data_9EIE
# 
_entry.id   9EIE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9EIE         pdb_00009eie 10.2210/pdb9eie/pdb 
WWPDB D_1000290271 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9EIE 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-25 
_pdbx_database_status.SG_entry                        Y 
_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    FoldIt 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        TargetTrack 
_pdbx_database_related.db_id          Tcru006532 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              merritt@uw.edu 
_pdbx_contact_author.name_first         Ethan 
_pdbx_contact_author.name_last          Merritt 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1498-244X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Merritt, E.A.'                                                1 0000-0003-1498-244X 
'Structural Genomics of Pathogenic Protozoa Consortium (SGPP)' 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                     'Prediction and determination of a Structure Genomics target after 20 years' 
_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 'Merritt, E.A.'     1  0000-0003-1498-244X 
primary 'Anderson, L.'      2  ?                   
primary 'Boni, E.'          3  ?                   
primary 'Buckner, F.S.'     4  ?                   
primary 'Earnest, T.N.'     5  ?                   
primary 'Hol, W.G.'         6  ?                   
primary 'Holmes, M.A.'      7  ?                   
primary 'Kim, D.'           8  ?                   
primary 'Mehlin, C.'        9  ?                   
primary 'Neely, H.'         10 ?                   
primary 'Van Voorhis, W.C.' 11 ?                   
primary 'Zucker, F.'        12 ?                   
# 
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 'Trypanosomatid-specific protein of unknown function' 23645.236 2  ? ? ? ? 
2 non-polymer syn 'POTASSIUM ION'                                       39.098    2  ? ? ? ? 
3 non-polymer syn GLYCEROL                                              92.094    2  ? ? ? ? 
4 water       nat water                                                 18.015    78 ? ? ? ? 
# 
_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       
;GPGSMEMSRSSDTFSASRNRVRADEINDEEDHADAAYVEKHNLQCLFSEMAEQLSEKDPKTEQEAERILLEFLTHRKAER
DRAALRLQFSHSFEVNLDNGRKIMRLQLGQETSTLQLEQKGRVLKMDEAFSISLEQTEELTEMFYELGRFVVDGTKGEQG
GFISIDERDVYLLAAGRECAEAGDELFNLAMLFSMDRGKKSEQTSGEA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPGSMEMSRSSDTFSASRNRVRADEINDEEDHADAAYVEKHNLQCLFSEMAEQLSEKDPKTEQEAERILLEFLTHRKAER
DRAALRLQFSHSFEVNLDNGRKIMRLQLGQETSTLQLEQKGRVLKMDEAFSISLEQTEELTEMFYELGRFVVDGTKGEQG
GFISIDERDVYLLAAGRECAEAGDELFNLAMLFSMDRGKKSEQTSGEA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         Tcru006532 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'POTASSIUM ION' K   
3 GLYCEROL        GOL 
4 water           HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   GLY n 
1 4   SER n 
1 5   MET n 
1 6   GLU n 
1 7   MET n 
1 8   SER n 
1 9   ARG n 
1 10  SER n 
1 11  SER n 
1 12  ASP n 
1 13  THR n 
1 14  PHE n 
1 15  SER n 
1 16  ALA n 
1 17  SER n 
1 18  ARG n 
1 19  ASN n 
1 20  ARG n 
1 21  VAL n 
1 22  ARG n 
1 23  ALA n 
1 24  ASP n 
1 25  GLU n 
1 26  ILE n 
1 27  ASN n 
1 28  ASP n 
1 29  GLU n 
1 30  GLU n 
1 31  ASP n 
1 32  HIS n 
1 33  ALA n 
1 34  ASP n 
1 35  ALA n 
1 36  ALA n 
1 37  TYR n 
1 38  VAL n 
1 39  GLU n 
1 40  LYS n 
1 41  HIS n 
1 42  ASN n 
1 43  LEU n 
1 44  GLN n 
1 45  CYS n 
1 46  LEU n 
1 47  PHE n 
1 48  SER n 
1 49  GLU n 
1 50  MET n 
1 51  ALA n 
1 52  GLU n 
1 53  GLN n 
1 54  LEU n 
1 55  SER n 
1 56  GLU n 
1 57  LYS n 
1 58  ASP n 
1 59  PRO n 
1 60  LYS n 
1 61  THR n 
1 62  GLU n 
1 63  GLN n 
1 64  GLU n 
1 65  ALA n 
1 66  GLU n 
1 67  ARG n 
1 68  ILE n 
1 69  LEU n 
1 70  LEU n 
1 71  GLU n 
1 72  PHE n 
1 73  LEU n 
1 74  THR n 
1 75  HIS n 
1 76  ARG n 
1 77  LYS n 
1 78  ALA n 
1 79  GLU n 
1 80  ARG n 
1 81  ASP n 
1 82  ARG n 
1 83  ALA n 
1 84  ALA n 
1 85  LEU n 
1 86  ARG n 
1 87  LEU n 
1 88  GLN n 
1 89  PHE n 
1 90  SER n 
1 91  HIS n 
1 92  SER n 
1 93  PHE n 
1 94  GLU n 
1 95  VAL n 
1 96  ASN n 
1 97  LEU n 
1 98  ASP n 
1 99  ASN n 
1 100 GLY n 
1 101 ARG n 
1 102 LYS n 
1 103 ILE n 
1 104 MET n 
1 105 ARG n 
1 106 LEU n 
1 107 GLN n 
1 108 LEU n 
1 109 GLY n 
1 110 GLN n 
1 111 GLU n 
1 112 THR n 
1 113 SER n 
1 114 THR n 
1 115 LEU n 
1 116 GLN n 
1 117 LEU n 
1 118 GLU n 
1 119 GLN n 
1 120 LYS n 
1 121 GLY n 
1 122 ARG n 
1 123 VAL n 
1 124 LEU n 
1 125 LYS n 
1 126 MET n 
1 127 ASP n 
1 128 GLU n 
1 129 ALA n 
1 130 PHE n 
1 131 SER n 
1 132 ILE n 
1 133 SER n 
1 134 LEU n 
1 135 GLU n 
1 136 GLN n 
1 137 THR n 
1 138 GLU n 
1 139 GLU n 
1 140 LEU n 
1 141 THR n 
1 142 GLU n 
1 143 MET n 
1 144 PHE n 
1 145 TYR n 
1 146 GLU n 
1 147 LEU n 
1 148 GLY n 
1 149 ARG n 
1 150 PHE n 
1 151 VAL n 
1 152 VAL n 
1 153 ASP n 
1 154 GLY n 
1 155 THR n 
1 156 LYS n 
1 157 GLY n 
1 158 GLU n 
1 159 GLN n 
1 160 GLY n 
1 161 GLY n 
1 162 PHE n 
1 163 ILE n 
1 164 SER n 
1 165 ILE n 
1 166 ASP n 
1 167 GLU n 
1 168 ARG n 
1 169 ASP n 
1 170 VAL n 
1 171 TYR n 
1 172 LEU n 
1 173 LEU n 
1 174 ALA n 
1 175 ALA n 
1 176 GLY n 
1 177 ARG n 
1 178 GLU n 
1 179 CYS n 
1 180 ALA n 
1 181 GLU n 
1 182 ALA n 
1 183 GLY n 
1 184 ASP n 
1 185 GLU n 
1 186 LEU n 
1 187 PHE n 
1 188 ASN n 
1 189 LEU n 
1 190 ALA n 
1 191 MET n 
1 192 LEU n 
1 193 PHE n 
1 194 SER n 
1 195 MET n 
1 196 ASP n 
1 197 ARG n 
1 198 GLY n 
1 199 LYS n 
1 200 LYS n 
1 201 SER n 
1 202 GLU n 
1 203 GLN n 
1 204 THR n 
1 205 SER n 
1 206 GLY n 
1 207 GLU n 
1 208 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   208 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Tc00.1047053506679.130 
_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      'Trypanosoma cruzi' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5693 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
K   non-polymer         . 'POTASSIUM ION' ?                               'K 1'            39.098  
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 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -3  ?   ?   ?   A . n 
A 1 2   PRO 2   -2  ?   ?   ?   A . n 
A 1 3   GLY 3   -1  ?   ?   ?   A . n 
A 1 4   SER 4   0   ?   ?   ?   A . n 
A 1 5   MET 5   1   ?   ?   ?   A . n 
A 1 6   GLU 6   2   ?   ?   ?   A . n 
A 1 7   MET 7   3   ?   ?   ?   A . n 
A 1 8   SER 8   4   ?   ?   ?   A . n 
A 1 9   ARG 9   5   ?   ?   ?   A . n 
A 1 10  SER 10  6   ?   ?   ?   A . n 
A 1 11  SER 11  7   ?   ?   ?   A . n 
A 1 12  ASP 12  8   ?   ?   ?   A . n 
A 1 13  THR 13  9   ?   ?   ?   A . n 
A 1 14  PHE 14  10  ?   ?   ?   A . n 
A 1 15  SER 15  11  ?   ?   ?   A . n 
A 1 16  ALA 16  12  ?   ?   ?   A . n 
A 1 17  SER 17  13  ?   ?   ?   A . n 
A 1 18  ARG 18  14  ?   ?   ?   A . n 
A 1 19  ASN 19  15  ?   ?   ?   A . n 
A 1 20  ARG 20  16  ?   ?   ?   A . n 
A 1 21  VAL 21  17  ?   ?   ?   A . n 
A 1 22  ARG 22  18  ?   ?   ?   A . n 
A 1 23  ALA 23  19  ?   ?   ?   A . n 
A 1 24  ASP 24  20  ?   ?   ?   A . n 
A 1 25  GLU 25  21  ?   ?   ?   A . n 
A 1 26  ILE 26  22  ?   ?   ?   A . n 
A 1 27  ASN 27  23  ?   ?   ?   A . n 
A 1 28  ASP 28  24  ?   ?   ?   A . n 
A 1 29  GLU 29  25  ?   ?   ?   A . n 
A 1 30  GLU 30  26  ?   ?   ?   A . n 
A 1 31  ASP 31  27  27  ASP ASP A . n 
A 1 32  HIS 32  28  28  HIS HIS A . n 
A 1 33  ALA 33  29  29  ALA ALA A . n 
A 1 34  ASP 34  30  30  ASP ASP A . n 
A 1 35  ALA 35  31  31  ALA ALA A . n 
A 1 36  ALA 36  32  32  ALA ALA A . n 
A 1 37  TYR 37  33  33  TYR TYR A . n 
A 1 38  VAL 38  34  34  VAL VAL A . n 
A 1 39  GLU 39  35  35  GLU GLU A . n 
A 1 40  LYS 40  36  36  LYS LYS A . n 
A 1 41  HIS 41  37  37  HIS HIS A . n 
A 1 42  ASN 42  38  38  ASN ASN A . n 
A 1 43  LEU 43  39  39  LEU LEU A . n 
A 1 44  GLN 44  40  40  GLN GLN A . n 
A 1 45  CYS 45  41  41  CYS CYS A . n 
A 1 46  LEU 46  42  42  LEU LEU A . n 
A 1 47  PHE 47  43  43  PHE PHE A . n 
A 1 48  SER 48  44  44  SER SER A . n 
A 1 49  GLU 49  45  45  GLU GLU A . n 
A 1 50  MET 50  46  46  MET MET A . n 
A 1 51  ALA 51  47  47  ALA ALA A . n 
A 1 52  GLU 52  48  48  GLU GLU A . n 
A 1 53  GLN 53  49  49  GLN GLN A . n 
A 1 54  LEU 54  50  50  LEU LEU A . n 
A 1 55  SER 55  51  51  SER SER A . n 
A 1 56  GLU 56  52  52  GLU GLU A . n 
A 1 57  LYS 57  53  53  LYS LYS A . n 
A 1 58  ASP 58  54  54  ASP ASP A . n 
A 1 59  PRO 59  55  55  PRO PRO A . n 
A 1 60  LYS 60  56  56  LYS LYS A . n 
A 1 61  THR 61  57  57  THR THR A . n 
A 1 62  GLU 62  58  58  GLU GLU A . n 
A 1 63  GLN 63  59  59  GLN GLN A . n 
A 1 64  GLU 64  60  60  GLU GLU A . n 
A 1 65  ALA 65  61  61  ALA ALA A . n 
A 1 66  GLU 66  62  62  GLU GLU A . n 
A 1 67  ARG 67  63  63  ARG ARG A . n 
A 1 68  ILE 68  64  64  ILE ILE A . n 
A 1 69  LEU 69  65  65  LEU LEU A . n 
A 1 70  LEU 70  66  66  LEU LEU A . n 
A 1 71  GLU 71  67  67  GLU GLU A . n 
A 1 72  PHE 72  68  68  PHE PHE A . n 
A 1 73  LEU 73  69  69  LEU LEU A . n 
A 1 74  THR 74  70  70  THR THR A . n 
A 1 75  HIS 75  71  71  HIS HIS A . n 
A 1 76  ARG 76  72  72  ARG ARG A . n 
A 1 77  LYS 77  73  73  LYS LYS A . n 
A 1 78  ALA 78  74  74  ALA ALA A . n 
A 1 79  GLU 79  75  75  GLU GLU A . n 
A 1 80  ARG 80  76  76  ARG ARG A . n 
A 1 81  ASP 81  77  77  ASP ASP A . n 
A 1 82  ARG 82  78  78  ARG ARG A . n 
A 1 83  ALA 83  79  79  ALA ALA A . n 
A 1 84  ALA 84  80  80  ALA ALA A . n 
A 1 85  LEU 85  81  81  LEU LEU A . n 
A 1 86  ARG 86  82  82  ARG ARG A . n 
A 1 87  LEU 87  83  83  LEU LEU A . n 
A 1 88  GLN 88  84  84  GLN GLN A . n 
A 1 89  PHE 89  85  85  PHE PHE A . n 
A 1 90  SER 90  86  86  SER SER A . n 
A 1 91  HIS 91  87  87  HIS HIS A . n 
A 1 92  SER 92  88  88  SER SER A . n 
A 1 93  PHE 93  89  89  PHE PHE A . n 
A 1 94  GLU 94  90  90  GLU GLU A . n 
A 1 95  VAL 95  91  91  VAL VAL A . n 
A 1 96  ASN 96  92  92  ASN ASN A . n 
A 1 97  LEU 97  93  93  LEU LEU A . n 
A 1 98  ASP 98  94  94  ASP ASP A . n 
A 1 99  ASN 99  95  95  ASN ASN A . n 
A 1 100 GLY 100 96  96  GLY GLY A . n 
A 1 101 ARG 101 97  97  ARG ARG A . n 
A 1 102 LYS 102 98  98  LYS LYS A . n 
A 1 103 ILE 103 99  99  ILE ILE A . n 
A 1 104 MET 104 100 100 MET MET A . n 
A 1 105 ARG 105 101 101 ARG ARG A . n 
A 1 106 LEU 106 102 102 LEU LEU A . n 
A 1 107 GLN 107 103 103 GLN GLN A . n 
A 1 108 LEU 108 104 104 LEU LEU A . n 
A 1 109 GLY 109 105 105 GLY GLY A . n 
A 1 110 GLN 110 106 106 GLN GLN A . n 
A 1 111 GLU 111 107 107 GLU GLU A . n 
A 1 112 THR 112 108 108 THR THR A . n 
A 1 113 SER 113 109 109 SER SER A . n 
A 1 114 THR 114 110 110 THR THR A . n 
A 1 115 LEU 115 111 111 LEU LEU A . n 
A 1 116 GLN 116 112 112 GLN GLN A . n 
A 1 117 LEU 117 113 113 LEU LEU A . n 
A 1 118 GLU 118 114 114 GLU GLU A . n 
A 1 119 GLN 119 115 115 GLN GLN A . n 
A 1 120 LYS 120 116 116 LYS LYS A . n 
A 1 121 GLY 121 117 117 GLY GLY A . n 
A 1 122 ARG 122 118 118 ARG ARG A . n 
A 1 123 VAL 123 119 119 VAL VAL A . n 
A 1 124 LEU 124 120 120 LEU LEU A . n 
A 1 125 LYS 125 121 121 LYS LYS A . n 
A 1 126 MET 126 122 122 MET MET A . n 
A 1 127 ASP 127 123 123 ASP ASP A . n 
A 1 128 GLU 128 124 124 GLU GLU A . n 
A 1 129 ALA 129 125 125 ALA ALA A . n 
A 1 130 PHE 130 126 126 PHE PHE A . n 
A 1 131 SER 131 127 127 SER SER A . n 
A 1 132 ILE 132 128 128 ILE ILE A . n 
A 1 133 SER 133 129 129 SER SER A . n 
A 1 134 LEU 134 130 130 LEU LEU A . n 
A 1 135 GLU 135 131 131 GLU GLU A . n 
A 1 136 GLN 136 132 132 GLN GLN A . n 
A 1 137 THR 137 133 133 THR THR A . n 
A 1 138 GLU 138 134 134 GLU GLU A . n 
A 1 139 GLU 139 135 135 GLU GLU A . n 
A 1 140 LEU 140 136 136 LEU LEU A . n 
A 1 141 THR 141 137 137 THR THR A . n 
A 1 142 GLU 142 138 138 GLU GLU A . n 
A 1 143 MET 143 139 139 MET MET A . n 
A 1 144 PHE 144 140 140 PHE PHE A . n 
A 1 145 TYR 145 141 141 TYR TYR A . n 
A 1 146 GLU 146 142 142 GLU GLU A . n 
A 1 147 LEU 147 143 143 LEU LEU A . n 
A 1 148 GLY 148 144 144 GLY GLY A . n 
A 1 149 ARG 149 145 145 ARG ARG A . n 
A 1 150 PHE 150 146 146 PHE PHE A . n 
A 1 151 VAL 151 147 147 VAL VAL A . n 
A 1 152 VAL 152 148 148 VAL VAL A . n 
A 1 153 ASP 153 149 149 ASP ASP A . n 
A 1 154 GLY 154 150 150 GLY GLY A . n 
A 1 155 THR 155 151 151 THR THR A . n 
A 1 156 LYS 156 152 152 LYS LYS A . n 
A 1 157 GLY 157 153 153 GLY GLY A . n 
A 1 158 GLU 158 154 154 GLU GLU A . n 
A 1 159 GLN 159 155 155 GLN GLN A . n 
A 1 160 GLY 160 156 156 GLY GLY A . n 
A 1 161 GLY 161 157 157 GLY GLY A . n 
A 1 162 PHE 162 158 158 PHE PHE A . n 
A 1 163 ILE 163 159 159 ILE ILE A . n 
A 1 164 SER 164 160 160 SER SER A . n 
A 1 165 ILE 165 161 161 ILE ILE A . n 
A 1 166 ASP 166 162 162 ASP ASP A . n 
A 1 167 GLU 167 163 163 GLU GLU A . n 
A 1 168 ARG 168 164 164 ARG ARG A . n 
A 1 169 ASP 169 165 165 ASP ASP A . n 
A 1 170 VAL 170 166 166 VAL VAL A . n 
A 1 171 TYR 171 167 167 TYR TYR A . n 
A 1 172 LEU 172 168 168 LEU LEU A . n 
A 1 173 LEU 173 169 169 LEU LEU A . n 
A 1 174 ALA 174 170 170 ALA ALA A . n 
A 1 175 ALA 175 171 171 ALA ALA A . n 
A 1 176 GLY 176 172 172 GLY GLY A . n 
A 1 177 ARG 177 173 173 ARG ARG A . n 
A 1 178 GLU 178 174 174 GLU GLU A . n 
A 1 179 CYS 179 175 175 CYS CYS A . n 
A 1 180 ALA 180 176 176 ALA ALA A . n 
A 1 181 GLU 181 177 177 GLU GLU A . n 
A 1 182 ALA 182 178 178 ALA ALA A . n 
A 1 183 GLY 183 179 179 GLY GLY A . n 
A 1 184 ASP 184 180 180 ASP ASP A . n 
A 1 185 GLU 185 181 181 GLU GLU A . n 
A 1 186 LEU 186 182 182 LEU LEU A . n 
A 1 187 PHE 187 183 183 PHE PHE A . n 
A 1 188 ASN 188 184 184 ASN ASN A . n 
A 1 189 LEU 189 185 185 LEU LEU A . n 
A 1 190 ALA 190 186 186 ALA ALA A . n 
A 1 191 MET 191 187 187 MET MET A . n 
A 1 192 LEU 192 188 188 LEU LEU A . n 
A 1 193 PHE 193 189 189 PHE PHE A . n 
A 1 194 SER 194 190 190 SER SER A . n 
A 1 195 MET 195 191 191 MET MET A . n 
A 1 196 ASP 196 192 192 ASP ASP A . n 
A 1 197 ARG 197 193 ?   ?   ?   A . n 
A 1 198 GLY 198 194 ?   ?   ?   A . n 
A 1 199 LYS 199 195 ?   ?   ?   A . n 
A 1 200 LYS 200 196 ?   ?   ?   A . n 
A 1 201 SER 201 197 ?   ?   ?   A . n 
A 1 202 GLU 202 198 ?   ?   ?   A . n 
A 1 203 GLN 203 199 ?   ?   ?   A . n 
A 1 204 THR 204 200 ?   ?   ?   A . n 
A 1 205 SER 205 201 ?   ?   ?   A . n 
A 1 206 GLY 206 202 ?   ?   ?   A . n 
A 1 207 GLU 207 203 ?   ?   ?   A . n 
A 1 208 ALA 208 204 ?   ?   ?   A . n 
B 1 1   GLY 1   -3  ?   ?   ?   B . n 
B 1 2   PRO 2   -2  ?   ?   ?   B . n 
B 1 3   GLY 3   -1  ?   ?   ?   B . n 
B 1 4   SER 4   0   ?   ?   ?   B . n 
B 1 5   MET 5   1   ?   ?   ?   B . n 
B 1 6   GLU 6   2   ?   ?   ?   B . n 
B 1 7   MET 7   3   ?   ?   ?   B . n 
B 1 8   SER 8   4   ?   ?   ?   B . n 
B 1 9   ARG 9   5   ?   ?   ?   B . n 
B 1 10  SER 10  6   ?   ?   ?   B . n 
B 1 11  SER 11  7   ?   ?   ?   B . n 
B 1 12  ASP 12  8   ?   ?   ?   B . n 
B 1 13  THR 13  9   ?   ?   ?   B . n 
B 1 14  PHE 14  10  ?   ?   ?   B . n 
B 1 15  SER 15  11  ?   ?   ?   B . n 
B 1 16  ALA 16  12  ?   ?   ?   B . n 
B 1 17  SER 17  13  ?   ?   ?   B . n 
B 1 18  ARG 18  14  ?   ?   ?   B . n 
B 1 19  ASN 19  15  ?   ?   ?   B . n 
B 1 20  ARG 20  16  ?   ?   ?   B . n 
B 1 21  VAL 21  17  ?   ?   ?   B . n 
B 1 22  ARG 22  18  ?   ?   ?   B . n 
B 1 23  ALA 23  19  ?   ?   ?   B . n 
B 1 24  ASP 24  20  ?   ?   ?   B . n 
B 1 25  GLU 25  21  ?   ?   ?   B . n 
B 1 26  ILE 26  22  ?   ?   ?   B . n 
B 1 27  ASN 27  23  ?   ?   ?   B . n 
B 1 28  ASP 28  24  ?   ?   ?   B . n 
B 1 29  GLU 29  25  ?   ?   ?   B . n 
B 1 30  GLU 30  26  ?   ?   ?   B . n 
B 1 31  ASP 31  27  27  ASP ASP B . n 
B 1 32  HIS 32  28  28  HIS HIS B . n 
B 1 33  ALA 33  29  29  ALA ALA B . n 
B 1 34  ASP 34  30  30  ASP ASP B . n 
B 1 35  ALA 35  31  31  ALA ALA B . n 
B 1 36  ALA 36  32  32  ALA ALA B . n 
B 1 37  TYR 37  33  33  TYR TYR B . n 
B 1 38  VAL 38  34  34  VAL VAL B . n 
B 1 39  GLU 39  35  35  GLU GLU B . n 
B 1 40  LYS 40  36  36  LYS LYS B . n 
B 1 41  HIS 41  37  37  HIS HIS B . n 
B 1 42  ASN 42  38  38  ASN ASN B . n 
B 1 43  LEU 43  39  39  LEU LEU B . n 
B 1 44  GLN 44  40  40  GLN GLN B . n 
B 1 45  CYS 45  41  41  CYS CYS B . n 
B 1 46  LEU 46  42  42  LEU LEU B . n 
B 1 47  PHE 47  43  43  PHE PHE B . n 
B 1 48  SER 48  44  44  SER SER B . n 
B 1 49  GLU 49  45  45  GLU GLU B . n 
B 1 50  MET 50  46  46  MET MET B . n 
B 1 51  ALA 51  47  47  ALA ALA B . n 
B 1 52  GLU 52  48  48  GLU GLU B . n 
B 1 53  GLN 53  49  49  GLN GLN B . n 
B 1 54  LEU 54  50  50  LEU LEU B . n 
B 1 55  SER 55  51  51  SER SER B . n 
B 1 56  GLU 56  52  52  GLU GLU B . n 
B 1 57  LYS 57  53  53  LYS LYS B . n 
B 1 58  ASP 58  54  54  ASP ASP B . n 
B 1 59  PRO 59  55  55  PRO PRO B . n 
B 1 60  LYS 60  56  56  LYS LYS B . n 
B 1 61  THR 61  57  57  THR THR B . n 
B 1 62  GLU 62  58  58  GLU GLU B . n 
B 1 63  GLN 63  59  59  GLN GLN B . n 
B 1 64  GLU 64  60  60  GLU GLU B . n 
B 1 65  ALA 65  61  61  ALA ALA B . n 
B 1 66  GLU 66  62  62  GLU GLU B . n 
B 1 67  ARG 67  63  63  ARG ARG B . n 
B 1 68  ILE 68  64  64  ILE ILE B . n 
B 1 69  LEU 69  65  65  LEU LEU B . n 
B 1 70  LEU 70  66  66  LEU LEU B . n 
B 1 71  GLU 71  67  67  GLU GLU B . n 
B 1 72  PHE 72  68  68  PHE PHE B . n 
B 1 73  LEU 73  69  69  LEU LEU B . n 
B 1 74  THR 74  70  70  THR THR B . n 
B 1 75  HIS 75  71  71  HIS HIS B . n 
B 1 76  ARG 76  72  72  ARG ARG B . n 
B 1 77  LYS 77  73  73  LYS LYS B . n 
B 1 78  ALA 78  74  74  ALA ALA B . n 
B 1 79  GLU 79  75  75  GLU GLU B . n 
B 1 80  ARG 80  76  76  ARG ARG B . n 
B 1 81  ASP 81  77  77  ASP ASP B . n 
B 1 82  ARG 82  78  78  ARG ARG B . n 
B 1 83  ALA 83  79  79  ALA ALA B . n 
B 1 84  ALA 84  80  80  ALA ALA B . n 
B 1 85  LEU 85  81  81  LEU LEU B . n 
B 1 86  ARG 86  82  82  ARG ARG B . n 
B 1 87  LEU 87  83  83  LEU LEU B . n 
B 1 88  GLN 88  84  84  GLN GLN B . n 
B 1 89  PHE 89  85  85  PHE PHE B . n 
B 1 90  SER 90  86  86  SER SER B . n 
B 1 91  HIS 91  87  87  HIS HIS B . n 
B 1 92  SER 92  88  88  SER SER B . n 
B 1 93  PHE 93  89  89  PHE PHE B . n 
B 1 94  GLU 94  90  90  GLU GLU B . n 
B 1 95  VAL 95  91  91  VAL VAL B . n 
B 1 96  ASN 96  92  92  ASN ASN B . n 
B 1 97  LEU 97  93  93  LEU LEU B . n 
B 1 98  ASP 98  94  94  ASP ASP B . n 
B 1 99  ASN 99  95  95  ASN ASN B . n 
B 1 100 GLY 100 96  96  GLY GLY B . n 
B 1 101 ARG 101 97  97  ARG ARG B . n 
B 1 102 LYS 102 98  98  LYS LYS B . n 
B 1 103 ILE 103 99  99  ILE ILE B . n 
B 1 104 MET 104 100 100 MET MET B . n 
B 1 105 ARG 105 101 101 ARG ARG B . n 
B 1 106 LEU 106 102 102 LEU LEU B . n 
B 1 107 GLN 107 103 103 GLN GLN B . n 
B 1 108 LEU 108 104 104 LEU LEU B . n 
B 1 109 GLY 109 105 105 GLY GLY B . n 
B 1 110 GLN 110 106 106 GLN GLN B . n 
B 1 111 GLU 111 107 107 GLU GLU B . n 
B 1 112 THR 112 108 108 THR THR B . n 
B 1 113 SER 113 109 109 SER SER B . n 
B 1 114 THR 114 110 110 THR THR B . n 
B 1 115 LEU 115 111 111 LEU LEU B . n 
B 1 116 GLN 116 112 112 GLN GLN B . n 
B 1 117 LEU 117 113 113 LEU LEU B . n 
B 1 118 GLU 118 114 114 GLU GLU B . n 
B 1 119 GLN 119 115 115 GLN GLN B . n 
B 1 120 LYS 120 116 116 LYS LYS B . n 
B 1 121 GLY 121 117 117 GLY GLY B . n 
B 1 122 ARG 122 118 118 ARG ARG B . n 
B 1 123 VAL 123 119 119 VAL VAL B . n 
B 1 124 LEU 124 120 120 LEU LEU B . n 
B 1 125 LYS 125 121 121 LYS LYS B . n 
B 1 126 MET 126 122 122 MET MET B . n 
B 1 127 ASP 127 123 123 ASP ASP B . n 
B 1 128 GLU 128 124 124 GLU GLU B . n 
B 1 129 ALA 129 125 125 ALA ALA B . n 
B 1 130 PHE 130 126 126 PHE PHE B . n 
B 1 131 SER 131 127 127 SER SER B . n 
B 1 132 ILE 132 128 128 ILE ILE B . n 
B 1 133 SER 133 129 129 SER SER B . n 
B 1 134 LEU 134 130 130 LEU LEU B . n 
B 1 135 GLU 135 131 131 GLU GLU B . n 
B 1 136 GLN 136 132 132 GLN GLN B . n 
B 1 137 THR 137 133 133 THR THR B . n 
B 1 138 GLU 138 134 134 GLU GLU B . n 
B 1 139 GLU 139 135 135 GLU GLU B . n 
B 1 140 LEU 140 136 136 LEU LEU B . n 
B 1 141 THR 141 137 137 THR THR B . n 
B 1 142 GLU 142 138 138 GLU GLU B . n 
B 1 143 MET 143 139 139 MET MET B . n 
B 1 144 PHE 144 140 140 PHE PHE B . n 
B 1 145 TYR 145 141 141 TYR TYR B . n 
B 1 146 GLU 146 142 142 GLU GLU B . n 
B 1 147 LEU 147 143 143 LEU LEU B . n 
B 1 148 GLY 148 144 144 GLY GLY B . n 
B 1 149 ARG 149 145 145 ARG ARG B . n 
B 1 150 PHE 150 146 146 PHE PHE B . n 
B 1 151 VAL 151 147 147 VAL VAL B . n 
B 1 152 VAL 152 148 148 VAL VAL B . n 
B 1 153 ASP 153 149 149 ASP ASP B . n 
B 1 154 GLY 154 150 150 GLY GLY B . n 
B 1 155 THR 155 151 151 THR THR B . n 
B 1 156 LYS 156 152 152 LYS LYS B . n 
B 1 157 GLY 157 153 153 GLY GLY B . n 
B 1 158 GLU 158 154 154 GLU GLU B . n 
B 1 159 GLN 159 155 155 GLN GLN B . n 
B 1 160 GLY 160 156 156 GLY GLY B . n 
B 1 161 GLY 161 157 157 GLY GLY B . n 
B 1 162 PHE 162 158 158 PHE PHE B . n 
B 1 163 ILE 163 159 159 ILE ILE B . n 
B 1 164 SER 164 160 160 SER SER B . n 
B 1 165 ILE 165 161 161 ILE ILE B . n 
B 1 166 ASP 166 162 162 ASP ASP B . n 
B 1 167 GLU 167 163 163 GLU GLU B . n 
B 1 168 ARG 168 164 164 ARG ARG B . n 
B 1 169 ASP 169 165 165 ASP ASP B . n 
B 1 170 VAL 170 166 166 VAL VAL B . n 
B 1 171 TYR 171 167 167 TYR TYR B . n 
B 1 172 LEU 172 168 168 LEU LEU B . n 
B 1 173 LEU 173 169 169 LEU LEU B . n 
B 1 174 ALA 174 170 170 ALA ALA B . n 
B 1 175 ALA 175 171 171 ALA ALA B . n 
B 1 176 GLY 176 172 172 GLY GLY B . n 
B 1 177 ARG 177 173 173 ARG ARG B . n 
B 1 178 GLU 178 174 174 GLU GLU B . n 
B 1 179 CYS 179 175 175 CYS CYS B . n 
B 1 180 ALA 180 176 176 ALA ALA B . n 
B 1 181 GLU 181 177 177 GLU GLU B . n 
B 1 182 ALA 182 178 178 ALA ALA B . n 
B 1 183 GLY 183 179 179 GLY GLY B . n 
B 1 184 ASP 184 180 180 ASP ASP B . n 
B 1 185 GLU 185 181 181 GLU GLU B . n 
B 1 186 LEU 186 182 182 LEU LEU B . n 
B 1 187 PHE 187 183 183 PHE PHE B . n 
B 1 188 ASN 188 184 184 ASN ASN B . n 
B 1 189 LEU 189 185 185 LEU LEU B . n 
B 1 190 ALA 190 186 186 ALA ALA B . n 
B 1 191 MET 191 187 187 MET MET B . n 
B 1 192 LEU 192 188 188 LEU LEU B . n 
B 1 193 PHE 193 189 189 PHE PHE B . n 
B 1 194 SER 194 190 190 SER SER B . n 
B 1 195 MET 195 191 191 MET MET B . n 
B 1 196 ASP 196 192 192 ASP ASP B . n 
B 1 197 ARG 197 193 ?   ?   ?   B . n 
B 1 198 GLY 198 194 ?   ?   ?   B . n 
B 1 199 LYS 199 195 ?   ?   ?   B . n 
B 1 200 LYS 200 196 ?   ?   ?   B . n 
B 1 201 SER 201 197 ?   ?   ?   B . n 
B 1 202 GLU 202 198 ?   ?   ?   B . n 
B 1 203 GLN 203 199 ?   ?   ?   B . n 
B 1 204 THR 204 200 ?   ?   ?   B . n 
B 1 205 SER 205 201 ?   ?   ?   B . n 
B 1 206 GLY 206 202 ?   ?   ?   B . n 
B 1 207 GLU 207 203 ?   ?   ?   B . n 
B 1 208 ALA 208 204 ?   ?   ?   B . n 
# 
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 K   1  301 1  K   K   A . 
D 3 GOL 1  302 3  GOL GOL A . 
E 2 K   1  301 2  K   K   B . 
F 3 GOL 1  302 4  GOL GOL B . 
G 4 HOH 1  401 50 HOH HOH A . 
G 4 HOH 2  402 76 HOH HOH A . 
G 4 HOH 3  403 27 HOH HOH A . 
G 4 HOH 4  404 72 HOH HOH A . 
G 4 HOH 5  405 3  HOH HOH A . 
G 4 HOH 6  406 58 HOH HOH A . 
G 4 HOH 7  407 43 HOH HOH A . 
G 4 HOH 8  408 5  HOH HOH A . 
G 4 HOH 9  409 28 HOH HOH A . 
G 4 HOH 10 410 20 HOH HOH A . 
G 4 HOH 11 411 31 HOH HOH A . 
G 4 HOH 12 412 10 HOH HOH A . 
G 4 HOH 13 413 37 HOH HOH A . 
G 4 HOH 14 414 42 HOH HOH A . 
G 4 HOH 15 415 34 HOH HOH A . 
G 4 HOH 16 416 8  HOH HOH A . 
G 4 HOH 17 417 70 HOH HOH A . 
G 4 HOH 18 418 45 HOH HOH A . 
G 4 HOH 19 419 36 HOH HOH A . 
G 4 HOH 20 420 48 HOH HOH A . 
G 4 HOH 21 421 63 HOH HOH A . 
G 4 HOH 22 422 1  HOH HOH A . 
G 4 HOH 23 423 18 HOH HOH A . 
G 4 HOH 24 424 33 HOH HOH A . 
G 4 HOH 25 425 23 HOH HOH A . 
G 4 HOH 26 426 71 HOH HOH A . 
G 4 HOH 27 427 56 HOH HOH A . 
G 4 HOH 28 428 13 HOH HOH A . 
G 4 HOH 29 429 24 HOH HOH A . 
G 4 HOH 30 430 14 HOH HOH A . 
G 4 HOH 31 431 26 HOH HOH A . 
G 4 HOH 32 432 40 HOH HOH A . 
G 4 HOH 33 433 53 HOH HOH A . 
G 4 HOH 34 434 35 HOH HOH A . 
G 4 HOH 35 435 68 HOH HOH A . 
G 4 HOH 36 436 66 HOH HOH A . 
G 4 HOH 37 437 59 HOH HOH A . 
G 4 HOH 38 438 60 HOH HOH A . 
G 4 HOH 39 439 73 HOH HOH A . 
H 4 HOH 1  401 64 HOH HOH B . 
H 4 HOH 2  402 29 HOH HOH B . 
H 4 HOH 3  403 77 HOH HOH B . 
H 4 HOH 4  404 19 HOH HOH B . 
H 4 HOH 5  405 6  HOH HOH B . 
H 4 HOH 6  406 54 HOH HOH B . 
H 4 HOH 7  407 62 HOH HOH B . 
H 4 HOH 8  408 57 HOH HOH B . 
H 4 HOH 9  409 44 HOH HOH B . 
H 4 HOH 10 410 21 HOH HOH B . 
H 4 HOH 11 411 22 HOH HOH B . 
H 4 HOH 12 412 17 HOH HOH B . 
H 4 HOH 13 413 2  HOH HOH B . 
H 4 HOH 14 414 69 HOH HOH B . 
H 4 HOH 15 415 39 HOH HOH B . 
H 4 HOH 16 416 30 HOH HOH B . 
H 4 HOH 17 417 78 HOH HOH B . 
H 4 HOH 18 418 38 HOH HOH B . 
H 4 HOH 19 419 11 HOH HOH B . 
H 4 HOH 20 420 52 HOH HOH B . 
H 4 HOH 21 421 47 HOH HOH B . 
H 4 HOH 22 422 7  HOH HOH B . 
H 4 HOH 23 423 16 HOH HOH B . 
H 4 HOH 24 424 9  HOH HOH B . 
H 4 HOH 25 425 55 HOH HOH B . 
H 4 HOH 26 426 25 HOH HOH B . 
H 4 HOH 27 427 12 HOH HOH B . 
H 4 HOH 28 428 75 HOH HOH B . 
H 4 HOH 29 429 32 HOH HOH B . 
H 4 HOH 30 430 15 HOH HOH B . 
H 4 HOH 31 431 4  HOH HOH B . 
H 4 HOH 32 432 46 HOH HOH B . 
H 4 HOH 33 433 49 HOH HOH B . 
H 4 HOH 34 434 41 HOH HOH B . 
H 4 HOH 35 435 67 HOH HOH B . 
H 4 HOH 36 436 51 HOH HOH B . 
H 4 HOH 37 437 61 HOH HOH B . 
H 4 HOH 38 438 65 HOH HOH B . 
H 4 HOH 39 439 74 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A ASP 27 ? CG  ? A ASP 31 CG  
2 1 Y 1 A ASP 27 ? OD1 ? A ASP 31 OD1 
3 1 Y 1 A ASP 27 ? OD2 ? A ASP 31 OD2 
4 1 Y 1 B ASP 27 ? CG  ? B ASP 31 CG  
5 1 Y 1 B ASP 27 ? OD1 ? B ASP 31 OD1 
6 1 Y 1 B ASP 27 ? OD2 ? B ASP 31 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DENZO   ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.616 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     110.225 
_cell.length_a_esd                 ? 
_cell.length_b                     71.647 
_cell.length_b_esd                 ? 
_cell.length_c                     67.084 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9EIE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EIE 
_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             2.84 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          57. 
_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              8.0 
_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    '0.1 M K2HPO4, 0.1 M Tris pH 8, 30% PEG 20000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295. 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 210' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2004-12-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 5.0.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EIE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               45.714 
_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                                     17796 
_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                           88.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.93 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.118 
_reflns.pdbx_Rpim_I_all                                0.062 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.099 
_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                                    2.42 
_reflns_shell.d_res_low                                     2.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           1471 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             851 
_reflns_shell.percent_possible_obs                          40.3 
_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                               1.7 
_reflns_shell.pdbx_chi_squared                              0.83 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.3 
_reflns_shell.pdbx_Rrim_I_all                               0.629 
_reflns_shell.pdbx_Rpim_I_all                               0.398 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.702 
_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                                  0.482 
_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]                            -0.340 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.368 
_refine.aniso_B[2][2]                            0.188 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            0.209 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               43.325 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.945 
_refine.correlation_coeff_Fo_to_Fc_free          0.911 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 9EIE 
_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                            2.450 
_refine.ls_d_res_low                             45.714 
_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                     17576 
_refine.ls_number_reflns_R_free                  908 
_refine.ls_number_reflns_R_work                  16668 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.115 
_refine.ls_percent_reflns_R_free                 5.166 
_refine.ls_R_factor_all                          0.204 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2310 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2025 
_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                    'MASK BULK SOLVENT' 
_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                          ? 
_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                      'AlphaFold3-generated model, from run in Oct 2024' 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.368 
_refine.pdbx_overall_ESU_R_Free                  0.242 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                             18.467 
_refine.overall_SU_ML                            0.197 
_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.pdbx_number_atoms_protein        2662 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.number_atoms_solvent             78 
_refine_hist.number_atoms_total               2754 
_refine_hist.d_res_high                       2.450 
_refine_hist.d_res_low                        45.714 
# 
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' ? 0.016  0.013  2729 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.018  0.017  2518 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 2.150  1.641  3655 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.551  1.579  5847 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.929  5.000  336  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 35.856 22.841 176  ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 19.945 15.000 523  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 26.192 15.000 23   ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.092  0.200  339  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  3091 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.020  0.020  586  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.241  0.200  569  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.202  0.200  2189 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.168  0.200  1243 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.089  0.200  1370 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.198  0.200  66   ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.174  0.200  2    ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.220  0.200  25   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.199  0.200  70   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.149  0.200  9    ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 2.790  3.522  1332 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.786  3.519  1331 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.579  5.266  1663 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.578  5.269  1664 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 3.175  3.968  1397 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.174  3.970  1398 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.379  5.795  1989 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.377  5.797  1990 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 8.004  39.514 2916 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 8.000  39.485 2911 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.082  0.050  5009 ? r_ncsr_local_group_1           ? ? 
# 
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' 2.450  2.514  . . 28 644  47.4912  . . . . 0.321 . . . . . . . . . . . 0.277 
'X-RAY DIFFRACTION' 2.514  2.582  . . 51 790  62.1582  . . . . 0.330 . . . . . . . . . . . 0.316 
'X-RAY DIFFRACTION' 2.582  2.657  . . 66 987  77.5976  . . . . 0.298 . . . . . . . . . . . 0.270 
'X-RAY DIFFRACTION' 2.657  2.739  . . 59 1152 92.5134  . . . . 0.279 . . . . . . . . . . . 0.216 
'X-RAY DIFFRACTION' 2.739  2.828  . . 55 1182 98.8019  . . . . 0.249 . . . . . . . . . . . 0.319 
'X-RAY DIFFRACTION' 2.828  2.927  . . 67 1158 99.4318  . . . . 0.246 . . . . . . . . . . . 0.260 
'X-RAY DIFFRACTION' 2.927  3.038  . . 44 1141 99.7475  . . . . 0.218 . . . . . . . . . . . 0.297 
'X-RAY DIFFRACTION' 3.038  3.162  . . 52 1082 99.9119  . . . . 0.210 . . . . . . . . . . . 0.266 
'X-RAY DIFFRACTION' 3.162  3.302  . . 69 1007 99.9072  . . . . 0.206 . . . . . . . . . . . 0.218 
'X-RAY DIFFRACTION' 3.302  3.462  . . 54 1020 99.7215  . . . . 0.216 . . . . . . . . . . . 0.250 
'X-RAY DIFFRACTION' 3.462  3.649  . . 44 930  99.7951  . . . . 0.213 . . . . . . . . . . . 0.293 
'X-RAY DIFFRACTION' 3.649  3.870  . . 42 889  99.4658  . . . . 0.193 . . . . . . . . . . . 0.238 
'X-RAY DIFFRACTION' 3.870  4.136  . . 51 841  99.7763  . . . . 0.171 . . . . . . . . . . . 0.163 
'X-RAY DIFFRACTION' 4.136  4.466  . . 55 778  99.7605  . . . . 0.149 . . . . . . . . . . . 0.201 
'X-RAY DIFFRACTION' 4.466  4.890  . . 35 706  99.5968  . . . . 0.123 . . . . . . . . . . . 0.165 
'X-RAY DIFFRACTION' 4.890  5.464  . . 42 673  100.0000 . . . . 0.169 . . . . . . . . . . . 0.197 
'X-RAY DIFFRACTION' 5.464  6.302  . . 42 558  99.8336  . . . . 0.228 . . . . . . . . . . . 0.316 
'X-RAY DIFFRACTION' 6.302  7.701  . . 19 506  100.0000 . . . . 0.186 . . . . . . . . . . . 0.158 
'X-RAY DIFFRACTION' 7.701  10.820 . . 20 394  99.5192  . . . . 0.136 . . . . . . . . . . . 0.139 
'X-RAY DIFFRACTION' 10.820 45.714 . . 12 226  97.5410  . . . . 0.266 . . . . . . . . . . . 0.325 
# 
_struct.entry_id                     9EIE 
_struct.title                        'Trypanosomatid-specific protein of unknown function' 
_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        9EIE 
_struct_keywords.text            
;Trypanosome structure prediction SGPP, Structural Genomics, PSI-2, Protein Structure Initiative, Structural Genomics of Pathogenic Protozoa Consortium, UNKNOWN FUNCTION
;
_struct_keywords.pdbx_keywords   'UNKNOWN FUNCTION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q4E090_TRYCC 
_struct_ref.pdbx_db_accession          Q4E090 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEMSRSSDTFSASRNRVRADEINDEEDHADAAYVEKHNLQCLFSEMAEQLSEKDPKTEQEAERILLEFLTHRKAERDRAA
LRLQFSHSFEVNLDNGRKIMRLQLGQETSTLQLEQKGRVLKMDEAFSISLEQTEELTEMFYELGRFVVDGTKGEQGGFIS
IDERDVYLLAAGRECAEAGDELFNLAMLFSMDRGKKSEQTSGEA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EIE A 5 ? 208 ? Q4E090 1 ? 204 ? 1 204 
2 1 9EIE B 5 ? 208 ? Q4E090 1 ? 204 ? 1 204 
# 
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 9EIE GLY A 1 ? UNP Q4E090 ? ? 'expression tag' -3 1 
1 9EIE PRO A 2 ? UNP Q4E090 ? ? 'expression tag' -2 2 
1 9EIE GLY A 3 ? UNP Q4E090 ? ? 'expression tag' -1 3 
1 9EIE SER A 4 ? UNP Q4E090 ? ? 'expression tag' 0  4 
2 9EIE GLY B 1 ? UNP Q4E090 ? ? 'expression tag' -3 5 
2 9EIE PRO B 2 ? UNP Q4E090 ? ? 'expression tag' -2 6 
2 9EIE GLY B 3 ? UNP Q4E090 ? ? 'expression tag' -1 7 
2 9EIE SER B 4 ? UNP Q4E090 ? ? 'expression tag' 0  8 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                
'dimer interface is mediated by two K+ ions from the crystallization buffer' 
# 
_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 ALA A 33  ? LYS A 40  ? ALA A 29  LYS A 36  1 ? 8  
HELX_P HELX_P2  AA2 LEU A 43  ? ASP A 58  ? LEU A 39  ASP A 54  1 ? 16 
HELX_P HELX_P3  AA3 THR A 61  ? LEU A 87  ? THR A 57  LEU A 83  1 ? 27 
HELX_P HELX_P4  AA4 SER A 133 ? ARG A 149 ? SER A 129 ARG A 145 1 ? 17 
HELX_P HELX_P5  AA5 GLY A 176 ? MET A 195 ? GLY A 172 MET A 191 1 ? 20 
HELX_P HELX_P6  AA6 ALA B 33  ? LYS B 40  ? ALA B 29  LYS B 36  1 ? 8  
HELX_P HELX_P7  AA7 LEU B 43  ? ASP B 58  ? LEU B 39  ASP B 54  1 ? 16 
HELX_P HELX_P8  AA8 THR B 61  ? LEU B 87  ? THR B 57  LEU B 83  1 ? 27 
HELX_P HELX_P9  AA9 LEU B 134 ? ARG B 149 ? LEU B 130 ARG B 145 1 ? 16 
HELX_P HELX_P10 AB1 GLY B 176 ? MET B 195 ? GLY B 172 MET B 191 1 ? 20 
# 
_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 SER 92  OG  ? ? ? 1_555 C K   .   K   ? ? A SER 88  A K   301 1_555 ? ? ? ? ? ? ? 2.913 ? ? 
metalc2 metalc ? ? A THR 155 OG1 ? ? ? 1_555 E K   .   K   ? ? A THR 151 B K   301 1_555 ? ? ? ? ? ? ? 3.321 ? ? 
metalc3 metalc ? ? A SER 164 OG  ? ? ? 1_555 C K   .   K   ? ? A SER 160 A K   301 1_555 ? ? ? ? ? ? ? 2.609 ? ? 
metalc4 metalc ? ? C K   .   K   ? ? ? 1_555 B THR 155 OG1 ? ? A K   301 B THR 151 1_555 ? ? ? ? ? ? ? 3.295 ? ? 
metalc5 metalc ? ? B SER 92  OG  ? ? ? 1_555 E K   .   K   ? ? B SER 88  B K   301 1_555 ? ? ? ? ? ? ? 2.820 ? ? 
metalc6 metalc ? ? B SER 164 OG  ? ? ? 1_555 E K   .   K   ? ? B SER 160 B K   301 1_555 ? ? ? ? ? ? ? 2.623 ? ? 
# 
_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 OG  ? A SER 92  ? A SER 88  ? 1_555 K ? C K . ? A K 301 ? 1_555 OG  ? A SER 164 ? A SER 160 ? 1_555 148.6 ? 
2 OG  ? A SER 92  ? A SER 88  ? 1_555 K ? C K . ? A K 301 ? 1_555 OG1 ? B THR 155 ? B THR 151 ? 1_555 101.0 ? 
3 OG  ? A SER 164 ? A SER 160 ? 1_555 K ? C K . ? A K 301 ? 1_555 OG1 ? B THR 155 ? B THR 151 ? 1_555 96.7  ? 
4 OG1 ? A THR 155 ? A THR 151 ? 1_555 K ? E K . ? B K 301 ? 1_555 OG  ? B SER 92  ? B SER 88  ? 1_555 103.1 ? 
5 OG1 ? A THR 155 ? A THR 151 ? 1_555 K ? E K . ? B K 301 ? 1_555 OG  ? B SER 164 ? B SER 160 ? 1_555 95.8  ? 
6 OG  ? B SER 92  ? B SER 88  ? 1_555 K ? E K . ? B K 301 ? 1_555 OG  ? B SER 164 ? B SER 160 ? 1_555 147.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
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 LYS A 125 ? ILE A 132 ? LYS A 121 ILE A 128 
AA1 2 SER A 113 ? LYS A 120 ? SER A 109 LYS A 116 
AA1 3 LYS A 102 ? LEU A 108 ? LYS A 98  LEU A 104 
AA1 4 SER A 92  ? LEU A 97  ? SER A 88  LEU A 93  
AA1 5 GLN A 159 ? ILE A 165 ? GLN A 155 ILE A 161 
AA1 6 ASP A 169 ? ALA A 174 ? ASP A 165 ALA A 170 
AA2 1 LYS B 125 ? SER B 133 ? LYS B 121 SER B 129 
AA2 2 THR B 112 ? LYS B 120 ? THR B 108 LYS B 116 
AA2 3 LYS B 102 ? LEU B 108 ? LYS B 98  LEU B 104 
AA2 4 SER B 92  ? LEU B 97  ? SER B 88  LEU B 93  
AA2 5 GLN B 159 ? ILE B 165 ? GLN B 155 ILE B 161 
AA2 6 ASP B 169 ? ALA B 174 ? ASP B 165 ALA B 170 
AA2 7 VAL B 151 ? VAL B 152 ? VAL B 147 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 128 ? O GLU A 124 N LEU A 117 ? N LEU A 113 
AA1 2 3 O GLU A 118 ? O GLU A 114 N ILE A 103 ? N ILE A 99  
AA1 3 4 O LYS A 102 ? O LYS A 98  N LEU A 97  ? N LEU A 93  
AA1 4 5 N ASN A 96  ? N ASN A 92  O PHE A 162 ? O PHE A 158 
AA1 5 6 N GLY A 161 ? N GLY A 157 O LEU A 173 ? O LEU A 169 
AA2 1 2 O GLU B 128 ? O GLU B 124 N LEU B 117 ? N LEU B 113 
AA2 2 3 O GLU B 118 ? O GLU B 114 N ILE B 103 ? N ILE B 99  
AA2 3 4 O LYS B 102 ? O LYS B 98  N LEU B 97  ? N LEU B 93  
AA2 4 5 N ASN B 96  ? N ASN B 92  O PHE B 162 ? O PHE B 158 
AA2 5 6 N GLY B 161 ? N GLY B 157 O LEU B 173 ? O LEU B 169 
AA2 6 7 O LEU B 172 ? O LEU B 168 N VAL B 152 ? N VAL B 148 
# 
_pdbx_entry_details.entry_id                   9EIE 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A ASN 95 ? ? O B ASN 95  ? ? 1.94 
2 1 OE1 A GLU 58 ? A O A HOH 401 ? ? 2.19 
3 1 OD2 B ASP 94 ? ? O B HOH 401 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 N  A ASP 27  ? ? CA  A ASP 27  ? ? 1.732 1.459 0.273  0.020 N 
2 1 CD B GLU 124 ? ? OE2 B GLU 124 ? ? 1.185 1.252 -0.067 0.011 N 
3 1 CD B ARG 173 ? ? NE  B ARG 173 ? ? 1.629 1.460 0.169  0.017 N 
4 1 NE B ARG 173 ? ? CZ  B ARG 173 ? ? 1.216 1.326 -0.110 0.013 N 
5 1 CZ B ARG 173 ? ? NH2 B ARG 173 ? ? 1.193 1.326 -0.133 0.013 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 27  ? ? CA A ASP 27  ? ? C   A ASP 27  ? ? 139.63 110.40 29.23  2.00 N 
2 1 NE A ARG 72  ? ? CZ A ARG 72  ? ? NH2 A ARG 72  ? ? 116.61 120.30 -3.69  0.50 N 
3 1 NE A ARG 145 ? ? CZ A ARG 145 ? ? NH2 A ARG 145 ? ? 116.41 120.30 -3.89  0.50 N 
4 1 NE B ARG 72  ? ? CZ B ARG 72  ? ? NH1 B ARG 72  ? ? 123.41 120.30 3.11   0.50 N 
5 1 NE B ARG 76  ? ? CZ B ARG 76  ? ? NH1 B ARG 76  ? ? 123.91 120.30 3.61   0.50 N 
6 1 NE B ARG 76  ? ? CZ B ARG 76  ? ? NH2 B ARG 76  ? ? 114.88 120.30 -5.42  0.50 N 
7 1 NE B ARG 173 ? ? CZ B ARG 173 ? ? NH1 B ARG 173 ? ? 126.72 120.30 6.42   0.50 N 
8 1 NE B ARG 173 ? ? CZ B ARG 173 ? ? NH2 B ARG 173 ? ? 108.42 120.30 -11.88 0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LYS A 36  ? ? -56.44  -9.89  
2  1 ASP A 54  ? ? 51.08   74.61  
3  1 HIS A 87  ? ? -136.30 -49.47 
4  1 ASN A 95  ? ? 16.61   101.64 
5  1 GLU A 163 ? ? 56.50   18.75  
6  1 MET A 191 ? ? -83.07  48.87  
7  1 ASP B 54  ? ? 49.21   74.63  
8  1 HIS B 87  ? ? -135.90 -52.87 
9  1 ASN B 95  ? ? 15.35   103.33 
10 1 MET B 191 ? ? -82.72  44.87  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    150 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   THR 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    151 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            145.21 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    B 
_pdbx_validate_planes.auth_seq_id     173 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.115 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             LEU 
_pdbx_validate_main_chain_plane.auth_asym_id             B 
_pdbx_validate_main_chain_plane.auth_seq_id              93 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -10.02 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'PSI, Protein Structure Initiative' 
_pdbx_SG_project.full_name_of_center   'Structural Genomics of Pathogenic Protozoa Consortium' 
_pdbx_SG_project.initial_of_center     SGPP 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     418 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 37.3761 7.2325  17.9321 0.0681 ? -0.0204 ? 0.0083  ? 0.1846 ? -0.0161 ? 0.0040 ? 0.1660 ? -0.0255 
? -0.4157 ? 0.3484 ? -0.2413 ? 1.3678 ? 0.0092 ? 0.0833  ? 0.0049 ? 0.0085 ? 0.0005  ? -0.0178 ? -0.0589 ? -0.1330 ? -0.0097 ? 
2 'X-RAY DIFFRACTION' ? refined 34.6654 16.9810 50.8147 0.0798 ? 0.0135  ? -0.0069 ? 0.1826 ? -0.0240 ? 0.0063 ? 0.0283 ? 0.0129  
? 0.1489  ? 0.3372 ? -0.1558 ? 1.4548 ? 0.0057 ? -0.0564 ? 0.0077 ? 0.0186 ? -0.0292 ? -0.0210 ? 0.1090  ? -0.1231 ? 0.0235  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? AAA 1 ? ? ? AAA 204 ? ALL ? 
2 'X-RAY DIFFRACTION' 2 ? ? BBB 1 ? ? ? BBB 204 ? ALL ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -3  ? A GLY 1   
2  1 Y 1 A PRO -2  ? A PRO 2   
3  1 Y 1 A GLY -1  ? A GLY 3   
4  1 Y 1 A SER 0   ? A SER 4   
5  1 Y 1 A MET 1   ? A MET 5   
6  1 Y 1 A GLU 2   ? A GLU 6   
7  1 Y 1 A MET 3   ? A MET 7   
8  1 Y 1 A SER 4   ? A SER 8   
9  1 Y 1 A ARG 5   ? A ARG 9   
10 1 Y 1 A SER 6   ? A SER 10  
11 1 Y 1 A SER 7   ? A SER 11  
12 1 Y 1 A ASP 8   ? A ASP 12  
13 1 Y 1 A THR 9   ? A THR 13  
14 1 Y 1 A PHE 10  ? A PHE 14  
15 1 Y 1 A SER 11  ? A SER 15  
16 1 Y 1 A ALA 12  ? A ALA 16  
17 1 Y 1 A SER 13  ? A SER 17  
18 1 Y 1 A ARG 14  ? A ARG 18  
19 1 Y 1 A ASN 15  ? A ASN 19  
20 1 Y 1 A ARG 16  ? A ARG 20  
21 1 Y 1 A VAL 17  ? A VAL 21  
22 1 Y 1 A ARG 18  ? A ARG 22  
23 1 Y 1 A ALA 19  ? A ALA 23  
24 1 Y 1 A ASP 20  ? A ASP 24  
25 1 Y 1 A GLU 21  ? A GLU 25  
26 1 Y 1 A ILE 22  ? A ILE 26  
27 1 Y 1 A ASN 23  ? A ASN 27  
28 1 Y 1 A ASP 24  ? A ASP 28  
29 1 Y 1 A GLU 25  ? A GLU 29  
30 1 Y 1 A GLU 26  ? A GLU 30  
31 1 Y 1 A ARG 193 ? A ARG 197 
32 1 Y 1 A GLY 194 ? A GLY 198 
33 1 Y 1 A LYS 195 ? A LYS 199 
34 1 Y 1 A LYS 196 ? A LYS 200 
35 1 Y 1 A SER 197 ? A SER 201 
36 1 Y 1 A GLU 198 ? A GLU 202 
37 1 Y 1 A GLN 199 ? A GLN 203 
38 1 Y 1 A THR 200 ? A THR 204 
39 1 Y 1 A SER 201 ? A SER 205 
40 1 Y 1 A GLY 202 ? A GLY 206 
41 1 Y 1 A GLU 203 ? A GLU 207 
42 1 Y 1 A ALA 204 ? A ALA 208 
43 1 Y 1 B GLY -3  ? B GLY 1   
44 1 Y 1 B PRO -2  ? B PRO 2   
45 1 Y 1 B GLY -1  ? B GLY 3   
46 1 Y 1 B SER 0   ? B SER 4   
47 1 Y 1 B MET 1   ? B MET 5   
48 1 Y 1 B GLU 2   ? B GLU 6   
49 1 Y 1 B MET 3   ? B MET 7   
50 1 Y 1 B SER 4   ? B SER 8   
51 1 Y 1 B ARG 5   ? B ARG 9   
52 1 Y 1 B SER 6   ? B SER 10  
53 1 Y 1 B SER 7   ? B SER 11  
54 1 Y 1 B ASP 8   ? B ASP 12  
55 1 Y 1 B THR 9   ? B THR 13  
56 1 Y 1 B PHE 10  ? B PHE 14  
57 1 Y 1 B SER 11  ? B SER 15  
58 1 Y 1 B ALA 12  ? B ALA 16  
59 1 Y 1 B SER 13  ? B SER 17  
60 1 Y 1 B ARG 14  ? B ARG 18  
61 1 Y 1 B ASN 15  ? B ASN 19  
62 1 Y 1 B ARG 16  ? B ARG 20  
63 1 Y 1 B VAL 17  ? B VAL 21  
64 1 Y 1 B ARG 18  ? B ARG 22  
65 1 Y 1 B ALA 19  ? B ALA 23  
66 1 Y 1 B ASP 20  ? B ASP 24  
67 1 Y 1 B GLU 21  ? B GLU 25  
68 1 Y 1 B ILE 22  ? B ILE 26  
69 1 Y 1 B ASN 23  ? B ASN 27  
70 1 Y 1 B ASP 24  ? B ASP 28  
71 1 Y 1 B GLU 25  ? B GLU 29  
72 1 Y 1 B GLU 26  ? B GLU 30  
73 1 Y 1 B ARG 193 ? B ARG 197 
74 1 Y 1 B GLY 194 ? B GLY 198 
75 1 Y 1 B LYS 195 ? B LYS 199 
76 1 Y 1 B LYS 196 ? B LYS 200 
77 1 Y 1 B SER 197 ? B SER 201 
78 1 Y 1 B GLU 198 ? B GLU 202 
79 1 Y 1 B GLN 199 ? B GLN 203 
80 1 Y 1 B THR 200 ? B THR 204 
81 1 Y 1 B SER 201 ? B SER 205 
82 1 Y 1 B GLY 202 ? B GLY 206 
83 1 Y 1 B GLU 203 ? B GLU 207 
84 1 Y 1 B ALA 204 ? B ALA 208 
# 
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 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
K   K    K N N 197 
LEU N    N N N 198 
LEU CA   C N S 199 
LEU C    C N N 200 
LEU O    O N N 201 
LEU CB   C N N 202 
LEU CG   C N N 203 
LEU CD1  C N N 204 
LEU CD2  C N N 205 
LEU OXT  O N N 206 
LEU H    H N N 207 
LEU H2   H N N 208 
LEU HA   H N N 209 
LEU HB2  H N N 210 
LEU HB3  H N N 211 
LEU HG   H N N 212 
LEU HD11 H N N 213 
LEU HD12 H N N 214 
LEU HD13 H N N 215 
LEU HD21 H N N 216 
LEU HD22 H N N 217 
LEU HD23 H N N 218 
LEU HXT  H N N 219 
LYS N    N N N 220 
LYS CA   C N S 221 
LYS C    C N N 222 
LYS O    O N N 223 
LYS CB   C N N 224 
LYS CG   C N N 225 
LYS CD   C N N 226 
LYS CE   C N N 227 
LYS NZ   N N N 228 
LYS OXT  O N N 229 
LYS H    H N N 230 
LYS H2   H N N 231 
LYS HA   H N N 232 
LYS HB2  H N N 233 
LYS HB3  H N N 234 
LYS HG2  H N N 235 
LYS HG3  H N N 236 
LYS HD2  H N N 237 
LYS HD3  H N N 238 
LYS HE2  H N N 239 
LYS HE3  H N N 240 
LYS HZ1  H N N 241 
LYS HZ2  H N N 242 
LYS HZ3  H N N 243 
LYS HXT  H N N 244 
MET N    N N N 245 
MET CA   C N S 246 
MET C    C N N 247 
MET O    O N N 248 
MET CB   C N N 249 
MET CG   C N N 250 
MET SD   S N N 251 
MET CE   C N N 252 
MET OXT  O N N 253 
MET H    H N N 254 
MET H2   H N N 255 
MET HA   H N N 256 
MET HB2  H N N 257 
MET HB3  H N N 258 
MET HG2  H N N 259 
MET HG3  H N N 260 
MET HE1  H N N 261 
MET HE2  H N N 262 
MET HE3  H N N 263 
MET HXT  H N N 264 
PHE N    N N N 265 
PHE CA   C N S 266 
PHE C    C N N 267 
PHE O    O N N 268 
PHE CB   C N N 269 
PHE CG   C Y N 270 
PHE CD1  C Y N 271 
PHE CD2  C Y N 272 
PHE CE1  C Y N 273 
PHE CE2  C Y N 274 
PHE CZ   C Y N 275 
PHE OXT  O N N 276 
PHE H    H N N 277 
PHE H2   H N N 278 
PHE HA   H N N 279 
PHE HB2  H N N 280 
PHE HB3  H N N 281 
PHE HD1  H N N 282 
PHE HD2  H N N 283 
PHE HE1  H N N 284 
PHE HE2  H N N 285 
PHE HZ   H N N 286 
PHE HXT  H N N 287 
PRO N    N N N 288 
PRO CA   C N S 289 
PRO C    C N N 290 
PRO O    O N N 291 
PRO CB   C N N 292 
PRO CG   C N N 293 
PRO CD   C N N 294 
PRO OXT  O N N 295 
PRO H    H N N 296 
PRO HA   H N N 297 
PRO HB2  H N N 298 
PRO HB3  H N N 299 
PRO HG2  H N N 300 
PRO HG3  H N N 301 
PRO HD2  H N N 302 
PRO HD3  H N N 303 
PRO HXT  H N N 304 
SER N    N N N 305 
SER CA   C N S 306 
SER C    C N N 307 
SER O    O N N 308 
SER CB   C N N 309 
SER OG   O N N 310 
SER OXT  O N N 311 
SER H    H N N 312 
SER H2   H N N 313 
SER HA   H N N 314 
SER HB2  H N N 315 
SER HB3  H N N 316 
SER HG   H N N 317 
SER HXT  H N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TYR N    N N N 336 
TYR CA   C N S 337 
TYR C    C N N 338 
TYR O    O N N 339 
TYR CB   C N N 340 
TYR CG   C Y N 341 
TYR CD1  C Y N 342 
TYR CD2  C Y N 343 
TYR CE1  C Y N 344 
TYR CE2  C Y N 345 
TYR CZ   C Y N 346 
TYR OH   O N N 347 
TYR OXT  O N N 348 
TYR H    H N N 349 
TYR H2   H N N 350 
TYR HA   H N N 351 
TYR HB2  H N N 352 
TYR HB3  H N N 353 
TYR HD1  H N N 354 
TYR HD2  H N N 355 
TYR HE1  H N N 356 
TYR HE2  H N N 357 
TYR HH   H N N 358 
TYR HXT  H N N 359 
VAL N    N N N 360 
VAL CA   C N S 361 
VAL C    C N N 362 
VAL O    O N N 363 
VAL CB   C N N 364 
VAL CG1  C N N 365 
VAL CG2  C N N 366 
VAL OXT  O N N 367 
VAL H    H N N 368 
VAL H2   H N N 369 
VAL HA   H N N 370 
VAL HB   H N N 371 
VAL HG11 H N N 372 
VAL HG12 H N N 373 
VAL HG13 H N N 374 
VAL HG21 H N N 375 
VAL HG22 H N N 376 
VAL HG23 H N N 377 
VAL HXT  H N N 378 
# 
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 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TYR N   CA   sing N N 319 
TYR N   H    sing N N 320 
TYR N   H2   sing N N 321 
TYR CA  C    sing N N 322 
TYR CA  CB   sing N N 323 
TYR CA  HA   sing N N 324 
TYR C   O    doub N N 325 
TYR C   OXT  sing N N 326 
TYR CB  CG   sing N N 327 
TYR CB  HB2  sing N N 328 
TYR CB  HB3  sing N N 329 
TYR CG  CD1  doub Y N 330 
TYR CG  CD2  sing Y N 331 
TYR CD1 CE1  sing Y N 332 
TYR CD1 HD1  sing N N 333 
TYR CD2 CE2  doub Y N 334 
TYR CD2 HD2  sing N N 335 
TYR CE1 CZ   doub Y N 336 
TYR CE1 HE1  sing N N 337 
TYR CE2 CZ   sing Y N 338 
TYR CE2 HE2  sing N N 339 
TYR CZ  OH   sing N N 340 
TYR OH  HH   sing N N 341 
TYR OXT HXT  sing N N 342 
VAL N   CA   sing N N 343 
VAL N   H    sing N N 344 
VAL N   H2   sing N N 345 
VAL CA  C    sing N N 346 
VAL CA  CB   sing N N 347 
VAL CA  HA   sing N N 348 
VAL C   O    doub N N 349 
VAL C   OXT  sing N N 350 
VAL CB  CG1  sing N N 351 
VAL CB  CG2  sing N N 352 
VAL CB  HB   sing N N 353 
VAL CG1 HG11 sing N N 354 
VAL CG1 HG12 sing N N 355 
VAL CG1 HG13 sing N N 356 
VAL CG2 HG21 sing N N 357 
VAL CG2 HG22 sing N N 358 
VAL CG2 HG23 sing N N 359 
VAL OXT HXT  sing N N 360 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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          'AlphaFold3 run Oct 2024' 
# 
_atom_sites.entry_id                    9EIE 
_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]   0.009072 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000732 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013957 
_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]   0.014955 
_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.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C 6  6  2.310  20.844 1.020 10.208 1.589 0.569   0.865 51.651 0.216   
H 1  1  0.493  10.511 0.323 26.126 0.140 3.142   0.041 57.800 0.003   
K 19 19 8.219  12.795 7.440 0.775  1.052 213.187 0.866 41.684 1.699   
N 7  7  12.222 0.006  3.135 9.893  2.014 28.997  1.167 0.583  -11.538 
O 8  8  3.049  13.277 2.287 5.701  1.546 0.324   0.867 32.909 0.251   
S 16 16 6.905  1.468  5.203 22.215 1.438 0.254   1.586 56.172 1.056   
# 
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_site.calc_flag 
_atom_site.pdbx_tls_group_id 
ATOM   1    N N   . ASP A 1 31  ? 25.421 5.062   -8.502  1.000 101.176 ? 27  ASP A N   1 ? 1 
ATOM   2    C CA  . ASP A 1 31  ? 24.961 6.711   -8.767  1.000 104.248 ? 27  ASP A CA  1 ? 1 
ATOM   3    C C   . ASP A 1 31  ? 24.398 6.970   -7.264  1.000 111.515 ? 27  ASP A C   1 ? 1 
ATOM   4    O O   . ASP A 1 31  ? 24.796 8.003   -6.669  1.000 111.844 ? 27  ASP A O   1 ? 1 
ATOM   5    C CB  . ASP A 1 31  ? 24.589 6.962   -10.140 1.000 99.046  ? 27  ASP A CB  1 ? 1 
ATOM   6    N N   . HIS A 1 32  ? 23.444 6.143   -6.749  1.000 122.761 ? 28  HIS A N   1 ? 1 
ATOM   7    C CA  . HIS A 1 32  ? 22.634 6.379   -5.503  1.000 125.892 ? 28  HIS A CA  1 ? 1 
ATOM   8    C C   . HIS A 1 32  ? 22.498 5.106   -4.615  1.000 123.783 ? 28  HIS A C   1 ? 1 
ATOM   9    O O   . HIS A 1 32  ? 21.835 5.222   -3.541  1.000 111.834 ? 28  HIS A O   1 ? 1 
ATOM   10   C CB  . HIS A 1 32  ? 21.257 7.020   -5.846  1.000 123.757 ? 28  HIS A CB  1 ? 1 
ATOM   11   C CG  . HIS A 1 32  ? 20.738 7.982   -4.819  1.000 120.449 ? 28  HIS A CG  1 ? 1 
ATOM   12   N ND1 . HIS A 1 32  ? 19.383 8.262   -4.670  1.000 118.976 ? 28  HIS A ND1 1 ? 1 
ATOM   13   C CD2 . HIS A 1 32  ? 21.375 8.705   -3.867  1.000 116.130 ? 28  HIS A CD2 1 ? 1 
ATOM   14   C CE1 . HIS A 1 32  ? 19.214 9.124   -3.683  1.000 116.938 ? 28  HIS A CE1 1 ? 1 
ATOM   15   N NE2 . HIS A 1 32  ? 20.425 9.411   -3.174  1.000 116.112 ? 28  HIS A NE2 1 ? 1 
ATOM   16   N N   . ALA A 1 33  ? 23.099 3.957   -5.006  1.000 121.424 ? 29  ALA A N   1 ? 1 
ATOM   17   C CA  . ALA A 1 33  ? 23.431 2.773   -4.152  1.000 113.366 ? 29  ALA A CA  1 ? 1 
ATOM   18   C C   . ALA A 1 33  ? 24.649 3.106   -3.274  1.000 112.782 ? 29  ALA A C   1 ? 1 
ATOM   19   O O   . ALA A 1 33  ? 24.982 2.338   -2.339  1.000 106.833 ? 29  ALA A O   1 ? 1 
ATOM   20   C CB  . ALA A 1 33  ? 23.720 1.560   -5.009  1.000 106.898 ? 29  ALA A CB  1 ? 1 
ATOM   21   N N   . ASP A 1 34  ? 25.305 4.211   -3.630  1.000 112.983 ? 30  ASP A N   1 ? 1 
ATOM   22   C CA  . ASP A 1 34  ? 26.436 4.876   -2.935  1.000 107.498 ? 30  ASP A CA  1 ? 1 
ATOM   23   C C   . ASP A 1 34  ? 25.924 5.595   -1.677  1.000 106.556 ? 30  ASP A C   1 ? 1 
ATOM   24   O O   . ASP A 1 34  ? 26.422 5.266   -0.593  1.000 107.911 ? 30  ASP A O   1 ? 1 
ATOM   25   C CB  . ASP A 1 34  ? 27.138 5.866   -3.876  1.000 102.901 ? 30  ASP A CB  1 ? 1 
ATOM   26   C CG  . ASP A 1 34  ? 27.842 5.246   -5.078  1.000 94.240  ? 30  ASP A CG  1 ? 1 
ATOM   27   O OD1 . ASP A 1 34  ? 28.115 4.014   -5.052  1.000 88.612  ? 30  ASP A OD1 1 ? 1 
ATOM   28   O OD2 . ASP A 1 34  ? 28.115 6.007   -6.037  1.000 87.862  ? 30  ASP A OD2 1 ? 1 
ATOM   29   N N   . ALA A 1 35  ? 24.999 6.556   -1.814  1.000 106.145 ? 31  ALA A N   1 ? 1 
ATOM   30   C CA  . ALA A 1 35  ? 24.400 7.315   -0.686  1.000 110.055 ? 31  ALA A CA  1 ? 1 
ATOM   31   C C   . ALA A 1 35  ? 23.845 6.325   0.358   1.000 110.558 ? 31  ALA A C   1 ? 1 
ATOM   32   O O   . ALA A 1 35  ? 23.646 6.739   1.513   1.000 106.092 ? 31  ALA A O   1 ? 1 
ATOM   33   C CB  . ALA A 1 35  ? 23.332 8.257   -1.201  1.000 110.301 ? 31  ALA A CB  1 ? 1 
ATOM   34   N N   . ALA A 1 36  ? 23.631 5.061   -0.043  1.000 112.215 ? 32  ALA A N   1 ? 1 
ATOM   35   C CA  . ALA A 1 36  ? 23.167 3.916   0.782   1.000 105.867 ? 32  ALA A CA  1 ? 1 
ATOM   36   C C   . ALA A 1 36  ? 24.324 3.258   1.553   1.000 105.889 ? 32  ALA A C   1 ? 1 
ATOM   37   O O   . ALA A 1 36  ? 24.162 3.179   2.786   1.000 111.950 ? 32  ALA A O   1 ? 1 
ATOM   38   C CB  . ALA A 1 36  ? 22.468 2.905   -0.089  1.000 106.397 ? 32  ALA A CB  1 ? 1 
ATOM   39   N N   . TYR A 1 37  ? 25.414 2.801   0.886   1.000 103.111 ? 33  TYR A N   1 ? 1 
ATOM   40   C CA  . TYR A 1 37  ? 26.624 2.141   1.490   1.000 94.405  ? 33  TYR A CA  1 ? 1 
ATOM   41   C C   . TYR A 1 37  ? 27.251 3.026   2.584   1.000 89.160  ? 33  TYR A C   1 ? 1 
ATOM   42   O O   . TYR A 1 37  ? 27.872 2.485   3.527   1.000 80.106  ? 33  TYR A O   1 ? 1 
ATOM   43   C CB  . TYR A 1 37  ? 27.698 1.809   0.444   1.000 90.921  ? 33  TYR A CB  1 ? 1 
ATOM   44   C CG  . TYR A 1 37  ? 28.900 1.050   0.970   1.000 93.682  ? 33  TYR A CG  1 ? 1 
ATOM   45   C CD1 . TYR A 1 37  ? 28.849 -0.320  1.207   1.000 93.014  ? 33  TYR A CD1 1 ? 1 
ATOM   46   C CD2 . TYR A 1 37  ? 30.106 1.692   1.234   1.000 96.176  ? 33  TYR A CD2 1 ? 1 
ATOM   47   C CE1 . TYR A 1 37  ? 29.948 -1.026  1.686   1.000 94.469  ? 33  TYR A CE1 1 ? 1 
ATOM   48   C CE2 . TYR A 1 37  ? 31.213 1.003   1.719   1.000 96.235  ? 33  TYR A CE2 1 ? 1 
ATOM   49   C CZ  . TYR A 1 37  ? 31.139 -0.365  1.950   1.000 97.410  ? 33  TYR A CZ  1 ? 1 
ATOM   50   O OH  . TYR A 1 37  ? 32.224 -1.053  2.435   1.000 91.861  ? 33  TYR A OH  1 ? 1 
ATOM   51   N N   . VAL A 1 38  ? 27.066 4.344   2.454   1.000 86.392  ? 34  VAL A N   1 ? 1 
ATOM   52   C CA  . VAL A 1 38  ? 27.604 5.428   3.328   1.000 86.449  ? 34  VAL A CA  1 ? 1 
ATOM   53   C C   . VAL A 1 38  ? 26.749 5.561   4.607   1.000 92.909  ? 34  VAL A C   1 ? 1 
ATOM   54   O O   . VAL A 1 38  ? 27.357 5.684   5.692   1.000 98.167  ? 34  VAL A O   1 ? 1 
ATOM   55   C CB  . VAL A 1 38  ? 27.725 6.733   2.505   1.000 82.674  ? 34  VAL A CB  1 ? 1 
ATOM   56   C CG1 . VAL A 1 38  ? 27.555 8.011   3.314   1.000 81.024  ? 34  VAL A CG1 1 ? 1 
ATOM   57   C CG2 . VAL A 1 38  ? 29.034 6.762   1.724   1.000 80.748  ? 34  VAL A CG2 1 ? 1 
ATOM   58   N N   . GLU A 1 39  ? 25.410 5.544   4.520   1.000 97.704  ? 35  GLU A N   1 ? 1 
ATOM   59   C CA  . GLU A 1 39  ? 24.495 5.519   5.710   1.000 100.370 ? 35  GLU A CA  1 ? 1 
ATOM   60   C C   . GLU A 1 39  ? 24.597 4.136   6.381   1.000 94.699  ? 35  GLU A C   1 ? 1 
ATOM   61   O O   . GLU A 1 39  ? 24.785 4.082   7.604   1.000 93.689  ? 35  GLU A O   1 ? 1 
ATOM   62   C CB  . GLU A 1 39  ? 23.031 5.766   5.325   1.000 105.168 ? 35  GLU A CB  1 ? 1 
ATOM   63   C CG  . GLU A 1 39  ? 22.610 7.218   5.164   1.000 105.147 ? 35  GLU A CG  1 ? 1 
ATOM   64   C CD  . GLU A 1 39  ? 21.243 7.309   4.493   1.000 105.584 ? 35  GLU A CD  1 ? 1 
ATOM   65   O OE1 . GLU A 1 39  ? 20.272 6.769   5.064   1.000 104.764 ? 35  GLU A OE1 1 ? 1 
ATOM   66   O OE2 . GLU A 1 39  ? 21.154 7.855   3.373   1.000 100.184 ? 35  GLU A OE2 1 ? 1 
ATOM   67   N N   . LYS A 1 40  ? 24.532 3.071   5.572   1.000 90.175  ? 36  LYS A N   1 ? 1 
ATOM   68   C CA  . LYS A 1 40  ? 24.606 1.631   5.948   1.000 90.668  ? 36  LYS A CA  1 ? 1 
ATOM   69   C C   . LYS A 1 40  ? 25.880 1.266   6.722   1.000 89.128  ? 36  LYS A C   1 ? 1 
ATOM   70   O O   . LYS A 1 40  ? 25.923 0.120   7.175   1.000 86.977  ? 36  LYS A O   1 ? 1 
ATOM   71   C CB  . LYS A 1 40  ? 24.582 0.753   4.688   1.000 96.441  ? 36  LYS A CB  1 ? 1 
ATOM   72   C CG  . LYS A 1 40  ? 23.356 -0.131  4.523   1.000 101.119 ? 36  LYS A CG  1 ? 1 
ATOM   73   C CD  . LYS A 1 40  ? 23.095 -0.532  3.076   1.000 104.194 ? 36  LYS A CD  1 ? 1 
ATOM   74   C CE  . LYS A 1 40  ? 22.772 -2.004  2.910   1.000 105.999 ? 36  LYS A CE  1 ? 1 
ATOM   75   N NZ  . LYS A 1 40  ? 21.503 -2.208  2.174   1.000 107.752 ? 36  LYS A NZ  1 ? 1 
ATOM   76   N N   . HIS A 1 41  ? 26.889 2.143   6.833   1.000 91.813  ? 37  HIS A N   1 ? 1 
ATOM   77   C CA  . HIS A 1 41  ? 28.202 1.833   7.477   1.000 90.050  ? 37  HIS A CA  1 ? 1 
ATOM   78   C C   . HIS A 1 41  ? 28.676 2.966   8.410   1.000 85.135  ? 37  HIS A C   1 ? 1 
ATOM   79   O O   . HIS A 1 41  ? 29.849 2.917   8.820   1.000 82.523  ? 37  HIS A O   1 ? 1 
ATOM   80   C CB  . HIS A 1 41  ? 29.273 1.540   6.406   1.000 93.736  ? 37  HIS A CB  1 ? 1 
ATOM   81   C CG  . HIS A 1 41  ? 29.259 0.175   5.788   1.000 96.898  ? 37  HIS A CG  1 ? 1 
ATOM   82   N ND1 . HIS A 1 41  ? 30.283 -0.742  6.006   1.000 97.155  ? 37  HIS A ND1 1 ? 1 
ATOM   83   C CD2 . HIS A 1 41  ? 28.416 -0.402  4.899   1.000 98.368  ? 37  HIS A CD2 1 ? 1 
ATOM   84   C CE1 . HIS A 1 41  ? 30.046 -1.837  5.308   1.000 100.007 ? 37  HIS A CE1 1 ? 1 
ATOM   85   N NE2 . HIS A 1 41  ? 28.905 -1.653  4.620   1.000 99.751  ? 37  HIS A NE2 1 ? 1 
ATOM   86   N N   . ASN A 1 42  ? 27.825 3.946   8.742   1.000 83.989  ? 38  ASN A N   1 ? 1 
ATOM   87   C CA  . ASN A 1 42  ? 28.121 5.039   9.718   1.000 82.378  ? 38  ASN A CA  1 ? 1 
ATOM   88   C C   . ASN A 1 42  ? 29.279 5.909   9.237   1.000 78.011  ? 38  ASN A C   1 ? 1 
ATOM   89   O O   . ASN A 1 42  ? 30.080 6.390   10.104  1.000 73.414  ? 38  ASN A O   1 ? 1 
ATOM   90   C CB  . ASN A 1 42  ? 28.422 4.502   11.119  1.000 83.055  ? 38  ASN A CB  1 ? 1 
ATOM   91   C CG  . ASN A 1 42  ? 27.174 4.513   11.964  1.000 81.374  ? 38  ASN A CG  1 ? 1 
ATOM   92   O OD1 . ASN A 1 42  ? 26.531 3.476   12.109  1.000 76.525  ? 38  ASN A OD1 1 ? 1 
ATOM   93   N ND2 . ASN A 1 42  ? 26.785 5.694   12.424  1.000 78.810  ? 38  ASN A ND2 1 ? 1 
ATOM   94   N N   . LEU A 1 43  ? 29.336 6.106   7.913   1.000 71.526  ? 39  LEU A N   1 ? 1 
ATOM   95   C CA  . LEU A 1 43  ? 30.383 6.893   7.214   1.000 63.292  ? 39  LEU A CA  1 ? 1 
ATOM   96   C C   . LEU A 1 43  ? 29.782 8.239   6.807   1.000 60.170  ? 39  LEU A C   1 ? 1 
ATOM   97   O O   . LEU A 1 43  ? 30.507 9.109   6.257   1.000 58.671  ? 39  LEU A O   1 ? 1 
ATOM   98   C CB  . LEU A 1 43  ? 30.892 6.052   6.039   1.000 60.539  ? 39  LEU A CB  1 ? 1 
ATOM   99   C CG  . LEU A 1 43  ? 31.773 4.870   6.450   1.000 59.968  ? 39  LEU A CG  1 ? 1 
ATOM   100  C CD1 . LEU A 1 43  ? 31.783 3.754   5.417   1.000 59.940  ? 39  LEU A CD1 1 ? 1 
ATOM   101  C CD2 . LEU A 1 43  ? 33.197 5.332   6.713   1.000 59.802  ? 39  LEU A CD2 1 ? 1 
ATOM   102  N N   . GLN A 1 44  ? 28.509 8.431   7.130   1.000 61.825  ? 40  GLN A N   1 ? 1 
ATOM   103  C CA  . GLN A 1 44  ? 27.803 9.695   6.830   1.000 70.191  ? 40  GLN A CA  1 ? 1 
ATOM   104  C C   . GLN A 1 44  ? 28.536 10.826  7.571   1.000 63.509  ? 40  GLN A C   1 ? 1 
ATOM   105  O O   . GLN A 1 44  ? 28.603 11.935  7.037   1.000 62.774  ? 40  GLN A O   1 ? 1 
ATOM   106  C CB  . GLN A 1 44  ? 26.295 9.554   7.126   1.000 79.287  ? 40  GLN A CB  1 ? 1 
ATOM   107  C CG  . GLN A 1 44  ? 25.437 10.741  6.659   1.000 85.666  ? 40  GLN A CG  1 ? 1 
ATOM   108  C CD  . GLN A 1 44  ? 25.935 11.464  5.415   1.000 90.417  ? 40  GLN A CD  1 ? 1 
ATOM   109  O OE1 . GLN A 1 44  ? 26.056 10.898  4.323   1.000 88.708  ? 40  GLN A OE1 1 ? 1 
ATOM   110  N NE2 . GLN A 1 44  ? 26.244 12.745  5.568   1.000 89.410  ? 40  GLN A NE2 1 ? 1 
ATOM   111  N N   . CYS A 1 45  ? 29.095 10.561  8.747   1.000 64.872  ? 41  CYS A N   1 ? 1 
ATOM   112  C CA  . CYS A 1 45  ? 29.749 11.610  9.570   1.000 65.231  ? 41  CYS A CA  1 ? 1 
ATOM   113  C C   . CYS A 1 45  ? 31.024 12.092  8.863   1.000 57.400  ? 41  CYS A C   1 ? 1 
ATOM   114  O O   . CYS A 1 45  ? 31.209 13.335  8.696   1.000 50.243  ? 41  CYS A O   1 ? 1 
ATOM   115  C CB  . CYS A 1 45  ? 30.075 11.118  10.974  1.000 69.110  ? 41  CYS A CB  1 ? 1 
ATOM   116  S SG  . CYS A 1 45  ? 30.787 12.446  11.990  1.000 79.612  ? 41  CYS A SG  1 ? 1 
ATOM   117  N N   . LEU A 1 46  ? 31.860 11.140  8.448   1.000 52.517  ? 42  LEU A N   1 ? 1 
ATOM   118  C CA  . LEU A 1 46  ? 33.107 11.410  7.684   1.000 51.744  ? 42  LEU A CA  1 ? 1 
ATOM   119  C C   . LEU A 1 46  ? 32.770 12.227  6.415   1.000 54.326  ? 42  LEU A C   1 ? 1 
ATOM   120  O O   . LEU A 1 46  ? 33.391 13.338  6.206   1.000 52.312  ? 42  LEU A O   1 ? 1 
