1 17  ? 10.166  -6.956  22.567 1.00 14.28 ? 43  TRP   A NE1   1 
ATOM   142  C  CE2   . TRP   A 1 17  ? 9.183   -7.860  22.255 1.00 13.76 ? 43  TRP   A CE2   1 
ATOM   143  C  CE3   . TRP   A 1 17  ? 6.772   -7.887  22.063 1.00 13.75 ? 43  TRP   A CE3   1 
ATOM   144  C  CZ2   . TRP   A 1 17  ? 9.274   -9.185  21.842 1.00 14.45 ? 43  TRP   A CZ2   1 
ATOM   145  C  CZ3   . TRP   A 1 17  ? 6.864   -9.207  21.674 1.00 14.75 ? 43  TRP   A CZ3   1 
ATOM   146  C  CH2   . TRP   A 1 17  ? 8.097   -9.842  21.556 1.00 14.55 ? 43  TRP   A CH2   1 
ATOM   147  N  N     . ALA   A 1 18  ? 4.652   -3.343  21.928 1.00 15.97 ? 44  ALA   A N     1 
ATOM   148  C  CA    . ALA   A 1 18  ? 3.544   -2.485  22.260 1.00 16.60 ? 44  ALA   A CA    1 
ATOM   149  C  C     . ALA   A 1 18  ? 2.602   -3.204  23.192 1.00 17.55 ? 44  ALA   A C     1 
ATOM   150  O  O     . ALA   A 1 18  ? 2.287   -4.380  22.993 1.00 17.19 ? 44  ALA   A O     1 
ATOM   151  C  CB    . ALA   A 1 18  ? 2.811   -2.047  20.998 1.00 16.92 ? 44  ALA   A CB    1 
ATOM   152  N  N     . LEU   A 1 19  ? 2.115   -2.481  24.192 1.00 18.36 ? 45  LEU   A N     1 
ATOM   153  C  CA    . LEU   A 1 19  ? 1.151   -3.033  25.126 1.00 19.39 ? 45  LEU   A CA    1 
ATOM   154  C  C     . LEU   A 1 19  ? -0.233  -2.606  24.662 1.00 18.86 ? 45  LEU   A C     1 
ATOM   155  O  O     . LEU   A 1 19  ? -0.460  -1.439  24.373 1.00 18.68 ? 45  LEU   A O     1 
ATOM   156  C  CB    . LEU   A 1 19  ? 1.414   -2.527  26.552 1.00 19.94 ? 45  LEU   A CB    1 
ATOM   157  C  CG    . LEU   A 1 19  ? 0.386   -2.991  27.593 1.00 21.50 ? 45  LEU   A CG    1 
ATOM   158  C  CD1   . LEU   A 1 19  ? 0.601   -4.450  27.941 1.00 21.33 ? 45  LEU   A CD1   1 
ATOM   159  C  CD2   . LEU   A 1 19  ? 0.467   -2.131  28.852 1.00 22.77 ? 45  LEU   A CD2   1 
ATOM   160  N  N     . TRP   A 1 20  ? -1.135  -3.554  24.554 1.00 18.31 ? 46  TRP   A N     1 
ATOM   161  C  CA    . TRP   A 1 20  ? -2.497  -3.301  24.142 1.00 19.10 ? 46  TRP   A CA    1 
ATOM   162  C  C     . TRP   A 1 20  ? -3.424  -3.657  25.288 1.00 19.58 ? 46  TRP   A C     1 
ATOM   163  O  O     . TRP   A 1 20  ? -3.082  -4.454  26.173 1.00 19.19 ? 46  TRP   A O     1 
ATOM   164  C  CB    . TRP   A 1 20  ? -2.884  -4.114  22.878 1.00 19.01 ? 46  TRP   A CB    1 
ATOM   165  C  CG    . TRP   A 1 20  ? -2.096  -3.794  21.638 1.00 19.82 ? 46  TRP   A CG    1 
ATOM   166  C  CD1   . TRP   A 1 20  ? -0.795  -4.128  21.383 1.00 20.53 ? 46  TRP   A CD1   1 
ATOM   167  C  CD2   . TRP   A 1 20  ? -2.582  -3.143  20.451 1.00 19.79 ? 46  TRP   A CD2   1 
ATOM   168  N  NE1   . TRP   A 1 20  ? -0.439  -3.711  20.121 1.00 20.65 ? 46  TRP   A NE1   1 
ATOM   169  C  CE2   . TRP   A 1 20  ? -1.517  -3.106  19.527 1.00 20.71 ? 46  TRP   A CE2   1 
ATOM   170  C  CE3   . TRP   A 1 20  ? -3.818  -2.615  20.072 1.00 20.75 ? 46  TRP   A CE3   1 
ATOM   171  C  CZ2   . TRP   A 1 20  ? -1.650  -2.543  18.251 1.00 21.50 ? 46  TRP   A CZ2   1 
ATOM   172  C  CZ3   . TRP   A 1 20  ? -3.954  -2.077  18.800 1.00 22.28 ? 46  TRP   A CZ3   1 
ATOM   173  C  CH2   . TRP   A 1 20  ? -2.869  -2.019  17.919 1.00 22.05 ? 46  TRP   A CH2   1 
ATOM   174  N  N     . PHE   A 1 21  ? -4.591  -3.037  25.284 1.00 20.30 ? 47  PHE   A N     1 
ATOM   175  C  CA    . PHE   A 1 21  ? -5.607  -3.281  26.275 1.00 22.45 ? 47  PHE   A CA    1 
ATOM   176  C  C     . PHE   A 1 21  ? -6.942  -3.456  25.593 1.00 23.26 ? 47  PHE   A C     1 
ATOM   177  O  O     . PHE   A 1 21  ? -7.263  -2.778  24.616 1.00 23.18 ? 47  PHE   A O     1 
ATOM   178  C  CB    . PHE   A 1 21  ? -5.661  -2.148  27.309 1.00 23.76 ? 47  PHE   A CB    1 
ATOM   179  C  CG    . PHE   A 1 21  ? -6.796  -2.256  28.301 1.00 25.95 ? 47  PHE   A CG    1 
ATOM   180  C  CD1   . PHE   A 1 21  ? -6.759  -3.188  29.322 1.00 27.12 ? 47  PHE   A CD1   1 
ATOM   181  C  CD2   . PHE   A 1 21  ? -7.879  -1.399  28.235 1.00 27.57 ? 47  PHE   A CD2   1 
ATOM   182  C  CE1   . PHE   A 1 21  ? -7.811  -3.303  30.217 1.00 28.16 ? 47  PHE   A CE1   1 
ATOM   183  C  CE2   . PHE   A 1 21  ? -8.905  -1.482  29.166 1.00 28.90 ? 47  PHE   A CE2   1 
ATOM   184  C  CZ    . PHE   A 1 21  ? -8.860  -2.430  30.158 1.00 28.44 ? 47  PHE   A CZ    1 
ATOM   185  N  N     . PHE   A 1 22  ? -7.715  -4.396  26.103 1.00 23.64 ? 48  PHE   A N     1 
ATOM   186  C  CA    . PHE   A 1 22  ? -9.043  -4.648  25.606 1.00 24.78 ? 48  PHE   A CA    1 
ATOM   187  C  C     . PHE   A 1 22  ? -9.981  -4.489  26.782 1.00 27.54 ? 48  PHE   A C     1 
ATOM   188  O  O     . PHE   A 1 22  ? -9.753  -5.056  27.844 1.00 27.93 ? 48  PHE   A O     1 
ATOM   189  C  CB    . PHE   A 1 22  ? -9.158  -6.064  25.029 1.00 23.87 ? 48  PHE   A CB    1 
ATOM   190  C  CG    . PHE   A 1 22  ? -10.537 -6.379  24.507 1.00 24.44 ? 48  PHE   A CG    1 
ATOM   191  C  CD1   . PHE   A 1 22  ? -11.522 -6.860  25.351 1.00 25.19 ? 48  PHE   A CD1   1 
ATOM   192  C  CD2   . PHE   A 1 22  ? -10.839 -6.226  23.167 1.00 25.02 ? 48  PHE   A CD2   1 
ATOM   193  C  CE1   . PHE   A 1 22  ? -12.803 -7.111  24.874 1.00 26.21 ? 48  PHE   A CE1   1 
ATOM   194  C  CE2   . PHE   A 1 22  ? -12.104 -6.535  22.686 1.00 25.67 ? 48  PHE   A CE2   1 
ATOM   195  C  CZ    . PHE   A 1 22  ? -13.086 -6.949  23.545 1.00 25.62 ? 48  PHE   A CZ    1 
ATOM   196  N  N     . LYS   A 1 23  ? -11.021 -3.724  26.591 1.00 29.43 ? 49  LYS   A N     1 
ATOM   197  C  CA    . LYS   A 1 23  ? -12.068 -3.515  27.573 1.00 32.12 ? 49  LYS   A CA    1 
ATOM   198  C  C     . LYS   A 1 23  ? -13.362 -3.900  26.881 1.00 33.67 ? 49  LYS   A C     1 
ATOM   199  O  O     . LYS   A 1 23  ? -13.540 -3.549  25.710 1.00 34.08 ? 49  LYS   A O     1 
ATOM   200  C  CB    . LYS   A 1 23  ? -12.101 -2.023  27.955 1.00 35.78 ? 49  LYS   A CB    1 
ATOM   201  C  CG    . LYS   A 1 23  ? -13.367 -1.535  28.644 1.00 41.83 ? 49  LYS   A CG    1 
ATOM   202  C  CD    . LYS   A 1 23  ? -13.543 -0.030  28.468 1.00 46.84 ? 49  LYS   A CD    1 
ATOM   203  C  CE    . LYS   A 1 23  ? -14.821 0.424   29.122 1.00 50.91 ? 49  LYS   A CE    1 
ATOM   204  N  NZ    . LYS   A 1 23  ? -15.245 1.788   28.693 1.00 53.33 ? 49  LYS   A NZ    1 
ATOM   205  N  N     . ASN   A 1 24  ? -14.273 -4.591  27.581 1.00 34.43 ? 50  ASN   A N     1 
ATOM   206  C  CA    . ASN   A 1 24  ? -15.556 -4.898  26.974 1.00 35.95 ? 50  ASN   A CA    1 
ATOM   207  C  C     . ASN   A 1 24  ? -16.528 -3.713  27.029 1.00 35.43 ? 50  ASN   A C     1 
ATOM   208  O  O     . ASN   A 1 24  ? -17.542 -3.783  27.708 1.00 35.63 ? 50  ASN   A O     1 
ATOM   209  C  CB    . ASN   A 1 24  ? -16.183 -6.167  27.518 1.00 39.01 ? 50  ASN   A CB    1 
ATOM   210  C  CG    . ASN   A 1 24  ? -16.807 -6.951  26.401 1.00 44.18 ? 50  ASN   A CG    1 
ATOM   211  O  OD1   . ASN   A 1 24  ? -17.601 -6.419  25.594 1.00 45.55 ? 50  ASN   A OD1   1 
ATOM   212  N  ND2   . ASN   A 1 24  ? -16.422 -8.217  26.302 1.00 45.40 ? 50  ASN   A ND2   1 
ATOM   213  N  N     . ASP   A 1 25  ? -16.222 -2.628  26.306 1.00 34.46 ? 51  ASP   A N     1 
ATOM   214  C  CA    . ASP   A 1 25  ? -17.127 -1.485  26.223 1.00 33.86 ? 51  ASP   A CA    1 
ATOM   215  C  C     . ASP   A 1 25  ? -18.214 -1.895  25.221 1.00 33.99 ? 51  ASP   A C     1 
ATOM   216  O  O     . ASP   A 1 25  ? -17.955 -1.949  24.020 1.00 34.06 ? 51  ASP   A O     1 
ATOM   217  C  CB    . ASP   A 1 25  ? -16.370 -0.220  25.770 1.00 33.90 ? 51  ASP   A CB    1 
ATOM   218  C  CG    . ASP   A 1 25  ? -17.233 1.021   25.605 1.00 36.34 ? 51  ASP   A CG    1 
ATOM   219  O  OD1   . ASP   A 1 25  ? -18.471 0.877   25.492 1.00 36.06 ? 51  ASP   A OD1   1 
ATOM   220  O  OD2   . ASP   A 1 25  ? -16.671 2.129   25.564 1.00 37.51 ? 51  ASP   A OD2   1 
ATOM   221  N  N     . LYS   A 1 26  ? -19.427 -2.181  25.720 1.00 33.89 ? 52  LYS   A N     1 
ATOM   222  C  CA    . LYS   A 1 26  ? -20.564 -2.670  24.939 1.00 34.45 ? 52  LYS   A CA    1 
ATOM   223  C  C     . LYS   A 1 26  ? -21.086 -1.688  23.879 1.00 34.91 ? 52  LYS   A C     1 
ATOM   224  O  O     . LYS   A 1 26  ? -21.901 -2.087  23.044 1.00 35.08 ? 52  LYS   A O     1 
ATOM   225  C  CB    . LYS   A 1 26  ? -21.714 -3.140  25.853 1.00 36.79 ? 52  LYS   A CB    1 
ATOM   226  C  CG    . LYS   A 1 26  ? -21.268 -3.936  27.083 1.00 42.09 ? 52  LYS   A CG    1 
ATOM   227  C  CD    . LYS   A 1 26  ? -21.491 -5.434  26.950 1.00 47.12 ? 52  LYS   A CD    1 
ATOM   228  C  CE    . LYS   A 1 26  ? -22.153 -6.015  28.179 1.00 50.79 ? 52  LYS   A CE    1 
ATOM   229  N  NZ    . LYS   A 1 26  ? -21.335 -5.837  29.409 1.00 52.92 ? 52  LYS   A NZ    1 
ATOM   230  N  N     . SER   A 1 27  ? -20.642 -0.420  23.901 1.00 34.83 ? 53  SER   A N     1 
ATOM   231  C  CA    . SER   A 1 27  ? -21.047 0.526   22.849 1.00 35.17 ? 53  SER   A CA    1 
ATOM   232  C  C     . SER   A 1 27  ? -20.148 0.404   21.594 1.00 35.07 ? 53  SER   A C     1 
ATOM   233  O  O     . SER   A 1 27  ? -20.463 0.988   20.562 1.00 35.08 ? 53  SER   A O     1 
ATOM   234  C  CB    . SER   A 1 27  ? -21.051 1.963   23.361 1.00 37.07 ? 53  SER   A CB    1 
ATOM   235  O  OG    . SER   A 1 27  ? -19.763 2.375   23.791 1.00 39.96 ? 53  SER   A OG    1 
ATOM   236  N  N     . LYS   A 1 28  ? -19.027 -0.345  21.681 1.00 34.62 ? 54  LYS   A N     1 
ATOM   237  C  CA    . LYS   A 1 28  ? -18.125 -0.530  20.560 1.00 34.49 ? 54  LYS   A CA    1 
ATOM   238  C  C     . LYS   A 1 28  ? -18.018 -2.008  20.153 1.00 34.29 ? 54  LYS   A C     1 
ATOM   239  O  O     . LYS   A 1 28  ? -18.243 -2.913  20.956 1.00 34.86 ? 54  LYS   A O     1 
ATOM   240  C  CB    . LYS   A 1 28  ? -16.728 -0.004  20.912 1.00 36.12 ? 54  LYS   A CB    1 
ATOM   241  C  CG    . LYS   A 1 28  ? -16.698 1.410   21.469 1.00 40.10 ? 54  LYS   A CG    1 
ATOM   242  C  CD    . LYS   A 1 28  ? -15.445 1.578   22.292 1.00 44.34 ? 54  LYS   A CD    1 
ATOM   243  C  CE    . LYS   A 1 28  ? -15.171 2.992   22.727 1.00 48.81 ? 54  LYS   A CE    1 
ATOM   244  N  NZ    . LYS   A 1 28  ? -14.039 3.034   23.694 1.00 51.01 ? 54  LYS   A NZ    1 
ATOM   245  N  N     . THR   A 1 29  ? -17.616 -2.249  18.915 1.00 33.20 ? 55  THR   A N     1 
ATOM   246  C  CA    . THR   A 1 29  ? -17.404 -3.597  18.404 1.00 32.58 ? 55  THR   A CA    1 
ATOM   247  C  C     . THR   A 1 29  ? -16.070 -4.152  18.969 1.00 30.07 ? 55  THR   A C     1 
ATOM   248  O  O     . THR   A 1 29  ? -15.274 -3.400  19.535 1.00 29.98 ? 55  THR   A O     1 
ATOM   249  C  CB    . THR   A 1 29  ? -17.350 -3.511  16.893 1.00 35.40 ? 55  THR   A CB    1 
ATOM   250  O  OG1   . THR   A 1 29  ? -17.249 -4.829  16.356 1.00 38.44 ? 55  THR   A OG1   1 
ATOM   251  C  CG2   . THR   A 1 29  ? -16.183 -2.698  16.446 1.00 35.15 ? 55  THR   A CG2   1 
ATOM   252  N  N     . TRP   A 1 30  ? -15.815 -5.458  18.807 1.00 28.06 ? 56  TRP   A N     1 
ATOM   253  C  CA    . TRP   A 1 30  ? -14.591 -6.098  19.290 1.00 26.63 ? 56  TRP   A CA    1 
ATOM   254  C  C     . TRP   A 1 30  ? -13.325 -5.357  18.877 1.00 25.35 ? 56  TRP   A C     1 
ATOM   255  O  O     . TRP   A 1 30  ? -12.516 -5.019  19.735 1.00 25.58 ? 56  TRP   A O     1 
ATOM   256  C  CB    . TRP   A 1 30  ? -14.517 -7.589  18.871 1.00 26.25 ? 56  TRP   A CB    1 
ATOM   257  C  CG    . TRP   A 1 30  ? -13.447 -8.341  19.608 1.00 26.60 ? 56  TRP   A CG    1 
ATOM   258  C  CD1   . TRP   A 1 30  ? -13.583 -8.988  20.798 1.00 27.48 ? 56  TRP   A CD1   1 
ATOM   259  C  CD2   . TRP   A 1 30  ? -12.051 -8.426  19.262 1.00 26.72 ? 56  TRP   A CD2   1 
ATOM   260  N  NE1   . TRP   A 1 30  ? -12.353 -9.410  21.250 1.00 27.81 ? 56  TRP   A NE1   1 
ATOM   261  C  CE2   . TRP   A 1 30  ? -11.406 -9.131  20.296 1.00 27.46 ? 56  TRP   A CE2   1 
ATOM   262  C  CE3   . TRP   A 1 30  ? -11.290 -7.995  18.167 1.00 27.49 ? 56  TRP   A CE3   1 
ATOM   263  C  CZ2   . TRP   A 1 30  ? -10.035 -9.379  20.287 1.00 28.00 ? 56  TRP   A CZ2   1 
ATOM   264  C  CZ3   . TRP   A 1 30  ? -9.935  -8.262  18.148 1.00 28.09 ? 56  TRP   A CZ3   1 
ATOM   265  C  CH2   . TRP   A 1 30  ? -9.319  -8.934  19.205 1.00 28.20 ? 56  TRP   A CH2   1 
ATOM   266  N  N     . GLN   A 1 31  ? -13.159 -5.081  17.574 1.00 23.82 ? 57  GLN   A N     1 
ATOM   267  C  CA    . GLN   A 1 31  ? -11.962 -4.413  17.087 1.00 23.27 ? 57  GLN   A CA    1 
ATOM   268  C  C     . GLN   A 1 31  ? -11.791 -2.994  17.603 1.00 22.62 ? 57  GLN   A C     1 
ATOM   269  O  O     . GLN   A 1 31  ? -10.667 -2.595  17.887 1.00 22.18 ? 57  GLN   A O     1 
ATOM   270  C  CB    . GLN   A 1 31  ? -11.891 -4.451  15.550 1.00 24.89 ? 57  GLN   A CB    1 
ATOM   271  C  CG    . GLN   A 1 31  ? -11.311 -5.761  15.000 1.00 27.14 ? 57  GLN   A CG    1 
ATOM   272  C  CD    . GLN   A 1 31  ? -11.057 -5.639  13.514 1.00 30.32 ? 57  GLN   A CD    1 
ATOM   273  O  OE1   . GLN   A 1 31  ? -10.465 -4.666  13.037 1.00 32.66 ? 57  GLN   A OE1   1 
ATOM   274  N  NE2   . GLN   A 1 31  ? -11.510 -6.599  12.754 1.00 30.18 ? 57  GLN   A NE2   1 
ATOM   275  N  N     . ALA   A 1 32  ? -12.888 -2.243  17.764 1.00 22.65 ? 58  ALA   A N     1 
ATOM   276  C  CA    . ALA   A 1 32  ? -12.802 -0.880  18.282 1.00 23.46 ? 58  ALA   A CA    1 
ATOM   277  C  C     . ALA   A 1 32  ? -12.367 -0.854  19.771 1.00 24.39 ? 58  ALA   A C     1 
ATOM   278  O  O     . ALA   A 1 32  ? -11.694 0.087   20.194 1.00 25.50 ? 58  ALA   A O     1 
ATOM   279  C  CB    . ALA   A 1 32  ? -14.123 -0.171  18.106 1.00 23.60 ? 58  ALA   A CB    1 
ATOM   280  N  N     . ASN   A 1 33  ? -12.662 -1.937  20.515 1.00 23.18 ? 59  ASN   A N     1 
ATOM   281  C  CA    . ASN   A 1 33  ? -12.336 -2.141  21.925 1.00 22.90 ? 59  ASN   A CA    1 
ATOM   282  C  C     . ASN   A 1 33  ? -10.880 -2.561  22.185 1.00 23.07 ? 59  ASN   A C     1 
ATOM   283  O  O     . ASN   A 1 33  ? -10.450 -2.573  23.337 1.00 22.16 ? 59  ASN   A O     1 
ATOM   284  C  CB    . ASN   A 1 33  ? -13.293 -3.191  22.486 1.00 23.57 ? 59  ASN   A CB    1 
ATOM   285  C  CG    . ASN   A 1 33  ? -14.593 -2.575  22.935 1.00 26.50 ? 59  ASN   A CG    1 
ATOM   286  O  OD1   . ASN   A 1 33  ? -14.610 -1.460  23.460 1.00 29.26 ? 59  ASN   A OD1   1 
ATOM   287  N  ND2   . ASN   A 1 33  ? -15.688 -3.273  22.775 1.00 24.66 ? 59  ASN   A ND2   1 
ATOM   288  N  N     . LEU   A 1 34  ? -10.133 -2.924  21.131 1.00 23.54 ? 60  LEU   A N     1 
ATOM   289  C  CA    . LEU   A 1 34  ? -8.735  -3.359  21.238 1.00 25.32 ? 60  LEU   A CA    1 
ATOM   290  C  C     . LEU   A 1 34  ? -7.836  -2.161  20.977 1.00 27.29 ? 60  LEU   A C     1 
ATOM   291  O  O     . LEU   A 1 34  ? -7.711  -1.763  19.818 1.00 28.67 ? 60  LEU   A O     1 
ATOM   292  C  CB    . LEU   A 1 34  ? -8.476  -4.419  20.171 1.00 25.64 ? 60  LEU   A CB    1 
ATOM   293  C  CG    . LEU   A 1 34  ? -7.083  -4.997  20.128 1.00 27.50 ? 60  LEU   A CG    1 
ATOM   294  C  CD1   . LEU   A 1 34  ? -6.747  -5.696  21.436 1.00 27.48 ? 60  LEU   A CD1   1 
ATOM   295  C  CD2   . LEU   A 1 34  ? -6.918  -5.912  18.905 1.00 28.06 ? 60  LEU   A CD2   1 
ATOM   296  N  N     . ARG   A 1 35  ? -7.249  -1.552  22.037 1.00 27.05 ? 61  ARG   A N     1 
ATOM   297  C  CA    . ARG   A 1 35  ? -6.490  -0.306  21.900 1.00 27.52 ? 61  ARG   A CA    1 
ATOM   298  C  C     . ARG   A 1 35  ? -5.013  -0.312  22.355 1.00 26.51 ? 61  ARG   A C     1 
ATOM   299  O  O     . ARG   A 1 35  ? -4.646  -0.957  23.322 1.00 25.42 ? 61  ARG   A O     1 
ATOM   300  C  CB    . ARG   A 1 35  ? -7.227  0.805   22.638 1.00 30.09 ? 61  ARG   A CB    1 
ATOM   301  C  CG    . ARG   A 1 35  ? -8.582  1.128   22.001 1.00 35.44 ? 61  ARG   A CG    1 
ATOM   302  C  CD    . ARG   A 1 35  ? -9.297  2.263   22.699 1.00 38.98 ? 61  ARG   A CD    1 
ATOM   303  N  NE    . ARG   A 1 35  ? -10.318 1.762   23.617 1.00 44.18 ? 61  ARG   A NE    1 
ATOM   304  C  CZ    . ARG   A 1 35  ? -11.589 1.549   23.283 1.00 46.44 ? 61  ARG   A CZ    1 
ATOM   305  N  NH1   . ARG   A 1 35  ? -12.008 1.795   22.049 1.00 45.53 ? 61  ARG   A NH1   1 
ATOM   306  N  NH2   . ARG   A 1 35  ? -12.451 1.091   24.183 1.00 46.17 ? 61  ARG   A NH2   1 
ATOM   307  N  N     . LEU   A 1 36  ? -4.194  0.475   21.666 1.00 26.26 ? 62  LEU   A N     1 
ATOM   308  C  CA    . LEU   A 1 36  ? -2.767  0.607   21.923 1.00 26.63 ? 62  LEU   A CA    1 
ATOM   309  C  C     . LEU   A 1 36  ? -2.498  1.535   23.102 1.00 26.22 ? 62  LEU   A C     1 
ATOM   310  O  O     . LEU   A 1 36  ? -2.879  2.700   23.062 1.00 26.05 ? 62  LEU   A O     1 
ATOM   311  C  CB    . LEU   A 1 36  ? -2.086  1.151   20.662 1.00 27.30 ? 62  LEU   A CB    1 
ATOM   312  C  CG    . LEU   A 1 36  ? -0.576  1.374   20.794 1.00 29.10 ? 62  LEU   A CG    1 
ATOM   313  C  CD1   . LEU   A 1 36  ? 0.118   0.085   20.914 1.00 28.78 ? 62  LEU   A CD1   1 
ATOM   314  C  CD2   . LEU   A 1 36  ? -0.042  2.144   19.599 1.00 30.00 ? 62  LEU   A CD2   1 
ATOM   315  N  N     . ILE   A 1 37  ? -1.865  1.017   24.163 1.00 25.74 ? 63  ILE   A N     1 
ATOM   316  C  CA    . ILE   A 1 37  ? -1.552  1.823   25.335 1.00 25.99 ? 63  ILE   A CA    1 
ATOM   317  C  C     . ILE   A 1 37  ? -0.229  2.557   25.163 1.00 26.05 ? 63  ILE   A C     1 
ATOM   318  O  O     . ILE   A 1 37  ? -0.179  3.771   25.347 1.00 27.00 ? 63  ILE   A O     1 
ATOM   319  C  CB    . ILE   A 1 37  ? -1.590  0.981   26.639 1.00 26.74 ? 63  ILE   A CB    1 
ATOM   320  C  CG1   . ILE   A 1 37  ? -2.996  0.375   26.888 1.00 27.71 ? 63  ILE   A CG1   1 
ATOM   321  C  CG2   . ILE   A 1 37  ? -1.125  1.808   27.825 1.00 27.45 ? 63  ILE   A CG2   1 
ATOM   322  C  CD1   . ILE   A 1 37  ? -4.269  1.291   26.495 1.00 28.87 ? 63  ILE   A CD1   1 
ATOM   323  N  N     . SER   A 1 38  ? 0.840   1.837   24.827 1.00 25.10 ? 64  SER   A N     1 
ATOM   324  C  CA    . SER   A 1 38  ? 2.153   2.459   24.645 1.00 25.63 ? 64  SER   A CA    1 
ATOM   325  C  C     . SER   A 1 38  ? 3.157   1.493   24.048 1.00 24.56 ? 64  SER   A C     1 
ATOM   326  O  O     . SER   A 1 38  ? 2.906   0.292   23.995 1.00 24.85 ? 64  SER   A O     1 
ATOM   327  C  CB    . SER   A 1 38  ? 2.696   3.015   25.965 1.00 28.49 ? 64  SER   A CB    1 
ATOM   328  O  OG    . SER   A 1 38  ? 2.673   2.023   26.973 1.00 32.83 ? 64  SER   A OG    1 
ATOM   329  N  N     . LYS   A 1 39  ? 4.267   2.031   23.540 1.00 23.15 ? 65  LYS   A N     1 
ATOM   330  C  CA    . LYS   A 1 39  ? 5.344   1.255   22.972 1.00 22.70 ? 65  LYS   A CA    1 
ATOM   331  C  C     . LYS   A 1 39  ? 6.621   1.488   23.793 1.00 22.42 ? 65  LYS   A C     1 
ATOM   332  O  O     . LYS   A 1 39  ? 6.780   2.520   24.443 1.00 23.00 ? 65  LYS   A O     1 
ATOM   333  C  CB    . LYS   A 1 39  ? 5.576   1.632   21.503 1.00 24.10 ? 65  LYS   A CB    1 
ATOM   334  C  CG    . LYS   A 1 39  ? 4.320   1.473   20.642 1.00 28.13 ? 65  LYS   A CG    1 
ATOM   335  C  CD    . LYS   A 1 39  ? 4.558   1.763   19.160 1.00 31.91 ? 65  LYS   A CD    1 
ATOM   336  C  CE    . LYS   A 1 39  ? 3.348   1.366   18.339 1.00 36.09 ? 65  LYS   A CE    1 
ATOM   337  N  NZ    . LYS   A 1 39  ? 3.577   1.556   16.878 1.00 38.07 ? 65  LYS   A NZ    1 
ATOM   338  N  N     . PHE   A 1 40  ? 7.522   0.528   23.753 1.00 21.24 ? 66  PHE   A N     1 
ATOM   339  C  CA    . PHE   A 1 40  ? 8.795   0.629   24.443 1.00 20.46 ? 66  PHE   A CA    1 
ATOM   340  C  C     . PHE   A 1 40  ? 9.819   -0.226  23.707 1.00 20.73 ? 66  PHE   A C     1 
ATOM   341  O  O     . PHE   A 1 40  ? 9.465   -1.227  23.075 1.00 20.83 ? 66  PHE   A O     1 
ATOM   342  C  CB    . PHE   A 1 40  ? 8.672   0.226   25.924 1.00 19.34 ? 66  PHE   A CB    1 
ATOM   343  C  CG    . PHE   A 1 40  ? 8.210   -1.190  26.151 1.00 19.69 ? 66  PHE   A CG    1 
ATOM   344  C  CD1   . PHE   A 1 40  ? 9.122   -2.224  26.269 1.00 20.28 ? 66  PHE   A CD1   1 
ATOM   345  C  CD2   . PHE   A 1 40  ? 6.863   -1.488  26.257 1.00 19.99 ? 66  PHE   A CD2   1 
ATOM   346  C  CE1   . PHE   A 1 40  ? 8.698   -3.526  26.449 1.00 20.78 ? 66  PHE   A CE1   1 
ATOM   347  C  CE2   . PHE   A 1 40  ? 6.441   -2.789  26.453 1.00 20.36 ? 66  PHE   A CE2   1 
ATOM   348  C  CZ    . PHE   A 1 40  ? 7.358   -3.799  26.559 1.00 20.63 ? 66  PHE   A CZ    1 
ATOM   349  N  N     . ASP   A 1 41  ? 11.087  0.169   23.781 1.00 20.22 ? 67  ASP   A N     1 
ATOM   350  C  CA    . ASP   A 1 41  ? 12.152  -0.601  23.171 1.00 20.27 ? 67  ASP   A CA    1 
ATOM   351  C  C     . ASP   A 1 41  ? 13.407  -0.684  24.062 1.00 18.79 ? 67  ASP   A C     1 
ATOM   352  O  O     . ASP   A 1 41  ? 14.462  -1.048  23.557 1.00 18.40 ? 67  ASP   A O     1 
ATOM   353  C  CB    . ASP   A 1 41  ? 12.471  -0.098  21.755 1.00 23.61 ? 67  ASP   A CB    1 
ATOM   354  C  CG    . ASP   A 1 41  ? 13.030  1.314   21.681 1.00 31.37 ? 67  ASP   A CG    1 
ATOM   355  O  OD1   . ASP   A 1 41  ? 13.220  1.939   22.749 1.00 32.99 ? 67  ASP   A OD1   1 
ATOM   356  O  OD2   . ASP   A 1 41  ? 13.290  1.791   20.553 1.00 35.34 ? 67  ASP   A OD2   1 
ATOM   357  N  N     . THR   A 1 42  ? 13.295  -0.355  25.372 1.00 17.78 ? 68  THR   A N     1 
ATOM   358  C  CA    . THR   A 1 42  ? 14.383  -0.467  26.349 1.00 17.88 ? 68  THR   A CA    1 
ATOM   359  C  C     . THR   A 1 42  ? 13.900  -1.170  27.646 1.00 17.11 ? 68  THR   A C     1 
ATOM   360  O  O     . THR   A 1 42  ? 12.698  -1.205  27.941 1.00 16.32 ? 68  THR   A O     1 
ATOM   361  C  CB    . THR   A 1 42  ? 15.012  0.911   26.688 1.00 19.74 ? 68  THR   A CB    1 
ATOM   362  O  OG1   . THR   A 1 42  ? 14.083  1.678   27.454 1.00 21.66 ? 68  THR   A OG1   1 
ATOM   363  C  CG2   . THR   A 1 42  ? 15.468  1.698   25.447 1.00 19.82 ? 68  THR   A CG2   1 
ATOM   364  N  N     . VAL   A 1 43  ? 14.851  -1.723  28.412 1.00 16.57 ? 69  VAL   A N     1 
ATOM   365  C  CA    . VAL   A 1 43  ? 14.602  -2.354  29.709 1.00 16.34 ? 69  VAL   A CA    1 
ATOM   366  C  C     . VAL   A 1 43  ? 13.987  -1.313  30.682 1.00 16.08 ? 69  VAL   A C     1 
ATOM   367  O  O     . VAL   A 1 43  ? 12.969  -1.592  31.315 1.00 15.64 ? 69  VAL   A O     1 
ATOM   368  C  CB    . VAL   A 1 43  ? 15.941  -2.907  30.260 1.00 16.72 ? 69  VAL   A CB    1 
ATOM   369  C  CG1   . VAL   A 1 43  ? 15.805  -3.320  31.716 1.00 17.15 ? 69  VAL   A CG1   1 
ATOM   370  C  CG2   . VAL   A 1 43  ? 16.452  -4.078  29.396 1.00 16.90 ? 69  VAL   A CG2   1 
ATOM   371  N  N     . GLU   A 1 44  ? 14.576  -0.097  30.739 1.00 16.10 ? 70  GLU   A N     1 
ATOM   372  C  CA    . GLU   A 1 44  ? 14.115  0.988   31.610 1.00 17.26 ? 70  GLU   A CA    1 
ATOM   373  C  C     . GLU   A 1 44  ? 12.654  1.347   31.323 1.00 17.89 ? 70  GLU   A C     1 
ATOM   374  O  O     . GLU   A 1 44  ? 11.896  1.545   32.260 1.00 18.38 ? 70  GLU   A O     1 
ATOM   375  C  CB    . GLU   A 1 44  ? 14.986  2.261   31.449 1.00 19.80 ? 70  GLU   A CB    1 
ATOM   376  C  CG    . GLU   A 1 44  ? 16.417  2.151   31.984 1.00 24.16 ? 70  GLU   A CG    1 
ATOM   377  C  CD    . GLU   A 1 44  ? 17.368  1.335   31.124 1.00 28.45 ? 70  GLU   A CD    1 
ATOM   378  O  OE1   . GLU   A 1 44  ? 18.498  1.055   31.591 1.00 28.52 ? 70  GLU   A OE1   1 
ATOM   379  O  OE2   . GLU   A 1 44  ? 16.988  0.975   29.982 1.00 28.26 ? 70  GLU   A OE2   1 
ATOM   380  N  N     . ASP   A 1 45  ? 12.265  1.439   30.039 1.00 17.47 ? 71  ASP   A N     1 
ATOM   381  C  CA    . ASP   A 1 45  ? 10.899  1.803   29.694 1.00 17.62 ? 71  ASP   A CA    1 
ATOM   382  C  C     . ASP   A 1 45  ? 9.894   0.651   29.933 1.00 16.95 ? 71  ASP   A C     1 
ATOM   383  O  O     . ASP   A 1 45  ? 8.731   0.914   30.248 1.00 17.55 ? 71  ASP   A O     1 
ATOM   384  C  CB    . ASP   A 1 45  ? 10.817  2.372   28.268 1.00 19.93 ? 71  ASP   A CB    1 
ATOM   385  C  CG    . ASP   A 1 45  ? 11.548  3.710   28.104 1.00 27.96 ? 71  ASP   A CG    1 
ATOM   386  O  OD1   . ASP   A 1 45  ? 11.877  4.338   29.126 1.00 29.74 ? 71  ASP   A OD1   1 
ATOM   387  O  OD2   . ASP   A 1 45  ? 11.772  4.130   26.950 1.00 31.81 ? 71  ASP   A OD2   1 
ATOM   388  N  N     . PHE   A 1 46  ? 10.340  -0.604  29.840 1.00 15.58 ? 72  PHE   A N     1 
ATOM   389  C  CA    . PHE   A 1 46  ? 9.481   -1.763  30.142 1.00 15.15 ? 72  PHE   A CA    1 
ATOM   390  C  C     . PHE   A 1 46  ? 9.138   -1.718  31.620 1.00 14.87 ? 72  PHE   A C     1 
ATOM   391  O  O     . PHE   A 1 46  ? 7.972   -1.859  31.974 1.00 16.40 ? 72  PHE   A O     1 
ATOM   392  C  CB    . PHE   A 1 46  ? 10.157  -3.138  29.790 1.00 14.62 ? 72  PHE   A CB    1 
ATOM   393  C  CG    . PHE   A 1 46  ? 9.447   -4.297  30.466 1.00 15.60 ? 72  PHE   A CG    1 
ATOM   394  C  CD1   . PHE   A 1 46  ? 8.204   -4.714  30.032 1.00 17.33 ? 72  PHE   A CD1   1 
ATOM   395  C  CD2   . PHE   A 1 46  ? 9.948   -4.855  31.635 1.00 16.31 ? 72  PHE   A CD2   1 
ATOM   396  C  CE1   . PHE   A 1 46  ? 7.493   -5.694  30.731 1.00 17.68 ? 72  PHE   A CE1   1 
ATOM   397  C  CE2   . PHE   A 1 46  ? 9.233   -5.830  32.329 1.00 16.88 ? 72  PHE   A CE2   1 
ATOM   398  C  CZ    . PHE   A 1 46  ? 8.021   -6.251  31.866 1.00 16.62 ? 72  PHE   A CZ    1 
ATOM   399  N  N     . TRP   A 1 47  ? 10.144  -1.514  32.479 1.00 13.89 ? 73  TRP   A N     1 
ATOM   400  C  CA    . TRP   A 1 47  ? 9.898   -1.473  33.918 1.00 14.34 ? 73  TRP   A CA    1 
ATOM   401  C  C     . TRP   A 1 47  ? 9.106   -0.250  34.309 1.00 15.53 ? 73  TRP   A C     1 
ATOM   402  O  O     . TRP   A 1 47  ? 8.246   -0.377  35.160 1.00 15.82 ? 73  TRP   A O     1 
ATOM   403  C  CB    . TRP   A 1 47  ? 11.181  -1.644  34.743 1.00 13.92 ? 73  TRP   A CB    1 
ATOM   404  C  CG    . TRP   A 1 47  ? 11.771  -3.029  34.628 1.00 14.74 ? 73  TRP   A CG    1 
ATOM   405  C  CD1   . TRP   A 1 47  ? 12.908  -3.384  33.965 1.00 16.31 ? 73  TRP   A CD1   1 
ATOM   406  C  CD2   . TRP   A 1 47  ? 11.197  -4.247  35.123 1.00 15.44 ? 73  TRP   A CD2   1 
ATOM   407  N  NE1   . TRP   A 1 47  ? 13.114  -4.744  34.066 1.00 16.98 ? 73  TRP   A NE1   1 
ATOM   408  C  CE2   . TRP   A 1 47  ? 12.064  -5.301  34.755 1.00 16.85 ? 73  TRP   A CE2   1 
ATOM   409  C  CE3   . TRP   A 1 47  ? 10.006  -4.558  35.797 1.00 16.42 ? 73  TRP   A CE3   1 
ATOM   410  C  CZ2   . TRP   A 1 47  ? 11.848  -6.617  35.162 1.00 17.41 ? 73  TRP   A CZ2   1 
ATOM   411  C  CZ3   . TRP   A 1 47  ? 9.782   -5.871  36.173 1.00 17.65 ? 73  TRP   A CZ3   1 
ATOM   412  C  CH2   . TRP   A 1 47  ? 10.687  -6.884  35.837 1.00 17.70 ? 73  TRP   A CH2   1 
ATOM   413  N  N     . ALA   A 1 48  ? 9.314   0.903   33.646 1.00 16.37 ? 74  ALA   A N     1 
ATOM   414  C  CA    . ALA   A 1 48  ? 8.528   2.107   33.965 1.00 18.36 ? 74  ALA   A CA    1 
ATOM   415  C  C     . ALA   A 1 48  ? 7.039   1.902   33.643 1.00 19.81 ? 74  ALA   A C     1 
ATOM   416  O  O     . ALA   A 1 48  ? 6.184   2.397   34.364 1.00 21.10 ? 74  ALA   A O     1 
ATOM   417  C  CB    . ALA   A 1 48  ? 9.073   3.317   33.221 1.00 18.73 ? 74  ALA   A CB    1 
ATOM   418  N  N     . LEU   A 1 49  ? 6.729   1.130   32.604 1.00 19.60 ? 75  LEU   A N     1 
ATOM   419  C  CA    . LEU   A 1 49  ? 5.341   0.827   32.261 1.00 19.37 ? 75  LEU   A CA    1 
ATOM   420  C  C     . LEU   A 1 49  ? 4.784   -0.234  33.223 1.00 18.48 ? 75  LEU   A C     1 
ATOM   421  O  O     . LEU   A 1 49  ? 3.702   -0.041  33.777 1.00 18.26 ? 75  LEU   A O     1 
ATOM   422  C  CB    . LEU   A 1 49  ? 5.245   0.335   30.808 1.00 19.93 ? 75  LEU   A CB    1 
ATOM   423  C  CG    . LEU   A 1 49  ? 3.872   -0.126  30.390 1.00 22.44 ? 75  LEU   A CG    1 
ATOM   424  C  CD1   . LEU   A 1 49  ? 2.935   1.060   30.302 1.00 22.95 ? 75  LEU   A CD1   1 
ATOM   425  C  CD2   . LEU   A 1 49  ? 3.945   -0.899  29.068 1.00 24.03 ? 75  LEU   A CD2   1 
ATOM   426  N  N     . TYR   A 1 50  ? 5.499   -1.357  33.402 1.00 17.40 ? 76  TYR   A N     1 
ATOM   427  C  CA    . TYR   A 1 50  ? 5.040   -2.437  34.266 1.00 16.74 ? 76  TYR   A CA    1 
ATOM   428  C  C     . TYR   A 1 50  ? 4.770   -1.987  35.722 1.00 17.48 ? 76  TYR   A C     1 
ATOM   429  O  O     . TYR   A 1 50  ? 3.734   -2.353  36.289 1.00 18.17 ? 76  TYR   A O     1 
ATOM   430  C  CB    . TYR   A 1 50  ? 6.014   -3.640  34.208 1.00 16.60 ? 76  TYR   A CB    1 
ATOM   431  C  CG    . TYR   A 1 50  ? 5.513   -4.786  35.056 1.00 16.37 ? 76  TYR   A CG    1 
ATOM   432  C  CD1   . TYR   A 1 50  ? 4.496   -5.615  34.601 1.00 16.58 ? 76  TYR   A CD1   1 
ATOM   433  C  CD2   . TYR   A 1 50  ? 5.934   -4.940  36.373 1.00 16.34 ? 76  TYR   A CD2   1 
ATOM   434  C  CE1   . TYR   A 1 50  ? 3.978   -6.625  35.396 1.00 17.08 ? 76  TYR   A CE1   1 
ATOM   435  C  CE2   . TYR   A 1 50  ? 5.388   -5.920  37.193 1.00 17.11 ? 76  TYR   A CE2   1 
ATOM   436  C  CZ    . TYR   A 1 50  ? 4.383   -6.741  36.706 1.00 18.01 ? 76  TYR   A CZ    1 
ATOM   437  O  OH    . TYR   A 1 50  ? 3.818   -7.723  37.484 1.00 19.79 ? 76  TYR   A OH    1 
ATOM   438  N  N     . ASN   A 1 51  ? 5.683   -1.218  36.324 1.00 17.08 ? 77  ASN   A N     1 
ATOM   439  C  CA    . ASN   A 1 51  ? 5.499   -0.779  37.699 1.00 19.07 ? 77  ASN   A CA    1 
ATOM   440  C  C     . ASN   A 1 51  ? 4.362   0.236   37.870 1.00 21.60 ? 77  ASN   A C     1 
ATOM   441  O  O     . ASN   A 1 51  ? 3.917   0.431   38.989 1.00 22.28 ? 77  ASN   A O     1 
ATOM   442  C  CB    . ASN   A 1 51  ? 6.779   -0.184  38.281 1.00 19.65 ? 77  ASN   A CB    1 
ATOM   443  C  CG    . ASN   A 1 51  ? 7.914   -1.149  38.466 1.00 21.64 ? 77  ASN   A CG    1 
ATOM   444  O  OD1   . ASN   A 1 51  ? 9.093   -0.783  38.354 1.00 22.91 ? 77  ASN   A OD1   1 
ATOM   445  N  ND2   . ASN   A 1 51  ? 7.589   -2.385  38.747 1.00 20.13 ? 77  ASN   A ND2   1 
ATOM   446  N  N     . HIS   A 1 52  ? 3.920   0.891   36.790 1.00 22.98 ? 78  HIS   A N     1 
ATOM   447  C  CA    . HIS   A 1 52  ? 2.906   1.926   36.907 1.00 24.88 ? 78  HIS   A CA    1 
ATOM   448  C  C     . HIS   A 1 52  ? 1.564   1.548   36.256 1.00 26.18 ? 78  HIS   A C     1 
ATOM   449  O  O     . HIS   A 1 52  ? 0.680   2.397   36.185 1.00 27.86 ? 78  HIS   A O     1 
ATOM   450  C  CB    . HIS   A 1 52  ? 3.476   3.268   36.404 1.00 26.61 ? 78  HIS   A CB    1 
ATOM   451  C  CG    . HIS   A 1 52  ? 4.631   3.720   37.257 1.00 31.02 ? 78  HIS   A CG    1 
ATOM   452  N  ND1   . HIS   A 1 52  ? 5.953   3.452   36.895 1.00 33.67 ? 78  HIS   A ND1   1 
ATOM   453  C  CD2   . HIS   A 1 52  ? 4.625   4.235   38.511 1.00 32.36 ? 78  HIS   A CD2   1 
ATOM   454  C  CE1   . HIS   A 1 52  ? 6.698   3.891   37.900 1.00 34.43 ? 78  HIS   A CE1   1 
ATOM   455  N  NE2   . HIS   A 1 52  ? 5.946   4.358   38.901 1.00 34.08 ? 78  HIS   A NE2   1 
ATOM   456  N  N     . ILE   A 1 53  ? 1.364   0.283   35.861 1.00 25.24 ? 79  ILE   A N     1 
ATOM   457  C  CA    . ILE   A 1 53  ? 0.068   -0.157  35.330 1.00 26.25 ? 79  ILE   A CA    1 
ATOM   458  C  C     . ILE   A 1 53  ? -0.610  -1.129  36.303 1.00 25.77 ? 79  ILE   A C     1 
ATOM   459  O  O     . ILE   A 1 53  ? 0.055   -1.792  37.090 1.00 24.95 ? 79  ILE   A O     1 
ATOM   460  C  CB    . ILE   A 1 53  ? 0.131   -0.762  33.902 1.00 27.66 ? 79  ILE   A CB    1 
ATOM   461  C  CG1   . ILE   A 1 53  ? 1.127   -1.942  33.842 1.00 28.68 ? 79  ILE   A CG1   1 
ATOM   462  C  CG2   . ILE   A 1 53  ? 0.390   0.308   32.837 1.00 28.88 ? 79  ILE   A CG2   1 
ATOM   463  C  CD1   . ILE   A 1 53  ? 1.322   -2.575  32.464 1.00 29.99 ? 79  ILE   A CD1   1 
ATOM   464  N  N     . GLN   A 1 54  ? -1.933  -1.212  36.226 1.00 26.50 ? 80  GLN   A N     1 
ATOM   465  C  CA    . GLN   A 1 54  ? -2.772  -2.101  37.023 1.00 27.84 ? 80  GLN   A CA    1 
ATOM   466  C  C     . GLN   A 1 54  ? -2.358  -3.559  36.758 1.00 28.02 ? 80  GLN   A C     1 
ATOM   467  O  O     . GLN   A 1 54  ? -2.119  -3.920  35.609 1.00 27.63 ? 80  GLN   A O     1 
ATOM   468  C  CB    . GLN   A 1 54  ? -4.235  -1.923  36.552 1.00 30.85 ? 80  GLN   A CB    1 
ATOM   469  C  CG    . GLN   A 1 54  ? -5.289  -1.825  37.642 1.00 37.04 ? 80  GLN   A CG    1 
ATOM   470  C  CD    . GLN   A 1 54  ? -6.670  -1.657  37.038 1.00 43.32 ? 80  GLN   A CD    1 
ATOM   471  O  OE1   . GLN   A 1 54  ? -6.845  -1.033  35.978 1.00 45.32 ? 80  GLN   A OE1   1 
ATOM   472  N  NE2   . GLN   A 1 54  ? -7.682  -2.202  37.695 1.00 43.88 ? 80  GLN   A NE2   1 
ATOM   473  N  N     . LEU   A 1 55  ? -2.285  -4.390  37.809 1.00 28.12 ? 81  LEU   A N     1 
ATOM   474  C  CA    . LEU   A 1 55  ? -2.008  -5.817  37.673 1.00 28.88 ? 81  LEU   A CA    1 
ATOM   475  C  C     . LEU   A 1 55  ? -3.170  -6.502  36.952 1.00 29.45 ? 81  LEU   A C     1 
ATOM   476  O  O     . LEU   A 1 55  ? -4.317  -6.040  37.033 1.00 29.04 ? 81  LEU   A O     1 
ATOM   477  C  CB    . LEU   A 1 55  ? -1.845  -6.462  39.064 1.00 29.20 ? 81  LEU   A CB    1 
ATOM   478  C  CG    . LEU   A 1 55  ? -0.546  -6.123  39.776 1.00 31.44 ? 81  LEU   A CG    1 
ATOM   479  C  CD1   . LEU   A 1 55  ? -0.630  -6.430  41.268 1.00 32.17 ? 81  LEU   A CD1   1 
ATOM   480  C  CD2   . LEU   A 1 55  ? 0.627   -6.834  39.120 1.00 32.18 ? 81  LEU   A CD2   1 
ATOM   481  N  N     . SER   A 1 56  ? -2.882  -7.624  36.283 1.00 30.06 ? 82  SER   A N     1 
ATOM   482  C  CA    . SER   A 1 56  ? -3.878  -8.437  35.580 1.00 31.42 ? 82  SER   A CA    1 
ATOM   483  C  C     . SER   A 1 56  ? -4.898  -8.995  36.558 1.00 33.11 ? 82  SER   A C     1 
ATOM   484  O  O     . SER   A 1 56  ? -6.074  -9.041  36.237 1.00 33.03 ? 82  SER   A O     1 
ATOM   485  C  CB    . SER   A 1 56  ? -3.205  -9.588  34.841 1.00 32.68 ? 82  SER   A CB    1 
ATOM   486  O  OG    . SER   A 1 56  ? -2.300  -9.091  33.869 1.00 34.52 ? 82  SER   A OG    1 
ATOM   487  N  N     . SER   A 1 57  ? -4.464  -9.368  37.776 1.00 34.73 ? 83  SER   A N     1 
ATOM   488  C  CA    . SER   A 1 57  ? -5.385  -9.868  38.806 1.00 36.26 ? 83  SER   A CA    1 
ATOM   489  C  C     . SER   A 1 57  ? -6.309  -8.786  39.378 1.00 37.69 ? 83  SER   A C     1 
ATOM   490  O  O     . SER   A 1 57  ? -7.222  -9.114  40.134 1.00 38.26 ? 83  SER   A O     1 
ATOM   491  C  CB    . SER   A 1 57  ? -4.614  -10.530 39.937 1.00 37.21 ? 83  SER   A CB    1 
ATOM   492  O  OG    . SER   A 1 57  ? -3.824  -9.548  40.578 1.00 40.37 ? 83  SER   A OG    1 
ATOM   493  N  N     . ASN   A 1 58  ? -6.071  -7.505  39.046 1.00 37.89 ? 84  ASN   A N     1 
ATOM   494  C  CA    . ASN   A 1 58  ? -6.916  -6.396  39.497 1.00 38.53 ? 84  ASN   A CA    1 
ATOM   495  C  C     . ASN   A 1 58  ? -7.790  -5.819  38.363 1.00 38.62 ? 84  ASN   A C     1 
ATOM   496  O  O     . ASN   A 1 58  ? -8.491  -4.836  38.585 1.00 38.89 ? 84  ASN   A O     1 
ATOM   497  C  CB    . ASN   A 1 58  ? -6.079  -5.296  40.158 1.00 40.37 ? 84  ASN   A CB    1 
ATOM   498  C  CG    . ASN   A 1 58  ? -5.555  -5.681  41.516 1.00 45.07 ? 84  ASN   A CG    1 
ATOM   499  O  OD1   . ASN   A 1 58  ? -6.173  -6.464  42.243 1.00 47.07 ? 84  ASN   A OD1   1 
ATOM   500  N  ND2   . ASN   A 1 58  ? -4.402  -5.144  41.896 1.00 45.54 ? 84  ASN   A ND2   1 
ATOM   501  N  N     . LEU   A 1 59  ? -7.762  -6.424  37.158 1.00 38.17 ? 85  LEU   A N     1 
ATOM   502  C  CA    . LEU   A 1 59  ? -8.589  -5.988  36.039 1.00 38.29 ? 85  LEU   A CA    1 
ATOM   503  C  C     . LEU   A 1 59  ? -10.011 -6.505  36.204 1.00 38.31 ? 85  LEU   A C     1 
ATOM   504  O  O     . LEU   A 1 59  ? -10.220 -7.560  36.802 1.00 38.28 ? 85  LEU   A O     1 
ATOM   505  C  CB    . LEU   A 1 59  ? -8.031  -6.511  34.702 1.00 38.32 ? 85  LEU   A CB    1 
ATOM   506  C  CG    . LEU   A 1 59  ? -6.688  -5.947  34.227 1.00 39.60 ? 85  LEU   A CG    1 
ATOM   507  C  CD1   . LEU   A 1 59  ? -6.350  -6.479  32.835 1.00 39.60 ? 85  LEU   A CD1   1 
ATOM   508  C  CD2   . LEU   A 1 59  ? -6.683  -4.411  34.244 1.00 39.94 ? 85  LEU   A CD2   1 
ATOM   509  N  N     . MET   A 1 60  ? -10.983 -5.787  35.641 1.00 38.22 ? 86  MET   A N     1 
ATOM   510  C  CA    . MET   A 1 60  ? -12.378 -6.226  35.708 1.00 38.64 ? 86  MET   A CA    1 
ATOM   511  C  C     . MET   A 1 60  ? -12.552 -7.438  34.800 1.00 37.87 ? 86  MET   A C     1 
ATOM   512  O  O     . MET   A 1 60  ? -11.859 -7.537  33.783 1.00 38.01 ? 86  MET   A O     1 
ATOM   513  C  CB    . MET   A 1 60  ? -13.317 -5.113  35.223 1.00 40.37 ? 86  MET   A CB    1 
ATOM   514  C  CG    . MET   A 1 60  ? -13.110 -3.794  35.909 1.00 44.79 ? 86  MET   A CG    1 
ATOM   515  S  SD    . MET   A 1 60  ? -14.104 -2.494  35.133 1.00 55.10 ? 86  MET   A SD    1 
ATOM   516  C  CE    . MET   A 1 60  ? -13.497 -2.579  33.418 1.00 52.95 ? 86  MET   A CE    1 
ATOM   517  N  N     . PRO   A 1 61  ? -13.507 -8.349  35.090 1.00 36.90 ? 87  PRO   A N     1 
ATOM   518  C  CA    . PRO   A 1 61  ? -13.727 -9.485  34.179 1.00 35.88 ? 87  PRO   A CA    1 
ATOM   519  C  C     . PRO   A 1 61  ? -14.065 -9.003  32.769 1.00 34.04 ? 87  PRO   A C     1 
ATOM   520  O  O     . PRO   A 1 61  ? -14.713 -7.968  32.609 1.00 34.30 ? 87  PRO   A O     1 
ATOM   521  C  CB    . PRO   A 1 61  ? -14.918 -10.230 34.814 1.00 37.05 ? 87  PRO   A CB    1 
ATOM   522  C  CG    . PRO   A 1 61  ? -14.928 -9.803  36.236 1.00 37.78 ? 87  PRO   A CG    1 
ATOM   523  C  CD    . PRO   A 1 61  ? -14.442 -8.383  36.233 1.00 36.57 ? 87  PRO   A CD    1 
ATOM   524  N  N     . GLY   A 1 62  ? -13.583 -9.718  31.766 1.00 31.88 ? 88  GLY   A N     1 
ATOM   525  C  CA    . GLY   A 1 62  ? -13.807 -9.331  30.380 1.00 30.32 ? 88  GLY   A CA    1 
ATOM   526  C  C     . GLY   A 1 62  ? -12.697 -8.485  29.781 1.00 28.50 ? 88  GLY   A C     1 
ATOM   527  O  O     . GLY   A 1 62  ? -12.733 -8.178  28.588 1.00 28.41 ? 88  GLY   A O     1 
ATOM   528  N  N     . CYS   A 1 63  ? -11.696 -8.098  30.589 1.00 27.11 ? 89  CYS   A N     1 
ATOM   529  C  CA    . CYS   A 1 63  ? -10.565 -7.301  30.100 1.00 26.89 ? 89  CYS   A CA    1 
ATOM   530  C  C     . CYS   A 1 63  ? -9.385  -8.177  29.658 1.00 25.78 ? 89  CYS   A C     1 
ATOM   531  O  O     . CYS   A 1 63  ? -9.258  -9.332  30.073 1.00 25.64 ? 89  CYS   A O     1 
ATOM   532  C  CB    . CYS   A 1 63  ? -10.118 -6.277  31.142 1.00 28.12 ? 89  CYS   A CB    1 
ATOM   533  S  SG    . CYS   A 1 63  ? -11.372 -5.036  31.549 1.00 35.21 ? 89  CYS   A SG    1 
ATOM   534  N  N     . ASP   A 1 64  ? -8.522  -7.617  28.803 1.00 24.16 ? 90  ASP   A N     1 
ATOM   535  C  CA    . ASP   A 1 64  ? -7.322  -8.291  28.360 1.00 22.22 ? 90  ASP   A CA    1 
ATOM   536  C  C     . ASP   A 1 64  ? -6.166  -7.311  28.276 1.00 20.03 ? 90  ASP   A C     1 
ATOM   537  O  O     . ASP   A 1 64  ? -6.369  -6.167  27.902 1.00 19.73 ? 90  ASP   A O     1 
ATOM   538  C  CB    . ASP   A 1 64  ? -7.459  -8.820  26.916 1.00 23.85 ? 90  ASP   A CB    1 
ATOM   539  C  CG    . ASP   A 1 64  ? -8.648  -9.661  26.498 1.00 29.58 ? 90  ASP   A CG    1 
ATOM   540  O  OD1   . ASP   A 1 64  ? -9.185  -10.398 27.350 1.00 29.72 ? 90  ASP   A OD1   1 
ATOM   541  O  OD2   . ASP   A 1 64  ? -8.975  -9.662  25.273 1.00 31.86 ? 90  ASP   A OD2   1 
ATOM   542  N  N     . TYR   A 1 65  ? -4.938  -7.809  28.443 1.00 18.00 ? 91  TYR   A N     1 
ATOM   543  C  CA    . TYR   A 1 65  ? -3.709  -7.102  28.104 1.00 17.37 ? 91  TYR   A CA    1 
ATOM   544  C  C     . TYR   A 1 65  ? -3.040  -7.969  27.022 1.00 16.50 ? 91  TYR   A C     1 
ATOM   545  O  O     . TYR   A 1 65  ? -3.195  -9.186  27.014 1.00 16.12 ? 91  TYR   A O     1 
ATOM   546  C  CB    . TYR   A 1 65  ? -2.712  -7.061  29.269 1.00 17.59 ? 91  TYR   A CB    1 
ATOM   547  C  CG    . TYR   A 1 65  ? -2.928  -6.015  30.338 1.00 19.22 ? 91  TYR   A CG    1 
ATOM   548  C  CD1   . TYR   A 1 65  ? -3.055  -4.670  30.009 1.00 20.22 ? 91  TYR   A CD1   1 
ATOM   549  C  CD2   . TYR   A 1 65  ? -2.806  -6.340  31.681 1.00 20.62 ? 91  TYR   A CD2   1 
ATOM   550  C  CE1   . TYR   A 1 65  ? -3.123  -3.688  30.993 1.00 21.14 ? 91  TYR   A CE1   1 
ATOM   551  C  CE2   . TYR   A 1 65  ? -2.841  -5.366  32.669 1.00 21.86 ? 91  TYR   A CE2   1 
ATOM   552  C  CZ    . TYR   A 1 65  ? -3.029  -4.044  32.324 1.00 22.97 ? 91  TYR   A CZ    1 
ATOM   553  O  OH    . TYR   A 1 65  ? -3.044  -3.099  33.324 1.00 25.61 ? 91  TYR   A OH    1 
ATOM   554  N  N     . SER   A 1 66  ? -2.249  -7.363  26.164 1.00 16.02 ? 92  SER   A N     1 
ATOM   555  C  CA    . SER   A 1 66  ? -1.510  -8.066  25.132 1.00 16.52 ? 92  SER   A CA    1 
ATOM   556  C  C     . SER   A 1 66  ? -0.216  -7.331  24.944 1.00 16.53 ? 92  SER   A C     1 
ATOM   557  O  O     . SER   A 1 66  ? -0.239  -6.120  24.866 1.00 16.99 ? 92  SER   A O     1 
ATOM   558  C  CB    . SER   A 1 66  ? -2.255  -8.000  23.793 1.00 19.03 ? 92  SER   A CB    1 
ATOM   559  O  OG    . SER   A 1 66  ? -3.528  -8.615  23.873 1.00 24.37 ? 92  SER   A OG    1 
ATOM   560  N  N     . LEU   A 1 67  ? 0.883   -8.037  24.744 1.00 15.72 ? 93  LEU   A N     1 
ATOM   561  C  CA    . LEU   A 1 67  ? 2.154   -7.401  24.406 1.00 15.16 ? 93  LEU   A CA    1 
ATOM   562  C  C     . LEU   A 1 67  ? 2.523   -7.998  23.050 1.00 14.64 ? 93  LEU   A C     1 
ATOM   563  O  O     . LEU   A 1 67  ? 2.695   -9.199  22.989 1.00 15.42 ? 93  LEU   A O     1 
ATOM   564  C  CB    . LEU   A 1 67  ? 3.256   -7.773  25.403 1.00 15.36 ? 93  LEU   A CB    1 
ATOM   565  C  CG    . LEU   A 1 67  ? 4.525   -6.949  25.151 1.00 16.88 ? 93  LEU   A CG    1 
ATOM   566  C  CD1   . LEU   A 1 67  ? 4.317   -5.525  25.605 1.00 17.72 ? 93  LEU   A CD1   1 
ATOM   567  C  CD2   . LEU   A 1 67  ? 5.734   -7.564  25.808 1.00 16.75 ? 93  LEU   A CD2   1 
ATOM   568  N  N     . PHE   A 1 68  ? 2.571   -7.213  21.970 1.00 13.36 ? 94  PHE   A N     1 
ATOM   569  C  CA    . PHE   A 1 68  ? 2.927   -7.746  20.651 1.00 13.48 ? 94  PHE   A CA    1 
ATOM   570  C  C     . PHE   A 1 68  ? 4.080   -6.937  20.076 1.00 14.80 ? 94  PHE   A C     1 
ATOM   571  O  O     . PHE   A 1 68  ? 4.251   -5.777  20.438 1.00 14.37 ? 94  PHE   A O     1 
ATOM   572  C  CB    . PHE   A 1 68  ? 1.712   -7.683  19.691 1.00 12.94 ? 94  PHE   A CB    1 
ATOM   573  C  CG    . PHE   A 1 68  ? 0.840   -8.913  19.801 1.00 13.14 ? 94  PHE   A CG    1 
ATOM   574  C  CD1   . PHE   A 1 68  ? 0.155   -9.193  20.967 1.00 12.88 ? 94  PHE   A CD1   1 
ATOM   575  C  CD2   . PHE   A 1 68  ? 0.734   -9.807  18.744 1.00 13.48 ? 94  PHE   A CD2   1 
ATOM   576  C  CE1   . PHE   A 1 68  ? -0.578  -10.364 21.099 1.00 13.42 ? 94  PHE   A CE1   1 
ATOM   577  C  CE2   . PHE   A 1 68  ? -0.034  -10.960 18.869 1.00 13.73 ? 94  PHE   A CE2   1 
ATOM   578  C  CZ    . PHE   A 1 68  ? -0.686  -11.226 20.037 1.00 13.15 ? 94  PHE   A CZ    1 
ATOM   579  N  N     . LYS   A 1 69  ? 4.874   -7.522  19.159 1.00 15.66 ? 95  LYS   A N     1 
ATOM   580  C  CA    . LYS   A 1 69  ? 5.938   -6.760  18.496 1.00 16.72 ? 95  LYS   A CA    1 
ATOM   581  C  C     . LYS   A 1 69  ? 5.325   -5.608  17.729 1.00 18.19 ? 95  LYS   A C     1 
ATOM   582  O  O     . LYS   A 1 69  ? 4.161   -5.678  17.293 1.00 18.36 ? 95  LYS   A O     1 
ATOM   583  C  CB    . LYS   A 1 69  ? 6.763   -7.625  17.537 1.00 18.19 ? 95  LYS   A CB    1 
ATOM   584  C  CG    . LYS   A 1 69  ? 7.298   -8.872  18.186 1.00 21.95 ? 95  LYS   A CG    1 
ATOM   585  C  CD    . LYS   A 1 69  ? 8.262   -9.582  17.293 1.00 25.60 ? 95  LYS   A CD    1 
ATOM   586  C  CE    . LYS   A 1 69  ? 8.923   -10.715 18.018 1.00 26.97 ? 95  LYS   A CE    1 
ATOM   587  N  NZ    . LYS   A 1 69  ? 9.379   -11.733 17.044 1.00 27.37 ? 95  LYS   A NZ    1 
ATOM   588  N  N     . ASP   A 1 70  ? 6.077   -4.513  17.632 1.00 19.00 ? 96  ASP   A N     1 
ATOM   589  C  CA    . ASP   A 1 70  ? 5.654   -3.311  16.925 1.00 20.14 ? 96  ASP   A CA    1 
ATOM   590  C  C     . ASP   A 1 70  ? 5.242   -3.644  15.479 1.00 19.84 ? 96  ASP   A C     1 
ATOM   591  O  O     . ASP   A 1 70  ? 5.966   -4.366  14.792 1.00 19.35 ? 96  ASP   A O     1 
ATOM   592  C  CB    . ASP   A 1 70  ? 6.830   -2.320  16.919 1.00 23.53 ? 96  ASP   A CB    1 
ATOM   593  C  CG    . ASP   A 1 70  ? 6.437   -0.970  16.387 1.00 29.16 ? 96  ASP   A CG    1 
ATOM   594  O  OD1   . ASP   A 1 70  ? 5.310   -0.540  16.664 1.00 30.12 ? 96  ASP   A OD1   1 
ATOM   595  O  OD2   . ASP   A 1 70  ? 7.260   -0.347  15.688 1.00 32.02 ? 96  ASP   A OD2   1 
ATOM   596  N  N     . GLY   A 1 71  ? 4.061   -3.188  15.065 1.00 19.83 ? 97  GLY   A N     1 
ATOM   597  C  CA    . GLY   A 1 71  ? 3.582   -3.476  13.722 1.00 20.28 ? 97  GLY   A CA    1 
ATOM   598  C  C     . GLY   A 1 71  ? 2.654   -4.678  13.652 1.00 21.00 ? 97  GLY   A C     1 
ATOM   599  O  O     . GLY   A 1 71  ? 2.092   -4.947  12.590 1.00 21.75 ? 97  GLY   A O     1 
ATOM   600  N  N     . ILE   A 1 72  ? 2.491   -5.421  14.761 1.00 20.15 ? 98  ILE   A N     1 
ATOM   601  C  CA    . ILE   A 1 72  ? 1.580   -6.561  14.815 1.00 20.51 ? 98  ILE   A CA    1 
ATOM   602  C  C     . ILE   A 1 72  ? 0.431   -6.251  15.757 1.00 20.97 ? 98  ILE   A C     1 
ATOM   603  O  O     . ILE   A 1 72  ? 0.644   -6.098  16.954 1.00 21.01 ? 98  ILE   A O     1 
ATOM   604  C  CB    . ILE   A 1 72  ? 2.262   -7.892  15.241 1.00 20.75 ? 98  ILE   A CB    1 
ATOM   605  C  CG1   . ILE   A 1 72  ? 3.536   -8.183  14.425 1.00 21.41 ? 98  ILE   A CG1   1 
ATOM   606  C  CG2   . ILE   A 1 72  ? 1.258   -9.073  15.175 1.00 20.89 ? 98  ILE   A CG2   1 
ATOM   607  C  CD1   . ILE   A 1 72  ? 4.301   -9.459  14.864 1.00 22.06 ? 98  ILE   A CD1   1 
ATOM   608  N  N     . GLU   A 1 73  ? -0.792  -6.168  15.231 1.00 20.86 ? 99  GLU   A N     1 
ATOM   609  C  CA    . GLU   A 1 73  ? -1.962  -5.965  16.066 1.00 20.83 ? 99  GLU   A CA    1 
ATOM   610  C  C     . GLU   A 1 73  ? -2.338  -7.313  16.700 1.00 20.30 ? 99  GLU   A C     1 
ATOM   611  O  O     . GLU   A 1 73  ? -2.189  -8.352  16.069 1.00 19.35 ? 99  GLU   A O     1 
ATOM   612  C  CB    . GLU   A 1 73  ? -3.123  -5.405  15.241 1.00 23.95 ? 99  GLU   A CB    1 
ATOM   613  C  CG    . GLU   A 1 73  ? -2.748  -4.140  14.496 1.00 32.14 ? 99  GLU   A CG    1 
ATOM   614  C  CD    . GLU   A 1 73  ? -3.920  -3.506  13.781 1.00 41.57 ? 99  GLU   A CD    1 
ATOM   615  O  OE1   . GLU   A 1 73  ? -4.771  -2.891  14.462 1.00 42.28 ? 99  GLU   A OE1   1 
ATOM   616  O  OE2   . GLU   A 1 73  ? -3.996  -3.639  12.538 1.00 46.96 ? 99  GLU   A OE2   1 
ATOM   617  N  N     . PRO   A 1 74  ? -2.811  -7.306  17.962 1.00 20.69 ? 100 PRO   A N     1 
ATOM   618  C  CA    . PRO   A 1 74  ? -3.170  -8.565  18.637 1.00 21.13 ? 100 PRO   A CA    1 
ATOM   619  C  C     . PRO   A 1 74  ? -4.512  -9.161  18.220 1.00 21.47 ? 100 PRO   A C     1 
ATOM   620  O  O     . PRO   A 1 74  ? -5.410  -9.355  19.041 1.00 21.14 ? 100 PRO   A O     1 
ATOM   621  C  CB    . PRO   A 1 74  ? -3.181  -8.183  20.113 1.00 21.89 ? 100 PRO   A CB    1 
ATOM   622  C  CG    . PRO   A 1 74  ? -3.473  -6.739  20.128 1.00 22.80 ? 100 PRO   A CG    1 
ATOM   623  C  CD    . PRO   A 1 74  ? -2.998  -6.142  18.840 1.00 20.80 ? 100 PRO   A CD    1 
ATOM   624  N  N     . MET   A 1 75  ? -4.638  -9.461  16.941 1.00 21.29 ? 101 MET   A N     1 
ATOM   625  C  CA    . MET   A 1 75  ? -5.837  -10.049 16.394 1.00 21.81 ? 101 MET   A CA    1 
ATOM   626  C  C     . MET   A 1 75  ? -5.496  -11.009 15.259 1.00 20.71 ? 101 MET   A C     1 
ATOM   627  O  O     . MET   A 1 75  ? -4.449  -10.866 14.610 1.00 19.76 ? 101 MET   A O     1 
ATOM   628  C  CB    . MET   A 1 75  ? -6.853  -8.966  15.968 1.00 22.97 ? 101 MET   A CB    1 
ATOM   629  C  CG    . MET   A 1 75  ? -6.359  -8.059  14.896 1.00 26.27 ? 101 MET   A CG    1 
ATOM   630  S  SD    . MET   A 1 75  ? -7.587  -6.762  14.475 1.00 32.48 ? 101 MET   A SD    1 
ATOM   631  C  CE    . MET   A 1 75  ? -6.638  -5.855  13.266 1.00 28.41 ? 101 MET   A CE    1 
ATOM   632  N  N     . TRP   A 1 76  ? -6.363  -12.007 15.056 1.00 20.55 ? 102 TRP   A N     1 
ATOM   633  C  CA    . TRP   A 1 76  ? -6.200  -13.049 14.033 1.00 21.91 ? 102 TRP   A CA    1 
ATOM   634  C  C     . TRP   A 1 76  ? -6.079  -12.445 12.626 1.00 22.75 ? 102 TRP   A C     1 
ATOM   635  O  O     . TRP   A 1 76  ? -5.395  -13.014 11.779 1.00 23.22 ? 102 TRP   A O     1 
ATOM   636  C  CB    . TRP   A 1 76  ? -7.400  -14.022 14.025 1.00 21.76 ? 102 TRP   A CB    1 
ATOM   637  C  CG    . TRP   A 1 76  ? -7.854  -14.580 15.343 1.00 22.57 ? 102 TRP   A CG    1 
ATOM   638  C  CD1   . TRP   A 1 76  ? -7.070  -15.071 16.344 1.00 23.72 ? 102 TRP   A CD1   1 
ATOM   639  C  CD2   . TRP   A 1 76  ? -9.207  -14.873 15.713 1.00 22.67 ? 102 TRP   A CD2   1 
ATOM   640  N  NE1   . TRP   A 1 76  ? -7.854  -15.618 17.331 1.00 24.14 ? 102 TRP   A NE1   1 
ATOM   641  C  CE2   . TRP   A 1 76  ? -9.172  -15.496 16.974 1.00 23.62 ? 102 TRP   A CE2   1 
ATOM   642  C  CE3   . TRP   A 1 76  ? -10.452 -14.600 15.135 1.00 23.53 ? 102 TRP   A CE3   1 
ATOM   643  C  CZ2   . TRP   A 1 76  ? -10.332 -15.870 17.656 1.00 24.48 ? 102 TRP   A CZ2   1 
ATOM   644  C  CZ3   . TRP   A 1 76  ? -11.601 -14.980 15.809 1.00 24.53 ? 102 TRP   A CZ3   1 
ATOM   645  C  CH2   . TRP   A 1 76  ? -11.532 -15.617 17.048 1.00 24.41 ? 102 TRP   A CH2   1 
ATOM   646  N  N     . GLU   A 1 77  ? -6.760  -11.312 12.387 1.00 22.85 ? 103 GLU   A N     1 
ATOM   647  C  CA    . GLU   A 1 77  ? -6.832  -10.579 11.119 1.00 23.97 ? 103 GLU   A CA    1 
ATOM   648  C  C     . GLU   A 1 77  ? -5.488  -10.044 10.662 1.00 24.23 ? 103 GLU   A C     1 
ATOM   649  O  O     . GLU   A 1 77  ? -5.282  -9.878  9.465  1.00 24.52 ? 103 GLU   A O     1 
ATOM   650  C  CB    . GLU   A 1 77  ? -7.833  -9.414  11.222 1.00 26.36 ? 103 GLU   A CB    1 
ATOM   651  C  CG    . GLU   A 1 77  ? -9.288  -9.840  11.372 1.00 30.28 ? 103 GLU   A CG    1 
ATOM   652  C  CD    . GLU   A 1 77  ? -9.777  -10.103 12.788 1.00 34.15 ? 103 GLU   A CD    1 
ATOM   653  O  OE1   . GLU   A 1 77  ? -8.955  -10.450 13.665 1.00 31.99 ? 103 GLU   A OE1   1 
ATOM   654  O  OE2   . GLU   A 1 77  ? -10.999 -9.967  13.019 1.00 37.17 ? 103 GLU   A OE2   1 
ATOM   655  N  N     . ASP   A 1 78  ? -4.569  -9.760  11.595 1.00 23.86 ? 104 ASP   A N     1 
ATOM   656  C  CA    . ASP   A 1 78  ? -3.238  -9.245  11.226 1.00 23.98 ? 104 ASP   A CA    1 
ATOM   657  C  C     . ASP   A 1 78  ? -2.507  -10.277 10.377 1.00 24.62 ? 104 ASP   A C     1 
ATOM   658  O  O     . ASP   A 1 78  ? -2.604  -11.472 10.661 1.00 24.57 ? 104 ASP   A O     1 
ATOM   659  C  CB    . ASP   A 1 78  ? -2.410  -8.941  12.488 1.00 24.85 ? 104 ASP   A CB    1 
ATOM   660  C  CG    . ASP   A 1 78  ? -1.207  -8.076  12.200 1.00 28.87 ? 104 ASP   A CG    1 
ATOM   661  O  OD1   . ASP   A 1 78  ? -0.224  -8.594  11.623 1.00 30.33 ? 104 ASP   A OD1   1 
ATOM   662  O  OD2   . ASP   A 1 78  ? -1.234  -6.885  12.565 1.00 29.36 ? 104 ASP   A OD2   1 
ATOM   663  N  N     . GLU   A 1 79  ? -1.820  -9.824  9.318  1.00 24.99 ? 105 GLU   A N     1 
ATOM   664  C  CA    . GLU   A 1 79  ? -1.060  -10.678 8.401  1.00 25.93 ? 105 GLU   A CA    1 
ATOM   665  C  C     . GLU   A 1 79  ? -0.060  -11.587 9.127  1.00 25.28 ? 105 GLU   A C     1 
ATOM   666  O  O     . GLU   A 1 79  ? 0.120   -12.730 8.721  1.00 25.91 ? 105 GLU   A O     1 
ATOM   667  C  CB    . GLU   A 1 79  ? -0.318  -9.804  7.376  1.00 30.84 ? 105 GLU   A CB    1 
ATOM   668  C  CG    . GLU   A 1 79  ? 0.397   -10.589 6.296  1.00 39.89 ? 105 GLU   A CG    1 
ATOM   669  C  CD    . GLU   A 1 79  ? -0.519  -11.218 5.265  1.00 49.89 ? 105 GLU   A CD    1 
ATOM   670  O  OE1   . GLU   A 1 79  ? -1.632  -10.684 5.053  1.00 52.86 ? 105 GLU   A OE1   1 
ATOM   671  O  OE2   . GLU   A 1 79  ? -0.117  -12.234 4.652  1.00 53.02 ? 105 GLU   A OE2   1 
ATOM   672  N  N     . LYS   A 1 80  ? 0.565   -11.103 10.217 1.00 24.14 ? 106 LYS   A N     1 
ATOM   673  C  CA    . LYS   A 1 80  ? 1.536   -11.922 10.951 1.00 23.98 ? 106 LYS   A CA    1 
ATOM   674  C  C     . LYS   A 1 80  ? 0.902   -12.955 11.910 1.00 23.17 ? 106 LYS   A C     1 
ATOM   675  O  O     . LYS   A 1 80  ? 1.631   -13.762 12.486 1.00 23.33 ? 106 LYS   A O     1 
ATOM   676  C  CB    . LYS   A 1 80  ? 2.545   -11.043 11.692 1.00 25.86 ? 106 LYS   A CB    1 
ATOM   677  C  CG    . LYS   A 1 80  ? 3.505   -10.317 10.762 1.00 31.90 ? 106 LYS   A CG    1 
ATOM   678  C  CD    . LYS   A 1 80  ? 4.444   -11.277 10.037 1.00 38.47 ? 106 LYS   A CD    1 
ATOM   679  C  CE    . LYS   A 1 80  ? 5.475   -10.584 9.168  1.00 43.52 ? 106 LYS   A CE    1 
ATOM   680  N  NZ    . LYS   A 1 80  ? 4.877   -10.047 7.914  1.00 46.68 ? 106 LYS   A NZ    1 
ATOM   681  N  N     . ASN   A 1 81  ? -0.438  -12.950 12.053 1.00 21.63 ? 107 ASN   A N     1 
ATOM   682  C  CA    . ASN   A 1 81  ? -1.188  -13.877 12.912 1.00 21.19 ? 107 ASN   A CA    1 
ATOM   683  C  C     . ASN   A 1 81  ? -2.141  -14.788 12.130 1.00 21.88 ? 107 ASN   A C     1 
ATOM   684  O  O     . ASN   A 1 81  ? -2.480  -15.862 12.610 1.00 22.13 ? 107 ASN   A O     1 
ATOM   685  C  CB    . ASN   A 1 81  ? -2.016  -13.094 13.927 1.00 20.74 ? 107 ASN   A CB    1 
ATOM   686  C  CG    . ASN   A 1 81  ? -1.172  -12.327 14.894 1.00 21.41 ? 107 ASN   A CG    1 
ATOM   687  O  OD1   . ASN   A 1 81  ? -0.096  -12.794 15.310 1.00 21.68 ? 107 ASN   A OD1   1 
ATOM   688  N  ND2   . ASN   A 1 81  ? -1.642  -11.144 15.276 1.00 19.78 ? 107 ASN   A ND2   1 
ATOM   689  N  N     . LYS   A 1 82  ? -2.586  -14.361 10.948 1.00 22.24 ? 108 LYS   A N     1 
ATOM   690  C  CA    . LYS   A 1 82  ? -3.557  -15.075 10.109 1.00 22.93 ? 108 LYS   A CA    1 
ATOM   691  C  C     . LYS   A 1 82  ? -3.292  -16.595 9.957  1.00 22.37 ? 108 LYS   A C     1 
ATOM   692  O  O     . LYS   A 1 82  ? -4.198  -17.403 10.135 1.00 22.63 ? 108 LYS   A O     1 
ATOM   693  C  CB    . LYS   A 1 82  ? -3.623  -14.372 8.744  1.00 25.90 ? 108 LYS   A CB    1 
ATOM   694  C  CG    . LYS   A 1 82  ? -4.757  -14.826 7.869  1.00 32.88 ? 108 LYS   A CG    1 
ATOM   695  C  CD    . LYS   A 1 82  ? -4.918  -13.898 6.657  1.00 38.65 ? 108 LYS   A CD    1 
ATOM   696  C  CE    . LYS   A 1 82  ? -6.134  -14.304 5.864  1.00 44.20 ? 108 LYS   A CE    1 
ATOM   697  N  NZ    . LYS   A 1 82  ? -6.231  -13.566 4.572  1.00 47.99 ? 108 LYS   A NZ    1 
ATOM   698  N  N     . ARG   A 1 83  ? -2.055  -16.981 9.631  1.00 21.61 ? 109 ARG   A N     1 
ATOM   699  C  CA    . ARG   A 1 83  ? -1.681  -18.391 9.493  1.00 21.93 ? 109 ARG   A CA    1 
ATOM   700  C  C     . ARG   A 1 83  ? -1.074  -18.990 10.794 1.00 21.09 ? 109 ARG   A C     1 
ATOM   701  O  O     . ARG   A 1 83  ? -0.535  -20.092 10.765 1.00 21.14 ? 109 ARG   A O     1 
ATOM   702  C  CB    . ARG   A 1 83  ? -0.656  -18.529 8.348  1.00 24.23 ? 109 ARG   A CB    1 
ATOM   703  C  CG    . ARG   A 1 83  ? -1.170  -17.994 7.010  1.00 29.06 ? 109 ARG   A CG    1 
ATOM   704  C  CD    . ARG   A 1 83  ? -0.084  -17.926 5.946  1.00 35.22 ? 109 ARG   A CD    1 
ATOM   705  N  NE    . ARG   A 1 83  ? 1.017   -17.050 6.355  1.00 41.74 ? 109 ARG   A NE    1 
ATOM   706  C  CZ    . ARG   A 1 83  ? 1.056   -15.737 6.138  1.00 46.59 ? 109 ARG   A CZ    1 
ATOM   707  N  NH1   . ARG   A 1 83  ? 0.058   -15.130 5.503  1.00 47.41 ? 109 ARG   A NH1   1 
ATOM   708  N  NH2   . ARG   A 1 83  ? 2.094   -15.022 6.550  1.00 47.11 ? 109 ARG   A NH2   1 
ATOM   709  N  N     . GLY   A 1 84  ? -1.170  -18.264 11.905 1.00 19.75 ? 110 GLY   A N     1 
ATOM   710  C  CA    . GLY   A 1 84  ? -0.593  -18.679 13.174 1.00 18.77 ? 110 GLY   A CA    1 
ATOM   711  C  C     . GLY   A 1 84  ? -1.542  -19.328 14.141 1.00 17.39 ? 110 GLY   A C     1 
ATOM   712  O  O     . GLY   A 1 84  ? -2.582  -19.859 13.769 1.00 16.51 ? 110 GLY   A O     1 
ATOM   713  N  N     . GLY   A 1 85  ? -1.144  -19.325 15.394 1.00 16.82 ? 111 GLY   A N     1 
ATOM   714  C  CA    . GLY   A 1 85  ? -1.923  -19.923 16.463 1.00 16.02 ? 111 GLY   A CA    1 
ATOM   715  C  C     . GLY   A 1 85  ? -1.354  -19.529 17.815 1.00 15.65 ? 111 GLY   A C     1 
ATOM   716  O  O     . GLY   A 1 85  ? -0.504  -18.632 17.908 1.00 16.01 ? 111 GLY   A O     1 
ATOM   717  N  N     . ARG   A 1 86  ? -1.800  -20.200 18.862 1.00 14.33 ? 112 ARG   A N     1 
ATOM   718  C  CA    . ARG   A 1 86  ? -1.380  -19.860 20.219 1.00 14.88 ? 112 ARG   A CA    1 
ATOM   719  C  C     . ARG   A 1 86  ? -1.227  -21.061 21.132 1.00 15.63 ? 112 ARG   A C     1 
ATOM   720  O  O     . ARG   A 1 86  ? -1.981  -22.040 21.037 1.00 15.72 ? 112 ARG   A O     1 
ATOM   721  C  CB    . ARG   A 1 86  ? -2.408  -18.889 20.848 1.00 15.42 ? 112 ARG   A CB    1 
ATOM   722  C  CG    . ARG   A 1 86  ? -3.837  -19.500 20.914 1.00 18.93 ? 112 ARG   A CG    1 
ATOM   723  C  CD    . ARG   A 1 86  ? -4.849  -18.616 21.637 1.00 21.81 ? 112 ARG   A CD    1 
ATOM   724  N  NE    . ARG   A 1 86  ? -6.183  -19.210 21.574 1.00 24.99 ? 112 ARG   A NE    1 
ATOM   725  C  CZ    . ARG   A 1 86  ? -7.227  -18.815 22.296 1.00 25.61 ? 112 ARG   A CZ    1 
ATOM   726  N  NH1   . ARG   A 1 86  ? -7.109  -17.806 23.152 1.00 23.48 ? 112 ARG   A NH1   1 
ATOM   727  N  NH2   . ARG   A 1 86  ? -8.396  -19.426 22.168 1.00 24.95 ? 112 ARG   A NH2   1 
ATOM   728  N  N     . TRP   A 1 87  ? -0.279  -20.962 22.063 1.00 15.71 ? 113 TRP   A N     1 
ATOM   729  C  CA    . TRP   A 1 87  ? -0.136  -21.955 23.106 1.00 16.68 ? 113 TRP   A CA    1 
ATOM   730  C  C     . TRP   A 1 87  ? -0.980  -21.406 24.216 1.00 19.67 ? 113 TRP   A C     1 
ATOM   731  O  O     . TRP   A 1 87  ? -0.693  -20.315 24.686 1.00 19.94 ? 113 TRP   A O     1 
ATOM   732  C  CB    . TRP   A 1 87  ? 1.315   -22.052 23.579 1.00 15.92 ? 113 TRP   A CB    1 
ATOM   733  C  CG    . TRP   A 1 87  ? 2.151   -22.947 22.716 1.00 15.81 ? 113 TRP   A CG    1 
ATOM   734  C  CD1   . TRP   A 1 87  ? 3.147   -22.572 21.864 1.00 16.18 ? 113 TRP   A CD1   1 
ATOM   735  C  CD2   . TRP   A 1 87  ? 2.052   -24.368 22.622 1.00 16.11 ? 113 TRP   A CD2   1 
ATOM   736  N  NE1   . TRP   A 1 87  ? 3.708   -23.674 21.285 1.00 16.37 ? 113 TRP   A NE1   1 
ATOM   737  C  CE2   . TRP   A 1 87  ? 3.002   -24.790 21.674 1.00 16.63 ? 113 TRP   A CE2   1 
ATOM   738  C  CE3   . TRP   A 1 87  ? 1.238   -25.330 23.234 1.00 17.55 ? 113 TRP   A CE3   1 
ATOM   739  C  CZ2   . TRP   A 1 87  ? 3.207   -26.137 21.377 1.00 17.10 ? 113 TRP   A CZ2   1 
ATOM   740  C  CZ3   . TRP   A 1 87  ? 1.403   -26.662 22.892 1.00 17.84 ? 113 TRP   A CZ3   1 
ATOM   741  C  CH2   . TRP   A 1 87  ? 2.385   -27.053 21.982 1.00 17.58 ? 113 TRP   A CH2   1 
ATOM   742  N  N     . LEU   A 1 88  ? -1.995  -22.148 24.666 1.00 21.10 ? 114 LEU   A N     1 
ATOM   743  C  CA    . LEU   A 1 88  ? -2.916  -21.645 25.676 1.00 22.56 ? 114 LEU   A CA    1 
ATOM   744  C  C     . LEU   A 1 88  ? -2.767  -22.297 27.055 1.00 23.99 ? 114 LEU   A C     1 
ATOM   745  O  O     . LEU   A 1 88  ? -2.671  -23.523 27.175 1.00 24.49 ? 114 LEU   A O     1 
ATOM   746  C  CB    . LEU   A 1 88  ? -4.355  -21.794 25.144 1.00 22.97 ? 114 LEU   A CB    1 
ATOM   747  C  CG    . LEU   A 1 88  ? -5.445  -21.179 25.994 1.00 25.64 ? 114 LEU   A CG    1 
ATOM   748  C  CD1   . LEU   A 1 88  ? -5.554  -19.700 25.751 1.00 25.88 ? 114 LEU   A CD1   1 
ATOM   749  C  CD2   . LEU   A 1 88  ? -6.788  -21.868 25.747 1.00 26.87 ? 114 LEU   A CD2   1 
ATOM   750  N  N     . ILE   A 1 89  ? -2.708  -21.463 28.092 1.00 24.41 ? 115 ILE   A N     1 
ATOM   751  C  CA    . ILE   A 1 89  ? -2.624  -21.874 29.484 1.00 25.59 ? 115 ILE   A CA    1 
ATOM   752  C  C     . ILE   A 1 89  ? -3.904  -21.441 30.174 1.00 26.80 ? 115 ILE   A C     1 
ATOM   753  O  O     . ILE   A 1 89  ? -4.286  -20.277 30.092 1.00 25.37 ? 115 ILE   A O     1 
ATOM   754  C  CB    . ILE   A 1 89  ? -1.368  -21.312 30.164 1.00 27.39 ? 115 ILE   A CB    1 
ATOM   755  C  CG1   . ILE   A 1 89  ? -0.128  -21.869 29.440 1.00 29.59 ? 115 ILE   A CG1   1 
ATOM   756  C  CG2   . ILE   A 1 89  ? -1.366  -21.682 31.655 1.00 28.31 ? 115 ILE   A CG2   1 
ATOM   757  C  CD1   . ILE   A 1 89  ? 1.084   -21.358 29.868 1.00 31.97 ? 115 ILE   A CD1   1 
ATOM   758  N  N     . THR   A 1 90  ? -4.597  -22.398 30.809 1.00 28.91 ? 116 THR   A N     1 
ATOM   759  C  CA    . THR   A 1 90  ? -5.865  -22.177 31.493 1.00 31.30 ? 116 THR   A CA    1 
ATOM   760  C  C     . THR   A 1 90  ? -5.678  -22.199 33.010 1.00 32.95 ? 116 THR   A C     1 
ATOM   761  O  O     . THR   A 1 90  ? -4.975  -23.054 33.546 1.00 33.40 ? 116 THR   A O     1 
ATOM   762  C  CB    . THR   A 1 90  ? -6.889  -23.187 30.959 1.00 34.03 ? 116 THR   A CB    1 
ATOM   763  O  OG1   . THR   A 1 90  ? -7.214  -22.821 29.609 1.00 35.31 ? 116 THR   A OG1   1 
ATOM   764  C  CG2   . THR   A 1 90  ? -8.163  -23.251 31.800 1.00 34.69 ? 116 THR   A CG2   1 
ATOM   765  N  N     . LEU   A 1 91  ? -6.235  -21.206 33.697 1.00 33.63 ? 117 LEU   A N     1 
ATOM   766  C  CA    . LEU   A 1 91  ? -6.131  -21.102 35.147 1.00 34.80 ? 117 LEU   A CA    1 
ATOM   767  C  C     . LEU   A 1 91  ? -7.525  -21.199 35.776 1.00 37.20 ? 117 LEU   A C     1 
ATOM   768  O  O     . LEU   A 1 91  ? -8.489  -20.679 35.213 1.00 37.48 ? 117 LEU   A O     1 
ATOM   769  C  CB    . LEU   A 1 91  ? -5.495  -19.758 35.550 1.00 34.77 ? 117 LEU   A CB    1 
ATOM   770  C  CG    . LEU   A 1 91  ? -3.995  -19.581 35.296 1.00 36.33 ? 117 LEU   A CG    1 
ATOM   771  C  CD1   . LEU   A 1 91  ? -3.736  -18.991 33.927 1.00 36.63 ? 117 LEU   A CD1   1 
ATOM   772  C  CD2   . LEU   A 1 91  ? -3.382  -18.658 36.326 1.00 37.04 ? 117 LEU   A CD2   1 
ATOM   773  N  N     . ASN   A 1 92  ? -7.636  -21.834 36.949 1.00 39.20 ? 118 ASN   A N     1 
ATOM   774  C  CA    . ASN   A 1 92  ? -8.928  -21.890 37.640 1.00 41.49 ? 118 ASN   A CA    1 
ATOM   775  C  C     . ASN   A 1 92  ? -9.084  -20.682 38.575 1.00 42.93 ? 118 ASN   A C     1 
ATOM   776  O  O     . ASN   A 1 92  ? -8.127  -19.917 38.748 1.00 42.78 ? 118 ASN   A O     1 
ATOM   777  C  CB    . ASN   A 1 92  ? -9.170  -23.242 38.334 1.00 43.36 ? 118 ASN   A CB    1 
ATOM   778  C  CG    . ASN   A 1 92  ? -8.065  -23.698 39.236 1.00 47.09 ? 118 ASN   A CG    1 
ATOM   779  O  OD1   . ASN   A 1 92  ? -7.496  -22.924 40.010 1.00 49.01 ? 118 ASN   A OD1   1 
ATOM   780  N  ND2   . ASN   A 1 92  ? -7.747  -24.979 39.165 1.00 47.90 ? 118 ASN   A ND2   1 
ATOM   781  N  N     . LYS   A 1 93  ? -10.288 -20.480 39.143 1.00 43.95 ? 119 LYS   A N     1 
ATOM   782  C  CA    . LYS   A 1 93  ? -10.586 -19.362 40.040 1.00 45.68 ? 119 LYS   A CA    1 
ATOM   783  C  C     . LYS   A 1 93  ? -9.570  -19.201 41.163 1.00 47.22 ? 119 LYS   A C     1 
ATOM   784  O  O     . LYS   A 1 93  ? -9.155  -18.082 41.458 1.00 47.79 ? 119 LYS   A O     1 
ATOM   785  C  CB    . LYS   A 1 93  ? -12.003 -19.509 40.609 1.00 48.42 ? 119 LYS   A CB    1 
ATOM   786  C  CG    . LYS   A 1 93  ? -13.072 -19.393 39.533 1.00 53.12 ? 119 LYS   A CG    1 
ATOM   787  C  CD    . LYS   A 1 93  ? -14.375 -20.045 39.957 1.00 58.00 ? 119 LYS   A CD    1 
ATOM   788  C  CE    . LYS   A 1 93  ? -15.232 -20.361 38.759 1.00 62.35 ? 119 LYS   A CE    1 
ATOM   789  N  NZ    . LYS   A 1 93  ? -16.458 -21.112 39.139 1.00 65.47 ? 119 LYS   A NZ    1 
ATOM   790  N  N     . GLN   A 1 94  ? -9.116  -20.323 41.739 1.00 47.90 ? 120 GLN   A N     1 
ATOM   791  C  CA    . GLN   A 1 94  ? -8.123  -20.351 42.814 1.00 48.97 ? 120 GLN   A CA    1 
ATOM   792  C  C     . GLN   A 1 94  ? -6.773  -19.778 42.387 1.00 49.10 ? 120 GLN   A C     1 
ATOM   793  O  O     . GLN   A 1 94  ? -6.041  -19.250 43.221 1.00 49.41 ? 120 GLN   A O     1 
ATOM   794  C  CB    . GLN   A 1 94  ? -7.913  -21.795 43.319 1.00 51.36 ? 120 GLN   A CB    1 
ATOM   795  C  CG    . GLN   A 1 94  ? -9.003  -22.309 44.258 1.00 56.42 ? 120 GLN   A CG    1 
ATOM   796  C  CD    . GLN   A 1 94  ? -10.274 -22.652 43.522 1.00 61.49 ? 120 GLN   A CD    1 
ATOM   797  O  OE1   . GLN   A 1 94  ? -10.251 -23.230 42.425 1.00 62.49 ? 120 GLN   A OE1   1 
ATOM   798  N  NE2   . GLN   A 1 94  ? -11.411 -22.291 44.108 1.00 62.37 ? 120 GLN   A NE2   1 
ATOM   799  N  N     . GLN   A 1 95  ? -6.427  -19.899 41.102 1.00 48.77 ? 121 GLN   A N     1 
ATOM   800  C  CA    . GLN   A 1 95  ? -5.126  -19.441 40.610 1.00 48.75 ? 121 GLN   A CA    1 
ATOM   801  C  C     . GLN   A 1 95  ? -5.008  -17.948 40.338 1.00 48.86 ? 121 GLN   A C     1 
ATOM   802  O  O     . GLN   A 1 95  ? -3.920  -17.512 39.973 1.00 49.39 ? 121 GLN   A O     1 
ATOM   803  C  CB    . GLN   A 1 95  ? -4.707  -20.221 39.357 1.00 49.19 ? 121 GLN   A CB    1 
ATOM   804  C  CG    . GLN   A 1 95  ? -4.299  -21.652 39.643 1.00 50.32 ? 121 GLN   A CG    1 
ATOM   805  C  CD    . GLN   A 1 95  ? -3.973  -22.382 38.374 1.00 52.24 ? 121 GLN   A CD    1 
ATOM   806  O  OE1   . GLN   A 1 95  ? -4.863  -22.816 37.633 1.00 52.69 ? 121 GLN   A OE1   1 
ATOM   807  N  NE2   . GLN   A 1 95  ? -2.686  -22.539 38.099 1.00 52.37 ? 121 GLN   A NE2   1 
ATOM   808  N  N     . ARG   A 1 96  ? -6.087  -17.168 40.481 1.00 48.33 ? 122 ARG   A N     1 
ATOM   809  C  CA    . ARG   A 1 96  ? -6.011  -15.728 40.219 1.00 48.33 ? 122 ARG   A CA    1 
ATOM   810  C  C     . ARG   A 1 96  ? -5.040  -15.011 41.176 1.00 48.15 ? 122 ARG   A C     1 
ATOM   811  O  O     . ARG   A 1 96  ? -4.172  -14.257 40.729 1.00 48.23 ? 122 ARG   A O     1 
ATOM   812  C  CB    . ARG   A 1 96  ? -7.400  -15.076 40.242 1.00 49.47 ? 122 ARG   A CB    1 
ATOM   813  C  CG    . ARG   A 1 96  ? -7.334  -13.569 40.036 1.00 51.95 ? 122 ARG   A CG    1 
ATOM   814  C  CD    . ARG   A 1 96  ? -8.685  -12.978 39.792 1.00 54.31 ? 122 ARG   A CD    1 
ATOM   815  N  NE    . ARG   A 1 96  ? -9.202  -13.365 38.483 1.00 56.08 ? 122 ARG   A NE    1 
ATOM   816  C  CZ    . ARG   A 1 96  ? -10.332 -12.902 37.962 1.00 57.80 ? 122 ARG   A CZ    1 
ATOM   817  N  NH1   . ARG   A 1 96  ? -11.074 -12.027 38.633 1.00 57.69 ? 122 ARG   A NH1   1 
ATOM   818  N  NH2   . ARG   A 1 96  ? -10.732 -13.310 36.768 1.00 57.05 ? 122 ARG   A NH2   1 
ATOM   819  N  N     . ARG   A 1 97  ? -5.178  -15.256 42.481 1.00 47.60 ? 123 ARG   A N     1 
ATOM   820  C  CA    . ARG   A 1 97  ? -4.306  -14.621 43.463 1.00 47.48 ? 123 ARG   A CA    1 
ATOM   821  C  C     . ARG   A 1 97  ? -2.938  -15.295 43.538 1.00 45.93 ? 123 ARG   A C     1 
ATOM   822  O  O     . ARG   A 1 97  ? -1.933  -14.619 43.779 1.00 46.33 ? 123 ARG   A O     1 
ATOM   823  C  CB    . ARG   A 1 97  ? -4.968  -14.602 44.853 1.00 49.67 ? 123 ARG   A CB    1 
ATOM   824  C  CG    . ARG   A 1 97  ? -4.157  -13.829 45.888 1.00 54.63 ? 123 ARG   A CG    1 
ATOM   825  C  CD    . ARG   A 1 97  ? -4.658  -14.000 47.312 1.00 59.73 ? 123 ARG   A CD    1 
ATOM   826  N  NE    . ARG   A 1 97  ? -4.665  -15.400 47.746 1.00 63.72 ? 123 ARG   A NE    1 
ATOM   827  C  CZ    . ARG   A 1 97  ? -5.766  -16.131 47.898 1.00 67.00 ? 123 ARG   A CZ    1 
ATOM   828  N  NH1   . ARG   A 1 97  ? -6.961  -15.609 47.638 1.00 66.76 ? 123 ARG   A NH1   1 
ATOM   829  N  NH2   . ARG   A 1 97  ? -5.681  -17.392 48.301 1.00 67.50 ? 123 ARG   A NH2   1 
ATOM   830  N  N     . SER   A 1 98  ? -2.889  -16.615 43.324 1.00 43.97 ? 124 SER   A N     1 
ATOM   831  C  CA    . SER   A 1 98  ? -1.635  -17.351 43.454 1.00 42.89 ? 124 SER   A CA    1 
ATOM   832  C  C     . SER   A 1 98  ? -0.741  -17.446 42.215 1.00 40.87 ? 124 SER   A C     1 
ATOM   833  O  O     . SER   A 1 98  ? 0.455   -17.688 42.387 1.00 41.82 ? 124 SER   A O     1 
ATOM   834  C  CB    . SER   A 1 98  ? -1.903  -18.765 43.955 1.00 44.55 ? 124 SER   A CB    1 
ATOM   835  O  OG    . SER   A 1 98  ? -2.553  -19.537 42.958 1.00 46.85 ? 124 SER   A OG    1 
ATOM   836  N  N     . ASP   A 1 99  ? -1.291  -17.372 40.990 1.00 38.04 ? 125 ASP   A N     1 
ATOM   837  C  CA    . ASP   A 1 99  ? -0.482  -17.605 39.795 1.00 35.97 ? 125 ASP   A CA    1 
ATOM   838  C  C     . ASP   A 1 99  ? -0.537  -16.536 38.685 1.00 32.39 ? 125 ASP   A C     1 
ATOM   839  O  O     . ASP   A 1 99  ? 0.501   -16.270 38.098 1.00 32.11 ? 125 ASP   A O     1 
ATOM   840  C  CB    . ASP   A 1 99  ? -0.824  -18.977 39.189 1.00 38.91 ? 125 ASP   A CB    1 
ATOM   841  C  CG    . ASP   A 1 99  ? -0.391  -20.174 40.032 1.00 45.63 ? 125 ASP   A CG    1 
ATOM   842  O  OD1   . ASP   A 1 99  ? 0.366   -19.975 41.009 1.00 45.77 ? 125 ASP   A OD1   1 
ATOM   843  O  OD2   . ASP   A 1 99  ? -0.805  -21.312 39.706 1.00 49.34 ? 125 ASP   A OD2   1 
ATOM   844  N  N     . LEU   A 1 100 ? -1.719  -15.977 38.366 1.00 29.49 ? 126 LEU   A N     1 
ATOM   845  C  CA    . LEU   A 1 100 ? -1.942  -15.024 37.274 1.00 27.38 ? 126 LEU   A CA    1 
ATOM   846  C  C     . LEU   A 1 100 ? -0.856  -13.931 37.089 1.00 25.81 ? 126 LEU   A C     1 
ATOM   847  O  O     . LEU   A 1 100 ? -0.330  -13.798 35.990 1.00 25.28 ? 126 LEU   A O     1 
ATOM   848  C  CB    . LEU   A 1 100 ? -3.330  -14.359 37.393 1.00 27.00 ? 126 LEU   A CB    1 
ATOM   849  C  CG    . LEU   A 1 100 ? -3.766  -13.520 36.185 1.00 28.30 ? 126 LEU   A CG    1 
ATOM   850  C  CD1   . LEU   A 1 100 ? -3.868  -14.361 34.936 1.00 28.86 ? 126 LEU   A CD1   1 
ATOM   851  C  CD2   . LEU   A 1 100 ? -5.086  -12.846 36.431 1.00 29.02 ? 126 LEU   A CD2   1 
ATOM   852  N  N     . ASP   A 1 101 ? -0.539  -13.152 38.138 1.00 24.99 ? 127 ASP   A N     1 
ATOM   853  C  CA    . ASP   A 1 101 ? 0.436   -12.069 38.018 1.00 25.03 ? 127 ASP   A CA    1 
