data_8S6R
# 
_entry.id   8S6R 
# 
_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   8S6R         pdb_00008s6r 10.2210/pdb8s6r/pdb 
WWPDB D_1292136472 ?            ?                   
# 
_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       2025-03-12 
_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                        8S6R 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              m.mack@hs-mannheim.de 
_pdbx_contact_author.name_first         Matthias 
_pdbx_contact_author.name_last          Mack 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7753-2422 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ermler, U.'    1 ? 
'Warkentin, E.' 2 ? 
'Demmer, U.'    3 ? 
'Mack, M.'      4 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_id_ASTM           JMOBAK 
_citation.journal_id_CSD            0070 
_citation.journal_id_ISSN           1089-8638 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            436 
_citation.language                  ? 
_citation.page_first                168734 
_citation.page_last                 168734 
_citation.title                     
;The Phosphatase RosC from Streptomyces davaonensis is Used for Roseoflavin Biosynthesis and has Evolved to Largely Prevent Dephosphorylation of the Important Cofactor Riboflavin-5'-phosphate.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2024.168734 
_citation.pdbx_database_id_PubMed   39097184 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Joshi, T.'     1 ? 
primary 'Demmer, U.'    2 ? 
primary 'Schneider, C.' 3 ? 
primary 'Glaser, T.'    4 ? 
primary 'Warkentin, E.' 5 ? 
primary 'Ermler, U.'    6 ? 
primary 'Mack, M.'      7 ? 
# 
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 'Phosphoglycerate mutase'                                                                          25478.873 2   
? ? ? ? 
2 non-polymer syn '1-deoxy-1-[8-(dimethylamino)-7-methyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl]-D-ribitol' 405.405   2   
? ? ? ? 
3 non-polymer nat GLYCEROL                                                                                           92.094    1   
? ? ? ? 
4 water       nat water                                                                                              18.015    311 
? ? ? ? 
# 
_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       
;WSHPQFEKIEGRMSDGRESFLEVMRSVYERYLVGVPGVSEVWLIRHADSYTGLEDYDGDPRDPALSEKGRAQARLLAARL
AGVPLHGVWASGAHRAQQTASAVAAEHGLRVRTDARLREVRTNWDDGRPSELKPHGVYPFPEPEKEVAERMRTAVTAAVA
ATPPAPDGTTRVAVVGHDSALVILMGSLMNLGWGQLDMILPLTSVSVLAVKDERMVVRSIGDATHLAAAPSDVI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;WSHPQFEKIEGRMSDGRESFLEVMRSVYERYLVGVPGVSEVWLIRHADSYTGLEDYDGDPRDPALSEKGRAQARLLAARL
AGVPLHGVWASGAHRAQQTASAVAAEHGLRVRTDARLREVRTNWDDGRPSELKPHGVYPFPEPEKEVAERMRTAVTAAVA
ATPPAPDGTTRVAVVGHDSALVILMGSLMNLGWGQLDMILPLTSVSVLAVKDERMVVRSIGDATHLAAAPSDVI
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1-deoxy-1-[8-(dimethylamino)-7-methyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl]-D-ribitol' RS3 
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   TRP n 
1 2   SER n 
1 3   HIS n 
1 4   PRO n 
1 5   GLN n 
1 6   PHE n 
1 7   GLU n 
1 8   LYS n 
1 9   ILE n 
1 10  GLU n 
1 11  GLY n 
1 12  ARG n 
1 13  MET n 
1 14  SER n 
1 15  ASP n 
1 16  GLY n 
1 17  ARG n 
1 18  GLU n 
1 19  SER n 
1 20  PHE n 
1 21  LEU n 
1 22  GLU n 
1 23  VAL n 
1 24  MET n 
1 25  ARG n 
1 26  SER n 
1 27  VAL n 
1 28  TYR n 
1 29  GLU n 
1 30  ARG n 
1 31  TYR n 
1 32  LEU n 
1 33  VAL n 
1 34  GLY n 
1 35  VAL n 
1 36  PRO n 
1 37  GLY n 
1 38  VAL n 
1 39  SER n 
1 40  GLU n 
1 41  VAL n 
1 42  TRP n 
1 43  LEU n 
1 44  ILE n 
1 45  ARG n 
1 46  HIS n 
1 47  ALA n 
1 48  ASP n 
1 49  SER n 
1 50  TYR n 
1 51  THR n 
1 52  GLY n 
1 53  LEU n 
1 54  GLU n 
1 55  ASP n 
1 56  TYR n 
1 57  ASP n 
1 58  GLY n 
1 59  ASP n 
1 60  PRO n 
1 61  ARG n 
1 62  ASP n 
1 63  PRO n 
1 64  ALA n 
1 65  LEU n 
1 66  SER n 
1 67  GLU n 
1 68  LYS n 
1 69  GLY n 
1 70  ARG n 
1 71  ALA n 
1 72  GLN n 
1 73  ALA n 
1 74  ARG n 
1 75  LEU n 
1 76  LEU n 
1 77  ALA n 
1 78  ALA n 
1 79  ARG n 
1 80  LEU n 
1 81  ALA n 
1 82  GLY n 
1 83  VAL n 
1 84  PRO n 
1 85  LEU n 
1 86  HIS n 
1 87  GLY n 
1 88  VAL n 
1 89  TRP n 
1 90  ALA n 
1 91  SER n 
1 92  GLY n 
1 93  ALA n 
1 94  HIS n 
1 95  ARG n 
1 96  ALA n 
1 97  GLN n 
1 98  GLN n 
1 99  THR n 
1 100 ALA n 
1 101 SER n 
1 102 ALA n 
1 103 VAL n 
1 104 ALA n 
1 105 ALA n 
1 106 GLU n 
1 107 HIS n 
1 108 GLY n 
1 109 LEU n 
1 110 ARG n 
1 111 VAL n 
1 112 ARG n 
1 113 THR n 
1 114 ASP n 
1 115 ALA n 
1 116 ARG n 
1 117 LEU n 
1 118 ARG n 
1 119 GLU n 
1 120 VAL n 
1 121 ARG n 
1 122 THR n 
1 123 ASN n 
1 124 TRP n 
1 125 ASP n 
1 126 ASP n 
1 127 GLY n 
1 128 ARG n 
1 129 PRO n 
1 130 SER n 
1 131 GLU n 
1 132 LEU n 
1 133 LYS n 
1 134 PRO n 
1 135 HIS n 
1 136 GLY n 
1 137 VAL n 
1 138 TYR n 
1 139 PRO n 
1 140 PHE n 
1 141 PRO n 
1 142 GLU n 
1 143 PRO n 
1 144 GLU n 
1 145 LYS n 
1 146 GLU n 
1 147 VAL n 
1 148 ALA n 
1 149 GLU n 
1 150 ARG n 
1 151 MET n 
1 152 ARG n 
1 153 THR n 
1 154 ALA n 
1 155 VAL n 
1 156 THR n 
1 157 ALA n 
1 158 ALA n 
1 159 VAL n 
1 160 ALA n 
1 161 ALA n 
1 162 THR n 
1 163 PRO n 
1 164 PRO n 
1 165 ALA n 
1 166 PRO n 
1 167 ASP n 
1 168 GLY n 
1 169 THR n 
1 170 THR n 
1 171 ARG n 
1 172 VAL n 
1 173 ALA n 
1 174 VAL n 
1 175 VAL n 
1 176 GLY n 
1 177 HIS n 
1 178 ASP n 
1 179 SER n 
1 180 ALA n 
1 181 LEU n 
1 182 VAL n 
1 183 ILE n 
1 184 LEU n 
1 185 MET n 
1 186 GLY n 
1 187 SER n 
1 188 LEU n 
1 189 MET n 
1 190 ASN n 
1 191 LEU n 
1 192 GLY n 
1 193 TRP n 
1 194 GLY n 
1 195 GLN n 
1 196 LEU n 
1 197 ASP n 
1 198 MET n 
1 199 ILE n 
1 200 LEU n 
1 201 PRO n 
1 202 LEU n 
1 203 THR n 
1 204 SER n 
1 205 VAL n 
1 206 SER n 
1 207 VAL n 
1 208 LEU n 
1 209 ALA n 
1 210 VAL n 
1 211 LYS n 
1 212 ASP n 
1 213 GLU n 
1 214 ARG n 
1 215 MET n 
1 216 VAL n 
1 217 VAL n 
1 218 ARG n 
1 219 SER n 
1 220 ILE n 
1 221 GLY n 
1 222 ASP n 
1 223 ALA n 
1 224 THR n 
1 225 HIS n 
1 226 LEU n 
1 227 ALA n 
1 228 ALA n 
1 229 ALA n 
1 230 PRO n 
1 231 SER n 
1 232 ASP n 
1 233 VAL n 
1 234 ILE 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                   234 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 BN159_8033 
_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      'Streptomyces davaonensis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     348043 
_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 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_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 
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 
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 
RS3 non-polymer         . '1-deoxy-1-[8-(dimethylamino)-7-methyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl]-D-ribitol' 
Roseoflavin                     'C18 H23 N5 O6'  405.405 
SER 'L-peptide linking' y SERINE                                                                                             ? 
'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                                                                          ? 
'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                         ? 
'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                           ? 
'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                                                             ? 
'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   TRP 1   -11 ?   ?   ?   A . n 
A 1 2   SER 2   -10 ?   ?   ?   A . n 
A 1 3   HIS 3   -9  ?   ?   ?   A . n 
A 1 4   PRO 4   -8  ?   ?   ?   A . n 
A 1 5   GLN 5   -7  ?   ?   ?   A . n 
A 1 6   PHE 6   -6  ?   ?   ?   A . n 
A 1 7   GLU 7   -5  ?   ?   ?   A . n 
A 1 8   LYS 8   -4  ?   ?   ?   A . n 
A 1 9   ILE 9   -3  ?   ?   ?   A . n 
A 1 10  GLU 10  -2  ?   ?   ?   A . n 
A 1 11  GLY 11  -1  ?   ?   ?   A . n 
A 1 12  ARG 12  0   ?   ?   ?   A . n 
A 1 13  MET 13  1   ?   ?   ?   A . n 
A 1 14  SER 14  2   2   SER SER A . n 
A 1 15  ASP 15  3   3   ASP ASP A . n 
A 1 16  GLY 16  4   4   GLY GLY A . n 
A 1 17  ARG 17  5   5   ARG ARG A . n 
A 1 18  GLU 18  6   6   GLU GLU A . n 
A 1 19  SER 19  7   7   SER SER A . n 
A 1 20  PHE 20  8   8   PHE PHE A . n 
A 1 21  LEU 21  9   9   LEU LEU A . n 
A 1 22  GLU 22  10  10  GLU GLU A . n 
A 1 23  VAL 23  11  11  VAL VAL A . n 
A 1 24  MET 24  12  12  MET MET A . n 
A 1 25  ARG 25  13  13  ARG ARG A . n 
A 1 26  SER 26  14  14  SER SER A . n 
A 1 27  VAL 27  15  15  VAL VAL A . n 
A 1 28  TYR 28  16  16  TYR TYR A . n 
A 1 29  GLU 29  17  17  GLU GLU A . n 
A 1 30  ARG 30  18  18  ARG ARG A . n 
A 1 31  TYR 31  19  19  TYR TYR A . n 
A 1 32  LEU 32  20  20  LEU LEU A . n 
A 1 33  VAL 33  21  21  VAL VAL A . n 
A 1 34  GLY 34  22  22  GLY GLY A . n 
A 1 35  VAL 35  23  23  VAL VAL A . n 
A 1 36  PRO 36  24  24  PRO PRO A . n 
A 1 37  GLY 37  25  25  GLY GLY A . n 
A 1 38  VAL 38  26  26  VAL VAL A . n 
A 1 39  SER 39  27  27  SER SER A . n 
A 1 40  GLU 40  28  28  GLU GLU A . n 
A 1 41  VAL 41  29  29  VAL VAL A . n 
A 1 42  TRP 42  30  30  TRP TRP A . n 
A 1 43  LEU 43  31  31  LEU LEU A . n 
A 1 44  ILE 44  32  32  ILE ILE A . n 
A 1 45  ARG 45  33  33  ARG ARG A . n 
A 1 46  HIS 46  34  34  HIS HIS A . n 
A 1 47  ALA 47  35  35  ALA ALA A . n 
A 1 48  ASP 48  36  36  ASP ASP A . n 
A 1 49  SER 49  37  37  SER SER A . n 
A 1 50  TYR 50  38  38  TYR TYR A . n 
A 1 51  THR 51  39  39  THR THR A . n 
A 1 52  GLY 52  40  40  GLY GLY A . n 
A 1 53  LEU 53  41  41  LEU LEU A . n 
A 1 54  GLU 54  42  42  GLU GLU A . n 
A 1 55  ASP 55  43  43  ASP ASP A . n 
A 1 56  TYR 56  44  44  TYR TYR A . n 
A 1 57  ASP 57  45  45  ASP ASP A . n 
A 1 58  GLY 58  46  46  GLY GLY A . n 
A 1 59  ASP 59  47  47  ASP ASP A . n 
A 1 60  PRO 60  48  48  PRO PRO A . n 
A 1 61  ARG 61  49  49  ARG ARG A . n 
A 1 62  ASP 62  50  50  ASP ASP A . n 
A 1 63  PRO 63  51  51  PRO PRO A . n 
A 1 64  ALA 64  52  52  ALA ALA A . n 
A 1 65  LEU 65  53  53  LEU LEU A . n 
A 1 66  SER 66  54  54  SER SER A . n 
A 1 67  GLU 67  55  55  GLU GLU A . n 
A 1 68  LYS 68  56  56  LYS LYS A . n 
A 1 69  GLY 69  57  57  GLY GLY A . n 
A 1 70  ARG 70  58  58  ARG ARG A . n 
A 1 71  ALA 71  59  59  ALA ALA A . n 
A 1 72  GLN 72  60  60  GLN GLN A . n 
A 1 73  ALA 73  61  61  ALA ALA A . n 
A 1 74  ARG 74  62  62  ARG ARG A . n 
A 1 75  LEU 75  63  63  LEU LEU A . n 
A 1 76  LEU 76  64  64  LEU LEU A . n 
A 1 77  ALA 77  65  65  ALA ALA A . n 
A 1 78  ALA 78  66  66  ALA ALA A . n 
A 1 79  ARG 79  67  67  ARG ARG A . n 
A 1 80  LEU 80  68  68  LEU LEU A . n 
A 1 81  ALA 81  69  69  ALA ALA A . n 
A 1 82  GLY 82  70  70  GLY GLY A . n 
A 1 83  VAL 83  71  71  VAL VAL A . n 
A 1 84  PRO 84  72  72  PRO PRO A . n 
A 1 85  LEU 85  73  73  LEU LEU A . n 
A 1 86  HIS 86  74  74  HIS HIS A . n 
A 1 87  GLY 87  75  75  GLY GLY A . n 
A 1 88  VAL 88  76  76  VAL VAL A . n 
A 1 89  TRP 89  77  77  TRP TRP A . n 
A 1 90  ALA 90  78  78  ALA ALA A . n 
A 1 91  SER 91  79  79  SER SER A . n 
A 1 92  GLY 92  80  80  GLY GLY A . n 
A 1 93  ALA 93  81  81  ALA ALA A . n 
A 1 94  HIS 94  82  82  HIS HIS A . n 
A 1 95  ARG 95  83  83  ARG ARG A . n 
A 1 96  ALA 96  84  84  ALA ALA A . n 
A 1 97  GLN 97  85  85  GLN GLN A . n 
A 1 98  GLN 98  86  86  GLN GLN A . n 
A 1 99  THR 99  87  87  THR THR A . n 
A 1 100 ALA 100 88  88  ALA ALA A . n 
A 1 101 SER 101 89  89  SER SER A . n 
A 1 102 ALA 102 90  90  ALA ALA A . n 
A 1 103 VAL 103 91  91  VAL VAL A . n 
A 1 104 ALA 104 92  92  ALA ALA A . n 
A 1 105 ALA 105 93  93  ALA ALA A . n 
A 1 106 GLU 106 94  94  GLU GLU A . n 
A 1 107 HIS 107 95  95  HIS HIS A . n 
A 1 108 GLY 108 96  96  GLY GLY A . n 
A 1 109 LEU 109 97  97  LEU LEU A . n 
A 1 110 ARG 110 98  98  ARG ARG A . n 
A 1 111 VAL 111 99  99  VAL VAL A . n 
A 1 112 ARG 112 100 100 ARG ARG A . n 
A 1 113 THR 113 101 101 THR THR A . n 
A 1 114 ASP 114 102 102 ASP ASP A . n 
A 1 115 ALA 115 103 103 ALA ALA A . n 
A 1 116 ARG 116 104 104 ARG ARG A . n 
A 1 117 LEU 117 105 105 LEU LEU A . n 
A 1 118 ARG 118 106 106 ARG ARG A . n 
A 1 119 GLU 119 107 107 GLU GLU A . n 
A 1 120 VAL 120 108 108 VAL VAL A . n 
A 1 121 ARG 121 109 109 ARG ARG A . n 
A 1 122 THR 122 110 110 THR THR A . n 
A 1 123 ASN 123 111 111 ASN ASN A . n 
A 1 124 TRP 124 112 112 TRP TRP A . n 
A 1 125 ASP 125 113 113 ASP ASP A . n 
A 1 126 ASP 126 114 114 ASP ASP A . n 
A 1 127 GLY 127 115 115 GLY GLY A . n 
A 1 128 ARG 128 116 116 ARG ARG A . n 
A 1 129 PRO 129 117 117 PRO PRO A . n 
A 1 130 SER 130 118 118 SER SER A . n 
A 1 131 GLU 131 119 119 GLU GLU A . n 
A 1 132 LEU 132 120 120 LEU LEU A . n 
A 1 133 LYS 133 121 121 LYS LYS A . n 
A 1 134 PRO 134 122 122 PRO PRO A . n 
A 1 135 HIS 135 123 123 HIS HIS A . n 
A 1 136 GLY 136 124 124 GLY GLY A . n 
A 1 137 VAL 137 125 125 VAL VAL A . n 
A 1 138 TYR 138 126 126 TYR TYR A . n 
A 1 139 PRO 139 127 127 PRO PRO A . n 
A 1 140 PHE 140 128 128 PHE PHE A . n 
A 1 141 PRO 141 129 129 PRO PRO A . n 
A 1 142 GLU 142 130 130 GLU GLU A . n 
A 1 143 PRO 143 131 131 PRO PRO A . n 
A 1 144 GLU 144 132 132 GLU GLU A . n 
A 1 145 LYS 145 133 133 LYS LYS A . n 
A 1 146 GLU 146 134 134 GLU GLU A . n 
A 1 147 VAL 147 135 135 VAL VAL A . n 
A 1 148 ALA 148 136 136 ALA ALA A . n 
A 1 149 GLU 149 137 137 GLU GLU A . n 
A 1 150 ARG 150 138 138 ARG ARG A . n 
A 1 151 MET 151 139 139 MET MET A . n 
A 1 152 ARG 152 140 140 ARG ARG A . n 
A 1 153 THR 153 141 141 THR THR A . n 
A 1 154 ALA 154 142 142 ALA ALA A . n 
A 1 155 VAL 155 143 143 VAL VAL A . n 
A 1 156 THR 156 144 144 THR THR A . n 
A 1 157 ALA 157 145 145 ALA ALA A . n 
A 1 158 ALA 158 146 146 ALA ALA A . n 
A 1 159 VAL 159 147 147 VAL VAL A . n 
A 1 160 ALA 160 148 148 ALA ALA A . n 
A 1 161 ALA 161 149 149 ALA ALA A . n 
A 1 162 THR 162 150 150 THR THR A . n 
A 1 163 PRO 163 151 151 PRO PRO A . n 
A 1 164 PRO 164 152 152 PRO PRO A . n 
A 1 165 ALA 165 153 153 ALA ALA A . n 
A 1 166 PRO 166 154 154 PRO PRO A . n 
A 1 167 ASP 167 155 155 ASP ASP A . n 
A 1 168 GLY 168 156 156 GLY GLY A . n 
A 1 169 THR 169 157 157 THR THR A . n 
A 1 170 THR 170 158 158 THR THR A . n 
A 1 171 ARG 171 159 159 ARG ARG A . n 
A 1 172 VAL 172 160 160 VAL VAL A . n 
A 1 173 ALA 173 161 161 ALA ALA A . n 
A 1 174 VAL 174 162 162 VAL VAL A . n 
A 1 175 VAL 175 163 163 VAL VAL A . n 
A 1 176 GLY 176 164 164 GLY GLY A . n 
A 1 177 HIS 177 165 165 HIS HIS A . n 
A 1 178 ASP 178 166 166 ASP ASP A . n 
A 1 179 SER 179 167 167 SER SER A . n 
A 1 180 ALA 180 168 168 ALA ALA A . n 
A 1 181 LEU 181 169 169 LEU LEU A . n 
A 1 182 VAL 182 170 170 VAL VAL A . n 
A 1 183 ILE 183 171 171 ILE ILE A . n 
A 1 184 LEU 184 172 172 LEU LEU A . n 
A 1 185 MET 185 173 173 MET MET A . n 
A 1 186 GLY 186 174 174 GLY GLY A . n 
A 1 187 SER 187 175 175 SER SER A . n 
A 1 188 LEU 188 176 176 LEU LEU A . n 
A 1 189 MET 189 177 177 MET MET A . n 
A 1 190 ASN 190 178 178 ASN ASN A . n 
A 1 191 LEU 191 179 179 LEU LEU A . n 
A 1 192 GLY 192 180 180 GLY GLY A . n 
A 1 193 TRP 193 181 181 TRP TRP A . n 
A 1 194 GLY 194 182 182 GLY GLY A . n 
A 1 195 GLN 195 183 183 GLN GLN A . n 
A 1 196 LEU 196 184 184 LEU LEU A . n 
A 1 197 ASP 197 185 185 ASP ASP A . n 
A 1 198 MET 198 186 186 MET MET A . n 
A 1 199 ILE 199 187 187 ILE ILE A . n 
A 1 200 LEU 200 188 188 LEU LEU A . n 
A 1 201 PRO 201 189 189 PRO PRO A . n 
A 1 202 LEU 202 190 190 LEU LEU A . n 
A 1 203 THR 203 191 191 THR THR A . n 
A 1 204 SER 204 192 192 SER SER A . n 
A 1 205 VAL 205 193 193 VAL VAL A . n 
A 1 206 SER 206 194 194 SER SER A . n 
A 1 207 VAL 207 195 195 VAL VAL A . n 
A 1 208 LEU 208 196 196 LEU LEU A . n 
A 1 209 ALA 209 197 197 ALA ALA A . n 
A 1 210 VAL 210 198 198 VAL VAL A . n 
A 1 211 LYS 211 199 199 LYS LYS A . n 
A 1 212 ASP 212 200 200 ASP ASP A . n 
A 1 213 GLU 213 201 201 GLU GLU A . n 
A 1 214 ARG 214 202 202 ARG ARG A . n 
A 1 215 MET 215 203 203 MET MET A . n 
A 1 216 VAL 216 204 204 VAL VAL A . n 
A 1 217 VAL 217 205 205 VAL VAL A . n 
A 1 218 ARG 218 206 206 ARG ARG A . n 
A 1 219 SER 219 207 207 SER SER A . n 
A 1 220 ILE 220 208 208 ILE ILE A . n 
A 1 221 GLY 221 209 209 GLY GLY A . n 
A 1 222 ASP 222 210 210 ASP ASP A . n 
A 1 223 ALA 223 211 211 ALA ALA A . n 
A 1 224 THR 224 212 212 THR THR A . n 
A 1 225 HIS 225 213 213 HIS HIS A . n 
A 1 226 LEU 226 214 214 LEU LEU A . n 
A 1 227 ALA 227 215 215 ALA ALA A . n 
A 1 228 ALA 228 216 216 ALA ALA A . n 
A 1 229 ALA 229 217 217 ALA ALA A . n 
A 1 230 PRO 230 218 218 PRO PRO A . n 
A 1 231 SER 231 219 219 SER SER A . n 
A 1 232 ASP 232 220 220 ASP ASP A . n 
A 1 233 VAL 233 221 221 VAL VAL A . n 
A 1 234 ILE 234 222 222 ILE ILE A . n 
B 1 1   TRP 1   -11 ?   ?   ?   B . n 
B 1 2   SER 2   -10 ?   ?   ?   B . n 
B 1 3   HIS 3   -9  ?   ?   ?   B . n 
B 1 4   PRO 4   -8  ?   ?   ?   B . n 
B 1 5   GLN 5   -7  ?   ?   ?   B . n 
B 1 6   PHE 6   -6  ?   ?   ?   B . n 
B 1 7   GLU 7   -5  ?   ?   ?   B . n 
B 1 8   LYS 8   -4  ?   ?   ?   B . n 
B 1 9   ILE 9   -3  ?   ?   ?   B . n 
B 1 10  GLU 10  -2  ?   ?   ?   B . n 
B 1 11  GLY 11  -1  ?   ?   ?   B . n 
B 1 12  ARG 12  0   ?   ?   ?   B . n 
B 1 13  MET 13  1   1   MET MET B . n 
B 1 14  SER 14  2   2   SER SER B . n 
B 1 15  ASP 15  3   3   ASP ASP B . n 
B 1 16  GLY 16  4   4   GLY GLY B . n 
B 1 17  ARG 17  5   5   ARG ARG B . n 
B 1 18  GLU 18  6   6   GLU GLU B . n 
B 1 19  SER 19  7   7   SER SER B . n 
B 1 20  PHE 20  8   8   PHE PHE B . n 
B 1 21  LEU 21  9   9   LEU LEU B . n 
B 1 22  GLU 22  10  10  GLU GLU B . n 
B 1 23  VAL 23  11  11  VAL VAL B . n 
B 1 24  MET 24  12  12  MET MET B . n 
B 1 25  ARG 25  13  13  ARG ARG B . n 
B 1 26  SER 26  14  14  SER SER B . n 
B 1 27  VAL 27  15  15  VAL VAL B . n 
B 1 28  TYR 28  16  16  TYR TYR B . n 
B 1 29  GLU 29  17  17  GLU GLU B . n 
B 1 30  ARG 30  18  18  ARG ARG B . n 
B 1 31  TYR 31  19  19  TYR TYR B . n 
B 1 32  LEU 32  20  20  LEU LEU B . n 
B 1 33  VAL 33  21  21  VAL VAL B . n 
B 1 34  GLY 34  22  22  GLY GLY B . n 
B 1 35  VAL 35  23  23  VAL VAL B . n 
B 1 36  PRO 36  24  24  PRO PRO B . n 
B 1 37  GLY 37  25  25  GLY GLY B . n 
B 1 38  VAL 38  26  26  VAL VAL B . n 
B 1 39  SER 39  27  27  SER SER B . n 
B 1 40  GLU 40  28  28  GLU GLU B . n 
B 1 41  VAL 41  29  29  VAL VAL B . n 
B 1 42  TRP 42  30  30  TRP TRP B . n 
B 1 43  LEU 43  31  31  LEU LEU B . n 
B 1 44  ILE 44  32  32  ILE ILE B . n 
B 1 45  ARG 45  33  33  ARG ARG B . n 
B 1 46  HIS 46  34  34  HIS HIS B . n 
B 1 47  ALA 47  35  35  ALA ALA B . n 
B 1 48  ASP 48  36  36  ASP ASP B . n 
B 1 49  SER 49  37  37  SER SER B . n 
B 1 50  TYR 50  38  38  TYR TYR B . n 
B 1 51  THR 51  39  39  THR THR B . n 
B 1 52  GLY 52  40  40  GLY GLY B . n 
B 1 53  LEU 53  41  41  LEU LEU B . n 
B 1 54  GLU 54  42  42  GLU GLU B . n 
B 1 55  ASP 55  43  43  ASP ASP B . n 
B 1 56  TYR 56  44  44  TYR TYR B . n 
B 1 57  ASP 57  45  45  ASP ASP B . n 
B 1 58  GLY 58  46  46  GLY GLY B . n 
B 1 59  ASP 59  47  47  ASP ASP B . n 
B 1 60  PRO 60  48  48  PRO PRO B . n 
B 1 61  ARG 61  49  49  ARG ARG B . n 
B 1 62  ASP 62  50  50  ASP ASP B . n 
B 1 63  PRO 63  51  51  PRO PRO B . n 
B 1 64  ALA 64  52  52  ALA ALA B . n 
B 1 65  LEU 65  53  53  LEU LEU B . n 
B 1 66  SER 66  54  54  SER SER B . n 
B 1 67  GLU 67  55  55  GLU GLU B . n 
B 1 68  LYS 68  56  56  LYS LYS B . n 
B 1 69  GLY 69  57  57  GLY GLY B . n 
B 1 70  ARG 70  58  58  ARG ARG B . n 
B 1 71  ALA 71  59  59  ALA ALA B . n 
B 1 72  GLN 72  60  60  GLN GLN B . n 
B 1 73  ALA 73  61  61  ALA ALA B . n 
B 1 74  ARG 74  62  62  ARG ARG B . n 
B 1 75  LEU 75  63  63  LEU LEU B . n 
B 1 76  LEU 76  64  64  LEU LEU B . n 
B 1 77  ALA 77  65  65  ALA ALA B . n 
B 1 78  ALA 78  66  66  ALA ALA B . n 
B 1 79  ARG 79  67  67  ARG ARG B . n 
B 1 80  LEU 80  68  68  LEU LEU B . n 
B 1 81  ALA 81  69  69  ALA ALA B . n 
B 1 82  GLY 82  70  70  GLY GLY B . n 
B 1 83  VAL 83  71  71  VAL VAL B . n 
B 1 84  PRO 84  72  72  PRO PRO B . n 
B 1 85  LEU 85  73  73  LEU LEU B . n 
B 1 86  HIS 86  74  74  HIS HIS B . n 
B 1 87  GLY 87  75  75  GLY GLY B . n 
B 1 88  VAL 88  76  76  VAL VAL B . n 
B 1 89  TRP 89  77  77  TRP TRP B . n 
B 1 90  ALA 90  78  78  ALA ALA B . n 
B 1 91  SER 91  79  79  SER SER B . n 
B 1 92  GLY 92  80  80  GLY GLY B . n 
B 1 93  ALA 93  81  81  ALA ALA B . n 
B 1 94  HIS 94  82  82  HIS HIS B . n 
B 1 95  ARG 95  83  83  ARG ARG B . n 
B 1 96  ALA 96  84  84  ALA ALA B . n 
B 1 97  GLN 97  85  85  GLN GLN B . n 
B 1 98  GLN 98  86  86  GLN GLN B . n 
B 1 99  THR 99  87  87  THR THR B . n 
B 1 100 ALA 100 88  88  ALA ALA B . n 
B 1 101 SER 101 89  89  SER SER B . n 
B 1 102 ALA 102 90  90  ALA ALA B . n 
B 1 103 VAL 103 91  91  VAL VAL B . n 
B 1 104 ALA 104 92  92  ALA ALA B . n 
B 1 105 ALA 105 93  93  ALA ALA B . n 
B 1 106 GLU 106 94  94  GLU GLU B . n 
B 1 107 HIS 107 95  95  HIS HIS B . n 
B 1 108 GLY 108 96  96  GLY GLY B . n 
B 1 109 LEU 109 97  97  LEU LEU B . n 
B 1 110 ARG 110 98  98  ARG ARG B . n 
B 1 111 VAL 111 99  99  VAL VAL B . n 
B 1 112 ARG 112 100 100 ARG ARG B . n 
B 1 113 THR 113 101 101 THR THR B . n 
B 1 114 ASP 114 102 102 ASP ASP B . n 
B 1 115 ALA 115 103 103 ALA ALA B . n 
B 1 116 ARG 116 104 104 ARG ARG B . n 
B 1 117 LEU 117 105 105 LEU LEU B . n 
B 1 118 ARG 118 106 106 ARG ARG B . n 
B 1 119 GLU 119 107 107 GLU GLU B . n 
B 1 120 VAL 120 108 108 VAL VAL B . n 
B 1 121 ARG 121 109 109 ARG ARG B . n 
B 1 122 THR 122 110 110 THR THR B . n 
B 1 123 ASN 123 111 111 ASN ASN B . n 
B 1 124 TRP 124 112 112 TRP TRP B . n 
B 1 125 ASP 125 113 113 ASP ASP B . n 
B 1 126 ASP 126 114 114 ASP ASP B . n 
B 1 127 GLY 127 115 115 GLY GLY B . n 
B 1 128 ARG 128 116 116 ARG ARG B . n 
B 1 129 PRO 129 117 117 PRO PRO B . n 
B 1 130 SER 130 118 118 SER SER B . n 
B 1 131 GLU 131 119 119 GLU GLU B . n 
B 1 132 LEU 132 120 120 LEU LEU B . n 
B 1 133 LYS 133 121 121 LYS LYS B . n 
B 1 134 PRO 134 122 122 PRO PRO B . n 
B 1 135 HIS 135 123 123 HIS HIS B . n 
B 1 136 GLY 136 124 124 GLY GLY B . n 
B 1 137 VAL 137 125 125 VAL VAL B . n 
B 1 138 TYR 138 126 126 TYR TYR B . n 
B 1 139 PRO 139 127 127 PRO PRO B . n 
B 1 140 PHE 140 128 128 PHE PHE B . n 
B 1 141 PRO 141 129 129 PRO PRO B . n 
B 1 142 GLU 142 130 130 GLU GLU B . n 
B 1 143 PRO 143 131 131 PRO PRO B . n 
B 1 144 GLU 144 132 132 GLU GLU B . n 
B 1 145 LYS 145 133 133 LYS LYS B . n 
B 1 146 GLU 146 134 134 GLU GLU B . n 
B 1 147 VAL 147 135 135 VAL VAL B . n 
B 1 148 ALA 148 136 136 ALA ALA B . n 
B 1 149 GLU 149 137 137 GLU GLU B . n 
B 1 150 ARG 150 138 138 ARG ARG B . n 
B 1 151 MET 151 139 139 MET MET B . n 
B 1 152 ARG 152 140 140 ARG ARG B . n 
B 1 153 THR 153 141 141 THR THR B . n 
B 1 154 ALA 154 142 142 ALA ALA B . n 
B 1 155 VAL 155 143 143 VAL VAL B . n 
B 1 156 THR 156 144 144 THR THR B . n 
B 1 157 ALA 157 145 145 ALA ALA B . n 
B 1 158 ALA 158 146 146 ALA ALA B . n 
B 1 159 VAL 159 147 147 VAL VAL B . n 
B 1 160 ALA 160 148 148 ALA ALA B . n 
B 1 161 ALA 161 149 149 ALA ALA B . n 
B 1 162 THR 162 150 150 THR THR B . n 
B 1 163 PRO 163 151 151 PRO PRO B . n 
B 1 164 PRO 164 152 152 PRO PRO B . n 
B 1 165 ALA 165 153 153 ALA ALA B . n 
B 1 166 PRO 166 154 154 PRO PRO B . n 
B 1 167 ASP 167 155 155 ASP ASP B . n 
B 1 168 GLY 168 156 156 GLY GLY B . n 
B 1 169 THR 169 157 157 THR THR B . n 
B 1 170 THR 170 158 158 THR THR B . n 
B 1 171 ARG 171 159 159 ARG ARG B . n 
B 1 172 VAL 172 160 160 VAL VAL B . n 
B 1 173 ALA 173 161 161 ALA ALA B . n 
B 1 174 VAL 174 162 162 VAL VAL B . n 
B 1 175 VAL 175 163 163 VAL VAL B . n 
B 1 176 GLY 176 164 164 GLY GLY B . n 
B 1 177 HIS 177 165 165 HIS HIS B . n 
B 1 178 ASP 178 166 166 ASP ASP B . n 
B 1 179 SER 179 167 167 SER SER B . n 
B 1 180 ALA 180 168 168 ALA ALA B . n 
B 1 181 LEU 181 169 169 LEU LEU B . n 
B 1 182 VAL 182 170 170 VAL VAL B . n 
B 1 183 ILE 183 171 171 ILE ILE B . n 
B 1 184 LEU 184 172 172 LEU LEU B . n 
B 1 185 MET 185 173 173 MET MET B . n 
B 1 186 GLY 186 174 174 GLY GLY B . n 
B 1 187 SER 187 175 175 SER SER B . n 
B 1 188 LEU 188 176 176 LEU LEU B . n 
B 1 189 MET 189 177 177 MET MET B . n 
B 1 190 ASN 190 178 178 ASN ASN B . n 
B 1 191 LEU 191 179 179 LEU LEU B . n 
B 1 192 GLY 192 180 180 GLY GLY B . n 
B 1 193 TRP 193 181 181 TRP TRP B . n 
B 1 194 GLY 194 182 182 GLY GLY B . n 
B 1 195 GLN 195 183 183 GLN GLN B . n 
B 1 196 LEU 196 184 184 LEU LEU B . n 
B 1 197 ASP 197 185 185 ASP ASP B . n 
B 1 198 MET 198 186 186 MET MET B . n 
B 1 199 ILE 199 187 187 ILE ILE B . n 
B 1 200 LEU 200 188 188 LEU LEU B . n 
B 1 201 PRO 201 189 189 PRO PRO B . n 
B 1 202 LEU 202 190 190 LEU LEU B . n 
B 1 203 THR 203 191 191 THR THR B . n 
B 1 204 SER 204 192 192 SER SER B . n 
B 1 205 VAL 205 193 193 VAL VAL B . n 
B 1 206 SER 206 194 194 SER SER B . n 
B 1 207 VAL 207 195 195 VAL VAL B . n 
B 1 208 LEU 208 196 196 LEU LEU B . n 
B 1 209 ALA 209 197 197 ALA ALA B . n 
B 1 210 VAL 210 198 198 VAL VAL B . n 
B 1 211 LYS 211 199 199 LYS LYS B . n 
B 1 212 ASP 212 200 200 ASP ASP B . n 
B 1 213 GLU 213 201 201 GLU GLU B . n 
B 1 214 ARG 214 202 202 ARG ARG B . n 
B 1 215 MET 215 203 203 MET MET B . n 
B 1 216 VAL 216 204 204 VAL VAL B . n 
B 1 217 VAL 217 205 205 VAL VAL B . n 
B 1 218 ARG 218 206 206 ARG ARG B . n 
B 1 219 SER 219 207 207 SER SER B . n 
B 1 220 ILE 220 208 208 ILE ILE B . n 
B 1 221 GLY 221 209 209 GLY GLY B . n 
B 1 222 ASP 222 210 210 ASP ASP B . n 
B 1 223 ALA 223 211 211 ALA ALA B . n 
B 1 224 THR 224 212 212 THR THR B . n 
B 1 225 HIS 225 213 213 HIS HIS B . n 
B 1 226 LEU 226 214 214 LEU LEU B . n 
B 1 227 ALA 227 215 215 ALA ALA B . n 
B 1 228 ALA 228 216 216 ALA ALA B . n 
B 1 229 ALA 229 217 217 ALA ALA B . n 
B 1 230 PRO 230 218 218 PRO PRO B . n 
B 1 231 SER 231 219 219 SER SER B . n 
B 1 232 ASP 232 220 220 ASP ASP B . n 
B 1 233 VAL 233 221 221 VAL VAL B . n 
B 1 234 ILE 234 222 222 ILE ILE B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 RS3 ? ? RS3 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 GOL ? ? GOL ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 RS3 1   301 251 RS3 ARF A . 
D 3 GOL 1   302 1   GOL GOL A . 
E 2 RS3 1   301 251 RS3 ARF B . 
F 4 HOH 1   401 150 HOH HOH A . 
F 4 HOH 2   402 66  HOH HOH A . 
F 4 HOH 3   403 288 HOH HOH A . 
F 4 HOH 4   404 82  HOH HOH A . 
F 4 HOH 5   405 154 HOH HOH A . 
F 4 HOH 6   406 104 HOH HOH A . 
F 4 HOH 7   407 337 HOH HOH A . 
F 4 HOH 8   408 141 HOH HOH A . 
F 4 HOH 9   409 187 HOH HOH A . 
F 4 HOH 10  410 139 HOH HOH A . 
F 4 HOH 11  411 6   HOH HOH A . 
F 4 HOH 12  412 93  HOH HOH A . 
F 4 HOH 13  413 295 HOH HOH A . 
F 4 HOH 14  414 250 HOH HOH A . 
F 4 HOH 15  415 14  HOH HOH A . 
F 4 HOH 16  416 313 HOH HOH A . 
F 4 HOH 17  417 323 HOH HOH A . 
F 4 HOH 18  418 245 HOH HOH A . 
F 4 HOH 19  419 117 HOH HOH A . 
F 4 HOH 20  420 324 HOH HOH A . 
F 4 HOH 21  421 13  HOH HOH A . 
F 4 HOH 22  422 222 HOH HOH A . 
F 4 HOH 23  423 305 HOH HOH A . 
F 4 HOH 24  424 23  HOH HOH A . 
F 4 HOH 25  425 61  HOH HOH A . 
F 4 HOH 26  426 24  HOH HOH A . 
F 4 HOH 27  427 348 HOH HOH A . 
F 4 HOH 28  428 229 HOH HOH A . 
F 4 HOH 29  429 112 HOH HOH A . 
F 4 HOH 30  430 48  HOH HOH A . 
F 4 HOH 31  431 51  HOH HOH A . 
F 4 HOH 32  432 2   HOH HOH A . 
F 4 HOH 33  433 19  HOH HOH A . 
F 4 HOH 34  434 11  HOH HOH A . 
F 4 HOH 35  435 46  HOH HOH A . 
F 4 HOH 36  436 251 HOH HOH A . 
F 4 HOH 37  437 144 HOH HOH A . 
F 4 HOH 38  438 4   HOH HOH A . 
F 4 HOH 39  439 21  HOH HOH A . 
F 4 HOH 40  440 73  HOH HOH A . 
F 4 HOH 41  441 45  HOH HOH A . 
F 4 HOH 42  442 172 HOH HOH A . 
F 4 HOH 43  443 91  HOH HOH A . 
F 4 HOH 44  444 168 HOH HOH A . 
F 4 HOH 45  445 274 HOH HOH A . 
F 4 HOH 46  446 347 HOH HOH A . 
F 4 HOH 47  447 212 HOH HOH A . 
F 4 HOH 48  448 240 HOH HOH A . 
F 4 HOH 49  449 26  HOH HOH A . 
F 4 HOH 50  450 276 HOH HOH A . 
F 4 HOH 51  451 100 HOH HOH A . 
F 4 HOH 52  452 130 HOH HOH A . 
F 4 HOH 53  453 317 HOH HOH A . 
F 4 HOH 54  454 79  HOH HOH A . 
F 4 HOH 55  455 133 HOH HOH A . 
F 4 HOH 56  456 28  HOH HOH A . 
F 4 HOH 57  457 50  HOH HOH A . 
F 4 HOH 58  458 267 HOH HOH A . 
F 4 HOH 59  459 283 HOH HOH A . 
F 4 HOH 60  460 103 HOH HOH A . 
F 4 HOH 61  461 70  HOH HOH A . 
F 4 HOH 62  462 319 HOH HOH A . 
F 4 HOH 63  463 268 HOH HOH A . 
F 4 HOH 64  464 118 HOH HOH A . 
F 4 HOH 65  465 275 HOH HOH A . 
F 4 HOH 66  466 107 HOH HOH A . 
F 4 HOH 67  467 67  HOH HOH A . 
F 4 HOH 68  468 128 HOH HOH A . 
F 4 HOH 69  469 202 HOH HOH A . 
F 4 HOH 70  470 43  HOH HOH A . 
F 4 HOH 71  471 120 HOH HOH A . 
F 4 HOH 72  472 236 HOH HOH A . 
F 4 HOH 73  473 29  HOH HOH A . 
F 4 HOH 74  474 10  HOH HOH A . 
F 4 HOH 75  475 357 HOH HOH A . 
F 4 HOH 76  476 106 HOH HOH A . 
F 4 HOH 77  477 95  HOH HOH A . 
F 4 HOH 78  478 53  HOH HOH A . 
F 4 HOH 79  479 136 HOH HOH A . 
F 4 HOH 80  480 271 HOH HOH A . 
F 4 HOH 81  481 160 HOH HOH A . 
F 4 HOH 82  482 211 HOH HOH A . 
F 4 HOH 83  483 280 HOH HOH A . 
F 4 HOH 84  484 249 HOH HOH A . 
F 4 HOH 85  485 272 HOH HOH A . 
F 4 HOH 86  486 121 HOH HOH A . 
F 4 HOH 87  487 259 HOH HOH A . 
F 4 HOH 88  488 116 HOH HOH A . 
F 4 HOH 89  489 235 HOH HOH A . 
F 4 HOH 90  490 7   HOH HOH A . 
F 4 HOH 91  491 165 HOH HOH A . 
F 4 HOH 92  492 215 HOH HOH A . 
F 4 HOH 93  493 5   HOH HOH A . 
F 4 HOH 94  494 101 HOH HOH A . 
F 4 HOH 95  495 221 HOH HOH A . 
F 4 HOH 96  496 155 HOH HOH A . 
F 4 HOH 97  497 230 HOH HOH A . 
F 4 HOH 98  498 209 HOH HOH A . 
F 4 HOH 99  499 98  HOH HOH A . 
F 4 HOH 100 500 342 HOH HOH A . 
F 4 HOH 101 501 277 HOH HOH A . 
F 4 HOH 102 502 170 HOH HOH A . 
F 4 HOH 103 503 129 HOH HOH A . 
F 4 HOH 104 504 131 HOH HOH A . 
F 4 HOH 105 505 64  HOH HOH A . 
F 4 HOH 106 506 149 HOH HOH A . 
F 4 HOH 107 507 353 HOH HOH A . 
F 4 HOH 108 508 294 HOH HOH A . 
F 4 HOH 109 509 183 HOH HOH A . 
F 4 HOH 110 510 12  HOH HOH A . 
F 4 HOH 111 511 190 HOH HOH A . 
F 4 HOH 112 512 189 HOH HOH A . 
F 4 HOH 113 513 327 HOH HOH A . 
F 4 HOH 114 514 355 HOH HOH A . 
F 4 HOH 115 515 44  HOH HOH A . 
F 4 HOH 116 516 96  HOH HOH A . 
F 4 HOH 117 517 17  HOH HOH A . 
F 4 HOH 118 518 80  HOH HOH A . 
F 4 HOH 119 519 47  HOH HOH A . 
F 4 HOH 120 520 115 HOH HOH A . 
F 4 HOH 121 521 351 HOH HOH A . 
F 4 HOH 122 522 352 HOH HOH A . 
F 4 HOH 123 523 334 HOH HOH A . 
F 4 HOH 124 524 254 HOH HOH A . 
F 4 HOH 125 525 279 HOH HOH A . 
G 4 HOH 1   401 264 HOH HOH B . 
G 4 HOH 2   402 311 HOH HOH B . 
G 4 HOH 3   403 203 HOH HOH B . 
G 4 HOH 4   404 349 HOH HOH B . 
G 4 HOH 5   405 175 HOH HOH B . 
G 4 HOH 6   406 360 HOH HOH B . 
G 4 HOH 7   407 255 HOH HOH B . 
G 4 HOH 8   408 231 HOH HOH B . 
G 4 HOH 9   409 36  HOH HOH B . 
G 4 HOH 10  410 201 HOH HOH B . 
G 4 HOH 11  411 232 HOH HOH B . 
G 4 HOH 12  412 27  HOH HOH B . 
G 4 HOH 13  413 16  HOH HOH B . 
G 4 HOH 14  414 227 HOH HOH B . 
G 4 HOH 15  415 97  HOH HOH B . 
G 4 HOH 16  416 322 HOH HOH B . 
G 4 HOH 17  417 173 HOH HOH B . 
G 4 HOH 18  418 63  HOH HOH B . 
G 4 HOH 19  419 316 HOH HOH B . 
G 4 HOH 20  420 321 HOH HOH B . 
G 4 HOH 21  421 57  HOH HOH B . 
G 4 HOH 22  422 218 HOH HOH B . 
G 4 HOH 23  423 54  HOH HOH B . 
G 4 HOH 24  424 1   HOH HOH B . 
G 4 HOH 25  425 105 HOH HOH B . 
G 4 HOH 26  426 72  HOH HOH B . 
G 4 HOH 27  427 257 HOH HOH B . 
G 4 HOH 28  428 261 HOH HOH B . 
G 4 HOH 29  429 270 HOH HOH B . 
G 4 HOH 30  430 77  HOH HOH B . 
G 4 HOH 31  431 252 HOH HOH B . 
G 4 HOH 32  432 84  HOH HOH B . 
G 4 HOH 33  433 217 HOH HOH B . 
G 4 HOH 34  434 281 HOH HOH B . 
G 4 HOH 35  435 81  HOH HOH B . 
G 4 HOH 36  436 278 HOH HOH B . 
G 4 HOH 37  437 30  HOH HOH B . 
G 4 HOH 38  438 108 HOH HOH B . 
G 4 HOH 39  439 134 HOH HOH B . 
G 4 HOH 40  440 156 HOH HOH B . 
G 4 HOH 41  441 244 HOH HOH B . 
G 4 HOH 42  442 180 HOH HOH B . 
G 4 HOH 43  443 56  HOH HOH B . 
G 4 HOH 44  444 94  HOH HOH B . 
G 4 HOH 45  445 195 HOH HOH B . 
G 4 HOH 46  446 37  HOH HOH B . 
G 4 HOH 47  447 262 HOH HOH B . 
G 4 HOH 48  448 99  HOH HOH B . 
G 4 HOH 49  449 124 HOH HOH B . 
G 4 HOH 50  450 49  HOH HOH B . 
G 4 HOH 51  451 315 HOH HOH B . 
G 4 HOH 52  452 208 HOH HOH B . 
G 4 HOH 53  453 219 HOH HOH B . 
G 4 HOH 54  454 15  HOH HOH B . 
G 4 HOH 55  455 18  HOH HOH B . 
G 4 HOH 56  456 52  HOH HOH B . 
G 4 HOH 57  457 344 HOH HOH B . 
G 4 HOH 58  458 325 HOH HOH B . 
G 4 HOH 59  459 220 HOH HOH B . 
G 4 HOH 60  460 69  HOH HOH B . 
G 4 HOH 61  461 58  HOH HOH B . 
G 4 HOH 62  462 285 HOH HOH B . 
G 4 HOH 63  463 284 HOH HOH B . 
G 4 HOH 64  464 153 HOH HOH B . 
G 4 HOH 65  465 157 HOH HOH B . 
G 4 HOH 66  466 291 HOH HOH B . 
G 4 HOH 67  467 213 HOH HOH B . 
G 4 HOH 68  468 86  HOH HOH B . 
G 4 HOH 69  469 110 HOH HOH B . 
G 4 HOH 70  470 87  HOH HOH B . 
G 4 HOH 71  471 76  HOH HOH B . 
G 4 HOH 72  472 341 HOH HOH B . 
G 4 HOH 73  473 200 HOH HOH B . 
G 4 HOH 74  474 38  HOH HOH B . 
G 4 HOH 75  475 241 HOH HOH B . 
G 4 HOH 76  476 33  HOH HOH B . 
G 4 HOH 77  477 248 HOH HOH B . 
G 4 HOH 78  478 247 HOH HOH B . 
G 4 HOH 79  479 308 HOH HOH B . 
G 4 HOH 80  480 176 HOH HOH B . 
G 4 HOH 81  481 92  HOH HOH B . 
G 4 HOH 82  482 90  HOH HOH B . 
G 4 HOH 83  483 102 HOH HOH B . 
G 4 HOH 84  484 242 HOH HOH B . 
G 4 HOH 85  485 83  HOH HOH B . 
G 4 HOH 86  486 312 HOH HOH B . 
G 4 HOH 87  487 345 HOH HOH B . 
G 4 HOH 88  488 336 HOH HOH B . 
G 4 HOH 89  489 263 HOH HOH B . 
G 4 HOH 90  490 109 HOH HOH B . 
G 4 HOH 91  491 122 HOH HOH B . 
G 4 HOH 92  492 68  HOH HOH B . 
G 4 HOH 93  493 210 HOH HOH B . 
G 4 HOH 94  494 88  HOH HOH B . 
G 4 HOH 95  495 293 HOH HOH B . 
G 4 HOH 96  496 59  HOH HOH B . 
G 4 HOH 97  497 320 HOH HOH B . 
G 4 HOH 98  498 243 HOH HOH B . 
G 4 HOH 99  499 216 HOH HOH B . 
G 4 HOH 100 500 223 HOH HOH B . 
G 4 HOH 101 501 307 HOH HOH B . 
G 4 HOH 102 502 260 HOH HOH B . 
G 4 HOH 103 503 22  HOH HOH B . 
G 4 HOH 104 504 3   HOH HOH B . 
G 4 HOH 105 505 174 HOH HOH B . 
G 4 HOH 106 506 35  HOH HOH B . 
G 4 HOH 107 507 239 HOH HOH B . 
G 4 HOH 108 508 265 HOH HOH B . 
G 4 HOH 109 509 42  HOH HOH B . 
G 4 HOH 110 510 290 HOH HOH B . 
G 4 HOH 111 511 228 HOH HOH B . 
G 4 HOH 112 512 330 HOH HOH B . 
G 4 HOH 113 513 78  HOH HOH B . 
G 4 HOH 114 514 41  HOH HOH B . 
G 4 HOH 115 515 207 HOH HOH B . 
G 4 HOH 116 516 253 HOH HOH B . 
G 4 HOH 117 517 9   HOH HOH B . 
G 4 HOH 118 518 148 HOH HOH B . 
G 4 HOH 119 519 158 HOH HOH B . 
G 4 HOH 120 520 32  HOH HOH B . 
G 4 HOH 121 521 40  HOH HOH B . 
G 4 HOH 122 522 89  HOH HOH B . 
G 4 HOH 123 523 346 HOH HOH B . 
G 4 HOH 124 524 111 HOH HOH B . 
G 4 HOH 125 525 39  HOH HOH B . 
G 4 HOH 126 526 206 HOH HOH B . 
G 4 HOH 127 527 8   HOH HOH B . 
G 4 HOH 128 528 123 HOH HOH B . 
G 4 HOH 129 529 137 HOH HOH B . 
G 4 HOH 130 530 340 HOH HOH B . 
G 4 HOH 131 531 354 HOH HOH B . 
G 4 HOH 132 532 152 HOH HOH B . 
G 4 HOH 133 533 339 HOH HOH B . 
G 4 HOH 134 534 184 HOH HOH B . 
G 4 HOH 135 535 125 HOH HOH B . 
G 4 HOH 136 536 256 HOH HOH B . 
G 4 HOH 137 537 204 HOH HOH B . 
G 4 HOH 138 538 31  HOH HOH B . 
G 4 HOH 139 539 289 HOH HOH B . 
G 4 HOH 140 540 287 HOH HOH B . 
G 4 HOH 141 541 20  HOH HOH B . 
G 4 HOH 142 542 273 HOH HOH B . 
G 4 HOH 143 543 326 HOH HOH B . 
G 4 HOH 144 544 25  HOH HOH B . 
G 4 HOH 145 545 196 HOH HOH B . 
G 4 HOH 146 546 177 HOH HOH B . 
G 4 HOH 147 547 178 HOH HOH B . 
G 4 HOH 148 548 356 HOH HOH B . 
G 4 HOH 149 549 34  HOH HOH B . 
G 4 HOH 150 550 146 HOH HOH B . 
G 4 HOH 151 551 258 HOH HOH B . 
G 4 HOH 152 552 246 HOH HOH B . 
G 4 HOH 153 553 192 HOH HOH B . 
G 4 HOH 154 554 328 HOH HOH B . 
G 4 HOH 155 555 309 HOH HOH B . 
G 4 HOH 156 556 162 HOH HOH B . 
G 4 HOH 157 557 60  HOH HOH B . 
G 4 HOH 158 558 310 HOH HOH B . 
G 4 HOH 159 559 127 HOH HOH B . 
G 4 HOH 160 560 331 HOH HOH B . 
G 4 HOH 161 561 185 HOH HOH B . 
G 4 HOH 162 562 343 HOH HOH B . 
G 4 HOH 163 563 350 HOH HOH B . 
G 4 HOH 164 564 292 HOH HOH B . 
G 4 HOH 165 565 194 HOH HOH B . 
G 4 HOH 166 566 234 HOH HOH B . 
G 4 HOH 167 567 75  HOH HOH B . 
G 4 HOH 168 568 186 HOH HOH B . 
G 4 HOH 169 569 188 HOH HOH B . 
G 4 HOH 170 570 179 HOH HOH B . 
G 4 HOH 171 571 55  HOH HOH B . 
G 4 HOH 172 572 266 HOH HOH B . 
G 4 HOH 173 573 332 HOH HOH B . 
G 4 HOH 174 574 214 HOH HOH B . 
G 4 HOH 175 575 181 HOH HOH B . 
G 4 HOH 176 576 335 HOH HOH B . 
G 4 HOH 177 577 358 HOH HOH B . 
G 4 HOH 178 578 338 HOH HOH B . 
G 4 HOH 179 579 161 HOH HOH B . 
G 4 HOH 180 580 166 HOH HOH B . 
G 4 HOH 181 581 314 HOH HOH B . 
G 4 HOH 182 582 306 HOH HOH B . 
G 4 HOH 183 583 304 HOH HOH B . 
G 4 HOH 184 584 329 HOH HOH B . 
G 4 HOH 185 585 182 HOH HOH B . 
G 4 HOH 186 586 269 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 N 1 A RS3 301 ? C19 ? C RS3 1 C19 
2 1 N 1 A RS3 301 ? C20 ? C RS3 1 C20 
3 1 N 1 B RS3 301 ? C19 ? E RS3 1 C19 
4 1 N 1 B RS3 301 ? C20 ? E RS3 1 C20 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8S6R 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.780 
_cell.length_a_esd                 ? 
_cell.length_b                     81.420 
_cell.length_b_esd                 ? 
_cell.length_c                     89.350 
_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                         8S6R 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8S6R 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.37 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.0 
_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    'PEG 1500, TGB' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-02 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8S6R 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.25 
_reflns.d_resolution_low                               50. 
_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                                     117944 
_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                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.70 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.054000000000000006 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.052000000000000005 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.25  1.3  ? ? ? ? ? ? 12023 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 1.732                ? ? 1  1 0.474              ? ? ? ? 1.541 ? ? ? ? 
? ? ? ? ? 
1.30  1.4  ? ? ? ? ? ? 20864 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 3.139                ? ? 2  1 0.629              ? ? ? ? 2.972 ? ? ? ? 
? ? ? ? ? 
1.40  1.6  ? ? ? ? ? ? 27742 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.78                 ? ? 3  1 0.958              ? ? ? ? 0.741 ? ? ? ? 
? ? ? ? ? 
1.60  1.9  ? ? ? ? ? ? 22787 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.168                ? ? 4  1 0.996              ? ? ? ? 0.16 ? ? ? ? ? 
? ? ? ? 
1.90  2.4  ? ? ? ? ? ? 17136 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.07400000000000001  ? ? 5  1 0.9990000000000001 ? ? ? ? 
0.07200000000000001  ? ? ? ? ? ? ? ? ? 
2.40  3.0  ? ? ? ? ? ? 8333  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.049                ? ? 6  1 0.9990000000000001 ? ? ? ? 0.047 ? ? ? ? 
? ? ? ? ? 
3.00  3.8  ? ? ? ? ? ? 4501  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.04                 ? ? 7  1 0.9990000000000001 ? ? ? ? 0.038 ? ? ? ? 
? ? ? ? ? 
3.80  4.6  ? ? ? ? ? ? 1932  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.034                ? ? 8  1 1.0                ? ? ? ? 0.033 ? ? ? ? 
? ? ? ? ? 
4.60  5.9  ? ? ? ? ? ? 1345  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.033                ? ? 9  1 0.9990000000000001 ? ? ? ? 0.032 ? ? ? ? 
? ? ? ? ? 
5.90  8.0  ? ? ? ? ? ? 737   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.035                ? ? 10 1 1.0                ? ? ? ? 0.034 ? ? ? ? 
? ? ? ? ? 
8.00  12.0 ? ? ? ? ? ? 375   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.028999999999999998 ? ? 11 1 1.0                ? ? ? ? 
0.027999999999999997 ? ? ? ? ? ? ? ? ? 
12.00 50.0 ? ? ? ? ? ? 169   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.03                 ? ? 12 1 1.0                ? ? ? ? 
0.028999999999999998 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8S6R 
_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                            1.25 
_refine.ls_d_res_low                             32.59 
_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                     117823 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.35 
_refine.ls_percent_reflns_R_free                 1.70 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1895 
_refine.ls_R_factor_R_free                       0.2085 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1891 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.61 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.18 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.25 
_refine_hist.d_res_low                        32.59 
_refine_hist.number_atoms_solvent             311 
_refine_hist.number_atoms_total               3731 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3360 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         60 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.187  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.756 ? 1343 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.099  ? 556  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 647  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.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' 1.25 1.28  . . 131 7636 93.00  . . . . 0.3634 . . . . . . . . . . . 0.3554 
'X-RAY DIFFRACTION' 1.28 1.32  . . 141 8136 99.00  . . . . 0.3426 . . . . . . . . . . . 0.3528 
'X-RAY DIFFRACTION' 1.32 1.36  . . 142 8239 100.00 . . . . 0.3269 . . . . . . . . . . . 0.3596 
'X-RAY DIFFRACTION' 1.36 1.40  . . 142 8223 100.00 . . . . 0.3488 . . . . . . . . . . . 0.3613 
'X-RAY DIFFRACTION' 1.40 1.45  . . 142 8209 100.00 . . . . 0.3060 . . . . . . . . . . . 0.3299 
'X-RAY DIFFRACTION' 1.45 1.51  . . 145 8325 100.00 . . . . 0.2569 . . . . . . . . . . . 0.2902 
'X-RAY DIFFRACTION' 1.51 1.58  . . 142 8229 100.00 . . . . 0.2283 . . . . . . . . . . . 0.2440 
'X-RAY DIFFRACTION' 1.58 1.66  . . 143 8275 100.00 . . . . 0.2146 . . . . . . . . . . . 0.2708 
'X-RAY DIFFRACTION' 1.66 1.76  . . 143 8300 100.00 . . . . 0.2186 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 1.76 1.90  . . 144 8338 100.00 . . . . 0.1867 . . . . . . . . . . . 0.2352 
'X-RAY DIFFRACTION' 1.90 2.09  . . 144 8348 100.00 . . . . 0.1721 . . . . . . . . . . . 0.1888 
'X-RAY DIFFRACTION' 2.09 2.39  . . 144 8376 100.00 . . . . 0.1735 . . . . . . . . . . . 0.2206 
'X-RAY DIFFRACTION' 2.39 3.01  . . 146 8447 100.00 . . . . 0.1821 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 3.01 32.59 . . 151 8742 100.00 . . . . 0.1623 . . . . . . . . . . . 0.1728 
# 
_struct.entry_id                     8S6R 
_struct.title                        'RosC-8.demethyl-8-amino-riboflavin complex' 
_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        8S6R 
_struct_keywords.text            'Streptomyces davaonensis, roseoflavin, riboflavin, phosphatases, antibiotics, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    K4R812_STRDJ 
_struct_ref.pdbx_db_accession          K4R812 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSDGRESFLEVMRSVYERYLVGVPGVSEVWLIRHADSYTGLEDYDGDPRDPALSEKGRAQARLLAARLAGVPLHGVWASG
AHRAQQTASAVAAEHGLRVRTDARLREVRTNWDDGRPSELKPHGVYPFPEPEKEVAERMRTAVTAAVAATPPAPDGTTRV
AVVGHDSALVILMGSLMNLGWGQLDMILPLTSVSVLAVKDERMVVRSIGDATHLAAAPSDVI
;
_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 8S6R A 13 ? 234 ? K4R812 1 ? 222 ? 1 222 
2 1 8S6R B 13 ? 234 ? K4R812 1 ? 222 ? 1 222 
# 
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 8S6R TRP A 1  ? UNP K4R812 ? ? 'expression tag' -11 1  
1 8S6R SER A 2  ? UNP K4R812 ? ? 'expression tag' -10 2  
1 8S6R HIS A 3  ? UNP K4R812 ? ? 'expression tag' -9  3  
1 8S6R PRO A 4  ? UNP K4R812 ? ? 'expression tag' -8  4  
1 8S6R GLN A 5  ? UNP K4R812 ? ? 'expression tag' -7  5  
1 8S6R PHE A 6  ? UNP K4R812 ? ? 'expression tag' -6  6  
1 8S6R GLU A 7  ? UNP K4R812 ? ? 'expression tag' -5  7  
1 8S6R LYS A 8  ? UNP K4R812 ? ? 'expression tag' -4  8  
1 8S6R ILE A 9  ? UNP K4R812 ? ? 'expression tag' -3  9  
1 8S6R GLU A 10 ? UNP K4R812 ? ? 'expression tag' -2  10 
1 8S6R GLY A 11 ? UNP K4R812 ? ? 'expression tag' -1  11 
1 8S6R ARG A 12 ? UNP K4R812 ? ? 'expression tag' 0   12 
2 8S6R TRP B 1  ? UNP K4R812 ? ? 'expression tag' -11 13 
2 8S6R SER B 2  ? UNP K4R812 ? ? 'expression tag' -10 14 
2 8S6R HIS B 3  ? UNP K4R812 ? ? 'expression tag' -9  15 
2 8S6R PRO B 4  ? UNP K4R812 ? ? 'expression tag' -8  16 
2 8S6R GLN B 5  ? UNP K4R812 ? ? 'expression tag' -7  17 
2 8S6R PHE B 6  ? UNP K4R812 ? ? 'expression tag' -6  18 
2 8S6R GLU B 7  ? UNP K4R812 ? ? 'expression tag' -5  19 
2 8S6R LYS B 8  ? UNP K4R812 ? ? 'expression tag' -4  20 
2 8S6R ILE B 9  ? UNP K4R812 ? ? 'expression tag' -3  21 
2 8S6R GLU B 10 ? UNP K4R812 ? ? 'expression tag' -2  22 
2 8S6R GLY B 11 ? UNP K4R812 ? ? 'expression tag' -1  23 
2 8S6R ARG B 12 ? UNP K4R812 ? ? 'expression tag' 0   24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5490  ? 
1 MORE         -40   ? 
1 'SSA (A^2)'  18600 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? TYR A 31  ? GLY A 4   TYR A 19  1 ? 16 
HELX_P HELX_P2  AA2 GLY A 52  ? TYR A 56  ? GLY A 40  TYR A 44  5 ? 5  
HELX_P HELX_P3  AA3 SER A 66  ? GLY A 82  ? SER A 54  GLY A 70  1 ? 17 
HELX_P HELX_P4  AA4 ALA A 93  ? GLU A 106 ? ALA A 81  GLU A 94  1 ? 14 
HELX_P HELX_P5  AA5 ALA A 115 ? ARG A 118 ? ALA A 103 ARG A 106 5 ? 4  
HELX_P HELX_P6  AA6 PRO A 143 ? THR A 162 ? PRO A 131 THR A 150 1 ? 20 
HELX_P HELX_P7  AA7 HIS A 177 ? MET A 189 ? HIS A 165 MET A 177 1 ? 13 
HELX_P HELX_P8  AA8 ALA A 223 ? ALA A 227 ? ALA A 211 ALA A 215 5 ? 5  
HELX_P HELX_P9  AA9 GLY B 16  ? TYR B 31  ? GLY B 4   TYR B 19  1 ? 16 
HELX_P HELX_P10 AB1 SER B 66  ? GLY B 82  ? SER B 54  GLY B 70  1 ? 17 
HELX_P HELX_P11 AB2 ALA B 93  ? GLU B 106 ? ALA B 81  GLU B 94  1 ? 14 
HELX_P HELX_P12 AB3 ALA B 115 ? ARG B 118 ? ALA B 103 ARG B 106 5 ? 4  
HELX_P HELX_P13 AB4 ASN B 123 ? GLY B 127 ? ASN B 111 GLY B 115 5 ? 5  
HELX_P HELX_P14 AB5 PRO B 143 ? ALA B 161 ? PRO B 131 ALA B 149 1 ? 19 
HELX_P HELX_P15 AB6 HIS B 177 ? MET B 189 ? HIS B 165 MET B 177 1 ? 13 
HELX_P HELX_P16 AB7 ALA B 223 ? ALA B 227 ? ALA B 211 ALA B 215 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? 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 VAL A 111 ? THR A 113 ? VAL A 99  THR A 101 
AA1 2 GLY A 87  ? ALA A 90  ? GLY A 75  ALA A 78  
AA1 3 ARG A 171 ? GLY A 176 ? ARG A 159 GLY A 164 
AA1 4 SER A 39  ? ARG A 45  ? SER A 27  ARG A 33  
AA1 5 VAL A 205 ? LYS A 211 ? VAL A 193 LYS A 199 
AA1 6 ARG A 214 ? ASP A 222 ? ARG A 202 ASP A 210 
AA2 1 VAL B 111 ? THR B 113 ? VAL B 99  THR B 101 
AA2 2 GLY B 87  ? ALA B 90  ? GLY B 75  ALA B 78  
AA2 3 ARG B 171 ? GLY B 176 ? ARG B 159 GLY B 164 
AA2 4 SER B 39  ? ARG B 45  ? SER B 27  ARG B 33  
AA2 5 VAL B 205 ? LYS B 211 ? VAL B 193 LYS B 199 
AA2 6 ARG B 214 ? ASP B 222 ? ARG B 202 ASP B 210 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ARG A 112 ? O ARG A 100 N VAL A 88  ? N VAL A 76  
AA1 2 3 N TRP A 89  ? N TRP A 77  O VAL A 175 ? O VAL A 163 
AA1 3 4 O VAL A 174 ? O VAL A 162 N ILE A 44  ? N ILE A 32  
AA1 4 5 N SER A 39  ? N SER A 27  O VAL A 210 ? O VAL A 198 
AA1 5 6 N ALA A 209 ? N ALA A 197 O VAL A 216 ? O VAL A 204 
AA2 1 2 O ARG B 112 ? O ARG B 100 N VAL B 88  ? N VAL B 76  
AA2 2 3 N TRP B 89  ? N TRP B 77  O VAL B 175 ? O VAL B 163 
AA2 3 4 O VAL B 174 ? O VAL B 162 N ILE B 44  ? N ILE B 32  
AA2 4 5 N SER B 39  ? N SER B 27  O VAL B 210 ? O VAL B 198 
AA2 5 6 N ALA B 209 ? N ALA B 197 O VAL B 216 ? O VAL B 204 
# 
_pdbx_entry_details.entry_id                   8S6R 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    406 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    466 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                110.55 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            -7.75 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 3   ? ? 61.65  -17.07  
2 1 ASP A 200 ? ? 59.47  -132.86 
3 1 SER B 2   ? ? -94.04 -106.24 
4 1 GLU B 201 ? ? 75.02  -13.34  
# 
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 33.2548 12.3315  -6.3604  0.3327 ? 0.0330  ? -0.0630 ? 0.2330 ? -0.0764 ? 0.3193 ? 3.4066 ? 
5.3451  ? -0.2510 ? 8.4445 ? 0.2836  ? 8.6871 ? 0.0279  ? -0.5474 ? -0.0659 ? 0.4069  ? 0.0059  ? -0.7863 ? -0.1986 ? 0.6356  ? 
-0.1008 ? 
2  'X-RAY DIFFRACTION' ? refined 13.7159 3.2306   -1.1391  0.2461 ? 0.0605  ? 0.0255  ? 0.2845 ? -0.0203 ? 0.1583 ? 4.8870 ? 
2.8158  ? -0.7326 ? 3.3733 ? -1.0065 ? 1.2785 ? 0.1975  ? -0.6241 ? 0.3390  ? 0.3937  ? -0.1956 ? 0.2016  ? -0.1284 ? 0.1099  ? 
-0.0046 ? 
3  'X-RAY DIFFRACTION' ? refined -7.7955 -14.7941 -11.7531 0.2735 ? -0.0225 ? 0.0020  ? 0.2382 ? 0.0313  ? 0.4094 ? 8.4222 ? 
-4.6767 ? 1.7674  ? 2.6731 ? -1.7420 ? 6.9377 ? 0.2184  ? 0.2695  ? -1.0818 ? -0.4483 ? -0.0050 ? 0.6357  ? 0.6741  ? -0.2470 ? 
-0.1560 ? 
4  'X-RAY DIFFRACTION' ? refined 0.7746  -7.2404  -1.1413  0.1996 ? 0.0384  ? 0.0567  ? 0.2710 ? 0.0578  ? 0.2226 ? 1.7816 ? 
-0.9193 ? 0.4093  ? 1.6449 ? -0.9712 ? 2.1017 ? -0.1543 ? -0.3281 ? -0.1349 ? 0.2638  ? 0.1711  ? 0.1661  ? -0.0010 ? -0.1878 ? 
-0.0175 ? 
5  'X-RAY DIFFRACTION' ? refined -5.7071 -0.2961  -23.7861 0.1819 ? 0.0017  ? -0.0313 ? 0.2875 ? 0.0626  ? 0.2494 ? 1.7135 ? 
0.4410  ? -1.5307 ? 2.7974 ? 0.4006  ? 2.6613 ? -0.1636 ? 0.2681  ? -0.0227 ? -0.1903 ? 0.0859  ? 0.3369  ? 0.0283  ? -0.3250 ? 
0.0885  ? 
6  'X-RAY DIFFRACTION' ? refined 0.6514  9.0915   -7.2641  0.2468 ? 0.0624  ? 0.0131  ? 0.1908 ? -0.0226 ? 0.2722 ? 8.3164 ? 
-1.0019 ? 5.4746  ? 1.3958 ? -1.1702 ? 3.8191 ? -0.3167 ? -0.4145 ? 0.4819  ? 0.1523  ? 0.1349  ? -0.0570 ? -0.6517 ? -0.4363 ? 
0.1723  ? 
7  'X-RAY DIFFRACTION' ? refined 8.0152  1.8158   -8.4279  0.1637 ? 0.0465  ? 0.0075  ? 0.2013 ? 0.0130  ? 0.1662 ? 2.1132 ? 
-0.2691 ? -0.2133 ? 1.4416 ? -0.7626 ? 1.6912 ? -0.1258 ? -0.3004 ? 0.0949  ? 0.1749  ? 0.1170  ? 0.0040  ? -0.1362 ? 0.0058  ? 
0.0080  ? 
8  'X-RAY DIFFRACTION' ? refined 12.6024 -3.5073  -6.7656  0.0945 ? 0.0394  ? 0.0066  ? 0.2090 ? 0.0328  ? 0.0989 ? 4.9448 ? 
0.5430  ? -0.1815 ? 6.9592 ? -0.3958 ? 4.1029 ? -0.0430 ? -0.2239 ? -0.1044 ? 0.0536  ? -0.0068 ? 0.2244  ? 0.0047  ? -0.1592 ? 
0.0777  ? 
9  'X-RAY DIFFRACTION' ? refined -3.1133 -11.5161 -23.2821 0.2209 ? -0.0059 ? 0.0104  ? 0.2130 ? -0.0194 ? 0.3148 ? 2.7863 ? 
3.8191  ? -1.7948 ? 6.5229 ? -0.2948 ? 5.7037 ? 0.0166  ? 0.5100  ? -0.4662 ? -0.0369 ? 0.1394  ? 0.3242  ? 0.2081  ? -0.4250 ? 
-0.1228 ? 
10 'X-RAY DIFFRACTION' ? refined 18.3732 -13.0953 -18.0443 0.1578 ? -0.0072 ? 0.0244  ? 0.1695 ? 0.0042  ? 0.2274 ? 1.3085 ? 
-0.5087 ? 1.7361  ? 4.9128 ? 2.4665  ? 5.3395 ? 0.1937  ? 0.0006  ? -0.5306 ? 0.0030  ? -0.1059 ? 0.3238  ? 0.3110  ? -0.3332 ? 
-0.1168 ? 
11 'X-RAY DIFFRACTION' ? refined 40.1965 1.6682   -3.7879  0.2594 ? -0.0258 ? -0.0674 ? 0.3839 ? -0.0924 ? 0.3471 ? 5.1661 ? 
0.5666  ? -0.8905 ? 7.9468 ? -2.4514 ? 4.4898 ? -0.0356 ? -0.8914 ? 0.8395  ? 0.7643  ? -0.0899 ? -0.7722 ? -0.6056 ? 0.9016  ? 
0.1188  ? 
12 'X-RAY DIFFRACTION' ? refined 31.4448 -11.6963 -6.2088  0.1931 ? 0.0370  ? -0.0166 ? 0.2130 ? 0.0456  ? 0.2149 ? 1.8059 ? 
0.3516  ? -0.3593 ? 1.6519 ? 0.1906  ? 1.6380 ? -0.0616 ? -0.2541 ? -0.1640 ? 0.2069  ? 0.0430  ? -0.2038 ? 0.1020  ? 0.1027  ? 
0.0196  ? 
13 'X-RAY DIFFRACTION' ? refined 36.8865 -3.2192  -17.5088 0.1142 ? 0.0117  ? -0.0096 ? 0.1650 ? 0.0028  ? 0.1983 ? 2.7184 ? 
1.5203  ? -1.8973 ? 6.6500 ? -2.7894 ? 2.8811 ? -0.0006 ? -0.0679 ? 0.1226  ? -0.1213 ? -0.0190 ? -0.4156 ? -0.0250 ? 0.0917  ? 
0.0252  ? 
14 'X-RAY DIFFRACTION' ? refined 31.1840 13.8014  -18.5527 0.2120 ? -0.0228 ? 0.0338  ? 0.1216 ? 0.0152  ? 0.2422 ? 1.4947 ? 
-2.4393 ? 0.6238  ? 6.8305 ? 2.5534  ? 5.4114 ? -0.0341 ? -0.0448 ? 0.2832  ? -0.0138 ? 0.1121  ? -0.3504 ? -0.1854 ? 0.1270  ? 
-0.0571 ? 
15 'X-RAY DIFFRACTION' ? refined 28.5935 -4.8075  -26.0808 0.2197 ? 0.0202  ? 0.0077  ? 0.1657 ? -0.0111 ? 0.1447 ? 2.3328 ? 
1.3959  ? -0.2855 ? 3.0884 ? -3.0817 ? 3.8158 ? -0.0861 ? 0.1306  ? 0.0614  ? -0.7701 ? 0.0098  ? -0.2445 ? 0.0222  ? -0.1774 ? 
0.0737  ? 
16 'X-RAY DIFFRACTION' ? refined 24.7898 -18.0531 -16.7826 0.1527 ? 0.0123  ? 0.0333  ? 0.1260 ? 0.0272  ? 0.1785 ? 1.6063 ? 
0.5867  ? 1.3858  ? 8.5163 ? 4.8143  ? 3.6023 ? -0.0065 ? -0.1093 ? -0.2395 ? 0.0184  ? -0.1612 ? 0.2445  ? 0.2520  ? -0.1409 ? 
0.1715  ? 
17 'X-RAY DIFFRACTION' ? refined 21.0052 -2.4274  -14.4770 0.1740 ? 0.0131  ? 0.0102  ? 0.1728 ? -0.0002 ? 0.1732 ? 1.6776 ? 
0.1554  ? 0.3830  ? 1.1687 ? -0.5348 ? 1.3062 ? -0.0538 ? -0.0289 ? 0.0017  ? -0.0635 ? 0.0355  ? -0.0207 ? -0.0605 ? -0.0425 ? 