ATOM   121  C CB  . LEU A 1 46  ? 33.780 10.077  7.335   1.000 49.420  ? 42  LEU A CB  1 ? 1 
ATOM   122  C CG  . LEU A 1 46  ? 35.063 10.210  6.508   1.000 46.599  ? 42  LEU A CG  1 ? 1 
ATOM   123  C CD1 . LEU A 1 46  ? 36.023 11.158  7.197   1.000 44.576  ? 42  LEU A CD1 1 ? 1 
ATOM   124  C CD2 . LEU A 1 46  ? 35.719 8.866   6.261   1.000 43.726  ? 42  LEU A CD2 1 ? 1 
ATOM   125  N N   . PHE A 1 47  ? 31.815 11.740  5.604   1.000 52.888  ? 43  PHE A N   1 ? 1 
ATOM   126  C CA  . PHE A 1 47  ? 31.444 12.372  4.303   1.000 49.490  ? 43  PHE A CA  1 ? 1 
ATOM   127  C C   . PHE A 1 47  ? 30.967 13.798  4.564   1.000 47.195  ? 43  PHE A C   1 ? 1 
ATOM   128  O O   . PHE A 1 47  ? 31.321 14.766  3.833   1.000 44.537  ? 43  PHE A O   1 ? 1 
ATOM   129  C CB  . PHE A 1 47  ? 30.458 11.489  3.545   1.000 49.115  ? 43  PHE A CB  1 ? 1 
ATOM   130  C CG  . PHE A 1 47  ? 31.180 10.487  2.693   1.000 50.293  ? 43  PHE A CG  1 ? 1 
ATOM   131  C CD1 . PHE A 1 47  ? 31.308 10.683  1.335   1.000 52.823  ? 43  PHE A CD1 1 ? 1 
ATOM   132  C CD2 . PHE A 1 47  ? 31.820 9.405   3.266   1.000 52.484  ? 43  PHE A CD2 1 ? 1 
ATOM   133  C CE1 . PHE A 1 47  ? 32.020 9.789   0.552   1.000 54.734  ? 43  PHE A CE1 1 ? 1 
ATOM   134  C CE2 . PHE A 1 47  ? 32.534 8.510   2.487   1.000 53.401  ? 43  PHE A CE2 1 ? 1 
ATOM   135  C CZ  . PHE A 1 47  ? 32.642 8.707   1.131   1.000 54.806  ? 43  PHE A CZ  1 ? 1 
ATOM   136  N N   . SER A 1 48  ? 30.235 13.940  5.658   1.000 48.679  ? 44  SER A N   1 ? 1 
ATOM   137  C CA  . SER A 1 48  ? 29.686 15.245  6.086   1.000 50.339  ? 44  SER A CA  1 ? 1 
ATOM   138  C C   . SER A 1 48  ? 30.836 16.154  6.538   1.000 47.764  ? 44  SER A C   1 ? 1 
ATOM   139  O O   . SER A 1 48  ? 30.804 17.321  6.155   1.000 47.379  ? 44  SER A O   1 ? 1 
ATOM   140  C CB  . SER A 1 48  ? 28.603 15.097  7.126   1.000 53.114  ? 44  SER A CB  1 ? 1 
ATOM   141  O OG  . SER A 1 48  ? 27.612 16.101  6.934   1.000 57.603  ? 44  SER A OG  1 ? 1 
ATOM   142  N N   . GLU A 1 49  ? 31.837 15.666  7.279   1.000 46.227  ? 45  GLU A N   1 ? 1 
ATOM   143  C CA  . GLU A 1 49  ? 32.928 16.570  7.745   1.000 47.009  ? 45  GLU A CA  1 ? 1 
ATOM   144  C C   . GLU A 1 49  ? 33.720 17.000  6.503   1.000 44.900  ? 45  GLU A C   1 ? 1 
ATOM   145  O O   . GLU A 1 49  ? 34.224 18.159  6.455   1.000 42.738  ? 45  GLU A O   1 ? 1 
ATOM   146  C CB  . GLU A 1 49  ? 33.850 15.949  8.796   1.000 49.451  ? 45  GLU A CB  1 ? 1 
ATOM   147  C CG  . GLU A 1 49  ? 33.177 15.056  9.825   1.000 51.340  ? 45  GLU A CG  1 ? 1 
ATOM   148  C CD  . GLU A 1 49  ? 34.059 14.765  11.030  1.000 52.569  ? 45  GLU A CD  1 ? 1 
ATOM   149  O OE1 . GLU A 1 49  ? 34.298 13.546  11.344  1.000 50.826  ? 45  GLU A OE1 1 ? 1 
ATOM   150  O OE2 . GLU A 1 49  ? 34.515 15.769  11.648  1.000 53.180  ? 45  GLU A OE2 1 ? 1 
ATOM   151  N N   . MET A 1 50  ? 33.773 16.139  5.485   1.000 44.219  ? 46  MET A N   1 ? 1 
ATOM   152  C CA  . MET A 1 50  ? 34.476 16.507  4.222   1.000 43.240  ? 46  MET A CA  1 ? 1 
ATOM   153  C C   . MET A 1 50  ? 33.700 17.637  3.526   1.000 44.365  ? 46  MET A C   1 ? 1 
ATOM   154  O O   . MET A 1 50  ? 34.288 18.737  3.274   1.000 42.624  ? 46  MET A O   1 ? 1 
ATOM   155  C CB  . MET A 1 50  ? 34.683 15.291  3.310   1.000 40.411  ? 46  MET A CB  1 ? 1 
ATOM   156  C CG  . MET A 1 50  ? 35.732 14.388  3.875   1.000 38.245  ? 46  MET A CG  1 ? 1 
ATOM   157  S SD  . MET A 1 50  ? 36.295 13.191  2.709   1.000 37.934  ? 46  MET A SD  1 ? 1 
ATOM   158  C CE  . MET A 1 50  ? 34.901 12.095  2.476   1.000 37.068  ? 46  MET A CE  1 ? 1 
ATOM   159  N N   . ALA A 1 51  ? 32.420 17.429  3.253   1.000 45.671  ? 47  ALA A N   1 ? 1 
ATOM   160  C CA  . ALA A 1 51  ? 31.612 18.488  2.621   1.000 49.350  ? 47  ALA A CA  1 ? 1 
ATOM   161  C C   . ALA A 1 51  ? 31.791 19.765  3.462   1.000 51.763  ? 47  ALA A C   1 ? 1 
ATOM   162  O O   . ALA A 1 51  ? 32.083 20.848  2.867   1.000 50.733  ? 47  ALA A O   1 ? 1 
ATOM   163  C CB  . ALA A 1 51  ? 30.191 18.017  2.478   1.000 48.925  ? 47  ALA A CB  1 ? 1 
ATOM   164  N N   . GLU A 1 52  ? 31.738 19.637  4.800   1.000 56.562  ? 48  GLU A N   1 ? 1 
ATOM   165  C CA  . GLU A 1 52  ? 31.802 20.792  5.749   1.000 60.660  ? 48  GLU A CA  1 ? 1 
ATOM   166  C C   . GLU A 1 52  ? 33.100 21.540  5.455   1.000 55.038  ? 48  GLU A C   1 ? 1 
ATOM   167  O O   . GLU A 1 52  ? 33.037 22.774  5.298   1.000 55.013  ? 48  GLU A O   1 ? 1 
ATOM   168  C CB  . GLU A 1 52  ? 31.713 20.385  7.236   1.000 67.479  ? 48  GLU A CB  1 ? 1 
ATOM   169  C CG  . GLU A 1 52  ? 31.457 21.542  8.221   1.000 74.717  ? 48  GLU A CG  1 ? 1 
ATOM   170  C CD  . GLU A 1 52  ? 31.770 21.258  9.696   1.000 83.899  ? 48  GLU A CD  1 ? 1 
ATOM   171  O OE1 . GLU A 1 52  ? 31.508 20.115  10.141  1.000 93.498  ? 48  GLU A OE1 1 ? 1 
ATOM   172  O OE2 . GLU A 1 52  ? 32.283 22.171  10.415  1.000 83.936  ? 48  GLU A OE2 1 ? 1 
ATOM   173  N N   . GLN A 1 53  ? 34.207 20.802  5.341   1.000 53.045  ? 49  GLN A N   1 ? 1 
ATOM   174  C CA  . GLN A 1 53  ? 35.586 21.353  5.167   1.000 52.946  ? 49  GLN A CA  1 ? 1 
ATOM   175  C C   . GLN A 1 53  ? 35.668 22.138  3.842   1.000 51.102  ? 49  GLN A C   1 ? 1 
ATOM   176  O O   . GLN A 1 53  ? 36.429 23.168  3.781   1.000 46.779  ? 49  GLN A O   1 ? 1 
ATOM   177  C CB  . GLN A 1 53  ? 36.572 20.189  5.323   1.000 53.144  ? 49  GLN A CB  1 ? 1 
ATOM   178  C CG  . GLN A 1 53  ? 38.018 20.524  5.001   1.000 54.436  ? 49  GLN A CG  1 ? 1 
ATOM   179  C CD  . GLN A 1 53  ? 38.655 21.400  6.038   1.000 57.154  ? 49  GLN A CD  1 ? 1 
ATOM   180  O OE1 . GLN A 1 53  ? 38.110 21.592  7.123   1.000 59.036  ? 49  GLN A OE1 1 ? 1 
ATOM   181  N NE2 . GLN A 1 53  ? 39.830 21.915  5.705   1.000 58.964  ? 49  GLN A NE2 1 ? 1 
ATOM   182  N N   . LEU A 1 54  ? 34.868 21.742  2.842   1.000 50.385  ? 50  LEU A N   1 ? 1 
ATOM   183  C CA  . LEU A 1 54  ? 34.865 22.438  1.528   1.000 54.578  ? 50  LEU A CA  1 ? 1 
ATOM   184  C C   . LEU A 1 54  ? 34.063 23.764  1.623   1.000 60.585  ? 50  LEU A C   1 ? 1 
ATOM   185  O O   . LEU A 1 54  ? 34.456 24.755  0.967   1.000 61.599  ? 50  LEU A O   1 ? 1 
ATOM   186  C CB  . LEU A 1 54  ? 34.375 21.469  0.433   1.000 50.917  ? 50  LEU A CB  1 ? 1 
ATOM   187  C CG  . LEU A 1 54  ? 35.299 20.279  0.112   1.000 47.805  ? 50  LEU A CG  1 ? 1 
ATOM   188  C CD1 . LEU A 1 54  ? 34.670 19.305  -0.889  1.000 45.309  ? 50  LEU A CD1 1 ? 1 
ATOM   189  C CD2 . LEU A 1 54  ? 36.671 20.743  -0.373  1.000 46.352  ? 50  LEU A CD2 1 ? 1 
ATOM   190  N N   . SER A 1 55  ? 33.011 23.843  2.443   1.000 65.470  ? 51  SER A N   1 ? 1 
ATOM   191  C CA  . SER A 1 55  ? 32.251 25.102  2.687   1.000 67.590  ? 51  SER A CA  1 ? 1 
ATOM   192  C C   . SER A 1 55  ? 33.124 26.158  3.363   1.000 66.954  ? 51  SER A C   1 ? 1 
ATOM   193  O O   . SER A 1 55  ? 32.987 27.331  3.036   1.000 67.205  ? 51  SER A O   1 ? 1 
ATOM   194  C CB  . SER A 1 55  ? 31.049 24.830  3.501   1.000 70.019  ? 51  SER A CB  1 ? 1 
ATOM   195  O OG  . SER A 1 55  ? 30.278 23.843  2.839   1.000 75.549  ? 51  SER A OG  1 ? 1 
ATOM   196  N N   . GLU A 1 56  ? 33.993 25.756  4.276   1.000 70.033  ? 52  GLU A N   1 ? 1 
ATOM   197  C CA  . GLU A 1 56  ? 34.795 26.705  5.085   1.000 76.753  ? 52  GLU A CA  1 ? 1 
ATOM   198  C C   . GLU A 1 56  ? 35.898 27.325  4.226   1.000 75.728  ? 52  GLU A C   1 ? 1 
ATOM   199  O O   . GLU A 1 56  ? 36.273 28.464  4.528   1.000 80.674  ? 52  GLU A O   1 ? 1 
ATOM   200  C CB  . GLU A 1 56  ? 35.308 26.024  6.351   1.000 79.288  ? 52  GLU A CB  1 ? 1 
ATOM   201  C CG  . GLU A 1 56  ? 34.229 26.037  7.419   1.000 85.219  ? 52  GLU A CG  1 ? 1 
ATOM   202  C CD  . GLU A 1 56  ? 34.509 25.182  8.634   1.000 88.368  ? 52  GLU A CD  1 ? 1 
ATOM   203  O OE1 . GLU A 1 56  ? 35.711 25.041  8.960   1.000 90.482  ? 52  GLU A OE1 1 ? 1 
ATOM   204  O OE2 . GLU A 1 56  ? 33.524 24.660  9.242   1.000 84.148  ? 52  GLU A OE2 1 ? 1 
ATOM   205  N N   . LYS A 1 57  ? 36.393 26.618  3.208   1.000 72.568  ? 53  LYS A N   1 ? 1 
ATOM   206  C CA  . LYS A 1 57  ? 37.583 27.047  2.415   1.000 68.753  ? 53  LYS A CA  1 ? 1 
ATOM   207  C C   . LYS A 1 57  ? 37.159 27.585  1.042   1.000 66.731  ? 53  LYS A C   1 ? 1 
ATOM   208  O O   . LYS A 1 57  ? 37.909 28.409  0.501   1.000 66.292  ? 53  LYS A O   1 ? 1 
ATOM   209  C CB  . LYS A 1 57  ? 38.561 25.878  2.277   1.000 69.254  ? 53  LYS A CB  1 ? 1 
ATOM   210  C CG  . LYS A 1 57  ? 39.138 25.335  3.575   1.000 70.727  ? 53  LYS A CG  1 ? 1 
ATOM   211  C CD  . LYS A 1 57  ? 40.629 25.517  3.737   1.000 72.123  ? 53  LYS A CD  1 ? 1 
ATOM   212  C CE  . LYS A 1 57  ? 41.077 25.170  5.138   1.000 74.760  ? 53  LYS A CE  1 ? 1 
ATOM   213  N NZ  . LYS A 1 57  ? 42.237 25.993  5.545   1.000 78.794  ? 53  LYS A NZ  1 ? 1 
ATOM   214  N N   . ASP A 1 58  ? 36.014 27.106  0.534   1.000 66.797  ? 54  ASP A N   1 ? 1 
ATOM   215  C CA  . ASP A 1 58  ? 35.274 27.498  -0.702  1.000 72.008  ? 54  ASP A CA  1 ? 1 
ATOM   216  C C   . ASP A 1 58  ? 36.182 27.514  -1.942  1.000 70.518  ? 54  ASP A C   1 ? 1 
ATOM   217  O O   . ASP A 1 58  ? 36.498 28.572  -2.517  1.000 69.515  ? 54  ASP A O   1 ? 1 
ATOM   218  C CB  . ASP A 1 58  ? 34.492 28.795  -0.512  1.000 75.695  ? 54  ASP A CB  1 ? 1 
ATOM   219  C CG  . ASP A 1 58  ? 33.595 29.092  -1.699  1.000 78.417  ? 54  ASP A CG  1 ? 1 
ATOM   220  O OD1 . ASP A 1 58  ? 32.985 28.137  -2.253  1.000 80.966  ? 54  ASP A OD1 1 ? 1 
ATOM   221  O OD2 . ASP A 1 58  ? 33.537 30.263  -2.075  1.000 83.858  ? 54  ASP A OD2 1 ? 1 
ATOM   222  N N   . PRO A 1 59  ? 36.533 26.310  -2.451  1.000 63.020  ? 55  PRO A N   1 ? 1 
ATOM   223  C CA  . PRO A 1 59  ? 37.471 26.181  -3.564  1.000 59.995  ? 55  PRO A CA  1 ? 1 
ATOM   224  C C   . PRO A 1 59  ? 36.855 26.605  -4.900  1.000 56.035  ? 55  PRO A C   1 ? 1 
ATOM   225  O O   . PRO A 1 59  ? 35.710 26.374  -5.095  1.000 53.230  ? 55  PRO A O   1 ? 1 
ATOM   226  C CB  . PRO A 1 59  ? 37.768 24.680  -3.601  1.000 59.098  ? 55  PRO A CB  1 ? 1 
ATOM   227  C CG  . PRO A 1 59  ? 36.495 24.037  -3.058  1.000 58.767  ? 55  PRO A CG  1 ? 1 
ATOM   228  C CD  . PRO A 1 59  ? 35.969 25.015  -2.033  1.000 59.888  ? 55  PRO A CD  1 ? 1 
ATOM   229  N N   . LYS A 1 60  ? 37.674 27.161  -5.786  1.000 58.268  ? 56  LYS A N   1 ? 1 
ATOM   230  C CA  . LYS A 1 60  ? 37.275 27.733  -7.102  1.000 60.080  ? 56  LYS A CA  1 ? 1 
ATOM   231  C C   . LYS A 1 60  ? 37.065 26.631  -8.155  1.000 54.405  ? 56  LYS A C   1 ? 1 
ATOM   232  O O   . LYS A 1 60  ? 36.285 26.923  -9.092  1.000 57.858  ? 56  LYS A O   1 ? 1 
ATOM   233  C CB  . LYS A 1 60  ? 38.320 28.773  -7.527  1.000 66.846  ? 56  LYS A CB  1 ? 1 
ATOM   234  C CG  . LYS A 1 60  ? 38.477 29.944  -6.552  1.000 70.547  ? 56  LYS A CG  1 ? 1 
ATOM   235  C CD  . LYS A 1 60  ? 39.896 30.457  -6.387  1.000 75.319  ? 56  LYS A CD  1 ? 1 
ATOM   236  C CE  . LYS A 1 60  ? 39.934 31.925  -5.989  1.000 79.792  ? 56  LYS A CE  1 ? 1 
ATOM   237  N NZ  . LYS A 1 60  ? 41.309 32.492  -5.975  1.000 81.775  ? 56  LYS A NZ  1 ? 1 
ATOM   238  N N   . THR A 1 61  ? 37.693 25.438  -8.010  1.000 47.915  ? 57  THR A N   1 ? 1 
ATOM   239  C CA  . THR A 1 61  ? 37.665 24.298  -8.994  1.000 43.321  ? 57  THR A CA  1 ? 1 
ATOM   240  C C   . THR A 1 61  ? 37.503 22.925  -8.322  1.000 42.305  ? 57  THR A C   1 ? 1 
ATOM   241  O O   . THR A 1 61  ? 37.764 22.832  -7.037  1.000 41.400  ? 57  THR A O   1 ? 1 
ATOM   242  C CB  . THR A 1 61  ? 38.967 24.218  -9.802  1.000 42.326  ? 57  THR A CB  1 ? 1 
ATOM   243  O OG1 . THR A 1 61  ? 39.920 23.359  -9.184  1.000 38.552  ? 57  THR A OG1 1 ? 1 
ATOM   244  C CG2 . THR A 1 61  ? 39.643 25.557  -9.999  1.000 43.394  ? 57  THR A CG2 1 ? 1 
ATOM   245  N N   . GLU A 1 62  ? 37.186 21.863  -9.095  1.000 38.858  ? 58  GLU A N   1 ? 1 
ATOM   246  C CA  A GLU A 1 62  ? 37.181 20.485  -8.524  0.500 37.446  ? 58  GLU A CA  1 ? 1 
ATOM   247  C CA  B GLU A 1 62  ? 37.180 20.491  -8.537  0.500 38.010  ? 58  GLU A CA  1 ? 1 
ATOM   248  C C   . GLU A 1 62  ? 38.610 20.109  -8.110  1.000 38.691  ? 58  GLU A C   1 ? 1 
ATOM   249  O O   . GLU A 1 62  ? 38.756 19.405  -7.037  1.000 37.698  ? 58  GLU A O   1 ? 1 
ATOM   250  C CB  A GLU A 1 62  ? 36.650 19.374  -9.428  0.500 36.015  ? 58  GLU A CB  1 ? 1 
ATOM   251  C CB  B GLU A 1 62  ? 36.556 19.523  -9.528  0.500 37.364  ? 58  GLU A CB  1 ? 1 
ATOM   252  C CG  A GLU A 1 62  ? 36.281 18.111  -8.633  0.500 34.570  ? 58  GLU A CG  1 ? 1 
ATOM   253  C CG  B GLU A 1 62  ? 35.066 19.760  -9.701  0.500 37.682  ? 58  GLU A CG  1 ? 1 
ATOM   254  C CD  A GLU A 1 62  ? 37.102 16.827  -8.770  0.500 33.364  ? 58  GLU A CD  1 ? 1 
ATOM   255  C CD  B GLU A 1 62  ? 34.642 20.565  -10.914 0.500 37.674  ? 58  GLU A CD  1 ? 1 
ATOM   256  O OE1 A GLU A 1 62  ? 36.534 15.863  -9.327  0.500 31.833  ? 58  GLU A OE1 1 ? 1 
ATOM   257  O OE1 B GLU A 1 62  ? 35.363 21.547  -11.309 0.500 35.575  ? 58  GLU A OE1 1 ? 1 
ATOM   258  O OE2 A GLU A 1 62  ? 38.262 16.757  -8.261  0.500 31.673  ? 58  GLU A OE2 1 ? 1 
ATOM   259  O OE2 B GLU A 1 62  ? 33.574 20.206  -11.460 0.500 38.341  ? 58  GLU A OE2 1 ? 1 
ATOM   260  N N   . GLN A 1 63  ? 39.651 20.532  -8.864  1.000 37.929  ? 59  GLN A N   1 ? 1 
ATOM   261  C CA  . GLN A 1 63  ? 41.036 20.157  -8.442  1.000 36.824  ? 59  GLN A CA  1 ? 1 
ATOM   262  C C   . GLN A 1 63  ? 41.356 20.781  -7.062  1.000 36.848  ? 59  GLN A C   1 ? 1 
ATOM   263  O O   . GLN A 1 63  ? 41.895 20.043  -6.232  1.000 34.406  ? 59  GLN A O   1 ? 1 
ATOM   264  C CB  . GLN A 1 63  ? 42.111 20.484  -9.476  1.000 36.272  ? 59  GLN A CB  1 ? 1 
ATOM   265  C CG  . GLN A 1 63  ? 42.320 19.386  -10.492 1.000 35.837  ? 59  GLN A CG  1 ? 1 
ATOM   266  C CD  . GLN A 1 63  ? 42.336 18.038  -9.827  1.000 36.216  ? 59  GLN A CD  1 ? 1 
ATOM   267  O OE1 . GLN A 1 63  ? 41.290 17.366  -9.719  1.000 37.256  ? 59  GLN A OE1 1 ? 1 
ATOM   268  N NE2 . GLN A 1 63  ? 43.519 17.674  -9.339  1.000 34.022  ? 59  GLN A NE2 1 ? 1 
ATOM   269  N N   . GLU A 1 64  ? 41.020 22.055  -6.825  1.000 37.349  ? 60  GLU A N   1 ? 1 
ATOM   270  C CA  . GLU A 1 64  ? 41.207 22.744  -5.521  1.000 39.901  ? 60  GLU A CA  1 ? 1 
ATOM   271  C C   . GLU A 1 64  ? 40.471 21.970  -4.404  1.000 38.529  ? 60  GLU A C   1 ? 1 
ATOM   272  O O   . GLU A 1 64  ? 41.125 21.661  -3.403  1.000 38.285  ? 60  GLU A O   1 ? 1 
ATOM   273  C CB  . GLU A 1 64  ? 40.776 24.221  -5.551  1.000 43.772  ? 60  GLU A CB  1 ? 1 
ATOM   274  C CG  . GLU A 1 64  ? 41.649 25.125  -6.423  1.000 47.796  ? 60  GLU A CG  1 ? 1 
ATOM   275  C CD  . GLU A 1 64  ? 41.425 26.646  -6.375  1.000 51.815  ? 60  GLU A CD  1 ? 1 
ATOM   276  O OE1 . GLU A 1 64  ? 40.860 27.158  -5.347  1.000 54.120  ? 60  GLU A OE1 1 ? 1 
ATOM   277  O OE2 . GLU A 1 64  ? 41.883 27.354  -7.337  1.000 52.203  ? 60  GLU A OE2 1 ? 1 
ATOM   278  N N   . ALA A 1 65  ? 39.179 21.651  -4.560  1.000 37.555  ? 61  ALA A N   1 ? 1 
ATOM   279  C CA  . ALA A 1 65  ? 38.406 20.818  -3.604  1.000 35.237  ? 61  ALA A CA  1 ? 1 
ATOM   280  C C   . ALA A 1 65  ? 39.163 19.529  -3.262  1.000 36.247  ? 61  ALA A C   1 ? 1 
ATOM   281  O O   . ALA A 1 65  ? 39.355 19.236  -2.068  1.000 40.692  ? 61  ALA A O   1 ? 1 
ATOM   282  C CB  . ALA A 1 65  ? 37.054 20.492  -4.169  1.000 34.923  ? 61  ALA A CB  1 ? 1 
ATOM   283  N N   . GLU A 1 66  ? 39.633 18.772  -4.250  1.000 35.941  ? 62  GLU A N   1 ? 1 
ATOM   284  C CA  . GLU A 1 66  ? 40.213 17.426  -3.991  1.000 34.385  ? 62  GLU A CA  1 ? 1 
ATOM   285  C C   . GLU A 1 66  ? 41.518 17.595  -3.213  1.000 33.971  ? 62  GLU A C   1 ? 1 
ATOM   286  O O   . GLU A 1 66  ? 41.753 16.842  -2.336  1.000 33.291  ? 62  GLU A O   1 ? 1 
ATOM   287  C CB  . GLU A 1 66  ? 40.400 16.691  -5.300  1.000 33.966  ? 62  GLU A CB  1 ? 1 
ATOM   288  C CG  . GLU A 1 66  ? 41.158 15.392  -5.190  1.000 33.323  ? 62  GLU A CG  1 ? 1 
ATOM   289  C CD  . GLU A 1 66  ? 41.234 14.656  -6.518  1.000 33.019  ? 62  GLU A CD  1 ? 1 
ATOM   290  O OE1 . GLU A 1 66  ? 40.450 15.022  -7.469  1.000 33.660  ? 62  GLU A OE1 1 ? 1 
ATOM   291  O OE2 . GLU A 1 66  ? 42.051 13.715  -6.601  1.000 31.895  ? 62  GLU A OE2 1 ? 1 
ATOM   292  N N   . ARG A 1 67  ? 42.314 18.591  -3.548  1.000 36.175  ? 63  ARG A N   1 ? 1 
ATOM   293  C CA  . ARG A 1 67  ? 43.530 18.973  -2.798  1.000 38.743  ? 63  ARG A CA  1 ? 1 
ATOM   294  C C   . ARG A 1 67  ? 43.115 19.168  -1.328  1.000 36.687  ? 63  ARG A C   1 ? 1 
ATOM   295  O O   . ARG A 1 67  ? 43.685 18.498  -0.457  1.000 35.531  ? 63  ARG A O   1 ? 1 
ATOM   296  C CB  . ARG A 1 67  ? 44.137 20.209  -3.465  1.000 42.429  ? 63  ARG A CB  1 ? 1 
ATOM   297  C CG  . ARG A 1 67  ? 45.446 20.735  -2.883  1.000 46.406  ? 63  ARG A CG  1 ? 1 
ATOM   298  C CD  . ARG A 1 67  ? 45.746 22.053  -3.622  1.000 53.211  ? 63  ARG A CD  1 ? 1 
ATOM   299  N NE  . ARG A 1 67  ? 45.748 21.910  -5.110  1.000 57.583  ? 63  ARG A NE  1 ? 1 
ATOM   300  C CZ  . ARG A 1 67  ? 45.476 22.867  -6.007  1.000 58.448  ? 63  ARG A CZ  1 ? 1 
ATOM   301  N NH1 . ARG A 1 67  ? 45.139 24.083  -5.603  1.000 59.429  ? 63  ARG A NH1 1 ? 1 
ATOM   302  N NH2 . ARG A 1 67  ? 45.530 22.596  -7.309  1.000 60.130  ? 63  ARG A NH2 1 ? 1 
ATOM   303  N N   . ILE A 1 68  ? 42.093 19.976  -1.076  1.000 35.203  ? 64  ILE A N   1 ? 1 
ATOM   304  C CA  . ILE A 1 68  ? 41.627 20.284  0.304   1.000 35.633  ? 64  ILE A CA  1 ? 1 
ATOM   305  C C   . ILE A 1 68  ? 41.257 18.979  1.022   1.000 33.623  ? 64  ILE A C   1 ? 1 
ATOM   306  O O   . ILE A 1 68  ? 41.652 18.841  2.181   1.000 32.530  ? 64  ILE A O   1 ? 1 
ATOM   307  C CB  . ILE A 1 68  ? 40.462 21.281  0.310   1.000 36.448  ? 64  ILE A CB  1 ? 1 
ATOM   308  C CG1 . ILE A 1 68  ? 40.890 22.670  -0.160  1.000 37.228  ? 64  ILE A CG1 1 ? 1 
ATOM   309  C CG2 . ILE A 1 68  ? 39.855 21.336  1.693   1.000 37.118  ? 64  ILE A CG2 1 ? 1 
ATOM   310  C CD1 . ILE A 1 68  ? 39.719 23.553  -0.555  1.000 37.942  ? 64  ILE A CD1 1 ? 1 
ATOM   311  N N   . LEU A 1 69  ? 40.596 18.029  0.356   1.000 33.476  ? 65  LEU A N   1 ? 1 
ATOM   312  C CA  . LEU A 1 69  ? 40.222 16.746  1.012   1.000 33.599  ? 65  LEU A CA  1 ? 1 
ATOM   313  C C   . LEU A 1 69  ? 41.479 15.921  1.311   1.000 33.311  ? 65  LEU A C   1 ? 1 
ATOM   314  O O   . LEU A 1 69  ? 41.505 15.281  2.374   1.000 32.232  ? 65  LEU A O   1 ? 1 
ATOM   315  C CB  . LEU A 1 69  ? 39.240 15.954  0.148   1.000 34.144  ? 65  LEU A CB  1 ? 1 
ATOM   316  C CG  . LEU A 1 69  ? 37.821 16.537  0.012   1.000 36.462  ? 65  LEU A CG  1 ? 1 
ATOM   317  C CD1 . LEU A 1 69  ? 36.821 15.483  -0.461  1.000 37.080  ? 65  LEU A CD1 1 ? 1 
ATOM   318  C CD2 . LEU A 1 69  ? 37.281 17.198  1.289   1.000 36.959  ? 65  LEU A CD2 1 ? 1 
ATOM   319  N N   . LEU A 1 70  ? 42.464 15.920  0.404   1.000 32.858  ? 66  LEU A N   1 ? 1 
ATOM   320  C CA  . LEU A 1 70  ? 43.779 15.270  0.620   1.000 32.207  ? 66  LEU A CA  1 ? 1 
ATOM   321  C C   . LEU A 1 70  ? 44.519 15.950  1.801   1.000 32.887  ? 66  LEU A C   1 ? 1 
ATOM   322  O O   . LEU A 1 70  ? 45.141 15.220  2.549   1.000 32.938  ? 66  LEU A O   1 ? 1 
ATOM   323  C CB  . LEU A 1 70  ? 44.577 15.306  -0.691  1.000 31.908  ? 66  LEU A CB  1 ? 1 
ATOM   324  C CG  . LEU A 1 70  ? 45.991 14.708  -0.635  1.000 31.695  ? 66  LEU A CG  1 ? 1 
ATOM   325  C CD1 . LEU A 1 70  ? 46.012 13.322  -0.010  1.000 31.123  ? 66  LEU A CD1 1 ? 1 
ATOM   326  C CD2 . LEU A 1 70  ? 46.608 14.624  -2.016  1.000 32.111  ? 66  LEU A CD2 1 ? 1 
ATOM   327  N N   . GLU A 1 71  ? 44.472 17.280  1.986   1.000 34.526  ? 67  GLU A N   1 ? 1 
ATOM   328  C CA  . GLU A 1 71  ? 45.145 17.996  3.115   1.000 37.418  ? 67  GLU A CA  1 ? 1 
ATOM   329  C C   . GLU A 1 71  ? 44.423 17.679  4.457   1.000 36.279  ? 67  GLU A C   1 ? 1 
ATOM   330  O O   . GLU A 1 71  ? 45.084 17.383  5.438   1.000 31.418  ? 67  GLU A O   1 ? 1 
ATOM   331  C CB  . GLU A 1 71  ? 45.219 19.498  2.815   1.000 41.304  ? 67  GLU A CB  1 ? 1 
ATOM   332  C CG  . GLU A 1 71  ? 46.540 19.939  2.172   1.000 47.239  ? 67  GLU A CG  1 ? 1 
ATOM   333  C CD  . GLU A 1 71  ? 46.568 21.220  1.302   1.000 52.067  ? 67  GLU A CD  1 ? 1 
ATOM   334  O OE1 . GLU A 1 71  ? 45.600 22.074  1.350   1.000 51.794  ? 67  GLU A OE1 1 ? 1 
ATOM   335  O OE2 . GLU A 1 71  ? 47.569 21.375  0.543   1.000 54.041  ? 67  GLU A OE2 1 ? 1 
ATOM   336  N N   . PHE A 1 72  ? 43.092 17.706  4.454   1.000 36.523  ? 68  PHE A N   1 ? 1 
ATOM   337  C CA  . PHE A 1 72  ? 42.193 17.385  5.586   1.000 36.630  ? 68  PHE A CA  1 ? 1 
ATOM   338  C C   . PHE A 1 72  ? 42.557 16.028  6.190   1.000 36.119  ? 68  PHE A C   1 ? 1 
ATOM   339  O O   . PHE A 1 72  ? 42.838 15.912  7.400   1.000 38.079  ? 68  PHE A O   1 ? 1 
ATOM   340  C CB  . PHE A 1 72  ? 40.758 17.420  5.074   1.000 36.853  ? 68  PHE A CB  1 ? 1 
ATOM   341  C CG  . PHE A 1 72  ? 39.713 17.215  6.128   1.000 37.525  ? 68  PHE A CG  1 ? 1 
ATOM   342  C CD1 . PHE A 1 72  ? 39.643 18.052  7.238   1.000 39.093  ? 68  PHE A CD1 1 ? 1 
ATOM   343  C CD2 . PHE A 1 72  ? 38.770 16.197  6.008   1.000 37.826  ? 68  PHE A CD2 1 ? 1 
ATOM   344  C CE1 . PHE A 1 72  ? 38.685 17.853  8.226   1.000 36.260  ? 68  PHE A CE1 1 ? 1 
ATOM   345  C CE2 . PHE A 1 72  ? 37.802 16.010  6.986   1.000 36.406  ? 68  PHE A CE2 1 ? 1 
ATOM   346  C CZ  . PHE A 1 72  ? 37.762 16.840  8.087   1.000 35.508  ? 68  PHE A CZ  1 ? 1 
ATOM   347  N N   . LEU A 1 73  ? 42.559 15.005  5.357   1.000 35.964  ? 69  LEU A N   1 ? 1 
ATOM   348  C CA  . LEU A 1 73  ? 42.837 13.612  5.769   1.000 35.515  ? 69  LEU A CA  1 ? 1 
ATOM   349  C C   . LEU A 1 73  ? 44.280 13.490  6.276   1.000 35.068  ? 69  LEU A C   1 ? 1 
ATOM   350  O O   . LEU A 1 73  ? 44.511 12.634  7.150   1.000 36.647  ? 69  LEU A O   1 ? 1 
ATOM   351  C CB  . LEU A 1 73  ? 42.581 12.673  4.585   1.000 35.182  ? 69  LEU A CB  1 ? 1 
ATOM   352  C CG  . LEU A 1 73  ? 41.127 12.563  4.109   1.000 36.049  ? 69  LEU A CG  1 ? 1 
ATOM   353  C CD1 . LEU A 1 73  ? 41.013 11.507  2.995   1.000 37.613  ? 69  LEU A CD1 1 ? 1 
ATOM   354  C CD2 . LEU A 1 73  ? 40.180 12.234  5.241   1.000 33.092  ? 69  LEU A CD2 1 ? 1 
ATOM   355  N N   . THR A 1 74  ? 45.209 14.263  5.706   1.000 34.268  ? 70  THR A N   1 ? 1 
ATOM   356  C CA  . THR A 1 74  ? 46.661 14.171  5.974   1.000 33.718  ? 70  THR A CA  1 ? 1 
ATOM   357  C C   . THR A 1 74  ? 46.875 14.755  7.381   1.000 34.326  ? 70  THR A C   1 ? 1 
ATOM   358  O O   . THR A 1 74  ? 47.633 14.150  8.135   1.000 32.869  ? 70  THR A O   1 ? 1 
ATOM   359  C CB  . THR A 1 74  ? 47.484 14.862  4.868   1.000 32.375  ? 70  THR A CB  1 ? 1 
ATOM   360  O OG1 . THR A 1 74  ? 47.371 14.062  3.700   1.000 34.243  ? 70  THR A OG1 1 ? 1 
ATOM   361  C CG2 . THR A 1 74  ? 48.961 15.008  5.176   1.000 31.525  ? 70  THR A CG2 1 ? 1 
ATOM   362  N N   . HIS A 1 75  ? 46.254 15.903  7.669   1.000 34.472  ? 71  HIS A N   1 ? 1 
ATOM   363  C CA  . HIS A 1 75  ? 46.348 16.651  8.946   1.000 36.548  ? 71  HIS A CA  1 ? 1 
ATOM   364  C C   . HIS A 1 75  ? 45.761 15.763  10.058  1.000 36.921  ? 71  HIS A C   1 ? 1 
ATOM   365  O O   . HIS A 1 75  ? 46.451 15.595  11.049  1.000 39.633  ? 71  HIS A O   1 ? 1 
ATOM   366  C CB  . HIS A 1 75  ? 45.711 18.043  8.830   1.000 37.932  ? 71  HIS A CB  1 ? 1 
ATOM   367  C CG  . HIS A 1 75  ? 45.759 18.866  10.085  1.000 42.126  ? 71  HIS A CG  1 ? 1 
ATOM   368  N ND1 . HIS A 1 75  ? 46.944 19.361  10.622  1.000 45.285  ? 71  HIS A ND1 1 ? 1 
ATOM   369  C CD2 . HIS A 1 75  ? 44.770 19.340  10.885  1.000 42.060  ? 71  HIS A CD2 1 ? 1 
ATOM   370  C CE1 . HIS A 1 75  ? 46.678 20.098  11.684  1.000 44.746  ? 71  HIS A CE1 1 ? 1 
ATOM   371  N NE2 . HIS A 1 75  ? 45.348 20.111  11.853  1.000 42.760  ? 71  HIS A NE2 1 ? 1 
ATOM   372  N N   . ARG A 1 76  ? 44.609 15.113  9.839   1.000 35.488  ? 72  ARG A N   1 ? 1 
ATOM   373  C CA  . ARG A 1 76  ? 43.998 14.126  10.755  1.000 33.431  ? 72  ARG A CA  1 ? 1 
ATOM   374  C C   . ARG A 1 76  ? 44.881 12.891  10.978  1.000 33.909  ? 72  ARG A C   1 ? 1 
ATOM   375  O O   . ARG A 1 76  ? 44.751 12.249  12.077  1.000 30.638  ? 72  ARG A O   1 ? 1 
ATOM   376  C CB  . ARG A 1 76  ? 42.707 13.611  10.155  1.000 32.658  ? 72  ARG A CB  1 ? 1 
ATOM   377  C CG  . ARG A 1 76  ? 41.577 14.612  10.121  1.000 33.669  ? 72  ARG A CG  1 ? 1 
ATOM   378  C CD  . ARG A 1 76  ? 40.504 13.953  9.294   1.000 33.230  ? 72  ARG A CD  1 ? 1 
ATOM   379  N NE  . ARG A 1 76  ? 39.295 14.203  9.983   1.000 33.439  ? 72  ARG A NE  1 ? 1 
ATOM   380  C CZ  . ARG A 1 76  ? 38.462 13.296  10.452  1.000 34.075  ? 72  ARG A CZ  1 ? 1 
ATOM   381  N NH1 . ARG A 1 76  ? 38.653 11.997  10.297  1.000 32.308  ? 72  ARG A NH1 1 ? 1 
ATOM   382  N NH2 . ARG A 1 76  ? 37.378 13.745  11.055  1.000 36.410  ? 72  ARG A NH2 1 ? 1 
ATOM   383  N N   . LYS A 1 77  ? 45.634 12.470  9.959   1.000 33.598  ? 73  LYS A N   1 ? 1 
ATOM   384  C CA  . LYS A 1 77  ? 46.548 11.312  10.108  1.000 35.449  ? 73  LYS A CA  1 ? 1 
ATOM   385  C C   . LYS A 1 77  ? 47.672 11.765  11.036  1.000 33.502  ? 73  LYS A C   1 ? 1 
ATOM   386  O O   . LYS A 1 77  ? 48.158 10.949  11.801  1.000 35.044  ? 73  LYS A O   1 ? 1 
ATOM   387  C CB  . LYS A 1 77  ? 47.078 10.826  8.753   1.000 39.361  ? 73  LYS A CB  1 ? 1 
ATOM   388  C CG  . LYS A 1 77  ? 48.352 9.982   8.764   1.000 42.560  ? 73  LYS A CG  1 ? 1 
ATOM   389  C CD  . LYS A 1 77  ? 48.159 8.533   8.448   1.000 46.912  ? 73  LYS A CD  1 ? 1 
ATOM   390  C CE  . LYS A 1 77  ? 49.336 7.915   7.719   1.000 52.879  ? 73  LYS A CE  1 ? 1 
ATOM   391  N NZ  . LYS A 1 77  ? 50.452 7.690   8.661   1.000 56.057  ? 73  LYS A NZ  1 ? 1 
ATOM   392  N N   . ALA A 1 78  ? 48.049 13.035  10.952  1.000 31.803  ? 74  ALA A N   1 ? 1 
ATOM   393  C CA  . ALA A 1 78  ? 49.126 13.637  11.760  1.000 31.676  ? 74  ALA A CA  1 ? 1 
ATOM   394  C C   . ALA A 1 78  ? 48.634 13.701  13.213  1.000 31.143  ? 74  ALA A C   1 ? 1 
ATOM   395  O O   . ALA A 1 78  ? 49.403 13.266  14.078  1.000 32.194  ? 74  ALA A O   1 ? 1 
ATOM   396  C CB  . ALA A 1 78  ? 49.530 14.992  11.207  1.000 30.070  ? 74  ALA A CB  1 ? 1 
ATOM   397  N N   . GLU A 1 79  ? 47.419 14.218  13.444  1.000 29.612  ? 75  GLU A N   1 ? 1 
ATOM   398  C CA  . GLU A 1 79  ? 46.796 14.340  14.780  1.000 30.489  ? 75  GLU A CA  1 ? 1 
ATOM   399  C C   . GLU A 1 79  ? 46.739 12.945  15.384  1.000 28.769  ? 75  GLU A C   1 ? 1 
ATOM   400  O O   . GLU A 1 79  ? 47.007 12.805  16.547  1.000 30.231  ? 75  GLU A O   1 ? 1 
ATOM   401  C CB  . GLU A 1 79  ? 45.384 14.935  14.750  1.000 31.722  ? 75  GLU A CB  1 ? 1 
ATOM   402  C CG  . GLU A 1 79  ? 45.306 16.394  14.329  1.000 32.779  ? 75  GLU A CG  1 ? 1 
ATOM   403  C CD  . GLU A 1 79  ? 43.884 16.923  14.153  1.000 35.701  ? 75  GLU A CD  1 ? 1 
ATOM   404  O OE1 . GLU A 1 79  ? 42.905 16.095  14.071  1.000 39.358  ? 75  GLU A OE1 1 ? 1 
ATOM   405  O OE2 . GLU A 1 79  ? 43.730 18.157  14.115  1.000 36.341  ? 75  GLU A OE2 1 ? 1 
ATOM   406  N N   . ARG A 1 80  ? 46.452 11.947  14.580  1.000 28.261  ? 76  ARG A N   1 ? 1 
ATOM   407  C CA  . ARG A 1 80  ? 46.209 10.566  15.038  1.000 28.217  ? 76  ARG A CA  1 ? 1 
ATOM   408  C C   . ARG A 1 80  ? 47.562 9.931   15.378  1.000 29.783  ? 76  ARG A C   1 ? 1 
ATOM   409  O O   . ARG A 1 80  ? 47.616 9.092   16.318  1.000 28.730  ? 76  ARG A O   1 ? 1 
ATOM   410  C CB  . ARG A 1 80  ? 45.425 9.807   13.959  1.000 27.212  ? 76  ARG A CB  1 ? 1 
ATOM   411  C CG  . ARG A 1 80  ? 44.766 8.528   14.460  1.000 26.812  ? 76  ARG A CG  1 ? 1 
ATOM   412  C CD  . ARG A 1 80  ? 43.850 7.880   13.446  1.000 26.614  ? 76  ARG A CD  1 ? 1 
ATOM   413  N NE  . ARG A 1 80  ? 42.807 8.781   13.017  1.000 26.763  ? 76  ARG A NE  1 ? 1 
ATOM   414  C CZ  . ARG A 1 80  ? 42.666 9.278   11.796  1.000 27.398  ? 76  ARG A CZ  1 ? 1 
ATOM   415  N NH1 . ARG A 1 80  ? 43.530 8.952   10.842  1.000 28.301  ? 76  ARG A NH1 1 ? 1 
ATOM   416  N NH2 . ARG A 1 80  ? 41.624 10.058  11.544  1.000 26.550  ? 76  ARG A NH2 1 ? 1 
ATOM   417  N N   . ASP A 1 81  ? 48.592 10.287  14.598  1.000 33.055  ? 77  ASP A N   1 ? 1 
ATOM   418  C CA  . ASP A 1 81  ? 49.996 9.809   14.740  1.000 35.765  ? 77  ASP A CA  1 ? 1 
ATOM   419  C C   . ASP A 1 81  ? 50.532 10.347  16.089  1.000 35.543  ? 77  ASP A C   1 ? 1 
ATOM   420  O O   . ASP A 1 81  ? 51.216 9.579   16.807  1.000 33.381  ? 77  ASP A O   1 ? 1 
ATOM   421  C CB  . ASP A 1 81  ? 50.831 10.207  13.512  1.000 38.161  ? 77  ASP A CB  1 ? 1 
ATOM   422  C CG  . ASP A 1 81  ? 50.760 9.202   12.337  1.000 41.508  ? 77  ASP A CG  1 ? 1 
ATOM   423  O OD1 . ASP A 1 81  ? 49.755 8.445   12.266  1.000 43.707  ? 77  ASP A OD1 1 ? 1 
ATOM   424  O OD2 . ASP A 1 81  ? 51.744 9.118   11.509  1.000 38.612  ? 77  ASP A OD2 1 ? 1 
ATOM   425  N N   . ARG A 1 82  ? 50.176 11.589  16.434  1.000 33.024  ? 78  ARG A N   1 ? 1 
ATOM   426  C CA  . ARG A 1 82  ? 50.556 12.206  17.713  1.000 35.683  ? 78  ARG A CA  1 ? 1 
ATOM   427  C C   . ARG A 1 82  ? 49.748 11.592  18.886  1.000 34.858  ? 78  ARG A C   1 ? 1 
ATOM   428  O O   . ARG A 1 82  ? 50.373 11.197  19.886  1.000 31.014  ? 78  ARG A O   1 ? 1 
ATOM   429  C CB  . ARG A 1 82  ? 50.389 13.711  17.618  1.000 38.455  ? 78  ARG A CB  1 ? 1 
ATOM   430  C CG  . ARG A 1 82  ? 50.356 14.364  18.989  1.000 42.151  ? 78  ARG A CG  1 ? 1 
ATOM   431  C CD  . ARG A 1 82  ? 50.616 15.817  18.751  1.000 48.831  ? 78  ARG A CD  1 ? 1 
ATOM   432  N NE  . ARG A 1 82  ? 50.381 16.673  19.895  1.000 56.168  ? 78  ARG A NE  1 ? 1 
ATOM   433  C CZ  . ARG A 1 82  ? 51.049 16.630  21.045  1.000 61.146  ? 78  ARG A CZ  1 ? 1 
ATOM   434  N NH1 . ARG A 1 82  ? 51.955 15.697  21.320  1.000 63.423  ? 78  ARG A NH1 1 ? 1 
ATOM   435  N NH2 . ARG A 1 82  ? 50.753 17.521  21.962  1.000 64.325  ? 78  ARG A NH2 1 ? 1 
ATOM   436  N N   . ALA A 1 83  ? 48.415 11.472  18.786  1.000 34.472  ? 79  ALA A N   1 ? 1 
ATOM   437  C CA  . ALA A 1 83  ? 47.604 10.749  19.791  1.000 34.570  ? 79  ALA A CA  1 ? 1 
ATOM   438  C C   . ALA A 1 83  ? 48.214 9.359   20.078  1.000 34.308  ? 79  ALA A C   1 ? 1 
ATOM   439  O O   . ALA A 1 83  ? 48.382 9.037   21.265  1.000 33.046  ? 79  ALA A O   1 ? 1 
ATOM   440  C CB  . ALA A 1 83  ? 46.169 10.696  19.369  1.000 34.975  ? 79  ALA A CB  1 ? 1 
ATOM   441  N N   . ALA A 1 84  ? 48.649 8.601   19.060  1.000 34.096  ? 80  ALA A N   1 ? 1 
ATOM   442  C CA  . ALA A 1 84  ? 49.281 7.266   19.248  1.000 33.522  ? 80  ALA A CA  1 ? 1 
ATOM   443  C C   . ALA A 1 84  ? 50.605 7.361   20.051  1.000 33.985  ? 80  ALA A C   1 ? 1 
ATOM   444  O O   . ALA A 1 84  ? 50.947 6.448   20.850  1.000 32.772  ? 80  ALA A O   1 ? 1 
ATOM   445  C CB  . ALA A 1 84  ? 49.477 6.626   17.905  1.000 32.932  ? 80  ALA A CB  1 ? 1 
ATOM   446  N N   . LEU A 1 85  ? 51.390 8.392   19.811  1.000 33.970  ? 81  LEU A N   1 ? 1 
ATOM   447  C CA  . LEU A 1 85  ? 52.659 8.588   20.552  1.000 35.833  ? 81  LEU A CA  1 ? 1 
ATOM   448  C C   . LEU A 1 85  ? 52.349 8.884   22.026  1.000 36.722  ? 81  LEU A C   1 ? 1 
ATOM   449  O O   . LEU A 1 85  ? 53.029 8.343   22.852  1.000 37.935  ? 81  LEU A O   1 ? 1 
ATOM   450  C CB  . LEU A 1 85  ? 53.445 9.726   19.874  1.000 35.868  ? 81  LEU A CB  1 ? 1 
ATOM   451  C CG  . LEU A 1 85  ? 54.165 9.299   18.597  1.000 34.324  ? 81  LEU A CG  1 ? 1 
ATOM   452  C CD1 . LEU A 1 85  ? 54.486 10.488  17.735  1.000 35.114  ? 81  LEU A CD1 1 ? 1 
ATOM   453  C CD2 . LEU A 1 85  ? 55.391 8.508   18.945  1.000 33.446  ? 81  LEU A CD2 1 ? 1 
ATOM   454  N N   . ARG A 1 86  ? 51.333 9.693   22.299  1.000 37.927  ? 82  ARG A N   1 ? 1 
ATOM   455  C CA  . ARG A 1 86  ? 51.001 10.177  23.648  1.000 40.021  ? 82  ARG A CA  1 ? 1 
ATOM   456  C C   . ARG A 1 86  ? 50.241 9.090   24.415  1.000 37.472  ? 82  ARG A C   1 ? 1 
ATOM   457  O O   . ARG A 1 86  ? 50.507 8.961   25.590  1.000 36.813  ? 82  ARG A O   1 ? 1 
ATOM   458  C CB  . ARG A 1 86  ? 50.271 11.510  23.500  1.000 46.241  ? 82  ARG A CB  1 ? 1 
ATOM   459  C CG  . ARG A 1 86  ? 49.281 11.853  24.600  1.000 53.714  ? 82  ARG A CG  1 ? 1 
ATOM   460  C CD  . ARG A 1 86  ? 48.334 12.889  23.998  1.000 61.091  ? 82  ARG A CD  1 ? 1 
ATOM   461  N NE  . ARG A 1 86  ? 48.654 14.253  24.391  1.000 68.275  ? 82  ARG A NE  1 ? 1 
ATOM   462  C CZ  . ARG A 1 86  ? 48.086 15.346  23.884  1.000 67.253  ? 82  ARG A CZ  1 ? 1 
ATOM   463  N NH1 . ARG A 1 86  ? 47.205 15.249  22.897  1.000 67.130  ? 82  ARG A NH1 1 ? 1 
ATOM   464  N NH2 . ARG A 1 86  ? 48.411 16.532  24.375  1.000 65.400  ? 82  ARG A NH2 1 ? 1 
ATOM   465  N N   . LEU A 1 87  ? 49.396 8.291   23.758  1.000 35.122  ? 83  LEU A N   1 ? 1 
ATOM   466  C CA  . LEU A 1 87  ? 48.492 7.301   24.401  1.000 33.411  ? 83  LEU A CA  1 ? 1 
ATOM   467  C C   . LEU A 1 87  ? 48.993 5.869   24.229  1.000 35.961  ? 83  LEU A C   1 ? 1 
ATOM   468  O O   . LEU A 1 87  ? 48.225 4.960   24.411  1.000 39.329  ? 83  LEU A O   1 ? 1 
ATOM   469  C CB  . LEU A 1 87  ? 47.100 7.442   23.789  1.000 30.234  ? 83  LEU A CB  1 ? 1 
ATOM   470  C CG  . LEU A 1 87  ? 46.485 8.829   23.897  1.000 29.152  ? 83  LEU A CG  1 ? 1 
ATOM   471  C CD1 . LEU A 1 87  ? 45.147 8.830   23.201  1.000 28.971  ? 83  LEU A CD1 1 ? 1 
ATOM   472  C CD2 . LEU A 1 87  ? 46.289 9.259   25.348  1.000 29.338  ? 83  LEU A CD2 1 ? 1 
ATOM   473  N N   . GLN A 1 88  ? 50.238 5.683   23.839  1.000 39.964  ? 84  GLN A N   1 ? 1 
ATOM   474  C CA  . GLN A 1 88  ? 50.966 4.381   23.815  1.000 40.599  ? 84  GLN A CA  1 ? 1 
ATOM   475  C C   . GLN A 1 88  ? 50.705 3.657   25.140  1.000 38.081  ? 84  GLN A C   1 ? 1 
ATOM   476  O O   . GLN A 1 88  ? 51.007 4.299   26.204  1.000 37.539  ? 84  GLN A O   1 ? 1 
ATOM   477  C CB  . GLN A 1 88  ? 52.431 4.787   23.683  1.000 46.620  ? 84  GLN A CB  1 ? 1 
ATOM   478  C CG  . GLN A 1 88  ? 53.357 3.803   23.016  1.000 54.033  ? 84  GLN A CG  1 ? 1 
ATOM   479  C CD  . GLN A 1 88  ? 54.730 4.423   22.788  1.000 58.661  ? 84  GLN A CD  1 ? 1 
ATOM   480  O OE1 . GLN A 1 88  ? 54.962 5.643   22.925  1.000 53.162  ? 84  GLN A OE1 1 ? 1 
ATOM   481  N NE2 . GLN A 1 88  ? 55.672 3.559   22.429  1.000 63.358  ? 84  GLN A NE2 1 ? 1 
ATOM   482  N N   . PHE A 1 89  ? 50.197 2.418   25.107  1.000 33.775  ? 85  PHE A N   1 ? 1 
ATOM   483  C CA  . PHE A 1 89  ? 49.907 1.597   26.315  1.000 32.232  ? 85  PHE A CA  1 ? 1 
ATOM   484  C C   . PHE A 1 89  ? 50.493 0.168   26.227  1.000 33.510  ? 85  PHE A C   1 ? 1 
ATOM   485  O O   . PHE A 1 89  ? 50.428 -0.484  25.144  1.000 33.707  ? 85  PHE A O   1 ? 1 
ATOM   486  C CB  . PHE A 1 89  ? 48.397 1.617   26.573  1.000 30.960  ? 85  PHE A CB  1 ? 1 
ATOM   487  C CG  . PHE A 1 89  ? 47.531 0.888   25.584  1.000 30.959  ? 85  PHE A CG  1 ? 1 
ATOM   488  C CD1 . PHE A 1 89  ? 47.106 1.512   24.422  1.000 30.844  ? 85  PHE A CD1 1 ? 1 
ATOM   489  C CD2 . PHE A 1 89  ? 47.130 -0.429  25.813  1.000 31.153  ? 85  PHE A CD2 1 ? 1 
ATOM   490  C CE1 . PHE A 1 89  ? 46.282 0.858   23.521  1.000 30.520  ? 85  PHE A CE1 1 ? 1 
ATOM   491  C CE2 . PHE A 1 89  ? 46.362 -1.106  24.874  1.000 30.571  ? 85  PHE A CE2 1 ? 1 
ATOM   492  C CZ  . PHE A 1 89  ? 45.952 -0.464  23.726  1.000 30.303  ? 85  PHE A CZ  1 ? 1 
ATOM   493  N N   . SER A 1 90  ? 51.011 -0.342  27.357  1.000 34.464  ? 86  SER A N   1 ? 1 
ATOM   494  C CA  . SER A 1 90  ? 51.692 -1.658  27.531  1.000 35.935  ? 86  SER A CA  1 ? 1 
ATOM   495  C C   . SER A 1 90  ? 50.780 -2.686  28.215  1.000 36.216  ? 86  SER A C   1 ? 1 
ATOM   496  O O   . SER A 1 90  ? 51.136 -3.857  28.171  1.000 40.387  ? 86  SER A O   1 ? 1 
ATOM   497  C CB  . SER A 1 90  ? 52.947 -1.519  28.390  1.000 37.270  ? 86  SER A CB  1 ? 1 
ATOM   498  O OG  . SER A 1 90  ? 53.737 -0.407  27.992  1.000 40.041  ? 86  SER A OG  1 ? 1 
ATOM   499  N N   . HIS A 1 91  ? 49.710 -2.282  28.911  1.000 34.955  ? 87  HIS A N   1 ? 1 
ATOM   500  C CA  . HIS A 1 91  ? 48.892 -3.174  29.791  1.000 33.353  ? 87  HIS A CA  1 ? 1 
ATOM   501  C C   . HIS A 1 91  ? 47.387 -2.935  29.592  1.000 31.530  ? 87  HIS A C   1 ? 1 
ATOM   502  O O   . HIS A 1 91  ? 46.659 -3.892  29.457  1.000 31.278  ? 87  HIS A O   1 ? 1 
ATOM   503  C CB  . HIS A 1 91  ? 49.279 -3.026  31.275  1.000 32.465  ? 87  HIS A CB  1 ? 1 
ATOM   504  C CG  . HIS A 1 91  ? 50.733 -3.267  31.540  1.000 33.861  ? 87  HIS A CG  1 ? 1 
ATOM   505  N ND1 . HIS A 1 91  ? 51.272 -4.560  31.625  1.000 36.176  ? 87  HIS A ND1 1 ? 1 
ATOM   506  C CD2 . HIS A 1 91  ? 51.768 -2.410  31.704  1.000 32.520  ? 87  HIS A CD2 1 ? 1 
ATOM   507  C CE1 . HIS A 1 91  ? 52.574 -4.474  31.818  1.000 34.658  ? 87  HIS A CE1 1 ? 1 
ATOM   508  N NE2 . HIS A 1 91  ? 52.896 -3.167  31.870  1.000 33.819  ? 87  HIS A NE2 1 ? 1 
ATOM   509  N N   . SER A 1 92  ? 46.911 -1.704  29.625  1.000 29.721  ? 88  SER A N   1 ? 1 
ATOM   510  C CA  . SER A 1 92  ? 45.491 -1.434  29.949  1.000 28.018  ? 88  SER A CA  1 ? 1 
ATOM   511  C C   . SER A 1 92  ? 45.107 -0.039  29.462  1.000 26.495  ? 88  SER A C   1 ? 1 
ATOM   512  O O   . SER A 1 92  ? 45.983 0.839   29.414  1.000 25.884  ? 88  SER A O   1 ? 1 
ATOM   513  C CB  . SER A 1 92  ? 45.282 -1.604  31.460  1.000 27.379  ? 88  SER A CB  1 ? 1 
ATOM   514  O OG  . SER A 1 92  ? 45.417 -0.373  32.179  1.000 27.320  ? 88  SER A OG  1 ? 1 
ATOM   515  N N   . PHE A 1 93  ? 43.849 0.188   29.148  1.000 25.121  ? 89  PHE A N   1 ? 1 
ATOM   516  C CA  . PHE A 1 93  ? 43.341 1.568   28.973  1.000 24.529  ? 89  PHE A CA  1 ? 1 
ATOM   517  C C   . PHE A 1 93  ? 41.939 1.599   29.530  1.000 24.504  ? 89  PHE A C   1 ? 1 
ATOM   518  O O   . PHE A 1 93  ? 41.271 0.579   29.512  1.000 25.552  ? 89  PHE A O   1 ? 1 
ATOM   519  C CB  . PHE A 1 93  ? 43.411 2.052   27.516  1.000 23.947  ? 89  PHE A CB  1 ? 1 
ATOM   520  C CG  . PHE A 1 93  ? 42.445 1.492   26.514  1.000 23.956  ? 89  PHE A CG  1 ? 1 
ATOM   521  C CD1 . PHE A 1 93  ? 42.907 0.941   25.327  1.000 25.684  ? 89  PHE A CD1 1 ? 1 
ATOM   522  C CD2 . PHE A 1 93  ? 41.076 1.598   26.672  1.000 25.113  ? 89  PHE A CD2 1 ? 1 
ATOM   523  C CE1 . PHE A 1 93  ? 42.044 0.453   24.347  1.000 25.054  ? 89  PHE A CE1 1 ? 1 
ATOM   524  C CE2 . PHE A 1 93  ? 40.202 1.129   25.696  1.000 26.428  ? 89  PHE A CE2 1 ? 1 
ATOM   525  C CZ  . PHE A 1 93  ? 40.687 0.547   24.529  1.000 25.493  ? 89  PHE A CZ  1 ? 1 
ATOM   526  N N   . GLU A 1 94  ? 41.481 2.768   29.911  1.000 25.423  ? 90  GLU A N   1 ? 1 
ATOM   527  C CA  . GLU A 1 94  ? 40.042 3.006   30.175  1.000 25.917  ? 90  GLU A CA  1 ? 1 
ATOM   528  C C   . GLU A 1 94  ? 39.630 4.238   29.394  1.000 23.924  ? 90  GLU A C   1 ? 1 
ATOM   529  O O   . GLU A 1 94  ? 40.350 5.234   29.382  1.000 24.868  ? 90  GLU A O   1 ? 1 
ATOM   530  C CB  . GLU A 1 94  ? 39.778 3.186   31.672  1.000 28.650  ? 90  GLU A CB  1 ? 1 
ATOM   531  C CG  . GLU A 1 94  ? 38.366 3.683   31.997  1.000 31.985  ? 90  GLU A CG  1 ? 1 
ATOM   532  C CD  . GLU A 1 94  ? 37.950 3.765   33.464  1.000 33.669  ? 90  GLU A CD  1 ? 1 
ATOM   533  O OE1 . GLU A 1 94  ? 37.218 4.685   33.822  1.000 34.595  ? 90  GLU A OE1 1 ? 1 
ATOM   534  O OE2 . GLU A 1 94  ? 38.394 2.921   34.235  1.000 38.708  ? 90  GLU A OE2 1 ? 1 
ATOM   535  N N   . VAL A 1 95  ? 38.481 4.163   28.772  1.000 23.360  ? 91  VAL A N   1 ? 1 
ATOM   536  C CA  . VAL A 1 95  ? 37.770 5.333   28.201  1.000 23.075  ? 91  VAL A CA  1 ? 1 
ATOM   537  C C   . VAL A 1 95  ? 36.519 5.540   29.032  1.000 22.916  ? 91  VAL A C   1 ? 1 
ATOM   538  O O   . VAL A 1 95  ? 35.779 4.601   29.149  1.000 23.673  ? 91  VAL A O   1 ? 1 
ATOM   539  C CB  . VAL A 1 95  ? 37.421 5.009   26.746  1.000 23.542  ? 91  VAL A CB  1 ? 1 
ATOM   540  C CG1 . VAL A 1 95  ? 36.607 6.122   26.127  1.000 23.638  ? 91  VAL A CG1 1 ? 1 
ATOM   541  C CG2 . VAL A 1 95  ? 38.689 4.672   25.968  1.000 23.689  ? 91  VAL A CG2 1 ? 1 
ATOM   542  N N   . ASN A 1 96  ? 36.283 6.732   29.536  1.000 24.052  ? 92  ASN A N   1 ? 1 
ATOM   543  C CA  . ASN A 1 96  ? 35.067 7.094   30.303  1.000 25.466  ? 92  ASN A CA  1 ? 1 
ATOM   544  C C   . ASN A 1 96  ? 34.471 8.371   29.688  1.000 26.092  ? 92  ASN A C   1 ? 1 
ATOM   545  O O   . ASN A 1 96  ? 35.140 9.395   29.824  1.000 25.708  ? 92  ASN A O   1 ? 1 
ATOM   546  C CB  . ASN A 1 96  ? 35.506 7.224   31.759  1.000 26.749  ? 92  ASN A CB  1 ? 1 
ATOM   547  C CG  . ASN A 1 96  ? 34.390 7.572   32.710  1.000 28.554  ? 92  ASN A CG  1 ? 1 
ATOM   548  O OD1 . ASN A 1 96  ? 33.621 8.525   32.461  1.000 30.473  ? 92  ASN A OD1 1 ? 1 
ATOM   549  N ND2 . ASN A 1 96  ? 34.353 6.840   33.827  1.000 29.296  ? 92  ASN A ND2 1 ? 1 
ATOM   550  N N   . LEU A 1 97  ? 33.270 8.340   29.079  1.000 29.023  ? 93  LEU A N   1 ? 1 
ATOM   551  C CA  . LEU A 1 97  ? 32.647 9.501   28.355  1.000 32.007  ? 93  LEU A CA  1 ? 1 
ATOM   552  C C   . LEU A 1 97  ? 31.317 9.981   28.970  1.000 34.035  ? 93  LEU A C   1 ? 1 
ATOM   553  O O   . LEU A 1 97  ? 30.731 9.197   29.645  1.000 31.073  ? 93  LEU A O   1 ? 1 
ATOM   554  C CB  . LEU A 1 97  ? 32.350 9.050   26.919  1.000 31.791  ? 93  LEU A CB  1 ? 1 
ATOM   555  C CG  . LEU A 1 97  ? 33.501 8.353   26.243  1.000 33.789  ? 93  LEU A CG  1 ? 1 
ATOM   556  C CD1 . LEU A 1 97  ? 33.084 7.726   24.938  1.000 34.910  ? 93  LEU A CD1 1 ? 1 
ATOM   557  C CD2 . LEU A 1 97  ? 34.608 9.357   26.023  1.000 35.353  ? 93  LEU A CD2 1 ? 1 
ATOM   558  N N   . ASP A 1 98  ? 30.750 11.067  28.406  1.000 43.038  ? 94  ASP A N   1 ? 1 
ATOM   559  C CA  . ASP A 1 98  ? 29.440 11.732  28.672  1.000 47.853  ? 94  ASP A CA  1 ? 1 
ATOM   560  C C   . ASP A 1 98  ? 29.533 11.897  30.151  1.000 53.662  ? 94  ASP A C   1 ? 1 
ATOM   561  O O   . ASP A 1 98  ? 28.547 11.653  30.836  1.000 58.962  ? 94  ASP A O   1 ? 1 
ATOM   562  C CB  . ASP A 1 98  ? 28.160 10.983  28.300  1.000 49.376  ? 94  ASP A CB  1 ? 1 
ATOM   563  C CG  . ASP A 1 98  ? 28.039 10.551  26.841  1.000 58.213  ? 94  ASP A CG  1 ? 1 
ATOM   564  O OD1 . ASP A 1 98  ? 28.855 11.063  25.994  1.000 61.725  ? 94  ASP A OD1 1 ? 1 
ATOM   565  O OD2 . ASP A 1 98  ? 27.117 9.696   26.535  1.000 55.537  ? 94  ASP A OD2 1 ? 1 
ATOM   566  N N   . ASN A 1 99  ? 30.784 12.114  30.539  1.000 60.168  ? 95  ASN A N   1 ? 1 
ATOM   567  C CA  . ASN A 1 99  ? 31.385 11.823  31.875  1.000 67.537  ? 95  ASN A CA  1 ? 1 
ATOM   568  C C   . ASN A 1 99  ? 30.513 10.830  32.732  1.000 65.052  ? 95  ASN A C   1 ? 1 
ATOM   569  O O   . ASN A 1 99  ? 29.505 11.238  33.342  1.000 66.441  ? 95  ASN A O   1 ? 1 
ATOM   570  C CB  . ASN A 1 99  ? 31.792 13.191  32.452  1.000 73.477  ? 95  ASN A CB  1 ? 1 
ATOM   571  C CG  . ASN A 1 99  ? 32.586 14.082  31.498  1.000 74.845  ? 95  ASN A CG  1 ? 1 
ATOM   572  O OD1 . ASN A 1 99  ? 33.746 14.395  31.791  1.000 77.036  ? 95  ASN A OD1 1 ? 1 
ATOM   573  N ND2 . ASN A 1 99  ? 31.969 14.540  30.405  1.000 59.039  ? 95  ASN A ND2 1 ? 1 
ATOM   574  N N   . GLY A 1 100 ? 30.883 9.535   32.812  1.000 61.658  ? 96  GLY A N   1 ? 1 
ATOM   575  C CA  . GLY A 1 100 ? 30.247 8.525   33.692  1.000 59.813  ? 96  GLY A CA  1 ? 1 
ATOM   576  C C   . GLY A 1 100 ? 29.417 7.460   32.961  1.000 61.685  ? 96  GLY A C   1 ? 1 
ATOM   577  O O   . GLY A 1 100 ? 29.466 6.253   33.375  1.000 60.742  ? 96  GLY A O   1 ? 1 
ATOM   578  N N   . ARG A 1 101 ? 28.667 7.872   31.929  1.000 57.498  ? 97  ARG A N   1 ? 1 
ATOM   579  C CA  . ARG A 1 101 ? 27.534 7.132   31.331  1.000 54.725  ? 97  ARG A CA  1 ? 1 
ATOM   580  C C   . ARG A 1 101 ? 27.950 6.389   30.055  1.000 49.748  ? 97  ARG A C   1 ? 1 
ATOM   581  O O   . ARG A 1 101 ? 27.068 6.108   29.243  1.000 56.819  ? 97  ARG A O   1 ? 1 
ATOM   582  C CB  . ARG A 1 101 ? 26.447 8.155   31.007  1.000 64.433  ? 97  ARG A CB  1 ? 1 
ATOM   583  C CG  . ARG A 1 101 ? 25.904 8.933   32.206  1.000 71.416  ? 97  ARG A CG  1 ? 1 
ATOM   584  C CD  . ARG A 1 101 ? 24.640 9.719   31.821  1.000 81.764  ? 97  ARG A CD  1 ? 1 
ATOM   585  N NE  . ARG A 1 101 ? 24.778 10.794  30.813  1.000 88.613  ? 97  ARG A NE  1 ? 1 
ATOM   586  C CZ  . ARG A 1 101 ? 24.402 10.749  29.516  1.000 90.469  ? 97  ARG A CZ  1 ? 1 
ATOM   587  N NH1 . ARG A 1 101 ? 23.845 9.667   28.990  1.000 88.809  ? 97  ARG A NH1 1 ? 1 
ATOM   588  N NH2 . ARG A 1 101 ? 24.597 11.805  28.738  1.000 90.657  ? 97  ARG A NH2 1 ? 1 
ATOM   589  N N   . LYS A 1 102 ? 29.245 6.172   29.822  1.000 43.498  ? 98  LYS A N   1 ? 1 
ATOM   590  C CA  . LYS A 1 102 ? 29.815 5.190   28.860  1.000 39.895  ? 98  LYS A CA  1 ? 1 
ATOM   591  C C   . LYS A 1 102 ? 31.256 4.889   29.257  1.000 35.939  ? 98  LYS A C   1 ? 1 
ATOM   592  O O   . LYS A 1 102 ? 32.042 5.837   29.342  1.000 37.259  ? 98  LYS A O   1 ? 1 
ATOM   593  C CB  . LYS A 1 102 ? 29.817 5.708   27.422  1.000 41.217  ? 98  LYS A CB  1 ? 1 
ATOM   594  C CG  . LYS A 1 102 ? 28.952 4.899   26.482  1.000 42.899  ? 98  LYS A CG  1 ? 1 
ATOM   595  C CD  . LYS A 1 102 ? 29.072 5.260   25.029  1.000 44.867  ? 98  LYS A CD  1 ? 1 
ATOM   596  C CE  . LYS A 1 102 ? 28.629 6.669   24.717  1.000 45.447  ? 98  LYS A CE  1 ? 1 
ATOM   597  N NZ  . LYS A 1 102 ? 28.828 6.899   23.271  1.000 47.326  ? 98  LYS A NZ  1 ? 1 
ATOM   598  N N   . ILE A 1 103 ? 31.586 3.624   29.478  1.000 31.139  ? 99  ILE A N   1 ? 1 
ATOM   599  C CA  . ILE A 1 103 ? 32.921 3.222   29.988  1.000 29.313  ? 99  ILE A CA  1 ? 1 
ATOM   600  C C   . ILE A 1 103 ? 33.354 1.974   29.246  1.000 26.861  ? 99  ILE A C   1 ? 1 
ATOM   601  O O   . ILE A 1 103 ? 32.564 1.057   29.204  1.000 25.897  ? 99  ILE A O   1 ? 1 
ATOM   602  C CB  . ILE A 1 103 ? 32.921 2.925   31.508  1.000 28.593  ? 99  ILE A CB  1 ? 1 
ATOM   603  C CG1 . ILE A 1 103 ? 32.482 4.105   32.375  1.000 28.225  ? 99  ILE A CG1 1 ? 1 
ATOM   604  C CG2 . ILE A 1 103 ? 34.291 2.409   31.922  1.000 28.677  ? 99  ILE A CG2 1 ? 1 
ATOM   605  C CD1 . ILE A 1 103 ? 32.019 3.704   33.805  1.000 27.626  ? 99  ILE A CD1 1 ? 1 
ATOM   606  N N   . MET A 1 104 ? 34.611 1.929   28.831  1.000 27.015  ? 100 MET A N   1 ? 1 
ATOM   607  C CA  . MET A 1 104 ? 35.313 0.741   28.245  1.000 28.779  ? 100 MET A CA  1 ? 1 
ATOM   608  C C   . MET A 1 104 ? 36.676 0.602   28.939  1.000 26.750  ? 100 MET A C   1 ? 1 
ATOM   609  O O   . MET A 1 104 ? 37.338 1.608   29.081  1.000 24.635  ? 100 MET A O   1 ? 1 
ATOM   610  C CB  . MET A 1 104 ? 35.521 0.942   26.726  1.000 30.303  ? 100 MET A CB  1 ? 1 
ATOM   611  C CG  . MET A 1 104 ? 36.368 -0.113  25.975  1.000 32.057  ? 100 MET A CG  1 ? 1 
ATOM   612  S SD  . MET A 1 104 ? 36.550 0.331   24.141  1.000 33.323  ? 100 MET A SD  1 ? 1 
ATOM   613  C CE  . MET A 1 104 ? 34.827 0.324   23.644  1.000 33.785  ? 100 MET A CE  1 ? 1 
ATOM   614  N N   . ARG A 1 105 ? 37.027 -0.593  29.374  1.000 26.793  ? 101 ARG A N   1 ? 1 
ATOM   615  C CA  . ARG A 1 105 ? 38.344 -0.949  29.915  1.000 27.938  ? 101 ARG A CA  1 ? 1 
ATOM   616  C C   . ARG A 1 105 ? 38.850 -2.110  29.085  1.000 27.795  ? 101 ARG A C   1 ? 1 
ATOM   617  O O   . ARG A 1 105 ? 38.039 -2.986  28.768  1.000 26.912  ? 101 ARG A O   1 ? 1 
ATOM   618  C CB  . ARG A 1 105 ? 38.237 -1.460  31.342  1.000 31.350  ? 101 ARG A CB  1 ? 1 
ATOM   619  C CG  . ARG A 1 105 ? 37.714 -0.430  32.325  1.000 36.232  ? 101 ARG A CG  1 ? 1 
ATOM   620  C CD  . ARG A 1 105 ? 37.790 -0.972  33.759  1.000 39.969  ? 101 ARG A CD  1 ? 1 
ATOM   621  N NE  . ARG A 1 105 ? 37.184 -0.182  34.832  1.000 41.189  ? 101 ARG A NE  1 ? 1 
ATOM   622  C CZ  . ARG A 1 105 ? 35.883 0.004   35.039  1.000 42.875  ? 101 ARG A CZ  1 ? 1 
ATOM   623  N NH1 . ARG A 1 105 ? 34.984 -0.498  34.218  1.000 45.455  ? 101 ARG A NH1 1 ? 1 
ATOM   624  N NH2 . ARG A 1 105 ? 35.479 0.713   36.080  1.000 47.138  ? 101 ARG A NH2 1 ? 1 
ATOM   625  N N   . LEU A 1 106 ? 40.130 -2.100  28.754  1.000 28.765  ? 102 LEU A N   1 ? 1 
ATOM   626  C CA  . LEU A 1 106 ? 40.842 -3.152  27.972  1.000 30.704  ? 102 LEU A CA  1 ? 1 
ATOM   627  C C   . LEU A 1 106 ? 42.107 -3.531  28.732  1.000 30.481  ? 102 LEU A C   1 ? 1 
ATOM   628  O O   . LEU A 1 106 ? 42.837 -2.605  29.105  1.000 29.763  ? 102 LEU A O   1 ? 1 
ATOM   629  C CB  . LEU A 1 106 ? 41.233 -2.618  26.586  1.000 32.219  ? 102 LEU A CB  1 ? 1 
ATOM   630  C CG  . LEU A 1 106 ? 42.050 -3.606  25.760  1.000 33.471  ? 102 LEU A CG  1 ? 1 
ATOM   631  C CD1 . LEU A 1 106 ? 41.154 -4.387  24.826  1.000 36.258  ? 102 LEU A CD1 1 ? 1 
ATOM   632  C CD2 . LEU A 1 106 ? 43.076 -2.911  24.938  1.000 34.239  ? 102 LEU A CD2 1 ? 1 
ATOM   633  N N   . GLN A 1 107 ? 42.335 -4.819  28.953  1.000 31.839  ? 103 GLN A N   1 ? 1 
ATOM   634  C CA  . GLN A 1 107 ? 43.631 -5.360  29.417  1.000 34.936  ? 103 GLN A CA  1 ? 1 
ATOM   635  C C   . GLN A 1 107 ? 44.199 -6.239  28.295  1.000 35.968  ? 103 GLN A C   1 ? 1 
ATOM   636  O O   . GLN A 1 107 ? 43.452 -7.069  27.711  1.000 35.098  ? 103 GLN A O   1 ? 1 
ATOM   637  C CB  . GLN A 1 107 ? 43.490 -6.166  30.708  1.000 37.491  ? 103 GLN A CB  1 ? 1 
ATOM   638  C CG  . GLN A 1 107 ? 42.715 -5.471  31.820  1.000 40.383  ? 103 GLN A CG  1 ? 1 
ATOM   639  C CD  . GLN A 1 107 ? 41.211 -5.346  31.603  1.000 43.085  ? 103 GLN A CD  1 ? 1 
ATOM   640  O OE1 . GLN A 1 107 ? 40.495 -6.323  31.318  1.000 44.580  ? 103 GLN A OE1 1 ? 1 
ATOM   641  N NE2 . GLN A 1 107 ? 40.691 -4.130  31.786  1.000 43.903  ? 103 GLN A NE2 1 ? 1 
ATOM   642  N N   . LEU A 1 108 ? 45.480 -6.063  27.996  1.000 38.092  ? 104 LEU A N   1 ? 1 
ATOM   643  C CA  . LEU A 1 108 ? 46.255 -6.928  27.071  1.000 40.248  ? 104 LEU A CA  1 ? 1 
ATOM   644  C C   . LEU A 1 108 ? 46.608 -8.230  27.765  1.000 43.221  ? 104 LEU A C   1 ? 1 
ATOM   645  O O   . LEU A 1 108 ? 46.836 -8.181  28.999  1.000 43.112  ? 104 LEU A O   1 ? 1 
ATOM   646  C CB  . LEU A 1 108 ? 47.537 -6.199  26.702  1.000 41.241  ? 104 LEU A CB  1 ? 1 
ATOM   647  C CG  . LEU A 1 108 ? 47.354 -4.939  25.854  1.000 42.113  ? 104 LEU A CG  1 ? 1 
ATOM   648  C CD1 . LEU A 1 108 ? 48.689 -4.287  25.535  1.000 41.454  ? 104 LEU A CD1 1 ? 1 
ATOM   649  C CD2 . LEU A 1 108 ? 46.613 -5.251  24.567  1.000 41.582  ? 104 LEU A CD2 1 ? 1 
ATOM   650  N N   . GLY A 1 109 ? 46.627 -9.323  26.997  1.000 49.185  ? 105 GLY A N   1 ? 1 
ATOM   651  C CA  . GLY A 1 109 ? 47.372 -10.577 27.285  1.000 54.832  ? 105 GLY A CA  1 ? 1 
ATOM   652  C C   . GLY A 1 109 ? 48.130 -11.134 26.073  1.000 59.844  ? 105 GLY A C   1 ? 1 
ATOM   653  O O   . GLY A 1 109 ? 47.877 -10.636 24.938  1.000 59.299  ? 105 GLY A O   1 ? 1 
ATOM   654  N N   . GLN A 1 110 ? 48.965 -12.172 26.271  1.000 65.981  ? 106 GLN A N   1 ? 1 
ATOM   655  C CA  . GLN A 1 110 ? 49.808 -12.804 25.206  1.000 71.547  ? 106 GLN A CA  1 ? 1 
ATOM   656  C C   . GLN A 1 110 ? 48.937 -13.138 23.985  1.000 72.288  ? 106 GLN A C   1 ? 1 
ATOM   657  O O   . GLN A 1 110 ? 49.257 -12.624 22.896  1.000 71.181  ? 106 GLN A O   1 ? 1 
ATOM   658  C CB  . GLN A 1 110 ? 50.508 -14.098 25.651  1.000 78.802  ? 106 GLN A CB  1 ? 1 
ATOM   659  C CG  . GLN A 1 110 ? 51.767 -13.926 26.507  1.000 85.805  ? 106 GLN A CG  1 ? 1 
ATOM   660  C CD  . GLN A 1 110 ? 51.529 -14.198 27.984  1.000 92.110  ? 106 GLN A CD  1 ? 1 
ATOM   661  O OE1 . GLN A 1 110 ? 50.567 -13.701 28.576  1.000 94.497  ? 106 GLN A OE1 1 ? 1 
ATOM   662  N NE2 . GLN A 1 110 ? 52.397 -14.994 28.603  1.000 87.652  ? 106 GLN A NE2 1 ? 1 
ATOM   663  N N   . GLU A 1 111 ? 47.868 -13.931 24.155  1.000 73.106  ? 107 GLU A N   1 ? 1 
ATOM   664  C CA  . GLU A 1 111 ? 47.110 -14.539 23.019  1.000 73.743  ? 107 GLU A CA  1 ? 1 
ATOM   665  C C   . GLU A 1 111 ? 45.778 -13.801 22.755  1.000 66.226  ? 107 GLU A C   1 ? 1 
ATOM   666  O O   . GLU A 1 111 ? 45.322 -13.858 21.595  1.000 65.611  ? 107 GLU A O   1 ? 1 
ATOM   667  C CB  . GLU A 1 111 ? 46.928 -16.041 23.260  1.000 78.201  ? 107 GLU A CB  1 ? 1 
ATOM   668  C CG  . GLU A 1 111 ? 48.090 -16.890 22.761  1.000 80.351  ? 107 GLU A CG  1 ? 1 
ATOM   669  C CD  . GLU A 1 111 ? 47.945 -18.383 23.031  1.000 87.259  ? 107 GLU A CD  1 ? 1 
ATOM   670  O OE1 . GLU A 1 111 ? 47.124 -18.763 23.897  1.000 90.077  ? 107 GLU A OE1 1 ? 1 
ATOM   671  O OE2 . GLU A 1 111 ? 48.657 -19.172 22.383  1.000 90.930  ? 107 GLU A OE2 1 ? 1 
ATOM   672  N N   . THR A 1 112 ? 45.175 -13.134 23.752  1.000 58.136  ? 108 THR A N   1 ? 1 
ATOM   673  C CA  . THR A 1 112 ? 43.909 -12.351 23.620  1.000 50.624  ? 108 THR A CA  1 ? 1 
ATOM   674  C C   . THR A 1 112 ? 43.970 -11.100 24.498  1.000 47.716  ? 108 THR A C   1 ? 1 
ATOM   675  O O   . THR A 1 112 ? 44.770 -11.086 25.436  1.000 52.954  ? 108 THR A O   1 ? 1 
ATOM   676  C CB  . THR A 1 112 ? 42.685 -13.179 24.038  1.000 48.246  ? 108 THR A CB  1 ? 1 
ATOM   677  O OG1 . THR A 1 112 ? 42.834 -13.568 25.395  1.000 46.386  ? 108 THR A OG1 1 ? 1 
ATOM   678  C CG2 . THR A 1 112 ? 42.490 -14.431 23.220  1.000 48.121  ? 108 THR A CG2 1 ? 1 
ATOM   679  N N   . SER A 1 113 ? 43.128 -10.105 24.226  1.000 45.502  ? 109 SER A N   1 ? 1 
ATOM   680  C CA  . SER A 1 113 ? 42.790 -8.983  25.151  1.000 44.638  ? 109 SER A CA  1 ? 1 
ATOM   681  C C   . SER A 1 113 ? 41.465 -9.245  25.890  1.000 42.652  ? 109 SER A C   1 ? 1 
ATOM   682  O O   . SER A 1 113 ? 40.589 -9.868  25.313  1.000 43.176  ? 109 SER A O   1 ? 1 
ATOM   683  C CB  . SER A 1 113 ? 42.736 -7.731  24.356  1.000 44.092  ? 109 SER A CB  1 ? 1 
ATOM   684  O OG  . SER A 1 113 ? 44.001 -7.554  23.744  1.000 43.923  ? 109 SER A OG  1 ? 1 
ATOM   685  N N   . THR A 1 114 ? 41.307 -8.831  27.139  1.000 40.302  ? 110 THR A N   1 ? 1 
ATOM   686  C CA  . THR A 1 114 ? 39.982 -8.874  27.819  1.000 40.621  ? 110 THR A CA  1 ? 1 
ATOM   687  C C   . THR A 1 114 ? 39.392 -7.460  27.790  1.000 37.406  ? 110 THR A C   1 ? 1 
ATOM   688  O O   . THR A 1 114 ? 40.163 -6.520  27.727  1.000 36.188  ? 110 THR A O   1 ? 1 
ATOM   689  C CB  . THR A 1 114 ? 40.099 -9.498  29.209  1.000 41.659  ? 110 THR A CB  1 ? 1 
ATOM   690  O OG1 . THR A 1 114 ? 41.141 -8.795  29.884  1.000 45.287  ? 110 THR A OG1 1 ? 1 
ATOM   691  C CG2 . THR A 1 114 ? 40.430 -10.971 29.161  1.000 41.771  ? 110 THR A CG2 1 ? 1 
ATOM   692  N N   . LEU A 1 115 ? 38.074 -7.343  27.798  1.000 37.311  ? 111 LEU A N   1 ? 1 
ATOM   693  C CA  . LEU A 1 115 ? 37.312 -6.103  27.450  1.000 38.351  ? 111 LEU A CA  1 ? 1 
ATOM   694  C C   . LEU A 1 115 ? 36.049 -6.012  28.324  1.000 36.773  ? 111 LEU A C   1 ? 1 
ATOM   695  O O   . LEU A 1 115 ? 35.352 -7.000  28.406  1.000 36.498  ? 111 LEU A O   1 ? 1 
ATOM   696  C CB  . LEU A 1 115 ? 36.980 -6.211  25.961  1.000 39.336  ? 111 LEU A CB  1 ? 1 
ATOM   697  C CG  . LEU A 1 115 ? 36.566 -4.924  25.263  1.000 41.675  ? 111 LEU A CG  1 ? 1 
ATOM   698  C CD1 . LEU A 1 115 ? 37.665 -3.895  25.413  1.000 45.114  ? 111 LEU A CD1 1 ? 1 
ATOM   699  C CD2 . LEU A 1 115 ? 36.251 -5.136  23.779  1.000 41.091  ? 111 LEU A CD2 1 ? 1 
ATOM   700  N N   . GLN A 1 116 ? 35.833 -4.924  29.064  1.000 37.741  ? 112 GLN A N   1 ? 1 
ATOM   701  C CA  . GLN A 1 116 ? 34.622 -4.707  29.919  1.000 36.911  ? 112 GLN A CA  1 ? 1 
ATOM   702  C C   . GLN A 1 116 ? 33.916 -3.440  29.420  1.000 33.636  ? 112 GLN A C   1 ? 1 
ATOM   703  O O   . GLN A 1 116 ? 34.598 -2.445  29.290  1.000 35.713  ? 112 GLN A O   1 ? 1 
ATOM   704  C CB  . GLN A 1 116 ? 35.002 -4.548  31.397  1.000 38.465  ? 112 GLN A CB  1 ? 1 
ATOM   705  C CG  . GLN A 1 116 ? 35.691 -5.764  32.023  1.000 42.042  ? 112 GLN A CG  1 ? 1 
ATOM   706  C CD  . GLN A 1 116 ? 37.152 -5.908  31.657  1.000 46.250  ? 112 GLN A CD  1 ? 1 
ATOM   707  O OE1 . GLN A 1 116 ? 37.957 -5.013  31.887  1.000 51.390  ? 112 GLN A OE1 1 ? 1 
ATOM   708  N NE2 . GLN A 1 116 ? 37.534 -7.032  31.063  1.000 49.431  ? 112 GLN A NE2 1 ? 1 
ATOM   709  N N   . LEU A 1 117 ? 32.641 -3.456  29.072  1.000 31.958  ? 113 LEU A N   1 ? 1 
ATOM   710  C CA  . LEU A 1 117 ? 31.927 -2.201  28.733  1.000 32.767  ? 113 LEU A CA  1 ? 1 
ATOM   711  C C   . LEU A 1 117 ? 30.774 -1.974  29.680  1.000 33.666  ? 113 LEU A C   1 ? 1 
ATOM   712  O O   . LEU A 1 117 ? 30.142 -2.989  30.074  1.000 33.811  ? 113 LEU A O   1 ? 1 
ATOM   713  C CB  . LEU A 1 117 ? 31.294 -2.313  27.362  1.000 33.885  ? 113 LEU A CB  1 ? 1 
ATOM   714  C CG  . LEU A 1 117 ? 32.158 -2.913  26.290  1.000 35.726  ? 113 LEU A CG  1 ? 1 
ATOM   715  C CD1 . LEU A 1 117 ? 31.419 -2.844  24.957  1.000 38.429  ? 113 LEU A CD1 1 ? 1 
ATOM   716  C CD2 . LEU A 1 117 ? 33.474 -2.178  26.212  1.000 36.663  ? 113 LEU A CD2 1 ? 1 
ATOM   717  N N   . GLU A 1 118 ? 30.443 -0.701  29.875  1.000 35.574  ? 114 GLU A N   1 ? 1 
ATOM   718  C CA  . GLU A 1 118 ? 29.227 -0.197  30.578  1.000 39.894  ? 114 GLU A CA  1 ? 1 
ATOM   719  C C   . GLU A 1 118 ? 28.672 0.999   29.820  1.000 36.863  ? 114 GLU A C   1 ? 1 
ATOM   720  O O   . GLU A 1 118 ? 29.470 1.821   29.331  1.000 34.649  ? 114 GLU A O   1 ? 1 
ATOM   721  C CB  . GLU A 1 118 ? 29.457 0.351   31.993  1.000 44.899  ? 114 GLU A CB  1 ? 1 
ATOM   722  C CG  . GLU A 1 118 ? 29.764 -0.710  33.022  1.000 50.514  ? 114 GLU A CG  1 ? 1 
ATOM   723  C CD  . GLU A 1 118 ? 30.330 -0.199  34.338  1.000 55.308  ? 114 GLU A CD  1 ? 1 
ATOM   724  O OE1 . GLU A 1 118 ? 31.209 -0.917  34.914  1.000 59.155  ? 114 GLU A OE1 1 ? 1 
ATOM   725  O OE2 . GLU A 1 118 ? 29.892 0.900   34.780  1.000 57.718  ? 114 GLU A OE2 1 ? 1 
ATOM   726  N N   . GLN A 1 119 ? 27.355 1.105   29.811  1.000 37.716  ? 115 GLN A N   1 ? 1 
ATOM   727  C CA  . GLN A 1 119 ? 26.623 2.227   29.185  1.000 41.753  ? 115 GLN A CA  1 ? 1 
ATOM   728  C C   . GLN A 1 119 ? 25.382 2.429   30.036  1.000 43.031  ? 115 GLN A C   1 ? 1 
ATOM   729  O O   . GLN A 1 119 ? 24.822 1.435   30.436  1.000 45.683  ? 115 GLN A O   1 ? 1 
ATOM   730  C CB  . GLN A 1 119 ? 26.317 1.862   27.734  1.000 43.930  ? 115 GLN A CB  1 ? 1 
ATOM   731  C CG  . GLN A 1 119 ? 25.903 3.014   26.834  1.000 45.995  ? 115 GLN A CG  1 ? 1 
ATOM   732  C CD  . GLN A 1 119 ? 26.438 2.852   25.433  1.000 47.905  ? 115 GLN A CD  1 ? 1 
ATOM   733  O OE1 . GLN A 1 119 ? 27.313 2.019   25.156  1.000 47.429  ? 115 GLN A OE1 1 ? 1 
ATOM   734  N NE2 . GLN A 1 119 ? 25.906 3.663   24.532  1.000 51.279  ? 115 GLN A NE2 1 ? 1 
ATOM   735  N N   . LYS A 1 120 ? 25.073 3.659   30.410  1.000 45.453  ? 116 LYS A N   1 ? 1 
ATOM   736  C CA  . LYS A 1 120 ? 23.845 4.000   31.151  1.000 48.242  ? 116 LYS A CA  1 ? 1 
ATOM   737  C C   . LYS A 1 120 ? 23.323 5.288   30.530  1.000 49.308  ? 116 LYS A C   1 ? 1 
ATOM   738  O O   . LYS A 1 120 ? 23.506 6.301   31.116  1.000 52.988  ? 116 LYS A O   1 ? 1 
ATOM   739  C CB  . LYS A 1 120 ? 24.157 4.127   32.641  1.000 49.955  ? 116 LYS A CB  1 ? 1 
ATOM   740  C CG  . LYS A 1 120 ? 24.703 2.877   33.316  1.000 54.321  ? 116 LYS A CG  1 ? 1 
ATOM   741  C CD  . LYS A 1 120 ? 25.662 3.208   34.473  1.000 59.465  ? 116 LYS A CD  1 ? 1 
ATOM   742  C CE  . LYS A 1 120 ? 25.850 2.103   35.511  1.000 66.394  ? 116 LYS A CE  1 ? 1 
ATOM   743  N NZ  . LYS A 1 120 ? 26.878 1.088   35.134  1.000 67.941  ? 116 LYS A NZ  1 ? 1 
ATOM   744  N N   . GLY A 1 121 ? 22.819 5.247   29.310  1.000 53.530  ? 117 GLY A N   1 ? 1 
ATOM   745  C CA  . GLY A 1 121 ? 22.169 6.392   28.646  1.000 57.332  ? 117 GLY A CA  1 ? 1 
ATOM   746  C C   . GLY A 1 121 ? 20.669 6.267   28.775  1.000 61.356  ? 117 GLY A C   1 ? 1 
ATOM   747  O O   . GLY A 1 121 ? 20.228 5.330   29.439  1.000 64.312  ? 117 GLY A O   1 ? 1 
ATOM   748  N N   . ARG A 1 122 ? 19.904 7.186   28.193  1.000 68.535  ? 118 ARG A N   1 ? 1 
ATOM   749  C CA  . ARG A 1 122 ? 18.427 7.159   28.306  1.000 72.155  ? 118 ARG A CA  1 ? 1 
ATOM   750  C C   . ARG A 1 122 ? 17.963 6.056   27.350  1.000 68.878  ? 118 ARG A C   1 ? 1 
ATOM   751  O O   . ARG A 1 122 ? 16.959 5.380   27.667  1.000 71.098  ? 118 ARG A O   1 ? 1 
ATOM   752  C CB  . ARG A 1 122 ? 17.831 8.548   28.016  1.000 78.549  ? 118 ARG A CB  1 ? 1 
ATOM   753  C CG  . ARG A 1 122 ? 16.431 8.822   28.579  1.000 86.869  ? 118 ARG A CG  1 ? 1 
ATOM   754  C CD  . ARG A 1 122 ? 15.475 9.576   27.637  1.000 93.087  ? 118 ARG A CD  1 ? 1 
ATOM   755  N NE  . ARG A 1 122 ? 16.177 10.032  26.425  1.000 96.534  ? 118 ARG A NE  1 ? 1 
ATOM   756  C CZ  . ARG A 1 122 ? 15.647 10.207  25.215  1.000 95.212  ? 118 ARG A CZ  1 ? 1 
ATOM   757  N NH1 . ARG A 1 122 ? 14.355 9.999   25.002  1.000 98.079  ? 118 ARG A NH1 1 ? 1 
ATOM   758  N NH2 . ARG A 1 122 ? 16.431 10.596  24.216  1.000 86.662  ? 118 ARG A NH2 1 ? 1 
ATOM   759  N N   . VAL A 1 123 ? 18.703 5.858   26.252  1.000 64.720  ? 119 VAL A N   1 ? 1 
ATOM   760  C CA  . VAL A 1 123 ? 18.258 5.060   25.067  1.000 61.359  ? 119 VAL A CA  1 ? 1 
ATOM   761  C C   . VAL A 1 123 ? 18.734 3.590   25.232  1.000 53.910  ? 119 VAL A C   1 ? 1 
ATOM   762  O O   . VAL A 1 123 ? 17.995 2.671   24.803  1.000 55.314  ? 119 VAL A O   1 ? 1 
ATOM   763  C CB  . VAL A 1 123 ? 18.676 5.782   23.754  1.000 65.623  ? 119 VAL A CB  1 ? 1 
ATOM   764  C CG1 . VAL A 1 123 ? 19.084 4.850   22.618  1.000 68.740  ? 119 VAL A CG1 1 ? 1 
ATOM   765  C CG2 . VAL A 1 123 ? 17.596 6.742   23.246  1.000 64.921  ? 119 VAL A CG2 1 ? 1 
ATOM   766  N N   . LEU A 1 124 ? 19.836 3.344   25.953  1.000 48.599  ? 120 LEU A N   1 ? 1 
ATOM   767  C CA  . LEU A 1 124 ? 20.454 2.002   26.104  1.000 44.319  ? 120 LEU A CA  1 ? 1 
ATOM   768  C C   . LEU A 1 124 ? 21.164 1.902   27.434  1.000 43.202  ? 120 LEU A C   1 ? 1 
ATOM   769  O O   . LEU A 1 124 ? 22.047 2.698   27.650  1.000 43.738  ? 120 LEU A O   1 ? 1 
ATOM   770  C CB  . LEU A 1 124 ? 21.484 1.796   24.997  1.000 42.368  ? 120 LEU A CB  1 ? 1 
ATOM   771  C CG  . LEU A 1 124 ? 22.453 0.632   25.199  1.000 40.971  ? 120 LEU A CG  1 ? 1 
ATOM   772  C CD1 . LEU A 1 124 ? 21.720 -0.656  25.488  1.000 42.038  ? 120 LEU A CD1 1 ? 1 
ATOM   773  C CD2 . LEU A 1 124 ? 23.316 0.437   23.980  1.000 39.690  ? 120 LEU A CD2 1 ? 1 
ATOM   774  N N   . LYS A 1 125 ? 20.833 0.902   28.241  1.000 44.436  ? 121 LYS A N   1 ? 1 
ATOM   775  C CA  . LYS A 1 125 ? 21.580 0.524   29.459  1.000 43.898  ? 121 LYS A CA  1 ? 1 
ATOM   776  C C   . LYS A 1 125 ? 22.269 -0.825  29.178  1.000 41.442  ? 121 LYS A C   1 ? 1 
ATOM   777  O O   . LYS A 1 125 ? 21.571 -1.730  28.752  1.000 42.578  ? 121 LYS A O   1 ? 1 
ATOM   778  C CB  . LYS A 1 125 ? 20.613 0.481   30.648  1.000 47.373  ? 121 LYS A CB  1 ? 1 
ATOM   779  C CG  . LYS A 1 125 ? 21.223 -0.261  31.837  1.000 54.961  ? 121 LYS A CG  1 ? 1 
ATOM   780  C CD  . LYS A 1 125 ? 20.423 -0.321  33.136  1.000 61.855  ? 121 LYS A CD  1 ? 1 
ATOM   781  C CE  . LYS A 1 125 ? 21.290 -0.671  34.336  1.000 66.578  ? 121 LYS A CE  1 ? 1 
ATOM   782  N NZ  . LYS A 1 125 ? 20.859 0.107   35.526  1.000 70.930  ? 121 LYS A NZ  1 ? 1 
ATOM   783  N N   . MET A 1 126 ? 23.573 -0.996  29.383  1.000 39.251  ? 122 MET A N   1 ? 1 
