data_8V0D
# 
_entry.id   8V0D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8V0D         pdb_00008v0d 10.2210/pdb8v0d/pdb 
WWPDB D_1000279159 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-27 
# 
_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                        8V0D 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-17 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              stephen_blacklow@hms.harvard.edu 
_pdbx_contact_author.name_first         Stephen 
_pdbx_contact_author.name_last          Blacklow 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6904-1981 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cao, R.'        1 ? 
'Blacklow, S.C.' 2 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Ubch5b-RING3 fusion structure' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cao, R.'        1 ? 
primary 'Blacklow, S.C.' 2 ? 
# 
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 'Ubch5B-RING3 of MIB1 fusion protein' 26212.041 2  2.3.2.23,2.3.2.24,2.3.2.27 ? ? ? 
2 non-polymer syn 'ZINC ION'                            65.409    5  ?                          ? ? ? 
3 water       nat water                                 18.015    39 ?                          ? ? ? 
# 
_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       
;SMALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNIN
SNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAMGGGSGGGSGGGS
GGGSGGKDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNIN
SNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAMGGGSGGGSGGGS
GGGSGGKDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY
;
_entity_poly.pdbx_strand_id                 B,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   ALA n 
1 4   LEU n 
1 5   LYS n 
1 6   ARG n 
1 7   ILE n 
1 8   HIS n 
1 9   LYS n 
1 10  GLU n 
1 11  LEU n 
1 12  ASN n 
1 13  ASP n 
1 14  LEU n 
1 15  ALA n 
1 16  ARG n 
1 17  ASP n 
1 18  PRO n 
1 19  PRO n 
1 20  ALA n 
1 21  GLN n 
1 22  CYS n 
1 23  SER n 
1 24  ALA n 
1 25  GLY n 
1 26  PRO n 
1 27  VAL n 
1 28  GLY n 
1 29  ASP n 
1 30  ASP n 
1 31  MET n 
1 32  PHE n 
1 33  HIS n 
1 34  TRP n 
1 35  GLN n 
1 36  ALA n 
1 37  THR n 
1 38  ILE n 
1 39  MET n 
1 40  GLY n 
1 41  PRO n 
1 42  ASN n 
1 43  ASP n 
1 44  SER n 
1 45  PRO n 
1 46  TYR n 
1 47  GLN n 
1 48  GLY n 
1 49  GLY n 
1 50  VAL n 
1 51  PHE n 
1 52  PHE n 
1 53  LEU n 
1 54  THR n 
1 55  ILE n 
1 56  HIS n 
1 57  PHE n 
1 58  PRO n 
1 59  THR n 
1 60  ASP n 
1 61  TYR n 
1 62  PRO n 
1 63  PHE n 
1 64  LYS n 
1 65  PRO n 
1 66  PRO n 
1 67  LYS n 
1 68  VAL n 
1 69  ALA n 
1 70  PHE n 
1 71  THR n 
1 72  THR n 
1 73  ARG n 
1 74  ILE n 
1 75  TYR n 
1 76  HIS n 
1 77  PRO n 
1 78  ASN n 
1 79  ILE n 
1 80  ASN n 
1 81  SER n 
1 82  ASN n 
1 83  GLY n 
1 84  SER n 
1 85  ILE n 
1 86  CYS n 
1 87  LEU n 
1 88  ASP n 
1 89  ILE n 
1 90  LEU n 
1 91  ARG n 
1 92  SER n 
1 93  GLN n 
1 94  TRP n 
1 95  SER n 
1 96  PRO n 
1 97  ALA n 
1 98  LEU n 
1 99  THR n 
1 100 ILE n 
1 101 SER n 
1 102 LYS n 
1 103 VAL n 
1 104 LEU n 
1 105 LEU n 
1 106 SER n 
1 107 ILE n 
1 108 CYS n 
1 109 SER n 
1 110 LEU n 
1 111 LEU n 
1 112 CYS n 
1 113 ASP n 
1 114 PRO n 
1 115 ASN n 
1 116 PRO n 
1 117 ASP n 
1 118 ASP n 
1 119 PRO n 
1 120 LEU n 
1 121 VAL n 
1 122 PRO n 
1 123 GLU n 
1 124 ILE n 
1 125 ALA n 
1 126 ARG n 
1 127 ILE n 
1 128 TYR n 
1 129 LYS n 
1 130 THR n 
1 131 ASP n 
1 132 ARG n 
1 133 GLU n 
1 134 LYS n 
1 135 TYR n 
1 136 ASN n 
1 137 ARG n 
1 138 ILE n 
1 139 ALA n 
1 140 ARG n 
1 141 GLU n 
1 142 TRP n 
1 143 THR n 
1 144 GLN n 
1 145 LYS n 
1 146 TYR n 
1 147 ALA n 
1 148 MET n 
1 149 GLY n 
1 150 GLY n 
1 151 GLY n 
1 152 SER n 
1 153 GLY n 
1 154 GLY n 
1 155 GLY n 
1 156 SER n 
1 157 GLY n 
1 158 GLY n 
1 159 GLY n 
1 160 SER n 
1 161 GLY n 
1 162 GLY n 
1 163 GLY n 
1 164 SER n 
1 165 GLY n 
1 166 GLY n 
1 167 LYS n 
1 168 ASP n 
1 169 LYS n 
1 170 ASP n 
1 171 ASN n 
1 172 THR n 
1 173 ASN n 
1 174 VAL n 
1 175 ASN n 
1 176 ALA n 
1 177 ASP n 
1 178 VAL n 
1 179 GLN n 
1 180 LYS n 
1 181 LEU n 
1 182 GLN n 
1 183 GLN n 
1 184 GLN n 
1 185 LEU n 
1 186 GLN n 
1 187 ASP n 
1 188 ILE n 
1 189 LYS n 
1 190 GLU n 
1 191 GLN n 
1 192 THR n 
1 193 MET n 
1 194 CYS n 
1 195 PRO n 
1 196 VAL n 
1 197 CYS n 
1 198 LEU n 
1 199 ASP n 
1 200 ARG n 
1 201 LEU n 
1 202 LYS n 
1 203 ASN n 
1 204 MET n 
1 205 ILE n 
1 206 PHE n 
1 207 LEU n 
1 208 CYS n 
1 209 GLY n 
1 210 HIS n 
1 211 GLY n 
1 212 THR n 
1 213 CYS n 
1 214 GLN n 
1 215 LEU n 
1 216 CYS n 
1 217 GLY n 
1 218 ASP n 
1 219 ARG n 
1 220 MET n 
1 221 SER n 
1 222 GLU n 
1 223 CYS n 
1 224 PRO n 
1 225 ILE n 
1 226 CYS n 
1 227 ARG n 
1 228 LYS n 
1 229 ALA n 
1 230 ILE n 
1 231 GLU n 
1 232 ARG n 
1 233 ARG n 
1 234 ILE n 
1 235 LEU n 
1 236 LEU n 
1 237 TYR n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1   148 human ? 'UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? 
? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 149 237 human ? 'MIB1, DIP1, KIAA1323, ZZANK2'              ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? 
? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
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   SER 1   0    0    SER SER B . n 
A 1 2   MET 2   1    1    MET MET B . n 
A 1 3   ALA 3   2    2    ALA ALA B . n 
A 1 4   LEU 4   3    3    LEU LEU B . n 
A 1 5   LYS 5   4    4    LYS LYS B . n 
A 1 6   ARG 6   5    5    ARG ARG B . n 
A 1 7   ILE 7   6    6    ILE ILE B . n 
A 1 8   HIS 8   7    7    HIS HIS B . n 
A 1 9   LYS 9   8    8    LYS LYS B . n 
A 1 10  GLU 10  9    9    GLU GLU B . n 
A 1 11  LEU 11  10   10   LEU LEU B . n 
A 1 12  ASN 12  11   11   ASN ASN B . n 
A 1 13  ASP 13  12   12   ASP ASP B . n 
A 1 14  LEU 14  13   13   LEU LEU B . n 
A 1 15  ALA 15  14   14   ALA ALA B . n 
A 1 16  ARG 16  15   15   ARG ARG B . n 
A 1 17  ASP 17  16   16   ASP ASP B . n 
A 1 18  PRO 18  17   17   PRO PRO B . n 
A 1 19  PRO 19  18   18   PRO PRO B . n 
A 1 20  ALA 20  19   19   ALA ALA B . n 
A 1 21  GLN 21  20   20   GLN GLN B . n 
A 1 22  CYS 22  21   21   CYS CYS B . n 
A 1 23  SER 23  22   22   SER SER B . n 
A 1 24  ALA 24  23   23   ALA ALA B . n 
A 1 25  GLY 25  24   24   GLY GLY B . n 
A 1 26  PRO 26  25   25   PRO PRO B . n 
A 1 27  VAL 27  26   26   VAL VAL B . n 
A 1 28  GLY 28  27   27   GLY GLY B . n 
A 1 29  ASP 29  28   28   ASP ASP B . n 
A 1 30  ASP 30  29   29   ASP ASP B . n 
A 1 31  MET 31  30   30   MET MET B . n 
A 1 32  PHE 32  31   31   PHE PHE B . n 
A 1 33  HIS 33  32   32   HIS HIS B . n 
A 1 34  TRP 34  33   33   TRP TRP B . n 
A 1 35  GLN 35  34   34   GLN GLN B . n 
A 1 36  ALA 36  35   35   ALA ALA B . n 
A 1 37  THR 37  36   36   THR THR B . n 
A 1 38  ILE 38  37   37   ILE ILE B . n 
A 1 39  MET 39  38   38   MET MET B . n 
A 1 40  GLY 40  39   39   GLY GLY B . n 
A 1 41  PRO 41  40   40   PRO PRO B . n 
A 1 42  ASN 42  41   41   ASN ASN B . n 
A 1 43  ASP 43  42   42   ASP ASP B . n 
A 1 44  SER 44  43   43   SER SER B . n 
A 1 45  PRO 45  44   44   PRO PRO B . n 
A 1 46  TYR 46  45   45   TYR TYR B . n 
A 1 47  GLN 47  46   46   GLN GLN B . n 
A 1 48  GLY 48  47   47   GLY GLY B . n 
A 1 49  GLY 49  48   48   GLY GLY B . n 
A 1 50  VAL 50  49   49   VAL VAL B . n 
A 1 51  PHE 51  50   50   PHE PHE B . n 
A 1 52  PHE 52  51   51   PHE PHE B . n 
A 1 53  LEU 53  52   52   LEU LEU B . n 
A 1 54  THR 54  53   53   THR THR B . n 
A 1 55  ILE 55  54   54   ILE ILE B . n 
A 1 56  HIS 56  55   55   HIS HIS B . n 
A 1 57  PHE 57  56   56   PHE PHE B . n 
A 1 58  PRO 58  57   57   PRO PRO B . n 
A 1 59  THR 59  58   58   THR THR B . n 
A 1 60  ASP 60  59   59   ASP ASP B . n 
A 1 61  TYR 61  60   60   TYR TYR B . n 
A 1 62  PRO 62  61   61   PRO PRO B . n 
A 1 63  PHE 63  62   62   PHE PHE B . n 
A 1 64  LYS 64  63   63   LYS LYS B . n 
A 1 65  PRO 65  64   64   PRO PRO B . n 
A 1 66  PRO 66  65   65   PRO PRO B . n 
A 1 67  LYS 67  66   66   LYS LYS B . n 
A 1 68  VAL 68  67   67   VAL VAL B . n 
A 1 69  ALA 69  68   68   ALA ALA B . n 
A 1 70  PHE 70  69   69   PHE PHE B . n 
A 1 71  THR 71  70   70   THR THR B . n 
A 1 72  THR 72  71   71   THR THR B . n 
A 1 73  ARG 73  72   72   ARG ARG B . n 
A 1 74  ILE 74  73   73   ILE ILE B . n 
A 1 75  TYR 75  74   74   TYR TYR B . n 
A 1 76  HIS 76  75   75   HIS HIS B . n 
A 1 77  PRO 77  76   76   PRO PRO B . n 
A 1 78  ASN 78  77   77   ASN ASN B . n 
A 1 79  ILE 79  78   78   ILE ILE B . n 
A 1 80  ASN 80  79   79   ASN ASN B . n 
A 1 81  SER 81  80   80   SER SER B . n 
A 1 82  ASN 82  81   81   ASN ASN B . n 
A 1 83  GLY 83  82   82   GLY GLY B . n 
A 1 84  SER 84  83   83   SER SER B . n 
A 1 85  ILE 85  84   84   ILE ILE B . n 
A 1 86  CYS 86  85   85   CYS CYS B . n 
A 1 87  LEU 87  86   86   LEU LEU B . n 
A 1 88  ASP 88  87   87   ASP ASP B . n 
A 1 89  ILE 89  88   88   ILE ILE B . n 
A 1 90  LEU 90  89   89   LEU LEU B . n 
A 1 91  ARG 91  90   90   ARG ARG B . n 
A 1 92  SER 92  91   91   SER SER B . n 
A 1 93  GLN 93  92   92   GLN GLN B . n 
A 1 94  TRP 94  93   93   TRP TRP B . n 
A 1 95  SER 95  94   94   SER SER B . n 
A 1 96  PRO 96  95   95   PRO PRO B . n 
A 1 97  ALA 97  96   96   ALA ALA B . n 
A 1 98  LEU 98  97   97   LEU LEU B . n 
A 1 99  THR 99  98   98   THR THR B . n 
A 1 100 ILE 100 99   99   ILE ILE B . n 
A 1 101 SER 101 100  100  SER SER B . n 
A 1 102 LYS 102 101  101  LYS LYS B . n 
A 1 103 VAL 103 102  102  VAL VAL B . n 
A 1 104 LEU 104 103  103  LEU LEU B . n 
A 1 105 LEU 105 104  104  LEU LEU B . n 
A 1 106 SER 106 105  105  SER SER B . n 
A 1 107 ILE 107 106  106  ILE ILE B . n 
A 1 108 CYS 108 107  107  CYS CYS B . n 
A 1 109 SER 109 108  108  SER SER B . n 
A 1 110 LEU 110 109  109  LEU LEU B . n 
A 1 111 LEU 111 110  110  LEU LEU B . n 
A 1 112 CYS 112 111  111  CYS CYS B . n 
A 1 113 ASP 113 112  112  ASP ASP B . n 
A 1 114 PRO 114 113  113  PRO PRO B . n 
A 1 115 ASN 115 114  114  ASN ASN B . n 
A 1 116 PRO 116 115  115  PRO PRO B . n 
A 1 117 ASP 117 116  116  ASP ASP B . n 
A 1 118 ASP 118 117  117  ASP ASP B . n 
A 1 119 PRO 119 118  118  PRO PRO B . n 
A 1 120 LEU 120 119  119  LEU LEU B . n 
A 1 121 VAL 121 120  120  VAL VAL B . n 
A 1 122 PRO 122 121  121  PRO PRO B . n 
A 1 123 GLU 123 122  122  GLU GLU B . n 
A 1 124 ILE 124 123  123  ILE ILE B . n 
A 1 125 ALA 125 124  124  ALA ALA B . n 
A 1 126 ARG 126 125  125  ARG ARG B . n 
A 1 127 ILE 127 126  126  ILE ILE B . n 
A 1 128 TYR 128 127  127  TYR TYR B . n 
A 1 129 LYS 129 128  128  LYS LYS B . n 
A 1 130 THR 130 129  129  THR THR B . n 
A 1 131 ASP 131 130  130  ASP ASP B . n 
A 1 132 ARG 132 131  131  ARG ARG B . n 
A 1 133 GLU 133 132  132  GLU GLU B . n 
A 1 134 LYS 134 133  133  LYS LYS B . n 
A 1 135 TYR 135 134  134  TYR TYR B . n 
A 1 136 ASN 136 135  135  ASN ASN B . n 
A 1 137 ARG 137 136  136  ARG ARG B . n 
A 1 138 ILE 138 137  137  ILE ILE B . n 
A 1 139 ALA 139 138  138  ALA ALA B . n 
A 1 140 ARG 140 139  139  ARG ARG B . n 
A 1 141 GLU 141 140  140  GLU GLU B . n 
A 1 142 TRP 142 141  141  TRP TRP B . n 
A 1 143 THR 143 142  142  THR THR B . n 
A 1 144 GLN 144 143  143  GLN GLN B . n 
A 1 145 LYS 145 144  144  LYS LYS B . n 
A 1 146 TYR 146 145  145  TYR TYR B . n 
A 1 147 ALA 147 146  146  ALA ALA B . n 
A 1 148 MET 148 147  147  MET MET B . n 
A 1 149 GLY 149 148  148  GLY GLY B . n 
A 1 150 GLY 150 149  ?    ?   ?   B . n 
A 1 151 GLY 151 150  ?    ?   ?   B . n 
A 1 152 SER 152 151  ?    ?   ?   B . n 
A 1 153 GLY 153 152  ?    ?   ?   B . n 
A 1 154 GLY 154 153  ?    ?   ?   B . n 
A 1 155 GLY 155 154  ?    ?   ?   B . n 
A 1 156 SER 156 155  ?    ?   ?   B . n 
A 1 157 GLY 157 156  ?    ?   ?   B . n 
A 1 158 GLY 158 157  ?    ?   ?   B . n 
A 1 159 GLY 159 158  ?    ?   ?   B . n 
A 1 160 SER 160 159  ?    ?   ?   B . n 
A 1 161 GLY 161 160  ?    ?   ?   B . n 
A 1 162 GLY 162 161  ?    ?   ?   B . n 
A 1 163 GLY 163 162  ?    ?   ?   B . n 
A 1 164 SER 164 163  ?    ?   ?   B . n 
A 1 165 GLY 165 164  ?    ?   ?   B . n 
A 1 166 GLY 166 165  ?    ?   ?   B . n 
A 1 167 LYS 167 936  ?    ?   ?   B . n 
A 1 168 ASP 168 937  ?    ?   ?   B . n 
A 1 169 LYS 169 938  ?    ?   ?   B . n 
A 1 170 ASP 170 939  ?    ?   ?   B . n 
A 1 171 ASN 171 940  ?    ?   ?   B . n 
A 1 172 THR 172 941  ?    ?   ?   B . n 
A 1 173 ASN 173 942  ?    ?   ?   B . n 
A 1 174 VAL 174 943  943  VAL VAL B . n 
A 1 175 ASN 175 944  944  ASN ASN B . n 
A 1 176 ALA 176 945  945  ALA ALA B . n 
A 1 177 ASP 177 946  946  ASP ASP B . n 
A 1 178 VAL 178 947  947  VAL VAL B . n 
A 1 179 GLN 179 948  948  GLN GLN B . n 
A 1 180 LYS 180 949  949  LYS LYS B . n 
A 1 181 LEU 181 950  950  LEU LEU B . n 
A 1 182 GLN 182 951  951  GLN GLN B . n 
A 1 183 GLN 183 952  952  GLN GLN B . n 
A 1 184 GLN 184 953  953  GLN GLN B . n 
A 1 185 LEU 185 954  954  LEU LEU B . n 
A 1 186 GLN 186 955  955  GLN GLN B . n 
A 1 187 ASP 187 956  956  ASP ASP B . n 
A 1 188 ILE 188 957  957  ILE ILE B . n 
A 1 189 LYS 189 958  958  LYS LYS B . n 
A 1 190 GLU 190 959  959  GLU GLU B . n 
A 1 191 GLN 191 960  960  GLN GLN B . n 
A 1 192 THR 192 961  961  THR THR B . n 
A 1 193 MET 193 962  962  MET MET B . n 
A 1 194 CYS 194 963  963  CYS CYS B . n 
A 1 195 PRO 195 964  964  PRO PRO B . n 
A 1 196 VAL 196 965  965  VAL VAL B . n 
A 1 197 CYS 197 966  966  CYS CYS B . n 
A 1 198 LEU 198 967  967  LEU LEU B . n 
A 1 199 ASP 199 968  968  ASP ASP B . n 
A 1 200 ARG 200 969  969  ARG ARG B . n 
A 1 201 LEU 201 970  970  LEU LEU B . n 
A 1 202 LYS 202 971  971  LYS LYS B . n 
A 1 203 ASN 203 972  972  ASN ASN B . n 
A 1 204 MET 204 973  973  MET MET B . n 
A 1 205 ILE 205 974  974  ILE ILE B . n 
A 1 206 PHE 206 975  975  PHE PHE B . n 
A 1 207 LEU 207 976  976  LEU LEU B . n 
A 1 208 CYS 208 977  977  CYS CYS B . n 
A 1 209 GLY 209 978  978  GLY GLY B . n 
A 1 210 HIS 210 979  979  HIS HIS B . n 
A 1 211 GLY 211 980  980  GLY GLY B . n 
A 1 212 THR 212 981  981  THR THR B . n 
A 1 213 CYS 213 982  982  CYS CYS B . n 
A 1 214 GLN 214 983  983  GLN GLN B . n 
A 1 215 LEU 215 984  984  LEU LEU B . n 
A 1 216 CYS 216 985  985  CYS CYS B . n 
A 1 217 GLY 217 986  986  GLY GLY B . n 
A 1 218 ASP 218 987  987  ASP ASP B . n 
A 1 219 ARG 219 988  988  ARG ARG B . n 
A 1 220 MET 220 989  989  MET MET B . n 
A 1 221 SER 221 990  990  SER SER B . n 
A 1 222 GLU 222 991  991  GLU GLU B . n 
A 1 223 CYS 223 992  992  CYS CYS B . n 
A 1 224 PRO 224 993  993  PRO PRO B . n 
A 1 225 ILE 225 994  994  ILE ILE B . n 
A 1 226 CYS 226 995  995  CYS CYS B . n 
A 1 227 ARG 227 996  996  ARG ARG B . n 
A 1 228 LYS 228 997  997  LYS LYS B . n 
A 1 229 ALA 229 998  998  ALA ALA B . n 
A 1 230 ILE 230 999  999  ILE ILE B . n 
A 1 231 GLU 231 1000 1000 GLU GLU B . n 
A 1 232 ARG 232 1001 1001 ARG ARG B . n 
A 1 233 ARG 233 1002 1002 ARG ARG B . n 
A 1 234 ILE 234 1003 1003 ILE ILE B . n 
A 1 235 LEU 235 1004 1004 LEU LEU B . n 
A 1 236 LEU 236 1005 1005 LEU LEU B . n 
A 1 237 TYR 237 1006 1006 TYR TYR B . n 
B 1 1   SER 1   0    0    SER SER A . n 
B 1 2   MET 2   1    1    MET MET A . n 
B 1 3   ALA 3   2    2    ALA ALA A . n 
B 1 4   LEU 4   3    3    LEU LEU A . n 
B 1 5   LYS 5   4    4    LYS LYS A . n 
B 1 6   ARG 6   5    5    ARG ARG A . n 
B 1 7   ILE 7   6    6    ILE ILE A . n 
B 1 8   HIS 8   7    7    HIS HIS A . n 
B 1 9   LYS 9   8    8    LYS LYS A . n 
B 1 10  GLU 10  9    9    GLU GLU A . n 
B 1 11  LEU 11  10   10   LEU LEU A . n 
B 1 12  ASN 12  11   11   ASN ASN A . n 
B 1 13  ASP 13  12   12   ASP ASP A . n 
B 1 14  LEU 14  13   13   LEU LEU A . n 
B 1 15  ALA 15  14   14   ALA ALA A . n 
B 1 16  ARG 16  15   15   ARG ARG A . n 
B 1 17  ASP 17  16   16   ASP ASP A . n 
B 1 18  PRO 18  17   17   PRO PRO A . n 
B 1 19  PRO 19  18   18   PRO PRO A . n 
B 1 20  ALA 20  19   19   ALA ALA A . n 
B 1 21  GLN 21  20   20   GLN GLN A . n 
B 1 22  CYS 22  21   21   CYS CYS A . n 
B 1 23  SER 23  22   22   SER SER A . n 
B 1 24  ALA 24  23   23   ALA ALA A . n 
B 1 25  GLY 25  24   24   GLY GLY A . n 
B 1 26  PRO 26  25   25   PRO PRO A . n 
B 1 27  VAL 27  26   26   VAL VAL A . n 
B 1 28  GLY 28  27   27   GLY GLY A . n 
B 1 29  ASP 29  28   28   ASP ASP A . n 
B 1 30  ASP 30  29   29   ASP ASP A . n 
B 1 31  MET 31  30   30   MET MET A . n 
B 1 32  PHE 32  31   31   PHE PHE A . n 
B 1 33  HIS 33  32   32   HIS HIS A . n 
B 1 34  TRP 34  33   33   TRP TRP A . n 
B 1 35  GLN 35  34   34   GLN GLN A . n 
B 1 36  ALA 36  35   35   ALA ALA A . n 
B 1 37  THR 37  36   36   THR THR A . n 
B 1 38  ILE 38  37   37   ILE ILE A . n 
B 1 39  MET 39  38   38   MET MET A . n 
B 1 40  GLY 40  39   39   GLY GLY A . n 
B 1 41  PRO 41  40   40   PRO PRO A . n 
B 1 42  ASN 42  41   41   ASN ASN A . n 
B 1 43  ASP 43  42   42   ASP ASP A . n 
B 1 44  SER 44  43   43   SER SER A . n 
B 1 45  PRO 45  44   44   PRO PRO A . n 
B 1 46  TYR 46  45   45   TYR TYR A . n 
B 1 47  GLN 47  46   46   GLN GLN A . n 
B 1 48  GLY 48  47   47   GLY GLY A . n 
B 1 49  GLY 49  48   48   GLY GLY A . n 
B 1 50  VAL 50  49   49   VAL VAL A . n 
B 1 51  PHE 51  50   50   PHE PHE A . n 
B 1 52  PHE 52  51   51   PHE PHE A . n 
B 1 53  LEU 53  52   52   LEU LEU A . n 
B 1 54  THR 54  53   53   THR THR A . n 
B 1 55  ILE 55  54   54   ILE ILE A . n 
B 1 56  HIS 56  55   55   HIS HIS A . n 
B 1 57  PHE 57  56   56   PHE PHE A . n 
B 1 58  PRO 58  57   57   PRO PRO A . n 
B 1 59  THR 59  58   58   THR THR A . n 
B 1 60  ASP 60  59   59   ASP ASP A . n 
B 1 61  TYR 61  60   60   TYR TYR A . n 
B 1 62  PRO 62  61   61   PRO PRO A . n 
B 1 63  PHE 63  62   62   PHE PHE A . n 
B 1 64  LYS 64  63   63   LYS LYS A . n 
B 1 65  PRO 65  64   64   PRO PRO A . n 
B 1 66  PRO 66  65   65   PRO PRO A . n 
B 1 67  LYS 67  66   66   LYS LYS A . n 
B 1 68  VAL 68  67   67   VAL VAL A . n 
B 1 69  ALA 69  68   68   ALA ALA A . n 
B 1 70  PHE 70  69   69   PHE PHE A . n 
B 1 71  THR 71  70   70   THR THR A . n 
B 1 72  THR 72  71   71   THR THR A . n 
B 1 73  ARG 73  72   72   ARG ARG A . n 
B 1 74  ILE 74  73   73   ILE ILE A . n 
B 1 75  TYR 75  74   74   TYR TYR A . n 
B 1 76  HIS 76  75   75   HIS HIS A . n 
B 1 77  PRO 77  76   76   PRO PRO A . n 
B 1 78  ASN 78  77   77   ASN ASN A . n 
B 1 79  ILE 79  78   78   ILE ILE A . n 
B 1 80  ASN 80  79   79   ASN ASN A . n 
B 1 81  SER 81  80   80   SER SER A . n 
B 1 82  ASN 82  81   81   ASN ASN A . n 
B 1 83  GLY 83  82   82   GLY GLY A . n 
B 1 84  SER 84  83   83   SER SER A . n 
B 1 85  ILE 85  84   84   ILE ILE A . n 
B 1 86  CYS 86  85   85   CYS CYS A . n 
B 1 87  LEU 87  86   86   LEU LEU A . n 
B 1 88  ASP 88  87   87   ASP ASP A . n 
B 1 89  ILE 89  88   88   ILE ILE A . n 
B 1 90  LEU 90  89   89   LEU LEU A . n 
B 1 91  ARG 91  90   90   ARG ARG A . n 
B 1 92  SER 92  91   91   SER SER A . n 
B 1 93  GLN 93  92   92   GLN GLN A . n 
B 1 94  TRP 94  93   93   TRP TRP A . n 
B 1 95  SER 95  94   94   SER SER A . n 
B 1 96  PRO 96  95   95   PRO PRO A . n 
B 1 97  ALA 97  96   96   ALA ALA A . n 
B 1 98  LEU 98  97   97   LEU LEU A . n 
B 1 99  THR 99  98   98   THR THR A . n 
B 1 100 ILE 100 99   99   ILE ILE A . n 
B 1 101 SER 101 100  100  SER SER A . n 
B 1 102 LYS 102 101  101  LYS LYS A . n 
B 1 103 VAL 103 102  102  VAL VAL A . n 
B 1 104 LEU 104 103  103  LEU LEU A . n 
B 1 105 LEU 105 104  104  LEU LEU A . n 
B 1 106 SER 106 105  105  SER SER A . n 
B 1 107 ILE 107 106  106  ILE ILE A . n 
B 1 108 CYS 108 107  107  CYS CYS A . n 
B 1 109 SER 109 108  108  SER SER A . n 
B 1 110 LEU 110 109  109  LEU LEU A . n 
B 1 111 LEU 111 110  110  LEU LEU A . n 
B 1 112 CYS 112 111  111  CYS CYS A . n 
B 1 113 ASP 113 112  112  ASP ASP A . n 
B 1 114 PRO 114 113  113  PRO PRO A . n 
B 1 115 ASN 115 114  114  ASN ASN A . n 
B 1 116 PRO 116 115  115  PRO PRO A . n 
B 1 117 ASP 117 116  116  ASP ASP A . n 
B 1 118 ASP 118 117  117  ASP ASP A . n 
B 1 119 PRO 119 118  118  PRO PRO A . n 
B 1 120 LEU 120 119  119  LEU LEU A . n 
B 1 121 VAL 121 120  120  VAL VAL A . n 
B 1 122 PRO 122 121  121  PRO PRO A . n 
B 1 123 GLU 123 122  122  GLU GLU A . n 
B 1 124 ILE 124 123  123  ILE ILE A . n 
B 1 125 ALA 125 124  124  ALA ALA A . n 
B 1 126 ARG 126 125  125  ARG ARG A . n 
B 1 127 ILE 127 126  126  ILE ILE A . n 
B 1 128 TYR 128 127  127  TYR TYR A . n 
B 1 129 LYS 129 128  128  LYS LYS A . n 
B 1 130 THR 130 129  129  THR THR A . n 
B 1 131 ASP 131 130  130  ASP ASP A . n 
B 1 132 ARG 132 131  131  ARG ARG A . n 
B 1 133 GLU 133 132  132  GLU GLU A . n 
B 1 134 LYS 134 133  133  LYS LYS A . n 
B 1 135 TYR 135 134  134  TYR TYR A . n 
B 1 136 ASN 136 135  135  ASN ASN A . n 
B 1 137 ARG 137 136  136  ARG ARG A . n 
B 1 138 ILE 138 137  137  ILE ILE A . n 
B 1 139 ALA 139 138  138  ALA ALA A . n 
B 1 140 ARG 140 139  139  ARG ARG A . n 
B 1 141 GLU 141 140  140  GLU GLU A . n 
B 1 142 TRP 142 141  141  TRP TRP A . n 
B 1 143 THR 143 142  142  THR THR A . n 
B 1 144 GLN 144 143  143  GLN GLN A . n 
B 1 145 LYS 145 144  144  LYS LYS A . n 
B 1 146 TYR 146 145  145  TYR TYR A . n 
B 1 147 ALA 147 146  146  ALA ALA A . n 
B 1 148 MET 148 147  147  MET MET A . n 
B 1 149 GLY 149 148  148  GLY GLY A . n 
B 1 150 GLY 150 149  ?    ?   ?   A . n 
B 1 151 GLY 151 150  ?    ?   ?   A . n 
B 1 152 SER 152 151  ?    ?   ?   A . n 
B 1 153 GLY 153 152  ?    ?   ?   A . n 
B 1 154 GLY 154 153  ?    ?   ?   A . n 
B 1 155 GLY 155 154  ?    ?   ?   A . n 
B 1 156 SER 156 155  ?    ?   ?   A . n 
B 1 157 GLY 157 156  ?    ?   ?   A . n 
B 1 158 GLY 158 157  ?    ?   ?   A . n 
B 1 159 GLY 159 158  ?    ?   ?   A . n 
B 1 160 SER 160 159  ?    ?   ?   A . n 
B 1 161 GLY 161 160  ?    ?   ?   A . n 
B 1 162 GLY 162 161  ?    ?   ?   A . n 
B 1 163 GLY 163 162  ?    ?   ?   A . n 
B 1 164 SER 164 163  ?    ?   ?   A . n 
B 1 165 GLY 165 164  ?    ?   ?   A . n 
B 1 166 GLY 166 165  ?    ?   ?   A . n 
B 1 167 LYS 167 936  ?    ?   ?   A . n 
B 1 168 ASP 168 937  ?    ?   ?   A . n 
B 1 169 LYS 169 938  ?    ?   ?   A . n 
B 1 170 ASP 170 939  ?    ?   ?   A . n 
B 1 171 ASN 171 940  ?    ?   ?   A . n 
B 1 172 THR 172 941  ?    ?   ?   A . n 
B 1 173 ASN 173 942  ?    ?   ?   A . n 
B 1 174 VAL 174 943  ?    ?   ?   A . n 
B 1 175 ASN 175 944  ?    ?   ?   A . n 
B 1 176 ALA 176 945  945  ALA ALA A . n 
B 1 177 ASP 177 946  946  ASP ASP A . n 
B 1 178 VAL 178 947  947  VAL VAL A . n 
B 1 179 GLN 179 948  948  GLN GLN A . n 
B 1 180 LYS 180 949  949  LYS LYS A . n 
B 1 181 LEU 181 950  950  LEU LEU A . n 
B 1 182 GLN 182 951  951  GLN GLN A . n 
B 1 183 GLN 183 952  952  GLN GLN A . n 
B 1 184 GLN 184 953  953  GLN GLN A . n 
B 1 185 LEU 185 954  954  LEU LEU A . n 
B 1 186 GLN 186 955  955  GLN GLN A . n 
B 1 187 ASP 187 956  956  ASP ASP A . n 
B 1 188 ILE 188 957  957  ILE ILE A . n 
B 1 189 LYS 189 958  958  LYS LYS A . n 
B 1 190 GLU 190 959  959  GLU GLU A . n 
B 1 191 GLN 191 960  960  GLN GLN A . n 
B 1 192 THR 192 961  961  THR THR A . n 
B 1 193 MET 193 962  962  MET MET A . n 
B 1 194 CYS 194 963  963  CYS CYS A . n 
B 1 195 PRO 195 964  964  PRO PRO A . n 
B 1 196 VAL 196 965  965  VAL VAL A . n 
B 1 197 CYS 197 966  966  CYS CYS A . n 
B 1 198 LEU 198 967  967  LEU LEU A . n 
B 1 199 ASP 199 968  968  ASP ASP A . n 
B 1 200 ARG 200 969  969  ARG ARG A . n 
B 1 201 LEU 201 970  970  LEU LEU A . n 
B 1 202 LYS 202 971  971  LYS LYS A . n 
B 1 203 ASN 203 972  972  ASN ASN A . n 
B 1 204 MET 204 973  973  MET MET A . n 
B 1 205 ILE 205 974  974  ILE ILE A . n 
B 1 206 PHE 206 975  975  PHE PHE A . n 
B 1 207 LEU 207 976  976  LEU LEU A . n 
B 1 208 CYS 208 977  977  CYS CYS A . n 
B 1 209 GLY 209 978  978  GLY GLY A . n 
B 1 210 HIS 210 979  979  HIS HIS A . n 
B 1 211 GLY 211 980  980  GLY GLY A . n 
B 1 212 THR 212 981  981  THR THR A . n 
B 1 213 CYS 213 982  982  CYS CYS A . n 
B 1 214 GLN 214 983  983  GLN GLN A . n 
B 1 215 LEU 215 984  984  LEU LEU A . n 
B 1 216 CYS 216 985  985  CYS CYS A . n 
B 1 217 GLY 217 986  986  GLY GLY A . n 
B 1 218 ASP 218 987  987  ASP ASP A . n 
B 1 219 ARG 219 988  988  ARG ARG A . n 
B 1 220 MET 220 989  989  MET MET A . n 
B 1 221 SER 221 990  990  SER SER A . n 
B 1 222 GLU 222 991  991  GLU GLU A . n 
B 1 223 CYS 223 992  992  CYS CYS A . n 
B 1 224 PRO 224 993  993  PRO PRO A . n 
B 1 225 ILE 225 994  994  ILE ILE A . n 
B 1 226 CYS 226 995  995  CYS CYS A . n 
B 1 227 ARG 227 996  996  ARG ARG A . n 
B 1 228 LYS 228 997  997  LYS LYS A . n 
B 1 229 ALA 229 998  998  ALA ALA A . n 
B 1 230 ILE 230 999  999  ILE ILE A . n 
B 1 231 GLU 231 1000 1000 GLU GLU A . n 
B 1 232 ARG 232 1001 1001 ARG ARG A . n 
B 1 233 ARG 233 1002 1002 ARG ARG A . n 
B 1 234 ILE 234 1003 1003 ILE ILE A . n 
B 1 235 LEU 235 1004 1004 LEU LEU A . n 
B 1 236 LEU 236 1005 1005 LEU LEU A . n 
B 1 237 TYR 237 1006 1006 TYR TYR A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ZN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZN 
_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 ZN  1  1101 1  ZN  ZN  B . 
D 2 ZN  1  1102 2  ZN  ZN  B . 
E 2 ZN  1  1101 3  ZN  ZN  A . 
F 2 ZN  1  1102 4  ZN  ZN  A . 
G 2 ZN  1  1103 5  ZN  ZN  A . 
H 3 HOH 1  1201 24 HOH HOH B . 
H 3 HOH 2  1202 30 HOH HOH B . 
H 3 HOH 3  1203 8  HOH HOH B . 
H 3 HOH 4  1204 39 HOH HOH B . 
H 3 HOH 5  1205 7  HOH HOH B . 
H 3 HOH 6  1206 21 HOH HOH B . 
H 3 HOH 7  1207 22 HOH HOH B . 
H 3 HOH 8  1208 1  HOH HOH B . 
H 3 HOH 9  1209 25 HOH HOH B . 
H 3 HOH 10 1210 3  HOH HOH B . 
H 3 HOH 11 1211 9  HOH HOH B . 
H 3 HOH 12 1212 17 HOH HOH B . 
H 3 HOH 13 1213 5  HOH HOH B . 
H 3 HOH 14 1214 36 HOH HOH B . 
H 3 HOH 15 1215 31 HOH HOH B . 
H 3 HOH 16 1216 2  HOH HOH B . 
H 3 HOH 17 1217 14 HOH HOH B . 
H 3 HOH 18 1218 20 HOH HOH B . 
H 3 HOH 19 1219 33 HOH HOH B . 
H 3 HOH 20 1220 12 HOH HOH B . 
H 3 HOH 21 1221 38 HOH HOH B . 
H 3 HOH 22 1222 4  HOH HOH B . 
H 3 HOH 23 1223 10 HOH HOH B . 
H 3 HOH 24 1224 11 HOH HOH B . 
H 3 HOH 25 1225 23 HOH HOH B . 
H 3 HOH 26 1226 6  HOH HOH B . 
H 3 HOH 27 1227 18 HOH HOH B . 
H 3 HOH 28 1228 35 HOH HOH B . 
I 3 HOH 1  1201 27 HOH HOH A . 
I 3 HOH 2  1202 15 HOH HOH A . 
I 3 HOH 3  1203 37 HOH HOH A . 
I 3 HOH 4  1204 16 HOH HOH A . 
I 3 HOH 5  1205 29 HOH HOH A . 
I 3 HOH 6  1206 19 HOH HOH A . 
I 3 HOH 7  1207 26 HOH HOH A . 
I 3 HOH 8  1208 13 HOH HOH A . 
I 3 HOH 9  1209 32 HOH HOH A . 
I 3 HOH 10 1210 28 HOH HOH A . 
I 3 HOH 11 1211 34 HOH HOH A . 
# 
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 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot     ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.030 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8V0D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     28.985 
_cell.length_a_esd                 ? 
_cell.length_b                     65.119 
_cell.length_b_esd                 ? 
_cell.length_c                     135.931 
_cell.length_c_esd                 ? 
_cell.volume                       256207.577 
_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                         8V0D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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                   8V0D 
_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             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.66 
_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              6.0 
_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    
;4% v/v TacsimateTM pH 6.0, 
12% w/v Polyethylene glycol 3,350
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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 EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-20 
_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   0.9792 
_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 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          45.79 
_reflns.entry_id                                       8V0D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.40 
_reflns.d_resolution_low                               37.16 
_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                                     18194 
_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                           91.35 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.86 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.057 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.4 
_reflns_shell.d_res_low                                     2.44 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             932 
_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                               0.288 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.903 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               64.45 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8V0D 
_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                            2.40 
_refine.ls_d_res_low                             37.16 
_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                     18180 
_refine.ls_number_reflns_R_free                  938 
_refine.ls_number_reflns_R_work                  17242 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.36 
_refine.ls_percent_reflns_R_free                 5.16 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2142 
_refine.ls_R_factor_R_free                       0.2434 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2127 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 29.0030 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3252 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        37.16 
_refine_hist.number_atoms_solvent             39 
_refine_hist.number_atoms_total               3423 
_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        3379 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_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' ? 0.0072  ? 3475 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9546  ? 4717 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0552  ? 517  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0092  ? 615  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0071 ? 1341 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.ncs_model_details 
1 'X-RAY DIFFRACTION' d_2 ens_1 1.12392001655 ? ? ? 'Torsion NCS' C B ? ? ? ? 
2 'X-RAY DIFFRACTION' d_2 ens_2 3.00079986885 ? ? ? 'Torsion NCS' B A ? ? ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.40 2.53  . . 114 2292 86.24 . . . . 0.3074 . . . . . . . . . . . 0.3103 
'X-RAY DIFFRACTION' 2.53 2.69  . . 123 2465 91.58 . . . . 0.2712 . . . . . . . . . . . 0.3276 
'X-RAY DIFFRACTION' 2.69 2.89  . . 153 2476 91.86 . . . . 0.2821 . . . . . . . . . . . 0.2810 
'X-RAY DIFFRACTION' 2.89 3.18  . . 132 2470 92.33 . . . . 0.2668 . . . . . . . . . . . 0.2779 
'X-RAY DIFFRACTION' 3.18 3.65  . . 172 2529 94.71 . . . . 0.2366 . . . . . . . . . . . 0.2828 
'X-RAY DIFFRACTION' 3.65 4.59  . . 128 2447 90.93 . . . . 0.1807 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 4.59 37.16 . . 116 2563 91.84 . . . . 0.1668 . . . . . . . . . . . 0.1672 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 0 through 99 or resid 101 through 104 or resid 106 through 148))
;
ens_1 d_2 
;(chain "B" and (resid 0 through 99 or resid 101 through 104 or resid 106 through 148))
;
ens_2 d_1 
;(chain "C" and resid 945 through 1006)
;
ens_2 d_2 
;chain "D"
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 B SER 1   . B ILE 100 . A SER 0   A ILE 99   ? ? 
ens_1 d_1 2 B LYS 102 . B LEU 105 . A LYS 101 A LEU 104  ? ? 
ens_1 d_1 3 B ILE 107 . B GLY 149 . A ILE 106 A GLY 148  ? ? 
ens_1 d_2 1 A SER 1   . A ILE 100 . B SER 0   B ILE 99   ? ? 
ens_1 d_2 2 A LYS 102 . A LEU 105 . B LYS 101 B LEU 104  ? ? 
ens_1 d_2 3 A ILE 107 . A GLY 149 . B ILE 106 B GLY 148  ? ? 
ens_2 d_1 1 A ALA 176 . A TYR 237 . B ALA 945 B TYR 1006 ? ? 
ens_2 d_2 1 B ALA 176 . B TYR 237 . A ALA 945 A TYR 1006 ? ? 
# 
loop_
_struct_ncs_ens.id 
_struct_ncs_ens.details 
ens_1 ? 
ens_2 ? 
# 
_struct.entry_id                     8V0D 
_struct.title                        'Ubch5B-RING3 of MIB1 fusion structure' 
_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        8V0D 
_struct_keywords.text            'E3 ligase, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP UB2D2_HUMAN P62837 ? 1 
;MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINS
NGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM
;
1   
2 UNP MIB1_HUMAN  Q86YT6 ? 1 KDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY 936 
# 
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 8V0D B 2   ? 148 ? P62837 1   ? 147  ? 1   147  
2 2 8V0D B 167 ? 237 ? Q86YT6 936 ? 1006 ? 936 1006 
3 1 8V0D A 2   ? 148 ? P62837 1   ? 147  ? 1   147  
4 2 8V0D A 167 ? 237 ? Q86YT6 936 ? 1006 ? 936 1006 
# 
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 8V0D SER B 1   ? UNP P62837 ? ? 'expression tag' 0   1  
1 8V0D GLY B 149 ? UNP P62837 ? ? linker           148 2  
1 8V0D GLY B 150 ? UNP P62837 ? ? linker           149 3  
1 8V0D GLY B 151 ? UNP P62837 ? ? linker           150 4  
1 8V0D SER B 152 ? UNP P62837 ? ? linker           151 5  
1 8V0D GLY B 153 ? UNP P62837 ? ? linker           152 6  
1 8V0D GLY B 154 ? UNP P62837 ? ? linker           153 7  
1 8V0D GLY B 155 ? UNP P62837 ? ? linker           154 8  
1 8V0D SER B 156 ? UNP P62837 ? ? linker           155 9  
1 8V0D GLY B 157 ? UNP P62837 ? ? linker           156 10 
1 8V0D GLY B 158 ? UNP P62837 ? ? linker           157 11 
1 8V0D GLY B 159 ? UNP P62837 ? ? linker           158 12 
1 8V0D SER B 160 ? UNP P62837 ? ? linker           159 13 
1 8V0D GLY B 161 ? UNP P62837 ? ? linker           160 14 
1 8V0D GLY B 162 ? UNP P62837 ? ? linker           161 15 
1 8V0D GLY B 163 ? UNP P62837 ? ? linker           162 16 
1 8V0D SER B 164 ? UNP P62837 ? ? linker           163 17 
1 8V0D GLY B 165 ? UNP P62837 ? ? linker           164 18 
1 8V0D GLY B 166 ? UNP P62837 ? ? linker           165 19 
3 8V0D SER A 1   ? UNP P62837 ? ? 'expression tag' 0   20 
3 8V0D GLY A 149 ? UNP P62837 ? ? linker           148 21 
3 8V0D GLY A 150 ? UNP P62837 ? ? linker           149 22 
3 8V0D GLY A 151 ? UNP P62837 ? ? linker           150 23 
3 8V0D SER A 152 ? UNP P62837 ? ? linker           151 24 
3 8V0D GLY A 153 ? UNP P62837 ? ? linker           152 25 
3 8V0D GLY A 154 ? UNP P62837 ? ? linker           153 26 
3 8V0D GLY A 155 ? UNP P62837 ? ? linker           154 27 
3 8V0D SER A 156 ? UNP P62837 ? ? linker           155 28 
3 8V0D GLY A 157 ? UNP P62837 ? ? linker           156 29 
3 8V0D GLY A 158 ? UNP P62837 ? ? linker           157 30 
3 8V0D GLY A 159 ? UNP P62837 ? ? linker           158 31 
3 8V0D SER A 160 ? UNP P62837 ? ? linker           159 32 
3 8V0D GLY A 161 ? UNP P62837 ? ? linker           160 33 
3 8V0D GLY A 162 ? UNP P62837 ? ? linker           161 34 
3 8V0D GLY A 163 ? UNP P62837 ? ? linker           162 35 
3 8V0D SER A 164 ? UNP P62837 ? ? linker           163 36 
3 8V0D GLY A 165 ? UNP P62837 ? ? linker           164 37 
3 8V0D GLY A 166 ? UNP P62837 ? ? linker           165 38 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1960  ? 
1 MORE         -31   ? 
1 'SSA (A^2)'  22630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_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 SER A 1   ? ASP A 17  ? SER B 0   ASP B 16  1 ? 17 
HELX_P HELX_P2  AA2 LEU A 87  ? ARG A 91  ? LEU B 86  ARG B 90  5 ? 5  
HELX_P HELX_P3  AA3 THR A 99  ? ASP A 113 ? THR B 98  ASP B 112 1 ? 15 
HELX_P HELX_P4  AA4 VAL A 121 ? ASP A 131 ? VAL B 120 ASP B 130 1 ? 11 
HELX_P HELX_P5  AA5 ASP A 131 ? ALA A 147 ? ASP B 130 ALA B 146 1 ? 17 
HELX_P HELX_P6  AA6 ASN A 175 ? MET A 193 ? ASN B 944 MET B 962 1 ? 19 
HELX_P HELX_P7  AA7 CYS A 213 ? ASP A 218 ? CYS B 982 ASP B 987 1 ? 6  
HELX_P HELX_P8  AA8 MET B 2   ? ASP B 17  ? MET A 1   ASP A 16  1 ? 16 
HELX_P HELX_P9  AA9 LEU B 87  ? ARG B 91  ? LEU A 86  ARG A 90  5 ? 5  
HELX_P HELX_P10 AB1 THR B 99  ? ASP B 113 ? THR A 98  ASP A 112 1 ? 15 
HELX_P HELX_P11 AB2 VAL B 121 ? ASP B 131 ? VAL A 120 ASP A 130 1 ? 11 
HELX_P HELX_P12 AB3 ASP B 131 ? ALA B 147 ? ASP A 130 ALA A 146 1 ? 17 
HELX_P HELX_P13 AB4 LYS B 180 ? GLN B 186 ? LYS A 949 GLN A 955 1 ? 7  
HELX_P HELX_P14 AB5 ASP B 187 ? MET B 193 ? ASP A 956 MET A 962 1 ? 7  
HELX_P HELX_P15 AB6 CYS B 213 ? ASP B 218 ? CYS A 982 ASP A 987 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 194 SG  ? ? ? 1_555 C ZN . ZN ? ? B CYS 963 B ZN 1101 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc2  metalc ? ? A CYS 197 SG  ? ? ? 1_555 C ZN . ZN ? ? B CYS 966 B ZN 1101 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc3  metalc ? ? A CYS 208 SG  ? ? ? 1_555 D ZN . ZN ? ? B CYS 977 B ZN 1102 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc4  metalc ? ? A HIS 210 ND1 ? ? ? 1_555 D ZN . ZN ? ? B HIS 979 B ZN 1102 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc5  metalc ? ? A CYS 213 SG  ? ? ? 1_555 C ZN . ZN ? ? B CYS 982 B ZN 1101 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc6  metalc ? ? A CYS 216 SG  ? ? ? 1_555 C ZN . ZN ? ? B CYS 985 B ZN 1101 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc7  metalc ? ? A CYS 223 SG  ? ? ? 1_555 D ZN . ZN ? ? B CYS 992 B ZN 1102 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc8  metalc ? ? A CYS 226 SG  ? ? ? 1_555 D ZN . ZN ? ? B CYS 995 B ZN 1102 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc9  metalc ? ? B HIS 33  NE2 ? ? ? 1_555 G ZN . ZN ? ? A HIS 32  A ZN 1103 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc10 metalc ? ? B ASP 43  OD2 ? ? ? 1_555 G ZN . ZN ? ? A ASP 42  A ZN 1103 1_455 ? ? ? ? ? ? ? 2.150 ? ? 
metalc11 metalc ? ? B HIS 56  NE2 ? ? ? 1_555 G ZN . ZN ? ? A HIS 55  A ZN 1103 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc12 metalc ? ? B CYS 112 SG  ? ? ? 1_555 G ZN . ZN ? ? A CYS 111 A ZN 1103 1_455 ? ? ? ? ? ? ? 2.324 ? ? 
metalc13 metalc ? ? B CYS 194 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 963 A ZN 1101 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc14 metalc ? ? B CYS 197 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 966 A ZN 1101 1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc15 metalc ? ? B CYS 208 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 977 A ZN 1102 1_555 ? ? ? ? ? ? ? 2.284 ? ? 
metalc16 metalc ? ? B HIS 210 ND1 ? ? ? 1_555 F ZN . ZN ? ? A HIS 979 A ZN 1102 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc17 metalc ? ? B CYS 213 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 982 A ZN 1101 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc18 metalc ? ? B CYS 216 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 985 A ZN 1101 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc19 metalc ? ? B CYS 223 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 992 A ZN 1102 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc20 metalc ? ? B CYS 226 SG  ? ? ? 1_555 F ZN . ZN ? ? A CYS 995 A ZN 1102 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 194 ? B CYS 963 ? 1_555 ZN ? C ZN . ? B ZN 1101 ? 1_555 SG  ? A CYS 197 ? B CYS 966 ? 1_555 103.0 ? 
2  SG  ? A CYS 194 ? B CYS 963 ? 1_555 ZN ? C ZN . ? B ZN 1101 ? 1_555 SG  ? A CYS 213 ? B CYS 982 ? 1_555 122.2 ? 
3  SG  ? A CYS 197 ? B CYS 966 ? 1_555 ZN ? C ZN . ? B ZN 1101 ? 1_555 SG  ? A CYS 213 ? B CYS 982 ? 1_555 113.9 ? 
4  SG  ? A CYS 194 ? B CYS 963 ? 1_555 ZN ? C ZN . ? B ZN 1101 ? 1_555 SG  ? A CYS 216 ? B CYS 985 ? 1_555 116.7 ? 
5  SG  ? A CYS 197 ? B CYS 966 ? 1_555 ZN ? C ZN . ? B ZN 1101 ? 1_555 SG  ? A CYS 216 ? B CYS 985 ? 1_555 104.9 ? 
6  SG  ? A CYS 213 ? B CYS 982 ? 1_555 ZN ? C ZN . ? B ZN 1101 ? 1_555 SG  ? A CYS 216 ? B CYS 985 ? 1_555 95.4  ? 
7  SG  ? A CYS 208 ? B CYS 977 ? 1_555 ZN ? D ZN . ? B ZN 1102 ? 1_555 ND1 ? A HIS 210 ? B HIS 979 ? 1_555 114.6 ? 
8  SG  ? A CYS 208 ? B CYS 977 ? 1_555 ZN ? D ZN . ? B ZN 1102 ? 1_555 SG  ? A CYS 223 ? B CYS 992 ? 1_555 103.4 ? 
9  ND1 ? A HIS 210 ? B HIS 979 ? 1_555 ZN ? D ZN . ? B ZN 1102 ? 1_555 SG  ? A CYS 223 ? B CYS 992 ? 1_555 101.6 ? 
10 SG  ? A CYS 208 ? B CYS 977 ? 1_555 ZN ? D ZN . ? B ZN 1102 ? 1_555 SG  ? A CYS 226 ? B CYS 995 ? 1_555 109.9 ? 
11 ND1 ? A HIS 210 ? B HIS 979 ? 1_555 ZN ? D ZN . ? B ZN 1102 ? 1_555 SG  ? A CYS 226 ? B CYS 995 ? 1_555 116.8 ? 
12 SG  ? A CYS 223 ? B CYS 992 ? 1_555 ZN ? D ZN . ? B ZN 1102 ? 1_555 SG  ? A CYS 226 ? B CYS 995 ? 1_555 109.2 ? 
13 NE2 ? B HIS 33  ? A HIS 32  ? 1_555 ZN ? G ZN . ? A ZN 1103 ? 1_555 OD2 ? B ASP 43  ? A ASP 42  ? 1_555 91.4  ? 
14 NE2 ? B HIS 33  ? A HIS 32  ? 1_555 ZN ? G ZN . ? A ZN 1103 ? 1_555 NE2 ? B HIS 56  ? A HIS 55  ? 1_555 112.6 ? 
15 OD2 ? B ASP 43  ? A ASP 42  ? 1_555 ZN ? G ZN . ? A ZN 1103 ? 1_555 NE2 ? B HIS 56  ? A HIS 55  ? 1_555 98.0  ? 
16 NE2 ? B HIS 33  ? A HIS 32  ? 1_555 ZN ? G ZN . ? A ZN 1103 ? 1_555 SG  ? B CYS 112 ? A CYS 111 ? 1_555 91.5  ? 
17 OD2 ? B ASP 43  ? A ASP 42  ? 1_555 ZN ? G ZN . ? A ZN 1103 ? 1_555 SG  ? B CYS 112 ? A CYS 111 ? 1_555 0.8   ? 
18 NE2 ? B HIS 56  ? A HIS 55  ? 1_555 ZN ? G ZN . ? A ZN 1103 ? 1_555 SG  ? B CYS 112 ? A CYS 111 ? 1_555 98.7  ? 
19 SG  ? B CYS 194 ? A CYS 963 ? 1_555 ZN ? E ZN . ? A ZN 1101 ? 1_555 SG  ? B CYS 197 ? A CYS 966 ? 1_555 101.8 ? 
20 SG  ? B CYS 194 ? A CYS 963 ? 1_555 ZN ? E ZN . ? A ZN 1101 ? 1_555 SG  ? B CYS 213 ? A CYS 982 ? 1_555 117.8 ? 
21 SG  ? B CYS 197 ? A CYS 966 ? 1_555 ZN ? E ZN . ? A ZN 1101 ? 1_555 SG  ? B CYS 213 ? A CYS 982 ? 1_555 113.7 ? 
22 SG  ? B CYS 194 ? A CYS 963 ? 1_555 ZN ? E ZN . ? A ZN 1101 ? 1_555 SG  ? B CYS 216 ? A CYS 985 ? 1_555 112.1 ? 
23 SG  ? B CYS 197 ? A CYS 966 ? 1_555 ZN ? E ZN . ? A ZN 1101 ? 1_555 SG  ? B CYS 216 ? A CYS 985 ? 1_555 115.8 ? 
24 SG  ? B CYS 213 ? A CYS 982 ? 1_555 ZN ? E ZN . ? A ZN 1101 ? 1_555 SG  ? B CYS 216 ? A CYS 985 ? 1_555 96.3  ? 
25 SG  ? B CYS 208 ? A CYS 977 ? 1_555 ZN ? F ZN . ? A ZN 1102 ? 1_555 ND1 ? B HIS 210 ? A HIS 979 ? 1_555 118.1 ? 
26 SG  ? B CYS 208 ? A CYS 977 ? 1_555 ZN ? F ZN . ? A ZN 1102 ? 1_555 SG  ? B CYS 223 ? A CYS 992 ? 1_555 104.7 ? 
27 ND1 ? B HIS 210 ? A HIS 979 ? 1_555 ZN ? F ZN . ? A ZN 1102 ? 1_555 SG  ? B CYS 223 ? A CYS 992 ? 1_555 104.9 ? 
28 SG  ? B CYS 208 ? A CYS 977 ? 1_555 ZN ? F ZN . ? A ZN 1102 ? 1_555 SG  ? B CYS 226 ? A CYS 995 ? 1_555 106.5 ? 
29 ND1 ? B HIS 210 ? A HIS 979 ? 1_555 ZN ? F ZN . ? A ZN 1102 ? 1_555 SG  ? B CYS 226 ? A CYS 995 ? 1_555 110.6 ? 
30 SG  ? B CYS 223 ? A CYS 992 ? 1_555 ZN ? F ZN . ? A ZN 1102 ? 1_555 SG  ? B CYS 226 ? A CYS 995 ? 1_555 111.8 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 61 A . ? TYR 60 B PRO 62 A ? PRO 61 B 1 3.30 
2 TYR 61 B . ? TYR 60 A PRO 62 B ? PRO 61 A 1 4.73 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? 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 SER A 23  ? PRO A 26  ? SER B 22   PRO B 25   
AA1 2 HIS A 33  ? MET A 39  ? HIS B 32   MET B 38   
AA1 3 VAL A 50  ? HIS A 56  ? VAL B 49   HIS B 55   
AA1 4 LYS A 67  ? PHE A 70  ? LYS B 66   PHE B 69   
AA2 1 GLY A 211 ? THR A 212 ? GLY B 980  THR B 981  
AA2 2 MET A 204 ? PHE A 206 ? MET B 973  PHE B 975  
AA2 3 ARG A 233 ? LEU A 235 ? ARG B 1002 LEU B 1004 
AA3 1 CYS B 22  ? PRO B 26  ? CYS A 21   PRO A 25   
AA3 2 HIS B 33  ? MET B 39  ? HIS A 32   MET A 38   
AA3 3 VAL B 50  ? HIS B 56  ? VAL A 49   HIS A 55   
AA3 4 LYS B 67  ? PHE B 70  ? LYS A 66   PHE A 69   
AA4 1 GLY B 211 ? THR B 212 ? GLY A 980  THR A 981  
AA4 2 MET B 204 ? ILE B 205 ? MET A 973  ILE A 974  
AA4 3 ILE B 234 ? LEU B 235 ? ILE A 1003 LEU A 1004 
# 
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 N GLY A 25  ? N GLY B 24  O GLN A 35  ? O GLN B 34   
AA1 2 3 N ILE A 38  ? N ILE B 37  O PHE A 51  ? O PHE B 50   
AA1 3 4 N HIS A 56  ? N HIS B 55  O LYS A 67  ? O LYS B 66   
AA2 1 2 O THR A 212 ? O THR B 981 N MET A 204 ? N MET B 973  
AA2 2 3 N ILE A 205 ? N ILE B 974 O ILE A 234 ? O ILE B 1003 
AA3 1 2 N GLY B 25  ? N GLY A 24  O GLN B 35  ? O GLN A 34   
AA3 2 3 N ILE B 38  ? N ILE A 37  O PHE B 51  ? O PHE A 50   
AA3 3 4 N THR B 54  ? N THR A 53  O ALA B 69  ? O ALA A 68   
AA4 1 2 O THR B 212 ? O THR A 981 N MET B 204 ? N MET A 973  
AA4 2 3 N ILE B 205 ? N ILE A 974 O ILE B 234 ? O ILE A 1003 
# 
_pdbx_entry_details.entry_id                   8V0D 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B GLN 46   ? ? O B HOH 1201 ? ? 2.05 
2 1 NH2 A ARG 5    ? ? O A LEU 97   ? ? 2.19 
3 1 OXT A TYR 1006 ? ? O A HOH 1201 ? ? 2.19 
# 
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 ARG B 90  ? ? -136.88 -85.71 
2 1 ARG B 996 ? ? 73.89   -1.18  
3 1 ASP A 16  ? ? -152.14 75.39  
4 1 ARG A 90  ? ? -140.63 -78.32 
5 1 PRO A 115 ? ? -74.88  25.13  
6 1 LEU A 967 ? ? 56.61   17.93  
7 1 ARG A 996 ? ? 74.93   -0.53  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.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[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1  ? refined 0.516  -7.995  55.299 0.55532249081  0.419143814099 0.559042339395 0.00628518401051  
0.0477887887466   -0.0187658676539 0.353690267145  1.26424571275   0.630065595866  -0.304758251409    -0.271083263792  
0.258821805486   0.0100293837005  -0.163887599363  -0.0000804948279   0.0181256649879   -0.0635064948104 0.212927345739   
0.0378208477521  0.385408288974   -0.00364065306385 
'X-RAY DIFFRACTION' 2  ? refined 6.205  3.906   63.961 0.47843622065  0.313618108998 0.50658739471  0.0334221141432   
0.0299443439673   0.0245642450712  0.36611462198   2.67980355553   1.56597121408   0.506959967651     -0.115736076753  
1.73611710449    -0.100393378522  -0.0660286189276 -0.0014325554395   -0.00145014149933 0.104460129635   -0.0949485692329 
0.0390428972127  -0.0970194989778 -0.175280531123   
'X-RAY DIFFRACTION' 3  ? refined 8.781  7.056   51.343 0.625918013356 0.434076223345 0.560674338555 -0.0979177426854  
0.00456357177724  -0.0275213997106 0.566918643588  0.182846757399  0.224223591663  -0.058201248681    0.187602933963   
-0.196237113859  -0.42028755177   0.274133471424   0.000611274648174  -0.0868133417907  0.0916170682886  -0.218223772459  
-0.0761600949393 -0.251539554791  0.290854198545    
'X-RAY DIFFRACTION' 4  ? refined 16.475 10.516  63.999 0.515888017025 0.362582221476 0.532073780072 -0.00883259183616 
0.0217723814171   -0.0551094877371 0.286053264273  0.302128771031  0.302032468827  0.101073438623     0.133109547001   
0.0292680114981  -0.112687575472  0.336179013582   0.000102057506938  0.209873489965    -0.133535287625  -0.420629330311  
-0.338468493997  -0.21453986874   0.38698806312     
'X-RAY DIFFRACTION' 5  ? refined 17.044 7.511   77.494 0.86182442776  0.44088162341  0.642218689873 0.0853683041646   
0.0410540220746   0.0118071108945  0.185965300499  0.668900180943  0.501874696233  0.350313248457     -0.364906830016  
0.128200556826   -0.0255172013114 -0.266619921249  0.000175243638293  -0.333870864966   0.198884136628   -0.224298607146  
0.699404258296   0.0735568060389  0.0413276850487   
'X-RAY DIFFRACTION' 6  ? refined 11.358 -23.457 43.590 1.5093603246   0.689631209209 0.668317902178 0.130932600846    
0.0230419582949   0.00133307125575 0.0503341864644 0.150048288843  0.0225400633428 -0.157557355334    0.00810827743313 
-0.0583910343169 -0.355004185696  0.358901435874   -0.00074008080205  0.180465704426    0.258840103371   -0.743576205632  
0.572388464103   -0.428754221026  0.0502374659752   
'X-RAY DIFFRACTION' 7  ? refined 7.213  -0.688  34.917 0.804441488718 0.588564930977 0.57606212446  0.0318718723722   
0.117224525304    -0.0282208687631 1.15794175703   0.120616785836  1.12007848979   -0.071776224557    0.634065914708   
-0.554516136077  0.303081494882   -0.0925577867559 0.0001993590387    0.237815858644    0.149303807672   0.189617433923   
0.014125300383   -0.0254614053789 -0.0932407104261  
'X-RAY DIFFRACTION' 8  ? refined 18.493 -34.068 18.692 0.460901570377 0.779214751609 0.587111091752 0.0564320209288   
-0.0242359751797  0.103160255769   0.989932978866  1.34565971697   1.3706724656    -0.861724545812    -0.447579548468  
0.0341027955415  0.16943893671    0.0185558150692  -4.12878307879e-05 -0.500272093912   -0.518500279123  -0.189601330352  
0.411821419274   0.244115666221   -0.365177382803   
'X-RAY DIFFRACTION' 9  ? refined 13.265 -30.219 6.195  0.309045964098 0.678085320508 0.504372954469 0.0727849429121   
-0.0295480568181  -0.0161486386807 1.03586146398   0.88748638507   2.70073802099   -0.000943257475056 0.265320384252   
-0.17410624457   0.0562402747549  -0.03047510922   0.000390336415     -0.146951217713   0.159896202154   -0.163702977946  
-0.133485468846  -0.330973684781  -0.529672672983   
'X-RAY DIFFRACTION' 10 ? refined 7.003  -24.913 -4.348 0.917535580105 0.733537549003 0.674553974389 0.328150560008    
-0.00188659171725 0.0249037841728  0.120915711124  0.661429374504  0.144672983477  0.17960647459      0.14953110952    
0.252204356257   -0.147038480672  0.176507725731   0.00137185130944   0.275243315552    0.833827404154   -0.327015329606  
0.0286163928625  -1.3426553805    -0.785302660002   
'X-RAY DIFFRACTION' 11 ? refined 3.224  -37.516 -7.862 0.303733559841 1.34127053732  0.489989817905 -0.0376504481428  
-0.24863025533    0.0117069761957  0.808105101031  0.74898972266   1.89504644954   -0.57613265884     -0.523721840919  
0.602503332081   -0.116923869836  -0.109770348494  -0.338420005099    0.761693684464    -0.694479544614  1.04439526534    
0.0873928095693  0.675931844897   -2.00129324177    
'X-RAY DIFFRACTION' 12 ? refined 5.221  -26.335 35.859 1.15692004202  0.764538398748 0.870603795385 -0.0114108727771  
0.166340600302    0.0364778686105  0.151214240598  0.0462152232612 0.0186439227796 0.110886521564     0.093371658468   
0.0395615062262  -0.0359936341182 0.400783587366   -0.00067005725222  0.358903526209    -0.463864097808  0.563713035421   
-0.171153727459  0.0883605916762  -0.210166858217   
'X-RAY DIFFRACTION' 13 ? refined 17.414 -10.365 23.058 0.648423577607 0.778910113781 0.468800628519 0.15942009647     
-0.0126269469988  -0.0133755799668 0.967459257385  0.921789346235  0.299313471156  0.255608514931     0.345373059412   
0.0127936349207  0.268627927613   -0.255057055992  0.000222663720502  0.078954777198    -0.0531312564929 -0.0488941838289 
-0.184011007289  -0.305385500615  0.386576074204    
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1  B 0   B 31   '( CHAIN B AND RESID 0:31 )'     ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  B 32  B 84   '( CHAIN B AND RESID 32:84 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  B 85  B 98   '( CHAIN B AND RESID 85:98 )'    ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  B 99  B 130  '( CHAIN B AND RESID 99:130 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  B 131 B 148  '( CHAIN B AND RESID 131:148 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  B 943 B 961  '( CHAIN B AND RESID 943:961 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  B 962 B 1006 '( CHAIN B AND RESID 962:1006 )' ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  A 0   A 38   '( CHAIN A AND RESID 0:38 )'     ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  A 39  A 111  '( CHAIN A AND RESID 39:111 )'   ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 A 112 A 120  '( CHAIN A AND RESID 112:120 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 A 121 A 148  '( CHAIN A AND RESID 121:148 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 A 945 A 961  '( CHAIN A AND RESID 945:961 )'  ? ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 A 962 A 1006 '( CHAIN A AND RESID 962:1006 )' ? ? ? ? ? 
# 
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 B GLY 149 ? A GLY 150 
2  1 Y 1 B GLY 150 ? A GLY 151 
3  1 Y 1 B SER 151 ? A SER 152 
4  1 Y 1 B GLY 152 ? A GLY 153 
5  1 Y 1 B GLY 153 ? A GLY 154 
6  1 Y 1 B GLY 154 ? A GLY 155 
7  1 Y 1 B SER 155 ? A SER 156 
8  1 Y 1 B GLY 156 ? A GLY 157 
9  1 Y 1 B GLY 157 ? A GLY 158 
10 1 Y 1 B GLY 158 ? A GLY 159 
11 1 Y 1 B SER 159 ? A SER 160 
12 1 Y 1 B GLY 160 ? A GLY 161 
13 1 Y 1 B GLY 161 ? A GLY 162 
14 1 Y 1 B GLY 162 ? A GLY 163 
15 1 Y 1 B SER 163 ? A SER 164 
16 1 Y 1 B GLY 164 ? A GLY 165 
17 1 Y 1 B GLY 165 ? A GLY 166 
18 1 Y 1 B LYS 936 ? A LYS 167 
19 1 Y 1 B ASP 937 ? A ASP 168 
20 1 Y 1 B LYS 938 ? A LYS 169 
21 1 Y 1 B ASP 939 ? A ASP 170 
22 1 Y 1 B ASN 940 ? A ASN 171 
23 1 Y 1 B THR 941 ? A THR 172 
24 1 Y 1 B ASN 942 ? A ASN 173 
25 1 Y 1 A GLY 149 ? B GLY 150 
26 1 Y 1 A GLY 150 ? B GLY 151 
27 1 Y 1 A SER 151 ? B SER 152 
28 1 Y 1 A GLY 152 ? B GLY 153 
29 1 Y 1 A GLY 153 ? B GLY 154 
30 1 Y 1 A GLY 154 ? B GLY 155 
31 1 Y 1 A SER 155 ? B SER 156 
32 1 Y 1 A GLY 156 ? B GLY 157 
33 1 Y 1 A GLY 157 ? B GLY 158 
34 1 Y 1 A GLY 158 ? B GLY 159 
35 1 Y 1 A SER 159 ? B SER 160 
36 1 Y 1 A GLY 160 ? B GLY 161 
37 1 Y 1 A GLY 161 ? B GLY 162 
38 1 Y 1 A GLY 162 ? B GLY 163 
39 1 Y 1 A SER 163 ? B SER 164 
40 1 Y 1 A GLY 164 ? B GLY 165 
41 1 Y 1 A GLY 165 ? B GLY 166 
42 1 Y 1 A LYS 936 ? B LYS 167 
43 1 Y 1 A ASP 937 ? B ASP 168 
44 1 Y 1 A LYS 938 ? B LYS 169 
45 1 Y 1 A ASP 939 ? B ASP 170 
46 1 Y 1 A ASN 940 ? B ASN 171 
47 1 Y 1 A THR 941 ? B THR 172 
48 1 Y 1 A ASN 942 ? B ASN 173 
49 1 Y 1 A VAL 943 ? B VAL 174 
50 1 Y 1 A ASN 944 ? B ASN 175 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
PHE N    N  N N 250 
PHE CA   C  N S 251 
PHE C    C  N N 252 
PHE O    O  N N 253 
PHE CB   C  N N 254 
PHE CG   C  Y N 255 
PHE CD1  C  Y N 256 
PHE CD2  C  Y N 257 
PHE CE1  C  Y N 258 
PHE CE2  C  Y N 259 
PHE CZ   C  Y N 260 
PHE OXT  O  N N 261 
PHE H    H  N N 262 
PHE H2   H  N N 263 
PHE HA   H  N N 264 
PHE HB2  H  N N 265 
PHE HB3  H  N N 266 
PHE HD1  H  N N 267 
PHE HD2  H  N N 268 
PHE HE1  H  N N 269 
PHE HE2  H  N N 270 
PHE HZ   H  N N 271 
PHE HXT  H  N N 272 
PRO N    N  N N 273 
PRO CA   C  N S 274 
PRO C    C  N N 275 
PRO O    O  N N 276 
PRO CB   C  N N 277 
PRO CG   C  N N 278 
PRO CD   C  N N 279 
PRO OXT  O  N N 280 
PRO H    H  N N 281 
PRO HA   H  N N 282 
PRO HB2  H  N N 283 
PRO HB3  H  N N 284 
PRO HG2  H  N N 285 
PRO HG3  H  N N 286 
PRO HD2  H  N N 287 
PRO HD3  H  N N 288 
PRO HXT  H  N N 289 
SER N    N  N N 290 
SER CA   C  N S 291 
SER C    C  N N 292 
SER O    O  N N 293 
SER CB   C  N N 294 
SER OG   O  N N 295 
SER OXT  O  N N 296 
SER H    H  N N 297 
SER H2   H  N N 298 
SER HA   H  N N 299 
SER HB2  H  N N 300 
SER HB3  H  N N 301 
SER HG   H  N N 302 
SER HXT  H  N N 303 
THR N    N  N N 304 
THR CA   C  N S 305 
THR C    C  N N 306 
THR O    O  N N 307 
THR CB   C  N R 308 
THR OG1  O  N N 309 
THR CG2  C  N N 310 
THR OXT  O  N N 311 
THR H    H  N N 312 
THR H2   H  N N 313 
THR HA   H  N N 314 
THR HB   H  N N 315 
THR HG1  H  N N 316 
THR HG21 H  N N 317 
THR HG22 H  N N 318 
THR HG23 H  N N 319 
THR HXT  H  N N 320 
TRP N    N  N N 321 
TRP CA   C  N S 322 
TRP C    C  N N 323 
TRP O    O  N N 324 
TRP CB   C  N N 325 
TRP CG   C  Y N 326 
TRP CD1  C  Y N 327 
TRP CD2  C  Y N 328 
TRP NE1  N  Y N 329 
TRP CE2  C  Y N 330 
TRP CE3  C  Y N 331 
TRP CZ2  C  Y N 332 
TRP CZ3  C  Y N 333 
TRP CH2  C  Y N 334 
TRP OXT  O  N N 335 
TRP H    H  N N 336 
TRP H2   H  N N 337 
TRP HA   H  N N 338 
TRP HB2  H  N N 339 
TRP HB3  H  N N 340 
TRP HD1  H  N N 341 
TRP HE1  H  N N 342 
TRP HE3  H  N N 343 
TRP HZ2  H  N N 344 
TRP HZ3  H  N N 345 
TRP HH2  H  N N 346 
TRP HXT  H  N N 347 
TYR N    N  N N 348 
TYR CA   C  N S 349 
TYR C    C  N N 350 
TYR O    O  N N 351 
TYR CB   C  N N 352 
TYR CG   C  Y N 353 
TYR CD1  C  Y N 354 
TYR CD2  C  Y N 355 
TYR CE1  C  Y N 356 
TYR CE2  C  Y N 357 
TYR CZ   C  Y N 358 
TYR OH   O  N N 359 
TYR OXT  O  N N 360 
TYR H    H  N N 361 
TYR H2   H  N N 362 
TYR HA   H  N N 363 
TYR HB2  H  N N 364 
TYR HB3  H  N N 365 
TYR HD1  H  N N 366 
TYR HD2  H  N N 367 
TYR HE1  H  N N 368 
TYR HE2  H  N N 369 
TYR HH   H  N N 370 
TYR HXT  H  N N 371 
VAL N    N  N N 372 
VAL CA   C  N S 373 
VAL C    C  N N 374 
VAL O    O  N N 375 
VAL CB   C  N N 376 
VAL CG1  C  N N 377 
VAL CG2  C  N N 378 
VAL OXT  O  N N 379 
VAL H    H  N N 380 
VAL H2   H  N N 381 
VAL HA   H  N N 382 
VAL HB   H  N N 383 
VAL HG11 H  N N 384 
VAL HG12 H  N N 385 
VAL HG13 H  N N 386 
VAL HG21 H  N N 387 
VAL HG22 H  N N 388 
VAL HG23 H  N N 389 
VAL HXT  H  N N 390 
ZN  ZN   ZN N N 391 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Cancer Institute (NIH/NCI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'R35 CA220340' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8V0D 
_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]   0.034501 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001826 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015357 
_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]   0.007367 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 25.62398 1.50364  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 19.97189 1.75589  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 15.80542 1.70748  0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 1.23737  29.19336 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 2.14387  29.76375 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . SER A 1 1   ? -9.24605  -4.85164  45.53105  1.000 63.65495  ? 0    SER B N   1 
ATOM   2    C  CA  . SER A 1 1   ? -8.58472  -3.71377  44.91491  1.000 58.48141  ? 0    SER B CA  1 
ATOM   3    C  C   . SER A 1 1   ? -7.09797  -3.96301  44.91941  1.000 58.74512  ? 0    SER B C   1 
ATOM   4    O  O   . SER A 1 1   ? -6.61318  -4.79524  45.68592  1.000 58.33201  ? 0    SER B O   1 
ATOM   5    C  CB  . SER A 1 1   ? -8.89687  -2.42999  45.66983  1.000 62.08785  ? 0    SER B CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -8.27902  -2.44903  46.94661  1.000 57.69266  ? 0    SER B OG  1 
ATOM   7    N  N   . MET A 1 2   ? -6.37106  -3.20234  44.10226  1.000 59.22215  ? 1    MET B N   1 
ATOM   8    C  CA  . MET A 1 2   ? -4.92296  -3.36042  44.03515  1.000 60.23886  ? 1    MET B CA  1 
ATOM   9    C  C   . MET A 1 2   ? -4.28838  -3.16119  45.40755  1.000 57.01157  ? 1    MET B C   1 
ATOM   10   O  O   . MET A 1 2   ? -3.39584  -3.92089  45.80936  1.000 54.95451  ? 1    MET B O   1 
ATOM   11   C  CB  . MET A 1 2   ? -4.36544  -2.38892  42.99432  1.000 62.79271  ? 1    MET B CB  1 
ATOM   12   C  CG  . MET A 1 2   ? -2.94586  -2.67299  42.56734  1.000 72.36399  ? 1    MET B CG  1 
ATOM   13   S  SD  . MET A 1 2   ? -2.46845  -1.69372  41.12172  1.000 90.06603  ? 1    MET B SD  1 
ATOM   14   C  CE  . MET A 1 2   ? -3.76058  -2.12160  39.95848  1.000 79.38836  ? 1    MET B CE  1 
ATOM   15   N  N   . ALA A 1 3   ? -4.78202  -2.17280  46.15638  1.000 58.09444  ? 2    ALA B N   1 
ATOM   16   C  CA  . ALA A 1 3   ? -4.27691  -1.88735  47.49561  1.000 55.03638  ? 2    ALA B CA  1 
ATOM   17   C  C   . ALA A 1 3   ? -4.49958  -3.06067  48.44716  1.000 53.84493  ? 2    ALA B C   1 
ATOM   18   O  O   . ALA A 1 3   ? -3.58630  -3.46866  49.17570  1.000 51.92365  ? 2    ALA B O   1 
ATOM   19   C  CB  . ALA A 1 3   ? -4.96466  -0.63777  48.01791  1.000 54.04370  ? 2    ALA B CB  1 
ATOM   20   N  N   . LEU A 1 4   ? -5.71053  -3.62687  48.44079  1.000 54.58364  ? 3    LEU B N   1 
ATOM   21   C  CA  . LEU A 1 4   ? -6.02954  -4.73941  49.33287  1.000 53.70423  ? 3    LEU B CA  1 
ATOM   22   C  C   . LEU A 1 4   ? -5.26555  -6.00692  48.94433  1.000 54.43655  ? 3    LEU B C   1 
ATOM   23   O  O   . LEU A 1 4   ? -4.79831  -6.75342  49.81990  1.000 53.15375  ? 3    LEU B O   1 
ATOM   24   C  CB  . LEU A 1 4   ? -7.53946  -4.98391  49.32253  1.000 54.86689  ? 3    LEU B CB  1 
ATOM   25   C  CG  . LEU A 1 4   ? -8.05933  -6.14281  50.16144  1.000 56.43791  ? 3    LEU B CG  1 
ATOM   26   C  CD1 . LEU A 1 4   ? -7.72297  -5.88036  51.59354  1.000 56.67138  ? 3    LEU B CD1 1 
ATOM   27   C  CD2 . LEU A 1 4   ? -9.55415  -6.23941  49.98469  1.000 59.52644  ? 3    LEU B CD2 1 
ATOM   28   N  N   . LYS A 1 5   ? -5.12295  -6.27129  47.63627  1.000 55.90165  ? 4    LYS B N   1 
ATOM   29   C  CA  . LYS A 1 5   ? -4.31035  -7.40950  47.21773  1.000 53.55169  ? 4    LYS B CA  1 
ATOM   30   C  C   . LYS A 1 5   ? -2.87055  -7.23754  47.67164  1.000 52.13872  ? 4    LYS B C   1 
ATOM   31   O  O   . LYS A 1 5   ? -2.28070  -8.15337  48.26007  1.000 48.47004  ? 4    LYS B O   1 
ATOM   32   C  CB  . LYS A 1 5   ? -4.37442  -7.60378  45.69697  1.000 55.96500  ? 4    LYS B CB  1 
ATOM   33   C  CG  . LYS A 1 5   ? -5.76292  -7.84663  45.09833  1.000 58.65065  ? 4    LYS B CG  1 
ATOM   34   C  CD  . LYS A 1 5   ? -5.67349  -8.06769  43.58323  1.000 63.31590  ? 4    LYS B CD  1 
ATOM   35   C  CE  . LYS A 1 5   ? -6.99272  -7.76912  42.86433  1.000 67.14003  ? 4    LYS B CE  1 
ATOM   36   N  NZ  . LYS A 1 5   ? -8.07631  -8.73009  43.21438  1.000 67.71359  ? 4    LYS B NZ  1 
ATOM   37   N  N   . ARG A 1 6   ? -2.32018  -6.04353  47.48448  1.000 51.16496  ? 5    ARG B N   1 
ATOM   38   C  CA  . ARG A 1 6   ? -0.94343  -5.80691  47.88490  1.000 51.14782  ? 5    ARG B CA  1 
ATOM   39   C  C   . ARG A 1 6   ? -0.76273  -5.93201  49.40597  1.000 52.96481  ? 5    ARG B C   1 
ATOM   40   O  O   . ARG A 1 6   ? 0.24678   -6.48265  49.87361  1.000 50.29814  ? 5    ARG B O   1 
ATOM   41   C  CB  . ARG A 1 6   ? -0.52166  -4.45074  47.34252  1.000 51.36158  ? 5    ARG B CB  1 
ATOM   42   C  CG  . ARG A 1 6   ? 0.62123   -3.85473  48.03865  1.000 52.25392  ? 5    ARG B CG  1 
ATOM   43   C  CD  . ARG A 1 6   ? 1.93640   -4.32784  47.51750  1.000 54.57962  ? 5    ARG B CD  1 
ATOM   44   N  NE  . ARG A 1 6   ? 2.92688   -3.66927  48.34891  1.000 57.68233  ? 5    ARG B NE  1 
ATOM   45   C  CZ  . ARG A 1 6   ? 3.80908   -2.78843  47.91200  1.000 53.14858  ? 5    ARG B CZ  1 
ATOM   46   N  NH1 . ARG A 1 6   ? 3.93326   -2.51559  46.62329  1.000 51.61122  ? 5    ARG B NH1 1 
ATOM   47   N  NH2 . ARG A 1 6   ? 4.57189   -2.15115  48.79420  1.000 54.84984  ? 5    ARG B NH2 1 
ATOM   48   N  N   . ILE A 1 7   ? -1.75081  -5.48286  50.19119  1.000 50.82229  ? 6    ILE B N   1 
ATOM   49   C  CA  . ILE A 1 7   ? -1.69109  -5.62978  51.65135  1.000 50.12763  ? 6    ILE B CA  1 
ATOM   50   C  C   . ILE A 1 7   ? -1.71311  -7.10676  52.05672  1.000 47.48669  ? 6    ILE B C   1 
ATOM   51   O  O   . ILE A 1 7   ? -0.97384  -7.53136  52.95953  1.000 46.67257  ? 6    ILE B O   1 
ATOM   52   C  CB  . ILE A 1 7   ? -2.84874  -4.85803  52.31591  1.000 49.54332  ? 6    ILE B CB  1 
ATOM   53   C  CG1 . ILE A 1 7   ? -2.68112  -3.35303  52.14344  1.000 46.55330  ? 6    ILE B CG1 1 
ATOM   54   C  CG2 . ILE A 1 7   ? -2.90820  -5.15847  53.81386  1.000 49.01016  ? 6    ILE B CG2 1 
ATOM   55   C  CD1 . ILE A 1 7   ? -3.95632  -2.59190  52.43644  1.000 47.32479  ? 6    ILE B CD1 1 
ATOM   56   N  N   . HIS A 1 8   ? -2.56716  -7.91249  51.41711  1.000 49.29226  ? 7    HIS B N   1 
ATOM   57   C  CA  . HIS A 1 8   ? -2.54158  -9.34281  51.72020  1.000 50.80449  ? 7    HIS B CA  1 
ATOM   58   C  C   . HIS A 1 8   ? -1.19234  -9.94600  51.36617  1.000 49.97702  ? 7    HIS B C   1 
ATOM   59   O  O   . HIS A 1 8   ? -0.66950  -10.79676 52.10307  1.000 47.42343  ? 7    HIS B O   1 
ATOM   60   C  CB  . HIS A 1 8   ? -3.66039  -10.07372 50.99038  1.000 50.23034  ? 7    HIS B CB  1 
ATOM   61   C  CG  . HIS A 1 8   ? -4.96183  -10.01213 51.70923  1.000 55.61022  ? 7    HIS B CG  1 
ATOM   62   N  ND1 . HIS A 1 8   ? -6.04047  -9.30714  51.22898  1.000 57.17861  ? 7    HIS B ND1 1 
ATOM   63   C  CD2 . HIS A 1 8   ? -5.35788  -10.55638 52.88233  1.000 61.71878  ? 7    HIS B CD2 1 
ATOM   64   C  CE1 . HIS A 1 8   ? -7.04880  -9.41916  52.07339  1.000 59.81406  ? 7    HIS B CE1 1 
ATOM   65   N  NE2 . HIS A 1 8   ? -6.66021  -10.17241 53.08557  1.000 61.28152  ? 7    HIS B NE2 1 
ATOM   66   N  N   . LYS A 1 9   ? -0.61303  -9.50805  50.24024  1.000 49.16671  ? 8    LYS B N   1 
ATOM   67   C  CA  . LYS A 1 9   ? 0.67600   -10.04016 49.80693  1.000 51.96717  ? 8    LYS B CA  1 
ATOM   68   C  C   . LYS A 1 9   ? 1.76735   -9.74660  50.82053  1.000 47.67482  ? 8    LYS B C   1 
ATOM   69   O  O   . LYS A 1 9   ? 2.54365   -10.64088 51.18721  1.000 48.34193  ? 8    LYS B O   1 
ATOM   70   C  CB  . LYS A 1 9   ? 1.05441   -9.46124  48.44042  1.000 49.96521  ? 8    LYS B CB  1 
ATOM   71   C  CG  . LYS A 1 9   ? 2.41099   -9.90280  47.92778  1.000 50.77566  ? 8    LYS B CG  1 
ATOM   72   C  CD  . LYS A 1 9   ? 2.42572   -11.37268 47.58398  1.000 51.11998  ? 8    LYS B CD  1 
ATOM   73   C  CE  . LYS A 1 9   ? 3.83832   -11.88899 47.36325  1.000 56.51802  ? 8    LYS B CE  1 
ATOM   74   N  NZ  . LYS A 1 9   ? 3.84013   -13.34928 47.00730  1.000 63.93071  ? 8    LYS B NZ  1 
ATOM   75   N  N   . GLU A 1 10  ? 1.81008   -8.51252  51.31382  1.000 44.19440  ? 9    GLU B N   1 
ATOM   76   C  CA  . GLU A 1 10  ? 2.82885   -8.13786  52.28643  1.000 45.57283  ? 9    GLU B CA  1 
ATOM   77   C  C   . GLU A 1 10  ? 2.64054   -8.91237  53.57513  1.000 44.80779  ? 9    GLU B C   1 
ATOM   78   O  O   . GLU A 1 10  ? 3.62003   -9.31050  54.21408  1.000 43.30473  ? 9    GLU B O   1 
ATOM   79   C  CB  . GLU A 1 10  ? 2.76952   -6.63220  52.58013  1.000 45.29672  ? 9    GLU B CB  1 
ATOM   80   C  CG  . GLU A 1 10  ? 3.29099   -5.74708  51.46791  1.000 46.26317  ? 9    GLU B CG  1 
ATOM   81   C  CD  . GLU A 1 10  ? 3.47635   -4.29833  51.87554  1.000 46.91627  ? 9    GLU B CD  1 
ATOM   82   O  OE1 . GLU A 1 10  ? 4.14574   -4.04546  52.89186  1.000 45.99676  ? 9    GLU B OE1 1 
ATOM   83   O  OE2 . GLU A 1 10  ? 2.95053   -3.40835  51.17163  1.000 48.79211  ? 9    GLU B OE2 1 
ATOM   84   N  N   . LEU A 1 11  ? 1.38251   -9.16618  53.94808  1.000 42.80119  ? 10   LEU B N   1 
ATOM   85   C  CA  . LEU A 1 11  ? 1.11119   -9.93635  55.15562  1.000 47.03120  ? 10   LEU B CA  1 
ATOM   86   C  C   . LEU A 1 11  ? 1.59734   -11.37528 55.02999  1.000 47.20461  ? 10   LEU B C   1 
ATOM   87   O  O   . LEU A 1 11  ? 2.21463   -11.91353 55.95935  1.000 45.24832  ? 10   LEU B O   1 
ATOM   88   C  CB  . LEU A 1 11  ? -0.38413  -9.90360  55.45448  1.000 47.70556  ? 10   LEU B CB  1 
ATOM   89   C  CG  . LEU A 1 11  ? -0.78554  -10.46744 56.80656  1.000 52.31585  ? 10   LEU B CG  1 
ATOM   90   C  CD1 . LEU A 1 11  ? 0.04324   -9.85735  57.92648  1.000 54.95495  ? 10   LEU B CD1 1 
ATOM   91   C  CD2 . LEU A 1 11  ? -2.26983  -10.20199 56.99950  1.000 55.63307  ? 10   LEU B CD2 1 
ATOM   92   N  N   . ASN A 1 12  ? 1.35510   -12.00336 53.88015  1.000 48.68202  ? 11   ASN B N   1 
ATOM   93   C  CA  . ASN A 1 12  ? 1.84002   -13.36696 53.69253  1.000 49.22764  ? 11   ASN B CA  1 
ATOM   94   C  C   . ASN A 1 12  ? 3.35803   -13.41681 53.66928  1.000 48.69368  ? 11   ASN B C   1 
ATOM   95   O  O   . ASN A 1 12  ? 3.95903   -14.31944 54.26057  1.000 49.71641  ? 11   ASN B O   1 
ATOM   96   C  CB  . ASN A 1 12  ? 1.26188   -13.96569 52.41793  1.000 52.19653  ? 11   ASN B CB  1 
ATOM   97   C  CG  . ASN A 1 12  ? -0.23862  -14.10883 52.48384  1.000 54.86029  ? 11   ASN B CG  1 
ATOM   98   O  OD1 . ASN A 1 12  ? -0.78465  -14.49024 53.51220  1.000 64.58390  ? 11   ASN B OD1 1 
ATOM   99   N  ND2 . ASN A 1 12  ? -0.91848  -13.75939 51.40270  1.000 58.57251  ? 11   ASN B ND2 1 
ATOM   100  N  N   . ASP A 1 13  ? 4.00186   -12.44656 53.02076  1.000 47.35886  ? 12   ASP B N   1 
ATOM   101  C  CA  . ASP A 1 13  ? 5.46133   -12.47119 52.99394  1.000 50.17745  ? 12   ASP B CA  1 
ATOM   102  C  C   . ASP A 1 13  ? 6.05768   -12.20661 54.36892  1.000 47.89819  ? 12   ASP B C   1 
ATOM   103  O  O   . ASP A 1 13  ? 7.05744   -12.83541 54.73655  1.000 44.96541  ? 12   ASP B O   1 
ATOM   104  C  CB  . ASP A 1 13  ? 5.98404   -11.45118 51.98417  1.000 49.09249  ? 12   ASP B CB  1 
ATOM   105  C  CG  . ASP A 1 13  ? 5.61272   -11.80621 50.54855  1.000 53.02994  ? 12   ASP B CG  1 
ATOM   106  O  OD1 . ASP A 1 13  ? 4.97048   -12.86778 50.34692  1.000 52.64169  ? 12   ASP B OD1 1 
ATOM   107  O  OD2 . ASP A 1 13  ? 5.96265   -11.02343 49.63035  1.000 53.09750  ? 12   ASP B OD2 1 
ATOM   108  N  N   . LEU A 1 14  ? 5.39351   -11.38037 55.18219  1.000 46.97109  ? 13   LEU B N   1 
ATOM   109  C  CA  . LEU A 1 14  ? 5.85331   -11.16887 56.54482  1.000 45.85294  ? 13   LEU B CA  1 
ATOM   110  C  C   . LEU A 1 14  ? 5.65082   -12.40354 57.39714  1.000 46.84659  ? 13   LEU B C   1 
ATOM   111  O  O   . LEU A 1 14  ? 6.49305   -12.70847 58.24676  1.000 46.10126  ? 13   LEU B O   1 
ATOM   112  C  CB  . LEU A 1 14  ? 5.06595   -10.03272 57.18280  1.000 47.18349  ? 13   LEU B CB  1 
ATOM   113  C  CG  . LEU A 1 14  ? 5.42566   -8.60597  56.83826  1.000 45.82469  ? 13   LEU B CG  1 
ATOM   114  C  CD1 . LEU A 1 14  ? 4.31767   -7.74558  57.36751  1.000 44.34581  ? 13   LEU B CD1 1 
ATOM   115  C  CD2 . LEU A 1 14  ? 6.73652   -8.30665  57.51789  1.000 46.28934  ? 13   LEU B CD2 1 
ATOM   116  N  N   . ALA A 1 15  ? 4.62751   -13.19556 57.08669  1.000 46.57724  ? 14   ALA B N   1 
ATOM   117  C  CA  . ALA A 1 15  ? 4.37796   -14.37275 57.90265  1.000 46.97791  ? 14   ALA B CA  1 
ATOM   118  C  C   . ALA A 1 15  ? 5.28947   -15.52934 57.51226  1.000 49.61977  ? 14   ALA B C   1 
ATOM   119  O  O   . ALA A 1 15  ? 5.84570   -16.18923 58.39354  1.000 46.90350  ? 14   ALA B O   1 
ATOM   120  C  CB  . ALA A 1 15  ? 2.90800   -14.78762 57.79205  1.000 46.12870  ? 14   ALA B CB  1 
ATOM   121  N  N   . ARG A 1 16  ? 5.52044   -15.74379 56.21005  1.000 48.97804  ? 15   ARG B N   1 
ATOM   122  C  CA  . ARG A 1 16  ? 6.41225   -16.81936 55.78033  1.000 50.67436  ? 15   ARG B CA  1 
ATOM   123  C  C   . ARG A 1 16  ? 7.88127   -16.45078 55.91377  1.000 49.91758  ? 15   ARG B C   1 
ATOM   124  O  O   . ARG A 1 16  ? 8.72781   -17.34676 55.93998  1.000 54.87777  ? 15   ARG B O   1 
ATOM   125  C  CB  . ARG A 1 16  ? 6.15926   -17.24536 54.32527  1.000 55.43684  ? 15   ARG B CB  1 
ATOM   126  C  CG  . ARG A 1 16  ? 4.75293   -17.70291 53.97236  1.000 57.03787  ? 15   ARG B CG  1 
ATOM   127  C  CD  . ARG A 1 16  ? 4.67042   -18.01890 52.48218  1.000 64.50993  ? 15   ARG B CD  1 
ATOM   128  N  NE  . ARG A 1 16  ? 5.14155   -16.87857 51.70420  1.000 75.26997  ? 15   ARG B NE  1 
ATOM   129  C  CZ  . ARG A 1 16  ? 6.27660   -16.85320 51.01506  1.000 80.95440  ? 15   ARG B CZ  1 
ATOM   130  N  NH1 . ARG A 1 16  ? 7.03430   -17.93328 50.88523  1.000 75.64212  ? 15   ARG B NH1 1 
ATOM   131  N  NH2 . ARG A 1 16  ? 6.67231   -15.70991 50.46021  1.000 69.82691  ? 15   ARG B NH2 1 
ATOM   132  N  N   . ASP A 1 17  ? 8.20266   -15.16806 56.03180  1.000 51.84864  ? 16   ASP B N   1 
ATOM   133  C  CA  . ASP A 1 17  ? 9.58508   -14.70350 56.16687  1.000 53.40771  ? 16   ASP B CA  1 
ATOM   134  C  C   . ASP A 1 17  ? 9.59833   -13.67460 57.27272  1.000 52.50593  ? 16   ASP B C   1 
ATOM   135  O  O   . ASP A 1 17  ? 9.74208   -12.47019 57.02941  1.000 61.42434  ? 16   ASP B O   1 
ATOM   136  C  CB  . ASP A 1 17  ? 10.09904  -14.07564 54.87211  1.000 57.25453  ? 16   ASP B CB  1 
ATOM   137  C  CG  . ASP A 1 17  ? 11.58922  -13.81017 54.90751  1.000 61.26311  ? 16   ASP B CG  1 
ATOM   138  O  OD1 . ASP A 1 17  ? 12.21675  -14.02582 55.96398  1.000 58.31487  ? 16   ASP B OD1 1 
ATOM   139  O  OD2 . ASP A 1 17  ? 12.10274  -13.23390 53.92509  1.000 74.76482  ? 16   ASP B OD2 1 
ATOM   140  N  N   . PRO A 1 18  ? 9.43610   -14.11815 58.51718  1.000 51.47089  ? 17   PRO B N   1 
ATOM   141  C  CA  . PRO A 1 18  ? 9.28934   -13.16947 59.60757  1.000 48.07013  ? 17   PRO B CA  1 
ATOM   142  C  C   . PRO A 1 18  ? 10.57773  -12.38980 59.84335  1.000 47.36084  ? 17   PRO B C   1 
ATOM   143  O  O   . PRO A 1 18  ? 11.67904  -12.95171 59.76230  1.000 48.29046  ? 17   PRO B O   1 
ATOM   144  C  CB  . PRO A 1 18  ? 8.95232   -14.06407 60.81277  1.000 45.84012  ? 17   PRO B CB  1 
ATOM   145  C  CG  . PRO A 1 18  ? 9.54711   -15.38626 60.46342  1.000 48.30748  ? 17   PRO B CG  1 
ATOM   146  C  CD  . PRO A 1 18  ? 9.35365   -15.51299 58.98454  1.000 50.04946  ? 17   PRO B CD  1 
ATOM   147  N  N   . PRO A 1 19  ? 10.46522  -11.12740 60.22296  1.000 44.08746  ? 18   PRO B N   1 
ATOM   148  C  CA  . PRO A 1 19  ? 11.64249  -10.41605 60.71858  1.000 46.10634  ? 18   PRO B CA  1 
ATOM   149  C  C   . PRO A 1 19  ? 11.99439  -11.00033 62.07071  1.000 48.08754  ? 18   PRO B C   1 
ATOM   150  O  O   . PRO A 1 19  ? 11.17313  -11.66514 62.71124  1.000 46.97867  ? 18   PRO B O   1 
ATOM   151  C  CB  . PRO A 1 19  ? 11.16646  -8.96184  60.84234  1.000 43.33192  ? 18   PRO B CB  1 
ATOM   152  C  CG  . PRO A 1 19  ? 9.90854   -8.88821  60.03787  1.000 40.89903  ? 18   PRO B CG  1 
ATOM   153  C  CD  . PRO A 1 19  ? 9.28854   -10.25179 60.16044  1.000 44.48657  ? 18   PRO B CD  1 
ATOM   154  N  N   . ALA A 1 20  ? 13.26509  -10.88701 62.44347  1.000 47.23616  ? 19   ALA B N   1 
ATOM   155  C  CA  . ALA A 1 20  ? 13.65165  -11.42987 63.73825  1.000 48.08409  ? 19   ALA B CA  1 
ATOM   156  C  C   . ALA A 1 20  ? 13.02491  -10.62392 64.87899  1.000 48.59713  ? 19   ALA B C   1 
ATOM   157  O  O   . ALA A 1 20  ? 12.61450  -11.19970 65.89618  1.000 44.77753  ? 19   ALA B O   1 
ATOM   158  C  CB  . ALA A 1 20  ? 15.17351  -11.46927 63.86772  1.000 44.73427  ? 19   ALA B CB  1 
ATOM   159  N  N   . GLN A 1 21  ? 12.98826  -9.29840  64.76443  1.000 42.95417  ? 20   GLN B N   1 
ATOM   160  C  CA  . GLN A 1 21  ? 12.50135  -8.49592  65.87866  1.000 45.85272  ? 20   GLN B CA  1 
ATOM   161  C  C   . GLN A 1 21  ? 11.19719  -7.73725  65.63104  1.000 44.74607  ? 20   GLN B C   1 
ATOM   162  O  O   . GLN A 1 21  ? 10.36766  -7.68638  66.54316  1.000 45.18780  ? 20   GLN B O   1 
ATOM   163  C  CB  . GLN A 1 21  ? 13.59208  -7.51264  66.31978  1.000 46.18950  ? 20   GLN B CB  1 
ATOM   164  C  CG  . GLN A 1 21  ? 14.85345  -8.18243  66.83307  1.000 48.56039  ? 20   GLN B CG  1 
ATOM   165  C  CD  . GLN A 1 21  ? 15.80375  -7.21144  67.52479  1.000 54.15388  ? 20   GLN B CD  1 
ATOM   166  O  OE1 . GLN A 1 21  ? 16.43107  -6.36685  66.88001  1.000 55.27117  ? 20   GLN B OE1 1 
ATOM   167  N  NE2 . GLN A 1 21  ? 15.90575  -7.32389  68.84437  1.000 59.39185  ? 20   GLN B NE2 1 
ATOM   168  N  N   . CYS A 1 22  ? 10.92925  -7.25019  64.41725  1.000 42.82414  ? 21   CYS B N   1 
ATOM   169  C  CA  . CYS A 1 22  ? 9.77239   -6.38511  64.23350  1.000 46.54334  ? 21   CYS B CA  1 
ATOM   170  C  C   . CYS A 1 22  ? 8.53169   -7.23135  64.00806  1.000 45.43063  ? 21   CYS B C   1 
ATOM   171  O  O   . CYS A 1 22  ? 8.61362   -8.41807  63.69993  1.000 52.83640  ? 21   CYS B O   1 
ATOM   172  C  CB  . CYS A 1 22  ? 9.96569   -5.46539  63.02748  1.000 48.05024  ? 21   CYS B CB  1 
ATOM   173  S  SG  . CYS A 1 22  ? 11.62994  -4.85306  62.86236  1.000 62.98471  ? 21   CYS B SG  1 
ATOM   174  N  N   . SER A 1 23  ? 7.37568   -6.57827  64.01319  1.000 43.78829  ? 22   SER B N   1 
ATOM   175  C  CA  . SER A 1 23  ? 6.14095   -7.32916  63.82776  1.000 43.38016  ? 22   SER B CA  1 
ATOM   176  C  C   . SER A 1 23  ? 5.04685   -6.37675  63.36493  1.000 42.11622  ? 22   SER B C   1 
ATOM   177  O  O   . SER A 1 23  ? 5.03064   -5.22010  63.77531  1.000 40.04909  ? 22   SER B O   1 
ATOM   178  C  CB  . SER A 1 23  ? 5.75837   -8.04446  65.13876  1.000 42.99391  ? 22   SER B CB  1 
ATOM   179  O  OG  . SER A 1 23  ? 4.40440   -8.45461  65.15833  1.000 46.01600  ? 22   SER B OG  1 
ATOM   180  N  N   . ALA A 1 24  ? 4.18565   -6.83433  62.45397  1.000 41.25600  ? 23   ALA B N   1 
ATOM   181  C  CA  . ALA A 1 24  ? 3.13581   -5.94763  61.96420  1.000 41.60427  ? 23   ALA B CA  1 
ATOM   182  C  C   . ALA A 1 24  ? 1.97368   -6.75073  61.39217  1.000 40.35529  ? 23   ALA B C   1 
ATOM   183  O  O   . ALA A 1 24  ? 2.18985   -7.70638  60.64865  1.000 41.80950  ? 23   ALA B O   1 
ATOM   184  C  CB  . ALA A 1 24  ? 3.68640   -4.99973  60.88810  1.000 39.42377  ? 23   ALA B CB  1 
ATOM   185  N  N   . GLY A 1 25  ? 0.74760   -6.29496  61.65871  1.000 40.38571  ? 24   GLY B N   1 
ATOM   186  C  CA  . GLY A 1 25  ? -0.42998  -6.93713  61.11744  1.000 41.48314  ? 24   GLY B CA  1 
ATOM   187  C  C   . GLY A 1 25  ? -1.73934  -6.21730  61.37613  1.000 45.38387  ? 24   GLY B C   1 
ATOM   188  O  O   . GLY A 1 25  ? -1.81818  -5.27662  62.17008  1.000 47.07388  ? 24   GLY B O   1 
ATOM   189  N  N   . PRO A 1 26  ? -2.80729  -6.67907  60.72330  1.000 47.95786  ? 25   PRO B N   1 
ATOM   190  C  CA  . PRO A 1 26  ? -4.12296  -6.04419  60.89482  1.000 50.81402  ? 25   PRO B CA  1 
ATOM   191  C  C   . PRO A 1 26  ? -4.57918  -6.10579  62.34066  1.000 55.61541  ? 25   PRO B C   1 
ATOM   192  O  O   . PRO A 1 26  ? -4.35902  -7.10154  63.03578  1.000 59.06673  ? 25   PRO B O   1 
ATOM   193  C  CB  . PRO A 1 26  ? -5.04095  -6.88874  60.00120  1.000 53.01057  ? 25   PRO B CB  1 
ATOM   194  C  CG  . PRO A 1 26  ? -4.11632  -7.52473  59.02894  1.000 50.07380  ? 25   PRO B CG  1 
ATOM   195  C  CD  . PRO A 1 26  ? -2.86386  -7.79707  59.77738  1.000 45.42399  ? 25   PRO B CD  1 
ATOM   196  N  N   . VAL A 1 27  ? -5.24026  -5.03993  62.79952  1.000 61.98156  ? 26   VAL B N   1 
ATOM   197  C  CA  . VAL A 1 27  ? -5.73924  -5.06765  64.17142  1.000 61.01890  ? 26   VAL B CA  1 
ATOM   198  C  C   . VAL A 1 27  ? -6.97556  -5.96048  64.28643  1.000 61.24625  ? 26   VAL B C   1 
ATOM   199  O  O   . VAL A 1 27  ? -7.07088  -6.78502  65.20462  1.000 65.93757  ? 26   VAL B O   1 
ATOM   200  C  CB  . VAL A 1 27  ? -5.96093  -3.64763  64.71383  1.000 64.85634  ? 26   VAL B CB  1 
ATOM   201  C  CG1 . VAL A 1 27  ? -4.54602  -2.97847  64.99344  1.000 58.43114  ? 26   VAL B CG1 1 
ATOM   202  C  CG2 . VAL A 1 27  ? -6.88309  -2.87418  63.72094  1.000 64.46019  ? 26   VAL B CG2 1 
ATOM   203  N  N   . GLY A 1 28  ? -7.94640  -5.81017  63.38184  1.000 59.12807  ? 27   GLY B N   1 
ATOM   204  C  CA  . GLY A 1 28  ? -9.05794  -6.75726  63.37363  1.000 56.96614  ? 27   GLY B CA  1 
ATOM   205  C  C   . GLY A 1 28  ? -9.43115  -7.24910  61.98773  1.000 57.19630  ? 27   GLY B C   1 
ATOM   206  O  O   . GLY A 1 28  ? -8.64127  -7.93789  61.33517  1.000 55.48241  ? 27   GLY B O   1 
ATOM   207  N  N   . ASP A 1 29  ? -10.61203 -6.85580  61.50600  1.000 60.95300  ? 28   ASP B N   1 
ATOM   208  C  CA  . ASP A 1 29  ? -11.05054 -7.18113  60.15293  1.000 60.99481  ? 28   ASP B CA  1 
ATOM   209  C  C   . ASP A 1 29  ? -10.71922 -6.08045  59.15533  1.000 59.29765  ? 28   ASP B C   1 
ATOM   210  O  O   . ASP A 1 29  ? -10.97353 -6.24647  57.95823  1.000 61.57493  ? 28   ASP B O   1 
ATOM   211  C  CB  . ASP A 1 29  ? -12.57058 -7.42005  60.11826  1.000 61.59316  ? 28   ASP B CB  1 
ATOM   212  C  CG  . ASP A 1 29  ? -12.96318 -8.75724  60.68546  1.000 60.26504  ? 28   ASP B CG  1 
ATOM   213  O  OD1 . ASP A 1 29  ? -12.05602 -9.57943  60.89514  1.000 61.19852  ? 28   ASP B OD1 1 
ATOM   214  O  OD2 . ASP A 1 29  ? -14.17630 -9.00504  60.88127  1.000 61.05341  ? 28   ASP B OD2 1 
ATOM   215  N  N   . ASP A 1 30  ? -10.13549 -4.97589  59.61360  1.000 56.89420  ? 29   ASP B N   1 
ATOM   216  C  CA  . ASP A 1 30  ? -9.77588  -3.85146  58.74943  1.000 57.55965  ? 29   ASP B CA  1 
ATOM   217  C  C   . ASP A 1 30  ? -8.34450  -4.07549  58.28457  1.000 55.56105  ? 29   ASP B C   1 
ATOM   218  O  O   . ASP A 1 30  ? -7.39061  -3.86712  59.04126  1.000 54.50691  ? 29   ASP B O   1 
ATOM   219  C  CB  . ASP A 1 30  ? -9.91901  -2.51257  59.47187  1.000 55.98013  ? 29   ASP B CB  1 
ATOM   220  C  CG  . ASP A 1 30  ? -9.77143  -1.32735  58.52713  1.000 56.29974  ? 29   ASP B CG  1 
ATOM   221  O  OD1 . ASP A 1 30  ? -9.87159  -1.55392  57.30035  1.000 56.64086  ? 29   ASP B OD1 1 
ATOM   222  O  OD2 . ASP A 1 30  ? -9.56822  -0.18001  58.99101  1.000 62.91645  ? 29   ASP B OD2 1 
ATOM   223  N  N   . MET A 1 31  ? -8.19392  -4.50729  57.03422  1.000 55.00731  ? 30   MET B N   1 
ATOM   224  C  CA  . MET A 1 31  ? -6.86400  -4.70878  56.47575  1.000 57.27364  ? 30   MET B CA  1 
ATOM   225  C  C   . MET A 1 31  ? -6.13426  -3.40140  56.23221  1.000 53.10874  ? 30   MET B C   1 
ATOM   226  O  O   . MET A 1 31  ? -4.90863  -3.40810  56.07668  1.000 50.23474  ? 30   MET B O   1 
ATOM   227  C  CB  . MET A 1 31  ? -6.94310  -5.48848  55.17093  1.000 56.28964  ? 30   MET B CB  1 
ATOM   228  C  CG  . MET A 1 31  ? -7.57976  -6.82374  55.34325  1.000 60.99439  ? 30   MET B CG  1 
ATOM   229  S  SD  . MET A 1 31  ? -6.51292  -7.78861  56.42267  1.000 66.48831  ? 30   MET B SD  1 
ATOM   230  C  CE  . MET A 1 31  ? -4.94135  -7.68362  55.56249  1.000 55.20623  ? 30   MET B CE  1 
ATOM   231  N  N   . PHE A 1 32  ? -6.84609  -2.28476  56.20385  1.000 53.21382  ? 31   PHE B N   1 
ATOM   232  C  CA  . PHE A 1 32  ? -6.22105  -1.00467  55.93025  1.000 53.20264  ? 31   PHE B CA  1 
ATOM   233  C  C   . PHE A 1 32  ? -5.74846  -0.30416  57.20288  1.000 52.73237  ? 31   PHE B C   1 
ATOM   234  O  O   . PHE A 1 32  ? -5.21342  0.80523   57.12156  1.000 49.24823  ? 31   PHE B O   1 
ATOM   235  C  CB  . PHE A 1 32  ? -7.19663  -0.12291  55.14165  1.000 51.88665  ? 31   PHE B CB  1 
ATOM   236  C  CG  . PHE A 1 32  ? -7.36685  -0.53760  53.69451  1.000 50.85436  ? 31   PHE B CG  1 
ATOM   237  C  CD1 . PHE A 1 32  ? -8.26161  -1.54849  53.34616  1.000 52.87885  ? 31   PHE B CD1 1 
ATOM   238  C  CD2 . PHE A 1 32  ? -6.66766  0.10365   52.68061  1.000 51.13703  ? 31   PHE B CD2 1 
ATOM   239  C  CE1 . PHE A 1 32  ? -8.43350  -1.92807  52.02050  1.000 53.13141  ? 31   PHE B CE1 1 
ATOM   240  C  CE2 . PHE A 1 32  ? -6.84108  -0.27427  51.34543  1.000 52.53640  ? 31   PHE B CE2 1 
ATOM   241  C  CZ  . PHE A 1 32  ? -7.72005  -1.28904  51.02182  1.000 52.97645  ? 31   PHE B CZ  1 
ATOM   242  N  N   . HIS A 1 33  ? -5.87533  -0.95289  58.36320  1.000 52.97528  ? 32   HIS B N   1 
ATOM   243  C  CA  . HIS A 1 33  ? -5.33937  -0.43755  59.62169  1.000 52.60193  ? 32   HIS B CA  1 
ATOM   244  C  C   . HIS A 1 33  ? -4.56367  -1.55118  60.32050  1.000 53.04359  ? 32   HIS B C   1 
ATOM   245  O  O   . HIS A 1 33  ? -5.13995  -2.58444  60.68860  1.000 53.31043  ? 32   HIS B O   1 
ATOM   246  C  CB  . HIS A 1 33  ? -6.45362  0.11487   60.52563  1.000 53.93284  ? 32   HIS B CB  1 
ATOM   247  C  CG  . HIS A 1 33  ? -5.96236  0.60061   61.85584  1.000 59.98488  ? 32   HIS B CG  1 
ATOM   248  N  ND1 . HIS A 1 33  ? -6.64486  0.37423   63.03171  1.000 61.89057  ? 32   HIS B ND1 1 
ATOM   249  C  CD2 . HIS A 1 33  ? -4.84937  1.29483   62.19631  1.000 57.13582  ? 32   HIS B CD2 1 
ATOM   250  C  CE1 . HIS A 1 33  ? -5.96620  0.89716   64.03859  1.000 60.65550  ? 32   HIS B CE1 1 
ATOM   251  N  NE2 . HIS A 1 33  ? -4.87803  1.46982   63.55772  1.000 57.08244  ? 32   HIS B NE2 1 
ATOM   252  N  N   . TRP A 1 34  ? -3.25595  -1.34413  60.48269  1.000 49.07046  ? 33   TRP B N   1 
ATOM   253  C  CA  . TRP A 1 34  ? -2.35928  -2.29654  61.12247  1.000 47.96606  ? 33   TRP B CA  1 
ATOM   254  C  C   . TRP A 1 34  ? -1.79599  -1.74645  62.42428  1.000 47.27040  ? 33   TRP B C   1 
ATOM   255  O  O   . TRP A 1 34  ? -1.71463  -0.53526  62.64550  1.000 48.45233  ? 33   TRP B O   1 
ATOM   256  C  CB  . TRP A 1 34  ? -1.16694  -2.66759  60.21582  1.000 45.60135  ? 33   TRP B CB  1 
ATOM   257  C  CG  . TRP A 1 34  ? -1.43914  -3.56787  59.04503  1.000 44.71078  ? 33   TRP B CG  1 
ATOM   258  C  CD1 . TRP A 1 34  ? -2.65059  -3.89412  58.51908  1.000 45.49295  ? 33   TRP B CD1 1 
ATOM   259  C  CD2 . TRP A 1 34  ? -0.45848  -4.26907  58.26699  1.000 45.06529  ? 33   TRP B CD2 1 
ATOM   260  N  NE1 . TRP A 1 34  ? -2.48873  -4.75032  57.45519  1.000 47.14444  ? 33   TRP B NE1 1 
ATOM   261  C  CE2 . TRP A 1 34  ? -1.15109  -4.98815  57.27268  1.000 45.75681  ? 33   TRP B CE2 1 
ATOM   262  C  CE3 . TRP A 1 34  ? 0.93769   -4.34316  58.30523  1.000 44.48178  ? 33   TRP B CE3 1 
ATOM   263  C  CZ2 . TRP A 1 34  ? -0.49656  -5.79101  56.33183  1.000 47.01910  ? 33   TRP B CZ2 1 
ATOM   264  C  CZ3 . TRP A 1 34  ? 1.59097   -5.13712  57.36275  1.000 45.95219  ? 33   TRP B CZ3 1 
ATOM   265  C  CH2 . TRP A 1 34  ? 0.86988   -5.85254  56.39174  1.000 46.46581  ? 33   TRP B CH2 1 
ATOM   266  N  N   . GLN A 1 35  ? -1.33921  -2.67100  63.25211  1.000 47.74765  ? 34   GLN B N   1 
ATOM   267  C  CA  . GLN A 1 35  ? -0.46898  -2.37111  64.37260  1.000 47.43934  ? 34   GLN B CA  1 
ATOM   268  C  C   . GLN A 1 35  ? 0.90728   -2.94751  64.07152  1.000 44.03971  ? 34   GLN B C   1 
ATOM   269  O  O   . GLN A 1 35  ? 1.02347   -4.00897  63.44631  1.000 38.86981  ? 34   GLN B O   1 
ATOM   270  C  CB  . GLN A 1 35  ? -1.01472  -2.96587  65.67836  1.000 48.98330  ? 34   GLN B CB  1 
ATOM   271  C  CG  . GLN A 1 35  ? -0.00384  -2.99857  66.80023  1.000 49.58969  ? 34   GLN B CG  1 
ATOM   272  C  CD  . GLN A 1 35  ? -0.59003  -3.46768  68.11628  1.000 55.77031  ? 34   GLN B CD  1 
ATOM   273  O  OE1 . GLN A 1 35  ? -0.77314  -4.65856  68.32556  1.000 58.68167  ? 34   GLN B OE1 1 
ATOM   274  N  NE2 . GLN A 1 35  ? -0.86552  -2.53892  69.01377  1.000 58.00010  ? 34   GLN B NE2 1 
ATOM   275  N  N   . ALA A 1 36  ? 1.94701   -2.22850  64.47822  1.000 42.83272  ? 35   ALA B N   1 
ATOM   276  C  CA  . ALA A 1 36  ? 3.31060   -2.70187  64.33005  1.000 42.40789  ? 35   ALA B CA  1 
ATOM   277  C  C   . ALA A 1 36  ? 4.01817   -2.56492  65.66487  1.000 39.95043  ? 35   ALA B C   1 
ATOM   278  O  O   . ALA A 1 36  ? 3.59597   -1.81243  66.54240  1.000 44.64421  ? 35   ALA B O   1 
ATOM   279  C  CB  . ALA A 1 36  ? 4.08923   -1.93909  63.22905  1.000 40.93935  ? 35   ALA B CB  1 
ATOM   280  N  N   . THR A 1 37  ? 5.08817   -3.32358  65.79910  1.000 39.33490  ? 36   THR B N   1 
ATOM   281  C  CA  . THR A 1 37  ? 5.92288   -3.40858  66.98088  1.000 41.66301  ? 36   THR B CA  1 
ATOM   282  C  C   . THR A 1 37  ? 7.37355   -3.39401  66.53607  1.000 42.74515  ? 36   THR B C   1 
ATOM   283  O  O   . THR A 1 37  ? 7.73527   -4.08041  65.57333  1.000 45.64154  ? 36   THR B O   1 
ATOM   284  C  CB  . THR A 1 37  ? 5.61758   -4.69006  67.77065  1.000 47.30860  ? 36   THR B CB  1 
ATOM   285  O  OG1 . THR A 1 37  ? 4.45863   -4.49428  68.59500  1.000 47.17458  ? 36   THR B OG1 1 
ATOM   286  C  CG2 . THR A 1 37  ? 6.81121   -5.12003  68.60200  1.000 47.47190  ? 36   THR B CG2 1 
ATOM   287  N  N   . ILE A 1 38  ? 8.18550   -2.59086  67.21233  1.000 43.48609  ? 37   ILE B N   1 
ATOM   288  C  CA  . ILE A 1 38  ? 9.61324   -2.50209  66.96055  1.000 44.85425  ? 37   ILE B CA  1 
ATOM   289  C  C   . ILE A 1 38  ? 10.35085  -2.67568  68.28139  1.000 46.07953  ? 37   ILE B C   1 
ATOM   290  O  O   . ILE A 1 38  ? 10.01878  -2.01243  69.27148  1.000 44.76887  ? 37   ILE B O   1 
ATOM   291  C  CB  . ILE A 1 38  ? 9.95276   -1.14448  66.30563  1.000 47.33844  ? 37   ILE B CB  1 
ATOM   292  C  CG1 . ILE A 1 38  ? 9.57962   -1.14554  64.82742  1.000 46.19318  ? 37   ILE B CG1 1 
ATOM   293  C  CG2 . ILE A 1 38  ? 11.40432  -0.78699  66.48361  1.000 48.93361  ? 37   ILE B CG2 1 
ATOM   294  C  CD1 . ILE A 1 38  ? 9.73751   0.22484   64.21294  1.000 45.22336  ? 37   ILE B CD1 1 
ATOM   295  N  N   . MET A 1 39  ? 11.37482  -3.52801  68.28494  1.000 47.52163  ? 38   MET B N   1 
ATOM   296  C  CA  . MET A 1 39  ? 12.24584  -3.68896  69.44190  1.000 48.61386  ? 38   MET B CA  1 
ATOM   297  C  C   . MET A 1 39  ? 13.39538  -2.71359  69.30105  1.000 53.23306  ? 38   MET B C   1 
ATOM   298  O  O   . MET A 1 39  ? 13.91078  -2.50473  68.20000  1.000 52.45959  ? 38   MET B O   1 
ATOM   299  C  CB  . MET A 1 39  ? 12.79828  -5.11420  69.59655  1.000 50.44329  ? 38   MET B CB  1 
ATOM   300  C  CG  . MET A 1 39  ? 11.78094  -6.23410  69.58902  1.000 50.39465  ? 38   MET B CG  1 
ATOM   301  S  SD  . MET A 1 39  ? 12.47042  -7.91021  69.69941  1.000 53.75687  ? 38   MET B SD  1 
ATOM   302  C  CE  . MET A 1 39  ? 13.24895  -7.93580  71.30460  1.000 52.42371  ? 38   MET B CE  1 
ATOM   303  N  N   . GLY A 1 40  ? 13.77083  -2.09820  70.41852  1.000 52.63749  ? 39   GLY B N   1 
ATOM   304  C  CA  . GLY A 1 40  ? 14.86635  -1.15795  70.43801  1.000 53.22229  ? 39   GLY B CA  1 
ATOM   305  C  C   . GLY A 1 40  ? 16.11607  -1.75976  69.83074  1.000 54.62316  ? 39   GLY B C   1 
ATOM   306  O  O   . GLY A 1 40  ? 16.55374  -2.84606  70.22042  1.000 55.69024  ? 39   GLY B O   1 
ATOM   307  N  N   . PRO A 1 41  ? 16.66159  -1.10653  68.80650  1.000 52.58370  ? 40   PRO B N   1 
ATOM   308  C  CA  . PRO A 1 41  ? 17.85052  -1.64307  68.13322  1.000 54.25188  ? 40   PRO B CA  1 
ATOM   309  C  C   . PRO A 1 41  ? 18.97705  -1.88660  69.12587  1.000 57.34956  ? 40   PRO B C   1 
ATOM   310  O  O   . PRO A 1 41  ? 19.23185  -1.07154  70.01181  1.000 57.39025  ? 40   PRO B O   1 
ATOM   311  C  CB  . PRO A 1 41  ? 18.19917  -0.55157  67.12047  1.000 53.69766  ? 40   PRO B CB  1 
ATOM   312  C  CG  . PRO A 1 41  ? 16.88657  0.08735   66.80996  1.000 51.71788  ? 40   PRO B CG  1 
ATOM   313  C  CD  . PRO A 1 41  ? 16.10113  0.05589   68.10129  1.000 53.49216  ? 40   PRO B CD  1 
ATOM   314  N  N   . ASN A 1 42  ? 19.67271  -3.01585  68.94931  1.000 56.39268  ? 41   ASN B N   1 
ATOM   315  C  CA  . ASN A 1 42  ? 20.58572  -3.49760  69.98395  1.000 62.76261  ? 41   ASN B CA  1 
ATOM   316  C  C   . ASN A 1 42  ? 21.72880  -2.53213  70.27636  1.000 65.22515  ? 41   ASN B C   1 
ATOM   317  O  O   . ASN A 1 42  ? 22.16995  -2.43710  71.42681  1.000 67.34916  ? 41   ASN B O   1 
ATOM   318  C  CB  . ASN A 1 42  ? 21.17577  -4.85049  69.56730  1.000 65.81017  ? 41   ASN B CB  1 
ATOM   319  C  CG  . ASN A 1 42  ? 20.15605  -5.97710  69.58152  1.000 67.88870  ? 41   ASN B CG  1 
ATOM   320  O  OD1 . ASN A 1 42  ? 19.28637  -6.04609  70.45350  1.000 66.26179  ? 41   ASN B OD1 1 
ATOM   321  N  ND2 . ASN A 1 42  ? 20.25789  -6.86960  68.59423  1.000 75.60805  ? 41   ASN B ND2 1 
ATOM   322  N  N   . ASP A 1 43  ? 22.23912  -1.82309  69.27006  1.000 65.18754  ? 42   ASP B N   1 
ATOM   323  C  CA  . ASP A 1 43  ? 23.33506  -0.88279  69.49463  1.000 69.22113  ? 42   ASP B CA  1 