ATOM   854  C  C     . ASP   A 1 101 ? 1.837   -12.545 37.839 1.00 23.95 ? 127 ASP   A C     1 
ATOM   855  O  O     . ASP   A 1 101 ? 2.592   -11.934 37.080 1.00 24.57 ? 127 ASP   A O     1 
ATOM   856  C  CB    . ASP   A 1 101 ? 0.352   -11.089 39.193 1.00 27.57 ? 127 ASP   A CB    1 
ATOM   857  C  CG    . ASP   A 1 101 ? -0.907  -10.240 39.185 1.00 33.21 ? 127 ASP   A CG    1 
ATOM   858  O  OD1   . ASP   A 1 101 ? -1.554  -10.141 38.118 1.00 34.24 ? 127 ASP   A OD1   1 
ATOM   859  O  OD2   . ASP   A 1 101 ? -1.248  -9.684  40.241 1.00 36.03 ? 127 ASP   A OD2   1 
ATOM   860  N  N     . ARG   A 1 102 ? 2.194   -13.633 38.510 1.00 22.47 ? 128 ARG   A N     1 
ATOM   861  C  CA    . ARG   A 1 102 ? 3.526   -14.221 38.368 1.00 21.62 ? 128 ARG   A CA    1 
ATOM   862  C  C     . ARG   A 1 102 ? 3.690   -14.761 36.946 1.00 20.15 ? 128 ARG   A C     1 
ATOM   863  O  O     . ARG   A 1 102 ? 4.696   -14.489 36.297 1.00 19.49 ? 128 ARG   A O     1 
ATOM   864  C  CB    . ARG   A 1 102 ? 3.753   -15.345 39.402 1.00 22.96 ? 128 ARG   A CB    1 
ATOM   865  C  CG    . ARG   A 1 102 ? 5.097   -16.065 39.194 1.00 27.09 ? 128 ARG   A CG    1 
ATOM   866  C  CD    . ARG   A 1 102 ? 5.472   -17.038 40.295 1.00 31.56 ? 128 ARG   A CD    1 
ATOM   867  N  NE    . ARG   A 1 102 ? 4.398   -17.982 40.605 1.00 37.58 ? 128 ARG   A NE    1 
ATOM   868  C  CZ    . ARG   A 1 102 ? 4.174   -19.112 39.943 1.00 41.14 ? 128 ARG   A CZ    1 
ATOM   869  N  NH1   . ARG   A 1 102 ? 4.925   -19.438 38.896 1.00 42.98 ? 128 ARG   A NH1   1 
ATOM   870  N  NH2   . ARG   A 1 102 ? 3.178   -19.910 40.302 1.00 39.74 ? 128 ARG   A NH2   1 
ATOM   871  N  N     . PHE   A 1 103 ? 2.690   -15.507 36.460 1.00 19.70 ? 129 PHE   A N     1 
ATOM   872  C  CA    . PHE   A 1 103 ? 2.723   -16.103 35.126 1.00 19.86 ? 129 PHE   A CA    1 
ATOM   873  C  C     . PHE   A 1 103 ? 2.799   -15.027 34.036 1.00 17.28 ? 129 PHE   A C     1 
ATOM   874  O  O     . PHE   A 1 103 ? 3.517   -15.211 33.060 1.00 16.36 ? 129 PHE   A O     1 
ATOM   875  C  CB    . PHE   A 1 103 ? 1.460   -16.959 34.876 1.00 21.35 ? 129 PHE   A CB    1 
ATOM   876  C  CG    . PHE   A 1 103 ? 1.448   -18.369 35.412 1.00 24.08 ? 129 PHE   A CG    1 
ATOM   877  C  CD1   . PHE   A 1 103 ? 2.482   -18.838 36.206 1.00 25.31 ? 129 PHE   A CD1   1 
ATOM   878  C  CD2   . PHE   A 1 103 ? 0.360   -19.199 35.196 1.00 26.07 ? 129 PHE   A CD2   1 
ATOM   879  C  CE1   . PHE   A 1 103 ? 2.442   -20.116 36.747 1.00 26.31 ? 129 PHE   A CE1   1 
ATOM   880  C  CE2   . PHE   A 1 103 ? 0.326   -20.481 35.736 1.00 27.05 ? 129 PHE   A CE2   1 
ATOM   881  C  CZ    . PHE   A 1 103 ? 1.369   -20.928 36.508 1.00 26.48 ? 129 PHE   A CZ    1 
ATOM   882  N  N     . TRP   A 1 104 ? 2.054   -13.911 34.202 1.00 15.83 ? 130 TRP   A N     1 
ATOM   883  C  CA    . TRP   A 1 104 ? 2.051   -12.859 33.182 1.00 15.44 ? 130 TRP   A CA    1 
ATOM   884  C  C     . TRP   A 1 104 ? 3.363   -12.118 33.125 1.00 14.79 ? 130 TRP   A C     1 
ATOM   885  O  O     . TRP   A 1 104 ? 3.859   -11.862 32.021 1.00 13.48 ? 130 TRP   A O     1 
ATOM   886  C  CB    . TRP   A 1 104 ? 0.862   -11.890 33.341 1.00 15.33 ? 130 TRP   A CB    1 
ATOM   887  C  CG    . TRP   A 1 104 ? 0.783   -10.802 32.306 1.00 16.96 ? 130 TRP   A CG    1 
ATOM   888  C  CD1   . TRP   A 1 104 ? 0.811   -9.458  32.536 1.00 18.10 ? 130 TRP   A CD1   1 
ATOM   889  C  CD2   . TRP   A 1 104 ? 0.646   -10.962 30.881 1.00 17.22 ? 130 TRP   A CD2   1 
ATOM   890  N  NE1   . TRP   A 1 104 ? 0.707   -8.771  31.344 1.00 18.76 ? 130 TRP   A NE1   1 
ATOM   891  C  CE2   . TRP   A 1 104 ? 0.598   -9.669  30.316 1.00 18.26 ? 130 TRP   A CE2   1 
ATOM   892  C  CE3   . TRP   A 1 104 ? 0.577   -12.069 30.026 1.00 17.70 ? 130 TRP   A CE3   1 
ATOM   893  C  CZ2   . TRP   A 1 104 ? 0.440   -9.455  28.943 1.00 19.05 ? 130 TRP   A CZ2   1 
ATOM   894  C  CZ3   . TRP   A 1 104 ? 0.421   -11.852 28.668 1.00 18.70 ? 130 TRP   A CZ3   1 
ATOM   895  C  CH2   . TRP   A 1 104 ? 0.367   -10.557 28.141 1.00 18.78 ? 130 TRP   A CH2   1 
ATOM   896  N  N     . LEU   A 1 105 ? 3.963   -11.809 34.302 1.00 14.67 ? 131 LEU   A N     1 
ATOM   897  C  CA    . LEU   A 1 105 ? 5.252   -11.111 34.284 1.00 15.05 ? 131 LEU   A CA    1 
ATOM   898  C  C     . LEU   A 1 105 ? 6.327   -12.037 33.674 1.00 15.13 ? 131 LEU   A C     1 
ATOM   899  O  O     . LEU   A 1 105 ? 7.102   -11.600 32.829 1.00 15.24 ? 131 LEU   A O     1 
ATOM   900  C  CB    . LEU   A 1 105 ? 5.653   -10.591 35.670 1.00 15.29 ? 131 LEU   A CB    1 
ATOM   901  C  CG    . LEU   A 1 105 ? 7.045   -9.927  35.743 1.00 17.35 ? 131 LEU   A CG    1 
ATOM   902  C  CD1   . LEU   A 1 105 ? 7.154   -8.720  34.818 1.00 17.40 ? 131 LEU   A CD1   1 
ATOM   903  C  CD2   . LEU   A 1 105 ? 7.412   -9.567  37.174 1.00 18.53 ? 131 LEU   A CD2   1 
ATOM   904  N  N     . GLU   A 1 106 ? 6.287   -13.326 34.008 1.00 14.91 ? 132 GLU   A N     1 
ATOM   905  C  CA    . GLU   A 1 106 ? 7.225   -14.301 33.438 1.00 14.96 ? 132 GLU   A CA    1 
ATOM   906  C  C     . GLU   A 1 106 ? 7.042   -14.448 31.930 1.00 15.39 ? 132 GLU   A C     1 
ATOM   907  O  O     . GLU   A 1 106 ? 8.027   -14.567 31.219 1.00 15.91 ? 132 GLU   A O     1 
ATOM   908  C  CB    . GLU   A 1 106 ? 7.091   -15.647 34.148 1.00 15.94 ? 132 GLU   A CB    1 
ATOM   909  C  CG    . GLU   A 1 106 ? 7.671   -15.602 35.549 1.00 17.85 ? 132 GLU   A CG    1 
ATOM   910  C  CD    . GLU   A 1 106 ? 7.486   -16.874 36.356 1.00 23.32 ? 132 GLU   A CD    1 
ATOM   911  O  OE1   . GLU   A 1 106 ? 6.975   -17.873 35.798 1.00 23.52 ? 132 GLU   A OE1   1 
ATOM   912  O  OE2   . GLU   A 1 106 ? 7.846   -16.869 37.556 1.00 23.46 ? 132 GLU   A OE2   1 
ATOM   913  N  N     . THR   A 1 107 ? 5.799   -14.292 31.440 1.00 14.85 ? 133 THR   A N     1 
ATOM   914  C  CA    . THR   A 1 107 ? 5.473   -14.310 30.017 1.00 14.77 ? 133 THR   A CA    1 
ATOM   915  C  C     . THR   A 1 107 ? 6.059   -13.057 29.319 1.00 15.62 ? 133 THR   A C     1 
ATOM   916  O  O     . THR   A 1 107 ? 6.703   -13.194 28.279 1.00 16.42 ? 133 THR   A O     1 
ATOM   917  C  CB    . THR   A 1 107 ? 3.958   -14.373 29.831 1.00 15.12 ? 133 THR   A CB    1 
ATOM   918  O  OG1   . THR   A 1 107 ? 3.431   -15.561 30.440 1.00 15.42 ? 133 THR   A OG1   1 
ATOM   919  C  CG2   . THR   A 1 107 ? 3.565   -14.333 28.384 1.00 15.88 ? 133 THR   A CG2   1 
ATOM   920  N  N     . LEU   A 1 108 ? 5.889   -11.864 29.920 1.00 14.80 ? 134 LEU   A N     1 
ATOM   921  C  CA    . LEU   A 1 108 ? 6.396   -10.593 29.396 1.00 14.90 ? 134 LEU   A CA    1 
ATOM   922  C  C     . LEU   A 1 108 ? 7.925   -10.636 29.283 1.00 15.26 ? 134 LEU   A C     1 
ATOM   923  O  O     . LEU   A 1 108 ? 8.482   -10.245 28.254 1.00 14.56 ? 134 LEU   A O     1 
ATOM   924  C  CB    . LEU   A 1 108 ? 5.977   -9.420  30.300 1.00 14.20 ? 134 LEU   A CB    1 
ATOM   925  C  CG    . LEU   A 1 108 ? 4.475   -9.114  30.406 1.00 16.32 ? 134 LEU   A CG    1 
ATOM   926  C  CD1   . LEU   A 1 108 ? 4.200   -8.111  31.509 1.00 16.28 ? 134 LEU   A CD1   1 
ATOM   927  C  CD2   . LEU   A 1 108 ? 3.931   -8.586  29.105 1.00 17.69 ? 134 LEU   A CD2   1 
ATOM   928  N  N     . LEU   A 1 109 ? 8.592   -11.160 30.322 1.00 15.53 ? 135 LEU   A N     1 
ATOM   929  C  CA    . LEU   A 1 109 ? 10.060  -11.283 30.354 1.00 16.68 ? 135 LEU   A CA    1 
ATOM   930  C  C     . LEU   A 1 109 ? 10.580  -12.292 29.337 1.00 17.83 ? 135 LEU   A C     1 
ATOM   931  O  O     . LEU   A 1 109 ? 11.623  -12.083 28.727 1.00 17.73 ? 135 LEU   A O     1 
ATOM   932  C  CB    . LEU   A 1 109 ? 10.531  -11.642 31.783 1.00 16.91 ? 135 LEU   A CB    1 
ATOM   933  C  CG    . LEU   A 1 109 ? 10.320  -10.511 32.789 1.00 18.91 ? 135 LEU   A CG    1 
ATOM   934  C  CD1   . LEU   A 1 109 ? 10.586  -10.979 34.230 1.00 18.55 ? 135 LEU   A CD1   1 
ATOM   935  C  CD2   . LEU   A 1 109 ? 11.222  -9.318  32.443 1.00 20.05 ? 135 LEU   A CD2   1 
ATOM   936  N  N     . CYS   A 1 110 ? 9.823   -13.367 29.117 1.00 19.01 ? 136 CYS   A N     1 
ATOM   937  C  CA    . CYS   A 1 110 ? 10.076  -14.394 28.110 1.00 20.34 ? 136 CYS   A CA    1 
ATOM   938  C  C     . CYS   A 1 110 ? 10.132  -13.728 26.718 1.00 20.34 ? 136 CYS   A C     1 
ATOM   939  O  O     . CYS   A 1 110 ? 11.036  -14.012 25.927 1.00 21.19 ? 136 CYS   A O     1 
ATOM   940  C  CB    . CYS   A 1 110 ? 8.941   -15.414 28.148 1.00 23.22 ? 136 CYS   A CB    1 
ATOM   941  S  SG    . CYS   A 1 110 ? 9.460   -17.107 28.455 1.00 33.53 ? 136 CYS   A SG    1 
ATOM   942  N  N     . LEU   A 1 111 ? 9.138   -12.868 26.424 1.00 18.65 ? 137 LEU   A N     1 
ATOM   943  C  CA    . LEU   A 1 111 ? 9.000   -12.152 25.151 1.00 18.16 ? 137 LEU   A CA    1 
ATOM   944  C  C     . LEU   A 1 111 ? 10.128  -11.161 24.917 1.00 16.95 ? 137 LEU   A C     1 
ATOM   945  O  O     . LEU   A 1 111 ? 10.891  -11.314 23.978 1.00 16.91 ? 137 LEU   A O     1 
ATOM   946  C  CB    . LEU   A 1 111 ? 7.644   -11.388 25.093 1.00 18.02 ? 137 LEU   A CB    1 
ATOM   947  C  CG    . LEU   A 1 111 ? 6.365   -12.209 24.982 1.00 20.55 ? 137 LEU   A CG    1 
ATOM   948  C  CD1   . LEU   A 1 111 ? 5.137   -11.280 24.801 1.00 21.51 ? 137 LEU   A CD1   1 
ATOM   949  C  CD2   . LEU   A 1 111 ? 6.423   -13.149 23.821 1.00 20.87 ? 137 LEU   A CD2   1 
ATOM   950  N  N     . ILE   A 1 112 ? 10.268  -10.175 25.807 1.00 16.00 ? 138 ILE   A N     1 
ATOM   951  C  CA    . ILE   A 1 112 ? 11.222  -9.093  25.644 1.00 15.76 ? 138 ILE   A CA    1 
ATOM   952  C  C     . ILE   A 1 112 ? 12.677  -9.541  25.792 1.00 15.64 ? 138 ILE   A C     1 
ATOM   953  O  O     . ILE   A 1 112 ? 13.570  -8.865  25.254 1.00 15.43 ? 138 ILE   A O     1 
ATOM   954  C  CB    . ILE   A 1 112 ? 10.882  -7.903  26.569 1.00 15.87 ? 138 ILE   A CB    1 
ATOM   955  C  CG1   . ILE   A 1 112 ? 11.166  -8.263  28.054 1.00 16.67 ? 138 ILE   A CG1   1 
ATOM   956  C  CG2   . ILE   A 1 112 ? 9.432   -7.473  26.350 1.00 16.02 ? 138 ILE   A CG2   1 
ATOM   957  C  CD1   . ILE   A 1 112 ? 11.275  -7.063  29.026 1.00 18.49 ? 138 ILE   A CD1   1 
ATOM   958  N  N     . GLY   A 1 113 ? 12.898  -10.637 26.518 1.00 15.13 ? 139 GLY   A N     1 
ATOM   959  C  CA    . GLY   A 1 113 ? 14.222  -11.231 26.687 1.00 16.11 ? 139 GLY   A CA    1 
ATOM   960  C  C     . GLY   A 1 113 ? 14.597  -12.188 25.562 1.00 17.12 ? 139 GLY   A C     1 
ATOM   961  O  O     . GLY   A 1 113 ? 15.699  -12.731 25.565 1.00 17.62 ? 139 GLY   A O     1 
ATOM   962  N  N     . GLU   A 1 114 ? 13.706  -12.398 24.569 1.00 17.46 ? 140 GLU   A N     1 
ATOM   963  C  CA    . GLU   A 1 114 ? 13.980  -13.258 23.412 1.00 18.69 ? 140 GLU   A CA    1 
ATOM   964  C  C     . GLU   A 1 114 ? 14.391  -14.671 23.859 1.00 19.91 ? 140 GLU   A C     1 
ATOM   965  O  O     . GLU   A 1 114 ? 15.419  -15.181 23.437 1.00 19.90 ? 140 GLU   A O     1 
ATOM   966  C  CB    . GLU   A 1 114 ? 15.054  -12.634 22.475 1.00 20.39 ? 140 GLU   A CB    1 
ATOM   967  C  CG    . GLU   A 1 114 ? 14.735  -11.229 22.001 1.00 25.47 ? 140 GLU   A CG    1 
ATOM   968  C  CD    . GLU   A 1 114 ? 13.534  -11.123 21.072 1.00 34.15 ? 140 GLU   A CD    1 
ATOM   969  O  OE1   . GLU   A 1 114 ? 13.169  -12.151 20.461 1.00 37.23 ? 140 GLU   A OE1   1 
ATOM   970  O  OE2   . GLU   A 1 114 ? 12.968  -10.013 20.939 1.00 34.94 ? 140 GLU   A OE2   1 
ATOM   971  N  N     . SER   A 1 115 ? 13.607  -15.276 24.753 1.00 20.00 ? 141 SER   A N     1 
ATOM   972  C  CA    . SER   A 1 115 ? 13.951  -16.565 25.327 1.00 20.38 ? 141 SER   A CA    1 
ATOM   973  C  C     . SER   A 1 115 ? 13.863  -17.745 24.366 1.00 20.16 ? 141 SER   A C     1 
ATOM   974  O  O     . SER   A 1 115 ? 14.304  -18.830 24.722 1.00 19.96 ? 141 SER   A O     1 
ATOM   975  C  CB    . SER   A 1 115 ? 13.058  -16.841 26.531 1.00 21.39 ? 141 SER   A CB    1 
ATOM   976  O  OG    . SER   A 1 115 ? 13.205  -15.798 27.472 1.00 23.21 ? 141 SER   A OG    1 
ATOM   977  N  N     . PHE   A 1 116 ? 13.271  -17.557 23.191 1.00 20.05 ? 142 PHE   A N     1 
ATOM   978  C  CA    . PHE   A 1 116 ? 13.075  -18.654 22.245 1.00 21.01 ? 142 PHE   A CA    1 
ATOM   979  C  C     . PHE   A 1 116 ? 14.198  -18.781 21.203 1.00 23.45 ? 142 PHE   A C     1 
ATOM   980  O  O     . PHE   A 1 116 ? 14.062  -19.540 20.233 1.00 23.80 ? 142 PHE   A O     1 
ATOM   981  C  CB    . PHE   A 1 116 ? 11.685  -18.559 21.600 1.00 19.65 ? 142 PHE   A CB    1 
ATOM   982  C  CG    . PHE   A 1 116 ? 10.599  -18.451 22.648 1.00 19.06 ? 142 PHE   A CG    1 
ATOM   983  C  CD1   . PHE   A 1 116 ? 10.285  -19.529 23.455 1.00 18.90 ? 142 PHE   A CD1   1 
ATOM   984  C  CD2   . PHE   A 1 116 ? 9.965   -17.242 22.892 1.00 19.15 ? 142 PHE   A CD2   1 
ATOM   985  C  CE1   . PHE   A 1 116 ? 9.295   -19.425 24.426 1.00 19.58 ? 142 PHE   A CE1   1 
ATOM   986  C  CE2   . PHE   A 1 116 ? 8.979   -17.136 23.869 1.00 19.18 ? 142 PHE   A CE2   1 
ATOM   987  C  CZ    . PHE   A 1 116 ? 8.638   -18.231 24.618 1.00 18.99 ? 142 PHE   A CZ    1 
ATOM   988  N  N     . ASP   A 1 117 ? 15.332  -18.079 21.440 1.00 24.86 ? 143 ASP   A N     1 
ATOM   989  C  CA    . ASP   A 1 117 ? 16.544  -18.130 20.646 1.00 26.54 ? 143 ASP   A CA    1 
ATOM   990  C  C     . ASP   A 1 117 ? 16.276  -18.056 19.107 1.00 26.87 ? 143 ASP   A C     1 
ATOM   991  O  O     . ASP   A 1 117 ? 15.747  -17.049 18.666 1.00 26.36 ? 143 ASP   A O     1 
ATOM   992  C  CB    . ASP   A 1 117 ? 17.381  -19.355 21.077 1.00 29.65 ? 143 ASP   A CB    1 
ATOM   993  C  CG    . ASP   A 1 117 ? 18.104  -19.178 22.402 1.00 37.74 ? 143 ASP   A CG    1 
ATOM   994  O  OD1   . ASP   A 1 117 ? 17.913  -18.122 23.056 1.00 39.84 ? 143 ASP   A OD1   1 
ATOM   995  O  OD2   . ASP   A 1 117 ? 18.867  -20.082 22.781 1.00 41.53 ? 143 ASP   A OD2   1 
ATOM   996  N  N     . ASP   A 1 118 ? 16.648  -19.076 18.309 1.00 27.48 ? 144 ASP   A N     1 
ATOM   997  C  CA    . ASP   A 1 118 ? 16.483  -19.064 16.859 1.00 28.47 ? 144 ASP   A CA    1 
ATOM   998  C  C     . ASP   A 1 118 ? 15.042  -19.066 16.385 1.00 28.15 ? 144 ASP   A C     1 
ATOM   999  O  O     . ASP   A 1 118 ? 14.807  -18.838 15.203 1.00 28.66 ? 144 ASP   A O     1 
ATOM   1000 C  CB    . ASP   A 1 118 ? 17.259  -20.225 16.211 1.00 31.26 ? 144 ASP   A CB    1 
ATOM   1001 C  CG    . ASP   A 1 118 ? 18.740  -20.200 16.534 1.00 39.29 ? 144 ASP   A CG    1 
ATOM   1002 O  OD1   . ASP   A 1 118 ? 19.313  -19.086 16.629 1.00 40.69 ? 144 ASP   A OD1   1 
ATOM   1003 O  OD2   . ASP   A 1 118 ? 19.327  -21.287 16.694 1.00 42.95 ? 144 ASP   A OD2   1 
ATOM   1004 N  N     . TYR   A 1 119 ? 14.081  -19.352 17.266 1.00 27.38 ? 145 TYR   A N     1 
ATOM   1005 C  CA    . TYR   A 1 119 ? 12.670  -19.321 16.888 1.00 27.22 ? 145 TYR   A CA    1 
ATOM   1006 C  C     . TYR   A 1 119 ? 11.963  -18.041 17.368 1.00 27.00 ? 145 TYR   A C     1 
ATOM   1007 O  O     . TYR   A 1 119 ? 10.741  -17.991 17.384 1.00 26.25 ? 145 TYR   A O     1 
ATOM   1008 C  CB    . TYR   A 1 119 ? 11.952  -20.565 17.393 1.00 27.59 ? 145 TYR   A CB    1 
ATOM   1009 C  CG    . TYR   A 1 119 ? 12.614  -21.844 16.931 1.00 28.96 ? 145 TYR   A CG    1 
ATOM   1010 C  CD1   . TYR   A 1 119 ? 12.610  -22.209 15.594 1.00 30.19 ? 145 TYR   A CD1   1 
ATOM   1011 C  CD2   . TYR   A 1 119 ? 13.265  -22.675 17.829 1.00 30.19 ? 145 TYR   A CD2   1 
ATOM   1012 C  CE1   . TYR   A 1 119 ? 13.195  -23.395 15.167 1.00 31.56 ? 145 TYR   A CE1   1 
ATOM   1013 C  CE2   . TYR   A 1 119 ? 13.858  -23.862 17.416 1.00 31.45 ? 145 TYR   A CE2   1 
ATOM   1014 C  CZ    . TYR   A 1 119 ? 13.818  -24.220 16.084 1.00 32.87 ? 145 TYR   A CZ    1 
ATOM   1015 O  OH    . TYR   A 1 119 ? 14.439  -25.376 15.678 1.00 36.20 ? 145 TYR   A OH    1 
ATOM   1016 N  N     . SER   A 1 120 ? 12.743  -17.002 17.736 1.00 27.32 ? 146 SER   A N     1 
ATOM   1017 C  CA    . SER   A 1 120 ? 12.278  -15.696 18.180 1.00 27.90 ? 146 SER   A CA    1 
ATOM   1018 C  C     . SER   A 1 120 ? 11.429  -15.008 17.137 1.00 26.73 ? 146 SER   A C     1 
ATOM   1019 O  O     . SER   A 1 120 ? 10.433  -14.376 17.480 1.00 26.48 ? 146 SER   A O     1 
ATOM   1020 C  CB    . SER   A 1 120 ? 13.481  -14.814 18.507 1.00 30.70 ? 146 SER   A CB    1 
ATOM   1021 O  OG    . SER   A 1 120 ? 14.125  -15.297 19.677 1.00 33.11 ? 146 SER   A OG    1 
ATOM   1022 N  N     . ASP   A 1 121 ? 11.798  -15.152 15.862 1.00 26.26 ? 147 ASP   A N     1 
ATOM   1023 C  CA    . ASP   A 1 121 ? 11.045  -14.524 14.790 1.00 27.22 ? 147 ASP   A CA    1 
ATOM   1024 C  C     . ASP   A 1 121 ? 9.654   -15.117 14.608 1.00 26.51 ? 147 ASP   A C     1 
ATOM   1025 O  O     . ASP   A 1 121 ? 8.793   -14.443 14.063 1.00 27.32 ? 147 ASP   A O     1 
ATOM   1026 C  CB    . ASP   A 1 121 ? 11.839  -14.521 13.486 1.00 30.71 ? 147 ASP   A CB    1 
ATOM   1027 C  CG    . ASP   A 1 121 ? 13.088  -13.663 13.612 1.00 39.67 ? 147 ASP   A CG    1 
ATOM   1028 O  OD1   . ASP   A 1 121 ? 12.948  -12.428 13.782 1.00 40.91 ? 147 ASP   A OD1   1 
ATOM   1029 O  OD2   . ASP   A 1 121 ? 14.205  -14.231 13.584 1.00 43.39 ? 147 ASP   A OD2   1 
ATOM   1030 N  N     . ASP   A 1 122 ? 9.415   -16.359 15.072 1.00 25.26 ? 148 ASP   A N     1 
ATOM   1031 C  CA    . ASP   A 1 122 ? 8.090   -16.970 14.976 1.00 24.33 ? 148 ASP   A CA    1 
ATOM   1032 C  C     . ASP   A 1 122 ? 7.126   -16.402 16.021 1.00 22.62 ? 148 ASP   A C     1 
ATOM   1033 O  O     . ASP   A 1 122 ? 5.925   -16.567 15.863 1.00 23.30 ? 148 ASP   A O     1 
ATOM   1034 C  CB    . ASP   A 1 122 ? 8.165   -18.494 15.103 1.00 27.12 ? 148 ASP   A CB    1 
ATOM   1035 C  CG    . ASP   A 1 122 ? 8.293   -19.192 13.761 1.00 35.58 ? 148 ASP   A CG    1 
ATOM   1036 O  OD1   . ASP   A 1 122 ? 9.374   -19.106 13.152 1.00 38.28 ? 148 ASP   A OD1   1 
ATOM   1037 O  OD2   . ASP   A 1 122 ? 7.307   -19.829 13.321 1.00 37.74 ? 148 ASP   A OD2   1 
ATOM   1038 N  N     . VAL   A 1 123 ? 7.632   -15.771 17.084 1.00 19.80 ? 149 VAL   A N     1 
ATOM   1039 C  CA    . VAL   A 1 123 ? 6.829   -15.204 18.153 1.00 18.89 ? 149 VAL   A CA    1 
ATOM   1040 C  C     . VAL   A 1 123 ? 6.208   -13.874 17.754 1.00 18.31 ? 149 VAL   A C     1 
ATOM   1041 O  O     . VAL   A 1 123 ? 6.899   -12.998 17.249 1.00 17.87 ? 149 VAL   A O     1 
ATOM   1042 C  CB    . VAL   A 1 123 ? 7.659   -15.030 19.448 1.00 19.50 ? 149 VAL   A CB    1 
ATOM   1043 C  CG1   . VAL   A 1 123 ? 6.791   -14.456 20.568 1.00 20.16 ? 149 VAL   A CG1   1 
ATOM   1044 C  CG2   . VAL   A 1 123 ? 8.286   -16.354 19.874 1.00 19.78 ? 149 VAL   A CG2   1 
ATOM   1045 N  N     . CYS   A 1 124 ? 4.920   -13.694 18.028 1.00 17.41 ? 150 CYS   A N     1 
ATOM   1046 C  CA    . CYS   A 1 124 ? 4.215   -12.454 17.715 1.00 17.01 ? 150 CYS   A CA    1 
ATOM   1047 C  C     . CYS   A 1 124 ? 3.922   -11.651 18.969 1.00 15.91 ? 150 CYS   A C     1 
ATOM   1048 O  O     . CYS   A 1 124 ? 4.060   -10.435 18.967 1.00 15.99 ? 150 CYS   A O     1 
ATOM   1049 C  CB    . CYS   A 1 124 ? 2.936   -12.766 16.952 1.00 17.66 ? 150 CYS   A CB    1 
ATOM   1050 S  SG    . CYS   A 1 124 ? 3.236   -13.540 15.352 1.00 21.38 ? 150 CYS   A SG    1 
ATOM   1051 N  N     . GLY   A 1 125 ? 3.509   -12.335 20.022 1.00 14.92 ? 151 GLY   A N     1 
ATOM   1052 C  CA    . GLY   A 1 125 ? 3.203   -11.692 21.285 1.00 14.62 ? 151 GLY   A CA    1 
ATOM   1053 C  C     . GLY   A 1 125 ? 2.476   -12.610 22.242 1.00 14.45 ? 151 GLY   A C     1 
ATOM   1054 O  O     . GLY   A 1 125 ? 2.524   -13.837 22.099 1.00 13.89 ? 151 GLY   A O     1 
ATOM   1055 N  N     . ALA   A 1 126 ? 1.883   -12.017 23.285 1.00 13.60 ? 152 ALA   A N     1 
ATOM   1056 C  CA    . ALA   A 1 126 ? 1.166   -12.768 24.299 1.00 13.33 ? 152 ALA   A CA    1 
ATOM   1057 C  C     . ALA   A 1 126 ? -0.085  -12.028 24.731 1.00 13.06 ? 152 ALA   A C     1 
ATOM   1058 O  O     . ALA   A 1 126 ? -0.124  -10.815 24.649 1.00 11.71 ? 152 ALA   A O     1 
ATOM   1059 C  CB    . ALA   A 1 126 ? 2.066   -12.999 25.512 1.00 13.64 ? 152 ALA   A CB    1 
ATOM   1060 N  N     . VAL   A 1 127 ? -1.084  -12.754 25.260 1.00 13.82 ? 153 VAL   A N     1 
ATOM   1061 C  CA    . VAL   A 1 127 ? -2.340  -12.148 25.692 1.00 14.45 ? 153 VAL   A CA    1 
ATOM   1062 C  C     . VAL   A 1 127 ? -2.745  -12.760 27.028 1.00 15.15 ? 153 VAL   A C     1 
ATOM   1063 O  O     . VAL   A 1 127 ? -2.653  -13.978 27.213 1.00 14.37 ? 153 VAL   A O     1 
ATOM   1064 C  CB    . VAL   A 1 127 ? -3.469  -12.464 24.659 1.00 15.60 ? 153 VAL   A CB    1 
ATOM   1065 C  CG1   . VAL   A 1 127 ? -4.806  -11.855 25.088 1.00 16.78 ? 153 VAL   A CG1   1 
ATOM   1066 C  CG2   . VAL   A 1 127 ? -3.098  -12.014 23.243 1.00 15.88 ? 153 VAL   A CG2   1 
ATOM   1067 N  N     . VAL   A 1 128 ? -3.309  -11.942 27.912 1.00 15.43 ? 154 VAL   A N     1 
ATOM   1068 C  CA    . VAL   A 1 128 ? -3.849  -12.445 29.151 1.00 16.35 ? 154 VAL   A CA    1 
ATOM   1069 C  C     . VAL   A 1 128 ? -5.321  -12.015 29.170 1.00 17.50 ? 154 VAL   A C     1 
ATOM   1070 O  O     . VAL   A 1 128 ? -5.628  -10.852 28.965 1.00 17.11 ? 154 VAL   A O     1 
ATOM   1071 C  CB    . VAL   A 1 128 ? -3.021  -12.019 30.401 1.00 16.77 ? 154 VAL   A CB    1 
ATOM   1072 C  CG1   . VAL   A 1 128 ? -2.859  -10.497 30.467 1.00 17.63 ? 154 VAL   A CG1   1 
ATOM   1073 C  CG2   . VAL   A 1 128 ? -3.646  -12.549 31.685 1.00 17.16 ? 154 VAL   A CG2   1 
ATOM   1074 N  N     . ASN   A 1 129 ? -6.225  -12.977 29.339 1.00 18.68 ? 155 ASN   A N     1 
ATOM   1075 C  CA    . ASN   A 1 129 ? -7.659  -12.763 29.433 1.00 19.83 ? 155 ASN   A CA    1 
ATOM   1076 C  C     . ASN   A 1 129 ? -8.062  -12.927 30.888 1.00 21.25 ? 155 ASN   A C     1 
ATOM   1077 O  O     . ASN   A 1 129 ? -7.847  -13.992 31.475 1.00 21.08 ? 155 ASN   A O     1 
ATOM   1078 C  CB    . ASN   A 1 129 ? -8.409  -13.793 28.601 1.00 20.13 ? 155 ASN   A CB    1 
ATOM   1079 C  CG    . ASN   A 1 129 ? -7.977  -13.831 27.159 1.00 23.50 ? 155 ASN   A CG    1 
ATOM   1080 O  OD1   . ASN   A 1 129 ? -7.400  -14.806 26.678 1.00 25.00 ? 155 ASN   A OD1   1 
ATOM   1081 N  ND2   . ASN   A 1 129 ? -8.232  -12.767 26.438 1.00 24.21 ? 155 ASN   A ND2   1 
ATOM   1082 N  N     . VAL   A 1 130 ? -8.658  -11.891 31.467 1.00 21.86 ? 156 VAL   A N     1 
ATOM   1083 C  CA    . VAL   A 1 130 ? -9.124  -11.942 32.846 1.00 23.32 ? 156 VAL   A CA    1 
ATOM   1084 C  C     . VAL   A 1 130 ? -10.613 -12.193 32.769 1.00 25.29 ? 156 VAL   A C     1 
ATOM   1085 O  O     . VAL   A 1 130 ? -11.329 -11.412 32.136 1.00 25.33 ? 156 VAL   A O     1 
ATOM   1086 C  CB    . VAL   A 1 130 ? -8.738  -10.639 33.575 1.00 24.17 ? 156 VAL   A CB    1 
ATOM   1087 C  CG1   . VAL   A 1 130 ? -9.396  -10.540 34.947 1.00 24.92 ? 156 VAL   A CG1   1 
ATOM   1088 C  CG2   . VAL   A 1 130 ? -7.222  -10.540 33.677 1.00 24.51 ? 156 VAL   A CG2   1 
ATOM   1089 N  N     . ARG   A 1 131 ? -11.063 -13.358 33.292 1.00 26.45 ? 157 ARG   A N     1 
ATOM   1090 C  CA    . ARG   A 1 131 ? -12.447 -13.828 33.190 1.00 27.79 ? 157 ARG   A CA    1 
ATOM   1091 C  C     . ARG   A 1 131 ? -12.897 -14.448 34.504 1.00 30.01 ? 157 ARG   A C     1 
ATOM   1092 O  O     . ARG   A 1 131 ? -12.104 -15.118 35.176 1.00 30.81 ? 157 ARG   A O     1 
ATOM   1093 C  CB    . ARG   A 1 131 ? -12.579 -14.910 32.095 1.00 28.15 ? 157 ARG   A CB    1 
ATOM   1094 C  CG    . ARG   A 1 131 ? -12.135 -14.514 30.684 1.00 29.97 ? 157 ARG   A CG    1 
ATOM   1095 C  CD    . ARG   A 1 131 ? -13.093 -13.518 30.048 1.00 31.13 ? 157 ARG   A CD    1 
ATOM   1096 N  NE    . ARG   A 1 131 ? -12.756 -13.218 28.654 1.00 30.39 ? 157 ARG   A NE    1 
ATOM   1097 C  CZ    . ARG   A 1 131 ? -11.899 -12.272 28.274 1.00 30.36 ? 157 ARG   A CZ    1 
ATOM   1098 N  NH1   . ARG   A 1 131 ? -11.250 -11.549 29.181 1.00 27.86 ? 157 ARG   A NH1   1 
ATOM   1099 N  NH2   . ARG   A 1 131 ? -11.660 -12.063 26.985 1.00 29.80 ? 157 ARG   A NH2   1 
ATOM   1100 N  N     . ALA   A 1 132 ? -14.172 -14.260 34.843 1.00 30.50 ? 158 ALA   A N     1 
ATOM   1101 C  CA    . ALA   A 1 132 ? -14.791 -14.788 36.053 1.00 32.19 ? 158 ALA   A CA    1 
ATOM   1102 C  C     . ALA   A 1 132 ? -14.789 -16.316 36.059 1.00 33.86 ? 158 ALA   A C     1 
ATOM   1103 O  O     . ALA   A 1 132 ? -14.593 -16.913 37.114 1.00 34.33 ? 158 ALA   A O     1 
ATOM   1104 C  CB    . ALA   A 1 132 ? -16.214 -14.261 36.176 1.00 32.25 ? 158 ALA   A CB    1 
ATOM   1105 N  N     . LYS   A 1 133 ? -14.979 -16.942 34.876 1.00 34.60 ? 159 LYS   A N     1 
ATOM   1106 C  CA    . LYS   A 1 133 ? -14.971 -18.399 34.678 1.00 35.77 ? 159 LYS   A CA    1 
ATOM   1107 C  C     . LYS   A 1 133 ? -13.572 -19.020 34.802 1.00 36.11 ? 159 LYS   A C     1 
ATOM   1108 O  O     . LYS   A 1 133 ? -13.450 -20.222 35.038 1.00 36.98 ? 159 LYS   A O     1 
ATOM   1109 C  CB    . LYS   A 1 133 ? -15.515 -18.745 33.280 1.00 38.40 ? 159 LYS   A CB    1 
ATOM   1110 C  CG    . LYS   A 1 133 ? -16.970 -19.202 33.274 1.00 44.10 ? 159 LYS   A CG    1 
ATOM   1111 C  CD    . LYS   A 1 133 ? -17.306 -19.977 32.008 1.00 49.86 ? 159 LYS   A CD    1 
ATOM   1112 C  CE    . LYS   A 1 133 ? -18.610 -20.734 32.134 1.00 55.08 ? 159 LYS   A CE    1 
ATOM   1113 N  NZ    . LYS   A 1 133 ? -18.956 -21.462 30.879 1.00 58.06 ? 159 LYS   A NZ    1 
ATOM   1114 N  N     . GLY   A 1 134 ? -12.536 -18.231 34.554 1.00 34.87 ? 160 GLY   A N     1 
ATOM   1115 C  CA    . GLY   A 1 134 ? -11.166 -18.719 34.602 1.00 33.42 ? 160 GLY   A CA    1 
ATOM   1116 C  C     . GLY   A 1 134 ? -10.256 -17.913 33.706 1.00 31.39 ? 160 GLY   A C     1 
ATOM   1117 O  O     . GLY   A 1 134 ? -10.574 -17.661 32.543 1.00 31.63 ? 160 GLY   A O     1 
ATOM   1118 N  N     . ASP   A 1 135 ? -9.121  -17.505 34.235 1.00 29.68 ? 161 ASP   A N     1 
ATOM   1119 C  CA    . ASP   A 1 135 ? -8.157  -16.700 33.481 1.00 28.25 ? 161 ASP   A CA    1 
ATOM   1120 C  C     . ASP   A 1 135 ? -7.389  -17.533 32.442 1.00 26.27 ? 161 ASP   A C     1 
ATOM   1121 O  O     . ASP   A 1 135 ? -7.289  -18.759 32.573 1.00 25.98 ? 161 ASP   A O     1 
ATOM   1122 C  CB    . ASP   A 1 135 ? -7.210  -15.999 34.448 1.00 30.35 ? 161 ASP   A CB    1 
ATOM   1123 C  CG    . ASP   A 1 135 ? -7.986  -15.246 35.509 1.00 37.27 ? 161 ASP   A CG    1 
ATOM   1124 O  OD1   . ASP   A 1 135 ? -9.034  -14.642 35.160 1.00 37.09 ? 161 ASP   A OD1   1 
ATOM   1125 O  OD2   . ASP   A 1 135 ? -7.583  -15.308 36.700 1.00 40.75 ? 161 ASP   A OD2   1 
ATOM   1126 N  N     . LYS   A 1 136 ? -6.886  -16.868 31.386 1.00 24.44 ? 162 LYS   A N     1 
ATOM   1127 C  CA    . LYS   A 1 136 ? -6.123  -17.529 30.329 1.00 22.83 ? 162 LYS   A CA    1 
ATOM   1128 C  C     . LYS   A 1 136 ? -4.910  -16.693 29.926 1.00 20.73 ? 162 LYS   A C     1 
ATOM   1129 O  O     . LYS   A 1 136 ? -4.996  -15.468 29.871 1.00 20.38 ? 162 LYS   A O     1 
ATOM   1130 C  CB    . LYS   A 1 136 ? -7.004  -17.768 29.079 1.00 24.33 ? 162 LYS   A CB    1 
ATOM   1131 C  CG    . LYS   A 1 136 ? -8.186  -18.708 29.309 1.00 29.17 ? 162 LYS   A CG    1 
ATOM   1132 C  CD    . LYS   A 1 136 ? -8.955  -18.945 28.026 1.00 34.34 ? 162 LYS   A CD    1 
ATOM   1133 C  CE    . LYS   A 1 136 ? -10.222 -18.136 27.972 1.00 38.80 ? 162 LYS   A CE    1 
ATOM   1134 N  NZ    . LYS   A 1 136 ? -10.772 -18.070 26.587 1.00 40.83 ? 162 LYS   A NZ    1 
ATOM   1135 N  N     . ILE   A 1 137 ? -3.792  -17.349 29.638 1.00 18.93 ? 163 ILE   A N     1 
ATOM   1136 C  CA    . ILE   A 1 137 ? -2.584  -16.697 29.134 1.00 19.10 ? 163 ILE   A CA    1 
ATOM   1137 C  C     . ILE   A 1 137 ? -2.163  -17.472 27.877 1.00 18.64 ? 163 ILE   A C     1 
ATOM   1138 O  O     . ILE   A 1 137 ? -2.258  -18.709 27.847 1.00 18.64 ? 163 ILE   A O     1 
ATOM   1139 C  CB    . ILE   A 1 137 ? -1.433  -16.585 30.181 1.00 20.09 ? 163 ILE   A CB    1 
ATOM   1140 C  CG1   . ILE   A 1 137 ? -1.926  -15.826 31.443 1.00 21.52 ? 163 ILE   A CG1   1 
ATOM   1141 C  CG2   . ILE   A 1 137 ? -0.229  -15.838 29.580 1.00 20.63 ? 163 ILE   A CG2   1 
ATOM   1142 C  CD1   . ILE   A 1 137 ? -0.913  -15.733 32.571 1.00 23.11 ? 163 ILE   A CD1   1 
ATOM   1143 N  N     . ALA   A 1 138 ? -1.755  -16.757 26.832 1.00 17.52 ? 164 ALA   A N     1 
ATOM   1144 C  CA    . ALA   A 1 138 ? -1.360  -17.406 25.596 1.00 17.58 ? 164 ALA   A CA    1 
ATOM   1145 C  C     . ALA   A 1 138 ? -0.192  -16.742 24.942 1.00 17.92 ? 164 ALA   A C     1 
ATOM   1146 O  O     . ALA   A 1 138 ? -0.061  -15.536 25.046 1.00 18.29 ? 164 ALA   A O     1 
ATOM   1147 C  CB    . ALA   A 1 138 ? -2.537  -17.440 24.623 1.00 17.66 ? 164 ALA   A CB    1 
ATOM   1148 N  N     . ILE   A 1 139 ? 0.668   -17.521 24.263 1.00 17.51 ? 165 ILE   A N     1 
ATOM   1149 C  CA    . ILE   A 1 139 ? 1.733   -16.945 23.460 1.00 17.94 ? 165 ILE   A CA    1 
ATOM   1150 C  C     . ILE   A 1 139 ? 1.315   -17.218 22.013 1.00 17.28 ? 165 ILE   A C     1 
ATOM   1151 O  O     . ILE   A 1 139 ? 1.019   -18.357 21.657 1.00 17.32 ? 165 ILE   A O     1 
ATOM   1152 C  CB    . ILE   A 1 139 ? 3.154   -17.493 23.756 1.00 19.69 ? 165 ILE   A CB    1 
ATOM   1153 C  CG1   . ILE   A 1 139 ? 3.676   -16.922 25.102 1.00 21.86 ? 165 ILE   A CG1   1 
ATOM   1154 C  CG2   . ILE   A 1 139 ? 4.125   -17.159 22.571 1.00 19.83 ? 165 ILE   A CG2   1 
ATOM   1155 C  CD1   . ILE   A 1 139 ? 5.217   -17.004 25.337 1.00 24.16 ? 165 ILE   A CD1   1 
ATOM   1156 N  N     . TRP   A 1 140 ? 1.275   -16.165 21.203 1.00 16.20 ? 166 TRP   A N     1 
ATOM   1157 C  CA    . TRP   A 1 140 ? 0.872   -16.182 19.799 1.00 15.52 ? 166 TRP   A CA    1 
ATOM   1158 C  C     . TRP   A 1 140 ? 2.071   -16.314 18.879 1.00 16.04 ? 166 TRP   A C     1 
ATOM   1159 O  O     . TRP   A 1 140 ? 3.059   -15.583 19.044 1.00 16.47 ? 166 TRP   A O     1 
ATOM   1160 C  CB    . TRP   A 1 140 ? 0.114   -14.895 19.481 1.00 14.33 ? 166 TRP   A CB    1 
ATOM   1161 C  CG    . TRP   A 1 140 ? -1.308  -14.877 19.957 1.00 13.96 ? 166 TRP   A CG    1 
ATOM   1162 C  CD1   . TRP   A 1 140 ? -1.798  -15.384 21.124 1.00 14.56 ? 166 TRP   A CD1   1 
ATOM   1163 C  CD2   . TRP   A 1 140 ? -2.409  -14.258 19.297 1.00 13.42 ? 166 TRP   A CD2   1 
ATOM   1164 N  NE1   . TRP   A 1 140 ? -3.127  -15.080 21.249 1.00 13.99 ? 166 TRP   A NE1   1 
ATOM   1165 C  CE2   . TRP   A 1 140 ? -3.534  -14.408 20.128 1.00 14.11 ? 166 TRP   A CE2   1 
ATOM   1166 C  CE3   . TRP   A 1 140 ? -2.546  -13.555 18.091 1.00 13.54 ? 166 TRP   A CE3   1 
ATOM   1167 C  CZ2   . TRP   A 1 140 ? -4.793  -13.913 19.773 1.00 14.51 ? 166 TRP   A CZ2   1 
ATOM   1168 C  CZ3   . TRP   A 1 140 ? -3.783  -13.046 17.760 1.00 14.29 ? 166 TRP   A CZ3   1 
ATOM   1169 C  CH2   . TRP   A 1 140 ? -4.887  -13.230 18.593 1.00 14.54 ? 166 TRP   A CH2   1 
ATOM   1170 N  N     . THR   A 1 141 ? 2.003   -17.265 17.919 1.00 15.38 ? 167 THR   A N     1 
ATOM   1171 C  CA    . THR   A 1 141 ? 3.076   -17.491 16.954 1.00 16.02 ? 167 THR   A CA    1 
ATOM   1172 C  C     . THR   A 1 141 ? 2.542   -17.286 15.519 1.00 16.67 ? 167 THR   A C     1 
ATOM   1173 O  O     . THR   A 1 141 ? 1.334   -17.352 15.280 1.00 16.48 ? 167 THR   A O     1 
ATOM   1174 C  CB    . THR   A 1 141 ? 3.820   -18.849 17.184 1.00 17.68 ? 167 THR   A CB    1 
ATOM   1175 O  OG1   . THR   A 1 141 ? 3.220   -19.883 16.403 1.00 18.60 ? 167 THR   A OG1   1 
ATOM   1176 C  CG2   . THR   A 1 141 ? 3.936   -19.250 18.687 1.00 17.37 ? 167 THR   A CG2   1 
ATOM   1177 N  N     . THR   A 1 142 ? 3.439   -17.014 14.584 1.00 17.10 ? 168 THR   A N     1 
ATOM   1178 C  CA    . THR   A 1 142 ? 3.095   -16.604 13.231 1.00 19.11 ? 168 THR   A CA    1 
ATOM   1179 C  C     . THR   A 1 142 ? 2.687   -17.704 12.238 1.00 20.91 ? 168 THR   A C     1 
ATOM   1180 O  O     . THR   A 1 142 ? 1.989   -17.386 11.283 1.00 21.29 ? 168 THR   A O     1 
ATOM   1181 C  CB    . THR   A 1 142 ? 4.269   -15.797 12.654 1.00 19.72 ? 168 THR   A CB    1 
ATOM   1182 O  OG1   . THR   A 1 142 ? 3.798   -14.951 11.606 1.00 20.24 ? 168 THR   A OG1   1 
ATOM   1183 C  CG2   . THR   A 1 142 ? 5.416   -16.689 12.162 1.00 19.79 ? 168 THR   A CG2   1 
ATOM   1184 N  N     . GLU   A 1 143 ? 3.108   -18.963 12.435 1.00 21.68 ? 169 GLU   A N     1 
ATOM   1185 C  CA    . GLU   A 1 143 ? 2.836   -20.014 11.464 1.00 23.76 ? 169 GLU   A CA    1 
ATOM   1186 C  C     . GLU   A 1 143 ? 2.567   -21.366 12.132 1.00 25.68 ? 169 GLU   A C     1 
ATOM   1187 O  O     . GLU   A 1 143 ? 3.488   -21.986 12.670 1.00 25.78 ? 169 GLU   A O     1 
ATOM   1188 C  CB    . GLU   A 1 143 ? 4.018   -20.115 10.480 1.00 25.65 ? 169 GLU   A CB    1 
ATOM   1189 C  CG    . GLU   A 1 143 ? 3.850   -21.161 9.397  1.00 31.25 ? 169 GLU   A CG    1 
ATOM   1190 C  CD    . GLU   A 1 143 ? 2.564   -21.074 8.597  1.00 37.86 ? 169 GLU   A CD    1 
ATOM   1191 O  OE1   . GLU   A 1 143 ? 2.508   -20.237 7.668  1.00 38.26 ? 169 GLU   A OE1   1 
ATOM   1192 O  OE2   . GLU   A 1 143 ? 1.617   -21.844 8.891  1.00 39.62 ? 169 GLU   A OE2   1 
ATOM   1193 N  N     . CYS   A 1 144 ? 1.312   -21.825 12.095 1.00 27.11 ? 170 CYS   A N     1 
ATOM   1194 C  CA    . CYS   A 1 144 ? 0.950   -23.085 12.741 1.00 29.17 ? 170 CYS   A CA    1 
ATOM   1195 C  C     . CYS   A 1 144 ? 1.516   -24.324 12.023 1.00 30.83 ? 170 CYS   A C     1 
ATOM   1196 O  O     . CYS   A 1 144 ? 1.587   -25.375 12.653 1.00 32.11 ? 170 CYS   A O     1 
ATOM   1197 C  CB    . CYS   A 1 144 ? -0.553  -23.195 12.995 1.00 30.17 ? 170 CYS   A CB    1 
ATOM   1198 S  SG    . CYS   A 1 144 ? -1.580  -23.167 11.511 1.00 38.18 ? 170 CYS   A SG    1 
ATOM   1199 N  N     . GLU   A 1 145 ? 2.047   -24.192 10.793 1.00 31.01 ? 171 GLU   A N     1 
ATOM   1200 C  CA    . GLU   A 1 145 ? 2.666   -25.335 10.109 1.00 31.88 ? 171 GLU   A CA    1 
ATOM   1201 C  C     . GLU   A 1 145 ? 4.168   -25.480 10.398 1.00 31.38 ? 171 GLU   A C     1 
ATOM   1202 O  O     . GLU   A 1 145 ? 4.761   -26.480 9.993  1.00 32.04 ? 171 GLU   A O     1 
ATOM   1203 C  CB    . GLU   A 1 145 ? 2.393   -25.331 8.593  1.00 35.79 ? 171 GLU   A CB    1 
ATOM   1204 C  CG    . GLU   A 1 145 ? 0.918   -25.297 8.228  1.00 43.68 ? 171 GLU   A CG    1 
ATOM   1205 C  CD    . GLU   A 1 145 ? 0.140   -26.585 8.430  1.00 55.09 ? 171 GLU   A CD    1 
ATOM   1206 O  OE1   . GLU   A 1 145 ? 0.701   -27.675 8.172  1.00 58.43 ? 171 GLU   A OE1   1 
ATOM   1207 O  OE2   . GLU   A 1 145 ? -1.047  -26.502 8.822  1.00 57.96 ? 171 GLU   A OE2   1 
ATOM   1208 N  N     . ASN   A 1 146 ? 4.796   -24.502 11.086 1.00 30.18 ? 172 ASN   A N     1 
ATOM   1209 C  CA    . ASN   A 1 146 ? 6.212   -24.606 11.441 1.00 29.78 ? 172 ASN   A CA    1 
ATOM   1210 C  C     . ASN   A 1 146 ? 6.290   -25.410 12.766 1.00 28.39 ? 172 ASN   A C     1 
ATOM   1211 O  O     . ASN   A 1 146 ? 6.513   -24.822 13.828 1.00 27.04 ? 172 ASN   A O     1 
ATOM   1212 C  CB    . ASN   A 1 146 ? 6.838   -23.210 11.641 1.00 31.58 ? 172 ASN   A CB    1 
ATOM   1213 C  CG    . ASN   A 1 146 ? 7.125   -22.419 10.389 1.00 37.13 ? 172 ASN   A CG    1 
ATOM   1214 O  OD1   . ASN   A 1 146 ? 7.026   -22.913 9.252  1.00 38.52 ? 172 ASN   A OD1   1 
ATOM   1215 N  ND2   . ASN   A 1 146 ? 7.500   -21.156 10.581 1.00 38.31 ? 172 ASN   A ND2   1 
ATOM   1216 N  N     . ARG   A 1 147 ? 6.096   -26.752 12.692 1.00 27.85 ? 173 ARG   A N     1 
ATOM   1217 C  CA    . ARG   A 1 147 ? 6.047   -27.647 13.860 1.00 27.47 ? 173 ARG   A CA    1 
ATOM   1218 C  C     . ARG   A 1 147 ? 7.260   -27.562 14.787 1.00 26.51 ? 173 ARG   A C     1 
ATOM   1219 O  O     . ARG   A 1 147 ? 7.095   -27.602 16.004 1.00 25.94 ? 173 ARG   A O     1 
ATOM   1220 C  CB    . ARG   A 1 147 ? 5.798   -29.108 13.435 1.00 28.68 ? 173 ARG   A CB    1 
ATOM   1221 C  CG    . ARG   A 1 147 ? 5.610   -30.076 14.617 1.00 30.70 ? 173 ARG   A CG    1 
ATOM   1222 C  CD    . ARG   A 1 147 ? 5.367   -31.495 14.158 1.00 32.36 ? 173 ARG   A CD    1 
ATOM   1223 N  NE    . ARG   A 1 147 ? 6.541   -32.030 13.468 1.00 33.17 ? 173 ARG   A NE    1 
ATOM   1224 C  CZ    . ARG   A 1 147 ? 6.524   -33.087 12.665 1.00 33.53 ? 173 ARG   A CZ    1 
ATOM   1225 N  NH1   . ARG   A 1 147 ? 5.390   -33.740 12.436 1.00 32.73 ? 173 ARG   A NH1   1 
ATOM   1226 N  NH2   . ARG   A 1 147 ? 7.641   -33.501 12.084 1.00 32.07 ? 173 ARG   A NH2   1 
ATOM   1227 N  N     . GLU   A 1 148 ? 8.467   -27.436 14.229 1.00 26.16 ? 174 GLU   A N     1 
ATOM   1228 C  CA    . GLU   A 1 148 ? 9.679   -27.378 15.037 1.00 25.85 ? 174 GLU   A CA    1 
ATOM   1229 C  C     . GLU   A 1 148 ? 9.712   -26.078 15.860 1.00 24.50 ? 174 GLU   A C     1 
ATOM   1230 O  O     . GLU   A 1 148 ? 9.968   -26.139 17.057 1.00 24.63 ? 174 GLU   A O     1 
ATOM   1231 C  CB    . GLU   A 1 148 ? 10.945  -27.641 14.181 1.00 29.34 ? 174 GLU   A CB    1 
ATOM   1232 C  CG    . GLU   A 1 148 ? 11.850  -26.463 13.861 1.00 37.12 ? 174 GLU   A CG    1 
ATOM   1233 C  CD    . GLU   A 1 148 ? 12.851  -26.672 12.733 1.00 47.31 ? 174 GLU   A CD    1 
ATOM   1234 O  OE1   . GLU   A 1 148 ? 13.131  -27.843 12.384 1.00 50.22 ? 174 GLU   A OE1   1 
ATOM   1235 O  OE2   . GLU   A 1 148 ? 13.356  -25.659 12.196 1.00 49.51 ? 174 GLU   A OE2   1 
ATOM   1236 N  N     . ALA   A 1 149 ? 9.346   -24.936 15.260 1.00 22.91 ? 175 ALA   A N     1 
ATOM   1237 C  CA    . ALA   A 1 149 ? 9.309   -23.666 15.980 1.00 22.01 ? 175 ALA   A CA    1 
ATOM   1238 C  C     . ALA   A 1 149 ? 8.220   -23.669 17.061 1.00 20.76 ? 175 ALA   A C     1 
ATOM   1239 O  O     . ALA   A 1 149 ? 8.509   -23.354 18.208 1.00 20.43 ? 175 ALA   A O     1 
ATOM   1240 C  CB    . ALA   A 1 149 ? 9.100   -22.503 15.000 1.00 21.96 ? 175 ALA   A CB    1 
ATOM   1241 N  N     . VAL   A 1 150 ? 6.990   -24.074 16.714 1.00 20.35 ? 176 VAL   A N     1 
ATOM   1242 C  CA    . VAL   A 1 150 ? 5.861   -24.115 17.640 1.00 20.27 ? 176 VAL   A CA    1 
ATOM   1243 C  C     . VAL   A 1 150 ? 6.149   -24.988 18.882 1.00 19.12 ? 176 VAL   A C     1 
ATOM   1244 O  O     . VAL   A 1 150 ? 5.893   -24.551 20.008 1.00 18.59 ? 176 VAL   A O     1 
ATOM   1245 C  CB    . VAL   A 1 150 ? 4.581   -24.586 16.901 1.00 21.59 ? 176 VAL   A CB    1 
ATOM   1246 C  CG1   . VAL   A 1 150 ? 3.458   -24.889 17.880 1.00 22.71 ? 176 VAL   A CG1   1 
ATOM   1247 C  CG2   . VAL   A 1 150 ? 4.124   -23.560 15.864 1.00 21.87 ? 176 VAL   A CG2   1 
ATOM   1248 N  N     . THR   A 1 151 ? 6.662   -26.217 18.676 1.00 18.58 ? 177 THR   A N     1 
ATOM   1249 C  CA    . THR   A 1 151 ? 6.902   -27.122 19.799 1.00 19.38 ? 177 THR   A CA    1 
ATOM   1250 C  C     . THR   A 1 151 ? 8.082   -26.645 20.636 1.00 19.88 ? 177 THR   A C     1 
ATOM   1251 O  O     . THR   A 1 151 ? 8.031   -26.778 21.862 1.00 20.18 ? 177 THR   A O     1 
ATOM   1252 C  CB    . THR   A 1 151 ? 6.984   -28.606 19.344 1.00 21.16 ? 177 THR   A CB    1 
ATOM   1253 O  OG1   . THR   A 1 151 ? 8.048   -28.748 18.414 1.00 22.01 ? 177 THR   A OG1   1 
ATOM   1254 C  CG2   . THR   A 1 151 ? 5.691   -29.070 18.682 1.00 22.01 ? 177 THR   A CG2   1 
ATOM   1255 N  N     . HIS   A 1 152 ? 9.111   -26.018 20.013 1.00 20.26 ? 178 HIS   A N     1 
ATOM   1256 C  CA    . HIS   A 1 152 ? 10.228  -25.476 20.802 1.00 20.71 ? 178 HIS   A CA    1 
ATOM   1257 C  C     . HIS   A 1 152 ? 9.698   -24.347 21.705 1.00 18.95 ? 178 HIS   A C     1 
ATOM   1258 O  O     . HIS   A 1 152 ? 9.976   -24.313 22.910 1.00 19.14 ? 178 HIS   A O     1 
ATOM   1259 C  CB    . HIS   A 1 152 ? 11.365  -24.948 19.913 1.00 22.22 ? 178 HIS   A CB    1 
ATOM   1260 C  CG    . HIS   A 1 152 ? 12.451  -24.284 20.708 1.00 26.38 ? 178 HIS   A CG    1 
ATOM   1261 N  ND1   . HIS   A 1 152 ? 12.376  -22.946 21.068 1.00 28.85 ? 178 HIS   A ND1   1 
ATOM   1262 C  CD2   . HIS   A 1 152 ? 13.599  -24.802 21.205 1.00 28.14 ? 178 HIS   A CD2   1 
ATOM   1263 C  CE1   . HIS   A 1 152 ? 13.482  -22.698 21.753 1.00 29.54 ? 178 HIS   A CE1   1 
ATOM   1264 N  NE2   . HIS   A 1 152 ? 14.243  -23.785 21.871 1.00 29.20 ? 178 HIS   A NE2   1 
ATOM   1265 N  N     . ILE   A 1 153 ? 8.895   -23.458 21.126 1.00 17.33 ? 179 ILE   A N     1 
ATOM   1266 C  CA    . ILE   A 1 153 ? 8.291   -22.342 21.862 1.00 16.76 ? 179 ILE   A CA    1 
ATOM   1267 C  C     . ILE   A 1 153 ? 7.455   -22.865 23.029 1.00 16.14 ? 179 ILE   A C     1 
ATOM   1268 O  O     . ILE   A 1 153 ? 7.706   -22.498 24.176 1.00 15.72 ? 179 ILE   A O     1 
ATOM   1269 C  CB    . ILE   A 1 153 ? 7.505   -21.407 20.913 1.00 17.15 ? 179 ILE   A CB    1 
ATOM   1270 C  CG1   . ILE   A 1 153 ? 8.473   -20.642 19.981 1.00 17.26 ? 179 ILE   A CG1   1 
ATOM   1271 C  CG2   . ILE   A 1 153 ? 6.619   -20.421 21.686 1.00 18.14 ? 179 ILE   A CG2   1 
ATOM   1272 C  CD1   . ILE   A 1 153 ? 7.769   -20.003 18.805 1.00 17.43 ? 179 ILE   A CD1   1 
ATOM   1273 N  N     . GLY   A 1 154 ? 6.587   -23.830 22.740 1.00 15.95 ? 180 GLY   A N     1 
ATOM   1274 C  CA    . GLY   A 1 154 ? 5.729   -24.433 23.745 1.00 16.00 ? 180 GLY   A CA    1 
ATOM   1275 C  C     . GLY   A 1 154 ? 6.497   -25.056 24.892 1.00 17.03 ? 180 GLY   A C     1 
ATOM   1276 O  O     . GLY   A 1 154 ? 6.152   -24.826 26.047 1.00 17.45 ? 180 GLY   A O     1 
ATOM   1277 N  N     . ARG   A 1 155 ? 7.544   -25.835 24.585 1.00 17.51 ? 181 ARG   A N     1 
ATOM   1278 C  CA    . ARG   A 1 155 ? 8.358   -26.516 25.588 1.00 19.33 ? 181 ARG   A CA    1 
ATOM   1279 C  C     . ARG   A 1 155 ? 9.136   -25.559 26.505 1.00 19.45 ? 181 ARG   A C     1 
ATOM   1280 O  O     . ARG   A 1 155 ? 9.142   -25.753 27.727 1.00 19.72 ? 181 ARG   A O     1 
ATOM   1281 C  CB    . ARG   A 1 155 ? 9.291   -27.539 24.914 1.00 22.28 ? 181 ARG   A CB    1 
ATOM   1282 C  CG    . ARG   A 1 155 ? 10.115  -28.368 25.901 1.00 29.58 ? 181 ARG   A CG    1 
ATOM   1283 C  CD    . ARG   A 1 155 ? 10.839  -29.526 25.216 1.00 35.76 ? 181 ARG   A CD    1 
ATOM   1284 N  NE    . ARG   A 1 155 ? 9.917   -30.540 24.687 1.00 42.00 ? 181 ARG   A NE    1 
ATOM   1285 C  CZ    . ARG   A 1 155 ? 9.710   -30.770 23.393 1.00 45.65 ? 181 ARG   A CZ    1 
ATOM   1286 N  NH1   . ARG   A 1 155 ? 10.343  -30.052 22.473 1.00 44.92 ? 181 ARG   A NH1   1 
ATOM   1287 N  NH2   . ARG   A 1 155 ? 8.864   -31.715 23.009 1.00 47.25 ? 181 ARG   A NH2   1 
ATOM   1288 N  N     . VAL   A 1 156 ? 9.787   -24.537 25.926 1.00 19.11 ? 182 VAL   A N     1 
ATOM   1289 C  CA    . VAL   A 1 156 ? 10.536  -23.535 26.687 1.00 20.23 ? 182 VAL   A CA    1 
ATOM   1290 C  C     . VAL   A 1 156 ? 9.543   -22.725 27.581 1.00 20.45 ? 182 VAL   A C     1 
ATOM   1291 O  O     . VAL   A 1 156 ? 9.796   -22.501 28.771 1.00 19.95 ? 182 VAL   A O     1 
ATOM   1292 C  CB    . VAL   A 1 156 ? 11.311  -22.577 25.719 1.00 20.97 ? 182 VAL   A CB    1 
ATOM   1293 C  CG1   . VAL   A 1 156 ? 11.822  -21.342 26.449 1.00 21.92 ? 182 VAL   A CG1   1 
ATOM   1294 C  CG2   . VAL   A 1 156 ? 12.455  -23.296 25.008 1.00 21.26 ? 182 VAL   A CG2   1 
ATOM   1295 N  N     . TYR   A 1 157 ? 8.404   -22.340 27.002 1.00 19.75 ? 183 TYR   A N     1 
ATOM   1296 C  CA    . TYR   A 1 157 ? 7.386   -21.571 27.712 1.00 20.20 ? 183 TYR   A CA    1 
ATOM   1297 C  C     . TYR   A 1 157 ? 6.773   -22.356 28.882 1.00 20.65 ? 183 TYR   A C     1 
ATOM   1298 O  O     . TYR   A 1 157 ? 6.646   -21.808 29.992 1.00 20.44 ? 183 TYR   A O     1 
ATOM   1299 C  CB    . TYR   A 1 157 ? 6.290   -21.153 26.739 1.00 20.39 ? 183 TYR   A CB    1 
ATOM   1300 C  CG    . TYR   A 1 157 ? 5.239   -20.259 27.348 1.00 21.70 ? 183 TYR   A CG    1 
ATOM   1301 C  CD1   . TYR   A 1 157 ? 5.592   -19.186 28.155 1.00 22.90 ? 183 TYR   A CD1   1 
ATOM   1302 C  CD2   . TYR   A 1 157 ? 3.895   -20.465 27.092 1.00 22.41 ? 183 TYR   A CD2   1 
ATOM   1303 C  CE1   . TYR   A 1 157 ? 4.624   -18.341 28.694 1.00 24.12 ? 183 TYR   A CE1   1 
ATOM   1304 C  CE2   . TYR   A 1 157 ? 2.925   -19.615 27.603 1.00 23.36 ? 183 TYR   A CE2   1 
ATOM   1305 C  CZ    . TYR   A 1 157 ? 3.289   -18.575 28.429 1.00 24.87 ? 183 TYR   A CZ    1 
ATOM   1306 O  OH    . TYR   A 1 157 ? 2.318   -17.729 28.899 1.00 27.13 ? 183 TYR   A OH    1 
ATOM   1307 N  N     . LYS   A 1 158 ? 6.392   -23.623 28.645 1.00 20.46 ? 184 LYS   A N     1 
ATOM   1308 C  CA    . LYS   A 1 158 ? 5.814   -24.433 29.715 1.00 21.50 ? 184 LYS   A CA    1 
ATOM   1309 C  C     . LYS   A 1 158 ? 6.813   -24.622 30.895 1.00 22.15 ? 184 LYS   A C     1 
ATOM   1310 O  O     . LYS   A 1 158 ? 6.422   -24.493 32.062 1.00 22.67 ? 184 LYS   A O     1 
ATOM   1311 C  CB    . LYS   A 1 158 ? 5.317   -25.776 29.171 1.00 23.89 ? 184 LYS   A CB    1 
ATOM   1312 C  CG    . LYS   A 1 158 ? 4.829   -26.726 30.254 1.00 29.07 ? 184 LYS   A CG    1 
ATOM   1313 C  CD    . LYS   A 1 158 ? 4.051   -27.882 29.700 1.00 34.14 ? 184 LYS   A CD    1 
ATOM   1314 C  CE    . LYS   A 1 158 ? 3.586   -28.787 30.818 1.00 38.87 ? 184 LYS   A CE    1 
ATOM   1315 N  NZ    . LYS   A 1 158 ? 3.094   -30.090 30.306 1.00 41.83 ? 184 LYS   A NZ    1 
ATOM   1316 N  N     . GLU   A 1 159 ? 8.095   -24.880 30.580 1.00 21.64 ? 185 GLU   A N     1 
ATOM   1317 C  CA    . GLU   A 1 159 ? 9.151   -25.063 31.575 1.00 21.83 ? 185 GLU   A CA    1 
ATOM   1318 C  C     . GLU   A 1 159 ? 9.422   -23.749 32.339 1.00 20.78 ? 185 GLU   A C     1 
ATOM   1319 O  O     . GLU   A 1 159 ? 9.633   -23.764 33.561 1.00 20.41 ? 185 GLU   A O     1 
ATOM   1320 C  CB    . GLU   A 1 159 ? 10.442  -25.586 30.894 1.00 25.69 ? 185 GLU   A CB    1 
ATOM   1321 C  CG    . GLU   A 1 159 ? 11.635  -25.697 31.831 1.00 35.04 ? 185 GLU   A CG    1 
ATOM   1322 C  CD    . GLU   A 1 159 ? 13.015  -25.801 31.196 1.00 47.48 ? 185 GLU   A CD    1 
ATOM   1323 O  OE1   . GLU   A 1 159 ? 13.247  -25.164 30.142 1.00 49.82 ? 185 GLU   A OE1   1 
ATOM   1324 O  OE2   . GLU   A 1 159 ? 13.880  -26.492 31.781 1.00 51.51 ? 185 GLU   A OE2   1 
ATOM   1325 N  N     . ARG   A 1 160 ? 9.392   -22.620 31.628 1.00 20.08 ? 186 ARG   A N     1 
ATOM   1326 C  CA    . ARG   A 1 160 ? 9.620   -21.306 32.220 1.00 20.72 ? 186 ARG   A CA    1 
ATOM   1327 C  C     . ARG   A 1 160 ? 8.586   -20.983 33.306 1.00 21.67 ? 186 ARG   A C     1 
ATOM   1328 O  O     . ARG   A 1 160 ? 8.945   -20.487 34.375 1.00 20.95 ? 186 ARG   A O     1 
ATOM   1329 C  CB    . ARG   A 1 160 ? 9.627   -20.197 31.149 1.00 21.27 ? 186 ARG   A CB    1 
ATOM   1330 C  CG    . ARG   A 1 160 ? 9.850   -18.791 31.703 1.00 23.06 ? 186 ARG   A CG    1 
ATOM   1331 C  CD    . ARG   A 1 160 ? 11.187  -18.644 32.444 1.00 24.64 ? 186 ARG   A CD    1 
ATOM   1332 N  NE    . ARG   A 1 160 ? 12.326  -19.021 31.611 1.00 25.60 ? 186 ARG   A NE    1 
ATOM   1333 C  CZ    . ARG   A 1 160 ? 12.945  -18.208 30.761 1.00 25.00 ? 186 ARG   A CZ    1 
ATOM   1334 N  NH1   . ARG   A 1 160 ? 12.576  -16.938 30.657 1.00 26.19 ? 186 ARG   A NH1   1 
ATOM   1335 N  NH2   . ARG   A 1 160 ? 13.938  -18.657 30.012 1.00 22.30 ? 186 ARG   A NH2   1 
ATOM   1336 N  N     . LEU   A 1 161 ? 7.321   -21.262 33.027 1.00 22.69 ? 187 LEU   A N     1 
ATOM   1337 C  CA    . LEU   A 1 161 ? 6.252   -20.995 33.978 1.00 25.20 ? 187 LEU   A CA    1 
ATOM   1338 C  C     . LEU   A 1 161 ? 6.214   -21.985 35.163 1.00 27.54 ? 187 LEU   A C     1 
ATOM   1339 O  O     . LEU   A 1 161 ? 5.536   -21.719 36.143 1.00 28.15 ? 187 LEU   A O     1 
ATOM   1340 C  CB    . LEU   A 1 161 ? 4.895   -20.919 33.253 1.00 25.75 ? 187 LEU   A CB    1 
ATOM   1341 C  CG    . LEU   A 1 161 ? 4.383   -19.501 32.887 1.00 27.44 ? 187 LEU   A CG    1 
ATOM   1342 C  CD1   . LEU   A 1 161 ? 5.444   -18.642 32.198 1.00 28.30 ? 187 LEU   A CD1   1 
ATOM   1343 C  CD2   . LEU   A 1 161 ? 3.157   -19.585 32.033 1.00 28.28 ? 187 LEU   A CD2   1 
ATOM   1344 N  N     . GLY   A 1 162 ? 6.941   -23.093 35.066 1.00 28.84 ? 188 GLY   A N     1 
ATOM   1345 C  CA    . GLY   A 1 162 ? 7.022   -24.092 36.121 1.00 31.34 ? 188 GLY   A CA    1 
ATOM   1346 C  C     . GLY   A 1 162 ? 5.788   -24.960 36.232 1.00 33.73 ? 188 GLY   A C     1 
ATOM   1347 O  O     . GLY   A 1 162 ? 5.494   -25.463 37.317 1.00 34.10 ? 188 GLY   A O     1 
ATOM   1348 N  N     . LEU   A 1 163 ? 5.048   -25.121 35.117 1.00 34.84 ? 189 LEU   A N     1 
ATOM   1349 C  CA    . LEU   A 1 163 ? 3.822   -25.914 35.059 1.00 37.06 ? 189 LEU   A CA    1 
ATOM   1350 C  C     . LEU   A 1 163 ? 4.116   -27.392 35.281 1.00 39.53 ? 189 LEU   A C     1 
ATOM   1351 O  O     . LEU   A 1 163 ? 5.162   -27.880 34.845 1.00 39.59 ? 189 LEU   A O     1 
ATOM   1352 C  CB    . LEU   A 1 163 ? 3.134   -25.722 33.695 1.00 37.37 ? 189 LEU   A CB    1 
ATOM   1353 C  CG    . LEU   A 1 163 ? 2.583   -24.323 33.395 1.00 39.30 ? 189 LEU   A CG    1 
ATOM   1354 C  CD1   . LEU   A 1 163 ? 1.982   -24.265 31.996 1.00 40.11 ? 189 LEU   A CD1   1 
ATOM   1355 C  CD2   . LEU   A 1 163 ? 1.536   -23.923 34.391 1.00 40.09 ? 189 LEU   A CD2   1 
ATOM   1356 N  N     . PRO   A 1 164 ? 3.207   -28.135 35.944 1.00 41.49 ? 190 PRO   A N     1 
ATOM   1357 C  CA    . PRO   A 1 164 ? 3.470   -29.570 36.167 1.00 42.70 ? 190 PRO   A CA    1 
ATOM   1358 C  C     . PRO   A 1 164 ? 3.555   -30.323 34.845 1.00 44.04 ? 190 PRO   A C     1 
ATOM   1359 O  O     . PRO   A 1 164 ? 2.722   -30.128 33.967 1.00 44.54 ? 190 PRO   A O     1 
ATOM   1360 C  CB    . PRO   A 1 164 ? 2.293   -30.029 37.037 1.00 43.36 ? 190 PRO   A CB    1 
ATOM   1361 C  CG    . PRO   A 1 164 ? 1.222   -29.014 36.822 1.00 43.61 ? 190 PRO   A CG    1 
ATOM   1362 C  CD    . PRO   A 1 164 ? 1.915   -27.711 36.522 1.00 41.63 ? 190 PRO   A CD    1 
ATOM   1363 N  N     . PRO   A 1 165 ? 4.617   -31.117 34.650 1.00 44.67 ? 191 PRO   A N     1 
ATOM   1364 C  CA    . PRO   A 1 165 ? 4.801   -31.798 33.361 1.00 45.08 ? 191 PRO   A CA    1 
ATOM   1365 C  C     . PRO   A 1 165 ? 3.693   -32.753 32.929 1.00 45.33 ? 191 PRO   A C     1 
ATOM   1366 O  O     . PRO   A 1 165 ? 3.551   -32.987 31.733 1.00 45.95 ? 191 PRO   A O     1 
ATOM   1367 C  CB    . PRO   A 1 165 ? 6.132   -32.539 33.537 1.00 45.83 ? 191 PRO   A CB    1 
ATOM   1368 C  CG    . PRO   A 1 165 ? 6.829   -31.825 34.651 1.00 46.19 ? 191 PRO   A CG    1 
ATOM   1369 C  CD    . PRO   A 1 165 ? 5.731   -31.398 35.573 1.00 44.44 ? 191 PRO   A CD    1 
ATOM   1370 N  N     . LYS   A 1 166 ? 2.906   -33.285 33.871 1.00 44.49 ? 192 LYS   A N     1 
ATOM   1371 C  CA    . LYS   A 1 166 ? 1.843   -34.237 33.557 1.00 44.09 ? 192 LYS   A CA    1 
ATOM   1372 C  C     . LYS   A 1 166 ? 0.623   -33.636 32.855 1.00 43.49 ? 192 LYS   A C     1 
ATOM   1373 O  O     . LYS   A 1 166 ? 0.026   -34.315 32.025 1.00 44.12 ? 192 LYS   A O     1 
ATOM   1374 C  CB    . LYS   A 1 166 ? 1.412   -34.998 34.816 1.00 45.89 ? 192 LYS   A CB    1 
ATOM   1375 C  CG    . LYS   A 1 166 ? 1.338   -36.504 34.619 1.00 49.42 ? 192 LYS   A CG    1 
ATOM   1376 C  CD    . LYS   A 1 166 ? 0.853   -37.196 35.879 1.00 53.21 ? 192 LYS   A CD    1 
ATOM   1377 C  CE    . LYS   A 1 166 ? 0.304   -38.569 35.599 1.00 56.25 ? 192 LYS   A CE    1 
ATOM   1378 N  NZ    . LYS   A 1 166 ? 1.316   -39.453 34.970 1.00 57.67 ? 192 LYS   A NZ    1 
ATOM   1379 N  N     . ILE   A 1 167 ? 0.213   -32.413 33.208 1.00 42.32 ? 193 ILE   A N     1 
ATOM   1380 C  CA    . ILE   A 1 167 ? -0.942  -31.794 32.550 1.00 41.62 ? 193 ILE   A CA    1 
ATOM   1381 C  C     . ILE   A 1 167 ? -0.442  -31.098 31.284 1.00 39.51 ? 193 ILE   A C     1 
ATOM   1382 O  O     . ILE   A 1 167 ? 0.532   -30.354 31.347 1.00 39.66 ? 193 ILE   A O     1 
ATOM   1383 C  CB    . ILE   A 1 167 ? -1.704  -30.823 33.483 1.00 42.85 ? 193 ILE   A CB    1 
ATOM   1384 C  CG1   . ILE   A 1 167 ? -2.035  -31.487 34.827 1.00 44.09 ? 193 ILE   A CG1   1 
ATOM   1385 C  CG2   . ILE   A 1 167 ? -2.975  -30.277 32.793 1.00 43.47 ? 193 ILE   A CG2   1 
ATOM   1386 C  CD1   . ILE   A 1 167 ? -2.642  -30.524 35.846 1.00 45.67 ? 193 ILE   A CD1   1 
ATOM   1387 N  N     . VAL   A 1 168 ? -1.072  -31.374 30.141 1.00 37.01 ? 194 VAL   A N     1 
ATOM   1388 C  CA    . VAL   A 1 168 ? -0.647  -30.794 28.882 1.00 34.87 ? 194 VAL   A CA    1 
ATOM   1389 C  C     . VAL   A 1 168 ? -1.304  -29.442 28.606 1.00 31.88 ? 194 VAL   A C     1 
ATOM   1390 O  O     . VAL   A 1 168 ? -2.372  -29.131 29.135 1.00 31.38 ? 194 VAL   A O     1 
ATOM   1391 C  CB    . VAL   A 1 168 ? -0.857  -31.765 27.680 1.00 36.17 ? 194 VAL   A CB    1 
ATOM   1392 C  CG1   . VAL   A 1 168 ? -0.354  -33.169 27.999 1.00 36.90 ? 194 VAL   A CG1   1 
ATOM   1393 C  CG2   . VAL   A 1 168 ? -2.319  -31.809 27.246 1.00 36.73 ? 194 VAL   A CG2   1 
ATOM   1394 N  N     . ILE   A 1 169 ? -0.629  -28.630 27.782 1.00 28.86 ? 195 ILE   A N     1 
ATOM   1395 C  CA    . ILE   A 1 169 ? -1.154  -27.381 27.265 1.00 26.42 ? 195 ILE   A CA    1 
ATOM   1396 C  C     . ILE   A 1 169 ? -1.300  -27.615 25.739 1.00 24.61 ? 195 ILE   A C     1 
ATOM   1397 O  O     . ILE   A 1 169 ? -0.536  -28.386 25.154 1.00 24.31 ? 195 ILE   A O     1 
ATOM   1398 C  CB    . ILE   A 1 169 ? -0.229  -26.188 27.616 1.00 26.12 ? 195 ILE   A CB    1 
ATOM   1399 C  CG1   . ILE   A 1 169 ? 1.184   -26.361 27.026 1.00 26.44 ? 195 ILE   A CG1   1 
ATOM   1400 C  CG2   . ILE   A 1 169 ? -0.160  -26.004 29.123 1.00 26.40 ? 195 ILE   A CG2   1 
ATOM   1401 C  CD1   . ILE   A 1 169 ? 1.955   -25.074 26.960 1.00 27.85 ? 195 ILE   A CD1   1 
ATOM   1402 N  N     . GLY   A 1 170 ? -2.320  -27.026 25.132 1.00 23.10 ? 196 GLY   A N     1 
ATOM   1403 C  CA    . GLY   A 1 170 ? -2.554  -27.195 23.708 1.00 22.33 ? 196 GLY   A CA    1 
ATOM   1404 C  C     . GLY   A 1 170 ? -2.190  -25.990 22.861 1.00 20.89 ? 196 GLY   A C     1 
ATOM   1405 O  O     . GLY   A 1 170 ? -2.186  -24.860 23.340 1.00 20.95 ? 196 GLY   A O     1 
ATOM   1406 N  N     . TYR   A 1 171 ? -1.900  -26.230 21.593 1.00 19.70 ? 197 TYR   A N     1 
ATOM   1407 C  CA    . TYR   A 1 171 ? -1.628  -25.179 20.633 1.00 19.53 ? 197 TYR   A CA    1 
ATOM   1408 C  C     . TYR   A 1 171 ? -2.760  -25.228 19.661 1.00 19.62 ? 197 TYR   A C     1 
ATOM   1409 O  O     . TYR   A 1 171 ? -2.934  -26.258 19.011 1.00 20.12 ? 197 TYR   A O     1 
ATOM   1410 C  CB    . TYR   A 1 171 ? -0.305  -25.390 19.889 1.00 19.03 ? 197 TYR   A CB    1 
ATOM   1411 C  CG    . TYR   A 1 171 ? -0.014  -24.326 18.849 1.00 19.20 ? 197 TYR   A CG    1 
ATOM   1412 C  CD1   . TYR   A 1 171 ? 0.710   -23.186 19.174 1.00 19.57 ? 197 TYR   A CD1   1 
ATOM   1413 C  CD2   . TYR   A 1 171 ? -0.369  -24.508 17.517 1.00 20.04 ? 197 TYR   A CD2   1 
ATOM   1414 C  CE1   . TYR   A 1 171 ? 0.999   -22.212 18.218 1.00 19.93 ? 197 TYR   A CE1   1 
ATOM   1415 C  CE2   . TYR   A 1 171 ? -0.086  -23.541 16.553 1.00 20.49 ? 197 TYR   A CE2   1 
ATOM   1416 C  CZ    . TYR   A 1 171 ? 0.604   -22.398 16.906 1.00 21.05 ? 197 TYR   A CZ    1 
ATOM   1417 O  OH    . TYR   A 1 171 ? 0.932   -21.463 15.944 1.00 22.31 ? 197 TYR   A OH    1 
ATOM   1418 N  N     . GLN   A 1 172 ? -3.533  -24.129 19.564 1.00 18.93 ? 198 GLN   A N     1 
ATOM   1419 C  CA    . GLN   A 1 172 ? -4.653  -24.017 18.657 1.00 19.52 ? 198 GLN   A CA    1 
ATOM   1420 C  C     . GLN   A 1 172 ? -4.307  -23.068 17.520 1.00 18.99 ? 198 GLN   A C     1 
ATOM   1421 O  O     . GLN   A 1 172 ? -3.795  -21.988 17.762 1.00 18.02 ? 198 GLN   A O     1 
ATOM   1422 C  CB    . GLN   A 1 172 ? -5.896  -23.419 19.358 1.00 23.07 ? 198 GLN   A CB    1 
ATOM   1423 C  CG    . GLN   A 1 172 ? -6.101  -23.775 20.845 1.00 28.61 ? 198 GLN   A CG    1 
ATOM   1424 C  CD    . GLN   A 1 172 ? -7.239  -22.987 21.466 1.00 34.95 ? 198 GLN   A CD    1 
ATOM   1425 O  OE1   . GLN   A 1 172 ? -7.786  -22.029 20.886 1.00 37.14 ? 198 GLN   A OE1   1 
ATOM   1426 N  NE2   . GLN   A 1 172 ? -7.626  -23.377 22.666 1.00 36.94 ? 198 GLN   A NE2   1 
ATOM   1427 N  N     . SER   A 1 173 ? -4.636  -23.451 16.289 1.00 18.54 ? 199 SER   A N     1 
ATOM   1428 C  CA    . SER   A 1 173 ? -4.484  -22.579 15.123 1.00 19.21 ? 199 SER   A CA    1 
ATOM   1429 C  C     . SER   A 1 173 ? -5.554  -21.482 15.238 1.00 18.47 ? 199 SER   A C     1 
ATOM   1430 O  O     . SER   A 1 173 ? -6.663  -21.773 15.684 1.00 18.93 ? 199 SER   A O     1 
ATOM   1431 C  CB    . SER   A 1 173 ? -4.764  -23.397 13.859 1.00 21.57 ? 199 SER   A CB    1 
ATOM   1432 O  OG    . SER   A 1 173 ? -5.093  -22.597 12.740 1.00 26.52 ? 199 SER   A OG    1 
ATOM   1433 N  N     . HIS   A 1 174 ? -5.256  -20.252 14.798 1.00 17.94 ? 200 HIS   A N     1 
ATOM   1434 C  CA    . HIS   A 1 174 ? -6.252  -19.178 14.838 1.00 18.79 ? 200 HIS   A CA    1 
ATOM   1435 C  C     . HIS   A 1 174 ? -7.394  -19.464 13.860 1.00 19.97 ? 200 HIS   A C     1 
ATOM   1436 O  O     . HIS   A 1 174 ? -8.521  -19.084 14.141 1.00 20.59 ? 200 HIS   A O     1 
ATOM   1437 C  CB    . HIS   A 1 174 ? -5.622  -17.804 14.523 1.00 19.04 ? 200 HIS   A CB    1 
ATOM   1438 C  CG    . HIS   A 1 174 ? -4.649  -17.343 15.569 1.00 18.95 ? 200 HIS   A CG    1 
ATOM   1439 N  ND1   . HIS   A 1 174 ? -4.901  -17.526 16.905 1.00 19.26 ? 200 HIS   A ND1   1 
ATOM   1440 C  CD2   . HIS   A 1 174 ? -3.459  -16.715 15.426 1.00 19.32 ? 200 HIS   A CD2   1 
ATOM   1441 C  CE1   . HIS   A 1 174 ? -3.865  -17.002 17.539 1.00 20.24 ? 200 HIS   A CE1   1 
ATOM   1442 N  NE2   . HIS   A 1 174 ? -2.964  -16.518 16.686 1.00 20.56 ? 200 HIS   A NE2   1 
ATOM   1443 N  N     . ALA   A 1 175 ? -7.105  -20.128 12.724 1.00 20.72 ? 201 ALA   A N     1 
ATOM   1444 C  CA    . ALA   A 1 175 ? -8.112  -20.515 11.732 1.00 22.09 ? 201 ALA   A CA    1 
ATOM   1445 C  C     . ALA   A 1 175 ? -9.127  -21.492 12.350 1.00 22.56 ? 201 ALA   A C     1 
ATOM   1446 O  O     . ALA   A 1 175 ? -10.310 -21.436 12.001 1.00 23.19 ? 201 ALA   A O     1 
ATOM   1447 C  CB    . ALA   A 1 175 ? -7.440  -21.150 10.512 1.00 22.26 ? 201 ALA   A CB    1 
ATOM   1448 N  N     . ASP   A 1 176 ? -8.682  -22.355 13.286 1.00 22.09 ? 202 ASP   A N     1 
ATOM   1449 C  CA    . ASP   A 1 176 ? -9.576  -23.283 13.969 1.00 22.61 ? 202 ASP   A CA    1 
ATOM   1450 C  C     . ASP   A 1 176 ? -10.361 -22.570 15.047 1.00 22.76 ? 202 ASP   A C     1 
ATOM   1451 O  O     . ASP   A 1 176 ? -11.542 -22.852 15.210 1.00 22.88 ? 202 ASP   A O     1 
ATOM   1452 C  CB    . ASP   A 1 176 ? -8.816  -24.484 14.567 1.00 25.38 ? 202 ASP   A CB    1 
ATOM   1453 C  CG    . ASP   A 1 176 ? -8.306  -25.470 13.528 1.00 31.23 ? 202 ASP   A CG    1 
ATOM   1454 O  OD1   . ASP   A 1 176 ? -8.812  -25.443 12.378 1.00 33.37 ? 202 ASP   A OD1   1 
ATOM   1455 O  OD2   . ASP   A 1 176 ? -7.390  -26.246 13.851 1.00 32.01 ? 202 ASP   A OD2   1 
ATOM   1456 N  N     . THR   A 1 177 ? -9.724  -21.658 15.807 1.00 22.57 ? 203 THR   A N     1 
ATOM   1457 C  CA    . THR   A 1 177 ? -10.442 -20.916 16.853 1.00 23.16 ? 203 THR   A CA    1 
ATOM   1458 C  C     . THR   A 1 177 ? -11.542 -20.052 16.232 1.00 23.81 ? 203 THR   A C     1 
ATOM   1459 O  O     . THR   A 1 177 ? -12.673 -20.033 16.740 1.00 23.77 ? 203 THR   A O     1 
ATOM   1460 C  CB    . THR   A 1 177 ? -9.494  -20.014 17.651 1.00 23.69 ? 203 THR   A CB    1 
ATOM   1461 O  OG1   . THR   A 1 177 ? -8.376  -20.772 18.074 1.00 23.85 ? 203 THR   A OG1   1 
ATOM   1462 C  CG2   . THR   A 1 177 ? -10.182 -19.370 18.842 1.00 24.26 ? 203 THR   A CG2   1 
ATOM   1463 N  N     . ALA   A 1 178 ? -11.222 -19.378 15.107 1.00 24.53 ? 204 ALA   A N     1 
ATOM   1464 C  CA    . ALA   A 1 178 ? -12.175 -18.524 14.383 1.00 26.14 ? 204 ALA   A CA    1 
ATOM   1465 C  C     . ALA   A 1 178 ? -13.380 -19.269 13.791 1.00 27.57 ? 204 ALA   A C     1 
ATOM   1466 O  O     . ALA   A 1 178 ? -14.351 -18.621 13.417 1.00 27.45 ? 204 ALA   A O     1 
ATOM   1467 C  CB    . ALA   A 1 178 ? -11.462 -17.751 13.281 1.00 26.34 ? 204 ALA   A CB    1 
ATOM   1468 N  N     . THR   A 1 179 ? -13.308 -20.598 13.661 1.00 28.97 ? 205 THR   A N     1 
ATOM   1469 C  CA    . THR   A 1 179 ? -14.391 -21.406 13.076 1.00 31.16 ? 205 THR   A CA    1 
ATOM   1470 C  C     . THR   A 1 179 ? -14.928 -22.462 14.047 1.00 33.57 ? 205 THR   A C     1 
ATOM   1471 O  O     . THR   A 1 179 ? -15.550 -23.422 13.600 1.00 34.35 ? 205 THR   A O     1 
ATOM   1472 C  CB    . THR   A 1 179 ? -13.870 -22.143 11.828 1.00 32.16 ? 205 THR   A CB    1 
ATOM   1473 O  OG1   . THR   A 1 179 ? -12.690 -22.866 12.193 1.00 32.73 ? 205 THR   A OG1   1 
ATOM   1474 C  CG2   . THR   A 1 179 ? -13.568 -21.205 10.668 1.00 32.42 ? 205 THR   A CG2   1 
ATOM   1475 N  N     . LYS   A 1 180 ? -14.665 -22.320 15.352 1.00 34.69 ? 206 LYS   A N     1 
ATOM   1476 C  CA    . LYS   A 1 180 ? -15.073 -23.286 16.361 1.00 36.48 ? 206 LYS   A CA    1 
ATOM   1477 C  C     . LYS   A 1 180 ? -16.582 -23.487 16.424 1.00 38.78 ? 206 LYS   A C     1 
ATOM   1478 O  O     . LYS   A 1 180 ? -17.348 -22.527 16.431 1.00 38.83 ? 206 LYS   A O     1 
ATOM   1479 C  CB    . LYS   A 1 180 ? -14.515 -22.900 17.738 1.00 37.65 ? 206 LYS   A CB    1 
ATOM   1480 N  N     . SER   A 1 181 ? -17.003 -24.740 16.486 1.00 40.53 ? 207 SER   A N     1 
ATOM   1481 C  CA    . SER   A 1 181 ? -18.420 -25.083 16.569 1.00 42.83 ? 207 SER   A CA    1 
ATOM   1482 C  C     . SER   A 1 181 ? -18.833 -25.451 18.010 1.00 44.47 ? 207 SER   A C     1 
ATOM   1483 O  O     . SER   A 1 181 ? -17.987 -25.799 18.841 1.00 45.38 ? 207 SER   A O     1 
ATOM   1484 C  CB    . SER   A 1 181 ? -18.740 -26.230 15.616 1.00 44.51 ? 207 SER   A CB    1 
ATOM   1485 O  OG    . SER   A 1 181 ? -20.077 -26.668 15.788 1.00 47.57 ? 207 SER   A OG    1 
ATOM   1486 N  N     . LYS   A 1 186 ? -10.164 -27.438 19.410 1.00 34.40 ? 212 LYS   A N     1 
ATOM   1487 C  CA    . LYS   A 1 186 ? -9.326  -28.404 18.698 1.00 34.92 ? 212 LYS   A CA    1 
ATOM   1488 C  C     . LYS   A 1 186 ? -7.863  -27.953 18.667 1.00 34.98 ? 212 LYS   A C     1 
ATOM   1489 O  O     . LYS   A 1 186 ? -7.558  -26.855 18.201 1.00 35.62 ? 212 LYS   A O     1 
ATOM   1490 C  CB    . LYS   A 1 186 ? -9.848  -28.640 17.277 1.00 36.90 ? 212 LYS   A CB    1 
ATOM   1491 N  N     . ASN   A 1 187 ? -6.964  -28.802 19.143 1.00 34.06 ? 213 ASN   A N     1 
ATOM   1492 C  CA    . ASN   A 1 187 ? -5.535  -28.501 19.219 1.00 33.96 ? 213 ASN   A CA    1 
ATOM   1493 C  C     . ASN   A 1 187 ? -4.712  -29.204 18.133 1.00 32.63 ? 213 ASN   A C     1 
ATOM   1494 O  O     . ASN   A 1 187 ? -4.836  -30.418 17.981 1.00 33.48 ? 213 ASN   A O     1 
ATOM   1495 C  CB    . ASN   A 1 187 ? -4.996  -28.974 20.577 1.00 35.60 ? 213 ASN   A CB    1 
ATOM   1496 C  CG    . ASN   A 1 187 ? -5.477  -28.174 21.754 1.00 39.24 ? 213 ASN   A CG    1 
ATOM   1497 O  OD1   . ASN   A 1 187 ? -5.545  -26.946 21.723 1.00 40.38 ? 213 ASN   A OD1   1 
ATOM   1498 N  ND2   . ASN   A 1 187 ? -5.786  -28.858 22.832 1.00 40.58 ? 213 ASN   A ND2   1 
ATOM   1499 N  N     . ARG   A 1 188 ? -3.802  -28.469 17.464 1.00 30.09 ? 214 ARG   A N     1 
ATOM   1500 C  CA    . ARG   A 1 188 ? -2.878  -29.018 16.467 1.00 28.67 ? 214 ARG   A CA    1 
ATOM   1501 C  C     . ARG   A 1 188 ? -1.753  -29.769 17.175 1.00 27.17 ? 214 ARG   A C     1 
ATOM   1502 O  O     . ARG   A 1 188 ? -1.315  -30.807 16.696 1.00 26.78 ? 214 ARG   A O     1 
ATOM   1503 C  CB    . ARG   A 1 188 ? -2.252  -27.887 15.616 1.00 30.30 ? 214 ARG   A CB    1 
ATOM   1504 C  CG    . ARG   A 1 188 ? -3.253  -27.033 14.855 1.00 34.08 ? 214 ARG   A CG    1 
ATOM   1505 C  CD    . ARG   A 1 188 ? -3.970  -27.815 13.762 1.00 37.33 ? 214 ARG   A CD    1 
ATOM   1506 N  NE    . ARG   A 1 188 ? -4.785  -26.932 12.924 1.00 40.57 ? 214 ARG   A NE    1 
ATOM   1507 C  CZ    . ARG   A 1 188 ? -4.351  -26.334 11.817 1.00 43.38 ? 214 ARG   A CZ    1 
ATOM   1508 N  NH1   . ARG   A 1 188 ? -3.109  -26.534 11.389 1.00 43.26 ? 214 ARG   A NH1   1 
ATOM   1509 N  NH2   . ARG   A 1 188 ? -5.156  -25.535 11.127 1.00 43.15 ? 214 ARG   A NH2   1 
ATOM   1510 N  N     . PHE   A 1 189 ? -1.250  -29.223 18.299 1.00 26.37 ? 215 PHE   A N     1 
ATOM   1511 C  CA    . PHE   A 1 189 ? -0.166  -29.828 19.075 1.00 25.83 ? 215 PHE   A CA    1 
ATOM   1512 C  C     . PHE   A 1 189 ? -0.441  -29.737 20.589 1.00 25.16 ? 215 PHE   A C     1 
ATOM   1513 O  O     . PHE   A 1 189 ? -1.276  -28.943 21.027 1.00 24.25 ? 215 PHE   A O     1 
ATOM   1514 C  CB    . PHE   A 1 189 ? 1.186   -29.119 18.757 1.00 25.89 ? 215 PHE   A CB    1 
ATOM   1515 C  CG    . PHE   A 1 189 ? 1.492   -28.949 17.284 1.00 27.10 ? 215 PHE   A CG    1 
ATOM   1516 C  CD1   . PHE   A 1 189 ? 1.796   -30.040 16.490 1.00 28.21 ? 215 PHE   A CD1   1 
ATOM   1517 C  CD2   . PHE   A 1 189 ? 1.484   -27.694 16.697 1.00 28.26 ? 215 PHE   A CD2   1 
ATOM   1518 C  CE1   . PHE   A 1 189 ? 2.012   -29.886 15.119 1.00 29.11 ? 215 PHE   A CE1   1 
ATOM   1519 C  CE2   . PHE   A 1 189 ? 1.751   -27.541 15.340 1.00 29.08 ? 215 PHE   A CE2   1 
ATOM   1520 C  CZ    . PHE   A 1 189 ? 1.999   -28.638 14.558 1.00 28.83 ? 215 PHE   A CZ    1 
ATOM   1521 N  N     . VAL   A 1 190 ? 0.243   -30.573 21.376 1.00 25.33 ? 216 VAL   A N     1 
ATOM   1522 C  CA    . VAL   A 1 190 ? 0.222   -30.571 22.844 1.00 26.80 ? 216 VAL   A CA    1 
ATOM   1523 C  C     . VAL   A 1 190 ? 1.682   -30.632 23.360 1.00 28.34 ? 216 VAL   A C     1 
ATOM   1524 O  O     . VAL   A 1 190 ? 2.562   -31.122 22.647 1.00 28.34 ? 216 VAL   A O     1 
ATOM   1525 C  CB    . VAL   A 1 190 ? -0.628  -31.721 23.474 1.00 27.50 ? 216 VAL   A CB    1 
ATOM   1526 C  CG1   . VAL   A 1 190 ? -2.078  -31.696 22.993 1.00 27.55 ? 216 VAL   A CG1   1 
ATOM   1527 C  CG2   . VAL   A 1 190 ? 0.005   -33.090 23.224 1.00 28.06 ? 216 VAL   A CG2   1 
ATOM   1528 N  N     . VAL   A 1 191 ? 1.942   -30.152 24.589 1.00 29.42 ? 217 VAL   A N     1 
ATOM   1529 C  CA    . VAL   A 1 191 ? 3.278   -30.242 25.193 1.00 30.90 ? 217 VAL   A CA    1 
ATOM   1530 C  C     . VAL   A 1 191 ? 3.162   -30.377 26.732 1.00 32.02 ? 217 VAL   A C     1 
ATOM   1531 O  O     . VAL   A 1 191 ? 4.036   -31.011 27.361 1.00 32.70 ? 217 VAL   A O     1 
ATOM   1532 C  CB    . VAL   A 1 191 ? 4.260   -29.114 24.738 1.00 32.24 ? 217 VAL   A CB    1 
ATOM   1533 C  CG1   . VAL   A 1 191 ? 4.043   -27.826 25.504 1.00 32.78 ? 217 VAL   A CG1   1 
ATOM   1534 C  CG2   . VAL   A 1 191 ? 5.711   -29.560 24.859 1.00 33.15 ? 217 VAL   A CG2   1 
ATOM   1535 O  OXT   . VAL   A 1 191 ? 2.177   -29.883 27.315 1.00 31.19 ? 217 VAL   A OXT   1 
ATOM   1536 N  N     . ALA   B 1 3   ? 22.846  -37.648 32.614 1.00 48.72 ? 29  ALA   B N     1 
ATOM   1537 C  CA    . ALA   B 1 3   ? 22.333  -39.017 32.604 1.00 49.01 ? 29  ALA   B CA    1 
ATOM   1538 C  C     . ALA   B 1 3   ? 21.074  -39.150 31.746 1.00 48.91 ? 29  ALA   B C     1 
ATOM   1539 O  O     . ALA   B 1 3   ? 20.838  -40.205 31.158 1.00 49.43 ? 29  ALA   B O     1 
ATOM   1540 C  CB    . ALA   B 1 3   ? 22.056  -39.480 34.023 1.00 49.37 ? 29  ALA   B CB    1 
ATOM   1541 N  N     . ASN   B 1 4   ? 20.261  -38.090 31.670 1.00 48.17 ? 30  ASN   B N     1 
ATOM   1542 C  CA    . ASN   B 1 4   ? 19.039  -38.099 30.859 1.00 47.75 ? 30  ASN   B CA    1 
ATOM   1543 C  C     . ASN   B 1 4   ? 19.269  -37.212 29.636 1.00 45.54 ? 30  ASN   B C     1 
ATOM   1544 O  O     . ASN   B 1 4   ? 19.746  -36.085 29.792 1.00 45.43 ? 30  ASN   B O     1 
ATOM   1545 C  CB    . ASN   B 1 4   ? 17.859  -37.517 31.669 1.00 50.06 ? 30  ASN   B CB    1 
ATOM   1546 C  CG    . ASN   B 1 4   ? 16.883  -38.522 32.245 1.00 54.68 ? 30  ASN   B CG    1 
ATOM   1547 O  OD1   . ASN   B 1 4   ? 16.958  -39.731 31.996 1.00 56.56 ? 30  ASN   B OD1   1 
ATOM   1548 N  ND2   . ASN   B 1 4   ? 15.925  -38.029 33.025 1.00 55.46 ? 30  ASN   B ND2   1 
ATOM   1549 N  N     . PRO   B 1 5   ? 18.892  -37.655 28.420 1.00 43.63 ? 31  PRO   B N     1 
ATOM   1550 C  CA    . PRO   B 1 5   ? 19.069  -36.785 27.241 1.00 42.41 ? 31  PRO   B CA    1 
ATOM   1551 C  C     . PRO   B 1 5   ? 18.368  -35.434 27.409 1.00 41.12 ? 31  PRO   B C     1 
ATOM   1552 O  O     . PRO   B 1 5   ? 17.260  -35.375 27.931 1.00 41.35 ? 31  PRO   B O     1 
ATOM   1553 C  CB    . PRO   B 1 5   ? 18.458  -37.596 26.092 1.00 43.22 ? 31  PRO   B CB    1 
ATOM   1554 C  CG    . PRO   B 1 5   ? 18.457  -39.011 26.564 1.00 44.26 ? 31  PRO   B CG    1 
ATOM   1555 C  CD    . PRO   B 1 5   ? 18.325  -38.967 28.060 1.00 42.97 ? 31  PRO   B CD    1 
ATOM   1556 N  N     . GLU   B 1 6   ? 19.046  -34.351 27.048 1.00 39.41 ? 32  GLU   B N     1 
ATOM   1557 C  CA    . GLU   B 1 6   ? 18.495  -33.013 27.180 1.00 38.33 ? 32  GLU   B CA    1 
ATOM   1558 C  C     . GLU   B 1 6   ? 17.880  -32.557 25.874 1.00 36.51 ? 32  GLU   B C     1 
ATOM   1559 O  O     . GLU   B 1 6   ? 18.434  -32.831 24.812 1.00 36.16 ? 32  GLU   B O     1 
ATOM   1560 C  CB    . GLU   B 1 6   ? 19.601  -32.022 27.559 1.00 41.32 ? 32  GLU   B CB    1 
ATOM   1561 C  CG    . GLU   B 1 6   ? 20.031  -32.082 29.010 1.00 47.93 ? 32  GLU   B CG    1 
ATOM   1562 C  CD    . GLU   B 1 6   ? 20.997  -30.972 29.368 1.00 56.16 ? 32  GLU   B CD    1 
ATOM   1563 O  OE1   . GLU   B 1 6   ? 20.689  -29.795 29.069 1.00 57.77 ? 32  GLU   B OE1   1 
ATOM   1564 O  OE2   . GLU   B 1 6   ? 22.068  -31.279 29.938 1.00 59.90 ? 32  GLU   B OE2   1 
ATOM   1565 N  N     . HIS   B 1 7   ? 16.785  -31.799 25.946 1.00 35.35 ? 33  HIS   B N     1 
ATOM   1566 C  CA    . HIS   B 1 7   ? 16.162  -31.269 24.750 1.00 35.13 ? 33  HIS   B CA    1 
ATOM   1567 C  C     . HIS   B 1 7   ? 16.951  -30.059 24.261 1.00 35.94 ? 33  HIS   B C     1 