ATOM   784  C CA  . MET A 1 126 ? 24.207 -2.325  29.152  1.000 39.586  ? 122 MET A CA  1 ? 1 
ATOM   785  C C   . MET A 1 126 ? 25.557 -2.504  29.862  1.000 37.688  ? 122 MET A C   1 ? 1 
ATOM   786  O O   . MET A 1 126 ? 26.205 -1.503  30.191  1.000 34.614  ? 122 MET A O   1 ? 1 
ATOM   787  C CB  . MET A 1 126 ? 24.433 -2.552  27.664  1.000 41.096  ? 122 MET A CB  1 ? 1 
ATOM   788  C CG  . MET A 1 126 ? 25.473 -1.669  27.110  1.000 43.273  ? 122 MET A CG  1 ? 1 
ATOM   789  S SD  . MET A 1 126 ? 27.079 -2.484  27.027  1.000 46.192  ? 122 MET A SD  1 ? 1 
ATOM   790  C CE  . MET A 1 126 ? 28.045 -1.169  26.283  1.000 47.873  ? 122 MET A CE  1 ? 1 
ATOM   791  N N   . ASP A 1 127 ? 25.919 -3.769  30.082  1.000 37.916  ? 123 ASP A N   1 ? 1 
ATOM   792  C CA  . ASP A 1 127 ? 27.241 -4.243  30.549  1.000 39.922  ? 123 ASP A CA  1 ? 1 
ATOM   793  C C   . ASP A 1 127 ? 27.718 -5.346  29.640  1.000 39.631  ? 123 ASP A C   1 ? 1 
ATOM   794  O O   . ASP A 1 127 ? 26.904 -6.161  29.296  1.000 39.669  ? 123 ASP A O   1 ? 1 
ATOM   795  C CB  . ASP A 1 127 ? 27.155 -5.023  31.836  1.000 42.128  ? 123 ASP A CB  1 ? 1 
ATOM   796  C CG  . ASP A 1 127 ? 26.776 -4.070  32.908  1.000 49.416  ? 123 ASP A CG  1 ? 1 
ATOM   797  O OD1 . ASP A 1 127 ? 25.580 -3.632  32.952  1.000 57.620  ? 123 ASP A OD1 1 ? 1 
ATOM   798  O OD2 . ASP A 1 127 ? 27.696 -3.731  33.653  1.000 61.357  ? 123 ASP A OD2 1 ? 1 
ATOM   799  N N   . GLU A 1 128 ? 29.005 -5.448  29.394  1.000 37.238  ? 124 GLU A N   1 ? 1 
ATOM   800  C CA  . GLU A 1 128 ? 29.505 -6.605  28.653  1.000 36.392  ? 124 GLU A CA  1 ? 1 
ATOM   801  C C   . GLU A 1 128 ? 30.886 -6.879  29.171  1.000 34.393  ? 124 GLU A C   1 ? 1 
ATOM   802  O O   . GLU A 1 128 ? 31.588 -5.914  29.433  1.000 32.218  ? 124 GLU A O   1 ? 1 
ATOM   803  C CB  . GLU A 1 128 ? 29.638 -6.278  27.176  1.000 37.838  ? 124 GLU A CB  1 ? 1 
ATOM   804  C CG  . GLU A 1 128 ? 28.335 -6.122  26.496  1.000 41.434  ? 124 GLU A CG  1 ? 1 
ATOM   805  C CD  . GLU A 1 128 ? 28.546 -6.228  25.003  1.000 44.893  ? 124 GLU A CD  1 ? 1 
ATOM   806  O OE1 . GLU A 1 128 ? 29.224 -5.360  24.417  1.000 49.552  ? 124 GLU A OE1 1 ? 1 
ATOM   807  O OE2 . GLU A 1 128 ? 28.106 -7.207  24.449  1.000 46.514  ? 124 GLU A OE2 1 ? 1 
ATOM   808  N N   . ALA A 1 129 ? 31.259 -8.141  29.196  1.000 33.716  ? 125 ALA A N   1 ? 1 
ATOM   809  C CA  . ALA A 1 129 ? 32.618 -8.586  29.546  1.000 32.967  ? 125 ALA A CA  1 ? 1 
ATOM   810  C C   . ALA A 1 129 ? 32.949 -9.790  28.670  1.000 32.013  ? 125 ALA A C   1 ? 1 
ATOM   811  O O   . ALA A 1 129 ? 32.085 -10.610 28.532  1.000 31.520  ? 125 ALA A O   1 ? 1 
ATOM   812  C CB  . ALA A 1 129 ? 32.656 -8.863  31.037  1.000 31.508  ? 125 ALA A CB  1 ? 1 
ATOM   813  N N   . PHE A 1 130 ? 34.112 -9.828  28.011  1.000 34.349  ? 126 PHE A N   1 ? 1 
ATOM   814  C CA  . PHE A 1 130 ? 34.465 -10.865 27.002  1.000 35.320  ? 126 PHE A CA  1 ? 1 
ATOM   815  C C   . PHE A 1 130 ? 35.874 -10.623 26.492  1.000 34.646  ? 126 PHE A C   1 ? 1 
ATOM   816  O O   . PHE A 1 130 ? 36.442 -9.624  26.839  1.000 33.021  ? 126 PHE A O   1 ? 1 
ATOM   817  C CB  . PHE A 1 130 ? 33.452 -10.893 25.851  1.000 36.299  ? 126 PHE A CB  1 ? 1 
ATOM   818  C CG  . PHE A 1 130 ? 33.344 -9.602  25.089  1.000 37.028  ? 126 PHE A CG  1 ? 1 
ATOM   819  C CD1 . PHE A 1 130 ? 32.524 -8.585  25.525  1.000 37.025  ? 126 PHE A CD1 1 ? 1 
ATOM   820  C CD2 . PHE A 1 130 ? 34.080 -9.395  23.926  1.000 39.479  ? 126 PHE A CD2 1 ? 1 
ATOM   821  C CE1 . PHE A 1 130 ? 32.448 -7.395  24.815  1.000 37.965  ? 126 PHE A CE1 1 ? 1 
ATOM   822  C CE2 . PHE A 1 130 ? 33.995 -8.201  23.206  1.000 38.905  ? 126 PHE A CE2 1 ? 1 
ATOM   823  C CZ  . PHE A 1 130 ? 33.182 -7.198  23.665  1.000 38.467  ? 126 PHE A CZ  1 ? 1 
ATOM   824  N N   . SER A 1 131 ? 36.382 -11.540 25.674  1.000 36.773  ? 127 SER A N   1 ? 1 
ATOM   825  C CA  . SER A 1 131 ? 37.782 -11.570 25.182  1.000 37.381  ? 127 SER A CA  1 ? 1 
ATOM   826  C C   . SER A 1 131 ? 37.773 -11.263 23.683  1.000 36.065  ? 127 SER A C   1 ? 1 
ATOM   827  O O   . SER A 1 131 ? 36.802 -11.534 23.062  1.000 37.039  ? 127 SER A O   1 ? 1 
ATOM   828  C CB  . SER A 1 131 ? 38.427 -12.901 25.522  1.000 39.228  ? 127 SER A CB  1 ? 1 
ATOM   829  O OG  . SER A 1 131 ? 38.832 -12.934 26.903  1.000 43.587  ? 127 SER A OG  1 ? 1 
ATOM   830  N N   . ILE A 1 132 ? 38.806 -10.642 23.139  1.000 37.286  ? 128 ILE A N   1 ? 1 
ATOM   831  C CA  . ILE A 1 132 ? 38.927 -10.404 21.673  1.000 38.788  ? 128 ILE A CA  1 ? 1 
ATOM   832  C C   . ILE A 1 132 ? 40.306 -10.854 21.173  1.000 41.126  ? 128 ILE A C   1 ? 1 
ATOM   833  O O   . ILE A 1 132 ? 41.245 -11.018 21.985  1.000 42.114  ? 128 ILE A O   1 ? 1 
ATOM   834  C CB  . ILE A 1 132 ? 38.601 -8.940  21.333  1.000 38.201  ? 128 ILE A CB  1 ? 1 
ATOM   835  C CG1 . ILE A 1 132 ? 39.546 -7.932  21.984  1.000 36.782  ? 128 ILE A CG1 1 ? 1 
ATOM   836  C CG2 . ILE A 1 132 ? 37.155 -8.650  21.684  1.000 38.599  ? 128 ILE A CG2 1 ? 1 
ATOM   837  C CD1 . ILE A 1 132 ? 39.327 -6.527  21.511  1.000 35.626  ? 128 ILE A CD1 1 ? 1 
ATOM   838  N N   . SER A 1 133 ? 40.405 -11.125 19.873  1.000 43.456  ? 129 SER A N   1 ? 1 
ATOM   839  C CA  . SER A 1 133 ? 41.643 -11.642 19.224  1.000 44.286  ? 129 SER A CA  1 ? 1 
ATOM   840  C C   . SER A 1 133 ? 42.659 -10.504 19.159  1.000 44.472  ? 129 SER A C   1 ? 1 
ATOM   841  O O   . SER A 1 133 ? 42.243 -9.324  19.372  1.000 43.724  ? 129 SER A O   1 ? 1 
ATOM   842  C CB  . SER A 1 133 ? 41.342 -12.194 17.853  1.000 42.774  ? 129 SER A CB  1 ? 1 
ATOM   843  O OG  . SER A 1 133 ? 40.989 -11.129 16.982  1.000 42.869  ? 129 SER A OG  1 ? 1 
ATOM   844  N N   . LEU A 1 134 ? 43.910 -10.838 18.831  1.000 47.579  ? 130 LEU A N   1 ? 1 
ATOM   845  C CA  . LEU A 1 134 ? 45.001 -9.849  18.589  1.000 48.676  ? 130 LEU A CA  1 ? 1 
ATOM   846  C C   . LEU A 1 134 ? 44.656 -9.000  17.374  1.000 45.340  ? 130 LEU A C   1 ? 1 
ATOM   847  O O   . LEU A 1 134 ? 44.940 -7.807  17.433  1.000 43.361  ? 130 LEU A O   1 ? 1 
ATOM   848  C CB  . LEU A 1 134 ? 46.350 -10.541 18.408  1.000 53.732  ? 130 LEU A CB  1 ? 1 
ATOM   849  C CG  . LEU A 1 134 ? 46.813 -11.322 19.641  1.000 61.786  ? 130 LEU A CG  1 ? 1 
ATOM   850  C CD1 . LEU A 1 134 ? 47.928 -12.300 19.271  1.000 66.261  ? 130 LEU A CD1 1 ? 1 
ATOM   851  C CD2 . LEU A 1 134 ? 47.233 -10.384 20.782  1.000 60.050  ? 130 LEU A CD2 1 ? 1 
ATOM   852  N N   . GLU A 1 135 ? 44.013 -9.570  16.357  1.000 44.490  ? 131 GLU A N   1 ? 1 
ATOM   853  C CA  . GLU A 1 135 ? 43.585 -8.771  15.182  1.000 45.904  ? 131 GLU A CA  1 ? 1 
ATOM   854  C C   . GLU A 1 135 ? 42.509 -7.789  15.683  1.000 44.769  ? 131 GLU A C   1 ? 1 
ATOM   855  O O   . GLU A 1 135 ? 42.614 -6.549  15.359  1.000 41.222  ? 131 GLU A O   1 ? 1 
ATOM   856  C CB  . GLU A 1 135 ? 43.203 -9.699  14.016  1.000 51.340  ? 131 GLU A CB  1 ? 1 
ATOM   857  C CG  . GLU A 1 135 ? 42.257 -9.118  12.947  1.000 57.038  ? 131 GLU A CG  1 ? 1 
ATOM   858  C CD  . GLU A 1 135 ? 42.859 -8.434  11.714  1.000 63.399  ? 131 GLU A CD  1 ? 1 
ATOM   859  O OE1 . GLU A 1 135 ? 42.428 -8.781  10.576  1.000 70.865  ? 131 GLU A OE1 1 ? 1 
ATOM   860  O OE2 . GLU A 1 135 ? 43.748 -7.529  11.877  1.000 64.598  ? 131 GLU A OE2 1 ? 1 
ATOM   861  N N   . GLN A 1 136 ? 41.540 -8.268  16.480  1.000 42.271  ? 132 GLN A N   1 ? 1 
ATOM   862  C CA  . GLN A 1 136 ? 40.449 -7.395  16.981  1.000 41.818  ? 132 GLN A CA  1 ? 1 
ATOM   863  C C   . GLN A 1 136 ? 41.035 -6.240  17.815  1.000 41.863  ? 132 GLN A C   1 ? 1 
ATOM   864  O O   . GLN A 1 136 ? 40.645 -5.064  17.582  1.000 44.070  ? 132 GLN A O   1 ? 1 
ATOM   865  C CB  . GLN A 1 136 ? 39.421 -8.237  17.712  1.000 43.297  ? 132 GLN A CB  1 ? 1 
ATOM   866  C CG  . GLN A 1 136 ? 38.555 -9.087  16.768  1.000 43.515  ? 132 GLN A CG  1 ? 1 
ATOM   867  C CD  . GLN A 1 136 ? 37.652 -10.012 17.546  1.000 43.153  ? 132 GLN A CD  1 ? 1 
ATOM   868  O OE1 . GLN A 1 136 ? 38.047 -10.601 18.552  1.000 45.809  ? 132 GLN A OE1 1 ? 1 
ATOM   869  N NE2 . GLN A 1 136 ? 36.408 -10.108 17.138  1.000 42.353  ? 132 GLN A NE2 1 ? 1 
ATOM   870  N N   . THR A 1 137 ? 42.037 -6.509  18.649  1.000 40.869  ? 133 THR A N   1 ? 1 
ATOM   871  C CA  . THR A 1 137 ? 42.700 -5.495  19.516  1.000 39.268  ? 133 THR A CA  1 ? 1 
ATOM   872  C C   . THR A 1 137 ? 43.298 -4.370  18.678  1.000 40.177  ? 133 THR A C   1 ? 1 
ATOM   873  O O   . THR A 1 137 ? 43.171 -3.181  19.065  1.000 38.914  ? 133 THR A O   1 ? 1 
ATOM   874  C CB  . THR A 1 137 ? 43.811 -6.138  20.337  1.000 37.815  ? 133 THR A CB  1 ? 1 
ATOM   875  O OG1 . THR A 1 137 ? 43.219 -7.237  21.024  1.000 40.097  ? 133 THR A OG1 1 ? 1 
ATOM   876  C CG2 . THR A 1 137 ? 44.430 -5.171  21.308  1.000 35.917  ? 133 THR A CG2 1 ? 1 
ATOM   877  N N   . GLU A 1 138 ? 43.977 -4.758  17.607  1.000 43.042  ? 134 GLU A N   1 ? 1 
ATOM   878  C CA  . GLU A 1 138 ? 44.581 -3.837  16.606  1.000 45.814  ? 134 GLU A CA  1 ? 1 
ATOM   879  C C   . GLU A 1 138 ? 43.471 -2.953  16.025  1.000 42.964  ? 134 GLU A C   1 ? 1 
ATOM   880  O O   . GLU A 1 138 ? 43.650 -1.706  16.033  1.000 44.813  ? 134 GLU A O   1 ? 1 
ATOM   881  C CB  . GLU A 1 138 ? 45.333 -4.622  15.518  1.000 49.967  ? 134 GLU A CB  1 ? 1 
ATOM   882  C CG  . GLU A 1 138 ? 46.844 -4.383  15.428  1.000 53.859  ? 134 GLU A CG  1 ? 1 
ATOM   883  C CD  . GLU A 1 138 ? 47.756 -5.604  15.593  1.000 58.136  ? 134 GLU A CD  1 ? 1 
ATOM   884  O OE1 . GLU A 1 138 ? 48.443 -5.651  16.623  1.000 61.994  ? 134 GLU A OE1 1 ? 1 
ATOM   885  O OE2 . GLU A 1 138 ? 47.793 -6.512  14.713  1.000 58.536  ? 134 GLU A OE2 1 ? 1 
ATOM   886  N N   . GLU A 1 139 ? 42.375 -3.541  15.547  1.000 40.138  ? 135 GLU A N   1 ? 1 
ATOM   887  C CA  . GLU A 1 139 ? 41.276 -2.727  14.953  1.000 41.506  ? 135 GLU A CA  1 ? 1 
ATOM   888  C C   . GLU A 1 139 ? 40.767 -1.741  16.021  1.000 39.339  ? 135 GLU A C   1 ? 1 
ATOM   889  O O   . GLU A 1 139 ? 40.637 -0.543  15.692  1.000 36.942  ? 135 GLU A O   1 ? 1 
ATOM   890  C CB  . GLU A 1 139 ? 40.125 -3.588  14.417  1.000 44.819  ? 135 GLU A CB  1 ? 1 
ATOM   891  C CG  . GLU A 1 139 ? 40.384 -4.242  13.053  1.000 46.213  ? 135 GLU A CG  1 ? 1 
ATOM   892  C CD  . GLU A 1 139 ? 39.536 -5.489  12.760  1.000 47.258  ? 135 GLU A CD  1 ? 1 
ATOM   893  O OE1 . GLU A 1 139 ? 38.412 -5.581  13.258  1.000 44.536  ? 135 GLU A OE1 1 ? 1 
ATOM   894  O OE2 . GLU A 1 139 ? 40.026 -6.401  12.077  1.000 49.723  ? 135 GLU A OE2 1 ? 1 
ATOM   895  N N   . LEU A 1 140 ? 40.523 -2.213  17.257  1.000 36.884  ? 136 LEU A N   1 ? 1 
ATOM   896  C CA  . LEU A 1 140 ? 39.984 -1.361  18.356  1.000 36.128  ? 136 LEU A CA  1 ? 1 
ATOM   897  C C   . LEU A 1 140 ? 41.001 -0.262  18.684  1.000 35.294  ? 136 LEU A C   1 ? 1 
ATOM   898  O O   . LEU A 1 140 ? 40.589 0.926   18.854  1.000 35.241  ? 136 LEU A O   1 ? 1 
ATOM   899  C CB  . LEU A 1 140 ? 39.673 -2.206  19.605  1.000 36.466  ? 136 LEU A CB  1 ? 1 
ATOM   900  C CG  . LEU A 1 140 ? 38.836 -1.513  20.690  1.000 35.937  ? 136 LEU A CG  1 ? 1 
ATOM   901  C CD1 . LEU A 1 140 ? 37.433 -1.146  20.207  1.000 36.011  ? 136 LEU A CD1 1 ? 1 
ATOM   902  C CD2 . LEU A 1 140 ? 38.722 -2.403  21.917  1.000 37.977  ? 136 LEU A CD2 1 ? 1 
ATOM   903  N N   . THR A 1 141 ? 42.284 -0.617  18.731  1.000 34.191  ? 137 THR A N   1 ? 1 
ATOM   904  C CA  . THR A 1 141 ? 43.340 0.337   19.120  1.000 33.595  ? 137 THR A CA  1 ? 1 
ATOM   905  C C   . THR A 1 141 ? 43.296 1.514   18.152  1.000 33.261  ? 137 THR A C   1 ? 1 
ATOM   906  O O   . THR A 1 141 ? 43.483 2.637   18.629  1.000 31.900  ? 137 THR A O   1 ? 1 
ATOM   907  C CB  . THR A 1 141 ? 44.707 -0.331  19.238  1.000 33.859  ? 137 THR A CB  1 ? 1 
ATOM   908  O OG1 . THR A 1 141 ? 44.744 -1.215  20.362  1.000 34.147  ? 137 THR A OG1 1 ? 1 
ATOM   909  C CG2 . THR A 1 141 ? 45.797 0.681   19.437  1.000 34.684  ? 137 THR A CG2 1 ? 1 
ATOM   910  N N   . GLU A 1 142 ? 42.996 1.308   16.869  1.000 34.071  ? 138 GLU A N   1 ? 1 
ATOM   911  C CA  . GLU A 1 142 ? 43.025 2.438   15.898  1.000 37.748  ? 138 GLU A CA  1 ? 1 
ATOM   912  C C   . GLU A 1 142 ? 41.844 3.383   16.172  1.000 34.478  ? 138 GLU A C   1 ? 1 
ATOM   913  O O   . GLU A 1 142 ? 41.988 4.620   15.894  1.000 32.863  ? 138 GLU A O   1 ? 1 
ATOM   914  C CB  . GLU A 1 142 ? 43.048 1.970   14.423  1.000 45.602  ? 138 GLU A CB  1 ? 1 
ATOM   915  C CG  . GLU A 1 142 ? 44.404 1.486   13.913  1.000 49.440  ? 138 GLU A CG  1 ? 1 
ATOM   916  C CD  . GLU A 1 142 ? 45.552 2.475   14.153  1.000 58.256  ? 138 GLU A CD  1 ? 1 
ATOM   917  O OE1 . GLU A 1 142 ? 45.320 3.720   13.963  1.000 65.152  ? 138 GLU A OE1 1 ? 1 
ATOM   918  O OE2 . GLU A 1 142 ? 46.683 2.025   14.536  1.000 60.890  ? 138 GLU A OE2 1 ? 1 
ATOM   919  N N   . MET A 1 143 ? 40.700 2.840   16.619  1.000 32.408  ? 139 MET A N   1 ? 1 
ATOM   920  C CA  . MET A 1 143 ? 39.473 3.640   16.866  1.000 31.375  ? 139 MET A CA  1 ? 1 
ATOM   921  C C   . MET A 1 143 ? 39.711 4.469   18.130  1.000 30.065  ? 139 MET A C   1 ? 1 
ATOM   922  O O   . MET A 1 143 ? 39.224 5.599   18.204  1.000 27.206  ? 139 MET A O   1 ? 1 
ATOM   923  C CB  . MET A 1 143 ? 38.235 2.759   17.067  1.000 32.876  ? 139 MET A CB  1 ? 1 
ATOM   924  C CG  . MET A 1 143 ? 37.780 1.900   15.862  1.000 34.254  ? 139 MET A CG  1 ? 1 
ATOM   925  S SD  . MET A 1 143 ? 37.492 2.817   14.300  1.000 35.084  ? 139 MET A SD  1 ? 1 
ATOM   926  C CE  . MET A 1 143 ? 35.983 3.706   14.625  1.000 34.435  ? 139 MET A CE  1 ? 1 
ATOM   927  N N   . PHE A 1 144 ? 40.448 3.885   19.081  1.000 30.589  ? 140 PHE A N   1 ? 1 
ATOM   928  C CA  . PHE A 1 144 ? 40.942 4.515   20.336  1.000 30.654  ? 140 PHE A CA  1 ? 1 
ATOM   929  C C   . PHE A 1 144 ? 41.877 5.720   20.028  1.000 30.625  ? 140 PHE A C   1 ? 1 
ATOM   930  O O   . PHE A 1 144 ? 41.649 6.863   20.538  1.000 31.194  ? 140 PHE A O   1 ? 1 
ATOM   931  C CB  . PHE A 1 144 ? 41.554 3.399   21.188  1.000 30.995  ? 140 PHE A CB  1 ? 1 
ATOM   932  C CG  . PHE A 1 144 ? 42.321 3.877   22.391  1.000 34.168  ? 140 PHE A CG  1 ? 1 
ATOM   933  C CD1 . PHE A 1 144 ? 43.694 4.010   22.357  1.000 34.938  ? 140 PHE A CD1 1 ? 1 
ATOM   934  C CD2 . PHE A 1 144 ? 41.663 4.216   23.565  1.000 35.396  ? 140 PHE A CD2 1 ? 1 
ATOM   935  C CE1 . PHE A 1 144 ? 44.393 4.389   23.493  1.000 36.369  ? 140 PHE A CE1 1 ? 1 
ATOM   936  C CE2 . PHE A 1 144 ? 42.358 4.647   24.680  1.000 33.976  ? 140 PHE A CE2 1 ? 1 
ATOM   937  C CZ  . PHE A 1 144 ? 43.724 4.757   24.637  1.000 34.459  ? 140 PHE A CZ  1 ? 1 
ATOM   938  N N   . TYR A 1 145 ? 42.926 5.540   19.211  1.000 28.608  ? 141 TYR A N   1 ? 1 
ATOM   939  C CA  . TYR A 1 145 ? 43.831 6.662   18.843  1.000 27.392  ? 141 TYR A CA  1 ? 1 
ATOM   940  C C   . TYR A 1 145 ? 43.026 7.774   18.168  1.000 25.743  ? 141 TYR A C   1 ? 1 
ATOM   941  O O   . TYR A 1 145 ? 43.239 8.927   18.412  1.000 25.954  ? 141 TYR A O   1 ? 1 
ATOM   942  C CB  . TYR A 1 145 ? 44.960 6.202   17.919  1.000 29.380  ? 141 TYR A CB  1 ? 1 
ATOM   943  C CG  . TYR A 1 145 ? 45.966 5.257   18.532  1.000 30.362  ? 141 TYR A CG  1 ? 1 
ATOM   944  C CD1 . TYR A 1 145 ? 46.276 5.317   19.883  1.000 31.247  ? 141 TYR A CD1 1 ? 1 
ATOM   945  C CD2 . TYR A 1 145 ? 46.569 4.279   17.756  1.000 30.711  ? 141 TYR A CD2 1 ? 1 
ATOM   946  C CE1 . TYR A 1 145 ? 47.180 4.437   20.445  1.000 33.082  ? 141 TYR A CE1 1 ? 1 
ATOM   947  C CE2 . TYR A 1 145 ? 47.463 3.385   18.305  1.000 31.344  ? 141 TYR A CE2 1 ? 1 
ATOM   948  C CZ  . TYR A 1 145 ? 47.775 3.481   19.644  1.000 33.319  ? 141 TYR A CZ  1 ? 1 
ATOM   949  O OH  . TYR A 1 145 ? 48.654 2.607   20.183  1.000 36.323  ? 141 TYR A OH  1 ? 1 
ATOM   950  N N   . GLU A 1 146 ? 42.066 7.421   17.356  1.000 24.743  ? 142 GLU A N   1 ? 1 
ATOM   951  C CA  . GLU A 1 146 ? 41.137 8.398   16.746  1.000 26.200  ? 142 GLU A CA  1 ? 1 
ATOM   952  C C   . GLU A 1 146 ? 40.423 9.223   17.822  1.000 26.884  ? 142 GLU A C   1 ? 1 
ATOM   953  O O   . GLU A 1 146 ? 40.430 10.441  17.717  1.000 27.175  ? 142 GLU A O   1 ? 1 
ATOM   954  C CB  . GLU A 1 146 ? 40.209 7.625   15.803  1.000 27.440  ? 142 GLU A CB  1 ? 1 
ATOM   955  C CG  . GLU A 1 146 ? 39.007 8.386   15.286  1.000 27.012  ? 142 GLU A CG  1 ? 1 
ATOM   956  C CD  . GLU A 1 146 ? 39.279 9.727   14.629  1.000 26.893  ? 142 GLU A CD  1 ? 1 
ATOM   957  O OE1 . GLU A 1 146 ? 40.467 10.086  14.336  1.000 26.481  ? 142 GLU A OE1 1 ? 1 
ATOM   958  O OE2 . GLU A 1 146 ? 38.284 10.429  14.459  1.000 26.418  ? 142 GLU A OE2 1 ? 1 
ATOM   959  N N   . LEU A 1 147 ? 39.865 8.594   18.860  1.000 29.433  ? 143 LEU A N   1 ? 1 
ATOM   960  C CA  . LEU A 1 147 ? 39.335 9.294   20.077  1.000 26.422  ? 143 LEU A CA  1 ? 1 
ATOM   961  C C   . LEU A 1 147 ? 40.487 10.084  20.682  1.000 24.186  ? 143 LEU A C   1 ? 1 
ATOM   962  O O   . LEU A 1 147 ? 40.255 11.220  21.020  1.000 23.772  ? 143 LEU A O   1 ? 1 
ATOM   963  C CB  . LEU A 1 147 ? 38.701 8.307   21.077  1.000 27.155  ? 143 LEU A CB  1 ? 1 
ATOM   964  C CG  . LEU A 1 147 ? 37.972 8.973   22.268  1.000 28.535  ? 143 LEU A CG  1 ? 1 
ATOM   965  C CD1 . LEU A 1 147 ? 36.726 9.761   21.837  1.000 28.817  ? 143 LEU A CD1 1 ? 1 
ATOM   966  C CD2 . LEU A 1 147 ? 37.577 7.959   23.333  1.000 27.288  ? 143 LEU A CD2 1 ? 1 
ATOM   967  N N   . GLY A 1 148 ? 41.700 9.557   20.694  1.000 22.788  ? 144 GLY A N   1 ? 1 
ATOM   968  C CA  . GLY A 1 148 ? 42.832 10.290  21.289  1.000 23.819  ? 144 GLY A CA  1 ? 1 
ATOM   969  C C   . GLY A 1 148 ? 43.090 11.688  20.700  1.000 25.400  ? 144 GLY A C   1 ? 1 
ATOM   970  O O   . GLY A 1 148 ? 43.799 12.512  21.313  1.000 23.360  ? 144 GLY A O   1 ? 1 
ATOM   971  N N   . ARG A 1 149 ? 42.622 11.958  19.469  1.000 28.300  ? 145 ARG A N   1 ? 1 
ATOM   972  C CA  . ARG A 1 149 ? 42.833 13.267  18.790  1.000 28.076  ? 145 ARG A CA  1 ? 1 
ATOM   973  C C   . ARG A 1 149 ? 42.098 14.351  19.564  1.000 27.691  ? 145 ARG A C   1 ? 1 
ATOM   974  O O   . ARG A 1 149 ? 42.361 15.481  19.291  1.000 27.615  ? 145 ARG A O   1 ? 1 
ATOM   975  C CB  . ARG A 1 149 ? 42.291 13.268  17.360  1.000 29.817  ? 145 ARG A CB  1 ? 1 
ATOM   976  C CG  . ARG A 1 149 ? 43.161 12.574  16.301  1.000 30.482  ? 145 ARG A CG  1 ? 1 
ATOM   977  C CD  . ARG A 1 149 ? 42.445 12.335  14.981  1.000 30.286  ? 145 ARG A CD  1 ? 1 
ATOM   978  N NE  . ARG A 1 149 ? 41.790 13.565  14.611  1.000 31.004  ? 145 ARG A NE  1 ? 1 
ATOM   979  C CZ  . ARG A 1 149 ? 40.516 13.703  14.300  1.000 31.175  ? 145 ARG A CZ  1 ? 1 
ATOM   980  N NH1 . ARG A 1 149 ? 39.693 12.674  14.172  1.000 30.635  ? 145 ARG A NH1 1 ? 1 
ATOM   981  N NH2 . ARG A 1 149 ? 40.096 14.928  14.090  1.000 32.074  ? 145 ARG A NH2 1 ? 1 
ATOM   982  N N   . PHE A 1 150 ? 41.161 14.005  20.451  1.000 27.790  ? 146 PHE A N   1 ? 1 
ATOM   983  C CA  . PHE A 1 150 ? 40.324 14.980  21.207  1.000 27.355  ? 146 PHE A CA  1 ? 1 
ATOM   984  C C   . PHE A 1 150 ? 40.858 15.249  22.610  1.000 28.249  ? 146 PHE A C   1 ? 1 
ATOM   985  O O   . PHE A 1 150 ? 40.249 15.960  23.376  1.000 29.041  ? 146 PHE A O   1 ? 1 
ATOM   986  C CB  . PHE A 1 150 ? 38.919 14.443  21.233  1.000 27.056  ? 146 PHE A CB  1 ? 1 
ATOM   987  C CG  . PHE A 1 150 ? 38.381 14.445  19.848  1.000 26.811  ? 146 PHE A CG  1 ? 1 
ATOM   988  C CD1 . PHE A 1 150 ? 37.977 15.639  19.268  1.000 28.227  ? 146 PHE A CD1 1 ? 1 
ATOM   989  C CD2 . PHE A 1 150 ? 38.419 13.301  19.083  1.000 26.788  ? 146 PHE A CD2 1 ? 1 
ATOM   990  C CE1 . PHE A 1 150 ? 37.619 15.680  17.923  1.000 28.364  ? 146 PHE A CE1 1 ? 1 
ATOM   991  C CE2 . PHE A 1 150 ? 38.053 13.339  17.740  1.000 26.549  ? 146 PHE A CE2 1 ? 1 
ATOM   992  C CZ  . PHE A 1 150 ? 37.609 14.517  17.180  1.000 26.707  ? 146 PHE A CZ  1 ? 1 
ATOM   993  N N   . VAL A 1 151 ? 42.017 14.716  22.934  1.000 29.089  ? 147 VAL A N   1 ? 1 
ATOM   994  C CA  . VAL A 1 151 ? 42.705 15.021  24.203  1.000 30.067  ? 147 VAL A CA  1 ? 1 
ATOM   995  C C   . VAL A 1 151 ? 42.986 16.515  24.237  1.000 31.426  ? 147 VAL A C   1 ? 1 
ATOM   996  O O   . VAL A 1 151 ? 43.440 17.018  23.243  1.000 32.456  ? 147 VAL A O   1 ? 1 
ATOM   997  C CB  . VAL A 1 151 ? 43.981 14.173  24.293  1.000 30.695  ? 147 VAL A CB  1 ? 1 
ATOM   998  C CG1 . VAL A 1 151 ? 44.969 14.688  25.328  1.000 31.267  ? 147 VAL A CG1 1 ? 1 
ATOM   999  C CG2 . VAL A 1 151 ? 43.591 12.724  24.568  1.000 30.925  ? 147 VAL A CG2 1 ? 1 
ATOM   1000 N N   . VAL A 1 152 ? 42.713 17.179  25.362  1.000 34.482  ? 148 VAL A N   1 ? 1 
ATOM   1001 C CA  . VAL A 1 152 ? 43.091 18.605  25.651  1.000 36.936  ? 148 VAL A CA  1 ? 1 
ATOM   1002 C C   . VAL A 1 152 ? 44.239 18.690  26.676  1.000 39.142  ? 148 VAL A C   1 ? 1 
ATOM   1003 O O   . VAL A 1 152 ? 44.364 17.780  27.558  1.000 36.465  ? 148 VAL A O   1 ? 1 
ATOM   1004 C CB  . VAL A 1 152 ? 41.861 19.399  26.124  1.000 38.224  ? 148 VAL A CB  1 ? 1 
ATOM   1005 C CG1 . VAL A 1 152 ? 40.707 19.240  25.160  1.000 40.383  ? 148 VAL A CG1 1 ? 1 
ATOM   1006 C CG2 . VAL A 1 152 ? 41.391 18.994  27.505  1.000 39.415  ? 148 VAL A CG2 1 ? 1 
ATOM   1007 N N   . ASP A 1 153 ? 45.018 19.774  26.607  1.000 45.347  ? 149 ASP A N   1 ? 1 
ATOM   1008 C CA  . ASP A 1 153 ? 46.073 20.108  27.611  1.000 52.423  ? 149 ASP A CA  1 ? 1 
ATOM   1009 C C   . ASP A 1 153 ? 45.463 21.022  28.677  1.000 49.649  ? 149 ASP A C   1 ? 1 
ATOM   1010 O O   . ASP A 1 153 ? 45.807 20.796  29.859  1.000 54.376  ? 149 ASP A O   1 ? 1 
ATOM   1011 C CB  . ASP A 1 153 ? 47.365 20.602  26.938  1.000 59.199  ? 149 ASP A CB  1 ? 1 
ATOM   1012 C CG  . ASP A 1 153 ? 47.985 19.529  26.047  1.000 62.196  ? 149 ASP A CG  1 ? 1 
ATOM   1013 O OD1 . ASP A 1 153 ? 49.042 18.944  26.431  1.000 65.097  ? 149 ASP A OD1 1 ? 1 
ATOM   1014 O OD2 . ASP A 1 153 ? 47.375 19.232  24.995  1.000 66.225  ? 149 ASP A OD2 1 ? 1 
ATOM   1015 N N   . GLY A 1 154 ? 44.528 21.909  28.305  1.000 46.868  ? 150 GLY A N   1 ? 1 
ATOM   1016 C CA  . GLY A 1 154 ? 43.737 22.742  29.244  1.000 48.690  ? 150 GLY A CA  1 ? 1 
ATOM   1017 C C   . GLY A 1 154 ? 43.028 21.977  30.392  1.000 47.406  ? 150 GLY A C   1 ? 1 
ATOM   1018 O O   . GLY A 1 154 ? 42.927 20.743  30.334  1.000 49.069  ? 150 GLY A O   1 ? 1 
ATOM   1019 N N   . THR A 1 155 ? 42.544 22.698  31.407  1.000 43.490  ? 151 THR A N   1 ? 1 
ATOM   1020 C CA  . THR A 1 155 ? 41.301 22.398  32.174  1.000 43.125  ? 151 THR A CA  1 ? 1 
ATOM   1021 C C   . THR A 1 155 ? 40.291 23.541  31.979  1.000 45.831  ? 151 THR A C   1 ? 1 
ATOM   1022 O O   . THR A 1 155 ? 39.177 23.451  32.506  1.000 46.922  ? 151 THR A O   1 ? 1 
ATOM   1023 C CB  . THR A 1 155 ? 41.567 22.141  33.675  1.000 40.772  ? 151 THR A CB  1 ? 1 
ATOM   1024 O OG1 . THR A 1 155 ? 42.077 23.280  34.363  1.000 36.992  ? 151 THR A OG1 1 ? 1 
ATOM   1025 C CG2 . THR A 1 155 ? 42.534 20.998  33.887  1.000 39.993  ? 151 THR A CG2 1 ? 1 
ATOM   1026 N N   . LYS A 1 156 ? 40.678 24.601  31.280  1.000 52.346  ? 152 LYS A N   1 ? 1 
ATOM   1027 C CA  . LYS A 1 156 ? 39.812 25.723  30.831  1.000 57.487  ? 152 LYS A CA  1 ? 1 
ATOM   1028 C C   . LYS A 1 156 ? 39.252 25.246  29.497  1.000 57.457  ? 152 LYS A C   1 ? 1 
ATOM   1029 O O   . LYS A 1 156 ? 40.070 24.931  28.618  1.000 63.587  ? 152 LYS A O   1 ? 1 
ATOM   1030 C CB  . LYS A 1 156 ? 40.672 26.993  30.729  1.000 62.319  ? 152 LYS A CB  1 ? 1 
ATOM   1031 C CG  . LYS A 1 156 ? 41.241 27.474  32.077  1.000 66.919  ? 152 LYS A CG  1 ? 1 
ATOM   1032 C CD  . LYS A 1 156 ? 42.702 27.964  32.064  1.000 69.653  ? 152 LYS A CD  1 ? 1 
ATOM   1033 C CE  . LYS A 1 156 ? 42.989 29.140  31.149  1.000 70.357  ? 152 LYS A CE  1 ? 1 
ATOM   1034 N NZ  . LYS A 1 156 ? 43.892 30.111  31.810  1.000 72.256  ? 152 LYS A NZ  1 ? 1 
ATOM   1035 N N   . GLY A 1 157 ? 37.954 25.003  29.407  1.000 51.730  ? 153 GLY A N   1 ? 1 
ATOM   1036 C CA  . GLY A 1 157 ? 37.413 24.192  28.304  1.000 49.242  ? 153 GLY A CA  1 ? 1 
ATOM   1037 C C   . GLY A 1 157 ? 36.385 23.205  28.804  1.000 49.206  ? 153 GLY A C   1 ? 1 
ATOM   1038 O O   . GLY A 1 157 ? 36.621 22.636  29.915  1.000 49.594  ? 153 GLY A O   1 ? 1 
ATOM   1039 N N   . GLU A 1 158 ? 35.279 23.042  28.052  1.000 46.678  ? 154 GLU A N   1 ? 1 
ATOM   1040 C CA  . GLU A 1 158 ? 34.234 22.011  28.322  1.000 47.435  ? 154 GLU A CA  1 ? 1 
ATOM   1041 C C   . GLU A 1 158 ? 34.910 20.669  28.007  1.000 40.599  ? 154 GLU A C   1 ? 1 
ATOM   1042 O O   . GLU A 1 158 ? 35.701 20.664  27.060  1.000 39.931  ? 154 GLU A O   1 ? 1 
ATOM   1043 C CB  . GLU A 1 158 ? 32.904 22.239  27.575  1.000 53.721  ? 154 GLU A CB  1 ? 1 
ATOM   1044 C CG  . GLU A 1 158 ? 32.186 23.583  27.857  1.000 61.972  ? 154 GLU A CG  1 ? 1 
ATOM   1045 C CD  . GLU A 1 158 ? 31.532 23.861  29.227  1.000 70.852  ? 154 GLU A CD  1 ? 1 
ATOM   1046 O OE1 . GLU A 1 158 ? 31.310 25.089  29.602  1.000 70.865  ? 154 GLU A OE1 1 ? 1 
ATOM   1047 O OE2 . GLU A 1 158 ? 31.210 22.866  29.933  1.000 81.125  ? 154 GLU A OE2 1 ? 1 
ATOM   1048 N N   . GLN A 1 159 ? 34.654 19.628  28.821  1.000 34.583  ? 155 GLN A N   1 ? 1 
ATOM   1049 C CA  . GLN A 1 159 ? 35.272 18.279  28.799  1.000 31.093  ? 155 GLN A CA  1 ? 1 
ATOM   1050 C C   . GLN A 1 159 ? 34.213 17.196  28.634  1.000 29.393  ? 155 GLN A C   1 ? 1 
ATOM   1051 O O   . GLN A 1 159 ? 33.153 17.365  29.209  1.000 29.649  ? 155 GLN A O   1 ? 1 
ATOM   1052 C CB  . GLN A 1 159 ? 36.016 18.067  30.109  1.000 30.268  ? 155 GLN A CB  1 ? 1 
ATOM   1053 C CG  . GLN A 1 159 ? 37.066 19.134  30.320  1.000 30.588  ? 155 GLN A CG  1 ? 1 
ATOM   1054 C CD  . GLN A 1 159 ? 37.396 19.386  31.762  1.000 29.899  ? 155 GLN A CD  1 ? 1 
ATOM   1055 O OE1 . GLN A 1 159 ? 36.924 18.691  32.642  1.000 29.247  ? 155 GLN A OE1 1 ? 1 
ATOM   1056 N NE2 . GLN A 1 159 ? 38.260 20.364  31.987  1.000 30.415  ? 155 GLN A NE2 1 ? 1 
ATOM   1057 N N   . GLY A 1 160 ? 34.517 16.122  27.894  1.000 28.054  ? 156 GLY A N   1 ? 1 
ATOM   1058 C CA  . GLY A 1 160 ? 33.580 15.032  27.557  1.000 26.815  ? 156 GLY A CA  1 ? 1 
ATOM   1059 C C   . GLY A 1 160 ? 33.963 13.745  28.274  1.000 27.199  ? 156 GLY A C   1 ? 1 
ATOM   1060 O O   . GLY A 1 160 ? 33.314 12.691  28.053  1.000 28.279  ? 156 GLY A O   1 ? 1 
ATOM   1061 N N   . GLY A 1 161 ? 34.979 13.795  29.138  1.000 26.310  ? 157 GLY A N   1 ? 1 
ATOM   1062 C CA  . GLY A 1 161 ? 35.494 12.583  29.794  1.000 25.073  ? 157 GLY A CA  1 ? 1 
ATOM   1063 C C   . GLY A 1 161 ? 37.005 12.494  29.810  1.000 23.980  ? 157 GLY A C   1 ? 1 
ATOM   1064 O O   . GLY A 1 161 ? 37.695 13.538  29.736  1.000 23.114  ? 157 GLY A O   1 ? 1 
ATOM   1065 N N   . PHE A 1 162 ? 37.501 11.271  30.002  1.000 23.543  ? 158 PHE A N   1 ? 1 
ATOM   1066 C CA  . PHE A 1 162 ? 38.954 11.043  30.124  1.000 23.762  ? 158 PHE A CA  1 ? 1 
ATOM   1067 C C   . PHE A 1 162 ? 39.374 9.692   29.598  1.000 23.676  ? 158 PHE A C   1 ? 1 
ATOM   1068 O O   . PHE A 1 162 ? 38.524 8.836   29.386  1.000 23.394  ? 158 PHE A O   1 ? 1 
ATOM   1069 C CB  . PHE A 1 162 ? 39.390 11.147  31.577  1.000 24.052  ? 158 PHE A CB  1 ? 1 
ATOM   1070 C CG  . PHE A 1 162 ? 38.754 10.170  32.523  1.000 24.235  ? 158 PHE A CG  1 ? 1 
ATOM   1071 C CD1 . PHE A 1 162 ? 37.666 10.552  33.302  1.000 23.346  ? 158 PHE A CD1 1 ? 1 
ATOM   1072 C CD2 . PHE A 1 162 ? 39.329 8.922   32.735  1.000 24.148  ? 158 PHE A CD2 1 ? 1 
ATOM   1073 C CE1 . PHE A 1 162 ? 37.079 9.655   34.166  1.000 23.016  ? 158 PHE A CE1 1 ? 1 
ATOM   1074 C CE2 . PHE A 1 162 ? 38.729 8.028   33.613  1.000 23.806  ? 158 PHE A CE2 1 ? 1 
ATOM   1075 C CZ  . PHE A 1 162 ? 37.601 8.402   34.319  1.000 23.558  ? 158 PHE A CZ  1 ? 1 
ATOM   1076 N N   . ILE A 1 163 ? 40.684 9.535   29.482  1.000 23.989  ? 159 ILE A N   1 ? 1 
ATOM   1077 C CA  . ILE A 1 163 ? 41.349 8.258   29.128  1.000 25.035  ? 159 ILE A CA  1 ? 1 
ATOM   1078 C C   . ILE A 1 163 ? 42.437 7.974   30.158  1.000 26.164  ? 159 ILE A C   1 ? 1 
ATOM   1079 O O   . ILE A 1 163 ? 43.313 8.867   30.371  1.000 25.152  ? 159 ILE A O   1 ? 1 
ATOM   1080 C CB  . ILE A 1 163 ? 41.980 8.412   27.739  1.000 25.345  ? 159 ILE A CB  1 ? 1 
ATOM   1081 C CG1 . ILE A 1 163 ? 40.889 8.651   26.686  1.000 25.992  ? 159 ILE A CG1 1 ? 1 
ATOM   1082 C CG2 . ILE A 1 163 ? 42.880 7.232   27.424  1.000 24.704  ? 159 ILE A CG2 1 ? 1 
ATOM   1083 C CD1 . ILE A 1 163 ? 41.374 8.602   25.246  1.000 25.915  ? 159 ILE A CD1 1 ? 1 
ATOM   1084 N N   . SER A 1 164 ? 42.448 6.775   30.720  1.000 27.404  ? 160 SER A N   1 ? 1 
ATOM   1085 C CA  . SER A 1 164 ? 43.579 6.344   31.575  1.000 30.456  ? 160 SER A CA  1 ? 1 
ATOM   1086 C C   . SER A 1 164 ? 44.421 5.359   30.750  1.000 29.087  ? 160 SER A C   1 ? 1 
ATOM   1087 O O   . SER A 1 164 ? 43.819 4.550   30.098  1.000 26.839  ? 160 SER A O   1 ? 1 
ATOM   1088 C CB  . SER A 1 164 ? 43.119 5.811   32.972  1.000 31.518  ? 160 SER A CB  1 ? 1 
ATOM   1089 O OG  . SER A 1 164 ? 43.725 4.546   33.278  1.000 34.801  ? 160 SER A OG  1 ? 1 
ATOM   1090 N N   . ILE A 1 165 ? 45.746 5.438   30.869  1.000 29.761  ? 161 ILE A N   1 ? 1 
ATOM   1091 C CA  . ILE A 1 165 ? 46.751 4.491   30.326  1.000 30.793  ? 161 ILE A CA  1 ? 1 
ATOM   1092 C C   . ILE A 1 165 ? 47.484 3.792   31.475  1.000 32.465  ? 161 ILE A C   1 ? 1 
ATOM   1093 O O   . ILE A 1 165 ? 48.099 4.475   32.304  1.000 35.508  ? 161 ILE A O   1 ? 1 
ATOM   1094 C CB  . ILE A 1 165 ? 47.764 5.229   29.434  1.000 31.979  ? 161 ILE A CB  1 ? 1 
ATOM   1095 C CG1 . ILE A 1 165 ? 47.085 6.007   28.298  1.000 32.646  ? 161 ILE A CG1 1 ? 1 
ATOM   1096 C CG2 . ILE A 1 165 ? 48.775 4.231   28.872  1.000 31.693  ? 161 ILE A CG2 1 ? 1 
ATOM   1097 C CD1 . ILE A 1 165 ? 46.177 5.160   27.452  1.000 32.594  ? 161 ILE A CD1 1 ? 1 
ATOM   1098 N N   . ASP A 1 166 ? 47.490 2.467   31.469  1.000 34.253  ? 162 ASP A N   1 ? 1 
ATOM   1099 C CA  . ASP A 1 166 ? 48.348 1.607   32.327  1.000 35.901  ? 162 ASP A CA  1 ? 1 
ATOM   1100 C C   . ASP A 1 166 ? 48.130 1.981   33.809  1.000 35.936  ? 162 ASP A C   1 ? 1 
ATOM   1101 O O   . ASP A 1 166 ? 49.050 1.919   34.589  1.000 34.705  ? 162 ASP A O   1 ? 1 
ATOM   1102 C CB  . ASP A 1 166 ? 49.791 1.681   31.829  1.000 37.032  ? 162 ASP A CB  1 ? 1 
ATOM   1103 C CG  . ASP A 1 166 ? 50.073 0.993   30.492  1.000 40.155  ? 162 ASP A CG  1 ? 1 
ATOM   1104 O OD1 . ASP A 1 166 ? 49.202 0.187   30.017  1.000 39.914  ? 162 ASP A OD1 1 ? 1 
ATOM   1105 O OD2 . ASP A 1 166 ? 51.176 1.272   29.915  1.000 41.582  ? 162 ASP A OD2 1 ? 1 
ATOM   1106 N N   . GLU A 1 167 ? 46.927 2.398   34.170  1.000 38.971  ? 163 GLU A N   1 ? 1 
ATOM   1107 C CA  . GLU A 1 167 ? 46.537 2.762   35.570  1.000 41.407  ? 163 GLU A CA  1 ? 1 
ATOM   1108 C C   . GLU A 1 167 ? 47.452 3.854   36.135  1.000 41.397  ? 163 GLU A C   1 ? 1 
ATOM   1109 O O   . GLU A 1 167 ? 47.440 3.972   37.337  1.000 41.636  ? 163 GLU A O   1 ? 1 
ATOM   1110 C CB  . GLU A 1 167 ? 46.501 1.530   36.491  1.000 40.873  ? 163 GLU A CB  1 ? 1 
ATOM   1111 C CG  . GLU A 1 167 ? 45.393 0.555   36.099  1.000 42.483  ? 163 GLU A CG  1 ? 1 
ATOM   1112 C CD  . GLU A 1 167 ? 45.051 -0.594  37.047  1.000 43.786  ? 163 GLU A CD  1 ? 1 
ATOM   1113 O OE1 . GLU A 1 167 ? 44.002 -0.536  37.729  1.000 43.318  ? 163 GLU A OE1 1 ? 1 
ATOM   1114 O OE2 . GLU A 1 167 ? 45.807 -1.587  37.070  1.000 47.369  ? 163 GLU A OE2 1 ? 1 
ATOM   1115 N N   . ARG A 1 168 ? 48.185 4.613   35.308  1.000 41.145  ? 164 ARG A N   1 ? 1 
ATOM   1116 C CA  A ARG A 1 168 ? 49.137 5.666   35.766  0.500 40.388  ? 164 ARG A CA  1 ? 1 
ATOM   1117 C CA  B ARG A 1 168 ? 49.145 5.665   35.756  0.500 41.601  ? 164 ARG A CA  1 ? 1 
ATOM   1118 C C   . ARG A 1 168 ? 48.644 7.033   35.270  1.000 42.526  ? 164 ARG A C   1 ? 1 
ATOM   1119 O O   . ARG A 1 168 ? 48.324 7.865   36.073  1.000 47.909  ? 164 ARG A O   1 ? 1 
ATOM   1120 C CB  A ARG A 1 168 ? 50.552 5.379   35.250  0.500 38.734  ? 164 ARG A CB  1 ? 1 
ATOM   1121 C CB  B ARG A 1 168 ? 50.545 5.449   35.168  0.500 41.450  ? 164 ARG A CB  1 ? 1 
ATOM   1122 C CG  A ARG A 1 168 ? 51.540 4.904   36.309  0.500 37.310  ? 164 ARG A CG  1 ? 1 
ATOM   1123 C CG  B ARG A 1 168 ? 51.410 4.397   35.846  0.500 41.298  ? 164 ARG A CG  1 ? 1 
ATOM   1124 C CD  A ARG A 1 168 ? 52.537 5.992   36.577  0.500 35.042  ? 164 ARG A CD  1 ? 1 
ATOM   1125 C CD  B ARG A 1 168 ? 52.189 4.925   37.039  0.500 39.169  ? 164 ARG A CD  1 ? 1 
ATOM   1126 N NE  A ARG A 1 168 ? 52.821 6.047   37.982  0.500 33.720  ? 164 ARG A NE  1 ? 1 
ATOM   1127 N NE  B ARG A 1 168 ? 52.386 3.821   37.947  0.500 38.564  ? 164 ARG A NE  1 ? 1 
ATOM   1128 C CZ  A ARG A 1 168 ? 53.461 7.043   38.569  0.500 32.245  ? 164 ARG A CZ  1 ? 1 
ATOM   1129 C CZ  B ARG A 1 168 ? 51.405 3.231   38.622  0.500 38.562  ? 164 ARG A CZ  1 ? 1 
ATOM   1130 N NH1 A ARG A 1 168 ? 53.871 8.069   37.841  0.500 30.411  ? 164 ARG A NH1 1 ? 1 
ATOM   1131 N NH1 B ARG A 1 168 ? 50.170 3.649   38.483  0.500 38.933  ? 164 ARG A NH1 1 ? 1 
ATOM   1132 N NH2 A ARG A 1 168 ? 53.673 6.982   39.878  0.500 32.275  ? 164 ARG A NH2 1 ? 1 
ATOM   1133 N NH2 B ARG A 1 168 ? 51.635 2.225   39.437  0.500 38.808  ? 164 ARG A NH2 1 ? 1 
ATOM   1134 N N   . ASP A 1 169 ? 48.576 7.226   33.962  1.000 41.677  ? 165 ASP A N   1 ? 1 
ATOM   1135 C CA  . ASP A 1 169 ? 48.336 8.559   33.376  1.000 39.100  ? 165 ASP A CA  1 ? 1 
ATOM   1136 C C   . ASP A 1 169 ? 46.869 8.663   33.017  1.000 34.705  ? 165 ASP A C   1 ? 1 
ATOM   1137 O O   . ASP A 1 169 ? 46.297 7.651   32.577  1.000 32.282  ? 165 ASP A O   1 ? 1 
ATOM   1138 C CB  . ASP A 1 169 ? 49.264 8.791   32.185  1.000 40.040  ? 165 ASP A CB  1 ? 1 
ATOM   1139 C CG  . ASP A 1 169 ? 50.668 8.953   32.690  1.000 42.660  ? 165 ASP A CG  1 ? 1 
ATOM   1140 O OD1 . ASP A 1 169 ? 50.814 9.750   33.630  1.000 44.757  ? 165 ASP A OD1 1 ? 1 
ATOM   1141 O OD2 . ASP A 1 169 ? 51.579 8.271   32.168  1.000 46.398  ? 165 ASP A OD2 1 ? 1 
ATOM   1142 N N   . VAL A 1 170 ? 46.347 9.884   33.137  1.000 31.751  ? 166 VAL A N   1 ? 1 
ATOM   1143 C CA  . VAL A 1 170 ? 44.941 10.235  32.837  1.000 29.760  ? 166 VAL A CA  1 ? 1 
ATOM   1144 C C   . VAL A 1 170 ? 44.862 11.506  31.987  1.000 27.413  ? 166 VAL A C   1 ? 1 
ATOM   1145 O O   . VAL A 1 170 ? 45.311 12.549  32.436  1.000 27.444  ? 166 VAL A O   1 ? 1 
ATOM   1146 C CB  . VAL A 1 170 ? 44.150 10.425  34.139  1.000 30.421  ? 166 VAL A CB  1 ? 1 
ATOM   1147 C CG1 . VAL A 1 170 ? 42.681 10.726  33.811  1.000 31.408  ? 166 VAL A CG1 1 ? 1 
ATOM   1148 C CG2 . VAL A 1 170 ? 44.269 9.225   35.067  1.000 30.016  ? 166 VAL A CG2 1 ? 1 
ATOM   1149 N N   . TYR A 1 171 ? 44.169 11.456  30.863  1.000 25.599  ? 167 TYR A N   1 ? 1 
ATOM   1150 C CA  . TYR A 1 171 ? 44.070 12.626  29.973  1.000 25.537  ? 167 TYR A CA  1 ? 1 
ATOM   1151 C C   . TYR A 1 171 ? 42.615 12.946  29.856  1.000 25.170  ? 167 TYR A C   1 ? 1 
ATOM   1152 O O   . TYR A 1 171 ? 41.869 11.988  29.771  1.000 25.015  ? 167 TYR A O   1 ? 1 
ATOM   1153 C CB  . TYR A 1 171 ? 44.623 12.309  28.588  1.000 25.665  ? 167 TYR A CB  1 ? 1 
ATOM   1154 C CG  . TYR A 1 171 ? 46.051 11.874  28.593  1.000 24.968  ? 167 TYR A CG  1 ? 1 
ATOM   1155 C CD1 . TYR A 1 171 ? 47.067 12.793  28.426  1.000 26.384  ? 167 TYR A CD1 1 ? 1 
ATOM   1156 C CD2 . TYR A 1 171 ? 46.375 10.567  28.835  1.000 24.289  ? 167 TYR A CD2 1 ? 1 
ATOM   1157 C CE1 . TYR A 1 171 ? 48.403 12.402  28.433  1.000 27.011  ? 167 TYR A CE1 1 ? 1 
ATOM   1158 C CE2 . TYR A 1 171 ? 47.695 10.155  28.870  1.000 25.550  ? 167 TYR A CE2 1 ? 1 
ATOM   1159 C CZ  . TYR A 1 171 ? 48.710 11.079  28.667  1.000 26.468  ? 167 TYR A CZ  1 ? 1 
ATOM   1160 O OH  . TYR A 1 171 ? 50.004 10.687  28.697  1.000 28.362  ? 167 TYR A OH  1 ? 1 
ATOM   1161 N N   . LEU A 1 172 ? 42.270 14.214  29.851  1.000 26.123  ? 168 LEU A N   1 ? 1 
ATOM   1162 C CA  . LEU A 1 172 ? 40.868 14.670  29.678  1.000 27.782  ? 168 LEU A CA  1 ? 1 
ATOM   1163 C C   . LEU A 1 172 ? 40.534 14.808  28.173  1.000 27.350  ? 168 LEU A C   1 ? 1 
ATOM   1164 O O   . LEU A 1 172 ? 41.394 15.253  27.410  1.000 26.262  ? 168 LEU A O   1 ? 1 
ATOM   1165 C CB  . LEU A 1 172 ? 40.751 16.019  30.384  1.000 28.622  ? 168 LEU A CB  1 ? 1 
ATOM   1166 C CG  . LEU A 1 172 ? 41.199 15.987  31.831  1.000 29.186  ? 168 LEU A CG  1 ? 1 
ATOM   1167 C CD1 . LEU A 1 172 ? 41.437 17.382  32.355  1.000 29.247  ? 168 LEU A CD1 1 ? 1 
ATOM   1168 C CD2 . LEU A 1 172 ? 40.175 15.213  32.647  1.000 29.665  ? 168 LEU A CD2 1 ? 1 
ATOM   1169 N N   . LEU A 1 173 ? 39.297 14.493  27.795  1.000 27.508  ? 169 LEU A N   1 ? 1 
ATOM   1170 C CA  . LEU A 1 173 ? 38.757 14.639  26.423  1.000 27.612  ? 169 LEU A CA  1 ? 1 
ATOM   1171 C C   . LEU A 1 173 ? 37.922 15.912  26.335  1.000 28.532  ? 169 LEU A C   1 ? 1 
ATOM   1172 O O   . LEU A 1 173 ? 37.243 16.245  27.358  1.000 28.369  ? 169 LEU A O   1 ? 1 
ATOM   1173 C CB  . LEU A 1 173 ? 37.906 13.409  26.129  1.000 27.064  ? 169 LEU A CB  1 ? 1 
ATOM   1174 C CG  . LEU A 1 173 ? 38.729 12.145  25.956  1.000 27.294  ? 169 LEU A CG  1 ? 1 
ATOM   1175 C CD1 . LEU A 1 173 ? 37.864 10.911  25.855  1.000 27.108  ? 169 LEU A CD1 1 ? 1 
ATOM   1176 C CD2 . LEU A 1 173 ? 39.606 12.244  24.722  1.000 28.589  ? 169 LEU A CD2 1 ? 1 
ATOM   1177 N N   . ALA A 1 174 ? 37.948 16.571  25.164  1.000 29.305  ? 170 ALA A N   1 ? 1 
ATOM   1178 C CA  . ALA A 1 174 ? 37.121 17.766  24.832  1.000 31.230  ? 170 ALA A CA  1 ? 1 
ATOM   1179 C C   . ALA A 1 174 ? 35.667 17.324  24.694  1.000 32.316  ? 170 ALA A C   1 ? 1 
ATOM   1180 O O   . ALA A 1 174 ? 35.459 16.127  24.522  1.000 34.833  ? 170 ALA A O   1 ? 1 
ATOM   1181 C CB  . ALA A 1 174 ? 37.640 18.437  23.577  1.000 30.439  ? 170 ALA A CB  1 ? 1 
ATOM   1182 N N   . ALA A 1 175 ? 34.701 18.234  24.811  1.000 36.514  ? 171 ALA A N   1 ? 1 
ATOM   1183 C CA  . ALA A 1 175 ? 33.237 18.001  24.593  1.000 37.955  ? 171 ALA A CA  1 ? 1 
ATOM   1184 C C   . ALA A 1 175 ? 32.914 18.195  23.112  1.000 38.193  ? 171 ALA A C   1 ? 1 
ATOM   1185 O O   . ALA A 1 175 ? 33.809 18.532  22.426  1.000 38.324  ? 171 ALA A O   1 ? 1 
ATOM   1186 C CB  . ALA A 1 175 ? 32.455 18.967  25.456  1.000 37.043  ? 171 ALA A CB  1 ? 1 
ATOM   1187 N N   . GLY A 1 176 ? 31.670 18.057  22.665  1.000 42.763  ? 172 GLY A N   1 ? 1 
ATOM   1188 C CA  . GLY A 1 176 ? 31.253 18.455  21.301  1.000 45.090  ? 172 GLY A CA  1 ? 1 
ATOM   1189 C C   . GLY A 1 176 ? 31.025 17.262  20.379  1.000 47.417  ? 172 GLY A C   1 ? 1 
ATOM   1190 O O   . GLY A 1 176 ? 31.480 16.142  20.730  1.000 48.684  ? 172 GLY A O   1 ? 1 
ATOM   1191 N N   . ARG A 1 177 ? 30.377 17.479  19.229  1.000 48.739  ? 173 ARG A N   1 ? 1 
ATOM   1192 C CA  . ARG A 1 177 ? 29.808 16.375  18.410  1.000 53.668  ? 173 ARG A CA  1 ? 1 
ATOM   1193 C C   . ARG A 1 177 ? 30.897 15.482  17.792  1.000 47.590  ? 173 ARG A C   1 ? 1 
ATOM   1194 O O   . ARG A 1 177 ? 30.673 14.258  17.690  1.000 41.325  ? 173 ARG A O   1 ? 1 
ATOM   1195 C CB  . ARG A 1 177 ? 28.884 16.878  17.296  1.000 64.204  ? 173 ARG A CB  1 ? 1 
ATOM   1196 C CG  . ARG A 1 177 ? 28.049 15.755  16.683  1.000 74.731  ? 173 ARG A CG  1 ? 1 
ATOM   1197 C CD  . ARG A 1 177 ? 28.142 15.659  15.164  1.000 81.262  ? 173 ARG A CD  1 ? 1 
ATOM   1198 N NE  . ARG A 1 177 ? 27.363 16.740  14.578  1.000 88.185  ? 173 ARG A NE  1 ? 1 
ATOM   1199 C CZ  . ARG A 1 177 ? 27.033 16.833  13.294  1.000 92.321  ? 173 ARG A CZ  1 ? 1 
ATOM   1200 N NH1 . ARG A 1 177 ? 27.419 15.916  12.423  1.000 91.611  ? 173 ARG A NH1 1 ? 1 
ATOM   1201 N NH2 . ARG A 1 177 ? 26.310 17.857  12.882  1.000 97.801  ? 173 ARG A NH2 1 ? 1 
ATOM   1202 N N   . GLU A 1 178 ? 32.025 16.033  17.370  1.000 46.237  ? 174 GLU A N   1 ? 1 
ATOM   1203 C CA  . GLU A 1 178 ? 33.064 15.184  16.729  1.000 48.408  ? 174 GLU A CA  1 ? 1 
ATOM   1204 C C   . GLU A 1 178 ? 33.664 14.249  17.784  1.000 41.740  ? 174 GLU A C   1 ? 1 
ATOM   1205 O O   . GLU A 1 178 ? 33.783 13.041  17.489  1.000 37.963  ? 174 GLU A O   1 ? 1 
ATOM   1206 C CB  . GLU A 1 178 ? 34.075 16.046  15.978  1.000 56.047  ? 174 GLU A CB  1 ? 1 
ATOM   1207 C CG  . GLU A 1 178 ? 33.408 16.775  14.807  1.000 63.635  ? 174 GLU A CG  1 ? 1 
ATOM   1208 C CD  . GLU A 1 178 ? 34.094 18.046  14.322  1.000 70.518  ? 174 GLU A CD  1 ? 1 
ATOM   1209 O OE1 . GLU A 1 178 ? 33.683 18.588  13.243  1.000 71.488  ? 174 GLU A OE1 1 ? 1 
ATOM   1210 O OE2 . GLU A 1 178 ? 35.037 18.500  15.030  1.000 74.670  ? 174 GLU A OE2 1 ? 1 
ATOM   1211 N N   . CYS A 1 179 ? 33.965 14.742  18.996  1.000 36.382  ? 175 CYS A N   1 ? 1 
ATOM   1212 C CA  . CYS A 1 179 ? 34.425 13.851  20.089  1.000 32.769  ? 175 CYS A CA  1 ? 1 
ATOM   1213 C C   . CYS A 1 179 ? 33.382 12.776  20.369  1.000 30.031  ? 175 CYS A C   1 ? 1 
ATOM   1214 O O   . CYS A 1 179 ? 33.777 11.612  20.431  1.000 29.780  ? 175 CYS A O   1 ? 1 
ATOM   1215 C CB  . CYS A 1 179 ? 34.693 14.580  21.385  1.000 34.185  ? 175 CYS A CB  1 ? 1 
ATOM   1216 S SG  . CYS A 1 179 ? 35.306 13.431  22.647  1.000 34.392  ? 175 CYS A SG  1 ? 1 
ATOM   1217 N N   . ALA A 1 180 ? 32.103 13.127  20.510  1.000 28.694  ? 176 ALA A N   1 ? 1 
ATOM   1218 C CA  . ALA A 1 180 ? 31.015 12.128  20.721  1.000 29.827  ? 176 ALA A CA  1 ? 1 
ATOM   1219 C C   . ALA A 1 180 ? 30.944 11.097  19.595  1.000 29.685  ? 176 ALA A C   1 ? 1 
ATOM   1220 O O   . ALA A 1 180 ? 30.755 9.902   19.907  1.000 29.853  ? 176 ALA A O   1 ? 1 
ATOM   1221 C CB  . ALA A 1 180 ? 29.662 12.765  20.902  1.000 29.772  ? 176 ALA A CB  1 ? 1 
ATOM   1222 N N   . GLU A 1 181 ? 31.070 11.524  18.334  1.000 31.300  ? 177 GLU A N   1 ? 1 
ATOM   1223 C CA  . GLU A 1 181 ? 31.004 10.598  17.183  1.000 31.239  ? 177 GLU A CA  1 ? 1 
ATOM   1224 C C   . GLU A 1 181 ? 32.138 9.582   17.326  1.000 29.319  ? 177 GLU A C   1 ? 1 
ATOM   1225 O O   . GLU A 1 181 ? 31.885 8.384   17.266  1.000 29.323  ? 177 GLU A O   1 ? 1 
ATOM   1226 C CB  . GLU A 1 181 ? 31.004 11.386  15.880  1.000 34.948  ? 177 GLU A CB  1 ? 1 
ATOM   1227 C CG  . GLU A 1 181 ? 30.907 10.502  14.652  1.000 38.351  ? 177 GLU A CG  1 ? 1 
ATOM   1228 C CD  . GLU A 1 181 ? 29.691 9.584   14.657  1.000 42.729  ? 177 GLU A CD  1 ? 1 
ATOM   1229 O OE1 . GLU A 1 181 ? 29.769 8.475   14.057  1.000 44.040  ? 177 GLU A OE1 1 ? 1 
ATOM   1230 O OE2 . GLU A 1 181 ? 28.661 9.968   15.285  1.000 48.218  ? 177 GLU A OE2 1 ? 1 
ATOM   1231 N N   . ALA A 1 182 ? 33.341 10.022  17.642  1.000 28.748  ? 178 ALA A N   1 ? 1 
ATOM   1232 C CA  . ALA A 1 182 ? 34.511 9.123   17.761  1.000 28.175  ? 178 ALA A CA  1 ? 1 
ATOM   1233 C C   . ALA A 1 182 ? 34.268 8.082   18.853  1.000 28.323  ? 178 ALA A C   1 ? 1 
ATOM   1234 O O   . ALA A 1 182 ? 34.588 6.879   18.624  1.000 27.937  ? 178 ALA A O   1 ? 1 
ATOM   1235 C CB  . ALA A 1 182 ? 35.734 9.939   18.039  1.000 28.061  ? 178 ALA A CB  1 ? 1 
ATOM   1236 N N   . GLY A 1 183 ? 33.749 8.522   20.001  1.000 28.457  ? 179 GLY A N   1 ? 1 
ATOM   1237 C CA  . GLY A 1 183 ? 33.308 7.597   21.068  1.000 28.617  ? 179 GLY A CA  1 ? 1 
ATOM   1238 C C   . GLY A 1 183 ? 32.248 6.593   20.591  1.000 28.144  ? 179 GLY A C   1 ? 1 
ATOM   1239 O O   . GLY A 1 183 ? 32.396 5.352   20.826  1.000 26.116  ? 179 GLY A O   1 ? 1 
ATOM   1240 N N   . ASP A 1 184 ? 31.198 7.082   19.931  1.000 29.436  ? 180 ASP A N   1 ? 1 
ATOM   1241 C CA  . ASP A 1 184 ? 30.146 6.199   19.370  1.000 29.903  ? 180 ASP A CA  1 ? 1 
ATOM   1242 C C   . ASP A 1 184 ? 30.839 5.132   18.534  1.000 29.662  ? 180 ASP A C   1 ? 1 
ATOM   1243 O O   . ASP A 1 184 ? 30.560 3.971   18.753  1.000 30.043  ? 180 ASP A O   1 ? 1 
ATOM   1244 C CB  . ASP A 1 184 ? 29.087 6.997   18.620  1.000 31.606  ? 180 ASP A CB  1 ? 1 
ATOM   1245 C CG  . ASP A 1 184 ? 28.199 7.833   19.539  1.000 33.914  ? 180 ASP A CG  1 ? 1 
ATOM   1246 O OD1 . ASP A 1 184 ? 28.339 7.699   20.757  1.000 33.513  ? 180 ASP A OD1 1 ? 1 
ATOM   1247 O OD2 . ASP A 1 184 ? 27.361 8.624   19.027  1.000 37.801  ? 180 ASP A OD2 1 ? 1 
ATOM   1248 N N   . GLU A 1 185 ? 31.772 5.491   17.663  1.000 31.267  ? 181 GLU A N   1 ? 1 
ATOM   1249 C CA  . GLU A 1 185 ? 32.320 4.515   16.671  1.000 33.104  ? 181 GLU A CA  1 ? 1 
ATOM   1250 C C   . GLU A 1 185 ? 33.150 3.482   17.455  1.000 30.480  ? 181 GLU A C   1 ? 1 
ATOM   1251 O O   . GLU A 1 185 ? 33.118 2.261   17.132  1.000 29.835  ? 181 GLU A O   1 ? 1 
ATOM   1252 C CB  . GLU A 1 185 ? 33.018 5.245   15.508  1.000 35.186  ? 181 GLU A CB  1 ? 1 
ATOM   1253 C CG  . GLU A 1 185 ? 32.081 6.089   14.623  1.000 39.374  ? 181 GLU A CG  1 ? 1 
ATOM   1254 C CD  . GLU A 1 185 ? 32.702 6.949   13.494  1.000 44.706  ? 181 GLU A CD  1 ? 1 
ATOM   1255 O OE1 . GLU A 1 185 ? 33.838 6.665   13.072  1.000 49.374  ? 181 GLU A OE1 1 ? 1 
ATOM   1256 O OE2 . GLU A 1 185 ? 32.064 7.951   13.042  1.000 46.827  ? 181 GLU A OE2 1 ? 1 
ATOM   1257 N N   . LEU A 1 186 ? 33.817 3.931   18.511  1.000 29.241  ? 182 LEU A N   1 ? 1 
ATOM   1258 C CA  . LEU A 1 186 ? 34.682 3.056   19.316  1.000 28.713  ? 182 LEU A CA  1 ? 1 
ATOM   1259 C C   . LEU A 1 186 ? 33.810 2.081   20.084  1.000 29.011  ? 182 LEU A C   1 ? 1 
ATOM   1260 O O   . LEU A 1 186 ? 34.149 0.925   20.076  1.000 29.093  ? 182 LEU A O   1 ? 1 
ATOM   1261 C CB  . LEU A 1 186 ? 35.509 3.907   20.274  1.000 29.760  ? 182 LEU A CB  1 ? 1 
ATOM   1262 C CG  . LEU A 1 186 ? 36.324 3.129   21.310  1.000 29.727  ? 182 LEU A CG  1 ? 1 
ATOM   1263 C CD1 . LEU A 1 186 ? 37.457 2.316   20.675  1.000 29.408  ? 182 LEU A CD1 1 ? 1 
ATOM   1264 C CD2 . LEU A 1 186 ? 36.852 4.079   22.353  1.000 30.175  ? 182 LEU A CD2 1 ? 1 
ATOM   1265 N N   . PHE A 1 187 ? 32.723 2.499   20.722  1.000 29.990  ? 183 PHE A N   1 ? 1 
ATOM   1266 C CA  . PHE A 1 187 ? 31.894 1.522   21.477  1.000 33.284  ? 183 PHE A CA  1 ? 1 
ATOM   1267 C C   . PHE A 1 187 ? 31.221 0.552   20.507  1.000 32.714  ? 183 PHE A C   1 ? 1 
ATOM   1268 O O   . PHE A 1 187 ? 31.218 -0.680  20.738  1.000 31.947  ? 183 PHE A O   1 ? 1 
ATOM   1269 C CB  . PHE A 1 187 ? 30.897 2.203   22.423  1.000 35.947  ? 183 PHE A CB  1 ? 1 
ATOM   1270 C CG  . PHE A 1 187 ? 31.499 2.602   23.748  1.000 36.198  ? 183 PHE A CG  1 ? 1 
ATOM   1271 C CD1 . PHE A 1 187 ? 31.279 1.840   24.885  1.000 37.421  ? 183 PHE A CD1 1 ? 1 
ATOM   1272 C CD2 . PHE A 1 187 ? 32.335 3.713   23.851  1.000 37.641  ? 183 PHE A CD2 1 ? 1 
ATOM   1273 C CE1 . PHE A 1 187 ? 31.849 2.192   26.099  1.000 35.617  ? 183 PHE A CE1 1 ? 1 
ATOM   1274 C CE2 . PHE A 1 187 ? 32.907 4.065   25.066  1.000 37.341  ? 183 PHE A CE2 1 ? 1 
ATOM   1275 C CZ  . PHE A 1 187 ? 32.664 3.301   26.195  1.000 35.848  ? 183 PHE A CZ  1 ? 1 
ATOM   1276 N N   . ASN A 1 188 ? 30.670 1.095   19.431  1.000 34.594  ? 184 ASN A N   1 ? 1 
ATOM   1277 C CA  . ASN A 1 188 ? 29.936 0.291   18.418  1.000 37.108  ? 184 ASN A CA  1 ? 1 
ATOM   1278 C C   . ASN A 1 188 ? 30.874 -0.828  17.918  1.000 34.207  ? 184 ASN A C   1 ? 1 
ATOM   1279 O O   . ASN A 1 188 ? 30.421 -1.980  17.816  1.000 34.479  ? 184 ASN A O   1 ? 1 
ATOM   1280 C CB  . ASN A 1 188 ? 29.214 1.196   17.398  1.000 40.617  ? 184 ASN A CB  1 ? 1 
ATOM   1281 C CG  . ASN A 1 188 ? 27.851 1.750   17.842  1.000 45.941  ? 184 ASN A CG  1 ? 1 
ATOM   1282 O OD1 . ASN A 1 188 ? 27.462 1.875   19.040  1.000 48.815  ? 184 ASN A OD1 1 ? 1 
ATOM   1283 N ND2 . ASN A 1 188 ? 27.074 2.116   16.842  1.000 50.209  ? 184 ASN A ND2 1 ? 1 
ATOM   1284 N N   . LEU A 1 189 ? 32.159 -0.593  17.732  1.000 31.430  ? 185 LEU A N   1 ? 1 
ATOM   1285 C CA  . LEU A 1 189 ? 33.004 -1.689  17.201  1.000 32.040  ? 185 LEU A CA  1 ? 1 
ATOM   1286 C C   . LEU A 1 189 ? 33.182 -2.773  18.254  1.000 32.015  ? 185 LEU A C   1 ? 1 
ATOM   1287 O O   . LEU A 1 189 ? 33.110 -4.000  17.898  1.000 31.084  ? 185 LEU A O   1 ? 1 
ATOM   1288 C CB  . LEU A 1 189 ? 34.351 -1.127  16.750  1.000 32.224  ? 185 LEU A CB  1 ? 1 
ATOM   1289 C CG  . LEU A 1 189 ? 35.284 -2.118  16.050  1.000 31.228  ? 185 LEU A CG  1 ? 1 
ATOM   1290 C CD1 . LEU A 1 189 ? 34.643 -2.733  14.839  1.000 31.585  ? 185 LEU A CD1 1 ? 1 
ATOM   1291 C CD2 . LEU A 1 189 ? 36.559 -1.403  15.674  1.000 32.007  ? 185 LEU A CD2 1 ? 1 
ATOM   1292 N N   . ALA A 1 190 ? 33.445 -2.378  19.504  1.000 31.903  ? 186 ALA A N   1 ? 1 
ATOM   1293 C CA  . ALA A 1 190 ? 33.604 -3.358  20.599  1.000 31.394  ? 186 ALA A CA  1 ? 1 
ATOM   1294 C C   . ALA A 1 190 ? 32.306 -4.177  20.690  1.000 31.612  ? 186 ALA A C   1 ? 1 
ATOM   1295 O O   . ALA A 1 190 ? 32.367 -5.426  20.794  1.000 29.694  ? 186 ALA A O   1 ? 1 
ATOM   1296 C CB  . ALA A 1 190 ? 33.922 -2.648  21.887  1.000 32.468  ? 186 ALA A CB  1 ? 1 
ATOM   1297 N N   . MET A 1 191 ? 31.147 -3.525  20.631  1.000 32.954  ? 187 MET A N   1 ? 1 
ATOM   1298 C CA  . MET A 1 191 ? 29.867 -4.286  20.711  1.000 36.614  ? 187 MET A CA  1 ? 1 
ATOM   1299 C C   . MET A 1 191 ? 29.816 -5.341  19.590  1.000 39.325  ? 187 MET A C   1 ? 1 
ATOM   1300 O O   . MET A 1 191 ? 29.499 -6.512  19.907  1.000 40.447  ? 187 MET A O   1 ? 1 
ATOM   1301 C CB  . MET A 1 191 ? 28.633 -3.388  20.637  1.000 37.189  ? 187 MET A CB  1 ? 1 
ATOM   1302 C CG  . MET A 1 191 ? 28.562 -2.367  21.758  1.000 37.158  ? 187 MET A CG  1 ? 1 
ATOM   1303 S SD  . MET A 1 191 ? 26.958 -1.545  21.775  1.000 39.853  ? 187 MET A SD  1 ? 1 
ATOM   1304 C CE  . MET A 1 191 ? 27.404 0.050   22.447  1.000 43.691  ? 187 MET A CE  1 ? 1 
ATOM   1305 N N   . LEU A 1 192 ? 30.147 -4.965  18.348  1.000 42.044  ? 188 LEU A N   1 ? 1 
ATOM   1306 C CA  . LEU A 1 192 ? 30.178 -5.881  17.175  1.000 44.042  ? 188 LEU A CA  1 ? 1 
ATOM   1307 C C   . LEU A 1 192 ? 31.040 -7.090  17.493  1.000 43.435  ? 188 LEU A C   1 ? 1 
ATOM   1308 O O   . LEU A 1 192 ? 30.607 -8.188  17.177  1.000 43.697  ? 188 LEU A O   1 ? 1 
ATOM   1309 C CB  . LEU A 1 192 ? 30.737 -5.161  15.946  1.000 49.032  ? 188 LEU A CB  1 ? 1 
ATOM   1310 C CG  . LEU A 1 192 ? 29.668 -4.459  15.108  1.000 55.925  ? 188 LEU A CG  1 ? 1 
ATOM   1311 C CD1 . LEU A 1 192 ? 30.233 -3.325  14.229  1.000 57.007  ? 188 LEU A CD1 1 ? 1 
ATOM   1312 C CD2 . LEU A 1 192 ? 28.913 -5.499  14.284  1.000 58.141  ? 188 LEU A CD2 1 ? 1 
ATOM   1313 N N   . PHE A 1 193 ? 32.217 -6.889  18.086  1.000 44.385  ? 189 PHE A N   1 ? 1 
ATOM   1314 C CA  . PHE A 1 193 ? 33.140 -7.993  18.475  1.000 45.276  ? 189 PHE A CA  1 ? 1 
ATOM   1315 C C   . PHE A 1 193 ? 32.541 -8.910  19.547  1.000 45.612  ? 189 PHE A C   1 ? 1 
ATOM   1316 O O   . PHE A 1 193 ? 32.947 -10.111 19.592  1.000 46.128  ? 189 PHE A O   1 ? 1 
ATOM   1317 C CB  . PHE A 1 193 ? 34.445 -7.472  19.063  1.000 45.170  ? 189 PHE A CB  1 ? 1 
ATOM   1318 C CG  . PHE A 1 193 ? 35.341 -6.724  18.116  1.000 45.100  ? 189 PHE A CG  1 ? 1 
ATOM   1319 C CD1 . PHE A 1 193 ? 35.242 -6.886  16.742  1.000 45.716  ? 189 PHE A CD1 1 ? 1 
ATOM   1320 C CD2 . PHE A 1 193 ? 36.321 -5.891  18.623  1.000 42.476  ? 189 PHE A CD2 1 ? 1 
ATOM   1321 C CE1 . PHE A 1 193 ? 36.098 -6.208  15.896  1.000 44.259  ? 189 PHE A CE1 1 ? 1 
ATOM   1322 C CE2 . PHE A 1 193 ? 37.180 -5.232  17.771  1.000 41.202  ? 189 PHE A CE2 1 ? 1 
ATOM   1323 C CZ  . PHE A 1 193 ? 37.069 -5.393  16.415  1.000 43.113  ? 189 PHE A CZ  1 ? 1 
ATOM   1324 N N   . SER A 1 194 ? 31.621 -8.384  20.363  1.000 45.463  ? 190 SER A N   1 ? 1 
ATOM   1325 C CA  . SER A 1 194 ? 30.880 -9.165  21.395  1.000 48.052  ? 190 SER A CA  1 ? 1 
ATOM   1326 C C   . SER A 1 194 ? 30.008 -10.262 20.742  1.000 51.407  ? 190 SER A C   1 ? 1 
ATOM   1327 O O   . SER A 1 194 ? 29.866 -11.353 21.341  1.000 51.363  ? 190 SER A O   1 ? 1 
ATOM   1328 C CB  . SER A 1 194 ? 30.082 -8.263  22.305  1.000 44.009  ? 190 SER A CB  1 ? 1 
ATOM   1329 O OG  . SER A 1 194 ? 28.829 -7.980  21.728  1.000 42.354  ? 190 SER A OG  1 ? 1 
ATOM   1330 N N   . MET A 1 195 ? 29.502 -10.019 19.533  1.000 56.236  ? 191 MET A N   1 ? 1 
ATOM   1331 C CA  . MET A 1 195 ? 28.707 -10.994 18.741  1.000 59.535  ? 191 MET A CA  1 ? 1 
ATOM   1332 C C   . MET A 1 195 ? 29.615 -11.980 17.960  1.000 63.913  ? 191 MET A C   1 ? 1 
ATOM   1333 O O   . MET A 1 195 ? 29.351 -12.192 16.777  1.000 66.874  ? 191 MET A O   1 ? 1 
ATOM   1334 C CB  . MET A 1 195 ? 27.836 -10.211 17.759  1.000 61.077  ? 191 MET A CB  1 ? 1 
ATOM   1335 C CG  . MET A 1 195 ? 26.893 -9.190  18.385  1.000 62.244  ? 191 MET A CG  1 ? 1 
ATOM   1336 S SD  . MET A 1 195 ? 25.935 -8.190  17.130  1.000 69.933  ? 191 MET A SD  1 ? 1 
ATOM   1337 C CE  . MET A 1 195 ? 25.756 -9.297  15.726  1.000 72.469  ? 191 MET A CE  1 ? 1 
ATOM   1338 N N   . ASP A 1 196 ? 30.621 -12.610 18.590  1.000 70.947  ? 192 ASP A N   1 ? 1 
ATOM   1339 C CA  . ASP A 1 196 ? 31.725 -13.372 17.930  1.000 73.599  ? 192 ASP A CA  1 ? 1 
ATOM   1340 C C   . ASP A 1 196 ? 32.379 -12.485 16.857  1.000 75.178  ? 192 ASP A C   1 ? 1 
ATOM   1341 O O   . ASP A 1 196 ? 33.562 -12.121 16.811  1.000 72.623  ? 192 ASP A O   1 ? 1 
ATOM   1342 C CB  . ASP A 1 196 ? 31.243 -14.672 17.276  1.000 76.710  ? 192 ASP A CB  1 ? 1 
ATOM   1343 C CG  . ASP A 1 196 ? 30.752 -15.759 18.217  1.000 79.840  ? 192 ASP A CG  1 ? 1 
ATOM   1344 O OD1 . ASP A 1 196 ? 30.516 -15.463 19.413  1.000 75.614  ? 192 ASP A OD1 1 ? 1 
ATOM   1345 O OD2 . ASP A 1 196 ? 30.592 -16.889 17.729  1.000 81.074  ? 192 ASP A OD2 1 ? 1 
ATOM   1346 N N   . ASP B 1 31  ? 18.427 19.541  75.542  1.000 103.708 ? 27  ASP B N   1 ? 2 
ATOM   1347 C CA  . ASP B 1 31  ? 18.842 18.187  75.111  1.000 104.977 ? 27  ASP B CA  1 ? 2 
ATOM   1348 C C   . ASP B 1 31  ? 18.091 17.739  73.835  1.000 110.312 ? 27  ASP B C   1 ? 2 
ATOM   1349 O O   . ASP B 1 31  ? 18.367 16.611  73.388  1.000 107.746 ? 27  ASP B O   1 ? 2 
ATOM   1350 C CB  . ASP B 1 31  ? 18.699 17.189  76.268  1.000 98.408  ? 27  ASP B CB  1 ? 2 
ATOM   1351 N N   . HIS B 1 32  ? 17.191 18.565  73.258  1.000 120.762 ? 28  HIS B N   1 ? 2 
ATOM   1352 C CA  . HIS B 1 32  ? 16.458 18.308  71.965  1.000 128.109 ? 28  HIS B CA  1 ? 2 
ATOM   1353 C C   . HIS B 1 32  ? 16.540 19.495  70.961  1.000 126.217 ? 28  HIS B C   1 ? 2 
ATOM   1354 O O   . HIS B 1 32  ? 16.044 19.312  69.804  1.000 114.124 ? 28  HIS B O   1 ? 2 
ATOM   1355 C CB  . HIS B 1 32  ? 14.991 17.889  72.242  1.000 131.133 ? 28  HIS B CB  1 ? 2 
ATOM   1356 C CG  . HIS B 1 32  ? 14.519 16.671  71.500  1.000 131.867 ? 28  HIS B CG  1 ? 2 
ATOM   1357 N ND1 . HIS B 1 32  ? 13.447 15.906  71.951  1.000 128.537 ? 28  HIS B ND1 1 ? 2 
ATOM   1358 C CD2 . HIS B 1 32  ? 14.974 16.052  70.383  1.000 128.112 ? 28  HIS B CD2 1 ? 2 
ATOM   1359 C CE1 . HIS B 1 32  ? 13.254 14.889  71.134  1.000 125.979 ? 28  HIS B CE1 1 ? 2 
ATOM   1360 N NE2 . HIS B 1 32  ? 14.182 14.953  70.167  1.000 127.921 ? 28  HIS B NE2 1 ? 2 
ATOM   1361 N N   . ALA B 1 33  ? 17.113 20.654  71.375  1.000 121.996 ? 29  ALA B N   1 ? 2 
ATOM   1362 C CA  . ALA B 1 33  ? 17.586 21.799  70.542  1.000 111.463 ? 29  ALA B CA  1 ? 2 
ATOM   1363 C C   . ALA B 1 33  ? 18.877 21.402  69.812  1.000 105.624 ? 29  ALA B C   1 ? 2 
ATOM   1364 O O   . ALA B 1 33  ? 19.323 22.138  68.902  1.000 93.827  ? 29  ALA B O   1 ? 2 
ATOM   1365 C CB  . ALA B 1 33  ? 17.830 23.018  71.412  1.000 105.691 ? 29  ALA B CB  1 ? 2 
ATOM   1366 N N   . ASP B 1 34  ? 19.460 20.294  70.282  1.000 102.298 ? 30  ASP B N   1 ? 2 
ATOM   1367 C CA  . ASP B 1 34  ? 20.652 19.593  69.747  1.000 96.237  ? 30  ASP B CA  1 ? 2 
ATOM   1368 C C   . ASP B 1 34  ? 20.295 18.865  68.447  1.000 99.455  ? 30  ASP B C   1 ? 2 
ATOM   1369 O O   . ASP B 1 34  ? 20.950 19.172  67.435  1.000 98.422  ? 30  ASP B O   1 ? 2 
ATOM   1370 C CB  . ASP B 1 34  ? 21.198 18.601  70.783  1.000 86.306  ? 30  ASP B CB  1 ? 2 
ATOM   1371 C CG  . ASP B 1 34  ? 21.836 19.240  72.006  1.000 79.737  ? 30  ASP B CG  1 ? 2 
ATOM   1372 O OD1 . ASP B 1 34  ? 22.092 20.484  72.002  1.000 72.397  ? 30  ASP B OD1 1 ? 2 
ATOM   1373 O OD2 . ASP B 1 34  ? 22.111 18.480  72.937  1.000 74.063  ? 30  ASP B OD2 1 ? 2 
ATOM   1374 N N   . ALA B 1 35  ? 19.335 17.927  68.481  1.000 102.825 ? 31  ALA B N   1 ? 2 
ATOM   1375 C CA  . ALA B 1 35  ? 18.886 17.141  67.303  1.000 106.130 ? 31  ALA B CA  1 ? 2 
ATOM   1376 C C   . ALA B 1 35  ? 18.541 18.112  66.153  1.000 106.139 ? 31  ALA B C   1 ? 2 
ATOM   1377 O O   . ALA B 1 35  ? 18.562 17.678  64.970  1.000 100.322 ? 31  ALA B O   1 ? 2 
ATOM   1378 C CB  . ALA B 1 35  ? 17.729 16.236  67.686  1.000 102.575 ? 31  ALA B CB  1 ? 2 
ATOM   1379 N N   . ALA B 1 36  ? 18.279 19.387  66.497  1.000 107.745 ? 32  ALA B N   1 ? 2 
ATOM   1380 C CA  . ALA B 1 36  ? 17.959 20.513  65.582  1.000 105.995 ? 32  ALA B CA  1 ? 2 
ATOM   1381 C C   . ALA B 1 36  ? 19.231 21.143  64.977  1.000 109.185 ? 32  ALA B C   1 ? 2 
ATOM   1382 O O   . ALA B 1 36  ? 19.265 21.197  63.729  1.000 115.573 ? 32  ALA B O   1 ? 2 
ATOM   1383 C CB  . ALA B 1 36  ? 17.144 21.539  66.326  1.000 106.060 ? 32  ALA B CB  1 ? 2 
ATOM   1384 N N   . TYR B 1 37  ? 20.207 21.613  65.794  1.000 104.578 ? 33  TYR B N   1 ? 2 
ATOM   1385 C CA  . TYR B 1 37  ? 21.487 22.277  65.370  1.000 95.610  ? 33  TYR B CA  1 ? 2 
ATOM   1386 C C   . TYR B 1 37  ? 22.289 21.388  64.405  1.000 89.587  ? 33  TYR B C   1 ? 2 
ATOM   1387 O O   . TYR B 1 37  ? 23.047 21.926  63.577  1.000 78.363  ? 33  TYR B O   1 ? 2 
ATOM   1388 C CB  . TYR B 1 37  ? 22.391 22.616  66.560  1.000 95.997  ? 33  TYR B CB  1 ? 2 
ATOM   1389 C CG  . TYR B 1 37  ? 23.641 23.399  66.222  1.000 99.014  ? 33  TYR B CG  1 ? 2 
ATOM   1390 C CD1 . TYR B 1 37  ? 23.590 24.768  65.995  1.000 102.920 ? 33  TYR B CD1 1 ? 2 
ATOM   1391 C CD2 . TYR B 1 37  ? 24.884 22.786  66.150  1.000 100.086 ? 33  TYR B CD2 1 ? 2 
ATOM   1392 C CE1 . TYR B 1 37  ? 24.729 25.507  65.702  1.000 104.880 ? 33  TYR B CE1 1 ? 2 
ATOM   1393 C CE2 . TYR B 1 37  ? 26.034 23.506  65.849  1.000 104.103 ? 33  TYR B CE2 1 ? 2 
ATOM   1394 C CZ  . TYR B 1 37  ? 25.962 24.875  65.630  1.000 108.742 ? 33  TYR B CZ  1 ? 2 
ATOM   1395 O OH  . TYR B 1 37  ? 27.088 25.595  65.323  1.000 109.195 ? 33  TYR B OH  1 ? 2 
ATOM   1396 N N   . VAL B 1 38  ? 22.092 20.070  64.514  1.000 88.916  ? 34  VAL B N   1 ? 2 
ATOM   1397 C CA  . VAL B 1 38  ? 22.768 18.978  63.750  1.000 85.737  ? 34  VAL B CA  1 ? 2 
ATOM   1398 C C   . VAL B 1 38  ? 22.141 18.838  62.349  1.000 88.261  ? 34  VAL B C   1 ? 2 
ATOM   1399 O O   . VAL B 1 38  ? 22.924 18.710  61.377  1.000 88.497  ? 34  VAL B O   1 ? 2 
ATOM   1400 C CB  . VAL B 1 38  ? 22.738 17.673  64.580  1.000 81.875  ? 34  VAL B CB  1 ? 2 
ATOM   1401 C CG1 . VAL B 1 38  ? 22.734 16.398  63.747  1.000 80.702  ? 34  VAL B CG1 1 ? 2 
ATOM   1402 C CG2 . VAL B 1 38  ? 23.877 17.656  65.586  1.000 79.146  ? 34  VAL B CG2 1 ? 2 
ATOM   1403 N N   . GLU B 1 39  ? 20.804 18.852  62.223  1.000 96.174  ? 35  GLU B N   1 ? 2 
ATOM   1404 C CA  . GLU B 1 39  ? 20.088 18.864  60.904  1.000 95.881  ? 35  GLU B CA  1 ? 2 
ATOM   1405 C C   . GLU B 1 39  ? 20.300 20.243  60.247  1.000 87.749  ? 35  GLU B C   1 ? 2 
ATOM   1406 O O   . GLU B 1 39  ? 20.699 20.288  59.072  1.000 85.453  ? 35  GLU B O   1 ? 2 
ATOM   1407 C CB  . GLU B 1 39  ? 18.598 18.553  61.102  1.000 96.701  ? 35  GLU B CB  1 ? 2 
ATOM   1408 C CG  . GLU B 1 39  ? 18.048 17.418  60.256  1.000 95.756  ? 35  GLU B CG  1 ? 2 
ATOM   1409 C CD  . GLU B 1 39  ? 16.527 17.369  60.326  1.000 98.202  ? 35  GLU B CD  1 ? 2 
ATOM   1410 O OE1 . GLU B 1 39  ? 15.993 17.160  61.445  1.000 95.967  ? 35  GLU B OE1 1 ? 2 
ATOM   1411 O OE2 . GLU B 1 39  ? 15.877 17.600  59.274  1.000 93.819  ? 35  GLU B OE2 1 ? 2 
ATOM   1412 N N   . LYS B 1 40  ? 20.090 21.311  61.024  1.000 82.850  ? 36  LYS B N   1 ? 2 
ATOM   1413 C CA  . LYS B 1 40  ? 20.214 22.754  60.660  1.000 87.302  ? 36  LYS B CA  1 ? 2 
ATOM   1414 C C   . LYS B 1 40  ? 21.595 23.116  60.086  1.000 85.610  ? 36  LYS B C   1 ? 2 
ATOM   1415 O O   . LYS B 1 40  ? 21.709 24.251  59.607  1.000 88.351  ? 36  LYS B O   1 ? 2 
ATOM   1416 C CB  . LYS B 1 40  ? 19.944 23.614  61.910  1.000 92.081  ? 36  LYS B CB  1 ? 2 
ATOM   1417 C CG  . LYS B 1 40  ? 20.096 25.141  61.821  1.000 93.956  ? 36  LYS B CG  1 ? 2 
ATOM   1418 C CD  . LYS B 1 40  ? 18.862 25.936  61.352  1.000 97.416  ? 36  LYS B CD  1 ? 2 
ATOM   1419 C CE  . LYS B 1 40  ? 19.029 26.632  60.007  1.000 94.221  ? 36  LYS B CE  1 ? 2 
ATOM   1420 N NZ  . LYS B 1 40  ? 17.742 27.132  59.465  1.000 92.519  ? 36  LYS B NZ  1 ? 2 
ATOM   1421 N N   . HIS B 1 41  ? 22.616 22.253  60.167  1.000 83.492  ? 37  HIS B N   1 ? 2 
ATOM   1422 C CA  . HIS B 1 41  ? 24.018 22.572  59.758  1.000 78.855  ? 37  HIS B CA  1 ? 2 
ATOM   1423 C C   . HIS B 1 41  ? 24.654 21.434  58.936  1.000 73.150  ? 37  HIS B C   1 ? 2 
ATOM   1424 O O   . HIS B 1 41  ? 25.863 21.501  58.738  1.000 71.366  ? 37  HIS B O   1 ? 2 
ATOM   1425 C CB  . HIS B 1 41  ? 24.883 22.908  60.995  1.000 82.413  ? 37  HIS B CB  1 ? 2 
ATOM   1426 C CG  . HIS B 1 41  ? 24.725 24.280  61.582  1.000 84.369  ? 37  HIS B CG  1 ? 2 
ATOM   1427 N ND1 . HIS B 1 41  ? 25.732 25.240  61.515  1.000 86.043  ? 37  HIS B ND1 1 ? 2 
ATOM   1428 C CD2 . HIS B 1 41  ? 23.727 24.843  62.304  1.000 84.114  ? 37  HIS B CD2 1 ? 2 
ATOM   1429 C CE1 . HIS B 1 41  ? 25.347 26.335  62.148  1.000 85.259  ? 37  HIS B CE1 1 ? 2 
ATOM   1430 N NE2 . HIS B 1 41  ? 24.121 26.116  62.645  1.000 83.722  ? 37  HIS B NE2 1 ? 2 
ATOM   1431 N N   . ASN B 1 42  ? 23.883 20.450  58.446  1.000 72.707  ? 38  ASN B N   1 ? 2 
ATOM   1432 C CA  . ASN B 1 42  ? 24.350 19.363  57.533  1.000 71.807  ? 38  ASN B CA  1 ? 2 
ATOM   1433 C C   . ASN B 1 42  ? 25.415 18.501  58.206  1.000 70.725  ? 38  ASN B C   1 ? 2 
ATOM   1434 O O   . ASN B 1 42  ? 26.379 18.045  57.498  1.000 71.716  ? 38  ASN B O   1 ? 2 
ATOM   1435 C CB  . ASN B 1 42  ? 24.894 19.915  56.211  1.000 71.419  ? 38  ASN B CB  1 ? 2 
ATOM   1436 C CG  . ASN B 1 42  ? 23.855 19.817  55.131  1.000 69.364  ? 38  ASN B CG  1 ? 2 
ATOM   1437 O OD1 . ASN B 1 42  ? 23.109 20.762  54.915  1.000 72.906  ? 38  ASN B OD1 1 ? 2 
ATOM   1438 N ND2 . ASN B 1 42  ? 23.742 18.643  54.538  1.000 67.969  ? 38  ASN B ND2 1 ? 2 
ATOM   1439 N N   . LEU B 1 43  ? 25.251 18.296  59.515  1.000 67.646  ? 39  LEU B N   1 ? 2 
ATOM   1440 C CA  . LEU B 1 43  ? 26.174 17.503  60.367  1.000 63.056  ? 39  LEU B CA  1 ? 2 
ATOM   1441 C C   . LEU B 1 43  ? 25.512 16.154  60.654  1.000 61.546  ? 39  LEU B C   1 ? 2 
ATOM   1442 O O   . LEU B 1 43  ? 26.155 15.275  61.283  1.000 61.631  ? 39  LEU B O   1 ? 2 
ATOM   1443 C CB  . LEU B 1 43  ? 26.488 18.341  61.611  1.000 63.186  ? 39  LEU B CB  1 ? 2 
ATOM   1444 C CG  . LEU B 1 43  ? 27.420 19.530  61.341  1.000 62.607  ? 39  LEU B CG  1 ? 2 
ATOM   1445 C CD1 . LEU B 1 43  ? 27.248 20.685  62.324  1.000 62.028  ? 39  LEU B CD1 1 ? 2 
ATOM   1446 C CD2 . LEU B 1 43  ? 28.857 19.059  61.372  1.000 66.302  ? 39  LEU B CD2 1 ? 2 