ATOM   324  C  C   . ASP A 1 43  ? 22.86268  0.54868   69.73795  1.000 67.15379  ? 42   ASP B C   1 
ATOM   325  O  O   . ASP A 1 43  ? 23.65186  1.49195   69.59706  1.000 74.06812  ? 42   ASP B O   1 
ATOM   326  C  CB  . ASP A 1 43  ? 24.35577  -0.92594  68.35998  1.000 74.18989  ? 42   ASP B CB  1 
ATOM   327  C  CG  . ASP A 1 43  ? 25.72965  -0.43323  68.81592  1.000 83.60705  ? 42   ASP B CG  1 
ATOM   328  O  OD1 . ASP A 1 43  ? 25.85482  -0.03202  70.00366  1.000 88.11897  ? 42   ASP B OD1 1 
ATOM   329  O  OD2 . ASP A 1 43  ? 26.68201  -0.47058  68.00719  1.000 81.97567  ? 42   ASP B OD2 1 
ATOM   330  N  N   . SER A 1 44  ? 21.59326  0.74164   70.03233  1.000 62.34103  ? 43   SER B N   1 
ATOM   331  C  CA  . SER A 1 44  ? 21.05132  2.06954   70.20551  1.000 59.12478  ? 43   SER B CA  1 
ATOM   332  C  C   . SER A 1 44  ? 20.73706  2.26845   71.66610  1.000 57.20309  ? 43   SER B C   1 
ATOM   333  O  O   . SER A 1 44  ? 20.76841  1.31863   72.45378  1.000 56.30449  ? 43   SER B O   1 
ATOM   334  C  CB  . SER A 1 44  ? 19.77966  2.24530   69.37149  1.000 56.06207  ? 43   SER B CB  1 
ATOM   335  O  OG  . SER A 1 44  ? 18.74522  1.42396   69.86457  1.000 54.06766  ? 43   SER B OG  1 
ATOM   336  N  N   . PRO A 1 45  ? 20.44565  3.50384   72.08175  1.000 56.75044  ? 44   PRO B N   1 
ATOM   337  C  CA  . PRO A 1 45  ? 19.99929  3.72296   73.46193  1.000 56.01105  ? 44   PRO B CA  1 
ATOM   338  C  C   . PRO A 1 45  ? 18.57830  3.27080   73.70826  1.000 54.56067  ? 44   PRO B C   1 
ATOM   339  O  O   . PRO A 1 45  ? 18.12116  3.31028   74.85506  1.000 54.01440  ? 44   PRO B O   1 
ATOM   340  C  CB  . PRO A 1 45  ? 20.11721  5.24492   73.62581  1.000 56.00214  ? 44   PRO B CB  1 
ATOM   341  C  CG  . PRO A 1 45  ? 19.97475  5.76902   72.21835  1.000 55.28629  ? 44   PRO B CG  1 
ATOM   342  C  CD  . PRO A 1 45  ? 20.68193  4.77082   71.36886  1.000 54.16753  ? 44   PRO B CD  1 
ATOM   343  N  N   . TYR A 1 46  ? 17.87444  2.81665   72.68244  1.000 52.17522  ? 45   TYR B N   1 
ATOM   344  C  CA  . TYR A 1 46  ? 16.53509  2.28561   72.86166  1.000 51.60973  ? 45   TYR B CA  1 
ATOM   345  C  C   . TYR A 1 46  ? 16.52733  0.78456   73.13087  1.000 51.73388  ? 45   TYR B C   1 
ATOM   346  O  O   . TYR A 1 46  ? 15.44604  0.20447   73.27147  1.000 50.96918  ? 45   TYR B O   1 
ATOM   347  C  CB  . TYR A 1 46  ? 15.68169  2.62266   71.63098  1.000 48.31058  ? 45   TYR B CB  1 
ATOM   348  C  CG  . TYR A 1 46  ? 15.81615  4.06207   71.19949  1.000 49.80358  ? 45   TYR B CG  1 
ATOM   349  C  CD1 . TYR A 1 46  ? 15.16797  5.07920   71.89519  1.000 47.28699  ? 45   TYR B CD1 1 
ATOM   350  C  CD2 . TYR A 1 46  ? 16.60031  4.41069   70.11176  1.000 49.53888  ? 45   TYR B CD2 1 
ATOM   351  C  CE1 . TYR A 1 46  ? 15.29651  6.39053   71.51107  1.000 46.16652  ? 45   TYR B CE1 1 
ATOM   352  C  CE2 . TYR A 1 46  ? 16.72603  5.71064   69.71885  1.000 46.76095  ? 45   TYR B CE2 1 
ATOM   353  C  CZ  . TYR A 1 46  ? 16.07687  6.70431   70.42128  1.000 46.76743  ? 45   TYR B CZ  1 
ATOM   354  O  OH  . TYR A 1 46  ? 16.20536  8.02259   70.02770  1.000 47.05060  ? 45   TYR B OH  1 
ATOM   355  N  N   . GLN A 1 47  ? 17.70082  0.14908   73.19784  1.000 53.93321  ? 46   GLN B N   1 
ATOM   356  C  CA  . GLN A 1 47  ? 17.77854  -1.29591  73.38657  1.000 55.39398  ? 46   GLN B CA  1 
ATOM   357  C  C   . GLN A 1 47  ? 17.07465  -1.72522  74.66155  1.000 55.75432  ? 46   GLN B C   1 
ATOM   358  O  O   . GLN A 1 47  ? 17.32301  -1.18608  75.74219  1.000 52.81588  ? 46   GLN B O   1 
ATOM   359  C  CB  . GLN A 1 47  ? 19.23310  -1.76565  73.41156  1.000 59.63337  ? 46   GLN B CB  1 
ATOM   360  C  CG  . GLN A 1 47  ? 19.42362  -3.16100  74.01089  1.000 68.11835  ? 46   GLN B CG  1 
ATOM   361  C  CD  . GLN A 1 47  ? 20.86012  -3.43577  74.41992  1.000 76.06673  ? 46   GLN B CD  1 
ATOM   362  O  OE1 . GLN A 1 47  ? 21.17534  -3.53892  75.60436  1.000 82.88349  ? 46   GLN B OE1 1 
ATOM   363  N  NE2 . GLN A 1 47  ? 21.73989  -3.56143  73.43254  1.000 75.56799  ? 46   GLN B NE2 1 
ATOM   364  N  N   . GLY A 1 48  ? 16.22142  -2.72982  74.53357  1.000 53.87043  ? 47   GLY B N   1 
ATOM   365  C  CA  . GLY A 1 48  ? 15.41707  -3.20247  75.62564  1.000 54.38160  ? 47   GLY B CA  1 
ATOM   366  C  C   . GLY A 1 48  ? 13.98243  -2.73312  75.57657  1.000 52.56812  ? 47   GLY B C   1 
ATOM   367  O  O   . GLY A 1 48  ? 13.13058  -3.32102  76.24495  1.000 54.70663  ? 47   GLY B O   1 
ATOM   368  N  N   . GLY A 1 49  ? 13.68895  -1.71842  74.77812  1.000 47.81073  ? 48   GLY B N   1 
ATOM   369  C  CA  . GLY A 1 49  ? 12.35165  -1.18733  74.71974  1.000 47.32599  ? 48   GLY B CA  1 
ATOM   370  C  C   . GLY A 1 49  ? 11.53465  -1.81646  73.61133  1.000 45.32678  ? 48   GLY B C   1 
ATOM   371  O  O   . GLY A 1 49  ? 12.06958  -2.34258  72.63502  1.000 49.93214  ? 48   GLY B O   1 
ATOM   372  N  N   . VAL A 1 50  ? 10.22052  -1.80108  73.80387  1.000 43.11912  ? 49   VAL B N   1 
ATOM   373  C  CA  . VAL A 1 50  ? 9.26200   -2.21823  72.78894  1.000 42.33239  ? 49   VAL B CA  1 
ATOM   374  C  C   . VAL A 1 50  ? 8.38599   -1.00960  72.46753  1.000 42.15337  ? 49   VAL B C   1 
ATOM   375  O  O   . VAL A 1 50  ? 7.84490   -0.36632  73.37833  1.000 42.56336  ? 49   VAL B O   1 
ATOM   376  C  CB  . VAL A 1 50  ? 8.41401   -3.41814  73.23184  1.000 39.45118  ? 49   VAL B CB  1 
ATOM   377  C  CG1 . VAL A 1 50  ? 7.54004   -3.89822  72.07696  1.000 41.17280  ? 49   VAL B CG1 1 
ATOM   378  C  CG2 . VAL A 1 50  ? 9.30404   -4.54871  73.70924  1.000 40.22340  ? 49   VAL B CG2 1 
ATOM   379  N  N   . PHE A 1 51  ? 8.33711   -0.64619  71.18836  1.000 40.82015  ? 50   PHE B N   1 
ATOM   380  C  CA  . PHE A 1 51  ? 7.61363   0.51579   70.69639  1.000 41.13625  ? 50   PHE B CA  1 
ATOM   381  C  C   . PHE A 1 51  ? 6.50773   0.05487   69.75902  1.000 40.96200  ? 50   PHE B C   1 
ATOM   382  O  O   . PHE A 1 51  ? 6.76547   -0.70598  68.82154  1.000 41.98654  ? 50   PHE B O   1 
ATOM   383  C  CB  . PHE A 1 51  ? 8.59457   1.45870   69.99484  1.000 36.59761  ? 50   PHE B CB  1 
ATOM   384  C  CG  . PHE A 1 51  ? 9.76335   1.82405   70.85625  1.000 38.08178  ? 50   PHE B CG  1 
ATOM   385  C  CD1 . PHE A 1 51  ? 10.89535  1.02500   70.88817  1.000 37.37805  ? 50   PHE B CD1 1 
ATOM   386  C  CD2 . PHE A 1 51  ? 9.72293   2.95491   71.66558  1.000 37.01090  ? 50   PHE B CD2 1 
ATOM   387  C  CE1 . PHE A 1 51  ? 11.96439  1.33493   71.71482  1.000 39.35511  ? 50   PHE B CE1 1 
ATOM   388  C  CE2 . PHE A 1 51  ? 10.79439  3.27657   72.48106  1.000 38.46708  ? 50   PHE B CE2 1 
ATOM   389  C  CZ  . PHE A 1 51  ? 11.91392  2.45934   72.51016  1.000 43.87114  ? 50   PHE B CZ  1 
ATOM   390  N  N   . PHE A 1 52  ? 5.29077   0.51428   70.00637  1.000 40.60421  ? 51   PHE B N   1 
ATOM   391  C  CA  . PHE A 1 52  ? 4.14435   0.20193   69.17088  1.000 41.98109  ? 51   PHE B CA  1 
ATOM   392  C  C   . PHE A 1 52  ? 3.91571   1.34899   68.19452  1.000 42.55487  ? 51   PHE B C   1 
ATOM   393  O  O   . PHE A 1 52  ? 4.24051   2.50171   68.47704  1.000 37.31596  ? 51   PHE B O   1 
ATOM   394  C  CB  . PHE A 1 52  ? 2.87682   -0.02561  70.00759  1.000 44.61310  ? 51   PHE B CB  1 
ATOM   395  C  CG  . PHE A 1 52  ? 2.92216   -1.25637  70.87137  1.000 42.70055  ? 51   PHE B CG  1 
ATOM   396  C  CD1 . PHE A 1 52  ? 3.56905   -1.23458  72.09331  1.000 44.81646  ? 51   PHE B CD1 1 
ATOM   397  C  CD2 . PHE A 1 52  ? 2.30284   -2.41848  70.46922  1.000 47.33316  ? 51   PHE B CD2 1 
ATOM   398  C  CE1 . PHE A 1 52  ? 3.61126   -2.34746  72.88635  1.000 48.23076  ? 51   PHE B CE1 1 
ATOM   399  C  CE2 . PHE A 1 52  ? 2.34645   -3.55758  71.25923  1.000 50.05876  ? 51   PHE B CE2 1 
ATOM   400  C  CZ  . PHE A 1 52  ? 3.00276   -3.52165  72.47136  1.000 47.45972  ? 51   PHE B CZ  1 
ATOM   401  N  N   . LEU A 1 53  ? 3.38286   1.01401   67.02434  1.000 42.61092  ? 52   LEU B N   1 
ATOM   402  C  CA  . LEU A 1 53  ? 3.08724   1.99407   65.99574  1.000 41.63606  ? 52   LEU B CA  1 
ATOM   403  C  C   . LEU A 1 53  ? 1.72780   1.65582   65.42114  1.000 39.59247  ? 52   LEU B C   1 
ATOM   404  O  O   . LEU A 1 53  ? 1.30849   0.49968   65.43468  1.000 41.69569  ? 52   LEU B O   1 
ATOM   405  C  CB  . LEU A 1 53  ? 4.14917   2.00288   64.86846  1.000 40.23976  ? 52   LEU B CB  1 
ATOM   406  C  CG  . LEU A 1 53  ? 5.62269   2.26973   65.18656  1.000 37.46379  ? 52   LEU B CG  1 
ATOM   407  C  CD1 . LEU A 1 53  ? 6.29442   0.96535   65.59468  1.000 40.52902  ? 52   LEU B CD1 1 
ATOM   408  C  CD2 . LEU A 1 53  ? 6.34078   2.87006   63.99427  1.000 41.14014  ? 52   LEU B CD2 1 
ATOM   409  N  N   . THR A 1 54  ? 1.05010   2.66510   64.90661  1.000 41.53382  ? 53   THR B N   1 
ATOM   410  C  CA  . THR A 1 54  ? -0.14436  2.43546   64.11565  1.000 42.88999  ? 53   THR B CA  1 
ATOM   411  C  C   . THR A 1 54  ? 0.18414   2.72658   62.66356  1.000 44.16889  ? 53   THR B C   1 
ATOM   412  O  O   . THR A 1 54  ? 0.92932   3.67165   62.35881  1.000 43.55595  ? 53   THR B O   1 
ATOM   413  C  CB  . THR A 1 54  ? -1.31353  3.30619   64.54841  1.000 42.08346  ? 53   THR B CB  1 
ATOM   414  O  OG1 . THR A 1 54  ? -0.99854  4.67558   64.27374  1.000 45.15781  ? 53   THR B OG1 1 
ATOM   415  C  CG2 . THR A 1 54  ? -1.57381  3.12517   66.03221  1.000 46.79207  ? 53   THR B CG2 1 
ATOM   416  N  N   . ILE A 1 55  ? -0.37254  1.90200   61.78170  1.000 43.35548  ? 54   ILE B N   1 
ATOM   417  C  CA  . ILE A 1 55  ? -0.21997  2.03242   60.34477  1.000 44.40317  ? 54   ILE B CA  1 
ATOM   418  C  C   . ILE A 1 55  ? -1.60865  2.17816   59.74646  1.000 44.23703  ? 54   ILE B C   1 
ATOM   419  O  O   . ILE A 1 55  ? -2.54072  1.48551   60.17066  1.000 46.21310  ? 54   ILE B O   1 
ATOM   420  C  CB  . ILE A 1 55  ? 0.49844   0.80513   59.76057  1.000 43.24368  ? 54   ILE B CB  1 
ATOM   421  C  CG1 . ILE A 1 55  ? 1.88404   0.64682   60.39279  1.000 39.65977  ? 54   ILE B CG1 1 
ATOM   422  C  CG2 . ILE A 1 55  ? 0.54672   0.89124   58.23119  1.000 43.20111  ? 54   ILE B CG2 1 
ATOM   423  C  CD1 . ILE A 1 55  ? 2.57567   -0.64353  60.00691  1.000 43.05205  ? 54   ILE B CD1 1 
ATOM   424  N  N   . HIS A 1 56  ? -1.76044  3.11250   58.81025  1.000 46.26054  ? 55   HIS B N   1 
ATOM   425  C  CA  . HIS A 1 56  ? -3.02012  3.29514   58.09541  1.000 50.06094  ? 55   HIS B CA  1 
ATOM   426  C  C   . HIS A 1 56  ? -2.71887  3.32532   56.59954  1.000 47.85228  ? 55   HIS B C   1 
ATOM   427  O  O   . HIS A 1 56  ? -1.99574  4.21167   56.12679  1.000 42.90680  ? 55   HIS B O   1 
ATOM   428  C  CB  . HIS A 1 56  ? -3.75352  4.56725   58.54618  1.000 51.39229  ? 55   HIS B CB  1 
ATOM   429  C  CG  . HIS A 1 56  ? -5.21326  4.56050   58.21694  1.000 56.91474  ? 55   HIS B CG  1 
ATOM   430  N  ND1 . HIS A 1 56  ? -5.68919  4.40266   56.93301  1.000 67.60062  ? 55   HIS B ND1 1 
ATOM   431  C  CD2 . HIS A 1 56  ? -6.30421  4.64603   59.01280  1.000 63.61509  ? 55   HIS B CD2 1 
ATOM   432  C  CE1 . HIS A 1 56  ? -7.01008  4.41302   56.94813  1.000 62.72607  ? 55   HIS B CE1 1 
ATOM   433  N  NE2 . HIS A 1 56  ? -7.40825  4.56022   58.19827  1.000 68.12066  ? 55   HIS B NE2 1 
ATOM   434  N  N   . PHE A 1 57  ? -3.28637  2.35409   55.84603  1.000 49.67546  ? 56   PHE B N   1 
ATOM   435  C  CA  . PHE A 1 57  ? -3.04464  2.25343   54.40692  1.000 49.50320  ? 56   PHE B CA  1 
ATOM   436  C  C   . PHE A 1 57  ? -4.08201  3.06320   53.64076  1.000 50.59374  ? 56   PHE B C   1 
ATOM   437  O  O   . PHE A 1 57  ? -5.28818  2.85292   53.83619  1.000 51.63872  ? 56   PHE B O   1 
ATOM   438  C  CB  . PHE A 1 57  ? -3.09868  0.80209   53.93453  1.000 47.00751  ? 56   PHE B CB  1 
ATOM   439  C  CG  . PHE A 1 57  ? -1.99614  -0.07146  54.46697  1.000 46.03492  ? 56   PHE B CG  1 
ATOM   440  C  CD1 . PHE A 1 57  ? -0.72132  -0.01669  53.93205  1.000 41.49303  ? 56   PHE B CD1 1 
ATOM   441  C  CD2 . PHE A 1 57  ? -2.24654  -0.98285  55.48076  1.000 46.44274  ? 56   PHE B CD2 1 
ATOM   442  C  CE1 . PHE A 1 57  ? 0.29147   -0.83739  54.40412  1.000 38.89553  ? 56   PHE B CE1 1 
ATOM   443  C  CE2 . PHE A 1 57  ? -1.23441  -1.79625  55.96412  1.000 44.02186  ? 56   PHE B CE2 1 
ATOM   444  C  CZ  . PHE A 1 57  ? 0.03440   -1.72516  55.41529  1.000 41.66032  ? 56   PHE B CZ  1 
ATOM   445  N  N   . PRO A 1 58  ? -3.65032  3.98238   52.77326  1.000 51.04471  ? 57   PRO B N   1 
ATOM   446  C  CA  . PRO A 1 58  ? -4.59704  4.70416   51.91233  1.000 52.55791  ? 57   PRO B CA  1 
ATOM   447  C  C   . PRO A 1 58  ? -5.24981  3.78677   50.89596  1.000 53.88165  ? 57   PRO B C   1 
ATOM   448  O  O   . PRO A 1 58  ? -4.71159  2.74506   50.51281  1.000 54.55537  ? 57   PRO B O   1 
ATOM   449  C  CB  . PRO A 1 58  ? -3.72025  5.74900   51.20703  1.000 50.49630  ? 57   PRO B CB  1 
ATOM   450  C  CG  . PRO A 1 58  ? -2.33598  5.18331   51.25496  1.000 51.06510  ? 57   PRO B CG  1 
ATOM   451  C  CD  . PRO A 1 58  ? -2.26634  4.44949   52.58359  1.000 51.08106  ? 57   PRO B CD  1 
ATOM   452  N  N   . THR A 1 59  ? -6.39565  4.23798   50.39258  1.000 55.26780  ? 58   THR B N   1 
ATOM   453  C  CA  . THR A 1 59  ? -7.17499  3.40060   49.49222  1.000 58.79680  ? 58   THR B CA  1 
ATOM   454  C  C   . THR A 1 59  ? -6.42638  3.09377   48.20563  1.000 60.67553  ? 58   THR B C   1 
ATOM   455  O  O   . THR A 1 59  ? -6.72535  2.09119   47.54798  1.000 59.54705  ? 58   THR B O   1 
ATOM   456  C  CB  . THR A 1 59  ? -8.49790  4.07562   49.16298  1.000 61.38054  ? 58   THR B CB  1 
ATOM   457  O  OG1 . THR A 1 59  ? -8.24859  5.18684   48.29194  1.000 63.28416  ? 58   THR B OG1 1 
ATOM   458  C  CG2 . THR A 1 59  ? -9.16513  4.55938   50.43785  1.000 62.23292  ? 58   THR B CG2 1 
ATOM   459  N  N   . ASP A 1 60  ? -5.48284  3.94876   47.80728  1.000 59.94322  ? 59   ASP B N   1 
ATOM   460  C  CA  . ASP A 1 60  ? -4.69976  3.70958   46.60288  1.000 60.19314  ? 59   ASP B CA  1 
ATOM   461  C  C   . ASP A 1 60  ? -3.23145  3.43708   46.92171  1.000 57.86802  ? 59   ASP B C   1 
ATOM   462  O  O   . ASP A 1 60  ? -2.33053  3.86822   46.19856  1.000 59.38123  ? 59   ASP B O   1 
ATOM   463  C  CB  . ASP A 1 60  ? -4.85921  4.87252   45.63069  1.000 63.01977  ? 59   ASP B CB  1 
ATOM   464  C  CG  . ASP A 1 60  ? -4.40530  6.19357   46.21741  1.000 69.06318  ? 59   ASP B CG  1 
ATOM   465  O  OD1 . ASP A 1 60  ? -4.58318  6.41209   47.42994  1.000 70.59228  ? 59   ASP B OD1 1 
ATOM   466  O  OD2 . ASP A 1 60  ? -3.88918  7.05220   45.46644  1.000 73.60359  ? 59   ASP B OD2 1 
ATOM   467  N  N   . TYR A 1 61  ? -2.99343  2.75730   48.03277  1.000 54.64330  ? 60   TYR B N   1 
ATOM   468  C  CA  . TYR A 1 61  ? -1.70224  2.17409   48.32039  1.000 52.15956  ? 60   TYR B CA  1 
ATOM   469  C  C   . TYR A 1 61  ? -1.41250  1.14658   47.22725  1.000 52.22673  ? 60   TYR B C   1 
ATOM   470  O  O   . TYR A 1 61  ? -2.34727  0.56031   46.67826  1.000 53.03163  ? 60   TYR B O   1 
ATOM   471  C  CB  . TYR A 1 61  ? -1.77412  1.54865   49.71426  1.000 49.41953  ? 60   TYR B CB  1 
ATOM   472  C  CG  . TYR A 1 61  ? -0.55640  0.85678   50.23654  1.000 47.22155  ? 60   TYR B CG  1 
ATOM   473  C  CD1 . TYR A 1 61  ? 0.50697   1.58395   50.72275  1.000 46.42445  ? 60   TYR B CD1 1 
ATOM   474  C  CD2 . TYR A 1 61  ? -0.50565  -0.53473  50.33065  1.000 47.63070  ? 60   TYR B CD2 1 
ATOM   475  C  CE1 . TYR A 1 61  ? 1.62071   0.96397   51.23127  1.000 44.96087  ? 60   TYR B CE1 1 
ATOM   476  C  CE2 . TYR A 1 61  ? 0.61259   -1.17441  50.84425  1.000 46.08421  ? 60   TYR B CE2 1 
ATOM   477  C  CZ  . TYR A 1 61  ? 1.67504   -0.41613  51.29386  1.000 45.91401  ? 60   TYR B CZ  1 
ATOM   478  O  OH  . TYR A 1 61  ? 2.80162   -1.01944  51.80439  1.000 42.65973  ? 60   TYR B OH  1 
ATOM   479  N  N   . PRO A 1 62  ? -0.13944  0.96085   46.81970  1.000 50.70104  ? 61   PRO B N   1 
ATOM   480  C  CA  . PRO A 1 62  ? 1.11170   1.55819   47.30340  1.000 49.77124  ? 61   PRO B CA  1 
ATOM   481  C  C   . PRO A 1 62  ? 1.56579   2.74512   46.49883  1.000 53.21868  ? 61   PRO B C   1 
ATOM   482  O  O   . PRO A 1 62  ? 2.70265   3.20196   46.60870  1.000 51.92337  ? 61   PRO B O   1 
ATOM   483  C  CB  . PRO A 1 62  ? 2.10004   0.41339   47.14746  1.000 49.61875  ? 61   PRO B CB  1 
ATOM   484  C  CG  . PRO A 1 62  ? 1.65162   -0.23575  45.85529  1.000 52.50352  ? 61   PRO B CG  1 
ATOM   485  C  CD  . PRO A 1 62  ? 0.13764   -0.09107  45.82092  1.000 52.44664  ? 61   PRO B CD  1 
ATOM   486  N  N   . PHE A 1 63  ? 0.69074   3.26412   45.65151  1.000 54.66835  ? 62   PHE B N   1 
ATOM   487  C  CA  . PHE A 1 63  ? 1.05017   4.45804   44.91735  1.000 57.16722  ? 62   PHE B CA  1 
ATOM   488  C  C   . PHE A 1 63  ? 1.09631   5.65407   45.85545  1.000 58.67526  ? 62   PHE B C   1 
ATOM   489  O  O   . PHE A 1 63  ? 1.75225   6.65246   45.54604  1.000 64.81727  ? 62   PHE B O   1 
ATOM   490  C  CB  . PHE A 1 63  ? 0.08574   4.63905   43.76010  1.000 58.90556  ? 62   PHE B CB  1 
ATOM   491  C  CG  . PHE A 1 63  ? 0.02789   3.42754   42.86916  1.000 61.38897  ? 62   PHE B CG  1 
ATOM   492  C  CD1 . PHE A 1 63  ? 1.04343   3.16788   41.95231  1.000 63.60073  ? 62   PHE B CD1 1 
ATOM   493  C  CD2 . PHE A 1 63  ? -1.00276  2.51456   42.99374  1.000 64.99518  ? 62   PHE B CD2 1 
ATOM   494  C  CE1 . PHE A 1 63  ? 1.00120   2.03960   41.15967  1.000 65.11263  ? 62   PHE B CE1 1 
ATOM   495  C  CE2 . PHE A 1 63  ? -1.04983  1.38303   42.20172  1.000 68.59859  ? 62   PHE B CE2 1 
ATOM   496  C  CZ  . PHE A 1 63  ? -0.04591  1.14772   41.28330  1.000 67.95326  ? 62   PHE B CZ  1 
ATOM   497  N  N   . LYS A 1 64  ? 0.44939   5.55775   47.00822  1.000 57.21467  ? 63   LYS B N   1 
ATOM   498  C  CA  . LYS A 1 64  ? 0.59651   6.56910   48.03311  1.000 57.07879  ? 63   LYS B CA  1 
ATOM   499  C  C   . LYS A 1 64  ? 1.13801   5.96866   49.32276  1.000 52.37269  ? 63   LYS B C   1 
ATOM   500  O  O   . LYS A 1 64  ? 0.82628   4.81979   49.62579  1.000 50.60148  ? 63   LYS B O   1 
ATOM   501  C  CB  . LYS A 1 64  ? -0.75802  7.26074   48.24898  1.000 62.81758  ? 63   LYS B CB  1 
ATOM   502  C  CG  . LYS A 1 64  ? -1.06572  8.27645   47.14570  1.000 70.38863  ? 63   LYS B CG  1 
ATOM   503  C  CD  . LYS A 1 64  ? -2.38211  9.02473   47.30056  1.000 83.31775  ? 63   LYS B CD  1 
ATOM   504  C  CE  . LYS A 1 64  ? -2.39384  10.11145  48.33457  1.000 84.23376  ? 63   LYS B CE  1 
ATOM   505  N  NZ  . LYS A 1 64  ? -3.68347  10.88301  48.27095  1.000 78.24180  ? 63   LYS B NZ  1 
ATOM   506  N  N   . PRO A 1 65  ? 2.00477   6.66782   50.05487  1.000 50.35735  ? 64   PRO B N   1 
ATOM   507  C  CA  . PRO A 1 65  ? 2.64722   6.04366   51.26014  1.000 47.60617  ? 64   PRO B CA  1 
ATOM   508  C  C   . PRO A 1 65  ? 1.65688   5.80793   52.38598  1.000 47.23863  ? 64   PRO B C   1 
ATOM   509  O  O   . PRO A 1 65  ? 0.62327   6.49151   52.47746  1.000 44.81471  ? 64   PRO B O   1 
ATOM   510  C  CB  . PRO A 1 65  ? 3.70782   7.06264   51.66228  1.000 48.72868  ? 64   PRO B CB  1 
ATOM   511  C  CG  . PRO A 1 65  ? 3.20175   8.36120   51.12388  1.000 51.26100  ? 64   PRO B CG  1 
ATOM   512  C  CD  . PRO A 1 65  ? 2.48403   8.03887   49.84442  1.000 51.00431  ? 64   PRO B CD  1 
ATOM   513  N  N   . PRO A 1 66  ? 1.95848   4.86393   53.27470  1.000 47.03364  ? 65   PRO B N   1 
ATOM   514  C  CA  . PRO A 1 66  ? 1.11828   4.63983   54.44976  1.000 45.14453  ? 65   PRO B CA  1 
ATOM   515  C  C   . PRO A 1 66  ? 1.38412   5.68176   55.52574  1.000 46.47087  ? 65   PRO B C   1 
ATOM   516  O  O   . PRO A 1 66  ? 2.46345   6.27589   55.61622  1.000 45.63894  ? 65   PRO B O   1 
ATOM   517  C  CB  . PRO A 1 66  ? 1.57804   3.26304   54.94252  1.000 44.40364  ? 65   PRO B CB  1 
ATOM   518  C  CG  . PRO A 1 66  ? 3.03073   3.27421   54.61939  1.000 44.97507  ? 65   PRO B CG  1 
ATOM   519  C  CD  . PRO A 1 66  ? 3.13771   3.97804   53.27697  1.000 44.47650  ? 65   PRO B CD  1 
ATOM   520  N  N   . LYS A 1 67  ? 0.38588   5.87328   56.37901  1.000 47.89731  ? 66   LYS B N   1 
ATOM   521  C  CA  . LYS A 1 67  ? 0.50921   6.78942   57.50362  1.000 46.84822  ? 66   LYS B CA  1 
ATOM   522  C  C   . LYS A 1 67  ? 1.02893   5.97580   58.68410  1.000 44.39815  ? 66   LYS B C   1 
ATOM   523  O  O   . LYS A 1 67  ? 0.38078   5.02424   59.11691  1.000 42.58276  ? 66   LYS B O   1 
ATOM   524  C  CB  . LYS A 1 67  ? -0.83691  7.43814   57.81115  1.000 48.28133  ? 66   LYS B CB  1 
ATOM   525  C  CG  . LYS A 1 67  ? -0.79171  8.45129   58.93253  1.000 54.23851  ? 66   LYS B CG  1 
ATOM   526  C  CD  . LYS A 1 67  ? -2.17830  9.04295   59.23755  1.000 65.16436  ? 66   LYS B CD  1 
ATOM   527  C  CE  . LYS A 1 67  ? -2.94573  9.46596   57.98776  1.000 65.07321  ? 66   LYS B CE  1 
ATOM   528  N  NZ  . LYS A 1 67  ? -4.35843  9.85474   58.31232  1.000 68.03439  ? 66   LYS B NZ  1 
ATOM   529  N  N   . VAL A 1 68  ? 2.23091   6.29223   59.14861  1.000 42.47099  ? 67   VAL B N   1 
ATOM   530  C  CA  . VAL A 1 68  ? 2.87129   5.56325   60.23235  1.000 38.53223  ? 67   VAL B CA  1 
ATOM   531  C  C   . VAL A 1 68  ? 3.11531   6.51926   61.40107  1.000 42.27500  ? 67   VAL B C   1 
ATOM   532  O  O   . VAL A 1 68  ? 3.66556   7.61059   61.21736  1.000 43.42631  ? 67   VAL B O   1 
ATOM   533  C  CB  . VAL A 1 68  ? 4.18548   4.91886   59.75765  1.000 42.37056  ? 67   VAL B CB  1 
ATOM   534  C  CG1 . VAL A 1 68  ? 4.81162   4.09917   60.86094  1.000 42.57977  ? 67   VAL B CG1 1 
ATOM   535  C  CG2 . VAL A 1 68  ? 3.93130   4.05958   58.52642  1.000 41.71098  ? 67   VAL B CG2 1 
ATOM   536  N  N   . ALA A 1 69  ? 2.74672   6.09821   62.60688  1.000 42.12222  ? 68   ALA B N   1 
ATOM   537  C  CA  . ALA A 1 69  ? 3.00401   6.93857   63.77175  1.000 40.07516  ? 68   ALA B CA  1 
ATOM   538  C  C   . ALA A 1 69  ? 3.33330   6.05362   64.96520  1.000 41.07104  ? 68   ALA B C   1 
ATOM   539  O  O   . ALA A 1 69  ? 2.91849   4.89448   65.01403  1.000 40.92422  ? 68   ALA B O   1 
ATOM   540  C  CB  . ALA A 1 69  ? 1.80938   7.84788   64.09801  1.000 41.64794  ? 68   ALA B CB  1 
ATOM   541  N  N   . PHE A 1 70  ? 4.15912   6.57242   65.87601  1.000 39.74134  ? 69   PHE B N   1 
ATOM   542  C  CA  . PHE A 1 70  ? 4.38961   5.90552   67.15142  1.000 38.84276  ? 69   PHE B CA  1 
ATOM   543  C  C   . PHE A 1 70  ? 3.20027   6.10938   68.08393  1.000 42.90284  ? 69   PHE B C   1 
ATOM   544  O  O   . PHE A 1 70  ? 2.53471   7.14705   68.04783  1.000 43.92757  ? 69   PHE B O   1 
ATOM   545  C  CB  . PHE A 1 70  ? 5.64164   6.44019   67.83559  1.000 38.95948  ? 69   PHE B CB  1 
ATOM   546  C  CG  . PHE A 1 70  ? 6.90448   5.84116   67.34407  1.000 41.33754  ? 69   PHE B CG  1 
ATOM   547  C  CD1 . PHE A 1 70  ? 7.49975   6.29443   66.17833  1.000 40.23929  ? 69   PHE B CD1 1 
ATOM   548  C  CD2 . PHE A 1 70  ? 7.51698   4.81093   68.05217  1.000 41.49139  ? 69   PHE B CD2 1 
ATOM   549  C  CE1 . PHE A 1 70  ? 8.67839   5.72758   65.72651  1.000 39.56671  ? 69   PHE B CE1 1 
ATOM   550  C  CE2 . PHE A 1 70  ? 8.69689   4.23772   67.60254  1.000 41.05916  ? 69   PHE B CE2 1 
ATOM   551  C  CZ  . PHE A 1 70  ? 9.27424   4.69774   66.43822  1.000 43.28656  ? 69   PHE B CZ  1 
ATOM   552  N  N   . THR A 1 71  ? 2.89520   5.09463   68.88465  1.000 43.38598  ? 70   THR B N   1 
ATOM   553  C  CA  . THR A 1 71  ? 1.99544   5.26756   70.01177  1.000 42.85324  ? 70   THR B CA  1 
ATOM   554  C  C   . THR A 1 71  ? 2.70858   5.11557   71.34423  1.000 43.37056  ? 70   THR B C   1 
ATOM   555  O  O   . THR A 1 71  ? 2.12258   5.41927   72.38445  1.000 52.17052  ? 70   THR B O   1 
ATOM   556  C  CB  . THR A 1 71  ? 0.81179   4.29652   69.90967  1.000 43.39881  ? 70   THR B CB  1 
ATOM   557  O  OG1 . THR A 1 71  ? 1.29654   2.97367   69.70367  1.000 48.16562  ? 70   THR B OG1 1 
ATOM   558  C  CG2 . THR A 1 71  ? -0.08458  4.69267   68.73545  1.000 44.15671  ? 70   THR B CG2 1 
ATOM   559  N  N   . THR A 1 72  ? 3.95054   4.65836   71.33066  1.000 43.60504  ? 71   THR B N   1 
ATOM   560  C  CA  . THR A 1 72  ? 4.79569   4.58607   72.51130  1.000 43.76894  ? 71   THR B CA  1 
ATOM   561  C  C   . THR A 1 72  ? 5.70291   5.80995   72.51421  1.000 42.11923  ? 71   THR B C   1 
ATOM   562  O  O   . THR A 1 72  ? 6.32302   6.11880   71.49015  1.000 38.78681  ? 71   THR B O   1 
ATOM   563  C  CB  . THR A 1 72  ? 5.60908   3.28698   72.49436  1.000 41.08072  ? 71   THR B CB  1 
ATOM   564  O  OG1 . THR A 1 72  ? 4.70594   2.17849   72.50942  1.000 45.91932  ? 71   THR B OG1 1 
ATOM   565  C  CG2 . THR A 1 72  ? 6.52983   3.18699   73.69538  1.000 42.38609  ? 71   THR B CG2 1 
ATOM   566  N  N   . ARG A 1 73  ? 5.72923   6.53261   73.64086  1.000 41.93657  ? 72   ARG B N   1 
ATOM   567  C  CA  . ARG A 1 73  ? 6.58485   7.70670   73.76561  1.000 44.85910  ? 72   ARG B CA  1 
ATOM   568  C  C   . ARG A 1 73  ? 8.03889   7.29924   73.57815  1.000 43.61710  ? 72   ARG B C   1 
ATOM   569  O  O   . ARG A 1 73  ? 8.46135   6.22952   74.02386  1.000 43.10498  ? 72   ARG B O   1 
ATOM   570  C  CB  . ARG A 1 73  ? 6.40210   8.40386   75.12987  1.000 48.93346  ? 72   ARG B CB  1 
ATOM   571  C  CG  . ARG A 1 73  ? 5.01724   9.04270   75.37597  1.000 49.84722  ? 72   ARG B CG  1 
ATOM   572  C  CD  . ARG A 1 73  ? 4.73870   10.41554  74.70693  1.000 59.84644  ? 72   ARG B CD  1 
ATOM   573  N  NE  . ARG A 1 73  ? 5.42122   11.53704  75.34568  1.000 56.90272  ? 72   ARG B NE  1 
ATOM   574  C  CZ  . ARG A 1 73  ? 6.36863   12.25820  74.76365  1.000 52.33802  ? 72   ARG B CZ  1 
ATOM   575  N  NH1 . ARG A 1 73  ? 6.75883   12.01207  73.52227  1.000 54.69228  ? 72   ARG B NH1 1 
ATOM   576  N  NH2 . ARG A 1 73  ? 6.98979   13.19898  75.46614  1.000 55.32949  ? 72   ARG B NH2 1 
ATOM   577  N  N   . ILE A 1 74  ? 8.79611   8.15099   72.89174  1.000 40.90624  ? 73   ILE B N   1 
ATOM   578  C  CA  . ILE A 1 74  ? 10.18967  7.88051   72.55583  1.000 41.31899  ? 73   ILE B CA  1 
ATOM   579  C  C   . ILE A 1 74  ? 10.94229  9.20255   72.45671  1.000 44.14882  ? 73   ILE B C   1 
ATOM   580  O  O   . ILE A 1 74  ? 10.40695  10.19968  71.96613  1.000 42.52561  ? 73   ILE B O   1 
ATOM   581  C  CB  . ILE A 1 74  ? 10.28461  7.07036   71.25028  1.000 40.00812  ? 73   ILE B CB  1 
ATOM   582  C  CG1 . ILE A 1 74  ? 11.74097  6.78699   70.90695  1.000 40.99840  ? 73   ILE B CG1 1 
ATOM   583  C  CG2 . ILE A 1 74  ? 9.57651   7.79692   70.12031  1.000 42.05355  ? 73   ILE B CG2 1 
ATOM   584  C  CD1 . ILE A 1 74  ? 11.90049  5.73466   69.83531  1.000 43.86923  ? 73   ILE B CD1 1 
ATOM   585  N  N   . TYR A 1 75  ? 12.18899  9.20981   72.92981  1.000 45.30769  ? 74   TYR B N   1 
ATOM   586  C  CA  . TYR A 1 75  ? 13.02014  10.41176  72.95029  1.000 43.37480  ? 74   TYR B CA  1 
ATOM   587  C  C   . TYR A 1 75  ? 13.87460  10.48252  71.69907  1.000 45.09640  ? 74   TYR B C   1 
ATOM   588  O  O   . TYR A 1 75  ? 14.95134  9.88888   71.63947  1.000 44.62376  ? 74   TYR B O   1 
ATOM   589  C  CB  . TYR A 1 75  ? 13.89576  10.42296  74.19352  1.000 45.27077  ? 74   TYR B CB  1 
ATOM   590  C  CG  . TYR A 1 75  ? 14.70609  11.69857  74.37107  1.000 48.42957  ? 74   TYR B CG  1 
ATOM   591  C  CD1 . TYR A 1 75  ? 14.15420  12.82695  74.99416  1.000 46.90324  ? 74   TYR B CD1 1 
ATOM   592  C  CD2 . TYR A 1 75  ? 16.02483  11.77115  73.93784  1.000 46.18199  ? 74   TYR B CD2 1 
ATOM   593  C  CE1 . TYR A 1 75  ? 14.89628  13.98011  75.17398  1.000 44.27632  ? 74   TYR B CE1 1 
ATOM   594  C  CE2 . TYR A 1 75  ? 16.77190  12.92271  74.11304  1.000 45.59956  ? 74   TYR B CE2 1 
ATOM   595  C  CZ  . TYR A 1 75  ? 16.20051  14.02378  74.72667  1.000 44.95397  ? 74   TYR B CZ  1 
ATOM   596  O  OH  . TYR A 1 75  ? 16.94723  15.15488  74.90457  1.000 42.94552  ? 74   TYR B OH  1 
ATOM   597  N  N   . HIS A 1 76  ? 13.43861  11.28214  70.72370  1.000 46.59649  ? 75   HIS B N   1 
ATOM   598  C  CA  . HIS A 1 76  ? 14.08845  11.27108  69.42609  1.000 45.31814  ? 75   HIS B CA  1 
ATOM   599  C  C   . HIS A 1 76  ? 13.93062  12.59472  68.69102  1.000 44.01322  ? 75   HIS B C   1 
ATOM   600  O  O   . HIS A 1 76  ? 12.84487  13.18378  68.73314  1.000 41.64551  ? 75   HIS B O   1 
ATOM   601  C  CB  . HIS A 1 76  ? 13.50749  10.14414  68.57012  1.000 44.32319  ? 75   HIS B CB  1 
ATOM   602  C  CG  . HIS A 1 76  ? 14.34258  9.81028   67.38040  1.000 47.20854  ? 75   HIS B CG  1 
ATOM   603  N  ND1 . HIS A 1 76  ? 14.25329  10.50095  66.19169  1.000 46.82805  ? 75   HIS B ND1 1 
ATOM   604  C  CD2 . HIS A 1 76  ? 15.26585  8.83817   67.18502  1.000 45.55329  ? 75   HIS B CD2 1 
ATOM   605  C  CE1 . HIS A 1 76  ? 15.10973  9.98895   65.32639  1.000 49.75906  ? 75   HIS B CE1 1 
ATOM   606  N  NE2 . HIS A 1 76  ? 15.73548  8.98016   65.90514  1.000 44.09536  ? 75   HIS B NE2 1 
ATOM   607  N  N   . PRO A 1 77  ? 14.96012  13.04042  67.96057  1.000 45.38748  ? 76   PRO B N   1 
ATOM   608  C  CA  . PRO A 1 77  ? 14.86138  14.31222  67.22462  1.000 42.73269  ? 76   PRO B CA  1 
ATOM   609  C  C   . PRO A 1 77  ? 13.79634  14.35117  66.14287  1.000 43.75787  ? 76   PRO B C   1 
ATOM   610  O  O   . PRO A 1 77  ? 13.31478  15.44309  65.82895  1.000 44.39837  ? 76   PRO B O   1 
ATOM   611  C  CB  . PRO A 1 77  ? 16.25230  14.45226  66.59361  1.000 42.87918  ? 76   PRO B CB  1 
ATOM   612  C  CG  . PRO A 1 77  ? 17.12988  13.66817  67.45790  1.000 45.87950  ? 76   PRO B CG  1 
ATOM   613  C  CD  . PRO A 1 77  ? 16.32151  12.48536  67.89341  1.000 44.53440  ? 76   PRO B CD  1 
ATOM   614  N  N   . ASN A 1 78  ? 13.40291  13.21617  65.56671  1.000 44.88388  ? 77   ASN B N   1 
ATOM   615  C  CA  . ASN A 1 78  ? 12.47833  13.20132  64.43920  1.000 45.96755  ? 77   ASN B CA  1 
ATOM   616  C  C   . ASN A 1 78  ? 11.10893  12.62124  64.76877  1.000 46.05350  ? 77   ASN B C   1 
ATOM   617  O  O   . ASN A 1 78  ? 10.37139  12.25885  63.84622  1.000 45.79528  ? 77   ASN B O   1 
ATOM   618  C  CB  . ASN A 1 78  ? 13.08631  12.43892  63.26652  1.000 47.48634  ? 77   ASN B CB  1 
ATOM   619  C  CG  . ASN A 1 78  ? 14.43084  12.98280  62.86909  1.000 48.37075  ? 77   ASN B CG  1 
ATOM   620  O  OD1 . ASN A 1 78  ? 15.47075  12.44383  63.23896  1.000 50.03264  ? 77   ASN B OD1 1 
ATOM   621  N  ND2 . ASN A 1 78  ? 14.42100  14.07636  62.15049  1.000 41.89628  ? 77   ASN B ND2 1 
ATOM   622  N  N   . ILE A 1 79  ? 10.77187  12.47661  66.05047  1.000 44.81156  ? 78   ILE B N   1 
ATOM   623  C  CA  . ILE A 1 79  ? 9.48045   11.95875  66.49630  1.000 43.31514  ? 78   ILE B CA  1 
ATOM   624  C  C   . ILE A 1 79  ? 8.96497   12.88120  67.59218  1.000 43.62212  ? 78   ILE B C   1 
ATOM   625  O  O   . ILE A 1 79  ? 9.65006   13.08788  68.60224  1.000 45.40336  ? 78   ILE B O   1 
ATOM   626  C  CB  . ILE A 1 79  ? 9.58314   10.51878  67.01918  1.000 44.11181  ? 78   ILE B CB  1 
ATOM   627  C  CG1 . ILE A 1 79  ? 10.14819  9.61022   65.93673  1.000 45.02439  ? 78   ILE B CG1 1 
ATOM   628  C  CG2 . ILE A 1 79  ? 8.22182   10.00637  67.45945  1.000 38.68553  ? 78   ILE B CG2 1 
ATOM   629  C  CD1 . ILE A 1 79  ? 10.88978  8.46034   66.50169  1.000 41.00761  ? 78   ILE B CD1 1 
ATOM   630  N  N   . ASN A 1 80  ? 7.77240   13.44828  67.39421  1.000 42.52254  ? 79   ASN B N   1 
ATOM   631  C  CA  . ASN A 1 80  ? 7.23782   14.41509  68.34696  1.000 39.49828  ? 79   ASN B CA  1 
ATOM   632  C  C   . ASN A 1 80  ? 6.40958   13.72375  69.43681  1.000 40.76406  ? 79   ASN B C   1 
ATOM   633  O  O   . ASN A 1 80  ? 6.32989   12.48761  69.52877  1.000 44.95460  ? 79   ASN B O   1 
ATOM   634  C  CB  . ASN A 1 80  ? 6.42514   15.50514  67.64015  1.000 38.83226  ? 79   ASN B CB  1 
ATOM   635  C  CG  . ASN A 1 80  ? 5.12858   15.00093  67.01980  1.000 38.59918  ? 79   ASN B CG  1 
ATOM   636  O  OD1 . ASN A 1 80  ? 4.62431   13.94078  67.34187  1.000 40.28867  ? 79   ASN B OD1 1 
ATOM   637  N  ND2 . ASN A 1 80  ? 4.53898   15.83113  66.17578  1.000 39.48724  ? 79   ASN B ND2 1 
ATOM   638  N  N   . SER A 1 81  ? 5.78841   14.53021  70.29402  1.000 40.09778  ? 80   SER B N   1 
ATOM   639  C  CA  . SER A 1 81  ? 5.06758   13.95801  71.42008  1.000 42.32726  ? 80   SER B CA  1 
ATOM   640  C  C   . SER A 1 81  ? 3.77770   13.26827  71.00386  1.000 42.81927  ? 80   SER B C   1 
ATOM   641  O  O   . SER A 1 81  ? 3.26721   12.44991  71.77012  1.000 44.31747  ? 80   SER B O   1 
ATOM   642  C  CB  . SER A 1 81  ? 4.76628   15.02863  72.46830  1.000 44.64522  ? 80   SER B CB  1 
ATOM   643  O  OG  . SER A 1 81  ? 3.75099   15.91977  72.03633  1.000 43.68226  ? 80   SER B OG  1 
ATOM   644  N  N   . ASN A 1 82  ? 3.25571   13.55977  69.81377  1.000 44.03019  ? 81   ASN B N   1 
ATOM   645  C  CA  . ASN A 1 82  ? 2.12583   12.83452  69.24305  1.000 43.22450  ? 81   ASN B CA  1 
ATOM   646  C  C   . ASN A 1 82  ? 2.58427   11.61374  68.44570  1.000 43.22746  ? 81   ASN B C   1 
ATOM   647  O  O   . ASN A 1 82  ? 1.76907   10.98107  67.76524  1.000 42.16824  ? 81   ASN B O   1 
ATOM   648  C  CB  . ASN A 1 82  ? 1.26568   13.76109  68.35829  1.000 44.53697  ? 81   ASN B CB  1 
ATOM   649  C  CG  . ASN A 1 82  ? 0.46278   14.80513  69.17669  1.000 50.84253  ? 81   ASN B CG  1 
ATOM   650  O  OD1 . ASN A 1 82  ? 0.41653   14.74833  70.40007  1.000 47.20340  ? 81   ASN B OD1 1 
ATOM   651  N  ND2 . ASN A 1 82  ? -0.17825  15.74423  68.48503  1.000 50.90894  ? 81   ASN B ND2 1 
ATOM   652  N  N   . GLY A 1 83  ? 3.87701   11.30384  68.46497  1.000 40.75912  ? 82   GLY B N   1 
ATOM   653  C  CA  . GLY A 1 83  ? 4.35183   10.14391  67.75051  1.000 43.31629  ? 82   GLY B CA  1 
ATOM   654  C  C   . GLY A 1 83  ? 4.55006   10.30833  66.26796  1.000 41.12208  ? 82   GLY B C   1 
ATOM   655  O  O   . GLY A 1 83  ? 4.87869   9.32349   65.60776  1.000 42.35064  ? 82   GLY B O   1 
ATOM   656  N  N   . SER A 1 84  ? 4.37313   11.50804  65.71771  1.000 43.36927  ? 83   SER B N   1 
ATOM   657  C  CA  . SER A 1 84  ? 4.62088   11.67693  64.29405  1.000 43.13890  ? 83   SER B CA  1 
ATOM   658  C  C   . SER A 1 84  ? 6.09038   11.43964  63.99365  1.000 43.71184  ? 83   SER B C   1 
ATOM   659  O  O   . SER A 1 84  ? 6.95987   11.70197  64.82677  1.000 42.68128  ? 83   SER B O   1 
ATOM   660  C  CB  . SER A 1 84  ? 4.21317   13.07036  63.83068  1.000 39.69052  ? 83   SER B CB  1 
ATOM   661  O  OG  . SER A 1 84  ? 2.82356   13.11020  63.59173  1.000 39.07848  ? 83   SER B OG  1 
ATOM   662  N  N   . ILE A 1 85  ? 6.35841   10.92558  62.79240  1.000 43.55281  ? 84   ILE B N   1 
ATOM   663  C  CA  . ILE A 1 85  ? 7.69673   10.53678  62.36270  1.000 43.23696  ? 84   ILE B CA  1 
ATOM   664  C  C   . ILE A 1 85  ? 8.08989   11.35974  61.14896  1.000 45.87342  ? 84   ILE B C   1 
ATOM   665  O  O   . ILE A 1 85  ? 7.37067   11.37284  60.14418  1.000 45.64951  ? 84   ILE B O   1 
ATOM   666  C  CB  . ILE A 1 85  ? 7.76309   9.04220   62.01007  1.000 45.08523  ? 84   ILE B CB  1 
ATOM   667  C  CG1 . ILE A 1 85  ? 7.20104   8.19549   63.14314  1.000 44.39038  ? 84   ILE B CG1 1 
ATOM   668  C  CG2 . ILE A 1 85  ? 9.18488   8.65397   61.64068  1.000 45.39867  ? 84   ILE B CG2 1 
ATOM   669  C  CD1 . ILE A 1 85  ? 6.92890   6.78799   62.72501  1.000 41.87681  ? 84   ILE B CD1 1 
ATOM   670  N  N   . CYS A 1 86  ? 9.25222   11.99690  61.22239  1.000 45.72825  ? 85   CYS B N   1 
ATOM   671  C  CA  . CYS A 1 86  ? 9.82979   12.73226  60.09965  1.000 45.96906  ? 85   CYS B CA  1 
ATOM   672  C  C   . CYS A 1 86  ? 10.79912  11.80052  59.39057  1.000 48.45137  ? 85   CYS B C   1 
ATOM   673  O  O   . CYS A 1 86  ? 11.94559  11.64179  59.81600  1.000 49.85239  ? 85   CYS B O   1 
ATOM   674  C  CB  . CYS A 1 86  ? 10.53470  14.00672  60.55474  1.000 47.79240  ? 85   CYS B CB  1 
ATOM   675  S  SG  . CYS A 1 86  ? 11.36606  14.92744  59.17757  1.000 50.60140  ? 85   CYS B SG  1 
ATOM   676  N  N   . LEU A 1 87  ? 10.33841  11.19817  58.29895  1.000 47.42644  ? 86   LEU B N   1 
ATOM   677  C  CA  . LEU A 1 87  ? 11.11817  10.20088  57.57555  1.000 50.54703  ? 86   LEU B CA  1 
ATOM   678  C  C   . LEU A 1 87  ? 10.80892  10.34750  56.09344  1.000 49.51010  ? 86   LEU B C   1 
ATOM   679  O  O   . LEU A 1 87  ? 9.64183   10.27808  55.68876  1.000 48.74077  ? 86   LEU B O   1 
ATOM   680  C  CB  . LEU A 1 87  ? 10.79656  8.78179   58.05094  1.000 47.54864  ? 86   LEU B CB  1 
ATOM   681  C  CG  . LEU A 1 87  ? 11.67027  7.71534   57.38943  1.000 49.09876  ? 86   LEU B CG  1 
ATOM   682  C  CD1 . LEU A 1 87  ? 13.14314  8.06133   57.57288  1.000 48.40103  ? 86   LEU B CD1 1 
ATOM   683  C  CD2 . LEU A 1 87  ? 11.36732  6.34071   57.93747  1.000 47.45934  ? 86   LEU B CD2 1 
ATOM   684  N  N   . ASP A 1 88  ? 11.85210  10.58413  55.29641  1.000 50.49279  ? 87   ASP B N   1 
ATOM   685  C  CA  . ASP A 1 88  ? 11.65412  10.90257  53.88619  1.000 54.87401  ? 87   ASP B CA  1 
ATOM   686  C  C   . ASP A 1 88  ? 10.85868  9.82179   53.16895  1.000 56.11822  ? 87   ASP B C   1 
ATOM   687  O  O   . ASP A 1 88  ? 9.99665   10.12782  52.33573  1.000 53.84904  ? 87   ASP B O   1 
ATOM   688  C  CB  . ASP A 1 88  ? 13.01162  11.05693  53.20161  1.000 59.73393  ? 87   ASP B CB  1 
ATOM   689  C  CG  . ASP A 1 88  ? 13.91711  9.81794   53.39026  1.000 69.88353  ? 87   ASP B CG  1 
ATOM   690  O  OD1 . ASP A 1 88  ? 13.55378  8.90574   54.18107  1.000 61.52526  ? 87   ASP B OD1 1 
ATOM   691  O  OD2 . ASP A 1 88  ? 14.97479  9.74569   52.71278  1.000 71.25415  ? 87   ASP B OD2 1 
ATOM   692  N  N   . ILE A 1 89  ? 11.07324  8.56238   53.54830  1.000 53.31432  ? 88   ILE B N   1 
ATOM   693  C  CA  . ILE A 1 89  ? 10.39316  7.44408   52.91391  1.000 54.27584  ? 88   ILE B CA  1 
ATOM   694  C  C   . ILE A 1 89  ? 8.89025   7.59082   53.01490  1.000 53.79649  ? 88   ILE B C   1 
ATOM   695  O  O   . ILE A 1 89  ? 8.15994   7.14438   52.12192  1.000 52.70562  ? 88   ILE B O   1 
ATOM   696  C  CB  . ILE A 1 89  ? 10.89505  6.13780   53.55993  1.000 52.97187  ? 88   ILE B CB  1 
ATOM   697  C  CG1 . ILE A 1 89  ? 12.39697  6.04598   53.33110  1.000 52.58157  ? 88   ILE B CG1 1 
ATOM   698  C  CG2 . ILE A 1 89  ? 10.11785  4.93117   53.07983  1.000 52.65767  ? 88   ILE B CG2 1 
ATOM   699  C  CD1 . ILE A 1 89  ? 12.75779  6.07324   51.87061  1.000 50.40767  ? 88   ILE B CD1 1 
ATOM   700  N  N   . LEU A 1 90  ? 8.41985   8.30663   54.03072  1.000 52.88566  ? 89   LEU B N   1 
ATOM   701  C  CA  . LEU A 1 90  ? 7.00566   8.45269   54.31872  1.000 53.24242  ? 89   LEU B CA  1 
ATOM   702  C  C   . LEU A 1 90  ? 6.37733   9.62858   53.59777  1.000 56.53828  ? 89   LEU B C   1 
ATOM   703  O  O   . LEU A 1 90  ? 5.15639   9.78896   53.67259  1.000 59.64869  ? 89   LEU B O   1 
ATOM   704  C  CB  . LEU A 1 90  ? 6.79354   8.62316   55.82485  1.000 50.00113  ? 89   LEU B CB  1 
ATOM   705  C  CG  . LEU A 1 90  ? 7.12099   7.37025   56.62677  1.000 46.16044  ? 89   LEU B CG  1 
ATOM   706  C  CD1 . LEU A 1 90  ? 6.95702   7.62843   58.09564  1.000 48.10333  ? 89   LEU B CD1 1 
ATOM   707  C  CD2 . LEU A 1 90  ? 6.20860   6.28502   56.16372  1.000 45.74065  ? 89   LEU B CD2 1 
ATOM   708  N  N   . ARG A 1 91  ? 7.16461   10.44868  52.89840  1.000 57.50219  ? 90   ARG B N   1 
ATOM   709  C  CA  . ARG A 1 91  ? 6.56838   11.55852  52.16621  1.000 62.04293  ? 90   ARG B CA  1 
ATOM   710  C  C   . ARG A 1 91  ? 7.17387   11.70953  50.77242  1.000 59.58946  ? 90   ARG B C   1 
ATOM   711  O  O   . ARG A 1 91  ? 6.64533   11.16932  49.79358  1.000 58.98497  ? 90   ARG B O   1 
ATOM   712  C  CB  . ARG A 1 91  ? 6.73142   12.86236  52.95251  1.000 66.23539  ? 90   ARG B CB  1 
ATOM   713  C  CG  . ARG A 1 91  ? 5.86681   14.01800  52.41377  1.000 82.10090  ? 90   ARG B CG  1 
ATOM   714  C  CD  . ARG A 1 91  ? 6.13784   15.39076  53.08667  1.000 93.90229  ? 90   ARG B CD  1 
ATOM   715  N  NE  . ARG A 1 91  ? 5.03910   16.33427  52.87535  1.000 102.89996 ? 90   ARG B NE  1 
ATOM   716  C  CZ  . ARG A 1 91  ? 5.14360   17.65807  52.92041  1.000 106.65088 ? 90   ARG B CZ  1 
ATOM   717  N  NH1 . ARG A 1 91  ? 6.29820   18.25619  53.16832  1.000 105.89606 ? 90   ARG B NH1 1 
ATOM   718  N  NH2 . ARG A 1 91  ? 4.05860   18.40153  52.71632  1.000 106.81348 ? 90   ARG B NH2 1 
ATOM   719  N  N   . SER A 1 92  ? 8.28770   12.42833  50.67062  1.000 61.61857  ? 91   SER B N   1 
ATOM   720  C  CA  . SER A 1 92  ? 8.84191   12.72663  49.35393  1.000 63.41154  ? 91   SER B CA  1 
ATOM   721  C  C   . SER A 1 92  ? 9.46573   11.49387  48.71878  1.000 61.14486  ? 91   SER B C   1 
ATOM   722  O  O   . SER A 1 92  ? 9.22538   11.20813  47.54076  1.000 61.79532  ? 91   SER B O   1 
ATOM   723  C  CB  . SER A 1 92  ? 9.86062   13.86351  49.45400  1.000 65.96177  ? 91   SER B CB  1 
ATOM   724  O  OG  . SER A 1 92  ? 11.06584  13.43047  50.06045  1.000 74.04442  ? 91   SER B OG  1 
ATOM   725  N  N   . GLN A 1 93  ? 10.22640  10.72750  49.49393  1.000 60.03167  ? 92   GLN B N   1 
ATOM   726  C  CA  . GLN A 1 93  ? 10.97695  9.59787   48.97493  1.000 59.15325  ? 92   GLN B CA  1 
ATOM   727  C  C   . GLN A 1 93  ? 10.17346  8.30617   48.97061  1.000 57.71993  ? 92   GLN B C   1 
ATOM   728  O  O   . GLN A 1 93  ? 10.76051  7.21759   48.89680  1.000 57.95512  ? 92   GLN B O   1 
ATOM   729  C  CB  . GLN A 1 93  ? 12.25168  9.39685   49.78690  1.000 59.34892  ? 92   GLN B CB  1 
ATOM   730  C  CG  . GLN A 1 93  ? 13.24271  10.51449  49.62743  1.000 63.26429  ? 92   GLN B CG  1 
ATOM   731  C  CD  . GLN A 1 93  ? 13.66990  10.71140  48.19106  1.000 71.74538  ? 92   GLN B CD  1 
ATOM   732  O  OE1 . GLN A 1 93  ? 13.05791  11.48701  47.44823  1.000 69.48968  ? 92   GLN B OE1 1 
ATOM   733  N  NE2 . GLN A 1 93  ? 14.70185  9.98727   47.77809  1.000 73.49317  ? 92   GLN B NE2 1 
ATOM   734  N  N   . TRP A 1 94  ? 8.85052   8.39207   49.02576  1.000 55.04208  ? 93   TRP B N   1 
ATOM   735  C  CA  . TRP A 1 94  ? 8.05417   7.18531   48.90983  1.000 52.86663  ? 93   TRP B CA  1 
ATOM   736  C  C   . TRP A 1 94  ? 8.13289   6.64859   47.48439  1.000 52.18782  ? 93   TRP B C   1 
ATOM   737  O  O   . TRP A 1 94  ? 8.08464   7.40276   46.50703  1.000 54.78864  ? 93   TRP B O   1 
ATOM   738  C  CB  . TRP A 1 94  ? 6.60176   7.44416   49.30148  1.000 49.67508  ? 93   TRP B CB  1 
ATOM   739  C  CG  . TRP A 1 94  ? 5.73091   6.25919   49.06553  1.000 50.51088  ? 93   TRP B CG  1 
ATOM   740  C  CD1 . TRP A 1 94  ? 4.79628   6.10270   48.08462  1.000 51.40434  ? 93   TRP B CD1 1 
ATOM   741  C  CD2 . TRP A 1 94  ? 5.75884   5.02859   49.79125  1.000 49.23648  ? 93   TRP B CD2 1 
ATOM   742  N  NE1 . TRP A 1 94  ? 4.21807   4.85945   48.17355  1.000 51.14813  ? 93   TRP B NE1 1 
ATOM   743  C  CE2 . TRP A 1 94  ? 4.79159   4.18084   49.21551  1.000 48.71346  ? 93   TRP B CE2 1 
ATOM   744  C  CE3 . TRP A 1 94  ? 6.48836   4.57170   50.89348  1.000 50.78835  ? 93   TRP B CE3 1 
ATOM   745  C  CZ2 . TRP A 1 94  ? 4.53542   2.89939   49.70247  1.000 49.12786  ? 93   TRP B CZ2 1 
ATOM   746  C  CZ3 . TRP A 1 94  ? 6.23174   3.28793   51.38345  1.000 49.29692  ? 93   TRP B CZ3 1 
ATOM   747  C  CH2 . TRP A 1 94  ? 5.26570   2.46957   50.78275  1.000 47.90412  ? 93   TRP B CH2 1 
ATOM   748  N  N   . SER A 1 95  ? 8.28514   5.33429   47.37893  1.000 51.71496  ? 94   SER B N   1 
ATOM   749  C  CA  . SER A 1 95  ? 8.26149   4.58547   46.13725  1.000 52.76228  ? 94   SER B CA  1 
ATOM   750  C  C   . SER A 1 95  ? 7.21172   3.49016   46.24582  1.000 51.15940  ? 94   SER B C   1 
ATOM   751  O  O   . SER A 1 95  ? 7.03546   2.90990   47.31857  1.000 49.41130  ? 94   SER B O   1 
ATOM   752  C  CB  . SER A 1 95  ? 9.63241   3.96710   45.82718  1.000 52.21994  ? 94   SER B CB  1 
ATOM   753  O  OG  . SER A 1 95  ? 9.50721   2.93907   44.85802  1.000 55.88501  ? 94   SER B OG  1 
ATOM   754  N  N   . PRO A 1 96  ? 6.46515   3.21936   45.17093  1.000 52.30742  ? 95   PRO B N   1 
ATOM   755  C  CA  . PRO A 1 96  ? 5.50249   2.10897   45.21437  1.000 52.94809  ? 95   PRO B CA  1 
ATOM   756  C  C   . PRO A 1 96  ? 6.14655   0.72150   45.34507  1.000 52.61662  ? 95   PRO B C   1 
ATOM   757  O  O   . PRO A 1 96  ? 5.42308   -0.25600  45.57321  1.000 48.87677  ? 95   PRO B O   1 
ATOM   758  C  CB  . PRO A 1 96  ? 4.73412   2.26820   43.89490  1.000 54.00935  ? 95   PRO B CB  1 
ATOM   759  C  CG  . PRO A 1 96  ? 4.84972   3.73556   43.57846  1.000 55.18487  ? 95   PRO B CG  1 
ATOM   760  C  CD  . PRO A 1 96  ? 6.24424   4.09169   44.00225  1.000 54.19515  ? 95   PRO B CD  1 
ATOM   761  N  N   . ALA A 1 97  ? 7.46958   0.60673   45.23642  1.000 52.87820  ? 96   ALA B N   1 
ATOM   762  C  CA  . ALA A 1 97  ? 8.17424   -0.65211  45.45266  1.000 52.39569  ? 96   ALA B CA  1 
ATOM   763  C  C   . ALA A 1 97  ? 8.53559   -0.90776  46.90606  1.000 52.16555  ? 96   ALA B C   1 
ATOM   764  O  O   . ALA A 1 97  ? 9.06577   -1.97692  47.21969  1.000 52.53816  ? 96   ALA B O   1 
ATOM   765  C  CB  . ALA A 1 97  ? 9.46472   -0.68949  44.62950  1.000 52.81962  ? 96   ALA B CB  1 
ATOM   766  N  N   . LEU A 1 98  ? 8.29565   0.03174   47.80108  1.000 51.23206  ? 97   LEU B N   1 
ATOM   767  C  CA  . LEU A 1 98  ? 8.66103   -0.21679  49.17942  1.000 50.12298  ? 97   LEU B CA  1 
ATOM   768  C  C   . LEU A 1 98  ? 7.52153   -0.90759  49.91523  1.000 49.48857  ? 97   LEU B C   1 
ATOM   769  O  O   . LEU A 1 98  ? 6.34953   -0.79423  49.54491  1.000 49.14029  ? 97   LEU B O   1 
ATOM   770  C  CB  . LEU A 1 98  ? 9.03519   1.07842   49.88117  1.000 49.61059  ? 97   LEU B CB  1 
ATOM   771  C  CG  . LEU A 1 98  ? 10.37881  1.64061   49.44492  1.000 49.91313  ? 97   LEU B CG  1 
ATOM   772  C  CD1 . LEU A 1 98  ? 10.42429  3.07824   49.89427  1.000 50.25093  ? 97   LEU B CD1 1 
ATOM   773  C  CD2 . LEU A 1 98  ? 11.52331  0.83484   50.01097  1.000 48.25993  ? 97   LEU B CD2 1 
ATOM   774  N  N   . THR A 1 99  ? 7.88427   -1.64958  50.95139  1.000 48.80684  ? 98   THR B N   1 
ATOM   775  C  CA  . THR A 1 99  ? 6.93921   -2.41868  51.73661  1.000 47.86386  ? 98   THR B CA  1 
ATOM   776  C  C   . THR A 1 99  ? 6.99844   -1.95845  53.18844  1.000 47.16991  ? 98   THR B C   1 
ATOM   777  O  O   . THR A 1 99  ? 7.93077   -1.26755  53.61127  1.000 44.84188  ? 98   THR B O   1 
ATOM   778  C  CB  . THR A 1 99  ? 7.24884   -3.91341  51.65556  1.000 48.63962  ? 98   THR B CB  1 
ATOM   779  O  OG1 . THR A 1 99  ? 8.51793   -4.15776  52.27158  1.000 48.77018  ? 98   THR B OG1 1 
ATOM   780  C  CG2 . THR A 1 99  ? 7.28818   -4.37518  50.19877  1.000 49.53286  ? 98   THR B CG2 1 
ATOM   781  N  N   . ILE A 1 100 ? 5.98624   -2.36812  53.95460  1.000 43.66431  ? 99   ILE B N   1 
ATOM   782  C  CA  . ILE A 1 100 ? 5.95480   -2.06510  55.38425  1.000 47.03778  ? 99   ILE B CA  1 
ATOM   783  C  C   . ILE A 1 100 ? 7.20530   -2.59881  56.06620  1.000 46.82913  ? 99   ILE B C   1 
ATOM   784  O  O   . ILE A 1 100 ? 7.74434   -1.97221  56.98063  1.000 44.76845  ? 99   ILE B O   1 
ATOM   785  C  CB  . ILE A 1 100 ? 4.68332   -2.65655  56.01370  1.000 44.38230  ? 99   ILE B CB  1 
ATOM   786  C  CG1 . ILE A 1 100 ? 3.43744   -1.91318  55.54753  1.000 43.42855  ? 99   ILE B CG1 1 
ATOM   787  C  CG2 . ILE A 1 100 ? 4.76259   -2.55079  57.51153  1.000 45.93833  ? 99   ILE B CG2 1 
ATOM   788  C  CD1 . ILE A 1 100 ? 3.41974   -0.48602  55.98254  1.000 40.67724  ? 99   ILE B CD1 1 
ATOM   789  N  N   . SER A 1 101 ? 7.66485   -3.78069  55.64073  1.000 46.99986  ? 100  SER B N   1 
ATOM   790  C  CA  A SER A 1 101 ? 8.88647   -4.36451  56.18733  0.918 46.15561  ? 100  SER B CA  1 
ATOM   791  C  CA  B SER A 1 101 ? 8.88513   -4.36839  56.18559  0.082 48.51667  ? 100  SER B CA  1 
ATOM   792  C  C   . SER A 1 101 ? 10.06349  -3.41452  56.04169  1.000 45.98967  ? 100  SER B C   1 
ATOM   793  O  O   . SER A 1 101 ? 10.79115  -3.15192  57.00889  1.000 46.44403  ? 100  SER B O   1 
ATOM   794  C  CB  A SER A 1 101 ? 9.18547   -5.69420  55.48154  0.918 48.45499  ? 100  SER B CB  1 
ATOM   795  C  CB  B SER A 1 101 ? 9.18094   -5.69411  55.47576  0.082 50.57076  ? 100  SER B CB  1 
ATOM   796  O  OG  A SER A 1 101 ? 10.45665  -6.21074  55.84436  0.918 49.56330  ? 100  SER B OG  1 
ATOM   797  O  OG  B SER A 1 101 ? 7.98803   -6.39630  55.18104  0.082 49.08225  ? 100  SER B OG  1 
ATOM   798  N  N   . LYS A 1 102 ? 10.27256  -2.89841  54.82638  1.000 46.87063  ? 101  LYS B N   1 
ATOM   799  C  CA  . LYS A 1 102 ? 11.33967  -1.93693  54.60149  1.000 41.75488  ? 101  LYS B CA  1 
ATOM   800  C  C   . LYS A 1 102 ? 11.12676  -0.68548  55.43244  1.000 43.97332  ? 101  LYS B C   1 
ATOM   801  O  O   . LYS A 1 102 ? 12.08498  -0.11712  55.95726  1.000 42.56183  ? 101  LYS B O   1 
ATOM   802  C  CB  . LYS A 1 102 ? 11.43321  -1.58783  53.11739  1.000 45.68082  ? 101  LYS B CB  1 
ATOM   803  C  CG  . LYS A 1 102 ? 11.42724  -2.80355  52.20671  1.000 49.64209  ? 101  LYS B CG  1 
ATOM   804  C  CD  . LYS A 1 102 ? 12.79048  -3.48523  52.20521  1.000 54.86851  ? 101  LYS B CD  1 
ATOM   805  C  CE  . LYS A 1 102 ? 12.77781  -4.86486  51.51503  1.000 66.02310  ? 101  LYS B CE  1 
ATOM   806  N  NZ  . LYS A 1 102 ? 11.90072  -5.91084  52.16930  1.000 55.21280  ? 101  LYS B NZ  1 
ATOM   807  N  N   . VAL A 1 103 ? 9.87779   -0.24205  55.56628  1.000 43.91415  ? 102  VAL B N   1 
ATOM   808  C  CA  . VAL A 1 103 ? 9.59643   0.96947   56.33093  1.000 42.26966  ? 102  VAL B CA  1 
ATOM   809  C  C   . VAL A 1 103 ? 9.98739   0.77884   57.78922  1.000 42.01735  ? 102  VAL B C   1 
ATOM   810  O  O   . VAL A 1 103 ? 10.57793  1.66941   58.40713  1.000 41.85798  ? 102  VAL B O   1 
ATOM   811  C  CB  . VAL A 1 103 ? 8.11275   1.35941   56.19476  1.000 38.78613  ? 102  VAL B CB  1 
ATOM   812  C  CG1 . VAL A 1 103 ? 7.75378   2.43771   57.18846  1.000 41.91971  ? 102  VAL B CG1 1 
ATOM   813  C  CG2 . VAL A 1 103 ? 7.81112   1.80729   54.78670  1.000 39.24685  ? 102  VAL B CG2 1 
ATOM   814  N  N   . LEU A 1 104 ? 9.65019   -0.37487  58.36594  1.000 40.73127  ? 103  LEU B N   1 
ATOM   815  C  CA  . LEU A 1 104 ? 10.02934  -0.65243  59.74567  1.000 43.00595  ? 103  LEU B CA  1 
ATOM   816  C  C   . LEU A 1 104 ? 11.54015  -0.71261  59.88928  1.000 43.70715  ? 103  LEU B C   1 
ATOM   817  O  O   . LEU A 1 104 ? 12.10021  -0.19176  60.86232  1.000 42.29263  ? 103  LEU B O   1 
ATOM   818  C  CB  . LEU A 1 104 ? 9.39540   -1.97027  60.19706  1.000 43.83633  ? 103  LEU B CB  1 
ATOM   819  C  CG  . LEU A 1 104 ? 7.86764   -1.92406  60.28553  1.000 42.10491  ? 103  LEU B CG  1 
ATOM   820  C  CD1 . LEU A 1 104 ? 7.25073   -3.28454  60.41309  1.000 42.10507  ? 103  LEU B CD1 1 
ATOM   821  C  CD2 . LEU A 1 104 ? 7.42229   -1.06192  61.44761  1.000 40.63556  ? 103  LEU B CD2 1 
ATOM   822  N  N   . LEU A 1 105 ? 12.22675  -1.28914  58.89855  1.000 43.77913  ? 104  LEU B N   1 
ATOM   823  C  CA  . LEU A 1 105 ? 13.68692  -1.30114  58.96727  1.000 44.47254  ? 104  LEU B CA  1 
ATOM   824  C  C   . LEU A 1 105 ? 14.25007  0.11146   58.85123  1.000 43.76758  ? 104  LEU B C   1 
ATOM   825  O  O   . LEU A 1 105 ? 15.22000  0.45465   59.53028  1.000 45.25580  ? 104  LEU B O   1 
ATOM   826  C  CB  . LEU A 1 105 ? 14.27483  -2.20949  57.88007  1.000 46.49648  ? 104  LEU B CB  1 
ATOM   827  C  CG  . LEU A 1 105 ? 14.06164  -3.71840  58.03954  1.000 49.25276  ? 104  LEU B CG  1 
ATOM   828  C  CD1 . LEU A 1 105 ? 14.68762  -4.52616  56.90141  1.000 48.72196  ? 104  LEU B CD1 1 
ATOM   829  C  CD2 . LEU A 1 105 ? 14.60597  -4.17010  59.39457  1.000 52.12094  ? 104  LEU B CD2 1 
ATOM   830  N  N   . SER A 1 106 ? 13.64707  0.94748   58.00977  1.000 44.65375  ? 105  SER B N   1 
ATOM   831  C  CA  A SER A 1 106 ? 14.10923  2.32347   57.89182  0.624 45.93703  ? 105  SER B CA  1 
ATOM   832  C  CA  B SER A 1 106 ? 14.09643  2.33059   57.88759  0.376 45.54062  ? 105  SER B CA  1 
ATOM   833  C  C   . SER A 1 106 ? 13.83299  3.11453   59.16800  1.000 44.51924  ? 105  SER B C   1 
ATOM   834  O  O   . SER A 1 106 ? 14.61083  3.99838   59.52504  1.000 44.27739  ? 105  SER B O   1 
ATOM   835  C  CB  A SER A 1 106 ? 13.45882  2.99257   56.67962  0.624 44.44242  ? 105  SER B CB  1 
ATOM   836  C  CB  B SER A 1 106 ? 13.41831  3.00204   56.68790  0.376 43.89002  ? 105  SER B CB  1 
ATOM   837  O  OG  A SER A 1 106 ? 13.72847  2.26328   55.49270  0.624 44.93541  ? 105  SER B OG  1 
ATOM   838  O  OG  B SER A 1 106 ? 13.82040  4.35634   56.54798  0.376 45.26429  ? 105  SER B OG  1 
ATOM   839  N  N   . ILE A 1 107 ? 12.75186  2.79888   59.87332  1.000 44.62164  ? 106  ILE B N   1 
ATOM   840  C  CA  . ILE A 1 107 ? 12.50844  3.42596   61.16603  1.000 44.43399  ? 106  ILE B CA  1 
ATOM   841  C  C   . ILE A 1 107 ? 13.54442  2.97397   62.18434  1.000 44.91644  ? 106  ILE B C   1 
ATOM   842  O  O   . ILE A 1 107 ? 14.02686  3.77468   62.98669  1.000 43.47465  ? 106  ILE B O   1 
ATOM   843  C  CB  . ILE A 1 107 ? 11.07846  3.13011   61.63917  1.000 44.37638  ? 106  ILE B CB  1 
ATOM   844  C  CG1 . ILE A 1 107 ? 10.09864  3.93949   60.80400  1.000 44.61510  ? 106  ILE B CG1 1 
ATOM   845  C  CG2 . ILE A 1 107 ? 10.91667  3.46910   63.09569  1.000 43.59046  ? 106  ILE B CG2 1 
ATOM   846  C  CD1 . ILE A 1 107 ? 8.68938   3.60201   61.10895  1.000 48.60734  ? 106  ILE B CD1 1 
ATOM   847  N  N   . CYS A 1 108 ? 13.90233  1.68868   62.18153  1.000 44.88213  ? 107  CYS B N   1 
ATOM   848  C  CA  . CYS A 1 108 ? 14.97743  1.24561   63.06922  1.000 45.27637  ? 107  CYS B CA  1 
ATOM   849  C  C   . CYS A 1 108 ? 16.28894  1.93467   62.72071  1.000 46.87805  ? 107  CYS B C   1 
ATOM   850  O  O   . CYS A 1 108 ? 17.06107  2.31988   63.60917  1.000 48.48850  ? 107  CYS B O   1 
ATOM   851  C  CB  . CYS A 1 108 ? 15.14639  -0.26983  63.00663  1.000 45.50919  ? 107  CYS B CB  1 
ATOM   852  S  SG  . CYS A 1 108 ? 13.70342  -1.21242  63.52150  1.000 49.24417  ? 107  CYS B SG  1 
ATOM   853  N  N   . SER A 1 109 ? 16.55601  2.10917   61.42896  1.000 46.32588  ? 108  SER B N   1 
ATOM   854  C  CA  . SER A 1 109 ? 17.75825  2.83069   61.04268  1.000 48.22041  ? 108  SER B CA  1 
ATOM   855  C  C   . SER A 1 109 ? 17.68368  4.28497   61.50192  1.000 46.11543  ? 108  SER B C   1 
ATOM   856  O  O   . SER A 1 109 ? 18.65809  4.82913   62.02803  1.000 48.12023  ? 108  SER B O   1 
ATOM   857  C  CB  . SER A 1 109 ? 17.96903  2.72966   59.53343  1.000 50.34228  ? 108  SER B CB  1 
ATOM   858  O  OG  . SER A 1 109 ? 19.31881  3.02522   59.21938  1.000 58.44250  ? 108  SER B OG  1 
ATOM   859  N  N   . LEU A 1 110 ? 16.51306  4.90621   61.36795  1.000 45.57491  ? 109  LEU B N   1 
ATOM   860  C  CA  . LEU A 1 110 ? 16.31368  6.25973   61.87315  1.000 46.85628  ? 109  LEU B CA  1 
ATOM   861  C  C   . LEU A 1 110 ? 16.55691  6.33359   63.38092  1.000 47.08408  ? 109  LEU B C   1 
ATOM   862  O  O   . LEU A 1 110 ? 17.16722  7.29158   63.86872  1.000 46.30982  ? 109  LEU B O   1 
ATOM   863  C  CB  . LEU A 1 110 ? 14.90123  6.73649   61.52553  1.000 45.76831  ? 109  LEU B CB  1 
ATOM   864  C  CG  . LEU A 1 110 ? 14.48963  8.15112   61.95199  1.000 48.52124  ? 109  LEU B CG  1 
ATOM   865  C  CD1 . LEU A 1 110 ? 15.27641  9.24138   61.20677  1.000 49.11797  ? 109  LEU B CD1 1 
ATOM   866  C  CD2 . LEU A 1 110 ? 12.98983  8.34342   61.80187  1.000 47.21439  ? 109  LEU B CD2 1 
ATOM   867  N  N   . LEU A 1 111 ? 16.08365  5.33392   64.13641  1.000 48.03352  ? 110  LEU B N   1 
ATOM   868  C  CA  . LEU A 1 111 ? 16.36879  5.28202   65.57211  1.000 48.26874  ? 110  LEU B CA  1 
ATOM   869  C  C   . LEU A 1 111 ? 17.85547  5.14176   65.84549  1.000 49.87370  ? 110  LEU B C   1 
ATOM   870  O  O   . LEU A 1 111 ? 18.34023  5.60116   66.88499  1.000 53.30650  ? 110  LEU B O   1 
ATOM   871  C  CB  . LEU A 1 111 ? 15.64704  4.11611   66.24621  1.000 45.66324  ? 110  LEU B CB  1 
ATOM   872  C  CG  . LEU A 1 111 ? 14.12861  4.09817   66.30272  1.000 44.86955  ? 110  LEU B CG  1 
ATOM   873  C  CD1 . LEU A 1 111 ? 13.67810  3.23081   67.47455  1.000 45.02452  ? 110  LEU B CD1 1 
ATOM   874  C  CD2 . LEU A 1 111 ? 13.61430  5.49288   66.44852  1.000 45.79839  ? 110  LEU B CD2 1 
ATOM   875  N  N   . CYS A 1 112 ? 18.59015  4.49681   64.94467  1.000 47.55366  ? 111  CYS B N   1 
ATOM   876  C  CA  . CYS A 1 112 ? 20.02958  4.38135   65.14492  1.000 50.28145  ? 111  CYS B CA  1 
ATOM   877  C  C   . CYS A 1 112 ? 20.77173  5.62853   64.67784  1.000 52.93144  ? 111  CYS B C   1 
ATOM   878  O  O   . CYS A 1 112 ? 21.78253  6.00769   65.27695  1.000 54.28535  ? 111  CYS B O   1 
ATOM   879  C  CB  . CYS A 1 112 ? 20.57056  3.14376   64.42265  1.000 51.89186  ? 111  CYS B CB  1 
ATOM   880  S  SG  . CYS A 1 112 ? 20.10533  1.52291   65.14969  1.000 56.05766  ? 111  CYS B SG  1 
ATOM   881  N  N   . ASP A 1 113 ? 20.30653  6.26794   63.60838  1.000 52.88033  ? 112  ASP B N   1 
ATOM   882  C  CA  . ASP A 1 113 ? 21.02630  7.37426   62.97675  1.000 55.64260  ? 112  ASP B CA  1 
ATOM   883  C  C   . ASP A 1 113 ? 20.05007  8.51837   62.73146  1.000 53.68755  ? 112  ASP B C   1 
ATOM   884  O  O   . ASP A 1 113 ? 19.56694  8.69928   61.60679  1.000 52.04167  ? 112  ASP B O   1 
ATOM   885  C  CB  . ASP A 1 113 ? 21.68245  6.89814   61.67504  1.000 59.77798  ? 112  ASP B CB  1 
ATOM   886  C  CG  . ASP A 1 113 ? 22.87766  7.73793   61.27419  1.000 69.19363  ? 112  ASP B CG  1 
ATOM   887  O  OD1 . ASP A 1 113 ? 23.90438  7.68908   61.98743  1.000 68.47073  ? 112  ASP B OD1 1 
ATOM   888  O  OD2 . ASP A 1 113 ? 22.79278  8.43343   60.23891  1.000 77.56727  ? 112  ASP B OD2 1 
ATOM   889  N  N   . PRO A 1 114 ? 19.75141  9.32457   63.75658  1.000 55.59287  ? 113  PRO B N   1 
ATOM   890  C  CA  . PRO A 1 114 ? 18.80000  10.43465  63.57470  1.000 53.13702  ? 113  PRO B CA  1 
ATOM   891  C  C   . PRO A 1 114 ? 19.30649  11.47220  62.57882  1.000 54.74297  ? 113  PRO B C   1 
ATOM   892  O  O   . PRO A 1 114 ? 20.50505  11.56926  62.30365  1.000 55.30512  ? 113  PRO B O   1 
ATOM   893  C  CB  . PRO A 1 114 ? 18.67778  11.03476  64.98328  1.000 51.61296  ? 113  PRO B CB  1 
ATOM   894  C  CG  . PRO A 1 114 ? 19.04971  9.91617   65.90234  1.000 50.90954  ? 113  PRO B CG  1 
ATOM   895  C  CD  . PRO A 1 114 ? 20.15767  9.18570   65.16575  1.000 53.80037  ? 113  PRO B CD  1 
ATOM   896  N  N   . ASN A 1 115 ? 18.35761  12.23304  62.00886  1.000 53.70933  ? 114  ASN B N   1 
ATOM   897  C  CA  . ASN A 1 115 ? 18.61294  13.35651  61.10454  1.000 54.55305  ? 114  ASN B CA  1 
ATOM   898  C  C   . ASN A 1 115 ? 18.32465  14.60890  61.92428  1.000 54.55112  ? 114  ASN B C   1 
ATOM   899  O  O   . ASN A 1 115 ? 17.18878  15.11073  61.91935  1.000 53.80698  ? 114  ASN B O   1 
ATOM   900  C  CB  . ASN A 1 115 ? 17.69086  13.31199  59.88259  1.000 55.31658  ? 114  ASN B CB  1 
ATOM   901  C  CG  . ASN A 1 115 ? 17.79620  12.02508  59.11081  1.000 64.88896  ? 114  ASN B CG  1 
ATOM   902  O  OD1 . ASN A 1 115 ? 18.87265  11.44208  58.97942  1.000 65.80063  ? 114  ASN B OD1 1 
ATOM   903  N  ND2 . ASN A 1 115 ? 16.65075  11.53056  58.65129  1.000 63.47791  ? 114  ASN B ND2 1 
ATOM   904  N  N   . PRO A 1 116 ? 19.30813  15.17627  62.62368  1.000 53.86847  ? 115  PRO B N   1 
ATOM   905  C  CA  . PRO A 1 116 ? 19.03639  16.37809  63.42988  1.000 55.04182  ? 115  PRO B CA  1 
ATOM   906  C  C   . PRO A 1 116 ? 18.90001  17.67768  62.64668  1.000 56.42756  ? 115  PRO B C   1 
ATOM   907  O  O   . PRO A 1 116 ? 18.57642  18.70844  63.24903  1.000 56.34042  ? 115  PRO B O   1 
ATOM   908  C  CB  . PRO A 1 116 ? 20.25265  16.43492  64.36484  1.000 54.32470  ? 115  PRO B CB  1 
ATOM   909  C  CG  . PRO A 1 116 ? 21.32879  15.68741  63.64470  1.000 53.74997  ? 115  PRO B CG  1 
ATOM   910  C  CD  . PRO A 1 116 ? 20.63911  14.60552  62.88567  1.000 50.60840  ? 115  PRO B CD  1 
ATOM   911  N  N   . ASP A 1 117 ? 19.14695  17.67044  61.34022  1.000 58.20494  ? 116  ASP B N   1 
ATOM   912  C  CA  . ASP A 1 117 ? 18.96480  18.84211  60.49640  1.000 58.16245  ? 116  ASP B CA  1 
ATOM   913  C  C   . ASP A 1 117 ? 17.54056  18.97295  59.99256  1.000 58.02494  ? 116  ASP B C   1 
ATOM   914  O  O   . ASP A 1 117 ? 17.22666  19.95060  59.30747  1.000 59.59319  ? 116  ASP B O   1 
ATOM   915  C  CB  . ASP A 1 117 ? 19.93569  18.82270  59.32418  1.000 59.63177  ? 116  ASP B CB  1 
ATOM   916  C  CG  . ASP A 1 117 ? 21.35922  19.06163  59.76539  1.000 65.45898  ? 116  ASP B CG  1 
ATOM   917  O  OD1 . ASP A 1 117 ? 21.54506  19.60606  60.88046  1.000 62.81013  ? 116  ASP B OD1 1 
ATOM   918  O  OD2 . ASP A 1 117 ? 22.28369  18.70662  58.99825  1.000 72.06138  ? 116  ASP B OD2 1 
ATOM   919  N  N   . ASP A 1 118 ? 16.67941  18.00353  60.29095  1.000 55.06506  ? 117  ASP B N   1 
ATOM   920  C  CA  . ASP A 1 118 ? 15.25966  18.08565  59.95096  1.000 54.94831  ? 117  ASP B CA  1 
ATOM   921  C  C   . ASP A 1 118 ? 14.45807  17.61440  61.15481  1.000 54.35834  ? 117  ASP B C   1 
ATOM   922  O  O   . ASP A 1 118 ? 13.72801  16.62197  61.08026  1.000 51.12937  ? 117  ASP B O   1 
ATOM   923  C  CB  . ASP A 1 118 ? 14.94681  17.23169  58.71638  1.000 56.05057  ? 117  ASP B CB  1 
ATOM   924  C  CG  . ASP A 1 118 ? 13.56767  17.52045  58.12956  1.000 56.62909  ? 117  ASP B CG  1 
ATOM   925  O  OD1 . ASP A 1 118 ? 12.89320  18.43103  58.64689  1.000 59.33625  ? 117  ASP B OD1 1 
ATOM   926  O  OD2 . ASP A 1 118 ? 13.13165  16.79792  57.20015  1.000 54.64096  ? 117  ASP B OD2 1 
ATOM   927  N  N   . PRO A 1 119 ? 14.52377  18.34919  62.26930  1.000 54.86338  ? 118  PRO B N   1 
ATOM   928  C  CA  . PRO A 1 119 ? 13.94126  17.86314  63.52482  1.000 54.05383  ? 118  PRO B CA  1 
ATOM   929  C  C   . PRO A 1 119 ? 12.43434  18.02219  63.57101  1.000 48.01820  ? 118  PRO B C   1 
ATOM   930  O  O   . PRO A 1 119 ? 11.85000  18.87468  62.90918  1.000 45.70536  ? 118  PRO B O   1 
ATOM   931  C  CB  . PRO A 1 119 ? 14.55657  18.79119  64.58486  1.000 48.65866  ? 118  PRO B CB  1 
ATOM   932  C  CG  . PRO A 1 119 ? 15.59302  19.56391  63.89164  1.000 51.48864  ? 118  PRO B CG  1 
ATOM   933  C  CD  . PRO A 1 119 ? 15.16525  19.65480  62.46974  1.000 53.16662  ? 118  PRO B CD  1 
ATOM   934  N  N   . LEU A 1 120 ? 11.82402  17.24314  64.45747  1.000 47.22923  ? 119  LEU B N   1 
ATOM   935  C  CA  . LEU A 1 120 ? 10.45552  17.47867  64.88943  1.000 45.04616  ? 119  LEU B CA  1 
ATOM   936  C  C   . LEU A 1 120 ? 10.41266  18.01800  66.30731  1.000 46.46017  ? 119  LEU B C   1 
ATOM   937  O  O   . LEU A 1 120 ? 9.38123   18.55366  66.72508  1.000 47.17004  ? 119  LEU B O   1 
ATOM   938  C  CB  . LEU A 1 120 ? 9.62573   16.18984  64.79658  1.000 46.52913  ? 119  LEU B CB  1 
ATOM   939  C  CG  . LEU A 1 120 ? 8.87664   15.88264  63.49038  1.000 46.00700  ? 119  LEU B CG  1 
ATOM   940  C  CD1 . LEU A 1 120 ? 7.81354   14.81291  63.72671  1.000 43.10284  ? 119  LEU B CD1 1 
ATOM   941  C  CD2 . LEU A 1 120 ? 8.26726   17.11929  62.81709  1.000 43.02366  ? 119  LEU B CD2 1 
ATOM   942  N  N   . VAL A 1 121 ? 11.49509  17.83554  67.05818  1.000 42.40631  ? 120  VAL B N   1 
ATOM   943  C  CA  . VAL A 1 121 ? 11.69470  18.38166  68.39369  1.000 43.02412  ? 120  VAL B CA  1 
ATOM   944  C  C   . VAL A 1 121 ? 13.05817  19.06950  68.40202  1.000 42.28929  ? 120  VAL B C   1 
ATOM   945  O  O   . VAL A 1 121 ? 14.09057  18.39845  68.55242  1.000 41.54715  ? 120  VAL B O   1 
ATOM   946  C  CB  . VAL A 1 121 ? 11.57672  17.29729  69.47905  1.000 44.52134  ? 120  VAL B CB  1 
ATOM   947  C  CG1 . VAL A 1 121 ? 11.62987  17.94127  70.84606  1.000 42.63778  ? 120  VAL B CG1 1 
ATOM   948  C  CG2 . VAL A 1 121 ? 10.27048  16.53065  69.34125  1.000 42.70254  ? 120  VAL B CG2 1 
ATOM   949  N  N   . PRO A 1 122 ? 13.10775  20.39668  68.19696  1.000 40.32401  ? 121  PRO B N   1 
ATOM   950  C  CA  . PRO A 1 122 ? 14.41084  21.07736  68.07530  1.000 41.32525  ? 121  PRO B CA  1 
ATOM   951  C  C   . PRO A 1 122 ? 15.34304  20.88941  69.26922  1.000 42.46569  ? 121  PRO B C   1 
ATOM   952  O  O   . PRO A 1 122 ? 16.56386  20.80887  69.07591  1.000 42.92248  ? 121  PRO B O   1 
ATOM   953  C  CB  . PRO A 1 122 ? 14.01338  22.55743  67.87728  1.000 40.77743  ? 121  PRO B CB  1 
ATOM   954  C  CG  . PRO A 1 122 ? 12.64343  22.50183  67.27363  1.000 40.19342  ? 121  PRO B CG  1 
ATOM   955  C  CD  . PRO A 1 122 ? 11.97532  21.29113  67.90115  1.000 41.84868  ? 121  PRO B CD  1 
ATOM   956  N  N   . GLU A 1 123 ? 14.82508  20.84916  70.49815  1.000 42.29115  ? 122  GLU B N   1 
ATOM   957  C  CA  . GLU A 1 123 ? 15.71996  20.72417  71.64743  1.000 42.39419  ? 122  GLU B CA  1 
ATOM   958  C  C   . GLU A 1 123 ? 16.42418  19.36899  71.67753  1.000 42.46486  ? 122  GLU B C   1 
ATOM   959  O  O   . GLU A 1 123 ? 17.59966  19.27679  72.07675  1.000 42.13658  ? 122  GLU B O   1 
ATOM   960  C  CB  . GLU A 1 123 ? 14.96945  20.99577  72.95194  1.000 43.23192  ? 122  GLU B CB  1 
ATOM   961  C  CG  . GLU A 1 123 ? 15.88067  20.85677  74.16791  1.000 42.23334  ? 122  GLU B CG  1 
ATOM   962  C  CD  . GLU A 1 123 ? 17.09794  21.79098  74.11672  1.000 44.92790  ? 122  GLU B CD  1 
ATOM   963  O  OE1 . GLU A 1 123 ? 17.11980  22.74574  73.30961  1.000 44.48584  ? 122  GLU B OE1 1 
ATOM   964  O  OE2 . GLU A 1 123 ? 18.06943  21.54418  74.86631  1.000 45.19278  ? 122  GLU B OE2 1 
ATOM   965  N  N   . ILE A 1 124 ? 15.72306  18.30452  71.27336  1.000 41.59651  ? 123  ILE B N   1 
ATOM   966  C  CA  . ILE A 1 124 ? 16.35634  16.99242  71.18714  1.000 42.14710  ? 123  ILE B CA  1 
ATOM   967  C  C   . ILE A 1 124 ? 17.40930  16.96328  70.07137  1.000 42.47598  ? 123  ILE B C   1 
ATOM   968  O  O   . ILE A 1 124 ? 18.50188  16.41144  70.24610  1.000 43.73343  ? 123  ILE B O   1 
ATOM   969  C  CB  . ILE A 1 124 ? 15.29005  15.90441  70.98783  1.000 43.74931  ? 123  ILE B CB  1 
ATOM   970  C  CG1 . ILE A 1 124 ? 14.29321  15.87606  72.14216  1.000 42.94401  ? 123  ILE B CG1 1 
ATOM   971  C  CG2 . ILE A 1 124 ? 15.94410  14.55748  70.98222  1.000 42.65948  ? 123  ILE B CG2 1 
ATOM   972  C  CD1 . ILE A 1 124 ? 13.24596  14.81929  71.93347  1.000 42.07240  ? 123  ILE B CD1 1 
ATOM   973  N  N   . ALA A 1 125 ? 17.10884  17.55753  68.91585  1.000 39.43233  ? 124  ALA B N   1 
ATOM   974  C  CA  . ALA A 1 125 ? 18.11407  17.64328  67.85874  1.000 44.36355  ? 124  ALA B CA  1 
ATOM   975  C  C   . ALA A 1 125 ? 19.34228  18.41659  68.32870  1.000 46.55482  ? 124  ALA B C   1 
ATOM   976  O  O   . ALA A 1 125 ? 20.48057  18.06915  67.98347  1.000 49.49263  ? 124  ALA B O   1 
ATOM   977  C  CB  . ALA A 1 125 ? 17.52269  18.31170  66.61599  1.000 45.74555  ? 124  ALA B CB  1 
ATOM   978  N  N   . ARG A 1 126 ? 19.12889  19.46695  69.12607  1.000 44.18141  ? 125  ARG B N   1 
ATOM   979  C  CA  . ARG A 1 126 ? 20.24436  20.24941  69.65038  1.000 46.60500  ? 125  ARG B CA  1 
ATOM   980  C  C   . ARG A 1 126 ? 21.12821  19.43017  70.58602  1.000 48.80849  ? 125  ARG B C   1 
ATOM   981  O  O   . ARG A 1 126 ? 22.36602  19.51846  70.52111  1.000 47.92881  ? 125  ARG B O   1 
ATOM   982  C  CB  . ARG A 1 126 ? 19.71974  21.50601  70.34336  1.000 45.20510  ? 125  ARG B CB  1 
ATOM   983  C  CG  . ARG A 1 126 ? 20.81690  22.29106  71.03236  1.000 46.96995  ? 125  ARG B CG  1 
ATOM   984  C  CD  . ARG A 1 126 ? 20.29323  23.50837  71.75369  1.000 44.22871  ? 125  ARG B CD  1 
ATOM   985  N  NE  . ARG A 1 126 ? 19.84270  24.48835  70.77544  1.000 47.86613  ? 125  ARG B NE  1 
ATOM   986  C  CZ  . ARG A 1 126 ? 20.64966  25.31908  70.13291  1.000 46.28099  ? 125  ARG B CZ  1 
ATOM   987  N  NH1 . ARG A 1 126 ? 21.95209  25.33868  70.37027  1.000 44.87645  ? 125  ARG B NH1 1 
ATOM   988  N  NH2 . ARG A 1 126 ? 20.14526  26.11752  69.19741  1.000 48.37911  ? 125  ARG B NH2 1 
ATOM   989  N  N   . ILE A 1 127 ? 20.51133  18.66784  71.49665  1.000 47.15919  ? 126  ILE B N   1 
ATOM   990  C  CA  . ILE A 1 127 ? 21.28293  17.78838  72.37885  1.000 47.31597  ? 126  ILE B CA  1 
ATOM   991  C  C   . ILE A 1 127 ? 22.03853  16.72781  71.57400  1.000 51.77125  ? 126  ILE B C   1 
ATOM   992  O  O   . ILE A 1 127 ? 23.22720  16.47062  71.81295  1.000 52.13810  ? 126  ILE B O   1 
ATOM   993  C  CB  . ILE A 1 127 ? 20.35861  17.15412  73.42880  1.000 48.81120  ? 126  ILE B CB  1 
ATOM   994  C  CG1 . ILE A 1 127 ? 19.79382  18.25478  74.30486  1.000 44.84354  ? 126  ILE B CG1 1 
ATOM   995  C  CG2 . ILE A 1 127 ? 21.12934  16.21675  74.32973  1.000 49.11253  ? 126  ILE B CG2 1 
ATOM   996  C  CD1 . ILE A 1 127 ? 20.88821  18.96294  75.02610  1.000 44.01023  ? 126  ILE B CD1 1 
ATOM   997  N  N   . TYR A 1 128 ? 21.36299  16.09572  70.60785  1.000 48.48451  ? 127  TYR B N   1 
ATOM   998  C  CA  . TYR A 1 128 ? 22.03870  15.10680  69.77665  1.000 50.32961  ? 127  TYR B CA  1 
ATOM   999  C  C   . TYR A 1 128 ? 23.26196  15.70590  69.10124  1.000 52.26219  ? 127  TYR B C   1 
ATOM   1000 O  O   . TYR A 1 128 ? 24.33197  15.08511  69.08033  1.000 53.03146  ? 127  TYR B O   1 
ATOM   1001 C  CB  . TYR A 1 128 ? 21.08133  14.54625  68.71916  1.000 50.22857  ? 127  TYR B CB  1 
ATOM   1002 C  CG  . TYR A 1 128 ? 21.67562  13.45485  67.84248  1.000 51.34626  ? 127  TYR B CG  1 
ATOM   1003 C  CD1 . TYR A 1 128 ? 21.69045  12.12707  68.25514  1.000 52.25751  ? 127  TYR B CD1 1 
ATOM   1004 C  CD2 . TYR A 1 128 ? 22.22564  13.75535  66.59889  1.000 52.14988  ? 127  TYR B CD2 1 
ATOM   1005 C  CE1 . TYR A 1 128 ? 22.23064  11.12822  67.44621  1.000 53.38459  ? 127  TYR B CE1 1 
ATOM   1006 C  CE2 . TYR A 1 128 ? 22.76877  12.77245  65.78838  1.000 52.80203  ? 127  TYR B CE2 1 
ATOM   1007 C  CZ  . TYR A 1 128 ? 22.77380  11.45453  66.21035  1.000 59.36580  ? 127  TYR B CZ  1 
ATOM   1008 O  OH  . TYR A 1 128 ? 23.31263  10.46053  65.40112  1.000 55.84019  ? 127  TYR B OH  1 
ATOM   1009 N  N   . LYS A 1 129 ? 23.14615  16.94101  68.59651  1.000 51.17846  ? 128  LYS B N   1 
ATOM   1010 C  CA  . LYS A 1 129 ? 24.26869  17.52678  67.87275  1.000 51.30360  ? 128  LYS B CA  1 
ATOM   1011 C  C   . LYS A 1 129 ? 25.37408  18.02603  68.79423  1.000 52.74941  ? 128  LYS B C   1 
ATOM   1012 O  O   . LYS A 1 129 ? 26.53417  18.06593  68.37367  1.000 53.91502  ? 128  LYS B O   1 
ATOM   1013 C  CB  . LYS A 1 129 ? 23.78063  18.67862  66.98464  1.000 53.96594  ? 128  LYS B CB  1 
ATOM   1014 C  CG  . LYS A 1 129 ? 22.88396  18.23656  65.85031  1.000 54.86978  ? 128  LYS B CG  1 
ATOM   1015 C  CD  . LYS A 1 129 ? 22.40445  19.40075  64.98641  1.000 60.92366  ? 128  LYS B CD  1 
ATOM   1016 C  CE  . LYS A 1 129 ? 23.53802  20.05353  64.21452  1.000 66.24825  ? 128  LYS B CE  1 
ATOM   1017 N  NZ  . LYS A 1 129 ? 23.01808  20.87748  63.08850  1.000 65.03471  ? 128  LYS B NZ  1 
ATOM   1018 N  N   . THR A 1 130 ? 25.07188  18.32862  70.05276  1.000 54.96139  ? 129  THR B N   1 
ATOM   1019 C  CA  . THR A 1 130 ? 26.06734  18.94343  70.92450  1.000 57.09251  ? 129  THR B CA  1 
ATOM   1020 C  C   . THR A 1 130 ? 26.68195  17.97443  71.91630  1.000 58.27266  ? 129  THR B C   1 
ATOM   1021 O  O   . THR A 1 130 ? 27.89436  18.01497  72.13019  1.000 59.38416  ? 129  THR B O   1 
ATOM   1022 C  CB  . THR A 1 130 ? 25.45953  20.11685  71.71099  1.000 53.97480  ? 129  THR B CB  1 
ATOM   1023 O  OG1 . THR A 1 130 ? 24.32051  19.66096  72.43990  1.000 59.98236  ? 129  THR B OG1 1 
ATOM   1024 C  CG2 . THR A 1 130 ? 25.03041  21.22388  70.78045  1.000 54.35942  ? 129  THR B CG2 1 
ATOM   1025 N  N   . ASP A 1 131 ? 25.87824  17.08096  72.51348  1.000 57.76144  ? 130  ASP B N   1 
ATOM   1026 C  CA  . ASP A 1 131 ? 26.33128  16.20774  73.59828  1.000 66.30897  ? 130  ASP B CA  1 
ATOM   1027 C  C   . ASP A 1 131 ? 25.76922  14.79118  73.39063  1.000 61.03949  ? 130  ASP B C   1 
ATOM   1028 O  O   . ASP A 1 131 ? 24.83577  14.35673  74.06560  1.000 62.20868  ? 130  ASP B O   1 
ATOM   1029 C  CB  . ASP A 1 131 ? 25.93555  16.79341  74.96213  1.000 62.53439  ? 130  ASP B CB  1 
ATOM   1030 C  CG  . ASP A 1 131 ? 26.64273  16.11718  76.12494  1.000 66.45610  ? 130  ASP B CG  1 
ATOM   1031 O  OD1 . ASP A 1 131 ? 27.35056  15.10797  75.89753  1.000 69.03953  ? 130  ASP B OD1 1 
ATOM   1032 O  OD2 . ASP A 1 131 ? 26.50599  16.60578  77.26751  1.000 67.89922  ? 130  ASP B OD2 1 
ATOM   1033 N  N   . ARG A 1 132 ? 26.35318  14.06750  72.42857  1.000 58.15142  ? 131  ARG B N   1 
ATOM   1034 C  CA  . ARG A 1 132 ? 25.87637  12.72583  72.08579  1.000 60.53437  ? 131  ARG B CA  1 
ATOM   1035 C  C   . ARG A 1 132 ? 25.74368  11.83592  73.31556  1.000 60.89848  ? 131  ARG B C   1 
ATOM   1036 O  O   . ARG A 1 132 ? 24.75766  11.10439  73.46215  1.000 57.40978  ? 131  ARG B O   1 
ATOM   1037 C  CB  . ARG A 1 132 ? 26.82385  12.09235  71.06819  1.000 55.16597  ? 131  ARG B CB  1 
ATOM   1038 C  CG  . ARG A 1 132 ? 26.30924  10.84195  70.44128  1.000 51.14986  ? 131  ARG B CG  1 
ATOM   1039 C  CD  . ARG A 1 132 ? 25.04925  11.11261  69.62409  1.000 52.40264  ? 131  ARG B CD  1 
ATOM   1040 N  NE  . ARG A 1 132 ? 25.16207  12.27375  68.75099  1.000 52.15727  ? 131  ARG B NE  1 
ATOM   1041 C  CZ  . ARG A 1 132 ? 25.82435  12.31101  67.60349  1.000 52.32695  ? 131  ARG B CZ  1 
ATOM   1042 N  NH1 . ARG A 1 132 ? 26.45482  11.24965  67.13266  1.000 52.76022  ? 131  ARG B NH1 1 
ATOM   1043 N  NH2 . ARG A 1 132 ? 25.84998  13.44460  66.90709  1.000 57.28863  ? 131  ARG B NH2 1 
ATOM   1044 N  N   . GLU A 1 133 ? 26.70135  11.93608  74.23455  1.000 62.95095  ? 132  GLU B N   1 
ATOM   1045 C  CA  . GLU A 1 133 ? 26.67124  11.15354  75.46551  1.000 67.40526  ? 132  GLU B CA  1 
ATOM   1046 C  C   . GLU A 1 133 ? 25.41092  11.44141  76.28111  1.000 66.48498  ? 132  GLU B C   1 
ATOM   1047 O  O   . GLU A 1 133 ? 24.73467  10.51465  76.75759  1.000 66.31488  ? 132  GLU B O   1 
ATOM   1048 C  CB  . GLU A 1 133 ? 27.93677  11.49025  76.25379  1.000 74.57450  ? 132  GLU B CB  1 
ATOM   1049 C  CG  . GLU A 1 133 ? 28.05778  10.95205  77.63666  1.000 83.90049  ? 132  GLU B CG  1 
ATOM   1050 C  CD  . GLU A 1 133 ? 29.30010  11.48305  78.34209  1.000 97.79930  ? 132  GLU B CD  1 
ATOM   1051 O  OE1 . GLU A 1 133 ? 29.49154  12.72746  78.36400  1.000 98.23415  ? 132  GLU B OE1 1 
ATOM   1052 O  OE2 . GLU A 1 133 ? 30.08062  10.66167  78.87068  1.000 101.54968 ? 132  GLU B OE2 1 
ATOM   1053 N  N   . LYS A 1 134 ? 25.03858  12.72086  76.39311  1.000 64.80398  ? 133  LYS B N   1 
ATOM   1054 C  CA  . LYS A 1 134 ? 23.85140  13.08033  77.16244  1.000 64.01337  ? 133  LYS B CA  1 
ATOM   1055 C  C   . LYS A 1 134 ? 22.57464  12.69102  76.43101  1.000 59.13484  ? 133  LYS B C   1 
ATOM   1056 O  O   . LYS A 1 134 ? 21.60249  12.24703  77.06121  1.000 56.55513  ? 133  LYS B O   1 
ATOM   1057 C  CB  . LYS A 1 134 ? 23.86356  14.57908  77.47443  1.000 65.21367  ? 133  LYS B CB  1 
ATOM   1058 C  CG  . LYS A 1 134 ? 22.69729  15.04760  78.33009  1.000 63.70880  ? 133  LYS B CG  1 
ATOM   1059 C  CD  . LYS A 1 134 ? 22.39675  14.03934  79.47761  1.000 78.91160  ? 133  LYS B CD  1 
ATOM   1060 C  CE  . LYS A 1 134 ? 23.46241  14.04390  80.58641  1.000 85.91423  ? 133  LYS B CE  1 
ATOM   1061 N  NZ  . LYS A 1 134 ? 23.13141  13.20233  81.79383  1.000 81.45750  ? 133  LYS B NZ  1 
ATOM   1062 N  N   . TYR A 1 135 ? 22.55464  12.86415  75.10376  1.000 57.39089  ? 134  TYR B N   1 
ATOM   1063 C  CA  . TYR A 1 135 ? 21.42303  12.38964  74.31699  1.000 55.81517  ? 134  TYR B CA  1 
ATOM   1064 C  C   . TYR A 1 135 ? 21.18932  10.90265  74.56942  1.000 54.44703  ? 134  TYR B C   1 
ATOM   1065 O  O   . TYR A 1 135 ? 20.05705  10.47621  74.81490  1.000 51.92695  ? 134  TYR B O   1 
ATOM   1066 C  CB  . TYR A 1 135 ? 21.64793  12.66185  72.82219  1.000 51.70351  ? 134  TYR B CB  1 
ATOM   1067 C  CG  . TYR A 1 135 ? 20.63237  11.96944  71.93121  1.000 49.96305  ? 134  TYR B CG  1 
ATOM   1068 C  CD1 . TYR A 1 135 ? 19.44905  12.59401  71.59469  1.000 47.25200  ? 134  TYR B CD1 1 
ATOM   1069 C  CD2 . TYR A 1 135 ? 20.84865  10.67097  71.44905  1.000 52.40522  ? 134  TYR B CD2 1 
ATOM   1070 C  CE1 . TYR A 1 135 ? 18.50069  11.96878  70.79996  1.000 47.40247  ? 134  TYR B CE1 1 
ATOM   1071 C  CE2 . TYR A 1 135 ? 19.90090  10.03619  70.65195  1.000 50.10609  ? 134  TYR B CE2 1 
ATOM   1072 C  CZ  . TYR A 1 135 ? 18.72866  10.69596  70.32938  1.000 50.84364  ? 134  TYR B CZ  1 
ATOM   1073 O  OH  . TYR A 1 135 ? 17.76429  10.10633  69.54615  1.000 51.35456  ? 134  TYR B OH  1 
ATOM   1074 N  N   . ASN A 1 136 ? 22.25599  10.10147  74.53440  1.000 54.25739  ? 135  ASN B N   1 
ATOM   1075 C  CA  . ASN A 1 136 ? 22.09409  8.66465   74.75736  1.000 59.19459  ? 135  ASN B CA  1 
ATOM   1076 C  C   . ASN A 1 136 ? 21.55720  8.37678   76.15657  1.000 60.48100  ? 135  ASN B C   1 
ATOM   1077 O  O   . ASN A 1 136 ? 20.64409  7.55460   76.31365  1.000 58.62820  ? 135  ASN B O   1 
ATOM   1078 C  CB  . ASN A 1 136 ? 23.41585  7.92990   74.51946  1.000 58.83714  ? 135  ASN B CB  1 
ATOM   1079 C  CG  . ASN A 1 136 ? 23.80634  7.88656   73.05033  1.000 55.67949  ? 135  ASN B CG  1 
ATOM   1080 O  OD1 . ASN A 1 136 ? 22.95437  7.97745   72.16254  1.000 56.04427  ? 135  ASN B OD1 1 
ATOM   1081 N  ND2 . ASN A 1 136 ? 25.10030  7.74817   72.78797  1.000 61.40628  ? 135  ASN B ND2 1 
ATOM   1082 N  N   . ARG A 1 137 ? 22.08289  9.06596   77.18256  1.000 62.86871  ? 136  ARG B N   1 
ATOM   1083 C  CA  . ARG A 1 137 ? 21.58722  8.83262   78.54088  1.000 60.58687  ? 136  ARG B CA  1 
ATOM   1084 C  C   . ARG A 1 137 ? 20.09324  9.10314   78.62202  1.000 57.72284  ? 136  ARG B C   1 
ATOM   1085 O  O   . ARG A 1 137 ? 19.32975  8.30820   79.18456  1.000 56.54380  ? 136  ARG B O   1 
ATOM   1086 C  CB  . ARG A 1 137 ? 22.32951  9.71114   79.55374  1.000 65.19294  ? 136  ARG B CB  1 
ATOM   1087 C  CG  . ARG A 1 137 ? 23.54725  9.06124   80.17233  1.000 71.33833  ? 136  ARG B CG  1 
ATOM   1088 C  CD  . ARG A 1 137 ? 24.76364  9.97039   80.10695  1.000 77.00299  ? 136  ARG B CD  1 
ATOM   1089 N  NE  . ARG A 1 137 ? 26.01034  9.23612   80.30104  1.000 87.80992  ? 136  ARG B NE  1 
ATOM   1090 C  CZ  . ARG A 1 137 ? 26.65539  8.57520   79.34595  1.000 95.83885  ? 136  ARG B CZ  1 
ATOM   1091 N  NH1 . ARG A 1 137 ? 26.14636  8.43975   78.13123  1.000 96.50896  ? 136  ARG B NH1 1 
ATOM   1092 N  NH2 . ARG A 1 137 ? 27.83220  8.01740   79.62148  1.000 96.56575  ? 136  ARG B NH2 1 
ATOM   1093 N  N   . ILE A 1 138 ? 19.65140  10.22112  78.04970  1.000 58.16497  ? 137  ILE B N   1 
ATOM   1094 C  CA  . ILE A 1 138 ? 18.24194  10.57248  78.17112  1.000 55.66366  ? 137  ILE B CA  1 
ATOM   1095 C  C   . ILE A 1 138 ? 17.36408  9.62797   77.36061  1.000 52.66763  ? 137  ILE B C   1 
ATOM   1096 O  O   . ILE A 1 138 ? 16.26363  9.25619   77.78987  1.000 51.65441  ? 137  ILE B O   1 
ATOM   1097 C  CB  . ILE A 1 138 ? 18.04114  12.03079  77.76057  1.000 53.05006  ? 137  ILE B CB  1 
ATOM   1098 C  CG1 . ILE A 1 138 ? 18.98644  12.88280  78.58107  1.000 55.38983  ? 137  ILE B CG1 1 
ATOM   1099 C  CG2 . ILE A 1 138 ? 16.62225  12.44943  78.03944  1.000 52.46115  ? 137  ILE B CG2 1 
ATOM   1100 C  CD1 . ILE A 1 138 ? 19.02564  14.26097  78.10302  1.000 60.45047  ? 137  ILE B CD1 1 
ATOM   1101 N  N   . ALA A 1 139 ? 17.81278  9.25423   76.16776  1.000 52.32592  ? 138  ALA B N   1 
ATOM   1102 C  CA  . ALA A 1 139 ? 17.04011  8.31875   75.36698  1.000 52.50956  ? 138  ALA B CA  1 
ATOM   1103 C  C   . ALA A 1 139 ? 16.86424  6.98773   76.10290  1.000 51.46486  ? 138  ALA B C   1 
ATOM   1104 O  O   . ALA A 1 139 ? 15.78144  6.39289   76.06909  1.000 50.00103  ? 138  ALA B O   1 
ATOM   1105 C  CB  . ALA A 1 139 ? 17.70585  8.13800   74.00445  1.000 50.17001  ? 138  ALA B CB  1 
ATOM   1106 N  N   . ARG A 1 140 ? 17.91171  6.51905   76.79442  1.000 51.82056  ? 139  ARG B N   1 
ATOM   1107 C  CA  . ARG A 1 140 ? 17.78209  5.32487   77.63866  1.000 56.11636  ? 139  ARG B CA  1 
ATOM   1108 C  C   . ARG A 1 140 ? 16.77971  5.52723   78.77739  1.000 54.61112  ? 139  ARG B C   1 
ATOM   1109 O  O   . ARG A 1 140 ? 15.96496  4.63908   79.05614  1.000 56.21189  ? 139  ARG B O   1 
ATOM   1110 C  CB  . ARG A 1 140 ? 19.15254  4.91520   78.19594  1.000 60.66230  ? 139  ARG B CB  1 
ATOM   1111 C  CG  . ARG A 1 140 ? 20.08687  4.29968   77.16522  1.000 66.19637  ? 139  ARG B CG  1 
ATOM   1112 C  CD  . ARG A 1 140 ? 21.42233  3.80429   77.73555  1.000 73.05621  ? 139  ARG B CD  1 
ATOM   1113 N  NE  . ARG A 1 140 ? 22.54346  4.72475   77.53467  1.000 74.42631  ? 139  ARG B NE  1 
ATOM   1114 C  CZ  . ARG A 1 140 ? 23.16897  5.42154   78.47823  1.000 77.80162  ? 139  ARG B CZ  1 
ATOM   1115 N  NH1 . ARG A 1 140 ? 22.79310  5.37669   79.74891  1.000 76.11744  ? 139  ARG B NH1 1 
ATOM   1116 N  NH2 . ARG A 1 140 ? 24.23724  6.14158   78.14599  1.000 83.73019  ? 139  ARG B NH2 1 
ATOM   1117 N  N   . GLU A 1 141 ? 16.82728  6.68161   79.44843  1.000 53.07188  ? 140  GLU B N   1 
ATOM   1118 C  CA  . GLU A 1 141 ? 15.89151  6.93957   80.54597  1.000 55.75967  ? 140  GLU B CA  1 
ATOM   1119 C  C   . GLU A 1 141 ? 14.44842  6.92687   80.05770  1.000 53.25417  ? 140  GLU B C   1 
ATOM   1120 O  O   . GLU A 1 141 ? 13.55850  6.36149   80.70974  1.000 54.24986  ? 140  GLU B O   1 
ATOM   1121 C  CB  . GLU A 1 141 ? 16.20048  8.29895   81.18267  1.000 54.80407  ? 140  GLU B CB  1 
ATOM   1122 C  CG  . GLU A 1 141 ? 17.54856  8.36823   81.87956  1.000 55.86071  ? 140  GLU B CG  1 
ATOM   1123 C  CD  . GLU A 1 141 ? 18.00091  9.78372   82.25731  1.000 63.04992  ? 140  GLU B CD  1 
ATOM   1124 O  OE1 . GLU A 1 141 ? 17.32298  10.79052  81.92538  1.000 60.89922  ? 140  GLU B OE1 1 
ATOM   1125 O  OE2 . GLU A 1 141 ? 19.07929  9.88066   82.87685  1.000 62.25818  ? 140  GLU B OE2 1 
ATOM   1126 N  N   . TRP A 1 142 ? 14.20037  7.53814   78.90043  1.000 53.53558  ? 141  TRP B N   1 
ATOM   1127 C  CA  . TRP A 1 142 ? 12.85729  7.51919   78.32848  1.000 52.43087  ? 141  TRP B CA  1 
ATOM   1128 C  C   . TRP A 1 142 ? 12.44915  6.10975   77.90754  1.000 50.60868  ? 141  TRP B C   1 
ATOM   1129 O  O   . TRP A 1 142 ? 11.27907  5.73009   78.04544  1.000 50.50352  ? 141  TRP B O   1 
ATOM   1130 C  CB  . TRP A 1 142 ? 12.76877  8.47550   77.13167  1.000 50.26900  ? 141  TRP B CB  1 
ATOM   1131 C  CG  . TRP A 1 142 ? 12.55270  9.94271   77.49884  1.000 50.86430  ? 141  TRP B CG  1 
ATOM   1132 C  CD1 . TRP A 1 142 ? 13.16219  10.63208  78.50556  1.000 51.94773  ? 141  TRP B CD1 1 
ATOM   1133 C  CD2 . TRP A 1 142 ? 11.65584  10.86843  76.86950  1.000 50.27646  ? 141  TRP B CD2 1 
ATOM   1134 N  NE1 . TRP A 1 142 ? 12.71108  11.92438  78.54432  1.000 53.64684  ? 141  TRP B NE1 1 
ATOM   1135 C  CE2 . TRP A 1 142 ? 11.78334  12.10319  77.55431  1.000 57.61534  ? 141  TRP B CE2 1 
ATOM   1136 C  CE3 . TRP A 1 142 ? 10.76576  10.77993  75.79238  1.000 49.57572  ? 141  TRP B CE3 1 
ATOM   1137 C  CZ2 . TRP A 1 142 ? 11.05776  13.24841  77.19659  1.000 51.35682  ? 141  TRP B CZ2 1 
ATOM   1138 C  CZ3 . TRP A 1 142 ? 10.03491  11.92277  75.43262  1.000 51.25137  ? 141  TRP B CZ3 1 
ATOM   1139 C  CH2 . TRP A 1 142 ? 10.19084  13.14104  76.14044  1.000 53.66085  ? 141  TRP B CH2 1 
ATOM   1140 N  N   . THR A 1 143 ? 13.39191  5.32917   77.37859  1.000 50.19141  ? 142  THR B N   1 
ATOM   1141 C  CA  . THR A 1 143 ? 13.08785  3.94329   77.03707  1.000 52.80789  ? 142  THR B CA  1 
ATOM   1142 C  C   . THR A 1 143 ? 12.63667  3.17339   78.27558  1.000 51.70172  ? 142  THR B C   1 
ATOM   1143 O  O   . THR A 1 143 ? 11.59460  2.50685   78.26038  1.000 52.33091  ? 142  THR B O   1 
ATOM   1144 C  CB  . THR A 1 143 ? 14.31355  3.29684   76.38287  1.000 50.47899  ? 142  THR B CB  1 
ATOM   1145 O  OG1 . THR A 1 143 ? 14.70043  4.07610   75.25217  1.000 48.35992  ? 142  THR B OG1 1 
ATOM   1146 C  CG2 . THR A 1 143 ? 13.99157  1.89977   75.90131  1.000 52.64628  ? 142  THR B CG2 1 
ATOM   1147 N  N   . GLN A 1 144 ? 13.38323  3.31082   79.37919  1.000 53.63752  ? 143  GLN B N   1 
ATOM   1148 C  CA  . GLN A 1 144 ? 13.02751  2.64793   80.63416  1.000 59.48163  ? 143  GLN B CA  1 
ATOM   1149 C  C   . GLN A 1 144 ? 11.71488  3.14692   81.20626  1.000 59.43405  ? 143  GLN B C   1 
ATOM   1150 O  O   . GLN A 1 144 ? 11.02504  2.40062   81.90565  1.000 59.77009  ? 143  GLN B O   1 
ATOM   1151 C  CB  . GLN A 1 144 ? 14.13970  2.83175   81.66128  1.000 64.53954  ? 143  GLN B CB  1 
ATOM   1152 C  CG  . GLN A 1 144 ? 15.42249  2.15002   81.25670  1.000 67.99775  ? 143  GLN B CG  1 
ATOM   1153 C  CD  . GLN A 1 144 ? 16.55674  2.46398   82.18863  1.000 73.40965  ? 143  GLN B CD  1 
ATOM   1154 O  OE1 . GLN A 1 144 ? 16.37087  3.12673   83.20755  1.000 77.86112  ? 143  GLN B OE1 1 
ATOM   1155 N  NE2 . GLN A 1 144 ? 17.74180  1.96730   81.86232  1.000 74.80671  ? 143  GLN B NE2 1 
ATOM   1156 N  N   . LYS A 1 145 ? 11.33677  4.37525   80.89076  1.000 58.22673  ? 144  LYS B N   1 
ATOM   1157 C  CA  . LYS A 1 145 ? 10.12503  4.91827   81.47423  1.000 57.15762  ? 144  LYS B CA  1 
ATOM   1158 C  C   . LYS A 1 145 ? 8.87272   4.52107   80.69222  1.000 54.07622  ? 144  LYS B C   1 
ATOM   1159 O  O   . LYS A 1 145 ? 7.86982   4.12788   81.29838  1.000 53.70116  ? 144  LYS B O   1 
ATOM   1160 C  CB  . LYS A 1 145 ? 10.25404  6.43976   81.55957  1.000 56.25003  ? 144  LYS B CB  1 
ATOM   1161 C  CG  . LYS A 1 145 ? 9.21319   7.14496   82.38552  1.000 58.05562  ? 144  LYS B CG  1 
ATOM   1162 C  CD  . LYS A 1 145 ? 9.57216   8.60805   82.46440  1.000 59.12524  ? 144  LYS B CD  1 
ATOM   1163 C  CE  . LYS A 1 145 ? 8.74064   9.36999   83.49261  1.000 67.06652  ? 144  LYS B CE  1 
ATOM   1164 N  NZ  . LYS A 1 145 ? 7.74056   10.29102  82.86722  1.000 69.04904  ? 144  LYS B NZ  1 
ATOM   1165 N  N   . TYR A 1 146 ? 8.91233   4.56314   79.35584  1.000 53.64897  ? 145  TYR B N   1 
ATOM   1166 C  CA  . TYR A 1 146 ? 7.70145   4.35646   78.56851  1.000 53.31712  ? 145  TYR B CA  1 
ATOM   1167 C  C   . TYR A 1 146 ? 7.66265   3.07241   77.76632  1.000 54.96726  ? 145  TYR B C   1 
ATOM   1168 O  O   . TYR A 1 146 ? 6.56956   2.64747   77.37830  1.000 56.99398  ? 145  TYR B O   1 
ATOM   1169 C  CB  . TYR A 1 146 ? 7.48874   5.51727   77.57818  1.000 56.36312  ? 145  TYR B CB  1 
ATOM   1170 C  CG  . TYR A 1 146 ? 7.39325   6.88721   78.21209  1.000 51.16710  ? 145  TYR B CG  1 
ATOM   1171 C  CD1 . TYR A 1 146 ? 6.20197   7.32532   78.77832  1.000 52.90544  ? 145  TYR B CD1 1 
ATOM   1172 C  CD2 . TYR A 1 146 ? 8.47530   7.76160   78.20359  1.000 55.27071  ? 145  TYR B CD2 1 
ATOM   1173 C  CE1 . TYR A 1 146 ? 6.09553   8.59115   79.35695  1.000 53.51010  ? 145  TYR B CE1 1 
ATOM   1174 C  CE2 . TYR A 1 146 ? 8.37758   9.04425   78.78040  1.000 53.65757  ? 145  TYR B CE2 1 
ATOM   1175 C  CZ  . TYR A 1 146 ? 7.18513   9.44756   79.35018  1.000 53.75900  ? 145  TYR B CZ  1 
ATOM   1176 O  OH  . TYR A 1 146 ? 7.08345   10.70696  79.91577  1.000 68.38221  ? 145  TYR B OH  1 
ATOM   1177 N  N   . ALA A 1 147 ? 8.81059   2.46054   77.48860  1.000 53.07488  ? 146  ALA B N   1 
ATOM   1178 C  CA  . ALA A 1 147 ? 8.88913   1.39563   76.50779  1.000 52.99664  ? 146  ALA B CA  1 
ATOM   1179 C  C   . ALA A 1 147 ? 9.15620   0.02676   77.11963  1.000 56.05706  ? 146  ALA B C   1 
ATOM   1180 O  O   . ALA A 1 147 ? 9.54559   -0.89462  76.39488  1.000 48.09448  ? 146  ALA B O   1 
ATOM   1181 C  CB  . ALA A 1 147 ? 9.96007   1.73955   75.45974  1.000 49.32175  ? 146  ALA B CB  1 
ATOM   1182 N  N   . MET A 1 148 ? 8.97979   -0.12835  78.43028  1.000 56.82880  ? 147  MET B N   1 
ATOM   1183 C  CA  . MET A 1 148 ? 9.25540   -1.38960  79.10504  1.000 57.41860  ? 147  MET B CA  1 
ATOM   1184 C  C   . MET A 1 148 ? 8.05947   -1.78902  79.97132  1.000 62.47155  ? 147  MET B C   1 
ATOM   1185 O  O   . MET A 1 148 ? 7.14421   -0.99732  80.20915  1.000 67.66620  ? 147  MET B O   1 
ATOM   1186 C  CB  . MET A 1 148 ? 10.55968  -1.27694  79.90169  1.000 58.37999  ? 147  MET B CB  1 
ATOM   1187 C  CG  . MET A 1 148 ? 11.78325  -1.18748  78.97002  1.000 58.49882  ? 147  MET B CG  1 
ATOM   1188 S  SD  . MET A 1 148 ? 13.32709  -0.87498  79.84807  1.000 61.05087  ? 147  MET B SD  1 
ATOM   1189 C  CE  . MET A 1 148 ? 14.50546  -0.69968  78.53451  1.000 56.27339  ? 147  MET B CE  1 
ATOM   1190 N  N   . GLY A 1 149 ? 8.04056   -3.03845  80.41899  1.000 66.19792  ? 148  GLY B N   1 
ATOM   1191 C  CA  . GLY A 1 149 ? 6.90472   -3.52003  81.18664  1.000 77.25143  ? 148  GLY B CA  1 
ATOM   1192 C  C   . GLY A 1 149 ? 5.62585   -3.59848  80.36466  1.000 78.73186  ? 148  GLY B C   1 
ATOM   1193 O  O   . GLY A 1 149 ? 5.38005   -4.58109  79.65818  1.000 82.90596  ? 148  GLY B O   1 
ATOM   1194 N  N   . VAL A 1 174 ? 10.13893  -37.65728 47.56972  1.000 101.65231 ? 943  VAL B N   1 
ATOM   1195 C  CA  . VAL A 1 174 ? 8.91276   -37.10961 47.01036  1.000 106.44365 ? 943  VAL B CA  1 
ATOM   1196 C  C   . VAL A 1 174 ? 8.71070   -35.69571 47.53840  1.000 115.76461 ? 943  VAL B C   1 
ATOM   1197 O  O   . VAL A 1 174 ? 8.00761   -34.88898 46.92895  1.000 114.40381 ? 943  VAL B O   1 
ATOM   1198 C  CB  . VAL A 1 174 ? 7.70364   -38.00654 47.33266  1.000 105.58350 ? 943  VAL B CB  1 
ATOM   1199 C  CG1 . VAL A 1 174 ? 7.38902   -37.97789 48.82413  1.000 108.77902 ? 943  VAL B CG1 1 
ATOM   1200 C  CG2 . VAL A 1 174 ? 6.49327   -37.59541 46.49958  1.000 107.64564 ? 943  VAL B CG2 1 
ATOM   1201 N  N   . ASN A 1 175 ? 9.33361   -35.40436 48.68230  1.000 126.77511 ? 944  ASN B N   1 
ATOM   1202 C  CA  . ASN A 1 175 ? 9.31568   -34.07373 49.27881  1.000 119.52435 ? 944  ASN B CA  1 
ATOM   1203 C  C   . ASN A 1 175 ? 10.54449  -33.25227 48.92468  1.000 111.29523 ? 944  ASN B C   1 
ATOM   1204 O  O   . ASN A 1 175 ? 10.43202  -32.03536 48.76959  1.000 108.28820 ? 944  ASN B O   1 
ATOM   1205 C  CB  . ASN A 1 175 ? 9.19238   -34.16982 50.80928  1.000 126.25826 ? 944  ASN B CB  1 
ATOM   1206 C  CG  . ASN A 1 175 ? 8.97985   -32.80775 51.47836  1.000 130.60620 ? 944  ASN B CG  1 
ATOM   1207 O  OD1 . ASN A 1 175 ? 7.89394   -32.23497 51.41205  1.000 130.70974 ? 944  ASN B OD1 1 
ATOM   1208 N  ND2 . ASN A 1 175 ? 10.01390  -32.30107 52.14262  1.000 133.37754 ? 944  ASN B ND2 1 
ATOM   1209 N  N   . ALA A 1 176 ? 11.71507  -33.87759 48.79438  1.000 110.22414 ? 945  ALA B N   1 