ATOM   1568 O  O     . HIS   B 1 7   ? 17.250  -29.983 23.074 1.00 36.07 ? 33  HIS   B O     1 
ATOM   1569 C  CB    . HIS   B 1 7   ? 14.692  -30.888 25.000 1.00 35.06 ? 33  HIS   B CB    1 
ATOM   1570 C  CG    . HIS   B 1 7   ? 13.735  -32.016 24.797 1.00 35.88 ? 33  HIS   B CG    1 
ATOM   1571 N  ND1   . HIS   B 1 7   ? 13.267  -32.760 25.858 1.00 37.37 ? 33  HIS   B ND1   1 
ATOM   1572 C  CD2   . HIS   B 1 7   ? 13.212  -32.511 23.653 1.00 36.56 ? 33  HIS   B CD2   1 
ATOM   1573 C  CE1   . HIS   B 1 7   ? 12.469  -33.678 25.334 1.00 37.50 ? 33  HIS   B CE1   1 
ATOM   1574 N  NE2   . HIS   B 1 7   ? 12.408  -33.571 24.011 1.00 37.58 ? 33  HIS   B NE2   1 
ATOM   1575 N  N     . TYR   B 1 8   ? 17.267  -29.104 25.160 1.00 35.90 ? 34  TYR   B N     1 
ATOM   1576 C  CA    . TYR   B 1 8   ? 17.960  -27.852 24.813 1.00 36.57 ? 34  TYR   B CA    1 
ATOM   1577 C  C     . TYR   B 1 8   ? 19.037  -27.513 25.832 1.00 35.59 ? 34  TYR   B C     1 
ATOM   1578 O  O     . TYR   B 1 8   ? 18.952  -27.922 26.982 1.00 35.73 ? 34  TYR   B O     1 
ATOM   1579 C  CB    . TYR   B 1 8   ? 16.967  -26.658 24.758 1.00 37.70 ? 34  TYR   B CB    1 
ATOM   1580 C  CG    . TYR   B 1 8   ? 15.636  -26.990 24.125 1.00 39.66 ? 34  TYR   B CG    1 
ATOM   1581 C  CD1   . TYR   B 1 8   ? 15.556  -27.390 22.800 1.00 40.79 ? 34  TYR   B CD1   1 
ATOM   1582 C  CD2   . TYR   B 1 8   ? 14.461  -26.948 24.864 1.00 40.76 ? 34  TYR   B CD2   1 
ATOM   1583 C  CE1   . TYR   B 1 8   ? 14.357  -27.807 22.244 1.00 41.95 ? 34  TYR   B CE1   1 
ATOM   1584 C  CE2   . TYR   B 1 8   ? 13.240  -27.283 24.290 1.00 41.82 ? 34  TYR   B CE2   1 
ATOM   1585 C  CZ    . TYR   B 1 8   ? 13.192  -27.707 22.975 1.00 42.82 ? 34  TYR   B CZ    1 
ATOM   1586 O  OH    . TYR   B 1 8   ? 12.011  -28.086 22.385 1.00 44.76 ? 34  TYR   B OH    1 
ATOM   1587 N  N     . ILE   B 1 9   ? 20.032  -26.732 25.416 1.00 34.59 ? 35  ILE   B N     1 
ATOM   1588 C  CA    . ILE   B 1 9   ? 21.116  -26.264 26.274 1.00 33.93 ? 35  ILE   B CA    1 
ATOM   1589 C  C     . ILE   B 1 9   ? 20.574  -25.134 27.180 1.00 32.05 ? 35  ILE   B C     1 
ATOM   1590 O  O     . ILE   B 1 9   ? 19.792  -24.292 26.727 1.00 32.35 ? 35  ILE   B O     1 
ATOM   1591 C  CB    . ILE   B 1 9   ? 22.284  -25.757 25.368 1.00 35.15 ? 35  ILE   B CB    1 
ATOM   1592 C  CG1   . ILE   B 1 9   ? 22.810  -26.880 24.452 1.00 36.95 ? 35  ILE   B CG1   1 
ATOM   1593 C  CG2   . ILE   B 1 9   ? 23.423  -25.161 26.180 1.00 35.89 ? 35  ILE   B CG2   1 
ATOM   1594 C  CD1   . ILE   B 1 9   ? 23.322  -28.120 25.214 1.00 38.64 ? 35  ILE   B CD1   1 
ATOM   1595 N  N     . LYS   B 1 10  ? 20.968  -25.129 28.450 1.00 29.94 ? 36  LYS   B N     1 
ATOM   1596 C  CA    . LYS   B 1 10  ? 20.551  -24.074 29.368 1.00 28.43 ? 36  LYS   B CA    1 
ATOM   1597 C  C     . LYS   B 1 10  ? 21.380  -22.791 29.115 1.00 27.12 ? 36  LYS   B C     1 
ATOM   1598 O  O     . LYS   B 1 10  ? 22.484  -22.865 28.585 1.00 27.78 ? 36  LYS   B O     1 
ATOM   1599 C  CB    . LYS   B 1 10  ? 20.642  -24.561 30.816 1.00 29.31 ? 36  LYS   B CB    1 
ATOM   1600 C  CG    . LYS   B 1 10  ? 19.544  -25.558 31.171 1.00 31.50 ? 36  LYS   B CG    1 
ATOM   1601 C  CD    . LYS   B 1 10  ? 19.683  -26.048 32.602 1.00 34.52 ? 36  LYS   B CD    1 
ATOM   1602 C  CE    . LYS   B 1 10  ? 18.621  -27.065 32.949 1.00 37.13 ? 36  LYS   B CE    1 
ATOM   1603 N  NZ    . LYS   B 1 10  ? 18.880  -27.699 34.271 1.00 38.61 ? 36  LYS   B NZ    1 
ATOM   1604 N  N     . HIS   B 1 11  ? 20.807  -21.628 29.411 1.00 24.88 ? 37  HIS   B N     1 
ATOM   1605 C  CA    . HIS   B 1 11  ? 21.407  -20.321 29.191 1.00 23.65 ? 37  HIS   B CA    1 
ATOM   1606 C  C     . HIS   B 1 11  ? 22.169  -19.878 30.428 1.00 22.78 ? 37  HIS   B C     1 
ATOM   1607 O  O     . HIS   B 1 11  ? 21.562  -19.668 31.456 1.00 22.48 ? 37  HIS   B O     1 
ATOM   1608 C  CB    . HIS   B 1 11  ? 20.299  -19.315 28.855 1.00 23.50 ? 37  HIS   B CB    1 
ATOM   1609 C  CG    . HIS   B 1 11  ? 19.557  -19.707 27.612 1.00 26.05 ? 37  HIS   B CG    1 
ATOM   1610 N  ND1   . HIS   B 1 11  ? 18.534  -20.639 27.644 1.00 27.85 ? 37  HIS   B ND1   1 
ATOM   1611 C  CD2   . HIS   B 1 11  ? 19.771  -19.336 26.330 1.00 27.11 ? 37  HIS   B CD2   1 
ATOM   1612 C  CE1   . HIS   B 1 11  ? 18.148  -20.788 26.385 1.00 28.56 ? 37  HIS   B CE1   1 
ATOM   1613 N  NE2   . HIS   B 1 11  ? 18.863  -20.020 25.561 1.00 28.26 ? 37  HIS   B NE2   1 
ATOM   1614 N  N     . PRO   B 1 12  ? 23.493  -19.719 30.336 1.00 22.41 ? 38  PRO   B N     1 
ATOM   1615 C  CA    . PRO   B 1 12  ? 24.270  -19.343 31.518 1.00 21.40 ? 38  PRO   B CA    1 
ATOM   1616 C  C     . PRO   B 1 12  ? 24.085  -17.912 31.999 1.00 19.35 ? 38  PRO   B C     1 
ATOM   1617 O  O     . PRO   B 1 12  ? 23.903  -16.993 31.215 1.00 18.88 ? 38  PRO   B O     1 
ATOM   1618 C  CB    . PRO   B 1 12  ? 25.737  -19.555 31.076 1.00 22.71 ? 38  PRO   B CB    1 
ATOM   1619 C  CG    . PRO   B 1 12  ? 25.672  -20.332 29.794 1.00 24.33 ? 38  PRO   B CG    1 
ATOM   1620 C  CD    . PRO   B 1 12  ? 24.362  -19.959 29.165 1.00 22.91 ? 38  PRO   B CD    1 
ATOM   1621 N  N     . LEU   B 1 13  ? 24.196  -17.737 33.304 1.00 17.47 ? 39  LEU   B N     1 
ATOM   1622 C  CA    . LEU   B 1 13  ? 24.181  -16.433 33.960 1.00 16.35 ? 39  LEU   B CA    1 
ATOM   1623 C  C     . LEU   B 1 13  ? 25.646  -15.977 34.027 1.00 17.31 ? 39  LEU   B C     1 
ATOM   1624 O  O     . LEU   B 1 13  ? 26.559  -16.806 33.925 1.00 16.66 ? 39  LEU   B O     1 
ATOM   1625 C  CB    . LEU   B 1 13  ? 23.642  -16.565 35.406 1.00 14.98 ? 39  LEU   B CB    1 
ATOM   1626 C  CG    . LEU   B 1 13  ? 22.148  -16.945 35.532 1.00 15.70 ? 39  LEU   B CG    1 
ATOM   1627 C  CD1   . LEU   B 1 13  ? 21.737  -17.139 37.015 1.00 15.90 ? 39  LEU   B CD1   1 
ATOM   1628 C  CD2   . LEU   B 1 13  ? 21.246  -15.933 34.825 1.00 15.31 ? 39  LEU   B CD2   1 
ATOM   1629 N  N     . GLN   B 1 14  ? 25.877  -14.676 34.218 1.00 17.94 ? 40  GLN   B N     1 
ATOM   1630 C  CA    . GLN   B 1 14  ? 27.247  -14.166 34.352 1.00 19.42 ? 40  GLN   B CA    1 
ATOM   1631 C  C     . GLN   B 1 14  ? 27.875  -14.722 35.646 1.00 19.56 ? 40  GLN   B C     1 
ATOM   1632 O  O     . GLN   B 1 14  ? 29.064  -15.032 35.656 1.00 20.51 ? 40  GLN   B O     1 
ATOM   1633 C  CB    . GLN   B 1 14  ? 27.214  -12.632 34.358 1.00 23.32 ? 40  GLN   B CB    1 
ATOM   1634 C  CG    . GLN   B 1 14  ? 28.534  -11.927 34.704 1.00 30.44 ? 40  GLN   B CG    1 
ATOM   1635 C  CD    . GLN   B 1 14  ? 29.647  -12.126 33.696 1.00 37.79 ? 40  GLN   B CD    1 
ATOM   1636 O  OE1   . GLN   B 1 14  ? 30.832  -12.152 34.059 1.00 39.51 ? 40  GLN   B OE1   1 
ATOM   1637 N  NE2   . GLN   B 1 14  ? 29.308  -12.270 32.412 1.00 39.10 ? 40  GLN   B NE2   1 
ATOM   1638 N  N     . ASN   B 1 15  ? 27.070  -14.932 36.709 1.00 18.02 ? 41  ASN   B N     1 
ATOM   1639 C  CA    . ASN   B 1 15  ? 27.611  -15.450 37.961 1.00 18.35 ? 41  ASN   B CA    1 
ATOM   1640 C  C     . ASN   B 1 15  ? 26.861  -16.681 38.475 1.00 18.26 ? 41  ASN   B C     1 
ATOM   1641 O  O     . ASN   B 1 15  ? 25.730  -16.933 38.071 1.00 18.37 ? 41  ASN   B O     1 
ATOM   1642 C  CB    . ASN   B 1 15  ? 27.586  -14.347 39.031 1.00 19.03 ? 41  ASN   B CB    1 
ATOM   1643 C  CG    . ASN   B 1 15  ? 28.659  -13.307 38.822 1.00 21.65 ? 41  ASN   B CG    1 
ATOM   1644 O  OD1   . ASN   B 1 15  ? 29.838  -13.558 39.058 1.00 24.14 ? 41  ASN   B OD1   1 
ATOM   1645 N  ND2   . ASN   B 1 15  ? 28.282  -12.135 38.377 1.00 19.89 ? 41  ASN   B ND2   1 
ATOM   1646 N  N     . ARG   B 1 16  ? 27.488  -17.423 39.388 1.00 17.07 ? 42  ARG   B N     1 
ATOM   1647 C  CA    . ARG   B 1 16  ? 26.838  -18.526 40.068 1.00 17.19 ? 42  ARG   B CA    1 
ATOM   1648 C  C     . ARG   B 1 16  ? 26.299  -17.902 41.366 1.00 15.91 ? 42  ARG   B C     1 
ATOM   1649 O  O     . ARG   B 1 16  ? 26.957  -17.048 41.981 1.00 15.28 ? 42  ARG   B O     1 
ATOM   1650 C  CB    . ARG   B 1 16  ? 27.825  -19.693 40.352 1.00 19.32 ? 42  ARG   B CB    1 
ATOM   1651 C  CG    . ARG   B 1 16  ? 27.160  -20.936 40.966 1.00 24.82 ? 42  ARG   B CG    1 
ATOM   1652 C  CD    . ARG   B 1 16  ? 28.078  -22.160 40.953 1.00 32.37 ? 42  ARG   B CD    1 
ATOM   1653 N  NE    . ARG   B 1 16  ? 28.433  -22.541 39.585 1.00 40.12 ? 42  ARG   B NE    1 
ATOM   1654 C  CZ    . ARG   B 1 16  ? 29.537  -23.204 39.245 1.00 46.02 ? 42  ARG   B CZ    1 
ATOM   1655 N  NH1   . ARG   B 1 16  ? 30.408  -23.580 40.174 1.00 46.49 ? 42  ARG   B NH1   1 
ATOM   1656 N  NH2   . ARG   B 1 16  ? 29.777  -23.497 37.973 1.00 47.39 ? 42  ARG   B NH2   1 
ATOM   1657 N  N     . TRP   B 1 17  ? 25.081  -18.273 41.738 1.00 14.90 ? 43  TRP   B N     1 
ATOM   1658 C  CA    . TRP   B 1 17  ? 24.413  -17.692 42.882 1.00 15.29 ? 43  TRP   B CA    1 
ATOM   1659 C  C     . TRP   B 1 17  ? 24.000  -18.771 43.890 1.00 16.50 ? 43  TRP   B C     1 
ATOM   1660 O  O     . TRP   B 1 17  ? 23.753  -19.899 43.503 1.00 15.85 ? 43  TRP   B O     1 
ATOM   1661 C  CB    . TRP   B 1 17  ? 23.146  -16.952 42.397 1.00 14.58 ? 43  TRP   B CB    1 
ATOM   1662 C  CG    . TRP   B 1 17  ? 23.457  -15.781 41.520 1.00 15.26 ? 43  TRP   B CG    1 
ATOM   1663 C  CD1   . TRP   B 1 17  ? 23.588  -15.781 40.162 1.00 16.49 ? 43  TRP   B CD1   1 
ATOM   1664 C  CD2   . TRP   B 1 17  ? 23.777  -14.455 41.956 1.00 15.15 ? 43  TRP   B CD2   1 
ATOM   1665 N  NE1   . TRP   B 1 17  ? 23.982  -14.535 39.725 1.00 16.51 ? 43  TRP   B NE1   1 
ATOM   1666 C  CE2   . TRP   B 1 17  ? 24.042  -13.686 40.804 1.00 15.74 ? 43  TRP   B CE2   1 
ATOM   1667 C  CE3   . TRP   B 1 17  ? 23.784  -13.820 43.208 1.00 15.61 ? 43  TRP   B CE3   1 
ATOM   1668 C  CZ2   . TRP   B 1 17  ? 24.358  -12.329 40.868 1.00 15.54 ? 43  TRP   B CZ2   1 
ATOM   1669 C  CZ3   . TRP   B 1 17  ? 24.090  -12.472 43.267 1.00 16.51 ? 43  TRP   B CZ3   1 
ATOM   1670 C  CH2   . TRP   B 1 17  ? 24.386  -11.746 42.107 1.00 16.29 ? 43  TRP   B CH2   1 
ATOM   1671 N  N     . ALA   B 1 18  ? 23.860  -18.399 45.165 1.00 16.91 ? 44  ALA   B N     1 
ATOM   1672 C  CA    . ALA   B 1 18  ? 23.401  -19.343 46.173 1.00 17.36 ? 44  ALA   B CA    1 
ATOM   1673 C  C     . ALA   B 1 18  ? 22.243  -18.742 46.933 1.00 16.59 ? 44  ALA   B C     1 
ATOM   1674 O  O     . ALA   B 1 18  ? 22.330  -17.600 47.350 1.00 16.88 ? 44  ALA   B O     1 
ATOM   1675 C  CB    . ALA   B 1 18  ? 24.544  -19.694 47.126 1.00 17.76 ? 44  ALA   B CB    1 
ATOM   1676 N  N     . LEU   B 1 19  ? 21.172  -19.511 47.141 1.00 16.15 ? 45  LEU   B N     1 
ATOM   1677 C  CA    . LEU   B 1 19  ? 20.041  -19.079 47.937 1.00 16.94 ? 45  LEU   B CA    1 
ATOM   1678 C  C     . LEU   B 1 19  ? 20.274  -19.550 49.382 1.00 17.71 ? 45  LEU   B C     1 
ATOM   1679 O  O     . LEU   B 1 19  ? 20.545  -20.732 49.603 1.00 17.77 ? 45  LEU   B O     1 
ATOM   1680 C  CB    . LEU   B 1 19  ? 18.741  -19.698 47.407 1.00 17.68 ? 45  LEU   B CB    1 
ATOM   1681 C  CG    . LEU   B 1 19  ? 17.485  -19.486 48.268 1.00 19.91 ? 45  LEU   B CG    1 
ATOM   1682 C  CD1   . LEU   B 1 19  ? 16.982  -18.061 48.169 1.00 19.90 ? 45  LEU   B CD1   1 
ATOM   1683 C  CD2   . LEU   B 1 19  ? 16.365  -20.455 47.868 1.00 21.26 ? 45  LEU   B CD2   1 
ATOM   1684 N  N     . TRP   B 1 20  ? 20.149  -18.629 50.351 1.00 18.08 ? 46  TRP   B N     1 
ATOM   1685 C  CA    . TRP   B 1 20  ? 20.282  -18.887 51.779 1.00 19.65 ? 46  TRP   B CA    1 
ATOM   1686 C  C     . TRP   B 1 20  ? 18.998  -18.507 52.546 1.00 22.44 ? 46  TRP   B C     1 
ATOM   1687 O  O     . TRP   B 1 20  ? 18.321  -17.554 52.166 1.00 21.95 ? 46  TRP   B O     1 
ATOM   1688 C  CB    . TRP   B 1 20  ? 21.418  -18.047 52.364 1.00 18.58 ? 46  TRP   B CB    1 
ATOM   1689 C  CG    . TRP   B 1 20  ? 22.771  -18.340 51.805 1.00 18.18 ? 46  TRP   B CG    1 
ATOM   1690 C  CD1   . TRP   B 1 20  ? 23.281  -17.925 50.607 1.00 18.56 ? 46  TRP   B CD1   1 
ATOM   1691 C  CD2   . TRP   B 1 20  ? 23.834  -19.005 52.487 1.00 17.79 ? 46  TRP   B CD2   1 
ATOM   1692 N  NE1   . TRP   B 1 20  ? 24.605  -18.288 50.508 1.00 18.63 ? 46  TRP   B NE1   1 
ATOM   1693 C  CE2   . TRP   B 1 20  ? 24.959  -18.987 51.634 1.00 18.41 ? 46  TRP   B CE2   1 
ATOM   1694 C  CE3   . TRP   B 1 20  ? 23.955  -19.588 53.755 1.00 18.77 ? 46  TRP   B CE3   1 
ATOM   1695 C  CZ2   . TRP   B 1 20  ? 26.187  -19.514 52.018 1.00 18.84 ? 46  TRP   B CZ2   1 
ATOM   1696 C  CZ3   . TRP   B 1 20  ? 25.155  -20.180 54.103 1.00 19.29 ? 46  TRP   B CZ3   1 
ATOM   1697 C  CH2   . TRP   B 1 20  ? 26.261  -20.116 53.252 1.00 19.21 ? 46  TRP   B CH2   1 
ATOM   1698 N  N     . PHE   B 1 21  ? 18.712  -19.222 53.661 1.00 24.21 ? 47  PHE   B N     1 
ATOM   1699 C  CA    . PHE   B 1 21  ? 17.588  -18.955 54.569 1.00 26.84 ? 47  PHE   B CA    1 
ATOM   1700 C  C     . PHE   B 1 21  ? 18.134  -18.678 55.970 1.00 27.23 ? 47  PHE   B C     1 
ATOM   1701 O  O     . PHE   B 1 21  ? 19.162  -19.224 56.358 1.00 25.57 ? 47  PHE   B O     1 
ATOM   1702 C  CB    . PHE   B 1 21  ? 16.668  -20.183 54.730 1.00 28.82 ? 47  PHE   B CB    1 
ATOM   1703 C  CG    . PHE   B 1 21  ? 15.715  -20.515 53.625 1.00 32.37 ? 47  PHE   B CG    1 
ATOM   1704 C  CD1   . PHE   B 1 21  ? 15.691  -19.772 52.461 1.00 34.44 ? 47  PHE   B CD1   1 
ATOM   1705 C  CD2   . PHE   B 1 21  ? 14.843  -21.584 53.741 1.00 34.40 ? 47  PHE   B CD2   1 
ATOM   1706 C  CE1   . PHE   B 1 21  ? 14.831  -20.108 51.428 1.00 36.00 ? 47  PHE   B CE1   1 
ATOM   1707 C  CE2   . PHE   B 1 21  ? 13.956  -21.889 52.723 1.00 35.75 ? 47  PHE   B CE2   1 
ATOM   1708 C  CZ    . PHE   B 1 21  ? 13.951  -21.146 51.576 1.00 36.00 ? 47  PHE   B CZ    1 
ATOM   1709 N  N     . PHE   B 1 22  ? 17.399  -17.902 56.753 1.00 29.31 ? 48  PHE   B N     1 
ATOM   1710 C  CA    . PHE   B 1 22  ? 17.747  -17.645 58.138 1.00 32.40 ? 48  PHE   B CA    1 
ATOM   1711 C  C     . PHE   B 1 22  ? 16.558  -18.090 58.987 1.00 36.17 ? 48  PHE   B C     1 
ATOM   1712 O  O     . PHE   B 1 22  ? 15.443  -17.591 58.802 1.00 36.35 ? 48  PHE   B O     1 
ATOM   1713 C  CB    . PHE   B 1 22  ? 18.083  -16.180 58.383 1.00 32.20 ? 48  PHE   B CB    1 
ATOM   1714 C  CG    . PHE   B 1 22  ? 18.597  -15.946 59.779 1.00 33.13 ? 48  PHE   B CG    1 
ATOM   1715 C  CD1   . PHE   B 1 22  ? 19.932  -16.117 60.079 1.00 34.01 ? 48  PHE   B CD1   1 
ATOM   1716 C  CD2   . PHE   B 1 22  ? 17.738  -15.582 60.800 1.00 34.37 ? 48  PHE   B CD2   1 
ATOM   1717 C  CE1   . PHE   B 1 22  ? 20.399  -15.912 61.365 1.00 34.93 ? 48  PHE   B CE1   1 
ATOM   1718 C  CE2   . PHE   B 1 22  ? 18.213  -15.376 62.090 1.00 35.01 ? 48  PHE   B CE2   1 
ATOM   1719 C  CZ    . PHE   B 1 22  ? 19.537  -15.556 62.366 1.00 34.77 ? 48  PHE   B CZ    1 
ATOM   1720 N  N     . LYS   B 1 23  ? 16.796  -19.058 59.877 1.00 38.82 ? 49  LYS   B N     1 
ATOM   1721 C  CA    . LYS   B 1 23  ? 15.788  -19.678 60.734 1.00 42.63 ? 49  LYS   B CA    1 
ATOM   1722 C  C     . LYS   B 1 23  ? 15.543  -18.907 62.033 1.00 45.63 ? 49  LYS   B C     1 
ATOM   1723 O  O     . LYS   B 1 23  ? 16.444  -18.244 62.543 1.00 45.92 ? 49  LYS   B O     1 
ATOM   1724 C  CB    . LYS   B 1 23  ? 16.262  -21.101 61.081 1.00 45.62 ? 49  LYS   B CB    1 
ATOM   1725 C  CG    . LYS   B 1 23  ? 15.163  -22.056 61.513 1.00 50.95 ? 49  LYS   B CG    1 
ATOM   1726 C  CD    . LYS   B 1 23  ? 15.731  -23.437 61.815 1.00 55.59 ? 49  LYS   B CD    1 
ATOM   1727 C  CE    . LYS   B 1 23  ? 14.791  -24.259 62.663 1.00 59.26 ? 49  LYS   B CE    1 
ATOM   1728 N  NZ    . LYS   B 1 23  ? 14.534  -23.610 63.976 1.00 61.64 ? 49  LYS   B NZ    1 
ATOM   1729 N  N     . ASN   B 1 24  ? 14.329  -18.999 62.576 1.00 47.78 ? 50  ASN   B N     1 
ATOM   1730 C  CA    . ASN   B 1 24  ? 14.012  -18.373 63.857 1.00 50.21 ? 50  ASN   B CA    1 
ATOM   1731 C  C     . ASN   B 1 24  ? 14.218  -19.428 64.937 1.00 51.44 ? 50  ASN   B C     1 
ATOM   1732 O  O     . ASN   B 1 24  ? 13.310  -20.213 65.191 1.00 51.60 ? 50  ASN   B O     1 
ATOM   1733 C  CB    . ASN   B 1 24  ? 12.555  -17.894 63.887 1.00 52.61 ? 50  ASN   B CB    1 
ATOM   1734 C  CG    . ASN   B 1 24  ? 12.297  -16.853 64.950 1.00 57.26 ? 50  ASN   B CG    1 
ATOM   1735 O  OD1   . ASN   B 1 24  ? 12.926  -15.790 64.963 1.00 58.88 ? 50  ASN   B OD1   1 
ATOM   1736 N  ND2   . ASN   B 1 24  ? 11.370  -17.134 65.870 1.00 58.31 ? 50  ASN   B ND2   1 
ATOM   1737 N  N     . ASP   B 1 25  ? 15.408  -19.485 65.541 1.00 52.38 ? 51  ASP   B N     1 
ATOM   1738 C  CA    . ASP   B 1 25  ? 15.683  -20.460 66.604 1.00 53.73 ? 51  ASP   B CA    1 
ATOM   1739 C  C     . ASP   B 1 25  ? 16.447  -19.756 67.715 1.00 54.38 ? 51  ASP   B C     1 
ATOM   1740 O  O     . ASP   B 1 25  ? 17.646  -19.508 67.580 1.00 54.86 ? 51  ASP   B O     1 
ATOM   1741 C  CB    . ASP   B 1 25  ? 16.485  -21.656 66.059 1.00 56.14 ? 51  ASP   B CB    1 
ATOM   1742 C  CG    . ASP   B 1 25  ? 16.692  -22.804 67.035 1.00 61.55 ? 51  ASP   B CG    1 
ATOM   1743 O  OD1   . ASP   B 1 25  ? 16.557  -22.581 68.258 1.00 62.36 ? 51  ASP   B OD1   1 
ATOM   1744 O  OD2   . ASP   B 1 25  ? 16.993  -23.924 66.574 1.00 64.05 ? 51  ASP   B OD2   1 
ATOM   1745 N  N     . LYS   B 1 26  ? 15.755  -19.443 68.818 1.00 54.19 ? 52  LYS   B N     1 
ATOM   1746 C  CA    . LYS   B 1 26  ? 16.339  -18.714 69.934 1.00 54.18 ? 52  LYS   B CA    1 
ATOM   1747 C  C     . LYS   B 1 26  ? 17.374  -19.503 70.721 1.00 53.60 ? 52  LYS   B C     1 
ATOM   1748 O  O     . LYS   B 1 26  ? 18.254  -18.891 71.324 1.00 54.05 ? 52  LYS   B O     1 
ATOM   1749 C  CB    . LYS   B 1 26  ? 15.249  -18.149 70.861 1.00 56.67 ? 52  LYS   B CB    1 
ATOM   1750 C  CG    . LYS   B 1 26  ? 14.673  -16.822 70.361 1.00 61.72 ? 52  LYS   B CG    1 
ATOM   1751 C  CD    . LYS   B 1 26  ? 15.752  -15.717 70.268 1.00 66.54 ? 52  LYS   B CD    1 
ATOM   1752 C  CE    . LYS   B 1 26  ? 15.413  -14.638 69.265 1.00 70.03 ? 52  LYS   B CE    1 
ATOM   1753 N  NZ    . LYS   B 1 26  ? 16.475  -13.600 69.193 1.00 72.10 ? 52  LYS   B NZ    1 
ATOM   1754 N  N     . SER   B 1 27  ? 17.310  -20.842 70.695 1.00 52.45 ? 53  SER   B N     1 
ATOM   1755 C  CA    . SER   B 1 27  ? 18.306  -21.655 71.392 1.00 51.78 ? 53  SER   B CA    1 
ATOM   1756 C  C     . SER   B 1 27  ? 19.657  -21.753 70.644 1.00 50.66 ? 53  SER   B C     1 
ATOM   1757 O  O     . SER   B 1 27  ? 20.525  -22.525 71.058 1.00 51.07 ? 53  SER   B O     1 
ATOM   1758 C  CB    . SER   B 1 27  ? 17.756  -23.045 71.699 1.00 53.14 ? 53  SER   B CB    1 
ATOM   1759 O  OG    . SER   B 1 27  ? 17.749  -23.885 70.558 1.00 55.30 ? 53  SER   B OG    1 
ATOM   1760 N  N     . LYS   B 1 28  ? 19.842  -20.969 69.561 1.00 48.97 ? 54  LYS   B N     1 
ATOM   1761 C  CA    . LYS   B 1 28  ? 21.071  -20.972 68.779 1.00 47.79 ? 54  LYS   B CA    1 
ATOM   1762 C  C     . LYS   B 1 28  ? 21.646  -19.571 68.599 1.00 45.74 ? 54  LYS   B C     1 
ATOM   1763 O  O     . LYS   B 1 28  ? 20.907  -18.584 68.590 1.00 46.31 ? 54  LYS   B O     1 
ATOM   1764 C  CB    . LYS   B 1 28  ? 20.828  -21.591 67.395 1.00 50.11 ? 54  LYS   B CB    1 
ATOM   1765 C  CG    . LYS   B 1 28  ? 20.550  -23.085 67.406 1.00 55.30 ? 54  LYS   B CG    1 
ATOM   1766 C  CD    . LYS   B 1 28  ? 20.366  -23.598 65.989 1.00 61.07 ? 54  LYS   B CD    1 
ATOM   1767 C  CE    . LYS   B 1 28  ? 20.076  -25.078 65.930 1.00 65.59 ? 54  LYS   B CE    1 
ATOM   1768 N  NZ    . LYS   B 1 28  ? 19.856  -25.529 64.528 1.00 68.23 ? 54  LYS   B NZ    1 
ATOM   1769 N  N     . THR   B 1 29  ? 22.972  -19.488 68.410 1.00 42.97 ? 55  THR   B N     1 
ATOM   1770 C  CA    . THR   B 1 29  ? 23.662  -18.227 68.128 1.00 40.24 ? 55  THR   B CA    1 
ATOM   1771 C  C     . THR   B 1 29  ? 23.306  -17.782 66.676 1.00 36.25 ? 55  THR   B C     1 
ATOM   1772 O  O     . THR   B 1 29  ? 22.811  -18.598 65.890 1.00 36.34 ? 55  THR   B O     1 
ATOM   1773 C  CB    . THR   B 1 29  ? 25.160  -18.429 68.344 1.00 42.04 ? 55  THR   B CB    1 
ATOM   1774 O  OG1   . THR   B 1 29  ? 25.848  -17.180 68.230 1.00 43.81 ? 55  THR   B OG1   1 
ATOM   1775 C  CG2   . THR   B 1 29  ? 25.729  -19.413 67.374 1.00 42.32 ? 55  THR   B CG2   1 
ATOM   1776 N  N     . TRP   B 1 30  ? 23.518  -16.494 66.327 1.00 32.96 ? 56  TRP   B N     1 
ATOM   1777 C  CA    . TRP   B 1 30  ? 23.125  -15.967 65.001 1.00 30.38 ? 56  TRP   B CA    1 
ATOM   1778 C  C     . TRP   B 1 30  ? 23.582  -16.837 63.796 1.00 27.86 ? 56  TRP   B C     1 
ATOM   1779 O  O     . TRP   B 1 30  ? 22.726  -17.303 63.057 1.00 27.47 ? 56  TRP   B O     1 
ATOM   1780 C  CB    . TRP   B 1 30  ? 23.551  -14.490 64.802 1.00 29.79 ? 56  TRP   B CB    1 
ATOM   1781 C  CG    . TRP   B 1 30  ? 22.870  -13.828 63.630 1.00 29.32 ? 56  TRP   B CG    1 
ATOM   1782 C  CD1   . TRP   B 1 30  ? 21.664  -13.193 63.637 1.00 30.05 ? 56  TRP   B CD1   1 
ATOM   1783 C  CD2   . TRP   B 1 30  ? 23.333  -13.795 62.270 1.00 28.75 ? 56  TRP   B CD2   1 
ATOM   1784 N  NE1   . TRP   B 1 30  ? 21.323  -12.811 62.357 1.00 30.31 ? 56  TRP   B NE1   1 
ATOM   1785 C  CE2   . TRP   B 1 30  ? 22.354  -13.125 61.508 1.00 29.71 ? 56  TRP   B CE2   1 
ATOM   1786 C  CE3   . TRP   B 1 30  ? 24.493  -14.243 61.626 1.00 28.66 ? 56  TRP   B CE3   1 
ATOM   1787 C  CZ2   . TRP   B 1 30  ? 22.465  -12.966 60.123 1.00 29.66 ? 56  TRP   B CZ2   1 
ATOM   1788 C  CZ3   . TRP   B 1 30  ? 24.607  -14.066 60.260 1.00 29.21 ? 56  TRP   B CZ3   1 
ATOM   1789 C  CH2   . TRP   B 1 30  ? 23.608  -13.423 59.526 1.00 29.13 ? 56  TRP   B CH2   1 
ATOM   1790 N  N     . GLN   B 1 31  ? 24.900  -17.078 63.608 1.00 26.25 ? 57  GLN   B N     1 
ATOM   1791 C  CA    . GLN   B 1 31  ? 25.399  -17.853 62.452 1.00 25.37 ? 57  GLN   B CA    1 
ATOM   1792 C  C     . GLN   B 1 31  ? 24.822  -19.253 62.332 1.00 24.05 ? 57  GLN   B C     1 
ATOM   1793 O  O     . GLN   B 1 31  ? 24.556  -19.720 61.221 1.00 23.09 ? 57  GLN   B O     1 
ATOM   1794 C  CB    . GLN   B 1 31  ? 26.931  -17.916 62.441 1.00 26.70 ? 57  GLN   B CB    1 
ATOM   1795 C  CG    . GLN   B 1 31  ? 27.566  -16.566 62.185 1.00 29.82 ? 57  GLN   B CG    1 
ATOM   1796 C  CD    . GLN   B 1 31  ? 29.027  -16.709 61.869 1.00 32.66 ? 57  GLN   B CD    1 
ATOM   1797 O  OE1   . GLN   B 1 31  ? 29.451  -17.645 61.195 1.00 33.25 ? 57  GLN   B OE1   1 
ATOM   1798 N  NE2   . GLN   B 1 31  ? 29.814  -15.767 62.334 1.00 33.23 ? 57  GLN   B NE2   1 
ATOM   1799 N  N     . ALA   B 1 32  ? 24.575  -19.901 63.482 1.00 23.37 ? 58  ALA   B N     1 
ATOM   1800 C  CA    . ALA   B 1 32  ? 23.998  -21.237 63.543 1.00 23.78 ? 58  ALA   B CA    1 
ATOM   1801 C  C     . ALA   B 1 32  ? 22.579  -21.335 62.931 1.00 24.56 ? 58  ALA   B C     1 
ATOM   1802 O  O     . ALA   B 1 32  ? 22.090  -22.436 62.741 1.00 24.90 ? 58  ALA   B O     1 
ATOM   1803 C  CB    . ALA   B 1 32  ? 23.995  -21.743 64.985 1.00 23.96 ? 58  ALA   B CB    1 
ATOM   1804 N  N     . ASN   B 1 33  ? 21.937  -20.205 62.600 1.00 24.89 ? 59  ASN   B N     1 
ATOM   1805 C  CA    . ASN   B 1 33  ? 20.601  -20.231 62.001 1.00 25.40 ? 59  ASN   B CA    1 
ATOM   1806 C  C     . ASN   B 1 33  ? 20.611  -20.048 60.469 1.00 24.90 ? 59  ASN   B C     1 
ATOM   1807 O  O     . ASN   B 1 33  ? 19.550  -20.113 59.847 1.00 25.45 ? 59  ASN   B O     1 
ATOM   1808 C  CB    . ASN   B 1 33  ? 19.685  -19.225 62.691 1.00 27.14 ? 59  ASN   B CB    1 
ATOM   1809 C  CG    . ASN   B 1 33  ? 19.458  -19.582 64.140 1.00 31.88 ? 59  ASN   B CG    1 
ATOM   1810 O  OD1   . ASN   B 1 33  ? 19.303  -20.756 64.498 1.00 32.18 ? 59  ASN   B OD1   1 
ATOM   1811 N  ND2   . ASN   B 1 33  ? 19.464  -18.583 65.013 1.00 33.86 ? 59  ASN   B ND2   1 
ATOM   1812 N  N     . LEU   B 1 34  ? 21.802  -19.837 59.860 1.00 23.65 ? 60  LEU   B N     1 
ATOM   1813 C  CA    . LEU   B 1 34  ? 21.941  -19.686 58.411 1.00 23.08 ? 60  LEU   B CA    1 
ATOM   1814 C  C     . LEU   B 1 34  ? 21.931  -21.058 57.768 1.00 21.65 ? 60  LEU   B C     1 
ATOM   1815 O  O     . LEU   B 1 34  ? 22.490  -22.010 58.317 1.00 21.42 ? 60  LEU   B O     1 
ATOM   1816 C  CB    . LEU   B 1 34  ? 23.257  -18.979 58.053 1.00 24.05 ? 60  LEU   B CB    1 
ATOM   1817 C  CG    . LEU   B 1 34  ? 23.305  -17.457 58.232 1.00 26.07 ? 60  LEU   B CG    1 
ATOM   1818 C  CD1   . LEU   B 1 34  ? 24.696  -16.946 57.989 1.00 26.58 ? 60  LEU   B CD1   1 
ATOM   1819 C  CD2   . LEU   B 1 34  ? 22.318  -16.752 57.285 1.00 26.87 ? 60  LEU   B CD2   1 
ATOM   1820 N  N     . ARG   B 1 35  ? 21.265  -21.170 56.632 1.00 20.22 ? 61  ARG   B N     1 
ATOM   1821 C  CA    . ARG   B 1 35  ? 21.106  -22.429 55.910 1.00 20.22 ? 61  ARG   B CA    1 
ATOM   1822 C  C     . ARG   B 1 35  ? 21.312  -22.154 54.422 1.00 20.18 ? 61  ARG   B C     1 
ATOM   1823 O  O     . ARG   B 1 35  ? 20.679  -21.277 53.891 1.00 18.53 ? 61  ARG   B O     1 
ATOM   1824 C  CB    . ARG   B 1 35  ? 19.668  -22.962 56.095 1.00 20.68 ? 61  ARG   B CB    1 
ATOM   1825 C  CG    . ARG   B 1 35  ? 19.308  -23.487 57.478 1.00 24.17 ? 61  ARG   B CG    1 
ATOM   1826 C  CD    . ARG   B 1 35  ? 20.197  -24.651 57.890 1.00 26.34 ? 61  ARG   B CD    1 
ATOM   1827 N  NE    . ARG   B 1 35  ? 19.846  -25.193 59.201 1.00 30.42 ? 61  ARG   B NE    1 
ATOM   1828 C  CZ    . ARG   B 1 35  ? 20.309  -24.732 60.362 1.00 32.63 ? 61  ARG   B CZ    1 
ATOM   1829 N  NH1   . ARG   B 1 35  ? 21.141  -23.699 60.392 1.00 30.94 ? 61  ARG   B NH1   1 
ATOM   1830 N  NH2   . ARG   B 1 35  ? 19.949  -25.309 61.504 1.00 33.79 ? 61  ARG   B NH2   1 
ATOM   1831 N  N     . LEU   B 1 36  ? 22.200  -22.885 53.768 1.00 21.42 ? 62  LEU   B N     1 
ATOM   1832 C  CA    . LEU   B 1 36  ? 22.443  -22.748 52.339 1.00 22.51 ? 62  LEU   B CA    1 
ATOM   1833 C  C     . LEU   B 1 36  ? 21.519  -23.753 51.667 1.00 22.94 ? 62  LEU   B C     1 
ATOM   1834 O  O     . LEU   B 1 36  ? 21.664  -24.941 51.884 1.00 23.59 ? 62  LEU   B O     1 
ATOM   1835 C  CB    . LEU   B 1 36  ? 23.920  -23.068 52.034 1.00 23.28 ? 62  LEU   B CB    1 
ATOM   1836 C  CG    . LEU   B 1 36  ? 24.311  -23.173 50.552 1.00 25.89 ? 62  LEU   B CG    1 
ATOM   1837 C  CD1   . LEU   B 1 36  ? 23.953  -21.929 49.807 1.00 26.47 ? 62  LEU   B CD1   1 
ATOM   1838 C  CD2   . LEU   B 1 36  ? 25.823  -23.431 50.398 1.00 26.68 ? 62  LEU   B CD2   1 
ATOM   1839 N  N     . ILE   B 1 37  ? 20.547  -23.285 50.911 1.00 23.50 ? 63  ILE   B N     1 
ATOM   1840 C  CA    . ILE   B 1 37  ? 19.540  -24.121 50.258 1.00 24.88 ? 63  ILE   B CA    1 
ATOM   1841 C  C     . ILE   B 1 37  ? 20.042  -24.766 48.950 1.00 25.64 ? 63  ILE   B C     1 
ATOM   1842 O  O     . ILE   B 1 37  ? 20.019  -25.998 48.819 1.00 26.01 ? 63  ILE   B O     1 
ATOM   1843 C  CB    . ILE   B 1 37  ? 18.218  -23.319 50.047 1.00 26.34 ? 63  ILE   B CB    1 
ATOM   1844 C  CG1   . ILE   B 1 37  ? 17.763  -22.605 51.333 1.00 27.75 ? 63  ILE   B CG1   1 
ATOM   1845 C  CG2   . ILE   B 1 37  ? 17.107  -24.211 49.478 1.00 27.31 ? 63  ILE   B CG2   1 
ATOM   1846 C  CD1   . ILE   B 1 37  ? 17.641  -23.521 52.536 1.00 29.69 ? 63  ILE   B CD1   1 
ATOM   1847 N  N     . SER   B 1 38  ? 20.469  -23.946 47.979 1.00 24.77 ? 64  SER   B N     1 
ATOM   1848 C  CA    . SER   B 1 38  ? 20.974  -24.473 46.723 1.00 25.15 ? 64  SER   B CA    1 
ATOM   1849 C  C     . SER   B 1 38  ? 21.686  -23.399 45.923 1.00 23.67 ? 64  SER   B C     1 
ATOM   1850 O  O     . SER   B 1 38  ? 21.567  -22.209 46.214 1.00 23.04 ? 64  SER   B O     1 
ATOM   1851 C  CB    . SER   B 1 38  ? 19.848  -25.087 45.886 1.00 28.24 ? 64  SER   B CB    1 
ATOM   1852 O  OG    . SER   B 1 38  ? 18.984  -24.088 45.375 1.00 31.91 ? 64  SER   B OG    1 
ATOM   1853 N  N     . LYS   B 1 39  ? 22.428  -23.832 44.905 1.00 22.65 ? 65  LYS   B N     1 
ATOM   1854 C  CA    . LYS   B 1 39  ? 23.133  -22.946 43.996 1.00 22.39 ? 65  LYS   B CA    1 
ATOM   1855 C  C     . LYS   B 1 39  ? 22.594  -23.130 42.575 1.00 21.41 ? 65  LYS   B C     1 
ATOM   1856 O  O     . LYS   B 1 39  ? 21.962  -24.136 42.287 1.00 22.11 ? 65  LYS   B O     1 
ATOM   1857 C  CB    . LYS   B 1 39  ? 24.637  -23.235 44.050 1.00 24.66 ? 65  LYS   B CB    1 
ATOM   1858 C  CG    . LYS   B 1 39  ? 25.213  -23.089 45.454 1.00 28.75 ? 65  LYS   B CG    1 
ATOM   1859 C  CD    . LYS   B 1 39  ? 26.712  -23.251 45.448 1.00 33.08 ? 65  LYS   B CD    1 
ATOM   1860 C  CE    . LYS   B 1 39  ? 27.278  -23.071 46.832 1.00 36.73 ? 65  LYS   B CE    1 
ATOM   1861 N  NZ    . LYS   B 1 39  ? 28.756  -23.199 46.827 1.00 38.79 ? 65  LYS   B NZ    1 
ATOM   1862 N  N     . PHE   B 1 40  ? 22.847  -22.164 41.690 1.00 19.58 ? 66  PHE   B N     1 
ATOM   1863 C  CA    . PHE   B 1 40  ? 22.416  -22.203 40.290 1.00 18.45 ? 66  PHE   B CA    1 
ATOM   1864 C  C     . PHE   B 1 40  ? 23.261  -21.201 39.486 1.00 18.51 ? 66  PHE   B C     1 
ATOM   1865 O  O     . PHE   B 1 40  ? 23.761  -20.206 40.038 1.00 18.73 ? 66  PHE   B O     1 
ATOM   1866 C  CB    . PHE   B 1 40  ? 20.912  -21.885 40.150 1.00 17.71 ? 66  PHE   B CB    1 
ATOM   1867 C  CG    . PHE   B 1 40  ? 20.501  -20.504 40.603 1.00 17.84 ? 66  PHE   B CG    1 
ATOM   1868 C  CD1   . PHE   B 1 40  ? 20.539  -19.425 39.728 1.00 18.76 ? 66  PHE   B CD1   1 
ATOM   1869 C  CD2   . PHE   B 1 40  ? 20.053  -20.284 41.891 1.00 17.75 ? 66  PHE   B CD2   1 
ATOM   1870 C  CE1   . PHE   B 1 40  ? 20.194  -18.144 40.161 1.00 19.08 ? 66  PHE   B CE1   1 
ATOM   1871 C  CE2   . PHE   B 1 40  ? 19.671  -19.011 42.304 1.00 18.35 ? 66  PHE   B CE2   1 
ATOM   1872 C  CZ    . PHE   B 1 40  ? 19.753  -17.951 41.441 1.00 18.51 ? 66  PHE   B CZ    1 
ATOM   1873 N  N     . ASP   B 1 41  ? 23.440  -21.464 38.195 1.00 17.76 ? 67  ASP   B N     1 
ATOM   1874 C  CA    . ASP   B 1 41  ? 24.191  -20.565 37.323 1.00 17.34 ? 67  ASP   B CA    1 
ATOM   1875 C  C     . ASP   B 1 41  ? 23.590  -20.454 35.912 1.00 16.13 ? 67  ASP   B C     1 
ATOM   1876 O  O     . ASP   B 1 41  ? 24.279  -20.059 34.974 1.00 15.44 ? 67  ASP   B O     1 
ATOM   1877 C  CB    . ASP   B 1 41  ? 25.687  -20.920 37.278 1.00 20.13 ? 67  ASP   B CB    1 
ATOM   1878 C  CG    . ASP   B 1 41  ? 25.986  -22.366 36.908 1.00 28.44 ? 67  ASP   B CG    1 
ATOM   1879 O  OD1   . ASP   B 1 41  ? 25.038  -23.097 36.542 1.00 29.06 ? 67  ASP   B OD1   1 
ATOM   1880 O  OD2   . ASP   B 1 41  ? 27.167  -22.768 36.995 1.00 32.54 ? 67  ASP   B OD2   1 
ATOM   1881 N  N     . THR   B 1 42  ? 22.304  -20.765 35.767 1.00 15.53 ? 68  THR   B N     1 
ATOM   1882 C  CA    . THR   B 1 42  ? 21.604  -20.604 34.511 1.00 16.19 ? 68  THR   B CA    1 
ATOM   1883 C  C     . THR   B 1 42  ? 20.244  -19.898 34.770 1.00 16.05 ? 68  THR   B C     1 
ATOM   1884 O  O     . THR   B 1 42  ? 19.727  -19.927 35.884 1.00 16.14 ? 68  THR   B O     1 
ATOM   1885 C  CB    . THR   B 1 42  ? 21.381  -21.944 33.783 1.00 18.35 ? 68  THR   B CB    1 
ATOM   1886 O  OG1   . THR   B 1 42  ? 20.391  -22.701 34.491 1.00 19.81 ? 68  THR   B OG1   1 
ATOM   1887 C  CG2   . THR   B 1 42  ? 22.668  -22.748 33.560 1.00 18.77 ? 68  THR   B CG2   1 
ATOM   1888 N  N     . VAL   B 1 43  ? 19.670  -19.309 33.725 1.00 15.84 ? 69  VAL   B N     1 
ATOM   1889 C  CA    . VAL   B 1 43  ? 18.372  -18.655 33.748 1.00 16.85 ? 69  VAL   B CA    1 
ATOM   1890 C  C     . VAL   B 1 43  ? 17.287  -19.706 34.112 1.00 17.16 ? 69  VAL   B C     1 
ATOM   1891 O  O     . VAL   B 1 43  ? 16.434  -19.426 34.953 1.00 17.76 ? 69  VAL   B O     1 
ATOM   1892 C  CB    . VAL   B 1 43  ? 18.109  -18.064 32.326 1.00 18.33 ? 69  VAL   B CB    1 
ATOM   1893 C  CG1   . VAL   B 1 43  ? 16.640  -17.719 32.118 1.00 18.66 ? 69  VAL   B CG1   1 
ATOM   1894 C  CG2   . VAL   B 1 43  ? 19.014  -16.846 32.042 1.00 19.14 ? 69  VAL   B CG2   1 
ATOM   1895 N  N     . GLU   B 1 44  ? 17.308  -20.891 33.463 1.00 16.65 ? 70  GLU   B N     1 
ATOM   1896 C  CA    . GLU   B 1 44  ? 16.316  -21.954 33.703 1.00 17.09 ? 70  GLU   B CA    1 
ATOM   1897 C  C     . GLU   B 1 44  ? 16.346  -22.443 35.154 1.00 16.78 ? 70  GLU   B C     1 
ATOM   1898 O  O     . GLU   B 1 44  ? 15.292  -22.723 35.714 1.00 17.08 ? 70  GLU   B O     1 
ATOM   1899 C  CB    . GLU   B 1 44  ? 16.499  -23.153 32.726 1.00 19.19 ? 70  GLU   B CB    1 
ATOM   1900 C  CG    . GLU   B 1 44  ? 16.230  -22.836 31.246 1.00 23.11 ? 70  GLU   B CG    1 
ATOM   1901 C  CD    . GLU   B 1 44  ? 17.371  -22.169 30.492 1.00 28.25 ? 70  GLU   B CD    1 
ATOM   1902 O  OE1   . GLU   B 1 44  ? 17.233  -21.945 29.268 1.00 31.33 ? 70  GLU   B OE1   1 
ATOM   1903 O  OE2   . GLU   B 1 44  ? 18.414  -21.880 31.120 1.00 28.00 ? 70  GLU   B OE2   1 
ATOM   1904 N  N     . ASP   B 1 45  ? 17.529  -22.572 35.747 1.00 16.44 ? 71  ASP   B N     1 
ATOM   1905 C  CA    . ASP   B 1 45  ? 17.634  -23.016 37.147 1.00 17.09 ? 71  ASP   B CA    1 
ATOM   1906 C  C     . ASP   B 1 45  ? 17.202  -21.907 38.103 1.00 16.63 ? 71  ASP   B C     1 
ATOM   1907 O  O     . ASP   B 1 45  ? 16.661  -22.210 39.155 1.00 17.49 ? 71  ASP   B O     1 
ATOM   1908 C  CB    . ASP   B 1 45  ? 19.022  -23.565 37.496 1.00 19.80 ? 71  ASP   B CB    1 
ATOM   1909 C  CG    . ASP   B 1 45  ? 19.370  -24.834 36.745 1.00 28.54 ? 71  ASP   B CG    1 
ATOM   1910 O  OD1   . ASP   B 1 45  ? 18.471  -25.688 36.571 1.00 30.01 ? 71  ASP   B OD1   1 
ATOM   1911 O  OD2   . ASP   B 1 45  ? 20.544  -24.969 36.313 1.00 32.12 ? 71  ASP   B OD2   1 
ATOM   1912 N  N     . PHE   B 1 46  ? 17.364  -20.627 37.723 1.00 15.82 ? 72  PHE   B N     1 
ATOM   1913 C  CA    . PHE   B 1 46  ? 16.854  -19.519 38.539 1.00 15.18 ? 72  PHE   B CA    1 
ATOM   1914 C  C     . PHE   B 1 46  ? 15.333  -19.596 38.571 1.00 15.29 ? 72  PHE   B C     1 
ATOM   1915 O  O     . PHE   B 1 46  ? 14.741  -19.564 39.651 1.00 15.49 ? 72  PHE   B O     1 
ATOM   1916 C  CB    . PHE   B 1 46  ? 17.273  -18.137 37.971 1.00 14.49 ? 72  PHE   B CB    1 
ATOM   1917 C  CG    . PHE   B 1 46  ? 16.460  -17.013 38.577 1.00 14.38 ? 72  PHE   B CG    1 
ATOM   1918 C  CD1   . PHE   B 1 46  ? 16.638  -16.645 39.900 1.00 14.93 ? 72  PHE   B CD1   1 
ATOM   1919 C  CD2   . PHE   B 1 46  ? 15.447  -16.401 37.854 1.00 15.39 ? 72  PHE   B CD2   1 
ATOM   1920 C  CE1   . PHE   B 1 46  ? 15.841  -15.665 40.476 1.00 16.00 ? 72  PHE   B CE1   1 
ATOM   1921 C  CE2   . PHE   B 1 46  ? 14.665  -15.408 38.427 1.00 16.40 ? 72  PHE   B CE2   1 
ATOM   1922 C  CZ    . PHE   B 1 46  ? 14.861  -15.050 39.736 1.00 15.96 ? 72  PHE   B CZ    1 
ATOM   1923 N  N     . TRP   B 1 47  ? 14.696  -19.682 37.378 1.00 14.89 ? 73  TRP   B N     1 
ATOM   1924 C  CA    . TRP   B 1 47  ? 13.244  -19.674 37.323 1.00 15.23 ? 73  TRP   B CA    1 
ATOM   1925 C  C     . TRP   B 1 47  ? 12.642  -20.891 37.973 1.00 16.12 ? 73  TRP   B C     1 
ATOM   1926 O  O     . TRP   B 1 47  ? 11.573  -20.777 38.565 1.00 16.73 ? 73  TRP   B O     1 
ATOM   1927 C  CB    . TRP   B 1 47  ? 12.734  -19.469 35.874 1.00 14.97 ? 73  TRP   B CB    1 
ATOM   1928 C  CG    . TRP   B 1 47  ? 12.948  -18.068 35.388 1.00 15.39 ? 73  TRP   B CG    1 
ATOM   1929 C  CD1   . TRP   B 1 47  ? 13.846  -17.649 34.452 1.00 16.47 ? 73  TRP   B CD1   1 
ATOM   1930 C  CD2   . TRP   B 1 47  ? 12.229  -16.898 35.808 1.00 15.35 ? 73  TRP   B CD2   1 
ATOM   1931 N  NE1   . TRP   B 1 47  ? 13.728  -16.289 34.260 1.00 16.69 ? 73  TRP   B NE1   1 
ATOM   1932 C  CE2   . TRP   B 1 47  ? 12.776  -15.798 35.113 1.00 16.16 ? 73  TRP   B CE2   1 
ATOM   1933 C  CE3   . TRP   B 1 47  ? 11.245  -16.659 36.775 1.00 15.81 ? 73  TRP   B CE3   1 
ATOM   1934 C  CZ2   . TRP   B 1 47  ? 12.334  -14.493 35.315 1.00 16.83 ? 73  TRP   B CZ2   1 
ATOM   1935 C  CZ3   . TRP   B 1 47  ? 10.834  -15.365 36.993 1.00 17.02 ? 73  TRP   B CZ3   1 
ATOM   1936 C  CH2   . TRP   B 1 47  ? 11.349  -14.302 36.242 1.00 17.13 ? 73  TRP   B CH2   1 
ATOM   1937 N  N     . ALA   B 1 48  ? 13.307  -22.059 37.874 1.00 16.03 ? 74  ALA   B N     1 
ATOM   1938 C  CA    . ALA   B 1 48  ? 12.783  -23.270 38.502 1.00 16.42 ? 74  ALA   B CA    1 
ATOM   1939 C  C     . ALA   B 1 48  ? 12.779  -23.138 40.019 1.00 15.77 ? 74  ALA   B C     1 
ATOM   1940 O  O     . ALA   B 1 48  ? 11.808  -23.535 40.651 1.00 15.96 ? 74  ALA   B O     1 
ATOM   1941 C  CB    . ALA   B 1 48  ? 13.579  -24.496 38.075 1.00 16.81 ? 74  ALA   B CB    1 
ATOM   1942 N  N     . LEU   B 1 49  ? 13.818  -22.553 40.592 1.00 15.29 ? 75  LEU   B N     1 
ATOM   1943 C  CA    . LEU   B 1 49  ? 13.910  -22.332 42.041 1.00 16.24 ? 75  LEU   B CA    1 
ATOM   1944 C  C     . LEU   B 1 49  ? 12.914  -21.233 42.491 1.00 17.83 ? 75  LEU   B C     1 
ATOM   1945 O  O     . LEU   B 1 49  ? 12.162  -21.453 43.449 1.00 18.95 ? 75  LEU   B O     1 
ATOM   1946 C  CB    . LEU   B 1 49  ? 15.334  -21.916 42.404 1.00 17.06 ? 75  LEU   B CB    1 
ATOM   1947 C  CG    . LEU   B 1 49  ? 15.587  -21.649 43.871 1.00 19.88 ? 75  LEU   B CG    1 
ATOM   1948 C  CD1   . LEU   B 1 49  ? 15.379  -22.937 44.699 1.00 21.09 ? 75  LEU   B CD1   1 
ATOM   1949 C  CD2   . LEU   B 1 49  ? 16.983  -21.097 44.072 1.00 20.68 ? 75  LEU   B CD2   1 
ATOM   1950 N  N     . TYR   B 1 50  ? 12.859  -20.087 41.770 1.00 17.25 ? 76  TYR   B N     1 
ATOM   1951 C  CA    . TYR   B 1 50  ? 11.914  -18.998 42.059 1.00 17.36 ? 76  TYR   B CA    1 
ATOM   1952 C  C     . TYR   B 1 50  ? 10.482  -19.505 42.051 1.00 17.93 ? 76  TYR   B C     1 
ATOM   1953 O  O     . TYR   B 1 50  ? 9.771   -19.292 43.024 1.00 18.21 ? 76  TYR   B O     1 
ATOM   1954 C  CB    . TYR   B 1 50  ? 12.053  -17.806 41.073 1.00 17.10 ? 76  TYR   B CB    1 
ATOM   1955 C  CG    . TYR   B 1 50  ? 11.086  -16.683 41.397 1.00 18.01 ? 76  TYR   B CG    1 
ATOM   1956 C  CD1   . TYR   B 1 50  ? 11.296  -15.856 42.492 1.00 18.77 ? 76  TYR   B CD1   1 
ATOM   1957 C  CD2   . TYR   B 1 50  ? 9.919   -16.511 40.665 1.00 18.63 ? 76  TYR   B CD2   1 
ATOM   1958 C  CE1   . TYR   B 1 50  ? 10.379  -14.878 42.843 1.00 19.79 ? 76  TYR   B CE1   1 
ATOM   1959 C  CE2   . TYR   B 1 50  ? 8.974   -15.555 41.027 1.00 20.08 ? 76  TYR   B CE2   1 
ATOM   1960 C  CZ    . TYR   B 1 50  ? 9.212   -14.737 42.115 1.00 21.27 ? 76  TYR   B CZ    1 
ATOM   1961 O  OH    . TYR   B 1 50  ? 8.308   -13.767 42.479 1.00 23.23 ? 76  TYR   B OH    1 
ATOM   1962 N  N     . ASN   B 1 51  ? 10.060  -20.191 40.984 1.00 18.45 ? 77  ASN   B N     1 
ATOM   1963 C  CA    . ASN   B 1 51  ? 8.696   -20.731 40.915 1.00 20.02 ? 77  ASN   B CA    1 
ATOM   1964 C  C     . ASN   B 1 51  ? 8.388   -21.757 41.991 1.00 21.83 ? 77  ASN   B C     1 
ATOM   1965 O  O     . ASN   B 1 51  ? 7.265   -21.800 42.490 1.00 21.79 ? 77  ASN   B O     1 
ATOM   1966 C  CB    . ASN   B 1 51  ? 8.414   -21.334 39.546 1.00 20.67 ? 77  ASN   B CB    1 
ATOM   1967 C  CG    . ASN   B 1 51  ? 8.341   -20.299 38.447 1.00 21.97 ? 77  ASN   B CG    1 
ATOM   1968 O  OD1   . ASN   B 1 51  ? 8.786   -20.532 37.316 1.00 22.13 ? 77  ASN   B OD1   1 
ATOM   1969 N  ND2   . ASN   B 1 51  ? 7.777   -19.134 38.766 1.00 21.31 ? 77  ASN   B ND2   1 
ATOM   1970 N  N     . HIS   B 1 52  ? 9.363   -22.596 42.330 1.00 23.37 ? 78  HIS   B N     1 
ATOM   1971 C  CA    . HIS   B 1 52  ? 9.170   -23.610 43.358 1.00 25.56 ? 78  HIS   B CA    1 
ATOM   1972 C  C     . HIS   B 1 52  ? 8.993   -22.955 44.735 1.00 27.37 ? 78  HIS   B C     1 
ATOM   1973 O  O     . HIS   B 1 52  ? 8.071   -23.306 45.458 1.00 28.05 ? 78  HIS   B O     1 
ATOM   1974 C  CB    . HIS   B 1 52  ? 10.347  -24.605 43.347 1.00 26.50 ? 78  HIS   B CB    1 
ATOM   1975 C  CG    . HIS   B 1 52  ? 10.302  -25.591 44.463 1.00 28.23 ? 78  HIS   B CG    1 
ATOM   1976 N  ND1   . HIS   B 1 52  ? 11.222  -25.553 45.489 1.00 29.98 ? 78  HIS   B ND1   1 
ATOM   1977 C  CD2   . HIS   B 1 52  ? 9.440   -26.611 44.680 1.00 28.93 ? 78  HIS   B CD2   1 
ATOM   1978 C  CE1   . HIS   B 1 52  ? 10.895  -26.545 46.293 1.00 30.15 ? 78  HIS   B CE1   1 
ATOM   1979 N  NE2   . HIS   B 1 52  ? 9.826   -27.207 45.848 1.00 29.90 ? 78  HIS   B NE2   1 
ATOM   1980 N  N     . ILE   B 1 53  ? 9.831   -21.986 45.074 1.00 28.37 ? 79  ILE   B N     1 
ATOM   1981 C  CA    . ILE   B 1 53  ? 9.752   -21.288 46.359 1.00 30.63 ? 79  ILE   B CA    1 
ATOM   1982 C  C     . ILE   B 1 53  ? 8.433   -20.515 46.510 1.00 32.16 ? 79  ILE   B C     1 
ATOM   1983 O  O     . ILE   B 1 53  ? 7.835   -20.534 47.592 1.00 32.13 ? 79  ILE   B O     1 
ATOM   1984 C  CB    . ILE   B 1 53  ? 11.000  -20.374 46.578 1.00 32.10 ? 79  ILE   B CB    1 
ATOM   1985 C  CG1   . ILE   B 1 53  ? 12.314  -21.192 46.585 1.00 33.44 ? 79  ILE   B CG1   1 
ATOM   1986 C  CG2   . ILE   B 1 53  ? 10.880  -19.550 47.866 1.00 32.69 ? 79  ILE   B CG2   1 
ATOM   1987 C  CD1   . ILE   B 1 53  ? 12.341  -22.330 47.518 1.00 35.05 ? 79  ILE   B CD1   1 
ATOM   1988 N  N     . GLN   B 1 54  ? 7.946   -19.896 45.410 1.00 32.85 ? 80  GLN   B N     1 
ATOM   1989 C  CA    . GLN   B 1 54  ? 6.687   -19.144 45.401 1.00 34.35 ? 80  GLN   B CA    1 
ATOM   1990 C  C     . GLN   B 1 54  ? 5.477   -20.012 45.690 1.00 37.08 ? 80  GLN   B C     1 
ATOM   1991 O  O     . GLN   B 1 54  ? 4.480   -19.505 46.198 1.00 37.83 ? 80  GLN   B O     1 
ATOM   1992 C  CB    . GLN   B 1 54  ? 6.480   -18.400 44.074 1.00 34.15 ? 80  GLN   B CB    1 
ATOM   1993 C  CG    . GLN   B 1 54  ? 7.381   -17.197 43.890 1.00 34.37 ? 80  GLN   B CG    1 
ATOM   1994 C  CD    . GLN   B 1 54  ? 7.222   -16.155 44.969 1.00 36.98 ? 80  GLN   B CD    1 
ATOM   1995 O  OE1   . GLN   B 1 54  ? 8.084   -15.999 45.839 1.00 38.49 ? 80  GLN   B OE1   1 
ATOM   1996 N  NE2   . GLN   B 1 54  ? 6.133   -15.403 44.929 1.00 36.60 ? 80  GLN   B NE2   1 
ATOM   1997 N  N     . LEU   B 1 55  ? 5.540   -21.302 45.343 1.00 38.38 ? 81  LEU   B N     1 
ATOM   1998 C  CA    . LEU   B 1 55  ? 4.448   -22.226 45.604 1.00 40.32 ? 81  LEU   B CA    1 
ATOM   1999 C  C     . LEU   B 1 55  ? 4.714   -23.168 46.796 1.00 42.56 ? 81  LEU   B C     1 
ATOM   2000 O  O     . LEU   B 1 55  ? 4.013   -24.166 46.942 1.00 43.15 ? 81  LEU   B O     1 
ATOM   2001 C  CB    . LEU   B 1 55  ? 4.125   -23.031 44.348 1.00 40.30 ? 81  LEU   B CB    1 
ATOM   2002 C  CG    . LEU   B 1 55  ? 3.579   -22.216 43.183 1.00 41.98 ? 81  LEU   B CG    1 
ATOM   2003 C  CD1   . LEU   B 1 55  ? 3.386   -23.088 41.961 1.00 42.67 ? 81  LEU   B CD1   1 
ATOM   2004 C  CD2   . LEU   B 1 55  ? 2.256   -21.559 43.540 1.00 42.59 ? 81  LEU   B CD2   1 
ATOM   2005 N  N     . SER   B 1 56  ? 5.707   -22.855 47.646 1.00 43.73 ? 82  SER   B N     1 
ATOM   2006 C  CA    . SER   B 1 56  ? 6.049   -23.669 48.817 1.00 45.11 ? 82  SER   B CA    1 
ATOM   2007 C  C     . SER   B 1 56  ? 6.131   -22.800 50.069 1.00 46.27 ? 82  SER   B C     1 
ATOM   2008 O  O     . SER   B 1 56  ? 5.250   -21.973 50.305 1.00 46.95 ? 82  SER   B O     1 
ATOM   2009 C  CB    . SER   B 1 56  ? 7.383   -24.379 48.610 1.00 46.54 ? 82  SER   B CB    1 
ATOM   2010 O  OG    . SER   B 1 56  ? 7.322   -25.267 47.507 1.00 49.21 ? 82  SER   B OG    1 
ATOM   2011 N  N     . CYS   B 1 63  ? 10.648  -17.106 58.055 1.00 38.18 ? 89  CYS   B N     1 
ATOM   2012 C  CA    . CYS   B 1 63  ? 12.089  -17.174 57.811 1.00 37.76 ? 89  CYS   B CA    1 
ATOM   2013 C  C     . CYS   B 1 63  ? 12.546  -16.115 56.816 1.00 36.20 ? 89  CYS   B C     1 
ATOM   2014 O  O     . CYS   B 1 63  ? 11.815  -15.785 55.891 1.00 37.16 ? 89  CYS   B O     1 
ATOM   2015 C  CB    . CYS   B 1 63  ? 12.494  -18.574 57.358 1.00 38.91 ? 89  CYS   B CB    1 
ATOM   2016 N  N     . ASP   B 1 64  ? 13.759  -15.586 56.992 1.00 34.00 ? 90  ASP   B N     1 
ATOM   2017 C  CA    . ASP   B 1 64  ? 14.325  -14.595 56.068 1.00 31.66 ? 90  ASP   B CA    1 
ATOM   2018 C  C     . ASP   B 1 64  ? 15.107  -15.293 54.929 1.00 30.11 ? 90  ASP   B C     1 
ATOM   2019 O  O     . ASP   B 1 64  ? 15.572  -16.415 55.122 1.00 29.35 ? 90  ASP   B O     1 
ATOM   2020 C  CB    . ASP   B 1 64  ? 15.207  -13.601 56.838 1.00 31.53 ? 90  ASP   B CB    1 
ATOM   2021 C  CG    . ASP   B 1 64  ? 14.450  -12.690 57.791 1.00 34.26 ? 90  ASP   B CG    1 
ATOM   2022 O  OD1   . ASP   B 1 64  ? 13.194  -12.653 57.716 1.00 33.72 ? 90  ASP   B OD1   1 
ATOM   2023 O  OD2   . ASP   B 1 64  ? 15.111  -11.988 58.595 1.00 36.03 ? 90  ASP   B OD2   1 
ATOM   2024 N  N     . TYR   B 1 65  ? 15.199  -14.656 53.724 1.00 28.74 ? 91  TYR   B N     1 
ATOM   2025 C  CA    . TYR   B 1 65  ? 15.849  -15.204 52.520 1.00 28.70 ? 91  TYR   B CA    1 
ATOM   2026 C  C     . TYR   B 1 65  ? 17.001  -14.270 52.028 1.00 24.27 ? 91  TYR   B C     1 
ATOM   2027 O  O     . TYR   B 1 65  ? 16.951  -13.070 52.244 1.00 22.58 ? 91  TYR   B O     1 
ATOM   2028 C  CB    . TYR   B 1 65  ? 14.845  -15.318 51.343 1.00 31.89 ? 91  TYR   B CB    1 
ATOM   2029 C  CG    . TYR   B 1 65  ? 13.633  -16.197 51.551 1.00 36.00 ? 91  TYR   B CG    1 
ATOM   2030 C  CD1   . TYR   B 1 65  ? 13.354  -17.242 50.684 1.00 38.16 ? 91  TYR   B CD1   1 
ATOM   2031 C  CD2   . TYR   B 1 65  ? 12.683  -15.891 52.514 1.00 38.44 ? 91  TYR   B CD2   1 
ATOM   2032 C  CE1   . TYR   B 1 65  ? 12.225  -18.040 50.851 1.00 40.01 ? 91  TYR   B CE1   1 
ATOM   2033 C  CE2   . TYR   B 1 65  ? 11.567  -16.700 52.711 1.00 40.33 ? 91  TYR   B CE2   1 
ATOM   2034 C  CZ    . TYR   B 1 65  ? 11.347  -17.782 51.882 1.00 41.68 ? 91  TYR   B CZ    1 
ATOM   2035 O  OH    . TYR   B 1 65  ? 10.223  -18.559 52.050 1.00 45.02 ? 91  TYR   B OH    1 
ATOM   2036 N  N     . SER   B 1 66  ? 17.967  -14.834 51.292 1.00 22.20 ? 92  SER   B N     1 
ATOM   2037 C  CA    . SER   B 1 66  ? 19.165  -14.171 50.766 1.00 20.95 ? 92  SER   B CA    1 
ATOM   2038 C  C     . SER   B 1 66  ? 19.558  -14.775 49.439 1.00 17.99 ? 92  SER   B C     1 
ATOM   2039 O  O     . SER   B 1 66  ? 19.584  -15.999 49.342 1.00 18.44 ? 92  SER   B O     1 
ATOM   2040 C  CB    . SER   B 1 66  ? 20.357  -14.523 51.656 1.00 23.46 ? 92  SER   B CB    1 
ATOM   2041 O  OG    . SER   B 1 66  ? 20.611  -13.530 52.615 1.00 30.24 ? 92  SER   B OG    1 
ATOM   2042 N  N     . LEU   B 1 67  ? 20.043  -13.963 48.505 1.00 15.01 ? 93  LEU   B N     1 
ATOM   2043 C  CA    . LEU   B 1 67  ? 20.614  -14.475 47.272 1.00 14.31 ? 93  LEU   B CA    1 
ATOM   2044 C  C     . LEU   B 1 67  ? 21.991  -13.846 47.174 1.00 13.73 ? 93  LEU   B C     1 
ATOM   2045 O  O     . LEU   B 1 67  ? 22.077  -12.635 47.001 1.00 13.25 ? 93  LEU   B O     1 
ATOM   2046 C  CB    . LEU   B 1 67  ? 19.808  -14.147 46.010 1.00 13.69 ? 93  LEU   B CB    1 
ATOM   2047 C  CG    . LEU   B 1 67  ? 20.347  -14.948 44.805 1.00 15.49 ? 93  LEU   B CG    1 
ATOM   2048 C  CD1   . LEU   B 1 67  ? 19.911  -16.436 44.892 1.00 15.99 ? 93  LEU   B CD1   1 
ATOM   2049 C  CD2   . LEU   B 1 67  ? 19.943  -14.317 43.471 1.00 16.16 ? 93  LEU   B CD2   1 
ATOM   2050 N  N     . PHE   B 1 68  ? 23.066  -14.638 47.297 1.00 12.85 ? 94  PHE   B N     1 
ATOM   2051 C  CA    . PHE   B 1 68  ? 24.428  -14.046 47.243 1.00 12.75 ? 94  PHE   B CA    1 
ATOM   2052 C  C     . PHE   B 1 68  ? 25.252  -14.736 46.196 1.00 12.99 ? 94  PHE   B C     1 
ATOM   2053 O  O     . PHE   B 1 68  ? 24.997  -15.892 45.886 1.00 13.77 ? 94  PHE   B O     1 
ATOM   2054 C  CB    . PHE   B 1 68  ? 25.139  -14.196 48.632 1.00 11.86 ? 94  PHE   B CB    1 
ATOM   2055 C  CG    . PHE   B 1 68  ? 24.885  -13.019 49.525 1.00 11.54 ? 94  PHE   B CG    1 
ATOM   2056 C  CD1   . PHE   B 1 68  ? 23.614  -12.772 50.027 1.00 13.20 ? 94  PHE   B CD1   1 
ATOM   2057 C  CD2   . PHE   B 1 68  ? 25.891  -12.101 49.794 1.00 11.12 ? 94  PHE   B CD2   1 
ATOM   2058 C  CE1   . PHE   B 1 68  ? 23.372  -11.657 50.824 1.00 13.60 ? 94  PHE   B CE1   1 
ATOM   2059 C  CE2   . PHE   B 1 68  ? 25.634  -10.976 50.550 1.00 11.52 ? 94  PHE   B CE2   1 
ATOM   2060 C  CZ    . PHE   B 1 68  ? 24.379  -10.764 51.066 1.00 12.42 ? 94  PHE   B CZ    1 
ATOM   2061 N  N     . LYS   B 1 69  ? 26.290  -14.077 45.690 1.00 13.27 ? 95  LYS   B N     1 
ATOM   2062 C  CA    . LYS   B 1 69  ? 27.183  -14.697 44.727 1.00 14.14 ? 95  LYS   B CA    1 
ATOM   2063 C  C     . LYS   B 1 69  ? 27.898  -15.882 45.381 1.00 16.09 ? 95  LYS   B C     1 
ATOM   2064 O  O     . LYS   B 1 69  ? 28.141  -15.892 46.599 1.00 15.72 ? 95  LYS   B O     1 
ATOM   2065 C  CB    . LYS   B 1 69  ? 28.224  -13.697 44.219 1.00 15.14 ? 95  LYS   B CB    1 
ATOM   2066 C  CG    . LYS   B 1 69  ? 27.636  -12.685 43.262 1.00 17.38 ? 95  LYS   B CG    1 
ATOM   2067 C  CD    . LYS   B 1 69  ? 28.640  -11.639 42.849 1.00 19.59 ? 95  LYS   B CD    1 
ATOM   2068 C  CE    . LYS   B 1 69  ? 27.980  -10.683 41.882 1.00 20.79 ? 95  LYS   B CE    1 
ATOM   2069 N  NZ    . LYS   B 1 69  ? 28.835  -9.495  41.665 1.00 20.87 ? 95  LYS   B NZ    1 
ATOM   2070 N  N     . ASP   B 1 70  ? 28.213  -16.881 44.577 1.00 17.27 ? 96  ASP   B N     1 
ATOM   2071 C  CA    . ASP   B 1 70  ? 28.907  -18.082 45.035 1.00 19.01 ? 96  ASP   B CA    1 
ATOM   2072 C  C     . ASP   B 1 70  ? 30.223  -17.744 45.769 1.00 19.81 ? 96  ASP   B C     1 
ATOM   2073 O  O     . ASP   B 1 70  ? 30.996  -16.927 45.294 1.00 20.17 ? 96  ASP   B O     1 
ATOM   2074 C  CB    . ASP   B 1 70  ? 29.168  -19.003 43.835 1.00 20.99 ? 96  ASP   B CB    1 
ATOM   2075 C  CG    . ASP   B 1 70  ? 29.669  -20.371 44.254 1.00 26.34 ? 96  ASP   B CG    1 
ATOM   2076 O  OD1   . ASP   B 1 70  ? 29.236  -20.858 45.310 1.00 26.79 ? 96  ASP   B OD1   1 
ATOM   2077 O  OD2   . ASP   B 1 70  ? 30.506  -20.940 43.526 1.00 29.15 ? 96  ASP   B OD2   1 
ATOM   2078 N  N     . GLY   B 1 71  ? 30.422  -18.321 46.942 1.00 20.33 ? 97  GLY   B N     1 
ATOM   2079 C  CA    . GLY   B 1 71  ? 31.621  -18.040 47.735 1.00 20.97 ? 97  GLY   B CA    1 
ATOM   2080 C  C     . GLY   B 1 71  ? 31.465  -16.903 48.731 1.00 20.56 ? 97  GLY   B C     1 
ATOM   2081 O  O     . GLY   B 1 71  ? 32.387  -16.621 49.498 1.00 21.62 ? 97  GLY   B O     1 
ATOM   2082 N  N     . ILE   B 1 72  ? 30.319  -16.219 48.726 1.00 19.10 ? 98  ILE   B N     1 
ATOM   2083 C  CA    . ILE   B 1 72  ? 30.073  -15.120 49.659 1.00 18.26 ? 98  ILE   B CA    1 
ATOM   2084 C  C     . ILE   B 1 72  ? 28.936  -15.535 50.555 1.00 17.38 ? 98  ILE   B C     1 
ATOM   2085 O  O     . ILE   B 1 72  ? 27.837  -15.761 50.068 1.00 17.70 ? 98  ILE   B O     1 
ATOM   2086 C  CB    . ILE   B 1 72  ? 29.725  -13.783 48.954 1.00 18.88 ? 98  ILE   B CB    1 
ATOM   2087 C  CG1   . ILE   B 1 72  ? 30.690  -13.468 47.798 1.00 20.45 ? 98  ILE   B CG1   1 
ATOM   2088 C  CG2   . ILE   B 1 72  ? 29.629  -12.623 49.982 1.00 18.68 ? 98  ILE   B CG2   1 
ATOM   2089 C  CD1   . ILE   B 1 72  ? 30.479  -12.068 47.127 1.00 21.84 ? 98  ILE   B CD1   1 
ATOM   2090 N  N     . GLU   B 1 73  ? 29.202  -15.679 51.854 1.00 16.19 ? 99  GLU   B N     1 
ATOM   2091 C  CA    . GLU   B 1 73  ? 28.190  -16.021 52.834 1.00 16.43 ? 99  GLU   B CA    1 
ATOM   2092 C  C     . GLU   B 1 73  ? 27.398  -14.727 53.150 1.00 16.19 ? 99  GLU   B C     1 
ATOM   2093 O  O     . GLU   B 1 73  ? 27.985  -13.655 53.162 1.00 14.66 ? 99  GLU   B O     1 
ATOM   2094 C  CB    . GLU   B 1 73  ? 28.881  -16.580 54.104 1.00 19.72 ? 99  GLU   B CB    1 
ATOM   2095 C  CG    . GLU   B 1 73  ? 29.541  -17.924 53.837 1.00 27.16 ? 99  GLU   B CG    1 
ATOM   2096 C  CD    . GLU   B 1 73  ? 29.898  -18.707 55.081 1.00 37.70 ? 99  GLU   B CD    1 
ATOM   2097 O  OE1   . GLU   B 1 73  ? 29.439  -19.864 55.210 1.00 41.41 ? 99  GLU   B OE1   1 
ATOM   2098 O  OE2   . GLU   B 1 73  ? 30.636  -18.164 55.930 1.00 42.30 ? 99  GLU   B OE2   1 
ATOM   2099 N  N     . PRO   B 1 74  ? 26.074  -14.825 53.397 1.00 17.01 ? 100 PRO   B N     1 
ATOM   2100 C  CA    . PRO   B 1 74  ? 25.254  -13.618 53.632 1.00 17.77 ? 100 PRO   B CA    1 
ATOM   2101 C  C     . PRO   B 1 74  ? 25.402  -13.040 55.036 1.00 18.47 ? 100 PRO   B C     1 
ATOM   2102 O  O     . PRO   B 1 74  ? 24.463  -13.088 55.831 1.00 19.43 ? 100 PRO   B O     1 
ATOM   2103 C  CB    . PRO   B 1 74  ? 23.818  -14.127 53.392 1.00 18.29 ? 100 PRO   B CB    1 
ATOM   2104 C  CG    . PRO   B 1 74  ? 23.871  -15.551 53.771 1.00 18.40 ? 100 PRO   B CG    1 
ATOM   2105 C  CD    . PRO   B 1 74  ? 25.249  -16.041 53.382 1.00 16.85 ? 100 PRO   B CD    1 
ATOM   2106 N  N     . MET   B 1 75  ? 26.589  -12.550 55.356 1.00 17.96 ? 101 MET   B N     1 
ATOM   2107 C  CA    . MET   B 1 75  ? 26.855  -12.009 56.682 1.00 18.68 ? 101 MET   B CA    1 
ATOM   2108 C  C     . MET   B 1 75  ? 28.011  -11.012 56.655 1.00 18.53 ? 101 MET   B C     1 
ATOM   2109 O  O     . MET   B 1 75  ? 28.939  -11.160 55.857 1.00 17.73 ? 101 MET   B O     1 
ATOM   2110 C  CB    . MET   B 1 75  ? 27.114  -13.145 57.691 1.00 18.75 ? 101 MET   B CB    1 
ATOM   2111 C  CG    . MET   B 1 75  ? 28.305  -14.000 57.347 1.00 20.84 ? 101 MET   B CG    1 
ATOM   2112 S  SD    . MET   B 1 75  ? 28.554  -15.289 58.596 1.00 31.34 ? 101 MET   B SD    1 
ATOM   2113 C  CE    . MET   B 1 75  ? 30.246  -15.796 58.194 1.00 31.68 ? 101 MET   B CE    1 
ATOM   2114 N  N     . TRP   B 1 76  ? 27.942  -9.997  57.522 1.00 19.58 ? 102 TRP   B N     1 
ATOM   2115 C  CA    . TRP   B 1 76  ? 28.966  -8.946  57.653 1.00 21.45 ? 102 TRP   B CA    1 
ATOM   2116 C  C     . TRP   B 1 76  ? 30.375  -9.512  57.849 1.00 21.74 ? 102 TRP   B C     1 
ATOM   2117 O  O     . TRP   B 1 76  ? 31.358  -8.877  57.471 1.00 21.70 ? 102 TRP   B O     1 
ATOM   2118 C  CB    . TRP   B 1 76  ? 28.671  -8.060  58.877 1.00 22.06 ? 102 TRP   B CB    1 
ATOM   2119 C  CG    . TRP   B 1 76  ? 27.304  -7.473  58.924 1.00 22.88 ? 102 TRP   B CG    1 
ATOM   2120 C  CD1   . TRP   B 1 76  ? 26.506  -7.150  57.864 1.00 24.33 ? 102 TRP   B CD1   1 
ATOM   2121 C  CD2   . TRP   B 1 76  ? 26.544  -7.197  60.098 1.00 23.14 ? 102 TRP   B CD2   1 
ATOM   2122 N  NE1   . TRP   B 1 76  ? 25.317  -6.637  58.311 1.00 24.46 ? 102 TRP   B NE1   1 
ATOM   2123 C  CE2   . TRP   B 1 76  ? 25.307  -6.668  59.682 1.00 24.03 ? 102 TRP   B CE2   1 
ATOM   2124 C  CE3   . TRP   B 1 76  ? 26.780  -7.370  61.466 1.00 23.99 ? 102 TRP   B CE3   1 
ATOM   2125 C  CZ2   . TRP   B 1 76  ? 24.316  -6.301  60.582 1.00 24.95 ? 102 TRP   B CZ2   1 
ATOM   2126 C  CZ3   . TRP   B 1 76  ? 25.822  -6.947  62.362 1.00 25.28 ? 102 TRP   B CZ3   1 
ATOM   2127 C  CH2   . TRP   B 1 76  ? 24.609  -6.413  61.919 1.00 25.73 ? 102 TRP   B CH2   1 
ATOM   2128 N  N     . GLU   B 1 77  ? 30.464  -10.681 58.468 1.00 21.75 ? 103 GLU   B N     1 
ATOM   2129 C  CA    . GLU   B 1 77  ? 31.704  -11.375 58.782 1.00 22.99 ? 103 GLU   B CA    1 
ATOM   2130 C  C     . GLU   B 1 77  ? 32.473  -11.853 57.584 1.00 23.82 ? 103 GLU   B C     1 
ATOM   2131 O  O     . GLU   B 1 77  ? 33.690  -12.034 57.680 1.00 25.37 ? 103 GLU   B O     1 
ATOM   2132 C  CB    . GLU   B 1 77  ? 31.429  -12.540 59.732 1.00 25.56 ? 103 GLU   B CB    1 
ATOM   2133 C  CG    . GLU   B 1 77  ? 31.022  -12.053 61.111 1.00 29.53 ? 103 GLU   B CG    1 
ATOM   2134 C  CD    . GLU   B 1 77  ? 29.535  -11.884 61.356 1.00 33.51 ? 103 GLU   B CD    1 
ATOM   2135 O  OE1   . GLU   B 1 77  ? 28.757  -11.778 60.379 1.00 28.29 ? 103 GLU   B OE1   1 
ATOM   2136 O  OE2   . GLU   B 1 77  ? 29.147  -11.849 62.547 1.00 38.81 ? 103 GLU   B OE2   1 
ATOM   2137 N  N     . ASP   B 1 78  ? 31.792  -12.064 56.455 1.00 22.17 ? 104 ASP   B N     1 
ATOM   2138 C  CA    . ASP   B 1 78  ? 32.452  -12.495 55.240 1.00 21.86 ? 104 ASP   B CA    1 
ATOM   2139 C  C     . ASP   B 1 78  ? 33.404  -11.405 54.745 1.00 21.65 ? 104 ASP   B C     1 
ATOM   2140 O  O     . ASP   B 1 78  ? 33.065  -10.227 54.799 1.00 20.75 ? 104 ASP   B O     1 
ATOM   2141 C  CB    . ASP   B 1 78  ? 31.414  -12.804 54.156 1.00 22.34 ? 104 ASP   B CB    1 
ATOM   2142 C  CG    . ASP   B 1 78  ? 31.995  -13.564 52.984 1.00 26.59 ? 104 ASP   B CG    1 
ATOM   2143 O  OD1   . ASP   B 1 78  ? 32.705  -12.941 52.158 1.00 28.20 ? 104 ASP   B OD1   1 
ATOM   2144 O  OD2   . ASP   B 1 78  ? 31.718  -14.776 52.868 1.00 26.89 ? 104 ASP   B OD2   1 
ATOM   2145 N  N     . GLU   B 1 79  ? 34.568  -11.805 54.228 1.00 22.19 ? 105 GLU   B N     1 
ATOM   2146 C  CA    . GLU   B 1 79  ? 35.588  -10.889 53.682 1.00 23.12 ? 105 GLU   B CA    1 
ATOM   2147 C  C     . GLU   B 1 79  ? 35.028  -9.936  52.606 1.00 22.50 ? 105 GLU   B C     1 
ATOM   2148 O  O     . GLU   B 1 79  ? 35.481  -8.790  52.490 1.00 22.50 ? 105 GLU   B O     1 
ATOM   2149 C  CB    . GLU   B 1 79  ? 36.704  -11.721 53.035 1.00 27.06 ? 105 GLU   B CB    1 
ATOM   2150 C  CG    . GLU   B 1 79  ? 37.947  -10.912 52.717 1.00 37.12 ? 105 GLU   B CG    1 
ATOM   2151 C  CD    . GLU   B 1 79  ? 38.752  -10.532 53.946 1.00 49.32 ? 105 GLU   B CD    1 
ATOM   2152 O  OE1   . GLU   B 1 79  ? 38.733  -11.305 54.935 1.00 51.84 ? 105 GLU   B OE1   1 
ATOM   2153 O  OE2   . GLU   B 1 79  ? 39.406  -9.461  53.919 1.00 53.15 ? 105 GLU   B OE2   1 
ATOM   2154 N  N     . LYS   B 1 80  ? 34.081  -10.428 51.778 1.00 21.22 ? 106 LYS   B N     1 
ATOM   2155 C  CA    . LYS   B 1 80  ? 33.521  -9.600  50.706 1.00 21.05 ? 106 LYS   B CA    1 
ATOM   2156 C  C     . LYS   B 1 80  ? 32.433  -8.630  51.171 1.00 19.72 ? 106 LYS   B C     1 
ATOM   2157 O  O     . LYS   B 1 80  ? 31.998  -7.774  50.399 1.00 20.26 ? 106 LYS   B O     1 
ATOM   2158 C  CB    . LYS   B 1 80  ? 33.014  -10.470 49.538 1.00 23.76 ? 106 LYS   B CB    1 
ATOM   2159 C  CG    . LYS   B 1 80  ? 34.127  -11.219 48.814 1.00 30.14 ? 106 LYS   B CG    1 
ATOM   2160 C  CD    . LYS   B 1 80  ? 34.924  -10.300 47.898 1.00 36.93 ? 106 LYS   B CD    1 
ATOM   2161 C  CE    . LYS   B 1 80  ? 36.096  -10.998 47.236 1.00 42.22 ? 106 LYS   B CE    1 
ATOM   2162 N  NZ    . LYS   B 1 80  ? 35.664  -11.952 46.168 1.00 45.14 ? 106 LYS   B NZ    1 
ATOM   2163 N  N     . ASN   B 1 81  ? 31.963  -8.774  52.400 1.00 18.32 ? 107 ASN   B N     1 
ATOM   2164 C  CA    . ASN   B 1 81  ? 30.943  -7.889  52.956 1.00 17.29 ? 107 ASN   B CA    1 
ATOM   2165 C  C     . ASN   B 1 81  ? 31.488  -7.021  54.087 1.00 17.82 ? 107 ASN   B C     1 
ATOM   2166 O  O     . ASN   B 1 81  ? 30.886  -6.004  54.385 1.00 19.27 ? 107 ASN   B O     1 
ATOM   2167 C  CB    . ASN   B 1 81  ? 29.805  -8.714  53.536 1.00 16.56 ? 107 ASN   B CB    1 
ATOM   2168 C  CG    . ASN   B 1 81  ? 29.075  -9.550  52.528 1.00 17.81 ? 107 ASN   B CG    1 
ATOM   2169 O  OD1   . ASN   B 1 81  ? 28.843  -9.127  51.391 1.00 17.49 ? 107 ASN   B OD1   1 
ATOM   2170 N  ND2   . ASN   B 1 81  ? 28.691  -10.763 52.933 1.00 16.91 ? 107 ASN   B ND2   1 
ATOM   2171 N  N     . LYS   B 1 82  ? 32.582  -7.417  54.739 1.00 17.47 ? 108 LYS   B N     1 
ATOM   2172 C  CA    . LYS   B 1 82  ? 33.106  -6.742  55.925 1.00 18.74 ? 108 LYS   B CA    1 
ATOM   2173 C  C     . LYS   B 1 82  ? 33.351  -5.230  55.743 1.00 19.16 ? 108 LYS   B C     1 
ATOM   2174 O  O     . LYS   B 1 82  ? 33.064  -4.469  56.665 1.00 20.11 ? 108 LYS   B O     1 
ATOM   2175 C  CB    . LYS   B 1 82  ? 34.346  -7.488  56.479 1.00 21.06 ? 108 LYS   B CB    1 
ATOM   2176 C  CG    . LYS   B 1 82  ? 35.714  -6.889  56.218 1.00 27.14 ? 108 LYS   B CG    1 
ATOM   2177 C  CD    . LYS   B 1 82  ? 36.809  -7.659  56.929 1.00 32.71 ? 108 LYS   B CD    1 
ATOM   2178 C  CE    . LYS   B 1 82  ? 36.676  -7.546  58.435 1.00 38.20 ? 108 LYS   B CE    1 
ATOM   2179 N  NZ    . LYS   B 1 82  ? 37.932  -7.937  59.135 1.00 40.96 ? 108 LYS   B NZ    1 
ATOM   2180 N  N     . ARG   B 1 83  ? 33.816  -4.787  54.570 1.00 18.57 ? 109 ARG   B N     1 
ATOM   2181 C  CA    . ARG   B 1 83  ? 34.027  -3.351  54.336 1.00 18.59 ? 109 ARG   B CA    1 
ATOM   2182 C  C     . ARG   B 1 83  ? 32.858  -2.699  53.568 1.00 17.08 ? 109 ARG   B C     1 
ATOM   2183 O  O     . ARG   B 1 83  ? 32.941  -1.527  53.204 1.00 16.81 ? 109 ARG   B O     1 
ATOM   2184 C  CB    . ARG   B 1 83  ? 35.345  -3.138  53.576 1.00 21.81 ? 109 ARG   B CB    1 
ATOM   2185 C  CG    . ARG   B 1 83  ? 36.589  -3.516  54.374 1.00 28.17 ? 109 ARG   B CG    1 
ATOM   2186 C  CD    . ARG   B 1 83  ? 37.883  -3.471  53.549 1.00 34.85 ? 109 ARG   B CD    1 
ATOM   2187 N  NE    . ARG   B 1 83  ? 38.011  -2.230  52.775 1.00 41.29 ? 109 ARG   B NE    1 
ATOM   2188 C  CZ    . ARG   B 1 83  ? 38.534  -1.100  53.239 1.00 46.02 ? 109 ARG   B CZ    1 
ATOM   2189 N  NH1   . ARG   B 1 83  ? 39.024  -1.042  54.472 1.00 46.19 ? 109 ARG   B NH1   1 
ATOM   2190 N  NH2   . ARG   B 1 83  ? 38.585  -0.021  52.467 1.00 46.72 ? 109 ARG   B NH2   1 
ATOM   2191 N  N     . GLY   B 1 84  ? 31.770  -3.443  53.364 1.00 16.00 ? 110 GLY   B N     1 
ATOM   2192 C  CA    . GLY   B 1 84  ? 30.641  -2.981  52.581 1.00 15.35 ? 110 GLY   B CA    1 
ATOM   2193 C  C     . GLY   B 1 84  ? 29.476  -2.434  53.365 1.00 15.13 ? 110 GLY   B C     1 
ATOM   2194 O  O     . GLY   B 1 84  ? 29.611  -1.953  54.494 1.00 15.00 ? 110 GLY   B O     1 
ATOM   2195 N  N     . GLY   B 1 85  ? 28.335  -2.479  52.730 1.00 14.84 ? 111 GLY   B N     1 
ATOM   2196 C  CA    . GLY   B 1 85  ? 27.106  -1.936  53.279 1.00 15.04 ? 111 GLY   B CA    1 
ATOM   2197 C  C     . GLY   B 1 85  ? 25.927  -2.311  52.405 1.00 15.13 ? 111 GLY   B C     1 
ATOM   2198 O  O     . GLY   B 1 85  ? 26.060  -3.141  51.500 1.00 15.48 ? 111 GLY   B O     1 
ATOM   2199 N  N     . ARG   B 1 86  ? 24.786  -1.676  52.639 1.00 14.28 ? 112 ARG   B N     1 
ATOM   2200 C  CA    . ARG   B 1 86  ? 23.583  -2.027  51.914 1.00 14.86 ? 112 ARG   B CA    1 
ATOM   2201 C  C     . ARG   B 1 86  ? 22.669  -0.866  51.630 1.00 14.96 ? 112 ARG   B C     1 
ATOM   2202 O  O     . ARG   B 1 86  ? 22.552  0.055   52.432 1.00 14.76 ? 112 ARG   B O     1 
ATOM   2203 C  CB    . ARG   B 1 86  ? 22.795  -3.083  52.712 1.00 16.07 ? 112 ARG   B CB    1 
ATOM   2204 C  CG    . ARG   B 1 86  ? 22.420  -2.562  54.091 1.00 21.09 ? 112 ARG   B CG    1 
ATOM   2205 C  CD    . ARG   B 1 86  ? 21.476  -3.423  54.862 1.00 26.11 ? 112 ARG   B CD    1 
ATOM   2206 N  NE    . ARG   B 1 86  ? 21.251  -2.840  56.185 1.00 30.65 ? 112 ARG   B NE    1 
ATOM   2207 C  CZ    . ARG   B 1 86  ? 20.507  -3.396  57.135 1.00 34.83 ? 112 ARG   B CZ    1 
ATOM   2208 N  NH1   . ARG   B 1 86  ? 19.894  -4.550  56.917 1.00 35.12 ? 112 ARG   B NH1   1 
ATOM   2209 N  NH2   . ARG   B 1 86  ? 20.369  -2.798  58.313 1.00 35.84 ? 112 ARG   B NH2   1 
ATOM   2210 N  N     . TRP   B 1 87  ? 21.984  -0.941  50.488 1.00 15.06 ? 113 TRP   B N     1 
ATOM   2211 C  CA    . TRP   B 1 87  ? 20.943  0.001   50.134 1.00 15.53 ? 113 TRP   B CA    1 
ATOM   2212 C  C     . TRP   B 1 87  ? 19.708  -0.627  50.747 1.00 17.31 ? 113 TRP   B C     1 
ATOM   2213 O  O     . TRP   B 1 87  ? 19.433  -1.778  50.457 1.00 17.50 ? 113 TRP   B O     1 
ATOM   2214 C  CB    . TRP   B 1 87  ? 20.775  0.094   48.593 1.00 14.61 ? 113 TRP   B CB    1 
ATOM   2215 C  CG    . TRP   B 1 87  ? 21.737  1.058   47.961 1.00 14.30 ? 113 TRP   B CG    1 
ATOM   2216 C  CD1   . TRP   B 1 87  ? 22.845  0.745   47.229 1.00 14.94 ? 113 TRP   B CD1   1 
ATOM   2217 C  CD2   . TRP   B 1 87  ? 21.777  2.480   48.165 1.00 13.90 ? 113 TRP   B CD2   1 
ATOM   2218 N  NE1   . TRP   B 1 87  ? 23.542  1.893   46.913 1.00 14.94 ? 113 TRP   B NE1   1 
ATOM   2219 C  CE2   . TRP   B 1 87  ? 22.910  2.971   47.486 1.00 14.83 ? 113 TRP   B CE2   1 
ATOM   2220 C  CE3   . TRP   B 1 87  ? 20.930  3.391   48.811 1.00 14.33 ? 113 TRP   B CE3   1 
ATOM   2221 C  CZ2   . TRP   B 1 87  ? 23.208  4.336   47.417 1.00 15.74 ? 113 TRP   B CZ2   1 
ATOM   2222 C  CZ3   . TRP   B 1 87  ? 21.219  4.738   48.736 1.00 15.56 ? 113 TRP   B CZ3   1 
ATOM   2223 C  CH2   . TRP   B 1 87  ? 22.346  5.200   48.042 1.00 16.26 ? 113 TRP   B CH2   1 
ATOM   2224 N  N     . LEU   B 1 88  ? 18.960  0.097   51.578 1.00 18.97 ? 114 LEU   B N     1 
ATOM   2225 C  CA    . LEU   B 1 88  ? 17.830  -0.504  52.273 1.00 20.87 ? 114 LEU   B CA    1 
ATOM   2226 C  C     . LEU   B 1 88  ? 16.500  0.109   51.867 1.00 22.80 ? 114 LEU   B C     1 
ATOM   2227 O  O     . LEU   B 1 88  ? 16.380  1.326   51.697 1.00 22.62 ? 114 LEU   B O     1 
ATOM   2228 C  CB    . LEU   B 1 88  ? 18.076  -0.407  53.798 1.00 21.97 ? 114 LEU   B CB    1 
ATOM   2229 C  CG    . LEU   B 1 88  ? 16.941  -0.819  54.736 1.00 24.68 ? 114 LEU   B CG    1 
ATOM   2230 C  CD1   . LEU   B 1 88  ? 16.842  -2.343  54.845 1.00 24.82 ? 114 LEU   B CD1   1 
ATOM   2231 C  CD2   . LEU   B 1 88  ? 17.132  -0.196  56.119 1.00 26.27 ? 114 LEU   B CD2   1 
ATOM   2232 N  N     . ILE   B 1 89  ? 15.521  -0.750  51.645 1.00 23.89 ? 115 ILE   B N     1 
ATOM   2233 C  CA    . ILE   B 1 89  ? 14.170  -0.345  51.318 1.00 26.51 ? 115 ILE   B CA    1 
ATOM   2234 C  C     . ILE   B 1 89  ? 13.262  -0.869  52.428 1.00 28.02 ? 115 ILE   B C     1 
ATOM   2235 O  O     . ILE   B 1 89  ? 13.327  -2.045  52.787 1.00 27.54 ? 115 ILE   B O     1 
ATOM   2236 C  CB    . ILE   B 1 89  ? 13.738  -0.817  49.909 1.00 28.35 ? 115 ILE   B CB    1 
ATOM   2237 C  CG1   . ILE   B 1 89  ? 14.657  -0.181  48.848 1.00 30.51 ? 115 ILE   B CG1   1 
ATOM   2238 C  CG2   . ILE   B 1 89  ? 12.246  -0.492  49.643 1.00 29.02 ? 115 ILE   B CG2   1 
ATOM   2239 C  CD1   . ILE   B 1 89  ? 14.418  -0.615  47.490 1.00 33.20 ? 115 ILE   B CD1   1 
ATOM   2240 N  N     . THR   B 1 90  ? 12.465  0.015   53.010 1.00 29.28 ? 116 THR   B N     1 
ATOM   2241 C  CA    . THR   B 1 90  ? 11.535  -0.370  54.061 1.00 31.74 ? 116 THR   B CA    1 
ATOM   2242 C  C     . THR   B 1 90  ? 10.124  -0.268  53.504 1.00 34.08 ? 116 THR   B C     1 
ATOM   2243 O  O     . THR   B 1 90  ? 9.756   0.768   52.956 1.00 33.96 ? 116 THR   B O     1 
ATOM   2244 C  CB    . THR   B 1 90  ? 11.717  0.516   55.306 1.00 33.47 ? 116 THR   B CB    1 
ATOM   2245 O  OG1   . THR   B 1 90  ? 13.065  0.403   55.770 1.00 34.57 ? 116 THR   B OG1   1 
ATOM   2246 C  CG2   . THR   B 1 90  ? 10.758  0.137   56.434 1.00 34.03 ? 116 THR   B CG2   1 
ATOM   2247 N  N     . LEU   B 1 91  ? 9.334   -1.339  53.645 1.00 36.19 ? 117 LEU   B N     1 
ATOM   2248 C  CA    . LEU   B 1 91  ? 7.939   -1.385  53.193 1.00 38.84 ? 117 LEU   B CA    1 
ATOM   2249 C  C     . LEU   B 1 91  ? 6.973   -1.091  54.366 1.00 42.18 ? 117 LEU   B C     1 
ATOM   2250 O  O     . LEU   B 1 91  ? 7.380   -1.184  55.523 1.00 42.55 ? 117 LEU   B O     1 
ATOM   2251 C  CB    . LEU   B 1 91  ? 7.629   -2.784  52.635 1.00 38.67 ? 117 LEU   B CB    1 
ATOM   2252 C  CG    . LEU   B 1 91  ? 8.195   -3.124  51.270 1.00 40.24 ? 117 LEU   B CG    1 
ATOM   2253 C  CD1   . LEU   B 1 91  ? 9.614   -3.679  51.379 1.00 41.00 ? 117 LEU   B CD1   1 
ATOM   2254 C  CD2   . LEU   B 1 91  ? 7.319   -4.146  50.579 1.00 40.62 ? 117 LEU   B CD2   1 
ATOM   2255 N  N     . ASN   B 1 92  ? 5.687   -0.783  54.081 1.00 44.61 ? 118 ASN   B N     1 
ATOM   2256 C  CA    . ASN   B 1 92  ? 4.712   -0.572  55.163 1.00 47.21 ? 118 ASN   B CA    1 
ATOM   2257 C  C     . ASN   B 1 92  ? 3.930   -1.863  55.479 1.00 49.25 ? 118 ASN   B C     1 
ATOM   2258 O  O     . ASN   B 1 92  ? 3.802   -2.726  54.616 1.00 49.52 ? 118 ASN   B O     1 
ATOM   2259 C  CB    . ASN   B 1 92  ? 3.777   0.612   54.885 1.00 49.04 ? 118 ASN   B CB    1 
ATOM   2260 C  CG    . ASN   B 1 92  ? 3.037   0.551   53.570 1.00 53.71 ? 118 ASN   B CG    1 
ATOM   2261 O  OD1   . ASN   B 1 92  ? 3.017   -0.476  52.879 1.00 55.49 ? 118 ASN   B OD1   1 
ATOM   2262 N  ND2   . ASN   B 1 92  ? 2.408   1.659   53.191 1.00 54.38 ? 118 ASN   B ND2   1 
ATOM   2263 N  N     . LYS   B 1 93  ? 3.424   -2.005  56.709 1.00 50.45 ? 119 LYS   B N     1 
ATOM   2264 C  CA    . LYS   B 1 93  ? 2.659   -3.195  57.097 1.00 51.86 ? 119 LYS   B CA    1 
ATOM   2265 C  C     . LYS   B 1 93  ? 1.259   -3.187  56.480 1.00 52.89 ? 119 LYS   B C     1 
ATOM   2266 O  O     . LYS   B 1 93  ? 1.048   -3.790  55.424 1.00 53.51 ? 119 LYS   B O     1 
ATOM   2267 C  CB    . LYS   B 1 93  ? 2.557   -3.307  58.626 1.00 53.77 ? 119 LYS   B CB    1 
ATOM   2268 N  N     . ASP   B 1 99  ? 3.239   -5.680  46.868 1.00 33.76 ? 125 ASP   B N     1 
ATOM   2269 C  CA    . ASP   B 1 99  ? 4.486   -4.932  46.744 1.00 33.33 ? 125 ASP   B CA    1 
ATOM   2270 C  C     . ASP   B 1 99  ? 5.736   -5.748  47.072 1.00 31.29 ? 125 ASP   B C     1 
ATOM   2271 O  O     . ASP   B 1 99  ? 6.713   -5.667  46.330 1.00 30.75 ? 125 ASP   B O     1 
ATOM   2272 C  CB    . ASP   B 1 99  ? 4.420   -3.655  47.577 1.00 36.25 ? 125 ASP   B CB    1 
ATOM   2273 C  CG    . ASP   B 1 99  ? 3.313   -2.764  47.079 1.00 44.24 ? 125 ASP   B CG    1 
ATOM   2274 O  OD1   . ASP   B 1 99  ? 3.149   -2.656  45.835 1.00 45.40 ? 125 ASP   B OD1   1 
ATOM   2275 O  OD2   . ASP   B 1 99  ? 2.581   -2.200  47.923 1.00 48.09 ? 125 ASP   B OD2   1 
ATOM   2276 N  N     . LEU   B 1 100 ? 5.723   -6.515  48.181 1.00 29.44 ? 126 LEU   B N     1 
ATOM   2277 C  CA    . LEU   B 1 100 ? 6.881   -7.324  48.564 1.00 28.50 ? 126 LEU   B CA    1 
ATOM   2278 C  C     . LEU   B 1 100 ? 7.300   -8.305  47.462 1.00 26.64 ? 126 LEU   B C     1 
ATOM   2279 O  O     . LEU   B 1 100 ? 8.481   -8.381  47.156 1.00 26.41 ? 126 LEU   B O     1 
ATOM   2280 C  CB    . LEU   B 1 100 ? 6.655   -8.082  49.885 1.00 29.06 ? 126 LEU   B CB    1 