ATOM   1447 N N   . GLN B 1 44  ? 24.296 15.979  60.135  1.000 62.726  ? 40  GLN B N   1 ? 2 
ATOM   1448 C CA  . GLN B 1 44  ? 23.525 14.730  60.305  1.000 68.733  ? 40  GLN B CA  1 ? 2 
ATOM   1449 C C   . GLN B 1 44  ? 24.346 13.589  59.683  1.000 66.276  ? 40  GLN B C   1 ? 2 
ATOM   1450 O O   . GLN B 1 44  ? 24.308 12.463  60.214  1.000 69.853  ? 40  GLN B O   1 ? 2 
ATOM   1451 C CB  . GLN B 1 44  ? 22.094 14.888  59.755  1.000 77.019  ? 40  GLN B CB  1 ? 2 
ATOM   1452 C CG  . GLN B 1 44  ? 21.159 13.703  60.062  1.000 84.606  ? 40  GLN B CG  1 ? 2 
ATOM   1453 C CD  . GLN B 1 44  ? 21.423 12.983  61.381  1.000 93.846  ? 40  GLN B CD  1 ? 2 
ATOM   1454 O OE1 . GLN B 1 44  ? 21.347 13.564  62.469  1.000 92.904  ? 40  GLN B OE1 1 ? 2 
ATOM   1455 N NE2 . GLN B 1 44  ? 21.757 11.696  61.310  1.000 92.131  ? 40  GLN B NE2 1 ? 2 
ATOM   1456 N N   . CYS B 1 45  ? 25.095 13.853  58.616  1.000 64.266  ? 41  CYS B N   1 ? 2 
ATOM   1457 C CA  . CYS B 1 45  ? 25.824 12.791  57.874  1.000 62.525  ? 41  CYS B CA  1 ? 2 
ATOM   1458 C C   . CYS B 1 45  ? 26.974 12.274  58.755  1.000 55.340  ? 41  CYS B C   1 ? 2 
ATOM   1459 O O   . CYS B 1 45  ? 27.119 11.021  58.929  1.000 48.356  ? 41  CYS B O   1 ? 2 
ATOM   1460 C CB  . CYS B 1 45  ? 26.301 13.279  56.507  1.000 63.770  ? 41  CYS B CB  1 ? 2 
ATOM   1461 S SG  . CYS B 1 45  ? 27.190 11.976  55.631  1.000 74.703  ? 41  CYS B SG  1 ? 2 
ATOM   1462 N N   . LEU B 1 46  ? 27.746 13.209  59.309  1.000 51.288  ? 42  LEU B N   1 ? 2 
ATOM   1463 C CA  . LEU B 1 46  ? 28.859 12.919  60.255  1.000 49.101  ? 42  LEU B CA  1 ? 2 
ATOM   1464 C C   . LEU B 1 46  ? 28.323 12.098  61.441  1.000 48.052  ? 42  LEU B C   1 ? 2 
ATOM   1465 O O   . LEU B 1 46  ? 28.900 10.982  61.733  1.000 44.252  ? 42  LEU B O   1 ? 2 
ATOM   1466 C CB  . LEU B 1 46  ? 29.477 14.240  60.732  1.000 45.912  ? 42  LEU B CB  1 ? 2 
ATOM   1467 C CG  . LEU B 1 46  ? 30.623 14.081  61.726  1.000 42.497  ? 42  LEU B CG  1 ? 2 
ATOM   1468 C CD1 . LEU B 1 46  ? 31.670 13.149  61.163  1.000 39.924  ? 42  LEU B CD1 1 ? 2 
ATOM   1469 C CD2 . LEU B 1 46  ? 31.208 15.427  62.091  1.000 41.124  ? 42  LEU B CD2 1 ? 2 
ATOM   1470 N N   . PHE B 1 47  ? 27.258 12.597  62.088  1.000 45.489  ? 43  PHE B N   1 ? 2 
ATOM   1471 C CA  . PHE B 1 47  ? 26.701 11.958  63.314  1.000 46.616  ? 43  PHE B CA  1 ? 2 
ATOM   1472 C C   . PHE B 1 47  ? 26.254 10.538  62.962  1.000 46.310  ? 43  PHE B C   1 ? 2 
ATOM   1473 O O   . PHE B 1 47  ? 26.471 9.552   63.732  1.000 44.812  ? 43  PHE B O   1 ? 2 
ATOM   1474 C CB  . PHE B 1 47  ? 25.618 12.836  63.932  1.000 45.420  ? 43  PHE B CB  1 ? 2 
ATOM   1475 C CG  . PHE B 1 47  ? 26.179 13.829  64.909  1.000 46.325  ? 43  PHE B CG  1 ? 2 
ATOM   1476 C CD1 . PHE B 1 47  ? 26.113 13.592  66.271  1.000 48.001  ? 43  PHE B CD1 1 ? 2 
ATOM   1477 C CD2 . PHE B 1 47  ? 26.824 14.968  64.466  1.000 46.043  ? 43  PHE B CD2 1 ? 2 
ATOM   1478 C CE1 . PHE B 1 47  ? 26.619 14.506  67.179  1.000 48.232  ? 43  PHE B CE1 1 ? 2 
ATOM   1479 C CE2 . PHE B 1 47  ? 27.361 15.867  65.372  1.000 47.263  ? 43  PHE B CE2 1 ? 2 
ATOM   1480 C CZ  . PHE B 1 47  ? 27.251 15.640  66.730  1.000 48.948  ? 43  PHE B CZ  1 ? 2 
ATOM   1481 N N   . SER B 1 48  ? 25.695 10.411  61.764  1.000 47.487  ? 44  SER B N   1 ? 2 
ATOM   1482 C CA  . SER B 1 48  ? 25.203 9.111   61.264  1.000 48.801  ? 44  SER B CA  1 ? 2 
ATOM   1483 C C   . SER B 1 48  ? 26.401 8.180   60.995  1.000 47.417  ? 44  SER B C   1 ? 2 
ATOM   1484 O O   . SER B 1 48  ? 26.293 6.996   61.368  1.000 42.055  ? 44  SER B O   1 ? 2 
ATOM   1485 C CB  . SER B 1 48  ? 24.279 9.294   60.090  1.000 50.348  ? 44  SER B CB  1 ? 2 
ATOM   1486 O OG  . SER B 1 48  ? 23.909 8.032   59.550  1.000 51.989  ? 44  SER B OG  1 ? 2 
ATOM   1487 N N   . GLU B 1 49  ? 27.519 8.667   60.429  1.000 48.881  ? 45  GLU B N   1 ? 2 
ATOM   1488 C CA  . GLU B 1 49  ? 28.669 7.758   60.146  1.000 50.824  ? 45  GLU B CA  1 ? 2 
ATOM   1489 C C   . GLU B 1 49  ? 29.236 7.320   61.510  1.000 48.407  ? 45  GLU B C   1 ? 2 
ATOM   1490 O O   . GLU B 1 49  ? 29.704 6.155   61.664  1.000 45.719  ? 45  GLU B O   1 ? 2 
ATOM   1491 C CB  . GLU B 1 49  ? 29.737 8.383   59.232  1.000 54.644  ? 45  GLU B CB  1 ? 2 
ATOM   1492 C CG  . GLU B 1 49  ? 29.226 9.280   58.101  1.000 56.004  ? 45  GLU B CG  1 ? 2 
ATOM   1493 C CD  . GLU B 1 49  ? 30.288 9.628   57.055  1.000 56.622  ? 45  GLU B CD  1 ? 2 
ATOM   1494 O OE1 . GLU B 1 49  ? 30.564 10.848  56.821  1.000 56.591  ? 45  GLU B OE1 1 ? 2 
ATOM   1495 O OE2 . GLU B 1 49  ? 30.834 8.690   56.459  1.000 55.492  ? 45  GLU B OE2 1 ? 2 
ATOM   1496 N N   . MET B 1 50  ? 29.131 8.181   62.520  1.000 47.624  ? 46  MET B N   1 ? 2 
ATOM   1497 C CA  . MET B 1 50  ? 29.622 7.816   63.877  1.000 48.007  ? 46  MET B CA  1 ? 2 
ATOM   1498 C C   . MET B 1 50  ? 28.743 6.696   64.459  1.000 48.419  ? 46  MET B C   1 ? 2 
ATOM   1499 O O   . MET B 1 50  ? 29.282 5.584   64.802  1.000 47.370  ? 46  MET B O   1 ? 2 
ATOM   1500 C CB  . MET B 1 50  ? 29.712 9.040   64.793  1.000 45.181  ? 46  MET B CB  1 ? 2 
ATOM   1501 C CG  . MET B 1 50  ? 30.858 9.917   64.397  1.000 41.778  ? 46  MET B CG  1 ? 2 
ATOM   1502 S SD  . MET B 1 50  ? 31.304 11.107  65.660  1.000 40.331  ? 46  MET B SD  1 ? 2 
ATOM   1503 C CE  . MET B 1 50  ? 29.926 12.257  65.597  1.000 39.970  ? 46  MET B CE  1 ? 2 
ATOM   1504 N N   . ALA B 1 51  ? 27.436 6.916   64.527  1.000 48.776  ? 47  ALA B N   1 ? 2 
ATOM   1505 C CA  . ALA B 1 51  ? 26.523 5.855   65.001  1.000 49.799  ? 47  ALA B CA  1 ? 2 
ATOM   1506 C C   . ALA B 1 51  ? 26.828 4.576   64.199  1.000 51.719  ? 47  ALA B C   1 ? 2 
ATOM   1507 O O   . ALA B 1 51  ? 27.016 3.484   64.808  1.000 50.866  ? 47  ALA B O   1 ? 2 
ATOM   1508 C CB  . ALA B 1 51  ? 25.102 6.344   64.897  1.000 49.009  ? 47  ALA B CB  1 ? 2 
ATOM   1509 N N   . GLU B 1 52  ? 26.982 4.706   62.875  1.000 57.982  ? 48  GLU B N   1 ? 2 
ATOM   1510 C CA  . GLU B 1 52  ? 27.182 3.546   61.953  1.000 63.934  ? 48  GLU B CA  1 ? 2 
ATOM   1511 C C   . GLU B 1 52  ? 28.422 2.788   62.429  1.000 60.461  ? 48  GLU B C   1 ? 2 
ATOM   1512 O O   . GLU B 1 52  ? 28.336 1.555   62.563  1.000 64.276  ? 48  GLU B O   1 ? 2 
ATOM   1513 C CB  . GLU B 1 52  ? 27.301 3.947   60.473  1.000 72.058  ? 48  GLU B CB  1 ? 2 
ATOM   1514 C CG  . GLU B 1 52  ? 26.946 2.812   59.506  1.000 78.732  ? 48  GLU B CG  1 ? 2 
ATOM   1515 C CD  . GLU B 1 52  ? 28.042 1.805   59.130  1.000 86.502  ? 48  GLU B CD  1 ? 2 
ATOM   1516 O OE1 . GLU B 1 52  ? 28.824 2.105   58.179  1.000 88.027  ? 48  GLU B OE1 1 ? 2 
ATOM   1517 O OE2 . GLU B 1 52  ? 28.105 0.693   59.756  1.000 87.342  ? 48  GLU B OE2 1 ? 2 
ATOM   1518 N N   . GLN B 1 53  ? 29.496 3.518   62.734  1.000 56.771  ? 49  GLN B N   1 ? 2 
ATOM   1519 C CA  . GLN B 1 53  ? 30.813 2.943   63.132  1.000 56.670  ? 49  GLN B CA  1 ? 2 
ATOM   1520 C C   . GLN B 1 53  ? 30.674 2.156   64.448  1.000 55.438  ? 49  GLN B C   1 ? 2 
ATOM   1521 O O   . GLN B 1 53  ? 31.406 1.122   64.647  1.000 51.269  ? 49  GLN B O   1 ? 2 
ATOM   1522 C CB  . GLN B 1 53  ? 31.833 4.079   63.152  1.000 56.406  ? 49  GLN B CB  1 ? 2 
ATOM   1523 C CG  . GLN B 1 53  ? 33.213 3.686   63.659  1.000 58.302  ? 49  GLN B CG  1 ? 2 
ATOM   1524 C CD  . GLN B 1 53  ? 33.970 2.800   62.715  1.000 58.529  ? 49  GLN B CD  1 ? 2 
ATOM   1525 O OE1 . GLN B 1 53  ? 33.586 2.644   61.560  1.000 60.595  ? 49  GLN B OE1 1 ? 2 
ATOM   1526 N NE2 . GLN B 1 53  ? 35.051 2.225   63.216  1.000 57.760  ? 49  GLN B NE2 1 ? 2 
ATOM   1527 N N   . LEU B 1 54  ? 29.726 2.560   65.299  1.000 54.682  ? 50  LEU B N   1 ? 2 
ATOM   1528 C CA  . LEU B 1 54  ? 29.505 1.868   66.594  1.000 57.113  ? 50  LEU B CA  1 ? 2 
ATOM   1529 C C   . LEU B 1 54  ? 28.719 0.549   66.372  1.000 61.883  ? 50  LEU B C   1 ? 2 
ATOM   1530 O O   . LEU B 1 54  ? 29.002 -0.453  67.103  1.000 63.020  ? 50  LEU B O   1 ? 2 
ATOM   1531 C CB  . LEU B 1 54  ? 28.867 2.857   67.588  1.000 53.411  ? 50  LEU B CB  1 ? 2 
ATOM   1532 C CG  . LEU B 1 54  ? 29.773 4.010   68.071  1.000 48.321  ? 50  LEU B CG  1 ? 2 
ATOM   1533 C CD1 . LEU B 1 54  ? 29.030 5.012   68.955  1.000 45.758  ? 50  LEU B CD1 1 ? 2 
ATOM   1534 C CD2 . LEU B 1 54  ? 31.008 3.498   68.789  1.000 45.905  ? 50  LEU B CD2 1 ? 2 
ATOM   1535 N N   . SER B 1 55  ? 27.819 0.486   65.381  1.000 64.885  ? 51  SER B N   1 ? 2 
ATOM   1536 C CA  . SER B 1 55  ? 27.096 -0.768  65.011  1.000 65.530  ? 51  SER B CA  1 ? 2 
ATOM   1537 C C   . SER B 1 55  ? 28.059 -1.840  64.505  1.000 64.214  ? 51  SER B C   1 ? 2 
ATOM   1538 O O   . SER B 1 55  ? 27.840 -2.996  64.790  1.000 64.867  ? 51  SER B O   1 ? 2 
ATOM   1539 C CB  . SER B 1 55  ? 26.050 -0.492  63.993  1.000 65.094  ? 51  SER B CB  1 ? 2 
ATOM   1540 O OG  . SER B 1 55  ? 25.192 0.510   64.491  1.000 66.799  ? 51  SER B OG  1 ? 2 
ATOM   1541 N N   . GLU B 1 56  ? 29.075 -1.459  63.752  1.000 67.863  ? 52  GLU B N   1 ? 2 
ATOM   1542 C CA  . GLU B 1 56  ? 29.985 -2.408  63.060  1.000 74.328  ? 52  GLU B CA  1 ? 2 
ATOM   1543 C C   . GLU B 1 56  ? 30.910 -3.063  64.087  1.000 72.940  ? 52  GLU B C   1 ? 2 
ATOM   1544 O O   . GLU B 1 56  ? 31.321 -4.198  63.839  1.000 73.593  ? 52  GLU B O   1 ? 2 
ATOM   1545 C CB  . GLU B 1 56  ? 30.777 -1.676  61.966  1.000 77.124  ? 52  GLU B CB  1 ? 2 
ATOM   1546 C CG  . GLU B 1 56  ? 31.495 -2.575  60.977  1.000 81.060  ? 52  GLU B CG  1 ? 2 
ATOM   1547 C CD  . GLU B 1 56  ? 31.492 -2.026  59.553  1.000 85.300  ? 52  GLU B CD  1 ? 2 
ATOM   1548 O OE1 . GLU B 1 56  ? 30.814 -0.995  59.313  1.000 85.042  ? 52  GLU B OE1 1 ? 2 
ATOM   1549 O OE2 . GLU B 1 56  ? 32.148 -2.636  58.678  1.000 88.757  ? 52  GLU B OE2 1 ? 2 
ATOM   1550 N N   . LYS B 1 57  ? 31.244 -2.359  65.175  1.000 75.392  ? 53  LYS B N   1 ? 2 
ATOM   1551 C CA  . LYS B 1 57  ? 32.302 -2.782  66.134  1.000 75.499  ? 53  LYS B CA  1 ? 2 
ATOM   1552 C C   . LYS B 1 57  ? 31.684 -3.287  67.452  1.000 73.779  ? 53  LYS B C   1 ? 2 
ATOM   1553 O O   . LYS B 1 57  ? 32.384 -4.073  68.130  1.000 69.006  ? 53  LYS B O   1 ? 2 
ATOM   1554 C CB  . LYS B 1 57  ? 33.278 -1.624  66.354  1.000 76.060  ? 53  LYS B CB  1 ? 2 
ATOM   1555 C CG  . LYS B 1 57  ? 34.156 -1.275  65.159  1.000 73.859  ? 53  LYS B CG  1 ? 2 
ATOM   1556 C CD  . LYS B 1 57  ? 35.563 -0.909  65.604  1.000 74.534  ? 53  LYS B CD  1 ? 2 
ATOM   1557 C CE  . LYS B 1 57  ? 36.541 -0.717  64.466  1.000 74.985  ? 53  LYS B CE  1 ? 2 
ATOM   1558 N NZ  . LYS B 1 57  ? 36.760 -1.981  63.727  1.000 76.641  ? 53  LYS B NZ  1 ? 2 
ATOM   1559 N N   . ASP B 1 58  ? 30.455 -2.838  67.780  1.000 74.046  ? 54  ASP B N   1 ? 2 
ATOM   1560 C CA  . ASP B 1 58  ? 29.568 -3.260  68.911  1.000 79.742  ? 54  ASP B CA  1 ? 2 
ATOM   1561 C C   . ASP B 1 58  ? 30.296 -3.286  70.269  1.000 79.196  ? 54  ASP B C   1 ? 2 
ATOM   1562 O O   . ASP B 1 58  ? 30.555 -4.343  70.867  1.000 75.946  ? 54  ASP B O   1 ? 2 
ATOM   1563 C CB  . ASP B 1 58  ? 28.862 -4.583  68.620  1.000 82.003  ? 54  ASP B CB  1 ? 2 
ATOM   1564 C CG  . ASP B 1 58  ? 27.836 -4.933  69.685  1.000 88.831  ? 54  ASP B CG  1 ? 2 
ATOM   1565 O OD1 . ASP B 1 58  ? 27.123 -3.999  70.174  1.000 90.236  ? 54  ASP B OD1 1 ? 2 
ATOM   1566 O OD2 . ASP B 1 58  ? 27.791 -6.122  70.050  1.000 94.043  ? 54  ASP B OD2 1 ? 2 
ATOM   1567 N N   . PRO B 1 59  ? 30.560 -2.095  70.851  1.000 73.966  ? 55  PRO B N   1 ? 2 
ATOM   1568 C CA  . PRO B 1 59  ? 31.322 -1.995  72.096  1.000 69.195  ? 55  PRO B CA  1 ? 2 
ATOM   1569 C C   . PRO B 1 59  ? 30.504 -2.439  73.312  1.000 64.244  ? 55  PRO B C   1 ? 2 
ATOM   1570 O O   . PRO B 1 59  ? 29.311 -2.198  73.323  1.000 59.669  ? 55  PRO B O   1 ? 2 
ATOM   1571 C CB  . PRO B 1 59  ? 31.609 -0.495  72.186  1.000 68.850  ? 55  PRO B CB  1 ? 2 
ATOM   1572 C CG  . PRO B 1 59  ? 30.405 0.143   71.507  1.000 71.311  ? 55  PRO B CG  1 ? 2 
ATOM   1573 C CD  . PRO B 1 59  ? 30.080 -0.789  70.360  1.000 72.460  ? 55  PRO B CD  1 ? 2 
ATOM   1574 N N   . LYS B 1 60  ? 31.189 -2.979  74.322  1.000 66.277  ? 56  LYS B N   1 ? 2 
ATOM   1575 C CA  . LYS B 1 60  ? 30.597 -3.555  75.566  1.000 64.825  ? 56  LYS B CA  1 ? 2 
ATOM   1576 C C   . LYS B 1 60  ? 30.144 -2.462  76.552  1.000 58.845  ? 56  LYS B C   1 ? 2 
ATOM   1577 O O   . LYS B 1 60  ? 29.261 -2.785  77.380  1.000 63.264  ? 56  LYS B O   1 ? 2 
ATOM   1578 C CB  . LYS B 1 60  ? 31.617 -4.520  76.188  1.000 68.192  ? 56  LYS B CB  1 ? 2 
ATOM   1579 C CG  . LYS B 1 60  ? 31.996 -5.702  75.299  1.000 71.199  ? 56  LYS B CG  1 ? 2 
ATOM   1580 C CD  . LYS B 1 60  ? 33.438 -6.125  75.471  1.000 77.155  ? 56  LYS B CD  1 ? 2 
ATOM   1581 C CE  . LYS B 1 60  ? 34.035 -6.830  74.271  1.000 83.497  ? 56  LYS B CE  1 ? 2 
ATOM   1582 N NZ  . LYS B 1 60  ? 34.404 -8.226  74.609  1.000 89.718  ? 56  LYS B NZ  1 ? 2 
ATOM   1583 N N   . THR B 1 61  ? 30.748 -1.256  76.500  1.000 53.050  ? 57  THR B N   1 ? 2 
ATOM   1584 C CA  . THR B 1 61  ? 30.594 -0.104  77.456  1.000 47.481  ? 57  THR B CA  1 ? 2 
ATOM   1585 C C   . THR B 1 61  ? 30.542 1.250   76.715  1.000 45.155  ? 57  THR B C   1 ? 2 
ATOM   1586 O O   . THR B 1 61  ? 31.026 1.335   75.517  1.000 44.626  ? 57  THR B O   1 ? 2 
ATOM   1587 C CB  . THR B 1 61  ? 31.776 -0.021  78.439  1.000 45.551  ? 57  THR B CB  1 ? 2 
ATOM   1588 O OG1 . THR B 1 61  ? 32.832 0.839   77.996  1.000 41.695  ? 57  THR B OG1 1 ? 2 
ATOM   1589 C CG2 . THR B 1 61  ? 32.401 -1.365  78.732  1.000 46.107  ? 57  THR B CG2 1 ? 2 
ATOM   1590 N N   . GLU B 1 62  ? 30.087 2.317   77.386  1.000 41.161  ? 58  GLU B N   1 ? 2 
ATOM   1591 C CA  A GLU B 1 62  ? 30.180 3.681   76.819  0.500 40.177  ? 58  GLU B CA  1 ? 2 
ATOM   1592 C CA  B GLU B 1 62  ? 30.178 3.697   76.822  0.500 40.180  ? 58  GLU B CA  1 ? 2 
ATOM   1593 C C   . GLU B 1 62  ? 31.658 4.091   76.666  1.000 41.006  ? 58  GLU B C   1 ? 2 
ATOM   1594 O O   . GLU B 1 62  ? 31.966 4.810   75.668  1.000 41.460  ? 58  GLU B O   1 ? 2 
ATOM   1595 C CB  A GLU B 1 62  ? 29.370 4.656   77.662  0.500 39.332  ? 58  GLU B CB  1 ? 2 
ATOM   1596 C CB  B GLU B 1 62  ? 29.485 4.780   77.657  0.500 39.323  ? 58  GLU B CB  1 ? 2 
ATOM   1597 C CG  A GLU B 1 62  ? 27.881 4.409   77.570  0.500 39.142  ? 58  GLU B CG  1 ? 2 
ATOM   1598 C CG  B GLU B 1 62  ? 29.306 6.130   76.930  0.500 37.960  ? 58  GLU B CG  1 ? 2 
ATOM   1599 C CD  A GLU B 1 62  ? 27.283 3.583   78.690  0.500 39.121  ? 58  GLU B CD  1 ? 2 
ATOM   1600 C CD  B GLU B 1 62  ? 30.353 7.248   77.030  0.500 36.597  ? 58  GLU B CD  1 ? 2 
ATOM   1601 O OE1 A GLU B 1 62  ? 27.955 2.661   79.231  0.500 37.062  ? 58  GLU B OE1 1 ? 2 
ATOM   1602 O OE1 B GLU B 1 62  ? 31.530 7.004   77.384  0.500 36.080  ? 58  GLU B OE1 1 ? 2 
ATOM   1603 O OE2 A GLU B 1 62  ? 26.138 3.877   79.018  0.500 40.257  ? 58  GLU B OE2 1 ? 2 
ATOM   1604 O OE2 B GLU B 1 62  ? 29.985 8.388   76.733  0.500 35.080  ? 58  GLU B OE2 1 ? 2 
ATOM   1605 N N   . GLN B 1 63  ? 32.565 3.678   77.574  1.000 40.239  ? 59  GLN B N   1 ? 2 
ATOM   1606 C CA  . GLN B 1 63  ? 34.004 4.068   77.393  1.000 39.691  ? 59  GLN B CA  1 ? 2 
ATOM   1607 C C   . GLN B 1 63  ? 34.566 3.436   76.106  1.000 40.942  ? 59  GLN B C   1 ? 2 
ATOM   1608 O O   . GLN B 1 63  ? 35.290 4.143   75.395  1.000 39.716  ? 59  GLN B O   1 ? 2 
ATOM   1609 C CB  . GLN B 1 63  ? 34.918 3.741   78.585  1.000 38.262  ? 59  GLN B CB  1 ? 2 
ATOM   1610 C CG  . GLN B 1 63  ? 34.994 4.844   79.610  1.000 36.398  ? 59  GLN B CG  1 ? 2 
ATOM   1611 C CD  . GLN B 1 63  ? 35.078 6.193   78.952  1.000 35.771  ? 59  GLN B CD  1 ? 2 
ATOM   1612 O OE1 . GLN B 1 63  ? 34.055 6.845   78.696  1.000 34.737  ? 59  GLN B OE1 1 ? 2 
ATOM   1613 N NE2 . GLN B 1 63  ? 36.305 6.591   78.642  1.000 34.581  ? 59  GLN B NE2 1 ? 2 
ATOM   1614 N N   . GLU B 1 64  ? 34.251 2.172   75.814  1.000 43.062  ? 60  GLU B N   1 ? 2 
ATOM   1615 C CA  . GLU B 1 64  ? 34.685 1.480   74.570  1.000 45.869  ? 60  GLU B CA  1 ? 2 
ATOM   1616 C C   . GLU B 1 64  ? 34.133 2.231   73.339  1.000 43.101  ? 60  GLU B C   1 ? 2 
ATOM   1617 O O   . GLU B 1 64  ? 34.933 2.526   72.449  1.000 38.958  ? 60  GLU B O   1 ? 2 
ATOM   1618 C CB  . GLU B 1 64  ? 34.289 -0.002  74.561  1.000 51.877  ? 60  GLU B CB  1 ? 2 
ATOM   1619 C CG  . GLU B 1 64  ? 35.053 -0.852  75.586  1.000 57.898  ? 60  GLU B CG  1 ? 2 
ATOM   1620 C CD  . GLU B 1 64  ? 34.891 -2.368  75.532  1.000 62.273  ? 60  GLU B CD  1 ? 2 
ATOM   1621 O OE1 . GLU B 1 64  ? 34.450 -2.911  74.437  1.000 69.567  ? 60  GLU B OE1 1 ? 2 
ATOM   1622 O OE2 . GLU B 1 64  ? 35.229 -3.012  76.576  1.000 61.156  ? 60  GLU B OE2 1 ? 2 
ATOM   1623 N N   . ALA B 1 65  ? 32.835 2.550   73.294  1.000 40.755  ? 61  ALA B N   1 ? 2 
ATOM   1624 C CA  . ALA B 1 65  ? 32.223 3.377   72.236  1.000 38.995  ? 61  ALA B CA  1 ? 2 
ATOM   1625 C C   . ALA B 1 65  ? 33.031 4.661   72.025  1.000 39.744  ? 61  ALA B C   1 ? 2 
ATOM   1626 O O   . ALA B 1 65  ? 33.394 4.969   70.875  1.000 45.931  ? 61  ALA B O   1 ? 2 
ATOM   1627 C CB  . ALA B 1 65  ? 30.801 3.688   72.584  1.000 38.909  ? 61  ALA B CB  1 ? 2 
ATOM   1628 N N   . GLU B 1 66  ? 33.348 5.400   73.079  1.000 38.564  ? 62  GLU B N   1 ? 2 
ATOM   1629 C CA  . GLU B 1 66  ? 33.967 6.746   72.938  1.000 37.569  ? 62  GLU B CA  1 ? 2 
ATOM   1630 C C   . GLU B 1 66  ? 35.356 6.577   72.334  1.000 37.561  ? 62  GLU B C   1 ? 2 
ATOM   1631 O O   . GLU B 1 66  ? 35.696 7.356   71.486  1.000 37.209  ? 62  GLU B O   1 ? 2 
ATOM   1632 C CB  . GLU B 1 66  ? 34.001 7.449   74.290  1.000 36.149  ? 62  GLU B CB  1 ? 2 
ATOM   1633 C CG  . GLU B 1 66  ? 34.810 8.717   74.316  1.000 34.347  ? 62  GLU B CG  1 ? 2 
ATOM   1634 C CD  . GLU B 1 66  ? 34.568 9.546   75.564  1.000 33.188  ? 62  GLU B CD  1 ? 2 
ATOM   1635 O OE1 . GLU B 1 66  ? 33.562 9.265   76.315  1.000 32.617  ? 62  GLU B OE1 1 ? 2 
ATOM   1636 O OE2 . GLU B 1 66  ? 35.336 10.507  75.746  1.000 31.219  ? 62  GLU B OE2 1 ? 2 
ATOM   1637 N N   . ARG B 1 67  ? 36.096 5.570   72.790  1.000 40.425  ? 63  ARG B N   1 ? 2 
ATOM   1638 C CA  . ARG B 1 67  ? 37.411 5.174   72.227  1.000 42.392  ? 63  ARG B CA  1 ? 2 
ATOM   1639 C C   . ARG B 1 67  ? 37.219 5.001   70.705  1.000 39.212  ? 63  ARG B C   1 ? 2 
ATOM   1640 O O   . ARG B 1 67  ? 37.906 5.698   69.948  1.000 35.925  ? 63  ARG B O   1 ? 2 
ATOM   1641 C CB  . ARG B 1 67  ? 37.912 3.936   72.969  1.000 45.048  ? 63  ARG B CB  1 ? 2 
ATOM   1642 C CG  . ARG B 1 67  ? 39.289 3.418   72.581  1.000 48.780  ? 63  ARG B CG  1 ? 2 
ATOM   1643 C CD  . ARG B 1 67  ? 39.455 2.021   73.193  1.000 55.368  ? 63  ARG B CD  1 ? 2 
ATOM   1644 N NE  . ARG B 1 67  ? 39.256 2.073   74.668  1.000 63.680  ? 63  ARG B NE  1 ? 2 
ATOM   1645 C CZ  . ARG B 1 67  ? 38.820 1.081   75.466  1.000 66.216  ? 63  ARG B CZ  1 ? 2 
ATOM   1646 N NH1 . ARG B 1 67  ? 38.512 -0.099  74.946  1.000 67.630  ? 63  ARG B NH1 1 ? 2 
ATOM   1647 N NH2 . ARG B 1 67  ? 38.704 1.285   76.777  1.000 67.117  ? 63  ARG B NH2 1 ? 2 
ATOM   1648 N N   . ILE B 1 68  ? 36.241 4.202   70.296  1.000 38.044  ? 64  ILE B N   1 ? 2 
ATOM   1649 C CA  . ILE B 1 68  ? 35.982 3.883   68.867  1.000 38.140  ? 64  ILE B CA  1 ? 2 
ATOM   1650 C C   . ILE B 1 68  ? 35.743 5.187   68.098  1.000 36.126  ? 64  ILE B C   1 ? 2 
ATOM   1651 O O   . ILE B 1 68  ? 36.330 5.324   67.026  1.000 37.487  ? 64  ILE B O   1 ? 2 
ATOM   1652 C CB  . ILE B 1 68  ? 34.817 2.903   68.688  1.000 39.460  ? 64  ILE B CB  1 ? 2 
ATOM   1653 C CG1 . ILE B 1 68  ? 35.132 1.514   69.256  1.000 40.132  ? 64  ILE B CG1 1 ? 2 
ATOM   1654 C CG2 . ILE B 1 68  ? 34.453 2.833   67.213  1.000 40.456  ? 64  ILE B CG2 1 ? 2 
ATOM   1655 C CD1 . ILE B 1 68  ? 33.910 0.623   69.396  1.000 40.247  ? 64  ILE B CD1 1 ? 2 
ATOM   1656 N N   . LEU B 1 69  ? 34.999 6.143   68.643  1.000 35.214  ? 65  LEU B N   1 ? 2 
ATOM   1657 C CA  . LEU B 1 69  ? 34.754 7.422   67.925  1.000 34.780  ? 65  LEU B CA  1 ? 2 
ATOM   1658 C C   . LEU B 1 69  ? 36.047 8.242   67.837  1.000 34.328  ? 65  LEU B C   1 ? 2 
ATOM   1659 O O   . LEU B 1 69  ? 36.244 8.901   66.776  1.000 33.237  ? 65  LEU B O   1 ? 2 
ATOM   1660 C CB  . LEU B 1 69  ? 33.653 8.230   68.617  1.000 34.991  ? 65  LEU B CB  1 ? 2 
ATOM   1661 C CG  . LEU B 1 69  ? 32.233 7.671   68.555  1.000 35.927  ? 65  LEU B CG  1 ? 2 
ATOM   1662 C CD1 . LEU B 1 69  ? 31.238 8.775   68.876  1.000 37.238  ? 65  LEU B CD1 1 ? 2 
ATOM   1663 C CD2 . LEU B 1 69  ? 31.903 7.055   67.211  1.000 35.788  ? 65  LEU B CD2 1 ? 2 
ATOM   1664 N N   . LEU B 1 70  ? 36.864 8.246   68.907  1.000 33.872  ? 66  LEU B N   1 ? 2 
ATOM   1665 C CA  . LEU B 1 70  ? 38.196 8.908   68.913  1.000 33.192  ? 66  LEU B CA  1 ? 2 
ATOM   1666 C C   . LEU B 1 70  ? 39.129 8.241   67.861  1.000 34.395  ? 66  LEU B C   1 ? 2 
ATOM   1667 O O   . LEU B 1 70  ? 39.871 8.971   67.237  1.000 33.390  ? 66  LEU B O   1 ? 2 
ATOM   1668 C CB  . LEU B 1 70  ? 38.768 8.870   70.335  1.000 31.769  ? 66  LEU B CB  1 ? 2 
ATOM   1669 C CG  . LEU B 1 70  ? 40.183 9.466   70.479  1.000 31.455  ? 66  LEU B CG  1 ? 2 
ATOM   1670 C CD1 . LEU B 1 70  ? 40.274 10.880  69.882  1.000 30.520  ? 66  LEU B CD1 1 ? 2 
ATOM   1671 C CD2 . LEU B 1 70  ? 40.651 9.501   71.923  1.000 31.191  ? 66  LEU B CD2 1 ? 2 
ATOM   1672 N N   . GLU B 1 71  ? 39.105 6.912   67.671  1.000 37.112  ? 67  GLU B N   1 ? 2 
ATOM   1673 C CA  . GLU B 1 71  ? 39.932 6.180   66.673  1.000 40.644  ? 67  GLU B CA  1 ? 2 
ATOM   1674 C C   . GLU B 1 71  ? 39.436 6.510   65.233  1.000 40.202  ? 67  GLU B C   1 ? 2 
ATOM   1675 O O   . GLU B 1 71  ? 40.276 6.813   64.357  1.000 36.991  ? 67  GLU B O   1 ? 2 
ATOM   1676 C CB  . GLU B 1 71  ? 39.943 4.673   66.956  1.000 44.535  ? 67  GLU B CB  1 ? 2 
ATOM   1677 C CG  . GLU B 1 71  ? 40.885 4.266   68.094  1.000 51.279  ? 67  GLU B CG  1 ? 2 
ATOM   1678 C CD  . GLU B 1 71  ? 40.790 2.848   68.706  1.000 55.283  ? 67  GLU B CD  1 ? 2 
ATOM   1679 O OE1 . GLU B 1 71  ? 39.834 2.082   68.365  1.000 62.602  ? 67  GLU B OE1 1 ? 2 
ATOM   1680 O OE2 . GLU B 1 71  ? 41.679 2.484   69.538  1.000 54.870  ? 67  GLU B OE2 1 ? 2 
ATOM   1681 N N   . PHE B 1 72  ? 38.125 6.477   65.011  1.000 37.072  ? 68  PHE B N   1 ? 2 
ATOM   1682 C CA  . PHE B 1 72  ? 37.441 6.794   63.742  1.000 37.604  ? 68  PHE B CA  1 ? 2 
ATOM   1683 C C   . PHE B 1 72  ? 37.913 8.148   63.187  1.000 37.800  ? 68  PHE B C   1 ? 2 
ATOM   1684 O O   . PHE B 1 72  ? 38.389 8.263   62.038  1.000 37.754  ? 68  PHE B O   1 ? 2 
ATOM   1685 C CB  . PHE B 1 72  ? 35.941 6.756   64.019  1.000 37.942  ? 68  PHE B CB  1 ? 2 
ATOM   1686 C CG  . PHE B 1 72  ? 35.066 7.007   62.825  1.000 39.877  ? 68  PHE B CG  1 ? 2 
ATOM   1687 C CD1 . PHE B 1 72  ? 35.146 6.183   61.704  1.000 42.197  ? 68  PHE B CD1 1 ? 2 
ATOM   1688 C CD2 . PHE B 1 72  ? 34.138 8.048   62.812  1.000 39.763  ? 68  PHE B CD2 1 ? 2 
ATOM   1689 C CE1 . PHE B 1 72  ? 34.349 6.420   60.588  1.000 39.814  ? 68  PHE B CE1 1 ? 2 
ATOM   1690 C CE2 . PHE B 1 72  ? 33.344 8.275   61.691  1.000 39.272  ? 68  PHE B CE2 1 ? 2 
ATOM   1691 C CZ  . PHE B 1 72  ? 33.448 7.459   60.589  1.000 38.107  ? 68  PHE B CZ  1 ? 2 
ATOM   1692 N N   . LEU B 1 73  ? 37.791 9.183   63.999  1.000 39.077  ? 69  LEU B N   1 ? 2 
ATOM   1693 C CA  . LEU B 1 73  ? 38.136 10.575  63.624  1.000 38.763  ? 69  LEU B CA  1 ? 2 
ATOM   1694 C C   . LEU B 1 73  ? 39.643 10.708  63.375  1.000 39.862  ? 69  LEU B C   1 ? 2 
ATOM   1695 O O   . LEU B 1 73  ? 40.026 11.563  62.552  1.000 40.349  ? 69  LEU B O   1 ? 2 
ATOM   1696 C CB  . LEU B 1 73  ? 37.679 11.488  64.768  1.000 38.943  ? 69  LEU B CB  1 ? 2 
ATOM   1697 C CG  . LEU B 1 73  ? 36.158 11.672  64.866  1.000 38.440  ? 69  LEU B CG  1 ? 2 
ATOM   1698 C CD1 . LEU B 1 73  ? 35.816 12.729  65.916  1.000 38.653  ? 69  LEU B CD1 1 ? 2 
ATOM   1699 C CD2 . LEU B 1 73  ? 35.551 12.032  63.515  1.000 34.877  ? 69  LEU B CD2 1 ? 2 
ATOM   1700 N N   . THR B 1 74  ? 40.459 9.941   64.112  1.000 39.527  ? 70  THR B N   1 ? 2 
ATOM   1701 C CA  . THR B 1 74  ? 41.939 10.022  64.088  1.000 37.641  ? 70  THR B CA  1 ? 2 
ATOM   1702 C C   . THR B 1 74  ? 42.376 9.440   62.736  1.000 37.397  ? 70  THR B C   1 ? 2 
ATOM   1703 O O   . THR B 1 74  ? 43.256 10.045  62.101  1.000 34.992  ? 70  THR B O   1 ? 2 
ATOM   1704 C CB  . THR B 1 74  ? 42.553 9.353   65.337  1.000 35.216  ? 70  THR B CB  1 ? 2 
ATOM   1705 O OG1 . THR B 1 74  ? 42.251 10.187  66.458  1.000 34.030  ? 70  THR B OG1 1 ? 2 
ATOM   1706 C CG2 . THR B 1 74  ? 44.053 9.143   65.255  1.000 33.510  ? 70  THR B CG2 1 ? 2 
ATOM   1707 N N   . HIS B 1 75  ? 41.801 8.289   62.367  1.000 38.903  ? 71  HIS B N   1 ? 2 
ATOM   1708 C CA  . HIS B 1 75  ? 42.098 7.549   61.116  1.000 41.797  ? 71  HIS B CA  1 ? 2 
ATOM   1709 C C   . HIS B 1 75  ? 41.695 8.441   59.916  1.000 41.832  ? 71  HIS B C   1 ? 2 
ATOM   1710 O O   . HIS B 1 75  ? 42.525 8.605   59.031  1.000 42.872  ? 71  HIS B O   1 ? 2 
ATOM   1711 C CB  . HIS B 1 75  ? 41.464 6.159   61.142  1.000 42.968  ? 71  HIS B CB  1 ? 2 
ATOM   1712 C CG  . HIS B 1 75  ? 41.758 5.341   59.920  1.000 50.960  ? 71  HIS B CG  1 ? 2 
ATOM   1713 N ND1 . HIS B 1 75  ? 43.041 4.885   59.612  1.000 53.179  ? 71  HIS B ND1 1 ? 2 
ATOM   1714 C CD2 . HIS B 1 75  ? 40.947 4.870   58.934  1.000 51.989  ? 71  HIS B CD2 1 ? 2 
ATOM   1715 C CE1 . HIS B 1 75  ? 42.993 4.183   58.495  1.000 53.127  ? 71  HIS B CE1 1 ? 2 
ATOM   1716 N NE2 . HIS B 1 75  ? 41.724 4.151   58.070  1.000 51.060  ? 71  HIS B NE2 1 ? 2 
ATOM   1717 N N   . ARG B 1 76  ? 40.531 9.101   59.955  1.000 39.244  ? 72  ARG B N   1 ? 2 
ATOM   1718 C CA  . ARG B 1 76  ? 40.085 10.096  58.946  1.000 36.983  ? 72  ARG B CA  1 ? 2 
ATOM   1719 C C   . ARG B 1 76  ? 40.992 11.331  58.854  1.000 35.600  ? 72  ARG B C   1 ? 2 
ATOM   1720 O O   . ARG B 1 76  ? 41.067 11.949  57.747  1.000 33.370  ? 72  ARG B O   1 ? 2 
ATOM   1721 C CB  . ARG B 1 76  ? 38.690 10.577  59.291  1.000 36.760  ? 72  ARG B CB  1 ? 2 
ATOM   1722 C CG  . ARG B 1 76  ? 37.595 9.554   59.070  1.000 37.487  ? 72  ARG B CG  1 ? 2 
ATOM   1723 C CD  . ARG B 1 76  ? 36.415 10.164  59.780  1.000 39.106  ? 72  ARG B CD  1 ? 2 
ATOM   1724 N NE  . ARG B 1 76  ? 35.270 10.042  58.938  1.000 42.651  ? 72  ARG B NE  1 ? 2 
ATOM   1725 C CZ  . ARG B 1 76  ? 34.571 11.035  58.412  1.000 42.684  ? 72  ARG B CZ  1 ? 2 
ATOM   1726 N NH1 . ARG B 1 76  ? 34.831 12.306  58.641  1.000 42.516  ? 72  ARG B NH1 1 ? 2 
ATOM   1727 N NH2 . ARG B 1 76  ? 33.548 10.719  57.659  1.000 46.884  ? 72  ARG B NH2 1 ? 2 
ATOM   1728 N N   . LYS B 1 77  ? 41.592 11.742  59.964  1.000 35.831  ? 73  LYS B N   1 ? 2 
ATOM   1729 C CA  . LYS B 1 77  ? 42.543 12.880  59.949  1.000 36.536  ? 73  LYS B CA  1 ? 2 
ATOM   1730 C C   . LYS B 1 77  ? 43.772 12.404  59.182  1.000 36.011  ? 73  LYS B C   1 ? 2 
ATOM   1731 O O   . LYS B 1 77  ? 44.359 13.202  58.471  1.000 39.742  ? 73  LYS B O   1 ? 2 
ATOM   1732 C CB  . LYS B 1 77  ? 42.897 13.368  61.360  1.000 37.807  ? 73  LYS B CB  1 ? 2 
ATOM   1733 C CG  . LYS B 1 77  ? 43.541 14.752  61.457  1.000 38.521  ? 73  LYS B CG  1 ? 2 
ATOM   1734 C CD  . LYS B 1 77  ? 44.947 14.699  61.951  1.000 42.988  ? 73  LYS B CD  1 ? 2 
ATOM   1735 C CE  . LYS B 1 77  ? 45.478 16.022  62.446  1.000 44.815  ? 73  LYS B CE  1 ? 2 
ATOM   1736 N NZ  . LYS B 1 77  ? 45.857 16.874  61.298  1.000 46.583  ? 73  LYS B NZ  1 ? 2 
ATOM   1737 N N   . ALA B 1 78  ? 44.125 11.134  59.343  1.000 34.635  ? 74  ALA B N   1 ? 2 
ATOM   1738 C CA  . ALA B 1 78  ? 45.308 10.520  58.725  1.000 34.132  ? 74  ALA B CA  1 ? 2 
ATOM   1739 C C   . ALA B 1 78  ? 45.059 10.428  57.201  1.000 33.900  ? 74  ALA B C   1 ? 2 
ATOM   1740 O O   . ALA B 1 78  ? 45.950 10.880  56.462  1.000 32.982  ? 74  ALA B O   1 ? 2 
ATOM   1741 C CB  . ALA B 1 78  ? 45.595 9.179   59.357  1.000 33.057  ? 74  ALA B CB  1 ? 2 
ATOM   1742 N N   . GLU B 1 79  ? 43.907 9.883   56.785  1.000 31.896  ? 75  GLU B N   1 ? 2 
ATOM   1743 C CA  . GLU B 1 79  ? 43.498 9.763   55.367  1.000 33.446  ? 75  GLU B CA  1 ? 2 
ATOM   1744 C C   . GLU B 1 79  ? 43.551 11.158  54.740  1.000 32.145  ? 75  GLU B C   1 ? 2 
ATOM   1745 O O   . GLU B 1 79  ? 44.017 11.270  53.629  1.000 31.182  ? 75  GLU B O   1 ? 2 
ATOM   1746 C CB  . GLU B 1 79  ? 42.076 9.228   55.175  1.000 34.652  ? 75  GLU B CB  1 ? 2 
ATOM   1747 C CG  . GLU B 1 79  ? 41.879 7.788   55.605  1.000 36.383  ? 75  GLU B CG  1 ? 2 
ATOM   1748 C CD  . GLU B 1 79  ? 40.461 7.256   55.486  1.000 38.245  ? 75  GLU B CD  1 ? 2 
ATOM   1749 O OE1 . GLU B 1 79  ? 39.513 8.032   55.252  1.000 42.781  ? 75  GLU B OE1 1 ? 2 
ATOM   1750 O OE2 . GLU B 1 79  ? 40.306 6.059   55.612  1.000 40.672  ? 75  GLU B OE2 1 ? 2 
ATOM   1751 N N   . ARG B 1 80  ? 43.123 12.174  55.475  1.000 31.720  ? 76  ARG B N   1 ? 2 
ATOM   1752 C CA  . ARG B 1 80  ? 42.933 13.547  54.959  1.000 31.359  ? 76  ARG B CA  1 ? 2 
ATOM   1753 C C   . ARG B 1 80  ? 44.303 14.211  54.852  1.000 33.021  ? 76  ARG B C   1 ? 2 
ATOM   1754 O O   . ARG B 1 80  ? 44.486 15.052  53.941  1.000 30.265  ? 76  ARG B O   1 ? 2 
ATOM   1755 C CB  . ARG B 1 80  ? 41.970 14.296  55.889  1.000 30.872  ? 76  ARG B CB  1 ? 2 
ATOM   1756 C CG  . ARG B 1 80  ? 41.333 15.544  55.291  1.000 31.031  ? 76  ARG B CG  1 ? 2 
ATOM   1757 C CD  . ARG B 1 80  ? 39.864 15.740  55.654  1.000 31.382  ? 76  ARG B CD  1 ? 2 
ATOM   1758 N NE  . ARG B 1 80  ? 39.835 15.750  57.071  1.000 33.975  ? 76  ARG B NE  1 ? 2 
ATOM   1759 C CZ  . ARG B 1 80  ? 39.119 14.996  57.891  1.000 34.444  ? 76  ARG B CZ  1 ? 2 
ATOM   1760 N NH1 . ARG B 1 80  ? 38.141 14.194  57.494  1.000 32.852  ? 76  ARG B NH1 1 ? 2 
ATOM   1761 N NH2 . ARG B 1 80  ? 39.416 15.130  59.171  1.000 36.922  ? 76  ARG B NH2 1 ? 2 
ATOM   1762 N N   . ASP B 1 81  ? 45.205 13.859  55.788  1.000 35.626  ? 77  ASP B N   1 ? 2 
ATOM   1763 C CA  . ASP B 1 81  ? 46.612 14.356  55.858  1.000 36.232  ? 77  ASP B CA  1 ? 2 
ATOM   1764 C C   . ASP B 1 81  ? 47.377 13.845  54.624  1.000 35.492  ? 77  ASP B C   1 ? 2 
ATOM   1765 O O   . ASP B 1 81  ? 48.169 14.611  54.035  1.000 33.945  ? 77  ASP B O   1 ? 2 
ATOM   1766 C CB  . ASP B 1 81  ? 47.255 13.932  57.181  1.000 36.760  ? 77  ASP B CB  1 ? 2 
ATOM   1767 C CG  . ASP B 1 81  ? 47.019 14.892  58.326  1.000 37.992  ? 77  ASP B CG  1 ? 2 
ATOM   1768 O OD1 . ASP B 1 81  ? 46.200 15.788  58.154  1.000 42.155  ? 77  ASP B OD1 1 ? 2 
ATOM   1769 O OD2 . ASP B 1 81  ? 47.666 14.742  59.360  1.000 40.563  ? 77  ASP B OD2 1 ? 2 
ATOM   1770 N N   . ARG B 1 82  ? 47.102 12.599  54.248  1.000 34.269  ? 78  ARG B N   1 ? 2 
ATOM   1771 C CA  . ARG B 1 82  ? 47.640 11.922  53.063  1.000 36.556  ? 78  ARG B CA  1 ? 2 
ATOM   1772 C C   . ARG B 1 82  ? 47.028 12.545  51.781  1.000 34.178  ? 78  ARG B C   1 ? 2 
ATOM   1773 O O   . ARG B 1 82  ? 47.775 12.951  50.912  1.000 32.391  ? 78  ARG B O   1 ? 2 
ATOM   1774 C CB  . ARG B 1 82  ? 47.341 10.446  53.271  1.000 39.543  ? 78  ARG B CB  1 ? 2 
ATOM   1775 C CG  . ARG B 1 82  ? 48.010 9.561   52.239  1.000 45.866  ? 78  ARG B CG  1 ? 2 
ATOM   1776 C CD  . ARG B 1 82  ? 48.067 8.150   52.816  1.000 53.037  ? 78  ARG B CD  1 ? 2 
ATOM   1777 N NE  . ARG B 1 82  ? 48.125 7.128   51.774  1.000 56.350  ? 78  ARG B NE  1 ? 2 
ATOM   1778 C CZ  . ARG B 1 82  ? 47.134 6.855   50.927  1.000 58.129  ? 78  ARG B CZ  1 ? 2 
ATOM   1779 N NH1 . ARG B 1 82  ? 46.003 7.538   50.992  1.000 57.292  ? 78  ARG B NH1 1 ? 2 
ATOM   1780 N NH2 . ARG B 1 82  ? 47.287 5.914   50.006  1.000 58.273  ? 78  ARG B NH2 1 ? 2 
ATOM   1781 N N   . ALA B 1 83  ? 45.711 12.681  51.683  1.000 32.790  ? 79  ALA B N   1 ? 2 
ATOM   1782 C CA  . ALA B 1 83  ? 45.050 13.384  50.562  1.000 32.741  ? 79  ALA B CA  1 ? 2 
ATOM   1783 C C   . ALA B 1 83  ? 45.680 14.781  50.352  1.000 32.478  ? 79  ALA B C   1 ? 2 
ATOM   1784 O O   . ALA B 1 83  ? 45.971 15.134  49.198  1.000 32.906  ? 79  ALA B O   1 ? 2 
ATOM   1785 C CB  . ALA B 1 83  ? 43.574 13.431  50.808  1.000 31.868  ? 79  ALA B CB  1 ? 2 
ATOM   1786 N N   . ALA B 1 84  ? 45.960 15.543  51.406  1.000 32.038  ? 80  ALA B N   1 ? 2 
ATOM   1787 C CA  . ALA B 1 84  ? 46.612 16.881  51.320  1.000 31.531  ? 80  ALA B CA  1 ? 2 
ATOM   1788 C C   . ALA B 1 84  ? 48.022 16.779  50.718  1.000 31.480  ? 80  ALA B C   1 ? 2 
ATOM   1789 O O   . ALA B 1 84  ? 48.471 17.707  50.010  1.000 31.477  ? 80  ALA B O   1 ? 2 
ATOM   1790 C CB  . ALA B 1 84  ? 46.659 17.533  52.692  1.000 31.593  ? 80  ALA B CB  1 ? 2 
ATOM   1791 N N   . LEU B 1 85  ? 48.765 15.736  51.048  1.000 31.142  ? 81  LEU B N   1 ? 2 
ATOM   1792 C CA  . LEU B 1 85  ? 50.122 15.582  50.486  1.000 32.427  ? 81  LEU B CA  1 ? 2 
ATOM   1793 C C   . LEU B 1 85  ? 49.968 15.276  48.987  1.000 33.973  ? 81  LEU B C   1 ? 2 
ATOM   1794 O O   . LEU B 1 85  ? 50.638 15.896  48.146  1.000 33.742  ? 81  LEU B O   1 ? 2 
ATOM   1795 C CB  . LEU B 1 85  ? 50.844 14.447  51.212  1.000 32.968  ? 81  LEU B CB  1 ? 2 
ATOM   1796 C CG  . LEU B 1 85  ? 51.330 14.727  52.638  1.000 32.050  ? 81  LEU B CG  1 ? 2 
ATOM   1797 C CD1 . LEU B 1 85  ? 51.953 13.454  53.156  1.000 32.447  ? 81  LEU B CD1 1 ? 2 
ATOM   1798 C CD2 . LEU B 1 85  ? 52.325 15.885  52.705  1.000 31.525  ? 81  LEU B CD2 1 ? 2 
ATOM   1799 N N   . ARG B 1 86  ? 49.027 14.415  48.646  1.000 34.246  ? 82  ARG B N   1 ? 2 
ATOM   1800 C CA  . ARG B 1 86  ? 48.854 13.935  47.273  1.000 35.480  ? 82  ARG B CA  1 ? 2 
ATOM   1801 C C   . ARG B 1 86  ? 48.373 15.096  46.406  1.000 35.499  ? 82  ARG B C   1 ? 2 
ATOM   1802 O O   . ARG B 1 86  ? 48.875 15.214  45.297  1.000 39.251  ? 82  ARG B O   1 ? 2 
ATOM   1803 C CB  . ARG B 1 86  ? 47.872 12.769  47.263  1.000 36.511  ? 82  ARG B CB  1 ? 2 
ATOM   1804 C CG  . ARG B 1 86  ? 47.534 12.376  45.837  1.000 38.312  ? 82  ARG B CG  1 ? 2 
ATOM   1805 C CD  . ARG B 1 86  ? 46.172 11.741  45.749  1.000 39.911  ? 82  ARG B CD  1 ? 2 
ATOM   1806 N NE  . ARG B 1 86  ? 46.479 10.328  45.617  1.000 41.714  ? 82  ARG B NE  1 ? 2 
ATOM   1807 C CZ  . ARG B 1 86  ? 46.046 9.373   46.405  1.000 40.112  ? 82  ARG B CZ  1 ? 2 
ATOM   1808 N NH1 . ARG B 1 86  ? 45.253 9.670   47.420  1.000 41.169  ? 82  ARG B NH1 1 ? 2 
ATOM   1809 N NH2 . ARG B 1 86  ? 46.360 8.123   46.107  1.000 39.522  ? 82  ARG B NH2 1 ? 2 
ATOM   1810 N N   . LEU B 1 87  ? 47.421 15.905  46.888  1.000 34.372  ? 83  LEU B N   1 ? 2 
ATOM   1811 C CA  . LEU B 1 87  ? 46.659 16.907  46.092  1.000 31.479  ? 83  LEU B CA  1 ? 2 
ATOM   1812 C C   . LEU B 1 87  ? 47.139 18.335  46.351  1.000 31.742  ? 83  LEU B C   1 ? 2 
ATOM   1813 O O   . LEU B 1 87  ? 46.421 19.255  46.042  1.000 30.363  ? 83  LEU B O   1 ? 2 
ATOM   1814 C CB  . LEU B 1 87  ? 45.193 16.763  46.477  1.000 30.867  ? 83  LEU B CB  1 ? 2 
ATOM   1815 C CG  . LEU B 1 87  ? 44.574 15.390  46.221  1.000 30.894  ? 83  LEU B CG  1 ? 2 
ATOM   1816 C CD1 . LEU B 1 87  ? 43.123 15.412  46.652  1.000 30.737  ? 83  LEU B CD1 1 ? 2 
ATOM   1817 C CD2 . LEU B 1 87  ? 44.667 15.008  44.751  1.000 31.447  ? 83  LEU B CD2 1 ? 2 
ATOM   1818 N N   . GLN B 1 88  ? 48.316 18.501  46.932  1.000 34.313  ? 84  GLN B N   1 ? 2 
ATOM   1819 C CA  . GLN B 1 88  ? 49.003 19.804  47.108  1.000 35.975  ? 84  GLN B CA  1 ? 2 
ATOM   1820 C C   . GLN B 1 88  ? 49.008 20.557  45.767  1.000 34.910  ? 84  GLN B C   1 ? 2 
ATOM   1821 O O   . GLN B 1 88  ? 49.526 19.986  44.807  1.000 34.320  ? 84  GLN B O   1 ? 2 
ATOM   1822 C CB  . GLN B 1 88  ? 50.426 19.470  47.536  1.000 39.343  ? 84  GLN B CB  1 ? 2 
ATOM   1823 C CG  . GLN B 1 88  ? 51.059 20.465  48.477  1.000 43.477  ? 84  GLN B CG  1 ? 2 
ATOM   1824 C CD  . GLN B 1 88  ? 52.483 20.060  48.746  1.000 45.601  ? 84  GLN B CD  1 ? 2 
ATOM   1825 O OE1 . GLN B 1 88  ? 52.785 18.877  48.943  1.000 46.225  ? 84  GLN B OE1 1 ? 2 
ATOM   1826 N NE2 . GLN B 1 88  ? 53.363 21.051  48.696  1.000 48.567  ? 84  GLN B NE2 1 ? 2 
ATOM   1827 N N   . PHE B 1 89  ? 48.468 21.778  45.716  1.000 33.111  ? 85  PHE B N   1 ? 2 
ATOM   1828 C CA  . PHE B 1 89  ? 48.383 22.634  44.509  1.000 32.223  ? 85  PHE B CA  1 ? 2 
ATOM   1829 C C   . PHE B 1 89  ? 48.922 24.064  44.753  1.000 34.385  ? 85  PHE B C   1 ? 2 
ATOM   1830 O O   . PHE B 1 89  ? 48.660 24.683  45.836  1.000 35.397  ? 85  PHE B O   1 ? 2 
ATOM   1831 C CB  . PHE B 1 89  ? 46.935 22.617  44.013  1.000 31.689  ? 85  PHE B CB  1 ? 2 
ATOM   1832 C CG  . PHE B 1 89  ? 45.910 23.324  44.869  1.000 30.203  ? 85  PHE B CG  1 ? 2 
ATOM   1833 C CD1 . PHE B 1 89  ? 45.318 22.686  45.945  1.000 30.552  ? 85  PHE B CD1 1 ? 2 
ATOM   1834 C CD2 . PHE B 1 89  ? 45.536 24.624  44.590  1.000 29.448  ? 85  PHE B CD2 1 ? 2 
ATOM   1835 C CE1 . PHE B 1 89  ? 44.381 23.335  46.729  1.000 30.188  ? 85  PHE B CE1 1 ? 2 
ATOM   1836 C CE2 . PHE B 1 89  ? 44.611 25.275  45.389  1.000 29.928  ? 85  PHE B CE2 1 ? 2 
ATOM   1837 C CZ  . PHE B 1 89  ? 44.047 24.638  46.466  1.000 29.655  ? 85  PHE B CZ  1 ? 2 
ATOM   1838 N N   . SER B 1 90  ? 49.647 24.592  43.755  1.000 35.565  ? 86  SER B N   1 ? 2 
ATOM   1839 C CA  . SER B 1 90  ? 50.296 25.933  43.710  1.000 38.247  ? 86  SER B CA  1 ? 2 
ATOM   1840 C C   . SER B 1 90  ? 49.486 26.961  42.894  1.000 38.822  ? 86  SER B C   1 ? 2 
ATOM   1841 O O   . SER B 1 90  ? 49.796 28.139  43.018  1.000 39.312  ? 86  SER B O   1 ? 2 
ATOM   1842 C CB  . SER B 1 90  ? 51.677 25.815  43.092  1.000 39.789  ? 86  SER B CB  1 ? 2 
ATOM   1843 O OG  . SER B 1 90  ? 52.414 24.785  43.730  1.000 42.284  ? 86  SER B OG  1 ? 2 
ATOM   1844 N N   . HIS B 1 91  ? 48.569 26.537  42.012  1.000 38.547  ? 87  HIS B N   1 ? 2 
ATOM   1845 C CA  . HIS B 1 91  ? 47.909 27.414  41.006  1.000 39.067  ? 87  HIS B CA  1 ? 2 
ATOM   1846 C C   . HIS B 1 91  ? 46.408 27.133  40.950  1.000 35.000  ? 87  HIS B C   1 ? 2 
ATOM   1847 O O   . HIS B 1 91  ? 45.653 28.072  41.059  1.000 33.792  ? 87  HIS B O   1 ? 2 
ATOM   1848 C CB  . HIS B 1 91  ? 48.568 27.281  39.611  1.000 42.752  ? 87  HIS B CB  1 ? 2 
ATOM   1849 C CG  . HIS B 1 91  ? 50.043 27.568  39.616  1.000 47.287  ? 87  HIS B CG  1 ? 2 
ATOM   1850 N ND1 . HIS B 1 91  ? 50.564 28.885  39.674  1.000 49.085  ? 87  HIS B ND1 1 ? 2 
ATOM   1851 C CD2 . HIS B 1 91  ? 51.111 26.727  39.634  1.000 47.448  ? 87  HIS B CD2 1 ? 2 
ATOM   1852 C CE1 . HIS B 1 91  ? 51.883 28.823  39.704  1.000 48.565  ? 87  HIS B CE1 1 ? 2 
ATOM   1853 N NE2 . HIS B 1 91  ? 52.241 27.505  39.693  1.000 49.515  ? 87  HIS B NE2 1 ? 2 
ATOM   1854 N N   . SER B 1 92  ? 45.981 25.894  40.771  1.000 32.239  ? 88  SER B N   1 ? 2 
ATOM   1855 C CA  . SER B 1 92  ? 44.611 25.629  40.246  1.000 30.724  ? 88  SER B CA  1 ? 2 
ATOM   1856 C C   . SER B 1 92  ? 44.131 24.246  40.658  1.000 28.300  ? 88  SER B C   1 ? 2 
ATOM   1857 O O   . SER B 1 92  ? 44.982 23.370  40.854  1.000 29.135  ? 88  SER B O   1 ? 2 
ATOM   1858 C CB  . SER B 1 92  ? 44.589 25.811  38.753  1.000 29.958  ? 88  SER B CB  1 ? 2 
ATOM   1859 O OG  . SER B 1 92  ? 44.877 24.606  38.053  1.000 30.602  ? 88  SER B OG  1 ? 2 
ATOM   1860 N N   . PHE B 1 93  ? 42.833 24.036  40.793  1.000 26.004  ? 89  PHE B N   1 ? 2 
ATOM   1861 C CA  . PHE B 1 93  ? 42.284 22.657  40.852  1.000 25.027  ? 89  PHE B CA  1 ? 2 
ATOM   1862 C C   . PHE B 1 93  ? 40.991 22.640  40.064  1.000 24.185  ? 89  PHE B C   1 ? 2 
ATOM   1863 O O   . PHE B 1 93  ? 40.339 23.668  39.959  1.000 25.347  ? 89  PHE B O   1 ? 2 
ATOM   1864 C CB  . PHE B 1 93  ? 42.121 22.108  42.277  1.000 24.645  ? 89  PHE B CB  1 ? 2 
ATOM   1865 C CG  . PHE B 1 93  ? 41.019 22.654  43.138  1.000 24.811  ? 89  PHE B CG  1 ? 2 
ATOM   1866 C CD1 . PHE B 1 93  ? 41.295 23.205  44.376  1.000 25.554  ? 89  PHE B CD1 1 ? 2 
ATOM   1867 C CD2 . PHE B 1 93  ? 39.701 22.575  42.758  1.000 25.975  ? 89  PHE B CD2 1 ? 2 
ATOM   1868 C CE1 . PHE B 1 93  ? 40.289 23.710  45.198  1.000 26.443  ? 89  PHE B CE1 1 ? 2 
ATOM   1869 C CE2 . PHE B 1 93  ? 38.690 23.047  43.598  1.000 27.636  ? 89  PHE B CE2 1 ? 2 
ATOM   1870 C CZ  . PHE B 1 93  ? 38.974 23.622  44.830  1.000 25.933  ? 89  PHE B CZ  1 ? 2 
ATOM   1871 N N   . GLU B 1 94  ? 40.622 21.479  39.575  1.000 23.699  ? 90  GLU B N   1 ? 2 
ATOM   1872 C CA  . GLU B 1 94  ? 39.265 21.235  39.082  1.000 24.082  ? 90  GLU B CA  1 ? 2 
ATOM   1873 C C   . GLU B 1 94  ? 38.737 19.993  39.762  1.000 22.809  ? 90  GLU B C   1 ? 2 
ATOM   1874 O O   . GLU B 1 94  ? 39.420 18.987  39.787  1.000 23.658  ? 90  GLU B O   1 ? 2 
ATOM   1875 C CB  . GLU B 1 94  ? 39.239 21.081  37.552  1.000 26.284  ? 90  GLU B CB  1 ? 2 
ATOM   1876 C CG  . GLU B 1 94  ? 37.875 20.663  36.973  1.000 28.422  ? 90  GLU B CG  1 ? 2 
ATOM   1877 C CD  . GLU B 1 94  ? 37.834 20.389  35.460  1.000 30.892  ? 90  GLU B CD  1 ? 2 
ATOM   1878 O OE1 . GLU B 1 94  ? 37.071 19.517  35.019  1.000 33.093  ? 90  GLU B OE1 1 ? 2 
ATOM   1879 O OE2 . GLU B 1 94  ? 38.545 21.063  34.715  1.000 33.111  ? 90  GLU B OE2 1 ? 2 
ATOM   1880 N N   . VAL B 1 95  ? 37.508 20.053  40.204  1.000 22.542  ? 91  VAL B N   1 ? 2 
ATOM   1881 C CA  . VAL B 1 95  ? 36.723 18.879  40.645  1.000 22.821  ? 91  VAL B CA  1 ? 2 
ATOM   1882 C C   . VAL B 1 95  ? 35.609 18.676  39.647  1.000 22.999  ? 91  VAL B C   1 ? 2 
ATOM   1883 O O   . VAL B 1 95  ? 34.873 19.606  39.474  1.000 23.626  ? 91  VAL B O   1 ? 2 
ATOM   1884 C CB  . VAL B 1 95  ? 36.155 19.178  42.039  1.000 23.376  ? 91  VAL B CB  1 ? 2 
ATOM   1885 C CG1 . VAL B 1 95  ? 35.269 18.050  42.525  1.000 23.325  ? 91  VAL B CG1 1 ? 2 
ATOM   1886 C CG2 . VAL B 1 95  ? 37.297 19.503  43.017  1.000 23.488  ? 91  VAL B CG2 1 ? 2 
ATOM   1887 N N   . ASN B 1 96  ? 35.469 17.486  39.096  1.000 24.386  ? 92  ASN B N   1 ? 2 
ATOM   1888 C CA  . ASN B 1 96  ? 34.382 17.122  38.164  1.000 26.388  ? 92  ASN B CA  1 ? 2 
ATOM   1889 C C   . ASN B 1 96  ? 33.692 15.842  38.670  1.000 28.101  ? 92  ASN B C   1 ? 2 
ATOM   1890 O O   . ASN B 1 96  ? 34.366 14.805  38.617  1.000 30.335  ? 92  ASN B O   1 ? 2 
ATOM   1891 C CB  . ASN B 1 96  ? 35.038 17.006  36.795  1.000 26.805  ? 92  ASN B CB  1 ? 2 
ATOM   1892 C CG  . ASN B 1 96  ? 34.083 16.672  35.675  1.000 28.549  ? 92  ASN B CG  1 ? 2 
ATOM   1893 O OD1 . ASN B 1 96  ? 33.259 15.747  35.802  1.000 31.315  ? 92  ASN B OD1 1 ? 2 
ATOM   1894 N ND2 . ASN B 1 96  ? 34.254 17.379  34.556  1.000 27.224  ? 92  ASN B ND2 1 ? 2 
ATOM   1895 N N   . LEU B 1 97  ? 32.414 15.871  39.077  1.000 30.410  ? 93  LEU B N   1 ? 2 
ATOM   1896 C CA  . LEU B 1 97  ? 31.692 14.712  39.711  1.000 34.865  ? 93  LEU B CA  1 ? 2 
ATOM   1897 C C   . LEU B 1 97  ? 30.492 14.209  38.893  1.000 35.774  ? 93  LEU B C   1 ? 2 
ATOM   1898 O O   . LEU B 1 97  ? 30.030 14.987  38.129  1.000 33.977  ? 93  LEU B O   1 ? 2 
ATOM   1899 C CB  . LEU B 1 97  ? 31.157 15.176  41.078  1.000 34.627  ? 93  LEU B CB  1 ? 2 
ATOM   1900 C CG  . LEU B 1 97  ? 32.209 15.852  41.931  1.000 37.136  ? 93  LEU B CG  1 ? 2 
ATOM   1901 C CD1 . LEU B 1 97  ? 31.633 16.455  43.202  1.000 38.760  ? 93  LEU B CD1 1 ? 2 
ATOM   1902 C CD2 . LEU B 1 97  ? 33.274 14.842  42.278  1.000 37.538  ? 93  LEU B CD2 1 ? 2 
ATOM   1903 N N   . ASP B 1 98  ? 29.850 13.123  39.360  1.000 44.000  ? 94  ASP B N   1 ? 2 
ATOM   1904 C CA  . ASP B 1 98  ? 28.605 12.447  38.877  1.000 50.546  ? 94  ASP B CA  1 ? 2 
ATOM   1905 C C   . ASP B 1 98  ? 28.952 12.254  37.439  1.000 56.046  ? 94  ASP B C   1 ? 2 
ATOM   1906 O O   . ASP B 1 98  ? 28.093 12.463  36.604  1.000 67.456  ? 94  ASP B O   1 ? 2 
ATOM   1907 C CB  . ASP B 1 98  ? 27.273 13.204  38.998  1.000 53.279  ? 94  ASP B CB  1 ? 2 
ATOM   1908 C CG  . ASP B 1 98  ? 26.890 13.659  40.407  1.000 60.416  ? 94  ASP B CG  1 ? 2 
ATOM   1909 O OD1 . ASP B 1 98  ? 27.536 13.144  41.398  1.000 59.784  ? 94  ASP B OD1 1 ? 2 
ATOM   1910 O OD2 . ASP B 1 98  ? 25.952 14.553  40.518  1.000 56.892  ? 94  ASP B OD2 1 ? 2 
ATOM   1911 N N   . ASN B 1 99  ? 30.253 12.064  37.253  1.000 61.884  ? 95  ASN B N   1 ? 2 
ATOM   1912 C CA  . ASN B 1 99  ? 31.058 12.381  36.036  1.000 66.190  ? 95  ASN B CA  1 ? 2 
ATOM   1913 C C   . ASN B 1 99  ? 30.298 13.346  35.049  1.000 65.278  ? 95  ASN B C   1 ? 2 
ATOM   1914 O O   . ASN B 1 99  ? 29.396 12.925  34.302  1.000 61.009  ? 95  ASN B O   1 ? 2 
ATOM   1915 C CB  . ASN B 1 99  ? 31.605 11.044  35.526  1.000 71.169  ? 95  ASN B CB  1 ? 2 
ATOM   1916 C CG  . ASN B 1 99  ? 32.213 10.134  36.589  1.000 74.962  ? 95  ASN B CG  1 ? 2 
ATOM   1917 O OD1 . ASN B 1 99  ? 33.409 9.821   36.506  1.000 77.415  ? 95  ASN B OD1 1 ? 2 
ATOM   1918 N ND2 . ASN B 1 99  ? 31.404 9.663   37.545  1.000 63.648  ? 95  ASN B ND2 1 ? 2 
ATOM   1919 N N   . GLY B 1 100 ? 30.653 14.643  35.011  1.000 64.878  ? 96  GLY B N   1 ? 2 
ATOM   1920 C CA  . GLY B 1 100 ? 30.122 15.629  34.039  1.000 65.141  ? 96  GLY B CA  1 ? 2 
ATOM   1921 C C   . GLY B 1 100 ? 29.211 16.701  34.651  1.000 67.040  ? 96  GLY B C   1 ? 2 
ATOM   1922 O O   . GLY B 1 100 ? 29.353 17.909  34.294  1.000 65.160  ? 96  GLY B O   1 ? 2 
ATOM   1923 N N   . ARG B 1 101 ? 28.309 16.279  35.545  1.000 64.450  ? 97  ARG B N   1 ? 2 
ATOM   1924 C CA  . ARG B 1 101 ? 27.095 17.007  35.983  1.000 58.469  ? 97  ARG B CA  1 ? 2 
ATOM   1925 C C   . ARG B 1 101 ? 27.325 17.789  37.286  1.000 52.105  ? 97  ARG B C   1 ? 2 
ATOM   1926 O O   . ARG B 1 101 ? 26.328 18.086  37.926  1.000 58.416  ? 97  ARG B O   1 ? 2 
ATOM   1927 C CB  . ARG B 1 101 ? 25.985 15.965  36.153  1.000 65.210  ? 97  ARG B CB  1 ? 2 
ATOM   1928 C CG  . ARG B 1 101 ? 25.640 15.190  34.883  1.000 72.407  ? 97  ARG B CG  1 ? 2 
ATOM   1929 C CD  . ARG B 1 101 ? 24.703 14.009  35.159  1.000 81.891  ? 97  ARG B CD  1 ? 2 
ATOM   1930 N NE  . ARG B 1 101 ? 25.379 12.718  35.393  1.000 86.288  ? 97  ARG B NE  1 ? 2 
ATOM   1931 C CZ  . ARG B 1 101 ? 24.827 11.491  35.276  1.000 89.303  ? 97  ARG B CZ  1 ? 2 
ATOM   1932 N NH1 . ARG B 1 101 ? 23.560 11.339  34.919  1.000 89.532  ? 97  ARG B NH1 1 ? 2 
ATOM   1933 N NH2 . ARG B 1 101 ? 25.557 10.403  35.496  1.000 89.041  ? 97  ARG B NH2 1 ? 2 
ATOM   1934 N N   . LYS B 1 102 ? 28.572 18.004  37.725  1.000 46.404  ? 98  LYS B N   1 ? 2 
ATOM   1935 C CA  . LYS B 1 102 ? 28.991 18.976  38.784  1.000 39.340  ? 98  LYS B CA  1 ? 2 
ATOM   1936 C C   . LYS B 1 102 ? 30.476 19.295  38.648  1.000 33.011  ? 98  LYS B C   1 ? 2 
ATOM   1937 O O   . LYS B 1 102 ? 31.269 18.375  38.696  1.000 31.092  ? 98  LYS B O   1 ? 2 
ATOM   1938 C CB  . LYS B 1 102 ? 28.773 18.435  40.188  1.000 42.562  ? 98  LYS B CB  1 ? 2 
ATOM   1939 C CG  . LYS B 1 102 ? 27.767 19.230  40.991  1.000 48.211  ? 98  LYS B CG  1 ? 2 
ATOM   1940 C CD  . LYS B 1 102 ? 27.697 18.908  42.464  1.000 49.545  ? 98  LYS B CD  1 ? 2 
ATOM   1941 C CE  . LYS B 1 102 ? 27.167 17.532  42.742  1.000 51.819  ? 98  LYS B CE  1 ? 2 
ATOM   1942 N NZ  . LYS B 1 102 ? 26.824 17.471  44.178  1.000 53.931  ? 98  LYS B NZ  1 ? 2 
ATOM   1943 N N   . ILE B 1 103 ? 30.828 20.553  38.460  1.000 28.861  ? 99  ILE B N   1 ? 2 
ATOM   1944 C CA  . ILE B 1 103 ? 32.221 20.965  38.171  1.000 27.903  ? 99  ILE B CA  1 ? 2 
ATOM   1945 C C   . ILE B 1 103 ? 32.535 22.216  38.978  1.000 26.305  ? 99  ILE B C   1 ? 2 
ATOM   1946 O O   . ILE B 1 103 ? 31.749 23.132  38.880  1.000 25.691  ? 99  ILE B O   1 ? 2 
ATOM   1947 C CB  . ILE B 1 103 ? 32.430 21.271  36.669  1.000 27.565  ? 99  ILE B CB  1 ? 2 
ATOM   1948 C CG1 . ILE B 1 103 ? 32.155 20.074  35.752  1.000 28.439  ? 99  ILE B CG1 1 ? 2 
ATOM   1949 C CG2 . ILE B 1 103 ? 33.833 21.801  36.451  1.000 27.143  ? 99  ILE B CG2 1 ? 2 
ATOM   1950 C CD1 . ILE B 1 103 ? 31.912 20.435  34.281  1.000 28.661  ? 99  ILE B CD1 1 ? 2 
ATOM   1951 N N   . MET B 1 104 ? 33.706 22.264  39.600  1.000 25.844  ? 100 MET B N   1 ? 2 
ATOM   1952 C CA  . MET B 1 104 ? 34.287 23.447  40.307  1.000 27.210  ? 100 MET B CA  1 ? 2 
ATOM   1953 C C   . MET B 1 104 ? 35.731 23.634  39.842  1.000 25.978  ? 100 MET B C   1 ? 2 
ATOM   1954 O O   . MET B 1 104 ? 36.435 22.634  39.794  1.000 24.338  ? 100 MET B O   1 ? 2 
ATOM   1955 C CB  . MET B 1 104 ? 34.276 23.219  41.829  1.000 28.501  ? 100 MET B CB  1 ? 2 
ATOM   1956 C CG  . MET B 1 104 ? 34.954 24.289  42.702  1.000 30.295  ? 100 MET B CG  1 ? 2 
ATOM   1957 S SD  . MET B 1 104 ? 34.857 23.844  44.516  1.000 32.121  ? 100 MET B SD  1 ? 2 
ATOM   1958 C CE  . MET B 1 104 ? 33.078 23.864  44.733  1.000 32.632  ? 100 MET B CE  1 ? 2 
ATOM   1959 N N   . ARG B 1 105 ? 36.098 24.858  39.487  1.000 25.613  ? 101 ARG B N   1 ? 2 
ATOM   1960 C CA  . ARG B 1 105 ? 37.479 25.238  39.174  1.000 28.407  ? 101 ARG B CA  1 ? 2 
ATOM   1961 C C   . ARG B 1 105 ? 37.868 26.341  40.140  1.000 28.865  ? 101 ARG B C   1 ? 2 
ATOM   1962 O O   . ARG B 1 105 ? 37.036 27.217  40.325  1.000 28.092  ? 101 ARG B O   1 ? 2 
ATOM   1963 C CB  . ARG B 1 105 ? 37.565 25.825  37.768  1.000 31.306  ? 101 ARG B CB  1 ? 2 
ATOM   1964 C CG  . ARG B 1 105 ? 37.162 24.876  36.654  1.000 34.571  ? 101 ARG B CG  1 ? 2 
ATOM   1965 C CD  . ARG B 1 105 ? 37.432 25.467  35.269  1.000 37.681  ? 101 ARG B CD  1 ? 2 
ATOM   1966 N NE  . ARG B 1 105 ? 37.193 24.598  34.097  1.000 39.871  ? 101 ARG B NE  1 ? 2 
ATOM   1967 C CZ  . ARG B 1 105 ? 36.001 24.253  33.609  1.000 38.836  ? 101 ARG B CZ  1 ? 2 
ATOM   1968 N NH1 . ARG B 1 105 ? 34.910 24.631  34.221  1.000 39.703  ? 101 ARG B NH1 1 ? 2 
ATOM   1969 N NH2 . ARG B 1 105 ? 35.885 23.530  32.508  1.000 41.959  ? 101 ARG B NH2 1 ? 2 
ATOM   1970 N N   . LEU B 1 106 ? 39.084 26.293  40.673  1.000 30.717  ? 102 LEU B N   1 ? 2 
ATOM   1971 C CA  . LEU B 1 106 ? 39.679 27.338  41.551  1.000 32.924  ? 102 LEU B CA  1 ? 2 
ATOM   1972 C C   . LEU B 1 106 ? 41.050 27.734  41.014  1.000 32.935  ? 102 LEU B C   1 ? 2 
ATOM   1973 O O   . LEU B 1 106 ? 41.836 26.821  40.776  1.000 34.974  ? 102 LEU B O   1 ? 2 
ATOM   1974 C CB  . LEU B 1 106 ? 39.832 26.798  42.975  1.000 32.519  ? 102 LEU B CB  1 ? 2 
ATOM   1975 C CG  . LEU B 1 106 ? 40.480 27.782  43.935  1.000 33.710  ? 102 LEU B CG  1 ? 2 
ATOM   1976 C CD1 . LEU B 1 106 ? 39.421 28.519  44.690  1.000 35.788  ? 102 LEU B CD1 1 ? 2 
ATOM   1977 C CD2 . LEU B 1 106 ? 41.368 27.084  44.920  1.000 34.412  ? 102 LEU B CD2 1 ? 2 
ATOM   1978 N N   . GLN B 1 107 ? 41.306 29.021  40.832  1.000 34.205  ? 103 GLN B N   1 ? 2 
ATOM   1979 C CA  . GLN B 1 107 ? 42.661 29.567  40.572  1.000 37.319  ? 103 GLN B CA  1 ? 2 
ATOM   1980 C C   . GLN B 1 107 ? 43.035 30.471  41.746  1.000 37.326  ? 103 GLN B C   1 ? 2 
ATOM   1981 O O   . GLN B 1 107 ? 42.211 31.310  42.171  1.000 36.262  ? 103 GLN B O   1 ? 2 
ATOM   1982 C CB  . GLN B 1 107 ? 42.753 30.354  39.266  1.000 40.944  ? 103 GLN B CB  1 ? 2 
ATOM   1983 C CG  . GLN B 1 107 ? 42.146 29.662  38.050  1.000 46.597  ? 103 GLN B CG  1 ? 2 
ATOM   1984 C CD  . GLN B 1 107 ? 40.628 29.524  38.039  1.000 52.581  ? 103 GLN B CD  1 ? 2 
ATOM   1985 O OE1 . GLN B 1 107 ? 39.861 30.480  38.237  1.000 58.934  ? 103 GLN B OE1 1 ? 2 
ATOM   1986 N NE2 . GLN B 1 107 ? 40.160 28.313  37.766  1.000 53.714  ? 103 GLN B NE2 1 ? 2 
ATOM   1987 N N   . LEU B 1 108 ? 44.232 30.265  42.282  1.000 39.557  ? 104 LEU B N   1 ? 2 
ATOM   1988 C CA  . LEU B 1 108 ? 44.817 31.094  43.359  1.000 40.243  ? 104 LEU B CA  1 ? 2 
ATOM   1989 C C   . LEU B 1 108 ? 45.293 32.413  42.780  1.000 43.096  ? 104 LEU B C   1 ? 2 
ATOM   1990 O O   . LEU B 1 108 ? 45.811 32.393  41.628  1.000 43.261  ? 104 LEU B O   1 ? 2 
ATOM   1991 C CB  . LEU B 1 108 ? 46.010 30.356  43.942  1.000 38.544  ? 104 LEU B CB  1 ? 2 
ATOM   1992 C CG  . LEU B 1 108 ? 45.678 29.105  44.726  1.000 38.272  ? 104 LEU B CG  1 ? 2 
ATOM   1993 C CD1 . LEU B 1 108 ? 46.963 28.498  45.252  1.000 39.004  ? 104 LEU B CD1 1 ? 2 
ATOM   1994 C CD2 . LEU B 1 108 ? 44.691 29.390  45.843  1.000 37.266  ? 104 LEU B CD2 1 ? 2 
ATOM   1995 N N   . GLY B 1 109 ? 45.162 33.468  43.585  1.000 46.278  ? 105 GLY B N   1 ? 2 
ATOM   1996 C CA  . GLY B 1 109 ? 45.860 34.752  43.405  1.000 50.020  ? 105 GLY B CA  1 ? 2 
ATOM   1997 C C   . GLY B 1 109 ? 46.486 35.291  44.687  1.000 54.176  ? 105 GLY B C   1 ? 2 
ATOM   1998 O O   . GLY B 1 109 ? 46.347 34.667  45.780  1.000 50.664  ? 105 GLY B O   1 ? 2 
ATOM   1999 N N   . GLN B 1 110 ? 47.141 36.452  44.554  1.000 63.939  ? 106 GLN B N   1 ? 2 
ATOM   2000 C CA  . GLN B 1 110 ? 47.837 37.181  45.652  1.000 67.830  ? 106 GLN B CA  1 ? 2 
ATOM   2001 C C   . GLN B 1 110 ? 46.825 37.445  46.776  1.000 67.333  ? 106 GLN B C   1 ? 2 
ATOM   2002 O O   . GLN B 1 110 ? 47.011 36.930  47.914  1.000 64.354  ? 106 GLN B O   1 ? 2 
ATOM   2003 C CB  . GLN B 1 110 ? 48.469 38.456  45.068  1.000 71.765  ? 106 GLN B CB  1 ? 2 
ATOM   2004 C CG  . GLN B 1 110 ? 49.266 39.310  46.054  1.000 75.550  ? 106 GLN B CG  1 ? 2 
ATOM   2005 C CD  . GLN B 1 110 ? 50.615 38.755  46.456  1.000 76.506  ? 106 GLN B CD  1 ? 2 
ATOM   2006 O OE1 . GLN B 1 110 ? 51.123 37.756  45.942  1.000 77.323  ? 106 GLN B OE1 1 ? 2 
ATOM   2007 N NE2 . GLN B 1 110 ? 51.217 39.423  47.415  1.000 74.284  ? 106 GLN B NE2 1 ? 2 
ATOM   2008 N N   . GLU B 1 111 ? 45.765 38.195  46.460  1.000 68.383  ? 107 GLU B N   1 ? 2 
ATOM   2009 C CA  . GLU B 1 111 ? 44.832 38.771  47.472  1.000 72.104  ? 107 GLU B CA  1 ? 2 
ATOM   2010 C C   . GLU B 1 111 ? 43.509 37.981  47.507  1.000 68.516  ? 107 GLU B C   1 ? 2 
ATOM   2011 O O   . GLU B 1 111 ? 42.863 37.964  48.559  1.000 72.780  ? 107 GLU B O   1 ? 2 
ATOM   2012 C CB  . GLU B 1 111 ? 44.660 40.274  47.205  1.000 77.565  ? 107 GLU B CB  1 ? 2 
ATOM   2013 C CG  . GLU B 1 111 ? 45.673 41.130  47.953  1.000 81.825  ? 107 GLU B CG  1 ? 2 
ATOM   2014 C CD  . GLU B 1 111 ? 45.372 41.173  49.445  1.000 90.513  ? 107 GLU B CD  1 ? 2 
ATOM   2015 O OE1 . GLU B 1 111 ? 44.314 41.725  49.787  1.000 90.603  ? 107 GLU B OE1 1 ? 2 
ATOM   2016 O OE2 . GLU B 1 111 ? 46.159 40.610  50.261  1.000 96.673  ? 107 GLU B OE2 1 ? 2 
ATOM   2017 N N   . THR B 1 112 ? 43.112 37.337  46.406  1.000 64.891  ? 108 THR B N   1 ? 2 
ATOM   2018 C CA  . THR B 1 112 ? 41.849 36.566  46.275  1.000 56.569  ? 108 THR B CA  1 ? 2 
ATOM   2019 C C   . THR B 1 112 ? 42.106 35.303  45.447  1.000 54.065  ? 108 THR B C   1 ? 2 
ATOM   2020 O O   . THR B 1 112 ? 43.078 35.292  44.677  1.000 55.197  ? 108 THR B O   1 ? 2 
ATOM   2021 C CB  . THR B 1 112 ? 40.759 37.409  45.600  1.000 54.318  ? 108 THR B CB  1 ? 2 
ATOM   2022 O OG1 . THR B 1 112 ? 41.219 37.730  44.284  1.000 52.685  ? 108 THR B OG1 1 ? 2 
ATOM   2023 C CG2 . THR B 1 112 ? 40.396 38.671  46.350  1.000 51.831  ? 108 THR B CG2 1 ? 2 
ATOM   2024 N N   . SER B 1 113 ? 41.237 34.297  45.569  1.000 49.536  ? 109 SER B N   1 ? 2 
ATOM   2025 C CA  . SER B 1 113 ? 41.080 33.185  44.589  1.000 45.174  ? 109 SER B CA  1 ? 2 
ATOM   2026 C C   . SER B 1 113 ? 39.896 33.468  43.643  1.000 42.595  ? 109 SER B C   1 ? 2 
ATOM   2027 O O   . SER B 1 113 ? 38.928 34.091  44.062  1.000 42.390  ? 109 SER B O   1 ? 2 
ATOM   2028 C CB  . SER B 1 113 ? 40.910 31.897  45.330  1.000 42.796  ? 109 SER B CB  1 ? 2 
ATOM   2029 O OG  . SER B 1 113 ? 42.020 31.741  46.187  1.000 41.007  ? 109 SER B OG  1 ? 2 
ATOM   2030 N N   . THR B 1 114 ? 39.951 33.042  42.393  1.000 40.267  ? 110 THR B N   1 ? 2 
ATOM   2031 C CA  . THR B 1 114 ? 38.753 33.063  41.518  1.000 40.338  ? 110 THR B CA  1 ? 2 
ATOM   2032 C C   . THR B 1 114 ? 38.191 31.647  41.484  1.000 37.055  ? 110 THR B C   1 ? 2 
ATOM   2033 O O   . THR B 1 114 ? 38.958 30.720  41.677  1.000 36.238  ? 110 THR B O   1 ? 2 
ATOM   2034 C CB  . THR B 1 114 ? 39.088 33.675  40.156  1.000 42.072  ? 110 THR B CB  1 ? 2 
ATOM   2035 O OG1 . THR B 1 114 ? 40.252 32.998  39.677  1.000 44.278  ? 110 THR B OG1 1 ? 2 
ATOM   2036 C CG2 . THR B 1 114 ? 39.357 35.159  40.243  1.000 41.385  ? 110 THR B CG2 1 ? 2 
ATOM   2037 N N   . LEU B 1 115 ? 36.892 31.524  41.263  1.000 36.744  ? 111 LEU B N   1 ? 2 
ATOM   2038 C CA  . LEU B 1 115 ? 36.096 30.278  41.437  1.000 36.465  ? 111 LEU B CA  1 ? 2 
ATOM   2039 C C   . LEU B 1 115 ? 34.986 30.216  40.381  1.000 35.788  ? 111 LEU B C   1 ? 2 
ATOM   2040 O O   . LEU B 1 115 ? 34.304 31.194  40.203  1.000 34.054  ? 111 LEU B O   1 ? 2 
ATOM   2041 C CB  . LEU B 1 115 ? 35.526 30.348  42.847  1.000 38.086  ? 111 LEU B CB  1 ? 2 
ATOM   2042 C CG  . LEU B 1 115 ? 35.000 29.056  43.450  1.000 38.408  ? 111 LEU B CG  1 ? 2 
ATOM   2043 C CD1 . LEU B 1 115 ? 36.087 28.033  43.483  1.000 40.337  ? 111 LEU B CD1 1 ? 2 
ATOM   2044 C CD2 . LEU B 1 115 ? 34.493 29.291  44.860  1.000 38.865  ? 111 LEU B CD2 1 ? 2 
ATOM   2045 N N   . GLN B 1 116 ? 34.889 29.138  39.609  1.000 37.825  ? 112 GLN B N   1 ? 2 
ATOM   2046 C CA  . GLN B 1 116 ? 33.825 28.928  38.577  1.000 37.678  ? 112 GLN B CA  1 ? 2 
ATOM   2047 C C   . GLN B 1 116 ? 33.078 27.643  38.954  1.000 34.819  ? 112 GLN B C   1 ? 2 
ATOM   2048 O O   . GLN B 1 116 ? 33.746 26.652  39.153  1.000 37.730  ? 112 GLN B O   1 ? 2 
ATOM   2049 C CB  . GLN B 1 116 ? 34.421 28.799  37.163  1.000 42.022  ? 112 GLN B CB  1 ? 2 
ATOM   2050 C CG  . GLN B 1 116 ? 35.247 29.996  36.677  1.000 46.179  ? 112 GLN B CG  1 ? 2 
ATOM   2051 C CD  . GLN B 1 116 ? 36.634 30.109  37.295  1.000 50.266  ? 112 GLN B CD  1 ? 2 
ATOM   2052 O OE1 . GLN B 1 116 ? 37.457 29.199  37.202  1.000 52.725  ? 112 GLN B OE1 1 ? 2 
ATOM   2053 N NE2 . GLN B 1 116 ? 36.920 31.228  37.953  1.000 50.526  ? 112 GLN B NE2 1 ? 2 
ATOM   2054 N N   . LEU B 1 117 ? 31.769 27.630  39.113  1.000 32.426  ? 113 LEU B N   1 ? 2 
ATOM   2055 C CA  . LEU B 1 117 ? 31.047 26.352  39.296  1.000 32.694  ? 113 LEU B CA  1 ? 2 
ATOM   2056 C C   . LEU B 1 117 ? 30.067 26.137  38.172  1.000 32.922  ? 113 LEU B C   1 ? 2 
ATOM   2057 O O   . LEU B 1 117 ? 29.507 27.148  37.713  1.000 31.633  ? 113 LEU B O   1 ? 2 
ATOM   2058 C CB  . LEU B 1 117 ? 30.201 26.397  40.553  1.000 35.691  ? 113 LEU B CB  1 ? 2 
ATOM   2059 C CG  . LEU B 1 117 ? 30.850 27.049  41.748  1.000 37.805  ? 113 LEU B CG  1 ? 2 
ATOM   2060 C CD1 . LEU B 1 117 ? 29.878 27.049  42.920  1.000 39.514  ? 113 LEU B CD1 1 ? 2 
ATOM   2061 C CD2 . LEU B 1 117 ? 32.111 26.304  42.069  1.000 39.000  ? 113 LEU B CD2 1 ? 2 
ATOM   2062 N N   . GLU B 1 118 ? 29.789 24.868  37.892  1.000 35.022  ? 114 GLU B N   1 ? 2 
ATOM   2063 C CA  . GLU B 1 118 ? 28.671 24.389  37.025  1.000 40.546  ? 114 GLU B CA  1 ? 2 
ATOM   2064 C C   . GLU B 1 118 ? 28.009 23.172  37.659  1.000 39.384  ? 114 GLU B C   1 ? 2 
ATOM   2065 O O   . GLU B 1 118 ? 28.719 22.344  38.232  1.000 39.143  ? 114 GLU B O   1 ? 2 
ATOM   2066 C CB  . GLU B 1 118 ? 29.090 23.876  35.644  1.000 45.642  ? 114 GLU B CB  1 ? 2 
ATOM   2067 C CG  . GLU B 1 118 ? 29.584 24.939  34.694  1.000 50.638  ? 114 GLU B CG  1 ? 2 
ATOM   2068 C CD  . GLU B 1 118 ? 30.227 24.377  33.439  1.000 55.054  ? 114 GLU B CD  1 ? 2 
ATOM   2069 O OE1 . GLU B 1 118 ? 31.262 24.962  33.001  1.000 56.163  ? 114 GLU B OE1 1 ? 2 
ATOM   2070 O OE2 . GLU B 1 118 ? 29.678 23.371  32.902  1.000 57.607  ? 114 GLU B OE2 1 ? 2 
ATOM   2071 N N   . GLN B 1 119 ? 26.706 23.066  37.475  1.000 40.427  ? 115 GLN B N   1 ? 2 
ATOM   2072 C CA  . GLN B 1 119 ? 25.878 21.934  37.932  1.000 45.878  ? 115 GLN B CA  1 ? 2 
ATOM   2073 C C   . GLN B 1 119 ? 24.815 21.752  36.847  1.000 47.196  ? 115 GLN B C   1 ? 2 
ATOM   2074 O O   . GLN B 1 119 ? 24.342 22.760  36.316  1.000 45.916  ? 115 GLN B O   1 ? 2 
ATOM   2075 C CB  . GLN B 1 119 ? 25.345 22.300  39.318  1.000 52.161  ? 115 GLN B CB  1 ? 2 
ATOM   2076 C CG  . GLN B 1 119 ? 24.862 21.163  40.216  1.000 54.929  ? 115 GLN B CG  1 ? 2 
ATOM   2077 C CD  . GLN B 1 119 ? 25.249 21.384  41.672  1.000 56.483  ? 115 GLN B CD  1 ? 2 
ATOM   2078 O OE1 . GLN B 1 119 ? 26.136 22.174  42.024  1.000 54.014  ? 115 GLN B OE1 1 ? 2 
ATOM   2079 N NE2 . GLN B 1 119 ? 24.572 20.671  42.559  1.000 61.515  ? 115 GLN B NE2 1 ? 2 
ATOM   2080 N N   . LYS B 1 120 ? 24.549 20.523  36.446  1.000 47.919  ? 116 LYS B N   1 ? 2 
ATOM   2081 C CA  . LYS B 1 120 ? 23.471 20.189  35.500  1.000 49.330  ? 116 LYS B CA  1 ? 2 
ATOM   2082 C C   . LYS B 1 120 ? 22.854 18.905  36.008  1.000 48.944  ? 116 LYS B C   1 ? 2 
ATOM   2083 O O   . LYS B 1 120 ? 23.128 17.901  35.434  1.000 54.116  ? 116 LYS B O   1 ? 2 
ATOM   2084 C CB  . LYS B 1 120 ? 24.040 20.021  34.095  1.000 51.870  ? 116 LYS B CB  1 ? 2 
ATOM   2085 C CG  . LYS B 1 120 ? 24.617 21.279  33.485  1.000 57.626  ? 116 LYS B CG  1 ? 2 
ATOM   2086 C CD  . LYS B 1 120 ? 25.706 20.987  32.459  1.000 63.162  ? 116 LYS B CD  1 ? 2 
ATOM   2087 C CE  . LYS B 1 120 ? 27.113 21.357  32.923  1.000 70.085  ? 116 LYS B CE  1 ? 2 
ATOM   2088 N NZ  . LYS B 1 120 ? 27.793 20.282  33.704  1.000 70.931  ? 116 LYS B NZ  1 ? 2 
ATOM   2089 N N   . GLY B 1 121 ? 22.155 18.941  37.127  1.000 54.468  ? 117 GLY B N   1 ? 2 
ATOM   2090 C CA  . GLY B 1 121 ? 21.392 17.797  37.665  1.000 58.965  ? 117 GLY B CA  1 ? 2 
ATOM   2091 C C   . GLY B 1 121 ? 19.944 17.902  37.229  1.000 63.883  ? 117 GLY B C   1 ? 2 
ATOM   2092 O O   . GLY B 1 121 ? 19.609 18.866  36.506  1.000 67.079  ? 117 GLY B O   1 ? 2 
ATOM   2093 N N   . ARG B 1 122 ? 19.100 16.949  37.609  1.000 71.836  ? 118 ARG B N   1 ? 2 
ATOM   2094 C CA  . ARG B 1 122 ? 17.662 17.013  37.251  1.000 78.103  ? 118 ARG B CA  1 ? 2 
ATOM   2095 C C   . ARG B 1 122 ? 17.041 18.053  38.189  1.000 75.664  ? 118 ARG B C   1 ? 2 
ATOM   2096 O O   . ARG B 1 122 ? 16.095 18.741  37.747  1.000 82.683  ? 118 ARG B O   1 ? 2 
ATOM   2097 C CB  . ARG B 1 122 ? 17.012 15.627  37.288  1.000 86.179  ? 118 ARG B CB  1 ? 2 
ATOM   2098 C CG  . ARG B 1 122 ? 15.836 15.441  36.326  1.000 100.064 ? 118 ARG B CG  1 ? 2 
ATOM   2099 C CD  . ARG B 1 122 ? 14.883 14.304  36.715  1.000 107.425 ? 118 ARG B CD  1 ? 2 
ATOM   2100 N NE  . ARG B 1 122 ? 15.157 13.837  38.081  1.000 116.449 ? 118 ARG B NE  1 ? 2 
ATOM   2101 C CZ  . ARG B 1 122 ? 14.264 13.510  39.019  1.000 117.588 ? 118 ARG B CZ  1 ? 2 
ATOM   2102 N NH1 . ARG B 1 122 ? 12.967 13.585  38.772  1.000 121.966 ? 118 ARG B NH1 1 ? 2 
ATOM   2103 N NH2 . ARG B 1 122 ? 14.692 13.127  40.215  1.000 113.002 ? 118 ARG B NH2 1 ? 2 
ATOM   2104 N N   . VAL B 1 123 ? 17.619 18.233  39.386  1.000 66.610  ? 119 VAL B N   1 ? 2 
ATOM   2105 C CA  . VAL B 1 123 ? 17.007 19.013  40.505  1.000 64.737  ? 119 VAL B CA  1 ? 2 
ATOM   2106 C C   . VAL B 1 123 ? 17.493 20.493  40.481  1.000 59.186  ? 119 VAL B C   1 ? 2 
ATOM   2107 O O   . VAL B 1 123 ? 16.696 21.382  40.899  1.000 59.271  ? 119 VAL B O   1 ? 2 
ATOM   2108 C CB  . VAL B 1 123 ? 17.170 18.222  41.838  1.000 68.820  ? 119 VAL B CB  1 ? 2 
ATOM   2109 C CG1 . VAL B 1 123 ? 17.603 19.053  43.046  1.000 69.547  ? 119 VAL B CG1 1 ? 2 
ATOM   2110 C CG2 . VAL B 1 123 ? 15.900 17.423  42.179  1.000 64.687  ? 119 VAL B CG2 1 ? 2 