0.0154  ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 19 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 20 through 33 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 34 through 54 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 55 through 110 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 111 through 131 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 132 through 148 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 149 through 192 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 193 through 222 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 19 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 20 through 33 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 34 through 54 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 55 through 94 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 95 through 115 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 116 through 131 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 132 through 148 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 149 through 165 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 166 through 222 )
;
# 
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 TRP -11 ? A TRP 1  
2  1 Y 1 A SER -10 ? A SER 2  
3  1 Y 1 A HIS -9  ? A HIS 3  
4  1 Y 1 A PRO -8  ? A PRO 4  
5  1 Y 1 A GLN -7  ? A GLN 5  
6  1 Y 1 A PHE -6  ? A PHE 6  
7  1 Y 1 A GLU -5  ? A GLU 7  
8  1 Y 1 A LYS -4  ? A LYS 8  
9  1 Y 1 A ILE -3  ? A ILE 9  
10 1 Y 1 A GLU -2  ? A GLU 10 
11 1 Y 1 A GLY -1  ? A GLY 11 
12 1 Y 1 A ARG 0   ? A ARG 12 
13 1 Y 1 A MET 1   ? A MET 13 
14 1 Y 1 B TRP -11 ? B TRP 1  
15 1 Y 1 B SER -10 ? B SER 2  
16 1 Y 1 B HIS -9  ? B HIS 3  
17 1 Y 1 B PRO -8  ? B PRO 4  
18 1 Y 1 B GLN -7  ? B GLN 5  
19 1 Y 1 B PHE -6  ? B PHE 6  
20 1 Y 1 B GLU -5  ? B GLU 7  
21 1 Y 1 B LYS -4  ? B LYS 8  
22 1 Y 1 B ILE -3  ? B ILE 9  
23 1 Y 1 B GLU -2  ? B GLU 10 
24 1 Y 1 B GLY -1  ? B GLY 11 
25 1 Y 1 B ARG 0   ? B ARG 12 
# 
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  
GLN N      N N N 74  
GLN CA     C N S 75  
GLN C      C N N 76  
GLN O      O N N 77  
GLN CB     C N N 78  
GLN CG     C N N 79  
GLN CD     C N N 80  
GLN OE1    O N N 81  
GLN NE2    N N N 82  
GLN OXT    O N N 83  
GLN H      H N N 84  
GLN H2     H N N 85  
GLN HA     H N N 86  
GLN HB2    H N N 87  
GLN HB3    H N N 88  
GLN HG2    H N N 89  
GLN HG3    H N N 90  
GLN HE21   H N N 91  
GLN HE22   H N N 92  
GLN HXT    H N N 93  
GLU N      N N N 94  
GLU CA     C N S 95  
GLU C      C N N 96  
GLU O      O N N 97  
GLU CB     C N N 98  
GLU CG     C N N 99  
GLU CD     C N N 100 
GLU OE1    O N N 101 
GLU OE2    O N N 102 
GLU OXT    O N N 103 
GLU H      H N N 104 
GLU H2     H N N 105 
GLU HA     H N N 106 
GLU HB2    H N N 107 
GLU HB3    H N N 108 
GLU HG2    H N N 109 
GLU HG3    H N N 110 
GLU HE2    H N N 111 
GLU HXT    H N N 112 
GLY N      N N N 113 
GLY CA     C N N 114 
GLY C      C N N 115 
GLY O      O N N 116 
GLY OXT    O N N 117 
GLY H      H N N 118 
GLY H2     H N N 119 
GLY HA2    H N N 120 
GLY HA3    H N N 121 
GLY HXT    H N N 122 
GOL C1     C N N 123 
GOL O1     O N N 124 
GOL C2     C N N 125 
GOL O2     O N N 126 
GOL C3     C N N 127 
GOL O3     O N N 128 
GOL H11    H N N 129 
GOL H12    H N N 130 
GOL HO1    H N N 131 
GOL H2     H N N 132 
GOL HO2    H N N 133 
GOL H31    H N N 134 
GOL H32    H N N 135 
GOL HO3    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LYS N      N N N 205 
LYS CA     C N S 206 
LYS C      C N N 207 
LYS O      O N N 208 
LYS CB     C N N 209 
LYS CG     C N N 210 
LYS CD     C N N 211 
LYS CE     C N N 212 
LYS NZ     N N N 213 
LYS OXT    O N N 214 
LYS H      H N N 215 
LYS H2     H N N 216 
LYS HA     H N N 217 
LYS HB2    H N N 218 
LYS HB3    H N N 219 
LYS HG2    H N N 220 
LYS HG3    H N N 221 
LYS HD2    H N N 222 
LYS HD3    H N N 223 
LYS HE2    H N N 224 
LYS HE3    H N N 225 
LYS HZ1    H N N 226 
LYS HZ2    H N N 227 
LYS HZ3    H N N 228 
LYS HXT    H N N 229 
MET N      N N N 230 
MET CA     C N S 231 
MET C      C N N 232 
MET O      O N N 233 
MET CB     C N N 234 
MET CG     C N N 235 
MET SD     S N N 236 
MET CE     C N N 237 
MET OXT    O N N 238 
MET H      H N N 239 
MET H2     H N N 240 
MET HA     H N N 241 
MET HB2    H N N 242 
MET HB3    H N N 243 
MET HG2    H N N 244 
MET HG3    H N N 245 
MET HE1    H N N 246 
MET HE2    H N N 247 
MET HE3    H N N 248 
MET HXT    H N N 249 
PHE N      N N N 250 
PHE CA     C N S 251 
PHE C      C N N 252 
PHE O      O N N 253 
PHE CB     C N N 254 
PHE CG     C Y N 255 
PHE CD1    C Y N 256 
PHE CD2    C Y N 257 
PHE CE1    C Y N 258 
PHE CE2    C Y N 259 
PHE CZ     C Y N 260 
PHE OXT    O N N 261 
PHE H      H N N 262 
PHE H2     H N N 263 
PHE HA     H N N 264 
PHE HB2    H N N 265 
PHE HB3    H N N 266 
PHE HD1    H N N 267 
PHE HD2    H N N 268 
PHE HE1    H N N 269 
PHE HE2    H N N 270 
PHE HZ     H N N 271 
PHE HXT    H N N 272 
PRO N      N N N 273 
PRO CA     C N S 274 
PRO C      C N N 275 
PRO O      O N N 276 
PRO CB     C N N 277 
PRO CG     C N N 278 
PRO CD     C N N 279 
PRO OXT    O N N 280 
PRO H      H N N 281 
PRO HA     H N N 282 
PRO HB2    H N N 283 
PRO HB3    H N N 284 
PRO HG2    H N N 285 
PRO HG3    H N N 286 
PRO HD2    H N N 287 
PRO HD3    H N N 288 
PRO HXT    H N N 289 
RS3 O4     O N N 290 
RS3 C4     C N N 291 
RS3 N3     N N N 292 
RS3 C2     C N N 293 
RS3 O2     O N N 294 
RS3 C4A    C N N 295 
RS3 C10    C N N 296 
RS3 N1     N N N 297 
RS3 N5     N N N 298 
RS3 C5A    C Y N 299 
RS3 C6     C Y N 300 
RS3 C7     C Y N 301 
RS3 C7M    C N N 302 
RS3 C8     C Y N 303 
RS3 N8     N N N 304 
RS3 C19    C N N 305 
RS3 C20    C N N 306 
RS3 C9     C Y N 307 
RS3 C9A    C Y N 308 
RS3 N10    N N N 309 
RS3 "C1'"  C N N 310 
RS3 "C2'"  C N S 311 
RS3 "O2'"  O N N 312 
RS3 "C3'"  C N S 313 
RS3 "O3'"  O N N 314 
RS3 "C4'"  C N R 315 
RS3 "O4'"  O N N 316 
RS3 "C5'"  C N N 317 
RS3 "O5'"  O N N 318 
RS3 HN3    H N N 319 
RS3 H6     H N N 320 
RS3 H17M   H N N 321 
RS3 H27M   H N N 322 
RS3 H37M   H N N 323 
RS3 H119   H N N 324 
RS3 H219   H N N 325 
RS3 H319   H N N 326 
RS3 H120   H N N 327 
RS3 H220   H N N 328 
RS3 H320   H N N 329 
RS3 H9     H N N 330 
RS3 "H11'" H N N 331 
RS3 "H21'" H N N 332 
RS3 "H2'"  H N N 333 
RS3 "HO2'" H N N 334 
RS3 "H3'"  H N N 335 
RS3 "HO3'" H N N 336 
RS3 "H4'"  H N N 337 
RS3 "HO4'" H N N 338 
RS3 "H15'" H N N 339 
RS3 "H25'" H N N 340 
RS3 "HO5'" H N N 341 
SER N      N N N 342 
SER CA     C N S 343 
SER C      C N N 344 
SER O      O N N 345 
SER CB     C N N 346 
SER OG     O N N 347 
SER OXT    O N N 348 
SER H      H N N 349 
SER H2     H N N 350 
SER HA     H N N 351 
SER HB2    H N N 352 
SER HB3    H N N 353 
SER HG     H N N 354 
SER HXT    H N N 355 
THR N      N N N 356 
THR CA     C N S 357 
THR C      C N N 358 
THR O      O N N 359 
THR CB     C N R 360 
THR OG1    O N N 361 
THR CG2    C N N 362 
THR OXT    O N N 363 
THR H      H N N 364 
THR H2     H N N 365 
THR HA     H N N 366 
THR HB     H N N 367 
THR HG1    H N N 368 
THR HG21   H N N 369 
THR HG22   H N N 370 
THR HG23   H N N 371 
THR HXT    H N N 372 
TRP N      N N N 373 
TRP CA     C N S 374 
TRP C      C N N 375 
TRP O      O N N 376 
TRP CB     C N N 377 
TRP CG     C Y N 378 
TRP CD1    C Y N 379 
TRP CD2    C Y N 380 
TRP NE1    N Y N 381 
TRP CE2    C Y N 382 
TRP CE3    C Y N 383 
TRP CZ2    C Y N 384 
TRP CZ3    C Y N 385 
TRP CH2    C Y N 386 
TRP OXT    O N N 387 
TRP H      H N N 388 
TRP H2     H N N 389 
TRP HA     H N N 390 
TRP HB2    H N N 391 
TRP HB3    H N N 392 
TRP HD1    H N N 393 
TRP HE1    H N N 394 
TRP HE3    H N N 395 
TRP HZ2    H N N 396 
TRP HZ3    H N N 397 
TRP HH2    H N N 398 
TRP HXT    H N N 399 
TYR N      N N N 400 
TYR CA     C N S 401 
TYR C      C N N 402 
TYR O      O N N 403 
TYR CB     C N N 404 
TYR CG     C Y N 405 
TYR CD1    C Y N 406 
TYR CD2    C Y N 407 
TYR CE1    C Y N 408 
TYR CE2    C Y N 409 
TYR CZ     C Y N 410 
TYR OH     O N N 411 
TYR OXT    O N N 412 
TYR H      H N N 413 
TYR H2     H N N 414 
TYR HA     H N N 415 
TYR HB2    H N N 416 
TYR HB3    H N N 417 
TYR HD1    H N N 418 
TYR HD2    H N N 419 
TYR HE1    H N N 420 
TYR HE2    H N N 421 
TYR HH     H N N 422 
TYR HXT    H N N 423 
VAL N      N N N 424 
VAL CA     C N S 425 
VAL C      C N N 426 
VAL O      O N N 427 
VAL CB     C N N 428 
VAL CG1    C N N 429 
VAL CG2    C N N 430 
VAL OXT    O N N 431 
VAL H      H N N 432 
VAL H2     H N N 433 
VAL HA     H N N 434 
VAL HB     H N N 435 
VAL HG11   H N N 436 
VAL HG12   H N N 437 
VAL HG13   H N N 438 
VAL HG21   H N N 439 
VAL HG22   H N N 440 
VAL HG23   H N N 441 
VAL HXT    H N N 442 
# 
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  
GLN N     CA     sing N N 70  
GLN N     H      sing N N 71  
GLN N     H2     sing N N 72  
GLN CA    C      sing N N 73  
GLN CA    CB     sing N N 74  
GLN CA    HA     sing N N 75  
GLN C     O      doub N N 76  
GLN C     OXT    sing N N 77  
GLN CB    CG     sing N N 78  
GLN CB    HB2    sing N N 79  
GLN CB    HB3    sing N N 80  
GLN CG    CD     sing N N 81  
GLN CG    HG2    sing N N 82  
GLN CG    HG3    sing N N 83  
GLN CD    OE1    doub N N 84  
GLN CD    NE2    sing N N 85  
GLN NE2   HE21   sing N N 86  
GLN NE2   HE22   sing N N 87  
GLN OXT   HXT    sing N N 88  
GLU N     CA     sing N N 89  
GLU N     H      sing N N 90  
GLU N     H2     sing N N 91  
GLU CA    C      sing N N 92  
GLU CA    CB     sing N N 93  
GLU CA    HA     sing N N 94  
GLU C     O      doub N N 95  
GLU C     OXT    sing N N 96  
GLU CB    CG     sing N N 97  
GLU CB    HB2    sing N N 98  
GLU CB    HB3    sing N N 99  
GLU CG    CD     sing N N 100 
GLU CG    HG2    sing N N 101 
GLU CG    HG3    sing N N 102 
GLU CD    OE1    doub N N 103 
GLU CD    OE2    sing N N 104 
GLU OE2   HE2    sing N N 105 
GLU OXT   HXT    sing N N 106 
GLY N     CA     sing N N 107 
GLY N     H      sing N N 108 
GLY N     H2     sing N N 109 
GLY CA    C      sing N N 110 
GLY CA    HA2    sing N N 111 
GLY CA    HA3    sing N N 112 
GLY C     O      doub N N 113 
GLY C     OXT    sing N N 114 
GLY OXT   HXT    sing N N 115 
GOL C1    O1     sing N N 116 
GOL C1    C2     sing N N 117 
GOL C1    H11    sing N N 118 
GOL C1    H12    sing N N 119 
GOL O1    HO1    sing N N 120 
GOL C2    O2     sing N N 121 
GOL C2    C3     sing N N 122 
GOL C2    H2     sing N N 123 
GOL O2    HO2    sing N N 124 
GOL C3    O3     sing N N 125 
GOL C3    H31    sing N N 126 
GOL C3    H32    sing N N 127 
GOL O3    HO3    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PRO N     CA     sing N N 260 
PRO N     CD     sing N N 261 
PRO N     H      sing N N 262 
PRO CA    C      sing N N 263 
PRO CA    CB     sing N N 264 
PRO CA    HA     sing N N 265 
PRO C     O      doub N N 266 
PRO C     OXT    sing N N 267 
PRO CB    CG     sing N N 268 
PRO CB    HB2    sing N N 269 
PRO CB    HB3    sing N N 270 
PRO CG    CD     sing N N 271 
PRO CG    HG2    sing N N 272 
PRO CG    HG3    sing N N 273 
PRO CD    HD2    sing N N 274 
PRO CD    HD3    sing N N 275 
PRO OXT   HXT    sing N N 276 
RS3 C4    C4A    sing N N 277 
RS3 C4    O4     doub N N 278 
RS3 N3    C4     sing N N 279 
RS3 N3    HN3    sing N N 280 
RS3 C2    N1     sing N N 281 
RS3 C2    N3     sing N N 282 
RS3 O2    C2     doub N N 283 
RS3 C4A   N5     doub N N 284 
RS3 C10   N10    sing N N 285 
RS3 C10   C4A    sing N N 286 
RS3 N1    C10    doub N N 287 
RS3 N5    C5A    sing N N 288 
RS3 C5A   C6     doub Y N 289 
RS3 C6    C7     sing Y N 290 
RS3 C6    H6     sing N N 291 
RS3 C7    C7M    sing N N 292 
RS3 C7M   H17M   sing N N 293 
RS3 C7M   H27M   sing N N 294 
RS3 C7M   H37M   sing N N 295 
RS3 C8    N8     sing N N 296 
RS3 C8    C7     doub Y N 297 
RS3 N8    C20    sing N N 298 
RS3 C19   N8     sing N N 299 
RS3 C19   H119   sing N N 300 
RS3 C19   H219   sing N N 301 
RS3 C19   H319   sing N N 302 
RS3 C20   H120   sing N N 303 
RS3 C20   H220   sing N N 304 
RS3 C20   H320   sing N N 305 
RS3 C9    C8     sing Y N 306 
RS3 C9    H9     sing N N 307 
RS3 C9A   C9     doub Y N 308 
RS3 C9A   C5A    sing Y N 309 
RS3 N10   C9A    sing N N 310 
RS3 "C1'" N10    sing N N 311 
RS3 "C1'" "H11'" sing N N 312 
RS3 "C1'" "H21'" sing N N 313 
RS3 "C2'" "C1'"  sing N N 314 
RS3 "C2'" "H2'"  sing N N 315 
RS3 "O2'" "C2'"  sing N N 316 
RS3 "O2'" "HO2'" sing N N 317 
RS3 "C3'" "C4'"  sing N N 318 
RS3 "C3'" "C2'"  sing N N 319 
RS3 "C3'" "H3'"  sing N N 320 
RS3 "O3'" "C3'"  sing N N 321 
RS3 "O3'" "HO3'" sing N N 322 
RS3 "C4'" "O4'"  sing N N 323 
RS3 "C4'" "H4'"  sing N N 324 
RS3 "O4'" "HO4'" sing N N 325 
RS3 "C5'" "C4'"  sing N N 326 
RS3 "C5'" "H15'" sing N N 327 
RS3 "C5'" "H25'" sing N N 328 
RS3 "O5'" "C5'"  sing N N 329 
RS3 "O5'" "HO5'" sing N N 330 
SER N     CA     sing N N 331 
SER N     H      sing N N 332 
SER N     H2     sing N N 333 
SER CA    C      sing N N 334 
SER CA    CB     sing N N 335 
SER CA    HA     sing N N 336 
SER C     O      doub N N 337 
SER C     OXT    sing N N 338 
SER CB    OG     sing N N 339 
SER CB    HB2    sing N N 340 
SER CB    HB3    sing N N 341 
SER OG    HG     sing N N 342 
SER OXT   HXT    sing N N 343 
THR N     CA     sing N N 344 
THR N     H      sing N N 345 
THR N     H2     sing N N 346 
THR CA    C      sing N N 347 
THR CA    CB     sing N N 348 
THR CA    HA     sing N N 349 
THR C     O      doub N N 350 
THR C     OXT    sing N N 351 
THR CB    OG1    sing N N 352 
THR CB    CG2    sing N N 353 
THR CB    HB     sing N N 354 
THR OG1   HG1    sing N N 355 
THR CG2   HG21   sing N N 356 
THR CG2   HG22   sing N N 357 
THR CG2   HG23   sing N N 358 
THR OXT   HXT    sing N N 359 
TRP N     CA     sing N N 360 
TRP N     H      sing N N 361 
TRP N     H2     sing N N 362 
TRP CA    C      sing N N 363 
TRP CA    CB     sing N N 364 
TRP CA    HA     sing N N 365 
TRP C     O      doub N N 366 
TRP C     OXT    sing N N 367 
TRP CB    CG     sing N N 368 
TRP CB    HB2    sing N N 369 
TRP CB    HB3    sing N N 370 
TRP CG    CD1    doub Y N 371 
TRP CG    CD2    sing Y N 372 
TRP CD1   NE1    sing Y N 373 
TRP CD1   HD1    sing N N 374 
TRP CD2   CE2    doub Y N 375 
TRP CD2   CE3    sing Y N 376 
TRP NE1   CE2    sing Y N 377 
TRP NE1   HE1    sing N N 378 
TRP CE2   CZ2    sing Y N 379 
TRP CE3   CZ3    doub Y N 380 
TRP CE3   HE3    sing N N 381 
TRP CZ2   CH2    doub Y N 382 
TRP CZ2   HZ2    sing N N 383 
TRP CZ3   CH2    sing Y N 384 
TRP CZ3   HZ3    sing N N 385 
TRP CH2   HH2    sing N N 386 
TRP OXT   HXT    sing N N 387 
TYR N     CA     sing N N 388 
TYR N     H      sing N N 389 
TYR N     H2     sing N N 390 
TYR CA    C      sing N N 391 
TYR CA    CB     sing N N 392 
TYR CA    HA     sing N N 393 
TYR C     O      doub N N 394 
TYR C     OXT    sing N N 395 
TYR CB    CG     sing N N 396 
TYR CB    HB2    sing N N 397 
TYR CB    HB3    sing N N 398 
TYR CG    CD1    doub Y N 399 
TYR CG    CD2    sing Y N 400 
TYR CD1   CE1    sing Y N 401 
TYR CD1   HD1    sing N N 402 
TYR CD2   CE2    doub Y N 403 
TYR CD2   HD2    sing N N 404 
TYR CE1   CZ     doub Y N 405 
TYR CE1   HE1    sing N N 406 
TYR CE2   CZ     sing Y N 407 
TYR CE2   HE2    sing N N 408 
TYR CZ    OH     sing N N 409 
TYR OH    HH     sing N N 410 
TYR OXT   HXT    sing N N 411 
VAL N     CA     sing N N 412 
VAL N     H      sing N N 413 
VAL N     H2     sing N N 414 
VAL CA    C      sing N N 415 
VAL CA    CB     sing N N 416 
VAL CA    HA     sing N N 417 
VAL C     O      doub N N 418 
VAL C     OXT    sing N N 419 
VAL CB    CG1    sing N N 420 
VAL CB    CG2    sing N N 421 
VAL CB    HB     sing N N 422 
VAL CG1   HG11   sing N N 423 
VAL CG1   HG12   sing N N 424 
VAL CG1   HG13   sing N N 425 
VAL CG2   HG21   sing N N 426 
VAL CG2   HG22   sing N N 427 
VAL CG2   HG23   sing N N 428 
VAL OXT   HXT    sing N N 429 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8S6R 
_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]   0.017013 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012282 
_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]   0.011192 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . SER A 1 14  ? 46.288  18.481  -7.597  1.00 81.18  ? 2   SER A N     1 
ATOM   2    C CA    . SER A 1 14  ? 47.172  17.582  -8.331  1.00 81.63  ? 2   SER A CA    1 
ATOM   3    C C     . SER A 1 14  ? 46.651  16.152  -8.285  1.00 87.00  ? 2   SER A C     1 
ATOM   4    O O     . SER A 1 14  ? 45.688  15.846  -7.570  1.00 78.95  ? 2   SER A O     1 
ATOM   5    C CB    . SER A 1 14  ? 48.601  17.645  -7.776  1.00 85.88  ? 2   SER A CB    1 
ATOM   6    O OG    . SER A 1 14  ? 49.448  16.680  -8.385  1.00 87.81  ? 2   SER A OG    1 
ATOM   7    N N     . ASP A 1 15  ? 47.273  15.291  -9.092  1.00 84.37  ? 3   ASP A N     1 
ATOM   8    C CA    . ASP A 1 15  ? 46.971  13.863  -9.124  1.00 78.55  ? 3   ASP A CA    1 
ATOM   9    C C     . ASP A 1 15  ? 45.531  13.543  -9.535  1.00 78.03  ? 3   ASP A C     1 
ATOM   10   O O     . ASP A 1 15  ? 45.241  12.399  -9.903  1.00 73.93  ? 3   ASP A O     1 
ATOM   11   C CB    . ASP A 1 15  ? 47.331  13.216  -7.783  1.00 80.93  ? 3   ASP A CB    1 
ATOM   12   C CG    . ASP A 1 15  ? 47.648  11.741  -7.915  1.00 94.74  ? 3   ASP A CG    1 
ATOM   13   O OD1   . ASP A 1 15  ? 47.441  11.175  -9.010  1.00 97.43  ? 3   ASP A OD1   1 
ATOM   14   O OD2   . ASP A 1 15  ? 48.115  11.148  -6.921  1.00 105.62 ? 3   ASP A OD2   1 
ATOM   15   N N     . GLY A 1 16  ? 44.624  14.529  -9.479  1.00 61.90  ? 4   GLY A N     1 
ATOM   16   C CA    . GLY A 1 16  ? 43.261  14.375  -9.944  1.00 49.07  ? 4   GLY A CA    1 
ATOM   17   C C     . GLY A 1 16  ? 42.412  13.412  -9.151  1.00 44.94  ? 4   GLY A C     1 
ATOM   18   O O     . GLY A 1 16  ? 41.241  13.206  -9.502  1.00 40.24  ? 4   GLY A O     1 
ATOM   19   N N     . ARG A 1 17  ? 42.958  12.817  -8.093  1.00 47.90  ? 5   ARG A N     1 
ATOM   20   C CA    . ARG A 1 17  ? 42.188  11.871  -7.296  1.00 45.54  ? 5   ARG A CA    1 
ATOM   21   C C     . ARG A 1 17  ? 41.126  12.583  -6.466  1.00 41.93  ? 5   ARG A C     1 
ATOM   22   O O     . ARG A 1 17  ? 39.986  12.114  -6.376  1.00 38.48  ? 5   ARG A O     1 
ATOM   23   C CB    . ARG A 1 17  ? 43.125  11.062  -6.398  1.00 54.46  ? 5   ARG A CB    1 
ATOM   24   C CG    . ARG A 1 17  ? 42.405  10.005  -5.590  1.00 50.85  ? 5   ARG A CG    1 
ATOM   25   C CD    . ARG A 1 17  ? 43.385  9.257   -4.696  1.00 63.28  ? 5   ARG A CD    1 
ATOM   26   N NE    . ARG A 1 17  ? 42.829  9.016   -3.369  1.00 78.63  ? 5   ARG A NE    1 
ATOM   27   C CZ    . ARG A 1 17  ? 42.934  9.862   -2.352  1.00 89.49  ? 5   ARG A CZ    1 
ATOM   28   N NH1   . ARG A 1 17  ? 43.569  11.017  -2.475  1.00 85.49  ? 5   ARG A NH1   1 
ATOM   29   N NH2   . ARG A 1 17  ? 42.387  9.541   -1.181  1.00 91.17  ? 5   ARG A NH2   1 
ATOM   30   N N     . GLU A 1 18  ? 41.479  13.707  -5.835  1.00 44.65  ? 6   GLU A N     1 
ATOM   31   C CA    . GLU A 1 18  ? 40.509  14.388  -4.983  1.00 40.87  ? 6   GLU A CA    1 
ATOM   32   C C     . GLU A 1 18  ? 39.318  14.861  -5.792  1.00 36.49  ? 6   GLU A C     1 
ATOM   33   O O     . GLU A 1 18  ? 38.167  14.703  -5.375  1.00 33.90  ? 6   GLU A O     1 
ATOM   34   C CB    . GLU A 1 18  ? 41.165  15.563  -4.262  1.00 43.81  ? 6   GLU A CB    1 
ATOM   35   C CG    . GLU A 1 18  ? 41.724  15.206  -2.895  1.00 50.21  ? 6   GLU A CG    1 
ATOM   36   C CD    . GLU A 1 18  ? 43.047  14.455  -2.950  1.00 76.21  ? 6   GLU A CD    1 
ATOM   37   O OE1   . GLU A 1 18  ? 43.519  14.122  -4.062  1.00 70.76  ? 6   GLU A OE1   1 
ATOM   38   O OE2   . GLU A 1 18  ? 43.624  14.208  -1.867  1.00 82.88  ? 6   GLU A OE2   1 
ATOM   39   N N     . SER A 1 19  ? 39.576  15.415  -6.969  1.00 36.24  ? 7   SER A N     1 
ATOM   40   C CA    . SER A 1 19  ? 38.505  15.811  -7.873  1.00 32.93  ? 7   SER A CA    1 
ATOM   41   C C     . SER A 1 19  ? 37.607  14.625  -8.244  1.00 30.26  ? 7   SER A C     1 
ATOM   42   O O     . SER A 1 19  ? 36.375  14.723  -8.199  1.00 28.59  ? 7   SER A O     1 
ATOM   43   C CB    . SER A 1 19  ? 39.153  16.426  -9.111  1.00 38.55  ? 7   SER A CB    1 
ATOM   44   O OG    . SER A 1 19  ? 38.227  16.631  -10.134 1.00 38.35  ? 7   SER A OG    1 
ATOM   45   N N     . PHE A 1 20  ? 38.207  13.492  -8.629  1.00 31.45  ? 8   PHE A N     1 
ATOM   46   C CA    . PHE A 1 20  ? 37.427  12.299  -8.941  1.00 29.54  ? 8   PHE A CA    1 
ATOM   47   C C     . PHE A 1 20  ? 36.536  11.905  -7.773  1.00 29.32  ? 8   PHE A C     1 
ATOM   48   O O     . PHE A 1 20  ? 35.354  11.591  -7.960  1.00 27.27  ? 8   PHE A O     1 
ATOM   49   C CB    . PHE A 1 20  ? 38.370  11.143  -9.269  1.00 32.34  ? 8   PHE A CB    1 
ATOM   50   C CG    . PHE A 1 20  ? 37.665  9.885   -9.706  1.00 31.04  ? 8   PHE A CG    1 
ATOM   51   C CD1   . PHE A 1 20  ? 37.191  9.781   -10.985 1.00 30.15  ? 8   PHE A CD1   1 
ATOM   52   C CD2   . PHE A 1 20  ? 37.481  8.833   -8.824  1.00 38.96  ? 8   PHE A CD2   1 
ATOM   53   C CE1   . PHE A 1 20  ? 36.571  8.615   -11.411 1.00 35.02  ? 8   PHE A CE1   1 
ATOM   54   C CE2   . PHE A 1 20  ? 36.850  7.664   -9.225  1.00 35.93  ? 8   PHE A CE2   1 
ATOM   55   C CZ    . PHE A 1 20  ? 36.388  7.558   -10.526 1.00 43.85  ? 8   PHE A CZ    1 
ATOM   56   N N     . LEU A 1 21  ? 37.091  11.894  -6.556  1.00 30.34  ? 9   LEU A N     1 
ATOM   57   C CA    . LEU A 1 21  ? 36.323  11.416  -5.414  1.00 33.25  ? 9   LEU A CA    1 
ATOM   58   C C     . LEU A 1 21  ? 35.222  12.399  -5.032  1.00 27.81  ? 9   LEU A C     1 
ATOM   59   O O     . LEU A 1 21  ? 34.135  11.984  -4.613  1.00 28.01  ? 9   LEU A O     1 
ATOM   60   C CB    . LEU A 1 21  ? 37.254  11.157  -4.239  1.00 35.61  ? 9   LEU A CB    1 
ATOM   61   C CG    . LEU A 1 21  ? 38.207  9.968   -4.376  1.00 37.40  ? 9   LEU A CG    1 
ATOM   62   C CD1   . LEU A 1 21  ? 39.239  10.019  -3.274  1.00 46.22  ? 9   LEU A CD1   1 
ATOM   63   C CD2   . LEU A 1 21  ? 37.421  8.648   -4.335  1.00 38.25  ? 9   LEU A CD2   1 
ATOM   64   N N     . GLU A 1 22  ? 35.478  13.707  -5.184  1.00 29.63  ? 10  GLU A N     1 
ATOM   65   C CA    . GLU A 1 22  ? 34.458  14.704  -4.870  1.00 28.75  ? 10  GLU A CA    1 
ATOM   66   C C     . GLU A 1 22  ? 33.289  14.601  -5.832  1.00 28.37  ? 10  GLU A C     1 
ATOM   67   O O     . GLU A 1 22  ? 32.123  14.642  -5.410  1.00 27.64  ? 10  GLU A O     1 
ATOM   68   C CB    . GLU A 1 22  ? 35.063  16.103  -4.940  1.00 35.42  ? 10  GLU A CB    1 
ATOM   69   C CG    . GLU A 1 22  ? 34.054  17.202  -4.704  1.00 50.28  ? 10  GLU A CG    1 
ATOM   70   C CD    . GLU A 1 22  ? 34.703  18.566  -4.601  1.00 74.75  ? 10  GLU A CD    1 
ATOM   71   O OE1   . GLU A 1 22  ? 35.954  18.629  -4.663  1.00 70.67  ? 10  GLU A OE1   1 
ATOM   72   O OE2   . GLU A 1 22  ? 33.965  19.569  -4.456  1.00 84.32  ? 10  GLU A OE2   1 
ATOM   73   N N     . VAL A 1 23  ? 33.575  14.446  -7.121  1.00 26.87  ? 11  VAL A N     1 
ATOM   74   C CA    . VAL A 1 23  ? 32.508  14.244  -8.097  1.00 26.51  ? 11  VAL A CA    1 
ATOM   75   C C     . VAL A 1 23  ? 31.747  12.934  -7.822  1.00 26.58  ? 11  VAL A C     1 
ATOM   76   O O     . VAL A 1 23  ? 30.510  12.907  -7.845  1.00 27.75  ? 11  VAL A O     1 
ATOM   77   C CB    . VAL A 1 23  ? 33.050  14.343  -9.534  1.00 27.24  ? 11  VAL A CB    1 
ATOM   78   C CG1   . VAL A 1 23  ? 31.989  13.942  -10.523 1.00 30.14  ? 11  VAL A CG1   1 
ATOM   79   C CG2   . VAL A 1 23  ? 33.563  15.731  -9.839  1.00 29.67  ? 11  VAL A CG2   1 
ATOM   80   N N     . MET A 1 24  ? 32.449  11.849  -7.498  1.00 24.51  ? 12  MET A N     1 
ATOM   81   C CA    A MET A 1 24  ? 31.751  10.605  -7.186  0.70 24.23  ? 12  MET A CA    1 
ATOM   82   C CA    B MET A 1 24  ? 31.763  10.600  -7.173  0.30 24.96  ? 12  MET A CA    1 
ATOM   83   C C     . MET A 1 24  ? 30.773  10.822  -6.040  1.00 27.27  ? 12  MET A C     1 
ATOM   84   O O     . MET A 1 24  ? 29.626  10.359  -6.093  1.00 26.34  ? 12  MET A O     1 
ATOM   85   C CB    A MET A 1 24  ? 32.780  9.547   -6.815  0.70 28.04  ? 12  MET A CB    1 
ATOM   86   C CB    B MET A 1 24  ? 32.782  9.538   -6.759  0.30 28.07  ? 12  MET A CB    1 
ATOM   87   C CG    A MET A 1 24  ? 32.205  8.199   -6.527  0.70 29.70  ? 12  MET A CG    1 
ATOM   88   C CG    B MET A 1 24  ? 33.377  8.726   -7.893  0.30 25.31  ? 12  MET A CG    1 
ATOM   89   S SD    A MET A 1 24  ? 33.560  7.019   -6.510  0.70 46.43  ? 12  MET A SD    1 
ATOM   90   S SD    B MET A 1 24  ? 34.158  7.212   -7.266  0.30 26.24  ? 12  MET A SD    1 
ATOM   91   C CE    A MET A 1 24  ? 32.712  5.578   -7.110  0.70 39.09  ? 12  MET A CE    1 
ATOM   92   C CE    B MET A 1 24  ? 33.112  6.895   -5.838  0.30 25.82  ? 12  MET A CE    1 
ATOM   93   N N     . ARG A 1 25  ? 31.217  11.520  -4.986  1.00 25.20  ? 13  ARG A N     1 
ATOM   94   C CA    . ARG A 1 25  ? 30.349  11.796  -3.853  1.00 24.55  ? 13  ARG A CA    1 
ATOM   95   C C     . ARG A 1 25  ? 29.155  12.624  -4.283  1.00 30.24  ? 13  ARG A C     1 
ATOM   96   O O     . ARG A 1 25  ? 28.019  12.348  -3.874  1.00 28.32  ? 13  ARG A O     1 
ATOM   97   C CB    . ARG A 1 25  ? 31.115  12.528  -2.743  1.00 30.98  ? 13  ARG A CB    1 
ATOM   98   C CG    . ARG A 1 25  ? 30.262  12.879  -1.558  1.00 30.42  ? 13  ARG A CG    1 
ATOM   99   C CD    . ARG A 1 25  ? 30.944  13.918  -0.676  1.00 44.35  ? 13  ARG A CD    1 
ATOM   100  N NE    . ARG A 1 25  ? 31.506  13.309  0.520   1.00 59.45  ? 13  ARG A NE    1 
ATOM   101  C CZ    . ARG A 1 25  ? 31.802  13.977  1.627   1.00 59.54  ? 13  ARG A CZ    1 
ATOM   102  N NH1   . ARG A 1 25  ? 31.605  15.284  1.718   1.00 58.99  ? 13  ARG A NH1   1 
ATOM   103  N NH2   . ARG A 1 25  ? 32.303  13.318  2.668   1.00 68.91  ? 13  ARG A NH2   1 
ATOM   104  N N     . SER A 1 26  ? 29.390  13.654  -5.109  1.00 25.11  ? 14  SER A N     1 
ATOM   105  C CA    . SER A 1 26  ? 28.293  14.518  -5.518  1.00 29.54  ? 14  SER A CA    1 
ATOM   106  C C     . SER A 1 26  ? 27.276  13.747  -6.340  1.00 27.01  ? 14  SER A C     1 
ATOM   107  O O     . SER A 1 26  ? 26.069  13.966  -6.214  1.00 27.18  ? 14  SER A O     1 
ATOM   108  C CB    . SER A 1 26  ? 28.833  15.680  -6.348  1.00 29.72  ? 14  SER A CB    1 
ATOM   109  O OG    . SER A 1 26  ? 29.612  16.524  -5.544  1.00 34.60  ? 14  SER A OG    1 
ATOM   110  N N     . VAL A 1 27  ? 27.754  12.878  -7.215  1.00 27.25  ? 15  VAL A N     1 
ATOM   111  C CA    . VAL A 1 27  ? 26.855  12.042  -8.006  1.00 25.08  ? 15  VAL A CA    1 
ATOM   112  C C     . VAL A 1 27  ? 26.017  11.156  -7.096  1.00 26.66  ? 15  VAL A C     1 
ATOM   113  O O     . VAL A 1 27  ? 24.784  11.126  -7.199  1.00 24.25  ? 15  VAL A O     1 
ATOM   114  C CB    . VAL A 1 27  ? 27.649  11.232  -9.043  1.00 25.70  ? 15  VAL A CB    1 
ATOM   115  C CG1   . VAL A 1 27  ? 26.753  10.198  -9.692  1.00 24.59  ? 15  VAL A CG1   1 
ATOM   116  C CG2   . VAL A 1 27  ? 28.277  12.154  -10.070 1.00 26.65  ? 15  VAL A CG2   1 
ATOM   117  N N     . TYR A 1 28  ? 26.661  10.459  -6.164  1.00 24.47  ? 16  TYR A N     1 
ATOM   118  C CA    . TYR A 1 28  ? 25.904  9.648   -5.218  1.00 25.52  ? 16  TYR A CA    1 
ATOM   119  C C     . TYR A 1 28  ? 24.846  10.478  -4.518  1.00 27.66  ? 16  TYR A C     1 
ATOM   120  O O     . TYR A 1 28  ? 23.683  10.076  -4.406  1.00 27.25  ? 16  TYR A O     1 
ATOM   121  C CB    . TYR A 1 28  ? 26.855  9.004   -4.219  1.00 25.50  ? 16  TYR A CB    1 
ATOM   122  C CG    . TYR A 1 28  ? 27.446  7.667   -4.618  1.00 24.48  ? 16  TYR A CG    1 
ATOM   123  C CD1   . TYR A 1 28  ? 26.663  6.660   -5.154  1.00 26.12  ? 16  TYR A CD1   1 
ATOM   124  C CD2   . TYR A 1 28  ? 28.779  7.404   -4.380  1.00 27.45  ? 16  TYR A CD2   1 
ATOM   125  C CE1   . TYR A 1 28  ? 27.220  5.425   -5.460  1.00 29.02  ? 16  TYR A CE1   1 
ATOM   126  C CE2   . TYR A 1 28  ? 29.343  6.181   -4.667  1.00 25.95  ? 16  TYR A CE2   1 
ATOM   127  C CZ    . TYR A 1 28  ? 28.558  5.190   -5.224  1.00 25.09  ? 16  TYR A CZ    1 
ATOM   128  O OH    . TYR A 1 28  ? 29.120  3.945   -5.513  1.00 27.33  ? 16  TYR A OH    1 
ATOM   129  N N     . GLU A 1 29  ? 25.224  11.660  -4.043  1.00 25.35  ? 17  GLU A N     1 
ATOM   130  C CA    . GLU A 1 29  ? 24.259  12.456  -3.286  1.00 29.72  ? 17  GLU A CA    1 
ATOM   131  C C     . GLU A 1 29  ? 23.085  12.916  -4.154  1.00 27.20  ? 17  GLU A C     1 
ATOM   132  O O     . GLU A 1 29  ? 21.936  12.975  -3.686  1.00 29.82  ? 17  GLU A O     1 
ATOM   133  C CB    . GLU A 1 29  ? 24.998  13.622  -2.647  1.00 30.33  ? 17  GLU A CB    1 
ATOM   134  C CG    . GLU A 1 29  ? 25.951  13.161  -1.557  1.00 39.33  ? 17  GLU A CG    1 
ATOM   135  C CD    . GLU A 1 29  ? 26.836  14.262  -0.999  1.00 55.99  ? 17  GLU A CD    1 
ATOM   136  O OE1   . GLU A 1 29  ? 26.921  15.355  -1.614  1.00 54.17  ? 17  GLU A OE1   1 
ATOM   137  O OE2   . GLU A 1 29  ? 27.454  14.012  0.066   1.00 52.27  ? 17  GLU A OE2   1 
ATOM   138  N N     . ARG A 1 30  ? 23.344  13.153  -5.434  1.00 25.63  ? 18  ARG A N     1 
ATOM   139  C CA    . ARG A 1 30  ? 22.273  13.559  -6.333  1.00 29.03  ? 18  ARG A CA    1 
ATOM   140  C C     . ARG A 1 30  ? 21.192  12.485  -6.437  1.00 27.72  ? 18  ARG A C     1 
ATOM   141  O O     . ARG A 1 30  ? 20.017  12.810  -6.654  1.00 30.54  ? 18  ARG A O     1 
ATOM   142  C CB    . ARG A 1 30  ? 22.879  13.881  -7.700  1.00 27.88  ? 18  ARG A CB    1 
ATOM   143  C CG    . ARG A 1 30  ? 21.880  14.231  -8.788  1.00 29.78  ? 18  ARG A CG    1 
ATOM   144  C CD    . ARG A 1 30  ? 22.565  14.773  -10.076 1.00 31.64  ? 18  ARG A CD    1 
ATOM   145  N NE    . ARG A 1 30  ? 23.090  16.130  -9.929  1.00 32.21  ? 18  ARG A NE    1 
ATOM   146  C CZ    . ARG A 1 30  ? 23.706  16.785  -10.906 1.00 31.84  ? 18  ARG A CZ    1 
ATOM   147  N NH1   . ARG A 1 30  ? 23.918  16.223  -12.087 1.00 31.90  ? 18  ARG A NH1   1 
ATOM   148  N NH2   . ARG A 1 30  ? 24.144  18.021  -10.685 1.00 36.45  ? 18  ARG A NH2   1 
ATOM   149  N N     . TYR A 1 31  ? 21.568  11.204  -6.270  1.00 25.80  ? 19  TYR A N     1 
ATOM   150  C CA    . TYR A 1 31  ? 20.655  10.069  -6.343  1.00 26.51  ? 19  TYR A CA    1 
ATOM   151  C C     . TYR A 1 31  ? 20.353  9.492   -4.963  1.00 28.03  ? 19  TYR A C     1 
ATOM   152  O O     . TYR A 1 31  ? 19.953  8.330   -4.849  1.00 28.29  ? 19  TYR A O     1 
ATOM   153  C CB    . TYR A 1 31  ? 21.199  9.035   -7.347  1.00 24.09  ? 19  TYR A CB    1 
ATOM   154  C CG    . TYR A 1 31  ? 21.272  9.679   -8.722  1.00 23.62  ? 19  TYR A CG    1 
ATOM   155  C CD1   . TYR A 1 31  ? 20.177  9.696   -9.562  1.00 25.47  ? 19  TYR A CD1   1 
ATOM   156  C CD2   . TYR A 1 31  ? 22.425  10.359  -9.145  1.00 23.73  ? 19  TYR A CD2   1 
ATOM   157  C CE1   . TYR A 1 31  ? 20.223  10.342  -10.814 1.00 25.76  ? 19  TYR A CE1   1 
ATOM   158  C CE2   . TYR A 1 31  ? 22.482  10.983  -10.406 1.00 22.16  ? 19  TYR A CE2   1 
ATOM   159  C CZ    . TYR A 1 31  ? 21.381  10.980  -11.229 1.00 24.05  ? 19  TYR A CZ    1 
ATOM   160  O OH    . TYR A 1 31  ? 21.439  11.621  -12.441 1.00 24.81  ? 19  TYR A OH    1 
ATOM   161  N N     . LEU A 1 32  ? 20.494  10.321  -3.920  1.00 24.55  ? 20  LEU A N     1 
ATOM   162  C CA    . LEU A 1 32  ? 20.087  10.003  -2.551  1.00 26.01  ? 20  LEU A CA    1 
ATOM   163  C C     . LEU A 1 32  ? 20.880  8.858   -1.931  1.00 28.03  ? 20  LEU A C     1 
ATOM   164  O O     . LEU A 1 32  ? 20.414  8.217   -0.982  1.00 29.26  ? 20  LEU A O     1 
ATOM   165  C CB    . LEU A 1 32  ? 18.578  9.771   -2.428  1.00 25.37  ? 20  LEU A CB    1 
ATOM   166  C CG    . LEU A 1 32  ? 17.745  11.024  -2.667  1.00 24.26  ? 20  LEU A CG    1 
ATOM   167  C CD1   . LEU A 1 32  ? 16.298  10.672  -2.389  1.00 25.23  ? 20  LEU A CD1   1 
ATOM   168  C CD2   . LEU A 1 32  ? 18.164  12.196  -1.778  1.00 30.36  ? 20  LEU A CD2   1 
ATOM   169  N N     . VAL A 1 33  ? 22.107  8.638   -2.400  1.00 25.98  ? 21  VAL A N     1 
ATOM   170  C CA    . VAL A 1 33  ? 23.006  7.622   -1.853  1.00 28.49  ? 21  VAL A CA    1 
ATOM   171  C C     . VAL A 1 33  ? 23.944  8.303   -0.864  1.00 32.85  ? 21  VAL A C     1 
ATOM   172  O O     . VAL A 1 33  ? 24.578  9.321   -1.188  1.00 31.52  ? 21  VAL A O     1 
ATOM   173  C CB    . VAL A 1 33  ? 23.783  6.906   -2.977  1.00 26.83  ? 21  VAL A CB    1 
ATOM   174  C CG1   . VAL A 1 33  ? 24.747  5.869   -2.377  1.00 29.25  ? 21  VAL A CG1   1 
ATOM   175  C CG2   . VAL A 1 33  ? 22.819  6.256   -3.982  1.00 28.05  ? 21  VAL A CG2   1 
ATOM   176  N N     . GLY A 1 34  ? 24.035  7.752   0.348   1.00 38.93  ? 22  GLY A N     1 
ATOM   177  C CA    . GLY A 1 34  ? 24.832  8.387   1.379   1.00 43.90  ? 22  GLY A CA    1 
ATOM   178  C C     . GLY A 1 34  ? 24.265  9.704   1.859   1.00 44.36  ? 22  GLY A C     1 
ATOM   179  O O     . GLY A 1 34  ? 25.030  10.619  2.190   1.00 46.03  ? 22  GLY A O     1 
ATOM   180  N N     . VAL A 1 35  ? 22.941  9.829   1.892   1.00 40.56  ? 23  VAL A N     1 
ATOM   181  C CA    . VAL A 1 35  ? 22.257  11.051  2.300   1.00 43.62  ? 23  VAL A CA    1 
ATOM   182  C C     . VAL A 1 35  ? 21.410  10.719  3.523   1.00 35.21  ? 23  VAL A C     1 
ATOM   183  O O     . VAL A 1 35  ? 20.628  9.765   3.476   1.00 41.99  ? 23  VAL A O     1 
ATOM   184  C CB    . VAL A 1 35  ? 21.368  11.613  1.174   1.00 37.50  ? 23  VAL A CB    1 
ATOM   185  C CG1   . VAL A 1 35  ? 20.614  12.826  1.639   1.00 38.64  ? 23  VAL A CG1   1 
ATOM   186  C CG2   . VAL A 1 35  ? 22.206  11.955  -0.048  1.00 38.51  ? 23  VAL A CG2   1 
ATOM   187  N N     . PRO A 1 36  ? 21.528  11.457  4.626   1.00 36.71  ? 24  PRO A N     1 
ATOM   188  C CA    . PRO A 1 36  ? 20.700  11.146  5.796   1.00 40.96  ? 24  PRO A CA    1 
ATOM   189  C C     . PRO A 1 36  ? 19.231  11.440  5.529   1.00 39.68  ? 24  PRO A C     1 
ATOM   190  O O     . PRO A 1 36  ? 18.879  12.261  4.676   1.00 43.57  ? 24  PRO A O     1 
ATOM   191  C CB    . PRO A 1 36  ? 21.257  12.071  6.888   1.00 48.57  ? 24  PRO A CB    1 
ATOM   192  C CG    . PRO A 1 36  ? 21.928  13.186  6.150   1.00 43.00  ? 24  PRO A CG    1 
ATOM   193  C CD    . PRO A 1 36  ? 22.437  12.600  4.862   1.00 39.47  ? 24  PRO A CD    1 
ATOM   194  N N     . GLY A 1 37  ? 18.368  10.731  6.256   1.00 40.33  ? 25  GLY A N     1 
ATOM   195  C CA    . GLY A 1 37  ? 16.946  11.008  6.217   1.00 41.49  ? 25  GLY A CA    1 
ATOM   196  C C     . GLY A 1 37  ? 16.194  10.401  5.054   1.00 36.39  ? 25  GLY A C     1 
ATOM   197  O O     . GLY A 1 37  ? 15.055  10.802  4.795   1.00 43.21  ? 25  GLY A O     1 
ATOM   198  N N     . VAL A 1 38  ? 16.779  9.436   4.354   1.00 34.34  ? 26  VAL A N     1 
ATOM   199  C CA    . VAL A 1 38  ? 16.150  8.837   3.181   1.00 29.55  ? 26  VAL A CA    1 
ATOM   200  C C     . VAL A 1 38  ? 15.341  7.625   3.607   1.00 36.98  ? 26  VAL A C     1 
ATOM   201  O O     . VAL A 1 38  ? 15.834  6.773   4.352   1.00 35.92  ? 26  VAL A O     1 
ATOM   202  C CB    . VAL A 1 38  ? 17.218  8.448   2.151   1.00 32.35  ? 26  VAL A CB    1 
ATOM   203  C CG1   . VAL A 1 38  ? 16.615  7.631   0.990   1.00 29.52  ? 26  VAL A CG1   1 
ATOM   204  C CG2   . VAL A 1 38  ? 17.887  9.728   1.647   1.00 33.86  ? 26  VAL A CG2   1 
ATOM   205  N N     . SER A 1 39  ? 14.103  7.543   3.132   1.00 28.93  ? 27  SER A N     1 
ATOM   206  C CA    . SER A 1 39  ? 13.267  6.365   3.343   1.00 32.19  ? 27  SER A CA    1 
ATOM   207  C C     . SER A 1 39  ? 13.262  5.516   2.078   1.00 25.50  ? 27  SER A C     1 
ATOM   208  O O     . SER A 1 39  ? 13.630  5.965   1.000   1.00 26.41  ? 27  SER A O     1 
ATOM   209  C CB    . SER A 1 39  ? 11.838  6.790   3.703   1.00 29.92  ? 27  SER A CB    1 
ATOM   210  O OG    . SER A 1 39  ? 11.814  7.407   4.968   1.00 39.16  ? 27  SER A OG    1 
ATOM   211  N N     . GLU A 1 40  ? 12.791  4.268   2.198   1.00 27.47  ? 28  GLU A N     1 
ATOM   212  C CA    . GLU A 1 40  ? 12.625  3.430   1.022   1.00 23.34  ? 28  GLU A CA    1 
ATOM   213  C C     . GLU A 1 40  ? 11.191  2.946   0.864   1.00 21.82  ? 28  GLU A C     1 
ATOM   214  O O     . GLU A 1 40  ? 10.505  2.651   1.850   1.00 25.95  ? 28  GLU A O     1 
ATOM   215  C CB    . GLU A 1 40  ? 13.572  2.213   1.017   1.00 24.33  ? 28  GLU A CB    1 
ATOM   216  C CG    . GLU A 1 40  ? 15.049  2.602   0.768   1.00 29.18  ? 28  GLU A CG    1 
ATOM   217  C CD    . GLU A 1 40  ? 16.020  1.424   0.902   1.00 30.89  ? 28  GLU A CD    1 
ATOM   218  O OE1   . GLU A 1 40  ? 15.594  0.239   0.887   1.00 28.03  ? 28  GLU A OE1   1 
ATOM   219  O OE2   . GLU A 1 40  ? 17.248  1.669   1.019   1.00 37.74  ? 28  GLU A OE2   1 
ATOM   220  N N     . VAL A 1 41  ? 10.789  2.847   -0.405  1.00 23.11  ? 29  VAL A N     1 
ATOM   221  C CA    . VAL A 1 41  ? 9.506   2.282   -0.803  1.00 23.26  ? 29  VAL A CA    1 
ATOM   222  C C     . VAL A 1 41  ? 9.844   1.109   -1.685  1.00 19.51  ? 29  VAL A C     1 
ATOM   223  O O     . VAL A 1 41  ? 10.503  1.267   -2.717  1.00 22.44  ? 29  VAL A O     1 
ATOM   224  C CB    . VAL A 1 41  ? 8.623   3.303   -1.542  1.00 23.36  ? 29  VAL A CB    1 
ATOM   225  C CG1   . VAL A 1 41  ? 7.290   2.686   -1.937  1.00 25.54  ? 29  VAL A CG1   1 
ATOM   226  C CG2   . VAL A 1 41  ? 8.406   4.501   -0.657  1.00 24.92  ? 29  VAL A CG2   1 
ATOM   227  N N     . TRP A 1 42  ? 9.418   -0.089  -1.262  1.00 21.63  ? 30  TRP A N     1 
ATOM   228  C CA    . TRP A 1 42  ? 9.595   -1.294  -2.072  1.00 20.87  ? 30  TRP A CA    1 
ATOM   229  C C     . TRP A 1 42  ? 8.285   -1.567  -2.800  1.00 20.47  ? 30  TRP A C     1 
ATOM   230  O O     . TRP A 1 42  ? 7.320   -2.062  -2.185  1.00 21.91  ? 30  TRP A O     1 
ATOM   231  C CB    . TRP A 1 42  ? 10.030  -2.482  -1.221  1.00 21.72  ? 30  TRP A CB    1 
ATOM   232  C CG    . TRP A 1 42  ? 11.506  -2.370  -0.746  1.00 24.67  ? 30  TRP A CG    1 
ATOM   233  C CD1   . TRP A 1 42  ? 12.243  -1.210  -0.584  1.00 22.76  ? 30  TRP A CD1   1 
ATOM   234  C CD2   . TRP A 1 42  ? 12.408  -3.453  -0.453  1.00 23.53  ? 30  TRP A CD2   1 
ATOM   235  N NE1   . TRP A 1 42  ? 13.546  -1.525  -0.180  1.00 24.60  ? 30  TRP A NE1   1 
ATOM   236  C CE2   . TRP A 1 42  ? 13.647  -2.883  -0.071  1.00 24.53  ? 30  TRP A CE2   1 
ATOM   237  C CE3   . TRP A 1 42  ? 12.277  -4.848  -0.425  1.00 23.71  ? 30  TRP A CE3   1 
ATOM   238  C CZ2   . TRP A 1 42  ? 14.754  -3.661  0.288   1.00 26.30  ? 30  TRP A CZ2   1 
ATOM   239  C CZ3   . TRP A 1 42  ? 13.384  -5.601  -0.083  1.00 27.62  ? 30  TRP A CZ3   1 
ATOM   240  C CH2   . TRP A 1 42  ? 14.578  -5.005  0.303   1.00 27.10  ? 30  TRP A CH2   1 
ATOM   241  N N     . LEU A 1 43  ? 8.257   -1.194  -4.083  1.00 19.99  ? 31  LEU A N     1 
ATOM   242  C CA    . LEU A 1 43  ? 7.100   -1.383  -4.935  1.00 19.77  ? 31  LEU A CA    1 
ATOM   243  C C     . LEU A 1 43  ? 7.121   -2.832  -5.395  1.00 19.50  ? 31  LEU A C     1 
ATOM   244  O O     . LEU A 1 43  ? 8.107   -3.315  -5.985  1.00 20.67  ? 31  LEU A O     1 
ATOM   245  C CB    . LEU A 1 43  ? 7.232   -0.475  -6.145  1.00 20.36  ? 31  LEU A CB    1 
ATOM   246  C CG    . LEU A 1 43  ? 7.369   1.008   -5.878  1.00 20.83  ? 31  LEU A CG    1 
ATOM   247  C CD1   . LEU A 1 43  ? 7.667   1.725   -7.216  1.00 21.55  ? 31  LEU A CD1   1 
ATOM   248  C CD2   . LEU A 1 43  ? 6.034   1.515   -5.348  1.00 22.12  ? 31  LEU A CD2   1 
ATOM   249  N N     . ILE A 1 44  ? 6.034   -3.553  -5.141  1.00 19.34  ? 32  ILE A N     1 
ATOM   250  C CA    . ILE A 1 44  ? 5.967   -4.985  -5.422  1.00 19.12  ? 32  ILE A CA    1 
ATOM   251  C C     . ILE A 1 44  ? 4.815   -5.236  -6.363  1.00 19.52  ? 32  ILE A C     1 
ATOM   252  O O     . ILE A 1 44  ? 3.689   -4.789  -6.104  1.00 20.79  ? 32  ILE A O     1 
ATOM   253  C CB    . ILE A 1 44  ? 5.745   -5.746  -4.114  1.00 20.05  ? 32  ILE A CB    1 
ATOM   254  C CG1   . ILE A 1 44  ? 6.931   -5.466  -3.199  1.00 21.70  ? 32  ILE A CG1   1 
ATOM   255  C CG2   . ILE A 1 44  ? 5.526   -7.252  -4.314  1.00 21.96  ? 32  ILE A CG2   1 
ATOM   256  C CD1   . ILE A 1 44  ? 6.796   -5.962  -1.822  1.00 23.69  ? 32  ILE A CD1   1 
ATOM   257  N N     . ARG A 1 45  ? 5.057   -5.912  -7.464  1.00 18.30  ? 33  ARG A N     1 
ATOM   258  C CA    . ARG A 1 45  ? 3.919   -6.335  -8.266  1.00 18.14  ? 33  ARG A CA    1 
ATOM   259  C C     . ARG A 1 45  ? 3.299   -7.575  -7.616  1.00 19.26  ? 33  ARG A C     1 
ATOM   260  O O     . ARG A 1 45  ? 4.014   -8.479  -7.149  1.00 20.01  ? 33  ARG A O     1 
ATOM   261  C CB    . ARG A 1 45  ? 4.332   -6.684  -9.679  1.00 18.87  ? 33  ARG A CB    1 
ATOM   262  C CG    . ARG A 1 45  ? 3.128   -7.101  -10.540 1.00 20.10  ? 33  ARG A CG    1 
ATOM   263  C CD    . ARG A 1 45  ? 3.476   -7.388  -11.974 1.00 20.90  ? 33  ARG A CD    1 
ATOM   264  N NE    . ARG A 1 45  ? 2.283   -7.813  -12.697 1.00 21.28  ? 33  ARG A NE    1 
ATOM   265  C CZ    . ARG A 1 45  ? 2.272   -8.479  -13.842 1.00 22.67  ? 33  ARG A CZ    1 
ATOM   266  N NH1   . ARG A 1 45  ? 3.393   -8.833  -14.450 1.00 24.54  ? 33  ARG A NH1   1 
ATOM   267  N NH2   . ARG A 1 45  ? 1.093   -8.817  -14.387 1.00 24.13  ? 33  ARG A NH2   1 
ATOM   268  N N     . HIS A 1 46  ? 1.982   -7.642  -7.579  1.00 22.24  ? 34  HIS A N     1 
ATOM   269  C CA    . HIS A 1 46  ? 1.334   -8.815  -7.013  1.00 20.63  ? 34  HIS A CA    1 
ATOM   270  C C     . HIS A 1 46  ? 1.769   -10.103 -7.732  1.00 20.35  ? 34  HIS A C     1 
ATOM   271  O O     . HIS A 1 46  ? 2.327   -10.100 -8.826  1.00 21.09  ? 34  HIS A O     1 
ATOM   272  C CB    . HIS A 1 46  ? -0.185  -8.667  -7.103  1.00 21.27  ? 34  HIS A CB    1 
ATOM   273  C CG    . HIS A 1 46  ? -0.679  -8.585  -8.507  1.00 19.80  ? 34  HIS A CG    1 
ATOM   274  N ND1   . HIS A 1 46  ? -0.859  -9.688  -9.317  1.00 23.93  ? 34  HIS A ND1   1 
ATOM   275  C CD2   . HIS A 1 46  ? -1.035  -7.508  -9.248  1.00 21.19  ? 34  HIS A CD2   1 
ATOM   276  C CE1   . HIS A 1 46  ? -1.257  -9.279  -10.517 1.00 23.24  ? 34  HIS A CE1   1 
ATOM   277  N NE2   . HIS A 1 46  ? -1.386  -7.958  -10.496 1.00 23.94  ? 34  HIS A NE2   1 
ATOM   278  N N     . ALA A 1 47  ? 1.371   -11.230 -7.087  1.00 20.11  ? 35  ALA A N     1 
ATOM   279  C CA    . ALA A 1 47  ? 1.677   -12.563 -7.616  1.00 22.48  ? 35  ALA A CA    1 
ATOM   280  C C     . ALA A 1 47  ? 0.629   -13.009 -8.656  1.00 22.73  ? 35  ALA A C     1 
ATOM   281  O O     . ALA A 1 47  ? -0.379  -12.345 -8.892  1.00 21.76  ? 35  ALA A O     1 
ATOM   282  C CB    . ALA A 1 47  ? 1.795   -13.583 -6.478  1.00 22.99  ? 35  ALA A CB    1 
ATOM   283  N N     . ASP A 1 48  ? 0.859   -14.166 -9.270  1.00 23.13  ? 36  ASP A N     1 
ATOM   284  C CA    . ASP A 1 48  ? 0.058   -14.605 -10.408 1.00 23.81  ? 36  ASP A CA    1 
ATOM   285  C C     . ASP A 1 48  ? -1.384  -14.862 -10.015 1.00 22.91  ? 36  ASP A C     1 
ATOM   286  O O     . ASP A 1 48  ? -1.657  -15.542 -9.023  1.00 23.36  ? 36  ASP A O     1 
ATOM   287  C CB    . ASP A 1 48  ? 0.571   -15.925 -10.978 1.00 25.59  ? 36  ASP A CB    1 
ATOM   288  C CG    . ASP A 1 48  ? -0.267  -16.358 -12.164 1.00 35.46  ? 36  ASP A CG    1 
ATOM   289  O OD1   . ASP A 1 48  ? -0.266  -15.637 -13.181 1.00 32.58  ? 36  ASP A OD1   1 
ATOM   290  O OD2   . ASP A 1 48  ? -0.981  -17.370 -12.067 1.00 28.90  ? 36  ASP A OD2   1 
ATOM   291  N N     . SER A 1 49  ? -2.302  -14.329 -10.822 1.00 23.18  ? 37  SER A N     1 
ATOM   292  C CA    A SER A 1 49  ? -3.712  -14.680 -10.722 0.50 25.08  ? 37  SER A CA    1 
ATOM   293  C CA    B SER A 1 49  ? -3.717  -14.668 -10.726 0.50 25.12  ? 37  SER A CA    1 
ATOM   294  C C     . SER A 1 49  ? -4.297  -14.997 -12.091 1.00 34.55  ? 37  SER A C     1 
ATOM   295  O O     . SER A 1 49  ? -5.520  -15.049 -12.231 1.00 35.39  ? 37  SER A O     1 
ATOM   296  C CB    A SER A 1 49  ? -4.472  -13.492 -10.144 0.50 33.30  ? 37  SER A CB    1 
ATOM   297  C CB    B SER A 1 49  ? -4.521  -13.499 -10.144 0.50 33.27  ? 37  SER A CB    1 
ATOM   298  O OG    A SER A 1 49  ? -4.194  -12.365 -10.952 0.50 26.81  ? 37  SER A OG    1 
ATOM   299  O OG    B SER A 1 49  ? -4.482  -13.485 -8.737  0.50 35.39  ? 37  SER A OG    1 
ATOM   300  N N     . TYR A 1 50  ? -3.463  -15.171 -13.102 1.00 27.92  ? 38  TYR A N     1 
ATOM   301  C CA    . TYR A 1 50  ? -3.909  -15.365 -14.462 1.00 34.01  ? 38  TYR A CA    1 
ATOM   302  C C     . TYR A 1 50  ? -3.914  -16.821 -14.883 1.00 33.00  ? 38  TYR A C     1 
ATOM   303  O O     . TYR A 1 50  ? -4.650  -17.176 -15.813 1.00 35.85  ? 38  TYR A O     1 
ATOM   304  C CB    . TYR A 1 50  ? -2.976  -14.575 -15.380 1.00 39.37  ? 38  TYR A CB    1 
ATOM   305  C CG    . TYR A 1 50  ? -2.721  -13.149 -14.889 1.00 48.86  ? 38  TYR A CG    1 
ATOM   306  C CD1   . TYR A 1 50  ? -1.722  -12.867 -13.940 1.00 42.73  ? 38  TYR A CD1   1 
ATOM   307  C CD2   . TYR A 1 50  ? -3.486  -12.089 -15.366 1.00 41.32  ? 38  TYR A CD2   1 
ATOM   308  C CE1   . TYR A 1 50  ? -1.498  -11.566 -13.497 1.00 44.18  ? 38  TYR A CE1   1 
ATOM   309  C CE2   . TYR A 1 50  ? -3.262  -10.782 -14.940 1.00 49.96  ? 38  TYR A CE2   1 
ATOM   310  C CZ    . TYR A 1 50  ? -2.261  -10.518 -14.014 1.00 51.23  ? 38  TYR A CZ    1 
ATOM   311  O OH    . TYR A 1 50  ? -2.049  -9.209  -13.608 1.00 34.33  ? 38  TYR A OH    1 
ATOM   312  N N     . THR A 1 51  ? -3.093  -17.672 -14.253 1.00 30.44  ? 39  THR A N     1 
ATOM   313  C CA    . THR A 1 51  ? -3.132  -19.094 -14.565 1.00 34.25  ? 39  THR A CA    1 
ATOM   314  C C     . THR A 1 51  ? -4.486  -19.652 -14.159 1.00 41.30  ? 39  THR A C     1 
ATOM   315  O O     . THR A 1 51  ? -4.908  -19.498 -13.007 1.00 39.85  ? 39  THR A O     1 
ATOM   316  C CB    . THR A 1 51  ? -2.012  -19.841 -13.845 1.00 41.69  ? 39  THR A CB    1 
ATOM   317  O OG1   . THR A 1 51  ? -0.760  -19.270 -14.236 1.00 36.77  ? 39  THR A OG1   1 
ATOM   318  C CG2   . THR A 1 51  ? -2.031  -21.313 -14.223 1.00 40.74  ? 39  THR A CG2   1 
ATOM   319  N N     . GLY A 1 52  ? -5.178  -20.256 -15.119 1.00 41.57  ? 40  GLY A N     1 
ATOM   320  C CA    . GLY A 1 52  ? -6.523  -20.742 -14.895 1.00 42.42  ? 40  GLY A CA    1 
ATOM   321  C C     . GLY A 1 52  ? -7.610  -19.694 -14.978 1.00 39.40  ? 40  GLY A C     1 
ATOM   322  O O     . GLY A 1 52  ? -8.772  -20.013 -14.693 1.00 42.71  ? 40  GLY A O     1 
ATOM   323  N N     . LEU A 1 53  ? -7.288  -18.453 -15.368 1.00 37.09  ? 41  LEU A N     1 
ATOM   324  C CA    . LEU A 1 53  ? -8.310  -17.406 -15.418 1.00 38.07  ? 41  LEU A CA    1 
ATOM   325  C C     . LEU A 1 53  ? -9.410  -17.711 -16.435 1.00 49.66  ? 41  LEU A C     1 
ATOM   326  O O     . LEU A 1 53  ? -10.540 -17.231 -16.269 1.00 42.12  ? 41  LEU A O     1 
ATOM   327  C CB    . LEU A 1 53  ? -7.662  -16.037 -15.670 1.00 40.58  ? 41  LEU A CB    1 
ATOM   328  C CG    . LEU A 1 53  ? -8.453  -14.767 -15.309 1.00 48.17  ? 41  LEU A CG    1 
ATOM   329  C CD1   . LEU A 1 53  ? -9.034  -14.807 -13.901 1.00 37.70  ? 41  LEU A CD1   1 
ATOM   330  C CD2   . LEU A 1 53  ? -7.552  -13.538 -15.448 1.00 45.51  ? 41  LEU A CD2   1 
ATOM   331  N N     . GLU A 1 54  ? -9.116  -18.518 -17.462 1.00 48.59  ? 42  GLU A N     1 
ATOM   332  C CA    . GLU A 1 54  ? -10.129 -18.864 -18.459 1.00 54.14  ? 42  GLU A CA    1 
ATOM   333  C C     . GLU A 1 54  ? -11.305 -19.623 -17.854 1.00 63.21  ? 42  GLU A C     1 
ATOM   334  O O     . GLU A 1 54  ? -12.438 -19.502 -18.342 1.00 62.06  ? 42  GLU A O     1 
ATOM   335  C CB    . GLU A 1 54  ? -9.505  -19.698 -19.578 1.00 60.25  ? 42  GLU A CB    1 
ATOM   336  C CG    . GLU A 1 54  ? -8.404  -18.989 -20.347 1.00 66.14  ? 42  GLU A CG    1 
ATOM   337  C CD    . GLU A 1 54  ? -7.017  -19.313 -19.824 1.00 65.11  ? 42  GLU A CD    1 
ATOM   338  O OE1   . GLU A 1 54  ? -6.854  -19.485 -18.591 1.00 47.13  ? 42  GLU A OE1   1 
ATOM   339  O OE2   . GLU A 1 54  ? -6.088  -19.397 -20.657 1.00 73.77  ? 42  GLU A OE2   1 
ATOM   340  N N     . ASP A 1 55  ? -11.062 -20.427 -16.817 1.00 62.55  ? 43  ASP A N     1 
ATOM   341  C CA    . ASP A 1 55  ? -12.109 -21.226 -16.187 1.00 63.31  ? 43  ASP A CA    1 
ATOM   342  C C     . ASP A 1 55  ? -12.477 -20.727 -14.794 1.00 58.11  ? 43  ASP A C     1 
ATOM   343  O O     . ASP A 1 55  ? -13.252 -21.386 -14.095 1.00 60.16  ? 43  ASP A O     1 
ATOM   344  C CB    . ASP A 1 55  ? -11.703 -22.699 -16.130 1.00 66.88  ? 43  ASP A CB    1 
ATOM   345  C CG    . ASP A 1 55  ? -11.529 -23.309 -17.505 1.00 78.64  ? 43  ASP A CG    1 
ATOM   346  O OD1   . ASP A 1 55  ? -12.206 -22.851 -18.453 1.00 87.12  ? 43  ASP A OD1   1 
ATOM   347  O OD2   . ASP A 1 55  ? -10.719 -24.250 -17.638 1.00 84.82  ? 43  ASP A OD2   1 
ATOM   348  N N     . TYR A 1 56  ? -11.944 -19.579 -14.383 1.00 52.83  ? 44  TYR A N     1 
ATOM   349  C CA    . TYR A 1 56  ? -12.203 -19.044 -13.050 1.00 52.31  ? 44  TYR A CA    1 
ATOM   350  C C     . TYR A 1 56  ? -13.694 -18.803 -12.843 1.00 52.54  ? 44  TYR A C     1 
ATOM   351  O O     . TYR A 1 56  ? -14.348 -18.141 -13.656 1.00 46.42  ? 44  TYR A O     1 
ATOM   352  C CB    . TYR A 1 56  ? -11.457 -17.729 -12.891 1.00 46.49  ? 44  TYR A CB    1 
ATOM   353  C CG    . TYR A 1 56  ? -11.451 -17.188 -11.486 1.00 49.91  ? 44  TYR A CG    1 
ATOM   354  C CD1   . TYR A 1 56  ? -10.914 -17.934 -10.440 1.00 59.76  ? 44  TYR A CD1   1 
ATOM   355  C CD2   . TYR A 1 56  ? -11.948 -15.924 -11.207 1.00 40.92  ? 44  TYR A CD2   1 
ATOM   356  C CE1   . TYR A 1 56  ? -10.878 -17.437 -9.150  1.00 60.23  ? 44  TYR A CE1   1 
ATOM   357  C CE2   . TYR A 1 56  ? -11.918 -15.404 -9.912  1.00 40.16  ? 44  TYR A CE2   1 
ATOM   358  C CZ    . TYR A 1 56  ? -11.380 -16.177 -8.886  1.00 54.18  ? 44  TYR A CZ    1 
ATOM   359  O OH    . TYR A 1 56  ? -11.321 -15.706 -7.595  1.00 45.39  ? 44  TYR A OH    1 
ATOM   360  N N     . ASP A 1 57  ? -14.230 -19.328 -11.739 1.00 48.08  ? 45  ASP A N     1 
ATOM   361  C CA    . ASP A 1 57  ? -15.649 -19.213 -11.425 1.00 47.40  ? 45  ASP A CA    1 
ATOM   362  C C     . ASP A 1 57  ? -15.973 -18.094 -10.431 1.00 49.06  ? 45  ASP A C     1 
ATOM   363  O O     . ASP A 1 57  ? -16.975 -18.177 -9.714  1.00 66.04  ? 45  ASP A O     1 
ATOM   364  C CB    . ASP A 1 57  ? -16.170 -20.548 -10.903 1.00 58.61  ? 45  ASP A CB    1 
ATOM   365  C CG    . ASP A 1 57  ? -16.394 -21.569 -12.015 1.00 79.68  ? 45  ASP A CG    1 
ATOM   366  O OD1   . ASP A 1 57  ? -16.586 -21.162 -13.185 1.00 78.07  ? 45  ASP A OD1   1 
ATOM   367  O OD2   . ASP A 1 57  ? -16.388 -22.785 -11.715 1.00 88.62  ? 45  ASP A OD2   1 
ATOM   368  N N     . GLY A 1 58  ? -15.174 -17.040 -10.393 1.00 50.22  ? 46  GLY A N     1 
ATOM   369  C CA    . GLY A 1 58  ? -15.454 -15.855 -9.594  1.00 44.69  ? 46  GLY A CA    1 
ATOM   370  C C     . GLY A 1 58  ? -15.447 -14.600 -10.457 1.00 38.66  ? 46  GLY A C     1 
ATOM   371  O O     . GLY A 1 58  ? -15.628 -14.695 -11.675 1.00 40.66  ? 46  GLY A O     1 
ATOM   372  N N     . ASP A 1 59  ? -15.232 -13.433 -9.871  1.00 32.90  ? 47  ASP A N     1 
ATOM   373  C CA    . ASP A 1 59  ? -15.213 -12.224 -10.699 1.00 30.85  ? 47  ASP A CA    1 
ATOM   374  C C     . ASP A 1 59  ? -13.911 -12.268 -11.477 1.00 29.14  ? 47  ASP A C     1 
ATOM   375  O O     . ASP A 1 59  ? -12.863 -12.163 -10.853 1.00 26.53  ? 47  ASP A O     1 
ATOM   376  C CB    . ASP A 1 59  ? -15.201 -11.030 -9.735  1.00 31.13  ? 47  ASP A CB    1 
ATOM   377  C CG    . ASP A 1 59  ? -15.259 -9.668  -10.452 1.00 29.13  ? 47  ASP A CG    1 
ATOM   378  O OD1   . ASP A 1 59  ? -14.784 -9.559  -11.590 1.00 25.89  ? 47  ASP A OD1   1 
ATOM   379  O OD2   . ASP A 1 59  ? -15.825 -8.728  -9.850  1.00 29.00  ? 47  ASP A OD2   1 
ATOM   380  N N     . PRO A 1 60  ? -13.896 -12.398 -12.813 1.00 28.57  ? 48  PRO A N     1 
ATOM   381  C CA    . PRO A 1 60  ? -12.588 -12.588 -13.473 1.00 30.90  ? 48  PRO A CA    1 
ATOM   382  C C     . PRO A 1 60  ? -11.705 -11.356 -13.436 1.00 30.61  ? 48  PRO A C     1 
ATOM   383  O O     . PRO A 1 60  ? -10.502 -11.452 -13.717 1.00 31.69  ? 48  PRO A O     1 
ATOM   384  C CB    . PRO A 1 60  ? -12.958 -12.982 -14.905 1.00 34.46  ? 48  PRO A CB    1 
ATOM   385  C CG    . PRO A 1 60  ? -14.158 -12.228 -15.150 1.00 30.46  ? 48  PRO A CG    1 
ATOM   386  C CD    . PRO A 1 60  ? -14.969 -12.296 -13.818 1.00 34.06  ? 48  PRO A CD    1 
ATOM   387  N N     . ARG A 1 61  ? -12.254 -10.172 -13.122 1.00 23.82  ? 49  ARG A N     1 
ATOM   388  C CA    . ARG A 1 61  ? -11.442 -8.975  -12.957 1.00 24.06  ? 49  ARG A CA    1 
ATOM   389  C C     . ARG A 1 61  ? -11.051 -8.719  -11.516 1.00 30.12  ? 49  ARG A C     1 
ATOM   390  O O     . ARG A 1 61  ? -10.478 -7.662  -11.216 1.00 33.09  ? 49  ARG A O     1 
ATOM   391  C CB    . ARG A 1 61  ? -12.185 -7.759  -13.489 1.00 22.77  ? 49  ARG A CB    1 
ATOM   392  C CG    . ARG A 1 61  ? -12.439 -7.810  -14.979 1.00 24.06  ? 49  ARG A CG    1 
ATOM   393  C CD    . ARG A 1 61  ? -12.917 -6.466  -15.512 1.00 24.72  ? 49  ARG A CD    1 
ATOM   394  N NE    . ARG A 1 61  ? -14.083 -6.037  -14.743 1.00 25.74  ? 49  ARG A NE    1 
ATOM   395  C CZ    . ARG A 1 61  ? -14.148 -4.949  -13.980 1.00 27.43  ? 49  ARG A CZ    1 
ATOM   396  N NH1   . ARG A 1 61  ? -13.192 -4.026  -14.011 1.00 27.42  ? 49  ARG A NH1   1 
ATOM   397  N NH2   . ARG A 1 61  ? -15.219 -4.753  -13.211 1.00 26.40  ? 49  ARG A NH2   1 
ATOM   398  N N     . ASP A 1 62  ? -11.312 -9.654  -10.628 1.00 26.83  ? 50  ASP A N     1 
ATOM   399  C CA    . ASP A 1 62  ? -10.762 -9.570  -9.278  1.00 27.11  ? 50  ASP A CA    1 
ATOM   400  C C     . ASP A 1 62  ? -10.532 -10.976 -8.717  1.00 26.29  ? 50  ASP A C     1 
ATOM   401  O O     . ASP A 1 62  ? -11.091 -11.375 -7.683  1.00 29.02  ? 50  ASP A O     1 
ATOM   402  C CB    . ASP A 1 62  ? -11.699 -8.757  -8.396  1.00 30.66  ? 50  ASP A CB    1 
ATOM   403  C CG    . ASP A 1 62  ? -11.074 -8.346  -7.090  1.00 31.23  ? 50  ASP A CG    1 
ATOM   404  O OD1   . ASP A 1 62  ? -9.847  -8.426  -6.946  1.00 28.57  ? 50  ASP A OD1   1 
ATOM   405  O OD2   . ASP A 1 62  ? -11.809 -7.921  -6.191  1.00 35.02  ? 50  ASP A OD2   1 
ATOM   406  N N     . PRO A 1 63  ? -9.652  -11.746 -9.348  1.00 28.46  ? 51  PRO A N     1 
ATOM   407  C CA    . PRO A 1 63  ? -9.415  -13.124 -8.907  1.00 31.11  ? 51  PRO A CA    1 
ATOM   408  C C     . PRO A 1 63  ? -8.501  -13.227 -7.687  1.00 29.08  ? 51  PRO A C     1 
ATOM   409  O O     . PRO A 1 63  ? -7.668  -12.354 -7.430  1.00 27.91  ? 51  PRO A O     1 
ATOM   410  C CB    . PRO A 1 63  ? -8.728  -13.751 -10.130 1.00 33.07  ? 51  PRO A CB    1 
ATOM   411  C CG    . PRO A 1 63  ? -7.965  -12.583 -10.760 1.00 30.18  ? 51  PRO A CG    1 
ATOM   412  C CD    . PRO A 1 63  ? -8.872  -11.381 -10.547 1.00 27.56  ? 51  PRO A CD    1 
ATOM   413  N N     . ALA A 1 64  ? -8.611  -14.354 -6.986  1.00 29.72  ? 52  ALA A N     1 
ATOM   414  C CA    . ALA A 1 64  ? -7.622  -14.749 -5.992  1.00 28.25  ? 52  ALA A CA    1 
ATOM   415  C C     . ALA A 1 64  ? -6.323  -15.135 -6.701  1.00 27.55  ? 52  ALA A C     1 
ATOM   416  O O     . ALA A 1 64  ? -6.288  -15.330 -7.912  1.00 29.49  ? 52  ALA A O     1 
ATOM   417  C CB    . ALA A 1 64  ? -8.114  -15.967 -5.203  1.00 33.23  ? 52  ALA A CB    1 
ATOM   418  N N     . LEU A 1 65  ? -5.250  -15.284 -5.930  1.00 28.79  ? 53  LEU A N     1 
ATOM   419  C CA    . LEU A 1 65  ? -4.027  -15.837 -6.508  1.00 25.41  ? 53  LEU A CA    1 
ATOM   420  C C     . LEU A 1 65  ? -4.284  -17.264 -7.007  1.00 25.79  ? 53  LEU A C     1 
ATOM   421  O O     . LEU A 1 65  ? -5.100  -18.004 -6.458  1.00 29.11  ? 53  LEU A O     1 
ATOM   422  C CB    . LEU A 1 65  ? -2.939  -15.903 -5.436  1.00 25.67  ? 53  LEU A CB    1 
ATOM   423  C CG    . LEU A 1 65  ? -2.386  -14.514 -5.017  1.00 24.13  ? 53  LEU A CG    1 
ATOM   424  C CD1   . LEU A 1 65  ? -1.228  -14.670 -4.076  1.00 24.99  ? 53  LEU A CD1   1 
ATOM   425  C CD2   . LEU A 1 65  ? -1.976  -13.606 -6.177  1.00 26.33  ? 53  LEU A CD2   1 
ATOM   426  N N     . SER A 1 66  ? -3.568  -17.657 -8.059  1.00 28.58  ? 54  SER A N     1 
ATOM   427  C CA    . SER A 1 66  ? -3.557  -19.035 -8.512  1.00 28.96  ? 54  SER A CA    1 
ATOM   428  C C     . SER A 1 66  ? -2.640  -19.859 -7.620  1.00 34.31  ? 54  SER A C     1 
ATOM   429  O O     . SER A 1 66  ? -1.983  -19.327 -6.722  1.00 29.29  ? 54  SER A O     1 
ATOM   430  C CB    . SER A 1 66  ? -3.015  -19.107 -9.939  1.00 30.26  ? 54  SER A CB    1 
ATOM   431  O OG    . SER A 1 66  ? -1.644  -18.661 -9.972  1.00 27.15  ? 54  SER A OG    1 
ATOM   432  N N     . GLU A 1 67  ? -2.609  -21.179 -7.864  1.00 27.63  ? 55  GLU A N     1 
ATOM   433  C CA    . GLU A 1 67  ? -1.636  -22.028 -7.184  1.00 27.45  ? 55  GLU A CA    1 
ATOM   434  C C     . GLU A 1 67  ? -0.219  -21.525 -7.443  1.00 26.02  ? 55  GLU A C     1 
ATOM   435  O O     . GLU A 1 67  ? 0.613   -21.457 -6.518  1.00 27.08  ? 55  GLU A O     1 
ATOM   436  C CB    . GLU A 1 67  ? -1.804  -23.493 -7.610  1.00 29.36  ? 55  GLU A CB    1 
ATOM   437  C CG    . GLU A 1 67  ? -0.726  -24.442 -7.038  1.00 32.80  ? 55  GLU A CG    1 
ATOM   438  C CD    . GLU A 1 67  ? -1.008  -25.915 -7.315  1.00 57.37  ? 55  GLU A CD    1 
ATOM   439  O OE1   . GLU A 1 67  ? -1.809  -26.212 -8.233  1.00 51.32  ? 55  GLU A OE1   1 
ATOM   440  O OE2   . GLU A 1 67  ? -0.428  -26.775 -6.609  1.00 73.72  ? 55  GLU A OE2   1 
ATOM   441  N N     . LYS A 1 68  ? 0.080   -21.214 -8.702  1.00 25.58  ? 56  LYS A N     1 
ATOM   442  C CA    . LYS A 1 68  ? 1.379   -20.614 -9.026  1.00 24.48  ? 56  LYS A CA    1 
ATOM   443  C C     . LYS A 1 68  ? 1.597   -19.346 -8.232  1.00 24.21  ? 56  LYS A C     1 
ATOM   444  O O     . LYS A 1 68  ? 2.692   -19.112 -7.692  1.00 23.43  ? 56  LYS A O     1 
ATOM   445  C CB    . LYS A 1 68  ? 1.450   -20.342 -10.518 1.00 25.64  ? 56  LYS A CB    1 
ATOM   446  C CG    . LYS A 1 68  ? 2.788   -19.776 -10.986 1.00 34.01  ? 56  LYS A CG    1 
ATOM   447  C CD    . LYS A 1 68  ? 2.655   -19.310 -12.429 1.00 40.23  ? 56  LYS A CD    1 
ATOM   448  C CE    . LYS A 1 68  ? 3.999   -19.073 -13.079 1.00 53.48  ? 56  LYS A CE    1 
ATOM   449  N NZ    . LYS A 1 68  ? 3.817   -18.677 -14.503 1.00 61.61  ? 56  LYS A NZ    1 
ATOM   450  N N     . GLY A 1 69  ? 0.573   -18.481 -8.178  1.00 22.50  ? 57  GLY A N     1 
ATOM   451  C CA    . GLY A 1 69  ? 0.745   -17.223 -7.465  1.00 22.75  ? 57  GLY A CA    1 
ATOM   452  C C     . GLY A 1 69  ? 1.015   -17.424 -5.986  1.00 22.53  ? 57  GLY A C     1 
ATOM   453  O O     . GLY A 1 69  ? 1.810   -16.681 -5.398  1.00 22.20  ? 57  GLY A O     1 
ATOM   454  N N     . ARG A 1 70  ? 0.315   -18.376 -5.346  1.00 23.10  ? 58  ARG A N     1 
ATOM   455  C CA    . ARG A 1 70  ? 0.601   -18.617 -3.938  1.00 23.56  ? 58  ARG A CA    1 
ATOM   456  C C     . ARG A 1 70  ? 2.053   -19.023 -3.741  1.00 26.71  ? 58  ARG A C     1 
ATOM   457  O O     . ARG A 1 70  ? 2.676   -18.630 -2.747  1.00 23.33  ? 58  ARG A O     1 
ATOM   458  C CB    . ARG A 1 70  ? -0.357  -19.669 -3.377  1.00 26.02  ? 58  ARG A CB    1 
ATOM   459  C CG    . ARG A 1 70  ? -1.824  -19.196 -3.302  1.00 25.90  ? 58  ARG A CG    1 
ATOM   460  C CD    . ARG A 1 70  ? -2.612  -20.097 -2.314  1.00 28.16  ? 58  ARG A CD    1 
ATOM   461  N NE    . ARG A 1 70  ? -2.682  -21.485 -2.756  1.00 31.17  ? 58  ARG A NE    1 
ATOM   462  C CZ    . ARG A 1 70  ? -3.489  -21.938 -3.703  1.00 33.24  ? 58  ARG A CZ    1 
ATOM   463  N NH1   . ARG A 1 70  ? -4.387  -21.153 -4.280  1.00 31.56  ? 58  ARG A NH1   1 
ATOM   464  N NH2   . ARG A 1 70  ? -3.361  -23.197 -4.111  1.00 34.85  ? 58  ARG A NH2   1 
ATOM   465  N N     . ALA A 1 71  ? 2.596   -19.841 -4.662  1.00 23.15  ? 59  ALA A N     1 
ATOM   466  C CA    . ALA A 1 71  ? 3.992   -20.278 -4.551  1.00 23.34  ? 59  ALA A CA    1 
ATOM   467  C C     . ALA A 1 71  ? 4.922   -19.079 -4.727  1.00 22.57  ? 59  ALA A C     1 
ATOM   468  O O     . ALA A 1 71  ? 5.912   -18.941 -3.993  1.00 22.63  ? 59  ALA A O     1 
ATOM   469  C CB    . ALA A 1 71  ? 4.273   -21.310 -5.636  1.00 23.94  ? 59  ALA A CB    1 
ATOM   470  N N     . GLN A 1 72  ? 4.618   -18.197 -5.672  1.00 21.15  ? 60  GLN A N     1 
ATOM   471  C CA    . GLN A 1 72  ? 5.445   -17.003 -5.822  1.00 19.87  ? 60  GLN A CA    1 
ATOM   472  C C     . GLN A 1 72  ? 5.367   -16.114 -4.593  1.00 23.46  ? 60  GLN A C     1 
ATOM   473  O O     . GLN A 1 72  ? 6.376   -15.575 -4.143  1.00 21.31  ? 60  GLN A O     1 
ATOM   474  C CB    . GLN A 1 72  ? 5.011   -16.204 -7.042  1.00 21.26  ? 60  GLN A CB    1 
ATOM   475  C CG    . GLN A 1 72  ? 5.147   -16.947 -8.371  1.00 21.67  ? 60  GLN A CG    1 
ATOM   476  C CD    . GLN A 1 72  ? 4.494   -16.145 -9.509  1.00 21.64  ? 60  GLN A CD    1 
ATOM   477  O OE1   . GLN A 1 72  ? 3.541   -15.336 -9.301  1.00 21.05  ? 60  GLN A OE1   1 
ATOM   478  N NE2   . GLN A 1 72  ? 4.996   -16.321 -10.714 1.00 25.39  ? 60  GLN A NE2   1 
ATOM   479  N N     . ALA A 1 73  ? 4.173   -15.912 -4.062  1.00 22.19  ? 61  ALA A N     1 
ATOM   480  C CA    . ALA A 1 73  ? 4.044   -15.079 -2.875  1.00 23.06  ? 61  ALA A CA    1 
ATOM   481  C C     . ALA A 1 73  ? 4.828   -15.666 -1.699  1.00 24.15  ? 61  ALA A C     1 
ATOM   482  O O     . ALA A 1 73  ? 5.369   -14.919 -0.872  1.00 24.57  ? 61  ALA A O     1 
ATOM   483  C CB    . ALA A 1 73  ? 2.558   -14.966 -2.503  1.00 24.05  ? 61  ALA A CB    1 
ATOM   484  N N     . ARG A 1 74  ? 4.876   -16.993 -1.580  1.00 23.16  ? 62  ARG A N     1 
ATOM   485  C CA    . ARG A 1 74  ? 5.638   -17.602 -0.496  1.00 24.52  ? 62  ARG A CA    1 
ATOM   486  C C     . ARG A 1 74  ? 7.114   -17.271 -0.648  1.00 24.18  ? 62  ARG A C     1 
ATOM   487  O O     . ARG A 1 74  ? 7.792   -16.944 0.336   1.00 26.74  ? 62  ARG A O     1 
ATOM   488  C CB    . ARG A 1 74  ? 5.448   -19.111 -0.550  1.00 27.02  ? 62  ARG A CB    1 
ATOM   489  C CG    . ARG A 1 74  ? 4.107   -19.586 -0.005  1.00 36.70  ? 62  ARG A CG    1 
ATOM   490  C CD    . ARG A 1 74  ? 4.120   -21.079 0.336   1.00 42.16  ? 62  ARG A CD    1 
ATOM   491  N NE    . ARG A 1 74  ? 4.567   -21.943 -0.758  1.00 37.87  ? 62  ARG A NE    1 
ATOM   492  C CZ    . ARG A 1 74  ? 3.790   -22.434 -1.721  1.00 42.65  ? 62  ARG A CZ    1 
ATOM   493  N NH1   . ARG A 1 74  ? 2.499   -22.108 -1.824  1.00 29.49  ? 62  ARG A NH1   1 
ATOM   494  N NH2   . ARG A 1 74  ? 4.323   -23.260 -2.614  1.00 41.43  ? 62  ARG A NH2   1 
ATOM   495  N N     . LEU A 1 75  ? 7.629   -17.396 -1.869  1.00 22.61  ? 63  LEU A N     1 
ATOM   496  C CA    . LEU A 1 75  ? 9.043   -17.117 -2.085  1.00 23.08  ? 63  LEU A CA    1 
ATOM   497  C C     . LEU A 1 75  ? 9.339   -15.651 -1.825  1.00 23.33  ? 63  LEU A C     1 
ATOM   498  O O     . LEU A 1 75  ? 10.374  -15.311 -1.261  1.00 23.40  ? 63  LEU A O     1 
ATOM   499  C CB    . LEU A 1 75  ? 9.436   -17.503 -3.508  1.00 22.57  ? 63  LEU A CB    1 
ATOM   500  C CG    . LEU A 1 75  ? 9.502   -19.011 -3.742  1.00 22.18  ? 63  LEU A CG    1 
ATOM   501  C CD1   . LEU A 1 75  ? 9.589   -19.306 -5.219  1.00 26.55  ? 63  LEU A CD1   1 
ATOM   502  C CD2   . LEU A 1 75  ? 10.689  -19.622 -2.949  1.00 28.39  ? 63  LEU A CD2   1 
ATOM   503  N N     . LEU A 1 76  ? 8.438   -14.760 -2.237  1.00 19.68  ? 64  LEU A N     1 
ATOM   504  C CA    . LEU A 1 76  ? 8.614   -13.334 -1.966  1.00 19.96  ? 64  LEU A CA    1 
ATOM   505  C C     . LEU A 1 76  ? 8.572   -13.047 -0.476  1.00 24.46  ? 64  LEU A C     1 
ATOM   506  O O     . LEU A 1 76  ? 9.399   -12.283 0.044   1.00 21.96  ? 64  LEU A O     1 
ATOM   507  C CB    . LEU A 1 76  ? 7.473   -12.568 -2.632  1.00 20.71  ? 64  LEU A CB    1 
ATOM   508  C CG    . LEU A 1 76  ? 7.394   -11.076 -2.293  1.00 20.36  ? 64  LEU A CG    1 
ATOM   509  C CD1   . LEU A 1 76  ? 8.558   -10.331 -2.896  1.00 25.10  ? 64  LEU A CD1   1 
ATOM   510  C CD2   . LEU A 1 76  ? 6.092   -10.475 -2.780  1.00 23.13  ? 64  LEU A CD2   1 
ATOM   511  N N     . ALA A 1 77  ? 7.616   -13.651 0.231   1.00 22.89  ? 65  ALA A N     1 
ATOM   512  C CA    . ALA A 1 77  ? 7.491   -13.403 1.662   1.00 23.89  ? 65  ALA A CA    1 
ATOM   513  C C     . ALA A 1 77  ? 8.738   -13.852 2.389   1.00 25.44  ? 65  ALA A C     1 
ATOM   514  O O     . ALA A 1 77  ? 9.170   -13.211 3.358   1.00 27.48  ? 65  ALA A O     1 
ATOM   515  C CB    . ALA A 1 77  ? 6.274   -14.144 2.235   1.00 27.72  ? 65  ALA A CB    1 
ATOM   516  N N     . ALA A 1 78  ? 9.290   -15.005 1.989   1.00 22.88  ? 66  ALA A N     1 
ATOM   517  C CA    . ALA A 1 78  ? 10.530  -15.484 2.603   1.00 25.33  ? 66  ALA A CA    1 
ATOM   518  C C     . ALA A 1 78  ? 11.698  -14.541 2.298   1.00 24.35  ? 66  ALA A C     1 
ATOM   519  O O     . ALA A 1 78  ? 12.517  -14.255 3.176   1.00 27.31  ? 66  ALA A O     1 
ATOM   520  C CB    . ALA A 1 78  ? 10.838  -16.900 2.136   1.00 25.01  ? 66  ALA A CB    1 
ATOM   521  N N     . ARG A 1 79  ? 11.777  -14.054 1.064   1.00 23.52  ? 67  ARG A N     1 
ATOM   522  C CA    . ARG A 1 79  ? 12.809  -13.081 0.718   1.00 23.72  ? 67  ARG A CA    1 
ATOM   523  C C     . ARG A 1 79  ? 12.730  -11.843 1.612   1.00 26.30  ? 67  ARG A C     1 
ATOM   524  O O     . ARG A 1 79  ? 13.767  -11.340 2.065   1.00 26.54  ? 67  ARG A O     1 
ATOM   525  C CB    . ARG A 1 79  ? 12.675  -12.684 -0.748  1.00 23.06  ? 67  ARG A CB    1 
ATOM   526  C CG    . ARG A 1 79  ? 13.552  -11.483 -1.121  1.00 22.35  ? 67  ARG A CG    1 
ATOM   527  C CD    . ARG A 1 79  ? 13.315  -11.052 -2.542  1.00 21.06  ? 67  ARG A CD    1 
ATOM   528  N NE    . ARG A 1 79  ? 14.044  -9.820  -2.850  1.00 21.73  ? 67  ARG A NE    1 
ATOM   529  C CZ    . ARG A 1 79  ? 14.137  -9.302  -4.066  1.00 23.15  ? 67  ARG A CZ    1 
ATOM   530  N NH1   . ARG A 1 79  ? 13.499  -9.824  -5.099  1.00 21.09  ? 67  ARG A NH1   1 
ATOM   531  N NH2   . ARG A 1 79  ? 14.867  -8.194  -4.247  1.00 23.58  ? 67  ARG A NH2   1 
ATOM   532  N N     . LEU A 1 80  ? 11.519  -11.335 1.865   1.00 23.85  ? 68  LEU A N     1 
ATOM   533  C CA    . LEU A 1 80  ? 11.363  -10.104 2.620   1.00 27.53  ? 68  LEU A CA    1 
ATOM   534  C C     . LEU A 1 80  ? 11.276  -10.328 4.126   1.00 25.55  ? 68  LEU A C     1 
ATOM   535  O O     . LEU A 1 80  ? 11.269  -9.349  4.884   1.00 27.32  ? 68  LEU A O     1 
ATOM   536  C CB    . LEU A 1 80  ? 10.152  -9.311  2.126   1.00 26.78  ? 68  LEU A CB    1 
ATOM   537  C CG    . LEU A 1 80  ? 10.188  -8.882  0.660   1.00 28.41  ? 68  LEU A CG    1 
ATOM   538  C CD1   . LEU A 1 80  ? 9.053   -7.882  0.413   1.00 30.30  ? 68  LEU A CD1   1 
ATOM   539  C CD2   . LEU A 1 80  ? 11.509  -8.341  0.277   1.00 31.53  ? 68  LEU A CD2   1 
ATOM   540  N N     . ALA A 1 81  ? 11.275  -11.572 4.589   1.00 27.41  ? 69  ALA A N     1 
ATOM   541  C CA    . ALA A 1 81  ? 11.115  -11.791 6.017   1.00 25.53  ? 69  ALA A CA    1 
ATOM   542  C C     . ALA A 1 81  ? 12.262  -11.194 6.814   1.00 26.27  ? 69  ALA A C     1 
ATOM   543  O O     . ALA A 1 81  ? 12.058  -10.723 7.943   1.00 31.39  ? 69  ALA A O     1 
ATOM   544  C CB    . ALA A 1 81  ? 11.002  -13.287 6.286   1.00 28.07  ? 69  ALA A CB    1 
ATOM   545  N N     . GLY A 1 82  ? 13.469  -11.214 6.251   1.00 29.23  ? 70  GLY A N     1 
ATOM   546  C CA    . GLY A 1 82  ? 14.649  -10.706 6.924   1.00 31.72  ? 70  GLY A CA    1 
ATOM   547  C C     . GLY A 1 82  ? 14.949  -9.245  6.683   1.00 29.87  ? 70  GLY A C     1 
ATOM   548  O O     . GLY A 1 82  ? 15.899  -8.703  7.268   1.00 32.90  ? 70  GLY A O     1 
ATOM   549  N N     . VAL A 1 83  ? 14.144  -8.583  5.875   1.00 25.62  ? 71  VAL A N     1 
ATOM   550  C CA    . VAL A 1 83  ? 14.305  -7.176  5.519   1.00 25.33  ? 71  VAL A CA    1 
ATOM   551  C C     . VAL A 1 83  ? 13.561  -6.336  6.552   1.00 28.57  ? 71  VAL A C     1 
ATOM   552  O O     . VAL A 1 83  ? 12.385  -6.610  6.821   1.00 30.42  ? 71  VAL A O     1 
ATOM   553  C CB    . VAL A 1 83  ? 13.736  -6.910  4.113   1.00 25.53  ? 71  VAL A CB    1 
ATOM   554  C CG1   . VAL A 1 83  ? 13.756  -5.410  3.791   1.00 28.09  ? 71  VAL A CG1   1 
ATOM   555  C CG2   . VAL A 1 83  ? 14.512  -7.722  3.041   1.00 27.16  ? 71  VAL A CG2   1 
ATOM   556  N N     . PRO A 1 84  ? 14.166  -5.296  7.121   1.00 29.09  ? 72  PRO A N     1 
ATOM   557  C CA    . PRO A 1 84  ? 13.398  -4.412  8.015   1.00 28.55  ? 72  PRO A CA    1 
ATOM   558  C C     . PRO A 1 84  ? 12.268  -3.770  7.236   1.00 28.71  ? 72  PRO A C     1 
ATOM   559  O O     . PRO A 1 84  ? 12.485  -3.143  6.195   1.00 26.96  ? 72  PRO A O     1 
ATOM   560  C CB    . PRO A 1 84  ? 14.431  -3.374  8.450   1.00 27.71  ? 72  PRO A CB    1 
ATOM   561  C CG    . PRO A 1 84  ? 15.778  -4.137  8.333   1.00 29.10  ? 72  PRO A CG    1 
ATOM   562  C CD    . PRO A 1 84  ? 15.588  -4.912  7.054   1.00 28.50  ? 72  PRO A CD    1 
ATOM   563  N N     . LEU A 1 85  ? 11.034  -3.959  7.738   1.00 26.21  ? 73  LEU A N     1 
ATOM   564  C CA    . LEU A 1 85  ? 9.819   -3.516  7.071   1.00 25.99  ? 73  LEU A CA    1 
ATOM   565  C C     . LEU A 1 85  ? 8.937   -2.876  8.123   1.00 25.78  ? 73  LEU A C     1 
ATOM   566  O O     . LEU A 1 85  ? 8.698   -3.461  9.185   1.00 26.67  ? 73  LEU A O     1 
ATOM   567  C CB    . LEU A 1 85  ? 9.065   -4.714  6.491   1.00 35.14  ? 73  LEU A CB    1 
ATOM   568  C CG    . LEU A 1 85  ? 9.340   -5.057  5.040   1.00 40.42  ? 73  LEU A CG    1 
ATOM   569  C CD1   . LEU A 1 85  ? 8.116   -5.807  4.501   1.00 35.06  ? 73  LEU A CD1   1 
ATOM   570  C CD2   . LEU A 1 85  ? 9.643   -3.790  4.251   1.00 38.64  ? 73  LEU A CD2   1 
ATOM   571  N N     . HIS A 1 86  ? 8.440   -1.675  7.811   1.00 25.90  ? 74  HIS A N     1 
ATOM   572  C CA    . HIS A 1 86  ? 7.721   -0.877  8.782   1.00 27.66  ? 74  HIS A CA    1 
ATOM   573  C C     . HIS A 1 86  ? 6.271   -0.633  8.419   1.00 26.87  ? 74  HIS A C     1 
ATOM   574  O O     . HIS A 1 86  ? 5.502   -0.186  9.283   1.00 30.29  ? 74  HIS A O     1 
ATOM   575  C CB    . HIS A 1 86  ? 8.502   0.419   9.051   1.00 28.56  ? 74  HIS A CB    1 
ATOM   576  C CG    . HIS A 1 86  ? 9.940   0.135   9.355   1.00 31.69  ? 74  HIS A CG    1 
ATOM   577  N ND1   . HIS A 1 86  ? 10.943  0.268   8.413   1.00 31.35  ? 74  HIS A ND1   1 
ATOM   578  C CD2   . HIS A 1 86  ? 10.512  -0.444  10.431  1.00 32.04  ? 74  HIS A CD2   1 