ATOM   1210 C  CA  . ALA A 1 176 ? 12.88319  -33.12946 48.34798  1.000 107.93725 ? 945  ALA B CA  1 
ATOM   1211 C  C   . ALA A 1 176 ? 12.65997  -32.56095 46.95486  1.000 106.15556 ? 945  ALA B C   1 
ATOM   1212 O  O   . ALA A 1 176 ? 13.03955  -31.41855 46.67393  1.000 105.37111 ? 945  ALA B O   1 
ATOM   1213 C  CB  . ALA A 1 176 ? 14.12550  -34.01547 48.37319  1.000 110.35028 ? 945  ALA B CB  1 
ATOM   1214 N  N   . ASP A 1 177 ? 12.02431  -33.33645 46.07038  1.000 107.57627 ? 946  ASP B N   1 
ATOM   1215 C  CA  . ASP A 1 177 ? 11.79043  -32.85347 44.71204  1.000 112.15358 ? 946  ASP B CA  1 
ATOM   1216 C  C   . ASP A 1 177 ? 10.75500  -31.72950 44.66640  1.000 106.06310 ? 946  ASP B C   1 
ATOM   1217 O  O   . ASP A 1 177 ? 10.88495  -30.79736 43.85865  1.000 100.17610 ? 946  ASP B O   1 
ATOM   1218 C  CB  . ASP A 1 177 ? 11.34434  -34.01434 43.81873  1.000 114.81675 ? 946  ASP B CB  1 
ATOM   1219 C  CG  . ASP A 1 177 ? 12.49856  -34.91925 43.40669  1.000 119.45652 ? 946  ASP B CG  1 
ATOM   1220 O  OD1 . ASP A 1 177 ? 13.63321  -34.70969 43.89104  1.000 117.50467 ? 946  ASP B OD1 1 
ATOM   1221 O  OD2 . ASP A 1 177 ? 12.28048  -35.82286 42.56926  1.000 125.16110 ? 946  ASP B OD2 1 
ATOM   1222 N  N   . VAL A 1 178 ? 9.74594   -31.77996 45.54126  1.000 105.06510 ? 947  VAL B N   1 
ATOM   1223 C  CA  . VAL A 1 178 ? 8.76337   -30.69952 45.61461  1.000 103.65937 ? 947  VAL B CA  1 
ATOM   1224 C  C   . VAL A 1 178 ? 9.38256   -29.44398 46.22540  1.000 99.80892  ? 947  VAL B C   1 
ATOM   1225 O  O   . VAL A 1 178 ? 9.12820   -28.32541 45.76220  1.000 98.19139  ? 947  VAL B O   1 
ATOM   1226 C  CB  . VAL A 1 178 ? 7.50783   -31.17115 46.37499  1.000 101.64611 ? 947  VAL B CB  1 
ATOM   1227 C  CG1 . VAL A 1 178 ? 6.54841   -30.01970 46.61980  1.000 99.28731  ? 947  VAL B CG1 1 
ATOM   1228 C  CG2 . VAL A 1 178 ? 6.80488   -32.26619 45.58270  1.000 101.60864 ? 947  VAL B CG2 1 
ATOM   1229 N  N   . GLN A 1 179 ? 10.28347  -29.61204 47.19821  1.000 98.63532  ? 948  GLN B N   1 
ATOM   1230 C  CA  . GLN A 1 179 ? 10.99699  -28.47696 47.77126  1.000 97.54808  ? 948  GLN B CA  1 
ATOM   1231 C  C   . GLN A 1 179 ? 12.10915  -27.96678 46.86561  1.000 97.13827  ? 948  GLN B C   1 
ATOM   1232 O  O   . GLN A 1 179 ? 12.66390  -26.89393 47.13166  1.000 96.02411  ? 948  GLN B O   1 
ATOM   1233 C  CB  . GLN A 1 179 ? 11.60585  -28.88101 49.12399  1.000 91.12440  ? 948  GLN B CB  1 
ATOM   1234 C  CG  . GLN A 1 179 ? 10.61705  -29.30760 50.19071  1.000 90.58615  ? 948  GLN B CG  1 
ATOM   1235 C  CD  . GLN A 1 179 ? 9.72884   -28.16484 50.64089  1.000 86.54044  ? 948  GLN B CD  1 
ATOM   1236 O  OE1 . GLN A 1 179 ? 10.21336  -27.06527 50.89270  1.000 75.20806  ? 948  GLN B OE1 1 
ATOM   1237 N  NE2 . GLN A 1 179 ? 8.42931   -28.41686 50.75002  1.000 88.94061  ? 948  GLN B NE2 1 
ATOM   1238 N  N   . LYS A 1 180 ? 12.43137  -28.69433 45.79846  1.000 98.60921  ? 949  LYS B N   1 
ATOM   1239 C  CA  . LYS A 1 180 ? 13.33754  -28.16690 44.78728  1.000 97.98187  ? 949  LYS B CA  1 
ATOM   1240 C  C   . LYS A 1 180 ? 12.58493  -27.40755 43.68835  1.000 95.11099  ? 949  LYS B C   1 
ATOM   1241 O  O   . LYS A 1 180 ? 12.99456  -26.30782 43.29846  1.000 93.91564  ? 949  LYS B O   1 
ATOM   1242 C  CB  . LYS A 1 180 ? 14.17444  -29.31653 44.20402  1.000 98.26302  ? 949  LYS B CB  1 
ATOM   1243 C  CG  . LYS A 1 180 ? 15.26730  -28.89048 43.24278  1.000 97.85598  ? 949  LYS B CG  1 
ATOM   1244 C  CD  . LYS A 1 180 ? 16.03642  -30.08752 42.72253  1.000 100.77077 ? 949  LYS B CD  1 
ATOM   1245 C  CE  . LYS A 1 180 ? 17.03904  -29.66861 41.65753  1.000 105.89613 ? 949  LYS B CE  1 
ATOM   1246 N  NZ  . LYS A 1 180 ? 17.76289  -30.84832 41.11003  1.000 106.05465 ? 949  LYS B NZ  1 
ATOM   1247 N  N   . LEU A 1 181 ? 11.48080  -27.98139 43.18533  1.000 95.59543  ? 950  LEU B N   1 
ATOM   1248 C  CA  . LEU A 1 181 ? 10.60647  -27.25486 42.26031  1.000 96.27564  ? 950  LEU B CA  1 
ATOM   1249 C  C   . LEU A 1 181 ? 10.08542  -25.94985 42.85649  1.000 96.68807  ? 950  LEU B C   1 
ATOM   1250 O  O   . LEU A 1 181 ? 9.97399   -24.93735 42.15104  1.000 96.49639  ? 950  LEU B O   1 
ATOM   1251 C  CB  . LEU A 1 181 ? 9.43753   -28.13852 41.81307  1.000 97.50144  ? 950  LEU B CB  1 
ATOM   1252 C  CG  . LEU A 1 181 ? 9.75627   -29.40523 41.00832  1.000 98.26362  ? 950  LEU B CG  1 
ATOM   1253 C  CD1 . LEU A 1 181 ? 8.47464   -30.08929 40.52814  1.000 104.09200 ? 950  LEU B CD1 1 
ATOM   1254 C  CD2 . LEU A 1 181 ? 10.68074  -29.09955 39.83064  1.000 92.30295  ? 950  LEU B CD2 1 
ATOM   1255 N  N   . GLN A 1 182 ? 9.75875   -25.94611 44.15167  1.000 97.45182  ? 951  GLN B N   1 
ATOM   1256 C  CA  . GLN A 1 182 ? 9.26570   -24.71919 44.76594  1.000 96.50938  ? 951  GLN B CA  1 
ATOM   1257 C  C   . GLN A 1 182 ? 10.36639  -23.67621 44.85307  1.000 98.03913  ? 951  GLN B C   1 
ATOM   1258 O  O   . GLN A 1 182 ? 10.12333  -22.49431 44.59142  1.000 98.68332  ? 951  GLN B O   1 
ATOM   1259 C  CB  . GLN A 1 182 ? 8.67396   -25.01271 46.13938  1.000 95.70387  ? 951  GLN B CB  1 
ATOM   1260 C  CG  . GLN A 1 182 ? 7.42410   -25.85627 46.06953  1.000 100.41248 ? 951  GLN B CG  1 
ATOM   1261 C  CD  . GLN A 1 182 ? 6.53435   -25.70160 47.27690  1.000 104.33407 ? 951  GLN B CD  1 
ATOM   1262 O  OE1 . GLN A 1 182 ? 7.00941   -25.43463 48.38041  1.000 102.61469 ? 951  GLN B OE1 1 
ATOM   1263 N  NE2 . GLN A 1 182 ? 5.23343   -25.87937 47.07951  1.000 106.93765 ? 951  GLN B NE2 1 
ATOM   1264 N  N   . GLN A 1 183 ? 11.57426  -24.08465 45.25385  1.000 97.16454  ? 952  GLN B N   1 
ATOM   1265 C  CA  . GLN A 1 183 ? 12.69197  -23.14463 45.27875  1.000 100.49160 ? 952  GLN B CA  1 
ATOM   1266 C  C   . GLN A 1 183 ? 12.98721  -22.57423 43.89015  1.000 100.27137 ? 952  GLN B C   1 
ATOM   1267 O  O   . GLN A 1 183 ? 13.28503  -21.37809 43.75807  1.000 99.92068  ? 952  GLN B O   1 
ATOM   1268 C  CB  . GLN A 1 183 ? 13.93667  -23.81193 45.86705  1.000 99.03833  ? 952  GLN B CB  1 
ATOM   1269 C  CG  . GLN A 1 183 ? 15.18902  -22.92720 45.84242  1.000 103.71644 ? 952  GLN B CG  1 
ATOM   1270 C  CD  . GLN A 1 183 ? 14.96634  -21.55440 46.46961  1.000 107.50345 ? 952  GLN B CD  1 
ATOM   1271 O  OE1 . GLN A 1 183 ? 15.20407  -20.51477 45.83360  1.000 103.34472 ? 952  GLN B OE1 1 
ATOM   1272 N  NE2 . GLN A 1 183 ? 14.51587  -21.54405 47.72449  1.000 106.12851 ? 952  GLN B NE2 1 
ATOM   1273 N  N   . GLN A 1 184 ? 12.87940  -23.40213 42.84026  1.000 99.05800  ? 953  GLN B N   1 
ATOM   1274 C  CA  . GLN A 1 184 ? 13.08750  -22.91135 41.47536  1.000 97.45815  ? 953  GLN B CA  1 
ATOM   1275 C  C   . GLN A 1 184 ? 11.99643  -21.92455 41.05221  1.000 97.65278  ? 953  GLN B C   1 
ATOM   1276 O  O   . GLN A 1 184 ? 12.29603  -20.85107 40.50505  1.000 98.21966  ? 953  GLN B O   1 
ATOM   1277 C  CB  . GLN A 1 184 ? 13.19265  -24.08783 40.50375  1.000 93.72361  ? 953  GLN B CB  1 
ATOM   1278 C  CG  . GLN A 1 184 ? 14.57548  -24.74991 40.49828  1.000 93.57268  ? 953  GLN B CG  1 
ATOM   1279 C  CD  . GLN A 1 184 ? 14.63490  -26.02028 39.65062  1.000 96.45096  ? 953  GLN B CD  1 
ATOM   1280 O  OE1 . GLN A 1 184 ? 13.60723  -26.53386 39.21291  1.000 97.92782  ? 953  GLN B OE1 1 
ATOM   1281 N  NE2 . GLN A 1 184 ? 15.84186  -26.52771 39.41855  1.000 92.55636  ? 953  GLN B NE2 1 
ATOM   1282 N  N   . LEU A 1 185 ? 10.72119  -22.26911 41.27139  1.000 97.77039  ? 954  LEU B N   1 
ATOM   1283 C  CA  . LEU A 1 185 ? 9.65636   -21.31513 40.95773  1.000 96.60903  ? 954  LEU B CA  1 
ATOM   1284 C  C   . LEU A 1 185 ? 9.83242   -20.01369 41.73710  1.000 96.12239  ? 954  LEU B C   1 
ATOM   1285 O  O   . LEU A 1 185 ? 9.64495   -18.91871 41.18791  1.000 93.33168  ? 954  LEU B O   1 
ATOM   1286 C  CB  . LEU A 1 185 ? 8.28114   -21.92494 41.25405  1.000 94.48799  ? 954  LEU B CB  1 
ATOM   1287 C  CG  . LEU A 1 185 ? 7.78333   -23.03675 40.31839  1.000 101.17693 ? 954  LEU B CG  1 
ATOM   1288 C  CD1 . LEU A 1 185 ? 6.51270   -23.71021 40.83967  1.000 105.12080 ? 954  LEU B CD1 1 
ATOM   1289 C  CD2 . LEU A 1 185 ? 7.56771   -22.52480 38.89819  1.000 104.37242 ? 954  LEU B CD2 1 
ATOM   1290 N  N   . GLN A 1 186 ? 10.26167  -20.11103 43.00246  1.000 97.07975  ? 955  GLN B N   1 
ATOM   1291 C  CA  . GLN A 1 186 ? 10.37834  -18.92620 43.84339  1.000 95.77006  ? 955  GLN B CA  1 
ATOM   1292 C  C   . GLN A 1 186 ? 11.53647  -18.02961 43.42394  1.000 96.49128  ? 955  GLN B C   1 
ATOM   1293 O  O   . GLN A 1 186 ? 11.38774  -16.80218 43.39412  1.000 97.18667  ? 955  GLN B O   1 
ATOM   1294 C  CB  . GLN A 1 186 ? 10.54382  -19.34038 45.30568  1.000 99.42503  ? 955  GLN B CB  1 
ATOM   1295 C  CG  . GLN A 1 186 ? 10.65717  -18.15761 46.26691  1.000 100.90187 ? 955  GLN B CG  1 
ATOM   1296 C  CD  . GLN A 1 186 ? 10.89442  -18.58279 47.70828  1.000 106.67072 ? 955  GLN B CD  1 
ATOM   1297 O  OE1 . GLN A 1 186 ? 9.98159   -19.05201 48.39534  1.000 101.43638 ? 955  GLN B OE1 1 
ATOM   1298 N  NE2 . GLN A 1 186 ? 12.12678  -18.41519 48.17427  1.000 109.08895 ? 955  GLN B NE2 1 
ATOM   1299 N  N   . ASP A 1 187 ? 12.69820  -18.60747 43.09190  1.000 96.37104  ? 956  ASP B N   1 
ATOM   1300 C  CA  . ASP A 1 187 ? 13.79650  -17.75575 42.64296  1.000 96.02616  ? 956  ASP B CA  1 
ATOM   1301 C  C   . ASP A 1 187 ? 13.62363  -17.24542 41.21256  1.000 93.31009  ? 956  ASP B C   1 
ATOM   1302 O  O   . ASP A 1 187 ? 14.28505  -16.26780 40.84497  1.000 93.49150  ? 956  ASP B O   1 
ATOM   1303 C  CB  . ASP A 1 187 ? 15.14946  -18.47363 42.82685  1.000 99.03173  ? 956  ASP B CB  1 
ATOM   1304 C  CG  . ASP A 1 187 ? 15.41774  -19.58334 41.79334  1.000 107.07313 ? 956  ASP B CG  1 
ATOM   1305 O  OD1 . ASP A 1 187 ? 14.62378  -19.78657 40.85277  1.000 107.13399 ? 956  ASP B OD1 1 
ATOM   1306 O  OD2 . ASP A 1 187 ? 16.44805  -20.28244 41.93899  1.000 107.91619 ? 956  ASP B OD2 1 
ATOM   1307 N  N   . ILE A 1 188 ? 12.76457  -17.86592 40.39216  1.000 91.95178  ? 957  ILE B N   1 
ATOM   1308 C  CA  . ILE A 1 188 ? 12.40964  -17.21637 39.12859  1.000 90.70511  ? 957  ILE B CA  1 
ATOM   1309 C  C   . ILE A 1 188 ? 11.45807  -16.04962 39.37704  1.000 87.64458  ? 957  ILE B C   1 
ATOM   1310 O  O   . ILE A 1 188 ? 11.62379  -14.95239 38.81257  1.000 85.83972  ? 957  ILE B O   1 
ATOM   1311 C  CB  . ILE A 1 188 ? 11.81565  -18.23531 38.13455  1.000 87.97920  ? 957  ILE B CB  1 
ATOM   1312 C  CG1 . ILE A 1 188 ? 12.92899  -19.03971 37.45596  1.000 88.33281  ? 957  ILE B CG1 1 
ATOM   1313 C  CG2 . ILE A 1 188 ? 10.95487  -17.54667 37.08735  1.000 83.04641  ? 957  ILE B CG2 1 
ATOM   1314 C  CD1 . ILE A 1 188 ? 12.42845  -20.02551 36.40557  1.000 85.86038  ? 957  ILE B CD1 1 
ATOM   1315 N  N   . LYS A 1 189 ? 10.48048  -16.24469 40.26902  1.000 87.45956  ? 958  LYS B N   1 
ATOM   1316 C  CA  . LYS A 1 189 ? 9.56326   -15.15819 40.59521  1.000 87.92594  ? 958  LYS B CA  1 
ATOM   1317 C  C   . LYS A 1 189 ? 10.28907  -13.96000 41.19042  1.000 85.25292  ? 958  LYS B C   1 
ATOM   1318 O  O   . LYS A 1 189 ? 10.01235  -12.81701 40.81602  1.000 84.97602  ? 958  LYS B O   1 
ATOM   1319 C  CB  . LYS A 1 189 ? 8.46392   -15.65284 41.53324  1.000 90.32259  ? 958  LYS B CB  1 
ATOM   1320 C  CG  . LYS A 1 189 ? 7.23886   -16.14921 40.79228  1.000 93.06706  ? 958  LYS B CG  1 
ATOM   1321 C  CD  . LYS A 1 189 ? 6.39561   -17.07577 41.65232  1.000 97.85701  ? 958  LYS B CD  1 
ATOM   1322 C  CE  . LYS A 1 189 ? 4.92155   -16.91095 41.32493  1.000 101.80003 ? 958  LYS B CE  1 
ATOM   1323 N  NZ  . LYS A 1 189 ? 4.66589   -17.00220 39.85630  1.000 97.41039  ? 958  LYS B NZ  1 
ATOM   1324 N  N   . GLU A 1 190 ? 11.23442  -14.19523 42.10059  1.000 87.36409  ? 959  GLU B N   1 
ATOM   1325 C  CA  . GLU A 1 190 ? 11.91705  -13.06454 42.72012  1.000 88.79919  ? 959  GLU B CA  1 
ATOM   1326 C  C   . GLU A 1 190 ? 12.58534  -12.15614 41.69579  1.000 86.71521  ? 959  GLU B C   1 
ATOM   1327 O  O   . GLU A 1 190 ? 12.63411  -10.93687 41.89448  1.000 85.50346  ? 959  GLU B O   1 
ATOM   1328 C  CB  . GLU A 1 190 ? 12.92717  -13.53311 43.76673  1.000 91.48889  ? 959  GLU B CB  1 
ATOM   1329 C  CG  . GLU A 1 190 ? 12.27127  -14.17229 44.98474  1.000 100.49400 ? 959  GLU B CG  1 
ATOM   1330 C  CD  . GLU A 1 190 ? 13.27660  -14.57557 46.04135  1.000 110.44649 ? 959  GLU B CD  1 
ATOM   1331 O  OE1 . GLU A 1 190 ? 14.48083  -14.32248 45.82691  1.000 118.62513 ? 959  GLU B OE1 1 
ATOM   1332 O  OE2 . GLU A 1 190 ? 12.86683  -15.13558 47.08221  1.000 111.50965 ? 959  GLU B OE2 1 
ATOM   1333 N  N   . GLN A 1 191 ? 13.09717  -12.71418 40.60509  1.000 86.81435  ? 960  GLN B N   1 
ATOM   1334 C  CA  . GLN A 1 191 ? 13.80023  -11.91030 39.61574  1.000 85.81496  ? 960  GLN B CA  1 
ATOM   1335 C  C   . GLN A 1 191 ? 12.89960  -11.34628 38.51969  1.000 82.68069  ? 960  GLN B C   1 
ATOM   1336 O  O   . GLN A 1 191 ? 13.27294  -10.34088 37.89595  1.000 83.39513  ? 960  GLN B O   1 
ATOM   1337 C  CB  . GLN A 1 191 ? 14.92748  -12.73431 38.98536  1.000 89.97147  ? 960  GLN B CB  1 
ATOM   1338 C  CG  . GLN A 1 191 ? 15.74551  -13.51706 40.00065  1.000 92.50001  ? 960  GLN B CG  1 
ATOM   1339 C  CD  . GLN A 1 191 ? 16.81074  -14.36175 39.33978  1.000 100.23892 ? 960  GLN B CD  1 
ATOM   1340 O  OE1 . GLN A 1 191 ? 17.57201  -13.86892 38.50992  1.000 106.74040 ? 960  GLN B OE1 1 
ATOM   1341 N  NE2 . GLN A 1 191 ? 16.86264  -15.64739 39.69208  1.000 98.03897  ? 960  GLN B NE2 1 
ATOM   1342 N  N   . THR A 1 192 ? 11.72484  -11.94140 38.27364  1.000 81.31514  ? 961  THR B N   1 
ATOM   1343 C  CA  . THR A 1 192 ? 10.90528  -11.52004 37.13841  1.000 80.56245  ? 961  THR B CA  1 
ATOM   1344 C  C   . THR A 1 192 ? 9.57795   -10.85919 37.50746  1.000 80.10727  ? 961  THR B C   1 
ATOM   1345 O  O   . THR A 1 192 ? 8.92111   -10.30049 36.61763  1.000 79.65240  ? 961  THR B O   1 
ATOM   1346 C  CB  . THR A 1 192 ? 10.63913  -12.69511 36.19311  1.000 79.28295  ? 961  THR B CB  1 
ATOM   1347 O  OG1 . THR A 1 192 ? 9.76260   -13.62846 36.82281  1.000 78.46822  ? 961  THR B OG1 1 
ATOM   1348 C  CG2 . THR A 1 192 ? 11.94489  -13.37109 35.82492  1.000 79.71311  ? 961  THR B CG2 1 
ATOM   1349 N  N   . MET A 1 193 ? 9.17057   -10.86543 38.77394  1.000 76.16614  ? 962  MET B N   1 
ATOM   1350 C  CA  . MET A 1 193 ? 7.86042   -10.31520 39.10576  1.000 77.90375  ? 962  MET B CA  1 
ATOM   1351 C  C   . MET A 1 193 ? 7.89547   -8.79420  39.20824  1.000 63.19637  ? 962  MET B C   1 
ATOM   1352 O  O   . MET A 1 193 ? 8.93356   -8.19017  39.49282  1.000 56.65053  ? 962  MET B O   1 
ATOM   1353 C  CB  . MET A 1 193 ? 7.34592   -10.89129 40.42654  1.000 77.77281  ? 962  MET B CB  1 
ATOM   1354 C  CG  . MET A 1 193 ? 7.07399   -12.37394 40.36800  1.000 90.28933  ? 962  MET B CG  1 
ATOM   1355 S  SD  . MET A 1 193 ? 5.50243   -12.78025 39.59002  1.000 102.29204 ? 962  MET B SD  1 
ATOM   1356 C  CE  . MET A 1 193 ? 4.42821   -12.64568 41.01119  1.000 102.74455 ? 962  MET B CE  1 
ATOM   1357 N  N   . CYS A 1 194 ? 6.73705   -8.18577  38.96614  1.000 61.68801  ? 963  CYS B N   1 
ATOM   1358 C  CA  . CYS A 1 194 ? 6.59407   -6.74510  39.13125  1.000 60.73617  ? 963  CYS B CA  1 
ATOM   1359 C  C   . CYS A 1 194 ? 6.96180   -6.36656  40.55782  1.000 59.12927  ? 963  CYS B C   1 
ATOM   1360 O  O   . CYS A 1 194 ? 6.53354   -7.04750  41.49733  1.000 58.66434  ? 963  CYS B O   1 
ATOM   1361 C  CB  . CYS A 1 194 ? 5.16414   -6.28770  38.85511  1.000 58.91392  ? 963  CYS B CB  1 
ATOM   1362 S  SG  . CYS A 1 194 ? 4.91154   -4.54697  39.25355  1.000 51.53736  ? 963  CYS B SG  1 
ATOM   1363 N  N   . PRO A 1 195 ? 7.76169   -5.31626  40.76771  1.000 55.89828  ? 964  PRO B N   1 
ATOM   1364 C  CA  . PRO A 1 195 ? 8.13525   -4.95165  42.13656  1.000 56.36504  ? 964  PRO B CA  1 
ATOM   1365 C  C   . PRO A 1 195 ? 7.07326   -4.14535  42.87104  1.000 56.24525  ? 964  PRO B C   1 
ATOM   1366 O  O   . PRO A 1 195 ? 7.23798   -3.90228  44.07415  1.000 54.90246  ? 964  PRO B O   1 
ATOM   1367 C  CB  . PRO A 1 195 ? 9.40735   -4.11888  41.93463  1.000 53.97808  ? 964  PRO B CB  1 
ATOM   1368 C  CG  . PRO A 1 195 ? 9.17698   -3.44344  40.65345  1.000 51.76003  ? 964  PRO B CG  1 
ATOM   1369 C  CD  . PRO A 1 195 ? 8.40128   -4.42481  39.78423  1.000 57.31913  ? 964  PRO B CD  1 
ATOM   1370 N  N   . VAL A 1 196 ? 6.01311   -3.70318  42.19868  1.000 56.83161  ? 965  VAL B N   1 
ATOM   1371 C  CA  . VAL A 1 196 ? 4.97285   -2.91630  42.85927  1.000 56.38387  ? 965  VAL B CA  1 
ATOM   1372 C  C   . VAL A 1 196 ? 3.87815   -3.81812  43.40625  1.000 59.94475  ? 965  VAL B C   1 
ATOM   1373 O  O   . VAL A 1 196 ? 3.54330   -3.75685  44.59062  1.000 66.73065  ? 965  VAL B O   1 
ATOM   1374 C  CB  . VAL A 1 196 ? 4.40700   -1.84490  41.89736  1.000 57.56147  ? 965  VAL B CB  1 
ATOM   1375 C  CG1 . VAL A 1 196 ? 3.28783   -1.06593  42.55351  1.000 58.43890  ? 965  VAL B CG1 1 
ATOM   1376 C  CG2 . VAL A 1 196 ? 5.49343   -0.89174  41.46369  1.000 56.00677  ? 965  VAL B CG2 1 
ATOM   1377 N  N   . CYS A 1 197 ? 3.30750   -4.67956  42.56307  1.000 59.77507  ? 966  CYS B N   1 
ATOM   1378 C  CA  . CYS A 1 197 ? 2.23540   -5.56447  42.99451  1.000 59.79868  ? 966  CYS B CA  1 
ATOM   1379 C  C   . CYS A 1 197 ? 2.73315   -6.90105  43.52046  1.000 62.03047  ? 966  CYS B C   1 
ATOM   1380 O  O   . CYS A 1 197 ? 2.02934   -7.54144  44.31192  1.000 61.25856  ? 966  CYS B O   1 
ATOM   1381 C  CB  . CYS A 1 197 ? 1.26853   -5.80196  41.83235  1.000 60.31110  ? 966  CYS B CB  1 
ATOM   1382 S  SG  . CYS A 1 197 ? 2.06909   -6.53410  40.38809  1.000 66.96275  ? 966  CYS B SG  1 
ATOM   1383 N  N   . LEU A 1 198 ? 3.93671   -7.31316  43.12892  1.000 64.13747  ? 967  LEU B N   1 
ATOM   1384 C  CA  . LEU A 1 198 ? 4.49442   -8.62658  43.45233  1.000 67.62861  ? 967  LEU B CA  1 
ATOM   1385 C  C   . LEU A 1 198 ? 3.60573   -9.77705  42.95733  1.000 71.03606  ? 967  LEU B C   1 
ATOM   1386 O  O   . LEU A 1 198 ? 3.75013   -10.92001 43.41152  1.000 70.15816  ? 967  LEU B O   1 
ATOM   1387 C  CB  . LEU A 1 198 ? 4.76765   -8.75068  44.95981  1.000 67.46137  ? 967  LEU B CB  1 
ATOM   1388 C  CG  . LEU A 1 198 ? 5.48599   -7.58004  45.64191  1.000 64.12444  ? 967  LEU B CG  1 
ATOM   1389 C  CD1 . LEU A 1 198 ? 4.52030   -6.58299  46.21718  1.000 62.83110  ? 967  LEU B CD1 1 
ATOM   1390 C  CD2 . LEU A 1 198 ? 6.37372   -8.11238  46.74241  1.000 67.17110  ? 967  LEU B CD2 1 
ATOM   1391 N  N   . ASP A 1 199 ? 2.74214   -9.48705  41.97596  1.000 73.14102  ? 968  ASP B N   1 
ATOM   1392 C  CA  . ASP A 1 199 ? 1.63057   -10.32858 41.53584  1.000 74.32346  ? 968  ASP B CA  1 
ATOM   1393 C  C   . ASP A 1 199 ? 1.74215   -10.75020 40.08181  1.000 75.49304  ? 968  ASP B C   1 
ATOM   1394 O  O   . ASP A 1 199 ? 1.68926   -11.94517 39.78632  1.000 77.96055  ? 968  ASP B O   1 
ATOM   1395 C  CB  . ASP A 1 199 ? 0.30591   -9.55360  41.75227  1.000 74.07877  ? 968  ASP B CB  1 
ATOM   1396 C  CG  . ASP A 1 199 ? -0.94394  -10.35994 41.38567  1.000 78.71361  ? 968  ASP B CG  1 
ATOM   1397 O  OD1 . ASP A 1 199 ? -0.82209  -11.55284 41.03426  1.000 72.24517  ? 968  ASP B OD1 1 
ATOM   1398 O  OD2 . ASP A 1 199 ? -2.06139  -9.79696  41.47805  1.000 82.82782  ? 968  ASP B OD2 1 
ATOM   1399 N  N   . ARG A 1 200 ? 1.86602   -9.80772  39.15848  1.000 73.42412  ? 969  ARG B N   1 
ATOM   1400 C  CA  . ARG A 1 200 ? 2.06369   -10.15666 37.76572  1.000 71.98196  ? 969  ARG B CA  1 
ATOM   1401 C  C   . ARG A 1 200 ? 3.53312   -10.03070 37.39569  1.000 71.03088  ? 969  ARG B C   1 
ATOM   1402 O  O   . ARG A 1 200 ? 4.33603   -9.42198  38.10740  1.000 67.90244  ? 969  ARG B O   1 
ATOM   1403 C  CB  . ARG A 1 200 ? 1.18812   -9.28978  36.85876  1.000 68.09905  ? 969  ARG B CB  1 
ATOM   1404 C  CG  . ARG A 1 200 ? -0.29463  -9.45337  37.10747  1.000 69.69146  ? 969  ARG B CG  1 
ATOM   1405 C  CD  . ARG A 1 200 ? -1.09045  -8.26634  36.60148  1.000 69.05169  ? 969  ARG B CD  1 
ATOM   1406 N  NE  . ARG A 1 200 ? -0.78652  -7.05386  37.34675  1.000 67.74084  ? 969  ARG B NE  1 
ATOM   1407 C  CZ  . ARG A 1 200 ? -1.41812  -6.68838  38.45323  1.000 71.44137  ? 969  ARG B CZ  1 
ATOM   1408 N  NH1 . ARG A 1 200 ? -2.41394  -7.40399  38.94501  1.000 73.10051  ? 969  ARG B NH1 1 
ATOM   1409 N  NH2 . ARG A 1 200 ? -1.04084  -5.57805  39.08214  1.000 70.08307  ? 969  ARG B NH2 1 
ATOM   1410 N  N   . LEU A 1 201 ? 3.85429   -10.51986 36.20615  1.000 72.33155  ? 970  LEU B N   1 
ATOM   1411 C  CA  . LEU A 1 201 ? 5.22006   -10.44160 35.73264  1.000 69.14038  ? 970  LEU B CA  1 
ATOM   1412 C  C   . LEU A 1 201 ? 5.42188   -9.10357  35.05927  1.000 63.67739  ? 970  LEU B C   1 
ATOM   1413 O  O   . LEU A 1 201 ? 4.48149   -8.49413  34.54322  1.000 62.01659  ? 970  LEU B O   1 
ATOM   1414 C  CB  . LEU A 1 201 ? 5.52123   -11.56835 34.74806  1.000 71.67363  ? 970  LEU B CB  1 
ATOM   1415 C  CG  . LEU A 1 201 ? 5.40807   -12.96313 35.35314  1.000 76.27934  ? 970  LEU B CG  1 
ATOM   1416 C  CD1 . LEU A 1 201 ? 4.96493   -14.00411 34.32420  1.000 75.97462  ? 970  LEU B CD1 1 
ATOM   1417 C  CD2 . LEU A 1 201 ? 6.73248   -13.33842 35.98310  1.000 79.07537  ? 970  LEU B CD2 1 
ATOM   1418 N  N   . LYS A 1 202 ? 6.67277   -8.66458  35.05254  1.000 62.77256  ? 971  LYS B N   1 
ATOM   1419 C  CA  . LYS A 1 202 ? 7.05213   -7.39154  34.45093  1.000 61.75065  ? 971  LYS B CA  1 
ATOM   1420 C  C   . LYS A 1 202 ? 6.88854   -7.50715  32.93949  1.000 62.17901  ? 971  LYS B C   1 
ATOM   1421 O  O   . LYS A 1 202 ? 7.71836   -8.11069  32.26041  1.000 67.66577  ? 971  LYS B O   1 
ATOM   1422 C  CB  . LYS A 1 202 ? 8.49285   -7.04187  34.81878  1.000 60.56618  ? 971  LYS B CB  1 
ATOM   1423 C  CG  . LYS A 1 202 ? 8.78862   -6.88802  36.31077  1.000 61.85697  ? 971  LYS B CG  1 
ATOM   1424 C  CD  . LYS A 1 202 ? 10.23247  -6.44480  36.53785  1.000 61.83039  ? 971  LYS B CD  1 
ATOM   1425 C  CE  . LYS A 1 202 ? 11.20640  -7.60400  36.37870  1.000 67.60288  ? 971  LYS B CE  1 
ATOM   1426 N  NZ  . LYS A 1 202 ? 12.63199  -7.17551  36.40633  1.000 70.04910  ? 971  LYS B NZ  1 
ATOM   1427 N  N   . ASN A 1 203 ? 5.81289   -6.93632  32.39636  1.000 61.31657  ? 972  ASN B N   1 
ATOM   1428 C  CA  . ASN A 1 203 ? 5.58728   -6.91759  30.95419  1.000 60.48436  ? 972  ASN B CA  1 
ATOM   1429 C  C   . ASN A 1 203 ? 5.63801   -5.50102  30.39405  1.000 60.29910  ? 972  ASN B C   1 
ATOM   1430 O  O   . ASN A 1 203 ? 5.01701   -5.21403  29.36333  1.000 59.54491  ? 972  ASN B O   1 
ATOM   1431 C  CB  . ASN A 1 203 ? 4.26179   -7.59997  30.61339  1.000 61.28548  ? 972  ASN B CB  1 
ATOM   1432 C  CG  . ASN A 1 203 ? 3.08254   -6.88067  31.19697  1.000 59.33253  ? 972  ASN B CG  1 
ATOM   1433 O  OD1 . ASN A 1 203 ? 3.23493   -6.14286  32.16544  1.000 61.18460  ? 972  ASN B OD1 1 
ATOM   1434 N  ND2 . ASN A 1 203 ? 1.89357   -7.12945  30.66091  1.000 57.77321  ? 972  ASN B ND2 1 
ATOM   1435 N  N   . MET A 1 204 ? 6.32034   -4.59703  31.09624  1.000 60.43500  ? 973  MET B N   1 
ATOM   1436 C  CA  . MET A 1 204 ? 6.52028   -3.22712  30.64281  1.000 61.03425  ? 973  MET B CA  1 
ATOM   1437 C  C   . MET A 1 204 ? 7.85462   -2.74780  31.18978  1.000 61.28171  ? 973  MET B C   1 
ATOM   1438 O  O   . MET A 1 204 ? 8.06353   -2.74050  32.40496  1.000 61.15481  ? 973  MET B O   1 
ATOM   1439 C  CB  . MET A 1 204 ? 5.37884   -2.30365  31.11215  1.000 61.17037  ? 973  MET B CB  1 
ATOM   1440 C  CG  . MET A 1 204 ? 5.67159   -0.82337  30.95822  1.000 59.66816  ? 973  MET B CG  1 
ATOM   1441 S  SD  . MET A 1 204 ? 4.34102   0.27317   31.52938  1.000 76.16945  ? 973  MET B SD  1 
ATOM   1442 C  CE  . MET A 1 204 ? 3.05798   -0.12996  30.33677  1.000 71.45484  ? 973  MET B CE  1 
ATOM   1443 N  N   . ILE A 1 205 ? 8.72353   -2.29220  30.30190  1.000 59.41538  ? 974  ILE B N   1 
ATOM   1444 C  CA  . ILE A 1 205 ? 10.08873  -1.95128  30.66187  1.000 59.53236  ? 974  ILE B CA  1 
ATOM   1445 C  C   . ILE A 1 205 ? 10.32912  -0.49270  30.31320  1.000 60.77190  ? 974  ILE B C   1 
ATOM   1446 O  O   . ILE A 1 205 ? 9.81540   0.01322   29.30515  1.000 62.68810  ? 974  ILE B O   1 
ATOM   1447 C  CB  . ILE A 1 205 ? 11.10222  -2.87035  29.95403  1.000 63.24528  ? 974  ILE B CB  1 
ATOM   1448 C  CG1 . ILE A 1 205 ? 10.84461  -4.32287  30.36168  1.000 61.43012  ? 974  ILE B CG1 1 
ATOM   1449 C  CG2 . ILE A 1 205 ? 12.53115  -2.46077  30.28445  1.000 63.49243  ? 974  ILE B CG2 1 
ATOM   1450 C  CD1 . ILE A 1 205 ? 11.07970  -4.60164  31.81298  1.000 59.52807  ? 974  ILE B CD1 1 
ATOM   1451 N  N   . PHE A 1 206 ? 11.05930  0.19117   31.18923  1.000 60.52692  ? 975  PHE B N   1 
ATOM   1452 C  CA  . PHE A 1 206 ? 11.49505  1.55595   30.97056  1.000 63.56814  ? 975  PHE B CA  1 
ATOM   1453 C  C   . PHE A 1 206 ? 12.94459  1.57228   30.50487  1.000 64.25189  ? 975  PHE B C   1 
ATOM   1454 O  O   . PHE A 1 206 ? 13.69335  0.60817   30.67959  1.000 62.50694  ? 975  PHE B O   1 
ATOM   1455 C  CB  . PHE A 1 206 ? 11.32658  2.38590   32.24657  1.000 61.64089  ? 975  PHE B CB  1 
ATOM   1456 C  CG  . PHE A 1 206 ? 10.09555  2.03284   33.04146  1.000 61.35163  ? 975  PHE B CG  1 
ATOM   1457 C  CD1 . PHE A 1 206 ? 8.84516   2.03188   32.44431  1.000 62.41824  ? 975  PHE B CD1 1 
ATOM   1458 C  CD2 . PHE A 1 206 ? 10.18587  1.72253   34.38657  1.000 58.20396  ? 975  PHE B CD2 1 
ATOM   1459 C  CE1 . PHE A 1 206 ? 7.71343   1.70600   33.15937  1.000 61.87102  ? 975  PHE B CE1 1 
ATOM   1460 C  CE2 . PHE A 1 206 ? 9.05065   1.40291   35.11905  1.000 57.50153  ? 975  PHE B CE2 1 
ATOM   1461 C  CZ  . PHE A 1 206 ? 7.81280   1.39608   34.50559  1.000 58.98692  ? 975  PHE B CZ  1 
ATOM   1462 N  N   . LEU A 1 207 ? 13.33491  2.70881   29.93115  1.000 65.22461  ? 976  LEU B N   1 
ATOM   1463 C  CA  . LEU A 1 207 ? 14.65540  2.84819   29.33836  1.000 66.81496  ? 976  LEU B CA  1 
ATOM   1464 C  C   . LEU A 1 207 ? 15.76808  2.81388   30.37874  1.000 65.49514  ? 976  LEU B C   1 
ATOM   1465 O  O   . LEU A 1 207 ? 16.93081  2.59416   30.01613  1.000 64.86049  ? 976  LEU B O   1 
ATOM   1466 C  CB  . LEU A 1 207 ? 14.71249  4.15155   28.53831  1.000 68.77587  ? 976  LEU B CB  1 
ATOM   1467 C  CG  . LEU A 1 207 ? 14.00720  4.08594   27.18390  1.000 68.60471  ? 976  LEU B CG  1 
ATOM   1468 C  CD1 . LEU A 1 207 ? 14.09932  5.38492   26.44260  1.000 70.40120  ? 976  LEU B CD1 1 
ATOM   1469 C  CD2 . LEU A 1 207 ? 14.61363  2.98676   26.37082  1.000 66.49027  ? 976  LEU B CD2 1 
ATOM   1470 N  N   . CYS A 1 208 ? 15.44411  3.05373   31.65260  1.000 66.25132  ? 977  CYS B N   1 
ATOM   1471 C  CA  . CYS A 1 208 ? 16.43424  2.99510   32.72316  1.000 67.90565  ? 977  CYS B CA  1 
ATOM   1472 C  C   . CYS A 1 208 ? 16.85635  1.57182   33.04624  1.000 65.27584  ? 977  CYS B C   1 
ATOM   1473 O  O   . CYS A 1 208 ? 17.76804  1.38461   33.86063  1.000 65.14256  ? 977  CYS B O   1 
ATOM   1474 C  CB  . CYS A 1 208 ? 15.90370  3.63113   34.00818  1.000 64.98152  ? 977  CYS B CB  1 
ATOM   1475 S  SG  . CYS A 1 208 ? 14.47677  2.77651   34.68399  1.000 63.70400  ? 977  CYS B SG  1 
ATOM   1476 N  N   . GLY A 1 209 ? 16.19241  0.57281   32.47085  1.000 61.67610  ? 978  GLY B N   1 
ATOM   1477 C  CA  . GLY A 1 209 ? 16.52946  -0.80910  32.68732  1.000 64.75943  ? 978  GLY B CA  1 
ATOM   1478 C  C   . GLY A 1 209 ? 15.60112  -1.55477  33.62297  1.000 67.44501  ? 978  GLY B C   1 
ATOM   1479 O  O   . GLY A 1 209 ? 15.66054  -2.78977  33.67715  1.000 71.54933  ? 978  GLY B O   1 
ATOM   1480 N  N   . HIS A 1 210 ? 14.76716  -0.84938  34.37190  1.000 63.05179  ? 979  HIS B N   1 
ATOM   1481 C  CA  . HIS A 1 210 ? 13.82420  -1.49552  35.26808  1.000 61.26642  ? 979  HIS B CA  1 
ATOM   1482 C  C   . HIS A 1 210 ? 12.46256  -1.60827  34.59479  1.000 59.04411  ? 979  HIS B C   1 
ATOM   1483 O  O   . HIS A 1 210 ? 12.21901  -1.05140  33.52334  1.000 59.74519  ? 979  HIS B O   1 
ATOM   1484 C  CB  . HIS A 1 210 ? 13.71402  -0.74077  36.60168  1.000 61.24191  ? 979  HIS B CB  1 
ATOM   1485 C  CG  . HIS A 1 210 ? 15.02423  -0.54608  37.30830  1.000 60.12319  ? 979  HIS B CG  1 
ATOM   1486 N  ND1 . HIS A 1 210 ? 15.57522  0.70162   37.52383  1.000 58.22815  ? 979  HIS B ND1 1 
ATOM   1487 C  CD2 . HIS A 1 210 ? 15.90879  -1.43963  37.81092  1.000 59.23391  ? 979  HIS B CD2 1 
ATOM   1488 C  CE1 . HIS A 1 210 ? 16.73197  0.56752   38.14755  1.000 57.90080  ? 979  HIS B CE1 1 
ATOM   1489 N  NE2 . HIS A 1 210 ? 16.95646  -0.72157  38.33483  1.000 54.47226  ? 979  HIS B NE2 1 
ATOM   1490 N  N   . GLY A 1 211 ? 11.58674  -2.38964  35.22321  1.000 54.94547  ? 980  GLY B N   1 
ATOM   1491 C  CA  . GLY A 1 211 ? 10.27800  -2.66051  34.67235  1.000 56.91582  ? 980  GLY B CA  1 
ATOM   1492 C  C   . GLY A 1 211 ? 9.27617   -2.99645  35.75073  1.000 56.96816  ? 980  GLY B C   1 
ATOM   1493 O  O   . GLY A 1 211 ? 9.62048   -3.24007  36.90905  1.000 57.76573  ? 980  GLY B O   1 
ATOM   1494 N  N   . THR A 1 212 ? 8.01254   -2.99683  35.33902  1.000 57.18221  ? 981  THR B N   1 
ATOM   1495 C  CA  . THR A 1 212 ? 6.87593   -3.35316  36.17324  1.000 56.81899  ? 981  THR B CA  1 
ATOM   1496 C  C   . THR A 1 212 ? 5.91618   -4.18289  35.34225  1.000 59.60186  ? 981  THR B C   1 
ATOM   1497 O  O   . THR A 1 212 ? 6.17183   -4.48311  34.17395  1.000 60.61472  ? 981  THR B O   1 
ATOM   1498 C  CB  . THR A 1 212 ? 6.11825   -2.12289  36.64432  1.000 61.97899  ? 981  THR B CB  1 
ATOM   1499 O  OG1 . THR A 1 212 ? 5.48441   -1.54626  35.49604  1.000 61.81431  ? 981  THR B OG1 1 
ATOM   1500 C  CG2 . THR A 1 212 ? 7.06032   -1.10513  37.26885  1.000 59.81136  ? 981  THR B CG2 1 
ATOM   1501 N  N   . CYS A 1 213 ? 4.77585   -4.51365  35.92638  1.000 58.40262  ? 982  CYS B N   1 
ATOM   1502 C  CA  . CYS A 1 213 ? 3.67835   -4.93870  35.07890  1.000 61.94664  ? 982  CYS B CA  1 
ATOM   1503 C  C   . CYS A 1 213 ? 3.02153   -3.71811  34.42843  1.000 63.16703  ? 982  CYS B C   1 
ATOM   1504 O  O   . CYS A 1 213 ? 3.24496   -2.57450  34.83282  1.000 63.16382  ? 982  CYS B O   1 
ATOM   1505 C  CB  . CYS A 1 213 ? 2.67045   -5.75276  35.88164  1.000 62.08986  ? 982  CYS B CB  1 
ATOM   1506 S  SG  . CYS A 1 213 ? 1.56897   -4.79866  36.91020  1.000 68.64266  ? 982  CYS B SG  1 
ATOM   1507 N  N   . GLN A 1 214 ? 2.23287   -3.96984  33.37924  1.000 62.10589  ? 983  GLN B N   1 
ATOM   1508 C  CA  . GLN A 1 214 ? 1.57178   -2.87190  32.67093  1.000 65.59469  ? 983  GLN B CA  1 
ATOM   1509 C  C   . GLN A 1 214 ? 0.60635   -2.13907  33.58311  1.000 66.93145  ? 983  GLN B C   1 
ATOM   1510 O  O   . GLN A 1 214 ? 0.48660   -0.90684  33.53098  1.000 68.76102  ? 983  GLN B O   1 
ATOM   1511 C  CB  . GLN A 1 214 ? 0.83407   -3.40081  31.43680  1.000 68.37051  ? 983  GLN B CB  1 
ATOM   1512 C  CG  . GLN A 1 214 ? 0.04812   -2.33092  30.67543  1.000 71.89162  ? 983  GLN B CG  1 
ATOM   1513 C  CD  . GLN A 1 214 ? -0.51642  -2.81278  29.34004  1.000 72.28921  ? 983  GLN B CD  1 
ATOM   1514 O  OE1 . GLN A 1 214 ? -0.75894  -4.00313  29.12775  1.000 67.83631  ? 983  GLN B OE1 1 
ATOM   1515 N  NE2 . GLN A 1 214 ? -0.72565  -1.87164  28.43104  1.000 73.20511  ? 983  GLN B NE2 1 
ATOM   1516 N  N   . LEU A 1 215 ? -0.08105  -2.89715  34.43297  1.000 65.91845  ? 984  LEU B N   1 
ATOM   1517 C  CA  . LEU A 1 215 ? -1.11900  -2.35875  35.29778  1.000 66.35925  ? 984  LEU B CA  1 
ATOM   1518 C  C   . LEU A 1 215 ? -0.55416  -1.34302  36.28643  1.000 66.12966  ? 984  LEU B C   1 
ATOM   1519 O  O   . LEU A 1 215 ? -1.08467  -0.23660  36.43241  1.000 66.70401  ? 984  LEU B O   1 
ATOM   1520 C  CB  . LEU A 1 215 ? -1.77943  -3.52664  36.02487  1.000 66.78485  ? 984  LEU B CB  1 
ATOM   1521 C  CG  . LEU A 1 215 ? -3.29739  -3.49924  36.10631  1.000 70.17536  ? 984  LEU B CG  1 
ATOM   1522 C  CD1 . LEU A 1 215 ? -3.87657  -3.18827  34.74027  1.000 66.69803  ? 984  LEU B CD1 1 
ATOM   1523 C  CD2 . LEU A 1 215 ? -3.81845  -4.82716  36.65601  1.000 74.57874  ? 984  LEU B CD2 1 
ATOM   1524 N  N   . CYS A 1 216 ? 0.52352   -1.71383  36.98254  1.000 66.23109  ? 985  CYS B N   1 
ATOM   1525 C  CA  . CYS A 1 216 ? 1.16451   -0.80815  37.92853  1.000 65.56757  ? 985  CYS B CA  1 
ATOM   1526 C  C   . CYS A 1 216 ? 1.93345   0.28700   37.19266  1.000 67.67589  ? 985  CYS B C   1 
ATOM   1527 O  O   . CYS A 1 216 ? 1.93158   1.44982   37.61340  1.000 69.62334  ? 985  CYS B O   1 
ATOM   1528 C  CB  . CYS A 1 216 ? 2.10104   -1.60152  38.84713  1.000 63.67840  ? 985  CYS B CB  1 
ATOM   1529 S  SG  . CYS A 1 216 ? 1.32285   -2.95562  39.82714  1.000 61.82164  ? 985  CYS B SG  1 
ATOM   1530 N  N   . GLY A 1 217 ? 2.59090   -0.06765  36.08238  1.000 67.23888  ? 986  GLY B N   1 
ATOM   1531 C  CA  . GLY A 1 217 ? 3.43143   0.88333   35.37371  1.000 66.18495  ? 986  GLY B CA  1 
ATOM   1532 C  C   . GLY A 1 217 ? 2.66171   2.02905   34.75673  1.000 68.99791  ? 986  GLY B C   1 
ATOM   1533 O  O   . GLY A 1 217 ? 3.16927   3.14982   34.68607  1.000 67.93667  ? 986  GLY B O   1 
ATOM   1534 N  N   . ASP A 1 218 ? 1.44183   1.76985   34.28073  1.000 69.90212  ? 987  ASP B N   1 
ATOM   1535 C  CA  . ASP A 1 218 ? 0.63432   2.86137   33.74759  1.000 70.69254  ? 987  ASP B CA  1 
ATOM   1536 C  C   . ASP A 1 218 ? 0.19655   3.84357   34.83382  1.000 71.05161  ? 987  ASP B C   1 
ATOM   1537 O  O   . ASP A 1 218 ? -0.28221  4.93470   34.50624  1.000 68.91359  ? 987  ASP B O   1 
ATOM   1538 C  CB  . ASP A 1 218 ? -0.58940  2.31064   33.00740  1.000 72.30100  ? 987  ASP B CB  1 
ATOM   1539 C  CG  . ASP A 1 218 ? -0.24770  1.76602   31.63196  1.000 72.99160  ? 987  ASP B CG  1 
ATOM   1540 O  OD1 . ASP A 1 218 ? 0.75948   2.20906   31.04058  1.000 72.52070  ? 987  ASP B OD1 1 
ATOM   1541 O  OD2 . ASP A 1 218 ? -0.99323  0.89310   31.14124  1.000 76.05322  ? 987  ASP B OD2 1 
ATOM   1542 N  N   . ARG A 1 219 ? 0.33386   3.48910   36.11119  1.000 71.44986  ? 988  ARG B N   1 
ATOM   1543 C  CA  . ARG A 1 219 ? -0.06322  4.37237   37.19925  1.000 70.35966  ? 988  ARG B CA  1 
ATOM   1544 C  C   . ARG A 1 219 ? 1.10861   5.16535   37.77644  1.000 71.72816  ? 988  ARG B C   1 
ATOM   1545 O  O   . ARG A 1 219 ? 0.97382   5.73686   38.85876  1.000 75.01462  ? 988  ARG B O   1 
ATOM   1546 C  CB  . ARG A 1 219 ? -0.74573  3.56588   38.31164  1.000 72.99341  ? 988  ARG B CB  1 
ATOM   1547 C  CG  . ARG A 1 219 ? -2.14214  3.04923   37.94789  1.000 76.84795  ? 988  ARG B CG  1 
ATOM   1548 C  CD  . ARG A 1 219 ? -3.24076  3.63240   38.81450  1.000 80.71565  ? 988  ARG B CD  1 
ATOM   1549 N  NE  . ARG A 1 219 ? -3.49647  2.86270   40.02626  1.000 84.91368  ? 988  ARG B NE  1 
ATOM   1550 C  CZ  . ARG A 1 219 ? -4.29135  1.80085   40.08868  1.000 91.47513  ? 988  ARG B CZ  1 
ATOM   1551 N  NH1 . ARG A 1 219 ? -4.92101  1.34305   39.01711  1.000 95.29928  ? 988  ARG B NH1 1 
ATOM   1552 N  NH2 . ARG A 1 219 ? -4.48859  1.20500   41.26239  1.000 84.06100  ? 988  ARG B NH2 1 
ATOM   1553 N  N   . MET A 1 220 ? 2.26136   5.19353   37.10366  1.000 72.82885  ? 989  MET B N   1 
ATOM   1554 C  CA  . MET A 1 220 ? 3.44329   5.87810   37.61845  1.000 73.34523  ? 989  MET B CA  1 
ATOM   1555 C  C   . MET A 1 220 ? 4.07159   6.74729   36.53928  1.000 71.25161  ? 989  MET B C   1 
ATOM   1556 O  O   . MET A 1 220 ? 3.93489   6.47494   35.34599  1.000 69.55025  ? 989  MET B O   1 
ATOM   1557 C  CB  . MET A 1 220 ? 4.51239   4.90454   38.14051  1.000 75.20211  ? 989  MET B CB  1 
ATOM   1558 C  CG  . MET A 1 220 ? 4.00471   3.73388   38.96532  1.000 71.33393  ? 989  MET B CG  1 
ATOM   1559 S  SD  . MET A 1 220 ? 5.40295   2.73817   39.53034  1.000 71.18051  ? 989  MET B SD  1 
ATOM   1560 C  CE  . MET A 1 220 ? 6.31982   4.01392   40.39768  1.000 67.28808  ? 989  MET B CE  1 
ATOM   1561 N  N   . SER A 1 221 ? 4.76275   7.80381   36.97310  1.000 70.86957  ? 990  SER B N   1 
ATOM   1562 C  CA  . SER A 1 221 ? 5.54068   8.64253   36.06957  1.000 69.09950  ? 990  SER B CA  1 
ATOM   1563 C  C   . SER A 1 221 ? 7.04151   8.48298   36.24310  1.000 68.12533  ? 990  SER B C   1 
ATOM   1564 O  O   . SER A 1 221 ? 7.80533   8.92946   35.37922  1.000 67.00987  ? 990  SER B O   1 
ATOM   1565 C  CB  . SER A 1 221 ? 5.16442   10.12307  36.25725  1.000 70.81599  ? 990  SER B CB  1 
ATOM   1566 O  OG  . SER A 1 221 ? 5.38728   10.57795  37.58660  1.000 69.94148  ? 990  SER B OG  1 
ATOM   1567 N  N   . GLU A 1 222 ? 7.48407   7.87535   37.32735  1.000 69.85561  ? 991  GLU B N   1 
ATOM   1568 C  CA  . GLU A 1 222 ? 8.89794   7.65787   37.55675  1.000 69.46941  ? 991  GLU B CA  1 
ATOM   1569 C  C   . GLU A 1 222 ? 9.11694   6.20906   37.95942  1.000 68.03760  ? 991  GLU B C   1 
ATOM   1570 O  O   . GLU A 1 222 ? 8.22692   5.55974   38.51412  1.000 66.82084  ? 991  GLU B O   1 
ATOM   1571 C  CB  . GLU A 1 222 ? 9.41702   8.61415   38.60475  1.000 71.86875  ? 991  GLU B CB  1 
ATOM   1572 C  CG  . GLU A 1 222 ? 8.39985   8.86871   39.67842  1.000 76.84848  ? 991  GLU B CG  1 
ATOM   1573 C  CD  . GLU A 1 222 ? 8.77966   10.03491  40.54285  1.000 84.57359  ? 991  GLU B CD  1 
ATOM   1574 O  OE1 . GLU A 1 222 ? 9.98218   10.37408  40.56434  1.000 86.51094  ? 991  GLU B OE1 1 
ATOM   1575 O  OE2 . GLU A 1 222 ? 7.87963   10.61378  41.18883  1.000 89.83520  ? 991  GLU B OE2 1 
ATOM   1576 N  N   . CYS A 1 223 ? 10.29498  5.70165   37.64141  1.000 66.12603  ? 992  CYS B N   1 
ATOM   1577 C  CA  . CYS A 1 223 ? 10.60428  4.31246   37.93332  1.000 63.49012  ? 992  CYS B CA  1 
ATOM   1578 C  C   . CYS A 1 223 ? 10.57980  4.08248   39.44347  1.000 61.49826  ? 992  CYS B C   1 
ATOM   1579 O  O   . CYS A 1 223 ? 11.14460  4.88444   40.19677  1.000 61.96399  ? 992  CYS B O   1 
ATOM   1580 C  CB  . CYS A 1 223 ? 11.96498  3.96591   37.33601  1.000 63.69746  ? 992  CYS B CB  1 
ATOM   1581 S  SG  . CYS A 1 223 ? 12.63765  2.38590   37.81800  1.000 61.28403  ? 992  CYS B SG  1 
ATOM   1582 N  N   . PRO A 1 224 ? 9.93905   3.01536   39.92686  1.000 60.95068  ? 993  PRO B N   1 
ATOM   1583 C  CA  . PRO A 1 224 ? 9.84425   2.80799   41.37553  1.000 60.57461  ? 993  PRO B CA  1 
ATOM   1584 C  C   . PRO A 1 224 ? 11.12832  2.34297   42.03903  1.000 58.83355  ? 993  PRO B C   1 
ATOM   1585 O  O   . PRO A 1 224 ? 11.17278  2.28870   43.27234  1.000 54.96462  ? 993  PRO B O   1 
ATOM   1586 C  CB  . PRO A 1 224 ? 8.75064   1.74052   41.49290  1.000 58.99333  ? 993  PRO B CB  1 
ATOM   1587 C  CG  . PRO A 1 224 ? 8.77133   1.02756   40.17958  1.000 59.54942  ? 993  PRO B CG  1 
ATOM   1588 C  CD  . PRO A 1 224 ? 9.11981   2.05391   39.16760  1.000 60.40000  ? 993  PRO B CD  1 
ATOM   1589 N  N   . ILE A 1 225 ? 12.18546  2.07137   41.28041  1.000 60.26944  ? 994  ILE B N   1 
ATOM   1590 C  CA  . ILE A 1 225 ? 13.42894  1.52267   41.81632  1.000 59.86156  ? 994  ILE B CA  1 
ATOM   1591 C  C   . ILE A 1 225 ? 14.55333  2.55028   41.79429  1.000 62.26123  ? 994  ILE B C   1 
ATOM   1592 O  O   . ILE A 1 225 ? 15.28359  2.69796   42.77340  1.000 65.51574  ? 994  ILE B O   1 
ATOM   1593 C  CB  . ILE A 1 225 ? 13.84139  0.22350   41.08353  1.000 60.90767  ? 994  ILE B CB  1 
ATOM   1594 C  CG1 . ILE A 1 225 ? 12.86532  -0.91341  41.40539  1.000 60.94416  ? 994  ILE B CG1 1 
ATOM   1595 C  CG2 . ILE A 1 225 ? 15.29570  -0.15636  41.37507  1.000 58.92092  ? 994  ILE B CG2 1 
ATOM   1596 C  CD1 . ILE A 1 225 ? 11.77752  -1.06000  40.40518  1.000 67.59703  ? 994  ILE B CD1 1 
ATOM   1597 N  N   . CYS A 1 226 ? 14.71351  3.26934   40.68981  1.000 61.17297  ? 995  CYS B N   1 
ATOM   1598 C  CA  . CYS A 1 226 ? 15.75583  4.27857   40.61693  1.000 61.58942  ? 995  CYS B CA  1 
ATOM   1599 C  C   . CYS A 1 226 ? 15.20230  5.68618   40.56654  1.000 62.04219  ? 995  CYS B C   1 
ATOM   1600 O  O   . CYS A 1 226 ? 15.98332  6.63851   40.63963  1.000 62.51658  ? 995  CYS B O   1 
ATOM   1601 C  CB  . CYS A 1 226 ? 16.66160  4.04550   39.39972  1.000 62.76888  ? 995  CYS B CB  1 
ATOM   1602 S  SG  . CYS A 1 226 ? 15.84935  4.39944   37.83529  1.000 65.92627  ? 995  CYS B SG  1 
ATOM   1603 N  N   . ARG A 1 227 ? 13.88651  5.83316   40.43210  1.000 63.35046  ? 996  ARG B N   1 
ATOM   1604 C  CA  . ARG A 1 227 ? 13.14798  7.08015   40.55250  1.000 67.14396  ? 996  ARG B CA  1 
ATOM   1605 C  C   . ARG A 1 227 ? 13.34920  7.99485   39.34070  1.000 67.79365  ? 996  ARG B C   1 
ATOM   1606 O  O   . ARG A 1 227 ? 12.71287  9.05304   39.26536  1.000 70.14922  ? 996  ARG B O   1 
ATOM   1607 C  CB  . ARG A 1 227 ? 13.50879  7.79936   41.86451  1.000 68.54881  ? 996  ARG B CB  1 
ATOM   1608 C  CG  . ARG A 1 227 ? 12.59425  8.90841   42.30705  1.000 67.59484  ? 996  ARG B CG  1 
ATOM   1609 C  CD  . ARG A 1 227 ? 12.94479  9.33142   43.73178  1.000 73.14477  ? 996  ARG B CD  1 
ATOM   1610 N  NE  . ARG A 1 227 ? 12.46885  8.38901   44.73877  1.000 79.24967  ? 996  ARG B NE  1 
ATOM   1611 C  CZ  . ARG A 1 227 ? 11.20082  8.27915   45.11585  1.000 69.96094  ? 996  ARG B CZ  1 
ATOM   1612 N  NH1 . ARG A 1 227 ? 10.25432  9.03998   44.58804  1.000 77.34483  ? 996  ARG B NH1 1 
ATOM   1613 N  NH2 . ARG A 1 227 ? 10.87565  7.39006   46.04907  1.000 70.77297  ? 996  ARG B NH2 1 
ATOM   1614 N  N   . LYS A 1 228 ? 14.15340  7.59525   38.36211  1.000 67.11070  ? 997  LYS B N   1 
ATOM   1615 C  CA  . LYS A 1 228 ? 14.27616  8.36437   37.13040  1.000 67.47049  ? 997  LYS B CA  1 
ATOM   1616 C  C   . LYS A 1 228 ? 12.92621  8.42843   36.42143  1.000 67.36682  ? 997  LYS B C   1 
ATOM   1617 O  O   . LYS A 1 228 ? 12.10443  7.51683   36.52846  1.000 70.36859  ? 997  LYS B O   1 
ATOM   1618 C  CB  . LYS A 1 228 ? 15.33967  7.72645   36.23355  1.000 67.55040  ? 997  LYS B CB  1 
ATOM   1619 C  CG  . LYS A 1 228 ? 16.72660  7.80527   36.84110  1.000 67.42673  ? 997  LYS B CG  1 
ATOM   1620 C  CD  . LYS A 1 228 ? 17.70140  6.81620   36.23659  1.000 68.90148  ? 997  LYS B CD  1 
ATOM   1621 C  CE  . LYS A 1 228 ? 18.36541  7.31519   34.98232  1.000 72.74279  ? 997  LYS B CE  1 
ATOM   1622 N  NZ  . LYS A 1 228 ? 19.28849  6.26156   34.43658  1.000 75.35553  ? 997  LYS B NZ  1 
ATOM   1623 N  N   . ALA A 1 229 ? 12.67387  9.54154   35.74027  1.000 67.07403  ? 998  ALA B N   1 
ATOM   1624 C  CA  . ALA A 1 229 ? 11.41525  9.70591   35.02395  1.000 67.31301  ? 998  ALA B CA  1 
ATOM   1625 C  C   . ALA A 1 229 ? 11.28048  8.68400   33.89682  1.000 68.22189  ? 998  ALA B C   1 
ATOM   1626 O  O   . ALA A 1 229 ? 12.25929  8.33608   33.22936  1.000 67.40423  ? 998  ALA B O   1 
ATOM   1627 C  CB  . ALA A 1 229 ? 11.31205  11.12001  34.46267  1.000 65.04373  ? 998  ALA B CB  1 
ATOM   1628 N  N   . ILE A 1 230 ? 10.05638  8.19379   33.69968  1.000 67.88274  ? 999  ILE B N   1 
ATOM   1629 C  CA  . ILE A 1 230 ? 9.74410   7.19065   32.67879  1.000 70.15377  ? 999  ILE B CA  1 
ATOM   1630 C  C   . ILE A 1 230 ? 9.72009   7.88922   31.32079  1.000 72.64655  ? 999  ILE B C   1 
ATOM   1631 O  O   . ILE A 1 230 ? 8.74329   8.55803   30.97758  1.000 74.63226  ? 999  ILE B O   1 
ATOM   1632 C  CB  . ILE A 1 230 ? 8.41507   6.48622   32.95845  1.000 68.00641  ? 999  ILE B CB  1 
ATOM   1633 C  CG1 . ILE A 1 230 ? 8.49660   5.67643   34.25271  1.000 66.43214  ? 999  ILE B CG1 1 
ATOM   1634 C  CG2 . ILE A 1 230 ? 8.02651   5.59976   31.77318  1.000 67.31882  ? 999  ILE B CG2 1 
ATOM   1635 C  CD1 . ILE A 1 230 ? 7.19734   4.98460   34.63591  1.000 67.91383  ? 999  ILE B CD1 1 
ATOM   1636 N  N   . GLU A 1 231 ? 10.78698  7.73465   30.53432  1.000 72.18960  ? 1000 GLU B N   1 
ATOM   1637 C  CA  . GLU A 1 231 ? 10.79913  8.34737   29.20767  1.000 76.20311  ? 1000 GLU B CA  1 
ATOM   1638 C  C   . GLU A 1 231 ? 9.88917   7.60349   28.24003  1.000 76.11612  ? 1000 GLU B C   1 
ATOM   1639 O  O   . GLU A 1 231 ? 9.22373   8.22308   27.39900  1.000 77.74645  ? 1000 GLU B O   1 
ATOM   1640 C  CB  . GLU A 1 231 ? 12.21707  8.39591   28.64150  1.000 79.29593  ? 1000 GLU B CB  1 
ATOM   1641 C  CG  . GLU A 1 231 ? 13.19529  9.29111   29.37588  1.000 84.40410  ? 1000 GLU B CG  1 
ATOM   1642 C  CD  . GLU A 1 231 ? 14.55582  9.29165   28.70061  1.000 92.50562  ? 1000 GLU B CD  1 
ATOM   1643 O  OE1 . GLU A 1 231 ? 14.71372  8.56196   27.70089  1.000 84.93329  ? 1000 GLU B OE1 1 
ATOM   1644 O  OE2 . GLU A 1 231 ? 15.45674  10.03607  29.14404  1.000 101.45815 ? 1000 GLU B OE2 1 
ATOM   1645 N  N   . ARG A 1 232 ? 9.84513   6.27795   28.35252  1.000 72.07369  ? 1001 ARG B N   1 
ATOM   1646 C  CA  . ARG A 1 232 ? 9.22154   5.42452   27.35450  1.000 69.95927  ? 1001 ARG B CA  1 
ATOM   1647 C  C   . ARG A 1 232 ? 8.86264   4.09075   28.00059  1.000 64.91349  ? 1001 ARG B C   1 
ATOM   1648 O  O   . ARG A 1 232 ? 9.59552   3.59312   28.86047  1.000 63.34015  ? 1001 ARG B O   1 
ATOM   1649 C  CB  . ARG A 1 232 ? 10.17774  5.22909   26.17417  1.000 71.63751  ? 1001 ARG B CB  1 
ATOM   1650 C  CG  . ARG A 1 232 ? 9.64809   4.38655   25.06053  1.000 71.45279  ? 1001 ARG B CG  1 
ATOM   1651 C  CD  . ARG A 1 232 ? 10.75893  4.08513   24.10600  1.000 73.02320  ? 1001 ARG B CD  1 
ATOM   1652 N  NE  . ARG A 1 232 ? 10.27520  3.34478   22.95270  1.000 76.66637  ? 1001 ARG B NE  1 
ATOM   1653 C  CZ  . ARG A 1 232 ? 10.88203  3.33539   21.77640  1.000 78.98682  ? 1001 ARG B CZ  1 
ATOM   1654 N  NH1 . ARG A 1 232 ? 11.98810  4.03099   21.56597  1.000 84.52280  ? 1001 ARG B NH1 1 
ATOM   1655 N  NH2 . ARG A 1 232 ? 10.36655  2.61334   20.78672  1.000 78.57921  ? 1001 ARG B NH2 1 
ATOM   1656 N  N   . ARG A 1 233 ? 7.71990   3.53635   27.60285  1.000 64.58347  ? 1002 ARG B N   1 
ATOM   1657 C  CA  . ARG A 1 233 ? 7.21140   2.27962   28.14435  1.000 64.91024  ? 1002 ARG B CA  1 
ATOM   1658 C  C   . ARG A 1 233 ? 7.13347   1.27671   27.00053  1.000 63.49807  ? 1002 ARG B C   1 
ATOM   1659 O  O   . ARG A 1 233 ? 6.32622   1.45233   26.08023  1.000 64.91479  ? 1002 ARG B O   1 
ATOM   1660 C  CB  . ARG A 1 233 ? 5.83662   2.51412   28.76655  1.000 64.18966  ? 1002 ARG B CB  1 
ATOM   1661 C  CG  . ARG A 1 233 ? 5.88678   3.60804   29.80762  1.000 67.41275  ? 1002 ARG B CG  1 
ATOM   1662 C  CD  . ARG A 1 233 ? 4.57991   4.36632   29.93448  1.000 69.92853  ? 1002 ARG B CD  1 
ATOM   1663 N  NE  . ARG A 1 233 ? 4.76992   5.53222   30.78741  1.000 70.04332  ? 1002 ARG B NE  1 
ATOM   1664 C  CZ  . ARG A 1 233 ? 4.42642   5.59114   32.06332  1.000 66.63042  ? 1002 ARG B CZ  1 
ATOM   1665 N  NH1 . ARG A 1 233 ? 3.82466   4.57889   32.65985  1.000 70.02242  ? 1002 ARG B NH1 1 
ATOM   1666 N  NH2 . ARG A 1 233 ? 4.71376   6.68452   32.76190  1.000 65.38091  ? 1002 ARG B NH2 1 
ATOM   1667 N  N   . ILE A 1 234 ? 7.95771   0.23061   27.03579  1.000 61.41480  ? 1003 ILE B N   1 
ATOM   1668 C  CA  . ILE A 1 234 ? 7.94623   -0.76893  25.97443  1.000 61.26841  ? 1003 ILE B CA  1 
ATOM   1669 C  C   . ILE A 1 234 ? 7.33788   -2.03879  26.53840  1.000 60.12222  ? 1003 ILE B C   1 
ATOM   1670 O  O   . ILE A 1 234 ? 7.78191   -2.55424  27.57236  1.000 61.11093  ? 1003 ILE B O   1 
ATOM   1671 C  CB  . ILE A 1 234 ? 9.33680   -1.00455  25.35898  1.000 63.63455  ? 1003 ILE B CB  1 
ATOM   1672 C  CG1 . ILE A 1 234 ? 10.37835  -1.38809  26.39187  1.000 62.12838  ? 1003 ILE B CG1 1 
ATOM   1673 C  CG2 . ILE A 1 234 ? 9.81876   0.25403   24.63343  1.000 66.45328  ? 1003 ILE B CG2 1 
ATOM   1674 C  CD1 . ILE A 1 234 ? 11.73706  -1.40502  25.78547  1.000 60.73515  ? 1003 ILE B CD1 1 
ATOM   1675 N  N   . LEU A 1 235 ? 6.27534   -2.49367  25.89231  1.000 57.98903  ? 1004 LEU B N   1 
ATOM   1676 C  CA  . LEU A 1 235 ? 5.53818   -3.65458  26.34898  1.000 59.23749  ? 1004 LEU B CA  1 
ATOM   1677 C  C   . LEU A 1 235 ? 6.17459   -4.93004  25.82979  1.000 61.54298  ? 1004 LEU B C   1 
ATOM   1678 O  O   . LEU A 1 235 ? 6.67658   -4.97930  24.70382  1.000 61.77165  ? 1004 LEU B O   1 
ATOM   1679 C  CB  . LEU A 1 235 ? 4.09241   -3.56049  25.88799  1.000 61.29387  ? 1004 LEU B CB  1 
ATOM   1680 C  CG  . LEU A 1 235 ? 3.45551   -2.28271  26.42409  1.000 65.68647  ? 1004 LEU B CG  1 
ATOM   1681 C  CD1 . LEU A 1 235 ? 2.93021   -1.42369  25.29287  1.000 59.92596  ? 1004 LEU B CD1 1 
ATOM   1682 C  CD2 . LEU A 1 235 ? 2.36301   -2.62095  27.43512  1.000 71.00629  ? 1004 LEU B CD2 1 
ATOM   1683 N  N   . LEU A 1 236 ? 6.15038   -5.96650  26.65344  1.000 61.22031  ? 1005 LEU B N   1 
ATOM   1684 C  CA  . LEU A 1 236 ? 6.81336   -7.21610  26.32904  1.000 61.50339  ? 1005 LEU B CA  1 
ATOM   1685 C  C   . LEU A 1 236 ? 5.80179   -8.24406  25.85798  1.000 62.51642  ? 1005 LEU B C   1 
ATOM   1686 O  O   . LEU A 1 236 ? 4.64666   -8.25277  26.29220  1.000 64.36684  ? 1005 LEU B O   1 
ATOM   1687 C  CB  . LEU A 1 236 ? 7.56509   -7.76304  27.53654  1.000 61.80052  ? 1005 LEU B CB  1 
ATOM   1688 C  CG  . LEU A 1 236 ? 8.57381   -6.78779  28.13769  1.000 60.65673  ? 1005 LEU B CG  1 
ATOM   1689 C  CD1 . LEU A 1 236 ? 9.49787   -7.50340  29.09332  1.000 59.54640  ? 1005 LEU B CD1 1 
ATOM   1690 C  CD2 . LEU A 1 236 ? 9.35408   -6.08646  27.06284  1.000 60.07358  ? 1005 LEU B CD2 1 
ATOM   1691 N  N   . TYR A 1 237 ? 6.26540   -9.12476  24.97979  1.000 64.92848  ? 1006 TYR B N   1 
ATOM   1692 C  CA  . TYR A 1 237 ? 5.48079   -10.24410 24.48842  1.000 66.05959  ? 1006 TYR B CA  1 
ATOM   1693 C  C   . TYR A 1 237 ? 6.35032   -11.50064 24.41472  1.000 69.99081  ? 1006 TYR B C   1 
ATOM   1694 O  O   . TYR A 1 237 ? 7.58180   -11.42956 24.48222  1.000 68.70984  ? 1006 TYR B O   1 
ATOM   1695 C  CB  . TYR A 1 237 ? 4.88947   -9.93635  23.11070  1.000 66.35502  ? 1006 TYR B CB  1 
ATOM   1696 C  CG  . TYR A 1 237 ? 4.13428   -8.64026  23.05303  1.000 67.86379  ? 1006 TYR B CG  1 
ATOM   1697 C  CD1 . TYR A 1 237 ? 2.89800   -8.52597  23.66377  1.000 69.85369  ? 1006 TYR B CD1 1 
ATOM   1698 C  CD2 . TYR A 1 237 ? 4.63947   -7.54031  22.37414  1.000 65.94019  ? 1006 TYR B CD2 1 
ATOM   1699 C  CE1 . TYR A 1 237 ? 2.19116   -7.35542  23.62340  1.000 69.96590  ? 1006 TYR B CE1 1 
ATOM   1700 C  CE2 . TYR A 1 237 ? 3.93700   -6.36756  22.31834  1.000 66.38155  ? 1006 TYR B CE2 1 
ATOM   1701 C  CZ  . TYR A 1 237 ? 2.70998   -6.28085  22.94719  1.000 69.69596  ? 1006 TYR B CZ  1 
ATOM   1702 O  OH  . TYR A 1 237 ? 1.98688   -5.11379  22.91186  1.000 76.92675  ? 1006 TYR B OH  1 
ATOM   1703 O  OXT . TYR A 1 237 ? 5.84129   -12.61988 24.30489  1.000 72.13903  ? 1006 TYR B OXT 1 
ATOM   1704 N  N   . SER B 1 1   ? 30.71285  -25.73524 23.88848  1.000 66.99680  ? 0    SER A N   1 
ATOM   1705 C  CA  . SER B 1 1   ? 30.37550  -24.56525 23.08640  1.000 65.45490  ? 0    SER A CA  1 
ATOM   1706 C  C   . SER B 1 1   ? 28.89372  -24.28563 23.20083  1.000 64.45880  ? 0    SER A C   1 
ATOM   1707 O  O   . SER B 1 1   ? 28.13844  -25.14609 23.65265  1.000 65.19495  ? 0    SER A O   1 
ATOM   1708 C  CB  . SER B 1 1   ? 30.73510  -24.78054 21.61480  1.000 63.77870  ? 0    SER A CB  1 
ATOM   1709 O  OG  . SER B 1 1   ? 29.88527  -25.75009 21.02326  1.000 60.56580  ? 0    SER A OG  1 
ATOM   1710 N  N   . MET B 1 2   ? 28.47202  -23.08342 22.79943  1.000 63.66524  ? 1    MET A N   1 
ATOM   1711 C  CA  . MET B 1 2   ? 27.04412  -22.78591 22.80070  1.000 65.68479  ? 1    MET A CA  1 
ATOM   1712 C  C   . MET B 1 2   ? 26.28297  -23.75692 21.90795  1.000 61.72168  ? 1    MET A C   1 
ATOM   1713 O  O   . MET B 1 2   ? 25.22284  -24.26771 22.29341  1.000 61.89163  ? 1    MET A O   1 
ATOM   1714 C  CB  . MET B 1 2   ? 26.79087  -21.35626 22.33157  1.000 69.26749  ? 1    MET A CB  1 
ATOM   1715 C  CG  . MET B 1 2   ? 25.36944  -20.88350 22.56676  1.000 71.03787  ? 1    MET A CG  1 
ATOM   1716 S  SD  . MET B 1 2   ? 25.14895  -19.16201 22.07940  1.000 105.40761 ? 1    MET A SD  1 
ATOM   1717 C  CE  . MET B 1 2   ? 26.44200  -18.30565 22.99009  1.000 86.29689  ? 1    MET A CE  1 
ATOM   1718 N  N   . ALA B 1 3   ? 26.82747  -24.05183 20.72266  1.000 61.12800  ? 2    ALA A N   1 
ATOM   1719 C  CA  . ALA B 1 3   ? 26.13861  -24.96025 19.81430  1.000 58.43504  ? 2    ALA A CA  1 
ATOM   1720 C  C   . ALA B 1 3   ? 25.95263  -26.32710 20.45284  1.000 56.83115  ? 2    ALA A C   1 
ATOM   1721 O  O   . ALA B 1 3   ? 24.86465  -26.90420 20.38095  1.000 55.96913  ? 2    ALA A O   1 
ATOM   1722 C  CB  . ALA B 1 3   ? 26.89853  -25.07612 18.49397  1.000 56.19540  ? 2    ALA A CB  1 
ATOM   1723 N  N   . LEU B 1 4   ? 26.99035  -26.84376 21.11392  1.000 57.39946  ? 3    LEU A N   1 
ATOM   1724 C  CA  . LEU B 1 4   ? 26.90501  -28.18254 21.69503  1.000 57.85562  ? 3    LEU A CA  1 
ATOM   1725 C  C   . LEU B 1 4   ? 25.93660  -28.23093 22.88016  1.000 59.13603  ? 3    LEU A C   1 
ATOM   1726 O  O   . LEU B 1 4   ? 25.18172  -29.20333 23.03336  1.000 60.40473  ? 3    LEU A O   1 
ATOM   1727 C  CB  . LEU B 1 4   ? 28.30011  -28.65795 22.10095  1.000 57.22798  ? 3    LEU A CB  1 
ATOM   1728 C  CG  . LEU B 1 4   ? 28.35626  -30.04199 22.73847  1.000 58.28698  ? 3    LEU A CG  1 
ATOM   1729 C  CD1 . LEU B 1 4   ? 27.90060  -31.11936 21.77211  1.000 61.42752  ? 3    LEU A CD1 1 
ATOM   1730 C  CD2 . LEU B 1 4   ? 29.75397  -30.31646 23.23698  1.000 58.03738  ? 3    LEU A CD2 1 
ATOM   1731 N  N   . LYS B 1 5   ? 25.93277  -27.19300 23.72136  1.000 59.23077  ? 4    LYS A N   1 
ATOM   1732 C  CA  . LYS B 1 5   ? 24.96030  -27.13247 24.80594  1.000 59.97383  ? 4    LYS A CA  1 
ATOM   1733 C  C   . LYS B 1 5   ? 23.54171  -27.09053 24.26240  1.000 59.24910  ? 4    LYS A C   1 
ATOM   1734 O  O   . LYS B 1 5   ? 22.64796  -27.77720 24.77102  1.000 59.48019  ? 4    LYS A O   1 
ATOM   1735 C  CB  . LYS B 1 5   ? 25.22666  -25.90500 25.67240  1.000 62.94765  ? 4    LYS A CB  1 
ATOM   1736 C  CG  . LYS B 1 5   ? 26.63111  -25.82612 26.21050  1.000 63.87682  ? 4    LYS A CG  1 
ATOM   1737 C  CD  . LYS B 1 5   ? 26.76192  -26.41328 27.58514  1.000 67.01445  ? 4    LYS A CD  1 
ATOM   1738 C  CE  . LYS B 1 5   ? 28.13038  -26.06792 28.14830  1.000 70.79160  ? 4    LYS A CE  1 
ATOM   1739 N  NZ  . LYS B 1 5   ? 28.41628  -24.60562 28.00556  1.000 72.00179  ? 4    LYS A NZ  1 
ATOM   1740 N  N   . ARG B 1 6   ? 23.31555  -26.28543 23.22927  1.000 58.52603  ? 5    ARG A N   1 
ATOM   1741 C  CA  . ARG B 1 6   ? 21.97746  -26.19333 22.65868  1.000 58.31303  ? 5    ARG A CA  1 
ATOM   1742 C  C   . ARG B 1 6   ? 21.55714  -27.50909 21.99388  1.000 58.78829  ? 5    ARG A C   1 
ATOM   1743 O  O   . ARG B 1 6   ? 20.39068  -27.91151 22.07556  1.000 60.00703  ? 5    ARG A O   1 
ATOM   1744 C  CB  . ARG B 1 6   ? 21.92556  -25.00068 21.70189  1.000 57.83451  ? 5    ARG A CB  1 
ATOM   1745 C  CG  . ARG B 1 6   ? 20.79221  -25.00561 20.72050  1.000 57.75236  ? 5    ARG A CG  1 
ATOM   1746 C  CD  . ARG B 1 6   ? 19.52159  -24.41412 21.28431  1.000 58.51131  ? 5    ARG A CD  1 
ATOM   1747 N  NE  . ARG B 1 6   ? 18.48235  -24.50836 20.26847  1.000 58.54821  ? 5    ARG A NE  1 
ATOM   1748 C  CZ  . ARG B 1 6   ? 17.89027  -23.47228 19.69712  1.000 56.92380  ? 5    ARG A CZ  1 
ATOM   1749 N  NH1 . ARG B 1 6   ? 18.14144  -22.23280 20.08203  1.000 57.83745  ? 5    ARG A NH1 1 
ATOM   1750 N  NH2 . ARG B 1 6   ? 17.02117  -23.68620 18.71775  1.000 56.08533  ? 5    ARG A NH2 1 
ATOM   1751 N  N   . ILE B 1 7   ? 22.49196  -28.20827 21.35181  1.000 56.46555  ? 6    ILE A N   1 
ATOM   1752 C  CA  . ILE B 1 7   ? 22.16172  -29.49230 20.73360  1.000 57.68884  ? 6    ILE A CA  1 
ATOM   1753 C  C   . ILE B 1 7   ? 21.78776  -30.52574 21.79477  1.000 60.76092  ? 6    ILE A C   1 
ATOM   1754 O  O   . ILE B 1 7   ? 20.78822  -31.24083 21.65707  1.000 61.31538  ? 6    ILE A O   1 
ATOM   1755 C  CB  . ILE B 1 7   ? 23.32783  -29.96196 19.83759  1.000 55.06318  ? 6    ILE A CB  1 
ATOM   1756 C  CG1 . ILE B 1 7   ? 23.40571  -29.08988 18.57569  1.000 52.70742  ? 6    ILE A CG1 1 
ATOM   1757 C  CG2 . ILE B 1 7   ? 23.19354  -31.43320 19.48654  1.000 55.40584  ? 6    ILE A CG2 1 
ATOM   1758 C  CD1 . ILE B 1 7   ? 24.69690  -29.20266 17.79376  1.000 51.96678  ? 6    ILE A CD1 1 
ATOM   1759 N  N   . HIS B 1 8   ? 22.55729  -30.60177 22.88186  1.000 60.89229  ? 7    HIS A N   1 
ATOM   1760 C  CA  . HIS B 1 8   ? 22.18947  -31.51004 23.96609  1.000 63.93689  ? 7    HIS A CA  1 
ATOM   1761 C  C   . HIS B 1 8   ? 20.84162  -31.14220 24.57899  1.000 66.51217  ? 7    HIS A C   1 
ATOM   1762 O  O   . HIS B 1 8   ? 20.03656  -32.02622 24.89320  1.000 67.46412  ? 7    HIS A O   1 
ATOM   1763 C  CB  . HIS B 1 8   ? 23.27014  -31.50986 25.04410  1.000 64.20447  ? 7    HIS A CB  1 
ATOM   1764 C  CG  . HIS B 1 8   ? 24.40289  -32.44021 24.75552  1.000 65.40398  ? 7    HIS A CG  1 
ATOM   1765 N  ND1 . HIS B 1 8   ? 25.67503  -31.99386 24.46825  1.000 66.24564  ? 7    HIS A ND1 1 
ATOM   1766 C  CD2 . HIS B 1 8   ? 24.45743  -33.79268 24.70900  1.000 64.85088  ? 7    HIS A CD2 1 
ATOM   1767 C  CE1 . HIS B 1 8   ? 26.46454  -33.03126 24.25274  1.000 66.87509  ? 7    HIS A CE1 1 
ATOM   1768 N  NE2 . HIS B 1 8   ? 25.75069  -34.13410 24.39478  1.000 66.31272  ? 7    HIS A NE2 1 
ATOM   1769 N  N   . LYS B 1 9   ? 20.58276  -29.84534 24.78023  1.000 66.31920  ? 8    LYS A N   1 
ATOM   1770 C  CA  . LYS B 1 9   ? 19.30370  -29.44777 25.36165  1.000 68.13059  ? 8    LYS A CA  1 
ATOM   1771 C  C   . LYS B 1 9   ? 18.15044  -29.86595 24.46033  1.000 69.53301  ? 8    LYS A C   1 
ATOM   1772 O  O   . LYS B 1 9   ? 17.12964  -30.37633 24.94169  1.000 72.23076  ? 8    LYS A O   1 
ATOM   1773 C  CB  . LYS B 1 9   ? 19.27038  -27.93760 25.61725  1.000 68.53299  ? 8    LYS A CB  1 
ATOM   1774 C  CG  . LYS B 1 9   ? 17.96094  -27.43431 26.24588  1.000 75.76967  ? 8    LYS A CG  1 
ATOM   1775 C  CD  . LYS B 1 9   ? 17.78765  -27.90495 27.69017  1.000 79.66862  ? 8    LYS A CD  1 
ATOM   1776 C  CE  . LYS B 1 9   ? 16.36757  -27.68120 28.22603  1.000 84.89222  ? 8    LYS A CE  1 
ATOM   1777 N  NZ  . LYS B 1 9   ? 16.23755  -28.13347 29.65093  1.000 88.84656  ? 8    LYS A NZ  1 
ATOM   1778 N  N   . GLU B 1 10  ? 18.30298  -29.67391 23.14376  1.000 67.08759  ? 9    GLU A N   1 
ATOM   1779 C  CA  . GLU B 1 10  ? 17.25156  -30.06974 22.21138  1.000 67.15870  ? 9    GLU A CA  1 
ATOM   1780 C  C   . GLU B 1 10  ? 17.08026  -31.57613 22.19279  1.000 67.41059  ? 9    GLU A C   1 
ATOM   1781 O  O   . GLU B 1 10  ? 15.96266  -32.07891 22.06393  1.000 69.84035  ? 9    GLU A O   1 
ATOM   1782 C  CB  . GLU B 1 10  ? 17.56797  -29.57101 20.80176  1.000 61.01011  ? 9    GLU A CB  1 
ATOM   1783 C  CG  . GLU B 1 10  ? 17.33151  -28.09630 20.54781  1.000 57.32794  ? 9    GLU A CG  1 
ATOM   1784 C  CD  . GLU B 1 10  ? 17.43697  -27.76208 19.07460  1.000 56.24398  ? 9    GLU A CD  1 
ATOM   1785 O  OE1 . GLU B 1 10  ? 16.76097  -28.42873 18.26192  1.000 55.00261  ? 9    GLU A OE1 1 
ATOM   1786 O  OE2 . GLU B 1 10  ? 18.23848  -26.87762 18.72196  1.000 52.48225  ? 9    GLU A OE2 1 
ATOM   1787 N  N   . LEU B 1 11  ? 18.17583  -32.30866 22.34028  1.000 66.25830  ? 10   LEU A N   1 
ATOM   1788 C  CA  . LEU B 1 11  ? 18.09340  -33.76014 22.34969  1.000 67.81506  ? 10   LEU A CA  1 
ATOM   1789 C  C   . LEU B 1 11  ? 17.36270  -34.25135 23.60162  1.000 73.39897  ? 10   LEU A C   1 
ATOM   1790 O  O   . LEU B 1 11  ? 16.49607  -35.13553 23.52674  1.000 76.59085  ? 10   LEU A O   1 
ATOM   1791 C  CB  . LEU B 1 11  ? 19.51101  -34.31566 22.23573  1.000 64.64393  ? 10   LEU A CB  1 
ATOM   1792 C  CG  . LEU B 1 11  ? 19.75189  -35.76606 21.85156  1.000 63.98061  ? 10   LEU A CG  1 
ATOM   1793 C  CD1 . LEU B 1 11  ? 18.97920  -36.08448 20.58264  1.000 62.17135  ? 10   LEU A CD1 1 
ATOM   1794 C  CD2 . LEU B 1 11  ? 21.23591  -35.94867 21.62849  1.000 60.66650  ? 10   LEU A CD2 1 
ATOM   1795 N  N   . ASN B 1 12  ? 17.65551  -33.64527 24.75514  1.000 73.22951  ? 11   ASN A N   1 
ATOM   1796 C  CA  . ASN B 1 12  ? 16.95257  -34.01559 25.97978  1.000 77.08313  ? 11   ASN A CA  1 
ATOM   1797 C  C   . ASN B 1 12  ? 15.47508  -33.66945 25.89400  1.000 81.34345  ? 11   ASN A C   1 
ATOM   1798 O  O   . ASN B 1 12  ? 14.62559  -34.45412 26.32798  1.000 85.34684  ? 11   ASN A O   1 
ATOM   1799 C  CB  . ASN B 1 12  ? 17.58050  -33.31903 27.18249  1.000 76.06960  ? 11   ASN A CB  1 
ATOM   1800 C  CG  . ASN B 1 12  ? 19.01085  -33.74169 27.40942  1.000 77.10274  ? 11   ASN A CG  1 
ATOM   1801 O  OD1 . ASN B 1 12  ? 19.35615  -34.91864 27.25792  1.000 77.44954  ? 11   ASN A OD1 1 
ATOM   1802 N  ND2 . ASN B 1 12  ? 19.86325  -32.77984 27.75393  1.000 75.03766  ? 11   ASN A ND2 1 
ATOM   1803 N  N   . ASP B 1 13  ? 15.14617  -32.50222 25.33255  1.000 79.31273  ? 12   ASP A N   1 
ATOM   1804 C  CA  . ASP B 1 13  ? 13.73968  -32.13805 25.18149  1.000 83.34665  ? 12   ASP A CA  1 
ATOM   1805 C  C   . ASP B 1 13  ? 13.04342  -33.03269 24.16260  1.000 83.58722  ? 12   ASP A C   1 
ATOM   1806 O  O   . ASP B 1 13  ? 11.83822  -33.27707 24.27057  1.000 90.30296  ? 12   ASP A O   1 
ATOM   1807 C  CB  . ASP B 1 13  ? 13.61231  -30.66676 24.78273  1.000 82.16884  ? 12   ASP A CB  1 
ATOM   1808 C  CG  . ASP B 1 13  ? 14.12307  -29.71316 25.86450  1.000 86.78109  ? 12   ASP A CG  1 
ATOM   1809 O  OD1 . ASP B 1 13  ? 14.57098  -30.17775 26.93818  1.000 87.14378  ? 12   ASP A OD1 1 
ATOM   1810 O  OD2 . ASP B 1 13  ? 14.07084  -28.48506 25.63725  1.000 92.93333  ? 12   ASP A OD2 1 
ATOM   1811 N  N   . LEU B 1 14  ? 13.78117  -33.53608 23.17500  1.000 79.26866  ? 13   LEU A N   1 
ATOM   1812 C  CA  . LEU B 1 14  ? 13.22560  -34.52130 22.26141  1.000 82.42972  ? 13   LEU A CA  1 
ATOM   1813 C  C   . LEU B 1 14  ? 13.02476  -35.85056 22.96138  1.000 87.84503  ? 13   LEU A C   1 
ATOM   1814 O  O   . LEU B 1 14  ? 12.28496  -36.70098 22.46083  1.000 91.10401  ? 13   LEU A O   1 
ATOM   1815 C  CB  . LEU B 1 14  ? 14.13912  -34.69308 21.05120  1.000 76.81323  ? 13   LEU A CB  1 
ATOM   1816 C  CG  . LEU B 1 14  ? 14.07428  -33.59191 19.99859  1.000 70.53294  ? 13   LEU A CG  1 
ATOM   1817 C  CD1 . LEU B 1 14  ? 15.20050  -33.79611 19.04924  1.000 65.08938  ? 13   LEU A CD1 1 
ATOM   1818 C  CD2 . LEU B 1 14  ? 12.76290  -33.64204 19.26893  1.000 67.77952  ? 13   LEU A CD2 1 
ATOM   1819 N  N   . ALA B 1 15  ? 13.70983  -36.05846 24.08395  1.000 87.47908  ? 14   ALA A N   1 
ATOM   1820 C  CA  . ALA B 1 15  ? 13.52822  -37.26682 24.87481  1.000 92.61161  ? 14   ALA A CA  1 
ATOM   1821 C  C   . ALA B 1 15  ? 12.34908  -37.16354 25.84395  1.000 96.38776  ? 14   ALA A C   1 
ATOM   1822 O  O   . ALA B 1 15  ? 11.60154  -38.13463 26.00738  1.000 96.73337  ? 14   ALA A O   1 
ATOM   1823 C  CB  . ALA B 1 15  ? 14.81047  -37.57984 25.65372  1.000 91.04577  ? 14   ALA A CB  1 
ATOM   1824 N  N   . ARG B 1 16  ? 12.14228  -35.99330 26.46457  1.000 98.38739  ? 15   ARG A N   1 
ATOM   1825 C  CA  . ARG B 1 16  ? 11.06639  -35.81844 27.43828  1.000 102.37785 ? 15   ARG A CA  1 
ATOM   1826 C  C   . ARG B 1 16  ? 9.69442   -35.66492 26.80061  1.000 105.37021 ? 15   ARG A C   1 
ATOM   1827 O  O   . ARG B 1 16  ? 8.68464   -35.90992 27.47164  1.000 108.09098 ? 15   ARG A O   1 
ATOM   1828 C  CB  . ARG B 1 16  ? 11.34783  -34.58299 28.30927  1.000 101.36756 ? 15   ARG A CB  1 
ATOM   1829 C  CG  . ARG B 1 16  ? 12.68949  -34.62155 29.02523  1.000 100.58848 ? 15   ARG A CG  1 
ATOM   1830 C  CD  . ARG B 1 16  ? 12.98640  -33.33865 29.79597  1.000 105.10768 ? 15   ARG A CD  1 
ATOM   1831 N  NE  . ARG B 1 16  ? 12.95121  -32.13850 28.96511  1.000 101.98354 ? 15   ARG A NE  1 
ATOM   1832 C  CZ  . ARG B 1 16  ? 12.00847  -31.20577 29.02562  1.000 103.17825 ? 15   ARG A CZ  1 
ATOM   1833 N  NH1 . ARG B 1 16  ? 11.03537  -31.26143 29.92123  1.000 103.79853 ? 15   ARG A NH1 1 
ATOM   1834 N  NH2 . ARG B 1 16  ? 12.06933  -30.16630 28.19743  1.000 99.37051  ? 15   ARG A NH2 1 
ATOM   1835 N  N   . ASP B 1 17  ? 9.63015   -35.23346 25.54546  1.000 103.56956 ? 16   ASP A N   1 
ATOM   1836 C  CA  . ASP B 1 17  ? 8.36271   -35.12965 24.82336  1.000 107.02305 ? 16   ASP A CA  1 
ATOM   1837 C  C   . ASP B 1 17  ? 8.62864   -35.29480 23.33273  1.000 105.24841 ? 16   ASP A C   1 
ATOM   1838 O  O   . ASP B 1 17  ? 8.63909   -34.32103 22.57051  1.000 106.19315 ? 16   ASP A O   1 
ATOM   1839 C  CB  . ASP B 1 17  ? 7.65356   -33.81339 25.14492  1.000 114.39667 ? 16   ASP A CB  1 
ATOM   1840 C  CG  . ASP B 1 17  ? 6.21026   -33.80369 24.68939  1.000 124.00689 ? 16   ASP A CG  1 
ATOM   1841 O  OD1 . ASP B 1 17  ? 5.84302   -34.64472 23.83883  1.000 122.27417 ? 16   ASP A OD1 1 
ATOM   1842 O  OD2 . ASP B 1 17  ? 5.42102   -33.02098 25.26008  1.000 131.74197 ? 16   ASP A OD2 1 
ATOM   1843 N  N   . PRO B 1 18  ? 8.87840   -36.52803 22.88709  1.000 101.77828 ? 17   PRO A N   1 
ATOM   1844 C  CA  . PRO B 1 18  ? 9.26159   -36.73407 21.48898  1.000 96.98673  ? 17   PRO A CA  1 
ATOM   1845 C  C   . PRO B 1 18  ? 8.14050   -36.32022 20.55221  1.000 94.94211  ? 17   PRO A C   1 
ATOM   1846 O  O   . PRO B 1 18  ? 6.95216   -36.41244 20.90513  1.000 97.35276  ? 17   PRO A O   1 
ATOM   1847 C  CB  . PRO B 1 18  ? 9.52339   -38.24674 21.41820  1.000 96.10317  ? 17   PRO A CB  1 
ATOM   1848 C  CG  . PRO B 1 18  ? 9.73157   -38.67888 22.83656  1.000 97.30052  ? 17   PRO A CG  1 
ATOM   1849 C  CD  . PRO B 1 18  ? 8.86819   -37.78069 23.65727  1.000 100.17551 ? 17   PRO A CD  1 
ATOM   1850 N  N   . PRO B 1 19  ? 8.47932   -35.84628 19.35028  1.000 90.58475  ? 18   PRO A N   1 
ATOM   1851 C  CA  . PRO B 1 19  ? 7.43288   -35.56674 18.35758  1.000 87.10502  ? 18   PRO A CA  1 
ATOM   1852 C  C   . PRO B 1 19  ? 6.89685   -36.85388 17.75540  1.000 86.28530  ? 18   PRO A C   1 
ATOM   1853 O  O   . PRO B 1 19  ? 7.64695   -37.77805 17.44061  1.000 85.62913  ? 18   PRO A O   1 
ATOM   1854 C  CB  . PRO B 1 19  ? 8.16529   -34.71770 17.31208  1.000 80.83744  ? 18   PRO A CB  1 
ATOM   1855 C  CG  . PRO B 1 19  ? 9.56706   -35.21644 17.37803  1.000 79.07267  ? 18   PRO A CG  1 
ATOM   1856 C  CD  . PRO B 1 19  ? 9.82775   -35.62527 18.80508  1.000 85.53017  ? 18   PRO A CD  1 
ATOM   1857 N  N   . ALA B 1 20  ? 5.57915   -36.88431 17.55443  1.000 87.44528  ? 19   ALA A N   1 
ATOM   1858 C  CA  . ALA B 1 20  ? 4.91552   -38.11121 17.11811  1.000 86.98617  ? 19   ALA A CA  1 
ATOM   1859 C  C   . ALA B 1 20  ? 5.25233   -38.44819 15.67825  1.000 85.05945  ? 19   ALA A C   1 
ATOM   1860 O  O   . ALA B 1 20  ? 5.44528   -39.61859 15.32894  1.000 86.05480  ? 19   ALA A O   1 
ATOM   1861 C  CB  . ALA B 1 20  ? 3.40654   -37.98158 17.29257  1.000 84.07978  ? 19   ALA A CB  1 
ATOM   1862 N  N   . GLN B 1 21  ? 5.34578   -37.43689 14.83343  1.000 82.64131  ? 20   GLN A N   1 
ATOM   1863 C  CA  . GLN B 1 21  ? 5.47538   -37.71519 13.41896  1.000 82.67785  ? 20   GLN A CA  1 
ATOM   1864 C  C   . GLN B 1 21  ? 6.92586   -38.01097 13.05457  1.000 81.53232  ? 20   GLN A C   1 
ATOM   1865 O  O   . GLN B 1 21  ? 7.18678   -38.78595 12.12679  1.000 84.01476  ? 20   GLN A O   1 
ATOM   1866 C  CB  . GLN B 1 21  ? 4.92628   -36.50772 12.64345  1.000 82.13260  ? 20   GLN A CB  1 
ATOM   1867 C  CG  . GLN B 1 21  ? 4.19094   -36.79428 11.33420  1.000 80.37914  ? 20   GLN A CG  1 
ATOM   1868 C  CD  . GLN B 1 21  ? 3.42144   -35.57751 10.82055  1.000 76.64939  ? 20   GLN A CD  1 
ATOM   1869 O  OE1 . GLN B 1 21  ? 3.11120   -34.64998 11.57950  1.000 74.16369  ? 20   GLN A OE1 1 
ATOM   1870 N  NE2 . GLN B 1 21  ? 3.11327   -35.57777 9.53080   1.000 72.96630  ? 20   GLN A NE2 1 
ATOM   1871 N  N   . CYS B 1 22  ? 7.86875   -37.43088 13.78639  1.000 78.99199  ? 21   CYS A N   1 
ATOM   1872 C  CA  . CYS B 1 22  ? 9.28659   -37.45921 13.46295  1.000 72.50437  ? 21   CYS A CA  1 
ATOM   1873 C  C   . CYS B 1 22  ? 10.08878  -38.23491 14.50293  1.000 71.68005  ? 21   CYS A C   1 
ATOM   1874 O  O   . CYS B 1 22  ? 9.57003   -38.68917 15.52429  1.000 75.69910  ? 21   CYS A O   1 
ATOM   1875 C  CB  . CYS B 1 22  ? 9.79457   -36.02674 13.36613  1.000 70.79919  ? 21   CYS A CB  1 
ATOM   1876 S  SG  . CYS B 1 22  ? 8.52507   -34.98646 12.64578  1.000 83.43105  ? 21   CYS A SG  1 
ATOM   1877 N  N   . SER B 1 23  ? 11.38434  -38.35853 14.22476  1.000 66.16932  ? 22   SER A N   1 
ATOM   1878 C  CA  . SER B 1 23  ? 12.35064  -38.92857 15.16024  1.000 64.42162  ? 22   SER A CA  1 
ATOM   1879 C  C   . SER B 1 23  ? 13.73891  -38.49883 14.70151  1.000 61.89752  ? 22   SER A C   1 
ATOM   1880 O  O   . SER B 1 23  ? 13.99007  -38.42974 13.50066  1.000 64.16692  ? 22   SER A O   1 
ATOM   1881 C  CB  . SER B 1 23  ? 12.25341  -40.45496 15.23647  1.000 64.16549  ? 22   SER A CB  1 
ATOM   1882 O  OG  . SER B 1 23  ? 13.21491  -41.05714 14.39579  1.000 69.96940  ? 22   SER A OG  1 
ATOM   1883 N  N   . ALA B 1 24  ? 14.62363  -38.16773 15.63951  1.000 59.32260  ? 23   ALA A N   1 
ATOM   1884 C  CA  . ALA B 1 24  ? 15.93515  -37.69094 15.21584  1.000 57.55544  ? 23   ALA A CA  1 
ATOM   1885 C  C   . ALA B 1 24  ? 16.96488  -37.87852 16.31343  1.000 56.40971  ? 23   ALA A C   1 
ATOM   1886 O  O   . ALA B 1 24  ? 16.64873  -37.79443 17.49866  1.000 59.04450  ? 23   ALA A O   1 
ATOM   1887 C  CB  . ALA B 1 24  ? 15.88564  -36.21798 14.80620  1.000 57.08688  ? 23   ALA A CB  1 
ATOM   1888 N  N   . GLY B 1 25  ? 18.19805  -38.13472 15.90731  1.000 52.26977  ? 24   GLY A N   1 
ATOM   1889 C  CA  . GLY B 1 25  ? 19.25533  -38.24141 16.87464  1.000 52.40803  ? 24   GLY A CA  1 
ATOM   1890 C  C   . GLY B 1 25  ? 20.62783  -38.37531 16.26584  1.000 56.50151  ? 24   GLY A C   1 
ATOM   1891 O  O   . GLY B 1 25  ? 20.78669  -38.54235 15.05682  1.000 55.44796  ? 24   GLY A O   1 
ATOM   1892 N  N   . PRO B 1 26  ? 21.65359  -38.31794 17.10882  1.000 57.25132  ? 25   PRO A N   1 
ATOM   1893 C  CA  . PRO B 1 26  ? 23.02566  -38.48402 16.61513  1.000 60.64446  ? 25   PRO A CA  1 
ATOM   1894 C  C   . PRO B 1 26  ? 23.19626  -39.82457 15.92470  1.000 64.93313  ? 25   PRO A C   1 
ATOM   1895 O  O   . PRO B 1 26  ? 22.63832  -40.83324 16.35361  1.000 65.45326  ? 25   PRO A O   1 
ATOM   1896 C  CB  . PRO B 1 26  ? 23.86505  -38.41977 17.89748  1.000 61.76980  ? 25   PRO A CB  1 
ATOM   1897 C  CG  . PRO B 1 26  ? 23.00812  -37.65180 18.86238  1.000 56.77569  ? 25   PRO A CG  1 
ATOM   1898 C  CD  . PRO B 1 26  ? 21.60767  -38.06464 18.56046  1.000 55.13998  ? 25   PRO A CD  1 
ATOM   1899 N  N   . VAL B 1 27  ? 23.99667  -39.83762 14.85698  1.000 70.60653  ? 26   VAL A N   1 
ATOM   1900 C  CA  . VAL B 1 27  ? 24.24770  -41.09234 14.15019  1.000 74.07026  ? 26   VAL A CA  1 
ATOM   1901 C  C   . VAL B 1 27  ? 25.13104  -42.00709 14.99734  1.000 79.82212  ? 26   VAL A C   1 
ATOM   1902 O  O   . VAL B 1 27  ? 24.82213  -43.18858 15.19787  1.000 84.93579  ? 26   VAL A O   1 
ATOM   1903 C  CB  . VAL B 1 27  ? 24.84880  -40.82359 12.75652  1.000 75.14577  ? 26   VAL A CB  1 
ATOM   1904 C  CG1 . VAL B 1 27  ? 23.80819  -40.19388 11.84358  1.000 66.83554  ? 26   VAL A CG1 1 
ATOM   1905 C  CG2 . VAL B 1 27  ? 26.05869  -39.91767 12.85454  1.000 72.44121  ? 26   VAL A CG2 1 
ATOM   1906 N  N   . GLY B 1 28  ? 26.22138  -41.46782 15.53482  1.000 82.55365  ? 27   GLY A N   1 
ATOM   1907 C  CA  . GLY B 1 28  ? 27.04843  -42.17656 16.49274  1.000 80.02455  ? 27   GLY A CA  1 
ATOM   1908 C  C   . GLY B 1 28  ? 27.38085  -41.24736 17.63949  1.000 80.42930  ? 27   GLY A C   1 
ATOM   1909 O  O   . GLY B 1 28  ? 26.50613  -40.90642 18.44154  1.000 79.67074  ? 27   GLY A O   1 
ATOM   1910 N  N   . ASP B 1 29  ? 28.64168  -40.83253 17.72580  1.000 81.71429  ? 28   ASP A N   1 
ATOM   1911 C  CA  . ASP B 1 29  ? 29.09186  -39.84293 18.69668  1.000 82.16573  ? 28   ASP A CA  1 
ATOM   1912 C  C   . ASP B 1 29  ? 29.16979  -38.44074 18.11579  1.000 77.50625  ? 28   ASP A C   1 
ATOM   1913 O  O   . ASP B 1 29  ? 29.65669  -37.52678 18.78964  1.000 75.83289  ? 28   ASP A O   1 
ATOM   1914 C  CB  . ASP B 1 29  ? 30.44870  -40.24133 19.27885  1.000 88.38147  ? 28   ASP A CB  1 
ATOM   1915 C  CG  . ASP B 1 29  ? 30.32693  -41.29411 20.36112  1.000 96.09806  ? 28   ASP A CG  1 
ATOM   1916 O  OD1 . ASP B 1 29  ? 29.20260  -41.49145 20.87318  1.000 97.71280  ? 28   ASP A OD1 1 
ATOM   1917 O  OD2 . ASP B 1 29  ? 31.34871  -41.93791 20.68893  1.000 98.37755  ? 28   ASP A OD2 1 
ATOM   1918 N  N   . ASP B 1 30  ? 28.73852  -38.25090 16.87733  1.000 74.34752  ? 29   ASP A N   1 
ATOM   1919 C  CA  . ASP B 1 30  ? 28.80981  -36.93970 16.24872  1.000 68.75906  ? 29   ASP A CA  1 
ATOM   1920 C  C   . ASP B 1 30  ? 27.52241  -36.20315 16.58585  1.000 64.94794  ? 29   ASP A C   1 
ATOM   1921 O  O   . ASP B 1 30  ? 26.45629  -36.49863 16.04037  1.000 63.17323  ? 29   ASP A O   1 
ATOM   1922 C  CB  . ASP B 1 30  ? 29.02941  -37.05917 14.74619  1.000 67.81258  ? 29   ASP A CB  1 
ATOM   1923 C  CG  . ASP B 1 30  ? 29.35515  -35.72922 14.11301  1.000 67.72848  ? 29   ASP A CG  1 
ATOM   1924 O  OD1 . ASP B 1 30  ? 29.68796  -34.79341 14.87260  1.000 66.40796  ? 29   ASP A OD1 1 
ATOM   1925 O  OD2 . ASP B 1 30  ? 29.31559  -35.62185 12.86976  1.000 67.23025  ? 29   ASP A OD2 1 
ATOM   1926 N  N   . MET B 1 31  ? 27.62062  -35.25935 17.52380  1.000 63.19328  ? 30   MET A N   1 
ATOM   1927 C  CA  . MET B 1 31  ? 26.46018  -34.47815 17.92172  1.000 59.25486  ? 30   MET A CA  1 
ATOM   1928 C  C   . MET B 1 31  ? 26.03796  -33.49819 16.84719  1.000 57.50815  ? 30   MET A C   1 
ATOM   1929 O  O   . MET B 1 31  ? 24.88047  -33.06494 16.83836  1.000 54.84687  ? 30   MET A O   1 
ATOM   1930 C  CB  . MET B 1 31  ? 26.76731  -33.72942 19.21287  1.000 57.71954  ? 30   MET A CB  1 
ATOM   1931 C  CG  . MET B 1 31  ? 27.14552  -34.64976 20.34355  1.000 58.98072  ? 30   MET A CG  1 
ATOM   1932 S  SD  . MET B 1 31  ? 25.73015  -35.64976 20.84143  1.000 62.38389  ? 30   MET A SD  1 
ATOM   1933 C  CE  . MET B 1 31  ? 24.52136  -34.38732 21.24306  1.000 58.24532  ? 30   MET A CE  1 
ATOM   1934 N  N   . PHE B 1 32  ? 26.93754  -33.16376 15.93059  1.000 58.05449  ? 31   PHE A N   1 
ATOM   1935 C  CA  . PHE B 1 32  ? 26.64701  -32.20509 14.88048  1.000 54.56671  ? 31   PHE A CA  1 
ATOM   1936 C  C   . PHE B 1 32  ? 26.14797  -32.85878 13.60204  1.000 56.64907  ? 31   PHE A C   1 
ATOM   1937 O  O   . PHE B 1 32  ? 25.88632  -32.14794 12.62725  1.000 56.65914  ? 31   PHE A O   1 
ATOM   1938 C  CB  . PHE B 1 32  ? 27.88635  -31.35994 14.59035  1.000 53.41930  ? 31   PHE A CB  1 
ATOM   1939 C  CG  . PHE B 1 32  ? 28.16563  -30.31227 15.63401  1.000 53.63842  ? 31   PHE A CG  1 
ATOM   1940 C  CD1 . PHE B 1 32  ? 28.88784  -30.61768 16.78324  1.000 54.87685  ? 31   PHE A CD1 1 
ATOM   1941 C  CD2 . PHE B 1 32  ? 27.70351  -29.01702 15.46223  1.000 52.48568  ? 31   PHE A CD2 1 
ATOM   1942 C  CE1 . PHE B 1 32  ? 29.14717  -29.63913 17.73609  1.000 54.82623  ? 31   PHE A CE1 1 
ATOM   1943 C  CE2 . PHE B 1 32  ? 27.95383  -28.04168 16.40174  1.000 55.10990  ? 31   PHE A CE2 1 
ATOM   1944 C  CZ  . PHE B 1 32  ? 28.67196  -28.35207 17.54628  1.000 56.18600  ? 31   PHE A CZ  1 
ATOM   1945 N  N   . HIS B 1 33  ? 25.97497  -34.18036 13.59851  1.000 58.47746  ? 32   HIS A N   1 
ATOM   1946 C  CA  . HIS B 1 33  ? 25.38478  -34.91627 12.48460  1.000 57.39866  ? 32   HIS A CA  1 
ATOM   1947 C  C   . HIS B 1 33  ? 24.33274  -35.85623 13.04510  1.000 55.63334  ? 32   HIS A C   1 
ATOM   1948 O  O   . HIS B 1 33  ? 24.64667  -36.72756 13.86135  1.000 58.12619  ? 32   HIS A O   1 
ATOM   1949 C  CB  . HIS B 1 33  ? 26.43449  -35.70586 11.70001  1.000 59.50980  ? 32   HIS A CB  1 
ATOM   1950 C  CG  . HIS B 1 33  ? 27.15430  -34.89593 10.67044  1.000 64.69673  ? 32   HIS A CG  1 
ATOM   1951 N  ND1 . HIS B 1 33  ? 28.36368  -34.28106 10.91741  1.000 67.48307  ? 32   HIS A ND1 1 
ATOM   1952 C  CD2 . HIS B 1 33  ? 26.83124  -34.59407 9.39060   1.000 67.53469  ? 32   HIS A CD2 1 
ATOM   1953 C  CE1 . HIS B 1 33  ? 28.75740  -33.64107 9.83155   1.000 70.61325  ? 32   HIS A CE1 1 
ATOM   1954 N  NE2 . HIS B 1 33  ? 27.84401  -33.81297 8.89256   1.000 71.87743  ? 32   HIS A NE2 1 
ATOM   1955 N  N   . TRP B 1 34  ? 23.08754  -35.64503 12.65055  1.000 52.26709  ? 33   TRP A N   1 
ATOM   1956 C  CA  . TRP B 1 34  ? 21.98114  -36.46841 13.08737  1.000 51.81201  ? 33   TRP A CA  1 
ATOM   1957 C  C   . TRP B 1 34  ? 21.37260  -37.18996 11.89681  1.000 50.84125  ? 33   TRP A C   1 
ATOM   1958 O  O   . TRP B 1 34  ? 21.52064  -36.77912 10.74195  1.000 49.32776  ? 33   TRP A O   1 
ATOM   1959 C  CB  . TRP B 1 34  ? 20.89843  -35.63303 13.75834  1.000 51.19910  ? 33   TRP A CB  1 
ATOM   1960 C  CG  . TRP B 1 34  ? 21.28711  -35.03455 15.06174  1.000 53.38027  ? 33   TRP A CG  1 
ATOM   1961 C  CD1 . TRP B 1 34  ? 22.54881  -34.90219 15.57442  1.000 55.21048  ? 33   TRP A CD1 1 
ATOM   1962 C  CD2 . TRP B 1 34  ? 20.39647  -34.49133 16.03612  1.000 53.63880  ? 33   TRP A CD2 1 
ATOM   1963 N  NE1 . TRP B 1 34  ? 22.49364  -34.28755 16.80111  1.000 54.43785  ? 33   TRP A NE1 1 
ATOM   1964 C  CE2 . TRP B 1 34  ? 21.18177  -34.03018 17.10901  1.000 53.98335  ? 33   TRP A CE2 1 
ATOM   1965 C  CE3 . TRP B 1 34  ? 19.00605  -34.34877 16.10427  1.000 53.33013  ? 33   TRP A CE3 1 
ATOM   1966 C  CZ2 . TRP B 1 34  ? 20.62226  -33.44488 18.23797  1.000 54.96965  ? 33   TRP A CZ2 1 
ATOM   1967 C  CZ3 . TRP B 1 34  ? 18.45623  -33.75826 17.21459  1.000 52.96506  ? 33   TRP A CZ3 1 
ATOM   1968 C  CH2 . TRP B 1 34  ? 19.26062  -33.31452 18.26850  1.000 54.73843  ? 33   TRP A CH2 1 
ATOM   1969 N  N   . GLN B 1 35  ? 20.65332  -38.25592 12.20878  1.000 52.56757  ? 34   GLN A N   1 
ATOM   1970 C  CA  . GLN B 1 35  ? 19.72344  -38.87903 11.28808  1.000 52.72465  ? 34   GLN A CA  1 
ATOM   1971 C  C   . GLN B 1 35  ? 18.31023  -38.64041 11.79795  1.000 53.03924  ? 34   GLN A C   1 
ATOM   1972 O  O   . GLN B 1 35  ? 18.06198  -38.64355 13.00971  1.000 55.03981  ? 34   GLN A O   1 
ATOM   1973 C  CB  . GLN B 1 35  ? 20.00090  -40.37300 11.13726  1.000 55.53246  ? 34   GLN A CB  1 
ATOM   1974 C  CG  . GLN B 1 35  ? 18.85638  -41.12483 10.46836  1.000 60.28568  ? 34   GLN A CG  1 
ATOM   1975 C  CD  . GLN B 1 35  ? 19.18126  -42.57747 10.14715  1.000 69.19856  ? 34   GLN A CD  1 
ATOM   1976 O  OE1 . GLN B 1 35  ? 20.12988  -42.87654 9.41466   1.000 69.36317  ? 34   GLN A OE1 1 
ATOM   1977 N  NE2 . GLN B 1 35  ? 18.37772  -43.48859 10.68485  1.000 65.66293  ? 34   GLN A NE2 1 
ATOM   1978 N  N   . ALA B 1 36  ? 17.39903  -38.39351 10.87057  1.000 51.00491  ? 35   ALA A N   1 
ATOM   1979 C  CA  . ALA B 1 36  ? 16.00746  -38.15492 11.18785  1.000 52.69967  ? 35   ALA A CA  1 
ATOM   1980 C  C   . ALA B 1 36  ? 15.13742  -39.02759 10.30605  1.000 54.72669  ? 35   ALA A C   1 
ATOM   1981 O  O   . ALA B 1 36  ? 15.55622  -39.49824 9.24695   1.000 52.60757  ? 35   ALA A O   1 
ATOM   1982 C  CB  . ALA B 1 36  ? 15.62063  -36.68921 10.99800  1.000 52.66320  ? 35   ALA A CB  1 
ATOM   1983 N  N   . THR B 1 37  ? 13.92347  -39.24954 10.78560  1.000 57.32271  ? 36   THR A N   1 
ATOM   1984 C  CA  . THR B 1 37  ? 12.90895  -40.02501 10.10016  1.000 57.88788  ? 36   THR A CA  1 
ATOM   1985 C  C   . THR B 1 37  ? 11.58602  -39.29791 10.24120  1.000 60.49444  ? 36   THR A C   1 
ATOM   1986 O  O   . THR B 1 37  ? 11.25365  -38.83414 11.33561  1.000 62.63583  ? 36   THR A O   1 
ATOM   1987 C  CB  . THR B 1 37  ? 12.81159  -41.43173 10.68277  1.000 58.30635  ? 36   THR A CB  1 
ATOM   1988 O  OG1 . THR B 1 37  ? 13.84989  -42.24924 10.12883  1.000 56.31886  ? 36   THR A OG1 1 
ATOM   1989 C  CG2 . THR B 1 37  ? 11.46440  -42.03192 10.39280  1.000 60.08873  ? 36   THR A CG2 1 
ATOM   1990 N  N   . ILE B 1 38  ? 10.85745  -39.14739 9.13838   1.000 57.94577  ? 37   ILE A N   1 
ATOM   1991 C  CA  . ILE B 1 38  ? 9.50826   -38.60163 9.20088   1.000 62.56435  ? 37   ILE A CA  1 
ATOM   1992 C  C   . ILE B 1 38  ? 8.57666   -39.58257 8.50170   1.000 63.97461  ? 37   ILE A C   1 
ATOM   1993 O  O   . ILE B 1 38  ? 8.94092   -40.20679 7.49808   1.000 62.52101  ? 37   ILE A O   1 
ATOM   1994 C  CB  . ILE B 1 38  ? 9.38006   -37.16855 8.62997   1.000 61.75987  ? 37   ILE A CB  1 
ATOM   1995 C  CG1 . ILE B 1 38  ? 9.26222   -37.15853 7.12248   1.000 60.69241  ? 37   ILE A CG1 1 
ATOM   1996 C  CG2 . ILE B 1 38  ? 10.54027  -36.29188 9.03219   1.000 58.14668  ? 37   ILE A CG2 1 
ATOM   1997 C  CD1 . ILE B 1 38  ? 9.20189   -35.75420 6.61141   1.000 61.46309  ? 37   ILE A CD1 1 
ATOM   1998 N  N   . MET B 1 39  ? 7.39834   -39.76836 9.08242   1.000 68.35011  ? 38   MET A N   1 
ATOM   1999 C  CA  . MET B 1 39  ? 6.38860   -40.65101 8.53183   1.000 69.85876  ? 38   MET A CA  1 
ATOM   2000 C  C   . MET B 1 39  ? 5.50325   -39.85477 7.58859   1.000 68.93979  ? 38   MET A C   1 
ATOM   2001 O  O   . MET B 1 39  ? 5.12930   -38.72119 7.89428   1.000 70.00299  ? 38   MET A O   1 
ATOM   2002 C  CB  . MET B 1 39  ? 5.54346   -41.23436 9.66266   1.000 76.24522  ? 38   MET A CB  1 
ATOM   2003 C  CG  . MET B 1 39  ? 6.36853   -41.69213 10.86175  1.000 84.85395  ? 38   MET A CG  1 
ATOM   2004 S  SD  . MET B 1 39  ? 5.38150   -42.35092 12.23018  1.000 94.23362  ? 38   MET A SD  1 
ATOM   2005 C  CE  . MET B 1 39  ? 4.72550   -43.83021 11.46340  1.000 98.91828  ? 38   MET A CE  1 
ATOM   2006 N  N   . GLY B 1 40  ? 5.19499   -40.43153 6.42646   1.000 68.43627  ? 39   GLY A N   1 
ATOM   2007 C  CA  . GLY B 1 40  ? 4.31413   -39.77029 5.48909   1.000 68.85280  ? 39   GLY A CA  1 
ATOM   2008 C  C   . GLY B 1 40  ? 2.97311   -39.46509 6.12564   1.000 71.45897  ? 39   GLY A C   1 
ATOM   2009 O  O   . GLY B 1 40  ? 2.24832   -40.37326 6.54748   1.000 74.14025  ? 39   GLY A O   1 
ATOM   2010 N  N   . PRO B 1 41  ? 2.62736   -38.18342 6.23904   1.000 71.91984  ? 40   PRO A N   1 
ATOM   2011 C  CA  . PRO B 1 41  ? 1.35165   -37.82534 6.87426   1.000 75.11825  ? 40   PRO A CA  1 
ATOM   2012 C  C   . PRO B 1 41  ? 0.14278   -38.39909 6.14031   1.000 77.11390  ? 40   PRO A C   1 
ATOM   2013 O  O   . PRO B 1 41  ? 0.09516   -38.41949 4.90925   1.000 76.09542  ? 40   PRO A O   1 
ATOM   2014 C  CB  . PRO B 1 41  ? 1.35817   -36.29023 6.84636   1.000 74.41988  ? 40   PRO A CB  1 
ATOM   2015 C  CG  . PRO B 1 41  ? 2.44664   -35.90347 5.88763   1.000 70.48439  ? 40   PRO A CG  1 
ATOM   2016 C  CD  . PRO B 1 41  ? 3.44755   -36.99864 5.93424   1.000 68.97366  ? 40   PRO A CD  1 
ATOM   2017 N  N   . ASN B 1 42  ? -0.84205  -38.88283 6.91765   1.000 81.38970  ? 41   ASN A N   1 
ATOM   2018 C  CA  . ASN B 1 42  ? -2.07414  -39.43281 6.34174   1.000 83.98533  ? 41   ASN A CA  1 
ATOM   2019 C  C   . ASN B 1 42  ? -2.81886  -38.37536 5.54487   1.000 81.14877  ? 41   ASN A C   1 
ATOM   2020 O  O   . ASN B 1 42  ? -3.67878  -38.69987 4.71590   1.000 78.04142  ? 41   ASN A O   1 
ATOM   2021 C  CB  . ASN B 1 42  ? -2.96641  -40.04229 7.42635   1.000 86.18817  ? 41   ASN A CB  1 
ATOM   2022 C  CG  . ASN B 1 42  ? -2.44177  -41.38261 7.91900   1.000 90.02838  ? 41   ASN A CG  1 
ATOM   2023 O  OD1 . ASN B 1 42  ? -1.44296  -41.44762 8.63643   1.000 91.12990  ? 41   ASN A OD1 1 
ATOM   2024 N  ND2 . ASN B 1 42  ? -3.10928  -42.46385 7.51833   1.000 91.16663  ? 41   ASN A ND2 1 
ATOM   2025 N  N   . ASP B 1 43  ? -2.46464  -37.11818 5.77459   1.000 81.83922  ? 42   ASP A N   1 
ATOM   2026 C  CA  . ASP B 1 43  ? -3.03226  -35.97812 5.08842   1.000 77.57169  ? 42   ASP A CA  1 
ATOM   2027 C  C   . ASP B 1 43  ? -2.53889  -35.84111 3.64653   1.000 77.48753  ? 42   ASP A C   1 
ATOM   2028 O  O   . ASP B 1 43  ? -3.20444  -35.18276 2.84047   1.000 77.22598  ? 42   ASP A O   1 
ATOM   2029 C  CB  . ASP B 1 43  ? -2.60980  -34.75585 5.89997   1.000 76.42016  ? 42   ASP A CB  1 
ATOM   2030 C  CG  . ASP B 1 43  ? -3.38165  -33.54335 5.57265   1.000 79.50550  ? 42   ASP A CG  1 
ATOM   2031 O  OD1 . ASP B 1 43  ? -4.26513  -33.60746 4.69766   1.000 85.10199  ? 42   ASP A OD1 1 
ATOM   2032 O  OD2 . ASP B 1 43  ? -3.03670  -32.49794 6.14583   1.000 90.94511  ? 42   ASP A OD2 1 
ATOM   2033 N  N   . SER B 1 44  ? -1.41762  -36.48705 3.29285   1.000 76.75351  ? 43   SER A N   1 
ATOM   2034 C  CA  . SER B 1 44  ? -0.76846  -36.37567 1.98528   1.000 73.76411  ? 43   SER A CA  1 
ATOM   2035 C  C   . SER B 1 44  ? -0.71517  -37.70103 1.22186   1.000 72.13829  ? 43   SER A C   1 
ATOM   2036 O  O   . SER B 1 44  ? -1.02588  -38.75781 1.79179   1.000 73.72155  ? 43   SER A O   1 
ATOM   2037 C  CB  . SER B 1 44  ? 0.64832   -35.84045 2.17348   1.000 70.79807  ? 43   SER A CB  1 
ATOM   2038 O  OG  . SER B 1 44  ? 1.41974   -36.79320 2.87985   1.000 68.40265  ? 43   SER A OG  1 
ATOM   2039 N  N   . PRO B 1 45  ? -0.30238  -37.68913 -0.05651  1.000 71.09043  ? 44   PRO A N   1 
ATOM   2040 C  CA  . PRO B 1 45  ? -0.06413  -38.95089 -0.78709  1.000 69.31359  ? 44   PRO A CA  1 
ATOM   2041 C  C   . PRO B 1 45  ? 1.20239   -39.69390 -0.37487  1.000 66.56380  ? 44   PRO A C   1 
ATOM   2042 O  O   . PRO B 1 45  ? 1.46742   -40.78522 -0.89629  1.000 65.46303  ? 44   PRO A O   1 
ATOM   2043 C  CB  . PRO B 1 45  ? 0.03140   -38.48775 -2.25210  1.000 69.73112  ? 44   PRO A CB  1 
ATOM   2044 C  CG  . PRO B 1 45  ? 0.46781   -37.07015 -2.16716  1.000 69.34730  ? 44   PRO A CG  1 
ATOM   2045 C  CD  . PRO B 1 45  ? -0.23914  -36.52407 -0.96323  1.000 71.44670  ? 44   PRO A CD  1 
ATOM   2046 N  N   . TYR B 1 46  ? 1.97763   -39.15500 0.55606   1.000 66.67150  ? 45   TYR A N   1 
ATOM   2047 C  CA  . TYR B 1 46  ? 3.15744   -39.81893 1.08321   1.000 65.11333  ? 45   TYR A CA  1 
ATOM   2048 C  C   . TYR B 1 46  ? 2.81205   -40.74081 2.24335   1.000 65.79915  ? 45   TYR A C   1 
ATOM   2049 O  O   . TYR B 1 46  ? 3.69944   -41.41125 2.78041   1.000 65.30523  ? 45   TYR A O   1 
ATOM   2050 C  CB  . TYR B 1 46  ? 4.18442   -38.76182 1.51814   1.000 62.76779  ? 45   TYR A CB  1 
ATOM   2051 C  CG  . TYR B 1 46  ? 4.38196   -37.66736 0.48258   1.000 62.09344  ? 45   TYR A CG  1 
ATOM   2052 C  CD1 . TYR B 1 46  ? 5.15248   -37.89158 -0.65549  1.000 60.93351  ? 45   TYR A CD1 1 
ATOM   2053 C  CD2 . TYR B 1 46  ? 3.77607   -36.42183 0.62817   1.000 63.11151  ? 45   TYR A CD2 1 
ATOM   2054 C  CE1 . TYR B 1 46  ? 5.32353   -36.90293 -1.61102  1.000 59.34226  ? 45   TYR A CE1 1 
ATOM   2055 C  CE2 . TYR B 1 46  ? 3.93944   -35.43198 -0.31721  1.000 63.08021  ? 45   TYR A CE2 1 
ATOM   2056 C  CZ  . TYR B 1 46  ? 4.71477   -35.67471 -1.43715  1.000 62.26175  ? 45   TYR A CZ  1 
ATOM   2057 O  OH  . TYR B 1 46  ? 4.87971   -34.68283 -2.38119  1.000 61.09429  ? 45   TYR A OH  1 
ATOM   2058 N  N   . GLN B 1 47  ? 1.53251   -40.80784 2.60023   1.000 67.91280  ? 46   GLN A N   1 
ATOM   2059 C  CA  . GLN B 1 47  ? 1.05747   -41.64798 3.68961   1.000 71.43500  ? 46   GLN A CA  1 
ATOM   2060 C  C   . GLN B 1 47  ? 1.44604   -43.10875 3.48569   1.000 67.80645  ? 46   GLN A C   1 
ATOM   2061 O  O   . GLN B 1 47  ? 1.25350   -43.67891 2.40957   1.000 66.98587  ? 46   GLN A O   1 
ATOM   2062 C  CB  . GLN B 1 47  ? -0.45881  -41.50353 3.78641   1.000 76.21829  ? 46   GLN A CB  1 
ATOM   2063 C  CG  . GLN B 1 47  ? -1.16290  -42.60956 4.49789   1.000 79.99076  ? 46   GLN A CG  1 
ATOM   2064 C  CD  . GLN B 1 47  ? -2.62400  -42.65107 4.12897   1.000 88.88628  ? 46   GLN A CD  1 
ATOM   2065 O  OE1 . GLN B 1 47  ? -3.41161  -41.80863 4.56596   1.000 95.61666  ? 46   GLN A OE1 1 
ATOM   2066 N  NE2 . GLN B 1 47  ? -2.99715  -43.61846 3.29904   1.000 93.54876  ? 46   GLN A NE2 1 
ATOM   2067 N  N   . GLY B 1 48  ? 1.99623   -43.71155 4.52862   1.000 66.92520  ? 47   GLY A N   1 
ATOM   2068 C  CA  . GLY B 1 48  ? 2.46040   -45.07271 4.48648   1.000 63.30217  ? 47   GLY A CA  1 
ATOM   2069 C  C   . GLY B 1 48  ? 3.95713   -45.21249 4.35622   1.000 63.46830  ? 47   GLY A C   1 
ATOM   2070 O  O   . GLY B 1 48  ? 4.49875   -46.26760 4.69327   1.000 64.98012  ? 47   GLY A O   1 
ATOM   2071 N  N   . GLY B 1 49  ? 4.63973   -44.16844 3.92101   1.000 62.97485  ? 48   GLY A N   1 
ATOM   2072 C  CA  . GLY B 1 49  ? 6.06802   -44.21908 3.72883   1.000 61.46851  ? 48   GLY A CA  1 
ATOM   2073 C  C   . GLY B 1 49  ? 6.84468   -43.68545 4.91598   1.000 60.85402  ? 48   GLY A C   1 
ATOM   2074 O  O   . GLY B 1 49  ? 6.34284   -42.89851 5.71988   1.000 62.55145  ? 48   GLY A O   1 
ATOM   2075 N  N   . VAL B 1 50  ? 8.08623   -44.14724 5.02746   1.000 59.56271  ? 49   VAL A N   1 
ATOM   2076 C  CA  . VAL B 1 50  ? 9.02463   -43.66099 6.03183   1.000 58.66662  ? 49   VAL A CA  1 
ATOM   2077 C  C   . VAL B 1 50  ? 10.21292  -43.04013 5.29927   1.000 57.17332  ? 49   VAL A C   1 
ATOM   2078 O  O   . VAL B 1 50  ? 10.88625  -43.71466 4.50610   1.000 57.26438  ? 49   VAL A O   1 
ATOM   2079 C  CB  . VAL B 1 50  ? 9.48035   -44.77676 6.98520   1.000 58.24801  ? 49   VAL A CB  1 
ATOM   2080 C  CG1 . VAL B 1 50  ? 9.98746   -46.01205 6.21026   1.000 59.60214  ? 49   VAL A CG1 1 
ATOM   2081 C  CG2 . VAL B 1 50  ? 10.55461  -44.23635 7.91447   1.000 55.30288  ? 49   VAL A CG2 1 
ATOM   2082 N  N   . PHE B 1 51  ? 10.48021  -41.76428 5.56518   1.000 55.48013  ? 50   PHE A N   1 
ATOM   2083 C  CA  . PHE B 1 51  ? 11.48878  -41.01649 4.83057   1.000 53.07429  ? 50   PHE A CA  1 
ATOM   2084 C  C   . PHE B 1 51  ? 12.64628  -40.68518 5.75436   1.000 52.31573  ? 50   PHE A C   1 
ATOM   2085 O  O   . PHE B 1 51  ? 12.43436  -40.24585 6.88995   1.000 55.21731  ? 50   PHE A O   1 
ATOM   2086 C  CB  . PHE B 1 51  ? 10.89479  -39.73755 4.23745   1.000 53.20564  ? 50   PHE A CB  1 
ATOM   2087 C  CG  . PHE B 1 51  ? 9.66795   -39.97015 3.39254   1.000 54.88322  ? 50   PHE A CG  1 
ATOM   2088 C  CD1 . PHE B 1 51  ? 8.40086   -39.98770 3.96691   1.000 56.59861  ? 50   PHE A CD1 1 
ATOM   2089 C  CD2 . PHE B 1 51  ? 9.77932   -40.16820 2.02578   1.000 52.67082  ? 50   PHE A CD2 1 
ATOM   2090 C  CE1 . PHE B 1 51  ? 7.27575   -40.20485 3.19280   1.000 58.12535  ? 50   PHE A CE1 1 
ATOM   2091 C  CE2 . PHE B 1 51  ? 8.66078   -40.38067 1.24596   1.000 54.80945  ? 50   PHE A CE2 1 
ATOM   2092 C  CZ  . PHE B 1 51  ? 7.40896   -40.40397 1.82701   1.000 57.93894  ? 50   PHE A CZ  1 
ATOM   2093 N  N   . PHE B 1 52  ? 13.86107  -40.92348 5.28082   1.000 50.26623  ? 51   PHE A N   1 
ATOM   2094 C  CA  . PHE B 1 52  ? 15.05273  -40.61919 6.05247   1.000 49.73494  ? 51   PHE A CA  1 
ATOM   2095 C  C   . PHE B 1 52  ? 15.65390  -39.29079 5.62775   1.000 49.63831  ? 51   PHE A C   1 