ATOM   2281 C  CG    . LEU   B 1 100 ? 7.850   -8.946  50.348 1.00 31.21 ? 126 LEU   B CG    1 
ATOM   2282 C  CD1   . LEU   B 1 100 ? 9.023   -8.076  50.816 1.00 31.70 ? 126 LEU   B CD1   1 
ATOM   2283 C  CD2   . LEU   B 1 100 ? 7.446   -9.911  51.429 1.00 32.22 ? 126 LEU   B CD2   1 
ATOM   2284 N  N     . ASP   B 1 101 ? 6.342   -9.038  46.871 1.00 25.13 ? 127 ASP   B N     1 
ATOM   2285 C  CA    . ASP   B 1 101 ? 6.641   -10.005 45.806 1.00 24.28 ? 127 ASP   B CA    1 
ATOM   2286 C  C     . ASP   B 1 101 ? 7.282   -9.334  44.586 1.00 22.13 ? 127 ASP   B C     1 
ATOM   2287 O  O     . ASP   B 1 101 ? 8.296   -9.825  44.072 1.00 22.37 ? 127 ASP   B O     1 
ATOM   2288 C  CB    . ASP   B 1 101 ? 5.381   -10.773 45.364 1.00 26.61 ? 127 ASP   B CB    1 
ATOM   2289 C  CG    . ASP   B 1 101 ? 4.866   -11.752 46.396 1.00 33.72 ? 127 ASP   B CG    1 
ATOM   2290 O  OD1   . ASP   B 1 101 ? 5.695   -12.320 47.140 1.00 34.47 ? 127 ASP   B OD1   1 
ATOM   2291 O  OD2   . ASP   B 1 101 ? 3.631   -11.947 46.461 1.00 36.97 ? 127 ASP   B OD2   1 
ATOM   2292 N  N     . ARG   B 1 102 ? 6.686   -8.234  44.116 1.00 19.78 ? 128 ARG   B N     1 
ATOM   2293 C  CA    . ARG   B 1 102 ? 7.200   -7.485  42.979 1.00 19.46 ? 128 ARG   B CA    1 
ATOM   2294 C  C     . ARG   B 1 102 ? 8.626   -6.969  43.265 1.00 17.82 ? 128 ARG   B C     1 
ATOM   2295 O  O     . ARG   B 1 102 ? 9.551   -7.285  42.507 1.00 17.28 ? 128 ARG   B O     1 
ATOM   2296 C  CB    . ARG   B 1 102 ? 6.244   -6.321  42.606 1.00 21.30 ? 128 ARG   B CB    1 
ATOM   2297 C  CG    . ARG   B 1 102 ? 6.786   -5.429  41.477 1.00 24.63 ? 128 ARG   B CG    1 
ATOM   2298 C  CD    . ARG   B 1 102 ? 5.773   -4.429  40.928 1.00 28.49 ? 128 ARG   B CD    1 
ATOM   2299 N  NE    . ARG   B 1 102 ? 5.130   -3.641  41.984 1.00 32.66 ? 128 ARG   B NE    1 
ATOM   2300 C  CZ    . ARG   B 1 102 ? 5.614   -2.505  42.472 1.00 36.97 ? 128 ARG   B CZ    1 
ATOM   2301 N  NH1   . ARG   B 1 102 ? 6.755   -2.004  42.005 1.00 38.97 ? 128 ARG   B NH1   1 
ATOM   2302 N  NH2   . ARG   B 1 102 ? 4.978   -1.872  43.447 1.00 36.44 ? 128 ARG   B NH2   1 
ATOM   2303 N  N     . PHE   B 1 103 ? 8.817   -6.276  44.398 1.00 16.78 ? 129 PHE   B N     1 
ATOM   2304 C  CA    . PHE   B 1 103 ? 10.119  -5.716  44.756 1.00 17.64 ? 129 PHE   B CA    1 
ATOM   2305 C  C     . PHE   B 1 103 ? 11.202  -6.776  44.900 1.00 16.86 ? 129 PHE   B C     1 
ATOM   2306 O  O     . PHE   B 1 103 ? 12.349  -6.523  44.521 1.00 16.11 ? 129 PHE   B O     1 
ATOM   2307 C  CB    . PHE   B 1 103 ? 10.060  -4.848  46.034 1.00 18.64 ? 129 PHE   B CB    1 
ATOM   2308 C  CG    . PHE   B 1 103 ? 9.294   -3.542  45.972 1.00 20.63 ? 129 PHE   B CG    1 
ATOM   2309 C  CD1   . PHE   B 1 103 ? 8.937   -2.983  44.761 1.00 22.02 ? 129 PHE   B CD1   1 
ATOM   2310 C  CD2   . PHE   B 1 103 ? 8.973   -2.854  47.127 1.00 22.59 ? 129 PHE   B CD2   1 
ATOM   2311 C  CE1   . PHE   B 1 103 ? 8.253   -1.770  44.711 1.00 23.06 ? 129 PHE   B CE1   1 
ATOM   2312 C  CE2   . PHE   B 1 103 ? 8.265   -1.652  47.071 1.00 23.48 ? 129 PHE   B CE2   1 
ATOM   2313 C  CZ    . PHE   B 1 103 ? 7.906   -1.124  45.864 1.00 22.92 ? 129 PHE   B CZ    1 
ATOM   2314 N  N     . TRP   B 1 104 ? 10.855  -7.944  45.481 1.00 15.89 ? 130 TRP   B N     1 
ATOM   2315 C  CA    . TRP   B 1 104 ? 11.829  -9.020  45.632 1.00 15.70 ? 130 TRP   B CA    1 
ATOM   2316 C  C     . TRP   B 1 104 ? 12.227  -9.634  44.293 1.00 15.19 ? 130 TRP   B C     1 
ATOM   2317 O  O     . TRP   B 1 104 ? 13.425  -9.798  44.023 1.00 15.69 ? 130 TRP   B O     1 
ATOM   2318 C  CB    . TRP   B 1 104 ? 11.345  -10.083 46.633 1.00 16.11 ? 130 TRP   B CB    1 
ATOM   2319 C  CG    . TRP   B 1 104 ? 12.308  -11.217 46.887 1.00 17.21 ? 130 TRP   B CG    1 
ATOM   2320 C  CD1   . TRP   B 1 104 ? 12.048  -12.549 46.762 1.00 17.95 ? 130 TRP   B CD1   1 
ATOM   2321 C  CD2   . TRP   B 1 104 ? 13.686  -11.113 47.310 1.00 17.35 ? 130 TRP   B CD2   1 
ATOM   2322 N  NE1   . TRP   B 1 104 ? 13.168  -13.281 47.085 1.00 18.50 ? 130 TRP   B NE1   1 
ATOM   2323 C  CE2   . TRP   B 1 104 ? 14.181  -12.423 47.444 1.00 18.25 ? 130 TRP   B CE2   1 
ATOM   2324 C  CE3   . TRP   B 1 104 ? 14.532  -10.039 47.624 1.00 18.24 ? 130 TRP   B CE3   1 
ATOM   2325 C  CZ2   . TRP   B 1 104 ? 15.489  -12.691 47.867 1.00 19.29 ? 130 TRP   B CZ2   1 
ATOM   2326 C  CZ3   . TRP   B 1 104 ? 15.827  -10.307 48.047 1.00 19.23 ? 130 TRP   B CZ3   1 
ATOM   2327 C  CH2   . TRP   B 1 104 ? 16.306  -11.618 48.122 1.00 19.37 ? 130 TRP   B CH2   1 
ATOM   2328 N  N     . LEU   B 1 105 ? 11.254  -9.936  43.433 1.00 14.16 ? 131 LEU   B N     1 
ATOM   2329 C  CA    . LEU   B 1 105 ? 11.578  -10.444 42.089 1.00 14.25 ? 131 LEU   B CA    1 
ATOM   2330 C  C     . LEU   B 1 105 ? 12.401  -9.415  41.286 1.00 13.79 ? 131 LEU   B C     1 
ATOM   2331 O  O     . LEU   B 1 105 ? 13.377  -9.775  40.643 1.00 13.54 ? 131 LEU   B O     1 
ATOM   2332 C  CB    . LEU   B 1 105 ? 10.323  -10.865 41.302 1.00 13.93 ? 131 LEU   B CB    1 
ATOM   2333 C  CG    . LEU   B 1 105 ? 10.599  -11.459 39.882 1.00 14.58 ? 131 LEU   B CG    1 
ATOM   2334 C  CD1   . LEU   B 1 105 ? 11.620  -12.608 39.927 1.00 13.98 ? 131 LEU   B CD1   1 
ATOM   2335 C  CD2   . LEU   B 1 105 ? 9.319   -11.977 39.274 1.00 14.77 ? 131 LEU   B CD2   1 
ATOM   2336 N  N     . GLU   B 1 106 ? 12.041  -8.138  41.370 1.00 13.18 ? 132 GLU   B N     1 
ATOM   2337 C  CA    . GLU   B 1 106 ? 12.769  -7.081  40.674 1.00 12.65 ? 132 GLU   B CA    1 
ATOM   2338 C  C     . GLU   B 1 106 ? 14.223  -6.973  41.180 1.00 12.75 ? 132 GLU   B C     1 
ATOM   2339 O  O     . GLU   B 1 106 ? 15.147  -6.718  40.402 1.00 13.41 ? 132 GLU   B O     1 
ATOM   2340 C  CB    . GLU   B 1 106 ? 12.002  -5.752  40.821 1.00 13.14 ? 132 GLU   B CB    1 
ATOM   2341 C  CG    . GLU   B 1 106 ? 10.756  -5.770  39.951 1.00 14.96 ? 132 GLU   B CG    1 
ATOM   2342 C  CD    . GLU   B 1 106 ? 9.943   -4.493  39.948 1.00 18.17 ? 132 GLU   B CD    1 
ATOM   2343 O  OE1   . GLU   B 1 106 ? 10.205  -3.622  40.803 1.00 17.87 ? 132 GLU   B OE1   1 
ATOM   2344 O  OE2   . GLU   B 1 106 ? 9.046   -4.358  39.087 1.00 20.28 ? 132 GLU   B OE2   1 
ATOM   2345 N  N     . THR   B 1 107 ? 14.418  -7.169  42.480 1.00 11.55 ? 133 THR   B N     1 
ATOM   2346 C  CA    . THR   B 1 107 ? 15.735  -7.165  43.077 1.00 11.65 ? 133 THR   B CA    1 
ATOM   2347 C  C     . THR   B 1 107 ? 16.540  -8.355  42.569 1.00 11.84 ? 133 THR   B C     1 
ATOM   2348 O  O     . THR   B 1 107 ? 17.696  -8.177  42.166 1.00 11.46 ? 133 THR   B O     1 
ATOM   2349 C  CB    . THR   B 1 107 ? 15.620  -7.228  44.606 1.00 13.00 ? 133 THR   B CB    1 
ATOM   2350 O  OG1   . THR   B 1 107 ? 14.802  -6.151  45.027 1.00 13.37 ? 133 THR   B OG1   1 
ATOM   2351 C  CG2   . THR   B 1 107 ? 16.996  -7.164  45.293 1.00 13.76 ? 133 THR   B CG2   1 
ATOM   2352 N  N     . LEU   B 1 108 ? 15.950  -9.578  42.589 1.00 11.41 ? 134 LEU   B N     1 
ATOM   2353 C  CA    . LEU   B 1 108 ? 16.635  -10.795 42.118 1.00 11.58 ? 134 LEU   B CA    1 
ATOM   2354 C  C     . LEU   B 1 108 ? 17.067  -10.637 40.664 1.00 11.59 ? 134 LEU   B C     1 
ATOM   2355 O  O     . LEU   B 1 108 ? 18.175  -11.069 40.305 1.00 12.33 ? 134 LEU   B O     1 
ATOM   2356 C  CB    . LEU   B 1 108 ? 15.711  -12.033 42.238 1.00 11.54 ? 134 LEU   B CB    1 
ATOM   2357 C  CG    . LEU   B 1 108 ? 15.313  -12.448 43.649 1.00 13.34 ? 134 LEU   B CG    1 
ATOM   2358 C  CD1   . LEU   B 1 108 ? 14.332  -13.608 43.608 1.00 14.04 ? 134 LEU   B CD1   1 
ATOM   2359 C  CD2   . LEU   B 1 108 ? 16.549  -12.812 44.477 1.00 13.90 ? 134 LEU   B CD2   1 
ATOM   2360 N  N     . LEU   B 1 109 ? 16.194  -10.055 39.824 1.00 10.88 ? 135 LEU   B N     1 
ATOM   2361 C  CA    . LEU   B 1 109 ? 16.493  -9.801  38.402 1.00 12.46 ? 135 LEU   B CA    1 
ATOM   2362 C  C     . LEU   B 1 109 ? 17.645  -8.788  38.221 1.00 13.28 ? 135 LEU   B C     1 
ATOM   2363 O  O     . LEU   B 1 109 ? 18.448  -8.978  37.327 1.00 13.95 ? 135 LEU   B O     1 
ATOM   2364 C  CB    . LEU   B 1 109 ? 15.229  -9.352  37.638 1.00 13.26 ? 135 LEU   B CB    1 
ATOM   2365 C  CG    . LEU   B 1 109 ? 14.132  -10.436 37.582 1.00 15.07 ? 135 LEU   B CG    1 
ATOM   2366 C  CD1   . LEU   B 1 109 ? 12.776  -9.870  37.101 1.00 14.54 ? 135 LEU   B CD1   1 
ATOM   2367 C  CD2   . LEU   B 1 109 ? 14.604  -11.665 36.786 1.00 15.35 ? 135 LEU   B CD2   1 
ATOM   2368 N  N     . CYS   B 1 110 ? 17.769  -7.764  39.083 1.00 13.60 ? 136 CYS   B N     1 
ATOM   2369 C  CA    . CYS   B 1 110 ? 18.916  -6.811  39.041 1.00 14.98 ? 136 CYS   B CA    1 
ATOM   2370 C  C     . CYS   B 1 110 ? 20.216  -7.566  39.295 1.00 15.15 ? 136 CYS   B C     1 
ATOM   2371 O  O     . CYS   B 1 110 ? 21.250  -7.239  38.709 1.00 15.66 ? 136 CYS   B O     1 
ATOM   2372 C  CB    . CYS   B 1 110 ? 18.755  -5.707  40.084 1.00 16.73 ? 136 CYS   B CB    1 
ATOM   2373 S  SG    . CYS   B 1 110 ? 17.513  -4.461  39.671 1.00 20.80 ? 136 CYS   B SG    1 
ATOM   2374 N  N     . LEU   B 1 111 ? 20.174  -8.522  40.226 1.00 14.44 ? 137 LEU   B N     1 
ATOM   2375 C  CA    . LEU   B 1 111 ? 21.328  -9.302  40.593 1.00 14.73 ? 137 LEU   B CA    1 
ATOM   2376 C  C     . LEU   B 1 111 ? 21.691  -10.250 39.459 1.00 13.96 ? 137 LEU   B C     1 
ATOM   2377 O  O     . LEU   B 1 111 ? 22.757  -10.097 38.895 1.00 14.84 ? 137 LEU   B O     1 
ATOM   2378 C  CB    . LEU   B 1 111 ? 21.056  -10.093 41.908 1.00 14.92 ? 137 LEU   B CB    1 
ATOM   2379 C  CG    . LEU   B 1 111 ? 21.501  -9.496  43.255 1.00 16.98 ? 137 LEU   B CG    1 
ATOM   2380 C  CD1   . LEU   B 1 111 ? 21.155  -8.022  43.385 1.00 17.33 ? 137 LEU   B CD1   1 
ATOM   2381 C  CD2   . LEU   B 1 111 ? 20.918  -10.322 44.429 1.00 16.70 ? 137 LEU   B CD2   1 
ATOM   2382 N  N     . ILE   B 1 112 ? 20.826  -11.205 39.110 1.00 12.77 ? 138 ILE   B N     1 
ATOM   2383 C  CA    . ILE   B 1 112 ? 21.177  -12.216 38.109 1.00 13.29 ? 138 ILE   B CA    1 
ATOM   2384 C  C     . ILE   B 1 112 ? 21.349  -11.617 36.712 1.00 13.07 ? 138 ILE   B C     1 
ATOM   2385 O  O     . ILE   B 1 112 ? 22.150  -12.141 35.933 1.00 13.23 ? 138 ILE   B O     1 
ATOM   2386 C  CB    . ILE   B 1 112 ? 20.206  -13.441 38.112 1.00 13.92 ? 138 ILE   B CB    1 
ATOM   2387 C  CG1   . ILE   B 1 112 ? 18.862  -13.060 37.471 1.00 15.21 ? 138 ILE   B CG1   1 
ATOM   2388 C  CG2   . ILE   B 1 112 ? 20.048  -14.003 39.539 1.00 13.97 ? 138 ILE   B CG2   1 
ATOM   2389 C  CD1   . ILE   B 1 112 ? 18.053  -14.154 37.068 1.00 17.75 ? 138 ILE   B CD1   1 
ATOM   2390 N  N     . GLY   B 1 113 ? 20.668  -10.508 36.431 1.00 12.36 ? 139 GLY   B N     1 
ATOM   2391 C  CA    . GLY   B 1 113 ? 20.787  -9.830  35.145 1.00 12.87 ? 139 GLY   B CA    1 
ATOM   2392 C  C     . GLY   B 1 113 ? 21.930  -8.832  35.085 1.00 13.98 ? 139 GLY   B C     1 
ATOM   2393 O  O     . GLY   B 1 113 ? 22.145  -8.211  34.044 1.00 14.33 ? 139 GLY   B O     1 
ATOM   2394 N  N     . GLU   B 1 114 ? 22.686  -8.631  36.195 1.00 14.12 ? 140 GLU   B N     1 
ATOM   2395 C  CA    . GLU   B 1 114 ? 23.804  -7.667  36.235 1.00 14.81 ? 140 GLU   B CA    1 
ATOM   2396 C  C     . GLU   B 1 114 ? 23.338  -6.285  35.734 1.00 15.42 ? 140 GLU   B C     1 
ATOM   2397 O  O     . GLU   B 1 114 ? 23.959  -5.700  34.848 1.00 15.77 ? 140 GLU   B O     1 
ATOM   2398 C  CB    . GLU   B 1 114 ? 25.015  -8.182  35.427 1.00 18.79 ? 140 GLU   B CB    1 
ATOM   2399 C  CG    . GLU   B 1 114 ? 25.343  -9.664  35.615 1.00 24.53 ? 140 GLU   B CG    1 
ATOM   2400 C  CD    . GLU   B 1 114 ? 26.065  -9.984  36.911 1.00 33.71 ? 140 GLU   B CD    1 
ATOM   2401 O  OE1   . GLU   B 1 114 ? 26.757  -9.075  37.421 1.00 38.14 ? 140 GLU   B OE1   1 
ATOM   2402 O  OE2   . GLU   B 1 114 ? 25.971  -11.133 37.408 1.00 32.25 ? 140 GLU   B OE2   1 
ATOM   2403 N  N     . SER   B 1 115 ? 22.179  -5.811  36.255 1.00 15.79 ? 141 SER   B N     1 
ATOM   2404 C  CA    . SER   B 1 115 ? 21.536  -4.569  35.807 1.00 16.13 ? 141 SER   B CA    1 
ATOM   2405 C  C     . SER   B 1 115 ? 22.330  -3.286  36.062 1.00 15.64 ? 141 SER   B C     1 
ATOM   2406 O  O     . SER   B 1 115 ? 21.934  -2.240  35.562 1.00 16.41 ? 141 SER   B O     1 
ATOM   2407 C  CB    . SER   B 1 115 ? 20.158  -4.423  36.448 1.00 17.34 ? 141 SER   B CB    1 
ATOM   2408 O  OG    . SER   B 1 115 ? 19.337  -5.532  36.119 1.00 19.37 ? 141 SER   B OG    1 
ATOM   2409 N  N     . PHE   B 1 116 ? 23.371  -3.342  36.878 1.00 14.44 ? 142 PHE   B N     1 
ATOM   2410 C  CA    . PHE   B 1 116 ? 24.168  -2.143  37.183 1.00 15.40 ? 142 PHE   B CA    1 
ATOM   2411 C  C     . PHE   B 1 116 ? 25.448  -2.033  36.334 1.00 16.25 ? 142 PHE   B C     1 
ATOM   2412 O  O     . PHE   B 1 116 ? 26.397  -1.332  36.724 1.00 16.65 ? 142 PHE   B O     1 
ATOM   2413 C  CB    . PHE   B 1 116 ? 24.467  -2.072  38.697 1.00 15.09 ? 142 PHE   B CB    1 
ATOM   2414 C  CG    . PHE   B 1 116 ? 23.238  -2.329  39.550 1.00 15.07 ? 142 PHE   B CG    1 
ATOM   2415 C  CD1   . PHE   B 1 116 ? 22.190  -1.415  39.583 1.00 15.30 ? 142 PHE   B CD1   1 
ATOM   2416 C  CD2   . PHE   B 1 116 ? 23.130  -3.482  40.310 1.00 15.11 ? 142 PHE   B CD2   1 
ATOM   2417 C  CE1   . PHE   B 1 116 ? 21.056  -1.657  40.358 1.00 15.67 ? 142 PHE   B CE1   1 
ATOM   2418 C  CE2   . PHE   B 1 116 ? 21.996  -3.722  41.083 1.00 16.03 ? 142 PHE   B CE2   1 
ATOM   2419 C  CZ    . PHE   B 1 116 ? 20.964  -2.804  41.105 1.00 15.60 ? 142 PHE   B CZ    1 
ATOM   2420 N  N     . ASP   B 1 117 ? 25.469  -2.727  35.174 1.00 16.90 ? 143 ASP   B N     1 
ATOM   2421 C  CA    . ASP   B 1 117 ? 26.573  -2.759  34.211 1.00 17.77 ? 143 ASP   B CA    1 
ATOM   2422 C  C     . ASP   B 1 117 ? 27.887  -3.172  34.920 1.00 18.25 ? 143 ASP   B C     1 
ATOM   2423 O  O     . ASP   B 1 117 ? 27.835  -4.122  35.686 1.00 18.50 ? 143 ASP   B O     1 
ATOM   2424 C  CB    . ASP   B 1 117 ? 26.620  -1.438  33.417 1.00 19.87 ? 143 ASP   B CB    1 
ATOM   2425 C  CG    . ASP   B 1 117 ? 25.291  -1.182  32.718 1.00 25.66 ? 143 ASP   B CG    1 
ATOM   2426 O  OD1   . ASP   B 1 117 ? 24.740  -2.142  32.107 1.00 26.48 ? 143 ASP   B OD1   1 
ATOM   2427 O  OD2   . ASP   B 1 117 ? 24.781  -0.034  32.799 1.00 27.51 ? 143 ASP   B OD2   1 
ATOM   2428 N  N     . ASP   B 1 118 ? 29.039  -2.502  34.702 1.00 17.67 ? 144 ASP   B N     1 
ATOM   2429 C  CA    . ASP   B 1 118 ? 30.276  -2.869  35.366 1.00 18.06 ? 144 ASP   B CA    1 
ATOM   2430 C  C     . ASP   B 1 118 ? 30.217  -2.677  36.885 1.00 17.98 ? 144 ASP   B C     1 
ATOM   2431 O  O     . ASP   B 1 118 ? 30.959  -3.347  37.590 1.00 18.25 ? 144 ASP   B O     1 
ATOM   2432 C  CB    . ASP   B 1 118 ? 31.477  -2.153  34.735 1.00 21.60 ? 144 ASP   B CB    1 
ATOM   2433 C  CG    . ASP   B 1 118 ? 31.786  -2.639  33.318 1.00 30.02 ? 144 ASP   B CG    1 
ATOM   2434 O  OD1   . ASP   B 1 118 ? 31.354  -3.752  32.964 1.00 31.42 ? 144 ASP   B OD1   1 
ATOM   2435 O  OD2   . ASP   B 1 118 ? 32.453  -1.890  32.562 1.00 33.58 ? 144 ASP   B OD2   1 
ATOM   2436 N  N     . TYR   B 1 119 ? 29.309  -1.822  37.403 1.00 17.32 ? 145 TYR   B N     1 
ATOM   2437 C  CA    . TYR   B 1 119 ? 29.143  -1.661  38.863 1.00 17.40 ? 145 TYR   B CA    1 
ATOM   2438 C  C     . TYR   B 1 119 ? 28.485  -2.885  39.521 1.00 16.22 ? 145 TYR   B C     1 
ATOM   2439 O  O     . TYR   B 1 119 ? 28.580  -3.044  40.731 1.00 15.25 ? 145 TYR   B O     1 
ATOM   2440 C  CB    . TYR   B 1 119 ? 28.330  -0.415  39.193 1.00 18.73 ? 145 TYR   B CB    1 
ATOM   2441 C  CG    . TYR   B 1 119 ? 28.981  0.859   38.703 1.00 21.81 ? 145 TYR   B CG    1 
ATOM   2442 C  CD1   . TYR   B 1 119 ? 30.267  1.204   39.098 1.00 23.33 ? 145 TYR   B CD1   1 
ATOM   2443 C  CD2   . TYR   B 1 119 ? 28.310  1.720   37.848 1.00 24.12 ? 145 TYR   B CD2   1 
ATOM   2444 C  CE1   . TYR   B 1 119 ? 30.833  2.418   38.728 1.00 25.08 ? 145 TYR   B CE1   1 
ATOM   2445 C  CE2   . TYR   B 1 119 ? 28.879  2.919   37.443 1.00 26.11 ? 145 TYR   B CE2   1 
ATOM   2446 C  CZ    . TYR   B 1 119 ? 30.143  3.262   37.883 1.00 27.01 ? 145 TYR   B CZ    1 
ATOM   2447 O  OH    . TYR   B 1 119 ? 30.692  4.444   37.464 1.00 30.57 ? 145 TYR   B OH    1 
ATOM   2448 N  N     . SER   B 1 120 ? 27.886  -3.785  38.722 1.00 15.79 ? 146 SER   B N     1 
ATOM   2449 C  CA    . SER   B 1 120 ? 27.357  -5.034  39.243 1.00 17.16 ? 146 SER   B CA    1 
ATOM   2450 C  C     . SER   B 1 120 ? 28.492  -5.912  39.852 1.00 18.06 ? 146 SER   B C     1 
ATOM   2451 O  O     . SER   B 1 120 ? 28.199  -6.754  40.689 1.00 18.28 ? 146 SER   B O     1 
ATOM   2452 C  CB    . SER   B 1 120 ? 26.652  -5.801  38.136 1.00 18.85 ? 146 SER   B CB    1 
ATOM   2453 O  OG    . SER   B 1 120 ? 25.367  -5.234  37.989 1.00 20.75 ? 146 SER   B OG    1 
ATOM   2454 N  N     . ASP   B 1 121 ? 29.787  -5.654  39.511 1.00 17.73 ? 147 ASP   B N     1 
ATOM   2455 C  CA    . ASP   B 1 121 ? 30.895  -6.392  40.128 1.00 18.17 ? 147 ASP   B CA    1 
ATOM   2456 C  C     . ASP   B 1 121 ? 30.972  -6.069  41.661 1.00 18.20 ? 147 ASP   B C     1 
ATOM   2457 O  O     . ASP   B 1 121 ? 31.412  -6.905  42.445 1.00 18.62 ? 147 ASP   B O     1 
ATOM   2458 C  CB    . ASP   B 1 121 ? 32.218  -6.023  39.427 1.00 21.51 ? 147 ASP   B CB    1 
ATOM   2459 C  CG    . ASP   B 1 121 ? 33.327  -7.029  39.663 1.00 30.75 ? 147 ASP   B CG    1 
ATOM   2460 O  OD1   . ASP   B 1 121 ? 33.021  -8.234  39.788 1.00 32.84 ? 147 ASP   B OD1   1 
ATOM   2461 O  OD2   . ASP   B 1 121 ? 34.492  -6.617  39.713 1.00 35.30 ? 147 ASP   B OD2   1 
ATOM   2462 N  N     . ASP   B 1 122 ? 30.478  -4.885  42.093 1.00 17.44 ? 148 ASP   B N     1 
ATOM   2463 C  CA    . ASP   B 1 122 ? 30.436  -4.490  43.509 1.00 16.85 ? 148 ASP   B CA    1 
ATOM   2464 C  C     . ASP   B 1 122 ? 29.298  -5.156  44.295 1.00 16.37 ? 148 ASP   B C     1 
ATOM   2465 O  O     . ASP   B 1 122 ? 29.328  -5.136  45.524 1.00 16.65 ? 148 ASP   B O     1 
ATOM   2466 C  CB    . ASP   B 1 122 ? 30.298  -2.973  43.642 1.00 19.12 ? 148 ASP   B CB    1 
ATOM   2467 C  CG    . ASP   B 1 122 ? 31.642  -2.290  43.828 1.00 25.71 ? 148 ASP   B CG    1 
ATOM   2468 O  OD1   . ASP   B 1 122 ? 32.566  -2.581  43.042 1.00 28.09 ? 148 ASP   B OD1   1 
ATOM   2469 O  OD2   . ASP   B 1 122 ? 31.787  -1.518  44.803 1.00 26.51 ? 148 ASP   B OD2   1 
ATOM   2470 N  N     . VAL   B 1 123 ? 28.270  -5.688  43.607 1.00 15.18 ? 149 VAL   B N     1 
ATOM   2471 C  CA    . VAL   B 1 123 ? 27.132  -6.314  44.279 1.00 14.60 ? 149 VAL   B CA    1 
ATOM   2472 C  C     . VAL   B 1 123 ? 27.507  -7.666  44.868 1.00 14.66 ? 149 VAL   B C     1 
ATOM   2473 O  O     . VAL   B 1 123 ? 28.095  -8.494  44.176 1.00 15.60 ? 149 VAL   B O     1 
ATOM   2474 C  CB    . VAL   B 1 123 ? 25.913  -6.439  43.328 1.00 15.14 ? 149 VAL   B CB    1 
ATOM   2475 C  CG1   . VAL   B 1 123 ? 24.771  -7.234  43.984 1.00 15.31 ? 149 VAL   B CG1   1 
ATOM   2476 C  CG2   . VAL   B 1 123 ? 25.430  -5.062  42.877 1.00 15.10 ? 149 VAL   B CG2   1 
ATOM   2477 N  N     . CYS   B 1 124 ? 27.190  -7.886  46.143 1.00 13.60 ? 150 CYS   B N     1 
ATOM   2478 C  CA    . CYS   B 1 124 ? 27.433  -9.164  46.820 1.00 13.26 ? 150 CYS   B CA    1 
ATOM   2479 C  C     . CYS   B 1 124 ? 26.198  -10.039 46.829 1.00 12.54 ? 150 CYS   B C     1 
ATOM   2480 O  O     . CYS   B 1 124 ? 26.285  -11.256 46.647 1.00 13.17 ? 150 CYS   B O     1 
ATOM   2481 C  CB    . CYS   B 1 124 ? 27.930  -8.916  48.237 1.00 13.55 ? 150 CYS   B CB    1 
ATOM   2482 S  SG    . CYS   B 1 124 ? 29.519  -8.066  48.286 1.00 16.56 ? 150 CYS   B SG    1 
ATOM   2483 N  N     . GLY   B 1 125 ? 25.062  -9.424  47.100 1.00 11.06 ? 151 GLY   B N     1 
ATOM   2484 C  CA    . GLY   B 1 125 ? 23.804  -10.141 47.142 1.00 10.98 ? 151 GLY   B CA    1 
ATOM   2485 C  C     . GLY   B 1 125 ? 22.667  -9.262  47.613 1.00 11.92 ? 151 GLY   B C     1 
ATOM   2486 O  O     . GLY   B 1 125 ? 22.779  -8.034  47.627 1.00 11.40 ? 151 GLY   B O     1 
ATOM   2487 N  N     . ALA   B 1 126 ? 21.553  -9.887  47.976 1.00 12.06 ? 152 ALA   B N     1 
ATOM   2488 C  CA    . ALA   B 1 126 ? 20.385  -9.153  48.436 1.00 12.78 ? 152 ALA   B CA    1 
ATOM   2489 C  C     . ALA   B 1 126 ? 19.706  -9.936  49.549 1.00 12.79 ? 152 ALA   B C     1 
ATOM   2490 O  O     . ALA   B 1 126 ? 19.773  -11.151 49.557 1.00 12.48 ? 152 ALA   B O     1 
ATOM   2491 C  CB    . ALA   B 1 126 ? 19.419  -8.938  47.280 1.00 12.70 ? 152 ALA   B CB    1 
ATOM   2492 N  N     . VAL   B 1 127 ? 19.094  -9.243  50.507 1.00 13.68 ? 153 VAL   B N     1 
ATOM   2493 C  CA    . VAL   B 1 127 ? 18.450  -9.887  51.649 1.00 15.74 ? 153 VAL   B CA    1 
ATOM   2494 C  C     . VAL   B 1 127 ? 17.026  -9.388  51.797 1.00 18.79 ? 153 VAL   B C     1 
ATOM   2495 O  O     . VAL   B 1 127 ? 16.793  -8.192  51.661 1.00 19.16 ? 153 VAL   B O     1 
ATOM   2496 C  CB    . VAL   B 1 127 ? 19.252  -9.591  52.948 1.00 15.88 ? 153 VAL   B CB    1 
ATOM   2497 C  CG1   . VAL   B 1 127 ? 18.621  -10.262 54.170 1.00 16.97 ? 153 VAL   B CG1   1 
ATOM   2498 C  CG2   . VAL   B 1 127 ? 20.701  -10.017 52.802 1.00 15.83 ? 153 VAL   B CG2   1 
ATOM   2499 N  N     . VAL   B 1 128 ? 16.080  -10.277 52.115 1.00 20.52 ? 154 VAL   B N     1 
ATOM   2500 C  CA    . VAL   B 1 128 ? 14.719  -9.858  52.418 1.00 23.61 ? 154 VAL   B CA    1 
ATOM   2501 C  C     . VAL   B 1 128 ? 14.445  -10.262 53.870 1.00 26.12 ? 154 VAL   B C     1 
ATOM   2502 O  O     . VAL   B 1 128 ? 14.729  -11.397 54.249 1.00 26.00 ? 154 VAL   B O     1 
ATOM   2503 C  CB    . VAL   B 1 128 ? 13.623  -10.376 51.447 1.00 25.21 ? 154 VAL   B CB    1 
ATOM   2504 C  CG1   . VAL   B 1 128 ? 13.754  -11.872 51.199 1.00 26.10 ? 154 VAL   B CG1   1 
ATOM   2505 C  CG2   . VAL   B 1 128 ? 12.225  -10.041 51.984 1.00 25.63 ? 154 VAL   B CG2   1 
ATOM   2506 N  N     . ASN   B 1 129 ? 13.997  -9.310  54.700 1.00 28.07 ? 155 ASN   B N     1 
ATOM   2507 C  CA    . ASN   B 1 129 ? 13.676  -9.549  56.102 1.00 30.60 ? 155 ASN   B CA    1 
ATOM   2508 C  C     . ASN   B 1 129 ? 12.187  -9.464  56.282 1.00 33.55 ? 155 ASN   B C     1 
ATOM   2509 O  O     . ASN   B 1 129 ? 11.604  -8.407  56.080 1.00 33.40 ? 155 ASN   B O     1 
ATOM   2510 C  CB    . ASN   B 1 129 ? 14.343  -8.529  57.012 1.00 31.41 ? 155 ASN   B CB    1 
ATOM   2511 C  CG    . ASN   B 1 129 ? 15.839  -8.571  56.932 1.00 33.34 ? 155 ASN   B CG    1 
ATOM   2512 O  OD1   . ASN   B 1 129 ? 16.493  -7.588  56.575 1.00 35.04 ? 155 ASN   B OD1   1 
ATOM   2513 N  ND2   . ASN   B 1 129 ? 16.404  -9.715  57.236 1.00 32.34 ? 155 ASN   B ND2   1 
ATOM   2514 N  N     . VAL   B 1 130 ? 11.568  -10.587 56.628 1.00 35.84 ? 156 VAL   B N     1 
ATOM   2515 C  CA    . VAL   B 1 130 ? 10.143  -10.660 56.883 1.00 38.20 ? 156 VAL   B CA    1 
ATOM   2516 C  C     . VAL   B 1 130 ? 9.925   -10.369 58.361 1.00 40.48 ? 156 VAL   B C     1 
ATOM   2517 O  O     . VAL   B 1 130 ? 10.395  -11.122 59.220 1.00 40.91 ? 156 VAL   B O     1 
ATOM   2518 C  CB    . VAL   B 1 130 ? 9.602   -12.046 56.504 1.00 39.27 ? 156 VAL   B CB    1 
ATOM   2519 C  CG1   . VAL   B 1 130 ? 8.141   -12.193 56.927 1.00 40.22 ? 156 VAL   B CG1   1 
ATOM   2520 C  CG2   . VAL   B 1 130 ? 9.769   -12.298 55.008 1.00 39.90 ? 156 VAL   B CG2   1 
ATOM   2521 N  N     . ARG   B 1 131 ? 9.286   -9.241  58.664 1.00 41.35 ? 157 ARG   B N     1 
ATOM   2522 C  CA    . ARG   B 1 131 ? 9.011   -8.870  60.047 1.00 42.73 ? 157 ARG   B CA    1 
ATOM   2523 C  C     . ARG   B 1 131 ? 7.523   -8.604  60.184 1.00 43.71 ? 157 ARG   B C     1 
ATOM   2524 O  O     . ARG   B 1 131 ? 6.928   -8.000  59.286 1.00 43.99 ? 157 ARG   B O     1 
ATOM   2525 C  CB    . ARG   B 1 131 ? 9.761   -7.588  60.439 1.00 44.41 ? 157 ARG   B CB    1 
ATOM   2526 C  CG    . ARG   B 1 131 ? 11.273  -7.662  60.331 1.00 48.40 ? 157 ARG   B CG    1 
ATOM   2527 C  CD    . ARG   B 1 131 ? 11.899  -8.266  61.575 1.00 51.31 ? 157 ARG   B CD    1 
ATOM   2528 N  NE    . ARG   B 1 131 ? 13.336  -8.465  61.384 1.00 53.90 ? 157 ARG   B NE    1 
ATOM   2529 C  CZ    . ARG   B 1 131 ? 13.880  -9.566  60.875 1.00 55.33 ? 157 ARG   B CZ    1 
ATOM   2530 N  NH1   . ARG   B 1 131 ? 13.115  -10.594 60.527 1.00 53.87 ? 157 ARG   B NH1   1 
ATOM   2531 N  NH2   . ARG   B 1 131 ? 15.195  -9.653  60.723 1.00 55.66 ? 157 ARG   B NH2   1 
ATOM   2532 N  N     . ALA   B 1 132 ? 6.931   -8.982  61.325 1.00 44.01 ? 158 ALA   B N     1 
ATOM   2533 C  CA    . ALA   B 1 132 ? 5.516   -8.682  61.556 1.00 44.92 ? 158 ALA   B CA    1 
ATOM   2534 C  C     . ALA   B 1 132 ? 5.279   -7.159  61.613 1.00 45.16 ? 158 ALA   B C     1 
ATOM   2535 O  O     . ALA   B 1 132 ? 4.197   -6.707  61.257 1.00 46.07 ? 158 ALA   B O     1 
ATOM   2536 C  CB    . ALA   B 1 132 ? 5.034   -9.346  62.836 1.00 45.38 ? 158 ALA   B CB    1 
ATOM   2537 N  N     . LYS   B 1 133 ? 6.310   -6.371  61.975 1.00 44.59 ? 159 LYS   B N     1 
ATOM   2538 C  CA    . LYS   B 1 133 ? 6.226   -4.916  62.084 1.00 44.31 ? 159 LYS   B CA    1 
ATOM   2539 C  C     . LYS   B 1 133 ? 6.620   -4.141  60.821 1.00 43.02 ? 159 LYS   B C     1 
ATOM   2540 O  O     . LYS   B 1 133 ? 6.485   -2.922  60.811 1.00 43.42 ? 159 LYS   B O     1 
ATOM   2541 C  CB    . LYS   B 1 133 ? 7.049   -4.419  63.288 1.00 46.49 ? 159 LYS   B CB    1 
ATOM   2542 C  CG    . LYS   B 1 133 ? 6.684   -5.117  64.603 1.00 50.57 ? 159 LYS   B CG    1 
ATOM   2543 C  CD    . LYS   B 1 133 ? 6.791   -4.168  65.809 1.00 54.72 ? 159 LYS   B CD    1 
ATOM   2544 C  CE    . LYS   B 1 133 ? 6.666   -4.863  67.152 1.00 57.20 ? 159 LYS   B CE    1 
ATOM   2545 N  NZ    . LYS   B 1 133 ? 7.888   -5.646  67.496 1.00 58.44 ? 159 LYS   B NZ    1 
ATOM   2546 N  N     . GLY   B 1 134 ? 7.106   -4.827  59.780 1.00 41.39 ? 160 GLY   B N     1 
ATOM   2547 C  CA    . GLY   B 1 134 ? 7.501   -4.173  58.531 1.00 39.49 ? 160 GLY   B CA    1 
ATOM   2548 C  C     . GLY   B 1 134 ? 8.584   -4.919  57.772 1.00 36.86 ? 160 GLY   B C     1 
ATOM   2549 O  O     . GLY   B 1 134 ? 9.611   -5.264  58.353 1.00 37.47 ? 160 GLY   B O     1 
ATOM   2550 N  N     . ASP   B 1 135 ? 8.372   -5.193  56.468 1.00 33.66 ? 161 ASP   B N     1 
ATOM   2551 C  CA    . ASP   B 1 135 ? 9.342   -5.958  55.685 1.00 31.12 ? 161 ASP   B CA    1 
ATOM   2552 C  C     . ASP   B 1 135 ? 10.462  -5.082  55.122 1.00 28.67 ? 161 ASP   B C     1 
ATOM   2553 O  O     . ASP   B 1 135 ? 10.251  -3.906  54.831 1.00 28.62 ? 161 ASP   B O     1 
ATOM   2554 C  CB    . ASP   B 1 135 ? 8.652   -6.755  54.567 1.00 32.56 ? 161 ASP   B CB    1 
ATOM   2555 C  CG    . ASP   B 1 135 ? 7.473   -7.579  55.049 1.00 38.36 ? 161 ASP   B CG    1 
ATOM   2556 O  OD1   . ASP   B 1 135 ? 7.626   -8.309  56.058 1.00 38.78 ? 161 ASP   B OD1   1 
ATOM   2557 O  OD2   . ASP   B 1 135 ? 6.392   -7.483  54.432 1.00 41.55 ? 161 ASP   B OD2   1 
ATOM   2558 N  N     . LYS   B 1 136 ? 11.654  -5.663  54.953 1.00 26.18 ? 162 LYS   B N     1 
ATOM   2559 C  CA    . LYS   B 1 136 ? 12.802  -4.920  54.439 1.00 24.18 ? 162 LYS   B CA    1 
ATOM   2560 C  C     . LYS   B 1 136 ? 13.476  -5.666  53.305 1.00 21.88 ? 162 LYS   B C     1 
ATOM   2561 O  O     . LYS   B 1 136 ? 13.567  -6.887  53.339 1.00 21.53 ? 162 LYS   B O     1 
ATOM   2562 C  CB    . LYS   B 1 136 ? 13.839  -4.713  55.553 1.00 25.62 ? 162 LYS   B CB    1 
ATOM   2563 C  CG    . LYS   B 1 136 ? 13.418  -3.748  56.650 1.00 30.08 ? 162 LYS   B CG    1 
ATOM   2564 C  CD    . LYS   B 1 136 ? 14.507  -3.691  57.725 1.00 35.43 ? 162 LYS   B CD    1 
ATOM   2565 C  CE    . LYS   B 1 136 ? 14.083  -2.942  58.958 1.00 39.56 ? 162 LYS   B CE    1 
ATOM   2566 N  NZ    . LYS   B 1 136 ? 15.143  -2.988  60.001 1.00 42.56 ? 162 LYS   B NZ    1 
ATOM   2567 N  N     . ILE   B 1 137 ? 13.986  -4.944  52.322 1.00 20.11 ? 163 ILE   B N     1 
ATOM   2568 C  CA    . ILE   B 1 137 ? 14.744  -5.546  51.226 1.00 19.40 ? 163 ILE   B CA    1 
ATOM   2569 C  C     . ILE   B 1 137 ? 16.012  -4.711  51.089 1.00 16.97 ? 163 ILE   B C     1 
ATOM   2570 O  O     . ILE   B 1 137 ? 15.945  -3.484  51.153 1.00 15.96 ? 163 ILE   B O     1 
ATOM   2571 C  CB    . ILE   B 1 137 ? 13.941  -5.597  49.893 1.00 21.39 ? 163 ILE   B CB    1 
ATOM   2572 C  CG1   . ILE   B 1 137 ? 12.633  -6.375  50.068 1.00 24.36 ? 163 ILE   B CG1   1 
ATOM   2573 C  CG2   . ILE   B 1 137 ? 14.774  -6.240  48.787 1.00 22.33 ? 163 ILE   B CG2   1 
ATOM   2574 C  CD1   . ILE   B 1 137 ? 11.668  -6.166  48.926 1.00 26.94 ? 163 ILE   B CD1   1 
ATOM   2575 N  N     . ALA   B 1 138 ? 17.151  -5.362  50.916 1.00 15.47 ? 164 ALA   B N     1 
ATOM   2576 C  CA    . ALA   B 1 138 ? 18.404  -4.652  50.810 1.00 15.47 ? 164 ALA   B CA    1 
ATOM   2577 C  C     . ALA   B 1 138 ? 19.311  -5.259  49.771 1.00 15.63 ? 164 ALA   B C     1 
ATOM   2578 O  O     . ALA   B 1 138 ? 19.303  -6.472  49.585 1.00 15.99 ? 164 ALA   B O     1 
ATOM   2579 C  CB    . ALA   B 1 138 ? 19.112  -4.658  52.159 1.00 15.27 ? 164 ALA   B CB    1 
ATOM   2580 N  N     . ILE   B 1 139 ? 20.089  -4.421  49.095 1.00 14.88 ? 165 ILE   B N     1 
ATOM   2581 C  CA    . ILE   B 1 139 ? 21.111  -4.903  48.181 1.00 15.18 ? 165 ILE   B CA    1 
ATOM   2582 C  C     . ILE   B 1 139 ? 22.432  -4.636  48.887 1.00 14.33 ? 165 ILE   B C     1 
ATOM   2583 O  O     . ILE   B 1 139 ? 22.699  -3.503  49.285 1.00 14.49 ? 165 ILE   B O     1 
ATOM   2584 C  CB    . ILE   B 1 139 ? 21.069  -4.274  46.767 1.00 16.43 ? 165 ILE   B CB    1 
ATOM   2585 C  CG1   . ILE   B 1 139 ? 19.875  -4.848  45.977 1.00 18.44 ? 165 ILE   B CG1   1 
ATOM   2586 C  CG2   . ILE   B 1 139 ? 22.418  -4.530  46.024 1.00 16.06 ? 165 ILE   B CG2   1 
ATOM   2587 C  CD1   . ILE   B 1 139 ? 19.793  -4.431  44.461 1.00 21.27 ? 165 ILE   B CD1   1 
ATOM   2588 N  N     . TRP   B 1 140 ? 23.261  -5.659  49.009 1.00 13.18 ? 166 TRP   B N     1 
ATOM   2589 C  CA    . TRP   B 1 140 ? 24.549  -5.566  49.692 1.00 13.56 ? 166 TRP   B CA    1 
ATOM   2590 C  C     . TRP   B 1 140 ? 25.642  -5.365  48.692 1.00 14.09 ? 166 TRP   B C     1 
ATOM   2591 O  O     . TRP   B 1 140 ? 25.650  -6.037  47.670 1.00 14.72 ? 166 TRP   B O     1 
ATOM   2592 C  CB    . TRP   B 1 140 ? 24.833  -6.857  50.480 1.00 12.74 ? 166 TRP   B CB    1 
ATOM   2593 C  CG    . TRP   B 1 140 ? 24.047  -6.999  51.755 1.00 12.94 ? 166 TRP   B CG    1 
ATOM   2594 C  CD1   . TRP   B 1 140 ? 22.777  -6.562  52.000 1.00 13.67 ? 166 TRP   B CD1   1 
ATOM   2595 C  CD2   . TRP   B 1 140 ? 24.458  -7.709  52.926 1.00 12.57 ? 166 TRP   B CD2   1 
ATOM   2596 N  NE1   . TRP   B 1 140 ? 22.402  -6.898  53.280 1.00 13.50 ? 166 TRP   B NE1   1 
ATOM   2597 C  CE2   . TRP   B 1 140 ? 23.427  -7.582  53.878 1.00 13.23 ? 166 TRP   B CE2   1 
ATOM   2598 C  CE3   . TRP   B 1 140 ? 25.629  -8.382  53.288 1.00 13.21 ? 166 TRP   B CE3   1 
ATOM   2599 C  CZ2   . TRP   B 1 140 ? 23.527  -8.124  55.164 1.00 13.81 ? 166 TRP   B CZ2   1 
ATOM   2600 C  CZ3   . TRP   B 1 140 ? 25.728  -8.915  54.566 1.00 13.67 ? 166 TRP   B CZ3   1 
ATOM   2601 C  CH2   . TRP   B 1 140 ? 24.669  -8.823  55.467 1.00 13.80 ? 166 TRP   B CH2   1 
ATOM   2602 N  N     . THR   B 1 141 ? 26.573  -4.442  48.973 1.00 14.20 ? 167 THR   B N     1 
ATOM   2603 C  CA    . THR   B 1 141 ? 27.715  -4.174  48.102 1.00 14.94 ? 167 THR   B CA    1 
ATOM   2604 C  C     . THR   B 1 141 ? 29.023  -4.378  48.885 1.00 15.05 ? 167 THR   B C     1 
ATOM   2605 O  O     . THR   B 1 141 ? 29.028  -4.402  50.117 1.00 15.04 ? 167 THR   B O     1 
ATOM   2606 C  CB    . THR   B 1 141 ? 27.602  -2.805  47.360 1.00 16.88 ? 167 THR   B CB    1 
ATOM   2607 O  OG1   . THR   B 1 141 ? 28.130  -1.741  48.159 1.00 19.15 ? 167 THR   B OG1   1 
ATOM   2608 C  CG2   . THR   B 1 141 ? 26.186  -2.489  46.873 1.00 16.40 ? 167 THR   B CG2   1 
ATOM   2609 N  N     . THR   B 1 142 ? 30.136  -4.539  48.172 1.00 15.46 ? 168 THR   B N     1 
ATOM   2610 C  CA    . THR   B 1 142 ? 31.384  -4.954  48.791 1.00 16.22 ? 168 THR   B CA    1 
ATOM   2611 C  C     . THR   B 1 142 ? 32.215  -3.866  49.465 1.00 16.86 ? 168 THR   B C     1 
ATOM   2612 O  O     . THR   B 1 142 ? 32.991  -4.201  50.373 1.00 16.64 ? 168 THR   B O     1 
ATOM   2613 C  CB    . THR   B 1 142 ? 32.258  -5.713  47.781 1.00 17.45 ? 168 THR   B CB    1 
ATOM   2614 O  OG1   . THR   B 1 142 ? 33.283  -6.411  48.499 1.00 18.22 ? 168 THR   B OG1   1 
ATOM   2615 C  CG2   . THR   B 1 142 ? 32.881  -4.800  46.710 1.00 17.60 ? 168 THR   B CG2   1 
ATOM   2616 N  N     . GLU   B 1 143 ? 32.107  -2.607  49.024 1.00 17.01 ? 169 GLU   B N     1 
ATOM   2617 C  CA    . GLU   B 1 143 ? 32.979  -1.559  49.572 1.00 18.26 ? 169 GLU   B CA    1 
ATOM   2618 C  C     . GLU   B 1 143 ? 32.228  -0.243  49.776 1.00 19.12 ? 169 GLU   B C     1 
ATOM   2619 O  O     . GLU   B 1 143 ? 31.841  0.410   48.800 1.00 18.79 ? 169 GLU   B O     1 
ATOM   2620 C  CB    . GLU   B 1 143 ? 34.196  -1.379  48.636 1.00 19.46 ? 169 GLU   B CB    1 
ATOM   2621 C  CG    . GLU   B 1 143 ? 35.138  -0.265  49.051 1.00 21.35 ? 169 GLU   B CG    1 
ATOM   2622 C  CD    . GLU   B 1 143 ? 35.663  -0.459  50.456 1.00 27.00 ? 169 GLU   B CD    1 
ATOM   2623 O  OE1   . GLU   B 1 143 ? 35.303  0.349   51.344 1.00 26.62 ? 169 GLU   B OE1   1 
ATOM   2624 O  OE2   . GLU   B 1 143 ? 36.363  -1.474  50.684 1.00 29.28 ? 169 GLU   B OE2   1 
ATOM   2625 N  N     . CYS   B 1 144 ? 31.986  0.126   51.039 1.00 19.80 ? 170 CYS   B N     1 
ATOM   2626 C  CA    . CYS   B 1 144 ? 31.231  1.337   51.359 1.00 21.56 ? 170 CYS   B CA    1 
ATOM   2627 C  C     . CYS   B 1 144 ? 31.969  2.635   50.929 1.00 23.56 ? 170 CYS   B C     1 
ATOM   2628 O  O     . CYS   B 1 144 ? 31.322  3.656   50.712 1.00 24.08 ? 170 CYS   B O     1 
ATOM   2629 C  CB    . CYS   B 1 144 ? 30.817  1.366   52.831 1.00 22.33 ? 170 CYS   B CB    1 
ATOM   2630 S  SG    . CYS   B 1 144 ? 32.203  1.535   53.988 1.00 28.50 ? 170 CYS   B SG    1 
ATOM   2631 N  N     . GLU   B 1 145 ? 33.284  2.565   50.696 1.00 24.13 ? 171 GLU   B N     1 
ATOM   2632 C  CA    . GLU   B 1 145 ? 34.051  3.720   50.224 1.00 25.46 ? 171 GLU   B CA    1 
ATOM   2633 C  C     . GLU   B 1 145 ? 34.004  3.908   48.705 1.00 26.44 ? 171 GLU   B C     1 
ATOM   2634 O  O     . GLU   B 1 145 ? 34.527  4.913   48.210 1.00 27.07 ? 171 GLU   B O     1 
ATOM   2635 C  CB    . GLU   B 1 145 ? 35.500  3.626   50.692 1.00 28.58 ? 171 GLU   B CB    1 
ATOM   2636 C  CG    . GLU   B 1 145 ? 35.599  3.710   52.205 1.00 37.38 ? 171 GLU   B CG    1 
ATOM   2637 C  CD    . GLU   B 1 145 ? 37.009  3.727   52.757 1.00 48.54 ? 171 GLU   B CD    1 
ATOM   2638 O  OE1   . GLU   B 1 145 ? 37.957  3.956   51.971 1.00 51.42 ? 171 GLU   B OE1   1 
ATOM   2639 O  OE2   . GLU   B 1 145 ? 37.164  3.518   53.982 1.00 52.92 ? 171 GLU   B OE2   1 
ATOM   2640 N  N     . ASN   B 1 146 ? 33.409  2.952   47.948 1.00 25.55 ? 172 ASN   B N     1 
ATOM   2641 C  CA    . ASN   B 1 146 ? 33.322  3.109   46.498 1.00 25.32 ? 172 ASN   B CA    1 
ATOM   2642 C  C     . ASN   B 1 146 ? 32.081  3.978   46.180 1.00 24.52 ? 172 ASN   B C     1 
ATOM   2643 O  O     . ASN   B 1 146 ? 31.083  3.473   45.686 1.00 23.80 ? 172 ASN   B O     1 
ATOM   2644 C  CB    . ASN   B 1 146 ? 33.251  1.740   45.809 1.00 26.99 ? 172 ASN   B CB    1 
ATOM   2645 C  CG    . ASN   B 1 146 ? 34.583  1.012   45.752 1.00 31.83 ? 172 ASN   B CG    1 
ATOM   2646 O  OD1   . ASN   B 1 146 ? 35.651  1.581   46.037 1.00 33.68 ? 172 ASN   B OD1   1 
ATOM   2647 N  ND2   . ASN   B 1 146 ? 34.554  -0.260  45.384 1.00 31.69 ? 172 ASN   B ND2   1 
ATOM   2648 N  N     . ARG   B 1 147 ? 32.145  5.274   46.487 1.00 24.57 ? 173 ARG   B N     1 
ATOM   2649 C  CA    . ARG   B 1 147 ? 31.012  6.198   46.313 1.00 25.22 ? 173 ARG   B CA    1 
ATOM   2650 C  C     . ARG   B 1 147 ? 30.371  6.173   44.901 1.00 23.53 ? 173 ARG   B C     1 
ATOM   2651 O  O     . ARG   B 1 147 ? 29.142  6.095   44.797 1.00 22.67 ? 173 ARG   B O     1 
ATOM   2652 C  CB    . ARG   B 1 147 ? 31.416  7.633   46.712 1.00 28.82 ? 173 ARG   B CB    1 
ATOM   2653 C  CG    . ARG   B 1 147 ? 32.648  8.138   45.960 1.00 36.72 ? 173 ARG   B CG    1 
ATOM   2654 C  CD    . ARG   B 1 147 ? 32.936  9.618   46.179 1.00 43.64 ? 173 ARG   B CD    1 
ATOM   2655 N  NE    . ARG   B 1 147 ? 33.918  9.837   47.247 1.00 49.14 ? 173 ARG   B NE    1 
ATOM   2656 C  CZ    . ARG   B 1 147 ? 34.290  11.039  47.684 1.00 53.82 ? 173 ARG   B CZ    1 
ATOM   2657 N  NH1   . ARG   B 1 147 ? 33.774  12.139  47.145 1.00 54.47 ? 173 ARG   B NH1   1 
ATOM   2658 N  NH2   . ARG   B 1 147 ? 35.181  11.150  48.663 1.00 54.04 ? 173 ARG   B NH2   1 
ATOM   2659 N  N     . GLU   B 1 148 ? 31.184  6.190   43.832 1.00 22.31 ? 174 GLU   B N     1 
ATOM   2660 C  CA    . GLU   B 1 148 ? 30.648  6.161   42.469 1.00 22.07 ? 174 GLU   B CA    1 
ATOM   2661 C  C     . GLU   B 1 148 ? 29.839  4.886   42.163 1.00 20.21 ? 174 GLU   B C     1 
ATOM   2662 O  O     . GLU   B 1 148 ? 28.719  4.995   41.648 1.00 19.87 ? 174 GLU   B O     1 
ATOM   2663 C  CB    . GLU   B 1 148 ? 31.754  6.403   41.437 1.00 25.84 ? 174 GLU   B CB    1 
ATOM   2664 C  CG    . GLU   B 1 148 ? 32.018  7.890   41.252 1.00 34.97 ? 174 GLU   B CG    1 
ATOM   2665 C  CD    . GLU   B 1 148 ? 33.458  8.371   41.257 1.00 46.37 ? 174 GLU   B CD    1 
ATOM   2666 O  OE1   . GLU   B 1 148 ? 34.383  7.524   41.258 1.00 50.75 ? 174 GLU   B OE1   1 
ATOM   2667 O  OE2   . GLU   B 1 148 ? 33.660  9.608   41.257 1.00 48.13 ? 174 GLU   B OE2   1 
ATOM   2668 N  N     . ALA   B 1 149 ? 30.382  3.696   42.499 1.00 18.14 ? 175 ALA   B N     1 
ATOM   2669 C  CA    . ALA   B 1 149 ? 29.655  2.452   42.279 1.00 17.78 ? 175 ALA   B CA    1 
ATOM   2670 C  C     . ALA   B 1 149 ? 28.398  2.400   43.143 1.00 17.28 ? 175 ALA   B C     1 
ATOM   2671 O  O     . ALA   B 1 149 ? 27.321  2.156   42.608 1.00 17.33 ? 175 ALA   B O     1 
ATOM   2672 C  CB    . ALA   B 1 149 ? 30.546  1.232   42.546 1.00 17.84 ? 175 ALA   B CB    1 
ATOM   2673 N  N     . VAL   B 1 150 ? 28.529  2.676   44.455 1.00 16.40 ? 176 VAL   B N     1 
ATOM   2674 C  CA    . VAL   B 1 150 ? 27.420  2.629   45.392 1.00 16.62 ? 176 VAL   B CA    1 
ATOM   2675 C  C     . VAL   B 1 150 ? 26.270  3.550   44.959 1.00 15.96 ? 176 VAL   B C     1 
ATOM   2676 O  O     . VAL   B 1 150 ? 25.121  3.108   44.939 1.00 15.48 ? 176 VAL   B O     1 
ATOM   2677 C  CB    . VAL   B 1 150 ? 27.907  2.944   46.823 1.00 18.05 ? 176 VAL   B CB    1 
ATOM   2678 C  CG1   . VAL   B 1 150 ? 26.727  3.151   47.758 1.00 18.90 ? 176 VAL   B CG1   1 
ATOM   2679 C  CG2   . VAL   B 1 150 ? 28.815  1.832   47.352 1.00 18.55 ? 176 VAL   B CG2   1 
ATOM   2680 N  N     . THR   B 1 151 ? 26.575  4.804   44.576 1.00 15.68 ? 177 THR   B N     1 
ATOM   2681 C  CA    . THR   B 1 151 ? 25.519  5.752   44.203 1.00 16.36 ? 177 THR   B CA    1 
ATOM   2682 C  C     . THR   B 1 151 ? 24.842  5.365   42.880 1.00 15.78 ? 177 THR   B C     1 
ATOM   2683 O  O     . THR   B 1 151 ? 23.631  5.530   42.757 1.00 15.54 ? 177 THR   B O     1 
ATOM   2684 C  CB    . THR   B 1 151 ? 26.014  7.215   44.224 1.00 19.79 ? 177 THR   B CB    1 
ATOM   2685 O  OG1   . THR   B 1 151 ? 26.936  7.411   43.169 1.00 23.06 ? 177 THR   B OG1   1 
ATOM   2686 C  CG2   . THR   B 1 151 ? 26.650  7.614   45.551 1.00 20.24 ? 177 THR   B CG2   1 
ATOM   2687 N  N     . HIS   B 1 152 ? 25.586  4.777   41.935 1.00 15.61 ? 178 HIS   B N     1 
ATOM   2688 C  CA    . HIS   B 1 152 ? 24.990  4.341   40.674 1.00 16.21 ? 178 HIS   B CA    1 
ATOM   2689 C  C     . HIS   B 1 152 ? 24.050  3.151   40.931 1.00 15.31 ? 178 HIS   B C     1 
ATOM   2690 O  O     . HIS   B 1 152 ? 22.940  3.114   40.412 1.00 14.74 ? 178 HIS   B O     1 
ATOM   2691 C  CB    . HIS   B 1 152 ? 26.062  3.950   39.654 1.00 18.38 ? 178 HIS   B CB    1 
ATOM   2692 C  CG    . HIS   B 1 152 ? 25.474  3.512   38.353 1.00 21.25 ? 178 HIS   B CG    1 
ATOM   2693 N  ND1   . HIS   B 1 152 ? 25.159  2.185   38.111 1.00 24.34 ? 178 HIS   B ND1   1 
ATOM   2694 C  CD2   . HIS   B 1 152 ? 25.109  4.248   37.284 1.00 21.78 ? 178 HIS   B CD2   1 
ATOM   2695 C  CE1   . HIS   B 1 152 ? 24.673  2.153   36.882 1.00 23.92 ? 178 HIS   B CE1   1 
ATOM   2696 N  NE2   . HIS   B 1 152 ? 24.629  3.375   36.346 1.00 23.57 ? 178 HIS   B NE2   1 
ATOM   2697 N  N     . ILE   B 1 153 ? 24.480  2.187   41.766 1.00 15.01 ? 179 ILE   B N     1 
ATOM   2698 C  CA    . ILE   B 1 153 ? 23.659  1.028   42.127 1.00 14.09 ? 179 ILE   B CA    1 
ATOM   2699 C  C     . ILE   B 1 153 ? 22.343  1.517   42.773 1.00 14.12 ? 179 ILE   B C     1 
ATOM   2700 O  O     . ILE   B 1 153 ? 21.273  1.144   42.317 1.00 13.96 ? 179 ILE   B O     1 
ATOM   2701 C  CB    . ILE   B 1 153 ? 24.435  0.047   43.042 1.00 13.72 ? 179 ILE   B CB    1 
ATOM   2702 C  CG1   . ILE   B 1 153 ? 25.591  -0.632  42.263 1.00 14.65 ? 179 ILE   B CG1   1 
ATOM   2703 C  CG2   . ILE   B 1 153 ? 23.489  -0.997  43.640 1.00 13.77 ? 179 ILE   B CG2   1 
ATOM   2704 C  CD1   . ILE   B 1 153 ? 26.681  -1.265  43.152 1.00 14.59 ? 179 ILE   B CD1   1 
ATOM   2705 N  N     . GLY   B 1 154 ? 22.445  2.423   43.739 1.00 13.90 ? 180 GLY   B N     1 
ATOM   2706 C  CA    . GLY   B 1 154 ? 21.274  2.983   44.396 1.00 14.93 ? 180 GLY   B CA    1 
ATOM   2707 C  C     . GLY   B 1 154 ? 20.300  3.700   43.482 1.00 16.49 ? 180 GLY   B C     1 
ATOM   2708 O  O     . GLY   B 1 154 ? 19.096  3.457   43.575 1.00 17.15 ? 180 GLY   B O     1 
ATOM   2709 N  N     . ARG   B 1 155 ? 20.809  4.600   42.605 1.00 17.31 ? 181 ARG   B N     1 
ATOM   2710 C  CA    . ARG   B 1 155 ? 19.992  5.356   41.649 1.00 19.09 ? 181 ARG   B CA    1 
ATOM   2711 C  C     . ARG   B 1 155 ? 19.205  4.439   40.712 1.00 17.73 ? 181 ARG   B C     1 
ATOM   2712 O  O     . ARG   B 1 155 ? 18.004  4.643   40.537 1.00 16.91 ? 181 ARG   B O     1 
ATOM   2713 C  CB    . ARG   B 1 155 ? 20.852  6.322   40.796 1.00 23.01 ? 181 ARG   B CB    1 
ATOM   2714 C  CG    . ARG   B 1 155 ? 21.498  7.463   41.554 1.00 30.22 ? 181 ARG   B CG    1 
ATOM   2715 C  CD    . ARG   B 1 155 ? 22.026  8.541   40.608 1.00 37.00 ? 181 ARG   B CD    1 
ATOM   2716 N  NE    . ARG   B 1 155 ? 23.024  8.031   39.663 1.00 42.07 ? 181 ARG   B NE    1 
ATOM   2717 C  CZ    . ARG   B 1 155 ? 24.337  8.027   39.883 1.00 45.53 ? 181 ARG   B CZ    1 
ATOM   2718 N  NH1   . ARG   B 1 155 ? 24.827  8.491   41.024 1.00 45.69 ? 181 ARG   B NH1   1 
ATOM   2719 N  NH2   . ARG   B 1 155 ? 25.169  7.556   38.963 1.00 46.40 ? 181 ARG   B NH2   1 
ATOM   2720 N  N     . VAL   B 1 156 ? 19.891  3.461   40.088 1.00 16.68 ? 182 VAL   B N     1 
ATOM   2721 C  CA    . VAL   B 1 156 ? 19.286  2.499   39.169 1.00 16.47 ? 182 VAL   B CA    1 
ATOM   2722 C  C     . VAL   B 1 156 ? 18.306  1.595   39.919 1.00 15.53 ? 182 VAL   B C     1 
ATOM   2723 O  O     . VAL   B 1 156 ? 17.217  1.345   39.424 1.00 14.74 ? 182 VAL   B O     1 
ATOM   2724 C  CB    . VAL   B 1 156 ? 20.375  1.658   38.451 1.00 17.74 ? 182 VAL   B CB    1 
ATOM   2725 C  CG1   . VAL   B 1 156 ? 19.754  0.511   37.652 1.00 17.76 ? 182 VAL   B CG1   1 
ATOM   2726 C  CG2   . VAL   B 1 156 ? 21.252  2.539   37.563 1.00 18.92 ? 182 VAL   B CG2   1 
ATOM   2727 N  N     . TYR   B 1 157 ? 18.681  1.115   41.118 1.00 15.12 ? 183 TYR   B N     1 
ATOM   2728 C  CA    . TYR   B 1 157 ? 17.812  0.252   41.909 1.00 16.34 ? 183 TYR   B CA    1 
ATOM   2729 C  C     . TYR   B 1 157 ? 16.488  0.951   42.251 1.00 17.75 ? 183 TYR   B C     1 
ATOM   2730 O  O     . TYR   B 1 157 ? 15.419  0.358   42.094 1.00 18.36 ? 183 TYR   B O     1 
ATOM   2731 C  CB    . TYR   B 1 157 ? 18.533  -0.162  43.197 1.00 16.58 ? 183 TYR   B CB    1 
ATOM   2732 C  CG    . TYR   B 1 157 ? 17.798  -1.134  44.086 1.00 18.25 ? 183 TYR   B CG    1 
ATOM   2733 C  CD1   . TYR   B 1 157 ? 17.094  -2.205  43.547 1.00 19.16 ? 183 TYR   B CD1   1 
ATOM   2734 C  CD2   . TYR   B 1 157 ? 17.955  -1.092  45.468 1.00 19.66 ? 183 TYR   B CD2   1 
ATOM   2735 C  CE1   . TYR   B 1 157 ? 16.500  -3.162  44.364 1.00 20.48 ? 183 TYR   B CE1   1 
ATOM   2736 C  CE2   . TYR   B 1 157 ? 17.380  -2.047  46.292 1.00 20.58 ? 183 TYR   B CE2   1 
ATOM   2737 C  CZ    . TYR   B 1 157 ? 16.649  -3.077  45.739 1.00 21.45 ? 183 TYR   B CZ    1 
ATOM   2738 O  OH    . TYR   B 1 157 ? 16.077  -4.001  46.563 1.00 22.90 ? 183 TYR   B OH    1 
ATOM   2739 N  N     . LYS   B 1 158 ? 16.560  2.195   42.716 1.00 17.97 ? 184 LYS   B N     1 
ATOM   2740 C  CA    . LYS   B 1 158 ? 15.369  2.955   43.078 1.00 18.90 ? 184 LYS   B CA    1 
ATOM   2741 C  C     . LYS   B 1 158 ? 14.478  3.175   41.853 1.00 19.65 ? 184 LYS   B C     1 
ATOM   2742 O  O     . LYS   B 1 158 ? 13.266  3.006   41.940 1.00 19.74 ? 184 LYS   B O     1 
ATOM   2743 C  CB    . LYS   B 1 158 ? 15.778  4.280   43.726 1.00 21.23 ? 184 LYS   B CB    1 
ATOM   2744 C  CG    . LYS   B 1 158 ? 14.635  5.266   43.934 1.00 25.44 ? 184 LYS   B CG    1 
ATOM   2745 C  CD    . LYS   B 1 158 ? 15.083  6.420   44.802 1.00 29.64 ? 184 LYS   B CD    1 
ATOM   2746 C  CE    . LYS   B 1 158 ? 13.988  7.429   45.028 1.00 33.11 ? 184 LYS   B CE    1 
ATOM   2747 N  NZ    . LYS   B 1 158 ? 14.464  8.517   45.906 1.00 35.98 ? 184 LYS   B NZ    1 
ATOM   2748 N  N     . GLU   B 1 159 ? 15.081  3.535   40.717 1.00 20.09 ? 185 GLU   B N     1 
ATOM   2749 C  CA    . GLU   B 1 159 ? 14.369  3.746   39.455 1.00 21.13 ? 185 GLU   B CA    1 
ATOM   2750 C  C     . GLU   B 1 159 ? 13.698  2.452   38.967 1.00 21.55 ? 185 GLU   B C     1 
ATOM   2751 O  O     . GLU   B 1 159 ? 12.525  2.480   38.612 1.00 21.93 ? 185 GLU   B O     1 
ATOM   2752 C  CB    . GLU   B 1 159 ? 15.358  4.265   38.401 1.00 25.54 ? 185 GLU   B CB    1 
ATOM   2753 C  CG    . GLU   B 1 159 ? 14.810  4.411   36.983 1.00 35.43 ? 185 GLU   B CG    1 
ATOM   2754 C  CD    . GLU   B 1 159 ? 15.842  4.860   35.958 1.00 48.61 ? 185 GLU   B CD    1 
ATOM   2755 O  OE1   . GLU   B 1 159 ? 17.030  5.032   36.335 1.00 50.85 ? 185 GLU   B OE1   1 
ATOM   2756 O  OE2   . GLU   B 1 159 ? 15.463  5.036   34.773 1.00 52.94 ? 185 GLU   B OE2   1 
ATOM   2757 N  N     . ARG   B 1 160 ? 14.428  1.317   38.998 1.00 21.46 ? 186 ARG   B N     1 
ATOM   2758 C  CA    . ARG   B 1 160 ? 13.998  -0.018  38.550 1.00 22.26 ? 186 ARG   B CA    1 
ATOM   2759 C  C     . ARG   B 1 160 ? 12.810  -0.519  39.376 1.00 22.66 ? 186 ARG   B C     1 
ATOM   2760 O  O     . ARG   B 1 160 ? 11.893  -1.148  38.832 1.00 22.78 ? 186 ARG   B O     1 
ATOM   2761 C  CB    . ARG   B 1 160 ? 15.193  -1.001  38.640 1.00 23.94 ? 186 ARG   B CB    1 
ATOM   2762 C  CG    . ARG   B 1 160 ? 15.132  -2.264  37.794 1.00 27.77 ? 186 ARG   B CG    1 
ATOM   2763 C  CD    . ARG   B 1 160 ? 14.853  -2.070  36.311 1.00 29.83 ? 186 ARG   B CD    1 
ATOM   2764 N  NE    . ARG   B 1 160 ? 15.824  -1.201  35.646 1.00 32.10 ? 186 ARG   B NE    1 
ATOM   2765 C  CZ    . ARG   B 1 160 ? 16.890  -1.627  34.976 1.00 32.85 ? 186 ARG   B CZ    1 
ATOM   2766 N  NH1   . ARG   B 1 160 ? 17.138  -2.927  34.863 1.00 30.80 ? 186 ARG   B NH1   1 
ATOM   2767 N  NH2   . ARG   B 1 160 ? 17.715  -0.757  34.412 1.00 32.23 ? 186 ARG   B NH2   1 
ATOM   2768 N  N     . LEU   B 1 161 ? 12.801  -0.203  40.681 1.00 22.20 ? 187 LEU   B N     1 
ATOM   2769 C  CA    . LEU   B 1 161 ? 11.687  -0.597  41.530 1.00 23.03 ? 187 LEU   B CA    1 
ATOM   2770 C  C     . LEU   B 1 161 ? 10.482  0.393   41.479 1.00 22.87 ? 187 LEU   B C     1 
ATOM   2771 O  O     . LEU   B 1 161 ? 9.423   0.074   42.015 1.00 23.58 ? 187 LEU   B O     1 
ATOM   2772 C  CB    . LEU   B 1 161 ? 12.147  -0.867  42.967 1.00 23.89 ? 187 LEU   B CB    1 
ATOM   2773 C  CG    . LEU   B 1 161 ? 12.487  -2.347  43.305 1.00 25.44 ? 187 LEU   B CG    1 
ATOM   2774 C  CD1   . LEU   B 1 161 ? 13.549  -2.926  42.366 1.00 25.25 ? 187 LEU   B CD1   1 
ATOM   2775 C  CD2   . LEU   B 1 161 ? 12.980  -2.464  44.716 1.00 26.55 ? 187 LEU   B CD2   1 
ATOM   2776 N  N     . GLY   B 1 162 ? 10.625  1.520   40.793 1.00 21.97 ? 188 GLY   B N     1 
ATOM   2777 C  CA    . GLY   B 1 162 ? 9.558   2.504   40.645 1.00 23.65 ? 188 GLY   B CA    1 
ATOM   2778 C  C     . GLY   B 1 162 ? 9.188   3.267   41.907 1.00 25.80 ? 188 GLY   B C     1 
ATOM   2779 O  O     . GLY   B 1 162 ? 8.059   3.747   42.030 1.00 25.22 ? 188 GLY   B O     1 
ATOM   2780 N  N     . LEU   B 1 163 ? 10.133  3.378   42.860 1.00 27.38 ? 189 LEU   B N     1 
ATOM   2781 C  CA    . LEU   B 1 163 ? 9.921   4.021   44.163 1.00 29.49 ? 189 LEU   B CA    1 
ATOM   2782 C  C     . LEU   B 1 163 ? 9.589   5.506   44.056 1.00 31.22 ? 189 LEU   B C     1 
ATOM   2783 O  O     . LEU   B 1 163 ? 10.004  6.150   43.092 1.00 31.65 ? 189 LEU   B O     1 
ATOM   2784 C  CB    . LEU   B 1 163 ? 11.170  3.843   45.039 1.00 30.07 ? 189 LEU   B CB    1 
ATOM   2785 C  CG    . LEU   B 1 163 ? 11.520  2.418   45.441 1.00 32.43 ? 189 LEU   B CG    1 
ATOM   2786 C  CD1   . LEU   B 1 163 ? 12.814  2.394   46.198 1.00 33.42 ? 189 LEU   B CD1   1 
ATOM   2787 C  CD2   . LEU   B 1 163 ? 10.440  1.810   46.297 1.00 33.69 ? 189 LEU   B CD2   1 
ATOM   2788 N  N     . PRO   B 1 164 ? 8.845   6.078   45.037 1.00 31.85 ? 190 PRO   B N     1 
ATOM   2789 C  CA    . PRO   B 1 164 ? 8.556   7.524   44.993 1.00 32.27 ? 190 PRO   B CA    1 
ATOM   2790 C  C     . PRO   B 1 164 ? 9.859   8.338   45.000 1.00 32.29 ? 190 PRO   B C     1 
ATOM   2791 O  O     . PRO   B 1 164 ? 10.706  8.168   45.877 1.00 32.97 ? 190 PRO   B O     1 
ATOM   2792 C  CB    . PRO   B 1 164 ? 7.746   7.768   46.272 1.00 32.84 ? 190 PRO   B CB    1 
ATOM   2793 C  CG    . PRO   B 1 164 ? 7.235   6.430   46.667 1.00 33.52 ? 190 PRO   B CG    1 
ATOM   2794 C  CD    . PRO   B 1 164 ? 8.284   5.454   46.249 1.00 31.60 ? 190 PRO   B CD    1 
ATOM   2795 N  N     . PRO   B 1 165 ? 10.065  9.150   43.965 1.00 31.43 ? 191 PRO   B N     1 
ATOM   2796 C  CA    . PRO   B 1 165 ? 11.339  9.870   43.833 1.00 30.84 ? 191 PRO   B CA    1 
ATOM   2797 C  C     . PRO   B 1 165 ? 11.696  10.843  44.954 1.00 29.39 ? 191 PRO   B C     1 
ATOM   2798 O  O     . PRO   B 1 165 ? 12.876  11.003  45.233 1.00 29.05 ? 191 PRO   B O     1 
ATOM   2799 C  CB    . PRO   B 1 165 ? 11.181  10.595  42.491 1.00 31.76 ? 191 PRO   B CB    1 
ATOM   2800 C  CG    . PRO   B 1 165 ? 10.173  9.730   41.721 1.00 32.57 ? 191 PRO   B CG    1 
ATOM   2801 C  CD    . PRO   B 1 165 ? 9.188   9.398   42.803 1.00 31.05 ? 191 PRO   B CD    1 
ATOM   2802 N  N     . LYS   B 1 166 ? 10.708  11.489  45.584 1.00 28.07 ? 192 LYS   B N     1 
ATOM   2803 C  CA    . LYS   B 1 166 ? 10.981  12.434  46.665 1.00 28.67 ? 192 LYS   B CA    1 
ATOM   2804 C  C     . LYS   B 1 166 ? 11.456  11.746  47.941 1.00 28.47 ? 192 LYS   B C     1 
ATOM   2805 O  O     . LYS   B 1 166 ? 12.139  12.371  48.738 1.00 29.17 ? 192 LYS   B O     1 
ATOM   2806 C  CB    . LYS   B 1 166 ? 9.727   13.275  46.986 1.00 30.39 ? 192 LYS   B CB    1 
ATOM   2807 C  CG    . LYS   B 1 166 ? 9.863   14.746  46.662 1.00 34.09 ? 192 LYS   B CG    1 
ATOM   2808 C  CD    . LYS   B 1 166 ? 8.521   15.486  46.793 1.00 39.00 ? 192 LYS   B CD    1 
ATOM   2809 C  CE    . LYS   B 1 166 ? 7.889   15.759  45.444 1.00 44.00 ? 192 LYS   B CE    1 
ATOM   2810 N  NZ    . LYS   B 1 166 ? 6.608   16.521  45.559 1.00 47.12 ? 192 LYS   B NZ    1 
ATOM   2811 N  N     . ILE   B 1 167 ? 11.053  10.490  48.171 1.00 27.76 ? 193 ILE   B N     1 
ATOM   2812 C  CA    . ILE   B 1 167 ? 11.421  9.770   49.385 1.00 27.86 ? 193 ILE   B CA    1 
ATOM   2813 C  C     . ILE   B 1 167 ? 12.736  9.030   49.168 1.00 26.65 ? 193 ILE   B C     1 
ATOM   2814 O  O     . ILE   B 1 167 ? 12.813  8.199   48.275 1.00 27.04 ? 193 ILE   B O     1 
ATOM   2815 C  CB    . ILE   B 1 167 ? 10.288  8.800   49.787 1.00 29.42 ? 193 ILE   B CB    1 
ATOM   2816 C  CG1   . ILE   B 1 167 ? 8.955   9.563   50.024 1.00 31.38 ? 193 ILE   B CG1   1 
ATOM   2817 C  CG2   . ILE   B 1 167 ? 10.696  7.943   50.985 1.00 29.88 ? 193 ILE   B CG2   1 
ATOM   2818 C  CD1   . ILE   B 1 167 ? 9.037   10.723  51.036 1.00 32.99 ? 193 ILE   B CD1   1 
ATOM   2819 N  N     . VAL   B 1 168 ? 13.765  9.335   49.965 1.00 24.94 ? 194 VAL   B N     1 
ATOM   2820 C  CA    . VAL   B 1 168 ? 15.070  8.711   49.777 1.00 24.40 ? 194 VAL   B CA    1 
ATOM   2821 C  C     . VAL   B 1 168 ? 15.186  7.278   50.310 1.00 22.97 ? 194 VAL   B C     1 
ATOM   2822 O  O     . VAL   B 1 168 ? 14.451  6.854   51.207 1.00 22.71 ? 194 VAL   B O     1 
ATOM   2823 C  CB    . VAL   B 1 168 ? 16.221  9.586   50.355 1.00 25.74 ? 194 VAL   B CB    1 
ATOM   2824 C  CG1   . VAL   B 1 168 ? 16.204  10.995  49.784 1.00 26.30 ? 194 VAL   B CG1   1 
ATOM   2825 C  CG2   . VAL   B 1 168 ? 16.205  9.599   51.879 1.00 26.84 ? 194 VAL   B CG2   1 
ATOM   2826 N  N     . ILE   B 1 169 ? 16.136  6.540   49.737 1.00 21.55 ? 195 ILE   B N     1 
ATOM   2827 C  CA    . ILE   B 1 169 ? 16.590  5.257   50.236 1.00 20.77 ? 195 ILE   B CA    1 
ATOM   2828 C  C     . ILE   B 1 169 ? 18.039  5.523   50.734 1.00 19.49 ? 195 ILE   B C     1 
ATOM   2829 O  O     . ILE   B 1 169 ? 18.727  6.406   50.208 1.00 18.92 ? 195 ILE   B O     1 
ATOM   2830 C  CB    . ILE   B 1 169 ? 16.465  4.090   49.221 1.00 21.10 ? 195 ILE   B CB    1 
ATOM   2831 C  CG1   . ILE   B 1 169 ? 17.333  4.306   47.971 1.00 21.82 ? 195 ILE   B CG1   1 
ATOM   2832 C  CG2   . ILE   B 1 169 ? 14.988  3.837   48.863 1.00 20.92 ? 195 ILE   B CG2   1 
ATOM   2833 C  CD1   . ILE   B 1 169 ? 17.504  2.999   47.080 1.00 23.14 ? 195 ILE   B CD1   1 
ATOM   2834 N  N     . GLY   B 1 170 ? 18.426  4.878   51.824 1.00 18.50 ? 196 GLY   B N     1 
ATOM   2835 C  CA    . GLY   B 1 170 ? 19.746  5.114   52.402 1.00 18.19 ? 196 GLY   B CA    1 
ATOM   2836 C  C     . GLY   B 1 170 ? 20.703  3.955   52.238 1.00 17.04 ? 196 GLY   B C     1 
ATOM   2837 O  O     . GLY   B 1 170 ? 20.279  2.806   52.163 1.00 17.09 ? 196 GLY   B O     1 
ATOM   2838 N  N     . TYR   B 1 171 ? 21.988  4.251   52.189 1.00 15.81 ? 197 TYR   B N     1 
ATOM   2839 C  CA    . TYR   B 1 171 ? 23.001  3.223   52.131 1.00 15.70 ? 197 TYR   B CA    1 
ATOM   2840 C  C     . TYR   B 1 171 ? 23.676  3.255   53.488 1.00 17.29 ? 197 TYR   B C     1 
ATOM   2841 O  O     . TYR   B 1 171 ? 24.194  4.297   53.868 1.00 18.44 ? 197 TYR   B O     1 
ATOM   2842 C  CB    . TYR   B 1 171 ? 24.007  3.487   51.000 1.00 14.93 ? 197 TYR   B CB    1 
ATOM   2843 C  CG    . TYR   B 1 171 ? 25.091  2.427   50.886 1.00 15.24 ? 197 TYR   B CG    1 
ATOM   2844 C  CD1   . TYR   B 1 171 ? 26.277  2.538   51.601 1.00 15.73 ? 197 TYR   B CD1   1 
ATOM   2845 C  CD2   . TYR   B 1 171 ? 24.926  1.316   50.069 1.00 15.14 ? 197 TYR   B CD2   1 
ATOM   2846 C  CE1   . TYR   B 1 171 ? 27.281  1.583   51.490 1.00 15.29 ? 197 TYR   B CE1   1 
ATOM   2847 C  CE2   . TYR   B 1 171 ? 25.931  0.357   49.943 1.00 15.32 ? 197 TYR   B CE2   1 
ATOM   2848 C  CZ    . TYR   B 1 171 ? 27.111  0.500   50.655 1.00 15.33 ? 197 TYR   B CZ    1 
ATOM   2849 O  OH    . TYR   B 1 171 ? 28.114  -0.435  50.562 1.00 14.76 ? 197 TYR   B OH    1 
ATOM   2850 N  N     . GLN   B 1 172 ? 23.665  2.141   54.221 1.00 17.45 ? 198 GLN   B N     1 
ATOM   2851 C  CA    . GLN   B 1 172 ? 24.332  2.083   55.519 1.00 18.38 ? 198 GLN   B CA    1 
ATOM   2852 C  C     . GLN   B 1 172 ? 25.511  1.144   55.438 1.00 16.75 ? 198 GLN   B C     1 
ATOM   2853 O  O     . GLN   B 1 172 ? 25.365  0.063   54.911 1.00 15.36 ? 198 GLN   B O     1 
ATOM   2854 C  CB    . GLN   B 1 172 ? 23.393  1.538   56.595 1.00 21.19 ? 198 GLN   B CB    1 
ATOM   2855 C  CG    . GLN   B 1 172 ? 22.195  2.413   56.885 1.00 28.41 ? 198 GLN   B CG    1 
ATOM   2856 C  CD    . GLN   B 1 172 ? 21.508  1.943   58.142 1.00 38.59 ? 198 GLN   B CD    1 
ATOM   2857 O  OE1   . GLN   B 1 172 ? 20.435  1.310   58.087 1.00 41.53 ? 198 GLN   B OE1   1 
ATOM   2858 N  NE2   . GLN   B 1 172 ? 22.131  2.217   59.308 1.00 39.54 ? 198 GLN   B NE2   1 
ATOM   2859 N  N     . SER   B 1 173 ? 26.656  1.535   55.981 1.00 16.37 ? 199 SER   B N     1 
ATOM   2860 C  CA    . SER   B 1 173 ? 27.811  0.621   56.069 1.00 17.01 ? 199 SER   B CA    1 
ATOM   2861 C  C     . SER   B 1 173 ? 27.455  -0.503  57.070 1.00 15.83 ? 199 SER   B C     1 
ATOM   2862 O  O     . SER   B 1 173 ? 26.746  -0.238  58.049 1.00 15.28 ? 199 SER   B O     1 
ATOM   2863 C  CB    . SER   B 1 173 ? 29.013  1.369   56.628 1.00 19.96 ? 199 SER   B CB    1 
ATOM   2864 O  OG    . SER   B 1 173 ? 30.109  0.477   56.695 1.00 26.47 ? 199 SER   B OG    1 
ATOM   2865 N  N     . HIS   B 1 174 ? 27.936  -1.739  56.843 1.00 15.22 ? 200 HIS   B N     1 
ATOM   2866 C  CA    . HIS   B 1 174 ? 27.693  -2.823  57.808 1.00 15.24 ? 200 HIS   B CA    1 
ATOM   2867 C  C     . HIS   B 1 174 ? 28.427  -2.521  59.137 1.00 16.42 ? 200 HIS   B C     1 
ATOM   2868 O  O     . HIS   B 1 174 ? 27.937  -2.931  60.175 1.00 16.93 ? 200 HIS   B O     1 
ATOM   2869 C  CB    . HIS   B 1 174 ? 28.150  -4.199  57.273 1.00 14.86 ? 200 HIS   B CB    1 
ATOM   2870 C  CG    . HIS   B 1 174 ? 27.448  -4.624  56.013 1.00 13.82 ? 200 HIS   B CG    1 
ATOM   2871 N  ND1   . HIS   B 1 174 ? 26.082  -4.460  55.859 1.00 14.83 ? 200 HIS   B ND1   1 
ATOM   2872 C  CD2   . HIS   B 1 174 ? 27.954  -5.144  54.876 1.00 14.41 ? 200 HIS   B CD2   1 
ATOM   2873 C  CE1   . HIS   B 1 174 ? 25.795  -4.895  54.645 1.00 15.29 ? 200 HIS   B CE1   1 
ATOM   2874 N  NE2   . HIS   B 1 174 ? 26.883  -5.322  54.012 1.00 15.26 ? 200 HIS   B NE2   1 
ATOM   2875 N  N     . ALA   B 1 175 ? 29.570  -1.814  59.106 1.00 16.99 ? 201 ALA   B N     1 
ATOM   2876 C  CA    . ALA   B 1 175 ? 30.314  -1.429  60.308 1.00 19.26 ? 201 ALA   B CA    1 
ATOM   2877 C  C     . ALA   B 1 175 ? 29.444  -0.509  61.168 1.00 21.19 ? 201 ALA   B C     1 
ATOM   2878 O  O     . ALA   B 1 175 ? 29.443  -0.662  62.388 1.00 21.60 ? 201 ALA   B O     1 
ATOM   2879 C  CB    . ALA   B 1 175 ? 31.599  -0.700  59.934 1.00 19.16 ? 201 ALA   B CB    1 
ATOM   2880 N  N     . ASP   B 1 176 ? 28.673  0.418   60.544 1.00 21.11 ? 202 ASP   B N     1 
ATOM   2881 C  CA    . ASP   B 1 176 ? 27.780  1.289   61.306 1.00 22.03 ? 202 ASP   B CA    1 
ATOM   2882 C  C     . ASP   B 1 176 ? 26.559  0.509   61.799 1.00 23.08 ? 202 ASP   B C     1 
ATOM   2883 O  O     . ASP   B 1 176 ? 26.054  0.794   62.886 1.00 23.52 ? 202 ASP   B O     1 
ATOM   2884 C  CB    . ASP   B 1 176 ? 27.331  2.512   60.484 1.00 23.97 ? 202 ASP   B CB    1 
ATOM   2885 C  CG    . ASP   B 1 176 ? 28.440  3.503   60.206 1.00 29.04 ? 202 ASP   B CG    1 
ATOM   2886 O  OD1   . ASP   B 1 176 ? 29.392  3.564   61.002 1.00 31.66 ? 202 ASP   B OD1   1 
ATOM   2887 O  OD2   . ASP   B 1 176 ? 28.355  4.213   59.196 1.00 30.48 ? 202 ASP   B OD2   1 
ATOM   2888 N  N     . THR   B 1 177 ? 26.067  -0.467  61.004 1.00 23.04 ? 203 THR   B N     1 
ATOM   2889 C  CA    . THR   B 1 177 ? 24.917  -1.262  61.425 1.00 24.09 ? 203 THR   B CA    1 
ATOM   2890 C  C     . THR   B 1 177 ? 25.284  -2.103  62.650 1.00 26.03 ? 203 THR   B C     1 
ATOM   2891 O  O     . THR   B 1 177 ? 24.538  -2.117  63.616 1.00 26.36 ? 203 THR   B O     1 
ATOM   2892 C  CB    . THR   B 1 177 ? 24.423  -2.167  60.306 1.00 24.71 ? 203 THR   B CB    1 
ATOM   2893 O  OG1   . THR   B 1 177 ? 24.260  -1.416  59.100 1.00 25.31 ? 203 THR   B OG1   1 
ATOM   2894 C  CG2   . THR   B 1 177 ? 23.147  -2.878  60.676 1.00 24.99 ? 203 THR   B CG2   1 
ATOM   2895 N  N     . ALA   B 1 178 ? 26.470  -2.735  62.631 1.00 27.24 ? 204 ALA   B N     1 
ATOM   2896 C  CA    . ALA   B 1 178 ? 26.991  -3.586  63.696 1.00 29.22 ? 204 ALA   B CA    1 
ATOM   2897 C  C     . ALA   B 1 178 ? 27.377  -2.853  64.979 1.00 32.75 ? 204 ALA   B C     1 
ATOM   2898 O  O     . ALA   B 1 178 ? 27.544  -3.515  66.003 1.00 32.92 ? 204 ALA   B O     1 
ATOM   2899 C  CB    . ALA   B 1 178 ? 28.195  -4.364  63.194 1.00 28.43 ? 204 ALA   B CB    1 
ATOM   2900 N  N     . THR   B 1 179 ? 27.630  -1.535  64.915 1.00 35.21 ? 205 THR   B N     1 
ATOM   2901 C  CA    . THR   B 1 179 ? 28.037  -0.753  66.090 1.00 38.46 ? 205 THR   B CA    1 
ATOM   2902 C  C     . THR   B 1 179 ? 26.991  0.312   66.480 1.00 41.93 ? 205 THR   B C     1 
ATOM   2903 O  O     . THR   B 1 179 ? 27.337  1.338   67.060 1.00 41.59 ? 205 THR   B O     1 
ATOM   2904 C  CB    . THR   B 1 179 ? 29.445  -0.160  65.900 1.00 39.73 ? 205 THR   B CB    1 
ATOM   2905 O  OG1   . THR   B 1 179 ? 29.426  0.777   64.823 1.00 40.76 ? 205 THR   B OG1   1 
ATOM   2906 C  CG2   . THR   B 1 179 ? 30.493  -1.224  65.626 1.00 40.11 ? 205 THR   B CG2   1 
ATOM   2907 N  N     . LYS   B 1 180 ? 25.712  0.029   66.179 1.00 45.06 ? 206 LYS   B N     1 
ATOM   2908 C  CA    . LYS   B 1 180 ? 24.511  0.841   66.403 1.00 48.34 ? 206 LYS   B CA    1 
ATOM   2909 C  C     . LYS   B 1 180 ? 24.285  1.272   67.874 1.00 51.21 ? 206 LYS   B C     1 
ATOM   2910 O  O     . LYS   B 1 180 ? 24.721  0.590   68.812 1.00 51.60 ? 206 LYS   B O     1 
ATOM   2911 C  CB    . LYS   B 1 180 ? 23.302  0.031   65.897 1.00 51.08 ? 206 LYS   B CB    1 
ATOM   2912 C  CG    . LYS   B 1 180 ? 21.992  0.786   65.761 1.00 56.52 ? 206 LYS   B CG    1 
ATOM   2913 C  CD    . LYS   B 1 180 ? 20.819  -0.192  65.778 1.00 61.43 ? 206 LYS   B CD    1 
ATOM   2914 C  CE    . LYS   B 1 180 ? 19.526  0.440   66.239 1.00 65.41 ? 206 LYS   B CE    1 
ATOM   2915 N  NZ    . LYS   B 1 180 ? 18.872  1.228   65.161 1.00 67.57 ? 206 LYS   B NZ    1 
ATOM   2916 N  N     . SER   B 1 181 ? 23.598  2.413   68.067 1.00 52.77 ? 207 SER   B N     1 
ATOM   2917 C  CA    . SER   B 1 181 ? 23.256  2.939   69.394 1.00 54.54 ? 207 SER   B CA    1 
ATOM   2918 C  C     . SER   B 1 181 ? 21.800  3.444   69.483 1.00 55.91 ? 207 SER   B C     1 
ATOM   2919 O  O     . SER   B 1 181 ? 21.479  4.195   70.402 1.00 56.31 ? 207 SER   B O     1 
ATOM   2920 C  CB    . SER   B 1 181 ? 24.208  4.063   69.793 1.00 56.36 ? 207 SER   B CB    1 
ATOM   2921 O  OG    . SER   B 1 181 ? 25.495  3.567   70.122 1.00 59.31 ? 207 SER   B OG    1 
ATOM   2922 N  N     . GLY   B 1 182 ? 20.941  3.037   68.549 1.00 56.37 ? 208 GLY   B N     1 
ATOM   2923 C  CA    . GLY   B 1 182 ? 19.542  3.451   68.546 1.00 57.31 ? 208 GLY   B CA    1 
ATOM   2924 C  C     . GLY   B 1 182 ? 19.166  4.298   67.347 1.00 58.15 ? 208 GLY   B C     1 
ATOM   2925 O  O     . GLY   B 1 182 ? 18.781  3.772   66.297 1.00 58.55 ? 208 GLY   B O     1 
ATOM   2926 N  N     . THR   B 1 185 ? 20.993  5.168   63.177 1.00 42.97 ? 211 THR   B N     1 
ATOM   2927 C  CA    . THR   B 1 185 ? 20.531  4.824   61.826 1.00 43.56 ? 211 THR   B CA    1 
ATOM   2928 C  C     . THR   B 1 185 ? 21.215  5.737   60.795 1.00 41.83 ? 211 THR   B C     1 
ATOM   2929 O  O     . THR   B 1 185 ? 20.541  6.506   60.119 1.00 42.82 ? 211 THR   B O     1 
ATOM   2930 C  CB    . THR   B 1 185 ? 19.007  4.932   61.783 1.00 46.41 ? 211 THR   B CB    1 
ATOM   2931 O  OG1   . THR   B 1 185 ? 18.650  6.282   62.096 1.00 48.02 ? 211 THR   B OG1   1 
ATOM   2932 C  CG2   . THR   B 1 185 ? 18.334  3.982   62.772 1.00 47.27 ? 211 THR   B CG2   1 
ATOM   2933 N  N     . LYS   B 1 186 ? 22.557  5.679   60.701 1.00 39.25 ? 212 LYS   B N     1 
ATOM   2934 C  CA    . LYS   B 1 186 ? 23.329  6.577   59.840 1.00 37.61 ? 212 LYS   B CA    1 
ATOM   2935 C  C     . LYS   B 1 186 ? 23.564  6.114   58.410 1.00 34.97 ? 212 LYS   B C     1 
ATOM   2936 O  O     . LYS   B 1 186 ? 24.234  5.113   58.176 1.00 35.56 ? 212 LYS   B O     1 
ATOM   2937 C  CB    . LYS   B 1 186 ? 24.681  6.913   60.476 1.00 40.17 ? 212 LYS   B CB    1 
ATOM   2938 C  CG    . LYS   B 1 186 ? 24.561  7.548   61.851 1.00 45.70 ? 212 LYS   B CG    1 
ATOM   2939 C  CD    . LYS   B 1 186 ? 25.761  7.190   62.721 1.00 50.69 ? 212 LYS   B CD    1 
ATOM   2940 C  CE    . LYS   B 1 186 ? 25.746  7.889   64.058 1.00 54.46 ? 212 LYS   B CE    1 
ATOM   2941 N  NZ    . LYS   B 1 186 ? 26.923  7.497   64.873 1.00 56.65 ? 212 LYS   B NZ    1 
ATOM   2942 N  N     . ASN   B 1 187 ? 23.101  6.916   57.460 1.00 31.76 ? 213 ASN   B N     1 
ATOM   2943 C  CA    . ASN   B 1 187 ? 23.243  6.666   56.042 1.00 29.32 ? 213 ASN   B CA    1 
ATOM   2944 C  C     . ASN   B 1 187 ? 24.467  7.377   55.514 1.00 27.26 ? 213 ASN   B C     1 
ATOM   2945 O  O     . ASN   B 1 187 ? 24.521  8.600   55.625 1.00 26.72 ? 213 ASN   B O     1 
ATOM   2946 C  CB    . ASN   B 1 187 ? 22.024  7.211   55.309 1.00 28.29 ? 213 ASN   B CB    1 
ATOM   2947 C  CG    . ASN   B 1 187 ? 20.781  6.423   55.567 1.00 27.98 ? 213 ASN   B CG    1 
ATOM   2948 O  OD1   . ASN   B 1 187 ? 20.814  5.194   55.673 1.00 26.97 ? 213 ASN   B OD1   1 
ATOM   2949 N  ND2   . ASN   B 1 187 ? 19.651  7.117   55.670 1.00 27.53 ? 213 ASN   B ND2   1 
ATOM   2950 N  N     . ARG   B 1 188 ? 25.418  6.626   54.902 1.00 25.26 ? 214 ARG   B N     1 
ATOM   2951 C  CA    . ARG   B 1 188 ? 26.618  7.172   54.268 1.00 24.43 ? 214 ARG   B CA    1 
ATOM   2952 C  C     . ARG   B 1 188 ? 26.199  7.975   53.028 1.00 23.26 ? 214 ARG   B C     1 
ATOM   2953 O  O     . ARG   B 1 188 ? 26.794  9.011   52.731 1.00 23.27 ? 214 ARG   B O     1 
ATOM   2954 C  CB    . ARG   B 1 188 ? 27.555  6.034   53.793 1.00 26.78 ? 214 ARG   B CB    1 
ATOM   2955 C  CG    . ARG   B 1 188 ? 28.127  5.140   54.872 1.00 32.52 ? 214 ARG   B CG    1 
ATOM   2956 C  CD    . ARG   B 1 188 ? 29.082  5.884   55.782 1.00 37.02 ? 214 ARG   B CD    1 
ATOM   2957 N  NE    . ARG   B 1 188 ? 29.692  5.008   56.779 1.00 40.28 ? 214 ARG   B NE    1 
ATOM   2958 C  CZ    . ARG   B 1 188 ? 30.954  4.598   56.743 1.00 44.03 ? 214 ARG   B CZ    1 
ATOM   2959 N  NH1   . ARG   B 1 188 ? 31.759  4.987   55.761 1.00 45.18 ? 214 ARG   B NH1   1 
ATOM   2960 N  NH2   . ARG   B 1 188 ? 31.429  3.806   57.699 1.00 43.39 ? 214 ARG   B NH2   1 
ATOM   2961 N  N     . PHE   B 1 189 ? 25.208  7.451   52.263 1.00 22.10 ? 215 PHE   B N     1 
ATOM   2962 C  CA    . PHE   B 1 189 ? 24.693  8.056   51.036 1.00 21.54 ? 215 PHE   B CA    1 
ATOM   2963 C  C     . PHE   B 1 189 ? 23.179  7.916   50.987 1.00 20.98 ? 215 PHE   B C     1 
ATOM   2964 O  O     . PHE   B 1 189 ? 22.615  7.005   51.584 1.00 20.22 ? 215 PHE   B O     1 
ATOM   2965 C  CB    . PHE   B 1 189 ? 25.267  7.374   49.762 1.00 21.84 ? 215 PHE   B CB    1 
ATOM   2966 C  CG    . PHE   B 1 189 ? 26.739  7.045   49.766 1.00 23.54 ? 215 PHE   B CG    1 
ATOM   2967 C  CD1   . PHE   B 1 189 ? 27.684  8.015   49.486 1.00 24.90 ? 215 PHE   B CD1   1 
ATOM   2968 C  CD2   . PHE   B 1 189 ? 27.178  5.764   50.043 1.00 24.60 ? 215 PHE   B CD2   1 
ATOM   2969 C  CE1   . PHE   B 1 189 ? 29.050  7.716   49.538 1.00 25.82 ? 215 PHE   B CE1   1 
ATOM   2970 C  CE2   . PHE   B 1 189 ? 28.539  5.459   50.053 1.00 25.46 ? 215 PHE   B CE2   1 
ATOM   2971 C  CZ    . PHE   B 1 189 ? 29.466  6.433   49.796 1.00 25.18 ? 215 PHE   B CZ    1 
ATOM   2972 N  N     . VAL   B 1 190 ? 22.524  8.798   50.236 1.00 21.15 ? 216 VAL   B N     1 
ATOM   2973 C  CA    . VAL   B 1 190 ? 21.084  8.726   50.029 1.00 22.54 ? 216 VAL   B CA    1 
ATOM   2974 C  C     . VAL   B 1 190 ? 20.809  8.936   48.529 1.00 23.70 ? 216 VAL   B C     1 
ATOM   2975 O  O     . VAL   B 1 190 ? 21.562  9.640   47.843 1.00 24.00 ? 216 VAL   B O     1 
ATOM   2976 C  CB    . VAL   B 1 190 ? 20.294  9.757   50.892 1.00 23.46 ? 216 VAL   B CB    1 
ATOM   2977 C  CG1   . VAL   B 1 190 ? 20.250  9.358   52.366 1.00 23.98 ? 216 VAL   B CG1   1 
ATOM   2978 C  CG2   . VAL   B 1 190 ? 20.853  11.169  50.732 1.00 24.13 ? 216 VAL   B CG2   1 
ATOM   2979 N  N     . VAL   B 1 191 ? 19.709  8.367   48.025 1.00 24.12 ? 217 VAL   B N     1 
ATOM   2980 C  CA    . VAL   B 1 191 ? 19.292  8.620   46.643 1.00 24.78 ? 217 VAL   B CA    1 
ATOM   2981 C  C     . VAL   B 1 191 ? 17.757  8.687   46.523 1.00 24.75 ? 217 VAL   B C     1 
ATOM   2982 O  O     . VAL   B 1 191 ? 17.218  9.338   45.593 1.00 24.87 ? 217 VAL   B O     1 
ATOM   2983 C  CB    . VAL   B 1 191 ? 19.911  7.627   45.656 1.00 26.12 ? 217 VAL   B CB    1 
ATOM   2984 C  CG1   . VAL   B 1 191 ? 19.397  6.229   45.916 1.00 26.58 ? 217 VAL   B CG1   1 
ATOM   2985 C  CG2   . VAL   B 1 191 ? 19.600  8.047   44.234 1.00 27.44 ? 217 VAL   B CG2   1 
ATOM   2986 O  OXT   . VAL   B 1 191 ? 17.088  8.084   47.375 1.00 24.43 ? 217 VAL   B OXT   1 
HETATM 2987 P  PA    . M7G   C 2 .   ? -11.824 -14.646 23.766 1.00 44.82 ? 301 M7G   A PA    1 
HETATM 2988 O  O1A   . M7G   C 2 .   ? -12.027 -13.327 24.390 1.00 45.24 ? 301 M7G   A O1A   1 
HETATM 2989 O  O2A   . M7G   C 2 .   ? -10.379 -14.956 23.334 1.00 44.30 ? 301 M7G   A O2A   1 
HETATM 2990 O  O3A   . M7G   C 2 .   ? -12.284 -15.798 24.765 1.00 46.11 ? 301 M7G   A O3A   1 
HETATM 2991 O  "O5'" . M7G   C 2 .   ? -12.776 -14.835 22.494 1.00 43.68 ? 301 M7G   A "O5'" 1 
HETATM 2992 P  PB    . M7G   C 2 .   ? -13.415 -15.940 25.886 1.00 47.08 ? 301 M7G   A PB    1 
HETATM 2993 O  O1B   . M7G   C 2 .   ? -12.812 -16.266 27.217 1.00 47.00 ? 301 M7G   A O1B   1 