ATOM   579  C CE1   . HIS A 1 86  ? 12.083  -0.154  8.929   1.00 30.97  ? 74  HIS A CE1   1 
ATOM   580  N NE2   . HIS A 1 86  ? 11.852  -0.595  10.153  1.00 30.98  ? 74  HIS A NE2   1 
ATOM   581  N N     . GLY A 1 87  ? 5.866   -0.956  7.201   1.00 25.36  ? 75  GLY A N     1 
ATOM   582  C CA    . GLY A 1 87  ? 4.459   -0.950  6.833   1.00 25.00  ? 75  GLY A CA    1 
ATOM   583  C C     . GLY A 1 87  ? 4.269   -1.682  5.527   1.00 23.39  ? 75  GLY A C     1 
ATOM   584  O O     . GLY A 1 87  ? 5.226   -1.870  4.755   1.00 24.75  ? 75  GLY A O     1 
ATOM   585  N N     . VAL A 1 88  ? 3.018   -2.095  5.278   1.00 23.15  ? 76  VAL A N     1 
ATOM   586  C CA    . VAL A 1 88  ? 2.672   -2.798  4.049   1.00 22.53  ? 76  VAL A CA    1 
ATOM   587  C C     . VAL A 1 88  ? 1.351   -2.219  3.554   1.00 23.28  ? 76  VAL A C     1 
ATOM   588  O O     . VAL A 1 88  ? 0.353   -2.223  4.288   1.00 26.51  ? 76  VAL A O     1 
ATOM   589  C CB    . VAL A 1 88  ? 2.530   -4.319  4.253   1.00 21.74  ? 76  VAL A CB    1 
ATOM   590  C CG1   . VAL A 1 88  ? 2.117   -4.976  2.942   1.00 24.69  ? 76  VAL A CG1   1 
ATOM   591  C CG2   . VAL A 1 88  ? 3.820   -4.965  4.750   1.00 25.33  ? 76  VAL A CG2   1 
ATOM   592  N N     . TRP A 1 89  ? 1.335   -1.734  2.319   1.00 21.02  ? 77  TRP A N     1 
ATOM   593  C CA    . TRP A 1 89  ? 0.174   -1.176  1.658   1.00 22.43  ? 77  TRP A CA    1 
ATOM   594  C C     . TRP A 1 89  ? -0.098  -1.970  0.397   1.00 22.53  ? 77  TRP A C     1 
ATOM   595  O O     . TRP A 1 89  ? 0.802   -2.627  -0.160  1.00 23.44  ? 77  TRP A O     1 
ATOM   596  C CB    . TRP A 1 89  ? 0.464   0.280   1.279   1.00 23.22  ? 77  TRP A CB    1 
ATOM   597  C CG    . TRP A 1 89  ? 0.464   1.184   2.495   1.00 29.05  ? 77  TRP A CG    1 
ATOM   598  C CD1   . TRP A 1 89  ? 1.441   1.250   3.465   1.00 32.29  ? 77  TRP A CD1   1 
ATOM   599  C CD2   . TRP A 1 89  ? -0.548  2.109   2.891   1.00 42.11  ? 77  TRP A CD2   1 
ATOM   600  N NE1   . TRP A 1 89  ? 1.100   2.175   4.415   1.00 38.59  ? 77  TRP A NE1   1 
ATOM   601  C CE2   . TRP A 1 89  ? -0.124  2.705   4.103   1.00 32.67  ? 77  TRP A CE2   1 
ATOM   602  C CE3   . TRP A 1 89  ? -1.778  2.483   2.353   1.00 37.58  ? 77  TRP A CE3   1 
ATOM   603  C CZ2   . TRP A 1 89  ? -0.880  3.662   4.773   1.00 45.49  ? 77  TRP A CZ2   1 
ATOM   604  C CZ3   . TRP A 1 89  ? -2.537  3.430   3.025   1.00 45.96  ? 77  TRP A CZ3   1 
ATOM   605  C CH2   . TRP A 1 89  ? -2.083  4.011   4.222   1.00 46.71  ? 77  TRP A CH2   1 
ATOM   606  N N     . ALA A 1 90  ? -1.350  -1.946  -0.048  1.00 23.07  ? 78  ALA A N     1 
ATOM   607  C CA    . ALA A 1 90  ? -1.761  -2.684  -1.236  1.00 22.85  ? 78  ALA A CA    1 
ATOM   608  C C     . ALA A 1 90  ? -2.955  -1.972  -1.865  1.00 21.07  ? 78  ALA A C     1 
ATOM   609  O O     . ALA A 1 90  ? -3.740  -1.309  -1.180  1.00 23.45  ? 78  ALA A O     1 
ATOM   610  C CB    . ALA A 1 90  ? -2.140  -4.140  -0.899  1.00 22.85  ? 78  ALA A CB    1 
ATOM   611  N N     . SER A 1 91  ? -3.086  -2.129  -3.181  1.00 20.92  ? 79  SER A N     1 
ATOM   612  C CA    . SER A 1 91  ? -4.385  -1.840  -3.775  1.00 24.08  ? 79  SER A CA    1 
ATOM   613  C C     . SER A 1 91  ? -5.455  -2.759  -3.164  1.00 27.40  ? 79  SER A C     1 
ATOM   614  O O     . SER A 1 91  ? -5.172  -3.723  -2.449  1.00 26.38  ? 79  SER A O     1 
ATOM   615  C CB    . SER A 1 91  ? -4.340  -2.055  -5.283  1.00 26.45  ? 79  SER A CB    1 
ATOM   616  O OG    . SER A 1 91  ? -4.667  -3.397  -5.594  1.00 24.96  ? 79  SER A OG    1 
ATOM   617  N N     . GLY A 1 92  ? -6.717  -2.418  -3.435  1.00 25.68  ? 80  GLY A N     1 
ATOM   618  C CA    . GLY A 1 92  ? -7.804  -3.254  -2.977  1.00 26.44  ? 80  GLY A CA    1 
ATOM   619  C C     . GLY A 1 92  ? -8.056  -4.555  -3.718  1.00 24.83  ? 80  GLY A C     1 
ATOM   620  O O     . GLY A 1 92  ? -8.867  -5.363  -3.253  1.00 27.46  ? 80  GLY A O     1 
ATOM   621  N N     . ALA A 1 93  ? -7.359  -4.825  -4.817  1.00 23.04  ? 81  ALA A N     1 
ATOM   622  C CA    . ALA A 1 93  ? -7.612  -6.060  -5.550  1.00 27.53  ? 81  ALA A CA    1 
ATOM   623  C C     . ALA A 1 93  ? -7.203  -7.262  -4.711  1.00 24.70  ? 81  ALA A C     1 
ATOM   624  O O     . ALA A 1 93  ? -6.169  -7.238  -4.044  1.00 24.98  ? 81  ALA A O     1 
ATOM   625  C CB    . ALA A 1 93  ? -6.802  -6.068  -6.838  1.00 24.81  ? 81  ALA A CB    1 
ATOM   626  N N     . HIS A 1 94  ? -7.976  -8.345  -4.811  1.00 25.75  ? 82  HIS A N     1 
ATOM   627  C CA    . HIS A 1 94  ? -7.668  -9.556  -4.051  1.00 26.34  ? 82  HIS A CA    1 
ATOM   628  C C     . HIS A 1 94  ? -6.245  -10.036 -4.292  1.00 25.09  ? 82  HIS A C     1 
ATOM   629  O O     . HIS A 1 94  ? -5.547  -10.423 -3.337  1.00 25.70  ? 82  HIS A O     1 
ATOM   630  C CB    . HIS A 1 94  ? -8.671  -10.660 -4.383  1.00 28.57  ? 82  HIS A CB    1 
ATOM   631  C CG    . HIS A 1 94  ? -10.040 -10.387 -3.844  1.00 36.83  ? 82  HIS A CG    1 
ATOM   632  N ND1   . HIS A 1 94  ? -10.263 -10.047 -2.524  1.00 35.41  ? 82  HIS A ND1   1 
ATOM   633  C CD2   . HIS A 1 94  ? -11.255 -10.385 -4.445  1.00 43.45  ? 82  HIS A CD2   1 
ATOM   634  C CE1   . HIS A 1 94  ? -11.557 -9.845  -2.336  1.00 44.50  ? 82  HIS A CE1   1 
ATOM   635  N NE2   . HIS A 1 94  ? -12.182 -10.049 -3.484  1.00 40.72  ? 82  HIS A NE2   1 
ATOM   636  N N     . ARG A 1 95  ? -5.799  -10.026 -5.548  1.00 22.31  ? 83  ARG A N     1 
ATOM   637  C CA    . ARG A 1 95  ? -4.468  -10.533 -5.849  1.00 22.33  ? 83  ARG A CA    1 
ATOM   638  C C     . ARG A 1 95  ? -3.391  -9.705  -5.161  1.00 23.25  ? 83  ARG A C     1 
ATOM   639  O O     . ARG A 1 95  ? -2.354  -10.248 -4.738  1.00 23.14  ? 83  ARG A O     1 
ATOM   640  C CB    . ARG A 1 95  ? -4.241  -10.582 -7.355  1.00 23.50  ? 83  ARG A CB    1 
ATOM   641  C CG    . ARG A 1 95  ? -4.400  -9.228  -8.108  1.00 24.24  ? 83  ARG A CG    1 
ATOM   642  C CD    . ARG A 1 95  ? -4.607  -9.523  -9.609  1.00 27.91  ? 83  ARG A CD    1 
ATOM   643  N NE    . ARG A 1 95  ? -4.758  -8.333  -10.442 1.00 29.84  ? 83  ARG A NE    1 
ATOM   644  C CZ    . ARG A 1 95  ? -5.865  -7.599  -10.564 1.00 29.62  ? 83  ARG A CZ    1 
ATOM   645  N NH1   . ARG A 1 95  ? -6.957  -7.856  -9.864  1.00 29.80  ? 83  ARG A NH1   1 
ATOM   646  N NH2   . ARG A 1 95  ? -5.876  -6.585  -11.433 1.00 34.55  ? 83  ARG A NH2   1 
ATOM   647  N N     . ALA A 1 96  ? -3.599  -8.393  -5.056  1.00 23.89  ? 84  ALA A N     1 
ATOM   648  C CA    . ALA A 1 96  ? -2.626  -7.564  -4.353  1.00 19.24  ? 84  ALA A CA    1 
ATOM   649  C C     . ALA A 1 96  ? -2.744  -7.741  -2.854  1.00 22.28  ? 84  ALA A C     1 
ATOM   650  O O     . ALA A 1 96  ? -1.730  -7.876  -2.166  1.00 23.94  ? 84  ALA A O     1 
ATOM   651  C CB    . ALA A 1 96  ? -2.801  -6.109  -4.717  1.00 22.43  ? 84  ALA A CB    1 
ATOM   652  N N     . GLN A 1 97  ? -3.977  -7.778  -2.331  1.00 21.11  ? 85  GLN A N     1 
ATOM   653  C CA    . GLN A 1 97  ? -4.168  -7.994  -0.906  1.00 24.01  ? 85  GLN A CA    1 
ATOM   654  C C     . GLN A 1 97  ? -3.498  -9.289  -0.472  1.00 24.69  ? 85  GLN A C     1 
ATOM   655  O O     . GLN A 1 97  ? -2.848  -9.342  0.578   1.00 25.01  ? 85  GLN A O     1 
ATOM   656  C CB    . GLN A 1 97  ? -5.679  -8.008  -0.613  1.00 23.69  ? 85  GLN A CB    1 
ATOM   657  C CG    . GLN A 1 97  ? -6.329  -6.600  -0.763  1.00 25.38  ? 85  GLN A CG    1 
ATOM   658  C CD    . GLN A 1 97  ? -6.070  -5.719  0.474   1.00 27.03  ? 85  GLN A CD    1 
ATOM   659  O OE1   . GLN A 1 97  ? -6.272  -6.149  1.612   1.00 32.12  ? 85  GLN A OE1   1 
ATOM   660  N NE2   . GLN A 1 97  ? -5.652  -4.468  0.244   1.00 28.53  ? 85  GLN A NE2   1 
ATOM   661  N N     . GLN A 1 98  ? -3.726  -10.373 -1.235  1.00 24.41  ? 86  GLN A N     1 
ATOM   662  C CA    . GLN A 1 98  ? -3.208  -11.678 -0.858  1.00 22.60  ? 86  GLN A CA    1 
ATOM   663  C C     . GLN A 1 98  ? -1.683  -11.700 -0.906  1.00 22.47  ? 86  GLN A C     1 
ATOM   664  O O     . GLN A 1 98  ? -1.055  -12.297 -0.026  1.00 23.25  ? 86  GLN A O     1 
ATOM   665  C CB    . GLN A 1 98  ? -3.814  -12.724 -1.793  1.00 26.24  ? 86  GLN A CB    1 
ATOM   666  C CG    . GLN A 1 98  ? -3.666  -14.151 -1.342  1.00 29.28  ? 86  GLN A CG    1 
ATOM   667  C CD    . GLN A 1 98  ? -4.438  -15.115 -2.222  1.00 34.22  ? 86  GLN A CD    1 
ATOM   668  O OE1   . GLN A 1 98  ? -5.333  -14.706 -2.990  1.00 30.05  ? 86  GLN A OE1   1 
ATOM   669  N NE2   . GLN A 1 98  ? -4.103  -16.408 -2.112  1.00 32.03  ? 86  GLN A NE2   1 
ATOM   670  N N     . THR A 1 99  ? -1.085  -11.078 -1.925  1.00 21.95  ? 87  THR A N     1 
ATOM   671  C CA    . THR A 1 99  ? 0.376   -10.974 -1.964  1.00 22.17  ? 87  THR A CA    1 
ATOM   672  C C     . THR A 1 99  ? 0.890   -10.169 -0.777  1.00 21.12  ? 87  THR A C     1 
ATOM   673  O O     . THR A 1 99  ? 1.852   -10.580 -0.100  1.00 23.53  ? 87  THR A O     1 
ATOM   674  C CB    . THR A 1 99  ? 0.824   -10.342 -3.274  1.00 18.58  ? 87  THR A CB    1 
ATOM   675  O OG1   . THR A 1 99  ? 0.285   -11.118 -4.363  1.00 21.51  ? 87  THR A OG1   1 
ATOM   676  C CG2   . THR A 1 99  ? 2.324   -10.379 -3.345  1.00 20.68  ? 87  THR A CG2   1 
ATOM   677  N N     . ALA A 1 100 ? 0.231   -9.035  -0.490  1.00 24.05  ? 88  ALA A N     1 
ATOM   678  C CA    . ALA A 1 100 ? 0.643   -8.171  0.619   1.00 21.35  ? 88  ALA A CA    1 
ATOM   679  C C     . ALA A 1 100 ? 0.510   -8.891  1.957   1.00 21.92  ? 88  ALA A C     1 
ATOM   680  O O     . ALA A 1 100 ? 1.355   -8.713  2.842   1.00 24.51  ? 88  ALA A O     1 
ATOM   681  C CB    . ALA A 1 100 ? -0.201  -6.887  0.633   1.00 21.43  ? 88  ALA A CB    1 
ATOM   682  N N     A SER A 1 101 ? -0.566  -9.675  2.134   0.48 22.38  ? 89  SER A N     1 
ATOM   683  N N     B SER A 1 101 ? -0.571  -9.673  2.145   0.52 22.43  ? 89  SER A N     1 
ATOM   684  C CA    A SER A 1 101 ? -0.776  -10.410 3.383   0.48 26.90  ? 89  SER A CA    1 
ATOM   685  C CA    B SER A 1 101 ? -0.764  -10.400 3.405   0.52 26.90  ? 89  SER A CA    1 
ATOM   686  C C     A SER A 1 101 ? 0.341   -11.413 3.650   0.48 23.50  ? 89  SER A C     1 
ATOM   687  C C     B SER A 1 101 ? 0.345   -11.418 3.657   0.52 23.45  ? 89  SER A C     1 
ATOM   688  O O     A SER A 1 101 ? 0.738   -11.613 4.801   0.48 25.24  ? 89  SER A O     1 
ATOM   689  O O     B SER A 1 101 ? 0.745   -11.629 4.804   0.52 25.27  ? 89  SER A O     1 
ATOM   690  C CB    A SER A 1 101 ? -2.114  -11.143 3.324   0.48 25.62  ? 89  SER A CB    1 
ATOM   691  C CB    B SER A 1 101 ? -2.128  -11.096 3.424   0.52 25.63  ? 89  SER A CB    1 
ATOM   692  O OG    A SER A 1 101 ? -2.386  -11.773 4.554   0.48 27.67  ? 89  SER A OG    1 
ATOM   693  O OG    B SER A 1 101 ? -3.188  -10.157 3.573   0.52 26.64  ? 89  SER A OG    1 
ATOM   694  N N     . ALA A 1 102 ? 0.841   -12.062 2.597   1.00 24.67  ? 90  ALA A N     1 
ATOM   695  C CA    . ALA A 1 102 ? 1.939   -13.011 2.766   1.00 24.45  ? 90  ALA A CA    1 
ATOM   696  C C     . ALA A 1 102 ? 3.191   -12.270 3.236   1.00 23.05  ? 90  ALA A C     1 
ATOM   697  O O     . ALA A 1 102 ? 3.870   -12.714 4.176   1.00 26.62  ? 90  ALA A O     1 
ATOM   698  C CB    . ALA A 1 102 ? 2.174   -13.708 1.426   1.00 23.64  ? 90  ALA A CB    1 
ATOM   699  N N     . VAL A 1 103 ? 3.483   -11.112 2.628   1.00 23.71  ? 91  VAL A N     1 
ATOM   700  C CA    . VAL A 1 103 ? 4.631   -10.326 3.063   1.00 22.04  ? 91  VAL A CA    1 
ATOM   701  C C     . VAL A 1 103 ? 4.435   -9.852  4.493   1.00 23.24  ? 91  VAL A C     1 
ATOM   702  O O     . VAL A 1 103 ? 5.291   -10.042 5.367   1.00 25.83  ? 91  VAL A O     1 
ATOM   703  C CB    . VAL A 1 103 ? 4.835   -9.143  2.103   1.00 24.71  ? 91  VAL A CB    1 
ATOM   704  C CG1   . VAL A 1 103 ? 5.825   -8.167  2.673   1.00 24.25  ? 91  VAL A CG1   1 
ATOM   705  C CG2   . VAL A 1 103 ? 5.315   -9.648  0.716   1.00 22.57  ? 91  VAL A CG2   1 
ATOM   706  N N     . ALA A 1 104 ? 3.258   -9.298  4.777   1.00 22.88  ? 92  ALA A N     1 
ATOM   707  C CA    . ALA A 1 104 ? 3.038   -8.669  6.063   1.00 23.18  ? 92  ALA A CA    1 
ATOM   708  C C     . ALA A 1 104 ? 3.034   -9.671  7.205   1.00 25.37  ? 92  ALA A C     1 
ATOM   709  O O     . ALA A 1 104 ? 3.410   -9.329  8.336   1.00 25.14  ? 92  ALA A O     1 
ATOM   710  C CB    . ALA A 1 104 ? 1.710   -7.889  6.035   1.00 25.98  ? 92  ALA A CB    1 
ATOM   711  N N     . ALA A 1 105 ? 2.537   -10.895 6.957   1.00 28.03  ? 93  ALA A N     1 
ATOM   712  C CA    . ALA A 1 105 ? 2.424   -11.862 8.049   1.00 29.43  ? 93  ALA A CA    1 
ATOM   713  C C     . ALA A 1 105 ? 3.775   -12.179 8.674   1.00 25.80  ? 93  ALA A C     1 
ATOM   714  O O     . ALA A 1 105 ? 3.837   -12.405 9.890   1.00 30.49  ? 93  ALA A O     1 
ATOM   715  C CB    . ALA A 1 105 ? 1.710   -13.145 7.592   1.00 36.62  ? 93  ALA A CB    1 
ATOM   716  N N     . GLU A 1 106 ? 4.858   -12.110 7.880   1.00 26.63  ? 94  GLU A N     1 
ATOM   717  C CA    . GLU A 1 106 ? 6.200   -12.391 8.393   1.00 31.17  ? 94  GLU A CA    1 
ATOM   718  C C     . GLU A 1 106 ? 6.666   -11.339 9.379   1.00 31.89  ? 94  GLU A C     1 
ATOM   719  O O     . GLU A 1 106 ? 7.592   -11.594 10.157  1.00 35.89  ? 94  GLU A O     1 
ATOM   720  C CB    . GLU A 1 106 ? 7.229   -12.460 7.273   1.00 28.29  ? 94  GLU A CB    1 
ATOM   721  C CG    . GLU A 1 106 ? 6.972   -13.500 6.230   1.00 30.85  ? 94  GLU A CG    1 
ATOM   722  C CD    . GLU A 1 106 ? 6.972   -14.901 6.805   1.00 38.23  ? 94  GLU A CD    1 
ATOM   723  O OE1   . GLU A 1 106 ? 7.731   -15.168 7.776   1.00 43.01  ? 94  GLU A OE1   1 
ATOM   724  O OE2   . GLU A 1 106 ? 6.220   -15.748 6.273   1.00 45.26  ? 94  GLU A OE2   1 
ATOM   725  N N     . HIS A 1 107 ? 6.050   -10.172 9.352   1.00 26.74  ? 95  HIS A N     1 
ATOM   726  C CA    . HIS A 1 107 ? 6.444   -9.055  10.179  1.00 29.61  ? 95  HIS A CA    1 
ATOM   727  C C     . HIS A 1 107 ? 5.357   -8.649  11.154  1.00 28.17  ? 95  HIS A C     1 
ATOM   728  O O     . HIS A 1 107 ? 5.547   -7.651  11.870  1.00 30.56  ? 95  HIS A O     1 
ATOM   729  C CB    . HIS A 1 107 ? 6.756   -7.843  9.300   1.00 28.38  ? 95  HIS A CB    1 
ATOM   730  C CG    . HIS A 1 107 ? 7.867   -8.079  8.323   1.00 27.64  ? 95  HIS A CG    1 
ATOM   731  N ND1   . HIS A 1 107 ? 9.166   -7.703  8.586   1.00 30.63  ? 95  HIS A ND1   1 
ATOM   732  C CD2   . HIS A 1 107 ? 7.881   -8.669  7.103   1.00 26.30  ? 95  HIS A CD2   1 
ATOM   733  C CE1   . HIS A 1 107 ? 9.928   -8.035  7.557   1.00 28.88  ? 95  HIS A CE1   1 
ATOM   734  N NE2   . HIS A 1 107 ? 9.177   -8.613  6.639   1.00 27.67  ? 95  HIS A NE2   1 
ATOM   735  N N     . GLY A 1 108 ? 4.250   -9.409  11.257  1.00 28.25  ? 96  GLY A N     1 
ATOM   736  C CA    . GLY A 1 108 ? 3.178   -9.035  12.167  1.00 30.43  ? 96  GLY A CA    1 
ATOM   737  C C     . GLY A 1 108 ? 2.475   -7.734  11.829  1.00 29.34  ? 96  GLY A C     1 
ATOM   738  O O     . GLY A 1 108 ? 1.927   -7.097  12.749  1.00 30.75  ? 96  GLY A O     1 
ATOM   739  N N     . LEU A 1 109 ? 2.503   -7.315  10.564  1.00 27.84  ? 97  LEU A N     1 
ATOM   740  C CA    . LEU A 1 109 ? 1.982   -6.026  10.133  1.00 27.64  ? 97  LEU A CA    1 
ATOM   741  C C     . LEU A 1 109 ? 0.590   -6.193  9.553   1.00 33.48  ? 97  LEU A C     1 
ATOM   742  O O     . LEU A 1 109 ? 0.274   -7.213  8.931   1.00 31.55  ? 97  LEU A O     1 
ATOM   743  C CB    . LEU A 1 109 ? 2.896   -5.430  9.051   1.00 26.58  ? 97  LEU A CB    1 
ATOM   744  C CG    . LEU A 1 109 ? 4.210   -4.902  9.633   1.00 28.38  ? 97  LEU A CG    1 
ATOM   745  C CD1   . LEU A 1 109 ? 5.194   -4.634  8.563   1.00 29.51  ? 97  LEU A CD1   1 
ATOM   746  C CD2   . LEU A 1 109 ? 3.922   -3.633  10.405  1.00 31.10  ? 97  LEU A CD2   1 
ATOM   747  N N     . ARG A 1 110 ? -0.225  -5.153  9.727   1.00 31.43  ? 98  ARG A N     1 
ATOM   748  C CA    . ARG A 1 110 ? -1.530  -5.051  9.103   1.00 31.34  ? 98  ARG A CA    1 
ATOM   749  C C     . ARG A 1 110 ? -1.369  -4.454  7.706   1.00 36.15  ? 98  ARG A C     1 
ATOM   750  O O     . ARG A 1 110 ? -0.664  -3.451  7.529   1.00 41.47  ? 98  ARG A O     1 
ATOM   751  C CB    . ARG A 1 110 ? -2.374  -4.112  9.960   1.00 38.12  ? 98  ARG A CB    1 
ATOM   752  C CG    . ARG A 1 110 ? -3.798  -3.929  9.497   1.00 52.46  ? 98  ARG A CG    1 
ATOM   753  C CD    . ARG A 1 110 ? -4.590  -3.139  10.527  1.00 45.53  ? 98  ARG A CD    1 
ATOM   754  N NE    . ARG A 1 110 ? -4.064  -1.791  10.714  1.00 58.40  ? 98  ARG A NE    1 
ATOM   755  C CZ    . ARG A 1 110 ? -4.470  -0.726  10.033  1.00 68.80  ? 98  ARG A CZ    1 
ATOM   756  N NH1   . ARG A 1 110 ? -5.373  -0.823  9.068   1.00 58.38  ? 98  ARG A NH1   1 
ATOM   757  N NH2   . ARG A 1 110 ? -3.966  0.469   10.334  1.00 62.85  ? 98  ARG A NH2   1 
ATOM   758  N N     . VAL A 1 111 ? -2.029  -5.057  6.718   1.00 27.43  ? 99  VAL A N     1 
ATOM   759  C CA    . VAL A 1 111 ? -2.033  -4.523  5.360   1.00 28.77  ? 99  VAL A CA    1 
ATOM   760  C C     . VAL A 1 111 ? -2.984  -3.335  5.290   1.00 27.41  ? 99  VAL A C     1 
ATOM   761  O O     . VAL A 1 111 ? -4.162  -3.440  5.652   1.00 29.57  ? 99  VAL A O     1 
ATOM   762  C CB    . VAL A 1 111 ? -2.451  -5.605  4.355   1.00 25.27  ? 99  VAL A CB    1 
ATOM   763  C CG1   . VAL A 1 111 ? -2.540  -5.024  2.923   1.00 26.90  ? 99  VAL A CG1   1 
ATOM   764  C CG2   . VAL A 1 111 ? -1.459  -6.783  4.397   1.00 28.32  ? 99  VAL A CG2   1 
ATOM   765  N N     . ARG A 1 112 ? -2.480  -2.210  4.804   1.00 25.70  ? 100 ARG A N     1 
ATOM   766  C CA    . ARG A 1 112 ? -3.283  -1.010  4.587   1.00 27.28  ? 100 ARG A CA    1 
ATOM   767  C C     . ARG A 1 112 ? -3.685  -0.963  3.116   1.00 25.71  ? 100 ARG A C     1 
ATOM   768  O O     . ARG A 1 112 ? -2.919  -1.368  2.245   1.00 26.47  ? 100 ARG A O     1 
ATOM   769  C CB    . ARG A 1 112 ? -2.467  0.240   4.928   1.00 28.38  ? 100 ARG A CB    1 
ATOM   770  C CG    . ARG A 1 112 ? -1.765  0.171   6.278   1.00 44.81  ? 100 ARG A CG    1 
ATOM   771  C CD    . ARG A 1 112 ? -2.538  0.895   7.356   1.00 57.04  ? 100 ARG A CD    1 
ATOM   772  N NE    . ARG A 1 112 ? -1.771  2.018   7.886   1.00 73.45  ? 100 ARG A NE    1 
ATOM   773  C CZ    . ARG A 1 112 ? -0.791  1.910   8.775   1.00 69.20  ? 100 ARG A CZ    1 
ATOM   774  N NH1   . ARG A 1 112 ? -0.435  0.736   9.277   1.00 67.71  ? 100 ARG A NH1   1 
ATOM   775  N NH2   . ARG A 1 112 ? -0.144  3.006   9.165   1.00 67.54  ? 100 ARG A NH2   1 
ATOM   776  N N     . THR A 1 113 ? -4.907  -0.502  2.836   1.00 26.67  ? 101 THR A N     1 
ATOM   777  C CA    . THR A 1 113 ? -5.402  -0.468  1.470   1.00 25.36  ? 101 THR A CA    1 
ATOM   778  C C     . THR A 1 113 ? -5.448  0.976   0.993   1.00 27.61  ? 101 THR A C     1 
ATOM   779  O O     . THR A 1 113 ? -5.881  1.871   1.727   1.00 28.88  ? 101 THR A O     1 
ATOM   780  C CB    . THR A 1 113 ? -6.813  -1.067  1.411   1.00 29.53  ? 101 THR A CB    1 
ATOM   781  O OG1   . THR A 1 113 ? -6.754  -2.391  1.959   1.00 31.90  ? 101 THR A OG1   1 
ATOM   782  C CG2   . THR A 1 113 ? -7.273  -1.161  -0.020  1.00 31.34  ? 101 THR A CG2   1 
ATOM   783  N N     . ASP A 1 114 ? -5.026  1.210   -0.241  1.00 25.90  ? 102 ASP A N     1 
ATOM   784  C CA    . ASP A 1 114 ? -5.203  2.531   -0.845  1.00 25.18  ? 102 ASP A CA    1 
ATOM   785  C C     . ASP A 1 114 ? -5.650  2.291   -2.277  1.00 25.29  ? 102 ASP A C     1 
ATOM   786  O O     . ASP A 1 114 ? -4.880  1.748   -3.074  1.00 25.61  ? 102 ASP A O     1 
ATOM   787  C CB    . ASP A 1 114 ? -3.887  3.314   -0.813  1.00 24.96  ? 102 ASP A CB    1 
ATOM   788  C CG    . ASP A 1 114 ? -4.045  4.760   -1.300  1.00 30.22  ? 102 ASP A CG    1 
ATOM   789  O OD1   . ASP A 1 114 ? -4.966  5.020   -2.080  1.00 29.21  ? 102 ASP A OD1   1 
ATOM   790  O OD2   . ASP A 1 114 ? -3.234  5.633   -0.916  1.00 35.97  ? 102 ASP A OD2   1 
ATOM   791  N N     . ALA A 1 115 ? -6.878  2.712   -2.597  1.00 26.69  ? 103 ALA A N     1 
ATOM   792  C CA    . ALA A 1 115 ? -7.403  2.539   -3.938  1.00 27.48  ? 103 ALA A CA    1 
ATOM   793  C C     . ALA A 1 115 ? -6.595  3.270   -4.998  1.00 26.74  ? 103 ALA A C     1 
ATOM   794  O O     . ALA A 1 115 ? -6.712  2.938   -6.184  1.00 24.49  ? 103 ALA A O     1 
ATOM   795  C CB    . ALA A 1 115 ? -8.789  3.154   -3.986  1.00 30.27  ? 103 ALA A CB    1 
ATOM   796  N N     . ARG A 1 116 ? -5.803  4.280   -4.613  1.00 23.38  ? 104 ARG A N     1 
ATOM   797  C CA    . ARG A 1 116 ? -4.954  4.961   -5.597  1.00 25.72  ? 104 ARG A CA    1 
ATOM   798  C C     . ARG A 1 116 ? -3.861  4.058   -6.166  1.00 22.61  ? 104 ARG A C     1 
ATOM   799  O O     . ARG A 1 116 ? -3.248  4.417   -7.187  1.00 22.55  ? 104 ARG A O     1 
ATOM   800  C CB    . ARG A 1 116 ? -4.331  6.207   -4.975  1.00 25.20  ? 104 ARG A CB    1 
ATOM   801  C CG    . ARG A 1 116 ? -5.357  7.324   -4.743  1.00 28.35  ? 104 ARG A CG    1 
ATOM   802  C CD    . ARG A 1 116 ? -4.799  8.490   -3.922  1.00 29.84  ? 104 ARG A CD    1 
ATOM   803  N NE    . ARG A 1 116 ? -4.364  8.061   -2.598  1.00 29.51  ? 104 ARG A NE    1 
ATOM   804  C CZ    . ARG A 1 116 ? -4.142  8.880   -1.583  1.00 29.90  ? 104 ARG A CZ    1 
ATOM   805  N NH1   . ARG A 1 116 ? -4.393  10.172  -1.682  1.00 34.39  ? 104 ARG A NH1   1 
ATOM   806  N NH2   . ARG A 1 116 ? -3.695  8.388   -0.433  1.00 33.72  ? 104 ARG A NH2   1 
ATOM   807  N N     . LEU A 1 117 ? -3.619  2.889   -5.545  1.00 22.30  ? 105 LEU A N     1 
ATOM   808  C CA    . LEU A 1 117 ? -2.667  1.914   -6.053  1.00 21.91  ? 105 LEU A CA    1 
ATOM   809  C C     . LEU A 1 117 ? -3.267  0.955   -7.077  1.00 20.76  ? 105 LEU A C     1 
ATOM   810  O O     . LEU A 1 117 ? -2.579  0.021   -7.495  1.00 22.00  ? 105 LEU A O     1 
ATOM   811  C CB    . LEU A 1 117 ? -2.073  1.109   -4.894  1.00 21.88  ? 105 LEU A CB    1 
ATOM   812  C CG    . LEU A 1 117 ? -1.370  1.969   -3.860  1.00 20.89  ? 105 LEU A CG    1 
ATOM   813  C CD1   . LEU A 1 117 ? -1.028  1.104   -2.625  1.00 24.35  ? 105 LEU A CD1   1 
ATOM   814  C CD2   . LEU A 1 117 ? -0.059  2.486   -4.474  1.00 21.39  ? 105 LEU A CD2   1 
ATOM   815  N N     . ARG A 1 118 ? -4.529  1.126   -7.460  1.00 22.01  ? 106 ARG A N     1 
ATOM   816  C CA    . ARG A 1 118 ? -5.138  0.236   -8.428  1.00 21.98  ? 106 ARG A CA    1 
ATOM   817  C C     . ARG A 1 118 ? -4.415  0.266   -9.775  1.00 22.37  ? 106 ARG A C     1 
ATOM   818  O O     . ARG A 1 118 ? -3.705  1.220   -10.129 1.00 21.23  ? 106 ARG A O     1 
ATOM   819  C CB    . ARG A 1 118 ? -6.596  0.641   -8.607  1.00 21.38  ? 106 ARG A CB    1 
ATOM   820  C CG    . ARG A 1 118 ? -6.736  2.056   -9.256  1.00 22.14  ? 106 ARG A CG    1 
ATOM   821  C CD    . ARG A 1 118 ? -8.241  2.443   -9.267  1.00 24.59  ? 106 ARG A CD    1 
ATOM   822  N NE    . ARG A 1 118 ? -8.452  3.781   -9.841  1.00 22.72  ? 106 ARG A NE    1 
ATOM   823  C CZ    . ARG A 1 118 ? -8.394  4.910   -9.141  1.00 26.34  ? 106 ARG A CZ    1 
ATOM   824  N NH1   . ARG A 1 118 ? -8.127  4.907   -7.850  1.00 26.35  ? 106 ARG A NH1   1 
ATOM   825  N NH2   . ARG A 1 118 ? -8.638  6.077   -9.751  1.00 27.49  ? 106 ARG A NH2   1 
ATOM   826  N N     . GLU A 1 119 ? -4.575  -0.807  -10.547 1.00 21.15  ? 107 GLU A N     1 
ATOM   827  C CA    . GLU A 1 119 ? -4.025  -0.849  -11.883 1.00 22.14  ? 107 GLU A CA    1 
ATOM   828  C C     . GLU A 1 119 ? -4.659  0.245   -12.737 1.00 20.07  ? 107 GLU A C     1 
ATOM   829  O O     . GLU A 1 119 ? -5.761  0.723   -12.471 1.00 21.40  ? 107 GLU A O     1 
ATOM   830  C CB    . GLU A 1 119 ? -4.225  -2.248  -12.489 1.00 23.14  ? 107 GLU A CB    1 
ATOM   831  C CG    . GLU A 1 119 ? -3.592  -2.518  -13.895 1.00 20.30  ? 107 GLU A CG    1 
ATOM   832  C CD    . GLU A 1 119 ? -2.098  -2.223  -14.020 1.00 20.94  ? 107 GLU A CD    1 
ATOM   833  O OE1   . GLU A 1 119 ? -1.662  -1.091  -13.731 1.00 20.89  ? 107 GLU A OE1   1 
ATOM   834  O OE2   . GLU A 1 119 ? -1.319  -3.116  -14.473 1.00 22.52  ? 107 GLU A OE2   1 
ATOM   835  N N     . VAL A 1 120 ? -3.938  0.624   -13.781 1.00 19.73  ? 108 VAL A N     1 
ATOM   836  C CA    . VAL A 1 120 ? -4.527  1.506   -14.779 1.00 21.41  ? 108 VAL A CA    1 
ATOM   837  C C     . VAL A 1 120 ? -5.841  0.906   -15.265 1.00 22.73  ? 108 VAL A C     1 
ATOM   838  O O     . VAL A 1 120 ? -5.957  -0.311  -15.453 1.00 22.72  ? 108 VAL A O     1 
ATOM   839  C CB    . VAL A 1 120 ? -3.526  1.733   -15.932 1.00 22.10  ? 108 VAL A CB    1 
ATOM   840  C CG1   . VAL A 1 120 ? -3.175  0.408   -16.636 1.00 23.68  ? 108 VAL A CG1   1 
ATOM   841  C CG2   . VAL A 1 120 ? -4.058  2.747   -16.932 1.00 23.27  ? 108 VAL A CG2   1 
ATOM   842  N N     A ARG A 1 121 ? -6.848  1.755   -15.451 0.50 21.16  ? 109 ARG A N     1 
ATOM   843  N N     B ARG A 1 121 ? -6.838  1.757   -15.502 0.50 21.14  ? 109 ARG A N     1 
ATOM   844  C CA    A ARG A 1 121 ? -8.066  1.292   -16.098 0.50 21.29  ? 109 ARG A CA    1 
ATOM   845  C CA    B ARG A 1 121 ? -8.085  1.252   -16.061 0.50 21.29  ? 109 ARG A CA    1 
ATOM   846  C C     A ARG A 1 121 ? -7.708  0.707   -17.456 0.50 21.34  ? 109 ARG A C     1 
ATOM   847  C C     B ARG A 1 121 ? -7.842  0.770   -17.487 0.50 21.27  ? 109 ARG A C     1 
ATOM   848  O O     A ARG A 1 121 ? -6.860  1.252   -18.169 0.50 20.98  ? 109 ARG A O     1 
ATOM   849  O O     B ARG A 1 121 ? -7.208  1.459   -18.286 0.50 22.80  ? 109 ARG A O     1 
ATOM   850  C CB    A ARG A 1 121 ? -9.007  2.478   -16.301 0.50 22.04  ? 109 ARG A CB    1 
ATOM   851  C CB    B ARG A 1 121 ? -9.165  2.335   -16.044 0.50 22.89  ? 109 ARG A CB    1 
ATOM   852  C CG    A ARG A 1 121 ? -10.341 2.101   -16.887 0.50 24.31  ? 109 ARG A CG    1 
ATOM   853  C CG    B ARG A 1 121 ? -10.536 1.782   -16.395 0.50 25.63  ? 109 ARG A CG    1 
ATOM   854  C CD    A ARG A 1 121 ? -11.463 2.000   -15.840 0.50 24.93  ? 109 ARG A CD    1 
ATOM   855  C CD    B ARG A 1 121 ? -11.571 2.879   -16.754 0.50 28.25  ? 109 ARG A CD    1 
ATOM   856  N NE    A ARG A 1 121 ? -12.742 1.907   -16.527 0.50 25.88  ? 109 ARG A NE    1 
ATOM   857  N NE    B ARG A 1 121 ? -10.953 4.014   -17.433 0.50 33.80  ? 109 ARG A NE    1 
ATOM   858  C CZ    A ARG A 1 121 ? -13.924 1.912   -15.930 0.50 26.20  ? 109 ARG A CZ    1 
ATOM   859  C CZ    B ARG A 1 121 ? -11.568 4.863   -18.246 0.50 31.32  ? 109 ARG A CZ    1 
ATOM   860  N NH1   A ARG A 1 121 ? -14.032 1.963   -14.613 0.50 31.77  ? 109 ARG A NH1   1 
ATOM   861  N NH1   B ARG A 1 121 ? -12.843 4.722   -18.565 0.50 27.27  ? 109 ARG A NH1   1 
ATOM   862  N NH2   A ARG A 1 121 ? -15.025 1.894   -16.674 0.50 26.98  ? 109 ARG A NH2   1 
ATOM   863  N NH2   B ARG A 1 121 ? -10.892 5.904   -18.724 0.50 38.28  ? 109 ARG A NH2   1 
ATOM   864  N N     . THR A 1 122 ? -8.338  -0.421  -17.809 1.00 25.86  ? 110 THR A N     1 
ATOM   865  C CA    . THR A 1 122 ? -8.078  -1.082  -19.082 1.00 22.70  ? 110 THR A CA    1 
ATOM   866  C C     . THR A 1 122 ? -9.319  -1.113  -19.978 1.00 22.23  ? 110 THR A C     1 
ATOM   867  O O     . THR A 1 122 ? -10.451 -0.857  -19.555 1.00 25.31  ? 110 THR A O     1 
ATOM   868  C CB    . THR A 1 122 ? -7.638  -2.535  -18.849 1.00 23.26  ? 110 THR A CB    1 
ATOM   869  O OG1   . THR A 1 122 ? -8.740  -3.255  -18.230 1.00 22.95  ? 110 THR A OG1   1 
ATOM   870  C CG2   . THR A 1 122 ? -6.399  -2.618  -17.959 1.00 25.02  ? 110 THR A CG2   1 
ATOM   871  N N     . ASN A 1 123 ? -9.076  -1.455  -21.248 1.00 23.17  ? 111 ASN A N     1 
ATOM   872  C CA    . ASN A 1 123 ? -10.181 -1.750  -22.167 1.00 26.41  ? 111 ASN A CA    1 
ATOM   873  C C     . ASN A 1 123 ? -11.138 -2.773  -21.578 1.00 25.44  ? 111 ASN A C     1 
ATOM   874  O O     . ASN A 1 123 ? -12.355 -2.621  -21.669 1.00 25.20  ? 111 ASN A O     1 
ATOM   875  C CB    . ASN A 1 123 ? -9.633  -2.296  -23.487 1.00 24.38  ? 111 ASN A CB    1 
ATOM   876  C CG    . ASN A 1 123 ? -9.157  -1.211  -24.415 1.00 31.31  ? 111 ASN A CG    1 
ATOM   877  O OD1   . ASN A 1 123 ? -8.986  -0.066  -24.009 1.00 33.65  ? 111 ASN A OD1   1 
ATOM   878  N ND2   . ASN A 1 123 ? -8.918  -1.575  -25.668 1.00 29.88  ? 111 ASN A ND2   1 
ATOM   879  N N     . TRP A 1 124 ? -10.599 -3.817  -20.958 1.00 23.43  ? 112 TRP A N     1 
ATOM   880  C CA    . TRP A 1 124 ? -11.462 -4.836  -20.372 1.00 25.96  ? 112 TRP A CA    1 
ATOM   881  C C     . TRP A 1 124 ? -12.357 -4.241  -19.288 1.00 26.34  ? 112 TRP A C     1 
ATOM   882  O O     . TRP A 1 124 ? -13.553 -4.543  -19.240 1.00 25.44  ? 112 TRP A O     1 
ATOM   883  C CB    . TRP A 1 124 ? -10.592 -5.984  -19.842 1.00 26.31  ? 112 TRP A CB    1 
ATOM   884  C CG    . TRP A 1 124 ? -11.379 -7.186  -19.306 1.00 24.78  ? 112 TRP A CG    1 
ATOM   885  C CD1   . TRP A 1 124 ? -12.693 -7.496  -19.546 1.00 26.37  ? 112 TRP A CD1   1 
ATOM   886  C CD2   . TRP A 1 124 ? -10.870 -8.214  -18.449 1.00 26.62  ? 112 TRP A CD2   1 
ATOM   887  N NE1   . TRP A 1 124 ? -13.023 -8.669  -18.886 1.00 29.34  ? 112 TRP A NE1   1 
ATOM   888  C CE2   . TRP A 1 124 ? -11.915 -9.128  -18.227 1.00 27.13  ? 112 TRP A CE2   1 
ATOM   889  C CE3   . TRP A 1 124 ? -9.619  -8.467  -17.870 1.00 27.69  ? 112 TRP A CE3   1 
ATOM   890  C CZ2   . TRP A 1 124 ? -11.767 -10.247 -17.415 1.00 28.06  ? 112 TRP A CZ2   1 
ATOM   891  C CZ3   . TRP A 1 124 ? -9.477  -9.598  -17.068 1.00 28.02  ? 112 TRP A CZ3   1 
ATOM   892  C CH2   . TRP A 1 124 ? -10.539 -10.463 -16.856 1.00 28.34  ? 112 TRP A CH2   1 
ATOM   893  N N     . ASP A 1 125 ? -11.807 -3.379  -18.424 1.00 25.57  ? 113 ASP A N     1 
ATOM   894  C CA    . ASP A 1 125 ? -12.613 -2.694  -17.412 1.00 26.43  ? 113 ASP A CA    1 
ATOM   895  C C     . ASP A 1 125 ? -13.737 -1.882  -18.041 1.00 26.75  ? 113 ASP A C     1 
ATOM   896  O O     . ASP A 1 125 ? -14.803 -1.717  -17.433 1.00 28.52  ? 113 ASP A O     1 
ATOM   897  C CB    . ASP A 1 125 ? -11.715 -1.743  -16.619 1.00 25.65  ? 113 ASP A CB    1 
ATOM   898  C CG    . ASP A 1 125 ? -10.664 -2.468  -15.810 1.00 26.91  ? 113 ASP A CG    1 
ATOM   899  O OD1   . ASP A 1 125 ? -10.823 -3.661  -15.451 1.00 25.77  ? 113 ASP A OD1   1 
ATOM   900  O OD2   . ASP A 1 125 ? -9.614  -1.826  -15.541 1.00 28.00  ? 113 ASP A OD2   1 
ATOM   901  N N     . ASP A 1 126 ? -13.517 -1.363  -19.250 1.00 25.08  ? 114 ASP A N     1 
ATOM   902  C CA    . ASP A 1 126 ? -14.509 -0.553  -19.957 1.00 27.80  ? 114 ASP A CA    1 
ATOM   903  C C     . ASP A 1 126 ? -15.450 -1.381  -20.811 1.00 31.61  ? 114 ASP A C     1 
ATOM   904  O O     . ASP A 1 126 ? -16.309 -0.816  -21.494 1.00 32.72  ? 114 ASP A O     1 
ATOM   905  C CB    . ASP A 1 126 ? -13.788 0.448   -20.870 1.00 29.41  ? 114 ASP A CB    1 
ATOM   906  C CG    . ASP A 1 126 ? -13.268 1.666   -20.120 1.00 29.54  ? 114 ASP A CG    1 
ATOM   907  O OD1   . ASP A 1 126 ? -13.576 1.833   -18.927 1.00 35.04  ? 114 ASP A OD1   1 
ATOM   908  O OD2   . ASP A 1 126 ? -12.556 2.462   -20.751 1.00 29.59  ? 114 ASP A OD2   1 
ATOM   909  N N     . GLY A 1 127 ? -15.307 -2.699  -20.799 1.00 27.91  ? 115 GLY A N     1 
ATOM   910  C CA    . GLY A 1 127 ? -16.166 -3.538  -21.622 1.00 32.54  ? 115 GLY A CA    1 
ATOM   911  C C     . GLY A 1 127 ? -15.812 -3.537  -23.097 1.00 32.16  ? 115 GLY A C     1 
ATOM   912  O O     . GLY A 1 127 ? -16.689 -3.794  -23.937 1.00 35.03  ? 115 GLY A O     1 
ATOM   913  N N     . ARG A 1 128 ? -14.555 -3.257  -23.441 1.00 30.78  ? 116 ARG A N     1 
ATOM   914  C CA    . ARG A 1 128 ? -14.118 -3.284  -24.821 1.00 32.24  ? 116 ARG A CA    1 
ATOM   915  C C     . ARG A 1 128 ? -13.086 -4.375  -25.022 1.00 32.27  ? 116 ARG A C     1 
ATOM   916  O O     . ARG A 1 128 ? -12.414 -4.772  -24.066 1.00 32.86  ? 116 ARG A O     1 
ATOM   917  C CB    . ARG A 1 128 ? -13.505 -1.940  -25.216 1.00 37.06  ? 116 ARG A CB    1 
ATOM   918  C CG    . ARG A 1 128 ? -14.550 -0.863  -25.220 1.00 39.73  ? 116 ARG A CG    1 
ATOM   919  C CD    . ARG A 1 128 ? -13.962 0.443   -24.782 1.00 48.71  ? 116 ARG A CD    1 
ATOM   920  N NE    . ARG A 1 128 ? -12.858 0.838   -25.641 1.00 53.42  ? 116 ARG A NE    1 
ATOM   921  C CZ    . ARG A 1 128 ? -11.829 1.559   -25.225 1.00 61.56  ? 116 ARG A CZ    1 
ATOM   922  N NH1   . ARG A 1 128 ? -11.698 1.898   -23.950 1.00 43.29  ? 116 ARG A NH1   1 
ATOM   923  N NH2   . ARG A 1 128 ? -10.906 1.939   -26.106 1.00 65.15  ? 116 ARG A NH2   1 
ATOM   924  N N     . PRO A 1 129 ? -12.961 -4.898  -26.247 1.00 33.07  ? 117 PRO A N     1 
ATOM   925  C CA    . PRO A 1 129 ? -11.872 -5.841  -26.545 1.00 30.02  ? 117 PRO A CA    1 
ATOM   926  C C     . PRO A 1 129 ? -10.517 -5.254  -26.195 1.00 30.64  ? 117 PRO A C     1 
ATOM   927  O O     . PRO A 1 129 ? -10.263 -4.062  -26.379 1.00 28.89  ? 117 PRO A O     1 
ATOM   928  C CB    . PRO A 1 129 ? -11.978 -6.037  -28.062 1.00 32.63  ? 117 PRO A CB    1 
ATOM   929  C CG    . PRO A 1 129 ? -13.393 -5.696  -28.399 1.00 39.83  ? 117 PRO A CG    1 
ATOM   930  C CD    . PRO A 1 129 ? -13.792 -4.610  -27.433 1.00 36.67  ? 117 PRO A CD    1 
ATOM   931  N N     . SER A 1 130 ? -9.641  -6.099  -25.681 1.00 26.60  ? 118 SER A N     1 
ATOM   932  C CA    . SER A 1 130 ? -8.256  -5.700  -25.477 1.00 26.69  ? 118 SER A CA    1 
ATOM   933  C C     . SER A 1 130 ? -7.539  -5.695  -26.815 1.00 30.36  ? 118 SER A C     1 
ATOM   934  O O     . SER A 1 130 ? -7.870  -6.462  -27.723 1.00 30.84  ? 118 SER A O     1 
ATOM   935  C CB    . SER A 1 130 ? -7.585  -6.708  -24.550 1.00 28.23  ? 118 SER A CB    1 
ATOM   936  O OG    . SER A 1 130 ? -8.176  -6.691  -23.263 1.00 26.28  ? 118 SER A OG    1 
ATOM   937  N N     . GLU A 1 131 ? -6.539  -4.823  -26.939 1.00 25.73  ? 119 GLU A N     1 
ATOM   938  C CA    . GLU A 1 131 ? -5.775  -4.737  -28.175 1.00 28.98  ? 119 GLU A CA    1 
ATOM   939  C C     . GLU A 1 131 ? -4.292  -4.706  -27.849 1.00 28.88  ? 119 GLU A C     1 
ATOM   940  O O     . GLU A 1 131 ? -3.874  -3.990  -26.942 1.00 28.86  ? 119 GLU A O     1 
ATOM   941  C CB    . GLU A 1 131 ? -6.076  -3.433  -28.939 1.00 33.50  ? 119 GLU A CB    1 
ATOM   942  C CG    . GLU A 1 131 ? -7.533  -3.245  -29.328 1.00 39.91  ? 119 GLU A CG    1 
ATOM   943  C CD    . GLU A 1 131 ? -7.767  -1.913  -30.009 1.00 51.20  ? 119 GLU A CD    1 
ATOM   944  O OE1   . GLU A 1 131 ? -6.779  -1.318  -30.489 1.00 53.74  ? 119 GLU A OE1   1 
ATOM   945  O OE2   . GLU A 1 131 ? -8.929  -1.462  -30.054 1.00 71.07  ? 119 GLU A OE2   1 
ATOM   946  N N     . LEU A 1 132 ? -3.503  -5.454  -28.617 1.00 26.79  ? 120 LEU A N     1 
ATOM   947  C CA    . LEU A 1 132 ? -2.045  -5.343  -28.552 1.00 29.01  ? 120 LEU A CA    1 
ATOM   948  C C     . LEU A 1 132 ? -1.583  -4.116  -29.343 1.00 30.35  ? 120 LEU A C     1 
ATOM   949  O O     . LEU A 1 132 ? -1.825  -4.024  -30.548 1.00 31.50  ? 120 LEU A O     1 
ATOM   950  C CB    . LEU A 1 132 ? -1.410  -6.616  -29.111 1.00 28.88  ? 120 LEU A CB    1 
ATOM   951  C CG    . LEU A 1 132 ? 0.115   -6.584  -29.209 1.00 34.03  ? 120 LEU A CG    1 
ATOM   952  C CD1   . LEU A 1 132 ? 0.720   -6.510  -27.837 1.00 30.78  ? 120 LEU A CD1   1 
ATOM   953  C CD2   . LEU A 1 132 ? 0.609   -7.812  -29.908 1.00 35.10  ? 120 LEU A CD2   1 
ATOM   954  N N     . LYS A 1 133 ? -0.915  -3.155  -28.655 1.00 25.60  ? 121 LYS A N     1 
ATOM   955  C CA    . LYS A 1 133 ? -0.495  -1.932  -29.314 1.00 26.64  ? 121 LYS A CA    1 
ATOM   956  C C     . LYS A 1 133 ? 0.981   -2.022  -29.671 1.00 25.54  ? 121 LYS A C     1 
ATOM   957  O O     . LYS A 1 133 ? 1.751   -2.712  -28.996 1.00 24.98  ? 121 LYS A O     1 
ATOM   958  C CB    . LYS A 1 133 ? -0.676  -0.747  -28.367 1.00 26.86  ? 121 LYS A CB    1 
ATOM   959  C CG    . LYS A 1 133 ? -2.145  -0.299  -28.172 1.00 29.97  ? 121 LYS A CG    1 
ATOM   960  C CD    . LYS A 1 133 ? -2.833  -0.199  -29.529 1.00 35.83  ? 121 LYS A CD    1 
ATOM   961  C CE    . LYS A 1 133 ? -3.952  0.805   -29.548 1.00 43.85  ? 121 LYS A CE    1 
ATOM   962  N NZ    . LYS A 1 133 ? -4.448  0.917   -30.955 1.00 41.95  ? 121 LYS A NZ    1 
ATOM   963  N N     . PRO A 1 134 ? 1.381   -1.311  -30.717 1.00 23.70  ? 122 PRO A N     1 
ATOM   964  C CA    . PRO A 1 134 ? 2.814   -1.205  -31.023 1.00 27.10  ? 122 PRO A CA    1 
ATOM   965  C C     . PRO A 1 134 ? 3.572   -0.563  -29.874 1.00 26.91  ? 122 PRO A C     1 
ATOM   966  O O     . PRO A 1 134 ? 3.027   0.213   -29.081 1.00 24.31  ? 122 PRO A O     1 
ATOM   967  C CB    . PRO A 1 134 ? 2.856   -0.279  -32.247 1.00 28.99  ? 122 PRO A CB    1 
ATOM   968  C CG    . PRO A 1 134 ? 1.457   -0.371  -32.856 1.00 31.60  ? 122 PRO A CG    1 
ATOM   969  C CD    . PRO A 1 134 ? 0.543   -0.544  -31.652 1.00 25.08  ? 122 PRO A CD    1 
ATOM   970  N N     . HIS A 1 135 ? 4.871   -0.867  -29.814 1.00 25.16  ? 123 HIS A N     1 
ATOM   971  C CA    . HIS A 1 135 ? 5.721   -0.166  -28.863 1.00 26.89  ? 123 HIS A CA    1 
ATOM   972  C C     . HIS A 1 135 ? 5.590   1.345   -29.037 1.00 26.67  ? 123 HIS A C     1 
ATOM   973  O O     . HIS A 1 135 ? 5.566   1.870   -30.162 1.00 27.59  ? 123 HIS A O     1 
ATOM   974  C CB    . HIS A 1 135 ? 7.190   -0.590  -29.031 1.00 28.07  ? 123 HIS A CB    1 
ATOM   975  C CG    . HIS A 1 135 ? 8.114   0.203   -28.172 1.00 28.29  ? 123 HIS A CG    1 
ATOM   976  N ND1   . HIS A 1 135 ? 8.984   1.136   -28.687 1.00 33.40  ? 123 HIS A ND1   1 
ATOM   977  C CD2   . HIS A 1 135 ? 8.227   0.286   -26.825 1.00 28.40  ? 123 HIS A CD2   1 
ATOM   978  C CE1   . HIS A 1 135 ? 9.623   1.733   -27.694 1.00 35.11  ? 123 HIS A CE1   1 
ATOM   979  N NE2   . HIS A 1 135 ? 9.190   1.230   -26.554 1.00 28.36  ? 123 HIS A NE2   1 
ATOM   980  N N     . GLY A 1 136 ? 5.482   2.032   -27.893 1.00 25.21  ? 124 GLY A N     1 
ATOM   981  C CA    . GLY A 1 136 ? 5.371   3.471   -27.845 1.00 27.36  ? 124 GLY A CA    1 
ATOM   982  C C     . GLY A 1 136 ? 3.957   3.993   -27.968 1.00 26.10  ? 124 GLY A C     1 
ATOM   983  O O     . GLY A 1 136 ? 3.760   5.210   -27.887 1.00 26.47  ? 124 GLY A O     1 
ATOM   984  N N     . VAL A 1 137 ? 2.964   3.128   -28.152 1.00 24.37  ? 125 VAL A N     1 
ATOM   985  C CA    . VAL A 1 137 ? 1.575   3.573   -28.275 1.00 25.05  ? 125 VAL A CA    1 
ATOM   986  C C     . VAL A 1 137 ? 0.859   3.242   -26.977 1.00 23.93  ? 125 VAL A C     1 
ATOM   987  O O     . VAL A 1 137 ? 0.803   2.079   -26.584 1.00 23.64  ? 125 VAL A O     1 
ATOM   988  C CB    . VAL A 1 137 ? 0.883   2.905   -29.457 1.00 24.52  ? 125 VAL A CB    1 
ATOM   989  C CG1   . VAL A 1 137 ? -0.640  3.273   -29.469 1.00 28.28  ? 125 VAL A CG1   1 
ATOM   990  C CG2   . VAL A 1 137 ? 1.575   3.295   -30.763 1.00 27.29  ? 125 VAL A CG2   1 
ATOM   991  N N     . TYR A 1 138 ? 0.312   4.256   -26.314 1.00 24.56  ? 126 TYR A N     1 
ATOM   992  C CA    . TYR A 1 138 ? -0.297  4.072   -24.994 1.00 22.34  ? 126 TYR A CA    1 
ATOM   993  C C     . TYR A 1 138 ? -1.571  3.244   -25.142 1.00 21.43  ? 126 TYR A C     1 
ATOM   994  O O     . TYR A 1 138 ? -2.432  3.589   -25.978 1.00 24.78  ? 126 TYR A O     1 
ATOM   995  C CB    . TYR A 1 138 ? -0.644  5.450   -24.427 1.00 23.48  ? 126 TYR A CB    1 
ATOM   996  C CG    . TYR A 1 138 ? -1.034  5.394   -22.978 1.00 21.36  ? 126 TYR A CG    1 
ATOM   997  C CD1   . TYR A 1 138 ? -0.120  5.024   -21.982 1.00 23.18  ? 126 TYR A CD1   1 
ATOM   998  C CD2   . TYR A 1 138 ? -2.350  5.703   -22.590 1.00 23.19  ? 126 TYR A CD2   1 
ATOM   999  C CE1   . TYR A 1 138 ? -0.461  4.995   -20.631 1.00 20.71  ? 126 TYR A CE1   1 
ATOM   1000 C CE2   . TYR A 1 138 ? -2.725  5.656   -21.244 1.00 21.47  ? 126 TYR A CE2   1 
ATOM   1001 C CZ    . TYR A 1 138 ? -1.797  5.300   -20.257 1.00 19.99  ? 126 TYR A CZ    1 
ATOM   1002 O OH    . TYR A 1 138 ? -2.166  5.275   -18.961 1.00 21.44  ? 126 TYR A OH    1 
ATOM   1003 N N     . PRO A 1 139 ? -1.708  2.150   -24.392 1.00 21.00  ? 127 PRO A N     1 
ATOM   1004 C CA    . PRO A 1 139 ? -2.791  1.179   -24.648 1.00 21.69  ? 127 PRO A CA    1 
ATOM   1005 C C     . PRO A 1 139 ? -3.982  1.281   -23.696 1.00 24.06  ? 127 PRO A C     1 
ATOM   1006 O O     . PRO A 1 139 ? -4.887  0.434   -23.786 1.00 26.81  ? 127 PRO A O     1 
ATOM   1007 C CB    . PRO A 1 139 ? -2.067  -0.152  -24.440 1.00 23.89  ? 127 PRO A CB    1 
ATOM   1008 C CG    . PRO A 1 139 ? -1.080  0.151   -23.371 1.00 23.41  ? 127 PRO A CG    1 
ATOM   1009 C CD    . PRO A 1 139 ? -0.603  1.561   -23.625 1.00 21.20  ? 127 PRO A CD    1 
ATOM   1010 N N     . PHE A 1 140 ? -4.036  2.272   -22.812 1.00 22.50  ? 128 PHE A N     1 
ATOM   1011 C CA    . PHE A 1 140 ? -5.058  2.252   -21.775 1.00 23.12  ? 128 PHE A CA    1 
ATOM   1012 C C     . PHE A 1 140 ? -5.997  3.445   -21.879 1.00 23.02  ? 128 PHE A C     1 
ATOM   1013 O O     . PHE A 1 140 ? -5.605  4.532   -22.324 1.00 23.44  ? 128 PHE A O     1 
ATOM   1014 C CB    . PHE A 1 140 ? -4.411  2.280   -20.388 1.00 21.56  ? 128 PHE A CB    1 
ATOM   1015 C CG    . PHE A 1 140 ? -3.331  1.266   -20.232 1.00 21.19  ? 128 PHE A CG    1 
ATOM   1016 C CD1   . PHE A 1 140 ? -3.623  -0.086  -20.233 1.00 21.71  ? 128 PHE A CD1   1 
ATOM   1017 C CD2   . PHE A 1 140 ? -2.016  1.677   -20.069 1.00 21.44  ? 128 PHE A CD2   1 
ATOM   1018 C CE1   . PHE A 1 140 ? -2.605  -1.042  -20.109 1.00 21.76  ? 128 PHE A CE1   1 
ATOM   1019 C CE2   . PHE A 1 140 ? -0.974  0.736   -19.925 1.00 22.15  ? 128 PHE A CE2   1 
ATOM   1020 C CZ    . PHE A 1 140 ? -1.283  -0.644  -19.932 1.00 23.61  ? 128 PHE A CZ    1 
ATOM   1021 N N     . PRO A 1 141 ? -7.256  3.280   -21.464 1.00 22.65  ? 129 PRO A N     1 
ATOM   1022 C CA    . PRO A 1 141 ? -8.189  4.406   -21.471 1.00 23.01  ? 129 PRO A CA    1 
ATOM   1023 C C     . PRO A 1 141 ? -7.986  5.409   -20.354 1.00 24.95  ? 129 PRO A C     1 
ATOM   1024 O O     . PRO A 1 141 ? -8.438  6.540   -20.503 1.00 27.63  ? 129 PRO A O     1 
ATOM   1025 C CB    . PRO A 1 141 ? -9.561  3.722   -21.367 1.00 24.19  ? 129 PRO A CB    1 
ATOM   1026 C CG    . PRO A 1 141 ? -9.303  2.410   -20.720 1.00 23.32  ? 129 PRO A CG    1 
ATOM   1027 C CD    . PRO A 1 141 ? -7.932  1.990   -21.200 1.00 24.02  ? 129 PRO A CD    1 
ATOM   1028 N N     . GLU A 1 142 ? -7.319  5.077   -19.262 1.00 23.63  ? 130 GLU A N     1 
ATOM   1029 C CA    . GLU A 1 142 ? -7.030  6.069   -18.232 1.00 23.96  ? 130 GLU A CA    1 
ATOM   1030 C C     . GLU A 1 142 ? -5.741  6.794   -18.595 1.00 22.91  ? 130 GLU A C     1 
ATOM   1031 O O     . GLU A 1 142 ? -4.697  6.141   -18.728 1.00 24.79  ? 130 GLU A O     1 
ATOM   1032 C CB    . GLU A 1 142 ? -6.866  5.389   -16.875 1.00 21.99  ? 130 GLU A CB    1 
ATOM   1033 C CG    . GLU A 1 142 ? -6.502  6.353   -15.756 1.00 23.15  ? 130 GLU A CG    1 
ATOM   1034 C CD    . GLU A 1 142 ? -6.354  5.668   -14.408 1.00 21.46  ? 130 GLU A CD    1 
ATOM   1035 O OE1   . GLU A 1 142 ? -6.348  4.420   -14.328 1.00 21.92  ? 130 GLU A OE1   1 
ATOM   1036 O OE2   . GLU A 1 142 ? -6.206  6.391   -13.400 1.00 25.30  ? 130 GLU A OE2   1 
ATOM   1037 N N     . PRO A 1 143 ? -5.746  8.123   -18.732 1.00 24.23  ? 131 PRO A N     1 
ATOM   1038 C CA    . PRO A 1 143 ? -4.542  8.813   -19.198 1.00 23.99  ? 131 PRO A CA    1 
ATOM   1039 C C     . PRO A 1 143 ? -3.351  8.599   -18.271 1.00 23.35  ? 131 PRO A C     1 
ATOM   1040 O O     . PRO A 1 143 ? -3.482  8.508   -17.045 1.00 22.89  ? 131 PRO A O     1 
ATOM   1041 C CB    . PRO A 1 143 ? -4.957  10.283  -19.210 1.00 27.80  ? 131 PRO A CB    1 
ATOM   1042 C CG    . PRO A 1 143 ? -6.438  10.256  -19.361 1.00 31.62  ? 131 PRO A CG    1 
ATOM   1043 C CD    . PRO A 1 143 ? -6.908  9.029   -18.635 1.00 24.98  ? 131 PRO A CD    1 
ATOM   1044 N N     . GLU A 1 144 ? -2.181  8.538   -18.899 1.00 22.74  ? 132 GLU A N     1 
ATOM   1045 C CA    . GLU A 1 144 ? -0.947  8.299   -18.169 1.00 22.64  ? 132 GLU A CA    1 
ATOM   1046 C C     . GLU A 1 144 ? -0.740  9.308   -17.042 1.00 21.65  ? 132 GLU A C     1 
ATOM   1047 O O     . GLU A 1 144 ? -0.322  8.960   -15.932 1.00 21.50  ? 132 GLU A O     1 
ATOM   1048 C CB    . GLU A 1 144 ? 0.187   8.383   -19.189 1.00 29.58  ? 132 GLU A CB    1 
ATOM   1049 C CG    . GLU A 1 144 ? 1.518   8.071   -18.615 1.00 30.36  ? 132 GLU A CG    1 
ATOM   1050 C CD    . GLU A 1 144 ? 2.658   8.110   -19.627 1.00 31.20  ? 132 GLU A CD    1 
ATOM   1051 O OE1   . GLU A 1 144 ? 2.467   8.399   -20.821 1.00 40.19  ? 132 GLU A OE1   1 
ATOM   1052 O OE2   . GLU A 1 144 ? 3.767   7.851   -19.176 1.00 40.07  ? 132 GLU A OE2   1 
ATOM   1053 N N     . LYS A 1 145 ? -1.036  10.581  -17.309 1.00 23.51  ? 133 LYS A N     1 
ATOM   1054 C CA    . LYS A 1 145 ? -0.807  11.613  -16.311 1.00 28.84  ? 133 LYS A CA    1 
ATOM   1055 C C     . LYS A 1 145 ? -1.655  11.382  -15.070 1.00 25.13  ? 133 LYS A C     1 
ATOM   1056 O O     . LYS A 1 145 ? -1.203  11.654  -13.948 1.00 26.77  ? 133 LYS A O     1 
ATOM   1057 C CB    . LYS A 1 145 ? -1.122  12.975  -16.914 1.00 29.23  ? 133 LYS A CB    1 
ATOM   1058 C CG    . LYS A 1 145 ? -0.068  14.007  -16.644 1.00 49.36  ? 133 LYS A CG    1 
ATOM   1059 C CD    . LYS A 1 145 ? -0.460  15.346  -17.257 1.00 57.17  ? 133 LYS A CD    1 
ATOM   1060 C CE    . LYS A 1 145 ? 0.666   16.363  -17.156 1.00 60.75  ? 133 LYS A CE    1 
ATOM   1061 N NZ    . LYS A 1 145 ? 0.204   17.707  -17.602 1.00 69.33  ? 133 LYS A NZ    1 
ATOM   1062 N N     . GLU A 1 146 ? -2.891  10.882  -15.247 1.00 22.28  ? 134 GLU A N     1 
ATOM   1063 C CA    . GLU A 1 146 ? -3.739  10.592  -14.090 1.00 22.75  ? 134 GLU A CA    1 
ATOM   1064 C C     . GLU A 1 146 ? -3.182  9.448   -13.268 1.00 20.98  ? 134 GLU A C     1 
ATOM   1065 O O     . GLU A 1 146 ? -3.166  9.519   -12.030 1.00 23.57  ? 134 GLU A O     1 
ATOM   1066 C CB    . GLU A 1 146 ? -5.160  10.267  -14.535 1.00 24.28  ? 134 GLU A CB    1 
ATOM   1067 C CG    . GLU A 1 146 ? -5.822  11.477  -15.223 1.00 30.59  ? 134 GLU A CG    1 
ATOM   1068 C CD    . GLU A 1 146 ? -7.235  11.213  -15.686 1.00 30.67  ? 134 GLU A CD    1 
ATOM   1069 O OE1   . GLU A 1 146 ? -7.828  10.210  -15.213 1.00 29.61  ? 134 GLU A OE1   1 
ATOM   1070 O OE2   . GLU A 1 146 ? -7.752  12.036  -16.511 1.00 35.38  ? 134 GLU A OE2   1 
ATOM   1071 N N     . VAL A 1 147 ? -2.685  8.412   -13.939 1.00 20.36  ? 135 VAL A N     1 
ATOM   1072 C CA    . VAL A 1 147 ? -2.077  7.281   -13.232 1.00 21.14  ? 135 VAL A CA    1 
ATOM   1073 C C     . VAL A 1 147 ? -0.866  7.752   -12.435 1.00 20.21  ? 135 VAL A C     1 
ATOM   1074 O O     . VAL A 1 147 ? -0.707  7.400   -11.261 1.00 20.83  ? 135 VAL A O     1 
ATOM   1075 C CB    . VAL A 1 147 ? -1.679  6.179   -14.222 1.00 20.43  ? 135 VAL A CB    1 
ATOM   1076 C CG1   . VAL A 1 147 ? -1.038  5.003   -13.457 1.00 21.30  ? 135 VAL A CG1   1 
ATOM   1077 C CG2   . VAL A 1 147 ? -2.913  5.668   -14.971 1.00 21.57  ? 135 VAL A CG2   1 
ATOM   1078 N N     . ALA A 1 148 ? 0.018   8.507   -13.080 1.00 21.23  ? 136 ALA A N     1 
ATOM   1079 C CA    . ALA A 1 148 ? 1.231   8.943   -12.391 1.00 21.79  ? 136 ALA A CA    1 
ATOM   1080 C C     . ALA A 1 148 ? 0.889   9.775   -11.167 1.00 22.87  ? 136 ALA A C     1 
ATOM   1081 O O     . ALA A 1 148 ? 1.481   9.592   -10.100 1.00 24.18  ? 136 ALA A O     1 
ATOM   1082 C CB    . ALA A 1 148 ? 2.134   9.722   -13.341 1.00 22.67  ? 136 ALA A CB    1 
ATOM   1083 N N     . GLU A 1 149 ? -0.089  10.679  -11.289 1.00 22.12  ? 137 GLU A N     1 
ATOM   1084 C CA    . GLU A 1 149 ? -0.415  11.553  -10.171 1.00 24.96  ? 137 GLU A CA    1 
ATOM   1085 C C     . GLU A 1 149 ? -0.939  10.745  -8.993  1.00 26.45  ? 137 GLU A C     1 
ATOM   1086 O O     . GLU A 1 149 ? -0.516  10.946  -7.846  1.00 26.47  ? 137 GLU A O     1 
ATOM   1087 C CB    . GLU A 1 149 ? -1.475  12.549  -10.618 1.00 28.56  ? 137 GLU A CB    1 
ATOM   1088 C CG    . GLU A 1 149 ? -1.806  13.630  -9.613  1.00 39.58  ? 137 GLU A CG    1 
ATOM   1089 C CD    . GLU A 1 149 ? -2.569  14.791  -10.242 1.00 73.51  ? 137 GLU A CD    1 
ATOM   1090 O OE1   . GLU A 1 149 ? -2.401  15.024  -11.461 1.00 74.10  ? 137 GLU A OE1   1 
ATOM   1091 O OE2   . GLU A 1 149 ? -3.338  15.471  -9.521  1.00 84.31  ? 137 GLU A OE2   1 
ATOM   1092 N N     . ARG A 1 150 ? -1.898  9.849   -9.254  1.00 21.87  ? 138 ARG A N     1 
ATOM   1093 C CA    . ARG A 1 150 ? -2.498  9.103   -8.139  1.00 23.02  ? 138 ARG A CA    1 
ATOM   1094 C C     . ARG A 1 150 ? -1.496  8.131   -7.515  1.00 23.54  ? 138 ARG A C     1 
ATOM   1095 O O     . ARG A 1 150 ? -1.486  7.969   -6.287  1.00 22.80  ? 138 ARG A O     1 
ATOM   1096 C CB    . ARG A 1 150 ? -3.776  8.386   -8.555  1.00 24.27  ? 138 ARG A CB    1 
ATOM   1097 C CG    . ARG A 1 150 ? -3.667  7.322   -9.627  1.00 22.95  ? 138 ARG A CG    1 
ATOM   1098 C CD    . ARG A 1 150 ? -5.014  6.653   -9.789  1.00 23.23  ? 138 ARG A CD    1 
ATOM   1099 N NE    . ARG A 1 150 ? -5.042  5.735   -10.923 1.00 22.16  ? 138 ARG A NE    1 
ATOM   1100 C CZ    . ARG A 1 150 ? -4.558  4.495   -10.885 1.00 22.45  ? 138 ARG A CZ    1 
ATOM   1101 N NH1   . ARG A 1 150 ? -3.863  4.037   -9.831  1.00 23.56  ? 138 ARG A NH1   1 
ATOM   1102 N NH2   . ARG A 1 150 ? -4.754  3.691   -11.938 1.00 22.65  ? 138 ARG A NH2   1 
ATOM   1103 N N     . MET A 1 151 ? -0.637  7.526   -8.333  1.00 22.92  ? 139 MET A N     1 
ATOM   1104 C CA    . MET A 1 151 ? 0.406   6.642   -7.796  1.00 21.41  ? 139 MET A CA    1 
ATOM   1105 C C     . MET A 1 151 ? 1.404   7.411   -6.946  1.00 22.53  ? 139 MET A C     1 
ATOM   1106 O O     . MET A 1 151 ? 1.786   6.955   -5.857  1.00 24.47  ? 139 MET A O     1 
ATOM   1107 C CB    . MET A 1 151 ? 1.127   5.915   -8.926  1.00 20.68  ? 139 MET A CB    1 
ATOM   1108 C CG    . MET A 1 151 ? 0.344   4.767   -9.585  1.00 20.00  ? 139 MET A CG    1 
ATOM   1109 S SD    . MET A 1 151 ? -0.007  3.397   -8.459  1.00 21.14  ? 139 MET A SD    1 
ATOM   1110 C CE    . MET A 1 151 ? 1.667   2.764   -8.251  1.00 23.43  ? 139 MET A CE    1 
ATOM   1111 N N     . ARG A 1 152 ? 1.863   8.575   -7.416  1.00 21.75  ? 140 ARG A N     1 
ATOM   1112 C CA    . ARG A 1 152 ? 2.815   9.325   -6.616  1.00 23.69  ? 140 ARG A CA    1 
ATOM   1113 C C     . ARG A 1 152 ? 2.186   9.784   -5.303  1.00 24.65  ? 140 ARG A C     1 
ATOM   1114 O O     . ARG A 1 152 ? 2.821   9.731   -4.238  1.00 26.22  ? 140 ARG A O     1 
ATOM   1115 C CB    . ARG A 1 152 ? 3.348   10.495  -7.408  1.00 28.07  ? 140 ARG A CB    1 
ATOM   1116 C CG    . ARG A 1 152 ? 4.525   11.139  -6.713  1.00 34.79  ? 140 ARG A CG    1 
ATOM   1117 C CD    . ARG A 1 152 ? 5.025   12.331  -7.460  1.00 35.19  ? 140 ARG A CD    1 
ATOM   1118 N NE    . ARG A 1 152 ? 6.217   12.867  -6.804  1.00 46.49  ? 140 ARG A NE    1 
ATOM   1119 C CZ    . ARG A 1 152 ? 7.321   13.228  -7.440  1.00 52.75  ? 140 ARG A CZ    1 
ATOM   1120 N NH1   . ARG A 1 152 ? 7.380   13.241  -8.767  1.00 53.55  ? 140 ARG A NH1   1 
ATOM   1121 N NH2   . ARG A 1 152 ? 8.385   13.601  -6.731  1.00 48.81  ? 140 ARG A NH2   1 
ATOM   1122 N N     . THR A 1 153 ? 0.948   10.276  -5.366  1.00 25.31  ? 141 THR A N     1 
ATOM   1123 C CA    . THR A 1 153 ? 0.272   10.715  -4.153  1.00 27.22  ? 141 THR A CA    1 
ATOM   1124 C C     . THR A 1 153 ? 0.134   9.557   -3.160  1.00 26.20  ? 141 THR A C     1 
ATOM   1125 O O     . THR A 1 153 ? 0.330   9.740   -1.952  1.00 28.23  ? 141 THR A O     1 
ATOM   1126 C CB    . THR A 1 153 ? -1.081  11.304  -4.533  1.00 30.57  ? 141 THR A CB    1 
ATOM   1127 O OG1   . THR A 1 153 ? -0.858  12.474  -5.337  1.00 32.65  ? 141 THR A OG1   1 
ATOM   1128 C CG2   . THR A 1 153 ? -1.835  11.716  -3.287  1.00 37.69  ? 141 THR A CG2   1 
ATOM   1129 N N     . ALA A 1 154 ? -0.217  8.372   -3.660  1.00 26.81  ? 142 ALA A N     1 
ATOM   1130 C CA    . ALA A 1 154 ? -0.374  7.205   -2.797  1.00 25.95  ? 142 ALA A CA    1 
ATOM   1131 C C     . ALA A 1 154 ? 0.940   6.829   -2.127  1.00 23.98  ? 142 ALA A C     1 
ATOM   1132 O O     . ALA A 1 154 ? 0.959   6.523   -0.927  1.00 26.75  ? 142 ALA A O     1 
ATOM   1133 C CB    . ALA A 1 154 ? -0.891  6.026   -3.626  1.00 27.22  ? 142 ALA A CB    1 
ATOM   1134 N N     . VAL A 1 155 ? 2.039   6.845   -2.882  1.00 20.93  ? 143 VAL A N     1 
ATOM   1135 C CA    . VAL A 1 155 ? 3.331   6.513   -2.288  1.00 25.14  ? 143 VAL A CA    1 
ATOM   1136 C C     . VAL A 1 155 ? 3.735   7.549   -1.236  1.00 25.25  ? 143 VAL A C     1 
ATOM   1137 O O     . VAL A 1 155 ? 4.194   7.194   -0.137  1.00 25.98  ? 143 VAL A O     1 
ATOM   1138 C CB    . VAL A 1 155 ? 4.390   6.337   -3.380  1.00 24.21  ? 143 VAL A CB    1 
ATOM   1139 C CG1   . VAL A 1 155 ? 5.852   6.308   -2.752  1.00 25.98  ? 143 VAL A CG1   1 
ATOM   1140 C CG2   . VAL A 1 155 ? 4.094   5.087   -4.208  1.00 26.15  ? 143 VAL A CG2   1 
ATOM   1141 N N     . THR A 1 156 ? 3.570   8.846   -1.542  1.00 26.38  ? 144 THR A N     1 
ATOM   1142 C CA    . THR A 1 156 ? 3.867   9.885   -0.569  1.00 30.98  ? 144 THR A CA    1 
ATOM   1143 C C     . THR A 1 156 ? 3.067   9.678   0.711   1.00 26.55  ? 144 THR A C     1 
ATOM   1144 O O     . THR A 1 156 ? 3.585   9.864   1.817   1.00 32.60  ? 144 THR A O     1 
ATOM   1145 C CB    . THR A 1 156 ? 3.528   11.242  -1.187  1.00 34.73  ? 144 THR A CB    1 
ATOM   1146 O OG1   . THR A 1 156 ? 4.405   11.467  -2.294  1.00 36.48  ? 144 THR A OG1   1 
ATOM   1147 C CG2   . THR A 1 156 ? 3.670   12.377  -0.166  1.00 35.50  ? 144 THR A CG2   1 
ATOM   1148 N N     . ALA A 1 157 ? 1.790   9.294   0.570   1.00 27.47  ? 145 ALA A N     1 
ATOM   1149 C CA    . ALA A 1 157 ? 0.927   9.114   1.727   1.00 32.77  ? 145 ALA A CA    1 
ATOM   1150 C C     . ALA A 1 157 ? 1.349   7.904   2.553   1.00 29.22  ? 145 ALA A C     1 
ATOM   1151 O O     . ALA A 1 157 ? 1.349   7.955   3.783   1.00 32.80  ? 145 ALA A O     1 
ATOM   1152 C CB    . ALA A 1 157 ? -0.526  8.991   1.268   1.00 32.43  ? 145 ALA A CB    1 
ATOM   1153 N N     . ALA A 1 158 ? 1.737   6.811   1.883   1.00 26.82  ? 146 ALA A N     1 
ATOM   1154 C CA    . ALA A 1 158 ? 2.238   5.639   2.596   1.00 31.23  ? 146 ALA A CA    1 
ATOM   1155 C C     . ALA A 1 158 ? 3.497   5.961   3.390   1.00 29.21  ? 146 ALA A C     1 
ATOM   1156 O O     . ALA A 1 158 ? 3.650   5.514   4.532   1.00 33.35  ? 146 ALA A O     1 
ATOM   1157 C CB    . ALA A 1 158 ? 2.534   4.523   1.596   1.00 28.63  ? 146 ALA A CB    1 
ATOM   1158 N N     . VAL A 1 159 ? 4.423   6.712   2.797   1.00 27.14  ? 147 VAL A N     1 
ATOM   1159 C CA    . VAL A 1 159 ? 5.619   7.132   3.530   1.00 29.78  ? 147 VAL A CA    1 
ATOM   1160 C C     . VAL A 1 159 ? 5.235   7.971   4.744   1.00 30.91  ? 147 VAL A C     1 
ATOM   1161 O O     . VAL A 1 159 ? 5.745   7.771   5.856   1.00 31.85  ? 147 VAL A O     1 
ATOM   1162 C CB    . VAL A 1 159 ? 6.573   7.894   2.596   1.00 25.33  ? 147 VAL A CB    1 
ATOM   1163 C CG1   . VAL A 1 159 ? 7.776   8.422   3.369   1.00 29.27  ? 147 VAL A CG1   1 
ATOM   1164 C CG2   . VAL A 1 159 ? 7.051   6.973   1.496   1.00 28.68  ? 147 VAL A CG2   1 
ATOM   1165 N N     . ALA A 1 160 ? 4.333   8.938   4.545   1.00 35.76  ? 148 ALA A N     1 
ATOM   1166 C CA    . ALA A 1 160 ? 3.941   9.813   5.647   1.00 35.06  ? 148 ALA A CA    1 
ATOM   1167 C C     . ALA A 1 160 ? 3.230   9.043   6.753   1.00 37.50  ? 148 ALA A C     1 
ATOM   1168 O O     . ALA A 1 160 ? 3.324   9.416   7.926   1.00 46.57  ? 148 ALA A O     1 
ATOM   1169 C CB    . ALA A 1 160 ? 3.073   10.962  5.127   1.00 37.13  ? 148 ALA A CB    1 
ATOM   1170 N N     . ALA A 1 161 ? 2.518   7.968   6.399   1.00 35.06  ? 149 ALA A N     1 
ATOM   1171 C CA    . ALA A 1 161 ? 1.798   7.183   7.397   1.00 34.14  ? 149 ALA A CA    1 
ATOM   1172 C C     . ALA A 1 161 ? 2.689   6.206   8.145   1.00 42.41  ? 149 ALA A C     1 
ATOM   1173 O O     . ALA A 1 161 ? 2.240   5.622   9.138   1.00 42.35  ? 149 ALA A O     1 
ATOM   1174 C CB    . ALA A 1 161 ? 0.645   6.421   6.740   1.00 39.04  ? 149 ALA A CB    1 
ATOM   1175 N N     . THR A 1 162 ? 3.926   6.011   7.688   1.00 38.92  ? 150 THR A N     1 
ATOM   1176 C CA    . THR A 1 162 ? 4.882   5.104   8.304   1.00 40.13  ? 150 THR A CA    1 
ATOM   1177 C C     . THR A 1 162 ? 5.794   5.886   9.242   1.00 38.54  ? 150 THR A C     1 
ATOM   1178 O O     . THR A 1 162 ? 6.438   6.862   8.817   1.00 49.61  ? 150 THR A O     1 
ATOM   1179 C CB    . THR A 1 162 ? 5.714   4.420   7.217   1.00 38.83  ? 150 THR A CB    1 
ATOM   1180 O OG1   . THR A 1 162 ? 4.851   3.802   6.253   1.00 40.41  ? 150 THR A OG1   1 
ATOM   1181 C CG2   . THR A 1 162 ? 6.635   3.336   7.809   1.00 40.75  ? 150 THR A CG2   1 
ATOM   1182 N N     . PRO A 1 163 ? 5.874   5.477   10.499  1.00 56.01  ? 151 PRO A N     1 
ATOM   1183 C CA    . PRO A 1 163 ? 6.658   6.222   11.498  1.00 51.83  ? 151 PRO A CA    1 
ATOM   1184 C C     . PRO A 1 163 ? 8.134   5.884   11.380  1.00 44.52  ? 151 PRO A C     1 
ATOM   1185 O O     . PRO A 1 163 ? 8.479   4.757   11.001  1.00 47.55  ? 151 PRO A O     1 
ATOM   1186 C CB    . PRO A 1 163 ? 6.092   5.685   12.814  1.00 54.52  ? 151 PRO A CB    1 
ATOM   1187 C CG    . PRO A 1 163 ? 5.767   4.220   12.475  1.00 48.67  ? 151 PRO A CG    1 
ATOM   1188 C CD    . PRO A 1 163 ? 5.288   4.235   11.040  1.00 47.54  ? 151 PRO A CD    1 
ATOM   1189 N N     . PRO A 1 164 ? 9.029   6.820   11.696  1.00 44.15  ? 152 PRO A N     1 
ATOM   1190 C CA    . PRO A 1 164 ? 10.465  6.552   11.542  1.00 45.03  ? 152 PRO A CA    1 
ATOM   1191 C C     . PRO A 1 164 ? 10.875  5.240   12.201  1.00 50.14  ? 152 PRO A C     1 
ATOM   1192 O O     . PRO A 1 164 ? 10.472  4.929   13.330  1.00 44.83  ? 152 PRO A O     1 
ATOM   1193 C CB    . PRO A 1 164 ? 11.125  7.754   12.227  1.00 52.22  ? 152 PRO A CB    1 
ATOM   1194 C CG    . PRO A 1 164 ? 10.099  8.847   12.147  1.00 54.93  ? 152 PRO A CG    1 
ATOM   1195 C CD    . PRO A 1 164 ? 8.766   8.160   12.246  1.00 50.55  ? 152 PRO A CD    1 
ATOM   1196 N N     . ALA A 1 165 ? 11.655  4.455   11.467  1.00 46.60  ? 153 ALA A N     1 
ATOM   1197 C CA    . ALA A 1 165 ? 12.178  3.215   12.001  1.00 43.47  ? 153 ALA A CA    1 
ATOM   1198 C C     . ALA A 1 165 ? 13.059  3.524   13.207  1.00 41.13  ? 153 ALA A C     1 
ATOM   1199 O O     . ALA A 1 165 ? 13.653  4.605   13.292  1.00 50.52  ? 153 ALA A O     1 
ATOM   1200 C CB    . ALA A 1 165 ? 13.006  2.504   10.931  1.00 45.01  ? 153 ALA A CB    1 
ATOM   1201 N N     . PRO A 1 166 ? 13.097  2.624   14.200  1.00 47.24  ? 154 PRO A N     1 
ATOM   1202 C CA    . PRO A 1 166 ? 13.964  2.864   15.359  1.00 43.85  ? 154 PRO A CA    1 
ATOM   1203 C C     . PRO A 1 166 ? 15.405  3.136   14.984  1.00 51.19  ? 154 PRO A C     1 
ATOM   1204 O O     . PRO A 1 166 ? 16.018  4.067   15.524  1.00 50.80  ? 154 PRO A O     1 
ATOM   1205 C CB    . PRO A 1 166 ? 13.809  1.579   16.187  1.00 45.76  ? 154 PRO A CB    1 
ATOM   1206 C CG    . PRO A 1 166 ? 12.443  1.068   15.814  1.00 48.38  ? 154 PRO A CG    1 
ATOM   1207 C CD    . PRO A 1 166 ? 12.252  1.428   14.373  1.00 48.13  ? 154 PRO A CD    1 
ATOM   1208 N N     . ASP A 1 167 ? 15.966  2.348   14.070  1.00 48.92  ? 155 ASP A N     1 
ATOM   1209 C CA    . ASP A 1 167 ? 17.319  2.581   13.592  1.00 56.64  ? 155 ASP A CA    1 
ATOM   1210 C C     . ASP A 1 167 ? 17.359  2.310   12.098  1.00 51.58  ? 155 ASP A C     1 
ATOM   1211 O O     . ASP A 1 167 ? 16.671  1.415   11.599  1.00 46.60  ? 155 ASP A O     1 
ATOM   1212 C CB    . ASP A 1 167 ? 18.374  1.725   14.335  1.00 58.03  ? 155 ASP A CB    1 
ATOM   1213 C CG    . ASP A 1 167 ? 18.237  0.225   14.049  1.00 73.64  ? 155 ASP A CG    1 
ATOM   1214 O OD1   . ASP A 1 167 ? 17.242  -0.383  14.514  1.00 78.20  ? 155 ASP A OD1   1 
ATOM   1215 O OD2   . ASP A 1 167 ? 19.129  -0.346  13.367  1.00 62.15  ? 155 ASP A OD2   1 
ATOM   1216 N N     . GLY A 1 168 ? 18.133  3.114   11.384  1.00 48.96  ? 156 GLY A N     1 
ATOM   1217 C CA    . GLY A 1 168 ? 18.324  2.862   9.981   1.00 46.17  ? 156 GLY A CA    1 
ATOM   1218 C C     . GLY A 1 168 ? 17.177  3.372   9.131   1.00 52.10  ? 156 GLY A C     1 
ATOM   1219 O O     . GLY A 1 168 ? 16.381  4.240   9.517   1.00 48.26  ? 156 GLY A O     1 
ATOM   1220 N N     . THR A 1 169 ? 17.099  2.794   7.941   1.00 43.79  ? 157 THR A N     1 
ATOM   1221 C CA    . THR A 1 169 ? 16.210  3.282   6.908   1.00 40.59  ? 157 THR A CA    1 
ATOM   1222 C C     . THR A 1 169 ? 14.784  2.808   7.165   1.00 41.98  ? 157 THR A C     1 
ATOM   1223 O O     . THR A 1 169 ? 14.536  1.605   7.317   1.00 38.62  ? 157 THR A O     1 
ATOM   1224 C CB    . THR A 1 169 ? 16.698  2.763   5.557   1.00 40.67  ? 157 THR A CB    1 
ATOM   1225 O OG1   . THR A 1 169 ? 18.078  3.131   5.382   1.00 47.22  ? 157 THR A OG1   1 
ATOM   1226 C CG2   . THR A 1 169 ? 15.874  3.362   4.442   1.00 34.19  ? 157 THR A CG2   1 
ATOM   1227 N N     . THR A 1 170 ? 13.847  3.754   7.199   1.00 36.38  ? 158 THR A N     1 
ATOM   1228 C CA    . THR A 1 170 ? 12.431  3.434   7.281   1.00 33.40  ? 158 THR A CA    1 
ATOM   1229 C C     . THR A 1 170 ? 11.954  2.927   5.930   1.00 30.41  ? 158 THR A C     1 
ATOM   1230 O O     . THR A 1 170 ? 12.240  3.539   4.896   1.00 29.84  ? 158 THR A O     1 
ATOM   1231 C CB    . THR A 1 170 ? 11.662  4.697   7.638   1.00 37.10  ? 158 THR A CB    1 
ATOM   1232 O OG1   . THR A 1 170 ? 12.157  5.212   8.885   1.00 40.30  ? 158 THR A OG1   1 
ATOM   1233 C CG2   . THR A 1 170 ? 10.162  4.386   7.719   1.00 36.96  ? 158 THR A CG2   1 
ATOM   1234 N N     . ARG A 1 171 ? 11.202  1.824   5.925   1.00 30.17  ? 159 ARG A N     1 
ATOM   1235 C CA    . ARG A 1 171 ? 10.916  1.110   4.688   1.00 26.62  ? 159 ARG A CA    1 
ATOM   1236 C C     . ARG A 1 171 ? 9.460   0.658   4.661   1.00 25.44  ? 159 ARG A C     1 
ATOM   1237 O O     . ARG A 1 171 ? 8.996   0.040   5.619   1.00 28.06  ? 159 ARG A O     1 
ATOM   1238 C CB    . ARG A 1 171 ? 11.855  -0.111  4.553   1.00 26.07  ? 159 ARG A CB    1 
ATOM   1239 C CG    . ARG A 1 171 ? 11.680  -0.869  3.268   1.00 26.74  ? 159 ARG A CG    1 
ATOM   1240 C CD    . ARG A 1 171 ? 12.775  -1.947  3.145   1.00 27.91  ? 159 ARG A CD    1 
ATOM   1241 N NE    . ARG A 1 171 ? 14.111  -1.365  3.000   1.00 28.55  ? 159 ARG A NE    1 
ATOM   1242 C CZ    . ARG A 1 171 ? 15.027  -1.291  3.961   1.00 29.85  ? 159 ARG A CZ    1 
ATOM   1243 N NH1   . ARG A 1 171 ? 14.844  -1.847  5.162   1.00 30.00  ? 159 ARG A NH1   1 
ATOM   1244 N NH2   . ARG A 1 171 ? 16.182  -0.676  3.706   1.00 30.77  ? 159 ARG A NH2   1 
ATOM   1245 N N     . VAL A 1 172 ? 8.777   0.917   3.565   1.00 25.56  ? 160 VAL A N     1 
ATOM   1246 C CA    . VAL A 1 172 ? 7.378   0.518   3.419   1.00 23.68  ? 160 VAL A CA    1 
ATOM   1247 C C     . VAL A 1 172 ? 7.240   -0.295  2.143   1.00 23.44  ? 160 VAL A C     1 
ATOM   1248 O O     . VAL A 1 172 ? 7.804   0.067   1.104   1.00 27.04  ? 160 VAL A O     1 
ATOM   1249 C CB    . VAL A 1 172 ? 6.421   1.731   3.438   1.00 28.97  ? 160 VAL A CB    1 
ATOM   1250 C CG1   . VAL A 1 172 ? 6.728   2.713   2.337   1.00 27.27  ? 160 VAL A CG1   1 
ATOM   1251 C CG2   . VAL A 1 172 ? 4.949   1.264   3.359   1.00 30.57  ? 160 VAL A CG2   1 
ATOM   1252 N N     . ALA A 1 173 ? 6.533   -1.434  2.226   1.00 23.67  ? 161 ALA A N     1 
ATOM   1253 C CA    . ALA A 1 173 ? 6.226   -2.199  1.027   1.00 21.96  ? 161 ALA A CA    1 
ATOM   1254 C C     . ALA A 1 173 ? 4.877   -1.770  0.466   1.00 24.42  ? 161 ALA A C     1 
ATOM   1255 O O     . ALA A 1 173 ? 3.928   -1.509  1.216   1.00 25.14  ? 161 ALA A O     1 
ATOM   1256 C CB    . ALA A 1 173 ? 6.185   -3.697  1.356   1.00 23.33  ? 161 ALA A CB    1 
ATOM   1257 N N     . VAL A 1 174 ? 4.799   -1.702  -0.848  1.00 22.20  ? 162 VAL A N     1 
ATOM   1258 C CA    . VAL A 1 174 ? 3.613   -1.206  -1.537  1.00 20.98  ? 162 VAL A CA    1 
ATOM   1259 C C     . VAL A 1 174 ? 3.314   -2.188  -2.661  1.00 20.05  ? 162 VAL A C     1 
ATOM   1260 O O     . VAL A 1 174 ? 4.073   -2.278  -3.625  1.00 20.76  ? 162 VAL A O     1 
ATOM   1261 C CB    . VAL A 1 174 ? 3.838   0.213   -2.110  1.00 21.18  ? 162 VAL A CB    1 
ATOM   1262 C CG1   . VAL A 1 174 ? 2.600   0.609   -2.943  1.00 23.12  ? 162 VAL A CG1   1 
ATOM   1263 C CG2   . VAL A 1 174 ? 4.058   1.228   -0.990  1.00 25.11  ? 162 VAL A CG2   1 
ATOM   1264 N N     . VAL A 1 175 ? 2.205   -2.936  -2.532  1.00 23.44  ? 163 VAL A N     1 
ATOM   1265 C CA    . VAL A 1 175 ? 1.874   -3.978  -3.504  1.00 23.26  ? 163 VAL A CA    1 
ATOM   1266 C C     . VAL A 1 175 ? 0.862   -3.420  -4.497  1.00 20.64  ? 163 VAL A C     1 
ATOM   1267 O O     . VAL A 1 175 ? -0.257  -3.033  -4.122  1.00 22.27  ? 163 VAL A O     1 
ATOM   1268 C CB    . VAL A 1 175 ? 1.340   -5.246  -2.832  1.00 21.91  ? 163 VAL A CB    1 
ATOM   1269 C CG1   . VAL A 1 175 ? 1.074   -6.278  -3.896  1.00 24.78  ? 163 VAL A CG1   1 
ATOM   1270 C CG2   . VAL A 1 175 ? 2.341   -5.810  -1.794  1.00 23.86  ? 163 VAL A CG2   1 
ATOM   1271 N N     . GLY A 1 176 ? 1.263   -3.346  -5.741  1.00 20.60  ? 164 GLY A N     1 
ATOM   1272 C CA    . GLY A 1 176 ? 0.495   -2.798  -6.820  1.00 20.71  ? 164 GLY A CA    1 
ATOM   1273 C C     . GLY A 1 176 ? 0.529   -3.635  -8.078  1.00 19.53  ? 164 GLY A C     1 
ATOM   1274 O O     . GLY A 1 176 ? 0.641   -4.886  -8.003  1.00 20.85  ? 164 GLY A O     1 
ATOM   1275 N N     . HIS A 1 177 ? 0.424   -2.970  -9.225  1.00 19.56  ? 165 HIS A N     1 
ATOM   1276 C CA    . HIS A 1 177 ? 0.144   -3.610  -10.494 1.00 20.07  ? 165 HIS A CA    1 
ATOM   1277 C C     . HIS A 1 177 ? 1.127   -3.113  -11.533 1.00 20.71  ? 165 HIS A C     1 
ATOM   1278 O O     . HIS A 1 177 ? 1.538   -1.944  -11.512 1.00 20.32  ? 165 HIS A O     1 
ATOM   1279 C CB    . HIS A 1 177 ? -1.307  -3.294  -10.907 1.00 20.02  ? 165 HIS A CB    1 
ATOM   1280 C CG    . HIS A 1 177 ? -2.310  -3.762  -9.892  1.00 21.37  ? 165 HIS A CG    1 
ATOM   1281 N ND1   . HIS A 1 177 ? -2.988  -4.966  -9.985  1.00 21.01  ? 165 HIS A ND1   1 
ATOM   1282 C CD2   . HIS A 1 177 ? -2.766  -3.167  -8.757  1.00 21.01  ? 165 HIS A CD2   1 
ATOM   1283 C CE1   . HIS A 1 177 ? -3.782  -5.110  -8.935  1.00 22.81  ? 165 HIS A CE1   1 
ATOM   1284 N NE2   . HIS A 1 177 ? -3.666  -4.033  -8.166  1.00 22.73  ? 165 HIS A NE2   1 
ATOM   1285 N N     . ASP A 1 178 ? 1.494   -4.001  -12.447 1.00 19.01  ? 166 ASP A N     1 
ATOM   1286 C CA    . ASP A 1 178 ? 2.541   -3.727  -13.421 1.00 19.44  ? 166 ASP A CA    1 
ATOM   1287 C C     . ASP A 1 178 ? 2.449   -2.336  -14.040 1.00 19.65  ? 166 ASP A C     1 
ATOM   1288 O O     . ASP A 1 178 ? 3.408   -1.558  -13.941 1.00 18.28  ? 166 ASP A O     1 
ATOM   1289 C CB    . ASP A 1 178 ? 2.464   -4.798  -14.510 1.00 18.51  ? 166 ASP A CB    1 
ATOM   1290 C CG    . ASP A 1 178 ? 3.254   -4.427  -15.736 1.00 21.30  ? 166 ASP A CG    1 
ATOM   1291 O OD1   . ASP A 1 178 ? 4.471   -4.180  -15.565 1.00 20.69  ? 166 ASP A OD1   1 
ATOM   1292 O OD2   . ASP A 1 178 ? 2.655   -4.398  -16.843 1.00 24.43  ? 166 ASP A OD2   1 
ATOM   1293 N N     . SER A 1 179 ? 1.395   -2.061  -14.802 1.00 18.35  ? 167 SER A N     1 
ATOM   1294 C CA    . SER A 1 179 ? 1.468   -0.881  -15.658 1.00 18.88  ? 167 SER A CA    1 
ATOM   1295 C C     . SER A 1 179 ? 1.453   0.408   -14.845 1.00 17.33  ? 167 SER A C     1 
ATOM   1296 O O     . SER A 1 179 ? 2.183   1.364   -15.170 1.00 18.53  ? 167 SER A O     1 
ATOM   1297 C CB    . SER A 1 179 ? 0.345   -0.921  -16.690 1.00 20.82  ? 167 SER A CB    1 
ATOM   1298 O OG    . SER A 1 179 ? 0.570   -2.062  -17.536 1.00 24.52  ? 167 SER A OG    1 
ATOM   1299 N N     . ALA A 1 180 ? 0.665   0.454   -13.781 1.00 18.24  ? 168 ALA A N     1 
ATOM   1300 C CA    . ALA A 1 180 ? 0.646   1.642   -12.924 1.00 19.35  ? 168 ALA A CA    1 
ATOM   1301 C C     . ALA A 1 180 ? 2.004   1.865   -12.258 1.00 19.06  ? 168 ALA A C     1 
ATOM   1302 O O     . ALA A 1 180 ? 2.459   3.025   -12.117 1.00 19.65  ? 168 ALA A O     1 
ATOM   1303 C CB    . ALA A 1 180 ? -0.460  1.510   -11.884 1.00 20.10  ? 168 ALA A CB    1 
ATOM   1304 N N     . LEU A 1 181 ? 2.702   0.771   -11.891 1.00 18.75  ? 169 LEU A N     1 
ATOM   1305 C CA    . LEU A 1 181 ? 4.028   0.877   -11.286 1.00 18.96  ? 169 LEU A CA    1 
ATOM   1306 C C     . LEU A 1 181 ? 5.053   1.346   -12.311 1.00 18.81  ? 169 LEU A C     1 
ATOM   1307 O O     . LEU A 1 181 ? 5.896   2.202   -12.007 1.00 18.86  ? 169 LEU A O     1 
ATOM   1308 C CB    . LEU A 1 181 ? 4.437   -0.502  -10.740 1.00 17.69  ? 169 LEU A CB    1 
ATOM   1309 C CG    . LEU A 1 181 ? 3.703   -0.908  -9.448  1.00 19.52  ? 169 LEU A CG    1 
ATOM   1310 C CD1   . LEU A 1 181 ? 4.041   -2.370  -9.129  1.00 20.68  ? 169 LEU A CD1   1 
ATOM   1311 C CD2   . LEU A 1 181 ? 4.026   -0.014  -8.273  1.00 23.26  ? 169 LEU A CD2   1 
ATOM   1312 N N     . VAL A 1 182 ? 4.962   0.853   -13.544 1.00 17.74  ? 170 VAL A N     1 
ATOM   1313 C CA    . VAL A 1 182 ? 5.856   1.302   -14.619 1.00 17.53  ? 170 VAL A CA    1 
ATOM   1314 C C     . VAL A 1 182 ? 5.611   2.773   -14.960 1.00 18.94  ? 170 VAL A C     1 
ATOM   1315 O O     . VAL A 1 182 ? 6.559   3.528   -15.239 1.00 18.23  ? 170 VAL A O     1 
ATOM   1316 C CB    . VAL A 1 182 ? 5.723   0.388   -15.867 1.00 18.49  ? 170 VAL A CB    1 
ATOM   1317 C CG1   . VAL A 1 182 ? 6.429   0.996   -17.081 1.00 20.85  ? 170 VAL A CG1   1 
ATOM   1318 C CG2   . VAL A 1 182 ? 6.267   -1.017  -15.576 1.00 19.32  ? 170 VAL A CG2   1 
ATOM   1319 N N     . ILE A 1 183 ? 4.343   3.193   -14.987 1.00 18.59  ? 171 ILE A N     1 
ATOM   1320 C CA    . ILE A 1 183 ? 4.036   4.598   -15.225 1.00 17.58  ? 171 ILE A CA    1 
ATOM   1321 C C     . ILE A 1 183 ? 4.610   5.464   -14.115 1.00 19.09  ? 171 ILE A C     1 
ATOM   1322 O O     . ILE A 1 183 ? 5.234   6.504   -14.384 1.00 19.77  ? 171 ILE A O     1 
ATOM   1323 C CB    . ILE A 1 183 ? 2.515   4.756   -15.369 1.00 17.38  ? 171 ILE A CB    1 
ATOM   1324 C CG1   . ILE A 1 183 ? 2.104   4.216   -16.719 1.00 19.30  ? 171 ILE A CG1   1 
ATOM   1325 C CG2   . ILE A 1 183 ? 2.108   6.258   -15.201 1.00 20.31  ? 171 ILE A CG2   1 
ATOM   1326 C CD1   . ILE A 1 183 ? 0.574   4.018   -16.895 1.00 20.43  ? 171 ILE A CD1   1 
ATOM   1327 N N     . LEU A 1 184 ? 4.440   5.053   -12.859 1.00 17.72  ? 172 LEU A N     1 
ATOM   1328 C CA    . LEU A 1 184 ? 5.036   5.818   -11.770 1.00 19.24  ? 172 LEU A CA    1 
ATOM   1329 C C     . LEU A 1 184 ? 6.535   5.951   -11.965 1.00 20.06  ? 172 LEU A C     1 
ATOM   1330 O O     . LEU A 1 184 ? 7.058   7.068   -11.872 1.00 20.71  ? 172 LEU A O     1 
ATOM   1331 C CB    . LEU A 1 184 ? 4.725   5.152   -10.426 1.00 21.40  ? 172 LEU A CB    1 