ATOM   2096 O  O   . PHE B 1 52  ? 15.53236  -38.86705 4.47657   1.000 48.86893  ? 51   PHE A O   1 
ATOM   2097 C  CB  . PHE B 1 52  ? 16.09467  -41.72823 5.92681   1.000 49.48456  ? 51   PHE A CB  1 
ATOM   2098 C  CG  . PHE B 1 52  ? 15.66821  -43.01281 6.57321   1.000 51.52785  ? 51   PHE A CG  1 
ATOM   2099 C  CD1 . PHE B 1 52  ? 14.84196  -43.90095 5.90062   1.000 52.14618  ? 51   PHE A CD1 1 
ATOM   2100 C  CD2 . PHE B 1 52  ? 16.05076  -43.31308 7.87313   1.000 54.66583  ? 51   PHE A CD2 1 
ATOM   2101 C  CE1 . PHE B 1 52  ? 14.42470  -45.08264 6.49919   1.000 53.79443  ? 51   PHE A CE1 1 
ATOM   2102 C  CE2 . PHE B 1 52  ? 15.63581  -44.49524 8.47764   1.000 53.21378  ? 51   PHE A CE2 1 
ATOM   2103 C  CZ  . PHE B 1 52  ? 14.82121  -45.38006 7.78636   1.000 52.41791  ? 51   PHE A CZ  1 
ATOM   2104 N  N   . LEU B 1 53  ? 16.27297  -38.61991 6.59680   1.000 48.97235  ? 52   LEU A N   1 
ATOM   2105 C  CA  . LEU B 1 53  ? 16.93284  -37.34694 6.38043   1.000 47.76164  ? 52   LEU A CA  1 
ATOM   2106 C  C   . LEU B 1 53  ? 18.24194  -37.33371 7.15494   1.000 46.99872  ? 52   LEU A C   1 
ATOM   2107 O  O   . LEU B 1 53  ? 18.40565  -38.02962 8.16161   1.000 47.20560  ? 52   LEU A O   1 
ATOM   2108 C  CB  . LEU B 1 53  ? 16.04635  -36.16160 6.80321   1.000 48.50989  ? 52   LEU A CB  1 
ATOM   2109 C  CG  . LEU B 1 53  ? 14.67918  -35.94637 6.14559   1.000 49.12527  ? 52   LEU A CG  1 
ATOM   2110 C  CD1 . LEU B 1 53  ? 13.62838  -36.77750 6.83836   1.000 52.68931  ? 52   LEU A CD1 1 
ATOM   2111 C  CD2 . LEU B 1 53  ? 14.28660  -34.46947 6.19413   1.000 47.71630  ? 52   LEU A CD2 1 
ATOM   2112 N  N   . THR B 1 54  ? 19.16607  -36.51698 6.66512   1.000 44.99900  ? 53   THR A N   1 
ATOM   2113 C  CA  . THR B 1 54  ? 20.38256  -36.15679 7.37105   1.000 45.86667  ? 53   THR A CA  1 
ATOM   2114 C  C   . THR B 1 54  ? 20.23059  -34.73427 7.88909   1.000 46.14164  ? 53   THR A C   1 
ATOM   2115 O  O   . THR B 1 54  ? 19.56790  -33.89600 7.25271   1.000 45.27945  ? 53   THR A O   1 
ATOM   2116 C  CB  . THR B 1 54  ? 21.63542  -36.24671 6.47914   1.000 47.52467  ? 53   THR A CB  1 
ATOM   2117 O  OG1 . THR B 1 54  ? 21.54783  -35.29462 5.40372   1.000 50.82879  ? 53   THR A OG1 1 
ATOM   2118 C  CG2 . THR B 1 54  ? 21.84553  -37.66229 5.92215   1.000 47.33206  ? 53   THR A CG2 1 
ATOM   2119 N  N   . ILE B 1 55  ? 20.77698  -34.49861 9.08334   1.000 47.46806  ? 54   ILE A N   1 
ATOM   2120 C  CA  . ILE B 1 55  ? 20.81602  -33.18281 9.70777   1.000 46.43918  ? 54   ILE A CA  1 
ATOM   2121 C  C   . ILE B 1 55  ? 22.26490  -32.83657 9.99270   1.000 48.04209  ? 54   ILE A C   1 
ATOM   2122 O  O   . ILE B 1 55  ? 22.99030  -33.63463 10.59184  1.000 49.65175  ? 54   ILE A O   1 
ATOM   2123 C  CB  . ILE B 1 55  ? 19.98770  -33.12660 10.99857  1.000 46.73932  ? 54   ILE A CB  1 
ATOM   2124 C  CG1 . ILE B 1 55  ? 18.53369  -33.44880 10.70346  1.000 45.17919  ? 54   ILE A CG1 1 
ATOM   2125 C  CG2 . ILE B 1 55  ? 20.10935  -31.75588 11.66391  1.000 46.26031  ? 54   ILE A CG2 1 
ATOM   2126 C  CD1 . ILE B 1 55  ? 17.73403  -33.57176 11.95704  1.000 47.55861  ? 54   ILE A CD1 1 
ATOM   2127 N  N   . HIS B 1 56  ? 22.64670  -31.61475 9.64058   1.000 49.18539  ? 55   HIS A N   1 
ATOM   2128 C  CA  . HIS B 1 56  ? 23.99616  -31.09373 9.78302   1.000 55.05755  ? 55   HIS A CA  1 
ATOM   2129 C  C   . HIS B 1 56  ? 23.91975  -29.80226 10.58215  1.000 52.57321  ? 55   HIS A C   1 
ATOM   2130 O  O   . HIS B 1 56  ? 23.30049  -28.84246 10.12656  1.000 49.06233  ? 55   HIS A O   1 
ATOM   2131 C  CB  . HIS B 1 56  ? 24.56734  -30.81126 8.39102   1.000 58.44512  ? 55   HIS A CB  1 
ATOM   2132 C  CG  . HIS B 1 56  ? 26.04623  -30.58533 8.36227   1.000 65.38155  ? 55   HIS A CG  1 
ATOM   2133 N  ND1 . HIS B 1 56  ? 26.88217  -30.96790 9.38866   1.000 72.98196  ? 55   HIS A ND1 1 
ATOM   2134 C  CD2 . HIS B 1 56  ? 26.84059  -30.04230 7.40785   1.000 70.41566  ? 55   HIS A CD2 1 
ATOM   2135 C  CE1 . HIS B 1 56  ? 28.12742  -30.66686 9.06387   1.000 74.76085  ? 55   HIS A CE1 1 
ATOM   2136 N  NE2 . HIS B 1 56  ? 28.12889  -30.11256 7.86477   1.000 70.86964  ? 55   HIS A NE2 1 
ATOM   2137 N  N   . PHE B 1 57  ? 24.52102  -29.77566 11.76002  1.000 52.39608  ? 56   PHE A N   1 
ATOM   2138 C  CA  . PHE B 1 57  ? 24.51334  -28.54274 12.54416  1.000 51.51934  ? 56   PHE A CA  1 
ATOM   2139 C  C   . PHE B 1 57  ? 25.78276  -27.75843 12.26580  1.000 52.67151  ? 56   PHE A C   1 
ATOM   2140 O  O   . PHE B 1 57  ? 26.88002  -28.30890 12.41725  1.000 52.82313  ? 56   PHE A O   1 
ATOM   2141 C  CB  . PHE B 1 57  ? 24.42907  -28.82974 14.03760  1.000 51.69959  ? 56   PHE A CB  1 
ATOM   2142 C  CG  . PHE B 1 57  ? 23.14083  -29.45726 14.46333  1.000 51.32863  ? 56   PHE A CG  1 
ATOM   2143 C  CD1 . PHE B 1 57  ? 22.95341  -30.81910 14.34018  1.000 50.37598  ? 56   PHE A CD1 1 
ATOM   2144 C  CD2 . PHE B 1 57  ? 22.11974  -28.68781 14.99424  1.000 48.86980  ? 56   PHE A CD2 1 
ATOM   2145 C  CE1 . PHE B 1 57  ? 21.76715  -31.40611 14.73466  1.000 50.50652  ? 56   PHE A CE1 1 
ATOM   2146 C  CE2 . PHE B 1 57  ? 20.93250  -29.26979 15.39804  1.000 47.77163  ? 56   PHE A CE2 1 
ATOM   2147 C  CZ  . PHE B 1 57  ? 20.75733  -30.63260 15.26168  1.000 49.96972  ? 56   PHE A CZ  1 
ATOM   2148 N  N   . PRO B 1 58  ? 25.69476  -26.48991 11.86760  1.000 52.60834  ? 57   PRO A N   1 
ATOM   2149 C  CA  . PRO B 1 58  ? 26.91061  -25.68166 11.73524  1.000 51.15648  ? 57   PRO A CA  1 
ATOM   2150 C  C   . PRO B 1 58  ? 27.54381  -25.44454 13.10070  1.000 53.73713  ? 57   PRO A C   1 
ATOM   2151 O  O   . PRO B 1 58  ? 26.91489  -25.59973 14.15416  1.000 54.58536  ? 57   PRO A O   1 
ATOM   2152 C  CB  . PRO B 1 58  ? 26.40931  -24.38161 11.10261  1.000 51.85034  ? 57   PRO A CB  1 
ATOM   2153 C  CG  . PRO B 1 58  ? 24.96409  -24.32680 11.45512  1.000 51.57515  ? 57   PRO A CG  1 
ATOM   2154 C  CD  . PRO B 1 58  ? 24.49465  -25.75035 11.44161  1.000 50.78345  ? 57   PRO A CD  1 
ATOM   2155 N  N   . THR B 1 59  ? 28.82825  -25.08979 13.07413  1.000 53.76783  ? 58   THR A N   1 
ATOM   2156 C  CA  . THR B 1 59  ? 29.56929  -24.96655 14.32374  1.000 54.57384  ? 58   THR A CA  1 
ATOM   2157 C  C   . THR B 1 59  ? 29.01976  -23.85240 15.20775  1.000 55.92316  ? 58   THR A C   1 
ATOM   2158 O  O   . THR B 1 59  ? 29.20621  -23.89043 16.42975  1.000 56.04139  ? 58   THR A O   1 
ATOM   2159 C  CB  . THR B 1 59  ? 31.04831  -24.73135 14.03225  1.000 52.98840  ? 58   THR A CB  1 
ATOM   2160 O  OG1 . THR B 1 59  ? 31.21934  -23.39467 13.54825  1.000 59.72563  ? 58   THR A OG1 1 
ATOM   2161 C  CG2 . THR B 1 59  ? 31.52825  -25.70568 12.98081  1.000 51.92916  ? 58   THR A CG2 1 
ATOM   2162 N  N   . ASP B 1 60  ? 28.35772  -22.85346 14.61279  1.000 57.20398  ? 59   ASP A N   1 
ATOM   2163 C  CA  . ASP B 1 60  ? 27.76039  -21.73012 15.33319  1.000 58.15204  ? 59   ASP A CA  1 
ATOM   2164 C  C   . ASP B 1 60  ? 26.23746  -21.79437 15.29714  1.000 55.96194  ? 59   ASP A C   1 
ATOM   2165 O  O   . ASP B 1 60  ? 25.54978  -20.77716 15.17436  1.000 57.56968  ? 59   ASP A O   1 
ATOM   2166 C  CB  . ASP B 1 60  ? 28.23635  -20.38645 14.78420  1.000 62.96804  ? 59   ASP A CB  1 
ATOM   2167 C  CG  . ASP B 1 60  ? 27.90869  -20.19580 13.31461  1.000 63.55393  ? 59   ASP A CG  1 
ATOM   2168 O  OD1 . ASP B 1 60  ? 27.97724  -21.16907 12.53264  1.000 60.35141  ? 59   ASP A OD1 1 
ATOM   2169 O  OD2 . ASP B 1 60  ? 27.57893  -19.05334 12.94484  1.000 71.42440  ? 59   ASP A OD2 1 
ATOM   2170 N  N   . TYR B 1 61  ? 25.70803  -23.00712 15.35321  1.000 55.61993  ? 60   TYR A N   1 
ATOM   2171 C  CA  . TYR B 1 61  ? 24.29473  -23.20851 15.59441  1.000 53.71360  ? 60   TYR A CA  1 
ATOM   2172 C  C   . TYR B 1 61  ? 23.95804  -22.63700 16.97336  1.000 55.35078  ? 60   TYR A C   1 
ATOM   2173 O  O   . TYR B 1 61  ? 24.78427  -22.70493 17.88810  1.000 56.60529  ? 60   TYR A O   1 
ATOM   2174 C  CB  . TYR B 1 61  ? 24.00224  -24.70432 15.51387  1.000 51.69990  ? 60   TYR A CB  1 
ATOM   2175 C  CG  . TYR B 1 61  ? 22.58562  -25.15430 15.72725  1.000 48.82002  ? 60   TYR A CG  1 
ATOM   2176 C  CD1 . TYR B 1 61  ? 21.63648  -25.06691 14.71254  1.000 44.61347  ? 60   TYR A CD1 1 
ATOM   2177 C  CD2 . TYR B 1 61  ? 22.21350  -25.72836 16.93173  1.000 50.00792  ? 60   TYR A CD2 1 
ATOM   2178 C  CE1 . TYR B 1 61  ? 20.34428  -25.50819 14.91657  1.000 46.72724  ? 60   TYR A CE1 1 
ATOM   2179 C  CE2 . TYR B 1 61  ? 20.94061  -26.17395 17.14487  1.000 49.62819  ? 60   TYR A CE2 1 
ATOM   2180 C  CZ  . TYR B 1 61  ? 20.00428  -26.06592 16.14832  1.000 48.17645  ? 60   TYR A CZ  1 
ATOM   2181 O  OH  . TYR B 1 61  ? 18.73894  -26.53872 16.41796  1.000 44.86283  ? 60   TYR A OH  1 
ATOM   2182 N  N   . PRO B 1 62  ? 22.74816  -22.06562 17.16117  1.000 55.33363  ? 61   PRO A N   1 
ATOM   2183 C  CA  . PRO B 1 62  ? 21.61604  -21.97876 16.23742  1.000 53.24286  ? 61   PRO A CA  1 
ATOM   2184 C  C   . PRO B 1 62  ? 21.51658  -20.65732 15.49005  1.000 54.69627  ? 61   PRO A C   1 
ATOM   2185 O  O   . PRO B 1 62  ? 20.48872  -20.39223 14.86309  1.000 54.42438  ? 61   PRO A O   1 
ATOM   2186 C  CB  . PRO B 1 62  ? 20.42752  -22.14386 17.18410  1.000 52.74266  ? 61   PRO A CB  1 
ATOM   2187 C  CG  . PRO B 1 62  ? 20.87300  -21.32556 18.39078  1.000 56.09328  ? 61   PRO A CG  1 
ATOM   2188 C  CD  . PRO B 1 62  ? 22.38099  -21.50411 18.47661  1.000 55.44386  ? 61   PRO A CD  1 
ATOM   2189 N  N   . PHE B 1 63  ? 22.56078  -19.82119 15.53748  1.000 56.15449  ? 62   PHE A N   1 
ATOM   2190 C  CA  . PHE B 1 63  ? 22.53995  -18.55035 14.81636  1.000 57.31741  ? 62   PHE A CA  1 
ATOM   2191 C  C   . PHE B 1 63  ? 22.63028  -18.74165 13.30930  1.000 57.97165  ? 62   PHE A C   1 
ATOM   2192 O  O   . PHE B 1 63  ? 22.24143  -17.84082 12.55884  1.000 56.00561  ? 62   PHE A O   1 
ATOM   2193 C  CB  . PHE B 1 63  ? 23.66126  -17.64530 15.32722  1.000 59.62191  ? 62   PHE A CB  1 
ATOM   2194 C  CG  . PHE B 1 63  ? 23.56465  -17.35633 16.79742  1.000 63.61575  ? 62   PHE A CG  1 
ATOM   2195 C  CD1 . PHE B 1 63  ? 22.66025  -16.41758 17.27147  1.000 66.15760  ? 62   PHE A CD1 1 
ATOM   2196 C  CD2 . PHE B 1 63  ? 24.34521  -18.05098 17.70961  1.000 66.51189  ? 62   PHE A CD2 1 
ATOM   2197 C  CE1 . PHE B 1 63  ? 22.55105  -16.15371 18.62742  1.000 65.93389  ? 62   PHE A CE1 1 
ATOM   2198 C  CE2 . PHE B 1 63  ? 24.23951  -17.79506 19.06497  1.000 69.57252  ? 62   PHE A CE2 1 
ATOM   2199 C  CZ  . PHE B 1 63  ? 23.34152  -16.84329 19.52442  1.000 70.17260  ? 62   PHE A CZ  1 
ATOM   2200 N  N   . LYS B 1 64  ? 23.09805  -19.90548 12.85527  1.000 56.68267  ? 63   LYS A N   1 
ATOM   2201 C  CA  . LYS B 1 64  ? 22.93785  -20.33078 11.47665  1.000 60.10110  ? 63   LYS A CA  1 
ATOM   2202 C  C   . LYS B 1 64  ? 22.10064  -21.59455 11.42151  1.000 53.21153  ? 63   LYS A C   1 
ATOM   2203 O  O   . LYS B 1 64  ? 22.18421  -22.43741 12.32250  1.000 53.13244  ? 63   LYS A O   1 
ATOM   2204 C  CB  . LYS B 1 64  ? 24.27148  -20.57046 10.77502  1.000 58.38759  ? 63   LYS A CB  1 
ATOM   2205 C  CG  . LYS B 1 64  ? 24.62854  -19.36875 9.93729   1.000 61.14200  ? 63   LYS A CG  1 
ATOM   2206 C  CD  . LYS B 1 64  ? 25.95873  -18.80223 10.31271  1.000 66.27350  ? 63   LYS A CD  1 
ATOM   2207 C  CE  . LYS B 1 64  ? 27.08860  -19.69735 9.84705   1.000 73.77098  ? 63   LYS A CE  1 
ATOM   2208 N  NZ  . LYS B 1 64  ? 28.39047  -19.00685 10.06137  1.000 77.30721  ? 63   LYS A NZ  1 
ATOM   2209 N  N   . PRO B 1 65  ? 21.27209  -21.74404 10.39661  1.000 51.19599  ? 64   PRO A N   1 
ATOM   2210 C  CA  . PRO B 1 65  ? 20.34267  -22.86001 10.36146  1.000 50.46028  ? 64   PRO A CA  1 
ATOM   2211 C  C   . PRO B 1 65  ? 21.07640  -24.17864 10.19503  1.000 49.40936  ? 64   PRO A C   1 
ATOM   2212 O  O   . PRO B 1 65  ? 22.23349  -24.21738 9.74359   1.000 48.41131  ? 64   PRO A O   1 
ATOM   2213 C  CB  . PRO B 1 65  ? 19.47805  -22.55737 9.12505   1.000 49.91494  ? 64   PRO A CB  1 
ATOM   2214 C  CG  . PRO B 1 65  ? 20.37834  -21.80093 8.23979   1.000 50.33318  ? 64   PRO A CG  1 
ATOM   2215 C  CD  . PRO B 1 65  ? 21.23254  -20.95573 9.15252   1.000 52.37367  ? 64   PRO A CD  1 
ATOM   2216 N  N   . PRO B 1 66  ? 20.44793  -25.28449 10.56424  1.000 46.85258  ? 65   PRO A N   1 
ATOM   2217 C  CA  . PRO B 1 66  ? 21.01446  -26.58551 10.21866  1.000 48.60566  ? 65   PRO A CA  1 
ATOM   2218 C  C   . PRO B 1 66  ? 20.71615  -26.89470 8.75843   1.000 46.76056  ? 65   PRO A C   1 
ATOM   2219 O  O   . PRO B 1 66  ? 19.74189  -26.40474 8.18009   1.000 45.53439  ? 65   PRO A O   1 
ATOM   2220 C  CB  . PRO B 1 66  ? 20.27356  -27.54485 11.15496  1.000 47.18058  ? 65   PRO A CB  1 
ATOM   2221 C  CG  . PRO B 1 66  ? 18.91564  -26.91373 11.27476  1.000 44.74982  ? 65   PRO A CG  1 
ATOM   2222 C  CD  . PRO B 1 66  ? 19.18279  -25.41419 11.30887  1.000 45.43372  ? 65   PRO A CD  1 
ATOM   2223 N  N   . LYS B 1 67  ? 21.58331  -27.70931 8.15675   1.000 48.24120  ? 66   LYS A N   1 
ATOM   2224 C  CA  . LYS B 1 67  ? 21.40245  -28.17555 6.78374   1.000 48.83662  ? 66   LYS A CA  1 
ATOM   2225 C  C   . LYS B 1 67  ? 20.69882  -29.52880 6.83487   1.000 47.55358  ? 66   LYS A C   1 
ATOM   2226 O  O   . LYS B 1 67  ? 21.25675  -30.51320 7.33062   1.000 48.81311  ? 66   LYS A O   1 
ATOM   2227 C  CB  . LYS B 1 67  ? 22.74318  -28.23802 6.04621   1.000 50.93579  ? 66   LYS A CB  1 
ATOM   2228 C  CG  . LYS B 1 67  ? 22.62963  -28.63612 4.55839   1.000 55.10048  ? 66   LYS A CG  1 
ATOM   2229 C  CD  . LYS B 1 67  ? 23.98386  -28.64014 3.80537   1.000 63.45456  ? 66   LYS A CD  1 
ATOM   2230 C  CE  . LYS B 1 67  ? 24.96209  -29.69283 4.32345   1.000 67.17729  ? 66   LYS A CE  1 
ATOM   2231 N  NZ  . LYS B 1 67  ? 26.20647  -29.78196 3.50241   1.000 70.31384  ? 66   LYS A NZ  1 
ATOM   2232 N  N   . VAL B 1 68  ? 19.46974  -29.57356 6.33746   1.000 44.06009  ? 67   VAL A N   1 
ATOM   2233 C  CA  . VAL B 1 68  ? 18.63902  -30.76589 6.39107   1.000 46.21976  ? 67   VAL A CA  1 
ATOM   2234 C  C   . VAL B 1 68  ? 18.37191  -31.22258 4.96986   1.000 46.24052  ? 67   VAL A C   1 
ATOM   2235 O  O   . VAL B 1 68  ? 18.00001  -30.41188 4.11129   1.000 47.69458  ? 67   VAL A O   1 
ATOM   2236 C  CB  . VAL B 1 68  ? 17.31306  -30.51118 7.12421   1.000 45.71617  ? 67   VAL A CB  1 
ATOM   2237 C  CG1 . VAL B 1 68  ? 16.49834  -31.79396 7.18863   1.000 44.95257  ? 67   VAL A CG1 1 
ATOM   2238 C  CG2 . VAL B 1 68  ? 17.58859  -29.96014 8.51660   1.000 45.52589  ? 67   VAL A CG2 1 
ATOM   2239 N  N   . ALA B 1 69  ? 18.52942  -32.52331 4.73042   1.000 45.30730  ? 68   ALA A N   1 
ATOM   2240 C  CA  . ALA B 1 69  ? 18.26055  -33.03770 3.39758   1.000 46.42852  ? 68   ALA A CA  1 
ATOM   2241 C  C   . ALA B 1 69  ? 17.67527  -34.43542 3.49956   1.000 46.56685  ? 68   ALA A C   1 
ATOM   2242 O  O   . ALA B 1 69  ? 17.97770  -35.18598 4.42825   1.000 45.77844  ? 68   ALA A O   1 
ATOM   2243 C  CB  . ALA B 1 69  ? 19.52630  -33.04467 2.52638   1.000 46.98992  ? 68   ALA A CB  1 
ATOM   2244 N  N   . PHE B 1 70  ? 16.80914  -34.75827 2.54145   1.000 46.26316  ? 69   PHE A N   1 
ATOM   2245 C  CA  . PHE B 1 70  ? 16.27321  -36.10548 2.40397   1.000 47.85466  ? 69   PHE A CA  1 
ATOM   2246 C  C   . PHE B 1 70  ? 17.32922  -37.03597 1.81959   1.000 46.89664  ? 69   PHE A C   1 
ATOM   2247 O  O   . PHE B 1 70  ? 18.11278  -36.64559 0.94844   1.000 47.98385  ? 69   PHE A O   1 
ATOM   2248 C  CB  . PHE B 1 70  ? 15.04193  -36.09846 1.49001   1.000 47.42339  ? 69   PHE A CB  1 
ATOM   2249 C  CG  . PHE B 1 70  ? 13.75171  -35.68307 2.17096   1.000 46.75841  ? 69   PHE A CG  1 
ATOM   2250 C  CD1 . PHE B 1 70  ? 13.46681  -34.34231 2.39523   1.000 48.20143  ? 69   PHE A CD1 1 
ATOM   2251 C  CD2 . PHE B 1 70  ? 12.80601  -36.63060 2.54113   1.000 46.84151  ? 69   PHE A CD2 1 
ATOM   2252 C  CE1 . PHE B 1 70  ? 12.27474  -33.95558 3.01705   1.000 48.73291  ? 69   PHE A CE1 1 
ATOM   2253 C  CE2 . PHE B 1 70  ? 11.61655  -36.25326 3.15284   1.000 49.61076  ? 69   PHE A CE2 1 
ATOM   2254 C  CZ  . PHE B 1 70  ? 11.35208  -34.91476 3.39409   1.000 49.65047  ? 69   PHE A CZ  1 
ATOM   2255 N  N   . THR B 1 71  ? 17.34797  -38.27991 2.29143   1.000 47.55227  ? 70   THR A N   1 
ATOM   2256 C  CA  . THR B 1 71  ? 18.10121  -39.31788 1.60633   1.000 47.30309  ? 70   THR A CA  1 
ATOM   2257 C  C   . THR B 1 71  ? 17.19019  -40.30855 0.90332   1.000 48.62828  ? 70   THR A C   1 
ATOM   2258 O  O   . THR B 1 71  ? 17.65997  -41.05058 0.03650   1.000 52.40451  ? 70   THR A O   1 
ATOM   2259 C  CB  . THR B 1 71  ? 19.02998  -40.06313 2.57965   1.000 47.30139  ? 70   THR A CB  1 
ATOM   2260 O  OG1 . THR B 1 71  ? 18.28346  -40.52654 3.70379   1.000 48.00856  ? 70   THR A OG1 1 
ATOM   2261 C  CG2 . THR B 1 71  ? 20.11909  -39.12832 3.07895   1.000 46.82277  ? 70   THR A CG2 1 
ATOM   2262 N  N   . THR B 1 72  ? 15.89294  -40.26473 1.17798   1.000 47.88941  ? 71   THR A N   1 
ATOM   2263 C  CA  . THR B 1 72  ? 14.90826  -41.09119 0.50081   1.000 48.48942  ? 71   THR A CA  1 
ATOM   2264 C  C   . THR B 1 72  ? 14.29043  -40.28735 -0.63586  1.000 49.14756  ? 71   THR A C   1 
ATOM   2265 O  O   . THR B 1 72  ? 13.82853  -39.16666 -0.41169  1.000 48.52695  ? 71   THR A O   1 
ATOM   2266 C  CB  . THR B 1 72  ? 13.82289  -41.51862 1.49530   1.000 48.85648  ? 71   THR A CB  1 
ATOM   2267 O  OG1 . THR B 1 72  ? 14.41649  -42.26381 2.55950   1.000 49.45447  ? 71   THR A OG1 1 
ATOM   2268 C  CG2 . THR B 1 72  ? 12.75346  -42.37141 0.82261   1.000 50.84281  ? 71   THR A CG2 1 
ATOM   2269 N  N   . ARG B 1 73  ? 14.28043  -40.85167 -1.84335  1.000 49.66769  ? 72   ARG A N   1 
ATOM   2270 C  CA  . ARG B 1 73  ? 13.62629  -40.18882 -2.97085  1.000 51.50543  ? 72   ARG A CA  1 
ATOM   2271 C  C   . ARG B 1 73  ? 12.16881  -39.89856 -2.65927  1.000 51.60958  ? 72   ARG A C   1 
ATOM   2272 O  O   . ARG B 1 73  ? 11.47241  -40.72660 -2.07228  1.000 49.16050  ? 72   ARG A O   1 
ATOM   2273 C  CB  . ARG B 1 73  ? 13.65497  -41.05254 -4.22787  1.000 53.65165  ? 72   ARG A CB  1 
ATOM   2274 C  CG  . ARG B 1 73  ? 14.94245  -41.11983 -4.96819  1.000 57.98305  ? 72   ARG A CG  1 
ATOM   2275 C  CD  . ARG B 1 73  ? 15.02446  -39.91833 -5.86746  1.000 61.78392  ? 72   ARG A CD  1 
ATOM   2276 N  NE  . ARG B 1 73  ? 16.16044  -40.00636 -6.76852  1.000 66.53293  ? 72   ARG A NE  1 
ATOM   2277 C  CZ  . ARG B 1 73  ? 16.21144  -40.79888 -7.82984  1.000 69.42958  ? 72   ARG A CZ  1 
ATOM   2278 N  NH1 . ARG B 1 73  ? 15.21422  -41.61405 -8.13626  1.000 65.87052  ? 72   ARG A NH1 1 
ATOM   2279 N  NH2 . ARG B 1 73  ? 17.28117  -40.75612 -8.61677  1.000 74.09829  ? 72   ARG A NH2 1 
ATOM   2280 N  N   . ILE B 1 74  ? 11.69764  -38.73328 -3.09992  1.000 51.43694  ? 73   ILE A N   1 
ATOM   2281 C  CA  . ILE B 1 74  ? 10.32238  -38.30428 -2.86788  1.000 51.40559  ? 73   ILE A CA  1 
ATOM   2282 C  C   . ILE B 1 74  ? 9.89642   -37.41857 -4.03536  1.000 51.56621  ? 73   ILE A C   1 
ATOM   2283 O  O   . ILE B 1 74  ? 10.70431  -36.66348 -4.57974  1.000 52.19142  ? 73   ILE A O   1 
ATOM   2284 C  CB  . ILE B 1 74  ? 10.19075  -37.58770 -1.50325  1.000 49.48264  ? 73   ILE A CB  1 
ATOM   2285 C  CG1 . ILE B 1 74  ? 8.75364   -37.15773 -1.23631  1.000 51.93858  ? 73   ILE A CG1 1 
ATOM   2286 C  CG2 . ILE B 1 74  ? 11.10597  -36.38093 -1.41978  1.000 47.78027  ? 73   ILE A CG2 1 
ATOM   2287 C  CD1 . ILE B 1 74  ? 8.52332   -36.68822 0.19600   1.000 54.77519  ? 73   ILE A CD1 1 
ATOM   2288 N  N   . TYR B 1 75  ? 8.63859   -37.55983 -4.45734  1.000 52.23498  ? 74   TYR A N   1 
ATOM   2289 C  CA  . TYR B 1 75  ? 8.06338   -36.76965 -5.54943  1.000 53.20918  ? 74   TYR A CA  1 
ATOM   2290 C  C   . TYR B 1 75  ? 7.34938   -35.56394 -4.94274  1.000 55.87194  ? 74   TYR A C   1 
ATOM   2291 O  O   . TYR B 1 75  ? 6.22765   -35.68378 -4.44917  1.000 56.36139  ? 74   TYR A O   1 
ATOM   2292 C  CB  . TYR B 1 75  ? 7.11877   -37.62831 -6.39363  1.000 56.08093  ? 74   TYR A CB  1 
ATOM   2293 C  CG  . TYR B 1 75  ? 6.58876   -36.96431 -7.66238  1.000 58.34676  ? 74   TYR A CG  1 
ATOM   2294 C  CD1 . TYR B 1 75  ? 7.32113   -36.99701 -8.84694  1.000 56.66557  ? 74   TYR A CD1 1 
ATOM   2295 C  CD2 . TYR B 1 75  ? 5.35302   -36.32504 -7.67640  1.000 60.03284  ? 74   TYR A CD2 1 
ATOM   2296 C  CE1 . TYR B 1 75  ? 6.84101   -36.39373 -10.00574 1.000 59.15480  ? 74   TYR A CE1 1 
ATOM   2297 C  CE2 . TYR B 1 75  ? 4.87081   -35.72245 -8.82659  1.000 62.26017  ? 74   TYR A CE2 1 
ATOM   2298 C  CZ  . TYR B 1 75  ? 5.61414   -35.75956 -9.98626  1.000 61.05631  ? 74   TYR A CZ  1 
ATOM   2299 O  OH  . TYR B 1 75  ? 5.11765   -35.15770 -11.11830 1.000 63.48702  ? 74   TYR A OH  1 
ATOM   2300 N  N   . HIS B 1 76  ? 7.99372   -34.38915 -4.99290  1.000 55.15114  ? 75   HIS A N   1 
ATOM   2301 C  CA  . HIS B 1 76  ? 7.51608   -33.17472 -4.32132  1.000 55.12202  ? 75   HIS A CA  1 
ATOM   2302 C  C   . HIS B 1 76  ? 7.98100   -31.92839 -5.06128  1.000 56.18087  ? 75   HIS A C   1 
ATOM   2303 O  O   . HIS B 1 76  ? 9.13238   -31.88766 -5.52190  1.000 55.60357  ? 75   HIS A O   1 
ATOM   2304 C  CB  . HIS B 1 76  ? 8.01992   -33.12481 -2.87529  1.000 55.33745  ? 75   HIS A CB  1 
ATOM   2305 C  CG  . HIS B 1 76  ? 7.32778   -32.10784 -2.01925  1.000 56.39205  ? 75   HIS A CG  1 
ATOM   2306 N  ND1 . HIS B 1 76  ? 7.73832   -30.79456 -1.93890  1.000 56.47605  ? 75   HIS A ND1 1 
ATOM   2307 C  CD2 . HIS B 1 76  ? 6.25742   -32.21674 -1.19656  1.000 58.36203  ? 75   HIS A CD2 1 
ATOM   2308 C  CE1 . HIS B 1 76  ? 6.94760   -30.13786 -1.10857  1.000 57.95791  ? 75   HIS A CE1 1 
ATOM   2309 N  NE2 . HIS B 1 76  ? 6.03909   -30.97755 -0.64631  1.000 58.53806  ? 75   HIS A NE2 1 
ATOM   2310 N  N   . PRO B 1 77  ? 7.13469   -30.89749 -5.16705  1.000 56.36088  ? 76   PRO A N   1 
ATOM   2311 C  CA  . PRO B 1 77  ? 7.54589   -29.67159 -5.87778  1.000 57.94821  ? 76   PRO A CA  1 
ATOM   2312 C  C   . PRO B 1 77  ? 8.68436   -28.91338 -5.20963  1.000 58.87701  ? 76   PRO A C   1 
ATOM   2313 O  O   . PRO B 1 77  ? 9.33559   -28.10323 -5.87684  1.000 61.19428  ? 76   PRO A O   1 
ATOM   2314 C  CB  . PRO B 1 77  ? 6.25924   -28.83392 -5.90518  1.000 60.65807  ? 76   PRO A CB  1 
ATOM   2315 C  CG  . PRO B 1 77  ? 5.15789   -29.82764 -5.77049  1.000 61.66440  ? 76   PRO A CG  1 
ATOM   2316 C  CD  . PRO B 1 77  ? 5.70275   -30.87389 -4.82637  1.000 60.01242  ? 76   PRO A CD  1 
ATOM   2317 N  N   . ASN B 1 78  ? 8.91305   -29.09590 -3.90891  1.000 55.99875  ? 77   ASN A N   1 
ATOM   2318 C  CA  . ASN B 1 78  ? 9.92588   -28.32948 -3.19509  1.000 55.31082  ? 77   ASN A CA  1 
ATOM   2319 C  C   . ASN B 1 78  ? 11.10560  -29.16861 -2.73428  1.000 52.75942  ? 77   ASN A C   1 
ATOM   2320 O  O   . ASN B 1 78  ? 11.93770  -28.66703 -1.97157  1.000 51.03354  ? 77   ASN A O   1 
ATOM   2321 C  CB  . ASN B 1 78  ? 9.30488   -27.63945 -1.98458  1.000 57.03924  ? 77   ASN A CB  1 
ATOM   2322 C  CG  . ASN B 1 78  ? 8.11354   -26.81237 -2.35292  1.000 64.68211  ? 77   ASN A CG  1 
ATOM   2323 O  OD1 . ASN B 1 78  ? 6.98136   -27.26414 -2.22447  1.000 65.08155  ? 77   ASN A OD1 1 
ATOM   2324 N  ND2 . ASN B 1 78  ? 8.35508   -25.59554 -2.83687  1.000 71.71588  ? 77   ASN A ND2 1 
ATOM   2325 N  N   . ILE B 1 79  ? 11.21685  -30.41546 -3.19147  1.000 52.49633  ? 78   ILE A N   1 
ATOM   2326 C  CA  . ILE B 1 79  ? 12.32425  -31.30010 -2.83996  1.000 50.37320  ? 78   ILE A CA  1 
ATOM   2327 C  C   . ILE B 1 79  ? 12.85189  -31.92744 -4.12339  1.000 49.45922  ? 78   ILE A C   1 
ATOM   2328 O  O   . ILE B 1 79  ? 12.11633  -32.64048 -4.81747  1.000 48.40663  ? 78   ILE A O   1 
ATOM   2329 C  CB  . ILE B 1 79  ? 11.90266  -32.39253 -1.84223  1.000 47.88560  ? 78   ILE A CB  1 
ATOM   2330 C  CG1 . ILE B 1 79  ? 11.39704  -31.76152 -0.54224  1.000 50.42800  ? 78   ILE A CG1 1 
ATOM   2331 C  CG2 . ILE B 1 79  ? 13.06332  -33.33605 -1.58792  1.000 46.51865  ? 78   ILE A CG2 1 
ATOM   2332 C  CD1 . ILE B 1 79  ? 10.37672  -32.57910 0.20171   1.000 48.04567  ? 78   ILE A CD1 1 
ATOM   2333 N  N   . ASN B 1 80  ? 14.11975  -31.66459 -4.43737  1.000 48.76405  ? 79   ASN A N   1 
ATOM   2334 C  CA  . ASN B 1 80  ? 14.70486  -32.13410 -5.68400  1.000 49.38287  ? 79   ASN A CA  1 
ATOM   2335 C  C   . ASN B 1 80  ? 15.38378  -33.49681 -5.50638  1.000 50.00224  ? 79   ASN A C   1 
ATOM   2336 O  O   . ASN B 1 80  ? 15.36954  -34.11000 -4.43318  1.000 49.71699  ? 79   ASN A O   1 
ATOM   2337 C  CB  . ASN B 1 80  ? 15.66816  -31.08796 -6.26558  1.000 49.90574  ? 79   ASN A CB  1 
ATOM   2338 C  CG  . ASN B 1 80  ? 16.91468  -30.85442 -5.40457  1.000 49.46401  ? 79   ASN A CG  1 
ATOM   2339 O  OD1 . ASN B 1 80  ? 17.26917  -31.65702 -4.54424  1.000 51.31626  ? 79   ASN A OD1 1 
ATOM   2340 N  ND2 . ASN B 1 80  ? 17.60248  -29.76203 -5.67120  1.000 48.05609  ? 79   ASN A ND2 1 
ATOM   2341 N  N   . SER B 1 81  ? 16.01073  -33.96043 -6.58724  1.000 50.56694  ? 80   SER A N   1 
ATOM   2342 C  CA  . SER B 1 81  ? 16.63235  -35.27790 -6.64987  1.000 51.74650  ? 80   SER A CA  1 
ATOM   2343 C  C   . SER B 1 81  ? 17.88326  -35.39189 -5.79258  1.000 50.45758  ? 80   SER A C   1 
ATOM   2344 O  O   . SER B 1 81  ? 18.36676  -36.50860 -5.58124  1.000 52.78185  ? 80   SER A O   1 
ATOM   2345 C  CB  . SER B 1 81  ? 16.96949  -35.62130 -8.10232  1.000 53.83538  ? 80   SER A CB  1 
ATOM   2346 O  OG  . SER B 1 81  ? 18.03114  -34.81296 -8.58645  1.000 56.49954  ? 80   SER A OG  1 
ATOM   2347 N  N   . ASN B 1 82  ? 18.44727  -34.28395 -5.33922  1.000 50.66032  ? 81   ASN A N   1 
ATOM   2348 C  CA  . ASN B 1 82  ? 19.53945  -34.35158 -4.38257  1.000 52.15229  ? 81   ASN A CA  1 
ATOM   2349 C  C   . ASN B 1 82  ? 19.03384  -34.39350 -2.93524  1.000 49.62825  ? 81   ASN A C   1 
ATOM   2350 O  O   . ASN B 1 82  ? 19.84531  -34.44604 -2.00730  1.000 48.24979  ? 81   ASN A O   1 
ATOM   2351 C  CB  . ASN B 1 82  ? 20.47567  -33.14826 -4.58614  1.000 52.68669  ? 81   ASN A CB  1 
ATOM   2352 C  CG  . ASN B 1 82  ? 21.27714  -33.21558 -5.90697  1.000 60.00101  ? 81   ASN A CG  1 
ATOM   2353 O  OD1 . ASN B 1 82  ? 21.32045  -34.24087 -6.59129  1.000 64.63588  ? 81   ASN A OD1 1 
ATOM   2354 N  ND2 . ASN B 1 82  ? 21.85789  -32.08138 -6.28975  1.000 65.24776  ? 81   ASN A ND2 1 
ATOM   2355 N  N   . GLY B 1 83  ? 17.71719  -34.40323 -2.72092  1.000 48.44753  ? 82   GLY A N   1 
ATOM   2356 C  CA  . GLY B 1 83  ? 17.16736  -34.36799 -1.38018  1.000 47.77554  ? 82   GLY A CA  1 
ATOM   2357 C  C   . GLY B 1 83  ? 17.14671  -32.99533 -0.74534  1.000 48.48734  ? 82   GLY A C   1 
ATOM   2358 O  O   . GLY B 1 83  ? 16.74002  -32.87152 0.41681   1.000 49.45415  ? 82   GLY A O   1 
ATOM   2359 N  N   . SER B 1 84  ? 17.57294  -31.96216 -1.46771  1.000 48.90688  ? 83   SER A N   1 
ATOM   2360 C  CA  . SER B 1 84  ? 17.50065  -30.59911 -0.96694  1.000 49.20027  ? 83   SER A CA  1 
ATOM   2361 C  C   . SER B 1 84  ? 16.04980  -30.16910 -0.80962  1.000 49.33482  ? 83   SER A C   1 
ATOM   2362 O  O   . SER B 1 84  ? 15.17529  -30.55668 -1.58926  1.000 48.94111  ? 83   SER A O   1 
ATOM   2363 C  CB  . SER B 1 84  ? 18.21804  -29.63320 -1.91543  1.000 50.66132  ? 83   SER A CB  1 
ATOM   2364 O  OG  . SER B 1 84  ? 19.61804  -29.62817 -1.70942  1.000 53.27526  ? 83   SER A OG  1 
ATOM   2365 N  N   . ILE B 1 85  ? 15.81156  -29.31444 0.18069   1.000 48.67003  ? 84   ILE A N   1 
ATOM   2366 C  CA  . ILE B 1 85  ? 14.47469  -28.87368 0.54799   1.000 49.98621  ? 84   ILE A CA  1 
ATOM   2367 C  C   . ILE B 1 85  ? 14.39264  -27.37094 0.33236   1.000 51.14302  ? 84   ILE A C   1 
ATOM   2368 O  O   . ILE B 1 85  ? 15.25644  -26.62268 0.80392   1.000 52.52907  ? 84   ILE A O   1 
ATOM   2369 C  CB  . ILE B 1 85  ? 14.14686  -29.24839 2.00557   1.000 49.41814  ? 84   ILE A CB  1 
ATOM   2370 C  CG1 . ILE B 1 85  ? 14.41067  -30.74753 2.21157   1.000 48.07021  ? 84   ILE A CG1 1 
ATOM   2371 C  CG2 . ILE B 1 85  ? 12.70947  -28.84132 2.34906   1.000 48.82827  ? 84   ILE A CG2 1 
ATOM   2372 C  CD1 . ILE B 1 85  ? 14.46518  -31.19332 3.65399   1.000 45.31642  ? 84   ILE A CD1 1 
ATOM   2373 N  N   . CYS B 1 86  ? 13.37152  -26.93664 -0.40255  1.000 51.37421  ? 85   CYS A N   1 
ATOM   2374 C  CA  . CYS B 1 86  ? 13.08468  -25.51542 -0.57031  1.000 52.66315  ? 85   CYS A CA  1 
ATOM   2375 C  C   . CYS B 1 86  ? 12.04291  -25.12945 0.47747   1.000 53.88937  ? 85   CYS A C   1 
ATOM   2376 O  O   . CYS B 1 86  ? 10.83335  -25.29533 0.28619   1.000 54.38831  ? 85   CYS A O   1 
ATOM   2377 C  CB  . CYS B 1 86  ? 12.59064  -25.22773 -1.97786  1.000 55.04010  ? 85   CYS A CB  1 
ATOM   2378 S  SG  . CYS B 1 86  ? 12.08978  -23.53187 -2.22522  1.000 62.47081  ? 85   CYS A SG  1 
ATOM   2379 N  N   . LEU B 1 87  ? 12.51788  -24.60720 1.60295   1.000 52.57179  ? 86   LEU A N   1 
ATOM   2380 C  CA  . LEU B 1 87  ? 11.64396  -24.27003 2.71807   1.000 56.04798  ? 86   LEU A CA  1 
ATOM   2381 C  C   . LEU B 1 87  ? 12.24817  -23.08463 3.44044   1.000 57.81253  ? 86   LEU A C   1 
ATOM   2382 O  O   . LEU B 1 87  ? 13.36169  -23.18468 3.96282   1.000 55.18501  ? 86   LEU A O   1 
ATOM   2383 C  CB  . LEU B 1 87  ? 11.47552  -25.45583 3.66436   1.000 55.56139  ? 86   LEU A CB  1 
ATOM   2384 C  CG  . LEU B 1 87  ? 10.58359  -25.23457 4.88464   1.000 57.54425  ? 86   LEU A CG  1 
ATOM   2385 C  CD1 . LEU B 1 87  ? 9.22015   -24.65722 4.52096   1.000 58.61198  ? 86   LEU A CD1 1 
ATOM   2386 C  CD2 . LEU B 1 87  ? 10.44644  -26.56485 5.59953   1.000 55.33021  ? 86   LEU A CD2 1 
ATOM   2387 N  N   . ASP B 1 88  ? 11.51454  -21.97062 3.46308   1.000 60.05100  ? 87   ASP A N   1 
ATOM   2388 C  CA  . ASP B 1 88  ? 12.06572  -20.72263 3.98608   1.000 60.82048  ? 87   ASP A CA  1 
ATOM   2389 C  C   . ASP B 1 88  ? 12.53464  -20.87205 5.42868   1.000 61.00325  ? 87   ASP A C   1 
ATOM   2390 O  O   . ASP B 1 88  ? 13.49006  -20.20462 5.83843   1.000 59.69862  ? 87   ASP A O   1 
ATOM   2391 C  CB  . ASP B 1 88  ? 11.03162  -19.61430 3.83511   1.000 63.38470  ? 87   ASP A CB  1 
ATOM   2392 C  CG  . ASP B 1 88  ? 9.69887   -20.00885 4.39874   1.000 74.40639  ? 87   ASP A CG  1 
ATOM   2393 O  OD1 . ASP B 1 88  ? 9.55910   -21.19372 4.78453   1.000 74.05046  ? 87   ASP A OD1 1 
ATOM   2394 O  OD2 . ASP B 1 88  ? 8.80064   -19.14233 4.46099   1.000 83.50664  ? 87   ASP A OD2 1 
ATOM   2395 N  N   . ILE B 1 89  ? 11.91056  -21.77666 6.18978   1.000 58.86055  ? 88   ILE A N   1 
ATOM   2396 C  CA  . ILE B 1 89  ? 12.29877  -22.04917 7.57029   1.000 60.18580  ? 88   ILE A CA  1 
ATOM   2397 C  C   . ILE B 1 89  ? 13.76992  -22.42912 7.66582   1.000 57.96722  ? 88   ILE A C   1 
ATOM   2398 O  O   . ILE B 1 89  ? 14.40150  -22.23851 8.71182   1.000 57.35971  ? 88   ILE A O   1 
ATOM   2399 C  CB  . ILE B 1 89  ? 11.40417  -23.18931 8.12480   1.000 59.76730  ? 88   ILE A CB  1 
ATOM   2400 C  CG1 . ILE B 1 89  ? 9.92252   -22.80111 8.05837   1.000 66.04319  ? 88   ILE A CG1 1 
ATOM   2401 C  CG2 . ILE B 1 89  ? 11.79281  -23.57706 9.54668   1.000 58.77126  ? 88   ILE A CG2 1 
ATOM   2402 C  CD1 . ILE B 1 89  ? 9.54708   -21.59212 8.86759   1.000 62.25154  ? 88   ILE A CD1 1 
ATOM   2403 N  N   . LEU B 1 90  ? 14.33797  -22.95228 6.58649   1.000 55.96076  ? 89   LEU A N   1 
ATOM   2404 C  CA  . LEU B 1 90  ? 15.71223  -23.41546 6.60166   1.000 54.70660  ? 89   LEU A CA  1 
ATOM   2405 C  C   . LEU B 1 90  ? 16.70574  -22.34562 6.19278   1.000 55.68226  ? 89   LEU A C   1 
ATOM   2406 O  O   . LEU B 1 90  ? 17.91469  -22.56222 6.32898   1.000 55.71077  ? 89   LEU A O   1 
ATOM   2407 C  CB  . LEU B 1 90  ? 15.85831  -24.64221 5.69346   1.000 52.38875  ? 89   LEU A CB  1 
ATOM   2408 C  CG  . LEU B 1 90  ? 15.19646  -25.90052 6.24834   1.000 50.48358  ? 89   LEU A CG  1 
ATOM   2409 C  CD1 . LEU B 1 90  ? 15.28467  -27.02373 5.23859   1.000 49.71577  ? 89   LEU A CD1 1 
ATOM   2410 C  CD2 . LEU B 1 90  ? 15.89444  -26.29728 7.54398   1.000 48.44072  ? 89   LEU A CD2 1 
ATOM   2411 N  N   . ARG B 1 91  ? 16.23454  -21.20241 5.71046   1.000 58.32206  ? 90   ARG A N   1 
ATOM   2412 C  CA  . ARG B 1 91  ? 17.14581  -20.13352 5.34080   1.000 60.42280  ? 90   ARG A CA  1 
ATOM   2413 C  C   . ARG B 1 91  ? 16.60275  -18.76491 5.73102   1.000 60.41449  ? 90   ARG A C   1 
ATOM   2414 O  O   . ARG B 1 91  ? 17.04105  -18.17829 6.72486   1.000 60.10665  ? 90   ARG A O   1 
ATOM   2415 C  CB  . ARG B 1 91  ? 17.45916  -20.16691 3.84703   1.000 59.74771  ? 90   ARG A CB  1 
ATOM   2416 C  CG  . ARG B 1 91  ? 18.64564  -19.29648 3.49985   1.000 64.61554  ? 90   ARG A CG  1 
ATOM   2417 C  CD  . ARG B 1 91  ? 18.87458  -19.24392 2.00129   1.000 70.33700  ? 90   ARG A CD  1 
ATOM   2418 N  NE  . ARG B 1 91  ? 20.22209  -18.78720 1.68839   1.000 70.52820  ? 90   ARG A NE  1 
ATOM   2419 C  CZ  . ARG B 1 91  ? 21.22698  -19.58491 1.35669   1.000 75.63396  ? 90   ARG A CZ  1 
ATOM   2420 N  NH1 . ARG B 1 91  ? 21.07488  -20.89935 1.28857   1.000 76.57413  ? 90   ARG A NH1 1 
ATOM   2421 N  NH2 . ARG B 1 91  ? 22.41391  -19.05079 1.08553   1.000 75.60972  ? 90   ARG A NH2 1 
ATOM   2422 N  N   . SER B 1 92  ? 15.66591  -18.24012 4.93757   1.000 60.41247  ? 91   SER A N   1 
ATOM   2423 C  CA  . SER B 1 92  ? 15.20902  -16.86221 5.11354   1.000 58.15698  ? 91   SER A CA  1 
ATOM   2424 C  C   . SER B 1 92  ? 14.43137  -16.67368 6.41870   1.000 61.53482  ? 91   SER A C   1 
ATOM   2425 O  O   . SER B 1 92  ? 14.62716  -15.67177 7.11893   1.000 64.25504  ? 91   SER A O   1 
ATOM   2426 C  CB  . SER B 1 92  ? 14.38667  -16.45172 3.89224   1.000 52.41417  ? 91   SER A CB  1 
ATOM   2427 O  OG  . SER B 1 92  ? 13.14079  -17.11805 3.86724   1.000 58.88352  ? 91   SER A OG  1 
ATOM   2428 N  N   . GLN B 1 93  ? 13.52762  -17.59721 6.75047   1.000 60.63170  ? 92   GLN A N   1 
ATOM   2429 C  CA  . GLN B 1 93  ? 12.75880  -17.51957 7.98544   1.000 62.71755  ? 92   GLN A CA  1 
ATOM   2430 C  C   . GLN B 1 93  ? 13.41847  -18.27584 9.13623   1.000 62.47899  ? 92   GLN A C   1 
ATOM   2431 O  O   . GLN B 1 93  ? 12.74693  -18.58272 10.12914  1.000 62.29279  ? 92   GLN A O   1 
ATOM   2432 C  CB  . GLN B 1 93  ? 11.33931  -18.04788 7.77881   1.000 63.93503  ? 92   GLN A CB  1 
ATOM   2433 C  CG  . GLN B 1 93  ? 10.43398  -17.14291 6.97860   1.000 67.19936  ? 92   GLN A CG  1 
ATOM   2434 C  CD  . GLN B 1 93  ? 10.21847  -15.81610 7.65893   1.000 70.35529  ? 92   GLN A CD  1 
ATOM   2435 O  OE1 . GLN B 1 93  ? 10.99139  -14.87859 7.46152   1.000 79.06179  ? 92   GLN A OE1 1 
ATOM   2436 N  NE2 . GLN B 1 93  ? 9.16265   -15.72426 8.47005   1.000 72.02976  ? 92   GLN A NE2 1 
ATOM   2437 N  N   . TRP B 1 94  ? 14.71188  -18.57400 9.04382   1.000 60.71626  ? 93   TRP A N   1 
ATOM   2438 C  CA  . TRP B 1 94  ? 15.36207  -19.22222 10.17112  1.000 58.66022  ? 93   TRP A CA  1 
ATOM   2439 C  C   . TRP B 1 94  ? 15.53216  -18.24817 11.32119  1.000 59.85445  ? 93   TRP A C   1 
ATOM   2440 O  O   . TRP B 1 94  ? 15.94020  -17.10034 11.13487  1.000 61.04368  ? 93   TRP A O   1 
ATOM   2441 C  CB  . TRP B 1 94  ? 16.73563  -19.77680 9.80668   1.000 56.12379  ? 93   TRP A CB  1 
ATOM   2442 C  CG  . TRP B 1 94  ? 17.41296  -20.32431 11.04337  1.000 54.28881  ? 93   TRP A CG  1 
ATOM   2443 C  CD1 . TRP B 1 94  ? 18.42369  -19.74459 11.75219  1.000 54.24541  ? 93   TRP A CD1 1 
ATOM   2444 C  CD2 . TRP B 1 94  ? 17.11036  -21.55538 11.71681  1.000 52.82096  ? 93   TRP A CD2 1 
ATOM   2445 N  NE1 . TRP B 1 94  ? 18.76692  -20.53238 12.82804  1.000 53.18043  ? 93   TRP A NE1 1 
ATOM   2446 C  CE2 . TRP B 1 94  ? 17.97708  -21.65025 12.82627  1.000 51.12584  ? 93   TRP A CE2 1 
ATOM   2447 C  CE3 . TRP B 1 94  ? 16.19448  -22.58671 11.48620  1.000 52.77781  ? 93   TRP A CE3 1 
ATOM   2448 C  CZ2 . TRP B 1 94  ? 17.94620  -22.72648 13.70787  1.000 50.63760  ? 93   TRP A CZ2 1 
ATOM   2449 C  CZ3 . TRP B 1 94  ? 16.16704  -23.65104 12.35616  1.000 50.67284  ? 93   TRP A CZ3 1 
ATOM   2450 C  CH2 . TRP B 1 94  ? 17.03739  -23.71682 13.45691  1.000 50.37542  ? 93   TRP A CH2 1 
ATOM   2451 N  N   . SER B 1 95  ? 15.22634  -18.71548 12.51649  1.000 57.63024  ? 94   SER A N   1 
ATOM   2452 C  CA  . SER B 1 95  ? 15.51983  -17.97174 13.72472  1.000 56.88181  ? 94   SER A CA  1 
ATOM   2453 C  C   . SER B 1 95  ? 16.29805  -18.86814 14.67133  1.000 54.09092  ? 94   SER A C   1 
ATOM   2454 O  O   . SER B 1 95  ? 16.02592  -20.07194 14.73507  1.000 53.29990  ? 94   SER A O   1 
ATOM   2455 C  CB  . SER B 1 95  ? 14.25629  -17.48887 14.43106  1.000 57.41342  ? 94   SER A CB  1 
ATOM   2456 O  OG  . SER B 1 95  ? 14.58403  -17.18390 15.77601  1.000 56.34641  ? 94   SER A OG  1 
ATOM   2457 N  N   . PRO B 1 96  ? 17.27725  -18.33093 15.40152  1.000 53.96633  ? 95   PRO A N   1 
ATOM   2458 C  CA  . PRO B 1 96  ? 17.96270  -19.15593 16.40508  1.000 54.54839  ? 95   PRO A CA  1 
ATOM   2459 C  C   . PRO B 1 96  ? 17.06168  -19.57390 17.54807  1.000 55.15208  ? 95   PRO A C   1 
ATOM   2460 O  O   . PRO B 1 96  ? 17.49385  -20.37946 18.38209  1.000 55.48131  ? 95   PRO A O   1 
ATOM   2461 C  CB  . PRO B 1 96  ? 19.11399  -18.27014 16.88577  1.000 55.02131  ? 95   PRO A CB  1 
ATOM   2462 C  CG  . PRO B 1 96  ? 18.69582  -16.91980 16.56332  1.000 56.20425  ? 95   PRO A CG  1 
ATOM   2463 C  CD  . PRO B 1 96  ? 17.81935  -16.96904 15.34701  1.000 53.00293  ? 95   PRO A CD  1 
ATOM   2464 N  N   . ALA B 1 97  ? 15.83374  -19.06783 17.62406  1.000 53.90600  ? 96   ALA A N   1 
ATOM   2465 C  CA  . ALA B 1 97  ? 14.89588  -19.57065 18.61706  1.000 54.95156  ? 96   ALA A CA  1 
ATOM   2466 C  C   . ALA B 1 97  ? 14.16579  -20.81872 18.13540  1.000 55.79864  ? 96   ALA A C   1 
ATOM   2467 O  O   . ALA B 1 97  ? 13.41234  -21.41886 18.90779  1.000 57.09609  ? 96   ALA A O   1 
ATOM   2468 C  CB  . ALA B 1 97  ? 13.87997  -18.48686 19.00528  1.000 56.06840  ? 96   ALA A CB  1 
ATOM   2469 N  N   . LEU B 1 98  ? 14.39208  -21.23494 16.89279  1.000 55.34431  ? 97   LEU A N   1 
ATOM   2470 C  CA  . LEU B 1 98  ? 13.76621  -22.41746 16.32250  1.000 54.07289  ? 97   LEU A CA  1 
ATOM   2471 C  C   . LEU B 1 98  ? 14.59717  -23.65441 16.65165  1.000 52.59137  ? 97   LEU A C   1 
ATOM   2472 O  O   . LEU B 1 98  ? 15.79844  -23.56401 16.90797  1.000 52.25649  ? 97   LEU A O   1 
ATOM   2473 C  CB  . LEU B 1 98  ? 13.60995  -22.25790 14.80304  1.000 53.18512  ? 97   LEU A CB  1 
ATOM   2474 C  CG  . LEU B 1 98  ? 12.52208  -21.30348 14.28598  1.000 54.49882  ? 97   LEU A CG  1 
ATOM   2475 C  CD1 . LEU B 1 98  ? 12.76993  -20.90255 12.84199  1.000 56.89022  ? 97   LEU A CD1 1 
ATOM   2476 C  CD2 . LEU B 1 98  ? 11.14707  -21.92917 14.41335  1.000 57.30879  ? 97   LEU A CD2 1 
ATOM   2477 N  N   . THR B 1 99  ? 13.93813  -24.80986 16.68620  1.000 52.63002  ? 98   THR A N   1 
ATOM   2478 C  CA  . THR B 1 99  ? 14.58194  -26.06736 17.04136  1.000 51.04869  ? 98   THR A CA  1 
ATOM   2479 C  C   . THR B 1 99  ? 14.43196  -27.09021 15.92290  1.000 51.01633  ? 98   THR A C   1 
ATOM   2480 O  O   . THR B 1 99  ? 13.63665  -26.92839 14.99345  1.000 50.48121  ? 98   THR A O   1 
ATOM   2481 C  CB  . THR B 1 99  ? 14.00486  -26.63022 18.34622  1.000 52.40100  ? 98   THR A CB  1 
ATOM   2482 O  OG1 . THR B 1 99  ? 12.61862  -26.95558 18.16140  1.000 52.30500  ? 98   THR A OG1 1 
ATOM   2483 C  CG2 . THR B 1 99  ? 14.13840  -25.60922 19.45711  1.000 52.93467  ? 98   THR A CG2 1 
ATOM   2484 N  N   . ILE B 1 100 ? 15.20403  -28.17039 16.03583  1.000 49.80270  ? 99   ILE A N   1 
ATOM   2485 C  CA  . ILE B 1 100 ? 15.07991  -29.25640 15.07187  1.000 49.40049  ? 99   ILE A CA  1 
ATOM   2486 C  C   . ILE B 1 100 ? 13.65163  -29.76807 15.03482  1.000 50.27134  ? 99   ILE A C   1 
ATOM   2487 O  O   . ILE B 1 100 ? 13.12848  -30.08451 13.96580  1.000 50.69639  ? 99   ILE A O   1 
ATOM   2488 C  CB  . ILE B 1 100 ? 16.07541  -30.38387 15.39336  1.000 50.07554  ? 99   ILE A CB  1 
ATOM   2489 C  CG1 . ILE B 1 100 ? 17.48990  -29.88190 15.15442  1.000 50.12309  ? 99   ILE A CG1 1 
ATOM   2490 C  CG2 . ILE B 1 100 ? 15.83260  -31.58848 14.49502  1.000 49.21633  ? 99   ILE A CG2 1 
ATOM   2491 C  CD1 . ILE B 1 100 ? 17.72761  -29.45037 13.72035  1.000 48.08404  ? 99   ILE A CD1 1 
ATOM   2492 N  N   . SER B 1 101 ? 12.99476  -29.84319 16.19637  1.000 50.63610  ? 100  SER A N   1 
ATOM   2493 C  CA  A SER B 1 101 ? 11.62032  -30.33235 16.23343  0.549 51.95697  ? 100  SER A CA  1 
ATOM   2494 C  CA  B SER B 1 101 ? 11.61486  -30.31834 16.25220  0.451 50.44513  ? 100  SER A CA  1 
ATOM   2495 C  C   . SER B 1 101 ? 10.69525  -29.43604 15.42308  1.000 49.36202  ? 100  SER A C   1 
ATOM   2496 O  O   . SER B 1 101 ? 9.85860   -29.93018 14.66115  1.000 51.26637  ? 100  SER A O   1 
ATOM   2497 C  CB  A SER B 1 101 ? 11.12846  -30.44632 17.67702  0.549 50.79400  ? 100  SER A CB  1 
ATOM   2498 C  CB  B SER B 1 101 ? 11.13876  -30.35957 17.70171  0.451 52.15321  ? 100  SER A CB  1 
ATOM   2499 O  OG  A SER B 1 101 ? 9.89961   -31.15817 17.73815  0.549 52.91254  ? 100  SER A OG  1 
ATOM   2500 O  OG  B SER B 1 101 ? 12.19689  -30.72835 18.55796  0.451 52.09736  ? 100  SER A OG  1 
ATOM   2501 N  N   . LYS B 1 102 ? 10.81862  -28.11622 15.58125  1.000 50.60041  ? 101  LYS A N   1 
ATOM   2502 C  CA  . LYS B 1 102 ? 10.01501  -27.22796 14.75453  1.000 51.41571  ? 101  LYS A CA  1 
ATOM   2503 C  C   . LYS B 1 102 ? 10.32864  -27.46311 13.28191  1.000 51.08029  ? 101  LYS A C   1 
ATOM   2504 O  O   . LYS B 1 102 ? 9.41990   -27.52071 12.45057  1.000 50.18718  ? 101  LYS A O   1 
ATOM   2505 C  CB  . LYS B 1 102 ? 10.27167  -25.76396 15.11094  1.000 52.17493  ? 101  LYS A CB  1 
ATOM   2506 C  CG  . LYS B 1 102 ? 10.27320  -25.41383 16.57607  1.000 54.09136  ? 101  LYS A CG  1 
ATOM   2507 C  CD  . LYS B 1 102 ? 8.87965   -25.30270 17.16229  1.000 59.00607  ? 101  LYS A CD  1 
ATOM   2508 C  CE  . LYS B 1 102 ? 8.96209   -25.19431 18.68191  1.000 60.79911  ? 101  LYS A CE  1 
ATOM   2509 N  NZ  . LYS B 1 102 ? 9.61293   -26.41721 19.25995  1.000 64.23020  ? 101  LYS A NZ  1 
ATOM   2510 N  N   . VAL B 1 103 ? 11.60996  -27.66112 12.95531  1.000 50.36663  ? 102  VAL A N   1 
ATOM   2511 C  CA  . VAL B 1 103 ? 12.01186  -27.84714 11.56538  1.000 50.54029  ? 102  VAL A CA  1 
ATOM   2512 C  C   . VAL B 1 103 ? 11.39831  -29.11112 10.99663  1.000 50.84162  ? 102  VAL A C   1 
ATOM   2513 O  O   . VAL B 1 103 ? 10.89040  -29.12471 9.87090   1.000 51.05491  ? 102  VAL A O   1 
ATOM   2514 C  CB  . VAL B 1 103 ? 13.54369  -27.89003 11.44910  1.000 49.23641  ? 102  VAL A CB  1 
ATOM   2515 C  CG1 . VAL B 1 103 ? 13.93680  -28.40169 10.07469  1.000 48.69065  ? 102  VAL A CG1 1 
ATOM   2516 C  CG2 . VAL B 1 103 ? 14.11911  -26.51288 11.67953  1.000 47.51635  ? 102  VAL A CG2 1 
ATOM   2517 N  N   . LEU B 1 104 ? 11.46473  -30.20224 11.74641  1.000 50.88779  ? 103  LEU A N   1 
ATOM   2518 C  CA  . LEU B 1 104 ? 10.88547  -31.43309 11.24531  1.000 51.50545  ? 103  LEU A CA  1 
ATOM   2519 C  C   . LEU B 1 104 ? 9.38219   -31.29977 11.11385  1.000 52.66038  ? 103  LEU A C   1 
ATOM   2520 O  O   . LEU B 1 104 ? 8.79726   -31.82542 10.15857  1.000 55.49649  ? 103  LEU A O   1 
ATOM   2521 C  CB  . LEU B 1 104 ? 11.28616  -32.60651 12.13557  1.000 52.40464  ? 103  LEU A CB  1 
ATOM   2522 C  CG  . LEU B 1 104 ? 12.78833  -32.90112 12.04880  1.000 53.29851  ? 103  LEU A CG  1 
ATOM   2523 C  CD1 . LEU B 1 104 ? 13.19940  -33.88593 13.10467  1.000 53.80521  ? 103  LEU A CD1 1 
ATOM   2524 C  CD2 . LEU B 1 104 ? 13.14389  -33.43194 10.66862  1.000 50.74938  ? 103  LEU A CD2 1 
ATOM   2525 N  N   . LEU B 1 105 ? 8.74366   -30.56286 12.02602  1.000 51.14295  ? 104  LEU A N   1 
ATOM   2526 C  CA  . LEU B 1 105 ? 7.30709   -30.36238 11.89878  1.000 53.05325  ? 104  LEU A CA  1 
ATOM   2527 C  C   . LEU B 1 105 ? 6.99188   -29.50113 10.68445  1.000 52.88803  ? 104  LEU A C   1 
ATOM   2528 O  O   . LEU B 1 105 ? 6.00173   -29.73588 9.98673   1.000 52.81308  ? 104  LEU A O   1 
ATOM   2529 C  CB  . LEU B 1 105 ? 6.75138   -29.76336 13.19322  1.000 51.26340  ? 104  LEU A CB  1 
ATOM   2530 C  CG  . LEU B 1 105 ? 6.77483   -30.74254 14.38047  1.000 53.84064  ? 104  LEU A CG  1 
ATOM   2531 C  CD1 . LEU B 1 105 ? 6.24752   -30.10161 15.63567  1.000 56.99673  ? 104  LEU A CD1 1 
ATOM   2532 C  CD2 . LEU B 1 105 ? 5.97820   -32.00437 14.08402  1.000 57.21483  ? 104  LEU A CD2 1 
ATOM   2533 N  N   . SER B 1 106 ? 7.84501   -28.52610 10.39680  1.000 52.33728  ? 105  SER A N   1 
ATOM   2534 C  CA  A SER B 1 106 ? 7.67279   -27.72365 9.19404   0.631 53.41003  ? 105  SER A CA  1 
ATOM   2535 C  CA  B SER B 1 106 ? 7.66784   -27.72284 9.19624   0.369 53.55484  ? 105  SER A CA  1 
ATOM   2536 C  C   . SER B 1 106 ? 7.89156   -28.55061 7.93404   1.000 53.34451  ? 105  SER A C   1 
ATOM   2537 O  O   . SER B 1 106 ? 7.25643   -28.29089 6.91203   1.000 53.24261  ? 105  SER A O   1 
ATOM   2538 C  CB  A SER B 1 106 ? 8.62744   -26.53003 9.21057   0.631 53.74382  ? 105  SER A CB  1 
ATOM   2539 C  CB  B SER B 1 106 ? 8.60865   -26.51605 9.23802   0.369 53.39273  ? 105  SER A CB  1 
ATOM   2540 O  OG  A SER B 1 106 ? 8.32895   -25.65386 10.27945  0.631 53.80051  ? 105  SER A OG  1 
ATOM   2541 O  OG  B SER B 1 106 ? 8.43162   -25.67599 8.11398   0.369 54.69684  ? 105  SER A OG  1 
ATOM   2542 N  N   . ILE B 1 107 ? 8.76910   -29.55739 7.99079   1.000 52.09528  ? 106  ILE A N   1 
ATOM   2543 C  CA  . ILE B 1 107 ? 8.99945   -30.40482 6.81899   1.000 53.17326  ? 106  ILE A CA  1 
ATOM   2544 C  C   . ILE B 1 107 ? 7.80883   -31.32886 6.57981   1.000 55.21530  ? 106  ILE A C   1 
ATOM   2545 O  O   . ILE B 1 107 ? 7.40338   -31.55450 5.43202   1.000 54.21139  ? 106  ILE A O   1 
ATOM   2546 C  CB  . ILE B 1 107 ? 10.31512  -31.19471 6.95120   1.000 50.24239  ? 106  ILE A CB  1 
ATOM   2547 C  CG1 . ILE B 1 107 ? 11.52294  -30.27124 6.78570   1.000 46.75615  ? 106  ILE A CG1 1 
ATOM   2548 C  CG2 . ILE B 1 107 ? 10.37798  -32.27250 5.90572   1.000 48.67210  ? 106  ILE A CG2 1 
ATOM   2549 C  CD1 . ILE B 1 107 ? 12.85494  -30.95632 6.98497   1.000 44.00151  ? 106  ILE A CD1 1 
ATOM   2550 N  N   . CYS B 1 108 ? 7.23470   -31.88726 7.65171   1.000 54.22964  ? 107  CYS A N   1 
ATOM   2551 C  CA  . CYS B 1 108 ? 5.99031   -32.64883 7.51125   1.000 55.86831  ? 107  CYS A CA  1 
ATOM   2552 C  C   . CYS B 1 108 ? 4.86327   -31.76212 6.99133   1.000 58.80313  ? 107  CYS A C   1 
ATOM   2553 O  O   . CYS B 1 108 ? 4.02675   -32.19743 6.18478   1.000 62.03503  ? 107  CYS A O   1 
ATOM   2554 C  CB  . CYS B 1 108 ? 5.59744   -33.27093 8.84694   1.000 57.61757  ? 107  CYS A CB  1 
ATOM   2555 S  SG  . CYS B 1 108 ? 6.80898   -34.41580 9.50934   1.000 59.32525  ? 107  CYS A SG  1 
ATOM   2556 N  N   . SER B 1 109 ? 4.82341   -30.51174 7.45404   1.000 57.95678  ? 108  SER A N   1 
ATOM   2557 C  CA  . SER B 1 109 ? 3.83389   -29.56059 6.96673   1.000 58.70336  ? 108  SER A CA  1 
ATOM   2558 C  C   . SER B 1 109 ? 4.05073   -29.25764 5.48535   1.000 60.63590  ? 108  SER A C   1 
ATOM   2559 O  O   . SER B 1 109 ? 3.09299   -29.19719 4.70639   1.000 62.26460  ? 108  SER A O   1 
ATOM   2560 C  CB  . SER B 1 109 ? 3.90594   -28.29040 7.81917   1.000 58.36708  ? 108  SER A CB  1 
ATOM   2561 O  OG  . SER B 1 109 ? 2.72510   -27.51937 7.72162   1.000 66.23339  ? 108  SER A OG  1 
ATOM   2562 N  N   . LEU B 1 110 ? 5.30763   -29.09539 5.07237   1.000 58.61151  ? 109  LEU A N   1 
ATOM   2563 C  CA  . LEU B 1 110 ? 5.60624   -28.92034 3.65602   1.000 59.41263  ? 109  LEU A CA  1 
ATOM   2564 C  C   . LEU B 1 110 ? 5.14994   -30.12856 2.85460   1.000 60.54649  ? 109  LEU A C   1 
ATOM   2565 O  O   . LEU B 1 110 ? 4.59146   -29.98156 1.76316   1.000 62.25163  ? 109  LEU A O   1 
ATOM   2566 C  CB  . LEU B 1 110 ? 7.09820   -28.67923 3.45424   1.000 56.90000  ? 109  LEU A CB  1 
ATOM   2567 C  CG  . LEU B 1 110 ? 7.52582   -28.48371 2.00008   1.000 58.70728  ? 109  LEU A CG  1 
ATOM   2568 C  CD1 . LEU B 1 110 ? 6.95359   -27.19794 1.38903   1.000 62.59308  ? 109  LEU A CD1 1 
ATOM   2569 C  CD2 . LEU B 1 110 ? 9.03656   -28.52147 1.91446   1.000 57.06966  ? 109  LEU A CD2 1 
ATOM   2570 N  N   . LEU B 1 111 ? 5.36174   -31.33307 3.38827   1.000 59.50479  ? 110  LEU A N   1 
ATOM   2571 C  CA  . LEU B 1 111 ? 4.84668   -32.52258 2.71881   1.000 59.45228  ? 110  LEU A CA  1 
ATOM   2572 C  C   . LEU B 1 111 ? 3.33016   -32.47751 2.60127   1.000 63.37364  ? 110  LEU A C   1 
ATOM   2573 O  O   . LEU B 1 111 ? 2.76490   -33.02621 1.64791   1.000 65.69132  ? 110  LEU A O   1 
ATOM   2574 C  CB  . LEU B 1 111 ? 5.26152   -33.79289 3.46374   1.000 56.64350  ? 110  LEU A CB  1 
ATOM   2575 C  CG  . LEU B 1 111 ? 6.74373   -34.15595 3.55395   1.000 55.58889  ? 110  LEU A CG  1 
ATOM   2576 C  CD1 . LEU B 1 111 ? 6.89452   -35.63974 3.73302   1.000 54.62893  ? 110  LEU A CD1 1 
ATOM   2577 C  CD2 . LEU B 1 111 ? 7.50590   -33.70138 2.33806   1.000 54.11759  ? 110  LEU A CD2 1 
ATOM   2578 N  N   . CYS B 1 112 ? 2.65645   -31.80518 3.53870   1.000 63.80052  ? 111  CYS A N   1 
ATOM   2579 C  CA  . CYS B 1 112 ? 1.20212   -31.70098 3.46078   1.000 66.27482  ? 111  CYS A CA  1 
ATOM   2580 C  C   . CYS B 1 112 ? 0.76372   -30.61265 2.49115   1.000 67.37197  ? 111  CYS A C   1 
ATOM   2581 O  O   . CYS B 1 112 ? -0.24359  -30.76457 1.78922   1.000 69.19729  ? 111  CYS A O   1 
ATOM   2582 C  CB  . CYS B 1 112 ? 0.63828   -31.39758 4.84221   1.000 69.19266  ? 111  CYS A CB  1 
ATOM   2583 S  SG  . CYS B 1 112 ? 0.81655   -32.73809 5.98106   1.000 77.84183  ? 111  CYS A SG  1 
ATOM   2584 N  N   . ASP B 1 113 ? 1.50043   -29.50642 2.45597   1.000 67.90147  ? 112  ASP A N   1 
ATOM   2585 C  CA  . ASP B 1 113 ? 1.12762   -28.31698 1.69573   1.000 69.45393  ? 112  ASP A CA  1 
ATOM   2586 C  C   . ASP B 1 113 ? 2.33823   -27.83164 0.92112   1.000 71.05648  ? 112  ASP A C   1 
ATOM   2587 O  O   . ASP B 1 113 ? 3.06994   -26.94211 1.37846   1.000 72.07383  ? 112  ASP A O   1 
ATOM   2588 C  CB  . ASP B 1 113 ? 0.58949   -27.21585 2.60701   1.000 69.85600  ? 112  ASP A CB  1 
ATOM   2589 C  CG  . ASP B 1 113 ? -0.85935  -27.40430 2.92655   1.000 73.68266  ? 112  ASP A CG  1 
ATOM   2590 O  OD1 . ASP B 1 113 ? -1.66199  -27.53837 1.97186   1.000 77.47715  ? 112  ASP A OD1 1 
ATOM   2591 O  OD2 . ASP B 1 113 ? -1.18655  -27.45161 4.12662   1.000 73.53582  ? 112  ASP A OD2 1 
ATOM   2592 N  N   . PRO B 1 114 ? 2.59844   -28.41653 -0.24114  1.000 68.09831  ? 113  PRO A N   1 
ATOM   2593 C  CA  . PRO B 1 114 ? 3.72170   -27.95160 -1.05693  1.000 68.66532  ? 113  PRO A CA  1 
ATOM   2594 C  C   . PRO B 1 114 ? 3.51267   -26.51184 -1.51811  1.000 74.23750  ? 113  PRO A C   1 
ATOM   2595 O  O   . PRO B 1 114 ? 2.38587   -26.02095 -1.61177  1.000 75.25692  ? 113  PRO A O   1 
ATOM   2596 C  CB  . PRO B 1 114 ? 3.72474   -28.93559 -2.23308  1.000 70.01082  ? 113  PRO A CB  1 
ATOM   2597 C  CG  . PRO B 1 114 ? 3.05272   -30.18491 -1.66766  1.000 67.58995  ? 113  PRO A CG  1 
ATOM   2598 C  CD  . PRO B 1 114 ? 1.98276   -29.64457 -0.77427  1.000 68.03412  ? 113  PRO A CD  1 
ATOM   2599 N  N   . ASN B 1 115 ? 4.62783   -25.82354 -1.77950  1.000 77.62394  ? 114  ASN A N   1 
ATOM   2600 C  CA  . ASN B 1 115 ? 4.63805   -24.44910 -2.27940  1.000 88.78007  ? 114  ASN A CA  1 
ATOM   2601 C  C   . ASN B 1 115 ? 5.09979   -24.36218 -3.73468  1.000 94.28471  ? 114  ASN A C   1 
ATOM   2602 O  O   . ASN B 1 115 ? 6.30811   -24.29415 -4.00626  1.000 96.52967  ? 114  ASN A O   1 
ATOM   2603 C  CB  . ASN B 1 115 ? 5.50954   -23.55586 -1.38960  1.000 90.08133  ? 114  ASN A CB  1 
ATOM   2604 C  CG  . ASN B 1 115 ? 4.98645   -23.44012 0.03448   1.000 86.69195  ? 114  ASN A CG  1 
ATOM   2605 O  OD1 . ASN B 1 115 ? 3.77538   -23.44410 0.26895   1.000 89.47141  ? 114  ASN A OD1 1 
ATOM   2606 N  ND2 . ASN B 1 115 ? 5.90334   -23.30037 0.99184   1.000 82.19684  ? 114  ASN A ND2 1 
ATOM   2607 N  N   . PRO B 1 116 ? 4.17892   -24.36641 -4.71114  1.000 97.32934  ? 115  PRO A N   1 
ATOM   2608 C  CA  . PRO B 1 116 ? 4.56339   -24.14235 -6.11538  1.000 101.45740 ? 115  PRO A CA  1 
ATOM   2609 C  C   . PRO B 1 116 ? 4.88573   -22.68503 -6.40399  1.000 112.85993 ? 115  PRO A C   1 
ATOM   2610 O  O   . PRO B 1 116 ? 4.75530   -22.23715 -7.54624  1.000 113.97909 ? 115  PRO A O   1 
ATOM   2611 C  CB  . PRO B 1 116 ? 3.32726   -24.59232 -6.90460  1.000 94.93900  ? 115  PRO A CB  1 
ATOM   2612 C  CG  . PRO B 1 116 ? 2.54535   -25.41905 -5.96264  1.000 93.03675  ? 115  PRO A CG  1 
ATOM   2613 C  CD  . PRO B 1 116 ? 2.79372   -24.84136 -4.60184  1.000 91.57934  ? 115  PRO A CD  1 
ATOM   2614 N  N   . ASP B 1 117 ? 5.28871   -21.93259 -5.37767  1.000 120.36096 ? 116  ASP A N   1 
ATOM   2615 C  CA  . ASP B 1 117 ? 5.55406   -20.50706 -5.54935  1.000 134.84643 ? 116  ASP A CA  1 
ATOM   2616 C  C   . ASP B 1 117 ? 6.85123   -20.27556 -6.31454  1.000 141.64538 ? 116  ASP A C   1 
ATOM   2617 O  O   . ASP B 1 117 ? 6.85381   -19.67235 -7.39412  1.000 151.13920 ? 116  ASP A O   1 
ATOM   2618 C  CB  . ASP B 1 117 ? 5.61660   -19.82453 -4.17768  1.000 147.61960 ? 116  ASP A CB  1 
ATOM   2619 C  CG  . ASP B 1 117 ? 6.57375   -20.52606 -3.20134  1.000 148.22422 ? 116  ASP A CG  1 
ATOM   2620 O  OD1 . ASP B 1 117 ? 7.66614   -20.97810 -3.61950  1.000 146.99736 ? 116  ASP A OD1 1 
ATOM   2621 O  OD2 . ASP B 1 117 ? 6.23761   -20.60218 -2.00097  1.000 150.23566 ? 116  ASP A OD2 1 
ATOM   2622 N  N   . ASP B 1 118 ? 7.96365   -20.75683 -5.77086  1.000 135.31693 ? 117  ASP A N   1 
ATOM   2623 C  CA  . ASP B 1 118 ? 9.26286   -20.72058 -6.44134  1.000 135.86530 ? 117  ASP A CA  1 
ATOM   2624 C  C   . ASP B 1 118 ? 9.86480   -22.08601 -6.15211  1.000 121.22395 ? 117  ASP A C   1 
ATOM   2625 O  O   . ASP B 1 118 ? 10.75249  -22.23824 -5.30233  1.000 116.39899 ? 117  ASP A O   1 
ATOM   2626 C  CB  . ASP B 1 118 ? 10.13805  -19.55932 -5.95635  1.000 144.51162 ? 117  ASP A CB  1 
ATOM   2627 C  CG  . ASP B 1 118 ? 11.30372  -19.26336 -6.90634  1.000 145.40047 ? 117  ASP A CG  1 
ATOM   2628 O  OD1 . ASP B 1 118 ? 11.42082  -19.95083 -7.94291  1.000 145.07474 ? 117  ASP A OD1 1 
ATOM   2629 O  OD2 . ASP B 1 118 ? 12.09130  -18.33147 -6.63418  1.000 149.04729 ? 117  ASP A OD2 1 
ATOM   2630 N  N   . PRO B 1 119 ? 9.36899   -23.11943 -6.83003  1.000 109.93784 ? 118  PRO A N   1 
ATOM   2631 C  CA  . PRO B 1 119 ? 9.66984   -24.50099 -6.44861  1.000 92.29825  ? 118  PRO A CA  1 
ATOM   2632 C  C   . PRO B 1 119 ? 11.10140  -24.88919 -6.74722  1.000 81.91263  ? 118  PRO A C   1 
ATOM   2633 O  O   . PRO B 1 119 ? 11.86639  -24.10532 -7.31378  1.000 87.05415  ? 118  PRO A O   1 
ATOM   2634 C  CB  . PRO B 1 119 ? 8.69026   -25.31930 -7.30167  1.000 87.81436  ? 118  PRO A CB  1 
ATOM   2635 C  CG  . PRO B 1 119 ? 7.73672   -24.30646 -7.89709  1.000 100.78116 ? 118  PRO A CG  1 
ATOM   2636 C  CD  . PRO B 1 119 ? 8.51204   -23.06253 -8.02076  1.000 110.10803 ? 118  PRO A CD  1 
ATOM   2637 N  N   . LEU B 1 120 ? 11.47821  -26.09794 -6.34241  1.000 73.13175  ? 119  LEU A N   1 
ATOM   2638 C  CA  . LEU B 1 120 ? 12.75651  -26.65913 -6.74247  1.000 66.79782  ? 119  LEU A CA  1 
ATOM   2639 C  C   . LEU B 1 120 ? 12.64370  -27.59444 -7.93061  1.000 64.55684  ? 119  LEU A C   1 
ATOM   2640 O  O   . LEU B 1 120 ? 13.64734  -27.83581 -8.60878  1.000 63.49852  ? 119  LEU A O   1 
ATOM   2641 C  CB  . LEU B 1 120 ? 13.38061  -27.41777 -5.56814  1.000 60.50909  ? 119  LEU A CB  1 
ATOM   2642 C  CG  . LEU B 1 120 ? 14.36580  -26.64818 -4.70330  1.000 59.45058  ? 119  LEU A CG  1 
ATOM   2643 C  CD1 . LEU B 1 120 ? 15.14284  -27.62601 -3.86050  1.000 53.82954  ? 119  LEU A CD1 1 
ATOM   2644 C  CD2 . LEU B 1 120 ? 15.30992  -25.85211 -5.58965  1.000 60.77867  ? 119  LEU A CD2 1 
ATOM   2645 N  N   . VAL B 1 121 ? 11.45143  -28.10324 -8.21364  1.000 64.39670  ? 120  VAL A N   1 
ATOM   2646 C  CA  . VAL B 1 121 ? 11.26415  -28.94023 -9.39081  1.000 62.47547  ? 120  VAL A CA  1 
ATOM   2647 C  C   . VAL B 1 121 ? 10.08859  -28.37402 -10.17781 1.000 62.95689  ? 120  VAL A C   1 
ATOM   2648 O  O   . VAL B 1 121 ? 8.92556   -28.69564 -9.88573  1.000 61.13872  ? 120  VAL A O   1 
ATOM   2649 C  CB  . VAL B 1 121 ? 11.04323  -30.41472 -9.01830  1.000 61.24553  ? 120  VAL A CB  1 
ATOM   2650 C  CG1 . VAL B 1 121 ? 11.11786  -31.29091 -10.28719 1.000 59.57616  ? 120  VAL A CG1 1 
ATOM   2651 C  CG2 . VAL B 1 121 ? 12.04392  -30.86970 -7.93752  1.000 56.32040  ? 120  VAL A CG2 1 
ATOM   2652 N  N   . PRO B 1 122 ? 10.35317  -27.53078 -11.18200 1.000 62.43208  ? 121  PRO A N   1 
ATOM   2653 C  CA  . PRO B 1 122 ? 9.25027   -26.86647 -11.89987 1.000 63.09995  ? 121  PRO A CA  1 
ATOM   2654 C  C   . PRO B 1 122 ? 8.25104   -27.82795 -12.51911 1.000 62.98360  ? 121  PRO A C   1 
ATOM   2655 O  O   . PRO B 1 122 ? 7.05159   -27.53638 -12.52567 1.000 63.55909  ? 121  PRO A O   1 
ATOM   2656 C  CB  . PRO B 1 122 ? 9.98418   -26.05306 -12.97764 1.000 59.98719  ? 121  PRO A CB  1 
ATOM   2657 C  CG  . PRO B 1 122 ? 11.34560  -25.82806 -12.41770 1.000 60.16926  ? 121  PRO A CG  1 
ATOM   2658 C  CD  . PRO B 1 122 ? 11.67550  -27.06421 -11.63051 1.000 61.15850  ? 121  PRO A CD  1 
ATOM   2659 N  N   . GLU B 1 123 ? 8.70847   -28.96243 -13.05475 1.000 63.89725  ? 122  GLU A N   1 
ATOM   2660 C  CA  . GLU B 1 123 ? 7.79457   -29.88019 -13.73289 1.000 64.38637  ? 122  GLU A CA  1 
ATOM   2661 C  C   . GLU B 1 123 ? 6.81760   -30.51796 -12.74549 1.000 66.82654  ? 122  GLU A C   1 
ATOM   2662 O  O   . GLU B 1 123 ? 5.61585   -30.63505 -13.02991 1.000 69.56805  ? 122  GLU A O   1 
ATOM   2663 C  CB  . GLU B 1 123 ? 8.61335   -30.93702 -14.48514 1.000 63.45487  ? 122  GLU A CB  1 
ATOM   2664 C  CG  . GLU B 1 123 ? 7.82531   -31.95170 -15.30759 1.000 67.12355  ? 122  GLU A CG  1 
ATOM   2665 C  CD  . GLU B 1 123 ? 7.02442   -31.33439 -16.45575 1.000 73.82712  ? 122  GLU A CD  1 
ATOM   2666 O  OE1 . GLU B 1 123 ? 7.27260   -30.16069 -16.82376 1.000 77.33938  ? 122  GLU A OE1 1 
ATOM   2667 O  OE2 . GLU B 1 123 ? 6.14207   -32.03615 -16.99731 1.000 74.54003  ? 122  GLU A OE2 1 
ATOM   2668 N  N   . ILE B 1 124 ? 7.30557   -30.88937 -11.55967 1.000 64.61730  ? 123  ILE A N   1 
ATOM   2669 C  CA  . ILE B 1 124 ? 6.42366   -31.43688 -10.53833 1.000 65.32450  ? 123  ILE A CA  1 
ATOM   2670 C  C   . ILE B 1 124 ? 5.45336   -30.37341 -10.05408 1.000 68.69797  ? 123  ILE A C   1 
ATOM   2671 O  O   . ILE B 1 124 ? 4.27774   -30.65706 -9.81075  1.000 71.52681  ? 123  ILE A O   1 
ATOM   2672 C  CB  . ILE B 1 124 ? 7.24453   -32.01157 -9.37304  1.000 62.73021  ? 123  ILE A CB  1 
ATOM   2673 C  CG1 . ILE B 1 124 ? 8.13147   -33.14749 -9.86140  1.000 60.18181  ? 123  ILE A CG1 1 
ATOM   2674 C  CG2 . ILE B 1 124 ? 6.32656   -32.48559 -8.24821  1.000 61.06403  ? 123  ILE A CG2 1 
ATOM   2675 C  CD1 . ILE B 1 124 ? 8.96828   -33.73285 -8.75791  1.000 59.67029  ? 123  ILE A CD1 1 
ATOM   2676 N  N   . ALA B 1 125 ? 5.92962   -29.14077 -9.87834  1.000 66.84131  ? 124  ALA A N   1 
ATOM   2677 C  CA  . ALA B 1 125 ? 5.02393   -28.06782 -9.48567  1.000 69.97960  ? 124  ALA A CA  1 
ATOM   2678 C  C   . ALA B 1 125 ? 3.95036   -27.84203 -10.54231 1.000 74.21021  ? 124  ALA A C   1 
ATOM   2679 O  O   . ALA B 1 125 ? 2.77845   -27.61250 -10.21446 1.000 77.98782  ? 124  ALA A O   1 
ATOM   2680 C  CB  . ALA B 1 125 ? 5.81007   -26.78518 -9.24283  1.000 71.12761  ? 124  ALA A CB  1 
ATOM   2681 N  N   . ARG B 1 126 ? 4.32782   -27.93411 -11.81773 1.000 71.41107  ? 125  ARG A N   1 
ATOM   2682 C  CA  . ARG B 1 126 ? 3.35918   -27.78109 -12.89260 1.000 73.55611  ? 125  ARG A CA  1 
ATOM   2683 C  C   . ARG B 1 126 ? 2.30206   -28.86952 -12.81398 1.000 77.12215  ? 125  ARG A C   1 
ATOM   2684 O  O   . ARG B 1 126 ? 1.10721   -28.59650 -12.95354 1.000 81.18595  ? 125  ARG A O   1 
ATOM   2685 C  CB  . ARG B 1 126 ? 4.05822   -27.83523 -14.24689 1.000 73.19853  ? 125  ARG A CB  1 
ATOM   2686 C  CG  . ARG B 1 126 ? 3.07771   -27.83542 -15.40212 1.000 77.14421  ? 125  ARG A CG  1 
ATOM   2687 C  CD  . ARG B 1 126 ? 3.75962   -28.08650 -16.72553 1.000 77.11388  ? 125  ARG A CD  1 
ATOM   2688 N  NE  . ARG B 1 126 ? 4.15313   -29.48678 -16.87929 1.000 80.89170  ? 125  ARG A NE  1 
ATOM   2689 C  CZ  . ARG B 1 126 ? 3.35854   -30.45786 -17.31668 1.000 80.41321  ? 125  ARG A CZ  1 
ATOM   2690 N  NH1 . ARG B 1 126 ? 2.09437   -30.22929 -17.63522 1.000 83.40235  ? 125  ARG A NH1 1 
ATOM   2691 N  NH2 . ARG B 1 126 ? 3.85274   -31.68472 -17.46270 1.000 77.03395  ? 125  ARG A NH2 1 
ATOM   2692 N  N   . ILE B 1 127 ? 2.73125   -30.11886 -12.60164 1.000 75.22938  ? 126  ILE A N   1 
ATOM   2693 C  CA  . ILE B 1 127 ? 1.77760   -31.21811 -12.45547 1.000 78.03988  ? 126  ILE A CA  1 
ATOM   2694 C  C   . ILE B 1 127 ? 0.87291   -30.98036 -11.25250 1.000 81.29287  ? 126  ILE A C   1 
ATOM   2695 O  O   . ILE B 1 127 ? -0.34899  -31.16405 -11.32536 1.000 83.83991  ? 126  ILE A O   1 
ATOM   2696 C  CB  . ILE B 1 127 ? 2.52171   -32.56370 -12.34873 1.000 76.32268  ? 126  ILE A CB  1 
ATOM   2697 C  CG1 . ILE B 1 127 ? 3.28667   -32.84115 -13.63703 1.000 76.50665  ? 126  ILE A CG1 1 
ATOM   2698 C  CG2 . ILE B 1 127 ? 1.54950   -33.70950 -12.08060 1.000 80.66437  ? 126  ILE A CG2 1 
ATOM   2699 C  CD1 . ILE B 1 127 ? 2.38204   -32.92782 -14.83577 1.000 80.86599  ? 126  ILE A CD1 1 
ATOM   2700 N  N   . TYR B 1 128 ? 1.45995   -30.56253 -10.13081 1.000 78.74592  ? 127  TYR A N   1 
ATOM   2701 C  CA  . TYR B 1 128 ? 0.68392   -30.28062 -8.93232  1.000 79.97675  ? 127  TYR A CA  1 
ATOM   2702 C  C   . TYR B 1 128 ? -0.39983  -29.25428 -9.22212  1.000 83.26142  ? 127  TYR A C   1 
ATOM   2703 O  O   . TYR B 1 128 ? -1.54839  -29.40930 -8.79138  1.000 84.12498  ? 127  TYR A O   1 
ATOM   2704 C  CB  . TYR B 1 128 ? 1.62634   -29.79226 -7.82962  1.000 78.72929  ? 127  TYR A CB  1 
ATOM   2705 C  CG  . TYR B 1 128 ? 0.98380   -29.55868 -6.48207  1.000 79.13320  ? 127  TYR A CG  1 
ATOM   2706 C  CD1 . TYR B 1 128 ? 0.77888   -30.61237 -5.60653  1.000 78.43215  ? 127  TYR A CD1 1 
ATOM   2707 C  CD2 . TYR B 1 128 ? 0.61495   -28.28411 -6.07100  1.000 80.96966  ? 127  TYR A CD2 1 
ATOM   2708 C  CE1 . TYR B 1 128 ? 0.20400   -30.41406 -4.36725  1.000 79.46611  ? 127  TYR A CE1 1 
ATOM   2709 C  CE2 . TYR B 1 128 ? 0.03730   -28.07070 -4.82698  1.000 80.80116  ? 127  TYR A CE2 1 
ATOM   2710 C  CZ  . TYR B 1 128 ? -0.16635  -29.14227 -3.97609  1.000 80.33739  ? 127  TYR A CZ  1 
ATOM   2711 O  OH  . TYR B 1 128 ? -0.73534  -28.95893 -2.72792  1.000 79.76890  ? 127  TYR A OH  1 
ATOM   2712 N  N   . LYS B 1 129 ? -0.06264  -28.21986 -9.98906  1.000 82.87270  ? 128  LYS A N   1 
ATOM   2713 C  CA  . LYS B 1 129 ? -1.02948  -27.17805 -10.30670 1.000 85.26165  ? 128  LYS A CA  1 
ATOM   2714 C  C   . LYS B 1 129 ? -1.99277  -27.58353 -11.41630 1.000 89.03079  ? 128  LYS A C   1 
ATOM   2715 O  O   . LYS B 1 129 ? -3.07010  -26.98990 -11.52797 1.000 93.26019  ? 128  LYS A O   1 
ATOM   2716 C  CB  . LYS B 1 129 ? -0.30423  -25.88883 -10.69858 1.000 83.20219  ? 128  LYS A CB  1 
ATOM   2717 C  CG  . LYS B 1 129 ? 0.44157   -25.23896 -9.55058  1.000 83.71489  ? 128  LYS A CG  1 
ATOM   2718 C  CD  . LYS B 1 129 ? 1.12403   -23.95489 -9.97810  1.000 86.75152  ? 128  LYS A CD  1 
ATOM   2719 C  CE  . LYS B 1 129 ? 0.65444   -22.76672 -9.15654  1.000 89.94258  ? 128  LYS A CE  1 
ATOM   2720 N  NZ  . LYS B 1 129 ? -0.79202  -22.46425 -9.38942  1.000 92.68047  ? 128  LYS A NZ  1 
ATOM   2721 N  N   . THR B 1 130 ? -1.63641  -28.57932 -12.22512 1.000 88.50866  ? 129  THR A N   1 
ATOM   2722 C  CA  . THR B 1 130 ? -2.36300  -28.93729 -13.43914 1.000 91.06038  ? 129  THR A CA  1 
ATOM   2723 C  C   . THR B 1 130 ? -3.14997  -30.23387 -13.34707 1.000 93.81329  ? 129  THR A C   1 
ATOM   2724 O  O   . THR B 1 130 ? -4.29545  -30.28412 -13.79868 1.000 100.91581 ? 129  THR A O   1 
ATOM   2725 C  CB  . THR B 1 130 ? -1.36945  -29.03345 -14.60306 1.000 89.77211  ? 129  THR A CB  1 
ATOM   2726 O  OG1 . THR B 1 130 ? -1.00510  -27.71431 -15.02315 1.000 88.78755  ? 129  THR A OG1 1 
ATOM   2727 C  CG2 . THR B 1 130 ? -1.94087  -29.82382 -15.77480 1.000 96.77147  ? 129  THR A CG2 1 
ATOM   2728 N  N   . ASP B 1 131 ? -2.57177  -31.29295 -12.77539 1.000 91.76935  ? 130  ASP A N   1 
ATOM   2729 C  CA  . ASP B 1 131 ? -3.20943  -32.60331 -12.71307 1.000 92.41746  ? 130  ASP A CA  1 
ATOM   2730 C  C   . ASP B 1 131 ? -2.91307  -33.17580 -11.32457 1.000 91.21082  ? 130  ASP A C   1 
ATOM   2731 O  O   . ASP B 1 131 ? -2.12706  -34.10819 -11.16558 1.000 89.70216  ? 130  ASP A O   1 
ATOM   2732 C  CB  . ASP B 1 131 ? -2.71864  -33.52545 -13.83376 1.000 92.91489  ? 130  ASP A CB  1 
ATOM   2733 C  CG  . ASP B 1 131 ? -3.57176  -34.77497 -13.98372 1.000 95.61026  ? 130  ASP A CG  1 
ATOM   2734 O  OD1 . ASP B 1 131 ? -4.47769  -34.97866 -13.14780 1.000 97.32745  ? 130  ASP A OD1 1 
ATOM   2735 O  OD2 . ASP B 1 131 ? -3.33440  -35.55351 -14.93613 1.000 92.89474  ? 130  ASP A OD2 1 
ATOM   2736 N  N   . ARG B 1 132 ? -3.55468  -32.58375 -10.30996 1.000 91.74649  ? 131  ARG A N   1 
ATOM   2737 C  CA  . ARG B 1 132 ? -3.34673  -33.00275 -8.92619  1.000 88.62170  ? 131  ARG A CA  1 
ATOM   2738 C  C   . ARG B 1 132 ? -3.54721  -34.50238 -8.75547  1.000 88.73685  ? 131  ARG A C   1 
ATOM   2739 O  O   . ARG B 1 132 ? -2.89443  -35.13027 -7.91868  1.000 85.85271  ? 131  ARG A O   1 
ATOM   2740 C  CB  . ARG B 1 132 ? -4.28495  -32.25267 -7.98416  1.000 87.21507  ? 131  ARG A CB  1 
ATOM   2741 C  CG  . ARG B 1 132 ? -3.96252  -32.49750 -6.50899  1.000 84.73631  ? 131  ARG A CG  1 
ATOM   2742 C  CD  . ARG B 1 132 ? -2.63441  -31.88698 -6.09269  1.000 83.79342  ? 131  ARG A CD  1 
ATOM   2743 N  NE  . ARG B 1 132 ? -2.57622  -30.48583 -6.48704  1.000 86.22956  ? 131  ARG A NE  1 
ATOM   2744 C  CZ  . ARG B 1 132 ? -3.19319  -29.50567 -5.83866  1.000 87.34288  ? 131  ARG A CZ  1 
ATOM   2745 N  NH1 . ARG B 1 132 ? -3.89596  -29.73697 -4.74080  1.000 87.04785  ? 131  ARG A NH1 1 
ATOM   2746 N  NH2 . ARG B 1 132 ? -3.11927  -28.26541 -6.31297  1.000 87.01460  ? 131  ARG A NH2 1 
ATOM   2747 N  N   . GLU B 1 133 ? -4.51272  -35.08122 -9.46918  1.000 91.01787  ? 132  GLU A N   1 
ATOM   2748 C  CA  . GLU B 1 133 ? -4.71029  -36.52122 -9.36632  1.000 90.79693  ? 132  GLU A CA  1 
ATOM   2749 C  C   . GLU B 1 133 ? -3.48361  -37.27507 -9.86432  1.000 88.86828  ? 132  GLU A C   1 
ATOM   2750 O  O   . GLU B 1 133 ? -3.06375  -38.26770 -9.25740  1.000 87.64714  ? 132  GLU A O   1 
ATOM   2751 C  CB  . GLU B 1 133 ? -5.96974  -36.92445 -10.11091 1.000 94.36406  ? 132  GLU A CB  1 
ATOM   2752 C  CG  . GLU B 1 133 ? -6.18321  -38.40475 -10.16942 1.000 100.24780 ? 132  GLU A CG  1 
ATOM   2753 C  CD  . GLU B 1 133 ? -7.44294  -38.73653 -10.91855 1.000 111.04468 ? 132  GLU A CD  1 
ATOM   2754 O  OE1 . GLU B 1 133 ? -8.33887  -37.85974 -10.94993 1.000 109.32226 ? 132  GLU A OE1 1 
ATOM   2755 O  OE2 . GLU B 1 133 ? -7.54413  -39.86032 -11.45962 1.000 109.70297 ? 132  GLU A OE2 1 
ATOM   2756 N  N   . LYS B 1 134 ? -2.87545  -36.80175 -10.95500 1.000 88.82893  ? 133  LYS A N   1 
ATOM   2757 C  CA  . LYS B 1 134 ? -1.66108  -37.44086 -11.44944 1.000 86.69236  ? 133  LYS A CA  1 
ATOM   2758 C  C   . LYS B 1 134 ? -0.48567  -37.17666 -10.51607 1.000 83.01098  ? 133  LYS A C   1 
ATOM   2759 O  O   . LYS B 1 134 ? 0.34387   -38.06707 -10.29023 1.000 80.78042  ? 133  LYS A O   1 
ATOM   2760 C  CB  . LYS B 1 134 ? -1.35337  -36.94738 -12.85930 1.000 87.85749  ? 133  LYS A CB  1 
ATOM   2761 C  CG  . LYS B 1 134 ? -0.13328  -37.56280 -13.48556 1.000 84.45697  ? 133  LYS A CG  1 
ATOM   2762 C  CD  . LYS B 1 134 ? -0.03135  -37.13623 -14.93661 1.000 87.98867  ? 133  LYS A CD  1 
ATOM   2763 C  CE  . LYS B 1 134 ? 1.35396   -37.40501 -15.48144 1.000 85.21397  ? 133  LYS A CE  1 
ATOM   2764 N  NZ  . LYS B 1 134 ? 1.73437   -36.41745 -16.52572 1.000 86.40019  ? 133  LYS A NZ  1 
ATOM   2765 N  N   . TYR B 1 135 ? -0.39472  -35.95684 -9.96927  1.000 83.58430  ? 134  TYR A N   1 
ATOM   2766 C  CA  . TYR B 1 135 ? 0.60958   -35.66705 -8.94677  1.000 80.01415  ? 134  TYR A CA  1 
ATOM   2767 C  C   . TYR B 1 135 ? 0.48720   -36.63123 -7.77428  1.000 78.26911  ? 134  TYR A C   1 
ATOM   2768 O  O   . TYR B 1 135 ? 1.49069   -37.16167 -7.28607  1.000 75.32636  ? 134  TYR A O   1 
ATOM   2769 C  CB  . TYR B 1 135 ? 0.48505   -34.21851 -8.45756  1.000 79.50248  ? 134  TYR A CB  1 
ATOM   2770 C  CG  . TYR B 1 135 ? 1.26902   -33.93469 -7.17682  1.000 77.68693  ? 134  TYR A CG  1 
ATOM   2771 C  CD1 . TYR B 1 135 ? 0.70546   -34.18576 -5.91965  1.000 78.03597  ? 134  TYR A CD1 1 
ATOM   2772 C  CD2 . TYR B 1 135 ? 2.56001   -33.41249 -7.21654  1.000 73.70100  ? 134  TYR A CD2 1 
ATOM   2773 C  CE1 . TYR B 1 135 ? 1.40181   -33.94330 -4.75007  1.000 74.97500  ? 134  TYR A CE1 1 
ATOM   2774 C  CE2 . TYR B 1 135 ? 3.26782   -33.15874 -6.03594  1.000 70.49698  ? 134  TYR A CE2 1 
ATOM   2775 C  CZ  . TYR B 1 135 ? 2.67641   -33.43042 -4.80876  1.000 72.02614  ? 134  TYR A CZ  1 
ATOM   2776 O  OH  . TYR B 1 135 ? 3.34665   -33.19913 -3.62583  1.000 70.01646  ? 134  TYR A OH  1 
ATOM   2777 N  N   . ASN B 1 136 ? -0.73871  -36.83395 -7.28114  1.000 80.61091  ? 135  ASN A N   1 
ATOM   2778 C  CA  . ASN B 1 136 ? -0.95840  -37.74688 -6.16270  1.000 80.49852  ? 135  ASN A CA  1 
ATOM   2779 C  C   . ASN B 1 136 ? -0.57593  -39.17143 -6.53409  1.000 79.43242  ? 135  ASN A C   1 
ATOM   2780 O  O   . ASN B 1 136 ? 0.03414   -39.88025 -5.72927  1.000 75.98294  ? 135  ASN A O   1 
ATOM   2781 C  CB  . ASN B 1 136 ? -2.42017  -37.69767 -5.69808  1.000 81.97645  ? 135  ASN A CB  1 
ATOM   2782 C  CG  . ASN B 1 136 ? -2.76700  -36.41647 -4.94760  1.000 84.03511  ? 135  ASN A CG  1 
ATOM   2783 O  OD1 . ASN B 1 136 ? -1.89825  -35.76337 -4.36238  1.000 83.08489  ? 135  ASN A OD1 1 
ATOM   2784 N  ND2 . ASN B 1 136 ? -4.05084  -36.06727 -4.94237  1.000 87.23548  ? 135  ASN A ND2 1 
ATOM   2785 N  N   . ARG B 1 137 ? -0.94412  -39.61764 -7.74171  1.000 81.40365  ? 136  ARG A N   1 
ATOM   2786 C  CA  . ARG B 1 137 ? -0.59900  -40.97607 -8.15343  1.000 80.71772  ? 136  ARG A CA  1 
ATOM   2787 C  C   . ARG B 1 137 ? 0.90849   -41.16336 -8.18758  1.000 76.54411  ? 136  ARG A C   1 
ATOM   2788 O  O   . ARG B 1 137 ? 1.43009   -42.16356 -7.69167  1.000 76.15786  ? 136  ARG A O   1 
ATOM   2789 C  CB  . ARG B 1 137 ? -1.22483  -41.30945 -9.51158  1.000 83.15981  ? 136  ARG A CB  1 
ATOM   2790 C  CG  . ARG B 1 137 ? -0.84739  -42.70104 -10.03712 1.000 83.84096  ? 136  ARG A CG  1 
ATOM   2791 C  CD  . ARG B 1 137 ? -1.43906  -43.00559 -11.43004 1.000 89.55897  ? 136  ARG A CD  1 
ATOM   2792 N  NE  . ARG B 1 137 ? -1.28928  -41.88993 -12.36138 1.000 88.38338  ? 136  ARG A NE  1 
ATOM   2793 C  CZ  . ARG B 1 137 ? -0.27672  -41.72964 -13.20467 1.000 89.78932  ? 136  ARG A CZ  1 
ATOM   2794 N  NH1 . ARG B 1 137 ? 0.76457   -42.54508 -13.20102 1.000 91.21217  ? 136  ARG A NH1 1 
ATOM   2795 N  NH2 . ARG B 1 137 ? -0.28198  -40.68965 -14.03337 1.000 87.81153  ? 136  ARG A NH2 1 
ATOM   2796 N  N   . ILE B 1 138 ? 1.63002   -40.20831 -8.76761  1.000 72.76061  ? 137  ILE A N   1 
ATOM   2797 C  CA  . ILE B 1 138 ? 3.07440   -40.37594 -8.85965  1.000 69.60852  ? 137  ILE A CA  1 
ATOM   2798 C  C   . ILE B 1 138 ? 3.70167   -40.27689 -7.47853  1.000 67.41391  ? 137  ILE A C   1 
ATOM   2799 O  O   . ILE B 1 138 ? 4.62056   -41.03375 -7.14823  1.000 63.93751  ? 137  ILE A O   1 
ATOM   2800 C  CB  . ILE B 1 138 ? 3.69368   -39.36273 -9.84513  1.000 67.26183  ? 137  ILE A CB  1 
ATOM   2801 C  CG1 . ILE B 1 138 ? 3.03594   -39.48568 -11.21966 1.000 71.21861  ? 137  ILE A CG1 1 
ATOM   2802 C  CG2 . ILE B 1 138 ? 5.19135   -39.56390 -9.95514  1.000 60.99824  ? 137  ILE A CG2 1 
ATOM   2803 C  CD1 . ILE B 1 138 ? 3.43301   -38.39422 -12.17087 1.000 68.85704  ? 137  ILE A CD1 1 
ATOM   2804 N  N   . ALA B 1 139 ? 3.21990   -39.34868 -6.64673  1.000 68.06915  ? 138  ALA A N   1 
ATOM   2805 C  CA  . ALA B 1 139 ? 3.74472   -39.23460 -5.28978  1.000 66.01121  ? 138  ALA A CA  1 
ATOM   2806 C  C   . ALA B 1 139 ? 3.50465   -40.51510 -4.50644  1.000 66.49856  ? 138  ALA A C   1 
ATOM   2807 O  O   . ALA B 1 139 ? 4.39739   -40.99473 -3.80050  1.000 64.49255  ? 138  ALA A O   1 
ATOM   2808 C  CB  . ALA B 1 139 ? 3.11606   -38.03945 -4.57345  1.000 66.28169  ? 138  ALA A CB  1 
ATOM   2809 N  N   . ARG B 1 140 ? 2.31706   -41.10572 -4.64452  1.000 67.65093  ? 139  ARG A N   1 
ATOM   2810 C  CA  . ARG B 1 140 ? 2.06007   -42.37991 -3.99141  1.000 70.88033  ? 139  ARG A CA  1 
ATOM   2811 C  C   . ARG B 1 140 ? 2.97713   -43.47348 -4.52665  1.000 70.15864  ? 139  ARG A C   1 
ATOM   2812 O  O   . ARG B 1 140 ? 3.50904   -44.26792 -3.75040  1.000 68.48697  ? 139  ARG A O   1 
ATOM   2813 C  CB  . ARG B 1 140 ? 0.59567   -42.78004 -4.14932  1.000 78.37117  ? 139  ARG A CB  1 
ATOM   2814 C  CG  . ARG B 1 140 ? -0.39491  -41.86735 -3.44499  1.000 80.93494  ? 139  ARG A CG  1 
ATOM   2815 C  CD  . ARG B 1 140 ? -1.77491  -42.48662 -3.49445  1.000 91.50785  ? 139  ARG A CD  1 
ATOM   2816 N  NE  . ARG B 1 140 ? -2.41974  -42.20482 -4.76884  1.000 104.36759 ? 139  ARG A NE  1 
ATOM   2817 C  CZ  . ARG B 1 140 ? -2.64476  -43.13044 -5.69168  1.000 116.90467 ? 139  ARG A CZ  1 
ATOM   2818 N  NH1 . ARG B 1 140 ? -2.31152  -44.39570 -5.49478  1.000 115.42225 ? 139  ARG A NH1 1 
ATOM   2819 N  NH2 . ARG B 1 140 ? -3.19264  -42.77556 -6.84943  1.000 122.75468 ? 139  ARG A NH2 1 
ATOM   2820 N  N   . GLU B 1 141 ? 3.17761   -43.53402 -5.84790  1.000 73.59719  ? 140  GLU A N   1 
ATOM   2821 C  CA  . GLU B 1 141 ? 4.02745   -44.57795 -6.42925  1.000 70.66318  ? 140  GLU A CA  1 
ATOM   2822 C  C   . GLU B 1 141 ? 5.47900   -44.44241 -5.97927  1.000 67.79693  ? 140  GLU A C   1 
ATOM   2823 O  O   . GLU B 1 141 ? 6.12932   -45.43987 -5.63532  1.000 65.33647  ? 140  GLU A O   1 
ATOM   2824 C  CB  . GLU B 1 141 ? 3.92881   -44.53716 -7.95269  1.000 69.99461  ? 140  GLU A CB  1 
ATOM   2825 C  CG  . GLU B 1 141 ? 2.55495   -44.90422 -8.45276  1.000 74.57338  ? 140  GLU A CG  1 
ATOM   2826 C  CD  . GLU B 1 141 ? 2.37552   -44.62867 -9.92366  1.000 83.26350  ? 140  GLU A CD  1 
ATOM   2827 O  OE1 . GLU B 1 141 ? 3.30951   -44.07000 -10.53921 1.000 80.86717  ? 140  GLU A OE1 1 
ATOM   2828 O  OE2 . GLU B 1 141 ? 1.29859   -44.97503 -10.46008 1.000 88.03525  ? 140  GLU A OE2 1 
ATOM   2829 N  N   . TRP B 1 142 ? 5.99709   -43.21034 -5.94412  1.000 64.29417  ? 141  TRP A N   1 
ATOM   2830 C  CA  . TRP B 1 142 ? 7.34632   -42.99639 -5.43285  1.000 61.73212  ? 141  TRP A CA  1 
ATOM   2831 C  C   . TRP B 1 142 ? 7.41925   -43.33408 -3.94871  1.000 61.80453  ? 141  TRP A C   1 
ATOM   2832 O  O   . TRP B 1 142 ? 8.43421   -43.86818 -3.48409  1.000 58.47275  ? 141  TRP A O   1 
ATOM   2833 C  CB  . TRP B 1 142 ? 7.78995   -41.55210 -5.67437  1.000 58.16890  ? 141  TRP A CB  1 
ATOM   2834 C  CG  . TRP B 1 142 ? 8.28068   -41.26281 -7.06716  1.000 57.97486  ? 141  TRP A CG  1 
ATOM   2835 C  CD1 . TRP B 1 142 ? 7.73920   -41.71218 -8.23446  1.000 56.80781  ? 141  TRP A CD1 1 
ATOM   2836 C  CD2 . TRP B 1 142 ? 9.39968   -40.44129 -7.43663  1.000 57.34039  ? 141  TRP A CD2 1 
ATOM   2837 N  NE1 . TRP B 1 142 ? 8.44463   -41.22520 -9.30172  1.000 56.30840  ? 141  TRP A NE1 1 
ATOM   2838 C  CE2 . TRP B 1 142 ? 9.47013   -40.44337 -8.84213  1.000 54.36111  ? 141  TRP A CE2 1 
ATOM   2839 C  CE3 . TRP B 1 142 ? 10.34420  -39.70049 -6.71525  1.000 55.37427  ? 141  TRP A CE3 1 
ATOM   2840 C  CZ2 . TRP B 1 142 ? 10.44649  -39.73827 -9.54221  1.000 54.49300  ? 141  TRP A CZ2 1 
ATOM   2841 C  CZ3 . TRP B 1 142 ? 11.31425  -39.00029 -7.41455  1.000 55.73407  ? 141  TRP A CZ3 1 
ATOM   2842 C  CH2 . TRP B 1 142 ? 11.36081  -39.03174 -8.81098  1.000 52.82889  ? 141  TRP A CH2 1 
ATOM   2843 N  N   . THR B 1 143 ? 6.35385   -43.03691 -3.18771  1.000 61.55615  ? 142  THR A N   1 
ATOM   2844 C  CA  . THR B 1 143 ? 6.32027   -43.45158 -1.78518  1.000 62.36645  ? 142  THR A CA  1 
ATOM   2845 C  C   . THR B 1 143 ? 6.44594   -44.96305 -1.68797  1.000 63.95746  ? 142  THR A C   1 
ATOM   2846 O  O   . THR B 1 143 ? 7.33566   -45.48198 -1.00525  1.000 60.76152  ? 142  THR A O   1 
ATOM   2847 C  CB  . THR B 1 143 ? 5.02084   -42.99767 -1.08959  1.000 62.06963  ? 142  THR A CB  1 
ATOM   2848 O  OG1 . THR B 1 143 ? 4.86800   -41.57914 -1.15892  1.000 62.17522  ? 142  THR A OG1 1 
ATOM   2849 C  CG2 . THR B 1 143 ? 5.01530   -43.41937 0.38114   1.000 61.63441  ? 142  THR A CG2 1 
ATOM   2850 N  N   . GLN B 1 144 ? 5.63547   -45.67638 -2.47613  1.000 65.33033  ? 143  GLN A N   1 
ATOM   2851 C  CA  . GLN B 1 144 ? 5.62579   -47.13560 -2.46536  1.000 66.66759  ? 143  GLN A CA  1 
ATOM   2852 C  C   . GLN B 1 144 ? 6.97224   -47.70022 -2.89475  1.000 62.93050  ? 143  GLN A C   1 
ATOM   2853 O  O   . GLN B 1 144 ? 7.33881   -48.80596 -2.49115  1.000 64.75652  ? 143  GLN A O   1 
ATOM   2854 C  CB  . GLN B 1 144 ? 4.52354   -47.64352 -3.40855  1.000 74.94647  ? 143  GLN A CB  1 
ATOM   2855 C  CG  . GLN B 1 144 ? 3.06823   -47.26759 -3.03925  1.000 84.32206  ? 143  GLN A CG  1 
ATOM   2856 C  CD  . GLN B 1 144 ? 2.06403   -47.54504 -4.18098  1.000 95.96621  ? 143  GLN A CD  1 
ATOM   2857 O  OE1 . GLN B 1 144 ? 2.41475   -48.12439 -5.21757  1.000 92.87107  ? 143  GLN A OE1 1 
ATOM   2858 N  NE2 . GLN B 1 144 ? 0.82605   -47.07946 -4.00617  1.000 94.75325  ? 143  GLN A NE2 1 
ATOM   2859 N  N   . LYS B 1 145 ? 7.72653   -46.95034 -3.70001  1.000 62.15163  ? 144  LYS A N   1 
ATOM   2860 C  CA  . LYS B 1 145 ? 8.98253   -47.45043 -4.25026  1.000 59.41930  ? 144  LYS A CA  1 
ATOM   2861 C  C   . LYS B 1 145 ? 10.19678  -47.20907 -3.35863  1.000 57.54925  ? 144  LYS A C   1 
ATOM   2862 O  O   . LYS B 1 145 ? 11.04199  -48.09931 -3.20518  1.000 57.20458  ? 144  LYS A O   1 
ATOM   2863 C  CB  . LYS B 1 145 ? 9.22365   -46.82285 -5.62182  1.000 58.03851  ? 144  LYS A CB  1 
ATOM   2864 C  CG  . LYS B 1 145 ? 10.37891  -47.44366 -6.36047  1.000 57.45422  ? 144  LYS A CG  1 
ATOM   2865 C  CD  . LYS B 1 145 ? 10.46202  -46.91965 -7.76673  1.000 58.43556  ? 144  LYS A CD  1 
ATOM   2866 C  CE  . LYS B 1 145 ? 11.46108  -47.69714 -8.57294  1.000 60.35836  ? 144  LYS A CE  1 
ATOM   2867 N  NZ  . LYS B 1 145 ? 11.34797  -47.29047 -9.99060  1.000 66.78300  ? 144  LYS A NZ  1 
ATOM   2868 N  N   . TYR B 1 146 ? 10.32234  -46.02463 -2.77713  1.000 56.04645  ? 145  TYR A N   1 
ATOM   2869 C  CA  . TYR B 1 146 ? 11.52226  -45.71165 -2.01779  1.000 55.81805  ? 145  TYR A CA  1 
ATOM   2870 C  C   . TYR B 1 146 ? 11.29953  -45.60530 -0.51589  1.000 58.40556  ? 145  TYR A C   1 
ATOM   2871 O  O   . TYR B 1 146 ? 12.27015  -45.68942 0.24153   1.000 56.77128  ? 145  TYR A O   1 
ATOM   2872 C  CB  . TYR B 1 146 ? 12.14278  -44.39719 -2.51263  1.000 55.67437  ? 145  TYR A CB  1 
ATOM   2873 C  CG  . TYR B 1 146 ? 12.48722  -44.39149 -3.97951  1.000 55.04027  ? 145  TYR A CG  1 
ATOM   2874 C  CD1 . TYR B 1 146 ? 13.67278  -44.95162 -4.43141  1.000 55.67610  ? 145  TYR A CD1 1 
ATOM   2875 C  CD2 . TYR B 1 146 ? 11.63555  -43.81166 -4.91090  1.000 55.57225  ? 145  TYR A CD2 1 
ATOM   2876 C  CE1 . TYR B 1 146 ? 13.99811  -44.94446 -5.76149  1.000 57.23468  ? 145  TYR A CE1 1 
ATOM   2877 C  CE2 . TYR B 1 146 ? 11.95385  -43.79515 -6.24950  1.000 56.65636  ? 145  TYR A CE2 1 
ATOM   2878 C  CZ  . TYR B 1 146 ? 13.13718  -44.36119 -6.66864  1.000 59.88236  ? 145  TYR A CZ  1 
ATOM   2879 O  OH  . TYR B 1 146 ? 13.47005  -44.34892 -7.99902  1.000 62.50575  ? 145  TYR A OH  1 
ATOM   2880 N  N   . ALA B 1 147 ? 10.06541  -45.41383 -0.06489  1.000 58.57002  ? 146  ALA A N   1 
ATOM   2881 C  CA  . ALA B 1 147 ? 9.81868   -45.06878 1.32663   1.000 59.77802  ? 146  ALA A CA  1 
ATOM   2882 C  C   . ALA B 1 147 ? 9.18770   -46.21578 2.11609   1.000 65.41742  ? 146  ALA A C   1 
ATOM   2883 O  O   . ALA B 1 147 ? 8.59045   -45.98318 3.17343   1.000 62.88927  ? 146  ALA A O   1 
ATOM   2884 C  CB  . ALA B 1 147 ? 8.96116   -43.80671 1.40346   1.000 58.43982  ? 146  ALA A CB  1 
ATOM   2885 N  N   . MET B 1 148 ? 9.26959   -47.44617 1.60253   1.000 68.16443  ? 147  MET A N   1 
ATOM   2886 C  CA  . MET B 1 148 ? 8.69572   -48.61820 2.26017   1.000 71.38874  ? 147  MET A CA  1 
ATOM   2887 C  C   . MET B 1 148 ? 9.74214   -49.73439 2.35030   1.000 77.76685  ? 147  MET A C   1 
ATOM   2888 O  O   . MET B 1 148 ? 9.59658   -50.82006 1.78695   1.000 79.50026  ? 147  MET A O   1 
ATOM   2889 C  CB  . MET B 1 148 ? 7.43396   -49.02903 1.52053   1.000 71.23790  ? 147  MET A CB  1 
ATOM   2890 C  CG  . MET B 1 148 ? 6.34100   -48.01750 1.74941   1.000 69.53264  ? 147  MET A CG  1 
ATOM   2891 S  SD  . MET B 1 148 ? 4.89728   -48.32013 0.74678   1.000 86.45652  ? 147  MET A SD  1 
ATOM   2892 C  CE  . MET B 1 148 ? 3.89828   -46.89624 1.17349   1.000 71.89057  ? 147  MET A CE  1 
ATOM   2893 N  N   . GLY B 1 149 ? 10.81153  -49.45607 3.09192   1.000 77.31842  ? 148  GLY A N   1 
ATOM   2894 C  CA  . GLY B 1 149 ? 11.89385  -50.40681 3.26513   1.000 80.67169  ? 148  GLY A CA  1 
ATOM   2895 C  C   . GLY B 1 149 ? 11.71240  -51.28351 4.48850   1.000 82.35296  ? 148  GLY A C   1 
ATOM   2896 O  O   . GLY B 1 149 ? 11.50150  -50.78264 5.59629   1.000 86.35170  ? 148  GLY A O   1 
ATOM   2897 N  N   . ALA B 1 176 ? 3.42032   -37.25213 42.31961  1.000 131.19677 ? 945  ALA A N   1 
ATOM   2898 C  CA  . ALA B 1 176 ? 3.39266   -37.34393 40.86333  1.000 135.74231 ? 945  ALA A CA  1 
ATOM   2899 C  C   . ALA B 1 176 ? 2.69671   -36.12495 40.25831  1.000 141.36290 ? 945  ALA A C   1 
ATOM   2900 O  O   . ALA B 1 176 ? 3.06918   -34.98643 40.54988  1.000 141.12656 ? 945  ALA A O   1 
ATOM   2901 C  CB  . ALA B 1 176 ? 2.70565   -38.62577 40.42403  1.000 129.72360 ? 945  ALA A CB  1 
ATOM   2902 N  N   . ASP B 1 177 ? 1.66796   -36.37038 39.43673  1.000 144.01554 ? 946  ASP A N   1 
ATOM   2903 C  CA  . ASP B 1 177 ? 0.92813   -35.28689 38.78988  1.000 143.84359 ? 946  ASP A CA  1 
ATOM   2904 C  C   . ASP B 1 177 ? 0.18492   -34.41648 39.79273  1.000 143.06953 ? 946  ASP A C   1 
ATOM   2905 O  O   . ASP B 1 177 ? -0.18113  -33.28333 39.45594  1.000 142.78957 ? 946  ASP A O   1 
ATOM   2906 C  CB  . ASP B 1 177 ? -0.03640  -35.82769 37.73005  1.000 145.54548 ? 946  ASP A CB  1 
ATOM   2907 C  CG  . ASP B 1 177 ? 0.66024   -36.14570 36.41130  1.000 145.84531 ? 946  ASP A CG  1 
ATOM   2908 O  OD1 . ASP B 1 177 ? 1.89794   -36.00749 36.34142  1.000 143.29011 ? 946  ASP A OD1 1 
ATOM   2909 O  OD2 . ASP B 1 177 ? -0.03133  -36.51970 35.43936  1.000 147.00189 ? 946  ASP A OD2 1 
ATOM   2910 N  N   . VAL B 1 178 ? -0.06880  -34.92647 41.00193  1.000 143.10674 ? 947  VAL A N   1 
ATOM   2911 C  CA  . VAL B 1 178 ? -0.65837  -34.08697 42.03741  1.000 143.33730 ? 947  VAL A CA  1 
ATOM   2912 C  C   . VAL B 1 178 ? 0.29666   -32.95023 42.37739  1.000 141.62656 ? 947  VAL A C   1 
ATOM   2913 O  O   . VAL B 1 178 ? -0.13771  -31.83481 42.69213  1.000 141.52845 ? 947  VAL A O   1 
ATOM   2914 C  CB  . VAL B 1 178 ? -1.01447  -34.93249 43.28459  1.000 142.39524 ? 947  VAL A CB  1 
ATOM   2915 C  CG1 . VAL B 1 178 ? -2.14038  -35.91857 42.97671  1.000 136.79285 ? 947  VAL A CG1 1 
ATOM   2916 C  CG2 . VAL B 1 178 ? 0.20969   -35.68143 43.81541  1.000 138.54268 ? 947  VAL A CG2 1 
ATOM   2917 N  N   . GLN B 1 179 ? 1.60501   -33.21098 42.32799  1.000 140.82100 ? 948  GLN A N   1 
ATOM   2918 C  CA  . GLN B 1 179 ? 2.62341   -32.18693 42.50993  1.000 138.47474 ? 948  GLN A CA  1 
ATOM   2919 C  C   . GLN B 1 179 ? 3.37097   -31.82617 41.22304  1.000 137.91359 ? 948  GLN A C   1 
ATOM   2920 O  O   . GLN B 1 179 ? 4.29211   -31.00146 41.27317  1.000 134.75732 ? 948  GLN A O   1 
ATOM   2921 C  CB  . GLN B 1 179 ? 3.59072   -32.61182 43.61432  1.000 133.43933 ? 948  GLN A CB  1 
ATOM   2922 C  CG  . GLN B 1 179 ? 2.83184   -33.00422 44.88448  1.000 136.58370 ? 948  GLN A CG  1 
ATOM   2923 C  CD  . GLN B 1 179 ? 1.89144   -31.91834 45.39612  1.000 136.42007 ? 948  GLN A CD  1 
ATOM   2924 O  OE1 . GLN B 1 179 ? 2.24042   -30.73859 45.45083  1.000 135.37292 ? 948  GLN A OE1 1 
ATOM   2925 N  NE2 . GLN B 1 179 ? 0.67827   -32.32397 45.76586  1.000 135.27784 ? 948  GLN A NE2 1 
ATOM   2926 N  N   . LYS B 1 180 ? 3.01851   -32.42869 40.07653  1.000 138.54616 ? 949  LYS A N   1 
ATOM   2927 C  CA  . LYS B 1 180 ? 3.57944   -32.03424 38.78261  1.000 134.91649 ? 949  LYS A CA  1 
ATOM   2928 C  C   . LYS B 1 180 ? 2.89479   -30.79122 38.22083  1.000 132.41655 ? 949  LYS A C   1 
ATOM   2929 O  O   . LYS B 1 180 ? 3.29560   -30.29315 37.16063  1.000 129.47144 ? 949  LYS A O   1 
ATOM   2930 C  CB  . LYS B 1 180 ? 3.49348   -33.18843 37.76668  1.000 136.31624 ? 949  LYS A CB  1 
ATOM   2931 C  CG  . LYS B 1 180 ? 4.19152   -32.91620 36.41974  1.000 137.10127 ? 949  LYS A CG  1 
ATOM   2932 C  CD  . LYS B 1 180 ? 4.08280   -34.05328 35.40994  1.000 139.04814 ? 949  LYS A CD  1 
ATOM   2933 C  CE  . LYS B 1 180 ? 4.68083   -33.63599 34.06348  1.000 138.59325 ? 949  LYS A CE  1 
ATOM   2934 N  NZ  . LYS B 1 180 ? 4.57443   -34.69204 33.01868  1.000 143.38423 ? 949  LYS A NZ  1 
ATOM   2935 N  N   . LEU B 1 181 ? 1.88030   -30.26945 38.91794  1.000 132.55207 ? 950  LEU A N   1 
ATOM   2936 C  CA  . LEU B 1 181 ? 1.39042   -28.93531 38.60237  1.000 127.68780 ? 950  LEU A CA  1 
ATOM   2937 C  C   . LEU B 1 181 ? 2.55853   -27.97030 38.51569  1.000 123.06090 ? 950  LEU A C   1 
ATOM   2938 O  O   . LEU B 1 181 ? 2.54714   -27.04627 37.69780  1.000 122.39617 ? 950  LEU A O   1 
ATOM   2939 C  CB  . LEU B 1 181 ? 0.40479   -28.45990 39.67346  1.000 129.07624 ? 950  LEU A CB  1 
ATOM   2940 C  CG  . LEU B 1 181 ? -0.89056  -29.22562 39.93383  1.000 129.76999 ? 950  LEU A CG  1 
ATOM   2941 C  CD1 . LEU B 1 181 ? -1.73391  -28.48074 40.95182  1.000 130.06376 ? 950  LEU A CD1 1 
ATOM   2942 C  CD2 . LEU B 1 181 ? -1.66905  -29.42792 38.65165  1.000 132.21615 ? 950  LEU A CD2 1 
ATOM   2943 N  N   . GLN B 1 182 ? 3.59463   -28.20853 39.32514  1.000 121.24093 ? 951  GLN A N   1 
ATOM   2944 C  CA  . GLN B 1 182 ? 4.77594   -27.35357 39.34587  1.000 119.00958 ? 951  GLN A CA  1 
ATOM   2945 C  C   . GLN B 1 182 ? 5.55711   -27.44122 38.03978  1.000 119.79479 ? 951  GLN A C   1 
ATOM   2946 O  O   . GLN B 1 182 ? 5.97299   -26.41435 37.49031  1.000 118.68589 ? 951  GLN A O   1 
ATOM   2947 C  CB  . GLN B 1 182 ? 5.67020   -27.74832 40.51470  1.000 114.39713 ? 951  GLN A CB  1 
ATOM   2948 C  CG  . GLN B 1 182 ? 5.04946   -27.51905 41.85939  1.000 109.93959 ? 951  GLN A CG  1 
ATOM   2949 C  CD  . GLN B 1 182 ? 6.09494   -27.31178 42.91934  1.000 104.02219 ? 951  GLN A CD  1 
ATOM   2950 O  OE1 . GLN B 1 182 ? 6.58866   -26.19995 43.10024  1.000 103.99351 ? 951  GLN A OE1 1 
ATOM   2951 N  NE2 . GLN B 1 182 ? 6.45683   -28.38069 43.61686  1.000 99.75432  ? 951  GLN A NE2 1 
ATOM   2952 N  N   . GLN B 1 183 ? 5.79629   -28.66215 37.54058  1.000 122.48284 ? 952  GLN A N   1 
ATOM   2953 C  CA  . GLN B 1 183 ? 6.45404   -28.80783 36.24301  1.000 118.98713 ? 952  GLN A CA  1 
ATOM   2954 C  C   . GLN B 1 183 ? 5.64959   -28.10867 35.15793  1.000 120.30259 ? 952  GLN A C   1 
ATOM   2955 O  O   . GLN B 1 183 ? 6.21670   -27.53669 34.22002  1.000 120.23958 ? 952  GLN A O   1 
ATOM   2956 C  CB  . GLN B 1 183 ? 6.65822   -30.28244 35.90263  1.000 121.49241 ? 952  GLN A CB  1 
ATOM   2957 C  CG  . GLN B 1 183 ? 7.79567   -30.95170 36.66140  1.000 120.32964 ? 952  GLN A CG  1 
ATOM   2958 C  CD  . GLN B 1 183 ? 8.18405   -32.29619 36.05919  1.000 122.16822 ? 952  GLN A CD  1 
ATOM   2959 O  OE1 . GLN B 1 183 ? 7.46892   -32.84061 35.21877  1.000 124.04515 ? 952  GLN A OE1 1 
ATOM   2960 N  NE2 . GLN B 1 183 ? 9.32440   -32.83162 36.48196  1.000 115.67494 ? 952  GLN A NE2 1 
ATOM   2961 N  N   . GLN B 1 184 ? 4.32131   -28.15766 35.26603  1.000 123.92388 ? 953  GLN A N   1 
ATOM   2962 C  CA  . GLN B 1 184 ? 3.47065   -27.36186 34.39101  1.000 124.41266 ? 953  GLN A CA  1 
ATOM   2963 C  C   . GLN B 1 184 ? 3.65239   -25.87621 34.67587  1.000 123.92462 ? 953  GLN A C   1 
ATOM   2964 O  O   . GLN B 1 184 ? 3.84832   -25.07830 33.75330  1.000 126.71771 ? 953  GLN A O   1 
ATOM   2965 C  CB  . GLN B 1 184 ? 2.01280   -27.77463 34.57383  1.000 127.41293 ? 953  GLN A CB  1 
ATOM   2966 C  CG  . GLN B 1 184 ? 1.63588   -29.04352 33.84415  1.000 129.45223 ? 953  GLN A CG  1 
ATOM   2967 C  CD  . GLN B 1 184 ? 0.23886   -29.50805 34.19430  1.000 131.73590 ? 953  GLN A CD  1 
ATOM   2968 O  OE1 . GLN B 1 184 ? -0.37541  -29.00686 35.13693  1.000 131.31544 ? 953  GLN A OE1 1 
ATOM   2969 N  NE2 . GLN B 1 184 ? -0.28030  -30.45351 33.42473  1.000 129.02004 ? 953  GLN A NE2 1 
ATOM   2970 N  N   . LEU B 1 185 ? 3.59020   -25.49028 35.95695  1.000 118.74574 ? 954  LEU A N   1 
ATOM   2971 C  CA  . LEU B 1 185 ? 3.82572   -24.10185 36.34798  1.000 114.57352 ? 954  LEU A CA  1 
ATOM   2972 C  C   . LEU B 1 185 ? 5.18875   -23.61570 35.86988  1.000 110.15594 ? 954  LEU A C   1 
ATOM   2973 O  O   . LEU B 1 185 ? 5.34102   -22.44328 35.50072  1.000 107.38078 ? 954  LEU A O   1 
ATOM   2974 C  CB  . LEU B 1 185 ? 3.70584   -23.95464 37.87190  1.000 114.92058 ? 954  LEU A CB  1 
ATOM   2975 C  CG  . LEU B 1 185 ? 2.32548   -24.05795 38.54233  1.000 114.74733 ? 954  LEU A CG  1 
ATOM   2976 C  CD1 . LEU B 1 185 ? 2.45175   -24.11485 40.06519  1.000 108.56451 ? 954  LEU A CD1 1 
ATOM   2977 C  CD2 . LEU B 1 185 ? 1.40580   -22.91843 38.12118  1.000 113.73727 ? 954  LEU A CD2 1 
ATOM   2978 N  N   . GLN B 1 186 ? 6.17985   -24.50694 35.83325  1.000 109.52632 ? 955  GLN A N   1 
ATOM   2979 C  CA  . GLN B 1 186 ? 7.52832   -24.14624 35.41430  1.000 106.63732 ? 955  GLN A CA  1 
ATOM   2980 C  C   . GLN B 1 186 ? 7.61622   -23.77714 33.93572  1.000 104.90391 ? 955  GLN A C   1 
ATOM   2981 O  O   . GLN B 1 186 ? 8.69534   -23.36702 33.48919  1.000 99.83516  ? 955  GLN A O   1 