HETATM 2994 O  O2B   . M7G   C 2 .   ? -14.360 -17.017 25.345 1.00 47.25 ? 301 M7G   A O2B   1 
HETATM 2995 O  O3B   . M7G   C 2 .   ? -14.154 -14.607 25.872 1.00 47.46 ? 301 M7G   A O3B   1 
HETATM 2996 C  "C5'" . M7G   C 2 .   ? -14.214 -14.717 22.566 1.00 42.24 ? 301 M7G   A "C5'" 1 
HETATM 2997 C  "C4'" . M7G   C 2 .   ? -14.695 -14.002 21.330 1.00 40.61 ? 301 M7G   A "C4'" 1 
HETATM 2998 O  "O4'" . M7G   C 2 .   ? -13.914 -12.803 21.133 1.00 39.00 ? 301 M7G   A "O4'" 1 
HETATM 2999 C  "C3'" . M7G   C 2 .   ? -14.526 -14.779 20.033 1.00 40.31 ? 301 M7G   A "C3'" 1 
HETATM 3000 O  "O3'" . M7G   C 2 .   ? -15.587 -15.709 19.845 1.00 41.25 ? 301 M7G   A "O3'" 1 
HETATM 3001 C  "C2'" . M7G   C 2 .   ? -14.520 -13.657 18.999 1.00 39.12 ? 301 M7G   A "C2'" 1 
HETATM 3002 O  "O2'" . M7G   C 2 .   ? -15.837 -13.194 18.709 1.00 39.90 ? 301 M7G   A "O2'" 1 
HETATM 3003 C  "C1'" . M7G   C 2 .   ? -13.741 -12.565 19.745 1.00 37.32 ? 301 M7G   A "C1'" 1 
HETATM 3004 N  N9    . M7G   C 2 .   ? -12.362 -12.548 19.312 1.00 33.83 ? 301 M7G   A N9    1 
HETATM 3005 C  C8    . M7G   C 2 .   ? -11.296 -12.771 20.273 1.00 32.59 ? 301 M7G   A C8    1 
HETATM 3006 N  N7    . M7G   C 2 .   ? -10.143 -12.774 19.425 1.00 31.42 ? 301 M7G   A N7    1 
HETATM 3007 C  CM7   . M7G   C 2 .   ? -8.828  -12.877 20.038 1.00 31.05 ? 301 M7G   A CM7   1 
HETATM 3008 C  C5    . M7G   C 2 .   ? -10.453 -12.175 18.213 1.00 30.65 ? 301 M7G   A C5    1 
HETATM 3009 C  C6    . M7G   C 2 .   ? -9.647  -11.745 17.119 1.00 29.46 ? 301 M7G   A C6    1 
HETATM 3010 O  O6    . M7G   C 2 .   ? -8.427  -11.794 17.005 1.00 28.75 ? 301 M7G   A O6    1 
HETATM 3011 N  N1    . M7G   C 2 .   ? -10.424 -11.158 16.135 1.00 29.02 ? 301 M7G   A N1    1 
HETATM 3012 C  C2    . M7G   C 2 .   ? -11.784 -10.963 16.197 1.00 29.41 ? 301 M7G   A C2    1 
HETATM 3013 N  N2    . M7G   C 2 .   ? -12.345 -10.315 15.176 1.00 29.21 ? 301 M7G   A N2    1 
HETATM 3014 N  N3    . M7G   C 2 .   ? -12.544 -11.354 17.223 1.00 30.28 ? 301 M7G   A N3    1 
HETATM 3015 C  C4    . M7G   C 2 .   ? -11.839 -11.964 18.186 1.00 31.56 ? 301 M7G   A C4    1 
HETATM 3016 C  C1    . A1A8P D 3 .   ? 25.718  -10.920 62.454 1.00 29.16 ? 301 A1A8P B C1    1 
HETATM 3017 C  C2    . A1A8P D 3 .   ? 23.928  -9.911  60.717 1.00 30.51 ? 301 A1A8P B C2    1 
HETATM 3018 C  C3    . A1A8P D 3 .   ? 23.734  -9.977  62.062 1.00 31.16 ? 301 A1A8P B C3    1 
HETATM 3019 C  C4    . A1A8P D 3 .   ? 21.844  -9.235  63.609 1.00 36.46 ? 301 A1A8P B C4    1 
HETATM 3020 C  C5    . A1A8P D 3 .   ? 22.200  -7.893  64.207 1.00 39.33 ? 301 A1A8P B C5    1 
HETATM 3021 C  C6    . A1A8P D 3 .   ? 23.255  -7.772  65.102 1.00 40.04 ? 301 A1A8P B C6    1 
HETATM 3022 C  C7    . A1A8P D 3 .   ? 23.644  -6.529  65.568 1.00 40.74 ? 301 A1A8P B C7    1 
HETATM 3023 N  N1    . A1A8P D 3 .   ? 26.631  -11.500 63.239 1.00 29.11 ? 301 A1A8P B N1    1 
HETATM 3024 N  N2    . A1A8P D 3 .   ? 24.582  -10.469 62.986 1.00 29.49 ? 301 A1A8P B N2    1 
HETATM 3025 N  N3    . A1A8P D 3 .   ? 22.490  -9.454  62.308 1.00 33.39 ? 301 A1A8P B N3    1 
HETATM 3026 N  N4    . A1A8P D 3 .   ? 22.780  -9.369  60.159 1.00 31.39 1 301 A1A8P B N4    1 
HETATM 3027 C  C8    . A1A8P D 3 .   ? 22.981  -5.390  65.142 1.00 41.76 ? 301 A1A8P B C8    1 
HETATM 3028 CL CL    . A1A8P D 3 .   ? 19.580  -15.169 55.002 1.00 30.21 ? 301 A1A8P B CL    1 
HETATM 3029 C  C19   . A1A8P D 3 .   ? 19.789  -13.699 55.919 1.00 29.48 ? 301 A1A8P B C19   1 
HETATM 3030 C  C18   . A1A8P D 3 .   ? 21.040  -13.111 55.963 1.00 29.12 ? 301 A1A8P B C18   1 
HETATM 3031 C  C20   . A1A8P D 3 .   ? 18.707  -13.173 56.604 1.00 29.31 ? 301 A1A8P B C20   1 
HETATM 3032 C  C21   . A1A8P D 3 .   ? 18.880  -12.035 57.380 1.00 29.45 ? 301 A1A8P B C21   1 
HETATM 3033 C  C22   . A1A8P D 3 .   ? 20.143  -11.469 57.432 1.00 29.53 ? 301 A1A8P B C22   1 
HETATM 3034 C  C17   . A1A8P D 3 .   ? 21.237  -11.968 56.741 1.00 29.19 ? 301 A1A8P B C17   1 
HETATM 3035 C  C16   . A1A8P D 3 .   ? 22.350  -11.133 57.115 1.00 29.54 ? 301 A1A8P B C16   1 
HETATM 3036 O  O4    . A1A8P D 3 .   ? 20.524  -10.390 58.211 1.00 30.06 ? 301 A1A8P B O4    1 
HETATM 3037 C  C15   . A1A8P D 3 .   ? 21.885  -10.222 57.986 1.00 30.14 ? 301 A1A8P B C15   1 
HETATM 3038 C  C14   . A1A8P D 3 .   ? 22.527  -9.086  58.738 1.00 30.89 ? 301 A1A8P B C14   1 
HETATM 3039 C  C     . A1A8P D 3 .   ? 25.153  -10.364 60.135 1.00 29.51 ? 301 A1A8P B C     1 
HETATM 3040 O  O     . A1A8P D 3 .   ? 25.494  -10.339 58.960 1.00 29.10 ? 301 A1A8P B O     1 
HETATM 3041 C  C13   . A1A8P D 3 .   ? 21.930  -9.104  61.145 1.00 32.25 ? 301 A1A8P B C13   1 
HETATM 3042 N  N     . A1A8P D 3 .   ? 26.001  -10.863 61.111 1.00 29.12 ? 301 A1A8P B N     1 
HETATM 3043 C  C12   . A1A8P D 3 .   ? 21.533  -6.740  63.800 1.00 41.10 ? 301 A1A8P B C12   1 
HETATM 3044 C  C9    . A1A8P D 3 .   ? 21.924  -5.480  64.246 1.00 42.91 ? 301 A1A8P B C9    1 
HETATM 3045 C  C10   . A1A8P D 3 .   ? 21.270  -4.235  63.695 1.00 45.90 ? 301 A1A8P B C10   1 
HETATM 3046 C  C11   . A1A8P D 3 .   ? 19.751  -4.246  63.768 1.00 48.87 ? 301 A1A8P B C11   1 
HETATM 3047 P  P     . A1A8P D 3 .   ? 18.905  -4.598  62.237 1.00 51.82 ? 301 A1A8P B P     1 
HETATM 3048 O  O3    . A1A8P D 3 .   ? 17.888  -5.682  62.423 1.00 52.19 ? 301 A1A8P B O3    1 
HETATM 3049 O  O2    . A1A8P D 3 .   ? 18.275  -3.263  61.772 1.00 51.93 ? 301 A1A8P B O2    1 
HETATM 3050 O  O1    . A1A8P D 3 .   ? 19.959  -4.986  61.170 1.00 52.40 ? 301 A1A8P B O1    1 
HETATM 3051 O  O     . HOH   E 4 .   ? 40.877  4.495   32.085 1.00 34.00 ? 401 HOH   A O     1 
HETATM 3052 O  O     . HOH   E 4 .   ? 15.752  -1.875  20.477 1.00 40.75 ? 402 HOH   A O     1 
HETATM 3053 O  O     . HOH   E 4 .   ? 14.333  -16.562 14.580 1.00 38.29 ? 403 HOH   A O     1 
HETATM 3054 O  O     . HOH   E 4 .   ? -1.847  -13.435 40.734 1.00 35.76 ? 404 HOH   A O     1 
HETATM 3055 O  O     . HOH   E 4 .   ? -15.579 -16.458 13.655 1.00 24.76 ? 405 HOH   A O     1 
HETATM 3056 O  O     . HOH   E 4 .   ? 12.280  -15.145 21.382 1.00 28.93 ? 406 HOH   A O     1 
HETATM 3057 O  O     . HOH   E 4 .   ? -5.043  -15.637 26.217 1.00 17.02 ? 407 HOH   A O     1 
HETATM 3058 O  O     . HOH   E 4 .   ? -6.201  -25.967 16.237 1.00 23.24 ? 408 HOH   A O     1 
HETATM 3059 O  O     . HOH   E 4 .   ? 1.819   -4.021  36.554 1.00 26.36 ? 409 HOH   A O     1 
HETATM 3060 O  O     . HOH   E 4 .   ? -13.068 -9.349  11.633 1.00 44.14 ? 410 HOH   A O     1 
HETATM 3061 O  O     . HOH   E 4 .   ? 1.577   -6.850  10.943 1.00 21.71 ? 411 HOH   A O     1 
HETATM 3062 O  O     . HOH   E 4 .   ? 12.508  -22.736 29.729 1.00 24.42 ? 412 HOH   A O     1 
HETATM 3063 O  O     . HOH   E 4 .   ? 4.896   -22.300 38.576 1.00 36.50 ? 413 HOH   A O     1 
HETATM 3064 O  O     . HOH   E 4 .   ? 10.812  -20.977 12.103 1.00 42.41 ? 414 HOH   A O     1 
HETATM 3065 O  O     . HOH   E 4 .   ? 11.461  2.915   24.682 1.00 20.12 ? 415 HOH   A O     1 
HETATM 3066 O  O     . HOH   E 4 .   ? 15.870  -8.140  24.295 1.00 21.16 ? 416 HOH   A O     1 
HETATM 3067 O  O     . HOH   E 4 .   ? 15.193  -19.579 27.043 1.00 43.91 ? 417 HOH   A O     1 
HETATM 3068 O  O     . HOH   E 4 .   ? -0.289  -15.487 16.106 1.00 13.84 ? 418 HOH   A O     1 
HETATM 3069 O  O     . HOH   E 4 .   ? -4.244  -25.548 26.629 1.00 26.91 ? 419 HOH   A O     1 
HETATM 3070 O  O     . HOH   E 4 .   ? 1.831   -4.285  18.463 1.00 13.84 ? 420 HOH   A O     1 
HETATM 3071 O  O     . HOH   E 4 .   ? -9.928  -24.449 10.186 1.00 46.28 ? 421 HOH   A O     1 
HETATM 3072 O  O     . HOH   E 4 .   ? 4.421   -8.010  40.058 1.00 30.07 ? 422 HOH   A O     1 
HETATM 3073 O  O     . HOH   E 4 .   ? -9.152  -16.660 25.017 1.00 29.86 ? 423 HOH   A O     1 
HETATM 3074 O  O     . HOH   E 4 .   ? 4.888   -20.453 14.339 1.00 15.89 ? 424 HOH   A O     1 
HETATM 3075 O  O     . HOH   E 4 .   ? 12.484  1.965   34.827 1.00 16.61 ? 425 HOH   A O     1 
HETATM 3076 O  O     . HOH   E 4 .   ? 14.785  -29.803 11.624 1.00 39.48 ? 426 HOH   A O     1 
HETATM 3077 O  O     . HOH   E 4 .   ? -4.095  -20.063 11.564 1.00 21.69 ? 427 HOH   A O     1 
HETATM 3078 O  O     . HOH   E 4 .   ? 3.621   -15.453 8.972  1.00 44.39 ? 428 HOH   A O     1 
HETATM 3079 O  O     . HOH   E 4 .   ? 7.521   3.238   29.636 1.00 32.07 ? 429 HOH   A O     1 
HETATM 3080 O  O     . HOH   E 4 .   ? -7.189  -8.535  23.604 1.00 41.74 ? 430 HOH   A O     1 
HETATM 3081 O  O     . HOH   E 4 .   ? -10.214 -16.498 21.132 1.00 28.51 ? 431 HOH   A O     1 
HETATM 3082 O  O     . HOH   E 4 .   ? -5.540  -6.928  24.497 1.00 24.13 ? 432 HOH   A O     1 
HETATM 3083 O  O     . HOH   E 4 .   ? 1.968   -9.324  36.335 1.00 31.30 ? 433 HOH   A O     1 
HETATM 3084 O  O     . HOH   E 4 .   ? 0.404   -15.573 10.045 1.00 26.64 ? 434 HOH   A O     1 
HETATM 3085 O  O     . HOH   E 4 .   ? 13.077  -7.917  22.695 1.00 16.14 ? 435 HOH   A O     1 
HETATM 3086 O  O     . HOH   E 4 .   ? -6.525  -18.800 18.702 1.00 26.48 ? 436 HOH   A O     1 
HETATM 3087 O  O     . HOH   E 4 .   ? 15.344  -21.108 23.577 1.00 26.14 ? 437 HOH   A O     1 
HETATM 3088 O  O     . HOH   E 4 .   ? 13.717  -26.135 34.520 1.00 40.48 ? 438 HOH   A O     1 
HETATM 3089 O  O     . HOH   E 4 .   ? 8.009   -35.992 10.919 1.00 42.44 ? 439 HOH   A O     1 
HETATM 3090 O  O     . HOH   E 4 .   ? 10.620  -12.993 21.776 1.00 28.01 ? 440 HOH   A O     1 
HETATM 3091 O  O     . HOH   E 4 .   ? -0.182  -8.127  35.402 1.00 27.28 ? 441 HOH   A O     1 
HETATM 3092 O  O     . HOH   E 4 .   ? -15.034 -6.120  15.241 1.00 27.62 ? 442 HOH   A O     1 
HETATM 3093 O  O     . HOH   E 4 .   ? 39.230  0.329   37.761 1.00 36.64 ? 443 HOH   A O     1 
HETATM 3094 O  O     . HOH   E 4 .   ? 21.843  2.453   34.121 1.00 26.12 ? 444 HOH   A O     1 
HETATM 3095 O  O     . HOH   E 4 .   ? 10.524  -22.648 35.997 1.00 22.04 ? 445 HOH   A O     1 
HETATM 3096 O  O     . HOH   E 4 .   ? 28.513  6.116   31.100 1.00 33.99 ? 446 HOH   A O     1 
HETATM 3097 O  O     . HOH   E 4 .   ? -10.130 -22.570 23.718 1.00 43.26 ? 447 HOH   A O     1 
HETATM 3098 O  O     . HOH   E 4 .   ? 8.778   4.288   23.435 1.00 40.55 ? 448 HOH   A O     1 
HETATM 3099 O  O     . HOH   E 4 .   ? -5.247  -15.650 23.451 1.00 17.98 ? 449 HOH   A O     1 
HETATM 3100 O  O     . HOH   E 4 .   ? 13.043  -21.753 32.137 1.00 27.83 ? 450 HOH   A O     1 
HETATM 3101 O  O     . HOH   E 4 .   ? 9.407   2.755   21.369 1.00 39.18 ? 451 HOH   A O     1 
HETATM 3102 O  O     . HOH   E 4 .   ? 2.167   -2.058  16.936 1.00 23.45 ? 452 HOH   A O     1 
HETATM 3103 O  O     . HOH   E 4 .   ? -2.830  -3.211  40.397 1.00 29.01 ? 453 HOH   A O     1 
HETATM 3104 O  O     . HOH   E 4 .   ? -11.322 -7.136  9.914  1.00 40.95 ? 454 HOH   A O     1 
HETATM 3105 O  O     . HOH   E 4 .   ? 10.695  -15.261 32.156 1.00 20.21 ? 455 HOH   A O     1 
HETATM 3106 O  O     . HOH   E 4 .   ? -7.682  -16.303 20.156 1.00 24.20 ? 456 HOH   A O     1 
HETATM 3107 O  O     . HOH   E 4 .   ? 0.981   -1.440  39.839 1.00 54.91 ? 457 HOH   A O     1 
HETATM 3108 O  O     . HOH   E 4 .   ? 0.417   -27.926 32.979 1.00 39.71 ? 458 HOH   A O     1 
HETATM 3109 O  O     . HOH   E 4 .   ? 4.327   4.956   23.267 1.00 41.65 ? 459 HOH   A O     1 
HETATM 3110 O  O     . HOH   E 4 .   ? 13.906  -13.667 29.809 1.00 54.56 ? 460 HOH   A O     1 
HETATM 3111 O  O     . HOH   E 4 .   ? -3.306  -25.095 30.876 1.00 42.45 ? 461 HOH   A O     1 
HETATM 3112 O  O     . HOH   E 4 .   ? 11.416  -28.435 18.318 1.00 37.31 ? 462 HOH   A O     1 
HETATM 3113 O  O     . HOH   E 4 .   ? 0.421   -5.795  31.776 1.00 20.19 ? 463 HOH   A O     1 
HETATM 3114 O  O     . HOH   E 4 .   ? 0.205   -5.623  34.683 1.00 22.99 ? 464 HOH   A O     1 
HETATM 3115 O  O     . HOH   E 4 .   ? 0.898   -14.551 41.128 1.00 34.13 ? 465 HOH   A O     1 
HETATM 3116 O  O     . HOH   E 4 .   ? -6.422  -10.426 21.809 1.00 36.81 ? 466 HOH   A O     1 
HETATM 3117 O  O     . HOH   E 4 .   ? 15.826  -6.314  33.657 1.00 30.00 ? 467 HOH   A O     1 
HETATM 3118 O  O     . HOH   E 4 .   ? 16.881  -22.214 19.119 1.00 50.30 ? 468 HOH   A O     1 
HETATM 3119 O  O     . HOH   E 4 .   ? -10.195 -24.138 19.400 1.00 50.90 ? 469 HOH   A O     1 
HETATM 3120 O  O     . HOH   E 4 .   ? -3.835  -21.353 9.411  1.00 32.33 ? 470 HOH   A O     1 
HETATM 3121 O  O     . HOH   E 4 .   ? 4.398   -10.997 40.486 1.00 41.01 ? 471 HOH   A O     1 
HETATM 3122 O  O     . HOH   E 4 .   ? -12.354 -19.039 21.930 1.00 43.12 ? 472 HOH   A O     1 
HETATM 3123 O  O     . HOH   E 4 .   ? 0.201   -1.067  15.472 1.00 35.81 ? 473 HOH   A O     1 
HETATM 3124 O  O     . HOH   E 4 .   ? 9.727   6.125   35.584 1.00 41.42 ? 474 HOH   A O     1 
HETATM 3125 O  O     . HOH   F 4 .   ? 16.525  -30.251 20.868 1.00 43.02 ? 401 HOH   B O     1 
HETATM 3126 O  O     . HOH   F 4 .   ? 30.602  -1.183  46.942 1.00 17.20 ? 402 HOH   B O     1 
HETATM 3127 O  O     . HOH   F 4 .   ? 28.820  -9.233  38.841 1.00 29.73 ? 403 HOH   B O     1 
HETATM 3128 O  O     . HOH   F 4 .   ? 31.208  -15.589 43.147 1.00 30.92 ? 404 HOH   B O     1 
HETATM 3129 O  O     . HOH   F 4 .   ? 26.685  -17.490 48.608 1.00 11.97 ? 405 HOH   B O     1 
HETATM 3130 O  O     . HOH   F 4 .   ? 33.733  -14.591 50.253 1.00 29.22 ? 406 HOH   B O     1 
HETATM 3131 O  O     . HOH   F 4 .   ? 22.670  -24.181 37.511 1.00 22.34 ? 407 HOH   B O     1 
HETATM 3132 O  O     . HOH   F 4 .   ? 17.049  -6.574  54.281 1.00 20.05 ? 408 HOH   B O     1 
HETATM 3133 O  O     . HOH   F 4 .   ? 26.458  4.078   57.404 1.00 33.55 ? 409 HOH   B O     1 
HETATM 3134 O  O     . HOH   F 4 .   ? 31.354  -1.891  56.429 1.00 22.12 ? 410 HOH   B O     1 
HETATM 3135 O  O     . HOH   F 4 .   ? 8.773   -12.466 44.694 1.00 21.12 ? 411 HOH   B O     1 
HETATM 3136 O  O     . HOH   F 4 .   ? 14.920  1.239   35.430 1.00 29.19 ? 412 HOH   B O     1 
HETATM 3137 O  O     . HOH   F 4 .   ? 33.153  -16.834 52.140 1.00 44.90 ? 413 HOH   B O     1 
HETATM 3138 O  O     . HOH   F 4 .   ? 11.950  5.612   41.422 1.00 32.45 ? 414 HOH   B O     1 
HETATM 3139 O  O     . HOH   F 4 .   ? 33.012  5.589   37.926 1.00 47.78 ? 415 HOH   B O     1 
HETATM 3140 O  O     . HOH   F 4 .   ? 9.885   -25.029 39.615 1.00 27.18 ? 416 HOH   B O     1 
HETATM 3141 O  O     . HOH   F 4 .   ? 12.940  -22.973 34.521 1.00 21.18 ? 417 HOH   B O     1 
HETATM 3142 O  O     . HOH   F 4 .   ? 18.770  -5.609  33.528 1.00 34.60 ? 418 HOH   B O     1 
HETATM 3143 O  O     . HOH   F 4 .   ? 17.009  -24.514 40.431 1.00 27.57 ? 419 HOH   B O     1 
HETATM 3144 O  O     . HOH   F 4 .   ? 24.512  -13.334 37.116 1.00 10.14 ? 420 HOH   B O     1 
HETATM 3145 O  O     . HOH   F 4 .   ? 31.472  -10.034 40.981 1.00 39.10 ? 421 HOH   B O     1 
HETATM 3146 O  O     . HOH   F 4 .   ? 23.624  -12.832 33.821 1.00 16.03 ? 422 HOH   B O     1 
HETATM 3147 O  O     . HOH   F 4 .   ? 16.725  6.850   41.322 1.00 28.72 ? 423 HOH   B O     1 
HETATM 3148 O  O     . HOH   F 4 .   ? 23.078  0.407   34.809 1.00 31.33 ? 424 HOH   B O     1 
HETATM 3149 O  O     . HOH   F 4 .   ? 30.687  -12.885 64.486 1.00 43.55 ? 425 HOH   B O     1 
HETATM 3150 O  O     . HOH   F 4 .   ? 12.923  4.754   33.943 1.00 39.46 ? 426 HOH   B O     1 
HETATM 3151 O  O     . HOH   F 4 .   ? 28.012  -6.275  51.755 1.00 12.76 ? 427 HOH   B O     1 
HETATM 3152 O  O     . HOH   F 4 .   ? 23.988  -3.393  57.188 1.00 25.20 ? 428 HOH   B O     1 
HETATM 3153 O  O     . HOH   F 4 .   ? 31.507  -19.845 41.267 1.00 41.98 ? 429 HOH   B O     1 
HETATM 3154 O  O     . HOH   F 4 .   ? 25.869  -6.105  32.888 1.00 37.19 ? 430 HOH   B O     1 
HETATM 3155 O  O     . HOH   F 4 .   ? 16.562  -5.336  36.116 1.00 27.27 ? 431 HOH   B O     1 
HETATM 3156 O  O     . HOH   F 4 .   ? 31.354  5.763   53.121 1.00 35.03 ? 432 HOH   B O     1 
HETATM 3157 O  O     . HOH   F 4 .   ? 19.013  3.083   55.444 1.00 35.32 ? 433 HOH   B O     1 
HETATM 3158 O  O     . HOH   F 4 .   ? 10.516  1.606   36.840 1.00 23.82 ? 434 HOH   B O     1 
HETATM 3159 O  O     . HOH   F 4 .   ? 20.076  -6.593  54.979 1.00 23.65 ? 435 HOH   B O     1 
HETATM 3160 O  O     . HOH   F 4 .   ? 16.595  3.451   53.551 1.00 34.98 ? 436 HOH   B O     1 
HETATM 3161 O  O     . HOH   F 4 .   ? 34.313  -6.085  52.018 1.00 27.29 ? 437 HOH   B O     1 
HETATM 3162 O  O     . HOH   F 4 .   ? 33.416  -2.355  38.650 1.00 34.81 ? 438 HOH   B O     1 
HETATM 3163 O  O     . HOH   F 4 .   ? 32.868  -23.839 41.617 1.00 52.54 ? 439 HOH   B O     1 
HETATM 3164 O  O     . HOH   F 4 .   ? 23.772  -6.767  39.982 1.00 17.00 ? 440 HOH   B O     1 
HETATM 3165 O  O     . HOH   F 4 .   ? 19.945  -2.181  33.303 1.00 36.63 ? 441 HOH   B O     1 
HETATM 3166 O  O     . HOH   F 4 .   ? 3.722   -7.686  44.873 1.00 33.37 ? 442 HOH   B O     1 
HETATM 3167 O  O     . HOH   F 4 .   ? 14.464  -5.755  37.781 1.00 19.17 ? 443 HOH   B O     1 
HETATM 3168 O  O     . HOH   F 4 .   ? 23.305  -5.526  32.053 1.00 50.83 ? 444 HOH   B O     1 
HETATM 3169 O  O     . HOH   F 4 .   ? 21.873  1.635   62.144 1.00 50.60 ? 445 HOH   B O     1 
HETATM 3170 O  O     . HOH   F 4 .   ? 19.096  9.925   56.238 1.00 53.46 ? 446 HOH   B O     1 
HETATM 3171 O  O     . HOH   F 4 .   ? 22.453  5.873   65.609 1.00 46.19 ? 447 HOH   B O     1 
HETATM 3172 O  O     . HOH   F 4 .   ? 31.363  -8.453  44.932 1.00 36.68 ? 448 HOH   B O     1 
HETATM 3173 O  O     . HOH   F 4 .   ? 18.682  -27.954 61.629 1.00 39.81 ? 449 HOH   B O     1 
HETATM 3174 O  O     . HOH   F 4 .   ? 19.025  -24.268 42.313 1.00 46.47 ? 450 HOH   B O     1 
HETATM 3175 O  O     . HOH   F 4 .   ? 33.293  3.476   43.032 1.00 35.34 ? 451 HOH   B O     1 
HETATM 3176 O  O     . HOH   F 4 .   ? 8.585   -8.738  63.783 1.00 45.54 ? 452 HOH   B O     1 
HETATM 3177 O  O     . HOH   F 4 .   ? 12.454  -3.956  38.010 1.00 24.69 ? 453 HOH   B O     1 
HETATM 3178 O  O     . HOH   F 4 .   ? 34.371  5.899   43.790 1.00 45.55 ? 454 HOH   B O     1 
HETATM 3179 O  O     . HOH   F 4 .   ? 27.649  -19.503 34.729 1.00 44.07 ? 455 HOH   B O     1 
HETATM 3180 O  O     . HOH   F 4 .   ? 21.748  9.557   58.027 1.00 36.45 ? 456 HOH   B O     1 
HETATM 3181 O  O     . HOH   F 4 .   ? 24.441  10.881  49.169 1.00 28.29 ? 457 HOH   B O     1 
HETATM 3182 O  O     . HOH   F 4 .   ? 22.748  -26.843 44.609 1.00 36.27 ? 458 HOH   B O     1 
HETATM 3183 O  O     . HOH   F 4 .   ? 30.324  -16.536 40.093 1.00 42.85 ? 459 HOH   B O     1 
HETATM 3184 O  O     . HOH   F 4 .   ? 14.819  -13.984 32.491 1.00 26.22 ? 460 HOH   B O     1 
HETATM 3185 O  O     . HOH   F 4 .   ? 29.393  -26.080 45.858 1.00 51.51 ? 461 HOH   B O     1 
HETATM 3186 O  O     . HOH   F 4 .   ? 32.759  -8.301  60.190 1.00 36.61 ? 462 HOH   B O     1 
HETATM 3187 O  O     . HOH   F 4 .   ? 28.041  -19.687 48.410 1.00 27.03 ? 463 HOH   B O     1 
HETATM 3188 O  O     . HOH   F 4 .   ? 3.449   -8.968  48.035 1.00 32.68 ? 464 HOH   B O     1 
HETATM 3189 O  O     . HOH   F 4 .   ? 25.189  -8.663  40.347 1.00 20.70 ? 465 HOH   B O     1 
HETATM 3190 O  O     . HOH   F 4 .   ? 26.269  -22.121 33.547 1.00 37.10 ? 466 HOH   B O     1 
HETATM 3191 O  O     . HOH   F 4 .   ? 35.497  0.276   54.615 1.00 47.36 ? 467 HOH   B O     1 
HETATM 3192 O  O     . HOH   F 4 .   ? 34.140  -14.712 47.481 1.00 56.55 ? 468 HOH   B O     1 
HETATM 3193 O  O     . HOH   F 4 .   ? 32.188  -19.192 51.584 1.00 38.77 ? 469 HOH   B O     1 
HETATM 3194 O  O     . HOH   F 4 .   ? 28.772  -7.498  35.139 1.00 47.58 ? 470 HOH   B O     1 
HETATM 3195 O  O     . HOH   F 4 .   ? 18.347  -11.702 61.002 1.00 44.18 ? 471 HOH   B O     1 
HETATM 3196 O  O     . HOH   F 4 .   ? 2.751   -6.174  41.827 1.00 47.16 ? 472 HOH   B O     1 
HETATM 3197 O  O     . HOH   F 4 .   ? 2.505   -3.540  39.681 1.00 38.26 ? 473 HOH   B O     1 
HETATM 3198 O  O     . HOH   F 4 .   ? 9.645   4.110   37.170 1.00 32.68 ? 474 HOH   B O     1 
HETATM 3199 O  O     . HOH   F 4 .   ? 10.836  5.653   38.988 1.00 54.21 ? 475 HOH   B O     1 
HETATM 3200 O  O     . HOH   F 4 .   ? 33.724  -0.440  56.621 1.00 29.91 ? 476 HOH   B O     1 
HETATM 3201 O  O     . HOH   F 4 .   ? 26.539  12.728  51.569 1.00 53.39 ? 477 HOH   B 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   . MET A 1   ? 0.4765 0.7318 0.7212 -0.0376 -0.0815 -0.1348 27  MET A N   
2    C CA  . MET A 1   ? 0.4724 0.7302 0.7300 -0.0558 -0.0794 -0.1310 27  MET A CA  
3    C C   . MET A 1   ? 0.4656 0.7252 0.7189 -0.0650 -0.0679 -0.1210 27  MET A C   
4    O O   . MET A 1   ? 0.4716 0.7183 0.7231 -0.0773 -0.0662 -0.1128 27  MET A O   
5    C CB  . MET A 1   ? 0.4715 0.7540 0.7526 -0.0622 -0.0826 -0.1399 27  MET A CB  
6    C CG  . MET A 1   ? 0.4983 0.8094 0.7904 -0.0607 -0.0764 -0.1441 27  MET A CG  
7    S SD  . MET A 1   ? 0.6037 0.9407 0.9226 -0.0807 -0.0731 -0.1457 27  MET A SD  
8    C CE  . MET A 1   ? 0.5902 0.9210 0.9012 -0.0959 -0.0607 -0.1311 27  MET A CE  
9    N N   . VAL A 2   ? 0.4473 0.7250 0.7012 -0.0559 -0.0633 -0.1251 28  VAL A N   
10   C CA  . VAL A 2   ? 0.4496 0.7267 0.6952 -0.0618 -0.0525 -0.1159 28  VAL A CA  
11   C C   . VAL A 2   ? 0.4629 0.7177 0.6861 -0.0498 -0.0521 -0.1111 28  VAL A C   
12   O O   . VAL A 2   ? 0.4756 0.7153 0.6874 -0.0556 -0.0475 -0.1016 28  VAL A O   
13   C CB  . VAL A 2   ? 0.4457 0.7513 0.7020 -0.0633 -0.0445 -0.1195 28  VAL A CB  
14   C CG1 . VAL A 2   ? 0.4579 0.7614 0.7029 -0.0676 -0.0342 -0.1108 28  VAL A CG1 
15   C CG2 . VAL A 2   ? 0.4401 0.7699 0.7192 -0.0765 -0.0440 -0.1237 28  VAL A CG2 
16   N N   . ALA A 3   ? 0.4607 0.7066 0.6747 -0.0422 -0.0533 -0.1107 29  ALA A N   
17   C CA  . ALA A 3   ? 0.4729 0.6979 0.6665 -0.0335 -0.0522 -0.1049 29  ALA A CA  
18   C C   . ALA A 3   ? 0.4795 0.6806 0.6636 -0.0322 -0.0590 -0.1023 29  ALA A C   
19   O O   . ALA A 3   ? 0.4898 0.6831 0.6666 -0.0202 -0.0653 -0.1065 29  ALA A O   
20   C CB  . ALA A 3   ? 0.4786 0.7083 0.6667 -0.0177 -0.0535 -0.1102 29  ALA A CB  
21   N N   . ASN A 4   ? 0.4673 0.6571 0.6513 -0.0443 -0.0580 -0.0955 30  ASN A N   
22   C CA  . ASN A 4   ? 0.4638 0.6307 0.6394 -0.0429 -0.0643 -0.0935 30  ASN A CA  
23   C C   . ASN A 4   ? 0.4415 0.5929 0.5978 -0.0343 -0.0613 -0.0879 30  ASN A C   
24   O O   . ASN A 4   ? 0.4443 0.5966 0.5949 -0.0374 -0.0536 -0.0813 30  ASN A O   
25   C CB  . ASN A 4   ? 0.4924 0.6501 0.6730 -0.0580 -0.0642 -0.0869 30  ASN A CB  
26   C CG  . ASN A 4   ? 0.5487 0.7220 0.7489 -0.0698 -0.0657 -0.0903 30  ASN A CG  
27   O OD1 . ASN A 4   ? 0.5573 0.7436 0.7686 -0.0659 -0.0707 -0.0999 30  ASN A OD1 
28   N ND2 . ASN A 4   ? 0.5678 0.7409 0.7727 -0.0850 -0.0612 -0.0822 30  ASN A ND2 
29   N N   . PRO A 5   ? 0.4253 0.5631 0.5715 -0.0239 -0.0671 -0.0903 31  PRO A N   
30   C CA  . PRO A 5   ? 0.4240 0.5478 0.5524 -0.0162 -0.0640 -0.0848 31  PRO A CA  
31   C C   . PRO A 5   ? 0.4150 0.5244 0.5378 -0.0250 -0.0606 -0.0756 31  PRO A C   
32   O O   . PRO A 5   ? 0.4225 0.5219 0.5493 -0.0315 -0.0649 -0.0748 31  PRO A O   
33   C CB  . PRO A 5   ? 0.4396 0.5542 0.5605 -0.0051 -0.0716 -0.0900 31  PRO A CB  
34   C CG  . PRO A 5   ? 0.4415 0.5692 0.5755 -0.0042 -0.0781 -0.0994 31  PRO A CG  
35   C CD  . PRO A 5   ? 0.4144 0.5504 0.5645 -0.0185 -0.0766 -0.0987 31  PRO A CD  
36   N N   . GLU A 6   ? 0.3995 0.5085 0.5143 -0.0257 -0.0531 -0.0691 32  GLU A N   
37   C CA  . GLU A 6   ? 0.3967 0.4929 0.5049 -0.0333 -0.0497 -0.0599 32  GLU A CA  
38   C C   . GLU A 6   ? 0.3933 0.4726 0.4862 -0.0245 -0.0507 -0.0570 32  GLU A C   
39   O O   . GLU A 6   ? 0.4011 0.4815 0.4861 -0.0138 -0.0502 -0.0595 32  GLU A O   
40   C CB  . GLU A 6   ? 0.4198 0.5269 0.5278 -0.0395 -0.0409 -0.0546 32  GLU A CB  
41   N N   . HIS A 7   ? 0.3758 0.4397 0.4648 -0.0294 -0.0523 -0.0516 33  HIS A N   
42   C CA  . HIS A 7   ? 0.3753 0.4240 0.4514 -0.0225 -0.0531 -0.0486 33  HIS A CA  
43   C C   . HIS A 7   ? 0.3604 0.3979 0.4329 -0.0310 -0.0508 -0.0395 33  HIS A C   
44   O O   . HIS A 7   ? 0.3633 0.4016 0.4439 -0.0423 -0.0510 -0.0361 33  HIS A O   
45   C CB  . HIS A 7   ? 0.3945 0.4345 0.4699 -0.0153 -0.0610 -0.0551 33  HIS A CB  
46   C CG  . HIS A 7   ? 0.4275 0.4653 0.5153 -0.0222 -0.0676 -0.0589 33  HIS A CG  
47   N ND1 . HIS A 7   ? 0.4443 0.4958 0.5445 -0.0258 -0.0694 -0.0644 33  HIS A ND1 
48   C CD2 . HIS A 7   ? 0.4475 0.4707 0.5374 -0.0255 -0.0734 -0.0585 33  HIS A CD2 
49   C CE1 . HIS A 7   ? 0.4498 0.4944 0.5592 -0.0321 -0.0759 -0.0666 33  HIS A CE1 
50   N NE2 . HIS A 7   ? 0.4558 0.4827 0.5594 -0.0318 -0.0788 -0.0634 33  HIS A NE2 
51   N N   . TYR A 8   ? 0.3415 0.3692 0.4021 -0.0261 -0.0488 -0.0352 34  TYR A N   
52   C CA  . TYR A 8   ? 0.3389 0.3569 0.3951 -0.0331 -0.0467 -0.0264 34  TYR A CA  
53   C C   . TYR A 8   ? 0.3496 0.3508 0.3996 -0.0279 -0.0517 -0.0257 34  TYR A C   
54   O O   . TYR A 8   ? 0.3533 0.3530 0.3973 -0.0175 -0.0528 -0.0301 34  TYR A O   
55   C CB  . TYR A 8   ? 0.3348 0.3596 0.3833 -0.0335 -0.0386 -0.0213 34  TYR A CB  
56   C CG  . TYR A 8   ? 0.3385 0.3817 0.3931 -0.0353 -0.0340 -0.0246 34  TYR A CG  
57   C CD1 . TYR A 8   ? 0.3418 0.3946 0.4057 -0.0465 -0.0321 -0.0227 34  TYR A CD1 
58   C CD2 . TYR A 8   ? 0.3491 0.4005 0.4014 -0.0256 -0.0324 -0.0302 34  TYR A CD2 
59   C CE1 . TYR A 8   ? 0.3445 0.4161 0.4157 -0.0476 -0.0282 -0.0271 34  TYR A CE1 
60   C CE2 . TYR A 8   ? 0.3534 0.4218 0.4129 -0.0261 -0.0293 -0.0345 34  TYR A CE2 
61   C CZ  . TYR A 8   ? 0.3582 0.4375 0.4275 -0.0369 -0.0270 -0.0334 34  TYR A CZ  
62   O OH  . TYR A 8   ? 0.3691 0.4671 0.4466 -0.0369 -0.0240 -0.0386 34  TYR A OH  
63   N N   . ILE A 9   ? 0.3496 0.3388 0.4015 -0.0351 -0.0549 -0.0203 35  ILE A N   
64   C CA  . ILE A 9   ? 0.3591 0.3323 0.4072 -0.0305 -0.0604 -0.0202 35  ILE A CA  
65   C C   . ILE A 9   ? 0.3491 0.3192 0.3851 -0.0249 -0.0561 -0.0159 35  ILE A C   
66   O O   . ILE A 9   ? 0.3495 0.3128 0.3810 -0.0165 -0.0589 -0.0189 35  ILE A O   
67   C CB  . ILE A 9   ? 0.3812 0.3420 0.4358 -0.0407 -0.0658 -0.0149 35  ILE A CB  
68   C CG1 . ILE A 9   ? 0.4117 0.3558 0.4664 -0.0351 -0.0740 -0.0179 35  ILE A CG1 
69   C CG2 . ILE A 9   ? 0.3894 0.3494 0.4396 -0.0501 -0.0608 -0.0037 35  ILE A CG2 
70   C CD1 . ILE A 9   ? 0.4346 0.3791 0.4959 -0.0287 -0.0804 -0.0293 35  ILE A CD1 
71   N N   . LYS A 10  ? 0.3366 0.3131 0.3680 -0.0295 -0.0492 -0.0095 36  LYS A N   
72   C CA  . LYS A 10  ? 0.3351 0.3101 0.3561 -0.0256 -0.0449 -0.0053 36  LYS A CA  
73   C C   . LYS A 10  ? 0.3074 0.2960 0.3251 -0.0257 -0.0373 -0.0048 36  LYS A C   
74   O O   . LYS A 10  ? 0.2979 0.2964 0.3209 -0.0323 -0.0345 -0.0045 36  LYS A O   
75   C CB  . LYS A 10  ? 0.3860 0.3505 0.4041 -0.0322 -0.0460 0.0034  36  LYS A CB  
76   C CG  . LYS A 10  ? 0.4711 0.4203 0.4894 -0.0281 -0.0534 0.0027  36  LYS A CG  
77   C CD  . LYS A 10  ? 0.5486 0.4976 0.5607 -0.0164 -0.0529 -0.0021 36  LYS A CD  
78   C CE  . LYS A 10  ? 0.6059 0.5421 0.6170 -0.0124 -0.0585 -0.0016 36  LYS A CE  
79   N NZ  . LYS A 10  ? 0.6450 0.5772 0.6498 -0.0154 -0.0563 0.0066  36  LYS A NZ  
80   N N   . HIS A 11  ? 0.2919 0.2815 0.3015 -0.0184 -0.0341 -0.0052 37  HIS A N   
81   C CA  . HIS A 11  ? 0.2779 0.2783 0.2841 -0.0172 -0.0278 -0.0054 37  HIS A CA  
82   C C   . HIS A 11  ? 0.2840 0.2805 0.2819 -0.0182 -0.0244 0.0005  37  HIS A C   
83   O O   . HIS A 11  ? 0.2871 0.2783 0.2790 -0.0117 -0.0248 0.0005  37  HIS A O   
84   C CB  . HIS A 11  ? 0.2769 0.2814 0.2813 -0.0072 -0.0278 -0.0115 37  HIS A CB  
85   C CG  . HIS A 11  ? 0.2861 0.2959 0.2983 -0.0054 -0.0314 -0.0180 37  HIS A CG  
86   N ND1 . HIS A 11  ? 0.3013 0.3044 0.3164 -0.0032 -0.0375 -0.0213 37  HIS A ND1 
87   C CD2 . HIS A 11  ? 0.2863 0.3078 0.3039 -0.0050 -0.0301 -0.0222 37  HIS A CD2 
88   C CE1 . HIS A 11  ? 0.2899 0.3008 0.3119 -0.0020 -0.0397 -0.0272 37  HIS A CE1 
89   N NE2 . HIS A 11  ? 0.2854 0.3076 0.3093 -0.0029 -0.0355 -0.0278 37  HIS A NE2 
90   N N   . PRO A 12  ? 0.2819 0.2818 0.2791 -0.0266 -0.0212 0.0058  38  PRO A N   
91   C CA  . PRO A 12  ? 0.2807 0.2771 0.2695 -0.0277 -0.0186 0.0112  38  PRO A CA  
92   C C   . PRO A 12  ? 0.2719 0.2735 0.2552 -0.0215 -0.0143 0.0087  38  PRO A C   
93   O O   . PRO A 12  ? 0.2742 0.2851 0.2600 -0.0189 -0.0116 0.0040  38  PRO A O   
94   C CB  . PRO A 12  ? 0.2933 0.2945 0.2823 -0.0385 -0.0161 0.0169  38  PRO A CB  
95   C CG  . PRO A 12  ? 0.2993 0.3040 0.2980 -0.0441 -0.0183 0.0154  38  PRO A CG  
96   C CD  . PRO A 12  ? 0.2737 0.2817 0.2776 -0.0359 -0.0199 0.0070  38  PRO A CD  
97   N N   . LEU A 13  ? 0.2520 0.2472 0.2283 -0.0194 -0.0140 0.0120  39  LEU A N   
98   C CA  . LEU A 13  ? 0.2472 0.2453 0.2179 -0.0151 -0.0103 0.0109  39  LEU A CA  
99   C C   . LEU A 13  ? 0.2701 0.2748 0.2376 -0.0216 -0.0061 0.0138  39  LEU A C   
100  O O   . LEU A 13  ? 0.2767 0.2810 0.2441 -0.0292 -0.0067 0.0186  39  LEU A O   
101  C CB  . LEU A 13  ? 0.2324 0.2215 0.1981 -0.0107 -0.0123 0.0130  39  LEU A CB  
102  C CG  . LEU A 13  ? 0.2269 0.2106 0.1947 -0.0043 -0.0163 0.0101  39  LEU A CG  
103  C CD1 . LEU A 13  ? 0.2260 0.2029 0.1900 -0.0013 -0.0180 0.0124  39  LEU A CD1 
104  C CD2 . LEU A 13  ? 0.2228 0.2115 0.1914 0.0020  -0.0150 0.0049  39  LEU A CD2 
105  N N   . GLN A 14  ? 0.2695 0.2801 0.2341 -0.0188 -0.0023 0.0111  40  GLN A N   
106  C CA  . GLN A 14  ? 0.2824 0.3005 0.2434 -0.0242 0.0017  0.0125  40  GLN A CA  
107  C C   . GLN A 14  ? 0.2776 0.2893 0.2315 -0.0279 0.0007  0.0188  40  GLN A C   
108  O O   . GLN A 14  ? 0.2854 0.3026 0.2357 -0.0343 0.0030  0.0218  40  GLN A O   
109  C CB  . GLN A 14  ? 0.3336 0.3588 0.2941 -0.0197 0.0052  0.0068  40  GLN A CB  
110  C CG  . GLN A 14  ? 0.4200 0.4519 0.3878 -0.0156 0.0055  0.0006  40  GLN A CG  
111  C CD  . GLN A 14  ? 0.5390 0.5792 0.5072 -0.0124 0.0088  -0.0050 40  GLN A CD  
112  O OE1 . GLN A 14  ? 0.5828 0.6301 0.5481 -0.0163 0.0122  -0.0054 40  GLN A OE1 
113  N NE2 . GLN A 14  ? 0.5612 0.6006 0.5326 -0.0049 0.0075  -0.0099 40  GLN A NE2 
114  N N   . ASN A 15  ? 0.2629 0.2642 0.2147 -0.0237 -0.0027 0.0206  41  ASN A N   
115  C CA  . ASN A 15  ? 0.2618 0.2571 0.2080 -0.0260 -0.0046 0.0261  41  ASN A CA  
116  C C   . ASN A 15  ? 0.2505 0.2351 0.1988 -0.0242 -0.0101 0.0288  41  ASN A C   
117  O O   . ASN A 15  ? 0.2434 0.2253 0.1963 -0.0192 -0.0119 0.0253  41  ASN A O   
118  C CB  . ASN A 15  ? 0.2864 0.2813 0.2284 -0.0216 -0.0031 0.0241  41  ASN A CB  
119  C CG  . ASN A 15  ? 0.3468 0.3501 0.2848 -0.0242 0.0010  0.0224  41  ASN A CG  
120  O OD1 . ASN A 15  ? 0.3751 0.3815 0.3085 -0.0301 0.0016  0.0261  41  ASN A OD1 
121  N ND2 . ASN A 15  ? 0.3540 0.3610 0.2933 -0.0197 0.0035  0.0167  41  ASN A ND2 
122  N N   . ARG A 16  ? 0.2433 0.2221 0.1879 -0.0274 -0.0131 0.0344  42  ARG A N   
123  C CA  . ARG A 16  ? 0.2512 0.2196 0.1981 -0.0247 -0.0189 0.0364  42  ARG A CA  
124  C C   . ARG A 16  ? 0.2461 0.2130 0.1907 -0.0186 -0.0192 0.0349  42  ARG A C   
125  O O   . ARG A 16  ? 0.2519 0.2223 0.1916 -0.0199 -0.0168 0.0359  42  ARG A O   
126  C CB  . ARG A 16  ? 0.2761 0.2383 0.2209 -0.0311 -0.0230 0.0437  42  ARG A CB  
127  C CG  . ARG A 16  ? 0.3425 0.2931 0.2908 -0.0276 -0.0301 0.0450  42  ARG A CG  
128  C CD  . ARG A 16  ? 0.4310 0.3736 0.3768 -0.0336 -0.0352 0.0531  42  ARG A CD  
129  N NE  . ARG A 16  ? 0.5193 0.4570 0.4699 -0.0387 -0.0381 0.0552  42  ARG A NE  
130  C CZ  . ARG A 16  ? 0.5960 0.5384 0.5449 -0.0477 -0.0354 0.0595  42  ARG A CZ  
131  N NH1 . ARG A 16  ? 0.6006 0.5533 0.5426 -0.0520 -0.0297 0.0616  42  ARG A NH1 
132  N NH2 . ARG A 16  ? 0.6107 0.5484 0.5653 -0.0527 -0.0383 0.0614  42  ARG A NH2 
133  N N   . TRP A 17  ? 0.2304 0.1931 0.1789 -0.0124 -0.0219 0.0320  43  TRP A N   
134  C CA  . TRP A 17  ? 0.2280 0.1910 0.1755 -0.0070 -0.0216 0.0303  43  TRP A CA  
135  C C   . TRP A 17  ? 0.2410 0.1977 0.1912 -0.0038 -0.0271 0.0312  43  TRP A C   
136  O O   . TRP A 17  ? 0.2503 0.2012 0.2043 -0.0036 -0.0314 0.0312  43  TRP A O   
137  C CB  . TRP A 17  ? 0.2179 0.1849 0.1672 -0.0016 -0.0186 0.0250  43  TRP A CB  
138  C CG  . TRP A 17  ? 0.2058 0.1786 0.1534 -0.0033 -0.0139 0.0232  43  TRP A CG  
139  C CD1 . TRP A 17  ? 0.2067 0.1826 0.1566 -0.0051 -0.0128 0.0214  43  TRP A CD1 
140  C CD2 . TRP A 17  ? 0.1964 0.1730 0.1408 -0.0031 -0.0103 0.0225  43  TRP A CD2 
141  N NE1 . TRP A 17  ? 0.2042 0.1860 0.1524 -0.0056 -0.0086 0.0195  43  TRP A NE1 
142  C CE2 . TRP A 17  ? 0.1989 0.1803 0.1436 -0.0042 -0.0072 0.0200  43  TRP A CE2 
143  C CE3 . TRP A 17  ? 0.2013 0.1777 0.1432 -0.0021 -0.0097 0.0234  43  TRP A CE3 
144  C CZ2 . TRP A 17  ? 0.2072 0.1921 0.1497 -0.0039 -0.0040 0.0180  43  TRP A CZ2 
145  C CZ3 . TRP A 17  ? 0.2138 0.1932 0.1534 -0.0025 -0.0065 0.0218  43  TRP A CZ3 
146  C CH2 . TRP A 17  ? 0.2100 0.1931 0.1497 -0.0031 -0.0038 0.0190  43  TRP A CH2 
147  N N   . ALA A 18  ? 0.2333 0.1911 0.1824 -0.0009 -0.0274 0.0313  44  ALA A N   
148  C CA  . ALA A 18  ? 0.2414 0.1952 0.1941 0.0033  -0.0325 0.0309  44  ALA A CA  
149  C C   . ALA A 18  ? 0.2509 0.2104 0.2055 0.0091  -0.0303 0.0268  44  ALA A C   
150  O O   . ALA A 18  ? 0.2456 0.2104 0.1974 0.0083  -0.0261 0.0269  44  ALA A O   
151  C CB  . ALA A 18  ? 0.2475 0.1978 0.1976 0.0002  -0.0363 0.0362  44  ALA A CB  
152  N N   . LEU A 19  ? 0.2598 0.2185 0.2192 0.0149  -0.0334 0.0231  45  LEU A N   
153  C CA  . LEU A 19  ? 0.2698 0.2356 0.2312 0.0202  -0.0312 0.0193  45  LEU A CA  
154  C C   . LEU A 19  ? 0.2620 0.2284 0.2264 0.0224  -0.0350 0.0199  45  LEU A C   
155  O O   . LEU A 19  ? 0.2607 0.2208 0.2283 0.0238  -0.0411 0.0203  45  LEU A O   
156  C CB  . LEU A 19  ? 0.2752 0.2424 0.2400 0.0259  -0.0321 0.0137  45  LEU A CB  
157  C CG  . LEU A 19  ? 0.2913 0.2677 0.2578 0.0314  -0.0297 0.0099  45  LEU A CG  
158  C CD1 . LEU A 19  ? 0.2887 0.2711 0.2506 0.0295  -0.0231 0.0112  45  LEU A CD1 
159  C CD2 . LEU A 19  ? 0.3058 0.2836 0.2759 0.0377  -0.0322 0.0036  45  LEU A CD2 
160  N N   . TRP A 20  ? 0.2527 0.2263 0.2167 0.0224  -0.0318 0.0201  46  TRP A N   
161  C CA  . TRP A 20  ? 0.2605 0.2370 0.2282 0.0245  -0.0350 0.0202  46  TRP A CA  
162  C C   . TRP A 20  ? 0.2617 0.2485 0.2338 0.0297  -0.0324 0.0155  46  TRP A C   
163  O O   . TRP A 20  ? 0.2557 0.2475 0.2259 0.0299  -0.0271 0.0140  46  TRP A O   
164  C CB  . TRP A 20  ? 0.2602 0.2378 0.2242 0.0193  -0.0338 0.0244  46  TRP A CB  
165  C CG  . TRP A 20  ? 0.2749 0.2448 0.2336 0.0139  -0.0361 0.0292  46  TRP A CG  
166  C CD1 . TRP A 20  ? 0.2864 0.2534 0.2401 0.0095  -0.0329 0.0309  46  TRP A CD1 
167  C CD2 . TRP A 20  ? 0.2763 0.2419 0.2337 0.0120  -0.0416 0.0333  46  TRP A CD2 
168  N NE1 . TRP A 20  ? 0.2912 0.2532 0.2404 0.0046  -0.0356 0.0357  46  TRP A NE1 
169  C CE2 . TRP A 20  ? 0.2919 0.2524 0.2427 0.0058  -0.0411 0.0377  46  TRP A CE2 
170  C CE3 . TRP A 20  ? 0.2870 0.2533 0.2482 0.0149  -0.0471 0.0336  46  TRP A CE3 
171  C CZ2 . TRP A 20  ? 0.3049 0.2607 0.2514 0.0022  -0.0458 0.0431  46  TRP A CZ2 
172  C CZ3 . TRP A 20  ? 0.3095 0.2702 0.2668 0.0117  -0.0524 0.0389  46  TRP A CZ3 
173  C CH2 . TRP A 20  ? 0.3111 0.2663 0.2606 0.0053  -0.0517 0.0440  46  TRP A CH2 
174  N N   . PHE A 21  ? 0.2675 0.2580 0.2456 0.0339  -0.0363 0.0133  47  PHE A N   
175  C CA  . PHE A 21  ? 0.2890 0.2918 0.2723 0.0386  -0.0339 0.0086  47  PHE A CA  
176  C C   . PHE A 21  ? 0.2955 0.3049 0.2835 0.0387  -0.0356 0.0090  47  PHE A C   
177  O O   . PHE A 21  ? 0.2958 0.2995 0.2855 0.0388  -0.0417 0.0108  47  PHE A O   
178  C CB  . PHE A 21  ? 0.3036 0.3073 0.2918 0.0460  -0.0372 0.0022  47  PHE A CB  
179  C CG  . PHE A 21  ? 0.3244 0.3430 0.3185 0.0516  -0.0350 -0.0035 47  PHE A CG  
180  C CD1 . PHE A 21  ? 0.3367 0.3657 0.3281 0.0510  -0.0278 -0.0045 47  PHE A CD1 
181  C CD2 . PHE A 21  ? 0.3407 0.3636 0.3432 0.0575  -0.0403 -0.0079 47  PHE A CD2 
182  C CE1 . PHE A 21  ? 0.3430 0.3877 0.3393 0.0552  -0.0250 -0.0092 47  PHE A CE1 
183  C CE2 . PHE A 21  ? 0.3501 0.3892 0.3586 0.0627  -0.0377 -0.0140 47  PHE A CE2 
184  C CZ  . PHE A 21  ? 0.3416 0.3922 0.3468 0.0612  -0.0297 -0.0144 47  PHE A CZ  
185  N N   . PHE A 22  ? 0.2955 0.3172 0.2855 0.0382  -0.0304 0.0079  48  PHE A N   
186  C CA  . PHE A 22  ? 0.3050 0.3357 0.3010 0.0381  -0.0314 0.0075  48  PHE A CA  
187  C C   . PHE A 22  ? 0.3325 0.3781 0.3358 0.0437  -0.0293 0.0016  48  PHE A C   
188  O O   . PHE A 22  ? 0.3360 0.3882 0.3372 0.0435  -0.0233 0.0005  48  PHE A O   
189  C CB  . PHE A 22  ? 0.2938 0.3270 0.2863 0.0308  -0.0267 0.0117  48  PHE A CB  
190  C CG  . PHE A 22  ? 0.2953 0.3385 0.2947 0.0300  -0.0281 0.0111  48  PHE A CG  
191  C CD1 . PHE A 22  ? 0.2975 0.3561 0.3035 0.0310  -0.0240 0.0083  48  PHE A CD1 
192  C CD2 . PHE A 22  ? 0.3045 0.3427 0.3034 0.0278  -0.0333 0.0136  48  PHE A CD2 
193  C CE1 . PHE A 22  ? 0.3044 0.3735 0.3181 0.0301  -0.0255 0.0073  48  PHE A CE1 
194  C CE2 . PHE A 22  ? 0.3073 0.3553 0.3129 0.0272  -0.0350 0.0127  48  PHE A CE2 
195  C CZ  . PHE A 22  ? 0.2987 0.3622 0.3124 0.0284  -0.0312 0.0093  48  PHE A CZ  
196  N N   . LYS A 23  ? 0.3516 0.4032 0.3634 0.0488  -0.0343 -0.0022 49  LYS A N   
197  C CA  . LYS A 23  ? 0.3770 0.4457 0.3975 0.0546  -0.0326 -0.0088 49  LYS A CA  
198  C C   . LYS A 23  ? 0.3907 0.4699 0.4187 0.0532  -0.0337 -0.0087 49  LYS A C   
199  O O   . LYS A 23  ? 0.3983 0.4694 0.4271 0.0527  -0.0402 -0.0063 49  LYS A O   
200  C CB  . LYS A 23  ? 0.4227 0.4882 0.4485 0.0638  -0.0393 -0.0154 49  LYS A CB  
201  C CG  . LYS A 23  ? 0.4896 0.5730 0.5267 0.0716  -0.0401 -0.0238 49  LYS A CG  
202  C CD  . LYS A 23  ? 0.5533 0.6293 0.5971 0.0805  -0.0500 -0.0295 49  LYS A CD  
203  C CE  . LYS A 23  ? 0.5943 0.6893 0.6506 0.0889  -0.0512 -0.0387 49  LYS A CE  
204  N NZ  . LYS A 23  ? 0.6247 0.7121 0.6895 0.0977  -0.0625 -0.0439 49  LYS A NZ  
205  N N   . ASN A 24  ? 0.3923 0.4900 0.4258 0.0524  -0.0279 -0.0110 50  ASN A N   
206  C CA  . ASN A 24  ? 0.4047 0.5142 0.4471 0.0512  -0.0292 -0.0118 50  ASN A CA  
207  C C   . ASN A 24  ? 0.3912 0.5097 0.4453 0.0608  -0.0358 -0.0193 50  ASN A C   
208  O O   . ASN A 24  ? 0.3839 0.5224 0.4473 0.0637  -0.0328 -0.0248 50  ASN A O   
209  C CB  . ASN A 24  ? 0.4373 0.5629 0.4819 0.0451  -0.0208 -0.0104 50  ASN A CB  
210  C CG  . ASN A 24  ? 0.5015 0.6283 0.5489 0.0385  -0.0220 -0.0067 50  ASN A CG  
211  O OD1 . ASN A 24  ? 0.5154 0.6450 0.5702 0.0415  -0.0285 -0.0090 50  ASN A OD1 
212  N ND2 . ASN A 24  ? 0.5200 0.6435 0.5614 0.0297  -0.0165 -0.0011 50  ASN A ND2 
213  N N   . ASP A 25  ? 0.3839 0.4877 0.4377 0.0655  -0.0449 -0.0196 51  ASP A N   
214  C CA  . ASP A 25  ? 0.3706 0.4799 0.4358 0.0750  -0.0529 -0.0264 51  ASP A CA  
215  C C   . ASP A 25  ? 0.3673 0.4848 0.4393 0.0726  -0.0559 -0.0249 51  ASP A C   
216  O O   . ASP A 25  ? 0.3744 0.4786 0.4412 0.0688  -0.0610 -0.0189 51  ASP A O   
217  C CB  . ASP A 25  ? 0.3793 0.4676 0.4412 0.0798  -0.0623 -0.0258 51  ASP A CB  
218  C CG  . ASP A 25  ? 0.4057 0.4958 0.4793 0.0902  -0.0724 -0.0324 51  ASP A CG  
219  O OD1 . ASP A 25  ? 0.3929 0.4999 0.4771 0.0932  -0.0733 -0.0367 51  ASP A OD1 
220  O OD2 . ASP A 25  ? 0.4262 0.5003 0.4986 0.0951  -0.0799 -0.0333 51  ASP A OD2 
221  N N   . LYS A 26  ? 0.3547 0.4951 0.4381 0.0746  -0.0527 -0.0306 52  LYS A N   
222  C CA  . LYS A 26  ? 0.3549 0.5073 0.4468 0.0721  -0.0547 -0.0304 52  LYS A CA  
223  C C   . LYS A 26  ? 0.3610 0.5067 0.4587 0.0785  -0.0670 -0.0316 52  LYS A C   
224  O O   . LYS A 26  ? 0.3591 0.5117 0.4621 0.0759  -0.0700 -0.0304 52  LYS A O   
225  C CB  . LYS A 26  ? 0.3709 0.5518 0.4751 0.0729  -0.0480 -0.0367 52  LYS A CB  
226  C CG  . LYS A 26  ? 0.4373 0.6261 0.5359 0.0681  -0.0364 -0.0358 52  LYS A CG  
227  C CD  . LYS A 26  ? 0.4988 0.6956 0.5958 0.0563  -0.0286 -0.0299 52  LYS A CD  
228  C CE  . LYS A 26  ? 0.5351 0.7564 0.6383 0.0546  -0.0191 -0.0332 52  LYS A CE  
229  N NZ  . LYS A 26  ? 0.5653 0.7851 0.6602 0.0570  -0.0135 -0.0342 52  LYS A NZ  
230  N N   . SER A 27  ? 0.3648 0.4968 0.4619 0.0867  -0.0748 -0.0339 53  SER A N   
231  C CA  . SER A 27  ? 0.3710 0.4932 0.4720 0.0924  -0.0875 -0.0334 53  SER A CA  
232  C C   . SER A 27  ? 0.3820 0.4816 0.4690 0.0851  -0.0915 -0.0227 53  SER A C   
233  O O   . SER A 27  ? 0.3846 0.4759 0.4723 0.0875  -0.1015 -0.0201 53  SER A O   
234  C CB  . SER A 27  ? 0.3949 0.5114 0.5024 0.1043  -0.0953 -0.0403 53  SER A CB  
235  O OG  . SER A 27  ? 0.4408 0.5395 0.5381 0.1035  -0.0942 -0.0379 53  SER A OG  
236  N N   . LYS A 28  ? 0.3836 0.4739 0.4578 0.0765  -0.0838 -0.0167 54  LYS A N   
237  C CA  . LYS A 28  ? 0.3927 0.4643 0.4535 0.0694  -0.0863 -0.0075 54  LYS A CA  
238  C C   . LYS A 28  ? 0.3904 0.4674 0.4451 0.0590  -0.0786 -0.0031 54  LYS A C   
239  O O   . LYS A 28  ? 0.3919 0.4825 0.4500 0.0560  -0.0699 -0.0058 54  LYS A O   
240  C CB  . LYS A 28  ? 0.4226 0.4764 0.4735 0.0686  -0.0853 -0.0044 54  LYS A CB  
241  C CG  . LYS A 28  ? 0.4733 0.5202 0.5302 0.0784  -0.0926 -0.0093 54  LYS A CG  
242  C CD  . LYS A 28  ? 0.5324 0.5699 0.5825 0.0772  -0.0879 -0.0092 54  LYS A CD  
243  C CE  . LYS A 28  ? 0.5914 0.6174 0.6457 0.0854  -0.0960 -0.0131 54  LYS A CE  
244  N NZ  . LYS A 28  ? 0.6227 0.6435 0.6719 0.0845  -0.0905 -0.0148 54  LYS A NZ  
245  N N   . THR A 29  ? 0.3836 0.4491 0.4287 0.0533  -0.0819 0.0037  55  THR A N   
246  C CA  . THR A 29  ? 0.3771 0.4449 0.4157 0.0438  -0.0758 0.0073  55  THR A CA  
247  C C   . THR A 29  ? 0.3515 0.4109 0.3801 0.0386  -0.0673 0.0100  55  THR A C   
248  O O   . THR A 29  ? 0.3544 0.4048 0.3800 0.0419  -0.0674 0.0100  55  THR A O   
249  C CB  . THR A 29  ? 0.4185 0.4769 0.4495 0.0407  -0.0830 0.0128  55  THR A CB  
250  O OG1 . THR A 29  ? 0.4576 0.5194 0.4834 0.0323  -0.0780 0.0148  55  THR A OG1 
251  C CG2 . THR A 29  ? 0.4255 0.4649 0.4451 0.0403  -0.0865 0.0185  55  THR A CG2 
252  N N   . TRP A 30  ? 0.3268 0.3886 0.3507 0.0308  -0.0607 0.0120  56  TRP A N   
253  C CA  . TRP A 30  ? 0.3141 0.3685 0.3291 0.0261  -0.0532 0.0144  56  TRP A CA  
254  C C   . TRP A 30  ? 0.3070 0.3445 0.3117 0.0261  -0.0559 0.0185  56  TRP A C   
255  O O   . TRP A 30  ? 0.3123 0.3449 0.3149 0.0280  -0.0530 0.0179  56  TRP A O   
256  C CB  . TRP A 30  ? 0.3097 0.3666 0.3210 0.0178  -0.0479 0.0162  56  TRP A CB  
257  C CG  . TRP A 30  ? 0.3180 0.3698 0.3229 0.0142  -0.0401 0.0176  56  TRP A CG  
258  C CD1 . TRP A 30  ? 0.3252 0.3849 0.3340 0.0134  -0.0333 0.0159  56  TRP A CD1 
259  C CD2 . TRP A 30  ? 0.3277 0.3660 0.3214 0.0114  -0.0387 0.0209  56  TRP A CD2 
260  N NE1 . TRP A 30  ? 0.3351 0.3859 0.3357 0.0112  -0.0286 0.0181  56  TRP A NE1 
261  C CE2 . TRP A 30  ? 0.3377 0.3759 0.3296 0.0098  -0.0316 0.0207  56  TRP A CE2 
262  C CE3 . TRP A 30  ? 0.3440 0.3713 0.3290 0.0099  -0.0428 0.0243  56  TRP A CE3 
263  C CZ2 . TRP A 30  ? 0.3510 0.3787 0.3340 0.0076  -0.0289 0.0229  56  TRP A CZ2 
264  C CZ3 . TRP A 30  ? 0.3576 0.3757 0.3338 0.0070  -0.0392 0.0264  56  TRP A CZ3 
265  C CH2 . TRP A 30  ? 0.3591 0.3775 0.3350 0.0062  -0.0326 0.0254  56  TRP A CH2 
266  N N   . GLN A 31  ? 0.2924 0.3220 0.2907 0.0238  -0.0617 0.0227  57  GLN A N   
267  C CA  . GLN A 31  ? 0.2937 0.3084 0.2820 0.0224  -0.0640 0.0274  57  GLN A CA  
268  C C   . GLN A 31  ? 0.2868 0.2943 0.2783 0.0288  -0.0691 0.0270  57  GLN A C   
269  O O   . GLN A 31  ? 0.2861 0.2841 0.2724 0.0278  -0.0674 0.0288  57  GLN A O   
270  C CB  . GLN A 31  ? 0.3187 0.3283 0.2988 0.0181  -0.0690 0.0324  57  GLN A CB  
271  C CG  . GLN A 31  ? 0.3493 0.3601 0.3215 0.0106  -0.0630 0.0334  57  GLN A CG  
272  C CD  . GLN A 31  ? 0.3948 0.4004 0.3569 0.0066  -0.0677 0.0382  57  GLN A CD  
273  O OE1 . GLN A 31  ? 0.4298 0.4259 0.3854 0.0066  -0.0718 0.0430  57  GLN A OE1 
274  N NE2 . GLN A 31  ? 0.3914 0.4034 0.3518 0.0029  -0.0674 0.0370  57  GLN A NE2 
275  N N   . ALA A 32  ? 0.2824 0.2946 0.2835 0.0356  -0.0755 0.0237  58  ALA A N   
276  C CA  . ALA A 32  ? 0.2937 0.2984 0.2992 0.0426  -0.0815 0.0221  58  ALA A CA  
277  C C   . ALA A 32  ? 0.3030 0.3113 0.3125 0.0459  -0.0754 0.0166  58  ALA A C   
278  O O   . ALA A 32  ? 0.3206 0.3188 0.3296 0.0490  -0.0783 0.0162  58  ALA A O   
279  C CB  . ALA A 32  ? 0.2904 0.3004 0.3061 0.0500  -0.0901 0.0190  58  ALA A CB  
280  N N   . ASN A 33  ? 0.2822 0.3039 0.2945 0.0443  -0.0670 0.0132  59  ASN A N   
281  C CA  . ASN A 33  ? 0.2759 0.3036 0.2905 0.0465  -0.0602 0.0085  59  ASN A CA  
282  C C   . ASN A 33  ? 0.2845 0.3029 0.2892 0.0414  -0.0546 0.0118  59  ASN A C   
283  O O   . ASN A 33  ? 0.2719 0.2928 0.2771 0.0437  -0.0504 0.0085  59  ASN A O   
284  C CB  . ASN A 33  ? 0.2764 0.3222 0.2971 0.0455  -0.0538 0.0052  59  ASN A CB  
285  C CG  . ASN A 33  ? 0.3048 0.3639 0.3383 0.0532  -0.0574 -0.0015 59  ASN A CG  
286  O OD1 . ASN A 33  ? 0.3391 0.3958 0.3770 0.0608  -0.0618 -0.0059 59  ASN A OD1 
287  N ND2 . ASN A 33  ? 0.2743 0.3481 0.3145 0.0517  -0.0556 -0.0030 59  ASN A ND2 
288  N N   . LEU A 34  ? 0.2965 0.3056 0.2922 0.0348  -0.0546 0.0179  60  LEU A N   
289  C CA  . LEU A 34  ? 0.3245 0.3259 0.3114 0.0299  -0.0497 0.0208  60  LEU A CA  
290  C C   . LEU A 34  ? 0.3551 0.3429 0.3388 0.0307  -0.0551 0.0233  60  LEU A C   
291  O O   . LEU A 34  ? 0.3766 0.3568 0.3559 0.0277  -0.0600 0.0283  60  LEU A O   
292  C CB  . LEU A 34  ? 0.3313 0.3319 0.3111 0.0225  -0.0469 0.0251  60  LEU A CB  
293  C CG  . LEU A 34  ? 0.3598 0.3539 0.3312 0.0175  -0.0421 0.0276  60  LEU A CG  
294  C CD1 . LEU A 34  ? 0.3576 0.3564 0.3302 0.0185  -0.0353 0.0244  60  LEU A CD1 
295  C CD2 . LEU A 34  ? 0.3693 0.3628 0.3341 0.0111  -0.0409 0.0308  60  LEU A CD2 
296  N N   . ARG A 35  ? 0.3524 0.3372 0.3382 0.0345  -0.0547 0.0199  61  ARG A N   
297  C CA  . ARG A 35  ? 0.3631 0.3347 0.3479 0.0355  -0.0607 0.0216  61  ARG A CA  
298  C C   . ARG A 35  ? 0.3541 0.3192 0.3338 0.0322  -0.0570 0.0225  61  ARG A C   
299  O O   . ARG A 35  ? 0.3384 0.3097 0.3179 0.0329  -0.0509 0.0191  61  ARG A O   
300  C CB  . ARG A 35  ? 0.3924 0.3643 0.3866 0.0443  -0.0668 0.0157  61  ARG A CB  
301  C CG  . ARG A 35  ? 0.4571 0.4324 0.4572 0.0480  -0.0732 0.0155  61  ARG A CG  
302  C CD  . ARG A 35  ? 0.4981 0.4743 0.5086 0.0577  -0.0796 0.0085  61  ARG A CD  
303  N NE  . ARG A 35  ? 0.5555 0.5498 0.5734 0.0627  -0.0750 0.0011  61  ARG A NE  
304  C CZ  . ARG A 35  ? 0.5783 0.5834 0.6028 0.0655  -0.0769 -0.0008 61  ARG A CZ  
305  N NH1 . ARG A 35  ? 0.5691 0.5680 0.5930 0.0643  -0.0838 0.0040  61  ARG A NH1 
306  N NH2 . ARG A 35  ? 0.5666 0.5896 0.5981 0.0692  -0.0719 -0.0074 61  ARG A NH2 
307  N N   . LEU A 36  ? 0.3562 0.3093 0.3324 0.0288  -0.0615 0.0272  62  LEU A N   
308  C CA  . LEU A 36  ? 0.3641 0.3111 0.3365 0.0249  -0.0591 0.0284  62  LEU A CA  
309  C C   . LEU A 36  ? 0.3580 0.3014 0.3366 0.0306  -0.0620 0.0227  62  LEU A C   
310  O O   . LEU A 36  ? 0.3570 0.2925 0.3405 0.0343  -0.0699 0.0220  62  LEU A O   
311  C CB  . LEU A 36  ? 0.3780 0.3147 0.3447 0.0181  -0.0628 0.0362  62  LEU A CB  
312  C CG  . LEU A 36  ? 0.4036 0.3347 0.3674 0.0132  -0.0608 0.0380  62  LEU A CG  
313  C CD1 . LEU A 36  ? 0.3983 0.3377 0.3576 0.0098  -0.0520 0.0370  62  LEU A CD1 
314  C CD2 . LEU A 36  ? 0.4199 0.3410 0.3791 0.0064  -0.0654 0.0462  62  LEU A CD2 
315  N N   . ILE A 37  ? 0.3502 0.2991 0.3285 0.0318  -0.0563 0.0183  63  ILE A N   
316  C CA  . ILE A 37  ? 0.3524 0.2993 0.3358 0.0372  -0.0589 0.0120  63  ILE A CA  
317  C C   . ILE A 37  ? 0.3573 0.2928 0.3396 0.0329  -0.0618 0.0145  63  ILE A C   
318  O O   . ILE A 37  ? 0.3707 0.2970 0.3581 0.0355  -0.0691 0.0126  63  ILE A O   
319  C CB  . ILE A 37  ? 0.3579 0.3168 0.3413 0.0411  -0.0523 0.0060  63  ILE A CB  
320  C CG1 . ILE A 37  ? 0.3653 0.3363 0.3514 0.0452  -0.0498 0.0034  63  ILE A CG1 
321  C CG2 . ILE A 37  ? 0.3662 0.3233 0.3536 0.0464  -0.0550 -0.0009 63  ILE A CG2 
322  C CD1 . ILE A 37  ? 0.3778 0.3479 0.3711 0.0503  -0.0571 0.0016  63  ILE A CD1 
323  N N   . SER A 38  ? 0.3469 0.2834 0.3234 0.0262  -0.0565 0.0182  64  SER A N   
324  C CA  . SER A 38  ? 0.3566 0.2847 0.3326 0.0211  -0.0583 0.0206  64  SER A CA  
325  C C   . SER A 38  ? 0.3437 0.2759 0.3134 0.0138  -0.0517 0.0248  64  SER A C   
326  O O   . SER A 38  ? 0.3458 0.2867 0.3118 0.0138  -0.0457 0.0246  64  SER A O   
327  C CB  . SER A 38  ? 0.3914 0.3187 0.3726 0.0258  -0.0601 0.0134  64  SER A CB  
328  O OG  . SER A 38  ? 0.4432 0.3817 0.4226 0.0294  -0.0537 0.0084  64  SER A OG  
329  N N   . LYS A 39  ? 0.3282 0.2543 0.2972 0.0074  -0.0531 0.0286  65  LYS A N   
330  C CA  . LYS A 39  ? 0.3224 0.2535 0.2866 0.0007  -0.0472 0.0316  65  LYS A CA  
331  C C   . LYS A 39  ? 0.3175 0.2490 0.2853 -0.0001 -0.0464 0.0279  65  LYS A C   
332  O O   . LYS A 39  ? 0.3252 0.2501 0.2986 0.0020  -0.0518 0.0251  65  LYS A O   
333  C CB  . LYS A 39  ? 0.3431 0.2696 0.3029 -0.0075 -0.0488 0.0400  65  LYS A CB  
334  C CG  . LYS A 39  ? 0.3956 0.3214 0.3518 -0.0067 -0.0508 0.0437  65  LYS A CG  
335  C CD  . LYS A 39  ? 0.4466 0.3694 0.3964 -0.0149 -0.0519 0.0524  65  LYS A CD  
336  C CE  . LYS A 39  ? 0.5005 0.4249 0.4460 -0.0136 -0.0533 0.0550  65  LYS A CE  
337  N NZ  . LYS A 39  ? 0.5286 0.4516 0.4663 -0.0215 -0.0543 0.0634  65  LYS A NZ  
338  N N   . PHE A 40  ? 0.3008 0.2403 0.2660 -0.0029 -0.0402 0.0274  66  PHE A N   
339  C CA  . PHE A 40  ? 0.2890 0.2307 0.2577 -0.0040 -0.0392 0.0239  66  PHE A CA  
340  C C   . PHE A 40  ? 0.2910 0.2403 0.2564 -0.0100 -0.0333 0.0261  66  PHE A C   
341  O O   . PHE A 40  ? 0.2922 0.2466 0.2525 -0.0106 -0.0290 0.0278  66  PHE A O   
342  C CB  . PHE A 40  ? 0.2727 0.2188 0.2434 0.0041  -0.0383 0.0164  66  PHE A CB  
343  C CG  . PHE A 40  ? 0.2760 0.2301 0.2420 0.0075  -0.0325 0.0152  66  PHE A CG  
344  C CD1 . PHE A 40  ? 0.2818 0.2428 0.2459 0.0064  -0.0276 0.0141  66  PHE A CD1 
345  C CD2 . PHE A 40  ? 0.2802 0.2350 0.2444 0.0118  -0.0324 0.0152  66  PHE A CD2 
346  C CE1 . PHE A 40  ? 0.2877 0.2540 0.2478 0.0091  -0.0231 0.0136  66  PHE A CE1 
347  C CE2 . PHE A 40  ? 0.2839 0.2454 0.2444 0.0138  -0.0274 0.0148  66  PHE A CE2 
348  C CZ  . PHE A 40  ? 0.2865 0.2527 0.2447 0.0125  -0.0230 0.0142  66  PHE A CZ  
349  N N   . ASP A 41  ? 0.2828 0.2336 0.2520 -0.0143 -0.0333 0.0255  67  ASP A N   
350  C CA  . ASP A 41  ? 0.2808 0.2409 0.2484 -0.0194 -0.0277 0.0262  67  ASP A CA  
351  C C   . ASP A 41  ? 0.2582 0.2240 0.2316 -0.0185 -0.0268 0.0208  67  ASP A C   
352  O O   . ASP A 41  ? 0.2503 0.2241 0.2247 -0.0234 -0.0231 0.0210  67  ASP A O   
353  C CB  . ASP A 41  ? 0.3242 0.2837 0.2891 -0.0289 -0.0274 0.0335  67  ASP A CB  
354  C CG  . ASP A 41  ? 0.4232 0.3754 0.3932 -0.0349 -0.0325 0.0369  67  ASP A CG  
355  O OD1 . ASP A 41  ? 0.4431 0.3906 0.4196 -0.0314 -0.0366 0.0325  67  ASP A OD1 
356  O OD2 . ASP A 41  ? 0.4747 0.4260 0.4420 -0.0434 -0.0325 0.0440  67  ASP A OD2 
357  N N   . THR A 42  ? 0.2452 0.2080 0.2224 -0.0121 -0.0302 0.0154  68  THR A N   
358  C CA  . THR A 42  ? 0.2430 0.2113 0.2253 -0.0100 -0.0302 0.0095  68  THR A CA  
359  C C   . THR A 42  ? 0.2332 0.2035 0.2135 -0.0004 -0.0300 0.0040  68  THR A C   
360  O O   . THR A 42  ? 0.2257 0.1920 0.2026 0.0043  -0.0310 0.0041  68  THR A O   
361  C CB  . THR A 42  ? 0.2658 0.2285 0.2557 -0.0134 -0.0360 0.0083  68  THR A CB  
362  O OG1 . THR A 42  ? 0.2927 0.2464 0.2836 -0.0078 -0.0416 0.0059  68  THR A OG1 
363  C CG2 . THR A 42  ? 0.2673 0.2269 0.2589 -0.0239 -0.0367 0.0152  68  THR A CG2 
364  N N   . VAL A 43  ? 0.2233 0.2007 0.2057 0.0024  -0.0288 -0.0008 69  VAL A N   
365  C CA  . VAL A 43  ? 0.2203 0.2003 0.2003 0.0108  -0.0289 -0.0055 69  VAL A CA  
366  C C   . VAL A 43  ? 0.2183 0.1926 0.2001 0.0153  -0.0343 -0.0091 69  VAL A C   
367  O O   . VAL A 43  ? 0.2142 0.1881 0.1918 0.0211  -0.0341 -0.0102 69  VAL A O   
368  C CB  . VAL A 43  ? 0.2213 0.2094 0.2044 0.0120  -0.0281 -0.0097 69  VAL A CB  
369  C CG1 . VAL A 43  ? 0.2270 0.2172 0.2076 0.0204  -0.0297 -0.0144 69  VAL A CG1 
370  C CG2 . VAL A 43  ? 0.2221 0.2166 0.2036 0.0095  -0.0229 -0.0077 69  VAL A CG2 
371  N N   . GLU A 44  ? 0.2176 0.1879 0.2062 0.0120  -0.0392 -0.0110 70  GLU A N   
372  C CA  . GLU A 44  ? 0.2332 0.1977 0.2250 0.0163  -0.0452 -0.0158 70  GLU A CA  
373  C C   . GLU A 44  ? 0.2443 0.2021 0.2333 0.0185  -0.0465 -0.0134 70  GLU A C   
374  O O   . GLU A 44  ? 0.2509 0.2087 0.2388 0.0257  -0.0486 -0.0182 70  GLU A O   
375  C CB  . GLU A 44  ? 0.2642 0.2233 0.2647 0.0106  -0.0507 -0.0171 70  GLU A CB  
376  C CG  . GLU A 44  ? 0.3152 0.2818 0.3208 0.0092  -0.0511 -0.0216 70  GLU A CG  
377  C CD  . GLU A 44  ? 0.3668 0.3415 0.3728 0.0032  -0.0456 -0.0177 70  GLU A CD  
378  O OE1 . GLU A 44  ? 0.3635 0.3464 0.3737 0.0033  -0.0454 -0.0219 70  GLU A OE1 
379  O OE2 . GLU A 44  ? 0.3658 0.3397 0.3681 -0.0013 -0.0416 -0.0112 70  GLU A OE2 
380  N N   . ASP A 45  ? 0.2409 0.1941 0.2287 0.0127  -0.0453 -0.0065 71  ASP A N   
381  C CA  . ASP A 45  ? 0.2454 0.1926 0.2313 0.0149  -0.0472 -0.0041 71  ASP A CA  
382  C C   . ASP A 45  ? 0.2369 0.1905 0.2164 0.0201  -0.0423 -0.0039 71  ASP A C   
383  O O   . ASP A 45  ? 0.2452 0.1974 0.2243 0.0250  -0.0440 -0.0054 71  ASP A O   
384  C CB  . ASP A 45  ? 0.2771 0.2169 0.2635 0.0070  -0.0486 0.0034  71  ASP A CB  
385  C CG  . ASP A 45  ? 0.3793 0.3103 0.3727 0.0018  -0.0548 0.0040  71  ASP A CG  
386  O OD1 . ASP A 45  ? 0.4007 0.3299 0.3994 0.0054  -0.0592 -0.0027 71  ASP A OD1 
387  O OD2 . ASP A 45  ? 0.4298 0.3558 0.4231 -0.0062 -0.0556 0.0112  71  ASP A OD2 
388  N N   . PHE A 46  ? 0.2187 0.1796 0.1939 0.0191  -0.0365 -0.0024 72  PHE A N   
389  C CA  . PHE A 46  ? 0.2133 0.1795 0.1827 0.0233  -0.0321 -0.0018 72  PHE A CA  
390  C C   . PHE A 46  ? 0.2086 0.1787 0.1775 0.0309  -0.0333 -0.0078 72  PHE A C   
391  O O   . PHE A 46  ? 0.2280 0.2002 0.1949 0.0350  -0.0326 -0.0083 72  PHE A O   
392  C CB  . PHE A 46  ? 0.2059 0.1778 0.1716 0.0210  -0.0265 0.0004  72  PHE A CB  
393  C CG  . PHE A 46  ? 0.2185 0.1950 0.1791 0.0258  -0.0231 0.0002  72  PHE A CG  
394  C CD1 . PHE A 46  ? 0.2415 0.2178 0.1993 0.0258  -0.0212 0.0032  72  PHE A CD1 
395  C CD2 . PHE A 46  ? 0.2267 0.2078 0.1854 0.0303  -0.0225 -0.0031 72  PHE A CD2 
396  C CE1 . PHE A 46  ? 0.2458 0.2264 0.1996 0.0295  -0.0182 0.0034  72  PHE A CE1 
397  C CE2 . PHE A 46  ? 0.2343 0.2191 0.1879 0.0341  -0.0197 -0.0023 72  PHE A CE2 
398  C CZ  . PHE A 46  ? 0.2319 0.2164 0.1832 0.0333  -0.0174 0.0011  72  PHE A CZ  
399  N N   . TRP A 47  ? 0.1949 0.1672 0.1657 0.0327  -0.0351 -0.0124 73  TRP A N   
400  C CA  . TRP A 47  ? 0.1995 0.1767 0.1686 0.0401  -0.0363 -0.0183 73  TRP A CA  
401  C C   . TRP A 47  ? 0.2145 0.1882 0.1874 0.0439  -0.0413 -0.0229 73  TRP A C   
402  O O   . TRP A 47  ? 0.2172 0.1964 0.1873 0.0498  -0.0406 -0.0262 73  TRP A O   
403  C CB  . TRP A 47  ? 0.1926 0.1739 0.1622 0.0415  -0.0374 -0.0223 73  TRP A CB  
404  C CG  . TRP A 47  ? 0.2030 0.1890 0.1681 0.0404  -0.0327 -0.0189 73  TRP A CG  
405  C CD1 . TRP A 47  ? 0.2218 0.2083 0.1896 0.0359  -0.0316 -0.0173 73  TRP A CD1 
406  C CD2 . TRP A 47  ? 0.2128 0.2033 0.1706 0.0438  -0.0287 -0.0165 73  TRP A CD2 
407  N NE1 . TRP A 47  ? 0.2306 0.2212 0.1935 0.0372  -0.0278 -0.0149 73  TRP A NE1 
408  C CE2 . TRP A 47  ? 0.2306 0.2226 0.1872 0.0416  -0.0261 -0.0138 73  TRP A CE2 
409  C CE3 . TRP A 47  ? 0.2258 0.2196 0.1785 0.0479  -0.0269 -0.0162 73  TRP A CE3 
410  C CZ2 . TRP A 47  ? 0.2389 0.2336 0.1890 0.0441  -0.0229 -0.0110 73  TRP A CZ2 
411  C CZ3 . TRP A 47  ? 0.2424 0.2398 0.1884 0.0492  -0.0230 -0.0126 73  TRP A CZ3 
412  C CH2 . TRP A 47  ? 0.2437 0.2404 0.1885 0.0473  -0.0214 -0.0097 73  TRP A CH2 
413  N N   . ALA A 48  ? 0.2259 0.1909 0.2052 0.0403  -0.0463 -0.0228 74  ALA A N   
414  C CA  . ALA A 48  ? 0.2513 0.2112 0.2353 0.0445  -0.0522 -0.0277 74  ALA A CA  
415  C C   . ALA A 48  ? 0.2698 0.2312 0.2517 0.0474  -0.0505 -0.0256 74  ALA A C   
416  O O   . ALA A 48  ? 0.2846 0.2488 0.2681 0.0541  -0.0528 -0.0315 74  ALA A O   
417  C CB  . ALA A 48  ? 0.2574 0.2056 0.2486 0.0392  -0.0583 -0.0264 74  ALA A CB  
418  N N   . LEU A 49  ? 0.2682 0.2295 0.2469 0.0426  -0.0462 -0.0181 75  LEU A N   
419  C CA  . LEU A 49  ? 0.2650 0.2289 0.2422 0.0446  -0.0444 -0.0160 75  LEU A CA  
420  C C   . LEU A 49  ? 0.2514 0.2272 0.2234 0.0492  -0.0389 -0.0178 75  LEU A C   
421  O O   . LEU A 49  ? 0.2466 0.2279 0.2195 0.0546  -0.0392 -0.0216 75  LEU A O   
422  C CB  . LEU A 49  ? 0.2740 0.2341 0.2492 0.0376  -0.0421 -0.0076 75  LEU A CB  
423  C CG  . LEU A 49  ? 0.3051 0.2689 0.2787 0.0390  -0.0400 -0.0051 75  LEU A CG  
424  C CD1 . LEU A 49  ? 0.3111 0.2705 0.2904 0.0429  -0.0462 -0.0078 75  LEU A CD1 
425  C CD2 . LEU A 49  ? 0.3270 0.2893 0.2969 0.0321  -0.0366 0.0024  75  LEU A CD2 
426  N N   . TYR A 50  ? 0.2382 0.2181 0.2050 0.0469  -0.0341 -0.0151 76  TYR A N   
427  C CA  . TYR A 50  ? 0.2285 0.2181 0.1896 0.0500  -0.0290 -0.0151 76  TYR A CA  
428  C C   . TYR A 50  ? 0.2356 0.2325 0.1959 0.0573  -0.0304 -0.0225 76  TYR A C   
429  O O   . TYR A 50  ? 0.2422 0.2479 0.2002 0.0606  -0.0275 -0.0233 76  TYR A O   
430  C CB  . TYR A 50  ? 0.2280 0.2184 0.1841 0.0467  -0.0251 -0.0111 76  TYR A CB  
431  C CG  . TYR A 50  ? 0.2246 0.2231 0.1744 0.0492  -0.0205 -0.0097 76  TYR A CG  
432  C CD1 . TYR A 50  ? 0.2270 0.2279 0.1749 0.0471  -0.0166 -0.0050 76  TYR A CD1 
433  C CD2 . TYR A 50  ? 0.2236 0.2279 0.1694 0.0537  -0.0205 -0.0132 76  TYR A CD2 
434  C CE1 . TYR A 50  ? 0.2329 0.2409 0.1752 0.0484  -0.0125 -0.0029 76  TYR A CE1 
435  C CE2 . TYR A 50  ? 0.2330 0.2448 0.1722 0.0555  -0.0165 -0.0109 76  TYR A CE2 
436  C CZ  . TYR A 50  ? 0.2443 0.2578 0.1821 0.0526  -0.0124 -0.0056 76  TYR A CZ  
437  O OH  . TYR A 50  ? 0.2666 0.2871 0.1982 0.0532  -0.0084 -0.0023 76  TYR A OH  
438  N N   . ASN A 51  ? 0.2305 0.2253 0.1930 0.0595  -0.0347 -0.0281 77  ASN A N   
439  C CA  . ASN A 51  ? 0.2536 0.2560 0.2149 0.0667  -0.0364 -0.0360 77  ASN A CA  
440  C C   . ASN A 51  ? 0.2834 0.2874 0.2499 0.0718  -0.0398 -0.0420 77  ASN A C   
441  O O   . ASN A 51  ? 0.2894 0.3029 0.2542 0.0783  -0.0398 -0.0487 77  ASN A O   
442  C CB  . ASN A 51  ? 0.2613 0.2609 0.2244 0.0678  -0.0410 -0.0413 77  ASN A CB  
443  C CG  . ASN A 51  ? 0.2876 0.2888 0.2458 0.0652  -0.0384 -0.0379 77  ASN A CG  
444  O OD1 . ASN A 51  ? 0.3040 0.3008 0.2657 0.0630  -0.0416 -0.0395 77  ASN A OD1 
445  N ND2 . ASN A 51  ? 0.2689 0.2765 0.2196 0.0653  -0.0329 -0.0331 77  ASN A ND2 
446  N N   . HIS A 52  ? 0.3018 0.2970 0.2745 0.0694  -0.0429 -0.0399 78  HIS A N   
447  C CA  . HIS A 52  ? 0.3236 0.3189 0.3027 0.0749  -0.0474 -0.0461 78  HIS A CA  
448  C C   . HIS A 52  ? 0.3384 0.3378 0.3184 0.0746  -0.0445 -0.0422 78  HIS A C   
449  O O   . HIS A 52  ? 0.3577 0.3570 0.3440 0.0793  -0.0487 -0.0469 78  HIS A O   
450  C CB  . HIS A 52  ? 0.3477 0.3287 0.3346 0.0739  -0.0558 -0.0487 78  HIS A CB  
451  C CG  . HIS A 52  ? 0.4039 0.3834 0.3913 0.0755  -0.0592 -0.0549 78  HIS A CG  
452  N ND1 . HIS A 52  ? 0.4398 0.4135 0.4261 0.0690  -0.0590 -0.0506 78  HIS A ND1 
453  C CD2 . HIS A 52  ? 0.4185 0.4044 0.4065 0.0830  -0.0620 -0.0653 78  HIS A CD2 
454  C CE1 . HIS A 52  ? 0.4484 0.4241 0.4358 0.0726  -0.0624 -0.0583 78  HIS A CE1 
455  N NE2 . HIS A 52  ? 0.4414 0.4242 0.4293 0.0810  -0.0643 -0.0673 78  HIS A NE2 
456  N N   . ILE A 53  ? 0.3269 0.3308 0.3014 0.0699  -0.0379 -0.0345 79  ILE A N   
457  C CA  . ILE A 53  ? 0.3374 0.3469 0.3130 0.0694  -0.0350 -0.0313 79  ILE A CA  
458  C C   . ILE A 53  ? 0.3277 0.3530 0.2983 0.0716  -0.0283 -0.0319 79  ILE A C   
459  O O   . ILE A 53  ? 0.3182 0.3476 0.2822 0.0713  -0.0249 -0.0313 79  ILE A O   
460  C CB  . ILE A 53  ? 0.3581 0.3599 0.3329 0.0617  -0.0335 -0.0222 79  ILE A CB  
461  C CG1 . ILE A 53  ? 0.3737 0.3746 0.3414 0.0563  -0.0285 -0.0164 79  ILE A CG1 
462  C CG2 . ILE A 53  ? 0.3763 0.3646 0.3564 0.0597  -0.0403 -0.0210 79  ILE A CG2 
463  C CD1 . ILE A 53  ? 0.3929 0.3873 0.3592 0.0491  -0.0269 -0.0088 79  ILE A CD1 
464  N N   . GLN A 54  ? 0.3329 0.3672 0.3068 0.0736  -0.0265 -0.0327 80  GLN A N   
465  C CA  . GLN A 54  ? 0.3455 0.3961 0.3160 0.0746  -0.0199 -0.0325 80  GLN A CA  
466  C C   . GLN A 54  ? 0.3508 0.4001 0.3139 0.0672  -0.0141 -0.0230 80  GLN A C   
467  O O   . GLN A 54  ? 0.3489 0.3882 0.3126 0.0616  -0.0146 -0.0170 80  GLN A O   
468  C CB  . GLN A 54  ? 0.3787 0.4370 0.3565 0.0762  -0.0200 -0.0339 80  GLN A CB  
469  C CG  . GLN A 54  ? 0.4501 0.5288 0.4286 0.0806  -0.0154 -0.0387 80  GLN A CG  
470  C CD  . GLN A 54  ? 0.5238 0.6104 0.5117 0.0828  -0.0164 -0.0412 80  GLN A CD  
471  O OE1 . GLN A 54  ? 0.5505 0.6266 0.5448 0.0829  -0.0223 -0.0409 80  GLN A OE1 
472  N NE2 . GLN A 54  ? 0.5240 0.6302 0.5129 0.0845  -0.0110 -0.0436 80  GLN A NE2 
473  N N   . LEU A 55  ? 0.3511 0.4101 0.3071 0.0673  -0.0090 -0.0217 81  LEU A N   
474  C CA  . LEU A 55  ? 0.3635 0.4210 0.3129 0.0609  -0.0040 -0.0129 81  LEU A CA  
475  C C   . LEU A 55  ? 0.3682 0.4299 0.3208 0.0564  -0.0006 -0.0081 81  LEU A C   
476  O O   . LEU A 55  ? 0.3577 0.4296 0.3160 0.0591  -0.0003 -0.0118 81  LEU A O   
477  C CB  . LEU A 55  ? 0.3670 0.4347 0.3078 0.0625  0.0001  -0.0124 81  LEU A CB  
478  C CG  . LEU A 55  ? 0.3985 0.4617 0.3344 0.0659  -0.0029 -0.0157 81  LEU A CG  
479  C CD1 . LEU A 55  ? 0.4061 0.4825 0.3336 0.0692  0.0003  -0.0170 81  LEU A CD1 
480  C CD2 . LEU A 55  ? 0.4133 0.4627 0.3466 0.0612  -0.0039 -0.0099 81  LEU A CD2 
481  N N   . SER A 56  ? 0.3793 0.4340 0.3287 0.0498  0.0017  -0.0004 82  SER A N   
482  C CA  . SER A 56  ? 0.3946 0.4524 0.3469 0.0446  0.0047  0.0045  82  SER A CA  
483  C C   . SER A 56  ? 0.4111 0.4849 0.3621 0.0444  0.0101  0.0055  82  SER A C   
484  O O   . SER A 56  ? 0.4052 0.4877 0.3621 0.0429  0.0116  0.0054  82  SER A O   
485  C CB  . SER A 56  ? 0.4156 0.4622 0.3640 0.0382  0.0058  0.0116  82  SER A CB  
486  O OG  . SER A 56  ? 0.4427 0.4768 0.3923 0.0378  0.0016  0.0108  82  SER A OG  
487  N N   . SER A 57  ? 0.4325 0.5115 0.3757 0.0458  0.0127  0.0063  83  SER A N   
488  C CA  . SER A 57  ? 0.4470 0.5429 0.3877 0.0452  0.0183  0.0077  83  SER A CA  
489  C C   . SER A 57  ? 0.4578 0.5700 0.4041 0.0515  0.0184  -0.0010 83  SER A C   
490  O O   . SER A 57  ? 0.4596 0.5887 0.4053 0.0508  0.0235  -0.0006 83  SER A O   
491  C CB  . SER A 57  ? 0.4626 0.5592 0.3921 0.0450  0.0206  0.0116  83  SER A CB  
492  O OG  . SER A 57  ? 0.5034 0.6003 0.4302 0.0521  0.0173  0.0045  83  SER A OG  
493  N N   . ASN A 58  ? 0.4600 0.5675 0.4119 0.0577  0.0127  -0.0090 84  ASN A N   
494  C CA  . ASN A 58  ? 0.4614 0.5826 0.4201 0.0649  0.0115  -0.0187 84  ASN A CA  
495  C C   . ASN A 58  ? 0.4592 0.5788 0.4295 0.0654  0.0080  -0.0211 84  ASN A C   
496  O O   . ASN A 58  ? 0.4570 0.5858 0.4346 0.0721  0.0055  -0.0297 84  ASN A O   
497  C CB  . ASN A 58  ? 0.4862 0.6043 0.4433 0.0727  0.0067  -0.0272 84  ASN A CB  
498  C CG  . ASN A 58  ? 0.5468 0.6726 0.4932 0.0741  0.0100  -0.0272 84  ASN A CG  
499  O OD1 . ASN A 58  ? 0.5691 0.7090 0.5103 0.0715  0.0164  -0.0233 84  ASN A OD1 
500  N ND2 . ASN A 58  ? 0.5568 0.6740 0.4995 0.0780  0.0056  -0.0313 84  ASN A ND2 
501  N N   . LEU A 59  ? 0.4567 0.5650 0.4285 0.0588  0.0074  -0.0141 85  LEU A N   
502  C CA  . LEU A 59  ? 0.4555 0.5623 0.4370 0.0588  0.0038  -0.0154 85  LEU A CA  
503  C C   . LEU A 59  ? 0.4477 0.5731 0.4350 0.0569  0.0085  -0.0152 85  LEU A C   
504  O O   . LEU A 59  ? 0.4458 0.5801 0.4285 0.0518  0.0150  -0.0101 85  LEU A O   
505  C CB  . LEU A 59  ? 0.4621 0.5518 0.4422 0.0522  0.0016  -0.0082 85  LEU A CB  
506  C CG  . LEU A 59  ? 0.4855 0.5571 0.4619 0.0529  -0.0034 -0.0080 85  LEU A CG  
507  C CD1 . LEU A 59  ? 0.4901 0.5487 0.4657 0.0464  -0.0048 -0.0016 85  LEU A CD1 
508  C CD2 . LEU A 59  ? 0.4890 0.5576 0.4711 0.0604  -0.0100 -0.0158 85  LEU A CD2 
509  N N   . MET A 60  ? 0.4410 0.5721 0.4389 0.0605  0.0050  -0.0202 86  MET A N   
510  C CA  . MET A 60  ? 0.4375 0.5877 0.4430 0.0586  0.0090  -0.0207 86  MET A CA  
511  C C   . MET A 60  ? 0.4300 0.5745 0.4346 0.0488  0.0113  -0.0115 86  MET A C   
512  O O   . MET A 60  ? 0.4386 0.5650 0.4407 0.0459  0.0073  -0.0075 86  MET A O   
513  C CB  . MET A 60  ? 0.4533 0.6094 0.4711 0.0657  0.0032  -0.0287 86  MET A CB  
514  C CG  . MET A 60  ? 0.5079 0.6659 0.5281 0.0762  -0.0012 -0.0389 86  MET A CG  
515  S SD  . MET A 60  ? 0.6329 0.7926 0.6681 0.0846  -0.0101 -0.0474 86  MET A SD  
516  C CE  . MET A 60  ? 0.6153 0.7486 0.6481 0.0786  -0.0167 -0.0385 86  MET A CE  
517  N N   . PRO A 61  ? 0.4114 0.5717 0.4188 0.0433  0.0175  -0.0083 87  PRO A N   
518  C CA  . PRO A 61  ? 0.4004 0.5547 0.4083 0.0338  0.0188  -0.0004 87  PRO A CA  
519  C C   . PRO A 61  ? 0.3773 0.5235 0.3926 0.0347  0.0120  -0.0021 87  PRO A C   
520  O O   . PRO A 61  ? 0.3754 0.5288 0.3992 0.0415  0.0079  -0.0090 87  PRO A O   
521  C CB  . PRO A 61  ? 0.4061 0.5826 0.4190 0.0291  0.0257  0.0011  87  PRO A CB  
522  C CG  . PRO A 61  ? 0.4116 0.6027 0.4210 0.0342  0.0298  -0.0031 87  PRO A CG  
523  C CD  . PRO A 61  ? 0.3979 0.5830 0.4085 0.0449  0.0235  -0.0120 87  PRO A CD  
524  N N   . GLY A 62  ? 0.3562 0.4871 0.3679 0.0284  0.0104  0.0040  88  GLY A N   
525  C CA  . GLY A 62  ? 0.3377 0.4602 0.3542 0.0285  0.0039  0.0034  88  GLY A CA  
526  C C   . GLY A 62  ? 0.3226 0.4266 0.3337 0.0324  -0.0021 0.0027  88  GLY A C   
527  O O   . GLY A 62  ? 0.3238 0.4191 0.3367 0.0319  -0.0076 0.0034  88  GLY A O   
528  N N   . CYS A 63  ? 0.3092 0.4073 0.3135 0.0358  -0.0012 0.0017  89  CYS A N   
529  C CA  . CYS A 63  ? 0.3137 0.3948 0.3133 0.0385  -0.0066 0.0014  89  CYS A CA  
530  C C   . CYS A 63  ? 0.3075 0.3743 0.2979 0.0324  -0.0049 0.0075  89  CYS A C   
531  O O   . CYS A 63  ? 0.3062 0.3751 0.2927 0.0276  0.0003  0.0115  89  CYS A O   
532  C CB  . CYS A 63  ? 0.3290 0.4116 0.3280 0.0461  -0.0078 -0.0045 89  CYS A CB  
533  S SG  . CYS A 63  ? 0.4099 0.5071 0.4206 0.0553  -0.0116 -0.0138 89  CYS A SG  
534  N N   . ASP A 64  ? 0.2926 0.3451 0.2801 0.0326  -0.0097 0.0084  90  ASP A N   
535  C CA  . ASP A 64  ? 0.2749 0.3151 0.2545 0.0279  -0.0086 0.0128  90  ASP A CA  
536  C C   . ASP A 64  ? 0.2518 0.2810 0.2283 0.0309  -0.0124 0.0115  90  ASP A C   
537  O O   . ASP A 64  ? 0.2477 0.2741 0.2279 0.0344  -0.0177 0.0090  90  ASP A O   
538  C CB  . ASP A 64  ? 0.2976 0.3318 0.2768 0.0225  -0.0104 0.0163  90  ASP A CB  
539  C CG  . ASP A 64  ? 0.3658 0.4084 0.3496 0.0185  -0.0088 0.0176  90  ASP A CG  
540  O OD1 . ASP A 64  ? 0.3639 0.4158 0.3494 0.0171  -0.0041 0.0180  90  ASP A OD1 
541  O OD2 . ASP A 64  ? 0.3953 0.4348 0.3804 0.0160  -0.0123 0.0186  90  ASP A OD2 
542  N N   . TYR A 65  ? 0.2307 0.2526 0.2006 0.0286  -0.0103 0.0137  91  TYR A N   
543  C CA  . TYR A 65  ? 0.2274 0.2385 0.1942 0.0290  -0.0135 0.0136  91  TYR A CA  
544  C C   . TYR A 65  ? 0.2202 0.2242 0.1825 0.0229  -0.0123 0.0178  91  TYR A C   
545  O O   . TYR A 65  ? 0.2153 0.2215 0.1758 0.0196  -0.0086 0.0200  91  TYR A O   
546  C CB  . TYR A 65  ? 0.2314 0.2420 0.1948 0.0317  -0.0117 0.0116  91  TYR A CB  
547  C CG  . TYR A 65  ? 0.2495 0.2649 0.2159 0.0383  -0.0137 0.0061  91  TYR A CG  
548  C CD1 . TYR A 65  ? 0.2620 0.2730 0.2331 0.0416  -0.0196 0.0029  91  TYR A CD1 
549  C CD2 . TYR A 65  ? 0.2655 0.2884 0.2293 0.0412  -0.0103 0.0039  91  TYR A CD2 
550  C CE1 . TYR A 65  ? 0.2716 0.2858 0.2459 0.0481  -0.0222 -0.0034 91  TYR A CE1 
551  C CE2 . TYR A 65  ? 0.2791 0.3065 0.2450 0.0476  -0.0125 -0.0023 91  TYR A CE2 
552  C CZ  . TYR A 65  ? 0.2927 0.3158 0.2643 0.0513  -0.0184 -0.0065 91  TYR A CZ  
553  O OH  . TYR A 65  ? 0.3239 0.3510 0.2981 0.0580  -0.0210 -0.0137 91  TYR A OH  
554  N N   . SER A 66  ? 0.2175 0.2132 0.1781 0.0213  -0.0155 0.0189  92  SER A N   
555  C CA  . SER A 66  ? 0.2270 0.2175 0.1832 0.0161  -0.0144 0.0218  92  SER A CA  
556  C C   . SER A 66  ? 0.2300 0.2139 0.1841 0.0156  -0.0162 0.0218  92  SER A C   
557  O O   . SER A 66  ? 0.2362 0.2169 0.1926 0.0174  -0.0204 0.0213  92  SER A O   
558  C CB  . SER A 66  ? 0.2588 0.2486 0.2155 0.0131  -0.0171 0.0239  92  SER A CB  
559  O OG  . SER A 66  ? 0.3230 0.3199 0.2831 0.0130  -0.0160 0.0236  92  SER A OG  
560  N N   . LEU A 67  ? 0.2218 0.2033 0.1721 0.0130  -0.0136 0.0225  93  LEU A N   
561  C CA  . LEU A 67  ? 0.2167 0.1936 0.1657 0.0113  -0.0149 0.0226  93  LEU A CA  
562  C C   . LEU A 67  ? 0.2117 0.1876 0.1570 0.0060  -0.0137 0.0249  93  LEU A C   
563  O O   . LEU A 67  ? 0.2216 0.1994 0.1651 0.0050  -0.0104 0.0243  93  LEU A O   
564  C CB  . LEU A 67  ? 0.2193 0.1967 0.1676 0.0132  -0.0126 0.0204  93  LEU A CB  
565  C CG  . LEU A 67  ? 0.2395 0.2136 0.1883 0.0114  -0.0144 0.0200  93  LEU A CG  
566  C CD1 . LEU A 67  ? 0.2500 0.2210 0.2024 0.0139  -0.0189 0.0189  93  LEU A CD1 
567  C CD2 . LEU A 67  ? 0.2376 0.2132 0.1857 0.0123  -0.0120 0.0178  93  LEU A CD2 
568  N N   . PHE A 68  ? 0.1968 0.1699 0.1408 0.0028  -0.0166 0.0275  94  PHE A N   
569  C CA  . PHE A 68  ? 0.1996 0.1736 0.1391 -0.0023 -0.0153 0.0293  94  PHE A CA  
570  C C   . PHE A 68  ? 0.2175 0.1895 0.1553 -0.0060 -0.0162 0.0312  94  PHE A C   