ATOM   1332 C CG    . LEU A 1 184 ? 5.463   5.806   -9.247  1.00 20.44  ? 172 LEU A CG    1 
ATOM   1333 C CD1   . LEU A 1 184 ? 5.104   7.310   -9.084  1.00 22.30  ? 172 LEU A CD1   1 
ATOM   1334 C CD2   . LEU A 1 184 ? 5.235   5.017   -7.948  1.00 22.37  ? 172 LEU A CD2   1 
ATOM   1335 N N     . MET A 1 185 ? 7.250   4.839   -12.179 1.00 19.49  ? 173 MET A N     1 
ATOM   1336 C CA    . MET A 1 185 ? 8.705   4.936   -12.218 1.00 18.85  ? 173 MET A CA    1 
ATOM   1337 C C     . MET A 1 185 ? 9.184   5.678   -13.449 1.00 18.95  ? 173 MET A C     1 
ATOM   1338 O O     . MET A 1 185 ? 10.106  6.505   -13.346 1.00 19.00  ? 173 MET A O     1 
ATOM   1339 C CB    . MET A 1 185 ? 9.325   3.546   -12.145 1.00 18.21  ? 173 MET A CB    1 
ATOM   1340 C CG    . MET A 1 185 ? 9.227   2.944   -10.716 1.00 17.37  ? 173 MET A CG    1 
ATOM   1341 S SD    . MET A 1 185 ? 9.971   1.328   -10.535 1.00 19.23  ? 173 MET A SD    1 
ATOM   1342 C CE    . MET A 1 185 ? 8.714   0.297   -11.306 1.00 20.87  ? 173 MET A CE    1 
ATOM   1343 N N     . GLY A 1 186 ? 8.536   5.488   -14.601 1.00 19.91  ? 174 GLY A N     1 
ATOM   1344 C CA    . GLY A 1 186 ? 8.855   6.323   -15.753 1.00 19.53  ? 174 GLY A CA    1 
ATOM   1345 C C     . GLY A 1 186 ? 8.651   7.801   -15.479 1.00 21.83  ? 174 GLY A C     1 
ATOM   1346 O O     . GLY A 1 186 ? 9.527   8.612   -15.753 1.00 21.15  ? 174 GLY A O     1 
ATOM   1347 N N     . SER A 1 187 ? 7.523   8.150   -14.872 1.00 20.41  ? 175 SER A N     1 
ATOM   1348 C CA    . SER A 1 187 ? 7.218   9.551   -14.631 1.00 19.76  ? 175 SER A CA    1 
ATOM   1349 C C     . SER A 1 187 ? 8.226   10.181  -13.675 1.00 22.73  ? 175 SER A C     1 
ATOM   1350 O O     . SER A 1 187 ? 8.588   11.357  -13.842 1.00 21.79  ? 175 SER A O     1 
ATOM   1351 C CB    . SER A 1 187 ? 5.793   9.677   -14.098 1.00 24.17  ? 175 SER A CB    1 
ATOM   1352 O OG    . SER A 1 187 ? 5.687   9.267   -12.749 1.00 29.17  ? 175 SER A OG    1 
ATOM   1353 N N     . LEU A 1 188 ? 8.721   9.421   -12.686 1.00 21.18  ? 176 LEU A N     1 
ATOM   1354 C CA    . LEU A 1 188 ? 9.741   9.936   -11.772 1.00 20.26  ? 176 LEU A CA    1 
ATOM   1355 C C     . LEU A 1 188 ? 11.046  10.245  -12.500 1.00 21.00  ? 176 LEU A C     1 
ATOM   1356 O O     . LEU A 1 188 ? 11.845  11.072  -12.013 1.00 24.53  ? 176 LEU A O     1 
ATOM   1357 C CB    . LEU A 1 188 ? 9.973   8.977   -10.598 1.00 21.44  ? 176 LEU A CB    1 
ATOM   1358 C CG    . LEU A 1 188 ? 8.778   8.764   -9.660  1.00 22.33  ? 176 LEU A CG    1 
ATOM   1359 C CD1   . LEU A 1 188 ? 9.106   7.601   -8.716  1.00 23.36  ? 176 LEU A CD1   1 
ATOM   1360 C CD2   . LEU A 1 188 ? 8.495   10.080  -8.925  1.00 25.68  ? 176 LEU A CD2   1 
ATOM   1361 N N     A MET A 1 189 ? 11.262  9.653   -13.667 0.50 20.12  ? 177 MET A N     1 
ATOM   1362 N N     B MET A 1 189 ? 11.260  9.659   -13.669 0.50 20.11  ? 177 MET A N     1 
ATOM   1363 C CA    A MET A 1 189 ? 12.417  9.962   -14.489 0.50 19.88  ? 177 MET A CA    1 
ATOM   1364 C CA    B MET A 1 189 ? 12.426  9.970   -14.472 0.50 19.87  ? 177 MET A CA    1 
ATOM   1365 C C     A MET A 1 189 ? 12.064  10.865  -15.654 0.50 21.60  ? 177 MET A C     1 
ATOM   1366 C C     B MET A 1 189 ? 12.065  10.852  -15.667 0.50 21.58  ? 177 MET A C     1 
ATOM   1367 O O     A MET A 1 189 ? 12.862  11.006  -16.584 0.50 22.46  ? 177 MET A O     1 
ATOM   1368 O O     B MET A 1 189 ? 12.857  10.992  -16.602 0.50 22.49  ? 177 MET A O     1 
ATOM   1369 C CB    A MET A 1 189 ? 13.060  8.675   -14.992 0.50 21.29  ? 177 MET A CB    1 
ATOM   1370 C CB    B MET A 1 189 ? 13.139  8.670   -14.859 0.50 21.96  ? 177 MET A CB    1 
ATOM   1371 C CG    A MET A 1 189 ? 13.916  8.018   -13.916 0.50 21.09  ? 177 MET A CG    1 
ATOM   1372 C CG    B MET A 1 189 ? 13.452  7.753   -13.614 0.50 22.72  ? 177 MET A CG    1 
ATOM   1373 S SD    A MET A 1 189 ? 14.712  6.511   -14.508 0.50 23.35  ? 177 MET A SD    1 
ATOM   1374 S SD    B MET A 1 189 ? 14.866  6.644   -13.798 0.50 24.63  ? 177 MET A SD    1 
ATOM   1375 C CE    A MET A 1 189 ? 13.346  5.444   -14.753 0.50 18.89  ? 177 MET A CE    1 
ATOM   1376 C CE    B MET A 1 189 ? 14.445  6.271   -15.465 0.50 14.58  ? 177 MET A CE    1 
ATOM   1377 N N     . ASN A 1 190 ? 10.886  11.488  -15.624 1.00 20.66  ? 178 ASN A N     1 
ATOM   1378 C CA    A ASN A 1 190 ? 10.468  12.380  -16.703 0.70 24.26  ? 178 ASN A CA    1 
ATOM   1379 C CA    B ASN A 1 190 ? 10.408  12.365  -16.689 0.30 24.22  ? 178 ASN A CA    1 
ATOM   1380 C C     . ASN A 1 190 ? 10.372  11.656  -18.041 1.00 24.80  ? 178 ASN A C     1 
ATOM   1381 O O     . ASN A 1 190 ? 10.643  12.242  -19.093 1.00 24.89  ? 178 ASN A O     1 
ATOM   1382 C CB    A ASN A 1 190 ? 11.380  13.614  -16.814 0.70 22.64  ? 178 ASN A CB    1 
ATOM   1383 C CB    B ASN A 1 190 ? 11.174  13.689  -16.727 0.30 22.92  ? 178 ASN A CB    1 
ATOM   1384 C CG    A ASN A 1 190 ? 10.757  14.746  -17.623 0.70 34.45  ? 178 ASN A CG    1 
ATOM   1385 C CG    B ASN A 1 190 ? 11.069  14.453  -15.408 0.30 23.12  ? 178 ASN A CG    1 
ATOM   1386 O OD1   A ASN A 1 190 ? 9.537   14.881  -17.694 0.70 30.86  ? 178 ASN A OD1   1 
ATOM   1387 O OD1   B ASN A 1 190 ? 9.974   14.669  -14.894 0.30 24.02  ? 178 ASN A OD1   1 
ATOM   1388 N ND2   A ASN A 1 190 ? 11.607  15.559  -18.249 0.70 31.88  ? 178 ASN A ND2   1 
ATOM   1389 N ND2   B ASN A 1 190 ? 12.212  14.838  -14.848 0.30 28.06  ? 178 ASN A ND2   1 
ATOM   1390 N N     . LEU A 1 191 ? 10.003  10.382  -18.019 1.00 20.99  ? 179 LEU A N     1 
ATOM   1391 C CA    . LEU A 1 191 ? 9.858   9.607   -19.236 1.00 21.01  ? 179 LEU A CA    1 
ATOM   1392 C C     . LEU A 1 191 ? 8.388   9.241   -19.434 1.00 22.93  ? 179 LEU A C     1 
ATOM   1393 O O     . LEU A 1 191 ? 7.634   9.117   -18.466 1.00 25.84  ? 179 LEU A O     1 
ATOM   1394 C CB    . LEU A 1 191 ? 10.636  8.285   -19.112 1.00 21.54  ? 179 LEU A CB    1 
ATOM   1395 C CG    . LEU A 1 191 ? 12.145  8.382   -18.867 1.00 18.95  ? 179 LEU A CG    1 
ATOM   1396 C CD1   . LEU A 1 191 ? 12.675  6.988   -18.719 1.00 20.58  ? 179 LEU A CD1   1 
ATOM   1397 C CD2   . LEU A 1 191 ? 12.901  9.126   -19.979 1.00 23.38  ? 179 LEU A CD2   1 
ATOM   1398 N N     . GLY A 1 192 ? 8.007   9.065   -20.695 1.00 22.04  ? 180 GLY A N     1 
ATOM   1399 C CA    . GLY A 1 192 ? 6.633   8.741   -21.054 1.00 22.85  ? 180 GLY A CA    1 
ATOM   1400 C C     . GLY A 1 192 ? 6.511   7.260   -21.384 1.00 20.61  ? 180 GLY A C     1 
ATOM   1401 O O     . GLY A 1 192 ? 7.524   6.585   -21.566 1.00 22.38  ? 180 GLY A O     1 
ATOM   1402 N N     . TRP A 1 193 ? 5.269   6.769   -21.440 1.00 20.80  ? 181 TRP A N     1 
ATOM   1403 C CA    . TRP A 1 193 ? 5.041   5.340   -21.619 1.00 20.51  ? 181 TRP A CA    1 
ATOM   1404 C C     . TRP A 1 193 ? 5.778   4.868   -22.860 1.00 21.41  ? 181 TRP A C     1 
ATOM   1405 O O     . TRP A 1 193 ? 5.688   5.462   -23.934 1.00 22.69  ? 181 TRP A O     1 
ATOM   1406 C CB    . TRP A 1 193 ? 3.542   5.106   -21.819 1.00 21.52  ? 181 TRP A CB    1 
ATOM   1407 C CG    . TRP A 1 193 ? 3.199   3.619   -22.055 1.00 19.67  ? 181 TRP A CG    1 
ATOM   1408 C CD1   . TRP A 1 193 ? 3.010   3.026   -23.274 1.00 21.36  ? 181 TRP A CD1   1 
ATOM   1409 C CD2   . TRP A 1 193 ? 3.019   2.591   -21.057 1.00 20.27  ? 181 TRP A CD2   1 
ATOM   1410 N NE1   . TRP A 1 193 ? 2.754   1.682   -23.090 1.00 20.55  ? 181 TRP A NE1   1 
ATOM   1411 C CE2   . TRP A 1 193 ? 2.726   1.394   -21.753 1.00 18.28  ? 181 TRP A CE2   1 
ATOM   1412 C CE3   . TRP A 1 193 ? 3.070   2.550   -19.650 1.00 20.29  ? 181 TRP A CE3   1 
ATOM   1413 C CZ2   . TRP A 1 193 ? 2.508   0.185   -21.109 1.00 21.06  ? 181 TRP A CZ2   1 
ATOM   1414 C CZ3   . TRP A 1 193 ? 2.866   1.318   -18.993 1.00 21.07  ? 181 TRP A CZ3   1 
ATOM   1415 C CH2   . TRP A 1 193 ? 2.587   0.141   -19.747 1.00 21.26  ? 181 TRP A CH2   1 
ATOM   1416 N N     . GLY A 1 194 ? 6.514   3.765   -22.707 1.00 20.95  ? 182 GLY A N     1 
ATOM   1417 C CA    . GLY A 1 194 ? 7.278   3.211   -23.789 1.00 21.83  ? 182 GLY A CA    1 
ATOM   1418 C C     . GLY A 1 194 ? 8.777   3.457   -23.648 1.00 21.12  ? 182 GLY A C     1 
ATOM   1419 O O     . GLY A 1 194 ? 9.574   2.683   -24.184 1.00 23.53  ? 182 GLY A O     1 
ATOM   1420 N N     . GLN A 1 195 ? 9.180   4.512   -22.954 1.00 20.30  ? 183 GLN A N     1 
ATOM   1421 C CA    . GLN A 1 195 ? 10.619  4.777   -22.878 1.00 18.43  ? 183 GLN A CA    1 
ATOM   1422 C C     . GLN A 1 195 ? 11.272  3.828   -21.897 1.00 19.90  ? 183 GLN A C     1 
ATOM   1423 O O     . GLN A 1 195 ? 12.199  3.099   -22.256 1.00 19.79  ? 183 GLN A O     1 
ATOM   1424 C CB    . GLN A 1 195 ? 10.828  6.241   -22.480 1.00 19.53  ? 183 GLN A CB    1 
ATOM   1425 C CG    . GLN A 1 195 ? 10.346  7.208   -23.587 1.00 23.92  ? 183 GLN A CG    1 
ATOM   1426 C CD    . GLN A 1 195 ? 10.745  8.652   -23.330 1.00 23.73  ? 183 GLN A CD    1 
ATOM   1427 O OE1   . GLN A 1 195 ? 10.179  9.287   -22.471 1.00 23.21  ? 183 GLN A OE1   1 
ATOM   1428 N NE2   . GLN A 1 195 ? 11.767  9.139   -24.038 1.00 25.30  ? 183 GLN A NE2   1 
ATOM   1429 N N     . LEU A 1 196 ? 10.783  3.777   -20.669 1.00 18.73  ? 184 LEU A N     1 
ATOM   1430 C CA    . LEU A 1 196 ? 11.149  2.719   -19.724 1.00 19.04  ? 184 LEU A CA    1 
ATOM   1431 C C     . LEU A 1 196 ? 10.354  1.490   -20.127 1.00 19.30  ? 184 LEU A C     1 
ATOM   1432 O O     . LEU A 1 196 ? 9.221   1.271   -19.704 1.00 20.29  ? 184 LEU A O     1 
ATOM   1433 C CB    . LEU A 1 196 ? 10.812  3.146   -18.305 1.00 20.49  ? 184 LEU A CB    1 
ATOM   1434 C CG    . LEU A 1 196 ? 11.263  2.144   -17.250 1.00 21.26  ? 184 LEU A CG    1 
ATOM   1435 C CD1   . LEU A 1 196 ? 12.802  2.092   -17.157 1.00 21.96  ? 184 LEU A CD1   1 
ATOM   1436 C CD2   . LEU A 1 196 ? 10.651  2.547   -15.882 1.00 23.91  ? 184 LEU A CD2   1 
ATOM   1437 N N     . ASP A 1 197 ? 10.928  0.719   -21.043 1.00 18.85  ? 185 ASP A N     1 
ATOM   1438 C CA    . ASP A 1 197 ? 10.187  -0.282  -21.824 1.00 18.84  ? 185 ASP A CA    1 
ATOM   1439 C C     . ASP A 1 197 ? 10.309  -1.639  -21.145 1.00 18.18  ? 185 ASP A C     1 
ATOM   1440 O O     . ASP A 1 197 ? 11.159  -2.445  -21.519 1.00 19.71  ? 185 ASP A O     1 
ATOM   1441 C CB    . ASP A 1 197 ? 10.786  -0.342  -23.228 1.00 20.66  ? 185 ASP A CB    1 
ATOM   1442 C CG    . ASP A 1 197 ? 10.033  -1.273  -24.137 1.00 23.04  ? 185 ASP A CG    1 
ATOM   1443 O OD1   . ASP A 1 197 ? 8.815   -1.438  -23.872 1.00 22.87  ? 185 ASP A OD1   1 
ATOM   1444 O OD2   . ASP A 1 197 ? 10.641  -1.805  -25.084 1.00 24.87  ? 185 ASP A OD2   1 
ATOM   1445 N N     . MET A 1 198 ? 9.491   -1.862  -20.113 1.00 18.20  ? 186 MET A N     1 
ATOM   1446 C CA    . MET A 1 198 ? 9.643   -3.033  -19.253 1.00 19.32  ? 186 MET A CA    1 
ATOM   1447 C C     . MET A 1 198 ? 8.266   -3.510  -18.798 1.00 18.60  ? 186 MET A C     1 
ATOM   1448 O O     . MET A 1 198 ? 7.349   -2.696  -18.588 1.00 19.48  ? 186 MET A O     1 
ATOM   1449 C CB    . MET A 1 198 ? 10.422  -2.624  -17.990 1.00 21.20  ? 186 MET A CB    1 
ATOM   1450 C CG    . MET A 1 198 ? 11.853  -2.268  -18.269 1.00 21.47  ? 186 MET A CG    1 
ATOM   1451 S SD    . MET A 1 198 ? 12.808  -1.653  -16.831 1.00 22.10  ? 186 MET A SD    1 
ATOM   1452 C CE    . MET A 1 198 ? 13.134  -3.216  -16.041 1.00 18.83  ? 186 MET A CE    1 
ATOM   1453 N N     . ILE A 1 199 ? 8.124   -4.828  -18.663 1.00 18.28  ? 187 ILE A N     1 
ATOM   1454 C CA    . ILE A 1 199 ? 7.012   -5.407  -17.918 1.00 20.52  ? 187 ILE A CA    1 
ATOM   1455 C C     . ILE A 1 199 ? 7.567   -5.929  -16.598 1.00 18.52  ? 187 ILE A C     1 
ATOM   1456 O O     . ILE A 1 199 ? 8.537   -6.697  -16.590 1.00 20.75  ? 187 ILE A O     1 
ATOM   1457 C CB    . ILE A 1 199 ? 6.259   -6.488  -18.714 1.00 23.78  ? 187 ILE A CB    1 
ATOM   1458 C CG1   . ILE A 1 199 ? 5.116   -7.093  -17.862 1.00 25.66  ? 187 ILE A CG1   1 
ATOM   1459 C CG2   . ILE A 1 199 ? 7.143   -7.546  -19.185 1.00 26.65  ? 187 ILE A CG2   1 
ATOM   1460 C CD1   . ILE A 1 199 ? 3.956   -7.632  -18.724 1.00 38.94  ? 187 ILE A CD1   1 
ATOM   1461 N N     . LEU A 1 200 ? 7.011   -5.514  -15.514 1.00 17.82  ? 188 LEU A N     1 
ATOM   1462 C CA    . LEU A 1 200 ? 7.527   -5.905  -14.212 1.00 19.30  ? 188 LEU A CA    1 
ATOM   1463 C C     . LEU A 1 200 ? 7.126   -7.352  -13.923 1.00 18.96  ? 188 LEU A C     1 
ATOM   1464 O O     . LEU A 1 200 ? 5.928   -7.706  -14.026 1.00 19.64  ? 188 LEU A O     1 
ATOM   1465 C CB    . LEU A 1 200 ? 6.996   -5.003  -13.108 1.00 20.89  ? 188 LEU A CB    1 
ATOM   1466 C CG    . LEU A 1 200 ? 7.339   -3.541  -13.287 1.00 17.83  ? 188 LEU A CG    1 
ATOM   1467 C CD1   . LEU A 1 200 ? 6.683   -2.736  -12.197 1.00 20.48  ? 188 LEU A CD1   1 
ATOM   1468 C CD2   . LEU A 1 200 ? 8.865   -3.299  -13.261 1.00 20.38  ? 188 LEU A CD2   1 
ATOM   1469 N N     . PRO A 1 201 ? 8.063   -8.227  -13.539 1.00 18.24  ? 189 PRO A N     1 
ATOM   1470 C CA    . PRO A 1 201 ? 7.681   -9.613  -13.221 1.00 18.35  ? 189 PRO A CA    1 
ATOM   1471 C C     . PRO A 1 201 ? 6.714   -9.685  -12.052 1.00 18.92  ? 189 PRO A C     1 
ATOM   1472 O O     . PRO A 1 201 ? 6.698   -8.827  -11.167 1.00 19.03  ? 189 PRO A O     1 
ATOM   1473 C CB    . PRO A 1 201 ? 9.014   -10.263 -12.846 1.00 19.31  ? 189 PRO A CB    1 
ATOM   1474 C CG    . PRO A 1 201 ? 10.030  -9.480  -13.661 1.00 19.22  ? 189 PRO A CG    1 
ATOM   1475 C CD    . PRO A 1 201 ? 9.527   -8.051  -13.557 1.00 18.73  ? 189 PRO A CD    1 
ATOM   1476 N N     . LEU A 1 202 ? 5.870   -10.731 -12.058 1.00 19.74  ? 190 LEU A N     1 
ATOM   1477 C CA    . LEU A 1 202 ? 5.054   -11.036 -10.882 1.00 19.74  ? 190 LEU A CA    1 
ATOM   1478 C C     . LEU A 1 202 ? 5.926   -11.201 -9.649  1.00 20.95  ? 190 LEU A C     1 
ATOM   1479 O O     . LEU A 1 202 ? 6.956   -11.892 -9.681  1.00 19.97  ? 190 LEU A O     1 
ATOM   1480 C CB    . LEU A 1 202 ? 4.216   -12.296 -11.103 1.00 22.10  ? 190 LEU A CB    1 
ATOM   1481 C CG    . LEU A 1 202 ? 3.233   -12.129 -12.261 1.00 23.31  ? 190 LEU A CG    1 
ATOM   1482 C CD1   . LEU A 1 202 ? 2.794   -13.537 -12.729 1.00 25.47  ? 190 LEU A CD1   1 
ATOM   1483 C CD2   . LEU A 1 202 ? 2.007   -11.272 -11.871 1.00 22.05  ? 190 LEU A CD2   1 
ATOM   1484 N N     . THR A 1 203 ? 5.504   -10.583 -8.551  1.00 18.92  ? 191 THR A N     1 
ATOM   1485 C CA    . THR A 1 203 ? 6.251   -10.518 -7.289  1.00 19.33  ? 191 THR A CA    1 
ATOM   1486 C C     . THR A 1 203 ? 7.585   -9.783  -7.384  1.00 17.50  ? 191 THR A C     1 
ATOM   1487 O O     . THR A 1 203 ? 8.406   -9.886  -6.456  1.00 19.32  ? 191 THR A O     1 
ATOM   1488 C CB    . THR A 1 203 ? 6.389   -11.826 -6.502  1.00 19.31  ? 191 THR A CB    1 
ATOM   1489 O OG1   . THR A 1 203 ? 7.255   -12.760 -7.185  1.00 20.85  ? 191 THR A OG1   1 
ATOM   1490 C CG2   . THR A 1 203 ? 5.042   -12.464 -6.260  1.00 22.60  ? 191 THR A CG2   1 
ATOM   1491 N N     . SER A 1 204 ? 7.808   -9.008  -8.449  1.00 19.04  ? 192 SER A N     1 
ATOM   1492 C CA    . SER A 1 204 ? 9.069   -8.291  -8.488  1.00 18.41  ? 192 SER A CA    1 
ATOM   1493 C C     . SER A 1 204 ? 9.085   -7.151  -7.478  1.00 18.28  ? 192 SER A C     1 
ATOM   1494 O O     . SER A 1 204 ? 8.045   -6.600  -7.112  1.00 19.25  ? 192 SER A O     1 
ATOM   1495 C CB    . SER A 1 204 ? 9.332   -7.708  -9.867  1.00 19.97  ? 192 SER A CB    1 
ATOM   1496 O OG    . SER A 1 204 ? 8.351   -6.770  -10.269 1.00 19.01  ? 192 SER A OG    1 
ATOM   1497 N N     . VAL A 1 205 ? 10.293  -6.784  -7.078  1.00 19.69  ? 193 VAL A N     1 
ATOM   1498 C CA    . VAL A 1 205 ? 10.586  -5.708  -6.146  1.00 19.04  ? 193 VAL A CA    1 
ATOM   1499 C C     . VAL A 1 205 ? 11.313  -4.607  -6.913  1.00 18.04  ? 193 VAL A C     1 
ATOM   1500 O O     . VAL A 1 205 ? 12.337  -4.855  -7.578  1.00 18.89  ? 193 VAL A O     1 
ATOM   1501 C CB    . VAL A 1 205 ? 11.494  -6.212  -5.029  1.00 20.53  ? 193 VAL A CB    1 
ATOM   1502 C CG1   . VAL A 1 205 ? 11.997  -5.035  -4.166  1.00 22.98  ? 193 VAL A CG1   1 
ATOM   1503 C CG2   . VAL A 1 205 ? 10.813  -7.315  -4.223  1.00 20.84  ? 193 VAL A CG2   1 
ATOM   1504 N N     . SER A 1 206 ? 10.796  -3.381  -6.808  1.00 20.46  ? 194 SER A N     1 
ATOM   1505 C CA    . SER A 1 206 ? 11.464  -2.172  -7.294  1.00 19.70  ? 194 SER A CA    1 
ATOM   1506 C C     . SER A 1 206 ? 11.590  -1.244  -6.094  1.00 20.21  ? 194 SER A C     1 
ATOM   1507 O O     . SER A 1 206 ? 10.756  -1.293  -5.192  1.00 27.33  ? 194 SER A O     1 
ATOM   1508 C CB    . SER A 1 206 ? 10.620  -1.523  -8.387  1.00 19.55  ? 194 SER A CB    1 
ATOM   1509 O OG    . SER A 1 206 ? 10.292  -2.403  -9.462  1.00 18.80  ? 194 SER A OG    1 
ATOM   1510 N N     . VAL A 1 207 ? 12.678  -0.481  -6.014  1.00 20.01  ? 195 VAL A N     1 
ATOM   1511 C CA    . VAL A 1 207 ? 12.955  0.328   -4.829  1.00 20.16  ? 195 VAL A CA    1 
ATOM   1512 C C     . VAL A 1 207 ? 12.966  1.809   -5.206  1.00 20.64  ? 195 VAL A C     1 
ATOM   1513 O O     . VAL A 1 207 ? 13.600  2.202   -6.203  1.00 20.02  ? 195 VAL A O     1 
ATOM   1514 C CB    . VAL A 1 207 ? 14.275  -0.061  -4.147  1.00 22.63  ? 195 VAL A CB    1 
ATOM   1515 C CG1   . VAL A 1 207 ? 14.548  0.859   -2.941  1.00 20.98  ? 195 VAL A CG1   1 
ATOM   1516 C CG2   . VAL A 1 207 ? 14.249  -1.560  -3.756  1.00 23.63  ? 195 VAL A CG2   1 
ATOM   1517 N N     . LEU A 1 208 ? 12.225  2.611   -4.452  1.00 19.56  ? 196 LEU A N     1 
ATOM   1518 C CA    . LEU A 1 208 ? 12.362  4.061   -4.536  1.00 20.20  ? 196 LEU A CA    1 
ATOM   1519 C C     . LEU A 1 208 ? 13.045  4.557   -3.277  1.00 22.22  ? 196 LEU A C     1 
ATOM   1520 O O     . LEU A 1 208 ? 12.800  4.049   -2.174  1.00 21.81  ? 196 LEU A O     1 
ATOM   1521 C CB    . LEU A 1 208 ? 11.001  4.728   -4.595  1.00 23.01  ? 196 LEU A CB    1 
ATOM   1522 C CG    . LEU A 1 208 ? 9.982   4.292   -5.660  1.00 20.75  ? 196 LEU A CG    1 
ATOM   1523 C CD1   . LEU A 1 208 ? 8.652   5.076   -5.524  1.00 24.16  ? 196 LEU A CD1   1 
ATOM   1524 C CD2   . LEU A 1 208 ? 10.561  4.428   -7.059  1.00 23.15  ? 196 LEU A CD2   1 
ATOM   1525 N N     . ALA A 1 209 ? 13.893  5.580   -3.429  1.00 20.35  ? 197 ALA A N     1 
ATOM   1526 C CA    . ALA A 1 209 ? 14.478  6.283   -2.305  1.00 21.50  ? 197 ALA A CA    1 
ATOM   1527 C C     . ALA A 1 209 ? 13.806  7.636   -2.192  1.00 24.39  ? 197 ALA A C     1 
ATOM   1528 O O     . ALA A 1 209 ? 13.662  8.324   -3.209  1.00 24.62  ? 197 ALA A O     1 
ATOM   1529 C CB    . ALA A 1 209 ? 15.977  6.465   -2.544  1.00 23.59  ? 197 ALA A CB    1 
ATOM   1530 N N     . VAL A 1 210 ? 13.360  7.997   -0.993  1.00 24.36  ? 198 VAL A N     1 
ATOM   1531 C CA    . VAL A 1 210 ? 12.489  9.149   -0.820  1.00 28.73  ? 198 VAL A CA    1 
ATOM   1532 C C     . VAL A 1 210 ? 13.083  10.054  0.242   1.00 30.95  ? 198 VAL A C     1 
ATOM   1533 O O     . VAL A 1 210 ? 13.444  9.597   1.330   1.00 34.52  ? 198 VAL A O     1 
ATOM   1534 C CB    . VAL A 1 210 ? 11.067  8.723   -0.415  1.00 30.74  ? 198 VAL A CB    1 
ATOM   1535 C CG1   . VAL A 1 210 ? 10.224  9.927   -0.181  1.00 34.33  ? 198 VAL A CG1   1 
ATOM   1536 C CG2   . VAL A 1 210 ? 10.460  7.831   -1.524  1.00 31.94  ? 198 VAL A CG2   1 
ATOM   1537 N N     . LYS A 1 211 ? 13.150  11.352  -0.050  1.00 32.15  ? 199 LYS A N     1 
ATOM   1538 C CA    . LYS A 1 211 ? 13.496  12.355  0.954   1.00 38.09  ? 199 LYS A CA    1 
ATOM   1539 C C     . LYS A 1 211 ? 12.820  13.663  0.570   1.00 39.89  ? 199 LYS A C     1 
ATOM   1540 O O     . LYS A 1 211 ? 13.021  14.144  -0.548  1.00 39.89  ? 199 LYS A O     1 
ATOM   1541 C CB    . LYS A 1 211 ? 15.014  12.543  1.037   1.00 41.06  ? 199 LYS A CB    1 
ATOM   1542 C CG    . LYS A 1 211 ? 15.465  13.513  2.135   1.00 48.16  ? 199 LYS A CG    1 
ATOM   1543 C CD    . LYS A 1 211 ? 16.953  13.806  2.017   1.00 51.85  ? 199 LYS A CD    1 
ATOM   1544 C CE    . LYS A 1 211 ? 17.413  14.848  3.011   1.00 49.49  ? 199 LYS A CE    1 
ATOM   1545 N NZ    . LYS A 1 211 ? 17.137  14.421  4.399   1.00 55.17  ? 199 LYS A NZ    1 
ATOM   1546 N N     . ASP A 1 212 ? 12.007  14.216  1.467   1.00 48.92  ? 200 ASP A N     1 
ATOM   1547 C CA    . ASP A 1 212 ? 11.310  15.481  1.202   1.00 51.24  ? 200 ASP A CA    1 
ATOM   1548 C C     . ASP A 1 212 ? 10.435  15.282  -0.037  1.00 46.27  ? 200 ASP A C     1 
ATOM   1549 O O     . ASP A 1 212 ? 9.726   14.267  -0.130  1.00 48.67  ? 200 ASP A O     1 
ATOM   1550 C CB    . ASP A 1 212 ? 12.333  16.613  1.140   1.00 55.71  ? 200 ASP A CB    1 
ATOM   1551 C CG    . ASP A 1 212 ? 13.025  16.849  2.476   1.00 66.82  ? 200 ASP A CG    1 
ATOM   1552 O OD1   . ASP A 1 212 ? 12.381  16.641  3.525   1.00 69.76  ? 200 ASP A OD1   1 
ATOM   1553 O OD2   . ASP A 1 212 ? 14.213  17.237  2.483   1.00 67.96  ? 200 ASP A OD2   1 
ATOM   1554 N N     . GLU A 1 213 ? 10.456  16.192  -1.004  1.00 55.52  ? 201 GLU A N     1 
ATOM   1555 C CA    . GLU A 1 213 ? 9.644   16.073  -2.208  1.00 55.22  ? 201 GLU A CA    1 
ATOM   1556 C C     . GLU A 1 213 ? 10.301  15.219  -3.279  1.00 55.84  ? 201 GLU A C     1 
ATOM   1557 O O     . GLU A 1 213 ? 9.779   15.129  -4.395  1.00 56.81  ? 201 GLU A O     1 
ATOM   1558 C CB    . GLU A 1 213 ? 9.340   17.461  -2.780  1.00 62.70  ? 201 GLU A CB    1 
ATOM   1559 C CG    . GLU A 1 213 ? 10.536  18.128  -3.457  1.00 70.33  ? 201 GLU A CG    1 
ATOM   1560 C CD    . GLU A 1 213 ? 11.635  18.500  -2.479  1.00 74.39  ? 201 GLU A CD    1 
ATOM   1561 O OE1   . GLU A 1 213 ? 11.310  19.044  -1.401  1.00 78.99  ? 201 GLU A OE1   1 
ATOM   1562 O OE2   . GLU A 1 213 ? 12.819  18.237  -2.782  1.00 73.02  ? 201 GLU A OE2   1 
ATOM   1563 N N     . ARG A 1 214 ? 11.424  14.590  -2.973  1.00 41.51  ? 202 ARG A N     1 
ATOM   1564 C CA    . ARG A 1 214 ? 12.195  13.874  -3.986  1.00 33.12  ? 202 ARG A CA    1 
ATOM   1565 C C     . ARG A 1 214 ? 11.946  12.369  -3.905  1.00 32.95  ? 202 ARG A C     1 
ATOM   1566 O O     . ARG A 1 214 ? 11.964  11.789  -2.816  1.00 36.40  ? 202 ARG A O     1 
ATOM   1567 C CB    . ARG A 1 214 ? 13.684  14.198  -3.845  1.00 44.06  ? 202 ARG A CB    1 
ATOM   1568 C CG    . ARG A 1 214 ? 14.542  13.782  -5.036  1.00 51.74  ? 202 ARG A CG    1 
ATOM   1569 C CD    . ARG A 1 214 ? 15.758  14.708  -5.251  1.00 45.45  ? 202 ARG A CD    1 
ATOM   1570 N NE    . ARG A 1 214 ? 16.798  14.023  -6.018  1.00 43.50  ? 202 ARG A NE    1 
ATOM   1571 C CZ    . ARG A 1 214 ? 16.688  13.718  -7.306  1.00 60.99  ? 202 ARG A CZ    1 
ATOM   1572 N NH1   . ARG A 1 214 ? 15.646  14.111  -8.022  1.00 67.81  ? 202 ARG A NH1   1 
ATOM   1573 N NH2   . ARG A 1 214 ? 17.635  12.981  -7.886  1.00 45.96  ? 202 ARG A NH2   1 
ATOM   1574 N N     . MET A 1 215 ? 11.682  11.746  -5.057  1.00 32.41  ? 203 MET A N     1 
ATOM   1575 C CA    . MET A 1 215 ? 11.517  10.298  -5.158  1.00 27.50  ? 203 MET A CA    1 
ATOM   1576 C C     . MET A 1 215 ? 12.461  9.852   -6.256  1.00 30.48  ? 203 MET A C     1 
ATOM   1577 O O     . MET A 1 215 ? 12.292  10.272  -7.410  1.00 31.58  ? 203 MET A O     1 
ATOM   1578 C CB    . MET A 1 215 ? 10.098  9.907   -5.589  1.00 38.35  ? 203 MET A CB    1 
ATOM   1579 C CG    . MET A 1 215 ? 8.992   10.154  -4.613  1.00 44.18  ? 203 MET A CG    1 
ATOM   1580 S SD    . MET A 1 215 ? 7.593   9.051   -5.012  1.00 41.54  ? 203 MET A SD    1 
ATOM   1581 C CE    . MET A 1 215 ? 6.437   9.669   -3.788  1.00 43.59  ? 203 MET A CE    1 
ATOM   1582 N N     . VAL A 1 216 ? 13.449  9.027   -5.899  1.00 21.24  ? 204 VAL A N     1 
ATOM   1583 C CA    . VAL A 1 216 ? 14.477  8.527   -6.817  1.00 23.51  ? 204 VAL A CA    1 
ATOM   1584 C C     . VAL A 1 216 ? 14.197  7.049   -7.108  1.00 20.34  ? 204 VAL A C     1 
ATOM   1585 O O     . VAL A 1 216 ? 13.988  6.254   -6.178  1.00 21.78  ? 204 VAL A O     1 
ATOM   1586 C CB    . VAL A 1 216 ? 15.868  8.701   -6.182  1.00 22.52  ? 204 VAL A CB    1 
ATOM   1587 C CG1   . VAL A 1 216 ? 16.931  7.919   -6.953  1.00 24.63  ? 204 VAL A CG1   1 
ATOM   1588 C CG2   . VAL A 1 216 ? 16.240  10.181  -6.132  1.00 27.63  ? 204 VAL A CG2   1 
ATOM   1589 N N     . VAL A 1 217 ? 14.186  6.693   -8.392  1.00 19.74  ? 205 VAL A N     1 
ATOM   1590 C CA    . VAL A 1 217 ? 14.092  5.294   -8.786  1.00 18.90  ? 205 VAL A CA    1 
ATOM   1591 C C     . VAL A 1 217 ? 15.460  4.635   -8.562  1.00 17.85  ? 205 VAL A C     1 
ATOM   1592 O O     . VAL A 1 217 ? 16.428  4.926   -9.271  1.00 21.10  ? 205 VAL A O     1 
ATOM   1593 C CB    . VAL A 1 217 ? 13.630  5.155   -10.235 1.00 18.32  ? 205 VAL A CB    1 
ATOM   1594 C CG1   . VAL A 1 217 ? 13.548  3.664   -10.598 1.00 21.05  ? 205 VAL A CG1   1 
ATOM   1595 C CG2   . VAL A 1 217 ? 12.290  5.844   -10.403 1.00 22.99  ? 205 VAL A CG2   1 
ATOM   1596 N N     . ARG A 1 218 ? 15.556  3.739   -7.579  1.00 17.76  ? 206 ARG A N     1 
ATOM   1597 C CA    A ARG A 1 218 ? 16.811  3.074   -7.213  0.70 19.99  ? 206 ARG A CA    1 
ATOM   1598 C CA    B ARG A 1 218 ? 16.853  3.120   -7.336  0.30 20.63  ? 206 ARG A CA    1 
ATOM   1599 C C     . ARG A 1 218 ? 16.998  1.739   -7.937  1.00 18.88  ? 206 ARG A C     1 
ATOM   1600 O O     . ARG A 1 218 ? 18.108  1.413   -8.395  1.00 21.24  ? 206 ARG A O     1 
ATOM   1601 C CB    A ARG A 1 218 ? 16.824  2.867   -5.703  0.70 21.59  ? 206 ARG A CB    1 
ATOM   1602 C CB    B ARG A 1 218 ? 17.207  3.066   -5.856  0.30 19.15  ? 206 ARG A CB    1 
ATOM   1603 C CG    A ARG A 1 218 ? 17.868  1.937   -5.136  0.70 24.68  ? 206 ARG A CG    1 
ATOM   1604 C CG    B ARG A 1 218 ? 18.590  2.485   -5.575  0.30 16.76  ? 206 ARG A CG    1 
ATOM   1605 C CD    A ARG A 1 218 ? 19.198  2.603   -4.841  0.70 19.91  ? 206 ARG A CD    1 
ATOM   1606 C CD    B ARG A 1 218 ? 18.987  2.759   -4.123  0.30 18.37  ? 206 ARG A CD    1 
ATOM   1607 N NE    A ARG A 1 218 ? 19.101  3.786   -3.986  0.70 26.21  ? 206 ARG A NE    1 
ATOM   1608 N NE    B ARG A 1 218 ? 19.237  4.187   -3.925  0.30 21.26  ? 206 ARG A NE    1 
ATOM   1609 C CZ    A ARG A 1 218 ? 19.332  5.035   -4.369  0.70 23.61  ? 206 ARG A CZ    1 
ATOM   1610 C CZ    B ARG A 1 218 ? 19.254  4.810   -2.754  0.30 20.09  ? 206 ARG A CZ    1 
ATOM   1611 N NH1   A ARG A 1 218 ? 19.603  5.348   -5.635  0.70 26.01  ? 206 ARG A NH1   1 
ATOM   1612 N NH1   B ARG A 1 218 ? 18.983  4.180   -1.622  0.30 20.19  ? 206 ARG A NH1   1 
ATOM   1613 N NH2   A ARG A 1 218 ? 19.309  6.005   -3.447  0.70 26.00  ? 206 ARG A NH2   1 
ATOM   1614 N NH2   B ARG A 1 218 ? 19.559  6.105   -2.717  0.30 21.02  ? 206 ARG A NH2   1 
ATOM   1615 N N     . SER A 1 219 ? 15.928  0.961   -8.001  1.00 20.17  ? 207 SER A N     1 
ATOM   1616 C CA    . SER A 1 219 ? 16.052  -0.333  -8.680  1.00 18.24  ? 207 SER A CA    1 
ATOM   1617 C C     . SER A 1 219 ? 14.688  -0.740  -9.208  1.00 19.77  ? 207 SER A C     1 
ATOM   1618 O O     . SER A 1 219 ? 13.645  -0.268  -8.725  1.00 19.38  ? 207 SER A O     1 
ATOM   1619 C CB    . SER A 1 219 ? 16.616  -1.416  -7.757  1.00 20.19  ? 207 SER A CB    1 
ATOM   1620 O OG    . SER A 1 219 ? 15.846  -1.605  -6.596  1.00 22.21  ? 207 SER A OG    1 
ATOM   1621 N N     . ILE A 1 220 ? 14.677  -1.595  -10.237 1.00 18.75  ? 208 ILE A N     1 
ATOM   1622 C CA    . ILE A 1 220 ? 13.433  -1.877  -10.950 1.00 16.63  ? 208 ILE A CA    1 
ATOM   1623 C C     . ILE A 1 220 ? 13.303  -3.375  -11.235 1.00 18.51  ? 208 ILE A C     1 
ATOM   1624 O O     . ILE A 1 220 ? 14.192  -3.954  -11.866 1.00 18.48  ? 208 ILE A O     1 
ATOM   1625 C CB    . ILE A 1 220 ? 13.384  -1.159  -12.299 1.00 17.36  ? 208 ILE A CB    1 
ATOM   1626 C CG1   . ILE A 1 220 ? 13.595  0.370   -12.129 1.00 19.17  ? 208 ILE A CG1   1 
ATOM   1627 C CG2   . ILE A 1 220 ? 12.035  -1.424  -12.940 1.00 19.49  ? 208 ILE A CG2   1 
ATOM   1628 C CD1   . ILE A 1 220 ? 13.729  1.144   -13.420 1.00 21.80  ? 208 ILE A CD1   1 
ATOM   1629 N N     . GLY A 1 221 ? 12.157  -3.980  -10.890 1.00 18.39  ? 209 GLY A N     1 
ATOM   1630 C CA    . GLY A 1 221 ? 11.763  -5.238  -11.524 1.00 17.20  ? 209 GLY A CA    1 
ATOM   1631 C C     . GLY A 1 221 ? 12.402  -6.529  -11.036 1.00 15.65  ? 209 GLY A C     1 
ATOM   1632 O O     . GLY A 1 221 ? 12.312  -7.512  -11.769 1.00 18.79  ? 209 GLY A O     1 
ATOM   1633 N N     . ASP A 1 222 ? 12.981  -6.561  -9.865  1.00 16.72  ? 210 ASP A N     1 
ATOM   1634 C CA    . ASP A 1 222 ? 13.764  -7.744  -9.460  1.00 16.05  ? 210 ASP A CA    1 
ATOM   1635 C C     . ASP A 1 222 ? 12.845  -8.845  -8.892  1.00 18.36  ? 210 ASP A C     1 
ATOM   1636 O O     . ASP A 1 222 ? 12.252  -8.677  -7.826  1.00 17.43  ? 210 ASP A O     1 
ATOM   1637 C CB    . ASP A 1 222 ? 14.831  -7.312  -8.455  1.00 16.36  ? 210 ASP A CB    1 
ATOM   1638 C CG    . ASP A 1 222 ? 15.722  -8.455  -8.018  1.00 17.61  ? 210 ASP A CG    1 
ATOM   1639 O OD1   . ASP A 1 222 ? 15.187  -9.451  -7.457  1.00 19.51  ? 210 ASP A OD1   1 
ATOM   1640 O OD2   . ASP A 1 222 ? 16.944  -8.396  -8.251  1.00 19.81  ? 210 ASP A OD2   1 
ATOM   1641 N N     . ALA A 1 223 ? 12.826  -10.005 -9.567  1.00 18.32  ? 211 ALA A N     1 
ATOM   1642 C CA    . ALA A 1 223 ? 12.098  -11.183 -9.094  1.00 19.26  ? 211 ALA A CA    1 
ATOM   1643 C C     . ALA A 1 223 ? 13.056  -12.360 -8.908  1.00 20.48  ? 211 ALA A C     1 
ATOM   1644 O O     . ALA A 1 223 ? 12.725  -13.525 -9.183  1.00 22.01  ? 211 ALA A O     1 
ATOM   1645 C CB    . ALA A 1 223 ? 10.910  -11.535 -10.001 1.00 21.32  ? 211 ALA A CB    1 
ATOM   1646 N N     . THR A 1 224 ? 14.268  -12.045 -8.471  1.00 19.89  ? 212 THR A N     1 
ATOM   1647 C CA    . THR A 1 224 ? 15.315  -13.051 -8.398  1.00 18.86  ? 212 THR A CA    1 
ATOM   1648 C C     . THR A 1 224 ? 15.052  -14.119 -7.346  1.00 20.46  ? 212 THR A C     1 
ATOM   1649 O O     . THR A 1 224 ? 15.689  -15.180 -7.384  1.00 22.71  ? 212 THR A O     1 
ATOM   1650 C CB    . THR A 1 224 ? 16.694  -12.394 -8.217  1.00 20.78  ? 212 THR A CB    1 
ATOM   1651 O OG1   . THR A 1 224 ? 16.727  -11.600 -7.037  1.00 21.83  ? 212 THR A OG1   1 
ATOM   1652 C CG2   . THR A 1 224 ? 17.162  -11.579 -9.442  1.00 21.42  ? 212 THR A CG2   1 
ATOM   1653 N N     . HIS A 1 225 ? 14.123  -13.886 -6.405  1.00 20.89  ? 213 HIS A N     1 
ATOM   1654 C CA    . HIS A 1 225 ? 13.722  -14.968 -5.503  1.00 21.94  ? 213 HIS A CA    1 
ATOM   1655 C C     . HIS A 1 225 ? 13.033  -16.133 -6.222  1.00 23.87  ? 213 HIS A C     1 
ATOM   1656 O O     . HIS A 1 225 ? 12.888  -17.191 -5.634  1.00 26.68  ? 213 HIS A O     1 
ATOM   1657 C CB    . HIS A 1 225 ? 12.758  -14.427 -4.417  1.00 22.00  ? 213 HIS A CB    1 
ATOM   1658 C CG    . HIS A 1 225 ? 11.618  -13.628 -4.977  1.00 21.15  ? 213 HIS A CG    1 
ATOM   1659 N ND1   . HIS A 1 225 ? 11.787  -12.316 -5.369  1.00 21.30  ? 213 HIS A ND1   1 
ATOM   1660 C CD2   . HIS A 1 225 ? 10.337  -13.971 -5.266  1.00 22.47  ? 213 HIS A CD2   1 
ATOM   1661 C CE1   . HIS A 1 225 ? 10.625  -11.875 -5.833  1.00 21.29  ? 213 HIS A CE1   1 
ATOM   1662 N NE2   . HIS A 1 225 ? 9.743   -12.856 -5.815  1.00 20.83  ? 213 HIS A NE2   1 
ATOM   1663 N N     . LEU A 1 226 ? 12.624  -15.957 -7.480  1.00 23.08  ? 214 LEU A N     1 
ATOM   1664 C CA    . LEU A 1 226 ? 12.050  -17.041 -8.261  1.00 25.43  ? 214 LEU A CA    1 
ATOM   1665 C C     . LEU A 1 226 ? 13.102  -17.829 -9.035  1.00 27.01  ? 214 LEU A C     1 
ATOM   1666 O O     . LEU A 1 226 ? 12.767  -18.800 -9.703  1.00 29.49  ? 214 LEU A O     1 
ATOM   1667 C CB    . LEU A 1 226 ? 11.024  -16.454 -9.233  1.00 24.89  ? 214 LEU A CB    1 
ATOM   1668 C CG    . LEU A 1 226 ? 9.884   -15.653 -8.602  1.00 24.46  ? 214 LEU A CG    1 
ATOM   1669 C CD1   . LEU A 1 226 ? 8.957   -15.178 -9.721  1.00 29.19  ? 214 LEU A CD1   1 
ATOM   1670 C CD2   . LEU A 1 226 ? 9.144   -16.432 -7.522  1.00 27.65  ? 214 LEU A CD2   1 
ATOM   1671 N N     . ALA A 1 227 ? 14.370  -17.400 -9.004  1.00 26.02  ? 215 ALA A N     1 
ATOM   1672 C CA    . ALA A 1 227 ? 15.367  -18.008 -9.891  1.00 28.86  ? 215 ALA A CA    1 
ATOM   1673 C C     . ALA A 1 227 ? 15.563  -19.486 -9.632  1.00 37.36  ? 215 ALA A C     1 
ATOM   1674 O O     . ALA A 1 227 ? 15.741  -20.263 -10.575 1.00 42.41  ? 215 ALA A O     1 
ATOM   1675 C CB    . ALA A 1 227 ? 16.689  -17.242 -9.798  1.00 30.24  ? 215 ALA A CB    1 
ATOM   1676 N N     . ALA A 1 228 ? 15.529  -19.902 -8.379  1.00 36.99  ? 216 ALA A N     1 
ATOM   1677 C CA    . ALA A 1 228 ? 15.739  -21.315 -8.065  1.00 47.86  ? 216 ALA A CA    1 
ATOM   1678 C C     . ALA A 1 228 ? 14.455  -22.154 -8.123  1.00 39.91  ? 216 ALA A C     1 
ATOM   1679 O O     . ALA A 1 228 ? 14.519  -23.381 -7.955  1.00 49.31  ? 216 ALA A O     1 
ATOM   1680 C CB    . ALA A 1 228 ? 16.424  -21.444 -6.702  1.00 51.56  ? 216 ALA A CB    1 
ATOM   1681 N N     . ALA A 1 229 ? 13.312  -21.522 -8.410  1.00 44.38  ? 217 ALA A N     1 
ATOM   1682 C CA    . ALA A 1 229 ? 11.990  -22.128 -8.266  1.00 40.49  ? 217 ALA A CA    1 
ATOM   1683 C C     . ALA A 1 229 ? 11.710  -23.148 -9.373  1.00 53.34  ? 217 ALA A C     1 
ATOM   1684 O O     . ALA A 1 229 ? 12.391  -23.173 -10.402 1.00 49.19  ? 217 ALA A O     1 
ATOM   1685 C CB    . ALA A 1 229 ? 10.936  -21.023 -8.315  1.00 39.90  ? 217 ALA A CB    1 
ATOM   1686 N N     . PRO A 1 230 ? 10.702  -24.001 -9.185  1.00 48.89  ? 218 PRO A N     1 
ATOM   1687 C CA    . PRO A 1 230 ? 10.321  -24.943 -10.248 1.00 53.20  ? 218 PRO A CA    1 
ATOM   1688 C C     . PRO A 1 230 ? 9.764   -24.216 -11.468 1.00 64.31  ? 218 PRO A C     1 
ATOM   1689 O O     . PRO A 1 230 ? 9.446   -23.023 -11.439 1.00 63.58  ? 218 PRO A O     1 
ATOM   1690 C CB    . PRO A 1 230 ? 9.251   -25.815 -9.582  1.00 60.37  ? 218 PRO A CB    1 
ATOM   1691 C CG    . PRO A 1 230 ? 9.551   -25.726 -8.126  1.00 55.16  ? 218 PRO A CG    1 
ATOM   1692 C CD    . PRO A 1 230 ? 10.021  -24.313 -7.916  1.00 53.24  ? 218 PRO A CD    1 
ATOM   1693 N N     . SER A 1 231 ? 9.649   -24.973 -12.565 1.00 72.50  ? 219 SER A N     1 
ATOM   1694 C CA    . SER A 1 231 ? 9.196   -24.402 -13.832 1.00 77.45  ? 219 SER A CA    1 
ATOM   1695 C C     . SER A 1 231 ? 7.738   -23.955 -13.774 1.00 70.47  ? 219 SER A C     1 
ATOM   1696 O O     . SER A 1 231 ? 7.358   -22.993 -14.456 1.00 72.31  ? 219 SER A O     1 
ATOM   1697 C CB    . SER A 1 231 ? 9.410   -25.403 -14.974 1.00 71.61  ? 219 SER A CB    1 
ATOM   1698 O OG    . SER A 1 231 ? 8.542   -26.522 -14.863 1.00 73.42  ? 219 SER A OG    1 
ATOM   1699 N N     . ASP A 1 232 ? 6.909   -24.633 -12.977 1.00 71.17  ? 220 ASP A N     1 
ATOM   1700 C CA    . ASP A 1 232 ? 5.510   -24.255 -12.806 1.00 71.47  ? 220 ASP A CA    1 
ATOM   1701 C C     . ASP A 1 232 ? 5.315   -23.114 -11.801 1.00 67.74  ? 220 ASP A C     1 
ATOM   1702 O O     . ASP A 1 232 ? 4.181   -22.835 -11.397 1.00 73.41  ? 220 ASP A O     1 
ATOM   1703 C CB    . ASP A 1 232 ? 4.649   -25.481 -12.459 1.00 68.91  ? 220 ASP A CB    1 
ATOM   1704 C CG    . ASP A 1 232 ? 5.096   -26.183 -11.187 1.00 72.59  ? 220 ASP A CG    1 
ATOM   1705 O OD1   . ASP A 1 232 ? 6.058   -25.723 -10.533 1.00 80.49  ? 220 ASP A OD1   1 
ATOM   1706 O OD2   . ASP A 1 232 ? 4.471   -27.206 -10.839 1.00 70.08  ? 220 ASP A OD2   1 
ATOM   1707 N N     . VAL A 1 233 ? 6.392   -22.443 -11.397 1.00 53.81  ? 221 VAL A N     1 
ATOM   1708 C CA    . VAL A 1 233 ? 6.318   -21.335 -10.455 1.00 46.82  ? 221 VAL A CA    1 
ATOM   1709 C C     . VAL A 1 233 ? 6.902   -20.048 -11.021 1.00 54.55  ? 221 VAL A C     1 
ATOM   1710 O O     . VAL A 1 233 ? 6.373   -18.961 -10.764 1.00 51.30  ? 221 VAL A O     1 
ATOM   1711 C CB    . VAL A 1 233 ? 6.955   -21.695 -9.096  1.00 48.17  ? 221 VAL A CB    1 
ATOM   1712 C CG1   . VAL A 1 233 ? 7.001   -20.481 -8.174  1.00 39.20  ? 221 VAL A CG1   1 
ATOM   1713 C CG2   . VAL A 1 233 ? 6.152   -22.818 -8.451  1.00 48.43  ? 221 VAL A CG2   1 
ATOM   1714 N N     . ILE A 1 234 ? 7.983   -20.136 -11.794 1.00 62.88  ? 222 ILE A N     1 
ATOM   1715 C CA    . ILE A 1 234 ? 8.655   -18.932 -12.307 1.00 59.97  ? 222 ILE A CA    1 
ATOM   1716 C C     . ILE A 1 234 ? 7.736   -18.081 -13.189 1.00 63.01  ? 222 ILE A C     1 
ATOM   1717 O O     . ILE A 1 234 ? 6.934   -18.604 -13.961 1.00 65.91  ? 222 ILE A O     1 
ATOM   1718 C CB    . ILE A 1 234 ? 9.974   -19.279 -13.035 1.00 66.67  ? 222 ILE A CB    1 
ATOM   1719 C CG1   . ILE A 1 234 ? 10.829  -20.205 -12.171 1.00 59.75  ? 222 ILE A CG1   1 
ATOM   1720 C CG2   . ILE A 1 234 ? 10.758  -18.005 -13.381 1.00 55.71  ? 222 ILE A CG2   1 
ATOM   1721 C CD1   . ILE A 1 234 ? 12.008  -20.812 -12.903 1.00 64.39  ? 222 ILE A CD1   1 
ATOM   1722 O OXT   . ILE A 1 234 ? 7.772   -16.846 -13.160 1.00 58.98  ? 222 ILE A OXT   1 
ATOM   1723 N N     . MET B 1 13  ? -19.226 -6.847  -27.096 1.00 77.28  ? 1   MET B N     1 
ATOM   1724 C CA    . MET B 1 13  ? -19.750 -8.234  -27.121 1.00 69.78  ? 1   MET B CA    1 
ATOM   1725 C C     . MET B 1 13  ? -19.770 -8.804  -25.689 1.00 64.14  ? 1   MET B C     1 
ATOM   1726 O O     . MET B 1 13  ? -20.043 -8.016  -24.801 1.00 63.07  ? 1   MET B O     1 
ATOM   1727 C CB    . MET B 1 13  ? -19.025 -9.115  -28.147 1.00 80.77  ? 1   MET B CB    1 
ATOM   1728 C CG    . MET B 1 13  ? -19.943 -10.055 -28.926 1.00 68.02  ? 1   MET B CG    1 
ATOM   1729 S SD    . MET B 1 13  ? -20.234 -9.725  -30.693 1.00 87.26  ? 1   MET B SD    1 
ATOM   1730 C CE    . MET B 1 13  ? -21.600 -10.849 -30.981 1.00 55.89  ? 1   MET B CE    1 
ATOM   1731 N N     . SER B 1 14  ? -19.308 -10.030 -25.437 1.00 70.57  ? 2   SER B N     1 
ATOM   1732 C CA    . SER B 1 14  ? -19.588 -10.675 -24.124 1.00 58.79  ? 2   SER B CA    1 
ATOM   1733 C C     . SER B 1 14  ? -18.557 -10.549 -22.996 1.00 58.69  ? 2   SER B C     1 
ATOM   1734 O O     . SER B 1 14  ? -18.583 -9.572  -22.278 1.00 53.53  ? 2   SER B O     1 
ATOM   1735 C CB    . SER B 1 14  ? -19.951 -12.109 -24.332 1.00 62.29  ? 2   SER B CB    1 
ATOM   1736 O OG    . SER B 1 14  ? -20.937 -12.473 -23.393 1.00 66.05  ? 2   SER B OG    1 
ATOM   1737 N N     . ASP B 1 15  ? -17.847 -11.648 -22.730 1.00 54.87  ? 3   ASP B N     1 
ATOM   1738 C CA    . ASP B 1 15  ? -16.834 -11.758 -21.650 1.00 46.43  ? 3   ASP B CA    1 
ATOM   1739 C C     . ASP B 1 15  ? -15.468 -11.477 -22.284 1.00 53.66  ? 3   ASP B C     1 
ATOM   1740 O O     . ASP B 1 15  ? -15.035 -12.273 -23.114 1.00 55.54  ? 3   ASP B O     1 
ATOM   1741 C CB    . ASP B 1 15  ? -16.883 -13.154 -21.012 1.00 46.51  ? 3   ASP B CB    1 
ATOM   1742 C CG    . ASP B 1 15  ? -16.036 -13.323 -19.766 1.00 42.89  ? 3   ASP B CG    1 
ATOM   1743 O OD1   . ASP B 1 15  ? -14.911 -12.858 -19.771 1.00 40.12  ? 3   ASP B OD1   1 
ATOM   1744 O OD2   . ASP B 1 15  ? -16.489 -13.957 -18.822 1.00 48.02  ? 3   ASP B OD2   1 
ATOM   1745 N N     . GLY B 1 16  ? -14.814 -10.398 -21.867 1.00 45.43  ? 4   GLY B N     1 
ATOM   1746 C CA    . GLY B 1 16  ? -13.532 -10.044 -22.496 1.00 37.58  ? 4   GLY B CA    1 
ATOM   1747 C C     . GLY B 1 16  ? -12.328 -10.710 -21.866 1.00 33.62  ? 4   GLY B C     1 
ATOM   1748 O O     . GLY B 1 16  ? -11.246 -10.257 -22.161 1.00 31.16  ? 4   GLY B O     1 
ATOM   1749 N N     . ARG B 1 17  ? -12.489 -11.750 -21.055 1.00 34.27  ? 5   ARG B N     1 
ATOM   1750 C CA    . ARG B 1 17  ? -11.301 -12.305 -20.404 1.00 31.71  ? 5   ARG B CA    1 
ATOM   1751 C C     . ARG B 1 17  ? -10.361 -12.980 -21.403 1.00 29.24  ? 5   ARG B C     1 
ATOM   1752 O O     . ARG B 1 17  ? -9.141  -12.873 -21.271 1.00 30.72  ? 5   ARG B O     1 
ATOM   1753 C CB    . ARG B 1 17  ? -11.675 -13.242 -19.241 1.00 33.14  ? 5   ARG B CB    1 
ATOM   1754 C CG    . ARG B 1 17  ? -11.993 -14.689 -19.606 1.00 40.73  ? 5   ARG B CG    1 
ATOM   1755 C CD    . ARG B 1 17  ? -12.312 -15.528 -18.361 1.00 39.82  ? 5   ARG B CD    1 
ATOM   1756 N NE    . ARG B 1 17  ? -13.647 -15.222 -17.856 1.00 42.61  ? 5   ARG B NE    1 
ATOM   1757 C CZ    . ARG B 1 17  ? -14.163 -15.697 -16.731 1.00 40.37  ? 5   ARG B CZ    1 
ATOM   1758 N NH1   . ARG B 1 17  ? -13.483 -16.524 -15.951 1.00 43.99  ? 5   ARG B NH1   1 
ATOM   1759 N NH2   . ARG B 1 17  ? -15.411 -15.366 -16.398 1.00 42.50  ? 5   ARG B NH2   1 
ATOM   1760 N N     . GLU B 1 18  ? -10.895 -13.681 -22.405 1.00 33.81  ? 6   GLU B N     1 
ATOM   1761 C CA    . GLU B 1 18  ? -10.018 -14.332 -23.381 1.00 31.12  ? 6   GLU B CA    1 
ATOM   1762 C C     . GLU B 1 18  ? -9.241  -13.311 -24.203 1.00 29.04  ? 6   GLU B C     1 
ATOM   1763 O O     . GLU B 1 18  ? -8.048  -13.487 -24.445 1.00 29.25  ? 6   GLU B O     1 
ATOM   1764 C CB    . GLU B 1 18  ? -10.829 -15.275 -24.277 1.00 38.91  ? 6   GLU B CB    1 
ATOM   1765 C CG    . GLU B 1 18  ? -11.357 -16.512 -23.554 1.00 53.36  ? 6   GLU B CG    1 
ATOM   1766 C CD    . GLU B 1 18  ? -10.276 -17.560 -23.268 1.00 73.41  ? 6   GLU B CD    1 
ATOM   1767 O OE1   . GLU B 1 18  ? -9.076  -17.287 -23.506 1.00 64.82  ? 6   GLU B OE1   1 
ATOM   1768 O OE2   . GLU B 1 18  ? -10.632 -18.672 -22.811 1.00 77.40  ? 6   GLU B OE2   1 
ATOM   1769 N N     . SER B 1 19  ? -9.895  -12.245 -24.641 1.00 30.68  ? 7   SER B N     1 
ATOM   1770 C CA    . SER B 1 19  ? -9.210  -11.174 -25.362 1.00 29.28  ? 7   SER B CA    1 
ATOM   1771 C C     . SER B 1 19  ? -8.096  -10.573 -24.515 1.00 27.87  ? 7   SER B C     1 
ATOM   1772 O O     . SER B 1 19  ? -6.943  -10.427 -24.962 1.00 28.94  ? 7   SER B O     1 
ATOM   1773 C CB    . SER B 1 19  ? -10.268 -10.121 -25.716 1.00 36.59  ? 7   SER B CB    1 
ATOM   1774 O OG    . SER B 1 19  ? -9.687  -8.993  -26.337 1.00 39.91  ? 7   SER B OG    1 
ATOM   1775 N N     . PHE B 1 20  ? -8.410  -10.282 -23.253 1.00 26.97  ? 8   PHE B N     1 
ATOM   1776 C CA    . PHE B 1 20  ? -7.412  -9.791  -22.314 1.00 24.73  ? 8   PHE B CA    1 
ATOM   1777 C C     . PHE B 1 20  ? -6.224  -10.741 -22.195 1.00 24.28  ? 8   PHE B C     1 
ATOM   1778 O O     . PHE B 1 20  ? -5.064  -10.307 -22.247 1.00 26.09  ? 8   PHE B O     1 
ATOM   1779 C CB    . PHE B 1 20  ? -8.061  -9.557  -20.946 1.00 26.94  ? 8   PHE B CB    1 
ATOM   1780 C CG    . PHE B 1 20  ? -7.064  -9.068  -19.904 1.00 27.37  ? 8   PHE B CG    1 
ATOM   1781 C CD1   . PHE B 1 20  ? -6.751  -7.718  -19.827 1.00 33.51  ? 8   PHE B CD1   1 
ATOM   1782 C CD2   . PHE B 1 20  ? -6.461  -9.951  -19.022 1.00 32.12  ? 8   PHE B CD2   1 
ATOM   1783 C CE1   . PHE B 1 20  ? -5.858  -7.243  -18.884 1.00 35.02  ? 8   PHE B CE1   1 
ATOM   1784 C CE2   . PHE B 1 20  ? -5.553  -9.491  -18.075 1.00 40.32  ? 8   PHE B CE2   1 
ATOM   1785 C CZ    . PHE B 1 20  ? -5.252  -8.134  -18.008 1.00 35.30  ? 8   PHE B CZ    1 
ATOM   1786 N N     . LEU B 1 21  ? -6.483  -12.036 -22.027 1.00 26.96  ? 9   LEU B N     1 
ATOM   1787 C CA    . LEU B 1 21  ? -5.382  -12.957 -21.807 1.00 28.07  ? 9   LEU B CA    1 
ATOM   1788 C C     . LEU B 1 21  ? -4.581  -13.184 -23.067 1.00 24.69  ? 9   LEU B C     1 
ATOM   1789 O O     . LEU B 1 21  ? -3.355  -13.377 -22.980 1.00 28.26  ? 9   LEU B O     1 
ATOM   1790 C CB    . LEU B 1 21  ? -5.906  -14.280 -21.278 1.00 29.04  ? 9   LEU B CB    1 
ATOM   1791 C CG    . LEU B 1 21  ? -6.582  -14.232 -19.911 1.00 33.56  ? 9   LEU B CG    1 
ATOM   1792 C CD1   . LEU B 1 21  ? -7.235  -15.579 -19.644 1.00 33.09  ? 9   LEU B CD1   1 
ATOM   1793 C CD2   . LEU B 1 21  ? -5.611  -13.903 -18.820 1.00 35.44  ? 9   LEU B CD2   1 
ATOM   1794 N N     . GLU B 1 22  ? -5.219  -13.144 -24.230 1.00 26.86  ? 10  GLU B N     1 
ATOM   1795 C CA    . GLU B 1 22  ? -4.470  -13.269 -25.482 1.00 28.70  ? 10  GLU B CA    1 
ATOM   1796 C C     . GLU B 1 22  ? -3.515  -12.094 -25.647 1.00 26.71  ? 10  GLU B C     1 
ATOM   1797 O O     . GLU B 1 22  ? -2.349  -12.277 -26.008 1.00 27.74  ? 10  GLU B O     1 
ATOM   1798 C CB    . GLU B 1 22  ? -5.433  -13.344 -26.664 1.00 32.33  ? 10  GLU B CB    1 
ATOM   1799 C CG    . GLU B 1 22  ? -4.772  -13.673 -27.995 1.00 46.23  ? 10  GLU B CG    1 
ATOM   1800 C CD    . GLU B 1 22  ? -5.733  -14.361 -28.961 1.00 68.95  ? 10  GLU B CD    1 
ATOM   1801 O OE1   . GLU B 1 22  ? -6.954  -14.386 -28.678 1.00 70.09  ? 10  GLU B OE1   1 
ATOM   1802 O OE2   . GLU B 1 22  ? -5.269  -14.889 -29.997 1.00 78.65  ? 10  GLU B OE2   1 
ATOM   1803 N N     . VAL B 1 23  ? -3.979  -10.876 -25.357 1.00 26.81  ? 11  VAL B N     1 
ATOM   1804 C CA    . VAL B 1 23  ? -3.092  -9.715  -25.439 1.00 28.03  ? 11  VAL B CA    1 
ATOM   1805 C C     . VAL B 1 23  ? -1.991  -9.795  -24.379 1.00 25.25  ? 11  VAL B C     1 
ATOM   1806 O O     . VAL B 1 23  ? -0.798  -9.565  -24.676 1.00 24.92  ? 11  VAL B O     1 
ATOM   1807 C CB    . VAL B 1 23  ? -3.916  -8.423  -25.342 1.00 23.30  ? 11  VAL B CB    1 
ATOM   1808 C CG1   . VAL B 1 23  ? -2.968  -7.206  -25.228 1.00 26.53  ? 11  VAL B CG1   1 
ATOM   1809 C CG2   . VAL B 1 23  ? -4.734  -8.272  -26.538 1.00 29.53  ? 11  VAL B CG2   1 
ATOM   1810 N N     . MET B 1 24  ? -2.347  -10.177 -23.147 1.00 26.33  ? 12  MET B N     1 
ATOM   1811 C CA    . MET B 1 24  ? -1.359  -10.303 -22.081 1.00 27.25  ? 12  MET B CA    1 
ATOM   1812 C C     . MET B 1 24  ? -0.250  -11.274 -22.475 1.00 27.79  ? 12  MET B C     1 
ATOM   1813 O O     . MET B 1 24  ? 0.930   -11.012 -22.225 1.00 26.79  ? 12  MET B O     1 
ATOM   1814 C CB    . MET B 1 24  ? -2.023  -10.785 -20.795 1.00 32.59  ? 12  MET B CB    1 
ATOM   1815 C CG    . MET B 1 24  ? -1.072  -10.821 -19.610 1.00 37.14  ? 12  MET B CG    1 
ATOM   1816 S SD    . MET B 1 24  ? -1.801  -11.515 -18.148 1.00 56.73  ? 12  MET B SD    1 
ATOM   1817 C CE    . MET B 1 24  ? -1.962  -13.231 -18.634 1.00 53.63  ? 12  MET B CE    1 
ATOM   1818 N N     . ARG B 1 25  ? -0.606  -12.401 -23.094 1.00 26.44  ? 13  ARG B N     1 
ATOM   1819 C CA    . ARG B 1 25  ? 0.405   -13.362 -23.527 1.00 26.35  ? 13  ARG B CA    1 
ATOM   1820 C C     . ARG B 1 25  ? 1.270   -12.775 -24.631 1.00 28.67  ? 13  ARG B C     1 
ATOM   1821 O O     . ARG B 1 25  ? 2.489   -12.982 -24.647 1.00 29.84  ? 13  ARG B O     1 
ATOM   1822 C CB    . ARG B 1 25  ? -0.302  -14.635 -23.976 1.00 28.25  ? 13  ARG B CB    1 
ATOM   1823 C CG    . ARG B 1 25  ? 0.599   -15.762 -24.427 1.00 37.73  ? 13  ARG B CG    1 
ATOM   1824 C CD    . ARG B 1 25  ? -0.228  -17.046 -24.694 1.00 50.83  ? 13  ARG B CD    1 
ATOM   1825 N NE    . ARG B 1 25  ? -1.659  -16.809 -24.916 1.00 65.99  ? 13  ARG B NE    1 
ATOM   1826 C CZ    . ARG B 1 25  ? -2.635  -17.151 -24.076 1.00 61.27  ? 13  ARG B CZ    1 
ATOM   1827 N NH1   . ARG B 1 25  ? -2.379  -17.727 -22.911 1.00 62.90  ? 13  ARG B NH1   1 
ATOM   1828 N NH2   . ARG B 1 25  ? -3.904  -16.920 -24.419 1.00 40.52  ? 13  ARG B NH2   1 
ATOM   1829 N N     . SER B 1 26  ? 0.673   -12.022 -25.552 1.00 27.17  ? 14  SER B N     1 
ATOM   1830 C CA    . SER B 1 26  ? 1.434   -11.422 -26.641 1.00 26.27  ? 14  SER B CA    1 
ATOM   1831 C C     . SER B 1 26  ? 2.431   -10.394 -26.107 1.00 29.12  ? 14  SER B C     1 
ATOM   1832 O O     . SER B 1 26  ? 3.578   -10.315 -26.581 1.00 27.87  ? 14  SER B O     1 
ATOM   1833 C CB    . SER B 1 26  ? 0.481   -10.774 -27.641 1.00 32.00  ? 14  SER B CB    1 
ATOM   1834 O OG    . SER B 1 26  ? -0.230  -11.776 -28.341 1.00 36.69  ? 14  SER B OG    1 
ATOM   1835 N N     . VAL B 1 27  ? 2.027   -9.620  -25.103 1.00 25.12  ? 15  VAL B N     1 
ATOM   1836 C CA    . VAL B 1 27  ? 2.936   -8.657  -24.483 1.00 23.64  ? 15  VAL B CA    1 
ATOM   1837 C C     . VAL B 1 27  ? 4.067   -9.387  -23.785 1.00 26.76  ? 15  VAL B C     1 
ATOM   1838 O O     . VAL B 1 27  ? 5.246   -9.086  -24.012 1.00 27.58  ? 15  VAL B O     1 
ATOM   1839 C CB    . VAL B 1 27  ? 2.155   -7.750  -23.508 1.00 23.92  ? 15  VAL B CB    1 
ATOM   1840 C CG1   . VAL B 1 27  ? 3.106   -6.865  -22.645 1.00 25.28  ? 15  VAL B CG1   1 
ATOM   1841 C CG2   . VAL B 1 27  ? 1.162   -6.864  -24.264 1.00 24.85  ? 15  VAL B CG2   1 
ATOM   1842 N N     . TYR B 1 28  ? 3.737   -10.385 -22.953 1.00 26.34  ? 16  TYR B N     1 
ATOM   1843 C CA    . TYR B 1 28  ? 4.770   -11.157 -22.268 1.00 29.10  ? 16  TYR B CA    1 
ATOM   1844 C C     . TYR B 1 28  ? 5.796   -11.702 -23.254 1.00 32.25  ? 16  TYR B C     1 
ATOM   1845 O O     . TYR B 1 28  ? 7.005   -11.628 -23.014 1.00 29.28  ? 16  TYR B O     1 
ATOM   1846 C CB    . TYR B 1 28  ? 4.130   -12.308 -21.487 1.00 33.40  ? 16  TYR B CB    1 
ATOM   1847 C CG    . TYR B 1 28  ? 3.794   -12.030 -20.023 1.00 33.94  ? 16  TYR B CG    1 
ATOM   1848 C CD1   . TYR B 1 28  ? 4.644   -11.290 -19.202 1.00 39.30  ? 16  TYR B CD1   1 
ATOM   1849 C CD2   . TYR B 1 28  ? 2.632   -12.548 -19.459 1.00 40.78  ? 16  TYR B CD2   1 
ATOM   1850 C CE1   . TYR B 1 28  ? 4.334   -11.057 -17.864 1.00 32.55  ? 16  TYR B CE1   1 
ATOM   1851 C CE2   . TYR B 1 28  ? 2.314   -12.328 -18.130 1.00 33.17  ? 16  TYR B CE2   1 
ATOM   1852 C CZ    . TYR B 1 28  ? 3.167   -11.579 -17.341 1.00 32.85  ? 16  TYR B CZ    1 
ATOM   1853 O OH    . TYR B 1 28  ? 2.835   -11.406 -16.028 1.00 36.16  ? 16  TYR B OH    1 
ATOM   1854 N N     . GLU B 1 29  ? 5.335   -12.255 -24.381 1.00 27.41  ? 17  GLU B N     1 
ATOM   1855 C CA    . GLU B 1 29  ? 6.268   -12.843 -25.334 1.00 30.32  ? 17  GLU B CA    1 
ATOM   1856 C C     . GLU B 1 29  ? 7.202   -11.799 -25.940 1.00 27.82  ? 17  GLU B C     1 
ATOM   1857 O O     . GLU B 1 29  ? 8.374   -12.096 -26.220 1.00 29.93  ? 17  GLU B O     1 
ATOM   1858 C CB    . GLU B 1 29  ? 5.498   -13.627 -26.405 1.00 34.97  ? 17  GLU B CB    1 
ATOM   1859 C CG    . GLU B 1 29  ? 4.815   -14.869 -25.847 1.00 49.81  ? 17  GLU B CG    1 
ATOM   1860 C CD    . GLU B 1 29  ? 4.044   -15.646 -26.895 1.00 63.10  ? 17  GLU B CD    1 
ATOM   1861 O OE1   . GLU B 1 29  ? 4.038   -15.212 -28.071 1.00 68.78  ? 17  GLU B OE1   1 
ATOM   1862 O OE2   . GLU B 1 29  ? 3.444   -16.686 -26.534 1.00 56.20  ? 17  GLU B OE2   1 
ATOM   1863 N N     . ARG B 1 30  ? 6.734   -10.564 -26.095 1.00 28.34  ? 18  ARG B N     1 
ATOM   1864 C CA    . ARG B 1 30  ? 7.585   -9.517  -26.633 1.00 28.49  ? 18  ARG B CA    1 
ATOM   1865 C C     . ARG B 1 30  ? 8.776   -9.259  -25.723 1.00 27.31  ? 18  ARG B C     1 
ATOM   1866 O O     . ARG B 1 30  ? 9.841   -8.862  -26.201 1.00 31.37  ? 18  ARG B O     1 
ATOM   1867 C CB    . ARG B 1 30  ? 6.742   -8.249  -26.789 1.00 30.39  ? 18  ARG B CB    1 
ATOM   1868 C CG    . ARG B 1 30  ? 7.442   -7.100  -27.463 1.00 33.54  ? 18  ARG B CG    1 
ATOM   1869 C CD    . ARG B 1 30  ? 6.408   -5.983  -27.744 1.00 42.48  ? 18  ARG B CD    1 
ATOM   1870 N NE    . ARG B 1 30  ? 5.497   -6.366  -28.819 1.00 41.06  ? 18  ARG B NE    1 
ATOM   1871 C CZ    . ARG B 1 30  ? 4.491   -5.619  -29.260 1.00 40.12  ? 18  ARG B CZ    1 
ATOM   1872 N NH1   . ARG B 1 30  ? 4.167   -4.475  -28.669 1.00 31.62  ? 18  ARG B NH1   1 
ATOM   1873 N NH2   . ARG B 1 30  ? 3.811   -6.017  -30.337 1.00 42.78  ? 18  ARG B NH2   1 
ATOM   1874 N N     . TYR B 1 31  ? 8.586   -9.419  -24.404 1.00 25.60  ? 19  TYR B N     1 
ATOM   1875 C CA    . TYR B 1 31  ? 9.620   -9.188  -23.402 1.00 24.04  ? 19  TYR B CA    1 
ATOM   1876 C C     . TYR B 1 31  ? 10.219  -10.493 -22.892 1.00 26.60  ? 19  TYR B C     1 
ATOM   1877 O O     . TYR B 1 31  ? 10.852  -10.511 -21.838 1.00 27.89  ? 19  TYR B O     1 
ATOM   1878 C CB    . TYR B 1 31  ? 9.078   -8.328  -22.266 1.00 22.24  ? 19  TYR B CB    1 
ATOM   1879 C CG    . TYR B 1 31  ? 8.604   -7.000  -22.832 1.00 22.46  ? 19  TYR B CG    1 
ATOM   1880 C CD1   . TYR B 1 31  ? 9.494   -5.969  -23.005 1.00 22.59  ? 19  TYR B CD1   1 
ATOM   1881 C CD2   . TYR B 1 31  ? 7.298   -6.842  -23.284 1.00 24.35  ? 19  TYR B CD2   1 
ATOM   1882 C CE1   . TYR B 1 31  ? 9.081   -4.760  -23.576 1.00 25.19  ? 19  TYR B CE1   1 
ATOM   1883 C CE2   . TYR B 1 31  ? 6.851   -5.667  -23.842 1.00 25.71  ? 19  TYR B CE2   1 
ATOM   1884 C CZ    . TYR B 1 31  ? 7.747   -4.615  -23.979 1.00 25.53  ? 19  TYR B CZ    1 
ATOM   1885 O OH    . TYR B 1 31  ? 7.357   -3.421  -24.577 1.00 26.48  ? 19  TYR B OH    1 
ATOM   1886 N N     . LEU B 1 32  ? 10.064  -11.572 -23.666 1.00 25.75  ? 20  LEU B N     1 
ATOM   1887 C CA    . LEU B 1 32  ? 10.735  -12.862 -23.427 1.00 30.17  ? 20  LEU B CA    1 
ATOM   1888 C C     . LEU B 1 32  ? 10.213  -13.582 -22.183 1.00 28.84  ? 20  LEU B C     1 
ATOM   1889 O O     . LEU B 1 32  ? 10.961  -14.347 -21.559 1.00 30.20  ? 20  LEU B O     1 
ATOM   1890 C CB    . LEU B 1 32  ? 12.275  -12.777 -23.451 1.00 24.11  ? 20  LEU B CB    1 
ATOM   1891 C CG    . LEU B 1 32  ? 12.781  -12.397 -24.847 1.00 26.03  ? 20  LEU B CG    1 
ATOM   1892 C CD1   . LEU B 1 32  ? 14.298  -12.291 -24.823 1.00 25.50  ? 20  LEU B CD1   1 
ATOM   1893 C CD2   . LEU B 1 32  ? 12.331  -13.372 -25.918 1.00 25.52  ? 20  LEU B CD2   1 
ATOM   1894 N N     . VAL B 1 33  ? 8.974   -13.311 -21.788 1.00 31.25  ? 21  VAL B N     1 
ATOM   1895 C CA    . VAL B 1 33  ? 8.366   -13.969 -20.634 1.00 37.28  ? 21  VAL B CA    1 
ATOM   1896 C C     . VAL B 1 33  ? 7.451   -15.066 -21.143 1.00 38.28  ? 21  VAL B C     1 
ATOM   1897 O O     . VAL B 1 33  ? 6.675   -14.837 -22.068 1.00 39.64  ? 21  VAL B O     1 
ATOM   1898 C CB    . VAL B 1 33  ? 7.599   -12.965 -19.761 1.00 36.73  ? 21  VAL B CB    1 
ATOM   1899 C CG1   . VAL B 1 33  ? 6.916   -13.689 -18.599 1.00 43.52  ? 21  VAL B CG1   1 
ATOM   1900 C CG2   . VAL B 1 33  ? 8.537   -11.886 -19.245 1.00 34.94  ? 21  VAL B CG2   1 
ATOM   1901 N N     . GLY B 1 34  ? 7.566   -16.260 -20.571 1.00 43.57  ? 22  GLY B N     1 
ATOM   1902 C CA    . GLY B 1 34  ? 6.758   -17.367 -21.044 1.00 48.90  ? 22  GLY B CA    1 
ATOM   1903 C C     . GLY B 1 34  ? 7.192   -17.877 -22.399 1.00 42.18  ? 22  GLY B C     1 
ATOM   1904 O O     . GLY B 1 34  ? 6.357   -18.371 -23.173 1.00 53.35  ? 22  GLY B O     1 
ATOM   1905 N N     . VAL B 1 35  ? 8.481   -17.756 -22.700 1.00 41.77  ? 23  VAL B N     1 
ATOM   1906 C CA    . VAL B 1 35  ? 9.049   -18.086 -24.000 1.00 46.03  ? 23  VAL B CA    1 
ATOM   1907 C C     . VAL B 1 35  ? 10.142  -19.113 -23.742 1.00 36.88  ? 23  VAL B C     1 
ATOM   1908 O O     . VAL B 1 35  ? 11.021  -18.866 -22.915 1.00 38.39  ? 23  VAL B O     1 
ATOM   1909 C CB    . VAL B 1 35  ? 9.646   -16.850 -24.701 1.00 41.15  ? 23  VAL B CB    1 
ATOM   1910 C CG1   . VAL B 1 35  ? 10.407  -17.265 -25.947 1.00 44.35  ? 23  VAL B CG1   1 
ATOM   1911 C CG2   . VAL B 1 35  ? 8.530   -15.857 -25.079 1.00 43.40  ? 23  VAL B CG2   1 
ATOM   1912 N N     . PRO B 1 36  ? 10.117  -20.277 -24.383 1.00 39.50  ? 24  PRO B N     1 
ATOM   1913 C CA    . PRO B 1 36  ? 11.182  -21.255 -24.141 1.00 37.79  ? 24  PRO B CA    1 
ATOM   1914 C C     . PRO B 1 36  ? 12.507  -20.772 -24.711 1.00 36.58  ? 24  PRO B C     1 
ATOM   1915 O O     . PRO B 1 36  ? 12.567  -19.908 -25.592 1.00 34.84  ? 24  PRO B O     1 
ATOM   1916 C CB    . PRO B 1 36  ? 10.688  -22.505 -24.875 1.00 35.79  ? 24  PRO B CB    1 
ATOM   1917 C CG    . PRO B 1 36  ? 9.832   -21.970 -25.981 1.00 39.99  ? 24  PRO B CG    1 
ATOM   1918 C CD    . PRO B 1 36  ? 9.147   -20.747 -25.386 1.00 40.01  ? 24  PRO B CD    1 
ATOM   1919 N N     . GLY B 1 37  ? 13.589  -21.330 -24.176 1.00 31.80  ? 25  GLY B N     1 
ATOM   1920 C CA    . GLY B 1 37  ? 14.909  -21.052 -24.706 1.00 30.78  ? 25  GLY B CA    1 
ATOM   1921 C C     . GLY B 1 37  ? 15.496  -19.704 -24.356 1.00 31.48  ? 25  GLY B C     1 
ATOM   1922 O O     . GLY B 1 37  ? 16.343  -19.200 -25.098 1.00 33.60  ? 25  GLY B O     1 
ATOM   1923 N N     . VAL B 1 38  ? 15.073  -19.100 -23.250 1.00 27.78  ? 26  VAL B N     1 
ATOM   1924 C CA    . VAL B 1 38  ? 15.596  -17.807 -22.825 1.00 23.55  ? 26  VAL B CA    1 
ATOM   1925 C C     . VAL B 1 38  ? 16.694  -18.066 -21.800 1.00 26.09  ? 26  VAL B C     1 
ATOM   1926 O O     . VAL B 1 38  ? 16.515  -18.891 -20.895 1.00 32.70  ? 26  VAL B O     1 
ATOM   1927 C CB    . VAL B 1 38  ? 14.474  -16.955 -22.226 1.00 24.83  ? 26  VAL B CB    1 
ATOM   1928 C CG1   . VAL B 1 38  ? 15.087  -15.699 -21.615 1.00 23.68  ? 26  VAL B CG1   1 
ATOM   1929 C CG2   . VAL B 1 38  ? 13.443  -16.582 -23.285 1.00 25.62  ? 26  VAL B CG2   1 
ATOM   1930 N N     . SER B 1 39  ? 17.868  -17.465 -21.997 1.00 21.14  ? 27  SER B N     1 
ATOM   1931 C CA    A SER B 1 39  ? 18.956  -17.485 -21.021 0.70 20.36  ? 27  SER B CA    1 
ATOM   1932 C CA    B SER B 1 39  ? 18.927  -17.502 -20.996 0.30 20.59  ? 27  SER B CA    1 
ATOM   1933 C C     . SER B 1 39  ? 18.978  -16.153 -20.281 1.00 18.69  ? 27  SER B C     1 
ATOM   1934 O O     . SER B 1 39  ? 18.314  -15.169 -20.681 1.00 19.78  ? 27  SER B O     1 
ATOM   1935 C CB    A SER B 1 39  ? 20.315  -17.741 -21.681 0.70 23.35  ? 27  SER B CB    1 
ATOM   1936 C CB    B SER B 1 39  ? 20.283  -17.909 -21.605 0.30 22.29  ? 27  SER B CB    1 
ATOM   1937 O OG    A SER B 1 39  ? 20.309  -18.957 -22.355 0.70 27.29  ? 27  SER B OG    1 
ATOM   1938 O OG    B SER B 1 39  ? 20.791  -16.947 -22.518 0.30 19.65  ? 27  SER B OG    1 
ATOM   1939 N N     . GLU B 1 40  ? 19.715  -16.085 -19.188 1.00 17.14  ? 28  GLU B N     1 
ATOM   1940 C CA    . GLU B 1 40  ? 19.803  -14.848 -18.408 1.00 17.57  ? 28  GLU B CA    1 
ATOM   1941 C C     . GLU B 1 40  ? 21.244  -14.421 -18.199 1.00 16.26  ? 28  GLU B C     1 
ATOM   1942 O O     . GLU B 1 40  ? 22.137  -15.255 -18.027 1.00 18.91  ? 28  GLU B O     1 
ATOM   1943 C CB    . GLU B 1 40  ? 19.130  -14.978 -17.066 1.00 18.58  ? 28  GLU B CB    1 
ATOM   1944 C CG    . GLU B 1 40  ? 17.613  -15.177 -17.161 1.00 20.67  ? 28  GLU B CG    1 
ATOM   1945 C CD    . GLU B 1 40  ? 16.984  -15.491 -15.845 1.00 25.34  ? 28  GLU B CD    1 
ATOM   1946 O OE1   . GLU B 1 40  ? 17.624  -15.447 -14.756 1.00 23.13  ? 28  GLU B OE1   1 
ATOM   1947 O OE2   . GLU B 1 40  ? 15.786  -15.840 -15.872 1.00 26.50  ? 28  GLU B OE2   1 
ATOM   1948 N N     . VAL B 1 41  ? 21.465  -13.099 -18.211 1.00 17.42  ? 29  VAL B N     1 
ATOM   1949 C CA    . VAL B 1 41  ? 22.747  -12.482 -17.882 1.00 16.61  ? 29  VAL B CA    1 
ATOM   1950 C C     . VAL B 1 41  ? 22.513  -11.660 -16.632 1.00 16.47  ? 29  VAL B C     1 
ATOM   1951 O O     . VAL B 1 41  ? 21.652  -10.763 -16.647 1.00 17.39  ? 29  VAL B O     1 
ATOM   1952 C CB    . VAL B 1 41  ? 23.249  -11.598 -19.021 1.00 18.46  ? 29  VAL B CB    1 
ATOM   1953 C CG1   . VAL B 1 41  ? 24.593  -10.935 -18.598 1.00 18.65  ? 29  VAL B CG1   1 
ATOM   1954 C CG2   . VAL B 1 41  ? 23.475  -12.409 -20.249 1.00 19.93  ? 29  VAL B CG2   1 
ATOM   1955 N N     . TRP B 1 42  ? 23.173  -11.985 -15.545 1.00 17.04  ? 30  TRP B N     1 
ATOM   1956 C CA    . TRP B 1 42  ? 23.070  -11.224 -14.300 1.00 16.63  ? 30  TRP B CA    1 
ATOM   1957 C C     . TRP B 1 42  ? 24.250  -10.260 -14.275 1.00 15.93  ? 30  TRP B C     1 
ATOM   1958 O O     . TRP B 1 42  ? 25.398  -10.646 -13.986 1.00 17.08  ? 30  TRP B O     1 
ATOM   1959 C CB    . TRP B 1 42  ? 23.010  -12.150 -13.073 1.00 18.40  ? 30  TRP B CB    1 
ATOM   1960 C CG    . TRP B 1 42  ? 21.659  -12.886 -12.994 1.00 18.31  ? 30  TRP B CG    1 
ATOM   1961 C CD1   . TRP B 1 42  ? 20.882  -13.257 -14.054 1.00 19.79  ? 30  TRP B CD1   1 
ATOM   1962 C CD2   . TRP B 1 42  ? 20.975  -13.285 -11.809 1.00 18.53  ? 30  TRP B CD2   1 
ATOM   1963 N NE1   . TRP B 1 42  ? 19.731  -13.901 -13.566 1.00 20.38  ? 30  TRP B NE1   1 
ATOM   1964 C CE2   . TRP B 1 42  ? 19.779  -13.914 -12.201 1.00 19.03  ? 30  TRP B CE2   1 
ATOM   1965 C CE3   . TRP B 1 42  ? 21.256  -13.186 -10.437 1.00 20.12  ? 30  TRP B CE3   1 
ATOM   1966 C CZ2   . TRP B 1 42  ? 18.890  -14.439 -11.286 1.00 21.10  ? 30  TRP B CZ2   1 
ATOM   1967 C CZ3   . TRP B 1 42  ? 20.345  -13.683 -9.532  1.00 21.71  ? 30  TRP B CZ3   1 
ATOM   1968 C CH2   . TRP B 1 42  ? 19.198  -14.339 -9.959  1.00 22.42  ? 30  TRP B CH2   1 
ATOM   1969 N N     . LEU B 1 43  ? 23.972  -9.004  -14.609 1.00 16.08  ? 31  LEU B N     1 
ATOM   1970 C CA    . LEU B 1 43  ? 24.965  -7.918  -14.652 1.00 15.15  ? 31  LEU B CA    1 
ATOM   1971 C C     . LEU B 1 43  ? 25.157  -7.440  -13.227 1.00 17.10  ? 31  LEU B C     1 
ATOM   1972 O O     . LEU B 1 43  ? 24.190  -7.046  -12.577 1.00 17.90  ? 31  LEU B O     1 
ATOM   1973 C CB    . LEU B 1 43  ? 24.405  -6.769  -15.473 1.00 16.30  ? 31  LEU B CB    1 
ATOM   1974 C CG    . LEU B 1 43  ? 24.198  -7.059  -16.935 1.00 17.23  ? 31  LEU B CG    1 
ATOM   1975 C CD1   . LEU B 1 43  ? 23.458  -5.851  -17.622 1.00 19.33  ? 31  LEU B CD1   1 
ATOM   1976 C CD2   . LEU B 1 43  ? 25.482  -7.403  -17.655 1.00 17.96  ? 31  LEU B CD2   1 
ATOM   1977 N N     . ILE B 1 44  ? 26.389  -7.473  -12.704 1.00 15.80  ? 32  ILE B N     1 
ATOM   1978 C CA    . ILE B 1 44  ? 26.622  -7.156  -11.309 1.00 15.81  ? 32  ILE B CA    1 
ATOM   1979 C C     . ILE B 1 44  ? 27.612  -6.005  -11.269 1.00 16.32  ? 32  ILE B C     1 
ATOM   1980 O O     . ILE B 1 44  ? 28.685  -6.062  -11.871 1.00 16.61  ? 32  ILE B O     1 
ATOM   1981 C CB    . ILE B 1 44  ? 27.242  -8.387  -10.624 1.00 17.54  ? 32  ILE B CB    1 
ATOM   1982 C CG1   . ILE B 1 44  ? 26.231  -9.545  -10.614 1.00 19.99  ? 32  ILE B CG1   1 
ATOM   1983 C CG2   . ILE B 1 44  ? 27.640  -8.057  -9.222  1.00 19.53  ? 32  ILE B CG2   1 
ATOM   1984 C CD1   . ILE B 1 44  ? 26.848  -10.869 -10.174 1.00 20.74  ? 32  ILE B CD1   1 
ATOM   1985 N N     . ARG B 1 45  ? 27.286  -4.965  -10.516 1.00 16.90  ? 33  ARG B N     1 
ATOM   1986 C CA    . ARG B 1 45  ? 28.328  -3.951  -10.297 1.00 16.07  ? 33  ARG B CA    1 
ATOM   1987 C C     . ARG B 1 45  ? 29.262  -4.463  -9.201  1.00 19.09  ? 33  ARG B C     1 
ATOM   1988 O O     . ARG B 1 45  ? 28.817  -5.023  -8.193  1.00 18.41  ? 33  ARG B O     1 
ATOM   1989 C CB    . ARG B 1 45  ? 27.718  -2.595  -9.884  1.00 18.22  ? 33  ARG B CB    1 
ATOM   1990 C CG    . ARG B 1 45  ? 28.803  -1.547  -9.710  1.00 17.45  ? 33  ARG B CG    1 
ATOM   1991 C CD    . ARG B 1 45  ? 28.222  -0.171  -9.336  1.00 17.60  ? 33  ARG B CD    1 
ATOM   1992 N NE    . ARG B 1 45  ? 29.330  0.782   -9.226  1.00 19.26  ? 33  ARG B NE    1 
ATOM   1993 C CZ    . ARG B 1 45  ? 29.305  1.899   -8.503  1.00 21.22  ? 33  ARG B CZ    1 
ATOM   1994 N NH1   . ARG B 1 45  ? 28.203  2.298   -7.891  1.00 22.66  ? 33  ARG B NH1   1 
ATOM   1995 N NH2   . ARG B 1 45  ? 30.419  2.632   -8.398  1.00 20.35  ? 33  ARG B NH2   1 
ATOM   1996 N N     . HIS B 1 46  ? 30.567  -4.207  -9.371  1.00 18.76  ? 34  HIS B N     1 
ATOM   1997 C CA    . HIS B 1 46  ? 31.520  -4.593  -8.346  1.00 18.76  ? 34  HIS B CA    1 
ATOM   1998 C C     . HIS B 1 46  ? 31.194  -3.930  -6.993  1.00 19.40  ? 34  HIS B C     1 
ATOM   1999 O O     . HIS B 1 46  ? 30.383  -3.016  -6.881  1.00 19.17  ? 34  HIS B O     1 
ATOM   2000 C CB    . HIS B 1 46  ? 32.933  -4.197  -8.802  1.00 18.47  ? 34  HIS B CB    1 
ATOM   2001 C CG    . HIS B 1 46  ? 33.087  -2.717  -8.971  1.00 18.82  ? 34  HIS B CG    1 
ATOM   2002 N ND1   . HIS B 1 46  ? 33.169  -1.850  -7.892  1.00 19.52  ? 34  HIS B ND1   1 
ATOM   2003 C CD2   . HIS B 1 46  ? 32.996  -1.944  -10.079 1.00 19.93  ? 34  HIS B CD2   1 
ATOM   2004 C CE1   . HIS B 1 46  ? 33.189  -0.606  -8.345  1.00 23.66  ? 34  HIS B CE1   1 
ATOM   2005 N NE2   . HIS B 1 46  ? 33.103  -0.631  -9.669  1.00 24.27  ? 34  HIS B NE2   1 
ATOM   2006 N N     . ALA B 1 47  ? 31.875  -4.420  -5.951  1.00 19.81  ? 35  ALA B N     1 
ATOM   2007 C CA    . ALA B 1 47  ? 31.707  -3.897  -4.597  1.00 21.65  ? 35  ALA B CA    1 
ATOM   2008 C C     . ALA B 1 47  ? 32.600  -2.665  -4.349  1.00 20.28  ? 35  ALA B C     1 
ATOM   2009 O O     . ALA B 1 47  ? 33.451  -2.316  -5.178  1.00 20.77  ? 35  ALA B O     1 
ATOM   2010 C CB    . ALA B 1 47  ? 32.036  -4.989  -3.571  1.00 22.24  ? 35  ALA B CB    1 
ATOM   2011 N N     . ASP B 1 48  ? 32.487  -2.093  -3.162  1.00 21.28  ? 36  ASP B N     1 
ATOM   2012 C CA    . ASP B 1 48  ? 33.089  -0.792  -2.902  1.00 23.06  ? 36  ASP B CA    1 
ATOM   2013 C C     . ASP B 1 48  ? 34.613  -0.866  -2.901  1.00 25.77  ? 36  ASP B C     1 
ATOM   2014 O O     . ASP B 1 48  ? 35.232  -1.770  -2.315  1.00 24.69  ? 36  ASP B O     1 
ATOM   2015 C CB    . ASP B 1 48  ? 32.696  -0.292  -1.544  1.00 26.04  ? 36  ASP B CB    1 
ATOM   2016 C CG    . ASP B 1 48  ? 33.288  1.048   -1.277  1.00 27.71  ? 36  ASP B CG    1 
ATOM   2017 O OD1   . ASP B 1 48  ? 32.756  2.044   -1.824  1.00 31.34  ? 36  ASP B OD1   1 
ATOM   2018 O OD2   . ASP B 1 48  ? 34.305  1.112   -0.534  1.00 31.69  ? 36  ASP B OD2   1 
ATOM   2019 N N     . SER B 1 49  ? 35.217  0.158   -3.511  1.00 25.05  ? 37  SER B N     1 
ATOM   2020 C CA    . SER B 1 49  ? 36.615  0.498   -3.278  1.00 28.27  ? 37  SER B CA    1 
ATOM   2021 C C     . SER B 1 49  ? 36.767  1.910   -2.740  1.00 33.64  ? 37  SER B C     1 
ATOM   2022 O O     . SER B 1 49  ? 37.519  2.136   -1.789  1.00 38.62  ? 37  SER B O     1 
ATOM   2023 C CB    . SER B 1 49  ? 37.394  0.421   -4.584  1.00 27.08  ? 37  SER B CB    1 
ATOM   2024 O OG    . SER B 1 49  ? 37.696  -0.895  -4.961  1.00 28.87  ? 37  SER B OG    1 
ATOM   2025 N N     . TYR B 1 50  ? 36.044  2.880   -3.308  1.00 30.47  ? 38  TYR B N     1 
ATOM   2026 C CA    . TYR B 1 50  ? 36.405  4.277   -3.094  1.00 33.13  ? 38  TYR B CA    1 
ATOM   2027 C C     . TYR B 1 50  ? 35.742  4.887   -1.877  1.00 40.98  ? 38  TYR B C     1 
ATOM   2028 O O     . TYR B 1 50  ? 36.318  5.806   -1.274  1.00 40.43  ? 38  TYR B O     1 
ATOM   2029 C CB    . TYR B 1 50  ? 36.040  5.099   -4.331  1.00 33.14  ? 38  TYR B CB    1 
ATOM   2030 C CG    . TYR B 1 50  ? 36.982  4.838   -5.488  1.00 28.02  ? 38  TYR B CG    1 
ATOM   2031 C CD1   . TYR B 1 50  ? 38.310  5.227   -5.395  1.00 30.08  ? 38  TYR B CD1   1 
ATOM   2032 C CD2   . TYR B 1 50  ? 36.543  4.289   -6.669  1.00 28.96  ? 38  TYR B CD2   1 
ATOM   2033 C CE1   . TYR B 1 50  ? 39.167  5.009   -6.441  1.00 31.87  ? 38  TYR B CE1   1 
ATOM   2034 C CE2   . TYR B 1 50  ? 37.402  4.044   -7.724  1.00 30.93  ? 38  TYR B CE2   1 
ATOM   2035 C CZ    . TYR B 1 50  ? 38.724  4.430   -7.597  1.00 28.12  ? 38  TYR B CZ    1 
ATOM   2036 O OH    . TYR B 1 50  ? 39.607  4.227   -8.632  1.00 31.01  ? 38  TYR B OH    1 
ATOM   2037 N N     . THR B 1 51  ? 34.539  4.434   -1.505  1.00 37.71  ? 39  THR B N     1 
ATOM   2038 C CA    . THR B 1 51  ? 33.851  5.086   -0.388  1.00 42.05  ? 39  THR B CA    1 
ATOM   2039 C C     . THR B 1 51  ? 34.228  4.517   0.974   1.00 37.87  ? 39  THR B C     1 
ATOM   2040 O O     . THR B 1 51  ? 33.879  5.118   1.996   1.00 49.66  ? 39  THR B O     1 
ATOM   2041 C CB    . THR B 1 51  ? 32.311  5.113   -0.555  1.00 51.01  ? 39  THR B CB    1 
ATOM   2042 O OG1   . THR B 1 51  ? 31.748  3.811   -0.306  1.00 44.51  ? 39  THR B OG1   1 
ATOM   2043 C CG2   . THR B 1 51  ? 31.912  5.616   -1.957  1.00 49.89  ? 39  THR B CG2   1 
ATOM   2044 N N     . GLY B 1 52  ? 34.935  3.395   1.012   1.00 38.89  ? 40  GLY B N     1 
ATOM   2045 C CA    . GLY B 1 52  ? 35.222  2.772   2.285   1.00 46.60  ? 40  GLY B CA    1 
ATOM   2046 C C     . GLY B 1 52  ? 36.649  2.831   2.798   1.00 56.35  ? 40  GLY B C     1 
ATOM   2047 O O     . GLY B 1 52  ? 36.842  2.843   4.017   1.00 69.32  ? 40  GLY B O     1 
ATOM   2048 N N     . LEU B 1 53  ? 37.664  2.848   1.934   1.00 59.85  ? 41  LEU B N     1 
ATOM   2049 C CA    . LEU B 1 53  ? 39.032  2.687   2.423   1.00 79.90  ? 41  LEU B CA    1 
ATOM   2050 C C     . LEU B 1 53  ? 39.787  4.009   2.519   1.00 77.00  ? 41  LEU B C     1 
ATOM   2051 O O     . LEU B 1 53  ? 39.630  4.898   1.674   1.00 78.30  ? 41  LEU B O     1 
ATOM   2052 C CB    . LEU B 1 53  ? 39.831  1.650   1.631   1.00 77.45  ? 41  LEU B CB    1 
ATOM   2053 C CG    . LEU B 1 53  ? 40.487  0.600   2.543   1.00 69.54  ? 41  LEU B CG    1 
ATOM   2054 C CD1   . LEU B 1 53  ? 39.480  0.004   3.562   1.00 47.56  ? 41  LEU B CD1   1 
ATOM   2055 C CD2   . LEU B 1 53  ? 41.137  -0.497  1.704   1.00 69.05  ? 41  LEU B CD2   1 
ATOM   2056 N N     . GLU B 1 54  ? 40.621  4.115   3.557   1.00 77.83  ? 42  GLU B N     1 
ATOM   2057 C CA    . GLU B 1 54  ? 41.293  5.373   3.870   1.00 89.22  ? 42  GLU B CA    1 
ATOM   2058 C C     . GLU B 1 54  ? 42.402  5.677   2.866   1.00 93.87  ? 42  GLU B C     1 
ATOM   2059 O O     . GLU B 1 54  ? 42.372  6.709   2.184   1.00 99.91  ? 42  GLU B O     1 
ATOM   2060 C CB    . GLU B 1 54  ? 41.838  5.331   5.302   1.00 91.35  ? 42  GLU B CB    1 
ATOM   2061 C CG    . GLU B 1 54  ? 40.772  5.298   6.404   1.00 92.88  ? 42  GLU B CG    1 
ATOM   2062 C CD    . GLU B 1 54  ? 40.206  6.674   6.726   1.00 91.72  ? 42  GLU B CD    1 
ATOM   2063 O OE1   . GLU B 1 54  ? 39.492  7.240   5.869   1.00 89.96  ? 42  GLU B OE1   1 
ATOM   2064 O OE2   . GLU B 1 54  ? 40.484  7.192   7.833   1.00 83.50  ? 42  GLU B OE2   1 
ATOM   2065 N N     . ASP B 1 55  ? 43.395  4.797   2.764   1.00 91.08  ? 43  ASP B N     1 
ATOM   2066 C CA    . ASP B 1 55  ? 44.492  4.989   1.828   1.00 80.47  ? 43  ASP B CA    1 
ATOM   2067 C C     . ASP B 1 55  ? 44.481  3.905   0.756   1.00 82.60  ? 43  ASP B C     1 
ATOM   2068 O O     . ASP B 1 55  ? 43.812  2.873   0.875   1.00 80.90  ? 43  ASP B O     1 
ATOM   2069 C CB    . ASP B 1 55  ? 45.854  5.043   2.531   1.00 75.76  ? 43  ASP B CB    1 
ATOM   2070 C CG    . ASP B 1 55  ? 46.905  5.749   1.689   1.00 83.74  ? 43  ASP B CG    1 
ATOM   2071 O OD1   . ASP B 1 55  ? 46.566  6.141   0.550   1.00 73.92  ? 43  ASP B OD1   1 
ATOM   2072 O OD2   . ASP B 1 55  ? 48.056  5.916   2.156   1.00 86.39  ? 43  ASP B OD2   1 
ATOM   2073 N N     . TYR B 1 56  ? 45.248  4.160   -0.301  1.00 73.88  ? 44  TYR B N     1 
ATOM   2074 C CA    . TYR B 1 56  ? 45.261  3.337   -1.501  1.00 75.37  ? 44  TYR B CA    1 
ATOM   2075 C C     . TYR B 1 56  ? 46.650  2.747   -1.674  1.00 64.47  ? 44  TYR B C     1 
ATOM   2076 O O     . TYR B 1 56  ? 47.646  3.474   -1.637  1.00 68.47  ? 44  TYR B O     1 
ATOM   2077 C CB    . TYR B 1 56  ? 44.855  4.176   -2.714  1.00 73.24  ? 44  TYR B CB    1 
ATOM   2078 C CG    . TYR B 1 56  ? 43.466  4.750   -2.534  1.00 84.73  ? 44  TYR B CG    1 
ATOM   2079 C CD1   . TYR B 1 56  ? 43.267  5.948   -1.851  1.00 90.19  ? 44  TYR B CD1   1 
ATOM   2080 C CD2   . TYR B 1 56  ? 42.349  4.071   -3.002  1.00 68.22  ? 44  TYR B CD2   1 
ATOM   2081 C CE1   . TYR B 1 56  ? 41.994  6.462   -1.660  1.00 81.99  ? 44  TYR B CE1   1 
ATOM   2082 C CE2   . TYR B 1 56  ? 41.073  4.580   -2.819  1.00 76.29  ? 44  TYR B CE2   1 
ATOM   2083 C CZ    . TYR B 1 56  ? 40.902  5.778   -2.147  1.00 81.78  ? 44  TYR B CZ    1 