ATOM   2111 N N   . LEU B 1 124 ? 18.657 20.798  39.890  1.000 53.080  ? 120 LEU B N   1 ? 2 
ATOM   2112 C CA  . LEU B 1 124 ? 19.276 22.157  39.863  1.000 48.318  ? 120 LEU B CA  1 ? 2 
ATOM   2113 C C   . LEU B 1 124 ? 20.203 22.298  38.670  1.000 46.770  ? 120 LEU B C   1 ? 2 
ATOM   2114 O O   . LEU B 1 124 ? 21.143 21.507  38.609  1.000 47.406  ? 120 LEU B O   1 ? 2 
ATOM   2115 C CB  . LEU B 1 124 ? 20.127 22.360  41.120  1.000 47.681  ? 120 LEU B CB  1 ? 2 
ATOM   2116 C CG  . LEU B 1 124 ? 21.062 23.570  41.101  1.000 46.795  ? 120 LEU B CG  1 ? 2 
ATOM   2117 C CD1 . LEU B 1 124 ? 20.324 24.838  40.699  1.000 48.325  ? 120 LEU B CD1 1 ? 2 
ATOM   2118 C CD2 . LEU B 1 124 ? 21.729 23.777  42.447  1.000 45.965  ? 120 LEU B CD2 1 ? 2 
ATOM   2119 N N   . LYS B 1 125 ? 20.013 23.318  37.830  1.000 47.292  ? 121 LYS B N   1 ? 2 
ATOM   2120 C CA  . LYS B 1 125 ? 20.956 23.693  36.734  1.000 47.472  ? 121 LYS B CA  1 ? 2 
ATOM   2121 C C   . LYS B 1 125 ? 21.583 25.035  37.129  1.000 43.052  ? 121 LYS B C   1 ? 2 
ATOM   2122 O O   . LYS B 1 125 ? 20.830 25.946  37.402  1.000 43.230  ? 121 LYS B O   1 ? 2 
ATOM   2123 C CB  . LYS B 1 125 ? 20.221 23.675  35.379  1.000 51.284  ? 121 LYS B CB  1 ? 2 
ATOM   2124 C CG  . LYS B 1 125 ? 19.615 22.296  35.043  1.000 59.131  ? 121 LYS B CG  1 ? 2 
ATOM   2125 C CD  . LYS B 1 125 ? 18.966 22.018  33.654  1.000 64.199  ? 121 LYS B CD  1 ? 2 
ATOM   2126 C CE  . LYS B 1 125 ? 17.466 22.274  33.516  1.000 68.243  ? 121 LYS B CE  1 ? 2 
ATOM   2127 N NZ  . LYS B 1 125 ? 16.759 22.391  34.822  1.000 72.192  ? 121 LYS B NZ  1 ? 2 
ATOM   2128 N N   . MET B 1 126 ? 22.904 25.174  37.203  1.000 39.718  ? 122 MET B N   1 ? 2 
ATOM   2129 C CA  . MET B 1 126 ? 23.495 26.495  37.536  1.000 39.332  ? 122 MET B CA  1 ? 2 
ATOM   2130 C C   . MET B 1 126 ? 24.943 26.643  37.079  1.000 37.268  ? 122 MET B C   1 ? 2 
ATOM   2131 O O   . MET B 1 126 ? 25.614 25.650  36.934  1.000 37.155  ? 122 MET B O   1 ? 2 
ATOM   2132 C CB  . MET B 1 126 ? 23.450 26.723  39.040  1.000 41.447  ? 122 MET B CB  1 ? 2 
ATOM   2133 C CG  . MET B 1 126 ? 24.376 25.838  39.777  1.000 43.852  ? 122 MET B CG  1 ? 2 
ATOM   2134 S SD  . MET B 1 126 ? 25.945 26.660  40.137  1.000 47.883  ? 122 MET B SD  1 ? 2 
ATOM   2135 C CE  . MET B 1 126 ? 26.776 25.372  41.057  1.000 47.433  ? 122 MET B CE  1 ? 2 
ATOM   2136 N N   . ASP B 1 127 ? 25.370 27.881  36.877  1.000 36.930  ? 123 ASP B N   1 ? 2 
ATOM   2137 C CA  . ASP B 1 127 ? 26.771 28.317  36.697  1.000 38.523  ? 123 ASP B CA  1 ? 2 
ATOM   2138 C C   . ASP B 1 127 ? 27.020 29.466  37.642  1.000 36.343  ? 123 ASP B C   1 ? 2 
ATOM   2139 O O   . ASP B 1 127 ? 26.152 30.277  37.828  1.000 37.190  ? 123 ASP B O   1 ? 2 
ATOM   2140 C CB  . ASP B 1 127 ? 27.081 28.919  35.323  1.000 43.318  ? 123 ASP B CB  1 ? 2 
ATOM   2141 C CG  . ASP B 1 127 ? 26.270 28.221  34.273  1.000 49.959  ? 123 ASP B CG  1 ? 2 
ATOM   2142 O OD1 . ASP B 1 127 ? 25.131 28.641  34.099  1.000 57.149  ? 123 ASP B OD1 1 ? 2 
ATOM   2143 O OD2 . ASP B 1 127 ? 26.723 27.169  33.777  1.000 60.285  ? 123 ASP B OD2 1 ? 2 
ATOM   2144 N N   . GLU B 1 128 ? 28.228 29.596  38.117  1.000 35.042  ? 124 GLU B N   1 ? 2 
ATOM   2145 C CA  . GLU B 1 128 ? 28.586 30.790  38.882  1.000 33.938  ? 124 GLU B CA  1 ? 2 
ATOM   2146 C C   . GLU B 1 128 ? 30.040 31.060  38.597  1.000 31.111  ? 124 GLU B C   1 ? 2 
ATOM   2147 O O   . GLU B 1 128 ? 30.760 30.098  38.433  1.000 30.321  ? 124 GLU B O   1 ? 2 
ATOM   2148 C CB  . GLU B 1 128 ? 28.456 30.502  40.360  1.000 35.882  ? 124 GLU B CB  1 ? 2 
ATOM   2149 C CG  . GLU B 1 128 ? 27.041 30.359  40.807  1.000 38.593  ? 124 GLU B CG  1 ? 2 
ATOM   2150 C CD  . GLU B 1 128 ? 27.016 30.415  42.319  1.000 40.853  ? 124 GLU B CD  1 ? 2 
ATOM   2151 O OE1 . GLU B 1 128 ? 27.636 29.552  43.015  1.000 42.618  ? 124 GLU B OE1 1 ? 2 
ATOM   2152 O OE2 . GLU B 1 128 ? 26.479 31.363  42.784  1.000 44.076  ? 124 GLU B OE2 1 ? 2 
ATOM   2153 N N   . ALA B 1 129 ? 30.423 32.313  38.653  1.000 29.620  ? 125 ALA B N   1 ? 2 
ATOM   2154 C CA  . ALA B 1 129 ? 31.823 32.733  38.634  1.000 30.686  ? 125 ALA B CA  1 ? 2 
ATOM   2155 C C   . ALA B 1 129 ? 31.952 33.955  39.549  1.000 31.703  ? 125 ALA B C   1 ? 2 
ATOM   2156 O O   . ALA B 1 129 ? 31.060 34.774  39.521  1.000 31.826  ? 125 ALA B O   1 ? 2 
ATOM   2157 C CB  . ALA B 1 129 ? 32.264 32.969  37.208  1.000 29.371  ? 125 ALA B CB  1 ? 2 
ATOM   2158 N N   . PHE B 1 130 ? 32.988 34.017  40.394  1.000 33.589  ? 126 PHE B N   1 ? 2 
ATOM   2159 C CA  . PHE B 1 130 ? 33.165 35.060  41.437  1.000 35.139  ? 126 PHE B CA  1 ? 2 
ATOM   2160 C C   . PHE B 1 130 ? 34.491 34.833  42.161  1.000 35.156  ? 126 PHE B C   1 ? 2 
ATOM   2161 O O   . PHE B 1 130 ? 35.129 33.843  41.904  1.000 33.682  ? 126 PHE B O   1 ? 2 
ATOM   2162 C CB  . PHE B 1 130 ? 31.981 35.074  42.409  1.000 35.461  ? 126 PHE B CB  1 ? 2 
ATOM   2163 C CG  . PHE B 1 130 ? 31.767 33.765  43.120  1.000 35.909  ? 126 PHE B CG  1 ? 2 
ATOM   2164 C CD1 . PHE B 1 130 ? 31.044 32.743  42.528  1.000 35.042  ? 126 PHE B CD1 1 ? 2 
ATOM   2165 C CD2 . PHE B 1 130 ? 32.326 33.538  44.377  1.000 37.320  ? 126 PHE B CD2 1 ? 2 
ATOM   2166 C CE1 . PHE B 1 130 ? 30.878 31.532  43.187  1.000 35.978  ? 126 PHE B CE1 1 ? 2 
ATOM   2167 C CE2 . PHE B 1 130 ? 32.127 32.335  45.050  1.000 36.683  ? 126 PHE B CE2 1 ? 2 
ATOM   2168 C CZ  . PHE B 1 130 ? 31.410 31.330  44.445  1.000 36.220  ? 126 PHE B CZ  1 ? 2 
ATOM   2169 N N   . SER B 1 131 ? 34.847 35.754  43.050  1.000 36.615  ? 127 SER B N   1 ? 2 
ATOM   2170 C CA  . SER B 1 131 ? 36.135 35.783  43.766  1.000 37.953  ? 127 SER B CA  1 ? 2 
ATOM   2171 C C   . SER B 1 131 ? 35.882 35.472  45.255  1.000 37.553  ? 127 SER B C   1 ? 2 
ATOM   2172 O O   . SER B 1 131 ? 34.810 35.755  45.725  1.000 36.847  ? 127 SER B O   1 ? 2 
ATOM   2173 C CB  . SER B 1 131 ? 36.799 37.125  43.534  1.000 40.548  ? 127 SER B CB  1 ? 2 
ATOM   2174 O OG  . SER B 1 131 ? 37.438 37.171  42.251  1.000 46.031  ? 127 SER B OG  1 ? 2 
ATOM   2175 N N   . ILE B 1 132 ? 36.821 34.858  45.968  1.000 37.159  ? 128 ILE B N   1 ? 2 
ATOM   2176 C CA  . ILE B 1 132 ? 36.695 34.605  47.426  1.000 38.361  ? 128 ILE B CA  1 ? 2 
ATOM   2177 C C   . ILE B 1 132 ? 37.965 35.057  48.165  1.000 40.265  ? 128 ILE B C   1 ? 2 
ATOM   2178 O O   . ILE B 1 132 ? 39.034 35.249  47.515  1.000 41.033  ? 128 ILE B O   1 ? 2 
ATOM   2179 C CB  . ILE B 1 132 ? 36.335 33.136  47.688  1.000 39.216  ? 128 ILE B CB  1 ? 2 
ATOM   2180 C CG1 . ILE B 1 132 ? 37.397 32.149  47.205  1.000 39.017  ? 128 ILE B CG1 1 ? 2 
ATOM   2181 C CG2 . ILE B 1 132 ? 34.984 32.816  47.080  1.000 38.702  ? 128 ILE B CG2 1 ? 2 
ATOM   2182 C CD1 . ILE B 1 132 ? 37.125 30.731  47.653  1.000 38.832  ? 128 ILE B CD1 1 ? 2 
ATOM   2183 N N   . SER B 1 133 ? 37.844 35.278  49.474  1.000 40.195  ? 129 SER B N   1 ? 2 
ATOM   2184 C CA  . SER B 1 133 ? 38.948 35.799  50.314  1.000 42.221  ? 129 SER B CA  1 ? 2 
ATOM   2185 C C   . SER B 1 133 ? 39.961 34.678  50.522  1.000 43.085  ? 129 SER B C   1 ? 2 
ATOM   2186 O O   . SER B 1 133 ? 39.610 33.490  50.242  1.000 39.546  ? 129 SER B O   1 ? 2 
ATOM   2187 C CB  . SER B 1 133 ? 38.426 36.322  51.638  1.000 41.317  ? 129 SER B CB  1 ? 2 
ATOM   2188 O OG  . SER B 1 133 ? 37.965 35.247  52.434  1.000 39.207  ? 129 SER B OG  1 ? 2 
ATOM   2189 N N   . LEU B 1 134 ? 41.133 35.045  51.044  1.000 47.150  ? 130 LEU B N   1 ? 2 
ATOM   2190 C CA  . LEU B 1 134 ? 42.191 34.096  51.485  1.000 50.136  ? 130 LEU B CA  1 ? 2 
ATOM   2191 C C   . LEU B 1 134 ? 41.667 33.206  52.603  1.000 48.023  ? 130 LEU B C   1 ? 2 
ATOM   2192 O O   . LEU B 1 134 ? 41.991 32.016  52.577  1.000 49.669  ? 130 LEU B O   1 ? 2 
ATOM   2193 C CB  . LEU B 1 134 ? 43.432 34.867  51.933  1.000 54.531  ? 130 LEU B CB  1 ? 2 
ATOM   2194 C CG  . LEU B 1 134 ? 44.146 35.613  50.802  1.000 59.238  ? 130 LEU B CG  1 ? 2 
ATOM   2195 C CD1 . LEU B 1 134 ? 45.156 36.629  51.325  1.000 59.802  ? 130 LEU B CD1 1 ? 2 
ATOM   2196 C CD2 . LEU B 1 134 ? 44.822 34.632  49.848  1.000 61.112  ? 130 LEU B CD2 1 ? 2 
ATOM   2197 N N   . GLU B 1 135 ? 40.860 33.739  53.512  1.000 47.019  ? 131 GLU B N   1 ? 2 
ATOM   2198 C CA  . GLU B 1 135 ? 40.262 32.916  54.596  1.000 49.526  ? 131 GLU B CA  1 ? 2 
ATOM   2199 C C   . GLU B 1 135 ? 39.292 31.926  53.921  1.000 47.650  ? 131 GLU B C   1 ? 2 
ATOM   2200 O O   . GLU B 1 135 ? 39.366 30.700  54.244  1.000 44.208  ? 131 GLU B O   1 ? 2 
ATOM   2201 C CB  . GLU B 1 135 ? 39.675 33.826  55.697  1.000 56.157  ? 131 GLU B CB  1 ? 2 
ATOM   2202 C CG  . GLU B 1 135 ? 38.568 33.218  56.582  1.000 62.267  ? 131 GLU B CG  1 ? 2 
ATOM   2203 C CD  . GLU B 1 135 ? 38.945 32.568  57.914  1.000 67.941  ? 131 GLU B CD  1 ? 2 
ATOM   2204 O OE1 . GLU B 1 135 ? 39.973 31.808  57.990  1.000 67.248  ? 131 GLU B OE1 1 ? 2 
ATOM   2205 O OE2 . GLU B 1 135 ? 38.165 32.784  58.878  1.000 76.396  ? 131 GLU B OE2 1 ? 2 
ATOM   2206 N N   . GLN B 1 136 ? 38.456 32.398  52.984  1.000 42.776  ? 132 GLN B N   1 ? 2 
ATOM   2207 C CA  . GLN B 1 136 ? 37.465 31.519  52.308  1.000 41.554  ? 132 GLN B CA  1 ? 2 
ATOM   2208 C C   . GLN B 1 136 ? 38.198 30.387  51.570  1.000 39.574  ? 132 GLN B C   1 ? 2 
ATOM   2209 O O   . GLN B 1 136 ? 37.781 29.213  51.709  1.000 38.928  ? 132 GLN B O   1 ? 2 
ATOM   2210 C CB  . GLN B 1 136 ? 36.558 32.351  51.411  1.000 42.106  ? 132 GLN B CB  1 ? 2 
ATOM   2211 C CG  . GLN B 1 136 ? 35.553 33.177  52.208  1.000 41.100  ? 132 GLN B CG  1 ? 2 
ATOM   2212 C CD  . GLN B 1 136 ? 34.779 34.105  51.314  1.000 41.253  ? 132 GLN B CD  1 ? 2 
ATOM   2213 O OE1 . GLN B 1 136 ? 35.323 34.698  50.385  1.000 44.309  ? 132 GLN B OE1 1 ? 2 
ATOM   2214 N NE2 . GLN B 1 136 ? 33.485 34.189  51.543  1.000 41.025  ? 132 GLN B NE2 1 ? 2 
ATOM   2215 N N   . THR B 1 137 ? 39.320 30.685  50.922  1.000 38.373  ? 133 THR B N   1 ? 2 
ATOM   2216 C CA  . THR B 1 137 ? 40.133 29.690  50.165  1.000 37.914  ? 133 THR B CA  1 ? 2 
ATOM   2217 C C   . THR B 1 137 ? 40.598 28.555  51.079  1.000 37.390  ? 133 THR B C   1 ? 2 
ATOM   2218 O O   . THR B 1 137 ? 40.539 27.361  50.674  1.000 34.589  ? 133 THR B O   1 ? 2 
ATOM   2219 C CB  . THR B 1 137 ? 41.347 30.374  49.524  1.000 36.203  ? 133 THR B CB  1 ? 2 
ATOM   2220 O OG1 . THR B 1 137 ? 40.873 31.478  48.743  1.000 34.298  ? 133 THR B OG1 1 ? 2 
ATOM   2221 C CG2 . THR B 1 137 ? 42.138 29.404  48.685  1.000 34.906  ? 133 THR B CG2 1 ? 2 
ATOM   2222 N N   . GLU B 1 138 ? 41.096 28.942  52.246  1.000 39.965  ? 134 GLU B N   1 ? 2 
ATOM   2223 C CA  . GLU B 1 138 ? 41.528 28.022  53.328  1.000 43.200  ? 134 GLU B CA  1 ? 2 
ATOM   2224 C C   . GLU B 1 138 ? 40.360 27.118  53.710  1.000 38.738  ? 134 GLU B C   1 ? 2 
ATOM   2225 O O   . GLU B 1 138 ? 40.546 25.886  53.726  1.000 35.213  ? 134 GLU B O   1 ? 2 
ATOM   2226 C CB  . GLU B 1 138 ? 42.065 28.808  54.534  1.000 50.849  ? 134 GLU B CB  1 ? 2 
ATOM   2227 C CG  . GLU B 1 138 ? 43.592 28.905  54.570  1.000 57.784  ? 134 GLU B CG  1 ? 2 
ATOM   2228 C CD  . GLU B 1 138 ? 44.185 30.310  54.704  1.000 66.483  ? 134 GLU B CD  1 ? 2 
ATOM   2229 O OE1 . GLU B 1 138 ? 44.633 30.864  53.666  1.000 73.328  ? 134 GLU B OE1 1 ? 2 
ATOM   2230 O OE2 . GLU B 1 138 ? 44.208 30.860  55.845  1.000 72.563  ? 134 GLU B OE2 1 ? 2 
ATOM   2231 N N   . GLU B 1 139 ? 39.190 27.692  53.986  1.000 39.687  ? 135 GLU B N   1 ? 2 
ATOM   2232 C CA  . GLU B 1 139 ? 37.996 26.883  54.376  1.000 41.375  ? 135 GLU B CA  1 ? 2 
ATOM   2233 C C   . GLU B 1 139 ? 37.700 25.882  53.254  1.000 39.771  ? 135 GLU B C   1 ? 2 
ATOM   2234 O O   . GLU B 1 139 ? 37.566 24.678  53.561  1.000 35.728  ? 135 GLU B O   1 ? 2 
ATOM   2235 C CB  . GLU B 1 139 ? 36.776 27.754  54.703  1.000 43.209  ? 135 GLU B CB  1 ? 2 
ATOM   2236 C CG  . GLU B 1 139 ? 36.820 28.370  56.096  1.000 45.399  ? 135 GLU B CG  1 ? 2 
ATOM   2237 C CD  . GLU B 1 139 ? 36.038 29.652  56.330  1.000 45.426  ? 135 GLU B CD  1 ? 2 
ATOM   2238 O OE1 . GLU B 1 139 ? 35.168 29.965  55.513  1.000 44.990  ? 135 GLU B OE1 1 ? 2 
ATOM   2239 O OE2 . GLU B 1 139 ? 36.349 30.349  57.325  1.000 50.485  ? 135 GLU B OE2 1 ? 2 
ATOM   2240 N N   . LEU B 1 140 ? 37.649 26.362  51.996  1.000 39.910  ? 136 LEU B N   1 ? 2 
ATOM   2241 C CA  . LEU B 1 140 ? 37.299 25.511  50.816  1.000 37.331  ? 136 LEU B CA  1 ? 2 
ATOM   2242 C C   . LEU B 1 140 ? 38.379 24.432  50.660  1.000 36.077  ? 136 LEU B C   1 ? 2 
ATOM   2243 O O   . LEU B 1 140 ? 38.015 23.249  50.429  1.000 34.468  ? 136 LEU B O   1 ? 2 
ATOM   2244 C CB  . LEU B 1 140 ? 37.190 26.369  49.551  1.000 37.620  ? 136 LEU B CB  1 ? 2 
ATOM   2245 C CG  . LEU B 1 140 ? 36.521 25.688  48.353  1.000 39.287  ? 136 LEU B CG  1 ? 2 
ATOM   2246 C CD1 . LEU B 1 140 ? 35.072 25.330  48.619  1.000 39.036  ? 136 LEU B CD1 1 ? 2 
ATOM   2247 C CD2 . LEU B 1 140 ? 36.581 26.559  47.111  1.000 40.445  ? 136 LEU B CD2 1 ? 2 
ATOM   2248 N N   . THR B 1 141 ? 39.657 24.805  50.838  1.000 33.609  ? 137 THR B N   1 ? 2 
ATOM   2249 C CA  . THR B 1 141 ? 40.771 23.866  50.624  1.000 32.491  ? 137 THR B CA  1 ? 2 
ATOM   2250 C C   . THR B 1 141 ? 40.585 22.668  51.536  1.000 33.420  ? 137 THR B C   1 ? 2 
ATOM   2251 O O   . THR B 1 141 ? 40.850 21.552  51.058  1.000 34.701  ? 137 THR B O   1 ? 2 
ATOM   2252 C CB  . THR B 1 141 ? 42.138 24.525  50.729  1.000 32.004  ? 137 THR B CB  1 ? 2 
ATOM   2253 O OG1 . THR B 1 141 ? 42.328 25.405  49.612  1.000 31.461  ? 137 THR B OG1 1 ? 2 
ATOM   2254 C CG2 . THR B 1 141 ? 43.237 23.493  50.677  1.000 31.846  ? 137 THR B CG2 1 ? 2 
ATOM   2255 N N   . GLU B 1 142 ? 40.098 22.844  52.763  1.000 34.380  ? 138 GLU B N   1 ? 2 
ATOM   2256 C CA  . GLU B 1 142 ? 40.002 21.696  53.709  1.000 36.286  ? 138 GLU B CA  1 ? 2 
ATOM   2257 C C   . GLU B 1 142 ? 38.865 20.773  53.274  1.000 34.772  ? 138 GLU B C   1 ? 2 
ATOM   2258 O O   . GLU B 1 142 ? 38.943 19.562  53.584  1.000 33.986  ? 138 GLU B O   1 ? 2 
ATOM   2259 C CB  . GLU B 1 142 ? 39.807 22.150  55.160  1.000 41.714  ? 138 GLU B CB  1 ? 2 
ATOM   2260 C CG  . GLU B 1 142 ? 41.061 22.652  55.831  1.000 46.113  ? 138 GLU B CG  1 ? 2 
ATOM   2261 C CD  . GLU B 1 142 ? 42.226 21.662  55.801  1.000 55.115  ? 138 GLU B CD  1 ? 2 
ATOM   2262 O OE1 . GLU B 1 142 ? 41.956 20.383  55.951  1.000 57.103  ? 138 GLU B OE1 1 ? 2 
ATOM   2263 O OE2 . GLU B 1 142 ? 43.418 22.152  55.614  1.000 54.295  ? 138 GLU B OE2 1 ? 2 
ATOM   2264 N N   . MET B 1 143 ? 37.813 21.321  52.640  1.000 34.106  ? 139 MET B N   1 ? 2 
ATOM   2265 C CA  . MET B 1 143 ? 36.630 20.536  52.202  1.000 32.291  ? 139 MET B CA  1 ? 2 
ATOM   2266 C C   . MET B 1 143 ? 37.055 19.720  50.992  1.000 30.903  ? 139 MET B C   1 ? 2 
ATOM   2267 O O   . MET B 1 143 ? 36.584 18.595  50.834  1.000 30.005  ? 139 MET B O   1 ? 2 
ATOM   2268 C CB  . MET B 1 143 ? 35.446 21.424  51.818  1.000 33.582  ? 139 MET B CB  1 ? 2 
ATOM   2269 C CG  . MET B 1 143 ? 34.788 22.226  52.973  1.000 34.935  ? 139 MET B CG  1 ? 2 
ATOM   2270 S SD  . MET B 1 143 ? 34.306 21.197  54.402  1.000 35.460  ? 139 MET B SD  1 ? 2 
ATOM   2271 C CE  . MET B 1 143 ? 32.778 20.464  53.824  1.000 35.760  ? 139 MET B CE  1 ? 2 
ATOM   2272 N N   . PHE B 1 144 ? 37.944 20.289  50.187  1.000 30.347  ? 140 PHE B N   1 ? 2 
ATOM   2273 C CA  . PHE B 1 144 ? 38.595 19.661  49.007  1.000 29.893  ? 140 PHE B CA  1 ? 2 
ATOM   2274 C C   . PHE B 1 144 ? 39.487 18.471  49.452  1.000 29.415  ? 140 PHE B C   1 ? 2 
ATOM   2275 O O   . PHE B 1 144 ? 39.347 17.339  48.925  1.000 29.857  ? 140 PHE B O   1 ? 2 
ATOM   2276 C CB  . PHE B 1 144 ? 39.307 20.782  48.239  1.000 30.343  ? 140 PHE B CB  1 ? 2 
ATOM   2277 C CG  . PHE B 1 144 ? 40.259 20.299  47.168  1.000 31.955  ? 140 PHE B CG  1 ? 2 
ATOM   2278 C CD1 . PHE B 1 144 ? 41.622 20.185  47.418  1.000 30.794  ? 140 PHE B CD1 1 ? 2 
ATOM   2279 C CD2 . PHE B 1 144 ? 39.784 19.938  45.912  1.000 31.690  ? 140 PHE B CD2 1 ? 2 
ATOM   2280 C CE1 . PHE B 1 144 ? 42.490 19.777  46.422  1.000 31.642  ? 140 PHE B CE1 1 ? 2 
ATOM   2281 C CE2 . PHE B 1 144 ? 40.645 19.496  44.936  1.000 30.847  ? 140 PHE B CE2 1 ? 2 
ATOM   2282 C CZ  . PHE B 1 144 ? 41.996 19.393  45.199  1.000 31.981  ? 140 PHE B CZ  1 ? 2 
ATOM   2283 N N   . TYR B 1 145 ? 40.408 18.659  50.403  1.000 28.501  ? 141 TYR B N   1 ? 2 
ATOM   2284 C CA  . TYR B 1 145 ? 41.232 17.541  50.936  1.000 28.168  ? 141 TYR B CA  1 ? 2 
ATOM   2285 C C   . TYR B 1 145 ? 40.327 16.434  51.460  1.000 27.001  ? 141 TYR B C   1 ? 2 
ATOM   2286 O O   . TYR B 1 145 ? 40.588 15.285  51.225  1.000 26.911  ? 141 TYR B O   1 ? 2 
ATOM   2287 C CB  . TYR B 1 145 ? 42.175 18.008  52.044  1.000 30.042  ? 141 TYR B CB  1 ? 2 
ATOM   2288 C CG  . TYR B 1 145 ? 43.273 18.929  51.576  1.000 31.525  ? 141 TYR B CG  1 ? 2 
ATOM   2289 C CD1 . TYR B 1 145 ? 43.795 18.847  50.282  1.000 31.890  ? 141 TYR B CD1 1 ? 2 
ATOM   2290 C CD2 . TYR B 1 145 ? 43.753 19.918  52.418  1.000 31.134  ? 141 TYR B CD2 1 ? 2 
ATOM   2291 C CE1 . TYR B 1 145 ? 44.776 19.721  49.847  1.000 32.073  ? 141 TYR B CE1 1 ? 2 
ATOM   2292 C CE2 . TYR B 1 145 ? 44.730 20.801  52.003  1.000 31.853  ? 141 TYR B CE2 1 ? 2 
ATOM   2293 C CZ  . TYR B 1 145 ? 45.243 20.686  50.726  1.000 33.080  ? 141 TYR B CZ  1 ? 2 
ATOM   2294 O OH  . TYR B 1 145 ? 46.186 21.566  50.335  1.000 34.212  ? 141 TYR B OH  1 ? 2 
ATOM   2295 N N   . GLU B 1 146 ? 39.245 16.787  52.123  1.000 26.606  ? 142 GLU B N   1 ? 2 
ATOM   2296 C CA  . GLU B 1 146 ? 38.228 15.800  52.576  1.000 27.082  ? 142 GLU B CA  1 ? 2 
ATOM   2297 C C   . GLU B 1 146 ? 37.684 14.990  51.394  1.000 27.302  ? 142 GLU B C   1 ? 2 
ATOM   2298 O O   . GLU B 1 146 ? 37.671 13.751  51.487  1.000 28.158  ? 142 GLU B O   1 ? 2 
ATOM   2299 C CB  . GLU B 1 146 ? 37.162 16.559  53.351  1.000 27.301  ? 142 GLU B CB  1 ? 2 
ATOM   2300 C CG  . GLU B 1 146 ? 35.920 15.767  53.664  1.000 27.060  ? 142 GLU B CG  1 ? 2 
ATOM   2301 C CD  . GLU B 1 146 ? 36.093 14.445  54.386  1.000 26.848  ? 142 GLU B CD  1 ? 2 
ATOM   2302 O OE1 . GLU B 1 146 ? 37.197 14.067  54.838  1.000 25.870  ? 142 GLU B OE1 1 ? 2 
ATOM   2303 O OE2 . GLU B 1 146 ? 35.094 13.763  54.442  1.000 26.818  ? 142 GLU B OE2 1 ? 2 
ATOM   2304 N N   . LEU B 1 147 ? 37.300 15.637  50.286  1.000 28.497  ? 143 LEU B N   1 ? 2 
ATOM   2305 C CA  . LEU B 1 147 ? 36.967 14.937  49.000  1.000 26.638  ? 143 LEU B CA  1 ? 2 
ATOM   2306 C C   . LEU B 1 147 ? 38.186 14.111  48.596  1.000 24.811  ? 143 LEU B C   1 ? 2 
ATOM   2307 O O   . LEU B 1 147 ? 37.989 12.970  48.265  1.000 24.338  ? 143 LEU B O   1 ? 2 
ATOM   2308 C CB  . LEU B 1 147 ? 36.511 15.905  47.889  1.000 26.834  ? 143 LEU B CB  1 ? 2 
ATOM   2309 C CG  . LEU B 1 147 ? 35.979 15.199  46.612  1.000 27.854  ? 143 LEU B CG  1 ? 2 
ATOM   2310 C CD1 . LEU B 1 147 ? 34.659 14.477  46.849  1.000 27.545  ? 143 LEU B CD1 1 ? 2 
ATOM   2311 C CD2 . LEU B 1 147 ? 35.830 16.127  45.414  1.000 27.068  ? 143 LEU B CD2 1 ? 2 
ATOM   2312 N N   . GLY B 1 148 ? 39.396 14.627  48.775  1.000 24.340  ? 144 GLY B N   1 ? 2 
ATOM   2313 C CA  . GLY B 1 148 ? 40.631 13.912  48.383  1.000 25.055  ? 144 GLY B CA  1 ? 2 
ATOM   2314 C C   . GLY B 1 148 ? 40.775 12.511  48.976  1.000 26.313  ? 144 GLY B C   1 ? 2 
ATOM   2315 O O   . GLY B 1 148 ? 41.562 11.717  48.460  1.000 24.939  ? 144 GLY B O   1 ? 2 
ATOM   2316 N N   . ARG B 1 149 ? 40.107 12.223  50.102  1.000 29.618  ? 145 ARG B N   1 ? 2 
ATOM   2317 C CA  . ARG B 1 149 ? 40.227 10.918  50.814  1.000 30.171  ? 145 ARG B CA  1 ? 2 
ATOM   2318 C C   . ARG B 1 149 ? 39.631 9.833   49.944  1.000 30.078  ? 145 ARG B C   1 ? 2 
ATOM   2319 O O   . ARG B 1 149 ? 39.905 8.715   50.230  1.000 30.249  ? 145 ARG B O   1 ? 2 
ATOM   2320 C CB  . ARG B 1 149 ? 39.452 10.874  52.141  1.000 32.626  ? 145 ARG B CB  1 ? 2 
ATOM   2321 C CG  . ARG B 1 149 ? 40.127 11.570  53.327  1.000 33.489  ? 145 ARG B CG  1 ? 2 
ATOM   2322 C CD  . ARG B 1 149 ? 39.190 11.815  54.521  1.000 32.904  ? 145 ARG B CD  1 ? 2 
ATOM   2323 N NE  . ARG B 1 149 ? 38.475 10.598  54.790  1.000 32.734  ? 145 ARG B NE  1 ? 2 
ATOM   2324 C CZ  . ARG B 1 149 ? 37.170 10.473  54.892  1.000 32.572  ? 145 ARG B CZ  1 ? 2 
ATOM   2325 N NH1 . ARG B 1 149 ? 36.355 11.517  54.877  1.000 30.832  ? 145 ARG B NH1 1 ? 2 
ATOM   2326 N NH2 . ARG B 1 149 ? 36.690 9.261   55.062  1.000 33.394  ? 145 ARG B NH2 1 ? 2 
ATOM   2327 N N   . PHE B 1 150 ? 38.811 10.174  48.952  1.000 31.233  ? 146 PHE B N   1 ? 2 
ATOM   2328 C CA  . PHE B 1 150 ? 38.129 9.195   48.055  1.000 31.575  ? 146 PHE B CA  1 ? 2 
ATOM   2329 C C   . PHE B 1 150 ? 38.882 8.941   46.742  1.000 30.337  ? 146 PHE B C   1 ? 2 
ATOM   2330 O O   . PHE B 1 150 ? 38.402 8.205   45.904  1.000 30.566  ? 146 PHE B O   1 ? 2 
ATOM   2331 C CB  . PHE B 1 150 ? 36.733 9.722   47.802  1.000 32.377  ? 146 PHE B CB  1 ? 2 
ATOM   2332 C CG  . PHE B 1 150 ? 35.986 9.728   49.094  1.000 31.980  ? 146 PHE B CG  1 ? 2 
ATOM   2333 C CD1 . PHE B 1 150 ? 35.481 8.540   49.595  1.000 33.385  ? 146 PHE B CD1 1 ? 2 
ATOM   2334 C CD2 . PHE B 1 150 ? 35.878 10.881  49.828  1.000 31.604  ? 146 PHE B CD2 1 ? 2 
ATOM   2335 C CE1 . PHE B 1 150 ? 34.874 8.505   50.836  1.000 33.822  ? 146 PHE B CE1 1 ? 2 
ATOM   2336 C CE2 . PHE B 1 150 ? 35.296 10.847  51.082  1.000 31.385  ? 146 PHE B CE2 1 ? 2 
ATOM   2337 C CZ  . PHE B 1 150 ? 34.776 9.671   51.567  1.000 32.559  ? 146 PHE B CZ  1 ? 2 
ATOM   2338 N N   . VAL B 1 151 ? 40.053 9.518   46.577  1.000 29.236  ? 147 VAL B N   1 ? 2 
ATOM   2339 C CA  . VAL B 1 151 ? 40.921 9.207   45.420  1.000 29.599  ? 147 VAL B CA  1 ? 2 
ATOM   2340 C C   . VAL B 1 151 ? 41.246 7.717   45.431  1.000 29.769  ? 147 VAL B C   1 ? 2 
ATOM   2341 O O   . VAL B 1 151 ? 41.606 7.247   46.493  1.000 28.126  ? 147 VAL B O   1 ? 2 
ATOM   2342 C CB  . VAL B 1 151 ? 42.183 10.075  45.488  1.000 30.569  ? 147 VAL B CB  1 ? 2 
ATOM   2343 C CG1 . VAL B 1 151 ? 43.304 9.540   44.592  1.000 31.404  ? 147 VAL B CG1 1 ? 2 
ATOM   2344 C CG2 . VAL B 1 151 ? 41.822 11.533  45.155  1.000 29.971  ? 147 VAL B CG2 1 ? 2 
ATOM   2345 N N   . VAL B 1 152 ? 41.108 7.027   44.284  1.000 30.675  ? 148 VAL B N   1 ? 2 
ATOM   2346 C CA  . VAL B 1 152 ? 41.526 5.597   44.063  1.000 33.074  ? 148 VAL B CA  1 ? 2 
ATOM   2347 C C   . VAL B 1 152 ? 42.790 5.499   43.184  1.000 34.961  ? 148 VAL B C   1 ? 2 
ATOM   2348 O O   . VAL B 1 152 ? 43.025 6.377   42.337  1.000 34.167  ? 148 VAL B O   1 ? 2 
ATOM   2349 C CB  . VAL B 1 152 ? 40.371 4.750   43.498  1.000 32.269  ? 148 VAL B CB  1 ? 2 
ATOM   2350 C CG1 . VAL B 1 152 ? 39.138 4.904   44.349  1.000 33.823  ? 148 VAL B CG1 1 ? 2 
ATOM   2351 C CG2 . VAL B 1 152 ? 40.020 5.120   42.091  1.000 32.117  ? 148 VAL B CG2 1 ? 2 
ATOM   2352 N N   . ASP B 1 153 ? 43.571 4.438   43.367  1.000 41.393  ? 149 ASP B N   1 ? 2 
ATOM   2353 C CA  . ASP B 1 153 ? 44.807 4.146   42.574  1.000 47.139  ? 149 ASP B CA  1 ? 2 
ATOM   2354 C C   . ASP B 1 153 ? 44.435 3.216   41.420  1.000 48.876  ? 149 ASP B C   1 ? 2 
ATOM   2355 O O   . ASP B 1 153 ? 44.912 3.511   40.279  1.000 53.246  ? 149 ASP B O   1 ? 2 
ATOM   2356 C CB  . ASP B 1 153 ? 45.971 3.709   43.481  1.000 50.349  ? 149 ASP B CB  1 ? 2 
ATOM   2357 C CG  . ASP B 1 153 ? 46.391 4.846   44.427  1.000 50.485  ? 149 ASP B CG  1 ? 2 
ATOM   2358 O OD1 . ASP B 1 153 ? 46.787 5.918   43.921  1.000 48.150  ? 149 ASP B OD1 1 ? 2 
ATOM   2359 O OD2 . ASP B 1 153 ? 46.255 4.679   45.661  1.000 53.654  ? 149 ASP B OD2 1 ? 2 
ATOM   2360 N N   . GLY B 1 154 ? 43.515 2.262   41.633  1.000 48.161  ? 150 GLY B N   1 ? 2 
ATOM   2361 C CA  . GLY B 1 154 ? 42.965 1.429   40.529  1.000 50.909  ? 150 GLY B CA  1 ? 2 
ATOM   2362 C C   . GLY B 1 154 ? 42.296 2.216   39.381  1.000 49.000  ? 150 GLY B C   1 ? 2 
ATOM   2363 O O   . GLY B 1 154 ? 42.075 3.444   39.507  1.000 47.782  ? 150 GLY B O   1 ? 2 
ATOM   2364 N N   . THR B 1 155 ? 41.991 1.519   38.287  1.000 44.389  ? 151 THR B N   1 ? 2 
ATOM   2365 C CA  . THR B 1 155 ? 40.897 1.831   37.342  1.000 45.884  ? 151 THR B CA  1 ? 2 
ATOM   2366 C C   . THR B 1 155 ? 39.860 0.695   37.350  1.000 50.689  ? 151 THR B C   1 ? 2 
ATOM   2367 O O   . THR B 1 155 ? 38.840 0.823   36.656  1.000 49.776  ? 151 THR B O   1 ? 2 
ATOM   2368 C CB  . THR B 1 155 ? 41.396 2.104   35.916  1.000 43.287  ? 151 THR B CB  1 ? 2 
ATOM   2369 O OG1 . THR B 1 155 ? 42.033 0.980   35.297  1.000 40.920  ? 151 THR B OG1 1 ? 2 
ATOM   2370 C CG2 . THR B 1 155 ? 42.326 3.287   35.906  1.000 43.720  ? 151 THR B CG2 1 ? 2 
ATOM   2371 N N   . LYS B 1 156 ? 40.115 -0.386  38.082  1.000 58.432  ? 152 LYS B N   1 ? 2 
ATOM   2372 C CA  . LYS B 1 156 ? 39.102 -1.436  38.365  1.000 64.975  ? 152 LYS B CA  1 ? 2 
ATOM   2373 C C   . LYS B 1 156 ? 38.467 -0.967  39.665  1.000 61.002  ? 152 LYS B C   1 ? 2 
ATOM   2374 O O   . LYS B 1 156 ? 39.219 -0.753  40.620  1.000 70.366  ? 152 LYS B O   1 ? 2 
ATOM   2375 C CB  . LYS B 1 156 ? 39.748 -2.823  38.451  1.000 74.207  ? 152 LYS B CB  1 ? 2 
ATOM   2376 C CG  . LYS B 1 156 ? 40.528 -3.252  37.200  1.000 79.102  ? 152 LYS B CG  1 ? 2 
ATOM   2377 C CD  . LYS B 1 156 ? 41.713 -4.127  37.502  1.000 81.957  ? 152 LYS B CD  1 ? 2 
ATOM   2378 C CE  . LYS B 1 156 ? 42.335 -3.796  38.846  1.000 83.055  ? 152 LYS B CE  1 ? 2 
ATOM   2379 N NZ  . LYS B 1 156 ? 43.636 -4.473  38.999  1.000 85.136  ? 152 LYS B NZ  1 ? 2 
ATOM   2380 N N   . GLY B 1 157 ? 37.173 -0.703  39.633  1.000 53.041  ? 153 GLY B N   1 ? 2 
ATOM   2381 C CA  . GLY B 1 157 ? 36.471 0.149   40.601  1.000 49.277  ? 153 GLY B CA  1 ? 2 
ATOM   2382 C C   . GLY B 1 157 ? 35.489 1.058   39.876  1.000 47.829  ? 153 GLY B C   1 ? 2 
ATOM   2383 O O   . GLY B 1 157 ? 35.903 1.617   38.826  1.000 44.288  ? 153 GLY B O   1 ? 2 
ATOM   2384 N N   . GLU B 1 158 ? 34.238 1.180   40.372  1.000 46.095  ? 154 GLU B N   1 ? 2 
ATOM   2385 C CA  . GLU B 1 158 ? 33.277 2.239   39.952  1.000 44.874  ? 154 GLU B CA  1 ? 2 
ATOM   2386 C C   . GLU B 1 158 ? 33.883 3.568   40.402  1.000 38.574  ? 154 GLU B C   1 ? 2 
ATOM   2387 O O   . GLU B 1 158 ? 34.476 3.561   41.502  1.000 36.928  ? 154 GLU B O   1 ? 2 
ATOM   2388 C CB  . GLU B 1 158 ? 31.833 2.025   40.449  1.000 49.877  ? 154 GLU B CB  1 ? 2 
ATOM   2389 C CG  . GLU B 1 158 ? 31.095 0.834   39.831  1.000 57.017  ? 154 GLU B CG  1 ? 2 
ATOM   2390 C CD  . GLU B 1 158 ? 30.685 0.926   38.356  1.000 67.975  ? 154 GLU B CD  1 ? 2 
ATOM   2391 O OE1 . GLU B 1 158 ? 31.318 1.747   37.582  1.000 74.974  ? 154 GLU B OE1 1 ? 2 
ATOM   2392 O OE2 . GLU B 1 158 ? 29.738 0.157   37.952  1.000 72.030  ? 154 GLU B OE2 1 ? 2 
ATOM   2393 N N   . GLN B 1 159 ? 33.780 4.605   39.546  1.000 33.317  ? 155 GLN B N   1 ? 2 
ATOM   2394 C CA  . GLN B 1 159 ? 34.376 5.950   39.673  1.000 30.371  ? 155 GLN B CA  1 ? 2 
ATOM   2395 C C   . GLN B 1 159 ? 33.298 7.029   39.675  1.000 30.024  ? 155 GLN B C   1 ? 2 
ATOM   2396 O O   . GLN B 1 159 ? 32.298 6.859   38.977  1.000 33.025  ? 155 GLN B O   1 ? 2 
ATOM   2397 C CB  . GLN B 1 159 ? 35.304 6.154   38.502  1.000 28.978  ? 155 GLN B CB  1 ? 2 
ATOM   2398 C CG  . GLN B 1 159 ? 36.437 5.143   38.512  1.000 29.591  ? 155 GLN B CG  1 ? 2 
ATOM   2399 C CD  . GLN B 1 159 ? 37.013 4.864   37.145  1.000 29.011  ? 155 GLN B CD  1 ? 2 
ATOM   2400 O OE1 . GLN B 1 159 ? 36.632 5.476   36.143  1.000 27.707  ? 155 GLN B OE1 1 ? 2 
ATOM   2401 N NE2 . GLN B 1 159 ? 37.927 3.908   37.115  1.000 28.974  ? 155 GLN B NE2 1 ? 2 
ATOM   2402 N N   . GLY B 1 160 ? 33.500 8.103   40.437  1.000 28.749  ? 156 GLY B N   1 ? 2 
ATOM   2403 C CA  . GLY B 1 160 ? 32.514 9.183   40.640  1.000 28.063  ? 156 GLY B CA  1 ? 2 
ATOM   2404 C C   . GLY B 1 160 ? 32.986 10.468  39.994  1.000 27.626  ? 156 GLY B C   1 ? 2 
ATOM   2405 O O   . GLY B 1 160 ? 32.296 11.513  40.144  1.000 28.228  ? 156 GLY B O   1 ? 2 
ATOM   2406 N N   . GLY B 1 161 ? 34.125 10.426  39.301  1.000 25.639  ? 157 GLY B N   1 ? 2 
ATOM   2407 C CA  . GLY B 1 161 ? 34.736 11.657  38.799  1.000 24.599  ? 157 GLY B CA  1 ? 2 
ATOM   2408 C C   . GLY B 1 161 ? 36.231 11.725  39.073  1.000 24.734  ? 157 GLY B C   1 ? 2 
ATOM   2409 O O   . GLY B 1 161 ? 36.927 10.643  39.221  1.000 23.445  ? 157 GLY B O   1 ? 2 
ATOM   2410 N N   . PHE B 1 162 ? 36.754 12.944  38.960  1.000 23.902  ? 158 PHE B N   1 ? 2 
ATOM   2411 C CA  . PHE B 1 162 ? 38.210 13.149  38.999  1.000 24.703  ? 158 PHE B CA  1 ? 2 
ATOM   2412 C C   . PHE B 1 162 ? 38.535 14.519  39.536  1.000 23.825  ? 158 PHE B C   1 ? 2 
ATOM   2413 O O   . PHE B 1 162 ? 37.654 15.383  39.591  1.000 22.711  ? 158 PHE B O   1 ? 2 
ATOM   2414 C CB  . PHE B 1 162 ? 38.817 13.014  37.606  1.000 26.783  ? 158 PHE B CB  1 ? 2 
ATOM   2415 C CG  . PHE B 1 162 ? 38.327 13.989  36.559  1.000 26.752  ? 158 PHE B CG  1 ? 2 
ATOM   2416 C CD1 . PHE B 1 162 ? 37.345 13.615  35.658  1.000 26.248  ? 158 PHE B CD1 1 ? 2 
ATOM   2417 C CD2 . PHE B 1 162 ? 38.900 15.245  36.428  1.000 27.067  ? 158 PHE B CD2 1 ? 2 
ATOM   2418 C CE1 . PHE B 1 162 ? 36.884 14.496  34.707  1.000 25.744  ? 158 PHE B CE1 1 ? 2 
ATOM   2419 C CE2 . PHE B 1 162 ? 38.439 16.125  35.461  1.000 28.047  ? 158 PHE B CE2 1 ? 2 
ATOM   2420 C CZ  . PHE B 1 162 ? 37.438 15.740  34.593  1.000 26.563  ? 158 PHE B CZ  1 ? 2 
ATOM   2421 N N   . ILE B 1 163 ? 39.807 14.689  39.835  1.000 24.140  ? 159 ILE B N   1 ? 2 
ATOM   2422 C CA  . ILE B 1 163 ? 40.374 15.975  40.319  1.000 26.102  ? 159 ILE B CA  1 ? 2 
ATOM   2423 C C   . ILE B 1 163 ? 41.623 16.275  39.516  1.000 27.464  ? 159 ILE B C   1 ? 2 
ATOM   2424 O O   . ILE B 1 163 ? 42.476 15.375  39.440  1.000 29.919  ? 159 ILE B O   1 ? 2 
ATOM   2425 C CB  . ILE B 1 163 ? 40.738 15.836  41.798  1.000 26.276  ? 159 ILE B CB  1 ? 2 
ATOM   2426 C CG1 . ILE B 1 163 ? 39.488 15.559  42.637  1.000 27.299  ? 159 ILE B CG1 1 ? 2 
ATOM   2427 C CG2 . ILE B 1 163 ? 41.508 17.045  42.244  1.000 26.128  ? 159 ILE B CG2 1 ? 2 
ATOM   2428 C CD1 . ILE B 1 163 ? 39.717 15.587  44.125  1.000 28.024  ? 159 ILE B CD1 1 ? 2 
ATOM   2429 N N   . SER B 1 164 ? 41.766 17.481  38.991  1.000 28.550  ? 160 SER B N   1 ? 2 
ATOM   2430 C CA  . SER B 1 164 ? 43.015 17.901  38.304  1.000 31.403  ? 160 SER B CA  1 ? 2 
ATOM   2431 C C   . SER B 1 164 ? 43.709 18.887  39.245  1.000 30.494  ? 160 SER B C   1 ? 2 
ATOM   2432 O O   . SER B 1 164 ? 43.005 19.713  39.786  1.000 28.355  ? 160 SER B O   1 ? 2 
ATOM   2433 C CB  . SER B 1 164 ? 42.784 18.482  36.865  1.000 32.212  ? 160 SER B CB  1 ? 2 
ATOM   2434 O OG  . SER B 1 164 ? 43.442 19.763  36.696  1.000 34.567  ? 160 SER B OG  1 ? 2 
ATOM   2435 N N   . ILE B 1 165 ? 45.043 18.814  39.329  1.000 31.412  ? 161 ILE B N   1 ? 2 
ATOM   2436 C CA  . ILE B 1 165 ? 45.918 19.766  40.061  1.000 32.516  ? 161 ILE B CA  1 ? 2 
ATOM   2437 C C   . ILE B 1 165 ? 46.840 20.475  39.068  1.000 33.583  ? 161 ILE B C   1 ? 2 
ATOM   2438 O O   . ILE B 1 165 ? 47.553 19.790  38.341  1.000 32.339  ? 161 ILE B O   1 ? 2 
ATOM   2439 C CB  . ILE B 1 165 ? 46.751 19.032  41.122  1.000 34.023  ? 161 ILE B CB  1 ? 2 
ATOM   2440 C CG1 . ILE B 1 165 ? 45.891 18.236  42.108  1.000 35.498  ? 161 ILE B CG1 1 ? 2 
ATOM   2441 C CG2 . ILE B 1 165 ? 47.646 20.015  41.841  1.000 34.816  ? 161 ILE B CG2 1 ? 2 
ATOM   2442 C CD1 . ILE B 1 165 ? 44.807 19.030  42.779  1.000 34.462  ? 161 ILE B CD1 1 ? 2 
ATOM   2443 N N   . ASP B 1 166 ? 46.851 21.811  39.091  1.000 35.872  ? 162 ASP B N   1 ? 2 
ATOM   2444 C CA  . ASP B 1 166 ? 47.840 22.672  38.398  1.000 38.881  ? 162 ASP B CA  1 ? 2 
ATOM   2445 C C   . ASP B 1 166 ? 47.881 22.307  36.893  1.000 40.409  ? 162 ASP B C   1 ? 2 
ATOM   2446 O O   . ASP B 1 166 ? 48.927 22.376  36.257  1.000 38.623  ? 162 ASP B O   1 ? 2 
ATOM   2447 C CB  . ASP B 1 166 ? 49.187 22.571  39.125  1.000 39.722  ? 162 ASP B CB  1 ? 2 
ATOM   2448 C CG  . ASP B 1 166 ? 49.244 23.273  40.481  1.000 41.805  ? 162 ASP B CG  1 ? 2 
ATOM   2449 O OD1 . ASP B 1 166 ? 48.324 24.086  40.799  1.000 41.514  ? 162 ASP B OD1 1 ? 2 
ATOM   2450 O OD2 . ASP B 1 166 ? 50.234 23.013  41.225  1.000 46.052  ? 162 ASP B OD2 1 ? 2 
ATOM   2451 N N   . GLU B 1 167 ? 46.752 21.930  36.333  1.000 42.504  ? 163 GLU B N   1 ? 2 
ATOM   2452 C CA  . GLU B 1 167 ? 46.603 21.557  34.898  1.000 46.934  ? 163 GLU B CA  1 ? 2 
ATOM   2453 C C   . GLU B 1 167 ? 47.576 20.453  34.481  1.000 45.040  ? 163 GLU B C   1 ? 2 
ATOM   2454 O O   . GLU B 1 167 ? 47.741 20.332  33.294  1.000 43.306  ? 163 GLU B O   1 ? 2 
ATOM   2455 C CB  . GLU B 1 167 ? 46.723 22.802  34.013  1.000 47.094  ? 163 GLU B CB  1 ? 2 
ATOM   2456 C CG  . GLU B 1 167 ? 45.567 23.769  34.215  1.000 48.323  ? 163 GLU B CG  1 ? 2 
ATOM   2457 C CD  . GLU B 1 167 ? 45.332 24.728  33.073  1.000 52.549  ? 163 GLU B CD  1 ? 2 
ATOM   2458 O OE1 . GLU B 1 167 ? 44.608 24.352  32.103  1.000 51.763  ? 163 GLU B OE1 1 ? 2 
ATOM   2459 O OE2 . GLU B 1 167 ? 45.904 25.838  33.147  1.000 57.862  ? 163 GLU B OE2 1 ? 2 
ATOM   2460 N N   . ARG B 1 168 ? 48.126 19.668  35.412  1.000 47.020  ? 164 ARG B N   1 ? 2 
ATOM   2461 C CA  . ARG B 1 168 ? 49.165 18.637  35.124  1.000 50.856  ? 164 ARG B CA  1 ? 2 
ATOM   2462 C C   . ARG B 1 168 ? 48.627 17.258  35.480  1.000 50.864  ? 164 ARG B C   1 ? 2 
ATOM   2463 O O   . ARG B 1 168 ? 48.422 16.445  34.589  1.000 58.589  ? 164 ARG B O   1 ? 2 
ATOM   2464 C CB  . ARG B 1 168 ? 50.446 18.860  35.930  1.000 55.172  ? 164 ARG B CB  1 ? 2 
ATOM   2465 C CG  . ARG B 1 168 ? 51.008 20.260  35.790  1.000 61.159  ? 164 ARG B CG  1 ? 2 
ATOM   2466 C CD  . ARG B 1 168 ? 51.814 20.765  36.976  1.000 65.040  ? 164 ARG B CD  1 ? 2 
ATOM   2467 N NE  . ARG B 1 168 ? 53.150 20.177  37.022  1.000 70.717  ? 164 ARG B NE  1 ? 2 
ATOM   2468 C CZ  . ARG B 1 168 ? 54.080 20.251  36.057  1.000 71.601  ? 164 ARG B CZ  1 ? 2 
ATOM   2469 N NH1 . ARG B 1 168 ? 53.851 20.879  34.905  1.000 70.164  ? 164 ARG B NH1 1 ? 2 
ATOM   2470 N NH2 . ARG B 1 168 ? 55.254 19.677  36.263  1.000 70.239  ? 164 ARG B NH2 1 ? 2 
ATOM   2471 N N   . ASP B 1 169 ? 48.372 17.010  36.751  1.000 49.035  ? 165 ASP B N   1 ? 2 
ATOM   2472 C CA  . ASP B 1 169 ? 47.983 15.665  37.224  1.000 45.053  ? 165 ASP B CA  1 ? 2 
ATOM   2473 C C   . ASP B 1 169 ? 46.471 15.594  37.343  1.000 37.490  ? 165 ASP B C   1 ? 2 
ATOM   2474 O O   . ASP B 1 169 ? 45.856 16.600  37.755  1.000 37.544  ? 165 ASP B O   1 ? 2 
ATOM   2475 C CB  . ASP B 1 169 ? 48.675 15.348  38.545  1.000 49.172  ? 165 ASP B CB  1 ? 2 
ATOM   2476 C CG  . ASP B 1 169 ? 50.136 15.122  38.286  1.000 50.955  ? 165 ASP B CG  1 ? 2 
ATOM   2477 O OD1 . ASP B 1 169 ? 50.393 14.376  37.350  1.000 51.086  ? 165 ASP B OD1 1 ? 2 
ATOM   2478 O OD2 . ASP B 1 169 ? 50.969 15.719  39.002  1.000 52.260  ? 165 ASP B OD2 1 ? 2 
ATOM   2479 N N   . VAL B 1 170 ? 45.948 14.399  37.102  1.000 32.202  ? 166 VAL B N   1 ? 2 
ATOM   2480 C CA  . VAL B 1 170 ? 44.516 14.063  37.254  1.000 30.652  ? 166 VAL B CA  1 ? 2 
ATOM   2481 C C   . VAL B 1 170 ? 44.340 12.778  38.072  1.000 29.165  ? 166 VAL B C   1 ? 2 
ATOM   2482 O O   . VAL B 1 170 ? 44.912 11.742  37.678  1.000 29.015  ? 166 VAL B O   1 ? 2 
ATOM   2483 C CB  . VAL B 1 170 ? 43.889 13.888  35.858  1.000 30.489  ? 166 VAL B CB  1 ? 2 
ATOM   2484 C CG1 . VAL B 1 170 ? 42.407 13.529  35.985  1.000 30.140  ? 166 VAL B CG1 1 ? 2 
ATOM   2485 C CG2 . VAL B 1 170 ? 44.089 15.120  34.990  1.000 29.914  ? 166 VAL B CG2 1 ? 2 
ATOM   2486 N N   . TYR B 1 171 ? 43.477 12.801  39.092  1.000 27.291  ? 167 TYR B N   1 ? 2 
ATOM   2487 C CA  . TYR B 1 171 ? 43.273 11.629  39.967  1.000 26.652  ? 167 TYR B CA  1 ? 2 
ATOM   2488 C C   . TYR B 1 171 ? 41.819 11.280  39.873  1.000 25.099  ? 167 TYR B C   1 ? 2 
ATOM   2489 O O   . TYR B 1 171 ? 41.060 12.232  39.788  1.000 24.735  ? 167 TYR B O   1 ? 2 
ATOM   2490 C CB  . TYR B 1 171 ? 43.636 11.975  41.404  1.000 27.464  ? 167 TYR B CB  1 ? 2 
ATOM   2491 C CG  . TYR B 1 171 ? 45.035 12.487  41.562  1.000 27.902  ? 167 TYR B CG  1 ? 2 
ATOM   2492 C CD1 . TYR B 1 171 ? 46.055 11.664  41.990  1.000 29.673  ? 167 TYR B CD1 1 ? 2 
ATOM   2493 C CD2 . TYR B 1 171 ? 45.326 13.804  41.287  1.000 27.803  ? 167 TYR B CD2 1 ? 2 
ATOM   2494 C CE1 . TYR B 1 171 ? 47.349 12.145  42.122  1.000 30.208  ? 167 TYR B CE1 1 ? 2 
ATOM   2495 C CE2 . TYR B 1 171 ? 46.606 14.301  41.384  1.000 29.001  ? 167 TYR B CE2 1 ? 2 
ATOM   2496 C CZ  . TYR B 1 171 ? 47.623 13.462  41.799  1.000 30.622  ? 167 TYR B CZ  1 ? 2 
ATOM   2497 O OH  . TYR B 1 171 ? 48.882 13.982  41.923  1.000 33.433  ? 167 TYR B OH  1 ? 2 
ATOM   2498 N N   . LEU B 1 172 ? 41.482 10.002  39.887  1.000 25.138  ? 168 LEU B N   1 ? 2 
ATOM   2499 C CA  . LEU B 1 172 ? 40.069 9.550   39.771  1.000 26.335  ? 168 LEU B CA  1 ? 2 
ATOM   2500 C C   . LEU B 1 172 ? 39.455 9.379   41.179  1.000 26.432  ? 168 LEU B C   1 ? 2 
ATOM   2501 O O   . LEU B 1 172 ? 40.140 8.904   42.034  1.000 26.517  ? 168 LEU B O   1 ? 2 
ATOM   2502 C CB  . LEU B 1 172 ? 40.054 8.225   39.014  1.000 26.473  ? 168 LEU B CB  1 ? 2 
ATOM   2503 C CG  . LEU B 1 172 ? 40.693 8.243   37.633  1.000 26.563  ? 168 LEU B CG  1 ? 2 
ATOM   2504 C CD1 . LEU B 1 172 ? 40.758 6.855   37.077  1.000 26.430  ? 168 LEU B CD1 1 ? 2 
ATOM   2505 C CD2 . LEU B 1 172 ? 39.946 9.147   36.690  1.000 26.344  ? 168 LEU B CD2 1 ? 2 
ATOM   2506 N N   . LEU B 1 173 ? 38.180 9.705   41.367  1.000 26.633  ? 169 LEU B N   1 ? 2 
ATOM   2507 C CA  . LEU B 1 173 ? 37.411 9.536   42.633  1.000 27.476  ? 169 LEU B CA  1 ? 2 
ATOM   2508 C C   . LEU B 1 173 ? 36.567 8.264   42.583  1.000 28.024  ? 169 LEU B C   1 ? 2 
ATOM   2509 O O   . LEU B 1 173 ? 36.072 7.946   41.480  1.000 28.709  ? 169 LEU B O   1 ? 2 
ATOM   2510 C CB  . LEU B 1 173 ? 36.512 10.758  42.796  1.000 26.868  ? 169 LEU B CB  1 ? 2 
ATOM   2511 C CG  . LEU B 1 173 ? 37.299 12.028  43.078  1.000 27.386  ? 169 LEU B CG  1 ? 2 
ATOM   2512 C CD1 . LEU B 1 173 ? 36.411 13.247  42.879  1.000 27.402  ? 169 LEU B CD1 1 ? 2 
ATOM   2513 C CD2 . LEU B 1 173 ? 37.905 11.967  44.490  1.000 27.088  ? 169 LEU B CD2 1 ? 2 
ATOM   2514 N N   . ALA B 1 174 ? 36.414 7.594   43.725  1.000 28.987  ? 170 ALA B N   1 ? 2 
ATOM   2515 C CA  . ALA B 1 174 ? 35.531 6.418   43.943  1.000 31.782  ? 170 ALA B CA  1 ? 2 
ATOM   2516 C C   . ALA B 1 174 ? 34.073 6.849   43.812  1.000 33.982  ? 170 ALA B C   1 ? 2 
ATOM   2517 O O   . ALA B 1 174 ? 33.827 8.041   43.936  1.000 37.960  ? 170 ALA B O   1 ? 2 
ATOM   2518 C CB  . ALA B 1 174 ? 35.806 5.784   45.286  1.000 31.214  ? 170 ALA B CB  1 ? 2 
ATOM   2519 N N   . ALA B 1 175 ? 33.150 5.933   43.507  1.000 37.432  ? 171 ALA B N   1 ? 2 
ATOM   2520 C CA  . ALA B 1 175 ? 31.672 6.166   43.502  1.000 38.556  ? 171 ALA B CA  1 ? 2 
ATOM   2521 C C   . ALA B 1 175 ? 31.150 5.902   44.918  1.000 40.447  ? 171 ALA B C   1 ? 2 
ATOM   2522 O O   . ALA B 1 175 ? 31.932 5.487   45.717  1.000 41.130  ? 171 ALA B O   1 ? 2 
ATOM   2523 C CB  . ALA B 1 175 ? 31.001 5.242   42.519  1.000 36.512  ? 171 ALA B CB  1 ? 2 
ATOM   2524 N N   . GLY B 1 176 ? 29.863 6.028   45.195  1.000 43.566  ? 172 GLY B N   1 ? 2 
ATOM   2525 C CA  . GLY B 1 176 ? 29.316 5.641   46.506  1.000 46.003  ? 172 GLY B CA  1 ? 2 
ATOM   2526 C C   . GLY B 1 176 ? 28.926 6.862   47.319  1.000 49.637  ? 172 GLY B C   1 ? 2 
ATOM   2527 O O   . GLY B 1 176 ? 29.408 8.002   47.004  1.000 52.448  ? 172 GLY B O   1 ? 2 
ATOM   2528 N N   . ARG B 1 177 ? 28.085 6.663   48.339  1.000 51.935  ? 173 ARG B N   1 ? 2 
ATOM   2529 C CA  . ARG B 1 177 ? 27.367 7.788   48.976  1.000 54.171  ? 173 ARG B CA  1 ? 2 
ATOM   2530 C C   . ARG B 1 177 ? 28.312 8.678   49.791  1.000 49.883  ? 173 ARG B C   1 ? 2 
ATOM   2531 O O   . ARG B 1 177 ? 28.061 9.896   49.862  1.000 46.677  ? 173 ARG B O   1 ? 2 
ATOM   2532 C CB  . ARG B 1 177 ? 26.210 7.316   49.850  1.000 63.346  ? 173 ARG B CB  1 ? 2 
ATOM   2533 C CG  . ARG B 1 177 ? 25.302 8.489   50.222  1.000 73.619  ? 173 ARG B CG  1 ? 2 
ATOM   2534 C CD  . ARG B 1 177 ? 24.844 8.290   51.655  1.000 78.239  ? 173 ARG B CD  1 ? 2 
ATOM   2535 N NE  . ARG B 1 177 ? 23.500 7.395   51.437  1.000 81.198  ? 173 ARG B NE  1 ? 2 
ATOM   2536 C CZ  . ARG B 1 177 ? 22.829 7.080   52.401  1.000 81.521  ? 173 ARG B CZ  1 ? 2 
ATOM   2537 N NH1 . ARG B 1 177 ? 22.979 7.544   53.712  1.000 78.938  ? 173 ARG B NH1 1 ? 2 
ATOM   2538 N NH2 . ARG B 1 177 ? 22.208 6.100   52.124  1.000 82.061  ? 173 ARG B NH2 1 ? 2 
ATOM   2539 N N   . GLU B 1 178 ? 29.345 8.126   50.415  1.000 46.930  ? 174 GLU B N   1 ? 2 
ATOM   2540 C CA  . GLU B 1 178 ? 30.264 8.963   51.213  1.000 45.638  ? 174 GLU B CA  1 ? 2 
ATOM   2541 C C   . GLU B 1 178 ? 31.003 9.936   50.287  1.000 39.007  ? 174 GLU B C   1 ? 2 
ATOM   2542 O O   . GLU B 1 178 ? 31.067 11.134  50.607  1.000 37.144  ? 174 GLU B O   1 ? 2 
ATOM   2543 C CB  . GLU B 1 178 ? 31.251 8.084   51.960  1.000 51.804  ? 174 GLU B CB  1 ? 2 
ATOM   2544 C CG  . GLU B 1 178 ? 30.693 7.359   53.166  1.000 54.944  ? 174 GLU B CG  1 ? 2 
ATOM   2545 C CD  . GLU B 1 178 ? 31.804 6.549   53.818  1.000 59.888  ? 174 GLU B CD  1 ? 2 
ATOM   2546 O OE1 . GLU B 1 178 ? 31.495 5.393   54.228  1.000 63.348  ? 174 GLU B OE1 1 ? 2 
ATOM   2547 O OE2 . GLU B 1 178 ? 32.996 7.082   53.908  1.000 57.487  ? 174 GLU B OE2 1 ? 2 
ATOM   2548 N N   . CYS B 1 179 ? 31.520 9.461   49.160  1.000 35.112  ? 175 CYS B N   1 ? 2 
ATOM   2549 C CA  . CYS B 1 179 ? 32.149 10.352  48.156  1.000 32.406  ? 175 CYS B CA  1 ? 2 
ATOM   2550 C C   . CYS B 1 179 ? 31.155 11.425  47.701  1.000 29.943  ? 175 CYS B C   1 ? 2 
ATOM   2551 O O   . CYS B 1 179 ? 31.546 12.604  47.712  1.000 27.995  ? 175 CYS B O   1 ? 2 
ATOM   2552 C CB  . CYS B 1 179 ? 32.656 9.611   46.937  1.000 33.529  ? 175 CYS B CB  1 ? 2 
ATOM   2553 S SG  . CYS B 1 179 ? 33.432 10.747  45.755  1.000 34.284  ? 175 CYS B SG  1 ? 2 
ATOM   2554 N N   . ALA B 1 180 ? 29.915 11.058  47.335  1.000 29.092  ? 176 ALA B N   1 ? 2 
ATOM   2555 C CA  . ALA B 1 180 ? 28.853 12.041  46.960  1.000 28.945  ? 176 ALA B CA  1 ? 2 
ATOM   2556 C C   . ALA B 1 180 ? 28.597 13.069  48.065  1.000 28.754  ? 176 ALA B C   1 ? 2 
ATOM   2557 O O   . ALA B 1 180 ? 28.495 14.274  47.725  1.000 27.940  ? 176 ALA B O   1 ? 2 
ATOM   2558 C CB  . ALA B 1 180 ? 27.567 11.380  46.581  1.000 28.686  ? 176 ALA B CB  1 ? 2 
ATOM   2559 N N   . GLU B 1 181 ? 28.514 12.635  49.332  1.000 29.821  ? 177 GLU B N   1 ? 2 
ATOM   2560 C CA  . GLU B 1 181 ? 28.256 13.555  50.456  1.000 30.206  ? 177 GLU B CA  1 ? 2 
ATOM   2561 C C   . GLU B 1 181 ? 29.397 14.570  50.520  1.000 28.287  ? 177 GLU B C   1 ? 2 
ATOM   2562 O O   . GLU B 1 181 ? 29.139 15.756  50.519  1.000 28.952  ? 177 GLU B O   1 ? 2 
ATOM   2563 C CB  . GLU B 1 181 ? 28.039 12.766  51.742  1.000 33.744  ? 177 GLU B CB  1 ? 2 
ATOM   2564 C CG  . GLU B 1 181 ? 27.665 13.659  52.908  1.000 36.224  ? 177 GLU B CG  1 ? 2 
ATOM   2565 C CD  . GLU B 1 181 ? 26.468 14.575  52.660  1.000 41.263  ? 177 GLU B CD  1 ? 2 
ATOM   2566 O OE1 . GLU B 1 181 ? 25.504 14.116  51.933  1.000 44.862  ? 177 GLU B OE1 1 ? 2 
ATOM   2567 O OE2 . GLU B 1 181 ? 26.474 15.746  53.190  1.000 42.258  ? 177 GLU B OE2 1 ? 2 
ATOM   2568 N N   . ALA B 1 182 ? 30.636 14.135  50.441  1.000 27.212  ? 178 ALA B N   1 ? 2 
ATOM   2569 C CA  . ALA B 1 182 ? 31.806 15.038  50.506  1.000 26.987  ? 178 ALA B CA  1 ? 2 
ATOM   2570 C C   . ALA B 1 182 ? 31.763 16.076  49.380  1.000 27.175  ? 178 ALA B C   1 ? 2 
ATOM   2571 O O   . ALA B 1 182 ? 32.055 17.277  49.647  1.000 26.738  ? 178 ALA B O   1 ? 2 
ATOM   2572 C CB  . ALA B 1 182 ? 33.054 14.219  50.430  1.000 27.255  ? 178 ALA B CB  1 ? 2 
ATOM   2573 N N   . GLY B 1 183 ? 31.431 15.645  48.160  1.000 26.719  ? 179 GLY B N   1 ? 2 
ATOM   2574 C CA  . GLY B 1 183 ? 31.207 16.591  47.048  1.000 27.102  ? 179 GLY B CA  1 ? 2 
ATOM   2575 C C   . GLY B 1 183 ? 30.081 17.575  47.319  1.000 28.006  ? 179 GLY B C   1 ? 2 
ATOM   2576 O O   . GLY B 1 183 ? 30.284 18.810  47.122  1.000 26.426  ? 179 GLY B O   1 ? 2 
ATOM   2577 N N   . ASP B 1 184 ? 28.926 17.075  47.770  1.000 30.343  ? 180 ASP B N   1 ? 2 
ATOM   2578 C CA  . ASP B 1 184 ? 27.810 17.960  48.172  1.000 31.775  ? 180 ASP B CA  1 ? 2 
ATOM   2579 C C   . ASP B 1 184 ? 28.362 19.022  49.122  1.000 31.575  ? 180 ASP B C   1 ? 2 
ATOM   2580 O O   . ASP B 1 184 ? 28.107 20.188  48.879  1.000 31.929  ? 180 ASP B O   1 ? 2 
ATOM   2581 C CB  . ASP B 1 184 ? 26.643 17.154  48.735  1.000 34.261  ? 180 ASP B CB  1 ? 2 
ATOM   2582 C CG  . ASP B 1 184 ? 25.889 16.327  47.701  1.000 35.722  ? 180 ASP B CG  1 ? 2 
ATOM   2583 O OD1 . ASP B 1 184 ? 26.194 16.475  46.543  1.000 37.419  ? 180 ASP B OD1 1 ? 2 
ATOM   2584 O OD2 . ASP B 1 184 ? 25.030 15.508  48.071  1.000 39.095  ? 180 ASP B OD2 1 ? 2 
ATOM   2585 N N   . GLU B 1 185 ? 29.154 18.660  50.126  1.000 33.277  ? 181 GLU B N   1 ? 2 
ATOM   2586 C CA  . GLU B 1 185 ? 29.526 19.623  51.223  1.000 33.922  ? 181 GLU B CA  1 ? 2 
ATOM   2587 C C   . GLU B 1 185 ? 30.457 20.674  50.580  1.000 31.051  ? 181 GLU B C   1 ? 2 
ATOM   2588 O O   . GLU B 1 185 ? 30.343 21.921  50.876  1.000 28.649  ? 181 GLU B O   1 ? 2 
ATOM   2589 C CB  . GLU B 1 185 ? 30.011 18.882  52.491  1.000 36.055  ? 181 GLU B CB  1 ? 2 
ATOM   2590 C CG  . GLU B 1 185 ? 28.925 18.001  53.176  1.000 39.898  ? 181 GLU B CG  1 ? 2 
ATOM   2591 C CD  . GLU B 1 185 ? 29.235 17.128  54.431  1.000 45.009  ? 181 GLU B CD  1 ? 2 
ATOM   2592 O OE1 . GLU B 1 185 ? 28.536 16.045  54.677  1.000 45.151  ? 181 GLU B OE1 1 ? 2 
ATOM   2593 O OE2 . GLU B 1 185 ? 30.125 17.495  55.234  1.000 48.214  ? 181 GLU B OE2 1 ? 2 
ATOM   2594 N N   . LEU B 1 186 ? 31.297 20.229  49.644  1.000 29.276  ? 182 LEU B N   1 ? 2 
ATOM   2595 C CA  . LEU B 1 186 ? 32.273 21.126  49.002  1.000 28.625  ? 182 LEU B CA  1 ? 2 
ATOM   2596 C C   . LEU B 1 186 ? 31.533 22.111  48.106  1.000 29.067  ? 182 LEU B C   1 ? 2 
ATOM   2597 O O   . LEU B 1 186 ? 31.866 23.274  48.157  1.000 28.004  ? 182 LEU B O   1 ? 2 
ATOM   2598 C CB  . LEU B 1 186 ? 33.255 20.286  48.205  1.000 29.523  ? 182 LEU B CB  1 ? 2 
ATOM   2599 C CG  . LEU B 1 186 ? 34.225 21.085  47.339  1.000 29.948  ? 182 LEU B CG  1 ? 2 
ATOM   2600 C CD1 . LEU B 1 186 ? 35.196 21.908  48.184  1.000 29.838  ? 182 LEU B CD1 1 ? 2 
ATOM   2601 C CD2 . LEU B 1 186 ? 34.989 20.150  46.422  1.000 30.589  ? 182 LEU B CD2 1 ? 2 
ATOM   2602 N N   . PHE B 1 187 ? 30.554 21.686  47.311  1.000 30.100  ? 183 PHE B N   1 ? 2 
ATOM   2603 C CA  . PHE B 1 187 ? 29.847 22.646  46.425  1.000 32.154  ? 183 PHE B CA  1 ? 2 
ATOM   2604 C C   . PHE B 1 187 ? 29.013 23.611  47.266  1.000 32.150  ? 183 PHE B C   1 ? 2 
ATOM   2605 O O   . PHE B 1 187 ? 29.037 24.843  47.008  1.000 31.273  ? 183 PHE B O   1 ? 2 
ATOM   2606 C CB  . PHE B 1 187 ? 29.020 21.939  45.345  1.000 33.393  ? 183 PHE B CB  1 ? 2 
ATOM   2607 C CG  . PHE B 1 187 ? 29.815 21.578  44.124  1.000 32.576  ? 183 PHE B CG  1 ? 2 
ATOM   2608 C CD1 . PHE B 1 187 ? 29.750 22.349  42.964  1.000 33.087  ? 183 PHE B CD1 1 ? 2 
ATOM   2609 C CD2 . PHE B 1 187 ? 30.659 20.477  44.144  1.000 33.297  ? 183 PHE B CD2 1 ? 2 
ATOM   2610 C CE1 . PHE B 1 187 ? 30.508 22.023  41.842  1.000 31.707  ? 183 PHE B CE1 1 ? 2 
ATOM   2611 C CE2 . PHE B 1 187 ? 31.413 20.148  43.021  1.000 34.042  ? 183 PHE B CE2 1 ? 2 
ATOM   2612 C CZ  . PHE B 1 187 ? 31.338 20.930  41.872  1.000 32.179  ? 183 PHE B CZ  1 ? 2 
ATOM   2613 N N   . ASN B 1 188 ? 28.296 23.067  48.241  1.000 35.019  ? 184 ASN B N   1 ? 2 
ATOM   2614 C CA  . ASN B 1 188 ? 27.395 23.867  49.119  1.000 37.947  ? 184 ASN B CA  1 ? 2 
ATOM   2615 C C   . ASN B 1 188 ? 28.230 25.008  49.726  1.000 33.884  ? 184 ASN B C   1 ? 2 
ATOM   2616 O O   . ASN B 1 188 ? 27.779 26.137  49.738  1.000 32.740  ? 184 ASN B O   1 ? 2 
ATOM   2617 C CB  . ASN B 1 188 ? 26.546 23.005  50.093  1.000 43.234  ? 184 ASN B CB  1 ? 2 
ATOM   2618 C CG  . ASN B 1 188 ? 25.357 22.257  49.464  1.000 51.407  ? 184 ASN B CG  1 ? 2 
ATOM   2619 O OD1 . ASN B 1 188 ? 24.774 22.612  48.421  1.000 54.425  ? 184 ASN B OD1 1 ? 2 
ATOM   2620 N ND2 . ASN B 1 188 ? 24.989 21.139  50.070  1.000 59.117  ? 184 ASN B ND2 1 ? 2 
ATOM   2621 N N   . LEU B 1 189 ? 29.457 24.779  50.143  1.000 32.129  ? 185 LEU B N   1 ? 2 
ATOM   2622 C CA  . LEU B 1 189 ? 30.207 25.869  50.808  1.000 31.975  ? 185 LEU B CA  1 ? 2 
ATOM   2623 C C   . LEU B 1 189 ? 30.546 26.956  49.791  1.000 32.410  ? 185 LEU B C   1 ? 2 
ATOM   2624 O O   . LEU B 1 189 ? 30.424 28.141  50.105  1.000 31.754  ? 185 LEU B O   1 ? 2 
ATOM   2625 C CB  . LEU B 1 189 ? 31.463 25.272  51.427  1.000 31.357  ? 185 LEU B CB  1 ? 2 
ATOM   2626 C CG  . LEU B 1 189 ? 32.254 26.213  52.318  1.000 32.785  ? 185 LEU B CG  1 ? 2 
ATOM   2627 C CD1 . LEU B 1 189 ? 31.384 26.808  53.414  1.000 32.118  ? 185 LEU B CD1 1 ? 2 
ATOM   2628 C CD2 . LEU B 1 189 ? 33.467 25.484  52.909  1.000 33.226  ? 185 LEU B CD2 1 ? 2 
ATOM   2629 N N   . ALA B 1 190 ? 30.991 26.568  48.605  1.000 33.553  ? 186 ALA B N   1 ? 2 
ATOM   2630 C CA  . ALA B 1 190 ? 31.344 27.537  47.551  1.000 34.985  ? 186 ALA B CA  1 ? 2 
ATOM   2631 C C   . ALA B 1 190 ? 30.090 28.346  47.220  1.000 34.963  ? 186 ALA B C   1 ? 2 
ATOM   2632 O O   . ALA B 1 190 ? 30.160 29.606  47.131  1.000 32.391  ? 186 ALA B O   1 ? 2 
ATOM   2633 C CB  . ALA B 1 190 ? 31.909 26.827  46.348  1.000 36.119  ? 186 ALA B CB  1 ? 2 
ATOM   2634 N N   . MET B 1 191 ? 28.946 27.683  47.092  1.000 36.123  ? 187 MET B N   1 ? 2 
ATOM   2635 C CA  . MET B 1 191 ? 27.694 28.445  46.793  1.000 38.330  ? 187 MET B CA  1 ? 2 
ATOM   2636 C C   . MET B 1 191 ? 27.451 29.497  47.887  1.000 40.218  ? 187 MET B C   1 ? 2 
ATOM   2637 O O   . MET B 1 191 ? 27.164 30.664  47.534  1.000 39.979  ? 187 MET B O   1 ? 2 
ATOM   2638 C CB  . MET B 1 191 ? 26.472 27.544  46.661  1.000 38.018  ? 187 MET B CB  1 ? 2 
ATOM   2639 C CG  . MET B 1 191 ? 26.583 26.532  45.555  1.000 38.597  ? 187 MET B CG  1 ? 2 
ATOM   2640 S SD  . MET B 1 191 ? 24.951 25.858  45.200  1.000 41.399  ? 187 MET B SD  1 ? 2 
ATOM   2641 C CE  . MET B 1 191 ? 25.417 24.221  44.638  1.000 47.010  ? 187 MET B CE  1 ? 2 
ATOM   2642 N N   . LEU B 1 192 ? 27.585 29.113  49.162  1.000 42.463  ? 188 LEU B N   1 ? 2 
ATOM   2643 C CA  . LEU B 1 192 ? 27.361 30.017  50.310  1.000 44.887  ? 188 LEU B CA  1 ? 2 
ATOM   2644 C C   . LEU B 1 192 ? 28.292 31.213  50.184  1.000 43.110  ? 188 LEU B C   1 ? 2 
ATOM   2645 O O   . LEU B 1 192 ? 27.834 32.310  50.450  1.000 44.915  ? 188 LEU B O   1 ? 2 
ATOM   2646 C CB  . LEU B 1 192 ? 27.589 29.272  51.624  1.000 50.280  ? 188 LEU B CB  1 ? 2 
ATOM   2647 C CG  . LEU B 1 192 ? 27.806 30.159  52.854  1.000 55.523  ? 188 LEU B CG  1 ? 2 
ATOM   2648 C CD1 . LEU B 1 192 ? 26.684 31.211  53.021  1.000 56.056  ? 188 LEU B CD1 1 ? 2 
ATOM   2649 C CD2 . LEU B 1 192 ? 27.996 29.296  54.117  1.000 56.579  ? 188 LEU B CD2 1 ? 2 
ATOM   2650 N N   . PHE B 1 193 ? 29.543 31.014  49.784  1.000 43.202  ? 189 PHE B N   1 ? 2 
ATOM   2651 C CA  . PHE B 1 193 ? 30.518 32.122  49.572  1.000 43.823  ? 189 PHE B CA  1 ? 2 
ATOM   2652 C C   . PHE B 1 193 ? 30.095 33.053  48.424  1.000 46.293  ? 189 PHE B C   1 ? 2 
ATOM   2653 O O   . PHE B 1 193 ? 30.512 34.253  48.437  1.000 46.032  ? 189 PHE B O   1 ? 2 
ATOM   2654 C CB  . PHE B 1 193 ? 31.906 31.591  49.229  1.000 42.496  ? 189 PHE B CB  1 ? 2 
ATOM   2655 C CG  . PHE B 1 193 ? 32.630 30.823  50.304  1.000 41.224  ? 189 PHE B CG  1 ? 2 
ATOM   2656 C CD1 . PHE B 1 193 ? 32.305 30.960  51.646  1.000 40.832  ? 189 PHE B CD1 1 ? 2 
ATOM   2657 C CD2 . PHE B 1 193 ? 33.697 30.008  49.959  1.000 39.909  ? 189 PHE B CD2 1 ? 2 
ATOM   2658 C CE1 . PHE B 1 193 ? 33.016 30.271  52.614  1.000 40.198  ? 189 PHE B CE1 1 ? 2 
ATOM   2659 C CE2 . PHE B 1 193 ? 34.404 29.327  50.925  1.000 39.613  ? 189 PHE B CE2 1 ? 2 
ATOM   2660 C CZ  . PHE B 1 193 ? 34.065 29.463  52.251  1.000 40.516  ? 189 PHE B CZ  1 ? 2 
ATOM   2661 N N   . SER B 1 194 ? 29.328 32.533  47.453  1.000 47.887  ? 190 SER B N   1 ? 2 
ATOM   2662 C CA  . SER B 1 194 ? 28.768 33.324  46.317  1.000 50.140  ? 190 SER B CA  1 ? 2 
ATOM   2663 C C   . SER B 1 194 ? 27.795 34.409  46.839  1.000 52.933  ? 190 SER B C   1 ? 2 
ATOM   2664 O O   . SER B 1 194 ? 27.717 35.497  46.242  1.000 51.795  ? 190 SER B O   1 ? 2 
ATOM   2665 C CB  . SER B 1 194 ? 28.116 32.438  45.268  1.000 46.957  ? 190 SER B CB  1 ? 2 
ATOM   2666 O OG  . SER B 1 194 ? 26.782 32.134  45.628  1.000 45.051  ? 190 SER B OG  1 ? 2 
ATOM   2667 N N   . MET B 1 195 ? 27.109 34.151  47.948  1.000 55.694  ? 191 MET B N   1 ? 2 
ATOM   2668 C CA  . MET B 1 195 ? 26.196 35.112  48.607  1.000 59.976  ? 191 MET B CA  1 ? 2 
ATOM   2669 C C   . MET B 1 195 ? 26.944 36.113  49.527  1.000 66.511  ? 191 MET B C   1 ? 2 
ATOM   2670 O O   . MET B 1 195 ? 26.430 36.368  50.613  1.000 71.244  ? 191 MET B O   1 ? 2 
ATOM   2671 C CB  . MET B 1 195 ? 25.197 34.290  49.422  1.000 62.182  ? 191 MET B CB  1 ? 2 
ATOM   2672 C CG  . MET B 1 195 ? 24.357 33.315  48.600  1.000 63.655  ? 191 MET B CG  1 ? 2 
ATOM   2673 S SD  . MET B 1 195 ? 23.427 32.066  49.585  1.000 70.493  ? 191 MET B SD  1 ? 2 
ATOM   2674 C CE  . MET B 1 195 ? 22.968 32.963  51.068  1.000 71.883  ? 191 MET B CE  1 ? 2 
ATOM   2675 N N   . ASP B 1 196 ? 28.074 36.716  49.119  1.000 76.406  ? 192 ASP B N   1 ? 2 
ATOM   2676 C CA  . ASP B 1 196 ? 29.050 37.403  50.027  1.000 79.023  ? 192 ASP B CA  1 ? 2 
ATOM   2677 C C   . ASP B 1 196 ? 29.423 36.460  51.189  1.000 79.811  ? 192 ASP B C   1 ? 2 
ATOM   2678 O O   . ASP B 1 196 ? 30.563 36.065  51.452  1.000 73.402  ? 192 ASP B O   1 ? 2 
ATOM   2679 C CB  . ASP B 1 196 ? 28.519 38.741  50.565  1.000 80.312  ? 192 ASP B CB  1 ? 2 
ATOM   2680 C CG  . ASP B 1 196 ? 28.565 39.868  49.548  1.000 82.102  ? 192 ASP B CG  1 ? 2 
ATOM   2681 O OD1 . ASP B 1 196 ? 28.304 39.589  48.352  1.000 77.105  ? 192 ASP B OD1 1 ? 2 
ATOM   2682 O OD2 . ASP B 1 196 ? 28.883 41.014  49.957  1.000 78.449  ? 192 ASP B OD2 1 ? 2 
HETATM 2683 K K   . K   C 2 .   ? 43.815 1.999   32.720  1.000 17.837  ? 301 K   A K   1 ? ? 
HETATM 2684 C C1  . GOL D 3 .   ? 48.416 4.786   13.306  1.000 60.925  ? 302 GOL A C1  1 ? ? 
HETATM 2685 O O1  . GOL D 3 .   ? 49.165 4.803   14.523  1.000 52.408  ? 302 GOL A O1  1 ? ? 
HETATM 2686 C C2  . GOL D 3 .   ? 47.457 5.961   13.209  1.000 64.877  ? 302 GOL A C2  1 ? ? 
HETATM 2687 O O2  . GOL D 3 .   ? 47.880 6.968   14.128  1.000 64.106  ? 302 GOL A O2  1 ? ? 
HETATM 2688 C C3  . GOL D 3 .   ? 47.330 6.543   11.804  1.000 73.355  ? 302 GOL A C3  1 ? ? 
HETATM 2689 O O3  . GOL D 3 .   ? 45.981 6.839   11.419  1.000 68.110  ? 302 GOL A O3  1 ? ? 
HETATM 2690 K K   . K   E 2 .   ? 43.424 22.328  37.245  1.000 19.843  ? 301 K   B K   1 ? ? 
HETATM 2691 C C1  . GOL F 3 .   ? 42.698 17.259  57.664  1.000 65.871  ? 302 GOL B C1  1 ? ? 
HETATM 2692 O O1  . GOL F 3 .   ? 42.241 17.173  59.019  1.000 50.763  ? 302 GOL B O1  1 ? ? 
HETATM 2693 C C2  . GOL F 3 .   ? 44.139 17.719  57.469  1.000 65.157  ? 302 GOL B C2  1 ? ? 
HETATM 2694 O O2  . GOL F 3 .   ? 44.587 17.302  56.177  1.000 63.134  ? 302 GOL B O2  1 ? ? 
HETATM 2695 C C3  . GOL F 3 .   ? 44.371 19.217  57.577  1.000 67.622  ? 302 GOL B C3  1 ? ? 
HETATM 2696 O O3  . GOL F 3 .   ? 45.147 19.715  56.485  1.000 62.593  ? 302 GOL B O3  1 ? ? 
HETATM 2697 O O   . HOH G 4 .   ? 35.715 14.142  -10.412 1.000 35.399  ? 401 HOH A O   1 ? ? 
HETATM 2698 O O   . HOH G 4 .   ? 41.518 26.544  -3.143  1.000 50.783  ? 402 HOH A O   1 ? ? 
HETATM 2699 O O   . HOH G 4 .   ? 26.216 7.857   27.775  1.000 43.602  ? 403 HOH A O   1 ? ? 
HETATM 2700 O O   . HOH G 4 .   ? 33.849 25.694  -6.446  1.000 64.232  ? 404 HOH A O   1 ? ? 
HETATM 2701 O O   . HOH G 4 .   ? 27.588 11.134  23.802  1.000 32.280  ? 405 HOH A O   1 ? ? 
HETATM 2702 O O   . HOH G 4 .   ? 38.299 20.883  26.877  1.000 37.300  ? 406 HOH A O   1 ? ? 
HETATM 2703 O O   . HOH G 4 .   ? 33.818 -1.447  32.073  1.000 39.583  ? 407 HOH A O   1 ? ? 
HETATM 2704 O O   . HOH G 4 .   ? 26.521 2.960   21.245  1.000 42.623  ? 408 HOH A O   1 ? ? 
HETATM 2705 O O   . HOH G 4 .   ? 33.874 21.793  -13.542 1.000 30.724  ? 409 HOH A O   1 ? ? 
HETATM 2706 O O   . HOH G 4 .   ? 36.805 6.256   17.286  1.000 26.617  ? 410 HOH A O   1 ? ? 
HETATM 2707 O O   . HOH G 4 .   ? 50.001 12.899  8.165   1.000 37.253  ? 411 HOH A O   1 ? ? 
HETATM 2708 O O   . HOH G 4 .   ? 36.612 -9.369  30.023  1.000 36.491  ? 412 HOH A O   1 ? ? 
HETATM 2709 O O   . HOH G 4 .   ? 46.568 13.442  20.943  1.000 29.279  ? 413 HOH A O   1 ? ? 
HETATM 2710 O O   . HOH G 4 .   ? 50.986 11.480  10.338  1.000 41.476  ? 414 HOH A O   1 ? ? 
HETATM 2711 O O   . HOH G 4 .   ? 46.603 14.762  18.429  1.000 37.413  ? 415 HOH A O   1 ? ? 
HETATM 2712 O O   . HOH G 4 .   ? 35.849 14.118  13.563  1.000 25.048  ? 416 HOH A O   1 ? ? 
HETATM 2713 O O   . HOH G 4 .   ? 32.708 17.130  31.981  1.000 41.978  ? 417 HOH A O   1 ? ? 
HETATM 2714 O O   . HOH G 4 .   ? 46.903 19.558  5.630   1.000 50.749  ? 418 HOH A O   1 ? ? 
HETATM 2715 O O   . HOH G 4 .   ? 46.699 -1.870  34.276  1.000 36.362  ? 419 HOH A O   1 ? ? 
HETATM 2716 O O   . HOH G 4 .   ? 35.478 9.755   14.516  1.000 28.153  ? 420 HOH A O   1 ? ? 
HETATM 2717 O O   . HOH G 4 .   ? 33.143 18.798  17.194  1.000 47.435  ? 421 HOH A O   1 ? ? 
HETATM 2718 O O   . HOH G 4 .   ? 34.457 17.615  19.757  1.000 27.106  ? 422 HOH A O   1 ? ? 
HETATM 2719 O O   . HOH G 4 .   ? 44.502 16.186  29.972  1.000 37.837  ? 423 HOH A O   1 ? ? 
HETATM 2720 O O   . HOH G 4 .   ? 38.911 16.766  11.308  1.000 32.476  ? 424 HOH A O   1 ? ? 
HETATM 2721 O O   . HOH G 4 .   ? 43.735 17.686  -6.433  1.000 39.515  ? 425 HOH A O   1 ? ? 
HETATM 2722 O O   . HOH G 4 .   ? 39.863 20.919  29.616  1.000 47.869  ? 426 HOH A O   1 ? ? 
HETATM 2723 O O   . HOH G 4 .   ? 34.433 24.698  -8.585  1.000 50.867  ? 427 HOH A O   1 ? ? 
HETATM 2724 O O   . HOH G 4 .   ? 49.974 1.080   22.494  1.000 36.080  ? 428 HOH A O   1 ? ? 
HETATM 2725 O O   . HOH G 4 .   ? 42.700 7.201   8.580   1.000 45.916  ? 429 HOH A O   1 ? ? 
HETATM 2726 O O   . HOH G 4 .   ? 30.297 9.558   22.983  1.000 28.980  ? 430 HOH A O   1 ? ? 
HETATM 2727 O O   . HOH G 4 .   ? 47.479 -2.520  20.804  1.000 34.120  ? 431 HOH A O   1 ? ? 
HETATM 2728 O O   . HOH G 4 .   ? 49.508 12.681  33.418  1.000 39.550  ? 432 HOH A O   1 ? ? 
HETATM 2729 O O   . HOH G 4 .   ? 49.133 -1.359  22.317  1.000 39.613  ? 433 HOH A O   1 ? ? 
HETATM 2730 O O   . HOH G 4 .   ? 28.629 -0.349  15.403  1.000 43.407  ? 434 HOH A O   1 ? ? 
HETATM 2731 O O   . HOH G 4 .   ? 33.739 -12.773 21.314  1.000 42.669  ? 435 HOH A O   1 ? ? 
HETATM 2732 O O   . HOH G 4 .   ? 31.004 15.330  24.392  1.000 36.539  ? 436 HOH A O   1 ? ? 
HETATM 2733 O O   . HOH G 4 .   ? 40.895 -2.139  34.454  1.000 38.131  ? 437 HOH A O   1 ? ? 
HETATM 2734 O O   . HOH G 4 .   ? 40.838 26.566  34.728  1.000 38.507  ? 438 HOH A O   1 ? ? 
HETATM 2735 O O   . HOH G 4 .   ? 41.249 18.435  11.478  1.000 41.236  ? 439 HOH A O   1 ? ? 
HETATM 2736 O O   . HOH H 4 .   ? 25.475 16.233  39.191  1.000 48.385  ? 401 HOH B O   1 ? ? 
HETATM 2737 O O   . HOH H 4 .   ? 26.659 2.370   81.080  1.000 41.842  ? 402 HOH B O   1 ? ? 
HETATM 2738 O O   . HOH H 4 .   ? 35.148 -2.408  72.308  1.000 55.926  ? 403 HOH B O   1 ? ? 
HETATM 2739 O O   . HOH H 4 .   ? 34.303 18.162  51.362  1.000 33.766  ? 404 HOH B O   1 ? ? 
HETATM 2740 O O   . HOH H 4 .   ? 49.734 16.291  41.663  1.000 29.019  ? 405 HOH B O   1 ? ? 
HETATM 2741 O O   . HOH H 4 .   ? 38.222 5.050   79.030  1.000 57.667  ? 406 HOH B O   1 ? ? 
HETATM 2742 O O   . HOH H 4 .   ? 23.493 19.972  74.510  1.000 46.560  ? 407 HOH B O   1 ? ? 
HETATM 2743 O O   . HOH H 4 .   ? 36.937 3.126   42.216  1.000 32.470  ? 408 HOH B O   1 ? ? 
HETATM 2744 O O   . HOH H 4 .   ? 40.209 19.378  57.683  1.000 42.893  ? 409 HOH B O   1 ? ? 
HETATM 2745 O O   . HOH H 4 .   ? 38.954 14.068  61.575  1.000 28.101  ? 410 HOH B O   1 ? ? 
HETATM 2746 O O   . HOH H 4 .   ? 37.862 10.080  74.931  1.000 28.181  ? 411 HOH B O   1 ? ? 
HETATM 2747 O O   . HOH H 4 .   ? 43.715 8.225   40.506  1.000 29.695  ? 412 HOH B O   1 ? ? 
HETATM 2748 O O   . HOH H 4 .   ? 25.746 12.925  43.411  1.000 26.669  ? 413 HOH B O   1 ? ? 
HETATM 2749 O O   . HOH H 4 .   ? 32.459 7.300   36.152  1.000 43.032  ? 414 HOH B O   1 ? ? 
HETATM 2750 O O   . HOH H 4 .   ? 30.399 11.283  42.082  1.000 33.100  ? 415 HOH B O   1 ? ? 
HETATM 2751 O O   . HOH H 4 .   ? 43.648 9.279   51.805  1.000 32.643  ? 416 HOH B O   1 ? ? 
HETATM 2752 O O   . HOH H 4 .   ? 46.990 12.569  60.863  1.000 56.853  ? 417 HOH B O   1 ? ? 
HETATM 2753 O O   . HOH H 4 .   ? 52.413 22.715  33.433  0.500 64.373  ? 418 HOH B O   1 ? ? 
HETATM 2754 O O   . HOH H 4 .   ? 35.575 33.509  38.789  1.000 39.390  ? 419 HOH B O   1 ? ? 
HETATM 2755 O O   . HOH H 4 .   ? 27.758 15.557  57.801  1.000 53.821  ? 420 HOH B O   1 ? ? 
HETATM 2756 O O   . HOH H 4 .   ? 41.356 -0.126  42.371  1.000 53.429  ? 421 HOH B O   1 ? ? 
HETATM 2757 O O   . HOH H 4 .   ? 32.168 6.746   48.623  1.000 29.028  ? 422 HOH B O   1 ? ? 
HETATM 2758 O O   . HOH H 4 .   ? 45.751 11.251  62.762  1.000 34.933  ? 423 HOH B O   1 ? ? 
HETATM 2759 O O   . HOH H 4 .   ? 32.575 10.380  54.834  1.000 28.454  ? 424 HOH B O   1 ? ? 
HETATM 2760 O O   . HOH H 4 .   ? 33.424 25.156  36.705  1.000 38.068  ? 425 HOH B O   1 ? ? 
HETATM 2761 O O   . HOH H 4 .   ? 44.893 26.733  49.507  1.000 33.568  ? 426 HOH B O   1 ? ? 
HETATM 2762 O O   . HOH H 4 .   ? 47.630 23.194  48.328  1.000 34.272  ? 427 HOH B O   1 ? ? 
HETATM 2763 O O   . HOH H 4 .   ? 30.117 5.348   51.108  1.000 43.637  ? 428 HOH B O   1 ? ? 
HETATM 2764 O O   . HOH H 4 .   ? 35.306 7.452   57.482  1.000 25.280  ? 429 HOH B O   1 ? ? 
HETATM 2765 O O   . HOH H 4 .   ? 28.492 14.797  44.777  1.000 36.215  ? 430 HOH B O   1 ? ? 
HETATM 2766 O O   . HOH H 4 .   ? 25.425 20.864  46.027  1.000 46.348  ? 431 HOH B O   1 ? ? 
HETATM 2767 O O   . HOH H 4 .   ? 38.940 2.781   39.927  1.000 44.334  ? 432 HOH B O   1 ? ? 
HETATM 2768 O O   . HOH H 4 .   ? 27.628 -0.665  75.600  1.000 47.948  ? 433 HOH B O   1 ? ? 
HETATM 2769 O O   . HOH H 4 .   ? 48.791 11.626  37.887  1.000 46.972  ? 434 HOH B O   1 ? ? 
HETATM 2770 O O   . HOH H 4 .   ? 31.669 36.948  47.020  1.000 37.443  ? 435 HOH B O   1 ? ? 
HETATM 2771 O O   . HOH H 4 .   ? 39.837 16.676  62.120  1.000 37.304  ? 436 HOH B O   1 ? ? 
HETATM 2772 O O   . HOH H 4 .   ? 55.157 17.903  51.201  1.000 37.519  ? 437 HOH B O   1 ? ? 
HETATM 2773 O O   . HOH H 4 .   ? 29.685 9.264   43.777  1.000 28.933  ? 438 HOH B O   1 ? ? 