571  O O   . PHE A 68  ? 0.2126 0.1806 0.1529 -0.0053 -0.0195 0.0323  94  PHE A O   
572  C CB  . PHE A 68  ? 0.1930 0.1674 0.1313 -0.0038 -0.0180 0.0316  94  PHE A CB  
573  C CG  . PHE A 68  ? 0.1940 0.1723 0.1330 -0.0030 -0.0157 0.0298  94  PHE A CG  
574  C CD1 . PHE A 68  ? 0.1886 0.1689 0.1319 0.0009  -0.0147 0.0281  94  PHE A CD1 
575  C CD2 . PHE A 68  ? 0.1989 0.1792 0.1342 -0.0065 -0.0146 0.0297  94  PHE A CD2 
576  C CE1 . PHE A 68  ? 0.1940 0.1776 0.1383 0.0005  -0.0125 0.0271  94  PHE A CE1 
577  C CE2 . PHE A 68  ? 0.2007 0.1835 0.1376 -0.0063 -0.0130 0.0278  94  PHE A CE2 
578  C CZ  . PHE A 68  ? 0.1913 0.1754 0.1329 -0.0032 -0.0119 0.0270  94  PHE A CZ  
579  N N   . LYS A 69  ? 0.2287 0.2040 0.1625 -0.0102 -0.0134 0.0313  95  LYS A N   
580  C CA  . LYS A 69  ? 0.2426 0.2180 0.1745 -0.0150 -0.0136 0.0338  95  LYS A CA  
581  C C   . LYS A 69  ? 0.2635 0.2343 0.1934 -0.0179 -0.0184 0.0393  95  LYS A C   
582  O O   . LYS A 69  ? 0.2666 0.2363 0.1948 -0.0170 -0.0208 0.0408  95  LYS A O   
583  C CB  . LYS A 69  ? 0.2604 0.2426 0.1882 -0.0189 -0.0095 0.0324  95  LYS A CB  
584  C CG  . LYS A 69  ? 0.3061 0.2918 0.2360 -0.0156 -0.0056 0.0268  95  LYS A CG  
585  C CD  . LYS A 69  ? 0.3509 0.3438 0.2779 -0.0187 -0.0020 0.0243  95  LYS A CD  
586  C CE  . LYS A 69  ? 0.3664 0.3615 0.2968 -0.0145 0.0007  0.0187  95  LYS A CE  
587  N NZ  . LYS A 69  ? 0.3701 0.3717 0.2981 -0.0158 0.0036  0.0145  95  LYS A NZ  
588  N N   . ASP A 70  ? 0.2746 0.2422 0.2052 -0.0212 -0.0204 0.0424  96  ASP A N   
589  C CA  . ASP A 70  ? 0.2918 0.2530 0.2204 -0.0245 -0.0259 0.0487  96  ASP A CA  
590  C C   . ASP A 70  ? 0.2896 0.2541 0.2102 -0.0289 -0.0257 0.0526  96  ASP A C   
591  O O   . ASP A 70  ? 0.2823 0.2545 0.1984 -0.0328 -0.0210 0.0518  96  ASP A O   
592  C CB  . ASP A 70  ? 0.3351 0.2936 0.2653 -0.0295 -0.0268 0.0516  96  ASP A CB  
593  C CG  . ASP A 70  ? 0.4099 0.3590 0.3391 -0.0326 -0.0335 0.0586  96  ASP A CG  
594  O OD1 . ASP A 70  ? 0.4234 0.3660 0.3548 -0.0278 -0.0387 0.0589  96  ASP A OD1 
595  O OD2 . ASP A 70  ? 0.4472 0.3956 0.3738 -0.0400 -0.0338 0.0640  96  ASP A OD2 
596  N N   . GLY A 71  ? 0.2915 0.2514 0.2107 -0.0276 -0.0310 0.0559  97  GLY A N   
597  C CA  . GLY A 71  ? 0.2986 0.2618 0.2099 -0.0313 -0.0318 0.0595  97  GLY A CA  
598  C C   . GLY A 71  ? 0.3061 0.2748 0.2170 -0.0278 -0.0299 0.0548  97  GLY A C   
599  O O   . GLY A 71  ? 0.3166 0.2884 0.2215 -0.0301 -0.0313 0.0568  97  GLY A O   
600  N N   . ILE A 72  ? 0.2927 0.2629 0.2099 -0.0226 -0.0271 0.0488  98  ILE A N   
601  C CA  . ILE A 72  ? 0.2955 0.2701 0.2138 -0.0199 -0.0255 0.0447  98  ILE A CA  
602  C C   . ILE A 72  ? 0.2998 0.2717 0.2252 -0.0143 -0.0287 0.0435  98  ILE A C   
603  O O   . ILE A 72  ? 0.2991 0.2694 0.2298 -0.0106 -0.0276 0.0410  98  ILE A O   
604  C CB  . ILE A 72  ? 0.2966 0.2761 0.2157 -0.0193 -0.0193 0.0391  98  ILE A CB  
605  C CG1 . ILE A 72  ? 0.3053 0.2893 0.2189 -0.0240 -0.0157 0.0388  98  ILE A CG1 
606  C CG2 . ILE A 72  ? 0.2970 0.2796 0.2172 -0.0176 -0.0185 0.0356  98  ILE A CG2 
607  C CD1 . ILE A 72  ? 0.3116 0.2997 0.2270 -0.0224 -0.0105 0.0327  98  ILE A CD1 
608  N N   . GLU A 73  ? 0.2982 0.2708 0.2236 -0.0133 -0.0327 0.0447  99  GLU A N   
609  C CA  . GLU A 73  ? 0.2952 0.2681 0.2282 -0.0079 -0.0353 0.0427  99  GLU A CA  
610  C C   . GLU A 73  ? 0.2853 0.2643 0.2216 -0.0065 -0.0304 0.0379  99  GLU A C   
611  O O   . GLU A 73  ? 0.2735 0.2556 0.2060 -0.0097 -0.0276 0.0367  99  GLU A O   
612  C CB  . GLU A 73  ? 0.3349 0.3075 0.2677 -0.0074 -0.0418 0.0455  99  GLU A CB  
613  C CG  . GLU A 73  ? 0.4425 0.4078 0.3707 -0.0096 -0.0473 0.0516  99  GLU A CG  
614  C CD  . GLU A 73  ? 0.5624 0.5265 0.4907 -0.0081 -0.0549 0.0546  99  GLU A CD  
615  O OE1 . GLU A 73  ? 0.5690 0.5321 0.5054 -0.0023 -0.0590 0.0527  99  GLU A OE1 
616  O OE2 . GLU A 73  ? 0.6330 0.5981 0.5533 -0.0123 -0.0568 0.0585  99  GLU A OE2 
617  N N   . PRO A 74  ? 0.2875 0.2681 0.2306 -0.0020 -0.0294 0.0351  100 PRO A N   
618  C CA  . PRO A 74  ? 0.2903 0.2762 0.2363 -0.0014 -0.0248 0.0318  100 PRO A CA  
619  C C   . PRO A 74  ? 0.2917 0.2833 0.2407 -0.0020 -0.0261 0.0311  100 PRO A C   
620  O O   . PRO A 74  ? 0.2837 0.2804 0.2391 0.0006  -0.0254 0.0292  100 PRO A O   
621  C CB  . PRO A 74  ? 0.2979 0.2847 0.2491 0.0034  -0.0235 0.0298  100 PRO A CB  
622  C CG  . PRO A 74  ? 0.3107 0.2927 0.2630 0.0058  -0.0280 0.0309  100 PRO A CG  
623  C CD  . PRO A 74  ? 0.2881 0.2661 0.2364 0.0028  -0.0325 0.0347  100 PRO A CD  
624  N N   . MET A 75  ? 0.2909 0.2827 0.2354 -0.0057 -0.0279 0.0321  101 MET A N   
625  C CA  . MET A 75  ? 0.2947 0.2919 0.2419 -0.0068 -0.0298 0.0310  101 MET A CA  
626  C C   . MET A 75  ? 0.2828 0.2803 0.2238 -0.0115 -0.0289 0.0302  101 MET A C   
627  O O   . MET A 75  ? 0.2742 0.2685 0.2080 -0.0137 -0.0282 0.0313  101 MET A O   
628  C CB  . MET A 75  ? 0.3079 0.3067 0.2581 -0.0043 -0.0364 0.0328  101 MET A CB  
629  C CG  . MET A 75  ? 0.3539 0.3474 0.2968 -0.0059 -0.0409 0.0368  101 MET A CG  
630  S SD  . MET A 75  ? 0.4312 0.4247 0.3782 -0.0019 -0.0500 0.0392  101 MET A SD  
631  C CE  . MET A 75  ? 0.3863 0.3710 0.3221 -0.0054 -0.0541 0.0458  101 MET A CE  
632  N N   . TRP A 76  ? 0.2780 0.2802 0.2226 -0.0132 -0.0287 0.0276  102 TRP A N   
633  C CA  . TRP A 76  ? 0.2965 0.2995 0.2366 -0.0173 -0.0283 0.0252  102 TRP A CA  
634  C C   . TRP A 76  ? 0.3097 0.3131 0.2417 -0.0190 -0.0326 0.0270  102 TRP A C   
635  O O   . TRP A 76  ? 0.3180 0.3213 0.2431 -0.0219 -0.0314 0.0251  102 TRP A O   
636  C CB  . TRP A 76  ? 0.2907 0.2987 0.2374 -0.0190 -0.0291 0.0224  102 TRP A CB  
637  C CG  . TRP A 76  ? 0.2976 0.3072 0.2527 -0.0182 -0.0256 0.0218  102 TRP A CG  
638  C CD1 . TRP A 76  ? 0.3136 0.3191 0.2687 -0.0176 -0.0208 0.0219  102 TRP A CD1 
639  C CD2 . TRP A 76  ? 0.2935 0.3102 0.2576 -0.0188 -0.0265 0.0210  102 TRP A CD2 
640  N NE1 . TRP A 76  ? 0.3152 0.3242 0.2777 -0.0180 -0.0187 0.0220  102 TRP A NE1 
641  C CE2 . TRP A 76  ? 0.3040 0.3206 0.2726 -0.0190 -0.0217 0.0214  102 TRP A CE2 
642  C CE3 . TRP A 76  ? 0.3003 0.3244 0.2694 -0.0191 -0.0311 0.0203  102 TRP A CE3 
643  C CZ2 . TRP A 76  ? 0.3094 0.3338 0.2871 -0.0203 -0.0207 0.0213  102 TRP A CZ2 
644  C CZ3 . TRP A 76  ? 0.3068 0.3390 0.2862 -0.0200 -0.0302 0.0194  102 TRP A CZ3 
645  C CH2 . TRP A 76  ? 0.3038 0.3365 0.2874 -0.0209 -0.0248 0.0200  102 TRP A CH2 
646  N N   . GLU A 77  ? 0.3105 0.3145 0.2433 -0.0171 -0.0377 0.0304  103 GLU A N   
647  C CA  . GLU A 77  ? 0.3272 0.3312 0.2523 -0.0185 -0.0430 0.0338  103 GLU A CA  
648  C C   . GLU A 77  ? 0.3352 0.3347 0.2508 -0.0207 -0.0414 0.0370  103 GLU A C   
649  O O   . GLU A 77  ? 0.3414 0.3423 0.2480 -0.0238 -0.0438 0.0391  103 GLU A O   
650  C CB  . GLU A 77  ? 0.3559 0.3598 0.2857 -0.0149 -0.0495 0.0370  103 GLU A CB  
651  C CG  . GLU A 77  ? 0.4001 0.4112 0.3391 -0.0132 -0.0522 0.0338  103 GLU A CG  
652  C CD  . GLU A 77  ? 0.4443 0.4585 0.3946 -0.0102 -0.0486 0.0309  103 GLU A CD  
653  O OE1 . GLU A 77  ? 0.4179 0.4291 0.3684 -0.0104 -0.0426 0.0301  103 GLU A OE1 
654  O OE2 . GLU A 77  ? 0.4774 0.4982 0.4365 -0.0077 -0.0517 0.0295  103 GLU A OE2 
655  N N   . ASP A 78  ? 0.3313 0.3265 0.2487 -0.0195 -0.0375 0.0376  104 ASP A N   
656  C CA  . ASP A 78  ? 0.3363 0.3286 0.2462 -0.0221 -0.0355 0.0406  104 ASP A CA  
657  C C   . ASP A 78  ? 0.3452 0.3421 0.2481 -0.0259 -0.0318 0.0371  104 ASP A C   
658  O O   . ASP A 78  ? 0.3427 0.3419 0.2490 -0.0254 -0.0287 0.0316  104 ASP A O   
659  C CB  . ASP A 78  ? 0.3472 0.3353 0.2618 -0.0199 -0.0318 0.0403  104 ASP A CB  
660  C CG  . ASP A 78  ? 0.4010 0.3858 0.3100 -0.0226 -0.0313 0.0443  104 ASP A CG  
661  O OD1 . ASP A 78  ? 0.4203 0.4086 0.3237 -0.0261 -0.0273 0.0429  104 ASP A OD1 
662  O OD2 . ASP A 78  ? 0.4084 0.3877 0.3195 -0.0213 -0.0348 0.0484  104 ASP A OD2 
663  N N   . GLU A 79  ? 0.3526 0.3511 0.2459 -0.0298 -0.0322 0.0404  105 GLU A N   
664  C CA  . GLU A 79  ? 0.3648 0.3697 0.2507 -0.0332 -0.0286 0.0365  105 GLU A CA  
665  C C   . GLU A 79  ? 0.3550 0.3605 0.2449 -0.0320 -0.0223 0.0307  105 GLU A C   
666  O O   . GLU A 79  ? 0.3620 0.3718 0.2507 -0.0324 -0.0199 0.0244  105 GLU A O   
667  C CB  . GLU A 79  ? 0.4298 0.4370 0.3050 -0.0378 -0.0293 0.0423  105 GLU A CB  
668  C CG  . GLU A 79  ? 0.5442 0.5606 0.4107 -0.0413 -0.0257 0.0380  105 GLU A CG  
669  C CD  . GLU A 79  ? 0.6708 0.6925 0.5323 -0.0418 -0.0291 0.0348  105 GLU A CD  
670  O OE1 . GLU A 79  ? 0.7094 0.7285 0.5705 -0.0412 -0.0353 0.0391  105 GLU A OE1 
671  O OE2 . GLU A 79  ? 0.7092 0.7378 0.5675 -0.0426 -0.0260 0.0275  105 GLU A OE2 
672  N N   . LYS A 80  ? 0.3404 0.3413 0.2354 -0.0302 -0.0201 0.0324  106 LYS A N   
673  C CA  . LYS A 80  ? 0.3370 0.3384 0.2359 -0.0286 -0.0148 0.0272  106 LYS A CA  
674  C C   . LYS A 80  ? 0.3250 0.3234 0.2318 -0.0249 -0.0141 0.0229  106 LYS A C   
675  O O   . LYS A 80  ? 0.3263 0.3242 0.2360 -0.0233 -0.0106 0.0187  106 LYS A O   
676  C CB  . LYS A 80  ? 0.3610 0.3597 0.2619 -0.0284 -0.0130 0.0302  106 LYS A CB  
677  C CG  . LYS A 80  ? 0.4385 0.4416 0.3321 -0.0332 -0.0120 0.0337  106 LYS A CG  
678  C CD  . LYS A 80  ? 0.5201 0.5322 0.4094 -0.0352 -0.0075 0.0279  106 LYS A CD  
679  C CE  . LYS A 80  ? 0.5841 0.6030 0.4664 -0.0406 -0.0055 0.0313  106 LYS A CE  
680  N NZ  . LYS A 80  ? 0.6266 0.6476 0.4995 -0.0450 -0.0090 0.0370  106 LYS A NZ  
681  N N   . ASN A 81  ? 0.3049 0.3019 0.2151 -0.0239 -0.0176 0.0240  107 ASN A N   
682  C CA  . ASN A 81  ? 0.2974 0.2927 0.2151 -0.0217 -0.0170 0.0210  107 ASN A CA  
683  C C   . ASN A 81  ? 0.3051 0.3032 0.2228 -0.0235 -0.0192 0.0177  107 ASN A C   
684  O O   . ASN A 81  ? 0.3071 0.3038 0.2300 -0.0231 -0.0180 0.0143  107 ASN A O   
685  C CB  . ASN A 81  ? 0.2903 0.2834 0.2142 -0.0189 -0.0188 0.0245  107 ASN A CB  
686  C CG  . ASN A 81  ? 0.2995 0.2893 0.2248 -0.0166 -0.0169 0.0266  107 ASN A CG  
687  O OD1 . ASN A 81  ? 0.3034 0.2920 0.2282 -0.0162 -0.0133 0.0245  107 ASN A OD1 
688  N ND2 . ASN A 81  ? 0.2786 0.2669 0.2062 -0.0147 -0.0199 0.0301  107 ASN A ND2 
689  N N   . LYS A 82  ? 0.3103 0.3122 0.2224 -0.0256 -0.0227 0.0188  108 LYS A N   
690  C CA  . LYS A 82  ? 0.3179 0.3235 0.2300 -0.0274 -0.0259 0.0156  108 LYS A CA  
691  C C   . LYS A 82  ? 0.3104 0.3158 0.2237 -0.0283 -0.0237 0.0083  108 LYS A C   
692  O O   . LYS A 82  ? 0.3117 0.3168 0.2312 -0.0289 -0.0252 0.0056  108 LYS A O   
693  C CB  . LYS A 82  ? 0.3572 0.3672 0.2598 -0.0297 -0.0296 0.0179  108 LYS A CB  
694  C CG  . LYS A 82  ? 0.4442 0.4587 0.3465 -0.0311 -0.0343 0.0153  108 LYS A CG  
695  C CD  . LYS A 82  ? 0.5193 0.5378 0.4114 -0.0329 -0.0388 0.0194  108 LYS A CD  
696  C CE  . LYS A 82  ? 0.5879 0.6113 0.4801 -0.0338 -0.0442 0.0166  108 LYS A CE  
697  N NZ  . LYS A 82  ? 0.6384 0.6660 0.5191 -0.0356 -0.0490 0.0205  108 LYS A NZ  
698  N N   . ARG A 83  ? 0.3022 0.3082 0.2108 -0.0284 -0.0205 0.0048  109 ARG A N   
699  C CA  . ARG A 83  ? 0.3060 0.3109 0.2163 -0.0283 -0.0190 -0.0029 109 ARG A CA  
700  C C   . ARG A 83  ? 0.2955 0.2935 0.2124 -0.0257 -0.0156 -0.0036 109 ARG A C   
701  O O   . ARG A 83  ? 0.2963 0.2920 0.2148 -0.0248 -0.0145 -0.0097 109 ARG A O   
702  C CB  . ARG A 83  ? 0.3360 0.3471 0.2376 -0.0292 -0.0176 -0.0076 109 ARG A CB  
703  C CG  . ARG A 83  ? 0.3976 0.4160 0.2905 -0.0321 -0.0209 -0.0064 109 ARG A CG  
704  C CD  . ARG A 83  ? 0.4761 0.5028 0.3591 -0.0334 -0.0186 -0.0099 109 ARG A CD  
705  N NE  . ARG A 83  ? 0.5592 0.5867 0.4400 -0.0334 -0.0146 -0.0053 109 ARG A NE  
706  C CZ  . ARG A 83  ? 0.6220 0.6508 0.4976 -0.0356 -0.0153 0.0031  109 ARG A CZ  
707  N NH1 . ARG A 83  ? 0.6335 0.6629 0.5051 -0.0374 -0.0201 0.0081  109 ARG A NH1 
708  N NH2 . ARG A 83  ? 0.6285 0.6579 0.5035 -0.0361 -0.0117 0.0065  109 ARG A NH2 
709  N N   . GLY A 84  ? 0.2783 0.2733 0.1990 -0.0241 -0.0145 0.0022  110 GLY A N   
710  C CA  . GLY A 84  ? 0.2661 0.2554 0.1917 -0.0216 -0.0117 0.0025  110 GLY A CA  
711  C C   . GLY A 84  ? 0.2475 0.2325 0.1806 -0.0216 -0.0122 0.0039  110 GLY A C   
712  O O   . GLY A 84  ? 0.2353 0.2210 0.1712 -0.0240 -0.0146 0.0026  110 GLY A O   
713  N N   . GLY A 85  ? 0.2406 0.2215 0.1767 -0.0192 -0.0099 0.0065  111 GLY A N   
714  C CA  . GLY A 85  ? 0.2297 0.2071 0.1719 -0.0196 -0.0096 0.0088  111 GLY A CA  
715  C C   . GLY A 85  ? 0.2255 0.2006 0.1686 -0.0164 -0.0071 0.0125  111 GLY A C   
716  O O   . GLY A 85  ? 0.2307 0.2072 0.1705 -0.0141 -0.0060 0.0132  111 GLY A O   
717  N N   . ARG A 86  ? 0.2086 0.1802 0.1557 -0.0167 -0.0062 0.0149  112 ARG A N   
718  C CA  . ARG A 86  ? 0.2159 0.1863 0.1632 -0.0137 -0.0040 0.0184  112 ARG A CA  
719  C C   . ARG A 86  ? 0.2271 0.1907 0.1762 -0.0139 -0.0032 0.0199  112 ARG A C   
720  O O   . ARG A 86  ? 0.2281 0.1887 0.1805 -0.0174 -0.0042 0.0202  112 ARG A O   
721  C CB  . ARG A 86  ? 0.2197 0.1967 0.1695 -0.0135 -0.0036 0.0222  112 ARG A CB  
722  C CG  . ARG A 86  ? 0.2614 0.2414 0.2166 -0.0175 -0.0041 0.0236  112 ARG A CG  
723  C CD  . ARG A 86  ? 0.2938 0.2821 0.2526 -0.0166 -0.0032 0.0266  112 ARG A CD  
724  N NE  . ARG A 86  ? 0.3304 0.3236 0.2954 -0.0209 -0.0036 0.0274  112 ARG A NE  
725  C CZ  . ARG A 86  ? 0.3336 0.3358 0.3035 -0.0211 -0.0023 0.0295  112 ARG A CZ  
726  N NH1 . ARG A 86  ? 0.3055 0.3122 0.2746 -0.0166 -0.0009 0.0305  112 ARG A NH1 
727  N NH2 . ARG A 86  ? 0.3213 0.3288 0.2977 -0.0257 -0.0026 0.0300  112 ARG A NH2 
728  N N   . TRP A 87  ? 0.2297 0.1905 0.1767 -0.0102 -0.0019 0.0212  113 TRP A N   
729  C CA  . TRP A 87  ? 0.2440 0.1982 0.1916 -0.0100 -0.0016 0.0242  113 TRP A CA  
730  C C   . TRP A 87  ? 0.2797 0.2395 0.2281 -0.0104 0.0004  0.0295  113 TRP A C   
731  O O   . TRP A 87  ? 0.2820 0.2470 0.2286 -0.0072 0.0015  0.0299  113 TRP A O   
732  C CB  . TRP A 87  ? 0.2367 0.1866 0.1816 -0.0052 -0.0016 0.0228  113 TRP A CB  
733  C CG  . TRP A 87  ? 0.2372 0.1812 0.1824 -0.0043 -0.0035 0.0173  113 TRP A CG  
734  C CD1 . TRP A 87  ? 0.2413 0.1883 0.1851 -0.0020 -0.0036 0.0117  113 TRP A CD1 
735  C CD2 . TRP A 87  ? 0.2434 0.1779 0.1909 -0.0056 -0.0059 0.0163  113 TRP A CD2 
736  N NE1 . TRP A 87  ? 0.2452 0.1865 0.1903 -0.0010 -0.0055 0.0066  113 TRP A NE1 
737  C CE2 . TRP A 87  ? 0.2504 0.1832 0.1981 -0.0032 -0.0074 0.0089  113 TRP A CE2 
738  C CE3 . TRP A 87  ? 0.2631 0.1907 0.2130 -0.0090 -0.0069 0.0208  113 TRP A CE3 
739  C CZ2 . TRP A 87  ? 0.2588 0.1820 0.2092 -0.0030 -0.0105 0.0053  113 TRP A CZ2 
740  C CZ3 . TRP A 87  ? 0.2695 0.1864 0.2219 -0.0098 -0.0103 0.0182  113 TRP A CZ3 
741  C CH2 . TRP A 87  ? 0.2669 0.1813 0.2198 -0.0063 -0.0123 0.0100  113 TRP A CH2 
742  N N   . LEU A 88  ? 0.2970 0.2564 0.2484 -0.0145 0.0009  0.0332  114 LEU A N   
743  C CA  . LEU A 88  ? 0.3124 0.2800 0.2650 -0.0154 0.0034  0.0377  114 LEU A CA  
744  C C   . LEU A 88  ? 0.3323 0.2967 0.2824 -0.0154 0.0050  0.0433  114 LEU A C   
745  O O   . LEU A 88  ? 0.3417 0.2970 0.2920 -0.0182 0.0038  0.0458  114 LEU A O   
746  C CB  . LEU A 88  ? 0.3136 0.2873 0.2720 -0.0207 0.0033  0.0381  114 LEU A CB  
747  C CG  . LEU A 88  ? 0.3424 0.3280 0.3037 -0.0214 0.0060  0.0413  114 LEU A CG  
748  C CD1 . LEU A 88  ? 0.3427 0.3366 0.3041 -0.0170 0.0057  0.0382  114 LEU A CD1 
749  C CD2 . LEU A 88  ? 0.3542 0.3444 0.3223 -0.0281 0.0062  0.0430  114 LEU A CD2 
750  N N   . ILE A 89  ? 0.3362 0.3077 0.2836 -0.0121 0.0071  0.0452  115 ILE A N   
751  C CA  . ILE A 89  ? 0.3524 0.3238 0.2960 -0.0118 0.0089  0.0508  115 ILE A CA  
752  C C   . ILE A 89  ? 0.3627 0.3471 0.3084 -0.0142 0.0123  0.0538  115 ILE A C   
753  O O   . ILE A 89  ? 0.3407 0.3351 0.2883 -0.0114 0.0131  0.0503  115 ILE A O   
754  C CB  . ILE A 89  ? 0.3777 0.3473 0.3156 -0.0053 0.0084  0.0496  115 ILE A CB  
755  C CG1 . ILE A 89  ? 0.4096 0.3679 0.3468 -0.0032 0.0053  0.0461  115 ILE A CG1 
756  C CG2 . ILE A 89  ? 0.3907 0.3615 0.3235 -0.0049 0.0100  0.0557  115 ILE A CG2 
757  C CD1 . ILE A 89  ? 0.4412 0.3985 0.3748 0.0025  0.0044  0.0440  115 ILE A CD1 
758  N N   . THR A 90  ? 0.3892 0.3739 0.3354 -0.0197 0.0140  0.0600  116 THR A N   
759  C CA  . THR A 90  ? 0.4138 0.4127 0.3627 -0.0231 0.0179  0.0632  116 THR A CA  
760  C C   . THR A 90  ? 0.4354 0.4390 0.3774 -0.0217 0.0208  0.0686  116 THR A C   
761  O O   . THR A 90  ? 0.4465 0.4396 0.3827 -0.0223 0.0196  0.0736  116 THR A O   
762  C CB  . THR A 90  ? 0.4465 0.4446 0.4021 -0.0316 0.0179  0.0662  116 THR A CB  
763  O OG1 . THR A 90  ? 0.4609 0.4584 0.4224 -0.0317 0.0153  0.0600  116 THR A OG1 
764  C CG2 . THR A 90  ? 0.4485 0.4622 0.4075 -0.0366 0.0225  0.0706  116 THR A CG2 
765  N N   . LEU A 91  ? 0.4388 0.4581 0.3808 -0.0190 0.0239  0.0669  117 LEU A N   
766  C CA  . LEU A 91  ? 0.4536 0.4804 0.3883 -0.0172 0.0270  0.0709  117 LEU A CA  
767  C C   . LEU A 91  ? 0.4773 0.5212 0.4152 -0.0225 0.0320  0.0746  117 LEU A C   
768  O O   . LEU A 91  ? 0.4744 0.5290 0.4208 -0.0236 0.0330  0.0703  117 LEU A O   
769  C CB  . LEU A 91  ? 0.4523 0.4850 0.3839 -0.0083 0.0264  0.0644  117 LEU A CB  
770  C CG  . LEU A 91  ? 0.4780 0.4971 0.4052 -0.0028 0.0222  0.0614  117 LEU A CG  
771  C CD1 . LEU A 91  ? 0.4816 0.4953 0.4148 -0.0012 0.0191  0.0549  117 LEU A CD1 
772  C CD2 . LEU A 91  ? 0.4868 0.5124 0.4083 0.0042  0.0223  0.0583  117 LEU A CD2 
773  N N   . ASN A 92  ? 0.5035 0.5511 0.4348 -0.0259 0.0351  0.0824  118 ASN A N   
774  C CA  . ASN A 92  ? 0.5252 0.5919 0.4591 -0.0313 0.0408  0.0859  118 ASN A CA  
775  C C   . ASN A 92  ? 0.5383 0.6236 0.4693 -0.0243 0.0439  0.0806  118 ASN A C   
776  O O   . ASN A 92  ? 0.5394 0.6204 0.4656 -0.0160 0.0413  0.0753  118 ASN A O   
777  C CB  . ASN A 92  ? 0.5518 0.6149 0.4810 -0.0404 0.0430  0.0978  118 ASN A CB  
778  C CG  . ASN A 92  ? 0.6070 0.6587 0.5236 -0.0380 0.0412  0.1039  118 ASN A CG  
779  O OD1 . ASN A 92  ? 0.6318 0.6894 0.5409 -0.0307 0.0417  0.1011  118 ASN A OD1 
780  N ND2 . ASN A 92  ? 0.6237 0.6584 0.5380 -0.0440 0.0385  0.1123  118 ASN A ND2 
781  N N   . LYS A 93  ? 0.5428 0.6495 0.4775 -0.0275 0.0494  0.0812  119 LYS A N   
782  C CA  . LYS A 93  ? 0.5586 0.6854 0.4916 -0.0208 0.0527  0.0750  119 LYS A CA  
783  C C   . LYS A 93  ? 0.5833 0.7079 0.5028 -0.0154 0.0525  0.0766  119 LYS A C   
784  O O   . LYS A 93  ? 0.5893 0.7194 0.5073 -0.0064 0.0512  0.0682  119 LYS A O   
785  C CB  . LYS A 93  ? 0.5836 0.7343 0.5217 -0.0267 0.0594  0.0773  119 LYS A CB  
786  C CG  . LYS A 93  ? 0.6363 0.7928 0.5892 -0.0303 0.0590  0.0734  119 LYS A CG  
787  C CD  . LYS A 93  ? 0.6897 0.8659 0.6482 -0.0398 0.0655  0.0789  119 LYS A CD  
788  C CE  . LYS A 93  ? 0.7405 0.9157 0.7127 -0.0459 0.0638  0.0779  119 LYS A CE  
789  N NZ  . LYS A 93  ? 0.7717 0.9655 0.7503 -0.0566 0.0699  0.0839  119 LYS A NZ  
790  N N   . GLN A 94  ? 0.5982 0.7133 0.5084 -0.0208 0.0529  0.0872  120 GLN A N   
791  C CA  . GLN A 94  ? 0.6175 0.7292 0.5140 -0.0164 0.0520  0.0902  120 GLN A CA  
792  C C   . GLN A 94  ? 0.6251 0.7210 0.5196 -0.0076 0.0457  0.0835  120 GLN A C   
793  O O   . GLN A 94  ? 0.6307 0.7297 0.5169 -0.0009 0.0447  0.0807  120 GLN A O   
794  C CB  . GLN A 94  ? 0.6542 0.7550 0.5422 -0.0246 0.0523  0.1041  120 GLN A CB  
795  C CG  . GLN A 94  ? 0.7133 0.8323 0.5980 -0.0330 0.0592  0.1128  120 GLN A CG  
796  C CD  . GLN A 94  ? 0.7705 0.8974 0.6683 -0.0414 0.0625  0.1135  120 GLN A CD  
797  O OE1 . GLN A 94  ? 0.7861 0.8967 0.6915 -0.0458 0.0589  0.1149  120 GLN A OE1 
798  N NE2 . GLN A 94  ? 0.7719 0.9250 0.6730 -0.0435 0.0691  0.1117  120 GLN A NE2 
799  N N   . GLN A 95  ? 0.6237 0.7037 0.5257 -0.0080 0.0414  0.0809  121 GLN A N   
800  C CA  . GLN A 95  ? 0.6287 0.6940 0.5295 -0.0009 0.0357  0.0753  121 GLN A CA  
801  C C   . GLN A 95  ? 0.6262 0.6984 0.5318 0.0070  0.0343  0.0639  121 GLN A C   
802  O O   . GLN A 95  ? 0.6368 0.6981 0.5417 0.0121  0.0299  0.0594  121 GLN A O   
803  C CB  . GLN A 95  ? 0.6390 0.6850 0.5449 -0.0045 0.0318  0.0770  121 GLN A CB  
804  C CG  . GLN A 95  ? 0.6598 0.6925 0.5597 -0.0098 0.0306  0.0871  121 GLN A CG  
805  C CD  . GLN A 95  ? 0.6878 0.7031 0.5939 -0.0126 0.0267  0.0870  121 GLN A CD  
806  O OE1 . GLN A 95  ? 0.6909 0.7064 0.6045 -0.0190 0.0278  0.0881  121 GLN A OE1 
807  N NE2 . GLN A 95  ? 0.6952 0.6961 0.5984 -0.0079 0.0219  0.0850  121 GLN A NE2 
808  N N   . ARG A 96  ? 0.6117 0.7015 0.5230 0.0080  0.0376  0.0590  122 ARG A N   
809  C CA  . ARG A 96  ? 0.6084 0.7032 0.5249 0.0158  0.0352  0.0481  122 ARG A CA  
810  C C   . ARG A 96  ? 0.6083 0.7043 0.5169 0.0235  0.0333  0.0437  122 ARG A C   
811  O O   . ARG A 96  ? 0.6116 0.6987 0.5221 0.0287  0.0286  0.0376  122 ARG A O   
812  C CB  . ARG A 96  ? 0.6135 0.7276 0.5384 0.0160  0.0386  0.0433  122 ARG A CB  
813  C CG  . ARG A 96  ? 0.6417 0.7598 0.5722 0.0247  0.0352  0.0320  122 ARG A CG  
814  C CD  . ARG A 96  ? 0.6629 0.7970 0.6037 0.0253  0.0371  0.0269  122 ARG A CD  
815  N NE  . ARG A 96  ? 0.6848 0.8120 0.6341 0.0199  0.0357  0.0293  122 ARG A NE  
816  C CZ  . ARG A 96  ? 0.6995 0.8373 0.6595 0.0202  0.0358  0.0249  122 ARG A CZ  
817  N NH1 . ARG A 96  ? 0.6905 0.8465 0.6549 0.0261  0.0371  0.0174  122 ARG A NH1 
818  N NH2 . ARG A 96  ? 0.6900 0.8210 0.6567 0.0151  0.0340  0.0273  122 ARG A NH2 
819  N N   . ARG A 97  ? 0.6005 0.7080 0.5001 0.0237  0.0367  0.0469  123 ARG A N   
820  C CA  . ARG A 97  ? 0.6008 0.7110 0.4922 0.0309  0.0347  0.0425  123 ARG A CA  
821  C C   . ARG A 97  ? 0.5895 0.6825 0.4731 0.0311  0.0308  0.0475  123 ARG A C   
822  O O   . ARG A 97  ? 0.5967 0.6858 0.4777 0.0376  0.0267  0.0418  123 ARG A O   
823  C CB  . ARG A 97  ? 0.6241 0.7552 0.5080 0.0315  0.0399  0.0434  123 ARG A CB  
824  C CG  . ARG A 97  ? 0.6879 0.8242 0.5634 0.0398  0.0376  0.0371  123 ARG A CG  
825  C CD  . ARG A 97  ? 0.7494 0.9058 0.6144 0.0398  0.0428  0.0395  123 ARG A CD  
826  N NE  . ARG A 97  ? 0.8040 0.9574 0.6595 0.0318  0.0458  0.0536  123 ARG A NE  
827  C CZ  . ARG A 97  ? 0.8416 1.0064 0.6976 0.0239  0.0520  0.0610  123 ARG A CZ  
828  N NH1 . ARG A 97  ? 0.8298 1.0110 0.6959 0.0235  0.0561  0.0550  123 ARG A NH1 
829  N NH2 . ARG A 97  ? 0.8526 1.0123 0.6997 0.0163  0.0538  0.0744  123 ARG A NH2 
830  N N   . SER A 98  ? 0.5690 0.6518 0.4498 0.0243  0.0314  0.0577  124 SER A N   
831  C CA  . SER A 98  ? 0.5629 0.6300 0.4367 0.0249  0.0273  0.0626  124 SER A CA  
832  C C   . SER A 98  ? 0.5411 0.5901 0.4215 0.0254  0.0225  0.0603  124 SER A C   
833  O O   . SER A 98  ? 0.5583 0.5966 0.4341 0.0282  0.0185  0.0614  124 SER A O   
834  C CB  . SER A 98  ? 0.5874 0.6514 0.4537 0.0180  0.0295  0.0752  124 SER A CB  
835  O OG  . SER A 98  ? 0.6164 0.6734 0.4903 0.0105  0.0307  0.0797  124 SER A OG  
836  N N   . ASP A 99  ? 0.5031 0.5488 0.3936 0.0224  0.0229  0.0578  125 ASP A N   
837  C CA  . ASP A 99  ? 0.4804 0.5102 0.3761 0.0220  0.0189  0.0563  125 ASP A CA  
838  C C   . ASP A 99  ? 0.4321 0.4616 0.3371 0.0240  0.0174  0.0480  125 ASP A C   
839  O O   . ASP A 99  ? 0.4310 0.4514 0.3377 0.0267  0.0137  0.0444  125 ASP A O   
840  C CB  . ASP A 99  ? 0.5203 0.5405 0.4177 0.0146  0.0195  0.0640  125 ASP A CB  
841  C CG  . ASP A 99  ? 0.6108 0.6236 0.4993 0.0127  0.0187  0.0729  125 ASP A CG  
842  O OD1 . ASP A 99  ? 0.6148 0.6288 0.4955 0.0176  0.0171  0.0731  125 ASP A OD1 
843  O OD2 . ASP A 99  ? 0.6599 0.6652 0.5495 0.0062  0.0191  0.0798  125 ASP A OD2 
844  N N   . LEU A 100 ? 0.3900 0.4295 0.3011 0.0226  0.0198  0.0455  126 LEU A N   
845  C CA  . LEU A 100 ? 0.3606 0.3994 0.2803 0.0239  0.0179  0.0390  126 LEU A CA  
846  C C   . LEU A 100 ? 0.3421 0.3760 0.2626 0.0298  0.0137  0.0322  126 LEU A C   
847  O O   . LEU A 100 ? 0.3373 0.3617 0.2616 0.0288  0.0111  0.0307  126 LEU A O   
848  C CB  . LEU A 100 ? 0.3490 0.4027 0.2742 0.0240  0.0206  0.0361  126 LEU A CB  
849  C CG  . LEU A 100 ? 0.3629 0.4152 0.2972 0.0246  0.0181  0.0309  126 LEU A CG  
850  C CD1 . LEU A 100 ? 0.3723 0.4146 0.3098 0.0187  0.0173  0.0347  126 LEU A CD1 
851  C CD2 . LEU A 100 ? 0.3648 0.4327 0.3050 0.0260  0.0201  0.0273  126 LEU A CD2 
852  N N   . ASP A 101 ? 0.3306 0.3714 0.2476 0.0353  0.0131  0.0281  127 ASP A N   
853  C CA  . ASP A 101 ? 0.3319 0.3684 0.2507 0.0402  0.0088  0.0214  127 ASP A CA  
854  C C   . ASP A 101 ? 0.3229 0.3483 0.2387 0.0403  0.0062  0.0229  127 ASP A C   
855  O O   . ASP A 101 ? 0.3316 0.3504 0.2516 0.0411  0.0031  0.0192  127 ASP A O   
856  C CB  . ASP A 101 ? 0.3612 0.4084 0.2780 0.0464  0.0082  0.0154  127 ASP A CB  
857  C CG  . ASP A 101 ? 0.4270 0.4851 0.3496 0.0481  0.0094  0.0108  127 ASP A CG  
858  O OD1 . ASP A 101 ? 0.4386 0.4941 0.3681 0.0453  0.0092  0.0112  127 ASP A OD1 
859  O OD2 . ASP A 101 ? 0.4595 0.5295 0.3798 0.0527  0.0103  0.0063  127 ASP A OD2 
860  N N   . ARG A 102 ? 0.3071 0.3308 0.2159 0.0394  0.0073  0.0285  128 ARG A N   
861  C CA  . ARG A 102 ? 0.3005 0.3140 0.2069 0.0400  0.0045  0.0298  128 ARG A CA  
862  C C   . ARG A 102 ? 0.2833 0.2870 0.1952 0.0358  0.0040  0.0312  128 ARG A C   
863  O O   . ARG A 102 ? 0.2760 0.2738 0.1909 0.0368  0.0014  0.0278  128 ARG A O   
864  C CB  . ARG A 102 ? 0.3207 0.3335 0.2182 0.0400  0.0051  0.0364  128 ARG A CB  
865  C CG  . ARG A 102 ? 0.3770 0.3789 0.2733 0.0412  0.0015  0.0376  128 ARG A CG  
866  C CD  . ARG A 102 ? 0.4374 0.4374 0.3245 0.0425  0.0005  0.0438  128 ARG A CD  
867  N NE  . ARG A 102 ? 0.5147 0.5155 0.3978 0.0375  0.0039  0.0521  128 ARG A NE  
868  C CZ  . ARG A 102 ? 0.5624 0.5534 0.4475 0.0326  0.0040  0.0576  128 ARG A CZ  
869  N NH1 . ARG A 102 ? 0.5873 0.5678 0.4781 0.0327  0.0013  0.0549  128 ARG A NH1 
870  N NH2 . ARG A 102 ? 0.5454 0.5376 0.4271 0.0274  0.0069  0.0654  128 ARG A NH2 
871  N N   . PHE A 103 ? 0.2774 0.2804 0.1906 0.0308  0.0066  0.0356  129 PHE A N   
872  C CA  . PHE A 103 ? 0.2807 0.2752 0.1985 0.0267  0.0062  0.0365  129 PHE A CA  
873  C C   . PHE A 103 ? 0.2460 0.2405 0.1700 0.0269  0.0048  0.0311  129 PHE A C   
874  O O   . PHE A 103 ? 0.2358 0.2235 0.1621 0.0256  0.0033  0.0297  129 PHE A O   
875  C CB  . PHE A 103 ? 0.2988 0.2945 0.2178 0.0212  0.0090  0.0416  129 PHE A CB  
876  C CG  . PHE A 103 ? 0.3368 0.3270 0.2511 0.0184  0.0096  0.0486  129 PHE A CG  
877  C CD1 . PHE A 103 ? 0.3560 0.3414 0.2644 0.0216  0.0076  0.0506  129 PHE A CD1 
878  C CD2 . PHE A 103 ? 0.3614 0.3516 0.2775 0.0124  0.0118  0.0535  129 PHE A CD2 
879  C CE1 . PHE A 103 ? 0.3724 0.3514 0.2760 0.0190  0.0074  0.0580  129 PHE A CE1 
880  C CE2 . PHE A 103 ? 0.3773 0.3612 0.2893 0.0091  0.0118  0.0608  129 PHE A CE2 
881  C CZ  . PHE A 103 ? 0.3744 0.3521 0.2798 0.0126  0.0095  0.0633  129 PHE A CZ  
882  N N   . TRP A 104 ? 0.2243 0.2265 0.1509 0.0284  0.0051  0.0280  130 TRP A N   
883  C CA  . TRP A 104 ? 0.2179 0.2189 0.1500 0.0283  0.0031  0.0239  130 TRP A CA  
884  C C   . TRP A 104 ? 0.2108 0.2080 0.1433 0.0310  0.0001  0.0201  130 TRP A C   
885  O O   . TRP A 104 ? 0.1948 0.1871 0.1303 0.0289  -0.0013 0.0190  130 TRP A O   
886  C CB  . TRP A 104 ? 0.2125 0.2218 0.1483 0.0297  0.0033  0.0215  130 TRP A CB  
887  C CG  . TRP A 104 ? 0.2322 0.2388 0.1733 0.0297  0.0003  0.0183  130 TRP A CG  
888  C CD1 . TRP A 104 ? 0.2451 0.2534 0.1891 0.0336  -0.0026 0.0137  130 TRP A CD1 
889  C CD2 . TRP A 104 ? 0.2364 0.2377 0.1801 0.0255  -0.0006 0.0198  130 TRP A CD2 
890  N NE1 . TRP A 104 ? 0.2536 0.2572 0.2018 0.0317  -0.0054 0.0131  130 TRP A NE1 
891  C CE2 . TRP A 104 ? 0.2488 0.2487 0.1963 0.0267  -0.0040 0.0170  130 TRP A CE2 
892  C CE3 . TRP A 104 ? 0.2441 0.2413 0.1870 0.0208  0.0009  0.0231  130 TRP A CE3 
893  C CZ2 . TRP A 104 ? 0.2596 0.2552 0.2091 0.0233  -0.0058 0.0181  130 TRP A CZ2 
894  C CZ3 . TRP A 104 ? 0.2570 0.2510 0.2024 0.0178  -0.0008 0.0231  130 TRP A CZ3 
895  C CH2 . TRP A 104 ? 0.2574 0.2508 0.2055 0.0189  -0.0039 0.0210  130 TRP A CH2 
896  N N   . LEU A 105 ? 0.2093 0.2094 0.1387 0.0353  -0.0008 0.0181  131 LEU A N   
897  C CA  . LEU A 105 ? 0.2146 0.2118 0.1454 0.0375  -0.0039 0.0141  131 LEU A CA  
898  C C   . LEU A 105 ? 0.2179 0.2088 0.1483 0.0355  -0.0041 0.0157  131 LEU A C   
899  O O   . LEU A 105 ? 0.2189 0.2069 0.1530 0.0341  -0.0056 0.0134  131 LEU A O   
900  C CB  . LEU A 105 ? 0.2170 0.2193 0.1447 0.0428  -0.0055 0.0108  131 LEU A CB  
901  C CG  . LEU A 105 ? 0.2432 0.2431 0.1732 0.0448  -0.0091 0.0063  131 LEU A CG  
902  C CD1 . LEU A 105 ? 0.2425 0.2395 0.1793 0.0429  -0.0114 0.0031  131 LEU A CD1 
903  C CD2 . LEU A 105 ? 0.2575 0.2630 0.1837 0.0501  -0.0109 0.0028  131 LEU A CD2 
904  N N   . GLU A 106 ? 0.2170 0.2060 0.1434 0.0351  -0.0026 0.0197  132 GLU A N   
905  C CA  . GLU A 106 ? 0.2196 0.2024 0.1463 0.0341  -0.0032 0.0205  132 GLU A CA  
906  C C   . GLU A 106 ? 0.2249 0.2043 0.1555 0.0297  -0.0024 0.0202  132 GLU A C   
907  O O   . GLU A 106 ? 0.2314 0.2087 0.1645 0.0292  -0.0033 0.0178  132 GLU A O   
908  C CB  . GLU A 106 ? 0.2347 0.2145 0.1564 0.0346  -0.0027 0.0253  132 GLU A CB  
909  C CG  . GLU A 106 ? 0.2597 0.2424 0.1762 0.0394  -0.0043 0.0255  132 GLU A CG  
910  C CD  . GLU A 106 ? 0.3322 0.3114 0.2424 0.0397  -0.0043 0.0317  132 GLU A CD  
911  O OE1 . GLU A 106 ? 0.3365 0.3098 0.2472 0.0360  -0.0032 0.0357  132 GLU A OE1 
912  O OE2 . GLU A 106 ? 0.3349 0.3171 0.2394 0.0434  -0.0057 0.0327  132 GLU A OE2 
913  N N   . THR A 107 ? 0.2173 0.1981 0.1490 0.0267  -0.0008 0.0219  133 THR A N   
914  C CA  . THR A 107 ? 0.2159 0.1946 0.1506 0.0226  -0.0004 0.0217  133 THR A CA  
915  C C   . THR A 107 ? 0.2252 0.2051 0.1630 0.0221  -0.0020 0.0184  133 THR A C   
916  O O   . THR A 107 ? 0.2356 0.2137 0.1746 0.0197  -0.0020 0.0172  133 THR A O   
917  C CB  . THR A 107 ? 0.2194 0.2004 0.1548 0.0200  0.0010  0.0242  133 THR A CB  
918  O OG1 . THR A 107 ? 0.2243 0.2042 0.1573 0.0191  0.0026  0.0280  133 THR A OG1 
919  C CG2 . THR A 107 ? 0.2286 0.2081 0.1665 0.0161  0.0008  0.0238  133 THR A CG2 
920  N N   . LEU A 108 ? 0.2135 0.1963 0.1523 0.0243  -0.0034 0.0168  134 LEU A N   
921  C CA  . LEU A 108 ? 0.2139 0.1964 0.1559 0.0235  -0.0057 0.0145  134 LEU A CA  
922  C C   . LEU A 108 ? 0.2183 0.2001 0.1613 0.0235  -0.0063 0.0122  134 LEU A C   
923  O O   . LEU A 108 ? 0.2089 0.1901 0.1540 0.0201  -0.0067 0.0118  134 LEU A O   
924  C CB  . LEU A 108 ? 0.2038 0.1887 0.1472 0.0270  -0.0078 0.0123  134 LEU A CB  
925  C CG  . LEU A 108 ? 0.2294 0.2172 0.1736 0.0278  -0.0076 0.0131  134 LEU A CG  
926  C CD1 . LEU A 108 ? 0.2273 0.2187 0.1728 0.0327  -0.0097 0.0094  134 LEU A CD1 
927  C CD2 . LEU A 108 ? 0.2467 0.2318 0.1936 0.0243  -0.0090 0.0145  134 LEU A CD2 
928  N N   . LEU A 109 ? 0.2219 0.2048 0.1633 0.0272  -0.0065 0.0110  135 LEU A N   
929  C CA  . LEU A 109 ? 0.2356 0.2193 0.1789 0.0281  -0.0075 0.0083  135 LEU A CA  
930  C C   . LEU A 109 ? 0.2503 0.2330 0.1942 0.0257  -0.0058 0.0084  135 LEU A C   
931  O O   . LEU A 109 ? 0.2470 0.2322 0.1943 0.0241  -0.0059 0.0058  135 LEU A O   
932  C CB  . LEU A 109 ? 0.2387 0.2241 0.1796 0.0333  -0.0088 0.0071  135 LEU A CB  
933  C CG  . LEU A 109 ? 0.2632 0.2512 0.2041 0.0362  -0.0110 0.0049  135 LEU A CG  
934  C CD1 . LEU A 109 ? 0.2593 0.2498 0.1957 0.0414  -0.0121 0.0044  135 LEU A CD1 
935  C CD2 . LEU A 109 ? 0.2755 0.2643 0.2221 0.0347  -0.0135 0.0010  135 LEU A CD2 
936  N N   . CYS A 110 ? 0.2671 0.2469 0.2083 0.0251  -0.0042 0.0109  136 CYS A N   
937  C CA  . CYS A 110 ? 0.2844 0.2624 0.2261 0.0232  -0.0030 0.0104  136 CYS A CA  
938  C C   . CYS A 110 ? 0.2829 0.2633 0.2265 0.0184  -0.0020 0.0094  136 CYS A C   
939  O O   . CYS A 110 ? 0.2923 0.2753 0.2377 0.0172  -0.0013 0.0066  136 CYS A O   
940  C CB  . CYS A 110 ? 0.3233 0.2969 0.2621 0.0225  -0.0020 0.0138  136 CYS A CB  
941  S SG  . CYS A 110 ? 0.4560 0.4242 0.3940 0.0251  -0.0028 0.0137  136 CYS A SG  
942  N N   . LEU A 111 ? 0.2619 0.2420 0.2048 0.0159  -0.0022 0.0118  137 LEU A N   
943  C CA  . LEU A 111 ? 0.2550 0.2364 0.1984 0.0112  -0.0020 0.0124  137 LEU A CA  
944  C C   . LEU A 111 ? 0.2378 0.2223 0.1838 0.0095  -0.0028 0.0108  137 LEU A C   
945  O O   . LEU A 111 ? 0.2359 0.2241 0.1825 0.0065  -0.0013 0.0095  137 LEU A O   
946  C CB  . LEU A 111 ? 0.2542 0.2338 0.1968 0.0102  -0.0033 0.0154  137 LEU A CB  
947  C CG  . LEU A 111 ? 0.2872 0.2654 0.2281 0.0099  -0.0024 0.0174  137 LEU A CG  
948  C CD1 . LEU A 111 ? 0.2991 0.2775 0.2407 0.0092  -0.0041 0.0195  137 LEU A CD1 
949  C CD2 . LEU A 111 ? 0.2918 0.2699 0.2314 0.0068  -0.0011 0.0167  137 LEU A CD2 
950  N N   . ILE A 112 ? 0.2254 0.2093 0.1734 0.0114  -0.0049 0.0106  138 ILE A N   
951  C CA  . ILE A 112 ? 0.2204 0.2064 0.1719 0.0090  -0.0063 0.0096  138 ILE A CA  
952  C C   . ILE A 112 ? 0.2161 0.2074 0.1706 0.0096  -0.0053 0.0059  138 ILE A C   
953  O O   . ILE A 112 ? 0.2112 0.2063 0.1690 0.0057  -0.0053 0.0052  138 ILE A O   
954  C CB  . ILE A 112 ? 0.2222 0.2052 0.1756 0.0111  -0.0097 0.0095  138 ILE A CB  
955  C CG1 . ILE A 112 ? 0.2319 0.2161 0.1855 0.0171  -0.0106 0.0064  138 ILE A CG1 
956  C CG2 . ILE A 112 ? 0.2261 0.2051 0.1776 0.0109  -0.0109 0.0124  138 ILE A CG2 
957  C CD1 . ILE A 112 ? 0.2543 0.2376 0.2107 0.0195  -0.0143 0.0040  138 ILE A CD1 
958  N N   . GLY A 113 ? 0.2098 0.2015 0.1636 0.0144  -0.0048 0.0038  139 GLY A N   
959  C CA  . GLY A 113 ? 0.2194 0.2162 0.1765 0.0164  -0.0044 -0.0002 139 GLY A CA  
960  C C   . GLY A 113 ? 0.2309 0.2312 0.1882 0.0146  -0.0017 -0.0020 139 GLY A C   
961  O O   . GLY A 113 ? 0.2343 0.2400 0.1952 0.0165  -0.0013 -0.0061 139 GLY A O   
962  N N   . GLU A 114 ? 0.2373 0.2354 0.1909 0.0112  0.0000  0.0005  140 GLU A N   
963  C CA  . GLU A 114 ? 0.2517 0.2536 0.2048 0.0095  0.0024  -0.0019 140 GLU A CA  
964  C C   . GLU A 114 ? 0.2672 0.2679 0.2216 0.0150  0.0020  -0.0058 140 GLU A C   
965  O O   . GLU A 114 ? 0.2637 0.2708 0.2215 0.0161  0.0030  -0.0107 140 GLU A O   
966  C CB  . GLU A 114 ? 0.2690 0.2807 0.2251 0.0048  0.0044  -0.0040 140 GLU A CB  
967  C CG  . GLU A 114 ? 0.3337 0.3452 0.2886 -0.0013 0.0040  0.0006  140 GLU A CG  
968  C CD  . GLU A 114 ? 0.4469 0.4546 0.3961 -0.0049 0.0043  0.0048  140 GLU A CD  
969  O OE1 . GLU A 114 ? 0.4867 0.4947 0.4330 -0.0041 0.0057  0.0031  140 GLU A OE1 
970  O OE2 . GLU A 114 ? 0.4585 0.4625 0.4063 -0.0083 0.0025  0.0094  140 GLU A OE2 
971  N N   . SER A 115 ? 0.2718 0.2645 0.2236 0.0186  0.0003  -0.0034 141 SER A N   
972  C CA  . SER A 115 ? 0.2775 0.2667 0.2301 0.0239  -0.0011 -0.0055 141 SER A CA  
973  C C   . SER A 115 ? 0.2752 0.2629 0.2278 0.0238  -0.0004 -0.0086 141 SER A C   
974  O O   . SER A 115 ? 0.2732 0.2575 0.2275 0.0284  -0.0022 -0.0112 141 SER A O   
975  C CB  . SER A 115 ? 0.2942 0.2755 0.2431 0.0265  -0.0029 -0.0008 141 SER A CB  
976  O OG  . SER A 115 ? 0.3166 0.2999 0.2654 0.0274  -0.0039 0.0006  141 SER A OG  
977  N N   . PHE A 116 ? 0.2739 0.2635 0.2245 0.0190  0.0017  -0.0084 142 PHE A N   
978  C CA  . PHE A 116 ? 0.2866 0.2749 0.2369 0.0189  0.0020  -0.0120 142 PHE A CA  
979  C C   . PHE A 116 ? 0.3129 0.3117 0.2663 0.0186  0.0039  -0.0190 142 PHE A C   
980  O O   . PHE A 116 ? 0.3172 0.3170 0.2700 0.0182  0.0045  -0.0232 142 PHE A O   
981  C CB  . PHE A 116 ? 0.2720 0.2565 0.2180 0.0144  0.0026  -0.0083 142 PHE A CB  
982  C CG  . PHE A 116 ? 0.2677 0.2446 0.2118 0.0147  0.0012  -0.0020 142 PHE A CG  
983  C CD1 . PHE A 116 ? 0.2685 0.2371 0.2127 0.0177  -0.0006 -0.0008 142 PHE A CD1 
984  C CD2 . PHE A 116 ? 0.2690 0.2472 0.2114 0.0121  0.0016  0.0025  142 PHE A CD2 
985  C CE1 . PHE A 116 ? 0.2794 0.2432 0.2215 0.0174  -0.0012 0.0051  142 PHE A CE1 
986  C CE2 . PHE A 116 ? 0.2714 0.2449 0.2124 0.0129  0.0008  0.0072  142 PHE A CE2 
987  C CZ  . PHE A 116 ? 0.2711 0.2384 0.2118 0.0152  -0.0002 0.0086  142 PHE A CZ  
988  N N   . ASP A 117 ? 0.3268 0.3340 0.2839 0.0191  0.0048  -0.0209 143 ASP A N   
989  C CA  . ASP A 117 ? 0.3423 0.3622 0.3037 0.0191  0.0070  -0.0277 143 ASP A CA  
990  C C   . ASP A 117 ? 0.3453 0.3725 0.3032 0.0138  0.0102  -0.0296 143 ASP A C   
991  O O   . ASP A 117 ? 0.3397 0.3682 0.2935 0.0078  0.0116  -0.0243 143 ASP A O   
992  C CB  . ASP A 117 ? 0.3802 0.3995 0.3470 0.0266  0.0046  -0.0344 143 ASP A CB  
993  C CG  . ASP A 117 ? 0.4816 0.4998 0.4524 0.0312  0.0020  -0.0338 143 ASP A CG  
994  O OD1 . ASP A 117 ? 0.5089 0.5265 0.4783 0.0287  0.0019  -0.0285 143 ASP A OD1 
995  O OD2 . ASP A 117 ? 0.5280 0.5462 0.5037 0.0377  -0.0006 -0.0390 143 ASP A OD2 
996  N N   . ASP A 118 ? 0.3510 0.3828 0.3104 0.0162  0.0109  -0.0372 144 ASP A N   
997  C CA  . ASP A 118 ? 0.3619 0.4024 0.3173 0.0117  0.0139  -0.0401 144 ASP A CA  
998  C C   . ASP A 118 ? 0.3630 0.3951 0.3114 0.0080  0.0130  -0.0352 144 ASP A C   
999  O O   . ASP A 118 ? 0.3687 0.4081 0.3122 0.0033  0.0152  -0.0357 144 ASP A O   
1000 C CB  . ASP A 118 ? 0.3934 0.4414 0.3529 0.0165  0.0143  -0.0511 144 ASP A CB  
1001 C CG  . ASP A 118 ? 0.4886 0.5477 0.4564 0.0205  0.0152  -0.0572 144 ASP A CG  
1002 O OD1 . ASP A 118 ? 0.5024 0.5722 0.4715 0.0161  0.0181  -0.0548 144 ASP A OD1 
1003 O OD2 . ASP A 118 ? 0.5340 0.5907 0.5074 0.0280  0.0125  -0.0643 144 ASP A OD2 
1004 N N   . TYR A 119 ? 0.3582 0.3763 0.3059 0.0099  0.0098  -0.0305 145 TYR A N   
1005 C CA  . TYR A 119 ? 0.3603 0.3714 0.3025 0.0064  0.0088  -0.0259 145 TYR A CA  
1006 C C   . TYR A 119 ? 0.3595 0.3674 0.2990 0.0026  0.0086  -0.0169 145 TYR A C   
1007 O O   . TYR A 119 ? 0.3532 0.3543 0.2898 0.0009  0.0071  -0.0126 145 TYR A O   
1008 C CB  . TYR A 119 ? 0.3685 0.3675 0.3121 0.0100  0.0056  -0.0269 145 TYR A CB  
1009 C CG  . TYR A 119 ? 0.3845 0.3845 0.3315 0.0143  0.0047  -0.0363 145 TYR A CG  
1010 C CD1 . TYR A 119 ? 0.3984 0.4055 0.3433 0.0127  0.0059  -0.0427 145 TYR A CD1 
1011 C CD2 . TYR A 119 ? 0.4001 0.3943 0.3526 0.0206  0.0022  -0.0392 145 TYR A CD2 
1012 C CE1 . TYR A 119 ? 0.4141 0.4222 0.3628 0.0174  0.0045  -0.0526 145 TYR A CE1 
1013 C CE2 . TYR A 119 ? 0.4149 0.4088 0.3714 0.0254  0.0004  -0.0483 145 TYR A CE2 
1014 C CZ  . TYR A 119 ? 0.4310 0.4319 0.3860 0.0240  0.0016  -0.0555 145 TYR A CZ  
1015 O OH  . TYR A 119 ? 0.4715 0.4726 0.4312 0.0296  -0.0005 -0.0659 145 TYR A OH  
1016 N N   . SER A 120 ? 0.3613 0.3744 0.3024 0.0014  0.0098  -0.0148 146 SER A N   
1017 C CA  . SER A 120 ? 0.3699 0.3805 0.3096 -0.0016 0.0091  -0.0076 146 SER A CA  
1018 C C   . SER A 120 ? 0.3567 0.3684 0.2908 -0.0072 0.0092  -0.0035 146 SER A C   
1019 O O   . SER A 120 ? 0.3561 0.3614 0.2886 -0.0083 0.0072  0.0021  146 SER A O   
1020 C CB  . SER A 120 ? 0.4018 0.4194 0.3452 -0.0025 0.0102  -0.0078 146 SER A CB  
1021 O OG  . SER A 120 ? 0.4315 0.4467 0.3799 0.0032  0.0090  -0.0105 146 SER A OG  
1022 N N   . ASP A 121 ? 0.3488 0.3692 0.2797 -0.0105 0.0114  -0.0063 147 ASP A N   
1023 C CA  . ASP A 121 ? 0.3626 0.3846 0.2869 -0.0160 0.0111  -0.0021 147 ASP A CA  
1024 C C   . ASP A 121 ? 0.3569 0.3717 0.2786 -0.0151 0.0086  -0.0012 147 ASP A C   
1025 O O   . ASP A 121 ? 0.3690 0.3825 0.2864 -0.0186 0.0069  0.0037  147 ASP A O   
1026 C CB  . ASP A 121 ? 0.4038 0.4387 0.3243 -0.0200 0.0143  -0.0053 147 ASP A CB  
1027 C CG  . ASP A 121 ? 0.5136 0.5567 0.4370 -0.0227 0.0168  -0.0043 147 ASP A CG  
1028 O OD1 . ASP A 121 ? 0.5306 0.5709 0.4530 -0.0268 0.0155  0.0029  147 ASP A OD1 
1029 O OD2 . ASP A 121 ? 0.5563 0.6085 0.4838 -0.0206 0.0195  -0.0111 147 ASP A OD2 
1030 N N   . ASP A 122 ? 0.3415 0.3520 0.2662 -0.0106 0.0080  -0.0069 148 ASP A N   
1031 C CA  . ASP A 122 ? 0.3326 0.3359 0.2559 -0.0109 0.0054  -0.0047 148 ASP A CA  
1032 C C   . ASP A 122 ? 0.3126 0.3082 0.2385 -0.0097 0.0036  0.0014  148 ASP A C   
1033 O O   . ASP A 122 ? 0.3227 0.3147 0.2478 -0.0108 0.0016  0.0044  148 ASP A O   
1034 C CB  . ASP A 122 ? 0.3684 0.3681 0.2939 -0.0081 0.0046  -0.0109 148 ASP A CB  
1035 C CG  . ASP A 122 ? 0.4740 0.4815 0.3962 -0.0093 0.0055  -0.0179 148 ASP A CG  
1036 O OD1 . ASP A 122 ? 0.5072 0.5232 0.4240 -0.0133 0.0069  -0.0165 148 ASP A OD1 
1037 O OD2 . ASP A 122 ? 0.5012 0.5064 0.4262 -0.0062 0.0047  -0.0248 148 ASP A OD2 
1038 N N   . VAL A 123 ? 0.2767 0.2703 0.2053 -0.0079 0.0037  0.0039  149 VAL A N   
1039 C CA  . VAL A 123 ? 0.2664 0.2544 0.1969 -0.0065 0.0020  0.0087  149 VAL A CA  
1040 C C   . VAL A 123 ? 0.2595 0.2483 0.1877 -0.0096 0.0004  0.0137  149 VAL A C   
1041 O O   . VAL A 123 ? 0.2533 0.2457 0.1799 -0.0121 0.0007  0.0149  149 VAL A O   
1042 C CB  . VAL A 123 ? 0.2735 0.2600 0.2075 -0.0028 0.0025  0.0086  149 VAL A CB  
1043 C CG1 . VAL A 123 ? 0.2828 0.2650 0.2182 -0.0010 0.0009  0.0127  149 VAL A CG1 
1044 C CG2 . VAL A 123 ? 0.2770 0.2615 0.2132 0.0008  0.0031  0.0042  149 VAL A CG2 
1045 N N   . CYS A 124 ? 0.2490 0.2346 0.1779 -0.0093 -0.0017 0.0166  150 CYS A N   
1046 C CA  . CYS A 124 ? 0.2444 0.2297 0.1721 -0.0111 -0.0043 0.0210  150 CYS A CA  
1047 C C   . CYS A 124 ? 0.2303 0.2124 0.1619 -0.0078 -0.0057 0.0231  150 CYS A C   
1048 O O   . CYS A 124 ? 0.2316 0.2125 0.1633 -0.0084 -0.0077 0.0257  150 CYS A O   
1049 C CB  . CYS A 124 ? 0.2531 0.2388 0.1793 -0.0127 -0.0063 0.0218  150 CYS A CB  
1050 S SG  . CYS A 124 ? 0.3004 0.2909 0.2209 -0.0166 -0.0055 0.0187  150 CYS A SG  
1051 N N   . GLY A 125 ? 0.2173 0.1979 0.1518 -0.0046 -0.0048 0.0220  151 GLY A N   
1052 C CA  . GLY A 125 ? 0.2127 0.1921 0.1505 -0.0011 -0.0056 0.0230  151 GLY A CA  
1053 C C   . GLY A 125 ? 0.2099 0.1893 0.1496 0.0012  -0.0043 0.0227  151 GLY A C   
1054 O O   . GLY A 125 ? 0.2034 0.1819 0.1425 0.0003  -0.0027 0.0216  151 GLY A O   
1055 N N   . ALA A 126 ? 0.1980 0.1786 0.1401 0.0042  -0.0049 0.0235  152 ALA A N   
1056 C CA  . ALA A 126 ? 0.1935 0.1758 0.1371 0.0058  -0.0032 0.0240  152 ALA A CA  
1057 C C   . ALA A 126 ? 0.1875 0.1743 0.1344 0.0075  -0.0044 0.0247  152 ALA A C   
1058 O O   . ALA A 126 ? 0.1699 0.1569 0.1182 0.0092  -0.0070 0.0241  152 ALA A O   
1059 C CB  . ALA A 126 ? 0.1982 0.1795 0.1406 0.0091  -0.0018 0.0233  152 ALA A CB  
1060 N N   . VAL A 127 ? 0.1952 0.1858 0.1439 0.0071  -0.0027 0.0257  153 VAL A N   
1061 C CA  . VAL A 127 ? 0.1995 0.1970 0.1525 0.0088  -0.0034 0.0255  153 VAL A CA  
1062 C C   . VAL A 127 ? 0.2066 0.2093 0.1600 0.0100  0.0000  0.0264  153 VAL A C   
1063 O O   . VAL A 127 ? 0.1979 0.1987 0.1495 0.0072  0.0023  0.0286  153 VAL A O   
1064 C CB  . VAL A 127 ? 0.2122 0.2123 0.1682 0.0053  -0.0046 0.0262  153 VAL A CB  
1065 C CG1 . VAL A 127 ? 0.2222 0.2313 0.1841 0.0075  -0.0054 0.0253  153 VAL A CG1 
1066 C CG2 . VAL A 127 ? 0.2180 0.2136 0.1720 0.0035  -0.0079 0.0260  153 VAL A CG2 
1067 N N   . VAL A 128 ? 0.2068 0.2166 0.1627 0.0139  -0.0001 0.0248  154 VAL A N   
1068 C CA  . VAL A 128 ? 0.2159 0.2334 0.1718 0.0146  0.0034  0.0258  154 VAL A CA  
1069 C C   . VAL A 128 ? 0.2247 0.2532 0.1871 0.0152  0.0034  0.0244  154 VAL A C   
1070 O O   . VAL A 128 ? 0.2178 0.2486 0.1838 0.0190  0.0003  0.0209  154 VAL A O   
1071 C CB  . VAL A 128 ? 0.2225 0.2405 0.1744 0.0192  0.0041  0.0243  154 VAL A CB  
1072 C CG1 . VAL A 128 ? 0.2323 0.2509 0.1866 0.0243  0.0006  0.0196  154 VAL A CG1 
1073 C CG2 . VAL A 128 ? 0.2246 0.2522 0.1752 0.0197  0.0080  0.0259  154 VAL A CG2 
1074 N N   . ASN A 129 ? 0.2368 0.2715 0.2013 0.0111  0.0065  0.0270  155 ASN A N   
1075 C CA  . ASN A 129 ? 0.2448 0.2924 0.2164 0.0109  0.0073  0.0257  155 ASN A CA  
1076 C C   . ASN A 129 ? 0.2591 0.3183 0.2301 0.0122  0.0118  0.0262  155 ASN A C   
1077 O O   . ASN A 129 ? 0.2586 0.3169 0.2254 0.0083  0.0153  0.0308  155 ASN A O   
1078 C CB  . ASN A 129 ? 0.2473 0.2953 0.2225 0.0043  0.0078  0.0285  155 ASN A CB  
1079 C CG  . ASN A 129 ? 0.2937 0.3310 0.2680 0.0024  0.0038  0.0282  155 ASN A CG  
1080 O OD1 . ASN A 129 ? 0.3168 0.3454 0.2876 -0.0017 0.0042  0.0305  155 ASN A OD1 
1081 N ND2 . ASN A 129 ? 0.3017 0.3395 0.2787 0.0054  -0.0004 0.0253  155 ASN A ND2 
1082 N N   . VAL A 130 ? 0.2617 0.3321 0.2368 0.0177  0.0114  0.0214  156 VAL A N   
1083 C CA  . VAL A 130 ? 0.2758 0.3603 0.2501 0.0195  0.0160  0.0208  156 VAL A CA  
1084 C C   . VAL A 130 ? 0.2927 0.3926 0.2755 0.0166  0.0183  0.0205  156 VAL A C   
1085 O O   . VAL A 130 ? 0.2890 0.3938 0.2798 0.0196  0.0150  0.0159  156 VAL A O   
1086 C CB  . VAL A 130 ? 0.2857 0.3734 0.2593 0.0280  0.0139  0.0143  156 VAL A CB  
1087 C CG1 . VAL A 130 ? 0.2891 0.3949 0.2627 0.0307  0.0185  0.0119  156 VAL A CG1 
1088 C CG2 . VAL A 130 ? 0.2975 0.3706 0.2631 0.0296  0.0118  0.0151  156 VAL A CG2 
1089 N N   . ARG A 131 ? 0.3057 0.4119 0.2873 0.0100  0.0235  0.0261  157 ARG A N   
1090 C CA  . ARG A 131 ? 0.3149 0.4360 0.3052 0.0051  0.0264  0.0271  157 ARG A CA  
1091 C C   . ARG A 131 ? 0.3389 0.4746 0.3266 0.0018  0.0332  0.0308  157 ARG A C   
1092 O O   . ARG A 131 ? 0.3548 0.4832 0.3328 -0.0004 0.0354  0.0362  157 ARG A O   
1093 C CB  . ARG A 131 ? 0.3220 0.4331 0.3144 -0.0031 0.0251  0.0319  157 ARG A CB  
1094 C CG  . ARG A 131 ? 0.3496 0.4464 0.3429 -0.0014 0.0188  0.0295  157 ARG A CG  
1095 C CD  . ARG A 131 ? 0.3579 0.4641 0.3608 0.0025  0.0151  0.0236  157 ARG A CD  
1096 N NE  . ARG A 131 ? 0.3528 0.4462 0.3557 0.0030  0.0091  0.0225  157 ARG A NE  
1097 C CZ  . ARG A 131 ? 0.3572 0.4403 0.3561 0.0085  0.0049  0.0201  157 ARG A CZ  
1098 N NH1 . ARG A 131 ? 0.3269 0.4097 0.3220 0.0142  0.0055  0.0180  157 ARG A NH1 
1099 N NH2 . ARG A 131 ? 0.3536 0.4266 0.3519 0.0078  -0.0001 0.0201  157 ARG A NH2 
1100 N N   . ALA A 132 ? 0.3353 0.4920 0.3315 0.0013  0.0363  0.0281  158 ALA A N   
1101 C CA  . ALA A 132 ? 0.3510 0.5260 0.3460 -0.0025 0.0435  0.0314  158 ALA A CA  
1102 C C   . ALA A 132 ? 0.3756 0.5440 0.3671 -0.0138 0.0467  0.0420  158 ALA A C   
1103 O O   . ALA A 132 ? 0.3827 0.5553 0.3664 -0.0172 0.0514  0.0480  158 ALA A O   
1104 C CB  . ALA A 132 ? 0.3394 0.5391 0.3469 -0.0011 0.0458  0.0255  158 ALA A CB  
1105 N N   . LYS A 133 ? 0.3867 0.5443 0.3837 -0.0195 0.0435  0.0442  159 LYS A N   
1106 C CA  . LYS A 133 ? 0.4053 0.5533 0.4007 -0.0302 0.0448  0.0532  159 LYS A CA  
1107 C C   . LYS A 133 ? 0.4211 0.5467 0.4044 -0.0305 0.0429  0.0586  159 LYS A C   
1108 O O   . LYS A 133 ? 0.4357 0.5535 0.4157 -0.0383 0.0443  0.0668  159 LYS A O   
1109 C CB  . LYS A 133 ? 0.4371 0.5797 0.4423 -0.0345 0.0408  0.0517  159 LYS A CB  
1110 C CG  . LYS A 133 ? 0.4991 0.6605 0.5161 -0.0421 0.0441  0.0528  159 LYS A CG  
1111 C CD  . LYS A 133 ? 0.5730 0.7244 0.5969 -0.0489 0.0400  0.0537  159 LYS A CD  
1112 C CE  . LYS A 133 ? 0.6298 0.7980 0.6651 -0.0586 0.0434  0.0564  159 LYS A CE  
1113 N NZ  . LYS A 133 ? 0.6688 0.8265 0.7107 -0.0653 0.0388  0.0567  159 LYS A NZ  
1114 N N   . GLY A 134 ? 0.4108 0.5253 0.3887 -0.0222 0.0390  0.0539  160 GLY A N   
1115 C CA  . GLY A 134 ? 0.4025 0.4970 0.3702 -0.0214 0.0366  0.0576  160 GLY A CA  
1116 C C   . GLY A 134 ? 0.3813 0.4632 0.3483 -0.0146 0.0312  0.0515  160 GLY A C   
1117 O O   . GLY A 134 ? 0.3831 0.4622 0.3566 -0.0148 0.0279  0.0478  160 GLY A O   
1118 N N   . ASP A 135 ? 0.3648 0.4394 0.3235 -0.0089 0.0300  0.0505  161 ASP A N   
1119 C CA  . ASP A 135 ? 0.3508 0.4141 0.3084 -0.0030 0.0252  0.0452  161 ASP A CA  
1120 C C   . ASP A 135 ? 0.3321 0.3778 0.2883 -0.0064 0.0220  0.0473  161 ASP A C   
1121 O O   . ASP A 135 ? 0.3315 0.3703 0.2852 -0.0118 0.0230  0.0531  161 ASP A O   
1122 C CB  . ASP A 135 ? 0.3799 0.4429 0.3303 0.0038  0.0250  0.0430  161 ASP A CB  
1123 C CG  . ASP A 135 ? 0.4610 0.5424 0.4125 0.0074  0.0282  0.0400  161 ASP A CG  
1124 O OD1 . ASP A 135 ? 0.4523 0.5450 0.4121 0.0084  0.0283  0.0357  161 ASP A OD1 
1125 O OD2 . ASP A 135 ? 0.5063 0.5918 0.4502 0.0095  0.0304  0.0417  161 ASP A OD2 
1126 N N   . LYS A 136 ? 0.3107 0.3492 0.2686 -0.0033 0.0180  0.0426  162 LYS A N   
1127 C CA  . LYS A 136 ? 0.2957 0.3196 0.2522 -0.0056 0.0152  0.0430  162 LYS A CA  
1128 C C   . LYS A 136 ? 0.2728 0.2892 0.2258 -0.0002 0.0121  0.0391  162 LYS A C   
1129 O O   . LYS A 136 ? 0.2661 0.2875 0.2209 0.0041  0.0108  0.0352  162 LYS A O   
1130 C CB  . LYS A 136 ? 0.3123 0.3368 0.2754 -0.0100 0.0134  0.0417  162 LYS A CB  
1131 C CG  . LYS A 136 ? 0.3696 0.4011 0.3378 -0.0167 0.0159  0.0455  162 LYS A CG  
1132 C CD  . LYS A 136 ? 0.4328 0.4643 0.4076 -0.0206 0.0133  0.0434  162 LYS A CD  
1133 C CE  . LYS A 136 ? 0.4813 0.5288 0.4642 -0.0203 0.0139  0.0410  162 LYS A CE  
1134 N NZ  . LYS A 136 ? 0.5054 0.5524 0.4936 -0.0218 0.0098  0.0376  162 LYS A NZ  
1135 N N   . ILE A 137 ? 0.2553 0.2600 0.2041 -0.0006 0.0109  0.0399  163 ILE A N   
1136 C CA  . ILE A 137 ? 0.2604 0.2585 0.2067 0.0032  0.0083  0.0364  163 ILE A CA  
1137 C C   . ILE A 137 ? 0.2575 0.2467 0.2042 -0.0001 0.0065  0.0357  163 ILE A C   
1138 O O   . ILE A 137 ? 0.2592 0.2432 0.2057 -0.0036 0.0070  0.0382  163 ILE A O   
1139 C CB  . ILE A 137 ? 0.2758 0.2712 0.2166 0.0074  0.0085  0.0366  163 ILE A CB  
1140 C CG1 . ILE A 137 ? 0.2906 0.2964 0.2306 0.0108  0.0103  0.0365  163 ILE A CG1 
1141 C CG2 . ILE A 137 ? 0.2845 0.2748 0.2244 0.0105  0.0060  0.0326  163 ILE A CG2 
1142 C CD1 . ILE A 137 ? 0.3131 0.3178 0.2473 0.0152  0.0102  0.0365  163 ILE A CD1 
1143 N N   . ALA A 138 ? 0.2436 0.2311 0.1908 0.0008  0.0043  0.0322  164 ALA A N   
1144 C CA  . ALA A 138 ? 0.2465 0.2278 0.1935 -0.0019 0.0029  0.0306  164 ALA A CA  
1145 C C   . ALA A 138 ? 0.2526 0.2311 0.1971 0.0003  0.0015  0.0276  164 ALA A C   
1146 O O   . ALA A 138 ? 0.2562 0.2379 0.2008 0.0026  0.0007  0.0268  164 ALA A O   
1147 C CB  . ALA A 138 ? 0.2451 0.2300 0.1959 -0.0056 0.0018  0.0301  164 ALA A CB  
1148 N N   . ILE A 139 ? 0.2498 0.2227 0.1927 -0.0006 0.0010  0.0256  165 ILE A N   
1149 C CA  . ILE A 139 ? 0.2559 0.2285 0.1970 0.0003  0.0002  0.0225  165 ILE A CA  
1150 C C   . ILE A 139 ? 0.2475 0.2205 0.1885 -0.0033 -0.0009 0.0206  165 ILE A C   
1151 O O   . ILE A 139 ? 0.2487 0.2187 0.1906 -0.0053 -0.0012 0.0196  165 ILE A O   
1152 C CB  . ILE A 139 ? 0.2800 0.2487 0.2195 0.0029  0.0006  0.0204  165 ILE A CB  
1153 C CG1 . ILE A 139 ? 0.3073 0.2770 0.2463 0.0068  0.0010  0.0218  165 ILE A CG1 
1154 C CG2 . ILE A 139 ? 0.2816 0.2519 0.2200 0.0021  0.0003  0.0166  165 ILE A CG2 
1155 C CD1 . ILE A 139 ? 0.3371 0.3054 0.2754 0.0099  0.0007  0.0191  165 ILE A CD1 
1156 N N   . TRP A 140 ? 0.2331 0.2096 0.1730 -0.0041 -0.0021 0.0203  166 TRP A N   
1157 C CA  . TRP A 140 ? 0.2243 0.2026 0.1627 -0.0074 -0.0036 0.0190  166 TRP A CA  
1158 C C   . TRP A 140 ? 0.2320 0.2105 0.1668 -0.0080 -0.0030 0.0158  166 TRP A C   
1159 O O   . TRP A 140 ? 0.2375 0.2171 0.1711 -0.0068 -0.0023 0.0159  166 TRP A O   
1160 C CB  . TRP A 140 ? 0.2081 0.1899 0.1467 -0.0078 -0.0057 0.0215  166 TRP A CB  
1161 C CG  . TRP A 140 ? 0.2010 0.1854 0.1439 -0.0077 -0.0066 0.0232  166 TRP A CG  
1162 C CD1 . TRP A 140 ? 0.2073 0.1922 0.1536 -0.0065 -0.0049 0.0243  166 TRP A CD1 
1163 C CD2 . TRP A 140 ? 0.1924 0.1806 0.1369 -0.0088 -0.0095 0.0242  166 TRP A CD2 
1164 N NE1 . TRP A 140 ? 0.1970 0.1872 0.1476 -0.0070 -0.0060 0.0254  166 TRP A NE1 
1165 C CE2 . TRP A 140 ? 0.1981 0.1901 0.1481 -0.0080 -0.0092 0.0251  166 TRP A CE2 
1166 C CE3 . TRP A 140 ? 0.1946 0.1839 0.1361 -0.0103 -0.0127 0.0247  166 TRP A CE3 
1167 C CZ2 . TRP A 140 ? 0.2000 0.1975 0.1539 -0.0082 -0.0119 0.0256  166 TRP A CZ2 
1168 C CZ3 . TRP A 140 ? 0.2018 0.1949 0.1463 -0.0103 -0.0160 0.0258  166 TRP A CZ3 
1169 C CH2 . TRP A 140 ? 0.2013 0.1986 0.1525 -0.0091 -0.0157 0.0258  166 TRP A CH2 
1170 N N   . THR A 141 ? 0.2241 0.2025 0.1577 -0.0101 -0.0034 0.0123  167 THR A N   
1171 C CA  . THR A 141 ? 0.2325 0.2135 0.1628 -0.0107 -0.0025 0.0080  167 THR A CA  
1172 C C   . THR A 141 ? 0.2405 0.2261 0.1667 -0.0142 -0.0041 0.0070  167 THR A C   
1173 O O   . THR A 141 ? 0.2379 0.2233 0.1650 -0.0159 -0.0062 0.0084  167 THR A O   
1174 C CB  . THR A 141 ? 0.2541 0.2314 0.1864 -0.0085 -0.0017 0.0030  167 THR A CB  
1175 O OG1 . THR A 141 ? 0.2661 0.2418 0.1987 -0.0103 -0.0032 -0.0006 167 THR A OG1 
1176 C CG2 . THR A 141 ? 0.2510 0.2223 0.1869 -0.0053 -0.0013 0.0054  167 THR A CG2 
1177 N N   . THR A 142 ? 0.2458 0.2365 0.1674 -0.0155 -0.0030 0.0048  168 THR A N   
1178 C CA  . THR A 142 ? 0.2713 0.2676 0.1871 -0.0190 -0.0044 0.0050  168 THR A CA  
1179 C C   . THR A 142 ? 0.2940 0.2923 0.2080 -0.0202 -0.0055 -0.0009 168 THR A C   
1180 O O   . THR A 142 ? 0.2991 0.3010 0.2088 -0.0229 -0.0078 0.0002  168 THR A O   
1181 C CB  . THR A 142 ? 0.2786 0.2810 0.1897 -0.0207 -0.0023 0.0056  168 THR A CB  
1182 O OG1 . THR A 142 ? 0.2860 0.2923 0.1907 -0.0244 -0.0043 0.0094  168 THR A OG1 
1183 C CG2 . THR A 142 ? 0.2780 0.2856 0.1881 -0.0199 0.0006  -0.0017 168 THR A CG2 
1184 N N   . GLU A 143 ? 0.3036 0.2992 0.2208 -0.0181 -0.0047 -0.0071 169 GLU A N   
1185 C CA  . GLU A 143 ? 0.3299 0.3272 0.2458 -0.0190 -0.0062 -0.0140 169 GLU A CA  
1186 C C   . GLU A 143 ? 0.3548 0.3433 0.2775 -0.0170 -0.0074 -0.0178 169 GLU A C   
1187 O O   . GLU A 143 ? 0.3562 0.3414 0.2819 -0.0137 -0.0061 -0.0212 169 GLU A O   
1188 C CB  . GLU A 143 ? 0.3527 0.3586 0.2634 -0.0188 -0.0039 -0.0201 169 GLU A CB  
1189 C CG  . GLU A 143 ? 0.4233 0.4323 0.3319 -0.0191 -0.0055 -0.0288 169 GLU A CG  
1190 C CD  . GLU A 143 ? 0.5076 0.5182 0.4128 -0.0225 -0.0091 -0.0277 169 GLU A CD  
1191 O OE1 . GLU A 143 ? 0.5125 0.5315 0.4097 -0.0253 -0.0091 -0.0254 169 GLU A OE1 
1192 O OE2 . GLU A 143 ? 0.5303 0.5340 0.4409 -0.0227 -0.0122 -0.0287 169 GLU A OE2 
1193 N N   . CYS A 144 ? 0.3732 0.3581 0.2989 -0.0191 -0.0104 -0.0169 170 CYS A N   
1194 C CA  . CYS A 144 ? 0.4001 0.3757 0.3324 -0.0185 -0.0119 -0.0191 170 CYS A CA  
1195 C C   . CYS A 144 ? 0.4216 0.3953 0.3545 -0.0170 -0.0134 -0.0289 170 CYS A C   
1196 O O   . CYS A 144 ? 0.4391 0.4033 0.3775 -0.0157 -0.0148 -0.0309 170 CYS A O   
1197 C CB  . CYS A 144 ? 0.4122 0.3856 0.3487 -0.0219 -0.0144 -0.0152 170 CYS A CB  
1198 S SG  . CYS A 144 ? 0.5123 0.4924 0.4460 -0.0257 -0.0181 -0.0192 170 CYS A SG  
1199 N N   . GLU A 145 ? 0.4232 0.4029 0.3521 -0.0169 -0.0133 -0.0339 171 GLU A N   
1200 C CA  . GLU A 145 ? 0.4339 0.4154 0.3620 -0.0147 -0.0141 -0.0447 171 GLU A CA  
1201 C C   . GLU A 145 ? 0.4268 0.4100 0.3554 -0.0099 -0.0113 -0.0483 171 GLU A C   
1202 O O   . GLU A 145 ? 0.4346 0.4183 0.3646 -0.0068 -0.0122 -0.0581 171 GLU A O   
1203 C CB  . GLU A 145 ? 0.4822 0.4751 0.4027 -0.0170 -0.0147 -0.0492 171 GLU A CB  
1204 C CG  . GLU A 145 ? 0.5823 0.5740 0.5032 -0.0210 -0.0187 -0.0482 171 GLU A CG  
1205 C CD  . GLU A 145 ? 0.7276 0.7090 0.6564 -0.0211 -0.0227 -0.0537 171 GLU A CD  
1206 O OE1 . GLU A 145 ? 0.7703 0.7484 0.7012 -0.0179 -0.0236 -0.0628 171 GLU A OE1 
1207 O OE2 . GLU A 145 ? 0.7640 0.7406 0.6975 -0.0245 -0.0252 -0.0490 171 GLU A OE2 
1208 N N   . ASN A 146 ? 0.4109 0.3977 0.3381 -0.0088 -0.0080 -0.0436 172 ASN A N   
1209 C CA  . ASN A 146 ? 0.4044 0.3935 0.3336 -0.0043 -0.0056 -0.0475 172 ASN A CA  
1210 C C   . ASN A 146 ? 0.3889 0.3643 0.3254 -0.0008 -0.0076 -0.0456 172 ASN A C   
1211 O O   . ASN A 146 ? 0.3723 0.3451 0.3100 -0.0001 -0.0062 -0.0385 172 ASN A O   
1212 C CB  . ASN A 146 ? 0.4256 0.4234 0.3511 -0.0054 -0.0017 -0.0414 172 ASN A CB  
1213 C CG  . ASN A 146 ? 0.4938 0.5053 0.4116 -0.0087 0.0006  -0.0427 172 ASN A CG  
1214 O OD1 . ASN A 146 ? 0.5107 0.5281 0.4249 -0.0096 -0.0002 -0.0496 172 ASN A OD1 
1215 N ND2 . ASN A 146 ? 0.5079 0.5250 0.4227 -0.0109 0.0033  -0.0359 172 ASN A ND2 
1216 N N   . ARG A 147 ? 0.3835 0.3499 0.3246 0.0011  -0.0114 -0.0519 173 ARG A N   
1217 C CA  . ARG A 147 ? 0.3816 0.3333 0.3289 0.0035  -0.0142 -0.0495 173 ARG A CA  
1218 C C   . ARG A 147 ? 0.3690 0.3197 0.3186 0.0089  -0.0130 -0.0487 173 ARG A C   
1219 O O   . ARG A 147 ? 0.3640 0.3060 0.3156 0.0093  -0.0137 -0.0412 173 ARG A O   
1220 C CB  . ARG A 147 ? 0.3986 0.3405 0.3506 0.0047  -0.0192 -0.0576 173 ARG A CB  
1221 C CG  . ARG A 147 ? 0.4278 0.3526 0.3859 0.0061  -0.0229 -0.0534 173 ARG A CG  
1222 C CD  . ARG A 147 ? 0.4510 0.3643 0.4144 0.0069  -0.0286 -0.0613 173 ARG A CD  
1223 N NE  . ARG A 147 ? 0.4594 0.3763 0.4245 0.0135  -0.0298 -0.0739 173 ARG A NE  
1224 C CZ  . ARG A 147 ? 0.4643 0.3770 0.4328 0.0153  -0.0343 -0.0850 173 ARG A CZ  
1225 N NH1 . ARG A 147 ? 0.4563 0.3600 0.4272 0.0103  -0.0382 -0.0848 173 ARG A NH1 
1226 N NH2 . ARG A 147 ? 0.4434 0.3614 0.4138 0.0221  -0.0350 -0.0971 173 ARG A NH2 
1227 N N   . GLU A 148 ? 0.3614 0.3220 0.3107 0.0127  -0.0111 -0.0563 174 GLU A N   
1228 C CA  . GLU A 148 ? 0.3561 0.3174 0.3086 0.0181  -0.0103 -0.0567 174 GLU A CA  
1229 C C   . GLU A 148 ? 0.3387 0.3039 0.2884 0.0159  -0.0070 -0.0466 174 GLU A C   
1230 O O   . GLU A 148 ? 0.3419 0.3000 0.2940 0.0185  -0.0081 -0.0419 174 GLU A O   
1231 C CB  . GLU A 148 ? 0.3957 0.3689 0.3500 0.0227  -0.0090 -0.0684 174 GLU A CB  
1232 C CG  . GLU A 148 ? 0.4897 0.4806 0.4402 0.0209  -0.0035 -0.0682 174 GLU A CG  
1233 C CD  . GLU A 148 ? 0.6133 0.6194 0.5649 0.0239  -0.0014 -0.0801 174 GLU A CD  
1234 O OE1 . GLU A 148 ? 0.6498 0.6525 0.6060 0.0292  -0.0046 -0.0903 174 GLU A OE1 
1235 O OE2 . GLU A 148 ? 0.6372 0.6588 0.5850 0.0208  0.0034  -0.0794 174 GLU A OE2 
1236 N N   . ALA A 149 ? 0.3170 0.2920 0.2615 0.0110  -0.0038 -0.0431 175 ALA A N   
1237 C CA  . ALA A 149 ? 0.3054 0.2833 0.2477 0.0088  -0.0014 -0.0344 175 ALA A CA  
1238 C C   . ALA A 149 ? 0.2929 0.2600 0.2358 0.0074  -0.0031 -0.0258 175 ALA A C   
1239 O O   . ALA A 149 ? 0.2894 0.2533 0.2335 0.0094  -0.0029 -0.0210 175 ALA A O   
1240 C CB  . ALA A 149 ? 0.3028 0.2921 0.2394 0.0038  0.0014  -0.0326 175 ALA A CB  
1241 N N   . VAL A 150 ? 0.2897 0.2518 0.2318 0.0039  -0.0049 -0.0243 176 VAL A N   
1242 C CA  . VAL A 150 ? 0.2909 0.2451 0.2341 0.0017  -0.0060 -0.0166 176 VAL A CA  
1243 C C   . VAL A 150 ? 0.2787 0.2222 0.2255 0.0051  -0.0079 -0.0144 176 VAL A C   
1244 O O   . VAL A 150 ? 0.2729 0.2142 0.2192 0.0052  -0.0072 -0.0073 176 VAL A O   
1245 C CB  . VAL A 150 ? 0.3082 0.2603 0.2516 -0.0028 -0.0079 -0.0172 176 VAL A CB  
1246 C CG1 . VAL A 150 ? 0.3242 0.2685 0.2703 -0.0053 -0.0091 -0.0102 176 VAL A CG1 
1247 C CG2 . VAL A 150 ? 0.3100 0.2722 0.2489 -0.0063 -0.0066 -0.0169 176 VAL A CG2 
1248 N N   . THR A 151 ? 0.2731 0.2097 0.2231 0.0082  -0.0108 -0.0206 177 THR A N   
1249 C CA  . THR A 151 ? 0.2863 0.2109 0.2392 0.0113  -0.0136 -0.0178 177 THR A CA  
1250 C C   . THR A 151 ? 0.2917 0.2193 0.2443 0.0164  -0.0126 -0.0169 177 THR A C   
1251 O O   . THR A 151 ? 0.2978 0.2187 0.2500 0.0177  -0.0137 -0.0104 177 THR A O   
1252 C CB  . THR A 151 ? 0.3110 0.2250 0.2681 0.0130  -0.0182 -0.0244 177 THR A CB  
1253 O OG1 . THR A 151 ? 0.3190 0.2398 0.2775 0.0173  -0.0183 -0.0349 177 THR A OG1 
1254 C CG2 . THR A 151 ? 0.3226 0.2331 0.2805 0.0071  -0.0197 -0.0244 177 THR A CG2 
1255 N N   . HIS A 152 ? 0.2928 0.2316 0.2453 0.0188  -0.0104 -0.0228 178 HIS A N   
1256 C CA  . HIS A 152 ? 0.2970 0.2400 0.2501 0.0232  -0.0096 -0.0222 178 HIS A CA  
1257 C C   . HIS A 152 ? 0.2751 0.2202 0.2247 0.0205  -0.0075 -0.0132 178 HIS A C   
1258 O O   . HIS A 152 ? 0.2789 0.2200 0.2284 0.0233  -0.0085 -0.0089 178 HIS A O   
1259 C CB  . HIS A 152 ? 0.3112 0.2677 0.2655 0.0249  -0.0071 -0.0298 178 HIS A CB  
1260 C CG  . HIS A 152 ? 0.3614 0.3237 0.3172 0.0283  -0.0062 -0.0289 178 HIS A CG  
1261 N ND1 . HIS A 152 ? 0.3914 0.3602 0.3445 0.0252  -0.0034 -0.0235 178 HIS A ND1 
1262 C CD2 . HIS A 152 ? 0.3823 0.3444 0.3426 0.0346  -0.0084 -0.0332 178 HIS A CD2 
1263 C CE1 . HIS A 152 ? 0.3979 0.3706 0.3539 0.0293  -0.0038 -0.0249 178 HIS A CE1 
1264 N NE2 . HIS A 152 ? 0.3932 0.3625 0.3536 0.0351  -0.0067 -0.0305 178 HIS A NE2 
1265 N N   . ILE A 153 ? 0.2535 0.2045 0.2003 0.0155  -0.0050 -0.0108 179 ILE A N   
1266 C CA  . ILE A 153 ? 0.2463 0.1998 0.1906 0.0133  -0.0033 -0.0036 179 ILE A CA  
1267 C C   . ILE A 153 ? 0.2415 0.1862 0.1854 0.0131  -0.0047 0.0029  179 ILE A C   
1268 O O   . ILE A 153 ? 0.2366 0.1811 0.1794 0.0154  -0.0046 0.0068  179 ILE A O   
1269 C CB  . ILE A 153 ? 0.2498 0.2100 0.1918 0.0083  -0.0015 -0.0026 179 ILE A CB  
1270 C CG1 . ILE A 153 ? 0.2482 0.2182 0.1893 0.0079  0.0004  -0.0070 179 ILE A CG1 
1271 C CG2 . ILE A 153 ? 0.2626 0.2236 0.2030 0.0065  -0.0007 0.0043  179 ILE A CG2 
1272 C CD1 . ILE A 153 ? 0.2496 0.2251 0.1874 0.0030  0.0013  -0.0065 179 ILE A CD1 
1273 N N   . GLY A 154 ? 0.2411 0.1790 0.1860 0.0105  -0.0062 0.0035  180 GLY A N   
1274 C CA  . GLY A 154 ? 0.2444 0.1745 0.1891 0.0090  -0.0073 0.0102  180 GLY A CA  
1275 C C   . GLY A 154 ? 0.2599 0.1829 0.2042 0.0134  -0.0094 0.0126  180 GLY A C   
1276 O O   . GLY A 154 ? 0.2663 0.1886 0.2080 0.0133  -0.0087 0.0192  180 GLY A O   
1277 N N   . ARG A 155 ? 0.2667 0.1851 0.2134 0.0177  -0.0121 0.0068  181 ARG A N   
1278 C CA  . ARG A 155 ? 0.2923 0.2030 0.2391 0.0228  -0.0153 0.0085  181 ARG A CA  
1279 C C   . ARG A 155 ? 0.2923 0.2101 0.2367 0.0266  -0.0141 0.0103  181 ARG A C   
1280 O O   . ARG A 155 ? 0.2983 0.2114 0.2397 0.0283  -0.0155 0.0163  181 ARG A O   
1281 C CB  . ARG A 155 ? 0.3301 0.2352 0.2814 0.0273  -0.0190 0.0004  181 ARG A CB  
1282 C CG  . ARG A 155 ? 0.4255 0.3209 0.3776 0.0333  -0.0237 0.0019  181 ARG A CG  
1283 C CD  . ARG A 155 ? 0.5043 0.3924 0.4620 0.0379  -0.0283 -0.0065 181 ARG A CD  
1284 N NE  . ARG A 155 ? 0.5864 0.4633 0.5460 0.0340  -0.0308 -0.0066 181 ARG A NE  
1285 C CZ  . ARG A 155 ? 0.6306 0.5106 0.5933 0.0324  -0.0303 -0.0149 181 ARG A CZ  
1286 N NH1 . ARG A 155 ? 0.6164 0.5106 0.5798 0.0341  -0.0270 -0.0229 181 ARG A NH1 
1287 N NH2 . ARG A 155 ? 0.6539 0.5230 0.6187 0.0287  -0.0332 -0.0149 181 ARG A NH2 
1288 N N   . VAL A 156 ? 0.2840 0.2129 0.2294 0.0275  -0.0116 0.0052  182 VAL A N   
1289 C CA  . VAL A 156 ? 0.2961 0.2324 0.2403 0.0304  -0.0107 0.0058  182 VAL A CA  
1290 C C   . VAL A 156 ? 0.2997 0.2378 0.2395 0.0275  -0.0087 0.0132  182 VAL A C   
1291 O O   . VAL A 156 ? 0.2943 0.2324 0.2314 0.0303  -0.0096 0.0168  182 VAL A O   
1292 C CB  . VAL A 156 ? 0.3007 0.2486 0.2476 0.0300  -0.0082 -0.0006 182 VAL A CB  
1293 C CG1 . VAL A 156 ? 0.3105 0.2658 0.2565 0.0310  -0.0071 0.0009  182 VAL A CG1 
1294 C CG2 . VAL A 156 ? 0.3023 0.2517 0.2538 0.0339  -0.0098 -0.0087 182 VAL A CG2 
1295 N N   . TYR A 157 ? 0.2903 0.2306 0.2296 0.0223  -0.0064 0.0150  183 TYR A N   
1296 C CA  . TYR A 157 ? 0.2958 0.2395 0.2322 0.0199  -0.0044 0.0206  183 TYR A CA  
1297 C C   . TYR A 157 ? 0.3046 0.2422 0.2380 0.0197  -0.0053 0.0274  183 TYR A C   
1298 O O   . TYR A 157 ? 0.3018 0.2431 0.2318 0.0211  -0.0045 0.0311  183 TYR A O   
1299 C CB  . TYR A 157 ? 0.2967 0.2439 0.2342 0.0148  -0.0025 0.0205  183 TYR A CB  
1300 C CG  . TYR A 157 ? 0.3119 0.2644 0.2480 0.0129  -0.0007 0.0248  183 TYR A CG  
1301 C CD1 . TYR A 157 ? 0.3259 0.2838 0.2604 0.0158  -0.0002 0.0251  183 TYR A CD1 
1302 C CD2 . TYR A 157 ? 0.3205 0.2735 0.2575 0.0085  0.0003  0.0276  183 TYR A CD2 
1303 C CE1 . TYR A 157 ? 0.3398 0.3032 0.2736 0.0149  0.0012  0.0277  183 TYR A CE1 
1304 C CE2 . TYR A 157 ? 0.3304 0.2900 0.2671 0.0075  0.0019  0.0304  183 TYR A CE2 
1305 C CZ  . TYR A 157 ? 0.3484 0.3131 0.2834 0.0109  0.0024  0.0303  183 TYR A CZ  
1306 O OH  . TYR A 157 ? 0.3745 0.3462 0.3100 0.0106  0.0037  0.0318  183 TYR A OH  
1307 N N   . LYS A 158 ? 0.3049 0.2333 0.2392 0.0176  -0.0070 0.0291  184 LYS A N   
1308 C CA  . LYS A 158 ? 0.3213 0.2431 0.2526 0.0163  -0.0080 0.0367  184 LYS A CA  
1309 C C   . LYS A 158 ? 0.3317 0.2507 0.2592 0.0218  -0.0104 0.0389  184 LYS A C   
1310 O O   . LYS A 158 ? 0.3393 0.2603 0.2617 0.0216  -0.0095 0.0452  184 LYS A O   
1311 C CB  . LYS A 158 ? 0.3543 0.2651 0.2884 0.0128  -0.0103 0.0377  184 LYS A CB  
1312 C CG  . LYS A 158 ? 0.4240 0.3258 0.3549 0.0108  -0.0120 0.0465  184 LYS A CG  
1313 C CD  . LYS A 158 ? 0.4900 0.3827 0.4245 0.0049  -0.0134 0.0485  184 LYS A CD  
1314 C CE  . LYS A 158 ? 0.5542 0.4373 0.4853 0.0021  -0.0153 0.0584  184 LYS A CE  
1315 N NZ  . LYS A 158 ? 0.5944 0.4648 0.5301 -0.0030 -0.0185 0.0597  184 LYS A NZ  
1316 N N   . GLU A 159 ? 0.3255 0.2415 0.2554 0.0270  -0.0134 0.0333  185 GLU A N   
1317 C CA  . GLU A 159 ? 0.3294 0.2433 0.2567 0.0330  -0.0166 0.0342  185 GLU A CA  
1318 C C   . GLU A 159 ? 0.3134 0.2385 0.2376 0.0352  -0.0146 0.0341  185 GLU A C   
1319 O O   . GLU A 159 ? 0.3105 0.2355 0.2295 0.0379  -0.0161 0.0385  185 GLU A O   
1320 C CB  . GLU A 159 ? 0.3776 0.2882 0.3103 0.0382  -0.0201 0.0265  185 GLU A CB  
1321 C CG  . GLU A 159 ? 0.4965 0.4068 0.4280 0.0452  -0.0240 0.0259  185 GLU A CG  
1322 C CD  . GLU A 159 ? 0.6509 0.5641 0.5891 0.0509  -0.0264 0.0165  185 GLU A CD  
1323 O OE1 . GLU A 159 ? 0.6762 0.5978 0.6189 0.0493  -0.0233 0.0097  185 GLU A OE1 
1324 O OE2 . GLU A 159 ? 0.7035 0.6115 0.6423 0.0569  -0.0314 0.0162  185 GLU A OE2 
1325 N N   . ARG A 160 ? 0.3005 0.2349 0.2276 0.0338  -0.0116 0.0291  186 ARG A N   
1326 C CA  . ARG A 160 ? 0.3058 0.2499 0.2314 0.0355  -0.0102 0.0280  186 ARG A CA  
1327 C C   . ARG A 160 ? 0.3189 0.2659 0.2387 0.0339  -0.0084 0.0343  186 ARG A C   
1328 O O   . ARG A 160 ? 0.3096 0.2608 0.2255 0.0373  -0.0092 0.0351  186 ARG A O   
1329 C CB  . ARG A 160 ? 0.3089 0.2604 0.2388 0.0332  -0.0077 0.0227  186 ARG A CB  
1330 C CG  . ARG A 160 ? 0.3289 0.2888 0.2582 0.0346  -0.0071 0.0211  186 ARG A CG  
1331 C CD  . ARG A 160 ? 0.3481 0.3102 0.2778 0.0400  -0.0099 0.0182  186 ARG A CD  
1332 N NE  . ARG A 160 ? 0.3587 0.3205 0.2936 0.0414  -0.0112 0.0129  186 ARG A NE  
1333 C CZ  . ARG A 160 ? 0.3472 0.3154 0.2871 0.0400  -0.0101 0.0078  186 ARG A CZ  
1334 N NH1 . ARG A 160 ? 0.3605 0.3338 0.3008 0.0373  -0.0085 0.0076  186 ARG A NH1 
1335 N NH2 . ARG A 160 ? 0.3110 0.2807 0.2557 0.0412  -0.0108 0.0028  186 ARG A NH2 
1336 N N   . LEU A 161 ? 0.3322 0.2781 0.2517 0.0288  -0.0060 0.0381  187 LEU A N   
1337 C CA  . LEU A 161 ? 0.3639 0.3148 0.2789 0.0268  -0.0036 0.0436  187 LEU A CA  
1338 C C   . LEU A 161 ? 0.3973 0.3431 0.3058 0.0274  -0.0051 0.0510  187 LEU A C   
1339 O O   . LEU A 161 ? 0.4047 0.3567 0.3081 0.0265  -0.0030 0.0554  187 LEU A O   
1340 C CB  . LEU A 161 ? 0.3689 0.3223 0.2870 0.0209  -0.0005 0.0448  187 LEU A CB  
1341 C CG  . LEU A 161 ? 0.3861 0.3495 0.3069 0.0206  0.0017  0.0409  187 LEU A CG  
1342 C CD1 . LEU A 161 ? 0.3956 0.3602 0.3194 0.0235  0.0002  0.0343  187 LEU A CD1 
1343 C CD2 . LEU A 161 ? 0.3949 0.3598 0.3196 0.0153  0.0036  0.0416  187 LEU A CD2 
1344 N N   . GLY A 162 ? 0.4175 0.3524 0.3260 0.0290  -0.0088 0.0522  188 GLY A N   
1345 C CA  . GLY A 162 ? 0.4537 0.3813 0.3559 0.0297  -0.0114 0.0599  188 GLY A CA  
1346 C C   . GLY A 162 ? 0.4861 0.4089 0.3866 0.0228  -0.0097 0.0680  188 GLY A C   
1347 O O   . GLY A 162 ? 0.4937 0.4149 0.3870 0.0216  -0.0101 0.0763  188 GLY A O   
1348 N N   . LEU A 163 ? 0.4985 0.4199 0.4053 0.0178  -0.0079 0.0659  189 LEU A N   
1349 C CA  . LEU A 163 ? 0.5277 0.4454 0.4351 0.0103  -0.0063 0.0726  189 LEU A CA  
1350 C C   . LEU A 163 ? 0.5648 0.4662 0.4708 0.0092  -0.0110 0.0785  189 LEU A C   
1351 O O   . LEU A 163 ? 0.5679 0.4597 0.4765 0.0139  -0.0157 0.0742  189 LEU A O   
1352 C CB  . LEU A 163 ? 0.5283 0.4480 0.4437 0.0063  -0.0045 0.0671  189 LEU A CB  
1353 C CG  . LEU A 163 ? 0.5471 0.4813 0.4647 0.0063  -0.0004 0.0623  189 LEU A CG  
1354 C CD1 . LEU A 163 ? 0.5550 0.4894 0.4796 0.0027  0.0002  0.0574  189 LEU A CD1 
1355 C CD2 . LEU A 163 ? 0.5546 0.4998 0.4688 0.0034  0.0036  0.0676  189 LEU A CD2 
1356 N N   . PRO A 164 ? 0.5919 0.4899 0.4945 0.0028  -0.0102 0.0885  190 PRO A N   
1357 C CA  . PRO A 164 ? 0.6136 0.4937 0.5151 0.0013  -0.0156 0.0951  190 PRO A CA  
1358 C C   . PRO A 164 ? 0.6315 0.4999 0.5421 0.0000  -0.0189 0.0892  190 PRO A C   
1359 O O   . PRO A 164 ? 0.6343 0.5074 0.5508 -0.0050 -0.0160 0.0858  190 PRO A O   
1360 C CB  . PRO A 164 ? 0.6229 0.5049 0.5196 -0.0072 -0.0126 0.1070  190 PRO A CB  
1361 C CG  . PRO A 164 ? 0.6192 0.5191 0.5186 -0.0111 -0.0057 0.1042  190 PRO A CG  
1362 C CD  . PRO A 164 ? 0.5904 0.5010 0.4905 -0.0034 -0.0044 0.0941  190 PRO A CD  
1363 N N   . PRO A 165 ? 0.6437 0.4979 0.5558 0.0054  -0.0254 0.0865  191 PRO A N   
1364 C CA  . PRO A 165 ? 0.6492 0.4934 0.5701 0.0054  -0.0288 0.0788  191 PRO A CA  
1365 C C   . PRO A 165 ? 0.6542 0.4888 0.5795 -0.0034 -0.0296 0.0832  191 PRO A C   
1366 O O   . PRO A 165 ? 0.6604 0.4923 0.5931 -0.0045 -0.0306 0.0754  191 PRO A O   
1367 C CB  . PRO A 165 ? 0.6631 0.4942 0.5842 0.0135  -0.0360 0.0764  191 PRO A CB  
1368 C CG  . PRO A 165 ? 0.6673 0.5067 0.5809 0.0192  -0.0354 0.0791  191 PRO A CG  
1369 C CD  . PRO A 165 ? 0.6448 0.4926 0.5512 0.0125  -0.0302 0.0892  191 PRO A CD  
1370 N N   . LYS A 166 ? 0.6465 0.4769 0.5672 -0.0101 -0.0292 0.0955  192 LYS A N   
1371 C CA  . LYS A 166 ? 0.6431 0.4639 0.5684 -0.0196 -0.0303 0.1008  192 LYS A CA  
1372 C C   . LYS A 166 ? 0.6291 0.4638 0.5597 -0.0267 -0.0243 0.0979  192 LYS A C   
1373 O O   . LYS A 166 ? 0.6371 0.4643 0.5750 -0.0323 -0.0263 0.0961  192 LYS A O   
1374 C CB  . LYS A 166 ? 0.6708 0.4835 0.5893 -0.0254 -0.0316 0.1160  192 LYS A CB  
1375 C CG  . LYS A 166 ? 0.7217 0.5114 0.6445 -0.0302 -0.0387 0.1209  192 LYS A CG  