ATOM   2084 O OH    . TYR B 1 56  ? 39.636  6.294   -1.957  1.00 84.11  ? 44  TYR B OH    1 
ATOM   2085 N N     . ASP B 1 57  ? 46.710  1.430   -1.855  1.00 57.16  ? 45  ASP B N     1 
ATOM   2086 C CA    . ASP B 1 57  ? 47.974  0.710   -1.818  1.00 58.67  ? 45  ASP B CA    1 
ATOM   2087 C C     . ASP B 1 57  ? 48.482  0.287   -3.190  1.00 50.96  ? 45  ASP B C     1 
ATOM   2088 O O     . ASP B 1 57  ? 49.625  -0.177  -3.297  1.00 50.91  ? 45  ASP B O     1 
ATOM   2089 C CB    . ASP B 1 57  ? 47.887  -0.474  -0.848  1.00 61.95  ? 45  ASP B CB    1 
ATOM   2090 C CG    . ASP B 1 57  ? 48.006  -0.035  0.616   1.00 70.28  ? 45  ASP B CG    1 
ATOM   2091 O OD1   . ASP B 1 57  ? 48.372  1.141   0.868   1.00 71.95  ? 45  ASP B OD1   1 
ATOM   2092 O OD2   . ASP B 1 57  ? 47.737  -0.865  1.515   1.00 72.17  ? 45  ASP B OD2   1 
ATOM   2093 N N     . GLY B 1 58  ? 47.711  0.502   -4.241  1.00 55.74  ? 46  GLY B N     1 
ATOM   2094 C CA    . GLY B 1 58  ? 48.137  0.215   -5.598  1.00 52.28  ? 46  GLY B CA    1 
ATOM   2095 C C     . GLY B 1 58  ? 47.813  1.381   -6.514  1.00 56.65  ? 46  GLY B C     1 
ATOM   2096 O O     . GLY B 1 58  ? 47.999  2.534   -6.171  1.00 47.99  ? 46  GLY B O     1 
ATOM   2097 N N     . ASP B 1 59  ? 47.326  1.061   -7.698  1.00 42.95  ? 47  ASP B N     1 
ATOM   2098 C CA    . ASP B 1 59  ? 46.980  2.085   -8.668  1.00 36.23  ? 47  ASP B CA    1 
ATOM   2099 C C     . ASP B 1 59  ? 45.718  2.783   -8.152  1.00 34.03  ? 47  ASP B C     1 
ATOM   2100 O O     . ASP B 1 59  ? 44.715  2.117   -7.895  1.00 31.86  ? 47  ASP B O     1 
ATOM   2101 C CB    . ASP B 1 59  ? 46.722  1.345   -9.979  1.00 36.32  ? 47  ASP B CB    1 
ATOM   2102 C CG    . ASP B 1 59  ? 46.400  2.261   -11.144 1.00 49.58  ? 47  ASP B CG    1 
ATOM   2103 O OD1   . ASP B 1 59  ? 45.996  3.415   -10.906 1.00 42.30  ? 47  ASP B OD1   1 
ATOM   2104 O OD2   . ASP B 1 59  ? 46.531  1.799   -12.309 1.00 42.42  ? 47  ASP B OD2   1 
ATOM   2105 N N     . PRO B 1 60  ? 45.765  4.090   -7.882  1.00 36.17  ? 48  PRO B N     1 
ATOM   2106 C CA    . PRO B 1 60  ? 44.560  4.769   -7.385  1.00 34.72  ? 48  PRO B CA    1 
ATOM   2107 C C     . PRO B 1 60  ? 43.375  4.633   -8.321  1.00 31.13  ? 48  PRO B C     1 
ATOM   2108 O O     . PRO B 1 60  ? 42.211  4.676   -7.887  1.00 30.73  ? 48  PRO B O     1 
ATOM   2109 C CB    . PRO B 1 60  ? 45.021  6.232   -7.257  1.00 38.48  ? 48  PRO B CB    1 
ATOM   2110 C CG    . PRO B 1 60  ? 46.206  6.347   -8.123  1.00 46.71  ? 48  PRO B CG    1 
ATOM   2111 C CD    . PRO B 1 60  ? 46.900  5.018   -8.010  1.00 40.54  ? 48  PRO B CD    1 
ATOM   2112 N N     . ARG B 1 61  ? 43.629  4.439   -9.607  1.00 30.57  ? 49  ARG B N     1 
ATOM   2113 C CA    . ARG B 1 61  ? 42.550  4.259   -10.560 1.00 27.82  ? 49  ARG B CA    1 
ATOM   2114 C C     . ARG B 1 61  ? 42.071  2.818   -10.634 1.00 29.83  ? 49  ARG B C     1 
ATOM   2115 O O     . ARG B 1 61  ? 41.050  2.554   -11.277 1.00 28.46  ? 49  ARG B O     1 
ATOM   2116 C CB    . ARG B 1 61  ? 42.998  4.727   -11.941 1.00 31.93  ? 49  ARG B CB    1 
ATOM   2117 C CG    . ARG B 1 61  ? 43.288  6.214   -12.012 1.00 38.69  ? 49  ARG B CG    1 
ATOM   2118 C CD    . ARG B 1 61  ? 43.408  6.708   -13.457 1.00 44.14  ? 49  ARG B CD    1 
ATOM   2119 N NE    . ARG B 1 61  ? 44.699  6.388   -14.049 1.00 51.53  ? 49  ARG B NE    1 
ATOM   2120 C CZ    . ARG B 1 61  ? 44.902  5.724   -15.184 1.00 43.17  ? 49  ARG B CZ    1 
ATOM   2121 N NH1   . ARG B 1 61  ? 43.906  5.188   -15.877 1.00 46.42  ? 49  ARG B NH1   1 
ATOM   2122 N NH2   . ARG B 1 61  ? 46.145  5.606   -15.644 1.00 54.09  ? 49  ARG B NH2   1 
ATOM   2123 N N     . ASP B 1 62  ? 42.750  1.888   -9.972  1.00 26.34  ? 50  ASP B N     1 
ATOM   2124 C CA    . ASP B 1 62  ? 42.385  0.471   -10.031 1.00 25.81  ? 50  ASP B CA    1 
ATOM   2125 C C     . ASP B 1 62  ? 42.640  -0.169  -8.662  1.00 24.09  ? 50  ASP B C     1 
ATOM   2126 O O     . ASP B 1 62  ? 43.502  -1.027  -8.503  1.00 26.98  ? 50  ASP B O     1 
ATOM   2127 C CB    . ASP B 1 62  ? 43.187  -0.180  -11.154 1.00 25.67  ? 50  ASP B CB    1 
ATOM   2128 C CG    . ASP B 1 62  ? 42.764  -1.614  -11.482 1.00 24.41  ? 50  ASP B CG    1 
ATOM   2129 O OD1   . ASP B 1 62  ? 41.750  -2.150  -10.987 1.00 24.45  ? 50  ASP B OD1   1 
ATOM   2130 O OD2   . ASP B 1 62  ? 43.533  -2.115  -12.325 1.00 28.33  ? 50  ASP B OD2   1 
ATOM   2131 N N     . PRO B 1 63  ? 41.845  0.202   -7.658  1.00 24.40  ? 51  PRO B N     1 
ATOM   2132 C CA    . PRO B 1 63  ? 42.104  -0.275  -6.291  1.00 26.87  ? 51  PRO B CA    1 
ATOM   2133 C C     . PRO B 1 63  ? 41.495  -1.649  -5.998  1.00 23.25  ? 51  PRO B C     1 
ATOM   2134 O O     . PRO B 1 63  ? 40.575  -2.124  -6.674  1.00 23.83  ? 51  PRO B O     1 
ATOM   2135 C CB    . PRO B 1 63  ? 41.410  0.795   -5.434  1.00 27.86  ? 51  PRO B CB    1 
ATOM   2136 C CG    . PRO B 1 63  ? 40.273  1.219   -6.291  1.00 30.83  ? 51  PRO B CG    1 
ATOM   2137 C CD    . PRO B 1 63  ? 40.797  1.244   -7.699  1.00 26.55  ? 51  PRO B CD    1 
ATOM   2138 N N     . ALA B 1 64  ? 42.002  -2.271  -4.935  1.00 26.84  ? 52  ALA B N     1 
ATOM   2139 C CA    . ALA B 1 64  ? 41.330  -3.468  -4.424  1.00 28.83  ? 52  ALA B CA    1 
ATOM   2140 C C     . ALA B 1 64  ? 40.064  -3.059  -3.685  1.00 30.19  ? 52  ALA B C     1 
ATOM   2141 O O     . ALA B 1 64  ? 39.796  -1.877  -3.466  1.00 27.51  ? 52  ALA B O     1 
ATOM   2142 C CB    . ALA B 1 64  ? 42.248  -4.267  -3.488  1.00 29.33  ? 52  ALA B CB    1 
ATOM   2143 N N     . LEU B 1 65  ? 39.265  -4.047  -3.298  1.00 26.39  ? 53  LEU B N     1 
ATOM   2144 C CA    . LEU B 1 65  ? 38.083  -3.730  -2.497  1.00 27.56  ? 53  LEU B CA    1 
ATOM   2145 C C     . LEU B 1 65  ? 38.488  -3.148  -1.144  1.00 26.96  ? 53  LEU B C     1 
ATOM   2146 O O     . LEU B 1 65  ? 39.536  -3.475  -0.587  1.00 28.40  ? 53  LEU B O     1 
ATOM   2147 C CB    . LEU B 1 65  ? 37.217  -4.973  -2.261  1.00 27.10  ? 53  LEU B CB    1 
ATOM   2148 C CG    . LEU B 1 65  ? 36.571  -5.564  -3.501  1.00 22.86  ? 53  LEU B CG    1 
ATOM   2149 C CD1   . LEU B 1 65  ? 35.736  -6.766  -3.043  1.00 23.60  ? 53  LEU B CD1   1 
ATOM   2150 C CD2   . LEU B 1 65  ? 35.693  -4.508  -4.101  1.00 23.58  ? 53  LEU B CD2   1 
ATOM   2151 N N     . SER B 1 66  ? 37.662  -2.235  -0.635  1.00 28.72  ? 54  SER B N     1 
ATOM   2152 C CA    . SER B 1 66  ? 37.777  -1.744  0.719   1.00 27.54  ? 54  SER B CA    1 
ATOM   2153 C C     . SER B 1 66  ? 37.238  -2.775  1.705   1.00 30.05  ? 54  SER B C     1 
ATOM   2154 O O     . SER B 1 66  ? 36.644  -3.774  1.307   1.00 28.58  ? 54  SER B O     1 
ATOM   2155 C CB    . SER B 1 66  ? 36.963  -0.459  0.890   1.00 32.94  ? 54  SER B CB    1 
ATOM   2156 O OG    . SER B 1 66  ? 35.576  -0.744  0.716   1.00 30.63  ? 54  SER B OG    1 
ATOM   2157 N N     . GLU B 1 67  ? 37.427  -2.522  2.999   1.00 28.16  ? 55  GLU B N     1 
ATOM   2158 C CA    . GLU B 1 67  ? 36.773  -3.359  4.010   1.00 29.30  ? 55  GLU B CA    1 
ATOM   2159 C C     . GLU B 1 67  ? 35.257  -3.375  3.799   1.00 27.84  ? 55  GLU B C     1 
ATOM   2160 O O     . GLU B 1 67  ? 34.611  -4.436  3.899   1.00 28.99  ? 55  GLU B O     1 
ATOM   2161 C CB    . GLU B 1 67  ? 37.103  -2.841  5.410   1.00 31.62  ? 55  GLU B CB    1 
ATOM   2162 C CG    . GLU B 1 67  ? 36.520  -3.702  6.494   1.00 38.83  ? 55  GLU B CG    1 
ATOM   2163 C CD    . GLU B 1 67  ? 36.978  -3.288  7.879   1.00 51.21  ? 55  GLU B CD    1 
ATOM   2164 O OE1   . GLU B 1 67  ? 37.726  -2.297  7.988   1.00 44.05  ? 55  GLU B OE1   1 
ATOM   2165 O OE2   . GLU B 1 67  ? 36.596  -3.968  8.848   1.00 59.29  ? 55  GLU B OE2   1 
ATOM   2166 N N     . LYS B 1 68  ? 34.671  -2.212  3.487   1.00 26.08  ? 56  LYS B N     1 
ATOM   2167 C CA    . LYS B 1 68  ? 33.242  -2.157  3.197   1.00 24.65  ? 56  LYS B CA    1 
ATOM   2168 C C     . LYS B 1 68  ? 32.922  -3.019  1.991   1.00 24.51  ? 56  LYS B C     1 
ATOM   2169 O O     . LYS B 1 68  ? 31.943  -3.779  1.990   1.00 25.25  ? 56  LYS B O     1 
ATOM   2170 C CB    . LYS B 1 68  ? 32.831  -0.705  2.927   1.00 24.98  ? 56  LYS B CB    1 
ATOM   2171 C CG    . LYS B 1 68  ? 31.396  -0.495  2.481   1.00 26.32  ? 56  LYS B CG    1 
ATOM   2172 C CD    . LYS B 1 68  ? 31.116  1.005   2.354   1.00 29.32  ? 56  LYS B CD    1 
ATOM   2173 C CE    . LYS B 1 68  ? 29.772  1.302   1.703   1.00 39.46  ? 56  LYS B CE    1 
ATOM   2174 N NZ    . LYS B 1 68  ? 29.623  2.775   1.484   1.00 45.32  ? 56  LYS B NZ    1 
ATOM   2175 N N     . GLY B 1 69  ? 33.727  -2.893  0.935   1.00 23.56  ? 57  GLY B N     1 
ATOM   2176 C CA    . GLY B 1 69  ? 33.511  -3.705  -0.252  1.00 23.22  ? 57  GLY B CA    1 
ATOM   2177 C C     . GLY B 1 69  ? 33.596  -5.204  0.002   1.00 22.80  ? 57  GLY B C     1 
ATOM   2178 O O     . GLY B 1 69  ? 32.803  -5.987  -0.553  1.00 21.80  ? 57  GLY B O     1 
ATOM   2179 N N     . ARG B 1 70  ? 34.566  -5.636  0.819   1.00 23.80  ? 58  ARG B N     1 
ATOM   2180 C CA    . ARG B 1 70  ? 34.621  -7.059  1.122   1.00 24.17  ? 58  ARG B CA    1 
ATOM   2181 C C     . ARG B 1 70  ? 33.332  -7.527  1.796   1.00 24.82  ? 58  ARG B C     1 
ATOM   2182 O O     . ARG B 1 70  ? 32.822  -8.616  1.495   1.00 24.51  ? 58  ARG B O     1 
ATOM   2183 C CB    . ARG B 1 70  ? 35.864  -7.383  1.958   1.00 28.29  ? 58  ARG B CB    1 
ATOM   2184 C CG    . ARG B 1 70  ? 37.175  -7.138  1.214   1.00 26.52  ? 58  ARG B CG    1 
ATOM   2185 C CD    . ARG B 1 70  ? 38.401  -7.758  1.953   1.00 31.44  ? 58  ARG B CD    1 
ATOM   2186 N NE    . ARG B 1 70  ? 38.638  -7.117  3.241   1.00 32.51  ? 58  ARG B NE    1 
ATOM   2187 C CZ    . ARG B 1 70  ? 39.318  -5.988  3.432   1.00 33.93  ? 58  ARG B CZ    1 
ATOM   2188 N NH1   . ARG B 1 70  ? 39.817  -5.294  2.414   1.00 33.87  ? 58  ARG B NH1   1 
ATOM   2189 N NH2   . ARG B 1 70  ? 39.467  -5.524  4.670   1.00 35.10  ? 58  ARG B NH2   1 
ATOM   2190 N N     . ALA B 1 71  ? 32.780  -6.705  2.689   1.00 24.70  ? 59  ALA B N     1 
ATOM   2191 C CA    . ALA B 1 71  ? 31.548  -7.068  3.373   1.00 22.98  ? 59  ALA B CA    1 
ATOM   2192 C C     . ALA B 1 71  ? 30.390  -7.128  2.402   1.00 23.88  ? 59  ALA B C     1 
ATOM   2193 O O     . ALA B 1 71  ? 29.568  -8.060  2.456   1.00 24.23  ? 59  ALA B O     1 
ATOM   2194 C CB    . ALA B 1 71  ? 31.261  -6.067  4.488   1.00 23.53  ? 59  ALA B CB    1 
ATOM   2195 N N     . GLN B 1 72  ? 30.314  -6.162  1.486   1.00 22.73  ? 60  GLN B N     1 
ATOM   2196 C CA    . GLN B 1 72  ? 29.251  -6.195  0.486   1.00 20.84  ? 60  GLN B CA    1 
ATOM   2197 C C     . GLN B 1 72  ? 29.374  -7.420  -0.398  1.00 21.51  ? 60  GLN B C     1 
ATOM   2198 O O     . GLN B 1 72  ? 28.368  -8.056  -0.742  1.00 21.51  ? 60  GLN B O     1 
ATOM   2199 C CB    . GLN B 1 72  ? 29.309  -4.954  -0.408  1.00 20.68  ? 60  GLN B CB    1 
ATOM   2200 C CG    . GLN B 1 72  ? 29.100  -3.648  0.319   1.00 21.58  ? 60  GLN B CG    1 
ATOM   2201 C CD    . GLN B 1 72  ? 29.292  -2.476  -0.616  1.00 21.88  ? 60  GLN B CD    1 
ATOM   2202 O OE1   . GLN B 1 72  ? 30.099  -2.530  -1.547  1.00 20.92  ? 60  GLN B OE1   1 
ATOM   2203 N NE2   . GLN B 1 72  ? 28.569  -1.392  -0.351  1.00 25.73  ? 60  GLN B NE2   1 
ATOM   2204 N N     . ALA B 1 73  ? 30.602  -7.748  -0.820  1.00 22.90  ? 61  ALA B N     1 
ATOM   2205 C CA    . ALA B 1 73  ? 30.777  -8.922  -1.670  1.00 22.17  ? 61  ALA B CA    1 
ATOM   2206 C C     . ALA B 1 73  ? 30.396  -10.220 -0.959  1.00 20.25  ? 61  ALA B C     1 
ATOM   2207 O O     . ALA B 1 73  ? 29.831  -11.112 -1.603  1.00 22.05  ? 61  ALA B O     1 
ATOM   2208 C CB    . ALA B 1 73  ? 32.219  -8.980  -2.162  1.00 21.38  ? 61  ALA B CB    1 
ATOM   2209 N N     . ARG B 1 74  ? 30.617  -10.306 0.345   1.00 21.45  ? 62  ARG B N     1 
ATOM   2210 C CA    . ARG B 1 74  ? 30.189  -11.501 1.069   1.00 22.89  ? 62  ARG B CA    1 
ATOM   2211 C C     . ARG B 1 74  ? 28.676  -11.626 1.017   1.00 24.65  ? 62  ARG B C     1 
ATOM   2212 O O     . ARG B 1 74  ? 28.146  -12.721 0.817   1.00 24.14  ? 62  ARG B O     1 
ATOM   2213 C CB    . ARG B 1 74  ? 30.677  -11.435 2.507   1.00 23.89  ? 62  ARG B CB    1 
ATOM   2214 C CG    . ARG B 1 74  ? 32.172  -11.631 2.642   1.00 30.65  ? 62  ARG B CG    1 
ATOM   2215 C CD    . ARG B 1 74  ? 32.620  -11.751 4.110   1.00 33.03  ? 62  ARG B CD    1 
ATOM   2216 N NE    . ARG B 1 74  ? 34.063  -11.524 4.187   1.00 41.88  ? 62  ARG B NE    1 
ATOM   2217 C CZ    . ARG B 1 74  ? 34.634  -10.395 4.592   1.00 45.85  ? 62  ARG B CZ    1 
ATOM   2218 N NH1   . ARG B 1 74  ? 33.917  -9.384  5.070   1.00 32.30  ? 62  ARG B NH1   1 
ATOM   2219 N NH2   . ARG B 1 74  ? 35.964  -10.284 4.538   1.00 43.79  ? 62  ARG B NH2   1 
ATOM   2220 N N     . LEU B 1 75  ? 27.957  -10.522 1.221   1.00 21.40  ? 63  LEU B N     1 
ATOM   2221 C CA    . LEU B 1 75  ? 26.490  -10.592 1.211   1.00 21.44  ? 63  LEU B CA    1 
ATOM   2222 C C     . LEU B 1 75  ? 25.977  -10.902 -0.186  1.00 19.42  ? 63  LEU B C     1 
ATOM   2223 O O     . LEU B 1 75  ? 24.996  -11.644 -0.347  1.00 21.84  ? 63  LEU B O     1 
ATOM   2224 C CB    . LEU B 1 75  ? 25.888  -9.270  1.716   1.00 24.56  ? 63  LEU B CB    1 
ATOM   2225 C CG    . LEU B 1 75  ? 26.165  -8.965  3.199   1.00 26.90  ? 63  LEU B CG    1 
ATOM   2226 C CD1   . LEU B 1 75  ? 25.909  -7.481  3.513   1.00 28.18  ? 63  LEU B CD1   1 
ATOM   2227 C CD2   . LEU B 1 75  ? 25.331  -9.885  4.114   1.00 29.11  ? 63  LEU B CD2   1 
ATOM   2228 N N     . LEU B 1 76  ? 26.622  -10.364 -1.214  1.00 19.24  ? 64  LEU B N     1 
ATOM   2229 C CA    . LEU B 1 76  ? 26.242  -10.688 -2.583  1.00 17.96  ? 64  LEU B CA    1 
ATOM   2230 C C     . LEU B 1 76  ? 26.463  -12.166 -2.862  1.00 20.53  ? 64  LEU B C     1 
ATOM   2231 O O     . LEU B 1 76  ? 25.614  -12.829 -3.466  1.00 20.64  ? 64  LEU B O     1 
ATOM   2232 C CB    . LEU B 1 76  ? 27.048  -9.836  -3.561  1.00 18.55  ? 64  LEU B CB    1 
ATOM   2233 C CG    . LEU B 1 76  ? 26.893  -10.195 -5.023  1.00 18.68  ? 64  LEU B CG    1 
ATOM   2234 C CD1   . LEU B 1 76  ? 25.527  -9.811  -5.536  1.00 21.60  ? 64  LEU B CD1   1 
ATOM   2235 C CD2   . LEU B 1 76  ? 28.009  -9.525  -5.826  1.00 23.91  ? 64  LEU B CD2   1 
ATOM   2236 N N     . ALA B 1 77  ? 27.610  -12.689 -2.450  1.00 20.24  ? 65  ALA B N     1 
ATOM   2237 C CA    . ALA B 1 77  ? 27.936  -14.075 -2.747  1.00 19.84  ? 65  ALA B CA    1 
ATOM   2238 C C     . ALA B 1 77  ? 26.964  -15.003 -2.047  1.00 20.69  ? 65  ALA B C     1 
ATOM   2239 O O     . ALA B 1 77  ? 26.576  -16.043 -2.612  1.00 22.40  ? 65  ALA B O     1 
ATOM   2240 C CB    . ALA B 1 77  ? 29.389  -14.336 -2.359  1.00 23.17  ? 65  ALA B CB    1 
ATOM   2241 N N     . ALA B 1 78  ? 26.560  -14.660 -0.818  1.00 19.82  ? 66  ALA B N     1 
ATOM   2242 C CA    . ALA B 1 78  ? 25.557  -15.467 -0.126  1.00 22.14  ? 66  ALA B CA    1 
ATOM   2243 C C     . ALA B 1 78  ? 24.222  -15.409 -0.848  1.00 20.83  ? 66  ALA B C     1 
ATOM   2244 O O     . ALA B 1 78  ? 23.509  -16.420 -0.932  1.00 24.02  ? 66  ALA B O     1 
ATOM   2245 C CB    . ALA B 1 78  ? 25.421  -15.022 1.321   1.00 21.97  ? 66  ALA B CB    1 
ATOM   2246 N N     . ARG B 1 79  ? 23.831  -14.216 -1.310  1.00 22.99  ? 67  ARG B N     1 
ATOM   2247 C CA    . ARG B 1 79  ? 22.567  -14.071 -2.033  1.00 21.43  ? 67  ARG B CA    1 
ATOM   2248 C C     . ARG B 1 79  ? 22.562  -14.945 -3.272  1.00 20.58  ? 67  ARG B C     1 
ATOM   2249 O O     . ARG B 1 79  ? 21.572  -15.640 -3.547  1.00 24.61  ? 67  ARG B O     1 
ATOM   2250 C CB    . ARG B 1 79  ? 22.370  -12.597 -2.411  1.00 21.43  ? 67  ARG B CB    1 
ATOM   2251 C CG    . ARG B 1 79  ? 21.249  -12.434 -3.413  1.00 21.76  ? 67  ARG B CG    1 
ATOM   2252 C CD    . ARG B 1 79  ? 21.193  -11.014 -3.928  1.00 21.84  ? 67  ARG B CD    1 
ATOM   2253 N NE    . ARG B 1 79  ? 20.202  -10.900 -4.995  1.00 20.87  ? 67  ARG B NE    1 
ATOM   2254 C CZ    . ARG B 1 79  ? 19.791  -9.735  -5.486  1.00 23.42  ? 67  ARG B CZ    1 
ATOM   2255 N NH1   . ARG B 1 79  ? 20.321  -8.602  -5.074  1.00 20.07  ? 67  ARG B NH1   1 
ATOM   2256 N NH2   . ARG B 1 79  ? 18.853  -9.726  -6.431  1.00 20.69  ? 67  ARG B NH2   1 
ATOM   2257 N N     . LEU B 1 80  ? 23.680  -14.998 -3.989  1.00 21.69  ? 68  LEU B N     1 
ATOM   2258 C CA    . LEU B 1 80  ? 23.744  -15.743 -5.237  1.00 19.84  ? 68  LEU B CA    1 
ATOM   2259 C C     . LEU B 1 80  ? 24.123  -17.213 -5.040  1.00 22.92  ? 68  LEU B C     1 
ATOM   2260 O O     . LEU B 1 80  ? 24.082  -17.964 -6.021  1.00 24.23  ? 68  LEU B O     1 
ATOM   2261 C CB    . LEU B 1 80  ? 24.712  -15.071 -6.221  1.00 21.44  ? 68  LEU B CB    1 
ATOM   2262 C CG    . LEU B 1 80  ? 24.265  -13.646 -6.636  1.00 22.40  ? 68  LEU B CG    1 
ATOM   2263 C CD1   . LEU B 1 80  ? 25.263  -13.076 -7.647  1.00 25.75  ? 68  LEU B CD1   1 
ATOM   2264 C CD2   . LEU B 1 80  ? 22.863  -13.600 -7.147  1.00 23.79  ? 68  LEU B CD2   1 
ATOM   2265 N N     . ALA B 1 81  ? 24.436  -17.641 -3.811  1.00 22.84  ? 69  ALA B N     1 
ATOM   2266 C CA    . ALA B 1 81  ? 24.878  -19.016 -3.604  1.00 21.96  ? 69  ALA B CA    1 
ATOM   2267 C C     . ALA B 1 81  ? 23.821  -20.021 -4.014  1.00 26.22  ? 69  ALA B C     1 
ATOM   2268 O O     . ALA B 1 81  ? 24.158  -21.099 -4.525  1.00 29.14  ? 69  ALA B O     1 
ATOM   2269 C CB    . ALA B 1 81  ? 25.232  -19.206 -2.151  1.00 24.80  ? 69  ALA B CB    1 
ATOM   2270 N N     . GLY B 1 82  ? 22.543  -19.703 -3.788  1.00 25.95  ? 70  GLY B N     1 
ATOM   2271 C CA    . GLY B 1 82  ? 21.447  -20.611 -4.098  1.00 30.31  ? 70  GLY B CA    1 
ATOM   2272 C C     . GLY B 1 82  ? 20.861  -20.446 -5.486  1.00 28.76  ? 70  GLY B C     1 
ATOM   2273 O O     . GLY B 1 82  ? 19.867  -21.109 -5.812  1.00 33.92  ? 70  GLY B O     1 
ATOM   2274 N N     . VAL B 1 83  ? 21.433  -19.592 -6.315  1.00 23.47  ? 71  VAL B N     1 
ATOM   2275 C CA    . VAL B 1 83  ? 20.971  -19.375 -7.680  1.00 23.32  ? 71  VAL B CA    1 
ATOM   2276 C C     . VAL B 1 83  ? 21.810  -20.239 -8.622  1.00 23.73  ? 71  VAL B C     1 
ATOM   2277 O O     . VAL B 1 83  ? 23.046  -20.131 -8.600  1.00 23.24  ? 71  VAL B O     1 
ATOM   2278 C CB    . VAL B 1 83  ? 21.153  -17.886 -8.029  1.00 25.25  ? 71  VAL B CB    1 
ATOM   2279 C CG1   . VAL B 1 83  ? 20.871  -17.641 -9.461  1.00 24.97  ? 71  VAL B CG1   1 
ATOM   2280 C CG2   . VAL B 1 83  ? 20.274  -17.006 -7.132  1.00 25.17  ? 71  VAL B CG2   1 
ATOM   2281 N N     . PRO B 1 84  ? 21.206  -21.061 -9.485  1.00 22.14  ? 72  PRO B N     1 
ATOM   2282 C CA    . PRO B 1 84  ? 22.030  -21.805 -10.468 1.00 22.36  ? 72  PRO B CA    1 
ATOM   2283 C C     . PRO B 1 84  ? 22.750  -20.824 -11.374 1.00 22.49  ? 72  PRO B C     1 
ATOM   2284 O O     . PRO B 1 84  ? 22.115  -19.985 -12.019 1.00 23.59  ? 72  PRO B O     1 
ATOM   2285 C CB    . PRO B 1 84  ? 20.994  -22.626 -11.241 1.00 24.15  ? 72  PRO B CB    1 
ATOM   2286 C CG    . PRO B 1 84  ? 19.868  -22.790 -10.238 1.00 28.99  ? 72  PRO B CG    1 
ATOM   2287 C CD    . PRO B 1 84  ? 19.788  -21.473 -9.510  1.00 24.53  ? 72  PRO B CD    1 
ATOM   2288 N N     . LEU B 1 85  ? 24.080  -20.900 -11.386 1.00 21.18  ? 73  LEU B N     1 
ATOM   2289 C CA    . LEU B 1 85  ? 24.914  -20.048 -12.214 1.00 21.62  ? 73  LEU B CA    1 
ATOM   2290 C C     . LEU B 1 85  ? 25.864  -20.922 -13.003 1.00 20.63  ? 73  LEU B C     1 
ATOM   2291 O O     . LEU B 1 85  ? 26.416  -21.885 -12.464 1.00 21.72  ? 73  LEU B O     1 
ATOM   2292 C CB    . LEU B 1 85  ? 25.833  -19.064 -11.456 1.00 24.29  ? 73  LEU B CB    1 
ATOM   2293 C CG    . LEU B 1 85  ? 25.182  -17.900 -10.711 1.00 30.53  ? 73  LEU B CG    1 
ATOM   2294 C CD1   . LEU B 1 85  ? 26.320  -17.091 -10.061 1.00 25.00  ? 73  LEU B CD1   1 
ATOM   2295 C CD2   . LEU B 1 85  ? 24.334  -17.026 -11.644 1.00 25.90  ? 73  LEU B CD2   1 
ATOM   2296 N N     . HIS B 1 86  ? 26.096  -20.566 -14.250 1.00 18.74  ? 74  HIS B N     1 
ATOM   2297 C CA    . HIS B 1 86  ? 26.820  -21.433 -15.174 1.00 18.84  ? 74  HIS B CA    1 
ATOM   2298 C C     . HIS B 1 86  ? 28.104  -20.830 -15.707 1.00 21.11  ? 74  HIS B C     1 
ATOM   2299 O O     . HIS B 1 86  ? 28.890  -21.534 -16.356 1.00 20.67  ? 74  HIS B O     1 
ATOM   2300 C CB    . HIS B 1 86  ? 25.872  -21.904 -16.285 1.00 20.30  ? 74  HIS B CB    1 
ATOM   2301 C CG    . HIS B 1 86  ? 24.637  -22.487 -15.701 1.00 19.70  ? 74  HIS B CG    1 
ATOM   2302 N ND1   . HIS B 1 86  ? 23.492  -21.740 -15.522 1.00 19.24  ? 74  HIS B ND1   1 
ATOM   2303 C CD2   . HIS B 1 86  ? 24.425  -23.672 -15.087 1.00 22.09  ? 74  HIS B CD2   1 
ATOM   2304 C CE1   . HIS B 1 86  ? 22.609  -22.456 -14.873 1.00 20.03  ? 74  HIS B CE1   1 
ATOM   2305 N NE2   . HIS B 1 86  ? 23.147  -23.637 -14.591 1.00 20.80  ? 74  HIS B NE2   1 
ATOM   2306 N N     . GLY B 1 87  ? 28.352  -19.561 -15.417 1.00 18.94  ? 75  GLY B N     1 
ATOM   2307 C CA    . GLY B 1 87  ? 29.615  -18.920 -15.714 1.00 19.05  ? 75  GLY B CA    1 
ATOM   2308 C C     . GLY B 1 87  ? 29.707  -17.623 -14.963 1.00 18.85  ? 75  GLY B C     1 
ATOM   2309 O O     . GLY B 1 87  ? 28.683  -17.057 -14.556 1.00 18.29  ? 75  GLY B O     1 
ATOM   2310 N N     . VAL B 1 88  ? 30.935  -17.136 -14.803 1.00 18.72  ? 76  VAL B N     1 
ATOM   2311 C CA    . VAL B 1 88  ? 31.214  -15.839 -14.188 1.00 18.12  ? 76  VAL B CA    1 
ATOM   2312 C C     . VAL B 1 88  ? 32.289  -15.165 -15.009 1.00 18.02  ? 76  VAL B C     1 
ATOM   2313 O O     . VAL B 1 88  ? 33.402  -15.703 -15.175 1.00 18.58  ? 76  VAL B O     1 
ATOM   2314 C CB    . VAL B 1 88  ? 31.642  -15.981 -12.715 1.00 18.66  ? 76  VAL B CB    1 
ATOM   2315 C CG1   . VAL B 1 88  ? 31.992  -14.620 -12.157 1.00 22.38  ? 76  VAL B CG1   1 
ATOM   2316 C CG2   . VAL B 1 88  ? 30.590  -16.644 -11.846 1.00 21.18  ? 76  VAL B CG2   1 
ATOM   2317 N N     . TRP B 1 89  ? 31.955  -13.976 -15.528 1.00 17.43  ? 77  TRP B N     1 
ATOM   2318 C CA    . TRP B 1 89  ? 32.872  -13.109 -16.261 1.00 18.17  ? 77  TRP B CA    1 
ATOM   2319 C C     . TRP B 1 89  ? 33.030  -11.791 -15.518 1.00 18.07  ? 77  TRP B C     1 
ATOM   2320 O O     . TRP B 1 89  ? 32.158  -11.364 -14.743 1.00 18.94  ? 77  TRP B O     1 
ATOM   2321 C CB    . TRP B 1 89  ? 32.406  -12.890 -17.680 1.00 18.74  ? 77  TRP B CB    1 
ATOM   2322 C CG    . TRP B 1 89  ? 32.550  -14.132 -18.525 1.00 21.38  ? 77  TRP B CG    1 
ATOM   2323 C CD1   . TRP B 1 89  ? 31.720  -15.241 -18.540 1.00 22.22  ? 77  TRP B CD1   1 
ATOM   2324 C CD2   . TRP B 1 89  ? 33.610  -14.414 -19.447 1.00 23.45  ? 77  TRP B CD2   1 
ATOM   2325 N NE1   . TRP B 1 89  ? 32.228  -16.183 -19.420 1.00 28.41  ? 77  TRP B NE1   1 
ATOM   2326 C CE2   . TRP B 1 89  ? 33.382  -15.705 -19.985 1.00 24.29  ? 77  TRP B CE2   1 
ATOM   2327 C CE3   . TRP B 1 89  ? 34.740  -13.717 -19.847 1.00 26.62  ? 77  TRP B CE3   1 
ATOM   2328 C CZ2   . TRP B 1 89  ? 34.243  -16.291 -20.914 1.00 31.12  ? 77  TRP B CZ2   1 
ATOM   2329 C CZ3   . TRP B 1 89  ? 35.604  -14.302 -20.765 1.00 28.22  ? 77  TRP B CZ3   1 
ATOM   2330 C CH2   . TRP B 1 89  ? 35.351  -15.581 -21.286 1.00 30.05  ? 77  TRP B CH2   1 
ATOM   2331 N N     . ALA B 1 90  ? 34.165  -11.147 -15.736 1.00 17.52  ? 78  ALA B N     1 
ATOM   2332 C CA    . ALA B 1 90  ? 34.431  -9.882  -15.062 1.00 18.19  ? 78  ALA B CA    1 
ATOM   2333 C C     . ALA B 1 90  ? 35.350  -9.024  -15.911 1.00 18.00  ? 78  ALA B C     1 
ATOM   2334 O O     . ALA B 1 90  ? 36.158  -9.506  -16.708 1.00 19.00  ? 78  ALA B O     1 
ATOM   2335 C CB    . ALA B 1 90  ? 35.133  -10.121 -13.721 1.00 20.88  ? 78  ALA B CB    1 
ATOM   2336 N N     . SER B 1 91  ? 35.213  -7.707  -15.715 1.00 18.63  ? 79  SER B N     1 
ATOM   2337 C CA    . SER B 1 91  ? 36.220  -6.757  -16.142 1.00 17.77  ? 79  SER B CA    1 
ATOM   2338 C C     . SER B 1 91  ? 37.555  -7.132  -15.525 1.00 21.92  ? 79  SER B C     1 
ATOM   2339 O O     . SER B 1 91  ? 37.594  -7.782  -14.492 1.00 20.73  ? 79  SER B O     1 
ATOM   2340 C CB    . SER B 1 91  ? 35.723  -5.395  -15.648 1.00 20.83  ? 79  SER B CB    1 
ATOM   2341 O OG    . SER B 1 91  ? 36.712  -4.510  -15.326 1.00 23.40  ? 79  SER B OG    1 
ATOM   2342 N N     . GLY B 1 92  ? 38.646  -6.687  -16.142 1.00 19.06  ? 80  GLY B N     1 
ATOM   2343 C CA    . GLY B 1 92  ? 39.954  -6.913  -15.525 1.00 20.46  ? 80  GLY B CA    1 
ATOM   2344 C C     . GLY B 1 92  ? 40.216  -6.105  -14.273 1.00 19.54  ? 80  GLY B C     1 
ATOM   2345 O O     . GLY B 1 92  ? 41.209  -6.337  -13.591 1.00 21.74  ? 80  GLY B O     1 
ATOM   2346 N N     . ALA B 1 93  ? 39.413  -5.091  -14.006 1.00 19.86  ? 81  ALA B N     1 
ATOM   2347 C CA    . ALA B 1 93  ? 39.700  -4.238  -12.859 1.00 18.68  ? 81  ALA B CA    1 
ATOM   2348 C C     . ALA B 1 93  ? 39.758  -5.082  -11.585 1.00 20.05  ? 81  ALA B C     1 
ATOM   2349 O O     . ALA B 1 93  ? 38.944  -5.980  -11.390 1.00 19.51  ? 81  ALA B O     1 
ATOM   2350 C CB    . ALA B 1 93  ? 38.588  -3.204  -12.725 1.00 20.69  ? 81  ALA B CB    1 
ATOM   2351 N N     . HIS B 1 94  ? 40.682  -4.751  -10.686 1.00 20.40  ? 82  HIS B N     1 
ATOM   2352 C CA    . HIS B 1 94  ? 40.878  -5.594  -9.508  1.00 22.51  ? 82  HIS B CA    1 
ATOM   2353 C C     . HIS B 1 94  ? 39.603  -5.680  -8.686  1.00 21.37  ? 82  HIS B C     1 
ATOM   2354 O O     . HIS B 1 94  ? 39.267  -6.747  -8.174  1.00 21.53  ? 82  HIS B O     1 
ATOM   2355 C CB    . HIS B 1 94  ? 42.025  -5.054  -8.654  1.00 22.29  ? 82  HIS B CB    1 
ATOM   2356 C CG    . HIS B 1 94  ? 43.346  -5.038  -9.358  1.00 23.80  ? 82  HIS B CG    1 
ATOM   2357 N ND1   . HIS B 1 94  ? 43.948  -6.169  -9.875  1.00 24.60  ? 82  HIS B ND1   1 
ATOM   2358 C CD2   . HIS B 1 94  ? 44.205  -4.015  -9.594  1.00 24.30  ? 82  HIS B CD2   1 
ATOM   2359 C CE1   . HIS B 1 94  ? 45.120  -5.842  -10.399 1.00 26.22  ? 82  HIS B CE1   1 
ATOM   2360 N NE2   . HIS B 1 94  ? 45.302  -4.541  -10.243 1.00 25.80  ? 82  HIS B NE2   1 
ATOM   2361 N N     . ARG B 1 95  ? 38.880  -4.572  -8.557  1.00 20.49  ? 83  ARG B N     1 
ATOM   2362 C CA    . ARG B 1 95  ? 37.639  -4.573  -7.742  1.00 22.14  ? 83  ARG B CA    1 
ATOM   2363 C C     . ARG B 1 95  ? 36.587  -5.498  -8.372  1.00 20.43  ? 83  ARG B C     1 
ATOM   2364 O O     . ARG B 1 95  ? 35.857  -6.106  -7.634  1.00 22.92  ? 83  ARG B O     1 
ATOM   2365 C CB    . ARG B 1 95  ? 37.158  -3.150  -7.450  1.00 23.17  ? 83  ARG B CB    1 
ATOM   2366 C CG    . ARG B 1 95  ? 36.822  -2.301  -8.661  1.00 22.38  ? 83  ARG B CG    1 
ATOM   2367 C CD    . ARG B 1 95  ? 36.659  -0.837  -8.265  1.00 26.02  ? 83  ARG B CD    1 
ATOM   2368 N NE    . ARG B 1 95  ? 36.301  0.035   -9.367  1.00 27.83  ? 83  ARG B NE    1 
ATOM   2369 C CZ    . ARG B 1 95  ? 37.091  0.297   -10.397 1.00 29.84  ? 83  ARG B CZ    1 
ATOM   2370 N NH1   . ARG B 1 95  ? 38.292  -0.217  -10.472 1.00 32.43  ? 83  ARG B NH1   1 
ATOM   2371 N NH2   . ARG B 1 95  ? 36.711  1.092   -11.367 1.00 44.81  ? 83  ARG B NH2   1 
ATOM   2372 N N     . ALA B 1 96  ? 36.529  -5.575  -9.694  1.00 19.29  ? 84  ALA B N     1 
ATOM   2373 C CA    . ALA B 1 96  ? 35.581  -6.486  -10.347 1.00 19.44  ? 84  ALA B CA    1 
ATOM   2374 C C     . ALA B 1 96  ? 36.049  -7.923  -10.214 1.00 19.40  ? 84  ALA B C     1 
ATOM   2375 O O     . ALA B 1 96  ? 35.240  -8.819  -9.936  1.00 19.49  ? 84  ALA B O     1 
ATOM   2376 C CB    . ALA B 1 96  ? 35.412  -6.121  -11.812 1.00 18.66  ? 84  ALA B CB    1 
ATOM   2377 N N     . GLN B 1 97  ? 37.365  -8.177  -10.361 1.00 19.38  ? 85  GLN B N     1 
ATOM   2378 C CA    . GLN B 1 97  ? 37.895  -9.522  -10.174 1.00 18.33  ? 85  GLN B CA    1 
ATOM   2379 C C     . GLN B 1 97  ? 37.578  -10.036 -8.792  1.00 22.36  ? 85  GLN B C     1 
ATOM   2380 O O     . GLN B 1 97  ? 37.164  -11.194 -8.639  1.00 20.61  ? 85  GLN B O     1 
ATOM   2381 C CB    . GLN B 1 97  ? 39.414  -9.496  -10.356 1.00 21.76  ? 85  GLN B CB    1 
ATOM   2382 C CG    . GLN B 1 97  ? 39.847  -9.242  -11.795 1.00 23.42  ? 85  GLN B CG    1 
ATOM   2383 C CD    . GLN B 1 97  ? 39.675  -10.444 -12.691 1.00 23.37  ? 85  GLN B CD    1 
ATOM   2384 O OE1   . GLN B 1 97  ? 40.182  -11.548 -12.375 1.00 26.24  ? 85  GLN B OE1   1 
ATOM   2385 N NE2   . GLN B 1 97  ? 39.030  -10.285 -13.820 1.00 22.78  ? 85  GLN B NE2   1 
ATOM   2386 N N     . GLN B 1 98  ? 37.791  -9.205  -7.767  1.00 21.32  ? 86  GLN B N     1 
ATOM   2387 C CA    . GLN B 1 98  ? 37.590  -9.633  -6.389  1.00 22.70  ? 86  GLN B CA    1 
ATOM   2388 C C     . GLN B 1 98  ? 36.120  -9.920  -6.111  1.00 19.91  ? 86  GLN B C     1 
ATOM   2389 O O     . GLN B 1 98  ? 35.791  -10.883 -5.386  1.00 23.46  ? 86  GLN B O     1 
ATOM   2390 C CB    . GLN B 1 98  ? 38.077  -8.515  -5.477  1.00 26.00  ? 86  GLN B CB    1 
ATOM   2391 C CG    . GLN B 1 98  ? 38.821  -8.975  -4.284  1.00 35.73  ? 86  GLN B CG    1 
ATOM   2392 C CD    . GLN B 1 98  ? 39.397  -7.830  -3.466  1.00 32.69  ? 86  GLN B CD    1 
ATOM   2393 O OE1   . GLN B 1 98  ? 39.847  -6.811  -4.011  1.00 27.79  ? 86  GLN B OE1   1 
ATOM   2394 N NE2   . GLN B 1 98  ? 39.335  -7.977  -2.147  1.00 32.30  ? 86  GLN B NE2   1 
ATOM   2395 N N     . THR B 1 99  ? 35.242  -9.070  -6.624  1.00 19.71  ? 87  THR B N     1 
ATOM   2396 C CA    . THR B 1 99  ? 33.813  -9.299  -6.455  1.00 20.17  ? 87  THR B CA    1 
ATOM   2397 C C     . THR B 1 99  ? 33.404  -10.586 -7.151  1.00 19.70  ? 87  THR B C     1 
ATOM   2398 O O     . THR B 1 99  ? 32.656  -11.404 -6.579  1.00 19.61  ? 87  THR B O     1 
ATOM   2399 C CB    . THR B 1 99  ? 33.015  -8.109  -6.977  1.00 18.67  ? 87  THR B CB    1 
ATOM   2400 O OG1   . THR B 1 99  ? 33.478  -6.914  -6.304  1.00 19.87  ? 87  THR B OG1   1 
ATOM   2401 C CG2   . THR B 1 99  ? 31.543  -8.307  -6.633  1.00 18.64  ? 87  THR B CG2   1 
ATOM   2402 N N     . ALA B 1 100 ? 33.836  -10.761 -8.406  1.00 19.47  ? 88  ALA B N     1 
ATOM   2403 C CA    . ALA B 1 100 ? 33.522  -11.976 -9.163  1.00 19.98  ? 88  ALA B CA    1 
ATOM   2404 C C     . ALA B 1 100 ? 34.030  -13.220 -8.472  1.00 19.94  ? 88  ALA B C     1 
ATOM   2405 O O     . ALA B 1 100 ? 33.341  -14.243 -8.487  1.00 20.65  ? 88  ALA B O     1 
ATOM   2406 C CB    . ALA B 1 100 ? 34.056  -11.902 -10.593 1.00 21.72  ? 88  ALA B CB    1 
ATOM   2407 N N     . SER B 1 101 ? 35.225  -13.164 -7.865  1.00 20.59  ? 89  SER B N     1 
ATOM   2408 C CA    A SER B 1 101 ? 35.800  -14.336 -7.215  0.70 20.38  ? 89  SER B CA    1 
ATOM   2409 C CA    B SER B 1 101 ? 35.776  -14.357 -7.240  0.30 20.41  ? 89  SER B CA    1 
ATOM   2410 C C     . SER B 1 101 ? 34.926  -14.773 -6.050  1.00 22.80  ? 89  SER B C     1 
ATOM   2411 O O     . SER B 1 101 ? 34.700  -15.973 -5.836  1.00 22.37  ? 89  SER B O     1 
ATOM   2412 C CB    A SER B 1 101 ? 37.188  -13.970 -6.696  0.70 25.15  ? 89  SER B CB    1 
ATOM   2413 C CB    B SER B 1 101 ? 37.238  -14.131 -6.848  0.30 25.26  ? 89  SER B CB    1 
ATOM   2414 O OG    A SER B 1 101 ? 37.813  -15.092 -6.123  0.70 28.61  ? 89  SER B OG    1 
ATOM   2415 O OG    B SER B 1 101 ? 38.071  -14.067 -8.001  0.30 20.68  ? 89  SER B OG    1 
ATOM   2416 N N     . ALA B 1 102 ? 34.405  -13.806 -5.290  1.00 22.69  ? 90  ALA B N     1 
ATOM   2417 C CA    . ALA B 1 102 ? 33.517  -14.138 -4.178  1.00 24.84  ? 90  ALA B CA    1 
ATOM   2418 C C     . ALA B 1 102 ? 32.253  -14.835 -4.672  1.00 22.28  ? 90  ALA B C     1 
ATOM   2419 O O     . ALA B 1 102 ? 31.838  -15.845 -4.087  1.00 23.24  ? 90  ALA B O     1 
ATOM   2420 C CB    . ALA B 1 102 ? 33.127  -12.863 -3.435  1.00 23.57  ? 90  ALA B CB    1 
ATOM   2421 N N     . VAL B 1 103 ? 31.655  -14.340 -5.749  1.00 21.89  ? 91  VAL B N     1 
ATOM   2422 C CA    . VAL B 1 103 ? 30.443  -14.947 -6.303  1.00 21.93  ? 91  VAL B CA    1 
ATOM   2423 C C     . VAL B 1 103 ? 30.751  -16.344 -6.817  1.00 20.85  ? 91  VAL B C     1 
ATOM   2424 O O     . VAL B 1 103 ? 30.057  -17.313 -6.468  1.00 22.83  ? 91  VAL B O     1 
ATOM   2425 C CB    . VAL B 1 103 ? 29.889  -14.070 -7.428  1.00 20.26  ? 91  VAL B CB    1 
ATOM   2426 C CG1   . VAL B 1 103 ? 28.768  -14.766 -8.164  1.00 21.23  ? 91  VAL B CG1   1 
ATOM   2427 C CG2   . VAL B 1 103 ? 29.327  -12.730 -6.872  1.00 23.27  ? 91  VAL B CG2   1 
ATOM   2428 N N     . ALA B 1 104 ? 31.826  -16.478 -7.610  1.00 21.06  ? 92  ALA B N     1 
ATOM   2429 C CA    . ALA B 1 104 ? 32.122  -17.733 -8.310  1.00 20.21  ? 92  ALA B CA    1 
ATOM   2430 C C     . ALA B 1 104 ? 32.457  -18.846 -7.346  1.00 21.39  ? 92  ALA B C     1 
ATOM   2431 O O     . ALA B 1 104 ? 32.169  -20.015 -7.633  1.00 22.92  ? 92  ALA B O     1 
ATOM   2432 C CB    . ALA B 1 104 ? 33.336  -17.505 -9.221  1.00 21.72  ? 92  ALA B CB    1 
ATOM   2433 N N     . ALA B 1 105 ? 33.037  -18.505 -6.191  1.00 22.91  ? 93  ALA B N     1 
ATOM   2434 C CA    . ALA B 1 105 ? 33.506  -19.513 -5.262  1.00 25.73  ? 93  ALA B CA    1 
ATOM   2435 C C     . ALA B 1 105 ? 32.375  -20.325 -4.676  1.00 28.48  ? 93  ALA B C     1 
ATOM   2436 O O     . ALA B 1 105 ? 32.608  -21.456 -4.249  1.00 31.08  ? 93  ALA B O     1 
ATOM   2437 C CB    . ALA B 1 105 ? 34.319  -18.898 -4.125  1.00 28.08  ? 93  ALA B CB    1 
ATOM   2438 N N     . GLU B 1 106 ? 31.157  -19.814 -4.669  1.00 25.41  ? 94  GLU B N     1 
ATOM   2439 C CA    . GLU B 1 106 ? 30.032  -20.583 -4.148  1.00 26.67  ? 94  GLU B CA    1 
ATOM   2440 C C     . GLU B 1 106 ? 29.465  -21.546 -5.182  1.00 29.18  ? 94  GLU B C     1 
ATOM   2441 O O     . GLU B 1 106 ? 28.470  -22.222 -4.890  1.00 30.53  ? 94  GLU B O     1 
ATOM   2442 C CB    . GLU B 1 106 ? 28.913  -19.633 -3.697  1.00 27.92  ? 94  GLU B CB    1 
ATOM   2443 C CG    . GLU B 1 106 ? 29.303  -18.611 -2.641  1.00 28.55  ? 94  GLU B CG    1 
ATOM   2444 C CD    . GLU B 1 106 ? 29.730  -19.230 -1.334  1.00 37.56  ? 94  GLU B CD    1 
ATOM   2445 O OE1   . GLU B 1 106 ? 29.158  -20.264 -0.924  1.00 38.16  ? 94  GLU B OE1   1 
ATOM   2446 O OE2   . GLU B 1 106 ? 30.640  -18.665 -0.693  1.00 39.07  ? 94  GLU B OE2   1 
ATOM   2447 N N     . HIS B 1 107 ? 30.055  -21.611 -6.377  1.00 24.63  ? 95  HIS B N     1 
ATOM   2448 C CA    . HIS B 1 107 ? 29.524  -22.409 -7.477  1.00 25.88  ? 95  HIS B CA    1 
ATOM   2449 C C     . HIS B 1 107 ? 30.590  -23.267 -8.121  1.00 25.27  ? 95  HIS B C     1 
ATOM   2450 O O     . HIS B 1 107 ? 30.286  -23.962 -9.098  1.00 27.84  ? 95  HIS B O     1 
ATOM   2451 C CB    . HIS B 1 107 ? 28.879  -21.521 -8.552  1.00 23.42  ? 95  HIS B CB    1 
ATOM   2452 C CG    . HIS B 1 107 ? 27.802  -20.639 -8.008  1.00 22.67  ? 95  HIS B CG    1 
ATOM   2453 N ND1   . HIS B 1 107 ? 26.482  -21.027 -7.955  1.00 27.77  ? 95  HIS B ND1   1 
ATOM   2454 C CD2   . HIS B 1 107 ? 27.856  -19.392 -7.469  1.00 25.36  ? 95  HIS B CD2   1 
ATOM   2455 C CE1   . HIS B 1 107 ? 25.767  -20.059 -7.406  1.00 26.63  ? 95  HIS B CE1   1 
ATOM   2456 N NE2   . HIS B 1 107 ? 26.572  -19.058 -7.103  1.00 26.43  ? 95  HIS B NE2   1 
ATOM   2457 N N     . GLY B 1 108 ? 31.831  -23.219 -7.644  1.00 24.34  ? 96  GLY B N     1 
ATOM   2458 C CA    . GLY B 1 108 ? 32.862  -24.021 -8.282  1.00 26.96  ? 96  GLY B CA    1 
ATOM   2459 C C     . GLY B 1 108 ? 33.203  -23.539 -9.677  1.00 28.21  ? 96  GLY B C     1 
ATOM   2460 O O     . GLY B 1 108 ? 33.693  -24.318 -10.501 1.00 29.61  ? 96  GLY B O     1 
ATOM   2461 N N     . LEU B 1 109 ? 32.989  -22.265 -9.952  1.00 23.35  ? 97  LEU B N     1 
ATOM   2462 C CA    . LEU B 1 109 ? 33.247  -21.702 -11.266 1.00 23.68  ? 97  LEU B CA    1 
ATOM   2463 C C     . LEU B 1 109 ? 34.539  -20.893 -11.284 1.00 26.26  ? 97  LEU B C     1 
ATOM   2464 O O     . LEU B 1 109 ? 34.877  -20.194 -10.323 1.00 25.42  ? 97  LEU B O     1 
ATOM   2465 C CB    . LEU B 1 109 ? 32.109  -20.778 -11.705 1.00 23.18  ? 97  LEU B CB    1 
ATOM   2466 C CG    . LEU B 1 109 ? 30.797  -21.514 -11.919 1.00 22.99  ? 97  LEU B CG    1 
ATOM   2467 C CD1   . LEU B 1 109 ? 29.678  -20.471 -11.915 1.00 24.55  ? 97  LEU B CD1   1 
ATOM   2468 C CD2   . LEU B 1 109 ? 30.822  -22.247 -13.249 1.00 28.49  ? 97  LEU B CD2   1 
ATOM   2469 N N     . ARG B 1 110 ? 35.203  -20.906 -12.434 1.00 26.85  ? 98  ARG B N     1 
ATOM   2470 C CA    . ARG B 1 110 ? 36.381  -20.075 -12.644 1.00 24.87  ? 98  ARG B CA    1 
ATOM   2471 C C     . ARG B 1 110 ? 35.984  -18.713 -13.199 1.00 27.30  ? 98  ARG B C     1 
ATOM   2472 O O     . ARG B 1 110 ? 35.247  -18.642 -14.182 1.00 30.17  ? 98  ARG B O     1 
ATOM   2473 C CB    . ARG B 1 110 ? 37.280  -20.739 -13.679 1.00 29.59  ? 98  ARG B CB    1 
ATOM   2474 C CG    . ARG B 1 110 ? 38.323  -21.688 -13.115 1.00 45.90  ? 98  ARG B CG    1 
ATOM   2475 C CD    . ARG B 1 110 ? 39.270  -22.176 -14.218 1.00 58.65  ? 98  ARG B CD    1 
ATOM   2476 N NE    . ARG B 1 110 ? 39.650  -21.130 -15.168 1.00 67.35  ? 98  ARG B NE    1 
ATOM   2477 C CZ    . ARG B 1 110 ? 39.124  -20.981 -16.380 1.00 74.05  ? 98  ARG B CZ    1 
ATOM   2478 N NH1   . ARG B 1 110 ? 38.163  -21.779 -16.823 1.00 68.37  ? 98  ARG B NH1   1 
ATOM   2479 N NH2   . ARG B 1 110 ? 39.571  -20.005 -17.166 1.00 75.47  ? 98  ARG B NH2   1 
ATOM   2480 N N     . VAL B 1 111 ? 36.510  -17.642 -12.601 1.00 24.58  ? 99  VAL B N     1 
ATOM   2481 C CA    . VAL B 1 111 ? 36.300  -16.305 -13.137 1.00 22.62  ? 99  VAL B CA    1 
ATOM   2482 C C     . VAL B 1 111 ? 37.036  -16.158 -14.456 1.00 23.59  ? 99  VAL B C     1 
ATOM   2483 O O     . VAL B 1 111 ? 38.232  -16.470 -14.549 1.00 26.23  ? 99  VAL B O     1 
ATOM   2484 C CB    . VAL B 1 111 ? 36.764  -15.243 -12.131 1.00 24.79  ? 99  VAL B CB    1 
ATOM   2485 C CG1   . VAL B 1 111 ? 36.734  -13.867 -12.762 1.00 26.54  ? 99  VAL B CG1   1 
ATOM   2486 C CG2   . VAL B 1 111 ? 35.941  -15.315 -10.820 1.00 25.43  ? 99  VAL B CG2   1 
ATOM   2487 N N     . ARG B 1 112 ? 36.341  -15.691 -15.484 1.00 20.61  ? 100 ARG B N     1 
ATOM   2488 C CA    . ARG B 1 112 ? 36.969  -15.354 -16.749 1.00 21.79  ? 100 ARG B CA    1 
ATOM   2489 C C     . ARG B 1 112 ? 36.946  -13.848 -16.960 1.00 20.07  ? 100 ARG B C     1 
ATOM   2490 O O     . ARG B 1 112 ? 36.007  -13.171 -16.555 1.00 20.05  ? 100 ARG B O     1 
ATOM   2491 C CB    . ARG B 1 112 ? 36.332  -16.123 -17.892 1.00 24.48  ? 100 ARG B CB    1 
ATOM   2492 C CG    . ARG B 1 112 ? 36.683  -17.666 -17.752 1.00 31.05  ? 100 ARG B CG    1 
ATOM   2493 C CD    . ARG B 1 112 ? 36.399  -18.463 -19.017 1.00 39.93  ? 100 ARG B CD    1 
ATOM   2494 N NE    . ARG B 1 112 ? 37.275  -18.105 -20.124 1.00 51.09  ? 100 ARG B NE    1 
ATOM   2495 C CZ    . ARG B 1 112 ? 37.151  -18.561 -21.364 1.00 57.67  ? 100 ARG B CZ    1 
ATOM   2496 N NH1   . ARG B 1 112 ? 36.201  -19.427 -21.695 1.00 54.42  ? 100 ARG B NH1   1 
ATOM   2497 N NH2   . ARG B 1 112 ? 38.005  -18.146 -22.297 1.00 56.09  ? 100 ARG B NH2   1 
ATOM   2498 N N     . THR B 1 113 ? 37.938  -13.328 -17.664 1.00 19.50  ? 101 THR B N     1 
ATOM   2499 C CA    . THR B 1 113 ? 38.132  -11.890 -17.794 1.00 18.41  ? 101 THR B CA    1 
ATOM   2500 C C     . THR B 1 113 ? 37.837  -11.488 -19.230 1.00 20.26  ? 101 THR B C     1 
ATOM   2501 O O     . THR B 1 113 ? 38.281  -12.120 -20.181 1.00 21.49  ? 101 THR B O     1 
ATOM   2502 C CB    . THR B 1 113 ? 39.598  -11.517 -17.516 1.00 23.30  ? 101 THR B CB    1 
ATOM   2503 O OG1   . THR B 1 113 ? 39.874  -11.712 -16.132 1.00 25.61  ? 101 THR B OG1   1 
ATOM   2504 C CG2   . THR B 1 113 ? 39.843  -10.018 -17.856 1.00 25.04  ? 101 THR B CG2   1 
ATOM   2505 N N     . ASP B 1 114 ? 37.128  -10.361 -19.377 1.00 19.37  ? 102 ASP B N     1 
ATOM   2506 C CA    . ASP B 1 114 ? 36.950  -9.751  -20.690 1.00 19.45  ? 102 ASP B CA    1 
ATOM   2507 C C     . ASP B 1 114 ? 37.158  -8.251  -20.520 1.00 21.20  ? 102 ASP B C     1 
ATOM   2508 O O     . ASP B 1 114 ? 36.327  -7.551  -19.905 1.00 19.74  ? 102 ASP B O     1 
ATOM   2509 C CB    . ASP B 1 114 ? 35.557  -10.043 -21.254 1.00 20.88  ? 102 ASP B CB    1 
ATOM   2510 C CG    . ASP B 1 114 ? 35.417  -9.612  -22.708 1.00 21.63  ? 102 ASP B CG    1 
ATOM   2511 O OD1   . ASP B 1 114 ? 36.191  -8.771  -23.214 1.00 21.60  ? 102 ASP B OD1   1 
ATOM   2512 O OD2   . ASP B 1 114 ? 34.563  -10.175 -23.429 1.00 25.96  ? 102 ASP B OD2   1 
ATOM   2513 N N     . ALA B 1 115 ? 38.232  -7.739  -21.099 1.00 21.21  ? 103 ALA B N     1 
ATOM   2514 C CA    . ALA B 1 115 ? 38.538  -6.317  -20.946 1.00 20.87  ? 103 ALA B CA    1 
ATOM   2515 C C     . ALA B 1 115 ? 37.527  -5.420  -21.625 1.00 20.53  ? 103 ALA B C     1 
ATOM   2516 O O     . ALA B 1 115 ? 37.484  -4.213  -21.324 1.00 20.96  ? 103 ALA B O     1 
ATOM   2517 C CB    . ALA B 1 115 ? 39.931  -5.995  -21.482 1.00 27.47  ? 103 ALA B CB    1 
ATOM   2518 N N     . ARG B 1 116 ? 36.663  -5.958  -22.483 1.00 18.89  ? 104 ARG B N     1 
ATOM   2519 C CA    . ARG B 1 116 ? 35.595  -5.157  -23.050 1.00 18.99  ? 104 ARG B CA    1 
ATOM   2520 C C     . ARG B 1 116 ? 34.531  -4.819  -22.027 1.00 18.47  ? 104 ARG B C     1 
ATOM   2521 O O     . ARG B 1 116 ? 33.658  -3.988  -22.336 1.00 17.64  ? 104 ARG B O     1 
ATOM   2522 C CB    . ARG B 1 116 ? 34.984  -5.852  -24.261 1.00 20.37  ? 104 ARG B CB    1 
ATOM   2523 C CG    . ARG B 1 116 ? 35.999  -6.079  -25.401 1.00 23.52  ? 104 ARG B CG    1 
ATOM   2524 C CD    . ARG B 1 116 ? 35.452  -6.959  -26.486 1.00 26.58  ? 104 ARG B CD    1 
ATOM   2525 N NE    . ARG B 1 116 ? 35.249  -8.326  -25.989 1.00 25.65  ? 104 ARG B NE    1 
ATOM   2526 C CZ    . ARG B 1 116 ? 35.047  -9.383  -26.766 1.00 28.42  ? 104 ARG B CZ    1 
ATOM   2527 N NH1   . ARG B 1 116 ? 35.048  -9.289  -28.087 1.00 31.04  ? 104 ARG B NH1   1 
ATOM   2528 N NH2   . ARG B 1 116 ? 34.831  -10.568 -26.191 1.00 28.27  ? 104 ARG B NH2   1 
ATOM   2529 N N     . LEU B 1 117 ? 34.595  -5.357  -20.823 1.00 18.18  ? 105 LEU B N     1 
ATOM   2530 C CA    . LEU B 1 117 ? 33.701  -4.998  -19.739 1.00 16.86  ? 105 LEU B CA    1 
ATOM   2531 C C     . LEU B 1 117 ? 34.255  -3.854  -18.884 1.00 18.09  ? 105 LEU B C     1 
ATOM   2532 O O     . LEU B 1 117 ? 33.669  -3.526  -17.841 1.00 18.06  ? 105 LEU B O     1 
ATOM   2533 C CB    . LEU B 1 117 ? 33.471  -6.259  -18.852 1.00 17.02  ? 105 LEU B CB    1 
ATOM   2534 C CG    . LEU B 1 117 ? 32.744  -7.428  -19.493 1.00 16.60  ? 105 LEU B CG    1 
ATOM   2535 C CD1   . LEU B 1 117 ? 32.833  -8.711  -18.577 1.00 17.73  ? 105 LEU B CD1   1 
ATOM   2536 C CD2   . LEU B 1 117 ? 31.299  -7.034  -19.726 1.00 18.71  ? 105 LEU B CD2   1 
ATOM   2537 N N     . ARG B 1 118 ? 35.407  -3.299  -19.252 1.00 17.48  ? 106 ARG B N     1 
ATOM   2538 C CA    . ARG B 1 118 ? 36.006  -2.201  -18.465 1.00 17.47  ? 106 ARG B CA    1 
ATOM   2539 C C     . ARG B 1 118 ? 35.057  -0.987  -18.369 1.00 16.03  ? 106 ARG B C     1 
ATOM   2540 O O     . ARG B 1 118 ? 34.157  -0.789  -19.193 1.00 17.02  ? 106 ARG B O     1 
ATOM   2541 C CB    . ARG B 1 118 ? 37.329  -1.741  -19.104 1.00 19.13  ? 106 ARG B CB    1 
ATOM   2542 C CG    . ARG B 1 118 ? 37.144  -1.115  -20.491 1.00 19.59  ? 106 ARG B CG    1 
ATOM   2543 C CD    . ARG B 1 118 ? 38.542  -0.894  -21.190 1.00 21.96  ? 106 ARG B CD    1 
ATOM   2544 N NE    . ARG B 1 118 ? 38.347  -0.330  -22.522 1.00 25.63  ? 106 ARG B NE    1 
ATOM   2545 C CZ    . ARG B 1 118 ? 38.149  -1.018  -23.635 1.00 28.37  ? 106 ARG B CZ    1 
ATOM   2546 N NH1   . ARG B 1 118 ? 38.030  -2.336  -23.614 1.00 27.66  ? 106 ARG B NH1   1 
ATOM   2547 N NH2   . ARG B 1 118 ? 38.052  -0.367  -24.798 1.00 31.02  ? 106 ARG B NH2   1 
ATOM   2548 N N     . GLU B 1 119 ? 35.262  -0.195  -17.294 1.00 18.26  ? 107 GLU B N     1 
ATOM   2549 C CA    . GLU B 1 119 ? 34.448  1.013   -17.189 1.00 18.01  ? 107 GLU B CA    1 
ATOM   2550 C C     . GLU B 1 119 ? 34.732  1.933   -18.369 1.00 18.41  ? 107 GLU B C     1 
ATOM   2551 O O     . GLU B 1 119 ? 35.773  1.864   -19.012 1.00 18.00  ? 107 GLU B O     1 
ATOM   2552 C CB    . GLU B 1 119 ? 34.741  1.704   -15.851 1.00 20.67  ? 107 GLU B CB    1 
ATOM   2553 C CG    . GLU B 1 119 ? 33.917  2.985   -15.491 1.00 18.76  ? 107 GLU B CG    1 
ATOM   2554 C CD    . GLU B 1 119 ? 32.398  2.824   -15.531 1.00 20.87  ? 107 GLU B CD    1 
ATOM   2555 O OE1   . GLU B 1 119 ? 31.855  2.440   -16.591 1.00 21.13  ? 107 GLU B OE1   1 
ATOM   2556 O OE2   . GLU B 1 119 ? 31.714  3.146   -14.531 1.00 21.80  ? 107 GLU B OE2   1 
ATOM   2557 N N     . VAL B 1 120 ? 33.760  2.785   -18.632 1.00 18.46  ? 108 VAL B N     1 
ATOM   2558 C CA    A VAL B 1 120 ? 33.971  3.875   -19.586 0.70 19.66  ? 108 VAL B CA    1 
ATOM   2559 C CA    B VAL B 1 120 ? 33.985  3.865   -19.593 0.30 19.45  ? 108 VAL B CA    1 
ATOM   2560 C C     . VAL B 1 120 ? 35.275  4.611   -19.256 1.00 19.73  ? 108 VAL B C     1 
ATOM   2561 O O     . VAL B 1 120 ? 35.613  4.819   -18.078 1.00 20.70  ? 108 VAL B O     1 
ATOM   2562 C CB    A VAL B 1 120 ? 32.747  4.808   -19.589 0.70 20.20  ? 108 VAL B CB    1 
ATOM   2563 C CB    B VAL B 1 120 ? 32.795  4.838   -19.620 0.30 20.03  ? 108 VAL B CB    1 
ATOM   2564 C CG1   A VAL B 1 120 ? 32.558  5.526   -18.231 0.70 21.45  ? 108 VAL B CG1   1 
ATOM   2565 C CG1   B VAL B 1 120 ? 32.924  5.786   -20.805 0.30 21.43  ? 108 VAL B CG1   1 
ATOM   2566 C CG2   A VAL B 1 120 ? 32.825  5.818   -20.742 0.70 21.63  ? 108 VAL B CG2   1 
ATOM   2567 C CG2   B VAL B 1 120 ? 31.490  4.097   -19.689 0.30 19.47  ? 108 VAL B CG2   1 
ATOM   2568 N N     . ARG B 1 121 ? 36.020  4.989   -20.291 1.00 19.12  ? 109 ARG B N     1 
ATOM   2569 C CA    A ARG B 1 121 ? 37.200  5.826   -20.060 0.60 21.14  ? 109 ARG B CA    1 
ATOM   2570 C CA    B ARG B 1 121 ? 37.197  5.830   -20.061 0.40 21.06  ? 109 ARG B CA    1 
ATOM   2571 C C     . ARG B 1 121 ? 36.752  7.183   -19.508 1.00 21.97  ? 109 ARG B C     1 
ATOM   2572 O O     . ARG B 1 121 ? 35.811  7.801   -20.021 1.00 22.15  ? 109 ARG B O     1 
ATOM   2573 C CB    A ARG B 1 121 ? 38.001  5.998   -21.352 0.60 22.17  ? 109 ARG B CB    1 
ATOM   2574 C CB    B ARG B 1 121 ? 37.984  6.016   -21.358 0.40 22.18  ? 109 ARG B CB    1 
ATOM   2575 C CG    A ARG B 1 121 ? 39.390  6.588   -21.115 0.60 25.53  ? 109 ARG B CG    1 
ATOM   2576 C CG    B ARG B 1 121 ? 39.174  6.965   -21.221 0.40 24.62  ? 109 ARG B CG    1 
ATOM   2577 C CD    A ARG B 1 121 ? 40.209  6.662   -22.398 0.60 27.88  ? 109 ARG B CD    1 
ATOM   2578 C CD    B ARG B 1 121 ? 40.104  6.835   -22.422 0.40 27.83  ? 109 ARG B CD    1 
ATOM   2579 N NE    A ARG B 1 121 ? 39.888  7.824   -23.224 0.60 34.10  ? 109 ARG B NE    1 
ATOM   2580 N NE    B ARG B 1 121 ? 39.385  7.014   -23.678 0.40 29.70  ? 109 ARG B NE    1 
ATOM   2581 C CZ    A ARG B 1 121 ? 39.167  7.779   -24.340 0.60 32.64  ? 109 ARG B CZ    1 
ATOM   2582 C CZ    B ARG B 1 121 ? 39.299  8.162   -24.341 0.40 30.19  ? 109 ARG B CZ    1 
ATOM   2583 N NH1   A ARG B 1 121 ? 38.635  6.643   -24.778 0.60 35.22  ? 109 ARG B NH1   1 
ATOM   2584 N NH1   B ARG B 1 121 ? 39.919  9.252   -23.920 0.40 25.11  ? 109 ARG B NH1   1 
ATOM   2585 N NH2   A ARG B 1 121 ? 38.989  8.894   -25.044 0.60 32.50  ? 109 ARG B NH2   1 
ATOM   2586 N NH2   B ARG B 1 121 ? 38.564  8.218   -25.450 0.40 30.40  ? 109 ARG B NH2   1 
ATOM   2587 N N     . THR B 1 122 ? 37.401  7.623   -18.422 1.00 21.36  ? 110 THR B N     1 
ATOM   2588 C CA    . THR B 1 122 ? 37.025  8.854   -17.721 1.00 22.34  ? 110 THR B CA    1 
ATOM   2589 C C     . THR B 1 122 ? 38.034  9.978   -17.929 1.00 23.80  ? 110 THR B C     1 
ATOM   2590 O O     . THR B 1 122 ? 39.184  9.778   -18.356 1.00 23.83  ? 110 THR B O     1 
ATOM   2591 C CB    . THR B 1 122 ? 36.960  8.629   -16.207 1.00 23.35  ? 110 THR B CB    1 
ATOM   2592 O OG1   . THR B 1 122 ? 38.282  8.242   -15.737 1.00 25.04  ? 110 THR B OG1   1 
ATOM   2593 C CG2   . THR B 1 122 ? 35.969  7.548   -15.870 1.00 22.34  ? 110 THR B CG2   1 
ATOM   2594 N N     . ASN B 1 123 ? 37.589  11.189  -17.570 1.00 24.00  ? 111 ASN B N     1 
ATOM   2595 C CA    . ASN B 1 123 ? 38.516  12.312  -17.454 1.00 26.34  ? 111 ASN B CA    1 
ATOM   2596 C C     . ASN B 1 123 ? 39.746  11.949  -16.614 1.00 27.95  ? 111 ASN B C     1 
ATOM   2597 O O     . ASN B 1 123 ? 40.879  12.243  -17.003 1.00 28.19  ? 111 ASN B O     1 
ATOM   2598 C CB    . ASN B 1 123 ? 37.821  13.530  -16.849 1.00 28.14  ? 111 ASN B CB    1 
ATOM   2599 C CG    . ASN B 1 123 ? 36.975  14.279  -17.840 1.00 31.61  ? 111 ASN B CG    1 
ATOM   2600 O OD1   . ASN B 1 123 ? 36.993  14.005  -19.016 1.00 32.10  ? 111 ASN B OD1   1 
ATOM   2601 N ND2   . ASN B 1 123 ? 36.347  15.341  -17.375 1.00 41.18  ? 111 ASN B ND2   1 
ATOM   2602 N N     . TRP B 1 124 ? 39.532  11.352  -15.436 1.00 28.41  ? 112 TRP B N     1 
ATOM   2603 C CA    . TRP B 1 124 ? 40.654  10.972  -14.572 1.00 30.79  ? 112 TRP B CA    1 
ATOM   2604 C C     . TRP B 1 124 ? 41.612  10.000  -15.276 1.00 29.31  ? 112 TRP B C     1 
ATOM   2605 O O     . TRP B 1 124 ? 42.837  10.165  -15.165 1.00 32.05  ? 112 TRP B O     1 
ATOM   2606 C CB    . TRP B 1 124 ? 40.154  10.364  -13.263 1.00 30.26  ? 112 TRP B CB    1 
ATOM   2607 C CG    . TRP B 1 124 ? 41.241  10.262  -12.220 1.00 32.06  ? 112 TRP B CG    1 
ATOM   2608 C CD1   . TRP B 1 124 ? 42.395  10.965  -12.184 1.00 39.33  ? 112 TRP B CD1   1 
ATOM   2609 C CD2   . TRP B 1 124 ? 41.287  9.348   -11.114 1.00 32.66  ? 112 TRP B CD2   1 
ATOM   2610 N NE1   . TRP B 1 124 ? 43.152  10.604  -11.095 1.00 45.20  ? 112 TRP B NE1   1 
ATOM   2611 C CE2   . TRP B 1 124 ? 42.505  9.598   -10.429 1.00 34.71  ? 112 TRP B CE2   1 
ATOM   2612 C CE3   . TRP B 1 124 ? 40.422  8.357   -10.635 1.00 34.41  ? 112 TRP B CE3   1 
ATOM   2613 C CZ2   . TRP B 1 124 ? 42.876  8.899   -9.282  1.00 46.31  ? 112 TRP B CZ2   1 
ATOM   2614 C CZ3   . TRP B 1 124 ? 40.790  7.658   -9.479  1.00 37.83  ? 112 TRP B CZ3   1 
ATOM   2615 C CH2   . TRP B 1 124 ? 42.011  7.954   -8.812  1.00 37.15  ? 112 TRP B CH2   1 
ATOM   2616 N N     . ASP B 1 125 ? 41.093  9.052   -16.061 1.00 27.83  ? 113 ASP B N     1 
ATOM   2617 C CA    . ASP B 1 125 ? 41.967  8.159   -16.837 1.00 30.55  ? 113 ASP B CA    1 
ATOM   2618 C C     . ASP B 1 125 ? 42.838  8.925   -17.815 1.00 29.48  ? 113 ASP B C     1 
ATOM   2619 O O     . ASP B 1 125 ? 43.974  8.508   -18.080 1.00 34.43  ? 113 ASP B O     1 
ATOM   2620 C CB    . ASP B 1 125 ? 41.174  7.179   -17.686 1.00 24.76  ? 113 ASP B CB    1 
ATOM   2621 C CG    . ASP B 1 125 ? 40.453  6.129   -16.872 1.00 28.30  ? 113 ASP B CG    1 
ATOM   2622 O OD1   . ASP B 1 125 ? 40.909  5.762   -15.761 1.00 29.07  ? 113 ASP B OD1   1 
ATOM   2623 O OD2   . ASP B 1 125 ? 39.401  5.685   -17.352 1.00 23.65  ? 113 ASP B OD2   1 
ATOM   2624 N N     . ASP B 1 126 ? 42.340  10.049  -18.360 1.00 28.34  ? 114 ASP B N     1 
ATOM   2625 C CA    . ASP B 1 126 ? 43.090  10.928  -19.255 1.00 32.01  ? 114 ASP B CA    1 
ATOM   2626 C C     . ASP B 1 126 ? 43.949  11.939  -18.500 1.00 32.19  ? 114 ASP B C     1 
ATOM   2627 O O     . ASP B 1 126 ? 44.580  12.788  -19.144 1.00 37.72  ? 114 ASP B O     1 
ATOM   2628 C CB    . ASP B 1 126 ? 42.143  11.718  -20.190 1.00 34.36  ? 114 ASP B CB    1 
ATOM   2629 C CG    . ASP B 1 126 ? 41.398  10.833  -21.216 1.00 37.71  ? 114 ASP B CG    1 
ATOM   2630 O OD1   . ASP B 1 126 ? 41.820  9.694   -21.474 1.00 38.95  ? 114 ASP B OD1   1 
ATOM   2631 O OD2   . ASP B 1 126 ? 40.386  11.309  -21.783 1.00 48.90  ? 114 ASP B OD2   1 
ATOM   2632 N N     . GLY B 1 127 ? 43.975  11.882  -17.168 1.00 34.22  ? 115 GLY B N     1 
ATOM   2633 C CA    . GLY B 1 127 ? 44.799  12.768  -16.371 1.00 38.41  ? 115 GLY B CA    1 
ATOM   2634 C C     . GLY B 1 127 ? 44.179  14.103  -16.064 1.00 37.85  ? 115 GLY B C     1 
ATOM   2635 O O     . GLY B 1 127 ? 44.902  15.053  -15.737 1.00 42.82  ? 115 GLY B O     1 
ATOM   2636 N N     . ARG B 1 128 ? 42.868  14.223  -16.185 1.00 37.00  ? 116 ARG B N     1 
ATOM   2637 C CA    . ARG B 1 128 ? 42.224  15.517  -16.054 1.00 33.71  ? 116 ARG B CA    1 
ATOM   2638 C C     . ARG B 1 128 ? 41.296  15.556  -14.849 1.00 36.07  ? 116 ARG B C     1 
ATOM   2639 O O     . ARG B 1 128 ? 40.822  14.512  -14.373 1.00 33.52  ? 116 ARG B O     1 
ATOM   2640 C CB    . ARG B 1 128 ? 41.362  15.787  -17.291 1.00 32.74  ? 116 ARG B CB    1 
ATOM   2641 C CG    . ARG B 1 128 ? 42.112  15.797  -18.640 1.00 38.47  ? 116 ARG B CG    1 
ATOM   2642 C CD    . ARG B 1 128 ? 41.071  16.113  -19.750 1.00 54.97  ? 116 ARG B CD    1 
ATOM   2643 N NE    . ARG B 1 128 ? 41.371  15.488  -21.034 1.00 65.41  ? 116 ARG B NE    1 
ATOM   2644 C CZ    . ARG B 1 128 ? 41.771  16.140  -22.120 1.00 62.47  ? 116 ARG B CZ    1 
ATOM   2645 N NH1   . ARG B 1 128 ? 41.862  17.462  -22.142 1.00 57.71  ? 116 ARG B NH1   1 
ATOM   2646 N NH2   . ARG B 1 128 ? 42.083  15.446  -23.214 1.00 67.59  ? 116 ARG B NH2   1 
ATOM   2647 N N     . PRO B 1 129 ? 40.945  16.760  -14.389 1.00 34.99  ? 117 PRO B N     1 
ATOM   2648 C CA    . PRO B 1 129 ? 39.960  16.895  -13.317 1.00 33.95  ? 117 PRO B CA    1 
ATOM   2649 C C     . PRO B 1 129 ? 38.607  16.362  -13.729 1.00 29.57  ? 117 PRO B C     1 
ATOM   2650 O O     . PRO B 1 129 ? 38.213  16.378  -14.897 1.00 27.28  ? 117 PRO B O     1 
ATOM   2651 C CB    . PRO B 1 129 ? 39.899  18.413  -13.073 1.00 33.80  ? 117 PRO B CB    1 
ATOM   2652 C CG    . PRO B 1 129 ? 41.204  18.923  -13.575 1.00 43.82  ? 117 PRO B CG    1 
ATOM   2653 C CD    . PRO B 1 129 ? 41.496  18.064  -14.775 1.00 36.66  ? 117 PRO B CD    1 
ATOM   2654 N N     . SER B 1 130 ? 37.891  15.896  -12.732 1.00 28.78  ? 118 SER B N     1 
ATOM   2655 C CA    . SER B 1 130 ? 36.551  15.403  -12.932 1.00 27.52  ? 118 SER B CA    1 
ATOM   2656 C C     . SER B 1 130 ? 35.587  16.571  -12.786 1.00 28.35  ? 118 SER B C     1 
ATOM   2657 O O     . SER B 1 130 ? 35.886  17.598  -12.167 1.00 29.09  ? 118 SER B O     1 
ATOM   2658 C CB    . SER B 1 130 ? 36.281  14.309  -11.905 1.00 27.18  ? 118 SER B CB    1 
ATOM   2659 O OG    . SER B 1 130 ? 37.134  13.178  -12.121 1.00 27.52  ? 118 SER B OG    1 
ATOM   2660 N N     . GLU B 1 131 ? 34.435  16.421  -13.410 1.00 25.46  ? 119 GLU B N     1 
ATOM   2661 C CA    . GLU B 1 131 ? 33.398  17.424  -13.379 1.00 25.36  ? 119 GLU B CA    1 
ATOM   2662 C C     . GLU B 1 131 ? 32.039  16.777  -13.161 1.00 22.73  ? 119 GLU B C     1 
ATOM   2663 O O     . GLU B 1 131 ? 31.719  15.787  -13.822 1.00 22.71  ? 119 GLU B O     1 
ATOM   2664 C CB    . GLU B 1 131 ? 33.384  18.174  -14.711 1.00 28.95  ? 119 GLU B CB    1 
ATOM   2665 C CG    . GLU B 1 131 ? 32.416  19.297  -14.722 1.00 31.94  ? 119 GLU B CG    1 
ATOM   2666 C CD    . GLU B 1 131 ? 32.498  20.084  -16.003 1.00 33.55  ? 119 GLU B CD    1 
ATOM   2667 O OE1   . GLU B 1 131 ? 33.063  19.560  -16.996 1.00 29.59  ? 119 GLU B OE1   1 
ATOM   2668 O OE2   . GLU B 1 131 ? 31.957  21.191  -16.005 1.00 40.48  ? 119 GLU B OE2   1 
ATOM   2669 N N     . LEU B 1 132 ? 31.233  17.348  -12.256 1.00 22.99  ? 120 LEU B N     1 
ATOM   2670 C CA    . LEU B 1 132 ? 29.826  16.973  -12.139 1.00 24.40  ? 120 LEU B CA    1 
ATOM   2671 C C     . LEU B 1 132 ? 29.054  17.669  -13.255 1.00 22.76  ? 120 LEU B C     1 
ATOM   2672 O O     . LEU B 1 132 ? 28.926  18.885  -13.236 1.00 24.52  ? 120 LEU B O     1 
ATOM   2673 C CB    . LEU B 1 132 ? 29.304  17.420  -10.775 1.00 25.85  ? 120 LEU B CB    1 
ATOM   2674 C CG    . LEU B 1 132 ? 27.819  17.111  -10.488 1.00 26.77  ? 120 LEU B CG    1 
ATOM   2675 C CD1   . LEU B 1 132 ? 27.562  15.649  -10.431 1.00 28.54  ? 120 LEU B CD1   1 
ATOM   2676 C CD2   . LEU B 1 132 ? 27.408  17.690  -9.161  1.00 30.14  ? 120 LEU B CD2   1 
ATOM   2677 N N     . LYS B 1 133 ? 28.608  16.976  -14.250 1.00 21.47  ? 121 LYS B N     1 
ATOM   2678 C CA    . LYS B 1 133 ? 27.872  17.485  -15.393 1.00 22.17  ? 121 LYS B CA    1 
ATOM   2679 C C     . LYS B 1 133 ? 26.401  17.663  -15.070 1.00 21.70  ? 121 LYS B C     1 
ATOM   2680 O O     . LYS B 1 133 ? 25.854  16.938  -14.244 1.00 23.67  ? 121 LYS B O     1 
ATOM   2681 C CB    . LYS B 1 133 ? 27.944  16.503  -16.563 1.00 19.92  ? 121 LYS B CB    1 
ATOM   2682 C CG    . LYS B 1 133 ? 29.328  16.434  -17.199 1.00 22.16  ? 121 LYS B CG    1 
ATOM   2683 C CD    . LYS B 1 133 ? 29.792  17.781  -17.721 1.00 22.77  ? 121 LYS B CD    1 
ATOM   2684 C CE    . LYS B 1 133 ? 30.842  17.655  -18.845 1.00 24.06  ? 121 LYS B CE    1 
ATOM   2685 N NZ    . LYS B 1 133 ? 31.320  19.011  -19.255 1.00 25.32  ? 121 LYS B NZ    1 
ATOM   2686 N N     . PRO B 1 134 ? 25.748  18.622  -15.719 1.00 21.68  ? 122 PRO B N     1 
ATOM   2687 C CA    . PRO B 1 134 ? 24.294  18.732  -15.614 1.00 23.52  ? 122 PRO B CA    1 
ATOM   2688 C C     . PRO B 1 134 ? 23.674  17.429  -16.099 1.00 21.32  ? 122 PRO B C     1 
ATOM   2689 O O     . PRO B 1 134 ? 24.223  16.746  -16.958 1.00 22.39  ? 122 PRO B O     1 
ATOM   2690 C CB    . PRO B 1 134 ? 23.962  19.879  -16.582 1.00 26.26  ? 122 PRO B CB    1 
ATOM   2691 C CG    . PRO B 1 134 ? 25.259  20.678  -16.709 1.00 24.86  ? 122 PRO B CG    1 
ATOM   2692 C CD    . PRO B 1 134 ? 26.332  19.617  -16.628 1.00 22.62  ? 122 PRO B CD    1 
ATOM   2693 N N     . HIS B 1 135 ? 22.486  17.132  -15.566 1.00 24.80  ? 123 HIS B N     1 
ATOM   2694 C CA    . HIS B 1 135 ? 21.736  15.977  -16.056 1.00 23.28  ? 123 HIS B CA    1 
ATOM   2695 C C     . HIS B 1 135 ? 21.561  16.076  -17.572 1.00 24.25  ? 123 HIS B C     1 
ATOM   2696 O O     . HIS B 1 135 ? 21.240  17.148  -18.105 1.00 26.52  ? 123 HIS B O     1 
ATOM   2697 C CB    . HIS B 1 135 ? 20.383  15.887  -15.343 1.00 28.66  ? 123 HIS B CB    1 
ATOM   2698 C CG    . HIS B 1 135 ? 19.512  14.827  -15.922 1.00 26.11  ? 123 HIS B CG    1 
ATOM   2699 N ND1   . HIS B 1 135 ? 18.413  15.114  -16.686 1.00 30.27  ? 123 HIS B ND1   1 
ATOM   2700 C CD2   . HIS B 1 135 ? 19.680  13.484  -15.988 1.00 25.41  ? 123 HIS B CD2   1 
ATOM   2701 C CE1   . HIS B 1 135 ? 17.871  13.986  -17.119 1.00 32.81  ? 123 HIS B CE1   1 
ATOM   2702 N NE2   . HIS B 1 135 ? 18.639  12.986  -16.726 1.00 27.67  ? 123 HIS B NE2   1 
ATOM   2703 N N     . GLY B 1 136 ? 21.776  14.963  -18.271 1.00 23.48  ? 124 GLY B N     1 
ATOM   2704 C CA    . GLY B 1 136 ? 21.640  14.944  -19.708 1.00 23.65  ? 124 GLY B CA    1 
ATOM   2705 C C     . GLY B 1 136 ? 22.914  15.202  -20.479 1.00 22.22  ? 124 GLY B C     1 
ATOM   2706 O O     . GLY B 1 136 ? 22.946  14.974  -21.696 1.00 28.00  ? 124 GLY B O     1 
ATOM   2707 N N     . VAL B 1 137 ? 23.978  15.622  -19.806 1.00 20.03  ? 125 VAL B N     1 
ATOM   2708 C CA    . VAL B 1 137 ? 25.239  15.927  -20.466 1.00 20.22  ? 125 VAL B CA    1 
ATOM   2709 C C     . VAL B 1 137 ? 26.186  14.759  -20.232 1.00 19.56  ? 125 VAL B C     1 
ATOM   2710 O O     . VAL B 1 137 ? 26.551  14.468  -19.083 1.00 19.59  ? 125 VAL B O     1 
ATOM   2711 C CB    . VAL B 1 137 ? 25.845  17.239  -19.956 1.00 19.29  ? 125 VAL B CB    1 
ATOM   2712 C CG1   . VAL B 1 137 ? 27.184  17.482  -20.653 1.00 21.08  ? 125 VAL B CG1   1 
ATOM   2713 C CG2   . VAL B 1 137 ? 24.906  18.408  -20.228 1.00 23.28  ? 125 VAL B CG2   1 
ATOM   2714 N N     . TYR B 1 138 ? 26.576  14.090  -21.314 1.00 20.46  ? 126 TYR B N     1 
ATOM   2715 C CA    . TYR B 1 138 ? 27.435  12.903  -21.167 1.00 18.49  ? 126 TYR B CA    1 
ATOM   2716 C C     . TYR B 1 138 ? 28.805  13.305  -20.625 1.00 19.63  ? 126 TYR B C     1 
ATOM   2717 O O     . TYR B 1 138 ? 29.423  14.238  -21.158 1.00 21.43  ? 126 TYR B O     1 
ATOM   2718 C CB    . TYR B 1 138 ? 27.559  12.276  -22.554 1.00 22.66  ? 126 TYR B CB    1 
ATOM   2719 C CG    . TYR B 1 138 ? 28.273  10.940  -22.600 1.00 18.05  ? 126 TYR B CG    1 
ATOM   2720 C CD1   . TYR B 1 138 ? 27.692  9.795   -22.111 1.00 18.86  ? 126 TYR B CD1   1 
ATOM   2721 C CD2   . TYR B 1 138 ? 29.535  10.850  -23.182 1.00 19.82  ? 126 TYR B CD2   1 
ATOM   2722 C CE1   . TYR B 1 138 ? 28.343  8.543   -22.184 1.00 20.28  ? 126 TYR B CE1   1 
ATOM   2723 C CE2   . TYR B 1 138 ? 30.173  9.644   -23.278 1.00 20.32  ? 126 TYR B CE2   1 
ATOM   2724 C CZ    . TYR B 1 138 ? 29.590  8.511   -22.772 1.00 18.55  ? 126 TYR B CZ    1 
ATOM   2725 O OH    . TYR B 1 138 ? 30.240  7.282   -22.822 1.00 18.41  ? 126 TYR B OH    1 
ATOM   2726 N N     . PRO B 1 139 ? 29.297  12.655  -19.556 1.00 17.94  ? 127 PRO B N     1 
ATOM   2727 C CA    . PRO B 1 139 ? 30.506  13.147  -18.864 1.00 18.96  ? 127 PRO B CA    1 
ATOM   2728 C C     . PRO B 1 139 ? 31.816  12.491  -19.253 1.00 20.78  ? 127 PRO B C     1 
ATOM   2729 O O     . PRO B 1 139 ? 32.844  12.881  -18.707 1.00 20.65  ? 127 PRO B O     1 
ATOM   2730 C CB    . PRO B 1 139 ? 30.185  12.885  -17.386 1.00 20.05  ? 127 PRO B CB    1 
ATOM   2731 C CG    . PRO B 1 139 ? 29.256  11.645  -17.424 1.00 24.08  ? 127 PRO B CG    1 
ATOM   2732 C CD    . PRO B 1 139 ? 28.506  11.733  -18.716 1.00 18.38  ? 127 PRO B CD    1 
ATOM   2733 N N     . PHE B 1 140 ? 31.832  11.569  -20.236 1.00 19.78  ? 128 PHE B N     1 
ATOM   2734 C CA    . PHE B 1 140 ? 33.029  10.755  -20.441 1.00 19.14  ? 128 PHE B CA    1 
ATOM   2735 C C     . PHE B 1 140 ? 33.615  10.973  -21.832 1.00 19.16  ? 128 PHE B C     1 
ATOM   2736 O O     . PHE B 1 140 ? 32.889  11.164  -22.811 1.00 22.32  ? 128 PHE B O     1 
ATOM   2737 C CB    . PHE B 1 140 ? 32.690  9.255   -20.290 1.00 17.45  ? 128 PHE B CB    1 
ATOM   2738 C CG    . PHE B 1 140 ? 31.861  8.940   -19.078 1.00 17.80  ? 128 PHE B CG    1 
ATOM   2739 C CD1   . PHE B 1 140 ? 32.357  9.107   -17.789 1.00 18.23  ? 128 PHE B CD1   1 
ATOM   2740 C CD2   . PHE B 1 140 ? 30.544  8.484   -19.218 1.00 17.45  ? 128 PHE B CD2   1 
ATOM   2741 C CE1   . PHE B 1 140 ? 31.546  8.829   -16.661 1.00 21.31  ? 128 PHE B CE1   1 
ATOM   2742 C CE2   . PHE B 1 140 ? 29.753  8.198   -18.104 1.00 19.74  ? 128 PHE B CE2   1 
ATOM   2743 C CZ    . PHE B 1 140 ? 30.242  8.360   -16.832 1.00 20.40  ? 128 PHE B CZ    1 
ATOM   2744 N N     . PRO B 1 141 ? 34.930  10.903  -21.974 1.00 19.94  ? 129 PRO B N     1 
ATOM   2745 C CA    . PRO B 1 141 ? 35.510  11.056  -23.314 1.00 22.31  ? 129 PRO B CA    1 
ATOM   2746 C C     . PRO B 1 141 ? 35.244  9.859   -24.240 1.00 20.90  ? 129 PRO B C     1 
ATOM   2747 O O     . PRO B 1 141 ? 35.217  10.029  -25.457 1.00 23.08  ? 129 PRO B O     1 
ATOM   2748 C CB    . PRO B 1 141 ? 37.005  11.243  -23.027 1.00 22.84  ? 129 PRO B CB    1 
ATOM   2749 C CG    . PRO B 1 141 ? 37.207  10.593  -21.651 1.00 28.32  ? 129 PRO B CG    1 
ATOM   2750 C CD    . PRO B 1 141 ? 35.951  10.880  -20.909 1.00 22.54  ? 129 PRO B CD    1 
ATOM   2751 N N     . GLU B 1 142 ? 35.040  8.640   -23.705 1.00 19.91  ? 130 GLU B N     1 
ATOM   2752 C CA    . GLU B 1 142 ? 34.786  7.503   -24.615 1.00 18.40  ? 130 GLU B CA    1 
ATOM   2753 C C     . GLU B 1 142 ? 33.362  7.608   -25.137 1.00 17.61  ? 130 GLU B C     1 
ATOM   2754 O O     . GLU B 1 142 ? 32.445  7.657   -24.323 1.00 20.41  ? 130 GLU B O     1 
ATOM   2755 C CB    . GLU B 1 142 ? 34.982  6.169   -23.870 1.00 21.61  ? 130 GLU B CB    1 
ATOM   2756 C CG    . GLU B 1 142 ? 34.826  4.945   -24.782 1.00 21.05  ? 130 GLU B CG    1 
ATOM   2757 C CD    . GLU B 1 142 ? 35.039  3.621   -24.064 1.00 19.31  ? 130 GLU B CD    1 
ATOM   2758 O OE1   . GLU B 1 142 ? 35.291  3.596   -22.853 1.00 19.91  ? 130 GLU B OE1   1 
ATOM   2759 O OE2   . GLU B 1 142 ? 35.001  2.627   -24.810 1.00 21.66  ? 130 GLU B OE2   1 
ATOM   2760 N N     . PRO B 1 143 ? 33.152  7.580   -26.451 1.00 19.18  ? 131 PRO B N     1 
ATOM   2761 C CA    . PRO B 1 143 ? 31.796  7.776   -27.004 1.00 23.07  ? 131 PRO B CA    1 
ATOM   2762 C C     . PRO B 1 143 ? 30.801  6.736   -26.498 1.00 20.98  ? 131 PRO B C     1 
ATOM   2763 O O     . PRO B 1 143 ? 31.083  5.536   -26.389 1.00 20.17  ? 131 PRO B O     1 
ATOM   2764 C CB    . PRO B 1 143 ? 32.010  7.614   -28.512 1.00 27.30  ? 131 PRO B CB    1 
ATOM   2765 C CG    . PRO B 1 143 ? 33.467  8.037   -28.756 1.00 23.52  ? 131 PRO B CG    1 
ATOM   2766 C CD    . PRO B 1 143 ? 34.178  7.524   -27.521 1.00 22.89  ? 131 PRO B CD    1 
ATOM   2767 N N     . GLU B 1 144 ? 29.593  7.213   -26.228 1.00 21.47  ? 132 GLU B N     1 
ATOM   2768 C CA    . GLU B 1 144 ? 28.575  6.392   -25.587 1.00 20.98  ? 132 GLU B CA    1 
ATOM   2769 C C     . GLU B 1 144 ? 28.266  5.145   -26.395 1.00 22.35  ? 132 GLU B C     1 
ATOM   2770 O O     . GLU B 1 144 ? 28.220  4.054   -25.836 1.00 19.79  ? 132 GLU B O     1 
ATOM   2771 C CB    . GLU B 1 144 ? 27.319  7.242   -25.463 1.00 24.39  ? 132 GLU B CB    1 
ATOM   2772 C CG    . GLU B 1 144 ? 26.160  6.497   -24.775 1.00 26.43  ? 132 GLU B CG    1 
ATOM   2773 C CD    . GLU B 1 144 ? 24.898  7.381   -24.719 1.00 29.94  ? 132 GLU B CD    1 
ATOM   2774 O OE1   . GLU B 1 144 ? 24.964  8.552   -25.114 1.00 34.37  ? 132 GLU B OE1   1 
ATOM   2775 O OE2   . GLU B 1 144 ? 23.862  6.875   -24.266 1.00 48.12  ? 132 GLU B OE2   1 
ATOM   2776 N N     . LYS B 1 145 ? 27.998  5.272   -27.698 1.00 21.59  ? 133 LYS B N     1 
ATOM   2777 C CA    . LYS B 1 145 ? 27.620  4.053   -28.434 1.00 22.29  ? 133 LYS B CA    1 
ATOM   2778 C C     . LYS B 1 145 ? 28.801  3.112   -28.637 1.00 25.56  ? 133 LYS B C     1 
ATOM   2779 O O     . LYS B 1 145 ? 28.585  1.912   -28.887 1.00 23.00  ? 133 LYS B O     1 
ATOM   2780 C CB    . LYS B 1 145 ? 26.856  4.359   -29.714 1.00 23.79  ? 133 LYS B CB    1 
ATOM   2781 C CG    . LYS B 1 145 ? 25.464  5.035   -29.468 1.00 26.09  ? 133 LYS B CG    1 
ATOM   2782 C CD    . LYS B 1 145 ? 24.550  5.084   -30.689 1.00 30.16  ? 133 LYS B CD    1 
ATOM   2783 C CE    . LYS B 1 145 ? 23.171  5.698   -30.357 1.00 30.28  ? 133 LYS B CE    1 
ATOM   2784 N NZ    . LYS B 1 145 ? 22.258  5.731   -31.544 1.00 36.08  ? 133 LYS B NZ    1 
ATOM   2785 N N     . GLU B 1 146 ? 30.036  3.601   -28.522 1.00 19.65  ? 134 GLU B N     1 
ATOM   2786 C CA    . GLU B 1 146 ? 31.172  2.659   -28.497 1.00 20.69  ? 134 GLU B CA    1 
ATOM   2787 C C     . GLU B 1 146 ? 31.204  1.868   -27.206 1.00 19.03  ? 134 GLU B C     1 
ATOM   2788 O O     . GLU B 1 146 ? 31.512  0.665   -27.227 1.00 19.80  ? 134 GLU B O     1 
ATOM   2789 C CB    . GLU B 1 146 ? 32.502  3.391   -28.641 1.00 22.88  ? 134 GLU B CB    1 
ATOM   2790 C CG    . GLU B 1 146 ? 32.689  3.978   -30.028 1.00 25.20  ? 134 GLU B CG    1 
ATOM   2791 C CD    . GLU B 1 146 ? 34.032  4.682   -30.200 1.00 29.44  ? 134 GLU B CD    1 
ATOM   2792 O OE1   . GLU B 1 146 ? 34.925  4.490   -29.323 1.00 28.42  ? 134 GLU B OE1   1 
ATOM   2793 O OE2   . GLU B 1 146 ? 34.171  5.432   -31.206 1.00 30.81  ? 134 GLU B OE2   1 
ATOM   2794 N N     . VAL B 1 147 ? 30.926  2.504   -26.064 1.00 19.59  ? 135 VAL B N     1 
ATOM   2795 C CA    . VAL B 1 147 ? 30.763  1.746   -24.832 1.00 18.63  ? 135 VAL B CA    1 
ATOM   2796 C C     . VAL B 1 147 ? 29.661  0.719   -25.008 1.00 16.68  ? 135 VAL B C     1 
ATOM   2797 O O     . VAL B 1 147 ? 29.820  -0.463  -24.635 1.00 17.67  ? 135 VAL B O     1 
ATOM   2798 C CB    . VAL B 1 147 ? 30.468  2.672   -23.635 1.00 16.81  ? 135 VAL B CB    1 
ATOM   2799 C CG1   . VAL B 1 147 ? 30.264  1.832   -22.348 1.00 18.85  ? 135 VAL B CG1   1 
ATOM   2800 C CG2   . VAL B 1 147 ? 31.609  3.669   -23.448 1.00 19.87  ? 135 VAL B CG2   1 
ATOM   2801 N N     . ALA B 1 148 ? 28.516  1.137   -25.552 1.00 18.64  ? 136 ALA B N     1 
ATOM   2802 C CA    . ALA B 1 148 ? 27.388  0.226   -25.700 1.00 19.12  ? 136 ALA B CA    1 
ATOM   2803 C C     . ALA B 1 148 ? 27.765  -0.955  -26.577 1.00 19.30  ? 136 ALA B C     1 
ATOM   2804 O O     . ALA B 1 148 ? 27.440  -2.104  -26.245 1.00 20.26  ? 136 ALA B O     1 
ATOM   2805 C CB    . ALA B 1 148 ? 26.184  0.983   -26.264 1.00 21.19  ? 136 ALA B CB    1 
ATOM   2806 N N     . GLU B 1 149 ? 28.482  -0.709  -27.670 1.00 18.71  ? 137 GLU B N     1 
ATOM   2807 C CA    . GLU B 1 149 ? 28.856  -1.795  -28.587 1.00 19.99  ? 137 GLU B CA    1 
ATOM   2808 C C     . GLU B 1 149 ? 29.802  -2.780  -27.911 1.00 21.23  ? 137 GLU B C     1 
ATOM   2809 O O     . GLU B 1 149 ? 29.606  -4.004  -28.022 1.00 20.91  ? 137 GLU B O     1 
ATOM   2810 C CB    . GLU B 1 149 ? 29.517  -1.207  -29.819 1.00 23.45  ? 137 GLU B CB    1 
ATOM   2811 C CG    . GLU B 1 149 ? 30.116  -2.262  -30.749 1.00 31.01  ? 137 GLU B CG    1 
ATOM   2812 C CD    . GLU B 1 149 ? 30.502  -1.690  -32.097 1.00 60.61  ? 137 GLU B CD    1 
ATOM   2813 O OE1   . GLU B 1 149 ? 29.901  -0.665  -32.503 1.00 55.59  ? 137 GLU B OE1   1 
ATOM   2814 O OE2   . GLU B 1 149 ? 31.411  -2.260  -32.739 1.00 63.89  ? 137 GLU B OE2   1 
ATOM   2815 N N     . ARG B 1 150 ? 30.874  -2.293  -27.276 1.00 18.19  ? 138 ARG B N     1 
ATOM   2816 C CA    . ARG B 1 150 ? 31.829  -3.235  -26.674 1.00 19.05  ? 138 ARG B CA    1 
ATOM   2817 C C     . ARG B 1 150 ? 31.171  -3.995  -25.529 1.00 17.67  ? 138 ARG B C     1 
ATOM   2818 O O     . ARG B 1 150 ? 31.425  -5.204  -25.368 1.00 17.78  ? 138 ARG B O     1 
ATOM   2819 C CB    . ARG B 1 150 ? 33.132  -2.532  -26.267 1.00 19.54  ? 138 ARG B CB    1 
ATOM   2820 C CG    . ARG B 1 150 ? 33.031  -1.550  -25.095 1.00 18.51  ? 138 ARG B CG    1 
ATOM   2821 C CD    . ARG B 1 150 ? 34.447  -1.084  -24.726 1.00 19.52  ? 138 ARG B CD    1 
ATOM   2822 N NE    . ARG B 1 150 ? 34.398  0.051   -23.788 1.00 18.03  ? 138 ARG B NE    1 
ATOM   2823 C CZ    . ARG B 1 150 ? 34.173  -0.053  -22.490 1.00 17.05  ? 138 ARG B CZ    1 
ATOM   2824 N NH1   . ARG B 1 150 ? 33.824  -1.213  -21.933 1.00 18.22  ? 138 ARG B NH1   1 
ATOM   2825 N NH2   . ARG B 1 150 ? 34.251  1.043   -21.716 1.00 18.55  ? 138 ARG B NH2   1 
ATOM   2826 N N     . MET B 1 151 ? 30.282  -3.369  -24.780 1.00 17.42  ? 139 MET B N     1 
ATOM   2827 C CA    . MET B 1 151 ? 29.598  -4.046  -23.692 1.00 17.13  ? 139 MET B CA    1 
ATOM   2828 C C     . MET B 1 151 ? 28.642  -5.109  -24.239 1.00 20.58  ? 139 MET B C     1 
ATOM   2829 O O     . MET B 1 151 ? 28.577  -6.241  -23.701 1.00 18.10  ? 139 MET B O     1 
ATOM   2830 C CB    . MET B 1 151 ? 28.782  -3.071  -22.823 1.00 16.38  ? 139 MET B CB    1 
ATOM   2831 C CG    . MET B 1 151 ? 29.642  -2.200  -21.907 1.00 17.68  ? 139 MET B CG    1 
ATOM   2832 S SD    . MET B 1 151 ? 30.410  -3.208  -20.613 1.00 17.63  ? 139 MET B SD    1 
ATOM   2833 C CE    . MET B 1 151 ? 28.974  -3.817  -19.780 1.00 21.38  ? 139 MET B CE    1 
ATOM   2834 N N     A ARG B 1 152 ? 27.925  -4.819  -25.330 0.50 17.62  ? 140 ARG B N     1 
ATOM   2835 N N     B ARG B 1 152 ? 27.861  -4.768  -25.263 0.50 17.82  ? 140 ARG B N     1 
ATOM   2836 C CA    A ARG B 1 152 ? 26.991  -5.823  -25.854 0.50 19.20  ? 140 ARG B CA    1 