ATOM   2982 C  CB  . GLN B 1 186 ? 8.50946   -25.26119 35.74030  1.000 105.44017 ? 955  GLN A CB  1 
ATOM   2983 C  CG  . GLN B 1 186 ? 9.68681   -24.76721 36.53670  1.000 98.68298  ? 955  GLN A CG  1 
ATOM   2984 C  CD  . GLN B 1 186 ? 9.88991   -25.56030 37.79787  1.000 104.38244 ? 955  GLN A CD  1 
ATOM   2985 O  OE1 . GLN B 1 186 ? 8.93620   -26.09184 38.37313  1.000 109.57537 ? 955  GLN A OE1 1 
ATOM   2986 N  NE2 . GLN B 1 186 ? 11.13794  -25.66007 38.23500  1.000 101.42513 ? 955  GLN A NE2 1 
ATOM   2987 N  N   . ASP B 1 187 ? 6.52748   -23.92468 33.16884  1.000 107.91010 ? 956  ASP A N   1 
ATOM   2988 C  CA  . ASP B 1 187 ? 6.48061   -23.39003 31.81075  1.000 103.03930 ? 956  ASP A CA  1 
ATOM   2989 C  C   . ASP B 1 187 ? 6.51992   -21.86782 31.82804  1.000 98.96431  ? 956  ASP A C   1 
ATOM   2990 O  O   . ASP B 1 187 ? 6.54456   -21.24228 30.76236  1.000 95.99300  ? 956  ASP A O   1 
ATOM   2991 C  CB  . ASP B 1 187 ? 5.25001   -23.91109 31.04692  1.000 107.98719 ? 956  ASP A CB  1 
ATOM   2992 C  CG  . ASP B 1 187 ? 3.92593   -23.28870 31.50942  1.000 112.67067 ? 956  ASP A CG  1 
ATOM   2993 O  OD1 . ASP B 1 187 ? 3.90341   -22.40100 32.39002  1.000 111.10563 ? 956  ASP A OD1 1 
ATOM   2994 O  OD2 . ASP B 1 187 ? 2.87673   -23.72674 30.98327  1.000 114.68315 ? 956  ASP A OD2 1 
ATOM   2995 N  N   . ILE B 1 188 ? 6.48689   -21.27506 33.02669  1.000 95.23961  ? 957  ILE A N   1 
ATOM   2996 C  CA  . ILE B 1 188 ? 6.81816   -19.86792 33.19870  1.000 90.66400  ? 957  ILE A CA  1 
ATOM   2997 C  C   . ILE B 1 188 ? 8.20363   -19.59697 32.63590  1.000 86.10635  ? 957  ILE A C   1 
ATOM   2998 O  O   . ILE B 1 188 ? 8.51887   -18.46223 32.25044  1.000 80.39023  ? 957  ILE A O   1 
ATOM   2999 C  CB  . ILE B 1 188 ? 6.74264   -19.48589 34.68723  1.000 90.88671  ? 957  ILE A CB  1 
ATOM   3000 C  CG1 . ILE B 1 188 ? 7.02938   -18.00250 34.87499  1.000 87.37376  ? 957  ILE A CG1 1 
ATOM   3001 C  CG2 . ILE B 1 188 ? 7.75362   -20.27667 35.48659  1.000 89.88654  ? 957  ILE A CG2 1 
ATOM   3002 C  CD1 . ILE B 1 188 ? 7.24546   -17.62390 36.31223  1.000 83.75101  ? 957  ILE A CD1 1 
ATOM   3003 N  N   . LYS B 1 189 ? 9.06738   -20.61952 32.62214  1.000 88.09652  ? 958  LYS A N   1 
ATOM   3004 C  CA  . LYS B 1 189 ? 10.36948  -20.48837 31.98063  1.000 84.22626  ? 958  LYS A CA  1 
ATOM   3005 C  C   . LYS B 1 189 ? 10.19783  -20.02034 30.54223  1.000 80.88651  ? 958  LYS A C   1 
ATOM   3006 O  O   . LYS B 1 189 ? 10.92976  -19.14198 30.06965  1.000 77.99314  ? 958  LYS A O   1 
ATOM   3007 C  CB  . LYS B 1 189 ? 11.10579  -21.83008 32.00528  1.000 85.39968  ? 958  LYS A CB  1 
ATOM   3008 C  CG  . LYS B 1 189 ? 11.98387  -22.10590 33.22051  1.000 83.01909  ? 958  LYS A CG  1 
ATOM   3009 C  CD  . LYS B 1 189 ? 12.24399  -23.61392 33.33859  1.000 83.57279  ? 958  LYS A CD  1 
ATOM   3010 C  CE  . LYS B 1 189 ? 13.63197  -23.92905 33.88088  1.000 77.66705  ? 958  LYS A CE  1 
ATOM   3011 N  NZ  . LYS B 1 189 ? 13.87048  -25.39415 33.99135  1.000 70.16841  ? 958  LYS A NZ  1 
ATOM   3012 N  N   . GLU B 1 190 ? 9.19136   -20.56175 29.85114  1.000 83.57033  ? 959  GLU A N   1 
ATOM   3013 C  CA  . GLU B 1 190 ? 8.91517   -20.16410 28.47770  1.000 83.70438  ? 959  GLU A CA  1 
ATOM   3014 C  C   . GLU B 1 190 ? 8.73568   -18.65676 28.36245  1.000 78.90870  ? 959  GLU A C   1 
ATOM   3015 O  O   . GLU B 1 190 ? 9.14790   -18.05642 27.36358  1.000 77.81419  ? 959  GLU A O   1 
ATOM   3016 C  CB  . GLU B 1 190 ? 7.66300   -20.88658 27.97845  1.000 89.62809  ? 959  GLU A CB  1 
ATOM   3017 C  CG  . GLU B 1 190 ? 7.81587   -22.40583 27.89210  1.000 97.11351  ? 959  GLU A CG  1 
ATOM   3018 C  CD  . GLU B 1 190 ? 6.55273   -23.08717 27.41633  1.000 101.19480 ? 959  GLU A CD  1 
ATOM   3019 O  OE1 . GLU B 1 190 ? 5.56791   -22.37127 27.13246  1.000 104.11268 ? 959  GLU A OE1 1 
ATOM   3020 O  OE2 . GLU B 1 190 ? 6.54154   -24.33254 27.33361  1.000 103.24002 ? 959  GLU A OE2 1 
ATOM   3021 N  N   . GLN B 1 191 ? 8.16687   -18.01780 29.38500  1.000 78.04731  ? 960  GLN A N   1 
ATOM   3022 C  CA  . GLN B 1 191 ? 7.93429   -16.58198 29.31473  1.000 74.43464  ? 960  GLN A CA  1 
ATOM   3023 C  C   . GLN B 1 191 ? 9.11892   -15.75469 29.77831  1.000 70.39693  ? 960  GLN A C   1 
ATOM   3024 O  O   . GLN B 1 191 ? 9.19652   -14.57437 29.41921  1.000 69.93087  ? 960  GLN A O   1 
ATOM   3025 C  CB  . GLN B 1 191 ? 6.71747   -16.19495 30.14884  1.000 75.31829  ? 960  GLN A CB  1 
ATOM   3026 C  CG  . GLN B 1 191 ? 5.53923   -17.09982 29.95304  1.000 80.79918  ? 960  GLN A CG  1 
ATOM   3027 C  CD  . GLN B 1 191 ? 4.38849   -16.71054 30.84024  1.000 84.43669  ? 960  GLN A CD  1 
ATOM   3028 O  OE1 . GLN B 1 191 ? 4.04570   -17.42999 31.78616  1.000 85.35798  ? 960  GLN A OE1 1 
ATOM   3029 N  NE2 . GLN B 1 191 ? 3.78337   -15.55934 30.55082  1.000 84.74816  ? 960  GLN A NE2 1 
ATOM   3030 N  N   . THR B 1 192 ? 10.03147  -16.32566 30.57507  1.000 69.92253  ? 961  THR A N   1 
ATOM   3031 C  CA  . THR B 1 192 ? 11.12069  -15.54095 31.14131  1.000 67.14997  ? 961  THR A CA  1 
ATOM   3032 C  C   . THR B 1 192 ? 12.51309  -15.94879 30.67714  1.000 65.87322  ? 961  THR A C   1 
ATOM   3033 O  O   . THR B 1 192 ? 13.44828  -15.15836 30.83616  1.000 64.73600  ? 961  THR A O   1 
ATOM   3034 C  CB  . THR B 1 192 ? 11.07316  -15.59700 32.67857  1.000 71.65039  ? 961  THR A CB  1 
ATOM   3035 O  OG1 . THR B 1 192 ? 11.42608  -16.90797 33.13909  1.000 71.20814  ? 961  THR A OG1 1 
ATOM   3036 C  CG2 . THR B 1 192 ? 9.67413   -15.26736 33.17657  1.000 73.86453  ? 961  THR A CG2 1 
ATOM   3037 N  N   . MET B 1 193 ? 12.68219  -17.12839 30.10156  1.000 66.59102  ? 962  MET A N   1 
ATOM   3038 C  CA  . MET B 1 193 ? 14.00976  -17.57753 29.71654  1.000 64.47858  ? 962  MET A CA  1 
ATOM   3039 C  C   . MET B 1 193 ? 14.35738  -17.13289 28.29934  1.000 61.79750  ? 962  MET A C   1 
ATOM   3040 O  O   . MET B 1 193 ? 13.48148  -16.97120 27.44482  1.000 58.72937  ? 962  MET A O   1 
ATOM   3041 C  CB  . MET B 1 193 ? 14.10301  -19.09494 29.83393  1.000 66.50278  ? 962  MET A CB  1 
ATOM   3042 C  CG  . MET B 1 193 ? 13.88312  -19.54433 31.26174  1.000 70.62182  ? 962  MET A CG  1 
ATOM   3043 S  SD  . MET B 1 193 ? 15.34150  -19.29750 32.28002  1.000 72.53829  ? 962  MET A SD  1 
ATOM   3044 C  CE  . MET B 1 193 ? 16.19194  -20.83254 31.90781  1.000 76.52394  ? 962  MET A CE  1 
ATOM   3045 N  N   . CYS B 1 194 ? 15.65373  -16.97825 28.05149  1.000 61.26226  ? 963  CYS A N   1 
ATOM   3046 C  CA  . CYS B 1 194 ? 16.12745  -16.64909 26.71642  1.000 58.89685  ? 963  CYS A CA  1 
ATOM   3047 C  C   . CYS B 1 194 ? 15.66070  -17.72239 25.74271  1.000 57.96060  ? 963  CYS A C   1 
ATOM   3048 O  O   . CYS B 1 194 ? 15.77870  -18.91643 26.04367  1.000 59.76107  ? 963  CYS A O   1 
ATOM   3049 C  CB  . CYS B 1 194 ? 17.65056  -16.55528 26.70890  1.000 58.22703  ? 963  CYS A CB  1 
ATOM   3050 S  SG  . CYS B 1 194 ? 18.42023  -16.35164 25.08736  1.000 58.29774  ? 963  CYS A SG  1 
ATOM   3051 N  N   . PRO B 1 195 ? 15.09404  -17.34616 24.59472  1.000 57.43303  ? 964  PRO A N   1 
ATOM   3052 C  CA  . PRO B 1 195 ? 14.62116  -18.34543 23.62573  1.000 57.46323  ? 964  PRO A CA  1 
ATOM   3053 C  C   . PRO B 1 195 ? 15.72056  -18.92227 22.74986  1.000 57.59896  ? 964  PRO A C   1 
ATOM   3054 O  O   . PRO B 1 195 ? 15.44053  -19.82036 21.93917  1.000 56.51567  ? 964  PRO A O   1 
ATOM   3055 C  CB  . PRO B 1 195 ? 13.60905  -17.55731 22.79036  1.000 56.42633  ? 964  PRO A CB  1 
ATOM   3056 C  CG  . PRO B 1 195 ? 14.14973  -16.15659 22.80891  1.000 56.70171  ? 964  PRO A CG  1 
ATOM   3057 C  CD  . PRO B 1 195 ? 14.77752  -15.97126 24.18075  1.000 57.75934  ? 964  PRO A CD  1 
ATOM   3058 N  N   . VAL B 1 196 ? 16.94379  -18.40494 22.83937  1.000 57.00211  ? 965  VAL A N   1 
ATOM   3059 C  CA  . VAL B 1 196 ? 18.03720  -18.93745 22.03689  1.000 57.83345  ? 965  VAL A CA  1 
ATOM   3060 C  C   . VAL B 1 196 ? 18.75228  -20.01988 22.83379  1.000 59.11475  ? 965  VAL A C   1 
ATOM   3061 O  O   . VAL B 1 196 ? 18.77114  -21.18573 22.42467  1.000 60.19810  ? 965  VAL A O   1 
ATOM   3062 C  CB  . VAL B 1 196 ? 18.99984  -17.81913 21.59364  1.000 56.94845  ? 965  VAL A CB  1 
ATOM   3063 C  CG1 . VAL B 1 196 ? 20.19070  -18.39419 20.82013  1.000 57.39297  ? 965  VAL A CG1 1 
ATOM   3064 C  CG2 . VAL B 1 196 ? 18.25556  -16.83057 20.73779  1.000 54.85736  ? 965  VAL A CG2 1 
ATOM   3065 N  N   . CYS B 1 197 ? 19.26365  -19.67471 24.01559  1.000 58.79341  ? 966  CYS A N   1 
ATOM   3066 C  CA  . CYS B 1 197 ? 19.99119  -20.65478 24.81453  1.000 60.74754  ? 966  CYS A CA  1 
ATOM   3067 C  C   . CYS B 1 197 ? 19.09046  -21.46641 25.73733  1.000 63.29642  ? 966  CYS A C   1 
ATOM   3068 O  O   . CYS B 1 197 ? 19.51597  -22.52771 26.21079  1.000 63.44756  ? 966  CYS A O   1 
ATOM   3069 C  CB  . CYS B 1 197 ? 21.09928  -19.98317 25.63908  1.000 62.36616  ? 966  CYS A CB  1 
ATOM   3070 S  SG  . CYS B 1 197 ? 20.57545  -18.71012 26.82804  1.000 66.21549  ? 966  CYS A SG  1 
ATOM   3071 N  N   . LEU B 1 198 ? 17.88167  -20.97932 26.03329  1.000 65.10799  ? 967  LEU A N   1 
ATOM   3072 C  CA  . LEU B 1 198 ? 16.92047  -21.62833 26.93448  1.000 66.46834  ? 967  LEU A CA  1 
ATOM   3073 C  C   . LEU B 1 198 ? 17.49480  -21.88105 28.32230  1.000 70.32945  ? 967  LEU A C   1 
ATOM   3074 O  O   . LEU B 1 198 ? 16.92181  -22.63841 29.10862  1.000 77.37664  ? 967  LEU A O   1 
ATOM   3075 C  CB  . LEU B 1 198 ? 16.41508  -22.95132 26.34307  1.000 66.76634  ? 967  LEU A CB  1 
ATOM   3076 C  CG  . LEU B 1 198 ? 16.00519  -22.94805 24.86821  1.000 66.03847  ? 967  LEU A CG  1 
ATOM   3077 C  CD1 . LEU B 1 198 ? 15.41469  -24.29403 24.47855  1.000 68.33258  ? 967  LEU A CD1 1 
ATOM   3078 C  CD2 . LEU B 1 198 ? 15.03078  -21.81107 24.58830  1.000 63.96145  ? 967  LEU A CD2 1 
ATOM   3079 N  N   . ASP B 1 199 ? 18.57701  -21.19435 28.65885  1.000 70.08631  ? 968  ASP A N   1 
ATOM   3080 C  CA  . ASP B 1 199 ? 19.42123  -21.51701 29.79986  1.000 73.12147  ? 968  ASP A CA  1 
ATOM   3081 C  C   . ASP B 1 199 ? 19.50358  -20.36128 30.77970  1.000 73.53092  ? 968  ASP A C   1 
ATOM   3082 O  O   . ASP B 1 199 ? 19.34136  -20.55797 31.98927  1.000 73.41505  ? 968  ASP A O   1 
ATOM   3083 C  CB  . ASP B 1 199 ? 20.81752  -21.90338 29.28288  1.000 73.69579  ? 968  ASP A CB  1 
ATOM   3084 C  CG  . ASP B 1 199 ? 21.72214  -22.44304 30.35925  1.000 80.16218  ? 968  ASP A CG  1 
ATOM   3085 O  OD1 . ASP B 1 199 ? 21.25477  -22.62464 31.50422  1.000 83.80632  ? 968  ASP A OD1 1 
ATOM   3086 O  OD2 . ASP B 1 199 ? 22.90332  -22.70586 30.04202  1.000 84.71715  ? 968  ASP A OD2 1 
ATOM   3087 N  N   . ARG B 1 200 ? 19.76491  -19.15820 30.28258  1.000 71.62084  ? 969  ARG A N   1 
ATOM   3088 C  CA  . ARG B 1 200 ? 19.78366  -17.96141 31.09722  1.000 69.57762  ? 969  ARG A CA  1 
ATOM   3089 C  C   . ARG B 1 200 ? 18.41839  -17.28711 31.01825  1.000 68.05304  ? 969  ARG A C   1 
ATOM   3090 O  O   . ARG B 1 200 ? 17.52847  -17.71620 30.28079  1.000 67.53287  ? 969  ARG A O   1 
ATOM   3091 C  CB  . ARG B 1 200 ? 20.86776  -17.00435 30.61611  1.000 68.74995  ? 969  ARG A CB  1 
ATOM   3092 C  CG  . ARG B 1 200 ? 22.27197  -17.56380 30.59611  1.000 70.44624  ? 969  ARG A CG  1 
ATOM   3093 C  CD  . ARG B 1 200 ? 23.09137  -16.73259 29.61714  1.000 71.06269  ? 969  ARG A CD  1 
ATOM   3094 N  NE  . ARG B 1 200 ? 24.34752  -17.36768 29.25437  1.000 71.95139  ? 969  ARG A NE  1 
ATOM   3095 C  CZ  . ARG B 1 200 ? 24.45822  -18.34013 28.36057  1.000 76.07983  ? 969  ARG A CZ  1 
ATOM   3096 N  NH1 . ARG B 1 200 ? 23.39757  -18.83796 27.74450  1.000 75.00341  ? 969  ARG A NH1 1 
ATOM   3097 N  NH2 . ARG B 1 200 ? 25.66233  -18.83045 28.08260  1.000 79.03167  ? 969  ARG A NH2 1 
ATOM   3098 N  N   . LEU B 1 201 ? 18.24230  -16.22747 31.79659  1.000 66.61572  ? 970  LEU A N   1 
ATOM   3099 C  CA  . LEU B 1 201 ? 17.02515  -15.43621 31.75172  1.000 64.49290  ? 970  LEU A CA  1 
ATOM   3100 C  C   . LEU B 1 201 ? 17.16432  -14.27869 30.77274  1.000 61.91476  ? 970  LEU A C   1 
ATOM   3101 O  O   . LEU B 1 201 ? 18.26596  -13.87682 30.39607  1.000 62.02999  ? 970  LEU A O   1 
ATOM   3102 C  CB  . LEU B 1 201 ? 16.67230  -14.88441 33.12694  1.000 67.09364  ? 970  LEU A CB  1 
ATOM   3103 C  CG  . LEU B 1 201 ? 16.35427  -15.88593 34.22198  1.000 69.35563  ? 970  LEU A CG  1 
ATOM   3104 C  CD1 . LEU B 1 201 ? 16.74173  -15.29007 35.57152  1.000 68.27932  ? 970  LEU A CD1 1 
ATOM   3105 C  CD2 . LEU B 1 201 ? 14.88138  -16.23038 34.14855  1.000 67.25234  ? 970  LEU A CD2 1 
ATOM   3106 N  N   . LYS B 1 202 ? 16.02149  -13.76580 30.33542  1.000 61.28960  ? 971  LYS A N   1 
ATOM   3107 C  CA  . LYS B 1 202 ? 15.99129  -12.60593 29.45169  1.000 59.05460  ? 971  LYS A CA  1 
ATOM   3108 C  C   . LYS B 1 202 ? 16.39172  -11.35984 30.23734  1.000 59.43330  ? 971  LYS A C   1 
ATOM   3109 O  O   . LYS B 1 202 ? 15.60568  -10.83281 31.02626  1.000 61.59666  ? 971  LYS A O   1 
ATOM   3110 C  CB  . LYS B 1 202 ? 14.60788  -12.45036 28.83107  1.000 58.22747  ? 971  LYS A CB  1 
ATOM   3111 C  CG  . LYS B 1 202 ? 14.22231  -13.62512 27.95895  1.000 59.81626  ? 971  LYS A CG  1 
ATOM   3112 C  CD  . LYS B 1 202 ? 12.92979  -13.40420 27.19360  1.000 59.52024  ? 971  LYS A CD  1 
ATOM   3113 C  CE  . LYS B 1 202 ? 11.70687  -13.59277 28.04724  1.000 60.99518  ? 971  LYS A CE  1 
ATOM   3114 N  NZ  . LYS B 1 202 ? 10.47453  -13.22653 27.28297  1.000 61.24715  ? 971  LYS A NZ  1 
ATOM   3115 N  N   . ASN B 1 203 ? 17.63123  -10.88904 30.05273  1.000 59.98333  ? 972  ASN A N   1 
ATOM   3116 C  CA  . ASN B 1 203 ? 18.09345  -9.65607  30.68865  1.000 60.46435  ? 972  ASN A CA  1 
ATOM   3117 C  C   . ASN B 1 203 ? 18.43096  -8.56585  29.67324  1.000 60.49404  ? 972  ASN A C   1 
ATOM   3118 O  O   . ASN B 1 203 ? 19.17117  -7.63190  29.99856  1.000 60.25533  ? 972  ASN A O   1 
ATOM   3119 C  CB  . ASN B 1 203 ? 19.31003  -9.91614  31.58495  1.000 59.80353  ? 972  ASN A CB  1 
ATOM   3120 C  CG  . ASN B 1 203 ? 20.52379  -10.37889 30.80355  1.000 59.26011  ? 972  ASN A CG  1 
ATOM   3121 O  OD1 . ASN B 1 203 ? 20.39190  -10.94286 29.72193  1.000 60.46907  ? 972  ASN A OD1 1 
ATOM   3122 N  ND2 . ASN B 1 203 ? 21.71047  -10.12315 31.33590  1.000 57.32326  ? 972  ASN A ND2 1 
ATOM   3123 N  N   . MET B 1 204 ? 17.89821  -8.66073  28.45671  1.000 59.56875  ? 973  MET A N   1 
ATOM   3124 C  CA  . MET B 1 204 ? 18.12684  -7.66542  27.41348  1.000 59.23363  ? 973  MET A CA  1 
ATOM   3125 C  C   . MET B 1 204 ? 16.91606  -7.58963  26.49589  1.000 58.53866  ? 973  MET A C   1 
ATOM   3126 O  O   . MET B 1 204 ? 16.47710  -8.61691  25.97035  1.000 59.45381  ? 973  MET A O   1 
ATOM   3127 C  CB  . MET B 1 204 ? 19.37366  -7.99640  26.59239  1.000 61.07801  ? 973  MET A CB  1 
ATOM   3128 C  CG  . MET B 1 204 ? 19.39346  -7.26993  25.25960  1.000 60.46228  ? 973  MET A CG  1 
ATOM   3129 S  SD  . MET B 1 204 ? 20.81375  -7.70445  24.27577  1.000 65.94933  ? 973  MET A SD  1 
ATOM   3130 C  CE  . MET B 1 204 ? 22.13120  -6.97221  25.24266  1.000 66.96922  ? 973  MET A CE  1 
ATOM   3131 N  N   . ILE B 1 205 ? 16.41601  -6.37703  26.26413  1.000 57.23227  ? 974  ILE A N   1 
ATOM   3132 C  CA  . ILE B 1 205 ? 15.15640  -6.16090  25.56321  1.000 57.77566  ? 974  ILE A CA  1 
ATOM   3133 C  C   . ILE B 1 205 ? 15.35428  -5.31115  24.31215  1.000 58.21618  ? 974  ILE A C   1 
ATOM   3134 O  O   . ILE B 1 205 ? 16.12277  -4.34251  24.31210  1.000 57.19766  ? 974  ILE A O   1 
ATOM   3135 C  CB  . ILE B 1 205 ? 14.15318  -5.51760  26.53843  1.000 58.44379  ? 974  ILE A CB  1 
ATOM   3136 C  CG1 . ILE B 1 205 ? 13.91134  -6.52118  27.65333  1.000 59.81553  ? 974  ILE A CG1 1 
ATOM   3137 C  CG2 . ILE B 1 205 ? 12.86198  -5.06457  25.86054  1.000 56.58655  ? 974  ILE A CG2 1 
ATOM   3138 C  CD1 . ILE B 1 205 ? 12.61226  -6.37344  28.29819  1.000 65.65243  ? 974  ILE A CD1 1 
ATOM   3139 N  N   . PHE B 1 206 ? 14.66505  -5.69425  23.24006  1.000 57.93836  ? 975  PHE A N   1 
ATOM   3140 C  CA  . PHE B 1 206 ? 14.60096  -4.89775  22.02557  1.000 59.21411  ? 975  PHE A CA  1 
ATOM   3141 C  C   . PHE B 1 206 ? 13.29129  -4.12394  22.01578  1.000 60.98728  ? 975  PHE A C   1 
ATOM   3142 O  O   . PHE B 1 206 ? 12.36317  -4.41129  22.77484  1.000 60.30405  ? 975  PHE A O   1 
ATOM   3143 C  CB  . PHE B 1 206 ? 14.70443  -5.75608  20.75828  1.000 58.03393  ? 975  PHE A CB  1 
ATOM   3144 C  CG  . PHE B 1 206 ? 15.61275  -6.93936  20.89458  1.000 57.97173  ? 975  PHE A CG  1 
ATOM   3145 C  CD1 . PHE B 1 206 ? 16.92777  -6.78164  21.29165  1.000 58.79897  ? 975  PHE A CD1 1 
ATOM   3146 C  CD2 . PHE B 1 206 ? 15.15363  -8.21697  20.59883  1.000 56.78042  ? 975  PHE A CD2 1 
ATOM   3147 C  CE1 . PHE B 1 206 ? 17.76419  -7.88277  21.42053  1.000 58.77631  ? 975  PHE A CE1 1 
ATOM   3148 C  CE2 . PHE B 1 206 ? 15.98789  -9.32025  20.71217  1.000 57.07997  ? 975  PHE A CE2 1 
ATOM   3149 C  CZ  . PHE B 1 206 ? 17.29228  -9.15308  21.13149  1.000 57.69429  ? 975  PHE A CZ  1 
ATOM   3150 N  N   . LEU B 1 207 ? 13.23352  -3.11811  21.15103  1.000 61.98639  ? 976  LEU A N   1 
ATOM   3151 C  CA  . LEU B 1 207 ? 12.06344  -2.25423  21.10650  1.000 63.15500  ? 976  LEU A CA  1 
ATOM   3152 C  C   . LEU B 1 207 ? 10.82877  -2.98129  20.59718  1.000 62.53903  ? 976  LEU A C   1 
ATOM   3153 O  O   . LEU B 1 207 ? 9.71242   -2.50279  20.81774  1.000 64.78216  ? 976  LEU A O   1 
ATOM   3154 C  CB  . LEU B 1 207 ? 12.35309  -1.01679  20.25396  1.000 68.74076  ? 976  LEU A CB  1 
ATOM   3155 C  CG  . LEU B 1 207 ? 13.11940  0.13839   20.91722  1.000 72.09093  ? 976  LEU A CG  1 
ATOM   3156 C  CD1 . LEU B 1 207 ? 14.26245  -0.31634  21.82201  1.000 68.17109  ? 976  LEU A CD1 1 
ATOM   3157 C  CD2 . LEU B 1 207 ? 13.63002  1.13026   19.86895  1.000 74.42339  ? 976  LEU A CD2 1 
ATOM   3158 N  N   . CYS B 1 208 ? 10.99726  -4.12023  19.92613  1.000 60.53134  ? 977  CYS A N   1 
ATOM   3159 C  CA  . CYS B 1 208 ? 9.84806   -4.88710  19.46523  1.000 59.57133  ? 977  CYS A CA  1 
ATOM   3160 C  C   . CYS B 1 208 ? 9.09946   -5.55729  20.60938  1.000 60.77380  ? 977  CYS A C   1 
ATOM   3161 O  O   . CYS B 1 208 ? 8.01371   -6.11065  20.39415  1.000 60.48458  ? 977  CYS A O   1 
ATOM   3162 C  CB  . CYS B 1 208 ? 10.30064  -5.92774  18.43701  1.000 58.96441  ? 977  CYS A CB  1 
ATOM   3163 S  SG  . CYS B 1 208 ? 11.56039  -7.09667  19.04577  1.000 56.37769  ? 977  CYS A SG  1 
ATOM   3164 N  N   . GLY B 1 209 ? 9.63721   -5.52875  21.81481  1.000 59.91917  ? 978  GLY A N   1 
ATOM   3165 C  CA  . GLY B 1 209 ? 8.94398   -6.12662  22.92694  1.000 60.27215  ? 978  GLY A CA  1 
ATOM   3166 C  C   . GLY B 1 209 ? 9.45678   -7.48614  23.32449  1.000 58.53325  ? 978  GLY A C   1 
ATOM   3167 O  O   . GLY B 1 209 ? 9.07278   -7.98536  24.38702  1.000 60.90749  ? 978  GLY A O   1 
ATOM   3168 N  N   . HIS B 1 210 ? 10.27156  -8.11650  22.49113  1.000 57.18937  ? 979  HIS A N   1 
ATOM   3169 C  CA  . HIS B 1 210 ? 10.83809  -9.41168  22.81727  1.000 55.38015  ? 979  HIS A CA  1 
ATOM   3170 C  C   . HIS B 1 210 ? 12.22716  -9.22199  23.40665  1.000 55.03598  ? 979  HIS A C   1 
ATOM   3171 O  O   . HIS B 1 210 ? 12.79241  -8.12422  23.38816  1.000 56.45195  ? 979  HIS A O   1 
ATOM   3172 C  CB  . HIS B 1 210 ? 10.87121  -10.30264 21.58323  1.000 51.39925  ? 979  HIS A CB  1 
ATOM   3173 C  CG  . HIS B 1 210 ? 9.53137   -10.47522 20.94879  1.000 54.32226  ? 979  HIS A CG  1 
ATOM   3174 N  ND1 . HIS B 1 210 ? 9.22841   -9.97849  19.69880  1.000 55.15124  ? 979  HIS A ND1 1 
ATOM   3175 C  CD2 . HIS B 1 210 ? 8.40433   -11.06970 21.40309  1.000 54.80526  ? 979  HIS A CD2 1 
ATOM   3176 C  CE1 . HIS B 1 210 ? 7.97231   -10.26716 19.40937  1.000 55.19646  ? 979  HIS A CE1 1 
ATOM   3177 N  NE2 . HIS B 1 210 ? 7.45052   -10.93091 20.42644  1.000 57.23821  ? 979  HIS A NE2 1 
ATOM   3178 N  N   . GLY B 1 211 ? 12.75633  -10.29457 23.98958  1.000 52.47158  ? 980  GLY A N   1 
ATOM   3179 C  CA  . GLY B 1 211 ? 14.04897  -10.21014 24.64305  1.000 55.56451  ? 980  GLY A CA  1 
ATOM   3180 C  C   . GLY B 1 211 ? 14.81938  -11.51449 24.62940  1.000 56.95313  ? 980  GLY A C   1 
ATOM   3181 O  O   . GLY B 1 211 ? 14.26770  -12.59281 24.37860  1.000 56.97097  ? 980  GLY A O   1 
ATOM   3182 N  N   . THR B 1 212 ? 16.11830  -11.39614 24.92653  1.000 57.22200  ? 981  THR A N   1 
ATOM   3183 C  CA  . THR B 1 212 ? 17.04092  -12.52244 25.02803  1.000 57.88017  ? 981  THR A CA  1 
ATOM   3184 C  C   . THR B 1 212 ? 17.94617  -12.30597 26.23999  1.000 58.49092  ? 981  THR A C   1 
ATOM   3185 O  O   . THR B 1 212 ? 17.81313  -11.31928 26.96876  1.000 59.18908  ? 981  THR A O   1 
ATOM   3186 C  CB  . THR B 1 212 ? 17.90171  -12.66400 23.75849  1.000 58.75059  ? 981  THR A CB  1 
ATOM   3187 O  OG1 . THR B 1 212 ? 18.81797  -11.56618 23.68619  1.000 59.62994  ? 981  THR A OG1 1 
ATOM   3188 C  CG2 . THR B 1 212 ? 17.05095  -12.66954 22.48169  1.000 56.88361  ? 981  THR A CG2 1 
ATOM   3189 N  N   . CYS B 1 213 ? 18.88483  -13.22861 26.45231  1.000 58.20922  ? 982  CYS A N   1 
ATOM   3190 C  CA  . CYS B 1 213 ? 20.01782  -12.92389 27.31005  1.000 59.60110  ? 982  CYS A CA  1 
ATOM   3191 C  C   . CYS B 1 213 ? 20.99460  -12.05458 26.52762  1.000 61.85358  ? 982  CYS A C   1 
ATOM   3192 O  O   . CYS B 1 213 ? 20.93147  -11.96786 25.29850  1.000 62.56442  ? 982  CYS A O   1 
ATOM   3193 C  CB  . CYS B 1 213 ? 20.70735  -14.20067 27.81740  1.000 60.53405  ? 982  CYS A CB  1 
ATOM   3194 S  SG  . CYS B 1 213 ? 21.84469  -15.01867 26.64579  1.000 60.76915  ? 982  CYS A SG  1 
ATOM   3195 N  N   . GLN B 1 214 ? 21.89687  -11.39333 27.25435  1.000 62.03512  ? 983  GLN A N   1 
ATOM   3196 C  CA  . GLN B 1 214 ? 22.83949  -10.48319 26.61009  1.000 63.94075  ? 983  GLN A CA  1 
ATOM   3197 C  C   . GLN B 1 214 ? 23.76741  -11.21969 25.64854  1.000 64.81248  ? 983  GLN A C   1 
ATOM   3198 O  O   . GLN B 1 214 ? 24.06995  -10.72283 24.55541  1.000 65.62631  ? 983  GLN A O   1 
ATOM   3199 C  CB  . GLN B 1 214 ? 23.64491  -9.74601  27.67592  1.000 63.98112  ? 983  GLN A CB  1 
ATOM   3200 C  CG  . GLN B 1 214 ? 24.67940  -8.79767  27.11593  1.000 68.21951  ? 983  GLN A CG  1 
ATOM   3201 C  CD  . GLN B 1 214 ? 25.37425  -8.00474  28.19749  1.000 71.95725  ? 983  GLN A CD  1 
ATOM   3202 O  OE1 . GLN B 1 214 ? 25.47211  -8.44624  29.34686  1.000 68.57981  ? 983  GLN A OE1 1 
ATOM   3203 N  NE2 . GLN B 1 214 ? 25.86321  -6.82513  27.83837  1.000 72.97925  ? 983  GLN A NE2 1 
ATOM   3204 N  N   . LEU B 1 215 ? 24.22331  -12.40864 26.03839  1.000 65.32028  ? 984  LEU A N   1 
ATOM   3205 C  CA  . LEU B 1 215 ? 25.17966  -13.15061 25.22683  1.000 65.86060  ? 984  LEU A CA  1 
ATOM   3206 C  C   . LEU B 1 215 ? 24.58283  -13.52753 23.87665  1.000 65.29363  ? 984  LEU A C   1 
ATOM   3207 O  O   . LEU B 1 215 ? 25.22614  -13.36803 22.83288  1.000 63.62429  ? 984  LEU A O   1 
ATOM   3208 C  CB  . LEU B 1 215 ? 25.65168  -14.38604 25.98774  1.000 66.95907  ? 984  LEU A CB  1 
ATOM   3209 C  CG  . LEU B 1 215 ? 26.83466  -14.08568 26.90629  1.000 67.65378  ? 984  LEU A CG  1 
ATOM   3210 C  CD1 . LEU B 1 215 ? 27.04168  -15.22379 27.87422  1.000 69.90645  ? 984  LEU A CD1 1 
ATOM   3211 C  CD2 . LEU B 1 215 ? 28.08552  -13.86043 26.08652  1.000 70.18441  ? 984  LEU A CD2 1 
ATOM   3212 N  N   . CYS B 1 216 ? 23.35707  -14.05111 23.87804  1.000 64.11153  ? 985  CYS A N   1 
ATOM   3213 C  CA  . CYS B 1 216 ? 22.71995  -14.38888 22.61227  1.000 63.58738  ? 985  CYS A CA  1 
ATOM   3214 C  C   . CYS B 1 216 ? 22.30640  -13.13904 21.85665  1.000 64.04620  ? 985  CYS A C   1 
ATOM   3215 O  O   . CYS B 1 216 ? 22.45603  -13.07320 20.63540  1.000 64.73139  ? 985  CYS A O   1 
ATOM   3216 C  CB  . CYS B 1 216 ? 21.51389  -15.28399 22.85546  1.000 58.48923  ? 985  CYS A CB  1 
ATOM   3217 S  SG  . CYS B 1 216 ? 22.00190  -16.78623 23.66767  1.000 62.14282  ? 985  CYS A SG  1 
ATOM   3218 N  N   . GLY B 1 217 ? 21.80743  -12.13051 22.56963  1.000 63.62299  ? 986  GLY A N   1 
ATOM   3219 C  CA  . GLY B 1 217 ? 21.29259  -10.95369 21.89767  1.000 61.92841  ? 986  GLY A CA  1 
ATOM   3220 C  C   . GLY B 1 217 ? 22.36957  -10.17293 21.17505  1.000 64.87418  ? 986  GLY A C   1 
ATOM   3221 O  O   . GLY B 1 217 ? 22.15218  -9.69204  20.05863  1.000 66.18276  ? 986  GLY A O   1 
ATOM   3222 N  N   . ASP B 1 218 ? 23.56731  -10.09484 21.75774  1.000 65.13450  ? 987  ASP A N   1 
ATOM   3223 C  CA  . ASP B 1 218 ? 24.62239  -9.33706  21.09577  1.000 65.42072  ? 987  ASP A CA  1 
ATOM   3224 C  C   . ASP B 1 218 ? 25.08871  -9.99215  19.80757  1.000 65.71236  ? 987  ASP A C   1 
ATOM   3225 O  O   . ASP B 1 218 ? 25.71368  -9.32279  18.97972  1.000 66.45784  ? 987  ASP A O   1 
ATOM   3226 C  CB  . ASP B 1 218 ? 25.82052  -9.16150  22.02475  1.000 65.10666  ? 987  ASP A CB  1 
ATOM   3227 C  CG  . ASP B 1 218 ? 25.58311  -8.12462  23.09597  1.000 68.73836  ? 987  ASP A CG  1 
ATOM   3228 O  OD1 . ASP B 1 218 ? 24.73559  -7.22174  22.89832  1.000 68.06341  ? 987  ASP A OD1 1 
ATOM   3229 O  OD2 . ASP B 1 218 ? 26.26180  -8.21369  24.13956  1.000 71.36338  ? 987  ASP A OD2 1 
ATOM   3230 N  N   . ARG B 1 219 ? 24.77289  -11.26523 19.60506  1.000 65.33265  ? 988  ARG A N   1 
ATOM   3231 C  CA  . ARG B 1 219 ? 25.19597  -11.99932 18.42612  1.000 65.86542  ? 988  ARG A CA  1 
ATOM   3232 C  C   . ARG B 1 219 ? 24.13369  -12.02268 17.34024  1.000 64.85324  ? 988  ARG A C   1 
ATOM   3233 O  O   . ARG B 1 219 ? 24.27886  -12.75581 16.36004  1.000 63.13922  ? 988  ARG A O   1 
ATOM   3234 C  CB  . ARG B 1 219 ? 25.59159  -13.42579 18.81947  1.000 67.72910  ? 988  ARG A CB  1 
ATOM   3235 C  CG  . ARG B 1 219 ? 26.93763  -13.49334 19.51079  1.000 70.22130  ? 988  ARG A CG  1 
ATOM   3236 C  CD  . ARG B 1 219 ? 27.19972  -14.82338 20.20398  1.000 73.24145  ? 988  ARG A CD  1 
ATOM   3237 N  NE  . ARG B 1 219 ? 26.94029  -15.99505 19.37322  1.000 81.37432  ? 988  ARG A NE  1 
ATOM   3238 C  CZ  . ARG B 1 219 ? 27.75243  -16.45752 18.42833  1.000 84.50039  ? 988  ARG A CZ  1 
ATOM   3239 N  NH1 . ARG B 1 219 ? 28.89025  -15.85063 18.13227  1.000 84.94969  ? 988  ARG A NH1 1 
ATOM   3240 N  NH2 . ARG B 1 219 ? 27.42104  -17.56756 17.77338  1.000 79.44303  ? 988  ARG A NH2 1 
ATOM   3241 N  N   . MET B 1 220 ? 23.10231  -11.19889 17.46065  1.000 63.78795  ? 989  MET A N   1 
ATOM   3242 C  CA  . MET B 1 220 ? 21.99765  -11.20025 16.52045  1.000 63.25520  ? 989  MET A CA  1 
ATOM   3243 C  C   . MET B 1 220 ? 21.76826  -9.77658  16.04364  1.000 62.78865  ? 989  MET A C   1 
ATOM   3244 O  O   . MET B 1 220 ? 22.02655  -8.81508  16.77097  1.000 62.72152  ? 989  MET A O   1 
ATOM   3245 C  CB  . MET B 1 220 ? 20.71833  -11.73090 17.17287  1.000 63.95883  ? 989  MET A CB  1 
ATOM   3246 C  CG  . MET B 1 220 ? 20.91870  -12.95005 18.06430  1.000 65.19642  ? 989  MET A CG  1 
ATOM   3247 S  SD  . MET B 1 220 ? 19.37662  -13.46560 18.83913  1.000 69.13226  ? 989  MET A SD  1 
ATOM   3248 C  CE  . MET B 1 220 ? 18.41942  -13.66750 17.34799  1.000 60.29416  ? 989  MET A CE  1 
ATOM   3249 N  N   . SER B 1 221 ? 21.29651  -9.65232  14.80412  1.000 61.10110  ? 990  SER A N   1 
ATOM   3250 C  CA  . SER B 1 221 ? 20.89258  -8.37459  14.23939  1.000 58.51671  ? 990  SER A CA  1 
ATOM   3251 C  C   . SER B 1 221 ? 19.38685  -8.26623  14.07668  1.000 58.12629  ? 990  SER A C   1 
ATOM   3252 O  O   . SER B 1 221 ? 18.88877  -7.17320  13.79396  1.000 58.64024  ? 990  SER A O   1 
ATOM   3253 C  CB  . SER B 1 221 ? 21.58596  -8.13536  12.88424  1.000 57.19247  ? 990  SER A CB  1 
ATOM   3254 O  OG  . SER B 1 221 ? 21.26683  -9.15709  11.95873  1.000 56.79961  ? 990  SER A OG  1 
ATOM   3255 N  N   . GLU B 1 222 ? 18.65945  -9.37007  14.22562  1.000 58.52324  ? 991  GLU A N   1 
ATOM   3256 C  CA  . GLU B 1 222 ? 17.20946  -9.39202  14.12481  1.000 58.57527  ? 991  GLU A CA  1 
ATOM   3257 C  C   . GLU B 1 222 ? 16.62611  -10.09598 15.33600  1.000 58.52009  ? 991  GLU A C   1 
ATOM   3258 O  O   . GLU B 1 222 ? 17.23821  -11.01409 15.88624  1.000 55.97967  ? 991  GLU A O   1 
ATOM   3259 C  CB  . GLU B 1 222 ? 16.73152  -10.12289 12.87270  1.000 57.03755  ? 991  GLU A CB  1 
ATOM   3260 C  CG  . GLU B 1 222 ? 17.40059  -9.70474  11.59382  1.000 58.05518  ? 991  GLU A CG  1 
ATOM   3261 C  CD  . GLU B 1 222 ? 17.10087  -10.66451 10.45107  1.000 59.10688  ? 991  GLU A CD  1 
ATOM   3262 O  OE1 . GLU B 1 222 ? 17.75634  -11.72888 10.38270  1.000 60.68954  ? 991  GLU A OE1 1 
ATOM   3263 O  OE2 . GLU B 1 222 ? 16.20384  -10.36131 9.63103   1.000 58.20421  ? 991  GLU A OE2 1 
ATOM   3264 N  N   . CYS B 1 223 ? 15.42344  -9.67503  15.72918  1.000 57.07992  ? 992  CYS A N   1 
ATOM   3265 C  CA  . CYS B 1 223 ? 14.75536  -10.31608 16.85518  1.000 57.01692  ? 992  CYS A CA  1 
ATOM   3266 C  C   . CYS B 1 223 ? 14.46645  -11.77805 16.52135  1.000 56.92441  ? 992  CYS A C   1 
ATOM   3267 O  O   . CYS B 1 223 ? 13.95278  -12.07774 15.43790  1.000 58.16523  ? 992  CYS A O   1 
ATOM   3268 C  CB  . CYS B 1 223 ? 13.44642  -9.60800  17.20229  1.000 56.99666  ? 992  CYS A CB  1 
ATOM   3269 S  SG  . CYS B 1 223 ? 12.41550  -10.56504 18.39020  1.000 57.35217  ? 992  CYS A SG  1 
ATOM   3270 N  N   . PRO B 1 224 ? 14.74141  -12.71221 17.43370  1.000 56.38413  ? 993  PRO A N   1 
ATOM   3271 C  CA  . PRO B 1 224 ? 14.51097  -14.12425 17.11045  1.000 56.48413  ? 993  PRO A CA  1 
ATOM   3272 C  C   . PRO B 1 224 ? 13.04881  -14.53475 17.10782  1.000 55.14773  ? 993  PRO A C   1 
ATOM   3273 O  O   . PRO B 1 224 ? 12.75885  -15.67884 16.73882  1.000 55.81712  ? 993  PRO A O   1 
ATOM   3274 C  CB  . PRO B 1 224 ? 15.28058  -14.86105 18.21161  1.000 56.72698  ? 993  PRO A CB  1 
ATOM   3275 C  CG  . PRO B 1 224 ? 15.32033  -13.90980 19.34399  1.000 54.66751  ? 993  PRO A CG  1 
ATOM   3276 C  CD  . PRO B 1 224 ? 15.40067  -12.53914 18.73943  1.000 55.33657  ? 993  PRO A CD  1 
ATOM   3277 N  N   . ILE B 1 225 ? 12.11364  -13.65240 17.45525  1.000 54.62494  ? 994  ILE A N   1 
ATOM   3278 C  CA  . ILE B 1 225 ? 10.70685  -14.00963 17.59829  1.000 54.86543  ? 994  ILE A CA  1 
ATOM   3279 C  C   . ILE B 1 225 ? 9.85179   -13.36976 16.50383  1.000 54.72589  ? 994  ILE A C   1 
ATOM   3280 O  O   . ILE B 1 225 ? 9.02858   -14.03905 15.88191  1.000 52.17615  ? 994  ILE A O   1 
ATOM   3281 C  CB  . ILE B 1 225 ? 10.18539  -13.62334 19.00344  1.000 56.28470  ? 994  ILE A CB  1 
ATOM   3282 C  CG1 . ILE B 1 225 ? 10.96473  -14.35138 20.09708  1.000 54.00894  ? 994  ILE A CG1 1 
ATOM   3283 C  CG2 . ILE B 1 225 ? 8.69450   -13.94748 19.13228  1.000 54.23763  ? 994  ILE A CG2 1 
ATOM   3284 C  CD1 . ILE B 1 225 ? 10.51827  -15.75224 20.33790  1.000 49.90201  ? 994  ILE A CD1 1 
ATOM   3285 N  N   . CYS B 1 226 ? 10.03117  -12.06390 16.26475  1.000 54.85141  ? 995  CYS A N   1 
ATOM   3286 C  CA  . CYS B 1 226 ? 9.27290   -11.32241 15.26022  1.000 56.87653  ? 995  CYS A CA  1 
ATOM   3287 C  C   . CYS B 1 226 ? 10.11170  -10.83893 14.08900  1.000 57.51878  ? 995  CYS A C   1 
ATOM   3288 O  O   . CYS B 1 226 ? 9.54892   -10.28332 13.14290  1.000 57.90017  ? 995  CYS A O   1 
ATOM   3289 C  CB  . CYS B 1 226 ? 8.59000   -10.09469 15.88485  1.000 55.47104  ? 995  CYS A CB  1 
ATOM   3290 S  SG  . CYS B 1 226 ? 9.74817   -8.77730  16.30175  1.000 57.16473  ? 995  CYS A SG  1 
ATOM   3291 N  N   . ARG B 1 227 ? 11.43314  -10.97476 14.16144  1.000 58.96191  ? 996  ARG A N   1 
ATOM   3292 C  CA  . ARG B 1 227 ? 12.38198  -10.75304 13.08097  1.000 60.97823  ? 996  ARG A CA  1 
ATOM   3293 C  C   . ARG B 1 227 ? 12.63037  -9.27473  12.75724  1.000 61.89511  ? 996  ARG A C   1 
ATOM   3294 O  O   . ARG B 1 227 ? 13.47957  -8.98669  11.90954  1.000 62.08908  ? 996  ARG A O   1 
ATOM   3295 C  CB  . ARG B 1 227 ? 11.93701  -11.49237 11.80855  1.000 65.80655  ? 996  ARG A CB  1 
ATOM   3296 C  CG  . ARG B 1 227 ? 12.99369  -11.66007 10.75489  1.000 71.10549  ? 996  ARG A CG  1 
ATOM   3297 C  CD  . ARG B 1 227 ? 12.52175  -12.61736 9.66788   1.000 82.18392  ? 996  ARG A CD  1 
ATOM   3298 N  NE  . ARG B 1 227 ? 12.45907  -13.97565 10.19615  1.000 83.41161  ? 996  ARG A NE  1 
ATOM   3299 C  CZ  . ARG B 1 227 ? 13.50270  -14.75048 10.46006  1.000 75.15347  ? 996  ARG A CZ  1 
ATOM   3300 N  NH1 . ARG B 1 227 ? 14.74386  -14.34250 10.25011  1.000 75.89363  ? 996  ARG A NH1 1 
ATOM   3301 N  NH2 . ARG B 1 227 ? 13.29515  -15.94891 10.99612  1.000 72.32211  ? 996  ARG A NH2 1 
ATOM   3302 N  N   . LYS B 1 228 ? 11.98786  -8.32704  13.44098  1.000 63.29013  ? 997  LYS A N   1 
ATOM   3303 C  CA  . LYS B 1 228 ? 12.31057  -6.92496  13.19369  1.000 62.51469  ? 997  LYS A CA  1 
ATOM   3304 C  C   . LYS B 1 228 ? 13.77994  -6.67479  13.51070  1.000 60.91650  ? 997  LYS A C   1 
ATOM   3305 O  O   . LYS B 1 228 ? 14.37014  -7.32869  14.37587  1.000 58.21578  ? 997  LYS A O   1 
ATOM   3306 C  CB  . LYS B 1 228 ? 11.42609  -5.99136  14.02956  1.000 62.15436  ? 997  LYS A CB  1 
ATOM   3307 C  CG  . LYS B 1 228 ? 9.95006   -6.00641  13.66342  1.000 66.28198  ? 997  LYS A CG  1 
ATOM   3308 C  CD  . LYS B 1 228 ? 9.08709   -5.36245  14.74961  1.000 67.42598  ? 997  LYS A CD  1 
ATOM   3309 C  CE  . LYS B 1 228 ? 7.61255   -5.27507  14.36382  1.000 73.38685  ? 997  LYS A CE  1 
ATOM   3310 N  NZ  . LYS B 1 228 ? 7.28430   -4.05370  13.56411  1.000 83.94166  ? 997  LYS A NZ  1 
ATOM   3311 N  N   . ALA B 1 229 ? 14.39257  -5.76303  12.76103  1.000 60.43382  ? 998  ALA A N   1 
ATOM   3312 C  CA  . ALA B 1 229 ? 15.79522  -5.46160  13.00127  1.000 61.06440  ? 998  ALA A CA  1 
ATOM   3313 C  C   . ALA B 1 229 ? 15.96406  -4.89118  14.40428  1.000 61.06757  ? 998  ALA A C   1 
ATOM   3314 O  O   . ALA B 1 229 ? 15.14888  -4.09033  14.86674  1.000 63.93841  ? 998  ALA A O   1 
ATOM   3315 C  CB  . ALA B 1 229 ? 16.31263  -4.47805  11.95613  1.000 57.69379  ? 998  ALA A CB  1 
ATOM   3316 N  N   . ILE B 1 230 ? 17.03769  -5.29657  15.07814  1.000 60.50575  ? 999  ILE A N   1 
ATOM   3317 C  CA  . ILE B 1 230 ? 17.27320  -4.87028  16.45322  1.000 62.19472  ? 999  ILE A CA  1 
ATOM   3318 C  C   . ILE B 1 230 ? 17.70670  -3.41165  16.44812  1.000 64.62892  ? 999  ILE A C   1 
ATOM   3319 O  O   . ILE B 1 230 ? 18.85318  -3.08970  16.11855  1.000 64.84546  ? 999  ILE A O   1 
ATOM   3320 C  CB  . ILE B 1 230 ? 18.30804  -5.77196  17.16178  1.000 61.80500  ? 999  ILE A CB  1 
ATOM   3321 C  CG1 . ILE B 1 230 ? 17.77254  -7.19451  17.35794  1.000 59.31516  ? 999  ILE A CG1 1 
ATOM   3322 C  CG2 . ILE B 1 230 ? 18.72778  -5.19073  18.49415  1.000 60.96870  ? 999  ILE A CG2 1 
ATOM   3323 C  CD1 . ILE B 1 230 ? 18.76832  -8.11349  18.01247  1.000 58.97934  ? 999  ILE A CD1 1 
ATOM   3324 N  N   . GLU B 1 231 ? 16.76862  -2.52252  16.79072  1.000 67.22025  ? 1000 GLU A N   1 
ATOM   3325 C  CA  . GLU B 1 231 ? 17.05133  -1.09192  16.85002  1.000 69.57304  ? 1000 GLU A CA  1 
ATOM   3326 C  C   . GLU B 1 231 ? 17.91759  -0.74639  18.05355  1.000 67.79517  ? 1000 GLU A C   1 
ATOM   3327 O  O   . GLU B 1 231 ? 18.78842  0.12612   17.96668  1.000 69.23700  ? 1000 GLU A O   1 
ATOM   3328 C  CB  . GLU B 1 231 ? 15.73838  -0.30980  16.90622  1.000 75.82089  ? 1000 GLU A CB  1 
ATOM   3329 C  CG  . GLU B 1 231 ? 14.86887  -0.46628  15.66582  1.000 87.15604  ? 1000 GLU A CG  1 
ATOM   3330 C  CD  . GLU B 1 231 ? 13.54988  0.29526   15.76284  1.000 97.23118  ? 1000 GLU A CD  1 
ATOM   3331 O  OE1 . GLU B 1 231 ? 13.28671  0.92762   16.81172  1.000 90.30865  ? 1000 GLU A OE1 1 
ATOM   3332 O  OE2 . GLU B 1 231 ? 12.77203  0.25141   14.78246  1.000 109.03329 ? 1000 GLU A OE2 1 
ATOM   3333 N  N   . ARG B 1 232 ? 17.67432  -1.39381  19.19193  1.000 66.69109  ? 1001 ARG A N   1 
ATOM   3334 C  CA  . ARG B 1 232 ? 18.33719  -1.02252  20.43354  1.000 64.99331  ? 1001 ARG A CA  1 
ATOM   3335 C  C   . ARG B 1 232 ? 18.22770  -2.18649  21.40902  1.000 62.89908  ? 1001 ARG A C   1 
ATOM   3336 O  O   . ARG B 1 232 ? 17.23463  -2.91798  21.39482  1.000 61.76305  ? 1001 ARG A O   1 
ATOM   3337 C  CB  . ARG B 1 232 ? 17.72851  0.25918   21.02028  1.000 65.78819  ? 1001 ARG A CB  1 
ATOM   3338 C  CG  . ARG B 1 232 ? 18.39631  0.77077   22.27843  1.000 65.82206  ? 1001 ARG A CG  1 
ATOM   3339 C  CD  . ARG B 1 232 ? 17.58494  1.89667   22.90769  1.000 70.60111  ? 1001 ARG A CD  1 
ATOM   3340 N  NE  . ARG B 1 232 ? 18.23940  2.46899   24.08024  1.000 77.08664  ? 1001 ARG A NE  1 
ATOM   3341 C  CZ  . ARG B 1 232 ? 17.99832  3.68317   24.55752  1.000 73.63653  ? 1001 ARG A CZ  1 
ATOM   3342 N  NH1 . ARG B 1 232 ? 17.12903  4.49307   23.97718  1.000 74.48526  ? 1001 ARG A NH1 1 
ATOM   3343 N  NH2 . ARG B 1 232 ? 18.63446  4.08963   25.65401  1.000 71.58790  ? 1001 ARG A NH2 1 
ATOM   3344 N  N   . ARG B 1 233 ? 19.27060  -2.37594  22.21750  1.000 61.84415  ? 1002 ARG A N   1 
ATOM   3345 C  CA  . ARG B 1 233 ? 19.31506  -3.41620  23.24215  1.000 61.96671  ? 1002 ARG A CA  1 
ATOM   3346 C  C   . ARG B 1 233 ? 19.35510  -2.77133  24.61956  1.000 60.16805  ? 1002 ARG A C   1 
ATOM   3347 O  O   . ARG B 1 233 ? 20.33538  -2.10551  24.97078  1.000 59.09335  ? 1002 ARG A O   1 
ATOM   3348 C  CB  . ARG B 1 233 ? 20.51295  -4.34965  23.07700  1.000 63.42413  ? 1002 ARG A CB  1 
ATOM   3349 C  CG  . ARG B 1 233 ? 20.55661  -5.15752  21.79459  1.000 64.56237  ? 1002 ARG A CG  1 
ATOM   3350 C  CD  . ARG B 1 233 ? 21.97796  -5.58958  21.49372  1.000 66.80174  ? 1002 ARG A CD  1 
ATOM   3351 N  NE  . ARG B 1 233 ? 22.06294  -6.30907  20.23296  1.000 65.34339  ? 1002 ARG A NE  1 
ATOM   3352 C  CZ  . ARG B 1 233 ? 22.34335  -5.74230  19.07333  1.000 64.72252  ? 1002 ARG A CZ  1 
ATOM   3353 N  NH1 . ARG B 1 233 ? 22.54626  -4.43913  18.97580  1.000 61.61255  ? 1002 ARG A NH1 1 
ATOM   3354 N  NH2 . ARG B 1 233 ? 22.42135  -6.50204  17.98530  1.000 66.19572  ? 1002 ARG A NH2 1 
ATOM   3355 N  N   . ILE B 1 234 ? 18.30691  -3.00468  25.40292  1.000 59.28452  ? 1003 ILE A N   1 
ATOM   3356 C  CA  . ILE B 1 234 ? 18.13648  -2.42483  26.73128  1.000 58.54089  ? 1003 ILE A CA  1 
ATOM   3357 C  C   . ILE B 1 234 ? 18.35697  -3.52525  27.75441  1.000 58.07633  ? 1003 ILE A C   1 
ATOM   3358 O  O   . ILE B 1 234 ? 17.63310  -4.52683  27.75307  1.000 57.96708  ? 1003 ILE A O   1 
ATOM   3359 C  CB  . ILE B 1 234 ? 16.73428  -1.81771  26.88517  1.000 58.43945  ? 1003 ILE A CB  1 
ATOM   3360 C  CG1 . ILE B 1 234 ? 16.52531  -0.71871  25.84033  1.000 61.54010  ? 1003 ILE A CG1 1 
ATOM   3361 C  CG2 . ILE B 1 234 ? 16.49366  -1.34163  28.31627  1.000 58.53464  ? 1003 ILE A CG2 1 
ATOM   3362 C  CD1 . ILE B 1 234 ? 15.08696  -0.44483  25.52278  1.000 62.82309  ? 1003 ILE A CD1 1 
ATOM   3363 N  N   . LEU B 1 235 ? 19.32803  -3.33857  28.64324  1.000 58.24268  ? 1004 LEU A N   1 
ATOM   3364 C  CA  . LEU B 1 235 ? 19.61903  -4.35691  29.64755  1.000 63.48933  ? 1004 LEU A CA  1 
ATOM   3365 C  C   . LEU B 1 235 ? 18.66779  -4.23777  30.82664  1.000 64.29905  ? 1004 LEU A C   1 
ATOM   3366 O  O   . LEU B 1 235 ? 18.29986  -3.13657  31.22704  1.000 62.60898  ? 1004 LEU A O   1 
ATOM   3367 C  CB  . LEU B 1 235 ? 21.05547  -4.23207  30.14258  1.000 65.48503  ? 1004 LEU A CB  1 
ATOM   3368 C  CG  . LEU B 1 235 ? 22.11653  -4.39199  29.06991  1.000 65.41363  ? 1004 LEU A CG  1 
ATOM   3369 C  CD1 . LEU B 1 235 ? 23.42999  -3.86625  29.58985  1.000 64.67274  ? 1004 LEU A CD1 1 
ATOM   3370 C  CD2 . LEU B 1 235 ? 22.23168  -5.86793  28.69794  1.000 66.32748  ? 1004 LEU A CD2 1 
ATOM   3371 N  N   . LEU B 1 236 ? 18.26547  -5.37479  31.38001  1.000 64.14643  ? 1005 LEU A N   1 
ATOM   3372 C  CA  . LEU B 1 236 ? 17.28895  -5.37468  32.45992  1.000 67.04501  ? 1005 LEU A CA  1 
ATOM   3373 C  C   . LEU B 1 236 ? 17.94961  -5.59464  33.81025  1.000 70.33565  ? 1005 LEU A C   1 
ATOM   3374 O  O   . LEU B 1 236 ? 18.95719  -6.29823  33.91497  1.000 78.02013  ? 1005 LEU A O   1 
ATOM   3375 C  CB  . LEU B 1 236 ? 16.22960  -6.44815  32.25867  1.000 64.77240  ? 1005 LEU A CB  1 
ATOM   3376 C  CG  . LEU B 1 236 ? 15.40163  -6.39882  30.99276  1.000 63.31264  ? 1005 LEU A CG  1 
ATOM   3377 C  CD1 . LEU B 1 236 ? 14.21788  -7.29702  31.23956  1.000 61.89567  ? 1005 LEU A CD1 1 
ATOM   3378 C  CD2 . LEU B 1 236 ? 14.97667  -4.97383  30.74895  1.000 64.15220  ? 1005 LEU A CD2 1 
ATOM   3379 N  N   . TYR B 1 237 ? 17.35819  -4.97863  34.84405  1.000 73.08352  ? 1006 TYR A N   1 
ATOM   3380 C  CA  . TYR B 1 237 ? 17.76881  -5.10776  36.25115  1.000 70.20563  ? 1006 TYR A CA  1 
ATOM   3381 C  C   . TYR B 1 237 ? 16.54919  -5.11396  37.20928  1.000 74.20889  ? 1006 TYR A C   1 
ATOM   3382 O  O   . TYR B 1 237 ? 15.42974  -4.74665  36.82983  1.000 71.15360  ? 1006 TYR A O   1 
ATOM   3383 C  CB  . TYR B 1 237 ? 18.72282  -3.97074  36.62041  1.000 70.01230  ? 1006 TYR A CB  1 
ATOM   3384 C  CG  . TYR B 1 237 ? 19.81086  -3.82969  35.60674  1.000 72.42713  ? 1006 TYR A CG  1 
ATOM   3385 C  CD1 . TYR B 1 237 ? 20.85004  -4.74468  35.54229  1.000 72.61017  ? 1006 TYR A CD1 1 
ATOM   3386 C  CD2 . TYR B 1 237 ? 19.76154  -2.81616  34.65983  1.000 74.17197  ? 1006 TYR A CD2 1 
ATOM   3387 C  CE1 . TYR B 1 237 ? 21.83409  -4.63389  34.57196  1.000 75.59081  ? 1006 TYR A CE1 1 
ATOM   3388 C  CE2 . TYR B 1 237 ? 20.73559  -2.69144  33.69077  1.000 73.41340  ? 1006 TYR A CE2 1 
ATOM   3389 C  CZ  . TYR B 1 237 ? 21.77231  -3.60109  33.64982  1.000 75.02846  ? 1006 TYR A CZ  1 
ATOM   3390 O  OH  . TYR B 1 237 ? 22.74698  -3.48190  32.68591  1.000 70.20917  ? 1006 TYR A OH  1 
ATOM   3391 O  OXT . TYR B 1 237 ? 16.62498  -5.47851  38.39364  1.000 69.19927  ? 1006 TYR A OXT 1 
HETATM 3392 ZN ZN  . ZN  C 2 .   ? 2.60283   -4.72734  39.01183  1.000 56.01009  ? 1101 ZN  B ZN  1 
HETATM 3393 ZN ZN  . ZN  D 2 .   ? 14.80620  2.51812   36.97209  1.000 59.35462  ? 1102 ZN  B ZN  1 
HETATM 3394 ZN ZN  . ZN  E 2 .   ? 20.67728  -16.72095 25.58728  1.000 55.44433  ? 1101 ZN  A ZN  1 
HETATM 3395 ZN ZN  . ZN  F 2 .   ? 10.64571  -9.09449  18.42106  1.000 53.25214  ? 1102 ZN  A ZN  1 
HETATM 3396 ZN ZN  . ZN  G 2 .   ? 27.83836  -32.32989 7.15629   1.000 76.01411  ? 1103 ZN  A ZN  1 
HETATM 3397 O  O   . HOH H 3 .   ? 18.45234  0.43108   76.28614  1.000 53.84112  ? 1201 HOH B O   1 
HETATM 3398 O  O   . HOH H 3 .   ? -5.86555  10.38639  48.02111  1.000 75.05690  ? 1202 HOH B O   1 
HETATM 3399 O  O   . HOH H 3 .   ? 10.40567  5.63438   75.10921  1.000 40.98276  ? 1203 HOH B O   1 
HETATM 3400 O  O   . HOH H 3 .   ? 13.15203  4.56858   31.29671  1.000 69.47566  ? 1204 HOH B O   1 
HETATM 3401 O  O   . HOH H 3 .   ? 9.298     -10.582   64.588    1.000 38.46100  ? 1205 HOH B O   1 
HETATM 3402 O  O   . HOH H 3 .   ? 22.91942  8.16553   66.32490  1.000 53.58760  ? 1206 HOH B O   1 
HETATM 3403 O  O   . HOH H 3 .   ? 6.29145   1.36798   80.43172  1.000 52.88024  ? 1207 HOH B O   1 
HETATM 3404 O  O   . HOH H 3 .   ? 10.88187  12.58682  70.74890  1.000 39.32026  ? 1208 HOH B O   1 
HETATM 3405 O  O   . HOH H 3 .   ? 5.87402   11.09022  42.72386  1.000 64.43182  ? 1209 HOH B O   1 
HETATM 3406 O  O   . HOH H 3 .   ? 7.69417   10.72608  71.47883  1.000 45.22372  ? 1210 HOH B O   1 
HETATM 3407 O  O   . HOH H 3 .   ? 4.15532   10.17318  61.33730  1.000 42.56800  ? 1211 HOH B O   1 
HETATM 3408 O  O   . HOH H 3 .   ? 3.56696   1.21376   74.70285  1.000 49.03135  ? 1212 HOH B O   1 
HETATM 3409 O  O   . HOH H 3 .   ? 3.06352   9.06674   55.31933  1.000 49.20905  ? 1213 HOH B O   1 
HETATM 3410 O  O   . HOH H 3 .   ? 11.23955  -10.16985 56.71878  1.000 61.36720  ? 1214 HOH B O   1 
HETATM 3411 O  O   . HOH H 3 .   ? 13.86271  -9.01298  34.72004  1.000 69.05112  ? 1215 HOH B O   1 
HETATM 3412 O  O   . HOH H 3 .   ? 8.39764   1.28677   81.21999  1.000 54.47856  ? 1216 HOH B O   1 
HETATM 3413 O  O   . HOH H 3 .   ? 23.77616  24.10325  72.10087  1.000 47.16075  ? 1217 HOH B O   1 
HETATM 3414 O  O   . HOH H 3 .   ? 14.42583  -12.86729 67.25077  1.000 44.04701  ? 1218 HOH B O   1 
HETATM 3415 O  O   . HOH H 3 .   ? 5.50974   0.14954   78.12147  1.000 54.54088  ? 1219 HOH B O   1 
HETATM 3416 O  O   . HOH H 3 .   ? 13.40559  6.93622   74.18600  1.000 42.79112  ? 1220 HOH B O   1 
HETATM 3417 O  O   . HOH H 3 .   ? 18.89988  4.89138   31.82897  1.000 67.81264  ? 1221 HOH B O   1 
HETATM 3418 O  O   . HOH H 3 .   ? 3.44817   8.92622   58.12931  1.000 44.28263  ? 1222 HOH B O   1 
HETATM 3419 O  O   . HOH H 3 .   ? 13.86285  -4.85916  72.81307  1.000 48.44835  ? 1223 HOH B O   1 
HETATM 3420 O  O   . HOH H 3 .   ? 6.49141   -8.16230  50.75874  1.000 47.69065  ? 1224 HOH B O   1 
HETATM 3421 O  O   . HOH H 3 .   ? 7.82221   20.37837  51.33914  1.000 66.81189  ? 1225 HOH B O   1 
HETATM 3422 O  O   . HOH H 3 .   ? 5.04729   9.02169   70.78249  1.000 47.32857  ? 1226 HOH B O   1 
HETATM 3423 O  O   . HOH H 3 .   ? 12.95480  -4.65949  65.38002  1.000 44.14834  ? 1227 HOH B O   1 
HETATM 3424 O  O   . HOH H 3 .   ? 7.78868   -11.26309 30.35395  1.000 58.85302  ? 1228 HOH B O   1 
HETATM 3425 O  O   . HOH I 3 .   ? 15.52903  -5.09968  40.25238  1.000 64.37037  ? 1201 HOH A O   1 
HETATM 3426 O  O   . HOH I 3 .   ? 9.00000   -41.95270 -1.89824  1.000 53.51067  ? 1202 HOH A O   1 
HETATM 3427 O  O   . HOH I 3 .   ? 3.80536   -35.36954 -17.62428 1.000 67.10292  ? 1203 HOH A O   1 
HETATM 3428 O  O   . HOH I 3 .   ? 22.23880  -32.84948 5.86898   1.000 51.53758  ? 1204 HOH A O   1 
HETATM 3429 O  O   . HOH I 3 .   ? -5.74036  -34.10696 2.01731   1.000 63.82636  ? 1205 HOH A O   1 
HETATM 3430 O  O   . HOH I 3 .   ? 19.16729  -39.16814 -6.61637  1.000 60.92156  ? 1206 HOH A O   1 
HETATM 3431 O  O   . HOH I 3 .   ? 16.38219  7.38231   24.22499  1.000 63.70414  ? 1207 HOH A O   1 
HETATM 3432 O  O   . HOH I 3 .   ? 16.01934  -43.32435 -2.08959  1.000 44.04701  ? 1208 HOH A O   1 
HETATM 3433 O  O   . HOH I 3 .   ? -6.02947  -31.94556 2.69001   1.000 67.30037  ? 1209 HOH A O   1 
HETATM 3434 O  O   . HOH I 3 .   ? 13.42917  -5.48739  39.62949  1.000 67.25950  ? 1210 HOH A O   1 
HETATM 3435 O  O   . HOH I 3 .   ? 6.48074   -11.88607 28.53303  1.000 69.02838  ? 1211 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1   ? 0.79275 0.72002 0.90583 -0.00473 -0.02543 -0.09326 0    SER B N   
2    C CA  . SER A 1   ? 0.72678 0.66070 0.83454 0.00547  -0.02936 -0.08668 0    SER B CA  
3    C C   . SER A 1   ? 0.74056 0.66444 0.82705 0.01241  -0.02351 -0.07608 0    SER B C   
4    O O   . SER A 1   ? 0.74060 0.65577 0.81998 0.00861  -0.01575 -0.07311 0    SER B O   
5    C CB  . SER A 1   ? 0.76065 0.71120 0.88720 0.00278  -0.02725 -0.08518 0    SER B CB  
6    O OG  . SER A 1   ? 0.70512 0.65541 0.83153 -0.00171 -0.01666 -0.07894 0    SER B OG  
7    N N   . MET A 2   ? 0.74931 0.67455 0.82631 0.02273  -0.02672 -0.07024 1    MET B N   
8    C CA  . MET A 2   ? 0.77093 0.68804 0.82983 0.02994  -0.02107 -0.06026 1    MET B CA  
9    C C   . MET A 2   ? 0.72670 0.64859 0.79089 0.02554  -0.01170 -0.05400 1    MET B C   
10   O O   . MET A 2   ? 0.70790 0.62037 0.75976 0.02657  -0.00571 -0.04886 1    MET B O   
11   C CB  . MET A 2   ? 0.80495 0.72443 0.85645 0.04090  -0.02508 -0.05546 1    MET B CB  
12   C CG  . MET A 2   ? 0.93617 0.84540 0.96793 0.04964  -0.02040 -0.04660 1    MET B CG  
13   S SD  . MET A 2   ? 1.16456 1.07246 1.18508 0.06263  -0.02495 -0.04249 1    MET B SD  
14   C CE  . MET A 2   ? 1.03281 0.93439 1.04920 0.06374  -0.03717 -0.05338 1    MET B CE  
15   N N   . ALA A 3   ? 0.72970 0.66568 0.81194 0.02066  -0.01065 -0.05486 2    ALA B N   
16   C CA  . ALA A 3   ? 0.68756 0.62842 0.77514 0.01628  -0.00258 -0.04979 2    ALA B CA  
17   C C   . ALA A 3   ? 0.67635 0.60805 0.76147 0.00827  0.00321  -0.05210 2    ALA B C   
18   O O   . ALA A 3   ? 0.65711 0.58298 0.73276 0.00888  0.00951  -0.04601 2    ALA B O   
19   C CB  . ALA A 3   ? 0.66316 0.61969 0.77056 0.01222  -0.00322 -0.05187 2    ALA B CB  
20   N N   . LEU A 4   ? 0.68351 0.61334 0.77708 0.00092  0.00122  -0.06106 3    LEU B N   
21   C CA  . LEU A 4   ? 0.67634 0.59614 0.76804 -0.00735 0.00773  -0.06380 3    LEU B CA  
22   C C   . LEU A 4   ? 0.69861 0.60085 0.76889 -0.00329 0.00944  -0.06098 3    LEU B C   
23   O O   . LEU A 4   ? 0.68863 0.58106 0.74991 -0.00584 0.01684  -0.05757 3    LEU B O   
24   C CB  . LEU A 4   ? 0.68443 0.60738 0.79288 -0.01631 0.00531  -0.07475 3    LEU B CB  
25   C CG  . LEU A 4   ? 0.70805 0.61982 0.81651 -0.02593 0.01266  -0.07898 3    LEU B CG  
26   C CD1 . LEU A 4   ? 0.71031 0.62303 0.81992 -0.03008 0.02212  -0.07380 3    LEU B CD1 
27   C CD2 . LEU A 4   ? 0.73859 0.65609 0.86706 -0.03420 0.00940  -0.09044 3    LEU B CD2 
28   N N   . LYS A 5   ? 0.72214 0.61913 0.78275 0.00354  0.00277  -0.06228 4    LYS B N   
29   C CA  . LYS A 5   ? 0.70509 0.58517 0.74445 0.00846  0.00470  -0.05901 4    LYS B CA  
30   C C   . LYS A 5   ? 0.69145 0.57009 0.71949 0.01511  0.01021  -0.04823 4    LYS B C   
31   O O   . LYS A 5   ? 0.65282 0.51979 0.66903 0.01480  0.01623  -0.04473 4    LYS B O   
32   C CB  . LYS A 5   ? 0.74064 0.61525 0.77052 0.01550  -0.00352 -0.06209 4    LYS B CB  
33   C CG  . LYS A 5   ? 0.77089 0.64646 0.81111 0.01004  -0.01094 -0.07366 4    LYS B CG  
34   C CD  . LYS A 5   ? 0.83711 0.70501 0.86359 0.01851  -0.01945 -0.07598 4    LYS B CD  
35   C CE  . LYS A 5   ? 0.87871 0.75371 0.91860 0.01581  -0.02986 -0.08679 4    LYS B CE  
36   N NZ  . LYS A 5   ? 0.88403 0.75476 0.93402 0.00492  -0.02987 -0.09698 4    LYS B NZ  
37   N N   . ARG A 6   ? 0.67345 0.56427 0.70632 0.02079  0.00848  -0.04313 5    ARG B N   
38   C CA  . ARG A 6   ? 0.67565 0.56705 0.70069 0.02702  0.01319  -0.03354 5    ARG B CA  
39   C C   . ARG A 6   ? 0.69710 0.58954 0.72578 0.02103  0.01993  -0.03104 5    ARG B C   
40   O O   . ARG A 6   ? 0.66965 0.55480 0.68665 0.02464  0.02436  -0.02502 5    ARG B O   
41   C CB  . ARG A 6   ? 0.67186 0.57618 0.70347 0.03325  0.01020  -0.02973 5    ARG B CB  
42   C CG  . ARG A 6   ? 0.68062 0.59153 0.71326 0.03653  0.01488  -0.02164 5    ARG B CG  
43   C CD  . ARG A 6   ? 0.71783 0.62069 0.73526 0.04580  0.01716  -0.01484 5    ARG B CD  
44   N NE  . ARG A 6   ? 0.75231 0.66421 0.77515 0.04752  0.02112  -0.00825 5    ARG B NE  
45   C CZ  . ARG A 6   ? 0.69146 0.61099 0.71695 0.05422  0.02162  -0.00291 5    ARG B CZ  
46   N NH1 . ARG A 6   ? 0.67448 0.59173 0.69478 0.06094  0.01932  -0.00229 5    ARG B NH1 
47   N NH2 . ARG A 6   ? 0.70717 0.63631 0.74057 0.05412  0.02465  0.00166  5    ARG B NH2 
48   N N   . ILE A 7   ? 0.66228 0.56259 0.70614 0.01219  0.02080  -0.03583 6    ILE B N   
49   C CA  . ILE A 7   ? 0.65332 0.55251 0.69879 0.00625  0.02750  -0.03407 6    ILE B CA  
50   C C   . ILE A 7   ? 0.63058 0.51159 0.66210 0.00335  0.03238  -0.03503 6    ILE B C   
51   O O   . ILE A 7   ? 0.62591 0.50000 0.64743 0.00440  0.03764  -0.02980 6    ILE B O   
52   C CB  . ILE A 7   ? 0.63585 0.54613 0.70044 -0.00268 0.02803  -0.03968 6    ILE B CB  
53   C CG1 . ILE A 7   ? 0.58817 0.51544 0.66520 0.00043  0.02460  -0.03746 6    ILE B CG1 
54   C CG2 . ILE A 7   ? 0.63102 0.53661 0.69454 -0.00924 0.03574  -0.03864 6    ILE B CG2 
55   C CD1 . ILE A 7   ? 0.58773 0.52604 0.68435 -0.00708 0.02355  -0.04413 6    ILE B CD1 
56   N N   . HIS A 8   ? 0.65665 0.52913 0.68710 -0.00025 0.03059  -0.04194 7    HIS B N   
57   C CA  . HIS A 8   ? 0.68692 0.54044 0.70298 -0.00264 0.03570  -0.04273 7    HIS B CA  
58   C C   . HIS A 8   ? 0.68640 0.52973 0.68276 0.00730  0.03648  -0.03517 7    HIS B C   
59   O O   . HIS A 8   ? 0.66271 0.49320 0.64596 0.00771  0.04235  -0.03147 7    HIS B O   
60   C CB  . HIS A 8   ? 0.68088 0.52744 0.70020 -0.00812 0.03303  -0.05209 7    HIS B CB  
61   C CG  . HIS A 8   ? 0.74227 0.59245 0.77822 -0.01976 0.03609  -0.05964 7    HIS B CG  
62   N ND1 . HIS A 8   ? 0.75115 0.61468 0.80670 -0.02400 0.03033  -0.06720 7    HIS B ND1 
63   C CD2 . HIS A 8   ? 0.82237 0.66426 0.85841 -0.02779 0.04480  -0.06077 7    HIS B CD2 
64   C CE1 . HIS A 8   ? 0.77983 0.64422 0.84861 -0.03446 0.03556  -0.07290 7    HIS B CE1 
65   N NE2 . HIS A 8   ? 0.80698 0.65774 0.86370 -0.03709 0.04483  -0.06905 7    HIS B NE2 
66   N N   . LYS A 9   ? 0.67534 0.52368 0.66909 0.01582  0.03095  -0.03271 8    LYS B N   
67   C CA  . LYS A 9   ? 0.71950 0.55897 0.69605 0.02577  0.03202  -0.02571 8    LYS B CA  
68   C C   . LYS A 9   ? 0.66467 0.50798 0.63877 0.02938  0.03623  -0.01761 8    LYS B C   
69   O O   . LYS A 9   ? 0.68204 0.51314 0.64159 0.03328  0.04017  -0.01319 8    LYS B O   
70   C CB  . LYS A 9   ? 0.69264 0.53763 0.66819 0.03403  0.02623  -0.02454 8    LYS B CB  
71   C CG  . LYS A 9   ? 0.71083 0.54797 0.67045 0.04476  0.02802  -0.01723 8    LYS B CG  
72   C CD  . LYS A 9   ? 0.72775 0.54463 0.66994 0.04579  0.03003  -0.01899 8    LYS B CD  
73   C CE  . LYS A 9   ? 0.80391 0.61268 0.73085 0.05617  0.03340  -0.01105 8    LYS B CE  
74   N NZ  . LYS A 9   ? 0.91089 0.69844 0.81974 0.05744  0.03568  -0.01284 8    LYS B NZ  
75   N N   . GLU A 10  ? 0.61037 0.47019 0.59863 0.02808  0.03519  -0.01599 9    GLU B N   
76   C CA  . GLU A 10  ? 0.62639 0.49130 0.61386 0.03130  0.03804  -0.00912 9    GLU B CA  
77   C C   . GLU A 10  ? 0.62269 0.47680 0.60300 0.02598  0.04346  -0.00921 9    GLU B C   
78   O O   . GLU A 10  ? 0.60893 0.45764 0.57881 0.03089  0.04600  -0.00343 9    GLU B O   
79   C CB  . GLU A 10  ? 0.61070 0.49485 0.61551 0.02970  0.03588  -0.00853 9    GLU B CB  
80   C CG  . GLU A 10  ? 0.61772 0.51224 0.62782 0.03676  0.03188  -0.00612 9    GLU B CG  
81   C CD  . GLU A 10  ? 0.61503 0.52703 0.64055 0.03606  0.03090  -0.00426 9    GLU B CD  
82   O OE1 . GLU A 10  ? 0.60150 0.51768 0.62849 0.03614  0.03320  -0.00044 9    GLU B OE1 
83   O OE2 . GLU A 10  ? 0.63241 0.55342 0.66806 0.03569  0.02757  -0.00680 9    GLU B OE2 
84   N N   . LEU A 11  ? 0.59693 0.44696 0.58236 0.01628  0.04547  -0.01586 10   LEU B N   
85   C CA  . LEU A 11  ? 0.65746 0.49474 0.63477 0.01080  0.05196  -0.01619 10   LEU B CA  
86   C C   . LEU A 11  ? 0.67325 0.49009 0.63023 0.01477  0.05524  -0.01400 10   LEU B C   
87   O O   . LEU A 11  ? 0.65606 0.46292 0.60025 0.01708  0.05951  -0.00935 10   LEU B O   
88   C CB  . LEU A 11  ? 0.66208 0.49941 0.65110 -0.00068 0.05427  -0.02435 10   LEU B CB  
89   C CG  . LEU A 11  ? 0.72649 0.55188 0.70939 -0.00745 0.06232  -0.02491 10   LEU B CG  
90   C CD1 . LEU A 11  ? 0.75950 0.58968 0.73886 -0.00421 0.06383  -0.01851 10   LEU B CD1 
91   C CD2 . LEU A 11  ? 0.76162 0.59116 0.76102 -0.01873 0.06455  -0.03330 10   LEU B CD2 
92   N N   . ASN A 12  ? 0.69574 0.50549 0.64847 0.01625  0.05302  -0.01723 11   ASN B N   
93   C CA  . ASN A 12  ? 0.71596 0.50557 0.64889 0.02045  0.05627  -0.01518 11   ASN B CA  
94   C C   . ASN A 12  ? 0.71289 0.50239 0.63486 0.03212  0.05564  -0.00641 11   ASN B C   
95   O O   . ASN A 12  ? 0.73590 0.51098 0.64211 0.03565  0.05989  -0.00233 11   ASN B O   
96   C CB  . ASN A 12  ? 0.75670 0.53905 0.68749 0.01971  0.05340  -0.02104 11   ASN B CB  
97   C CG  . ASN A 12  ? 0.78718 0.56815 0.72912 0.00796  0.05421  -0.03048 11   ASN B CG  
98   O OD1 . ASN A 12  ? 0.91274 0.68639 0.85477 0.00045  0.06049  -0.03231 11   ASN B OD1 
99   N ND2 . ASN A 12  ? 0.82839 0.61673 0.78037 0.00651  0.04789  -0.03664 11   ASN B ND2 
100  N N   . ASP A 13  ? 0.68786 0.49318 0.61839 0.03836  0.05073  -0.00340 12   ASP B N   
101  C CA  . ASP A 13  ? 0.72567 0.53226 0.64858 0.04926  0.05054  0.00454  12   ASP B CA  
102  C C   . ASP A 13  ? 0.69563 0.50593 0.61835 0.04995  0.05249  0.00917  12   ASP B C   
103  O O   . ASP A 13  ? 0.66522 0.46764 0.57561 0.05728  0.05413  0.01465  12   ASP B O   
104  C CB  . ASP A 13  ? 0.70326 0.52558 0.63645 0.05518  0.04595  0.00644  12   ASP B CB  
105  C CG  . ASP A 13  ? 0.75677 0.57274 0.68539 0.05717  0.04365  0.00288  12   ASP B CG  
106  O OD1 . ASP A 13  ? 0.76060 0.56058 0.67897 0.05368  0.04518  -0.00141 12   ASP B OD1 
107  O OD2 . ASP A 13  ? 0.75225 0.57834 0.68687 0.06224  0.04048  0.00424  12   ASP B OD2 
108  N N   . LEU A 14  ? 0.67657 0.49678 0.61134 0.04233  0.05246  0.00658  13   LEU B N   
109  C CA  . LEU A 14  ? 0.66270 0.48430 0.59520 0.04245  0.05417  0.01017  13   LEU B CA  
110  C C   . LEU A 14  ? 0.68845 0.48865 0.60286 0.04055  0.05979  0.01043  13   LEU B C   
111  O O   . LEU A 14  ? 0.68443 0.47922 0.58799 0.04600  0.06075  0.01553  13   LEU B O   
112  C CB  . LEU A 14  ? 0.66972 0.50487 0.61817 0.03415  0.05357  0.00666  13   LEU B CB  
113  C CG  . LEU A 14  ? 0.63940 0.49637 0.60536 0.03607  0.04877  0.00772  13   LEU B CG  
114  C CD1 . LEU A 14  ? 0.61321 0.47882 0.59291 0.02639  0.04934  0.00269  13   LEU B CD1 
115  C CD2 . LEU A 14  ? 0.64416 0.50688 0.60774 0.04335  0.04731  0.01400  13   LEU B CD2 
116  N N   . ALA A 15  ? 0.69101 0.47777 0.60094 0.03393  0.06335  0.00513  14   ALA B N   
117  C CA  . ALA A 15  ? 0.70928 0.47395 0.60171 0.03148  0.07001  0.00524  14   ALA B CA  
118  C C   . ALA A 15  ? 0.75437 0.50313 0.62783 0.04077  0.07111  0.00977  14   ALA B C   
119  O O   . ALA A 15  ? 0.72973 0.46523 0.58717 0.04489  0.07444  0.01420  14   ALA B O   
120  C CB  . ALA A 15  ? 0.70001 0.45611 0.59657 0.01994  0.07433  -0.00272 14   ALA B CB  
121  N N   . ARG A 16  ? 0.74563 0.49548 0.61984 0.04516  0.06812  0.00911  15   ARG B N   
122  C CA  . ARG A 16  ? 0.77800 0.51288 0.63452 0.05451  0.06947  0.01343  15   ARG B CA  
123  C C   . ARG A 16  ? 0.76557 0.51001 0.62106 0.06620  0.06617  0.02109  15   ARG B C   
124  O O   . ARG A 16  ? 0.83781 0.56949 0.67781 0.07467  0.06792  0.02571  15   ARG B O   
125  C CB  . ARG A 16  ? 0.84010 0.57060 0.69564 0.05555  0.06790  0.00987  15   ARG B CB  
126  C CG  . ARG A 16  ? 0.86278 0.58403 0.72037 0.04475  0.06994  0.00131  15   ARG B CG  
127  C CD  . ARG A 16  ? 0.95901 0.67729 0.81478 0.04762  0.06664  -0.00190 15   ARG B CD  
128  N NE  . ARG A 16  ? 1.08441 0.82281 0.95270 0.05289  0.06039  -0.00010 15   ARG B NE  
129  C CZ  . ARG A 16  ? 1.15762 0.89803 1.02026 0.06390  0.05874  0.00543  15   ARG B CZ  
130  N NH1 . ARG A 16  ? 1.10177 0.82565 0.94664 0.07125  0.06209  0.00929  15   ARG B NH1 
131  N NH2 . ARG A 16  ? 1.00626 0.76528 0.88156 0.06775  0.05429  0.00725  15   ARG B NH2 
132  N N   . ASP A 17  ? 0.77717 0.54350 0.64934 0.06682  0.06166  0.02235  16   ASP B N   
133  C CA  . ASP A 17  ? 0.79201 0.57006 0.66718 0.07708  0.05830  0.02881  16   ASP B CA  
134  C C   . ASP A 17  ? 0.77228 0.56444 0.65827 0.07363  0.05612  0.02929  16   ASP B C   
135  O O   . ASP A 17  ? 0.87269 0.68483 0.77632 0.07291  0.05233  0.02895  16   ASP B O   
136  C CB  . ASP A 17  ? 0.83235 0.62420 0.71886 0.08232  0.05493  0.02966  16   ASP B CB  
137  C CG  . ASP A 17  ? 0.87894 0.68053 0.76825 0.09344  0.05280  0.03618  16   ASP B CG  
138  O OD1 . ASP A 17  ? 0.84403 0.64376 0.72790 0.09712  0.05249  0.03970  16   ASP B OD1 
139  O OD2 . ASP A 17  ? 1.04287 0.85591 0.94195 0.09804  0.05113  0.03744  16   ASP B OD2 
140  N N   . PRO A 18  ? 0.76673 0.54759 0.64134 0.07147  0.05879  0.03003  17   PRO B N   
141  C CA  . PRO A 18  ? 0.71719 0.50909 0.60017 0.06715  0.05714  0.02960  17   PRO B CA  
142  C C   . PRO A 18  ? 0.69965 0.50859 0.59125 0.07555  0.05142  0.03426  17   PRO B C   
143  O O   . PRO A 18  ? 0.71525 0.52067 0.59890 0.08574  0.04998  0.03902  17   PRO B O   
144  C CB  . PRO A 18  ? 0.70249 0.47338 0.56584 0.06499  0.06214  0.03012  17   PRO B CB  
145  C CG  . PRO A 18  ? 0.74600 0.49861 0.59085 0.07301  0.06440  0.03357  17   PRO B CG  
146  C CD  . PRO A 18  ? 0.76461 0.52036 0.61669 0.07294  0.06398  0.03124  17   PRO B CD  
147  N N   . PRO A 19  ? 0.64682 0.47367 0.55463 0.07144  0.04830  0.03276  18   PRO B N   
148  C CA  . PRO A 19  ? 0.66491 0.50654 0.58038 0.07826  0.04302  0.03646  18   PRO B CA  
149  C C   . PRO A 19  ? 0.69984 0.52902 0.59825 0.08144  0.04290  0.03888  18   PRO B C   
150  O O   . PRO A 19  ? 0.69675 0.50810 0.58013 0.07632  0.04764  0.03726  18   PRO B O   
151  C CB  . PRO A 19  ? 0.61680 0.47742 0.55220 0.07097  0.04081  0.03314  18   PRO B CB  
152  C CG  . PRO A 19  ? 0.58491 0.44350 0.52556 0.06258  0.04410  0.02835  18   PRO B CG  
153  C CD  . PRO A 19  ? 0.64448 0.47988 0.56592 0.06066  0.04918  0.02735  18   PRO B CD  
154  N N   . ALA A 20  ? 0.68634 0.52291 0.58551 0.09088  0.03781  0.04294  19   ALA B N   
155  C CA  . ALA A 20  ? 0.70708 0.53138 0.58851 0.09522  0.03652  0.04530  19   ALA B CA  
156  C C   . ALA A 20  ? 0.71214 0.53937 0.59496 0.08754  0.03590  0.04236  19   ALA B C   
157  O O   . ALA A 20  ? 0.67619 0.48546 0.53969 0.08608  0.03880  0.04248  19   ALA B O   
158  C CB  . ALA A 20  ? 0.66096 0.49405 0.54469 0.10760  0.03005  0.04973  19   ALA B CB  
159  N N   . GLN A 21  ? 0.62648 0.47493 0.53065 0.08313  0.03254  0.03993  20   GLN B N   
160  C CA  . GLN A 21  ? 0.66181 0.51329 0.56709 0.07674  0.03166  0.03724  20   GLN B CA  
161  C C   . GLN A 21  ? 0.64204 0.49872 0.55938 0.06465  0.03596  0.03225  20   GLN B C   
162  O O   . GLN A 21  ? 0.65362 0.50077 0.56253 0.05805  0.03956  0.02987  20   GLN B O   
163  C CB  . GLN A 21  ? 0.65523 0.52608 0.57369 0.08181  0.02343  0.03817  20   GLN B CB  
164  C CG  . GLN A 21  ? 0.69056 0.55704 0.59747 0.09379  0.01796  0.04237  20   GLN B CG  
165  C CD  . GLN A 21  ? 0.75150 0.63571 0.67039 0.09758  0.00929  0.04202  20   GLN B CD  
166  O OE1 . GLN A 21  ? 0.75092 0.65632 0.69281 0.09874  0.00576  0.04159  20   GLN B OE1 
167  N NE2 . GLN A 21  ? 0.82633 0.70111 0.72918 0.09947  0.00601  0.04195  20   GLN B NE2 
168  N N   . CYS A 22  ? 0.60772 0.47683 0.54258 0.06186  0.03639  0.03059  21   CYS B N   
169  C CA  . CYS A 22  ? 0.64785 0.52444 0.59614 0.05142  0.03904  0.02577  21   CYS B CA  
170  C C   . CYS A 22  ? 0.64248 0.50231 0.58137 0.04464  0.04597  0.02281  21   CYS B C   
171  O O   . CYS A 22  ? 0.74622 0.59056 0.67077 0.04810  0.04860  0.02450  21   CYS B O   
172  C CB  . CYS A 22  ? 0.65319 0.54924 0.62326 0.05165  0.03639  0.02511  21   CYS B CB  
173  S SG  . CYS A 22  ? 0.83276 0.74624 0.81413 0.06156  0.02966  0.02926  21   CYS B SG  
174  N N   . SER A 23  ? 0.61658 0.48098 0.56619 0.03495  0.04885  0.01799  22   SER B N   
175  C CA  . SER A 23  ? 0.61812 0.46816 0.56198 0.02763  0.05543  0.01422  22   SER B CA  
176  C C   . SER A 23  ? 0.59128 0.45403 0.55491 0.01882  0.05622  0.00879  22   SER B C   
177  O O   . SER A 23  ? 0.55647 0.43303 0.53219 0.01644  0.05404  0.00782  22   SER B O   
178  C CB  . SER A 23  ? 0.62635 0.45649 0.55073 0.02483  0.06118  0.01432  22   SER B CB  
179  O OG  . SER A 23  ? 0.66834 0.48775 0.59230 0.01525  0.06855  0.00947  22   SER B OG  
180  N N   . ALA A 24  ? 0.58042 0.43919 0.54792 0.01465  0.05861  0.00514  23   ALA B N   
181  C CA  . ALA A 24  ? 0.57425 0.44549 0.56103 0.00715  0.05847  -0.00028 23   ALA B CA  
182  C C   . ALA A 24  ? 0.56187 0.42283 0.54862 0.00085  0.06249  -0.00549 23   ALA B C   
183  O O   . ALA A 24  ? 0.58646 0.43781 0.56430 0.00447  0.06229  -0.00472 23   ALA B O   
184  C CB  . ALA A 24  ? 0.53536 0.42527 0.53728 0.01193  0.05206  0.00093  23   ALA B CB  
185  N N   . GLY A 25  ? 0.55712 0.42155 0.55580 -0.00845 0.06570  -0.01123 24   GLY B N   
186  C CA  . GLY A 25  ? 0.57193 0.42937 0.57488 -0.01528 0.06894  -0.01737 24   GLY B CA  
187  C C   . GLY A 25  ? 0.61260 0.47832 0.63346 -0.02499 0.07162  -0.02393 24   GLY B C   
188  O O   . GLY A 25  ? 0.62896 0.50306 0.65657 -0.02730 0.07259  -0.02366 24   GLY B O   
189  N N   . PRO A 26  ? 0.64331 0.50644 0.67244 -0.03089 0.07291  -0.03037 25   PRO B N   
190  C CA  . PRO A 26  ? 0.67005 0.54193 0.71873 -0.04008 0.07533  -0.03739 25   PRO B CA  
191  C C   . PRO A 26  ? 0.73528 0.59813 0.77971 -0.04672 0.08470  -0.03797 25   PRO B C   
192  O O   . PRO A 26  ? 0.79139 0.63540 0.81748 -0.04708 0.09112  -0.03570 25   PRO B O   
193  C CB  . PRO A 26  ? 0.69789 0.56418 0.75209 -0.04455 0.07535  -0.04408 25   PRO B CB  
194  C CG  . PRO A 26  ? 0.66674 0.52783 0.70801 -0.03596 0.06987  -0.04027 25   PRO B CG  
195  C CD  . PRO A 26  ? 0.61721 0.46964 0.63905 -0.02931 0.07186  -0.03202 25   PRO B CD  
196  N N   . VAL A 27  ? 0.80647 0.68158 0.86697 -0.05176 0.08599  -0.04103 26   VAL B N   
197  C CA  . VAL A 27  ? 0.79890 0.66453 0.85501 -0.05823 0.09577  -0.04191 26   VAL B CA  
198  C C   . VAL A 27  ? 0.80418 0.65811 0.86479 -0.06765 0.10440  -0.04859 26   VAL B C   
199  O O   . VAL A 27  ? 0.87517 0.70992 0.92024 -0.07078 0.11380  -0.04757 26   VAL B O   
200  C CB  . VAL A 27  ? 0.83778 0.71875 0.90771 -0.06014 0.09516  -0.04260 26   VAL B CB  
201  C CG1 . VAL A 27  ? 0.75803 0.64464 0.81745 -0.05116 0.08902  -0.03511 26   VAL B CG1 
202  C CG2 . VAL A 27  ? 0.81774 0.71726 0.91420 -0.06334 0.09029  -0.04889 26   VAL B CG2 
203  N N   . GLY A 28  ? 0.76668 0.63138 0.84854 -0.07227 0.10157  -0.05572 27   GLY B N   
204  C CA  . GLY A 28  ? 0.74098 0.59493 0.82854 -0.08114 0.10904  -0.06266 27   GLY B CA  
205  C C   . GLY A 28  ? 0.73914 0.59747 0.83658 -0.08096 0.10196  -0.06783 27   GLY B C   
206  O O   . GLY A 28  ? 0.72484 0.57572 0.80751 -0.07453 0.09734  -0.06431 27   GLY B O   
207  N N   . ASP A 29  ? 0.77414 0.64512 0.89668 -0.08736 0.10039  -0.07630 28   ASP B N   
208  C CA  . ASP A 29  ? 0.76890 0.64603 0.90259 -0.08696 0.09199  -0.08225 28   ASP B CA  
209  C C   . ASP A 29  ? 0.73759 0.63447 0.88098 -0.07939 0.07934  -0.08114 28   ASP B C   
210  O O   . ASP A 29  ? 0.76246 0.66454 0.91257 -0.07724 0.07087  -0.08539 28   ASP B O   
211  C CB  . ASP A 29  ? 0.76766 0.64785 0.92476 -0.09793 0.09636  -0.09314 28   ASP B CB  
212  C CG  . ASP A 29  ? 0.76091 0.61974 0.90914 -0.10544 0.10782  -0.09578 28   ASP B CG  
213  O OD1 . ASP A 29  ? 0.78703 0.62835 0.90989 -0.10110 0.11056  -0.08940 28   ASP B OD1 
214  O OD2 . ASP A 29  ? 0.76443 0.62378 0.93154 -0.11551 0.11413  -0.10440 28   ASP B OD2 
215  N N   . ASP A 30  ? 0.70403 0.61072 0.84698 -0.07507 0.07798  -0.07552 29   ASP B N   
216  C CA  . ASP A 30  ? 0.70381 0.62807 0.85512 -0.06784 0.06741  -0.07378 29   ASP B CA  
217  C C   . ASP A 30  ? 0.68717 0.60614 0.81775 -0.05769 0.06253  -0.06548 29   ASP B C   
218  O O   . ASP A 30  ? 0.67934 0.59478 0.79689 -0.05404 0.06535  -0.05831 29   ASP B O   
219  C CB  . ASP A 30  ? 0.67549 0.61296 0.83854 -0.06895 0.06904  -0.07256 29   ASP B CB  
220  C CG  . ASP A 30  ? 0.66977 0.62510 0.84427 -0.06255 0.05889  -0.07204 29   ASP B CG  
221  O OD1 . ASP A 30  ? 0.67240 0.63052 0.84918 -0.05874 0.05088  -0.07456 29   ASP B OD1 
222  O OD2 . ASP A 30  ? 0.74827 0.71371 0.92856 -0.06118 0.05904  -0.06929 29   ASP B OD2 
223  N N   . MET A 31  ? 0.68134 0.59965 0.80904 -0.05293 0.05510  -0.06676 30   MET B N   
224  C CA  . MET A 31  ? 0.71757 0.63141 0.82715 -0.04294 0.05075  -0.05925 30   MET B CA  
225  C C   . MET A 31  ? 0.65865 0.58714 0.77210 -0.03589 0.04544  -0.05401 30   MET B C   
226  O O   . MET A 31  ? 0.62762 0.55363 0.72744 -0.02807 0.04381  -0.04679 30   MET B O   
227  C CB  . MET A 31  ? 0.70852 0.61684 0.81338 -0.03965 0.04465  -0.06238 30   MET B CB  
228  C CG  . MET A 31  ? 0.77479 0.66757 0.87515 -0.04644 0.04986  -0.06760 30   MET B CG  
229  S SD  . MET A 31  ? 0.85933 0.73249 0.93443 -0.04464 0.05900  -0.05950 30   MET B SD  
230  C CE  . MET A 31  ? 0.72179 0.59544 0.78036 -0.03099 0.05201  -0.05072 30   MET B CE  
231  N N   . PHE A 32  ? 0.64874 0.59218 0.78096 -0.03843 0.04314  -0.05752 31   PHE B N   
232  C CA  . PHE A 32  ? 0.64270 0.59940 0.77936 -0.03213 0.03859  -0.05298 31   PHE B CA  
233  C C   . PHE A 32  ? 0.63581 0.59569 0.77209 -0.03371 0.04401  -0.04855 31   PHE B C   
234  O O   . PHE A 32  ? 0.58657 0.55727 0.72736 -0.02939 0.04121  -0.04492 31   PHE B O   
235  C CB  . PHE A 32  ? 0.61500 0.58554 0.77092 -0.03276 0.03251  -0.05888 31   PHE B CB  
236  C CG  . PHE A 32  ? 0.60318 0.57220 0.75685 -0.02789 0.02451  -0.06183 31   PHE B CG  
237  C CD1 . PHE A 32  ? 0.63030 0.59237 0.78648 -0.03281 0.02368  -0.06920 31   PHE B CD1 
238  C CD2 . PHE A 32  ? 0.60662 0.58060 0.75575 -0.01854 0.01803  -0.05767 31   PHE B CD2 
239  C CE1 . PHE A 32  ? 0.63520 0.59522 0.78833 -0.02820 0.01559  -0.07252 31   PHE B CE1 
240  C CE2 . PHE A 32  ? 0.62679 0.59774 0.77161 -0.01354 0.01065  -0.06049 31   PHE B CE2 
241  C CZ  . PHE A 32  ? 0.63412 0.59817 0.78057 -0.01826 0.00895  -0.06802 31   PHE B CZ  
242  N N   . HIS A 33  ? 0.64003 0.64273 0.73007 0.03762  0.05095  -0.08595 32   HIS B N   
243  C CA  . HIS A 33  ? 0.64066 0.63166 0.72631 0.03608  0.05443  -0.08086 32   HIS B CA  
244  C C   . HIS A 33  ? 0.65457 0.63445 0.72640 0.02273  0.07192  -0.07191 32   HIS B C   
245  O O   . HIS A 33  ? 0.65396 0.64367 0.72793 0.01292  0.08672  -0.08263 32   HIS B O   
246  C CB  . HIS A 33  ? 0.64545 0.65354 0.75022 0.03902  0.05432  -0.10160 32   HIS B CB  
247  C CG  . HIS A 33  ? 0.72870 0.72374 0.82671 0.03608  0.05894  -0.09741 32   HIS B CG  
248  N ND1 . HIS A 33  ? 0.74772 0.75123 0.85261 0.02824  0.07189  -0.11323 32   HIS B ND1 
249  C CD2 . HIS A 33  ? 0.70464 0.67771 0.78855 0.03900  0.05285  -0.08014 32   HIS B CD2 
250  C CE1 . HIS A 33  ? 0.74196 0.72773 0.83494 0.02691  0.07254  -0.10463 32   HIS B CE1 
251  N NE2 . HIS A 33  ? 0.70603 0.67481 0.78803 0.03392  0.06050  -0.08493 32   HIS B NE2 
252  N N   . TRP A 34  ? 0.61637 0.57445 0.67364 0.02249  0.06980  -0.05339 33   TRP B N   
253  C CA  . TRP A 34  ? 0.61180 0.55541 0.65528 0.01290  0.08169  -0.04372 33   TRP B CA  
254  C C   . TRP A 34  ? 0.61032 0.53930 0.64645 0.01301  0.08061  -0.03947 33   TRP B C   
255  O O   . TRP A 34  ? 0.62464 0.55125 0.66508 0.02071  0.06990  -0.03851 33   TRP B O   
256  C CB  . TRP A 34  ? 0.58882 0.51970 0.62413 0.01200  0.08020  -0.02728 33   TRP B CB  
257  C CG  . TRP A 34  ? 0.57435 0.51377 0.61069 0.00815  0.08529  -0.02851 33   TRP B CG  
258  C CD1 . TRP A 34  ? 0.57481 0.53354 0.62017 0.00776  0.08721  -0.04244 33   TRP B CD1 
259  C CD2 . TRP A 34  ? 0.58445 0.51392 0.61391 0.00371  0.08937  -0.01662 33   TRP B CD2 
260  N NE1 . TRP A 34  ? 0.59633 0.55659 0.63836 0.00325  0.09193  -0.03880 33   TRP B NE1 
261  C CE2 . TRP A 34  ? 0.58816 0.53019 0.62019 0.00046  0.09387  -0.02282 33   TRP B CE2 
262  C CE3 . TRP A 34  ? 0.58460 0.49705 0.60845 0.00216  0.08959  -0.00309 33   TRP B CE3 
263  C CZ2 . TRP A 34  ? 0.60777 0.54420 0.63454 -0.00503 0.09968  -0.01487 33   TRP B CZ2 
264  C CZ3 . TRP A 34  ? 0.60529 0.51371 0.62697 -0.00302 0.09545  0.00342  33   TRP B CZ3 
265  C CH2 . TRP A 34  ? 0.60799 0.52755 0.62995 -0.00687 0.10090  -0.00192 33   TRP B CH2 
266  N N   . GLN A 35  ? 0.62531 0.54132 0.64756 0.00457  0.09101  -0.03613 34   GLN B N   
267  C CA  . GLN A 35  ? 0.63212 0.52826 0.64211 0.00439  0.08843  -0.02827 34   GLN B CA  
268  C C   . GLN A 35  ? 0.59671 0.47751 0.59909 0.00389  0.08651  -0.01308 34   GLN B C   
269  O O   . GLN A 35  ? 0.53173 0.41334 0.53181 -0.00066 0.09354  -0.01101 34   GLN B O   
270  C CB  . GLN A 35  ? 0.65956 0.54684 0.65474 -0.00461 0.10022  -0.03760 34   GLN B CB  
271  C CG  . GLN A 35  ? 0.68265 0.54347 0.65805 -0.00581 0.09734  -0.02806 34   GLN B CG  
272  C CD  . GLN A 35  ? 0.77311 0.61891 0.72700 -0.01556 0.10876  -0.03752 34   GLN B CD  
273  O OE1 . GLN A 35  ? 0.81970 0.65399 0.75595 -0.02458 0.12063  -0.03988 34   GLN B OE1 
274  N NE2 . GLN A 35  ? 0.80286 0.64558 0.75529 -0.01472 0.10610  -0.04310 34   GLN B NE2 
275  N N   . ALA A 36  ? 0.58599 0.45432 0.58714 0.00862  0.07701  -0.00399 35   ALA B N   
276  C CA  . ALA A 36  ? 0.58583 0.44103 0.58445 0.00871  0.07423  0.00732  35   ALA B CA  
277  C C   . ALA A 36  ? 0.56475 0.40133 0.55185 0.00957  0.06905  0.01038  35   ALA B C   
278  O O   . ALA A 36  ? 0.62661 0.46060 0.60906 0.01071  0.06634  0.00590  35   ALA B O   
279  C CB  . ALA A 36  ? 0.56149 0.42047 0.57355 0.01337  0.06696  0.01442  35   ALA B CB  
280  N N   . THR A 37  ? 0.56290 0.38607 0.54558 0.00931  0.06706  0.01709  36   THR B N   
281  C CA  . THR A 37  ? 0.60345 0.40584 0.57372 0.01127  0.05946  0.02032  36   THR B CA  
282  C C   . THR A 37  ? 0.61275 0.41302 0.59835 0.01595  0.05089  0.02694  36   THR B C   
283  O O   . THR A 37  ? 0.64414 0.45031 0.63973 0.01455  0.05521  0.02905  36   THR B O   
284  C CB  . THR A 37  ? 0.69024 0.47302 0.63425 0.00573  0.06611  0.01840  36   THR B CB  
285  O OG1 . THR A 37  ? 0.69531 0.47446 0.62264 0.00024  0.07342  0.01021  36   THR B OG1 
286  C CG2 . THR A 37  ? 0.70464 0.46262 0.63646 0.00981  0.05509  0.02390  36   THR B CG2 
287  N N   . ILE A 38  ? 0.62323 0.41643 0.61261 0.02080  0.03963  0.02857  37   ILE B N   
288  C CA  . ILE A 38  ? 0.63497 0.42707 0.64221 0.02496  0.03108  0.03143  37   ILE B CA  
289  C C   . ILE A 38  ? 0.66107 0.43307 0.65668 0.02947  0.01870  0.03148  37   ILE B C   
290  O O   . ILE A 38  ? 0.65192 0.41538 0.63372 0.03027  0.01402  0.03024  37   ILE B O   
291  C CB  . ILE A 38  ? 0.65552 0.46056 0.68257 0.02628  0.02891  0.03154  37   ILE B CB  
292  C CG1 . ILE A 38  ? 0.63316 0.45197 0.67000 0.02249  0.03856  0.03232  37   ILE B CG1 
293  C CG2 . ILE A 38  ? 0.67081 0.47307 0.71537 0.02978  0.01942  0.03109  37   ILE B CG2 
294  C CD1 . ILE A 38  ? 0.61576 0.43999 0.66254 0.02303  0.03700  0.03263  37   ILE B CD1 
295  N N   . MET A 39  ? 0.68002 0.44387 0.68172 0.03292  0.01229  0.03210  38   MET B N   
296  C CA  . MET A 39  ? 0.70342 0.44720 0.69648 0.03947  -0.00357 0.03135  38   MET B CA  
297  C C   . MET A 39  ? 0.74794 0.50352 0.77115 0.04405  -0.01341 0.02838  38   MET B C   
298  O O   . MET A 39  ? 0.72262 0.49643 0.77417 0.04233  -0.00801 0.02667  38   MET B O   
299  C CB  . MET A 39  ? 0.73527 0.46166 0.71968 0.04295  -0.00864 0.03178  38   MET B CB  
300  C CG  . MET A 39  ? 0.74868 0.46202 0.70406 0.03702  0.00333  0.03394  38   MET B CG  
301  S SD  . MET A 39  ? 0.80338 0.49245 0.74669 0.04174  -0.00286 0.03478  38   MET B SD  
302  C CE  . MET A 39  ? 0.80715 0.46014 0.72458 0.05156  -0.02670 0.03444  38   MET B CE  
303  N N   . GLY A 40  ? 0.74689 0.49080 0.76229 0.04855  -0.02657 0.02684  39   GLY B N   
304  C CA  . GLY A 40  ? 0.74164 0.49573 0.78483 0.05242  -0.03626 0.02222  39   GLY B CA  
305  C C   . GLY A 40  ? 0.74639 0.50861 0.82042 0.05623  -0.04134 0.01694  39   GLY B C   
306  O O   . GLY A 40  ? 0.76668 0.51479 0.83451 0.06202  -0.05079 0.01585  39   GLY B O   
307  N N   . PRO A 41  ? 0.70277 0.48610 0.80908 0.05232  -0.03381 0.01284  40   PRO B N   
308  C CA  . PRO A 41  ? 0.70902 0.50294 0.84936 0.05388  -0.03539 0.00499  40   PRO B CA  
309  C C   . PRO A 41  ? 0.74695 0.53285 0.89922 0.06428  -0.05675 -0.00303 40   PRO B C   
310  O O   . PRO A 41  ? 0.74986 0.53129 0.89941 0.06779  -0.06819 -0.00542 40   PRO B O   
311  C CB  . PRO A 41  ? 0.68718 0.49982 0.85327 0.04587  -0.02339 0.00080  40   PRO B CB  
312  C CG  . PRO A 41  ? 0.67089 0.48230 0.81185 0.04004  -0.01185 0.00981  40   PRO B CG  
313  C CD  . PRO A 41  ? 0.70896 0.50479 0.81871 0.04513  -0.02126 0.01492  40   PRO B CD  
314  N N   . ASN A 42  ? 0.73064 0.51467 0.89735 0.06980  -0.06305 -0.00813 41   ASN B N   
315  C CA  . ASN A 42  ? 0.81462 0.58487 0.98520 0.08260  -0.08732 -0.01515 41   ASN B CA  
316  C C   . ASN A 42  ? 0.82912 0.61382 1.03532 0.08602  -0.09882 -0.02806 41   ASN B C   
317  O O   . ASN A 42  ? 0.86335 0.63396 1.06164 0.09586  -0.12051 -0.03165 41   ASN B O   
318  C CB  . ASN A 42  ? 0.84891 0.61697 1.03461 0.08844  -0.09149 -0.02017 41   ASN B CB  
319  C CG  . ASN A 42  ? 0.89579 0.64248 1.04119 0.08725  -0.08491 -0.00860 41   ASN B CG  
320  O OD1 . ASN A 42  ? 0.89799 0.62064 0.99902 0.08750  -0.08805 0.00046  41   ASN B OD1 
321  N ND2 . ASN A 42  ? 0.98562 0.74070 1.14644 0.08455  -0.07398 -0.01008 41   ASN B ND2 
322  N N   . ASP A 43  ? 0.80758 0.61804 1.05121 0.07749  -0.08471 -0.03611 42   ASP B N   
323  C CA  . ASP A 43  ? 0.84168 0.66712 1.12129 0.07855  -0.09264 -0.05061 42   ASP B CA  
324  C C   . ASP A 43  ? 0.81941 0.64620 1.08593 0.07151  -0.08607 -0.04605 42   ASP B C   
325  O O   . ASP A 43  ? 0.89192 0.73371 1.18863 0.06754  -0.08448 -0.05766 42   ASP B O   
326  C CB  . ASP A 43  ? 0.87945 0.72970 1.20973 0.07237  -0.08123 -0.06613 42   ASP B CB  
327  C CG  . ASP A 43  ? 0.97930 0.84401 1.35338 0.07764  -0.09597 -0.08660 42   ASP B CG  
328  O OD1 . ASP A 43  ? 1.04368 0.89830 1.40615 0.08663  -0.11609 -0.08711 42   ASP B OD1 
329  O OD2 . ASP A 43  ? 0.93620 0.82206 1.35644 0.07245  -0.08742 -0.10345 42   ASP B OD2 
330  N N   . SER A 44  ? 0.77736 0.58962 1.00170 0.06895  -0.08049 -0.03094 43   SER B N   
331  C CA  . SER A 44  ? 0.74070 0.55354 0.95223 0.06283  -0.07371 -0.02655 43   SER B CA  
332  C C   . SER A 44  ? 0.73241 0.52629 0.91476 0.07027  -0.09094 -0.02263 43   SER B C   
333  O O   . SER A 44  ? 0.73287 0.50919 0.89725 0.07896  -0.10605 -0.02106 43   SER B O   
334  C CB  . SER A 44  ? 0.70983 0.52212 0.89815 0.05399  -0.05370 -0.01450 43   SER B CB  
335  O OG  . SER A 44  ? 0.70172 0.49807 0.85453 0.05727  -0.05576 -0.00426 43   SER B OG  
336  N N   . PRO A 45  ? 0.72949 0.52313 0.90364 0.06677  -0.08927 -0.02128 44   PRO B N   
337  C CA  . PRO A 45  ? 0.73775 0.51122 0.87920 0.07184  -0.10293 -0.01690 44   PRO B CA  
338  C C   . PRO A 45  ? 0.73917 0.49585 0.83804 0.06945  -0.09523 -0.00437 44   PRO B C   
339  O O   . PRO A 45  ? 0.74974 0.48595 0.81662 0.07190  -0.10417 -0.00101 44   PRO B O   
340  C CB  . PRO A 45  ? 0.73190 0.51356 0.88237 0.06710  -0.09963 -0.02034 44   PRO B CB  
341  C CG  . PRO A 45  ? 0.71086 0.50968 0.88009 0.05758  -0.07855 -0.02001 44   PRO B CG  
342  C CD  . PRO A 45  ? 0.68456 0.49380 0.87975 0.05804  -0.07613 -0.02566 44   PRO B CD  
343  N N   . TYR A 46  ? 0.70710 0.47104 0.80428 0.06404  -0.07861 0.00124  45   TYR B N   
344  C CA  . TYR A 46  ? 0.71629 0.46712 0.77753 0.06119  -0.07034 0.01025  45   TYR B CA  
345  C C   . TYR A 46  ? 0.72942 0.46330 0.77293 0.06534  -0.07613 0.01240  45   TYR B C   
346  O O   . TYR A 46  ? 0.73391 0.45559 0.74710 0.06168  -0.06770 0.01835  45   TYR B O   
347  C CB  . TYR A 46  ? 0.66733 0.43412 0.73414 0.05355  -0.05047 0.01432  45   TYR B CB  
348  C CG  . TYR A 46  ? 0.67640 0.45597 0.75994 0.04991  -0.04515 0.01207  45   TYR B CG  
349  C CD1 . TYR A 46  ? 0.65164 0.42576 0.71928 0.04914  -0.04578 0.01352  45   TYR B CD1 
350  C CD2 . TYR A 46  ? 0.65821 0.45257 0.77147 0.04641  -0.03861 0.00771  45   TYR B CD2 
351  C CE1 . TYR A 46  ? 0.63057 0.41279 0.71076 0.04622  -0.04130 0.01162  45   TYR B CE1 
352  C CE2 . TYR A 46  ? 0.61785 0.41813 0.74072 0.04207  -0.03286 0.00569  45   TYR B CE2 
353  C CZ  . TYR A 46  ? 0.62572 0.41950 0.73173 0.04261  -0.03490 0.00809  45   TYR B CZ  
354  O OH  . TYR A 46  ? 0.62601 0.42248 0.73921 0.03860  -0.02939 0.00622  45   TYR B OH  
355  N N   . GLN A 47  ? 0.75147 0.48388 0.81387 0.07281  -0.09008 0.00636  46   GLN B N   
356  C CA  . GLN A 47  ? 0.78164 0.49546 0.82762 0.07798  -0.09684 0.00806  46   GLN B CA  
357  C C   . GLN A 47  ? 0.81500 0.49371 0.80970 0.07936  -0.10447 0.01365  46   GLN B C   
358  O O   . GLN A 47  ? 0.78782 0.45133 0.76761 0.08304  -0.11865 0.01186  46   GLN B O   
359  C CB  . GLN A 47  ? 0.82395 0.54089 0.90095 0.08814  -0.11491 -0.00183 46   GLN B CB  
360  C CG  . GLN A 47  ? 0.94948 0.63712 1.00158 0.09717  -0.12986 -0.00063 46   GLN B CG  
361  C CD  . GLN A 47  ? 1.04180 0.72769 1.12070 0.11062  -0.15516 -0.01242 46   GLN B CD  
362  O OE1 . GLN A 47  ? 1.14514 0.80419 1.19987 0.11975  -0.17754 -0.01375 46   GLN B OE1 
363  N NE2 . GLN A 47  ? 1.00939 0.72325 1.13860 0.11174  -0.15198 -0.02242 46   GLN B NE2 
364  N N   . GLY A 48  ? 0.80563 0.46947 0.77173 0.07542  -0.09438 0.01956  47   GLY B N   
365  C CA  . GLY A 48  ? 0.84170 0.46965 0.75491 0.07305  -0.09593 0.02412  47   GLY B CA  
366  C C   . GLY A 48  ? 0.82369 0.45608 0.71758 0.06120  -0.07509 0.02749  47   GLY B C   
367  O O   . GLY A 48  ? 0.87426 0.47914 0.72520 0.05565  -0.06926 0.02989  47   GLY B O   
368  N N   . GLY A 49  ? 0.74259 0.40736 0.66664 0.05700  -0.06351 0.02650  48   GLY B N   
369  C CA  . GLY A 49  ? 0.73852 0.41000 0.64965 0.04785  -0.04644 0.02746  48   GLY B CA  
370  C C   . GLY A 49  ? 0.70601 0.39281 0.62340 0.04199  -0.02852 0.02889  48   GLY B C   
371  O O   . GLY A 49  ? 0.75219 0.45229 0.69272 0.04425  -0.02722 0.02970  48   GLY B O   
372  N N   . VAL A 50  ? 0.68588 0.37016 0.58229 0.03392  -0.01443 0.02770  49   VAL B N   
373  C CA  . VAL A 50  ? 0.66762 0.36962 0.57119 0.02788  0.00280  0.02694  49   VAL B CA  
374  C C   . VAL A 50  ? 0.65330 0.37745 0.57088 0.02502  0.01083  0.02342  49   VAL B C   
375  O O   . VAL A 50  ? 0.66632 0.38219 0.56870 0.02246  0.01124  0.01985  49   VAL B O   
376  C CB  . VAL A 50  ? 0.65018 0.33028 0.51851 0.02051  0.01332  0.02553  49   VAL B CB  
377  C CG1 . VAL A 50  ? 0.66043 0.36237 0.54157 0.01492  0.02994  0.02354  49   VAL B CG1 
378  C CG2 . VAL A 50  ? 0.67659 0.32712 0.52460 0.02486  0.00233  0.02928  49   VAL B CG2 
379  N N   . PHE A 51  ? 0.61842 0.36825 0.56431 0.02609  0.01565  0.02414  50   PHE B N   
380  C CA  . PHE A 51  ? 0.61110 0.38032 0.57157 0.02580  0.02022  0.02122  50   PHE B CA  
381  C C   . PHE A 51  ? 0.60254 0.38709 0.56675 0.02169  0.03309  0.01807  50   PHE B C   
382  O O   . PHE A 51  ? 0.61066 0.40150 0.58314 0.02109  0.03668  0.02094  50   PHE B O   
383  C CB  . PHE A 51  ? 0.54128 0.32182 0.52744 0.03082  0.01278  0.02438  50   PHE B CB  
384  C CG  . PHE A 51  ? 0.56382 0.33224 0.55087 0.03484  -0.00022 0.02544  50   PHE B CG  
385  C CD1 . PHE A 51  ? 0.55560 0.31666 0.54793 0.03774  -0.00777 0.02712  50   PHE B CD1 
386  C CD2 . PHE A 51  ? 0.55267 0.31724 0.53634 0.03620  -0.00578 0.02339  50   PHE B CD2 
387  C CE1 . PHE A 51  ? 0.58313 0.33397 0.57821 0.04255  -0.02199 0.02596  50   PHE B CE1 
388  C CE2 . PHE A 51  ? 0.57438 0.32822 0.55898 0.03987  -0.01863 0.02327  50   PHE B CE2 
389  C CZ  . PHE A 51  ? 0.64296 0.39029 0.63365 0.04336  -0.02742 0.02415  50   PHE B CZ  
390  N N   . PHE A 52  ? 0.59712 0.38853 0.55712 0.01890  0.03974  0.01080  51   PHE B N   
391  C CA  . PHE A 52  ? 0.60654 0.41522 0.57333 0.01587  0.05027  0.00478  51   PHE B CA  
392  C C   . PHE A 52  ? 0.60062 0.42753 0.58875 0.02171  0.04596  0.00436  51   PHE B C   
393  O O   . PHE A 52  ? 0.53309 0.35832 0.52643 0.02623  0.03813  0.00560  51   PHE B O   
394  C CB  . PHE A 52  ? 0.64545 0.45196 0.59768 0.00896  0.06072  -0.00664 51   PHE B CB  
395  C CG  . PHE A 52  ? 0.63856 0.42169 0.56218 0.00113  0.06768  -0.00704 51   PHE B CG  
396  C CD1 . PHE A 52  ? 0.68192 0.43835 0.58255 0.00050  0.06134  -0.00363 51   PHE B CD1 
397  C CD2 . PHE A 52  ? 0.69891 0.48385 0.61569 -0.00571 0.08011  -0.01123 51   PHE B CD2 
398  C CE1 . PHE A 52  ? 0.74546 0.47373 0.61336 -0.00628 0.06628  -0.00355 51   PHE B CE1 
399  C CE2 . PHE A 52  ? 0.75294 0.51083 0.63823 -0.01343 0.08701  -0.01137 51   PHE B CE2 
400  C CZ  . PHE A 52  ? 0.73895 0.46646 0.59784 -0.01349 0.07962  -0.00717 51   PHE B CZ  
401  N N   . LEU A 53  ? 0.59327 0.43471 0.59104 0.02159  0.05056  0.00276  52   LEU B N   
402  C CA  . LEU A 53  ? 0.57223 0.42571 0.58404 0.02737  0.04546  0.00236  52   LEU B CA  
403  C C   . LEU A 53  ? 0.53914 0.40913 0.55606 0.02652  0.05139  -0.00780 52   LEU B C   
404  O O   . LEU A 53  ? 0.56627 0.43957 0.57840 0.02025  0.06105  -0.01172 52   LEU B O   
405  C CB  . LEU A 53  ? 0.55338 0.40414 0.57140 0.02871  0.04216  0.01215  52   LEU B CB  
406  C CG  . LEU A 53  ? 0.52178 0.36011 0.54156 0.02914  0.03680  0.01991  52   LEU B CG  
407  C CD1 . LEU A 53  ? 0.56447 0.39585 0.57960 0.02521  0.04018  0.02259  52   LEU B CD1 
408  C CD2 . LEU A 53  ? 0.56598 0.40326 0.59390 0.03011  0.03458  0.02508  52   LEU B CD2 
409  N N   . THR A 54  ? 0.55735 0.43676 0.58399 0.03320  0.04490  -0.01294 53   THR B N   
410  C CA  . THR A 54  ? 0.56582 0.46250 0.60131 0.03480  0.04664  -0.02321 53   THR B CA  
411  C C   . THR A 54  ? 0.58203 0.47736 0.61882 0.03966  0.03935  -0.01585 53   THR B C   
412  O O   . THR A 54  ? 0.57958 0.46237 0.61298 0.04415  0.03110  -0.00741 53   THR B O   
413  C CB  . THR A 54  ? 0.54814 0.45645 0.59438 0.04014  0.04284  -0.03769 53   THR B CB  
414  O OG1 . THR A 54  ? 0.58899 0.48973 0.63707 0.04959  0.02972  -0.03287 53   THR B OG1 
415  C CG2 . THR A 54  ? 0.61035 0.51576 0.65178 0.03342  0.05159  -0.04527 53   THR B CG2 
416  N N   . ILE A 55  ? 0.56730 0.47338 0.60662 0.03753  0.04346  -0.01971 54   ILE B N   
417  C CA  . ILE A 55  ? 0.58248 0.48567 0.61897 0.04069  0.03761  -0.01428 54   ILE B CA  
418  C C   . ILE A 55  ? 0.57197 0.49154 0.61729 0.04681  0.03179  -0.02790 54   ILE B C   
419  O O   . ILE A 55  ? 0.58766 0.52513 0.64310 0.04344  0.03922  -0.04105 54   ILE B O   
420  C CB  . ILE A 55  ? 0.57061 0.47070 0.60175 0.03213  0.04738  -0.00645 54   ILE B CB  
421  C CG1 . ILE A 55  ? 0.53151 0.41711 0.55827 0.02769  0.05101  0.00434  54   ILE B CG1 
422  C CG2 . ILE A 55  ? 0.57337 0.46926 0.59881 0.03367  0.04288  -0.00232 54   ILE B CG2 
423  C CD1 . ILE A 55  ? 0.57590 0.45931 0.60058 0.01994  0.06068  0.00983  54   ILE B CD1 
424  N N   . HIS A 56  ? 0.60167 0.51351 0.64251 0.05583  0.01811  -0.02624 55   HIS B N   
425  C CA  . HIS A 56  ? 0.64274 0.56790 0.69145 0.06414  0.00817  -0.03940 55   HIS B CA  
426  C C   . HIS A 56  ? 0.62532 0.53551 0.65734 0.06609  0.00072  -0.03083 55   HIS B C   
427  O O   . HIS A 56  ? 0.57672 0.46210 0.59145 0.06932  -0.00705 -0.01972 55   HIS B O   
428  C CB  . HIS A 56  ? 0.65581 0.58324 0.71362 0.07632  -0.00541 -0.04947 55   HIS B CB  
429  C CG  . HIS A 56  ? 0.71226 0.66201 0.78823 0.08460  -0.01386 -0.06944 55   HIS B CG  
430  N ND1 . HIS A 56  ? 0.84887 0.79913 0.92052 0.09039  -0.02451 -0.07220 55   HIS B ND1 
431  C CD2 . HIS A 56  ? 0.78120 0.75452 0.88136 0.08740  -0.01275 -0.08964 55   HIS B CD2 
432  C CE1 . HIS A 56  ? 0.77127 0.74609 0.86594 0.09788  -0.03153 -0.09369 55   HIS B CE1 
433  N NE2 . HIS A 56  ? 0.82810 0.81825 0.94193 0.09576  -0.02359 -0.10533 55   HIS B NE2 
434  N N   . PHE A 57  ? 0.64303 0.56635 0.67805 0.06297  0.00403  -0.03678 56   PHE B N   
435  C CA  . PHE A 57  ? 0.65216 0.56018 0.66855 0.06309  -0.00174 -0.02940 56   PHE B CA  
436  C C   . PHE A 57  ? 0.66748 0.57376 0.68109 0.07733  -0.02273 -0.03918 56   PHE B C   
437  O O   . PHE A 57  ? 0.66503 0.59710 0.69990 0.08315  -0.02745 -0.05708 56   PHE B O   
438  C CB  . PHE A 57  ? 0.61524 0.53635 0.63448 0.05260  0.01162  -0.03068 56   PHE B CB  
439  C CG  . PHE A 57  ? 0.60437 0.52210 0.62265 0.03981  0.02987  -0.02020 56   PHE B CG  
440  C CD1 . PHE A 57  ? 0.55963 0.45480 0.56212 0.03399  0.03383  -0.00514 56   PHE B CD1 
441  C CD2 . PHE A 57  ? 0.59892 0.53439 0.63130 0.03332  0.04311  -0.02693 56   PHE B CD2 
442  C CE1 . PHE A 57  ? 0.52633 0.41981 0.53172 0.02400  0.04840  0.00231  56   PHE B CE1 
443  C CE2 . PHE A 57  ? 0.57158 0.50033 0.60071 0.02352  0.05688  -0.01756 56   PHE B CE2 
444  C CZ  . PHE A 57  ? 0.55186 0.46126 0.56978 0.01985  0.05841  -0.00333 56   PHE B CZ  
445  N N   . PRO A 58  ? 0.69246 0.56735 0.67965 0.08300  -0.03569 -0.02924 57   PRO B N   
446  C CA  . PRO A 58  ? 0.71752 0.58395 0.69550 0.09779  -0.05871 -0.03755 57   PRO B CA  
447  C C   . PRO A 58  ? 0.73101 0.60830 0.70795 0.09670  -0.06125 -0.04459 57   PRO B C   
448  O O   . PRO A 58  ? 0.74065 0.61981 0.71240 0.08340  -0.04561 -0.03772 57   PRO B O   
449  C CB  . PRO A 58  ? 0.71905 0.54024 0.65934 0.09960  -0.06726 -0.02178 57   PRO B CB  
450  C CG  . PRO A 58  ? 0.73296 0.54347 0.66381 0.08241  -0.04593 -0.00658 57   PRO B CG  
451  C CD  . PRO A 58  ? 0.71141 0.55463 0.67481 0.07600  -0.03002 -0.01129 57   PRO B CD  
452  N N   . THR A 59  ? 0.74566 0.62784 0.72643 0.11178  -0.08300 -0.05874 58   THR B N   
453  C CA  . THR A 59  ? 0.78432 0.68118 0.76851 0.11242  -0.08793 -0.06916 58   THR B CA  
454  C C   . THR A 59  ? 0.83194 0.69624 0.77722 0.10444  -0.08659 -0.05337 58   THR B C   
455  O O   . THR A 59  ? 0.81298 0.68975 0.75980 0.09831  -0.08171 -0.05772 58   THR B O   
456  C CB  . THR A 59  ? 0.81043 0.71587 0.80587 0.13249  -0.11562 -0.08847 58   THR B CB  
457  O OG1 . THR A 59  ? 0.86272 0.72313 0.81865 0.14381  -0.13791 -0.07815 58   THR B OG1 
458  C CG2 . THR A 59  ? 0.79931 0.73298 0.83228 0.14012  -0.11655 -0.10465 58   THR B CG2 
459  N N   . ASP A 60  ? 0.84888 0.67046 0.75824 0.10347  -0.09001 -0.03640 59   ASP B N   
460  C CA  . ASP A 60  ? 0.87692 0.66357 0.74657 0.09331  -0.08580 -0.02214 59   ASP B CA  
461  C C   . ASP A 60  ? 0.85389 0.62829 0.71655 0.07555  -0.06088 -0.00595 59   ASP B C   
462  O O   . ASP A 60  ? 0.89833 0.63296 0.72492 0.06838  -0.05812 0.00712  59   ASP B O   
463  C CB  . ASP A 60  ? 0.94251 0.68287 0.76909 0.10521  -0.11056 -0.01800 59   ASP B CB  
464  C CG  . ASP A 60  ? 1.03117 0.74645 0.84647 0.11170  -0.11668 -0.01127 59   ASP B CG  
465  O OD1 . ASP A 60  ? 1.02980 0.77286 0.87953 0.11591  -0.11304 -0.01756 59   ASP B OD1 
466  O OD2 . ASP A 60  ? 1.12077 0.78575 0.89008 0.11215  -0.12501 -0.00020 59   ASP B OD2 
467  N N   . TYR A 61  ? 0.79090 0.59776 0.68754 0.06855  -0.04318 -0.00822 60   TYR B N   
468  C CA  . TYR A 61  ? 0.76035 0.56365 0.65782 0.05227  -0.02011 0.00357  60   TYR B CA  
469  C C   . TYR A 61  ? 0.76781 0.56542 0.65115 0.04036  -0.00982 0.00735  60   TYR B C   
470  O O   . TYR A 61  ? 0.77208 0.58421 0.65867 0.04365  -0.01621 -0.00185 60   TYR B O   
471  C CB  . TYR A 61  ? 0.70145 0.54034 0.63593 0.04979  -0.00750 -0.00230 60   TYR B CB  
472  C CG  . TYR A 61  ? 0.67073 0.51104 0.61243 0.03599  0.01344  0.00699  60   TYR B CG  
473  C CD1 . TYR A 61  ? 0.66827 0.49078 0.60487 0.03346  0.01694  0.01623  60   TYR B CD1 
474  C CD2 . TYR A 61  ? 0.66431 0.52508 0.62035 0.02636  0.02892  0.00481  60   TYR B CD2 