HETATM 2774 O O   . HOH H 4 .   ? 37.398 5.956   57.909  1.000 37.902  ? 439 HOH B O   1 ? ? 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ASP A 31  ? 1.207 1.559 1.079 -0.045 -0.018 -0.013 27  ASP A N   
2    C CA  . ASP A 31  ? 1.239 1.607 1.115 -0.028 -0.017 -0.005 27  ASP A CA  
3    C C   . ASP A 31  ? 1.326 1.700 1.211 -0.025 -0.017 -0.003 27  ASP A C   
4    O O   . ASP A 31  ? 1.332 1.697 1.221 -0.014 -0.014 0.001  27  ASP A O   
5    C CB  . ASP A 31  ? 1.171 1.552 1.041 -0.026 -0.020 -0.003 27  ASP A CB  
6    N N   . HIS A 32  ? 1.461 1.853 1.350 -0.035 -0.020 -0.005 28  HIS A N   
7    C CA  . HIS A 32  ? 1.493 1.900 1.390 -0.033 -0.020 -0.002 28  HIS A CA  
8    C C   . HIS A 32  ? 1.467 1.870 1.366 -0.047 -0.021 -0.007 28  HIS A C   
9    O O   . HIS A 32  ? 1.310 1.723 1.216 -0.045 -0.021 -0.005 28  HIS A O   
10   C CB  . HIS A 32  ? 1.454 1.895 1.354 -0.027 -0.023 0.004  28  HIS A CB  
11   C CG  . HIS A 32  ? 1.406 1.856 1.314 -0.015 -0.021 0.010  28  HIS A CG  
12   N ND1 . HIS A 32  ? 1.375 1.858 1.287 -0.011 -0.023 0.015  28  HIS A ND1 
13   C CD2 . HIS A 32  ? 1.357 1.788 1.267 -0.005 -0.017 0.011  28  HIS A CD2 
14   C CE1 . HIS A 32  ? 1.348 1.830 1.265 0.000  -0.020 0.019  28  HIS A CE1 
15   N NE2 . HIS A 32  ? 1.349 1.798 1.264 0.004  -0.016 0.017  28  HIS A NE2 
16   N N   . ALA A 33  ? 1.445 1.831 1.337 -0.059 -0.021 -0.014 29  ALA A N   
17   C CA  . ALA A 33  ? 1.349 1.719 1.239 -0.070 -0.020 -0.019 29  ALA A CA  
18   C C   . ALA A 33  ? 1.350 1.693 1.243 -0.063 -0.016 -0.019 29  ALA A C   
19   O O   . ALA A 33  ? 1.279 1.608 1.172 -0.069 -0.014 -0.023 29  ALA A O   
20   C CB  . ALA A 33  ? 1.274 1.634 1.153 -0.084 -0.020 -0.025 29  ALA A CB  
21   N N   . ASP A 34  ? 1.354 1.690 1.249 -0.051 -0.014 -0.016 30  ASP A N   
22   C CA  . ASP A 34  ? 1.291 1.604 1.189 -0.042 -0.010 -0.015 30  ASP A CA  
23   C C   . ASP A 34  ? 1.274 1.595 1.180 -0.035 -0.010 -0.011 30  ASP A C   
24   O O   . ASP A 34  ? 1.295 1.601 1.203 -0.037 -0.008 -0.013 30  ASP A O   
25   C CB  . ASP A 34  ? 1.237 1.542 1.131 -0.032 -0.009 -0.012 30  ASP A CB  
26   C CG  . ASP A 34  ? 1.133 1.428 1.020 -0.037 -0.008 -0.015 30  ASP A CG  
27   O OD1 . ASP A 34  ? 1.067 1.352 0.949 -0.048 -0.008 -0.020 30  ASP A OD1 
28   O OD2 . ASP A 34  ? 1.054 1.348 0.937 -0.030 -0.008 -0.013 30  ASP A OD2 
29   N N   . ALA A 35  ? 1.261 1.602 1.170 -0.026 -0.011 -0.006 31  ALA A N   
30   C CA  . ALA A 35  ? 1.306 1.655 1.221 -0.018 -0.009 -0.001 31  ALA A CA  
31   C C   . ALA A 35  ? 1.309 1.664 1.228 -0.028 -0.011 -0.004 31  ALA A C   
32   O O   . ALA A 35  ? 1.251 1.605 1.175 -0.023 -0.009 -0.002 31  ALA A O   
33   C CB  . ALA A 35  ? 1.301 1.674 1.216 -0.009 -0.010 0.005  31  ALA A CB  
34   N N   . ALA A 36  ? 1.330 1.688 1.246 -0.042 -0.013 -0.009 32  ALA A N   
35   C CA  . ALA A 36  ? 1.248 1.609 1.165 -0.053 -0.014 -0.013 32  ALA A CA  
36   C C   . ALA A 36  ? 1.259 1.591 1.174 -0.057 -0.011 -0.017 32  ALA A C   
37   O O   . ALA A 36  ? 1.335 1.664 1.255 -0.057 -0.010 -0.017 32  ALA A O   
38   C CB  . ALA A 36  ? 1.252 1.627 1.164 -0.066 -0.017 -0.016 32  ALA A CB  
39   N N   . TYR A 37  ? 1.232 1.544 1.141 -0.060 -0.010 -0.021 33  TYR A N   
40   C CA  . TYR A 37  ? 1.132 1.417 1.038 -0.063 -0.007 -0.024 33  TYR A CA  
41   C C   . TYR A 37  ? 1.067 1.341 0.980 -0.053 -0.005 -0.021 33  TYR A C   
42   O O   . TYR A 37  ? 0.958 1.215 0.871 -0.055 -0.003 -0.024 33  TYR A O   
43   C CB  . TYR A 37  ? 1.096 1.363 0.995 -0.064 -0.005 -0.027 33  TYR A CB  
44   C CG  . TYR A 37  ? 1.141 1.383 1.036 -0.067 -0.002 -0.030 33  TYR A CG  
45   C CD1 . TYR A 37  ? 1.137 1.371 1.026 -0.078 -0.001 -0.034 33  TYR A CD1 
46   C CD2 . TYR A 37  ? 1.177 1.403 1.075 -0.058 0.000  -0.028 33  TYR A CD2 
47   C CE1 . TYR A 37  ? 1.164 1.375 1.050 -0.079 0.002  -0.037 33  TYR A CE1 
48   C CE2 . TYR A 37  ? 1.185 1.390 1.081 -0.060 0.003  -0.031 33  TYR A CE2 
49   C CZ  . TYR A 37  ? 1.205 1.402 1.094 -0.070 0.004  -0.035 33  TYR A CZ  
50   O OH  . TYR A 37  ? 1.142 1.320 1.029 -0.070 0.007  -0.036 33  TYR A OH  
51   N N   . VAL A 38  ? 1.028 1.310 0.945 -0.042 -0.005 -0.017 34  VAL A N   
52   C CA  . VAL A 38  ? 1.031 1.302 0.951 -0.032 -0.003 -0.013 34  VAL A CA  
53   C C   . VAL A 38  ? 1.108 1.389 1.034 -0.031 -0.003 -0.012 34  VAL A C   
54   O O   . VAL A 38  ? 1.179 1.445 1.106 -0.029 -0.001 -0.012 34  VAL A O   
55   C CB  . VAL A 38  ? 0.983 1.257 0.902 -0.021 -0.002 -0.009 34  VAL A CB  
56   C CG1 . VAL A 38  ? 0.961 1.235 0.883 -0.011 0.000  -0.004 34  VAL A CG1 
57   C CG2 . VAL A 38  ? 0.966 1.222 0.881 -0.021 -0.000 -0.011 34  VAL A CG2 
58   N N   . GLU A 39  ? 1.160 1.464 1.088 -0.032 -0.005 -0.010 35  GLU A N   
59   C CA  . GLU A 39  ? 1.188 1.504 1.121 -0.032 -0.005 -0.008 35  GLU A CA  
60   C C   . GLU A 39  ? 1.119 1.427 1.052 -0.043 -0.005 -0.013 35  GLU A C   
61   O O   . GLU A 39  ? 1.109 1.407 1.044 -0.043 -0.003 -0.014 35  GLU A O   
62   C CB  . GLU A 39  ? 1.238 1.584 1.174 -0.030 -0.007 -0.004 35  GLU A CB  
63   C CG  . GLU A 39  ? 1.234 1.590 1.171 -0.016 -0.006 0.002  35  GLU A CG  
64   C CD  . GLU A 39  ? 1.229 1.616 1.167 -0.015 -0.008 0.006  35  GLU A CD  
65   O OE1 . GLU A 39  ? 1.211 1.616 1.153 -0.021 -0.009 0.006  35  GLU A OE1 
66   O OE2 . GLU A 39  ? 1.158 1.554 1.094 -0.010 -0.009 0.008  35  GLU A OE2 
67   N N   . LYS A 40  ? 1.063 1.373 0.991 -0.054 -0.006 -0.017 36  LYS A N   
68   C CA  . LYS A 40  ? 1.073 1.375 0.997 -0.067 -0.006 -0.023 36  LYS A CA  
69   C C   . LYS A 40  ? 1.063 1.338 0.986 -0.066 -0.003 -0.025 36  LYS A C   
70   O O   . LYS A 40  ? 1.040 1.306 0.959 -0.075 -0.002 -0.029 36  LYS A O   
71   C CB  . LYS A 40  ? 1.148 1.451 1.065 -0.077 -0.007 -0.026 36  LYS A CB  
72   C CG  . LYS A 40  ? 1.202 1.524 1.116 -0.089 -0.009 -0.028 36  LYS A CG  
73   C CD  . LYS A 40  ? 1.240 1.571 1.147 -0.096 -0.011 -0.030 36  LYS A CD  
74   C CE  . LYS A 40  ? 1.267 1.595 1.165 -0.113 -0.011 -0.036 36  LYS A CE  
75   N NZ  . LYS A 40  ? 1.281 1.636 1.177 -0.121 -0.015 -0.036 36  LYS A NZ  
76   N N   . HIS A 41  ? 1.101 1.362 1.025 -0.057 -0.002 -0.023 37  HIS A N   
77   C CA  . HIS A 41  ? 1.087 1.324 1.010 -0.056 0.001  -0.025 37  HIS A CA  
78   C C   . HIS A 41  ? 1.026 1.256 0.953 -0.046 0.002  -0.022 37  HIS A C   
79   O O   . HIS A 41  ? 0.999 1.211 0.926 -0.044 0.003  -0.023 37  HIS A O   
80   C CB  . HIS A 41  ? 1.140 1.364 1.058 -0.057 0.002  -0.027 37  HIS A CB  
81   C CG  . HIS A 41  ? 1.185 1.403 1.094 -0.067 0.002  -0.031 37  HIS A CG  
82   N ND1 . HIS A 41  ? 1.196 1.395 1.100 -0.070 0.005  -0.034 37  HIS A ND1 
83   C CD2 . HIS A 41  ? 1.201 1.431 1.105 -0.075 0.000  -0.033 37  HIS A CD2 
84   C CE1 . HIS A 41  ? 1.236 1.432 1.131 -0.080 0.005  -0.038 37  HIS A CE1 
85   N NE2 . HIS A 41  ? 1.227 1.442 1.122 -0.084 0.002  -0.037 37  HIS A NE2 
86   N N   . ASN A 42  ? 1.005 1.249 0.937 -0.039 0.001  -0.018 38  ASN A N   
87   C CA  . ASN A 42  ? 0.986 1.223 0.921 -0.030 0.002  -0.015 38  ASN A CA  
88   C C   . ASN A 42  ? 0.936 1.159 0.869 -0.024 0.004  -0.014 38  ASN A C   
89   O O   . ASN A 42  ? 0.882 1.092 0.816 -0.021 0.005  -0.013 38  ASN A O   
90   C CB  . ASN A 42  ? 0.998 1.224 0.934 -0.033 0.003  -0.017 38  ASN A CB  
91   C CG  . ASN A 42  ? 0.971 1.211 0.910 -0.033 0.003  -0.015 38  ASN A CG  
92   O OD1 . ASN A 42  ? 0.907 1.154 0.846 -0.041 0.002  -0.017 38  ASN A OD1 
93   N ND2 . ASN A 42  ? 0.937 1.181 0.877 -0.024 0.004  -0.011 38  ASN A ND2 
94   N N   . LEU A 43  ? 0.853 1.081 0.783 -0.024 0.003  -0.013 39  LEU A N   
95   C CA  . LEU A 43  ? 0.753 0.970 0.681 -0.018 0.004  -0.012 39  LEU A CA  
96   C C   . LEU A 43  ? 0.711 0.937 0.638 -0.009 0.005  -0.007 39  LEU A C   
97   O O   . LEU A 43  ? 0.696 0.913 0.620 -0.004 0.007  -0.006 39  LEU A O   
98   C CB  . LEU A 43  ? 0.721 0.934 0.645 -0.024 0.004  -0.015 39  LEU A CB  
99   C CG  . LEU A 43  ? 0.718 0.918 0.642 -0.031 0.005  -0.019 39  LEU A CG  
100  C CD1 . LEU A 43  ? 0.719 0.920 0.638 -0.038 0.004  -0.022 39  LEU A CD1 
101  C CD2 . LEU A 43  ? 0.721 0.905 0.646 -0.027 0.007  -0.018 39  LEU A CD2 
102  N N   . GLN A 44  ? 0.726 0.968 0.655 -0.007 0.004  -0.005 40  GLN A N   
103  C CA  . GLN A 44  ? 0.830 1.081 0.756 0.003  0.005  0.000  40  GLN A CA  
104  C C   . GLN A 44  ? 0.752 0.985 0.676 0.011  0.009  0.003  40  GLN A C   
105  O O   . GLN A 44  ? 0.745 0.976 0.664 0.019  0.011  0.006  40  GLN A O   
106  C CB  . GLN A 44  ? 0.936 1.210 0.866 0.004  0.004  0.003  40  GLN A CB  
107  C CG  . GLN A 44  ? 1.013 1.301 0.941 0.015  0.005  0.009  40  GLN A CG  
108  C CD  . GLN A 44  ? 1.077 1.360 0.999 0.021  0.006  0.010  40  GLN A CD  
109  O OE1 . GLN A 44  ? 1.053 1.342 0.975 0.016  0.004  0.008  40  GLN A OE1 
110  N NE2 . GLN A 44  ? 1.069 1.341 0.987 0.031  0.010  0.014  40  GLN A NE2 
111  N N   . CYS A 45  ? 0.773 0.994 0.698 0.008  0.009  0.000  41  CYS A N   
112  C CA  . CYS A 45  ? 0.784 0.988 0.706 0.013  0.012  0.002  41  CYS A CA  
113  C C   . CYS A 45  ? 0.691 0.880 0.610 0.014  0.013  0.002  41  CYS A C   
114  O O   . CYS A 45  ? 0.605 0.786 0.518 0.021  0.016  0.005  41  CYS A O   
115  C CB  . CYS A 45  ? 0.835 1.030 0.760 0.009  0.012  -0.000 41  CYS A CB  
116  S SG  . CYS A 45  ? 0.977 1.152 0.896 0.015  0.015  0.002  41  CYS A SG  
117  N N   . LEU A 46  ? 0.630 0.814 0.551 0.006  0.012  -0.002 42  LEU A N   
118  C CA  . LEU A 46  ? 0.625 0.797 0.544 0.006  0.013  -0.003 42  LEU A CA  
119  C C   . LEU A 46  ? 0.657 0.835 0.572 0.012  0.014  -0.000 42  LEU A C   
120  O O   . LEU A 46  ? 0.638 0.803 0.547 0.017  0.017  0.002  42  LEU A O   
121  C CB  . LEU A 46  ? 0.595 0.766 0.517 -0.002 0.011  -0.007 42  LEU A CB  
122  C CG  . LEU A 46  ? 0.563 0.724 0.484 -0.003 0.012  -0.008 42  LEU A CG  
123  C CD1 . LEU A 46  ? 0.542 0.689 0.462 -0.001 0.014  -0.006 42  LEU A CD1 
124  C CD2 . LEU A 46  ? 0.527 0.685 0.450 -0.010 0.011  -0.011 42  LEU A CD2 
125  N N   . PHE A 47  ? 0.633 0.828 0.549 0.011  0.012  0.000  43  PHE A N   
126  C CA  . PHE A 47  ? 0.589 0.791 0.500 0.017  0.013  0.003  43  PHE A CA  
127  C C   . PHE A 47  ? 0.563 0.762 0.468 0.027  0.016  0.008  43  PHE A C   
128  O O   . PHE A 47  ? 0.534 0.726 0.433 0.033  0.018  0.010  43  PHE A O   
129  C CB  . PHE A 47  ? 0.577 0.798 0.490 0.013  0.010  0.002  43  PHE A CB  
130  C CG  . PHE A 47  ? 0.594 0.811 0.507 0.005  0.008  -0.002 43  PHE A CG  
131  C CD1 . PHE A 47  ? 0.626 0.846 0.535 0.007  0.008  -0.001 43  PHE A CD1 
132  C CD2 . PHE A 47  ? 0.623 0.832 0.539 -0.003 0.008  -0.006 43  PHE A CD2 
133  C CE1 . PHE A 47  ? 0.652 0.867 0.560 0.001  0.008  -0.005 43  PHE A CE1 
134  C CE2 . PHE A 47  ? 0.637 0.841 0.551 -0.009 0.007  -0.009 43  PHE A CE2 
135  C CZ  . PHE A 47  ? 0.655 0.861 0.566 -0.007 0.007  -0.009 43  PHE A CZ  
136  N N   . SER A 48  ? 0.580 0.783 0.486 0.030  0.016  0.009  44  SER A N   
137  C CA  . SER A 48  ? 0.604 0.805 0.504 0.040  0.020  0.014  44  SER A CA  
138  C C   . SER A 48  ? 0.581 0.758 0.476 0.042  0.023  0.014  44  SER A C   
139  O O   . SER A 48  ? 0.582 0.751 0.467 0.050  0.027  0.018  44  SER A O   
140  C CB  . SER A 48  ? 0.634 0.846 0.538 0.042  0.019  0.016  44  SER A CB  
141  O OG  . SER A 48  ? 0.690 0.911 0.588 0.053  0.022  0.022  44  SER A OG  
142  N N   . GLU A 49  ? 0.565 0.729 0.462 0.034  0.022  0.010  45  GLU A N   
143  C CA  . GLU A 49  ? 0.584 0.727 0.475 0.034  0.025  0.010  45  GLU A CA  
144  C C   . GLU A 49  ? 0.561 0.697 0.448 0.035  0.027  0.011  45  GLU A C   
145  O O   . GLU A 49  ? 0.542 0.662 0.420 0.039  0.031  0.012  45  GLU A O   
146  C CB  . GLU A 49  ? 0.617 0.750 0.513 0.026  0.024  0.007  45  GLU A CB  
147  C CG  . GLU A 49  ? 0.635 0.778 0.538 0.023  0.021  0.005  45  GLU A CG  
148  C CD  . GLU A 49  ? 0.654 0.785 0.559 0.017  0.020  0.002  45  GLU A CD  
149  O OE1 . GLU A 49  ? 0.628 0.763 0.540 0.011  0.018  -0.001 45  GLU A OE1 
150  O OE2 . GLU A 49  ? 0.669 0.785 0.567 0.019  0.023  0.004  45  GLU A OE2 
151  N N   . MET A 50  ? 0.547 0.693 0.439 0.031  0.024  0.009  46  MET A N   
152  C CA  . MET A 50  ? 0.538 0.679 0.426 0.032  0.026  0.009  46  MET A CA  
153  C C   . MET A 50  ? 0.554 0.697 0.434 0.042  0.029  0.014  46  MET A C   
154  O O   . MET A 50  ? 0.541 0.668 0.411 0.046  0.033  0.016  46  MET A O   
155  C CB  . MET A 50  ? 0.497 0.647 0.391 0.026  0.022  0.006  46  MET A CB  
156  C CG  . MET A 50  ? 0.469 0.613 0.370 0.018  0.021  0.002  46  MET A CG  
157  S SD  . MET A 50  ? 0.463 0.611 0.367 0.012  0.019  -0.001 46  MET A SD  
158  C CE  . MET A 50  ? 0.444 0.612 0.352 0.009  0.015  -0.002 46  MET A CE  
159  N N   . ALA A 51  ? 0.564 0.725 0.445 0.047  0.027  0.016  47  ALA A N   
160  C CA  . ALA A 51  ? 0.613 0.778 0.485 0.058  0.030  0.021  47  ALA A CA  
161  C C   . ALA A 51  ? 0.653 0.799 0.515 0.064  0.036  0.024  47  ALA A C   
162  O O   . ALA A 51  ? 0.648 0.781 0.499 0.071  0.040  0.027  47  ALA A O   
163  C CB  . ALA A 51  ? 0.598 0.787 0.474 0.061  0.028  0.023  47  ALA A CB  
164  N N   . GLU A 52  ? 0.714 0.856 0.579 0.062  0.035  0.023  48  GLU A N   
165  C CA  . GLU A 52  ? 0.776 0.899 0.630 0.067  0.040  0.025  48  GLU A CA  
166  C C   . GLU A 52  ? 0.715 0.815 0.561 0.065  0.044  0.024  48  GLU A C   
167  O O   . GLU A 52  ? 0.724 0.810 0.556 0.072  0.049  0.028  48  GLU A O   
168  C CB  . GLU A 52  ? 0.862 0.983 0.720 0.063  0.039  0.023  48  GLU A CB  
169  C CG  . GLU A 52  ? 0.963 1.067 0.809 0.070  0.044  0.026  48  GLU A CG  
170  C CD  . GLU A 52  ? 1.081 1.177 0.929 0.064  0.043  0.024  48  GLU A CD  
171  O OE1 . GLU A 52  ? 1.194 1.304 1.054 0.058  0.038  0.021  48  GLU A OE1 
172  O OE2 . GLU A 52  ? 1.093 1.167 0.930 0.064  0.047  0.024  48  GLU A OE2 
173  N N   . GLN A 53  ? 0.688 0.786 0.542 0.054  0.041  0.020  49  GLN A N   
174  C CA  . GLN A 53  ? 0.695 0.773 0.543 0.049  0.043  0.018  49  GLN A CA  
175  C C   . GLN A 53  ? 0.676 0.750 0.516 0.055  0.047  0.021  49  GLN A C   
176  O O   . GLN A 53  ? 0.632 0.685 0.460 0.055  0.052  0.022  49  GLN A O   
177  C CB  . GLN A 53  ? 0.692 0.774 0.553 0.038  0.039  0.013  49  GLN A CB  
178  C CG  . GLN A 53  ? 0.714 0.782 0.572 0.032  0.041  0.012  49  GLN A CG  
179  C CD  . GLN A 53  ? 0.757 0.807 0.607 0.029  0.044  0.012  49  GLN A CD  
180  O OE1 . GLN A 53  ? 0.783 0.830 0.631 0.031  0.044  0.012  49  GLN A OE1 
181  N NE2 . GLN A 53  ? 0.786 0.823 0.632 0.024  0.046  0.011  49  GLN A NE2 
182  N N   . LEU A 54  ? 0.660 0.751 0.503 0.060  0.045  0.023  50  LEU A N   
183  C CA  . LEU A 54  ? 0.717 0.805 0.551 0.067  0.048  0.025  50  LEU A CA  
184  C C   . LEU A 54  ? 0.801 0.881 0.620 0.079  0.054  0.031  50  LEU A C   
185  O O   . LEU A 54  ? 0.823 0.887 0.630 0.083  0.060  0.033  50  LEU A O   
186  C CB  . LEU A 54  ? 0.661 0.770 0.503 0.066  0.044  0.025  50  LEU A CB  
187  C CG  . LEU A 54  ? 0.617 0.730 0.470 0.055  0.040  0.020  50  LEU A CG  
188  C CD1 . LEU A 54  ? 0.576 0.710 0.436 0.055  0.036  0.019  50  LEU A CD1 
189  C CD2 . LEU A 54  ? 0.605 0.701 0.455 0.051  0.043  0.019  50  LEU A CD2 
190  N N   . SER A 55  ? 0.861 0.948 0.679 0.085  0.054  0.033  51  SER A N   
191  C CA  . SER A 55  ? 0.896 0.973 0.699 0.097  0.061  0.039  51  SER A CA  
192  C C   . SER A 55  ? 0.903 0.949 0.692 0.096  0.067  0.038  51  SER A C   
193  O O   . SER A 55  ? 0.916 0.948 0.689 0.105  0.073  0.042  51  SER A O   
194  C CB  . SER A 55  ? 0.920 1.013 0.728 0.103  0.059  0.041  51  SER A CB  
195  O OG  . SER A 55  ? 0.977 1.098 0.796 0.103  0.054  0.041  51  SER A OG  
196  N N   . GLU A 56  ? 0.943 0.981 0.738 0.084  0.064  0.034  52  GLU A N   
197  C CA  . GLU A 56  ? 1.041 1.052 0.823 0.081  0.069  0.033  52  GLU A CA  
198  C C   . GLU A 56  ? 1.037 1.030 0.810 0.077  0.073  0.032  52  GLU A C   
199  O O   . GLU A 56  ? 1.113 1.082 0.870 0.078  0.079  0.033  52  GLU A O   
200  C CB  . GLU A 56  ? 1.071 1.080 0.862 0.070  0.065  0.029  52  GLU A CB  
201  C CG  . GLU A 56  ? 1.145 1.159 0.934 0.076  0.065  0.031  52  GLU A CG  
202  C CD  . GLU A 56  ? 1.180 1.198 0.980 0.067  0.061  0.027  52  GLU A CD  
203  O OE1 . GLU A 56  ? 1.209 1.217 1.012 0.056  0.059  0.023  52  GLU A OE1 
204  O OE2 . GLU A 56  ? 1.119 1.152 0.926 0.071  0.058  0.028  52  GLU A OE2 
205  N N   . LYS A 57  ? 0.989 0.995 0.773 0.073  0.069  0.030  53  LYS A N   
206  C CA  . LYS A 57  ? 0.947 0.939 0.726 0.067  0.072  0.029  53  LYS A CA  
207  C C   . LYS A 57  ? 0.924 0.917 0.695 0.077  0.075  0.033  53  LYS A C   
208  O O   . LYS A 57  ? 0.928 0.903 0.688 0.076  0.080  0.033  53  LYS A O   
209  C CB  . LYS A 57  ? 0.944 0.947 0.740 0.055  0.066  0.024  53  LYS A CB  
210  C CG  . LYS A 57  ? 0.960 0.962 0.765 0.045  0.062  0.021  53  LYS A CG  
211  C CD  . LYS A 57  ? 0.982 0.972 0.786 0.034  0.063  0.018  53  LYS A CD  
212  C CE  . LYS A 57  ? 1.015 1.002 0.824 0.026  0.060  0.015  53  LYS A CE  
213  N NZ  . LYS A 57  ? 1.075 1.044 0.875 0.017  0.064  0.014  53  LYS A NZ  
214  N N   . ASP A 58  ? 0.916 0.930 0.692 0.085  0.073  0.035  54  ASP A N   
215  C CA  . ASP A 58  ? 0.982 1.003 0.752 0.097  0.075  0.040  54  ASP A CA  
216  C C   . ASP A 58  ? 0.964 0.981 0.734 0.093  0.076  0.039  54  ASP A C   
217  O O   . ASP A 58  ? 0.963 0.961 0.717 0.098  0.082  0.041  54  ASP A O   
218  C CB  . ASP A 58  ? 1.039 1.047 0.790 0.110  0.083  0.046  54  ASP A CB  
219  C CG  . ASP A 58  ? 1.071 1.091 0.817 0.124  0.084  0.051  54  ASP A CG  
220  O OD1 . ASP A 58  ? 1.090 1.137 0.849 0.124  0.078  0.050  54  ASP A OD1 
221  O OD2 . ASP A 58  ? 1.153 1.154 0.880 0.133  0.092  0.055  54  ASP A OD2 
222  N N   . PRO A 59  ? 0.859 0.892 0.644 0.086  0.070  0.035  55  PRO A N   
223  C CA  . PRO A 59  ? 0.821 0.851 0.607 0.081  0.070  0.034  55  PRO A CA  
224  C C   . PRO A 59  ? 0.772 0.807 0.550 0.092  0.072  0.038  55  PRO A C   
225  O O   . PRO A 59  ? 0.730 0.782 0.510 0.100  0.070  0.040  55  PRO A O   
226  C CB  . PRO A 59  ? 0.798 0.846 0.602 0.072  0.063  0.029  55  PRO A CB  
227  C CG  . PRO A 59  ? 0.784 0.853 0.596 0.076  0.058  0.030  55  PRO A CG  
228  C CD  . PRO A 59  ? 0.806 0.863 0.607 0.082  0.062  0.033  55  PRO A CD  
229  N N   . LYS A 60  ? 0.808 0.829 0.578 0.091  0.077  0.038  56  LYS A N   
230  C CA  . LYS A 60  ? 0.834 0.855 0.594 0.102  0.080  0.042  56  LYS A CA  
231  C C   . LYS A 60  ? 0.751 0.794 0.522 0.100  0.074  0.041  56  LYS A C   
232  O O   . LYS A 60  ? 0.794 0.846 0.559 0.110  0.075  0.044  56  LYS A O   
233  C CB  . LYS A 60  ? 0.933 0.928 0.679 0.100  0.087  0.043  56  LYS A CB  
234  C CG  . LYS A 60  ? 0.993 0.963 0.724 0.102  0.094  0.044  56  LYS A CG  
235  C CD  . LYS A 60  ? 1.063 1.011 0.788 0.091  0.098  0.041  56  LYS A CD  
236  C CE  . LYS A 60  ? 1.137 1.056 0.839 0.095  0.107  0.044  56  LYS A CE  
237  N NZ  . LYS A 60  ? 1.172 1.068 0.867 0.084  0.112  0.042  56  LYS A NZ  
238  N N   . THR A 61  ? 0.661 0.713 0.447 0.089  0.068  0.036  57  THR A N   
239  C CA  . THR A 61  ? 0.593 0.664 0.389 0.085  0.063  0.034  57  THR A CA  
240  C C   . THR A 61  ? 0.570 0.656 0.381 0.077  0.056  0.030  57  THR A C   
241  O O   . THR A 61  ? 0.558 0.640 0.375 0.072  0.056  0.028  57  THR A O   
242  C CB  . THR A 61  ? 0.584 0.644 0.380 0.079  0.065  0.032  57  THR A CB  
243  O OG1 . THR A 61  ? 0.533 0.592 0.340 0.068  0.062  0.027  57  THR A OG1 
244  C CG2 . THR A 61  ? 0.610 0.646 0.392 0.082  0.073  0.034  57  THR A CG2 
245  N N   . GLU A 62  ? 0.518 0.622 0.337 0.074  0.051  0.028  58  GLU A N   
246  C CA  A GLU A 62  ? 0.492 0.608 0.323 0.065  0.046  0.023  58  GLU A CA  
247  C CA  B GLU A 62  ? 0.499 0.615 0.330 0.065  0.046  0.023  58  GLU A CA  
248  C C   . GLU A 62  ? 0.510 0.613 0.347 0.056  0.046  0.020  58  GLU A C   
249  O O   . GLU A 62  ? 0.494 0.599 0.340 0.049  0.043  0.017  58  GLU A O   
250  C CB  A GLU A 62  ? 0.466 0.600 0.302 0.063  0.041  0.022  58  GLU A CB  
251  C CB  B GLU A 62  ? 0.484 0.618 0.318 0.064  0.041  0.022  58  GLU A CB  
252  C CG  A GLU A 62  ? 0.440 0.586 0.287 0.055  0.035  0.018  58  GLU A CG  
253  C CG  B GLU A 62  ? 0.483 0.634 0.314 0.072  0.039  0.026  58  GLU A CG  
254  C CD  A GLU A 62  ? 0.423 0.568 0.277 0.045  0.033  0.013  58  GLU A CD  
255  C CD  B GLU A 62  ? 0.486 0.639 0.307 0.082  0.042  0.030  58  GLU A CD  
256  O OE1 A GLU A 62  ? 0.398 0.557 0.254 0.042  0.029  0.012  58  GLU A OE1 
257  O OE1 B GLU A 62  ? 0.468 0.603 0.280 0.087  0.048  0.032  58  GLU A OE1 
258  O OE2 A GLU A 62  ? 0.405 0.537 0.262 0.040  0.035  0.012  58  GLU A OE2 
259  O OE2 B GLU A 62  ? 0.487 0.661 0.308 0.085  0.038  0.032  58  GLU A OE2 
260  N N   . GLN A 63  ? 0.506 0.596 0.339 0.055  0.050  0.020  59  GLN A N   
261  C CA  . GLN A 63  ? 0.493 0.574 0.332 0.046  0.051  0.017  59  GLN A CA  
262  C C   . GLN A 63  ? 0.497 0.567 0.336 0.043  0.052  0.017  59  GLN A C   
263  O O   . GLN A 63  ? 0.462 0.534 0.311 0.036  0.050  0.014  59  GLN A O   
264  C CB  . GLN A 63  ? 0.491 0.561 0.326 0.045  0.055  0.018  59  GLN A CB  
265  C CG  . GLN A 63  ? 0.481 0.560 0.320 0.042  0.052  0.016  59  GLN A CG  
266  C CD  . GLN A 63  ? 0.479 0.568 0.329 0.036  0.048  0.012  59  GLN A CD  
267  O OE1 . GLN A 63  ? 0.487 0.589 0.340 0.036  0.043  0.011  59  GLN A OE1 
268  N NE2 . GLN A 63  ? 0.451 0.534 0.308 0.029  0.048  0.011  59  GLN A NE2 
269  N N   . GLU A 64  ? 0.510 0.570 0.339 0.049  0.057  0.020  60  GLU A N   
270  C CA  . GLU A 64  ? 0.548 0.596 0.373 0.047  0.059  0.020  60  GLU A CA  
271  C C   . GLU A 64  ? 0.523 0.583 0.357 0.046  0.054  0.019  60  GLU A C   
272  O O   . GLU A 64  ? 0.519 0.576 0.360 0.038  0.052  0.016  60  GLU A O   
273  C CB  . GLU A 64  ? 0.607 0.640 0.416 0.056  0.065  0.024  60  GLU A CB  
274  C CG  . GLU A 64  ? 0.667 0.684 0.466 0.056  0.071  0.026  60  GLU A CG  
275  C CD  . GLU A 64  ? 0.730 0.727 0.511 0.063  0.078  0.029  60  GLU A CD  
276  O OE1 . GLU A 64  ? 0.763 0.755 0.538 0.066  0.079  0.030  60  GLU A OE1 
277  O OE2 . GLU A 64  ? 0.742 0.728 0.513 0.065  0.083  0.031  60  GLU A OE2 
278  N N   . ALA A 65  ? 0.506 0.580 0.341 0.052  0.051  0.020  61  ALA A N   
279  C CA  . ALA A 65  ? 0.469 0.557 0.313 0.050  0.046  0.019  61  ALA A CA  
280  C C   . ALA A 65  ? 0.476 0.569 0.332 0.040  0.042  0.014  61  ALA A C   
281  O O   . ALA A 65  ? 0.531 0.623 0.392 0.035  0.041  0.012  61  ALA A O   
282  C CB  . ALA A 65  ? 0.459 0.565 0.303 0.056  0.044  0.020  61  ALA A CB  
283  N N   . GLU A 66  ? 0.469 0.567 0.329 0.037  0.041  0.013  62  GLU A N   
284  C CA  . GLU A 66  ? 0.444 0.548 0.314 0.028  0.037  0.009  62  GLU A CA  
285  C C   . GLU A 66  ? 0.442 0.533 0.315 0.022  0.039  0.008  62  GLU A C   
286  O O   . GLU A 66  ? 0.430 0.524 0.311 0.017  0.037  0.005  62  GLU A O   
287  C CB  . GLU A 66  ? 0.437 0.546 0.308 0.027  0.037  0.008  62  GLU A CB  
288  C CG  . GLU A 66  ? 0.426 0.536 0.304 0.020  0.035  0.004  62  GLU A CG  
289  C CD  . GLU A 66  ? 0.421 0.536 0.298 0.019  0.034  0.003  62  GLU A CD  
290  O OE1 . GLU A 66  ? 0.430 0.549 0.300 0.024  0.034  0.005  62  GLU A OE1 
291  O OE2 . GLU A 66  ? 0.406 0.519 0.287 0.014  0.034  0.001  62  GLU A OE2 
292  N N   . ARG A 67  ? 0.476 0.555 0.343 0.023  0.043  0.009  63  ARG A N   
293  C CA  . ARG A 67  ? 0.512 0.580 0.380 0.017  0.045  0.009  63  ARG A CA  
294  C C   . ARG A 67  ? 0.486 0.553 0.355 0.016  0.044  0.008  63  ARG A C   
295  O O   . ARG A 67  ? 0.468 0.537 0.345 0.010  0.042  0.006  63  ARG A O   
296  C CB  . ARG A 67  ? 0.566 0.621 0.425 0.019  0.051  0.011  63  ARG A CB  
297  C CG  . ARG A 67  ? 0.620 0.664 0.479 0.012  0.053  0.010  63  ARG A CG  
298  C CD  . ARG A 67  ? 0.715 0.745 0.562 0.014  0.059  0.013  63  ARG A CD  
299  N NE  . ARG A 67  ? 0.771 0.803 0.615 0.019  0.060  0.014  63  ARG A NE  
300  C CZ  . ARG A 67  ? 0.788 0.812 0.621 0.025  0.065  0.016  63  ARG A CZ  
301  N NH1 . ARG A 67  ? 0.810 0.819 0.630 0.028  0.069  0.018  63  ARG A NH1 
302  N NH2 . ARG A 67  ? 0.809 0.836 0.640 0.028  0.066  0.017  63  ARG A NH2 
303  N N   . ILE A 68  ? 0.471 0.535 0.332 0.022  0.045  0.010  64  ILE A N   
304  C CA  . ILE A 68  ? 0.478 0.538 0.338 0.022  0.045  0.010  64  ILE A CA  
305  C C   . ILE A 68  ? 0.444 0.518 0.316 0.019  0.040  0.008  64  ILE A C   
306  O O   . ILE A 68  ? 0.430 0.501 0.305 0.014  0.038  0.006  64  ILE A O   
307  C CB  . ILE A 68  ? 0.493 0.550 0.342 0.031  0.047  0.013  64  ILE A CB  
308  C CG1 . ILE A 68  ? 0.513 0.552 0.349 0.035  0.054  0.016  64  ILE A CG1 
309  C CG2 . ILE A 68  ? 0.501 0.558 0.351 0.032  0.046  0.013  64  ILE A CG2 
310  C CD1 . ILE A 68  ? 0.527 0.564 0.351 0.046  0.057  0.020  64  ILE A CD1 
311  N N   . LEU A 69  ? 0.436 0.524 0.313 0.020  0.037  0.007  65  LEU A N   
312  C CA  . LEU A 69  ? 0.430 0.530 0.317 0.016  0.032  0.004  65  LEU A CA  
313  C C   . LEU A 69  ? 0.425 0.522 0.319 0.009  0.031  0.002  65  LEU A C   
314  O O   . LEU A 69  ? 0.409 0.508 0.308 0.005  0.029  0.000  65  LEU A O   
315  C CB  . LEU A 69  ? 0.432 0.545 0.320 0.018  0.030  0.004  65  LEU A CB  
316  C CG  . LEU A 69  ? 0.460 0.582 0.343 0.026  0.030  0.007  65  LEU A CG  
317  C CD1 . LEU A 69  ? 0.461 0.600 0.348 0.025  0.026  0.006  65  LEU A CD1 
318  C CD2 . LEU A 69  ? 0.469 0.586 0.349 0.029  0.031  0.008  65  LEU A CD2 
319  N N   . LEU A 70  ? 0.421 0.514 0.314 0.007  0.033  0.002  66  LEU A N   
320  C CA  . LEU A 70  ? 0.411 0.502 0.311 0.001  0.033  0.000  66  LEU A CA  
321  C C   . LEU A 70  ? 0.422 0.506 0.322 -0.003 0.034  0.001  66  LEU A C   
322  O O   . LEU A 70  ? 0.419 0.506 0.326 -0.007 0.032  -0.001 66  LEU A O   
323  C CB  . LEU A 70  ? 0.408 0.498 0.307 0.001  0.035  0.001  66  LEU A CB  
324  C CG  . LEU A 70  ? 0.403 0.492 0.308 -0.004 0.036  0.000  66  LEU A CG  
325  C CD1 . LEU A 70  ? 0.391 0.487 0.304 -0.007 0.033  -0.002 66  LEU A CD1 
326  C CD2 . LEU A 70  ? 0.410 0.498 0.313 -0.003 0.038  0.001  66  LEU A CD2 
327  N N   . GLU A 71  ? 0.449 0.522 0.341 -0.001 0.036  0.002  67  GLU A N   
328  C CA  . GLU A 71  ? 0.489 0.554 0.379 -0.006 0.037  0.002  67  GLU A CA  
329  C C   . GLU A 71  ? 0.473 0.540 0.365 -0.006 0.034  0.001  67  GLU A C   
330  O O   . GLU A 71  ? 0.410 0.477 0.307 -0.011 0.033  -0.000 67  GLU A O   
331  C CB  . GLU A 71  ? 0.547 0.598 0.425 -0.004 0.042  0.004  67  GLU A CB  
332  C CG  . GLU A 71  ? 0.624 0.669 0.501 -0.009 0.045  0.005  67  GLU A CG  
333  C CD  . GLU A 71  ? 0.694 0.726 0.558 -0.006 0.050  0.007  67  GLU A CD  
334  O OE1 . GLU A 71  ? 0.697 0.721 0.550 0.001  0.052  0.008  67  GLU A OE1 
335  O OE2 . GLU A 71  ? 0.719 0.750 0.584 -0.009 0.052  0.007  67  GLU A OE2 
336  N N   . PHE A 72  ? 0.476 0.547 0.365 0.000  0.034  0.002  68  PHE A N   
337  C CA  . PHE A 72  ? 0.475 0.550 0.367 0.001  0.032  0.001  68  PHE A CA  
338  C C   . PHE A 72  ? 0.462 0.546 0.364 -0.004 0.028  -0.001 68  PHE A C   
339  O O   . PHE A 72  ? 0.487 0.568 0.391 -0.007 0.027  -0.002 68  PHE A O   
340  C CB  . PHE A 72  ? 0.477 0.559 0.365 0.008  0.031  0.003  68  PHE A CB  
341  C CG  . PHE A 72  ? 0.483 0.570 0.373 0.011  0.030  0.003  68  PHE A CG  
342  C CD1 . PHE A 72  ? 0.509 0.585 0.392 0.011  0.031  0.003  68  PHE A CD1 
343  C CD2 . PHE A 72  ? 0.480 0.581 0.375 0.011  0.027  0.002  68  PHE A CD2 
344  C CE1 . PHE A 72  ? 0.471 0.551 0.355 0.013  0.030  0.004  68  PHE A CE1 
345  C CE2 . PHE A 72  ? 0.460 0.566 0.357 0.013  0.025  0.002  68  PHE A CE2 
346  C CZ  . PHE A 72  ? 0.454 0.550 0.345 0.015  0.027  0.003  68  PHE A CZ  
347  N N   . LEU A 73  ? 0.456 0.548 0.363 -0.004 0.026  -0.002 69  LEU A N   
348  C CA  . LEU A 73  ? 0.445 0.544 0.360 -0.008 0.024  -0.005 69  LEU A CA  
349  C C   . LEU A 73  ? 0.439 0.534 0.359 -0.013 0.024  -0.005 69  LEU A C   
350  O O   . LEU A 73  ? 0.456 0.555 0.381 -0.016 0.022  -0.006 69  LEU A O   
351  C CB  . LEU A 73  ? 0.438 0.544 0.355 -0.007 0.023  -0.005 69  LEU A CB  
352  C CG  . LEU A 73  ? 0.447 0.561 0.362 -0.003 0.022  -0.005 69  LEU A CG  
353  C CD1 . LEU A 73  ? 0.465 0.585 0.380 -0.005 0.021  -0.007 69  LEU A CD1 
354  C CD2 . LEU A 73  ? 0.408 0.526 0.324 -0.004 0.020  -0.006 69  LEU A CD2 
355  N N   . THR A 74  ? 0.432 0.522 0.349 -0.014 0.026  -0.004 70  THR A N   
356  C CA  . THR A 74  ? 0.423 0.513 0.345 -0.019 0.027  -0.003 70  THR A CA  
357  C C   . THR A 74  ? 0.433 0.518 0.354 -0.023 0.026  -0.004 70  THR A C   
358  O O   . THR A 74  ? 0.411 0.500 0.338 -0.026 0.024  -0.004 70  THR A O   
359  C CB  . THR A 74  ? 0.408 0.494 0.327 -0.020 0.030  -0.002 70  THR A CB  
360  O OG1 . THR A 74  ? 0.430 0.521 0.351 -0.017 0.030  -0.002 70  THR A OG1 
361  C CG2 . THR A 74  ? 0.396 0.483 0.319 -0.025 0.031  -0.001 70  THR A CG2 
362  N N   . HIS A 75  ? 0.441 0.517 0.353 -0.021 0.027  -0.003 71  HIS A N   
363  C CA  . HIS A 75  ? 0.471 0.539 0.379 -0.024 0.027  -0.003 71  HIS A CA  
364  C C   . HIS A 75  ? 0.472 0.546 0.385 -0.024 0.024  -0.005 71  HIS A C   
365  O O   . HIS A 75  ? 0.505 0.580 0.421 -0.029 0.022  -0.005 71  HIS A O   
366  C CB  . HIS A 75  ? 0.497 0.553 0.392 -0.021 0.030  -0.002 71  HIS A CB  
367  C CG  . HIS A 75  ? 0.556 0.601 0.444 -0.025 0.031  -0.002 71  HIS A CG  
368  N ND1 . HIS A 75  ? 0.598 0.638 0.484 -0.033 0.031  -0.003 71  HIS A ND1 
369  C CD2 . HIS A 75  ? 0.560 0.598 0.440 -0.021 0.032  -0.002 71  HIS A CD2 
370  C CE1 . HIS A 75  ? 0.598 0.627 0.475 -0.034 0.032  -0.003 71  HIS A CE1 
371  N NE2 . HIS A 75  ? 0.575 0.602 0.448 -0.027 0.032  -0.002 71  HIS A NE2 
372  N N   . ARG A 76  ? 0.452 0.531 0.366 -0.019 0.023  -0.005 72  ARG A N   
373  C CA  . ARG A 76  ? 0.422 0.507 0.341 -0.019 0.020  -0.006 72  ARG A CA  
374  C C   . ARG A 76  ? 0.423 0.515 0.350 -0.022 0.018  -0.007 72  ARG A C   
375  O O   . ARG A 76  ? 0.380 0.474 0.310 -0.024 0.016  -0.009 72  ARG A O   
376  C CB  . ARG A 76  ? 0.410 0.502 0.329 -0.014 0.019  -0.007 72  ARG A CB  
377  C CG  . ARG A 76  ? 0.427 0.515 0.338 -0.009 0.021  -0.005 72  ARG A CG  
378  C CD  . ARG A 76  ? 0.417 0.516 0.330 -0.006 0.020  -0.005 72  ARG A CD  
379  N NE  . ARG A 76  ? 0.420 0.521 0.330 -0.002 0.020  -0.004 72  ARG A NE  
380  C CZ  . ARG A 76  ? 0.423 0.533 0.338 -0.002 0.018  -0.005 72  ARG A CZ  
381  N NH1 . ARG A 76  ? 0.397 0.513 0.318 -0.006 0.016  -0.007 72  ARG A NH1 
382  N NH2 . ARG A 76  ? 0.453 0.565 0.365 0.002  0.018  -0.004 72  ARG A NH2 
383  N N   . LYS A 77  ? 0.417 0.513 0.347 -0.023 0.019  -0.007 73  LYS A N   
384  C CA  . LYS A 77  ? 0.436 0.538 0.374 -0.025 0.018  -0.008 73  LYS A CA  
385  C C   . LYS A 77  ? 0.411 0.512 0.350 -0.029 0.017  -0.007 73  LYS A C   
386  O O   . LYS A 77  ? 0.427 0.533 0.372 -0.031 0.016  -0.007 73  LYS A O   
387  C CB  . LYS A 77  ? 0.484 0.589 0.423 -0.024 0.020  -0.007 73  LYS A CB  
388  C CG  . LYS A 77  ? 0.521 0.630 0.466 -0.025 0.020  -0.006 73  LYS A CG  
389  C CD  . LYS A 77  ? 0.574 0.687 0.521 -0.023 0.020  -0.007 73  LYS A CD  
390  C CE  . LYS A 77  ? 0.648 0.764 0.598 -0.022 0.022  -0.006 73  LYS A CE  
391  N NZ  . LYS A 77  ? 0.684 0.805 0.640 -0.024 0.022  -0.004 73  LYS A NZ  
392  N N   . ALA A 78  ? 0.393 0.488 0.328 -0.032 0.019  -0.006 74  ALA A N   
393  C CA  . ALA A 78  ? 0.391 0.486 0.327 -0.037 0.018  -0.005 74  ALA A CA  
394  C C   . ALA A 78  ? 0.386 0.477 0.320 -0.039 0.016  -0.006 74  ALA A C   
395  O O   . ALA A 78  ? 0.396 0.493 0.334 -0.042 0.014  -0.006 74  ALA A O   
396  C CB  . ALA A 78  ? 0.376 0.462 0.305 -0.040 0.021  -0.004 74  ALA A CB  
397  N N   . GLU A 79  ? 0.372 0.455 0.298 -0.036 0.017  -0.007 75  GLU A N   
398  C CA  . GLU A 79  ? 0.385 0.465 0.309 -0.036 0.015  -0.008 75  GLU A CA  
399  C C   . GLU A 79  ? 0.358 0.446 0.289 -0.035 0.012  -0.009 75  GLU A C   
400  O O   . GLU A 79  ? 0.376 0.464 0.308 -0.038 0.011  -0.009 75  GLU A O   
401  C CB  . GLU A 79  ? 0.406 0.478 0.322 -0.031 0.017  -0.008 75  GLU A CB  
402  C CG  . GLU A 79  ? 0.427 0.487 0.332 -0.031 0.020  -0.007 75  GLU A CG  
403  C CD  . GLU A 79  ? 0.468 0.523 0.366 -0.024 0.022  -0.006 75  GLU A CD  
404  O OE1 . GLU A 79  ? 0.510 0.574 0.412 -0.019 0.020  -0.006 75  GLU A OE1 
405  O OE2 . GLU A 79  ? 0.484 0.527 0.370 -0.023 0.025  -0.005 75  GLU A OE2 
406  N N   . ARG A 80  ? 0.348 0.442 0.284 -0.032 0.013  -0.009 76  ARG A N   
407  C CA  . ARG A 80  ? 0.344 0.444 0.285 -0.030 0.011  -0.010 76  ARG A CA  
408  C C   . ARG A 80  ? 0.359 0.466 0.307 -0.033 0.010  -0.009 76  ARG A C   
409  O O   . ARG A 80  ? 0.344 0.453 0.294 -0.033 0.009  -0.010 76  ARG A O   
410  C CB  . ARG A 80  ? 0.330 0.433 0.271 -0.027 0.012  -0.011 76  ARG A CB  
411  C CG  . ARG A 80  ? 0.323 0.429 0.267 -0.026 0.011  -0.012 76  ARG A CG  
412  C CD  . ARG A 80  ? 0.320 0.429 0.263 -0.024 0.012  -0.013 76  ARG A CD  
413  N NE  . ARG A 80  ? 0.323 0.431 0.262 -0.022 0.012  -0.013 76  ARG A NE  
414  C CZ  . ARG A 80  ? 0.332 0.441 0.268 -0.020 0.013  -0.012 76  ARG A CZ  
415  N NH1 . ARG A 80  ? 0.342 0.452 0.281 -0.021 0.014  -0.012 76  ARG A NH1 
416  N NH2 . ARG A 80  ? 0.322 0.432 0.255 -0.018 0.014  -0.011 76  ARG A NH2 
417  N N   . ASP A 81  ? 0.399 0.508 0.348 -0.034 0.011  -0.008 77  ASP A N   
418  C CA  . ASP A 81  ? 0.429 0.546 0.384 -0.036 0.011  -0.006 77  ASP A CA  
419  C C   . ASP A 81  ? 0.426 0.544 0.381 -0.041 0.009  -0.006 77  ASP A C   
420  O O   . ASP A 81  ? 0.395 0.520 0.354 -0.041 0.007  -0.005 77  ASP A O   
421  C CB  . ASP A 81  ? 0.458 0.578 0.414 -0.037 0.013  -0.004 77  ASP A CB  
422  C CG  . ASP A 81  ? 0.499 0.621 0.457 -0.033 0.015  -0.004 77  ASP A CG  
423  O OD1 . ASP A 81  ? 0.528 0.648 0.485 -0.029 0.015  -0.006 77  ASP A OD1 
424  O OD2 . ASP A 81  ? 0.459 0.587 0.421 -0.032 0.017  -0.002 77  ASP A OD2 
425  N N   . ARG A 82  ? 0.399 0.508 0.347 -0.044 0.009  -0.006 78  ARG A N   
426  C CA  . ARG A 82  ? 0.434 0.542 0.380 -0.049 0.007  -0.007 78  ARG A CA  
427  C C   . ARG A 82  ? 0.425 0.530 0.369 -0.047 0.005  -0.008 78  ARG A C   
428  O O   . ARG A 82  ? 0.373 0.484 0.321 -0.049 0.003  -0.008 78  ARG A O   
429  C CB  . ARG A 82  ? 0.476 0.572 0.412 -0.053 0.008  -0.007 78  ARG A CB  
430  C CG  . ARG A 82  ? 0.527 0.617 0.457 -0.058 0.007  -0.008 78  ARG A CG  
431  C CD  . ARG A 82  ? 0.619 0.698 0.539 -0.063 0.009  -0.008 78  ARG A CD  
432  N NE  . ARG A 82  ? 0.719 0.786 0.629 -0.067 0.008  -0.009 78  ARG A NE  
433  C CZ  . ARG A 82  ? 0.781 0.852 0.691 -0.073 0.005  -0.010 78  ARG A CZ  
434  N NH1 . ARG A 82  ? 0.801 0.888 0.721 -0.075 0.002  -0.009 78  ARG A NH1 
435  N NH2 . ARG A 82  ? 0.829 0.887 0.728 -0.077 0.006  -0.011 78  ARG A NH2 
436  N N   . ALA A 83  ? 0.423 0.522 0.364 -0.043 0.006  -0.009 79  ALA A N   
437  C CA  . ALA A 83  ? 0.425 0.523 0.366 -0.040 0.004  -0.010 79  ALA A CA  
438  C C   . ALA A 83  ? 0.416 0.523 0.364 -0.039 0.003  -0.010 79  ALA A C   
439  O O   . ALA A 83  ? 0.400 0.508 0.348 -0.040 0.001  -0.010 79  ALA A O   
440  C CB  . ALA A 83  ? 0.433 0.526 0.370 -0.036 0.006  -0.011 79  ALA A CB  
441  N N   . ALA A 84  ? 0.410 0.523 0.363 -0.036 0.004  -0.009 80  ALA A N   
442  C CA  . ALA A 84  ? 0.399 0.519 0.356 -0.034 0.004  -0.008 80  ALA A CA  
443  C C   . ALA A 84  ? 0.401 0.528 0.362 -0.037 0.003  -0.006 80  ALA A C   
444  O O   . ALA A 84  ? 0.383 0.515 0.347 -0.035 0.002  -0.005 80  ALA A O   
445  C CB  . ALA A 84  ? 0.390 0.512 0.350 -0.031 0.007  -0.007 80  ALA A CB  
446  N N   . LEU A 85  ? 0.399 0.530 0.361 -0.041 0.002  -0.005 81  LEU A N   
447  C CA  . LEU A 85  ? 0.419 0.559 0.384 -0.045 0.000  -0.003 81  LEU A CA  
448  C C   . LEU A 85  ? 0.433 0.569 0.394 -0.048 -0.003 -0.004 81  LEU A C   
449  O O   . LEU A 85  ? 0.444 0.589 0.409 -0.048 -0.005 -0.003 81  LEU A O   
450  C CB  . LEU A 85  ? 0.418 0.561 0.384 -0.051 0.001  -0.002 81  LEU A CB  
451  C CG  . LEU A 85  ? 0.394 0.545 0.365 -0.048 0.003  -0.000 81  LEU A CG  
452  C CD1 . LEU A 85  ? 0.406 0.554 0.375 -0.053 0.005  0.000  81  LEU A CD1 
453  C CD2 . LEU A 85  ? 0.376 0.541 0.354 -0.047 0.002  0.003  81  LEU A CD2 
454  N N   . ARG A 86  ? 0.454 0.578 0.408 -0.050 -0.003 -0.006 82  ARG A N   
455  C CA  . ARG A 86  ? 0.485 0.603 0.433 -0.053 -0.005 -0.008 82  ARG A CA  
456  C C   . ARG A 86  ? 0.453 0.569 0.402 -0.048 -0.005 -0.008 82  ARG A C   
457  O O   . ARG A 86  ? 0.444 0.562 0.392 -0.049 -0.008 -0.008 82  ARG A O   
458  C CB  . ARG A 86  ? 0.571 0.676 0.510 -0.056 -0.003 -0.009 82  ARG A CB  
459  C CG  . ARG A 86  ? 0.672 0.766 0.603 -0.055 -0.004 -0.011 82  ARG A CG  
460  C CD  . ARG A 86  ? 0.772 0.853 0.696 -0.054 -0.001 -0.012 82  ARG A CD  
461  N NE  . ARG A 86  ? 0.870 0.941 0.783 -0.060 -0.001 -0.012 82  ARG A NE  
462  C CZ  . ARG A 86  ? 0.864 0.923 0.768 -0.060 0.002  -0.012 82  ARG A CZ  
463  N NH1 . ARG A 86  ? 0.863 0.920 0.768 -0.054 0.005  -0.012 82  ARG A NH1 
464  N NH2 . ARG A 86  ? 0.848 0.895 0.741 -0.066 0.003  -0.013 82  ARG A NH2 
465  N N   . LEU A 87  ? 0.423 0.538 0.374 -0.042 -0.003 -0.009 83  LEU A N   
466  C CA  . LEU A 87  ? 0.403 0.514 0.352 -0.038 -0.003 -0.010 83  LEU A CA  
467  C C   . LEU A 87  ? 0.431 0.550 0.386 -0.034 -0.002 -0.009 83  LEU A C   
468  O O   . LEU A 87  ? 0.476 0.590 0.429 -0.030 -0.001 -0.010 83  LEU A O   
469  C CB  . LEU A 87  ? 0.366 0.470 0.312 -0.036 -0.001 -0.012 83  LEU A CB  
470  C CG  . LEU A 87  ? 0.357 0.453 0.297 -0.038 -0.001 -0.013 83  LEU A CG  
471  C CD1 . LEU A 87  ? 0.357 0.449 0.295 -0.034 0.001  -0.014 83  LEU A CD1 
472  C CD2 . LEU A 87  ? 0.363 0.453 0.298 -0.040 -0.003 -0.013 83  LEU A CD2 
473  N N   . GLN A 88  ? 0.477 0.605 0.436 -0.034 -0.002 -0.007 84  GLN A N   
474  C CA  . GLN A 88  ? 0.482 0.616 0.444 -0.029 -0.001 -0.004 84  GLN A CA  
475  C C   . GLN A 88  ? 0.451 0.584 0.412 -0.027 -0.002 -0.005 84  GLN A C   
476  O O   . GLN A 88  ? 0.444 0.579 0.404 -0.030 -0.005 -0.004 84  GLN A O   
477  C CB  . GLN A 88  ? 0.552 0.699 0.520 -0.031 -0.002 -0.001 84  GLN A CB  
478  C CG  . GLN A 88  ? 0.641 0.798 0.614 -0.026 0.000  0.002  84  GLN A CG  
479  C CD  . GLN A 88  ? 0.693 0.864 0.672 -0.029 -0.001 0.005  84  GLN A CD  
480  O OE1 . GLN A 88  ? 0.623 0.795 0.602 -0.037 -0.003 0.004  84  GLN A OE1 
481  N NE2 . GLN A 88  ? 0.748 0.929 0.731 -0.024 0.001  0.008  84  GLN A NE2 
482  N N   . PHE A 89  ? 0.399 0.527 0.357 -0.022 0.001  -0.005 85  PHE A N   
483  C CA  . PHE A 89  ? 0.381 0.506 0.337 -0.019 0.000  -0.005 85  PHE A CA  
484  C C   . PHE A 89  ? 0.397 0.524 0.352 -0.013 0.003  -0.003 85  PHE A C   
485  O O   . PHE A 89  ? 0.401 0.525 0.355 -0.010 0.007  -0.003 85  PHE A O   
486  C CB  . PHE A 89  ? 0.371 0.485 0.321 -0.021 0.001  -0.009 85  PHE A CB  
487  C CG  . PHE A 89  ? 0.374 0.481 0.322 -0.019 0.004  -0.010 85  PHE A CG  
488  C CD1 . PHE A 89  ? 0.372 0.479 0.321 -0.021 0.005  -0.011 85  PHE A CD1 
489  C CD2 . PHE A 89  ? 0.379 0.481 0.323 -0.016 0.007  -0.011 85  PHE A CD2 
490  C CE1 . PHE A 89  ? 0.370 0.473 0.317 -0.020 0.007  -0.013 85  PHE A CE1 
491  C CE2 . PHE A 89  ? 0.375 0.471 0.316 -0.016 0.010  -0.013 85  PHE A CE2 
492  C CZ  . PHE A 89  ? 0.371 0.468 0.313 -0.018 0.010  -0.014 85  PHE A CZ  
493  N N   . SER A 90  ? 0.408 0.539 0.362 -0.010 0.003  -0.001 86  SER A N   
494  C CA  . SER A 90  ? 0.427 0.559 0.379 -0.003 0.006  0.002  86  SER A CA  
495  C C   . SER A 90  ? 0.437 0.557 0.382 0.000  0.008  0.000  86  SER A C   
496  O O   . SER A 90  ? 0.492 0.609 0.433 0.007  0.012  0.002  86  SER A O   
497  C CB  . SER A 90  ? 0.438 0.584 0.394 -0.001 0.003  0.006  86  SER A CB  
498  O OG  . SER A 90  ? 0.467 0.625 0.430 -0.006 -0.000 0.007  86  SER A OG  
499  N N   . HIS A 91  ? 0.425 0.537 0.367 -0.004 0.006  -0.003 87  HIS A N   
500  C CA  . HIS A 91  ? 0.410 0.512 0.345 -0.002 0.008  -0.004 87  HIS A CA  
501  C C   . HIS A 91  ? 0.391 0.483 0.323 -0.006 0.009  -0.008 87  HIS A C   
502  O O   . HIS A 91  ? 0.393 0.476 0.320 -0.005 0.013  -0.010 87  HIS A O   
503  C CB  . HIS A 91  ? 0.398 0.503 0.332 -0.001 0.006  -0.003 87  HIS A CB  
504  C CG  . HIS A 91  ? 0.410 0.528 0.348 0.004  0.005  0.002  87  HIS A CG  
505  N ND1 . HIS A 91  ? 0.441 0.558 0.375 0.012  0.009  0.005  87  HIS A ND1 
506  C CD2 . HIS A 91  ? 0.386 0.519 0.331 0.002  0.001  0.004  87  HIS A CD2 
507  C CE1 . HIS A 91  ? 0.416 0.547 0.354 0.015  0.007  0.009  87  HIS A CE1 
508  N NE2 . HIS A 91  ? 0.399 0.541 0.345 0.009  0.002  0.009  87  HIS A NE2 
509  N N   . SER A 92  ? 0.367 0.461 0.302 -0.011 0.006  -0.010 88  SER A N   
510  C CA  . SER A 92  ? 0.349 0.435 0.281 -0.014 0.006  -0.013 88  SER A CA  
511  C C   . SER A 92  ? 0.327 0.416 0.263 -0.018 0.003  -0.014 88  SER A C   
512  O O   . SER A 92  ? 0.316 0.412 0.255 -0.020 0.001  -0.013 88  SER A O   
513  C CB  . SER A 92  ? 0.343 0.426 0.272 -0.013 0.005  -0.013 88  SER A CB  
514  O OG  . SER A 92  ? 0.341 0.426 0.271 -0.016 0.001  -0.013 88  SER A OG  
515  N N   . PHE A 93  ? 0.312 0.397 0.246 -0.020 0.004  -0.016 89  PHE A N   
516  C CA  . PHE A 93  ? 0.304 0.389 0.239 -0.023 0.002  -0.017 89  PHE A CA  
517  C C   . PHE A 93  ? 0.306 0.387 0.238 -0.024 0.003  -0.018 89  PHE A C   
518  O O   . PHE A 93  ? 0.321 0.399 0.251 -0.023 0.005  -0.020 89  PHE A O   
519  C CB  . PHE A 93  ? 0.294 0.384 0.232 -0.024 0.003  -0.017 89  PHE A CB  
520  C CG  . PHE A 93  ? 0.295 0.383 0.232 -0.024 0.005  -0.018 89  PHE A CG  
521  C CD1 . PHE A 93  ? 0.316 0.406 0.254 -0.024 0.007  -0.018 89  PHE A CD1 
522  C CD2 . PHE A 93  ? 0.311 0.397 0.246 -0.025 0.006  -0.020 89  PHE A CD2 
523  C CE1 . PHE A 93  ? 0.308 0.398 0.245 -0.025 0.009  -0.020 89  PHE A CE1 
524  C CE2 . PHE A 93  ? 0.327 0.415 0.262 -0.027 0.007  -0.021 89  PHE A CE2 
525  C CZ  . PHE A 93  ? 0.315 0.404 0.250 -0.027 0.009  -0.021 89  PHE A CZ  
526  N N   . GLU A 94  ? 0.319 0.398 0.249 -0.025 0.002  -0.018 90  GLU A N   
527  C CA  . GLU A 94  ? 0.327 0.403 0.254 -0.025 0.003  -0.019 90  GLU A CA  
528  C C   . GLU A 94  ? 0.301 0.379 0.229 -0.025 0.003  -0.019 90  GLU A C   
529  O O   . GLU A 94  ? 0.314 0.391 0.241 -0.026 0.001  -0.018 90  GLU A O   
530  C CB  . GLU A 94  ? 0.365 0.436 0.288 -0.024 0.002  -0.019 90  GLU A CB  
531  C CG  . GLU A 94  ? 0.408 0.478 0.329 -0.023 0.003  -0.020 90  GLU A CG  
532  C CD  . GLU A 94  ? 0.433 0.496 0.349 -0.022 0.003  -0.020 90  GLU A CD  
533  O OE1 . GLU A 94  ? 0.447 0.507 0.360 -0.021 0.004  -0.019 90  GLU A OE1 
534  O OE2 . GLU A 94  ? 0.498 0.559 0.413 -0.022 0.003  -0.020 90  GLU A OE2 
535  N N   . VAL A 95  ? 0.293 0.374 0.221 -0.025 0.004  -0.020 91  VAL A N   
536  C CA  . VAL A 95  ? 0.289 0.371 0.216 -0.023 0.005  -0.019 91  VAL A CA  
537  C C   . VAL A 95  ? 0.289 0.370 0.213 -0.022 0.006  -0.018 91  VAL A C   
538  O O   . VAL A 95  ? 0.297 0.381 0.222 -0.022 0.007  -0.019 91  VAL A O   
539  C CB  . VAL A 95  ? 0.292 0.381 0.222 -0.024 0.006  -0.019 91  VAL A CB  
540  C CG1 . VAL A 95  ? 0.292 0.384 0.221 -0.022 0.006  -0.018 91  VAL A CG1 
541  C CG2 . VAL A 95  ? 0.292 0.382 0.225 -0.025 0.005  -0.019 91  VAL A CG2 
542  N N   . ASN A 96  ? 0.306 0.382 0.226 -0.020 0.006  -0.017 92  ASN A N   
543  C CA  . ASN A 96  ? 0.326 0.400 0.241 -0.017 0.008  -0.016 92  ASN A CA  
544  C C   . ASN A 96  ? 0.335 0.410 0.247 -0.013 0.009  -0.014 92  ASN A C   
545  O O   . ASN A 96  ? 0.335 0.401 0.241 -0.013 0.009  -0.014 92  ASN A O   
546  C CB  . ASN A 96  ? 0.347 0.412 0.258 -0.017 0.007  -0.016 92  ASN A CB  
547  C CG  . ASN A 96  ? 0.372 0.434 0.278 -0.014 0.009  -0.015 92  ASN A CG  
548  O OD1 . ASN A 96  ? 0.398 0.460 0.300 -0.010 0.011  -0.014 92  ASN A OD1 
549  N ND2 . ASN A 96  ? 0.383 0.442 0.288 -0.015 0.009  -0.016 92  ASN A ND2 
550  N N   . LEU A 97  ? 0.368 0.452 0.282 -0.011 0.011  -0.013 93  LEU A N   
551  C CA  . LEU A 97  ? 0.407 0.492 0.317 -0.006 0.013  -0.011 93  LEU A CA  
552  C C   . LEU A 97  ? 0.433 0.520 0.340 -0.000 0.016  -0.008 93  LEU A C   
553  O O   . LEU A 97  ? 0.393 0.485 0.303 -0.001 0.016  -0.009 93  LEU A O   
554  C CB  . LEU A 97  ? 0.398 0.496 0.315 -0.007 0.013  -0.011 93  LEU A CB  
555  C CG  . LEU A 97  ? 0.422 0.519 0.343 -0.011 0.010  -0.013 93  LEU A CG  
556  C CD1 . LEU A 97  ? 0.430 0.540 0.356 -0.013 0.010  -0.014 93  LEU A CD1 
557  C CD2 . LEU A 97  ? 0.446 0.534 0.363 -0.011 0.010  -0.013 93  LEU A CD2 
558  N N   . ASP A 98  ? 0.548 0.636 0.451 0.005  0.018  -0.005 94  ASP A N   
559  C CA  . ASP A 98  ? 0.609 0.701 0.508 0.013  0.021  -0.002 94  ASP A CA  
560  C C   . ASP A 98  ? 0.689 0.769 0.581 0.013  0.022  -0.002 94  ASP A C   
561  O O   . ASP A 98  ? 0.754 0.839 0.647 0.016  0.024  -0.001 94  ASP A O   
562  C CB  . ASP A 98  ? 0.619 0.731 0.526 0.014  0.022  -0.000 94  ASP A CB  
563  C CG  . ASP A 98  ? 0.724 0.850 0.637 0.011  0.020  -0.001 94  ASP A CG  
564  O OD1 . ASP A 98  ? 0.771 0.892 0.682 0.011  0.020  -0.001 94  ASP A OD1 
565  O OD2 . ASP A 98  ? 0.682 0.826 0.602 0.010  0.020  -0.001 94  ASP A OD2 
566  N N   . ASN A 99  ? 0.777 0.843 0.666 0.009  0.021  -0.004 95  ASN A N   
567  C CA  . ASN A 99  ? 0.875 0.930 0.760 0.005  0.019  -0.006 95  ASN A CA  
568  C C   . ASN A 99  ? 0.840 0.902 0.729 0.006  0.020  -0.006 95  ASN A C   
569  O O   . ASN A 99  ? 0.859 0.921 0.744 0.011  0.023  -0.004 95  ASN A O   
570  C CB  . ASN A 99  ? 0.961 0.998 0.833 0.008  0.021  -0.005 95  ASN A CB  
571  C CG  . ASN A 99  ? 0.982 1.013 0.849 0.007  0.022  -0.005 95  ASN A CG  
572  O OD1 . ASN A 99  ? 1.014 1.035 0.878 0.001  0.020  -0.007 95  ASN A OD1 
573  N ND2 . ASN A 99  ? 0.779 0.817 0.647 0.011  0.024  -0.002 95  ASN A ND2 
574  N N   . GLY A 100 ? 0.793 0.860 0.690 0.000  0.017  -0.009 96  GLY A N   
575  C CA  . GLY A 100 ? 0.767 0.839 0.667 -0.001 0.018  -0.010 96  GLY A CA  
576  C C   . GLY A 100 ? 0.783 0.870 0.691 -0.003 0.018  -0.010 96  GLY A C   
577  O O   . GLY A 100 ? 0.769 0.858 0.681 -0.007 0.017  -0.012 96  GLY A O   
578  N N   . ARG A 101 ? 0.725 0.824 0.636 -0.000 0.019  -0.008 97  ARG A N   
579  C CA  . ARG A 101 ? 0.682 0.798 0.599 -0.002 0.019  -0.008 97  ARG A CA  
580  C C   . ARG A 101 ? 0.614 0.739 0.537 -0.007 0.017  -0.010 97  ARG A C   
581  O O   . ARG A 101 ? 0.697 0.837 0.625 -0.008 0.018  -0.009 97  ARG A O   
582  C CB  . ARG A 101 ? 0.802 0.928 0.718 0.006  0.022  -0.003 97  ARG A CB  
583  C CG  . ARG A 101 ? 0.896 1.013 0.804 0.012  0.025  -0.001 97  ARG A CG  
584  C CD  . ARG A 101 ? 1.023 1.153 0.931 0.020  0.028  0.004  97  ARG A CD  
585  N NE  . ARG A 101 ? 1.111 1.241 1.015 0.025  0.029  0.007  97  ARG A NE  
586  C CZ  . ARG A 101 ? 1.127 1.273 1.037 0.025  0.028  0.008  97  ARG A CZ  
587  N NH1 . ARG A 101 ? 1.097 1.261 1.016 0.020  0.027  0.006  97  ARG A NH1 
588  N NH2 . ARG A 101 ? 1.132 1.275 1.038 0.031  0.030  0.010  97  ARG A NH2 
589  N N   . LYS A 102 ? 0.538 0.653 0.461 -0.010 0.015  -0.012 98  LYS A N   
590  C CA  . LYS A 102 ? 0.490 0.609 0.417 -0.016 0.014  -0.015 98  LYS A CA  
591  C C   . LYS A 102 ? 0.445 0.551 0.370 -0.018 0.012  -0.017 98  LYS A C   
592  O O   . LYS A 102 ? 0.465 0.563 0.388 -0.015 0.011  -0.016 98  LYS A O   
593  C CB  . LYS A 102 ? 0.504 0.630 0.433 -0.015 0.013  -0.014 98  LYS A CB  
594  C CG  . LYS A 102 ? 0.518 0.659 0.452 -0.018 0.013  -0.014 98  LYS A CG  
595  C CD  . LYS A 102 ? 0.541 0.688 0.476 -0.018 0.012  -0.014 98  LYS A CD  
596  C CE  . LYS A 102 ? 0.547 0.699 0.481 -0.011 0.013  -0.010 98  LYS A CE  
597  N NZ  . LYS A 102 ? 0.569 0.726 0.503 -0.011 0.012  -0.010 98  LYS A NZ  
598  N N   . ILE A 103 ? 0.384 0.488 0.311 -0.022 0.012  -0.019 99  ILE A N   
599  C CA  . ILE A 103 ? 0.365 0.459 0.290 -0.023 0.011  -0.020 99  ILE A CA  
600  C C   . ILE A 103 ? 0.333 0.428 0.260 -0.027 0.011  -0.022 99  ILE A C   
601  O O   . ILE A 103 ? 0.319 0.418 0.246 -0.030 0.012  -0.023 99  ILE A O   
602  C CB  . ILE A 103 ? 0.359 0.446 0.281 -0.023 0.011  -0.020 99  ILE A CB  
603  C CG1 . ILE A 103 ? 0.357 0.440 0.275 -0.019 0.011  -0.018 99  ILE A CG1 
604  C CG2 . ILE A 103 ? 0.363 0.442 0.284 -0.023 0.010  -0.021 99  ILE A CG2 
605  C CD1 . ILE A 103 ? 0.353 0.430 0.267 -0.018 0.013  -0.018 99  ILE A CD1 
606  N N   . MET A 104 ? 0.336 0.427 0.264 -0.027 0.010  -0.022 100 MET A N   
607  C CA  . MET A 104 ? 0.359 0.448 0.287 -0.030 0.010  -0.024 100 MET A CA  
608  C C   . MET A 104 ? 0.336 0.418 0.263 -0.028 0.009  -0.023 100 MET A C   
609  O O   . MET A 104 ? 0.309 0.391 0.237 -0.026 0.008  -0.022 100 MET A O   
610  C CB  . MET A 104 ? 0.376 0.470 0.306 -0.030 0.010  -0.024 100 MET A CB  
611  C CG  . MET A 104 ? 0.399 0.491 0.328 -0.032 0.011  -0.025 100 MET A CG  
612  S SD  . MET A 104 ? 0.412 0.510 0.344 -0.033 0.011  -0.025 100 MET A SD  
613  C CE  . MET A 104 ? 0.415 0.522 0.346 -0.036 0.011  -0.026 100 MET A CE  
614  N N   . ARG A 105 ? 0.339 0.416 0.263 -0.028 0.011  -0.024 101 ARG A N   
615  C CA  . ARG A 105 ? 0.355 0.428 0.278 -0.026 0.010  -0.023 101 ARG A CA  
616  C C   . ARG A 105 ? 0.355 0.425 0.276 -0.027 0.013  -0.024 101 ARG A C   
617  O O   . ARG A 105 ? 0.346 0.414 0.263 -0.029 0.015  -0.026 101 ARG A O   
618  C CB  . ARG A 105 ? 0.402 0.468 0.321 -0.025 0.011  -0.023 101 ARG A CB  
619  C CG  . ARG A 105 ? 0.464 0.530 0.383 -0.024 0.009  -0.023 101 ARG A CG  
620  C CD  . ARG A 105 ? 0.515 0.574 0.430 -0.023 0.010  -0.022 101 ARG A CD  
621  N NE  . ARG A 105 ? 0.532 0.589 0.444 -0.022 0.009  -0.022 101 ARG A NE  
622  C CZ  . ARG A 105 ? 0.553 0.611 0.465 -0.023 0.010  -0.023 101 ARG A CZ  
623  N NH1 . ARG A 105 ? 0.584 0.646 0.497 -0.025 0.012  -0.024 101 ARG A NH1 
624  N NH2 . ARG A 105 ? 0.609 0.664 0.518 -0.021 0.010  -0.022 101 ARG A NH2 
625  N N   . LEU A 106 ? 0.366 0.437 0.289 -0.024 0.012  -0.022 102 LEU A N   
626  C CA  . LEU A 106 ? 0.393 0.461 0.313 -0.023 0.015  -0.022 102 LEU A CA  
627  C C   . LEU A 106 ? 0.391 0.457 0.310 -0.019 0.015  -0.020 102 LEU A C   
628  O O   . LEU A 106 ? 0.378 0.450 0.302 -0.018 0.011  -0.018 102 LEU A O   
629  C CB  . LEU A 106 ? 0.409 0.482 0.333 -0.024 0.014  -0.022 102 LEU A CB  
630  C CG  . LEU A 106 ? 0.427 0.497 0.348 -0.022 0.017  -0.021 102 LEU A CG  
631  C CD1 . LEU A 106 ? 0.465 0.531 0.381 -0.025 0.020  -0.024 102 LEU A CD1 
632  C CD2 . LEU A 106 ? 0.432 0.509 0.359 -0.020 0.016  -0.019 102 LEU A CD2 
633  N N   . GLN A 107 ? 0.412 0.472 0.326 -0.016 0.018  -0.020 103 GLN A N   
634  C CA  . GLN A 107 ? 0.452 0.511 0.364 -0.011 0.019  -0.017 103 GLN A CA  
635  C C   . GLN A 107 ? 0.467 0.523 0.376 -0.009 0.023  -0.016 103 GLN A C   
636  O O   . GLN A 107 ? 0.462 0.508 0.364 -0.011 0.027  -0.018 103 GLN A O   
637  C CB  . GLN A 107 ? 0.489 0.540 0.395 -0.008 0.021  -0.017 103 GLN A CB  
638  C CG  . GLN A 107 ? 0.525 0.577 0.432 -0.011 0.018  -0.018 103 GLN A CG  
639  C CD  . GLN A 107 ? 0.561 0.610 0.467 -0.016 0.019  -0.021 103 GLN A CD  
640  O OE1 . GLN A 107 ? 0.584 0.626 0.484 -0.018 0.023  -0.023 103 GLN A OE1 
641  N NE2 . GLN A 107 ? 0.567 0.622 0.479 -0.018 0.015  -0.021 103 GLN A NE2 
642  N N   . LEU A 108 ? 0.491 0.553 0.403 -0.004 0.022  -0.013 104 LEU A N   
643  C CA  . LEU A 108 ? 0.520 0.580 0.429 -0.000 0.026  -0.011 104 LEU A CA  
644  C C   . LEU A 108 ? 0.564 0.614 0.464 0.006  0.031  -0.010 104 LEU A C   
645  O O   . LEU A 108 ? 0.562 0.614 0.462 0.008  0.029  -0.008 104 LEU A O   
646  C CB  . LEU A 108 ? 0.526 0.598 0.443 0.003  0.024  -0.008 104 LEU A CB  
647  C CG  . LEU A 108 ? 0.532 0.612 0.456 -0.003 0.020  -0.009 104 LEU A CG  
648  C CD1 . LEU A 108 ? 0.517 0.610 0.449 -0.000 0.018  -0.006 104 LEU A CD1 
649  C CD2 . LEU A 108 ? 0.528 0.602 0.449 -0.005 0.023  -0.012 104 LEU A CD2 
650  N N   . GLY A 109 ? 0.647 0.685 0.537 0.008  0.037  -0.010 105 GLY A N   
651  C CA  . GLY A 109 ? 0.725 0.754 0.605 0.016  0.043  -0.007 105 GLY A CA  
652  C C   . GLY A 109 ? 0.791 0.817 0.666 0.020  0.047  -0.005 105 GLY A C   
653  O O   . GLY A 109 ? 0.782 0.811 0.661 0.015  0.046  -0.007 105 GLY A O   
654  N N   . GLN A 110 ? 0.874 0.893 0.740 0.029  0.053  -0.001 106 GLN A N   
655  C CA  . GLN A 110 ? 0.948 0.963 0.808 0.035  0.058  0.001  106 GLN A CA  
656  C C   . GLN A 110 ? 0.964 0.966 0.817 0.028  0.061  -0.003 106 GLN A C   
657  O O   . GLN A 110 ? 0.946 0.955 0.804 0.027  0.060  -0.003 106 GLN A O   
658  C CB  . GLN A 110 ? 1.048 1.051 0.895 0.046  0.066  0.006  106 GLN A CB  
659  C CG  . GLN A 110 ? 1.129 1.148 0.983 0.056  0.064  0.012  106 GLN A CG  
660  C CD  . GLN A 110 ? 1.210 1.227 1.062 0.058  0.063  0.012  106 GLN A CD  
661  O OE1 . GLN A 110 ? 1.240 1.256 1.095 0.050  0.059  0.008  106 GLN A OE1 
662  N NE2 . GLN A 110 ? 1.157 1.172 1.001 0.069  0.067  0.018  106 GLN A NE2 
663  N N   . GLU A 111 ? 0.984 0.969 0.824 0.023  0.065  -0.007 107 GLU A N   
664  C CA  . GLU A 111 ? 1.001 0.971 0.830 0.017  0.069  -0.011 107 GLU A CA  
665  C C   . GLU A 111 ? 0.902 0.877 0.737 0.005  0.064  -0.016 107 GLU A C   
666  O O   . GLU A 111 ? 0.897 0.868 0.728 -0.000 0.065  -0.019 107 GLU A O   
667  C CB  . GLU A 111 ? 1.073 1.018 0.880 0.020  0.078  -0.011 107 GLU A CB  
668  C CG  . GLU A 111 ? 1.107 1.042 0.904 0.031  0.085  -0.007 107 GLU A CG  
669  C CD  . GLU A 111 ? 1.211 1.120 0.984 0.034  0.095  -0.007 107 GLU A CD  
670  O OE1 . GLU A 111 ? 1.252 1.151 1.019 0.030  0.096  -0.010 107 GLU A OE1 
671  O OE2 . GLU A 111 ? 1.266 1.162 1.027 0.042  0.102  -0.004 107 GLU A OE2 
672  N N   . THR A 112 ? 0.794 0.777 0.638 0.002  0.059  -0.017 108 THR A N   
673  C CA  . THR A 112 ? 0.694 0.685 0.545 -0.008 0.054  -0.022 108 THR A CA  
674  C C   . THR A 112 ? 0.647 0.654 0.512 -0.008 0.047  -0.020 108 THR A C   
675  O O   . THR A 112 ? 0.711 0.721 0.579 -0.001 0.046  -0.017 108 THR A O   
676  C CB  . THR A 112 ? 0.672 0.649 0.511 -0.015 0.057  -0.025 108 THR A CB  
677  O OG1 . THR A 112 ? 0.651 0.624 0.488 -0.011 0.058  -0.024 108 THR A OG1 
678  C CG2 . THR A 112 ? 0.683 0.641 0.505 -0.018 0.064  -0.027 108 THR A CG2 
679  N N   . SER A 113 ? 0.613 0.630 0.487 -0.014 0.042  -0.023 109 SER A N   
680  C CA  . SER A 113 ? 0.594 0.623 0.479 -0.016 0.036  -0.022 109 SER A CA  
681  C C   . SER A 113 ? 0.572 0.596 0.453 -0.021 0.037  -0.025 109 SER A C   
682  O O   . SER A 113 ? 0.583 0.600 0.457 -0.027 0.039  -0.028 109 SER A O   
683  C CB  . SER A 113 ? 0.580 0.621 0.475 -0.018 0.032  -0.023 109 SER A CB  
684  O OG  . SER A 113 ? 0.575 0.620 0.473 -0.013 0.032  -0.020 109 SER A OG  
685  N N   . THR A 114 ? 0.540 0.567 0.425 -0.020 0.034  -0.025 110 THR A N   
686  C CA  . THR A 114 ? 0.545 0.570 0.428 -0.025 0.034  -0.027 110 THR A CA  
687  C C   . THR A 114 ? 0.496 0.535 0.390 -0.028 0.029  -0.027 110 THR A C   
688  O O   . THR A 114 ? 0.476 0.522 0.377 -0.025 0.025  -0.025 110 THR A O   
689  C CB  . THR A 114 ? 0.563 0.580 0.440 -0.022 0.036  -0.026 110 THR A CB  
690  O OG1 . THR A 114 ? 0.604 0.628 0.488 -0.016 0.032  -0.023 110 THR A OG1 
691  C CG2 . THR A 114 ? 0.574 0.575 0.438 -0.020 0.042  -0.026 110 THR A CG2 
692  N N   . LEU A 115 ? 0.494 0.535 0.388 -0.034 0.028  -0.030 111 LEU A N   
693  C CA  . LEU A 115 ? 0.501 0.554 0.403 -0.036 0.024  -0.030 111 LEU A CA  
694  C C   . LEU A 115 ? 0.480 0.535 0.382 -0.039 0.024  -0.031 111 LEU A C   
695  O O   . LEU A 115 ? 0.481 0.530 0.376 -0.044 0.028  -0.033 111 LEU A O   
696  C CB  . LEU A 115 ? 0.512 0.569 0.414 -0.040 0.025  -0.031 111 LEU A CB  
697  C CG  . LEU A 115 ? 0.535 0.604 0.445 -0.041 0.021  -0.031 111 LEU A CG  
698  C CD1 . LEU A 115 ? 0.575 0.648 0.491 -0.035 0.019  -0.028 111 LEU A CD1 
699  C CD2 . LEU A 115 ? 0.527 0.599 0.435 -0.045 0.022  -0.032 111 LEU A CD2 
700  N N   . GLN A 116 ? 0.488 0.549 0.396 -0.037 0.021  -0.030 112 GLN A N   
701  C CA  . GLN A 116 ? 0.477 0.541 0.385 -0.039 0.021  -0.030 112 GLN A CA  
702  C C   . GLN A 116 ? 0.429 0.505 0.344 -0.039 0.019  -0.029 112 GLN A C   
703  O O   . GLN A 116 ? 0.453 0.532 0.372 -0.036 0.016  -0.028 112 GLN A O   
704  C CB  . GLN A 116 ? 0.499 0.557 0.406 -0.035 0.021  -0.029 112 GLN A CB  
705  C CG  . GLN A 116 ? 0.550 0.597 0.450 -0.034 0.024  -0.029 112 GLN A CG  
706  C CD  . GLN A 116 ? 0.604 0.648 0.504 -0.029 0.023  -0.028 112 GLN A CD  
707  O OE1 . GLN A 116 ? 0.667 0.715 0.571 -0.026 0.020  -0.026 112 GLN A OE1 
708  N NE2 . GLN A 116 ? 0.649 0.686 0.543 -0.030 0.027  -0.028 112 GLN A NE2 
709  N N   . LEU A 117 ? 0.405 0.489 0.321 -0.043 0.019  -0.030 113 LEU A N   
710  C CA  . LEU A 117 ? 0.409 0.505 0.331 -0.042 0.017  -0.028 113 LEU A CA  
711  C C   . LEU A 117 ? 0.419 0.519 0.341 -0.042 0.018  -0.028 113 LEU A C   
712  O O   . LEU A 117 ? 0.423 0.521 0.341 -0.046 0.020  -0.029 113 LEU A O   
713  C CB  . LEU A 117 ? 0.420 0.525 0.342 -0.046 0.017  -0.029 113 LEU A CB  
714  C CG  . LEU A 117 ? 0.445 0.546 0.366 -0.047 0.018  -0.031 113 LEU A CG  
715  C CD1 . LEU A 117 ? 0.475 0.587 0.397 -0.051 0.017  -0.031 113 LEU A CD1 
716  C CD2 . LEU A 117 ? 0.458 0.554 0.381 -0.042 0.016  -0.029 113 LEU A CD2 
717  N N   . GLU A 118 ? 0.440 0.546 0.365 -0.037 0.016  -0.025 114 GLU A N   
718  C CA  . GLU A 118 ? 0.492 0.605 0.418 -0.036 0.017  -0.024 114 GLU A CA  
719  C C   . GLU A 118 ? 0.449 0.573 0.378 -0.032 0.016  -0.021 114 GLU A C   
720  O O   . GLU A 118 ? 0.422 0.543 0.352 -0.029 0.015  -0.021 114 GLU A O   
721  C CB  . GLU A 118 ? 0.560 0.663 0.483 -0.031 0.017  -0.022 114 GLU A CB  
722  C CG  . GLU A 118 ? 0.636 0.729 0.555 -0.033 0.019  -0.024 114 GLU A CG  
723  C CD  . GLU A 118 ? 0.701 0.784 0.617 -0.029 0.018  -0.023 114 GLU A CD  
724  O OE1 . GLU A 118 ? 0.754 0.827 0.666 -0.029 0.018  -0.024 114 GLU A OE1 
725  O OE2 . GLU A 118 ? 0.731 0.816 0.647 -0.025 0.018  -0.021 114 GLU A OE2 
726  N N   . GLN A 119 ? 0.455 0.592 0.386 -0.033 0.018  -0.020 115 GLN A N   
727  C CA  . GLN A 119 ? 0.501 0.650 0.435 -0.028 0.017  -0.017 115 GLN A CA  
728  C C   . GLN A 119 ? 0.514 0.672 0.449 -0.026 0.019  -0.015 115 GLN A C   
729  O O   . GLN A 119 ? 0.547 0.707 0.482 -0.031 0.020  -0.016 115 GLN A O   
730  C CB  . GLN A 119 ? 0.524 0.685 0.461 -0.032 0.016  -0.018 115 GLN A CB  
731  C CG  . GLN A 119 ? 0.545 0.718 0.485 -0.027 0.016  -0.015 115 GLN A CG  
732  C CD  . GLN A 119 ? 0.568 0.743 0.509 -0.030 0.014  -0.016 115 GLN A CD  
733  O OE1 . GLN A 119 ? 0.566 0.732 0.505 -0.035 0.013  -0.019 115 GLN A OE1 
734  N NE2 . GLN A 119 ? 0.606 0.794 0.549 -0.026 0.014  -0.014 115 GLN A NE2 
735  N N   . LYS A 120 ? 0.545 0.703 0.479 -0.018 0.020  -0.011 116 LYS A N   
736  C CA  . LYS A 120 ? 0.577 0.744 0.511 -0.014 0.023  -0.008 116 LYS A CA  
737  C C   . LYS A 120 ? 0.588 0.764 0.522 -0.006 0.023  -0.004 116 LYS A C   
738  O O   . LYS A 120 ? 0.639 0.806 0.568 0.001  0.025  -0.002 116 LYS A O   
739  C CB  . LYS A 120 ? 0.606 0.757 0.535 -0.012 0.024  -0.008 116 LYS A CB  
740  C CG  . LYS A 120 ? 0.665 0.806 0.592 -0.018 0.024  -0.012 116 LYS A CG  
741  C CD  . LYS A 120 ? 0.739 0.861 0.660 -0.015 0.023  -0.012 116 LYS A CD  
742  C CE  . LYS A 120 ? 0.830 0.943 0.749 -0.019 0.024  -0.015 116 LYS A CE  
743  N NZ  . LYS A 120 ? 0.852 0.958 0.771 -0.024 0.023  -0.018 116 LYS A NZ  
744  N N   . GLY A 121 ? 0.634 0.827 0.573 -0.008 0.022  -0.003 117 GLY A N   
745  C CA  . GLY A 121 ? 0.679 0.883 0.617 0.000  0.023  0.002  117 GLY A CA  
746  C C   . GLY A 121 ? 0.721 0.947 0.663 0.002  0.025  0.005  117 GLY A C   
747  O O   . GLY A 121 ? 0.756 0.986 0.701 -0.004 0.026  0.003  117 GLY A O   
748  N N   . ARG A 122 ? 0.807 1.047 0.750 0.010  0.027  0.010  118 ARG A N   
749  C CA  . ARG A 122 ? 0.843 1.108 0.791 0.012  0.029  0.014  118 ARG A CA  
750  C C   . ARG A 122 ? 0.792 1.078 0.747 0.001  0.026  0.012  118 ARG A C   
751  O O   . ARG A 122 ? 0.813 1.116 0.773 -0.003 0.027  0.012  118 ARG A O   
752  C CB  . ARG A 122 ? 0.922 1.195 0.867 0.026  0.031  0.021  118 ARG A CB  
753  C CG  . ARG A 122 ? 1.020 1.313 0.967 0.032  0.035  0.026  118 ARG A CG  
754  C CD  . ARG A 122 ? 1.090 1.407 1.040 0.041  0.036  0.033  118 ARG A CD  
755  N NE  . ARG A 122 ? 1.136 1.449 1.083 0.042  0.034  0.032  118 ARG A NE  
756  C CZ  . ARG A 122 ? 1.110 1.445 1.062 0.044  0.033  0.035  118 ARG A CZ  
757  N NH1 . ARG A 122 ? 1.134 1.500 1.093 0.045  0.033  0.039  118 ARG A NH1 
758  N NH2 . ARG A 122 ? 1.006 1.332 0.955 0.045  0.031  0.033  118 ARG A NH2 
759  N N   . VAL A 123 ? 0.740 1.023 0.696 -0.003 0.023  0.009  119 VAL A N   
760  C CA  . VAL A 123 ? 0.690 0.992 0.650 -0.012 0.020  0.007  119 VAL A CA  
761  C C   . VAL A 123 ? 0.598 0.891 0.559 -0.025 0.019  0.001  119 VAL A C   
762  O O   . VAL A 123 ? 0.609 0.919 0.573 -0.035 0.018  -0.001 119 VAL A O   
763  C CB  . VAL A 123 ? 0.743 1.047 0.703 -0.007 0.019  0.008  119 VAL A CB  
764  C CG1 . VAL A 123 ? 0.781 1.088 0.742 -0.018 0.015  0.004  119 VAL A CG1 
765  C CG2 . VAL A 123 ? 0.726 1.053 0.688 0.002  0.020  0.015  119 VAL A CG2 
766  N N   . LEU A 124 ? 0.541 0.809 0.497 -0.026 0.019  -0.003 120 LEU A N   
767  C CA  . LEU A 124 ? 0.492 0.747 0.445 -0.037 0.019  -0.008 120 LEU A CA  
768  C C   . LEU A 124 ? 0.486 0.720 0.436 -0.035 0.020  -0.010 120 LEU A C   
769  O O   . LEU A 124 ? 0.499 0.717 0.446 -0.028 0.020  -0.009 120 LEU A O   
770  C CB  . LEU A 124 ? 0.471 0.717 0.422 -0.040 0.016  -0.011 120 LEU A CB  
771  C CG  . LEU A 124 ? 0.461 0.688 0.408 -0.048 0.016  -0.016 120 LEU A CG  
772  C CD1 . LEU A 124 ? 0.473 0.706 0.419 -0.058 0.017  -0.019 120 LEU A CD1 
773  C CD2 . LEU A 124 ? 0.447 0.669 0.393 -0.051 0.014  -0.019 120 LEU A CD2 
774  N N   . LYS A 125 ? 0.503 0.734 0.452 -0.042 0.021  -0.012 121 LYS A N   
775  C CA  . LYS A 125 ? 0.505 0.714 0.449 -0.041 0.023  -0.014 121 LYS A CA  
776  C C   . LYS A 125 ? 0.478 0.677 0.419 -0.051 0.022  -0.019 121 LYS A C   
777  O O   . LYS A 125 ? 0.489 0.698 0.430 -0.060 0.023  -0.021 121 LYS A O   
778  C CB  . LYS A 125 ? 0.547 0.762 0.491 -0.040 0.025  -0.012 121 LYS A CB  
779  C CG  . LYS A 125 ? 0.651 0.846 0.591 -0.042 0.027  -0.014 121 LYS A CG  
780  C CD  . LYS A 125 ? 0.738 0.935 0.677 -0.041 0.030  -0.013 121 LYS A CD  
781  C CE  . LYS A 125 ? 0.808 0.982 0.741 -0.040 0.031  -0.015 121 LYS A CE  
782  N NZ  . LYS A 125 ? 0.864 1.036 0.796 -0.032 0.033  -0.011 121 LYS A NZ  
783  N N   . MET A 126 ? 0.459 0.637 0.395 -0.050 0.022  -0.021 122 MET A N   
784  C CA  . MET A 126 ? 0.468 0.635 0.400 -0.058 0.022  -0.025 122 MET A CA  
785  C C   . MET A 126 ? 0.453 0.598 0.380 -0.054 0.023  -0.026 122 MET A C   
786  O O   . MET A 126 ? 0.416 0.556 0.344 -0.047 0.021  -0.025 122 MET A O   
787  C CB  . MET A 126 ? 0.486 0.658 0.418 -0.062 0.021  -0.027 122 MET A CB  
788  C CG  . MET A 126 ? 0.515 0.681 0.448 -0.055 0.019  -0.026 122 MET A CG  
789  S SD  . MET A 126 ? 0.561 0.706 0.489 -0.057 0.019  -0.029 122 MET A SD  
790  C CE  . MET A 126 ? 0.581 0.725 0.512 -0.049 0.016  -0.027 122 MET A CE  
791  N N   . ASP A 127 ? 0.462 0.596 0.383 -0.060 0.024  -0.030 123 ASP A N   
792  C CA  . ASP A 127 ? 0.495 0.610 0.412 -0.058 0.025  -0.031 123 ASP A CA  
793  C C   . ASP A 127 ? 0.496 0.604 0.407 -0.064 0.026  -0.034 123 ASP A C   
794  O O   . ASP A 127 ? 0.496 0.608 0.404 -0.072 0.028  -0.036 123 ASP A O   
795  C CB  . ASP A 127 ? 0.529 0.632 0.440 -0.059 0.028  -0.032 123 ASP A CB  
796  C CG  . ASP A 127 ? 0.619 0.726 0.533 -0.053 0.027  -0.029 123 ASP A CG  
797  O OD1 . ASP A 127 ? 0.717 0.838 0.635 -0.054 0.027  -0.027 123 ASP A OD1 
798  O OD2 . ASP A 127 ? 0.774 0.870 0.687 -0.048 0.026  -0.028 123 ASP A OD2 
799  N N   . GLU A 128 ? 0.470 0.566 0.379 -0.061 0.026  -0.034 124 GLU A N   
800  C CA  . GLU A 128 ? 0.465 0.552 0.366 -0.066 0.028  -0.037 124 GLU A CA  
801  C C   . GLU A 128 ? 0.446 0.518 0.344 -0.060 0.029  -0.036 124 GLU A C   
802  O O   . GLU A 128 ? 0.416 0.489 0.319 -0.053 0.026  -0.034 124 GLU A O   
803  C CB  . GLU A 128 ? 0.479 0.574 0.384 -0.067 0.026  -0.037 124 GLU A CB  
804  C CG  . GLU A 128 ? 0.519 0.630 0.426 -0.073 0.025  -0.038 124 GLU A CG  
805  C CD  . GLU A 128 ? 0.562 0.676 0.468 -0.076 0.025  -0.039 124 GLU A CD  
806  O OE1 . GLU A 128 ? 0.618 0.736 0.529 -0.070 0.022  -0.037 124 GLU A OE1 
807  O OE2 . GLU A 128 ? 0.585 0.698 0.484 -0.084 0.027  -0.041 124 GLU A OE2 
808  N N   . ALA A 129 ? 0.445 0.503 0.333 -0.063 0.032  -0.038 125 ALA A N   
809  C CA  . ALA A 129 ? 0.441 0.486 0.325 -0.057 0.034  -0.037 125 ALA A CA  
810  C C   . ALA A 129 ? 0.436 0.470 0.310 -0.061 0.038  -0.039 125 ALA A C   
811  O O   . ALA A 129 ? 0.434 0.464 0.300 -0.068 0.041  -0.042 125 ALA A O   
812  C CB  . ALA A 129 ? 0.426 0.463 0.307 -0.054 0.035  -0.037 125 ALA A CB  
813  N N   . PHE A 130 ? 0.468 0.497 0.341 -0.056 0.038  -0.039 126 PHE A N   
814  C CA  . PHE A 130 ? 0.487 0.505 0.350 -0.059 0.042  -0.040 126 PHE A CA  
815  C C   . PHE A 130 ? 0.479 0.495 0.343 -0.052 0.041  -0.038 126 PHE A C   
816  O O   . PHE A 130 ? 0.452 0.476 0.326 -0.046 0.037  -0.035 126 PHE A O   
817  C CB  . PHE A 130 ? 0.497 0.523 0.359 -0.068 0.041  -0.043 126 PHE A CB  
818  C CG  . PHE A 130 ? 0.496 0.540 0.371 -0.067 0.036  -0.042 126 PHE A CG  
819  C CD1 . PHE A 130 ? 0.488 0.546 0.372 -0.067 0.032  -0.041 126 PHE A CD1 
820  C CD2 . PHE A 130 ? 0.527 0.571 0.402 -0.065 0.035  -0.041 126 PHE A CD2 
821  C CE1 . PHE A 130 ? 0.492 0.564 0.386 -0.065 0.028  -0.039 126 PHE A CE1 
822  C CE2 . PHE A 130 ? 0.511 0.570 0.397 -0.063 0.031  -0.040 126 PHE A CE2 
823  C CZ  . PHE A 130 ? 0.498 0.571 0.393 -0.063 0.027  -0.039 126 PHE A CZ  
824  N N   . SER A 131 ? 0.513 0.517 0.367 -0.052 0.045  -0.039 127 SER A N   
825  C CA  . SER A 131 ? 0.522 0.522 0.376 -0.045 0.046  -0.036 127 SER A CA  
826  C C   . SER A 131 ? 0.503 0.509 0.359 -0.048 0.045  -0.037 127 SER A C   
827  O O   . SER A 131 ? 0.516 0.523 0.368 -0.056 0.045  -0.040 127 SER A O   
828  C CB  . SER A 131 ? 0.556 0.538 0.396 -0.041 0.052  -0.036 127 SER A CB  
829  O OG  . SER A 131 ? 0.612 0.591 0.453 -0.035 0.052  -0.034 127 SER A OG  
830  N N   . ILE A 132 ? 0.514 0.526 0.377 -0.042 0.043  -0.035 128 ILE A N   
831  C CA  . ILE A 132 ? 0.532 0.547 0.395 -0.044 0.042  -0.035 128 ILE A CA  
832  C C   . ILE A 132 ? 0.565 0.573 0.424 -0.037 0.046  -0.033 128 ILE A C   
833  O O   . ILE A 132 ? 0.579 0.583 0.438 -0.030 0.047  -0.030 128 ILE A O   
834  C CB  . ILE A 132 ? 0.514 0.547 0.391 -0.045 0.036  -0.035 128 ILE A CB  
835  C CG1 . ILE A 132 ? 0.490 0.531 0.377 -0.037 0.033  -0.031 128 ILE A CG1 
836  C CG2 . ILE A 132 ? 0.515 0.556 0.395 -0.051 0.034  -0.037 128 ILE A CG2 
837  C CD1 . ILE A 132 ? 0.467 0.522 0.365 -0.038 0.028  -0.031 128 ILE A CD1 
838  N N   . SER A 133 ? 0.598 0.602 0.451 -0.039 0.048  -0.034 129 SER A N   
839  C CA  . SER A 133 ? 0.613 0.609 0.461 -0.033 0.052  -0.032 129 SER A CA  
840  C C   . SER A 133 ? 0.606 0.616 0.468 -0.026 0.047  -0.028 129 SER A C   
841  O O   . SER A 133 ? 0.588 0.612 0.462 -0.028 0.042  -0.028 129 SER A O   
842  C CB  . SER A 133 ? 0.600 0.588 0.437 -0.038 0.055  -0.034 129 SER A CB  
843  O OG  . SER A 133 ? 0.593 0.595 0.441 -0.041 0.050  -0.035 129 SER A OG  
844  N N   . LEU A 134 ? 0.647 0.654 0.507 -0.018 0.051  -0.025 130 LEU A N   
845  C CA  . LEU A 134 ? 0.653 0.672 0.524 -0.013 0.047  -0.021 130 LEU A CA  
846  C C   . LEU A 134 ? 0.606 0.634 0.483 -0.017 0.044  -0.023 130 LEU A C   
847  O O   . LEU A 134 ? 0.572 0.614 0.462 -0.016 0.040  -0.021 130 LEU A O   
848  C CB  . LEU A 134 ? 0.720 0.734 0.587 -0.004 0.052  -0.017 130 LEU A CB  
849  C CG  . LEU A 134 ? 0.826 0.834 0.688 0.002  0.055  -0.015 130 LEU A CG  
850  C CD1 . LEU A 134 ? 0.889 0.887 0.741 0.011  0.062  -0.011 130 LEU A CD1 
851  C CD2 . LEU A 134 ? 0.795 0.818 0.670 0.005  0.050  -0.012 130 LEU A CD2 
852  N N   . GLU A 135 ? 0.601 0.621 0.469 -0.022 0.047  -0.025 131 GLU A N   
853  C CA  . GLU A 135 ? 0.615 0.642 0.487 -0.026 0.044  -0.027 131 GLU A CA  
854  C C   . GLU A 135 ? 0.593 0.633 0.475 -0.031 0.038  -0.029 131 GLU A C   
855  O O   . GLU A 135 ? 0.541 0.593 0.433 -0.031 0.034  -0.027 131 GLU A O   
856  C CB  . GLU A 135 ? 0.692 0.708 0.551 -0.031 0.049  -0.030 131 GLU A CB  
857  C CG  . GLU A 135 ? 0.762 0.784 0.622 -0.038 0.045  -0.032 131 GLU A CG  
858  C CD  . GLU A 135 ? 0.839 0.867 0.703 -0.035 0.045  -0.031 131 GLU A CD  
859  O OE1 . GLU A 135 ? 0.938 0.961 0.794 -0.040 0.046  -0.033 131 GLU A OE1 
860  O OE2 . GLU A 135 ? 0.847 0.885 0.723 -0.029 0.042  -0.028 131 GLU A OE2 
861  N N   . GLN A 136 ? 0.564 0.600 0.442 -0.036 0.039  -0.031 132 GLN A N   
862  C CA  . GLN A 136 ? 0.552 0.599 0.438 -0.040 0.034  -0.032 132 GLN A CA  
863  C C   . GLN A 136 ? 0.545 0.602 0.443 -0.035 0.030  -0.029 132 GLN A C   
864  O O   . GLN A 136 ? 0.567 0.635 0.473 -0.036 0.026  -0.029 132 GLN A O   
865  C CB  . GLN A 136 ? 0.575 0.616 0.454 -0.046 0.036  -0.035 132 GLN A CB  
866  C CG  . GLN A 136 ? 0.584 0.619 0.451 -0.054 0.038  -0.038 132 GLN A CG  
867  C CD  . GLN A 136 ? 0.585 0.612 0.443 -0.059 0.041  -0.041 132 GLN A CD  
868  O OE1 . GLN A 136 ? 0.623 0.640 0.478 -0.056 0.043  -0.040 132 GLN A OE1 
869  N NE2 . GLN A 136 ? 0.573 0.606 0.430 -0.068 0.040  -0.044 132 GLN A NE2 
870  N N   . THR A 137 ? 0.534 0.587 0.432 -0.029 0.031  -0.027 133 THR A N   
871  C CA  . THR A 137 ? 0.507 0.569 0.415 -0.025 0.028  -0.024 133 THR A CA  
872  C C   . THR A 137 ? 0.513 0.584 0.429 -0.024 0.025  -0.022 133 THR A C   
873  O O   . THR A 137 ? 0.492 0.571 0.415 -0.025 0.021  -0.022 133 THR A O   
874  C CB  . THR A 137 ? 0.491 0.549 0.397 -0.020 0.030  -0.021 133 THR A CB  
875  O OG1 . THR A 137 ? 0.526 0.573 0.424 -0.021 0.033  -0.023 133 THR A OG1 
876  C CG2 . THR A 137 ? 0.461 0.528 0.376 -0.017 0.026  -0.019 133 THR A CG2 
877  N N   . GLU A 138 ? 0.551 0.620 0.464 -0.022 0.028  -0.022 134 GLU A N   
878  C CA  . GLU A 138 ? 0.582 0.658 0.501 -0.021 0.026  -0.020 134 GLU A CA  
879  C C   . GLU A 138 ? 0.543 0.625 0.464 -0.026 0.023  -0.022 134 GLU A C   
880  O O   . GLU A 138 ? 0.562 0.651 0.490 -0.025 0.020  -0.021 134 GLU A O   
881  C CB  . GLU A 138 ? 0.638 0.709 0.551 -0.019 0.031  -0.019 134 GLU A CB  
882  C CG  . GLU A 138 ? 0.684 0.759 0.602 -0.013 0.031  -0.015 134 GLU A CG  
883  C CD  . GLU A 138 ? 0.743 0.811 0.655 -0.007 0.036  -0.013 134 GLU A CD  
884  O OE1 . GLU A 138 ? 0.790 0.861 0.705 -0.003 0.036  -0.010 134 GLU A OE1 
885  O OE2 . GLU A 138 ? 0.755 0.813 0.657 -0.006 0.041  -0.014 134 GLU A OE2 
886  N N   . GLU A 139 ? 0.511 0.589 0.426 -0.030 0.024  -0.025 135 GLU A N   
887  C CA  . GLU A 139 ? 0.525 0.610 0.442 -0.034 0.022  -0.026 135 GLU A CA  
888  C C   . GLU A 139 ? 0.493 0.585 0.417 -0.033 0.018  -0.026 135 GLU A C   
889  O O   . GLU A 139 ? 0.459 0.558 0.387 -0.032 0.016  -0.025 135 GLU A O   
890  C CB  . GLU A 139 ? 0.570 0.653 0.480 -0.039 0.023  -0.030 135 GLU A CB  
891  C CG  . GLU A 139 ? 0.592 0.669 0.494 -0.041 0.026  -0.031 135 GLU A CG  
892  C CD  . GLU A 139 ? 0.612 0.681 0.503 -0.047 0.029  -0.034 135 GLU A CD  
893  O OE1 . GLU A 139 ? 0.576 0.650 0.467 -0.052 0.027  -0.036 135 GLU A OE1 