ATOM   2837 C CA    B ARG B 1 152 ? 26.993  -5.774  -25.863 0.50 19.19  ? 140 ARG B CA    1 
ATOM   2838 C C     A ARG B 1 152 ? 27.743  -6.961  -26.530 0.50 21.28  ? 140 ARG B C     1 
ATOM   2839 C C     B ARG B 1 152 ? 27.829  -6.943  -26.352 0.50 18.79  ? 140 ARG B C     1 
ATOM   2840 O O     A ARG B 1 152 ? 27.300  -8.126  -26.508 0.50 17.82  ? 140 ARG B O     1 
ATOM   2841 O O     B ARG B 1 152 ? 27.533  -8.110  -26.023 0.50 18.60  ? 140 ARG B O     1 
ATOM   2842 C CB    A ARG B 1 152 ? 25.971  -5.183  -26.791 0.50 20.90  ? 140 ARG B CB    1 
ATOM   2843 C CB    B ARG B 1 152 ? 26.138  -5.170  -26.977 0.50 21.07  ? 140 ARG B CB    1 
ATOM   2844 C CG    A ARG B 1 152 ? 24.764  -6.103  -27.071 0.50 25.18  ? 140 ARG B CG    1 
ATOM   2845 C CG    B ARG B 1 152 ? 24.806  -5.951  -27.218 0.50 26.23  ? 140 ARG B CG    1 
ATOM   2846 C CD    A ARG B 1 152 ? 23.994  -5.615  -28.286 0.50 31.18  ? 140 ARG B CD    1 
ATOM   2847 C CD    B ARG B 1 152 ? 24.207  -5.551  -28.557 0.50 31.79  ? 140 ARG B CD    1 
ATOM   2848 N NE    A ARG B 1 152 ? 22.622  -6.113  -28.345 0.50 31.32  ? 140 ARG B NE    1 
ATOM   2849 N NE    B ARG B 1 152 ? 22.751  -5.647  -28.663 0.50 38.83  ? 140 ARG B NE    1 
ATOM   2850 C CZ    A ARG B 1 152 ? 22.270  -7.332  -28.716 0.50 30.35  ? 140 ARG B CZ    1 
ATOM   2851 C CZ    B ARG B 1 152 ? 21.945  -4.593  -28.736 0.50 29.53  ? 140 ARG B CZ    1 
ATOM   2852 N NH1   A ARG B 1 152 ? 23.171  -8.254  -29.011 0.50 29.10  ? 140 ARG B NH1   1 
ATOM   2853 N NH1   B ARG B 1 152 ? 22.406  -3.360  -28.588 0.50 39.51  ? 140 ARG B NH1   1 
ATOM   2854 N NH2   A ARG B 1 152 ? 20.978  -7.629  -28.816 0.50 25.28  ? 140 ARG B NH2   1 
ATOM   2855 N NH2   B ARG B 1 152 ? 20.644  -4.777  -28.972 0.50 38.17  ? 140 ARG B NH2   1 
ATOM   2856 N N     . THR B 1 153 ? 28.874  -6.657  -27.151 1.00 19.23  ? 141 THR B N     1 
ATOM   2857 C CA    . THR B 1 153 ? 29.731  -7.721  -27.699 1.00 20.55  ? 141 THR B CA    1 
ATOM   2858 C C     . THR B 1 153 ? 30.277  -8.605  -26.586 1.00 21.62  ? 141 THR B C     1 
ATOM   2859 O O     . THR B 1 153 ? 30.314  -9.845  -26.724 1.00 20.09  ? 141 THR B O     1 
ATOM   2860 C CB    . THR B 1 153 ? 30.872  -7.070  -28.472 1.00 20.82  ? 141 THR B CB    1 
ATOM   2861 O OG1   . THR B 1 153 ? 30.326  -6.435  -29.626 1.00 25.91  ? 141 THR B OG1   1 
ATOM   2862 C CG2   . THR B 1 153 ? 31.895  -8.111  -28.917 1.00 27.74  ? 141 THR B CG2   1 
ATOM   2863 N N     . ALA B 1 154 ? 30.719  -8.005  -25.492 1.00 19.73  ? 142 ALA B N     1 
ATOM   2864 C CA    . ALA B 1 154 ? 31.249  -8.774  -24.374 1.00 19.52  ? 142 ALA B CA    1 
ATOM   2865 C C     . ALA B 1 154 ? 30.186  -9.660  -23.774 1.00 18.09  ? 142 ALA B C     1 
ATOM   2866 O O     . ALA B 1 154 ? 30.451  -10.851 -23.500 1.00 19.33  ? 142 ALA B O     1 
ATOM   2867 C CB    . ALA B 1 154 ? 31.811  -7.848  -23.295 1.00 20.84  ? 142 ALA B CB    1 
ATOM   2868 N N     . VAL B 1 155 ? 28.978  -9.154  -23.577 1.00 17.81  ? 143 VAL B N     1 
ATOM   2869 C CA    . VAL B 1 155 ? 27.903  -9.976  -23.035 1.00 19.26  ? 143 VAL B CA    1 
ATOM   2870 C C     . VAL B 1 155 ? 27.569  -11.118 -23.989 1.00 18.39  ? 143 VAL B C     1 
ATOM   2871 O O     . VAL B 1 155 ? 27.403  -12.268 -23.549 1.00 18.70  ? 143 VAL B O     1 
ATOM   2872 C CB    . VAL B 1 155 ? 26.672  -9.110  -22.690 1.00 19.36  ? 143 VAL B CB    1 
ATOM   2873 C CG1   . VAL B 1 155 ? 25.469  -9.971  -22.326 1.00 22.86  ? 143 VAL B CG1   1 
ATOM   2874 C CG2   . VAL B 1 155 ? 27.052  -8.178  -21.551 1.00 21.67  ? 143 VAL B CG2   1 
ATOM   2875 N N     . THR B 1 156 ? 27.484  -10.854 -25.288 1.00 18.75  ? 144 THR B N     1 
ATOM   2876 C CA    . THR B 1 156 ? 27.241  -11.894 -26.266 1.00 20.57  ? 144 THR B CA    1 
ATOM   2877 C C     . THR B 1 156 ? 28.321  -12.960 -26.179 1.00 20.27  ? 144 THR B C     1 
ATOM   2878 O O     . THR B 1 156 ? 28.010  -14.154 -26.201 1.00 21.42  ? 144 THR B O     1 
ATOM   2879 C CB    . THR B 1 156 ? 27.164  -11.286 -27.675 1.00 24.45  ? 144 THR B CB    1 
ATOM   2880 O OG1   . THR B 1 156 ? 26.056  -10.346 -27.728 1.00 24.53  ? 144 THR B OG1   1 
ATOM   2881 C CG2   . THR B 1 156 ? 26.994  -12.386 -28.748 1.00 25.81  ? 144 THR B CG2   1 
ATOM   2882 N N     . ALA B 1 157 ? 29.574  -12.559 -26.011 1.00 19.92  ? 145 ALA B N     1 
ATOM   2883 C CA    . ALA B 1 157 ? 30.671  -13.511 -25.946 1.00 21.89  ? 145 ALA B CA    1 
ATOM   2884 C C     . ALA B 1 157 ? 30.590  -14.330 -24.671 1.00 20.23  ? 145 ALA B C     1 
ATOM   2885 O O     . ALA B 1 157 ? 30.884  -15.536 -24.685 1.00 20.60  ? 145 ALA B O     1 
ATOM   2886 C CB    . ALA B 1 157 ? 32.007  -12.760 -26.005 1.00 21.86  ? 145 ALA B CB    1 
ATOM   2887 N N     . ALA B 1 158 ? 30.192  -13.735 -23.577 1.00 19.49  ? 146 ALA B N     1 
ATOM   2888 C CA    . ALA B 1 158 ? 30.090  -14.445 -22.311 1.00 18.35  ? 146 ALA B CA    1 
ATOM   2889 C C     . ALA B 1 158 ? 28.977  -15.471 -22.366 1.00 19.90  ? 146 ALA B C     1 
ATOM   2890 O O     . ALA B 1 158 ? 29.147  -16.617 -21.900 1.00 21.46  ? 146 ALA B O     1 
ATOM   2891 C CB    . ALA B 1 158 ? 29.807  -13.486 -21.165 1.00 19.02  ? 146 ALA B CB    1 
ATOM   2892 N N     . VAL B 1 159 ? 27.843  -15.141 -22.985 1.00 19.45  ? 147 VAL B N     1 
ATOM   2893 C CA    . VAL B 1 159 ? 26.788  -16.127 -23.165 1.00 20.26  ? 147 VAL B CA    1 
ATOM   2894 C C     . VAL B 1 159 ? 27.300  -17.263 -24.039 1.00 21.65  ? 147 VAL B C     1 
ATOM   2895 O O     . VAL B 1 159 ? 27.053  -18.445 -23.767 1.00 21.90  ? 147 VAL B O     1 
ATOM   2896 C CB    . VAL B 1 159 ? 25.558  -15.428 -23.787 1.00 21.11  ? 147 VAL B CB    1 
ATOM   2897 C CG1   . VAL B 1 159 ? 24.502  -16.445 -24.208 1.00 24.12  ? 147 VAL B CG1   1 
ATOM   2898 C CG2   . VAL B 1 159 ? 24.919  -14.428 -22.787 1.00 22.56  ? 147 VAL B CG2   1 
ATOM   2899 N N     . ALA B 1 160 ? 28.022  -16.933 -25.113 1.00 20.84  ? 148 ALA B N     1 
ATOM   2900 C CA    . ALA B 1 160 ? 28.518  -17.969 -26.010 1.00 24.45  ? 148 ALA B CA    1 
ATOM   2901 C C     . ALA B 1 160 ? 29.536  -18.878 -25.342 1.00 23.54  ? 148 ALA B C     1 
ATOM   2902 O O     . ALA B 1 160 ? 29.633  -20.072 -25.677 1.00 25.47  ? 148 ALA B O     1 
ATOM   2903 C CB    . ALA B 1 160 ? 29.109  -17.340 -27.282 1.00 24.94  ? 148 ALA B CB    1 
ATOM   2904 N N     . ALA B 1 161 ? 30.272  -18.359 -24.363 1.00 21.23  ? 149 ALA B N     1 
ATOM   2905 C CA    . ALA B 1 161 ? 31.286  -19.165 -23.696 1.00 22.77  ? 149 ALA B CA    1 
ATOM   2906 C C     . ALA B 1 161 ? 30.734  -19.948 -22.518 1.00 20.39  ? 149 ALA B C     1 
ATOM   2907 O O     . ALA B 1 161 ? 31.521  -20.636 -21.848 1.00 23.21  ? 149 ALA B O     1 
ATOM   2908 C CB    . ALA B 1 161 ? 32.431  -18.249 -23.226 1.00 29.45  ? 149 ALA B CB    1 
ATOM   2909 N N     . THR B 1 162 ? 29.439  -19.933 -22.293 1.00 20.26  ? 150 THR B N     1 
ATOM   2910 C CA    . THR B 1 162 ? 28.835  -20.607 -21.126 1.00 21.91  ? 150 THR B CA    1 
ATOM   2911 C C     . THR B 1 162 ? 28.222  -21.926 -21.564 1.00 21.05  ? 150 THR B C     1 
ATOM   2912 O O     . THR B 1 162 ? 27.358  -21.921 -22.441 1.00 19.82  ? 150 THR B O     1 
ATOM   2913 C CB    . THR B 1 162 ? 27.737  -19.733 -20.533 1.00 21.43  ? 150 THR B CB    1 
ATOM   2914 O OG1   . THR B 1 162 ? 28.299  -18.458 -20.129 1.00 24.19  ? 150 THR B OG1   1 
ATOM   2915 C CG2   . THR B 1 162 ? 27.083  -20.358 -19.276 1.00 23.09  ? 150 THR B CG2   1 
ATOM   2916 N N     . PRO B 1 163 ? 28.649  -23.062 -21.015 1.00 20.11  ? 151 PRO B N     1 
ATOM   2917 C CA    . PRO B 1 163 ? 27.999  -24.342 -21.329 1.00 18.81  ? 151 PRO B CA    1 
ATOM   2918 C C     . PRO B 1 163 ? 26.546  -24.282 -20.907 1.00 20.81  ? 151 PRO B C     1 
ATOM   2919 O O     . PRO B 1 163 ? 26.212  -23.660 -19.878 1.00 21.82  ? 151 PRO B O     1 
ATOM   2920 C CB    . PRO B 1 163 ? 28.774  -25.322 -20.437 1.00 23.92  ? 151 PRO B CB    1 
ATOM   2921 C CG    . PRO B 1 163 ? 30.126  -24.696 -20.278 1.00 24.85  ? 151 PRO B CG    1 
ATOM   2922 C CD    . PRO B 1 163 ? 29.802  -23.228 -20.120 1.00 24.58  ? 151 PRO B CD    1 
ATOM   2923 N N     . PRO B 1 164 ? 25.637  -24.891 -21.670 1.00 21.09  ? 152 PRO B N     1 
ATOM   2924 C CA    . PRO B 1 164 ? 24.222  -24.840 -21.296 1.00 20.96  ? 152 PRO B CA    1 
ATOM   2925 C C     . PRO B 1 164 ? 23.943  -25.477 -19.939 1.00 22.52  ? 152 PRO B C     1 
ATOM   2926 O O     . PRO B 1 164 ? 24.555  -26.464 -19.556 1.00 22.98  ? 152 PRO B O     1 
ATOM   2927 C CB    . PRO B 1 164 ? 23.522  -25.586 -22.440 1.00 27.38  ? 152 PRO B CB    1 
ATOM   2928 C CG    . PRO B 1 164 ? 24.574  -26.368 -23.092 1.00 25.76  ? 152 PRO B CG    1 
ATOM   2929 C CD    . PRO B 1 164 ? 25.848  -25.589 -22.952 1.00 20.48  ? 152 PRO B CD    1 
ATOM   2930 N N     . ALA B 1 165 ? 22.931  -24.968 -19.240 1.00 20.77  ? 153 ALA B N     1 
ATOM   2931 C CA    . ALA B 1 165 ? 22.545  -25.516 -17.958 1.00 21.53  ? 153 ALA B CA    1 
ATOM   2932 C C     . ALA B 1 165 ? 21.999  -26.925 -18.163 1.00 26.05  ? 153 ALA B C     1 
ATOM   2933 O O     . ALA B 1 165 ? 21.312  -27.195 -19.155 1.00 25.64  ? 153 ALA B O     1 
ATOM   2934 C CB    . ALA B 1 165 ? 21.422  -24.651 -17.358 1.00 22.59  ? 153 ALA B CB    1 
ATOM   2935 N N     . PRO B 1 166 ? 22.182  -27.816 -17.168 1.00 25.47  ? 154 PRO B N     1 
ATOM   2936 C CA    . PRO B 1 166 ? 21.614  -29.167 -17.262 1.00 28.07  ? 154 PRO B CA    1 
ATOM   2937 C C     . PRO B 1 166 ? 20.107  -29.182 -17.129 1.00 27.61  ? 154 PRO B C     1 
ATOM   2938 O O     . PRO B 1 166 ? 19.456  -30.104 -17.610 1.00 33.22  ? 154 PRO B O     1 
ATOM   2939 C CB    . PRO B 1 166 ? 22.281  -29.920 -16.098 1.00 31.13  ? 154 PRO B CB    1 
ATOM   2940 C CG    . PRO B 1 166 ? 22.788  -28.824 -15.153 1.00 32.31  ? 154 PRO B CG    1 
ATOM   2941 C CD    . PRO B 1 166 ? 23.091  -27.644 -16.021 1.00 29.46  ? 154 PRO B CD    1 
ATOM   2942 N N     . ASP B 1 167 ? 19.520  -28.166 -16.497 1.00 33.58  ? 155 ASP B N     1 
ATOM   2943 C CA    . ASP B 1 167 ? 18.067  -28.087 -16.438 1.00 32.83  ? 155 ASP B CA    1 
ATOM   2944 C C     . ASP B 1 167 ? 17.730  -26.636 -16.136 1.00 32.81  ? 155 ASP B C     1 
ATOM   2945 O O     . ASP B 1 167 ? 18.510  -25.937 -15.495 1.00 35.47  ? 155 ASP B O     1 
ATOM   2946 C CB    . ASP B 1 167 ? 17.468  -29.023 -15.377 1.00 44.00  ? 155 ASP B CB    1 
ATOM   2947 C CG    . ASP B 1 167 ? 17.853  -28.626 -13.970 1.00 66.34  ? 155 ASP B CG    1 
ATOM   2948 O OD1   . ASP B 1 167 ? 19.067  -28.493 -13.702 1.00 70.98  ? 155 ASP B OD1   1 
ATOM   2949 O OD2   . ASP B 1 167 ? 16.941  -28.433 -13.136 1.00 80.31  ? 155 ASP B OD2   1 
ATOM   2950 N N     . GLY B 1 168 ? 16.571  -26.200 -16.610 1.00 36.14  ? 156 GLY B N     1 
ATOM   2951 C CA    . GLY B 1 168 ? 16.210  -24.824 -16.359 1.00 30.40  ? 156 GLY B CA    1 
ATOM   2952 C C     . GLY B 1 168 ? 17.030  -23.838 -17.177 1.00 30.26  ? 156 GLY B C     1 
ATOM   2953 O O     . GLY B 1 168 ? 17.663  -24.151 -18.193 1.00 34.27  ? 156 GLY B O     1 
ATOM   2954 N N     . THR B 1 169 ? 17.098  -22.624 -16.646 1.00 27.21  ? 157 THR B N     1 
ATOM   2955 C CA    . THR B 1 169 ? 17.645  -21.489 -17.365 1.00 24.27  ? 157 THR B CA    1 
ATOM   2956 C C     . THR B 1 169 ? 19.164  -21.444 -17.215 1.00 21.33  ? 157 THR B C     1 
ATOM   2957 O O     . THR B 1 169 ? 19.692  -21.557 -16.105 1.00 23.64  ? 157 THR B O     1 
ATOM   2958 C CB    . THR B 1 169 ? 17.014  -20.245 -16.749 1.00 26.24  ? 157 THR B CB    1 
ATOM   2959 O OG1   . THR B 1 169 ? 15.585  -20.341 -16.863 1.00 32.49  ? 157 THR B OG1   1 
ATOM   2960 C CG2   . THR B 1 169 ? 17.510  -18.991 -17.432 1.00 26.28  ? 157 THR B CG2   1 
ATOM   2961 N N     . THR B 1 170 ? 19.853  -21.256 -18.324 1.00 19.61  ? 158 THR B N     1 
ATOM   2962 C CA    . THR B 1 170 ? 21.283  -20.983 -18.290 1.00 18.78  ? 158 THR B CA    1 
ATOM   2963 C C     . THR B 1 170 ? 21.507  -19.537 -17.870 1.00 19.09  ? 158 THR B C     1 
ATOM   2964 O O     . THR B 1 170 ? 20.865  -18.613 -18.402 1.00 19.85  ? 158 THR B O     1 
ATOM   2965 C CB    . THR B 1 170 ? 21.859  -21.185 -19.686 1.00 18.72  ? 158 THR B CB    1 
ATOM   2966 O OG1   . THR B 1 170 ? 21.587  -22.527 -20.098 1.00 20.67  ? 158 THR B OG1   1 
ATOM   2967 C CG2   . THR B 1 170 ? 23.346  -20.976 -19.671 1.00 23.01  ? 158 THR B CG2   1 
ATOM   2968 N N     . ARG B 1 171 ? 22.420  -19.317 -16.921 1.00 16.48  ? 159 ARG B N     1 
ATOM   2969 C CA    A ARG B 1 171 ? 22.637  -17.986 -16.372 0.40 17.90  ? 159 ARG B CA    1 
ATOM   2970 C CA    B ARG B 1 171 ? 22.615  -17.997 -16.330 0.60 17.85  ? 159 ARG B CA    1 
ATOM   2971 C C     . ARG B 1 171 ? 24.116  -17.721 -16.280 1.00 18.89  ? 159 ARG B C     1 
ATOM   2972 O O     . ARG B 1 171 ? 24.896  -18.557 -15.803 1.00 19.47  ? 159 ARG B O     1 
ATOM   2973 C CB    A ARG B 1 171 ? 22.097  -17.866 -14.973 0.40 20.02  ? 159 ARG B CB    1 
ATOM   2974 C CB    B ARG B 1 171 ? 21.948  -18.020 -14.940 0.60 20.05  ? 159 ARG B CB    1 
ATOM   2975 C CG    A ARG B 1 171 ? 20.647  -17.985 -14.903 0.40 15.98  ? 159 ARG B CG    1 
ATOM   2976 C CG    B ARG B 1 171 ? 21.911  -16.725 -14.147 0.60 19.97  ? 159 ARG B CG    1 
ATOM   2977 C CD    A ARG B 1 171 ? 20.202  -17.711 -13.480 0.40 20.21  ? 159 ARG B CD    1 
ATOM   2978 C CD    B ARG B 1 171 ? 21.059  -16.888 -12.892 0.60 21.38  ? 159 ARG B CD    1 
ATOM   2979 N NE    A ARG B 1 171 ? 18.773  -17.857 -13.308 0.40 21.14  ? 159 ARG B NE    1 
ATOM   2980 N NE    B ARG B 1 171 ? 19.642  -17.061 -13.181 0.60 23.58  ? 159 ARG B NE    1 
ATOM   2981 C CZ    A ARG B 1 171 ? 18.205  -19.000 -12.978 0.40 30.17  ? 159 ARG B CZ    1 
ATOM   2982 C CZ    B ARG B 1 171 ? 18.927  -18.167 -12.999 0.60 22.99  ? 159 ARG B CZ    1 
ATOM   2983 N NH1   A ARG B 1 171 ? 18.932  -20.055 -12.639 0.40 23.84  ? 159 ARG B NH1   1 
ATOM   2984 N NH1   B ARG B 1 171 ? 19.465  -19.297 -12.536 0.60 24.96  ? 159 ARG B NH1   1 
ATOM   2985 N NH2   A ARG B 1 171 ? 16.884  -19.088 -13.007 0.40 23.98  ? 159 ARG B NH2   1 
ATOM   2986 N NH2   B ARG B 1 171 ? 17.642  -18.160 -13.325 0.60 24.09  ? 159 ARG B NH2   1 
ATOM   2987 N N     . VAL B 1 172 ? 24.528  -16.558 -16.756 1.00 17.85  ? 160 VAL B N     1 
ATOM   2988 C CA    . VAL B 1 172 ? 25.925  -16.138 -16.676 1.00 19.12  ? 160 VAL B CA    1 
ATOM   2989 C C     . VAL B 1 172 ? 25.966  -14.850 -15.867 1.00 17.28  ? 160 VAL B C     1 
ATOM   2990 O O     . VAL B 1 172 ? 25.195  -13.912 -16.134 1.00 17.97  ? 160 VAL B O     1 
ATOM   2991 C CB    . VAL B 1 172 ? 26.548  -16.011 -18.074 1.00 20.72  ? 160 VAL B CB    1 
ATOM   2992 C CG1   . VAL B 1 172 ? 25.869  -15.013 -18.978 1.00 23.30  ? 160 VAL B CG1   1 
ATOM   2993 C CG2   . VAL B 1 172 ? 28.093  -15.726 -18.028 1.00 21.67  ? 160 VAL B CG2   1 
ATOM   2994 N N     . ALA B 1 173 ? 26.827  -14.806 -14.855 1.00 17.40  ? 161 ALA B N     1 
ATOM   2995 C CA    . ALA B 1 173 ? 27.092  -13.572 -14.094 1.00 18.19  ? 161 ALA B CA    1 
ATOM   2996 C C     . ALA B 1 173 ? 28.204  -12.780 -14.778 1.00 17.84  ? 161 ALA B C     1 
ATOM   2997 O O     . ALA B 1 173 ? 29.219  -13.349 -15.208 1.00 17.58  ? 161 ALA B O     1 
ATOM   2998 C CB    . ALA B 1 173 ? 27.483  -13.907 -12.663 1.00 19.54  ? 161 ALA B CB    1 
ATOM   2999 N N     . VAL B 1 174 ? 27.993  -11.476 -14.894 1.00 16.98  ? 162 VAL B N     1 
ATOM   3000 C CA    . VAL B 1 174 ? 28.928  -10.568 -15.546 1.00 16.66  ? 162 VAL B CA    1 
ATOM   3001 C C     . VAL B 1 174 ? 29.196  -9.388  -14.614 1.00 16.67  ? 162 VAL B C     1 
ATOM   3002 O O     . VAL B 1 174 ? 28.289  -8.587  -14.358 1.00 17.28  ? 162 VAL B O     1 
ATOM   3003 C CB    . VAL B 1 174 ? 28.393  -10.124 -16.891 1.00 16.96  ? 162 VAL B CB    1 
ATOM   3004 C CG1   . VAL B 1 174 ? 29.294  -9.081  -17.487 1.00 19.82  ? 162 VAL B CG1   1 
ATOM   3005 C CG2   . VAL B 1 174 ? 28.229  -11.347 -17.848 1.00 19.58  ? 162 VAL B CG2   1 
ATOM   3006 N N     . VAL B 1 175 ? 30.413  -9.296  -14.084 1.00 16.64  ? 163 VAL B N     1 
ATOM   3007 C CA    . VAL B 1 175 ? 30.766  -8.268  -13.095 1.00 18.00  ? 163 VAL B CA    1 
ATOM   3008 C C     . VAL B 1 175 ? 31.467  -7.120  -13.812 1.00 15.84  ? 163 VAL B C     1 
ATOM   3009 O O     . VAL B 1 175 ? 32.549  -7.275  -14.403 1.00 17.39  ? 163 VAL B O     1 
ATOM   3010 C CB    . VAL B 1 175 ? 31.639  -8.808  -11.957 1.00 18.72  ? 163 VAL B CB    1 
ATOM   3011 C CG1   . VAL B 1 175 ? 31.890  -7.685  -10.922 1.00 21.60  ? 163 VAL B CG1   1 
ATOM   3012 C CG2   . VAL B 1 175 ? 31.022  -10.042 -11.298 1.00 20.46  ? 163 VAL B CG2   1 
ATOM   3013 N N     . GLY B 1 176 ? 30.798  -5.972  -13.772 1.00 16.18  ? 164 GLY B N     1 
ATOM   3014 C CA    . GLY B 1 176 ? 31.306  -4.757  -14.401 1.00 16.43  ? 164 GLY B CA    1 
ATOM   3015 C C     . GLY B 1 176 ? 31.118  -3.524  -13.554 1.00 16.15  ? 164 GLY B C     1 
ATOM   3016 O O     . GLY B 1 176 ? 31.170  -3.536  -12.325 1.00 17.51  ? 164 GLY B O     1 
ATOM   3017 N N     . HIS B 1 177 ? 30.963  -2.398  -14.263 1.00 17.24  ? 165 HIS B N     1 
ATOM   3018 C CA    . HIS B 1 177 ? 31.075  -1.029  -13.733 1.00 15.29  ? 165 HIS B CA    1 
ATOM   3019 C C     . HIS B 1 177 ? 29.806  -0.231  -14.027 1.00 17.27  ? 165 HIS B C     1 
ATOM   3020 O O     . HIS B 1 177 ? 29.211  -0.377  -15.078 1.00 18.51  ? 165 HIS B O     1 
ATOM   3021 C CB    . HIS B 1 177 ? 32.315  -0.380  -14.389 1.00 17.34  ? 165 HIS B CB    1 
ATOM   3022 C CG    . HIS B 1 177 ? 33.596  -1.115  -14.083 1.00 19.43  ? 165 HIS B CG    1 
ATOM   3023 N ND1   . HIS B 1 177 ? 34.352  -0.833  -12.969 1.00 19.19  ? 165 HIS B ND1   1 
ATOM   3024 C CD2   . HIS B 1 177 ? 34.167  -2.195  -14.674 1.00 20.56  ? 165 HIS B CD2   1 
ATOM   3025 C CE1   . HIS B 1 177 ? 35.409  -1.654  -12.945 1.00 21.95  ? 165 HIS B CE1   1 
ATOM   3026 N NE2   . HIS B 1 177 ? 35.325  -2.482  -13.973 1.00 21.55  ? 165 HIS B NE2   1 
ATOM   3027 N N     . ASP B 1 178 ? 29.447  0.619   -13.059 1.00 17.21  ? 166 ASP B N     1 
ATOM   3028 C CA    . ASP B 1 178 ? 28.224  1.413   -13.121 1.00 16.72  ? 166 ASP B CA    1 
ATOM   3029 C C     . ASP B 1 178 ? 27.960  2.014   -14.503 1.00 16.49  ? 166 ASP B C     1 
ATOM   3030 O O     . ASP B 1 178 ? 26.941  1.734   -15.128 1.00 16.75  ? 166 ASP B O     1 
ATOM   3031 C CB    . ASP B 1 178 ? 28.343  2.545   -12.096 1.00 18.71  ? 166 ASP B CB    1 
ATOM   3032 C CG    . ASP B 1 178 ? 27.207  3.559   -12.240 1.00 18.59  ? 166 ASP B CG    1 
ATOM   3033 O OD1   . ASP B 1 178 ? 26.035  3.153   -12.263 1.00 20.73  ? 166 ASP B OD1   1 
ATOM   3034 O OD2   . ASP B 1 178 ? 27.519  4.759   -12.358 1.00 20.29  ? 166 ASP B OD2   1 
ATOM   3035 N N     . SER B 1 179 ? 28.823  2.898   -14.967 1.00 16.20  ? 167 SER B N     1 
ATOM   3036 C CA    . SER B 1 179 ? 28.435  3.697   -16.120 1.00 16.27  ? 167 SER B CA    1 
ATOM   3037 C C     . SER B 1 179 ? 28.349  2.860   -17.387 1.00 16.49  ? 167 SER B C     1 
ATOM   3038 O O     . SER B 1 179 ? 27.410  3.008   -18.179 1.00 16.11  ? 167 SER B O     1 
ATOM   3039 C CB    . SER B 1 179 ? 29.375  4.868   -16.329 1.00 17.09  ? 167 SER B CB    1 
ATOM   3040 O OG    . SER B 1 179 ? 29.292  5.754   -15.175 1.00 20.87  ? 167 SER B OG    1 
ATOM   3041 N N     . ALA B 1 180 ? 29.310  1.931   -17.578 1.00 18.06  ? 168 ALA B N     1 
ATOM   3042 C CA    . ALA B 1 180 ? 29.256  1.067   -18.758 1.00 16.24  ? 168 ALA B CA    1 
ATOM   3043 C C     . ALA B 1 180 ? 28.011  0.170   -18.732 1.00 16.37  ? 168 ALA B C     1 
ATOM   3044 O O     . ALA B 1 180 ? 27.403  -0.076  -19.783 1.00 16.90  ? 168 ALA B O     1 
ATOM   3045 C CB    . ALA B 1 180 ? 30.527  0.217   -18.816 1.00 17.54  ? 168 ALA B CB    1 
ATOM   3046 N N     . LEU B 1 181 ? 27.614  -0.287  -17.533 1.00 15.59  ? 169 LEU B N     1 
ATOM   3047 C CA    . LEU B 1 181 ? 26.411  -1.114  -17.417 1.00 16.23  ? 169 LEU B CA    1 
ATOM   3048 C C     . LEU B 1 181 ? 25.141  -0.322  -17.669 1.00 16.88  ? 169 LEU B C     1 
ATOM   3049 O O     . LEU B 1 181 ? 24.242  -0.803  -18.347 1.00 15.95  ? 169 LEU B O     1 
ATOM   3050 C CB    . LEU B 1 181 ? 26.355  -1.751  -16.031 1.00 15.32  ? 169 LEU B CB    1 
ATOM   3051 C CG    . LEU B 1 181 ? 27.365  -2.865  -15.782 1.00 16.99  ? 169 LEU B CG    1 
ATOM   3052 C CD1   . LEU B 1 181 ? 27.313  -3.249  -14.316 1.00 17.45  ? 169 LEU B CD1   1 
ATOM   3053 C CD2   . LEU B 1 181 ? 27.099  -4.103  -16.653 1.00 18.87  ? 169 LEU B CD2   1 
ATOM   3054 N N     . VAL B 1 182 ? 25.082  0.930   -17.179 1.00 16.32  ? 170 VAL B N     1 
ATOM   3055 C CA    . VAL B 1 182 ? 23.929  1.801   -17.436 1.00 16.32  ? 170 VAL B CA    1 
ATOM   3056 C C     . VAL B 1 182 ? 23.852  2.151   -18.908 1.00 15.87  ? 170 VAL B C     1 
ATOM   3057 O O     . VAL B 1 182 ? 22.750  2.216   -19.502 1.00 17.19  ? 170 VAL B O     1 
ATOM   3058 C CB    . VAL B 1 182 ? 23.999  3.069   -16.567 1.00 18.51  ? 170 VAL B CB    1 
ATOM   3059 C CG1   . VAL B 1 182 ? 22.971  4.130   -17.036 1.00 19.04  ? 170 VAL B CG1   1 
ATOM   3060 C CG2   . VAL B 1 182 ? 23.813  2.721   -15.110 1.00 19.05  ? 170 VAL B CG2   1 
ATOM   3061 N N     . ILE B 1 183 ? 24.992  2.383   -19.524 1.00 16.06  ? 171 ILE B N     1 
ATOM   3062 C CA    . ILE B 1 183 ? 25.023  2.617   -20.965 1.00 17.85  ? 171 ILE B CA    1 
ATOM   3063 C C     . ILE B 1 183 ? 24.480  1.412   -21.729 1.00 16.69  ? 171 ILE B C     1 
ATOM   3064 O O     . ILE B 1 183 ? 23.670  1.543   -22.654 1.00 17.32  ? 171 ILE B O     1 
ATOM   3065 C CB    . ILE B 1 183 ? 26.441  3.001   -21.406 1.00 16.41  ? 171 ILE B CB    1 
ATOM   3066 C CG1   . ILE B 1 183 ? 26.729  4.459   -20.937 1.00 16.78  ? 171 ILE B CG1   1 
ATOM   3067 C CG2   . ILE B 1 183 ? 26.544  2.931   -22.904 1.00 18.50  ? 171 ILE B CG2   1 
ATOM   3068 C CD1   . ILE B 1 183 ? 28.186  4.830   -21.038 1.00 19.09  ? 171 ILE B CD1   1 
ATOM   3069 N N     . LEU B 1 184 ? 24.961  0.206   -21.380 1.00 16.86  ? 172 LEU B N     1 
ATOM   3070 C CA    . LEU B 1 184 ? 24.422  -0.983  -22.043 1.00 16.06  ? 172 LEU B CA    1 
ATOM   3071 C C     . LEU B 1 184 ? 22.924  -1.077  -21.881 1.00 15.51  ? 172 LEU B C     1 
ATOM   3072 O O     . LEU B 1 184 ? 22.211  -1.316  -22.876 1.00 16.94  ? 172 LEU B O     1 
ATOM   3073 C CB    . LEU B 1 184 ? 25.120  -2.233  -21.500 1.00 17.92  ? 172 LEU B CB    1 
ATOM   3074 C CG    . LEU B 1 184 ? 24.522  -3.573  -21.995 1.00 16.18  ? 172 LEU B CG    1 
ATOM   3075 C CD1   . LEU B 1 184 ? 24.712  -3.694  -23.439 1.00 18.09  ? 172 LEU B CD1   1 
ATOM   3076 C CD2   . LEU B 1 184 ? 25.239  -4.727  -21.231 1.00 18.23  ? 172 LEU B CD2   1 
ATOM   3077 N N     . MET B 1 185 ? 22.454  -0.945  -20.643 1.00 15.57  ? 173 MET B N     1 
ATOM   3078 C CA    . MET B 1 185 ? 21.026  -1.174  -20.425 1.00 17.14  ? 173 MET B CA    1 
ATOM   3079 C C     . MET B 1 185 ? 20.190  -0.100  -21.116 1.00 17.30  ? 173 MET B C     1 
ATOM   3080 O O     . MET B 1 185 ? 19.141  -0.416  -21.699 1.00 18.42  ? 173 MET B O     1 
ATOM   3081 C CB    . MET B 1 185 ? 20.710  -1.307  -18.967 1.00 16.89  ? 173 MET B CB    1 
ATOM   3082 C CG    . MET B 1 185 ? 21.140  -2.686  -18.437 1.00 18.39  ? 173 MET B CG    1 
ATOM   3083 S SD    . MET B 1 185 ? 20.728  -2.992  -16.713 1.00 18.53  ? 173 MET B SD    1 
ATOM   3084 C CE    . MET B 1 185 ? 22.025  -2.052  -15.928 1.00 20.05  ? 173 MET B CE    1 
ATOM   3085 N N     . GLY B 1 186 ? 20.631  1.173   -21.076 1.00 17.73  ? 174 GLY B N     1 
ATOM   3086 C CA    . GLY B 1 186 ? 19.926  2.210   -21.832 1.00 18.66  ? 174 GLY B CA    1 
ATOM   3087 C C     . GLY B 1 186 ? 19.916  1.905   -23.315 1.00 18.39  ? 174 GLY B C     1 
ATOM   3088 O O     . GLY B 1 186 ? 18.869  1.969   -23.960 1.00 19.75  ? 174 GLY B O     1 
ATOM   3089 N N     . SER B 1 187 ? 21.061  1.504   -23.861 1.00 18.88  ? 175 SER B N     1 
ATOM   3090 C CA    A SER B 1 187 ? 21.133  1.191   -25.276 0.70 19.38  ? 175 SER B CA    1 
ATOM   3091 C CA    B SER B 1 187 ? 21.156  1.167   -25.281 0.30 19.41  ? 175 SER B CA    1 
ATOM   3092 C C     . SER B 1 187 ? 20.176  0.056   -25.660 1.00 19.63  ? 175 SER B C     1 
ATOM   3093 O O     . SER B 1 187 ? 19.590  0.074   -26.755 1.00 20.30  ? 175 SER B O     1 
ATOM   3094 C CB    A SER B 1 187 ? 22.565  0.830   -25.675 0.70 20.53  ? 175 SER B CB    1 
ATOM   3095 C CB    B SER B 1 187 ? 22.606  0.781   -25.640 0.30 20.56  ? 175 SER B CB    1 
ATOM   3096 O OG    A SER B 1 187 ? 22.804  -0.539  -25.394 0.70 25.26  ? 175 SER B OG    1 
ATOM   3097 O OG    B SER B 1 187 ? 22.760  0.180   -26.935 0.30 17.88  ? 175 SER B OG    1 
ATOM   3098 N N     . LEU B 1 188 ? 20.002  -0.947  -24.769 1.00 17.85  ? 176 LEU B N     1 
ATOM   3099 C CA    . LEU B 1 188 ? 19.106  -2.056  -25.063 1.00 20.20  ? 176 LEU B CA    1 
ATOM   3100 C C     . LEU B 1 188 ? 17.653  -1.618  -25.069 1.00 19.72  ? 176 LEU B C     1 
ATOM   3101 O O     . LEU B 1 188 ? 16.801  -2.360  -25.584 1.00 22.65  ? 176 LEU B O     1 
ATOM   3102 C CB    . LEU B 1 188 ? 19.303  -3.183  -24.042 1.00 18.27  ? 176 LEU B CB    1 
ATOM   3103 C CG    . LEU B 1 188 ? 20.638  -3.893  -24.197 1.00 19.22  ? 176 LEU B CG    1 
ATOM   3104 C CD1   . LEU B 1 188 ? 20.818  -4.898  -23.013 1.00 19.29  ? 176 LEU B CD1   1 
ATOM   3105 C CD2   . LEU B 1 188 ? 20.783  -4.582  -25.536 1.00 21.22  ? 176 LEU B CD2   1 
ATOM   3106 N N     . MET B 1 189 ? 17.347  -0.440  -24.506 1.00 19.89  ? 177 MET B N     1 
ATOM   3107 C CA    A MET B 1 189 ? 16.007  0.142   -24.563 0.70 21.36  ? 177 MET B CA    1 
ATOM   3108 C CA    B MET B 1 189 ? 16.000  0.112   -24.610 0.30 21.56  ? 177 MET B CA    1 
ATOM   3109 C C     . MET B 1 189 ? 15.943  1.350   -25.499 1.00 21.55  ? 177 MET B C     1 
ATOM   3110 O O     . MET B 1 189 ? 14.981  2.134   -25.443 1.00 22.24  ? 177 MET B O     1 
ATOM   3111 C CB    A MET B 1 189 ? 15.467  0.445   -23.149 0.70 22.34  ? 177 MET B CB    1 
ATOM   3112 C CB    B MET B 1 189 ? 15.417  0.357   -23.222 0.30 22.50  ? 177 MET B CB    1 
ATOM   3113 C CG    A MET B 1 189 ? 15.060  -0.821  -22.341 0.70 24.00  ? 177 MET B CG    1 
ATOM   3114 C CG    B MET B 1 189 ? 15.521  -0.873  -22.340 0.30 20.63  ? 177 MET B CG    1 
ATOM   3115 S SD    A MET B 1 189 ? 14.492  -0.557  -20.602 0.70 32.28  ? 177 MET B SD    1 
ATOM   3116 S SD    B MET B 1 189 ? 14.338  -0.737  -20.997 0.30 19.59  ? 177 MET B SD    1 
ATOM   3117 C CE    A MET B 1 189 ? 16.035  0.027   -19.924 0.70 20.76  ? 177 MET B CE    1 
ATOM   3118 C CE    B MET B 1 189 ? 14.586  0.937   -20.638 0.30 15.87  ? 177 MET B CE    1 
ATOM   3119 N N     . ASN B 1 190 ? 16.926  1.526   -26.380 1.00 19.68  ? 178 ASN B N     1 
ATOM   3120 C CA    . ASN B 1 190 ? 16.954  2.678   -27.295 1.00 23.18  ? 178 ASN B CA    1 
ATOM   3121 C C     . ASN B 1 190 ? 16.945  4.029   -26.564 1.00 20.48  ? 178 ASN B C     1 
ATOM   3122 O O     . ASN B 1 190 ? 16.335  5.001   -27.042 1.00 23.98  ? 178 ASN B O     1 
ATOM   3123 C CB    . ASN B 1 190 ? 15.815  2.605   -28.319 1.00 22.47  ? 178 ASN B CB    1 
ATOM   3124 C CG    . ASN B 1 190 ? 16.048  3.542   -29.471 1.00 30.14  ? 178 ASN B CG    1 
ATOM   3125 O OD1   . ASN B 1 190 ? 17.200  3.843   -29.816 1.00 36.03  ? 178 ASN B OD1   1 
ATOM   3126 N ND2   . ASN B 1 190 ? 14.975  4.064   -30.041 1.00 31.90  ? 178 ASN B ND2   1 
ATOM   3127 N N     . LEU B 1 191 ? 17.579  4.116   -25.406 1.00 19.34  ? 179 LEU B N     1 
ATOM   3128 C CA    . LEU B 1 191 ? 17.664  5.337   -24.622 1.00 20.67  ? 179 LEU B CA    1 
ATOM   3129 C C     . LEU B 1 191 ? 19.108  5.804   -24.606 1.00 21.56  ? 179 LEU B C     1 
ATOM   3130 O O     . LEU B 1 191 ? 20.036  4.975   -24.608 1.00 24.10  ? 179 LEU B O     1 
ATOM   3131 C CB    . LEU B 1 191 ? 17.238  5.094   -23.191 1.00 19.21  ? 179 LEU B CB    1 
ATOM   3132 C CG    . LEU B 1 191 ? 15.797  4.561   -23.070 1.00 19.95  ? 179 LEU B CG    1 
ATOM   3133 C CD1   . LEU B 1 191 ? 15.501  4.345   -21.608 1.00 21.98  ? 179 LEU B CD1   1 
ATOM   3134 C CD2   . LEU B 1 191 ? 14.751  5.514   -23.645 1.00 22.96  ? 179 LEU B CD2   1 
ATOM   3135 N N     . GLY B 1 192 ? 19.299  7.116   -24.545 1.00 21.35  ? 180 GLY B N     1 
ATOM   3136 C CA    . GLY B 1 192 ? 20.629  7.689   -24.477 1.00 21.44  ? 180 GLY B CA    1 
ATOM   3137 C C     . GLY B 1 192 ? 20.946  8.100   -23.047 1.00 19.49  ? 180 GLY B C     1 
ATOM   3138 O O     . GLY B 1 192 ? 20.076  8.170   -22.179 1.00 20.65  ? 180 GLY B O     1 
ATOM   3139 N N     . TRP B 1 193 ? 22.213  8.481   -22.829 1.00 20.25  ? 181 TRP B N     1 
ATOM   3140 C CA    . TRP B 1 193 ? 22.653  8.782   -21.477 1.00 20.47  ? 181 TRP B CA    1 
ATOM   3141 C C     . TRP B 1 193 ? 21.782  9.868   -20.870 1.00 18.95  ? 181 TRP B C     1 
ATOM   3142 O O     . TRP B 1 193 ? 21.591  10.941  -21.459 1.00 21.63  ? 181 TRP B O     1 
ATOM   3143 C CB    . TRP B 1 193 ? 24.101  9.262   -21.498 1.00 20.37  ? 181 TRP B CB    1 
ATOM   3144 C CG    . TRP B 1 193 ? 24.647  9.578   -20.137 1.00 18.73  ? 181 TRP B CG    1 
ATOM   3145 C CD1   . TRP B 1 193 ? 24.714  10.851  -19.556 1.00 19.22  ? 181 TRP B CD1   1 
ATOM   3146 C CD2   . TRP B 1 193 ? 25.216  8.680   -19.174 1.00 18.75  ? 181 TRP B CD2   1 
ATOM   3147 N NE1   . TRP B 1 193 ? 25.236  10.742  -18.302 1.00 19.48  ? 181 TRP B NE1   1 
ATOM   3148 C CE2   . TRP B 1 193 ? 25.620  9.451   -18.047 1.00 19.08  ? 181 TRP B CE2   1 
ATOM   3149 C CE3   . TRP B 1 193 ? 25.445  7.291   -19.152 1.00 17.90  ? 181 TRP B CE3   1 
ATOM   3150 C CZ2   . TRP B 1 193 ? 26.210  8.881   -16.903 1.00 19.57  ? 181 TRP B CZ2   1 
ATOM   3151 C CZ3   . TRP B 1 193 ? 26.043  6.722   -18.028 1.00 22.35  ? 181 TRP B CZ3   1 
ATOM   3152 C CH2   . TRP B 1 193 ? 26.428  7.516   -16.915 1.00 21.21  ? 181 TRP B CH2   1 
ATOM   3153 N N     . GLY B 1 194 ? 21.337  9.630   -19.653 1.00 19.35  ? 182 GLY B N     1 
ATOM   3154 C CA    . GLY B 1 194 ? 20.492  10.558  -18.929 1.00 20.73  ? 182 GLY B CA    1 
ATOM   3155 C C     . GLY B 1 194 ? 19.027  10.179  -18.938 1.00 20.72  ? 182 GLY B C     1 
ATOM   3156 O O     . GLY B 1 194 ? 18.292  10.632  -18.067 1.00 22.01  ? 182 GLY B O     1 
ATOM   3157 N N     . GLN B 1 195 ? 18.583  9.379   -19.920 1.00 19.47  ? 183 GLN B N     1 
ATOM   3158 C CA    . GLN B 1 195 ? 17.180  8.984   -19.920 1.00 19.79  ? 183 GLN B CA    1 
ATOM   3159 C C     . GLN B 1 195 ? 16.907  7.911   -18.865 1.00 18.26  ? 183 GLN B C     1 
ATOM   3160 O O     . GLN B 1 195 ? 16.062  8.097   -17.997 1.00 19.31  ? 183 GLN B O     1 
ATOM   3161 C CB    . GLN B 1 195 ? 16.769  8.533   -21.319 1.00 19.18  ? 183 GLN B CB    1 
ATOM   3162 C CG    . GLN B 1 195 ? 16.815  9.695   -22.300 1.00 20.27  ? 183 GLN B CG    1 
ATOM   3163 C CD    . GLN B 1 195 ? 16.238  9.349   -23.622 1.00 23.42  ? 183 GLN B CD    1 
ATOM   3164 O OE1   . GLN B 1 195 ? 16.799  8.544   -24.350 1.00 22.35  ? 183 GLN B OE1   1 
ATOM   3165 N NE2   . GLN B 1 195 ? 15.122  9.979   -23.978 1.00 25.96  ? 183 GLN B NE2   1 
ATOM   3166 N N     . LEU B 1 196 ? 17.675  6.825   -18.881 1.00 18.48  ? 184 LEU B N     1 
ATOM   3167 C CA    . LEU B 1 196 ? 17.641  5.865   -17.789 1.00 18.36  ? 184 LEU B CA    1 
ATOM   3168 C C     . LEU B 1 196 ? 18.541  6.461   -16.700 1.00 18.17  ? 184 LEU B C     1 
ATOM   3169 O O     . LEU B 1 196 ? 19.754  6.247   -16.634 1.00 18.80  ? 184 LEU B O     1 
ATOM   3170 C CB    . LEU B 1 196 ? 18.192  4.526   -18.250 1.00 18.55  ? 184 LEU B CB    1 
ATOM   3171 C CG    . LEU B 1 196 ? 18.044  3.371   -17.249 1.00 19.88  ? 184 LEU B CG    1 
ATOM   3172 C CD1   . LEU B 1 196 ? 16.620  2.947   -16.955 1.00 21.96  ? 184 LEU B CD1   1 
ATOM   3173 C CD2   . LEU B 1 196 ? 18.880  2.162   -17.787 1.00 21.87  ? 184 LEU B CD2   1 
ATOM   3174 N N     . ASP B 1 197 ? 17.941  7.262   -15.849 1.00 18.36  ? 185 ASP B N     1 
ATOM   3175 C CA    . ASP B 1 197 ? 18.687  8.202   -15.014 1.00 19.63  ? 185 ASP B CA    1 
ATOM   3176 C C     . ASP B 1 197 ? 18.911  7.549   -13.648 1.00 19.83  ? 185 ASP B C     1 
ATOM   3177 O O     . ASP B 1 197 ? 18.220  7.846   -12.660 1.00 20.26  ? 185 ASP B O     1 
ATOM   3178 C CB    . ASP B 1 197 ? 17.893  9.488   -14.905 1.00 20.44  ? 185 ASP B CB    1 
ATOM   3179 C CG    . ASP B 1 197 ? 18.607  10.569  -14.086 1.00 22.22  ? 185 ASP B CG    1 
ATOM   3180 O OD1   . ASP B 1 197 ? 19.860  10.559  -14.042 1.00 21.70  ? 185 ASP B OD1   1 
ATOM   3181 O OD2   . ASP B 1 197 ? 17.908  11.418  -13.488 1.00 23.46  ? 185 ASP B OD2   1 
ATOM   3182 N N     . MET B 1 198 ? 19.910  6.658   -13.607 1.00 19.71  ? 186 MET B N     1 
ATOM   3183 C CA    . MET B 1 198 ? 20.142  5.841   -12.420 1.00 18.59  ? 186 MET B CA    1 
ATOM   3184 C C     . MET B 1 198 ? 21.628  5.598   -12.203 1.00 16.51  ? 186 MET B C     1 
ATOM   3185 O O     . MET B 1 198 ? 22.381  5.492   -13.177 1.00 19.35  ? 186 MET B O     1 
ATOM   3186 C CB    . MET B 1 198 ? 19.495  4.435   -12.650 1.00 21.16  ? 186 MET B CB    1 
ATOM   3187 C CG    . MET B 1 198 ? 17.947  4.498   -12.823 1.00 19.12  ? 186 MET B CG    1 
ATOM   3188 S SD    . MET B 1 198 ? 17.305  2.862   -13.188 1.00 22.36  ? 186 MET B SD    1 
ATOM   3189 C CE    . MET B 1 198 ? 17.492  1.989   -11.625 1.00 21.17  ? 186 MET B CE    1 
ATOM   3190 N N     . ILE B 1 199 ? 22.028  5.537   -10.926 1.00 17.19  ? 187 ILE B N     1 
ATOM   3191 C CA    A ILE B 1 199 ? 23.333  5.006   -10.576 0.70 18.61  ? 187 ILE B CA    1 
ATOM   3192 C CA    B ILE B 1 199 ? 23.344  5.019   -10.509 0.30 18.61  ? 187 ILE B CA    1 
ATOM   3193 C C     . ILE B 1 199 ? 23.128  3.621   -9.979  1.00 18.79  ? 187 ILE B C     1 
ATOM   3194 O O     . ILE B 1 199 ? 22.378  3.451   -9.011  1.00 21.38  ? 187 ILE B O     1 
ATOM   3195 C CB    A ILE B 1 199 ? 24.109  5.938   -9.643  0.70 20.42  ? 187 ILE B CB    1 
ATOM   3196 C CB    B ILE B 1 199 ? 23.954  5.783   -9.326  0.30 18.90  ? 187 ILE B CB    1 
ATOM   3197 C CG1   A ILE B 1 199 ? 25.463  5.328   -9.252  0.70 22.46  ? 187 ILE B CG1   1 
ATOM   3198 C CG1   B ILE B 1 199 ? 24.146  7.262   -9.561  0.30 17.33  ? 187 ILE B CG1   1 
ATOM   3199 C CG2   A ILE B 1 199 ? 23.272  6.326   -8.426  0.70 22.14  ? 187 ILE B CG2   1 
ATOM   3200 C CG2   B ILE B 1 199 ? 25.310  5.108   -8.910  0.30 21.08  ? 187 ILE B CG2   1 
ATOM   3201 C CD1   A ILE B 1 199 ? 26.336  6.408   -8.678  0.70 30.01  ? 187 ILE B CD1   1 
ATOM   3202 C CD1   B ILE B 1 199 ? 24.585  7.937   -8.271  0.30 19.66  ? 187 ILE B CD1   1 
ATOM   3203 N N     . LEU B 1 200 ? 23.846  2.647   -10.530 1.00 17.42  ? 188 LEU B N     1 
ATOM   3204 C CA    . LEU B 1 200 ? 23.683  1.259   -10.046 1.00 17.26  ? 188 LEU B CA    1 
ATOM   3205 C C     . LEU B 1 200 ? 24.379  1.106   -8.701  1.00 16.08  ? 188 LEU B C     1 
ATOM   3206 O O     . LEU B 1 200 ? 25.551  1.469   -8.589  1.00 17.77  ? 188 LEU B O     1 
ATOM   3207 C CB    . LEU B 1 200 ? 24.283  0.295   -11.046 1.00 19.28  ? 188 LEU B CB    1 
ATOM   3208 C CG    . LEU B 1 200 ? 23.641  0.370   -12.417 1.00 17.52  ? 188 LEU B CG    1 
ATOM   3209 C CD1   . LEU B 1 200 ? 24.332  -0.625  -13.298 1.00 19.54  ? 188 LEU B CD1   1 
ATOM   3210 C CD2   . LEU B 1 200 ? 22.133  0.040   -12.315 1.00 21.58  ? 188 LEU B CD2   1 
ATOM   3211 N N     . PRO B 1 201 ? 23.700  0.653   -7.641  1.00 16.81  ? 189 PRO B N     1 
ATOM   3212 C CA    . PRO B 1 201 ? 24.391  0.439   -6.373  1.00 17.47  ? 189 PRO B CA    1 
ATOM   3213 C C     . PRO B 1 201 ? 25.549  -0.554  -6.492  1.00 17.97  ? 189 PRO B C     1 
ATOM   3214 O O     . PRO B 1 201 ? 25.553  -1.447  -7.342  1.00 17.64  ? 189 PRO B O     1 
ATOM   3215 C CB    . PRO B 1 201 ? 23.304  -0.080  -5.437  1.00 20.72  ? 189 PRO B CB    1 
ATOM   3216 C CG    . PRO B 1 201 ? 21.982  0.432   -6.086  1.00 20.55  ? 189 PRO B CG    1 
ATOM   3217 C CD    . PRO B 1 201 ? 22.255  0.406   -7.556  1.00 18.12  ? 189 PRO B CD    1 
ATOM   3218 N N     . LEU B 1 202 ? 26.545  -0.384  -5.628  1.00 18.55  ? 190 LEU B N     1 
ATOM   3219 C CA    . LEU B 1 202 ? 27.600  -1.373  -5.501  1.00 18.03  ? 190 LEU B CA    1 
ATOM   3220 C C     . LEU B 1 202 ? 26.988  -2.736  -5.177  1.00 18.25  ? 190 LEU B C     1 
ATOM   3221 O O     . LEU B 1 202 ? 26.135  -2.860  -4.292  1.00 20.29  ? 190 LEU B O     1 
ATOM   3222 C CB    . LEU B 1 202 ? 28.518  -0.915  -4.373  1.00 19.28  ? 190 LEU B CB    1 
ATOM   3223 C CG    . LEU B 1 202 ? 29.252  0.396   -4.698  1.00 19.70  ? 190 LEU B CG    1 
ATOM   3224 C CD1   . LEU B 1 202 ? 29.787  0.974   -3.396  1.00 22.79  ? 190 LEU B CD1   1 
ATOM   3225 C CD2   . LEU B 1 202 ? 30.366  0.123   -5.726  1.00 20.54  ? 190 LEU B CD2   1 
ATOM   3226 N N     . THR B 1 203 ? 27.510  -3.792  -5.841  1.00 17.34  ? 191 THR B N     1 
ATOM   3227 C CA    . THR B 1 203 ? 27.006  -5.174  -5.772  1.00 16.98  ? 191 THR B CA    1 
ATOM   3228 C C     . THR B 1 203 ? 25.581  -5.326  -6.243  1.00 16.67  ? 191 THR B C     1 
ATOM   3229 O O     . THR B 1 203 ? 24.982  -6.340  -6.002  1.00 18.83  ? 191 THR B O     1 
ATOM   3230 C CB    . THR B 1 203 ? 27.226  -5.898  -4.431  1.00 17.09  ? 191 THR B CB    1 
ATOM   3231 O OG1   . THR B 1 203 ? 26.411  -5.375  -3.370  1.00 18.94  ? 191 THR B OG1   1 
ATOM   3232 C CG2   . THR B 1 203 ? 28.703  -5.885  -4.045  1.00 18.13  ? 191 THR B CG2   1 
ATOM   3233 N N     . SER B 1 204 ? 25.039  -4.345  -6.971  1.00 17.38  ? 192 SER B N     1 
ATOM   3234 C CA    . SER B 1 204 ? 23.685  -4.551  -7.461  1.00 15.71  ? 192 SER B CA    1 
ATOM   3235 C C     . SER B 1 204 ? 23.659  -5.594  -8.570  1.00 15.77  ? 192 SER B C     1 
ATOM   3236 O O     . SER B 1 204 ? 24.628  -5.795  -9.300  1.00 16.98  ? 192 SER B O     1 
ATOM   3237 C CB    . SER B 1 204 ? 23.048  -3.237  -7.960  1.00 17.99  ? 192 SER B CB    1 
ATOM   3238 O OG    . SER B 1 204 ? 23.798  -2.701  -9.055  1.00 17.61  ? 192 SER B OG    1 
ATOM   3239 N N     . VAL B 1 205 ? 22.489  -6.215  -8.720  1.00 16.08  ? 193 VAL B N     1 
ATOM   3240 C CA    . VAL B 1 205 ? 22.192  -7.212  -9.753  1.00 17.33  ? 193 VAL B CA    1 
ATOM   3241 C C     . VAL B 1 205 ? 21.158  -6.621  -10.712 1.00 15.85  ? 193 VAL B C     1 
ATOM   3242 O O     . VAL B 1 205 ? 20.111  -6.121  -10.266 1.00 16.18  ? 193 VAL B O     1 
ATOM   3243 C CB    . VAL B 1 205 ? 21.613  -8.478  -9.093  1.00 17.09  ? 193 VAL B CB    1 
ATOM   3244 C CG1   . VAL B 1 205 ? 21.135  -9.490  -10.140 1.00 21.18  ? 193 VAL B CG1   1 
ATOM   3245 C CG2   . VAL B 1 205 ? 22.675  -9.107  -8.147  1.00 17.96  ? 193 VAL B CG2   1 
ATOM   3246 N N     . SER B 1 206 ? 21.441  -6.716  -11.993 1.00 14.97  ? 194 SER B N     1 
ATOM   3247 C CA    . SER B 1 206 ? 20.490  -6.374  -13.046 1.00 16.22  ? 194 SER B CA    1 
ATOM   3248 C C     . SER B 1 206 ? 20.401  -7.587  -13.949 1.00 17.39  ? 194 SER B C     1 
ATOM   3249 O O     . SER B 1 206 ? 21.392  -8.305  -14.096 1.00 20.80  ? 194 SER B O     1 
ATOM   3250 C CB    . SER B 1 206 ? 21.010  -5.174  -13.849 1.00 16.86  ? 194 SER B CB    1 
ATOM   3251 O OG    . SER B 1 206 ? 21.277  -4.042  -12.994 1.00 16.26  ? 194 SER B OG    1 
ATOM   3252 N N     . VAL B 1 207 ? 19.256  -7.889  -14.501 1.00 17.46  ? 195 VAL B N     1 
ATOM   3253 C CA    . VAL B 1 207 ? 19.069  -9.117  -15.255 1.00 16.03  ? 195 VAL B CA    1 
ATOM   3254 C C     . VAL B 1 207 ? 18.680  -8.777  -16.680 1.00 17.15  ? 195 VAL B C     1 
ATOM   3255 O O     . VAL B 1 207 ? 17.720  -8.010  -16.908 1.00 17.30  ? 195 VAL B O     1 
ATOM   3256 C CB    . VAL B 1 207 ? 17.996  -10.029 -14.637 1.00 18.16  ? 195 VAL B CB    1 
ATOM   3257 C CG1   . VAL B 1 207 ? 17.733  -11.254 -15.525 1.00 17.41  ? 195 VAL B CG1   1 
ATOM   3258 C CG2   . VAL B 1 207 ? 18.409  -10.476 -13.224 1.00 18.33  ? 195 VAL B CG2   1 
ATOM   3259 N N     . LEU B 1 208 ? 19.373  -9.382  -17.646 1.00 16.36  ? 196 LEU B N     1 
ATOM   3260 C CA    . LEU B 1 208 ? 18.966  -9.405  -19.034 1.00 15.45  ? 196 LEU B CA    1 
ATOM   3261 C C     . LEU B 1 208 ? 18.434  -10.777 -19.376 1.00 16.06  ? 196 LEU B C     1 
ATOM   3262 O O     . LEU B 1 208 ? 19.001  -11.819 -18.954 1.00 16.93  ? 196 LEU B O     1 
ATOM   3263 C CB    . LEU B 1 208 ? 20.126  -9.147  -20.006 1.00 16.44  ? 196 LEU B CB    1 
ATOM   3264 C CG    . LEU B 1 208 ? 20.994  -7.932  -19.657 1.00 15.66  ? 196 LEU B CG    1 
ATOM   3265 C CD1   . LEU B 1 208 ? 22.109  -7.838  -20.685 1.00 19.58  ? 196 LEU B CD1   1 
ATOM   3266 C CD2   . LEU B 1 208 ? 20.167  -6.666  -19.658 1.00 17.36  ? 196 LEU B CD2   1 
ATOM   3267 N N     . ALA B 1 209 ? 17.372  -10.800 -20.165 1.00 16.42  ? 197 ALA B N     1 
ATOM   3268 C CA    . ALA B 1 209 ? 16.859  -12.030 -20.751 1.00 17.20  ? 197 ALA B CA    1 
ATOM   3269 C C     . ALA B 1 209 ? 17.317  -12.069 -22.200 1.00 18.48  ? 197 ALA B C     1 
ATOM   3270 O O     . ALA B 1 209 ? 17.240  -11.056 -22.903 1.00 18.52  ? 197 ALA B O     1 
ATOM   3271 C CB    . ALA B 1 209 ? 15.331  -12.067 -20.664 1.00 19.89  ? 197 ALA B CB    1 
ATOM   3272 N N     . VAL B 1 210 ? 17.824  -13.223 -22.657 1.00 18.50  ? 198 VAL B N     1 
ATOM   3273 C CA    . VAL B 1 210 ? 18.515  -13.298 -23.939 1.00 19.25  ? 198 VAL B CA    1 
ATOM   3274 C C     . VAL B 1 210 ? 17.954  -14.464 -24.723 1.00 20.28  ? 198 VAL B C     1 
ATOM   3275 O O     . VAL B 1 210 ? 17.827  -15.589 -24.193 1.00 22.38  ? 198 VAL B O     1 
ATOM   3276 C CB    . VAL B 1 210 ? 20.040  -13.456 -23.754 1.00 21.74  ? 198 VAL B CB    1 
ATOM   3277 C CG1   . VAL B 1 210 ? 20.763  -13.547 -25.126 1.00 25.66  ? 198 VAL B CG1   1 
ATOM   3278 C CG2   . VAL B 1 210 ? 20.624  -12.355 -22.911 1.00 22.76  ? 198 VAL B CG2   1 
ATOM   3279 N N     . LYS B 1 211 ? 17.632  -14.236 -25.991 1.00 20.94  ? 199 LYS B N     1 
ATOM   3280 C CA    . LYS B 1 211 ? 17.184  -15.325 -26.868 1.00 24.05  ? 199 LYS B CA    1 
ATOM   3281 C C     . LYS B 1 211 ? 17.513  -14.935 -28.299 1.00 27.29  ? 199 LYS B C     1 
ATOM   3282 O O     . LYS B 1 211 ? 17.062  -13.882 -28.770 1.00 27.97  ? 199 LYS B O     1 
ATOM   3283 C CB    . LYS B 1 211 ? 15.668  -15.593 -26.729 1.00 26.98  ? 199 LYS B CB    1 
ATOM   3284 C CG    . LYS B 1 211 ? 15.116  -16.684 -27.673 1.00 33.27  ? 199 LYS B CG    1 
ATOM   3285 C CD    . LYS B 1 211 ? 13.623  -16.904 -27.455 1.00 35.17  ? 199 LYS B CD    1 
ATOM   3286 C CE    . LYS B 1 211 ? 13.045  -17.917 -28.462 1.00 38.26  ? 199 LYS B CE    1 
ATOM   3287 N NZ    . LYS B 1 211 ? 13.808  -19.176 -28.421 1.00 43.77  ? 199 LYS B NZ    1 
ATOM   3288 N N     . ASP B 1 212 ? 18.275  -15.784 -28.984 1.00 26.92  ? 200 ASP B N     1 
ATOM   3289 C CA    . ASP B 1 212 ? 18.614  -15.570 -30.391 1.00 31.30  ? 200 ASP B CA    1 
ATOM   3290 C C     . ASP B 1 212 ? 19.137  -14.152 -30.607 1.00 35.10  ? 200 ASP B C     1 
ATOM   3291 O O     . ASP B 1 212 ? 18.615  -13.384 -31.422 1.00 37.77  ? 200 ASP B O     1 
ATOM   3292 C CB    . ASP B 1 212 ? 17.405  -15.845 -31.284 1.00 36.18  ? 200 ASP B CB    1 
ATOM   3293 C CG    . ASP B 1 212 ? 16.840  -17.245 -31.087 1.00 43.90  ? 200 ASP B CG    1 
ATOM   3294 O OD1   . ASP B 1 212 ? 17.641  -18.167 -30.827 1.00 44.89  ? 200 ASP B OD1   1 
ATOM   3295 O OD2   . ASP B 1 212 ? 15.602  -17.418 -31.176 1.00 47.32  ? 200 ASP B OD2   1 
ATOM   3296 N N     . GLU B 1 213 ? 20.154  -13.797 -29.833 1.00 30.33  ? 201 GLU B N     1 
ATOM   3297 C CA    . GLU B 1 213 ? 20.838  -12.504 -30.015 1.00 39.11  ? 201 GLU B CA    1 
ATOM   3298 C C     . GLU B 1 213 ? 20.069  -11.280 -29.509 1.00 34.16  ? 201 GLU B C     1 
ATOM   3299 O O     . GLU B 1 213 ? 20.638  -10.181 -29.424 1.00 32.99  ? 201 GLU B O     1 
ATOM   3300 C CB    . GLU B 1 213 ? 21.243  -12.259 -31.482 1.00 48.09  ? 201 GLU B CB    1 
ATOM   3301 C CG    . GLU B 1 213 ? 22.111  -13.340 -32.122 1.00 55.22  ? 201 GLU B CG    1 
ATOM   3302 C CD    . GLU B 1 213 ? 23.578  -13.215 -31.744 1.00 64.22  ? 201 GLU B CD    1 
ATOM   3303 O OE1   . GLU B 1 213 ? 23.977  -12.132 -31.258 1.00 60.20  ? 201 GLU B OE1   1 
ATOM   3304 O OE2   . GLU B 1 213 ? 24.331  -14.198 -31.943 1.00 68.75  ? 201 GLU B OE2   1 
ATOM   3305 N N     . ARG B 1 214 ? 18.786  -11.448 -29.217 1.00 26.68  ? 202 ARG B N     1 
ATOM   3306 C CA    . ARG B 1 214 ? 18.015  -10.315 -28.668 1.00 27.81  ? 202 ARG B CA    1 
ATOM   3307 C C     . ARG B 1 214 ? 18.237  -10.251 -27.152 1.00 24.34  ? 202 ARG B C     1 
ATOM   3308 O O     . ARG B 1 214 ? 18.261  -11.314 -26.564 1.00 24.28  ? 202 ARG B O     1 
ATOM   3309 C CB    . ARG B 1 214 ? 16.526  -10.514 -28.902 1.00 31.55  ? 202 ARG B CB    1 
ATOM   3310 C CG    . ARG B 1 214 ? 15.699  -9.486  -28.153 1.00 40.83  ? 202 ARG B CG    1 
ATOM   3311 C CD    . ARG B 1 214 ? 14.628  -8.784  -28.964 1.00 57.10  ? 202 ARG B CD    1 
ATOM   3312 N NE    . ARG B 1 214 ? 13.470  -9.632  -28.863 1.00 59.02  ? 202 ARG B NE    1 
ATOM   3313 C CZ    . ARG B 1 214 ? 12.381  -9.352  -28.177 1.00 53.03  ? 202 ARG B CZ    1 
ATOM   3314 N NH1   . ARG B 1 214 ? 11.386  -10.213 -28.171 1.00 44.84  ? 202 ARG B NH1   1 
ATOM   3315 N NH2   . ARG B 1 214 ? 12.255  -8.183  -27.591 1.00 53.24  ? 202 ARG B NH2   1 
ATOM   3316 N N     A MET B 1 215 ? 18.393  -9.107  -26.591 0.70 21.74  ? 203 MET B N     1 
ATOM   3317 N N     B MET B 1 215 ? 18.266  -9.092  -26.557 0.30 21.73  ? 203 MET B N     1 
ATOM   3318 C CA    A MET B 1 215 ? 18.581  -8.922  -25.172 0.70 20.75  ? 203 MET B CA    1 
ATOM   3319 C CA    B MET B 1 215 ? 18.657  -8.886  -25.159 0.30 20.98  ? 203 MET B CA    1 
ATOM   3320 C C     A MET B 1 215 ? 17.495  -7.981  -24.710 0.70 20.48  ? 203 MET B C     1 
ATOM   3321 C C     B MET B 1 215 ? 17.734  -7.872  -24.483 0.30 20.88  ? 203 MET B C     1 
ATOM   3322 O O     A MET B 1 215 ? 17.307  -6.895  -25.302 0.70 22.09  ? 203 MET B O     1 
ATOM   3323 O O     B MET B 1 215 ? 17.886  -6.656  -24.687 0.30 17.05  ? 203 MET B O     1 
ATOM   3324 C CB    A MET B 1 215 ? 19.953  -8.331  -24.829 0.70 22.77  ? 203 MET B CB    1 
ATOM   3325 C CB    B MET B 1 215 ? 20.105  -8.408  -25.065 0.30 22.67  ? 203 MET B CB    1 
ATOM   3326 C CG    A MET B 1 215 ? 21.122  -9.218  -25.144 0.70 24.89  ? 203 MET B CG    1 
ATOM   3327 C CG    B MET B 1 215 ? 21.059  -8.970  -26.103 0.30 26.08  ? 203 MET B CG    1 
ATOM   3328 S SD    A MET B 1 215 ? 22.596  -8.217  -24.737 0.70 26.18  ? 203 MET B SD    1 
ATOM   3329 S SD    B MET B 1 215 ? 22.724  -8.564  -25.556 0.30 31.41  ? 203 MET B SD    1 
ATOM   3330 C CE    A MET B 1 215 ? 23.831  -9.383  -25.343 0.70 34.04  ? 203 MET B CE    1 
ATOM   3331 C CE    B MET B 1 215 ? 22.719  -9.625  -24.157 0.30 17.79  ? 203 MET B CE    1 
ATOM   3332 N N     . VAL B 1 216 ? 16.826  -8.362  -23.635 1.00 17.90  ? 204 VAL B N     1 
ATOM   3333 C CA    . VAL B 1 216 ? 15.751  -7.581  -23.036 1.00 18.00  ? 204 VAL B CA    1 
ATOM   3334 C C     . VAL B 1 216 ? 16.173  -7.233  -21.621 1.00 17.69  ? 204 VAL B C     1 
ATOM   3335 O O     . VAL B 1 216 ? 16.634  -8.100  -20.861 1.00 17.82  ? 204 VAL B O     1 
ATOM   3336 C CB    . VAL B 1 216 ? 14.465  -8.434  -23.009 1.00 21.43  ? 204 VAL B CB    1 
ATOM   3337 C CG1   . VAL B 1 216 ? 13.390  -7.748  -22.165 1.00 24.89  ? 204 VAL B CG1   1 
ATOM   3338 C CG2   . VAL B 1 216 ? 13.932  -8.599  -24.401 1.00 24.17  ? 204 VAL B CG2   1 
ATOM   3339 N N     . VAL B 1 217 ? 16.010  -5.976  -21.231 1.00 17.08  ? 205 VAL B N     1 
ATOM   3340 C CA    . VAL B 1 217 ? 16.337  -5.591  -19.864 1.00 16.92  ? 205 VAL B CA    1 
ATOM   3341 C C     . VAL B 1 217 ? 15.164  -6.000  -18.978 1.00 17.95  ? 205 VAL B C     1 
ATOM   3342 O O     . VAL B 1 217 ? 14.066  -5.419  -19.096 1.00 19.68  ? 205 VAL B O     1 
ATOM   3343 C CB    . VAL B 1 217 ? 16.600  -4.074  -19.759 1.00 16.66  ? 205 VAL B CB    1 
ATOM   3344 C CG1   . VAL B 1 217 ? 16.915  -3.725  -18.337 1.00 19.17  ? 205 VAL B CG1   1 
ATOM   3345 C CG2   . VAL B 1 217 ? 17.767  -3.705  -20.665 1.00 18.74  ? 205 VAL B CG2   1 
ATOM   3346 N N     . ARG B 1 218 ? 15.403  -6.941  -18.048 1.00 17.23  ? 206 ARG B N     1 
ATOM   3347 C CA    . ARG B 1 218 ? 14.312  -7.399  -17.186 1.00 17.83  ? 206 ARG B CA    1 
ATOM   3348 C C     . ARG B 1 218 ? 14.324  -6.774  -15.815 1.00 17.64  ? 206 ARG B C     1 
ATOM   3349 O O     . ARG B 1 218 ? 13.254  -6.503  -15.262 1.00 18.53  ? 206 ARG B O     1 
ATOM   3350 C CB    . ARG B 1 218 ? 14.348  -8.915  -17.034 1.00 22.11  ? 206 ARG B CB    1 
ATOM   3351 C CG    . ARG B 1 218 ? 13.040  -9.395  -16.313 1.00 25.23  ? 206 ARG B CG    1 
ATOM   3352 C CD    . ARG B 1 218 ? 12.758  -10.828 -16.513 1.00 23.60  ? 206 ARG B CD    1 
ATOM   3353 N NE    . ARG B 1 218 ? 12.413  -11.087 -17.886 1.00 22.81  ? 206 ARG B NE    1 
ATOM   3354 C CZ    . ARG B 1 218 ? 12.460  -12.272 -18.484 1.00 27.53  ? 206 ARG B CZ    1 
ATOM   3355 N NH1   . ARG B 1 218 ? 12.877  -13.373 -17.847 1.00 30.40  ? 206 ARG B NH1   1 
ATOM   3356 N NH2   . ARG B 1 218 ? 12.120  -12.347 -19.756 1.00 27.73  ? 206 ARG B NH2   1 
ATOM   3357 N N     . SER B 1 219 ? 15.496  -6.498  -15.245 1.00 16.84  ? 207 SER B N     1 
ATOM   3358 C CA    . SER B 1 219 ? 15.537  -5.859  -13.956 1.00 17.33  ? 207 SER B CA    1 
ATOM   3359 C C     . SER B 1 219 ? 16.836  -5.092  -13.834 1.00 16.25  ? 207 SER B C     1 
ATOM   3360 O O     . SER B 1 219 ? 17.808  -5.390  -14.529 1.00 16.96  ? 207 SER B O     1 
ATOM   3361 C CB    . SER B 1 219 ? 15.319  -6.816  -12.786 1.00 16.50  ? 207 SER B CB    1 
ATOM   3362 O OG    . SER B 1 219 ? 16.361  -7.804  -12.752 1.00 19.13  ? 207 SER B OG    1 
ATOM   3363 N N     . ILE B 1 220 ? 16.818  -4.055  -12.987 1.00 16.42  ? 208 ILE B N     1 
ATOM   3364 C CA    . ILE B 1 220 ? 17.905  -3.086  -12.948 1.00 16.16  ? 208 ILE B CA    1 
ATOM   3365 C C     . ILE B 1 220 ? 18.244  -2.732  -11.527 1.00 16.72  ? 208 ILE B C     1 
ATOM   3366 O O     . ILE B 1 220 ? 17.395  -2.236  -10.777 1.00 17.41  ? 208 ILE B O     1 
ATOM   3367 C CB    . ILE B 1 220 ? 17.536  -1.786  -13.678 1.00 17.36  ? 208 ILE B CB    1 
ATOM   3368 C CG1   . ILE B 1 220 ? 17.147  -2.046  -15.105 1.00 16.96  ? 208 ILE B CG1   1 
ATOM   3369 C CG2   . ILE B 1 220 ? 18.771  -0.834  -13.681 1.00 16.69  ? 208 ILE B CG2   1 
ATOM   3370 C CD1   . ILE B 1 220 ? 16.590  -0.832  -15.829 1.00 19.28  ? 208 ILE B CD1   1 
ATOM   3371 N N     . GLY B 1 221 ? 19.512  -2.902  -11.149 1.00 15.82  ? 209 GLY B N     1 
ATOM   3372 C CA    . GLY B 1 221 ? 19.991  -2.155  -9.998  1.00 17.08  ? 209 GLY B CA    1 
ATOM   3373 C C     . GLY B 1 221 ? 19.729  -2.652  -8.593  1.00 16.17  ? 209 GLY B C     1 
ATOM   3374 O O     . GLY B 1 221 ? 19.865  -1.877  -7.631  1.00 18.24  ? 209 GLY B O     1 
ATOM   3375 N N     . ASP B 1 222 ? 19.328  -3.921  -8.418  1.00 17.30  ? 210 ASP B N     1 
ATOM   3376 C CA    . ASP B 1 222 ? 18.884  -4.414  -7.108  1.00 17.47  ? 210 ASP B CA    1 
ATOM   3377 C C     . ASP B 1 222 ? 20.089  -4.753  -6.211  1.00 17.46  ? 210 ASP B C     1 
ATOM   3378 O O     . ASP B 1 222 ? 20.841  -5.704  -6.479  1.00 17.69  ? 210 ASP B O     1 
ATOM   3379 C CB    . ASP B 1 222 ? 17.981  -5.630  -7.329  1.00 17.45  ? 210 ASP B CB    1 
ATOM   3380 C CG    . ASP B 1 222 ? 17.389  -6.172  -6.049  1.00 21.03  ? 210 ASP B CG    1 
ATOM   3381 O OD1   . ASP B 1 222 ? 18.146  -6.608  -5.169  1.00 19.20  ? 210 ASP B OD1   1 
ATOM   3382 O OD2   . ASP B 1 222 ? 16.153  -6.170  -5.936  1.00 19.37  ? 210 ASP B OD2   1 
ATOM   3383 N N     . ALA B 1 223 ? 20.213  -4.069  -5.097  1.00 17.92  ? 211 ALA B N     1 
ATOM   3384 C CA    . ALA B 1 223 ? 21.183  -4.419  -4.061  1.00 19.65  ? 211 ALA B CA    1 
ATOM   3385 C C     . ALA B 1 223 ? 20.465  -4.641  -2.742  1.00 20.04  ? 211 ALA B C     1 
ATOM   3386 O O     . ALA B 1 223 ? 20.952  -4.273  -1.675  1.00 22.34  ? 211 ALA B O     1 
ATOM   3387 C CB    . ALA B 1 223 ? 22.298  -3.370  -3.934  1.00 21.47  ? 211 ALA B CB    1 
ATOM   3388 N N     . THR B 1 224 ? 19.288  -5.286  -2.805  1.00 19.94  ? 212 THR B N     1 
ATOM   3389 C CA    . THR B 1 224 ? 18.469  -5.518  -1.619  1.00 20.80  ? 212 THR B CA    1 
ATOM   3390 C C     . THR B 1 224 ? 19.083  -6.505  -0.629  1.00 21.63  ? 212 THR B C     1 
ATOM   3391 O O     . THR B 1 224 ? 18.648  -6.559  0.532   1.00 22.76  ? 212 THR B O     1 
ATOM   3392 C CB    . THR B 1 224 ? 17.078  -5.991  -2.031  1.00 23.42  ? 212 THR B CB    1 
ATOM   3393 O OG1   . THR B 1 224 ? 17.174  -7.181  -2.832  1.00 20.48  ? 212 THR B OG1   1 
ATOM   3394 C CG2   . THR B 1 224 ? 16.328  -4.856  -2.815  1.00 25.89  ? 212 THR B CG2   1 
ATOM   3395 N N     . HIS B 1 225 ? 20.150  -7.218  -1.026  1.00 20.04  ? 213 HIS B N     1 
ATOM   3396 C CA    . HIS B 1 225 ? 20.868  -8.025  -0.051  1.00 21.95  ? 213 HIS B CA    1 
ATOM   3397 C C     . HIS B 1 225 ? 21.622  -7.178  0.976   1.00 21.57  ? 213 HIS B C     1 
ATOM   3398 O O     . HIS B 1 225 ? 22.118  -7.738  1.957   1.00 24.97  ? 213 HIS B O     1 
ATOM   3399 C CB    . HIS B 1 225 ? 21.892  -8.972  -0.738  1.00 22.61  ? 213 HIS B CB    1 
ATOM   3400 C CG    . HIS B 1 225 ? 22.763  -8.254  -1.712  1.00 20.65  ? 213 HIS B CG    1 
ATOM   3401 N ND1   . HIS B 1 225 ? 22.316  -7.909  -2.967  1.00 20.27  ? 213 HIS B ND1   1 
ATOM   3402 C CD2   . HIS B 1 225 ? 24.013  -7.740  -1.588  1.00 21.53  ? 213 HIS B CD2   1 
ATOM   3403 C CE1   . HIS B 1 225 ? 23.271  -7.239  -3.596  1.00 19.71  ? 213 HIS B CE1   1 
ATOM   3404 N NE2   . HIS B 1 225 ? 24.308  -7.116  -2.781  1.00 22.67  ? 213 HIS B NE2   1 
ATOM   3405 N N     . LEU B 1 226 ? 21.768  -5.857  0.747   1.00 21.07  ? 214 LEU B N     1 
ATOM   3406 C CA    . LEU B 1 226 ? 22.374  -4.987  1.744   1.00 24.11  ? 214 LEU B CA    1 
ATOM   3407 C C     . LEU B 1 226 ? 21.375  -4.393  2.721   1.00 23.73  ? 214 LEU B C     1 
ATOM   3408 O O     . LEU B 1 226 ? 21.804  -3.790  3.706   1.00 25.59  ? 214 LEU B O     1 
ATOM   3409 C CB    . LEU B 1 226 ? 23.132  -3.841  1.066   1.00 22.85  ? 214 LEU B CB    1 
ATOM   3410 C CG    . LEU B 1 226 ? 24.178  -4.303  0.029   1.00 22.87  ? 214 LEU B CG    1 
ATOM   3411 C CD1   . LEU B 1 226 ? 24.791  -3.063  -0.716  1.00 24.96  ? 214 LEU B CD1   1 
ATOM   3412 C CD2   . LEU B 1 226 ? 25.260  -5.154  0.681   1.00 25.84  ? 214 LEU B CD2   1 
ATOM   3413 N N     . ALA B 1 227 ? 20.067  -4.599  2.513   1.00 22.47  ? 215 ALA B N     1 
ATOM   3414 C CA    . ALA B 1 227 ? 19.095  -3.875  3.342   1.00 26.17  ? 215 ALA B CA    1 
ATOM   3415 C C     . ALA B 1 227 ? 19.199  -4.207  4.827   1.00 25.38  ? 215 ALA B C     1 
ATOM   3416 O O     . ALA B 1 227 ? 18.912  -3.354  5.687   1.00 28.58  ? 215 ALA B O     1 
ATOM   3417 C CB    . ALA B 1 227 ? 17.673  -4.164  2.851   1.00 27.50  ? 215 ALA B CB    1 
ATOM   3418 N N     . ALA B 1 228 ? 19.551  -5.443  5.169   1.00 25.32  ? 216 ALA B N     1 
ATOM   3419 C CA    . ALA B 1 228 ? 19.612  -5.881  6.556   1.00 29.34  ? 216 ALA B CA    1 
ATOM   3420 C C     . ALA B 1 228 ? 21.005  -5.745  7.156   1.00 27.73  ? 216 ALA B C     1 
ATOM   3421 O O     . ALA B 1 228 ? 21.190  -6.092  8.331   1.00 31.38  ? 216 ALA B O     1 
ATOM   3422 C CB    . ALA B 1 228 ? 19.177  -7.349  6.690   1.00 29.09  ? 216 ALA B CB    1 
ATOM   3423 N N     . ALA B 1 229 ? 21.966  -5.243  6.363   1.00 26.49  ? 217 ALA B N     1 
ATOM   3424 C CA    . ALA B 1 229 ? 23.365  -5.163  6.789   1.00 28.24  ? 217 ALA B CA    1 
ATOM   3425 C C     . ALA B 1 229 ? 23.556  -4.017  7.778   1.00 27.84  ? 217 ALA B C     1 
ATOM   3426 O O     . ALA B 1 229 ? 22.737  -3.095  7.819   1.00 28.15  ? 217 ALA B O     1 
ATOM   3427 C CB    . ALA B 1 229 ? 24.215  -4.862  5.561   1.00 28.51  ? 217 ALA B CB    1 
ATOM   3428 N N     . PRO B 1 230 ? 24.663  -4.013  8.536   1.00 29.57  ? 218 PRO B N     1 
ATOM   3429 C CA    . PRO B 1 230 ? 24.995  -2.826  9.335   1.00 30.21  ? 218 PRO B CA    1 
ATOM   3430 C C     . PRO B 1 230 ? 25.094  -1.593  8.451   1.00 26.96  ? 218 PRO B C     1 
ATOM   3431 O O     . PRO B 1 230 ? 25.427  -1.663  7.263   1.00 30.62  ? 218 PRO B O     1 
ATOM   3432 C CB    . PRO B 1 230 ? 26.358  -3.182  9.948   1.00 31.90  ? 218 PRO B CB    1 
ATOM   3433 C CG    . PRO B 1 230 ? 26.360  -4.677  10.043  1.00 30.82  ? 218 PRO B CG    1 
ATOM   3434 C CD    . PRO B 1 230 ? 25.610  -5.120  8.783   1.00 31.44  ? 218 PRO B CD    1 
ATOM   3435 N N     . SER B 1 231 ? 24.812  -0.437  9.058   1.00 32.10  ? 219 SER B N     1 
ATOM   3436 C CA    . SER B 1 231 ? 24.672  0.775   8.264   1.00 32.19  ? 219 SER B CA    1 
ATOM   3437 C C     . SER B 1 231 ? 25.967  1.182   7.566   1.00 33.45  ? 219 SER B C     1 
ATOM   3438 O O     . SER B 1 231 ? 25.910  1.895   6.562   1.00 39.00  ? 219 SER B O     1 
ATOM   3439 C CB    . SER B 1 231 ? 24.123  1.907   9.138   1.00 36.34  ? 219 SER B CB    1 
ATOM   3440 O OG    . SER B 1 231 ? 25.009  2.192   10.200  1.00 37.34  ? 219 SER B OG    1 
ATOM   3441 N N     . ASP B 1 232 ? 27.124  0.738   8.063   1.00 31.55  ? 220 ASP B N     1 
ATOM   3442 C CA    . ASP B 1 232 ? 28.404  1.062   7.448   1.00 32.15  ? 220 ASP B CA    1 
ATOM   3443 C C     . ASP B 1 232 ? 28.760  0.143   6.280   1.00 34.23  ? 220 ASP B C     1 
ATOM   3444 O O     . ASP B 1 232 ? 29.850  0.276   5.714   1.00 32.33  ? 220 ASP B O     1 
ATOM   3445 C CB    . ASP B 1 232 ? 29.536  1.096   8.492   1.00 33.86  ? 220 ASP B CB    1 
ATOM   3446 C CG    . ASP B 1 232 ? 29.814  -0.262  9.128   1.00 34.04  ? 220 ASP B CG    1 
ATOM   3447 O OD1   . ASP B 1 232 ? 29.052  -1.218  8.899   1.00 31.82  ? 220 ASP B OD1   1 
ATOM   3448 O OD2   . ASP B 1 232 ? 30.814  -0.385  9.877   1.00 39.18  ? 220 ASP B OD2   1 
ATOM   3449 N N     . VAL B 1 233 ? 27.878  -0.779  5.906   1.00 28.72  ? 221 VAL B N     1 
ATOM   3450 C CA    . VAL B 1 233 ? 28.135  -1.675  4.784   1.00 26.18  ? 221 VAL B CA    1 
ATOM   3451 C C     . VAL B 1 233 ? 27.296  -1.222  3.597   1.00 29.31  ? 221 VAL B C     1 
ATOM   3452 O O     . VAL B 1 233 ? 27.650  -1.463  2.435   1.00 28.27  ? 221 VAL B O     1 
ATOM   3453 C CB    . VAL B 1 233 ? 27.807  -3.126  5.180   1.00 27.61  ? 221 VAL B CB    1 
ATOM   3454 C CG1   . VAL B 1 233 ? 27.812  -4.036  3.944   1.00 29.91  ? 221 VAL B CG1   1 
ATOM   3455 C CG2   . VAL B 1 233 ? 28.807  -3.635  6.194   1.00 30.93  ? 221 VAL B CG2   1 
ATOM   3456 N N     . ILE B 1 234 ? 26.181  -0.558  3.880   1.00 29.89  ? 222 ILE B N     1 
ATOM   3457 C CA    . ILE B 1 234 ? 25.213  -0.192  2.855   1.00 33.18  ? 222 ILE B CA    1 
ATOM   3458 C C     . ILE B 1 234 ? 25.828  0.812   1.872   1.00 34.10  ? 222 ILE B C     1 
ATOM   3459 O O     . ILE B 1 234 ? 26.487  1.765   2.274   1.00 36.42  ? 222 ILE B O     1 
ATOM   3460 C CB    . ILE B 1 234 ? 23.877  0.266   3.484   1.00 33.64  ? 222 ILE B CB    1 
ATOM   3461 C CG1   . ILE B 1 234 ? 23.405  -0.802  4.487   1.00 40.83  ? 222 ILE B CG1   1 
ATOM   3462 C CG2   . ILE B 1 234 ? 22.846  0.511   2.395   1.00 38.12  ? 222 ILE B CG2   1 
ATOM   3463 C CD1   . ILE B 1 234 ? 22.162  -0.467  5.318   1.00 37.81  ? 222 ILE B CD1   1 
ATOM   3464 O OXT   . ILE B 1 234 ? 25.708  0.667   0.649   1.00 38.93  ? 222 ILE B OXT   1 
HETATM 3465 O O4    . RS3 C 2 .   ? -0.309  -3.250  -26.033 1.00 24.37  ? 301 RS3 A O4    1 
HETATM 3466 C C4    . RS3 C 2 .   ? -0.827  -3.528  -24.786 1.00 21.84  ? 301 RS3 A C4    1 
HETATM 3467 N N3    . RS3 C 2 .   ? -2.109  -3.814  -24.684 1.00 22.28  ? 301 RS3 A N3    1 
HETATM 3468 C C2    . RS3 C 2 .   ? -2.625  -4.106  -23.479 1.00 25.38  ? 301 RS3 A C2    1 
HETATM 3469 O O2    . RS3 C 2 .   ? -3.942  -4.301  -23.412 1.00 24.55  ? 301 RS3 A O2    1 
HETATM 3470 C C4A   . RS3 C 2 .   ? -0.038  -3.488  -23.620 1.00 21.23  ? 301 RS3 A C4A   1 
HETATM 3471 C C10   . RS3 C 2 .   ? -0.604  -3.885  -22.442 1.00 20.75  ? 301 RS3 A C10   1 
HETATM 3472 N N1    . RS3 C 2 .   ? -1.945  -4.120  -22.367 1.00 20.66  ? 301 RS3 A N1    1 
HETATM 3473 N N5    . RS3 C 2 .   ? 1.346   -3.286  -23.778 1.00 20.62  ? 301 RS3 A N5    1 
HETATM 3474 C C5A   . RS3 C 2 .   ? 2.080   -3.325  -22.624 1.00 20.47  ? 301 RS3 A C5A   1 
HETATM 3475 C C6    . RS3 C 2 .   ? 3.511   -3.071  -22.662 1.00 21.95  ? 301 RS3 A C6    1 
HETATM 3476 C C7    . RS3 C 2 .   ? 4.279   -3.098  -21.493 1.00 19.61  ? 301 RS3 A C7    1 
HETATM 3477 C C7M   . RS3 C 2 .   ? 5.829   -2.933  -21.526 1.00 22.71  ? 301 RS3 A C7M   1 
HETATM 3478 C C8    . RS3 C 2 .   ? 3.638   -3.287  -20.276 1.00 21.85  ? 301 RS3 A C8    1 
HETATM 3479 N N8    . RS3 C 2 .   ? 4.387   -3.241  -19.034 1.00 22.95  ? 301 RS3 A N8    1 
HETATM 3480 C C9    . RS3 C 2 .   ? 2.257   -3.531  -20.216 1.00 20.62  ? 301 RS3 A C9    1 
HETATM 3481 C C9A   . RS3 C 2 .   ? 1.481   -3.611  -21.394 1.00 20.13  ? 301 RS3 A C9A   1 
HETATM 3482 N N10   . RS3 C 2 .   ? 0.134   -3.936  -21.291 1.00 19.73  ? 301 RS3 A N10   1 
HETATM 3483 C "C1'" . RS3 C 2 .   ? -0.483  -4.372  -20.070 1.00 20.51  ? 301 RS3 A "C1'" 1 
HETATM 3484 C "C2'" . RS3 C 2 .   ? -0.102  -5.878  -19.809 1.00 24.74  ? 301 RS3 A "C2'" 1 
HETATM 3485 O "O2'" . RS3 C 2 .   ? -0.396  -6.696  -20.940 1.00 26.56  ? 301 RS3 A "O2'" 1 
HETATM 3486 C "C3'" . RS3 C 2 .   ? -0.948  -6.460  -18.652 1.00 29.25  ? 301 RS3 A "C3'" 1 
HETATM 3487 O "O3'" . RS3 C 2 .   ? -2.362  -6.266  -18.885 1.00 29.98  ? 301 RS3 A "O3'" 1 
HETATM 3488 C "C4'" . RS3 C 2 .   ? -0.535  -5.818  -17.323 1.00 27.69  ? 301 RS3 A "C4'" 1 
HETATM 3489 O "O4'" . RS3 C 2 .   ? 0.769   -6.328  -17.124 1.00 30.54  ? 301 RS3 A "O4'" 1 
HETATM 3490 C "C5'" . RS3 C 2 .   ? -1.506  -6.287  -16.181 1.00 28.97  ? 301 RS3 A "C5'" 1 
HETATM 3491 O "O5'" . RS3 C 2 .   ? -1.293  -5.684  -14.882 1.00 27.03  ? 301 RS3 A "O5'" 1 
HETATM 3492 C C1    . GOL D 3 .   ? -6.039  -5.875  -14.655 1.00 39.19  ? 302 GOL A C1    1 
HETATM 3493 O O1    . GOL D 3 .   ? -6.371  -4.840  -13.765 1.00 32.38  ? 302 GOL A O1    1 
HETATM 3494 C C2    . GOL D 3 .   ? -7.329  -6.697  -14.824 1.00 48.90  ? 302 GOL A C2    1 
HETATM 3495 O O2    . GOL D 3 .   ? -7.660  -7.395  -13.681 1.00 38.98  ? 302 GOL A O2    1 
HETATM 3496 C C3    . GOL D 3 .   ? -8.404  -5.644  -15.130 1.00 41.17  ? 302 GOL A C3    1 
HETATM 3497 O O3    . GOL D 3 .   ? -8.137  -5.228  -16.414 1.00 41.10  ? 302 GOL A O3    1 
HETATM 3498 O O4    . RS3 E 2 .   ? 28.425  14.199  -13.967 1.00 20.46  ? 301 RS3 B O4    1 
HETATM 3499 C C4    . RS3 E 2 .   ? 29.254  13.091  -13.847 1.00 21.19  ? 301 RS3 B C4    1 
HETATM 3500 N N3    . RS3 E 2 .   ? 30.552  13.249  -13.828 1.00 19.71  ? 301 RS3 B N3    1 
HETATM 3501 C C2    . RS3 E 2 .   ? 31.341  12.163  -13.738 1.00 20.57  ? 301 RS3 B C2    1 
HETATM 3502 O O2    . RS3 E 2 .   ? 32.622  12.349  -13.696 1.00 21.60  ? 301 RS3 B O2    1 
HETATM 3503 C C4A   . RS3 E 2 .   ? 28.663  11.824  -13.619 1.00 19.49  ? 301 RS3 B C4A   1 
HETATM 3504 C C10   . RS3 E 2 .   ? 29.523  10.757  -13.527 1.00 19.84  ? 301 RS3 B C10   1 
HETATM 3505 N N1    . RS3 E 2 .   ? 30.858  10.935  -13.541 1.00 18.47  ? 301 RS3 B N1    1 
HETATM 3506 N N5    . RS3 E 2 .   ? 27.291  11.688  -13.627 1.00 18.73  ? 301 RS3 B N5    1 
HETATM 3507 C C5A   . RS3 E 2 .   ? 26.778  10.413  -13.491 1.00 17.57  ? 301 RS3 B C5A   1 
HETATM 3508 C C6    . RS3 E 2 .   ? 25.366  10.223  -13.510 1.00 19.47  ? 301 RS3 B C6    1 
HETATM 3509 C C7    . RS3 E 2 .   ? 24.834  8.941   -13.349 1.00 17.77  ? 301 RS3 B C7    1 
HETATM 3510 C C7M   . RS3 E 2 .   ? 23.322  8.724   -13.320 1.00 19.46  ? 301 RS3 B C7M   1 
HETATM 3511 C C8    . RS3 E 2 .   ? 25.728  7.846   -13.326 1.00 17.67  ? 301 RS3 B C8    1 
HETATM 3512 N N8    . RS3 E 2 .   ? 25.199  6.487   -13.269 1.00 19.18  ? 301 RS3 B N8    1 
HETATM 3513 C C9    . RS3 E 2 .   ? 27.114  8.001   -13.361 1.00 17.75  ? 301 RS3 B C9    1 
HETATM 3514 C C9A   . RS3 E 2 .   ? 27.659  9.310   -13.409 1.00 17.93  ? 301 RS3 B C9A   1 
HETATM 3515 N N10   . RS3 E 2 .   ? 29.014  9.508   -13.268 1.00 17.71  ? 301 RS3 B N10   1 
HETATM 3516 C "C1'" . RS3 E 2 .   ? 29.884  8.366   -13.067 1.00 19.21  ? 301 RS3 B "C1'" 1 
HETATM 3517 C "C2'" . RS3 E 2 .   ? 29.764  7.849   -11.615 1.00 22.21  ? 301 RS3 B "C2'" 1 
HETATM 3518 O "O2'" . RS3 E 2 .   ? 30.159  8.850   -10.659 1.00 23.75  ? 301 RS3 B "O2'" 1 
HETATM 3519 C "C3'" . RS3 E 2 .   ? 30.615  6.536   -11.539 1.00 26.35  ? 301 RS3 B "C3'" 1 
HETATM 3520 O "O3'" . RS3 E 2 .   ? 29.941  5.479   -12.293 1.00 26.18  ? 301 RS3 B "O3'" 1 
HETATM 3521 C "C4'" . RS3 E 2 .   ? 30.703  6.005   -10.107 1.00 30.94  ? 301 RS3 B "C4'" 1 
HETATM 3522 O "O4'" . RS3 E 2 .   ? 31.603  4.875   -10.047 1.00 27.44  ? 301 RS3 B "O4'" 1 
HETATM 3523 C "C5'" . RS3 E 2 .   ? 29.347  5.501   -9.646  1.00 33.49  ? 301 RS3 B "C5'" 1 
HETATM 3524 O "O5'" . RS3 E 2 .   ? 29.488  5.347   -8.240  1.00 27.02  ? 301 RS3 B "O5'" 1 
HETATM 3525 O O     . HOH F 4 .   ? 5.677   6.996   -17.971 1.00 26.43  ? 401 HOH A O     1 
HETATM 3526 O O     . HOH F 4 .   ? 1.297   -1.971  7.577   1.00 29.14  ? 402 HOH A O     1 
HETATM 3527 O O     . HOH F 4 .   ? -11.113 -7.069  -3.967  1.00 33.63  ? 403 HOH A O     1 
HETATM 3528 O O     . HOH F 4 .   ? -6.013  -3.266  -24.538 1.00 26.20  ? 404 HOH A O     1 
HETATM 3529 O O     . HOH F 4 .   ? -3.319  -9.502  6.071   1.00 44.31  ? 405 HOH A O     1 
HETATM 3530 O O     . HOH F 4 .   ? -7.456  -2.287  -14.181 1.00 27.04  ? 406 HOH A O     1 
HETATM 3531 O O     . HOH F 4 .   ? -7.933  -0.571  -11.870 1.00 35.30  ? 407 HOH A O     1 
HETATM 3532 O O     . HOH F 4 .   ? -5.990  -2.867  7.558   1.00 48.03  ? 408 HOH A O     1 
HETATM 3533 O O     . HOH F 4 .   ? -1.083  -29.166 -5.735  1.00 39.15  ? 409 HOH A O     1 
HETATM 3534 O O     . HOH F 4 .   ? -7.616  -9.749  -7.801  1.00 23.95  ? 410 HOH A O     1 
HETATM 3535 O O     . HOH F 4 .   ? 15.384  10.786  -17.316 1.00 22.62  ? 411 HOH A O     1 
HETATM 3536 O O     . HOH F 4 .   ? 11.017  -5.805  -16.706 1.00 24.33  ? 412 HOH A O     1 
HETATM 3537 O O     . HOH F 4 .   ? 11.822  12.066  -9.292  1.00 37.69  ? 413 HOH A O     1 
HETATM 3538 O O     . HOH F 4 .   ? -16.656 -9.064  -7.353  1.00 34.56  ? 414 HOH A O     1 
HETATM 3539 O O     . HOH F 4 .   ? 14.826  -4.042  -6.849  1.00 20.86  ? 415 HOH A O     1 
HETATM 3540 O O     . HOH F 4 .   ? -8.541  -9.865  -0.512  1.00 40.45  ? 416 HOH A O     1 
HETATM 3541 O O     . HOH F 4 .   ? 5.425   11.572  2.698   1.00 40.00  ? 417 HOH A O     1 
HETATM 3542 O O     . HOH F 4 .   ? 3.711   -15.192 5.140   1.00 31.85  ? 418 HOH A O     1 
HETATM 3543 O O     . HOH F 4 .   ? -5.113  -3.816  -21.055 1.00 29.10  ? 419 HOH A O     1 
HETATM 3544 O O     . HOH F 4 .   ? -16.257 -16.283 -13.918 1.00 42.99  ? 420 HOH A O     1 
HETATM 3545 O O     . HOH F 4 .   ? -15.816 -8.405  -13.774 1.00 21.67  ? 421 HOH A O     1 
HETATM 3546 O O     . HOH F 4 .   ? 1.279   -8.955  -17.266 1.00 31.52  ? 422 HOH A O     1 
HETATM 3547 O O     . HOH F 4 .   ? 19.107  1.521   -1.301  1.00 42.16  ? 423 HOH A O     1 
HETATM 3548 O O     . HOH F 4 .   ? -9.589  -4.954  -0.702  1.00 40.44  ? 424 HOH A O     1 
HETATM 3549 O O     . HOH F 4 .   ? -10.709 -7.553  -23.019 1.00 31.18  ? 425 HOH A O     1 
HETATM 3550 O O     . HOH F 4 .   ? 12.379  -4.819  -21.155 1.00 19.95  ? 426 HOH A O     1 
HETATM 3551 O O     . HOH F 4 .   ? 5.601   7.175   -27.758 1.00 37.27  ? 427 HOH A O     1 
HETATM 3552 O O     . HOH F 4 .   ? 31.725  3.756   -4.833  1.00 35.78  ? 428 HOH A O     1 
HETATM 3553 O O     . HOH F 4 .   ? 5.099   0.805   -25.510 1.00 27.71  ? 429 HOH A O     1 
HETATM 3554 O O     . HOH F 4 .   ? -7.824  8.532   -13.028 1.00 30.69  ? 430 HOH A O     1 
HETATM 3555 O O     . HOH F 4 .   ? -7.793  -4.562  -21.631 1.00 23.01  ? 431 HOH A O     1 
HETATM 3556 O O     . HOH F 4 .   ? -0.183  -6.383  -12.504 1.00 20.15  ? 432 HOH A O     1 
HETATM 3557 O O     . HOH F 4 .   ? -0.118  -0.095  -8.640  1.00 21.04  ? 433 HOH A O     1 
HETATM 3558 O O     . HOH F 4 .   ? 6.912   2.678   -20.024 1.00 22.15  ? 434 HOH A O     1 
HETATM 3559 O O     . HOH F 4 .   ? 6.567   0.003   -23.338 1.00 24.08  ? 435 HOH A O     1 
HETATM 3560 O O     . HOH F 4 .   ? 34.355  11.237  -10.472 1.00 29.36  ? 436 HOH A O     1 
HETATM 3561 O O     . HOH F 4 .   ? 18.333  -0.603  5.384   1.00 35.86  ? 437 HOH A O     1 
HETATM 3562 O O     . HOH F 4 .   ? 8.776   5.422   -19.436 1.00 20.89  ? 438 HOH A O     1 
HETATM 3563 O O     . HOH F 4 .   ? 8.203   -4.065  -8.882  1.00 19.90  ? 439 HOH A O     1 
HETATM 3564 O O     . HOH F 4 .   ? -5.404  -18.406 -3.773  1.00 26.11  ? 440 HOH A O     1 
HETATM 3565 O O     . HOH F 4 .   ? 1.753   -7.770  15.396  1.00 24.55  ? 441 HOH A O     1 
HETATM 3566 O O     . HOH F 4 .   ? 7.183   -18.152 2.732   1.00 40.01  ? 442 HOH A O     1 
HETATM 3567 O O     . HOH F 4 .   ? 20.899  7.650   1.668   1.00 43.19  ? 443 HOH A O     1 
HETATM 3568 O O     . HOH F 4 .   ? 12.687  -16.806 -1.164  1.00 30.00  ? 444 HOH A O     1 
HETATM 3569 O O     . HOH F 4 .   ? -3.511  -6.172  -12.789 1.00 35.14  ? 445 HOH A O     1 
HETATM 3570 O O     . HOH F 4 .   ? -9.180  -5.810  -9.633  1.00 42.28  ? 446 HOH A O     1 
HETATM 3571 O O     . HOH F 4 .   ? 25.028  16.450  -5.598  1.00 32.78  ? 447 HOH A O     1 
HETATM 3572 O O     . HOH F 4 .   ? 7.319   6.719   -25.780 1.00 32.70  ? 448 HOH A O     1 
HETATM 3573 O O     . HOH F 4 .   ? 2.443   0.128   -25.510 1.00 24.39  ? 449 HOH A O     1 
HETATM 3574 O O     . HOH F 4 .   ? 31.285  17.987  -7.194  1.00 41.94  ? 450 HOH A O     1 
HETATM 3575 O O     . HOH F 4 .   ? -3.627  -7.201  7.444   1.00 35.28  ? 451 HOH A O     1 
HETATM 3576 O O     . HOH F 4 .   ? 7.741   -3.321  11.786  1.00 34.76  ? 452 HOH A O     1 
HETATM 3577 O O     . HOH F 4 .   ? 16.164  -0.642  7.389   1.00 35.72  ? 453 HOH A O     1 
HETATM 3578 O O     . HOH F 4 .   ? -5.272  -0.865  -26.209 1.00 27.67  ? 454 HOH A O     1 
HETATM 3579 O O     . HOH F 4 .   ? 1.041   -23.110 -4.327  1.00 29.06  ? 455 HOH A O     1 
HETATM 3580 O O     . HOH F 4 .   ? -8.466  3.658   -12.699 1.00 29.87  ? 456 HOH A O     1 
HETATM 3581 O O     . HOH F 4 .   ? -7.712  -13.357 -2.490  1.00 36.52  ? 457 HOH A O     1 
HETATM 3582 O O     . HOH F 4 .   ? -0.676  9.465   4.969   1.00 40.40  ? 458 HOH A O     1 
HETATM 3583 O O     . HOH F 4 .   ? 12.675  -0.205  -26.131 1.00 35.24  ? 459 HOH A O     1 
HETATM 3584 O O     . HOH F 4 .   ? 18.322  4.235   1.289   1.00 45.47  ? 460 HOH A O     1 
HETATM 3585 O O     . HOH F 4 .   ? -7.860  -10.186 -13.647 1.00 34.14  ? 461 HOH A O     1 
HETATM 3586 O O     . HOH F 4 .   ? -2.234  -3.089  -17.119 1.00 35.45  ? 462 HOH A O     1 
HETATM 3587 O O     . HOH F 4 .   ? -4.726  -6.998  -30.612 1.00 39.48  ? 463 HOH A O     1 
HETATM 3588 O O     . HOH F 4 .   ? -1.602  -14.634 1.424   1.00 28.69  ? 464 HOH A O     1 