475  C CE1 . TYR A 61  ? 0.64543 0.47074 0.59213 0.02263  0.03345  0.02249  60   TYR B CE1 
476  C CE2 . TYR A 61  ? 0.64221 0.50303 0.60574 0.01580  0.04550  0.01227  60   TYR B CE2 
477  C CZ  . TYR A 61  ? 0.64685 0.49075 0.60693 0.01457  0.04678  0.02060  60   TYR B CZ  
478  O OH  . TYR A 61  ? 0.60198 0.44666 0.57224 0.00577  0.06054  0.02604  60   TYR B OH  
479  N N   . PRO A 62  ? 0.76124 0.53675 0.62842 0.02632  0.00560  0.01937  61   PRO B N   
480  C CA  . PRO A 62  ? 0.75657 0.51425 0.62025 0.01981  0.01525  0.02893  61   PRO B CA  
481  C C   . PRO A 62  ? 0.82853 0.54081 0.65273 0.01972  0.00735  0.03629  61   PRO B C   
482  O O   . PRO A 62  ? 0.82143 0.51380 0.63763 0.01082  0.01796  0.04346  61   PRO B O   
483  C CB  . PRO A 62  ? 0.74946 0.51360 0.62222 0.00354  0.03761  0.03335  61   PRO B CB  
484  C CG  . PRO A 62  ? 0.79503 0.55164 0.64822 -0.00106 0.03720  0.03194  61   PRO B CG  
485  C CD  . PRO A 62  ? 0.78804 0.56015 0.64455 0.01385  0.01750  0.02171  61   PRO B CD  
486  N N   . PHE A 63  ? 0.86248 0.55518 0.65948 0.02933  -0.01168 0.03367  62   PHE B N   
487  C CA  . PHE A 63  ? 0.92569 0.56826 0.67814 0.03005  -0.02081 0.04074  62   PHE B CA  
488  C C   . PHE A 63  ? 0.94463 0.58191 0.70285 0.04023  -0.02972 0.04113  62   PHE B C   
489  O O   . PHE A 63  ? 1.04675 0.64318 0.77283 0.03693  -0.03024 0.04825  62   PHE B O   
490  C CB  . PHE A 63  ? 0.96663 0.58632 0.68519 0.03892  -0.04137 0.03765  62   PHE B CB  
491  C CG  . PHE A 63  ? 0.99728 0.62397 0.71125 0.02820  -0.03189 0.03668  62   PHE B CG  
492  C CD1 . PHE A 63  ? 1.04639 0.64078 0.72937 0.00959  -0.01482 0.04528  62   PHE B CD1 
493  C CD2 . PHE A 63  ? 1.01981 0.68684 0.76287 0.03501  -0.03741 0.02584  62   PHE B CD2 
494  C CE1 . PHE A 63  ? 1.06419 0.66567 0.74412 -0.00083 -0.00506 0.04398  62   PHE B CE1 
495  C CE2 . PHE A 63  ? 1.06418 0.73842 0.80383 0.02464  -0.02778 0.02464  62   PHE B CE2 
496  C CZ  . PHE A 63  ? 1.07764 0.71887 0.78540 0.00708  -0.01204 0.03426  62   PHE B CZ  
497  N N   . LYS A 64  ? 0.90009 0.57635 0.69745 0.05079  -0.03464 0.03309  63   LYS B N   
498  C CA  . LYS A 64  ? 0.89514 0.57077 0.70283 0.05820  -0.03936 0.03320  63   LYS B CA  
499  C C   . LYS A 64  ? 0.81047 0.52137 0.65809 0.05172  -0.02254 0.03226  63   LYS B C   
500  O O   . LYS A 64  ? 0.76845 0.51241 0.64177 0.04857  -0.01442 0.02710  63   LYS B O   
501  C CB  . LYS A 64  ? 0.96375 0.64652 0.77651 0.07879  -0.06430 0.02283  63   LYS B CB  
502  C CG  . LYS A 64  ? 1.09142 0.72606 0.85696 0.08776  -0.08487 0.02585  63   LYS B CG  
503  C CD  . LYS A 64  ? 1.25180 0.89098 1.02292 0.11040  -0.11271 0.01413  63   LYS B CD  
504  C CE  . LYS A 64  ? 1.25936 0.89835 1.04278 0.11982  -0.11872 0.01235  63   LYS B CE  
505  N NZ  . LYS A 64  ? 1.18332 0.82103 0.96848 0.14290  -0.14813 -0.00023 63   LYS B NZ  
506  N N   . PRO A 65  ? 0.78700 0.48875 0.63760 0.04855  -0.01649 0.03719  64   PRO B N   
507  C CA  . PRO A 65  ? 0.73099 0.46200 0.61582 0.04194  -0.00148 0.03681  64   PRO B CA  
508  C C   . PRO A 65  ? 0.70468 0.47057 0.61960 0.05205  -0.00745 0.02712  64   PRO B C   
509  O O   . PRO A 65  ? 0.67363 0.44112 0.58800 0.06536  -0.02357 0.02003  64   PRO B O   
510  C CB  . PRO A 65  ? 0.75535 0.46397 0.63215 0.03794  0.00244  0.04283  64   PRO B CB  
511  C CG  . PRO A 65  ? 0.80846 0.48469 0.65453 0.04777  -0.01416 0.04371  64   PRO B CG  
512  C CD  . PRO A 65  ? 0.81797 0.48044 0.63952 0.05029  -0.02279 0.04294  64   PRO B CD  
513  N N   . PRO A 66  ? 0.68486 0.47686 0.62534 0.04580  0.00534  0.02555  65   PRO B N   
514  C CA  . PRO A 66  ? 0.64311 0.46377 0.60840 0.05222  0.00323  0.01595  65   PRO B CA  
515  C C   . PRO A 66  ? 0.65961 0.47580 0.63027 0.05709  -0.00099 0.01630  65   PRO B C   
516  O O   . PRO A 66  ? 0.65826 0.45546 0.62035 0.05269  0.00225  0.02448  65   PRO B O   
517  C CB  . PRO A 66  ? 0.62226 0.46153 0.60334 0.04176  0.01946  0.01662  65   PRO B CB  
518  C CG  . PRO A 66  ? 0.63858 0.45903 0.61124 0.03230  0.02831  0.02726  65   PRO B CG  
519  C CD  . PRO A 66  ? 0.65011 0.44337 0.59642 0.03226  0.02242  0.03178  65   PRO B CD  
520  N N   . LYS A 67  ? 0.66597 0.50117 0.65274 0.06519  -0.00692 0.00570  66   LYS B N   
521  C CA  . LYS A 67  ? 0.65088 0.48464 0.64449 0.06952  -0.01019 0.00434  66   LYS B CA  
522  C C   . LYS A 67  ? 0.61021 0.45846 0.61826 0.06099  0.00308  0.00478  66   LYS B C   
523  O O   . LYS A 67  ? 0.57639 0.44508 0.59649 0.05839  0.00947  -0.00301 66   LYS B O   
524  C CB  . LYS A 67  ? 0.66170 0.50720 0.66556 0.08216  -0.02293 -0.00912 66   LYS B CB  
525  C CG  . LYS A 67  ? 0.73574 0.57892 0.74615 0.08684  -0.02646 -0.01155 66   LYS B CG  
526  C CD  . LYS A 67  ? 0.86435 0.72197 0.88963 0.09939  -0.03835 -0.02779 66   LYS B CD  
527  C CE  . LYS A 67  ? 0.86920 0.71816 0.88512 0.11118  -0.05538 -0.03216 66   LYS B CE  
528  N NZ  . LYS A 67  ? 0.89235 0.76195 0.93070 0.12391  -0.06708 -0.05198 66   LYS B NZ  
529  N N   . VAL A 68  ? 0.59114 0.42657 0.59599 0.05603  0.00732  0.01337  67   VAL B N   
530  C CA  . VAL A 68  ? 0.53538 0.37878 0.54989 0.04918  0.01675  0.01472  67   VAL B CA  
531  C C   . VAL A 68  ? 0.58335 0.42211 0.60080 0.05237  0.01260  0.01383  67   VAL B C   
532  O O   . VAL A 68  ? 0.60552 0.42826 0.61622 0.05478  0.00722  0.01830  67   VAL B O   
533  C CB  . VAL A 68  ? 0.58769 0.42241 0.59979 0.04030  0.02494  0.02371  67   VAL B CB  
534  C CG1 . VAL A 68  ? 0.58531 0.42624 0.60629 0.03546  0.03137  0.02428  67   VAL B CG1 
535  C CG2 . VAL A 68  ? 0.58004 0.41737 0.58742 0.03665  0.02939  0.02452  67   VAL B CG2 
536  N N   . ALA A 69  ? 0.57521 0.42522 0.60003 0.05109  0.01622  0.00794  68   ALA B N   
537  C CA  . ALA A 69  ? 0.55069 0.39535 0.57664 0.05297  0.01293  0.00693  68   ALA B CA  
538  C C   . ALA A 69  ? 0.56234 0.40960 0.58857 0.04664  0.01983  0.00620  68   ALA B C   
539  O O   . ALA A 69  ? 0.55796 0.41328 0.58370 0.04215  0.02714  0.00304  68   ALA B O   
540  C CB  . ALA A 69  ? 0.56705 0.41792 0.59747 0.06093  0.00632  -0.00338 68   ALA B CB  
541  N N   . PHE A 70  ? 0.54944 0.38674 0.57380 0.04598  0.01710  0.00951  69   PHE B N   
542  C CA  . PHE A 70  ? 0.54086 0.37503 0.55996 0.04140  0.02052  0.00811  69   PHE B CA  
543  C C   . PHE A 70  ? 0.59138 0.43083 0.60790 0.04138  0.02308  -0.00267 69   PHE B C   
544  O O   . PHE A 70  ? 0.60089 0.44479 0.62336 0.04670  0.01895  -0.00836 69   PHE B O   
545  C CB  . PHE A 70  ? 0.54681 0.36851 0.56496 0.04131  0.01488  0.01360  69   PHE B CB  
546  C CG  . PHE A 70  ? 0.57690 0.39428 0.59946 0.03879  0.01478  0.02051  69   PHE B CG  
547  C CD1 . PHE A 70  ? 0.56076 0.37744 0.59072 0.03896  0.01458  0.02457  69   PHE B CD1 
548  C CD2 . PHE A 70  ? 0.58223 0.39388 0.60038 0.03598  0.01490  0.02187  69   PHE B CD2 
549  C CE1 . PHE A 70  ? 0.55043 0.36484 0.58809 0.03543  0.01628  0.02826  69   PHE B CE1 
550  C CE2 . PHE A 70  ? 0.57459 0.38411 0.60136 0.03472  0.01389  0.02598  69   PHE B CE2 
551  C CZ  . PHE A 70  ? 0.59760 0.41056 0.63653 0.03398  0.01547  0.02837  69   PHE B CZ  
552  N N   . THR A 71  ? 0.60140 0.43885 0.60822 0.03492  0.03068  -0.00669 70   THR B N   
553  C CA  . THR A 71  ? 0.59682 0.43389 0.59751 0.03166  0.03554  -0.01760 70   THR B CA  
554  C C   . THR A 71  ? 0.61608 0.43321 0.59859 0.02710  0.03473  -0.01441 70   THR B C   
555  O O   . THR A 71  ? 0.73219 0.54408 0.70597 0.02337  0.03857  -0.02272 70   THR B O   
556  C CB  . THR A 71  ? 0.60022 0.44833 0.60040 0.02581  0.04738  -0.02869 70   THR B CB  
557  O OG1 . THR A 71  ? 0.66663 0.50765 0.65580 0.02033  0.05275  -0.02245 70   THR B OG1 
558  C CG2 . THR A 71  ? 0.59623 0.46533 0.61619 0.03217  0.04515  -0.03548 70   THR B CG2 
559  N N   . THR A 72  ? 0.62488 0.43021 0.60171 0.02740  0.02931  -0.00385 71   THR B N   
560  C CA  . THR A 72  ? 0.63934 0.42412 0.59956 0.02561  0.02381  -0.00028 71   THR B CA  
561  C C   . THR A 72  ? 0.61466 0.39900 0.58667 0.03154  0.01289  0.00431  71   THR B C   
562  O O   . THR A 72  ? 0.56429 0.35679 0.55264 0.03551  0.00924  0.00952  71   THR B O   
563  C CB  . THR A 72  ? 0.61301 0.38546 0.56241 0.02373  0.02264  0.00621  71   THR B CB  
564  O OG1 . THR A 72  ? 0.67945 0.45006 0.61521 0.01703  0.03450  0.00133  71   THR B OG1 
565  C CG2 . THR A 72  ? 0.64360 0.39229 0.57459 0.02391  0.01317  0.00937  71   THR B CG2 
566  N N   . ARG A 73  ? 0.61901 0.39286 0.58153 0.03086  0.00926  0.00130  72   ARG B N   
567  C CA  . ARG A 73  ? 0.65328 0.42551 0.62565 0.03541  -0.00027 0.00443  72   ARG B CA  
568  C C   . ARG A 73  ? 0.63769 0.40423 0.61533 0.03739  -0.00870 0.01147  72   ARG B C   
569  O O   . ARG A 73  ? 0.63917 0.39429 0.60433 0.03579  -0.01105 0.01334  72   ARG B O   
570  C CB  . ARG A 73  ? 0.71366 0.47350 0.67209 0.03325  -0.00250 -0.00043 72   ARG B CB  
571  C CG  . ARG A 73  ? 0.72251 0.48990 0.68155 0.03155  0.00574  -0.01036 72   ARG B CG  
572  C CD  . ARG A 73  ? 0.83810 0.61841 0.81738 0.03819  0.00293  -0.01217 72   ARG B CD  
573  N NE  . ARG A 73  ? 0.80375 0.57537 0.78292 0.03998  -0.00433 -0.01074 72   ARG B NE  
574  C CZ  . ARG A 73  ? 0.74214 0.51391 0.73256 0.04426  -0.01129 -0.00453 72   ARG B CZ  
575  N NH1 . ARG A 73  ? 0.76609 0.54461 0.76735 0.04683  -0.01169 0.00103  72   ARG B NH1 
576  N NH2 . ARG A 73  ? 0.78324 0.54658 0.77245 0.04451  -0.01689 -0.00457 72   ARG B NH2 
577  N N   . ILE A 74  ? 0.59491 0.36827 0.59107 0.04071  -0.01297 0.01409  73   ILE B N   
578  C CA  . ILE A 74  ? 0.59618 0.36877 0.60499 0.04193  -0.01927 0.01748  73   ILE B CA  
579  C C   . ILE A 74  ? 0.62694 0.40094 0.64958 0.04328  -0.02367 0.01661  73   ILE B C   
580  O O   . ILE A 74  ? 0.60418 0.38186 0.62973 0.04386  -0.01979 0.01616  73   ILE B O   
581  C CB  . ILE A 74  ? 0.57282 0.35497 0.59234 0.04112  -0.01318 0.02051  73   ILE B CB  
582  C CG1 . ILE A 74  ? 0.57938 0.36236 0.61601 0.04160  -0.01832 0.02122  73   ILE B CG1 
583  C CG2 . ILE A 74  ? 0.59342 0.38499 0.61944 0.04133  -0.00646 0.02098  73   ILE B CG2 
584  C CD1 . ILE A 74  ? 0.61079 0.40051 0.65553 0.03991  -0.01221 0.02336  73   ILE B CD1 
585  N N   . TYR A 75  ? 0.64021 0.41012 0.67115 0.04404  -0.03238 0.01528  74   TYR B N   
586  C CA  . TYR A 75  ? 0.61079 0.38164 0.65561 0.04388  -0.03593 0.01247  74   TYR B CA  
587  C C   . TYR A 75  ? 0.62269 0.40176 0.68901 0.04148  -0.03112 0.01201  74   TYR B C   
588  O O   . TYR A 75  ? 0.61036 0.39288 0.69226 0.04135  -0.03539 0.00885  74   TYR B O   
589  C CB  . TYR A 75  ? 0.63783 0.40070 0.68156 0.04566  -0.04854 0.00861  74   TYR B CB  
590  C CG  . TYR A 75  ? 0.67266 0.43695 0.73050 0.04472  -0.05193 0.00394  74   TYR B CG  
591  C CD1 . TYR A 75  ? 0.65882 0.41736 0.70593 0.04416  -0.05138 0.00312  74   TYR B CD1 
592  C CD2 . TYR A 75  ? 0.63332 0.40493 0.71646 0.04367  -0.05474 -0.00133 74   TYR B CD2 
593  C CE1 . TYR A 75  ? 0.62170 0.38023 0.68036 0.04262  -0.05370 -0.00146 74   TYR B CE1 
594  C CE2 . TYR A 75  ? 0.62110 0.39400 0.71748 0.04134  -0.05625 -0.00735 74   TYR B CE2 
595  C CZ  . TYR A 75  ? 0.61991 0.38548 0.70265 0.04083  -0.05575 -0.00670 74   TYR B CZ  
596  O OH  . TYR A 75  ? 0.59037 0.35615 0.68521 0.03790  -0.05648 -0.01295 74   TYR B OH  
597  N N   . HIS A 76  ? 0.64127 0.42132 0.70787 0.03939  -0.02263 0.01383  75   HIS B N   
598  C CA  . HIS A 76  ? 0.61960 0.40277 0.69951 0.03494  -0.01512 0.01365  75   HIS B CA  
599  C C   . HIS A 76  ? 0.60737 0.38239 0.68254 0.03216  -0.00894 0.01419  75   HIS B C   
600  O O   . HIS A 76  ? 0.58423 0.35408 0.64403 0.03572  -0.00911 0.01704  75   HIS B O   
601  C CB  . HIS A 76  ? 0.60669 0.39470 0.68269 0.03468  -0.00929 0.01781  75   HIS B CB  
602  C CG  . HIS A 76  ? 0.63749 0.42844 0.72778 0.02903  -0.00172 0.01653  75   HIS B CG  
603  N ND1 . HIS A 76  ? 0.63651 0.42066 0.72209 0.02419  0.00727  0.01799  75   HIS B ND1 
604  C CD2 . HIS A 76  ? 0.60839 0.40631 0.71612 0.02707  -0.00144 0.01307  75   HIS B CD2 
605  C CE1 . HIS A 76  ? 0.66823 0.45504 0.76735 0.01778  0.01460  0.01515  75   HIS B CE1 
606  N NE2 . HIS A 76  ? 0.58754 0.38479 0.70309 0.01977  0.00948  0.01158  75   HIS B NE2 
607  N N   . PRO A 77  ? 0.62181 0.39384 0.70886 0.02555  -0.00289 0.01054  76   PRO B N   
608  C CA  . PRO A 77  ? 0.59679 0.35398 0.67288 0.02168  0.00382  0.01124  76   PRO B CA  
609  C C   . PRO A 77  ? 0.61960 0.36746 0.67554 0.02323  0.00830  0.01786  76   PRO B C   
610  O O   . PRO A 77  ? 0.63850 0.37055 0.67789 0.02439  0.00884  0.01973  76   PRO B O   
611  C CB  . PRO A 77  ? 0.59330 0.34928 0.68664 0.01164  0.01228  0.00413  76   PRO B CB  
612  C CG  . PRO A 77  ? 0.61765 0.39000 0.73556 0.01312  0.00510  -0.00252 76   PRO B CG  
613  C CD  . PRO A 77  ? 0.60010 0.38047 0.71154 0.02095  -0.00218 0.00342  76   PRO B CD  
614  N N   . ASN A 78  ? 0.63128 0.38696 0.68714 0.02390  0.01040  0.02096  77   ASN B N   
615  C CA  . ASN A 78  ? 0.65393 0.40093 0.69169 0.02510  0.01372  0.02601  77   ASN B CA  
616  C C   . ASN A 78  ? 0.65386 0.41096 0.68500 0.03362  0.00781  0.02837  77   ASN B C   
617  O O   . ASN A 78  ? 0.65445 0.40994 0.67563 0.03503  0.00951  0.03109  77   ASN B O   
618  C CB  . ASN A 78  ? 0.67230 0.41830 0.71366 0.01705  0.02328  0.02634  77   ASN B CB  
619  C CG  . ASN A 78  ? 0.68381 0.42038 0.73368 0.00640  0.03207  0.02100  77   ASN B CG  
620  O OD1 . ASN A 78  ? 0.69251 0.44186 0.76664 0.00228  0.03399  0.01472  77   ASN B OD1 
621  N ND2 . ASN A 78  ? 0.61639 0.32926 0.64622 0.00195  0.03712  0.02205  77   ASN B ND2 
622  N N   . ILE A 79  ? 0.63319 0.40011 0.66933 0.03823  0.00173  0.02613  78   ILE B N   
623  C CA  . ILE A 79  ? 0.61283 0.38921 0.64373 0.04413  -0.00138 0.02543  78   ILE B CA  
624  C C   . ILE A 79  ? 0.61857 0.39279 0.64608 0.04868  -0.00696 0.02193  78   ILE B C   
625  O O   . ILE A 79  ? 0.63984 0.41322 0.67206 0.04700  -0.00962 0.02017  78   ILE B O   
626  C CB  . ILE A 79  ? 0.61692 0.40513 0.65400 0.04242  -0.00017 0.02504  78   ILE B CB  
627  C CG1 . ILE A 79  ? 0.62579 0.41655 0.66838 0.03777  0.00584  0.02775  78   ILE B CG1 
628  C CG2 . ILE A 79  ? 0.54783 0.34406 0.57799 0.04599  -0.00028 0.02234  78   ILE B CG2 
629  C CD1 . ILE A 79  ? 0.56971 0.36657 0.62182 0.03566  0.00542  0.02701  78   ILE B CD1 
630  N N   . ASN A 80  ? 0.60738 0.38061 0.62766 0.05475  -0.00946 0.01977  79   ASN B N   
631  C CA  . ASN A 80  ? 0.57046 0.34131 0.58898 0.05908  -0.01391 0.01511  79   ASN B CA  
632  C C   . ASN A 80  ? 0.58167 0.36502 0.60216 0.05950  -0.01314 0.00925  79   ASN B C   
633  O O   . ASN A 80  ? 0.63173 0.42340 0.65294 0.05619  -0.00936 0.00944  79   ASN B O   
634  C CB  . ASN A 80  ? 0.56773 0.32895 0.57877 0.06636  -0.01829 0.01371  79   ASN B CB  
635  C CG  . ASN A 80  ? 0.56144 0.33252 0.57263 0.07234  -0.02011 0.00986  79   ASN B CG  
636  O OD1 . ASN A 80  ? 0.57538 0.36242 0.59298 0.07060  -0.01655 0.00636  79   ASN B OD1 
637  N ND2 . ASN A 80  ? 0.57916 0.33895 0.58222 0.07989  -0.02653 0.00918  79   ASN B ND2 
638  N N   . SER A 81  ? 0.57385 0.35625 0.59343 0.06258  -0.01556 0.00321  80   SER B N   
639  C CA  . SER A 81  ? 0.59988 0.39011 0.61825 0.06031  -0.01243 -0.00386 80   SER B CA  
640  C C   . SER A 81  ? 0.60043 0.40409 0.62241 0.06221  -0.00846 -0.01067 80   SER B C   
641  O O   . SER A 81  ? 0.61857 0.42782 0.63747 0.05729  -0.00245 -0.01647 80   SER B O   
642  C CB  . SER A 81  ? 0.63129 0.41663 0.64839 0.06164  -0.01447 -0.01004 80   SER B CB  
643  O OG  . SER A 81  ? 0.61625 0.40444 0.63903 0.06927  -0.01706 -0.01644 80   SER B OG  
644  N N   . ASN A 82  ? 0.61315 0.42010 0.63969 0.06863  -0.01166 -0.01088 81   ASN B N   
645  C CA  . ASN A 82  ? 0.59607 0.41765 0.62862 0.07082  -0.00919 -0.01794 81   ASN B CA  
646  C C   . ASN A 82  ? 0.59605 0.42055 0.62584 0.06622  -0.00498 -0.01081 81   ASN B C   
647  O O   . ASN A 82  ? 0.57734 0.41330 0.61156 0.06772  -0.00319 -0.01545 81   ASN B O   
648  C CB  . ASN A 82  ? 0.61070 0.43295 0.64855 0.08179  -0.01777 -0.02311 81   ASN B CB  
649  C CG  . ASN A 82  ? 0.68724 0.51171 0.73283 0.08743  -0.02122 -0.03471 81   ASN B CG  
650  O OD1 . ASN A 82  ? 0.63980 0.46713 0.68658 0.08162  -0.01511 -0.03998 81   ASN B OD1 
651  N ND2 . ASN A 82  ? 0.68804 0.50902 0.73726 0.09889  -0.03151 -0.03920 81   ASN B ND2 
652  N N   . GLY A 83  ? 0.56962 0.38477 0.59427 0.06106  -0.00386 -0.00087 82   GLY B N   
653  C CA  . GLY A 83  ? 0.60135 0.41923 0.62524 0.05667  0.00052  0.00485  82   GLY B CA  
654  C C   . GLY A 83  ? 0.57517 0.38912 0.59816 0.05889  -0.00133 0.01017  82   GLY B C   
655  O O   . GLY A 83  ? 0.58969 0.40669 0.61276 0.05477  0.00329  0.01404  82   GLY B O   
656  N N   . SER A 84  ? 0.60818 0.41228 0.62737 0.06483  -0.00776 0.01047  83   SER B N   
657  C CA  . SER A 84  ? 0.61169 0.40482 0.62258 0.06556  -0.00927 0.01607  83   SER B CA  
658  C C   . SER A 84  ? 0.62262 0.40614 0.63209 0.05708  -0.00353 0.02385  83   SER B C   
659  O O   . SER A 84  ? 0.60876 0.38972 0.62322 0.05370  -0.00254 0.02469  83   SER B O   
660  C CB  . SER A 84  ? 0.57666 0.35373 0.57767 0.07364  -0.01825 0.01521  83   SER B CB  
661  O OG  . SER A 84  ? 0.56469 0.35131 0.56880 0.08269  -0.02502 0.00691  83   SER B OG  
662  N N   . ILE A 85  ? 0.62400 0.40286 0.62796 0.05340  0.00027  0.02798  84   ILE B N   
663  C CA  . ILE A 85  ? 0.62127 0.39388 0.62766 0.04422  0.00779  0.03265  84   ILE B CA  
664  C C   . ILE A 85  ? 0.66801 0.41718 0.65780 0.04136  0.00909  0.03630  84   ILE B C   
665  O O   . ILE A 85  ? 0.67274 0.41384 0.64790 0.04425  0.00650  0.03753  84   ILE B O   
666  C CB  . ILE A 85  ? 0.63789 0.42378 0.65136 0.03967  0.01430  0.03340  84   ILE B CB  
667  C CG1 . ILE A 85  ? 0.62045 0.42354 0.64264 0.04192  0.01368  0.02958  84   ILE B CG1 
668  C CG2 . ILE A 85  ? 0.64082 0.42228 0.66184 0.03066  0.02187  0.03573  84   ILE B CG2 
669  C CD1 . ILE A 85  ? 0.58414 0.39813 0.60885 0.03869  0.01966  0.02959  84   ILE B CD1 
670  N N   . CYS A 86  ? 0.65997 0.48913 0.58837 -0.00125 -0.08394 -0.06022 85   CYS B N   
671  C CA  . CYS A 86  ? 0.66674 0.48538 0.59450 -0.02196 -0.08710 -0.06081 85   CYS B CA  
672  C C   . CYS A 86  ? 0.68949 0.52216 0.62928 -0.03162 -0.07375 -0.05818 85   CYS B C   
673  O O   . CYS A 86  ? 0.69853 0.54669 0.64894 -0.03150 -0.07309 -0.06084 85   CYS B O   
674  C CB  . CYS A 86  ? 0.69138 0.50606 0.61845 -0.02589 -0.10243 -0.06716 85   CYS B CB  
675  S SG  . CYS A 86  ? 0.73031 0.53389 0.65842 -0.05226 -0.10664 -0.06720 85   CYS B SG  
676  N N   . LEU A 87  ? 0.67895 0.50609 0.61695 -0.04006 -0.06329 -0.05305 86   LEU B N   
677  C CA  . LEU A 87  ? 0.71064 0.55061 0.65931 -0.04817 -0.04932 -0.05037 86   LEU B CA  
678  C C   . LEU A 87  ? 0.70405 0.53013 0.64698 -0.06569 -0.04521 -0.04688 86   LEU B C   
679  O O   . LEU A 87  ? 0.70192 0.51470 0.63530 -0.06466 -0.04391 -0.04356 86   LEU B O   
680  C CB  . LEU A 87  ? 0.66584 0.51988 0.62092 -0.03381 -0.03670 -0.04716 86   LEU B CB  
681  C CG  . LEU A 87  ? 0.67662 0.54507 0.64384 -0.04096 -0.02233 -0.04503 86   LEU B CG  
682  C CD1 . LEU A 87  ? 0.66023 0.54121 0.63758 -0.04754 -0.02525 -0.04893 86   LEU B CD1 
683  C CD2 . LEU A 87  ? 0.64881 0.53114 0.62329 -0.02611 -0.01083 -0.04195 86   LEU B CD2 
684  N N   . ASP A 88  ? 0.71348 0.54290 0.66212 -0.08178 -0.04357 -0.04749 87   ASP B N   
685  C CA  . ASP A 88  ? 0.77528 0.59161 0.71808 -0.09975 -0.04142 -0.04453 87   ASP B CA  
686  C C   . ASP A 88  ? 0.79243 0.60692 0.73289 -0.09922 -0.02805 -0.03963 87   ASP B C   
687  O O   . ASP A 88  ? 0.77249 0.57074 0.70278 -0.10695 -0.02885 -0.03673 87   ASP B O   
688  C CB  . ASP A 88  ? 0.83085 0.65615 0.78262 -0.11541 -0.03894 -0.04539 87   ASP B CB  
689  C CG  . ASP A 88  ? 0.94730 0.79489 0.91306 -0.11087 -0.02568 -0.04523 87   ASP B CG  
690  O OD1 . ASP A 88  ? 0.83729 0.69390 0.80649 -0.09483 -0.01976 -0.04480 87   ASP B OD1 
691  O OD2 . ASP A 88  ? 0.95923 0.81538 0.93273 -0.12356 -0.02096 -0.04516 87   ASP B OD2 
692  N N   . ILE A 89  ? 0.74850 0.57905 0.69815 -0.08916 -0.01636 -0.03860 88   ILE B N   
693  C CA  . ILE A 89  ? 0.76102 0.59117 0.71004 -0.08804 -0.00331 -0.03418 88   ILE B CA  
694  C C   . ILE A 89  ? 0.76431 0.57858 0.70113 -0.08076 -0.00699 -0.03140 88   ILE B C   
695  O O   . ILE A 89  ? 0.75511 0.56077 0.68669 -0.08615 -0.00007 -0.02750 88   ILE B O   
696  C CB  . ILE A 89  ? 0.73325 0.58408 0.69537 -0.07584 0.00785  -0.03397 88   ILE B CB  
697  C CG1 . ILE A 89  ? 0.71939 0.58514 0.69334 -0.08479 0.01158  -0.03645 88   ILE B CG1 
698  C CG2 . ILE A 89  ? 0.72933 0.57994 0.69149 -0.07205 0.02058  -0.02952 88   ILE B CG2 
699  C CD1 . ILE A 89  ? 0.69380 0.55483 0.66663 -0.10387 0.01763  -0.03498 88   ILE B CD1 
700  N N   . LEU A 90  ? 0.75621 0.56547 0.68773 -0.06969 -0.01859 -0.03349 89   LEU B N   
701  C CA  . LEU A 90  ? 0.76877 0.56479 0.68941 -0.06027 -0.02268 -0.03101 89   LEU B CA  
702  C C   . LEU A 90  ? 0.82195 0.59641 0.72984 -0.07193 -0.03246 -0.03057 89   LEU B C   
703  O O   . LEU A 90  ? 0.86879 0.63063 0.76697 -0.06600 -0.03562 -0.02802 89   LEU B O   
704  C CB  . LEU A 90  ? 0.72543 0.52777 0.64662 -0.04132 -0.03022 -0.03362 89   LEU B CB  
705  C CG  . LEU A 90  ? 0.66608 0.48894 0.59887 -0.02703 -0.02039 -0.03273 89   LEU B CG  
706  C CD1 . LEU A 90  ? 0.68846 0.51798 0.62126 -0.00913 -0.02858 -0.03542 89   LEU B CD1 
707  C CD2 . LEU A 90  ? 0.66159 0.48282 0.59352 -0.02348 -0.00899 -0.02695 89   LEU B CD2 
708  N N   . ARG A 91  ? 0.83555 0.60569 0.74358 -0.08832 -0.03733 -0.03256 90   ARG B N   
709  C CA  . ARG A 91  ? 0.90373 0.65337 0.80024 -0.10007 -0.04655 -0.03160 90   ARG B CA  
710  C C   . ARG A 91  ? 0.87333 0.62001 0.77079 -0.12109 -0.04220 -0.02990 90   ARG B C   
711  O O   . ARG A 91  ? 0.86868 0.61005 0.76243 -0.12812 -0.03355 -0.02569 90   ARG B O   
712  C CB  . ARG A 91  ? 0.96016 0.70324 0.85324 -0.09729 -0.06289 -0.03630 90   ARG B CB  
713  C CG  . ARG A 91  ? 1.17289 0.89329 1.05328 -0.10547 -0.07373 -0.03516 90   ARG B CG  
714  C CD  . ARG A 91  ? 1.32575 1.03868 1.20343 -0.10482 -0.09064 -0.04030 90   ARG B CD  
715  N NE  . ARG A 91  ? 1.45092 1.14265 1.31616 -0.10645 -0.10075 -0.03917 90   ARG B NE  
716  C CZ  . ARG A 91  ? 1.50398 1.18327 1.36500 -0.11267 -0.11519 -0.04218 90   ARG B CZ  
717  N NH1 . ARG A 91  ? 1.49009 1.17540 1.35808 -0.11835 -0.12203 -0.04654 90   ARG B NH1 
718  N NH2 . ARG A 91  ? 1.51609 1.17633 1.36600 -0.11316 -0.12318 -0.04066 90   ARG B NH2 
719  N N   . SER A 92  ? 0.89601 0.64665 0.79857 -0.13121 -0.04809 -0.03300 91   SER B N   
720  C CA  . SER A 92  ? 0.91976 0.66706 0.82253 -0.15167 -0.04549 -0.03110 91   SER B CA  
721  C C   . SER A 92  ? 0.88317 0.64547 0.79459 -0.15590 -0.02941 -0.02933 91   SER B C   
722  O O   . SER A 92  ? 0.89431 0.65150 0.80213 -0.16770 -0.02213 -0.02585 91   SER B O   
723  C CB  . SER A 92  ? 0.95069 0.69840 0.85715 -0.16116 -0.05685 -0.03448 91   SER B CB  
724  O OG  . SER A 92  ? 1.04236 0.80953 0.96146 -0.15711 -0.05342 -0.03762 91   SER B OG  
725  N N   . GLN A 93  ? 0.85914 0.63996 0.78183 -0.14584 -0.02359 -0.03171 92   GLN B N   
726  C CA  . GLN A 93  ? 0.83949 0.63602 0.77204 -0.14947 -0.00893 -0.03075 92   GLN B CA  
727  C C   . GLN A 93  ? 0.82047 0.61971 0.75292 -0.13912 0.00313  -0.02795 92   GLN B C   
728  O O   . GLN A 93  ? 0.81506 0.62954 0.75743 -0.13672 0.01517  -0.02787 92   GLN B O   
729  C CB  . GLN A 93  ? 0.83113 0.64691 0.77695 -0.14429 -0.00847 -0.03442 92   GLN B CB  
730  C CG  . GLN A 93  ? 0.87988 0.69568 0.82820 -0.15674 -0.01824 -0.03675 92   GLN B CG  
731  C CD  . GLN A 93  ? 0.98860 0.80139 0.93600 -0.17692 -0.01384 -0.03423 92   GLN B CD  
732  O OE1 . GLN A 93  ? 0.96897 0.76514 0.90618 -0.18741 -0.01974 -0.03211 92   GLN B OE1 
733  N NE2 . GLN A 93  ? 1.00172 0.83093 0.95975 -0.18229 -0.00314 -0.03422 92   GLN B NE2 
734  N N   . TRP A 94  ? 0.79486 0.57970 0.71679 -0.13317 0.00023  -0.02545 93   TRP B N   
735  C CA  . TRP A 94  ? 0.76685 0.55322 0.68862 -0.12488 0.01150  -0.02215 93   TRP B CA  
736  C C   . TRP A 94  ? 0.75918 0.54367 0.68005 -0.13958 0.02223  -0.01956 93   TRP B C   
737  O O   . TRP A 94  ? 0.79834 0.57145 0.71193 -0.15510 0.01848  -0.01851 93   TRP B O   
738  C CB  . TRP A 94  ? 0.73512 0.50652 0.64579 -0.11524 0.00541  -0.01968 93   TRP B CB  
739  C CG  . TRP A 94  ? 0.74589 0.51731 0.65598 -0.10847 0.01646  -0.01560 93   TRP B CG  
740  C CD1 . TRP A 94  ? 0.76466 0.52260 0.66587 -0.11574 0.02004  -0.01157 93   TRP B CD1 
741  C CD2 . TRP A 94  ? 0.72168 0.50784 0.64125 -0.09364 0.02558  -0.01495 93   TRP B CD2 
742  N NE1 . TRP A 94  ? 0.75869 0.52156 0.66315 -0.10612 0.03048  -0.00857 93   TRP B NE1 
743  C CE2 . TRP A 94  ? 0.71827 0.49842 0.63420 -0.09245 0.03405  -0.01045 93   TRP B CE2 
744  C CE3 . TRP A 94  ? 0.73164 0.53549 0.66260 -0.08107 0.02702  -0.01749 93   TRP B CE3 
745  C CZ2 . TRP A 94  ? 0.71731 0.50829 0.64104 -0.07924 0.04371  -0.00833 93   TRP B CZ2 
746  C CZ3 . TRP A 94  ? 0.70643 0.52152 0.64511 -0.06776 0.03690  -0.01522 93   TRP B CZ3 
747  C CH2 . TRP A 94  ? 0.69215 0.50061 0.62737 -0.06706 0.04505  -0.01064 93   TRP B CH2 
748  N N   . SER A 95  ? 0.74664 0.54294 0.67535 -0.13455 0.03557  -0.01862 94   SER B N   
749  C CA  . SER A 95  ? 0.76015 0.55603 0.68855 -0.14522 0.04732  -0.01647 94   SER B CA  
750  C C   . SER A 95  ? 0.74094 0.53474 0.66814 -0.13406 0.05532  -0.01328 94   SER B C   
751  O O   . SER A 95  ? 0.71403 0.51611 0.64726 -0.11765 0.05646  -0.01332 94   SER B O   
752  C CB  . SER A 95  ? 0.74303 0.55703 0.68406 -0.15085 0.05681  -0.01889 94   SER B CB  
753  O OG  . SER A 95  ? 0.78842 0.60435 0.73061 -0.15604 0.06993  -0.01720 94   SER B OG  
754  N N   . PRO A 96  ? 0.76185 0.54442 0.68117 -0.14251 0.06033  -0.01018 95   PRO B N   
755  C CA  . PRO A 96  ? 0.77056 0.55154 0.68968 -0.13260 0.06843  -0.00693 95   PRO B CA  
756  C C   . PRO A 96  ? 0.75599 0.55449 0.68871 -0.12616 0.08169  -0.00792 95   PRO B C   
757  O O   . PRO A 96  ? 0.70768 0.50689 0.64252 -0.11582 0.08801  -0.00527 95   PRO B O   
758  C CB  . PRO A 96  ? 0.79318 0.55825 0.70068 -0.14622 0.07011  -0.00392 95   PRO B CB  
759  C CG  . PRO A 96  ? 0.81467 0.56869 0.71341 -0.15808 0.05817  -0.00462 95   PRO B CG  
760  C CD  . PRO A 96  ? 0.79423 0.56231 0.70263 -0.16013 0.05608  -0.00890 95   PRO B CD  
761  N N   . ALA A 97  ? 0.75130 0.56405 0.69379 -0.13157 0.08581  -0.01141 96   ALA B N   
762  C CA  . ALA A 97  ? 0.73463 0.56499 0.69117 -0.12484 0.09772  -0.01268 96   ALA B CA  
763  C C   . ALA A 97  ? 0.72372 0.56770 0.69064 -0.10802 0.09544  -0.01382 96   ALA B C   
764  O O   . ALA A 97  ? 0.71926 0.57827 0.69868 -0.10061 0.10484  -0.01443 96   ALA B O   
765  C CB  . ALA A 97  ? 0.73458 0.57501 0.69731 -0.13856 0.10384  -0.01575 96   ALA B CB  
766  N N   . LEU A 98  ? 0.71481 0.55451 0.67727 -0.10175 0.08329  -0.01425 97   LEU B N   
767  C CA  . LEU A 98  ? 0.69294 0.54646 0.66504 -0.08578 0.08118  -0.01545 97   LEU B CA  
768  C C   . LEU A 98  ? 0.68577 0.53739 0.65718 -0.06937 0.08253  -0.01169 97   LEU B C   
769  O O   . LEU A 98  ? 0.68990 0.52646 0.65075 -0.06988 0.08063  -0.00839 97   LEU B O   
770  C CB  . LEU A 98  ? 0.68819 0.53991 0.65688 -0.08574 0.06748  -0.01828 97   LEU B CB  
771  C CG  . LEU A 98  ? 0.68802 0.54686 0.66160 -0.09902 0.06628  -0.02191 97   LEU B CG  
772  C CD1 . LEU A 98  ? 0.69748 0.54794 0.66388 -0.10154 0.05111  -0.02401 97   LEU B CD1 
773  C CD2 . LEU A 98  ? 0.65450 0.53505 0.64410 -0.09263 0.07365  -0.02398 97   LEU B CD2 
774  N N   . THR A 99  ? 0.66781 0.53552 0.65111 -0.05489 0.08605  -0.01180 98   THR B N   
775  C CA  . THR A 99  ? 0.65460 0.52413 0.63988 -0.03832 0.08822  -0.00782 98   THR B CA  
776  C C   . THR A 99  ? 0.64256 0.51970 0.62999 -0.02375 0.07916  -0.00879 98   THR B C   
777  O O   . THR A 99  ? 0.60987 0.49378 0.60014 -0.02579 0.07314  -0.01290 98   THR B O   
778  C CB  . THR A 99  ? 0.65537 0.53849 0.65422 -0.03303 0.10199  -0.00628 98   THR B CB  
779  O OG1 . THR A 99  ? 0.64626 0.54828 0.65851 -0.02935 0.10437  -0.00945 98   THR B OG1 
780  C CG2 . THR A 99  ? 0.66955 0.54603 0.66644 -0.04770 0.11113  -0.00622 98   THR B CG2 
781  N N   . ILE A 100 ? 0.67348 0.41801 0.56755 0.02942  -0.00260 -0.02679 99   ILE B N   
782  C CA  . ILE A 100 ? 0.70936 0.45933 0.61853 0.03878  -0.01170 -0.02078 99   ILE B CA  
783  C C   . ILE A 100 ? 0.68873 0.46048 0.63008 0.04406  -0.00957 -0.03373 99   ILE B C   
784  O O   . ILE A 100 ? 0.65594 0.43573 0.60932 0.04577  -0.01072 -0.03394 99   ILE B O   
785  C CB  . ILE A 100 ? 0.67941 0.42037 0.58655 0.05058  -0.02581 -0.00800 99   ILE B CB  
786  C CG1 . ILE A 100 ? 0.68474 0.40447 0.56087 0.04586  -0.02896 0.00631  99   ILE B CG1 
787  C CG2 . ILE A 100 ? 0.68995 0.43922 0.61628 0.06119  -0.03500 -0.00375 99   ILE B CG2 
788  C CD1 . ILE A 100 ? 0.65537 0.36943 0.52074 0.04087  -0.02832 0.01327  99   ILE B CD1 
789  N N   . SER A 101 ? 0.68284 0.46422 0.63872 0.04700  -0.00682 -0.04463 100  SER B N   
790  C CA  A SER A 101 ? 0.65475 0.45720 0.64175 0.05186  -0.00433 -0.05794 100  SER B CA  
791  C CA  B SER A 101 ? 0.68466 0.48710 0.67165 0.05188  -0.00434 -0.05794 100  SER B CA  
792  C C   . SER A 101 ? 0.64816 0.46030 0.63893 0.04171  0.00702  -0.06689 100  SER B C   
793  O O   . SER A 101 ? 0.64302 0.46794 0.65371 0.04558  0.00548  -0.07019 100  SER B O   
794  C CB  A SER A 101 ? 0.67810 0.48727 0.67570 0.05427  -0.00117 -0.06894 100  SER B CB  
795  C CB  B SER A 101 ? 0.70497 0.51406 0.70243 0.05423  -0.00116 -0.06891 100  SER B CB  
796  O OG  A SER A 101 ? 0.67554 0.50531 0.70233 0.05745  0.00298  -0.08321 100  SER B OG  
797  O OG  B SER A 101 ? 0.69483 0.49047 0.67960 0.05921  -0.00895 -0.06022 100  SER B OG  
798  N N   . LYS A 102 ? 0.66760 0.47395 0.63932 0.02838  0.01853  -0.07098 101  LYS B N   
799  C CA  . LYS A 102 ? 0.59982 0.41411 0.57257 0.01745  0.02979  -0.07882 101  LYS B CA  
800  C C   . LYS A 102 ? 0.63212 0.44072 0.59795 0.01626  0.02559  -0.06864 101  LYS B C   
801  O O   . LYS A 102 ? 0.60556 0.42620 0.58539 0.01392  0.02953  -0.07456 101  LYS B O   
802  C CB  . LYS A 102 ? 0.65971 0.46627 0.60968 0.00312  0.04208  -0.08310 101  LYS B CB  
803  C CG  . LYS A 102 ? 0.70854 0.51717 0.66046 0.00408  0.04553  -0.09143 101  LYS B CG  
804  C CD  . LYS A 102 ? 0.75795 0.58874 0.73807 0.00519  0.05311  -0.10897 101  LYS B CD  
805  C CE  . LYS A 102 ? 0.89577 0.73007 0.88273 0.00926  0.05442  -0.11756 101  LYS B CE  
806  N NZ  . LYS A 102 ? 0.75737 0.58768 0.75278 0.02371  0.04056  -0.11058 101  LYS B NZ  
807  N N   . VAL A 103 ? 0.64453 0.43493 0.58907 0.01792  0.01752  -0.05343 102  VAL B N   
808  C CA  . VAL A 103 ? 0.62872 0.41227 0.56506 0.01691  0.01326  -0.04327 102  VAL B CA  
809  C C   . VAL A 103 ? 0.61223 0.40910 0.57514 0.02839  0.00508  -0.04372 102  VAL B C   
810  O O   . VAL A 103 ? 0.60652 0.40875 0.57514 0.02573  0.00666  -0.04443 102  VAL B O   
811  C CB  . VAL A 103 ? 0.60086 0.36254 0.51029 0.01774  0.00544  -0.02689 102  VAL B CB  
812  C CG1 . VAL A 103 ? 0.64405 0.39979 0.54892 0.01988  -0.00116 -0.01617 102  VAL B CG1 
813  C CG2 . VAL A 103 ? 0.62058 0.36858 0.50204 0.00467  0.01410  -0.02599 102  VAL B CG2 
814  N N   . LEU A 104 ? 0.58886 0.39083 0.56791 0.04116  -0.00405 -0.04303 103  LEU B N   
815  C CA  . LEU A 104 ? 0.60468 0.41973 0.60963 0.05240  -0.01215 -0.04372 103  LEU B CA  
816  C C   . LEU A 104 ? 0.59873 0.43414 0.62781 0.04972  -0.00399 -0.05898 103  LEU B C   
817  O O   . LEU A 104 ? 0.57319 0.41755 0.61619 0.05217  -0.00621 -0.05968 103  LEU B O   
818  C CB  . LEU A 104 ? 0.61076 0.42712 0.62771 0.06581  -0.02283 -0.04072 103  LEU B CB  
819  C CG  . LEU A 104 ? 0.60201 0.39967 0.59811 0.07021  -0.03271 -0.02461 103  LEU B CG  
820  C CD1 . LEU A 104 ? 0.59907 0.39685 0.60389 0.08102  -0.04119 -0.02281 103  LEU B CD1 
821  C CD2 . LEU A 104 ? 0.58544 0.37893 0.57960 0.07483  -0.04108 -0.01338 103  LEU B CD2 
822  N N   . LEU A 105 ? 0.59567 0.43851 0.62922 0.04407  0.00595  -0.07145 104  LEU B N   
823  C CA  . LEU A 105 ? 0.59034 0.45295 0.64646 0.04073  0.01456  -0.08637 104  LEU B CA  
824  C C   . LEU A 105 ? 0.58500 0.44684 0.63113 0.02877  0.02271  -0.08691 104  LEU B C   
825  O O   . LEU A 105 ? 0.59279 0.46890 0.65783 0.02891  0.02459  -0.09337 104  LEU B O   
826  C CB  . LEU A 105 ? 0.61137 0.48184 0.67345 0.03697  0.02393  -0.09977 104  LEU B CB  
827  C CG  . LEU A 105 ? 0.63880 0.51481 0.71777 0.04897  0.01712  -0.10317 104  LEU B CG  
828  C CD1 . LEU A 105 ? 0.62804 0.51148 0.71169 0.04427  0.02742  -0.11714 104  LEU B CD1 
829  C CD2 . LEU A 105 ? 0.65970 0.55134 0.76931 0.06092  0.00892  -0.10592 104  LEU B CD2 
830  N N   . SER A 106 ? 0.61170 0.45675 0.62820 0.01834  0.02727  -0.07994 105  SER B N   
831  C CA  A SER A 106 ? 0.63252 0.47507 0.63781 0.00674  0.03445  -0.07942 105  SER B CA  
832  C CA  B SER A 106 ? 0.62769 0.47000 0.63265 0.00670  0.03442  -0.07927 105  SER B CA  
833  C C   . SER A 106 ? 0.61460 0.45443 0.62250 0.01225  0.02520  -0.06966 105  SER B C   
834  O O   . SER A 106 ? 0.60759 0.45398 0.62077 0.00664  0.02952  -0.07302 105  SER B O   
835  C CB  A SER A 106 ? 0.63086 0.45485 0.60290 -0.00538 0.04071  -0.07354 105  SER B CB  
836  C CB  B SER A 106 ? 0.62425 0.44767 0.59570 -0.00525 0.04041  -0.07307 105  SER B CB  
837  O OG  A SER A 106 ? 0.63717 0.46381 0.60636 -0.01071 0.04949  -0.08288 105  SER B OG  
838  O OG  B SER A 106 ? 0.64701 0.46663 0.60619 -0.01684 0.04708  -0.07190 105  SER B OG  
839  N N   . ILE A 107 ? 0.61999 0.45069 0.62474 0.02317  0.01255  -0.05788 106  ILE B N   
840  C CA  . ILE A 107 ? 0.61629 0.44601 0.62599 0.02979  0.00323  -0.04934 106  ILE B CA  
841  C C   . ILE A 107 ? 0.60446 0.45525 0.64690 0.03733  0.00102  -0.05855 106  ILE B C   
842  O O   . ILE A 107 ? 0.58215 0.43800 0.63168 0.03668  -0.00001 -0.05815 106  ILE B O   
843  C CB  . ILE A 107 ? 0.62404 0.43946 0.62260 0.03975  -0.00956 -0.03472 106  ILE B CB  
844  C CG1 . ILE A 107 ? 0.64539 0.43929 0.61049 0.03129  -0.00776 -0.02423 106  ILE B CG1 
845  C CG2 . ILE A 107 ? 0.60940 0.42770 0.61914 0.04917  -0.01999 -0.02782 106  ILE B CG2 
846  C CD1 . ILE A 107 ? 0.70450 0.48450 0.65785 0.04018  -0.01929 -0.01053 106  ILE B CD1 
847  N N   . CYS A 108 ? 0.59303 0.45625 0.65603 0.04468  -0.00005 -0.06694 107  CYS B N   
848  C CA  . CYS A 108 ? 0.58046 0.46451 0.67532 0.05116  -0.00140 -0.07677 107  CYS B CA  
849  C C   . CYS A 108 ? 0.59428 0.49038 0.69649 0.04006  0.01081  -0.08859 107  CYS B C   
850  O O   . CYS A 108 ? 0.60479 0.51295 0.72460 0.04184  0.00960  -0.09225 107  CYS B O   
851  C CB  . CYS A 108 ? 0.57324 0.46784 0.68805 0.06031  -0.00403 -0.08428 107  CYS B CB  
852  S SG  . CYS A 108 ? 0.62587 0.50885 0.73633 0.07426  -0.01901 -0.07131 107  CYS B SG  
853  N N   . SER A 109 ? 0.59282 0.48590 0.68145 0.02824  0.02268  -0.09460 108  SER B N   
854  C CA  . SER A 109 ? 0.61164 0.51534 0.70518 0.01663  0.03476  -0.10520 108  SER B CA  
855  C C   . SER A 109 ? 0.59213 0.48766 0.67238 0.01027  0.03431  -0.09733 108  SER B C   
856  O O   . SER A 109 ? 0.60850 0.51642 0.70343 0.00740  0.03746  -0.10351 108  SER B O   
857  C CB  . SER A 109 ? 0.64419 0.54502 0.72357 0.00498  0.04745  -0.11236 108  SER B CB  
858  O OG  . SER A 109 ? 0.73693 0.65389 0.82973 -0.00375 0.05906  -0.12594 108  SER B OG  
859  N N   . LEU A 110 ? 0.60120 0.47595 0.65450 0.00870  0.02965  -0.08346 109  LEU B N   
860  C CA  . LEU A 110 ? 0.62500 0.49029 0.66503 0.00403  0.02772  -0.07483 109  LEU B CA  
861  C C   . LEU A 110 ? 0.61778 0.49257 0.67863 0.01439  0.01808  -0.07291 109  LEU B C   
862  O O   . LEU A 110 ? 0.60558 0.48429 0.66970 0.00955  0.02016  -0.07412 109  LEU B O   
863  C CB  . LEU A 110 ? 0.62948 0.47085 0.63865 0.00289  0.02273  -0.05982 109  LEU B CB  
864  C CG  . LEU A 110 ? 0.67476 0.50274 0.66609 -0.00179 0.02009  -0.04929 109  LEU B CG  
865  C CD1 . LEU A 110 ? 0.68618 0.51343 0.66664 -0.01782 0.03248  -0.05474 109  LEU B CD1 
866  C CD2 . LEU A 110 ? 0.67402 0.48017 0.63974 0.00109  0.01243  -0.03413 109  LEU B CD2 
867  N N   . LEU A 111 ? 0.62397 0.50234 0.69874 0.02849  0.00734  -0.06981 110  LEU B N   
868  C CA  . LEU A 111 ? 0.61629 0.50514 0.71255 0.03878  -0.00187 -0.06884 110  LEU B CA  
869  C C   . LEU A 111 ? 0.62014 0.53113 0.74370 0.03696  0.00420  -0.08335 110  LEU B C   
870  O O   . LEU A 111 ? 0.65642 0.57544 0.79355 0.04005  0.00011  -0.08361 110  LEU B O   
871  C CB  . LEU A 111 ? 0.57939 0.46907 0.68654 0.05385  -0.01388 -0.06382 110  LEU B CB  
872  C CG  . LEU A 111 ? 0.58301 0.45327 0.66856 0.05915  -0.02290 -0.04865 110  LEU B CG  
873  C CD1 . LEU A 111 ? 0.57773 0.45292 0.68007 0.07471  -0.03621 -0.04371 110  LEU B CD1 
874  C CD2 . LEU A 111 ? 0.60720 0.46261 0.67032 0.05293  -0.02345 -0.03849 110  LEU B CD2 
875  N N   . CYS A 112 ? 0.58435 0.50575 0.71673 0.03224  0.01374  -0.09561 111  CYS B N   
876  C CA  . CYS A 112 ? 0.60297 0.54600 0.76149 0.02998  0.02018  -0.10989 111  CYS B CA  
877  C C   . CYS A 112 ? 0.63937 0.58296 0.78882 0.01521  0.03119  -0.11404 111  CYS B C   
878  O O   . CYS A 112 ? 0.64565 0.60360 0.81335 0.01373  0.03319  -0.12100 111  CYS B O   
879  C CB  . CYS A 112 ? 0.61407 0.56955 0.78803 0.03160  0.02587  -0.12218 111  CYS B CB  
880  S SG  . CYS A 112 ? 0.65786 0.61935 0.85273 0.04991  0.01311  -0.12124 111  CYS B SG  
881  N N   . ASP A 113 ? 0.65305 0.58140 0.77477 0.00400  0.03837  -0.10999 112  ASP B N   
882  C CA  . ASP A 113 ? 0.69127 0.61981 0.80308 -0.01129 0.05009  -0.11465 112  ASP B CA  
883  C C   . ASP A 113 ? 0.68498 0.59045 0.76445 -0.01799 0.04861  -0.10107 112  ASP B C   
884  O O   . ASP A 113 ? 0.67621 0.56877 0.73236 -0.02643 0.05472  -0.09846 112  ASP B O   
885  C CB  . ASP A 113 ? 0.74094 0.67703 0.85332 -0.02030 0.06328  -0.12676 112  ASP B CB  
886  C CG  . ASP A 113 ? 0.85556 0.80189 0.97159 -0.03383 0.07560  -0.13646 112  ASP B CG  
887  O OD1 . ASP A 113 ? 0.83161 0.79644 0.97352 -0.03141 0.07600  -0.14502 112  ASP B OD1 
888  O OD2 . ASP A 113 ? 0.97269 0.90871 1.06581 -0.04700 0.08481  -0.13552 112  ASP B OD2 
889  N N   . PRO A 114 ? 0.71181 0.61153 0.78894 -0.01459 0.04059  -0.09235 113  PRO B N   
890  C CA  . PRO A 114 ? 0.69827 0.57565 0.74505 -0.02031 0.03856  -0.07920 113  PRO B CA  
891  C C   . PRO A 114 ? 0.72597 0.59832 0.75569 -0.03742 0.05109  -0.08254 113  PRO B C   
892  O O   . PRO A 114 ? 0.72345 0.61098 0.76691 -0.04493 0.06063  -0.09460 113  PRO B O   
893  C CB  . PRO A 114 ? 0.67656 0.55379 0.73071 -0.01297 0.02838  -0.07241 113  PRO B CB  
894  C CG  . PRO A 114 ? 0.65186 0.54651 0.73597 0.00051  0.02134  -0.07789 113  PRO B CG  
895  C CD  . PRO A 114 ? 0.67675 0.58909 0.77834 -0.00411 0.03183  -0.09329 113  PRO B CD  
896  N N   . ASN A 115 ? 0.73032 0.58093 0.72946 -0.04366 0.05098  -0.07157 114  ASN B N   
897  C CA  . ASN A 115 ? 0.75117 0.59247 0.72912 -0.05991 0.06119  -0.07160 114  ASN B CA  
898  C C   . ASN A 115 ? 0.75792 0.58854 0.72623 -0.06087 0.05533  -0.06212 114  ASN B C   
899  O O   . ASN A 115 ? 0.76279 0.57341 0.70822 -0.05967 0.04916  -0.04918 114  ASN B O   
900  C CB  . ASN A 115 ? 0.77633 0.59957 0.72588 -0.06587 0.06440  -0.06536 114  ASN B CB  
901  C CG  . ASN A 115 ? 0.89226 0.72378 0.84945 -0.06355 0.06868  -0.07337 114  ASN B CG  
902  O OD1 . ASN A 115 ? 0.89016 0.74099 0.86897 -0.06467 0.07553  -0.08676 114  ASN B OD1 
903  N ND2 . ASN A 115 ? 0.88472 0.70193 0.82523 -0.05937 0.06391  -0.06512 114  ASN B ND2 
904  N N   . PRO A 116 ? 0.73983 0.58265 0.72427 -0.06326 0.05702  -0.06802 115  PRO B N   
905  C CA  . PRO A 116 ? 0.76125 0.59358 0.73651 -0.06402 0.05119  -0.05919 115  PRO B CA  
906  C C   . PRO A 116 ? 0.79355 0.60921 0.74123 -0.07896 0.05796  -0.05432 115  PRO B C   
907  O O   . PRO A 116 ? 0.79953 0.60413 0.73702 -0.07978 0.05292  -0.04623 115  PRO B O   
908  C CB  . PRO A 116 ? 0.73573 0.58878 0.73958 -0.06205 0.05157  -0.06884 115  PRO B CB  
909  C CG  . PRO A 116 ? 0.71654 0.58829 0.73742 -0.06712 0.06229  -0.08349 115  PRO B CG  
910  C CD  . PRO A 116 ? 0.68016 0.54782 0.69491 -0.06260 0.06222  -0.08261 115  PRO B CD  
911  N N   . ASP A 117 ? 0.82093 0.63435 0.75624 -0.09080 0.06908  -0.05905 116  ASP B N   
912  C CA  . ASP A 117 ? 0.83528 0.63185 0.74278 -0.10538 0.07558  -0.05404 116  ASP B CA  
913  C C   . ASP A 117 ? 0.85096 0.62391 0.72981 -0.10407 0.07037  -0.04070 116  ASP B C   
914  O O   . ASP A 117 ? 0.88479 0.64117 0.73831 -0.11528 0.07432  -0.03480 116  ASP B O   
915  C CB  . ASP A 117 ? 0.85103 0.65655 0.75816 -0.11956 0.09035  -0.06544 116  ASP B CB  
916  C CG  . ASP A 117 ? 0.91001 0.73610 0.84103 -0.12405 0.09643  -0.07739 116  ASP B CG  
917  O OD1 . ASP A 117 ? 0.87228 0.70088 0.81334 -0.11948 0.08984  -0.07498 116  ASP B OD1 
918  O OD2 . ASP A 117 ? 0.98617 0.82598 0.92586 -0.13215 0.10776  -0.08920 116  ASP B OD2 
919  N N   . ASP A 118 ? 0.81296 0.58404 0.69523 -0.09092 0.06164  -0.03586 117  ASP B N   
920  C CA  . ASP A 118 ? 0.82721 0.57646 0.68412 -0.08798 0.05515  -0.02251 117  ASP B CA  
921  C C   . ASP A 118 ? 0.81678 0.56518 0.68341 -0.07121 0.04115  -0.01472 117  ASP B C   
922  O O   . ASP A 118 ? 0.77602 0.52303 0.64364 -0.06203 0.03583  -0.01166 117  ASP B O   
923  C CB  . ASP A 118 ? 0.84527 0.59196 0.69243 -0.09114 0.06076  -0.02499 117  ASP B CB  
924  C CG  . ASP A 118 ? 0.87071 0.59330 0.68764 -0.09194 0.05623  -0.01153 117  ASP B CG  
925  O OD1 . ASP A 118 ? 0.91437 0.62235 0.71779 -0.09063 0.04935  -0.00059 117  ASP B OD1 
926  O OD2 . ASP A 118 ? 0.85001 0.56854 0.65756 -0.09303 0.05889  -0.01182 117  ASP B OD2 
927  N N   . PRO A 119 ? 0.82136 0.56944 0.69376 -0.06719 0.03474  -0.01076 118  PRO B N   
928  C CA  . PRO A 119 ? 0.80584 0.55662 0.69134 -0.05111 0.02192  -0.00502 118  PRO B CA  
929  C C   . PRO A 119 ? 0.74359 0.47368 0.60720 -0.04509 0.01275  0.00982  118  PRO B C   
930  O O   . PRO A 119 ? 0.72911 0.44080 0.56669 -0.05332 0.01470  0.01734  118  PRO B O   
931  C CB  . PRO A 119 ? 0.73258 0.48823 0.62801 -0.05132 0.01948  -0.00583 118  PRO B CB  
932  C CG  . PRO A 119 ? 0.76837 0.52742 0.66054 -0.06679 0.03142  -0.01384 118  PRO B CG  
933  C CD  . PRO A 119 ? 0.80216 0.54790 0.67003 -0.07716 0.03883  -0.01163 118  PRO B CD  
934  N N   . LEU A 120 ? 0.72853 0.46213 0.60384 -0.03029 0.00212  0.01424  119  LEU B N   
935  C CA  . LEU A 120 ? 0.71182 0.42847 0.57126 -0.02231 -0.00851 0.02854  119  LEU B CA  
936  C C   . LEU A 120 ? 0.72589 0.44449 0.59490 -0.01412 -0.01734 0.03286  119  LEU B C   
937  O O   . LEU A 120 ? 0.74487 0.44839 0.59898 -0.00947 -0.02527 0.04471  119  LEU B O   
938  C CB  . LEU A 120 ? 0.72936 0.44649 0.59204 -0.01157 -0.01458 0.03188  119  LEU B CB  
939  C CG  . LEU A 120 ? 0.73439 0.43826 0.57540 -0.01695 -0.01097 0.03577  119  LEU B CG  
940  C CD1 . LEU A 120 ? 0.69792 0.39920 0.54059 -0.00416 -0.02042 0.04260  119  LEU B CD1 
941  C CD2 . LEU A 120 ? 0.71395 0.39627 0.52448 -0.02725 -0.00865 0.04468  119  LEU B CD2 
942  N N   . VAL A 121 ? 0.65996 0.39724 0.55404 -0.01182 -0.01635 0.02336  120  VAL B N   
943  C CA  . VAL A 121 ? 0.66261 0.40419 0.56792 -0.00555 -0.02336 0.02525  120  VAL B CA  
944  C C   . VAL A 121 ? 0.64630 0.39868 0.56181 -0.01583 -0.01488 0.01483  120  VAL B C   
945  O O   . VAL A 121 ? 0.62239 0.39451 0.56170 -0.01502 -0.01108 0.00339  120  VAL B O   
946  C CB  . VAL A 121 ? 0.66935 0.42436 0.59790 0.01003  -0.03283 0.02472  120  VAL B CB  
947  C CG1 . VAL A 121 ? 0.64227 0.39909 0.57869 0.01643  -0.04069 0.02826  120  VAL B CG1 
948  C CG2 . VAL A 121 ? 0.65287 0.39802 0.57161 0.01919  -0.04023 0.03430  120  VAL B CG2 
949  N N   . PRO A 122 ? 0.63140 0.37131 0.52942 -0.02600 -0.01151 0.01826  121  PRO B N   
950  C CA  . PRO A 122 ? 0.63817 0.38768 0.54432 -0.03734 -0.00254 0.00831  121  PRO B CA  
951  C C   . PRO A 122 ? 0.63669 0.40560 0.57121 -0.03098 -0.00578 0.00079  121  PRO B C   
952  O O   . PRO A 122 ? 0.63195 0.41657 0.58234 -0.03767 0.00221  -0.01094 121  PRO B O   
953  C CB  . PRO A 122 ? 0.64642 0.37584 0.52710 -0.04649 -0.00178 0.01646  121  PRO B CB  
954  C CG  . PRO A 122 ? 0.65377 0.36344 0.50995 -0.04441 -0.00559 0.02805  121  PRO B CG  
955  C CD  . PRO A 122 ? 0.66837 0.38438 0.53730 -0.02865 -0.01485 0.03106  121  PRO B CD  
956  N N   . GLU A 123 ? 0.63237 0.40085 0.57365 -0.01864 -0.01713 0.00711  122  GLU B N   
957  C CA  . GLU A 123 ? 0.61897 0.40539 0.58643 -0.01301 -0.02045 0.00019  122  GLU B CA  
958  C C   . GLU A 123 ? 0.60384 0.41176 0.59787 -0.00731 -0.01883 -0.01024 122  GLU B C   
959  O O   . GLU A 123 ? 0.58637 0.41217 0.60245 -0.00890 -0.01562 -0.02068 122  GLU B O   
960  C CB  . GLU A 123 ? 0.63154 0.41208 0.59900 -0.00117 -0.03304 0.00960  122  GLU B CB  
961  C CG  . GLU A 123 ? 0.60385 0.40277 0.59805 0.00480  -0.03699 0.00267  122  GLU B CG  
962  C CD  . GLU A 123 ? 0.63405 0.43949 0.63352 -0.00717 -0.02918 -0.00578 122  GLU B CD  
963  O OE1 . GLU A 123 ? 0.63911 0.43211 0.61904 -0.01963 -0.02216 -0.00433 122  GLU B OE1 
964  O OE2 . GLU A 123 ? 0.62323 0.44685 0.64705 -0.00440 -0.02994 -0.01418 122  GLU B OE2 
965  N N   . ILE A 124 ? 0.59375 0.40027 0.58646 -0.00048 -0.02127 -0.00763 123  ILE B N   
966  C CA  . ILE A 124 ? 0.58639 0.41203 0.60298 0.00454  -0.01937 -0.01759 123  ILE B CA  
967  C C   . ILE A 124 ? 0.58639 0.42099 0.60651 -0.00836 -0.00577 -0.02947 123  ILE B C   
968  O O   . ILE A 124 ? 0.58748 0.44206 0.63213 -0.00800 -0.00205 -0.04112 123  ILE B O   
969  C CB  . ILE A 124 ? 0.60986 0.43012 0.62230 0.01450  -0.02543 -0.01132 123  ILE B CB  
970  C CG1 . ILE A 124 ? 0.60248 0.41580 0.61340 0.02757  -0.03882 -0.00005 123  ILE B CG1 
971  C CG2 . ILE A 124 ? 0.58110 0.42079 0.61898 0.02037  -0.02428 -0.02151 123  ILE B CG2 
972  C CD1 . ILE A 124 ? 0.59456 0.40266 0.60133 0.03685  -0.04469 0.00627  123  ILE B CD1 
973  N N   . ALA A 125 ? 0.56067 0.38098 0.55660 -0.01997 0.00185  -0.02679 124  ALA B N   
974  C CA  . ALA A 125 ? 0.61990 0.44816 0.61755 -0.03324 0.01521  -0.03777 124  ALA B CA  
975  C C   . ALA A 125 ? 0.63909 0.47931 0.65047 -0.04018 0.01979  -0.04584 124  ALA B C   
976  O O   . ALA A 125 ? 0.66476 0.52227 0.69347 -0.04554 0.02821  -0.05833 124  ALA B O   
977  C CB  . ALA A 125 ? 0.65416 0.46299 0.62097 -0.04502 0.02181  -0.03206 124  ALA B CB  
978  N N   . ARG A 126 ? 0.61438 0.44577 0.61854 -0.04008 0.01425  -0.03898 125  ARG B N   
979  C CA  . ARG A 126 ? 0.63745 0.47922 0.65411 -0.04636 0.01759  -0.04588 125  ARG B CA  
980  C C   . ARG A 126 ? 0.64633 0.51172 0.69645 -0.03736 0.01428  -0.05524 125  ARG B C   
981  O O   . ARG A 126 ? 0.62416 0.50574 0.69118 -0.04407 0.02156  -0.06657 125  ARG B O   
982  C CB  . ARG A 126 ? 0.63023 0.45616 0.63120 -0.04702 0.01129  -0.03585 125  ARG B CB  
983  C CG  . ARG A 126 ? 0.64446 0.48093 0.65926 -0.05212 0.01313  -0.04237 125  ARG B CG  
984  C CD  . ARG A 126 ? 0.62002 0.44071 0.61975 -0.05220 0.00650  -0.03273 125  ARG B CD  
985  N NE  . ARG A 126 ? 0.68248 0.48314 0.65307 -0.06443 0.01226  -0.02677 125  ARG B NE  
986  C CZ  . ARG A 126 ? 0.66431 0.46487 0.62929 -0.07933 0.02214  -0.03214 125  ARG B CZ  
987  N NH1 . ARG A 126 ? 0.63307 0.45254 0.61949 -0.08412 0.02753  -0.04360 125  ARG B NH1 
988  N NH2 . ARG A 126 ? 0.70646 0.48784 0.64388 -0.08987 0.02685  -0.02597 125  ARG B NH2 
989  N N   . ILE A 127 ? 0.62141 0.48897 0.68145 -0.02228 0.00304  -0.05041 126  ILE B N   
990  C CA  . ILE A 127 ? 0.60550 0.49503 0.69726 -0.01286 -0.00094 -0.05876 126  ILE B CA  
991  C C   . ILE A 127 ? 0.65111 0.55687 0.75909 -0.01494 0.00736  -0.07072 126  ILE B C   
992  O O   . ILE A 127 ? 0.64113 0.56670 0.77318 -0.01634 0.01131  -0.08225 126  ILE B O   
993  C CB  . ILE A 127 ? 0.62377 0.51058 0.72025 0.00342  -0.01467 -0.05017 126  ILE B CB  
994  C CG1 . ILE A 127 ? 0.58232 0.45578 0.66575 0.00511  -0.02221 -0.04012 126  ILE B CG1 
995  C CG2 . ILE A 127 ? 0.60948 0.51836 0.73822 0.01326  -0.01924 -0.05838 126  ILE B CG2 
996  C CD1 . ILE A 127 ? 0.56301 0.44791 0.66127 0.00101  -0.02095 -0.04686 126  ILE B CD1 
997  N N   . TYR A 128 ? 0.61640 0.51415 0.71164 -0.01512 0.01006  -0.06834 127  TYR B N   
998  C CA  . TYR A 128 ? 0.63045 0.54247 0.73938 -0.01743 0.01833  -0.07974 127  TYR B CA  
999  C C   . TYR A 128 ? 0.65032 0.57202 0.76339 -0.03199 0.03130  -0.09073 127  TYR B C   
1000 O O   . TYR A 128 ? 0.64509 0.58731 0.78256 -0.03211 0.03623  -0.10317 127  TYR B O   
1001 C CB  . TYR A 128 ? 0.63999 0.53884 0.72963 -0.01775 0.02022  -0.07477 127  TYR B CB  
1002 C CG  . TYR A 128 ? 0.64531 0.55770 0.74791 -0.01927 0.02826  -0.08618 127  TYR B CG  
1003 C CD1 . TYR A 128 ? 0.64566 0.57034 0.76955 -0.00676 0.02259  -0.09005 127  TYR B CD1 
1004 C CD2 . TYR A 128 ? 0.65845 0.57121 0.75180 -0.03333 0.04155  -0.09317 127  TYR B CD2 
1005 C CE1 . TYR A 128 ? 0.65197 0.58868 0.78772 -0.00794 0.02991  -0.10078 127  TYR B CE1 
1006 C CE2 . TYR A 128 ? 0.65874 0.58391 0.76358 -0.03476 0.04919  -0.10393 127  TYR B CE2 
1007 C CZ  . TYR A 128 ? 0.73075 0.66788 0.85701 -0.02192 0.04336  -0.10791 127  TYR B CZ  
1008 O OH  . TYR A 128 ? 0.67814 0.62742 0.81610 -0.02302 0.05088  -0.11897 127  TYR B OH  
1009 N N   . LYS A 129 ? 0.64892 0.55648 0.73914 -0.04432 0.03665  -0.08631 128  LYS B N   
1010 C CA  . LYS A 129 ? 0.64704 0.56293 0.73933 -0.05914 0.04949  -0.09629 128  LYS B CA  
1011 C C   . LYS A 129 ? 0.65307 0.58442 0.76675 -0.06033 0.04915  -0.10317 128  LYS B C   
1012 O O   . LYS A 129 ? 0.65828 0.60495 0.78530 -0.06907 0.05901  -0.11486 128  LYS B O   
1013 C CB  . LYS A 129 ? 0.69844 0.59350 0.75852 -0.07251 0.05537  -0.08912 128  LYS B CB  
1014 C CG  . LYS A 129 ? 0.72158 0.60291 0.76031 -0.07445 0.05835  -0.08436 128  LYS B CG  
1015 C CD  . LYS A 129 ? 0.81595 0.67629 0.82258 -0.08778 0.06373  -0.07694 128  LYS B CD  
1016 C CE  . LYS A 129 ? 0.88092 0.74870 0.88751 -0.10411 0.07720  -0.08651 128  LYS B CE  
1017 N NZ  . LYS A 129 ? 0.88288 0.73065 0.85748 -0.11715 0.08366  -0.08018 128  LYS B NZ  
1018 N N   . THR A 130 ? 0.68011 0.60922 0.79895 -0.05129 0.03802  -0.09681 129  THR B N   
1019 C CA  . THR A 130 ? 0.69715 0.63874 0.83337 -0.05337 0.03742  -0.10238 129  THR B CA  
1020 C C   . THR A 130 ? 0.69410 0.65702 0.86298 -0.04122 0.03117  -0.10954 129  THR B C   
1021 O O   . THR A 130 ? 0.69491 0.67625 0.88517 -0.04516 0.03586  -0.12038 129  THR B O   
1022 C CB  . THR A 130 ? 0.66853 0.59366 0.78861 -0.05305 0.02973  -0.09127 129  THR B CB  
1023 O OG1 . THR A 130 ? 0.74923 0.66494 0.86488 -0.03893 0.01737  -0.08090 129  THR B OG1 
1024 C CG2 . THR A 130 ? 0.69031 0.59537 0.77973 -0.06645 0.03630  -0.08513 129  THR B CG2 
1025 N N   . ASP A 131 ? 0.68668 0.64777 0.86021 -0.02661 0.02067  -0.10376 130  ASP B N   
1026 C CA  . ASP A 131 ? 0.77912 0.75822 0.98210 -0.01392 0.01270  -0.10860 130  ASP B CA  
1027 C C   . ASP A 131 ? 0.70923 0.69109 0.91891 -0.00290 0.00882  -0.10832 130  ASP B C   
1028 O O   . ASP A 131 ? 0.72740 0.70190 0.93435 0.00903  -0.00218 -0.09935 130  ASP B O   
1029 C CB  . ASP A 131 ? 0.73320 0.70673 0.93610 -0.00622 0.00082  -0.10017 130  ASP B CB  
1030 C CG  . ASP A 131 ? 0.76572 0.75937 0.99994 0.00434  -0.00637 -0.10639 130  ASP B CG  
1031 O OD1 . ASP A 131 ? 0.78518 0.79653 1.04148 0.00706  -0.00309 -0.11660 130  ASP B OD1 
1032 O OD2 . ASP A 131 ? 0.78376 0.77554 1.02056 0.00984  -0.01532 -0.10123 130  ASP B OD2 
1033 N N   . ARG A 132 ? 0.83792 0.50169 0.86988 0.10369  -0.07588 0.06865  131  ARG B N   
1034 C CA  . ARG A 132 ? 0.86958 0.53442 0.89603 0.10681  -0.06296 0.07466  131  ARG B CA  
1035 C C   . ARG A 132 ? 0.88964 0.54232 0.88191 0.10397  -0.06374 0.07596  131  ARG B C   
1036 O O   . ARG A 132 ? 0.85329 0.50083 0.82720 0.10407  -0.04994 0.07219  131  ARG B O   
1037 C CB  . ARG A 132 ? 0.78849 0.46448 0.84309 0.11122  -0.06483 0.08904  131  ARG B CB  
1038 C CG  . ARG A 132 ? 0.73670 0.41541 0.79136 0.11457  -0.04966 0.09481  131  ARG B CG  
1039 C CD  . ARG A 132 ? 0.74935 0.43210 0.80962 0.11584  -0.03345 0.08538  131  ARG B CD  
1040 N NE  . ARG A 132 ? 0.73467 0.42555 0.82152 0.11693  -0.03618 0.08149  131  ARG B NE  
1041 C CZ  . ARG A 132 ? 0.72333 0.42443 0.84043 0.11980  -0.03719 0.08952  131  ARG B CZ  
1042 N NH1 . ARG A 132 ? 0.72414 0.42949 0.85102 0.12202  -0.03533 0.10218  131  ARG B NH1 
1043 N NH2 . ARG A 132 ? 0.77751 0.48394 0.91526 0.12034  -0.03965 0.08463  131  ARG B NH2 
1044 N N   . GLU A 133 ? 0.92066 0.56817 0.90302 0.10100  -0.07989 0.08058  132  GLU B N   
1045 C CA  . GLU A 133 ? 0.99255 0.62735 0.94119 0.09789  -0.08269 0.08233  132  GLU B CA  
1046 C C   . GLU A 133 ? 0.99532 0.61751 0.91329 0.09333  -0.07357 0.06751  132  GLU B C   
1047 O O   . GLU A 133 ? 1.00438 0.61779 0.89749 0.09261  -0.06378 0.06651  132  GLU B O   
1048 C CB  . GLU A 133 ? 1.08469 0.71761 1.03119 0.09493  -0.10345 0.08854  132  GLU B CB  
1049 C CG  . GLU A 133 ? 1.21912 0.83820 1.13051 0.09063  -0.11050 0.08986  132  GLU B CG  
1050 C CD  . GLU A 133 ? 1.39485 1.01399 1.30709 0.08718  -0.13201 0.09488  132  GLU B CD  
1051 O OE1 . GLU A 133 ? 1.39649 1.01797 1.31799 0.08383  -0.13939 0.08741  132  GLU B OE1 
1052 O OE2 . GLU A 133 ? 1.44595 1.06285 1.34962 0.08777  -0.14143 0.10627  132  GLU B OE2 
1053 N N   . LYS A 134 ? 0.97366 0.59471 0.89389 0.09030  -0.07529 0.05550  133  LYS B N   
1054 C CA  . LYS A 134 ? 0.97673 0.58581 0.86967 0.08579  -0.06644 0.04073  133  LYS B CA  
1055 C C   . LYS A 134 ? 0.91284 0.52540 0.80861 0.08909  -0.04631 0.03456  133  LYS B C   
1056 O O   . LYS A 134 ? 0.89248 0.49492 0.76144 0.08645  -0.03564 0.02686  133  LYS B O   
1057 C CB  . LYS A 134 ? 0.99175 0.59847 0.88760 0.08175  -0.07386 0.03002  133  LYS B CB  
1058 C CG  . LYS A 134 ? 0.98630 0.57983 0.85451 0.07657  -0.06533 0.01429  133  LYS B CG  
1059 C CD  . LYS A 134 ? 1.19632 0.77520 1.02676 0.07240  -0.06293 0.01448  133  LYS B CD  
1060 C CE  . LYS A 134 ? 1.29404 0.86403 1.10628 0.06698  -0.08113 0.02030  133  LYS B CE  
1061 N NZ  . LYS A 134 ? 1.25644 0.80975 1.02882 0.06201  -0.07941 0.01919  133  LYS B NZ  
1062 N N   . TYR A 135 ? 0.87536 0.50210 0.80313 0.09443  -0.04088 0.03751  134  TYR B N   
1063 C CA  . TYR A 135 ? 0.85212 0.48406 0.78454 0.09768  -0.02236 0.03338  134  TYR B CA  
1064 C C   . TYR A 135 ? 0.84272 0.46992 0.75610 0.09812  -0.01367 0.03966  134  TYR B C   
1065 O O   . TYR A 135 ? 0.81887 0.44064 0.71347 0.09681  0.00044  0.03145  134  TYR B O   
1066 C CB  . TYR A 135 ? 0.78227 0.43011 0.75212 0.10310  -0.01973 0.03851  134  TYR B CB  
1067 C CG  . TYR A 135 ? 0.75599 0.41065 0.73173 0.10640  -0.00144 0.03713  134  TYR B CG  
1068 C CD1 . TYR A 135 ? 0.71999 0.37715 0.69822 0.10681  0.00964  0.02472  134  TYR B CD1 
1069 C CD2 . TYR A 135 ? 0.78479 0.44328 0.76308 0.10890  0.00498  0.04821  134  TYR B CD2 
1070 C CE1 . TYR A 135 ? 0.71786 0.38207 0.70115 0.10935  0.02602  0.02312  134  TYR B CE1 
1071 C CE2 . TYR A 135 ? 0.75224 0.41689 0.73467 0.11106  0.02209  0.04648  134  TYR B CE2 
1072 C CZ  . TYR A 135 ? 0.75963 0.42757 0.74463 0.11115  0.03224  0.03385  134  TYR B CZ  
1073 O OH  . TYR A 135 ? 0.76229 0.43733 0.75161 0.11291  0.04877  0.03163  134  TYR B OH  
1074 N N   . ASN A 136 ? 0.83834 0.46714 0.75605 0.09989  -0.02175 0.05404  135  ASN B N   
1075 C CA  . ASN A 136 ? 0.90862 0.53212 0.80839 0.10066  -0.01343 0.06090  135  ASN B CA  
1076 C C   . ASN A 136 ? 0.94415 0.55031 0.80355 0.09527  -0.01227 0.05361  135  ASN B C   
1077 O O   . ASN A 136 ? 0.92908 0.52932 0.76920 0.09459  0.00235  0.04979  135  ASN B O   
1078 C CB  . ASN A 136 ? 0.89834 0.52619 0.81101 0.10381  -0.02356 0.07800  135  ASN B CB  
1079 C CG  . ASN A 136 ? 0.84061 0.48434 0.79061 0.10899  -0.02013 0.08581  135  ASN B CG  
1080 O OD1 . ASN A 136 ? 0.83897 0.48970 0.80075 0.11065  -0.00653 0.08034  135  ASN B OD1 
1081 N ND2 . ASN A 136 ? 0.90495 0.55443 0.87378 0.11133  -0.03250 0.09860  135  ASN B ND2 
1082 N N   . ARG A 137 ? 0.98196 0.57936 0.82740 0.09081  -0.02702 0.05097  136  ARG B N   
1083 C CA  . ARG A 137 ? 0.97229 0.55183 0.77790 0.08484  -0.02623 0.04374  136  ARG B CA  
1084 C C   . ARG A 137 ? 0.94198 0.51688 0.73434 0.08244  -0.00945 0.02772  136  ARG B C   
1085 O O   . ARG A 137 ? 0.93987 0.50394 0.70460 0.08003  0.00161  0.02352  136  ARG B O   
1086 C CB  . ARG A 137 ? 1.03689 0.60862 0.83153 0.07959  -0.04448 0.04191  136  ARG B CB  
1087 C CG  . ARG A 137 ? 1.11910 0.68658 0.90485 0.07924  -0.05986 0.05575  136  ARG B CG  
1088 C CD  . ARG A 137 ? 1.18113 0.75646 0.98817 0.07895  -0.07906 0.06104  136  ARG B CD  
1089 N NE  . ARG A 137 ? 1.31636 0.89362 1.12640 0.08106  -0.09263 0.07701  136  ARG B NE  
1090 C CZ  . ARG A 137 ? 1.40511 0.99469 1.24164 0.08769  -0.09232 0.08996  136  ARG B CZ  
1091 N NH1 . ARG A 137 ? 1.40225 1.00250 1.26214 0.09253  -0.07840 0.08936  136  ARG B NH1 
1092 N NH2 . ARG A 137 ? 1.41287 1.00391 1.25228 0.08936  -0.10610 0.10392  136  ARG B NH2 
1093 N N   . ILE A 138 ? 0.93826 0.52125 0.75049 0.08320  -0.00702 0.01853  137  ILE B N   
1094 C CA  . ILE A 138 ? 0.91163 0.49069 0.71265 0.08104  0.00804  0.00281  137  ILE B CA  
1095 C C   . ILE A 138 ? 0.86983 0.45578 0.67553 0.08474  0.02643  0.00299  137  ILE B C   
1096 O O   . ILE A 138 ? 0.86687 0.44510 0.65066 0.08199  0.04013  -0.00692 137  ILE B O   
1097 C CB  . ILE A 138 ? 0.86926 0.45512 0.69128 0.08144  0.00530  -0.00631 137  ILE B CB  
1098 C CG1 . ILE A 138 ? 0.90325 0.48194 0.71937 0.07712  -0.01289 -0.00574 137  ILE B CG1 
1099 C CG2 . ILE A 138 ? 0.86790 0.44848 0.67691 0.07895  0.01965  -0.02293 137  ILE B CG2 
1100 C CD1 . ILE A 138 ? 0.95739 0.54303 0.79642 0.07798  -0.01717 -0.01206 137  ILE B CD1 
1101 N N   . ALA A 139 ? 0.85109 0.45161 0.68545 0.09050  0.02754  0.01360  138  ALA B N   
1102 C CA  . ALA A 139 ? 0.84964 0.45700 0.68849 0.09344  0.04483  0.01455  138  ALA B CA  
1103 C C   . ALA A 139 ? 0.85095 0.44594 0.65854 0.09108  0.05165  0.01791  138  ALA B C   
1104 O O   . ALA A 139 ? 0.83757 0.43039 0.63184 0.09001  0.06824  0.01084  138  ALA B O   
1105 C CB  . ALA A 139 ? 0.80284 0.42651 0.67688 0.09924  0.04345  0.02654  138  ALA B CB  
1106 N N   . ARG A 140 ? 0.86248 0.44897 0.65750 0.09012  0.03897  0.02844  139  ARG B N   
1107 C CA  . ARG A 140 ? 0.93278 0.50479 0.69459 0.08757  0.04401  0.03143  139  ARG B CA  
1108 C C   . ARG A 140 ? 0.93059 0.48668 0.65770 0.08107  0.05050  0.01638  139  ARG B C   
1109 O O   . ARG A 140 ? 0.96112 0.50914 0.66554 0.07918  0.06493  0.01228  139  ARG B O   
1110 C CB  . ARG A 140 ? 0.99413 0.56037 0.75039 0.08804  0.02699  0.04576  139  ARG B CB  
1111 C CG  . ARG A 140 ? 1.05045 0.62952 0.83519 0.09430  0.02408  0.06190  139  ARG B CG  
1112 C CD  . ARG A 140 ? 1.14085 0.71461 0.92034 0.09526  0.00779  0.07649  139  ARG B CD  
1113 N NE  . ARG A 140 ? 1.14681 0.72960 0.95144 0.09663  -0.01059 0.08209  139  ARG B NE  
1114 C CZ  . ARG A 140 ? 1.19533 0.77140 0.98937 0.09291  -0.02745 0.08102  139  ARG B CZ  
1115 N NH1 . ARG A 140 ? 1.19178 0.75099 0.94934 0.08717  -0.02925 0.07421  139  ARG B NH1 
1116 N NH2 . ARG A 140 ? 1.25839 0.84452 1.07846 0.09459  -0.04295 0.08730  139  ARG B NH2 
1117 N N   . GLU A 141 ? 0.91454 0.46533 0.63662 0.07719  0.04064  0.00777  140  GLU B N   
1118 C CA  . GLU A 141 ? 0.96476 0.49961 0.65424 0.07042  0.04693  -0.00710 140  GLU B CA  
1119 C C   . GLU A 141 ? 0.93081 0.47032 0.62229 0.07064  0.06723  -0.02005 140  GLU B C   
1120 O O   . GLU A 141 ? 0.95703 0.48443 0.61979 0.06645  0.07957  -0.02855 140  GLU B O   
1121 C CB  . GLU A 141 ? 0.95435 0.48469 0.64326 0.06640  0.03352  -0.01426 140  GLU B CB  
1122 C CG  . GLU A 141 ? 0.97229 0.49619 0.65397 0.06449  0.01302  -0.00352 140  GLU B CG  
1123 C CD  . GLU A 141 ? 1.06120 0.58456 0.74985 0.06113  -0.00099 -0.00904 140  GLU B CD  
1124 O OE1 . GLU A 141 ? 1.02806 0.55628 0.72955 0.06091  0.00464  -0.02076 140  GLU B OE1 
1125 O OE2 . GLU A 141 ? 1.05513 0.57346 0.73694 0.05880  -0.01807 -0.00109 140  GLU B OE2 
1126 N N   . TRP A 142 ? 0.91722 0.47436 0.64253 0.07542  0.07092  -0.02170 141  TRP B N   
1127 C CA  . TRP A 142 ? 0.89907 0.46325 0.62981 0.07627  0.08955  -0.03302 141  TRP B CA  
1128 C C   . TRP A 142 ? 0.87776 0.44374 0.60140 0.07773  0.10408  -0.02798 141  TRP B C   
1129 O O   . TRP A 142 ? 0.88234 0.44523 0.59133 0.07531  0.12043  -0.03867 141  TRP B O   
1130 C CB  . TRP A 142 ? 0.85256 0.43549 0.62195 0.08142  0.08890  -0.03432 141  TRP B CB  
1131 C CG  . TRP A 142 ? 0.85919 0.44012 0.63329 0.07949  0.08261  -0.04575 141  TRP B CG  
1132 C CD1 . TRP A 142 ? 0.88182 0.45041 0.64155 0.07511  0.06892  -0.04758 141  TRP B CD1 
1133 C CD2 . TRP A 142 ? 0.84178 0.43289 0.63560 0.08174  0.09029  -0.05678 141  TRP B CD2 
1134 N NE1 . TRP A 142 ? 0.89986 0.46967 0.66881 0.07431  0.06820  -0.05917 141  TRP B NE1 
1135 C CE2 . TRP A 142 ? 0.93850 0.52194 0.72868 0.07870  0.08106  -0.06491 141  TRP B CE2 
1136 C CE3 . TRP A 142 ? 0.82114 0.42715 0.63536 0.08597  0.10384  -0.06036 141  TRP B CE3 
1137 C CZ2 . TRP A 142 ? 0.85168 0.44132 0.65833 0.08029  0.08525  -0.07627 141  TRP B CZ2 
1138 C CZ3 . TRP A 142 ? 0.83446 0.44744 0.66541 0.08771  0.10726  -0.07152 141  TRP B CZ3 
1139 C CH2 . TRP A 142 ? 0.86911 0.47354 0.69622 0.08512  0.09810  -0.07926 141  TRP B CH2 
1140 N N   . THR A 143 ? 0.86718 0.43825 0.60161 0.08151  0.09896  -0.01207 142  THR B N   
1141 C CA  . THR A 143 ? 0.90328 0.47423 0.62895 0.08249  0.11268  -0.00648 142  THR B CA  
1142 C C   . THR A 143 ? 0.91022 0.46077 0.59344 0.07680  0.11902  -0.01167 142  THR B C   
1143 O O   . THR A 143 ? 0.92385 0.47181 0.59267 0.07479  0.13660  -0.01925 142  THR B O   
1144 C CB  . THR A 143 ? 0.86556 0.44332 0.60909 0.08728  0.10440  0.01208  142  THR B CB  
1145 O OG1 . THR A 143 ? 0.82000 0.41552 0.60194 0.09185  0.09885  0.01577  142  THR B OG1 
1146 C CG2 . THR A 143 ? 0.89478 0.47336 0.63218 0.08851  0.11979  0.01801  142  THR B CG2 
1147 N N   . GLN A 144 ? 0.94674 0.48234 0.60890 0.07364  0.10476  -0.00848 143  GLN B N   
1148 C CA  . GLN A 144 ? 1.04209 0.55619 0.66175 0.06767  0.10908  -0.01320 143  GLN B CA  
1149 C C   . GLN A 144 ? 1.05008 0.55661 0.65153 0.06205  0.12109  -0.03250 143  GLN B C   
1150 O O   . GLN A 144 ? 1.06983 0.56180 0.63936 0.05745  0.13269  -0.03881 143  GLN B O   
1151 C CB  . GLN A 144 ? 1.11610 0.61695 0.71916 0.06524  0.08948  -0.00574 143  GLN B CB  
1152 C CG  . GLN A 144 ? 1.15379 0.65972 0.77009 0.07048  0.07846  0.01360  143  GLN B CG  
1153 C CD  . GLN A 144 ? 1.22950 0.72553 0.83419 0.06844  0.05746  0.02099  143  GLN B CD  
1154 O OE1 . GLN A 144 ? 1.29733 0.78077 0.88027 0.06232  0.05157  0.01162  143  GLN B OE1 
1155 N NE2 . GLN A 144 ? 1.24073 0.74218 0.85940 0.07325  0.04622  0.03786  143  GLN B NE2 
1156 N N   . LYS A 145 ? 1.02488 0.54095 0.64652 0.06247  0.11941  -0.04209 144  LYS B N   
1157 C CA  . LYS A 145 ? 1.01915 0.52781 0.62478 0.05724  0.13026  -0.06059 144  LYS B CA  
1158 C C   . LYS A 145 ? 0.97350 0.49306 0.58809 0.05879  0.15110  -0.06913 144  LYS B C   
1159 O O   . LYS A 145 ? 0.98087 0.48968 0.56984 0.05380  0.16512  -0.08088 144  LYS B O   
1160 C CB  . LYS A 145 ? 1.00095 0.51354 0.62275 0.05684  0.11953  -0.06759 144  LYS B CB  
1161 C CG  . LYS A 145 ? 1.03375 0.53533 0.63677 0.05071  0.12726  -0.08610 144  LYS B CG  
1162 C CD  . LYS A 145 ? 1.04085 0.54541 0.66023 0.05063  0.11468  -0.09024 144  LYS B CD  
1163 C CE  . LYS A 145 ? 1.15375 0.64357 0.75090 0.04346  0.11974  -0.10774 144  LYS B CE  
1164 N NZ  . LYS A 145 ? 1.16700 0.66906 0.78749 0.04607  0.12980  -0.12046 144  LYS B NZ  
1165 N N   . TYR A 146 ? 0.94944 0.48991 0.59906 0.06520  0.15377  -0.06333 145  TYR B N   
1166 C CA  . TYR A 146 ? 0.93728 0.49020 0.59832 0.06648  0.17232  -0.07221 145  TYR B CA  
1167 C C   . TYR A 146 ? 0.95433 0.51474 0.61944 0.06904  0.18332  -0.06303 145  TYR B C   
1168 O O   . TYR A 146 ? 0.97831 0.54470 0.64250 0.06811  0.20076  -0.07145 145  TYR B O   
1169 C CB  . TYR A 146 ? 0.95687 0.52910 0.65557 0.07126  0.16975  -0.07581 145  TYR B CB  
1170 C CG  . TYR A 146 ? 0.89278 0.45967 0.59166 0.06921  0.16115  -0.08618 145  TYR B CG  
1171 C CD1 . TYR A 146 ? 0.92116 0.48231 0.60670 0.06518  0.17229  -0.10359 145  TYR B CD1 
1172 C CD2 . TYR A 146 ? 0.93942 0.50751 0.65310 0.07122  0.14266  -0.07896 145  TYR B CD2 
1173 C CE1 . TYR A 146 ? 0.93063 0.48615 0.61637 0.06311  0.16545  -0.11338 145  TYR B CE1 
1174 C CE2 . TYR A 146 ? 0.92089 0.48352 0.63433 0.06892  0.13553  -0.08886 145  TYR B CE2 
1175 C CZ  . TYR A 146 ? 0.92903 0.48514 0.62842 0.06494  0.14718  -0.10589 145  TYR B CZ  
1176 O OH  . TYR A 146 ? 1.11638 0.66635 0.81548 0.06252  0.14107  -0.11571 145  TYR B OH  
1177 N N   . ALA A 147 ? 0.92845 0.48920 0.59896 0.07210  0.17403  -0.04630 146  ALA B N   
1178 C CA  . ALA A 147 ? 0.92029 0.49102 0.60232 0.07538  0.18347  -0.03628 146  ALA B CA  
1179 C C   . ALA A 147 ? 0.97447 0.52950 0.62594 0.07298  0.18852  -0.02904 146  ALA B C   
1180 O O   . ALA A 147 ? 0.86876 0.42960 0.52901 0.07596  0.19311  -0.01737 146  ALA B O   
1181 C CB  . ALA A 147 ? 0.85662 0.44268 0.57469 0.08156  0.17110  -0.02221 146  ALA B CB  
1182 N N   . MET A 148 ? 1.00308 0.53759 0.61857 0.06757  0.18784  -0.03536 147  MET B N   
1183 C CA  . MET A 148 ? 1.02688 0.54416 0.61060 0.06524  0.19170  -0.02847 147  MET B CA  
1184 C C   . MET A 148 ? 1.10774 0.60980 0.65609 0.05838  0.20754  -0.04373 147  MET B C   
1185 O O   . MET A 148 ? 1.17343 0.67676 0.72082 0.05522  0.21278  -0.05933 147  MET B O   
1186 C CB  . MET A 148 ? 1.04657 0.55163 0.61997 0.06566  0.17123  -0.01702 147  MET B CB  
1187 C CG  . MET A 148 ? 1.03173 0.55164 0.63932 0.07257  0.15812  -0.00020 147  MET B CG  
1188 S SD  . MET A 148 ? 1.06990 0.57908 0.67068 0.07323  0.13241  0.01244  147  MET B SD  
1189 C CE  . MET A 148 ? 0.98711 0.51740 0.63362 0.08120  0.12142  0.02892  147  MET B CE  
1190 N N   . GLY A 149 ? 1.16939 0.65690 0.68893 0.05608  0.21614  -0.03946 148  GLY B N   
1191 C CA  . GLY A 149 ? 1.32576 0.79834 0.81111 0.04928  0.23270  -0.05374 148  GLY B CA  
1192 C C   . GLY A 149 ? 1.33509 0.82258 0.83378 0.04864  0.25273  -0.06565 148  GLY B C   
1193 O O   . GLY A 149 ? 1.38487 0.87853 0.88665 0.04987  0.26611  -0.06119 148  GLY B O   
1194 N N   . VAL A 174 ? 1.81311 1.09936 0.94985 0.20268  0.07271  -0.05249 943  VAL B N   
1195 C CA  . VAL A 174 ? 1.87985 1.17037 0.99415 0.20419  0.08831  -0.04033 943  VAL B CA  
1196 C C   . VAL A 174 ? 2.01785 1.27319 1.10749 0.21127  0.07509  -0.03684 943  VAL B C   
1197 O O   . VAL A 174 ? 2.00320 1.26119 1.08243 0.20801  0.08457  -0.02713 943  VAL B O   
1198 C CB  . VAL A 174 ? 1.87794 1.17140 0.96235 0.21809  0.10190  -0.03640 943  VAL B CB  
1199 C CG1 . VAL A 174 ? 1.94414 1.19785 0.99111 0.23969  0.08679  -0.04033 943  VAL B CG1 
1200 C CG2 . VAL A 174 ? 1.90475 1.21168 0.97361 0.21607  0.12142  -0.02364 943  VAL B CG2 
1201 N N   . ASN A 175 ? 2.17150 1.39367 1.25172 0.22112  0.05299  -0.04492 944  ASN B N   
1202 C CA  . ASN A 175 ? 2.09856 1.28511 1.15771 0.22787  0.03744  -0.04326 944  ASN B CA  
1203 C C   . ASN A 175 ? 1.98387 1.16947 1.07538 0.21334  0.02428  -0.04743 944  ASN B C   
1204 O O   . ASN A 175 ? 1.95306 1.12425 1.03715 0.21113  0.01966  -0.04228 944  ASN B O   
1205 C CB  . ASN A 175 ? 2.20795 1.35551 1.23377 0.24892  0.02036  -0.04923 944  ASN B CB  
1206 C CG  . ASN A 175 ? 2.28515 1.39415 1.28314 0.25820  0.00551  -0.04651 944  ASN B CG  
1207 O OD1 . ASN A 175 ? 2.29917 1.39944 1.26776 0.26506  0.01372  -0.03708 944  ASN B OD1 
1208 N ND2 . ASN A 175 ? 2.32512 1.41063 1.33199 0.25876  -0.01658 -0.05488 944  ASN B ND2 
1209 N N   . ALA A 176 ? 1.95343 1.15386 1.08073 0.20341  0.01810  -0.05653 945  ALA B N   
1210 C CA  . ALA A 176 ? 1.91242 1.11536 1.07334 0.18823  0.00723  -0.05992 945  ALA B CA  
1211 C C   . ALA A 176 ? 1.87439 1.10492 1.05411 0.17157  0.02343  -0.05053 945  ALA B C   
1212 O O   . ALA A 176 ? 1.86471 1.08617 1.05273 0.16415  0.01603  -0.04818 945  ALA B O   
1213 C CB  . ALA A 176 ? 1.92599 1.14375 1.12307 0.18002  0.00008  -0.07085 945  ALA B CB  
1214 N N   . ASP A 177 ? 1.87907 1.14318 1.06516 0.16577  0.04571  -0.04492 946  ASP B N   
1215 C CA  . ASP A 177 ? 1.92175 1.21364 1.12593 0.14997  0.06207  -0.03594 946  ASP B CA  
1216 C C   . ASP A 177 ? 1.86106 1.13560 1.03326 0.15612  0.06598  -0.02558 946  ASP B C   
1217 O O   . ASP A 177 ? 1.77953 1.06146 0.96524 0.14424  0.06916  -0.01996 946  ASP B O   
1218 C CB  . ASP A 177 ? 1.93776 1.26931 1.15544 0.14314  0.08474  -0.03283 946  ASP B CB  
1219 C CG  . ASP A 177 ? 1.97370 1.33136 1.23374 0.13027  0.08408  -0.04120 946  ASP B CG  
1220 O OD1 . ASP A 177 ? 1.94764 1.29167 1.22534 0.12769  0.06563  -0.04983 946  ASP B OD1 
1221 O OD2 . ASP A 177 ? 2.02897 1.42123 1.30535 0.12233  0.10211  -0.03901 946  ASP B OD2 
1222 N N   . VAL A 178 ? 1.87046 1.12120 1.00034 0.17472  0.06533  -0.02301 947  VAL B N   
1223 C CA  . VAL A 178 ? 1.87019 1.10120 0.96719 0.18205  0.06754  -0.01355 947  VAL B CA  
1224 C C   . VAL A 178 ? 1.83420 1.03150 0.92659 0.18411  0.04595  -0.01633 947  VAL B C   
1225 O O   . VAL A 178 ? 1.81680 1.00905 0.90498 0.17917  0.04743  -0.00919 947  VAL B O   
1226 C CB  . VAL A 178 ? 1.86416 1.08020 0.91773 0.20152  0.07347  -0.00999 947  VAL B CB  
1227 C CG1 . VAL A 178 ? 1.85481 1.04560 0.87205 0.21087  0.07293  -0.00108 947  VAL B CG1 
1228 C CG2 . VAL A 178 ? 1.84989 1.10179 0.90899 0.19759  0.09700  -0.00541 947  VAL B CG2 
1229 N N   . GLN A 179 ? 1.82506 1.00089 0.92174 0.18992  0.02569  -0.02699 948  GLN B N   
1230 C CA  . GLN A 179 ? 1.82177 0.96669 0.91792 0.19094  0.00412  -0.03068 948  GLN B CA  
1231 C C   . GLN A 179 ? 1.79604 0.95908 0.93569 0.17054  0.00126  -0.03232 948  GLN B C   
1232 O O   . GLN A 179 ? 1.78851 0.92938 0.93059 0.16883  -0.01449 -0.03378 948  GLN B O   
1233 C CB  . GLN A 179 ? 1.75306 0.86942 0.83983 0.20417  -0.01669 -0.04193 948  GLN B CB  
1234 C CG  . GLN A 179 ? 1.76877 0.86167 0.81142 0.22591  -0.01746 -0.04138 948  GLN B CG  
1235 C CD  . GLN A 179 ? 1.74077 0.80293 0.74444 0.23756  -0.02142 -0.03391 948  GLN B CD  
1236 O OE1 . GLN A 179 ? 1.60471 0.64434 0.60851 0.23627  -0.03665 -0.03494 948  GLN B OE1 
1237 N NE2 . GLN A 179 ? 1.78275 0.84364 0.75295 0.24906  -0.00789 -0.02635 948  GLN B NE2 
1238 N N   . LYS A 180 ? 1.79015 0.99271 0.96384 0.15521  0.01623  -0.03187 949  LYS B N   
1239 C CA  . LYS A 180 ? 1.76205 0.98482 0.97600 0.13525  0.01686  -0.03143 949  LYS B CA  
1240 C C   . LYS A 180 ? 1.72097 0.95984 0.93298 0.12647  0.03377  -0.01931 949  LYS B C   
1241 O O   . LYS A 180 ? 1.70370 0.93709 0.92757 0.11760  0.02798  -0.01665 949  LYS B O   
1242 C CB  . LYS A 180 ? 1.74105 0.99773 0.99477 0.12274  0.02314  -0.03766 949  LYS B CB  
1243 C CG  . LYS A 180 ? 1.71409 0.99148 1.01251 0.10230  0.02206  -0.03871 949  LYS B CG  
1244 C CD  . LYS A 180 ? 1.72783 1.03797 1.06303 0.09127  0.02854  -0.04484 949  LYS B CD  
1245 C CE  . LYS A 180 ? 1.77015 1.10359 1.14983 0.07044  0.02988  -0.04464 949  LYS B CE  
1246 N NZ  . LYS A 180 ? 1.74924 1.11567 1.16468 0.05953  0.03708  -0.05021 949  LYS B NZ  
1247 N N   . LEU A 181 ? 1.72549 0.98410 0.92260 0.12896  0.05466  -0.01189 950  LEU B N   
1248 C CA  . LEU A 181 ? 1.73298 1.00337 0.92168 0.12338  0.07070  0.00003  950  LEU B CA  
1249 C C   . LEU A 181 ? 1.76117 0.99566 0.91687 0.13350  0.06034  0.00482  950  LEU B C   
1250 O O   . LEU A 181 ? 1.75603 0.99368 0.91672 0.12472  0.06437  0.01185  950  LEU B O   
1251 C CB  . LEU A 181 ? 1.74611 1.03923 0.91926 0.12732  0.09320  0.00657  950  LEU B CB  
1252 C CG  . LEU A 181 ? 1.73184 1.06517 0.93656 0.11619  0.10781  0.00404  950  LEU B CG  
1253 C CD1 . LEU A 181 ? 1.80511 1.15874 0.99117 0.12039  0.13039  0.01199  950  LEU B CD1 
1254 C CD2 . LEU A 181 ? 1.63233 0.99323 0.88154 0.09477  0.11189  0.00440  950  LEU B CD2 
1255 N N   . GLN A 182 ? 1.79373 0.99370 0.91530 0.15208  0.04700  0.00120  951  GLN B N   
1256 C CA  . GLN A 182 ? 1.80440 0.96902 0.89349 0.16244  0.03654  0.00552  951  GLN B CA  
1257 C C   . GLN A 182 ? 1.82239 0.97097 0.93167 0.15438  0.01796  0.00130  951  GLN B C   
1258 O O   . GLN A 182 ? 1.83704 0.97436 0.93811 0.15189  0.01650  0.00773  951  GLN B O   
1259 C CB  . GLN A 182 ? 1.81876 0.95061 0.86693 0.18454  0.02672  0.00244  951  GLN B CB  
1260 C CG  . GLN A 182 ? 1.88261 1.02686 0.90574 0.19376  0.04541  0.00834  951  GLN B CG  
1261 C CD  . GLN A 182 ? 1.96014 1.06873 0.93535 0.21581  0.03814  0.00957  951  GLN B CD  
1262 O OE1 . GLN A 182 ? 1.95320 1.02939 0.91631 0.22629  0.01767  0.00250  951  GLN B OE1 
1263 N NE2 . GLN A 182 ? 2.00042 1.11474 0.94798 0.22321  0.05488  0.01858  951  GLN B NE2 
1264 N N   . GLN A 183 ? 1.80354 0.94979 0.93848 0.15072  0.00316  -0.00953 952  GLN B N   
1265 C CA  . GLN A 183 ? 1.84228 0.97572 1.00023 0.14182  -0.01426 -0.01384 952  GLN B CA  
1266 C C   . GLN A 183 ? 1.81919 0.98121 1.00945 0.12170  -0.00261 -0.00754 952  GLN B C   
1267 O O   . GLN A 183 ? 1.81819 0.96628 1.01205 0.11676  -0.01125 -0.00503 952  GLN B O   
1268 C CB  . GLN A 183 ? 1.81679 0.94693 0.99929 0.14047  -0.03031 -0.02655 952  GLN B CB  
1269 C CG  . GLN A 183 ? 1.87007 0.98978 1.08090 0.12995  -0.04820 -0.03160 952  GLN B CG  
1270 C CD  . GLN A 183 ? 1.93938 1.02138 1.12388 0.13832  -0.06291 -0.02887 952  GLN B CD  
1271 O OE1 . GLN A 183 ? 1.88171 0.96533 1.07958 0.12756  -0.06347 -0.02411 952  GLN B OE1 
1272 N NE2 . GLN A 183 ? 1.94591 0.99361 1.09288 0.15771  -0.07498 -0.03187 952  GLN B NE2 
1273 N N   . GLN A 184 ? 1.78292 0.98473 0.99610 0.11021  0.01728  -0.00464 953  GLN B N   
1274 C CA  . GLN A 184 ? 1.74313 0.97377 0.98606 0.09144  0.03006  0.00190  953  GLN B CA  
1275 C C   . GLN A 184 ? 1.75606 0.98113 0.97317 0.09351  0.04044  0.01373  953  GLN B C   
1276 O O   . GLN A 184 ? 1.75943 0.98337 0.98909 0.08366  0.03819  0.01782  953  GLN B O   
1277 C CB  . GLN A 184 ? 1.67195 0.94566 0.94346 0.07988  0.04881  0.00197  953  GLN B CB  
1278 C CG  . GLN A 184 ? 1.65258 0.93876 0.96400 0.07014  0.03927  -0.00856 953  GLN B CG  
1279 C CD  . GLN A 184 ? 1.66698 0.99414 1.00357 0.06063  0.05737  -0.00906 953  GLN B CD  
1280 O OE1 . GLN A 184 ? 1.68508 1.02932 1.00641 0.06344  0.07613  -0.00249 953  GLN B OE1 
1281 N NE2 . GLN A 184 ? 1.59951 0.94239 0.97482 0.04939  0.05166  -0.01686 953  GLN B NE2 
1282 N N   . LEU A 185 ? 1.77037 0.99258 0.95188 0.10600  0.05228  0.01956  954  LEU B N   
1283 C CA  . LEU A 185 ? 1.76732 0.98167 0.92170 0.10926  0.06119  0.03066  954  LEU B CA  
1284 C C   . LEU A 185 ? 1.78057 0.95535 0.91629 0.11638  0.04146  0.03020  954  LEU B C   
1285 O O   . LEU A 185 ? 1.74613 0.91866 0.88138 0.11008  0.04394  0.03733  954  LEU B O   
1286 C CB  . LEU A 185 ? 1.75342 0.96672 0.86997 0.12367  0.07462  0.03606  954  LEU B CB  
1287 C CG  . LEU A 185 ? 1.82060 1.07403 0.94964 0.11686  0.09819  0.03975  954  LEU B CG  
1288 C CD1 . LEU A 185 ? 1.88533 1.13300 0.97579 0.13327  0.10802  0.04341  954  LEU B CD1 
1289 C CD2 . LEU A 185 ? 1.84499 1.12744 0.99325 0.10077  0.11554  0.04893  954  LEU B CD2 
1290 N N   . GLN A 186 ? 1.80755 0.95124 0.92979 0.12891  0.02121  0.02148  955  GLN B N   
1291 C CA  . GLN A 186 ? 1.81120 0.91509 0.91253 0.13749  0.00175  0.02066  955  GLN B CA  
1292 C C   . GLN A 186 ? 1.80920 0.91274 0.94429 0.12276  -0.00990 0.01807  955  GLN B C   
1293 O O   . GLN A 186 ? 1.82748 0.91308 0.95209 0.12243  -0.01555 0.02301  955  GLN B O   
1294 C CB  . GLN A 186 ? 1.87581 0.94749 0.95440 0.15500  -0.01658 0.01167  955  GLN B CB  
1295 C CG  . GLN A 186 ? 1.91681 0.94528 0.97173 0.16533  -0.03778 0.01024  955  GLN B CG  
1296 C CD  . GLN A 186 ? 2.00729 1.00418 1.04152 0.18236  -0.05654 0.00080  955  GLN B CD  
1297 O OE1 . GLN A 186 ? 1.95703 0.94112 0.95597 0.19857  -0.05322 0.00223  955  GLN B OE1 
1298 N NE2 . GLN A 186 ? 2.03487 1.01890 1.09111 0.17886  -0.07644 -0.00887 955  GLN B NE2 
1299 N N   . ASP A 187 ? 1.78757 0.91062 0.96347 0.11042  -0.01363 0.01049  956  ASP B N   
1300 C CA  . ASP A 187 ? 1.77169 0.89578 0.98108 0.09586  -0.02393 0.00846  956  ASP B CA  
1301 C C   . ASP A 187 ? 1.72029 0.87418 0.95089 0.07915  -0.00620 0.01790  956  ASP B C   
1302 O O   . ASP A 187 ? 1.71725 0.86740 0.96759 0.06884  -0.01382 0.01874  956  ASP B O   
1303 C CB  . ASP A 187 ? 1.79482 0.92726 1.04067 0.08862  -0.03556 -0.00303 956  ASP B CB  
1304 C CG  . ASP A 187 ? 1.87058 1.04739 1.15032 0.07493  -0.01759 -0.00327 956  ASP B CG  
1305 O OD1 . ASP A 187 ? 1.86302 1.06616 1.14142 0.06958  0.00409  0.00538  956  ASP B OD1 
1306 O OD2 . ASP A 187 ? 1.86897 1.05428 1.17708 0.06965  -0.02552 -0.01246 956  ASP B OD2 
1307 N N   . ILE A 188 ? 1.69435 0.87758 0.92182 0.07613  0.01707  0.02503  957  ILE B N   
1308 C CA  . ILE A 188 ? 1.66694 0.87304 0.90640 0.06293  0.03353  0.03517  957  ILE B CA  
1309 C C   . ILE A 188 ? 1.64900 0.82948 0.85162 0.07198  0.03269  0.04356  957  ILE B C   
1310 O O   . ILE A 188 ? 1.62339 0.80264 0.83549 0.06296  0.03205  0.04871  957  ILE B O   
1311 C CB  . ILE A 188 ? 1.61587 0.86208 0.86485 0.05634  0.05864  0.04009  957  ILE B CB  
1312 C CG1 . ILE A 188 ? 1.59404 0.87189 0.89031 0.04074  0.06145  0.03395  957  ILE B CG1 
1313 C CG2 . ILE A 188 ? 1.55024 0.81205 0.79310 0.04965  0.07692  0.05234  957  ILE B CG2 
1314 C CD1 . ILE A 188 ? 1.54483 0.86369 0.85378 0.03293  0.08599  0.03860  957  ILE B CD1 
1315 N N   . LYS A 189 ? 1.66830 0.82650 0.82827 0.09026  0.03171  0.04483  958  LYS B N   
1316 C CA  . LYS A 189 ? 1.69543 0.82717 0.81819 0.10015  0.03002  0.05251  958  LYS B CA  
1317 C C   . LYS A 189 ? 1.67223 0.77155 0.79544 0.10095  0.00759  0.04908  958  LYS B C   
1318 O O   . LYS A 189 ? 1.67347 0.76506 0.79018 0.09744  0.00850  0.05617  958  LYS B O   
1319 C CB  . LYS A 189 ? 1.74720 0.85969 0.82495 0.12033  0.03157  0.05358  958  LYS B CB  
1320 C CG  . LYS A 189 ? 1.77849 0.91585 0.84178 0.12082  0.05657  0.06306  958  LYS B CG  
1321 C CD  . LYS A 189 ? 1.85375 0.98090 0.88347 0.13853  0.05927  0.06170  958  LYS B CD  
1322 C CE  . LYS A 189 ? 1.91343 1.04425 0.91026 0.14538  0.07731  0.07310  958  LYS B CE  
1323 N NZ  . LYS A 189 ? 1.83691 1.00728 0.85695 0.12929  0.09947  0.08077  958  LYS B NZ  
1324 N N   . GLU A 190 ? 1.70249 0.78289 0.83406 0.10526  -0.01269 0.03822  959  GLU B N   
1325 C CA  . GLU A 190 ? 1.73162 0.77974 0.86260 0.10678  -0.03486 0.03464  959  GLU B CA  
1326 C C   . GLU A 190 ? 1.68907 0.75193 0.85378 0.08831  -0.03332 0.03821  959  GLU B C   
1327 O O   . GLU A 190 ? 1.68473 0.72402 0.83999 0.08930  -0.04398 0.04084  959  GLU B O   
1328 C CB  . GLU A 190 ? 1.76913 0.79824 0.90879 0.11259  -0.05636 0.02190  959  GLU B CB  
1329 C CG  . GLU A 190 ? 1.90414 0.90928 1.00489 0.13338  -0.06213 0.01827  959  GLU B CG  
1330 C CD  . GLU A 190 ? 2.03439 1.01917 1.14290 0.13948  -0.08413 0.00563  959  GLU B CD  
1331 O OE1 . GLU A 190 ? 2.12478 1.11359 1.26884 0.12740  -0.09518 -0.00018 959  GLU B OE1 
1332 O OE2 . GLU A 190 ? 2.06429 1.02899 1.14358 0.15634  -0.09038 0.00159  959  GLU B OE2 
1333 N N   . GLN A 191 ? 1.66460 0.76569 0.86826 0.07162  -0.02027 0.03848  960  GLN B N   
1334 C CA  . GLN A 191 ? 1.63527 0.75176 0.87355 0.05364  -0.01873 0.04154  960  GLN B CA  
1335 C C   . GLN A 191 ? 1.59116 0.72657 0.82376 0.04670  0.00183  0.05403  960  GLN B C   
1336 O O   . GLN A 191 ? 1.59376 0.73128 0.84360 0.03555  0.00064  0.05804  960  GLN B O   
1337 C CB  . GLN A 191 ? 1.66165 0.80919 0.94767 0.03837  -0.01642 0.03517  960  GLN B CB  
1338 C CG  . GLN A 191 ? 1.69616 0.83008 0.98834 0.04517  -0.03371 0.02283  960  GLN B CG  
1339 C CD  . GLN A 191 ? 1.76794 0.93391 1.10677 0.03004  -0.03019 0.01701  960  GLN B CD  
1340 O OE1 . GLN A 191 ? 1.83335 1.01525 1.20704 0.01400  -0.02938 0.01823  960  GLN B OE1 
1341 N NE2 . GLN A 191 ? 1.73642 0.91240 1.07622 0.03507  -0.02770 0.01083  960  GLN B NE2 
1342 N N   . THR A 192 ? 1.57737 0.72605 0.78618 0.05306  0.02042  0.06034  961  THR B N   
1343 C CA  . THR A 192 ? 1.56111 0.73195 0.76795 0.04526  0.04144  0.07197  961  THR B CA  
1344 C C   . THR A 192 ? 1.57829 0.72721 0.73822 0.05897  0.04575  0.08042  961  THR B C   
1345 O O   . THR A 192 ? 1.56896 0.73183 0.72564 0.05278  0.06101  0.09032  961  THR B O   
1346 C CB  . THR A 192 ? 1.52496 0.73763 0.74980 0.03710  0.06369  0.07415  961  THR B CB  
1347 O OG1 . THR A 192 ? 1.52627 0.73474 0.72042 0.05189  0.06931  0.07347  961  THR B OG1 
1348 C CG2 . THR A 192 ? 1.50769 0.74237 0.77868 0.02369  0.05975  0.06590  961  THR B CG2 
1349 N N   . MET A 193 ? 1.14471 0.87860 0.87066 -0.01393 0.02221  -0.07406 962  MET B N   
1350 C CA  . MET A 193 ? 1.16072 0.90110 0.89817 -0.01875 0.02856  -0.06740 962  MET B CA  
1351 C C   . MET A 193 ? 0.97136 0.71690 0.71291 -0.01618 0.04749  -0.06324 962  MET B C   
1352 O O   . MET A 193 ? 0.89132 0.63325 0.62789 -0.01580 0.05646  -0.06488 962  MET B O   
1353 C CB  . MET A 193 ? 1.15833 0.89542 0.90127 -0.03270 0.02528  -0.06565 962  MET B CB  
1354 C CG  . MET A 193 ? 1.31918 1.05082 1.06059 -0.03681 0.00531  -0.06784 962  MET B CG  
1355 S SD  . MET A 193 ? 1.46592 1.20544 1.21527 -0.03546 -0.00549 -0.06247 962  MET B SD  
1356 C CE  . MET A 193 ? 1.46494 1.21193 1.22695 -0.05020 -0.00014 -0.05418 962  MET B CE  
1357 N N   . CYS A 194 ? 0.94641 0.70021 0.69724 -0.01448 0.05280  -0.05743 963  CYS B N   
1358 C CA  . CYS A 194 ? 0.93145 0.68877 0.68748 -0.01220 0.06996  -0.05322 963  CYS B CA  
1359 C C   . CYS A 194 ? 0.91326 0.66408 0.66930 -0.02195 0.07933  -0.05436 963  CYS B C   
1360 O O   . CYS A 194 ? 0.90678 0.65681 0.66539 -0.03147 0.07470  -0.05459 963  CYS B O   
1361 C CB  . CYS A 194 ? 0.90140 0.66873 0.66833 -0.01000 0.07335  -0.04663 963  CYS B CB  
1362 S SG  . CYS A 194 ? 0.80512 0.57420 0.57887 -0.00750 0.09391  -0.04207 963  CYS B SG  
1363 N N   . PRO A 195 ? 0.87474 0.62126 0.62788 -0.02047 0.09173  -0.05477 964  PRO B N   
1364 C CA  . PRO A 195 ? 0.88324 0.62305 0.63532 -0.02992 0.10025  -0.05653 964  PRO B CA  
1365 C C   . PRO A 195 ? 0.87764 0.62098 0.63844 -0.03253 0.11084  -0.05319 964  PRO B C   
1366 O O   . PRO A 195 ? 0.86227 0.60147 0.62230 -0.04047 0.11736  -0.05511 964  PRO B O   
1367 C CB  . PRO A 195 ? 0.85737 0.59106 0.60249 -0.02675 0.10811  -0.05775 964  PRO B CB  
1368 C CG  . PRO A 195 ? 0.82627 0.56611 0.57427 -0.01549 0.11040  -0.05371 964  PRO B CG  
1369 C CD  . PRO A 195 ? 0.89316 0.64105 0.64366 -0.01081 0.09778  -0.05319 964  PRO B CD  
1370 N N   . VAL A 196 ? 0.87967 0.63128 0.64839 -0.02563 0.11302  -0.04836 965  VAL B N   
1371 C CA  . VAL A 196 ? 0.86965 0.62600 0.64667 -0.02634 0.12332  -0.04511 965  VAL B CA  
1372 C C   . VAL A 196 ? 0.90937 0.67561 0.69265 -0.03270 0.11605  -0.04258 965  VAL B C   
1373 O O   . VAL A 196 ? 0.99383 0.76224 0.77939 -0.03983 0.12087  -0.04291 965  VAL B O   
1374 C CB  . VAL A 196 ? 0.88104 0.64186 0.66418 -0.01526 0.13074  -0.04020 965  VAL B CB  
1375 C CG1 . VAL A 196 ? 0.88749 0.65376 0.67916 -0.01446 0.14096  -0.03705 965  VAL B CG1 
1376 C CG2 . VAL A 196 ? 0.86615 0.61781 0.64404 -0.01044 0.13786  -0.04130 965  VAL B CG2 
1377 N N   . CYS A 197 ? 0.90397 0.67720 0.69001 -0.03058 0.10376  -0.03967 966  CYS B N   
1378 C CA  . CYS A 197 ? 0.89866 0.68209 0.69133 -0.03730 0.09512  -0.03561 966  CYS B CA  
1379 C C   . CYS A 197 ? 0.93013 0.70871 0.71804 -0.04735 0.08153  -0.03874 966  CYS B C   
1380 O O   . CYS A 197 ? 0.91607 0.70214 0.70934 -0.05626 0.07628  -0.03530 966  CYS B O   
1381 C CB  . CYS A 197 ? 0.89990 0.69318 0.69847 -0.03078 0.08783  -0.03001 966  CYS B CB  
1382 S SG  . CYS A 197 ? 0.98925 0.77570 0.77933 -0.02417 0.07425  -0.03398 966  CYS B SG  
1383 N N   . LEU A 198 ? 0.96378 0.73100 0.74215 -0.04606 0.07585  -0.04459 967  LEU B N   
1384 C CA  . LEU A 198 ? 1.01182 0.77268 0.78507 -0.05372 0.06149  -0.04799 967  LEU B CA  
1385 C C   . LEU A 198 ? 1.05194 0.81775 0.82936 -0.05583 0.04442  -0.04453 967  LEU B C   
1386 O O   . LEU A 198 ? 1.04266 0.80434 0.81869 -0.06423 0.03124  -0.04552 967  LEU B O   
1387 C CB  . LEU A 198 ? 1.01008 0.76958 0.78356 -0.06553 0.06557  -0.04890 967  LEU B CB  
1388 C CG  . LEU A 198 ? 0.97057 0.72541 0.74046 -0.06533 0.08247  -0.05194 967  LEU B CG  
1389 C CD1 . LEU A 198 ? 0.94858 0.71256 0.72615 -0.06491 0.09562  -0.04814 967  LEU B CD1 
1390 C CD2 . LEU A 198 ? 1.01297 0.76155 0.77768 -0.07585 0.08060  -0.05561 967  LEU B CD2 
1391 N N   . ASP A 199 ? 1.07436 0.84810 0.85656 -0.04821 0.04373  -0.04036 968  ASP B N   
1392 C CA  . ASP A 199 ? 1.08485 0.86610 0.87300 -0.05053 0.02980  -0.03501 968  ASP B CA  
1393 C C   . ASP A 199 ? 1.10244 0.88046 0.88548 -0.04121 0.01879  -0.03754 968  ASP B C   
1394 O O   . ASP A 199 ? 1.13641 0.90927 0.91648 -0.04436 0.00100  -0.03917 968  ASP B O   
1395 C CB  . ASP A 199 ? 1.07254 0.86984 0.87227 -0.05029 0.03961  -0.02631 968  ASP B CB  
1396 C CG  . ASP A 199 ? 1.12522 0.93313 0.93241 -0.05409 0.02585  -0.01873 968  ASP B CG  
1397 O OD1 . ASP A 199 ? 1.04679 0.84795 0.85025 -0.05799 0.00777  -0.02043 968  ASP B OD1 
1398 O OD2 . ASP A 199 ? 1.16907 0.99212 0.98589 -0.05329 0.03282  -0.01077 968  ASP B OD2 
1399 N N   . ARG A 200 ? 1.07550 0.85673 0.85755 -0.02977 0.02821  -0.03773 969  ARG B N   
1400 C CA  . ARG A 200 ? 1.05954 0.83959 0.83586 -0.02012 0.01862  -0.04061 969  ARG B CA  
1401 C C   . ARG A 200 ? 1.05438 0.82511 0.81936 -0.01335 0.02076  -0.04858 969  ARG B C   
1402 O O   . ARG A 200 ? 1.01705 0.78322 0.77971 -0.01528 0.03217  -0.05058 969  ARG B O   
1403 C CB  . ARG A 200 ? 1.00378 0.79658 0.78710 -0.01171 0.02578  -0.03429 969  ARG B CB  
1404 C CG  . ARG A 200 ? 1.01634 0.82080 0.81083 -0.01747 0.02282  -0.02549 969  ARG B CG  
1405 C CD  . ARG A 200 ? 1.00096 0.81858 0.80411 -0.00992 0.03598  -0.01836 969  ARG B CD  
1406 N NE  . ARG A 200 ? 0.98363 0.80068 0.78953 -0.00867 0.05480  -0.01798 969  ARG B NE  
1407 C CZ  . ARG A 200 ? 1.02625 0.84875 0.83945 -0.01482 0.06315  -0.01383 969  ARG B CZ  
1408 N NH1 . ARG A 200 ? 1.04213 0.87361 0.86175 -0.02298 0.05511  -0.00824 969  ARG B NH1 
1409 N NH2 . ARG A 200 ? 1.00985 0.82929 0.82370 -0.01270 0.07948  -0.01514 969  ARG B NH2 
1410 N N   . LEU A 201 ? 1.07352 0.84332 0.83143 -0.00449 0.01037  -0.05262 970  LEU B N   
1411 C CA  . LEU A 201 ? 1.03850 0.80302 0.78550 0.00337  0.01156  -0.05946 970  LEU B CA  
1412 C C   . LEU A 201 ? 0.96560 0.73922 0.71463 0.01265  0.02651  -0.05595 970  LEU B C   
1413 O O   . LEU A 201 ? 0.93854 0.72220 0.69560 0.01608  0.03121  -0.04970 970  LEU B O   
1414 C CB  . LEU A 201 ? 1.07503 0.83568 0.81256 0.01011  -0.00648 -0.06607 970  LEU B CB  
1415 C CG  . LEU A 201 ? 1.13813 0.88708 0.87305 0.00122  -0.02362 -0.06985 970  LEU B CG  
1416 C CD1 . LEU A 201 ? 1.13665 0.88329 0.86674 0.00638  -0.04308 -0.07349 970  LEU B CD1 
1417 C CD2 . LEU A 201 ? 1.18004 0.91819 0.90627 -0.00044 -0.02415 -0.07653 970  LEU B CD2 
1418 N N   . LYS A 202 ? 0.95752 0.72809 0.69947 0.01652  0.03331  -0.05930 971  LYS B N   
1419 C CA  . LYS A 202 ? 0.94148 0.71984 0.68492 0.02448  0.04670  -0.05539 971  LYS B CA  
1420 C C   . LYS A 202 ? 0.94403 0.73326 0.68523 0.03640  0.03996  -0.05503 971  LYS B C   
1421 O O   . LYS A 202 ? 1.01671 0.80652 0.74777 0.04338  0.03138  -0.06076 971  LYS B O   
1422 C CB  . LYS A 202 ? 0.93082 0.70391 0.66651 0.02455  0.05319  -0.05848 971  LYS B CB  
1423 C CG  . LYS A 202 ? 0.95032 0.71298 0.68698 0.01279  0.06020  -0.05930 971  LYS B CG  
1424 C CD  . LYS A 202 ? 0.95375 0.71280 0.68272 0.01332  0.06680  -0.06119 971  LYS B CD  
1425 C CE  . LYS A 202 ? 1.03180 0.78717 0.74964 0.01528  0.05451  -0.06816 971  LYS B CE  
1426 N NZ  . LYS A 202 ? 1.06523 0.82089 0.77542 0.01743  0.06039  -0.06879 971  LYS B NZ  
1427 N N   . ASN A 203 ? 0.92674 0.72581 0.67721 0.03933  0.04372  -0.04832 972  ASN B N   
1428 C CA  . ASN A 203 ? 0.91235 0.72395 0.66183 0.05038  0.03868  -0.04685 972  ASN B CA  
1429 C C   . ASN A 203 ? 0.90415 0.72675 0.66020 0.05683  0.05301  -0.03912 972  ASN B C   
1430 O O   . ASN A 203 ? 0.88885 0.72418 0.64940 0.06390  0.05218  -0.03441 972  ASN B O   
1431 C CB  . ASN A 203 ? 0.91962 0.73490 0.67405 0.04869  0.02796  -0.04498 972  ASN B CB  
1432 C CG  . ASN A 203 ? 0.88909 0.70826 0.65701 0.04274  0.03762  -0.03637 972  ASN B CG  
1433 O OD1 . ASN A 203 ? 0.91268 0.72713 0.68493 0.03757  0.05006  -0.03417 972  ASN B OD1 
1434 N ND2 . ASN A 203 ? 0.86438 0.69218 0.63855 0.04331  0.03147  -0.03168 972  ASN B ND2 
1435 N N   . MET A 204 ? 0.90718 0.72459 0.66448 0.05372  0.06577  -0.03719 973  MET B N   
1436 C CA  . MET A 204 ? 0.91024 0.73538 0.67341 0.05895  0.07860  -0.02967 973  MET B CA  
1437 C C   . MET A 204 ? 0.91772 0.73577 0.67493 0.05661  0.08559  -0.03122 973  MET B C   
1438 O O   . MET A 204 ? 0.92069 0.72584 0.67707 0.04759  0.08975  -0.03393 973  MET B O   
1439 C CB  . MET A 204 ? 0.90761 0.73265 0.68394 0.05564  0.08921  -0.02242 973  MET B CB  
1440 C CG  . MET A 204 ? 0.88577 0.71306 0.66830 0.05901  0.10301  -0.01518 973  MET B CG  
1441 S SD  . MET A 204 ? 1.09030 0.91617 0.88763 0.05702  0.11534  -0.00770 973  MET B SD  
1442 C CE  . MET A 204 ? 1.02239 0.86575 0.82682 0.06379  0.10778  -0.00246 973  MET B CE  
1443 N N   . ILE A 205 ? 0.89193 0.71997 0.64562 0.06435  0.08720  -0.02851 974  ILE B N   
1444 C CA  . ILE A 205 ? 0.89695 0.72116 0.64385 0.06266  0.09175  -0.02923 974  ILE B CA  
1445 C C   . ILE A 205 ? 0.90830 0.73843 0.66232 0.06510  0.10341  -0.01944 974  ILE B C   
1446 O O   . ILE A 205 ? 0.92591 0.76935 0.68661 0.07238  0.10452  -0.01284 974  ILE B O   