1376 C CD  . LYS A 166 ? 0.7747 0.5570 0.6899 -0.0373 -0.0396 0.1375  192 LYS A CD  
1377 C CE  . LYS A 166 ? 0.8183 0.5796 0.7393 -0.0455 -0.0455 0.1436  192 LYS A CE  
1378 N NZ  . LYS A 166 ? 0.8415 0.5816 0.7682 -0.0381 -0.0551 0.1360  192 LYS A NZ  
1379 N N   . ILE A 167 ? 0.6088 0.4630 0.5362 -0.0264 -0.0176 0.0975  193 ILE A N   
1380 C CA  . ILE A 167 ? 0.5935 0.4615 0.5265 -0.0321 -0.0126 0.0943  193 ILE A CA  
1381 C C   . ILE A 167 ? 0.5636 0.4361 0.5013 -0.0265 -0.0129 0.0814  193 ILE A C   
1382 O O   . ILE A 167 ? 0.5653 0.4421 0.4997 -0.0187 -0.0127 0.0765  193 ILE A O   
1383 C CB  . ILE A 167 ? 0.6043 0.4913 0.5326 -0.0343 -0.0057 0.0994  193 ILE A CB  
1384 C CG1 . ILE A 167 ? 0.6232 0.5073 0.5447 -0.0394 -0.0051 0.1127  193 ILE A CG1 
1385 C CG2 . ILE A 167 ? 0.6050 0.5060 0.5404 -0.0400 -0.0013 0.0961  193 ILE A CG2 
1386 C CD1 . ILE A 167 ? 0.6385 0.5427 0.5541 -0.0400 0.0016  0.1167  193 ILE A CD1 
1387 N N   . VAL A 168 ? 0.5298 0.4013 0.4750 -0.0308 -0.0136 0.0761  194 VAL A N   
1388 C CA  . VAL A 168 ? 0.5000 0.3760 0.4487 -0.0263 -0.0140 0.0646  194 VAL A CA  
1389 C C   . VAL A 168 ? 0.4558 0.3506 0.4049 -0.0268 -0.0086 0.0619  194 VAL A C   
1390 O O   . VAL A 168 ? 0.4463 0.3505 0.3956 -0.0319 -0.0049 0.0675  194 VAL A O   
1391 C CB  . VAL A 168 ? 0.5176 0.3831 0.4735 -0.0294 -0.0183 0.0587  194 VAL A CB  
1392 C CG1 . VAL A 168 ? 0.5333 0.3787 0.4902 -0.0292 -0.0245 0.0615  194 VAL A CG1 
1393 C CG2 . VAL A 168 ? 0.5207 0.3927 0.4822 -0.0384 -0.0163 0.0605  194 VAL A CG2 
1394 N N   . ILE A 169 ? 0.4158 0.3159 0.3649 -0.0212 -0.0085 0.0533  195 ILE A N   
1395 C CA  . ILE A 169 ? 0.3797 0.2946 0.3297 -0.0211 -0.0050 0.0496  195 ILE A CA  
1396 C C   . ILE A 169 ? 0.3557 0.2690 0.3105 -0.0226 -0.0073 0.0417  195 ILE A C   
1397 O O   . ILE A 169 ? 0.3549 0.2581 0.3107 -0.0204 -0.0109 0.0369  195 ILE A O   
1398 C CB  . ILE A 169 ? 0.3749 0.2972 0.3202 -0.0141 -0.0032 0.0472  195 ILE A CB  
1399 C CG1 . ILE A 169 ? 0.3814 0.2972 0.3259 -0.0083 -0.0061 0.0405  195 ILE A CG1 
1400 C CG2 . ILE A 169 ? 0.3794 0.3040 0.3196 -0.0128 -0.0014 0.0543  195 ILE A CG2 
1401 C CD1 . ILE A 169 ? 0.3971 0.3218 0.3392 -0.0032 -0.0044 0.0365  195 ILE A CD1 
1402 N N   . GLY A 170 ? 0.3322 0.2555 0.2901 -0.0261 -0.0056 0.0402  196 GLY A N   
1403 C CA  . GLY A 170 ? 0.3212 0.2445 0.2827 -0.0278 -0.0079 0.0332  196 GLY A CA  
1404 C C   . GLY A 170 ? 0.3006 0.2334 0.2598 -0.0240 -0.0069 0.0275  196 GLY A C   
1405 O O   . GLY A 170 ? 0.2992 0.2407 0.2560 -0.0217 -0.0042 0.0296  196 GLY A O   
1406 N N   . TYR A 171 ? 0.2859 0.2169 0.2457 -0.0236 -0.0093 0.0203  197 TYR A N   
1407 C CA  . TYR A 171 ? 0.2818 0.2215 0.2388 -0.0213 -0.0087 0.0156  197 TYR A CA  
1408 C C   . TYR A 171 ? 0.2802 0.2246 0.2405 -0.0260 -0.0103 0.0134  197 TYR A C   
1409 O O   . TYR A 171 ? 0.2877 0.2261 0.2507 -0.0285 -0.0132 0.0094  197 TYR A O   
1410 C CB  . TYR A 171 ? 0.2775 0.2138 0.2316 -0.0171 -0.0099 0.0087  197 TYR A CB  
1411 C CG  . TYR A 171 ? 0.2777 0.2236 0.2283 -0.0159 -0.0091 0.0048  197 TYR A CG  
1412 C CD1 . TYR A 171 ? 0.2817 0.2330 0.2287 -0.0126 -0.0068 0.0064  197 TYR A CD1 
1413 C CD2 . TYR A 171 ? 0.2874 0.2363 0.2377 -0.0181 -0.0110 -0.0006 197 TYR A CD2 
1414 C CE1 . TYR A 171 ? 0.2849 0.2439 0.2283 -0.0123 -0.0062 0.0040  197 TYR A CE1 
1415 C CE2 . TYR A 171 ? 0.2917 0.2493 0.2374 -0.0175 -0.0103 -0.0030 197 TYR A CE2 
1416 C CZ  . TYR A 171 ? 0.2984 0.2606 0.2407 -0.0149 -0.0079 -0.0003 197 TYR A CZ  
1417 O OH  . TYR A 171 ? 0.3134 0.2832 0.2510 -0.0151 -0.0075 -0.0018 197 TYR A OH  
1418 N N   . GLN A 172 ? 0.2680 0.2228 0.2283 -0.0268 -0.0091 0.0155  198 GLN A N   
1419 C CA  . GLN A 172 ? 0.2724 0.2334 0.2359 -0.0306 -0.0110 0.0136  198 GLN A CA  
1420 C C   . GLN A 172 ? 0.2653 0.2323 0.2240 -0.0284 -0.0120 0.0097  198 GLN A C   
1421 O O   . GLN A 172 ? 0.2530 0.2237 0.2079 -0.0250 -0.0104 0.0115  198 GLN A O   
1422 C CB  . GLN A 172 ? 0.3130 0.2827 0.2810 -0.0329 -0.0095 0.0188  198 GLN A CB  
1423 C CG  . GLN A 172 ? 0.3829 0.3510 0.3531 -0.0338 -0.0066 0.0251  198 GLN A CG  
1424 C CD  . GLN A 172 ? 0.4578 0.4378 0.4321 -0.0349 -0.0046 0.0288  198 GLN A CD  
1425 O OE1 . GLN A 172 ? 0.4823 0.4710 0.4578 -0.0338 -0.0057 0.0269  198 GLN A OE1 
1426 N NE2 . GLN A 172 ? 0.4820 0.4631 0.4585 -0.0371 -0.0018 0.0341  198 GLN A NE2 
1427 N N   . SER A 173 ? 0.2592 0.2275 0.2179 -0.0307 -0.0151 0.0046  199 SER A N   
1428 C CA  . SER A 173 ? 0.2672 0.2423 0.2205 -0.0296 -0.0164 0.0018  199 SER A CA  
1429 C C   . SER A 173 ? 0.2544 0.2378 0.2096 -0.0302 -0.0170 0.0061  199 SER A C   
1430 O O   . SER A 173 ? 0.2572 0.2430 0.2192 -0.0330 -0.0175 0.0081  199 SER A O   
1431 C CB  . SER A 173 ? 0.2972 0.2723 0.2502 -0.0322 -0.0199 -0.0050 199 SER A CB  
1432 O OG  . SER A 173 ? 0.3589 0.3420 0.3068 -0.0324 -0.0219 -0.0064 199 SER A OG  
1433 N N   . HIS A 174 ? 0.2478 0.2359 0.1978 -0.0279 -0.0172 0.0074  200 HIS A N   
1434 C CA  . HIS A 174 ? 0.2556 0.2507 0.2078 -0.0276 -0.0189 0.0109  200 HIS A CA  
1435 C C   . HIS A 174 ? 0.2679 0.2682 0.2227 -0.0308 -0.0231 0.0083  200 HIS A C   
1436 O O   . HIS A 174 ? 0.2717 0.2780 0.2326 -0.0313 -0.0246 0.0103  200 HIS A O   
1437 C CB  . HIS A 174 ? 0.2603 0.2571 0.2061 -0.0246 -0.0193 0.0132  200 HIS A CB  
1438 C CG  . HIS A 174 ? 0.2607 0.2538 0.2054 -0.0215 -0.0158 0.0157  200 HIS A CG  
1439 N ND1 . HIS A 174 ? 0.2632 0.2553 0.2131 -0.0202 -0.0134 0.0179  200 HIS A ND1 
1440 C CD2 . HIS A 174 ? 0.2680 0.2591 0.2069 -0.0197 -0.0145 0.0161  200 HIS A CD2 
1441 C CE1 . HIS A 174 ? 0.2776 0.2668 0.2246 -0.0172 -0.0112 0.0192  200 HIS A CE1 
1442 N NE2 . HIS A 174 ? 0.2840 0.2724 0.2250 -0.0170 -0.0118 0.0181  200 HIS A NE2 
1443 N N   . ALA A 175 ? 0.2791 0.2783 0.2298 -0.0326 -0.0251 0.0033  201 ALA A N   
1444 C CA  . ALA A 175 ? 0.2942 0.2982 0.2469 -0.0357 -0.0297 -0.0003 201 ALA A CA  
1445 C C   . ALA A 175 ? 0.2968 0.3004 0.2601 -0.0393 -0.0300 -0.0008 201 ALA A C   
1446 O O   . ALA A 175 ? 0.3006 0.3111 0.2693 -0.0416 -0.0333 -0.0013 201 ALA A O   
1447 C CB  . ALA A 175 ? 0.2992 0.3017 0.2448 -0.0365 -0.0312 -0.0067 201 ALA A CB  
1448 N N   . ASP A 176 ? 0.2922 0.2884 0.2589 -0.0401 -0.0267 -0.0001 202 ASP A N   
1449 C CA  . ASP A 176 ? 0.2958 0.2910 0.2722 -0.0445 -0.0266 0.0009  202 ASP A CA  
1450 C C   . ASP A 176 ? 0.2935 0.2957 0.2757 -0.0442 -0.0242 0.0069  202 ASP A C   
1451 O O   . ASP A 176 ? 0.2901 0.2984 0.2810 -0.0481 -0.0252 0.0075  202 ASP A O   
1452 C CB  . ASP A 176 ? 0.3345 0.3180 0.3118 -0.0456 -0.0248 0.0002  202 ASP A CB  
1453 C CG  . ASP A 176 ? 0.4115 0.3885 0.3864 -0.0465 -0.0281 -0.0075 202 ASP A CG  
1454 O OD1 . ASP A 176 ? 0.4370 0.4196 0.4111 -0.0479 -0.0319 -0.0124 202 ASP A OD1 
1455 O OD2 . ASP A 176 ? 0.4253 0.3922 0.3989 -0.0452 -0.0272 -0.0092 202 ASP A OD2 
1456 N N   . THR A 177 ? 0.2924 0.2946 0.2706 -0.0396 -0.0210 0.0108  203 THR A N   
1457 C CA  . THR A 177 ? 0.2956 0.3054 0.2790 -0.0384 -0.0187 0.0153  203 THR A CA  
1458 C C   . THR A 177 ? 0.2988 0.3197 0.2861 -0.0378 -0.0223 0.0144  203 THR A C   
1459 O O   . THR A 177 ? 0.2923 0.3223 0.2885 -0.0396 -0.0220 0.0156  203 THR A O   
1460 C CB  . THR A 177 ? 0.3050 0.3124 0.2828 -0.0331 -0.0156 0.0182  203 THR A CB  
1461 O OG1 . THR A 177 ? 0.3118 0.3092 0.2854 -0.0329 -0.0132 0.0184  203 THR A OG1 
1462 C CG2 . THR A 177 ? 0.3077 0.3232 0.2908 -0.0314 -0.0130 0.0218  203 THR A CG2 
1463 N N   . ALA A 178 ? 0.3102 0.3308 0.2910 -0.0355 -0.0260 0.0123  204 ALA A N   
1464 C CA  . ALA A 178 ? 0.3269 0.3565 0.3100 -0.0343 -0.0307 0.0117  204 ALA A CA  
1465 C C   . ALA A 178 ? 0.3401 0.3764 0.3310 -0.0390 -0.0343 0.0085  204 ALA A C   
1466 O O   . ALA A 178 ? 0.3340 0.3795 0.3295 -0.0379 -0.0382 0.0081  204 ALA A O   
1467 C CB  . ALA A 178 ? 0.3339 0.3604 0.3065 -0.0317 -0.0339 0.0112  204 ALA A CB  
1468 N N   . THR A 179 ? 0.3588 0.3903 0.3517 -0.0440 -0.0337 0.0058  205 THR A N   
1469 C CA  . THR A 179 ? 0.3821 0.4190 0.3830 -0.0492 -0.0374 0.0021  205 THR A CA  
1470 C C   . THR A 179 ? 0.4093 0.4460 0.4203 -0.0548 -0.0343 0.0035  205 THR A C   
1471 O O   . THR A 179 ? 0.4169 0.4541 0.4341 -0.0604 -0.0370 0.0002  205 THR A O   
1472 C CB  . THR A 179 ? 0.3990 0.4295 0.3932 -0.0510 -0.0410 -0.0036 205 THR A CB  
1473 O OG1 . THR A 179 ? 0.4119 0.4305 0.4010 -0.0509 -0.0374 -0.0040 205 THR A OG1 
1474 C CG2 . THR A 179 ? 0.4048 0.4380 0.3890 -0.0471 -0.0449 -0.0049 205 THR A CG2 
1475 N N   . LYS A 180 ? 0.4233 0.4591 0.4356 -0.0538 -0.0288 0.0085  206 LYS A N   
1476 C CA  . LYS A 180 ? 0.4435 0.4788 0.4637 -0.0595 -0.0252 0.0115  206 LYS A CA  
1477 C C   . LYS A 180 ? 0.4636 0.5127 0.4969 -0.0647 -0.0264 0.0112  206 LYS A C   
1478 O O   . LYS A 180 ? 0.4586 0.5208 0.4962 -0.0617 -0.0274 0.0110  206 LYS A O   
1479 C CB  . LYS A 180 ? 0.4598 0.4935 0.4771 -0.0565 -0.0193 0.0172  206 LYS A CB  
1480 N N   . SER A 181 ? 0.4845 0.5306 0.5248 -0.0725 -0.0265 0.0113  207 SER A N   
1481 C CA  . SER A 181 ? 0.5046 0.5642 0.5587 -0.0790 -0.0273 0.0111  207 SER A CA  
1482 C C   . SER A 181 ? 0.5215 0.5863 0.5819 -0.0836 -0.0209 0.0179  207 SER A C   
1483 O O   . SER A 181 ? 0.5388 0.5926 0.5929 -0.0835 -0.0170 0.0225  207 SER A O   
1484 C CB  . SER A 181 ? 0.5260 0.5800 0.5850 -0.0860 -0.0324 0.0064  207 SER A CB  
1485 O OG  . SER A 181 ? 0.5557 0.6226 0.6292 -0.0935 -0.0329 0.0067  207 SER A OG  
1486 N N   . LYS A 186 ? 0.4471 0.4133 0.4465 -0.0608 -0.0155 0.0228  212 LYS A N   
1487 C CA  . LYS A 186 ? 0.4592 0.4114 0.4563 -0.0602 -0.0193 0.0173  212 LYS A CA  
1488 C C   . LYS A 186 ? 0.4648 0.4117 0.4527 -0.0523 -0.0183 0.0151  212 LYS A C   
1489 O O   . LYS A 186 ? 0.4719 0.4265 0.4549 -0.0478 -0.0174 0.0128  212 LYS A O   
1490 C CB  . LYS A 186 ? 0.4823 0.4374 0.4825 -0.0624 -0.0240 0.0094  212 LYS A CB  
1491 N N   . ASN A 187 ? 0.4580 0.3918 0.4442 -0.0510 -0.0189 0.0159  213 ASN A N   
1492 C CA  . ASN A 187 ? 0.4608 0.3897 0.4396 -0.0437 -0.0180 0.0139  213 ASN A CA  
1493 C C   . ASN A 187 ? 0.4471 0.3680 0.4246 -0.0411 -0.0218 0.0048  213 ASN A C   
1494 O O   . ASN A 187 ? 0.4602 0.3696 0.4421 -0.0436 -0.0254 0.0028  213 ASN A O   
1495 C CB  . ASN A 187 ? 0.4849 0.4052 0.4625 -0.0428 -0.0164 0.0209  213 ASN A CB  
1496 C CG  . ASN A 187 ? 0.5283 0.4578 0.5049 -0.0434 -0.0118 0.0289  213 ASN A CG  
1497 O OD1 . ASN A 187 ? 0.5398 0.4807 0.5139 -0.0404 -0.0094 0.0285  213 ASN A OD1 
1498 N ND2 . ASN A 187 ? 0.5464 0.4709 0.5247 -0.0471 -0.0109 0.0363  213 ASN A ND2 
1499 N N   . ARG A 188 ? 0.4151 0.3416 0.3867 -0.0357 -0.0210 -0.0006 214 ARG A N   
1500 C CA  . ARG A 188 ? 0.3993 0.3215 0.3687 -0.0322 -0.0237 -0.0100 214 ARG A CA  
1501 C C   . ARG A 188 ? 0.3842 0.2946 0.3534 -0.0279 -0.0244 -0.0102 214 ARG A C   
1502 O O   . ARG A 188 ? 0.3815 0.2829 0.3531 -0.0266 -0.0282 -0.0171 214 ARG A O   
1503 C CB  . ARG A 188 ? 0.4185 0.3520 0.3809 -0.0283 -0.0217 -0.0139 214 ARG A CB  
1504 C CG  . ARG A 188 ? 0.4629 0.4078 0.4242 -0.0315 -0.0218 -0.0135 214 ARG A CG  
1505 C CD  . ARG A 188 ? 0.5032 0.4478 0.4674 -0.0351 -0.0262 -0.0204 214 ARG A CD  
1506 N NE  . ARG A 188 ? 0.5410 0.4973 0.5030 -0.0371 -0.0269 -0.0204 214 ARG A NE  
1507 C CZ  . ARG A 188 ? 0.5764 0.5405 0.5312 -0.0351 -0.0272 -0.0250 214 ARG A CZ  
1508 N NH1 . ARG A 188 ? 0.5771 0.5400 0.5267 -0.0312 -0.0263 -0.0305 214 ARG A NH1 
1509 N NH2 . ARG A 188 ? 0.5711 0.5447 0.5237 -0.0370 -0.0287 -0.0238 214 ARG A NH2 
1510 N N   . PHE A 189 ? 0.3749 0.2855 0.3415 -0.0252 -0.0212 -0.0034 215 PHE A N   
1511 C CA  . PHE A 189 ? 0.3717 0.2720 0.3378 -0.0206 -0.0221 -0.0027 215 PHE A CA  
1512 C C   . PHE A 189 ? 0.3643 0.2615 0.3300 -0.0219 -0.0201 0.0081  215 PHE A C   
1513 O O   . PHE A 189 ? 0.3501 0.2562 0.3152 -0.0250 -0.0169 0.0140  215 PHE A O   
1514 C CB  . PHE A 189 ? 0.3719 0.2786 0.3333 -0.0137 -0.0202 -0.0078 215 PHE A CB  
1515 C CG  . PHE A 189 ? 0.3853 0.2994 0.3450 -0.0126 -0.0207 -0.0176 215 PHE A CG  
1516 C CD1 . PHE A 189 ? 0.4005 0.3082 0.3631 -0.0112 -0.0246 -0.0266 215 PHE A CD1 
1517 C CD2 . PHE A 189 ? 0.3971 0.3244 0.3521 -0.0129 -0.0175 -0.0177 215 PHE A CD2 
1518 C CE1 . PHE A 189 ? 0.4099 0.3263 0.3700 -0.0103 -0.0249 -0.0359 215 PHE A CE1 
1519 C CE2 . PHE A 189 ? 0.4059 0.3409 0.3582 -0.0124 -0.0179 -0.0257 215 PHE A CE2 
1520 C CZ  . PHE A 189 ? 0.4035 0.3339 0.3580 -0.0112 -0.0213 -0.0350 215 PHE A CZ  
1521 N N   . VAL A 190 ? 0.3704 0.2555 0.3364 -0.0193 -0.0223 0.0104  216 VAL A N   
1522 C CA  . VAL A 190 ? 0.3909 0.2726 0.3549 -0.0196 -0.0208 0.0205  216 VAL A CA  
1523 C C   . VAL A 190 ? 0.4131 0.2898 0.3738 -0.0118 -0.0219 0.0191  216 VAL A C   
1524 O O   . VAL A 190 ? 0.4142 0.2860 0.3766 -0.0073 -0.0250 0.0108  216 VAL A O   
1525 C CB  . VAL A 190 ? 0.4024 0.2723 0.3702 -0.0262 -0.0234 0.0276  216 VAL A CB  
1526 C CG1 . VAL A 190 ? 0.3995 0.2756 0.3718 -0.0343 -0.0223 0.0289  216 VAL A CG1 
1527 C CG2 . VAL A 190 ? 0.4142 0.2665 0.3853 -0.0243 -0.0297 0.0236  216 VAL A CG2 
1528 N N   . VAL A 191 ? 0.4274 0.3063 0.3839 -0.0100 -0.0197 0.0264  217 VAL A N   
1529 C CA  . VAL A 191 ? 0.4486 0.3230 0.4025 -0.0027 -0.0213 0.0256  217 VAL A CA  
1530 C C   . VAL A 191 ? 0.4656 0.3358 0.4154 -0.0032 -0.0210 0.0364  217 VAL A C   
1531 O O   . VAL A 191 ? 0.4778 0.3384 0.4261 0.0014  -0.0246 0.0379  217 VAL A O   
1532 C CB  . VAL A 191 ? 0.4623 0.3487 0.4141 0.0030  -0.0188 0.0189  217 VAL A CB  
1533 C CG1 . VAL A 191 ? 0.4668 0.3645 0.4144 0.0029  -0.0143 0.0242  217 VAL A CG1 
1534 C CG2 . VAL A 191 ? 0.4753 0.3563 0.4279 0.0105  -0.0220 0.0139  217 VAL A CG2 
1535 O OXT . VAL A 191 ? 0.4534 0.3305 0.4013 -0.0082 -0.0174 0.0434  217 VAL A OXT 
1536 N N   . ALA B 3   ? 0.7148 0.4583 0.6782 0.0384  -0.0855 -0.0775 29  ALA B N   
1537 C CA  . ALA B 3   ? 0.7277 0.4462 0.6882 0.0364  -0.1007 -0.0761 29  ALA B CA  
1538 C C   . ALA B 3   ? 0.7357 0.4446 0.6782 0.0271  -0.1033 -0.0743 29  ALA B C   
1539 O O   . ALA B 3   ? 0.7516 0.4386 0.6880 0.0275  -0.1123 -0.0803 29  ALA B O   
1540 C CB  . ALA B 3   ? 0.7306 0.4456 0.6997 0.0318  -0.1124 -0.0611 29  ALA B CB  
1541 N N   . ASN B 4   ? 0.7239 0.4482 0.6582 0.0188  -0.0962 -0.0663 30  ASN B N   
1542 C CA  . ASN B 4   ? 0.7262 0.4435 0.6447 0.0096  -0.0989 -0.0638 30  ASN B CA  
1543 C C   . ASN B 4   ? 0.6990 0.4253 0.6060 0.0114  -0.0860 -0.0741 30  ASN B C   
1544 O O   . ASN B 4   ? 0.6897 0.4360 0.6004 0.0133  -0.0746 -0.0735 30  ASN B O   
1545 C CB  . ASN B 4   ? 0.7516 0.4803 0.6701 -0.0017 -0.1014 -0.0465 30  ASN B CB  
1546 C CG  . ASN B 4   ? 0.8147 0.5290 0.7338 -0.0100 -0.1163 -0.0355 30  ASN B CG  
1547 O OD1 . ASN B 4   ? 0.8464 0.5385 0.7642 -0.0085 -0.1269 -0.0399 30  ASN B OD1 
1548 N ND2 . ASN B 4   ? 0.8197 0.5467 0.7408 -0.0194 -0.1172 -0.0210 30  ASN B ND2 
1549 N N   . PRO B 5   ? 0.6849 0.3964 0.5765 0.0096  -0.0880 -0.0825 31  PRO B N   
1550 C CA  . PRO B 5   ? 0.6712 0.3908 0.5492 0.0097  -0.0760 -0.0912 31  PRO B CA  
1551 C C   . PRO B 5   ? 0.6496 0.3883 0.5246 0.0018  -0.0703 -0.0797 31  PRO B C   
1552 O O   . PRO B 5   ? 0.6518 0.3913 0.5280 -0.0063 -0.0778 -0.0668 31  PRO B O   
1553 C CB  . PRO B 5   ? 0.6948 0.3923 0.5551 0.0063  -0.0830 -0.0986 31  PRO B CB  
1554 C CG  . PRO B 5   ? 0.7124 0.3893 0.5799 0.0090  -0.0966 -0.0993 31  PRO B CG  
1555 C CD  . PRO B 5   ? 0.6872 0.3732 0.5721 0.0070  -0.1017 -0.0847 31  PRO B CD  
1556 N N   . GLU B 6   ? 0.6234 0.3779 0.4961 0.0045  -0.0571 -0.0843 32  GLU B N   
1557 C CA  . GLU B 6   ? 0.6048 0.3764 0.4750 -0.0018 -0.0518 -0.0747 32  GLU B CA  
1558 C C   . GLU B 6   ? 0.5900 0.3571 0.4400 -0.0079 -0.0499 -0.0778 32  GLU B C   
1559 O O   . GLU B 6   ? 0.5924 0.3511 0.4303 -0.0050 -0.0454 -0.0905 32  GLU B O   
1560 C CB  . GLU B 6   ? 0.6332 0.4243 0.5126 0.0038  -0.0394 -0.0768 32  GLU B CB  
1561 C CG  . GLU B 6   ? 0.7075 0.5073 0.6064 0.0078  -0.0413 -0.0700 32  GLU B CG  
1562 C CD  . GLU B 6   ? 0.8024 0.6218 0.7095 0.0119  -0.0300 -0.0711 32  GLU B CD  
1563 O OE1 . GLU B 6   ? 0.8216 0.6520 0.7215 0.0074  -0.0235 -0.0678 32  GLU B OE1 
1564 O OE2 . GLU B 6   ? 0.8439 0.6669 0.7651 0.0194  -0.0283 -0.0750 32  GLU B OE2 
1565 N N   . HIS B 7   ? 0.5743 0.3479 0.4207 -0.0161 -0.0528 -0.0668 33  HIS B N   
1566 C CA  . HIS B 7   ? 0.5793 0.3487 0.4067 -0.0224 -0.0523 -0.0684 33  HIS B CA  
1567 C C   . HIS B 7   ? 0.5871 0.3698 0.4086 -0.0207 -0.0394 -0.0726 33  HIS B C   
1568 O O   . HIS B 7   ? 0.5969 0.3729 0.4008 -0.0218 -0.0350 -0.0816 33  HIS B O   
1569 C CB  . HIS B 7   ? 0.5774 0.3493 0.4053 -0.0313 -0.0611 -0.0552 33  HIS B CB  
1570 C CG  . HIS B 7   ? 0.5949 0.3495 0.4191 -0.0364 -0.0743 -0.0530 33  HIS B CG  
1571 N ND1 . HIS B 7   ? 0.6091 0.3626 0.4479 -0.0376 -0.0824 -0.0450 33  HIS B ND1 
1572 C CD2 . HIS B 7   ? 0.6150 0.3524 0.4218 -0.0410 -0.0808 -0.0580 33  HIS B CD2 
1573 C CE1 . HIS B 7   ? 0.6192 0.3553 0.4503 -0.0431 -0.0937 -0.0449 33  HIS B CE1 
1574 N NE2 . HIS B 7   ? 0.6301 0.3557 0.4420 -0.0450 -0.0934 -0.0529 33  HIS B NE2 
1575 N N   . TYR B 8   ? 0.5761 0.3772 0.4109 -0.0189 -0.0336 -0.0659 34  TYR B N   
1576 C CA  . TYR B 8   ? 0.5815 0.3959 0.4120 -0.0186 -0.0224 -0.0679 34  TYR B CA  
1577 C C   . TYR B 8   ? 0.5583 0.3877 0.4065 -0.0117 -0.0150 -0.0680 34  TYR B C   
1578 O O   . TYR B 8   ? 0.5537 0.3861 0.4176 -0.0090 -0.0196 -0.0623 34  TYR B O   
1579 C CB  . TYR B 8   ? 0.5951 0.4166 0.4208 -0.0258 -0.0247 -0.0574 34  TYR B CB  
1580 C CG  . TYR B 8   ? 0.6280 0.4369 0.4422 -0.0331 -0.0355 -0.0534 34  TYR B CG  
1581 C CD1 . TYR B 8   ? 0.6541 0.4481 0.4477 -0.0364 -0.0367 -0.0613 34  TYR B CD1 
1582 C CD2 . TYR B 8   ? 0.6374 0.4497 0.4617 -0.0370 -0.0444 -0.0421 34  TYR B CD2 
1583 C CE1 . TYR B 8   ? 0.6764 0.4574 0.4600 -0.0431 -0.0480 -0.0579 34  TYR B CE1 
1584 C CE2 . TYR B 8   ? 0.6572 0.4588 0.4731 -0.0439 -0.0548 -0.0384 34  TYR B CE2 
1585 C CZ  . TYR B 8   ? 0.6820 0.4675 0.4775 -0.0470 -0.0572 -0.0461 34  TYR B CZ  
1586 O OH  . TYR B 8   ? 0.7133 0.4871 0.5001 -0.0542 -0.0686 -0.0425 34  TYR B OH  
1587 N N   . ILE B 9   ? 0.5434 0.3824 0.3887 -0.0097 -0.0038 -0.0738 35  ILE B N   
1588 C CA  . ILE B 9   ? 0.5244 0.3787 0.3860 -0.0040 0.0035  -0.0741 35  ILE B CA  
1589 C C   . ILE B 9   ? 0.4941 0.3605 0.3630 -0.0072 0.0020  -0.0617 35  ILE B C   
1590 O O   . ILE B 9   ? 0.5013 0.3682 0.3597 -0.0135 0.0005  -0.0562 35  ILE B O   
1591 C CB  . ILE B 9   ? 0.5401 0.4010 0.3945 -0.0025 0.0161  -0.0844 35  ILE B CB  
1592 C CG1 . ILE B 9   ? 0.5691 0.4186 0.4162 0.0014  0.0185  -0.0983 35  ILE B CG1 
1593 C CG2 . ILE B 9   ? 0.5379 0.4159 0.4096 0.0025  0.0236  -0.0843 35  ILE B CG2 
1594 C CD1 . ILE B 9   ? 0.5861 0.4312 0.4510 0.0104  0.0142  -0.1029 35  ILE B CD1 
1595 N N   . LYS B 10  ? 0.4586 0.3341 0.3450 -0.0028 0.0016  -0.0575 36  LYS B N   
1596 C CA  . LYS B 10  ? 0.4332 0.3204 0.3265 -0.0049 0.0010  -0.0473 36  LYS B CA  
1597 C C   . LYS B 10  ? 0.4132 0.3123 0.3049 -0.0052 0.0104  -0.0490 36  LYS B C   
1598 O O   . LYS B 10  ? 0.4210 0.3225 0.3121 -0.0023 0.0180  -0.0576 36  LYS B O   
1599 C CB  . LYS B 10  ? 0.4375 0.3286 0.3475 -0.0010 -0.0034 -0.0421 36  LYS B CB  
1600 C CG  . LYS B 10  ? 0.4683 0.3494 0.3790 -0.0037 -0.0136 -0.0367 36  LYS B CG  
1601 C CD  . LYS B 10  ? 0.5008 0.3850 0.4258 -0.0009 -0.0179 -0.0311 36  LYS B CD  
1602 C CE  . LYS B 10  ? 0.5370 0.4116 0.4622 -0.0049 -0.0279 -0.0249 36  LYS B CE  
1603 N NZ  . LYS B 10  ? 0.5517 0.4267 0.4887 -0.0028 -0.0326 -0.0199 36  LYS B NZ  
1604 N N   . HIS B 11  ? 0.3828 0.2889 0.2735 -0.0089 0.0098  -0.0411 37  HIS B N   
1605 C CA  . HIS B 11  ? 0.3650 0.2805 0.2531 -0.0105 0.0166  -0.0409 37  HIS B CA  
1606 C C   . HIS B 11  ? 0.3447 0.2722 0.2487 -0.0062 0.0191  -0.0384 37  HIS B C   
1607 O O   . HIS B 11  ? 0.3373 0.2681 0.2487 -0.0057 0.0142  -0.0312 37  HIS B O   
1608 C CB  . HIS B 11  ? 0.3669 0.2809 0.2452 -0.0166 0.0125  -0.0337 37  HIS B CB  
1609 C CG  . HIS B 11  ? 0.4088 0.3105 0.2706 -0.0216 0.0090  -0.0357 37  HIS B CG  
1610 N ND1 . HIS B 11  ? 0.4346 0.3276 0.2961 -0.0225 0.0008  -0.0335 37  HIS B ND1 
1611 C CD2 . HIS B 11  ? 0.4297 0.3260 0.2742 -0.0262 0.0125  -0.0398 37  HIS B CD2 
1612 C CE1 . HIS B 11  ? 0.4528 0.3350 0.2972 -0.0273 -0.0010 -0.0365 37  HIS B CE1 
1613 N NE2 . HIS B 11  ? 0.4525 0.3361 0.2854 -0.0298 0.0060  -0.0403 37  HIS B NE2 
1614 N N   . PRO B 12  ? 0.3359 0.2705 0.2453 -0.0032 0.0266  -0.0444 38  PRO B N   
1615 C CA  . PRO B 12  ? 0.3142 0.2597 0.2392 0.0007  0.0279  -0.0421 38  PRO B CA  
1616 C C   . PRO B 12  ? 0.2859 0.2387 0.2105 -0.0023 0.0282  -0.0354 38  PRO B C   
1617 O O   . PRO B 12  ? 0.2838 0.2363 0.1973 -0.0073 0.0305  -0.0345 38  PRO B O   
1618 C CB  . PRO B 12  ? 0.3268 0.2785 0.2578 0.0041  0.0362  -0.0512 38  PRO B CB  
1619 C CG  . PRO B 12  ? 0.3540 0.2969 0.2734 0.0032  0.0389  -0.0592 38  PRO B CG  
1620 C CD  . PRO B 12  ? 0.3449 0.2786 0.2471 -0.0034 0.0344  -0.0540 38  PRO B CD  
1621 N N   . LEU B 13  ? 0.2562 0.2150 0.1926 0.0007  0.0253  -0.0308 39  LEU B N   
1622 C CA  . LEU B 13  ? 0.2390 0.2049 0.1773 -0.0008 0.0253  -0.0255 39  LEU B CA  
1623 C C   . LEU B 13  ? 0.2457 0.2205 0.1917 0.0007  0.0314  -0.0295 39  LEU B C   
1624 O O   . LEU B 13  ? 0.2341 0.2111 0.1879 0.0043  0.0345  -0.0355 39  LEU B O   
1625 C CB  . LEU B 13  ? 0.2181 0.1862 0.1648 0.0018  0.0195  -0.0195 39  LEU B CB  
1626 C CG  . LEU B 13  ? 0.2307 0.1931 0.1727 0.0000  0.0135  -0.0147 39  LEU B CG  
1627 C CD1 . LEU B 13  ? 0.2293 0.1956 0.1793 0.0020  0.0092  -0.0092 39  LEU B CD1 
1628 C CD2 . LEU B 13  ? 0.2296 0.1903 0.1616 -0.0044 0.0127  -0.0121 39  LEU B CD2 
1629 N N   . GLN B 14  ? 0.2521 0.2323 0.1971 -0.0020 0.0328  -0.0264 40  GLN B N   
1630 C CA  . GLN B 14  ? 0.2650 0.2546 0.2184 -0.0017 0.0379  -0.0291 40  GLN B CA  
1631 C C   . GLN B 14  ? 0.2596 0.2543 0.2290 0.0042  0.0351  -0.0290 40  GLN B C   
1632 O O   . GLN B 14  ? 0.2657 0.2673 0.2460 0.0067  0.0388  -0.0337 40  GLN B O   
1633 C CB  . GLN B 14  ? 0.3154 0.3072 0.2634 -0.0064 0.0379  -0.0247 40  GLN B CB  
1634 C CG  . GLN B 14  ? 0.3991 0.4009 0.3567 -0.0070 0.0416  -0.0258 40  GLN B CG  
1635 C CD  . GLN B 14  ? 0.4894 0.4976 0.4486 -0.0093 0.0502  -0.0320 40  GLN B CD  
1636 O OE1 . GLN B 14  ? 0.5034 0.5218 0.4762 -0.0074 0.0535  -0.0349 40  GLN B OE1 
1637 N NE2 . GLN B 14  ? 0.5124 0.5156 0.4577 -0.0136 0.0540  -0.0345 40  GLN B NE2 
1638 N N   . ASN B 15  ? 0.2408 0.2322 0.2117 0.0062  0.0284  -0.0238 41  ASN B N   
1639 C CA  . ASN B 15  ? 0.2397 0.2345 0.2231 0.0108  0.0247  -0.0227 41  ASN B CA  
1640 C C   . ASN B 15  ? 0.2407 0.2284 0.2248 0.0132  0.0190  -0.0207 41  ASN B C   
1641 O O   . ASN B 15  ? 0.2471 0.2285 0.2222 0.0110  0.0173  -0.0187 41  ASN B O   
1642 C CB  . ASN B 15  ? 0.2465 0.2454 0.2310 0.0099  0.0219  -0.0176 41  ASN B CB  
1643 C CG  . ASN B 15  ? 0.2760 0.2822 0.2644 0.0080  0.0259  -0.0194 41  ASN B CG  
1644 O OD1 . ASN B 15  ? 0.3014 0.3140 0.3018 0.0103  0.0272  -0.0224 41  ASN B OD1 
1645 N ND2 . ASN B 15  ? 0.2570 0.2623 0.2363 0.0037  0.0272  -0.0175 41  ASN B ND2 
1646 N N   . ARG B 16  ? 0.2217 0.2104 0.2167 0.0172  0.0153  -0.0206 42  ARG B N   
1647 C CA  . ARG B 16  ? 0.2254 0.2070 0.2209 0.0186  0.0087  -0.0172 42  ARG B CA  
1648 C C   . ARG B 16  ? 0.2091 0.1933 0.2023 0.0169  0.0048  -0.0100 42  ARG B C   
1649 O O   . ARG B 16  ? 0.1978 0.1882 0.1947 0.0174  0.0053  -0.0092 42  ARG B O   
1650 C CB  . ARG B 16  ? 0.2488 0.2284 0.2570 0.0237  0.0055  -0.0207 42  ARG B CB  
1651 C CG  . ARG B 16  ? 0.3219 0.2917 0.3295 0.0242  -0.0024 -0.0167 42  ARG B CG  
1652 C CD  . ARG B 16  ? 0.4151 0.3801 0.4348 0.0298  -0.0062 -0.0215 42  ARG B CD  
1653 N NE  . ARG B 16  ? 0.5135 0.4768 0.5339 0.0321  -0.0007 -0.0306 42  ARG B NE  
1654 C CZ  . ARG B 16  ? 0.5837 0.5482 0.6168 0.0380  0.0003  -0.0385 42  ARG B CZ  
1655 N NH1 . ARG B 16  ? 0.5840 0.5508 0.6315 0.0425  -0.0051 -0.0379 42  ARG B NH1 
1656 N NH2 . ARG B 16  ? 0.6018 0.5654 0.6333 0.0397  0.0065  -0.0474 42  ARG B NH2 
1657 N N   . TRP B 17  ? 0.2000 0.1798 0.1865 0.0146  0.0013  -0.0050 43  TRP B N   
1658 C CA  . TRP B 17  ? 0.2050 0.1881 0.1879 0.0128  -0.0010 0.0010  43  TRP B CA  
1659 C C   . TRP B 17  ? 0.2215 0.2005 0.2050 0.0121  -0.0072 0.0063  43  TRP B C   
1660 O O   . TRP B 17  ? 0.2154 0.1874 0.1996 0.0119  -0.0100 0.0062  43  TRP B O   
1661 C CB  . TRP B 17  ? 0.1985 0.1828 0.1727 0.0097  0.0013  0.0028  43  TRP B CB  
1662 C CG  . TRP B 17  ? 0.2070 0.1940 0.1786 0.0092  0.0060  -0.0008 43  TRP B CG  
1663 C CD1 . TRP B 17  ? 0.2246 0.2087 0.1932 0.0082  0.0092  -0.0049 43  TRP B CD1 
1664 C CD2 . TRP B 17  ? 0.2041 0.1963 0.1751 0.0093  0.0074  -0.0006 43  TRP B CD2 
1665 N NE1 . TRP B 17  ? 0.2246 0.2119 0.1906 0.0070  0.0126  -0.0065 43  TRP B NE1 
1666 C CE2 . TRP B 17  ? 0.2129 0.2047 0.1806 0.0077  0.0111  -0.0037 43  TRP B CE2 
1667 C CE3 . TRP B 17  ? 0.2086 0.2047 0.1799 0.0101  0.0055  0.0021  43  TRP B CE3 
1668 C CZ2 . TRP B 17  ? 0.2100 0.2047 0.1759 0.0068  0.0123  -0.0038 43  TRP B CZ2 
1669 C CZ3 . TRP B 17  ? 0.2197 0.2185 0.1892 0.0099  0.0068  0.0011  43  TRP B CZ3 
1670 C CH2 . TRP B 17  ? 0.2179 0.2157 0.1853 0.0082  0.0099  -0.0016 43  TRP B CH2 
1671 N N   . ALA B 18  ? 0.2262 0.2087 0.2078 0.0111  -0.0096 0.0109  44  ALA B N   
1672 C CA  . ALA B 18  ? 0.2337 0.2125 0.2135 0.0089  -0.0153 0.0170  44  ALA B CA  
1673 C C   . ALA B 18  ? 0.2247 0.2092 0.1965 0.0052  -0.0139 0.0218  44  ALA B C   
1674 O O   . ALA B 18  ? 0.2271 0.2178 0.1964 0.0060  -0.0110 0.0208  44  ALA B O   
1675 C CB  . ALA B 18  ? 0.2376 0.2146 0.2228 0.0110  -0.0206 0.0182  44  ALA B CB  
1676 N N   . LEU B 19  ? 0.2210 0.2036 0.1891 0.0012  -0.0159 0.0266  45  LEU B N   
1677 C CA  . LEU B 19  ? 0.2305 0.2206 0.1925 -0.0025 -0.0140 0.0311  45  LEU B CA  
1678 C C   . LEU B 19  ? 0.2418 0.2312 0.1998 -0.0052 -0.0183 0.0367  45  LEU B C   
1679 O O   . LEU B 19  ? 0.2450 0.2261 0.2040 -0.0070 -0.0244 0.0404  45  LEU B O   
1680 C CB  . LEU B 19  ? 0.2402 0.2304 0.2013 -0.0067 -0.0139 0.0339  45  LEU B CB  
1681 C CG  . LEU B 19  ? 0.2667 0.2663 0.2236 -0.0113 -0.0119 0.0390  45  LEU B CG  
1682 C CD1 . LEU B 19  ? 0.2633 0.2730 0.2198 -0.0088 -0.0059 0.0353  45  LEU B CD1 
1683 C CD2 . LEU B 19  ? 0.2840 0.2822 0.2417 -0.0167 -0.0140 0.0434  45  LEU B CD2 
1684 N N   . TRP B 20  ? 0.2459 0.2427 0.1984 -0.0055 -0.0157 0.0373  46  TRP B N   
1685 C CA  . TRP B 20  ? 0.2682 0.2650 0.2135 -0.0088 -0.0190 0.0426  46  TRP B CA  
1686 C C   . TRP B 20  ? 0.3028 0.3097 0.2402 -0.0132 -0.0143 0.0457  46  TRP B C   
1687 O O   . TRP B 20  ? 0.2934 0.3086 0.2318 -0.0111 -0.0083 0.0417  46  TRP B O   
1688 C CB  . TRP B 20  ? 0.2549 0.2517 0.1994 -0.0051 -0.0200 0.0395  46  TRP B CB  
1689 C CG  . TRP B 20  ? 0.2490 0.2389 0.2028 -0.0009 -0.0242 0.0363  46  TRP B CG  
1690 C CD1 . TRP B 20  ? 0.2510 0.2410 0.2131 0.0034  -0.0212 0.0302  46  TRP B CD1 
1691 C CD2 . TRP B 20  ? 0.2456 0.2286 0.2016 -0.0005 -0.0320 0.0389  46  TRP B CD2 
1692 N NE1 . TRP B 20  ? 0.2506 0.2360 0.2211 0.0066  -0.0256 0.0282  46  TRP B NE1 
1693 C CE2 . TRP B 20  ? 0.2503 0.2310 0.2183 0.0047  -0.0329 0.0334  46  TRP B CE2 
1694 C CE3 . TRP B 20  ? 0.2618 0.2406 0.2106 -0.0044 -0.0387 0.0454  46  TRP B CE3 
1695 C CZ2 . TRP B 20  ? 0.2550 0.2304 0.2304 0.0070  -0.0402 0.0338  46  TRP B CZ2 
1696 C CZ3 . TRP B 20  ? 0.2691 0.2402 0.2238 -0.0025 -0.0472 0.0466  46  TRP B CZ3 
1697 C CH2 . TRP B 20  ? 0.2636 0.2337 0.2326 0.0036  -0.0480 0.0405  46  TRP B CH2 
1698 N N   . PHE B 21  ? 0.3279 0.3343 0.2575 -0.0192 -0.0173 0.0527  47  PHE B N   
1699 C CA  . PHE B 21  ? 0.3605 0.3778 0.2817 -0.0242 -0.0123 0.0558  47  PHE B CA  
1700 C C   . PHE B 21  ? 0.3694 0.3864 0.2789 -0.0261 -0.0141 0.0579  47  PHE B C   
1701 O O   . PHE B 21  ? 0.3525 0.3590 0.2601 -0.0265 -0.0217 0.0607  47  PHE B O   
1702 C CB  . PHE B 21  ? 0.3860 0.4035 0.3056 -0.0323 -0.0141 0.0637  47  PHE B CB  
1703 C CG  . PHE B 21  ? 0.4269 0.4476 0.3553 -0.0330 -0.0119 0.0632  47  PHE B CG  
1704 C CD1 . PHE B 21  ? 0.4500 0.4719 0.3867 -0.0265 -0.0088 0.0560  47  PHE B CD1 
1705 C CD2 . PHE B 21  ? 0.4526 0.4741 0.3802 -0.0410 -0.0136 0.0704  47  PHE B CD2 
1706 C CE1 . PHE B 21  ? 0.4670 0.4904 0.4106 -0.0276 -0.0080 0.0558  47  PHE B CE1 
1707 C CE2 . PHE B 21  ? 0.4661 0.4903 0.4019 -0.0421 -0.0125 0.0701  47  PHE B CE2 
1708 C CZ  . PHE B 21  ? 0.4665 0.4913 0.4101 -0.0352 -0.0099 0.0626  47  PHE B CZ  
1709 N N   . PHE B 22  ? 0.3946 0.4229 0.2962 -0.0276 -0.0074 0.0566  48  PHE B N   
1710 C CA  . PHE B 22  ? 0.4384 0.4669 0.3259 -0.0305 -0.0084 0.0585  48  PHE B CA  
1711 C C   . PHE B 22  ? 0.4862 0.5242 0.3638 -0.0390 -0.0039 0.0643  48  PHE B C   
1712 O O   . PHE B 22  ? 0.4829 0.5347 0.3635 -0.0389 0.0046  0.0614  48  PHE B O   
1713 C CB  . PHE B 22  ? 0.4353 0.4682 0.3201 -0.0241 -0.0041 0.0501  48  PHE B CB  
1714 C CG  . PHE B 22  ? 0.4532 0.4834 0.3224 -0.0269 -0.0067 0.0515  48  PHE B CG  
1715 C CD1 . PHE B 22  ? 0.4688 0.4870 0.3365 -0.0259 -0.0158 0.0530  48  PHE B CD1 
1716 C CD2 . PHE B 22  ? 0.4699 0.5102 0.3259 -0.0308 -0.0003 0.0514  48  PHE B CD2 
1717 C CE1 . PHE B 22  ? 0.4868 0.5014 0.3390 -0.0290 -0.0194 0.0548  48  PHE B CE1 
1718 C CE2 . PHE B 22  ? 0.4848 0.5216 0.3239 -0.0340 -0.0029 0.0526  48  PHE B CE2 
1719 C CZ  . PHE B 22  ? 0.4870 0.5102 0.3238 -0.0333 -0.0130 0.0547  48  PHE B CZ  
1720 N N   . LYS B 23  ? 0.5258 0.5568 0.3926 -0.0468 -0.0101 0.0729  49  LYS B N   
1721 C CA  . LYS B 23  ? 0.5751 0.6137 0.4309 -0.0571 -0.0070 0.0804  49  LYS B CA  
1722 C C   . LYS B 23  ? 0.6155 0.6635 0.4547 -0.0596 -0.0007 0.0785  49  LYS B C   
1723 O O   . LYS B 23  ? 0.6234 0.6659 0.4555 -0.0554 -0.0031 0.0743  49  LYS B O   
1724 C CB  . LYS B 23  ? 0.6198 0.6437 0.4699 -0.0649 -0.0182 0.0913  49  LYS B CB  
1725 C CG  . LYS B 23  ? 0.6875 0.7169 0.5313 -0.0768 -0.0167 0.1008  49  LYS B CG  
1726 C CD  . LYS B 23  ? 0.7542 0.7658 0.5923 -0.0842 -0.0298 0.1117  49  LYS B CD  
1727 C CE  . LYS B 23  ? 0.8030 0.8195 0.6291 -0.0983 -0.0288 0.1225  49  LYS B CE  
1728 N NZ  . LYS B 23  ? 0.8357 0.8635 0.6429 -0.1040 -0.0215 0.1233  49  LYS B NZ  
1729 N N   . ASN B 24  ? 0.6399 0.7026 0.4729 -0.0668 0.0076  0.0813  50  ASN B N   
1730 C CA  . ASN B 24  ? 0.6732 0.7458 0.4887 -0.0702 0.0147  0.0793  50  ASN B CA  
1731 C C   . ASN B 24  ? 0.6976 0.7625 0.4944 -0.0827 0.0084  0.0910  50  ASN B C   
1732 O O   . ASN B 24  ? 0.6982 0.7710 0.4915 -0.0927 0.0117  0.0986  50  ASN B O   
1733 C CB  . ASN B 24  ? 0.6945 0.7899 0.5146 -0.0711 0.0282  0.0752  50  ASN B CB  
1734 C CG  . ASN B 24  ? 0.7541 0.8609 0.5606 -0.0695 0.0374  0.0676  50  ASN B CG  
1735 O OD1 . ASN B 24  ? 0.7767 0.8787 0.5818 -0.0605 0.0368  0.0588  50  ASN B OD1 
1736 N ND2 . ASN B 24  ? 0.7657 0.8881 0.5616 -0.0784 0.0462  0.0707  50  ASN B ND2 
1737 N N   . ASP B 25  ? 0.7187 0.7676 0.5040 -0.0827 -0.0014 0.0932  51  ASP B N   
1738 C CA  . ASP B 25  ? 0.7455 0.7845 0.5114 -0.0946 -0.0093 0.1049  51  ASP B CA  
1739 C C   . ASP B 25  ? 0.7620 0.7956 0.5087 -0.0941 -0.0117 0.1020  51  ASP B C   
1740 O O   . ASP B 25  ? 0.7716 0.7914 0.5216 -0.0876 -0.0211 0.0996  51  ASP B O   
1741 C CB  . ASP B 25  ? 0.7798 0.7994 0.5539 -0.0963 -0.0241 0.1134  51  ASP B CB  
1742 C CG  . ASP B 25  ? 0.8586 0.8657 0.6143 -0.1091 -0.0344 0.1268  51  ASP B CG  
1743 O OD1 . ASP B 25  ? 0.8750 0.8860 0.6084 -0.1166 -0.0314 0.1294  51  ASP B OD1 
1744 O OD2 . ASP B 25  ? 0.8928 0.8853 0.6555 -0.1117 -0.0458 0.1345  51  ASP B OD2 
1745 N N   . LYS B 26  ? 0.7625 0.8074 0.4889 -0.1014 -0.0031 0.1022  52  LYS B N   
1746 C CA  . LYS B 26  ? 0.7709 0.8116 0.4759 -0.1017 -0.0041 0.0986  52  LYS B CA  
1747 C C   . LYS B 26  ? 0.7758 0.7961 0.4645 -0.1092 -0.0197 0.1091  52  LYS B C   
1748 O O   . LYS B 26  ? 0.7884 0.7997 0.4657 -0.1063 -0.0253 0.1056  52  LYS B O   
1749 C CB  . LYS B 26  ? 0.8020 0.8617 0.4896 -0.1071 0.0108  0.0946  52  LYS B CB  
1750 C CG  . LYS B 26  ? 0.8561 0.9322 0.5567 -0.0952 0.0238  0.0795  52  LYS B CG  
1751 C CD  . LYS B 26  ? 0.9203 0.9856 0.6222 -0.0836 0.0186  0.0695  52  LYS B CD  
1752 C CE  . LYS B 26  ? 0.9542 1.0293 0.6774 -0.0705 0.0263  0.0569  52  LYS B CE  
1753 N NZ  . LYS B 26  ? 0.9840 1.0477 0.7078 -0.0608 0.0204  0.0484  52  LYS B NZ  
1754 N N   . SER B 27  ? 0.7644 0.7759 0.4526 -0.1186 -0.0281 0.1220  53  SER B N   
1755 C CA  . SER B 27  ? 0.7675 0.7578 0.4420 -0.1254 -0.0450 0.1326  53  SER B CA  
1756 C C   . SER B 27  ? 0.7527 0.7261 0.4462 -0.1149 -0.0590 0.1306  53  SER B C   
1757 O O   . SER B 27  ? 0.7657 0.7209 0.4538 -0.1191 -0.0747 0.1394  53  SER B O   
1758 C CB  . SER B 27  ? 0.7891 0.7744 0.4554 -0.1397 -0.0502 0.1475  53  SER B CB  
1759 O OG  . SER B 27  ? 0.8105 0.7902 0.5005 -0.1364 -0.0557 0.1506  53  SER B OG  
1760 N N   . LYS B 28  ? 0.7217 0.7015 0.4376 -0.1016 -0.0535 0.1191  54  LYS B N   
1761 C CA  . LYS B 28  ? 0.7042 0.6718 0.4398 -0.0914 -0.0641 0.1159  54  LYS B CA  
1762 C C   . LYS B 28  ? 0.6751 0.6471 0.4159 -0.0807 -0.0599 0.1034  54  LYS B C   
1763 O O   . LYS B 28  ? 0.6786 0.6649 0.4160 -0.0780 -0.0468 0.0952  54  LYS B O   
1764 C CB  . LYS B 28  ? 0.7250 0.6935 0.4856 -0.0865 -0.0634 0.1155  54  LYS B CB  
1765 C CG  . LYS B 28  ? 0.7943 0.7527 0.5541 -0.0955 -0.0722 0.1278  54  LYS B CG  
1766 C CD  . LYS B 28  ? 0.8592 0.8177 0.6434 -0.0896 -0.0715 0.1255  54  LYS B CD  
1767 C CE  . LYS B 28  ? 0.9204 0.8675 0.7044 -0.0981 -0.0807 0.1371  54  LYS B CE  
1768 N NZ  . LYS B 28  ? 0.9465 0.8929 0.7530 -0.0920 -0.0801 0.1337  54  LYS B NZ  
1769 N N   . THR B 29  ? 0.6406 0.6006 0.3914 -0.0745 -0.0715 0.1020  55  THR B N   
1770 C CA  . THR B 29  ? 0.6028 0.5651 0.3612 -0.0648 -0.0696 0.0912  55  THR B CA  
1771 C C   . THR B 29  ? 0.5410 0.5134 0.3231 -0.0554 -0.0600 0.0828  55  THR B C   
1772 O O   . THR B 29  ? 0.5375 0.5115 0.3316 -0.0560 -0.0584 0.0860  55  THR B O   
1773 C CB  . THR B 29  ? 0.6288 0.5763 0.3924 -0.0624 -0.0854 0.0937  55  THR B CB  
1774 O OG1 . THR B 29  ? 0.6490 0.5985 0.4172 -0.0550 -0.0845 0.0842  55  THR B OG1 
1775 C CG2 . THR B 29  ? 0.6267 0.5674 0.4137 -0.0585 -0.0932 0.0969  55  THR B CG2 
1776 N N   . TRP B 30  ? 0.4954 0.4737 0.2831 -0.0475 -0.0542 0.0723  56  TRP B N   
1777 C CA  . TRP B 30  ? 0.4533 0.4405 0.2605 -0.0396 -0.0454 0.0647  56  TRP B CA  
1778 C C   . TRP B 30  ? 0.4157 0.3980 0.2448 -0.0362 -0.0503 0.0671  56  TRP B C   
1779 O O   . TRP B 30  ? 0.4066 0.3943 0.2427 -0.0369 -0.0446 0.0683  56  TRP B O   
1780 C CB  . TRP B 30  ? 0.4437 0.4337 0.2543 -0.0319 -0.0420 0.0542  56  TRP B CB  
1781 C CG  . TRP B 30  ? 0.4297 0.4295 0.2549 -0.0254 -0.0319 0.0469  56  TRP B CG  
1782 C CD1 . TRP B 30  ? 0.4365 0.4479 0.2573 -0.0246 -0.0207 0.0420  56  TRP B CD1 
1783 C CD2 . TRP B 30  ? 0.4157 0.4146 0.2622 -0.0193 -0.0326 0.0440  56  TRP B CD2 
1784 N NE1 . TRP B 30  ? 0.4323 0.4489 0.2704 -0.0186 -0.0156 0.0371  56  TRP B NE1 
1785 C CE2 . TRP B 30  ? 0.4225 0.4312 0.2751 -0.0155 -0.0224 0.0381  56  TRP B CE2 
1786 C CE3 . TRP B 30  ? 0.4123 0.4034 0.2733 -0.0166 -0.0407 0.0455  56  TRP B CE3 
1787 C CZ2 . TRP B 30  ? 0.4156 0.4253 0.2860 -0.0103 -0.0205 0.0348  56  TRP B CZ2 
1788 C CZ3 . TRP B 30  ? 0.4124 0.4061 0.2914 -0.0111 -0.0374 0.0412  56  TRP B CZ3 
1789 C CH2 . TRP B 30  ? 0.4075 0.4097 0.2897 -0.0084 -0.0277 0.0363  56  TRP B CH2 
1790 N N   . GLN B 31  ? 0.3951 0.3675 0.2347 -0.0328 -0.0608 0.0678  57  GLN B N   
1791 C CA  . GLN B 31  ? 0.3783 0.3466 0.2390 -0.0285 -0.0648 0.0683  57  GLN B CA  
1792 C C   . GLN B 31  ? 0.3630 0.3268 0.2239 -0.0338 -0.0679 0.0763  57  GLN B C   
1793 O O   . GLN B 31  ? 0.3458 0.3106 0.2209 -0.0308 -0.0652 0.0748  57  GLN B O   
1794 C CB  . GLN B 31  ? 0.3943 0.3542 0.2662 -0.0245 -0.0760 0.0677  57  GLN B CB  
1795 C CG  . GLN B 31  ? 0.4302 0.3950 0.3079 -0.0186 -0.0729 0.0592  57  GLN B CG  
1796 C CD  . GLN B 31  ? 0.4620 0.4218 0.3571 -0.0140 -0.0822 0.0580  57  GLN B CD  
1797 O OE1 . GLN B 31  ? 0.4655 0.4219 0.3759 -0.0117 -0.0864 0.0596  57  GLN B OE1 
1798 N NE2 . GLN B 31  ? 0.4697 0.4294 0.3637 -0.0126 -0.0854 0.0546  57  GLN B NE2 
1799 N N   . ALA B 32  ? 0.3621 0.3201 0.2055 -0.0425 -0.0736 0.0850  58  ALA B N   
1800 C CA  . ALA B 32  ? 0.3702 0.3224 0.2109 -0.0494 -0.0778 0.0941  58  ALA B CA  
1801 C C   . ALA B 32  ? 0.3762 0.3394 0.2178 -0.0519 -0.0661 0.0936  58  ALA B C   
1802 O O   . ALA B 32  ? 0.3816 0.3403 0.2241 -0.0572 -0.0693 0.1005  58  ALA B O   
1803 C CB  . ALA B 32  ? 0.3824 0.3268 0.2011 -0.0595 -0.0858 0.1039  58  ALA B CB  
1804 N N   . ASN B 33  ? 0.3753 0.3523 0.2180 -0.0480 -0.0536 0.0855  59  ASN B N   
1805 C CA  . ASN B 33  ? 0.3769 0.3654 0.2228 -0.0497 -0.0431 0.0846  59  ASN B CA  
1806 C C   . ASN B 33  ? 0.3629 0.3538 0.2292 -0.0416 -0.0395 0.0778  59  ASN B C   
1807 O O   . ASN B 33  ? 0.3655 0.3648 0.2364 -0.0426 -0.0323 0.0770  59  ASN B O   
1808 C CB  . ASN B 33  ? 0.3984 0.4013 0.2314 -0.0518 -0.0319 0.0809  59  ASN B CB  
1809 C CG  . ASN B 33  ? 0.4663 0.4680 0.2771 -0.0618 -0.0339 0.0885  59  ASN B CG  
1810 O OD1 . ASN B 33  ? 0.4742 0.4693 0.2793 -0.0704 -0.0401 0.0985  59  ASN B OD1 
1811 N ND2 . ASN B 33  ? 0.4942 0.5013 0.2910 -0.0615 -0.0294 0.0839  59  ASN B ND2 
1812 N N   . LEU B 34  ? 0.3456 0.3294 0.2237 -0.0341 -0.0446 0.0730  60  LEU B N   
1813 C CA  . LEU B 34  ? 0.3322 0.3171 0.2277 -0.0270 -0.0416 0.0666  60  LEU B CA  
1814 C C   . LEU B 34  ? 0.3143 0.2903 0.2180 -0.0286 -0.0476 0.0712  60  LEU B C   
1815 O O   . LEU B 34  ? 0.3157 0.2809 0.2172 -0.0317 -0.0576 0.0775  60  LEU B O   
1816 C CB  . LEU B 34  ? 0.3424 0.3242 0.2471 -0.0195 -0.0446 0.0603  60  LEU B CB  
1817 C CG  . LEU B 34  ? 0.3666 0.3563 0.2678 -0.0158 -0.0381 0.0533  60  LEU B CG  
1818 C CD1 . LEU B 34  ? 0.3712 0.3569 0.2819 -0.0103 -0.0427 0.0488  60  LEU B CD1 
1819 C CD2 . LEU B 34  ? 0.3719 0.3713 0.2777 -0.0132 -0.0279 0.0479  60  LEU B CD2 
1820 N N   . ARG B 35  ? 0.2920 0.2718 0.2046 -0.0268 -0.0423 0.0682  61  ARG B N   
1821 C CA  . ARG B 35  ? 0.2925 0.2636 0.2123 -0.0283 -0.0473 0.0714  61  ARG B CA  
1822 C C   . ARG B 35  ? 0.2872 0.2590 0.2206 -0.0211 -0.0435 0.0633  61  ARG B C   
1823 O O   . ARG B 35  ? 0.2627 0.2442 0.1971 -0.0194 -0.0350 0.0587  61  ARG B O   
1824 C CB  . ARG B 35  ? 0.2989 0.2749 0.2119 -0.0366 -0.0442 0.0777  61  ARG B CB  
1825 C CG  . ARG B 35  ? 0.3486 0.3230 0.2468 -0.0461 -0.0482 0.0874  61  ARG B CG  
1826 C CD  . ARG B 35  ? 0.3820 0.3391 0.2797 -0.0481 -0.0617 0.0937  61  ARG B CD  
1827 N NE  . ARG B 35  ? 0.4401 0.3940 0.3217 -0.0585 -0.0665 0.1041  61  ARG B NE  
1828 C CZ  . ARG B 35  ? 0.4721 0.4265 0.3412 -0.0607 -0.0683 0.1062  61  ARG B CZ  
1829 N NH1 . ARG B 35  ? 0.4486 0.4066 0.3204 -0.0530 -0.0659 0.0985  61  ARG B NH1 
1830 N NH2 . ARG B 35  ? 0.4935 0.4441 0.3461 -0.0713 -0.0729 0.1164  61  ARG B NH2 
1831 N N   . LEU B 36  ? 0.3029 0.2645 0.2464 -0.0171 -0.0497 0.0613  62  LEU B N   
1832 C CA  . LEU B 36  ? 0.3130 0.2746 0.2678 -0.0110 -0.0460 0.0536  62  LEU B CA  
1833 C C   . LEU B 36  ? 0.3199 0.2764 0.2753 -0.0147 -0.0472 0.0563  62  LEU B C   
1834 O O   . LEU B 36  ? 0.3317 0.2771 0.2875 -0.0173 -0.0556 0.0611  62  LEU B O   
1835 C CB  . LEU B 36  ? 0.3213 0.2756 0.2875 -0.0045 -0.0517 0.0492  62  LEU B CB  
1836 C CG  . LEU B 36  ? 0.3510 0.3042 0.3284 0.0014  -0.0481 0.0409  62  LEU B CG  
1837 C CD1 . LEU B 36  ? 0.3552 0.3190 0.3314 0.0029  -0.0380 0.0355  62  LEU B CD1 
1838 C CD2 . LEU B 36  ? 0.3582 0.3073 0.3483 0.0079  -0.0529 0.0361  62  LEU B CD2 
1839 N N   . ILE B 37  ? 0.3247 0.2885 0.2797 -0.0155 -0.0400 0.0538  63  ILE B N   
1840 C CA  . ILE B 37  ? 0.3433 0.3035 0.2985 -0.0197 -0.0410 0.0564  63  ILE B CA  
1841 C C   . ILE B 37  ? 0.3536 0.3036 0.3169 -0.0150 -0.0436 0.0506  63  ILE B C   
1842 O O   . ILE B 37  ? 0.3618 0.2999 0.3265 -0.0171 -0.0510 0.0535  63  ILE B O   
1843 C CB  . ILE B 37  ? 0.3585 0.3317 0.3105 -0.0227 -0.0328 0.0565  63  ILE B CB  
1844 C CG1 . ILE B 37  ? 0.3752 0.3598 0.3194 -0.0262 -0.0289 0.0603  63  ILE B CG1 
1845 C CG2 . ILE B 37  ? 0.3715 0.3421 0.3242 -0.0284 -0.0348 0.0604  63  ILE B CG2 
1846 C CD1 . ILE B 37  ? 0.4037 0.3843 0.3402 -0.0335 -0.0347 0.0694  63  ILE B CD1 
1847 N N   . SER B 38  ? 0.3397 0.2938 0.3076 -0.0091 -0.0376 0.0423  64  SER B N   
1848 C CA  . SER B 38  ? 0.3453 0.2911 0.3193 -0.0048 -0.0385 0.0356  64  SER B CA  
1849 C C   . SER B 38  ? 0.3231 0.2753 0.3009 0.0010  -0.0314 0.0273  64  SER B C   
1850 O O   . SER B 38  ? 0.3127 0.2748 0.2878 0.0010  -0.0260 0.0269  64  SER B O   
1851 C CB  . SER B 38  ? 0.3867 0.3281 0.3581 -0.0088 -0.0392 0.0367  64  SER B CB  
1852 O OG  . SER B 38  ? 0.4309 0.3825 0.3992 -0.0104 -0.0322 0.0356  64  SER B OG  
1853 N N   . LYS B 39  ? 0.3104 0.2564 0.2940 0.0055  -0.0315 0.0203  65  LYS B N   
1854 C CA  . LYS B 39  ? 0.3042 0.2556 0.2908 0.0098  -0.0245 0.0124  65  LYS B CA  
1855 C C   . LYS B 39  ? 0.2943 0.2417 0.2773 0.0092  -0.0214 0.0078  65  LYS B C   
1856 O O   . LYS B 39  ? 0.3068 0.2454 0.2876 0.0069  -0.0259 0.0094  65  LYS B O   
1857 C CB  . LYS B 39  ? 0.3300 0.2799 0.3270 0.0158  -0.0261 0.0073  65  LYS B CB  
1858 C CG  . LYS B 39  ? 0.3799 0.3326 0.3799 0.0161  -0.0307 0.0122  65  LYS B CG  
1859 C CD  . LYS B 39  ? 0.4303 0.3836 0.4430 0.0222  -0.0323 0.0069  65  LYS B CD  
1860 C CE  . LYS B 39  ? 0.4752 0.4301 0.4901 0.0220  -0.0382 0.0121  65  LYS B CE  
1861 N NZ  . LYS B 39  ? 0.4960 0.4522 0.5258 0.0281  -0.0409 0.0071  65  LYS B NZ  
1862 N N   . PHE B 40  ? 0.2698 0.2228 0.2514 0.0106  -0.0144 0.0023  66  PHE B N   
1863 C CA  . PHE B 40  ? 0.2586 0.2077 0.2347 0.0096  -0.0113 -0.0023 66  PHE B CA  
1864 C C   . PHE B 40  ? 0.2574 0.2125 0.2335 0.0118  -0.0039 -0.0087 66  PHE B C   
1865 O O   . PHE B 40  ? 0.2564 0.2200 0.2352 0.0125  -0.0011 -0.0078 66  PHE B O   
1866 C CB  . PHE B 40  ? 0.2515 0.2016 0.2197 0.0041  -0.0119 0.0029  66  PHE B CB  
1867 C CG  . PHE B 40  ? 0.2504 0.2111 0.2164 0.0028  -0.0082 0.0059  66  PHE B CG  
1868 C CD1 . PHE B 40  ? 0.2623 0.2263 0.2243 0.0028  -0.0033 0.0024  66  PHE B CD1 
1869 C CD2 . PHE B 40  ? 0.2469 0.2135 0.2140 0.0014  -0.0099 0.0120  66  PHE B CD2 
1870 C CE1 . PHE B 40  ? 0.2641 0.2362 0.2247 0.0023  -0.0010 0.0046  66  PHE B CE1 
1871 C CE2 . PHE B 40  ? 0.2520 0.2278 0.2173 0.0010  -0.0066 0.0135  66  PHE B CE2 
1872 C CZ  . PHE B 40  ? 0.2543 0.2323 0.2170 0.0018  -0.0026 0.0097  66  PHE B CZ  
1873 N N   . ASP B 41  ? 0.2505 0.2011 0.2231 0.0122  -0.0007 -0.0153 67  ASP B N   
1874 C CA  . ASP B 41  ? 0.2440 0.2001 0.2148 0.0128  0.0068  -0.0210 67  ASP B CA  
1875 C C   . ASP B 41  ? 0.2344 0.1853 0.1933 0.0093  0.0096  -0.0243 67  ASP B C   
1876 O O   . ASP B 41  ? 0.2259 0.1790 0.1817 0.0093  0.0158  -0.0303 67  ASP B O   
1877 C CB  . ASP B 41  ? 0.2745 0.2338 0.2563 0.0180  0.0097  -0.0279 67  ASP B CB  
1878 C CG  . ASP B 41  ? 0.3815 0.3316 0.3675 0.0219  0.0067  -0.0334 67  ASP B CG  
1879 O OD1 . ASP B 41  ? 0.3952 0.3352 0.3737 0.0197  0.0026  -0.0322 67  ASP B OD1 
1880 O OD2 . ASP B 41  ? 0.4286 0.3816 0.4263 0.0272  0.0079  -0.0391 67  ASP B OD2 
1881 N N   . THR B 42  ? 0.2312 0.1759 0.1830 0.0057  0.0050  -0.0200 68  THR B N   
1882 C CA  . THR B 42  ? 0.2455 0.1845 0.1851 0.0018  0.0058  -0.0218 68  THR B CA  
1883 C C   . THR B 42  ? 0.2444 0.1856 0.1799 -0.0026 0.0023  -0.0142 68  THR B C   
1884 O O   . THR B 42  ? 0.2421 0.1875 0.1837 -0.0025 -0.0011 -0.0083 68  THR B O   
1885 C CB  . THR B 42  ? 0.2783 0.2051 0.2139 0.0019  0.0025  -0.0262 68  THR B CB  
1886 O OG1 . THR B 42  ? 0.2975 0.2197 0.2355 0.0000  -0.0053 -0.0197 68  THR B OG1 
1887 C CG2 . THR B 42  ? 0.2822 0.2067 0.2243 0.0075  0.0053  -0.0346 68  THR B CG2 
1888 N N   . VAL B 43  ? 0.2462 0.1845 0.1713 -0.0064 0.0028  -0.0147 69  VAL B N   
1889 C CA  . VAL B 43  ? 0.2595 0.1993 0.1815 -0.0100 -0.0011 -0.0086 69  VAL B CA  
1890 C C   . VAL B 43  ? 0.2637 0.1995 0.1886 -0.0118 -0.0078 -0.0045 69  VAL B C   
1891 O O   . VAL B 43  ? 0.2673 0.2097 0.1979 -0.0128 -0.0104 0.0016  69  VAL B O   
1892 C CB  . VAL B 43  ? 0.2847 0.2186 0.1933 -0.0141 -0.0005 -0.0108 69  VAL B CB  
1893 C CG1 . VAL B 43  ? 0.2901 0.2229 0.1961 -0.0178 -0.0068 -0.0052 69  VAL B CG1 
1894 C CG2 . VAL B 43  ? 0.2944 0.2330 0.1997 -0.0140 0.0054  -0.0129 69  VAL B CG2 
1895 N N   . GLU B 44  ? 0.2623 0.1874 0.1830 -0.0126 -0.0103 -0.0080 70  GLU B N   
1896 C CA  . GLU B 44  ? 0.2690 0.1887 0.1918 -0.0154 -0.0175 -0.0040 70  GLU B CA  
1897 C C   . GLU B 44  ? 0.2596 0.1846 0.1934 -0.0139 -0.0194 0.0010  70  GLU B C   
1898 O O   . GLU B 44  ? 0.2614 0.1890 0.1987 -0.0174 -0.0239 0.0076  70  GLU B O   
1899 C CB  . GLU B 44  ? 0.3029 0.2079 0.2183 -0.0160 -0.0203 -0.0098 70  GLU B CB  
1900 C CG  . GLU B 44  ? 0.3597 0.2575 0.2610 -0.0193 -0.0199 -0.0140 70  GLU B CG  
1901 C CD  . GLU B 44  ? 0.4268 0.3255 0.3210 -0.0170 -0.0118 -0.0213 70  GLU B CD  
1902 O OE1 . GLU B 44  ? 0.4726 0.3647 0.3530 -0.0204 -0.0112 -0.0247 70  GLU B OE1 
1903 O OE2 . GLU B 44  ? 0.4185 0.3248 0.3205 -0.0125 -0.0062 -0.0233 70  GLU B OE2 
1904 N N   . ASP B 45  ? 0.2529 0.1797 0.1920 -0.0092 -0.0162 -0.0018 71  ASP B N   
1905 C CA  . ASP B 45  ? 0.2570 0.1876 0.2046 -0.0082 -0.0187 0.0034  71  ASP B CA  
1906 C C   . ASP B 45  ? 0.2456 0.1895 0.1966 -0.0090 -0.0163 0.0089  71  ASP B C   
1907 O O   . ASP B 45  ? 0.2538 0.2018 0.2088 -0.0111 -0.0191 0.0151  71  ASP B O   
1908 C CB  . ASP B 45  ? 0.2905 0.2180 0.2437 -0.0029 -0.0179 -0.0011 71  ASP B CB  
1909 C CG  . ASP B 45  ? 0.4064 0.3200 0.3581 -0.0014 -0.0214 -0.0068 71  ASP B CG  
1910 O OD1 . ASP B 45  ? 0.4288 0.3339 0.3774 -0.0053 -0.0277 -0.0038 71  ASP B OD1 
1911 O OD2 . ASP B 45  ? 0.4514 0.3632 0.4056 0.0038  -0.0179 -0.0146 71  ASP B OD2 
1912 N N   . PHE B 46  ? 0.2341 0.1843 0.1826 -0.0078 -0.0114 0.0067  72  PHE B N   
1913 C CA  . PHE B 46  ? 0.2213 0.1829 0.1726 -0.0079 -0.0096 0.0109  72  PHE B CA  
1914 C C   . PHE B 46  ? 0.2214 0.1862 0.1733 -0.0122 -0.0131 0.0161  72  PHE B C   
1915 O O   . PHE B 46  ? 0.2196 0.1927 0.1763 -0.0133 -0.0135 0.0210  72  PHE B O   
1916 C CB  . PHE B 46  ? 0.2126 0.1776 0.1604 -0.0063 -0.0052 0.0074  72  PHE B CB  
1917 C CG  . PHE B 46  ? 0.2073 0.1817 0.1573 -0.0065 -0.0048 0.0110  72  PHE B CG  
1918 C CD1 . PHE B 46  ? 0.2101 0.1924 0.1648 -0.0044 -0.0034 0.0132  72  PHE B CD1 
1919 C CD2 . PHE B 46  ? 0.2208 0.1956 0.1682 -0.0086 -0.0066 0.0120  72  PHE B CD2 
1920 C CE1 . PHE B 46  ? 0.2200 0.2110 0.1769 -0.0040 -0.0028 0.0153  72  PHE B CE1 
1921 C CE2 . PHE B 46  ? 0.2294 0.2130 0.1808 -0.0077 -0.0067 0.0144  72  PHE B CE2 
1922 C CZ  . PHE B 46  ? 0.2194 0.2113 0.1756 -0.0052 -0.0044 0.0156  72  PHE B CZ  
1923 N N   . TRP B 47  ? 0.2200 0.1789 0.1670 -0.0149 -0.0155 0.0148  73  TRP B N   
1924 C CA  . TRP B 47  ? 0.2221 0.1851 0.1715 -0.0189 -0.0193 0.0196  73  TRP B CA  
1925 C C   . TRP B 47  ? 0.2320 0.1946 0.1859 -0.0227 -0.0235 0.0246  73  TRP B C   
1926 O O   . TRP B 47  ? 0.2345 0.2069 0.1943 -0.0256 -0.0246 0.0298  73  TRP B O   
1927 C CB  . TRP B 47  ? 0.2236 0.1793 0.1660 -0.0214 -0.0223 0.0174  73  TRP B CB  
1928 C CG  . TRP B 47  ? 0.2291 0.1875 0.1680 -0.0193 -0.0195 0.0151  73  TRP B CG  
1929 C CD1 . TRP B 47  ? 0.2484 0.1995 0.1779 -0.0185 -0.0169 0.0101  73  TRP B CD1 
1930 C CD2 . TRP B 47  ? 0.2234 0.1920 0.1678 -0.0183 -0.0194 0.0177  73  TRP B CD2 
1931 N NE1 . TRP B 47  ? 0.2503 0.2053 0.1785 -0.0177 -0.0160 0.0104  73  TRP B NE1 
1932 C CE2 . TRP B 47  ? 0.2370 0.2024 0.1748 -0.0168 -0.0177 0.0146  73  TRP B CE2 
1933 C CE3 . TRP B 47  ? 0.2217 0.2026 0.1765 -0.0181 -0.0200 0.0219  73  TRP B CE3 
1934 C CZ2 . TRP B 47  ? 0.2422 0.2139 0.1834 -0.0149 -0.0182 0.0157  73  TRP B CZ2 
1935 C CZ3 . TRP B 47  ? 0.2330 0.2218 0.1919 -0.0153 -0.0193 0.0219  73  TRP B CZ3 
1936 C CH2 . TRP B 47  ? 0.2385 0.2217 0.1907 -0.0137 -0.0191 0.0189  73  TRP B CH2 
1937 N N   . ALA B 48  ? 0.2353 0.1869 0.1868 -0.0228 -0.0259 0.0230  74  ALA B N   
1938 C CA  . ALA B 48  ? 0.2401 0.1889 0.1949 -0.0271 -0.0311 0.0286  74  ALA B CA  
1939 C C   . ALA B 48  ? 0.2263 0.1860 0.1867 -0.0274 -0.0290 0.0339  74  ALA B C   
1940 O O   . ALA B 48  ? 0.2254 0.1913 0.1895 -0.0327 -0.0313 0.0405  74  ALA B O   
1941 C CB  . ALA B 48  ? 0.2515 0.1844 0.2028 -0.0261 -0.0350 0.0250  74  ALA B CB  
1942 N N   . LEU B 49  ? 0.2193 0.1820 0.1797 -0.0224 -0.0247 0.0312  75  LEU B N   
1943 C CA  . LEU B 49  ? 0.2271 0.1993 0.1905 -0.0225 -0.0227 0.0357  75  LEU B CA  
1944 C C   . LEU B 49  ? 0.2411 0.2289 0.2074 -0.0235 -0.0186 0.0380  75  LEU B C   
1945 O O   . LEU B 49  ? 0.2515 0.2481 0.2204 -0.0275 -0.0184 0.0437  75  LEU B O   
1946 C CB  . LEU B 49  ? 0.2382 0.2088 0.2010 -0.0167 -0.0198 0.0314  75  LEU B CB  
1947 C CG  . LEU B 49  ? 0.2712 0.2494 0.2348 -0.0166 -0.0184 0.0352  75  LEU B CG  
1948 C CD1 . LEU B 49  ? 0.2882 0.2615 0.2515 -0.0215 -0.0241 0.0419  75  LEU B CD1 
1949 C CD2 . LEU B 49  ? 0.2816 0.2587 0.2455 -0.0108 -0.0162 0.0305  75  LEU B CD2 
1950 N N   . TYR B 50  ? 0.2328 0.2238 0.1987 -0.0200 -0.0155 0.0335  76  TYR B N   
1951 C CA  . TYR B 50  ? 0.2282 0.2328 0.1984 -0.0196 -0.0125 0.0343  76  TYR B CA  
1952 C C   . TYR B 50  ? 0.2315 0.2427 0.2072 -0.0252 -0.0152 0.0394  76  TYR B C   
1953 O O   . TYR B 50  ? 0.2289 0.2534 0.2096 -0.0268 -0.0126 0.0427  76  TYR B O   
1954 C CB  . TYR B 50  ? 0.2261 0.2292 0.1945 -0.0157 -0.0112 0.0292  76  TYR B CB  
1955 C CG  . TYR B 50  ? 0.2314 0.2474 0.2056 -0.0143 -0.0093 0.0295  76  TYR B CG  
1956 C CD1 . TYR B 50  ? 0.2375 0.2626 0.2132 -0.0108 -0.0049 0.0286  76  TYR B CD1 
1957 C CD2 . TYR B 50  ? 0.2367 0.2557 0.2154 -0.0162 -0.0124 0.0306  76  TYR B CD2 
1958 C CE1 . TYR B 50  ? 0.2443 0.2813 0.2263 -0.0087 -0.0031 0.0279  76  TYR B CE1 
1959 C CE2 . TYR B 50  ? 0.2481 0.2800 0.2348 -0.0142 -0.0111 0.0306  76  TYR B CE2 
1960 C CZ  . TYR B 50  ? 0.2595 0.3005 0.2480 -0.0100 -0.0061 0.0288  76  TYR B CZ  
1961 O OH  . TYR B 50  ? 0.2774 0.3311 0.2743 -0.0070 -0.0046 0.0274  76  TYR B OH  
1962 N N   . ASN B 51  ? 0.2413 0.2436 0.2160 -0.0285 -0.0203 0.0398  77  ASN B N   
1963 C CA  . ASN B 51  ? 0.2572 0.2655 0.2382 -0.0347 -0.0239 0.0450  77  ASN B CA  
1964 C C   . ASN B 51  ? 0.2780 0.2902 0.2613 -0.0405 -0.0248 0.0516  77  ASN B C   
1965 O O   . ASN B 51  ? 0.2705 0.2961 0.2614 -0.0451 -0.0242 0.0564  77  ASN B O   
1966 C CB  . ASN B 51  ? 0.2706 0.2663 0.2484 -0.0375 -0.0303 0.0439  77  ASN B CB  
1967 C CG  . ASN B 51  ? 0.2885 0.2822 0.2640 -0.0342 -0.0305 0.0393  77  ASN B CG  
1968 O OD1 . ASN B 51  ? 0.2979 0.2777 0.2651 -0.0341 -0.0335 0.0356  77  ASN B OD1 
1969 N ND2 . ASN B 51  ? 0.2734 0.2805 0.2557 -0.0314 -0.0275 0.0391  77  ASN B ND2 
1970 N N   . HIS B 52  ? 0.3032 0.3042 0.2806 -0.0406 -0.0265 0.0521  78  HIS B N   
1971 C CA  . HIS B 52  ? 0.3305 0.3324 0.3081 -0.0467 -0.0285 0.0591  78  HIS B CA  
1972 C C   . HIS B 52  ? 0.3474 0.3658 0.3268 -0.0467 -0.0221 0.0618  78  HIS B C   
1973 O O   . HIS B 52  ? 0.3512 0.3805 0.3343 -0.0534 -0.0214 0.0681  78  HIS B O   
1974 C CB  . HIS B 52  ? 0.3505 0.3345 0.3218 -0.0455 -0.0332 0.0583  78  HIS B CB  
1975 C CG  . HIS B 52  ? 0.3735 0.3558 0.3435 -0.0517 -0.0366 0.0660  78  HIS B CG  
1976 N ND1 . HIS B 52  ? 0.3970 0.3786 0.3634 -0.0495 -0.0353 0.0669  78  HIS B ND1 
1977 C CD2 . HIS B 52  ? 0.3823 0.3633 0.3537 -0.0607 -0.0419 0.0736  78  HIS B CD2 
1978 C CE1 . HIS B 52  ? 0.4007 0.3797 0.3653 -0.0572 -0.0400 0.0751  78  HIS B CE1 
1979 N NE2 . HIS B 52  ? 0.3966 0.3753 0.3642 -0.0644 -0.0438 0.0795  78  HIS B NE2 
1980 N N   . ILE B 53  ? 0.3603 0.3809 0.3369 -0.0399 -0.0173 0.0569  79  ILE B N   
1981 C CA  . ILE B 53  ? 0.3844 0.4189 0.3606 -0.0392 -0.0112 0.0580  79  ILE B CA  
1982 C C   . ILE B 53  ? 0.3948 0.4480 0.3791 -0.0401 -0.0065 0.0582  79  ILE B C   
1983 O O   . ILE B 53  ? 0.3895 0.4563 0.3751 -0.0441 -0.0025 0.0621  79  ILE B O   
1984 C CB  . ILE B 53  ? 0.4057 0.4368 0.3771 -0.0314 -0.0082 0.0521  79  ILE B CB  
1985 C CG1 . ILE B 53  ? 0.4298 0.4447 0.3960 -0.0303 -0.0129 0.0519  79  ILE B CG1 
1986 C CG2 . ILE B 53  ? 0.4095 0.4538 0.3789 -0.0306 -0.0023 0.0524  79  ILE B CG2 
1987 C CD1 . ILE B 53  ? 0.4527 0.4639 0.4153 -0.0363 -0.0167 0.0589  79  ILE B CD1 
1988 N N   . GLN B 54  ? 0.4014 0.4555 0.3915 -0.0369 -0.0073 0.0542  80  GLN B N   
1989 C CA  . GLN B 54  ? 0.4111 0.4824 0.4116 -0.0366 -0.0042 0.0536  80  GLN B CA  
1990 C C   . GLN B 54  ? 0.4397 0.5216 0.4477 -0.0454 -0.0053 0.0606  80  GLN B C   
1991 O O   . GLN B 54  ? 0.4396 0.5406 0.4570 -0.0460 -0.0006 0.0610  80  GLN B O   
1992 C CB  . GLN B 54  ? 0.4088 0.4756 0.4130 -0.0320 -0.0071 0.0487  80  GLN B CB  
1993 C CG  . GLN B 54  ? 0.4148 0.4769 0.4143 -0.0238 -0.0047 0.0420  80  GLN B CG  
1994 C CD  . GLN B 54  ? 0.4420 0.5184 0.4446 -0.0194 0.0017  0.0393  80  GLN B CD  
1995 O OE1 . GLN B 54  ? 0.4639 0.5391 0.4595 -0.0177 0.0051  0.0383  80  GLN B OE1 
1996 N NE2 . GLN B 54  ? 0.4292 0.5190 0.4424 -0.0173 0.0031  0.0376  80  GLN B NE2 
1997 N N   . LEU B 55  ? 0.4612 0.5312 0.4659 -0.0520 -0.0116 0.0657  81  LEU B N   
1998 C CA  . LEU B 55  ? 0.4809 0.5591 0.4919 -0.0618 -0.0138 0.0734  81  LEU B CA  
1999 C C   . LEU B 55  ? 0.5118 0.5893 0.5159 -0.0690 -0.0133 0.0804  81  LEU B C   
2000 O O   . LEU B 55  ? 0.5181 0.5967 0.5247 -0.0786 -0.0171 0.0879  81  LEU B O   
2001 C CB  . LEU B 55  ? 0.4845 0.5495 0.4972 -0.0657 -0.0227 0.0750  81  LEU B CB  
2002 C CG  . LEU B 55  ? 0.5028 0.5699 0.5226 -0.0614 -0.0246 0.0701  81  LEU B CG  
2003 C CD1 . LEU B 55  ? 0.5174 0.5687 0.5353 -0.0658 -0.0341 0.0716  81  LEU B CD1 
2004 C CD2 . LEU B 55  ? 0.4972 0.5886 0.5323 -0.0626 -0.0205 0.0714  81  LEU B CD2 
2005 N N   . SER B 56  ? 0.5305 0.6055 0.5255 -0.0651 -0.0095 0.0786  82  SER B N   
2006 C CA  . SER B 56  ? 0.5517 0.6243 0.5381 -0.0718 -0.0099 0.0854  82  SER B CA  
2007 C C   . SER B 56  ? 0.5623 0.6505 0.5452 -0.0699 -0.0010 0.0841  82  SER B C   
2008 O O   . SER B 56  ? 0.5620 0.6690 0.5528 -0.0675 0.0061  0.0807  82  SER B O   
2009 C CB  . SER B 56  ? 0.5807 0.6301 0.5575 -0.0693 -0.0168 0.0849  82  SER B CB  
2010 O OG  . SER B 56  ? 0.6191 0.6531 0.5975 -0.0719 -0.0252 0.0862  82  SER B OG  
2011 N N   . CYS B 63  ? 0.4795 0.5878 0.3832 -0.0452 0.0319  0.0584  89  CYS B N   
2012 C CA  . CYS B 63  ? 0.4819 0.5707 0.3822 -0.0412 0.0233  0.0580  89  CYS B CA  
2013 C C   . CYS B 63  ? 0.4601 0.5452 0.3700 -0.0305 0.0231  0.0489  89  CYS B C   
2014 O O   . CYS B 63  ? 0.4661 0.5581 0.3879 -0.0272 0.0260  0.0455  89  CYS B O   
2015 C CB  . CYS B 63  ? 0.5002 0.5756 0.4027 -0.0467 0.0145  0.0664  89  CYS B CB  
2016 N N   . ASP B 64  ? 0.4377 0.5118 0.3424 -0.0256 0.0192  0.0454  90  ASP B N   
2017 C CA  . ASP B 64  ? 0.4071 0.4763 0.3196 -0.0168 0.0183  0.0378  90  ASP B CA  
2018 C C   . ASP B 64  ? 0.3892 0.4453 0.3095 -0.0159 0.0115  0.0398  90  ASP B C   
2019 O O   . ASP B 64  ? 0.3832 0.4311 0.3008 -0.0206 0.0061  0.0461  90  ASP B O   
2020 C CB  . ASP B 64  ? 0.4096 0.4750 0.3132 -0.0125 0.0179  0.0326  90  ASP B CB  
2021 C CG  . ASP B 64  ? 0.4424 0.5201 0.3391 -0.0112 0.0252  0.0276  90  ASP B CG  
2022 O OD1 . ASP B 64  ? 0.4292 0.5206 0.3313 -0.0120 0.0317  0.0267  90  ASP B OD1 
2023 O OD2 . ASP B 64  ? 0.4695 0.5434 0.3560 -0.0090 0.0245  0.0239  90  ASP B OD2 
2024 N N   . TYR B 65  ? 0.3699 0.4224 0.2996 -0.0108 0.0109  0.0355  91  TYR B N   
2025 C CA  . TYR B 65  ? 0.3704 0.4125 0.3075 -0.0090 0.0065  0.0351  91  TYR B CA  
2026 C C   . TYR B 65  ? 0.3162 0.3517 0.2543 -0.0029 0.0052  0.0292  91  TYR B C   
2027 O O   . TYR B 65  ? 0.2941 0.3337 0.2299 0.0006  0.0079  0.0246  91  TYR B O   
2028 C CB  . TYR B 65  ? 0.4064 0.4528 0.3523 -0.0087 0.0085  0.0341  91  TYR B CB  
2029 C CG  . TYR B 65  ? 0.4559 0.5084 0.4036 -0.0151 0.0090  0.0401  91  TYR B CG  
2030 C CD1 . TYR B 65  ? 0.4857 0.5294 0.4348 -0.0195 0.0039  0.0451  91  TYR B CD1 
2031 C CD2 . TYR B 65  ? 0.4818 0.5491 0.4295 -0.0174 0.0144  0.0408  91  TYR B CD2 
2032 C CE1 . TYR B 65  ? 0.5068 0.5555 0.4578 -0.0263 0.0035  0.0511  91  TYR B CE1 
2033 C CE2 . TYR B 65  ? 0.5024 0.5770 0.4530 -0.0243 0.0151  0.0467  91  TYR B CE2 
2034 C CZ  . TYR B 65  ? 0.5222 0.5870 0.4743 -0.0292 0.0093  0.0523  91  TYR B CZ  
2035 O OH  . TYR B 65  ? 0.5616 0.6326 0.5163 -0.0370 0.0091  0.0588  91  TYR B OH  
2036 N N   . SER B 66  ? 0.2916 0.3179 0.2338 -0.0020 0.0013  0.0293  92  SER B N   
2037 C CA  . SER B 66  ? 0.2769 0.2972 0.2218 0.0023  -0.0002 0.0247  92  SER B CA  
2038 C C   . SER B 66  ? 0.2394 0.2533 0.1911 0.0029  -0.0017 0.0238  92  SER B C   
2039 O O   . SER B 66  ? 0.2460 0.2554 0.1993 0.0004  -0.0047 0.0273  92  SER B O   
2040 C CB  . SER B 66  ? 0.3113 0.3265 0.2535 0.0019  -0.0048 0.0265  92  SER B CB  
2041 O OG  . SER B 66  ? 0.3985 0.4164 0.3342 0.0032  -0.0041 0.0245  92  SER B OG  
2042 N N   . LEU B 67  ? 0.2011 0.2132 0.1560 0.0060  -0.0003 0.0190  93  LEU B N   
2043 C CA  . LEU B 67  ? 0.1926 0.1987 0.1524 0.0065  -0.0009 0.0172  93  LEU B CA  
2044 C C   . LEU B 67  ? 0.1850 0.1893 0.1475 0.0091  -0.0012 0.0136  93  LEU B C   
2045 O O   . LEU B 67  ? 0.1787 0.1849 0.1398 0.0103  0.0007  0.0109  93  LEU B O   
2046 C CB  . LEU B 67  ? 0.1845 0.1907 0.1448 0.0062  0.0014  0.0153  93  LEU B CB  
2047 C CG  . LEU B 67  ? 0.2087 0.2079 0.1718 0.0060  0.0008  0.0134  93  LEU B CG  
2048 C CD1 . LEU B 67  ? 0.2160 0.2113 0.1801 0.0036  -0.0023 0.0168  93  LEU B CD1 
2049 C CD2 . LEU B 67  ? 0.2183 0.2160 0.1796 0.0056  0.0028  0.0106  93  LEU B CD2 
2050 N N   . PHE B 68  ? 0.1734 0.1740 0.1407 0.0098  -0.0041 0.0137  94  PHE B N   
2051 C CA  . PHE B 68  ? 0.1704 0.1714 0.1426 0.0119  -0.0044 0.0104  94  PHE B CA  
2052 C C   . PHE B 68  ? 0.1717 0.1700 0.1517 0.0131  -0.0036 0.0073  94  PHE B C   
2053 O O   . PHE B 68  ? 0.1825 0.1767 0.1642 0.0130  -0.0051 0.0081  94  PHE B O   
2054 C CB  . PHE B 68  ? 0.1591 0.1600 0.1315 0.0122  -0.0092 0.0129  94  PHE B CB  
2055 C CG  . PHE B 68  ? 0.1564 0.1604 0.1216 0.0119  -0.0089 0.0130  94  PHE B CG  
2056 C CD1 . PHE B 68  ? 0.1793 0.1860 0.1363 0.0105  -0.0070 0.0148  94  PHE B CD1 
2057 C CD2 . PHE B 68  ? 0.1502 0.1550 0.1174 0.0129  -0.0101 0.0107  94  PHE B CD2 
2058 C CE1 . PHE B 68  ? 0.1857 0.1951 0.1360 0.0111  -0.0063 0.0135  94  PHE B CE1 
2059 C CE2 . PHE B 68  ? 0.1573 0.1633 0.1170 0.0129  -0.0102 0.0099  94  PHE B CE2 
2060 C CZ  . PHE B 68  ? 0.1709 0.1790 0.1220 0.0124  -0.0082 0.0109  94  PHE B CZ  
2061 N N   . LYS B 69  ? 0.1728 0.1734 0.1579 0.0142  -0.0015 0.0034  95  LYS B N   
2062 C CA  . LYS B 69  ? 0.1812 0.1815 0.1747 0.0157  0.0003  -0.0007 95  LYS B CA  
2063 C C   . LYS B 69  ? 0.2037 0.2019 0.2058 0.0183  -0.0048 0.0000  95  LYS B C   
2064 O O   . LYS B 69  ? 0.1988 0.1970 0.2014 0.0185  -0.0099 0.0035  95  LYS B O   
2065 C CB  . LYS B 69  ? 0.1906 0.1961 0.1887 0.0154  0.0038  -0.0043 95  LYS B CB  
2066 C CG  . LYS B 69  ? 0.2217 0.2271 0.2118 0.0126  0.0084  -0.0054 95  LYS B CG  
2067 C CD  . LYS B 69  ? 0.2469 0.2568 0.2405 0.0109  0.0112  -0.0078 95  LYS B CD  
2068 C CE  . LYS B 69  ? 0.2661 0.2737 0.2499 0.0074  0.0142  -0.0078 95  LYS B CE  
2069 N NZ  . LYS B 69  ? 0.2657 0.2765 0.2509 0.0045  0.0156  -0.0085 95  LYS B NZ  
2070 N N   . ASP B 70  ? 0.2174 0.2129 0.2258 0.0203  -0.0041 -0.0034 96  ASP B N   
2071 C CA  . ASP B 70  ? 0.2374 0.2294 0.2555 0.0235  -0.0099 -0.0035 96  ASP B CA  
2072 C C   . ASP B 70  ? 0.2421 0.2395 0.2712 0.0258  -0.0129 -0.0042 96  ASP B C   
2073 O O   . ASP B 70  ? 0.2423 0.2470 0.2770 0.0260  -0.0083 -0.0080 96  ASP B O   
2074 C CB  . ASP B 70  ? 0.2615 0.2505 0.2854 0.0262  -0.0072 -0.0095 96  ASP B CB  
2075 C CG  . ASP B 70  ? 0.3281 0.3108 0.3618 0.0301  -0.0144 -0.0099 96  ASP B CG  
2076 O OD1 . ASP B 70  ? 0.3370 0.3139 0.3672 0.0288  -0.0218 -0.0034 96  ASP B OD1 
2077 O OD2 . ASP B 70  ? 0.3599 0.3432 0.4044 0.0345  -0.0126 -0.0167 96  ASP B OD2 
2078 N N   . GLY B 71  ? 0.2492 0.2428 0.2805 0.0265  -0.0211 0.0003  97  GLY B N   
2079 C CA  . GLY B 71  ? 0.2525 0.2503 0.2940 0.0283  -0.0259 0.0004  97  GLY B CA  
2080 C C   . GLY B 71  ? 0.2496 0.2497 0.2819 0.0249  -0.0275 0.0046  97  GLY B C   
2081 O O   . GLY B 71  ? 0.2602 0.2625 0.2988 0.0256  -0.0328 0.0056  97  GLY B O   
2082 N N   . ILE B 72  ? 0.2361 0.2357 0.2540 0.0216  -0.0233 0.0066  98  ILE B N   
2083 C CA  . ILE B 72  ? 0.2282 0.2293 0.2363 0.0190  -0.0243 0.0093  98  ILE B CA  
2084 C C   . ILE B 72  ? 0.2229 0.2193 0.2181 0.0165  -0.0270 0.0147  98  ILE B C   
2085 O O   . ILE B 72  ? 0.2294 0.2248 0.2184 0.0152  -0.0230 0.0154  98  ILE B O   
2086 C CB  . ILE B 72  ? 0.2364 0.2417 0.2394 0.0176  -0.0173 0.0063  98  ILE B CB  
2087 C CG1 . ILE B 72  ? 0.2508 0.2613 0.2651 0.0186  -0.0128 0.0011  98  ILE B CG1 
2088 C CG2 . ILE B 72  ? 0.2366 0.2425 0.2308 0.0159  -0.0194 0.0079  98  ILE B CG2 
2089 C CD1 . ILE B 72  ? 0.2693 0.2825 0.2778 0.0161  -0.0073 -0.0009 98  ILE B CD1 
2090 N N   . GLU B 73  ? 0.2102 0.2039 0.2012 0.0153  -0.0339 0.0189  99  GLU B N   
2091 C CA  . GLU B 73  ? 0.2190 0.2092 0.1962 0.0117  -0.0360 0.0245  99  GLU B CA  
2092 C C   . GLU B 73  ? 0.2184 0.2132 0.1838 0.0101  -0.0307 0.0233  99  GLU B C   
2093 O O   . GLU B 73  ? 0.1977 0.1950 0.1644 0.0113  -0.0299 0.0199  99  GLU B O   
2094 C CB  . GLU B 73  ? 0.2629 0.2478 0.2387 0.0104  -0.0460 0.0294  99  GLU B CB  
2095 C CG  . GLU B 73  ? 0.3549 0.3341 0.3430 0.0126  -0.0524 0.0306  99  GLU B CG  
2096 C CD  . GLU B 73  ? 0.4924 0.4637 0.4765 0.0103  -0.0635 0.0373  99  GLU B CD  
2097 O OE1 . GLU B 73  ? 0.5422 0.5062 0.5250 0.0086  -0.0678 0.0417  99  GLU B OE1 
2098 O OE2 . GLU B 73  ? 0.5514 0.5227 0.5331 0.0096  -0.0687 0.0386  99  GLU B OE2 
2099 N N   . PRO B 74  ? 0.2317 0.2277 0.1867 0.0075  -0.0272 0.0257  100 PRO B N   
2100 C CA  . PRO B 74  ? 0.2428 0.2438 0.1885 0.0072  -0.0218 0.0234  100 PRO B CA  
2101 C C   . PRO B 74  ? 0.2555 0.2562 0.1900 0.0056  -0.0248 0.0245  100 PRO B C   
2102 O O   . PRO B 74  ? 0.2707 0.2736 0.1938 0.0029  -0.0229 0.0268  100 PRO B O   
2103 C CB  . PRO B 74  ? 0.2500 0.2537 0.1914 0.0050  -0.0174 0.0257  100 PRO B CB  
2104 C CG  . PRO B 74  ? 0.2529 0.2518 0.1944 0.0020  -0.0226 0.0315  100 PRO B CG  
2105 C CD  . PRO B 74  ? 0.2315 0.2248 0.1842 0.0048  -0.0281 0.0303  100 PRO B CD  
2106 N N   . MET B 75  ? 0.2489 0.2471 0.1864 0.0069  -0.0295 0.0229  101 MET B N   
2107 C CA  . MET B 75  ? 0.2624 0.2587 0.1885 0.0052  -0.0336 0.0237  101 MET B CA  
2108 C C   . MET B 75  ? 0.2592 0.2542 0.1905 0.0072  -0.0369 0.0198  101 MET B C   
2109 O O   . MET B 75  ? 0.2441 0.2396 0.1899 0.0090  -0.0384 0.0186  101 MET B O   
2110 C CB  . MET B 75  ? 0.2669 0.2581 0.1875 0.0017  -0.0410 0.0303  101 MET B CB  
2111 C CG  . MET B 75  ? 0.2899 0.2768 0.2249 0.0031  -0.0483 0.0322  101 MET B CG  
2112 S SD  . MET B 75  ? 0.4283 0.4069 0.3557 -0.0013 -0.0590 0.0407  101 MET B SD  
2113 C CE  . MET B 75  ? 0.4265 0.4016 0.3754 0.0028  -0.0683 0.0400  101 MET B CE  
2114 N N   . TRP B 76  ? 0.2768 0.2707 0.1965 0.0066  -0.0379 0.0176  102 TRP B N   
2115 C CA  . TRP B 76  ? 0.3002 0.2919 0.2228 0.0075  -0.0420 0.0142  102 TRP B CA  
2116 C C   . TRP B 76  ? 0.3011 0.2904 0.2345 0.0068  -0.0507 0.0170  102 TRP B C   
2117 O O   . TRP B 76  ? 0.2970 0.2871 0.2405 0.0076  -0.0531 0.0146  102 TRP B O   
2118 C CB  . TRP B 76  ? 0.3148 0.3033 0.2199 0.0064  -0.0437 0.0121  102 TRP B CB  
2119 C CG  . TRP B 76  ? 0.3276 0.3193 0.2223 0.0078  -0.0359 0.0085  102 TRP B CG  
2120 C CD1 . TRP B 76  ? 0.3425 0.3384 0.2434 0.0104  -0.0287 0.0057  102 TRP B CD1 
2121 C CD2 . TRP B 76  ? 0.3371 0.3286 0.2137 0.0066  -0.0343 0.0073  102 TRP B CD2 
2122 N NE1 . TRP B 76  ? 0.3468 0.3458 0.2369 0.0116  -0.0233 0.0025  102 TRP B NE1 
2123 C CE2 . TRP B 76  ? 0.3470 0.3440 0.2220 0.0094  -0.0259 0.0030  102 TRP B CE2 
2124 C CE3 . TRP B 76  ? 0.3544 0.3417 0.2155 0.0033  -0.0393 0.0093  102 TRP B CE3 
2125 C CZ2 . TRP B 76  ? 0.3625 0.3627 0.2227 0.0095  -0.0213 -0.0001 102 TRP B CZ2 
2126 C CZ3 . TRP B 76  ? 0.3757 0.3652 0.2196 0.0028  -0.0346 0.0062  102 TRP B CZ3 
2127 C CH2 . TRP B 76  ? 0.3789 0.3754 0.2231 0.0062  -0.0253 0.0011  102 TRP B CH2 
2128 N N   . GLU B 77  ? 0.3029 0.2893 0.2343 0.0051  -0.0558 0.0224  103 GLU B N   
2129 C CA  . GLU B 77  ? 0.3161 0.2996 0.2580 0.0048  -0.0656 0.0256  103 GLU B CA  
2130 C C   . GLU B 77  ? 0.3177 0.3055 0.2818 0.0080  -0.0646 0.0239  103 GLU B C   
2131 O O   . GLU B 77  ? 0.3327 0.3210 0.3101 0.0089  -0.0716 0.0242  103 GLU B O   
2132 C CB  . GLU B 77  ? 0.3537 0.3314 0.2861 0.0018  -0.0716 0.0323  103 GLU B CB  
2133 C CG  . GLU B 77  ? 0.4130 0.3863 0.3227 -0.0023 -0.0745 0.0340  103 GLU B CG  
2134 C CD  . GLU B 77  ? 0.4681 0.4441 0.3610 -0.0041 -0.0653 0.0335  103 GLU B CD  
2135 O OE1 . GLU B 77  ? 0.3980 0.3799 0.2969 -0.0018 -0.0563 0.0306  103 GLU B OE1 
2136 O OE2 . GLU B 77  ? 0.5428 0.5156 0.4163 -0.0082 -0.0674 0.0358  103 GLU B OE2 
2137 N N   . ASP B 78  ? 0.2939 0.2855 0.2628 0.0097  -0.0560 0.0219  104 ASP B N   
2138 C CA  . ASP B 78  ? 0.2822 0.2783 0.2703 0.0127  -0.0535 0.0192  104 ASP B CA  
2139 C C   . ASP B 78  ? 0.2744 0.2758 0.2726 0.0132  -0.0524 0.0150  104 ASP B C   
2140 O O   . ASP B 78  ? 0.2660 0.2674 0.2551 0.0117  -0.0495 0.0129  104 ASP B O   
2141 C CB  . ASP B 78  ? 0.2879 0.2859 0.2750 0.0136  -0.0445 0.0176  104 ASP B CB  
2142 C CG  . ASP B 78  ? 0.3351 0.3360 0.3392 0.0165  -0.0423 0.0150  104 ASP B CG  
2143 O OD1 . ASP B 78  ? 0.3500 0.3568 0.3645 0.0175  -0.0386 0.0107  104 ASP B OD1 
2144 O OD2 . ASP B 78  ? 0.3392 0.3366 0.3458 0.0175  -0.0440 0.0170  104 ASP B OD2 
2145 N N   . GLU B 79  ? 0.2731 0.2793 0.2907 0.0152  -0.0544 0.0134  105 GLU B N   
2146 C CA  . GLU B 79  ? 0.2783 0.2916 0.3085 0.0147  -0.0531 0.0098  105 GLU B CA  
2147 C C   . GLU B 79  ? 0.2710 0.2871 0.2967 0.0134  -0.0433 0.0064  105 GLU B C   
2148 O O   . GLU B 79  ? 0.2701 0.2883 0.2964 0.0110  -0.0430 0.0048  105 GLU B O   
2149 C CB  . GLU B 79  ? 0.3180 0.3385 0.3715 0.0177  -0.0539 0.0078  105 GLU B CB  
2150 C CG  . GLU B 79  ? 0.4372 0.4668 0.5064 0.0165  -0.0544 0.0051  105 GLU B CG  
2151 C CD  . GLU B 79  ? 0.5918 0.6193 0.6629 0.0149  -0.0658 0.0080  105 GLU B CD  
2152 O OE1 . GLU B 79  ? 0.6272 0.6479 0.6944 0.0160  -0.0745 0.0118  105 GLU B OE1 
2153 O OE2 . GLU B 79  ? 0.6372 0.6692 0.7130 0.0118  -0.0666 0.0069  105 GLU B OE2 
2154 N N   . LYS B 80  ? 0.2564 0.2720 0.2780 0.0146  -0.0362 0.0055  106 LYS B N   
2155 C CA  . LYS B 80  ? 0.2551 0.2724 0.2722 0.0132  -0.0280 0.0028  106 LYS B CA  
2156 C C   . LYS B 80  ? 0.2460 0.2578 0.2455 0.0118  -0.0272 0.0034  106 LYS B C   
2157 O O   . LYS B 80  ? 0.2542 0.2659 0.2497 0.0105  -0.0224 0.0014  106 LYS B O   
2158 C CB  . LYS B 80  ? 0.2879 0.3065 0.3082 0.0148  -0.0213 0.0012  106 LYS B CB  
2159 C CG  . LYS B 80  ? 0.3604 0.3857 0.3989 0.0167  -0.0199 -0.0017 106 LYS B CG  
2160 C CD  . LYS B 80  ? 0.4413 0.4742 0.4878 0.0141  -0.0150 -0.0049 106 LYS B CD  
2161 C CE  . LYS B 80  ? 0.4986 0.5408 0.5649 0.0161  -0.0127 -0.0086 106 LYS B CE  
2162 N NZ  . LYS B 80  ? 0.5352 0.5773 0.6026 0.0185  -0.0063 -0.0119 106 LYS B NZ  
2163 N N   . ASN B 81  ? 0.2334 0.2405 0.2222 0.0120  -0.0320 0.0058  107 ASN B N   
2164 C CA  . ASN B 81  ? 0.2269 0.2301 0.1998 0.0114  -0.0310 0.0053  107 ASN B CA  
2165 C C   . ASN B 81  ? 0.2370 0.2366 0.2036 0.0102  -0.0376 0.0050  107 ASN B C   
2166 O O   . ASN B 81  ? 0.2602 0.2564 0.2156 0.0101  -0.0368 0.0029  107 ASN B O   
2167 C CB  . ASN B 81  ? 0.2217 0.2231 0.1845 0.0120  -0.0299 0.0078  107 ASN B CB  
2168 C CG  . ASN B 81  ? 0.2356 0.2390 0.2020 0.0128  -0.0243 0.0083  107 ASN B CG  
2169 O OD1 . ASN B 81  ? 0.2299 0.2350 0.1998 0.0131  -0.0192 0.0058  107 ASN B OD1 
2170 N ND2 . ASN B 81  ? 0.2251 0.2273 0.1898 0.0126  -0.0259 0.0119  107 ASN B ND2 
2171 N N   . LYS B 82  ? 0.2302 0.2299 0.2037 0.0094  -0.0447 0.0070  108 LYS B N   
2172 C CA  . LYS B 82  ? 0.2503 0.2454 0.2165 0.0077  -0.0525 0.0072  108 LYS B CA  
2173 C C   . LYS B 82  ? 0.2571 0.2501 0.2208 0.0063  -0.0527 0.0037  108 LYS B C   
2174 O O   . LYS B 82  ? 0.2759 0.2628 0.2256 0.0058  -0.0562 0.0023  108 LYS B O   
2175 C CB  . LYS B 82  ? 0.2756 0.2717 0.2530 0.0071  -0.0612 0.0103  108 LYS B CB  
2176 C CG  . LYS B 82  ? 0.3460 0.3462 0.3391 0.0056  -0.0654 0.0091  108 LYS B CG  
2177 C CD  . LYS B 82  ? 0.4128 0.4136 0.4165 0.0055  -0.0754 0.0122  108 LYS B CD  
2178 C CE  . LYS B 82  ? 0.4912 0.4829 0.4773 0.0035  -0.0843 0.0147  108 LYS B CE  
2179 N NZ  . LYS B 82  ? 0.5227 0.5141 0.5196 0.0026  -0.0962 0.0178  108 LYS B NZ  
2180 N N   . ARG B 83  ? 0.2442 0.2416 0.2199 0.0054  -0.0490 0.0022  109 ARG B N   
2181 C CA  . ARG B 83  ? 0.2465 0.2405 0.2195 0.0031  -0.0500 -0.0003 109 ARG B CA  