894  O OE2 . GLU A 139 ? 0.649 0.708 0.531 -0.048 0.032  -0.035 135 GLU A OE2 
895  N N   . LEU A 140 ? 0.463 0.552 0.386 -0.034 0.019  -0.026 136 LEU A N   
896  C CA  . LEU A 140 ? 0.451 0.544 0.378 -0.033 0.016  -0.026 136 LEU A CA  
897  C C   . LEU A 140 ? 0.437 0.533 0.370 -0.030 0.014  -0.023 136 LEU A C   
898  O O   . LEU A 140 ? 0.434 0.535 0.370 -0.029 0.012  -0.022 136 LEU A O   
899  C CB  . LEU A 140 ? 0.458 0.546 0.382 -0.034 0.017  -0.026 136 LEU A CB  
900  C CG  . LEU A 140 ? 0.449 0.541 0.376 -0.034 0.015  -0.026 136 LEU A CG  
901  C CD1 . LEU A 140 ? 0.447 0.547 0.375 -0.038 0.014  -0.027 136 LEU A CD1 
902  C CD2 . LEU A 140 ? 0.478 0.563 0.402 -0.035 0.016  -0.027 136 LEU A CD2 
903  N N   . THR A 141 ? 0.424 0.517 0.358 -0.027 0.015  -0.022 137 THR A N   
904  C CA  . THR A 141 ? 0.413 0.511 0.352 -0.025 0.013  -0.019 137 THR A CA  
905  C C   . THR A 141 ? 0.407 0.508 0.349 -0.026 0.012  -0.019 137 THR A C   
906  O O   . THR A 141 ? 0.388 0.492 0.332 -0.026 0.010  -0.018 137 THR A O   
907  C CB  . THR A 141 ? 0.417 0.513 0.356 -0.022 0.015  -0.017 137 THR A CB  
908  O OG1 . THR A 141 ? 0.423 0.515 0.360 -0.021 0.016  -0.017 137 THR A OG1 
909  C CG2 . THR A 141 ? 0.423 0.526 0.369 -0.021 0.013  -0.015 137 THR A CG2 
910  N N   . GLU A 142 ? 0.418 0.520 0.357 -0.026 0.013  -0.019 138 GLU A N   
911  C CA  . GLU A 142 ? 0.462 0.568 0.404 -0.026 0.013  -0.019 138 GLU A CA  
912  C C   . GLU A 142 ? 0.420 0.528 0.362 -0.027 0.011  -0.019 138 GLU A C   
913  O O   . GLU A 142 ? 0.399 0.508 0.341 -0.026 0.010  -0.018 138 GLU A O   
914  C CB  . GLU A 142 ? 0.563 0.668 0.502 -0.026 0.014  -0.019 138 GLU A CB  
915  C CG  . GLU A 142 ? 0.612 0.716 0.551 -0.024 0.017  -0.018 138 GLU A CG  
916  C CD  . GLU A 142 ? 0.720 0.828 0.665 -0.023 0.016  -0.015 138 GLU A CD  
917  O OE1 . GLU A 142 ? 0.806 0.916 0.753 -0.024 0.014  -0.015 138 GLU A OE1 
918  O OE2 . GLU A 142 ? 0.753 0.861 0.700 -0.021 0.016  -0.013 138 GLU A OE2 
919  N N   . MET A 143 ? 0.394 0.503 0.334 -0.028 0.011  -0.021 139 MET A N   
920  C CA  . MET A 143 ? 0.380 0.493 0.319 -0.028 0.010  -0.021 139 MET A CA  
921  C C   . MET A 143 ? 0.364 0.474 0.304 -0.026 0.008  -0.019 139 MET A C   
922  O O   . MET A 143 ? 0.328 0.439 0.267 -0.025 0.008  -0.018 139 MET A O   
923  C CB  . MET A 143 ? 0.399 0.514 0.336 -0.030 0.010  -0.022 139 MET A CB  
924  C CG  . MET A 143 ? 0.416 0.535 0.351 -0.033 0.011  -0.024 139 MET A CG  
925  S SD  . MET A 143 ? 0.424 0.550 0.359 -0.032 0.010  -0.023 139 MET A SD  
926  C CE  . MET A 143 ? 0.413 0.548 0.348 -0.030 0.009  -0.022 139 MET A CE  
927  N N   . PHE A 144 ? 0.372 0.478 0.313 -0.027 0.008  -0.019 140 PHE A N   
928  C CA  . PHE A 144 ? 0.373 0.476 0.315 -0.026 0.007  -0.018 140 PHE A CA  
929  C C   . PHE A 144 ? 0.373 0.475 0.315 -0.026 0.006  -0.017 140 PHE A C   
930  O O   . PHE A 144 ? 0.382 0.481 0.322 -0.026 0.006  -0.016 140 PHE A O   
931  C CB  . PHE A 144 ? 0.379 0.479 0.320 -0.027 0.007  -0.019 140 PHE A CB  
932  C CG  . PHE A 144 ? 0.419 0.518 0.361 -0.027 0.005  -0.018 140 PHE A CG  
933  C CD1 . PHE A 144 ? 0.428 0.528 0.372 -0.027 0.005  -0.016 140 PHE A CD1 
934  C CD2 . PHE A 144 ? 0.436 0.532 0.377 -0.027 0.005  -0.018 140 PHE A CD2 
935  C CE1 . PHE A 144 ? 0.446 0.545 0.391 -0.027 0.003  -0.015 140 PHE A CE1 
936  C CE2 . PHE A 144 ? 0.419 0.513 0.359 -0.027 0.003  -0.017 140 PHE A CE2 
937  C CZ  . PHE A 144 ? 0.424 0.520 0.366 -0.028 0.002  -0.016 140 PHE A CZ  
938  N N   . TYR A 145 ? 0.346 0.450 0.291 -0.027 0.007  -0.016 141 TYR A N   
939  C CA  . TYR A 145 ? 0.331 0.434 0.276 -0.027 0.007  -0.015 141 TYR A CA  
940  C C   . TYR A 145 ? 0.312 0.413 0.253 -0.026 0.007  -0.014 141 TYR A C   
941  O O   . TYR A 145 ? 0.316 0.414 0.255 -0.027 0.007  -0.014 141 TYR A O   
942  C CB  . TYR A 145 ? 0.354 0.461 0.302 -0.027 0.008  -0.014 141 TYR A CB  
943  C CG  . TYR A 145 ? 0.364 0.474 0.315 -0.027 0.007  -0.013 141 TYR A CG  
944  C CD1 . TYR A 145 ? 0.376 0.485 0.327 -0.028 0.006  -0.013 141 TYR A CD1 
945  C CD2 . TYR A 145 ? 0.368 0.479 0.320 -0.025 0.009  -0.012 141 TYR A CD2 
946  C CE1 . TYR A 145 ? 0.397 0.509 0.351 -0.027 0.006  -0.011 141 TYR A CE1 
947  C CE2 . TYR A 145 ? 0.374 0.488 0.329 -0.024 0.010  -0.011 141 TYR A CE2 
948  C CZ  . TYR A 145 ? 0.399 0.514 0.354 -0.024 0.008  -0.010 141 TYR A CZ  
949  O OH  . TYR A 145 ? 0.435 0.553 0.392 -0.022 0.008  -0.009 141 TYR A OH  
950  N N   . GLU A 146 ? 0.298 0.403 0.239 -0.025 0.008  -0.015 142 GLU A N   
951  C CA  . GLU A 146 ? 0.318 0.423 0.255 -0.023 0.009  -0.014 142 GLU A CA  
952  C C   . GLU A 146 ? 0.329 0.430 0.263 -0.021 0.009  -0.014 142 GLU A C   
953  O O   . GLU A 146 ? 0.336 0.432 0.265 -0.020 0.010  -0.012 142 GLU A O   
954  C CB  . GLU A 146 ? 0.331 0.442 0.269 -0.022 0.009  -0.015 142 GLU A CB  
955  C CG  . GLU A 146 ? 0.326 0.440 0.261 -0.019 0.010  -0.014 142 GLU A CG  
956  C CD  . GLU A 146 ? 0.326 0.437 0.258 -0.016 0.011  -0.012 142 GLU A CD  
957  O OE1 . GLU A 146 ? 0.323 0.429 0.254 -0.018 0.012  -0.012 142 GLU A OE1 
958  O OE2 . GLU A 146 ? 0.321 0.434 0.249 -0.013 0.012  -0.011 142 GLU A OE2 
959  N N   . LEU A 147 ? 0.361 0.462 0.295 -0.022 0.008  -0.015 143 LEU A N   
960  C CA  . LEU A 147 ? 0.326 0.422 0.256 -0.020 0.008  -0.014 143 LEU A CA  
961  C C   . LEU A 147 ? 0.301 0.389 0.229 -0.023 0.007  -0.014 143 LEU A C   
962  O O   . LEU A 147 ? 0.300 0.382 0.222 -0.021 0.008  -0.013 143 LEU A O   
963  C CB  . LEU A 147 ? 0.334 0.432 0.266 -0.021 0.007  -0.015 143 LEU A CB  
964  C CG  . LEU A 147 ? 0.354 0.448 0.282 -0.019 0.007  -0.015 143 LEU A CG  
965  C CD1 . LEU A 147 ? 0.358 0.455 0.282 -0.015 0.009  -0.013 143 LEU A CD1 
966  C CD2 . LEU A 147 ? 0.338 0.432 0.267 -0.020 0.007  -0.016 143 LEU A CD2 
967  N N   . GLY A 148 ? 0.281 0.371 0.213 -0.026 0.006  -0.014 144 GLY A N   
968  C CA  . GLY A 148 ? 0.297 0.382 0.227 -0.029 0.005  -0.014 144 GLY A CA  
969  C C   . GLY A 148 ? 0.321 0.400 0.245 -0.030 0.007  -0.012 144 GLY A C   
970  O O   . GLY A 148 ? 0.298 0.371 0.218 -0.033 0.007  -0.012 144 GLY A O   
971  N N   . ARG A 149 ? 0.357 0.438 0.281 -0.027 0.009  -0.012 145 ARG A N   
972  C CA  . ARG A 149 ? 0.359 0.432 0.276 -0.027 0.011  -0.011 145 ARG A CA  
973  C C   . ARG A 149 ? 0.361 0.424 0.268 -0.025 0.012  -0.010 145 ARG A C   
974  O O   . ARG A 149 ? 0.365 0.419 0.265 -0.026 0.015  -0.009 145 ARG A O   
975  C CB  . ARG A 149 ? 0.379 0.457 0.297 -0.023 0.013  -0.010 145 ARG A CB  
976  C CG  . ARG A 149 ? 0.383 0.468 0.307 -0.025 0.012  -0.010 145 ARG A CG  
977  C CD  . ARG A 149 ? 0.379 0.468 0.304 -0.021 0.013  -0.010 145 ARG A CD  
978  N NE  . ARG A 149 ? 0.392 0.476 0.310 -0.018 0.016  -0.008 145 ARG A NE  
979  C CZ  . ARG A 149 ? 0.394 0.481 0.309 -0.013 0.016  -0.008 145 ARG A CZ  
980  N NH1 . ARG A 149 ? 0.383 0.479 0.302 -0.011 0.015  -0.008 145 ARG A NH1 
981  N NH2 . ARG A 149 ? 0.411 0.491 0.317 -0.009 0.019  -0.006 145 ARG A NH2 
982  N N   . PHE A 150 ? 0.362 0.425 0.269 -0.022 0.012  -0.010 146 PHE A N   
983  C CA  . PHE A 150 ? 0.363 0.416 0.260 -0.019 0.014  -0.009 146 PHE A CA  
984  C C   . PHE A 150 ? 0.379 0.424 0.271 -0.023 0.013  -0.010 146 PHE A C   
985  O O   . PHE A 150 ? 0.395 0.430 0.278 -0.021 0.015  -0.009 146 PHE A O   
986  C CB  . PHE A 150 ? 0.356 0.417 0.255 -0.014 0.014  -0.009 146 PHE A CB  
987  C CG  . PHE A 150 ? 0.350 0.418 0.251 -0.010 0.016  -0.008 146 PHE A CG  
988  C CD1 . PHE A 150 ? 0.373 0.434 0.265 -0.005 0.019  -0.005 146 PHE A CD1 
989  C CD2 . PHE A 150 ? 0.343 0.422 0.253 -0.011 0.014  -0.009 146 PHE A CD2 
990  C CE1 . PHE A 150 ? 0.372 0.440 0.266 -0.002 0.020  -0.004 146 PHE A CE1 
991  C CE2 . PHE A 150 ? 0.337 0.423 0.249 -0.008 0.015  -0.008 146 PHE A CE2 
992  C CZ  . PHE A 150 ? 0.343 0.425 0.247 -0.004 0.018  -0.005 146 PHE A CZ  
993  N N   . VAL A 151 ? 0.387 0.435 0.284 -0.029 0.010  -0.011 147 VAL A N   
994  C CA  . VAL A 151 ? 0.403 0.444 0.296 -0.034 0.009  -0.012 147 VAL A CA  
995  C C   . VAL A 151 ? 0.429 0.456 0.309 -0.037 0.011  -0.012 147 VAL A C   
996  O O   . VAL A 151 ? 0.443 0.469 0.322 -0.038 0.013  -0.011 147 VAL A O   
997  C CB  . VAL A 151 ? 0.404 0.456 0.306 -0.039 0.006  -0.013 147 VAL A CB  
998  C CG1 . VAL A 151 ? 0.415 0.461 0.312 -0.046 0.004  -0.013 147 VAL A CG1 
999  C CG2 . VAL A 151 ? 0.401 0.462 0.312 -0.037 0.004  -0.013 147 VAL A CG2 
1000 N N   . VAL A 152 ? 0.476 0.490 0.345 -0.038 0.012  -0.012 148 VAL A N   
1001 C CA  . VAL A 152 ? 0.518 0.514 0.371 -0.042 0.015  -0.012 148 VAL A CA  
1002 C C   . VAL A 152 ? 0.547 0.541 0.399 -0.051 0.012  -0.013 148 VAL A C   
1003 O O   . VAL A 152 ? 0.508 0.511 0.367 -0.052 0.009  -0.014 148 VAL A O   
1004 C CB  . VAL A 152 ? 0.543 0.525 0.384 -0.036 0.019  -0.011 148 VAL A CB  
1005 C CG1 . VAL A 152 ? 0.567 0.556 0.411 -0.026 0.022  -0.009 148 VAL A CG1 
1006 C CG2 . VAL A 152 ? 0.559 0.540 0.398 -0.035 0.018  -0.011 148 VAL A CG2 
1007 N N   . ASP A 153 ? 0.633 0.616 0.474 -0.058 0.014  -0.014 149 ASP A N   
1008 C CA  . ASP A 153 ? 0.726 0.705 0.561 -0.069 0.011  -0.015 149 ASP A CA  
1009 C C   . ASP A 153 ? 0.704 0.662 0.521 -0.069 0.014  -0.016 149 ASP A C   
1010 O O   . ASP A 153 ? 0.764 0.722 0.579 -0.074 0.011  -0.017 149 ASP A O   
1011 C CB  . ASP A 153 ? 0.811 0.792 0.646 -0.078 0.011  -0.016 149 ASP A CB  
1012 C CG  . ASP A 153 ? 0.835 0.839 0.689 -0.077 0.008  -0.015 149 ASP A CG  
1013 O OD1 . ASP A 153 ? 0.865 0.882 0.727 -0.083 0.004  -0.015 149 ASP A OD1 
1014 O OD2 . ASP A 153 ? 0.883 0.890 0.743 -0.069 0.010  -0.014 149 ASP A OD2 
1015 N N   . GLY A 154 ? 0.678 0.620 0.482 -0.063 0.019  -0.015 150 GLY A N   
1016 C CA  . GLY A 154 ? 0.715 0.635 0.500 -0.060 0.023  -0.015 150 GLY A CA  
1017 C C   . GLY A 154 ? 0.696 0.621 0.485 -0.056 0.021  -0.015 150 GLY A C   
1018 O O   . GLY A 154 ? 0.704 0.649 0.511 -0.053 0.017  -0.015 150 GLY A O   
1019 N N   . THR A 155 ? 0.658 0.564 0.431 -0.055 0.024  -0.015 151 THR A N   
1020 C CA  . THR A 155 ? 0.655 0.558 0.426 -0.046 0.025  -0.014 151 THR A CA  
1021 C C   . THR A 155 ? 0.702 0.585 0.454 -0.038 0.033  -0.011 151 THR A C   
1022 O O   . THR A 155 ? 0.718 0.598 0.467 -0.029 0.035  -0.010 151 THR A O   
1023 C CB  . THR A 155 ? 0.628 0.527 0.394 -0.051 0.022  -0.016 151 THR A CB  
1024 O OG1 . THR A 155 ? 0.594 0.471 0.340 -0.059 0.025  -0.017 151 THR A OG1 
1025 C CG2 . THR A 155 ? 0.605 0.525 0.389 -0.058 0.015  -0.017 151 THR A CG2 
1026 N N   . LYS A 156 ? 0.793 0.662 0.533 -0.041 0.037  -0.011 152 LYS A N   
1027 C CA  . LYS A 156 ? 0.871 0.720 0.593 -0.032 0.045  -0.008 152 LYS A CA  
1028 C C   . LYS A 156 ? 0.860 0.727 0.597 -0.023 0.045  -0.006 152 LYS A C   
1029 O O   . LYS A 156 ? 0.930 0.809 0.678 -0.029 0.042  -0.007 152 LYS A O   
1030 C CB  . LYS A 156 ? 0.947 0.773 0.648 -0.041 0.049  -0.010 152 LYS A CB  
1031 C CG  . LYS A 156 ? 1.016 0.824 0.702 -0.051 0.048  -0.012 152 LYS A CG  
1032 C CD  . LYS A 156 ? 1.055 0.857 0.734 -0.067 0.046  -0.015 152 LYS A CD  
1033 C CE  . LYS A 156 ? 1.076 0.859 0.739 -0.069 0.052  -0.015 152 LYS A CE  
1034 N NZ  . LYS A 156 ? 1.115 0.875 0.756 -0.084 0.054  -0.018 152 LYS A NZ  
1035 N N   . GLY A 157 ? 0.784 0.657 0.524 -0.011 0.047  -0.003 153 GLY A N   
1036 C CA  . GLY A 157 ? 0.739 0.635 0.497 -0.004 0.046  -0.001 153 GLY A CA  
1037 C C   . GLY A 157 ? 0.729 0.642 0.499 0.002  0.044  -0.000 153 GLY A C   
1038 O O   . GLY A 157 ? 0.732 0.646 0.506 -0.002 0.040  -0.002 153 GLY A O   
1039 N N   . GLU A 158 ? 0.691 0.616 0.467 0.013  0.046  0.003  154 GLU A N   
1040 C CA  . GLU A 158 ? 0.690 0.633 0.479 0.019  0.044  0.004  154 GLU A CA  
1041 C C   . GLU A 158 ? 0.590 0.553 0.399 0.011  0.037  0.001  154 GLU A C   
1042 O O   . GLU A 158 ? 0.579 0.546 0.393 0.007  0.035  -0.000 154 GLU A O   
1043 C CB  . GLU A 158 ? 0.766 0.719 0.556 0.031  0.048  0.009  154 GLU A CB  
1044 C CG  . GLU A 158 ? 0.885 0.817 0.653 0.041  0.056  0.013  154 GLU A CG  
1045 C CD  . GLU A 158 ? 1.005 0.926 0.762 0.045  0.059  0.014  154 GLU A CD  
1046 O OE1 . GLU A 158 ? 1.020 0.917 0.755 0.051  0.066  0.016  154 GLU A OE1 
1047 O OE2 . GLU A 158 ? 1.126 1.061 0.896 0.043  0.055  0.013  154 GLU A OE2 
1048 N N   . GLN A 159 ? 0.507 0.481 0.326 0.010  0.033  -0.000 155 GLN A N   
1049 C CA  . GLN A 159 ? 0.452 0.442 0.288 0.003  0.028  -0.003 155 GLN A CA  
1050 C C   . GLN A 159 ? 0.420 0.429 0.268 0.007  0.026  -0.002 155 GLN A C   
1051 O O   . GLN A 159 ? 0.425 0.433 0.269 0.014  0.029  -0.000 155 GLN A O   
1052 C CB  . GLN A 159 ? 0.445 0.427 0.278 -0.004 0.025  -0.006 155 GLN A CB  
1053 C CG  . GLN A 159 ? 0.460 0.423 0.279 -0.010 0.026  -0.007 155 GLN A CG  
1054 C CD  . GLN A 159 ? 0.459 0.409 0.268 -0.014 0.025  -0.008 155 GLN A CD  
1055 O OE1 . GLN A 159 ? 0.448 0.402 0.261 -0.013 0.024  -0.008 155 GLN A OE1 
1056 N NE2 . GLN A 159 ? 0.475 0.409 0.272 -0.020 0.026  -0.009 155 GLN A NE2 
1057 N N   . GLY A 160 ? 0.393 0.417 0.255 0.004  0.023  -0.004 156 GLY A N   
1058 C CA  . GLY A 160 ? 0.367 0.410 0.241 0.006  0.022  -0.004 156 GLY A CA  
1059 C C   . GLY A 160 ? 0.368 0.416 0.250 0.001  0.018  -0.006 156 GLY A C   
1060 O O   . GLY A 160 ? 0.374 0.436 0.265 0.001  0.017  -0.007 156 GLY A O   
1061 N N   . GLY A 161 ? 0.361 0.399 0.240 -0.004 0.016  -0.008 157 GLY A N   
1062 C CA  . GLY A 161 ? 0.341 0.384 0.228 -0.009 0.013  -0.010 157 GLY A CA  
1063 C C   . GLY A 161 ? 0.328 0.368 0.216 -0.015 0.010  -0.012 157 GLY A C   
1064 O O   . GLY A 161 ? 0.323 0.353 0.203 -0.017 0.011  -0.012 157 GLY A O   
1065 N N   . PHE A 162 ? 0.317 0.364 0.213 -0.018 0.007  -0.014 158 PHE A N   
1066 C CA  . PHE A 162 ? 0.319 0.366 0.218 -0.024 0.005  -0.015 158 PHE A CA  
1067 C C   . PHE A 162 ? 0.311 0.369 0.220 -0.025 0.003  -0.016 158 PHE A C   
1068 O O   . PHE A 162 ? 0.304 0.368 0.217 -0.023 0.004  -0.016 158 PHE A O   
1069 C CB  . PHE A 162 ? 0.327 0.367 0.220 -0.026 0.003  -0.016 158 PHE A CB  
1070 C CG  . PHE A 162 ? 0.328 0.370 0.223 -0.024 0.003  -0.016 158 PHE A CG  
1071 C CD1 . PHE A 162 ? 0.321 0.356 0.210 -0.021 0.005  -0.015 158 PHE A CD1 
1072 C CD2 . PHE A 162 ? 0.322 0.371 0.224 -0.026 0.001  -0.017 158 PHE A CD2 
1073 C CE1 . PHE A 162 ? 0.316 0.353 0.206 -0.019 0.005  -0.016 158 PHE A CE1 
1074 C CE2 . PHE A 162 ? 0.318 0.366 0.220 -0.024 0.001  -0.017 158 PHE A CE2 
1075 C CZ  . PHE A 162 ? 0.318 0.361 0.215 -0.021 0.003  -0.017 158 PHE A CZ  
1076 N N   . ILE A 163 ? 0.313 0.373 0.225 -0.028 0.001  -0.016 159 ILE A N   
1077 C CA  . ILE A 163 ? 0.321 0.390 0.240 -0.029 -0.000 -0.017 159 ILE A CA  
1078 C C   . ILE A 163 ? 0.335 0.404 0.255 -0.032 -0.003 -0.017 159 ILE A C   
1079 O O   . ILE A 163 ? 0.324 0.391 0.241 -0.035 -0.004 -0.016 159 ILE A O   
1080 C CB  . ILE A 163 ? 0.322 0.396 0.245 -0.030 -0.000 -0.016 159 ILE A CB  
1081 C CG1 . ILE A 163 ? 0.330 0.405 0.253 -0.027 0.002  -0.016 159 ILE A CG1 
1082 C CG2 . ILE A 163 ? 0.309 0.390 0.239 -0.031 -0.001 -0.016 159 ILE A CG2 
1083 C CD1 . ILE A 163 ? 0.326 0.406 0.253 -0.028 0.003  -0.016 159 ILE A CD1 
1084 N N   . SER A 164 ? 0.349 0.421 0.271 -0.030 -0.003 -0.017 160 SER A N   
1085 C CA  . SER A 164 ? 0.387 0.461 0.310 -0.032 -0.006 -0.016 160 SER A CA  
1086 C C   . SER A 164 ? 0.364 0.447 0.294 -0.031 -0.005 -0.015 160 SER A C   
1087 O O   . SER A 164 ? 0.335 0.419 0.267 -0.028 -0.003 -0.016 160 SER A O   
1088 C CB  . SER A 164 ? 0.403 0.473 0.322 -0.030 -0.006 -0.017 160 SER A CB  
1089 O OG  . SER A 164 ? 0.442 0.516 0.364 -0.028 -0.006 -0.016 160 SER A OG  
1090 N N   . ILE A 165 ? 0.370 0.459 0.302 -0.033 -0.007 -0.014 161 ILE A N   
1091 C CA  . ILE A 165 ? 0.378 0.476 0.316 -0.031 -0.007 -0.012 161 ILE A CA  
1092 C C   . ILE A 165 ? 0.398 0.500 0.336 -0.029 -0.009 -0.011 161 ILE A C   
1093 O O   . ILE A 165 ? 0.436 0.541 0.372 -0.032 -0.012 -0.010 161 ILE A O   
1094 C CB  . ILE A 165 ? 0.389 0.495 0.331 -0.034 -0.008 -0.011 161 ILE A CB  
1095 C CG1 . ILE A 165 ? 0.400 0.500 0.340 -0.035 -0.006 -0.012 161 ILE A CG1 
1096 C CG2 . ILE A 165 ? 0.381 0.495 0.328 -0.031 -0.007 -0.009 161 ILE A CG2 
1097 C CD1 . ILE A 165 ? 0.399 0.498 0.341 -0.031 -0.004 -0.013 161 ILE A CD1 
1098 N N   . ASP A 166 ? 0.420 0.523 0.359 -0.024 -0.007 -0.010 162 ASP A N   
1099 C CA  . ASP A 166 ? 0.439 0.547 0.378 -0.021 -0.007 -0.008 162 ASP A CA  
1100 C C   . ASP A 166 ? 0.442 0.547 0.377 -0.023 -0.010 -0.008 162 ASP A C   
1101 O O   . ASP A 166 ? 0.424 0.536 0.359 -0.022 -0.012 -0.007 162 ASP A O   
1102 C CB  . ASP A 166 ? 0.447 0.568 0.392 -0.021 -0.008 -0.005 162 ASP A CB  
1103 C CG  . ASP A 166 ? 0.484 0.609 0.433 -0.017 -0.005 -0.004 162 ASP A CG  
1104 O OD1 . ASP A 166 ? 0.485 0.601 0.431 -0.015 -0.002 -0.005 162 ASP A OD1 
1105 O OD2 . ASP A 166 ? 0.497 0.632 0.450 -0.018 -0.006 -0.002 162 ASP A OD2 
1106 N N   . GLU A 167 ? 0.485 0.580 0.415 -0.024 -0.009 -0.011 163 GLU A N   
1107 C CA  . GLU A 167 ? 0.520 0.609 0.444 -0.025 -0.011 -0.012 163 GLU A CA  
1108 C C   . GLU A 167 ? 0.519 0.612 0.442 -0.030 -0.015 -0.011 163 GLU A C   
1109 O O   . GLU A 167 ? 0.525 0.615 0.443 -0.031 -0.017 -0.011 163 GLU A O   
1110 C CB  . GLU A 167 ? 0.515 0.602 0.437 -0.020 -0.010 -0.011 163 GLU A CB  
1111 C CG  . GLU A 167 ? 0.538 0.617 0.459 -0.017 -0.006 -0.012 163 GLU A CG  
1112 C CD  . GLU A 167 ? 0.558 0.632 0.474 -0.013 -0.004 -0.012 163 GLU A CD  
1113 O OE1 . GLU A 167 ? 0.556 0.622 0.468 -0.014 -0.003 -0.014 163 GLU A OE1 
1114 O OE2 . GLU A 167 ? 0.602 0.679 0.518 -0.009 -0.002 -0.010 163 GLU A OE2 
1115 N N   . ARG A 168 ? 0.512 0.612 0.439 -0.034 -0.016 -0.010 164 ARG A N   
1116 C CA  A ARG A 168 ? 0.502 0.606 0.427 -0.041 -0.020 -0.010 164 ARG A CA  
1117 C CA  B ARG A 168 ? 0.517 0.621 0.442 -0.041 -0.020 -0.010 164 ARG A CA  
1118 C C   . ARG A 168 ? 0.533 0.629 0.454 -0.046 -0.019 -0.012 164 ARG A C   
1119 O O   . ARG A 168 ? 0.607 0.694 0.519 -0.049 -0.020 -0.013 164 ARG A O   
1120 C CB  A ARG A 168 ? 0.473 0.593 0.405 -0.041 -0.021 -0.007 164 ARG A CB  
1121 C CB  B ARG A 168 ? 0.507 0.628 0.440 -0.041 -0.021 -0.007 164 ARG A CB  
1122 C CG  A ARG A 168 ? 0.451 0.583 0.384 -0.040 -0.024 -0.005 164 ARG A CG  
1123 C CG  B ARG A 168 ? 0.501 0.632 0.436 -0.037 -0.023 -0.004 164 ARG A CG  
1124 C CD  A ARG A 168 ? 0.420 0.560 0.352 -0.049 -0.028 -0.004 164 ARG A CD  
1125 C CD  B ARG A 168 ? 0.472 0.611 0.405 -0.042 -0.027 -0.003 164 ARG A CD  
1126 N NE  A ARG A 168 ? 0.404 0.546 0.331 -0.051 -0.032 -0.004 164 ARG A NE  
1127 N NE  B ARG A 168 ? 0.464 0.606 0.396 -0.036 -0.027 -0.001 164 ARG A NE  
1128 C CZ  A ARG A 168 ? 0.386 0.531 0.309 -0.060 -0.036 -0.004 164 ARG A CZ  
1129 C CZ  B ARG A 168 ? 0.469 0.600 0.396 -0.031 -0.026 -0.003 164 ARG A CZ  
1130 N NH1 A ARG A 168 ? 0.362 0.508 0.285 -0.067 -0.036 -0.005 164 ARG A NH1 
1131 N NH1 B ARG A 168 ? 0.480 0.596 0.403 -0.033 -0.024 -0.006 164 ARG A NH1 
1132 N NH2 A ARG A 168 ? 0.387 0.534 0.305 -0.061 -0.039 -0.004 164 ARG A NH2 
1133 N NH2 B ARG A 168 ? 0.472 0.605 0.398 -0.025 -0.025 -0.001 164 ARG A NH2 
1134 N N   . ASP A 169 ? 0.521 0.618 0.445 -0.045 -0.017 -0.012 165 ASP A N   
1135 C CA  . ASP A 169 ? 0.492 0.582 0.412 -0.050 -0.017 -0.013 165 ASP A CA  
1136 C C   . ASP A 169 ? 0.441 0.520 0.358 -0.046 -0.013 -0.014 165 ASP A C   
1137 O O   . ASP A 169 ? 0.408 0.489 0.329 -0.041 -0.012 -0.014 165 ASP A O   
1138 C CB  . ASP A 169 ? 0.499 0.598 0.425 -0.053 -0.017 -0.012 165 ASP A CB  
1139 C CG  . ASP A 169 ? 0.528 0.638 0.455 -0.058 -0.020 -0.010 165 ASP A CG  
1140 O OD1 . ASP A 169 ? 0.558 0.664 0.479 -0.063 -0.022 -0.011 165 ASP A OD1 
1141 O OD2 . ASP A 169 ? 0.568 0.692 0.504 -0.056 -0.020 -0.008 165 ASP A OD2 
1142 N N   . VAL A 170 ? 0.410 0.478 0.318 -0.049 -0.013 -0.015 166 VAL A N   
1143 C CA  . VAL A 170 ? 0.390 0.447 0.294 -0.045 -0.009 -0.016 166 VAL A CA  
1144 C C   . VAL A 170 ? 0.364 0.415 0.263 -0.047 -0.007 -0.016 166 VAL A C   
1145 O O   . VAL A 170 ? 0.370 0.413 0.260 -0.053 -0.008 -0.017 166 VAL A O   
1146 C CB  . VAL A 170 ? 0.404 0.452 0.300 -0.044 -0.009 -0.017 166 VAL A CB  
1147 C CG1 . VAL A 170 ? 0.421 0.460 0.312 -0.039 -0.005 -0.017 166 VAL A CG1 
1148 C CG2 . VAL A 170 ? 0.396 0.449 0.295 -0.042 -0.011 -0.017 166 VAL A CG2 
1149 N N   . TYR A 171 ? 0.340 0.391 0.241 -0.044 -0.005 -0.016 167 TYR A N   
1150 C CA  . TYR A 171 ? 0.343 0.388 0.239 -0.045 -0.003 -0.016 167 TYR A CA  
1151 C C   . TYR A 171 ? 0.342 0.380 0.234 -0.039 0.000  -0.015 167 TYR A C   
1152 O O   . TYR A 171 ? 0.336 0.381 0.234 -0.035 0.001  -0.015 167 TYR A O   
1153 C CB  . TYR A 171 ? 0.339 0.393 0.243 -0.045 -0.002 -0.015 167 TYR A CB  
1154 C CG  . TYR A 171 ? 0.324 0.389 0.235 -0.049 -0.005 -0.015 167 TYR A CG  
1155 C CD1 . TYR A 171 ? 0.344 0.407 0.251 -0.055 -0.006 -0.014 167 TYR A CD1 
1156 C CD2 . TYR A 171 ? 0.310 0.385 0.229 -0.047 -0.007 -0.014 167 TYR A CD2 
1157 C CE1 . TYR A 171 ? 0.345 0.421 0.260 -0.060 -0.008 -0.013 167 TYR A CE1 
1158 C CE2 . TYR A 171 ? 0.320 0.406 0.245 -0.050 -0.009 -0.013 167 TYR A CE2 
1159 C CZ  . TYR A 171 ? 0.332 0.419 0.255 -0.056 -0.010 -0.013 167 TYR A CZ  
1160 O OH  . TYR A 171 ? 0.349 0.450 0.279 -0.059 -0.012 -0.011 167 TYR A OH  
1161 N N   . LEU A 172 ? 0.362 0.388 0.242 -0.039 0.003  -0.015 168 LEU A N   
1162 C CA  . LEU A 172 ? 0.387 0.407 0.262 -0.032 0.007  -0.014 168 LEU A CA  
1163 C C   . LEU A 172 ? 0.379 0.403 0.257 -0.029 0.009  -0.013 168 LEU A C   
1164 O O   . LEU A 172 ? 0.365 0.389 0.243 -0.032 0.009  -0.013 168 LEU A O   
1165 C CB  . LEU A 172 ? 0.409 0.411 0.268 -0.033 0.009  -0.014 168 LEU A CB  
1166 C CG  . LEU A 172 ? 0.420 0.415 0.273 -0.038 0.007  -0.015 168 LEU A CG  
1167 C CD1 . LEU A 172 ? 0.433 0.409 0.269 -0.042 0.009  -0.015 168 LEU A CD1 
1168 C CD2 . LEU A 172 ? 0.424 0.422 0.280 -0.032 0.007  -0.015 168 LEU A CD2 
1169 N N   . LEU A 173 ? 0.378 0.408 0.259 -0.022 0.010  -0.012 169 LEU A N   
1170 C CA  . LEU A 173 ? 0.377 0.412 0.260 -0.018 0.012  -0.011 169 LEU A CA  
1171 C C   . LEU A 173 ? 0.396 0.420 0.268 -0.013 0.017  -0.009 169 LEU A C   
1172 O O   . LEU A 173 ? 0.399 0.416 0.263 -0.010 0.018  -0.008 169 LEU A O   
1173 C CB  . LEU A 173 ? 0.362 0.411 0.255 -0.015 0.011  -0.011 169 LEU A CB  
1174 C CG  . LEU A 173 ? 0.358 0.417 0.262 -0.020 0.008  -0.013 169 LEU A CG  
1175 C CD1 . LEU A 173 ? 0.350 0.419 0.261 -0.018 0.008  -0.013 169 LEU A CD1 
1176 C CD2 . LEU A 173 ? 0.372 0.434 0.280 -0.022 0.008  -0.013 169 LEU A CD2 
1177 N N   . ALA A 174 ? 0.407 0.430 0.276 -0.011 0.019  -0.007 170 ALA A N   
1178 C CA  . ALA A 174 ? 0.438 0.452 0.296 -0.004 0.024  -0.005 170 ALA A CA  
1179 C C   . ALA A 174 ? 0.447 0.472 0.309 0.004  0.025  -0.003 170 ALA A C   
1180 O O   . ALA A 174 ? 0.470 0.510 0.344 0.002  0.022  -0.004 170 ALA A O   
1181 C CB  . ALA A 174 ? 0.430 0.441 0.285 -0.005 0.025  -0.004 170 ALA A CB  
1182 N N   . ALA A 175 ? 0.506 0.524 0.357 0.011  0.029  0.000  171 ALA A N   
1183 C CA  . ALA A 175 ? 0.519 0.550 0.373 0.020  0.031  0.003  171 ALA A CA  
1184 C C   . ALA A 175 ? 0.518 0.558 0.375 0.024  0.032  0.005  171 ALA A C   
1185 O O   . ALA A 175 ? 0.522 0.557 0.377 0.021  0.032  0.004  171 ALA A O   
1186 C CB  . ALA A 175 ? 0.516 0.534 0.357 0.027  0.036  0.006  171 ALA A CB  
1187 N N   . GLY A 176 ? 0.570 0.625 0.430 0.031  0.033  0.008  172 GLY A N   
1188 C CA  . GLY A 176 ? 0.597 0.660 0.457 0.037  0.035  0.011  172 GLY A CA  
1189 C C   . GLY A 176 ? 0.614 0.699 0.489 0.034  0.031  0.009  172 GLY A C   
1190 O O   . GLY A 176 ? 0.625 0.715 0.509 0.026  0.027  0.006  172 GLY A O   
1191 N N   . ARG A 177 ? 0.627 0.723 0.502 0.039  0.032  0.012  173 ARG A N   
1192 C CA  . ARG A 177 ? 0.678 0.796 0.565 0.037  0.028  0.011  173 ARG A CA  
1193 C C   . ARG A 177 ? 0.598 0.717 0.493 0.028  0.025  0.007  173 ARG A C   
1194 O O   . ARG A 177 ? 0.511 0.644 0.416 0.023  0.021  0.005  173 ARG A O   
1195 C CB  . ARG A 177 ? 0.807 0.939 0.693 0.045  0.030  0.015  173 ARG A CB  
1196 C CG  . ARG A 177 ? 0.929 1.085 0.826 0.043  0.027  0.015  173 ARG A CG  
1197 C CD  . ARG A 177 ? 1.007 1.174 0.907 0.043  0.026  0.015  173 ARG A CD  
1198 N NE  . ARG A 177 ? 1.096 1.267 0.988 0.054  0.029  0.021  173 ARG A NE  
1199 C CZ  . ARG A 177 ? 1.144 1.327 1.037 0.057  0.029  0.022  173 ARG A CZ  
1200 N NH1 . ARG A 177 ? 1.130 1.321 1.030 0.049  0.025  0.019  173 ARG A NH1 
1201 N NH2 . ARG A 177 ? 1.215 1.401 1.100 0.068  0.032  0.028  173 ARG A NH2 
1202 N N   . GLU A 178 ? 0.587 0.693 0.477 0.026  0.025  0.006  174 GLU A N   
1203 C CA  . GLU A 178 ? 0.611 0.719 0.509 0.018  0.022  0.002  174 GLU A CA  
1204 C C   . GLU A 178 ? 0.526 0.631 0.429 0.011  0.019  -0.001 174 GLU A C   
1205 O O   . GLU A 178 ? 0.472 0.587 0.384 0.006  0.017  -0.003 174 GLU A O   
1206 C CB  . GLU A 178 ? 0.714 0.810 0.606 0.018  0.024  0.003  174 GLU A CB  
1207 C CG  . GLU A 178 ? 0.810 0.911 0.697 0.025  0.026  0.006  174 GLU A CG  
1208 C CD  . GLU A 178 ? 0.906 0.991 0.783 0.028  0.030  0.008  174 GLU A CD  
1209 O OE1 . GLU A 178 ? 0.918 1.007 0.791 0.034  0.032  0.010  174 GLU A OE1 
1210 O OE2 . GLU A 178 ? 0.966 1.034 0.837 0.023  0.031  0.006  174 GLU A OE2 
1211 N N   . CYS A 179 ? 0.464 0.557 0.362 0.010  0.020  -0.001 175 CYS A N   
1212 C CA  . CYS A 179 ? 0.417 0.508 0.320 0.005  0.018  -0.004 175 CYS A CA  
1213 C C   . CYS A 179 ? 0.375 0.480 0.285 0.005  0.016  -0.004 175 CYS A C   
1214 O O   . CYS A 179 ? 0.369 0.478 0.285 -0.001 0.014  -0.007 175 CYS A O   
1215 C CB  . CYS A 179 ? 0.442 0.519 0.337 0.005  0.019  -0.003 175 CYS A CB  
1216 S SG  . CYS A 179 ? 0.443 0.519 0.344 -0.002 0.016  -0.007 175 CYS A SG  
1217 N N   . ALA A 180 ? 0.357 0.469 0.265 0.010  0.018  -0.001 176 ALA A N   
1218 C CA  . ALA A 180 ? 0.364 0.491 0.278 0.010  0.017  -0.002 176 ALA A CA  
1219 C C   . ALA A 180 ? 0.355 0.496 0.277 0.005  0.015  -0.004 176 ALA A C   
1220 O O   . ALA A 180 ? 0.354 0.500 0.280 0.000  0.013  -0.006 176 ALA A O   
1221 C CB  . ALA A 180 ? 0.362 0.497 0.273 0.017  0.020  0.002  176 ALA A CB  
1222 N N   . GLU A 181 ? 0.375 0.519 0.296 0.007  0.015  -0.002 177 GLU A N   
1223 C CA  . GLU A 181 ? 0.369 0.524 0.295 0.003  0.013  -0.004 177 GLU A CA  
1224 C C   . GLU A 181 ? 0.346 0.494 0.275 -0.004 0.011  -0.008 177 GLU A C   
1225 O O   . GLU A 181 ? 0.342 0.497 0.275 -0.009 0.010  -0.010 177 GLU A O   
1226 C CB  . GLU A 181 ? 0.416 0.574 0.339 0.007  0.014  -0.002 177 GLU A CB  
1227 C CG  . GLU A 181 ? 0.453 0.623 0.381 0.003  0.012  -0.004 177 GLU A CG  
1228 C CD  . GLU A 181 ? 0.502 0.689 0.433 0.000  0.011  -0.004 177 GLU A CD  
1229 O OE1 . GLU A 181 ? 0.515 0.708 0.450 -0.007 0.009  -0.007 177 GLU A OE1 
1230 O OE2 . GLU A 181 ? 0.569 0.764 0.500 0.005  0.012  -0.002 177 GLU A OE2 
1231 N N   . ALA A 182 ? 0.344 0.478 0.271 -0.005 0.012  -0.009 178 ALA A N   
1232 C CA  . ALA A 182 ? 0.337 0.466 0.267 -0.011 0.010  -0.012 178 ALA A CA  
1233 C C   . ALA A 182 ? 0.338 0.467 0.271 -0.014 0.009  -0.013 178 ALA A C   
1234 O O   . ALA A 182 ? 0.332 0.462 0.267 -0.019 0.009  -0.016 178 ALA A O   
1235 C CB  . ALA A 182 ? 0.341 0.457 0.268 -0.011 0.011  -0.011 178 ALA A CB  
1236 N N   . GLY A 183 ? 0.341 0.468 0.272 -0.012 0.010  -0.012 179 GLY A N   
1237 C CA  . GLY A 183 ? 0.343 0.470 0.275 -0.014 0.010  -0.014 179 GLY A CA  
1238 C C   . GLY A 183 ? 0.331 0.472 0.267 -0.017 0.009  -0.015 179 GLY A C   
1239 O O   . GLY A 183 ? 0.305 0.445 0.242 -0.022 0.009  -0.017 179 GLY A O   
1240 N N   . ASP A 184 ? 0.344 0.495 0.279 -0.014 0.010  -0.013 180 ASP A N   
1241 C CA  . ASP A 184 ? 0.344 0.510 0.282 -0.018 0.009  -0.013 180 ASP A CA  
1242 C C   . ASP A 184 ? 0.341 0.506 0.280 -0.024 0.008  -0.017 180 ASP A C   
1243 O O   . ASP A 184 ? 0.345 0.511 0.285 -0.030 0.008  -0.019 180 ASP A O   
1244 C CB  . ASP A 184 ? 0.361 0.541 0.299 -0.013 0.010  -0.010 180 ASP A CB  
1245 C CG  . ASP A 184 ? 0.389 0.573 0.326 -0.006 0.011  -0.007 180 ASP A CG  
1246 O OD1 . ASP A 184 ? 0.387 0.563 0.323 -0.007 0.012  -0.007 180 ASP A OD1 
1247 O OD2 . ASP A 184 ? 0.435 0.630 0.371 -0.001 0.012  -0.003 180 ASP A OD2 
1248 N N   . GLU A 185 ? 0.364 0.523 0.302 -0.023 0.008  -0.017 181 GLU A N   
1249 C CA  . GLU A 185 ? 0.387 0.545 0.325 -0.028 0.008  -0.019 181 GLU A CA  
1250 C C   . GLU A 185 ? 0.358 0.505 0.295 -0.032 0.008  -0.022 181 GLU A C   
1251 O O   . GLU A 185 ? 0.351 0.497 0.286 -0.037 0.009  -0.024 181 GLU A O   
1252 C CB  . GLU A 185 ? 0.414 0.571 0.351 -0.025 0.008  -0.018 181 GLU A CB  
1253 C CG  . GLU A 185 ? 0.464 0.632 0.400 -0.021 0.008  -0.016 181 GLU A CG  
1254 C CD  . GLU A 185 ? 0.533 0.699 0.467 -0.018 0.008  -0.014 181 GLU A CD  
1255 O OE1 . GLU A 185 ? 0.595 0.752 0.529 -0.020 0.008  -0.015 181 GLU A OE1 
1256 O OE2 . GLU A 185 ? 0.558 0.730 0.491 -0.012 0.008  -0.011 181 GLU A OE2 
1257 N N   . LEU A 186 ? 0.345 0.483 0.283 -0.029 0.008  -0.021 182 LEU A N   
1258 C CA  . LEU A 186 ? 0.342 0.471 0.279 -0.031 0.009  -0.022 182 LEU A CA  
1259 C C   . LEU A 186 ? 0.345 0.476 0.281 -0.035 0.009  -0.024 182 LEU A C   
1260 O O   . LEU A 186 ? 0.349 0.474 0.282 -0.038 0.010  -0.026 182 LEU A O   
1261 C CB  . LEU A 186 ? 0.357 0.479 0.295 -0.028 0.008  -0.021 182 LEU A CB  
1262 C CG  . LEU A 186 ? 0.360 0.473 0.297 -0.029 0.008  -0.022 182 LEU A CG  
1263 C CD1 . LEU A 186 ? 0.357 0.466 0.294 -0.030 0.009  -0.023 182 LEU A CD1 
1264 C CD2 . LEU A 186 ? 0.367 0.475 0.304 -0.026 0.007  -0.020 182 LEU A CD2 
1265 N N   . PHE A 187 ? 0.355 0.492 0.292 -0.033 0.009  -0.023 183 PHE A N   
1266 C CA  . PHE A 187 ? 0.397 0.535 0.332 -0.037 0.010  -0.024 183 PHE A CA  
1267 C C   . PHE A 187 ? 0.388 0.534 0.322 -0.044 0.011  -0.026 183 PHE A C   
1268 O O   . PHE A 187 ? 0.381 0.522 0.311 -0.049 0.012  -0.029 183 PHE A O   
1269 C CB  . PHE A 187 ? 0.428 0.573 0.365 -0.034 0.010  -0.022 183 PHE A CB  
1270 C CG  . PHE A 187 ? 0.435 0.569 0.371 -0.031 0.010  -0.022 183 PHE A CG  
1271 C CD1 . PHE A 187 ? 0.453 0.582 0.387 -0.033 0.011  -0.023 183 PHE A CD1 
1272 C CD2 . PHE A 187 ? 0.456 0.583 0.391 -0.027 0.010  -0.020 183 PHE A CD2 
1273 C CE1 . PHE A 187 ? 0.434 0.553 0.367 -0.030 0.011  -0.022 183 PHE A CE1 
1274 C CE2 . PHE A 187 ? 0.456 0.573 0.389 -0.024 0.009  -0.019 183 PHE A CE2 
1275 C CZ  . PHE A 187 ? 0.439 0.552 0.371 -0.026 0.010  -0.020 183 PHE A CZ  
1276 N N   . ASN A 188 ? 0.407 0.564 0.343 -0.043 0.010  -0.025 184 ASN A N   
1277 C CA  . ASN A 188 ? 0.437 0.603 0.370 -0.050 0.010  -0.027 184 ASN A CA  
1278 C C   . ASN A 188 ? 0.406 0.560 0.334 -0.054 0.011  -0.030 184 ASN A C   
1279 O O   . ASN A 188 ? 0.411 0.564 0.335 -0.061 0.012  -0.033 184 ASN A O   
1280 C CB  . ASN A 188 ? 0.475 0.657 0.411 -0.047 0.008  -0.025 184 ASN A CB  
1281 C CG  . ASN A 188 ? 0.536 0.734 0.476 -0.045 0.008  -0.022 184 ASN A CG  
1282 O OD1 . ASN A 188 ? 0.572 0.769 0.513 -0.043 0.009  -0.021 184 ASN A OD1 
1283 N ND2 . ASN A 188 ? 0.584 0.798 0.525 -0.045 0.007  -0.021 184 ASN A ND2 
1284 N N   . LEU A 189 ? 0.374 0.518 0.303 -0.050 0.011  -0.030 185 LEU A N   
1285 C CA  . LEU A 189 ? 0.387 0.520 0.310 -0.054 0.013  -0.032 185 LEU A CA  
1286 C C   . LEU A 189 ? 0.392 0.514 0.311 -0.056 0.015  -0.034 185 LEU A C   
1287 O O   . LEU A 189 ? 0.385 0.500 0.296 -0.062 0.018  -0.036 185 LEU A O   
1288 C CB  . LEU A 189 ? 0.391 0.517 0.316 -0.049 0.013  -0.031 185 LEU A CB  
1289 C CG  . LEU A 189 ? 0.384 0.499 0.303 -0.050 0.015  -0.032 185 LEU A CG  
1290 C CD1 . LEU A 189 ? 0.389 0.508 0.303 -0.056 0.016  -0.034 185 LEU A CD1 
1291 C CD2 . LEU A 189 ? 0.394 0.506 0.316 -0.045 0.015  -0.030 185 LEU A CD2 
1292 N N   . ALA A 190 ? 0.391 0.509 0.312 -0.052 0.015  -0.032 186 ALA A N   
1293 C CA  . ALA A 190 ? 0.389 0.497 0.307 -0.054 0.017  -0.034 186 ALA A CA  
1294 C C   . ALA A 190 ? 0.392 0.504 0.305 -0.061 0.018  -0.036 186 ALA A C   
1295 O O   . ALA A 190 ? 0.374 0.475 0.279 -0.066 0.021  -0.038 186 ALA A O   
1296 C CB  . ALA A 190 ? 0.402 0.508 0.323 -0.048 0.016  -0.032 186 ALA A CB  
1297 N N   . MET A 191 ? 0.403 0.529 0.320 -0.062 0.017  -0.035 187 MET A N   
1298 C CA  . MET A 191 ? 0.448 0.581 0.362 -0.070 0.018  -0.037 187 MET A CA  
1299 C C   . MET A 191 ? 0.486 0.616 0.393 -0.078 0.019  -0.040 187 MET A C   
1300 O O   . MET A 191 ? 0.505 0.627 0.404 -0.085 0.022  -0.043 187 MET A O   
1301 C CB  . MET A 191 ? 0.446 0.599 0.368 -0.070 0.015  -0.035 187 MET A CB  
1302 C CG  . MET A 191 ? 0.443 0.598 0.370 -0.062 0.015  -0.032 187 MET A CG  
1303 S SD  . MET A 191 ? 0.468 0.646 0.401 -0.061 0.013  -0.029 187 MET A SD  
1304 C CE  . MET A 191 ? 0.516 0.691 0.453 -0.050 0.012  -0.025 187 MET A CE  
1305 N N   . LEU A 192 ? 0.519 0.652 0.426 -0.077 0.018  -0.040 188 LEU A N   
1306 C CA  . LEU A 192 ? 0.548 0.678 0.447 -0.084 0.019  -0.043 188 LEU A CA  
1307 C C   . LEU A 192 ? 0.551 0.659 0.440 -0.086 0.024  -0.045 188 LEU A C   
1308 O O   . LEU A 192 ? 0.560 0.662 0.439 -0.094 0.026  -0.048 188 LEU A O   
1309 C CB  . LEU A 192 ? 0.609 0.743 0.511 -0.080 0.018  -0.041 188 LEU A CB  
1310 C CG  . LEU A 192 ? 0.688 0.842 0.594 -0.082 0.015  -0.040 188 LEU A CG  
1311 C CD1 . LEU A 192 ? 0.699 0.857 0.610 -0.075 0.012  -0.038 188 LEU A CD1 
1312 C CD2 . LEU A 192 ? 0.718 0.875 0.616 -0.094 0.015  -0.044 188 LEU A CD2 
1313 N N   . PHE A 193 ? 0.566 0.663 0.457 -0.078 0.024  -0.043 189 PHE A N   
1314 C CA  . PHE A 193 ? 0.587 0.665 0.468 -0.077 0.029  -0.044 189 PHE A CA  
1315 C C   . PHE A 193 ? 0.596 0.666 0.471 -0.082 0.031  -0.046 189 PHE A C   
1316 O O   . PHE A 193 ? 0.613 0.665 0.475 -0.084 0.036  -0.047 189 PHE A O   
1317 C CB  . PHE A 193 ? 0.586 0.658 0.472 -0.067 0.028  -0.041 189 PHE A CB  
1318 C CG  . PHE A 193 ? 0.583 0.658 0.473 -0.062 0.027  -0.039 189 PHE A CG  
1319 C CD1 . PHE A 193 ? 0.591 0.668 0.478 -0.066 0.027  -0.041 189 PHE A CD1 
1320 C CD2 . PHE A 193 ? 0.546 0.623 0.445 -0.054 0.025  -0.036 189 PHE A CD2 
1321 C CE1 . PHE A 193 ? 0.571 0.649 0.462 -0.061 0.026  -0.039 189 PHE A CE1 
1322 C CE2 . PHE A 193 ? 0.528 0.607 0.430 -0.050 0.024  -0.035 189 PHE A CE2 
1323 C CZ  . PHE A 193 ? 0.553 0.633 0.452 -0.053 0.024  -0.036 189 PHE A CZ  
1324 N N   . SER A 194 ? 0.588 0.670 0.470 -0.083 0.029  -0.045 190 SER A N   
1325 C CA  . SER A 194 ? 0.624 0.701 0.501 -0.088 0.032  -0.046 190 SER A CA  
1326 C C   . SER A 194 ? 0.671 0.745 0.537 -0.100 0.035  -0.050 190 SER A C   
1327 O O   . SER A 194 ? 0.679 0.739 0.534 -0.104 0.039  -0.052 190 SER A O   
1328 C CB  . SER A 194 ? 0.565 0.656 0.451 -0.086 0.029  -0.044 190 SER A CB  
1329 O OG  . SER A 194 ? 0.537 0.646 0.427 -0.092 0.027  -0.045 190 SER A OG  
1330 N N   . MET A 195 ? 0.728 0.814 0.595 -0.105 0.033  -0.051 191 MET A N   
1331 C CA  . MET A 195 ? 0.774 0.859 0.629 -0.117 0.035  -0.055 191 MET A CA  
1332 C C   . MET A 195 ? 0.841 0.905 0.682 -0.119 0.039  -0.057 191 MET A C   
1333 O O   . MET A 195 ? 0.880 0.946 0.715 -0.125 0.039  -0.059 191 MET A O   
1334 C CB  . MET A 195 ? 0.783 0.891 0.646 -0.121 0.030  -0.054 191 MET A CB  
1335 C CG  . MET A 195 ? 0.786 0.917 0.663 -0.118 0.026  -0.051 191 MET A CG  
1336 S SD  . MET A 195 ? 0.870 1.030 0.756 -0.120 0.021  -0.050 191 MET A SD  
1337 C CE  . MET A 195 ? 0.909 1.064 0.781 -0.133 0.023  -0.054 191 MET A CE  
1338 N N   . ASP A 196 ? 0.940 0.982 0.774 -0.113 0.043  -0.057 192 ASP A N   
1339 C CA  . ASP A 196 ? 0.985 1.006 0.806 -0.111 0.048  -0.057 192 ASP A CA  
1340 C C   . ASP A 196 ? 0.999 1.029 0.828 -0.105 0.044  -0.056 192 ASP A C   
1341 O O   . ASP A 196 ? 0.967 0.993 0.800 -0.095 0.044  -0.053 192 ASP A O   
1342 C CB  . ASP A 196 ? 1.035 1.042 0.837 -0.123 0.053  -0.062 192 ASP A CB  
1343 C CG  . ASP A 196 ? 1.084 1.076 0.874 -0.129 0.058  -0.064 192 ASP A CG  
1344 O OD1 . ASP A 196 ? 1.026 1.024 0.824 -0.126 0.056  -0.062 192 ASP A OD1 
1345 O OD2 . ASP A 196 ? 1.112 1.086 0.883 -0.138 0.063  -0.068 192 ASP A OD2 
1346 N N   . ASP B 31  ? 1.258 1.560 1.123 0.011  0.032  -0.036 27  ASP B N   
1347 C CA  . ASP B 31  ? 1.276 1.570 1.142 -0.003 0.029  -0.034 27  ASP B CA  
1348 C C   . ASP B 31  ? 1.335 1.647 1.209 -0.008 0.030  -0.032 27  ASP B C   
1349 O O   . ASP B 31  ? 1.305 1.610 1.179 -0.020 0.028  -0.030 27  ASP B O   
1350 C CB  . ASP B 31  ? 1.196 1.490 1.054 -0.013 0.031  -0.032 27  ASP B CB  
1351 N N   . HIS B 32  ? 1.458 1.791 1.339 0.001  0.032  -0.033 28  HIS B N   
1352 C CA  . HIS B 32  ? 1.543 1.893 1.432 -0.003 0.032  -0.032 28  HIS B CA  
1353 C C   . HIS B 32  ? 1.517 1.867 1.412 0.010  0.030  -0.034 28  HIS B C   
1354 O O   . HIS B 32  ? 1.357 1.719 1.260 0.008  0.030  -0.033 28  HIS B O   
1355 C CB  . HIS B 32  ? 1.569 1.952 1.461 -0.008 0.036  -0.030 28  HIS B CB  
1356 C CG  . HIS B 32  ? 1.574 1.967 1.469 -0.023 0.035  -0.027 28  HIS B CG  
1357 N ND1 . HIS B 32  ? 1.524 1.941 1.419 -0.034 0.037  -0.025 28  HIS B ND1 
1358 C CD2 . HIS B 32  ? 1.530 1.911 1.427 -0.030 0.031  -0.026 28  HIS B CD2 
1359 C CE1 . HIS B 32  ? 1.491 1.910 1.386 -0.047 0.035  -0.022 28  HIS B CE1 
1360 N NE2 . HIS B 32  ? 1.522 1.919 1.419 -0.044 0.032  -0.023 28  HIS B NE2 
1361 N N   . ALA B 33  ? 1.470 1.805 1.361 0.023  0.030  -0.037 29  ALA B N   
1362 C CA  . ALA B 33  ? 1.339 1.664 1.232 0.035  0.028  -0.039 29  ALA B CA  
1363 C C   . ALA B 33  ? 1.273 1.573 1.167 0.029  0.023  -0.039 29  ALA B C   
1364 O O   . ALA B 33  ? 1.126 1.417 1.022 0.036  0.021  -0.040 29  ALA B O   
1365 C CB  . ALA B 33  ? 1.272 1.587 1.156 0.047  0.028  -0.042 29  ALA B CB  
1366 N N   . ASP B 34  ? 1.236 1.525 1.126 0.018  0.022  -0.037 30  ASP B N   
1367 C CA  . ASP B 34  ? 1.166 1.434 1.057 0.011  0.019  -0.036 30  ASP B CA  
1368 C C   . ASP B 34  ? 1.202 1.478 1.099 0.004  0.018  -0.034 30  ASP B C   
1369 O O   . ASP B 34  ? 1.192 1.456 1.092 0.007  0.016  -0.035 30  ASP B O   
1370 C CB  . ASP B 34  ? 1.046 1.303 0.930 0.002  0.018  -0.034 30  ASP B CB  
1371 C CG  . ASP B 34  ? 0.970 1.213 0.847 0.007  0.018  -0.036 30  ASP B CG  
1372 O OD1 . ASP B 34  ? 0.879 1.117 0.755 0.018  0.018  -0.038 30  ASP B OD1 
1373 O OD2 . ASP B 34  ? 0.902 1.139 0.773 0.000  0.018  -0.035 30  ASP B OD2 
1374 N N   . ALA B 35  ? 1.239 1.532 1.137 -0.006 0.020  -0.032 31  ALA B N   
1375 C CA  . ALA B 35  ? 1.276 1.577 1.179 -0.014 0.019  -0.030 31  ALA B CA  
1376 C C   . ALA B 35  ? 1.271 1.581 1.181 -0.004 0.019  -0.032 31  ALA B C   
1377 O O   . ALA B 35  ? 1.197 1.505 1.110 -0.009 0.017  -0.031 31  ALA B O   
1378 C CB  . ALA B 35  ? 1.225 1.547 1.126 -0.024 0.021  -0.028 31  ALA B CB  
1379 N N   . ALA B 36  ? 1.289 1.605 1.200 0.008  0.020  -0.034 32  ALA B N   
1380 C CA  . ALA B 36  ? 1.263 1.586 1.179 0.020  0.020  -0.036 32  ALA B CA  
1381 C C   . ALA B 36  ? 1.312 1.609 1.227 0.025  0.017  -0.037 32  ALA B C   
1382 O O   . ALA B 36  ? 1.392 1.688 1.311 0.025  0.015  -0.037 32  ALA B O   
1383 C CB  . ALA B 36  ? 1.259 1.597 1.173 0.031  0.023  -0.037 32  ALA B CB  
1384 N N   . TYR B 37  ? 1.263 1.540 1.171 0.029  0.016  -0.038 33  TYR B N   
1385 C CA  . TYR B 37  ? 1.158 1.411 1.064 0.034  0.012  -0.040 33  TYR B CA  
1386 C C   . TYR B 37  ? 1.084 1.326 0.994 0.025  0.010  -0.038 33  TYR B C   
1387 O O   . TYR B 37  ? 0.946 1.175 0.857 0.029  0.008  -0.039 33  TYR B O   
1388 C CB  . TYR B 37  ? 1.171 1.407 1.069 0.036  0.012  -0.040 33  TYR B CB  
1389 C CG  . TYR B 37  ? 1.217 1.432 1.113 0.040  0.008  -0.042 33  TYR B CG  
1390 C CD1 . TYR B 37  ? 1.269 1.479 1.162 0.051  0.008  -0.044 33  TYR B CD1 
1391 C CD2 . TYR B 37  ? 1.236 1.434 1.132 0.033  0.006  -0.040 33  TYR B CD2 
1392 C CE1 . TYR B 37  ? 1.302 1.492 1.191 0.053  0.005  -0.044 33  TYR B CE1 
1393 C CE2 . TYR B 37  ? 1.294 1.474 1.188 0.037  0.003  -0.041 33  TYR B CE2 
1394 C CZ  . TYR B 37  ? 1.355 1.531 1.246 0.046  0.002  -0.043 33  TYR B CZ  
1395 O OH  . TYR B 37  ? 1.368 1.526 1.255 0.048  -0.001 -0.043 33  TYR B OH  
1396 N N   . VAL B 38  ? 1.074 1.320 0.984 0.014  0.010  -0.036 34  VAL B N   
1397 C CA  . VAL B 38  ? 1.037 1.272 0.948 0.006  0.008  -0.034 34  VAL B CA  
1398 C C   . VAL B 38  ? 1.064 1.309 0.980 0.004  0.008  -0.033 34  VAL B C   
1399 O O   . VAL B 38  ? 1.071 1.303 0.989 0.004  0.006  -0.033 34  VAL B O   
1400 C CB  . VAL B 38  ? 0.990 1.224 0.896 -0.005 0.009  -0.032 34  VAL B CB  
1401 C CG1 . VAL B 38  ? 0.977 1.208 0.882 -0.015 0.008  -0.030 34  VAL B CG1 
1402 C CG2 . VAL B 38  ? 0.964 1.179 0.864 -0.004 0.008  -0.032 34  VAL B CG2 
1403 N N   . GLU B 39  ? 1.155 1.424 1.075 0.004  0.010  -0.033 35  GLU B N   
1404 C CA  . GLU B 39  ? 1.146 1.426 1.071 0.003  0.010  -0.033 35  GLU B CA  
1405 C C   . GLU B 39  ? 1.043 1.320 0.971 0.016  0.009  -0.035 35  GLU B C   
1406 O O   . GLU B 39  ? 1.016 1.285 0.946 0.016  0.007  -0.035 35  GLU B O   
1407 C CB  . GLU B 39  ? 1.146 1.454 1.074 -0.001 0.012  -0.031 35  GLU B CB  
1408 C CG  . GLU B 39  ? 1.131 1.447 1.060 -0.012 0.011  -0.029 35  GLU B CG  
1409 C CD  . GLU B 39  ? 1.150 1.498 1.083 -0.015 0.013  -0.028 35  GLU B CD  
1410 O OE1 . GLU B 39  ? 1.119 1.478 1.049 -0.018 0.016  -0.027 35  GLU B OE1 
1411 O OE2 . GLU B 39  ? 1.089 1.449 1.027 -0.013 0.013  -0.028 35  GLU B OE2 
1412 N N   . LYS B 40  ? 0.980 1.261 0.906 0.025  0.010  -0.037 36  LYS B N   
1413 C CA  . LYS B 40  ? 1.039 1.315 0.964 0.038  0.010  -0.039 36  LYS B CA  
1414 C C   . LYS B 40  ? 1.026 1.277 0.950 0.040  0.007  -0.040 36  LYS B C   
1415 O O   . LYS B 40  ? 1.063 1.309 0.985 0.049  0.006  -0.042 36  LYS B O   
1416 C CB  . LYS B 40  ? 1.100 1.379 1.020 0.047  0.011  -0.041 36  LYS B CB  
1417 C CG  . LYS B 40  ? 1.128 1.398 1.043 0.061  0.011  -0.044 36  LYS B CG  
1418 C CD  . LYS B 40  ? 1.165 1.455 1.081 0.071  0.012  -0.045 36  LYS B CD  
1419 C CE  . LYS B 40  ? 1.127 1.409 1.044 0.076  0.010  -0.046 36  LYS B CE  
1420 N NZ  . LYS B 40  ? 1.097 1.402 1.017 0.085  0.011  -0.046 36  LYS B NZ  
1421 N N   . HIS B 41  ? 1.004 1.241 0.927 0.032  0.005  -0.038 37  HIS B N   
1422 C CA  . HIS B 41  ? 0.954 1.168 0.875 0.033  0.003  -0.039 37  HIS B CA  
1423 C C   . HIS B 41  ? 0.883 1.090 0.807 0.024  0.002  -0.037 37  HIS B C   
1424 O O   . HIS B 41  ? 0.866 1.057 0.789 0.024  -0.000 -0.036 37  HIS B O   
1425 C CB  . HIS B 41  ? 1.005 1.206 0.920 0.034  0.002  -0.039 37  HIS B CB  
1426 C CG  . HIS B 41  ? 1.032 1.231 0.942 0.044  0.002  -0.042 37  HIS B CG  
1427 N ND1 . HIS B 41  ? 1.061 1.242 0.966 0.049  0.000  -0.043 37  HIS B ND1 
1428 C CD2 . HIS B 41  ? 1.026 1.237 0.933 0.050  0.005  -0.043 37  HIS B CD2 
1429 C CE1 . HIS B 41  ? 1.053 1.234 0.952 0.057  0.000  -0.044 37  HIS B CE1 
1430 N NE2 . HIS B 41  ? 1.028 1.226 0.927 0.059  0.003  -0.045 37  HIS B NE2 
1431 N N   . ASN B 42  ? 0.873 1.091 0.799 0.017  0.003  -0.035 38  ASN B N   
1432 C CA  . ASN B 42  ? 0.864 1.074 0.791 0.010  0.001  -0.033 38  ASN B CA  
1433 C C   . ASN B 42  ? 0.857 1.052 0.779 0.004  0.001  -0.032 38  ASN B C   
1434 O O   . ASN B 42  ? 0.874 1.055 0.796 0.003  -0.001 -0.031 38  ASN B O   
1435 C CB  . ASN B 42  ? 0.861 1.063 0.790 0.014  -0.000 -0.034 38  ASN B CB  
1436 C CG  . ASN B 42  ? 0.829 1.044 0.762 0.013  0.000  -0.033 38  ASN B CG  
1437 O OD1 . ASN B 42  ? 0.869 1.096 0.805 0.019  0.001  -0.035 38  ASN B OD1 
1438 N ND2 . ASN B 42  ? 0.812 1.026 0.744 0.004  -0.000 -0.032 38  ASN B ND2 
1439 N N   . LEU B 43  ? 0.818 1.015 0.737 0.003  0.002  -0.032 39  LEU B N   
1440 C CA  . LEU B 43  ? 0.766 0.950 0.680 -0.002 0.001  -0.031 39  LEU B CA  
1441 C C   . LEU B 43  ? 0.747 0.936 0.656 -0.012 0.002  -0.029 39  LEU B C   
1442 O O   . LEU B 43  ? 0.754 0.931 0.657 -0.016 0.001  -0.028 39  LEU B O   
1443 C CB  . LEU B 43  ? 0.769 0.951 0.681 0.004  0.001  -0.032 39  LEU B CB  
1444 C CG  . LEU B 43  ? 0.764 0.936 0.678 0.011  -0.001 -0.033 39  LEU B CG  
1445 C CD1 . LEU B 43  ? 0.757 0.931 0.668 0.018  -0.000 -0.035 39  LEU B CD1 
1446 C CD2 . LEU B 43  ? 0.817 0.973 0.729 0.009  -0.003 -0.032 39  LEU B CD2 
1447 N N   . GLN B 44  ? 0.756 0.960 0.667 -0.015 0.003  -0.029 40  GLN B N   
1448 C CA  . GLN B 44  ? 0.832 1.042 0.738 -0.026 0.003  -0.027 40  GLN B CA  
1449 C C   . GLN B 44  ? 0.809 1.001 0.709 -0.032 0.001  -0.025 40  GLN B C   
1450 O O   . GLN B 44  ? 0.859 1.045 0.750 -0.040 0.001  -0.023 40  GLN B O   
1451 C CB  . GLN B 44  ? 0.927 1.161 0.838 -0.028 0.005  -0.026 40  GLN B CB  
1452 C CG  . GLN B 44  ? 1.022 1.265 0.927 -0.040 0.005  -0.024 40  GLN B CG  
1453 C CD  . GLN B 44  ? 1.145 1.380 1.041 -0.046 0.006  -0.023 40  GLN B CD  
1454 O OE1 . GLN B 44  ? 1.130 1.371 1.028 -0.041 0.007  -0.024 40  GLN B OE1 
1455 N NE2 . GLN B 44  ? 1.131 1.352 1.018 -0.056 0.004  -0.021 40  GLN B NE2 
1456 N N   . CYS B 45  ? 0.786 0.968 0.688 -0.027 0.000  -0.025 41  CYS B N   
1457 C CA  . CYS B 45  ? 0.772 0.936 0.668 -0.032 -0.002 -0.024 41  CYS B CA  
1458 C C   . CYS B 45  ? 0.688 0.836 0.578 -0.031 -0.002 -0.023 41  CYS B C   
1459 O O   . CYS B 45  ? 0.607 0.744 0.486 -0.038 -0.003 -0.021 41  CYS B O   
1460 C CB  . CYS B 45  ? 0.787 0.947 0.688 -0.026 -0.002 -0.024 41  CYS B CB  
1461 S SG  . CYS B 45  ? 0.936 1.075 0.828 -0.030 -0.004 -0.022 41  CYS B SG  
1462 N N   . LEU B 46  ? 0.636 0.782 0.531 -0.023 -0.003 -0.024 42  LEU B N   
1463 C CA  . LEU B 46  ? 0.614 0.747 0.504 -0.022 -0.004 -0.024 42  LEU B CA  
1464 C C   . LEU B 46  ? 0.604 0.737 0.485 -0.029 -0.003 -0.023 42  LEU B C   
1465 O O   . LEU B 46  ? 0.563 0.682 0.436 -0.033 -0.004 -0.021 42  LEU B O   
1466 C CB  . LEU B 46  ? 0.571 0.705 0.468 -0.014 -0.004 -0.025 42  LEU B CB  
1467 C CG  . LEU B 46  ? 0.533 0.656 0.426 -0.012 -0.005 -0.025 42  LEU B CG  
1468 C CD1 . LEU B 46  ? 0.506 0.615 0.396 -0.013 -0.007 -0.023 42  LEU B CD1 
1469 C CD2 . LEU B 46  ? 0.513 0.637 0.412 -0.005 -0.006 -0.026 42  LEU B CD2 
1470 N N   . PHE B 47  ? 0.565 0.714 0.450 -0.030 -0.001 -0.024 43  PHE B N   
1471 C CA  . PHE B 47  ? 0.581 0.732 0.458 -0.037 -0.000 -0.023 43  PHE B CA  
1472 C C   . PHE B 47  ? 0.582 0.728 0.449 -0.047 -0.001 -0.021 43  PHE B C   
1473 O O   . PHE B 47  ? 0.570 0.706 0.427 -0.053 -0.002 -0.020 43  PHE B O   
1474 C CB  . PHE B 47  ? 0.557 0.729 0.440 -0.035 0.002  -0.024 43  PHE B CB  
1475 C CG  . PHE B 47  ? 0.568 0.738 0.453 -0.027 0.002  -0.026 43  PHE B CG  
1476 C CD1 . PHE B 47  ? 0.592 0.761 0.471 -0.029 0.003  -0.026 43  PHE B CD1 
1477 C CD2 . PHE B 47  ? 0.564 0.731 0.455 -0.018 0.001  -0.028 43  PHE B CD2 
1478 C CE1 . PHE B 47  ? 0.595 0.762 0.476 -0.023 0.003  -0.027 43  PHE B CE1 
1479 C CE2 . PHE B 47  ? 0.580 0.744 0.472 -0.012 0.001  -0.029 43  PHE B CE2 
1480 C CZ  . PHE B 47  ? 0.604 0.767 0.490 -0.014 0.002  -0.029 43  PHE B CZ  
1481 N N   . SER B 48  ? 0.594 0.746 0.464 -0.050 -0.001 -0.021 44  SER B N   
1482 C CA  . SER B 48  ? 0.616 0.762 0.475 -0.060 -0.002 -0.018 44  SER B CA  
1483 C C   . SER B 48  ? 0.611 0.731 0.459 -0.060 -0.004 -0.017 44  SER B C   
1484 O O   . SER B 48  ? 0.551 0.661 0.386 -0.068 -0.005 -0.016 44  SER B O   
1485 C CB  . SER B 48  ? 0.630 0.789 0.494 -0.063 -0.001 -0.018 44  SER B CB  
1486 O OG  . SER B 48  ? 0.657 0.808 0.510 -0.074 -0.003 -0.016 44  SER B OG  
1487 N N   . GLU B 49  ? 0.631 0.742 0.485 -0.051 -0.005 -0.018 45  GLU B N   
1488 C CA  . GLU B 49  ? 0.666 0.755 0.510 -0.050 -0.007 -0.017 45  GLU B CA  
1489 C C   . GLU B 49  ? 0.641 0.721 0.477 -0.050 -0.007 -0.017 45  GLU B C   
1490 O O   . GLU B 49  ? 0.618 0.679 0.440 -0.053 -0.009 -0.015 45  GLU B O   
1491 C CB  . GLU B 49  ? 0.713 0.798 0.565 -0.040 -0.007 -0.018 45  GLU B CB  
1492 C CG  . GLU B 49  ? 0.722 0.820 0.586 -0.037 -0.006 -0.019 45  GLU B CG  
1493 C CD  . GLU B 49  ? 0.731 0.821 0.599 -0.030 -0.007 -0.019 45  GLU B CD  
1494 O OE1 . GLU B 49  ? 0.724 0.822 0.604 -0.023 -0.006 -0.020 45  GLU B OE1 
1495 O OE2 . GLU B 49  ? 0.725 0.800 0.584 -0.030 -0.008 -0.018 45  GLU B OE2 
1496 N N   . MET B 50  ? 0.625 0.716 0.469 -0.047 -0.006 -0.018 46  MET B N   
1497 C CA  . MET B 50  ? 0.635 0.717 0.472 -0.047 -0.007 -0.017 46  MET B CA  
1498 C C   . MET B 50  ? 0.646 0.725 0.469 -0.058 -0.007 -0.016 46  MET B C   
1499 O O   . MET B 50  ? 0.644 0.704 0.452 -0.061 -0.008 -0.014 46  MET B O   
1500 C CB  . MET B 50  ? 0.592 0.686 0.439 -0.041 -0.006 -0.019 46  MET B CB  
1501 C CG  . MET B 50  ? 0.547 0.638 0.403 -0.032 -0.007 -0.020 46  MET B CG  
1502 S SD  . MET B 50  ? 0.525 0.621 0.387 -0.026 -0.007 -0.021 46  MET B SD  
1503 C CE  . MET B 50  ? 0.510 0.627 0.381 -0.025 -0.004 -0.023 46  MET B CE  
1504 N N   . ALA B 51  ? 0.644 0.740 0.470 -0.065 -0.005 -0.016 47  ALA B N   
1505 C CA  . ALA B 51  ? 0.661 0.757 0.474 -0.077 -0.005 -0.014 47  ALA B CA  
1506 C C   . ALA B 51  ? 0.698 0.772 0.495 -0.083 -0.007 -0.012 47  ALA B C   
1507 O O   . ALA B 51  ? 0.698 0.755 0.479 -0.089 -0.008 -0.011 47  ALA B O   
1508 C CB  . ALA B 51  ? 0.641 0.761 0.461 -0.082 -0.002 -0.015 47  ALA B CB  
1509 N N   . GLU B 52  ? 0.776 0.849 0.578 -0.080 -0.007 -0.013 48  GLU B N   
1510 C CA  . GLU B 52  ? 0.863 0.916 0.650 -0.084 -0.009 -0.011 48  GLU B CA  
1511 C C   . GLU B 52  ? 0.832 0.860 0.606 -0.080 -0.011 -0.010 48  GLU B C   
1512 O O   . GLU B 52  ? 0.893 0.903 0.647 -0.087 -0.013 -0.009 48  GLU B O   
1513 C CB  . GLU B 52  ? 0.962 1.018 0.757 -0.080 -0.009 -0.012 48  GLU B CB  
1514 C CG  . GLU B 52  ? 1.057 1.098 0.836 -0.088 -0.011 -0.010 48  GLU B CG  
1515 C CD  . GLU B 52  ? 1.170 1.183 0.933 -0.085 -0.013 -0.009 48  GLU B CD  
1516 O OE1 . GLU B 52  ? 1.190 1.197 0.958 -0.076 -0.013 -0.009 48  GLU B OE1 
1517 O OE2 . GLU B 52  ? 1.194 1.188 0.937 -0.091 -0.015 -0.007 48  GLU B OE2 
1518 N N   . GLN B 53  ? 0.781 0.810 0.566 -0.068 -0.011 -0.012 49  GLN B N   
1519 C CA  . GLN B 53  ? 0.790 0.798 0.565 -0.062 -0.013 -0.011 49  GLN B CA  
1520 C C   . GLN B 53  ? 0.783 0.781 0.543 -0.068 -0.014 -0.010 49  GLN B C   
1521 O O   . GLN B 53  ? 0.743 0.718 0.486 -0.067 -0.016 -0.009 49  GLN B O   
1522 C CB  . GLN B 53  ? 0.779 0.794 0.570 -0.049 -0.013 -0.012 49  GLN B CB  
1523 C CG  . GLN B 53  ? 0.810 0.810 0.595 -0.042 -0.015 -0.012 49  GLN B CG  
1524 C CD  . GLN B 53  ? 0.822 0.804 0.597 -0.038 -0.016 -0.010 49  GLN B CD  
1525 O OE1 . GLN B 53  ? 0.849 0.830 0.623 -0.040 -0.015 -0.010 49  GLN B OE1 
1526 N NE2 . GLN B 53  ? 0.821 0.788 0.586 -0.032 -0.018 -0.009 49  GLN B NE2 
1527 N N   . LEU B 54  ? 0.767 0.780 0.531 -0.074 -0.012 -0.010 50  LEU B N   
1528 C CA  . LEU B 54  ? 0.805 0.810 0.555 -0.081 -0.013 -0.009 50  LEU B CA  
1529 C C   . LEU B 54  ? 0.876 0.869 0.606 -0.094 -0.014 -0.007 50  LEU B C   
1530 O O   . LEU B 54  ? 0.904 0.876 0.615 -0.098 -0.016 -0.006 50  LEU B O   
1531 C CB  . LEU B 54  ? 0.746 0.774 0.510 -0.082 -0.011 -0.011 50  LEU B CB  
1532 C CG  . LEU B 54  ? 0.674 0.709 0.453 -0.070 -0.010 -0.012 50  LEU B CG  
1533 C CD1 . LEU B 54  ? 0.632 0.686 0.421 -0.070 -0.008 -0.014 50  LEU B CD1 
1534 C CD2 . LEU B 54  ? 0.653 0.668 0.422 -0.064 -0.013 -0.012 50  LEU B CD2 
1535 N N   . SER B 55  ? 0.911 0.912 0.643 -0.101 -0.013 -0.007 51  SER B N   
1536 C CA  . SER B 55  ? 0.931 0.918 0.641 -0.114 -0.015 -0.005 51  SER B CA  
1537 C C   . SER B 55  ? 0.931 0.886 0.622 -0.111 -0.018 -0.004 51  SER B C   
1538 O O   . SER B 55  ? 0.954 0.889 0.622 -0.120 -0.019 -0.002 51  SER B O   
1539 C CB  . SER B 55  ? 0.917 0.921 0.635 -0.121 -0.014 -0.005 51  SER B CB  
1540 O OG  . SER B 55  ? 0.923 0.957 0.659 -0.122 -0.011 -0.006 51  SER B OG  
1541 N N   . GLU B 56  ? 0.976 0.927 0.675 -0.098 -0.018 -0.005 52  GLU B N   
1542 C CA  . GLU B 56  ? 1.074 0.996 0.755 -0.093 -0.020 -0.004 52  GLU B CA  
1543 C C   . GLU B 56  ? 1.068 0.969 0.735 -0.089 -0.022 -0.003 52  GLU B C   
1544 O O   . GLU B 56  ? 1.093 0.967 0.737 -0.089 -0.024 -0.002 52  GLU B O   
1545 C CB  . GLU B 56  ? 1.102 1.030 0.799 -0.081 -0.020 -0.005 52  GLU B CB  
1546 C CG  . GLU B 56  ? 1.166 1.068 0.846 -0.076 -0.021 -0.004 52  GLU B CG  
1547 C CD  . GLU B 56  ? 1.212 1.124 0.905 -0.072 -0.020 -0.005 52  GLU B CD  
1548 O OE1 . GLU B 56  ? 1.194 1.130 0.907 -0.074 -0.018 -0.006 52  GLU B OE1 
1549 O OE2 . GLU B 56  ? 1.266 1.159 0.947 -0.066 -0.021 -0.004 52  GLU B OE2 
1550 N N   . LYS B 57  ? 1.091 1.004 0.770 -0.084 -0.021 -0.004 53  LYS B N   
1551 C CA  . LYS B 57  ? 1.101 0.998 0.770 -0.076 -0.023 -0.004 53  LYS B CA  
1552 C C   . LYS B 57  ? 1.085 0.977 0.741 -0.087 -0.023 -0.003 53  LYS B C   
1553 O O   . LYS B 57  ? 1.037 0.908 0.676 -0.084 -0.026 -0.002 53  LYS B O   
1554 C CB  . LYS B 57  ? 1.095 1.008 0.787 -0.063 -0.022 -0.005 53  LYS B CB  
1555 C CG  . LYS B 57  ? 1.064 0.977 0.765 -0.052 -0.022 -0.006 53  LYS B CG  
1556 C CD  . LYS B 57  ? 1.070 0.983 0.779 -0.039 -0.023 -0.006 53  LYS B CD  
1557 C CE  . LYS B 57  ? 1.074 0.985 0.789 -0.027 -0.023 -0.006 53  LYS B CE  
1558 N NZ  . LYS B 57  ? 1.111 0.997 0.804 -0.027 -0.025 -0.005 53  LYS B NZ  
1559 N N   . ASP B 58  ? 1.079 0.992 0.743 -0.097 -0.021 -0.003 54  ASP B N   
1560 C CA  . ASP B 58  ? 1.154 1.068 0.808 -0.110 -0.021 -0.003 54  ASP B CA  
1561 C C   . ASP B 58  ? 1.151 1.057 0.801 -0.105 -0.022 -0.003 54  ASP B C   
1562 O O   . ASP B 58  ? 1.126 1.008 0.752 -0.108 -0.024 -0.001 54  ASP B O   
1563 C CB  . ASP B 58  ? 1.198 1.092 0.825 -0.124 -0.023 -0.000 54  ASP B CB  
1564 C CG  . ASP B 58  ? 1.286 1.185 0.904 -0.138 -0.022 0.001  54  ASP B CG  
1565 O OD1 . ASP B 58  ? 1.288 1.216 0.925 -0.141 -0.019 -0.000 54  ASP B OD1 
1566 O OD2 . ASP B 58  ? 1.370 1.243 0.960 -0.147 -0.024 0.003  54  ASP B OD2 
1567 N N   . PRO B 59  ? 1.071 0.997 0.742 -0.097 -0.020 -0.004 55  PRO B N   
1568 C CA  . PRO B 59  ? 1.013 0.934 0.682 -0.091 -0.021 -0.005 55  PRO B CA  
1569 C C   . PRO B 59  ? 0.955 0.874 0.612 -0.103 -0.021 -0.004 55  PRO B C   
1570 O O   . PRO B 59  ? 0.890 0.826 0.551 -0.113 -0.018 -0.004 55  PRO B O   
1571 C CB  . PRO B 59  ? 0.992 0.937 0.687 -0.082 -0.019 -0.007 55  PRO B CB  
1572 C CG  . PRO B 59  ? 1.011 0.979 0.720 -0.088 -0.016 -0.007 55  PRO B CG  
1573 C CD  . PRO B 59  ? 1.034 0.989 0.730 -0.094 -0.017 -0.006 55  PRO B CD  
1574 N N   . LYS B 60  ? 0.991 0.893 0.634 -0.101 -0.023 -0.003 56  LYS B N   
1575 C CA  . LYS B 60  ? 0.980 0.875 0.607 -0.111 -0.023 -0.002 56  LYS B CA  
1576 C C   . LYS B 60  ? 0.891 0.810 0.535 -0.111 -0.020 -0.004 56  LYS B C   
1577 O O   . LYS B 60  ? 0.949 0.871 0.584 -0.123 -0.019 -0.003 56  LYS B O   
1578 C CB  . LYS B 60  ? 1.040 0.905 0.646 -0.107 -0.027 -0.001 56  LYS B CB  
1579 C CG  . LYS B 60  ? 1.094 0.932 0.679 -0.107 -0.030 0.000  56  LYS B CG  
1580 C CD  . LYS B 60  ? 1.180 0.996 0.755 -0.093 -0.033 0.000  56  LYS B CD  
1581 C CE  . LYS B 60  ? 1.270 1.068 0.834 -0.087 -0.035 0.001  56  LYS B CE  
1582 N NZ  . LYS B 60  ? 1.372 1.134 0.903 -0.088 -0.039 0.003  56  LYS B NZ  
1583 N N   . THR B 61  ? 0.805 0.740 0.471 -0.100 -0.019 -0.006 57  THR B N   
1584 C CA  . THR B 61  ? 0.723 0.677 0.404 -0.096 -0.017 -0.007 57  THR B CA  
1585 C C   . THR B 61  ? 0.677 0.655 0.383 -0.089 -0.015 -0.009 57  THR B C   
1586 O O   . THR B 61  ? 0.669 0.645 0.382 -0.083 -0.016 -0.009 57  THR B O   
1587 C CB  . THR B 61  ? 0.703 0.646 0.382 -0.088 -0.020 -0.007 57  THR B CB  
1588 O OG1 . THR B 61  ? 0.647 0.595 0.342 -0.075 -0.021 -0.008 57  THR B OG1 
1589 C CG2 . THR B 61  ? 0.728 0.642 0.382 -0.089 -0.023 -0.005 57  THR B CG2 
1590 N N   . GLU B 62  ? 0.616 0.613 0.335 -0.087 -0.013 -0.010 58  GLU B N   
1591 C CA  A GLU B 62  ? 0.590 0.606 0.330 -0.079 -0.011 -0.012 58  GLU B CA  
1592 C CA  B GLU B 62  ? 0.590 0.606 0.330 -0.079 -0.011 -0.012 58  GLU B CA  
1593 C C   . GLU B 62  ? 0.602 0.609 0.348 -0.067 -0.014 -0.013 58  GLU B C   
1594 O O   . GLU B 62  ? 0.600 0.615 0.360 -0.060 -0.014 -0.014 58  GLU B O   
1595 C CB  A GLU B 62  ? 0.570 0.606 0.319 -0.079 -0.008 -0.014 58  GLU B CB  
1596 C CB  B GLU B 62  ? 0.569 0.605 0.320 -0.078 -0.008 -0.014 58  GLU B CB  
1597 C CG  A GLU B 62  ? 0.563 0.614 0.310 -0.090 -0.004 -0.013 58  GLU B CG  
1598 C CG  B GLU B 62  ? 0.539 0.594 0.309 -0.071 -0.006 -0.016 58  GLU B CG  
1599 C CD  A GLU B 62  ? 0.570 0.616 0.301 -0.100 -0.004 -0.012 58  GLU B CD  
1600 C CD  B GLU B 62  ? 0.518 0.573 0.299 -0.059 -0.008 -0.017 58  GLU B CD  
1601 O OE1 A GLU B 62  ? 0.556 0.580 0.272 -0.103 -0.007 -0.011 58  GLU B OE1 
1602 O OE1 B GLU B 62  ? 0.518 0.558 0.295 -0.055 -0.011 -0.017 58  GLU B OE1 
1603 O OE2 A GLU B 62  ? 0.577 0.642 0.311 -0.106 -0.000 -0.012 58  GLU B OE2 
1604 O OE2 B GLU B 62  ? 0.490 0.560 0.283 -0.054 -0.006 -0.019 58  GLU B OE2 
1605 N N   . GLN B 63  ? 0.600 0.592 0.337 -0.064 -0.017 -0.012 59  GLN B N   
1606 C CA  . GLN B 63  ? 0.593 0.578 0.337 -0.053 -0.020 -0.012 59  GLN B CA  
1607 C C   . GLN B 63  ? 0.612 0.589 0.354 -0.050 -0.021 -0.011 59  GLN B C   
1608 O O   . GLN B 63  ? 0.590 0.573 0.346 -0.042 -0.022 -0.012 59  GLN B O   
1609 C CB  . GLN B 63  ? 0.583 0.554 0.317 -0.050 -0.023 -0.011 59  GLN B CB  
1610 C CG  . GLN B 63  ? 0.553 0.535 0.295 -0.047 -0.023 -0.013 59  GLN B CG  
1611 C CD  . GLN B 63  ? 0.533 0.532 0.294 -0.042 -0.021 -0.014 59  GLN B CD  
1612 O OE1 . GLN B 63  ? 0.512 0.526 0.281 -0.044 -0.018 -0.016 59  GLN B OE1 
1613 N NE2 . GLN B 63  ? 0.516 0.513 0.285 -0.033 -0.024 -0.014 59  GLN B NE2 
1614 N N   . GLU B 64  ? 0.650 0.611 0.375 -0.056 -0.022 -0.010 60  GLU B N   
1615 C CA  . GLU B 64  ? 0.691 0.641 0.411 -0.053 -0.023 -0.009 60  GLU B CA  
1616 C C   . GLU B 64  ? 0.645 0.612 0.381 -0.053 -0.021 -0.010 60  GLU B C   
1617 O O   . GLU B 64  ? 0.589 0.557 0.334 -0.045 -0.022 -0.010 60  GLU B O   
1618 C CB  . GLU B 64  ? 0.782 0.711 0.478 -0.061 -0.024 -0.007 60  GLU B CB  
1619 C CG  . GLU B 64  ? 0.871 0.779 0.550 -0.059 -0.027 -0.006 60  GLU B CG  
1620 C CD  . GLU B 64  ? 0.944 0.826 0.596 -0.065 -0.029 -0.004 60  GLU B CD  
1621 O OE1 . GLU B 64  ? 1.041 0.917 0.686 -0.069 -0.029 -0.004 60  GLU B OE1 
1622 O OE2 . GLU B 64  ? 0.940 0.807 0.576 -0.066 -0.031 -0.003 60  GLU B OE2 
1623 N N   . ALA B 65  ? 0.609 0.590 0.349 -0.061 -0.018 -0.011 61  ALA B N   
1624 C CA  . ALA B 65  ? 0.575 0.575 0.331 -0.061 -0.015 -0.012 61  ALA B CA  
1625 C C   . ALA B 65  ? 0.575 0.586 0.349 -0.050 -0.016 -0.013 61  ALA B C   
1626 O O   . ALA B 65  ? 0.650 0.663 0.432 -0.045 -0.016 -0.013 61  ALA B O   
1627 C CB  . ALA B 65  ? 0.568 0.584 0.326 -0.069 -0.012 -0.012 61  ALA B CB  
1628 N N   . GLU B 66  ? 0.557 0.572 0.336 -0.046 -0.016 -0.014 62  GLU B N   
1629 C CA  . GLU B 66  ? 0.535 0.562 0.331 -0.038 -0.016 -0.015 62  GLU B CA  
1630 C C   . GLU B 66  ? 0.538 0.555 0.335 -0.030 -0.019 -0.014 62  GLU B C   
1631 O O   . GLU B 66  ? 0.526 0.552 0.336 -0.025 -0.019 -0.015 62  GLU B O   
1632 C CB  . GLU B 66  ? 0.515 0.546 0.312 -0.037 -0.016 -0.016 62  GLU B CB  
1633 C CG  . GLU B 66  ? 0.486 0.524 0.296 -0.029 -0.017 -0.017 62  GLU B CG  
1634 C CD  . GLU B 66  ? 0.469 0.512 0.280 -0.029 -0.017 -0.018 62  GLU B CD  
1635 O OE1 . GLU B 66  ? 0.463 0.509 0.267 -0.035 -0.014 -0.019 62  GLU B OE1 
1636 O OE2 . GLU B 66  ? 0.441 0.486 0.259 -0.023 -0.018 -0.019 62  GLU B OE2 
1637 N N   . ARG B 67  ? 0.583 0.584 0.368 -0.029 -0.021 -0.013 63  ARG B N   
1638 C CA  . ARG B 67  ? 0.612 0.603 0.396 -0.021 -0.024 -0.011 63  ARG B CA  
1639 C C   . ARG B 67  ? 0.570 0.563 0.357 -0.021 -0.023 -0.011 63  ARG B C   
1640 O O   . ARG B 67  ? 0.522 0.522 0.321 -0.014 -0.023 -0.012 63  ARG B O   
1641 C CB  . ARG B 67  ? 0.658 0.630 0.424 -0.022 -0.026 -0.010 63  ARG B CB  
1642 C CG  . ARG B 67  ? 0.709 0.672 0.472 -0.012 -0.029 -0.008 63  ARG B CG  
1643 C CD  . ARG B 67  ? 0.807 0.748 0.548 -0.014 -0.031 -0.007 63  ARG B CD  
1644 N NE  . ARG B 67  ? 0.915 0.854 0.650 -0.018 -0.032 -0.007 63  ARG B NE  
1645 C CZ  . ARG B 67  ? 0.959 0.882 0.675 -0.024 -0.033 -0.006 63  ARG B CZ  
1646 N NH1 . ARG B 67  ? 0.988 0.895 0.687 -0.027 -0.033 -0.005 63  ARG B NH1 
1647 N NH2 . ARG B 67  ? 0.971 0.895 0.684 -0.026 -0.033 -0.007 63  ARG B NH2 
1648 N N   . ILE B 68  ? 0.560 0.547 0.338 -0.028 -0.021 -0.011 64  ILE B N   
1649 C CA  . ILE B 68  ? 0.562 0.548 0.339 -0.029 -0.020 -0.011 64  ILE B CA  
1650 C C   . ILE B 68  ? 0.524 0.528 0.320 -0.026 -0.018 -0.012 64  ILE B C   
1651 O O   . ILE B 68  ? 0.539 0.544 0.341 -0.021 -0.019 -0.012 64  ILE B O   
1652 C CB  . ILE B 68  ? 0.586 0.564 0.349 -0.039 -0.019 -0.010 64  ILE B CB  
1653 C CG1 . ILE B 68  ? 0.610 0.565 0.350 -0.042 -0.022 -0.009 64  ILE B CG1 
1654 C CG2 . ILE B 68  ? 0.597 0.577 0.363 -0.040 -0.018 -0.010 64  ILE B CG2 
1655 C CD1 . ILE B 68  ? 0.619 0.567 0.343 -0.054 -0.021 -0.008 64  ILE B CD1 
1656 N N   . LEU B 69  ? 0.504 0.524 0.310 -0.029 -0.017 -0.014 65  LEU B N   
1657 C CA  . LEU B 69  ? 0.488 0.524 0.310 -0.026 -0.015 -0.015 65  LEU B CA  
1658 C C   . LEU B 69  ? 0.478 0.516 0.310 -0.017 -0.017 -0.016 65  LEU B C   
1659 O O   . LEU B 69  ? 0.459 0.503 0.301 -0.013 -0.016 -0.016 65  LEU B O   
1660 C CB  . LEU B 69  ? 0.484 0.534 0.311 -0.029 -0.013 -0.017 65  LEU B CB  
1661 C CG  . LEU B 69  ? 0.496 0.551 0.317 -0.039 -0.011 -0.017 65  LEU B CG  
1662 C CD1 . LEU B 69  ? 0.503 0.578 0.334 -0.039 -0.008 -0.019 65  LEU B CD1 
1663 C CD2 . LEU B 69  ? 0.496 0.549 0.315 -0.042 -0.011 -0.016 65  LEU B CD2 
1664 N N   . LEU B 70  ? 0.475 0.508 0.304 -0.014 -0.019 -0.015 66  LEU B N   
1665 C CA  . LEU B 70  ? 0.463 0.498 0.301 -0.006 -0.021 -0.014 66  LEU B CA  
1666 C C   . LEU B 70  ? 0.481 0.509 0.317 -0.001 -0.022 -0.013 66  LEU B C   
1667 O O   . LEU B 70  ? 0.462 0.497 0.309 0.004  -0.022 -0.013 66  LEU B O   
1668 C CB  . LEU B 70  ? 0.448 0.478 0.281 -0.006 -0.023 -0.014 66  LEU B CB  
1669 C CG  . LEU B 70  ? 0.441 0.473 0.281 0.001  -0.026 -0.013 66  LEU B CG  
1670 C CD1 . LEU B 70  ? 0.420 0.465 0.274 0.003  -0.025 -0.014 66  LEU B CD1 
1671 C CD2 . LEU B 70  ? 0.440 0.469 0.276 0.001  -0.028 -0.012 66  LEU B CD2 
1672 N N   . GLU B 71  ? 0.524 0.538 0.347 -0.003 -0.022 -0.012 67  GLU B N   
1673 C CA  . GLU B 71  ? 0.573 0.579 0.392 0.003  -0.023 -0.010 67  GLU B CA  
1674 C C   . GLU B 71  ? 0.563 0.575 0.389 0.002  -0.021 -0.011 67  GLU B C   
1675 O O   . GLU B 71  ? 0.519 0.534 0.352 0.009  -0.021 -0.010 67  GLU B O   
1676 C CB  . GLU B 71  ? 0.635 0.622 0.435 0.002  -0.024 -0.009 67  GLU B CB  
1677 C CG  . GLU B 71  ? 0.726 0.705 0.518 0.006  -0.027 -0.008 67  GLU B CG  
1678 C CD  . GLU B 71  ? 0.790 0.749 0.561 0.004  -0.028 -0.006 67  GLU B CD  
1679 O OE1 . GLU B 71  ? 0.891 0.839 0.649 -0.003 -0.027 -0.007 67  GLU B OE1 
1680 O OE2 . GLU B 71  ? 0.789 0.741 0.554 0.009  -0.031 -0.005 67  GLU B OE2 
1681 N N   . PHE B 72  ? 0.524 0.537 0.348 -0.005 -0.019 -0.012 68  PHE B N   
1682 C CA  . PHE B 72  ? 0.526 0.546 0.356 -0.007 -0.017 -0.013 68  PHE B CA  
1683 C C   . PHE B 72  ? 0.518 0.552 0.365 -0.002 -0.016 -0.014 68  PHE B C   
1684 O O   . PHE B 72  ? 0.516 0.551 0.368 0.002  -0.016 -0.013 68  PHE B O   
1685 C CB  . PHE B 72  ? 0.530 0.555 0.357 -0.016 -0.015 -0.014 68  PHE B CB  
1686 C CG  . PHE B 72  ? 0.550 0.583 0.382 -0.019 -0.014 -0.015 68  PHE B CG  
1687 C CD1 . PHE B 72  ? 0.586 0.608 0.410 -0.019 -0.014 -0.014 68  PHE B CD1 
1688 C CD2 . PHE B 72  ? 0.540 0.589 0.382 -0.021 -0.012 -0.016 68  PHE B CD2 
1689 C CE1 . PHE B 72  ? 0.552 0.580 0.380 -0.022 -0.012 -0.014 68  PHE B CE1 
1690 C CE2 . PHE B 72  ? 0.530 0.586 0.377 -0.024 -0.011 -0.017 68  PHE B CE2 
1691 C CZ  . PHE B 72  ? 0.521 0.567 0.361 -0.024 -0.011 -0.016 68  PHE B CZ  
1692 N N   . LEU B 73  ? 0.528 0.573 0.384 -0.002 -0.017 -0.015 69  LEU B N   
1693 C CA  . LEU B 73  ? 0.516 0.572 0.385 0.002  -0.016 -0.016 69  LEU B CA  
1694 C C   . LEU B 73  ? 0.529 0.583 0.402 0.009  -0.018 -0.014 69  LEU B C   
1695 O O   . LEU B 73  ? 0.529 0.591 0.413 0.011  -0.018 -0.014 69  LEU B O   
1696 C CB  . LEU B 73  ? 0.515 0.578 0.387 0.000  -0.016 -0.017 69  LEU B CB  
1697 C CG  . LEU B 73  ? 0.506 0.576 0.378 -0.005 -0.014 -0.019 69  LEU B CG  
1698 C CD1 . LEU B 73  ? 0.505 0.583 0.381 -0.005 -0.014 -0.020 69  LEU B CD1 
1699 C CD2 . LEU B 73  ? 0.457 0.533 0.335 -0.005 -0.013 -0.020 69  LEU B CD2 
1700 N N   . THR B 74  ? 0.530 0.576 0.396 0.011  -0.020 -0.013 70  THR B N   
1701 C CA  . THR B 74  ? 0.504 0.552 0.374 0.017  -0.022 -0.011 70  THR B CA  
1702 C C   . THR B 74  ? 0.502 0.547 0.372 0.021  -0.021 -0.010 70  THR B C   
1703 O O   . THR B 74  ? 0.466 0.519 0.345 0.026  -0.021 -0.009 70  THR B O   
1704 C CB  . THR B 74  ? 0.478 0.519 0.340 0.019  -0.024 -0.010 70  THR B CB  
1705 O OG1 . THR B 74  ? 0.460 0.507 0.326 0.015  -0.025 -0.011 70  THR B OG1 
1706 C CG2 . THR B 74  ? 0.456 0.498 0.320 0.026  -0.026 -0.007 70  THR B CG2 
1707 N N   . HIS B 75  ? 0.529 0.562 0.387 0.020  -0.020 -0.010 71  HIS B N   
1708 C CA  . HIS B 75  ? 0.570 0.596 0.423 0.024  -0.019 -0.009 71  HIS B CA  
1709 C C   . HIS B 75  ? 0.563 0.599 0.427 0.023  -0.017 -0.010 71  HIS B C   
1710 O O   . HIS B 75  ? 0.574 0.612 0.443 0.028  -0.017 -0.009 71  HIS B O   
1711 C CB  . HIS B 75  ? 0.596 0.605 0.431 0.021  -0.019 -0.008 71  HIS B CB  
1712 C CG  . HIS B 75  ? 0.704 0.702 0.530 0.025  -0.018 -0.007 71  HIS B CG  
1713 N ND1 . HIS B 75  ? 0.734 0.729 0.558 0.034  -0.019 -0.006 71  HIS B ND1 
1714 C CD2 . HIS B 75  ? 0.721 0.713 0.541 0.021  -0.017 -0.008 71  HIS B CD2 
1715 C CE1 . HIS B 75  ? 0.739 0.724 0.555 0.037  -0.018 -0.005 71  HIS B CE1 
1716 N NE2 . HIS B 75  ? 0.715 0.697 0.528 0.028  -0.017 -0.007 71  HIS B NE2 
1717 N N   . ARG B 76  ? 0.527 0.569 0.395 0.016  -0.016 -0.012 72  ARG B N   
1718 C CA  . ARG B 76  ? 0.492 0.543 0.370 0.016  -0.015 -0.013 72  ARG B CA  
1719 C C   . ARG B 76  ? 0.467 0.528 0.358 0.020  -0.015 -0.013 72  ARG B C   
1720 O O   . ARG B 76  ? 0.434 0.501 0.332 0.021  -0.014 -0.013 72  ARG B O   
1721 C CB  . ARG B 76  ? 0.487 0.543 0.367 0.009  -0.014 -0.015 72  ARG B CB  
1722 C CG  . ARG B 76  ? 0.502 0.551 0.371 0.004  -0.013 -0.015 72  ARG B CG  
1723 C CD  . ARG B 76  ? 0.518 0.577 0.390 -0.002 -0.012 -0.017 72  ARG B CD  
1724 N NE  . ARG B 76  ? 0.562 0.624 0.434 -0.006 -0.011 -0.017 72  ARG B NE  
1725 C CZ  . ARG B 76  ? 0.556 0.630 0.436 -0.007 -0.010 -0.019 72  ARG B CZ  
1726 N NH1 . ARG B 76  ? 0.548 0.630 0.438 -0.003 -0.010 -0.020 72  ARG B NH1 
1727 N NH2 . ARG B 76  ? 0.609 0.685 0.487 -0.011 -0.009 -0.019 72  ARG B NH2 
1728 N N   . LYS B 77  ? 0.468 0.533 0.361 0.020  -0.017 -0.012 73  LYS B N   
1729 C CA  . LYS B 77  ? 0.470 0.544 0.374 0.023  -0.018 -0.012 73  LYS B CA  
1730 C C   . LYS B 77  ? 0.463 0.538 0.368 0.029  -0.018 -0.010 73  LYS B C   
1731 O O   . LYS B 77  ? 0.505 0.587 0.418 0.030  -0.018 -0.009 73  LYS B O   
1732 C CB  . LYS B 77  ? 0.485 0.562 0.390 0.022  -0.021 -0.012 73  LYS B CB  
1733 C CG  . LYS B 77  ? 0.488 0.574 0.402 0.022  -0.022 -0.012 73  LYS B CG  
1734 C CD  . LYS B 77  ? 0.543 0.632 0.459 0.025  -0.025 -0.009 73  LYS B CD  
1735 C CE  . LYS B 77  ? 0.562 0.658 0.483 0.023  -0.027 -0.009 73  LYS B CE  
1736 N NZ  . LYS B 77  ? 0.579 0.682 0.509 0.023  -0.026 -0.009 73  LYS B NZ  
1737 N N   . ALA B 78  ? 0.451 0.517 0.347 0.032  -0.019 -0.008 74  ALA B N   
1738 C CA  . ALA B 78  ? 0.445 0.511 0.341 0.039  -0.019 -0.006 74  ALA B CA  
1739 C C   . ALA B 78  ? 0.442 0.507 0.339 0.040  -0.016 -0.006 74  ALA B C   
1740 O O   . ALA B 78  ? 0.425 0.498 0.329 0.044  -0.016 -0.005 74  ALA B O   
1741 C CB  . ALA B 78  ? 0.440 0.494 0.322 0.042  -0.020 -0.005 74  ALA B CB  
1742 N N   . GLU B 79  ? 0.423 0.478 0.311 0.037  -0.015 -0.008 75  GLU B N   
1743 C CA  . GLU B 79  ? 0.444 0.496 0.331 0.037  -0.013 -0.008 75  GLU B CA  
1744 C C   . GLU B 79  ? 0.418 0.484 0.320 0.036  -0.012 -0.009 75  GLU B C   
1745 O O   . GLU B 79  ? 0.404 0.472 0.309 0.039  -0.011 -0.008 75  GLU B O   
1746 C CB  . GLU B 79  ? 0.465 0.508 0.344 0.031  -0.012 -0.010 75  GLU B CB  
1747 C CG  . GLU B 79  ? 0.498 0.525 0.360 0.030  -0.013 -0.009 75  GLU B CG  
1748 C CD  . GLU B 79  ? 0.527 0.547 0.380 0.022  -0.012 -0.010 75  GLU B CD  
1749 O OE1 . GLU B 79  ? 0.579 0.607 0.439 0.017  -0.011 -0.012 75  GLU B OE1 
1750 O OE2 . GLU B 79  ? 0.568 0.573 0.405 0.021  -0.013 -0.009 75  GLU B OE2 
1751 N N   . ARG B 80  ? 0.408 0.481 0.316 0.031  -0.013 -0.010 76  ARG B N   
1752 C CA  . ARG B 80  ? 0.398 0.479 0.315 0.030  -0.013 -0.011 76  ARG B CA  
1753 C C   . ARG B 80  ? 0.413 0.503 0.339 0.033  -0.014 -0.010 76  ARG B C   
1754 O O   . ARG B 80  ? 0.374 0.470 0.306 0.033  -0.013 -0.010 76  ARG B O   
1755 C CB  . ARG B 80  ? 0.390 0.474 0.309 0.025  -0.014 -0.013 76  ARG B CB  
1756 C CG  . ARG B 80  ? 0.388 0.478 0.313 0.023  -0.013 -0.015 76  ARG B CG  
1757 C CD  . ARG B 80  ? 0.393 0.483 0.316 0.019  -0.012 -0.018 76  ARG B CD  
1758 N NE  . ARG B 80  ? 0.427 0.517 0.347 0.018  -0.014 -0.018 76  ARG B NE  
1759 C CZ  . ARG B 80  ? 0.436 0.522 0.350 0.015  -0.013 -0.018 76  ARG B CZ  
1760 N NH1 . ARG B 80  ? 0.419 0.502 0.327 0.012  -0.012 -0.019 76  ARG B NH1 
1761 N NH2 . ARG B 80  ? 0.468 0.554 0.380 0.015  -0.015 -0.018 76  ARG B NH2 
1762 N N   . ASP B 81  ? 0.446 0.537 0.371 0.035  -0.016 -0.008 77  ASP B N   
1763 C CA  . ASP B 81  ? 0.448 0.549 0.380 0.038  -0.017 -0.005 77  ASP B CA  
1764 C C   . ASP B 81  ? 0.437 0.541 0.370 0.043  -0.015 -0.004 77  ASP B C   
1765 O O   . ASP B 81  ? 0.412 0.526 0.352 0.044  -0.015 -0.002 77  ASP B O   
1766 C CB  . ASP B 81  ? 0.455 0.557 0.384 0.039  -0.019 -0.004 77  ASP B CB  
1767 C CG  . ASP B 81  ? 0.469 0.574 0.401 0.034  -0.022 -0.005 77  ASP B CG  
1768 O OD1 . ASP B 81  ? 0.521 0.626 0.455 0.030  -0.021 -0.007 77  ASP B OD1 
1769 O OD2 . ASP B 81  ? 0.501 0.608 0.432 0.035  -0.024 -0.004 77  ASP B OD2 
1770 N N   . ARG B 82  ? 0.428 0.522 0.352 0.047  -0.014 -0.004 78  ARG B N   
1771 C CA  . ARG B 82  ? 0.459 0.551 0.380 0.053  -0.011 -0.002 78  ARG B CA  
1772 C C   . ARG B 82  ? 0.427 0.519 0.352 0.050  -0.009 -0.004 78  ARG B C   
1773 O O   . ARG B 82  ? 0.400 0.500 0.331 0.053  -0.008 -0.002 78  ARG B O   
1774 C CB  . ARG B 82  ? 0.506 0.583 0.413 0.057  -0.011 -0.002 78  ARG B CB  
1775 C CG  . ARG B 82  ? 0.590 0.662 0.491 0.065  -0.009 -0.000 78  ARG B CG  
1776 C CD  . ARG B 82  ? 0.690 0.749 0.576 0.069  -0.010 0.000  78  ARG B CD  
1777 N NE  . ARG B 82  ? 0.740 0.786 0.614 0.075  -0.008 0.001  78  ARG B NE  
1778 C CZ  . ARG B 82  ? 0.769 0.803 0.636 0.071  -0.007 -0.001 78  ARG B CZ  
1779 N NH1 . ARG B 82  ? 0.756 0.792 0.628 0.062  -0.007 -0.003 78  ARG B NH1 
1780 N NH2 . ARG B 82  ? 0.779 0.801 0.634 0.077  -0.005 -0.000 78  ARG B NH2 
1781 N N   . ALA B 83  ? 0.413 0.498 0.335 0.045  -0.009 -0.006 79  ALA B N   
1782 C CA  . ALA B 83  ? 0.411 0.497 0.336 0.042  -0.008 -0.007 79  ALA B CA  
1783 C C   . ALA B 83  ? 0.400 0.498 0.336 0.041  -0.008 -0.007 79  ALA B C   
1784 O O   . ALA B 83  ? 0.403 0.504 0.343 0.042  -0.007 -0.007 79  ALA B O   
1785 C CB  . ALA B 83  ? 0.403 0.483 0.324 0.037  -0.008 -0.010 79  ALA B CB  
1786 N N   . ALA B 84  ? 0.391 0.495 0.332 0.038  -0.010 -0.007 80  ALA B N   
1787 C CA  . ALA B 84  ? 0.378 0.493 0.327 0.036  -0.012 -0.006 80  ALA B CA  