HETATM 3589 O O     . HOH F 4 .   ? -5.814  7.329   -22.191 1.00 36.18  ? 465 HOH A O     1 
HETATM 3590 O O     . HOH F 4 .   ? 14.108  -17.675 -3.144  1.00 30.85  ? 466 HOH A O     1 
HETATM 3591 O O     . HOH F 4 .   ? 23.015  13.841  -13.299 1.00 26.15  ? 467 HOH A O     1 
HETATM 3592 O O     . HOH F 4 .   ? -4.992  11.230  -10.723 1.00 30.30  ? 468 HOH A O     1 
HETATM 3593 O O     . HOH F 4 .   ? -0.513  -5.766  13.276  1.00 27.07  ? 469 HOH A O     1 
HETATM 3594 O O     . HOH F 4 .   ? 2.481   -2.515  -26.263 1.00 23.12  ? 470 HOH A O     1 
HETATM 3595 O O     . HOH F 4 .   ? 5.085   4.117   -31.828 1.00 42.95  ? 471 HOH A O     1 
HETATM 3596 O O     . HOH F 4 .   ? -1.117  -24.914 -3.835  1.00 33.62  ? 472 HOH A O     1 
HETATM 3597 O O     A HOH F 4 .   ? 14.941  8.745   -10.203 0.50 30.84  ? 473 HOH A O     1 
HETATM 3598 O O     B HOH F 4 .   ? 15.534  10.627  -10.937 0.50 30.84  ? 473 HOH A O     1 
HETATM 3599 O O     . HOH F 4 .   ? 6.673   4.461   -17.921 1.00 20.57  ? 474 HOH A O     1 
HETATM 3600 O O     . HOH F 4 .   ? 3.243   6.143   -25.218 1.00 35.99  ? 475 HOH A O     1 
HETATM 3601 O O     . HOH F 4 .   ? 1.090   -18.244 -0.416  1.00 31.84  ? 476 HOH A O     1 
HETATM 3602 O O     . HOH F 4 .   ? -6.619  -5.309  4.312   1.00 46.38  ? 477 HOH A O     1 
HETATM 3603 O O     . HOH F 4 .   ? -2.026  9.279   -21.658 1.00 29.04  ? 478 HOH A O     1 
HETATM 3604 O O     . HOH F 4 .   ? 12.865  7.588   -26.187 1.00 45.91  ? 479 HOH A O     1 
HETATM 3605 O O     . HOH F 4 .   ? -0.004  12.219  -0.528  1.00 34.86  ? 480 HOH A O     1 
HETATM 3606 O O     . HOH F 4 .   ? 9.512   -3.462  -27.151 1.00 37.87  ? 481 HOH A O     1 
HETATM 3607 O O     . HOH F 4 .   ? 5.982   -2.425  -31.972 1.00 33.74  ? 482 HOH A O     1 
HETATM 3608 O O     . HOH F 4 .   ? -1.537  11.570  -19.973 1.00 26.85  ? 483 HOH A O     1 
HETATM 3609 O O     . HOH F 4 .   ? 0.307   6.896   -27.514 1.00 37.24  ? 484 HOH A O     1 
HETATM 3610 O O     . HOH F 4 .   ? 15.587  -8.725  -0.650  1.00 29.27  ? 485 HOH A O     1 
HETATM 3611 O O     . HOH F 4 .   ? 9.261   -9.456  -17.123 1.00 27.89  ? 486 HOH A O     1 
HETATM 3612 O O     . HOH F 4 .   ? -8.489  3.814   -0.448  1.00 37.09  ? 487 HOH A O     1 
HETATM 3613 O O     . HOH F 4 .   ? -1.006  -23.205 -1.119  1.00 31.89  ? 488 HOH A O     1 
HETATM 3614 O O     . HOH F 4 .   ? -6.319  0.417   5.205   1.00 40.46  ? 489 HOH A O     1 
HETATM 3615 O O     . HOH F 4 .   ? -6.277  -1.549  -22.169 1.00 23.75  ? 490 HOH A O     1 
HETATM 3616 O O     . HOH F 4 .   ? 14.861  -12.993 4.401   1.00 39.43  ? 491 HOH A O     1 
HETATM 3617 O O     . HOH F 4 .   ? -7.625  2.376   -24.855 1.00 39.30  ? 492 HOH A O     1 
HETATM 3618 O O     . HOH F 4 .   ? -6.421  -2.853  -9.572  1.00 24.81  ? 493 HOH A O     1 
HETATM 3619 O O     . HOH F 4 .   ? 8.156   -10.667 4.425   1.00 26.29  ? 494 HOH A O     1 
HETATM 3620 O O     . HOH F 4 .   ? 7.029   -21.520 -3.125  1.00 27.66  ? 495 HOH A O     1 
HETATM 3621 O O     . HOH F 4 .   ? 18.076  -1.984  -4.684  1.00 28.18  ? 496 HOH A O     1 
HETATM 3622 O O     . HOH F 4 .   ? -4.862  -22.176 -9.515  1.00 39.42  ? 497 HOH A O     1 
HETATM 3623 O O     . HOH F 4 .   ? -1.538  -22.105 -11.031 1.00 30.26  ? 498 HOH A O     1 
HETATM 3624 O O     . HOH F 4 .   ? 6.224   -12.566 -14.384 1.00 30.11  ? 499 HOH A O     1 
HETATM 3625 O O     . HOH F 4 .   ? 17.618  -1.796  0.035   1.00 38.50  ? 500 HOH A O     1 
HETATM 3626 O O     . HOH F 4 .   ? 25.543  19.979  -12.467 1.00 38.75  ? 501 HOH A O     1 
HETATM 3627 O O     . HOH F 4 .   ? -1.339  -14.383 5.590   1.00 45.81  ? 502 HOH A O     1 
HETATM 3628 O O     . HOH F 4 .   ? -3.857  9.927   2.147   1.00 37.12  ? 503 HOH A O     1 
HETATM 3629 O O     . HOH F 4 .   ? -3.406  -7.347  -21.493 1.00 34.64  ? 504 HOH A O     1 
HETATM 3630 O O     . HOH F 4 .   ? -9.870  8.390   -16.477 1.00 41.63  ? 505 HOH A O     1 
HETATM 3631 O O     . HOH F 4 .   ? 14.377  6.727   7.034   1.00 41.01  ? 506 HOH A O     1 
HETATM 3632 O O     . HOH F 4 .   ? -17.657 -1.043  -18.241 1.00 36.79  ? 507 HOH A O     1 
HETATM 3633 O O     . HOH F 4 .   ? 19.358  7.604   5.207   1.00 39.55  ? 508 HOH A O     1 
HETATM 3634 O O     . HOH F 4 .   ? 14.663  15.035  -17.981 1.00 36.26  ? 509 HOH A O     1 
HETATM 3635 O O     . HOH F 4 .   ? 10.697  -6.412  -19.431 1.00 19.65  ? 510 HOH A O     1 
HETATM 3636 O O     . HOH F 4 .   ? 11.042  -5.831  10.239  1.00 38.22  ? 511 HOH A O     1 
HETATM 3637 O O     . HOH F 4 .   ? -1.402  -16.687 -0.507  1.00 32.63  ? 512 HOH A O     1 
HETATM 3638 O O     . HOH F 4 .   ? 12.507  -4.253  -24.236 1.00 35.93  ? 513 HOH A O     1 
HETATM 3639 O O     . HOH F 4 .   ? -7.761  6.333   -1.063  1.00 49.65  ? 514 HOH A O     1 
HETATM 3640 O O     . HOH F 4 .   ? 13.187  -8.380  9.901   1.00 49.56  ? 515 HOH A O     1 
HETATM 3641 O O     . HOH F 4 .   ? 8.853   4.744   -26.904 1.00 37.58  ? 516 HOH A O     1 
HETATM 3642 O O     . HOH F 4 .   ? 11.561  4.511   -26.557 1.00 28.38  ? 517 HOH A O     1 
HETATM 3643 O O     . HOH F 4 .   ? 5.776   0.235   -20.710 1.00 24.60  ? 518 HOH A O     1 
HETATM 3644 O O     . HOH F 4 .   ? -8.158  -2.263  -7.468  1.00 32.03  ? 519 HOH A O     1 
HETATM 3645 O O     . HOH F 4 .   ? 2.511   -25.860 -0.438  1.00 31.13  ? 520 HOH A O     1 
HETATM 3646 O O     . HOH F 4 .   ? 14.065  -12.731 -12.805 1.00 41.41  ? 521 HOH A O     1 
HETATM 3647 O O     . HOH F 4 .   ? -7.854  -18.462 -2.565  1.00 35.70  ? 522 HOH A O     1 
HETATM 3648 O O     . HOH F 4 .   ? -5.250  -27.352 -4.093  1.00 36.56  ? 523 HOH A O     1 
HETATM 3649 O O     . HOH F 4 .   ? 8.174   -22.903 -5.192  1.00 36.36  ? 524 HOH A O     1 
HETATM 3650 O O     . HOH F 4 .   ? -4.109  8.975   -23.166 1.00 33.73  ? 525 HOH A O     1 
HETATM 3651 O O     . HOH G 4 .   ? 38.888  4.157   -24.616 1.00 37.18  ? 401 HOH B O     1 
HETATM 3652 O O     . HOH G 4 .   ? 23.742  -11.353 -28.884 1.00 37.46  ? 402 HOH B O     1 
HETATM 3653 O O     . HOH G 4 .   ? 32.986  -19.132 -15.242 1.00 23.67  ? 403 HOH B O     1 
HETATM 3654 O O     . HOH G 4 .   ? 34.315  1.832   -11.823 1.00 35.92  ? 404 HOH B O     1 
HETATM 3655 O O     . HOH G 4 .   ? 21.198  -7.545  4.330   1.00 43.54  ? 405 HOH B O     1 
HETATM 3656 O O     . HOH G 4 .   ? 40.432  -14.061 -12.875 1.00 40.28  ? 406 HOH B O     1 
HETATM 3657 O O     . HOH G 4 .   ? -18.727 -15.210 -18.528 1.00 28.25  ? 407 HOH B O     1 
HETATM 3658 O O     . HOH G 4 .   ? 33.605  22.719  -17.283 1.00 30.99  ? 408 HOH B O     1 
HETATM 3659 O O     . HOH G 4 .   ? 39.821  -1.887  -9.222  1.00 22.32  ? 409 HOH B O     1 
HETATM 3660 O O     . HOH G 4 .   ? 32.527  3.467   -12.093 1.00 25.94  ? 410 HOH B O     1 
HETATM 3661 O O     . HOH G 4 .   ? 32.504  9.675   -11.398 1.00 31.39  ? 411 HOH B O     1 
HETATM 3662 O O     . HOH G 4 .   ? 17.682  -7.340  -10.565 1.00 21.45  ? 412 HOH B O     1 
HETATM 3663 O O     . HOH G 4 .   ? 12.429  2.432   -25.049 1.00 22.84  ? 413 HOH B O     1 
HETATM 3664 O O     . HOH G 4 .   ? 39.146  6.641   -13.871 1.00 34.99  ? 414 HOH B O     1 
HETATM 3665 O O     . HOH G 4 .   ? 26.289  10.502  -26.234 1.00 31.79  ? 415 HOH B O     1 
HETATM 3666 O O     . HOH G 4 .   ? 34.184  5.205   -9.827  1.00 33.53  ? 416 HOH B O     1 
HETATM 3667 O O     A HOH G 4 .   ? 32.744  -11.684 -22.315 0.50 21.38  ? 417 HOH B O     1 
HETATM 3668 O O     B HOH G 4 .   ? 33.437  -14.091 -23.130 0.50 24.25  ? 417 HOH B O     1 
HETATM 3669 O O     . HOH G 4 .   ? 21.665  -10.133 2.901   1.00 36.28  ? 418 HOH B O     1 
HETATM 3670 O O     . HOH G 4 .   ? 38.880  13.921  -20.858 1.00 39.26  ? 419 HOH B O     1 
HETATM 3671 O O     . HOH G 4 .   ? 31.896  0.934   -31.846 1.00 38.45  ? 420 HOH B O     1 
HETATM 3672 O O     . HOH G 4 .   ? 19.789  3.241   -9.521  1.00 29.36  ? 421 HOH B O     1 
HETATM 3673 O O     . HOH G 4 .   ? 19.069  -23.629 -20.379 1.00 33.52  ? 422 HOH B O     1 
HETATM 3674 O O     . HOH G 4 .   ? 26.723  -27.973 -19.825 1.00 22.47  ? 423 HOH B O     1 
HETATM 3675 O O     . HOH G 4 .   ? 17.490  7.273   -10.163 1.00 21.15  ? 424 HOH B O     1 
HETATM 3676 O O     . HOH G 4 .   ? 29.189  20.949  -14.908 1.00 30.54  ? 425 HOH B O     1 
HETATM 3677 O O     . HOH G 4 .   ? 37.547  4.069   -16.296 1.00 24.61  ? 426 HOH B O     1 
HETATM 3678 O O     . HOH G 4 .   ? 4.206   -10.955 -29.106 1.00 39.34  ? 427 HOH B O     1 
HETATM 3679 O O     . HOH G 4 .   ? 10.803  -16.925 -20.844 1.00 36.63  ? 428 HOH B O     1 
HETATM 3680 O O     . HOH G 4 .   ? -13.797 -14.617 -22.709 1.00 36.93  ? 429 HOH B O     1 
HETATM 3681 O O     . HOH G 4 .   ? 32.258  -16.702 -1.543  1.00 27.16  ? 430 HOH B O     1 
HETATM 3682 O O     . HOH G 4 .   ? 35.902  0.346   4.318   1.00 34.60  ? 431 HOH B O     1 
HETATM 3683 O O     . HOH G 4 .   ? 28.890  -24.219 -16.238 1.00 28.30  ? 432 HOH B O     1 
HETATM 3684 O O     . HOH G 4 .   ? 39.772  13.607  -11.825 1.00 30.57  ? 433 HOH B O     1 
HETATM 3685 O O     . HOH G 4 .   ? 34.097  -20.915 -20.915 1.00 34.38  ? 434 HOH B O     1 
HETATM 3686 O O     . HOH G 4 .   ? 29.469  -14.966 1.525   1.00 27.43  ? 435 HOH B O     1 
HETATM 3687 O O     . HOH G 4 .   ? 15.075  -16.809 -13.450 1.00 36.80  ? 436 HOH B O     1 
HETATM 3688 O O     . HOH G 4 .   ? 34.298  10.400  -14.536 1.00 25.18  ? 437 HOH B O     1 
HETATM 3689 O O     . HOH G 4 .   ? 34.143  14.096  -15.092 1.00 23.10  ? 438 HOH B O     1 
HETATM 3690 O O     . HOH G 4 .   ? 19.432  12.286  -22.378 1.00 32.85  ? 439 HOH B O     1 
HETATM 3691 O O     . HOH G 4 .   ? 51.179  -0.717  -5.450  1.00 32.64  ? 440 HOH B O     1 
HETATM 3692 O O     . HOH G 4 .   ? 17.389  -4.723  -26.923 1.00 28.28  ? 441 HOH B O     1 
HETATM 3693 O O     . HOH G 4 .   ? 27.229  2.035   -1.131  1.00 39.56  ? 442 HOH B O     1 
HETATM 3694 O O     . HOH G 4 .   ? 31.109  -2.892  -17.206 1.00 19.31  ? 443 HOH B O     1 
HETATM 3695 O O     . HOH G 4 .   ? 20.277  -25.796 -21.237 1.00 32.52  ? 444 HOH B O     1 
HETATM 3696 O O     . HOH G 4 .   ? 31.585  -9.287  6.456   1.00 41.16  ? 445 HOH B O     1 
HETATM 3697 O O     . HOH G 4 .   ? 19.376  5.906   -20.854 1.00 21.75  ? 446 HOH B O     1 
HETATM 3698 O O     . HOH G 4 .   ? 31.412  -2.072  11.929  1.00 37.44  ? 447 HOH B O     1 
HETATM 3699 O O     . HOH G 4 .   ? 40.396  -6.053  -0.352  1.00 28.65  ? 448 HOH B O     1 
HETATM 3700 O O     . HOH G 4 .   ? 38.117  1.684   -17.625 1.00 31.76  ? 449 HOH B O     1 
HETATM 3701 O O     . HOH G 4 .   ? 15.410  11.762  -14.541 1.00 29.47  ? 450 HOH B O     1 
HETATM 3702 O O     . HOH G 4 .   ? -12.863 -12.117 -24.765 1.00 39.91  ? 451 HOH B O     1 
HETATM 3703 O O     . HOH G 4 .   ? 37.167  -12.147 -3.390  1.00 31.80  ? 452 HOH B O     1 
HETATM 3704 O O     . HOH G 4 .   ? 22.383  4.901   -23.079 1.00 27.81  ? 453 HOH B O     1 
HETATM 3705 O O     . HOH G 4 .   ? 25.464  13.245  -16.888 1.00 20.55  ? 454 HOH B O     1 
HETATM 3706 O O     . HOH G 4 .   ? 21.639  6.933   -18.505 1.00 19.99  ? 455 HOH B O     1 
HETATM 3707 O O     . HOH G 4 .   ? 23.703  -4.164  -11.719 1.00 18.06  ? 456 HOH B O     1 
HETATM 3708 O O     . HOH G 4 .   ? 31.100  -21.009 -17.896 1.00 41.66  ? 457 HOH B O     1 
HETATM 3709 O O     . HOH G 4 .   ? 14.022  -13.547 -15.356 1.00 38.64  ? 458 HOH B O     1 
HETATM 3710 O O     . HOH G 4 .   ? 37.800  2.500   -22.620 1.00 29.59  ? 459 HOH B O     1 
HETATM 3711 O O     . HOH G 4 .   ? 35.842  2.587   -27.427 1.00 27.67  ? 460 HOH B O     1 
HETATM 3712 O O     . HOH G 4 .   ? 22.760  12.719  -17.023 1.00 23.96  ? 461 HOH B O     1 
HETATM 3713 O O     . HOH G 4 .   ? 35.692  -20.258 -7.693  1.00 36.84  ? 462 HOH B O     1 
HETATM 3714 O O     . HOH G 4 .   ? 20.775  14.630  -23.359 1.00 35.30  ? 463 HOH B O     1 
HETATM 3715 O O     . HOH G 4 .   ? 32.750  -16.605 -26.411 1.00 27.56  ? 464 HOH B O     1 
HETATM 3716 O O     . HOH G 4 .   ? 25.379  -22.996 -9.542  1.00 27.39  ? 465 HOH B O     1 
HETATM 3717 O O     . HOH G 4 .   ? 40.210  -14.195 -14.977 1.00 38.69  ? 466 HOH B O     1 
HETATM 3718 O O     . HOH G 4 .   ? 12.321  -15.858 -18.922 1.00 42.09  ? 467 HOH B O     1 
HETATM 3719 O O     . HOH G 4 .   ? 30.845  -18.571 -19.053 1.00 25.92  ? 468 HOH B O     1 
HETATM 3720 O O     . HOH G 4 .   ? 18.777  -7.500  3.132   1.00 34.14  ? 469 HOH B O     1 
HETATM 3721 O O     . HOH G 4 .   ? 36.819  11.487  -14.290 1.00 23.90  ? 470 HOH B O     1 
HETATM 3722 O O     . HOH G 4 .   ? 10.932  -9.227  -19.380 1.00 28.48  ? 471 HOH B O     1 
HETATM 3723 O O     . HOH G 4 .   ? 23.225  2.205   -28.774 1.00 42.27  ? 472 HOH B O     1 
HETATM 3724 O O     . HOH G 4 .   ? 25.940  -15.288 -27.662 1.00 25.89  ? 473 HOH B O     1 
HETATM 3725 O O     . HOH G 4 .   ? 42.131  -6.968  -5.582  1.00 33.04  ? 474 HOH B O     1 
HETATM 3726 O O     . HOH G 4 .   ? 19.201  -23.487 -14.170 1.00 36.22  ? 475 HOH B O     1 
HETATM 3727 O O     . HOH G 4 .   ? 31.453  1.110   -11.079 1.00 22.69  ? 476 HOH B O     1 
HETATM 3728 O O     . HOH G 4 .   ? 23.325  12.282  -23.173 1.00 33.38  ? 477 HOH B O     1 
HETATM 3729 O O     . HOH G 4 .   ? 20.003  -2.709  8.197   1.00 35.79  ? 478 HOH B O     1 
HETATM 3730 O O     . HOH G 4 .   ? 11.226  -5.998  -26.196 1.00 37.88  ? 479 HOH B O     1 
HETATM 3731 O O     . HOH G 4 .   ? 23.123  -12.134 1.662   1.00 30.18  ? 480 HOH B O     1 
HETATM 3732 O O     . HOH G 4 .   ? 18.703  13.717  -12.112 1.00 37.11  ? 481 HOH B O     1 
HETATM 3733 O O     . HOH G 4 .   ? 5.321   -3.169  -26.477 1.00 28.17  ? 482 HOH B O     1 
HETATM 3734 O O     . HOH G 4 .   ? 40.195  12.333  -24.378 1.00 43.82  ? 483 HOH B O     1 
HETATM 3735 O O     . HOH G 4 .   ? 36.619  -17.763 -6.802  1.00 36.41  ? 484 HOH B O     1 
HETATM 3736 O O     . HOH G 4 .   ? 24.756  -22.212 -23.431 1.00 28.22  ? 485 HOH B O     1 
HETATM 3737 O O     . HOH G 4 .   ? 46.003  -1.025  -13.076 1.00 38.99  ? 486 HOH B O     1 
HETATM 3738 O O     . HOH G 4 .   ? 37.445  -7.804  5.683   1.00 42.48  ? 487 HOH B O     1 
HETATM 3739 O O     . HOH G 4 .   ? 33.869  -23.671 -3.081  1.00 40.98  ? 488 HOH B O     1 
HETATM 3740 O O     . HOH G 4 .   ? -15.204 -10.453 -18.359 1.00 33.15  ? 489 HOH B O     1 
HETATM 3741 O O     . HOH G 4 .   ? 12.898  -19.971 -21.147 1.00 33.61  ? 490 HOH B O     1 
HETATM 3742 O O     . HOH G 4 .   ? 21.851  10.385  -16.017 1.00 21.78  ? 491 HOH B O     1 
HETATM 3743 O O     . HOH G 4 .   ? 33.168  -0.381  -29.252 1.00 28.08  ? 492 HOH B O     1 
HETATM 3744 O O     . HOH G 4 .   ? 32.076  19.611  -10.800 1.00 32.50  ? 493 HOH B O     1 
HETATM 3745 O O     . HOH G 4 .   ? 25.639  14.055  -14.382 1.00 22.10  ? 494 HOH B O     1 
HETATM 3746 O O     . HOH G 4 .   ? 21.070  -18.023 -2.065  1.00 34.25  ? 495 HOH B O     1 
HETATM 3747 O O     . HOH G 4 .   ? 29.290  8.157   -8.025  1.00 24.23  ? 496 HOH B O     1 
HETATM 3748 O O     . HOH G 4 .   ? 22.191  3.969   -6.240  1.00 30.49  ? 497 HOH B O     1 
HETATM 3749 O O     . HOH G 4 .   ? 47.355  -2.771  -11.063 1.00 33.74  ? 498 HOH B O     1 
HETATM 3750 O O     . HOH G 4 .   ? 32.912  10.914  -26.848 1.00 27.73  ? 499 HOH B O     1 
HETATM 3751 O O     . HOH G 4 .   ? 38.923  -4.636  -18.078 1.00 30.66  ? 500 HOH B O     1 
HETATM 3752 O O     . HOH G 4 .   ? 39.996  0.230   -1.576  1.00 40.95  ? 501 HOH B O     1 
HETATM 3753 O O     . HOH G 4 .   ? 30.084  -3.782  9.554   1.00 36.64  ? 502 HOH B O     1 
HETATM 3754 O O     . HOH G 4 .   ? 35.015  -6.627  5.667   1.00 33.91  ? 503 HOH B O     1 
HETATM 3755 O O     . HOH G 4 .   ? 34.821  11.601  -17.061 1.00 21.62  ? 504 HOH B O     1 
HETATM 3756 O O     . HOH G 4 .   ? 29.164  -8.988  5.116   1.00 25.38  ? 505 HOH B O     1 
HETATM 3757 O O     . HOH G 4 .   ? 32.851  15.351  -17.290 1.00 22.90  ? 506 HOH B O     1 
HETATM 3758 O O     . HOH G 4 .   ? 26.096  -8.148  -29.547 1.00 37.08  ? 507 HOH B O     1 
HETATM 3759 O O     . HOH G 4 .   ? 34.334  -22.397 -14.720 1.00 39.19  ? 508 HOH B O     1 
HETATM 3760 O O     . HOH G 4 .   ? 37.613  -0.469  -15.679 1.00 25.00  ? 509 HOH B O     1 
HETATM 3761 O O     . HOH G 4 .   ? 35.418  -13.060 -27.499 1.00 35.72  ? 510 HOH B O     1 
HETATM 3762 O O     . HOH G 4 .   ? 38.521  -18.164 -10.612 1.00 35.81  ? 511 HOH B O     1 
HETATM 3763 O O     . HOH G 4 .   ? 40.097  -12.867 -9.815  1.00 36.15  ? 512 HOH B O     1 
HETATM 3764 O O     . HOH G 4 .   ? 34.689  -10.506 0.379   1.00 36.85  ? 513 HOH B O     1 
HETATM 3765 O O     . HOH G 4 .   ? 28.936  9.983   -26.739 1.00 22.62  ? 514 HOH B O     1 
HETATM 3766 O O     . HOH G 4 .   ? 32.118  7.128   -32.338 1.00 30.34  ? 515 HOH B O     1 
HETATM 3767 O O     . HOH G 4 .   ? 44.004  -0.743  -3.509  1.00 35.52  ? 516 HOH B O     1 
HETATM 3768 O O     . HOH G 4 .   ? 21.937  4.857   -20.383 1.00 20.49  ? 517 HOH B O     1 
HETATM 3769 O O     . HOH G 4 .   ? 18.694  -20.955 -21.006 1.00 29.01  ? 518 HOH B O     1 
HETATM 3770 O O     . HOH G 4 .   ? 20.153  6.871   -33.184 1.00 34.38  ? 519 HOH B O     1 
HETATM 3771 O O     . HOH G 4 .   ? 18.951  -13.373 -5.856  1.00 29.51  ? 520 HOH B O     1 
HETATM 3772 O O     . HOH G 4 .   ? 15.121  -4.140  -23.296 1.00 31.60  ? 521 HOH B O     1 
HETATM 3773 O O     . HOH G 4 .   ? 21.576  -25.825 -13.508 1.00 32.30  ? 522 HOH B O     1 
HETATM 3774 O O     . HOH G 4 .   ? 40.862  2.860   -15.671 1.00 36.50  ? 523 HOH B O     1 
HETATM 3775 O O     . HOH G 4 .   ? 27.396  -16.849 -5.304  1.00 23.06  ? 524 HOH B O     1 
HETATM 3776 O O     . HOH G 4 .   ? 25.376  14.604  -23.938 1.00 27.45  ? 525 HOH B O     1 
HETATM 3777 O O     . HOH G 4 .   ? 30.704  -11.296 -29.242 1.00 28.52  ? 526 HOH B O     1 
HETATM 3778 O O     . HOH G 4 .   ? 14.735  -10.123 -11.948 1.00 26.82  ? 527 HOH B O     1 
HETATM 3779 O O     . HOH G 4 .   ? 26.077  1.776   -3.682  1.00 32.51  ? 528 HOH B O     1 
HETATM 3780 O O     . HOH G 4 .   ? 45.477  9.270   -14.191 1.00 47.95  ? 529 HOH B O     1 
HETATM 3781 O O     . HOH G 4 .   ? 49.412  1.363   -12.814 1.00 41.09  ? 530 HOH B O     1 
HETATM 3782 O O     . HOH G 4 .   ? 1.483   -9.035  -20.091 1.00 39.60  ? 531 HOH B O     1 
HETATM 3783 O O     . HOH G 4 .   ? 21.358  18.953  -13.508 1.00 34.50  ? 532 HOH B O     1 
HETATM 3784 O O     . HOH G 4 .   ? 22.838  -19.957 -23.582 1.00 35.52  ? 533 HOH B O     1 
HETATM 3785 O O     . HOH G 4 .   ? 34.440  17.229  -18.715 1.00 28.19  ? 534 HOH B O     1 
HETATM 3786 O O     . HOH G 4 .   ? 23.346  -0.802  11.650  1.00 31.60  ? 535 HOH B O     1 
HETATM 3787 O O     . HOH G 4 .   ? 21.562  -15.586 -27.877 1.00 35.16  ? 536 HOH B O     1 
HETATM 3788 O O     . HOH G 4 .   ? 18.027  -6.990  -28.703 1.00 36.01  ? 537 HOH B O     1 
HETATM 3789 O O     . HOH G 4 .   ? 35.283  -6.990  -30.029 1.00 34.24  ? 538 HOH B O     1 
HETATM 3790 O O     . HOH G 4 .   ? 32.316  6.108   -14.595 1.00 28.09  ? 539 HOH B O     1 
HETATM 3791 O O     . HOH G 4 .   ? 38.661  2.274   -19.837 1.00 34.09  ? 540 HOH B O     1 
HETATM 3792 O O     . HOH G 4 .   ? 19.814  6.015   -8.896  1.00 20.83  ? 541 HOH B O     1 
HETATM 3793 O O     . HOH G 4 .   ? 42.435  -10.088 -15.836 1.00 33.02  ? 542 HOH B O     1 
HETATM 3794 O O     . HOH G 4 .   ? 33.552  -11.320 -29.809 1.00 38.14  ? 543 HOH B O     1 
HETATM 3795 O O     . HOH G 4 .   ? 2.056   -4.568  -32.389 1.00 42.44  ? 544 HOH B O     1 
HETATM 3796 O O     . HOH G 4 .   ? 28.011  4.495   -0.608  1.00 43.75  ? 545 HOH B O     1 
HETATM 3797 O O     . HOH G 4 .   ? 34.021  1.882   -5.883  1.00 17.60  ? 546 HOH B O     1 
HETATM 3798 O O     . HOH G 4 .   ? 31.657  -23.366 -1.841  1.00 38.28  ? 547 HOH B O     1 
HETATM 3799 O O     . HOH G 4 .   ? 29.641  -24.437 -2.859  1.00 40.99  ? 548 HOH B O     1 
HETATM 3800 O O     . HOH G 4 .   ? 33.640  2.552   -8.828  1.00 25.79  ? 549 HOH B O     1 
HETATM 3801 O O     . HOH G 4 .   ? 30.234  -24.964 -5.412  1.00 35.25  ? 550 HOH B O     1 
HETATM 3802 O O     . HOH G 4 .   ? 26.601  -25.392 -17.143 1.00 35.12  ? 551 HOH B O     1 
HETATM 3803 O O     . HOH G 4 .   ? 26.833  -15.444 -30.246 1.00 37.44  ? 552 HOH B O     1 
HETATM 3804 O O     . HOH G 4 .   ? 41.726  -3.462  -15.649 1.00 39.62  ? 553 HOH B O     1 
HETATM 3805 O O     . HOH G 4 .   ? 37.133  -10.163 -1.109  1.00 39.66  ? 554 HOH B O     1 
HETATM 3806 O O     . HOH G 4 .   ? 33.816  -5.591  7.888   1.00 42.01  ? 555 HOH B O     1 
HETATM 3807 O O     . HOH G 4 .   ? 17.954  13.215  -20.268 1.00 33.75  ? 556 HOH B O     1 
HETATM 3808 O O     . HOH G 4 .   ? 15.700  12.467  -19.390 1.00 29.51  ? 557 HOH B O     1 
HETATM 3809 O O     . HOH G 4 .   ? 25.107  8.892   -28.618 1.00 38.70  ? 558 HOH B O     1 
HETATM 3810 O O     . HOH G 4 .   ? 39.474  -2.442  -16.375 1.00 33.83  ? 559 HOH B O     1 
HETATM 3811 O O     . HOH G 4 .   ? 40.483  -11.508 -7.382  1.00 31.74  ? 560 HOH B O     1 
HETATM 3812 O O     . HOH G 4 .   ? 22.808  -8.718  6.530   1.00 39.16  ? 561 HOH B O     1 
HETATM 3813 O O     . HOH G 4 .   ? 24.343  17.032  -24.281 1.00 40.84  ? 562 HOH B O     1 
HETATM 3814 O O     . HOH G 4 .   ? 49.112  -1.300  -9.786  1.00 35.50  ? 563 HOH B O     1 
HETATM 3815 O O     . HOH G 4 .   ? 12.425  -7.590  -31.669 1.00 48.78  ? 564 HOH B O     1 
HETATM 3816 O O     . HOH G 4 .   ? 30.416  -13.961 -29.311 1.00 36.07  ? 565 HOH B O     1 
HETATM 3817 O O     . HOH G 4 .   ? 35.804  21.615  -18.389 1.00 34.53  ? 566 HOH B O     1 
HETATM 3818 O O     . HOH G 4 .   ? 23.107  7.869   -16.393 1.00 23.20  ? 567 HOH B O     1 
HETATM 3819 O O     . HOH G 4 .   ? 36.973  4.100   -13.612 1.00 34.43  ? 568 HOH B O     1 
HETATM 3820 O O     . HOH G 4 .   ? 23.409  -23.863 -7.370  1.00 45.30  ? 569 HOH B O     1 
HETATM 3821 O O     . HOH G 4 .   ? 18.930  -0.797  -2.278  1.00 47.13  ? 570 HOH B O     1 
HETATM 3822 O O     . HOH G 4 .   ? 33.701  7.942   -13.359 1.00 27.13  ? 571 HOH B O     1 
HETATM 3823 O O     . HOH G 4 .   ? 32.197  -3.672  7.677   1.00 47.42  ? 572 HOH B O     1 
HETATM 3824 O O     . HOH G 4 .   ? 34.874  5.401   -12.609 1.00 30.88  ? 573 HOH B O     1 
HETATM 3825 O O     . HOH G 4 .   ? 23.589  -13.890 -27.359 1.00 35.86  ? 574 HOH B O     1 
HETATM 3826 O O     . HOH G 4 .   ? 35.716  0.133   -28.337 1.00 38.43  ? 575 HOH B O     1 
HETATM 3827 O O     . HOH G 4 .   ? 33.337  7.888   -34.694 1.00 35.77  ? 576 HOH B O     1 
HETATM 3828 O O     . HOH G 4 .   ? 31.421  -25.082 -16.679 1.00 39.52  ? 577 HOH B O     1 
HETATM 3829 O O     . HOH G 4 .   ? 31.819  -7.426  8.382   1.00 41.28  ? 578 HOH B O     1 
HETATM 3830 O O     . HOH G 4 .   ? 27.563  23.003  -14.127 1.00 37.61  ? 579 HOH B O     1 
HETATM 3831 O O     . HOH G 4 .   ? 32.233  -15.923 -28.918 1.00 33.23  ? 580 HOH B O     1 
HETATM 3832 O O     . HOH G 4 .   ? 25.330  -8.345  7.675   1.00 39.51  ? 581 HOH B O     1 
HETATM 3833 O O     . HOH G 4 .   ? 34.398  -4.601  -28.991 1.00 37.99  ? 582 HOH B O     1 
HETATM 3834 O O     . HOH G 4 .   ? 26.904  13.491  -25.969 1.00 32.88  ? 583 HOH B O     1 
HETATM 3835 O O     . HOH G 4 .   ? 27.789  -7.261  6.832   1.00 31.56  ? 584 HOH B O     1 
HETATM 3836 O O     . HOH G 4 .   ? 29.111  -28.071 -18.325 1.00 27.11  ? 585 HOH B O     1 
HETATM 3837 O O     . HOH G 4 .   ? 29.445  -6.273  8.522   1.00 39.23  ? 586 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   . SER A 14  ? 0.7340 1.2081 1.1422 -0.2898 -0.0923 -0.1803 2   SER A N   
2    C CA  . SER A 14  ? 0.6627 1.2372 1.2016 -0.2671 -0.0663 -0.1879 2   SER A CA  
3    C C   . SER A 14  ? 0.7039 1.2909 1.3110 -0.1982 -0.0677 -0.1782 2   SER A C   
4    O O   . SER A 14  ? 0.6463 1.1633 1.1900 -0.1676 -0.0944 -0.1568 2   SER A O   
5    C CB  . SER A 14  ? 0.6493 1.3361 1.2778 -0.2801 -0.0915 -0.1747 2   SER A CB  
6    O OG  . SER A 14  ? 0.5975 1.3795 1.3593 -0.2460 -0.0663 -0.1784 2   SER A OG  
7    N N   . ASP A 15  ? 0.6139 1.2647 1.3273 -0.1708 -0.0322 -0.1898 3   ASP A N   
8    C CA  . ASP A 15  ? 0.5171 1.1709 1.2967 -0.1015 -0.0283 -0.1789 3   ASP A CA  
9    C C   . ASP A 15  ? 0.5919 1.1133 1.2596 -0.0806 -0.0099 -0.1738 3   ASP A C   
10   O O   . ASP A 15  ? 0.5354 1.0381 1.2353 -0.0342 0.0095  -0.1708 3   ASP A O   
11   C CB  . ASP A 15  ? 0.5116 1.2173 1.3461 -0.0623 -0.0907 -0.1420 3   ASP A CB  
12   C CG  . ASP A 15  ? 0.6520 1.3782 1.5695 0.0061  -0.0821 -0.1271 3   ASP A CG  
13   O OD1 . ASP A 15  ? 0.6947 1.3857 1.6216 0.0249  -0.0268 -0.1482 3   ASP A OD1 
14   O OD2 . ASP A 15  ? 0.7625 1.5296 1.7210 0.0367  -0.1303 -0.0937 3   ASP A OD2 
15   N N   . GLY A 16  ? 0.4607 0.8905 1.0006 -0.1141 -0.0160 -0.1726 4   GLY A N   
16   C CA  . GLY A 16  ? 0.3677 0.6857 0.8110 -0.1006 -0.0003 -0.1680 4   GLY A CA  
17   C C   . GLY A 16  ? 0.3314 0.6161 0.7601 -0.0505 -0.0268 -0.1428 4   GLY A C   
18   O O   . GLY A 16  ? 0.3230 0.5263 0.6796 -0.0397 -0.0149 -0.1380 4   GLY A O   
19   N N   . ARG A 17  ? 0.3277 0.6726 0.8195 -0.0241 -0.0653 -0.1248 5   ARG A N   
20   C CA  . ARG A 17  ? 0.3199 0.6250 0.7854 0.0162  -0.0923 -0.0999 5   ARG A CA  
21   C C   . ARG A 17  ? 0.3341 0.5704 0.6888 -0.0024 -0.1149 -0.0912 5   ARG A C   
22   O O   . ARG A 17  ? 0.3320 0.5029 0.6269 0.0159  -0.1107 -0.0830 5   ARG A O   
23   C CB  . ARG A 17  ? 0.3764 0.7578 0.9351 0.0460  -0.1339 -0.0793 5   ARG A CB  
24   C CG  . ARG A 17  ? 0.3597 0.6900 0.8822 0.0829  -0.1636 -0.0519 5   ARG A CG  
25   C CD  . ARG A 17  ? 0.4647 0.8632 1.0764 0.1111  -0.2148 -0.0259 5   ARG A CD  
26   N NE  . ARG A 17  ? 0.7001 1.0530 1.2345 0.1081  -0.2673 0.0035  5   ARG A NE  
27   C CZ  . ARG A 17  ? 0.8509 1.2141 1.3351 0.0665  -0.3070 0.0123  5   ARG A CZ  
28   N NH1 . ARG A 17  ? 0.7766 1.1930 1.2787 0.0255  -0.3034 -0.0041 5   ARG A NH1 
29   N NH2 . ARG A 17  ? 0.9175 1.2279 1.3186 0.0590  -0.3471 0.0365  5   ARG A NH2 
30   N N   . GLU A 18  ? 0.3735 0.6236 0.6993 -0.0410 -0.1360 -0.0951 6   GLU A N   
31   C CA  . GLU A 18  ? 0.3830 0.5640 0.6059 -0.0574 -0.1507 -0.0919 6   GLU A CA  
32   C C   . GLU A 18  ? 0.3768 0.4774 0.5322 -0.0572 -0.1158 -0.1044 6   GLU A C   
33   O O   . GLU A 18  ? 0.3811 0.4274 0.4797 -0.0429 -0.1161 -0.0989 6   GLU A O   
34   C CB  . GLU A 18  ? 0.4236 0.6222 0.6186 -0.1050 -0.1732 -0.0977 6   GLU A CB  
35   C CG  . GLU A 18  ? 0.4868 0.7278 0.6930 -0.1118 -0.2242 -0.0764 6   GLU A CG  
36   C CD  . GLU A 18  ? 0.7385 1.0884 1.0689 -0.0975 -0.2490 -0.0626 6   GLU A CD  
37   O OE1 . GLU A 18  ? 0.6275 1.0210 1.0399 -0.0788 -0.2177 -0.0744 6   GLU A OE1 
38   O OE2 . GLU A 18  ? 0.8032 1.1954 1.1504 -0.1065 -0.3005 -0.0400 6   GLU A OE2 
39   N N   . SER A 19  ? 0.3728 0.4681 0.5359 -0.0753 -0.0870 -0.1202 7   SER A N   
40   C CA  . SER A 19  ? 0.3751 0.3956 0.4804 -0.0756 -0.0614 -0.1263 7   SER A CA  
41   C C   . SER A 19  ? 0.3466 0.3471 0.4562 -0.0394 -0.0503 -0.1148 7   SER A C   
42   O O   . SER A 19  ? 0.3600 0.3078 0.4185 -0.0291 -0.0487 -0.1097 7   SER A O   
43   C CB  . SER A 19  ? 0.4438 0.4648 0.5562 -0.1086 -0.0360 -0.1424 7   SER A CB  
44   O OG  . SER A 19  ? 0.4813 0.4326 0.5432 -0.1106 -0.0168 -0.1428 7   SER A OG  
45   N N   . PHE A 20  ? 0.3267 0.3690 0.4993 -0.0205 -0.0406 -0.1117 8   PHE A N   
46   C CA  . PHE A 20  ? 0.3139 0.3285 0.4801 0.0085  -0.0294 -0.1011 8   PHE A CA  
47   C C   . PHE A 20  ? 0.3310 0.3244 0.4586 0.0269  -0.0546 -0.0852 8   PHE A C   
48   O O   . PHE A 20  ? 0.3343 0.2845 0.4173 0.0341  -0.0463 -0.0796 8   PHE A O   
49   C CB  . PHE A 20  ? 0.3090 0.3676 0.5520 0.0303  -0.0172 -0.1016 8   PHE A CB  
50   C CG  . PHE A 20  ? 0.3124 0.3287 0.5383 0.0545  -0.0003 -0.0933 8   PHE A CG  
51   C CD1 . PHE A 20  ? 0.3265 0.2994 0.5196 0.0387  0.0354  -0.1026 8   PHE A CD1 
52   C CD2 . PHE A 20  ? 0.4128 0.4245 0.6431 0.0858  -0.0225 -0.0751 8   PHE A CD2 
53   C CE1 . PHE A 20  ? 0.4114 0.3404 0.5790 0.0529  0.0524  -0.0958 8   PHE A CE1 
54   C CE2 . PHE A 20  ? 0.3996 0.3626 0.6028 0.1025  -0.0058 -0.0681 8   PHE A CE2 
55   C CZ  . PHE A 20  ? 0.5238 0.4467 0.6958 0.0854  0.0332  -0.0794 8   PHE A CZ  
56   N N   . LEU A 21  ? 0.3284 0.3542 0.4701 0.0289  -0.0861 -0.0776 9   LEU A N   
57   C CA  . LEU A 21  ? 0.3890 0.3900 0.4845 0.0384  -0.1078 -0.0637 9   LEU A CA  
58   C C   . LEU A 21  ? 0.3575 0.3154 0.3837 0.0219  -0.1017 -0.0731 9   LEU A C   
59   O O   . LEU A 21  ? 0.3841 0.3121 0.3682 0.0291  -0.0986 -0.0686 9   LEU A O   
60   C CB  . LEU A 21  ? 0.3978 0.4380 0.5171 0.0374  -0.1480 -0.0502 9   LEU A CB  
61   C CG  . LEU A 21  ? 0.3808 0.4618 0.5783 0.0671  -0.1615 -0.0353 9   LEU A CG  
62   C CD1 . LEU A 21  ? 0.4644 0.5962 0.6957 0.0600  -0.2103 -0.0195 9   LEU A CD1 
63   C CD2 . LEU A 21  ? 0.4180 0.4499 0.5852 0.0939  -0.1585 -0.0206 9   LEU A CD2 
64   N N   . GLU A 22  ? 0.3862 0.3387 0.4009 -0.0007 -0.0972 -0.0878 10  GLU A N   
65   C CA  . GLU A 22  ? 0.4105 0.3147 0.3674 -0.0094 -0.0876 -0.0993 10  GLU A CA  
66   C C   . GLU A 22  ? 0.4179 0.2920 0.3681 0.0067  -0.0658 -0.0987 10  GLU A C   
67   O O   . GLU A 22  ? 0.4253 0.2773 0.3474 0.0161  -0.0590 -0.1006 10  GLU A O   
68   C CB  . GLU A 22  ? 0.5050 0.3954 0.4453 -0.0372 -0.0875 -0.1143 10  GLU A CB  
69   C CG  . GLU A 22  ? 0.7321 0.5608 0.6174 -0.0397 -0.0743 -0.1282 10  GLU A CG  
70   C CD  . GLU A 22  ? 1.0635 0.8616 0.9148 -0.0714 -0.0757 -0.1431 10  GLU A CD  
71   O OE1 . GLU A 22  ? 0.9918 0.8291 0.8643 -0.0970 -0.0886 -0.1421 10  GLU A OE1 
72   O OE2 . GLU A 22  ? 1.2205 0.9563 1.0269 -0.0707 -0.0628 -0.1561 10  GLU A OE2 
73   N N   . VAL A 23  ? 0.3896 0.2659 0.3655 0.0061  -0.0542 -0.0965 11  VAL A N   
74   C CA  . VAL A 23  ? 0.3978 0.2465 0.3629 0.0143  -0.0404 -0.0906 11  VAL A CA  
75   C C   . VAL A 23  ? 0.3964 0.2539 0.3595 0.0313  -0.0388 -0.0784 11  VAL A C   
76   O O   . VAL A 23  ? 0.4216 0.2659 0.3669 0.0377  -0.0345 -0.0747 11  VAL A O   
77   C CB  . VAL A 23  ? 0.4068 0.2460 0.3823 -0.0022 -0.0276 -0.0914 11  VAL A CB  
78   C CG1 . VAL A 23  ? 0.4591 0.2702 0.4161 -0.0008 -0.0196 -0.0802 11  VAL A CG1 
79   C CG2 . VAL A 23  ? 0.4513 0.2667 0.4095 -0.0261 -0.0293 -0.1027 11  VAL A CG2 
80   N N   . MET A 24  ? 0.3566 0.2361 0.3386 0.0385  -0.0436 -0.0717 12  MET A N   
81   C CA  A MET A 24  ? 0.3613 0.2337 0.3255 0.0497  -0.0433 -0.0597 12  MET A CA  
82   C CA  B MET A 24  ? 0.3705 0.2430 0.3347 0.0498  -0.0435 -0.0597 12  MET A CA  
83   C C   . MET A 24  ? 0.4138 0.2810 0.3414 0.0481  -0.0496 -0.0615 12  MET A C   
84   O O   . MET A 24  ? 0.4122 0.2711 0.3177 0.0482  -0.0405 -0.0575 12  MET A O   
85   C CB  A MET A 24  ? 0.3965 0.2833 0.3857 0.0618  -0.0542 -0.0511 12  MET A CB  
86   C CB  B MET A 24  ? 0.3969 0.2841 0.3856 0.0619  -0.0552 -0.0508 12  MET A CB  
87   C CG  A MET A 24  ? 0.4354 0.2980 0.3951 0.0710  -0.0554 -0.0373 12  MET A CG  
88   C CG  B MET A 24  ? 0.3525 0.2359 0.3731 0.0700  -0.0363 -0.0498 12  MET A CG  
89   S SD  A MET A 24  ? 0.6296 0.4984 0.6360 0.0951  -0.0654 -0.0268 12  MET A SD  
90   S SD  B MET A 24  ? 0.3560 0.2396 0.4013 0.0975  -0.0513 -0.0350 12  MET A SD  
91   C CE  A MET A 24  ? 0.5714 0.3829 0.5310 0.0991  -0.0452 -0.0173 12  MET A CE  
92   C CE  B MET A 24  ? 0.3828 0.2411 0.3571 0.0913  -0.0771 -0.0210 12  MET A CE  
93   N N   . ARG A 25  ? 0.3888 0.2620 0.3067 0.0409  -0.0627 -0.0696 13  ARG A N   
94   C CA  . ARG A 25  ? 0.3981 0.2605 0.2741 0.0331  -0.0607 -0.0777 13  ARG A CA  
95   C C   . ARG A 25  ? 0.4724 0.3263 0.3504 0.0385  -0.0393 -0.0898 13  ARG A C   
96   O O   . ARG A 25  ? 0.4522 0.3095 0.3146 0.0390  -0.0264 -0.0937 13  ARG A O   
97   C CB  . ARG A 25  ? 0.4875 0.3476 0.3419 0.0159  -0.0762 -0.0864 13  ARG A CB  
98   C CG  . ARG A 25  ? 0.5054 0.3448 0.3057 0.0008  -0.0659 -0.1008 13  ARG A CG  
99   C CD  . ARG A 25  ? 0.6979 0.5212 0.4658 -0.0235 -0.0746 -0.1144 13  ARG A CD  
100  N NE  . ARG A 25  ? 0.9050 0.7257 0.6282 -0.0486 -0.1021 -0.1033 13  ARG A NE  
101  C CZ  . ARG A 25  ? 0.9334 0.7303 0.5986 -0.0829 -0.1093 -0.1145 13  ARG A CZ  
102  N NH1 . ARG A 25  ? 0.9427 0.7116 0.5872 -0.0935 -0.0856 -0.1405 13  ARG A NH1 
103  N NH2 . ARG A 25  ? 1.0693 0.8608 0.6882 -0.1098 -0.1425 -0.0980 13  ARG A NH2 
104  N N   . SER A 26  ? 0.4038 0.2474 0.3029 0.0417  -0.0365 -0.0954 14  SER A N   
105  C CA  . SER A 26  ? 0.4615 0.2918 0.3693 0.0527  -0.0238 -0.1029 14  SER A CA  
106  C C   . SER A 26  ? 0.4178 0.2650 0.3433 0.0604  -0.0195 -0.0885 14  SER A C   
107  O O   . SER A 26  ? 0.4113 0.2710 0.3504 0.0706  -0.0099 -0.0924 14  SER A O   
108  C CB  . SER A 26  ? 0.4712 0.2723 0.3859 0.0503  -0.0284 -0.1060 14  SER A CB  
109  O OG  . SER A 26  ? 0.5472 0.3294 0.4381 0.0376  -0.0306 -0.1214 14  SER A OG  
110  N N   . VAL A 27  ? 0.4194 0.2685 0.3474 0.0535  -0.0247 -0.0731 15  VAL A N   
111  C CA  . VAL A 27  ? 0.3885 0.2465 0.3179 0.0506  -0.0214 -0.0582 15  VAL A CA  
112  C C   . VAL A 27  ? 0.4069 0.2863 0.3199 0.0484  -0.0142 -0.0584 15  VAL A C   
113  O O   . VAL A 27  ? 0.3646 0.2675 0.2892 0.0484  -0.0083 -0.0565 15  VAL A O   
114  C CB  . VAL A 27  ? 0.4041 0.2462 0.3260 0.0387  -0.0208 -0.0469 15  VAL A CB  
115  C CG1 . VAL A 27  ? 0.3961 0.2379 0.3003 0.0270  -0.0160 -0.0322 15  VAL A CG1 
116  C CG2 . VAL A 27  ? 0.4209 0.2411 0.3508 0.0304  -0.0233 -0.0484 15  VAL A CG2 
117  N N   . TYR A 28  ? 0.3900 0.2635 0.2761 0.0437  -0.0168 -0.0602 16  TYR A N   
118  C CA  . TYR A 28  ? 0.4117 0.2933 0.2645 0.0330  -0.0105 -0.0610 16  TYR A CA  
119  C C   . TYR A 28  ? 0.4275 0.3330 0.2906 0.0341  0.0053  -0.0798 16  TYR A C   
120  O O   . TYR A 28  ? 0.4130 0.3457 0.2767 0.0258  0.0189  -0.0814 16  TYR A O   
121  C CB  . TYR A 28  ? 0.4305 0.2911 0.2470 0.0268  -0.0242 -0.0578 16  TYR A CB  
122  C CG  . TYR A 28  ? 0.4312 0.2677 0.2312 0.0273  -0.0339 -0.0389 16  TYR A CG  
123  C CD1 . TYR A 28  ? 0.4645 0.2890 0.2389 0.0168  -0.0239 -0.0287 16  TYR A CD1 
124  C CD2 . TYR A 28  ? 0.4694 0.2939 0.2795 0.0376  -0.0530 -0.0317 16  TYR A CD2 
125  C CE1 . TYR A 28  ? 0.5222 0.3079 0.2723 0.0186  -0.0289 -0.0140 16  TYR A CE1 
126  C CE2 . TYR A 28  ? 0.4617 0.2593 0.2647 0.0460  -0.0600 -0.0161 16  TYR A CE2 
127  C CZ  . TYR A 28  ? 0.4716 0.2419 0.2399 0.0373  -0.0456 -0.0084 16  TYR A CZ  
128  O OH  . TYR A 28  ? 0.5193 0.2464 0.2727 0.0473  -0.0485 0.0051  16  TYR A OH  
129  N N   . GLU A 29  ? 0.3980 0.2942 0.2710 0.0429  0.0073  -0.0965 17  GLU A N   
130  C CA  . GLU A 29  ? 0.4454 0.3558 0.3280 0.0468  0.0305  -0.1202 17  GLU A CA  
131  C C   . GLU A 29  ? 0.3822 0.3258 0.3256 0.0667  0.0389  -0.1188 17  GLU A C   
132  O O   . GLU A 29  ? 0.3953 0.3758 0.3619 0.0689  0.0614  -0.1332 17  GLU A O   
133  C CB  . GLU A 29  ? 0.4690 0.3464 0.3372 0.0486  0.0319  -0.1387 17  GLU A CB  
134  C CG  . GLU A 29  ? 0.6105 0.4658 0.4180 0.0224  0.0201  -0.1392 17  GLU A CG  
135  C CD  . GLU A 29  ? 0.8400 0.6624 0.6247 0.0140  0.0157  -0.1537 17  GLU A CD  
136  O OE1 . GLU A 29  ? 0.8127 0.6200 0.6256 0.0299  0.0198  -0.1613 17  GLU A OE1 
137  O OE2 . GLU A 29  ? 0.8167 0.6226 0.5468 -0.0135 0.0046  -0.1551 17  GLU A OE2 
138  N N   . ARG A 30  ? 0.3564 0.2912 0.3263 0.0772  0.0197  -0.0999 18  ARG A N   
139  C CA  . ARG A 30  ? 0.3715 0.3349 0.3968 0.0931  0.0157  -0.0904 18  ARG A CA  
140  C C   . ARG A 30  ? 0.3337 0.3501 0.3693 0.0781  0.0213  -0.0806 18  ARG A C   
141  O O   . ARG A 30  ? 0.3337 0.3991 0.4276 0.0906  0.0248  -0.0804 18  ARG A O   
142  C CB  . ARG A 30  ? 0.3673 0.2976 0.3943 0.0932  -0.0096 -0.0689 18  ARG A CB  
143  C CG  . ARG A 30  ? 0.3695 0.3196 0.4424 0.1026  -0.0270 -0.0493 18  ARG A CG  
144  C CD  . ARG A 30  ? 0.4161 0.3140 0.4719 0.0951  -0.0522 -0.0304 18  ARG A CD  
145  N NE  . ARG A 30  ? 0.4392 0.2891 0.4957 0.1131  -0.0554 -0.0426 18  ARG A NE  
146  C CZ  . ARG A 30  ? 0.4605 0.2560 0.4930 0.1026  -0.0748 -0.0305 18  ARG A CZ  
147  N NH1 . ARG A 30  ? 0.4745 0.2572 0.4803 0.0734  -0.0897 -0.0083 18  ARG A NH1 
148  N NH2 . ARG A 30  ? 0.5390 0.2835 0.5624 0.1151  -0.0763 -0.0430 18  ARG A NH2 
149  N N   . TYR A 31  ? 0.3305 0.3377 0.3119 0.0510  0.0213  -0.0719 19  TYR A N   
150  C CA  . TYR A 31  ? 0.3318 0.3748 0.3006 0.0263  0.0271  -0.0623 19  TYR A CA  
151  C C   . TYR A 31  ? 0.3609 0.4142 0.2900 0.0073  0.0501  -0.0812 19  TYR A C   
152  O O   . TYR A 31  ? 0.3767 0.4352 0.2629 -0.0230 0.0541  -0.0731 19  TYR A O   
153  C CB  . TYR A 31  ? 0.3275 0.3350 0.2527 0.0057  0.0115  -0.0373 19  TYR A CB  
154  C CG  . TYR A 31  ? 0.3136 0.3131 0.2707 0.0136  -0.0077 -0.0208 19  TYR A CG  
155  C CD1 . TYR A 31  ? 0.3132 0.3522 0.3024 0.0039  -0.0195 -0.0039 19  TYR A CD1 
156  C CD2 . TYR A 31  ? 0.3312 0.2850 0.2853 0.0265  -0.0165 -0.0216 19  TYR A CD2 
157  C CE1 . TYR A 31  ? 0.3166 0.3386 0.3238 0.0054  -0.0438 0.0151  19  TYR A CE1 
158  C CE2 . TYR A 31  ? 0.3128 0.2484 0.2809 0.0251  -0.0343 -0.0066 19  TYR A CE2 
159  C CZ  . TYR A 31  ? 0.3198 0.2840 0.3098 0.0144  -0.0498 0.0130  19  TYR A CZ  
160  O OH  . TYR A 31  ? 0.3381 0.2744 0.3300 0.0076  -0.0734 0.0314  19  TYR A OH  
161  N N   . LEU A 32  ? 0.3126 0.3285 0.2917 0.0356  -0.0072 -0.0416 20  LEU A N   
162  C CA  . LEU A 32  ? 0.3360 0.3579 0.2945 0.0293  -0.0016 -0.0548 20  LEU A CA  
163  C C   . LEU A 32  ? 0.3626 0.4051 0.2972 0.0256  -0.0102 -0.0442 20  LEU A C   
164  O O   . LEU A 32  ? 0.3819 0.4327 0.2971 0.0213  -0.0077 -0.0469 20  LEU A O   
165  C CB  . LEU A 32  ? 0.3290 0.3421 0.2930 0.0359  0.0093  -0.0601 20  LEU A CB  
166  C CG  . LEU A 32  ? 0.3101 0.3051 0.3067 0.0374  0.0196  -0.0721 20  LEU A CG  
167  C CD1 . LEU A 32  ? 0.3210 0.3120 0.3258 0.0433  0.0311  -0.0764 20  LEU A CD1 
168  C CD2 . LEU A 32  ? 0.3884 0.3775 0.3875 0.0240  0.0276  -0.0959 20  LEU A CD2 
169  N N   . VAL A 33  ? 0.3318 0.3843 0.2713 0.0257  -0.0201 -0.0308 21  VAL A N   
170  C CA  . VAL A 33  ? 0.3594 0.4334 0.2897 0.0226  -0.0296 -0.0162 21  VAL A CA  
171  C C   . VAL A 33  ? 0.4134 0.5017 0.3330 0.0045  -0.0380 -0.0218 21  VAL A C   
172  O O   . VAL A 33  ? 0.3946 0.4785 0.3246 -0.0007 -0.0398 -0.0282 21  VAL A O   
173  C CB  . VAL A 33  ? 0.3307 0.4082 0.2806 0.0334  -0.0324 0.0016  21  VAL A CB  
174  C CG1 . VAL A 33  ? 0.3523 0.4526 0.3066 0.0315  -0.0416 0.0195  21  VAL A CG1 
175  C CG2 . VAL A 33  ? 0.3494 0.4125 0.3038 0.0460  -0.0237 0.0042  21  VAL A CG2 
176  N N   . GLY A 34  ? 0.4914 0.5984 0.3893 -0.0077 -0.0442 -0.0181 22  GLY A N   
177  C CA  . GLY A 34  ? 0.5546 0.6781 0.4354 -0.0308 -0.0533 -0.0240 22  GLY A CA  
178  C C   . GLY A 34  ? 0.5705 0.6779 0.4370 -0.0444 -0.0413 -0.0558 22  GLY A C   
179  O O   . GLY A 34  ? 0.5916 0.7026 0.4545 -0.0609 -0.0459 -0.0659 22  GLY A O   
180  N N   . VAL A 35  ? 0.5295 0.6188 0.3929 -0.0382 -0.0248 -0.0722 23  VAL A N   
181  C CA  . VAL A 35  ? 0.5752 0.6457 0.4365 -0.0484 -0.0078 -0.1043 23  VAL A CA  
182  C C   . VAL A 35  ? 0.4771 0.5548 0.3061 -0.0629 0.0031  -0.1193 23  VAL A C   
183  O O   . VAL A 35  ? 0.5629 0.6433 0.3893 -0.0515 0.0058  -0.1084 23  VAL A O   
184  C CB  . VAL A 35  ? 0.4946 0.5374 0.3928 -0.0279 0.0047  -0.1094 23  VAL A CB  
185  C CG1 . VAL A 35  ? 0.5123 0.5350 0.4207 -0.0366 0.0247  -0.1414 23  VAL A CG1 
186  C CG2 . VAL A 35  ? 0.4999 0.5379 0.4252 -0.0176 -0.0057 -0.0937 23  VAL A CG2 
187  N N   . PRO A 36  ? 0.5036 0.5853 0.3057 -0.0902 0.0106  -0.1452 24  PRO A N   
188  C CA  . PRO A 36  ? 0.5663 0.6566 0.3333 -0.1078 0.0238  -0.1615 24  PRO A CA  
189  C C   . PRO A 36  ? 0.5506 0.6160 0.3412 -0.0926 0.0500  -0.1812 24  PRO A C   
190  O O   . PRO A 36  ? 0.5944 0.6344 0.4268 -0.0764 0.0600  -0.1903 24  PRO A O   
191  C CB  . PRO A 36  ? 0.6691 0.7638 0.4126 -0.1397 0.0277  -0.1834 24  PRO A CB  
192  C CG  . PRO A 36  ? 0.5963 0.6746 0.3631 -0.1388 0.0272  -0.1981 24  PRO A CG  
193  C CD  . PRO A 36  ? 0.5401 0.6192 0.3404 -0.1095 0.0083  -0.1621 24  PRO A CD  
194  N N   . GLY A 37  ? 0.5626 0.6369 0.3330 -0.0971 0.0589  -0.1817 25  GLY A N   
195  C CA  . GLY A 37  ? 0.5753 0.6298 0.3712 -0.0857 0.0840  -0.1983 25  GLY A CA  
196  C C   . GLY A 37  ? 0.5031 0.5484 0.3312 -0.0557 0.0836  -0.1817 25  GLY A C   
197  O O   . GLY A 37  ? 0.5844 0.6124 0.4450 -0.0443 0.1036  -0.1951 25  GLY A O   
198  N N   . VAL A 38  ? 0.4735 0.5293 0.3018 -0.0420 0.0601  -0.1477 26  VAL A N   
199  C CA  . VAL A 38  ? 0.4055 0.4515 0.2657 -0.0153 0.0563  -0.1269 26  VAL A CA  
200  C C   . VAL A 38  ? 0.5012 0.5589 0.3448 -0.0132 0.0584  -0.1159 26  VAL A C   
201  O O   . VAL A 38  ? 0.4917 0.5706 0.3023 -0.0254 0.0478  -0.1035 26  VAL A O   
202  C CB  . VAL A 38  ? 0.4367 0.4855 0.3070 -0.0037 0.0346  -0.1007 26  VAL A CB  
203  C CG1 . VAL A 38  ? 0.3957 0.4376 0.2883 0.0181  0.0305  -0.0799 26  VAL A CG1 
204  C CG2 . VAL A 38  ? 0.4532 0.4890 0.3443 -0.0052 0.0340  -0.1112 26  VAL A CG2 
205  N N   . SER A 39  ? 0.3944 0.4401 0.2646 0.0012  0.0706  -0.1175 27  SER A N   
206  C CA  . SER A 39  ? 0.4357 0.4905 0.2967 0.0056  0.0720  -0.1047 27  SER A CA  
207  C C   . SER A 39  ? 0.3461 0.3961 0.2267 0.0254  0.0572  -0.0776 27  SER A C   
208  O O   . SER A 39  ? 0.3536 0.3923 0.2575 0.0357  0.0501  -0.0718 27  SER A O   
209  C CB  . SER A 39  ? 0.4035 0.4504 0.2829 0.0061  0.0968  -0.1249 27  SER A CB  
210  O OG  . SER A 39  ? 0.5267 0.5793 0.3817 -0.0162 0.1148  -0.1534 27  SER A OG  
211  N N   . GLU A 40  ? 0.3715 0.4301 0.2421 0.0287  0.0539  -0.0618 28  GLU A N   
212  C CA  . GLU A 40  ? 0.3155 0.3675 0.2037 0.0445  0.0442  -0.0412 28  GLU A CA  
213  C C   . GLU A 40  ? 0.2928 0.3414 0.1948 0.0509  0.0534  -0.0393 28  GLU A C   
214  O O   . GLU A 40  ? 0.3465 0.4040 0.2356 0.0433  0.0640  -0.0454 28  GLU A O   
215  C CB  . GLU A 40  ? 0.3294 0.3922 0.2030 0.0445  0.0292  -0.0195 28  GLU A CB  
216  C CG  . GLU A 40  ? 0.3900 0.4559 0.2628 0.0424  0.0176  -0.0155 28  GLU A CG  
217  C CD  . GLU A 40  ? 0.4086 0.4875 0.2775 0.0423  0.0046  0.0072  28  GLU A CD  
218  O OE1 . GLU A 40  ? 0.3709 0.4514 0.2427 0.0470  0.0039  0.0213  28  GLU A OE1 
219  O OE2 . GLU A 40  ? 0.4925 0.5804 0.3610 0.0374  -0.0051 0.0125  28  GLU A OE2 
220  N N   . VAL A 41  ? 0.3046 0.3422 0.2312 0.0626  0.0485  -0.0294 29  VAL A N   
221  C CA  . VAL A 41  ? 0.3018 0.3373 0.2445 0.0683  0.0525  -0.0224 29  VAL A CA  
222  C C   . VAL A 41  ? 0.2571 0.2903 0.1938 0.0727  0.0401  -0.0042 29  VAL A C   
223  O O   . VAL A 41  ? 0.2949 0.3212 0.2366 0.0755  0.0316  0.0011  29  VAL A O   
224  C CB  . VAL A 41  ? 0.2933 0.3198 0.2746 0.0739  0.0573  -0.0261 29  VAL A CB  
225  C CG1 . VAL A 41  ? 0.3139 0.3421 0.3142 0.0779  0.0591  -0.0157 29  VAL A CG1 
226  C CG2 . VAL A 41  ? 0.3092 0.3344 0.3032 0.0698  0.0737  -0.0479 29  VAL A CG2 
227  N N   . TRP A 42  ? 0.2857 0.3245 0.2118 0.0715  0.0410  0.0044  30  TRP A N   
228  C CA  . TRP A 42  ? 0.2781 0.3117 0.2034 0.0747  0.0333  0.0187  30  TRP A CA  
229  C C   . TRP A 42  ? 0.2693 0.2980 0.2105 0.0762  0.0350  0.0226  30  TRP A C   
230  O O   . TRP A 42  ? 0.2850 0.3194 0.2280 0.0748  0.0411  0.0244  30  TRP A O   
231  C CB  . TRP A 42  ? 0.2910 0.3327 0.2017 0.0719  0.0316  0.0290  30  TRP A CB  
232  C CG  . TRP A 42  ? 0.3293 0.3783 0.2299 0.0693  0.0248  0.0322  30  TRP A CG  
233  C CD1 . TRP A 42  ? 0.3056 0.3573 0.2018 0.0665  0.0232  0.0220  30  TRP A CD1 
234  C CD2 . TRP A 42  ? 0.3127 0.3675 0.2137 0.0691  0.0179  0.0487  30  TRP A CD2 
235  N NE1 . TRP A 42  ? 0.3276 0.3888 0.2182 0.0634  0.0146  0.0318  30  TRP A NE1 
236  C CE2 . TRP A 42  ? 0.3238 0.3880 0.2202 0.0654  0.0111  0.0493  30  TRP A CE2 
237  C CE3 . TRP A 42  ? 0.3123 0.3659 0.2224 0.0710  0.0169  0.0644  30  TRP A CE3 
238  C CZ2 . TRP A 42  ? 0.3403 0.4146 0.2445 0.0644  0.0022  0.0677  30  TRP A CZ2 
239  C CZ3 . TRP A 42  ? 0.3559 0.4169 0.2765 0.0710  0.0096  0.0815  30  TRP A CZ3 
240  C CH2 . TRP A 42  ? 0.3460 0.4190 0.2645 0.0677  0.0018  0.0844  30  TRP A CH2 
241  N N   . LEU A 43  ? 0.2621 0.2830 0.2145 0.0768  0.0289  0.0250  31  LEU A N   
242  C CA  . LEU A 43  ? 0.2548 0.2739 0.2223 0.0744  0.0262  0.0322  31  LEU A CA  
243  C C   . LEU A 43  ? 0.2575 0.2713 0.2122 0.0707  0.0240  0.0387  31  LEU A C   
244  O O   . LEU A 43  ? 0.2786 0.2850 0.2217 0.0690  0.0218  0.0383  31  LEU A O   
245  C CB  . LEU A 43  ? 0.2596 0.2752 0.2390 0.0716  0.0178  0.0355  31  LEU A CB  
246  C CG  . LEU A 43  ? 0.2585 0.2756 0.2573 0.0752  0.0196  0.0298  31  LEU A CG  
247  C CD1 . LEU A 43  ? 0.2654 0.2798 0.2736 0.0701  0.0083  0.0387  31  LEU A CD1 
248  C CD2 . LEU A 43  ? 0.2625 0.2853 0.2926 0.0781  0.0271  0.0295  31  LEU A CD2 
249  N N   . ILE A 44  ? 0.2527 0.2694 0.2128 0.0687  0.0266  0.0438  32  ILE A N   
250  C CA  . ILE A 44  ? 0.2550 0.2649 0.2065 0.0645  0.0267  0.0487  32  ILE A CA  
251  C C   . ILE A 44  ? 0.2574 0.2668 0.2176 0.0557  0.0219  0.0543  32  ILE A C   
252  O O   . ILE A 44  ? 0.2641 0.2834 0.2425 0.0558  0.0217  0.0589  32  ILE A O   
253  C CB  . ILE A 44  ? 0.2657 0.2816 0.2146 0.0673  0.0332  0.0523  32  ILE A CB  
254  C CG1 . ILE A 44  ? 0.2886 0.3092 0.2269 0.0716  0.0344  0.0500  32  ILE A CG1 
255  C CG2 . ILE A 44  ? 0.2929 0.3005 0.2410 0.0633  0.0342  0.0592  32  ILE A CG2 
256  C CD1 . ILE A 44  ? 0.3123 0.3442 0.2437 0.0703  0.0385  0.0557  32  ILE A CD1 
257  N N   . ARG A 45  ? 0.2488 0.2482 0.1982 0.0460  0.0186  0.0537  33  ARG A N   
258  C CA  . ARG A 45  ? 0.2450 0.2460 0.1983 0.0330  0.0129  0.0599  33  ARG A CA  
259  C C   . ARG A 45  ? 0.2593 0.2575 0.2152 0.0329  0.0189  0.0624  33  ARG A C   
260  O O   . ARG A 45  ? 0.2742 0.2624 0.2236 0.0371  0.0265  0.0588  33  ARG A O   
261  C CB  . ARG A 45  ? 0.2635 0.2552 0.1983 0.0169  0.0091  0.0555  33  ARG A CB  
262  C CG  . ARG A 45  ? 0.2777 0.2740 0.2122 -0.0020 0.0005  0.0629  33  ARG A CG  
263  C CD  . ARG A 45  ? 0.2984 0.2881 0.2076 -0.0246 -0.0027 0.0567  33  ARG A CD  
264  N NE  . ARG A 45  ? 0.3017 0.2986 0.2084 -0.0461 -0.0128 0.0650  33  ARG A NE  
265  C CZ  . ARG A 45  ? 0.3304 0.3210 0.2101 -0.0726 -0.0136 0.0573  33  ARG A CZ  
266  N NH1 . ARG A 45  ? 0.3675 0.3428 0.2220 -0.0803 -0.0015 0.0387  33  ARG A NH1 
267  N NH2 . ARG A 45  ? 0.3457 0.3465 0.2245 -0.0938 -0.0255 0.0674  33  ARG A NH2 
268  N N   . HIS A 46  ? 0.1949 0.3184 0.3317 -0.0214 0.0383  0.0619  34  HIS A N   
269  C CA  . HIS A 46  ? 0.1836 0.3031 0.2972 0.0012  0.0472  0.0550  34  HIS A CA  
270  C C   . HIS A 46  ? 0.1809 0.3123 0.2798 0.0126  0.0629  0.0641  34  HIS A C   
271  O O   . HIS A 46  ? 0.1864 0.3310 0.2839 0.0089  0.0682  0.0744  34  HIS A O   
272  C CB  . HIS A 46  ? 0.2072 0.2921 0.3090 0.0042  0.0449  0.0526  34  HIS A CB  
273  C CG  . HIS A 46  ? 0.1966 0.2640 0.2916 -0.0044 0.0487  0.0620  34  HIS A CG  
274  N ND1 . HIS A 46  ? 0.2541 0.3199 0.3353 0.0030  0.0574  0.0647  34  HIS A ND1 
275  C CD2 . HIS A 46  ? 0.2185 0.2697 0.3170 -0.0156 0.0430  0.0681  34  HIS A CD2 
276  C CE1 . HIS A 46  ? 0.2500 0.3086 0.3245 -0.0012 0.0566  0.0699  34  HIS A CE1 
277  N NE2 . HIS A 46  ? 0.2578 0.3089 0.3428 -0.0125 0.0504  0.0758  34  HIS A NE2 
278  N N   . ALA A 47  ? 0.1846 0.3084 0.2712 0.0308  0.0696  0.0614  35  ALA A N   
279  C CA  . ALA A 47  ? 0.2217 0.3401 0.2922 0.0464  0.0798  0.0650  35  ALA A CA  
280  C C   . ALA A 47  ? 0.2413 0.3208 0.3017 0.0433  0.0769  0.0620  35  ALA A C   
281  O O   . ALA A 47  ? 0.2322 0.2960 0.2986 0.0300  0.0701  0.0607  35  ALA A O   
282  C CB  . ALA A 47  ? 0.2279 0.3501 0.2955 0.0667  0.0874  0.0684  35  ALA A CB  
283  N N   . ASP A 48  ? 0.2571 0.3209 0.3008 0.0591  0.0791  0.0578  36  ASP A N   
284  C CA  . ASP A 48  ? 0.2801 0.3117 0.3128 0.0595  0.0700  0.0469  36  ASP A CA  
285  C C   . ASP A 48  ? 0.2734 0.2723 0.3250 0.0451  0.0622  0.0465  36  ASP A C   
286  O O   . ASP A 48  ? 0.2780 0.2648 0.3450 0.0462  0.0660  0.0559  36  ASP A O   
287  C CB  . ASP A 48  ? 0.3173 0.3283 0.3268 0.0850  0.0678  0.0353  36  ASP A CB  
288  C CG  . ASP A 48  ? 0.4573 0.4352 0.4549 0.0881  0.0510  0.0153  36  ASP A CG  
289  O OD1 . ASP A 48  ? 0.4169 0.4201 0.4008 0.0907  0.0487  0.0119  36  ASP A OD1 
290  O OD2 . ASP A 48  ? 0.3876 0.3166 0.3938 0.0866  0.0387  0.0047  36  ASP A OD2 
291  N N   . SER A 49  ? 0.2784 0.2713 0.3311 0.0339  0.0525  0.0401  37  SER A N   
292  C CA  A SER A 49  ? 0.3028 0.2738 0.3765 0.0204  0.0424  0.0393  37  SER A CA  
293  C CA  B SER A 49  ? 0.3032 0.2744 0.3769 0.0203  0.0423  0.0393  37  SER A CA  
294  C C   . SER A 49  ? 0.4314 0.3862 0.4951 0.0215  0.0253  0.0189  37  SER A C   
295  O O   . SER A 49  ? 0.4375 0.3858 0.5213 0.0073  0.0135  0.0165  37  SER A O   
296  C CB  A SER A 49  ? 0.3953 0.3883 0.4818 0.0088  0.0451  0.0510  37  SER A CB  
297  C CB  B SER A 49  ? 0.3947 0.3874 0.4820 0.0084  0.0448  0.0510  37  SER A CB  
298  O OG  A SER A 49  ? 0.3142 0.3208 0.3837 0.0092  0.0444  0.0473  37  SER A OG  
299  O OG  B SER A 49  ? 0.4123 0.4186 0.5137 0.0110  0.0542  0.0662  37  SER A OG  
300  N N   . TYR A 50  ? 0.3566 0.3149 0.3893 0.0416  0.0229  0.0045  38  TYR A N   
301  C CA  . TYR A 50  ? 0.4412 0.3958 0.4551 0.0529  0.0054  -0.0188 38  TYR A CA  
302  C C   . TYR A 50  ? 0.4455 0.3561 0.4521 0.0671  -0.0149 -0.0466 38  TYR A C   
303  O O   . TYR A 50  ? 0.4876 0.3850 0.4896 0.0714  -0.0389 -0.0733 38  TYR A O   
304  C CB  . TYR A 50  ? 0.5058 0.5031 0.4870 0.0747  0.0158  -0.0138 38  TYR A CB  
305  C CG  . TYR A 50  ? 0.6112 0.6398 0.6054 0.0586  0.0337  0.0155  38  TYR A CG  
306  C CD1 . TYR A 50  ? 0.5258 0.5670 0.5309 0.0527  0.0483  0.0326  38  TYR A CD1 
307  C CD2 . TYR A 50  ? 0.5103 0.5527 0.5069 0.0509  0.0324  0.0236  38  TYR A CD2 
308  C CE1 . TYR A 50  ? 0.5323 0.5927 0.5537 0.0365  0.0568  0.0528  38  TYR A CE1 
309  C CE2 . TYR A 50  ? 0.6108 0.6672 0.6202 0.0374  0.0440  0.0476  38  TYR A CE2 
310  C CZ  . TYR A 50  ? 0.6202 0.6825 0.6438 0.0286  0.0540  0.0603  38  TYR A CZ  
311  O OH  . TYR A 50  ? 0.3989 0.4662 0.4394 0.0136  0.0580  0.0783  38  TYR A OH  
312  N N   . THR A 51  ? 0.4222 0.3082 0.4261 0.0778  -0.0086 -0.0438 39  THR A N   
313  C CA  . THR A 51  ? 0.4915 0.3192 0.4907 0.0919  -0.0310 -0.0705 39  THR A CA  
314  C C   . THR A 51  ? 0.5775 0.3638 0.6280 0.0577  -0.0498 -0.0704 39  THR A C   
315  O O   . THR A 51  ? 0.5440 0.3365 0.6337 0.0322  -0.0350 -0.0378 39  THR A O   
316  C CB  . THR A 51  ? 0.5958 0.4051 0.5832 0.1120  -0.0175 -0.0607 39  THR A CB  
317  O OG1 . THR A 51  ? 0.5288 0.3921 0.4763 0.1413  0.0000  -0.0565 39  THR A OG1 
318  C CG2 . THR A 51  ? 0.6111 0.3465 0.5903 0.1312  -0.0438 -0.0906 39  THR A CG2 
319  N N   . GLY A 52  ? 0.5911 0.3449 0.6435 0.0588  -0.0836 -0.1061 40  GLY A N   
320  C CA  . GLY A 52  ? 0.5920 0.3166 0.7030 0.0214  -0.1062 -0.1061 40  GLY A CA  
321  C C   . GLY A 52  ? 0.5280 0.3071 0.6621 -0.0033 -0.1038 -0.0934 40  GLY A C   
322  O O   . GLY A 52  ? 0.5535 0.3257 0.7436 -0.0367 -0.1192 -0.0854 40  GLY A O   
323  N N   . LEU A 53  ? 0.4927 0.3274 0.5891 0.0125  -0.0853 -0.0881 41  LEU A N   
324  C CA  . LEU A 53  ? 0.4837 0.3659 0.5968 -0.0051 -0.0820 -0.0746 41  LEU A CA  
325  C C   . LEU A 53  ? 0.6253 0.5093 0.7523 -0.0112 -0.1173 -0.1068 41  LEU A C   
326  O O   . LEU A 53  ? 0.5077 0.4245 0.6681 -0.0334 -0.1205 -0.0937 41  LEU A O   
327  C CB  . LEU A 53  ? 0.5136 0.4425 0.5855 0.0141  -0.0571 -0.0608 41  LEU A CB  
328  C CG  . LEU A 53  ? 0.5921 0.5615 0.6766 0.0005  -0.0442 -0.0361 41  LEU A CG  
329  C CD1 . LEU A 53  ? 0.4450 0.4150 0.5724 -0.0236 -0.0339 -0.0078 41  LEU A CD1 
330  C CD2 . LEU A 53  ? 0.5611 0.5567 0.6113 0.0170  -0.0213 -0.0200 41  LEU A CD2 
331  N N   . GLU A 54  ? 0.6304 0.4839 0.7319 0.0117  -0.1463 -0.1509 42  GLU A N   
332  C CA  . GLU A 54  ? 0.6955 0.5521 0.8096 0.0091  -0.1870 -0.1902 42  GLU A CA  
333  C C   . GLU A 54  ? 0.7922 0.6231 0.9865 -0.0391 -0.2105 -0.1842 42  GLU A C   
334  O O   . GLU A 54  ? 0.7573 0.6189 0.9816 -0.0556 -0.2356 -0.1983 42  GLU A O   
335  C CB  . GLU A 54  ? 0.7996 0.6222 0.8673 0.0499  -0.2182 -0.2447 42  GLU A CB  
336  C CG  . GLU A 54  ? 0.8849 0.7515 0.8767 0.1022  -0.1962 -0.2468 42  GLU A CG  
337  C CD  . GLU A 54  ? 0.8893 0.7307 0.8538 0.1219  -0.1715 -0.2313 42  GLU A CD  
338  O OE1 . GLU A 54  ? 0.6588 0.4725 0.6595 0.0917  -0.1519 -0.1983 42  GLU A OE1 
339  O OE2 . GLU A 54  ? 1.0127 0.8719 0.9184 0.1722  -0.1714 -0.2508 42  GLU A OE2 
340  N N   . ASP A 55  ? 0.7873 0.5683 1.0209 -0.0612 -0.2032 -0.1601 43  ASP A N   
341  C CA  . ASP A 55  ? 0.7756 0.5339 1.0960 -0.1091 -0.2227 -0.1426 43  ASP A CA  
342  C C   . ASP A 55  ? 0.6816 0.4817 1.0444 -0.1346 -0.1841 -0.0769 43  ASP A C   
343  O O   . ASP A 55  ? 0.6877 0.4905 1.1076 -0.1637 -0.1827 -0.0442 43  ASP A O   
344  C CB  . ASP A 55  ? 0.8440 0.5274 1.1698 -0.1065 -0.2371 -0.1533 43  ASP A CB  
345  C CG  . ASP A 55  ? 1.0171 0.6691 1.3018 -0.0768 -0.2765 -0.2160 43  ASP A CG  
346  O OD1 . ASP A 55  ? 1.1136 0.8065 1.3902 -0.0718 -0.2989 -0.2463 43  ASP A OD1 
347  O OD2 . ASP A 55  ? 1.1240 0.7168 1.3818 -0.0539 -0.2843 -0.2338 43  ASP A OD2 
348  N N   . TYR A 56  ? 0.6147 0.4611 0.9315 -0.1128 -0.1454 -0.0537 44  TYR A N   
349  C CA  . TYR A 56  ? 0.5851 0.4735 0.9290 -0.1248 -0.1111 0.0010  44  TYR A CA  
350  C C   . TYR A 56  ? 0.5492 0.4937 0.9533 -0.1542 -0.1192 0.0242  44  TYR A C   
351  O O   . TYR A 56  ? 0.4627 0.4464 0.8546 -0.1509 -0.1325 0.0040  44  TYR A O   
352  C CB  . TYR A 56  ? 0.5200 0.4445 0.8020 -0.0950 -0.0799 0.0078  44  TYR A CB  
353  C CG  . TYR A 56  ? 0.5476 0.5071 0.8419 -0.0951 -0.0478 0.0532  44  TYR A CG  
354  C CD1 . TYR A 56  ? 0.6733 0.6107 0.9868 -0.0961 -0.0328 0.0796  44  TYR A CD1 
355  C CD2 . TYR A 56  ? 0.4196 0.4343 0.7007 -0.0869 -0.0335 0.0679  44  TYR A CD2 
356  C CE1 . TYR A 56  ? 0.6638 0.6422 0.9824 -0.0873 -0.0050 0.1178  44  TYR A CE1 
357  C CE2 . TYR A 56  ? 0.3979 0.4457 0.6824 -0.0779 -0.0082 0.1023  44  TYR A CE2 
358  C CZ  . TYR A 56  ? 0.5740 0.6077 0.8770 -0.0772 0.0057  0.1263  44  TYR A CZ  
359  O OH  . TYR A 56  ? 0.4495 0.5237 0.7513 -0.0605 0.0288  0.1573  44  TYR A OH  
360  N N   . ASP A 57  ? 0.4707 0.4299 0.9263 -0.1732 -0.1057 0.0697  45  ASP A N   
361  C CA  . ASP A 57  ? 0.4270 0.4490 0.9252 -0.1909 -0.1062 0.0972  45  ASP A CA  
362  C C   . ASP A 57  ? 0.4270 0.5224 0.9146 -0.1741 -0.0728 0.1378  45  ASP A C   
363  O O   . ASP A 57  ? 0.6152 0.7601 1.1341 -0.1795 -0.0642 0.1734  45  ASP A O   
364  C CB  . ASP A 57  ? 0.5597 0.5591 1.1081 -0.2121 -0.1128 0.1202  45  ASP A CB  
365  C CG  . ASP A 57  ? 0.8387 0.7816 1.4070 -0.2317 -0.1545 0.0771  45  ASP A CG  
366  O OD1 . ASP A 57  ? 0.8229 0.7700 1.3733 -0.2300 -0.1803 0.0324  45  ASP A OD1 
367  O OD2 . ASP A 57  ? 0.9566 0.8530 1.5574 -0.2454 -0.1631 0.0869  45  ASP A OD2 
368  N N   . GLY A 58  ? 0.4535 0.5577 0.8968 -0.1510 -0.0561 0.1319  46  GLY A N   
369  C CA  . GLY A 58  ? 0.3694 0.5373 0.7912 -0.1275 -0.0301 0.1589  46  GLY A CA  
370  C C   . GLY A 58  ? 0.3078 0.4881 0.6728 -0.1058 -0.0336 0.1283  46  GLY A C   
371  O O   . GLY A 58  ? 0.3408 0.5061 0.6980 -0.1125 -0.0568 0.0948  46  GLY A O   
372  N N   . ASP A 59  ? 0.2412 0.4453 0.5636 -0.0762 -0.0130 0.1376  47  ASP A N   
373  C CA  . ASP A 59  ? 0.2323 0.4377 0.5024 -0.0553 -0.0160 0.1134  47  ASP A CA  
374  C C   . ASP A 59  ? 0.2445 0.3898 0.4729 -0.0506 -0.0187 0.0828  47  ASP A C   
375  O O   . ASP A 59  ? 0.2269 0.3463 0.4348 -0.0412 -0.0042 0.0860  47  ASP A O   
376  C CB  . ASP A 59  ? 0.2378 0.4686 0.4763 -0.0245 0.0033  0.1300  47  ASP A CB  
377  C CG  . ASP A 59  ? 0.2306 0.4568 0.4192 -0.0012 0.0012  0.1128  47  ASP A CG  
378  O OD1 . ASP A 59  ? 0.2076 0.4024 0.3736 -0.0043 -0.0071 0.0901  47  ASP A OD1 
379  O OD2 . ASP A 59  ? 0.2239 0.4815 0.3966 0.0242  0.0080  0.1252  47  ASP A OD2 
380  N N   . PRO A 60  ? 0.2469 0.3781 0.4605 -0.0521 -0.0365 0.0540  48  PRO A N   
381  C CA  . PRO A 60  ? 0.3040 0.3897 0.4803 -0.0425 -0.0363 0.0312  48  PRO A CA  
382  C C   . PRO A 60  ? 0.3174 0.3975 0.4481 -0.0213 -0.0177 0.0363  48  PRO A C   
383  O O   . PRO A 60  ? 0.3477 0.4019 0.4544 -0.0140 -0.0120 0.0281  48  PRO A O   
384  C CB  . PRO A 60  ? 0.3506 0.4381 0.5205 -0.0409 -0.0617 -0.0003 48  PRO A CB  
385  C CG  . PRO A 60  ? 0.2814 0.4179 0.4581 -0.0382 -0.0662 0.0067  48  PRO A CG  
386  C CD  . PRO A 60  ? 0.3021 0.4671 0.5250 -0.0547 -0.0568 0.0400  48  PRO A CD  
387  N N   . ARG A 61  ? 0.2272 0.3308 0.3471 -0.0101 -0.0098 0.0504  49  ARG A N   
388  C CA  . ARG A 61  ? 0.2466 0.3339 0.3337 0.0052  0.0033  0.0566  49  ARG A CA  
389  C C   . ARG A 61  ? 0.3235 0.4045 0.4163 0.0076  0.0141  0.0686  49  ARG A C   
390  O O   . ARG A 61  ? 0.3735 0.4381 0.4458 0.0183  0.0192  0.0705  49  ARG A O   
391  C CB  . ARG A 61  ? 0.2318 0.3351 0.2983 0.0219  0.0023  0.0617  49  ARG A CB  
392  C CG  . ARG A 61  ? 0.2483 0.3657 0.3000 0.0289  -0.0067 0.0506  49  ARG A CG  
393  C CD  . ARG A 61  ? 0.2623 0.3897 0.2874 0.0510  -0.0028 0.0620  49  ARG A CD  
394  N NE  . ARG A 61  ? 0.2642 0.4152 0.2987 0.0580  -0.0045 0.0707  49  ARG A NE  
395  C CZ  . ARG A 61  ? 0.2961 0.4304 0.3157 0.0738  0.0025  0.0825  49  ARG A CZ  
396  N NH1 . ARG A 61  ? 0.3179 0.4065 0.3172 0.0798  0.0090  0.0882  49  ARG A NH1 
397  N NH2 . ARG A 61  ? 0.2699 0.4367 0.2967 0.0861  0.0007  0.0893  49  ARG A NH2 
398  N N   . ASP A 62  ? 0.2681 0.3617 0.3898 -0.0009 0.0160  0.0772  50  ASP A N   
399  C CA  . ASP A 62  ? 0.2710 0.3655 0.3938 0.0078  0.0267  0.0870  50  ASP A CA  
400  C C   . ASP A 62  ? 0.2504 0.3452 0.4032 -0.0042 0.0309  0.0970  50  ASP A C   
401  O O   . ASP A 62  ? 0.2663 0.3922 0.4441 -0.0003 0.0379  0.1194  50  ASP A O   
402  C CB  . ASP A 62  ? 0.3053 0.4341 0.4255 0.0283  0.0288  0.0994  50  ASP A CB  
403  C CG  . ASP A 62  ? 0.3160 0.4472 0.4235 0.0485  0.0351  0.1006  50  ASP A CG  
404  O OD1 . ASP A 62  ? 0.2941 0.3981 0.3933 0.0443  0.0367  0.0902  50  ASP A OD1 
405  O OD2 . ASP A 62  ? 0.3529 0.5205 0.4572 0.0730  0.0370  0.1107  50  ASP A OD2 
406  N N   . PRO A 63  ? 0.2898 0.3520 0.4395 -0.0140 0.0283  0.0842  51  PRO A N   
407  C CA  . PRO A 63  ? 0.3186 0.3681 0.4953 -0.0232 0.0304  0.0931  51  PRO A CA  
408  C C   . PRO A 63  ? 0.2932 0.3474 0.4642 -0.0090 0.0459  0.1055  51  PRO A C   
409  O O   . PRO A 63  ? 0.2869 0.3433 0.4301 0.0040  0.0505  0.0963  51  PRO A O   
410  C CB  . PRO A 63  ? 0.3612 0.3725 0.5228 -0.0278 0.0193  0.0680  51  PRO A CB  
411  C CG  . PRO A 63  ? 0.3371 0.3507 0.4588 -0.0153 0.0229  0.0555  51  PRO A CG  
412  C CD  . PRO A 63  ? 0.2959 0.3351 0.4162 -0.0124 0.0235  0.0640  51  PRO A CD  
413  N N   . ALA A 64  ? 0.2912 0.3458 0.4924 -0.0124 0.0520  0.1267  52  ALA A N   
414  C CA  . ALA A 64  ? 0.2740 0.3310 0.4683 0.0042  0.0664  0.1376  52  ALA A CA  
415  C C   . ALA A 64  ? 0.2866 0.3049 0.4551 0.0062  0.0636  0.1145  52  ALA A C   
416  O O   . ALA A 64  ? 0.3238 0.3128 0.4838 -0.0035 0.0508  0.0937  52  ALA A O   
417  C CB  . ALA A 64  ? 0.3207 0.3842 0.5578 0.0005  0.0750  0.1736  52  ALA A CB  
418  N N   . LEU A 65  ? 0.3040 0.3312 0.4588 0.0242  0.0753  0.1187  53  LEU A N   
419  C CA  . LEU A 65  ? 0.2771 0.2779 0.4106 0.0310  0.0750  0.1030  53  LEU A CA  
420  C C   . LEU A 65  ? 0.2925 0.2455 0.4421 0.0250  0.0679  0.1048  53  LEU A C   
421  O O   . LEU A 65  ? 0.3253 0.2696 0.5111 0.0163  0.0692  0.1289  53  LEU A O   
422  C CB  . LEU A 65  ? 0.2752 0.3028 0.3973 0.0534  0.0889  0.1116  53  LEU A CB  
423  C CG  . LEU A 65  ? 0.2480 0.3145 0.3545 0.0592  0.0879  0.0998  53  LEU A CG  
424  C CD1 . LEU A 65  ? 0.2515 0.3495 0.3485 0.0814  0.0966  0.1021  53  LEU A CD1 
425  C CD2 . LEU A 65  ? 0.2831 0.3414 0.3758 0.0454  0.0780  0.0795  53  LEU A CD2 
426  N N   . SER A 66  ? 0.3463 0.2689 0.4708 0.0316  0.0588  0.0801  54  SER A N   
427  C CA  . SER A 66  ? 0.3677 0.2344 0.4982 0.0347  0.0474  0.0727  54  SER A CA  
428  C C   . SER A 66  ? 0.4401 0.2980 0.5655 0.0572  0.0625  0.0902  54  SER A C   
429  O O   . SER A 66  ? 0.3643 0.2686 0.4798 0.0707  0.0807  0.1045  54  SER A O   
430  C CB  . SER A 66  ? 0.4030 0.2500 0.4965 0.0475  0.0320  0.0367  54  SER A CB  
431  O OG  . SER A 66  ? 0.3645 0.2457 0.4213 0.0716  0.0462  0.0337  54  SER A OG  
432  N N   . GLU A 67  ? 0.3471 0.2498 0.4528 -0.0580 0.0104  0.0850  55  GLU A N   
433  C CA  . GLU A 67  ? 0.3556 0.2385 0.4488 -0.0501 0.0156  0.0898  55  GLU A CA  
434  C C   . GLU A 67  ? 0.3459 0.2270 0.4158 -0.0328 0.0193  0.0795  55  GLU A C   
435  O O   . GLU A 67  ? 0.3596 0.2469 0.4224 -0.0228 0.0282  0.0857  55  GLU A O   
436  C CB  . GLU A 67  ? 0.3927 0.2377 0.4852 -0.0585 0.0057  0.0896  55  GLU A CB  
437  C CG  . GLU A 67  ? 0.4498 0.2697 0.5267 -0.0482 0.0104  0.0937  55  GLU A CG  
438  C CD  . GLU A 67  ? 0.7743 0.5536 0.8520 -0.0574 0.0007  0.0955  55  GLU A CD  
439  O OE1 . GLU A 67  ? 0.7003 0.4652 0.7845 -0.0700 -0.0127 0.0882  55  GLU A OE1 
440  O OE2 . GLU A 67  ? 0.9896 0.7504 1.0611 -0.0520 0.0055  0.1043  55  GLU A OE2 
441  N N   . LYS A 68  ? 0.3467 0.2200 0.4051 -0.0289 0.0120  0.0649  56  LYS A N   
442  C CA  . LYS A 68  ? 0.3375 0.2148 0.3777 -0.0131 0.0161  0.0571  56  LYS A CA  
443  C C   . LYS A 68  ? 0.3214 0.2314 0.3669 -0.0087 0.0249  0.0618  56  LYS A C   
444  O O   . LYS A 68  ? 0.3128 0.2284 0.3492 0.0022  0.0310  0.0637  56  LYS A O   
445  C CB  . LYS A 68  ? 0.3585 0.2279 0.3879 -0.0103 0.0078  0.0427  56  LYS A CB  
446  C CG  . LYS A 68  ? 0.4684 0.3430 0.4809 0.0059  0.0122  0.0365  56  LYS A CG  
447  C CD  . LYS A 68  ? 0.5506 0.4238 0.5543 0.0082  0.0053  0.0244  56  LYS A CD  
448  C CE  . LYS A 68  ? 0.7245 0.5974 0.7101 0.0251  0.0092  0.0194  56  LYS A CE  
449  N NZ  . LYS A 68  ? 0.8315 0.7027 0.8066 0.0283  0.0029  0.0087  56  LYS A NZ  
450  N N   . GLY A 69  ? 0.2879 0.2193 0.3475 -0.0166 0.0249  0.0633  57  GLY A N   
451  C CA  . GLY A 69  ? 0.2814 0.2397 0.3432 -0.0114 0.0321  0.0659  57  GLY A CA  
452  C C   . GLY A 69  ? 0.2763 0.2413 0.3384 -0.0079 0.0405  0.0772  57  GLY A C   
453  O O   . GLY A 69  ? 0.2707 0.2478 0.3252 0.0009  0.0449  0.0770  57  GLY A O   
454  N N   . ARG A 70  ? 0.2824 0.2411 0.3540 -0.0150 0.0423  0.0880  58  ARG A N   
455  C CA  . ARG A 70  ? 0.2868 0.2520 0.3563 -0.0100 0.0508  0.0998  58  ARG A CA  
456  C C   . ARG A 70  ? 0.3364 0.2892 0.3892 0.0013  0.0518  0.0979  58  ARG A C   
457  O O   . ARG A 70  ? 0.2919 0.2570 0.3376 0.0097  0.0572  0.1024  58  ARG A O   
458  C CB  . ARG A 70  ? 0.3152 0.2745 0.3988 -0.0199 0.0528  0.1138  58  ARG A CB  
459  C CG  . ARG A 70  ? 0.2999 0.2803 0.4038 -0.0300 0.0540  0.1200  58  ARG A CG  
460  C CD  . ARG A 70  ? 0.3226 0.3057 0.4415 -0.0371 0.0600  0.1393  58  ARG A CD  
461  N NE  . ARG A 70  ? 0.3687 0.3225 0.4931 -0.0470 0.0530  0.1426  58  ARG A NE  
462  C CZ  . ARG A 70  ? 0.3939 0.3367 0.5325 -0.0611 0.0427  0.1397  58  ARG A CZ  
463  N NH1 . ARG A 70  ? 0.3617 0.3241 0.5134 -0.0675 0.0390  0.1356  58  ARG A NH1 
464  N NH2 . ARG A 70  ? 0.4254 0.3350 0.5637 -0.0682 0.0347  0.1399  58  ARG A NH2 
465  N N   . ALA A 71  ? 0.3018 0.2302 0.3474 0.0027  0.0461  0.0916  59  ALA A N   
466  C CA  . ALA A 71  ? 0.3128 0.2307 0.3434 0.0151  0.0475  0.0907  59  ALA A CA  
467  C C   . ALA A 71  ? 0.2988 0.2358 0.3229 0.0239  0.0482  0.0837  59  ALA A C   
468  O O   . ALA A 71  ? 0.2991 0.2443 0.3164 0.0330  0.0515  0.0876  59  ALA A O   
469  C CB  . ALA A 71  ? 0.3332 0.2205 0.3558 0.0164  0.0413  0.0839  59  ALA A CB  
470  N N   . GLN A 72  ? 0.2772 0.2221 0.3041 0.0207  0.0444  0.0744  60  GLN A N   
471  C CA  . GLN A 72  ? 0.2562 0.2191 0.2796 0.0272  0.0448  0.0695  60  GLN A CA  
472  C C   . GLN A 72  ? 0.2940 0.2773 0.3202 0.0276  0.0484  0.0744  60  GLN A C   
473  O O   . GLN A 72  ? 0.2650 0.2586 0.2862 0.0344  0.0487  0.0747  60  GLN A O   
474  C CB  . GLN A 72  ? 0.2713 0.2385 0.2978 0.0235  0.0405  0.0603  60  GLN A CB  
475  C CG  . GLN A 72  ? 0.2857 0.2330 0.3048 0.0254  0.0359  0.0532  60  GLN A CG  
476  C CD  . GLN A 72  ? 0.2822 0.2355 0.3045 0.0209  0.0313  0.0452  60  GLN A CD  
477  O OE1 . GLN A 72  ? 0.2664 0.2339 0.2993 0.0134  0.0310  0.0459  60  GLN A OE1 
478  N NE2 . GLN A 72  ? 0.3365 0.2801 0.3483 0.0272  0.0282  0.0381  60  GLN A NE2 
479  N N   . ALA A 73  ? 0.2730 0.2630 0.3071 0.0207  0.0506  0.0783  61  ALA A N   
480  C CA  . ALA A 73  ? 0.2787 0.2860 0.3113 0.0234  0.0544  0.0821  61  ALA A CA  
481  C C   . ALA A 73  ? 0.2957 0.3024 0.3195 0.0308  0.0577  0.0902  61  ALA A C   
482  O O   . ALA A 73  ? 0.2993 0.3182 0.3159 0.0367  0.0578  0.0900  61  ALA A O   
483  C CB  . ALA A 73  ? 0.2853 0.3005 0.3280 0.0167  0.0580  0.0872  61  ALA A CB  
484  N N   . ARG A 74  ? 0.2882 0.2799 0.3119 0.0306  0.0596  0.0974  62  ARG A N   
485  C CA  . ARG A 74  ? 0.3085 0.2995 0.3235 0.0386  0.0628  0.1062  62  ARG A CA  
486  C C   . ARG A 74  ? 0.3057 0.3005 0.3125 0.0474  0.0591  0.1014  62  ARG A C   
487  O O   . ARG A 74  ? 0.3367 0.3431 0.3362 0.0542  0.0592  0.1048  62  ARG A O   
488  C CB  . ARG A 74  ? 0.3466 0.3164 0.3635 0.0367  0.0648  0.1145  62  ARG A CB  
489  C CG  . ARG A 74  ? 0.4660 0.4355 0.4931 0.0282  0.0694  0.1250  62  ARG A CG  
490  C CD  . ARG A 74  ? 0.5418 0.4907 0.5695 0.0276  0.0718  0.1368  62  ARG A CD  
491  N NE  . ARG A 74  ? 0.4972 0.4189 0.5226 0.0269  0.0660  0.1305  62  ARG A NE  
492  C CZ  . ARG A 74  ? 0.5608 0.4650 0.5947 0.0163  0.0608  0.1263  62  ARG A CZ  
493  N NH1 . ARG A 74  ? 0.3858 0.2996 0.4349 0.0039  0.0602  0.1282  62  ARG A NH1 
494  N NH2 . ARG A 74  ? 0.5571 0.4337 0.5834 0.0190  0.0553  0.1198  62  ARG A NH2 
495  N N   . LEU A 75  ? 0.2883 0.2745 0.2963 0.0480  0.0555  0.0944  63  LEU A N   
496  C CA  . LEU A 75  ? 0.2933 0.2866 0.2970 0.0565  0.0529  0.0922  63  LEU A CA  
497  C C   . LEU A 75  ? 0.2891 0.3029 0.2945 0.0555  0.0492  0.0875  63  LEU A C   
498  O O   . LEU A 75  ? 0.2870 0.3125 0.2896 0.0612  0.0466  0.0897  63  LEU A O   
499  C CB  . LEU A 75  ? 0.2910 0.2722 0.2946 0.0587  0.0512  0.0863  63  LEU A CB  
500  C CG  . LEU A 75  ? 0.2961 0.2528 0.2939 0.0631  0.0531  0.0900  63  LEU A CG  
501  C CD1 . LEU A 75  ? 0.3574 0.2994 0.3518 0.0650  0.0508  0.0815  63  LEU A CD1 
502  C CD2 . LEU A 75  ? 0.3761 0.3350 0.3676 0.0750  0.0554  0.0986  63  LEU A CD2 
503  N N   . LEU A 76  ? 0.2398 0.2575 0.2503 0.0481  0.0481  0.0813  64  LEU A N   
504  C CA  . LEU A 76  ? 0.2382 0.2708 0.2493 0.0469  0.0441  0.0764  64  LEU A CA  
505  C C   . LEU A 76  ? 0.2953 0.3357 0.2984 0.0501  0.0443  0.0801  64  LEU A C   
506  O O   . LEU A 76  ? 0.2616 0.3118 0.2609 0.0529  0.0387  0.0782  64  LEU A O   
507  C CB  . LEU A 76  ? 0.2456 0.2784 0.2627 0.0398  0.0441  0.0702  64  LEU A CB  
508  C CG  . LEU A 76  ? 0.2379 0.2814 0.2543 0.0386  0.0403  0.0649  64  LEU A CG  
509  C CD1 . LEU A 76  ? 0.2947 0.3443 0.3146 0.0391  0.0344  0.0617  64  LEU A CD1 
510  C CD2 . LEU A 76  ? 0.2713 0.3148 0.2929 0.0334  0.0419  0.0609  64  LEU A CD2 
511  N N   . ALA A 77  ? 0.2777 0.3141 0.2779 0.0498  0.0501  0.0859  65  ALA A N   
512  C CA  . ALA A 77  ? 0.2913 0.3357 0.2808 0.0550  0.0516  0.0900  65  ALA A CA  
513  C C   . ALA A 77  ? 0.3126 0.3599 0.2939 0.0626  0.0487  0.0949  65  ALA A C   
514  O O   . ALA A 77  ? 0.3390 0.3953 0.3097 0.0675  0.0444  0.0937  65  ALA A O   
515  C CB  . ALA A 77  ? 0.3405 0.3822 0.3306 0.0540  0.0602  0.0990  65  ALA A CB  
516  N N   . ALA A 78  ? 0.2820 0.3209 0.2665 0.0647  0.0507  0.1007  66  ALA A N   
517  C CA  . ALA A 78  ? 0.3136 0.3569 0.2919 0.0732  0.0480  0.1065  66  ALA A CA  
518  C C   . ALA A 78  ? 0.2958 0.3519 0.2773 0.0739  0.0390  0.1004  66  ALA A C   
519  O O   . ALA A 78  ? 0.3317 0.3990 0.3069 0.0789  0.0333  0.1024  66  ALA A O   
520  C CB  . ALA A 78  ? 0.3134 0.3426 0.2943 0.0767  0.0525  0.1137  66  ALA A CB  
521  N N   . ARG A 79  ? 0.2821 0.3374 0.2739 0.0687  0.0372  0.0938  67  ARG A N   
522  C CA  . ARG A 79  ? 0.2780 0.3468 0.2764 0.0676  0.0290  0.0899  67  ARG A CA  
523  C C   . ARG A 79  ? 0.3099 0.3868 0.3025 0.0648  0.0213  0.0846  67  ARG A C   
524  O O   . ARG A 79  ? 0.3087 0.3974 0.3021 0.0660  0.0124  0.0850  67  ARG A O   
525  C CB  . ARG A 79  ? 0.2669 0.3332 0.2761 0.0625  0.0298  0.0846  67  ARG A CB  
526  C CG  . ARG A 79  ? 0.2499 0.3308 0.2685 0.0590  0.0218  0.0818  67  ARG A CG  
527  C CD  . ARG A 79  ? 0.2312 0.3101 0.2589 0.0548  0.0236  0.0778  67  ARG A CD  
528  N NE  . ARG A 79  ? 0.2317 0.3240 0.2700 0.0500  0.0162  0.0769  67  ARG A NE  
529  C CZ  . ARG A 79  ? 0.2454 0.3408 0.2934 0.0471  0.0171  0.0760  67  ARG A CZ  
530  N NH1 . ARG A 79  ? 0.2231 0.3089 0.2692 0.0488  0.0241  0.0740  67  ARG A NH1 
531  N NH2 . ARG A 79  ? 0.2427 0.3509 0.3024 0.0420  0.0100  0.0775  67  ARG A NH2 
532  N N   . LEU A 80  ? 0.2829 0.3536 0.2697 0.0615  0.0239  0.0794  68  LEU A N   
533  C CA  . LEU A 80  ? 0.3312 0.4054 0.3095 0.0604  0.0167  0.0725  68  LEU A CA  
534  C C   . LEU A 80  ? 0.3116 0.3876 0.2717 0.0682  0.0162  0.0754  68  LEU A C   
535  O O   . LEU A 80  ? 0.3375 0.4146 0.2858 0.0696  0.0087  0.0687  68  LEU A O   
536  C CB  . LEU A 80  ? 0.3233 0.3911 0.3031 0.0555  0.0197  0.0653  68  LEU A CB  
537  C CG  . LEU A 80  ? 0.3393 0.4058 0.3345 0.0485  0.0190  0.0618  68  LEU A CG  
538  C CD1 . LEU A 80  ? 0.3651 0.4268 0.3595 0.0451  0.0199  0.0546  68  LEU A CD1 
539  C CD2 . LEU A 80  ? 0.3733 0.4478 0.3771 0.0461  0.0101  0.0615  68  LEU A CD2 
540  N N   . ALA A 81  ? 0.3367 0.4120 0.2928 0.0740  0.0232  0.0853  69  ALA A N   
541  C CA  . ALA A 81  ? 0.3181 0.3961 0.2557 0.0825  0.0241  0.0896  69  ALA A CA  
542  C C   . ALA A 81  ? 0.3277 0.4148 0.2557 0.0863  0.0108  0.0864  69  ALA A C   
543  O O   . ALA A 81  ? 0.3986 0.4869 0.3070 0.0924  0.0070  0.0834  69  ALA A O   
544  C CB  . ALA A 81  ? 0.3516 0.4263 0.2887 0.0876  0.0339  0.1028  69  ALA A CB  
545  N N   . GLY A 82  ? 0.3584 0.4527 0.2996 0.0833  0.0033  0.0874  70  GLY A N   
546  C CA  . GLY A 82  ? 0.3876 0.4932 0.3246 0.0850  -0.0110 0.0860  70  GLY A CA  
547  C C   . GLY A 82  ? 0.3625 0.4688 0.3037 0.0766  -0.0244 0.0746  70  GLY A C   
548  O O   . GLY A 82  ? 0.3989 0.5136 0.3375 0.0759  -0.0391 0.0724  70  GLY A O   
549  N N   . VAL A 83  ? 0.3096 0.4067 0.2571 0.0700  -0.0206 0.0677  71  VAL A N   
550  C CA  . VAL A 83  ? 0.3053 0.3993 0.2580 0.0615  -0.0320 0.0576  71  VAL A CA  
551  C C   . VAL A 83  ? 0.3582 0.4410 0.2865 0.0658  -0.0368 0.0473  71  VAL A C   