1447 C CB  . ILE A 205 ? 0.94543 0.77760 0.68000 0.06965  0.08126  -0.03484 974  ILE B CB  
1448 C CG1 . ILE A 205 ? 0.92777 0.75070 0.65559 0.06674  0.06859  -0.04472 974  ILE B CG1 
1449 C CG2 . ILE A 205 ? 0.95102 0.78224 0.67916 0.06804  0.08640  -0.03386 974  ILE B CG2 
1450 C CD1 . ILE A 205 ? 0.90993 0.71569 0.63618 0.05496  0.07069  -0.04876 974  ILE B CD1 
1451 N N   . PHE A 206 ? 0.90908 0.72850 0.66217 0.05827  0.11170  -0.01816 975  PHE B N   
1452 C CA  . PHE A 206 ? 0.94498 0.76685 0.70347 0.05907  0.12144  -0.00900 975  PHE B CA  
1453 C C   . PHE A 206 ? 0.95338 0.78439 0.70350 0.06182  0.11944  -0.00702 975  PHE B C   
1454 O O   . PHE A 206 ? 0.93480 0.76583 0.67435 0.06146  0.11261  -0.01389 975  PHE B O   
1455 C CB  . PHE A 206 ? 0.92533 0.72863 0.68812 0.04959  0.13155  -0.00854 975  PHE B CB  
1456 C CG  . PHE A 206 ? 0.92316 0.71721 0.69072 0.04530  0.13225  -0.01314 975  PHE B CG  
1457 C CD1 . PHE A 206 ? 0.93104 0.73332 0.70726 0.05065  0.13114  -0.01008 975  PHE B CD1 
1458 C CD2 . PHE A 206 ? 0.88953 0.66866 0.65329 0.03571  0.13410  -0.01959 975  PHE B CD2 
1459 C CE1 . PHE A 206 ? 0.92439 0.72108 0.70535 0.04667  0.13156  -0.01296 975  PHE B CE1 
1460 C CE2 . PHE A 206 ? 0.88077 0.65466 0.64937 0.03177  0.13467  -0.02270 975  PHE B CE2 
1461 C CZ  . PHE A 206 ? 0.89365 0.67667 0.67092 0.03729  0.13337  -0.01913 975  PHE B CZ  
1462 N N   . LEU A 207 ? 0.96118 0.80041 0.71665 0.06444  0.12542  0.00325  976  LEU B N   
1463 C CA  . LEU A 207 ? 0.97881 0.83179 0.72806 0.06774  0.12372  0.00797  976  LEU B CA  
1464 C C   . LEU A 207 ? 0.96889 0.80962 0.71001 0.05882  0.12583  0.00513  976  LEU B C   
1465 O O   . LEU A 207 ? 0.95944 0.81208 0.69289 0.06131  0.12266  0.00699  976  LEU B O   
1466 C CB  . LEU A 207 ? 0.99660 0.86106 0.75551 0.07108  0.12943  0.02149  976  LEU B CB  
1467 C CG  . LEU A 207 ? 0.98550 0.87091 0.75026 0.08200  0.12561  0.02599  976  LEU B CG  
1468 C CD1 . LEU A 207 ? 1.00089 0.89794 0.77610 0.08443  0.13100  0.04040  976  LEU B CD1 
1469 C CD2 . LEU A 207 ? 0.95606 0.86018 0.71008 0.09051  0.11587  0.02103  976  LEU B CD2 
1470 N N   . CYS A 208 ? 0.98522 0.80414 0.72788 0.04875  0.13128  0.00115  977  CYS B N   
1471 C CA  . CYS A 208 ? 1.01287 0.81945 0.74778 0.03929  0.13327  -0.00199 977  CYS B CA  
1472 C C   . CYS A 208 ? 0.98310 0.78977 0.70732 0.03905  0.12500  -0.01202 977  CYS B C   
1473 O O   . CYS A 208 ? 0.98631 0.78547 0.70335 0.03187  0.12564  -0.01454 977  CYS B O   
1474 C CB  . CYS A 208 ? 0.98194 0.76597 0.72109 0.02910  0.14122  -0.00426 977  CYS B CB  
1475 S SG  . CYS A 208 ? 0.96803 0.74232 0.71011 0.02743  0.13923  -0.01410 977  CYS B SG  
1476 N N   . GLY A 209 ? 0.93553 0.74920 0.65868 0.04620  0.11687  -0.01773 978  GLY B N   
1477 C CA  . GLY A 209 ? 0.97818 0.79080 0.69158 0.04698  0.10741  -0.02730 978  GLY B CA  
1478 C C   . GLY A 209 ? 1.01690 0.81396 0.73173 0.04023  0.10456  -0.03540 978  GLY B C   
1479 O O   . GLY A 209 ? 1.07149 0.86738 0.77968 0.04162  0.09467  -0.04317 978  GLY B O   
1480 N N   . HIS A 210 ? 0.96230 0.74788 0.68550 0.03315  0.11246  -0.03356 979  HIS B N   
1481 C CA  . HIS A 210 ? 0.94267 0.71683 0.66834 0.02657  0.11021  -0.03970 979  HIS B CA  
1482 C C   . HIS A 210 ? 0.90975 0.69014 0.64352 0.03226  0.10732  -0.03836 979  HIS B C   
1483 O O   . HIS A 210 ? 0.91326 0.70531 0.65147 0.04062  0.10865  -0.03255 979  HIS B O   
1484 C CB  . HIS A 210 ? 0.94620 0.70551 0.67520 0.01557  0.12038  -0.03935 979  HIS B CB  
1485 C CG  . HIS A 210 ? 0.93675 0.68958 0.65807 0.00877  0.12360  -0.03996 979  HIS B CG  
1486 N ND1 . HIS A 210 ? 0.91378 0.66222 0.63640 0.00561  0.13303  -0.03416 979  HIS B ND1 
1487 C CD2 . HIS A 210 ? 0.92933 0.67964 0.64165 0.00454  0.11804  -0.04506 979  HIS B CD2 
1488 C CE1 . HIS A 210 ? 0.91379 0.65782 0.62835 -0.00089 0.13328  -0.03552 979  HIS B CE1 
1489 N NE2 . HIS A 210 ? 0.87189 0.61753 0.58028 -0.00140 0.12467  -0.04204 979  HIS B NE2 
1490 N N   . GLY A 211 ? 0.85933 0.63326 0.59508 0.02726  0.10257  -0.04314 980  GLY B N   
1491 C CA  . GLY A 211 ? 0.87986 0.65993 0.62275 0.03127  0.09826  -0.04182 980  GLY B CA  
1492 C C   . GLY A 211 ? 0.88145 0.65342 0.62966 0.02242  0.09854  -0.04378 980  GLY B C   
1493 O O   . GLY A 211 ? 0.89589 0.65780 0.64115 0.01328  0.10006  -0.04748 980  GLY B O   
1494 N N   . THR A 212 ? 0.87923 0.65774 0.63570 0.02523  0.09702  -0.04046 981  THR B N   
1495 C CA  . THR A 212 ? 0.87333 0.64928 0.63625 0.01816  0.09614  -0.04048 981  THR B CA  
1496 C C   . THR A 212 ? 0.90464 0.68953 0.67043 0.02208  0.08455  -0.03947 981  THR B C   
1497 O O   . THR A 212 ? 0.91647 0.70826 0.67835 0.03036  0.07746  -0.03996 981  THR B O   
1498 C CB  . THR A 212 ? 0.93542 0.71140 0.70810 0.01746  0.10981  -0.03500 981  THR B CB  
1499 O OG1 . THR A 212 ? 0.92747 0.71432 0.70688 0.02682  0.11153  -0.02875 981  THR B OG1 
1500 C CG2 . THR A 212 ? 0.91209 0.67857 0.68190 0.01499  0.12130  -0.03540 981  THR B CG2 
1501 N N   . CYS A 213 ? 0.88669 0.67288 0.65947 0.01627  0.08264  -0.03749 982  CYS B N   
1502 C CA  . CYS A 213 ? 0.92634 0.72288 0.70446 0.02024  0.07454  -0.03374 982  CYS B CA  
1503 C C   . CYS A 213 ? 0.93545 0.74185 0.72276 0.02778  0.08545  -0.02604 982  CYS B C   
1504 O O   . CYS A 213 ? 0.93528 0.73871 0.72595 0.02856  0.09905  -0.02362 982  CYS B O   
1505 C CB  . CYS A 213 ? 0.92643 0.72328 0.70942 0.01095  0.06756  -0.03265 982  CYS B CB  
1506 S SG  . CYS A 213 ? 1.00360 0.80569 0.79883 0.00641  0.08177  -0.02586 982  CYS B SG  
1507 N N   . GLN A 214 ? 0.91699 0.73464 0.70811 0.03352  0.07871  -0.02218 983  GLN B N   
1508 C CA  . GLN A 214 ? 0.95443 0.78288 0.75498 0.04104  0.08803  -0.01407 983  GLN B CA  
1509 C C   . GLN A 214 ? 0.96757 0.79689 0.77863 0.03731  0.09904  -0.00882 983  GLN B C   
1510 O O   . GLN A 214 ? 0.98815 0.81887 0.80558 0.04210  0.11173  -0.00405 983  GLN B O   
1511 C CB  . GLN A 214 ? 0.98463 0.82597 0.78717 0.04675  0.07759  -0.01088 983  GLN B CB  
1512 C CG  . GLN A 214 ? 1.02124 0.87563 0.83469 0.05426  0.08645  -0.00141 983  GLN B CG  
1513 C CD  . GLN A 214 ? 1.02142 0.88965 0.83559 0.06044  0.07614  0.00155  983  GLN B CD  
1514 O OE1 . GLN A 214 ? 0.96684 0.83498 0.77565 0.05762  0.06161  -0.00242 983  GLN B OE1 
1515 N NE2 . GLN A 214 ? 1.02691 0.90679 0.84776 0.06876  0.08319  0.00874  983  GLN B NE2 
1516 N N   . LEU A 215 ? 0.95425 0.78317 0.76718 0.02897  0.09380  -0.00947 984  LEU B N   
1517 C CA  . LEU A 215 ? 0.95500 0.78860 0.77776 0.02589  0.10280  -0.00428 984  LEU B CA  
1518 C C   . LEU A 215 ? 0.95568 0.77906 0.77788 0.02473  0.11727  -0.00679 984  LEU B C   
1519 O O   . LEU A 215 ? 0.95949 0.78567 0.78929 0.02941  0.12937  -0.00227 984  LEU B O   
1520 C CB  . LEU A 215 ? 0.95923 0.79554 0.78275 0.01599  0.09223  -0.00446 984  LEU B CB  
1521 C CG  . LEU A 215 ? 0.99320 0.84497 0.82817 0.01517  0.09257  0.00447  984  LEU B CG  
1522 C CD1 . LEU A 215 ? 0.94378 0.80671 0.78374 0.02424  0.09099  0.01063  984  LEU B CD1 
1523 C CD2 . LEU A 215 ? 1.04796 0.90285 0.88284 0.00436  0.07843  0.00512  984  LEU B CD2 
1524 N N   . CYS A 216 ? 0.96419 0.77514 0.77715 0.01859  0.11571  -0.01415 985  CYS B N   
1525 C CA  . CYS A 216 ? 0.96017 0.76011 0.77099 0.01652  0.12816  -0.01727 985  CYS B CA  
1526 C C   . CYS A 216 ? 0.98890 0.78404 0.79843 0.02442  0.13588  -0.01604 985  CYS B C   
1527 O O   . CYS A 216 ? 1.01433 0.80384 0.82719 0.02661  0.14804  -0.01469 985  CYS B O   
1528 C CB  . CYS A 216 ? 0.94287 0.73236 0.74426 0.00696  0.12317  -0.02471 985  CYS B CB  
1529 S SG  . CYS A 216 ? 0.91700 0.71176 0.72018 -0.00441 0.11266  -0.02530 985  CYS B SG  
1530 N N   . GLY A 217 ? 0.98410 0.78189 0.78879 0.02894  0.12837  -0.01625 986  GLY B N   
1531 C CA  . GLY A 217 ? 0.97197 0.76752 0.77524 0.03542  0.13433  -0.01405 986  GLY B CA  
1532 C C   . GLY A 217 ? 1.00174 0.80410 0.81577 0.04343  0.14282  -0.00591 986  GLY B C   
1533 O O   . GLY A 217 ? 0.98980 0.78621 0.80528 0.04647  0.15162  -0.00331 986  GLY B O   
1534 N N   . ASP A 218 ? 1.00639 0.82124 0.82833 0.04675  0.13970  -0.00112 987  ASP B N   
1535 C CA  . ASP A 218 ? 1.01028 0.83228 0.84343 0.05454  0.14811  0.00720  987  ASP B CA  
1536 C C   . ASP A 218 ? 1.01593 0.82929 0.85441 0.05361  0.16069  0.00754  987  ASP B C   
1537 O O   . ASP A 218 ? 0.98538 0.80054 0.83248 0.06060  0.16907  0.01371  987  ASP B O   
1538 C CB  . ASP A 218 ? 1.02271 0.86139 0.86300 0.05784  0.14150  0.01272  987  ASP B CB  
1539 C CG  . ASP A 218 ? 1.02925 0.87797 0.86613 0.06265  0.13140  0.01406  987  ASP B CG  
1540 O OD1 . ASP A 218 ? 1.02526 0.87212 0.85808 0.06653  0.13282  0.01403  987  ASP B OD1 
1541 O OD2 . ASP A 218 ? 1.06410 0.92341 0.90217 0.06251  0.12163  0.01537  987  ASP B OD2 
1542 N N   . ARG A 219 ? 1.02559 0.83002 0.85916 0.04566  0.16199  0.00103  988  ARG B N   
1543 C CA  . ARG A 219 ? 1.01318 0.80991 0.85025 0.04529  0.17356  -0.00006 988  ARG B CA  
1544 C C   . ARG A 219 ? 1.03895 0.81729 0.86911 0.04291  0.18036  -0.00494 988  ARG B C   
1545 O O   . ARG A 219 ? 1.08378 0.85289 0.91355 0.04094  0.18855  -0.00854 988  ARG B O   
1546 C CB  . ARG A 219 ? 1.04521 0.84624 0.88197 0.03804  0.17145  -0.00337 988  ARG B CB  
1547 C CG  . ARG A 219 ? 1.08475 0.90448 0.93064 0.04029  0.16706  0.00331  988  ARG B CG  
1548 C CD  . ARG A 219 ? 1.12915 0.95495 0.98273 0.04251  0.17658  0.00577  988  ARG B CD  
1549 N NE  . ARG A 219 ? 1.18213 1.01112 1.03308 0.03342  0.17420  0.00208  988  ARG B NE  
1550 C CZ  . ARG A 219 ? 1.25910 1.10311 1.11343 0.02821  0.16503  0.00591  988  ARG B CZ  
1551 N NH1 . ARG A 219 ? 1.30166 1.15797 1.16131 0.03104  0.15700  0.01277  988  ARG B NH1 
1552 N NH2 . ARG A 219 ? 1.16456 1.01213 1.01725 0.01963  0.16359  0.00343  988  ARG B NH2 
1553 N N   . MET A 220 ? 1.05641 0.83010 0.88066 0.04290  0.17676  -0.00510 989  MET B N   
1554 C CA  . MET A 220 ? 1.07077 0.82795 0.88807 0.03933  0.18179  -0.00866 989  MET B CA  
1555 C C   . MET A 220 ? 1.04366 0.80036 0.86322 0.04538  0.18321  -0.00211 989  MET B C   
1556 O O   . MET A 220 ? 1.01641 0.78679 0.83940 0.05087  0.17770  0.00337  989  MET B O   
1557 C CB  . MET A 220 ? 1.09993 0.85190 0.90551 0.03024  0.17513  -0.01570 989  MET B CB  
1558 C CG  . MET A 220 ? 1.05034 0.80637 0.85365 0.02339  0.16976  -0.02084 989  MET B CG  
1559 S SD  . MET A 220 ? 1.05547 0.80359 0.84547 0.01344  0.16239  -0.02833 989  MET B SD  
1560 C CE  . MET A 220 ? 1.01371 0.74377 0.79916 0.00997  0.17379  -0.03081 989  MET B CE  
1561 N N   . SER A 221 ? 1.04460 0.78590 0.86222 0.04400  0.19015  -0.00234 990  SER B N   
1562 C CA  . SER A 221 ? 1.02212 0.76203 0.84132 0.04759  0.19075  0.00465  990  SER B CA  
1563 C C   . SER A 221 ? 1.01575 0.74847 0.82423 0.04068  0.18763  0.00216  990  SER B C   
1564 O O   . SER A 221 ? 1.00020 0.73680 0.80907 0.04294  0.18589  0.00886  990  SER B O   
1565 C CB  . SER A 221 ? 1.04539 0.77307 0.87222 0.05198  0.20003  0.00875  990  SER B CB  
1566 O OG  . SER A 221 ? 1.04257 0.75095 0.86393 0.04639  0.20598  0.00143  990  SER B OG  
1567 N N   . GLU A 222 ? 1.04358 0.76762 0.84300 0.03225  0.18687  -0.00635 991  GLU B N   
1568 C CA  . GLU A 222 ? 1.04407 0.76232 0.83314 0.02533  0.18389  -0.00860 991  GLU B CA  
1569 C C   . GLU A 222 ? 1.02677 0.75041 0.80793 0.02004  0.17657  -0.01582 991  GLU B C   
1570 O O   . GLU A 222 ? 1.01010 0.73585 0.79294 0.01859  0.17565  -0.02036 991  GLU B O   
1571 C CB  . GLU A 222 ? 1.08244 0.78039 0.86785 0.01912  0.19105  -0.01126 991  GLU B CB  
1572 C CG  . GLU A 222 ? 1.14765 0.83647 0.93577 0.01848  0.19760  -0.01715 991  GLU B CG  
1573 C CD  . GLU A 222 ? 1.25338 0.92122 1.03882 0.01490  0.20489  -0.01941 991  GLU B CD  
1574 O OE1 . GLU A 222 ? 1.28284 0.94225 1.06193 0.00932  0.20364  -0.01789 991  GLU B OE1 
1575 O OE2 . GLU A 222 ? 1.32125 0.98144 1.11065 0.01793  0.21148  -0.02259 991  GLU B OE2 
1576 N N   . CYS A 223 ? 1.00416 0.73114 0.77719 0.01747  0.17086  -0.01606 992  CYS B N   
1577 C CA  . CYS A 223 ? 0.97189 0.70322 0.73722 0.01327  0.16280  -0.02264 992  CYS B CA  
1578 C C   . CYS A 223 ? 0.95236 0.67087 0.71342 0.00345  0.16600  -0.03008 992  CYS B C   
1579 O O   . CYS A 223 ? 0.96362 0.66909 0.72163 -0.00196 0.17258  -0.03094 992  CYS B O   
1580 C CB  . CYS A 223 ? 0.97531 0.71247 0.73243 0.01344  0.15719  -0.02113 992  CYS B CB  
1581 S SG  . CYS A 223 ? 0.94791 0.68652 0.69408 0.00799  0.14763  -0.02949 992  CYS B SG  
1582 N N   . PRO A 224 ? 0.94430 0.66644 0.70510 0.00047  0.16107  -0.03516 993  PRO B N   
1583 C CA  . PRO A 224 ? 0.94365 0.65648 0.70142 -0.00894 0.16426  -0.04135 993  PRO B CA  
1584 C C   . PRO A 224 ? 0.92732 0.63343 0.67465 -0.01760 0.16172  -0.04560 993  PRO B C   
1585 O O   . PRO A 224 ? 0.88190 0.58021 0.62629 -0.02602 0.16512  -0.05036 993  PRO B O   
1586 C CB  . PRO A 224 ? 0.91905 0.64134 0.68109 -0.00922 0.15789  -0.04318 993  PRO B CB  
1587 C CG  . PRO A 224 ? 0.92223 0.65584 0.68454 -0.00232 0.14812  -0.04046 993  PRO B CG  
1588 C CD  . PRO A 224 ? 0.93164 0.66705 0.69624 0.00563  0.15251  -0.03451 993  PRO B CD  
1589 N N   . ILE A 225 ? 0.94610 0.65610 0.68777 -0.01554 0.15646  -0.04365 994  ILE B N   
1590 C CA  . ILE A 225 ? 0.94552 0.65161 0.67733 -0.02288 0.15317  -0.04696 994  ILE B CA  
1591 C C   . ILE A 225 ? 0.97951 0.67910 0.70703 -0.02491 0.15882  -0.04308 994  ILE B C   
1592 O O   . ILE A 225 ? 1.02593 0.71601 0.74736 -0.03400 0.16185  -0.04575 994  ILE B O   
1593 C CB  . ILE A 225 ? 0.95681 0.67335 0.68405 -0.01922 0.14136  -0.04844 994  ILE B CB  
1594 C CG1 . ILE A 225 ? 0.95537 0.67475 0.68548 -0.02094 0.13417  -0.05284 994  ILE B CG1 
1595 C CG2 . ILE A 225 ? 0.93567 0.65026 0.65280 -0.02416 0.13860  -0.04997 994  ILE B CG2 
1596 C CD1 . ILE A 225 ? 1.03403 0.76295 0.77140 -0.01205 0.13031  -0.05010 994  ILE B CD1 
1597 N N   . CYS A 226 ? 0.96270 0.66806 0.69354 -0.01719 0.15983  -0.03605 995  CYS B N   
1598 C CA  . CYS A 226 ? 0.97072 0.67087 0.69852 -0.01973 0.16416  -0.03058 995  CYS B CA  
1599 C C   . CYS A 226 ? 0.97698 0.66815 0.71219 -0.01766 0.17220  -0.02601 995  CYS B C   
1600 O O   . CYS A 226 ? 0.98619 0.66965 0.71950 -0.02121 0.17570  -0.02127 995  CYS B O   
1601 C CB  . CYS A 226 ? 0.98155 0.69692 0.70647 -0.01346 0.15826  -0.02440 995  CYS B CB  
1602 S SG  . CYS A 226 ? 1.01329 0.74367 0.74793 -0.00003 0.15669  -0.01720 995  CYS B SG  
1603 N N   . ARG A 227 ? 0.99044 0.68247 0.73412 -0.01202 0.17459  -0.02683 996  ARG B N   
1604 C CA  . ARG A 227 ? 1.03929 0.72139 0.79048 -0.00927 0.18242  -0.02420 996  ARG B CA  
1605 C C   . ARG A 227 ? 1.04374 0.73112 0.80099 -0.00219 0.18279  -0.01384 996  ARG B C   
1606 O O   . ARG A 227 ? 1.07364 0.75334 0.83837 0.00153  0.18840  -0.01045 996  ARG B O   
1607 C CB  . ARG A 227 ? 1.06534 0.72771 0.81149 -0.01826 0.18891  -0.02880 996  ARG B CB  
1608 C CG  . ARG A 227 ? 1.05552 0.70500 0.80778 -0.01538 0.19686  -0.02975 996  ARG B CG  
1609 C CD  . ARG A 227 ? 1.13438 0.76558 0.87921 -0.02461 0.20192  -0.03702 996  ARG B CD  
1610 N NE  . ARG A 227 ? 1.21173 0.84604 0.95335 -0.02918 0.20198  -0.04566 996  ARG B NE  
1611 C CZ  . ARG A 227 ? 1.09105 0.72878 0.83837 -0.02487 0.20531  -0.04935 996  ARG B CZ  
1612 N NH1 . ARG A 227 ? 1.18156 0.81936 0.93784 -0.01528 0.20927  -0.04586 996  ARG B NH1 
1613 N NH2 . ARG A 227 ? 1.10072 0.74319 0.84514 -0.03038 0.20451  -0.05587 996  ARG B NH2 
1614 N N   . LYS A 228 ? 1.03111 0.73288 0.78590 0.00059  0.17670  -0.00846 997  LYS B N   
1615 C CA  . LYS A 228 ? 1.03020 0.74163 0.79174 0.00770  0.17632  0.00241  997  LYS B CA  
1616 C C   . LYS A 228 ? 1.02257 0.74230 0.79476 0.01725  0.17705  0.00448  997  LYS B C   
1617 O O   . LYS A 228 ? 1.05856 0.78380 0.83133 0.01951  0.17454  -0.00148 997  LYS B O   
1618 C CB  . LYS A 228 ? 1.02699 0.75665 0.78297 0.00990  0.16915  0.00676  997  LYS B CB  
1619 C CG  . LYS A 228 ? 1.03064 0.75417 0.77709 0.00075  0.16877  0.00716  997  LYS B CG  
1620 C CD  . LYS A 228 ? 1.04578 0.78767 0.78449 0.00307  0.16138  0.00788  997  LYS B CD  
1621 C CE  . LYS A 228 ? 1.08741 0.84767 0.82881 0.00901  0.15895  0.01991  997  LYS B CE  
1622 N NZ  . LYS A 228 ? 1.11697 0.89655 0.84965 0.01284  0.15174  0.01915  997  LYS B NZ  
1623 N N   . ALA A 229 ? 1.01574 0.73586 0.79691 0.02223  0.18031  0.01360  998  ALA B N   
1624 C CA  . ALA A 229 ? 1.01220 0.74108 0.80431 0.03142  0.18143  0.01700  998  ALA B CA  
1625 C C   . ALA A 229 ? 1.01586 0.76822 0.80805 0.03823  0.17382  0.01858  998  ALA B C   
1626 O O   . ALA A 229 ? 1.00311 0.76786 0.79008 0.03899  0.16851  0.02189  998  ALA B O   
1627 C CB  . ALA A 229 ? 0.98148 0.70651 0.78338 0.03517  0.18564  0.02765  998  ALA B CB  
1628 N N   . ILE A 230 ? 1.00752 0.76649 0.80522 0.04338  0.17297  0.01609  999  ILE B N   
1629 C CA  . ILE A 230 ? 1.02953 0.80883 0.82716 0.04988  0.16506  0.01638  999  ILE B CA  
1630 C C   . ILE A 230 ? 1.05313 0.84813 0.85898 0.05806  0.16476  0.02788  999  ILE B C   
1631 O O   . ILE A 230 ? 1.07404 0.87077 0.89087 0.06293  0.16881  0.03338  999  ILE B O   
1632 C CB  . ILE A 230 ? 1.00060 0.78146 0.80188 0.05136  0.16375  0.01110  999  ILE B CB  
1633 C CG1 . ILE A 230 ? 0.98736 0.75613 0.78063 0.04279  0.16268  0.00065  999  ILE B CG1 
1634 C CG2 . ILE A 230 ? 0.98492 0.78598 0.78691 0.05853  0.15501  0.01252  999  ILE B CG2 
1635 C CD1 . ILE A 230 ? 1.00398 0.77517 0.80127 0.04277  0.16098  -0.00337 999  ILE B CD1 
1636 N N   . GLU A 231 ? 1.04456 0.85285 0.84547 0.05992  0.15994  0.03213  1000 GLU B N   
1637 C CA  . GLU A 231 ? 1.08659 0.91338 0.89540 0.06756  0.15908  0.04385  1000 GLU B CA  
1638 C C   . GLU A 231 ? 1.07817 0.92360 0.89030 0.07601  0.15363  0.04349  1000 GLU B C   
1639 O O   . GLU A 231 ? 1.09156 0.94795 0.91450 0.08213  0.15539  0.05232  1000 GLU B O   
1640 C CB  . GLU A 231 ? 1.12373 0.96289 0.92626 0.06741  0.15544  0.04933  1000 GLU B CB  
1641 C CG  . GLU A 231 ? 1.19417 1.01810 0.99470 0.05894  0.15998  0.05312  1000 GLU B CG  
1642 C CD  . GLU A 231 ? 1.29282 1.13405 1.08792 0.05934  0.15572  0.06042  1000 GLU B CD  
1643 O OE1 . GLU A 231 ? 1.18999 1.05485 0.98224 0.06713  0.14962  0.06116  1000 GLU B OE1 
1644 O OE2 . GLU A 231 ? 1.40967 1.24197 1.20331 0.05217  0.15818  0.06579  1000 GLU B OE2 
1645 N N   . ARG A 232 ? 1.02894 0.87757 0.83196 0.07614  0.14646  0.03359  1001 ARG B N   
1646 C CA  . ARG A 232 ? 0.99606 0.86290 0.79917 0.08384  0.13877  0.03241  1001 ARG B CA  
1647 C C   . ARG A 232 ? 0.93746 0.79661 0.73235 0.08057  0.13217  0.02013  1001 ARG B C   
1648 O O   . ARG A 232 ? 0.92453 0.77196 0.71015 0.07435  0.13080  0.01281  1001 ARG B O   
1649 C CB  . ARG A 232 ? 1.01169 0.90048 0.80974 0.09062  0.13296  0.03670  1001 ARG B CB  
1650 C CG  . ARG A 232 ? 1.00324 0.91171 0.79993 0.09941  0.12441  0.03506  1001 ARG B CG  
1651 C CD  . ARG A 232 ? 1.01891 0.94801 0.80763 0.10600  0.11864  0.03689  1001 ARG B CD  
1652 N NE  . ARG A 232 ? 1.05902 1.00814 0.84582 0.11547  0.11020  0.03518  1001 ARG B NE  
1653 C CZ  . ARG A 232 ? 1.08094 1.05521 0.86499 0.12420  0.10621  0.03999  1001 ARG B CZ  
1654 N NH1 . ARG A 232 ? 1.14782 1.13203 0.93163 0.12443  0.10978  0.04814  1001 ARG B NH1 
1655 N NH2 . ARG A 232 ? 1.07113 1.06205 0.85248 0.13274  0.09807  0.03693  1001 ARG B NH2 
1656 N N   . ARG A 233 ? 0.92972 0.79553 0.72863 0.08412  0.12776  0.01876  1002 ARG B N   
1657 C CA  . ARG A 233 ? 0.93799 0.79731 0.73099 0.08059  0.12015  0.00883  1002 ARG B CA  
1658 C C   . ARG A 233 ? 0.91645 0.79220 0.70399 0.08808  0.10825  0.00617  1002 ARG B C   
1659 O O   . ARG A 233 ? 0.92743 0.81699 0.72205 0.09414  0.10695  0.01178  1002 ARG B O   
1660 C CB  . ARG A 233 ? 0.92791 0.78023 0.73077 0.07726  0.12480  0.01016  1002 ARG B CB  
1661 C CG  . ARG A 233 ? 0.97217 0.80907 0.78014 0.07186  0.13678  0.01244  1002 ARG B CG  
1662 C CD  . ARG A 233 ? 0.99970 0.83665 0.82062 0.07367  0.14407  0.01836  1002 ARG B CD  
1663 N NE  . ARG A 233 ? 1.00490 0.82676 0.82967 0.07049  0.15520  0.02030  1002 ARG B NE  
1664 C CZ  . ARG A 233 ? 0.96662 0.77407 0.79096 0.06438  0.16019  0.01509  1002 ARG B CZ  
1665 N NH1 . ARG A 233 ? 1.01046 0.81790 0.83218 0.06014  0.15544  0.00901  1002 ARG B NH1 
1666 N NH2 . ARG A 233 ? 0.95495 0.74794 0.78129 0.06227  0.16956  0.01612  1002 ARG B NH2 
1667 N N   . ILE A 234 ? 0.89476 0.76919 0.66953 0.08817  0.09929  -0.00250 1003 ILE B N   
1668 C CA  . ILE A 234 ? 0.89069 0.77888 0.65835 0.09618  0.08696  -0.00680 1003 ILE B CA  
1669 C C   . ILE A 234 ? 0.88164 0.75838 0.64434 0.09143  0.07682  -0.01625 1003 ILE B C   
1670 O O   . ILE A 234 ? 0.90122 0.76269 0.65803 0.08419  0.07541  -0.02289 1003 ILE B O   
1671 C CB  . ILE A 234 ? 0.92081 0.81954 0.67748 0.10265  0.08301  -0.00899 1003 ILE B CB  
1672 C CG1 . ILE A 234 ? 0.90971 0.79374 0.65715 0.09625  0.08310  -0.01568 1003 ILE B CG1 
1673 C CG2 . ILE A 234 ? 0.94912 0.86341 0.71239 0.10738  0.09160  0.00274  1003 ILE B CG2 
1674 C CD1 . ILE A 234 ? 0.89067 0.78790 0.62909 0.10292  0.08128  -0.01529 1003 ILE B CD1 
1675 N N   . LEU A 235 ? 0.85097 0.73526 0.61709 0.09458  0.06982  -0.01573 1004 LEU B N   
1676 C CA  . LEU A 235 ? 0.87098 0.74555 0.63422 0.08934  0.05907  -0.02261 1004 LEU B CA  
1677 C C   . LEU A 235 ? 0.90483 0.77967 0.65385 0.09433  0.04397  -0.03278 1004 LEU B C   
1678 O O   . LEU A 235 ? 0.90478 0.79413 0.64813 0.10468  0.03998  -0.03340 1004 LEU B O   
1679 C CB  . LEU A 235 ? 0.89088 0.77373 0.66428 0.08990  0.05765  -0.01658 1004 LEU B CB  
1680 C CG  . LEU A 235 ? 0.94204 0.82433 0.72941 0.08635  0.07278  -0.00691 1004 LEU B CG  
1681 C CD1 . LEU A 235 ? 0.85999 0.76037 0.65655 0.09439  0.07753  0.00293  1004 LEU B CD1 
1682 C CD2 . LEU A 235 ? 1.01051 0.88347 0.80394 0.07723  0.07238  -0.00687 1004 LEU B CD2 
1683 N N   . LEU A 236 ? 0.90785 0.76712 0.65113 0.08733  0.03522  -0.04071 1005 LEU B N   
1684 C CA  . LEU A 236 ? 0.91744 0.77273 0.64668 0.09169  0.02036  -0.05143 1005 LEU B CA  
1685 C C   . LEU A 236 ? 0.93112 0.78528 0.65894 0.09197  0.00506  -0.05510 1005 LEU B C   
1686 O O   . LEU A 236 ? 0.95261 0.80329 0.68975 0.08412  0.00493  -0.05050 1005 LEU B O   
1687 C CB  . LEU A 236 ? 0.92909 0.76679 0.65226 0.08373  0.01900  -0.05790 1005 LEU B CB  
1688 C CG  . LEU A 236 ? 0.91461 0.75139 0.63868 0.08153  0.03342  -0.05435 1005 LEU B CG  
1689 C CD1 . LEU A 236 ? 0.90829 0.73062 0.62359 0.07594  0.02957  -0.06187 1005 LEU B CD1 
1690 C CD2 . LEU A 236 ? 0.90227 0.75658 0.62367 0.09269  0.03832  -0.05062 1005 LEU B CD2 
1691 N N   . TYR A 237 ? 0.96469 0.82204 0.68026 0.10121  -0.00834 -0.06348 1006 TYR B N   
1692 C CA  . TYR A 237 ? 0.98176 0.83530 0.69290 0.10202  -0.02580 -0.06899 1006 TYR B CA  
1693 C C   . TYR A 237 ? 1.04065 0.88290 0.73579 0.10681  -0.04122 -0.08228 1006 TYR B C   
1694 O O   . TYR A 237 ? 1.02685 0.86978 0.71403 0.11231  -0.03762 -0.08657 1006 TYR B O   
1695 C CB  . TYR A 237 ? 0.97843 0.85137 0.69139 0.11154  -0.02773 -0.06511 1006 TYR B CB  
1696 C CG  . TYR A 237 ? 0.98808 0.87377 0.71666 0.10899  -0.01232 -0.05172 1006 TYR B CG  
1697 C CD1 . TYR A 237 ? 1.01097 0.89191 0.75124 0.09880  -0.01051 -0.04504 1006 TYR B CD1 
1698 C CD2 . TYR A 237 ? 0.95671 0.86005 0.68867 0.11704  -0.00019 -0.04518 1006 TYR B CD2 
1699 C CE1 . TYR A 237 ? 1.00397 0.89607 0.75835 0.09756  0.00335  -0.03320 1006 TYR B CE1 
1700 C CE2 . TYR A 237 ? 0.95411 0.86743 0.70065 0.11505  0.01297  -0.03296 1006 TYR B CE2 
1701 C CZ  . TYR A 237 ? 0.99452 0.90161 0.75200 0.10579  0.01485  -0.02747 1006 TYR B CZ  
1702 O OH  . TYR A 237 ? 1.07808 0.99471 0.85008 0.10481  0.02795  -0.01558 1006 TYR B OH  
1703 O OXT . TYR A 237 ? 1.07311 0.90487 0.76298 0.10521  -0.05808 -0.08877 1006 TYR B OXT 
1704 N N   . SER B 1   ? 0.69944 0.99768 0.84846 0.10725  -0.10415 -0.01178 0    SER A N   
1705 C CA  . SER B 1   ? 0.68034 0.97599 0.83065 0.10882  -0.08378 -0.02604 0    SER A CA  
1706 C C   . SER B 1   ? 0.67788 0.97760 0.79366 0.10855  -0.06958 -0.01955 0    SER A C   
1707 O O   . SER B 1   ? 0.69177 0.99538 0.78997 0.10632  -0.07380 -0.00322 0    SER A O   
1708 C CB  . SER B 1   ? 0.65082 0.93720 0.83527 0.11153  -0.07281 -0.03025 0    SER A CB  
1709 O OG  . SER B 1   ? 0.61206 0.89558 0.79359 0.11134  -0.06750 -0.01652 0    SER A OG  
1710 N N   . MET B 2   ? 0.67124 0.97011 0.77764 0.11108  -0.05208 -0.03189 1    MET A N   
1711 C CA  . MET B 2   ? 0.70530 1.00953 0.78089 0.11215  -0.03712 -0.02610 1    MET A CA  
1712 C C   . MET B 2   ? 0.65235 0.95650 0.73629 0.11179  -0.03019 -0.01400 1    MET A C   
1713 O O   . MET B 2   ? 0.65904 0.97094 0.72162 0.10939  -0.02881 -0.00054 1    MET A O   
1714 C CB  . MET B 2   ? 0.75442 1.05556 0.82187 0.11666  -0.01802 -0.04178 1    MET A CB  
1715 C CG  . MET B 2   ? 0.78627 1.09510 0.81774 0.11896  -0.00392 -0.03693 1    MET A CG  
1716 S SD  . MET B 2   ? 1.22759 1.53021 1.24721 0.12581  0.01853  -0.05546 1    MET A SD  
1717 C CE  . MET B 2   ? 0.98673 1.28267 1.00949 0.12310  0.00613  -0.07136 1    MET A CE  
1718 N N   . ALA B 3   ? 0.63718 0.93258 0.75283 0.11406  -0.02611 -0.01864 2    ALA A N   
1719 C CA  . ALA B 3   ? 0.60070 0.89482 0.72475 0.11405  -0.02025 -0.00920 2    ALA A CA  
1720 C C   . ALA B 3   ? 0.58055 0.87691 0.70187 0.10790  -0.03558 0.00861  2    ALA A C   
1721 O O   . ALA B 3   ? 0.57186 0.87362 0.68109 0.10494  -0.03105 0.01981  2    ALA A O   
1722 C CB  . ALA B 3   ? 0.56499 0.84741 0.72277 0.11875  -0.01494 -0.01751 2    ALA A CB  
1723 N N   . LEU B 4   ? 0.58534 0.87807 0.71751 0.10604  -0.05353 0.01157  3    LEU A N   
1724 C CA  . LEU B 4   ? 0.59213 0.88399 0.72213 0.10142  -0.06768 0.02918  3    LEU A CA  
1725 C C   . LEU B 4   ? 0.61684 0.91896 0.71110 0.09777  -0.06928 0.04121  3    LEU A C   
1726 O O   . LEU B 4   ? 0.63507 0.93809 0.72194 0.09329  -0.07021 0.05697  3    LEU A O   
1727 C CB  . LEU B 4   ? 0.57950 0.86560 0.72930 0.10245  -0.08626 0.02885  3    LEU A CB  
1728 C CG  . LEU B 4   ? 0.59491 0.87759 0.74214 0.09937  -0.10142 0.04726  3    LEU A CG  
1729 C CD1 . LEU B 4   ? 0.63282 0.90623 0.79491 0.09717  -0.09644 0.05633  3    LEU A CD1 
1730 C CD2 . LEU B 4   ? 0.58712 0.86703 0.75101 0.10234  -0.11991 0.04529  3    LEU A CD2 
1731 N N   . LYS B 5   ? 0.62321 0.93236 0.69493 0.09966  -0.06890 0.03403  4    LYS A N   
1732 C CA  . LYS B 5   ? 0.64151 0.96035 0.67688 0.09780  -0.06800 0.04490  4    LYS A CA  
1733 C C   . LYS B 5   ? 0.63368 0.95972 0.65779 0.09617  -0.05016 0.05028  4    LYS A C   
1734 O O   . LYS B 5   ? 0.63999 0.97207 0.64792 0.09205  -0.04970 0.06636  4    LYS A O   
1735 C CB  . LYS B 5   ? 0.68504 1.00846 0.69822 0.10133  -0.06938 0.03330  4    LYS A CB  
1736 C CG  . LYS B 5   ? 0.69407 1.01323 0.71973 0.10286  -0.08758 0.02532  4    LYS A CG  
1737 C CD  . LYS B 5   ? 0.74014 1.06272 0.74339 0.10284  -0.10471 0.03783  4    LYS A CD  
1738 C CE  . LYS B 5   ? 0.78489 1.10651 0.79837 0.10549  -0.12258 0.02593  4    LYS A CE  
1739 N NZ  . LYS B 5   ? 0.80008 1.12265 0.81301 0.10700  -0.11518 0.00439  4    LYS A NZ  
1740 N N   . ARG B 6   ? 0.62160 0.94765 0.65447 0.09978  -0.03495 0.03713  5    ARG A N   
1741 C CA  . ARG B 6   ? 0.61909 0.95423 0.64231 0.09958  -0.01841 0.04083  5    ARG A CA  
1742 C C   . ARG B 6   ? 0.61959 0.95291 0.66119 0.09422  -0.02003 0.05270  5    ARG A C   
1743 O O   . ARG B 6   ? 0.63541 0.97906 0.66553 0.09020  -0.01348 0.06359  5    ARG A O   
1744 C CB  . ARG B 6   ? 0.61201 0.94612 0.63932 0.10669  -0.00217 0.02355  5    ARG A CB  
1745 C CG  . ARG B 6   ? 0.60832 0.94994 0.63607 0.10857  0.01374  0.02444  5    ARG A CG  
1746 C CD  . ARG B 6   ? 0.62325 0.98077 0.61915 0.10975  0.02517  0.02901  5    ARG A CD  
1747 N NE  . ARG B 6   ? 0.61911 0.98577 0.61968 0.11180  0.03877  0.02947  5    ARG A NE  
1748 C CZ  . ARG B 6   ? 0.60012 0.97273 0.59000 0.12022  0.05556  0.01973  5    ARG A CZ  
1749 N NH1 . ARG B 6   ? 0.61878 0.98828 0.59050 0.12670  0.06246  0.00940  5    ARG A NH1 
1750 N NH2 . ARG B 6   ? 0.58414 0.96566 0.58118 0.12260  0.06550  0.02004  5    ARG A NH2 
1751 N N   . ILE B 7   ? 0.58484 0.90512 0.65547 0.09387  -0.02875 0.05080  6    ILE A N   
1752 C CA  . ILE B 7   ? 0.59623 0.91174 0.68394 0.08874  -0.03131 0.06125  6    ILE A CA  
1753 C C   . ILE B 7   ? 0.63880 0.95614 0.71369 0.08114  -0.04133 0.08073  6    ILE A C   
1754 O O   . ILE B 7   ? 0.64485 0.96709 0.71776 0.07495  -0.03674 0.09178  6    ILE A O   
1755 C CB  . ILE B 7   ? 0.55758 0.85697 0.67760 0.09166  -0.03816 0.05443  6    ILE A CB  
1756 C CG1 . ILE B 7   ? 0.52426 0.82157 0.65682 0.09926  -0.02409 0.03767  6    ILE A CG1 
1757 C CG2 . ILE B 7   ? 0.55978 0.85040 0.69499 0.08591  -0.04522 0.06687  6    ILE A CG2 
1758 C CD1 . ILE B 7   ? 0.51002 0.79242 0.67206 0.10439  -0.02853 0.02845  6    ILE A CD1 
1759 N N   . HIS B 8   ? 0.64472 0.95862 0.71029 0.08173  -0.05470 0.08522  7    HIS A N   
1760 C CA  . HIS B 8   ? 0.68848 1.00331 0.73753 0.07631  -0.06284 0.10461  7    HIS A CA  
1761 C C   . HIS B 8   ? 0.72548 1.05606 0.74562 0.07360  -0.05130 0.11261  7    HIS A C   
1762 O O   . HIS B 8   ? 0.73860 1.07174 0.75298 0.06684  -0.04976 0.12910  7    HIS A O   
1763 C CB  . HIS B 8   ? 0.69626 1.00613 0.73709 0.07995  -0.07932 0.10632  7    HIS A CB  
1764 C CG  . HIS B 8   ? 0.70775 1.00279 0.77452 0.08068  -0.09344 0.10846  7    HIS A CG  
1765 N ND1 . HIS B 8   ? 0.71373 1.00369 0.79962 0.08637  -0.10144 0.09436  7    HIS A ND1 
1766 C CD2 . HIS B 8   ? 0.70098 0.98490 0.77816 0.07672  -0.10042 0.12319  7    HIS A CD2 
1767 C CE1 . HIS B 8   ? 0.71883 0.99647 0.82565 0.08670  -0.11292 0.10053  7    HIS A CE1 
1768 N NE2 . HIS B 8   ? 0.71536 0.98795 0.81627 0.08113  -0.11256 0.11795  7    HIS A NE2 
1769 N N   . LYS B 9   ? 0.72574 1.06656 0.72752 0.07889  -0.04250 0.10151  8    LYS A N   
1770 C CA  . LYS B 9   ? 0.75281 1.10941 0.72643 0.07774  -0.03067 0.10903  8    LYS A CA  
1771 C C   . LYS B 9   ? 0.76390 1.12924 0.74880 0.07257  -0.01781 0.11331  8    LYS A C   
1772 O O   . LYS B 9   ? 0.79866 1.17412 0.77166 0.06681  -0.01284 0.12835  8    LYS A O   
1773 C CB  . LYS B 9   ? 0.76250 1.12624 0.71521 0.08544  -0.02267 0.09463  8    LYS A CB  
1774 C CG  . LYS B 9   ? 0.85902 1.23947 0.78040 0.08613  -0.00957 0.10194  8    LYS A CG  
1775 C CD  . LYS B 9   ? 0.91660 1.29920 0.81125 0.08445  -0.01732 0.11885  8    LYS A CD  
1776 C CE  . LYS B 9   ? 0.98586 1.38587 0.85379 0.08399  -0.00292 0.13010  8    LYS A CE  
1777 N NZ  . LYS B 9   ? 1.04509 1.44558 0.88510 0.08377  -0.00954 0.14730  8    LYS A NZ  
1778 N N   . GLU B 10  ? 0.72621 1.08811 0.73471 0.07478  -0.01235 0.10020  9    GLU A N   
1779 C CA  . GLU B 10  ? 0.72014 1.09094 0.74064 0.07072  -0.00179 0.10214  9    GLU A CA  
1780 C C   . GLU B 10  ? 0.72037 1.08448 0.75645 0.06052  -0.00957 0.11730  9    GLU A C   
1781 O O   . GLU B 10  ? 0.74705 1.12257 0.78399 0.05353  -0.00257 0.12627  9    GLU A O   
1782 C CB  . GLU B 10  ? 0.63706 1.00310 0.67795 0.07719  0.00451  0.08453  9    GLU A CB  
1783 C CG  . GLU B 10  ? 0.59242 0.96710 0.61867 0.08692  0.01799  0.07016  9    GLU A CG  
1784 C CD  . GLU B 10  ? 0.57362 0.94410 0.61929 0.09360  0.02631  0.05565  9    GLU A CD  
1785 O OE1 . GLU B 10  ? 0.55180 0.92703 0.61102 0.09059  0.02938  0.05811  9    GLU A OE1 
1786 O OE2 . GLU B 10  ? 0.52814 0.88950 0.57645 0.10183  0.02933  0.04175  9    GLU A OE2 
1787 N N   . LEU B 11  ? 0.70763 1.05337 0.75652 0.05952  -0.02385 0.12040  10   LEU A N   
1788 C CA  . LEU B 11  ? 0.72619 1.06171 0.78876 0.05045  -0.03123 0.13507  10   LEU A CA  
1789 C C   . LEU B 11  ? 0.80183 1.14452 0.84248 0.04382  -0.03098 0.15495  10   LEU A C   
1790 O O   . LEU B 11  ? 0.83931 1.18482 0.88597 0.03423  -0.02705 0.16719  10   LEU A O   
1791 C CB  . LEU B 11  ? 0.68750 1.00168 0.76700 0.05342  -0.04607 0.13306  10   LEU A CB  
1792 C CG  . LEU B 11  ? 0.67790 0.97480 0.77828 0.04694  -0.05418 0.14289  10   LEU A CG  
1793 C CD1 . LEU B 11  ? 0.64805 0.94700 0.76718 0.04255  -0.04540 0.13716  10   LEU A CD1 
1794 C CD2 . LEU B 11  ? 0.63646 0.91565 0.75294 0.05365  -0.06682 0.13644  10   LEU A CD2 
1795 N N   . ASN B 12  ? 0.80721 1.15343 0.82175 0.04898  -0.03421 0.15796  11   ASN A N   
1796 C CA  . ASN B 12  ? 0.86194 1.21501 0.85186 0.04481  -0.03245 0.17703  11   ASN A CA  
1797 C C   . ASN B 12  ? 0.91175 1.28641 0.89252 0.04065  -0.01572 0.18065  11   ASN A C   
1798 O O   . ASN B 12  ? 0.96189 1.34153 0.93937 0.03216  -0.01120 0.19786  11   ASN A O   
1799 C CB  . ASN B 12  ? 0.85866 1.21152 0.82011 0.05322  -0.03952 0.17695  11   ASN A CB  
1800 C CG  . ASN B 12  ? 0.87491 1.20944 0.84521 0.05730  -0.05735 0.17527  11   ASN A CG  
1801 O OD1 . ASN B 12  ? 0.87858 1.19901 0.86513 0.05277  -0.06512 0.18534  11   ASN A OD1 
1802 N ND2 . ASN B 12  ? 0.85190 1.18652 0.81267 0.06597  -0.06394 0.16194  11   ASN A ND2 
1803 N N   . ASP B 13  ? 0.88279 1.27064 0.86010 0.04678  -0.00573 0.16495  12   ASP A N   
1804 C CA  . ASP B 13  ? 0.92875 1.33930 0.89875 0.04424  0.01026  0.16751  12   ASP A CA  
1805 C C   . ASP B 13  ? 0.92107 1.33526 0.91960 0.03453  0.01411  0.16985  12   ASP A C   
1806 O O   . ASP B 13  ? 1.00070 1.43263 0.99776 0.02780  0.02416  0.17940  12   ASP A O   
1807 C CB  . ASP B 13  ? 0.91386 1.33560 0.87258 0.05481  0.02006  0.14975  12   ASP A CB  
1808 C CG  . ASP B 13  ? 0.98325 1.40310 0.91093 0.06354  0.01764  0.14700  12   ASP A CG  
1809 O OD1 . ASP B 13  ? 0.99526 1.40676 0.90905 0.06231  0.00768  0.15869  12   ASP A OD1 
1810 O OD2 . ASP B 13  ? 1.06296 1.48901 0.97907 0.07225  0.02580  0.13274  12   ASP A OD2 
1811 N N   . LEU B 14  ? 0.86293 1.26094 0.88798 0.03372  0.00616  0.16101  13   LEU A N   
1812 C CA  . LEU B 14  ? 0.89422 1.29179 0.94595 0.02407  0.00717  0.16322  13   LEU A CA  
1813 C C   . LEU B 14  ? 0.96465 1.35331 1.01975 0.01204  0.00192  0.18386  13   LEU A C   
1814 O O   . LEU B 14  ? 0.99870 1.39042 1.07242 0.00129  0.00480  0.18914  13   LEU A O   
1815 C CB  . LEU B 14  ? 0.82072 1.20080 0.89703 0.02810  0.00003  0.14824  13   LEU A CB  
1816 C CG  . LEU B 14  ? 0.73702 1.12606 0.81684 0.03838  0.00838  0.12817  13   LEU A CG  
1817 C CD1 . LEU B 14  ? 0.66821 1.03608 0.76881 0.04358  0.00040  0.11618  13   LEU A CD1 
1818 C CD2 . LEU B 14  ? 0.69263 1.10210 0.78058 0.03425  0.01899  0.12610  13   LEU A CD2 
1819 N N   . ALA B 15  ? 0.96982 1.34628 1.00771 0.01402  -0.00609 0.19505  14   ALA A N   
1820 C CA  . ALA B 15  ? 1.03867 1.40519 1.07496 0.00439  -0.00963 0.21654  14   ALA A CA  
1821 C C   . ALA B 15  ? 1.08696 1.47307 1.10227 -0.00026 0.00227  0.23228  14   ALA A C   
1822 O O   . ALA B 15  ? 1.08816 1.47501 1.11226 -0.01224 0.00674  0.24760  14   ALA A O   
1823 C CB  . ALA B 15  ? 1.02960 1.37418 1.05555 0.01041  -0.02397 0.22230  14   ALA A CB  
1824 N N   . ARG B 16  ? 1.11603 1.51786 1.10438 0.00891  0.00847  0.22859  15   ARG A N   
1825 C CA  . ARG B 16  ? 1.16796 1.58846 1.13347 0.00666  0.02048  0.24369  15   ARG A CA  
1826 C C   . ARG B 16  ? 1.19299 1.63930 1.17130 -0.00017 0.03535  0.24211  15   ARG A C   
1827 O O   . ARG B 16  ? 1.22543 1.68677 1.19476 -0.00622 0.04591  0.25807  15   ARG A O   
1828 C CB  . ARG B 16  ? 1.16468 1.59172 1.09510 0.02008  0.02163  0.23895  15   ARG A CB  
1829 C CG  . ARG B 16  ? 1.16680 1.57217 1.08294 0.02781  0.00599  0.23911  15   ARG A CG  
1830 C CD  . ARG B 16  ? 1.23299 1.64457 1.11605 0.04068  0.00612  0.23097  15   ARG A CD  
1831 N NE  . ARG B 16  ? 1.18867 1.61050 1.07574 0.04694  0.01217  0.20937  15   ARG A NE  
1832 C CZ  . ARG B 16  ? 1.20247 1.64464 1.07319 0.05088  0.02666  0.20583  15   ARG A CZ  
1833 N NH1 . ARG B 16  ? 1.21313 1.66918 1.06155 0.04964  0.03663  0.22192  15   ARG A NH1 
1834 N NH2 . ARG B 16  ? 1.15074 1.59873 1.02616 0.05739  0.03193  0.18610  15   ARG A NH2 
1835 N N   . ASP B 17  ? 1.16133 1.61426 1.15958 0.00167  0.03680  0.22344  16   ASP A N   
1836 C CA  . ASP B 17  ? 1.19153 1.67009 1.20477 -0.00403 0.04910  0.22017  16   ASP A CA  
1837 C C   . ASP B 17  ? 1.16096 1.63395 1.20405 -0.00474 0.04424  0.20250  16   ASP A C   
1838 O O   . ASP B 17  ? 1.17003 1.65221 1.21262 0.00526  0.04814  0.18497  16   ASP A O   
1839 C CB  . ASP B 17  ? 1.28451 1.78857 1.27347 0.00601  0.06213  0.21543  16   ASP A CB  
1840 C CG  . ASP B 17  ? 1.39181 1.92647 1.39341 -0.00020 0.07561  0.21714  16   ASP A CG  
1841 O OD1 . ASP B 17  ? 1.35894 1.89547 1.39144 -0.01106 0.07365  0.21570  16   ASP A OD1 
1842 O OD2 . ASP B 17  ? 1.48935 2.04644 1.46980 0.00532  0.08791  0.22114  16   ASP A OD2 
1843 N N   . PRO B 18  ? 1.11443 1.57024 1.18245 -0.01553 0.03595  0.20678  17   PRO A N   
1844 C CA  . PRO B 18  ? 1.04815 1.49463 1.14227 -0.01474 0.02999  0.18981  17   PRO A CA  
1845 C C   . PRO B 18  ? 1.00900 1.48275 1.11562 -0.01539 0.03989  0.17901  17   PRO A C   
1846 O O   . PRO B 18  ? 1.03148 1.52947 1.13801 -0.02308 0.04963  0.18846  17   PRO A O   
1847 C CB  . PRO B 18  ? 1.03747 1.46151 1.15250 -0.02800 0.02093  0.20056  17   PRO A CB  
1848 C CG  . PRO B 18  ? 1.06229 1.47681 1.15788 -0.03133 0.01948  0.22150  17   PRO A CG  
1849 C CD  . PRO B 18  ? 1.09778 1.53931 1.16913 -0.02775 0.03203  0.22748  17   PRO A CD  
1850 N N   . PRO B 19  ? 0.95096 1.42248 1.06836 -0.00653 0.03809  0.15936  18   PRO A N   
1851 C CA  . PRO B 19  ? 0.89408 1.39071 1.02481 -0.00629 0.04585  0.14844  18   PRO A CA  
1852 C C   . PRO B 19  ? 0.87421 1.36953 1.03470 -0.02177 0.04109  0.15137  18   PRO A C   
1853 O O   . PRO B 19  ? 0.87009 1.33818 1.04525 -0.02702 0.03023  0.15166  18   PRO A O   
1854 C CB  . PRO B 19  ? 0.81762 1.30585 0.94798 0.00964  0.04456  0.12754  18   PRO A CB  
1855 C CG  . PRO B 19  ? 0.80538 1.25939 0.93963 0.01063  0.03219  0.12771  18   PRO A CG  
1856 C CD  . PRO B 19  ? 0.89470 1.34062 1.01444 0.00367  0.02888  0.14671  18   PRO A CD  
1857 N N   . ALA B 20  ? 0.87557 1.40124 1.04572 -0.02868 0.04937  0.15250  19   ALA A N   
1858 C CA  . ALA B 20  ? 0.85928 1.38719 1.05860 -0.04596 0.04571  0.15624  19   ALA A CA  
1859 C C   . ALA B 20  ? 0.83185 1.34767 1.05235 -0.04318 0.03697  0.13768  19   ALA A C   
1860 O O   . ALA B 20  ? 0.84401 1.34031 1.08537 -0.05504 0.02811  0.13944  19   ALA A O   
1861 C CB  . ALA B 20  ? 0.80720 1.37445 1.01300 -0.05377 0.05702  0.16144  19   ALA A CB  
1862 N N   . GLN B 21  ? 0.80030 1.32550 1.01420 -0.02673 0.03981  0.11998  20   GLN A N   
1863 C CA  . GLN B 21  ? 0.79685 1.31504 1.02949 -0.02283 0.03315  0.10216  20   GLN A CA  
1864 C C   . GLN B 21  ? 0.79535 1.27427 1.02824 -0.01619 0.02299  0.09684  20   GLN A C   
1865 O O   . GLN B 21  ? 0.82606 1.28831 1.07781 -0.01893 0.01435  0.08827  20   GLN A O   
1866 C CB  . GLN B 21  ? 0.78387 1.32874 1.00806 -0.00637 0.04171  0.08622  20   GLN A CB  
1867 C CG  . GLN B 21  ? 0.74956 1.30979 0.99469 -0.00622 0.03892  0.07082  20   GLN A CG  
1868 C CD  . GLN B 21  ? 0.69519 1.28823 0.92891 0.00970  0.04952  0.05925  20   GLN A CD  
1869 O OE1 . GLN B 21  ? 0.66470 1.27525 0.87793 0.01603  0.06043  0.06568  20   GLN A OE1 
1870 N NE2 . GLN B 21  ? 0.64213 1.24277 0.88749 0.01732  0.04637  0.04210  20   GLN A NE2 
1871 N N   . CYS B 22  ? 0.77474 1.23903 0.98756 -0.00766 0.02360  0.10173  21   CYS A N   
1872 C CA  . CYS B 22  ? 0.70373 1.13548 0.91563 0.00158  0.01559  0.09552  21   CYS A CA  
1873 C C   . CYS B 22  ? 0.70233 1.10963 0.91155 -0.00693 0.00775  0.11192  21   CYS A C   
1874 O O   . CYS B 22  ? 0.75237 1.16652 0.95733 -0.01898 0.00946  0.12873  21   CYS A O   
1875 C CB  . CYS B 22  ? 0.68738 1.12321 0.87946 0.02030  0.02266  0.08501  21   CYS A CB  
1876 S SG  . CYS B 22  ? 0.83696 1.30956 1.02348 0.02967  0.03573  0.07262  21   CYS A SG  
1877 N N   . SER B 23  ? 0.64132 1.02020 0.85261 0.00078  -0.00035 0.10702  22   SER A N   
1878 C CA  . SER B 23  ? 0.62870 0.98380 0.83523 -0.00273 -0.00859 0.12045  22   SER A CA  
1879 C C   . SER B 23  ? 0.60383 0.93772 0.81027 0.01161  -0.01402 0.10945  22   SER A C   
1880 O O   . SER B 23  ? 0.63081 0.95777 0.84947 0.01914  -0.01463 0.09464  22   SER A O   
1881 C CB  . SER B 23  ? 0.62583 0.96285 0.84931 -0.01805 -0.01645 0.13200  22   SER A CB  
1882 O OG  . SER B 23  ? 0.70385 1.01266 0.94201 -0.01371 -0.02582 0.12401  22   SER A OG  
1883 N N   . ALA B 24  ? 0.57877 0.90375 0.77148 0.01609  -0.01757 0.11609  23   ALA A N   
1884 C CA  . ALA B 24  ? 0.56120 0.86914 0.75650 0.02927  -0.02201 0.10509  23   ALA A CA  
1885 C C   . ALA B 24  ? 0.55429 0.84774 0.74128 0.02975  -0.03098 0.11591  23   ALA A C   
1886 O O   . ALA B 24  ? 0.59037 0.89292 0.76013 0.02488  -0.03038 0.12866  23   ALA A O   
1887 C CB  . ALA B 24  ? 0.55367 0.87711 0.73826 0.04244  -0.01171 0.09015  23   ALA A CB  
1888 N N   . GLY B 25  ? 0.50513 0.77670 0.70418 0.03659  -0.03931 0.11074  24   GLY A N   
1889 C CA  . GLY B 25  ? 0.51292 0.77273 0.70562 0.03901  -0.04882 0.11891  24   GLY A CA  
1890 C C   . GLY B 25  ? 0.56614 0.80536 0.77530 0.04837  -0.05661 0.11053  24   GLY A C   
1891 O O   . GLY B 25  ? 0.55023 0.78043 0.77611 0.05271  -0.05483 0.09969  24   GLY A O   
1892 N N   . PRO B 26  ? 0.57953 0.81158 0.78418 0.05228  -0.06562 0.11556  25   PRO A N   
1893 C CA  . PRO B 26  ? 0.62256 0.83665 0.84500 0.06121  -0.07359 0.10880  25   PRO A CA  
1894 C C   . PRO B 26  ? 0.67820 0.87031 0.91866 0.05807  -0.07941 0.11350  25   PRO A C   
1895 O O   . PRO B 26  ? 0.68800 0.87376 0.92516 0.04802  -0.08273 0.12754  25   PRO A O   
1896 C CB  . PRO B 26  ? 0.64055 0.85383 0.85259 0.06309  -0.08419 0.11757  25   PRO A CB  
1897 C CG  . PRO B 26  ? 0.57894 0.81302 0.76526 0.05923  -0.07818 0.12169  25   PRO A CG  
1898 C CD  . PRO B 26  ? 0.55702 0.79844 0.73961 0.04970  -0.06904 0.12718  25   PRO A CD  
1899 N N   . VAL B 27  ? 0.74813 0.92713 1.00747 0.06709  -0.08004 0.10187  26   VAL A N   
1900 C CA  . VAL B 27  ? 0.79434 0.94994 1.07005 0.06581  -0.08574 0.10505  26   VAL A CA  
1901 C C   . VAL B 27  ? 0.87211 1.01127 1.14950 0.06518  -0.09885 0.11943  26   VAL A C   
1902 O O   . VAL B 27  ? 0.94165 1.06607 1.21946 0.05720  -0.10362 0.13201  26   VAL A O   
1903 C CB  . VAL B 27  ? 0.80528 0.95122 1.09870 0.07740  -0.08171 0.08877  26   VAL A CB  
1904 C CG1 . VAL B 27  ? 0.69665 0.85585 0.98694 0.07788  -0.06931 0.07656  26   VAL A CG1 
1905 C CG2 . VAL B 27  ? 0.76821 0.91679 1.06744 0.08906  -0.08245 0.08087  26   VAL A CG2 
1906 N N   . GLY B 28  ? 0.90557 1.04739 1.18370 0.07357  -0.10476 0.11788  27   GLY A N   
1907 C CA  . GLY B 28  ? 0.87764 1.00883 1.15410 0.07460  -0.11776 0.13147  27   GLY A CA  
1908 C C   . GLY B 28  ? 0.88163 1.03116 1.14316 0.07712  -0.12121 0.13234  27   GLY A C   
1909 O O   . GLY B 28  ? 0.87425 1.03814 1.11474 0.07029  -0.11748 0.13853  27   GLY A O   
1910 N N   . ASP B 29  ? 0.89417 1.04375 1.16685 0.08702  -0.12835 0.12579  28   ASP A N   
1911 C CA  . ASP B 29  ? 0.89776 1.06476 1.15941 0.09033  -0.13256 0.12259  28   ASP A CA  
1912 C C   . ASP B 29  ? 0.83227 1.01339 1.09922 0.09474  -0.12237 0.10367  28   ASP A C   
1913 O O   . ASP B 29  ? 0.80863 1.00280 1.06987 0.09788  -0.12550 0.09779  28   ASP A O   
1914 C CB  . ASP B 29  ? 0.97539 1.13607 1.24663 0.09795  -0.14812 0.12710  28   ASP A CB  
1915 C CG  . ASP B 29  ? 1.08131 1.23385 1.33612 0.09468  -0.15859 0.14736  28   ASP A CG  
1916 O OD1 . ASP B 29  ? 1.10785 1.26351 1.34128 0.08590  -0.15338 0.15751  28   ASP A OD1 
1917 O OD2 . ASP B 29  ? 1.11051 1.25343 1.37396 0.10149  -0.17134 0.15368  28   ASP A OD2 
1918 N N   . ASP B 30  ? 0.78989 0.96761 1.06737 0.09573  -0.11040 0.09367  29   ASP A N   
1919 C CA  . ASP B 30  ? 0.71406 0.90247 0.99600 0.10124  -0.09891 0.07637  29   ASP A CA  
1920 C C   . ASP B 30  ? 0.66830 0.87338 0.92605 0.09524  -0.08845 0.07561  29   ASP A C   
1921 O O   . ASP B 30  ? 0.64735 0.85288 0.90007 0.09068  -0.08029 0.07726  29   ASP A O   
1922 C CB  . ASP B 30  ? 0.69910 0.87527 1.00220 0.10785  -0.09073 0.06608  29   ASP A CB  
1923 C CG  . ASP B 30  ? 0.69314 0.87713 1.00311 0.11567  -0.07894 0.04907  29   ASP A CG  
1924 O OD1 . ASP B 30  ? 0.67445 0.87101 0.97774 0.11596  -0.07980 0.04477  29   ASP A OD1 
1925 O OD2 . ASP B 30  ? 0.68549 0.86185 1.00710 0.12200  -0.06884 0.03991  29   ASP A OD2 
1926 N N   . MET B 31  ? 0.64637 0.86574 0.88895 0.09540  -0.08932 0.07308  30   MET A N   
1927 C CA  . MET B 31  ? 0.59928 0.83486 0.81727 0.09120  -0.07909 0.07235  30   MET A CA  
1928 C C   . MET B 31  ? 0.57432 0.81506 0.79567 0.09616  -0.06274 0.05709  30   MET A C   
1929 O O   . MET B 31  ? 0.54240 0.79509 0.74645 0.09328  -0.05221 0.05697  30   MET A O   
1930 C CB  . MET B 31  ? 0.58213 0.82915 0.78179 0.09139  -0.08509 0.07281  30   MET A CB  
1931 C CG  . MET B 31  ? 0.60199 0.84484 0.79417 0.08834  -0.10113 0.08844  30   MET A CG  
1932 S SD  . MET B 31  ? 0.65168 0.89538 0.82324 0.07814  -0.09850 0.10829  30   MET A SD  
1933 C CE  . MET B 31  ? 0.60138 0.86661 0.74507 0.07614  -0.08409 0.10340  30   MET A CE  
1934 N N   . PHE B 32  ? 0.57689 0.80893 0.81999 0.10436  -0.05975 0.04493  31   PHE A N   
1935 C CA  . PHE B 32  ? 0.53095 0.76554 0.77680 0.11120  -0.04337 0.03055  31   PHE A CA  
1936 C C   . PHE B 32  ? 0.55679 0.78240 0.81321 0.11353  -0.03699 0.02916  31   PHE A C   
1937 O O   . PHE B 32  ? 0.55607 0.78260 0.81412 0.12099  -0.02324 0.01764  31   PHE A O   
1938 C CB  . PHE B 32  ? 0.51218 0.74238 0.77513 0.11942  -0.04131 0.01761  31   PHE A CB  
1939 C CG  . PHE B 32  ? 0.51555 0.75698 0.76548 0.11818  -0.04277 0.01313  31   PHE A CG  
1940 C CD1 . PHE B 32  ? 0.53068 0.77420 0.78019 0.11441  -0.05925 0.01947  31   PHE A CD1 
1941 C CD2 . PHE B 32  ? 0.50274 0.75190 0.73958 0.12160  -0.02780 0.00213  31   PHE A CD2 
1942 C CE1 . PHE B 32  ? 0.53100 0.78453 0.76761 0.11358  -0.06157 0.01377  31   PHE A CE1 
1943 C CE2 . PHE B 32  ? 0.53749 0.79493 0.76150 0.12041  -0.02901 -0.00314 31   PHE A CE2 
1944 C CZ  . PHE B 32  ? 0.55036 0.81024 0.77421 0.11607  -0.04639 0.00222  31   PHE A CZ  
1945 N N   . HIS B 33  ? 0.58118 0.79761 0.84309 0.10769  -0.04640 0.04044  32   HIS A N   
1946 C CA  . HIS B 33  ? 0.56774 0.77560 0.83755 0.10813  -0.04233 0.03949  32   HIS A CA  
1947 C C   . HIS B 33  ? 0.54784 0.75970 0.80627 0.09580  -0.04748 0.05330  32   HIS A C   
1948 O O   . HIS B 33  ? 0.58169 0.78647 0.84036 0.08932  -0.05947 0.06625  32   HIS A O   
1949 C CB  . HIS B 33  ? 0.59356 0.78010 0.88744 0.11437  -0.04841 0.03780  32   HIS A CB  
1950 C CG  . HIS B 33  ? 0.65647 0.83780 0.96391 0.12744  -0.03836 0.02301  32   HIS A CG  
1951 N ND1 . HIS B 33  ? 0.68824 0.86813 1.00767 0.13332  -0.03978 0.01800  32   HIS A ND1 
1952 C CD2 . HIS B 33  ? 0.69258 0.86990 1.00353 0.13617  -0.02617 0.01228  32   HIS A CD2 
1953 C CE1 . HIS B 33  ? 0.72602 0.90030 1.05666 0.14457  -0.02769 0.00557  32   HIS A CE1 
1954 N NE2 . HIS B 33  ? 0.74492 0.91698 1.06912 0.14731  -0.01918 0.00212  32   HIS A NE2 
1955 N N   . TRP B 34  ? 0.50448 0.72858 0.75285 0.09288  -0.03797 0.05088  33   TRP A N   
1956 C CA  . TRP B 34  ? 0.49938 0.72968 0.73956 0.08046  -0.04056 0.06292  33   TRP A CA  
1957 C C   . TRP B 34  ? 0.48543 0.70895 0.73735 0.07948  -0.03824 0.05842  33   TRP A C   
1958 O O   . TRP B 34  ? 0.46491 0.68477 0.72455 0.08982  -0.03148 0.04482  33   TRP A O   
1959 C CB  . TRP B 34  ? 0.49074 0.74550 0.70908 0.07648  -0.03183 0.06475  33   TRP A CB  
1960 C CG  . TRP B 34  ? 0.52124 0.78324 0.72373 0.07574  -0.03500 0.07057  33   TRP A CG  
1961 C CD1 . TRP B 34  ? 0.54631 0.79831 0.75313 0.08008  -0.04371 0.07044  33   TRP A CD1 
1962 C CD2 . TRP B 34  ? 0.52575 0.80731 0.70497 0.07082  -0.02998 0.07702  33   TRP A CD2 
1963 N NE1 . TRP B 34  ? 0.53932 0.80314 0.72593 0.07823  -0.04511 0.07536  33   TRP A NE1 
1964 C CE2 . TRP B 34  ? 0.53389 0.81495 0.70228 0.07288  -0.03633 0.07986  33   TRP A CE2 
1965 C CE3 . TRP B 34  ? 0.51971 0.82010 0.68650 0.06535  -0.02075 0.08049  33   TRP A CE3 
1966 C CZ2 . TRP B 34  ? 0.54960 0.84611 0.69288 0.07020  -0.03361 0.08605  33   TRP A CZ2 
1967 C CZ3 . TRP B 34  ? 0.51751 0.83409 0.66083 0.06278  -0.01704 0.08734  33   TRP A CZ3 
1968 C CH2 . TRP B 34  ? 0.54524 0.85877 0.67580 0.06546  -0.02335 0.09008  33   TRP A CH2 
1969 N N   . GLN B 35  ? 0.50772 0.72960 0.76000 0.06698  -0.04352 0.06994  34   GLN A N   
1970 C CA  . GLN B 35  ? 0.50709 0.72914 0.76706 0.06242  -0.04111 0.06617  34   GLN A CA  
1971 C C   . GLN B 35  ? 0.50687 0.75440 0.75398 0.05251  -0.03457 0.07140  34   GLN A C   
1972 O O   . GLN B 35  ? 0.53336 0.78968 0.76822 0.04453  -0.03583 0.08449  34   GLN A O   
1973 C CB  . GLN B 35  ? 0.54593 0.74401 0.82004 0.05490  -0.05192 0.07431  34   GLN A CB  
1974 C CG  . GLN B 35  ? 0.60309 0.80357 0.88393 0.04554  -0.05090 0.07268  34   GLN A CG  
1975 C CD  . GLN B 35  ? 0.72041 0.89301 1.01582 0.03927  -0.06086 0.07806  34   GLN A CD  
1976 O OE1 . GLN B 35  ? 0.72636 0.87705 1.03208 0.04901  -0.06505 0.07149  34   GLN A OE1 
1977 N NE2 . GLN B 35  ? 0.67531 0.84791 0.97167 0.02308  -0.06375 0.09023  34   GLN A NE2 
1978 N N   . ALA B 36  ? 0.47611 0.73646 0.72538 0.05436  -0.02726 0.06098  35   ALA A N   
1979 C CA  . ALA B 36  ? 0.49162 0.77884 0.73188 0.04611  -0.02035 0.06430  35   ALA A CA  
1980 C C   . ALA B 36  ? 0.51216 0.80044 0.76676 0.03874  -0.02223 0.06036  35   ALA A C   
1981 O O   . ALA B 36  ? 0.48691 0.75748 0.75446 0.04423  -0.02640 0.05067  35   ALA A O   
1982 C CB  . ALA B 36  ? 0.48864 0.79808 0.71424 0.05762  -0.00782 0.05378  35   ALA A CB  
1983 N N   . THR B 37  ? 0.53874 0.84817 0.79110 0.02607  -0.01921 0.06804  36   THR A N   
1984 C CA  . THR B 37  ? 0.53872 0.85527 0.80548 0.01631  -0.02075 0.06466  36   THR A CA  
1985 C C   . THR B 37  ? 0.56205 0.91534 0.82112 0.01417  -0.01068 0.06318  36   THR A C   
1986 O O   . THR B 37  ? 0.58854 0.95759 0.83375 0.01015  -0.00517 0.07450  36   THR A O   
1987 C CB  . THR B 37  ? 0.54550 0.84627 0.82361 -0.00182 -0.02914 0.07969  36   THR A CB  
1988 O OG1 . THR B 37  ? 0.52792 0.79467 0.81727 0.00130  -0.03873 0.07687  36   THR A OG1 
1989 C CG2 . THR B 37  ? 0.55801 0.87639 0.84871 -0.01612 -0.02797 0.07954  36   THR A CG2 
1990 N N   . ILE B 38  ? 0.52257 0.89001 0.78910 0.01859  -0.00815 0.04890  37   ILE A N   
1991 C CA  . ILE B 38  ? 0.57002 0.97444 0.83270 0.01591  0.00044  0.04749  37   ILE A CA  
1992 C C   . ILE B 38  ? 0.57822 0.99031 0.86221 0.00368  -0.00510 0.04289  37   ILE A C   
1993 O O   . ILE B 38  ? 0.56212 0.95469 0.85871 0.00623  -0.01296 0.03216  37   ILE A O   
1994 C CB  . ILE B 38  ? 0.55904 0.98137 0.80619 0.03582  0.01104  0.03383  37   ILE A CB  
1995 C CG1 . ILE B 38  ? 0.54315 0.96402 0.79886 0.04733  0.00955  0.01513  37   ILE A CG1 
1996 C CG2 . ILE B 38  ? 0.52406 0.93060 0.75464 0.04879  0.01474  0.03412  37   ILE A CG2 
1997 C CD1 . ILE B 38  ? 0.55392 0.98907 0.79233 0.06807  0.02119  0.00341  37   ILE A CD1 
1998 N N   . MET B 39  ? 0.62292 1.06245 0.91162 -0.01039 -0.00125 0.05156  38   MET A N   
1999 C CA  . MET B 39  ? 0.63040 1.08236 0.94155 -0.02436 -0.00592 0.04749  38   MET A CA  
2000 C C   . MET B 39  ? 0.60816 1.09224 0.91899 -0.01284 -0.00087 0.03079  38   MET A C   
2001 O O   . MET B 39  ? 0.61890 1.12785 0.91305 -0.00244 0.00978  0.03089  38   MET A O   
2002 C CB  . MET B 39  ? 0.70373 1.17113 1.02211 -0.04560 -0.00294 0.06610  38   MET A CB  
2003 C CG  . MET B 39  ? 0.82435 1.26566 1.13406 -0.05286 -0.00444 0.08552  38   MET A CG  
2004 S SD  . MET B 39  ? 0.93584 1.39358 1.25103 -0.07601 0.00142  0.10930  38   MET A SD  
2005 C CE  . MET B 39  ? 0.98603 1.43662 1.33579 -0.09640 -0.00719 0.10491  38   MET A CE  
2006 N N   . GLY B 40  ? 0.60572 1.21255 0.78199 -0.04326 -0.07592 0.01960  39   GLY A N   
2007 C CA  . GLY B 40  ? 0.60548 1.23261 0.77800 -0.03287 -0.07567 0.01861  39   GLY A CA  
2008 C C   . GLY B 40  ? 0.61878 1.30088 0.79545 -0.03141 -0.07871 0.02002  39   GLY A C   
2009 O O   . GLY B 40  ? 0.64970 1.34689 0.82041 -0.04928 -0.08168 0.02436  39   GLY A O   
2010 N N   . PRO B 41  ? 0.61792 1.31630 0.79840 -0.00916 -0.07521 0.01623  40   PRO A N   
2011 C CA  . PRO B 41  ? 0.65075 1.37842 0.82499 -0.00419 -0.07278 0.01651  40   PRO A CA  
2012 C C   . PRO B 41  ? 0.67168 1.42172 0.83658 -0.01458 -0.07537 0.02077  40   PRO A C   
2013 O O   . PRO B 41  ? 0.66061 1.40781 0.82286 -0.01344 -0.07822 0.02136  40   PRO A O   
2014 C CB  . PRO B 41  ? 0.63990 1.37077 0.81695 0.02429  -0.06885 0.01091  40   PRO A CB  
2015 C CG  . PRO B 41  ? 0.59876 1.29947 0.77986 0.03256  -0.06878 0.00902  40   PRO A CG  
2016 C CD  . PRO B 41  ? 0.59080 1.25801 0.77187 0.01246  -0.06932 0.01109  40   PRO A CD  
2017 N N   . ASN B 42  ? 0.71960 1.49366 0.87918 -0.02547 -0.07437 0.02399  41   ASN A N   
2018 C CA  . ASN B 42  ? 0.74667 1.54632 0.89806 -0.03677 -0.07634 0.02836  41   ASN A CA  
2019 C C   . ASN B 42  ? 0.70450 1.52426 0.85452 -0.01545 -0.07475 0.02600  41   ASN A C   
2020 O O   . ASN B 42  ? 0.66108 1.49876 0.80538 -0.02191 -0.07728 0.02899  41   ASN A O   
2021 C CB  . ASN B 42  ? 0.76766 1.59249 0.91461 -0.05095 -0.07444 0.03258  41   ASN A CB  
2022 C CG  . ASN B 42  ? 0.82366 1.62921 0.96780 -0.07719 -0.07808 0.03734  41   ASN A CG  
2023 O OD1 . ASN B 42  ? 0.84356 1.62665 0.99232 -0.07722 -0.07781 0.03599  41   ASN A OD1 
2024 N ND2 . ASN B 42  ? 0.83825 1.65172 0.97395 -0.09980 -0.08203 0.04310  41   ASN A ND2 
2025 N N   . ASP B 43  ? 0.71328 1.52856 0.86767 0.00986  -0.07111 0.02073  42   ASP A N   
2026 C CA  . ASP B 43  ? 0.65547 1.48439 0.80751 0.03403  -0.06976 0.01825  42   ASP A CA  
2027 C C   . ASP B 43  ? 0.66071 1.47166 0.81180 0.03878  -0.07363 0.01857  42   ASP A C   
2028 O O   . ASP B 43  ? 0.65426 1.47936 0.80061 0.05385  -0.07411 0.01868  42   ASP A O   
2029 C CB  . ASP B 43  ? 0.64212 1.46398 0.79752 0.05790  -0.06537 0.01228  42   ASP A CB  
2030 C CG  . ASP B 43  ? 0.67705 1.51626 0.82754 0.08446  -0.06332 0.00956  42   ASP A CG  
2031 O OD1 . ASP B 43  ? 0.74301 1.60203 0.88845 0.08538  -0.06507 0.01259  42   ASP A OD1 
2032 O OD2 . ASP B 43  ? 0.82469 1.65506 0.97575 0.10524  -0.06044 0.00418  42   ASP A OD2 
2033 N N   . SER B 44  ? 0.65992 1.44188 0.81448 0.02614  -0.07657 0.01907  43   SER A N   
2034 C CA  . SER B 44  ? 0.62844 1.39224 0.78202 0.03060  -0.07992 0.01914  43   SER A CA  
2035 C C   . SER B 44  ? 0.61148 1.36985 0.75959 0.00509  -0.08592 0.02265  43   SER A C   
2036 O O   . SER B 44  ? 0.63078 1.39363 0.77667 -0.01725 -0.08748 0.02520  43   SER A O   
2037 C CB  . SER B 44  ? 0.60289 1.32588 0.76123 0.04057  -0.07554 0.01548  43   SER A CB  
2038 O OG  . SER B 44  ? 0.57783 1.28110 0.74006 0.02107  -0.07533 0.01584  43   SER A OG  
2039 N N   . PRO B 45  ? 0.60940 1.34303 0.74868 0.00747  -0.08682 0.02254  44   PRO A N   
2040 C CA  . PRO B 45  ? 0.59763 1.30978 0.72619 -0.01612 -0.09066 0.02420  44   PRO A CA  
2041 C C   . PRO B 45  ? 0.57851 1.24413 0.70648 -0.02837 -0.08720 0.02279  44   PRO A C   
2042 O O   . PRO B 45  ? 0.57550 1.21879 0.69301 -0.04694 -0.09017 0.02356  44   PRO A O   
2043 C CB  . PRO B 45  ? 0.61386 1.30599 0.72962 -0.00472 -0.08965 0.02361  44   PRO A CB  
2044 C CG  . PRO B 45  ? 0.61211 1.29096 0.73180 0.02287  -0.08267 0.02137  44   PRO A CG  
2045 C CD  . PRO B 45  ? 0.62031 1.34103 0.75331 0.03182  -0.08346 0.02117  44   PRO A CD  
2046 N N   . TYR B 46  ? 0.58151 1.23221 0.71949 -0.01836 -0.08155 0.02057  45   TYR A N   
2047 C CA  . TYR B 46  ? 0.57387 1.18652 0.71362 -0.02844 -0.07881 0.01967  45   TYR A CA  
2048 C C   . TYR B 46  ? 0.57387 1.20749 0.71871 -0.04743 -0.08363 0.02256  45   TYR A C   
2049 O O   . TYR B 46  ? 0.57682 1.18201 0.72247 -0.05698 -0.08274 0.02274  45   TYR A O   
2050 C CB  . TYR B 46  ? 0.54984 1.13737 0.69768 -0.00950 -0.07107 0.01609  45   TYR A CB  
2051 C CG  . TYR B 46  ? 0.54850 1.11995 0.69082 0.01021  -0.06631 0.01426  45   TYR A CG  
2052 C CD1 . TYR B 46  ? 0.54957 1.08347 0.68215 0.00919  -0.06296 0.01390  45   TYR A CD1 
2053 C CD2 . TYR B 46  ? 0.55321 1.14649 0.69824 0.03025  -0.06515 0.01314  45   TYR A CD2 
2054 C CE1 . TYR B 46  ? 0.53661 1.05562 0.66251 0.02596  -0.05851 0.01328  45   TYR A CE1 
2055 C CE2 . TYR B 46  ? 0.56120 1.13684 0.69872 0.04786  -0.06133 0.01244  45   TYR A CE2 
2056 C CZ  . TYR B 46  ? 0.56629 1.10506 0.69431 0.04483  -0.05800 0.01293  45   TYR A CZ  
2057 O OH  . TYR B 46  ? 0.56047 1.08127 0.67956 0.06144  -0.05402 0.01320  45   TYR A OH  
2058 N N   . GLN B 47  ? 0.58296 1.26680 0.73062 -0.05326 -0.08883 0.02540  46   GLN A N   
2059 C CA  . GLN B 47  ? 0.61932 1.32535 0.76953 -0.07230 -0.09264 0.02921  46   GLN A CA  
2060 C C   . GLN B 47  ? 0.58555 1.26520 0.72559 -0.09821 -0.09797 0.03219  46   GLN A C   
2061 O O   . GLN B 47  ? 0.58356 1.25067 0.71093 -0.10783 -0.10151 0.03258  46   GLN A O   
2062 C CB  . GLN B 47  ? 0.67083 1.41062 0.81450 -0.07265 -0.09130 0.03161  46   GLN A CB  
2063 C CG  . GLN B 47  ? 0.71775 1.46744 0.85410 -0.09632 -0.09306 0.03688  46   GLN A CG  
2064 C CD  . GLN B 47  ? 0.82148 1.60499 0.95081 -0.10042 -0.09313 0.03979  46   GLN A CD  
2065 O OE1 . GLN B 47  ? 0.89602 1.70834 1.02864 -0.08528 -0.08794 0.03905  46   GLN A OE1 
2066 N NE2 . GLN B 47  ? 0.88493 1.66561 1.00389 -0.12073 -0.09925 0.04279  46   GLN A NE2 
2067 N N   . GLY B 48  ? 0.57793 1.24430 0.72063 -0.10860 -0.09821 0.03411  47   GLY A N   
2068 C CA  . GLY B 48  ? 0.54730 1.17998 0.67791 -0.13050 -0.10244 0.03698  47   GLY A CA  
2069 C C   . GLY B 48  ? 0.56853 1.14568 0.69729 -0.12277 -0.09765 0.03384  47   GLY A C   
2070 O O   . GLY B 48  ? 0.59974 1.14832 0.72088 -0.13716 -0.10050 0.03632  47   GLY A O   
2071 N N   . GLY B 49  ? 0.56501 1.12725 0.70049 -0.10037 -0.09053 0.02892  48   GLY A N   
2072 C CA  . GLY B 49  ? 0.56168 1.07650 0.69735 -0.09238 -0.08530 0.02604  48   GLY A CA  
2073 C C   . GLY B 49  ? 0.54989 1.06234 0.69994 -0.08286 -0.08159 0.02517  48   GLY A C   
2074 O O   . GLY B 49  ? 0.55725 1.10212 0.71730 -0.07562 -0.08101 0.02486  48   GLY A O   
2075 N N   . VAL B 50  ? 0.54624 1.02035 0.69652 -0.08264 -0.07936 0.02453  49   VAL A N   
2076 C CA  . VAL B 50  ? 0.53283 0.99977 0.69646 -0.07349 -0.07602 0.02330  49   VAL A CA  
2077 C C   . VAL B 50  ? 0.52289 0.95853 0.69091 -0.05817 -0.06855 0.01902  49   VAL A C   
2078 O O   . VAL B 50  ? 0.53702 0.94130 0.69746 -0.06046 -0.06710 0.01868  49   VAL A O   
2079 C CB  . VAL B 50  ? 0.53242 0.98653 0.69421 -0.08723 -0.08070 0.02752  49   VAL A CB  
2080 C CG1 . VAL B 50  ? 0.56708 0.98300 0.71453 -0.09691 -0.08272 0.02888  49   VAL A CG1 
2081 C CG2 . VAL B 50  ? 0.49327 0.93904 0.66895 -0.07670 -0.07747 0.02585  49   VAL A CG2 
2082 N N   . PHE B 51  ? 0.49517 0.93860 0.67423 -0.04286 -0.06372 0.01571  50   PHE A N   
2083 C CA  . PHE B 51  ? 0.47184 0.88993 0.65481 -0.02943 -0.05634 0.01227  50   PHE A CA  
2084 C C   . PHE B 51  ? 0.46158 0.86834 0.65783 -0.02470 -0.05398 0.01096  50   PHE A C   
2085 O O   . PHE B 51  ? 0.48958 0.91534 0.69309 -0.02355 -0.05623 0.01047  50   PHE A O   
2086 C CB  . PHE B 51  ? 0.46943 0.90063 0.65151 -0.01586 -0.05288 0.00977  50   PHE A CB  
2087 C CG  . PHE B 51  ? 0.48869 0.93771 0.65891 -0.01952 -0.05616 0.01128  50   PHE A CG  
2088 C CD1 . PHE B 51  ? 0.49783 0.98497 0.66769 -0.02396 -0.06167 0.01295  50   PHE A CD1 
2089 C CD2 . PHE B 51  ? 0.47054 0.90076 0.62994 -0.01869 -0.05378 0.01107  50   PHE A CD2 
2090 C CE1 . PHE B 51  ? 0.51355 1.02111 0.67384 -0.02812 -0.06532 0.01462  50   PHE A CE1 
2091 C CE2 . PHE B 51  ? 0.49558 0.94328 0.64365 -0.02270 -0.05768 0.01238  50   PHE A CE2 
2092 C CZ  . PHE B 51  ? 0.52172 1.00883 0.67087 -0.02776 -0.06376 0.01428  50   PHE A CZ  
2093 N N   . PHE B 52  ? 0.44431 0.82216 0.64342 -0.02217 -0.04965 0.01032  51   PHE A N   
2094 C CA  . PHE B 52  ? 0.43620 0.80448 0.64902 -0.01804 -0.04755 0.00927  51   PHE A CA  
2095 C C   . PHE B 52  ? 0.43518 0.79599 0.65485 -0.00571 -0.04048 0.00583  51   PHE A C   
2096 O O   . PHE B 52  ? 0.43057 0.78267 0.64356 -0.00012 -0.03569 0.00501  51   PHE A O   
2097 C CB  . PHE B 52  ? 0.44070 0.78518 0.65430 -0.02247 -0.04744 0.01117  51   PHE A CB  
2098 C CG  . PHE B 52  ? 0.46834 0.81492 0.67457 -0.03509 -0.05519 0.01516  51   PHE A CG  
2099 C CD1 . PHE B 52  ? 0.48287 0.82564 0.67281 -0.04426 -0.05848 0.01701  51   PHE A CD1 
2100 C CD2 . PHE B 52  ? 0.50361 0.85588 0.71756 -0.03891 -0.05978 0.01738  51   PHE A CD2 
2101 C CE1 . PHE B 52  ? 0.50699 0.84907 0.68789 -0.05799 -0.06603 0.02133  51   PHE A CE1 
2102 C CE2 . PHE B 52  ? 0.48823 0.84048 0.69317 -0.05142 -0.06711 0.02214  51   PHE A CE2 
2103 C CZ  . PHE B 52  ? 0.48579 0.83195 0.67390 -0.06144 -0.07016 0.02426  51   PHE A CZ  
2104 N N   . LEU B 53  ? 0.42175 0.78572 0.65326 -0.00241 -0.04040 0.00403  52   LEU A N   
2105 C CA  . LEU B 53  ? 0.40744 0.76214 0.64514 0.00679  -0.03464 0.00093  52   LEU A CA  
2106 C C   . LEU B 53  ? 0.39540 0.74274 0.64760 0.00513  -0.03438 0.00044  52   LEU A C   
2107 O O   . LEU B 53  ? 0.39371 0.74891 0.65098 -0.00084 -0.03990 0.00182  52   LEU A O   
2108 C CB  . LEU B 53  ? 0.41316 0.78283 0.64716 0.01408  -0.03575 -0.00216 52   LEU A CB  
2109 C CG  . LEU B 53  ? 0.42069 0.80391 0.64194 0.01843  -0.03651 -0.00184 52   LEU A CG  
2110 C CD1 . LEU B 53  ? 0.45810 0.86764 0.67622 0.01069  -0.04334 0.00005  52   LEU A CD1 
2111 C CD2 . LEU B 53  ? 0.40336 0.78861 0.62102 0.03116  -0.03448 -0.00546 52   LEU A CD2 
2112 N N   . THR B 54  ? 0.37273 0.70592 0.63111 0.00995  -0.02814 -0.00105 53   THR A N   
2113 C CA  . THR B 54  ? 0.37998 0.70966 0.65308 0.00876  -0.02769 -0.00214 53   THR A CA  
2114 C C   . THR B 54  ? 0.38307 0.71425 0.65585 0.01287  -0.02779 -0.00628 53   THR A C   
2115 O O   . THR B 54  ? 0.37730 0.70359 0.63951 0.01918  -0.02481 -0.00769 53   THR A O   
2116 C CB  . THR B 54  ? 0.40345 0.71770 0.68457 0.00952  -0.02039 -0.00062 53   THR A CB  
2117 O OG1 . THR B 54  ? 0.45147 0.75417 0.72562 0.01447  -0.01334 -0.00127 53   THR A OG1 
2118 C CG2 . THR B 54  ? 0.40349 0.71236 0.68256 0.00765  -0.01989 0.00251  53   THR A CG2 
2119 N N   . ILE B 55  ? 0.39463 0.73204 0.67690 0.00976  -0.03206 -0.00833 54   ILE A N   
2120 C CA  . ILE B 55  ? 0.38270 0.71782 0.66396 0.01262  -0.03293 -0.01324 54   ILE A CA  
2121 C C   . ILE B 55  ? 0.40083 0.72807 0.69648 0.00762  -0.03172 -0.01377 54   ILE A C   
2122 O O   . ILE B 55  ? 0.41442 0.74992 0.72220 0.00223  -0.03508 -0.01180 54   ILE A O   
2123 C CB  . ILE B 55  ? 0.38211 0.73500 0.65876 0.01305  -0.04015 -0.01633 54   ILE A CB  
2124 C CG1 . ILE B 55  ? 0.36222 0.72818 0.62620 0.01724  -0.04114 -0.01533 54   ILE A CG1 
2125 C CG2 . ILE B 55  ? 0.37925 0.72582 0.65261 0.01676  -0.04118 -0.02263 54   ILE A CG2 
2126 C CD1 . ILE B 55  ? 0.38613 0.77425 0.64663 0.01666  -0.04747 -0.01733 54   ILE A CD1 
2127 N N   . HIS B 56  ? 0.42111 0.73318 0.71454 0.00915  -0.02773 -0.01630 55   HIS A N   
2128 C CA  . HIS B 56  ? 0.49370 0.79836 0.79988 0.00271  -0.02602 -0.01671 55   HIS A CA  
2129 C C   . HIS B 56  ? 0.46721 0.76376 0.76658 0.00247  -0.02955 -0.02280 55   HIS A C   
2130 O O   . HIS B 56  ? 0.43291 0.71403 0.71720 0.00857  -0.02699 -0.02509 55   HIS A O   
2131 C CB  . HIS B 56  ? 0.54141 0.83097 0.84827 0.00278  -0.01672 -0.01319 55   HIS A CB  
2132 C CG  . HIS B 56  ? 0.62412 0.91240 0.94768 -0.00539 -0.01374 -0.01168 55   HIS A CG  
2133 N ND1 . HIS B 56  ? 0.71006 1.01303 1.04989 -0.01174 -0.01928 -0.01227 55   HIS A ND1 
2134 C CD2 . HIS B 56  ? 0.69058 0.96743 1.01747 -0.00867 -0.00572 -0.00898 55   HIS A CD2 
2135 C CE1 . HIS B 56  ? 0.72802 1.03071 1.08184 -0.01844 -0.01495 -0.01021 55   HIS A CE1 
2136 N NE2 . HIS B 56  ? 0.68639 0.97358 1.03275 -0.01722 -0.00633 -0.00808 55   HIS A NE2 
2137 N N   . PHE B 57  ? 0.45900 0.76437 0.76745 -0.00378 -0.03581 -0.02556 56   PHE A N   
2138 C CA  . PHE B 57  ? 0.45426 0.74904 0.75420 -0.00473 -0.03962 -0.03239 56   PHE A CA  
2139 C C   . PHE B 57  ? 0.47091 0.75124 0.77912 -0.01412 -0.03688 -0.03231 56   PHE A C   
2140 O O   . PHE B 57  ? 0.46244 0.75489 0.78970 -0.02254 -0.03745 -0.02913 56   PHE A O   
2141 C CB  . PHE B 57  ? 0.45009 0.76186 0.75240 -0.00724 -0.04861 -0.03628 56   PHE A CB  
2142 C CG  . PHE B 57  ? 0.44334 0.77091 0.73600 0.00027  -0.05160 -0.03660 56   PHE A CG  
2143 C CD1 . PHE B 57  ? 0.42326 0.76753 0.72326 -0.00083 -0.05216 -0.03052 56   PHE A CD1 
2144 C CD2 . PHE B 57  ? 0.41852 0.74435 0.69396 0.00830  -0.05385 -0.04292 56   PHE A CD2 
2145 C CE1 . PHE B 57  ? 0.42265 0.78275 0.71362 0.00343  -0.05504 -0.03004 56   PHE A CE1 
2146 C CE2 . PHE B 57  ? 0.40054 0.74606 0.66851 0.01434  -0.05616 -0.04271 56   PHE A CE2 
2147 C CZ  . PHE B 57  ? 0.41976 0.78298 0.69588 0.01063  -0.05680 -0.03588 56   PHE A CZ  
2148 N N   . PRO B 58  ? 0.48314 0.73829 0.77745 -0.01328 -0.03411 -0.03528 57   PRO A N   
2149 C CA  . PRO B 58  ? 0.46714 0.70845 0.76813 -0.02538 -0.03249 -0.03520 57   PRO A CA  
2150 C C   . PRO B 58  ? 0.49493 0.74411 0.80272 -0.03465 -0.04130 -0.04060 57   PRO A C   
2151 O O   . PRO B 58  ? 0.50475 0.76310 0.80614 -0.03005 -0.04833 -0.04574 57   PRO A O   
2152 C CB  . PRO B 58  ? 0.49445 0.70280 0.77282 -0.02083 -0.02886 -0.03743 57   PRO A CB  
2153 C CG  . PRO B 58  ? 0.49708 0.70529 0.75725 -0.00575 -0.03200 -0.04195 57   PRO A CG  
2154 C CD  . PRO B 58  ? 0.47350 0.71121 0.74483 -0.00122 -0.03219 -0.03800 57   PRO A CD  
2155 N N   . THR B 59  ? 0.49117 0.73926 0.81250 -0.04860 -0.04092 -0.03909 58   THR A N   
2156 C CA  . THR B 59  ? 0.49450 0.75402 0.82504 -0.05916 -0.04988 -0.04346 58   THR A CA  
2157 C C   . THR B 59  ? 0.52634 0.76425 0.83423 -0.05840 -0.05648 -0.05321 58   THR A C   
2158 O O   . THR B 59  ? 0.52359 0.77257 0.83316 -0.06267 -0.06531 -0.05849 58   THR A O   
2159 C CB  . THR B 59  ? 0.46629 0.73094 0.81609 -0.07525 -0.04796 -0.03958 58   THR A CB  
2160 O OG1 . THR B 59  ? 0.56711 0.80000 0.90220 -0.08270 -0.04493 -0.04157 58   THR A OG1 
2161 C CG2 . THR B 59  ? 0.44081 0.72291 0.80935 -0.07316 -0.03946 -0.03051 58   THR A CG2 
2162 N N   . ASP B 60  ? 0.56071 0.76687 0.84592 -0.05221 -0.05254 -0.05583 59   ASP A N   
2163 C CA  . ASP B 60  ? 0.58994 0.77007 0.84951 -0.04827 -0.05792 -0.06566 59   ASP A CA  
2164 C C   . ASP B 60  ? 0.56939 0.74693 0.80998 -0.02800 -0.05675 -0.06856 59   ASP A C   
2165 O O   . ASP B 60  ? 0.60773 0.75609 0.82357 -0.01888 -0.05627 -0.07382 59   ASP A O   
2166 C CB  . ASP B 60  ? 0.66880 0.80997 0.91373 -0.05688 -0.05555 -0.06701 59   ASP A CB  
2167 C CG  . ASP B 60  ? 0.68426 0.80808 0.92242 -0.05042 -0.04554 -0.05983 59   ASP A CG  
2168 O OD1 . ASP B 60  ? 0.63074 0.77660 0.88574 -0.04796 -0.03933 -0.05172 59   ASP A OD1 
2169 O OD2 . ASP B 60  ? 0.80468 0.89060 1.01852 -0.04740 -0.04420 -0.06247 59   ASP A OD2 
2170 N N   . TYR B 61  ? 0.55105 0.75932 0.80294 -0.02079 -0.05619 -0.06459 60   TYR A N   
2171 C CA  . TYR B 61  ? 0.52914 0.74517 0.76656 -0.00411 -0.05679 -0.06757 60   TYR A CA  
2172 C C   . TYR B 61  ? 0.55533 0.76931 0.77843 -0.00138 -0.06471 -0.07800 60   TYR A C   
2173 O O   . TYR B 61  ? 0.56582 0.78734 0.79759 -0.01320 -0.07096 -0.08084 60   TYR A O   
2174 C CB  . TYR B 61  ? 0.48673 0.73689 0.74075 -0.00220 -0.05593 -0.06076 60   TYR A CB  
2175 C CG  . TYR B 61  ? 0.44828 0.71479 0.69186 0.01172  -0.05643 -0.06181 60   TYR A CG  
2176 C CD1 . TYR B 61  ? 0.40025 0.66128 0.63358 0.02347  -0.05073 -0.05911 60   TYR A CD1 
2177 C CD2 . TYR B 61  ? 0.45485 0.74553 0.69969 0.01213  -0.06270 -0.06464 60   TYR A CD2 
2178 C CE1 . TYR B 61  ? 0.42285 0.70403 0.64853 0.03487  -0.05150 -0.05962 60   TYR A CE1 
2179 C CE2 . TYR B 61  ? 0.44644 0.75617 0.68303 0.02288  -0.06287 -0.06482 60   TYR A CE2 
2180 C CZ  . TYR B 61  ? 0.43212 0.73844 0.65992 0.03397  -0.05737 -0.06242 60   TYR A CZ  
2181 O OH  . TYR B 61  ? 0.38424 0.71483 0.60551 0.04324  -0.05804 -0.06234 60   TYR A OH  
2182 N N   . PRO B 62  ? 0.56552 0.77082 0.76609 0.01492  -0.06473 -0.08411 61   PRO A N   
2183 C CA  . PRO B 62  ? 0.54415 0.74564 0.73320 0.03118  -0.05883 -0.08150 61   PRO A CA  
2184 C C   . PRO B 62  ? 0.58344 0.74333 0.75144 0.03768  -0.05553 -0.08401 61   PRO A C   
2185 O O   . PRO B 62  ? 0.58640 0.74094 0.74054 0.05397  -0.05194 -0.08334 61   PRO A O   
2186 C CB  . PRO B 62  ? 0.53440 0.75718 0.71241 0.04488  -0.06234 -0.08757 61   PRO A CB  
2187 C CG  . PRO B 62  ? 0.58571 0.79350 0.75209 0.04082  -0.06904 -0.09808 61   PRO A CG  
2188 C CD  . PRO B 62  ? 0.57295 0.77624 0.75742 0.01950  -0.07158 -0.09500 61   PRO A CD  
2189 N N   . PHE B 63  ? 0.61293 0.74318 0.77750 0.02482  -0.05707 -0.08641 62   PHE A N   
2190 C CA  . PHE B 63  ? 0.64994 0.73560 0.79226 0.02891  -0.05426 -0.08783 62   PHE A CA  
2191 C C   . PHE B 63  ? 0.65834 0.73791 0.80641 0.02867  -0.04601 -0.07712 62   PHE A C   
2192 O O   . PHE B 63  ? 0.65131 0.69815 0.77850 0.03767  -0.04284 -0.07654 62   PHE A O   
2193 C CB  . PHE B 63  ? 0.69091 0.74696 0.82750 0.01188  -0.05883 -0.09299 62   PHE A CB  
2194 C CG  . PHE B 63  ? 0.74414 0.80206 0.87091 0.01242  -0.06739 -0.10461 62   PHE A CG  
2195 C CD1 . PHE B 63  ? 0.79493 0.82767 0.89109 0.02953  -0.07000 -0.11479 62   PHE A CD1 
2196 C CD2 . PHE B 63  ? 0.76467 0.85070 0.91178 -0.00248 -0.07287 -0.10542 62   PHE A CD2 
2197 C CE1 . PHE B 63  ? 0.79520 0.82973 0.88025 0.03096  -0.07748 -0.12624 62   PHE A CE1 
2198 C CE2 . PHE B 63  ? 0.80621 0.89459 0.94264 -0.00192 -0.08091 -0.11612 62   PHE A CE2 
2199 C CZ  . PHE B 63  ? 0.83293 0.89538 0.93792 0.01451  -0.08298 -0.12684 62   PHE A CZ  
2200 N N   . LYS B 64  ? 0.62343 0.73289 0.79737 0.01991  -0.04261 -0.06875 63   LYS A N   
2201 C CA  . LYS B 64  ? 0.66435 0.77602 0.84320 0.02316  -0.03475 -0.05926 63   LYS A CA  
2202 C C   . LYS B 64  ? 0.56088 0.71011 0.75081 0.03208  -0.03410 -0.05607 63   LYS A C   
2203 O O   . LYS B 64  ? 0.54571 0.72336 0.74972 0.02779  -0.03850 -0.05771 63   LYS A O   
2204 C CB  . LYS B 64  ? 0.63706 0.74716 0.83425 0.00501  -0.02998 -0.05172 63   LYS A CB  
2205 C CG  . LYS B 64  ? 0.69132 0.76038 0.87141 0.00138  -0.02580 -0.04950 63   LYS A CG  
2206 C CD  . LYS B 64  ? 0.75861 0.81403 0.94545 -0.01942 -0.02776 -0.05047 63   LYS A CD  
2207 C CE  . LYS B 64  ? 0.83480 0.91695 1.05122 -0.03455 -0.02304 -0.04244 63   LYS A CE  
2208 N NZ  . LYS B 64  ? 0.88194 0.95106 1.10432 -0.05590 -0.02429 -0.04231 63   LYS A NZ  
2209 N N   . PRO B 65  ? 0.53777 0.68723 0.72022 0.04379  -0.02928 -0.05131 64   PRO A N   
2210 C CA  . PRO B 65  ? 0.51483 0.69820 0.70423 0.05170  -0.02955 -0.04889 64   PRO A CA  
2211 C C   . PRO B 65  ? 0.48546 0.69274 0.69912 0.03893  -0.02804 -0.04275 64   PRO A C   
2212 O O   . PRO B 65  ? 0.47199 0.67032 0.69710 0.02685  -0.02458 -0.03882 64   PRO A O   
2213 C CB  . PRO B 65  ? 0.51632 0.68918 0.69104 0.06498  -0.02468 -0.04466 64   PRO A CB  
2214 C CG  . PRO B 65  ? 0.53425 0.67388 0.70430 0.05778  -0.01961 -0.04077 64   PRO A CG  
2215 C CD  . PRO B 65  ? 0.56775 0.68673 0.73549 0.04817  -0.02341 -0.04683 64   PRO A CD  
2216 N N   . PRO B 66  ? 0.44028 0.67819 0.66171 0.04122  -0.03057 -0.04162 65   PRO A N   
2217 C CA  . PRO B 66  ? 0.45022 0.70607 0.69050 0.03189  -0.02878 -0.03522 65   PRO A CA  
2218 C C   . PRO B 66  ? 0.42970 0.68055 0.66644 0.03589  -0.02213 -0.02896 65   PRO A C   
2219 O O   . PRO B 66  ? 0.42156 0.66606 0.64248 0.04723  -0.02064 -0.02911 65   PRO A O   
2220 C CB  . PRO B 66  ? 0.42093 0.70666 0.66505 0.03333  -0.03454 -0.03635 65   PRO A CB  
2221 C CG  . PRO B 66  ? 0.39542 0.68356 0.62131 0.04749  -0.03581 -0.04044 65   PRO A CG  
2222 C CD  . PRO B 66  ? 0.41874 0.67642 0.63112 0.05228  -0.03506 -0.04586 65   PRO A CD  
2223 N N   . LYS B 67  ? 0.44259 0.69680 0.69356 0.02732  -0.01821 -0.02358 66   LYS A N   
2224 C CA  . LYS B 67  ? 0.45224 0.70314 0.70018 0.02994  -0.01186 -0.01789 66   LYS A CA  
2225 C C   . LYS B 67  ? 0.42715 0.70131 0.67836 0.03082  -0.01467 -0.01589 66   LYS A C   
2226 O O   . LYS B 67  ? 0.43428 0.72117 0.69923 0.02361  -0.01693 -0.01461 66   LYS A O   
2227 C CB  . LYS B 67  ? 0.47854 0.71894 0.73784 0.02118  -0.00514 -0.01366 66   LYS A CB  
2228 C CG  . LYS B 67  ? 0.53509 0.76964 0.78884 0.02421  0.00237  -0.00820 66   LYS A CG  
2229 C CD  . LYS B 67  ? 0.63994 0.86643 0.90461 0.01621  0.01034  -0.00399 66   LYS A CD  
2230 C CE  . LYS B 67  ? 0.67387 0.91838 0.96018 0.00893  0.00937  -0.00324 66   LYS A CE  
2231 N NZ  . LYS B 67  ? 0.71069 0.95276 1.00816 0.00325  0.01802  0.00103  66   LYS A NZ  
2232 N N   . VAL B 68  ? 0.38562 0.66506 0.62340 0.03936  -0.01506 -0.01536 67   VAL A N   
2233 C CA  . VAL B 68  ? 0.40566 0.70694 0.64354 0.03874  -0.01853 -0.01352 67   VAL A CA  
2234 C C   . VAL B 68  ? 0.41011 0.70591 0.64091 0.04051  -0.01371 -0.00915 67   VAL A C   
2235 O O   . VAL B 68  ? 0.43668 0.72017 0.65533 0.04811  -0.01013 -0.00846 67   VAL A O   
2236 C CB  . VAL B 68  ? 0.39625 0.71579 0.62497 0.04604  -0.02415 -0.01680 67   VAL A CB  
2237 C CG1 . VAL B 68  ? 0.37842 0.72185 0.60772 0.04194  -0.02791 -0.01398 67   VAL A CG1 
2238 C CG2 . VAL B 68  ? 0.39142 0.71414 0.62422 0.04529  -0.02852 -0.02205 67   VAL A CG2 
2239 N N   . ALA B 69  ? 0.39395 0.69736 0.63015 0.03395  -0.01410 -0.00629 68   ALA A N   
2240 C CA  . ALA B 69  ? 0.41300 0.71064 0.64043 0.03507  -0.01007 -0.00300 68   ALA A CA  
2241 C C   . ALA B 69  ? 0.41029 0.72254 0.63650 0.02926  -0.01485 -0.00150 68   ALA A C   
2242 O O   . ALA B 69  ? 0.39448 0.71501 0.62987 0.02273  -0.01914 -0.00157 68   ALA A O   
2243 C CB  . ALA B 69  ? 0.42460 0.70352 0.65729 0.03266  -0.00202 -0.00076 68   ALA A CB  
2244 N N   . PHE B 70  ? 0.41001 0.72453 0.62325 0.03114  -0.01467 0.00012  69   PHE A N   
2245 C CA  . PHE B 70  ? 0.42875 0.75214 0.63737 0.02371  -0.01892 0.00179  69   PHE A CA  
2246 C C   . PHE B 70  ? 0.42156 0.72732 0.63298 0.01906  -0.01482 0.00311  69   PHE A C   
2247 O O   . PHE B 70  ? 0.44080 0.73023 0.65213 0.02302  -0.00728 0.00347  69   PHE A O   
2248 C CB  . PHE B 70  ? 0.42572 0.75736 0.61879 0.02657  -0.02037 0.00280  69   PHE A CB  
2249 C CG  . PHE B 70  ? 0.40943 0.76755 0.59963 0.02962  -0.02649 0.00200  69   PHE A CG  
2250 C CD1 . PHE B 70  ? 0.42710 0.78801 0.61632 0.04125  -0.02525 0.00004  69   PHE A CD1 
2251 C CD2 . PHE B 70  ? 0.40421 0.78425 0.59130 0.02108  -0.03329 0.00331  69   PHE A CD2 
2252 C CE1 . PHE B 70  ? 0.42595 0.81337 0.61232 0.04652  -0.03030 -0.00117 69   PHE A CE1 
2253 C CE2 . PHE B 70  ? 0.43000 0.83939 0.61559 0.02416  -0.03817 0.00284  69   PHE A CE2 
2254 C CZ  . PHE B 70  ? 0.42887 0.84307 0.61455 0.03805  -0.03643 0.00032  69   PHE A CZ  
2255 N N   . THR B 71  ? 0.42848 0.73713 0.64116 0.01106  -0.01963 0.00406  70   THR A N   
2256 C CA  . THR B 71  ? 0.43204 0.72311 0.64215 0.00844  -0.01656 0.00491  70   THR A CA  
2257 C C   . THR B 71  ? 0.45530 0.74442 0.64793 0.00285  -0.02025 0.00559  70   THR A C   
2258 O O   . THR B 71  ? 0.51177 0.78279 0.69657 0.00258  -0.01688 0.00532  70   THR A O   
2259 C CB  . THR B 71  ? 0.42865 0.71724 0.65135 0.00462  -0.01908 0.00561  70   THR A CB  
2260 O OG1 . THR B 71  ? 0.43261 0.73645 0.65505 -0.00243 -0.02796 0.00671  70   THR A OG1 
2261 C CG2 . THR B 71  ? 0.41667 0.70570 0.65668 0.00916  -0.01484 0.00476  70   THR A CG2 
2262 N N   . THR B 72  ? 0.44204 0.75002 0.62752 -0.00117 -0.02668 0.00617  71   THR A N   
2263 C CA  . THR B 72  ? 0.45464 0.76455 0.62319 -0.00839 -0.03111 0.00693  71   THR A CA  
2264 C C   . THR B 72  ? 0.46533 0.77828 0.62377 -0.00144 -0.02783 0.00634  71   THR A C   
2265 O O   . THR B 72  ? 0.45106 0.77908 0.61366 0.00595  -0.02738 0.00624  71   THR A O   
2266 C CB  . THR B 72  ? 0.45141 0.78568 0.61923 -0.01816 -0.04029 0.00875  71   THR A CB  
2267 O OG1 . THR B 72  ? 0.45797 0.78765 0.63342 -0.02454 -0.04359 0.01012  71   THR A OG1 
2268 C CG2 . THR B 72  ? 0.48081 0.81978 0.63121 -0.02845 -0.04581 0.00989  71   THR A CG2 
2269 N N   . ARG B 73  ? 0.48205 0.77948 0.62562 -0.00297 -0.02582 0.00585  72   ARG A N   
2270 C CA  . ARG B 73  ? 0.50825 0.80904 0.63969 0.00295  -0.02376 0.00591  72   ARG A CA  
2271 C C   . ARG B 73  ? 0.50051 0.83177 0.62865 0.00074  -0.03144 0.00717  72   ARG A C   
2272 O O   . ARG B 73  ? 0.46514 0.81109 0.59165 -0.01073 -0.03910 0.00800  72   ARG A O   
2273 C CB  . ARG B 73  ? 0.54785 0.82997 0.66070 -0.00100 -0.02256 0.00479  72   ARG A CB  
2274 C CG  . ARG B 73  ? 0.61207 0.86707 0.72395 0.00512  -0.01296 0.00338  72   ARG A CG  
2275 C CD  . ARG B 73  ? 0.66193 0.91517 0.77040 0.01587  -0.00586 0.00441  72   ARG A CD  
2276 N NE  . ARG B 73  ? 0.73109 0.96107 0.83579 0.02081  0.00410  0.00350  72   ARG A NE  
2277 C CZ  . ARG B 73  ? 0.77899 0.99338 0.86563 0.01907  0.00598  0.00150  72   ARG A CZ  
2278 N NH1 . ARG B 73  ? 0.73853 0.95567 0.80858 0.01088  -0.00218 0.00012  72   ARG A NH1 
2279 N NH2 . ARG B 73  ? 0.84487 1.04130 0.92922 0.02524  0.01635  0.00075  72   ARG A NH2 
2280 N N   . ILE B 74  ? 0.49579 0.83673 0.62185 0.01186  -0.02936 0.00773  73   ILE A N   
2281 C CA  . ILE B 74  ? 0.48542 0.85854 0.60922 0.01371  -0.03586 0.00889  73   ILE A CA  
2282 C C   . ILE B 74  ? 0.49160 0.86399 0.60369 0.02537  -0.03329 0.00990  73   ILE A C   
2283 O O   . ILE B 74  ? 0.50736 0.85738 0.61830 0.03491  -0.02566 0.01000  73   ILE A O   
2284 C CB  . ILE B 74  ? 0.44988 0.84147 0.58876 0.01878  -0.03727 0.00841  73   ILE A CB  
2285 C CG1 . ILE B 74  ? 0.46925 0.89787 0.60631 0.02260  -0.04339 0.00934  73   ILE A CG1 
2286 C CG2 . ILE B 74  ? 0.43219 0.80539 0.57786 0.03181  -0.02987 0.00724  73   ILE A CG2 
2287 C CD1 . ILE B 74  ? 0.49385 0.94356 0.64379 0.02585  -0.04543 0.00821  73   ILE A CD1 
2288 N N   . TYR B 75  ? 0.49494 0.89220 0.59754 0.02357  -0.03990 0.01122  74   TYR A N   
2289 C CA  . TYR B 75  ? 0.51017 0.91125 0.60029 0.03503  -0.03930 0.01290  74   TYR A CA  
2290 C C   . TYR B 75  ? 0.53371 0.95878 0.63039 0.04974  -0.04097 0.01376  74   TYR A C   
2291 O O   . TYR B 75  ? 0.52691 0.98803 0.62653 0.04815  -0.04807 0.01435  74   TYR A O   
2292 C CB  . TYR B 75  ? 0.54654 0.96227 0.62200 0.02486  -0.04630 0.01371  74   TYR A CB  
2293 C CG  . TYR B 75  ? 0.57968 0.99749 0.63974 0.03562  -0.04627 0.01576  74   TYR A CG  
2294 C CD1 . TYR B 75  ? 0.57359 0.95982 0.61963 0.03764  -0.04017 0.01566  74   TYR A CD1 
2295 C CD2 . TYR B 75  ? 0.58970 1.04259 0.64869 0.04437  -0.05236 0.01804  74   TYR A CD2 
2296 C CE1 . TYR B 75  ? 0.60992 0.99750 0.64020 0.04734  -0.04042 0.01817  74   TYR A CE1 
2297 C CE2 . TYR B 75  ? 0.62218 1.07706 0.66636 0.05518  -0.05307 0.02055  74   TYR A CE2 
2298 C CZ  . TYR B 75  ? 0.62308 1.04441 0.65237 0.05613  -0.04730 0.02080  74   TYR A CZ  
2299 O OH  . TYR B 75  ? 0.65855 1.08203 0.67164 0.06681  -0.04840 0.02392  74   TYR A OH  
2300 N N   . HIS B 76  ? 0.53090 0.93579 0.62880 0.06421  -0.03436 0.01385  75   HIS A N   
2301 C CA  . HIS B 76  ? 0.52449 0.94296 0.62694 0.07994  -0.03509 0.01361  75   HIS A CA  
2302 C C   . HIS B 76  ? 0.55034 0.94128 0.64301 0.09555  -0.02895 0.01534  75   HIS A C   
2303 O O   . HIS B 76  ? 0.55449 0.91259 0.64560 0.09234  -0.02178 0.01577  75   HIS A O   
2304 C CB  . HIS B 76  ? 0.52143 0.94115 0.64000 0.07704  -0.03437 0.01055  75   HIS A CB  
2305 C CG  . HIS B 76  ? 0.52686 0.96668 0.64911 0.09151  -0.03669 0.00900  75   HIS A CG  
2306 N ND1 . HIS B 76  ? 0.53617 0.95451 0.65516 0.10709  -0.03236 0.00796  75   HIS A ND1 
2307 C CD2 . HIS B 76  ? 0.53694 1.01592 0.66464 0.09293  -0.04269 0.00809  75   HIS A CD2 
2308 C CE1 . HIS B 76  ? 0.54658 0.98784 0.66772 0.11902  -0.03573 0.00575  75   HIS A CE1 
2309 N NE2 . HIS B 76  ? 0.53879 1.01929 0.66610 0.11117  -0.04163 0.00586  75   HIS A NE2 
2310 N N   . PRO B 77  ? 0.55085 0.95415 0.63646 0.11266  -0.03143 0.01667  76   PRO A N   
2311 C CA  . PRO B 77  ? 0.58519 0.95827 0.65831 0.12757  -0.02612 0.01922  76   PRO A CA  
2312 C C   . PRO B 77  ? 0.60524 0.94713 0.68468 0.12956  -0.01971 0.01727  76   PRO A C   
2313 O O   . PRO B 77  ? 0.64872 0.95845 0.71793 0.13561  -0.01392 0.01998  76   PRO A O   
2314 C CB  . PRO B 77  ? 0.61399 1.01161 0.67912 0.14654  -0.03187 0.02057  76   PRO A CB  
2315 C CG  . PRO B 77  ? 0.61002 1.05254 0.68041 0.13847  -0.03976 0.02025  76   PRO A CG  
2316 C CD  . PRO B 77  ? 0.58247 1.02895 0.66878 0.11922  -0.03945 0.01680  76   PRO A CD  
2317 N N   . ASN B 78  ? 0.56069 0.91157 0.65544 0.12440  -0.02094 0.01299  77   ASN A N   
2318 C CA  . ASN B 78  ? 0.55901 0.88308 0.65947 0.12587  -0.01622 0.01061  77   ASN A CA  
2319 C C   . ASN B 78  ? 0.52518 0.83901 0.64043 0.10859  -0.01274 0.00892  77   ASN A C   
2320 O O   . ASN B 78  ? 0.50609 0.80387 0.62908 0.10727  -0.01010 0.00647  77   ASN A O   
2321 C CB  . ASN B 78  ? 0.57440 0.91424 0.67859 0.13689  -0.02046 0.00639  77   ASN A CB  
2322 C CG  . ASN B 78  ? 0.67149 1.02431 0.76183 0.15674  -0.02416 0.00771  77   ASN A CG  
2323 O OD1 . ASN B 78  ? 0.66310 1.05436 0.75535 0.15962  -0.02992 0.00768  77   ASN A OD1 
2324 N ND2 . ASN B 78  ? 0.77602 1.09721 0.85164 0.17053  -0.02107 0.00940  77   ASN A ND2 
2325 N N   . ILE B 79  ? 0.51835 0.83975 0.63652 0.09583  -0.01301 0.01005  78   ILE A N   
2326 C CA  . ILE B 79  ? 0.49052 0.80205 0.62138 0.08142  -0.00992 0.00880  78   ILE A CA  
2327 C C   . ILE B 79  ? 0.48694 0.78234 0.60994 0.07564  -0.00491 0.01150  78   ILE A C   
2328 O O   . ILE B 79  ? 0.47274 0.78007 0.58642 0.07293  -0.00828 0.01258  78   ILE A O   
2329 C CB  . ILE B 79  ? 0.44666 0.78426 0.58852 0.07114  -0.01637 0.00657  78   ILE A CB  
2330 C CG1 . ILE B 79  ? 0.47064 0.82592 0.61948 0.07733  -0.02061 0.00359  78   ILE A CG1 
2331 C CG2 . ILE B 79  ? 0.43010 0.75464 0.58276 0.05829  -0.01349 0.00595  78   ILE A CG2 
2332 C CD1 . ILE B 79  ? 0.42722 0.81787 0.58043 0.07135  -0.02803 0.00292  78   ILE A CD1 
2333 N N   . ASN B 80  ? 0.48562 0.75531 0.61187 0.07335  0.00310  0.01239  79   ASN A N   
2334 C CA  . ASN B 80  ? 0.50162 0.75530 0.61940 0.06980  0.00947  0.01475  79   ASN A CA  
2335 C C   . ASN B 80  ? 0.50617 0.76035 0.63334 0.05812  0.01032  0.01267  79   ASN A C   
2336 O O   . ASN B 80  ? 0.49426 0.76083 0.63392 0.05204  0.00540  0.01019  79   ASN A O   
2337 C CB  . ASN B 80  ? 0.51815 0.74566 0.63239 0.07395  0.01855  0.01778  79   ASN A CB  
2338 C CG  . ASN B 80  ? 0.50970 0.72783 0.64187 0.06817  0.02272  0.01636  79   ASN A CG  
2339 O OD1 . ASN B 80  ? 0.52468 0.75319 0.67191 0.06091  0.02016  0.01336  79   ASN A OD1 
2340 N ND2 . ASN B 80  ? 0.49945 0.69743 0.62904 0.07061  0.02891  0.01903  79   ASN A ND2 
2341 N N   . SER B 81  ? 0.52092 0.75997 0.64042 0.05591  0.01690  0.01383  80   SER A N   
2342 C CA  . SER B 81  ? 0.53577 0.77109 0.65928 0.04761  0.01826  0.01168  80   SER A CA  
2343 C C   . SER B 81  ? 0.51439 0.74486 0.65790 0.04407  0.02211  0.01060  80   SER A C   
2344 O O   . SER B 81  ? 0.54253 0.77163 0.69131 0.03860  0.02171  0.00870  80   SER A O   
2345 C CB  . SER B 81  ? 0.57267 0.79257 0.68026 0.04866  0.02520  0.01266  80   SER A CB  
2346 O OG  . SER B 81  ? 0.61059 0.81527 0.72087 0.05245  0.03569  0.01530  80   SER A OG  
2347 N N   . ASN B 82  ? 0.51499 0.74148 0.66839 0.04705  0.02559  0.01184  81   ASN A N   
2348 C CA  . ASN B 82  ? 0.52706 0.75378 0.70071 0.04276  0.02730  0.01070  81   ASN A CA  
2349 C C   . ASN B 82  ? 0.48630 0.72881 0.67054 0.04040  0.01810  0.00832  81   ASN A C   
2350 O O   . ASN B 82  ? 0.46254 0.70747 0.66326 0.03668  0.01778  0.00725  81   ASN A O   
2351 C CB  . ASN B 82  ? 0.53631 0.75052 0.71502 0.04445  0.03529  0.01315  81   ASN A CB  
2352 C CG  . ASN B 82  ? 0.63562 0.83655 0.80759 0.04498  0.04616  0.01602  81   ASN A CG  
2353 O OD1 . ASN B 82  ? 0.69678 0.89684 0.86225 0.04474  0.04823  0.01514  81   ASN A OD1 
2354 N ND2 . ASN B 82  ? 0.70629 0.89557 0.87726 0.04561  0.05304  0.01949  81   ASN A ND2 
2355 N N   . GLY B 83  ? 0.46994 0.72568 0.64517 0.04235  0.01060  0.00762  82   GLY A N   
2356 C CA  . GLY B 83  ? 0.45285 0.72592 0.63648 0.04080  0.00270  0.00554  82   GLY A CA  
2357 C C   . GLY B 83  ? 0.46117 0.73312 0.64801 0.04707  0.00258  0.00452  82   GLY A C   
2358 O O   . GLY B 83  ? 0.46658 0.75273 0.65972 0.04683  -0.00340 0.00213  82   GLY A O   
2359 N N   . SER B 84  ? 0.47451 0.72838 0.65535 0.05241  0.00896  0.00623  83   SER A N   
2360 C CA  . SER B 84  ? 0.48125 0.72784 0.66030 0.05881  0.00851  0.00513  83   SER A CA  
2361 C C   . SER B 84  ? 0.48238 0.74257 0.64955 0.06867  0.00229  0.00404  83   SER A C   
2362 O O   . SER B 84  ? 0.47803 0.74723 0.63429 0.07196  0.00070  0.00591  83   SER A O   
2363 C CB  . SER B 84  ? 0.51073 0.73191 0.68226 0.06124  0.01668  0.00844  83   SER A CB  
2364 O OG  . SER B 84  ? 0.54229 0.75402 0.72790 0.05273  0.02203  0.00885  83   SER A OG  
2365 N N   . ILE B 85  ? 0.47289 0.73487 0.64148 0.07403  -0.00118 0.00078  84   ILE A N   
2366 C CA  . ILE B 85  ? 0.48692 0.76585 0.64648 0.08520  -0.00705 -0.00113 84   ILE A CA  
2367 C C   . ILE B 85  ? 0.51346 0.77013 0.65962 0.09784  -0.00513 -0.00140 84   ILE A C   
2368 O O   . ILE B 85  ? 0.53714 0.77277 0.68596 0.09581  -0.00288 -0.00325 84   ILE A O   
2369 C CB  . ILE B 85  ? 0.46833 0.77053 0.63880 0.08217  -0.01326 -0.00548 84   ILE A CB  
2370 C CG1 . ILE B 85  ? 0.44241 0.75946 0.62458 0.06822  -0.01501 -0.00422 84   ILE A CG1 
2371 C CG2 . ILE B 85  ? 0.45608 0.78141 0.61777 0.09464  -0.01857 -0.00737 84   ILE A CG2 
2372 C CD1 . ILE B 85  ? 0.39786 0.73203 0.59193 0.06202  -0.02008 -0.00726 84   ILE A CD1 
2373 N N   . CYS B 86  ? 0.52041 0.78050 0.65107 0.11051  -0.00645 0.00072  85   CYS A N   
2374 C CA  . CYS B 86  ? 0.54920 0.78808 0.66368 0.12562  -0.00597 0.00063  85   CYS A CA  
2375 C C   . CYS B 86  ? 0.55817 0.81839 0.67099 0.13795  -0.01242 -0.00459 85   CYS A C   
2376 O O   . CYS B 86  ? 0.55751 0.84405 0.66495 0.14804  -0.01648 -0.00397 85   CYS A O   
2377 C CB  . CYS B 86  ? 0.58792 0.81810 0.68526 0.13439  -0.00394 0.00642  85   CYS A CB  
2378 S SG  . CYS B 86  ? 0.69888 0.90190 0.77282 0.15555  -0.00451 0.00730  85   CYS A SG  
2379 N N   . LEU B 87  ? 0.54312 0.79388 0.66048 0.13712  -0.01338 -0.00997 86   LEU A N   
2380 C CA  . LEU B 87  ? 0.58081 0.85193 0.69683 0.14837  -0.01874 -0.01595 86   LEU A CA  
2381 C C   . LEU B 87  ? 0.61621 0.85562 0.72478 0.15301  -0.01832 -0.02117 86   LEU A C   
2382 O O   . LEU B 87  ? 0.58424 0.80960 0.70294 0.13882  -0.01685 -0.02294 86   LEU A O   
2383 C CB  . LEU B 87  ? 0.55672 0.86386 0.69049 0.13678  -0.02227 -0.01817 86   LEU A CB  
2384 C CG  . LEU B 87  ? 0.57294 0.90683 0.70664 0.14662  -0.02717 -0.02414 86   LEU A CG  
2385 C CD1 . LEU B 87  ? 0.58520 0.93642 0.70536 0.16750  -0.02936 -0.02409 86   LEU A CD1 
2386 C CD2 . LEU B 87  ? 0.52784 0.89648 0.67797 0.13196  -0.03017 -0.02382 86   LEU A CD2 
2387 N N   . ASP B 88  ? 0.65459 0.88246 0.74461 0.17309  -0.02004 -0.02372 87   ASP A N   
2388 C CA  . ASP B 88  ? 0.68166 0.87055 0.75869 0.17838  -0.01983 -0.02867 87   ASP A CA  
2389 C C   . ASP B 88  ? 0.67777 0.87410 0.76598 0.16958  -0.02253 -0.03631 87   ASP A C   
2390 O O   . ASP B 88  ? 0.67333 0.83696 0.75798 0.16246  -0.02187 -0.03951 87   ASP A O   
2391 C CB  . ASP B 88  ? 0.72543 0.90379 0.77912 0.20448  -0.02208 -0.03070 87   ASP A CB  
2392 C CG  . ASP B 88  ? 0.84823 1.07342 0.90546 0.21862  -0.02633 -0.03410 87   ASP A CG  
2393 O OD1 . ASP B 88  ? 0.82411 1.08848 0.90099 0.20597  -0.02745 -0.03363 87   ASP A OD1 
2394 O OD2 . ASP B 88  ? 0.96996 1.19299 1.00992 0.24232  -0.02852 -0.03697 87   ASP A OD2 
2395 N N   . ILE B 89  ? 0.63185 0.87123 0.73335 0.16807  -0.02576 -0.03871 88   ILE A N   
2396 C CA  . ILE B 89  ? 0.64124 0.89219 0.75336 0.15928  -0.02866 -0.04515 88   ILE A CA  
2397 C C   . ILE B 89  ? 0.61443 0.84759 0.74047 0.13731  -0.02674 -0.04348 88   ILE A C   
2398 O O   . ILE B 89  ? 0.60749 0.83432 0.73760 0.13020  -0.02908 -0.04908 88   ILE A O   
2399 C CB  . ILE B 89  ? 0.61437 0.91701 0.73950 0.15765  -0.03167 -0.04487 88   ILE A CB  
2400 C CG1 . ILE B 89  ? 0.68967 1.01668 0.80298 0.17969  -0.03350 -0.04642 88   ILE A CG1 
2401 C CG2 . ILE B 89  ? 0.59353 0.91030 0.72921 0.14773  -0.03477 -0.05036 88   ILE A CG2 
2402 C CD1 . ILE B 89  ? 0.65158 0.96549 0.74820 0.19875  -0.03513 -0.05517 88   ILE A CD1 
2403 N N   . LEU B 90  ? 0.58898 0.81521 0.72206 0.12696  -0.02256 -0.03600 89   LEU A N   
2404 C CA  . LEU B 90  ? 0.57154 0.78712 0.71994 0.10740  -0.02017 -0.03374 89   LEU A CA  
2405 C C   . LEU B 90  ? 0.60091 0.77410 0.74066 0.10341  -0.01670 -0.03323 89   LEU A C   
2406 O O   . LEU B 90  ? 0.59955 0.76483 0.75237 0.08727  -0.01494 -0.03208 89   LEU A O   
2407 C CB  . LEU B 90  ? 0.53251 0.76473 0.69330 0.09806  -0.01702 -0.02643 89   LEU A CB  
2408 C CG  . LEU B 90  ? 0.49138 0.76303 0.66374 0.09462  -0.02100 -0.02642 89   LEU A CG  
2409 C CD1 . LEU B 90  ? 0.47619 0.75725 0.65553 0.08665  -0.01818 -0.01981 89   LEU A CD1 
2410 C CD2 . LEU B 90  ? 0.45799 0.73830 0.64423 0.08356  -0.02441 -0.03023 89   LEU A CD2 
2411 N N   . ARG B 91  ? 0.65063 0.79694 0.76840 0.11741  -0.01594 -0.03367 90   ARG A N   
2412 C CA  . ARG B 91  ? 0.69555 0.79816 0.80208 0.11218  -0.01303 -0.03263 90   ARG A CA  
2413 C C   . ARG B 91  ? 0.71404 0.78656 0.79488 0.12830  -0.01626 -0.03860 90   ARG A C   
2414 O O   . ARG B 91  ? 0.71664 0.77342 0.79372 0.12449  -0.01970 -0.04578 90   ARG A O   
2415 C CB  . ARG B 91  ? 0.69306 0.78114 0.79594 0.10897  -0.00642 -0.02324 90   ARG A CB  
2416 C CG  . ARG B 91  ? 0.76994 0.81840 0.86675 0.09680  -0.00251 -0.02062 90   ARG A CG  
2417 C CD  . ARG B 91  ? 0.84962 0.88337 0.93950 0.09507  0.00458  -0.01096 90   ARG A CD  
2418 N NE  . ARG B 91  ? 0.85971 0.86769 0.95235 0.07717  0.00961  -0.00706 90   ARG A NE  
2419 C CZ  . ARG B 91  ? 0.91217 0.93565 1.02592 0.06066  0.01484  -0.00282 90   ARG A CZ  