2182 C C   . ARG B 83  ? 0.2311 0.2223 0.1957 0.0043  -0.0433 -0.0027 109 ARG B C   
2183 O O   . ARG B 83  ? 0.2297 0.2169 0.1923 0.0024  -0.0442 -0.0045 109 ARG B O   
2184 C CB  . ARG B 83  ? 0.2791 0.2797 0.2700 -0.0001 -0.0509 0.0002  109 ARG B CB  
2185 C CG  . ARG B 83  ? 0.3553 0.3587 0.3565 -0.0014 -0.0593 0.0021  109 ARG B CG  
2186 C CD  . ARG B 83  ? 0.4293 0.4430 0.4520 -0.0043 -0.0588 0.0023  109 ARG B CD  
2187 N NE  . ARG B 83  ? 0.5110 0.5243 0.5335 -0.0087 -0.0562 0.0011  109 ARG B NE  
2188 C CZ  . ARG B 83  ? 0.5735 0.5818 0.5931 -0.0127 -0.0630 0.0012  109 ARG B CZ  
2189 N NH1 . ARG B 83  ? 0.5782 0.5820 0.5949 -0.0129 -0.0727 0.0020  109 ARG B NH1 
2190 N NH2 . ARG B 83  ? 0.5832 0.5899 0.6021 -0.0173 -0.0609 0.0007  109 ARG B NH2 
2191 N N   . GLY B 84  ? 0.2184 0.2110 0.1783 0.0071  -0.0378 -0.0024 110 GLY B N   
2192 C CA  . GLY B 84  ? 0.2126 0.2036 0.1669 0.0085  -0.0321 -0.0043 110 GLY B CA  
2193 C C   . GLY B 84  ? 0.2163 0.2025 0.1562 0.0113  -0.0320 -0.0069 110 GLY B C   
2194 O O   . GLY B 84  ? 0.2190 0.2008 0.1502 0.0116  -0.0368 -0.0085 110 GLY B O   
2195 N N   . GLY B 85  ? 0.2129 0.2002 0.1506 0.0133  -0.0266 -0.0078 111 GLY B N   
2196 C CA  . GLY B 85  ? 0.2198 0.2048 0.1467 0.0167  -0.0252 -0.0111 111 GLY B CA  
2197 C C   . GLY B 85  ? 0.2190 0.2079 0.1480 0.0185  -0.0192 -0.0108 111 GLY B C   
2198 O O   . GLY B 85  ? 0.2197 0.2122 0.1562 0.0169  -0.0164 -0.0078 111 GLY B O   
2199 N N   . ARG B 86  ? 0.2106 0.1986 0.1334 0.0220  -0.0177 -0.0144 112 ARG B N   
2200 C CA  . ARG B 86  ? 0.2155 0.2080 0.1410 0.0238  -0.0129 -0.0141 112 ARG B CA  
2201 C C   . ARG B 86  ? 0.2186 0.2077 0.1423 0.0276  -0.0133 -0.0186 112 ARG B C   
2202 O O   . ARG B 86  ? 0.2193 0.2045 0.1368 0.0305  -0.0157 -0.0233 112 ARG B O   
2203 C CB  . ARG B 86  ? 0.2293 0.2296 0.1516 0.0244  -0.0089 -0.0126 112 ARG B CB  
2204 C CG  . ARG B 86  ? 0.2962 0.2968 0.2083 0.0268  -0.0093 -0.0165 112 ARG B CG  
2205 C CD  . ARG B 86  ? 0.3584 0.3677 0.2660 0.0268  -0.0044 -0.0154 112 ARG B CD  
2206 N NE  . ARG B 86  ? 0.4198 0.4292 0.3157 0.0286  -0.0043 -0.0200 112 ARG B NE  
2207 C CZ  . ARG B 86  ? 0.4727 0.4897 0.3612 0.0279  0.0001  -0.0197 112 ARG B CZ  
2208 N NH1 . ARG B 86  ? 0.4724 0.4972 0.3649 0.0251  0.0040  -0.0146 112 ARG B NH1 
2209 N NH2 . ARG B 86  ? 0.4897 0.5063 0.3659 0.0294  0.0005  -0.0247 112 ARG B NH2 
2210 N N   . TRP B 87  ? 0.2177 0.2077 0.1467 0.0278  -0.0114 -0.0174 113 TRP B N   
2211 C CA  . TRP B 87  ? 0.2243 0.2119 0.1537 0.0318  -0.0124 -0.0211 113 TRP B CA  
2212 C C   . TRP B 87  ? 0.2434 0.2413 0.1732 0.0351  -0.0074 -0.0224 113 TRP B C   
2213 O O   . TRP B 87  ? 0.2425 0.2470 0.1756 0.0327  -0.0038 -0.0183 113 TRP B O   
2214 C CB  . TRP B 87  ? 0.2122 0.1961 0.1466 0.0296  -0.0134 -0.0182 113 TRP B CB  
2215 C CG  . TRP B 87  ? 0.2122 0.1857 0.1453 0.0264  -0.0185 -0.0177 113 TRP B CG  
2216 C CD1 . TRP B 87  ? 0.2203 0.1922 0.1551 0.0205  -0.0184 -0.0138 113 TRP B CD1 
2217 C CD2 . TRP B 87  ? 0.2117 0.1753 0.1414 0.0285  -0.0245 -0.0213 113 TRP B CD2 
2218 N NE1 . TRP B 87  ? 0.2242 0.1866 0.1568 0.0179  -0.0237 -0.0140 113 TRP B NE1 
2219 C CE2 . TRP B 87  ? 0.2261 0.1821 0.1552 0.0226  -0.0281 -0.0184 113 TRP B CE2 
2220 C CE3 . TRP B 87  ? 0.2188 0.1792 0.1464 0.0349  -0.0272 -0.0272 113 TRP B CE3 
2221 C CZ2 . TRP B 87  ? 0.2429 0.1868 0.1685 0.0221  -0.0352 -0.0202 113 TRP B CZ2 
2222 C CZ3 . TRP B 87  ? 0.2397 0.1874 0.1643 0.0355  -0.0345 -0.0298 113 TRP B CZ3 
2223 C CH2 . TRP B 87  ? 0.2518 0.1907 0.1751 0.0288  -0.0389 -0.0258 113 TRP B CH2 
2224 N N   . LEU B 88  ? 0.2648 0.2644 0.1915 0.0403  -0.0069 -0.0282 114 LEU B N   
2225 C CA  . LEU B 88  ? 0.2847 0.2966 0.2119 0.0426  -0.0010 -0.0296 114 LEU B CA  
2226 C C   . LEU B 88  ? 0.3052 0.3214 0.2395 0.0481  -0.0001 -0.0339 114 LEU B C   
2227 O O   . LEU B 88  ? 0.3052 0.3139 0.2402 0.0527  -0.0045 -0.0390 114 LEU B O   
2228 C CB  . LEU B 88  ? 0.3013 0.3152 0.2182 0.0436  0.0005  -0.0332 114 LEU B CB  
2229 C CG  . LEU B 88  ? 0.3319 0.3591 0.2467 0.0457  0.0074  -0.0359 114 LEU B CG  
2230 C CD1 . LEU B 88  ? 0.3306 0.3664 0.2459 0.0399  0.0115  -0.0285 114 LEU B CD1 
2231 C CD2 . LEU B 88  ? 0.3566 0.3824 0.2591 0.0480  0.0078  -0.0421 114 LEU B CD2 
2232 N N   . ILE B 89  ? 0.3132 0.3407 0.2539 0.0475  0.0045  -0.0313 115 ILE B N   
2233 C CA  . ILE B 89  ? 0.3408 0.3755 0.2909 0.0525  0.0056  -0.0349 115 ILE B CA  
2234 C C   . ILE B 89  ? 0.3545 0.4052 0.3048 0.0539  0.0132  -0.0373 115 ILE B C   
2235 O O   . ILE B 89  ? 0.3472 0.4048 0.2945 0.0485  0.0174  -0.0321 115 ILE B O   
2236 C CB  . ILE B 89  ? 0.3614 0.3956 0.3202 0.0499  0.0035  -0.0296 115 ILE B CB  
2237 C CG1 . ILE B 89  ? 0.3949 0.4132 0.3514 0.0480  -0.0035 -0.0277 115 ILE B CG1 
2238 C CG2 . ILE B 89  ? 0.3627 0.4065 0.3333 0.0550  0.0043  -0.0328 115 ILE B CG2 
2239 C CD1 . ILE B 89  ? 0.4282 0.4439 0.3894 0.0445  -0.0058 -0.0227 115 ILE B CD1 
2240 N N   . THR B 90  ? 0.3679 0.4240 0.3208 0.0610  0.0150  -0.0455 116 THR B N   
2241 C CA  . THR B 90  ? 0.3931 0.4664 0.3465 0.0624  0.0234  -0.0490 116 THR B CA  
2242 C C   . THR B 90  ? 0.4130 0.4989 0.3828 0.0667  0.0254  -0.0512 116 THR B C   
2243 O O   . THR B 90  ? 0.4105 0.4913 0.3885 0.0734  0.0204  -0.0564 116 THR B O   
2244 C CB  . THR B 90  ? 0.4188 0.4909 0.3621 0.0674  0.0252  -0.0580 116 THR B CB  
2245 O OG1 . THR B 90  ? 0.4415 0.5017 0.3703 0.0626  0.0222  -0.0550 116 THR B OG1 
2246 C CG2 . THR B 90  ? 0.4199 0.5110 0.3621 0.0684  0.0353  -0.0622 116 THR B CG2 
2247 N N   . LEU B 91  ? 0.4326 0.5345 0.4079 0.0624  0.0317  -0.0469 117 LEU B N   
2248 C CA  . LEU B 91  ? 0.4554 0.5722 0.4480 0.0655  0.0340  -0.0482 117 LEU B CA  
2249 C C   . LEU B 91  ? 0.4901 0.6263 0.4863 0.0702  0.0431  -0.0564 117 LEU B C   
2250 O O   . LEU B 91  ? 0.4984 0.6372 0.4810 0.0683  0.0486  -0.0584 117 LEU B O   
2251 C CB  . LEU B 91  ? 0.4496 0.5730 0.4467 0.0569  0.0353  -0.0382 117 LEU B CB  
2252 C CG  . LEU B 91  ? 0.4743 0.5826 0.4720 0.0530  0.0273  -0.0312 117 LEU B CG  
2253 C CD1 . LEU B 91  ? 0.4936 0.5879 0.4762 0.0474  0.0253  -0.0264 117 LEU B CD1 
2254 C CD2 . LEU B 91  ? 0.4725 0.5902 0.4805 0.0478  0.0279  -0.0246 117 LEU B CD2 
2255 N N   . ASN B 92  ? 0.5098 0.6606 0.5244 0.0759  0.0450  -0.0609 118 ASN B N   
2256 C CA  . ASN B 92  ? 0.5337 0.7062 0.5537 0.0802  0.0552  -0.0691 118 ASN B CA  
2257 C C   . ASN B 92  ? 0.5511 0.7446 0.5756 0.0716  0.0638  -0.0622 118 ASN B C   
2258 O O   . ASN B 92  ? 0.5532 0.7453 0.5831 0.0648  0.0602  -0.0526 118 ASN B O   
2259 C CB  . ASN B 92  ? 0.5486 0.7276 0.5872 0.0922  0.0533  -0.0797 118 ASN B CB  
2260 C CG  . ASN B 92  ? 0.6011 0.7805 0.6592 0.0933  0.0459  -0.0755 118 ASN B CG  
2261 O OD1 . ASN B 92  ? 0.6225 0.8030 0.6828 0.0848  0.0444  -0.0651 118 ASN B OD1 
2262 N ND2 . ASN B 92  ? 0.6056 0.7828 0.6780 0.1039  0.0400  -0.0836 118 ASN B ND2 
2263 N N   . LYS B 93  ? 0.5614 0.7734 0.5823 0.0710  0.0749  -0.0669 119 LYS B N   
2264 C CA  . LYS B 93  ? 0.5711 0.8038 0.5953 0.0617  0.0834  -0.0600 119 LYS B CA  
2265 C C   . LYS B 93  ? 0.5688 0.8212 0.6195 0.0641  0.0849  -0.0607 119 LYS B C   
2266 O O   . LYS B 93  ? 0.5750 0.8234 0.6348 0.0596  0.0784  -0.0521 119 LYS B O   
2267 C CB  . LYS B 93  ? 0.5952 0.8422 0.6057 0.0594  0.0954  -0.0647 119 LYS B CB  
2268 N N   . ASP B 99  ? 0.3571 0.5020 0.4238 0.0419  0.0143  -0.0116 125 ASP B N   
2269 C CA  . ASP B 99  ? 0.3628 0.4885 0.4149 0.0448  0.0112  -0.0142 125 ASP B CA  
2270 C C   . ASP B 99  ? 0.3462 0.4618 0.3809 0.0383  0.0138  -0.0096 125 ASP B C   
2271 O O   . ASP B 99  ? 0.3485 0.4465 0.3735 0.0366  0.0088  -0.0076 125 ASP B O   
2272 C CB  . ASP B 99  ? 0.3977 0.5278 0.4520 0.0540  0.0140  -0.0235 125 ASP B CB  
2273 C CG  . ASP B 99  ? 0.4907 0.6272 0.5630 0.0617  0.0093  -0.0286 125 ASP B CG  
2274 O OD1 . ASP B 99  ? 0.5075 0.6335 0.5840 0.0610  0.0001  -0.0253 125 ASP B OD1 
2275 O OD2 . ASP B 99  ? 0.5307 0.6831 0.6134 0.0684  0.0146  -0.0359 125 ASP B OD2 
2276 N N   . LEU B 100 ? 0.3203 0.4470 0.3512 0.0345  0.0214  -0.0080 126 LEU B N   
2277 C CA  . LEU B 100 ? 0.3167 0.4339 0.3324 0.0287  0.0228  -0.0035 126 LEU B CA  
2278 C C   . LEU B 100 ? 0.2982 0.4033 0.3107 0.0224  0.0176  0.0033  126 LEU B C   
2279 O O   . LEU B 100 ? 0.3038 0.3941 0.3058 0.0213  0.0150  0.0043  126 LEU B O   
2280 C CB  . LEU B 100 ? 0.3205 0.4512 0.3325 0.0243  0.0306  -0.0015 126 LEU B CB  
2281 C CG  . LEU B 100 ? 0.3564 0.4765 0.3531 0.0186  0.0307  0.0033  126 LEU B CG  
2282 C CD1 . LEU B 100 ? 0.3698 0.4795 0.3553 0.0231  0.0302  -0.0016 126 LEU B CD1 
2283 C CD2 . LEU B 100 ? 0.3661 0.4983 0.3599 0.0118  0.0362  0.0081  126 LEU B CD2 
2284 N N   . ASP B 101 ? 0.2737 0.3856 0.2956 0.0183  0.0160  0.0075  127 ASP B N   
2285 C CA  . ASP B 101 ? 0.2680 0.3682 0.2864 0.0124  0.0108  0.0132  127 ASP B CA  
2286 C C   . ASP B 101 ? 0.2479 0.3313 0.2618 0.0149  0.0044  0.0114  127 ASP B C   
2287 O O   . ASP B 101 ? 0.2587 0.3286 0.2626 0.0118  0.0025  0.0134  127 ASP B O   
2288 C CB  . ASP B 101 ? 0.2902 0.4006 0.3202 0.0077  0.0092  0.0175  127 ASP B CB  
2289 C CG  . ASP B 101 ? 0.3747 0.4994 0.4070 0.0020  0.0149  0.0216  127 ASP B CG  
2290 O OD1 . ASP B 101 ? 0.3894 0.5098 0.4105 -0.0009 0.0178  0.0236  127 ASP B OD1 
2291 O OD2 . ASP B 101 ? 0.4061 0.5467 0.4518 0.0000  0.0161  0.0231  127 ASP B OD2 
2292 N N   . ARG B 102 ? 0.2151 0.2997 0.2366 0.0202  0.0010  0.0076  128 ARG B N   
2293 C CA  . ARG B 102 ? 0.2180 0.2869 0.2345 0.0219  -0.0056 0.0065  128 ARG B CA  
2294 C C   . ARG B 102 ? 0.2054 0.2627 0.2092 0.0233  -0.0042 0.0041  128 ARG B C   
2295 O O   . ARG B 102 ? 0.2059 0.2503 0.2003 0.0198  -0.0063 0.0062  128 ARG B O   
2296 C CB  . ARG B 102 ? 0.2363 0.3088 0.2642 0.0279  -0.0104 0.0029  128 ARG B CB  
2297 C CG  . ARG B 102 ? 0.2868 0.3414 0.3077 0.0289  -0.0182 0.0023  128 ARG B CG  
2298 C CD  . ARG B 102 ? 0.3313 0.3871 0.3639 0.0339  -0.0255 0.0002  128 ARG B CD  
2299 N NE  . ARG B 102 ? 0.3758 0.4449 0.4203 0.0419  -0.0224 -0.0059 128 ARG B NE  
2300 C CZ  . ARG B 102 ? 0.4332 0.4968 0.4746 0.0479  -0.0228 -0.0112 128 ARG B CZ  
2301 N NH1 . ARG B 102 ? 0.4693 0.5147 0.4967 0.0461  -0.0264 -0.0104 128 ARG B NH1 
2302 N NH2 . ARG B 102 ? 0.4187 0.4950 0.4708 0.0555  -0.0193 -0.0177 128 ARG B NH2 
2303 N N   . PHE B 103 ? 0.1904 0.2533 0.1940 0.0280  -0.0002 -0.0002 129 PHE B N   
2304 C CA  . PHE B 103 ? 0.2082 0.2610 0.2012 0.0293  0.0004  -0.0024 129 PHE B CA  
2305 C C   . PHE B 103 ? 0.2030 0.2507 0.1869 0.0240  0.0029  0.0013  129 PHE B C   
2306 O O   . PHE B 103 ? 0.1998 0.2362 0.1761 0.0231  0.0013  0.0010  129 PHE B O   
2307 C CB  . PHE B 103 ? 0.2184 0.2780 0.2120 0.0352  0.0039  -0.0081 129 PHE B CB  
2308 C CG  . PHE B 103 ? 0.2403 0.3017 0.2420 0.0424  0.0008  -0.0138 129 PHE B CG  
2309 C CD1 . PHE B 103 ? 0.2590 0.3125 0.2652 0.0434  -0.0066 -0.0132 129 PHE B CD1 
2310 C CD2 . PHE B 103 ? 0.2613 0.3314 0.2654 0.0483  0.0046  -0.0201 129 PHE B CD2 
2311 C CE1 . PHE B 103 ? 0.2693 0.3231 0.2838 0.0506  -0.0108 -0.0184 129 PHE B CE1 
2312 C CE2 . PHE B 103 ? 0.2692 0.3407 0.2821 0.0560  0.0013  -0.0263 129 PHE B CE2 
2313 C CZ  . PHE B 103 ? 0.2630 0.3261 0.2818 0.0573  -0.0069 -0.0253 129 PHE B CZ  
2314 N N   . TRP B 104 ? 0.1874 0.2437 0.1728 0.0204  0.0065  0.0046  130 TRP B N   
2315 C CA  . TRP B 104 ? 0.1891 0.2399 0.1674 0.0158  0.0075  0.0082  130 TRP B CA  
2316 C C   . TRP B 104 ? 0.1871 0.2269 0.1630 0.0122  0.0039  0.0106  130 TRP B C   
2317 O O   . TRP B 104 ? 0.1986 0.2292 0.1682 0.0112  0.0035  0.0104  130 TRP B O   
2318 C CB  . TRP B 104 ? 0.1905 0.2516 0.1699 0.0123  0.0113  0.0117  130 TRP B CB  
2319 C CG  . TRP B 104 ? 0.2089 0.2634 0.1817 0.0080  0.0110  0.0156  130 TRP B CG  
2320 C CD1 . TRP B 104 ? 0.2180 0.2724 0.1915 0.0026  0.0100  0.0207  130 TRP B CD1 
2321 C CD2 . TRP B 104 ? 0.2157 0.2623 0.1812 0.0089  0.0107  0.0145  130 TRP B CD2 
2322 N NE1 . TRP B 104 ? 0.2297 0.2760 0.1971 0.0007  0.0089  0.0226  130 TRP B NE1 
2323 C CE2 . TRP B 104 ? 0.2294 0.2717 0.1924 0.0046  0.0094  0.0189  130 TRP B CE2 
2324 C CE3 . TRP B 104 ? 0.2297 0.2722 0.1913 0.0128  0.0106  0.0103  130 TRP B CE3 
2325 C CZ2 . TRP B 104 ? 0.2465 0.2818 0.2046 0.0046  0.0081  0.0191  130 TRP B CZ2 
2326 C CZ3 . TRP B 104 ? 0.2461 0.2822 0.2025 0.0121  0.0096  0.0108  130 TRP B CZ3 
2327 C CH2 . TRP B 104 ? 0.2492 0.2821 0.2046 0.0083  0.0084  0.0150  130 TRP B CH2 
2328 N N   . LEU B 105 ? 0.1719 0.2130 0.1530 0.0103  0.0012  0.0125  131 LEU B N   
2329 C CA  . LEU B 105 ? 0.1782 0.2080 0.1551 0.0069  -0.0025 0.0140  131 LEU B CA  
2330 C C   . LEU B 105 ? 0.1780 0.1971 0.1487 0.0085  -0.0046 0.0112  131 LEU B C   
2331 O O   . LEU B 105 ? 0.1803 0.1902 0.1441 0.0061  -0.0046 0.0112  131 LEU B O   
2332 C CB  . LEU B 105 ? 0.1713 0.2038 0.1543 0.0042  -0.0062 0.0166  131 LEU B CB  
2333 C CG  . LEU B 105 ? 0.1860 0.2057 0.1624 0.0001  -0.0103 0.0178  131 LEU B CG  
2334 C CD1 . LEU B 105 ? 0.1827 0.1957 0.1526 -0.0027 -0.0082 0.0185  131 LEU B CD1 
2335 C CD2 . LEU B 105 ? 0.1853 0.2081 0.1679 -0.0030 -0.0147 0.0207  131 LEU B CD2 
2336 N N   . GLU B 106 ? 0.1690 0.1894 0.1423 0.0125  -0.0063 0.0087  132 GLU B N   
2337 C CA  . GLU B 106 ? 0.1679 0.1777 0.1351 0.0132  -0.0091 0.0068  132 GLU B CA  
2338 C C   . GLU B 106 ? 0.1725 0.1785 0.1335 0.0132  -0.0058 0.0054  132 GLU B C   
2339 O O   . GLU B 106 ? 0.1861 0.1831 0.1405 0.0107  -0.0066 0.0052  132 GLU B O   
2340 C CB  . GLU B 106 ? 0.1716 0.1833 0.1442 0.0182  -0.0127 0.0043  132 GLU B CB  
2341 C CG  . GLU B 106 ? 0.1925 0.2049 0.1710 0.0175  -0.0180 0.0061  132 GLU B CG  
2342 C CD  . GLU B 106 ? 0.2304 0.2437 0.2163 0.0229  -0.0231 0.0035  132 GLU B CD  
2343 O OE1 . GLU B 106 ? 0.2255 0.2408 0.2128 0.0279  -0.0217 -0.0004 132 GLU B OE1 
2344 O OE2 . GLU B 106 ? 0.2563 0.2677 0.2467 0.0224  -0.0293 0.0051  132 GLU B OE2 
2345 N N   . THR B 107 ? 0.1542 0.1675 0.1173 0.0154  -0.0022 0.0045  133 THR B N   
2346 C CA  . THR B 107 ? 0.1578 0.1685 0.1165 0.0153  0.0000  0.0036  133 THR B CA  
2347 C C   . THR B 107 ? 0.1623 0.1691 0.1186 0.0114  0.0014  0.0055  133 THR B C   
2348 O O   . THR B 107 ? 0.1605 0.1616 0.1133 0.0102  0.0018  0.0045  133 THR B O   
2349 C CB  . THR B 107 ? 0.1715 0.1906 0.1318 0.0178  0.0028  0.0027  133 THR B CB  
2350 O OG1 . THR B 107 ? 0.1739 0.1972 0.1371 0.0222  0.0021  -0.0004 133 THR B OG1 
2351 C CG2 . THR B 107 ? 0.1836 0.1995 0.1395 0.0177  0.0037  0.0019  133 THR B CG2 
2352 N N   . LEU B 108 ? 0.1549 0.1650 0.1136 0.0094  0.0020  0.0081  134 LEU B N   
2353 C CA  . LEU B 108 ? 0.1591 0.1646 0.1161 0.0065  0.0026  0.0093  134 LEU B CA  
2354 C C   . LEU B 108 ? 0.1636 0.1605 0.1161 0.0044  0.0017  0.0078  134 LEU B C   
2355 O O   . LEU B 108 ? 0.1751 0.1679 0.1255 0.0034  0.0034  0.0063  134 LEU B O   
2356 C CB  . LEU B 108 ? 0.1567 0.1653 0.1166 0.0041  0.0018  0.0125  134 LEU B CB  
2357 C CG  . LEU B 108 ? 0.1757 0.1928 0.1385 0.0043  0.0032  0.0150  134 LEU B CG  
2358 C CD1 . LEU B 108 ? 0.1827 0.2025 0.1484 0.0005  0.0019  0.0190  134 LEU B CD1 
2359 C CD2 . LEU B 108 ? 0.1842 0.1992 0.1448 0.0049  0.0040  0.0150  134 LEU B CD2 
2360 N N   . LEU B 109 ? 0.1559 0.1506 0.1069 0.0035  -0.0010 0.0081  135 LEU B N   
2361 C CA  . LEU B 109 ? 0.1812 0.1671 0.1252 0.0005  -0.0023 0.0073  135 LEU B CA  
2362 C C   . LEU B 109 ? 0.1941 0.1763 0.1339 0.0003  -0.0009 0.0053  135 LEU B C   
2363 O O   . LEU B 109 ? 0.2063 0.1834 0.1405 -0.0028 0.0010  0.0041  135 LEU B O   
2364 C CB  . LEU B 109 ? 0.1922 0.1759 0.1356 -0.0006 -0.0071 0.0088  135 LEU B CB  
2365 C CG  . LEU B 109 ? 0.2128 0.1996 0.1603 -0.0020 -0.0090 0.0111  135 LEU B CG  
2366 C CD1 . LEU B 109 ? 0.2045 0.1924 0.1555 -0.0021 -0.0145 0.0128  135 LEU B CD1 
2367 C CD2 . LEU B 109 ? 0.2205 0.2004 0.1622 -0.0057 -0.0082 0.0107  135 LEU B CD2 
2368 N N   . CYS B 110 ? 0.1964 0.1815 0.1388 0.0033  -0.0014 0.0047  136 CYS B N   
2369 C CA  . CYS B 110 ? 0.2160 0.1978 0.1553 0.0025  -0.0007 0.0033  136 CYS B CA  
2370 C C   . CYS B 110 ? 0.2169 0.2009 0.1578 0.0017  0.0036  0.0020  136 CYS B C   
2371 O O   . CYS B 110 ? 0.2251 0.2065 0.1632 -0.0011 0.0055  0.0009  136 CYS B O   
2372 C CB  . CYS B 110 ? 0.2365 0.2205 0.1786 0.0063  -0.0028 0.0025  136 CYS B CB  
2373 S SG  . CYS B 110 ? 0.2897 0.2693 0.2312 0.0080  -0.0090 0.0027  136 CYS B SG  
2374 N N   . LEU B 111 ? 0.2044 0.1937 0.1505 0.0041  0.0049  0.0023  137 LEU B N   
2375 C CA  . LEU B 111 ? 0.2062 0.1975 0.1559 0.0043  0.0075  0.0012  137 LEU B CA  
2376 C C   . LEU B 111 ? 0.1981 0.1861 0.1461 0.0020  0.0097  -0.0003 137 LEU B C   
2377 O O   . LEU B 111 ? 0.2096 0.1970 0.1573 0.0004  0.0125  -0.0026 137 LEU B O   
2378 C CB  . LEU B 111 ? 0.2055 0.2017 0.1598 0.0069  0.0067  0.0028  137 LEU B CB  
2379 C CG  . LEU B 111 ? 0.2298 0.2297 0.1858 0.0092  0.0059  0.0028  137 LEU B CG  
2380 C CD1 . LEU B 111 ? 0.2354 0.2346 0.1884 0.0102  0.0045  0.0017  137 LEU B CD1 
2381 C CD2 . LEU B 111 ? 0.2244 0.2285 0.1816 0.0103  0.0051  0.0052  137 LEU B CD2 
2382 N N   . ILE B 112 ? 0.1841 0.1701 0.1310 0.0014  0.0087  0.0007  138 ILE B N   
2383 C CA  . ILE B 112 ? 0.1928 0.1745 0.1376 -0.0003 0.0105  -0.0016 138 ILE B CA  
2384 C C   . ILE B 112 ? 0.1946 0.1714 0.1308 -0.0040 0.0121  -0.0034 138 ILE B C   
2385 O O   . ILE B 112 ? 0.1979 0.1728 0.1321 -0.0053 0.0158  -0.0070 138 ILE B O   
2386 C CB  . ILE B 112 ? 0.2014 0.1808 0.1468 -0.0004 0.0079  0.0000  138 ILE B CB  
2387 C CG1 . ILE B 112 ? 0.2203 0.1971 0.1606 -0.0029 0.0048  0.0023  138 ILE B CG1 
2388 C CG2 . ILE B 112 ? 0.1982 0.1823 0.1504 0.0019  0.0062  0.0028  138 ILE B CG2 
2389 C CD1 . ILE B 112 ? 0.2540 0.2270 0.1934 -0.0046 0.0022  0.0034  138 ILE B CD1 
2390 N N   . GLY B 113 ? 0.1879 0.1626 0.1192 -0.0057 0.0095  -0.0012 139 GLY B N   
2391 C CA  . GLY B 113 ? 0.1996 0.1683 0.1209 -0.0104 0.0098  -0.0017 139 GLY B CA  
2392 C C   . GLY B 113 ? 0.2136 0.1837 0.1338 -0.0123 0.0126  -0.0026 139 GLY B C   
2393 O O   . GLY B 113 ? 0.2227 0.1880 0.1336 -0.0173 0.0132  -0.0024 139 GLY B O   
2394 N N   . GLU B 114 ? 0.2104 0.1869 0.1394 -0.0092 0.0139  -0.0031 140 GLU B N   
2395 C CA  . GLU B 114 ? 0.2183 0.1968 0.1479 -0.0115 0.0158  -0.0035 140 GLU B CA  
2396 C C   . GLU B 114 ? 0.2309 0.2028 0.1521 -0.0151 0.0117  -0.0007 140 GLU B C   
2397 O O   . GLU B 114 ? 0.2385 0.2076 0.1530 -0.0208 0.0134  -0.0004 140 GLU B O   
2398 C CB  . GLU B 114 ? 0.2676 0.2491 0.1972 -0.0145 0.0224  -0.0071 140 GLU B CB  
2399 C CG  . GLU B 114 ? 0.3367 0.3220 0.2735 -0.0106 0.0254  -0.0106 140 GLU B CG  
2400 C CD  . GLU B 114 ? 0.4462 0.4384 0.3960 -0.0060 0.0251  -0.0112 140 GLU B CD  
2401 O OE1 . GLU B 114 ? 0.4998 0.4959 0.4534 -0.0069 0.0250  -0.0104 140 GLU B OE1 
2402 O OE2 . GLU B 114 ? 0.4255 0.4185 0.3813 -0.0020 0.0241  -0.0121 140 GLU B OE2 
2403 N N   . SER B 115 ? 0.2364 0.2056 0.1580 -0.0120 0.0060  0.0014  141 SER B N   
2404 C CA  . SER B 115 ? 0.2454 0.2069 0.1605 -0.0142 0.0003  0.0040  141 SER B CA  
2405 C C   . SER B 115 ? 0.2403 0.1995 0.1546 -0.0162 -0.0015 0.0047  141 SER B C   
2406 O O   . SER B 115 ? 0.2550 0.2058 0.1629 -0.0189 -0.0069 0.0070  141 SER B O   
2407 C CB  . SER B 115 ? 0.2592 0.2210 0.1787 -0.0089 -0.0049 0.0048  141 SER B CB  
2408 O OG  . SER B 115 ? 0.2842 0.2475 0.2043 -0.0083 -0.0044 0.0050  141 SER B OG  
2409 N N   . PHE B 116 ? 0.2207 0.1862 0.1417 -0.0149 0.0017  0.0031  142 PHE B N   
2410 C CA  . PHE B 116 ? 0.2337 0.1968 0.1545 -0.0174 -0.0006 0.0039  142 PHE B CA  
2411 C C   . PHE B 116 ? 0.2449 0.2096 0.1628 -0.0249 0.0040  0.0044  142 PHE B C   
2412 O O   . PHE B 116 ? 0.2485 0.2146 0.1695 -0.0273 0.0036  0.0048  142 PHE B O   
2413 C CB  . PHE B 116 ? 0.2252 0.1936 0.1547 -0.0118 -0.0015 0.0022  142 PHE B CB  
2414 C CG  . PHE B 116 ? 0.2236 0.1931 0.1558 -0.0050 -0.0041 0.0013  142 PHE B CG  
2415 C CD1 . PHE B 116 ? 0.2296 0.1929 0.1590 -0.0028 -0.0098 0.0017  142 PHE B CD1 
2416 C CD2 . PHE B 116 ? 0.2196 0.1968 0.1577 -0.0011 -0.0008 0.0001  142 PHE B CD2 
2417 C CE1 . PHE B 116 ? 0.2317 0.1986 0.1650 0.0034  -0.0110 0.0003  142 PHE B CE1 
2418 C CE2 . PHE B 116 ? 0.2297 0.2094 0.1699 0.0040  -0.0024 -0.0003 142 PHE B CE2 
2419 C CZ  . PHE B 116 ? 0.2264 0.2019 0.1646 0.0063  -0.0068 -0.0005 142 PHE B CZ  
2420 N N   . ASP B 117 ? 0.2551 0.2198 0.1670 -0.0289 0.0086  0.0040  143 ASP B N   
2421 C CA  . ASP B 117 ? 0.2664 0.2342 0.1745 -0.0363 0.0148  0.0036  143 ASP B CA  
2422 C C   . ASP B 117 ? 0.2641 0.2439 0.1853 -0.0347 0.0202  0.0007  143 ASP B C   
2423 O O   . ASP B 117 ? 0.2624 0.2478 0.1928 -0.0281 0.0214  -0.0020 143 ASP B O   
2424 C CB  . ASP B 117 ? 0.3000 0.2585 0.1966 -0.0447 0.0107  0.0080  143 ASP B CB  
2425 C CG  . ASP B 117 ? 0.3811 0.3278 0.2662 -0.0454 0.0044  0.0107  143 ASP B CG  
2426 O OD1 . ASP B 117 ? 0.3929 0.3396 0.2737 -0.0447 0.0071  0.0092  143 ASP B OD1 
2427 O OD2 . ASP B 117 ? 0.4091 0.3460 0.2901 -0.0462 -0.0040 0.0142  143 ASP B OD2 
2428 N N   . ASP B 118 ? 0.2548 0.2388 0.1777 -0.0410 0.0228  0.0015  144 ASP B N   
2429 C CA  . ASP B 118 ? 0.2509 0.2470 0.1883 -0.0394 0.0269  -0.0012 144 ASP B CA  
2430 C C   . ASP B 118 ? 0.2467 0.2432 0.1933 -0.0328 0.0209  -0.0009 144 ASP B C   
2431 O O   . ASP B 118 ? 0.2429 0.2485 0.2020 -0.0291 0.0230  -0.0034 144 ASP B O   
2432 C CB  . ASP B 118 ? 0.2938 0.2954 0.2315 -0.0486 0.0311  0.0000  144 ASP B CB  
2433 C CG  . ASP B 118 ? 0.4015 0.4071 0.3320 -0.0546 0.0399  -0.0020 144 ASP B CG  
2434 O OD1 . ASP B 118 ? 0.4193 0.4257 0.3486 -0.0502 0.0436  -0.0058 144 ASP B OD1 
2435 O OD2 . ASP B 118 ? 0.4477 0.4552 0.3729 -0.0643 0.0430  0.0003  144 ASP B OD2 
2436 N N   . TYR B 119 ? 0.2437 0.2302 0.1841 -0.0310 0.0133  0.0016  145 TYR B N   
2437 C CA  . TYR B 119 ? 0.2426 0.2291 0.1894 -0.0246 0.0081  0.0010  145 TYR B CA  
2438 C C   . TYR B 119 ? 0.2251 0.2151 0.1761 -0.0170 0.0091  -0.0011 145 TYR B C   
2439 O O   . TYR B 119 ? 0.2101 0.2026 0.1669 -0.0124 0.0065  -0.0018 145 TYR B O   
2440 C CB  . TYR B 119 ? 0.2658 0.2410 0.2049 -0.0242 0.0002  0.0031  145 TYR B CB  
2441 C CG  . TYR B 119 ? 0.3082 0.2777 0.2428 -0.0320 -0.0029 0.0059  145 TYR B CG  
2442 C CD1 . TYR B 119 ? 0.3231 0.2983 0.2651 -0.0357 -0.0025 0.0062  145 TYR B CD1 
2443 C CD2 . TYR B 119 ? 0.3449 0.3031 0.2684 -0.0362 -0.0071 0.0089  145 TYR B CD2 
2444 C CE1 . TYR B 119 ? 0.3485 0.3178 0.2865 -0.0436 -0.0063 0.0095  145 TYR B CE1 
2445 C CE2 . TYR B 119 ? 0.3741 0.3253 0.2926 -0.0441 -0.0112 0.0124  145 TYR B CE2 
2446 C CZ  . TYR B 119 ? 0.3812 0.3381 0.3068 -0.0481 -0.0106 0.0127  145 TYR B CZ  
2447 O OH  . TYR B 119 ? 0.4305 0.3801 0.3510 -0.0570 -0.0151 0.0168  145 TYR B OH  
2448 N N   . SER B 120 ? 0.2208 0.2108 0.1685 -0.0165 0.0127  -0.0019 146 SER B N   
2449 C CA  . SER B 120 ? 0.2357 0.2287 0.1876 -0.0106 0.0137  -0.0034 146 SER B CA  
2450 C C   . SER B 120 ? 0.2402 0.2420 0.2041 -0.0084 0.0164  -0.0056 146 SER B C   
2451 O O   . SER B 120 ? 0.2409 0.2444 0.2092 -0.0035 0.0150  -0.0059 146 SER B O   
2452 C CB  . SER B 120 ? 0.2600 0.2503 0.2059 -0.0117 0.0166  -0.0040 146 SER B CB  
2453 O OG  . SER B 120 ? 0.2891 0.2721 0.2271 -0.0114 0.0121  -0.0017 146 SER B OG  
2454 N N   . ASP B 121 ? 0.2319 0.2396 0.2020 -0.0121 0.0196  -0.0067 147 ASP B N   
2455 C CA  . ASP B 121 ? 0.2299 0.2466 0.2138 -0.0095 0.0209  -0.0089 147 ASP B CA  
2456 C C   . ASP B 121 ? 0.2292 0.2453 0.2171 -0.0060 0.0143  -0.0072 147 ASP B C   
2457 O O   . ASP B 121 ? 0.2302 0.2504 0.2270 -0.0021 0.0128  -0.0080 147 ASP B O   
2458 C CB  . ASP B 121 ? 0.2673 0.2920 0.2580 -0.0148 0.0257  -0.0104 147 ASP B CB  
2459 C CG  . ASP B 121 ? 0.3752 0.4109 0.3824 -0.0117 0.0286  -0.0140 147 ASP B CG  
2460 O OD1 . ASP B 121 ? 0.4004 0.4362 0.4112 -0.0064 0.0293  -0.0163 147 ASP B OD1 
2461 O OD2 . ASP B 121 ? 0.4266 0.4707 0.4441 -0.0145 0.0295  -0.0144 147 ASP B OD2 
2462 N N   . ASP B 122 ? 0.2243 0.2339 0.2043 -0.0072 0.0096  -0.0050 148 ASP B N   
2463 C CA  . ASP B 122 ? 0.2174 0.2251 0.1978 -0.0042 0.0036  -0.0041 148 ASP B CA  
2464 C C   . ASP B 122 ? 0.2138 0.2187 0.1895 0.0010  0.0017  -0.0038 148 ASP B C   
2465 O O   . ASP B 122 ? 0.2173 0.2221 0.1933 0.0035  -0.0023 -0.0034 148 ASP B O   
2466 C CB  . ASP B 122 ? 0.2507 0.2516 0.2241 -0.0071 -0.0007 -0.0030 148 ASP B CB  
2467 C CG  . ASP B 122 ? 0.3307 0.3351 0.3112 -0.0114 -0.0026 -0.0026 148 ASP B CG  
2468 O OD1 . ASP B 122 ? 0.3558 0.3676 0.3441 -0.0152 0.0020  -0.0030 148 ASP B OD1 
2469 O OD2 . ASP B 122 ? 0.3428 0.3430 0.3215 -0.0109 -0.0087 -0.0023 148 ASP B OD2 
2470 N N   . VAL B 123 ? 0.2010 0.2039 0.1719 0.0019  0.0045  -0.0037 149 VAL B N   
2471 C CA  . VAL B 123 ? 0.1953 0.1969 0.1625 0.0057  0.0032  -0.0028 149 VAL B CA  
2472 C C   . VAL B 123 ? 0.1926 0.1981 0.1664 0.0080  0.0032  -0.0025 149 VAL B C   
2473 O O   . VAL B 123 ? 0.2015 0.2095 0.1815 0.0076  0.0060  -0.0036 149 VAL B O   
2474 C CB  . VAL B 123 ? 0.2052 0.2035 0.1664 0.0053  0.0052  -0.0024 149 VAL B CB  
2475 C CG1 . VAL B 123 ? 0.2076 0.2069 0.1672 0.0084  0.0044  -0.0012 149 VAL B CG1 
2476 C CG2 . VAL B 123 ? 0.2086 0.2016 0.1633 0.0035  0.0032  -0.0023 149 VAL B CG2 
2477 N N   . CYS B 124 ? 0.1798 0.1853 0.1517 0.0103  -0.0001 -0.0010 150 CYS B N   
2478 C CA  . CYS B 124 ? 0.1734 0.1805 0.1498 0.0119  -0.0018 0.0004  150 CYS B CA  
2479 C C   . CYS B 124 ? 0.1662 0.1722 0.1382 0.0126  -0.0009 0.0023  150 CYS B C   
2480 O O   . CYS B 124 ? 0.1729 0.1784 0.1491 0.0130  -0.0010 0.0032  150 CYS B O   
2481 C CB  . CYS B 124 ? 0.1773 0.1846 0.1529 0.0126  -0.0067 0.0017  150 CYS B CB  
2482 S SG  . CYS B 124 ? 0.2121 0.2215 0.1957 0.0112  -0.0092 0.0000  150 CYS B SG  
2483 N N   . GLY B 125 ? 0.1501 0.1557 0.1146 0.0127  -0.0004 0.0029  151 GLY B N   
2484 C CA  . GLY B 125 ? 0.1499 0.1562 0.1112 0.0127  0.0006  0.0050  151 GLY B CA  
2485 C C   . GLY B 125 ? 0.1632 0.1714 0.1184 0.0136  0.0013  0.0046  151 GLY B C   
2486 O O   . GLY B 125 ? 0.1578 0.1648 0.1107 0.0146  0.0008  0.0022  151 GLY B O   
2487 N N   . ALA B 126 ? 0.1646 0.1760 0.1178 0.0132  0.0022  0.0068  152 ALA B N   
2488 C CA  . ALA B 126 ? 0.1735 0.1891 0.1230 0.0146  0.0036  0.0059  152 ALA B CA  
2489 C C   . ALA B 126 ? 0.1728 0.1938 0.1193 0.0133  0.0044  0.0089  152 ALA B C   
2490 O O   . ALA B 126 ? 0.1687 0.1889 0.1165 0.0108  0.0035  0.0126  152 ALA B O   
2491 C CB  . ALA B 126 ? 0.1716 0.1874 0.1235 0.0147  0.0049  0.0052  152 ALA B CB  
2492 N N   . VAL B 127 ? 0.1840 0.2100 0.1258 0.0149  0.0059  0.0072  153 VAL B N   
2493 C CA  . VAL B 127 ? 0.2096 0.2419 0.1466 0.0127  0.0076  0.0100  153 VAL B CA  
2494 C C   . VAL B 127 ? 0.2448 0.2865 0.1827 0.0142  0.0119  0.0079  153 VAL B C   
2495 O O   . VAL B 127 ? 0.2491 0.2913 0.1878 0.0184  0.0125  0.0027  153 VAL B O   
2496 C CB  . VAL B 127 ? 0.2147 0.2451 0.1434 0.0126  0.0057  0.0094  153 VAL B CB  
2497 C CG1 . VAL B 127 ? 0.2291 0.2657 0.1500 0.0092  0.0076  0.0128  153 VAL B CG1 
2498 C CG2 . VAL B 127 ? 0.2161 0.2385 0.1467 0.0117  0.0008  0.0112  153 VAL B CG2 
2499 N N   . VAL B 128 ? 0.2640 0.3133 0.2025 0.0107  0.0144  0.0117  154 VAL B N   
2500 C CA  . VAL B 128 ? 0.2983 0.3596 0.2393 0.0120  0.0192  0.0096  154 VAL B CA  
2501 C C   . VAL B 128 ? 0.3304 0.3993 0.2627 0.0086  0.0225  0.0115  154 VAL B C   
2502 O O   . VAL B 128 ? 0.3310 0.3978 0.2591 0.0030  0.0208  0.0178  154 VAL B O   
2503 C CB  . VAL B 128 ? 0.3136 0.3802 0.2643 0.0103  0.0200  0.0119  154 VAL B CB  
2504 C CG1 . VAL B 128 ? 0.3259 0.3890 0.2767 0.0042  0.0177  0.0190  154 VAL B CG1 
2505 C CG2 . VAL B 128 ? 0.3123 0.3944 0.2671 0.0112  0.0254  0.0100  154 VAL B CG2 
2506 N N   . ASN B 129 ? 0.3541 0.4302 0.2823 0.0121  0.0265  0.0059  155 ASN B N   
2507 C CA  . ASN B 129 ? 0.3868 0.4711 0.3047 0.0088  0.0308  0.0067  155 ASN B CA  
2508 C C   . ASN B 129 ? 0.4165 0.5178 0.3404 0.0088  0.0380  0.0049  155 ASN B C   
2509 O O   . ASN B 129 ? 0.4107 0.5179 0.3407 0.0153  0.0408  -0.0025 155 ASN B O   
2510 C CB  . ASN B 129 ? 0.4022 0.4822 0.3092 0.0126  0.0305  0.0006  155 ASN B CB  
2511 C CG  . ASN B 129 ? 0.4332 0.4982 0.3354 0.0121  0.0233  0.0025  155 ASN B CG  
2512 O OD1 . ASN B 129 ? 0.4568 0.5141 0.3604 0.0168  0.0201  -0.0024 155 ASN B OD1 
2513 N ND2 . ASN B 129 ? 0.4235 0.4842 0.3210 0.0061  0.0200  0.0098  155 ASN B ND2 
2514 N N   . VAL B 130 ? 0.4430 0.5524 0.3664 0.0014  0.0405  0.0118  156 VAL B N   
2515 C CA  . VAL B 130 ? 0.4645 0.5926 0.3945 -0.0001 0.0480  0.0111  156 VAL B CA  
2516 C C   . VAL B 130 ? 0.4944 0.6323 0.4114 -0.0017 0.0547  0.0082  156 VAL B C   
2517 O O   . VAL B 130 ? 0.5057 0.6399 0.4087 -0.0088 0.0539  0.0141  156 VAL B O   
2518 C CB  . VAL B 130 ? 0.4750 0.6069 0.4103 -0.0086 0.0470  0.0205  156 VAL B CB  
2519 C CG1 . VAL B 130 ? 0.4775 0.6312 0.4195 -0.0119 0.0553  0.0207  156 VAL B CG1 
2520 C CG2 . VAL B 130 ? 0.4824 0.6045 0.4293 -0.0067 0.0407  0.0222  156 VAL B CG2 
2521 N N   . ARG B 131 ? 0.5006 0.6494 0.4212 0.0053  0.0607  -0.0014 157 ARG B N   
2522 C CA  . ARG B 131 ? 0.5190 0.6780 0.4267 0.0046  0.0683  -0.0060 157 ARG B CA  
2523 C C   . ARG B 131 ? 0.5194 0.7019 0.4394 0.0065  0.0781  -0.0109 157 ARG B C   
2524 O O   . ARG B 131 ? 0.5157 0.7025 0.4532 0.0137  0.0775  -0.0158 157 ARG B O   
2525 C CB  . ARG B 131 ? 0.5466 0.6955 0.4456 0.0128  0.0664  -0.0156 157 ARG B CB  
2526 C CG  . ARG B 131 ? 0.6077 0.7349 0.4966 0.0119  0.0568  -0.0121 157 ARG B CG  
2527 C CD  . ARG B 131 ? 0.6527 0.7758 0.5211 0.0044  0.0564  -0.0074 157 ARG B CD  
2528 N NE  . ARG B 131 ? 0.6938 0.7975 0.5565 0.0033  0.0463  -0.0033 157 ARG B NE  
2529 C CZ  . ARG B 131 ? 0.7137 0.8093 0.5793 -0.0021 0.0402  0.0061  157 ARG B CZ  
2530 N NH1 . ARG B 131 ? 0.6902 0.7937 0.5628 -0.0077 0.0424  0.0129  157 ARG B NH1 
2531 N NH2 . ARG B 131 ? 0.7241 0.8039 0.5866 -0.0020 0.0315  0.0084  157 ARG B NH2 
2532 N N   . ALA B 132 ? 0.5212 0.7192 0.4319 0.0002  0.0869  -0.0099 158 ALA B N   
2533 C CA  . ALA B 132 ? 0.5200 0.7434 0.4433 0.0022  0.0976  -0.0157 158 ALA B CA  
2534 C C   . ALA B 132 ? 0.5200 0.7471 0.4488 0.0155  0.1009  -0.0306 158 ALA B C   
2535 O O   . ALA B 132 ? 0.5195 0.7639 0.4670 0.0212  0.1062  -0.0368 158 ALA B O   
2536 C CB  . ALA B 132 ? 0.5251 0.7643 0.4349 -0.0082 0.1071  -0.0117 158 ALA B CB  
2537 N N   . LYS B 133 ? 0.5233 0.7330 0.4379 0.0208  0.0962  -0.0361 159 LYS B N   
2538 C CA  . LYS B 133 ? 0.5191 0.7279 0.4365 0.0332  0.0974  -0.0502 159 LYS B CA  
2539 C C   . LYS B 133 ? 0.5038 0.6965 0.4344 0.0420  0.0872  -0.0530 159 LYS B C   
2540 O O   . LYS B 133 ? 0.5087 0.6986 0.4425 0.0523  0.0865  -0.0642 159 LYS B O   
2541 C CB  . LYS B 133 ? 0.5581 0.7577 0.4507 0.0333  0.0984  -0.0554 159 LYS B CB  
2542 C CG  . LYS B 133 ? 0.6104 0.8247 0.4863 0.0239  0.1085  -0.0529 159 LYS B CG  
2543 C CD  . LYS B 133 ? 0.6688 0.8838 0.5263 0.0285  0.1141  -0.0650 159 LYS B CD  
2544 C CE  . LYS B 133 ? 0.7045 0.9294 0.5393 0.0176  0.1226  -0.0614 159 LYS B CE  
2545 N NZ  . LYS B 133 ? 0.7335 0.9389 0.5480 0.0074  0.1135  -0.0494 159 LYS B NZ  
2546 N N   . GLY B 134 ? 0.4847 0.6663 0.4215 0.0378  0.0792  -0.0433 160 GLY B N   
2547 C CA  . GLY B 134 ? 0.4621 0.6286 0.4096 0.0443  0.0697  -0.0447 160 GLY B CA  
2548 C C   . GLY B 134 ? 0.4363 0.5850 0.3794 0.0382  0.0610  -0.0346 160 GLY B C   
2549 O O   . GLY B 134 ? 0.4528 0.5909 0.3799 0.0336  0.0587  -0.0310 160 GLY B O   
2550 N N   . ASP B 135 ? 0.3921 0.5375 0.3491 0.0381  0.0560  -0.0302 161 ASP B N   
2551 C CA  . ASP B 135 ? 0.3662 0.4961 0.3199 0.0326  0.0487  -0.0215 161 ASP B CA  
2552 C C   . ASP B 135 ? 0.3428 0.4537 0.2929 0.0372  0.0411  -0.0244 161 ASP B C   
2553 O O   . ASP B 135 ? 0.3413 0.4495 0.2966 0.0448  0.0392  -0.0318 161 ASP B O   
2554 C CB  . ASP B 135 ? 0.3784 0.5126 0.3461 0.0292  0.0469  -0.0153 161 ASP B CB  
2555 C CG  . ASP B 135 ? 0.4433 0.5974 0.4169 0.0240  0.0540  -0.0119 161 ASP B CG  
2556 O OD1 . ASP B 135 ? 0.4507 0.6099 0.4130 0.0178  0.0586  -0.0085 161 ASP B OD1 
2557 O OD2 . ASP B 135 ? 0.4748 0.6394 0.4644 0.0256  0.0547  -0.0124 161 ASP B OD2 
2558 N N   . LYS B 136 ? 0.3185 0.4160 0.2603 0.0324  0.0363  -0.0185 162 LYS B N   
2559 C CA  . LYS B 136 ? 0.2998 0.3806 0.2384 0.0352  0.0295  -0.0204 162 LYS B CA  
2560 C C   . LYS B 136 ? 0.2726 0.3439 0.2148 0.0311  0.0245  -0.0135 162 LYS B C   
2561 O O   . LYS B 136 ? 0.2680 0.3410 0.2090 0.0251  0.0251  -0.0069 162 LYS B O   
2562 C CB  . LYS B 136 ? 0.3252 0.3992 0.2489 0.0341  0.0285  -0.0217 162 LYS B CB  
2563 C CG  . LYS B 136 ? 0.3823 0.4613 0.2994 0.0392  0.0323  -0.0304 162 LYS B CG  
2564 C CD  . LYS B 136 ? 0.4582 0.5289 0.3590 0.0367  0.0301  -0.0306 162 LYS B CD  
2565 C CE  . LYS B 136 ? 0.5121 0.5880 0.4028 0.0406  0.0345  -0.0391 162 LYS B CE  
2566 N NZ  . LYS B 136 ? 0.5588 0.6262 0.4321 0.0369  0.0316  -0.0382 162 LYS B NZ  
2567 N N   . ILE B 137 ? 0.2525 0.3131 0.1982 0.0338  0.0194  -0.0152 163 ILE B N   
2568 C CA  . ILE B 137 ? 0.2461 0.2974 0.1938 0.0300  0.0154  -0.0100 163 ILE B CA  
2569 C C   . ILE B 137 ? 0.2211 0.2599 0.1638 0.0314  0.0109  -0.0122 163 ILE B C   
2570 O O   . ILE B 137 ? 0.2097 0.2449 0.1518 0.0359  0.0091  -0.0176 163 ILE B O   
2571 C CB  . ILE B 137 ? 0.2679 0.3196 0.2254 0.0303  0.0138  -0.0087 163 ILE B CB  
2572 C CG1 . ILE B 137 ? 0.2986 0.3640 0.2627 0.0287  0.0179  -0.0065 163 ILE B CG1 
2573 C CG2 . ILE B 137 ? 0.2830 0.3251 0.2402 0.0261  0.0106  -0.0041 163 ILE B CG2 
2574 C CD1 . ILE B 137 ? 0.3273 0.3946 0.3019 0.0305  0.0156  -0.0069 163 ILE B CD1 
2575 N N   . ALA B 138 ? 0.2052 0.2376 0.1452 0.0274  0.0088  -0.0083 164 ALA B N   
2576 C CA  . ALA B 138 ? 0.2094 0.2319 0.1463 0.0277  0.0048  -0.0098 164 ALA B CA  
2577 C C   . ALA B 138 ? 0.2121 0.2290 0.1526 0.0241  0.0030  -0.0060 164 ALA B C   
2578 O O   . ALA B 138 ? 0.2152 0.2347 0.1578 0.0212  0.0043  -0.0020 164 ALA B O   
2579 C CB  . ALA B 138 ? 0.2098 0.2318 0.1386 0.0271  0.0042  -0.0104 164 ALA B CB  
2580 N N   . ILE B 139 ? 0.2050 0.2143 0.1459 0.0240  -0.0001 -0.0074 165 ILE B N   
2581 C CA  . ILE B 139 ? 0.2093 0.2144 0.1532 0.0205  -0.0009 -0.0048 165 ILE B CA  
2582 C C   . ILE B 139 ? 0.2000 0.2022 0.1422 0.0196  -0.0034 -0.0053 165 ILE B C   
2583 O O   . ILE B 139 ? 0.2044 0.2026 0.1434 0.0209  -0.0061 -0.0081 165 ILE B O   
2584 C CB  . ILE B 139 ? 0.2263 0.2260 0.1720 0.0193  -0.0020 -0.0051 165 ILE B CB  
2585 C CG1 . ILE B 139 ? 0.2500 0.2525 0.1981 0.0192  -0.0003 -0.0036 165 ILE B CG1 
2586 C CG2 . ILE B 139 ? 0.2221 0.2184 0.1697 0.0154  -0.0021 -0.0037 165 ILE B CG2 
2587 C CD1 . ILE B 139 ? 0.2880 0.2842 0.2358 0.0170  -0.0020 -0.0030 165 ILE B CD1 
2588 N N   . TRP B 140 ? 0.1839 0.1876 0.1292 0.0174  -0.0033 -0.0026 166 TRP B N   
2589 C CA  . TRP B 140 ? 0.1891 0.1911 0.1349 0.0164  -0.0065 -0.0026 166 TRP B CA  
2590 C C   . TRP B 140 ? 0.1944 0.1944 0.1467 0.0141  -0.0069 -0.0026 166 TRP B C   
2591 O O   . TRP B 140 ? 0.2003 0.2016 0.1571 0.0128  -0.0041 -0.0016 166 TRP B O   
2592 C CB  . TRP B 140 ? 0.1776 0.1824 0.1243 0.0157  -0.0072 0.0005  166 TRP B CB  
2593 C CG  . TRP B 140 ? 0.1821 0.1892 0.1204 0.0165  -0.0073 0.0011  166 TRP B CG  
2594 C CD1 . TRP B 140 ? 0.1921 0.2022 0.1252 0.0182  -0.0043 -0.0007 166 TRP B CD1 
2595 C CD2 . TRP B 140 ? 0.1788 0.1859 0.1130 0.0151  -0.0103 0.0038  166 TRP B CD2 
2596 N NE1 . TRP B 140 ? 0.1916 0.2046 0.1168 0.0178  -0.0041 0.0002  166 TRP B NE1 
2597 C CE2 . TRP B 140 ? 0.1893 0.1996 0.1138 0.0155  -0.0082 0.0034  166 TRP B CE2 
2598 C CE3 . TRP B 140 ? 0.1864 0.1913 0.1244 0.0136  -0.0149 0.0064  166 TRP B CE3 
2599 C CZ2 . TRP B 140 ? 0.1993 0.2098 0.1154 0.0134  -0.0105 0.0060  166 TRP B CZ2 
2600 C CZ3 . TRP B 140 ? 0.1948 0.1989 0.1255 0.0120  -0.0185 0.0093  166 TRP B CZ3 
2601 C CH2 . TRP B 140 ? 0.1997 0.2062 0.1185 0.0114  -0.0161 0.0095  166 TRP B CH2 
2602 N N   . THR B 141 ? 0.1966 0.1938 0.1491 0.0130  -0.0103 -0.0039 167 THR B N   
2603 C CA  . THR B 141 ? 0.2037 0.2008 0.1631 0.0097  -0.0103 -0.0037 167 THR B CA  
2604 C C   . THR B 141 ? 0.2024 0.2017 0.1676 0.0087  -0.0140 -0.0031 167 THR B C   
2605 O O   . THR B 141 ? 0.2041 0.2023 0.1651 0.0102  -0.0177 -0.0030 167 THR B O   
2606 C CB  . THR B 141 ? 0.2313 0.2229 0.1872 0.0077  -0.0113 -0.0049 167 THR B CB  
2607 O OG1 . THR B 141 ? 0.2625 0.2496 0.2155 0.0073  -0.0165 -0.0062 167 THR B OG1 
2608 C CG2 . THR B 141 ? 0.2283 0.2167 0.1783 0.0097  -0.0099 -0.0055 167 THR B CG2 
2609 N N   . THR B 142 ? 0.2031 0.2061 0.1782 0.0060  -0.0129 -0.0029 168 THR B N   
2610 C CA  . THR B 142 ? 0.2082 0.2153 0.1927 0.0055  -0.0164 -0.0023 168 THR B CA  
2611 C C   . THR B 142 ? 0.2170 0.2220 0.2017 0.0031  -0.0222 -0.0025 168 THR B C   
2612 O O   . THR B 142 ? 0.2120 0.2186 0.2015 0.0035  -0.0272 -0.0016 168 THR B O   
2613 C CB  . THR B 142 ? 0.2169 0.2313 0.2147 0.0043  -0.0123 -0.0027 168 THR B CB  
2614 O OG1 . THR B 142 ? 0.2216 0.2405 0.2303 0.0055  -0.0163 -0.0022 168 THR B OG1 
2615 C CG2 . THR B 142 ? 0.2169 0.2336 0.2183 -0.0004 -0.0092 -0.0036 168 THR B CG2 
2616 N N   . GLU B 143 ? 0.2220 0.2223 0.2018 0.0005  -0.0227 -0.0033 169 GLU B N   
2617 C CA  . GLU B 143 ? 0.2385 0.2359 0.2192 -0.0026 -0.0289 -0.0034 169 GLU B CA  
2618 C C   . GLU B 143 ? 0.2572 0.2442 0.2252 -0.0026 -0.0320 -0.0051 169 GLU B C   
2619 O O   . GLU B 143 ? 0.2550 0.2385 0.2204 -0.0046 -0.0299 -0.0050 169 GLU B O   
2620 C CB  . GLU B 143 ? 0.2471 0.2514 0.2407 -0.0080 -0.0270 -0.0025 169 GLU B CB  
2621 C CG  . GLU B 143 ? 0.2711 0.2730 0.2672 -0.0127 -0.0336 -0.0019 169 GLU B CG  
2622 C CD  . GLU B 143 ? 0.3424 0.3436 0.3399 -0.0108 -0.0410 -0.0019 169 GLU B CD  
2623 O OE1 . GLU B 143 ? 0.3448 0.3361 0.3304 -0.0100 -0.0471 -0.0030 169 GLU B OE1 
2624 O OE2 . GLU B 143 ? 0.3644 0.3740 0.3739 -0.0096 -0.0411 -0.0011 169 GLU B OE2 
2625 N N   . CYS B 144 ? 0.2705 0.2517 0.2299 0.0000  -0.0374 -0.0067 170 CYS B N   
2626 C CA  . CYS B 144 ? 0.3002 0.2712 0.2478 0.0015  -0.0407 -0.0097 170 CYS B CA  
2627 C C   . CYS B 144 ? 0.3274 0.2916 0.2762 -0.0036 -0.0458 -0.0095 170 CYS B C   
2628 O O   . CYS B 144 ? 0.3398 0.2945 0.2808 -0.0028 -0.0481 -0.0115 170 CYS B O   
2629 C CB  . CYS B 144 ? 0.3148 0.2819 0.2518 0.0055  -0.0443 -0.0124 170 CYS B CB  
2630 S SG  . CYS B 144 ? 0.3931 0.3583 0.3313 0.0024  -0.0531 -0.0118 170 CYS B SG  
2631 N N   . GLU B 145 ? 0.3292 0.2987 0.2889 -0.0091 -0.0475 -0.0068 171 GLU B N   
2632 C CA  . GLU B 145 ? 0.3469 0.3115 0.3091 -0.0156 -0.0520 -0.0055 171 GLU B CA  
2633 C C   . GLU B 145 ? 0.3574 0.3242 0.3230 -0.0203 -0.0466 -0.0030 171 GLU B C   
2634 O O   . GLU B 145 ? 0.3670 0.3288 0.3329 -0.0268 -0.0502 -0.0011 171 GLU B O   
2635 C CB  . GLU B 145 ? 0.3804 0.3514 0.3540 -0.0202 -0.0563 -0.0035 171 GLU B CB  
2636 C CG  . GLU B 145 ? 0.4959 0.4613 0.4631 -0.0174 -0.0641 -0.0056 171 GLU B CG  
2637 C CD  . GLU B 145 ? 0.6321 0.6020 0.6104 -0.0221 -0.0707 -0.0036 171 GLU B CD  
2638 O OE1 . GLU B 145 ? 0.6616 0.6390 0.6533 -0.0284 -0.0696 -0.0008 171 GLU B OE1 
2639 O OE2 . GLU B 145 ? 0.6902 0.6568 0.6637 -0.0200 -0.0771 -0.0047 171 GLU B OE2 
2640 N N   . ASN B 146 ? 0.3433 0.3168 0.3107 -0.0178 -0.0386 -0.0026 172 ASN B N   
2641 C CA  . ASN B 146 ? 0.3398 0.3143 0.3078 -0.0226 -0.0336 -0.0004 172 ASN B CA  
2642 C C   . ASN B 146 ? 0.3383 0.2999 0.2936 -0.0206 -0.0363 -0.0012 172 ASN B C   
2643 O O   . ASN B 146 ? 0.3303 0.2922 0.2819 -0.0171 -0.0320 -0.0018 172 ASN B O   
2644 C CB  . ASN B 146 ? 0.3550 0.3409 0.3297 -0.0210 -0.0247 -0.0003 172 ASN B CB  
2645 C CG  . ASN B 146 ? 0.4069 0.4059 0.3967 -0.0237 -0.0218 0.0003  172 ASN B CG  
2646 O OD1 . ASN B 146 ? 0.4272 0.4286 0.4239 -0.0285 -0.0257 0.0015  172 ASN B OD1 
2647 N ND2 . ASN B 146 ? 0.4000 0.4079 0.3963 -0.0207 -0.0154 -0.0007 172 ASN B ND2 
2648 N N   . ARG B 147 ? 0.3449 0.2946 0.2942 -0.0228 -0.0442 -0.0015 173 ARG B N   
2649 C CA  . ARG B 147 ? 0.3612 0.2973 0.3000 -0.0199 -0.0486 -0.0030 173 ARG B CA  
2650 C C   . ARG B 147 ? 0.3413 0.2756 0.2771 -0.0225 -0.0450 -0.0002 173 ARG B C   
2651 O O   . ARG B 147 ? 0.3334 0.2637 0.2642 -0.0167 -0.0447 -0.0022 173 ARG B O   
2652 C CB  . ARG B 147 ? 0.4129 0.3352 0.3468 -0.0231 -0.0587 -0.0034 173 ARG B CB  
2653 C CG  . ARG B 147 ? 0.5111 0.4342 0.4500 -0.0343 -0.0605 0.0018  173 ARG B CG  
2654 C CD  . ARG B 147 ? 0.6061 0.5129 0.5390 -0.0386 -0.0715 0.0023  173 ARG B CD  
2655 N NE  . ARG B 147 ? 0.6741 0.5818 0.6112 -0.0405 -0.0769 0.0013  173 ARG B NE  
2656 C CZ  . ARG B 147 ? 0.7399 0.6331 0.6720 -0.0434 -0.0875 0.0007  173 ARG B CZ  
2657 N NH1 . ARG B 147 ? 0.7567 0.6331 0.6799 -0.0444 -0.0943 0.0010  173 ARG B NH1 
2658 N NH2 . ARG B 147 ? 0.7409 0.6354 0.6769 -0.0454 -0.0926 -0.0001 173 ARG B NH2 
2659 N N   . GLU B 148 ? 0.3235 0.2617 0.2624 -0.0315 -0.0420 0.0041  174 GLU B N   
2660 C CA  . GLU B 148 ? 0.3229 0.2587 0.2567 -0.0352 -0.0389 0.0071  174 GLU B CA  
2661 C C   . GLU B 148 ? 0.2963 0.2404 0.2312 -0.0296 -0.0313 0.0055  174 GLU B C   
2662 O O   . GLU B 148 ? 0.2963 0.2338 0.2247 -0.0271 -0.0324 0.0055  174 GLU B O   
2663 C CB  . GLU B 148 ? 0.3689 0.3083 0.3045 -0.0469 -0.0363 0.0118  174 GLU B CB  
2664 C CG  . GLU B 148 ? 0.4916 0.4165 0.4207 -0.0540 -0.0457 0.0152  174 GLU B CG  
2665 C CD  . GLU B 148 ? 0.6324 0.5619 0.5676 -0.0642 -0.0466 0.0186  174 GLU B CD  
2666 O OE1 . GLU B 148 ? 0.6787 0.6249 0.6246 -0.0666 -0.0386 0.0185  174 GLU B OE1 
2667 O OE2 . GLU B 148 ? 0.6609 0.5770 0.5908 -0.0698 -0.0558 0.0213  174 GLU B OE2 
2668 N N   . ALA B 149 ? 0.2628 0.2203 0.2063 -0.0275 -0.0247 0.0040  175 ALA B N   
2669 C CA  . ALA B 149 ? 0.2555 0.2198 0.2002 -0.0225 -0.0184 0.0026  175 ALA B CA  
2670 C C   . ALA B 149 ? 0.2518 0.2119 0.1928 -0.0139 -0.0213 -0.0002 175 ALA B C   
2671 O O   . ALA B 149 ? 0.2546 0.2124 0.1915 -0.0115 -0.0202 -0.0002 175 ALA B O   
2672 C CB  . ALA B 149 ? 0.2482 0.2260 0.2036 -0.0218 -0.0123 0.0015  175 ALA B CB  
2673 N N   . VAL B 150 ? 0.2406 0.1998 0.1826 -0.0098 -0.0253 -0.0026 176 VAL B N   
2674 C CA  . VAL B 150 ? 0.2453 0.2025 0.1837 -0.0019 -0.0269 -0.0059 176 VAL B CA  
2675 C C   . VAL B 150 ? 0.2424 0.1896 0.1745 0.0004  -0.0310 -0.0069 176 VAL B C   
2676 O O   . VAL B 150 ? 0.2357 0.1851 0.1672 0.0054  -0.0289 -0.0083 176 VAL B O   
2677 C CB  . VAL B 150 ? 0.2638 0.2202 0.2018 0.0006  -0.0309 -0.0085 176 VAL B CB  
2678 C CG1 . VAL B 150 ? 0.2775 0.2310 0.2098 0.0081  -0.0325 -0.0127 176 VAL B CG1 
2679 C CG2 . VAL B 150 ? 0.2643 0.2311 0.2094 0.0000  -0.0276 -0.0075 176 VAL B CG2 
2680 N N   . THR B 151 ? 0.2437 0.1799 0.1720 -0.0036 -0.0374 -0.0058 177 THR B N   
2681 C CA  . THR B 151 ? 0.2578 0.1826 0.1810 -0.0009 -0.0432 -0.0069 177 THR B CA  
2682 C C   . THR B 151 ? 0.2509 0.1758 0.1728 -0.0031 -0.0408 -0.0036 177 THR B C   
2683 O O   . THR B 151 ? 0.2492 0.1709 0.1703 0.0021  -0.0430 -0.0053 177 THR B O   
2684 C CB  . THR B 151 ? 0.3076 0.2181 0.2264 -0.0044 -0.0524 -0.0065 177 THR B CB  
2685 O OG1 . THR B 151 ? 0.3500 0.2585 0.2677 -0.0146 -0.0523 -0.0008 177 THR B OG1 
2686 C CG2 . THR B 151 ? 0.3137 0.2228 0.2326 -0.0022 -0.0557 -0.0102 177 THR B CG2 
2687 N N   . HIS B 152 ? 0.2471 0.1767 0.1693 -0.0105 -0.0359 0.0004  178 HIS B N   
2688 C CA  . HIS B 152 ? 0.2560 0.1852 0.1749 -0.0133 -0.0335 0.0033  178 HIS B CA  
2689 C C   . HIS B 152 ? 0.2402 0.1786 0.1631 -0.0067 -0.0284 0.0010  178 HIS B C   
2690 O O   . HIS B 152 ? 0.2346 0.1700 0.1556 -0.0043 -0.0302 0.0013  178 HIS B O   
2691 C CB  . HIS B 152 ? 0.2825 0.2158 0.2001 -0.0226 -0.0283 0.0070  178 HIS B CB  
2692 C CG  . HIS B 152 ? 0.3213 0.2531 0.2331 -0.0260 -0.0259 0.0094  178 HIS B CG  
2693 N ND1 . HIS B 152 ? 0.3564 0.2974 0.2708 -0.0236 -0.0189 0.0081  178 HIS B ND1 
2694 C CD2 . HIS B 152 ? 0.3348 0.2554 0.2373 -0.0316 -0.0309 0.0132  178 HIS B CD2 
2695 C CE1 . HIS B 152 ? 0.3556 0.2913 0.2620 -0.0280 -0.0193 0.0107  178 HIS B CE1 
2696 N NE2 . HIS B 152 ? 0.3578 0.2812 0.2565 -0.0331 -0.0265 0.0141  178 HIS B NE2 
2697 N N   . ILE B 153 ? 0.2309 0.1800 0.1595 -0.0040 -0.0228 -0.0008 179 ILE B N   
2698 C CA  . ILE B 153 ? 0.2153 0.1728 0.1474 0.0013  -0.0184 -0.0023 179 ILE B CA  
2699 C C   . ILE B 153 ? 0.2163 0.1716 0.1485 0.0084  -0.0222 -0.0051 179 ILE B C   
2700 O O   . ILE B 153 ? 0.2136 0.1703 0.1465 0.0105  -0.0218 -0.0048 179 ILE B O   
2701 C CB  . ILE B 153 ? 0.2055 0.1727 0.1431 0.0026  -0.0139 -0.0033 179 ILE B CB  
2702 C CG1 . ILE B 153 ? 0.2148 0.1865 0.1553 -0.0031 -0.0092 -0.0015 179 ILE B CG1 
2703 C CG2 . ILE B 153 ? 0.2029 0.1772 0.1431 0.0079  -0.0109 -0.0044 179 ILE B CG2 
2704 C CD1 . ILE B 153 ? 0.2091 0.1884 0.1567 -0.0024 -0.0073 -0.0024 179 ILE B CD1 
2705 N N   . GLY B 154 ? 0.2151 0.1665 0.1466 0.0117  -0.0263 -0.0081 180 GLY B N   
2706 C CA  . GLY B 154 ? 0.2284 0.1784 0.1605 0.0190  -0.0293 -0.0122 180 GLY B CA  
2707 C C   . GLY B 154 ? 0.2509 0.1930 0.1826 0.0201  -0.0347 -0.0117 180 GLY B C   
2708 O O   . GLY B 154 ? 0.2564 0.2032 0.1922 0.0254  -0.0341 -0.0136 180 GLY B O   
2709 N N   . ARG B 155 ? 0.2669 0.1970 0.1938 0.0147  -0.0404 -0.0088 181 ARG B N   
2710 C CA  . ARG B 155 ? 0.2935 0.2132 0.2186 0.0146  -0.0476 -0.0073 181 ARG B CA  
2711 C C   . ARG B 155 ? 0.2740 0.1989 0.2005 0.0134  -0.0447 -0.0044 181 ARG B C   
2712 O O   . ARG B 155 ? 0.2627 0.1868 0.1932 0.0184  -0.0485 -0.0058 181 ARG B O   
2713 C CB  . ARG B 155 ? 0.3503 0.2561 0.2679 0.0064  -0.0538 -0.0030 181 ARG B CB  
2714 C CG  . ARG B 155 ? 0.4452 0.3421 0.3610 0.0068  -0.0596 -0.0053 181 ARG B CG  
2715 C CD  . ARG B 155 ? 0.5388 0.4198 0.4472 -0.0015 -0.0679 -0.0003 181 ARG B CD  
2716 N NE  . ARG B 155 ? 0.6035 0.4876 0.5073 -0.0124 -0.0629 0.0058  181 ARG B NE  
2717 C CZ  . ARG B 155 ? 0.6463 0.5339 0.5498 -0.0188 -0.0596 0.0073  181 ARG B CZ  
2718 N NH1 . ARG B 155 ? 0.6474 0.5346 0.5539 -0.0157 -0.0618 0.0039  181 ARG B NH1 
2719 N NH2 . ARG B 155 ? 0.6568 0.5490 0.5572 -0.0282 -0.0542 0.0121  181 ARG B NH2 
2720 N N   . VAL B 156 ? 0.2601 0.1900 0.1838 0.0069  -0.0385 -0.0009 182 VAL B N   
2721 C CA  . VAL B 156 ? 0.2562 0.1899 0.1795 0.0049  -0.0357 0.0016  182 VAL B CA  
2722 C C   . VAL B 156 ? 0.2377 0.1832 0.1692 0.0116  -0.0317 -0.0011 182 VAL B C   
2723 O O   . VAL B 156 ? 0.2265 0.1730 0.1606 0.0133  -0.0338 -0.0004 182 VAL B O   
2724 C CB  . VAL B 156 ? 0.2729 0.2096 0.1915 -0.0029 -0.0293 0.0045  182 VAL B CB  
2725 C CG1 . VAL B 156 ? 0.2721 0.2130 0.1899 -0.0042 -0.0258 0.0059  182 VAL B CG1 
2726 C CG2 . VAL B 156 ? 0.2943 0.2205 0.2042 -0.0112 -0.0326 0.0079  182 VAL B CG2 
2727 N N   . TYR B 157 ? 0.2282 0.1827 0.1636 0.0149  -0.0265 -0.0039 183 TYR B N   
2728 C CA  . TYR B 157 ? 0.2376 0.2038 0.1796 0.0200  -0.0224 -0.0059 183 TYR B CA  
2729 C C   . TYR B 157 ? 0.2532 0.2204 0.2008 0.0268  -0.0265 -0.0091 183 TYR B C   
2730 O O   . TYR B 157 ? 0.2567 0.2310 0.2100 0.0288  -0.0254 -0.0087 183 TYR B O   
2731 C CB  . TYR B 157 ? 0.2381 0.2112 0.1808 0.0217  -0.0177 -0.0079 183 TYR B CB  
2732 C CG  . TYR B 157 ? 0.2537 0.2387 0.2011 0.0252  -0.0129 -0.0090 183 TYR B CG  
2733 C CD1 . TYR B 157 ? 0.2623 0.2528 0.2128 0.0237  -0.0104 -0.0064 183 TYR B CD1 
2734 C CD2 . TYR B 157 ? 0.2699 0.2601 0.2171 0.0285  -0.0108 -0.0120 183 TYR B CD2 
2735 C CE1 . TYR B 157 ? 0.2742 0.2755 0.2285 0.0253  -0.0061 -0.0063 183 TYR B CE1 
2736 C CE2 . TYR B 157 ? 0.2771 0.2781 0.2267 0.0300  -0.0060 -0.0119 183 TYR B CE2 
2737 C CZ  . TYR B 157 ? 0.2849 0.2916 0.2385 0.0282  -0.0038 -0.0089 183 TYR B CZ  
2738 O OH  . TYR B 157 ? 0.2991 0.3162 0.2548 0.0286  0.0005  -0.0081 183 TYR B OH  
2739 N N   . LYS B 158 ? 0.2585 0.2189 0.2054 0.0305  -0.0314 -0.0125 184 LYS B N   
2740 C CA  . LYS B 158 ? 0.2678 0.2289 0.2214 0.0382  -0.0355 -0.0170 184 LYS B CA  
2741 C C   . LYS B 158 ? 0.2781 0.2340 0.2347 0.0375  -0.0417 -0.0142 184 LYS B C   
2742 O O   . LYS B 158 ? 0.2734 0.2373 0.2394 0.0425  -0.0420 -0.0161 184 LYS B O   
2743 C CB  . LYS B 158 ? 0.3013 0.2530 0.2523 0.0419  -0.0406 -0.0215 184 LYS B CB  
2744 C CG  . LYS B 158 ? 0.3527 0.3029 0.3112 0.0506  -0.0462 -0.0272 184 LYS B CG  
2745 C CD  . LYS B 158 ? 0.4100 0.3511 0.3650 0.0549  -0.0504 -0.0329 184 LYS B CD  
2746 C CE  . LYS B 158 ? 0.4524 0.3904 0.4154 0.0644  -0.0566 -0.0397 184 LYS B CE  
2747 N NZ  . LYS B 158 ? 0.4934 0.4217 0.4519 0.0689  -0.0607 -0.0462 184 LYS B NZ  
2748 N N   . GLU B 159 ? 0.2903 0.2332 0.2398 0.0314  -0.0473 -0.0098 185 GLU B N   
2749 C CA  . GLU B 159 ? 0.3061 0.2422 0.2546 0.0282  -0.0535 -0.0055 185 GLU B CA  
2750 C C   . GLU B 159 ? 0.3064 0.2537 0.2586 0.0264  -0.0482 -0.0032 185 GLU B C   
2751 O O   . GLU B 159 ? 0.3081 0.2577 0.2674 0.0291  -0.0523 -0.0029 185 GLU B O   
2752 C CB  . GLU B 159 ? 0.3710 0.2929 0.3067 0.0189  -0.0570 -0.0003 185 GLU B CB  
2753 C CG  . GLU B 159 ? 0.5013 0.4130 0.4318 0.0139  -0.0645 0.0048  185 GLU B CG  
2754 C CD  . GLU B 159 ? 0.6776 0.5758 0.5936 0.0037  -0.0672 0.0100  185 GLU B CD  
2755 O OE1 . GLU B 159 ? 0.7074 0.6054 0.6192 0.0004  -0.0629 0.0097  185 GLU B OE1 
2756 O OE2 . GLU B 159 ? 0.7382 0.6264 0.6470 -0.0016 -0.0737 0.0146  185 GLU B OE2 
2757 N N   . ARG B 160 ? 0.3055 0.2571 0.2529 0.0216  -0.0412 -0.0013 186 ARG B N   
2758 C CA  . ARG B 160 ? 0.3126 0.2719 0.2614 0.0188  -0.0369 0.0011  186 ARG B CA  
2759 C C   . ARG B 160 ? 0.3088 0.2820 0.2701 0.0250  -0.0346 -0.0014 186 ARG B C   
2760 O O   . ARG B 160 ? 0.3075 0.2848 0.2734 0.0241  -0.0360 0.0007  186 ARG B O   
2761 C CB  . ARG B 160 ? 0.3348 0.2971 0.2777 0.0139  -0.0291 0.0023  186 ARG B CB  
2762 C CG  . ARG B 160 ? 0.3840 0.3476 0.3235 0.0088  -0.0261 0.0051  186 ARG B CG  
2763 C CD  . ARG B 160 ? 0.4162 0.3692 0.3479 0.0034  -0.0317 0.0084  186 ARG B CD  
2764 N NE  . ARG B 160 ? 0.4522 0.3939 0.3733 -0.0017 -0.0339 0.0099  186 ARG B NE  
2765 C CZ  . ARG B 160 ? 0.4658 0.4045 0.3776 -0.0082 -0.0294 0.0110  186 ARG B CZ  
2766 N NH1 . ARG B 160 ? 0.4379 0.3827 0.3497 -0.0096 -0.0230 0.0102  186 ARG B NH1 
2767 N NH2 . ARG B 160 ? 0.4639 0.3938 0.3668 -0.0135 -0.0312 0.0127  186 ARG B NH2 
2768 N N   . LEU B 161 ? 0.2988 0.2795 0.2653 0.0309  -0.0313 -0.0059 187 LEU B N   
2769 C CA  . LEU B 161 ? 0.3006 0.2962 0.2785 0.0362  -0.0279 -0.0086 187 LEU B CA  
2770 C C   . LEU B 161 ? 0.2945 0.2912 0.2832 0.0431  -0.0344 -0.0120 187 LEU B C   
2771 O O   . LEU B 161 ? 0.2950 0.3058 0.2953 0.0472  -0.0318 -0.0142 187 LEU B O   
2772 C CB  . LEU B 161 ? 0.3085 0.3132 0.2860 0.0387  -0.0205 -0.0118 187 LEU B CB  
2773 C CG  . LEU B 161 ? 0.3262 0.3389 0.3015 0.0340  -0.0135 -0.0085 187 LEU B CG  
2774 C CD1 . LEU B 161 ? 0.3299 0.3330 0.2965 0.0272  -0.0138 -0.0043 187 LEU B CD1 
2775 C CD2 . LEU B 161 ? 0.3389 0.3580 0.3118 0.0360  -0.0080 -0.0112 187 LEU B CD2 
2776 N N   . GLY B 162 ? 0.2890 0.2713 0.2744 0.0437  -0.0430 -0.0120 188 GLY B N   
2777 C CA  . GLY B 162 ? 0.3073 0.2881 0.3033 0.0505  -0.0511 -0.0152 188 GLY B CA  
2778 C C   . GLY B 162 ? 0.3293 0.3172 0.3337 0.0601  -0.0492 -0.0233 188 GLY B C   
2779 O O   . GLY B 162 ? 0.3153 0.3095 0.3335 0.0674  -0.0528 -0.0274 188 GLY B O   
2780 N N   . LEU B 163 ? 0.3521 0.3396 0.3486 0.0602  -0.0437 -0.0261 189 LEU B N   
2781 C CA  . LEU B 163 ? 0.3753 0.3691 0.3762 0.0686  -0.0407 -0.0345 189 LEU B CA  
2782 C C   . LEU B 163 ? 0.3997 0.3816 0.4048 0.0759  -0.0505 -0.0399 189 LEU B C   
2783 O O   . LEU B 163 ? 0.4130 0.3775 0.4123 0.0724  -0.0599 -0.0360 189 LEU B O   
2784 C CB  . LEU B 163 ? 0.3874 0.3792 0.3760 0.0655  -0.0348 -0.0352 189 LEU B CB  
2785 C CG  . LEU B 163 ? 0.4146 0.4182 0.3996 0.0599  -0.0253 -0.0312 189 LEU B CG  
2786 C CD1 . LEU B 163 ? 0.4323 0.4315 0.4060 0.0572  -0.0221 -0.0317 189 LEU B CD1 
2787 C CD2 . LEU B 163 ? 0.4209 0.4438 0.4155 0.0639  -0.0181 -0.0343 189 LEU B CD2 
2788 N N   . PRO B 164 ? 0.4015 0.3923 0.4164 0.0859  -0.0488 -0.0490 190 PRO B N   
2789 C CA  . PRO B 164 ? 0.4095 0.3876 0.4289 0.0940  -0.0589 -0.0552 190 PRO B CA  
2790 C C   . PRO B 164 ? 0.4218 0.3791 0.4259 0.0904  -0.0645 -0.0544 190 PRO B C   
2791 O O   . PRO B 164 ? 0.4331 0.3918 0.4277 0.0886  -0.0583 -0.0562 190 PRO B O   
2792 C CB  . PRO B 164 ? 0.4078 0.4020 0.4379 0.1047  -0.0523 -0.0663 190 PRO B CB  
2793 C CG  . PRO B 164 ? 0.4071 0.4242 0.4425 0.1017  -0.0405 -0.0640 190 PRO B CG  
2794 C CD  . PRO B 164 ? 0.3891 0.4013 0.4102 0.0900  -0.0374 -0.0543 190 PRO B CD  
2795 N N   . PRO B 165 ? 0.4183 0.3563 0.4194 0.0879  -0.0767 -0.0504 191 PRO B N   
2796 C CA  . PRO B 165 ? 0.4223 0.3407 0.4087 0.0823  -0.0824 -0.0478 191 PRO B CA  
2797 C C   . PRO B 165 ? 0.4071 0.3188 0.3908 0.0891  -0.0840 -0.0568 191 PRO B C   
2798 O O   . PRO B 165 ? 0.4097 0.3128 0.3811 0.0833  -0.0837 -0.0549 191 PRO B O   
2799 C CB  . PRO B 165 ? 0.4404 0.3404 0.4259 0.0790  -0.0960 -0.0420 191 PRO B CB  
2800 C CG  . PRO B 165 ? 0.4436 0.3553 0.4387 0.0783  -0.0946 -0.0380 191 PRO B CG  
2801 C CD  . PRO B 165 ? 0.4124 0.3450 0.4223 0.0886  -0.0865 -0.0467 191 PRO B CD  
2802 N N   . LYS B 166 ? 0.3852 0.3010 0.3804 0.1012  -0.0860 -0.0668 192 LYS B N   
2803 C CA  . LYS B 166 ? 0.3963 0.3050 0.3881 0.1084  -0.0878 -0.0767 192 LYS B CA  
2804 C C   . LYS B 166 ? 0.3914 0.3143 0.3762 0.1079  -0.0747 -0.0806 192 LYS B C   
2805 O O   . LYS B 166 ? 0.4064 0.3200 0.3818 0.1092  -0.0762 -0.0857 192 LYS B O   
2806 C CB  . LYS B 166 ? 0.4124 0.3228 0.4196 0.1226  -0.0928 -0.0877 192 LYS B CB  
2807 C CG  . LYS B 166 ? 0.4681 0.3528 0.4742 0.1267  -0.1088 -0.0907 192 LYS B CG  
2808 C CD  . LYS B 166 ? 0.5230 0.4105 0.5482 0.1412  -0.1148 -0.1009 192 LYS B CD  
2809 C CE  . LYS B 166 ? 0.5881 0.4626 0.6213 0.1401  -0.1290 -0.0940 192 LYS B CE  
2810 N NZ  . LYS B 166 ? 0.6180 0.4990 0.6734 0.1545  -0.1343 -0.1035 192 LYS B NZ  
2811 N N   . ILE B 167 ? 0.3738 0.3182 0.3627 0.1060  -0.0629 -0.0784 193 ILE B N   
2812 C CA  . ILE B 167 ? 0.3729 0.3308 0.3547 0.1049  -0.0512 -0.0813 193 ILE B CA  
2813 C C   . ILE B 167 ? 0.3634 0.3171 0.3322 0.0931  -0.0487 -0.0718 193 ILE B C   
2814 O O   . ILE B 167 ? 0.3666 0.3239 0.3369 0.0861  -0.0472 -0.0631 193 ILE B O   
2815 C CB  . ILE B 167 ? 0.3807 0.3636 0.3736 0.1083  -0.0402 -0.0834 193 ILE B CB  
2816 C CG1 . ILE B 167 ? 0.3980 0.3876 0.4066 0.1210  -0.0421 -0.0941 193 ILE B CG1 
2817 C CG2 . ILE B 167 ? 0.3852 0.3813 0.3687 0.1053  -0.0285 -0.0845 193 ILE B CG2 
2818 C CD1 . ILE B 167 ? 0.4226 0.4039 0.4269 0.1303  -0.0445 -0.1066 193 ILE B CD1 
2819 N N   . VAL B 168 ? 0.3484 0.2942 0.3051 0.0910  -0.0489 -0.0739 194 VAL B N   
2820 C CA  . VAL B 168 ? 0.3460 0.2882 0.2927 0.0804  -0.0475 -0.0655 194 VAL B CA  
2821 C C   . VAL B 168 ? 0.3228 0.2824 0.2677 0.0762  -0.0362 -0.0620 194 VAL B C   
2822 O O   . VAL B 168 ? 0.3140 0.2878 0.2610 0.0809  -0.0287 -0.0670 194 VAL B O   
2823 C CB  . VAL B 168 ? 0.3720 0.2985 0.3075 0.0787  -0.0534 -0.0681 194 VAL B CB  
2824 C CG1 . VAL B 168 ? 0.3855 0.2921 0.3217 0.0813  -0.0659 -0.0702 194 VAL B CG1 
2825 C CG2 . VAL B 168 ? 0.3858 0.3188 0.3153 0.0840  -0.0481 -0.0768 194 VAL B CG2 
2826 N N   . ILE B 169 ? 0.3066 0.2646 0.2474 0.0671  -0.0353 -0.0533 195 ILE B N   
2827 C CA  . ILE B 169 ? 0.2940 0.2637 0.2314 0.0621  -0.0272 -0.0493 195 ILE B CA  
2828 C C   . ILE B 169 ? 0.2842 0.2446 0.2118 0.0575  -0.0300 -0.0482 195 ILE B C   
2829 O O   . ILE B 169 ? 0.2824 0.2287 0.2077 0.0551  -0.0376 -0.0472 195 ILE B O   
2830 C CB  . ILE B 169 ? 0.2941 0.2710 0.2366 0.0564  -0.0236 -0.0411 195 ILE B CB  
2831 C CG1 . ILE B 169 ? 0.3078 0.2728 0.2486 0.0497  -0.0290 -0.0349 195 ILE B CG1 
2832 C CG2 . ILE B 169 ? 0.2851 0.2721 0.2378 0.0609  -0.0213 -0.0425 195 ILE B CG2 
2833 C CD1 . ILE B 169 ? 0.3214 0.2931 0.2646 0.0432  -0.0245 -0.0275 195 ILE B CD1 
2834 N N   . GLY B 170 ? 0.2712 0.2388 0.1929 0.0564  -0.0250 -0.0489 196 GLY B N   
2835 C CA  . GLY B 170 ? 0.2728 0.2324 0.1861 0.0523  -0.0285 -0.0482 196 GLY B CA  
2836 C C   . GLY B 170 ? 0.2564 0.2210 0.1698 0.0449  -0.0257 -0.0406 196 GLY B C   
2837 O O   . GLY B 170 ? 0.2523 0.2280 0.1689 0.0437  -0.0196 -0.0372 196 GLY B O   
2838 N N   . TYR B 171 ? 0.2445 0.2009 0.1552 0.0400  -0.0306 -0.0381 197 TYR B N   
2839 C CA  . TYR B 171 ? 0.2410 0.2022 0.1534 0.0339  -0.0286 -0.0320 197 TYR B CA  
2840 C C   . TYR B 171 ? 0.2642 0.2241 0.1686 0.0336  -0.0307 -0.0342 197 TYR B C   
2841 O O   . TYR B 171 ? 0.2837 0.2336 0.1834 0.0338  -0.0369 -0.0375 197 TYR B O   
2842 C CB  . TYR B 171 ? 0.2317 0.1869 0.1489 0.0278  -0.0322 -0.0272 197 TYR B CB  
2843 C CG  . TYR B 171 ? 0.2321 0.1935 0.1536 0.0224  -0.0300 -0.0219 197 TYR B CG  
2844 C CD1 . TYR B 171 ? 0.2394 0.1987 0.1596 0.0195  -0.0338 -0.0214 197 TYR B CD1 
2845 C CD2 . TYR B 171 ? 0.2262 0.1952 0.1538 0.0205  -0.0246 -0.0178 197 TYR B CD2 
2846 C CE1 . TYR B 171 ? 0.2296 0.1952 0.1562 0.0153  -0.0324 -0.0171 197 TYR B CE1 
2847 C CE2 . TYR B 171 ? 0.2249 0.1993 0.1578 0.0165  -0.0229 -0.0139 197 TYR B CE2 
2848 C CZ  . TYR B 171 ? 0.2254 0.1985 0.1586 0.0142  -0.0268 -0.0136 197 TYR B CZ  
2849 O OH  . TYR B 171 ? 0.2137 0.1927 0.1545 0.0111  -0.0258 -0.0104 197 TYR B OH  
2850 N N   . GLN B 172 ? 0.2641 0.2329 0.1662 0.0328  -0.0264 -0.0322 198 GLN B N   
2851 C CA  . GLN B 172 ? 0.2794 0.2464 0.1725 0.0317  -0.0291 -0.0335 198 GLN B CA  
2852 C C   . GLN B 172 ? 0.2564 0.2259 0.1542 0.0260  -0.0307 -0.0269 198 GLN B C   
2853 O O   . GLN B 172 ? 0.2341 0.2111 0.1385 0.0245  -0.0264 -0.0223 198 GLN B O   
2854 C CB  . GLN B 172 ? 0.3153 0.2900 0.2000 0.0345  -0.0238 -0.0361 198 GLN B CB  
2855 C CG  . GLN B 172 ? 0.4078 0.3829 0.2889 0.0411  -0.0211 -0.0439 198 GLN B CG  
2856 C CD  . GLN B 172 ? 0.5376 0.5206 0.4081 0.0427  -0.0158 -0.0471 198 GLN B CD  
2857 O OE1 . GLN B 172 ? 0.5700 0.5645 0.4435 0.0442  -0.0086 -0.0467 198 GLN B OE1 
2858 N NE2 . GLN B 172 ? 0.5559 0.5331 0.4133 0.0415  -0.0194 -0.0497 198 GLN B NE2 
2859 N N   . SER B 173 ? 0.2544 0.2178 0.1498 0.0231  -0.0372 -0.0267 199 SER B N   
2860 C CA  . SER B 173 ? 0.2595 0.2262 0.1608 0.0185  -0.0395 -0.0210 199 SER B CA  
2861 C C   . SER B 173 ? 0.2449 0.2172 0.1393 0.0187  -0.0372 -0.0191 199 SER B C   
2862 O O   . SER B 173 ? 0.2426 0.2139 0.1243 0.0211  -0.0361 -0.0230 199 SER B O   
2863 C CB  . SER B 173 ? 0.3000 0.2590 0.1993 0.0156  -0.0481 -0.0217 199 SER B CB  
2864 O OG  . SER B 173 ? 0.3782 0.3416 0.2858 0.0117  -0.0507 -0.0165 199 SER B OG  
2865 N N   . HIS B 174 ? 0.2328 0.2106 0.1350 0.0161  -0.0366 -0.0134 200 HIS B N   
2866 C CA  . HIS B 174 ? 0.2343 0.2155 0.1294 0.0151  -0.0361 -0.0104 200 HIS B CA  
2867 C C   . HIS B 174 ? 0.2549 0.2300 0.1390 0.0132  -0.0436 -0.0110 200 HIS B C   
2868 O O   . HIS B 174 ? 0.2655 0.2410 0.1365 0.0126  -0.0430 -0.0106 200 HIS B O   
2869 C CB  . HIS B 174 ? 0.2239 0.2101 0.1307 0.0131  -0.0356 -0.0042 200 HIS B CB  
2870 C CG  . HIS B 174 ? 0.2060 0.1973 0.1219 0.0144  -0.0289 -0.0035 200 HIS B CG  
2871 N ND1 . HIS B 174 ? 0.2195 0.2138 0.1302 0.0167  -0.0228 -0.0057 200 HIS B ND1 
2872 C CD2 . HIS B 174 ? 0.2081 0.2020 0.1375 0.0136  -0.0276 -0.0014 200 HIS B CD2 
2873 C CE1 . HIS B 174 ? 0.2210 0.2184 0.1414 0.0169  -0.0190 -0.0042 200 HIS B CE1 
2874 N NE2 . HIS B 174 ? 0.2173 0.2143 0.1481 0.0151  -0.0213 -0.0019 200 HIS B NE2 
2875 N N   . ALA B 175 ? 0.2625 0.2320 0.1510 0.0116  -0.0506 -0.0117 201 ALA B N   
2876 C CA  . ALA B 175 ? 0.2970 0.2595 0.1752 0.0094  -0.0591 -0.0124 201 ALA B CA  
2877 C C   . ALA B 175 ? 0.3295 0.2865 0.1890 0.0119  -0.0579 -0.0192 201 ALA B C   
2878 O O   . ALA B 175 ? 0.3409 0.2946 0.1851 0.0105  -0.0610 -0.0196 201 ALA B O   
2879 C CB  . ALA B 175 ? 0.2936 0.2521 0.1824 0.0070  -0.0664 -0.0123 201 ALA B CB  
2880 N N   . ASP B 176 ? 0.3287 0.2846 0.1888 0.0158  -0.0533 -0.0246 202 ASP B N   
2881 C CA  . ASP B 176 ? 0.3470 0.2986 0.1913 0.0196  -0.0514 -0.0324 202 ASP B CA  
2882 C C   . ASP B 176 ? 0.3602 0.3207 0.1962 0.0213  -0.0428 -0.0327 202 ASP B C   
2883 O O   . ASP B 176 ? 0.3717 0.3307 0.1911 0.0225  -0.0416 -0.0376 202 ASP B O   
2884 C CB  . ASP B 176 ? 0.3716 0.3186 0.2207 0.0237  -0.0505 -0.0382 202 ASP B CB  
2885 C CG  . ASP B 176 ? 0.4378 0.3743 0.2913 0.0213  -0.0596 -0.0386 202 ASP B CG  
2886 O OD1 . ASP B 176 ? 0.4744 0.4057 0.3229 0.0176  -0.0671 -0.0373 202 ASP B OD1 
2887 O OD2 . ASP B 176 ? 0.4543 0.3877 0.3161 0.0224  -0.0597 -0.0397 202 ASP B OD2 
2888 N N   . THR B 177 ? 0.3528 0.3226 0.1999 0.0210  -0.0367 -0.0277 203 THR B N   
2889 C CA  . THR B 177 ? 0.3651 0.3443 0.2060 0.0215  -0.0288 -0.0270 203 THR B CA  
2890 C C   . THR B 177 ? 0.3943 0.3729 0.2217 0.0166  -0.0316 -0.0227 203 THR B C   
2891 O O   . THR B 177 ? 0.4026 0.3842 0.2148 0.0165  -0.0275 -0.0255 203 THR B O   
2892 C CB  . THR B 177 ? 0.3653 0.3528 0.2208 0.0213  -0.0234 -0.0219 203 THR B CB  
2893 O OG1 . THR B 177 ? 0.3693 0.3556 0.2366 0.0247  -0.0224 -0.0247 203 THR B OG1 
2894 C CG2 . THR B 177 ? 0.3671 0.3647 0.2175 0.0213  -0.0153 -0.0212 203 THR B CG2 
2895 N N   . ALA B 178 ? 0.4092 0.3838 0.2421 0.0125  -0.0392 -0.0163 204 ALA B N   
2896 C CA  . ALA B 178 ? 0.4386 0.4107 0.2608 0.0074  -0.0447 -0.0108 204 ALA B CA  
2897 C C   . ALA B 178 ? 0.4928 0.4562 0.2955 0.0059  -0.0507 -0.0148 204 ALA B C   
2898 O O   . ALA B 178 ? 0.5002 0.4614 0.2891 0.0013  -0.0543 -0.0108 204 ALA B O   
2899 C CB  . ALA B 178 ? 0.4242 0.3944 0.2615 0.0048  -0.0521 -0.0037 204 ALA B CB  
2900 N N   . THR B 179 ? 0.5265 0.4834 0.3280 0.0091  -0.0533 -0.0221 205 THR B N   
2901 C CA  . THR B 179 ? 0.5773 0.5243 0.3599 0.0080  -0.0598 -0.0269 205 THR B CA  
2902 C C   . THR B 179 ? 0.6259 0.5722 0.3952 0.0130  -0.0532 -0.0376 205 THR B C   
2903 O O   . THR B 179 ? 0.6286 0.5649 0.3866 0.0141  -0.0586 -0.0443 205 THR B O   
2904 C CB  . THR B 179 ? 0.5938 0.5313 0.3846 0.0063  -0.0713 -0.0262 205 THR B CB  
2905 O OG1 . THR B 179 ? 0.6025 0.5391 0.4069 0.0102  -0.0696 -0.0304 205 THR B OG1 
2906 C CG2 . THR B 179 ? 0.5932 0.5327 0.3981 0.0020  -0.0779 -0.0167 205 THR B CG2 
2907 N N   . LYS B 180 ? 0.6612 0.6185 0.4324 0.0161  -0.0419 -0.0395 206 LYS B N   
2908 C CA  . LYS B 180 ? 0.7039 0.6651 0.4675 0.0221  -0.0334 -0.0496 206 LYS B CA  
2909 C C   . LYS B 180 ? 0.7504 0.7075 0.4880 0.0215  -0.0331 -0.0566 206 LYS B C   
2910 O O   . LYS B 180 ? 0.7611 0.7159 0.4837 0.0151  -0.0366 -0.0516 206 LYS B O   
2911 C CB  . LYS B 180 ? 0.7307 0.7073 0.5027 0.0231  -0.0221 -0.0469 206 LYS B CB  
2912 C CG  . LYS B 180 ? 0.7970 0.7810 0.5696 0.0303  -0.0128 -0.0567 206 LYS B CG  
2913 C CD  . LYS B 180 ? 0.8531 0.8536 0.6273 0.0288  -0.0019 -0.0535 206 LYS B CD  
2914 C CE  . LYS B 180 ? 0.9021 0.9122 0.6710 0.0347  0.0080  -0.0642 206 LYS B CE  
2915 N NZ  . LYS B 180 ? 0.9226 0.9348 0.7100 0.0429  0.0100  -0.0700 206 LYS B NZ  
2916 N N   . SER B 181 ? 0.7727 0.7281 0.5044 0.0283  -0.0292 -0.0685 207 SER B N   
2917 C CA  . SER B 181 ? 0.8045 0.7566 0.5112 0.0291  -0.0272 -0.0776 207 SER B CA  
2918 C C   . SER B 181 ? 0.8185 0.7816 0.5242 0.0368  -0.0147 -0.0886 207 SER B C   
2919 O O   . SER B 181 ? 0.8308 0.7898 0.5190 0.0403  -0.0130 -0.0997 207 SER B O   
2920 C CB  . SER B 181 ? 0.8368 0.7706 0.5340 0.0300  -0.0388 -0.0835 207 SER B CB  
2921 O OG  . SER B 181 ? 0.8781 0.8032 0.5721 0.0222  -0.0501 -0.0743 207 SER B OG  
2922 N N   . GLY B 182 ? 0.8136 0.7904 0.5380 0.0396  -0.0066 -0.0860 208 GLY B N   
2923 C CA  . GLY B 182 ? 0.8201 0.8096 0.5479 0.0470  0.0050  -0.0958 208 GLY B CA  
2924 C C   . GLY B 182 ? 0.8239 0.8119 0.5736 0.0554  0.0039  -0.1003 208 GLY B C   
2925 O O   . GLY B 182 ? 0.8194 0.8176 0.5877 0.0560  0.0080  -0.0949 208 GLY B O   
2926 N N   . THR B 185 ? 0.6213 0.5835 0.4278 0.0561  -0.0199 -0.0839 211 THR B N   
2927 C CA  . THR B 185 ? 0.6201 0.5889 0.4462 0.0570  -0.0173 -0.0786 211 THR B CA  
2928 C C   . THR B 185 ? 0.5995 0.5545 0.4353 0.0577  -0.0264 -0.0779 211 THR B C   
2929 O O   . THR B 185 ? 0.6098 0.5629 0.4545 0.0634  -0.0267 -0.0823 211 THR B O   
2930 C CB  . THR B 185 ? 0.6501 0.6317 0.4816 0.0640  -0.0081 -0.0852 211 THR B CB  
2931 O OG1 . THR B 185 ? 0.6744 0.6476 0.5025 0.0721  -0.0107 -0.0971 211 THR B OG1 
2932 C CG2 . THR B 185 ? 0.6592 0.6559 0.4809 0.0618  0.0017  -0.0850 211 THR B CG2 
2933 N N   . LYS B 186 ? 0.5688 0.5163 0.4061 0.0528  -0.0328 -0.0727 212 LYS B N   
2934 C CA  . LYS B 186 ? 0.5522 0.4843 0.3926 0.0515  -0.0429 -0.0728 212 LYS B CA  
2935 C C   . LYS B 186 ? 0.5136 0.4453 0.3697 0.0484  -0.0446 -0.0654 212 LYS B C   
2936 O O   . LYS B 186 ? 0.5167 0.4549 0.3794 0.0427  -0.0430 -0.0569 212 LYS B O   
2937 C CB  . LYS B 186 ? 0.5907 0.5142 0.4214 0.0457  -0.0504 -0.0707 212 LYS B CB  
2938 C CG  . LYS B 186 ? 0.6688 0.5868 0.4807 0.0486  -0.0516 -0.0795 212 LYS B CG  
2939 C CD  . LYS B 186 ? 0.7380 0.6470 0.5409 0.0421  -0.0606 -0.0764 212 LYS B CD  
2940 C CE  . LYS B 186 ? 0.7953 0.6971 0.5769 0.0441  -0.0627 -0.0852 212 LYS B CE  
2941 N NZ  . LYS B 186 ? 0.8288 0.7215 0.6022 0.0371  -0.0727 -0.0813 212 LYS B NZ  
2942 N N   . ASN B 187 ? 0.4700 0.4011 0.3356 0.0499  -0.0445 -0.0643 213 ASN B N   
2943 C CA  . ASN B 187 ? 0.4343 0.3669 0.3126 0.0465  -0.0445 -0.0572 213 ASN B CA  
2944 C C   . ASN B 187 ? 0.4118 0.3321 0.2920 0.0408  -0.0532 -0.0537 213 ASN B C   
2945 O O   . ASN B 187 ? 0.4107 0.3177 0.2868 0.0429  -0.0604 -0.0587 213 ASN B O   
2946 C CB  . ASN B 187 ? 0.4192 0.3517 0.3040 0.0526  -0.0431 -0.0609 213 ASN B CB  
2947 C CG  . ASN B 187 ? 0.4093 0.3569 0.2967 0.0571  -0.0339 -0.0628 213 ASN B CG  
2948 O OD1 . ASN B 187 ? 0.3924 0.3514 0.2809 0.0534  -0.0278 -0.0573 213 ASN B OD1 
2949 N ND2 . ASN B 187 ? 0.4028 0.3508 0.2922 0.0650  -0.0330 -0.0705 213 ASN B ND2 
2950 N N   . ARG B 188 ? 0.3826 0.3076 0.2696 0.0336  -0.0526 -0.0454 214 ARG B N   
2951 C CA  . ARG B 188 ? 0.3734 0.2903 0.2645 0.0268  -0.0593 -0.0411 214 ARG B CA  
2952 C C   . ARG B 188 ? 0.3594 0.2690 0.2553 0.0267  -0.0618 -0.0402 214 ARG B C   
2953 O O   . ARG B 188 ? 0.3639 0.2612 0.2589 0.0231  -0.0697 -0.0398 214 ARG B O   
2954 C CB  . ARG B 188 ? 0.3968 0.3240 0.2966 0.0203  -0.0559 -0.0332 214 ARG B CB  
2955 C CG  . ARG B 188 ? 0.4683 0.4020 0.3654 0.0193  -0.0552 -0.0322 214 ARG B CG  
2956 C CD  . ARG B 188 ? 0.5303 0.4547 0.4215 0.0165  -0.0640 -0.0340 214 ARG B CD  
2957 N NE  . ARG B 188 ? 0.5708 0.5005 0.4593 0.0149  -0.0647 -0.0321 214 ARG B NE  
2958 C CZ  . ARG B 188 ? 0.6143 0.5474 0.5113 0.0092  -0.0682 -0.0270 214 ARG B CZ  
2959 N NH1 . ARG B 188 ? 0.6250 0.5583 0.5335 0.0043  -0.0700 -0.0234 214 ARG B NH1 
2960 N NH2 . ARG B 188 ? 0.6060 0.5426 0.5000 0.0082  -0.0702 -0.0253 214 ARG B NH2 
2961 N N   . PHE B 189 ? 0.3407 0.2574 0.2416 0.0295  -0.0558 -0.0391 215 PHE B N   
2962 C CA  . PHE B 189 ? 0.3344 0.2446 0.2393 0.0292  -0.0583 -0.0375 215 PHE B CA  
2963 C C   . PHE B 189 ? 0.3252 0.2403 0.2318 0.0371  -0.0542 -0.0416 215 PHE B C   
2964 O O   . PHE B 189 ? 0.3114 0.2387 0.2183 0.0405  -0.0471 -0.0431 215 PHE B O   
2965 C CB  . PHE B 189 ? 0.3342 0.2497 0.2458 0.0215  -0.0551 -0.0292 215 PHE B CB  
2966 C CG  . PHE B 189 ? 0.3539 0.2722 0.2681 0.0137  -0.0555 -0.0245 215 PHE B CG  
2967 C CD1 . PHE B 189 ? 0.3747 0.2830 0.2882 0.0075  -0.0627 -0.0225 215 PHE B CD1 
2968 C CD2 . PHE B 189 ? 0.3616 0.2929 0.2801 0.0124  -0.0491 -0.0219 215 PHE B CD2 
2969 C CE1 . PHE B 189 ? 0.3832 0.2963 0.3015 0.0004  -0.0629 -0.0184 215 PHE B CE1 
2970 C CE2 . PHE B 189 ? 0.3696 0.3046 0.2931 0.0060  -0.0499 -0.0182 215 PHE B CE2 
2971 C CZ  . PHE B 189 ? 0.3685 0.2955 0.2926 0.0001  -0.0563 -0.0166 215 PHE B CZ  
2972 N N   . VAL B 190 ? 0.3299 0.2356 0.2383 0.0395  -0.0593 -0.0429 216 VAL B N   
2973 C CA  . VAL B 190 ? 0.3442 0.2550 0.2573 0.0469  -0.0566 -0.0464 216 VAL B CA  
2974 C C   . VAL B 190 ? 0.3592 0.2644 0.2769 0.0434  -0.0600 -0.0407 216 VAL B C   
2975 O O   . VAL B 190 ? 0.3680 0.2607 0.2831 0.0373  -0.0669 -0.0368 216 VAL B O   
2976 C CB  . VAL B 190 ? 0.3589 0.2629 0.2696 0.0566  -0.0607 -0.0566 216 VAL B CB  
2977 C CG1 . VAL B 190 ? 0.3646 0.2771 0.2693 0.0606  -0.0550 -0.0627 216 VAL B CG1 
2978 C CG2 . VAL B 190 ? 0.3756 0.2592 0.2820 0.0554  -0.0725 -0.0582 216 VAL B CG2 
2979 N N   . VAL B 191 ? 0.3595 0.2734 0.2835 0.0468  -0.0559 -0.0402 217 VAL B N   
2980 C CA  . VAL B 191 ? 0.3689 0.2764 0.2960 0.0441  -0.0604 -0.0355 217 VAL B CA  
2981 C C   . VAL B 191 ? 0.3646 0.2764 0.2994 0.0527  -0.0608 -0.0397 217 VAL B C   
2982 O O   . VAL B 191 ? 0.3685 0.2705 0.3060 0.0532  -0.0683 -0.0382 217 VAL B O   
2983 C CB  . VAL B 191 ? 0.3841 0.2972 0.3110 0.0351  -0.0556 -0.0271 217 VAL B CB  
2984 C CG1 . VAL B 191 ? 0.3828 0.3131 0.3142 0.0370  -0.0458 -0.0268 217 VAL B CG1 
2985 C CG2 . VAL B 191 ? 0.4040 0.3079 0.3308 0.0313  -0.0613 -0.0222 217 VAL B CG2 
2986 O OXT . VAL B 191 ? 0.3546 0.2803 0.2934 0.0585  -0.0537 -0.0443 217 VAL B OXT 
# 