1788 C C   . ALA B 84  ? 0.373 0.496 0.327 0.040  -0.011 -0.003 80  ALA B C   
1789 O O   . ALA B 84  ? 0.369 0.499 0.328 0.038  -0.011 -0.002 80  ALA B O   
1790 C CB  . ALA B 84  ? 0.378 0.495 0.328 0.032  -0.014 -0.007 80  ALA B CB  
1791 N N   . LEU B 85  ? 0.369 0.494 0.320 0.045  -0.011 -0.001 81  LEU B N   
1792 C CA  . LEU B 85  ? 0.380 0.516 0.336 0.050  -0.010 0.002  81  LEU B CA  
1793 C C   . LEU B 85  ? 0.401 0.534 0.356 0.053  -0.007 0.002  81  LEU B C   
1794 O O   . LEU B 85  ? 0.393 0.535 0.354 0.053  -0.006 0.003  81  LEU B O   
1795 C CB  . LEU B 85  ? 0.388 0.525 0.340 0.056  -0.011 0.004  81  LEU B CB  
1796 C CG  . LEU B 85  ? 0.373 0.516 0.328 0.054  -0.014 0.005  81  LEU B CG  
1797 C CD1 . LEU B 85  ? 0.381 0.522 0.330 0.062  -0.014 0.007  81  LEU B CD1 
1798 C CD2 . LEU B 85  ? 0.358 0.517 0.323 0.050  -0.016 0.007  81  LEU B CD2 
1799 N N   . ARG B 86  ? 0.412 0.531 0.358 0.055  -0.005 -0.000 82  ARG B N   
1800 C CA  . ARG B 86  ? 0.431 0.544 0.373 0.058  -0.002 -0.000 82  ARG B CA  
1801 C C   . ARG B 86  ? 0.429 0.544 0.376 0.053  -0.002 -0.002 82  ARG B C   
1802 O O   . ARG B 86  ? 0.474 0.594 0.423 0.055  0.000  -0.000 82  ARG B O   
1803 C CB  . ARG B 86  ? 0.454 0.550 0.383 0.059  -0.002 -0.002 82  ARG B CB  
1804 C CG  . ARG B 86  ? 0.481 0.570 0.405 0.061  0.001  -0.002 82  ARG B CG  
1805 C CD  . ARG B 86  ? 0.510 0.583 0.424 0.058  0.001  -0.005 82  ARG B CD  
1806 N NE  . ARG B 86  ? 0.541 0.602 0.442 0.064  0.001  -0.003 82  ARG B NE  
1807 C CZ  . ARG B 86  ? 0.528 0.578 0.418 0.064  0.000  -0.004 82  ARG B CZ  
1808 N NH1 . ARG B 86  ? 0.540 0.591 0.433 0.057  -0.002 -0.005 82  ARG B NH1 
1809 N NH2 . ARG B 86  ? 0.529 0.567 0.406 0.070  0.001  -0.003 82  ARG B NH2 
1810 N N   . LEU B 87  ? 0.415 0.528 0.363 0.046  -0.004 -0.004 83  LEU B N   
1811 C CA  . LEU B 87  ? 0.378 0.489 0.329 0.042  -0.003 -0.006 83  LEU B CA  
1812 C C   . LEU B 87  ? 0.376 0.496 0.334 0.038  -0.005 -0.005 83  LEU B C   
1813 O O   . LEU B 87  ? 0.359 0.477 0.317 0.034  -0.005 -0.007 83  LEU B O   
1814 C CB  . LEU B 87  ? 0.375 0.477 0.321 0.039  -0.004 -0.009 83  LEU B CB  
1815 C CG  . LEU B 87  ? 0.382 0.474 0.318 0.041  -0.003 -0.009 83  LEU B CG  
1816 C CD1 . LEU B 87  ? 0.383 0.469 0.316 0.037  -0.003 -0.012 83  LEU B CD1 
1817 C CD2 . LEU B 87  ? 0.391 0.479 0.325 0.044  -0.000 -0.009 83  LEU B CD2 
1818 N N   . GLN B 88  ? 0.404 0.534 0.366 0.038  -0.006 -0.003 84  GLN B N   
1819 C CA  . GLN B 88  ? 0.420 0.559 0.388 0.033  -0.008 -0.002 84  GLN B CA  
1820 C C   . GLN B 88  ? 0.406 0.545 0.375 0.031  -0.006 -0.002 84  GLN B C   
1821 O O   . GLN B 88  ? 0.397 0.540 0.367 0.035  -0.004 -0.000 84  GLN B O   
1822 C CB  . GLN B 88  ? 0.457 0.609 0.429 0.035  -0.008 0.002  84  GLN B CB  
1823 C CG  . GLN B 88  ? 0.505 0.665 0.482 0.030  -0.012 0.003  84  GLN B CG  
1824 C CD  . GLN B 88  ? 0.525 0.700 0.507 0.032  -0.012 0.007  84  GLN B CD  
1825 O OE1 . GLN B 88  ? 0.533 0.710 0.514 0.039  -0.011 0.008  84  GLN B OE1 
1826 N NE2 . GLN B 88  ? 0.557 0.744 0.544 0.027  -0.014 0.009  84  GLN B NE2 
1827 N N   . PHE B 89  ? 0.385 0.520 0.353 0.026  -0.008 -0.003 85  PHE B N   
1828 C CA  . PHE B 89  ? 0.374 0.508 0.342 0.024  -0.007 -0.004 85  PHE B CA  
1829 C C   . PHE B 89  ? 0.400 0.537 0.369 0.017  -0.010 -0.003 85  PHE B C   
1830 O O   . PHE B 89  ? 0.415 0.549 0.381 0.013  -0.013 -0.004 85  PHE B O   
1831 C CB  . PHE B 89  ? 0.373 0.495 0.336 0.024  -0.006 -0.007 85  PHE B CB  
1832 C CG  . PHE B 89  ? 0.358 0.473 0.317 0.022  -0.009 -0.010 85  PHE B CG  
1833 C CD1 . PHE B 89  ? 0.363 0.476 0.321 0.023  -0.009 -0.011 85  PHE B CD1 
1834 C CD2 . PHE B 89  ? 0.351 0.461 0.307 0.018  -0.010 -0.011 85  PHE B CD2 
1835 C CE1 . PHE B 89  ? 0.361 0.470 0.316 0.021  -0.011 -0.013 85  PHE B CE1 
1836 C CE2 . PHE B 89  ? 0.360 0.464 0.312 0.017  -0.012 -0.014 85  PHE B CE2 
1837 C CZ  . PHE B 89  ? 0.357 0.461 0.309 0.019  -0.013 -0.015 85  PHE B CZ  
1838 N N   . SER B 90  ? 0.413 0.555 0.383 0.015  -0.009 -0.001 86  SER B N   
1839 C CA  . SER B 90  ? 0.447 0.591 0.416 0.007  -0.011 0.001  86  SER B CA  
1840 C C   . SER B 90  ? 0.460 0.592 0.423 0.004  -0.012 -0.002 86  SER B C   
1841 O O   . SER B 90  ? 0.469 0.598 0.427 -0.002 -0.014 -0.001 86  SER B O   
1842 C CB  . SER B 90  ? 0.459 0.619 0.434 0.006  -0.010 0.005  86  SER B CB  
1843 O OG  . SER B 90  ? 0.485 0.656 0.466 0.010  -0.009 0.007  86  SER B OG  
1844 N N   . HIS B 91  ? 0.460 0.585 0.420 0.009  -0.009 -0.004 87  HIS B N   
1845 C CA  . HIS B 91  ? 0.472 0.586 0.426 0.007  -0.009 -0.006 87  HIS B CA  
1846 C C   . HIS B 91  ? 0.425 0.529 0.376 0.011  -0.009 -0.010 87  HIS B C   
1847 O O   . HIS B 91  ? 0.415 0.510 0.359 0.010  -0.011 -0.012 87  HIS B O   
1848 C CB  . HIS B 91  ? 0.516 0.635 0.473 0.007  -0.007 -0.004 87  HIS B CB  
1849 C CG  . HIS B 91  ? 0.568 0.700 0.529 0.002  -0.007 0.000  87  HIS B CG  
1850 N ND1 . HIS B 91  ? 0.592 0.724 0.549 -0.006 -0.009 0.001  87  HIS B ND1 
1851 C CD2 . HIS B 91  ? 0.562 0.710 0.531 0.005  -0.005 0.003  87  HIS B CD2 
1852 C CE1 . HIS B 91  ? 0.579 0.725 0.541 -0.009 -0.009 0.005  87  HIS B CE1 
1853 N NE2 . HIS B 91  ? 0.585 0.742 0.555 -0.002 -0.006 0.007  87  HIS B NE2 
1854 N N   . SER B 92  ? 0.389 0.494 0.342 0.017  -0.007 -0.010 88  SER B N   
1855 C CA  . SER B 92  ? 0.373 0.471 0.323 0.020  -0.006 -0.013 88  SER B CA  
1856 C C   . SER B 92  ? 0.342 0.440 0.293 0.024  -0.005 -0.013 88  SER B C   
1857 O O   . SER B 92  ? 0.349 0.454 0.304 0.025  -0.003 -0.011 88  SER B O   
1858 C CB  . SER B 92  ? 0.365 0.459 0.314 0.020  -0.004 -0.013 88  SER B CB  
1859 O OG  . SER B 92  ? 0.372 0.469 0.322 0.024  -0.001 -0.012 88  SER B OG  
1860 N N   . PHE B 93  ? 0.315 0.409 0.264 0.025  -0.005 -0.016 89  PHE B N   
1861 C CA  . PHE B 93  ? 0.303 0.396 0.252 0.028  -0.003 -0.016 89  PHE B CA  
1862 C C   . PHE B 93  ? 0.295 0.383 0.240 0.028  -0.003 -0.019 89  PHE B C   
1863 O O   . PHE B 93  ? 0.311 0.397 0.255 0.028  -0.005 -0.020 89  PHE B O   
1864 C CB  . PHE B 93  ? 0.297 0.392 0.247 0.028  -0.004 -0.017 89  PHE B CB  
1865 C CG  . PHE B 93  ? 0.301 0.394 0.248 0.027  -0.006 -0.019 89  PHE B CG  
1866 C CD1 . PHE B 93  ? 0.309 0.405 0.257 0.025  -0.008 -0.019 89  PHE B CD1 
1867 C CD2 . PHE B 93  ? 0.317 0.408 0.262 0.027  -0.006 -0.021 89  PHE B CD2 
1868 C CE1 . PHE B 93  ? 0.322 0.416 0.267 0.025  -0.010 -0.021 89  PHE B CE1 
1869 C CE2 . PHE B 93  ? 0.338 0.430 0.282 0.027  -0.007 -0.023 89  PHE B CE2 
1870 C CZ  . PHE B 93  ? 0.316 0.409 0.260 0.026  -0.009 -0.023 89  PHE B CZ  
1871 N N   . GLU B 94  ? 0.291 0.376 0.234 0.030  -0.002 -0.018 90  GLU B N   
1872 C CA  . GLU B 94  ? 0.298 0.380 0.237 0.030  -0.002 -0.020 90  GLU B CA  
1873 C C   . GLU B 94  ? 0.283 0.364 0.220 0.029  -0.002 -0.020 90  GLU B C   
1874 O O   . GLU B 94  ? 0.295 0.374 0.230 0.030  -0.000 -0.019 90  GLU B O   
1875 C CB  . GLU B 94  ? 0.328 0.405 0.265 0.030  -0.000 -0.020 90  GLU B CB  
1876 C CG  . GLU B 94  ? 0.358 0.432 0.291 0.030  -0.001 -0.022 90  GLU B CG  
1877 C CD  . GLU B 94  ? 0.392 0.460 0.321 0.030  0.000  -0.021 90  GLU B CD  
1878 O OE1 . GLU B 94  ? 0.423 0.487 0.347 0.029  0.000  -0.021 90  GLU B OE1 
1879 O OE2 . GLU B 94  ? 0.420 0.487 0.350 0.031  0.001  -0.021 90  GLU B OE2 
1880 N N   . VAL B 95  ? 0.279 0.362 0.215 0.028  -0.003 -0.022 91  VAL B N   
1881 C CA  . VAL B 95  ? 0.284 0.366 0.217 0.026  -0.003 -0.022 91  VAL B CA  
1882 C C   . VAL B 95  ? 0.288 0.369 0.217 0.024  -0.003 -0.023 91  VAL B C   
1883 O O   . VAL B 95  ? 0.294 0.379 0.225 0.024  -0.004 -0.025 91  VAL B O   
1884 C CB  . VAL B 95  ? 0.289 0.376 0.223 0.024  -0.004 -0.023 91  VAL B CB  
1885 C CG1 . VAL B 95  ? 0.289 0.377 0.219 0.021  -0.004 -0.023 91  VAL B CG1 
1886 C CG2 . VAL B 95  ? 0.289 0.378 0.226 0.026  -0.004 -0.022 91  VAL B CG2 
1887 N N   . ASN B 96  ? 0.310 0.384 0.233 0.023  -0.002 -0.022 92  ASN B N   
1888 C CA  . ASN B 96  ? 0.337 0.410 0.256 0.020  -0.003 -0.023 92  ASN B CA  
1889 C C   . ASN B 96  ? 0.362 0.432 0.274 0.016  -0.003 -0.022 92  ASN B C   
1890 O O   . ASN B 96  ? 0.395 0.456 0.301 0.016  -0.002 -0.021 92  ASN B O   
1891 C CB  . ASN B 96  ? 0.346 0.411 0.262 0.022  -0.001 -0.022 92  ASN B CB  
1892 C CG  . ASN B 96  ? 0.371 0.432 0.282 0.020  -0.002 -0.022 92  ASN B CG  
1893 O OD1 . ASN B 96  ? 0.408 0.468 0.313 0.015  -0.003 -0.022 92  ASN B OD1 
1894 N ND2 . ASN B 96  ? 0.354 0.414 0.266 0.022  -0.002 -0.023 92  ASN B ND2 
1895 N N   . LEU B 97  ? 0.388 0.466 0.301 0.012  -0.004 -0.023 93  LEU B N   
1896 C CA  . LEU B 97  ? 0.447 0.524 0.353 0.006  -0.005 -0.022 93  LEU B CA  
1897 C C   . LEU B 97  ? 0.460 0.538 0.361 0.000  -0.006 -0.022 93  LEU B C   
1898 O O   . LEU B 97  ? 0.434 0.518 0.339 0.002  -0.007 -0.023 93  LEU B O   
1899 C CB  . LEU B 97  ? 0.439 0.527 0.350 0.005  -0.006 -0.023 93  LEU B CB  
1900 C CG  . LEU B 97  ? 0.468 0.557 0.385 0.010  -0.005 -0.024 93  LEU B CG  
1901 C CD1 . LEU B 97  ? 0.484 0.584 0.405 0.009  -0.005 -0.025 93  LEU B CD1 
1902 C CD2 . LEU B 97  ? 0.479 0.557 0.390 0.010  -0.004 -0.022 93  LEU B CD2 
1903 N N   . ASP B 98  ? 0.568 0.644 0.461 -0.006 -0.007 -0.021 94  ASP B N   
1904 C CA  . ASP B 98  ? 0.652 0.730 0.538 -0.014 -0.009 -0.021 94  ASP B CA  
1905 C C   . ASP B 98  ? 0.727 0.794 0.608 -0.013 -0.009 -0.020 94  ASP B C   
1906 O O   . ASP B 98  ? 0.870 0.942 0.751 -0.016 -0.010 -0.021 94  ASP B O   
1907 C CB  . ASP B 98  ? 0.678 0.775 0.572 -0.017 -0.010 -0.022 94  ASP B CB  
1908 C CG  . ASP B 98  ? 0.761 0.872 0.662 -0.016 -0.009 -0.022 94  ASP B CG  
1909 O OD1 . ASP B 98  ? 0.756 0.861 0.654 -0.017 -0.009 -0.022 94  ASP B OD1 
1910 O OD2 . ASP B 98  ? 0.708 0.836 0.617 -0.015 -0.010 -0.024 94  ASP B OD2 
1911 N N   . ASN B 99  ? 0.806 0.860 0.685 -0.007 -0.007 -0.020 95  ASN B N   
1912 C CA  . ASN B 99  ? 0.864 0.910 0.742 -0.002 -0.006 -0.020 95  ASN B CA  
1913 C C   . ASN B 99  ? 0.847 0.902 0.731 -0.002 -0.007 -0.021 95  ASN B C   
1914 O O   . ASN B 99  ? 0.796 0.849 0.674 -0.007 -0.008 -0.021 95  ASN B O   
1915 C CB  . ASN B 99  ? 0.938 0.965 0.801 -0.003 -0.005 -0.018 95  ASN B CB  
1916 C CG  . ASN B 99  ? 0.991 1.010 0.847 -0.003 -0.005 -0.017 95  ASN B CG  
1917 O OD1 . ASN B 99  ? 1.026 1.036 0.879 0.003  -0.003 -0.017 95  ASN B OD1 
1918 N ND2 . ASN B 99  ? 0.847 0.870 0.701 -0.009 -0.006 -0.017 95  ASN B ND2 
1919 N N   . GLY B 100 ? 0.836 0.898 0.731 0.004  -0.006 -0.022 96  GLY B N   
1920 C CA  . GLY B 100 ? 0.836 0.904 0.735 0.006  -0.007 -0.023 96  GLY B CA  
1921 C C   . GLY B 100 ? 0.852 0.936 0.760 0.007  -0.008 -0.025 96  GLY B C   
1922 O O   . GLY B 100 ? 0.825 0.912 0.738 0.012  -0.008 -0.026 96  GLY B O   
1923 N N   . ARG B 101 ? 0.816 0.909 0.724 0.002  -0.009 -0.025 97  ARG B N   
1924 C CA  . ARG B 101 ? 0.732 0.843 0.646 0.002  -0.011 -0.026 97  ARG B CA  
1925 C C   . ARG B 101 ? 0.647 0.765 0.568 0.006  -0.010 -0.027 97  ARG B C   
1926 O O   . ARG B 101 ? 0.721 0.853 0.645 0.006  -0.011 -0.028 97  ARG B O   
1927 C CB  . ARG B 101 ? 0.817 0.934 0.727 -0.006 -0.012 -0.025 97  ARG B CB  
1928 C CG  . ARG B 101 ? 0.914 1.023 0.815 -0.012 -0.013 -0.024 97  ARG B CG  
1929 C CD  . ARG B 101 ? 1.035 1.147 0.929 -0.022 -0.015 -0.022 97  ARG B CD  
1930 N NE  . ARG B 101 ? 1.100 1.195 0.983 -0.026 -0.014 -0.020 97  ARG B NE  
1931 C CZ  . ARG B 101 ? 1.145 1.233 1.015 -0.036 -0.016 -0.019 97  ARG B CZ  
1932 N NH1 . ARG B 101 ? 1.144 1.244 1.014 -0.043 -0.018 -0.018 97  ARG B NH1 
1933 N NH2 . ARG B 101 ? 1.152 1.222 1.010 -0.038 -0.015 -0.018 97  ARG B NH2 
1934 N N   . LYS B 102 ? 0.577 0.687 0.499 0.010  -0.008 -0.027 98  LYS B N   
1935 C CA  . LYS B 102 ? 0.485 0.598 0.412 0.014  -0.008 -0.028 98  LYS B CA  
1936 C C   . LYS B 102 ? 0.408 0.511 0.336 0.018  -0.007 -0.028 98  LYS B C   
1937 O O   . LYS B 102 ? 0.387 0.482 0.312 0.016  -0.006 -0.026 98  LYS B O   
1938 C CB  . LYS B 102 ? 0.523 0.643 0.451 0.012  -0.008 -0.028 98  LYS B CB  
1939 C CG  . LYS B 102 ? 0.589 0.722 0.521 0.013  -0.008 -0.029 98  LYS B CG  
1940 C CD  . LYS B 102 ? 0.604 0.742 0.536 0.012  -0.008 -0.029 98  LYS B CD  
1941 C CE  . LYS B 102 ? 0.634 0.774 0.562 0.004  -0.008 -0.028 98  LYS B CE  
1942 N NZ  . LYS B 102 ? 0.657 0.805 0.586 0.003  -0.007 -0.028 98  LYS B NZ  
1943 N N   . ILE B 103 ? 0.354 0.457 0.285 0.023  -0.007 -0.029 99  ILE B N   
1944 C CA  . ILE B 103 ? 0.345 0.439 0.276 0.025  -0.006 -0.028 99  ILE B CA  
1945 C C   . ILE B 103 ? 0.323 0.419 0.257 0.028  -0.007 -0.029 99  ILE B C   
1946 O O   . ILE B 103 ? 0.314 0.414 0.248 0.031  -0.008 -0.031 99  ILE B O   
1947 C CB  . ILE B 103 ? 0.343 0.431 0.273 0.026  -0.006 -0.028 99  ILE B CB  
1948 C CG1 . ILE B 103 ? 0.357 0.441 0.282 0.023  -0.006 -0.027 99  ILE B CG1 
1949 C CG2 . ILE B 103 ? 0.340 0.422 0.270 0.028  -0.005 -0.027 99  ILE B CG2 
1950 C CD1 . ILE B 103 ? 0.362 0.442 0.285 0.024  -0.006 -0.027 99  ILE B CD1 
1951 N N   . MET B 104 ? 0.318 0.411 0.253 0.028  -0.006 -0.028 100 MET B N   
1952 C CA  . MET B 104 ? 0.335 0.427 0.271 0.030  -0.007 -0.029 100 MET B CA  
1953 C C   . MET B 104 ? 0.321 0.408 0.258 0.030  -0.007 -0.027 100 MET B C   
1954 O O   . MET B 104 ? 0.300 0.386 0.238 0.029  -0.005 -0.025 100 MET B O   
1955 C CB  . MET B 104 ? 0.350 0.446 0.287 0.030  -0.008 -0.029 100 MET B CB  
1956 C CG  . MET B 104 ? 0.373 0.468 0.310 0.031  -0.009 -0.029 100 MET B CG  
1957 S SD  . MET B 104 ? 0.394 0.494 0.333 0.030  -0.009 -0.029 100 MET B SD  
1958 C CE  . MET B 104 ? 0.398 0.506 0.336 0.031  -0.009 -0.031 100 MET B CE  
1959 N N   . ARG B 105 ? 0.318 0.401 0.254 0.031  -0.008 -0.028 101 ARG B N   
1960 C CA  . ARG B 105 ? 0.355 0.434 0.291 0.030  -0.007 -0.026 101 ARG B CA  
1961 C C   . ARG B 105 ? 0.361 0.440 0.296 0.030  -0.009 -0.026 101 ARG B C   
1962 O O   . ARG B 105 ? 0.354 0.430 0.284 0.032  -0.011 -0.028 101 ARG B O   
1963 C CB  . ARG B 105 ? 0.394 0.468 0.327 0.030  -0.007 -0.026 101 ARG B CB  
1964 C CG  . ARG B 105 ? 0.436 0.509 0.369 0.031  -0.006 -0.026 101 ARG B CG  
1965 C CD  . ARG B 105 ? 0.478 0.546 0.408 0.031  -0.005 -0.025 101 ARG B CD  
1966 N NE  . ARG B 105 ? 0.507 0.572 0.436 0.031  -0.004 -0.025 101 ARG B NE  
1967 C CZ  . ARG B 105 ? 0.494 0.560 0.421 0.032  -0.004 -0.026 101 ARG B CZ  
1968 N NH1 . ARG B 105 ? 0.504 0.574 0.431 0.033  -0.006 -0.028 101 ARG B NH1 
1969 N NH2 . ARG B 105 ? 0.536 0.598 0.460 0.032  -0.003 -0.026 101 ARG B NH2 
1970 N N   . LEU B 106 ? 0.384 0.463 0.320 0.027  -0.009 -0.024 102 LEU B N   
1971 C CA  . LEU B 106 ? 0.413 0.490 0.347 0.025  -0.011 -0.024 102 LEU B CA  
1972 C C   . LEU B 106 ? 0.413 0.490 0.348 0.022  -0.011 -0.022 102 LEU B C   
1973 O O   . LEU B 106 ? 0.435 0.518 0.376 0.022  -0.009 -0.020 102 LEU B O   
1974 C CB  . LEU B 106 ? 0.406 0.488 0.342 0.025  -0.012 -0.024 102 LEU B CB  
1975 C CG  . LEU B 106 ? 0.423 0.502 0.356 0.022  -0.014 -0.023 102 LEU B CG  
1976 C CD1 . LEU B 106 ? 0.452 0.527 0.380 0.025  -0.016 -0.026 102 LEU B CD1 
1977 C CD2 . LEU B 106 ? 0.428 0.513 0.366 0.021  -0.014 -0.021 102 LEU B CD2 
1978 N N   . GLN B 107 ? 0.433 0.504 0.362 0.020  -0.013 -0.022 103 GLN B N   
1979 C CA  . GLN B 107 ? 0.473 0.544 0.402 0.015  -0.014 -0.019 103 GLN B CA  
1980 C C   . GLN B 107 ? 0.476 0.543 0.400 0.012  -0.017 -0.019 103 GLN B C   
1981 O O   . GLN B 107 ? 0.468 0.526 0.384 0.013  -0.019 -0.022 103 GLN B O   
1982 C CB  . GLN B 107 ? 0.523 0.587 0.446 0.014  -0.014 -0.019 103 GLN B CB  
1983 C CG  . GLN B 107 ? 0.594 0.658 0.519 0.017  -0.011 -0.020 103 GLN B CG  
1984 C CD  . GLN B 107 ? 0.671 0.732 0.595 0.022  -0.012 -0.023 103 GLN B CD  
1985 O OE1 . GLN B 107 ? 0.756 0.810 0.673 0.024  -0.014 -0.025 103 GLN B OE1 
1986 N NE2 . GLN B 107 ? 0.682 0.748 0.611 0.025  -0.009 -0.023 103 GLN B NE2 
1987 N N   . LEU B 108 ? 0.500 0.575 0.428 0.008  -0.017 -0.016 104 LEU B N   
1988 C CA  . LEU B 108 ? 0.511 0.583 0.435 0.003  -0.020 -0.016 104 LEU B CA  
1989 C C   . LEU B 108 ? 0.553 0.616 0.468 -0.003 -0.023 -0.015 104 LEU B C   
1990 O O   . LEU B 108 ? 0.554 0.620 0.470 -0.005 -0.021 -0.013 104 LEU B O   
1991 C CB  . LEU B 108 ? 0.483 0.567 0.414 0.000  -0.020 -0.012 104 LEU B CB  
1992 C CG  . LEU B 108 ? 0.475 0.566 0.413 0.005  -0.018 -0.013 104 LEU B CG  
1993 C CD1 . LEU B 108 ? 0.477 0.581 0.423 0.002  -0.018 -0.009 104 LEU B CD1 
1994 C CD2 . LEU B 108 ? 0.466 0.551 0.399 0.007  -0.020 -0.016 104 LEU B CD2 
1995 N N   . GLY B 109 ? 0.601 0.653 0.505 -0.005 -0.026 -0.016 105 GLY B N   
1996 C CA  . GLY B 109 ? 0.655 0.698 0.548 -0.013 -0.029 -0.014 105 GLY B CA  
1997 C C   . GLY B 109 ? 0.710 0.751 0.598 -0.019 -0.033 -0.013 105 GLY B C   
1998 O O   . GLY B 109 ? 0.662 0.708 0.555 -0.016 -0.033 -0.014 105 GLY B O   
1999 N N   . GLN B 110 ? 0.841 0.872 0.717 -0.027 -0.036 -0.012 106 GLN B N   
2000 C CA  . GLN B 110 ? 0.895 0.920 0.762 -0.034 -0.040 -0.010 106 GLN B CA  
2001 C C   . GLN B 110 ? 0.895 0.909 0.754 -0.029 -0.042 -0.014 106 GLN B C   
2002 O O   . GLN B 110 ? 0.853 0.874 0.717 -0.028 -0.042 -0.013 106 GLN B O   
2003 C CB  . GLN B 110 ? 0.953 0.967 0.806 -0.044 -0.043 -0.008 106 GLN B CB  
2004 C CG  . GLN B 110 ? 1.007 1.014 0.849 -0.054 -0.048 -0.006 106 GLN B CG  
2005 C CD  . GLN B 110 ? 1.008 1.036 0.863 -0.062 -0.048 -0.002 106 GLN B CD  
2006 O OE1 . GLN B 110 ? 1.006 1.054 0.877 -0.060 -0.045 0.000  106 GLN B OE1 
2007 N NE2 . GLN B 110 ? 0.985 1.007 0.830 -0.070 -0.053 -0.000 106 GLN B NE2 
2008 N N   . GLU B 111 ? 0.919 0.915 0.765 -0.023 -0.043 -0.017 107 GLU B N   
2009 C CA  . GLU B 111 ? 0.975 0.957 0.808 -0.018 -0.045 -0.020 107 GLU B CA  
2010 C C   . GLU B 111 ? 0.925 0.913 0.766 -0.007 -0.041 -0.023 107 GLU B C   
2011 O O   . GLU B 111 ? 0.981 0.966 0.819 -0.002 -0.042 -0.026 107 GLU B O   
2012 C CB  . GLU B 111 ? 1.060 1.017 0.870 -0.021 -0.048 -0.021 107 GLU B CB  
2013 C CG  . GLU B 111 ? 1.121 1.069 0.919 -0.031 -0.053 -0.019 107 GLU B CG  
2014 C CD  . GLU B 111 ? 1.235 1.177 1.027 -0.029 -0.055 -0.020 107 GLU B CD  
2015 O OE1 . GLU B 111 ? 1.245 1.173 1.024 -0.021 -0.056 -0.024 107 GLU B OE1 
2016 O OE2 . GLU B 111 ? 1.305 1.261 1.107 -0.034 -0.055 -0.018 107 GLU B OE2 
2017 N N   . THR B 112 ? 0.873 0.869 0.724 -0.003 -0.038 -0.024 108 THR B N   
2018 C CA  . THR B 112 ? 0.763 0.766 0.621 0.007  -0.035 -0.027 108 THR B CA  
2019 C C   . THR B 112 ? 0.720 0.739 0.595 0.007  -0.031 -0.025 108 THR B C   
2020 O O   . THR B 112 ? 0.732 0.755 0.610 0.002  -0.031 -0.022 108 THR B O   
2021 C CB  . THR B 112 ? 0.743 0.732 0.589 0.014  -0.035 -0.030 108 THR B CB  
2022 O OG1 . THR B 112 ? 0.724 0.710 0.568 0.010  -0.035 -0.028 108 THR B OG1 
2023 C CG2 . THR B 112 ? 0.724 0.694 0.551 0.015  -0.039 -0.032 108 THR B CG2 
2024 N N   . SER B 113 ? 0.656 0.685 0.541 0.013  -0.028 -0.026 109 SER B N   
2025 C CA  . SER B 113 ? 0.593 0.633 0.490 0.015  -0.025 -0.026 109 SER B CA  
2026 C C   . SER B 113 ? 0.564 0.599 0.456 0.021  -0.024 -0.028 109 SER B C   
2027 O O   . SER B 113 ? 0.566 0.594 0.450 0.026  -0.025 -0.031 109 SER B O   
2028 C CB  . SER B 113 ? 0.556 0.608 0.462 0.017  -0.023 -0.026 109 SER B CB  
2029 O OG  . SER B 113 ? 0.531 0.587 0.440 0.012  -0.024 -0.023 109 SER B OG  
2030 N N   . THR B 114 ? 0.532 0.570 0.429 0.021  -0.022 -0.028 110 THR B N   
2031 C CA  . THR B 114 ? 0.534 0.570 0.429 0.027  -0.021 -0.030 110 THR B CA  
2032 C C   . THR B 114 ? 0.484 0.533 0.391 0.030  -0.019 -0.030 110 THR B C   
2033 O O   . THR B 114 ? 0.469 0.525 0.383 0.026  -0.017 -0.028 110 THR B O   
2034 C CB  . THR B 114 ? 0.560 0.589 0.450 0.025  -0.022 -0.029 110 THR B CB  
2035 O OG1 . THR B 114 ? 0.583 0.619 0.481 0.020  -0.020 -0.026 110 THR B OG1 
2036 C CG2 . THR B 114 ? 0.561 0.575 0.437 0.023  -0.025 -0.030 110 THR B CG2 
2037 N N   . LEU B 115 ? 0.480 0.531 0.386 0.035  -0.018 -0.032 111 LEU B N   
2038 C CA  . LEU B 115 ? 0.470 0.532 0.384 0.037  -0.016 -0.033 111 LEU B CA  
2039 C C   . LEU B 115 ? 0.461 0.525 0.374 0.040  -0.016 -0.034 111 LEU B C   
2040 O O   . LEU B 115 ? 0.443 0.501 0.349 0.045  -0.017 -0.036 111 LEU B O   
2041 C CB  . LEU B 115 ? 0.490 0.555 0.402 0.039  -0.017 -0.034 111 LEU B CB  
2042 C CG  . LEU B 115 ? 0.488 0.564 0.408 0.039  -0.015 -0.034 111 LEU B CG  
2043 C CD1 . LEU B 115 ? 0.509 0.588 0.435 0.034  -0.014 -0.031 111 LEU B CD1 
2044 C CD2 . LEU B 115 ? 0.493 0.572 0.411 0.041  -0.016 -0.035 111 LEU B CD2 
2045 N N   . GLN B 116 ? 0.483 0.552 0.402 0.039  -0.014 -0.033 112 GLN B N   
2046 C CA  . GLN B 116 ? 0.480 0.552 0.399 0.042  -0.013 -0.034 112 GLN B CA  
2047 C C   . GLN B 116 ? 0.439 0.521 0.364 0.041  -0.012 -0.034 112 GLN B C   
2048 O O   . GLN B 116 ? 0.474 0.558 0.403 0.037  -0.011 -0.032 112 GLN B O   
2049 C CB  . GLN B 116 ? 0.537 0.604 0.456 0.040  -0.013 -0.033 112 GLN B CB  
2050 C CG  . GLN B 116 ? 0.596 0.651 0.508 0.039  -0.014 -0.032 112 GLN B CG  
2051 C CD  . GLN B 116 ? 0.647 0.701 0.561 0.035  -0.014 -0.031 112 GLN B CD  
2052 O OE1 . GLN B 116 ? 0.675 0.734 0.595 0.032  -0.012 -0.028 112 GLN B OE1 
2053 N NE2 . GLN B 116 ? 0.655 0.702 0.562 0.034  -0.016 -0.031 112 GLN B NE2 
2054 N N   . LEU B 117 ? 0.406 0.495 0.331 0.044  -0.013 -0.035 113 LEU B N   
2055 C CA  . LEU B 117 ? 0.404 0.504 0.334 0.041  -0.012 -0.035 113 LEU B CA  
2056 C C   . LEU B 117 ? 0.406 0.510 0.335 0.042  -0.012 -0.035 113 LEU B C   
2057 O O   . LEU B 117 ? 0.391 0.494 0.317 0.047  -0.013 -0.037 113 LEU B O   
2058 C CB  . LEU B 117 ? 0.439 0.548 0.369 0.043  -0.012 -0.036 113 LEU B CB  
2059 C CG  . LEU B 117 ? 0.468 0.573 0.396 0.044  -0.012 -0.036 113 LEU B CG  
2060 C CD1 . LEU B 117 ? 0.486 0.601 0.415 0.047  -0.012 -0.038 113 LEU B CD1 
2061 C CD2 . LEU B 117 ? 0.483 0.584 0.415 0.040  -0.011 -0.034 113 LEU B CD2 
2062 N N   . GLU B 118 ? 0.430 0.538 0.362 0.038  -0.011 -0.034 114 GLU B N   
2063 C CA  . GLU B 118 ? 0.498 0.613 0.430 0.037  -0.011 -0.034 114 GLU B CA  
2064 C C   . GLU B 118 ? 0.480 0.603 0.413 0.032  -0.011 -0.033 114 GLU B C   
2065 O O   . GLU B 118 ? 0.478 0.598 0.412 0.028  -0.010 -0.032 114 GLU B O   
2066 C CB  . GLU B 118 ? 0.566 0.672 0.496 0.034  -0.011 -0.033 114 GLU B CB  
2067 C CG  . GLU B 118 ? 0.633 0.731 0.560 0.038  -0.012 -0.034 114 GLU B CG  
2068 C CD  . GLU B 118 ? 0.693 0.781 0.617 0.035  -0.011 -0.032 114 GLU B CD  
2069 O OE1 . GLU B 118 ? 0.711 0.790 0.633 0.036  -0.010 -0.032 114 GLU B OE1 
2070 O OE2 . GLU B 118 ? 0.725 0.815 0.648 0.032  -0.011 -0.031 114 GLU B OE2 
2071 N N   . GLN B 119 ? 0.489 0.624 0.423 0.032  -0.012 -0.034 115 GLN B N   
2072 C CA  . GLN B 119 ? 0.554 0.700 0.489 0.026  -0.012 -0.033 115 GLN B CA  
2073 C C   . GLN B 119 ? 0.568 0.722 0.503 0.024  -0.013 -0.032 115 GLN B C   
2074 O O   . GLN B 119 ? 0.551 0.708 0.486 0.030  -0.014 -0.034 115 GLN B O   
2075 C CB  . GLN B 119 ? 0.629 0.786 0.567 0.028  -0.011 -0.033 115 GLN B CB  
2076 C CG  . GLN B 119 ? 0.661 0.827 0.599 0.021  -0.011 -0.032 115 GLN B CG  
2077 C CD  . GLN B 119 ? 0.680 0.847 0.620 0.023  -0.010 -0.033 115 GLN B CD  
2078 O OE1 . GLN B 119 ? 0.651 0.810 0.591 0.027  -0.010 -0.034 115 GLN B OE1 
2079 N NE2 . GLN B 119 ? 0.740 0.917 0.680 0.018  -0.009 -0.032 115 GLN B NE2 
2080 N N   . LYS B 120 ? 0.579 0.731 0.511 0.016  -0.013 -0.031 116 LYS B N   
2081 C CA  . LYS B 120 ? 0.594 0.755 0.525 0.013  -0.015 -0.030 116 LYS B CA  
2082 C C   . LYS B 120 ? 0.588 0.756 0.516 0.004  -0.015 -0.028 116 LYS B C   
2083 O O   . LYS B 120 ? 0.659 0.816 0.581 -0.002 -0.016 -0.027 116 LYS B O   
2084 C CB  . LYS B 120 ? 0.633 0.779 0.559 0.012  -0.016 -0.030 116 LYS B CB  
2085 C CG  . LYS B 120 ? 0.708 0.847 0.635 0.020  -0.016 -0.031 116 LYS B CG  
2086 C CD  . LYS B 120 ? 0.786 0.907 0.708 0.020  -0.015 -0.030 116 LYS B CD  
2087 C CE  . LYS B 120 ? 0.877 0.987 0.799 0.023  -0.013 -0.030 116 LYS B CE  
2088 N NZ  . LYS B 120 ? 0.889 0.995 0.811 0.019  -0.011 -0.029 116 LYS B NZ  
2089 N N   . GLY B 121 ? 0.651 0.834 0.584 0.003  -0.015 -0.028 117 GLY B N   
2090 C CA  . GLY B 121 ? 0.706 0.898 0.636 -0.007 -0.016 -0.027 117 GLY B CA  
2091 C C   . GLY B 121 ? 0.761 0.974 0.693 -0.009 -0.017 -0.026 117 GLY B C   
2092 O O   . GLY B 121 ? 0.798 1.017 0.734 -0.002 -0.018 -0.027 117 GLY B O   
2093 N N   . ARG B 122 ? 0.858 1.083 0.789 -0.019 -0.018 -0.024 118 ARG B N   
2094 C CA  . ARG B 122 ? 0.929 1.177 0.862 -0.022 -0.020 -0.023 118 ARG B CA  
2095 C C   . ARG B 122 ? 0.888 1.157 0.830 -0.013 -0.019 -0.025 118 ARG B C   
2096 O O   . ARG B 122 ? 0.969 1.256 0.916 -0.009 -0.020 -0.025 118 ARG B O   
2097 C CB  . ARG B 122 ? 1.032 1.284 0.959 -0.037 -0.021 -0.020 118 ARG B CB  
2098 C CG  . ARG B 122 ? 1.202 1.470 1.129 -0.042 -0.024 -0.019 118 ARG B CG  
2099 C CD  . ARG B 122 ? 1.292 1.574 1.215 -0.057 -0.026 -0.016 118 ARG B CD  
2100 N NE  . ARG B 122 ? 1.407 1.688 1.329 -0.060 -0.024 -0.016 118 ARG B NE  
2101 C CZ  . ARG B 122 ? 1.414 1.716 1.338 -0.067 -0.023 -0.014 118 ARG B CZ  
2102 N NH1 . ARG B 122 ? 1.459 1.788 1.387 -0.071 -0.025 -0.013 118 ARG B NH1 
2103 N NH2 . ARG B 122 ? 1.358 1.655 1.280 -0.069 -0.021 -0.014 118 ARG B NH2 
2104 N N   . VAL B 123 ? 0.774 1.039 0.718 -0.010 -0.017 -0.026 119 VAL B N   
2105 C CA  . VAL B 123 ? 0.742 1.026 0.692 -0.004 -0.015 -0.027 119 VAL B CA  
2106 C C   . VAL B 123 ? 0.672 0.951 0.625 0.011  -0.015 -0.030 119 VAL B C   
2107 O O   . VAL B 123 ? 0.666 0.963 0.623 0.019  -0.014 -0.031 119 VAL B O   
2108 C CB  . VAL B 123 ? 0.794 1.079 0.742 -0.010 -0.014 -0.026 119 VAL B CB  
2109 C CG1 . VAL B 123 ? 0.802 1.087 0.753 -0.001 -0.011 -0.028 119 VAL B CG1 
2110 C CG2 . VAL B 123 ? 0.733 1.042 0.682 -0.020 -0.014 -0.024 119 VAL B CG2 
2111 N N   . LEU B 124 ? 0.604 0.860 0.553 0.014  -0.015 -0.031 120 LEU B N   
2112 C CA  . LEU B 124 ? 0.547 0.793 0.496 0.026  -0.014 -0.033 120 LEU B CA  
2113 C C   . LEU B 124 ? 0.535 0.761 0.481 0.027  -0.015 -0.033 120 LEU B C   
2114 O O   . LEU B 124 ? 0.549 0.759 0.492 0.021  -0.015 -0.032 120 LEU B O   
2115 C CB  . LEU B 124 ? 0.542 0.779 0.491 0.029  -0.013 -0.034 120 LEU B CB  
2116 C CG  . LEU B 124 ? 0.537 0.758 0.483 0.038  -0.013 -0.036 120 LEU B CG  
2117 C CD1 . LEU B 124 ? 0.553 0.783 0.500 0.048  -0.014 -0.038 120 LEU B CD1 
2118 C CD2 . LEU B 124 ? 0.528 0.744 0.474 0.040  -0.011 -0.037 120 LEU B CD2 
2119 N N   . LYS B 125 ? 0.542 0.767 0.488 0.035  -0.017 -0.035 121 LYS B N   
2120 C CA  . LYS B 125 ? 0.552 0.757 0.494 0.037  -0.017 -0.035 121 LYS B CA  
2121 C C   . LYS B 125 ? 0.500 0.695 0.440 0.047  -0.017 -0.037 121 LYS B C   
2122 O O   . LYS B 125 ? 0.499 0.704 0.439 0.055  -0.018 -0.039 121 LYS B O   
2123 C CB  . LYS B 125 ? 0.599 0.809 0.540 0.036  -0.019 -0.035 121 LYS B CB  
2124 C CG  . LYS B 125 ? 0.696 0.914 0.637 0.025  -0.020 -0.032 121 LYS B CG  
2125 C CD  . LYS B 125 ? 0.760 0.980 0.699 0.022  -0.022 -0.031 121 LYS B CD  
2126 C CE  . LYS B 125 ? 0.801 1.047 0.745 0.024  -0.024 -0.031 121 LYS B CE  
2127 N NZ  . LYS B 125 ? 0.843 1.109 0.791 0.025  -0.023 -0.031 121 LYS B NZ  
2128 N N   . MET B 126 ? 0.465 0.642 0.402 0.046  -0.016 -0.037 122 MET B N   
2129 C CA  . MET B 126 ? 0.465 0.631 0.399 0.054  -0.016 -0.039 122 MET B CA  
2130 C C   . MET B 126 ? 0.446 0.593 0.377 0.053  -0.016 -0.039 122 MET B C   
2131 O O   . MET B 126 ? 0.446 0.587 0.378 0.046  -0.015 -0.037 122 MET B O   
2132 C CB  . MET B 126 ? 0.489 0.661 0.424 0.057  -0.015 -0.040 122 MET B CB  
2133 C CG  . MET B 126 ? 0.521 0.687 0.458 0.050  -0.014 -0.039 122 MET B CG  
2134 S SD  . MET B 126 ? 0.580 0.726 0.513 0.052  -0.013 -0.039 122 MET B SD  
2135 C CE  . MET B 126 ? 0.574 0.718 0.510 0.044  -0.012 -0.037 122 MET B CE  
2136 N N   . ASP B 127 ? 0.447 0.583 0.373 0.059  -0.017 -0.040 123 ASP B N   
2137 C CA  . ASP B 127 ? 0.474 0.593 0.397 0.058  -0.016 -0.040 123 ASP B CA  
2138 C C   . ASP B 127 ? 0.450 0.563 0.367 0.063  -0.017 -0.041 123 ASP B C   
2139 O O   . ASP B 127 ? 0.461 0.578 0.374 0.070  -0.018 -0.043 123 ASP B O   
2140 C CB  . ASP B 127 ? 0.541 0.648 0.458 0.059  -0.017 -0.040 123 ASP B CB  
2141 C CG  . ASP B 127 ? 0.621 0.736 0.541 0.057  -0.018 -0.039 123 ASP B CG  
2142 O OD1 . ASP B 127 ? 0.710 0.833 0.628 0.062  -0.019 -0.040 123 ASP B OD1 
2143 O OD2 . ASP B 127 ? 0.752 0.864 0.674 0.051  -0.017 -0.038 123 ASP B OD2 
2144 N N   . GLU B 128 ? 0.438 0.540 0.354 0.060  -0.016 -0.041 124 GLU B N   
2145 C CA  . GLU B 128 ? 0.429 0.522 0.338 0.065  -0.018 -0.042 124 GLU B CA  
2146 C C   . GLU B 128 ? 0.399 0.478 0.305 0.060  -0.018 -0.041 124 GLU B C   
2147 O O   . GLU B 128 ? 0.387 0.467 0.299 0.054  -0.016 -0.039 124 GLU B O   
2148 C CB  . GLU B 128 ? 0.451 0.551 0.362 0.064  -0.017 -0.042 124 GLU B CB  
2149 C CG  . GLU B 128 ? 0.479 0.595 0.392 0.069  -0.017 -0.043 124 GLU B CG  
2150 C CD  . GLU B 128 ? 0.507 0.626 0.419 0.070  -0.016 -0.044 124 GLU B CD  
2151 O OE1 . GLU B 128 ? 0.527 0.648 0.445 0.064  -0.015 -0.042 124 GLU B OE1 
2152 O OE2 . GLU B 128 ? 0.550 0.669 0.456 0.077  -0.017 -0.046 124 GLU B OE2 
2153 N N   . ALA B 129 ? 0.388 0.454 0.284 0.063  -0.019 -0.042 125 ALA B N   
2154 C CA  . ALA B 129 ? 0.407 0.460 0.299 0.058  -0.020 -0.040 125 ALA B CA  
2155 C C   . ALA B 129 ? 0.426 0.470 0.308 0.061  -0.022 -0.042 125 ALA B C   
2156 O O   . ALA B 129 ? 0.432 0.472 0.306 0.069  -0.023 -0.044 125 ALA B O   
2157 C CB  . ALA B 129 ? 0.393 0.439 0.284 0.056  -0.020 -0.040 125 ALA B CB  
2158 N N   . PHE B 130 ? 0.452 0.491 0.334 0.057  -0.022 -0.041 126 PHE B N   
2159 C CA  . PHE B 130 ? 0.479 0.507 0.349 0.059  -0.024 -0.042 126 PHE B CA  
2160 C C   . PHE B 130 ? 0.479 0.505 0.352 0.051  -0.024 -0.039 126 PHE B C   
2161 O O   . PHE B 130 ? 0.454 0.488 0.338 0.046  -0.022 -0.037 126 PHE B O   
2162 C CB  . PHE B 130 ? 0.481 0.516 0.350 0.066  -0.024 -0.044 126 PHE B CB  
2163 C CG  . PHE B 130 ? 0.476 0.529 0.359 0.063  -0.022 -0.043 126 PHE B CG  
2164 C CD1 . PHE B 130 ? 0.458 0.524 0.350 0.063  -0.020 -0.042 126 PHE B CD1 
2165 C CD2 . PHE B 130 ? 0.494 0.547 0.378 0.060  -0.022 -0.042 126 PHE B CD2 
2166 C CE1 . PHE B 130 ? 0.462 0.541 0.364 0.060  -0.018 -0.042 126 PHE B CE1 
2167 C CE2 . PHE B 130 ? 0.478 0.544 0.372 0.058  -0.019 -0.041 126 PHE B CE2 
2168 C CZ  . PHE B 130 ? 0.465 0.544 0.368 0.057  -0.018 -0.041 126 PHE B CZ  
2169 N N   . SER B 131 ? 0.504 0.520 0.367 0.051  -0.027 -0.040 127 SER B N   
2170 C CA  . SER B 131 ? 0.523 0.534 0.385 0.043  -0.027 -0.038 127 SER B CA  
2171 C C   . SER B 131 ? 0.515 0.532 0.379 0.045  -0.027 -0.038 127 SER B C   
2172 O O   . SER B 131 ? 0.508 0.525 0.367 0.052  -0.027 -0.041 127 SER B O   
2173 C CB  . SER B 131 ? 0.567 0.560 0.414 0.040  -0.031 -0.038 127 SER B CB  
2174 O OG  . SER B 131 ? 0.637 0.627 0.485 0.036  -0.030 -0.036 127 SER B OG  
2175 N N   . ILE B 132 ? 0.506 0.529 0.377 0.038  -0.027 -0.036 128 ILE B N   
2176 C CA  . ILE B 132 ? 0.520 0.546 0.392 0.039  -0.027 -0.037 128 ILE B CA  
2177 C C   . ILE B 132 ? 0.548 0.567 0.415 0.032  -0.030 -0.035 128 ILE B C   
2178 O O   . ILE B 132 ? 0.559 0.574 0.426 0.026  -0.030 -0.033 128 ILE B O   
2179 C CB  . ILE B 132 ? 0.520 0.563 0.406 0.039  -0.024 -0.036 128 ILE B CB  
2180 C CG1 . ILE B 132 ? 0.512 0.562 0.409 0.033  -0.023 -0.033 128 ILE B CG1 
2181 C CG2 . ILE B 132 ? 0.511 0.561 0.399 0.045  -0.022 -0.038 128 ILE B CG2 
2182 C CD1 . ILE B 132 ? 0.502 0.565 0.409 0.033  -0.020 -0.033 128 ILE B CD1 
2183 N N   . SER B 133 ? 0.550 0.566 0.412 0.033  -0.031 -0.036 129 SER B N   
2184 C CA  . SER B 133 ? 0.581 0.588 0.435 0.026  -0.034 -0.034 129 SER B CA  
2185 C C   . SER B 133 ? 0.582 0.603 0.451 0.020  -0.033 -0.031 129 SER B C   
2186 O O   . SER B 133 ? 0.529 0.563 0.411 0.022  -0.029 -0.031 129 SER B O   
2187 C CB  . SER B 133 ? 0.575 0.575 0.419 0.030  -0.035 -0.036 129 SER B CB  
2188 O OG  . SER B 133 ? 0.540 0.554 0.395 0.032  -0.033 -0.036 129 SER B OG  
2189 N N   . LEU B 134 ? 0.636 0.653 0.502 0.013  -0.035 -0.029 130 LEU B N   
2190 C CA  . LEU B 134 ? 0.666 0.696 0.543 0.007  -0.035 -0.026 130 LEU B CA  
2191 C C   . LEU B 134 ? 0.635 0.672 0.518 0.011  -0.033 -0.027 130 LEU B C   
2192 O O   . LEU B 134 ? 0.647 0.698 0.543 0.010  -0.031 -0.025 130 LEU B O   
2193 C CB  . LEU B 134 ? 0.726 0.750 0.596 -0.001 -0.039 -0.023 130 LEU B CB  
2194 C CG  . LEU B 134 ? 0.789 0.807 0.655 -0.007 -0.040 -0.021 130 LEU B CG  
2195 C CD1 . LEU B 134 ? 0.803 0.812 0.658 -0.016 -0.044 -0.019 130 LEU B CD1 
2196 C CD2 . LEU B 134 ? 0.802 0.837 0.684 -0.008 -0.037 -0.019 130 LEU B CD2 
2197 N N   . GLU B 135 ? 0.628 0.657 0.501 0.015  -0.034 -0.029 131 GLU B N   
2198 C CA  . GLU B 135 ? 0.656 0.692 0.534 0.018  -0.033 -0.030 131 GLU B CA  
2199 C C   . GLU B 135 ? 0.625 0.673 0.513 0.023  -0.029 -0.031 131 GLU B C   
2200 O O   . GLU B 135 ? 0.574 0.633 0.472 0.023  -0.027 -0.030 131 GLU B O   
2201 C CB  . GLU B 135 ? 0.748 0.773 0.612 0.021  -0.035 -0.032 131 GLU B CB  
2202 C CG  . GLU B 135 ? 0.823 0.854 0.689 0.027  -0.032 -0.034 131 GLU B CG  
2203 C CD  . GLU B 135 ? 0.892 0.928 0.761 0.025  -0.033 -0.033 131 GLU B CD  
2204 O OE1 . GLU B 135 ? 0.878 0.921 0.756 0.019  -0.033 -0.031 131 GLU B OE1 
2205 O OE2 . GLU B 135 ? 1.003 1.035 0.865 0.029  -0.032 -0.035 131 GLU B OE2 
2206 N N   . GLN B 136 ? 0.565 0.610 0.450 0.028  -0.028 -0.033 132 GLN B N   
2207 C CA  . GLN B 136 ? 0.544 0.599 0.437 0.032  -0.025 -0.034 132 GLN B CA  
2208 C C   . GLN B 136 ? 0.511 0.576 0.416 0.028  -0.023 -0.031 132 GLN B C   
2209 O O   . GLN B 136 ? 0.498 0.571 0.410 0.029  -0.021 -0.031 132 GLN B O   
2210 C CB  . GLN B 136 ? 0.554 0.604 0.441 0.037  -0.025 -0.036 132 GLN B CB  
2211 C CG  . GLN B 136 ? 0.547 0.591 0.423 0.044  -0.025 -0.039 132 GLN B CG  
2212 C CD  . GLN B 136 ? 0.554 0.591 0.422 0.050  -0.026 -0.041 132 GLN B CD  
2213 O OE1 . GLN B 136 ? 0.597 0.626 0.461 0.048  -0.027 -0.040 132 GLN B OE1 
2214 N NE2 . GLN B 136 ? 0.550 0.593 0.416 0.057  -0.024 -0.043 132 GLN B NE2 
2215 N N   . THR B 137 ? 0.497 0.558 0.403 0.024  -0.024 -0.029 133 THR B N   
2216 C CA  . THR B 137 ? 0.485 0.555 0.401 0.021  -0.023 -0.027 133 THR B CA  
2217 C C   . THR B 137 ? 0.474 0.551 0.396 0.019  -0.022 -0.025 133 THR B C   
2218 O O   . THR B 137 ? 0.433 0.518 0.363 0.020  -0.020 -0.024 133 THR B O   
2219 C CB  . THR B 137 ? 0.465 0.531 0.379 0.016  -0.024 -0.025 133 THR B CB  
2220 O OG1 . THR B 137 ? 0.447 0.503 0.353 0.017  -0.025 -0.026 133 THR B OG1 
2221 C CG2 . THR B 137 ? 0.442 0.517 0.366 0.014  -0.022 -0.022 133 THR B CG2 
2222 N N   . GLU B 138 ? 0.508 0.583 0.427 0.017  -0.024 -0.025 134 GLU B N   
2223 C CA  . GLU B 138 ? 0.546 0.627 0.469 0.016  -0.024 -0.023 134 GLU B CA  
2224 C C   . GLU B 138 ? 0.488 0.572 0.412 0.019  -0.022 -0.025 134 GLU B C   
2225 O O   . GLU B 138 ? 0.439 0.530 0.369 0.019  -0.020 -0.024 134 GLU B O   
2226 C CB  . GLU B 138 ? 0.647 0.722 0.563 0.013  -0.028 -0.023 134 GLU B CB  
2227 C CG  . GLU B 138 ? 0.733 0.811 0.652 0.007  -0.030 -0.020 134 GLU B CG  
2228 C CD  . GLU B 138 ? 0.849 0.918 0.759 0.002  -0.033 -0.019 134 GLU B CD  
2229 O OE1 . GLU B 138 ? 0.936 1.004 0.846 -0.000 -0.034 -0.018 134 GLU B OE1 
2230 O OE2 . GLU B 138 ? 0.931 0.994 0.833 0.001  -0.036 -0.020 134 GLU B OE2 
2231 N N   . GLU B 139 ? 0.503 0.584 0.422 0.023  -0.022 -0.028 135 GLU B N   
2232 C CA  . GLU B 139 ? 0.522 0.608 0.442 0.025  -0.019 -0.029 135 GLU B CA  
2233 C C   . GLU B 139 ? 0.497 0.590 0.424 0.026  -0.017 -0.029 135 GLU B C   
2234 O O   . GLU B 139 ? 0.443 0.541 0.374 0.025  -0.016 -0.028 135 GLU B O   
2235 C CB  . GLU B 139 ? 0.548 0.632 0.462 0.030  -0.019 -0.032 135 GLU B CB  
2236 C CG  . GLU B 139 ? 0.580 0.659 0.486 0.030  -0.021 -0.033 135 GLU B CG  
2237 C CD  . GLU B 139 ? 0.586 0.658 0.482 0.035  -0.022 -0.036 135 GLU B CD  
2238 O OE1 . GLU B 139 ? 0.580 0.654 0.476 0.039  -0.021 -0.037 135 GLU B OE1 
2239 O OE2 . GLU B 139 ? 0.656 0.719 0.543 0.035  -0.024 -0.036 135 GLU B OE2 
2240 N N   . LEU B 140 ? 0.499 0.590 0.427 0.027  -0.017 -0.029 136 LEU B N   
2241 C CA  . LEU B 140 ? 0.464 0.559 0.396 0.027  -0.015 -0.029 136 LEU B CA  
2242 C C   . LEU B 140 ? 0.446 0.542 0.383 0.024  -0.014 -0.026 136 LEU B C   
2243 O O   . LEU B 140 ? 0.424 0.523 0.363 0.024  -0.012 -0.026 136 LEU B O   
2244 C CB  . LEU B 140 ? 0.469 0.560 0.400 0.028  -0.015 -0.029 136 LEU B CB  
2245 C CG  . LEU B 140 ? 0.488 0.583 0.422 0.029  -0.013 -0.029 136 LEU B CG  
2246 C CD1 . LEU B 140 ? 0.483 0.584 0.416 0.031  -0.012 -0.031 136 LEU B CD1 
2247 C CD2 . LEU B 140 ? 0.505 0.595 0.437 0.031  -0.014 -0.030 136 LEU B CD2 
2248 N N   . THR B 141 ? 0.415 0.510 0.352 0.022  -0.016 -0.024 137 THR B N   
2249 C CA  . THR B 141 ? 0.398 0.496 0.340 0.021  -0.015 -0.021 137 THR B CA  
2250 C C   . THR B 141 ? 0.409 0.509 0.351 0.022  -0.014 -0.021 137 THR B C   
2251 O O   . THR B 141 ? 0.424 0.526 0.368 0.022  -0.013 -0.020 137 THR B O   
2252 C CB  . THR B 141 ? 0.391 0.490 0.335 0.019  -0.017 -0.019 137 THR B CB  
2253 O OG1 . THR B 141 ? 0.385 0.482 0.328 0.018  -0.017 -0.019 137 THR B OG1 
2254 C CG2 . THR B 141 ? 0.386 0.490 0.334 0.019  -0.016 -0.017 137 THR B CG2 
2255 N N   . GLU B 142 ? 0.422 0.522 0.362 0.021  -0.015 -0.022 138 GLU B N   
2256 C CA  . GLU B 142 ? 0.446 0.547 0.385 0.021  -0.015 -0.022 138 GLU B CA  
2257 C C   . GLU B 142 ? 0.427 0.529 0.365 0.021  -0.013 -0.023 138 GLU B C   
2258 O O   . GLU B 142 ? 0.418 0.519 0.354 0.020  -0.012 -0.022 138 GLU B O   
2259 C CB  . GLU B 142 ? 0.517 0.617 0.452 0.020  -0.016 -0.023 138 GLU B CB  
2260 C CG  . GLU B 142 ? 0.572 0.672 0.508 0.018  -0.019 -0.021 138 GLU B CG  
2261 C CD  . GLU B 142 ? 0.684 0.787 0.623 0.018  -0.019 -0.018 138 GLU B CD  
2262 O OE1 . GLU B 142 ? 0.710 0.812 0.648 0.019  -0.018 -0.018 138 GLU B OE1 
2263 O OE2 . GLU B 142 ? 0.672 0.777 0.614 0.017  -0.021 -0.016 138 GLU B OE2 
2264 N N   . MET B 143 ? 0.419 0.521 0.356 0.022  -0.012 -0.025 139 MET B N   
2265 C CA  . MET B 143 ? 0.395 0.500 0.331 0.021  -0.010 -0.025 139 MET B CA  
2266 C C   . MET B 143 ? 0.378 0.481 0.315 0.021  -0.009 -0.024 139 MET B C   
2267 O O   . MET B 143 ? 0.368 0.470 0.302 0.019  -0.008 -0.024 139 MET B O   
2268 C CB  . MET B 143 ? 0.411 0.519 0.346 0.023  -0.010 -0.028 139 MET B CB  
2269 C CG  . MET B 143 ? 0.428 0.539 0.361 0.024  -0.011 -0.029 139 MET B CG  
2270 S SD  . MET B 143 ? 0.434 0.549 0.365 0.021  -0.010 -0.029 139 MET B SD  
2271 C CE  . MET B 143 ? 0.435 0.558 0.366 0.019  -0.008 -0.030 139 MET B CE  
2272 N N   . PHE B 144 ? 0.371 0.472 0.310 0.022  -0.010 -0.023 140 PHE B N   
2273 C CA  . PHE B 144 ? 0.366 0.464 0.306 0.023  -0.008 -0.022 140 PHE B CA  
2274 C C   . PHE B 144 ? 0.361 0.457 0.300 0.024  -0.008 -0.019 140 PHE B C   
2275 O O   . PHE B 144 ? 0.369 0.461 0.304 0.024  -0.007 -0.019 140 PHE B O   
2276 C CB  . PHE B 144 ? 0.370 0.469 0.314 0.024  -0.009 -0.021 140 PHE B CB  
2277 C CG  . PHE B 144 ? 0.391 0.488 0.335 0.026  -0.008 -0.019 140 PHE B CG  
2278 C CD1 . PHE B 144 ? 0.374 0.474 0.322 0.026  -0.008 -0.017 140 PHE B CD1 
2279 C CD2 . PHE B 144 ? 0.389 0.483 0.332 0.026  -0.006 -0.020 140 PHE B CD2 
2280 C CE1 . PHE B 144 ? 0.385 0.485 0.333 0.028  -0.007 -0.015 140 PHE B CE1 
2281 C CE2 . PHE B 144 ? 0.378 0.472 0.322 0.028  -0.005 -0.018 140 PHE B CE2 
2282 C CZ  . PHE B 144 ? 0.391 0.487 0.337 0.029  -0.005 -0.016 140 PHE B CZ  
2283 N N   . TYR B 145 ? 0.348 0.446 0.288 0.024  -0.009 -0.018 141 TYR B N   
2284 C CA  . TYR B 145 ? 0.346 0.441 0.283 0.025  -0.010 -0.016 141 TYR B CA  
2285 C C   . TYR B 145 ? 0.335 0.426 0.266 0.024  -0.009 -0.017 141 TYR B C   
2286 O O   . TYR B 145 ? 0.337 0.422 0.263 0.025  -0.008 -0.016 141 TYR B O   
2287 C CB  . TYR B 145 ? 0.367 0.467 0.308 0.025  -0.011 -0.015 141 TYR B CB  
2288 C CG  . TYR B 145 ? 0.382 0.487 0.328 0.026  -0.012 -0.014 141 TYR B CG  
2289 C CD1 . TYR B 145 ? 0.386 0.492 0.334 0.028  -0.011 -0.013 141 TYR B CD1 
2290 C CD2 . TYR B 145 ? 0.376 0.484 0.324 0.024  -0.014 -0.014 141 TYR B CD2 
2291 C CE1 . TYR B 145 ? 0.385 0.496 0.338 0.027  -0.011 -0.011 141 TYR B CE1 
2292 C CE2 . TYR B 145 ? 0.382 0.494 0.334 0.023  -0.015 -0.012 141 TYR B CE2 
2293 C CZ  . TYR B 145 ? 0.396 0.511 0.350 0.024  -0.014 -0.011 141 TYR B CZ  
2294 O OH  . TYR B 145 ? 0.407 0.527 0.365 0.022  -0.015 -0.009 141 TYR B OH  
2295 N N   . GLU B 146 ? 0.329 0.422 0.260 0.021  -0.009 -0.019 142 GLU B N   
2296 C CA  . GLU B 146 ? 0.339 0.428 0.262 0.018  -0.009 -0.019 142 GLU B CA  
2297 C C   . GLU B 146 ? 0.344 0.429 0.264 0.017  -0.008 -0.019 142 GLU B C   
2298 O O   . GLU B 146 ? 0.360 0.438 0.272 0.016  -0.007 -0.018 142 GLU B O   
2299 C CB  . GLU B 146 ? 0.339 0.434 0.264 0.016  -0.009 -0.021 142 GLU B CB  
2300 C CG  . GLU B 146 ? 0.338 0.433 0.257 0.012  -0.008 -0.022 142 GLU B CG  
2301 C CD  . GLU B 146 ? 0.340 0.429 0.252 0.009  -0.009 -0.021 142 GLU B CD  
2302 O OE1 . GLU B 146 ? 0.330 0.413 0.240 0.012  -0.009 -0.019 142 GLU B OE1 
2303 O OE2 . GLU B 146 ? 0.341 0.430 0.248 0.005  -0.008 -0.021 142 GLU B OE2 
2304 N N   . LEU B 147 ? 0.357 0.445 0.280 0.018  -0.007 -0.020 143 LEU B N   
2305 C CA  . LEU B 147 ? 0.337 0.420 0.256 0.017  -0.006 -0.020 143 LEU B CA  
2306 C C   . LEU B 147 ? 0.317 0.393 0.233 0.020  -0.005 -0.018 143 LEU B C   
2307 O O   . LEU B 147 ? 0.317 0.384 0.224 0.020  -0.005 -0.017 143 LEU B O   
2308 C CB  . LEU B 147 ? 0.336 0.423 0.260 0.018  -0.005 -0.021 143 LEU B CB  
2309 C CG  . LEU B 147 ? 0.352 0.435 0.272 0.016  -0.005 -0.021 143 LEU B CG  
2310 C CD1 . LEU B 147 ? 0.350 0.433 0.264 0.011  -0.005 -0.021 143 LEU B CD1 
2311 C CD2 . LEU B 147 ? 0.340 0.425 0.264 0.018  -0.004 -0.021 143 LEU B CD2 
2312 N N   . GLY B 148 ? 0.309 0.387 0.229 0.024  -0.006 -0.017 144 GLY B N   
2313 C CA  . GLY B 148 ? 0.320 0.394 0.238 0.029  -0.005 -0.014 144 GLY B CA  
2314 C C   . GLY B 148 ? 0.342 0.407 0.251 0.030  -0.005 -0.013 144 GLY B C   
2315 O O   . GLY B 148 ? 0.329 0.387 0.232 0.034  -0.004 -0.012 144 GLY B O   
2316 N N   . ARG B 149 ? 0.386 0.449 0.290 0.026  -0.006 -0.014 145 ARG B N   
2317 C CA  . ARG B 149 ? 0.400 0.453 0.293 0.026  -0.007 -0.013 145 ARG B CA  
2318 C C   . ARG B 149 ? 0.407 0.448 0.288 0.024  -0.006 -0.013 145 ARG B C   
2319 O O   . ARG B 149 ? 0.417 0.446 0.287 0.026  -0.007 -0.012 145 ARG B O   
2320 C CB  . ARG B 149 ? 0.431 0.486 0.323 0.021  -0.008 -0.014 145 ARG B CB  
2321 C CG  . ARG B 149 ? 0.438 0.499 0.336 0.023  -0.009 -0.014 145 ARG B CG  
2322 C CD  . ARG B 149 ? 0.429 0.494 0.327 0.017  -0.010 -0.015 145 ARG B CD  
2323 N NE  . ARG B 149 ? 0.434 0.490 0.320 0.013  -0.010 -0.015 145 ARG B NE  
2324 C CZ  . ARG B 149 ? 0.433 0.490 0.315 0.007  -0.009 -0.016 145 ARG B CZ  
2325 N NH1 . ARG B 149 ? 0.404 0.472 0.295 0.005  -0.009 -0.018 145 ARG B NH1 
2326 N NH2 . ARG B 149 ? 0.451 0.497 0.321 0.003  -0.010 -0.015 145 ARG B NH2 
2327 N N   . PHE B 150 ? 0.420 0.463 0.304 0.021  -0.005 -0.014 146 PHE B N   
2328 C CA  . PHE B 150 ? 0.432 0.464 0.304 0.018  -0.005 -0.014 146 PHE B CA  
2329 C C   . PHE B 150 ? 0.420 0.445 0.288 0.024  -0.004 -0.013 146 PHE B C   
2330 O O   . PHE B 150 ? 0.430 0.444 0.288 0.022  -0.003 -0.013 146 PHE B O   
2331 C CB  . PHE B 150 ? 0.439 0.477 0.314 0.012  -0.005 -0.015 146 PHE B CB  
2332 C CG  . PHE B 150 ? 0.432 0.476 0.307 0.006  -0.006 -0.016 146 PHE B CG  
2333 C CD1 . PHE B 150 ? 0.458 0.491 0.319 0.001  -0.007 -0.015 146 PHE B CD1 
2334 C CD2 . PHE B 150 ? 0.419 0.476 0.306 0.007  -0.006 -0.017 146 PHE B CD2 
2335 C CE1 . PHE B 150 ? 0.462 0.500 0.323 -0.004 -0.008 -0.016 146 PHE B CE1 
2336 C CE2 . PHE B 150 ? 0.415 0.476 0.301 0.003  -0.007 -0.018 146 PHE B CE2 
2337 C CZ  . PHE B 150 ? 0.437 0.489 0.311 -0.002 -0.007 -0.017 146 PHE B CZ  
2338 N N   . VAL B 151 ? 0.401 0.432 0.278 0.031  -0.003 -0.012 147 VAL B N   
2339 C CA  . VAL B 151 ? 0.408 0.434 0.282 0.037  -0.001 -0.011 147 VAL B CA  
2340 C C   . VAL B 151 ? 0.422 0.431 0.279 0.040  -0.001 -0.009 147 VAL B C   
2341 O O   . VAL B 151 ? 0.403 0.410 0.256 0.042  -0.002 -0.009 147 VAL B O   
2342 C CB  . VAL B 151 ? 0.412 0.451 0.299 0.043  -0.001 -0.010 147 VAL B CB  
2343 C CG1 . VAL B 151 ? 0.425 0.460 0.308 0.051  0.001  -0.008 147 VAL B CG1 
2344 C CG2 . VAL B 151 ? 0.396 0.447 0.296 0.039  -0.001 -0.011 147 VAL B CG2 
2345 N N   . VAL B 152 ? 0.441 0.438 0.287 0.042  -0.000 -0.009 148 VAL B N   
2346 C CA  . VAL B 152 ? 0.484 0.461 0.311 0.046  -0.000 -0.008 148 VAL B CA  
2347 C C   . VAL B 152 ? 0.508 0.485 0.335 0.057  0.002  -0.006 148 VAL B C   
2348 O O   . VAL B 152 ? 0.491 0.478 0.329 0.058  0.004  -0.007 148 VAL B O   
2349 C CB  . VAL B 152 ? 0.485 0.445 0.296 0.039  -0.001 -0.008 148 VAL B CB  
2350 C CG1 . VAL B 152 ? 0.503 0.467 0.315 0.029  -0.003 -0.009 148 VAL B CG1 
2351 C CG2 . VAL B 152 ? 0.482 0.443 0.295 0.038  0.000  -0.009 148 VAL B CG2 
2352 N N   . ASP B 153 ? 0.598 0.563 0.411 0.065  0.002  -0.005 149 ASP B N   
2353 C CA  . ASP B 153 ? 0.673 0.636 0.483 0.076  0.005  -0.003 149 ASP B CA  
2354 C C   . ASP B 153 ? 0.708 0.650 0.499 0.078  0.005  -0.003 149 ASP B C   
2355 O O   . ASP B 153 ? 0.761 0.707 0.555 0.083  0.008  -0.003 149 ASP B O   
2356 C CB  . ASP B 153 ? 0.713 0.679 0.521 0.086  0.004  -0.001 149 ASP B CB  
2357 C CG  . ASP B 153 ? 0.700 0.689 0.529 0.084  0.003  -0.001 149 ASP B CG  
2358 O OD1 . ASP B 153 ? 0.659 0.665 0.505 0.084  0.005  -0.001 149 ASP B OD1 
2359 O OD2 . ASP B 153 ? 0.740 0.729 0.569 0.081  0.001  -0.001 149 ASP B OD2 
2360 N N   . GLY B 154 ? 0.712 0.634 0.484 0.072  0.003  -0.004 150 GLY B N   
2361 C CA  . GLY B 154 ? 0.760 0.661 0.513 0.070  0.004  -0.004 150 GLY B CA  
2362 C C   . GLY B 154 ? 0.731 0.638 0.493 0.064  0.004  -0.005 150 GLY B C   
2363 O O   . GLY B 154 ? 0.701 0.630 0.484 0.060  0.005  -0.006 150 GLY B O   
2364 N N   . THR B 155 ? 0.684 0.573 0.429 0.065  0.005  -0.005 151 THR B N   
2365 C CA  . THR B 155 ? 0.704 0.591 0.449 0.055  0.004  -0.006 151 THR B CA  
2366 C C   . THR B 155 ? 0.780 0.644 0.502 0.047  0.001  -0.006 151 THR B C   
2367 O O   . THR B 155 ? 0.770 0.632 0.490 0.038  0.000  -0.007 151 THR B O   
2368 C CB  . THR B 155 ? 0.671 0.557 0.417 0.062  0.007  -0.006 151 THR B CB  
2369 O OG1 . THR B 155 ? 0.655 0.520 0.379 0.071  0.008  -0.005 151 THR B OG1 
2370 C CG2 . THR B 155 ? 0.660 0.571 0.430 0.068  0.009  -0.006 151 THR B CG2 
2371 N N   . LYS B 156 ? 0.890 0.736 0.593 0.049  0.000  -0.005 152 LYS B N   
2372 C CA  . LYS B 156 ? 0.988 0.812 0.668 0.039  -0.003 -0.005 152 LYS B CA  
2373 C C   . LYS B 156 ? 0.928 0.768 0.622 0.030  -0.005 -0.006 152 LYS B C   
2374 O O   . LYS B 156 ? 1.041 0.890 0.743 0.036  -0.004 -0.005 152 LYS B O   
2375 C CB  . LYS B 156 ? 1.124 0.919 0.776 0.046  -0.003 -0.004 152 LYS B CB  
2376 C CG  . LYS B 156 ? 1.196 0.976 0.834 0.058  -0.001 -0.003 152 LYS B CG  
2377 C CD  . LYS B 156 ? 1.242 1.007 0.865 0.072  -0.000 -0.002 152 LYS B CD  
2378 C CE  . LYS B 156 ? 1.246 1.027 0.883 0.076  -0.000 -0.002 152 LYS B CE  
2379 N NZ  . LYS B 156 ? 1.280 1.051 0.904 0.093  0.001  -0.001 152 LYS B NZ  
2380 N N   . GLY B 157 ? 0.824 0.670 0.521 0.017  -0.007 -0.006 153 GLY B N   
2381 C CA  . GLY B 157 ? 0.762 0.631 0.479 0.009  -0.007 -0.007 153 GLY B CA  
2382 C C   . GLY B 157 ? 0.734 0.619 0.464 0.001  -0.007 -0.008 153 GLY B C   
2383 O O   . GLY B 157 ? 0.685 0.575 0.423 0.007  -0.006 -0.009 153 GLY B O   
2384 N N   . GLU B 158 ? 0.708 0.602 0.441 -0.011 -0.009 -0.009 154 GLU B N   
2385 C CA  . GLU B 158 ? 0.680 0.595 0.430 -0.017 -0.010 -0.010 154 GLU B CA  
2386 C C   . GLU B 158 ? 0.584 0.522 0.360 -0.010 -0.008 -0.011 154 GLU B C   
2387 O O   . GLU B 158 ? 0.561 0.502 0.340 -0.006 -0.007 -0.011 154 GLU B O   
2388 C CB  . GLU B 158 ? 0.742 0.663 0.490 -0.031 -0.012 -0.009 154 GLU B CB  
2389 C CG  . GLU B 158 ? 0.847 0.748 0.571 -0.041 -0.015 -0.008 154 GLU B CG  
2390 C CD  . GLU B 158 ? 0.988 0.885 0.709 -0.043 -0.015 -0.008 154 GLU B CD  
2391 O OE1 . GLU B 158 ? 1.070 0.975 0.804 -0.034 -0.013 -0.009 154 GLU B OE1 
2392 O OE2 . GLU B 158 ? 1.049 0.935 0.753 -0.055 -0.018 -0.007 154 GLU B OE2 
2393 N N   . GLN B 159 ? 0.508 0.459 0.298 -0.007 -0.007 -0.012 155 GLN B N   
2394 C CA  . GLN B 159 ? 0.458 0.427 0.269 -0.000 -0.005 -0.013 155 GLN B CA  
2395 C C   . GLN B 159 ? 0.442 0.431 0.268 -0.006 -0.006 -0.014 155 GLN B C   
2396 O O   . GLN B 159 ? 0.482 0.470 0.303 -0.013 -0.007 -0.014 155 GLN B O   
2397 C CB  . GLN B 159 ? 0.442 0.406 0.253 0.008  -0.003 -0.013 155 GLN B CB  
2398 C CG  . GLN B 159 ? 0.460 0.407 0.258 0.015  -0.002 -0.011 155 GLN B CG  
2399 C CD  . GLN B 159 ? 0.459 0.395 0.249 0.021  -0.000 -0.011 155 GLN B CD  
2400 O OE1 . GLN B 159 ? 0.439 0.379 0.234 0.020  0.000  -0.011 155 GLN B OE1 
2401 N NE2 . GLN B 159 ? 0.469 0.388 0.244 0.028  0.001  -0.009 155 GLN B NE2 
2402 N N   . GLY B 160 ? 0.415 0.421 0.257 -0.003 -0.005 -0.015 156 GLY B N   
2403 C CA  . GLY B 160 ? 0.395 0.420 0.251 -0.006 -0.006 -0.017 156 GLY B CA  
2404 C C   . GLY B 160 ? 0.382 0.416 0.251 -0.000 -0.004 -0.018 156 GLY B C   
2405 O O   . GLY B 160 ? 0.381 0.430 0.261 -0.001 -0.005 -0.019 156 GLY B O   
2406 N N   . GLY B 161 ? 0.360 0.386 0.228 0.006  -0.003 -0.017 157 GLY B N   
2407 C CA  . GLY B 161 ? 0.340 0.375 0.220 0.012  -0.002 -0.018 157 GLY B CA  
2408 C C   . GLY B 161 ? 0.342 0.374 0.224 0.019  -0.000 -0.017 157 GLY B C   
2409 O O   . GLY B 161 ? 0.333 0.353 0.205 0.022  0.000  -0.015 157 GLY B O   
2410 N N   . PHE B 162 ? 0.324 0.366 0.218 0.023  0.000  -0.017 158 PHE B N   
2411 C CA  . PHE B 162 ? 0.333 0.376 0.230 0.029  0.002  -0.016 158 PHE B CA  
2412 C C   . PHE B 162 ? 0.313 0.369 0.223 0.029  0.002  -0.017 158 PHE B C   
2413 O O   . PHE B 162 ? 0.296 0.357 0.210 0.027  0.000  -0.018 158 PHE B O   
2414 C CB  . PHE B 162 ? 0.362 0.399 0.256 0.032  0.004  -0.015 158 PHE B CB  
2415 C CG  . PHE B 162 ? 0.359 0.399 0.258 0.031  0.004  -0.016 158 PHE B CG  
2416 C CD1 . PHE B 162 ? 0.357 0.391 0.249 0.028  0.003  -0.017 158 PHE B CD1 
2417 C CD2 . PHE B 162 ? 0.357 0.406 0.266 0.033  0.004  -0.016 158 PHE B CD2 
2418 C CE1 . PHE B 162 ? 0.348 0.385 0.244 0.027  0.003  -0.018 158 PHE B CE1 
2419 C CE2 . PHE B 162 ? 0.368 0.419 0.279 0.032  0.004  -0.017 158 PHE B CE2 
2420 C CZ  . PHE B 162 ? 0.353 0.398 0.258 0.030  0.003  -0.018 158 PHE B CZ  
2421 N N   . ILE B 163 ? 0.315 0.373 0.229 0.034  0.002  -0.015 159 ILE B N   
2422 C CA  . ILE B 163 ? 0.333 0.402 0.257 0.034  0.002  -0.015 159 ILE B CA  
2423 C C   . ILE B 163 ? 0.349 0.419 0.276 0.038  0.004  -0.014 159 ILE B C   
2424 O O   . ILE B 163 ? 0.382 0.450 0.305 0.042  0.005  -0.012 159 ILE B O   
2425 C CB  . ILE B 163 ? 0.333 0.406 0.259 0.034  0.001  -0.015 159 ILE B CB  
2426 C CG1 . ILE B 163 ? 0.348 0.419 0.271 0.030  -0.001 -0.017 159 ILE B CG1 
2427 C CG2 . ILE B 163 ? 0.326 0.407 0.260 0.034  -0.000 -0.015 159 ILE B CG2 
2428 C CD1 . ILE B 163 ? 0.355 0.430 0.280 0.029  -0.002 -0.016 159 ILE B CD1 
2429 N N   . SER B 164 ? 0.359 0.435 0.291 0.037  0.003  -0.014 160 SER B N   
2430 C CA  . SER B 164 ? 0.392 0.472 0.328 0.039  0.005  -0.012 160 SER B CA  
2431 C C   . SER B 164 ? 0.375 0.465 0.319 0.038  0.003  -0.012 160 SER B C   
2432 O O   . SER B 164 ? 0.347 0.437 0.292 0.034  0.001  -0.013 160 SER B O   
2433 C CB  . SER B 164 ? 0.404 0.481 0.339 0.039  0.006  -0.013 160 SER B CB  
2434 O OG  . SER B 164 ? 0.429 0.513 0.371 0.037  0.006  -0.012 160 SER B OG  
2435 N N   . ILE B 165 ? 0.383 0.480 0.330 0.040  0.004  -0.009 161 ILE B N   
2436 C CA  . ILE B 165 ? 0.392 0.498 0.345 0.037  0.003  -0.008 161 ILE B CA  
2437 C C   . ILE B 165 ? 0.402 0.515 0.359 0.037  0.004  -0.006 161 ILE B C   
2438 O O   . ILE B 165 ? 0.386 0.501 0.342 0.041  0.007  -0.004 161 ILE B O   
2439 C CB  . ILE B 165 ? 0.408 0.521 0.364 0.040  0.003  -0.006 161 ILE B CB  
2440 C CG1 . ILE B 165 ? 0.431 0.536 0.382 0.040  0.002  -0.007 161 ILE B CG1 
2441 C CG2 . ILE B 165 ? 0.413 0.536 0.374 0.037  0.001  -0.004 161 ILE B CG2 
2442 C CD1 . ILE B 165 ? 0.418 0.521 0.369 0.036  -0.001 -0.010 161 ILE B CD1 
2443 N N   . ASP B 166 ? 0.430 0.544 0.389 0.032  0.003  -0.006 162 ASP B N   
2444 C CA  . ASP B 166 ? 0.465 0.586 0.426 0.029  0.003  -0.004 162 ASP B CA  
2445 C C   . ASP B 166 ? 0.486 0.604 0.445 0.032  0.006  -0.004 162 ASP B C   
2446 O O   . ASP B 166 ? 0.460 0.586 0.422 0.032  0.008  -0.001 162 ASP B O   
2447 C CB  . ASP B 166 ? 0.469 0.604 0.436 0.029  0.003  -0.001 162 ASP B CB  
2448 C CG  . ASP B 166 ? 0.494 0.631 0.463 0.024  -0.001 -0.001 162 ASP B CG  
2449 O OD1 . ASP B 166 ? 0.495 0.623 0.460 0.021  -0.003 -0.004 162 ASP B OD1 
2450 O OD2 . ASP B 166 ? 0.543 0.691 0.516 0.024  -0.001 0.001  162 ASP B OD2 
2451 N N   . GLU B 167 ? 0.518 0.625 0.472 0.034  0.007  -0.006 163 GLU B N   
2452 C CA  . GLU B 167 ? 0.577 0.679 0.527 0.036  0.009  -0.006 163 GLU B CA  
2453 C C   . GLU B 167 ? 0.551 0.658 0.502 0.042  0.013  -0.004 163 GLU B C   
2454 O O   . GLU B 167 ? 0.531 0.636 0.479 0.044  0.015  -0.003 163 GLU B O   
2455 C CB  . GLU B 167 ? 0.579 0.681 0.529 0.032  0.009  -0.006 163 GLU B CB  
2456 C CG  . GLU B 167 ? 0.599 0.692 0.546 0.029  0.006  -0.009 163 GLU B CG  
2457 C CD  . GLU B 167 ? 0.655 0.743 0.598 0.026  0.006  -0.010 163 GLU B CD  
2458 O OE1 . GLU B 167 ? 0.649 0.729 0.588 0.028  0.007  -0.011 163 GLU B OE1 
2459 O OE2 . GLU B 167 ? 0.722 0.811 0.665 0.022  0.005  -0.009 163 GLU B OE2 
2460 N N   . ARG B 168 ? 0.574 0.686 0.526 0.045  0.013  -0.002 164 ARG B N   
2461 C CA  . ARG B 168 ? 0.621 0.739 0.572 0.052  0.016  0.000  164 ARG B CA  
2462 C C   . ARG B 168 ? 0.627 0.735 0.571 0.057  0.016  -0.001 164 ARG B C   
2463 O O   . ARG B 168 ? 0.730 0.829 0.667 0.062  0.018  -0.001 164 ARG B O   
2464 C CB  . ARG B 168 ? 0.668 0.802 0.627 0.052  0.015  0.003  164 ARG B CB  
2465 C CG  . ARG B 168 ? 0.738 0.882 0.703 0.046  0.014  0.004  164 ARG B CG  
2466 C CD  . ARG B 168 ? 0.780 0.938 0.753 0.042  0.012  0.006  164 ARG B CD  
2467 N NE  . ARG B 168 ? 0.845 1.019 0.822 0.047  0.014  0.010  164 ARG B NE  
2468 C CZ  . ARG B 168 ? 0.852 1.037 0.832 0.049  0.017  0.013  164 ARG B CZ  
2469 N NH1 . ARG B 168 ? 0.836 1.016 0.813 0.046  0.018  0.012  164 ARG B NH1 
2470 N NH2 . ARG B 168 ? 0.828 1.029 0.812 0.054  0.019  0.016  164 ARG B NH2 
2471 N N   . ASP B 169 ? 0.604 0.711 0.548 0.056  0.014  -0.001 165 ASP B N   
2472 C CA  . ASP B 169 ? 0.559 0.657 0.496 0.061  0.014  -0.002 165 ASP B CA  
2473 C C   . ASP B 169 ? 0.469 0.555 0.401 0.056  0.012  -0.005 165 ASP B C   
2474 O O   . ASP B 169 ? 0.467 0.555 0.404 0.050  0.010  -0.006 165 ASP B O   
2475 C CB  . ASP B 169 ? 0.608 0.713 0.548 0.063  0.012  -0.000 165 ASP B CB  
2476 C CG  . ASP B 169 ? 0.625 0.743 0.568 0.069  0.014  0.003  165 ASP B CG  
2477 O OD1 . ASP B 169 ? 0.630 0.743 0.567 0.075  0.017  0.004  165 ASP B OD1 
2478 O OD2 . ASP B 169 ? 0.634 0.766 0.586 0.067  0.013  0.005  165 ASP B OD2 
2479 N N   . VAL B 170 ? 0.410 0.483 0.331 0.059  0.012  -0.005 166 VAL B N   
2480 C CA  . VAL B 170 ? 0.396 0.458 0.311 0.054  0.011  -0.008 166 VAL B CA  
2481 C C   . VAL B 170 ? 0.383 0.436 0.289 0.056  0.010  -0.008 166 VAL B C   
2482 O O   . VAL B 170 ? 0.387 0.432 0.283 0.062  0.012  -0.006 166 VAL B O   
2483 C CB  . VAL B 170 ? 0.399 0.452 0.307 0.054  0.012  -0.009 166 VAL B CB  
2484 C CG1 . VAL B 170 ? 0.400 0.443 0.302 0.049  0.010  -0.011 166 VAL B CG1 
2485 C CG2 . VAL B 170 ? 0.387 0.447 0.303 0.052  0.013  -0.009 166 VAL B CG2 
2486 N N   . TYR B 171 ? 0.360 0.412 0.265 0.051  0.008  -0.009 167 TYR B N   
2487 C CA  . TYR B 171 ? 0.358 0.401 0.254 0.052  0.007  -0.009 167 TYR B CA  
2488 C C   . TYR B 171 ? 0.344 0.378 0.232 0.046  0.005  -0.011 167 TYR B C   
2489 O O   . TYR B 171 ? 0.334 0.375 0.230 0.041  0.004  -0.012 167 TYR B O   
2490 C CB  . TYR B 171 ? 0.363 0.415 0.266 0.051  0.005  -0.009 167 TYR B CB  
2491 C CG  . TYR B 171 ? 0.361 0.426 0.273 0.056  0.006  -0.007 167 TYR B CG  
2492 C CD1 . TYR B 171 ? 0.385 0.449 0.293 0.063  0.006  -0.005 167 TYR B CD1 
2493 C CD2 . TYR B 171 ? 0.352 0.428 0.275 0.054  0.006  -0.007 167 TYR B CD2 
2494 C CE1 . TYR B 171 ? 0.384 0.462 0.301 0.067  0.007  -0.002 167 TYR B CE1 
2495 C CE2 . TYR B 171 ? 0.361 0.449 0.292 0.057  0.006  -0.004 167 TYR B CE2 
2496 C CZ  . TYR B 171 ? 0.381 0.472 0.310 0.063  0.007  -0.002 167 TYR B CZ  
2497 O OH  . TYR B 171 ? 0.409 0.515 0.346 0.065  0.007  0.000  167 TYR B OH  
2498 N N   . LEU B 172 ? 0.354 0.373 0.228 0.046  0.005  -0.010 168 LEU B N   
2499 C CA  . LEU B 172 ? 0.374 0.386 0.241 0.038  0.004  -0.012 168 LEU B CA  
2500 C C   . LEU B 172 ? 0.375 0.388 0.241 0.033  0.002  -0.012 168 LEU B C   
2501 O O   . LEU B 172 ? 0.377 0.389 0.241 0.037  0.001  -0.011 168 LEU B O   
2502 C CB  . LEU B 172 ? 0.388 0.381 0.237 0.040  0.004  -0.011 168 LEU B CB  
2503 C CG  . LEU B 172 ? 0.392 0.380 0.238 0.046  0.006  -0.010 168 LEU B CG  
2504 C CD1 . LEU B 172 ? 0.404 0.371 0.229 0.049  0.007  -0.009 168 LEU B CD1 
2505 C CD2 . LEU B 172 ? 0.384 0.379 0.238 0.041  0.006  -0.011 168 LEU B CD2 
2506 N N   . LEU B 173 ? 0.375 0.393 0.244 0.026  0.000  -0.014 169 LEU B N   
2507 C CA  . LEU B 173 ? 0.385 0.406 0.253 0.020  -0.001 -0.014 169 LEU B CA  
2508 C C   . LEU B 173 ? 0.402 0.409 0.254 0.014  -0.003 -0.014 169 LEU B C   
2509 O O   . LEU B 173 ? 0.415 0.415 0.260 0.012  -0.003 -0.014 169 LEU B O   
2510 C CB  . LEU B 173 ? 0.368 0.404 0.248 0.016  -0.002 -0.016 169 LEU B CB  
2511 C CG  . LEU B 173 ? 0.367 0.414 0.260 0.021  -0.002 -0.016 169 LEU B CG  
2512 C CD1 . LEU B 173 ? 0.360 0.418 0.263 0.018  -0.002 -0.018 169 LEU B CD1 
2513 C CD2 . LEU B 173 ? 0.361 0.411 0.257 0.022  -0.002 -0.016 169 LEU B CD2 
2514 N N   . ALA B 174 ? 0.418 0.421 0.263 0.012  -0.004 -0.013 170 ALA B N   
2515 C CA  . ALA B 174 ? 0.463 0.453 0.292 0.004  -0.005 -0.013 170 ALA B CA  
2516 C C   . ALA B 174 ? 0.486 0.486 0.319 -0.005 -0.006 -0.014 170 ALA B C   
2517 O O   . ALA B 174 ? 0.525 0.543 0.374 -0.004 -0.006 -0.015 170 ALA B O   
2518 C CB  . ALA B 174 ? 0.460 0.445 0.282 0.004  -0.006 -0.012 170 ALA B CB  
2519 N N   . ALA B 175 ? 0.537 0.528 0.357 -0.013 -0.007 -0.013 171 ALA B N   
2520 C CA  . ALA B 175 ? 0.547 0.549 0.369 -0.023 -0.009 -0.014 171 ALA B CA  
2521 C C   . ALA B 175 ? 0.570 0.577 0.390 -0.029 -0.009 -0.014 171 ALA B C   
2522 O O   . ALA B 175 ? 0.582 0.582 0.398 -0.025 -0.009 -0.013 171 ALA B O   
2523 C CB  . ALA B 175 ? 0.531 0.520 0.337 -0.030 -0.010 -0.013 171 ALA B CB  
2524 N N   . GLY B 176 ? 0.604 0.624 0.427 -0.038 -0.010 -0.014 172 GLY B N   
2525 C CA  . GLY B 176 ? 0.635 0.659 0.454 -0.044 -0.011 -0.013 172 GLY B CA  
2526 C C   . GLY B 176 ? 0.667 0.714 0.504 -0.042 -0.010 -0.015 172 GLY B C   
2527 O O   . GLY B 176 ? 0.695 0.751 0.546 -0.034 -0.009 -0.016 172 GLY B O   
2528 N N   . ARG B 177 ? 0.694 0.750 0.530 -0.049 -0.010 -0.015 173 ARG B N   
2529 C CA  . ARG B 177 ? 0.709 0.789 0.560 -0.049 -0.009 -0.016 173 ARG B CA  
2530 C C   . ARG B 177 ? 0.650 0.733 0.512 -0.039 -0.008 -0.017 173 ARG B C   
2531 O O   . ARG B 177 ? 0.600 0.699 0.475 -0.034 -0.007 -0.019 173 ARG B O   
2532 C CB  . ARG B 177 ? 0.823 0.913 0.670 -0.059 -0.010 -0.015 173 ARG B CB  
2533 C CG  . ARG B 177 ? 0.940 1.056 0.802 -0.057 -0.009 -0.016 173 ARG B CG  
2534 C CD  . ARG B 177 ? 0.996 1.120 0.857 -0.062 -0.008 -0.016 173 ARG B CD  
2535 N NE  . ARG B 177 ? 1.034 1.165 0.886 -0.076 -0.009 -0.014 173 ARG B NE  
2536 C CZ  . ARG B 177 ? 1.036 1.176 0.885 -0.083 -0.009 -0.013 173 ARG B CZ  
2537 N NH1 . ARG B 177 ? 1.000 1.146 0.853 -0.079 -0.007 -0.014 173 ARG B NH1 
2538 N NH2 . ARG B 177 ? 1.048 1.184 0.885 -0.094 -0.010 -0.011 173 ARG B NH2 
2539 N N   . GLU B 178 ? 0.620 0.689 0.475 -0.036 -0.008 -0.017 174 GLU B N   
2540 C CA  . GLU B 178 ? 0.599 0.671 0.464 -0.028 -0.008 -0.018 174 GLU B CA  
2541 C C   . GLU B 178 ? 0.511 0.585 0.386 -0.020 -0.007 -0.019 174 GLU B C   
2542 O O   . GLU B 178 ? 0.480 0.566 0.366 -0.015 -0.006 -0.020 174 GLU B O   
2543 C CB  . GLU B 178 ? 0.686 0.742 0.540 -0.027 -0.008 -0.017 174 GLU B CB  
2544 C CG  . GLU B 178 ? 0.729 0.784 0.575 -0.034 -0.009 -0.016 174 GLU B CG  
2545 C CD  . GLU B 178 ? 0.801 0.838 0.636 -0.030 -0.009 -0.015 174 GLU B CD  
2546 O OE1 . GLU B 178 ? 0.854 0.879 0.674 -0.037 -0.010 -0.014 174 GLU B OE1 
2547 O OE2 . GLU B 178 ? 0.768 0.805 0.611 -0.021 -0.009 -0.015 174 GLU B OE2 
2548 N N   . CYS B 179 ? 0.467 0.530 0.337 -0.018 -0.007 -0.018 175 CYS B N   
2549 C CA  . CYS B 179 ? 0.429 0.494 0.308 -0.011 -0.006 -0.019 175 CYS B CA  
2550 C C   . CYS B 179 ? 0.389 0.470 0.278 -0.012 -0.006 -0.020 175 CYS B C   
2551 O O   . CYS B 179 ? 0.359 0.447 0.258 -0.006 -0.006 -0.021 175 CYS B O   
2552 C CB  . CYS B 179 ? 0.451 0.502 0.321 -0.009 -0.006 -0.017 175 CYS B CB  
2553 S SG  . CYS B 179 ? 0.455 0.511 0.337 -0.002 -0.005 -0.018 175 CYS B SG  
2554 N N   . ALA B 180 ? 0.378 0.464 0.263 -0.019 -0.007 -0.020 176 ALA B N   
2555 C CA  . ALA B 180 ? 0.368 0.470 0.262 -0.019 -0.007 -0.021 176 ALA B CA  
2556 C C   . ALA B 180 ? 0.358 0.474 0.261 -0.016 -0.006 -0.023 176 ALA B C   
2557 O O   . ALA B 180 ? 0.342 0.467 0.253 -0.010 -0.006 -0.024 176 ALA B O   
2558 C CB  . ALA B 180 ? 0.364 0.473 0.253 -0.027 -0.008 -0.020 176 ALA B CB  
2559 N N   . GLU B 181 ? 0.372 0.489 0.272 -0.019 -0.006 -0.022 177 GLU B N   
2560 C CA  . GLU B 181 ? 0.370 0.500 0.277 -0.016 -0.005 -0.024 177 GLU B CA  
2561 C C   . GLU B 181 ? 0.345 0.471 0.259 -0.007 -0.005 -0.025 177 GLU B C   
2562 O O   . GLU B 181 ? 0.349 0.483 0.269 -0.003 -0.005 -0.026 177 GLU B O   
2563 C CB  . GLU B 181 ? 0.417 0.546 0.318 -0.021 -0.005 -0.023 177 GLU B CB  
2564 C CG  . GLU B 181 ? 0.443 0.584 0.349 -0.018 -0.004 -0.024 177 GLU B CG  
2565 C CD  . GLU B 181 ? 0.498 0.658 0.412 -0.017 -0.004 -0.025 177 GLU B CD  
2566 O OE1 . GLU B 181 ? 0.542 0.709 0.454 -0.022 -0.004 -0.025 177 GLU B OE1 
2567 O OE2 . GLU B 181 ? 0.506 0.673 0.426 -0.010 -0.003 -0.027 177 GLU B OE2 
2568 N N   . ALA B 182 ? 0.337 0.449 0.247 -0.005 -0.006 -0.024 178 ALA B N   
2569 C CA  . ALA B 182 ? 0.333 0.443 0.249 0.002  -0.006 -0.024 178 ALA B CA  
2570 C C   . ALA B 182 ? 0.333 0.445 0.255 0.006  -0.006 -0.025 178 ALA B C   
2571 O O   . ALA B 182 ? 0.324 0.440 0.251 0.010  -0.006 -0.026 178 ALA B O   
2572 C CB  . ALA B 182 ? 0.343 0.439 0.254 0.003  -0.006 -0.022 178 ALA B CB  
2573 N N   . GLY B 183 ? 0.328 0.439 0.248 0.004  -0.006 -0.025 179 GLY B N   
2574 C CA  . GLY B 183 ? 0.331 0.444 0.255 0.007  -0.006 -0.026 179 GLY B CA  
2575 C C   . GLY B 183 ? 0.336 0.463 0.265 0.008  -0.006 -0.027 179 GLY B C   
2576 O O   . GLY B 183 ? 0.314 0.443 0.247 0.014  -0.006 -0.029 179 GLY B O   
2577 N N   . ASP B 184 ? 0.363 0.499 0.290 0.004  -0.006 -0.027 180 ASP B N   
2578 C CA  . ASP B 184 ? 0.375 0.526 0.306 0.006  -0.006 -0.029 180 ASP B CA  
2579 C C   . ASP B 184 ? 0.372 0.522 0.306 0.012  -0.006 -0.030 180 ASP B C   
2580 O O   . ASP B 184 ? 0.374 0.528 0.311 0.018  -0.006 -0.032 180 ASP B O   
2581 C CB  . ASP B 184 ? 0.404 0.565 0.333 -0.000 -0.005 -0.028 180 ASP B CB  
2582 C CG  . ASP B 184 ? 0.422 0.587 0.348 -0.006 -0.006 -0.027 180 ASP B CG  
2583 O OD1 . ASP B 184 ? 0.446 0.604 0.372 -0.005 -0.006 -0.027 180 ASP B OD1 
2584 O OD2 . ASP B 184 ? 0.464 0.635 0.386 -0.014 -0.006 -0.026 180 ASP B OD2 
2585 N N   . GLU B 185 ? 0.396 0.540 0.328 0.011  -0.005 -0.030 181 GLU B N   
2586 C CA  . GLU B 185 ? 0.404 0.548 0.337 0.015  -0.006 -0.031 181 GLU B CA  
2587 C C   . GLU B 185 ? 0.370 0.506 0.304 0.020  -0.007 -0.031 181 GLU B C   
2588 O O   . GLU B 185 ? 0.339 0.476 0.274 0.025  -0.007 -0.033 181 GLU B O   
2589 C CB  . GLU B 185 ? 0.433 0.574 0.363 0.012  -0.006 -0.030 181 GLU B CB  
2590 C CG  . GLU B 185 ? 0.480 0.629 0.407 0.007  -0.005 -0.029 181 GLU B CG  
2591 C CD  . GLU B 185 ? 0.548 0.693 0.470 0.003  -0.004 -0.028 181 GLU B CD  
2592 O OE1 . GLU B 185 ? 0.550 0.698 0.468 -0.004 -0.004 -0.027 181 GLU B OE1 
2593 O OE2 . GLU B 185 ? 0.590 0.729 0.512 0.005  -0.005 -0.029 181 GLU B OE2 
2594 N N   . LEU B 186 ? 0.350 0.478 0.285 0.019  -0.007 -0.030 182 LEU B N   
2595 C CA  . LEU B 186 ? 0.343 0.465 0.280 0.023  -0.008 -0.030 182 LEU B CA  
2596 C C   . LEU B 186 ? 0.348 0.472 0.285 0.026  -0.008 -0.032 182 LEU B C   
2597 O O   . LEU B 186 ? 0.335 0.457 0.272 0.030  -0.009 -0.033 182 LEU B O   
2598 C CB  . LEU B 186 ? 0.357 0.471 0.293 0.021  -0.007 -0.028 182 LEU B CB  
2599 C CG  . LEU B 186 ? 0.364 0.472 0.302 0.024  -0.008 -0.028 182 LEU B CG  
2600 C CD1 . LEU B 186 ? 0.363 0.469 0.302 0.025  -0.009 -0.028 182 LEU B CD1 
2601 C CD2 . LEU B 186 ? 0.374 0.477 0.311 0.023  -0.007 -0.026 182 LEU B CD2 
2602 N N   . PHE B 187 ? 0.359 0.489 0.296 0.025  -0.007 -0.032 183 PHE B N   
2603 C CA  . PHE B 187 ? 0.383 0.517 0.321 0.029  -0.008 -0.033 183 PHE B CA  
2604 C C   . PHE B 187 ? 0.381 0.523 0.318 0.034  -0.008 -0.035 183 PHE B C   
2605 O O   . PHE B 187 ? 0.372 0.510 0.307 0.039  -0.009 -0.037 183 PHE B O   
2606 C CB  . PHE B 187 ? 0.397 0.536 0.336 0.026  -0.008 -0.033 183 PHE B CB  
2607 C CG  . PHE B 187 ? 0.390 0.519 0.328 0.025  -0.008 -0.032 183 PHE B CG  
2608 C CD1 . PHE B 187 ? 0.398 0.524 0.335 0.028  -0.008 -0.032 183 PHE B CD1 
2609 C CD2 . PHE B 187 ? 0.402 0.524 0.339 0.021  -0.007 -0.030 183 PHE B CD2 
2610 C CE1 . PHE B 187 ? 0.383 0.501 0.320 0.027  -0.008 -0.031 183 PHE B CE1 
2611 C CE2 . PHE B 187 ? 0.415 0.528 0.350 0.021  -0.007 -0.029 183 PHE B CE2 
2612 C CZ  . PHE B 187 ? 0.392 0.503 0.327 0.024  -0.007 -0.029 183 PHE B CZ  
2613 N N   . ASN B 188 ? 0.414 0.565 0.352 0.032  -0.007 -0.035 184 ASN B N   
2614 C CA  . ASN B 188 ? 0.448 0.609 0.385 0.037  -0.007 -0.037 184 ASN B CA  
2615 C C   . ASN B 188 ? 0.402 0.551 0.334 0.041  -0.008 -0.038 184 ASN B C   
2616 O O   . ASN B 188 ? 0.388 0.538 0.318 0.048  -0.009 -0.040 184 ASN B O   
2617 C CB  . ASN B 188 ? 0.511 0.684 0.448 0.033  -0.006 -0.036 184 ASN B CB  
2618 C CG  . ASN B 188 ? 0.609 0.796 0.549 0.029  -0.005 -0.036 184 ASN B CG  
2619 O OD1 . ASN B 188 ? 0.645 0.837 0.586 0.031  -0.006 -0.036 184 ASN B OD1 
2620 N ND2 . ASN B 188 ? 0.705 0.897 0.644 0.022  -0.004 -0.034 184 ASN B ND2 
2621 N N   . LEU B 189 ? 0.383 0.522 0.315 0.038  -0.009 -0.037 185 LEU B N   
2622 C CA  . LEU B 189 ? 0.386 0.516 0.313 0.042  -0.010 -0.038 185 LEU B CA  
2623 C C   . LEU B 189 ? 0.395 0.516 0.320 0.045  -0.011 -0.038 185 LEU B C   
2624 O O   . LEU B 189 ? 0.391 0.507 0.309 0.050  -0.012 -0.040 185 LEU B O   
2625 C CB  . LEU B 189 ? 0.380 0.503 0.309 0.037  -0.010 -0.036 185 LEU B CB  
2626 C CG  . LEU B 189 ? 0.403 0.517 0.326 0.039  -0.012 -0.036 185 LEU B CG  
2627 C CD1 . LEU B 189 ? 0.395 0.512 0.313 0.043  -0.012 -0.038 185 LEU B CD1 
2628 C CD2 . LEU B 189 ? 0.409 0.519 0.335 0.034  -0.012 -0.034 185 LEU B CD2 
2629 N N   . ALA B 190 ? 0.410 0.528 0.337 0.043  -0.011 -0.037 186 ALA B N   
2630 C CA  . ALA B 190 ? 0.432 0.541 0.356 0.045  -0.013 -0.038 186 ALA B CA  
2631 C C   . ALA B 190 ? 0.431 0.545 0.352 0.052  -0.013 -0.040 186 ALA B C   
2632 O O   . ALA B 190 ? 0.404 0.509 0.317 0.057  -0.014 -0.041 186 ALA B O   
2633 C CB  . ALA B 190 ? 0.445 0.553 0.374 0.042  -0.012 -0.036 186 ALA B CB  
2634 N N   . MET B 191 ? 0.440 0.568 0.365 0.052  -0.012 -0.040 187 MET B N   
2635 C CA  . MET B 191 ? 0.467 0.601 0.389 0.059  -0.012 -0.042 187 MET B CA  
2636 C C   . MET B 191 ? 0.494 0.626 0.409 0.066  -0.013 -0.044 187 MET B C   
2637 O O   . MET B 191 ? 0.495 0.621 0.403 0.073  -0.014 -0.045 187 MET B O   
2638 C CB  . MET B 191 ? 0.455 0.607 0.382 0.058  -0.011 -0.042 187 MET B CB  
2639 C CG  . MET B 191 ? 0.460 0.614 0.393 0.052  -0.010 -0.040 187 MET B CG  
2640 S SD  . MET B 191 ? 0.487 0.662 0.424 0.051  -0.010 -0.040 187 MET B SD  
2641 C CE  . MET B 191 ? 0.558 0.730 0.498 0.040  -0.009 -0.037 187 MET B CE  
2642 N N   . LEU B 192 ? 0.521 0.656 0.436 0.064  -0.012 -0.044 188 LEU B N   
2643 C CA  . LEU B 192 ? 0.555 0.687 0.463 0.070  -0.012 -0.045 188 LEU B CA  
2644 C C   . LEU B 192 ? 0.543 0.655 0.441 0.072  -0.014 -0.046 188 LEU B C   
2645 O O   . LEU B 192 ? 0.571 0.677 0.459 0.080  -0.015 -0.048 188 LEU B O   
2646 C CB  . LEU B 192 ? 0.622 0.757 0.532 0.065  -0.011 -0.044 188 LEU B CB  
2647 C CG  . LEU B 192 ? 0.694 0.821 0.595 0.069  -0.012 -0.046 188 LEU B CG  
2648 C CD1 . LEU B 192 ? 0.702 0.833 0.595 0.080  -0.011 -0.048 188 LEU B CD1 
2649 C CD2 . LEU B 192 ? 0.705 0.837 0.608 0.065  -0.010 -0.045 188 LEU B CD2 
2650 N N   . PHE B 193 ? 0.547 0.649 0.446 0.065  -0.015 -0.044 189 PHE B N   
2651 C CA  . PHE B 193 ? 0.564 0.647 0.454 0.066  -0.018 -0.044 189 PHE B CA  
2652 C C   . PHE B 193 ? 0.599 0.677 0.483 0.071  -0.019 -0.046 189 PHE B C   
2653 O O   . PHE B 193 ? 0.606 0.667 0.477 0.074  -0.021 -0.047 189 PHE B O   
2654 C CB  . PHE B 193 ? 0.547 0.625 0.442 0.057  -0.018 -0.042 189 PHE B CB  
2655 C CG  . PHE B 193 ? 0.529 0.610 0.428 0.052  -0.018 -0.040 189 PHE B CG  
2656 C CD1 . PHE B 193 ? 0.524 0.607 0.420 0.054  -0.018 -0.041 189 PHE B CD1 
2657 C CD2 . PHE B 193 ? 0.509 0.591 0.416 0.045  -0.018 -0.038 189 PHE B CD2 
2658 C CE1 . PHE B 193 ? 0.515 0.598 0.414 0.049  -0.018 -0.040 189 PHE B CE1 
2659 C CE2 . PHE B 193 ? 0.504 0.587 0.414 0.041  -0.017 -0.037 189 PHE B CE2 
2660 C CZ  . PHE B 193 ? 0.516 0.600 0.423 0.042  -0.018 -0.038 189 PHE B CZ  
2661 N N   . SER B 194 ? 0.614 0.702 0.504 0.072  -0.018 -0.046 190 SER B N   
2662 C CA  . SER B 194 ? 0.645 0.729 0.530 0.078  -0.019 -0.047 190 SER B CA  
2663 C C   . SER B 194 ? 0.685 0.767 0.559 0.089  -0.020 -0.049 190 SER B C   
2664 O O   . SER B 194 ? 0.679 0.748 0.541 0.094  -0.022 -0.051 190 SER B O   
2665 C CB  . SER B 194 ? 0.597 0.695 0.492 0.077  -0.018 -0.046 190 SER B CB  
2666 O OG  . SER B 194 ? 0.566 0.681 0.464 0.082  -0.016 -0.047 190 SER B OG  
2667 N N   . MET B 195 ? 0.716 0.809 0.591 0.092  -0.018 -0.050 191 MET B N   
2668 C CA  . MET B 195 ? 0.774 0.867 0.638 0.103  -0.019 -0.053 191 MET B CA  
2669 C C   . MET B 195 ? 0.868 0.941 0.718 0.105  -0.021 -0.053 191 MET B C   
2670 O O   . MET B 195 ? 0.929 1.004 0.774 0.110  -0.020 -0.055 191 MET B O   
2671 C CB  . MET B 195 ? 0.791 0.907 0.665 0.104  -0.016 -0.053 191 MET B CB  
2672 C CG  . MET B 195 ? 0.799 0.935 0.685 0.102  -0.014 -0.051 191 MET B CG  
2673 S SD  . MET B 195 ? 0.873 1.035 0.770 0.099  -0.011 -0.051 191 MET B SD  
2674 C CE  . MET B 195 ? 0.894 1.056 0.781 0.109  -0.011 -0.053 191 MET B CE  
2675 N N   . ASP B 196 ? 1.003 1.055 0.845 0.100  -0.023 -0.053 192 ASP B N   
2676 C CA  . ASP B 196 ? 1.046 1.080 0.877 0.097  -0.025 -0.053 192 ASP B CA  
2677 C C   . ASP B 196 ? 1.050 1.093 0.890 0.091  -0.024 -0.051 192 ASP B C   
2678 O O   . ASP B 196 ? 0.969 1.008 0.812 0.082  -0.024 -0.050 192 ASP B O   
2679 C CB  . ASP B 196 ? 1.074 1.093 0.884 0.108  -0.027 -0.055 192 ASP B CB  
2680 C CG  . ASP B 196 ? 1.108 1.108 0.904 0.112  -0.030 -0.056 192 ASP B CG  
2681 O OD1 . ASP B 196 ? 1.040 1.047 0.843 0.112  -0.029 -0.056 192 ASP B OD1 
2682 O OD2 . ASP B 196 ? 1.075 1.054 0.852 0.115  -0.032 -0.057 192 ASP B OD2 
# 