2420 N NH1 . ARG B 91  ? 0.90580 0.96560 1.03807 0.05972  0.01550  -0.00216 90   ARG A NH1 
2421 N NH2 . ARG B 91  ? 0.91847 0.92035 1.03400 0.04473  0.01950  0.00093  90   ARG A NH2 
2422 N N   . SER B 92  ? 0.72366 0.78646 0.78528 0.14684  -0.01552 -0.03578 91   SER A N   
2423 C CA  . SER B 92  ? 0.71661 0.74307 0.75002 0.16425  -0.01804 -0.04037 91   SER A CA  
2424 C C   . SER B 92  ? 0.75530 0.79830 0.78444 0.17816  -0.02382 -0.05103 91   SER A C   
2425 O O   . SER B 92  ? 0.80621 0.81689 0.81829 0.18272  -0.02669 -0.05847 91   SER A O   
2426 C CB  . SER B 92  ? 0.65357 0.66941 0.66852 0.18194  -0.01608 -0.03362 91   SER A CB  
2427 O OG  . SER B 92  ? 0.71920 0.77864 0.73947 0.19700  -0.01829 -0.03377 91   SER A OG  
2428 N N   . GLN B 93  ? 0.72308 0.81513 0.76552 0.18494  -0.02555 -0.05199 92   GLN A N   
2429 C CA  . GLN B 93  ? 0.74281 0.85743 0.78274 0.19758  -0.03012 -0.06144 92   GLN A CA  
2430 C C   . GLN B 93  ? 0.72581 0.86210 0.78601 0.17917  -0.03226 -0.06591 92   GLN A C   
2431 O O   . GLN B 93  ? 0.71186 0.87956 0.77543 0.18617  -0.03543 -0.07193 92   GLN A O   
2432 C CB  . GLN B 93  ? 0.74260 0.90188 0.78476 0.21503  -0.03105 -0.05972 92   GLN A CB  
2433 C CG  . GLN B 93  ? 0.79705 0.94027 0.81595 0.24024  -0.03093 -0.05791 92   GLN A CG  
2434 C CD  . GLN B 93  ? 0.85704 0.96590 0.85024 0.25936  -0.03345 -0.06713 92   GLN A CD  
2435 O OE1 . GLN B 93  ? 0.99081 1.04619 0.96698 0.25623  -0.03290 -0.06789 92   GLN A OE1 
2436 N NE2 . GLN B 93  ? 0.86962 1.00857 0.85861 0.27912  -0.03617 -0.07433 92   GLN A NE2 
2437 N N   . TRP B 94  ? 0.70384 0.82583 0.77726 0.15637  -0.03063 -0.06284 93   TRP A N   
2438 C CA  . TRP B 94  ? 0.66556 0.80657 0.75669 0.14044  -0.03355 -0.06698 93   TRP A CA  
2439 C C   . TRP B 94  ? 0.69342 0.81156 0.76922 0.14462  -0.03796 -0.07787 93   TRP A C   
2440 O O   . TRP B 94  ? 0.73004 0.80281 0.78653 0.14680  -0.03802 -0.08060 93   TRP A O   
2441 C CB  . TRP B 94  ? 0.62934 0.76370 0.73942 0.11638  -0.03097 -0.06106 93   TRP A CB  
2442 C CG  . TRP B 94  ? 0.59493 0.74676 0.72104 0.10201  -0.03512 -0.06563 93   TRP A CG  
2443 C CD1 . TRP B 94  ? 0.60220 0.73147 0.72741 0.09015  -0.03792 -0.07070 93   TRP A CD1 
2444 C CD2 . TRP B 94  ? 0.55594 0.75114 0.69987 0.09765  -0.03755 -0.06509 93   TRP A CD2 
2445 N NE1 . TRP B 94  ? 0.57385 0.73117 0.71559 0.07994  -0.04211 -0.07342 93   TRP A NE1 
2446 C CE2 . TRP B 94  ? 0.53103 0.72764 0.68388 0.08447  -0.04179 -0.06974 93   TRP A CE2 
2447 C CE3 . TRP B 94  ? 0.54037 0.77249 0.69246 0.10247  -0.03701 -0.06073 93   TRP A CE3 
2448 C CZ2 . TRP B 94  ? 0.50773 0.73995 0.67632 0.07748  -0.04531 -0.06972 93   TRP A CZ2 
2449 C CZ3 . TRP B 94  ? 0.49743 0.76322 0.66468 0.09407  -0.04033 -0.06074 93   TRP A CZ3 
2450 C CH2 . TRP B 94  ? 0.49128 0.75642 0.66633 0.08231  -0.04434 -0.06495 93   TRP A CH2 
2451 N N   . SER B 95  ? 0.65294 0.80109 0.73566 0.14490  -0.04184 -0.08406 94   SER A N   
2452 C CA  . SER B 95  ? 0.65349 0.78389 0.72387 0.14543  -0.04648 -0.09499 94   SER A CA  
2453 C C   . SER B 95  ? 0.60268 0.75794 0.69459 0.12548  -0.04967 -0.09576 94   SER A C   
2454 O O   . SER B 95  ? 0.57256 0.76878 0.68381 0.12044  -0.04920 -0.09046 94   SER A O   
2455 C CB  . SER B 95  ? 0.66236 0.80475 0.71434 0.16996  -0.04855 -0.10372 94   SER A CB  
2456 O OG  . SER B 95  ? 0.65221 0.79057 0.69812 0.16647  -0.05329 -0.11414 94   SER A OG  
2457 N N   . PRO B 96  ? 0.61042 0.74129 0.69876 0.11324  -0.05346 -0.10184 95   PRO A N   
2458 C CA  . PRO B 96  ? 0.60279 0.75956 0.71024 0.09633  -0.05759 -0.10292 95   PRO A CA  
2459 C C   . PRO B 96  ? 0.59957 0.79125 0.70471 0.10635  -0.06089 -0.10894 95   PRO A C   
2460 O O   . PRO B 96  ? 0.59014 0.80735 0.71055 0.09364  -0.06443 -0.10859 95   PRO A O   
2461 C CB  . PRO B 96  ? 0.62374 0.74344 0.72338 0.08282  -0.06155 -0.10901 95   PRO A CB  
2462 C CG  . PRO B 96  ? 0.66308 0.73946 0.73297 0.09744  -0.06087 -0.11487 95   PRO A CG  
2463 C CD  . PRO B 96  ? 0.62324 0.70141 0.68921 0.11308  -0.05482 -0.10760 95   PRO A CD  
2464 N N   . ALA B 97  ? 0.58875 0.78412 0.67532 0.12895  -0.05980 -0.11399 96   ALA A N   
2465 C CA  . ALA B 97  ? 0.58848 0.82453 0.67490 0.13838  -0.06160 -0.11819 96   ALA A CA  
2466 C C   . ALA B 97  ? 0.57790 0.85935 0.68284 0.13799  -0.05864 -0.10820 96   ALA A C   
2467 O O   . ALA B 97  ? 0.58027 0.90082 0.68830 0.14197  -0.05980 -0.10938 96   ALA A O   
2468 C CB  . ALA B 97  ? 0.61569 0.84050 0.67415 0.16414  -0.06160 -0.12876 96   ALA A CB  
2469 N N   . LEU B 98  ? 0.56993 0.84673 0.68617 0.13197  -0.05498 -0.09840 97   LEU A N   
2470 C CA  . LEU B 98  ? 0.53609 0.85045 0.66798 0.12961  -0.05267 -0.08898 97   LEU A CA  
2471 C C   . LEU B 98  ? 0.50388 0.83623 0.65813 0.10760  -0.05466 -0.08292 97   LEU A C   
2472 O O   . LEU B 98  ? 0.50419 0.81646 0.66486 0.09394  -0.05656 -0.08371 97   LEU A O   
2473 C CB  . LEU B 98  ? 0.53061 0.82912 0.66106 0.13450  -0.04804 -0.08196 97   LEU A CB  
2474 C CG  . LEU B 98  ? 0.55678 0.84711 0.66681 0.15887  -0.04610 -0.08492 97   LEU A CG  
2475 C CD1 . LEU B 98  ? 0.59860 0.85899 0.70397 0.16070  -0.04226 -0.07853 97   LEU A CD1 
2476 C CD2 . LEU B 98  ? 0.57531 0.91398 0.68819 0.17011  -0.04604 -0.08319 97   LEU A CD2 
2477 N N   . THR B 99  ? 0.48784 0.85876 0.65310 0.10427  -0.05470 -0.07683 98   THR A N   
2478 C CA  . THR B 99  ? 0.45583 0.84421 0.63958 0.08556  -0.05709 -0.07064 98   THR A CA  
2479 C C   . THR B 99  ? 0.44811 0.84694 0.64334 0.07913  -0.05421 -0.06046 98   THR A C   
2480 O O   . THR B 99  ? 0.44244 0.84383 0.63178 0.08892  -0.05094 -0.05814 98   THR A O   
2481 C CB  . THR B 99  ? 0.46129 0.88460 0.64511 0.08420  -0.06103 -0.07272 98   THR A CB  
2482 O OG1 . THR B 99  ? 0.45066 0.90626 0.63042 0.09392  -0.05924 -0.07043 98   THR A OG1 
2483 C CG2 . THR B 99  ? 0.47636 0.88857 0.64635 0.09135  -0.06389 -0.08384 98   THR A CG2 
2484 N N   . ILE B 100 ? 0.42567 0.83033 0.63627 0.06301  -0.05593 -0.05455 99   ILE A N   
2485 C CA  . ILE B 100 ? 0.41474 0.82800 0.63426 0.05619  -0.05383 -0.04563 99   ILE A CA  
2486 C C   . ILE B 100 ? 0.41664 0.86238 0.63106 0.06136  -0.05421 -0.04318 99   ILE A C   
2487 O O   . ILE B 100 ? 0.42128 0.87016 0.63479 0.06323  -0.05159 -0.03852 99   ILE A O   
2488 C CB  . ILE B 100 ? 0.41756 0.83288 0.65220 0.04002  -0.05648 -0.04031 99   ILE A CB  
2489 C CG1 . ILE B 100 ? 0.42533 0.81185 0.66728 0.03502  -0.05514 -0.04157 99   ILE A CG1 
2490 C CG2 . ILE B 100 ? 0.40211 0.82551 0.64237 0.03359  -0.05496 -0.03194 99   ILE A CG2 
2491 C CD1 . ILE B 100 ? 0.40759 0.77133 0.64806 0.03860  -0.04886 -0.03926 99   ILE A CD1 
2492 N N   . SER B 101 ? 0.41373 0.88584 0.62438 0.06324  -0.05749 -0.04623 100  SER A N   
2493 C CA  A SER B 101 ? 0.41952 0.92811 0.62650 0.06670  -0.05777 -0.04348 100  SER A CA  
2494 C CA  B SER B 101 ? 0.40036 0.90911 0.60721 0.06687  -0.05779 -0.04362 100  SER A CA  
2495 C C   . SER B 101 ? 0.38973 0.89942 0.58638 0.08442  -0.05431 -0.04621 100  SER A C   
2496 O O   . SER B 101 ? 0.40739 0.93607 0.60443 0.08487  -0.05342 -0.04102 100  SER A O   
2497 C CB  A SER B 101 ? 0.39621 0.93370 0.60003 0.06637  -0.06105 -0.04667 100  SER A CB  
2498 C CB  B SER B 101 ? 0.41398 0.95041 0.61720 0.06731  -0.06098 -0.04729 100  SER A CB  
2499 O OG  A SER B 101 ? 0.41001 0.98717 0.61325 0.06469  -0.06145 -0.04194 100  SER A OG  
2500 O OG  B SER B 101 ? 0.41464 0.94078 0.62404 0.05532  -0.06457 -0.04734 100  SER A OG  
2501 N N   . LYS B 102 ? 0.41595 0.90470 0.60194 0.09922  -0.05294 -0.05426 101  LYS A N   
2502 C CA  . LYS B 102 ? 0.43140 0.91619 0.60597 0.11782  -0.04999 -0.05627 101  LYS A CA  
2503 C C   . LYS B 102 ? 0.43253 0.89781 0.61047 0.11385  -0.04726 -0.04959 101  LYS A C   
2504 O O   . LYS B 102 ? 0.41744 0.89768 0.59176 0.12166  -0.04606 -0.04622 101  LYS A O   
2505 C CB  . LYS B 102 ? 0.45589 0.91083 0.61570 0.13339  -0.04931 -0.06583 101  LYS A CB  
2506 C CG  . LYS B 102 ? 0.47920 0.94264 0.63339 0.13631  -0.05202 -0.07411 101  LYS A CG  
2507 C CD  . LYS B 102 ? 0.53038 1.03450 0.67708 0.15165  -0.05189 -0.07745 101  LYS A CD  
2508 C CE  . LYS B 102 ? 0.55049 1.06682 0.69279 0.15094  -0.05444 -0.08478 101  LYS A CE  
2509 N NZ  . LYS B 102 ? 0.58440 1.11418 0.74188 0.12727  -0.05749 -0.07873 101  LYS A NZ  
2510 N N   . VAL B 103 ? 0.43106 0.86625 0.61639 0.10125  -0.04634 -0.04736 102  VAL A N   
2511 C CA  . VAL B 103 ? 0.43925 0.85434 0.62670 0.09766  -0.04290 -0.04150 102  VAL A CA  
2512 C C   . VAL B 103 ? 0.43209 0.87363 0.62603 0.08915  -0.04360 -0.03420 102  VAL A C   
2513 O O   . VAL B 103 ? 0.43638 0.87792 0.62556 0.09398  -0.04162 -0.03059 102  VAL A O   
2514 C CB  . VAL B 103 ? 0.43034 0.81407 0.62634 0.08514  -0.04145 -0.04057 102  VAL A CB  
2515 C CG1 . VAL B 103 ? 0.42641 0.79718 0.62643 0.07926  -0.03751 -0.03368 102  VAL A CG1 
2516 C CG2 . VAL B 103 ? 0.42232 0.77419 0.60890 0.09261  -0.04047 -0.04701 102  VAL A CG2 
2517 N N   . LEU B 104 ? 0.42267 0.88482 0.62601 0.07551  -0.04688 -0.03169 103  LEU A N   
2518 C CA  . LEU B 104 ? 0.42207 0.90577 0.62913 0.06543  -0.04828 -0.02485 103  LEU A CA  
2519 C C   . LEU B 104 ? 0.42772 0.94538 0.62775 0.07491  -0.04935 -0.02460 103  LEU A C   
2520 O O   . LEU B 104 ? 0.46089 0.98845 0.65927 0.07227  -0.04938 -0.01980 103  LEU A O   
2521 C CB  . LEU B 104 ? 0.42672 0.92162 0.64281 0.04875  -0.05208 -0.02170 103  LEU A CB  
2522 C CG  . LEU B 104 ? 0.44544 0.90952 0.67015 0.03972  -0.05111 -0.02057 103  LEU A CG  
2523 C CD1 . LEU B 104 ? 0.44607 0.92020 0.67808 0.02660  -0.05566 -0.01802 103  LEU A CD1 
2524 C CD2 . LEU B 104 ? 0.41882 0.86505 0.64437 0.03556  -0.04792 -0.01583 103  LEU A CD2 
2525 N N   . LEU B 105 ? 0.40386 0.94028 0.59906 0.08686  -0.05020 -0.03006 104  LEU A N   
2526 C CA  . LEU B 105 ? 0.41775 0.99068 0.60735 0.09828  -0.05079 -0.02997 104  LEU A CA  
2527 C C   . LEU B 105 ? 0.42368 0.98144 0.60438 0.11433  -0.04815 -0.03032 104  LEU A C   
2528 O O   . LEU B 105 ? 0.41500 0.99799 0.59367 0.11797  -0.04900 -0.02662 104  LEU A O   
2529 C CB  . LEU B 105 ? 0.38843 0.98513 0.57421 0.10916  -0.05160 -0.03636 104  LEU A CB  
2530 C CG  . LEU B 105 ? 0.41029 1.03201 0.60339 0.09274  -0.05464 -0.03431 104  LEU A CG  
2531 C CD1 . LEU B 105 ? 0.44434 1.08932 0.63195 0.10442  -0.05475 -0.04116 104  LEU A CD1 
2532 C CD2 . LEU B 105 ? 0.43970 1.09598 0.63822 0.07766  -0.05702 -0.02586 104  LEU A CD2 
2533 N N   . SER B 106 ? 0.43248 0.94884 0.60726 0.12272  -0.04535 -0.03408 105  SER A N   
2534 C CA  A SER B 106 ? 0.45631 0.95221 0.62082 0.13659  -0.04281 -0.03320 105  SER A CA  
2535 C CA  B SER B 106 ? 0.45810 0.95415 0.62259 0.13664  -0.04281 -0.03321 105  SER A CA  
2536 C C   . SER B 106 ? 0.45662 0.94557 0.62465 0.12472  -0.04187 -0.02583 105  SER A C   
2537 O O   . SER B 106 ? 0.45682 0.94892 0.61723 0.13410  -0.04136 -0.02305 105  SER A O   
2538 C CB  A SER B 106 ? 0.47874 0.92842 0.63486 0.14483  -0.04010 -0.03815 105  SER A CB  
2539 C CB  B SER B 106 ? 0.47416 0.92438 0.63015 0.14516  -0.04016 -0.03832 105  SER A CB  
2540 O OG  A SER B 106 ? 0.48109 0.93358 0.62950 0.15844  -0.04123 -0.04607 105  SER A OG  
2541 O OG  B SER B 106 ? 0.50237 0.93006 0.64580 0.15906  -0.03779 -0.03684 105  SER A OG  
2542 N N   . ILE B 107 ? 0.44046 0.92016 0.61876 0.10512  -0.04190 -0.02277 106  ILE A N   
2543 C CA  . ILE B 107 ? 0.45633 0.92790 0.63611 0.09424  -0.04086 -0.01670 106  ILE A CA  
2544 C C   . ILE B 107 ? 0.46918 0.97957 0.64918 0.08855  -0.04480 -0.01262 106  ILE A C   
2545 O O   . ILE B 107 ? 0.45801 0.96939 0.63239 0.08886  -0.04471 -0.00894 106  ILE A O   
2546 C CB  . ILE B 107 ? 0.42342 0.87252 0.61304 0.07735  -0.03960 -0.01507 106  ILE A CB  
2547 C CG1 . ILE B 107 ? 0.39234 0.80267 0.58151 0.08145  -0.03510 -0.01763 106  ILE A CG1 
2548 C CG2 . ILE B 107 ? 0.40434 0.85085 0.59412 0.06604  -0.03927 -0.00958 106  ILE A CG2 
2549 C CD1 . ILE B 107 ? 0.35947 0.75218 0.56020 0.06686  -0.03379 -0.01628 106  ILE A CD1 
2550 N N   . CYS B 108 ? 0.44376 0.98723 0.62949 0.08198  -0.04853 -0.01292 107  CYS A N   
2551 C CA  . CYS B 108 ? 0.45066 1.03582 0.63626 0.07606  -0.05256 -0.00894 107  CYS A CA  
2552 C C   . CYS B 108 ? 0.48293 1.09030 0.66102 0.09543  -0.05268 -0.00992 107  CYS A C   
2553 O O   . CYS B 108 ? 0.51735 1.14694 0.69275 0.09283  -0.05519 -0.00581 107  CYS A O   
2554 C CB  . CYS B 108 ? 0.45992 1.07712 0.65216 0.06602  -0.05585 -0.00878 107  CYS A CB  
2555 S SG  . CYS B 108 ? 0.48657 1.08115 0.68637 0.04399  -0.05714 -0.00637 107  CYS A SG  
2556 N N   . SER B 109 ? 0.47578 1.07699 0.64932 0.11544  -0.05050 -0.01551 108  SER A N   
2557 C CA  . SER B 109 ? 0.48281 1.10014 0.64751 0.13772  -0.05052 -0.01671 108  SER A CA  
2558 C C   . SER B 109 ? 0.51945 1.10894 0.67550 0.14286  -0.04898 -0.01339 108  SER A C   
2559 O O   . SER B 109 ? 0.53393 1.14675 0.68509 0.15087  -0.05116 -0.01033 108  SER A O   
2560 C CB  . SER B 109 ? 0.48403 1.09098 0.64267 0.15813  -0.04847 -0.02419 108  SER A CB  
2561 O OG  . SER B 109 ? 0.57663 1.21197 0.72797 0.18091  -0.04933 -0.02590 108  SER A OG  
2562 N N   . LEU B 110 ? 0.51026 1.05226 0.66444 0.13762  -0.04531 -0.01352 109  LEU A N   
2563 C CA  . LEU B 110 ? 0.53222 1.04738 0.67780 0.13976  -0.04314 -0.00968 109  LEU A CA  
2564 C C   . LEU B 110 ? 0.53905 1.07472 0.68672 0.12470  -0.04607 -0.00420 109  LEU A C   
2565 O O   . LEU B 110 ? 0.56218 1.10210 0.70099 0.13136  -0.04704 -0.00096 109  LEU A O   
2566 C CB  . LEU B 110 ? 0.51683 0.98267 0.66244 0.13337  -0.03814 -0.01038 109  LEU A CB  
2567 C CG  . LEU B 110 ? 0.55275 0.98909 0.68876 0.13466  -0.03467 -0.00613 109  LEU A CG  
2568 C CD1 . LEU B 110 ? 0.61042 1.03716 0.73068 0.15735  -0.03412 -0.00586 109  LEU A CD1 
2569 C CD2 . LEU B 110 ? 0.54380 0.94052 0.68407 0.12374  -0.02948 -0.00625 109  LEU A CD2 
2570 N N   . LEU B 111 ? 0.51867 1.06604 0.67621 0.10422  -0.04810 -0.00308 110  LEU A N   
2571 C CA  . LEU B 111 ? 0.51186 1.07804 0.66901 0.08852  -0.05190 0.00156  110  LEU A CA  
2572 C C   . LEU B 111 ? 0.54608 1.16069 0.70114 0.09504  -0.05692 0.00333  110  LEU A C   
2573 O O   . LEU B 111 ? 0.57300 1.20019 0.72279 0.08862  -0.06015 0.00707  110  LEU A O   
2574 C CB  . LEU B 111 ? 0.47222 1.04175 0.63823 0.06621  -0.05397 0.00260  110  LEU A CB  
2575 C CG  . LEU B 111 ? 0.47143 0.99934 0.64136 0.05686  -0.05010 0.00183  110  LEU A CG  
2576 C CD1 . LEU B 111 ? 0.45730 0.98819 0.63016 0.03503  -0.05357 0.00483  110  LEU A CD1 
2577 C CD2 . LEU B 111 ? 0.46754 0.95851 0.63017 0.06311  -0.04498 0.00221  110  LEU A CD2 
2578 N N   . CYS B 112 ? 0.54073 1.18407 0.69933 0.10842  -0.05766 0.00045  111  CYS A N   
2579 C CA  . CYS B 112 ? 0.55498 1.24989 0.71327 0.11678  -0.06200 0.00217  111  CYS A CA  
2580 C C   . CYS B 112 ? 0.57421 1.26411 0.72151 0.14058  -0.06145 0.00238  111  CYS A C   
2581 O O   . CYS B 112 ? 0.58725 1.31012 0.73180 0.14342  -0.06572 0.00593  111  CYS A O   
2582 C CB  . CYS B 112 ? 0.57777 1.30782 0.74342 0.12385  -0.06231 -0.00124 111  CYS A CB  
2583 S SG  . CYS B 112 ? 0.68261 1.42008 0.85494 0.09449  -0.06285 0.00035  111  CYS A SG  
2584 N N   . ASP B 113 ? 0.90685 1.00819 0.66490 0.42461  -0.02173 -0.07847 112  ASP A N   
2585 C CA  . ASP B 113 ? 0.94428 1.01184 0.68282 0.44676  -0.01942 -0.06120 112  ASP A CA  
2586 C C   . ASP B 113 ? 0.97798 0.99864 0.72320 0.42250  -0.01887 -0.05085 112  ASP A C   
2587 O O   . ASP B 113 ? 1.01622 0.96976 0.75249 0.42043  -0.02411 -0.05567 112  ASP A O   
2588 C CB  . ASP B 113 ? 0.97361 0.99480 0.68580 0.47870  -0.02465 -0.06865 112  ASP A CB  
2589 C CG  . ASP B 113 ? 1.01058 1.07744 0.71158 0.50660  -0.02288 -0.07030 112  ASP A CG  
2590 O OD1 . ASP B 113 ? 1.04582 1.15240 0.74556 0.51341  -0.01729 -0.05432 112  ASP A OD1 
2591 O OD2 . ASP B 113 ? 1.01283 1.07464 0.70656 0.50486  -0.02834 -0.08460 112  ASP A OD2 
2592 N N   . PRO B 114 ? 0.92389 0.97825 0.68528 0.40288  -0.01245 -0.03710 113  PRO A N   
2593 C CA  . PRO B 114 ? 0.94342 0.95460 0.71096 0.37966  -0.01082 -0.02638 113  PRO A CA  
2594 C C   . PRO B 114 ? 1.04084 0.99674 0.78310 0.40235  -0.01096 -0.01246 113  PRO A C   
2595 O O   . PRO B 114 ? 1.05687 1.02267 0.77988 0.43486  -0.01021 -0.00562 113  PRO A O   
2596 C CB  . PRO B 114 ? 0.93415 1.00446 0.72148 0.36003  -0.00286 -0.01370 113  PRO A CB  
2597 C CG  . PRO B 114 ? 0.87606 1.01607 0.67599 0.36083  -0.00270 -0.02553 113  PRO A CG  
2598 C CD  . PRO B 114 ? 0.89104 1.02557 0.66837 0.39722  -0.00657 -0.03299 113  PRO A CD  
2599 N N   . ASN B 115 ? 1.10359 0.99945 0.84631 0.38480  -0.01226 -0.00889 114  ASN A N   
2600 C CA  . ASN B 115 ? 1.27191 1.10918 0.99216 0.40109  -0.01252 0.00475  114  ASN A CA  
2601 C C   . ASN B 115 ? 1.34019 1.17628 1.06591 0.38371  -0.00541 0.02507  114  ASN A C   
2602 O O   . ASN B 115 ? 1.37578 1.17823 1.11368 0.35484  -0.00475 0.02533  114  ASN A O   
2603 C CB  . ASN B 115 ? 1.31624 1.07778 1.02866 0.39790  -0.01994 -0.00691 114  ASN A CB  
2604 C CG  . ASN B 115 ? 1.27923 1.03372 0.98095 0.41903  -0.02711 -0.02571 114  ASN A CG  
2605 O OD1 . ASN B 115 ? 1.30826 1.09417 0.99708 0.44819  -0.02673 -0.02570 114  ASN A OD1 
2606 N ND2 . ASN B 115 ? 1.23520 0.94622 0.94169 0.40463  -0.03372 -0.04191 114  ASN A ND2 
2607 N N   . PRO B 116 ? 1.36969 1.24153 1.08685 0.39990  0.00013  0.04235  115  PRO A N   
2608 C CA  . PRO B 116 ? 1.42416 1.28878 1.14197 0.38608  0.00672  0.06285  115  PRO A CA  
2609 C C   . PRO B 116 ? 1.60113 1.39074 1.29629 0.39679  0.00462  0.07299  115  PRO A C   
2610 O O   . PRO B 116 ? 1.62101 1.40339 1.30629 0.39930  0.00930  0.09243  115  PRO A O   
2611 C CB  . PRO B 116 ? 1.32218 1.24956 1.03551 0.40462  0.01185  0.07632  115  PRO A CB  
2612 C CG  . PRO B 116 ? 1.27865 1.25759 0.99874 0.41690  0.00935  0.06094  115  PRO A CG  
2613 C CD  . PRO B 116 ? 1.27889 1.21028 0.99043 0.42642  0.00128  0.04276  115  PRO A CD  
2614 N N   . ASP B 117 ? 1.71802 1.45118 1.40397 0.40352  -0.00259 0.06013  116  ASP A N   
2615 C CA  . ASP B 117 ? 1.93342 1.59341 1.59672 0.41580  -0.00536 0.06861  116  ASP A CA  
2616 C C   . ASP B 117 ? 2.02953 1.65019 1.70216 0.38359  -0.00169 0.07667  116  ASP A C   
2617 O O   . ASP B 117 ? 2.16007 1.76162 1.82091 0.38510  0.00255  0.09553  116  ASP A O   
2618 C CB  . ASP B 117 ? 2.11477 1.72758 1.76652 0.43167  -0.01423 0.05135  116  ASP A CB  
2619 C CG  . ASP B 117 ? 2.11614 1.72590 1.78981 0.40501  -0.01786 0.03053  116  ASP A CG  
2620 O OD1 . ASP B 117 ? 2.09530 1.70062 1.78930 0.37068  -0.01489 0.03083  116  ASP A OD1 
2621 O OD2 . ASP B 117 ? 2.14268 1.75275 1.81284 0.41859  -0.02393 0.01355  116  ASP A OD2 
2622 N N   . ASP B 118 ? 1.94647 1.55460 1.64036 0.35390  -0.00330 0.06238  117  ASP A N   
2623 C CA  . ASP B 118 ? 1.95887 1.53645 1.66695 0.31941  0.00073  0.06749  117  ASP A CA  
2624 C C   . ASP B 118 ? 1.74735 1.37070 1.48790 0.28848  0.00220  0.05410  117  ASP A C   
2625 O O   . ASP B 118 ? 1.69006 1.28813 1.44444 0.27067  -0.00277 0.03744  117  ASP A O   
2626 C CB  . ASP B 118 ? 2.09976 1.59385 1.79718 0.31731  -0.00473 0.06281  117  ASP A CB  
2627 C CG  . ASP B 118 ? 2.12046 1.57802 1.82607 0.28742  0.00082  0.07344  117  ASP A CG  
2628 O OD1 . ASP B 118 ? 2.09882 1.59563 1.81773 0.26862  0.00903  0.08447  117  ASP A OD1 
2629 O OD2 . ASP B 118 ? 2.19178 1.58120 1.89014 0.28286  -0.00276 0.07096  117  ASP A OD2 
2630 N N   . PRO B 119 ? 1.57714 1.26949 1.33051 0.28209  0.00854  0.06075  118  PRO A N   
2631 C CA  . PRO B 119 ? 1.32619 1.07201 1.10872 0.25868  0.00909  0.04710  118  PRO A CA  
2632 C C   . PRO B 119 ? 1.19189 0.92055 0.99987 0.21780  0.01170  0.04338  118  PRO A C   
2633 O O   . PRO B 119 ? 1.27584 0.95264 1.07918 0.20663  0.01400  0.05213  118  PRO A O   
2634 C CB  . PRO B 119 ? 1.24386 1.06330 1.02938 0.26558  0.01597  0.05931  118  PRO A CB  
2635 C CG  . PRO B 119 ? 1.42364 1.22658 1.17900 0.29822  0.01719  0.07675  118  PRO A CG  
2636 C CD  . PRO B 119 ? 1.57271 1.29676 1.31413 0.29581  0.01533  0.08172  118  PRO A CD  
2637 N N   . LEU B 120 ? 1.05734 0.82869 0.89265 0.19521  0.01115  0.02980  119  LEU A N   
2638 C CA  . LEU B 120 ? 0.96896 0.73675 0.83230 0.15513  0.01459  0.02678  119  LEU A CA  
2639 C C   . LEU B 120 ? 0.91534 0.74267 0.79485 0.13783  0.02436  0.03929  119  LEU A C   
2640 O O   . LEU B 120 ? 0.89843 0.71754 0.79668 0.10658  0.02962  0.04270  119  LEU A O   
2641 C CB  . LEU B 120 ? 0.87984 0.65380 0.76543 0.13764  0.00726  0.00331  119  LEU A CB  
2642 C CG  . LEU B 120 ? 0.89080 0.59263 0.77541 0.13020  -0.00053 -0.00964 119  LEU A CG  
2643 C CD1 . LEU B 120 ? 0.80511 0.52195 0.71821 0.10417  -0.00607 -0.03031 119  LEU A CD1 
2644 C CD2 . LEU B 120 ? 0.92520 0.57454 0.80958 0.11312  0.00448  0.00234  119  LEU A CD2 
2645 N N   . VAL B 121 ? 0.89604 0.78204 0.76871 0.15740  0.02709  0.04629  120  VAL A N   
2646 C CA  . VAL B 121 ? 0.84858 0.79098 0.73422 0.14326  0.03642  0.05953  120  VAL A CA  
2647 C C   . VAL B 121 ? 0.85960 0.81409 0.71839 0.17363  0.04031  0.07909  120  VAL A C   
2648 O O   . VAL B 121 ? 0.82495 0.82294 0.67511 0.19875  0.03860  0.07845  120  VAL A O   
2649 C CB  . VAL B 121 ? 0.80079 0.81489 0.71137 0.13119  0.03616  0.04768  120  VAL A CB  
2650 C CG1 . VAL B 121 ? 0.75647 0.82278 0.68438 0.10984  0.04617  0.06068  120  VAL A CG1 
2651 C CG2 . VAL B 121 ? 0.73657 0.73400 0.66935 0.10831  0.02920  0.02531  120  VAL A CG2 
2652 N N   . PRO B 122 ? 0.66456 1.09969 0.60788 0.18629  -0.07866 0.03583  121  PRO A N   
2653 C CA  . PRO B 122 ? 0.65327 1.14202 0.60222 0.19652  -0.08032 0.03599  121  PRO A CA  
2654 C C   . PRO B 122 ? 0.63088 1.16357 0.59863 0.18143  -0.09968 0.03346  121  PRO A C   
2655 O O   . PRO B 122 ? 0.61740 1.20117 0.59639 0.18475  -0.10151 0.03561  121  PRO A O   
2656 C CB  . PRO B 122 ? 0.62394 1.09812 0.55719 0.21168  -0.07431 0.02909  121  PRO A CB  
2657 C CG  . PRO B 122 ? 0.65025 1.06731 0.56860 0.21444  -0.06201 0.02676  121  PRO A CG  
2658 C CD  . PRO B 122 ? 0.66879 1.06020 0.59475 0.19518  -0.06999 0.02895  121  PRO A CD  
2659 N N   . GLU B 123 ? 0.64710 1.16260 0.61810 0.16454  -0.11413 0.02767  122  GLU A N   
2660 C CA  . GLU B 123 ? 0.63336 1.19141 0.62162 0.14861  -0.13252 0.02197  122  GLU A CA  
2661 C C   . GLU B 123 ? 0.64849 1.23514 0.65547 0.13387  -0.13761 0.02576  122  GLU A C   
2662 O O   . GLU B 123 ? 0.65843 1.30157 0.68327 0.12911  -0.14503 0.02249  122  GLU A O   
2663 C CB  . GLU B 123 ? 0.63345 1.16038 0.61716 0.13342  -0.14566 0.01439  122  GLU A CB  
2664 C CG  . GLU B 123 ? 0.66181 1.22746 0.66112 0.11487  -0.16478 0.00515  122  GLU A CG  
2665 C CD  . GLU B 123 ? 0.72736 1.34510 0.73263 0.12622  -0.16753 -0.00059 122  GLU A CD  
2666 O OE1 . GLU B 123 ? 0.77651 1.39252 0.76951 0.14901  -0.15579 0.00206  122  GLU A OE1 
2667 O OE2 . GLU B 123 ? 0.71636 1.37740 0.73842 0.11191  -0.18134 -0.00900 122  GLU A OE2 
2668 N N   . ILE B 124 ? 0.63373 1.18397 0.63746 0.12731  -0.13280 0.03211  123  ILE A N   
2669 C CA  . ILE B 124 ? 0.62844 1.20401 0.64959 0.11448  -0.13583 0.03630  123  ILE A CA  
2670 C C   . ILE B 124 ? 0.65502 1.27239 0.68280 0.13001  -0.12425 0.04318  123  ILE A C   
2671 O O   . ILE B 124 ? 0.66713 1.33456 0.71601 0.12129  -0.12982 0.04273  123  ILE A O   
2672 C CB  . ILE B 124 ? 0.61579 1.13927 0.62840 0.10674  -0.13232 0.04211  123  ILE A CB  
2673 C CG1 . ILE B 124 ? 0.59989 1.08309 0.60365 0.09027  -0.14546 0.03486  123  ILE A CG1 
2674 C CG2 . ILE B 124 ? 0.57967 1.13013 0.61035 0.09531  -0.13350 0.04726  123  ILE A CG2 
2675 C CD1 . ILE B 124 ? 0.61527 1.04521 0.60672 0.08379  -0.14286 0.04003  123  ILE A CD1 
2676 N N   . ALA B 125 ? 0.64396 1.24172 0.65398 0.15228  -0.10749 0.04857  124  ALA A N   
2677 C CA  . ALA B 125 ? 0.67055 1.30604 0.68232 0.16822  -0.09636 0.05476  124  ALA A CA  
2678 C C   . ALA B 125 ? 0.70038 1.39585 0.72342 0.17164  -0.10506 0.04873  124  ALA A C   
2679 O O   . ALA B 125 ? 0.72720 1.47200 0.76399 0.17316  -0.10509 0.05144  124  ALA A O   
2680 C CB  . ALA B 125 ? 0.70433 1.30568 0.69252 0.19021  -0.07702 0.05864  124  ALA A CB  
2681 N N   . ARG B 126 ? 0.66739 1.36065 0.68526 0.17278  -0.11277 0.04000  125  ARG A N   
2682 C CA  . ARG B 126 ? 0.67230 1.42217 0.70033 0.17611  -0.12178 0.03286  125  ARG A CA  
2683 C C   . ARG B 126 ? 0.69239 1.48915 0.74875 0.15357  -0.13688 0.02719  125  ARG A C   
2684 O O   . ARG B 126 ? 0.71954 1.57464 0.79052 0.15654  -0.13933 0.02519  125  ARG A O   
2685 C CB  . ARG B 126 ? 0.67648 1.41080 0.69393 0.17933  -0.12798 0.02423  125  ARG A CB  
2686 C CG  . ARG B 126 ? 0.70303 1.49625 0.73185 0.18096  -0.13905 0.01537  125  ARG A CG  
2687 C CD  . ARG B 126 ? 0.71063 1.48855 0.73079 0.18110  -0.14697 0.00650  125  ARG A CD  
2688 N NE  . ARG B 126 ? 0.76167 1.52085 0.79100 0.15553  -0.16116 -0.00013 125  ARG A NE  
2689 C CZ  . ARG B 126 ? 0.73532 1.53483 0.78519 0.13607  -0.17677 -0.00990 125  ARG A CZ  
2690 N NH1 . ARG B 126 ? 0.74618 1.61043 0.81230 0.13858  -0.18087 -0.01458 125  ARG A NH1 
2691 N NH2 . ARG B 126 ? 0.69956 1.47413 0.75325 0.11331  -0.18830 -0.01634 125  ARG A NH2 
2692 N N   . ILE B 127 ? 0.67373 1.44627 0.73837 0.13024  -0.14695 0.02324  126  ILE A N   
2693 C CA  . ILE B 127 ? 0.68568 1.50033 0.77915 0.10528  -0.16007 0.01571  126  ILE A CA  
2694 C C   . ILE B 127 ? 0.71165 1.55646 0.82065 0.10508  -0.15274 0.02347  126  ILE A C   
2695 O O   . ILE B 127 ? 0.71534 1.62087 0.84933 0.09683  -0.15820 0.01777  126  ILE A O   
2696 C CB  . ILE B 127 ? 0.67665 1.45144 0.77182 0.08060  -0.17038 0.01020  126  ILE A CB  
2697 C CG1 . ILE B 127 ? 0.69118 1.44307 0.77265 0.07994  -0.17890 0.00150  126  ILE A CG1 
2698 C CG2 . ILE B 127 ? 0.70714 1.52361 0.83413 0.05188  -0.18143 0.00078  126  ILE A CG2 
2699 C CD1 . ILE B 127 ? 0.72230 1.53172 0.81852 0.07669  -0.18931 -0.01067 126  ILE A CD1 
2700 N N   . TYR B 128 ? 0.69770 1.50152 0.79276 0.11412  -0.13975 0.03595  127  TYR A N   
2701 C CA  . TYR B 128 ? 0.70136 1.52899 0.80841 0.11583  -0.13139 0.04479  127  TYR A CA  
2702 C C   . TYR B 128 ? 0.72313 1.60620 0.83422 0.13308  -0.12675 0.04590  127  TYR A C   
2703 O O   . TYR B 128 ? 0.70893 1.64333 0.84410 0.12575  -0.12878 0.04514  127  TYR A O   
2704 C CB  . TYR B 128 ? 0.71211 1.48215 0.79709 0.12768  -0.11627 0.05776  127  TYR A CB  
2705 C CG  . TYR B 128 ? 0.70905 1.49434 0.80332 0.12945  -0.10670 0.06822  127  TYR A CG  
2706 C CD1 . TYR B 128 ? 0.69313 1.47929 0.80765 0.10845  -0.11149 0.06892  127  TYR A CD1 
2707 C CD2 . TYR B 128 ? 0.73251 1.52950 0.81447 0.15198  -0.09224 0.07716  127  TYR A CD2 
2708 C CE1 . TYR B 128 ? 0.69646 1.50322 0.81967 0.11106  -0.10119 0.07941  127  TYR A CE1 
2709 C CE2 . TYR B 128 ? 0.72386 1.53341 0.81280 0.15395  -0.08334 0.08720  127  TYR A CE2 
2710 C CZ  . TYR B 128 ? 0.71009 1.52151 0.82085 0.13342  -0.08832 0.08835  127  TYR A CZ  
2711 O OH  . TYR B 128 ? 0.69584 1.51998 0.81504 0.13540  -0.07906 0.09857  127  TYR A OH  
2712 N N   . LYS B 129 ? 0.72831 1.60347 0.81701 0.15555  -0.12064 0.04657  128  LYS A N   
2713 C CA  . LYS B 129 ? 0.74239 1.66689 0.83027 0.17448  -0.11602 0.04764  128  LYS A CA  
2714 C C   . LYS B 129 ? 0.76282 1.74867 0.87128 0.16674  -0.13077 0.03445  128  LYS A C   
2715 O O   . LYS B 129 ? 0.79583 1.83551 0.91211 0.17713  -0.12986 0.03388  128  LYS A O   
2716 C CB  . LYS B 129 ? 0.73737 1.63044 0.79350 0.20137  -0.10276 0.05231  128  LYS A CB  
2717 C CG  . LYS B 129 ? 0.76699 1.61032 0.80348 0.21175  -0.08527 0.06412  128  LYS A CG  
2718 C CD  . LYS B 129 ? 0.82412 1.64016 0.83188 0.23611  -0.07148 0.06584  128  LYS A CD  
2719 C CE  . LYS B 129 ? 0.86547 1.69123 0.86071 0.25493  -0.05558 0.07544  128  LYS A CE  
2720 N NZ  . LYS B 129 ? 0.87325 1.76703 0.88116 0.26127  -0.06092 0.07521  128  LYS A NZ  
2721 N N   . THR B 130 ? 0.75556 1.73501 0.87236 0.14881  -0.14415 0.02331  129  THR A N   
2722 C CA  . THR B 130 ? 0.76548 1.79667 0.89774 0.14239  -0.15767 0.00910  129  THR A CA  
2723 C C   . THR B 130 ? 0.77542 1.84611 0.94294 0.11134  -0.17071 -0.00250 129  THR A C   
2724 O O   . THR B 130 ? 0.83672 1.97208 1.02554 0.10760  -0.17713 -0.01185 129  THR A O   
2725 C CB  . THR B 130 ? 0.76692 1.76322 0.88078 0.14605  -0.16269 0.00320  129  THR A CB  
2726 O OG1 . THR B 130 ? 0.76761 1.75076 0.85515 0.17570  -0.15145 0.00929  129  THR A OG1 
2727 C CG2 . THR B 130 ? 0.83490 1.87486 0.96712 0.13101  -0.17917 -0.01324 129  THR A CG2 
2728 N N   . ASP B 131 ? 0.75920 1.79353 0.93409 0.08823  -0.17423 -0.00333 130  ASP A N   
2729 C CA  . ASP B 131 ? 0.74568 1.81147 0.95430 0.05523  -0.18523 -0.01633 130  ASP A CA  
2730 C C   . ASP B 131 ? 0.73448 1.78208 0.94905 0.04096  -0.17756 -0.00898 130  ASP A C   
2731 O O   . ASP B 131 ? 0.72708 1.74375 0.93745 0.02297  -0.18039 -0.01219 130  ASP A O   
2732 C CB  . ASP B 131 ? 0.75662 1.80927 0.96445 0.03845  -0.19865 -0.03047 130  ASP A CB  
2733 C CG  . ASP B 131 ? 0.75980 1.87120 1.00175 0.00453  -0.20709 -0.04856 130  ASP A CG  
2734 O OD1 . ASP B 131 ? 0.75528 1.92054 1.02217 -0.00787 -0.20092 -0.05009 130  ASP A OD1 
2735 O OD2 . ASP B 131 ? 0.72609 1.83406 0.96942 -0.01096 -0.21819 -0.06220 130  ASP A OD2 
2736 N N   . ARG B 132 ? 0.73013 1.80362 0.95219 0.05018  -0.16664 0.00113  131  ARG A N   
2737 C CA  . ARG B 132 ? 0.69116 1.75824 0.91782 0.03980  -0.15676 0.01014  131  ARG A CA  
2738 C C   . ARG B 132 ? 0.67193 1.77479 0.92488 0.00083  -0.16116 -0.00316 131  ARG A C   
2739 O O   . ARG B 132 ? 0.64558 1.72166 0.89478 -0.01267 -0.15613 0.00202  131  ARG A O   
2740 C CB  . ARG B 132 ? 0.65681 1.76267 0.89430 0.05179  -0.14574 0.02017  131  ARG A CB  
2741 C CG  . ARG B 132 ? 0.63067 1.72084 0.86808 0.04664  -0.13373 0.03324  131  ARG A CG  
2742 C CD  . ARG B 132 ? 0.66032 1.66311 0.86034 0.06807  -0.12691 0.04763  131  ARG A CD  
2743 N NE  . ARG B 132 ? 0.70927 1.68047 0.88659 0.09802  -0.12301 0.05357  131  ARG A NE  
2744 C CZ  . ARG B 132 ? 0.72000 1.70390 0.89473 0.11539  -0.11297 0.06322  131  ARG A CZ  
2745 N NH1 . ARG B 132 ? 0.69633 1.72187 0.88922 0.10872  -0.10578 0.06959  131  ARG A NH1 
2746 N NH2 . ARG B 132 ? 0.72560 1.70602 0.87454 0.14171  -0.10613 0.06761  131  ARG A NH2 
2747 N N   . GLU B 133 ? 0.67055 1.83616 0.95156 -0.01974 -0.16888 -0.02091 132  GLU A N   
2748 C CA  . GLU B 133 ? 0.64984 1.84404 0.95599 -0.06209 -0.17100 -0.03670 132  GLU A CA  
2749 C C   . GLU B 133 ? 0.65266 1.78659 0.93734 -0.07324 -0.17865 -0.04176 132  GLU A C   
2750 O O   . GLU B 133 ? 0.64057 1.76054 0.92908 -0.10155 -0.17503 -0.04503 132  GLU A O   
2751 C CB  . GLU B 133 ? 0.65946 1.92761 0.99833 -0.08115 -0.17710 -0.05642 132  GLU A CB  
2752 C CG  . GLU B 133 ? 0.71816 2.00906 1.08174 -0.12798 -0.17812 -0.07613 132  GLU A CG  
2753 C CD  . GLU B 133 ? 0.82030 2.18302 1.21587 -0.14524 -0.18345 -0.09628 132  GLU A CD  
2754 O OE1 . GLU B 133 ? 0.78011 2.18790 1.18574 -0.12439 -0.18258 -0.09249 132  GLU A OE1 
2755 O OE2 . GLU B 133 ? 0.79532 2.16806 1.20483 -0.17949 -0.18804 -0.11614 132  GLU A OE2 
2756 N N   . LYS B 134 ? 0.67333 1.76775 0.93401 -0.05190 -0.18827 -0.04209 133  LYS A N   
2757 C CA  . LYS B 134 ? 0.67475 1.70673 0.91244 -0.05906 -0.19567 -0.04587 133  LYS A CA  
2758 C C   . LYS B 134 ? 0.65996 1.62419 0.86989 -0.04518 -0.18803 -0.02857 133  LYS A C   
2759 O O   . LYS B 134 ? 0.64777 1.57468 0.84684 -0.06354 -0.19000 -0.03170 133  LYS A O   
2760 C CB  . LYS B 134 ? 0.70296 1.71111 0.92412 -0.03961 -0.20650 -0.04966 133  LYS A CB  
2761 C CG  . LYS B 134 ? 0.68936 1.63286 0.88676 -0.04518 -0.21478 -0.05378 133  LYS A CG  
2762 C CD  . LYS B 134 ? 0.74109 1.67365 0.92843 -0.02999 -0.22503 -0.05862 133  LYS A CD  
2763 C CE  . LYS B 134 ? 0.74202 1.59622 0.89951 -0.02618 -0.23089 -0.05685 133  LYS A CE  
2764 N NZ  . LYS B 134 ? 0.76619 1.61311 0.90351 0.00121  -0.23048 -0.05296 133  LYS A NZ  
2765 N N   . TYR B 135 ? 0.67813 1.62304 0.87465 -0.01342 -0.17886 -0.01111 134  TYR A N   
2766 C CA  . TYR B 135 ? 0.66075 1.54586 0.83357 -0.00028 -0.16960 0.00516  134  TYR A CA  
2767 C C   . TYR B 135 ? 0.62564 1.53449 0.81374 -0.02765 -0.16362 0.00633  134  TYR A C   
2768 O O   . TYR B 135 ? 0.61048 1.47126 0.78032 -0.03436 -0.16292 0.01070  134  TYR A O   
2769 C CB  . TYR B 135 ? 0.66345 1.53283 0.82445 0.03305  -0.15818 0.02111  134  TYR A CB  
2770 C CG  . TYR B 135 ? 0.66293 1.48318 0.80564 0.04415  -0.14590 0.03731  134  TYR A CG  
2771 C CD1 . TYR B 135 ? 0.64893 1.50789 0.80819 0.03543  -0.13654 0.04553  134  TYR A CD1 
2772 C CD2 . TYR B 135 ? 0.65151 1.38673 0.76206 0.06199  -0.14272 0.04388  134  TYR A CD2 
2773 C CE1 . TYR B 135 ? 0.63040 1.44576 0.77255 0.04662  -0.12521 0.06103  134  TYR A CE1 
2774 C CE2 . TYR B 135 ? 0.63175 1.32084 0.72598 0.07167  -0.13093 0.05687  134  TYR A CE2 
2775 C CZ  . TYR B 135 ? 0.63259 1.36255 0.74153 0.06536  -0.12252 0.06605  134  TYR A CZ  
2776 O OH  . TYR B 135 ? 0.62743 1.31294 0.71994 0.07593  -0.11047 0.07959  134  TYR A OH  
2777 N N   . ASN B 136 ? 0.61995 1.60148 0.84142 -0.04433 -0.15813 0.00293  135  ASN A N   
2778 C CA  . ASN B 136 ? 0.60321 1.61080 0.84457 -0.07586 -0.14934 0.00366  135  ASN A CA  
2779 C C   . ASN B 136 ? 0.59158 1.58973 0.83676 -0.11705 -0.15564 -0.01380 135  ASN A C   
2780 O O   . ASN B 136 ? 0.55869 1.53089 0.79743 -0.13793 -0.14992 -0.00983 135  ASN A O   
2781 C CB  . ASN B 136 ? 0.58284 1.66901 0.86288 -0.08871 -0.14082 0.00050  135  ASN A CB  
2782 C CG  . ASN B 136 ? 0.60930 1.69999 0.88366 -0.05306 -0.13109 0.01992  135  ASN A CG  
2783 O OD1 . ASN B 136 ? 0.62533 1.66073 0.87078 -0.02662 -0.12585 0.03749  135  ASN A OD1 
2784 N ND2 . ASN B 136 ? 0.61989 1.77386 0.92080 -0.05328 -0.12797 0.01578  135  ASN A ND2 
2785 N N   . ARG B 137 ? 0.60736 1.62395 0.86166 -0.13081 -0.16653 -0.03347 136  ARG A N   
2786 C CA  . ARG B 137 ? 0.60409 1.60405 0.85876 -0.17086 -0.17146 -0.05202 136  ARG A CA  
2787 C C   . ARG B 137 ? 0.59191 1.51040 0.80602 -0.16177 -0.17714 -0.04572 136  ARG A C   
2788 O O   . ARG B 137 ? 0.59937 1.48886 0.80542 -0.19356 -0.17359 -0.05054 136  ARG A O   
2789 C CB  . ARG B 137 ? 0.62018 1.65057 0.88895 -0.18094 -0.18277 -0.07282 136  ARG A CB  
2790 C CG  . ARG B 137 ? 0.63852 1.64316 0.90389 -0.22058 -0.18753 -0.09311 136  ARG A CG  
2791 C CD  . ARG B 137 ? 0.69682 1.73080 0.97521 -0.22742 -0.19948 -0.11279 136  ARG A CD  
2792 N NE  . ARG B 137 ? 0.68826 1.71738 0.95252 -0.18427 -0.21051 -0.10469 136  ARG A NE  
2793 C CZ  . ARG B 137 ? 0.73526 1.70704 0.96929 -0.16487 -0.22102 -0.10241 136  ARG A CZ  
2794 N NH1 . ARG B 137 ? 0.78083 1.69277 0.99205 -0.17941 -0.22364 -0.10617 136  ARG A NH1 
2795 N NH2 . ARG B 137 ? 0.71392 1.68390 0.93861 -0.12997 -0.22759 -0.09535 136  ARG A NH2 
2796 N N   . ILE B 138 ? 0.56778 1.44245 0.75434 -0.12037 -0.18426 -0.03553 137  ILE A N   
2797 C CA  . ILE B 138 ? 0.56780 1.36130 0.71571 -0.11027 -0.18930 -0.03075 137  ILE A CA  
2798 C C   . ILE B 138 ? 0.55531 1.31876 0.68735 -0.10550 -0.17941 -0.01318 137  ILE A C   
2799 O O   . ILE B 138 ? 0.53566 1.25006 0.64361 -0.12113 -0.18113 -0.01409 137  ILE A O   
2800 C CB  . ILE B 138 ? 0.56094 1.30865 0.68605 -0.07067 -0.19598 -0.02506 137  ILE A CB  
2801 C CG1 . ILE B 138 ? 0.59455 1.37629 0.73513 -0.07646 -0.20639 -0.04081 137  ILE A CG1 
2802 C CG2 . ILE B 138 ? 0.52319 1.18411 0.61036 -0.06116 -0.20006 -0.02146 137  ILE A CG2 
2803 C CD1 . ILE B 138 ? 0.58191 1.32906 0.70528 -0.04204 -0.21036 -0.03411 137  ILE A CD1 
2804 N N   . ALA B 139 ? 0.55160 1.34079 0.69393 -0.08364 -0.16881 0.00334  138  ALA A N   
2805 C CA  . ALA B 139 ? 0.53809 1.30291 0.66713 -0.07730 -0.15882 0.02207  138  ALA A CA  
2806 C C   . ALA B 139 ? 0.52989 1.32146 0.67529 -0.12700 -0.15423 0.01645  138  ALA A C   
2807 O O   . ALA B 139 ? 0.52921 1.27275 0.64847 -0.13642 -0.15295 0.02462  138  ALA A O   
2808 C CB  . ALA B 139 ? 0.52901 1.32005 0.66934 -0.04708 -0.14662 0.03910  138  ALA A CB  
2809 N N   . ARG B 140 ? 0.50907 1.36644 0.69492 -0.16248 -0.14930 0.00116  139  ARG A N   
2810 C CA  . ARG B 140 ? 0.54067 1.40801 0.74445 -0.21898 -0.13775 -0.00857 139  ARG A CA  
2811 C C   . ARG B 140 ? 0.57010 1.35764 0.73797 -0.24411 -0.14212 -0.02372 139  ARG A C   
2812 O O   . ARG B 140 ? 0.58788 1.28854 0.72577 -0.26089 -0.12210 -0.01962 139  ARG A O   
2813 C CB  . ARG B 140 ? 0.59674 1.53407 0.84693 -0.24900 -0.12760 -0.02455 139  ARG A CB  
2814 C CG  . ARG B 140 ? 0.59963 1.59649 0.87904 -0.22717 -0.11622 -0.01018 139  ARG A CG  
2815 C CD  . ARG B 140 ? 0.69946 1.75621 1.02120 -0.26402 -0.10482 -0.02777 139  ARG A CD  
2816 N NE  . ARG B 140 ? 0.84752 1.93981 1.17816 -0.25154 -0.12056 -0.04360 139  ARG A NE  
2817 C CZ  . ARG B 140 ? 1.00331 2.09787 1.34067 -0.28246 -0.12699 -0.06756 139  ARG A CZ  
2818 N NH1 . ARG B 140 ? 0.99791 2.05603 1.33158 -0.32816 -0.11837 -0.07991 139  ARG A NH1 
2819 N NH2 . ARG B 140 ? 1.06394 2.19146 1.40872 -0.26684 -0.14115 -0.07892 139  ARG A NH2 
2820 N N   . GLU B 141 ? 0.61590 1.40361 0.77685 -0.23782 -0.16096 -0.03946 140  GLU A N   
2821 C CA  . GLU B 141 ? 0.61081 1.33316 0.74091 -0.26257 -0.16777 -0.05531 140  GLU A CA  
2822 C C   . GLU B 141 ? 0.62212 1.25476 0.69910 -0.24024 -0.17011 -0.04029 140  GLU A C   
2823 O O   . GLU B 141 ? 0.63082 1.17673 0.67494 -0.26170 -0.15754 -0.04425 140  GLU A O   
2824 C CB  . GLU B 141 ? 0.59997 1.32749 0.73201 -0.24796 -0.18221 -0.07052 140  GLU A CB  
2825 C CG  . GLU B 141 ? 0.62002 1.41796 0.79547 -0.27270 -0.17901 -0.08771 140  GLU A CG  
2826 C CD  . GLU B 141 ? 0.72455 1.53589 0.90319 -0.25229 -0.19429 -0.09809 140  GLU A CD  
2827 O OE1 . GLU B 141 ? 0.71944 1.48423 0.86892 -0.21768 -0.20521 -0.09050 140  GLU A OE1 
2828 O OE2 . GLU B 141 ? 0.75620 1.62224 0.96651 -0.27169 -0.19428 -0.11359 140  GLU A OE2 
2829 N N   . TRP B 142 ? 0.58370 1.21281 0.64637 -0.18904 -0.17844 -0.02125 141  TRP A N   
2830 C CA  . TRP B 142 ? 0.59818 1.13731 0.61005 -0.16210 -0.17708 -0.00549 141  TRP A CA  
2831 C C   . TRP B 142 ? 0.62393 1.10290 0.62146 -0.16746 -0.14764 0.00982  141  TRP A C   
2832 O O   . TRP B 142 ? 0.62810 1.01181 0.58179 -0.16642 -0.13864 0.01406  141  TRP A O   
2833 C CB  . TRP B 142 ? 0.55951 1.08720 0.56345 -0.10328 -0.18089 0.01041  141  TRP A CB  
2834 C CG  . TRP B 142 ? 0.57126 1.06421 0.56731 -0.08198 -0.19026 -0.00077 141  TRP A CG  
2835 C CD1 . TRP B 142 ? 0.53965 1.06358 0.55521 -0.09925 -0.19892 -0.01948 141  TRP A CD1 
2836 C CD2 . TRP B 142 ? 0.59766 1.01496 0.56606 -0.04226 -0.19067 0.00649  141  TRP A CD2 
2837 N NE1 . TRP B 142 ? 0.55440 1.03076 0.55430 -0.07209 -0.20630 -0.02139 141  TRP A NE1 
2838 C CE2 . TRP B 142 ? 0.56105 0.97089 0.53353 -0.03991 -0.20090 -0.00632 141  TRP A CE2 
2839 C CE3 . TRP B 142 ? 0.60349 0.95437 0.54611 -0.01222 -0.18186 0.02153  141  TRP A CE3 
2840 C CZ2 . TRP B 142 ? 0.59219 0.93370 0.54460 -0.01368 -0.20296 -0.00253 141  TRP A CZ2 
2841 C CZ3 . TRP B 142 ? 0.63706 0.91754 0.56304 0.01043  -0.18293 0.02160  141  TRP A CZ3 
2842 C CH2 . TRP B 142 ? 0.59943 0.87747 0.53036 0.00732  -0.19349 0.01116  141  TRP A CH2 
2843 N N   . THR B 143 ? 0.59068 1.12441 0.62376 -0.17237 -0.13221 0.01809  142  THR A N   
2844 C CA  . THR B 143 ? 0.62296 1.10265 0.64404 -0.18139 -0.10271 0.03139  142  THR A CA  
2845 C C   . THR B 143 ? 0.66914 1.08702 0.67393 -0.22746 -0.08837 0.01621  142  THR A C   
2846 O O   . THR B 143 ? 0.67515 0.99719 0.63632 -0.22548 -0.07488 0.02368  142  THR A O   
2847 C CB  . THR B 143 ? 0.57799 1.13552 0.64485 -0.18518 -0.08833 0.03946  142  THR A CB  
2848 O OG1 . THR B 143 ? 0.55561 1.17011 0.63666 -0.14123 -0.10092 0.05393  142  THR A OG1 
2849 C CG2 . THR B 143 ? 0.59717 1.09576 0.64890 -0.19318 -0.05691 0.05415  142  THR A CG2 
2850 N N   . GLN B 144 ? 0.65837 1.12871 0.69518 -0.26771 -0.09344 -0.00672 143  GLN A N   
2851 C CA  . GLN B 144 ? 0.69647 1.11481 0.72179 -0.31553 -0.07956 -0.02353 143  GLN A CA  
2852 C C   . GLN B 144 ? 0.69818 1.02240 0.67049 -0.31068 -0.08856 -0.02877 143  GLN A C   
2853 O O   . GLN B 144 ? 0.75692 1.00293 0.70060 -0.33717 -0.07189 -0.03377 143  GLN A O   
2854 C CB  . GLN B 144 ? 0.75728 1.26049 0.82985 -0.35617 -0.08816 -0.04944 143  GLN A CB  
2855 C CG  . GLN B 144 ? 0.82348 1.42689 0.95349 -0.36892 -0.07813 -0.04893 143  GLN A CG  
2856 C CD  . GLN B 144 ? 0.92239 1.62326 1.10063 -0.40041 -0.09399 -0.07608 143  GLN A CD  
2857 O OE1 . GLN B 144 ? 0.89006 1.58000 1.05862 -0.41705 -0.11063 -0.09623 143  GLN A OE1 
2858 N NE2 . GLN B 144 ? 0.85684 1.65626 1.08709 -0.40594 -0.08996 -0.07679 143  GLN A NE2 
2859 N N   . LYS B 145 ? 0.69162 1.02085 0.64901 -0.27628 -0.11404 -0.02739 144  LYS A N   
2860 C CA  . LYS B 145 ? 0.69920 0.94887 0.60959 -0.27140 -0.12521 -0.03454 144  LYS A CA  
2861 C C   . LYS B 145 ? 0.72333 0.87976 0.58352 -0.23809 -0.11597 -0.01453 144  LYS A C   
2862 O O   . LYS B 145 ? 0.76222 0.83041 0.58088 -0.24838 -0.10918 -0.01891 144  LYS A O   
2863 C CB  . LYS B 145 ? 0.66248 0.96239 0.58033 -0.25276 -0.15697 -0.04456 144  LYS A CB  
2864 C CG  . LYS B 145 ? 0.69267 0.92228 0.56805 -0.25406 -0.16979 -0.05633 144  LYS A CG  
2865 C CD  . LYS B 145 ? 0.68341 0.96482 0.57206 -0.23698 -0.19681 -0.06733 144  LYS A CD  
2866 C CE  . LYS B 145 ? 0.74172 0.95094 0.60069 -0.23377 -0.20033 -0.07980 144  LYS A CE  
2867 N NZ  . LYS B 145 ? 0.80176 1.04830 0.68739 -0.20711 -0.21325 -0.08864 144  LYS A NZ  
2868 N N   . TYR B 146 ? 0.69797 0.87155 0.55998 -0.19754 -0.11592 0.00661  145  TYR A N   
2869 C CA  . TYR B 146 ? 0.73823 0.82895 0.55366 -0.16349 -0.11004 0.02381  145  TYR A CA  
2870 C C   . TYR B 146 ? 0.78186 0.84461 0.59269 -0.15646 -0.08319 0.04330  145  TYR A C   
2871 O O   . TYR B 146 ? 0.80241 0.78390 0.57074 -0.13718 -0.07371 0.05461  145  TYR A O   
2872 C CB  . TYR B 146 ? 0.73029 0.84467 0.54042 -0.11704 -0.13159 0.03332  145  TYR A CB  
2873 C CG  . TYR B 146 ? 0.71483 0.85214 0.52431 -0.11776 -0.15843 0.01643  145  TYR A CG  
2874 C CD1 . TYR B 146 ? 0.76154 0.82541 0.52850 -0.11611 -0.16658 0.00814  145  TYR A CD1 
2875 C CD2 . TYR B 146 ? 0.67603 0.90915 0.52632 -0.11833 -0.17571 0.00886  145  TYR A CD2 
2876 C CE1 . TYR B 146 ? 0.77401 0.85675 0.54390 -0.11315 -0.18705 -0.00736 145  TYR A CE1 
2877 C CE2 . TYR B 146 ? 0.68539 0.92848 0.53881 -0.11189 -0.19356 -0.00679 145  TYR A CE2 
2878 C CZ  . TYR B 146 ? 0.76378 0.92915 0.58233 -0.10556 -0.19480 -0.01524 145  TYR A CZ  
2879 O OH  . TYR B 146 ? 0.79299 0.95782 0.62412 -0.08894 -0.20214 -0.03121 145  TYR A OH  
2880 N N   . ALA B 147 ? 0.74799 0.87667 0.60074 -0.17035 -0.07091 0.04722  146  ALA A N   
2881 C CA  . ALA B 147 ? 0.76865 0.88249 0.62015 -0.15675 -0.04759 0.06781  146  ALA A CA  
2882 C C   . ALA B 147 ? 0.84854 0.93420 0.70283 -0.19773 -0.01946 0.06469  146  ALA A C   
2883 O O   . ALA B 147 ? 0.80816 0.90597 0.67538 -0.19533 0.00110  0.07899  146  ALA A O   
2884 C CB  . ALA B 147 ? 0.70661 0.91357 0.60027 -0.13358 -0.05298 0.07881  146  ALA A CB  
2885 N N   . MET B 148 ? 0.89898 0.94890 0.74206 -0.23612 -0.01763 0.04588  147  MET A N   
2886 C CA  . MET B 148 ? 0.95053 0.96825 0.79368 -0.27848 0.00971  0.04108  147  MET A CA  
2887 C C   . MET B 148 ? 1.08661 0.99348 0.87470 -0.28985 0.01676  0.03528  147  MET A C   
2888 O O   . MET B 148 ? 1.11570 1.00361 0.90134 -0.32891 0.01849  0.01610  147  MET A O   
2889 C CB  . MET B 148 ? 0.90325 1.00520 0.79826 -0.32103 0.00721  0.02124  147  MET A CB  
2890 C CG  . MET B 148 ? 0.83083 1.03408 0.77701 -0.30977 0.00725  0.02993  147  MET A CG  
2891 S SD  . MET B 148 ? 0.98593 1.30252 0.99651 -0.35328 -0.00113 0.00499  147  MET A SD  
2892 C CE  . MET B 148 ? 0.74975 1.17282 0.80894 -0.32359 -0.00235 0.02120  147  MET A CE  
2893 N N   . GLY B 149 ? 1.12078 0.95348 0.86348 -0.25435 0.02118  0.05180  148  GLY A N   
2894 C CA  . GLY B 149 ? 1.21761 0.94336 0.90419 -0.25741 0.02744  0.04853  148  GLY A CA  
2895 C C   . GLY B 149 ? 1.26865 0.92826 0.93213 -0.27625 0.06082  0.05711  148  GLY A C   
2896 O O   . GLY B 149 ? 1.31947 0.97806 0.98344 -0.25759 0.07746  0.07642  148  GLY A O   
2897 N N   . ALA B 176 ? 1.83612 1.38058 1.76818 -0.00865 0.15650  0.04783  945  ALA A N   
2898 C CA  . ALA B 176 ? 1.89274 1.44635 1.81850 -0.01910 0.14200  0.03522  945  ALA A CA  
2899 C C   . ALA B 176 ? 1.96179 1.52861 1.88074 -0.01983 0.14217  0.04673  945  ALA A C   
2900 O O   . ALA B 176 ? 1.96610 1.53198 1.86409 -0.01283 0.15328  0.05102  945  ALA A O   
2901 C CB  . ALA B 176 ? 1.80583 1.36323 1.75985 -0.02819 0.12755  0.03306  945  ALA A CB  
2902 N N   . ASP B 177 ? 1.98519 1.56425 1.92250 -0.02824 0.12987  0.05214  946  ASP A N   
2903 C CA  . ASP B 177 ? 1.97998 1.57229 1.91313 -0.02993 0.12845  0.06315  946  ASP A CA  
2904 C C   . ASP B 177 ? 1.96668 1.56116 1.90815 -0.02073 0.14146  0.08664  946  ASP A C   
2905 O O   . ASP B 177 ? 1.96357 1.56662 1.89516 -0.01941 0.14422  0.09547  946  ASP A O   
2906 C CB  . ASP B 177 ? 1.99087 1.59541 1.94379 -0.04110 0.11214  0.06398  946  ASP A CB  
2907 C CG  . ASP B 177 ? 1.99944 1.60623 1.93579 -0.05067 0.09950  0.04162  946  ASP A CG  
2908 O OD1 . ASP B 177 ? 1.97849 1.57701 1.88887 -0.04868 0.10324  0.02514  946  ASP A OD1 
2909 O OD2 . ASP B 177 ? 2.00642 1.62346 1.95552 -0.06023 0.08588  0.04053  946  ASP A OD2 
2910 N N   . VAL B 178 ? 1.96338 1.55067 1.92336 -0.01462 0.14917  0.09705  947  VAL A N   
2911 C CA  . VAL B 178 ? 1.96393 1.55227 1.92997 -0.00517 0.16281  0.11836  947  VAL A CA  
2912 C C   . VAL B 178 ? 1.95467 1.53732 1.88917 0.00318  0.17594  0.11515  947  VAL A C   
2913 O O   . VAL B 178 ? 1.95316 1.54101 1.88327 0.00898  0.18474  0.12994  947  VAL A O   
2914 C CB  . VAL B 178 ? 1.94616 1.52701 1.93720 -0.00050 0.16847  0.12849  947  VAL A CB  
2915 C CG1 . VAL B 178 ? 1.86177 1.44993 1.88580 -0.00834 0.15605  0.13516  947  VAL A CG1 
2916 C CG2 . VAL B 178 ? 1.90602 1.47158 1.88639 0.00223  0.17214  0.11241  947  VAL A CG2 
2917 N N   . GLN B 179 ? 1.95541 1.52736 1.86778 0.00400  0.17750  0.09590  948  GLN A N   
2918 C CA  . GLN B 179 ? 1.93831 1.50466 1.81844 0.01092  0.18857  0.08994  948  GLN A CA  
2919 C C   . GLN B 179 ? 1.93893 1.50865 1.79251 0.00449  0.18048  0.07150  948  GLN A C   
2920 O O   . GLN B 179 ? 1.91002 1.47507 1.73507 0.00952  0.18870  0.06460  948  GLN A O   
2921 C CB  . GLN B 179 ? 1.88205 1.43270 1.75534 0.01854  0.19928  0.08380  948  GLN A CB  
2922 C CG  . GLN B 179 ? 1.91391 1.46150 1.81415 0.02443  0.20692  0.10212  948  GLN A CG  
2923 C CD  . GLN B 179 ? 1.90691 1.46255 1.81387 0.03060  0.21617  0.12498  948  GLN A CD  
2924 O OE1 . GLN B 179 ? 1.90065 1.45718 1.78572 0.03623  0.22512  0.12762  948  GLN A OE1 
2925 N NE2 . GLN B 179 ? 1.88012 1.44185 1.81797 0.02943  0.21381  0.14160  948  GLN A NE2 
2926 N N   . LYS B 180 ? 1.94153 1.51917 1.80342 -0.00653 0.16465  0.06307  949  LYS A N   
2927 C CA  . LYS B 180 ? 1.90165 1.48455 1.74001 -0.01344 0.15618  0.04722  949  LYS A CA  
2928 C C   . LYS B 180 ? 1.86793 1.46355 1.69975 -0.01396 0.15633  0.05930  949  LYS A C   
2929 O O   . LYS B 180 ? 1.83569 1.43670 1.64694 -0.01926 0.15018  0.04827  949  LYS A O   
2930 C CB  . LYS B 180 ? 1.91444 1.50083 1.76412 -0.02528 0.13903  0.03287  949  LYS A CB  
2931 C CG  . LYS B 180 ? 1.93118 1.52209 1.75595 -0.03303 0.12974  0.01388  949  LYS A CG  
2932 C CD  . LYS B 180 ? 1.95063 1.54546 1.78711 -0.04486 0.11275  -0.00021 949  LYS A CD  
2933 C CE  . LYS B 180 ? 1.95119 1.55209 1.76264 -0.05246 0.10412  -0.01704 949  LYS A CE  
2934 N NZ  . LYS B 180 ? 2.00684 1.61237 1.82874 -0.06432 0.08736  -0.03111 949  LYS A NZ  
2935 N N   . LEU B 181 ? 1.86237 1.46289 1.71112 -0.00854 0.16333  0.08168  950  LEU A N   
2936 C CA  . LEU B 181 ? 1.80068 1.41112 1.63975 -0.00659 0.16680  0.09366  950  LEU A CA  
2937 C C   . LEU B 181 ? 1.75580 1.36105 1.55890 -0.00174 0.17507  0.08332  950  LEU A C   
2938 O O   . LEU B 181 ? 1.75020 1.36358 1.53672 -0.00435 0.17239  0.08250  950  LEU A O   
2939 C CB  . LEU B 181 ? 1.81099 1.42381 1.66951 0.00144  0.17726  0.11817  950  LEU A CB  
2940 C CG  . LEU B 181 ? 1.80556 1.42422 1.70089 -0.00168 0.17151  0.13278  950  LEU A CG  
2941 C CD1 . LEU B 181 ? 1.80401 1.42549 1.71233 0.00711  0.18353  0.15635  950  LEU A CD1 
2942 C CD2 . LEU B 181 ? 1.82872 1.46039 1.73450 -0.01296 0.15544  0.13156  950  LEU A CD2 
2943 N N   . GLN B 182 ? 1.74147 1.33307 1.53207 0.00495  0.18463  0.07470  951  GLN A N   
2944 C CA  . GLN B 182 ? 1.72672 1.31200 1.48310 0.01021  0.19335  0.06440  951  GLN A CA  
2945 C C   . GLN B 182 ? 1.74320 1.33070 1.47776 0.00145  0.18232  0.04284  951  GLN A C   
2946 O O   . GLN B 182 ? 1.73623 1.32741 1.44588 0.00181  0.18415  0.03918  951  GLN A O   
2947 C CB  . GLN B 182 ? 1.67529 1.24515 1.42614 0.01870  0.20506  0.05967  951  GLN A CB  
2948 C CG  . GLN B 182 ? 1.61416 1.18109 1.38195 0.02829  0.21780  0.08023  951  GLN A CG  
2949 C CD  . GLN B 182 ? 1.54955 1.10255 1.30027 0.03837  0.23245  0.07633  951  GLN A CD  
2950 O OE1 . GLN B 182 ? 1.55734 1.10903 1.28491 0.04477  0.24234  0.07795  951  GLN A OE1 
2951 N NE2 . GLN B 182 ? 1.49539 1.03777 1.25705 0.03977  0.23379  0.07092  951  GLN A NE2 
2952 N N   . GLN B 183 ? 1.77519 1.36031 1.51829 -0.00643 0.17093  0.02800  952  GLN A N   
2953 C CA  . GLN B 183 ? 1.73601 1.32437 1.46059 -0.01566 0.15936  0.00758  952  GLN A CA  
2954 C C   . GLN B 183 ? 1.74759 1.35124 1.47211 -0.02258 0.15049  0.01387  952  GLN A C   
2955 O O   . GLN B 183 ? 1.75359 1.36116 1.45380 -0.02683 0.14632  0.00219  952  GLN A O   
2956 C CB  . GLN B 183 ? 1.76439 1.34893 1.50284 -0.02332 0.14789  -0.00728 952  GLN A CB  
2957 C CG  . GLN B 183 ? 1.75767 1.32664 1.48766 -0.01830 0.15452  -0.02052 952  GLN A CG  
2958 C CD  . GLN B 183 ? 1.77947 1.34545 1.51691 -0.02711 0.14168  -0.03937 952  GLN A CD  
2959 O OE1 . GLN B 183 ? 1.79471 1.36996 1.54848 -0.03652 0.12820  -0.04021 952  GLN A OE1 
2960 N NE2 . GLN B 183 ? 1.70555 1.25857 1.43101 -0.02411 0.14575  -0.05469 952  GLN A NE2 
2961 N N   . GLN B 184 ? 1.78142 1.39390 1.53322 -0.02399 0.14731  0.03229  953  GLN A N   
2962 C CA  . GLN B 184 ? 1.78248 1.40937 1.53527 -0.02908 0.14078  0.04158  953  GLN A CA  
2963 C C   . GLN B 184 ? 1.78293 1.41117 1.51446 -0.02121 0.15258  0.05077  953  GLN A C   
2964 O O   . GLN B 184 ? 1.82256 1.45785 1.53429 -0.02515 0.14853  0.04579  953  GLN A O   
2965 C CB  . GLN B 184 ? 1.80604 1.44109 1.59398 -0.03142 0.13585  0.05998  953  GLN A CB  
2966 C CG  . GLN B 184 ? 1.82412 1.46277 1.63171 -0.04219 0.12025  0.05122  953  GLN A CG  
2967 C CD  . GLN B 184 ? 1.83903 1.48416 1.68218 -0.04336 0.11683  0.06988  953  GLN A CD  
2968 O OE1 . GLN B 184 ? 1.82999 1.47513 1.68427 -0.03535 0.12717  0.08877  953  GLN A OE1 
2969 N NE2 . GLN B 184 ? 1.79669 1.44767 1.65781 -0.05344 0.10226  0.06475  953  GLN A NE2 
2970 N N   . LEU B 185 ? 1.71826 1.33983 1.45371 -0.01008 0.16724  0.06427  954  LEU A N   
2971 C CA  . LEU B 185 ? 1.67214 1.29374 1.38740 -0.00161 0.17966  0.07288  954  LEU A CA  
2972 C C   . LEU B 185 ? 1.63008 1.24621 1.30913 -0.00141 0.18174  0.05403  954  LEU A C   
2973 O O   . LEU B 185 ? 1.60009 1.22107 1.25881 0.00027  0.18503  0.05643  954  LEU A O   
2974 C CB  . LEU B 185 ? 1.67609 1.28938 1.40098 0.01031  0.19527  0.08748  954  LEU A CB  
2975 C CG  . LEU B 185 ? 1.66102 1.28016 1.41869 0.01280  0.19724  0.11032  954  LEU A CG  
2976 C CD1 . LEU B 185 ? 1.58379 1.19248 1.34869 0.02409  0.21245  0.12035  954  LEU A CD1 
2977 C CD2 . LEU B 185 ? 1.64338 1.27557 1.40255 0.01250  0.19670  0.12598  954  LEU A CD2 
2978 N N   . GLN B 186 ? 1.62813 1.23451 1.29886 -0.00344 0.17936  0.03495  955  GLN A N   
2979 C CA  . GLN B 186 ? 1.60483 1.20523 1.24167 -0.00329 0.18132  0.01585  955  GLN A CA  
2980 C C   . GLN B 186 ? 1.58459 1.19539 1.20589 -0.01335 0.16903  0.00510  955  GLN A C   
2981 O O   . GLN B 186 ? 1.53137 1.13869 1.12322 -0.01378 0.17018  -0.01035 955  GLN A O   
2982 C CB  . GLN B 186 ? 1.59481 1.18247 1.22896 -0.00334 0.18116  -0.00173 955  GLN A CB  
2983 C CG  . GLN B 186 ? 1.52168 1.09690 1.13092 0.00640  0.19535  -0.00787 955  GLN A CG  
2984 C CD  . GLN B 186 ? 1.59331 1.15612 1.21662 0.01341  0.20375  -0.00528 955  GLN A CD  
2985 O OE1 . GLN B 186 ? 1.64883 1.21323 1.30131 0.01428  0.20346  0.00886  955  GLN A OE1 
2986 N NE2 . GLN B 186 ? 1.56685 1.11719 1.16966 0.01830  0.21115  -0.01903 955  GLN A NE2 
2987 N N   . ASP B 187 ? 1.61221 1.23557 1.25231 -0.02155 0.15731  0.01259  956  ASP A N   
2988 C CA  . ASP B 187 ? 1.55161 1.18609 1.17733 -0.03051 0.14664  0.00578  956  ASP A CA  
2989 C C   . ASP B 187 ? 1.50545 1.14402 1.11072 -0.02491 0.15516  0.01527  956  ASP A C   
2990 O O   . ASP B 187 ? 1.46992 1.11739 1.05999 -0.03128 0.14793  0.01057  956  ASP A O   
2991 C CB  . ASP B 187 ? 1.60131 1.24817 1.25354 -0.04028 0.13243  0.01285  956  ASP A CB  
2992 C CG  . ASP B 187 ? 1.65090 1.30584 1.32423 -0.03632 0.13632  0.03832  956  ASP A CG  
2993 O OD1 . ASP B 187 ? 1.63394 1.28581 1.30176 -0.02617 0.14982  0.05126  956  ASP A OD1 
2994 O OD2 . ASP B 187 ? 1.66540 1.33001 1.36202 -0.04362 0.12547  0.04540  956  ASP A OD2 
2995 N N   . ILE B 188 ? 1.46016 1.09265 1.06586 -0.01325 0.17020  0.02903  957  ILE A N   
2996 C CA  . ILE B 188 ? 1.40986 1.04298 0.99197 -0.00635 0.18046  0.03502  957  ILE A CA  
2997 C C   . ILE B 188 ? 1.36550 0.99330 0.91285 -0.00787 0.18055  0.01388  957  ILE A C   
2998 O O   . ILE B 188 ? 1.29964 0.93111 0.82371 -0.00650 0.18362  0.01403  957  ILE A O   
2999 C CB  . ILE B 188 ? 1.41345 1.03841 1.00143 0.00677  0.19720  0.05014  957  ILE A CB  
3000 C CG1 . ILE B 188 ? 1.37637 1.00244 0.94100 0.01406  0.20783  0.05725  957  ILE A CG1 
3001 C CG2 . ILE B 188 ? 1.40753 1.01753 0.99022 0.01171  0.20408  0.03800  957  ILE A CG2 
3002 C CD1 . ILE B 188 ? 1.33382 0.95013 0.89822 0.02713  0.22501  0.06796  957  ILE A CD1 
3003 N N   . LYS B 189 ? 1.39511 1.01385 0.93831 -0.01035 0.17766  -0.00444 958  LYS A N   
3004 C CA  . LYS B 189 ? 1.35812 0.97245 0.86965 -0.01316 0.17601  -0.02618 958  LYS A CA  
3005 C C   . LYS B 189 ? 1.31551 0.94245 0.81536 -0.02351 0.16361  -0.03226 958  LYS A C   
3006 O O   . LYS B 189 ? 1.28830 0.91601 0.75908 -0.02331 0.16579  -0.04004 958  LYS A O   
3007 C CB  . LYS B 189 ? 1.37502 0.98005 0.88973 -0.01661 0.17133  -0.04476 958  LYS A CB  
3008 C CG  . LYS B 189 ? 1.35213 0.94160 0.86061 -0.00652 0.18456  -0.04858 958  LYS A CG  
3009 C CD  . LYS B 189 ? 1.35629 0.93859 0.88051 -0.01055 0.17817  -0.06105 958  LYS A CD  
3010 C CE  . LYS B 189 ? 1.29295 0.86058 0.79747 -0.00528 0.18596  -0.07747 958  LYS A CE  
3011 N NZ  . LYS B 189 ? 1.19497 0.75569 0.71542 -0.00927 0.17944  -0.08946 958  LYS A NZ  
3012 N N   . GLU B 190 ? 1.33846 0.97571 0.86113 -0.03254 0.15071  -0.02779 959  GLU A N   
3013 C CA  . GLU B 190 ? 1.33869 0.98867 0.85302 -0.04294 0.13820  -0.03233 959  GLU A CA  
3014 C C   . GLU B 190 ? 1.28141 0.93770 0.77906 -0.03898 0.14422  -0.02070 959  GLU A C   
3015 O O   . GLU B 190 ? 1.27304 0.93527 0.74827 -0.04478 0.13853  -0.03006 959  GLU A O   
3016 C CB  . GLU B 190 ? 1.39993 1.06000 0.94554 -0.05136 0.12550  -0.02419 959  GLU A CB  
3017 C CG  . GLU B 190 ? 1.49088 1.14620 1.05279 -0.05707 0.11717  -0.03713 959  GLU A CG  
3018 C CD  . GLU B 190 ? 1.52886 1.19426 1.12182 -0.06516 0.10487  -0.02834 959  GLU A CD  
3019 O OE1 . GLU B 190 ? 1.55941 1.23559 1.16081 -0.06646 0.10270  -0.01245 959  GLU A OE1 
3020 O OE2 . GLU B 190 ? 1.55034 1.21287 1.15944 -0.07011 0.09739  -0.03718 959  GLU A OE2 
3021 N N   . GLN B 191 ? 1.26772 0.92260 0.77512 -0.02903 0.15595  -0.00077 960  GLN A N   
3022 C CA  . GLN B 191 ? 1.22459 0.88562 0.71797 -0.02497 0.16173  0.01134  960  GLN A CA  
3023 C C   . GLN B 191 ? 1.18699 0.83893 0.64884 -0.01655 0.17434  0.00459  960  GLN A C   
3024 O O   . GLN B 191 ? 1.18559 0.84279 0.62867 -0.01537 0.17677  0.00865  960  GLN A O   
3025 C CB  . GLN B 191 ? 1.22611 0.89101 0.74463 -0.01838 0.16824  0.03655  960  GLN A CB  
3026 C CG  . GLN B 191 ? 1.28186 0.95376 0.83439 -0.02484 0.15797  0.04479  960  GLN A CG  
3027 C CD  . GLN B 191 ? 1.31877 0.99396 0.89548 -0.01778 0.16528  0.06939  960  GLN A CD  
3028 O OE1 . GLN B 191 ? 1.32510 0.99444 0.92368 -0.01309 0.17018  0.07651  960  GLN A OE1 
3029 N NE2 . GLN B 191 ? 1.32080 1.00543 0.89381 -0.01697 0.16612  0.08264  960  GLN A NE2 
3030 N N   . THR B 192 ? 1.18752 0.82598 0.64324 -0.01059 0.18246  -0.00521 961  THR A N   
3031 C CA  . THR B 192 ? 1.16499 0.79414 0.59227 -0.00158 0.19561  -0.01013 961  THR A CA  
3032 C C   . THR B 192 ? 1.15998 0.78150 0.56140 -0.00490 0.19330  -0.03513 961  THR A C   
3033 O O   . THR B 192 ? 1.15672 0.77286 0.53009 0.00051  0.20187  -0.04112 961  THR A O   
3034 C CB  . THR B 192 ? 1.22164 0.84039 0.66035 0.01086  0.21073  0.00212  961  THR A CB  
3035 O OG1 . THR B 192 ? 1.21502 0.82431 0.66625 0.01049  0.20976  -0.00759 961  THR A OG1 
3036 C CG2 . THR B 192 ? 1.23806 0.86434 0.70411 0.01409  0.21303  0.02671  961  THR A CG2 
3037 N N   . MET B 193 ? 0.80730 0.97706 0.74579 0.15397  -0.06618 -0.02139 962  MET A N   
3038 C CA  . MET B 193 ? 0.77264 0.95982 0.71743 0.15454  -0.06752 -0.01656 962  MET A CA  
3039 C C   . MET B 193 ? 0.74434 0.92509 0.67859 0.16565  -0.06325 -0.01938 962  MET A C   
3040 O O   . MET B 193 ? 0.71279 0.87781 0.64085 0.17787  -0.06344 -0.02512 962  MET A O   
3041 C CB  . MET B 193 ? 0.78530 0.98796 0.75353 0.16152  -0.07825 -0.01439 962  MET A CB  
3042 C CG  . MET B 193 ? 0.83154 1.04220 0.80957 0.14896  -0.08264 -0.01000 962  MET A CG  
3043 S SD  . MET B 193 ? 0.84967 1.07890 0.82756 0.12939  -0.08051 -0.00115 962  MET A SD  
3044 C CE  . MET B 193 ? 0.88420 1.13502 0.88834 0.13862  -0.09131 0.00305  962  MET A CE  
3045 N N   . CYS B 194 ? 0.73367 0.92744 0.66657 0.16127  -0.05977 -0.01502 963  CYS A N   
3046 C CA  . CYS B 194 ? 0.70771 0.89878 0.63133 0.17102  -0.05542 -0.01681 963  CYS A CA  
3047 C C   . CYS B 194 ? 0.69216 0.88353 0.62655 0.19003  -0.06264 -0.02162 963  CYS A C   
3048 O O   . CYS B 194 ? 0.70369 0.90874 0.65822 0.19387  -0.07080 -0.02068 963  CYS A O   
3049 C CB  . CYS B 194 ? 0.69239 0.90177 0.61820 0.16328  -0.05151 -0.01095 963  CYS A CB  
3050 S SG  . CYS B 194 ? 0.69536 0.90703 0.61266 0.17486  -0.04592 -0.01240 963  CYS A SG  
3051 N N   . PRO B 195 ? 0.69480 0.87078 0.61661 0.20204  -0.06067 -0.02678 964  PRO A N   
3052 C CA  . PRO B 195 ? 0.69250 0.86766 0.62318 0.22042  -0.06791 -0.03209 964  PRO A CA  
3053 C C   . PRO B 195 ? 0.68708 0.87830 0.62312 0.22795  -0.06754 -0.03181 964  PRO A C   
3054 O O   . PRO B 195 ? 0.67023 0.86261 0.61449 0.24328  -0.07371 -0.03676 964  PRO A O   
3055 C CB  . PRO B 195 ? 0.69341 0.84464 0.60590 0.22838  -0.06551 -0.03724 964  PRO A CB  
3056 C CG  . PRO B 195 ? 0.70562 0.85063 0.59816 0.21660  -0.05499 -0.03376 964  PRO A CG  
3057 C CD  . PRO B 195 ? 0.71285 0.87000 0.61174 0.19892  -0.05257 -0.02802 964  PRO A CD  
3058 N N   . VAL B 196 ? 0.67708 0.88024 0.60849 0.21801  -0.06023 -0.02675 965  VAL A N   
3059 C CA  . VAL B 196 ? 0.67983 0.89991 0.61766 0.22459  -0.05887 -0.02670 965  VAL A CA  
3060 C C   . VAL B 196 ? 0.68006 0.92244 0.64359 0.22088  -0.06529 -0.02328 965  VAL A C   
3061 O O   . VAL B 196 ? 0.68503 0.93658 0.66564 0.23301  -0.07262 -0.02679 965  VAL A O   
3062 C CB  . VAL B 196 ? 0.67392 0.89565 0.59421 0.21670  -0.04739 -0.02297 965  VAL A CB  
3063 C CG1 . VAL B 196 ? 0.67010 0.91177 0.59880 0.22276  -0.04507 -0.02297 965  VAL A CG1 
3064 C CG2 . VAL B 196 ? 0.66308 0.86219 0.55906 0.22141  -0.04249 -0.02604 965  VAL A CG2 
3065 N N   . CYS B 197 ? 0.67219 0.92236 0.63933 0.20419  -0.06373 -0.01658 966  CYS A N   
3066 C CA  . CYS B 197 ? 0.68183 0.95312 0.67319 0.19935  -0.07045 -0.01220 966  CYS A CA  
3067 C C   . CYS B 197 ? 0.70996 0.97917 0.71585 0.19892  -0.08082 -0.01198 966  CYS A C   
3068 O O   . CYS B 197 ? 0.69888 0.98430 0.72754 0.19901  -0.08898 -0.00924 966  CYS A O   
3069 C CB  . CYS B 197 ? 0.69901 0.98191 0.68871 0.18122  -0.06484 -0.00443 966  CYS A CB  
3070 S SG  . CYS B 197 ? 0.75890 1.02683 0.73016 0.16245  -0.06002 -0.00067 966  CYS A SG  
3071 N N   . LEU B 198 ? 0.74316 0.99334 0.73731 0.19779  -0.08066 -0.01438 967  LEU A N   
3072 C CA  . LEU B 198 ? 0.75761 1.00444 0.76345 0.19634  -0.08918 -0.01408 967  LEU A CA  
3073 C C   . LEU B 198 ? 0.79784 1.05920 0.81516 0.18012  -0.09237 -0.00622 967  LEU A C   
3074 O O   . LEU B 198 ? 0.88178 1.14549 0.91270 0.17832  -0.10059 -0.00447 967  LEU A O   
3075 C CB  . LEU B 198 ? 0.75431 1.00370 0.77880 0.21329  -0.09954 -0.01864 967  LEU A CB  
3076 C CG  . LEU B 198 ? 0.75159 0.98999 0.76758 0.23100  -0.09831 -0.02660 967  LEU A CG  
3077 C CD1 . LEU B 198 ? 0.77335 1.01369 0.80930 0.24628  -0.10991 -0.03116 967  LEU A CD1 
3078 C CD2 . LEU B 198 ? 0.74082 0.95601 0.73341 0.23084  -0.09198 -0.03005 967  LEU A CD2 
3079 N N   . ASP B 199 ? 0.79400 1.06418 0.80478 0.16745  -0.08595 -0.00115 968  ASP A N   
3080 C CA  . ASP B 199 ? 0.82255 1.10994 0.84579 0.15299  -0.08968 0.00681  968  ASP A CA  
3081 C C   . ASP B 199 ? 0.83535 1.11703 0.84146 0.13436  -0.08287 0.01060  968  ASP A C   
3082 O O   . ASP B 199 ? 0.83106 1.11660 0.84178 0.12236  -0.08719 0.01507  968  ASP A O   
3083 C CB  . ASP B 199 ? 0.81928 1.12596 0.85487 0.15532  -0.08954 0.00948  968  ASP A CB  
3084 C CG  . ASP B 199 ? 0.88890 1.21487 0.94202 0.14265  -0.09575 0.01780  968  ASP A CG  
3085 O OD1 . ASP B 199 ? 0.93449 1.25946 0.99031 0.13244  -0.10105 0.02178  968  ASP A OD1 
3086 O OD2 . ASP B 199 ? 0.93722 1.27974 1.00190 0.14305  -0.09550 0.02037  968  ASP A OD2 
3087 N N   . ARG B 200 ? 0.82084 1.09339 0.80703 0.13139  -0.07248 0.00896  969  ARG A N   
3088 C CA  . ARG B 200 ? 0.80348 1.06806 0.77210 0.11482  -0.06553 0.01116  969  ARG A CA  
3089 C C   . ARG B 200 ? 0.79715 1.03866 0.74989 0.11795  -0.06189 0.00482  969  ARG A C   
3090 O O   . ARG B 200 ? 0.79294 1.02503 0.74797 0.13282  -0.06468 -0.00070 969  ARG A O   
3091 C CB  . ARG B 200 ? 0.79576 1.06331 0.75312 0.10919  -0.05665 0.01340  969  ARG A CB  
3092 C CG  . ARG B 200 ? 0.80424 1.09475 0.77765 0.10640  -0.05901 0.01924  969  ARG A CG  
3093 C CD  . ARG B 200 ? 0.81565 1.10635 0.77806 0.10787  -0.04947 0.01914  969  ARG A CD  
3094 N NE  . ARG B 200 ? 0.81393 1.12641 0.79349 0.11012  -0.05092 0.02278  969  ARG A NE  
3095 C CZ  . ARG B 200 ? 0.85870 1.17962 0.85236 0.12585  -0.05450 0.01951  969  ARG A CZ  
3096 N NH1 . ARG B 200 ? 0.84915 1.15869 0.84195 0.14070  -0.05785 0.01292  969  ARG A NH1 
3097 N NH2 . ARG B 200 ? 0.88387 1.22529 0.89368 0.12674  -0.05488 0.02253  969  ARG A NH2 
3098 N N   . LEU B 201 ? 0.78715 1.01941 0.72453 0.10382  -0.05595 0.00529  970  LEU A N   
3099 C CA  . LEU B 201 ? 0.77259 0.98285 0.69500 0.10553  -0.05145 -0.00101 970  LEU A CA  
3100 C C   . LEU B 201 ? 0.75041 0.94714 0.65492 0.10874  -0.04270 -0.00382 970  LEU A C   
3101 O O   . LEU B 201 ? 0.75053 0.95503 0.65130 0.10490  -0.03852 -0.00006 970  LEU A O   
3102 C CB  . LEU B 201 ? 0.80919 1.01557 0.72449 0.08882  -0.04944 -0.00021 970  LEU A CB  
3103 C CG  . LEU B 201 ? 0.82955 1.04659 0.75905 0.08351  -0.05741 0.00275  970  LEU A CG  
3104 C CD1 . LEU B 201 ? 0.81729 1.03839 0.73863 0.06285  -0.05469 0.00646  970  LEU A CD1 
3105 C CD2 . LEU B 201 ? 0.80636 1.01042 0.73850 0.09324  -0.05985 -0.00333 970  LEU A CD2 
3106 N N   . LYS B 202 ? 0.75263 0.92906 0.64703 0.11607  -0.04034 -0.01019 971  LYS A N   
3107 C CA  . LYS B 202 ? 0.73551 0.89623 0.61207 0.11867  -0.03276 -0.01269 971  LYS A CA  
3108 C C   . LYS B 202 ? 0.74646 0.90228 0.60945 0.10108  -0.02553 -0.01076 971  LYS A C   
3109 O O   . LYS B 202 ? 0.77955 0.92400 0.63684 0.09392  -0.02380 -0.01420 971  LYS A O   
3110 C CB  . LYS B 202 ? 0.73359 0.87370 0.60508 0.13122  -0.03366 -0.01985 971  LYS A CB  
3111 C CG  . LYS B 202 ? 0.74847 0.89207 0.63221 0.14907  -0.04104 -0.02223 971  LYS A CG  
3112 C CD  . LYS B 202 ? 0.75370 0.87627 0.63152 0.16206  -0.04221 -0.02901 971  LYS A CD  
3113 C CE  . LYS B 202 ? 0.77293 0.88733 0.65728 0.16059  -0.04539 -0.03291 971  LYS A CE  
3114 N NZ  . LYS B 202 ? 0.78528 0.87808 0.66375 0.17251  -0.04610 -0.03947 971  LYS A NZ  
3115 N N   . ASN B 203 ? 0.75186 0.91682 0.61041 0.09369  -0.02122 -0.00551 972  ASN A N   
3116 C CA  . ASN B 203 ? 0.76401 0.92384 0.60953 0.07728  -0.01455 -0.00360 972  ASN A CA  
3117 C C   . ASN B 203 ? 0.77319 0.92156 0.60374 0.07910  -0.00744 -0.00327 972  ASN A C   
3118 O O   . ASN B 203 ? 0.77302 0.92138 0.59503 0.06603  -0.00216 0.00008  972  ASN A O   
3119 C CB  . ASN B 203 ? 0.74616 0.92666 0.59945 0.06308  -0.01586 0.00335  972  ASN A CB  
3120 C CG  . ASN B 203 ? 0.73083 0.92847 0.59231 0.06756  -0.01609 0.00876  972  ASN A CG  
3121 O OD1 . ASN B 203 ? 0.74443 0.94288 0.61024 0.08291  -0.01751 0.00702  972  ASN A OD1 
3122 N ND2 . ASN B 203 ? 0.70099 0.91239 0.56465 0.05415  -0.01453 0.01496  972  ASN A ND2 
3123 N N   . MET B 204 ? 0.76602 0.90434 0.59298 0.09463  -0.00760 -0.00640 973  MET A N   
3124 C CA  . MET B 204 ? 0.77079 0.89716 0.58266 0.09719  -0.00147 -0.00564 973  MET A CA  
3125 C C   . MET B 204 ? 0.77067 0.87738 0.57615 0.11213  -0.00308 -0.01155 973  MET A C   
3126 O O   . MET B 204 ? 0.77806 0.88847 0.59244 0.12601  -0.00868 -0.01410 973  MET A O   
3127 C CB  . MET B 204 ? 0.78753 0.93079 0.60236 0.10020  0.00045  -0.00003 973  MET A CB  
3128 C CG  . MET B 204 ? 0.78880 0.91975 0.58874 0.10766  0.00542  0.00023  973  MET A CG  
3129 S SD  . MET B 204 ? 0.85005 1.00209 0.65363 0.11164  0.00874  0.00602  973  MET A SD  
3130 C CE  . MET B 204 ? 0.85827 1.02318 0.66308 0.09041  0.01391  0.01342  973  MET A CE  
3131 N N   . ILE B 205 ? 0.76602 0.85183 0.55672 0.10942  0.00128  -0.01355 974  ILE A N   
3132 C CA  . ILE B 205 ? 0.78193 0.84653 0.56675 0.12165  -0.00080 -0.01934 974  ILE A CA  
3133 C C   . ILE B 205 ? 0.79686 0.84894 0.56614 0.12632  0.00307  -0.01711 974  ILE A C   
3134 O O   . ILE B 205 ? 0.78767 0.83839 0.54720 0.11558  0.00902  -0.01253 974  ILE A O   
3135 C CB  . ILE B 205 ? 0.79602 0.84510 0.57948 0.11451  -0.00023 -0.02477 974  ILE A CB  
3136 C CG1 . ILE B 205 ? 0.80382 0.86651 0.60239 0.11153  -0.00458 -0.02650 974  ILE A CG1 
3137 C CG2 . ILE B 205 ? 0.78250 0.80756 0.55997 0.12541  -0.00184 -0.03065 974  ILE A CG2 
3138 C CD1 . ILE B 205 ? 0.88154 0.93038 0.68258 0.11190  -0.00592 -0.03348 974  ILE A CD1 
3139 N N   . PHE B 206 ? 0.79712 0.84020 0.56408 0.14215  -0.00074 -0.02003 975  PHE A N   
3140 C CA  . PHE B 206 ? 0.82373 0.85154 0.57460 0.14770  0.00169  -0.01841 975  PHE A CA  
3141 C C   . PHE B 206 ? 0.85693 0.85849 0.60182 0.15041  -0.00015 -0.02364 975  PHE A C   
3142 O O   . PHE B 206 ? 0.84674 0.84334 0.60119 0.15132  -0.00366 -0.02938 975  PHE A O   
3143 C CB  . PHE B 206 ? 0.80707 0.84083 0.55713 0.16342  -0.00152 -0.01831 975  PHE A CB  
3144 C CG  . PHE B 206 ? 0.79304 0.85317 0.55645 0.16512  -0.00262 -0.01643 975  PHE A CG  
3145 C CD1 . PHE B 206 ? 0.79694 0.87484 0.56231 0.15323  0.00288  -0.01038 975  PHE A CD1 
3146 C CD2 . PHE B 206 ? 0.77173 0.83871 0.54696 0.17889  -0.00968 -0.02076 975  PHE A CD2 
3147 C CE1 . PHE B 206 ? 0.78372 0.88604 0.56348 0.15505  0.00132  -0.00875 975  PHE A CE1 
3148 C CE2 . PHE B 206 ? 0.76286 0.85380 0.55212 0.18088  -0.01131 -0.01930 975  PHE A CE2 
3149 C CZ  . PHE B 206 ? 0.76384 0.87255 0.55573 0.16898  -0.00581 -0.01331 975  PHE A CZ  
3150 N N   . LEU B 207 ? 0.88028 0.86517 0.60976 0.15129  0.00231  -0.02134 976  LEU A N   
3151 C CA  . LEU B 207 ? 0.90547 0.86447 0.62966 0.15309  0.00055  -0.02576 976  LEU A CA  
3152 C C   . LEU B 207 ? 0.89896 0.84836 0.62888 0.16931  -0.00720 -0.03191 976  LEU A C   
3153 O O   . LEU B 207 ? 0.93309 0.86369 0.66465 0.17124  -0.00968 -0.03715 976  LEU A O   
3154 C CB  . LEU B 207 ? 0.98721 0.93075 0.69388 0.14995  0.00415  -0.02067 976  LEU A CB  
3155 C CG  . LEU B 207 ? 1.03193 0.97422 0.73297 0.13244  0.01103  -0.01646 976  LEU A CG  
3156 C CD1 . LEU B 207 ? 0.97135 0.93845 0.68039 0.12119  0.01499  -0.01336 976  LEU A CD1 
3157 C CD2 . LEU B 207 ? 1.07062 1.00238 0.75474 0.13054  0.01425  -0.00933 976  LEU A CD2 
3158 N N   . CYS B 208 ? 0.86805 0.82984 0.60203 0.18102  -0.01123 -0.03177 977  CYS A N   
3159 C CA  . CYS B 208 ? 0.85638 0.80999 0.59707 0.19643  -0.01936 -0.03771 977  CYS A CA  
3160 C C   . CYS B 208 ? 0.86411 0.82206 0.62296 0.19570  -0.02278 -0.04349 977  CYS A C   
3161 O O   . CYS B 208 ? 0.86062 0.81028 0.62724 0.20717  -0.02956 -0.04887 977  CYS A O   
3162 C CB  . CYS B 208 ? 0.84470 0.81098 0.58469 0.20882  -0.02269 -0.03644 977  CYS A CB  
3163 S SG  . CYS B 208 ? 0.79632 0.79559 0.55018 0.20444  -0.02072 -0.03372 977  CYS A SG  
3164 N N   . GLY B 209 ? 0.84673 0.81748 0.61244 0.18232  -0.01851 -0.04231 978  GLY A N   
3165 C CA  . GLY B 209 ? 0.84449 0.81968 0.62590 0.18038  -0.02123 -0.04716 978  GLY A CA  
3166 C C   . GLY B 209 ? 0.80988 0.80874 0.60537 0.18213  -0.02454 -0.04575 978  GLY A C   
3167 O O   . GLY B 209 ? 0.83346 0.83909 0.64166 0.17764  -0.02614 -0.04818 978  GLY A O   
3168 N N   . HIS B 210 ? 0.78913 0.80052 0.58329 0.18882  -0.02584 -0.04210 979  HIS A N   
3169 C CA  . HIS B 210 ? 0.75367 0.78790 0.56263 0.19079  -0.02943 -0.04064 979  HIS A CA  
3170 C C   . HIS B 210 ? 0.74355 0.79585 0.55172 0.17673  -0.02357 -0.03433 979  HIS A C   
3171 O O   . HIS B 210 ? 0.76750 0.81475 0.56267 0.16692  -0.01680 -0.03097 979  HIS A O   
3172 C CB  . HIS B 210 ? 0.70150 0.73952 0.51192 0.20725  -0.03479 -0.04166 979  HIS A CB  
3173 C CG  . HIS B 210 ? 0.74447 0.76425 0.55528 0.22112  -0.04133 -0.04763 979  HIS A CG  
3174 N ND1 . HIS B 210 ? 0.76510 0.76914 0.56125 0.23053  -0.04199 -0.04853 979  HIS A ND1 
3175 C CD2 . HIS B 210 ? 0.74780 0.76241 0.57213 0.22671  -0.04774 -0.05269 979  HIS A CD2 
3176 C CE1 . HIS B 210 ? 0.76882 0.75853 0.56986 0.24158  -0.04906 -0.05408 979  HIS A CE1 
3177 N NE2 . HIS B 210 ? 0.78670 0.78272 0.60537 0.23960  -0.05242 -0.05678 979  HIS A NE2 
3178 N N   . GLY B 211 ? 0.69902 0.77222 0.52244 0.17521  -0.02681 -0.03252 980  GLY A N   
3179 C CA  . GLY B 211 ? 0.73145 0.82287 0.55688 0.16168  -0.02251 -0.02646 980  GLY A CA  
3180 C C   . GLY B 211 ? 0.73590 0.85075 0.57731 0.16597  -0.02708 -0.02394 980  GLY A C   
3181 O O   . GLY B 211 ? 0.73105 0.84899 0.58460 0.17805  -0.03439 -0.02724 980  GLY A O   
3182 N N   . THR B 212 ? 0.73340 0.86483 0.57595 0.15560  -0.02304 -0.01801 981  THR A N   
3183 C CA  . THR B 212 ? 0.72821 0.88364 0.58733 0.15713  -0.02674 -0.01482 981  THR A CA  
3184 C C   . THR B 212 ? 0.72961 0.89905 0.59373 0.13926  -0.02455 -0.00902 981  THR A C   
3185 O O   . THR B 212 ? 0.74489 0.90506 0.59897 0.12644  -0.02021 -0.00820 981  THR A O   
3186 C CB  . THR B 212 ? 0.73767 0.90127 0.59331 0.16583  -0.02376 -0.01346 981  THR A CB  
3187 O OG1 . THR B 212 ? 0.75281 0.91721 0.59564 0.15435  -0.01503 -0.00843 981  THR A OG1 
3188 C CG2 . THR B 212 ? 0.72266 0.87020 0.56846 0.18221  -0.02516 -0.01890 981  THR A CG2 
3189 N N   . CYS B 213 ? 0.71325 0.90504 0.59339 0.13836  -0.02794 -0.00517 982  CYS A N   
3190 C CA  . CYS B 213 ? 0.72499 0.93133 0.60825 0.12204  -0.02517 0.00136  982  CYS A CA  
3191 C C   . CYS B 213 ? 0.75687 0.96481 0.62847 0.11907  -0.01668 0.00461  982  CYS A C   
3192 O O   . CYS B 213 ? 0.77013 0.97265 0.63439 0.13078  -0.01392 0.00235  982  CYS A O   
3193 C CB  . CYS B 213 ? 0.72139 0.95117 0.62746 0.12177  -0.03242 0.00486  982  CYS A CB  
3194 S SG  . CYS B 213 ? 0.71360 0.96315 0.63220 0.13359  -0.03250 0.00612  982  CYS A SG  
3195 N N   . GLN B 214 ? 0.75743 0.97274 0.62688 0.10278  -0.01262 0.01017  983  GLN A N   
3196 C CA  . GLN B 214 ? 0.78464 1.00142 0.64339 0.09794  -0.00426 0.01406  983  GLN A CA  
3197 C C   . GLN B 214 ? 0.78618 1.02123 0.65516 0.10745  -0.00353 0.01583  983  GLN A C   
3198 O O   . GLN B 214 ? 0.80130 1.03286 0.65933 0.11270  0.00285  0.01608  983  GLN A O   
3199 C CB  . GLN B 214 ? 0.78366 1.00633 0.64100 0.07823  -0.00139 0.01967  983  GLN A CB  
3200 C CG  . GLN B 214 ? 0.83949 1.06485 0.68769 0.07149  0.00697  0.02458  983  GLN A CG  
3201 C CD  . GLN B 214 ? 0.88641 1.11512 0.73252 0.05176  0.00912  0.02953  983  GLN A CD  
3202 O OE1 . GLN B 214 ? 0.83742 1.07481 0.69349 0.04302  0.00372  0.03083  983  GLN A OE1 
3203 N NE2 . GLN B 214 ? 0.90614 1.12775 0.73899 0.04424  0.01664  0.03257  983  GLN A NE2 
3204 N N   . LEU B 215 ? 0.77898 1.03371 0.66918 0.10969  -0.01003 0.01700  984  LEU A N   
3205 C CA  . LEU B 215 ? 0.77510 1.04928 0.67803 0.11804  -0.00936 0.01811  984  LEU A CA  
3206 C C   . LEU B 215 ? 0.77239 1.03885 0.66962 0.13683  -0.00887 0.01187  984  LEU A C   
3207 O O   . LEU B 215 ? 0.75093 1.02313 0.64338 0.14230  -0.00263 0.01216  984  LEU A O   
3208 C CB  . LEU B 215 ? 0.77355 1.06846 0.70212 0.11707  -0.01800 0.02012  984  LEU A CB  
3209 C CG  . LEU B 215 ? 0.77440 1.08508 0.71106 0.09982  -0.01687 0.02778  984  LEU A CG  
3210 C CD1 . LEU B 215 ? 0.78988 1.11641 0.74984 0.09704  -0.02725 0.03020  984  LEU A CD1 
3211 C CD2 . LEU B 215 ? 0.80064 1.12601 0.74004 0.10014  -0.00948 0.03086  984  LEU A CD2 
3212 N N   . CYS B 216 ? 0.76141 1.01533 0.65920 0.14676  -0.01551 0.00618  985  CYS A N   
3213 C CA  . CYS B 216 ? 0.75989 1.00484 0.65130 0.16447  -0.01601 -0.00004 985  CYS A CA  
3214 C C   . CYS B 216 ? 0.78110 1.00553 0.64684 0.16449  -0.00850 -0.00065 985  CYS A C   
3215 O O   . CYS B 216 ? 0.79339 1.01625 0.64986 0.17439  -0.00459 -0.00252 985  CYS A O   
3216 C CB  . CYS B 216 ? 0.69497 0.93198 0.59538 0.17454  -0.02583 -0.00561 985  CYS A CB  
3217 S SG  . CYS B 216 ? 0.72310 0.98372 0.65433 0.17497  -0.03558 -0.00413 985  CYS A SG  
3218 N N   . GLY B 217 ? 0.78487 0.99361 0.63890 0.15315  -0.00648 0.00094  986  GLY A N   
3219 C CA  . GLY B 217 ? 0.77822 0.96537 0.60940 0.15348  -0.00081 0.00023  986  GLY A CA  
3220 C C   . GLY B 217 ? 0.81740 1.01004 0.63748 0.14848  0.00843  0.00541  986  GLY A C   
3221 O O   . GLY B 217 ? 0.84306 1.02440 0.64718 0.15578  0.01226  0.00448  986  GLY A O   
3222 N N   . ASP B 218 ? 0.81158 1.02260 0.64063 0.13633  0.01180  0.01123  987  ASP A N   
3223 C CA  . ASP B 218 ? 0.81623 1.03348 0.63599 0.13076  0.02099  0.01667  987  ASP A CA  
3224 C C   . ASP B 218 ? 0.81560 1.04450 0.63667 0.14440  0.02354  0.01496  987  ASP A C   
3225 O O   . ASP B 218 ? 0.82879 1.05870 0.63760 0.14276  0.03174  0.01852  987  ASP A O   
3226 C CB  . ASP B 218 ? 0.80235 1.03779 0.63362 0.11477  0.02341  0.02324  987  ASP A CB  
3227 C CG  . ASP B 218 ? 0.85526 1.07779 0.67869 0.09876  0.02408  0.02584  987  ASP A CG  
3228 O OD1 . ASP B 218 ? 0.86024 1.05965 0.66621 0.09849  0.02585  0.02394  987  ASP A OD1 
3229 O OD2 . ASP B 218 ? 0.88023 1.11587 0.71538 0.08632  0.02254  0.02964  987  ASP A OD2 
3230 N N   . ARG B 219 ? 0.80338 1.04049 0.63847 0.15773  0.01679  0.00940  988  ARG A N   
3231 C CA  . ARG B 219 ? 0.80517 1.05432 0.64309 0.17145  0.01865  0.00626  988  ARG A CA  
3232 C C   . ARG B 219 ? 0.80402 1.03436 0.62575 0.18637  0.01686  0.00023  988  ARG A C   
3233 O O   . ARG B 219 ? 0.77910 1.01734 0.60256 0.19969  0.01685  -0.00416 988  ARG A O   
3234 C CB  . ARG B 219 ? 0.81252 1.08332 0.67756 0.17734  0.01184  0.00353  988  ARG A CB  
3235 C CG  . ARG B 219 ? 0.83079 1.12487 0.71243 0.16496  0.01478  0.00978  988  ARG A CG  
3236 C CD  . ARG B 219 ? 0.85339 1.16599 0.76346 0.16800  0.00585  0.00819  988  ARG A CD  
3237 N NE  . ARG B 219 ? 0.95105 1.26970 0.87110 0.18619  0.00131  0.00076  988  ARG A NE  
3238 C CZ  . ARG B 219 ? 0.98321 1.31811 0.90931 0.19459  0.00601  -0.00157 988  ARG A CZ  
3239 N NH1 . ARG B 219 ? 0.98566 1.33312 0.90893 0.18676  0.01598  0.00337  988  ARG A NH1 
3240 N NH2 . ARG B 219 ? 0.91445 1.25358 0.85045 0.21118  0.00062  -0.00933 988  ARG A NH2 
3241 N N   . MET B 220 ? 0.80408 1.00973 0.60984 0.18425  0.01552  -0.00022 989  MET A N   
3242 C CA  . MET B 220 ? 0.80867 0.99473 0.60001 0.19786  0.01231  -0.00570 989  MET A CA  
3243 C C   . MET B 220 ? 0.81771 0.98373 0.58424 0.19173  0.01847  -0.00168 989  MET A C   
3244 O O   . MET B 220 ? 0.81968 0.98113 0.58232 0.17697  0.02235  0.00365  989  MET A O   
3245 C CB  . MET B 220 ? 0.81895 0.99246 0.61874 0.20330  0.00215  -0.01119 989  MET A CB  
3246 C CG  . MET B 220 ? 0.81986 1.01151 0.64580 0.20400  -0.00466 -0.01296 989  MET A CG  
3247 S SD  . MET B 220 ? 0.87203 1.04814 0.70654 0.20895  -0.01569 -0.01844 989  MET A SD  
3248 C CE  . MET B 220 ? 0.77031 0.92953 0.59106 0.22826  -0.01887 -0.02534 989  MET A CE  
3249 N N   . SER B 221 ? 0.80593 0.95991 0.55572 0.20306  0.01889  -0.00421 990  SER A N   
3250 C CA  . SER B 221 ? 0.78849 0.92049 0.51439 0.19940  0.02273  -0.00068 990  SER A CA  
3251 C C   . SER B 221 ? 0.79458 0.90103 0.51292 0.20812  0.01477  -0.00590 990  SER A C   
3252 O O   . SER B 221 ? 0.81384 0.89933 0.51490 0.20442  0.01622  -0.00321 990  SER A O   
3253 C CB  . SER B 221 ? 0.77553 0.91255 0.48497 0.20367  0.03010  0.00214  990  SER A CB  
3254 O OG  . SER B 221 ? 0.76928 0.90999 0.47886 0.22059  0.02600  -0.00471 990  SER A OG  
3255 N N   . GLU B 222 ? 0.79472 0.90239 0.52650 0.21964  0.00612  -0.01309 991  GLU A N   
3256 C CA  . GLU B 222 ? 0.80407 0.88923 0.53229 0.22849  -0.00216 -0.01850 991  GLU A CA  
3257 C C   . GLU B 222 ? 0.79524 0.88349 0.54476 0.22756  -0.00912 -0.02242 991  GLU A C   
3258 O O   . GLU B 222 ? 0.75000 0.85918 0.51780 0.22677  -0.01030 -0.02292 991  GLU A O   
3259 C CB  . GLU B 222 ? 0.78802 0.86936 0.50979 0.24622  -0.00708 -0.02411 991  GLU A CB  
3260 C CG  . GLU B 222 ? 0.80711 0.89003 0.50869 0.24879  -0.00031 -0.02091 991  GLU A CG  
3261 C CD  . GLU B 222 ? 0.82104 0.90567 0.51908 0.26637  -0.00517 -0.02759 991  GLU A CD  
3262 O OE1 . GLU B 222 ? 0.82918 0.93546 0.54129 0.27198  -0.00506 -0.03105 991  GLU A OE1 
3263 O OE2 . GLU B 222 ? 0.82187 0.88596 0.50367 0.27459  -0.00960 -0.02965 991  GLU A OE2 
3264 N N   . CYS B 223 ? 0.78462 0.85197 0.53219 0.22783  -0.01391 -0.02514 992  CYS A N   
3265 C CA  . CYS B 223 ? 0.77692 0.84596 0.54350 0.22700  -0.02029 -0.02893 992  CYS A CA  
3266 C C   . CYS B 223 ? 0.76751 0.84653 0.54882 0.24175  -0.02836 -0.03462 992  CYS A C   
3267 O O   . CYS B 223 ? 0.78865 0.85892 0.56244 0.25549  -0.03235 -0.03861 992  CYS A O   
3268 C CB  . CYS B 223 ? 0.78647 0.83081 0.54833 0.22621  -0.02358 -0.03175 992  CYS A CB  
3269 S SG  . CYS B 223 ? 0.78276 0.82848 0.56788 0.22848  -0.03216 -0.03750 992  CYS A SG  
3270 N N   . PRO B 224 ? 0.74786 0.84420 0.55029 0.23932  -0.03172 -0.03518 993  PRO A N   
3271 C CA  . PRO B 224 ? 0.74067 0.84675 0.55871 0.25329  -0.03994 -0.04044 993  PRO A CA  
3272 C C   . PRO B 224 ? 0.72753 0.81711 0.55072 0.26350  -0.04922 -0.04649 993  PRO A C   
3273 O O   . PRO B 224 ? 0.73009 0.82525 0.56545 0.27612  -0.05688 -0.05127 993  PRO A O   
3274 C CB  . PRO B 224 ? 0.72910 0.85784 0.56844 0.24505  -0.04078 -0.03768 993  PRO A CB  
3275 C CG  . PRO B 224 ? 0.70555 0.82986 0.54171 0.22811  -0.03609 -0.03304 993  PRO A CG  
3276 C CD  . PRO B 224 ? 0.72693 0.83602 0.53959 0.22346  -0.02831 -0.03051 993  PRO A CD  
3277 N N   . ILE B 225 ? 0.73032 0.79968 0.54550 0.25908  -0.04903 -0.04683 994  ILE A N   
3278 C CA  . ILE B 225 ? 0.73577 0.79032 0.55855 0.26735  -0.05749 -0.05235 994  ILE A CA  
3279 C C   . ILE B 225 ? 0.74759 0.77873 0.55301 0.27675  -0.05936 -0.05524 994  ILE A C   
3280 O O   . ILE B 225 ? 0.71649 0.74010 0.52587 0.29068  -0.06767 -0.06055 994  ILE A O   
3281 C CB  . ILE B 225 ? 0.75213 0.80289 0.58355 0.25507  -0.05666 -0.05143 994  ILE A CB  
3282 C CG1 . ILE B 225 ? 0.70990 0.78353 0.55867 0.24604  -0.05646 -0.04825 994  ILE A CG1 
3283 C CG2 . ILE B 225 ? 0.72843 0.76393 0.56842 0.26351  -0.06467 -0.05719 994  ILE A CG2 
3284 C CD1 . ILE B 225 ? 0.64772 0.73056 0.51778 0.25504  -0.06602 -0.05152 994  ILE A CD1 
3285 N N   . CYS B 226 ? 0.75957 0.77850 0.54603 0.26900  -0.05235 -0.05152 995  CYS A N   
3286 C CA  . CYS B 226 ? 0.79879 0.79453 0.56773 0.27613  -0.05414 -0.05293 995  CYS A CA  
3287 C C   . CYS B 226 ? 0.81366 0.80998 0.56181 0.27764  -0.04883 -0.04912 995  CYS A C   
3288 O O   . CYS B 226 ? 0.83005 0.80775 0.56214 0.28404  -0.05099 -0.04960 995  CYS A O   
3289 C CB  . CYS B 226 ? 0.78910 0.76580 0.55274 0.26644  -0.05145 -0.05190 995  CYS A CB  
3290 S SG  . CYS B 226 ? 0.81395 0.79407 0.56398 0.24795  -0.03935 -0.04408 995  CYS A SG  
3291 N N   . ARG B 227 ? 0.82515 0.84197 0.57317 0.27101  -0.04179 -0.04488 996  ARG A N   
3292 C CA  . ARG B 227 ? 0.85405 0.87732 0.58552 0.27272  -0.03599 -0.04150 996  ARG A CA  
3293 C C   . ARG B 227 ? 0.87740 0.88693 0.58740 0.26293  -0.02869 -0.03508 996  ARG A C   
3294 O O   . ARG B 227 ? 0.88277 0.89820 0.57813 0.26236  -0.02269 -0.03108 996  ARG A O   
3295 C CB  . ARG B 227 ? 0.91878 0.93763 0.64394 0.29020  -0.04259 -0.04685 996  ARG A CB  
3296 C CG  . ARG B 227 ? 0.98573 1.01766 0.69829 0.29375  -0.03689 -0.04513 996  ARG A CG  
3297 C CD  . ARG B 227 ? 1.12748 1.15752 0.83761 0.31154  -0.04454 -0.05224 996  ARG A CD  
3298 N NE  . ARG B 227 ? 1.12962 1.17486 0.86478 0.31837  -0.05093 -0.05810 996  ARG A NE  
3299 C CZ  . ARG B 227 ? 1.01209 1.08225 0.76115 0.31708  -0.04753 -0.05829 996  ARG A CZ  
3300 N NH1 . ARG B 227 ? 1.01927 1.10384 0.76050 0.30930  -0.03712 -0.05325 996  ARG A NH1 
3301 N NH2 . ARG B 227 ? 0.96466 1.04565 0.73760 0.32315  -0.05496 -0.06324 996  ARG A NH2 
3302 N N   . LYS B 228 ? 0.90115 0.89388 0.60970 0.25444  -0.02847 -0.03379 997  LYS A N   
3303 C CA  . LYS B 228 ? 0.90153 0.88209 0.59165 0.24422  -0.02175 -0.02732 997  LYS A CA  
3304 C C   . LYS B 228 ? 0.87481 0.87556 0.56418 0.23171  -0.01195 -0.02084 997  LYS A C   
3305 O O   . LYS B 228 ? 0.82850 0.84898 0.53445 0.22682  -0.01052 -0.02125 997  LYS A O   
3306 C CB  . LYS B 228 ? 0.90280 0.86372 0.59507 0.23644  -0.02298 -0.02801 997  LYS A CB  
3307 C CG  . LYS B 228 ? 0.96262 0.90096 0.65483 0.24772  -0.03212 -0.03365 997  LYS A CG  
3308 C CD  . LYS B 228 ? 0.97864 0.90308 0.68017 0.24031  -0.03310 -0.03630 997  LYS A CD  
3309 C CE  . LYS B 228 ? 1.06152 0.96277 0.76407 0.25112  -0.04191 -0.04168 997  LYS A CE  
3310 N NZ  . LYS B 228 ? 1.20907 1.08704 0.89329 0.25048  -0.04208 -0.03815 997  LYS A NZ  
3311 N N   . ALA B 229 ? 0.87649 0.87284 0.54687 0.22674  -0.00559 -0.01443 998  ALA A N   
3312 C CA  . ALA B 229 ? 0.87844 0.89357 0.54817 0.21461  0.00394  -0.00781 998  ALA A CA  
3313 C C   . ALA B 229 ? 0.87454 0.89086 0.55488 0.19927  0.00667  -0.00587 998  ALA A C   
3314 O O   . ALA B 229 ? 0.91836 0.91485 0.59615 0.19476  0.00458  -0.00679 998  ALA A O   
3315 C CB  . ALA B 229 ? 0.84586 0.85359 0.49265 0.21121  0.01011  -0.00067 998  ALA A CB  
3316 N N   . ILE B 230 ? 0.85560 0.89532 0.54802 0.19114  0.01124  -0.00342 999  ILE A N   
3317 C CA  . ILE B 230 ? 0.87242 0.91559 0.57511 0.17632  0.01335  -0.00183 999  ILE A CA  
3318 C C   . ILE B 230 ? 0.91165 0.94398 0.59997 0.16293  0.02009  0.00492  999  ILE A C   
3319 O O   . ILE B 230 ? 0.91206 0.95670 0.59507 0.15603  0.02710  0.01148  999  ILE A O   
3320 C CB  . ILE B 230 ? 0.85212 0.92361 0.57257 0.17161  0.01507  -0.00075 999  ILE A CB  
3321 C CG1 . ILE B 230 ? 0.81197 0.89243 0.54931 0.18367  0.00712  -0.00749 999  ILE A CG1 
3322 C CG2 . ILE B 230 ? 0.83792 0.91331 0.56530 0.15447  0.01803  0.00226  999  ILE A CG2 
3323 C CD1 . ILE B 230 ? 0.79245 0.90011 0.54838 0.17964  0.00763  -0.00611 999  ILE A CD1 
3324 N N   . GLU B 231 ? 0.95408 0.96301 0.63696 0.15948  0.01782  0.00317  1000 GLU A N   
3325 C CA  . GLU B 231 ? 0.99236 0.98812 0.66298 0.14679  0.02300  0.00890  1000 GLU A CA  
3326 C C   . GLU B 231 ? 0.96266 0.97114 0.64211 0.13011  0.02788  0.01186  1000 GLU A C   
3327 O O   . GLU B 231 ? 0.98297 0.99304 0.65468 0.11887  0.03409  0.01886  1000 GLU A O   
3328 C CB  . GLU B 231 ? 1.08292 1.04996 0.74797 0.14886  0.01835  0.00496  1000 GLU A CB  
3329 C CG  . GLU B 231 ? 1.23523 1.18663 0.88967 0.16418  0.01287  0.00304  1000 GLU A CG  
3330 C CD  . GLU B 231 ? 1.37317 1.29631 1.02486 0.16631  0.00761  -0.00101 1000 GLU A CD  
3331 O OE1 . GLU B 231 ? 1.28565 1.20164 0.94402 0.15621  0.00874  -0.00318 1000 GLU A OE1 
3332 O OE2 . GLU B 231 ? 1.53046 1.43866 1.17365 0.17824  0.00214  -0.00237 1000 GLU A OE2 
3333 N N   . ARG B 232 ? 0.94056 0.95756 0.63584 0.12781  0.02482  0.00689  1001 ARG A N   
3334 C CA  . ARG B 232 ? 0.91350 0.93975 0.61620 0.11154  0.02821  0.00890  1001 ARG A CA  
3335 C C   . ARG B 232 ? 0.87559 0.91799 0.59630 0.11273  0.02399  0.00436  1001 ARG A C   
3336 O O   . ARG B 232 ? 0.86083 0.89823 0.58765 0.12394  0.01801  -0.00188 1001 ARG A O   
3337 C CB  . ARG B 232 ? 0.93330 0.93704 0.62931 0.10178  0.02908  0.00738  1001 ARG A CB  
3338 C CG  . ARG B 232 ? 0.92955 0.94060 0.63080 0.08422  0.03258  0.00903  1001 ARG A CG  
3339 C CD  . ARG B 232 ? 0.99940 0.98721 0.69591 0.07677  0.03250  0.00486  1001 ARG A CD  
3340 N NE  . ARG B 232 ? 1.07860 1.07214 0.77821 0.05942  0.03586  0.00605  1001 ARG A NE  
3341 C CZ  . ARG B 232 ? 1.04266 1.01882 0.73637 0.04911  0.03783  0.00456  1001 ARG A CZ  
3342 N NH1 . ARG B 232 ? 1.06437 1.01604 0.74970 0.05405  0.03675  0.00226  1001 ARG A NH1 
3343 N NH2 . ARG B 232 ? 1.01333 0.99652 0.71016 0.03349  0.04039  0.00513  1001 ARG A NH2 
3344 N N   . ARG B 233 ? 0.85272 0.91479 0.58228 0.10118  0.02666  0.00808  1002 ARG A N   
3345 C CA  . ARG B 233 ? 0.84308 0.92167 0.58970 0.09965  0.02252  0.00541  1002 ARG A CA  
3346 C C   . ARG B 233 ? 0.82050 0.89652 0.56909 0.08329  0.02374  0.00500  1002 ARG A C   
3347 O O   . ARG B 233 ? 0.80565 0.88808 0.55155 0.06984  0.02838  0.01038  1002 ARG A O   
3348 C CB  . ARG B 233 ? 0.84879 0.95459 0.60645 0.10046  0.02320  0.00989  1002 ARG A CB  
3349 C CG  . ARG B 233 ? 0.86114 0.97311 0.61883 0.11676  0.02201  0.00919  1002 ARG A CG  
3350 C CD  . ARG B 233 ? 0.87891 1.01563 0.64361 0.11418  0.02600  0.01485  1002 ARG A CD  
3351 N NE  . ARG B 233 ? 0.85878 1.00165 0.62233 0.12950  0.02583  0.01344  1002 ARG A NE  
3352 C CZ  . ARG B 233 ? 0.85774 0.99532 0.60610 0.13305  0.03130  0.01628  1002 ARG A CZ  
3353 N NH1 . ARG B 233 ? 0.82735 0.95260 0.56104 0.12270  0.03695  0.02123  1002 ARG A NH1 
3354 N NH2 . ARG B 233 ? 0.87424 1.01898 0.62192 0.14710  0.03092  0.01408  1002 ARG A NH2 
3355 N N   . ILE B 234 ? 0.81044 0.87801 0.56410 0.08436  0.01957  -0.00153 1003 ILE A N   
3356 C CA  . ILE B 234 ? 0.80224 0.86545 0.55660 0.06993  0.02058  -0.00377 1003 ILE A CA  
3357 C C   . ILE B 234 ? 0.78477 0.86772 0.55414 0.06641  0.01644  -0.00407 1003 ILE A C   
3358 O O   . ILE B 234 ? 0.77942 0.86504 0.55803 0.07700  0.01109  -0.00792 1003 ILE A O   
3359 C CB  . ILE B 234 ? 0.81098 0.84960 0.55986 0.07321  0.01959  -0.01137 1003 ILE A CB  
3360 C CG1 . ILE B 234 ? 0.86181 0.88009 0.59635 0.07664  0.02262  -0.01026 1003 ILE A CG1 
3361 C CG2 . ILE B 234 ? 0.81270 0.84828 0.56306 0.05896  0.02083  -0.01518 1003 ILE A CG2 
3362 C CD1 . ILE B 234 ? 0.88663 0.88201 0.61835 0.08655  0.01973  -0.01733 1003 ILE A CD1 
3363 N N   . LEU B 235 ? 0.78154 0.87776 0.55366 0.05128  0.01827  0.00022  1004 LEU A N   
3364 C CA  . LEU B 235 ? 0.83697 0.95233 0.62301 0.04654  0.01368  0.00115  1004 LEU A CA  
3365 C C   . LEU B 235 ? 0.85019 0.95664 0.63623 0.04004  0.01200  -0.00491 1004 LEU A C   
3366 O O   . LEU B 235 ? 0.83762 0.92813 0.61310 0.03172  0.01594  -0.00827 1004 LEU A O   
3367 C CB  . LEU B 235 ? 0.85501 0.98862 0.64450 0.03261  0.01550  0.00849  1004 LEU A CB  
3368 C CG  . LEU B 235 ? 0.84934 0.99525 0.64083 0.03762  0.01798  0.01474  1004 LEU A CG  
3369 C CD1 . LEU B 235 ? 0.83551 0.99396 0.62780 0.02154  0.02111  0.02151  1004 LEU A CD1 
3370 C CD2 . LEU B 235 ? 0.84988 1.01331 0.65695 0.05017  0.01249  0.01519  1004 LEU A CD2 
3371 N N   . LEU B 236 ? 0.84069 0.95757 0.63901 0.04377  0.00623  -0.00644 1005 LEU A N   
3372 C CA  . LEU B 236 ? 0.87965 0.98930 0.67846 0.03859  0.00489  -0.01229 1005 LEU A CA  
3373 C C   . LEU B 236 ? 0.91483 1.03987 0.71774 0.02229  0.00341  -0.00898 1005 LEU A C   
3374 O O   . LEU B 236 ? 1.00244 1.14738 0.81459 0.01948  0.00011  -0.00226 1005 LEU A O   
3375 C CB  . LEU B 236 ? 0.84764 0.95660 0.65682 0.05279  -0.00076 -0.01640 1005 LEU A CB  
3376 C CG  . LEU B 236 ? 0.83520 0.92876 0.64162 0.06994  -0.00108 -0.02041 1005 LEU A CG  
3377 C CD1 . LEU B 236 ? 0.81454 0.90589 0.63132 0.07920  -0.00649 -0.02554 1005 LEU A CD1 
3378 C CD2 . LEU B 236 ? 0.85823 0.92954 0.64972 0.06662  0.00492  -0.02417 1005 LEU A CD2 
3379 N N   . TYR B 237 ? 0.95512 1.07057 0.75114 0.01154  0.00574  -0.01405 1006 TYR A N   
3380 C CA  . TYR B 237 ? 0.91448 1.04156 0.71145 -0.00493 0.00434  -0.01228 1006 TYR A CA  
3381 C C   . TYR B 237 ? 0.96881 1.08703 0.76376 -0.00815 0.00469  -0.02000 1006 TYR A C   
3382 O O   . TYR B 237 ? 0.93699 1.03778 0.72874 0.00050  0.00726  -0.02735 1006 TYR A O   
3383 C CB  . TYR B 237 ? 0.91609 1.04174 0.70232 -0.02055 0.00900  -0.00977 1006 TYR A CB  
3384 C CG  . TYR B 237 ? 0.94401 1.07631 0.73158 -0.01709 0.01006  -0.00283 1006 TYR A CG  
3385 C CD1 . TYR B 237 ? 0.93488 1.08948 0.73449 -0.01727 0.00561  0.00507  1006 TYR A CD1 
3386 C CD2 . TYR B 237 ? 0.97471 1.09107 0.75241 -0.01284 0.01544  -0.00417 1006 TYR A CD2 
3387 C CE1 . TYR B 237 ? 0.96958 1.13127 0.77125 -0.01354 0.00746  0.01093  1006 TYR A CE1 
3388 C CE2 . TYR B 237 ? 0.96272 1.08563 0.74103 -0.00965 0.01710  0.00240  1006 TYR A CE2 
3389 C CZ  . TYR B 237 ? 0.97148 1.11747 0.76179 -0.00996 0.01357  0.00964  1006 TYR A CZ  
3390 O OH  . TYR B 237 ? 0.90747 1.06112 0.69904 -0.00684 0.01609  0.01573  1006 TYR A OH  
3391 O OXT . TYR B 237 ? 0.90148 1.02974 0.69804 -0.01963 0.00253  -0.01918 1006 TYR A OXT 
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