552  O O   . VAL A 83  ? 0.3879 0.4637 0.3042 0.0718  -0.0252 0.0471  71  VAL A O   
553  C CB  . VAL A 83  ? 0.3039 0.3927 0.2735 0.0542  -0.0245 0.0560  71  VAL A CB  
554  C CG1 . VAL A 83  ? 0.3370 0.4198 0.3105 0.0460  -0.0353 0.0464  71  VAL A CG1 
555  C CG2 . VAL A 83  ? 0.3141 0.4132 0.3045 0.0522  -0.0196 0.0654  71  VAL A CG2 
556  N N   . PRO A 84  ? 0.3682 0.4484 0.2886 0.0632  -0.0538 0.0389  72  PRO A N   
557  C CA  . PRO A 84  ? 0.3752 0.4406 0.2691 0.0691  -0.0584 0.0270  72  PRO A CA  
558  C C   . PRO A 84  ? 0.3799 0.4332 0.2776 0.0664  -0.0500 0.0213  72  PRO A C   
559  O O   . PRO A 84  ? 0.3520 0.4031 0.2694 0.0560  -0.0536 0.0194  72  PRO A O   
560  C CB  . PRO A 84  ? 0.3666 0.4290 0.2573 0.0632  -0.0812 0.0185  72  PRO A CB  
561  C CG  . PRO A 84  ? 0.3710 0.4541 0.2806 0.0591  -0.0868 0.0298  72  PRO A CG  
562  C CD  . PRO A 84  ? 0.3525 0.4434 0.2869 0.0555  -0.0704 0.0401  72  PRO A CD  
563  N N   . LEU A 85  ? 0.3560 0.4038 0.2360 0.0766  -0.0378 0.0203  73  LEU A N   
564  C CA  . LEU A 85  ? 0.3545 0.3947 0.2384 0.0763  -0.0276 0.0172  73  LEU A CA  
565  C C   . LEU A 85  ? 0.3651 0.3950 0.2194 0.0891  -0.0267 0.0089  73  LEU A C   
566  O O   . LEU A 85  ? 0.3815 0.4160 0.2158 0.1007  -0.0215 0.0128  73  LEU A O   
567  C CB  . LEU A 85  ? 0.4627 0.5120 0.3603 0.0765  -0.0096 0.0289  73  LEU A CB  
568  C CG  . LEU A 85  ? 0.5188 0.5722 0.4445 0.0653  -0.0065 0.0337  73  LEU A CG  
569  C CD1 . LEU A 85  ? 0.4477 0.5031 0.3814 0.0660  0.0094  0.0401  73  LEU A CD1 
570  C CD2 . LEU A 85  ? 0.4955 0.5418 0.4309 0.0569  -0.0165 0.0253  73  LEU A CD2 
571  N N   . HIS A 86  ? 0.3727 0.3883 0.2231 0.0884  -0.0309 -0.0016 74  HIS A N   
572  C CA  . HIS A 86  ? 0.4097 0.4122 0.2292 0.1023  -0.0322 -0.0118 74  HIS A CA  
573  C C   . HIS A 86  ? 0.4000 0.4013 0.2198 0.1090  -0.0170 -0.0110 74  HIS A C   
574  O O   . HIS A 86  ? 0.4543 0.4491 0.2476 0.1243  -0.0132 -0.0164 74  HIS A O   
575  C CB  . HIS A 86  ? 0.4318 0.4144 0.2389 0.0989  -0.0539 -0.0267 74  HIS A CB  
576  C CG  . HIS A 86  ? 0.4679 0.4563 0.2797 0.0908  -0.0695 -0.0254 74  HIS A CG  
577  N ND1 . HIS A 86  ? 0.4522 0.4454 0.2936 0.0740  -0.0789 -0.0220 74  HIS A ND1 
578  C CD2 . HIS A 86  ? 0.4759 0.4713 0.2701 0.0979  -0.0748 -0.0237 74  HIS A CD2 
579  C CE1 . HIS A 86  ? 0.4438 0.4468 0.2860 0.0709  -0.0902 -0.0189 74  HIS A CE1 
580  N NE2 . HIS A 86  ? 0.4533 0.4573 0.2667 0.0851  -0.0885 -0.0202 74  HIS A NE2 
581  N N   . GLY A 87  ? 0.3688 0.3780 0.2168 0.0993  -0.0080 -0.0039 75  GLY A N   
582  C CA  . GLY A 87  ? 0.3611 0.3751 0.2139 0.1048  0.0071  0.0000  75  GLY A CA  
583  C C   . GLY A 87  ? 0.3262 0.3516 0.2109 0.0922  0.0149  0.0097  75  GLY A C   
584  O O   . GLY A 87  ? 0.3376 0.3633 0.2394 0.0800  0.0077  0.0107  75  GLY A O   
585  N N   . VAL A 88  ? 0.3170 0.3528 0.2097 0.0957  0.0294  0.0171  76  VAL A N   
586  C CA  . VAL A 88  ? 0.2968 0.3420 0.2174 0.0845  0.0360  0.0253  76  VAL A CA  
587  C C   . VAL A 88  ? 0.3030 0.3514 0.2300 0.0880  0.0436  0.0252  76  VAL A C   
588  O O   . VAL A 88  ? 0.3447 0.4006 0.2619 0.0994  0.0533  0.0289  76  VAL A O   
589  C CB  . VAL A 88  ? 0.2797 0.3377 0.2087 0.0826  0.0455  0.0384  76  VAL A CB  
590  C CG1 . VAL A 88  ? 0.3065 0.3699 0.2617 0.0713  0.0500  0.0444  76  VAL A CG1 
591  C CG2 . VAL A 88  ? 0.3277 0.3840 0.2507 0.0809  0.0388  0.0400  76  VAL A CG2 
592  N N   . TRP A 89  ? 0.2701 0.3150 0.2135 0.0793  0.0399  0.0222  77  TRP A N   
593  C CA  . TRP A 89  ? 0.2836 0.3324 0.2361 0.0813  0.0456  0.0226  77  TRP A CA  
594  C C   . TRP A 89  ? 0.2731 0.3318 0.2511 0.0694  0.0488  0.0298  77  TRP A C   
595  O O   . TRP A 89  ? 0.2823 0.3393 0.2690 0.0598  0.0443  0.0312  77  TRP A O   
596  C CB  . TRP A 89  ? 0.3012 0.3334 0.2476 0.0824  0.0360  0.0116  77  TRP A CB  
597  C CG  . TRP A 89  ? 0.3890 0.4077 0.3072 0.0962  0.0323  0.0026  77  TRP A CG  
598  C CD1 . TRP A 89  ? 0.4399 0.4481 0.3389 0.0987  0.0234  -0.0034 77  TRP A CD1 
599  C CD2 . TRP A 89  ? 0.5607 0.5744 0.4649 0.1107  0.0369  -0.0019 77  TRP A CD2 
600  N NE1 . TRP A 89  ? 0.5332 0.5279 0.4052 0.1135  0.0211  -0.0125 77  TRP A NE1 
601  C CE2 . TRP A 89  ? 0.4566 0.4541 0.3305 0.1221  0.0302  -0.0117 77  TRP A CE2 
602  C CE3 . TRP A 89  ? 0.4975 0.5194 0.4109 0.1164  0.0457  0.0017  77  TRP A CE3 
603  C CZ2 . TRP A 89  ? 0.6304 0.6170 0.4808 0.1400  0.0326  -0.0189 77  TRP A CZ2 
604  C CZ3 . TRP A 89  ? 0.6131 0.6272 0.5060 0.1342  0.0491  -0.0040 77  TRP A CZ3 
605  C CH2 . TRP A 89  ? 0.6396 0.6350 0.5001 0.1465  0.0429  -0.0146 77  TRP A CH2 
606  N N   . ALA A 90  ? 0.2725 0.3423 0.2618 0.0709  0.0563  0.0345  78  ALA A N   
607  C CA  . ALA A 90  ? 0.2592 0.3379 0.2712 0.0601  0.0579  0.0405  78  ALA A CA  
608  C C   . ALA A 90  ? 0.2307 0.3175 0.2522 0.0631  0.0611  0.0412  78  ALA A C   
609  O O   . ALA A 90  ? 0.2621 0.3535 0.2754 0.0748  0.0666  0.0414  78  ALA A O   
610  C CB  . ALA A 90  ? 0.2524 0.3425 0.2732 0.0561  0.0649  0.0514  78  ALA A CB  
611  N N   . SER A 91  ? 0.2226 0.3118 0.2604 0.0538  0.0578  0.0418  79  SER A N   
612  C CA  . SER A 91  ? 0.2535 0.3564 0.3049 0.0552  0.0616  0.0460  79  SER A CA  
613  C C   . SER A 91  ? 0.2858 0.4078 0.3475 0.0559  0.0707  0.0572  79  SER A C   
614  O O   . SER A 91  ? 0.2733 0.3962 0.3328 0.0536  0.0738  0.0623  79  SER A O   
615  C CB  . SER A 91  ? 0.2786 0.3818 0.3445 0.0448  0.0556  0.0453  79  SER A CB  
616  O OG  . SER A 91  ? 0.2526 0.3640 0.3318 0.0354  0.0566  0.0518  79  SER A OG  
617  N N   . GLY A 92  ? 0.2542 0.3930 0.3284 0.0594  0.0752  0.0627  80  GLY A N   
618  C CA  . GLY A 92  ? 0.2514 0.4123 0.3409 0.0585  0.0835  0.0759  80  GLY A CA  
619  C C   . GLY A 92  ? 0.2216 0.3890 0.3326 0.0422  0.0800  0.0829  80  GLY A C   
620  O O   . GLY A 92  ? 0.2444 0.4290 0.3701 0.0390  0.0862  0.0954  80  GLY A O   
621  N N   . ALA A 93  ? 0.2031 0.3565 0.3157 0.0320  0.0702  0.0756  81  ALA A N   
622  C CA  . ALA A 93  ? 0.2537 0.4090 0.3833 0.0176  0.0653  0.0803  81  ALA A CA  
623  C C   . ALA A 93  ? 0.2203 0.3702 0.3481 0.0132  0.0687  0.0866  81  ALA A C   
624  O O   . ALA A 93  ? 0.2342 0.3708 0.3441 0.0184  0.0701  0.0824  81  ALA A O   
625  C CB  . ALA A 93  ? 0.2263 0.3650 0.3515 0.0112  0.0549  0.0700  81  ALA A CB  
626  N N   . HIS A 94  ? 0.2240 0.3830 0.3713 0.0027  0.0687  0.0969  82  HIS A N   
627  C CA  . HIS A 94  ? 0.2335 0.3863 0.3811 -0.0021 0.0720  0.1049  82  HIS A CA  
628  C C   . HIS A 94  ? 0.2319 0.3587 0.3627 -0.0038 0.0662  0.0955  82  HIS A C   
629  O O   . HIS A 94  ? 0.2460 0.3658 0.3648 0.0008  0.0709  0.0983  82  HIS A O   
630  C CB  . HIS A 94  ? 0.2499 0.4120 0.4236 -0.0165 0.0695  0.1166  82  HIS A CB  
631  C CG  . HIS A 94  ? 0.3376 0.5305 0.5311 -0.0144 0.0778  0.1310  82  HIS A CG  
632  N ND1 . HIS A 94  ? 0.3168 0.5245 0.5042 -0.0018 0.0913  0.1404  82  HIS A ND1 
633  C CD2 . HIS A 94  ? 0.4061 0.6198 0.6253 -0.0221 0.0748  0.1383  82  HIS A CD2 
634  C CE1 . HIS A 94  ? 0.4170 0.6508 0.6229 -0.0006 0.0961  0.1517  82  HIS A CE1 
635  N NE2 . HIS A 94  ? 0.3602 0.5995 0.5875 -0.0134 0.0862  0.1514  82  HIS A NE2 
636  N N   . ARG A 95  ? 0.2016 0.3154 0.3307 -0.0090 0.0565  0.0853  83  ARG A N   
637  C CA  . ARG A 95  ? 0.2141 0.3057 0.3286 -0.0093 0.0519  0.0778  83  ARG A CA  
638  C C   . ARG A 95  ? 0.2333 0.3209 0.3290 0.0018  0.0551  0.0725  83  ARG A C   
639  O O   . ARG A 95  ? 0.2395 0.3153 0.3244 0.0038  0.0553  0.0719  83  ARG A O   
640  C CB  . ARG A 95  ? 0.2325 0.3135 0.3469 -0.0143 0.0420  0.0683  83  ARG A CB  
641  C CG  . ARG A 95  ? 0.2396 0.3289 0.3525 -0.0095 0.0396  0.0614  83  ARG A CG  
642  C CD  . ARG A 95  ? 0.2870 0.3702 0.4035 -0.0159 0.0298  0.0555  83  ARG A CD  
643  N NE  . ARG A 95  ? 0.3093 0.3998 0.4245 -0.0115 0.0272  0.0502  83  ARG A NE  
644  C CZ  . ARG A 95  ? 0.2968 0.4049 0.4237 -0.0109 0.0277  0.0535  83  ARG A CZ  
645  N NH1 . ARG A 95  ? 0.2888 0.4125 0.4311 -0.0141 0.0317  0.0627  83  ARG A NH1 
646  N NH2 . ARG A 95  ? 0.3593 0.4706 0.4831 -0.0064 0.0247  0.0487  83  ARG A NH2 
647  N N   . ALA A 96  ? 0.2399 0.3363 0.3317 0.0090  0.0567  0.0686  84  ALA A N   
648  C CA  . ALA A 96  ? 0.1885 0.2795 0.2630 0.0182  0.0577  0.0632  84  ALA A CA  
649  C C   . ALA A 96  ? 0.2277 0.3243 0.2945 0.0251  0.0653  0.0699  84  ALA A C   
650  O O   . ALA A 96  ? 0.2560 0.3444 0.3091 0.0291  0.0648  0.0683  84  ALA A O   
651  C CB  . ALA A 96  ? 0.2290 0.3229 0.3003 0.0237  0.0558  0.0566  84  ALA A CB  
652  N N   . GLN A 97  ? 0.2046 0.3171 0.2803 0.0271  0.0726  0.0788  85  GLN A N   
653  C CA  . GLN A 97  ? 0.2415 0.3616 0.3090 0.0353  0.0814  0.0870  85  GLN A CA  
654  C C   . GLN A 97  ? 0.2536 0.3652 0.3192 0.0308  0.0819  0.0932  85  GLN A C   
655  O O   . GLN A 97  ? 0.2642 0.3727 0.3134 0.0387  0.0847  0.0943  85  GLN A O   
656  C CB  . GLN A 97  ? 0.2250 0.3673 0.3078 0.0369  0.0900  0.0988  85  GLN A CB  
657  C CG  . GLN A 97  ? 0.2443 0.3957 0.3244 0.0466  0.0915  0.0933  85  GLN A CG  
658  C CD  . GLN A 97  ? 0.2740 0.4239 0.3293 0.0637  0.0968  0.0897  85  GLN A CD  
659  O OE1 . GLN A 97  ? 0.3380 0.4962 0.3862 0.0709  0.1055  0.0987  85  GLN A OE1 
660  N NE2 . GLN A 97  ? 0.3016 0.4397 0.3426 0.0705  0.0913  0.0767  85  GLN A NE2 
661  N N   . GLN A 98  ? 0.2461 0.3534 0.3279 0.0186  0.0789  0.0978  86  GLN A N   
662  C CA  . GLN A 98  ? 0.2268 0.3238 0.3080 0.0144  0.0797  0.1049  86  GLN A CA  
663  C C   . GLN A 98  ? 0.2365 0.3166 0.3006 0.0182  0.0742  0.0959  86  GLN A C   
664  O O   . GLN A 98  ? 0.2510 0.3268 0.3055 0.0225  0.0771  0.1012  86  GLN A O   
665  C CB  . GLN A 98  ? 0.2682 0.3598 0.3692 0.0004  0.0754  0.1093  86  GLN A CB  
666  C CG  . GLN A 98  ? 0.3087 0.3900 0.4136 -0.0050 0.0772  0.1202  86  GLN A CG  
667  C CD  . GLN A 98  ? 0.3667 0.4414 0.4922 -0.0200 0.0713  0.1244  86  GLN A CD  
668  O OE1 . GLN A 98  ? 0.3056 0.3906 0.4454 -0.0263 0.0674  0.1223  86  GLN A OE1 
669  N NE2 . GLN A 98  ? 0.3446 0.4012 0.4713 -0.0257 0.0697  0.1305  86  GLN A NE2 
670  N N   . THR A 99  ? 0.2333 0.3059 0.2947 0.0170  0.0666  0.0839  87  THR A N   
671  C CA  . THR A 99  ? 0.2443 0.3059 0.2923 0.0210  0.0619  0.0771  87  THR A CA  
672  C C   . THR A 99  ? 0.2345 0.3012 0.2669 0.0310  0.0635  0.0756  87  THR A C   
673  O O   . THR A 99  ? 0.2700 0.3322 0.2920 0.0352  0.0628  0.0774  87  THR A O   
674  C CB  . THR A 99  ? 0.1998 0.2564 0.2497 0.0183  0.0547  0.0668  87  THR A CB  
675  O OG1 . THR A 99  ? 0.2352 0.2860 0.2963 0.0102  0.0522  0.0672  87  THR A OG1 
676  C CG2 . THR A 99  ? 0.2323 0.2810 0.2725 0.0219  0.0507  0.0629  87  THR A CG2 
677  N N   . ALA A 100 ? 0.2696 0.3450 0.2991 0.0357  0.0652  0.0724  88  ALA A N   
678  C CA  . ALA A 100 ? 0.2409 0.3178 0.2523 0.0460  0.0650  0.0687  88  ALA A CA  
679  C C   . ALA A 100 ? 0.2495 0.3317 0.2516 0.0526  0.0722  0.0785  88  ALA A C   
680  O O   . ALA A 100 ? 0.2891 0.3681 0.2740 0.0598  0.0695  0.0763  88  ALA A O   
681  C CB  . ALA A 100 ? 0.2409 0.3234 0.2499 0.0513  0.0662  0.0636  88  ALA A CB  
682  N N   A SER A 101 ? 0.2485 0.3398 0.2622 0.0503  0.0809  0.0904  89  SER A N   
683  N N   B SER A 101 ? 0.2491 0.3405 0.2627 0.0504  0.0810  0.0904  89  SER A N   
684  C CA  A SER A 101 ? 0.3058 0.4038 0.3124 0.0566  0.0893  0.1028  89  SER A CA  
685  C CA  B SER A 101 ? 0.3059 0.4040 0.3120 0.0568  0.0893  0.1027  89  SER A CA  
686  C C   A SER A 101 ? 0.2682 0.3556 0.2691 0.0553  0.0865  0.1062  89  SER A C   
687  C C   B SER A 101 ? 0.2676 0.3550 0.2685 0.0554  0.0865  0.1062  89  SER A C   
688  O O   A SER A 101 ? 0.2946 0.3845 0.2798 0.0644  0.0895  0.1112  89  SER A O   
689  O O   B SER A 101 ? 0.2951 0.3848 0.2802 0.0644  0.0895  0.1113  89  SER A O   
690  C CB  A SER A 101 ? 0.2789 0.3894 0.3054 0.0510  0.0984  0.1171  89  SER A CB  
691  C CB  B SER A 101 ? 0.2792 0.3905 0.3043 0.0521  0.0989  0.1173  89  SER A CB  
692  O OG  A SER A 101 ? 0.3039 0.4233 0.3243 0.0580  0.1081  0.1314  89  SER A OG  
693  O OG  B SER A 101 ? 0.2863 0.4128 0.3133 0.0583  0.1043  0.1174  89  SER A OG  
694  N N   . ALA A 102 ? 0.2831 0.3589 0.2954 0.0456  0.0809  0.1037  90  ALA A N   
695  C CA  . ALA A 102 ? 0.2856 0.3507 0.2926 0.0461  0.0783  0.1068  90  ALA A CA  
696  C C   . ALA A 102 ? 0.2740 0.3383 0.2636 0.0540  0.0716  0.0982  90  ALA A C   
697  O O   . ALA A 102 ? 0.3232 0.3877 0.3007 0.0609  0.0721  0.1035  90  ALA A O   
698  C CB  . ALA A 102 ? 0.2753 0.3272 0.2956 0.0363  0.0735  0.1038  90  ALA A CB  
699  N N   . VAL A 103 ? 0.2827 0.3468 0.2715 0.0529  0.0646  0.0859  91  VAL A N   
700  C CA  . VAL A 103 ? 0.2663 0.3298 0.2415 0.0583  0.0563  0.0782  91  VAL A CA  
701  C C   . VAL A 103 ? 0.2859 0.3552 0.2417 0.0689  0.0582  0.0790  91  VAL A C   
702  O O   . VAL A 103 ? 0.3232 0.3930 0.2653 0.0751  0.0546  0.0805  91  VAL A O   
703  C CB  . VAL A 103 ? 0.2991 0.3603 0.2797 0.0538  0.0489  0.0666  91  VAL A CB  
704  C CG1 . VAL A 103 ? 0.2976 0.3582 0.2655 0.0579  0.0393  0.0591  91  VAL A CG1 
705  C CG2 . VAL A 103 ? 0.2686 0.3247 0.2641 0.0459  0.0464  0.0659  91  VAL A CG2 
706  N N   . ALA A 104 ? 0.2805 0.3552 0.2338 0.0724  0.0643  0.0791  92  ALA A N   
707  C CA  . ALA A 104 ? 0.2902 0.3692 0.2212 0.0851  0.0660  0.0777  92  ALA A CA  
708  C C   . ALA A 104 ? 0.3195 0.4046 0.2400 0.0927  0.0734  0.0906  92  ALA A C   
709  O O   . ALA A 104 ? 0.3239 0.4102 0.2209 0.1042  0.0711  0.0886  92  ALA A O   
710  C CB  . ALA A 104 ? 0.3235 0.4085 0.2551 0.0893  0.0728  0.0762  92  ALA A CB  
711  N N   . ALA A 105 ? 0.3466 0.4349 0.2834 0.0870  0.0822  0.1042  93  ALA A N   
712  C CA  . ALA A 105 ? 0.3651 0.4594 0.2937 0.0942  0.0907  0.1192  93  ALA A CA  
713  C C   . ALA A 105 ? 0.3260 0.4155 0.2389 0.0996  0.0833  0.1183  93  ALA A C   
714  O O   . ALA A 105 ? 0.3896 0.4852 0.2838 0.1112  0.0873  0.1256  93  ALA A O   
715  C CB  . ALA A 105 ? 0.4483 0.5433 0.3997 0.0847  0.0995  0.1344  93  ALA A CB  
716  N N   . GLU A 106 ? 0.3371 0.4179 0.2566 0.0928  0.0725  0.1096  94  GLU A N   
717  C CA  . GLU A 106 ? 0.3990 0.4782 0.3072 0.0975  0.0645  0.1094  94  GLU A CA  
718  C C   . GLU A 106 ? 0.4151 0.4978 0.2989 0.1074  0.0559  0.1001  94  GLU A C   
719  O O   . GLU A 106 ? 0.4695 0.5545 0.3395 0.1140  0.0501  0.1022  94  GLU A O   
720  C CB  . GLU A 106 ? 0.3598 0.4326 0.2826 0.0888  0.0555  0.1031  94  GLU A CB  
721  C CG  . GLU A 106 ? 0.3881 0.4533 0.3307 0.0804  0.0611  0.1095  94  GLU A CG  
722  C CD  . GLU A 106 ? 0.4828 0.5451 0.4244 0.0842  0.0687  0.1248  94  GLU A CD  
723  O OE1 . GLU A 106 ? 0.5467 0.6133 0.4741 0.0934  0.0667  0.1299  94  GLU A OE1 
724  O OE2 . GLU A 106 ? 0.5698 0.6247 0.5250 0.0778  0.0756  0.1321  94  GLU A OE2 
725  N N   . HIS A 107 ? 0.3523 0.4341 0.2295 0.1088  0.0542  0.0895  95  HIS A N   
726  C CA  . HIS A 107 ? 0.3976 0.4773 0.2501 0.1176  0.0440  0.0777  95  HIS A CA  
727  C C   . HIS A 107 ? 0.3852 0.4689 0.2163 0.1312  0.0529  0.0789  95  HIS A C   
728  O O   . HIS A 107 ? 0.4255 0.5041 0.2316 0.1405  0.0443  0.0672  95  HIS A O   
729  C CB  . HIS A 107 ? 0.3824 0.4535 0.2424 0.1092  0.0323  0.0623  95  HIS A CB  
730  C CG  . HIS A 107 ? 0.3668 0.4364 0.2471 0.0973  0.0237  0.0613  95  HIS A CG  
731  N ND1 . HIS A 107 ? 0.4063 0.4758 0.2816 0.0963  0.0088  0.0558  95  HIS A ND1 
732  C CD2 . HIS A 107 ? 0.3415 0.4111 0.2465 0.0872  0.0280  0.0658  95  HIS A CD2 
733  C CE1 . HIS A 107 ? 0.3761 0.4477 0.2737 0.0865  0.0057  0.0582  95  HIS A CE1 
734  N NE2 . HIS A 107 ? 0.3557 0.4261 0.2696 0.0816  0.0172  0.0634  95  HIS A NE2 
735  N N   . GLY A 108 ? 0.3804 0.4733 0.2197 0.1334  0.0694  0.0932  96  GLY A N   
736  C CA  . GLY A 108 ? 0.4116 0.5123 0.2322 0.1480  0.0800  0.0968  96  GLY A CA  
737  C C   . GLY A 108 ? 0.4007 0.4971 0.2172 0.1508  0.0786  0.0837  96  GLY A C   
738  O O   . GLY A 108 ? 0.4263 0.5251 0.2170 0.1672  0.0827  0.0808  96  GLY A O   
739  N N   . LEU A 109 ? 0.3765 0.4660 0.2153 0.1370  0.0730  0.0758  97  LEU A N   
740  C CA  . LEU A 109 ? 0.3772 0.4597 0.2132 0.1387  0.0696  0.0629  97  LEU A CA  
741  C C   . LEU A 109 ? 0.4404 0.5350 0.2969 0.1367  0.0838  0.0721  97  LEU A C   
742  O O   . LEU A 109 ? 0.4046 0.5074 0.2867 0.1257  0.0905  0.0844  97  LEU A O   
743  C CB  . LEU A 109 ? 0.3638 0.4329 0.2132 0.1247  0.0545  0.0503  97  LEU A CB  
744  C CG  . LEU A 109 ? 0.3970 0.4548 0.2266 0.1268  0.0378  0.0390  97  LEU A CG  
745  C CD1 . LEU A 109 ? 0.4072 0.4578 0.2563 0.1115  0.0254  0.0328  97  LEU A CD1 
746  C CD2 . LEU A 109 ? 0.4450 0.4915 0.2450 0.1403  0.0321  0.0256  97  LEU A CD2 
747  N N   . ARG A 110 ? 0.4182 0.5126 0.2633 0.1474  0.0869  0.0655  98  ARG A N   
748  C CA  . ARG A 110 ? 0.4063 0.5131 0.2714 0.1462  0.0982  0.0724  98  ARG A CA  
749  C C   . ARG A 110 ? 0.4639 0.5605 0.3490 0.1323  0.0889  0.0623  98  ARG A C   
750  O O   . ARG A 110 ? 0.5411 0.6203 0.4141 0.1324  0.0762  0.0469  98  ARG A O   
751  C CB  . ARG A 110 ? 0.4992 0.6095 0.3396 0.1673  0.1053  0.0690  98  ARG A CB  
752  C CG  . ARG A 110 ? 0.6688 0.7963 0.5280 0.1699  0.1182  0.0777  98  ARG A CG  
753  C CD  . ARG A 110 ? 0.5882 0.7185 0.4233 0.1920  0.1241  0.0760  98  ARG A CD  
754  N NE  . ARG A 110 ? 0.7697 0.8764 0.5727 0.2039  0.1139  0.0550  98  ARG A NE  
755  C CZ  . ARG A 110 ? 0.9039 1.0018 0.7084 0.2066  0.1114  0.0448  98  ARG A CZ  
756  N NH1 . ARG A 110 ? 0.7562 0.8695 0.5925 0.1985  0.1185  0.0536  98  ARG A NH1 
757  N NH2 . ARG A 110 ? 0.8473 0.9184 0.6222 0.2163  0.0991  0.0256  98  ARG A NH2 
758  N N   . VAL A 111 ? 0.3398 0.4471 0.2553 0.1201  0.0946  0.0715  99  VAL A N   
759  C CA  . VAL A 111 ? 0.3529 0.4534 0.2867 0.1086  0.0874  0.0637  99  VAL A CA  
760  C C   . VAL A 111 ? 0.3367 0.4393 0.2655 0.1191  0.0907  0.0584  99  VAL A C   
761  O O   . VAL A 111 ? 0.3567 0.4770 0.2897 0.1276  0.1033  0.0685  99  VAL A O   
762  C CB  . VAL A 111 ? 0.2950 0.4052 0.2599 0.0932  0.0911  0.0745  99  VAL A CB  
763  C CG1 . VAL A 111 ? 0.3118 0.4167 0.2934 0.0832  0.0842  0.0668  99  VAL A CG1 
764  C CG2 . VAL A 111 ? 0.3346 0.4390 0.3025 0.0846  0.0877  0.0790  99  VAL A CG2 
765  N N   . ARG A 112 ? 0.3233 0.4085 0.2449 0.1186  0.0798  0.0440  100 ARG A N   
766  C CA  . ARG A 112 ? 0.3457 0.4281 0.2627 0.1281  0.0813  0.0378  100 ARG A CA  
767  C C   . ARG A 112 ? 0.3147 0.4019 0.2601 0.1152  0.0799  0.0398  100 ARG A C   
768  O O   . ARG A 112 ? 0.3217 0.4032 0.2809 0.1002  0.0722  0.0383  100 ARG A O   
769  C CB  . ARG A 112 ? 0.3767 0.4333 0.2681 0.1348  0.0686  0.0209  100 ARG A CB  
770  C CG  . ARG A 112 ? 0.5978 0.6457 0.4592 0.1448  0.0648  0.0162  100 ARG A CG  
771  C CD  . ARG A 112 ? 0.7630 0.8088 0.5953 0.1678  0.0715  0.0124  100 ARG A CD  
772  N NE  . ARG A 112 ? 0.9906 1.0076 0.7927 0.1752  0.0567  -0.0055 100 ARG A NE  
773  C CZ  . ARG A 112 ? 0.9480 0.9539 0.7274 0.1774  0.0468  -0.0120 100 ARG A CZ  
774  N NH1 . ARG A 112 ? 0.9232 0.9444 0.7051 0.1744  0.0512  -0.0017 100 ARG A NH1 
775  N NH2 . ARG A 112 ? 0.9448 0.9227 0.6988 0.1823  0.0310  -0.0291 100 ARG A NH2 
776  N N   . THR A 113 ? 0.3200 0.4194 0.2739 0.1222  0.0876  0.0438  101 THR A N   
777  C CA  . THR A 113 ? 0.2923 0.3988 0.2723 0.1112  0.0862  0.0465  101 THR A CA  
778  C C   . THR A 113 ? 0.3285 0.4200 0.3005 0.1177  0.0802  0.0355  101 THR A C   
779  O O   . THR A 113 ? 0.3529 0.4390 0.3055 0.1347  0.0836  0.0310  101 THR A O   
780  C CB  . THR A 113 ? 0.3289 0.4638 0.3294 0.1128  0.0986  0.0614  101 THR A CB  
781  O OG1 . THR A 113 ? 0.3530 0.4991 0.3600 0.1069  0.1040  0.0727  101 THR A OG1 
782  C CG2 . THR A 113 ? 0.3404 0.4829 0.3676 0.1000  0.0948  0.0639  101 THR A CG2 
783  N N   . ASP A 114 ? 0.3047 0.3886 0.2906 0.1054  0.0718  0.0318  102 ASP A N   
784  C CA  . ASP A 114 ? 0.3009 0.3723 0.2836 0.1105  0.0670  0.0244  102 ASP A CA  
785  C C   . ASP A 114 ? 0.2895 0.3731 0.2983 0.0994  0.0662  0.0301  102 ASP A C   
786  O O   . ASP A 114 ? 0.2912 0.3715 0.3102 0.0852  0.0599  0.0299  102 ASP A O   
787  C CB  . ASP A 114 ? 0.3126 0.3560 0.2800 0.1074  0.0542  0.0123  102 ASP A CB  
788  C CG  . ASP A 114 ? 0.3868 0.4127 0.3486 0.1135  0.0489  0.0050  102 ASP A CG  
789  O OD1 . ASP A 114 ? 0.3658 0.4027 0.3414 0.1156  0.0535  0.0100  102 ASP A OD1 
790  O OD2 . ASP A 114 ? 0.4740 0.4745 0.4183 0.1156  0.0391  -0.0052 102 ASP A OD2 
791  N N   . ALA A 115 ? 0.2993 0.3972 0.3174 0.1071  0.0724  0.0351  103 ALA A N   
792  C CA  . ALA A 115 ? 0.2973 0.4081 0.3387 0.0979  0.0706  0.0403  103 ALA A CA  
793  C C   . ALA A 115 ? 0.2942 0.3865 0.3352 0.0914  0.0604  0.0332  103 ALA A C   
794  O O   . ALA A 115 ? 0.2575 0.3579 0.3150 0.0816  0.0571  0.0366  103 ALA A O   
795  C CB  . ALA A 115 ? 0.3246 0.4525 0.3730 0.1106  0.0781  0.0461  103 ALA A CB  
796  N N   . ARG A 116 ? 0.2662 0.3337 0.2886 0.0967  0.0548  0.0239  104 ARG A N   
797  C CA  . ARG A 116 ? 0.3006 0.3516 0.3250 0.0892  0.0454  0.0196  104 ARG A CA  
798  C C   . ARG A 116 ? 0.2586 0.3096 0.2910 0.0736  0.0401  0.0206  104 ARG A C   
799  O O   . ARG A 116 ? 0.2579 0.3023 0.2966 0.0666  0.0341  0.0204  104 ARG A O   
800  C CB  . ARG A 116 ? 0.3101 0.3331 0.3143 0.0966  0.0391  0.0102  104 ARG A CB  
801  C CG  . ARG A 116 ? 0.3549 0.3723 0.3502 0.1135  0.0431  0.0083  104 ARG A CG  
802  C CD  . ARG A 116 ? 0.3927 0.3777 0.3633 0.1225  0.0360  -0.0028 104 ARG A CD  
803  N NE  . ARG A 116 ? 0.3965 0.3762 0.3486 0.1263  0.0359  -0.0083 104 ARG A NE  
804  C CZ  . ARG A 116 ? 0.4185 0.3734 0.3441 0.1381  0.0313  -0.0189 104 ARG A CZ  
805  N NH1 . ARG A 116 ? 0.4870 0.4184 0.4012 0.1482  0.0271  -0.0252 104 ARG A NH1 
806  N NH2 . ARG A 116 ? 0.4734 0.4259 0.3819 0.1409  0.0305  -0.0232 104 ARG A NH2 
807  N N   . LEU A 117 ? 0.2519 0.3110 0.2843 0.0693  0.0430  0.0228  105 LEU A N   
808  C CA  . LEU A 117 ? 0.2443 0.3043 0.2837 0.0569  0.0393  0.0244  105 LEU A CA  
809  C C   . LEU A 117 ? 0.2187 0.2948 0.2752 0.0495  0.0414  0.0306  105 LEU A C   
810  O O   . LEU A 117 ? 0.2332 0.3092 0.2936 0.0410  0.0391  0.0317  105 LEU A O   
811  C CB  . LEU A 117 ? 0.2476 0.3061 0.2775 0.0566  0.0406  0.0240  105 LEU A CB  
812  C CG  . LEU A 117 ? 0.2471 0.2885 0.2580 0.0631  0.0359  0.0166  105 LEU A CG  
813  C CD1 . LEU A 117 ? 0.2937 0.3376 0.2938 0.0653  0.0385  0.0175  105 LEU A CD1 
814  C CD2 . LEU A 117 ? 0.2574 0.2853 0.2700 0.0548  0.0258  0.0130  105 LEU A CD2 
815  N N   . ARG A 118 ? 0.2269 0.3165 0.2929 0.0531  0.0451  0.0345  106 ARG A N   
816  C CA  . ARG A 118 ? 0.2165 0.3204 0.2983 0.0453  0.0446  0.0396  106 ARG A CA  
817  C C   . ARG A 118 ? 0.2229 0.3202 0.3070 0.0385  0.0377  0.0373  106 ARG A C   
818  O O   . ARG A 118 ? 0.2143 0.3000 0.2923 0.0407  0.0343  0.0341  106 ARG A O   
819  C CB  . ARG A 118 ? 0.1995 0.3207 0.2921 0.0511  0.0484  0.0447  106 ARG A CB  
820  C CG  . ARG A 118 ? 0.2121 0.3273 0.3017 0.0586  0.0459  0.0420  106 ARG A CG  
821  C CD  . ARG A 118 ? 0.2330 0.3680 0.3333 0.0670  0.0508  0.0482  106 ARG A CD  
822  N NE  . ARG A 118 ? 0.2125 0.3412 0.3095 0.0759  0.0490  0.0466  106 ARG A NE  
823  C CZ  . ARG A 118 ? 0.2678 0.3822 0.3508 0.0884  0.0515  0.0427  106 ARG A CZ  
824  N NH1 . ARG A 118 ? 0.2754 0.3812 0.3446 0.0943  0.0555  0.0391  106 ARG A NH1 
825  N NH2 . ARG A 118 ? 0.2853 0.3926 0.3666 0.0960  0.0495  0.0423  106 ARG A NH2 
826  N N   . GLU A 119 ? 0.2024 0.3064 0.2950 0.0305  0.0353  0.0393  107 GLU A N   
827  C CA  . GLU A 119 ? 0.2163 0.3161 0.3089 0.0266  0.0296  0.0375  107 GLU A CA  
828  C C   . GLU A 119 ? 0.1870 0.2921 0.2834 0.0314  0.0279  0.0386  107 GLU A C   
829  O O   . GLU A 119 ? 0.1983 0.3139 0.3009 0.0364  0.0304  0.0414  107 GLU A O   
830  C CB  . GLU A 119 ? 0.2260 0.3294 0.3239 0.0186  0.0265  0.0381  107 GLU A CB  
831  C CG  . GLU A 119 ? 0.1934 0.2911 0.2867 0.0163  0.0207  0.0352  107 GLU A CG  
832  C CD  . GLU A 119 ? 0.2088 0.2951 0.2920 0.0184  0.0212  0.0336  107 GLU A CD  
833  O OE1 . GLU A 119 ? 0.2097 0.2931 0.2909 0.0223  0.0226  0.0343  107 GLU A OE1 
834  O OE2 . GLU A 119 ? 0.2327 0.3127 0.3102 0.0164  0.0196  0.0319  107 GLU A OE2 
835  N N   . VAL A 120 ? 0.1861 0.2850 0.2786 0.0309  0.0241  0.0377  108 VAL A N   
836  C CA  . VAL A 120 ? 0.2043 0.3089 0.3002 0.0352  0.0219  0.0401  108 VAL A CA  
837  C C   . VAL A 120 ? 0.2120 0.3335 0.3182 0.0334  0.0197  0.0421  108 VAL A C   
838  O O   . VAL A 120 ? 0.2100 0.3346 0.3189 0.0263  0.0168  0.0410  108 VAL A O   
839  C CB  . VAL A 120 ? 0.2170 0.3152 0.3073 0.0345  0.0187  0.0406  108 VAL A CB  
840  C CG1 . VAL A 120 ? 0.2376 0.3373 0.3249 0.0292  0.0157  0.0385  108 VAL A CG1 
841  C CG2 . VAL A 120 ? 0.2296 0.3327 0.3220 0.0400  0.0169  0.0444  108 VAL A CG2 
842  N N   A ARG A 121 ? 0.1864 0.3183 0.2991 0.0397  0.0202  0.0456  109 ARG A N   
843  N N   B ARG A 121 ? 0.1863 0.3182 0.2989 0.0396  0.0200  0.0456  109 ARG A N   
844  C CA  A ARG A 121 ? 0.1777 0.3286 0.3025 0.0375  0.0162  0.0487  109 ARG A CA  
845  C CA  B ARG A 121 ? 0.1776 0.3287 0.3026 0.0372  0.0163  0.0487  109 ARG A CA  
846  C C   A ARG A 121 ? 0.1805 0.3296 0.3007 0.0325  0.0084  0.0462  109 ARG A C   
847  C C   B ARG A 121 ? 0.1786 0.3295 0.3000 0.0330  0.0082  0.0467  109 ARG A C   
848  O O   A ARG A 121 ? 0.1826 0.3220 0.2925 0.0359  0.0076  0.0454  109 ARG A O   
849  O O   B ARG A 121 ? 0.2033 0.3470 0.3158 0.0374  0.0071  0.0466  109 ARG A O   
850  C CB  A ARG A 121 ? 0.1816 0.3434 0.3124 0.0473  0.0177  0.0535  109 ARG A CB  
851  C CB  B ARG A 121 ? 0.1909 0.3550 0.3237 0.0468  0.0187  0.0538  109 ARG A CB  
852  C CG  A ARG A 121 ? 0.1973 0.3829 0.3435 0.0456  0.0131  0.0581  109 ARG A CG  
853  C CG  B ARG A 121 ? 0.2116 0.4006 0.3617 0.0438  0.0150  0.0588  109 ARG A CG  
854  C CD  A ARG A 121 ? 0.1941 0.3982 0.3551 0.0482  0.0189  0.0640  109 ARG A CD  
855  C CD  B ARG A 121 ? 0.2369 0.4415 0.3950 0.0546  0.0158  0.0649  109 ARG A CD  
856  N NE  A ARG A 121 ? 0.1916 0.4215 0.3701 0.0476  0.0137  0.0703  109 ARG A NE  
857  N NE  B ARG A 121 ? 0.3160 0.5063 0.4618 0.0624  0.0153  0.0637  109 ARG A NE  
858  C CZ  A ARG A 121 ? 0.1818 0.4357 0.3780 0.0508  0.0178  0.0785  109 ARG A CZ  
859  C CZ  B ARG A 121 ? 0.2806 0.4799 0.4295 0.0704  0.0129  0.0684  109 ARG A CZ  
860  N NH1 A ARG A 121 ? 0.2516 0.5069 0.4485 0.0559  0.0282  0.0813  109 ARG A NH1 
861  N NH1 B ARG A 121 ? 0.2154 0.4405 0.3800 0.0720  0.0099  0.0742  109 ARG A NH1 
862  N NH2 A ARG A 121 ? 0.1775 0.4566 0.3910 0.0500  0.0115  0.0849  109 ARG A NH2 
863  N NH2 B ARG A 121 ? 0.3780 0.5610 0.5155 0.0771  0.0136  0.0686  109 ARG A NH2 
864  N N   . THR A 122 ? 0.2324 0.3903 0.3597 0.0247  0.0022  0.0454  110 THR A N   
865  C CA  . THR A 122 ? 0.1963 0.3503 0.3157 0.0211  -0.0066 0.0412  110 THR A CA  
866  C C   . THR A 122 ? 0.1811 0.3531 0.3103 0.0200  -0.0155 0.0433  110 THR A C   
867  O O   . THR A 122 ? 0.2085 0.3987 0.3545 0.0199  -0.0149 0.0490  110 THR A O   
868  C CB  . THR A 122 ? 0.2084 0.3514 0.3242 0.0121  -0.0096 0.0363  110 THR A CB  
869  O OG1 . THR A 122 ? 0.1946 0.3497 0.3278 0.0040  -0.0118 0.0395  110 THR A OG1 
870  C CG2 . THR A 122 ? 0.2387 0.3662 0.3456 0.0132  -0.0017 0.0348  110 THR A CG2 
871  N N   . ASN A 123 ? 0.2071 0.3402 0.3329 0.0009  -0.0147 0.0559  111 ASN A N   
872  C CA  . ASN A 123 ? 0.2348 0.3916 0.3772 -0.0071 -0.0229 0.0519  111 ASN A CA  
873  C C   . ASN A 123 ? 0.2144 0.3780 0.3741 -0.0158 -0.0120 0.0441  111 ASN A C   
874  O O   . ASN A 123 ? 0.1942 0.3828 0.3804 -0.0181 -0.0154 0.0416  111 ASN A O   
875  C CB  . ASN A 123 ? 0.2154 0.3707 0.3402 -0.0165 -0.0304 0.0486  111 ASN A CB  
876  C CG  . ASN A 123 ? 0.3069 0.4634 0.4194 -0.0105 -0.0436 0.0557  111 ASN A CG  
877  O OD1 . ASN A 123 ? 0.3373 0.4902 0.4511 0.0012  -0.0452 0.0633  111 ASN A OD1 
878  N ND2 . ASN A 123 ? 0.2934 0.4514 0.3906 -0.0195 -0.0512 0.0527  111 ASN A ND2 
879  N N   . TRP A 124 ? 0.2010 0.3423 0.3470 -0.0204 0.0022  0.0404  112 TRP A N   
880  C CA  . TRP A 124 ? 0.2289 0.3701 0.3873 -0.0299 0.0162  0.0328  112 TRP A CA  
881  C C   . TRP A 124 ? 0.2240 0.3733 0.4034 -0.0237 0.0232  0.0345  112 TRP A C   
882  O O   . TRP A 124 ? 0.1977 0.3662 0.4027 -0.0316 0.0275  0.0279  112 TRP A O   
883  C CB  . TRP A 124 ? 0.2519 0.3611 0.3867 -0.0323 0.0315  0.0315  112 TRP A CB  
884  C CG  . TRP A 124 ? 0.2332 0.3339 0.3743 -0.0437 0.0496  0.0235  112 TRP A CG  
885  C CD1 . TRP A 124 ? 0.2374 0.3602 0.4042 -0.0567 0.0522  0.0142  112 TRP A CD1 
886  C CD2 . TRP A 124 ? 0.2744 0.3416 0.3955 -0.0431 0.0683  0.0245  112 TRP A CD2 
887  N NE1 . TRP A 124 ? 0.2832 0.3854 0.4461 -0.0662 0.0737  0.0079  112 TRP A NE1 
888  C CE2 . TRP A 124 ? 0.2773 0.3431 0.4102 -0.0571 0.0838  0.0151  112 TRP A CE2 
889  C CE3 . TRP A 124 ? 0.3060 0.3452 0.4007 -0.0317 0.0732  0.0327  112 TRP A CE3 
890  C CZ2 . TRP A 124 ? 0.3062 0.3380 0.4218 -0.0595 0.1058  0.0148  112 TRP A CZ2 
891  C CZ3 . TRP A 124 ? 0.3259 0.3344 0.4044 -0.0321 0.0927  0.0334  112 TRP A CZ3 
892  C CH2 . TRP A 124 ? 0.3291 0.3315 0.4162 -0.0456 0.1095  0.0250  112 TRP A CH2 
893  N N   . ASP A 125 ? 0.2222 0.3578 0.3918 -0.0108 0.0253  0.0421  113 ASP A N   
894  C CA  . ASP A 125 ? 0.2259 0.3659 0.4126 -0.0047 0.0335  0.0434  113 ASP A CA  
895  C C   . ASP A 125 ? 0.2075 0.3811 0.4277 -0.0023 0.0233  0.0434  113 ASP A C   
896  O O   . ASP A 125 ? 0.2171 0.4032 0.4633 -0.0019 0.0324  0.0406  113 ASP A O   
897  C CB  . ASP A 125 ? 0.2290 0.3497 0.3959 0.0074  0.0343  0.0507  113 ASP A CB  
898  C CG  . ASP A 125 ? 0.2646 0.3566 0.4012 0.0077  0.0432  0.0521  113 ASP A CG  
899  O OD1 . ASP A 125 ? 0.2561 0.3362 0.3868 0.0010  0.0548  0.0486  113 ASP A OD1 
900  O OD2 . ASP A 125 ? 0.2885 0.3694 0.4061 0.0150  0.0382  0.0569  113 ASP A OD2 
901  N N   . ASP A 126 ? 0.1816 0.3699 0.4015 0.0000  0.0050  0.0470  114 ASP A N   
902  C CA  . ASP A 126 ? 0.1955 0.4165 0.4445 0.0051  -0.0080 0.0497  114 ASP A CA  
903  C C   . ASP A 126 ? 0.2259 0.4781 0.4969 -0.0081 -0.0155 0.0414  114 ASP A C   
904  O O   . ASP A 126 ? 0.2205 0.5058 0.5172 -0.0040 -0.0295 0.0437  114 ASP A O   
905  C CB  . ASP A 126 ? 0.2222 0.4405 0.4546 0.0145  -0.0242 0.0590  114 ASP A CB  
906  C CG  . ASP A 126 ? 0.2338 0.4318 0.4568 0.0286  -0.0186 0.0668  114 ASP A CG  
907  O OD1 . ASP A 126 ? 0.3037 0.4931 0.5348 0.0320  -0.0038 0.0654  114 ASP A OD1 
908  O OD2 . ASP A 126 ? 0.2431 0.4323 0.4488 0.0349  -0.0277 0.0736  114 ASP A OD2 
909  N N   . GLY A 127 ? 0.1856 0.4282 0.4467 -0.0237 -0.0065 0.0318  115 GLY A N   
910  C CA  . GLY A 127 ? 0.2286 0.4995 0.5081 -0.0400 -0.0123 0.0213  115 GLY A CA  
911  C C   . GLY A 127 ? 0.2251 0.5073 0.4895 -0.0450 -0.0326 0.0217  115 GLY A C   
912  O O   . GLY A 127 ? 0.2435 0.5601 0.5274 -0.0554 -0.0449 0.0151  115 GLY A O   
913  N N   . ARG A 128 ? 0.2280 0.4834 0.4580 -0.0391 -0.0365 0.0285  116 ARG A N   
914  C CA  . ARG A 128 ? 0.2519 0.5114 0.4616 -0.0448 -0.0525 0.0286  116 ARG A CA  
915  C C   . ARG A 128 ? 0.2730 0.5015 0.4517 -0.0563 -0.0416 0.0220  116 ARG A C   
916  O O   . ARG A 128 ? 0.2933 0.4935 0.4616 -0.0529 -0.0248 0.0227  116 ARG A O   
917  C CB  . ARG A 128 ? 0.3196 0.5733 0.5153 -0.0281 -0.0651 0.0424  116 ARG A CB  
918  C CG  . ARG A 128 ? 0.3335 0.6172 0.5589 -0.0153 -0.0767 0.0501  116 ARG A CG  
919  C CD  . ARG A 128 ? 0.4565 0.7212 0.6731 0.0037  -0.0753 0.0629  116 ARG A CD  
920  N NE  . ARG A 128 ? 0.5348 0.7788 0.7162 0.0053  -0.0827 0.0687  116 ARG A NE  
921  C CZ  . ARG A 128 ? 0.6540 0.8692 0.8158 0.0142  -0.0756 0.0749  116 ARG A CZ  
922  N NH1 . ARG A 128 ? 0.4243 0.6265 0.5941 0.0215  -0.0617 0.0758  116 ARG A NH1 
923  N NH2 . ARG A 128 ? 0.7146 0.9137 0.8471 0.0143  -0.0817 0.0794  116 ARG A NH2 
924  N N   . PRO A 129 ? 0.2870 0.5199 0.4498 -0.0696 -0.0502 0.0157  117 PRO A N   
925  C CA  . PRO A 129 ? 0.2694 0.4699 0.4015 -0.0786 -0.0386 0.0102  117 PRO A CA  
926  C C   . PRO A 129 ? 0.2935 0.4659 0.4047 -0.0635 -0.0345 0.0205  117 PRO A C   
927  O O   . PRO A 129 ? 0.2707 0.4478 0.3794 -0.0511 -0.0459 0.0306  117 PRO A O   
928  C CB  . PRO A 129 ? 0.3035 0.5163 0.4199 -0.0923 -0.0529 0.0042  117 PRO A CB  
929  C CG  . PRO A 129 ? 0.3708 0.6271 0.5156 -0.0966 -0.0694 0.0018  117 PRO A CG  
930  C CD  . PRO A 129 ? 0.3182 0.5860 0.4892 -0.0764 -0.0715 0.0137  117 PRO A CD  
931  N N   . SER A 130 ? 0.2569 0.4002 0.3538 -0.0646 -0.0175 0.0180  118 SER A N   
932  C CA  . SER A 130 ? 0.2717 0.3924 0.3501 -0.0528 -0.0141 0.0256  118 SER A CA  
933  C C   . SER A 130 ? 0.3277 0.4422 0.3835 -0.0592 -0.0202 0.0236  118 SER A C   
934  O O   . SER A 130 ? 0.3359 0.4524 0.3836 -0.0746 -0.0203 0.0142  118 SER A O   
935  C CB  . SER A 130 ? 0.3022 0.3966 0.3739 -0.0508 0.0050  0.0242  118 SER A CB  
936  O OG  . SER A 130 ? 0.2720 0.3676 0.3589 -0.0449 0.0121  0.0267  118 SER A OG  
937  N N   . GLU A 131 ? 0.2760 0.3817 0.3201 -0.0488 -0.0239 0.0314  119 GLU A N   
938  C CA  . GLU A 131 ? 0.3279 0.4245 0.3487 -0.0545 -0.0270 0.0298  119 GLU A CA  
939  C C   . GLU A 131 ? 0.3369 0.4125 0.3479 -0.0465 -0.0163 0.0327  119 GLU A C   
940  O O   . GLU A 131 ? 0.3340 0.4095 0.3533 -0.0340 -0.0162 0.0397  119 GLU A O   
941  C CB  . GLU A 131 ? 0.3826 0.4924 0.3978 -0.0505 -0.0443 0.0372  119 GLU A CB  
942  C CG  . GLU A 131 ? 0.4502 0.5876 0.4784 -0.0549 -0.0593 0.0368  119 GLU A CG  
943  C CD  . GLU A 131 ? 0.5923 0.7395 0.6137 -0.0466 -0.0759 0.0473  119 GLU A CD  
944  O OE1 . GLU A 131 ? 0.6381 0.7666 0.6371 -0.0430 -0.0746 0.0521  119 GLU A OE1 
945  O OE2 . GLU A 131 ? 0.8293 1.0023 0.8685 -0.0430 -0.0891 0.0510  119 GLU A OE2 
946  N N   . LEU A 132 ? 0.3214 0.3808 0.3155 -0.0543 -0.0072 0.0265  120 LEU A N   
947  C CA  . LEU A 132 ? 0.3568 0.4012 0.3441 -0.0472 0.0018  0.0287  120 LEU A CA  
948  C C   . LEU A 132 ? 0.3776 0.4233 0.3523 -0.0461 -0.0069 0.0331  120 LEU A C   
949  O O   . LEU A 132 ? 0.3991 0.4428 0.3551 -0.0563 -0.0120 0.0302  120 LEU A O   
950  C CB  . LEU A 132 ? 0.3655 0.3906 0.3413 -0.0554 0.0176  0.0201  120 LEU A CB  
951  C CG  . LEU A 132 ? 0.4361 0.4487 0.4084 -0.0487 0.0281  0.0211  120 LEU A CG  
952  C CD1 . LEU A 132 ? 0.3876 0.4037 0.3782 -0.0327 0.0311  0.0280  120 LEU A CD1 
953  C CD2 . LEU A 132 ? 0.4602 0.4526 0.4209 -0.0571 0.0450  0.0122  120 LEU A CD2 
954  N N   . LYS A 133 ? 0.3143 0.3617 0.2966 -0.0347 -0.0081 0.0398  121 LYS A N   
955  C CA  . LYS A 133 ? 0.3325 0.3774 0.3024 -0.0340 -0.0136 0.0441  121 LYS A CA  
956  C C   . LYS A 133 ? 0.3252 0.3574 0.2879 -0.0352 -0.0015 0.0406  121 LYS A C   
957  O O   . LYS A 133 ? 0.3144 0.3454 0.2895 -0.0306 0.0083  0.0380  121 LYS A O   
958  C CB  . LYS A 133 ? 0.3283 0.3813 0.3108 -0.0230 -0.0199 0.0518  121 LYS A CB  
959  C CG  . LYS A 133 ? 0.3605 0.4269 0.3513 -0.0201 -0.0319 0.0567  121 LYS A CG  
960  C CD  . LYS A 133 ? 0.4394 0.5084 0.4137 -0.0277 -0.0419 0.0573  121 LYS A CD  
961  C CE  . LYS A 133 ? 0.5345 0.6165 0.5151 -0.0205 -0.0554 0.0659  121 LYS A CE  
962  N NZ  . LYS A 133 ? 0.5165 0.6010 0.4763 -0.0272 -0.0670 0.0677  121 LYS A NZ  
963  N N   . PRO A 134 ? 0.3115 0.3344 0.2546 -0.0406 -0.0018 0.0411  122 PRO A N   
964  C CA  . PRO A 134 ? 0.3592 0.3718 0.2988 -0.0421 0.0111  0.0373  122 PRO A CA  
965  C C   . PRO A 134 ? 0.3467 0.3685 0.3073 -0.0323 0.0129  0.0399  122 PRO A C   
966  O O   . PRO A 134 ? 0.3083 0.3383 0.2771 -0.0259 0.0041  0.0455  122 PRO A O   
967  C CB  . PRO A 134 ? 0.3966 0.3963 0.3085 -0.0493 0.0090  0.0395  122 PRO A CB  
968  C CG  . PRO A 134 ? 0.4337 0.4366 0.3305 -0.0535 -0.0051 0.0426  122 PRO A CG  
969  C CD  . PRO A 134 ? 0.3361 0.3578 0.2592 -0.0448 -0.0138 0.0458  122 PRO A CD  
970  N N   . HIS A 135 ? 0.3217 0.3429 0.2913 -0.0319 0.0250  0.0349  123 HIS A N   
971  C CA  . HIS A 135 ? 0.3336 0.3665 0.3217 -0.0254 0.0258  0.0355  123 HIS A CA  
972  C C   . HIS A 135 ? 0.3360 0.3640 0.3133 -0.0282 0.0213  0.0389  123 HIS A C   
973  O O   . HIS A 135 ? 0.3602 0.3728 0.3155 -0.0358 0.0241  0.0393  123 HIS A O   
974  C CB  . HIS A 135 ? 0.3433 0.3795 0.3438 -0.0260 0.0394  0.0289  123 HIS A CB  
975  C CG  . HIS A 135 ? 0.3342 0.3866 0.3539 -0.0223 0.0390  0.0277  123 HIS A CG  
976  N ND1 . HIS A 135 ? 0.4004 0.4506 0.4182 -0.0300 0.0466  0.0231  123 HIS A ND1 
977  C CD2 . HIS A 135 ? 0.3234 0.3939 0.3617 -0.0135 0.0316  0.0299  123 HIS A CD2 
978  C CE1 . HIS A 135 ? 0.4094 0.4780 0.4467 -0.0271 0.0438  0.0213  123 HIS A CE1 
979  N NE2 . HIS A 135 ? 0.3157 0.3973 0.3646 -0.0168 0.0339  0.0255  123 HIS A NE2 
980  N N   . GLY A 136 ? 0.3096 0.3481 0.3000 -0.0219 0.0155  0.0417  124 GLY A N   
981  C CA  . GLY A 136 ? 0.3419 0.3735 0.3243 -0.0235 0.0137  0.0446  124 GLY A CA  
982  C C   . GLY A 136 ? 0.3322 0.3567 0.3029 -0.0199 0.0038  0.0529  124 GLY A C   
983  O O   . GLY A 136 ? 0.3421 0.3577 0.3058 -0.0189 0.0034  0.0568  124 GLY A O   
984  N N   . VAL A 137 ? 0.3092 0.3378 0.2791 -0.0178 -0.0033 0.0554  125 VAL A N   
985  C CA  . VAL A 137 ? 0.3196 0.3480 0.2842 -0.0137 -0.0139 0.0630  125 VAL A CA  
986  C C   . VAL A 137 ? 0.2938 0.3362 0.2790 -0.0063 -0.0181 0.0640  125 VAL A C   
987  O O   . VAL A 137 ? 0.2845 0.3347 0.2792 -0.0065 -0.0170 0.0604  125 VAL A O   
988  C CB  . VAL A 137 ? 0.3186 0.3450 0.2681 -0.0191 -0.0195 0.0637  125 VAL A CB  
989  C CG1 . VAL A 137 ? 0.3626 0.3977 0.3143 -0.0133 -0.0330 0.0715  125 VAL A CG1 
990  C CG2 . VAL A 137 ? 0.3684 0.3769 0.2914 -0.0269 -0.0141 0.0632  125 VAL A CG2 
991  N N   . TYR A 138 ? 0.3004 0.3425 0.2904 0.0000  -0.0209 0.0688  126 TYR A N   
992  C CA  . TYR A 138 ? 0.2631 0.3153 0.2703 0.0062  -0.0222 0.0691  126 TYR A CA  
993  C C   . TYR A 138 ? 0.2456 0.3081 0.2603 0.0074  -0.0287 0.0709  126 TYR A C   
994  O O   . TYR A 138 ? 0.2890 0.3533 0.2993 0.0080  -0.0361 0.0757  126 TYR A O   
995  C CB  . TYR A 138 ? 0.2796 0.3251 0.2876 0.0117  -0.0212 0.0733  126 TYR A CB  
996  C CG  . TYR A 138 ? 0.2460 0.2979 0.2676 0.0165  -0.0192 0.0720  126 TYR A CG  
997  C CD1 . TYR A 138 ? 0.2668 0.3224 0.2916 0.0147  -0.0150 0.0661  126 TYR A CD1 
998  C CD2 . TYR A 138 ? 0.2649 0.3201 0.2963 0.0233  -0.0216 0.0767  126 TYR A CD2 
999  C CE1 . TYR A 138 ? 0.2324 0.2910 0.2636 0.0185  -0.0130 0.0651  126 TYR A CE1 
1000 C CE2 . TYR A 138 ? 0.2390 0.2968 0.2801 0.0267  -0.0173 0.0748  126 TYR A CE2 
1001 C CZ  . TYR A 138 ? 0.2211 0.2789 0.2594 0.0238  -0.0130 0.0691  126 TYR A CZ  
1002 O OH  . TYR A 138 ? 0.2383 0.2959 0.2804 0.0265  -0.0087 0.0677  126 TYR A OH  
1003 N N   . PRO A 139 ? 0.2342 0.3039 0.2597 0.0074  -0.0260 0.0672  127 PRO A N   
1004 C CA  . PRO A 139 ? 0.2378 0.3164 0.2701 0.0045  -0.0294 0.0661  127 PRO A CA  
1005 C C   . PRO A 139 ? 0.2591 0.3470 0.3082 0.0097  -0.0303 0.0681  127 PRO A C   
1006 O O   . PRO A 139 ? 0.2877 0.3849 0.3459 0.0058  -0.0313 0.0656  127 PRO A O   
1007 C CB  . PRO A 139 ? 0.2673 0.3419 0.2984 0.0008  -0.0216 0.0604  127 PRO A CB  
1008 C CG  . PRO A 139 ? 0.2616 0.3329 0.2950 0.0068  -0.0166 0.0608  127 PRO A CG  
1009 C CD  . PRO A 139 ? 0.2366 0.3048 0.2641 0.0078  -0.0191 0.0630  127 PRO A CD  
1010 N N   . PHE A 140 ? 0.2386 0.3239 0.2925 0.0168  -0.0283 0.0714  128 PHE A N   
1011 C CA  . PHE A 140 ? 0.2392 0.3307 0.3087 0.0212  -0.0252 0.0719  128 PHE A CA  
1012 C C   . PHE A 140 ? 0.2331 0.3292 0.3123 0.0281  -0.0290 0.0776  128 PHE A C   
1013 O O   . PHE A 140 ? 0.2444 0.3319 0.3144 0.0316  -0.0309 0.0819  128 PHE A O   
1014 C CB  . PHE A 140 ? 0.2235 0.3061 0.2897 0.0240  -0.0169 0.0701  128 PHE A CB  
1015 C CG  . PHE A 140 ? 0.2232 0.3014 0.2803 0.0210  -0.0139 0.0668  128 PHE A CG  
1016 C CD1 . PHE A 140 ? 0.2287 0.3076 0.2883 0.0179  -0.0105 0.0646  128 PHE A CD1 
1017 C CD2 . PHE A 140 ? 0.2311 0.3046 0.2788 0.0214  -0.0135 0.0658  128 PHE A CD2 
1018 C CE1 . PHE A 140 ? 0.2342 0.3067 0.2859 0.0178  -0.0063 0.0630  128 PHE A CE1 
1019 C CE2 . PHE A 140 ? 0.2418 0.3146 0.2851 0.0211  -0.0112 0.0637  128 PHE A CE2 
1020 C CZ  . PHE A 140 ? 0.2603 0.3314 0.3054 0.0207  -0.0073 0.0632  128 PHE A CZ  
1021 N N   . PRO A 141 ? 0.2175 0.3264 0.3166 0.0308  -0.0284 0.0780  129 PRO A N   
1022 C CA  . PRO A 141 ? 0.2155 0.3302 0.3286 0.0402  -0.0305 0.0841  129 PRO A CA  
1023 C C   . PRO A 141 ? 0.2457 0.3449 0.3572 0.0468  -0.0198 0.0852  129 PRO A C   
1024 O O   . PRO A 141 ? 0.2789 0.3750 0.3958 0.0556  -0.0197 0.0912  129 PRO A O   
1025 C CB  . PRO A 141 ? 0.2142 0.3516 0.3534 0.0393  -0.0319 0.0820  129 PRO A CB  
1026 C CG  . PRO A 141 ? 0.2053 0.3392 0.3415 0.0301  -0.0239 0.0742  129 PRO A CG  
1027 C CD  . PRO A 141 ? 0.2273 0.3470 0.3384 0.0246  -0.0256 0.0726  129 PRO A CD  
1028 N N   . GLU A 142 ? 0.2359 0.3238 0.3381 0.0432  -0.0108 0.0799  130 GLU A N   
1029 C CA  . GLU A 142 ? 0.2477 0.3196 0.3432 0.0467  -0.0010 0.0791  130 GLU A CA  
1030 C C   . GLU A 142 ? 0.2458 0.3038 0.3211 0.0439  -0.0022 0.0788  130 GLU A C   
1031 O O   . GLU A 142 ? 0.2733 0.3316 0.3371 0.0375  -0.0052 0.0752  130 GLU A O   
1032 C CB  . GLU A 142 ? 0.2261 0.2929 0.3166 0.0431  0.0079  0.0735  130 GLU A CB  
1033 C CG  . GLU A 142 ? 0.2503 0.3001 0.3290 0.0440  0.0179  0.0707  130 GLU A CG  
1034 C CD  . GLU A 142 ? 0.2345 0.2783 0.3028 0.0406  0.0254  0.0661  130 GLU A CD  
1035 O OE1 . GLU A 142 ? 0.2383 0.2881 0.3064 0.0382  0.0235  0.0658  130 GLU A OE1 
1036 O OE2 . GLU A 142 ? 0.2915 0.3215 0.3483 0.0398  0.0342  0.0627  130 GLU A OE2 
1037 N N   . PRO A 143 ? 0.2681 0.3130 0.3395 0.0484  0.0017  0.0820  131 PRO A N   
1038 C CA  . PRO A 143 ? 0.2760 0.3070 0.3286 0.0437  0.0022  0.0807  131 PRO A CA  
1039 C C   . PRO A 143 ? 0.2732 0.3002 0.3136 0.0350  0.0065  0.0718  131 PRO A C   
1040 O O   . PRO A 143 ? 0.2681 0.2934 0.3082 0.0343  0.0124  0.0675  131 PRO A O   
1041 C CB  . PRO A 143 ? 0.3308 0.3437 0.3819 0.0506  0.0103  0.0853  131 PRO A CB  
1042 C CG  . PRO A 143 ? 0.3682 0.3926 0.4408 0.0620  0.0079  0.0926  131 PRO A CG  
1043 C CD  . PRO A 143 ? 0.2737 0.3159 0.3595 0.0588  0.0066  0.0876  131 PRO A CD  
1044 N N   . GLU A 144 ? 0.2544 0.3276 0.2820 0.0372  0.0199  0.0560  132 GLU A N   
1045 C CA  . GLU A 144 ? 0.2513 0.3266 0.2822 0.0316  0.0235  0.0493  132 GLU A CA  
1046 C C   . GLU A 144 ? 0.2523 0.2830 0.2872 0.0240  0.0195  0.0583  132 GLU A C   
1047 O O   . GLU A 144 ? 0.2552 0.2683 0.2933 0.0258  0.0214  0.0455  132 GLU A O   
1048 C CB  . GLU A 144 ? 0.3214 0.4545 0.3479 0.0234  0.0264  0.0599  132 GLU A CB  
1049 C CG  . GLU A 144 ? 0.3253 0.4714 0.3570 0.0185  0.0302  0.0534  132 GLU A CG  
1050 C CD  . GLU A 144 ? 0.3112 0.5338 0.3404 0.0127  0.0345  0.0651  132 GLU A CD  
1051 O OE1 . GLU A 144 ? 0.4104 0.6846 0.4320 0.0116  0.0350  0.0807  132 GLU A OE1 
1052 O OE2 . GLU A 144 ? 0.4165 0.6542 0.4518 0.0093  0.0375  0.0600  132 GLU A OE2 
1053 N N   . LYS A 145 ? 0.2816 0.2931 0.3187 0.0165  0.0091  0.0793  133 LYS A N   
1054 C CA  . LYS A 145 ? 0.3618 0.3277 0.4062 0.0134  -0.0039 0.0824  133 LYS A CA  
1055 C C   . LYS A 145 ? 0.3254 0.2623 0.3672 0.0331  -0.0020 0.0574  133 LYS A C   
1056 O O   . LYS A 145 ? 0.3533 0.2676 0.3961 0.0365  -0.0070 0.0464  133 LYS A O   
1057 C CB  . LYS A 145 ? 0.3697 0.3162 0.4248 0.0039  -0.0249 0.1083  133 LYS A CB  
1058 C CG  . LYS A 145 ? 0.6262 0.5519 0.6975 -0.0142 -0.0463 0.1291  133 LYS A CG  
1059 C CD  . LYS A 145 ? 0.7267 0.6279 0.8179 -0.0257 -0.0769 0.1591  133 LYS A CD  
1060 C CE  . LYS A 145 ? 0.7690 0.6534 0.8860 -0.0505 -0.1066 0.1904  133 LYS A CE  
1061 N NZ  . LYS A 145 ? 0.8786 0.7334 1.0222 -0.0603 -0.1440 0.2123  133 LYS A NZ  
1062 N N   . GLU A 146 ? 0.2874 0.2327 0.3265 0.0463  0.0041  0.0501  134 GLU A N   
1063 C CA  . GLU A 146 ? 0.2953 0.2350 0.3341 0.0641  0.0074  0.0330  134 GLU A CA  
1064 C C   . GLU A 146 ? 0.2669 0.2240 0.3063 0.0622  0.0173  0.0235  134 GLU A C   
1065 O O   . GLU A 146 ? 0.3011 0.2554 0.3390 0.0705  0.0174  0.0133  134 GLU A O   
1066 C CB  . GLU A 146 ? 0.3092 0.2628 0.3504 0.0749  0.0103  0.0347  134 GLU A CB  
1067 C CG  . GLU A 146 ? 0.3953 0.3282 0.4388 0.0787  -0.0027 0.0433  134 GLU A CG  
1068 C CD  . GLU A 146 ? 0.3906 0.3373 0.4375 0.0895  -0.0004 0.0456  134 GLU A CD  
1069 O OE1 . GLU A 146 ? 0.3677 0.3396 0.4178 0.0962  0.0091  0.0410  134 GLU A OE1 
1070 O OE2 . GLU A 146 ? 0.4538 0.3867 0.5040 0.0893  -0.0114 0.0561  134 GLU A OE2 
1071 N N   . VAL A 147 ? 0.2509 0.2290 0.2937 0.0532  0.0221  0.0252  135 VAL A N   
1072 C CA  . VAL A 147 ? 0.2543 0.2444 0.3045 0.0499  0.0246  0.0170  135 VAL A CA  
1073 C C   . VAL A 147 ? 0.2485 0.2247 0.2947 0.0433  0.0247  0.0136  135 VAL A C   
1074 O O   . VAL A 147 ? 0.2556 0.2319 0.3041 0.0450  0.0254  0.0078  135 VAL A O   
1075 C CB  . VAL A 147 ? 0.2354 0.2475 0.2935 0.0468  0.0219  0.0120  135 VAL A CB  
1076 C CG1 . VAL A 147 ? 0.2394 0.2573 0.3126 0.0438  0.0168  0.0029  135 VAL A CG1 
1077 C CG2 . VAL A 147 ? 0.2445 0.2661 0.3089 0.0543  0.0164  0.0137  135 VAL A CG2 
1078 N N   . ALA A 148 ? 0.2646 0.2350 0.3072 0.0336  0.0223  0.0210  136 ALA A N   
1079 C CA  . ALA A 148 ? 0.2759 0.2328 0.3190 0.0247  0.0189  0.0210  136 ALA A CA  
1080 C C   . ALA A 148 ? 0.3015 0.2273 0.3403 0.0345  0.0107  0.0128  136 ALA A C   
1081 O O   . ALA A 148 ? 0.3203 0.2407 0.3579 0.0349  0.0102  0.0035  136 ALA A O   
1082 C CB  . ALA A 148 ? 0.2837 0.2480 0.3297 0.0095  0.0137  0.0399  136 ALA A CB  
1083 N N   . GLU A 149 ? 0.2984 0.2073 0.3350 0.0458  0.0021  0.0126  137 GLU A N   
1084 C CA  . GLU A 149 ? 0.3436 0.2282 0.3764 0.0630  -0.0109 -0.0037 137 GLU A CA  
1085 C C   . GLU A 149 ? 0.3552 0.2689 0.3808 0.0777  0.0007  -0.0184 137 GLU A C   
1086 O O   . GLU A 149 ? 0.3583 0.2694 0.3781 0.0858  -0.0043 -0.0327 137 GLU A O   
1087 C CB  . GLU A 149 ? 0.3943 0.2609 0.4301 0.0766  -0.0248 -0.0046 137 GLU A CB  
1088 C CG  . GLU A 149 ? 0.5430 0.3828 0.5783 0.1012  -0.0471 -0.0289 137 GLU A CG  
1089 C CD  . GLU A 149 ? 0.9790 0.7882 1.0260 0.1113  -0.0715 -0.0283 137 GLU A CD  
1090 O OE1 . GLU A 149 ? 0.9862 0.7854 1.0440 0.0896  -0.0763 -0.0004 137 GLU A OE1 
1091 O OE2 . GLU A 149 ? 1.1184 0.9199 1.1650 0.1423  -0.0877 -0.0560 137 GLU A OE2 
1092 N N   . ARG A 150 ? 0.2853 0.2321 0.3135 0.0806  0.0133  -0.0121 138 ARG A N   
1093 C CA  . ARG A 150 ? 0.2865 0.2742 0.3141 0.0907  0.0210  -0.0153 138 ARG A CA  
1094 C C   . ARG A 150 ? 0.2877 0.2865 0.3201 0.0754  0.0248  -0.0110 138 ARG A C   
1095 O O   . ARG A 150 ? 0.2712 0.2959 0.2993 0.0823  0.0258  -0.0154 138 ARG A O   
1096 C CB  . ARG A 150 ? 0.2877 0.3095 0.3249 0.0936  0.0276  -0.0021 138 ARG A CB  
1097 C CG  . ARG A 150 ? 0.2664 0.2876 0.3178 0.0756  0.0287  0.0122  138 ARG A CG  
1098 C CD  . ARG A 150 ? 0.2543 0.3088 0.3195 0.0794  0.0290  0.0261  138 ARG A CD  
1099 N NE  . ARG A 150 ? 0.2380 0.2862 0.3179 0.0677  0.0228  0.0337  138 ARG A NE  
1100 C CZ  . ARG A 150 ? 0.2331 0.2878 0.3323 0.0553  0.0136  0.0385  138 ARG A CZ  
1101 N NH1 . ARG A 150 ? 0.2418 0.3061 0.3474 0.0480  0.0120  0.0407  138 ARG A NH1 
1102 N NH2 . ARG A 150 ? 0.2320 0.2823 0.3464 0.0517  0.0016  0.0388  138 ARG A NH2 
1103 N N   . MET A 151 ? 0.2814 0.2667 0.3228 0.0570  0.0253  -0.0041 139 MET A N   
1104 C CA  . MET A 151 ? 0.2576 0.2485 0.3074 0.0439  0.0249  -0.0029 139 MET A CA  
1105 C C   . MET A 151 ? 0.2821 0.2530 0.3210 0.0441  0.0212  -0.0132 139 MET A C   
1106 O O   . MET A 151 ? 0.3016 0.2870 0.3410 0.0422  0.0207  -0.0145 139 MET A O   
1107 C CB  . MET A 151 ? 0.2455 0.2326 0.3075 0.0314  0.0235  -0.0008 139 MET A CB  
1108 C CG  . MET A 151 ? 0.2247 0.2308 0.3045 0.0313  0.0188  0.0045  139 MET A CG  
1109 S SD  . MET A 151 ? 0.2222 0.2532 0.3278 0.0243  0.0077  0.0170  139 MET A SD  
1110 C CE  . MET A 151 ? 0.2515 0.2706 0.3682 0.0134  0.0004  0.0064  139 MET A CE  
1111 N N   . ARG A 152 ? 0.2855 0.2234 0.3177 0.0444  0.0143  -0.0173 140 ARG A N   
1112 C CA  . ARG A 152 ? 0.3200 0.2332 0.3469 0.0440  0.0037  -0.0263 140 ARG A CA  
1113 C C   . ARG A 152 ? 0.3336 0.2558 0.3472 0.0668  -0.0019 -0.0446 140 ARG A C   
1114 O O   . ARG A 152 ? 0.3543 0.2795 0.3623 0.0685  -0.0058 -0.0538 140 ARG A O   
1115 C CB  . ARG A 152 ? 0.3859 0.2634 0.4174 0.0367  -0.0106 -0.0198 140 ARG A CB  
1116 C CG  . ARG A 152 ? 0.4797 0.3285 0.5137 0.0303  -0.0267 -0.0238 140 ARG A CG  
1117 C CD  . ARG A 152 ? 0.4913 0.3067 0.5389 0.0186  -0.0486 -0.0085 140 ARG A CD  
1118 N NE  . ARG A 152 ? 0.6409 0.4287 0.6968 0.0091  -0.0679 -0.0083 140 ARG A NE  
1119 C CZ  . ARG A 152 ? 0.7155 0.4986 0.7903 -0.0162 -0.0781 0.0185  140 ARG A CZ  
1120 N NH1 . ARG A 152 ? 0.7134 0.5224 0.7989 -0.0330 -0.0719 0.0471  140 ARG A NH1 
1121 N NH2 . ARG A 152 ? 0.6704 0.4300 0.7543 -0.0250 -0.0961 0.0187  140 ARG A NH2 
1122 N N   . THR A 153 ? 0.3404 0.2729 0.3483 0.0872  -0.0033 -0.0522 141 THR A N   
1123 C CA  . THR A 153 ? 0.3603 0.3195 0.3544 0.1161  -0.0084 -0.0743 141 THR A CA  
1124 C C   . THR A 153 ? 0.3279 0.3481 0.3195 0.1135  0.0063  -0.0654 141 THR A C   
1125 O O   . THR A 153 ? 0.3495 0.3948 0.3283 0.1281  0.0020  -0.0808 141 THR A O   
1126 C CB  . THR A 153 ? 0.3997 0.3698 0.3922 0.1390  -0.0109 -0.0822 141 THR A CB  
1127 O OG1 . THR A 153 ? 0.4437 0.3536 0.4431 0.1395  -0.0323 -0.0879 141 THR A OG1 
1128 C CG2 . THR A 153 ? 0.4792 0.4959 0.4569 0.1754  -0.0153 -0.1092 141 THR A CG2 
1129 N N   . ALA A 154 ? 0.3219 0.3685 0.3284 0.0952  0.0191  -0.0396 142 ALA A N   
1130 C CA  . ALA A 154 ? 0.2891 0.3930 0.3039 0.0863  0.0256  -0.0210 142 ALA A CA  
1131 C C   . ALA A 154 ? 0.2681 0.3594 0.2839 0.0713  0.0215  -0.0213 142 ALA A C   
1132 O O   . ALA A 154 ? 0.2892 0.4273 0.2999 0.0746  0.0217  -0.0177 142 ALA A O   
1133 C CB  . ALA A 154 ? 0.2924 0.4094 0.3326 0.0672  0.0286  0.0064  142 ALA A CB  
1134 N N   . VAL A 155 ? 0.2448 0.2826 0.2677 0.0550  0.0177  -0.0235 143 VAL A N   
1135 C CA  . VAL A 155 ? 0.3013 0.3263 0.3274 0.0410  0.0130  -0.0242 143 VAL A CA  
1136 C C   . VAL A 155 ? 0.3127 0.3296 0.3169 0.0576  0.0049  -0.0463 143 VAL A C   
1137 O O   . VAL A 155 ? 0.3152 0.3566 0.3152 0.0556  0.0028  -0.0461 143 VAL A O   
1138 C CB  . VAL A 155 ? 0.2988 0.2826 0.3386 0.0231  0.0113  -0.0218 143 VAL A CB  
1139 C CG1 . VAL A 155 ? 0.3266 0.2921 0.3684 0.0114  0.0051  -0.0260 143 VAL A CG1 
1140 C CG2 . VAL A 155 ? 0.3105 0.3096 0.3736 0.0116  0.0131  -0.0075 143 VAL A CG2 
1141 N N   . THR A 156 ? 0.3427 0.3245 0.3353 0.0750  -0.0048 -0.0663 144 THR A N   
1142 C CA  . THR A 156 ? 0.4111 0.3796 0.3865 0.0965  -0.0218 -0.0941 144 THR A CA  
1143 C C   . THR A 156 ? 0.3371 0.3769 0.2948 0.1209  -0.0171 -0.1052 144 THR A C   
1144 O O   . THR A 156 ? 0.4134 0.4676 0.3576 0.1312  -0.0258 -0.1212 144 THR A O   
1145 C CB  . THR A 156 ? 0.4744 0.3959 0.4491 0.1136  -0.0407 -0.1121 144 THR A CB  
1146 O OG1 . THR A 156 ? 0.5080 0.3776 0.5006 0.0872  -0.0466 -0.0942 144 THR A OG1 
1147 C CG2 . THR A 156 ? 0.4945 0.3990 0.4553 0.1441  -0.0684 -0.1494 144 THR A CG2 
1148 N N   . ALA A 157 ? 0.3305 0.4243 0.2888 0.1307  -0.0039 -0.0949 145 ALA A N   
1149 C CA  . ALA A 157 ? 0.3726 0.5563 0.3161 0.1544  0.0021  -0.0994 145 ALA A CA  
1150 C C   . ALA A 157 ? 0.3072 0.5451 0.2579 0.1313  0.0104  -0.0698 145 ALA A C   
1151 O O   . ALA A 157 ? 0.3377 0.6376 0.2710 0.1473  0.0088  -0.0784 145 ALA A O   
1152 C CB  . ALA A 157 ? 0.3507 0.5823 0.2993 0.1665  0.0131  -0.0887 145 ALA A CB  
1153 N N   . ALA A 158 ? 0.2749 0.4915 0.2527 0.0949  0.0153  -0.0361 146 ALA A N   
1154 C CA  . ALA A 158 ? 0.3127 0.5675 0.3063 0.0695  0.0149  -0.0060 146 ALA A CA  
1155 C C   . ALA A 158 ? 0.3001 0.5296 0.2801 0.0687  0.0063  -0.0240 146 ALA A C   
1156 O O   . ALA A 158 ? 0.3343 0.6230 0.3099 0.0660  0.0048  -0.0121 146 ALA A O   
1157 C CB  . ALA A 158 ? 0.2798 0.4988 0.3093 0.0365  0.0125  0.0218  146 ALA A CB  
1158 N N   . VAL A 159 ? 0.3028 0.4496 0.2787 0.0686  -0.0013 -0.0478 147 VAL A N   
1159 C CA  . VAL A 159 ? 0.3495 0.4674 0.3144 0.0685  -0.0131 -0.0654 147 VAL A CA  
1160 C C   . VAL A 159 ? 0.3595 0.5222 0.2926 0.1043  -0.0209 -0.0955 147 VAL A C   
1161 O O   . VAL A 159 ? 0.3636 0.5608 0.2857 0.1055  -0.0257 -0.0977 147 VAL A O   
1162 C CB  . VAL A 159 ? 0.3206 0.3498 0.2921 0.0611  -0.0232 -0.0793 147 VAL A CB  
1163 C CG1 . VAL A 159 ? 0.3838 0.3813 0.3471 0.0613  -0.0397 -0.0963 147 VAL A CG1 
1164 C CG2 . VAL A 159 ? 0.3614 0.3669 0.3614 0.0308  -0.0151 -0.0538 147 VAL A CG2 
1165 N N   . ALA A 160 ? 0.4249 0.5905 0.3432 0.1371  -0.0249 -0.1226 148 ALA A N   
1166 C CA  . ALA A 160 ? 0.4109 0.6218 0.2992 0.1807  -0.0374 -0.1625 148 ALA A CA  
1167 C C   . ALA A 160 ? 0.4042 0.7403 0.2802 0.1893  -0.0224 -0.1452 148 ALA A C   
1168 O O   . ALA A 160 ? 0.5086 0.8939 0.3668 0.2135  -0.0323 -0.1665 148 ALA A O   
1169 C CB  . ALA A 160 ? 0.4469 0.6344 0.3294 0.2154  -0.0494 -0.1954 148 ALA A CB  
1170 N N   . ALA A 161 ? 0.4980 0.5584 0.2757 0.1702  0.0495  -0.0763 149 ALA A N   
1171 C CA  . ALA A 161 ? 0.4809 0.5631 0.2530 0.1782  0.0584  -0.0627 149 ALA A CA  
1172 C C   . ALA A 161 ? 0.5830 0.6843 0.3441 0.1745  0.0516  -0.0565 149 ALA A C   
1173 O O   . ALA A 161 ? 0.5791 0.6970 0.3330 0.1808  0.0574  -0.0467 149 ALA A O   
1174 C CB  . ALA A 161 ? 0.5299 0.6252 0.3281 0.1809  0.0699  -0.0414 149 ALA A CB  
1175 N N   . THR A 162 ? 0.5392 0.6392 0.3002 0.1647  0.0395  -0.0609 150 THR A N   
1176 C CA  . THR A 162 ? 0.5510 0.6694 0.3045 0.1605  0.0317  -0.0538 150 THR A CA  
1177 C C   . THR A 162 ? 0.5410 0.6535 0.2698 0.1577  0.0196  -0.0728 150 THR A C   
1178 O O   . THR A 162 ? 0.6889 0.7822 0.4139 0.1508  0.0098  -0.0909 150 THR A O   
1179 C CB  . THR A 162 ? 0.5255 0.6446 0.3050 0.1469  0.0238  -0.0439 150 THR A CB  
1180 O OG1 . THR A 162 ? 0.5366 0.6561 0.3428 0.1458  0.0332  -0.0280 150 THR A OG1 
1181 C CG2 . THR A 162 ? 0.5442 0.6848 0.3192 0.1447  0.0177  -0.0327 150 THR A CG2 
1182 N N   . PRO A 163 ? 0.7621 0.8904 0.4754 0.1621  0.0197  -0.0689 151 PRO A N   
1183 C CA  . PRO A 163 ? 0.7191 0.8429 0.4074 0.1593  0.0086  -0.0869 151 PRO A CA  
1184 C C   . PRO A 163 ? 0.6230 0.7557 0.3130 0.1477  -0.0077 -0.0876 151 PRO A C   
1185 O O   . PRO A 163 ? 0.6503 0.8004 0.3561 0.1456  -0.0078 -0.0693 151 PRO A O   
1186 C CB  . PRO A 163 ? 0.7519 0.8938 0.4259 0.1694  0.0166  -0.0777 151 PRO A CB  
1187 C CG  . PRO A 163 ? 0.6634 0.8266 0.3593 0.1717  0.0242  -0.0507 151 PRO A CG  
1188 C CD  . PRO A 163 ? 0.6449 0.7966 0.3647 0.1689  0.0294  -0.0464 151 PRO A CD  
1189 N N   . PRO A 164 ? 0.6269 0.7480 0.3028 0.1393  -0.0215 -0.1075 152 PRO A N   
1190 C CA  . PRO A 164 ? 0.6326 0.7641 0.3142 0.1270  -0.0380 -0.1074 152 PRO A CA  
1191 C C   . PRO A 164 ? 0.6867 0.8484 0.3701 0.1297  -0.0383 -0.0871 152 PRO A C   
1192 O O   . PRO A 164 ? 0.6209 0.7941 0.2885 0.1379  -0.0327 -0.0825 152 PRO A O   
1193 C CB  . PRO A 164 ? 0.7354 0.8522 0.3966 0.1192  -0.0508 -0.1312 152 PRO A CB  
1194 C CG  . PRO A 164 ? 0.7819 0.8708 0.4343 0.1252  -0.0413 -0.1464 152 PRO A CG  
1195 C CD  . PRO A 164 ? 0.7223 0.8204 0.3779 0.1402  -0.0225 -0.1303 152 PRO A CD  
1196 N N   . ALA A 165 ? 0.6308 0.8049 0.3350 0.1234  -0.0440 -0.0740 153 ALA A N   
1197 C CA  . ALA A 165 ? 0.5805 0.7809 0.2904 0.1252  -0.0447 -0.0541 153 ALA A CA  
1198 C C   . ALA A 165 ? 0.5539 0.7647 0.2443 0.1214  -0.0573 -0.0627 153 ALA A C   
1199 O O   . ALA A 165 ? 0.6804 0.8787 0.3604 0.1123  -0.0697 -0.0828 153 ALA A O   
1200 C CB  . ALA A 165 ? 0.5886 0.7969 0.3248 0.1180  -0.0500 -0.0414 153 ALA A CB  
1201 N N   . PRO A 166 ? 0.6261 0.8585 0.3104 0.1281  -0.0541 -0.0481 154 PRO A N   
1202 C CA  . PRO A 166 ? 0.5857 0.8300 0.2505 0.1245  -0.0666 -0.0550 154 PRO A CA  
1203 C C   . PRO A 166 ? 0.6739 0.9222 0.3488 0.1104  -0.0849 -0.0602 154 PRO A C   
1204 O O   . PRO A 166 ? 0.6766 0.9192 0.3345 0.1021  -0.0982 -0.0782 154 PRO A O   
1205 C CB  . PRO A 166 ? 0.6013 0.8705 0.2670 0.1344  -0.0588 -0.0324 154 PRO A CB  
1206 C CG  . PRO A 166 ? 0.6331 0.8971 0.3080 0.1449  -0.0399 -0.0210 154 PRO A CG  
1207 C CD  . PRO A 166 ? 0.6299 0.8752 0.3235 0.1394  -0.0385 -0.0256 154 PRO A CD  
1208 N N   . ASP A 167 ? 0.6326 0.8904 0.3356 0.1071  -0.0858 -0.0446 155 ASP A N   
1209 C CA  . ASP A 167 ? 0.7236 0.9870 0.4415 0.0939  -0.1020 -0.0474 155 ASP A CA  
1210 C C   . ASP A 167 ? 0.6521 0.9090 0.3988 0.0906  -0.0983 -0.0402 155 ASP A C   
1211 O O   . ASP A 167 ? 0.5846 0.8427 0.3434 0.0990  -0.0845 -0.0242 155 ASP A O   
1212 C CB  . ASP A 167 ? 0.7303 1.0216 0.4528 0.0934  -0.1098 -0.0322 155 ASP A CB  
1213 C CG  . ASP A 167 ? 0.9159 1.2225 0.6595 0.1026  -0.0975 -0.0053 155 ASP A CG  
1214 O OD1 . ASP A 167 ? 0.9758 1.2838 0.7117 0.1141  -0.0834 0.0041  155 ASP A OD1 
1215 O OD2 . ASP A 167 ? 0.7586 1.0751 0.5277 0.0981  -0.1015 0.0067  155 ASP A OD2 
1216 N N   . GLY A 168 ? 0.6178 0.8669 0.3754 0.0779  -0.1107 -0.0521 156 GLY A N   
1217 C CA  . GLY A 168 ? 0.5742 0.8202 0.3597 0.0741  -0.1088 -0.0448 156 GLY A CA  
1218 C C   . GLY A 168 ? 0.6580 0.8798 0.4418 0.0776  -0.0987 -0.0536 156 GLY A C   
1219 O O   . GLY A 168 ? 0.6224 0.8257 0.3855 0.0801  -0.0957 -0.0701 156 GLY A O   
1220 N N   . THR A 169 ? 0.5452 0.7605 0.3579 0.0760  -0.0900 -0.0403 157 THR A N   
1221 C CA  . THR A 169 ? 0.5105 0.6975 0.3342 0.0743  -0.0796 -0.0455 157 THR A CA  
1222 C C   . THR A 169 ? 0.5335 0.7155 0.3459 0.0873  -0.0635 -0.0392 157 THR A C   
1223 O O   . THR A 169 ? 0.4846 0.6811 0.3016 0.0951  -0.0553 -0.0206 157 THR A O   
1224 C CB  . THR A 169 ? 0.5013 0.6855 0.3585 0.0678  -0.0765 -0.0330 157 THR A CB  
1225 O OG1 . THR A 169 ? 0.5769 0.7707 0.4465 0.0563  -0.0908 -0.0362 157 THR A OG1 
1226 C CG2 . THR A 169 ? 0.4247 0.5814 0.2928 0.0647  -0.0680 -0.0388 157 THR A CG2 
1227 N N   . THR A 170 ? 0.4737 0.6351 0.2733 0.0897  -0.0587 -0.0539 158 THR A N   
1228 C CA  . THR A 170 ? 0.4398 0.5959 0.2334 0.1012  -0.0428 -0.0478 158 THR A CA  
1229 C C   . THR A 170 ? 0.3957 0.5413 0.2183 0.0983  -0.0332 -0.0356 158 THR A C   
1230 O O   . THR A 170 ? 0.3885 0.5178 0.2274 0.0890  -0.0366 -0.0418 158 THR A O   
1231 C CB  . THR A 170 ? 0.4998 0.6364 0.2734 0.1048  -0.0407 -0.0678 158 THR A CB  
1232 O OG1 . THR A 170 ? 0.5477 0.6922 0.2915 0.1065  -0.0508 -0.0820 158 THR A OG1 
1233 C CG2 . THR A 170 ? 0.5001 0.6343 0.2701 0.1174  -0.0235 -0.0601 158 THR A CG2 
1234 N N   . ARG A 171 ? 0.3878 0.5422 0.2162 0.1060  -0.0214 -0.0183 159 ARG A N   
1235 C CA  . ARG A 171 ? 0.3362 0.4838 0.1915 0.1022  -0.0142 -0.0056 159 ARG A CA  
1236 C C   . ARG A 171 ? 0.3214 0.4672 0.1782 0.1101  0.0001  0.0034  159 ARG A C   
1237 O O   . ARG A 171 ? 0.3537 0.5142 0.1984 0.1194  0.0062  0.0124  159 ARG A O   
1238 C CB  . ARG A 171 ? 0.3197 0.4824 0.1886 0.1003  -0.0167 0.0103  159 ARG A CB  
1239 C CG  . ARG A 171 ? 0.3227 0.4765 0.2170 0.0960  -0.0101 0.0212  159 ARG A CG  
1240 C CD  . ARG A 171 ? 0.3290 0.4954 0.2360 0.0948  -0.0129 0.0345  159 ARG A CD  
1241 N NE  . ARG A 171 ? 0.3345 0.5052 0.2450 0.0876  -0.0253 0.0268  159 ARG A NE  
1242 C CZ  . ARG A 171 ? 0.3482 0.5373 0.2484 0.0888  -0.0351 0.0260  159 ARG A CZ  
1243 N NH1 . ARG A 171 ? 0.3499 0.5560 0.2340 0.0979  -0.0338 0.0337  159 ARG A NH1 
1244 N NH2 . ARG A 171 ? 0.3565 0.5491 0.2636 0.0803  -0.0467 0.0187  159 ARG A NH2 
1245 N N   . VAL A 172 ? 0.3228 0.4529 0.1954 0.1063  0.0052  0.0028  160 VAL A N   
1246 C CA  . VAL A 172 ? 0.2972 0.4271 0.1755 0.1122  0.0178  0.0119  160 VAL A CA  
1247 C C   . VAL A 172 ? 0.2877 0.4117 0.1913 0.1050  0.0209  0.0231  160 VAL A C   
1248 O O   . VAL A 172 ? 0.3333 0.4455 0.2485 0.0964  0.0153  0.0176  160 VAL A O   
1249 C CB  . VAL A 172 ? 0.3709 0.4887 0.2412 0.1165  0.0217  -0.0004 160 VAL A CB  
1250 C CG1 . VAL A 172 ? 0.3523 0.4504 0.2333 0.1078  0.0157  -0.0117 160 VAL A CG1 
1251 C CG2 . VAL A 172 ? 0.3869 0.5096 0.2652 0.1231  0.0350  0.0114  160 VAL A CG2 
1252 N N   . ALA A 173 ? 0.2851 0.4175 0.1969 0.1082  0.0297  0.0390  161 ALA A N   
1253 C CA  . ALA A 173 ? 0.2586 0.3834 0.1925 0.1012  0.0329  0.0478  161 ALA A CA  
1254 C C   . ALA A 173 ? 0.2891 0.4079 0.2309 0.1012  0.0392  0.0474  161 ALA A C   
1255 O O   . ALA A 173 ? 0.2982 0.4248 0.2323 0.1093  0.0459  0.0490  161 ALA A O   
1256 C CB  . ALA A 173 ? 0.2701 0.4049 0.2113 0.1032  0.0386  0.0654  161 ALA A CB  
1257 N N   . VAL A 174 ? 0.2599 0.3668 0.2169 0.0929  0.0371  0.0458  162 VAL A N   
1258 C CA  . VAL A 174 ? 0.2430 0.3450 0.2091 0.0919  0.0410  0.0453  162 VAL A CA  
1259 C C   . VAL A 174 ? 0.2263 0.3244 0.2111 0.0833  0.0421  0.0543  162 VAL A C   
1260 O O   . VAL A 174 ? 0.2367 0.3249 0.2271 0.0759  0.0367  0.0507  162 VAL A O   
1261 C CB  . VAL A 174 ? 0.2508 0.3400 0.2140 0.0900  0.0355  0.0311  162 VAL A CB  
1262 C CG1 . VAL A 174 ? 0.2723 0.3583 0.2479 0.0892  0.0394  0.0335  162 VAL A CG1 
1263 C CG2 . VAL A 174 ? 0.3070 0.3966 0.2506 0.0979  0.0342  0.0199  162 VAL A CG2 
1264 N N   . VAL A 175 ? 0.2634 0.3697 0.2576 0.0842  0.0492  0.0660  163 VAL A N   
1265 C CA  . VAL A 175 ? 0.2569 0.3589 0.2680 0.0751  0.0497  0.0741  163 VAL A CA  
1266 C C   . VAL A 175 ? 0.2208 0.3205 0.2429 0.0705  0.0490  0.0724  163 VAL A C   
1267 O O   . VAL A 175 ? 0.2368 0.3467 0.2625 0.0754  0.0540  0.0766  163 VAL A O   
1268 C CB  . VAL A 175 ? 0.2344 0.3459 0.2522 0.0763  0.0568  0.0891  163 VAL A CB  
1269 C CG1 . VAL A 175 ? 0.2681 0.3710 0.3025 0.0654  0.0560  0.0948  163 VAL A CG1 
1270 C CG2 . VAL A 175 ? 0.2613 0.3774 0.2681 0.0822  0.0576  0.0930  163 VAL A CG2 
1271 N N   . GLY A 176 ? 0.2225 0.3105 0.2496 0.0622  0.0431  0.0671  164 GLY A N   
1272 C CA  . GLY A 176 ? 0.2217 0.3073 0.2577 0.0573  0.0406  0.0654  164 GLY A CA  
1273 C C   . GLY A 176 ? 0.2063 0.2840 0.2516 0.0460  0.0369  0.0669  164 GLY A C   
1274 O O   . GLY A 176 ? 0.2223 0.2980 0.2720 0.0420  0.0388  0.0729  164 GLY A O   
1275 N N   . HIS A 177 ? 0.2078 0.2802 0.2553 0.0413  0.0319  0.0618  165 HIS A N   
1276 C CA  . HIS A 177 ? 0.2134 0.2807 0.2684 0.0308  0.0280  0.0628  165 HIS A CA  
1277 C C   . HIS A 177 ? 0.2279 0.2835 0.2756 0.0275  0.0229  0.0542  165 HIS A C   
1278 O O   . HIS A 177 ? 0.2252 0.2793 0.2676 0.0320  0.0214  0.0491  165 HIS A O   
1279 C CB  . HIS A 177 ? 0.2049 0.2838 0.2720 0.0284  0.0272  0.0685  165 HIS A CB  
1280 C CG  . HIS A 177 ? 0.2140 0.3072 0.2906 0.0318  0.0333  0.0787  165 HIS A CG  
1281 N ND1 . HIS A 177 ? 0.2040 0.3014 0.2928 0.0238  0.0341  0.0870  165 HIS A ND1 
1282 C CD2 . HIS A 177 ? 0.2061 0.3106 0.2816 0.0426  0.0395  0.0822  165 HIS A CD2 
1283 C CE1 . HIS A 177 ? 0.2194 0.3315 0.3156 0.0294  0.0409  0.0967  165 HIS A CE1 
1284 N NE2 . HIS A 177 ? 0.2197 0.3369 0.3069 0.0416  0.0447  0.0938  165 HIS A NE2 
1285 N N   . ASP A 178 ? 0.2093 0.2560 0.2570 0.0197  0.0207  0.0527  166 ASP A N   
1286 C CA  . ASP A 178 ? 0.2208 0.2572 0.2608 0.0172  0.0175  0.0456  166 ASP A CA  
1287 C C   . ASP A 178 ? 0.2232 0.2616 0.2617 0.0182  0.0139  0.0427  166 ASP A C   
1288 O O   . ASP A 178 ? 0.2090 0.2435 0.2421 0.0218  0.0135  0.0384  166 ASP A O   
1289 C CB  . ASP A 178 ? 0.2116 0.2396 0.2519 0.0082  0.0157  0.0443  166 ASP A CB  
1290 C CG  . ASP A 178 ? 0.2523 0.2725 0.2844 0.0055  0.0128  0.0379  166 ASP A CG  
1291 O OD1 . ASP A 178 ? 0.2479 0.2638 0.2745 0.0098  0.0147  0.0349  166 ASP A OD1 
1292 O OD2 . ASP A 178 ? 0.2922 0.3124 0.3235 -0.0011 0.0085  0.0368  166 ASP A OD2 
1293 N N   . SER A 179 ? 0.2030 0.2470 0.2471 0.0143  0.0108  0.0455  167 SER A N   
1294 C CA  . SER A 179 ? 0.2106 0.2542 0.2528 0.0146  0.0073  0.0438  167 SER A CA  
1295 C C   . SER A 179 ? 0.1898 0.2356 0.2329 0.0233  0.0091  0.0435  167 SER A C   
1296 O O   . SER A 179 ? 0.2084 0.2479 0.2476 0.0248  0.0077  0.0401  167 SER A O   
1297 C CB  . SER A 179 ? 0.2307 0.2818 0.2785 0.0086  0.0027  0.0481  167 SER A CB  
1298 O OG  . SER A 179 ? 0.2812 0.3261 0.3242 -0.0002 0.0003  0.0452  167 SER A OG  
1299 N N   . ALA A 180 ? 0.1972 0.2508 0.2451 0.0290  0.0126  0.0469  168 ALA A N   
1300 C CA  . ALA A 180 ? 0.2119 0.2652 0.2580 0.0382  0.0151  0.0446  168 ALA A CA  
1301 C C   . ALA A 180 ? 0.2146 0.2587 0.2508 0.0405  0.0154  0.0371  168 ALA A C   
1302 O O   . ALA A 180 ? 0.2254 0.2627 0.2583 0.0440  0.0143  0.0320  168 ALA A O   
1303 C CB  . ALA A 180 ? 0.2157 0.2807 0.2673 0.0448  0.0203  0.0498  168 ALA A CB  
1304 N N   . LEU A 181 ? 0.2121 0.2556 0.2446 0.0381  0.0163  0.0366  169 LEU A N   
1305 C CA  . LEU A 181 ? 0.2190 0.2574 0.2438 0.0399  0.0156  0.0310  169 LEU A CA  
1306 C C   . LEU A 181 ? 0.2201 0.2505 0.2441 0.0348  0.0118  0.0273  169 LEU A C   
1307 O O   . LEU A 181 ? 0.2231 0.2492 0.2441 0.0361  0.0098  0.0223  169 LEU A O   
1308 C CB  . LEU A 181 ? 0.2025 0.2438 0.2259 0.0393  0.0180  0.0340  169 LEU A CB  
1309 C CG  . LEU A 181 ? 0.2228 0.2733 0.2454 0.0455  0.0225  0.0385  169 LEU A CG  
1310 C CD1 . LEU A 181 ? 0.2367 0.2886 0.2605 0.0440  0.0252  0.0441  169 LEU A CD1 
1311 C CD2 . LEU A 181 ? 0.2725 0.3252 0.2860 0.0532  0.0228  0.0333  169 LEU A CD2 
1312 N N   . VAL A 182 ? 0.2063 0.2349 0.2328 0.0288  0.0108  0.0298  170 VAL A N   
1313 C CA  . VAL A 182 ? 0.2060 0.2289 0.2314 0.0247  0.0085  0.0279  170 VAL A CA  
1314 C C   . VAL A 182 ? 0.2239 0.2441 0.2518 0.0259  0.0063  0.0276  170 VAL A C   
1315 O O   . VAL A 182 ? 0.2166 0.2317 0.2444 0.0244  0.0048  0.0254  170 VAL A O   
1316 C CB  . VAL A 182 ? 0.2188 0.2405 0.2431 0.0187  0.0083  0.0299  170 VAL A CB  
1317 C CG1 . VAL A 182 ? 0.2507 0.2688 0.2728 0.0155  0.0068  0.0294  170 VAL A CG1 
1318 C CG2 . VAL A 182 ? 0.2308 0.2504 0.2527 0.0180  0.0112  0.0293  170 VAL A CG2 
1319 N N   . ILE A 183 ? 0.2170 0.2407 0.2488 0.0284  0.0064  0.0309  171 ILE A N   
1320 C CA  . ILE A 183 ? 0.2044 0.2241 0.2396 0.0313  0.0053  0.0315  171 ILE A CA  
1321 C C   . ILE A 183 ? 0.2267 0.2393 0.2594 0.0360  0.0058  0.0250  171 ILE A C   
1322 O O   . ILE A 183 ? 0.2378 0.2415 0.2718 0.0350  0.0040  0.0228  171 ILE A O   
1323 C CB  . ILE A 183 ? 0.1971 0.2247 0.2387 0.0346  0.0061  0.0375  171 ILE A CB  
1324 C CG1 . ILE A 183 ? 0.2188 0.2523 0.2622 0.0280  0.0031  0.0431  171 ILE A CG1 
1325 C CG2 . ILE A 183 ? 0.2346 0.2566 0.2804 0.0413  0.0068  0.0380  171 ILE A CG2 
1326 C CD1 . ILE A 183 ? 0.2262 0.2723 0.2777 0.0289  0.0024  0.0503  171 ILE A CD1 
1327 N N   . LEU A 184 ? 0.2095 0.2256 0.2381 0.0407  0.0080  0.0218  172 LEU A N   
1328 C CA  . LEU A 184 ? 0.2329 0.2424 0.2558 0.0446  0.0074  0.0138  172 LEU A CA  
1329 C C   . LEU A 184 ? 0.2452 0.2498 0.2671 0.0385  0.0034  0.0099  172 LEU A C   
1330 O O   . LEU A 184 ? 0.2565 0.2515 0.2790 0.0376  0.0008  0.0049  172 LEU A O   
1331 C CB  . LEU A 184 ? 0.2600 0.2770 0.2762 0.0504  0.0105  0.0120  172 LEU A CB  
1332 C CG  . LEU A 184 ? 0.2527 0.2644 0.2594 0.0537  0.0086  0.0023  172 LEU A CG  
1333 C CD1 . LEU A 184 ? 0.2810 0.2799 0.2865 0.0581  0.0085  -0.0041 172 LEU A CD1 
1334 C CD2 . LEU A 184 ? 0.2767 0.2986 0.2746 0.0596  0.0117  0.0021  172 LEU A CD2 
1335 N N   . MET A 185 ? 0.2361 0.2469 0.2575 0.0345  0.0032  0.0121  173 MET A N   
1336 C CA  . MET A 185 ? 0.2281 0.2378 0.2502 0.0299  0.0000  0.0094  173 MET A CA  
1337 C C   . MET A 185 ? 0.2291 0.2330 0.2578 0.0244  -0.0014 0.0118  173 MET A C   
1338 O O   . MET A 185 ? 0.2302 0.2297 0.2622 0.0210  -0.0047 0.0087  173 MET A O   
1339 C CB  . MET A 185 ? 0.2177 0.2356 0.2387 0.0290  0.0015  0.0124  173 MET A CB  
1340 C CG  . MET A 185 ? 0.2070 0.2315 0.2217 0.0343  0.0021  0.0107  173 MET A CG  
1341 S SD  . MET A 185 ? 0.2276 0.2604 0.2426 0.0347  0.0045  0.0160  173 MET A SD  
1342 C CE  . MET A 185 ? 0.2484 0.2792 0.2653 0.0342  0.0096  0.0219  173 MET A CE  
1343 N N   . GLY A 186 ? 0.2405 0.2448 0.2713 0.0231  0.0005  0.0178  174 GLY A N   
1344 C CA  . GLY A 186 ? 0.2354 0.2351 0.2714 0.0190  -0.0004 0.0216  174 GLY A CA  
1345 C C   . GLY A 186 ? 0.2666 0.2560 0.3067 0.0204  -0.0022 0.0195  174 GLY A C   
1346 O O   . GLY A 186 ? 0.2582 0.2418 0.3036 0.0161  -0.0041 0.0194  174 GLY A O   
1347 N N   . SER A 187 ? 0.2502 0.2368 0.2886 0.0266  -0.0011 0.0176  175 SER A N   
1348 C CA  . SER A 187 ? 0.2451 0.2189 0.2868 0.0296  -0.0016 0.0152  175 SER A CA  
1349 C C   . SER A 187 ? 0.2862 0.2510 0.3264 0.0274  -0.0050 0.0057  175 SER A C   
1350 O O   . SER A 187 ? 0.2769 0.2285 0.3226 0.0249  -0.0069 0.0041  175 SER A O   
1351 C CB  . SER A 187 ? 0.3013 0.2759 0.3413 0.0385  0.0016  0.0153  175 SER A CB  
1352 O OG  . SER A 187 ? 0.3665 0.3436 0.3984 0.0432  0.0026  0.0078  175 SER A OG  
1353 N N   . LEU A 188 ? 0.2666 0.2384 0.2997 0.0275  -0.0064 -0.0003 176 LEU A N   
1354 C CA  . LEU A 188 ? 0.2575 0.2240 0.2884 0.0242  -0.0113 -0.0096 176 LEU A CA  
1355 C C   . LEU A 188 ? 0.2636 0.2299 0.3045 0.0145  -0.0150 -0.0066 176 LEU A C   
1356 O O   . LEU A 188 ? 0.3099 0.2684 0.3536 0.0094  -0.0202 -0.0133 176 LEU A O   
1357 C CB  . LEU A 188 ? 0.2720 0.2497 0.2930 0.0271  -0.0123 -0.0143 176 LEU A CB  
1358 C CG  . LEU A 188 ? 0.2863 0.2652 0.2969 0.0369  -0.0083 -0.0175 176 LEU A CG  
1359 C CD1 . LEU A 188 ? 0.2972 0.2905 0.2997 0.0390  -0.0085 -0.0180 176 LEU A CD1 
1360 C CD2 . LEU A 188 ? 0.3359 0.2990 0.3409 0.0407  -0.0095 -0.0280 176 LEU A CD2 
1361 N N   A MET A 189 ? 0.2478 0.2222 0.2944 0.0115  -0.0123 0.0031  177 MET A N   
1362 N N   B MET A 189 ? 0.2477 0.2220 0.2943 0.0115  -0.0123 0.0031  177 MET A N   
1363 C CA  A MET A 189 ? 0.2408 0.2169 0.2978 0.0034  -0.0138 0.0081  177 MET A CA  
1364 C CA  B MET A 189 ? 0.2406 0.2166 0.2976 0.0034  -0.0139 0.0080  177 MET A CA  
1365 C C   A MET A 189 ? 0.2630 0.2303 0.3273 0.0018  -0.0117 0.0158  177 MET A C   
1366 C C   B MET A 189 ? 0.2627 0.2302 0.3270 0.0018  -0.0116 0.0159  177 MET A C   
1367 O O   A MET A 189 ? 0.2699 0.2410 0.3424 -0.0040 -0.0109 0.0232  177 MET A O   
1368 O O   B MET A 189 ? 0.2702 0.2415 0.3427 -0.0039 -0.0108 0.0233  177 MET A O   
1369 C CB  A MET A 189 ? 0.2534 0.2450 0.3104 0.0023  -0.0113 0.0137  177 MET A CB  
1370 C CB  B MET A 189 ? 0.2619 0.2538 0.3188 0.0022  -0.0118 0.0129  177 MET A CB  
1371 C CG  A MET A 189 ? 0.2483 0.2495 0.3035 0.0019  -0.0145 0.0087  177 MET A CG  
1372 C CG  B MET A 189 ? 0.2706 0.2716 0.3208 0.0051  -0.0138 0.0071  177 MET A CG  
1373 S SD  A MET A 189 ? 0.2711 0.2884 0.3278 0.0025  -0.0101 0.0159  177 MET A SD  
1374 S SD  B MET A 189 ? 0.2873 0.3052 0.3431 0.0025  -0.0131 0.0121  177 MET A SD  
1375 C CE  A MET A 189 ? 0.2187 0.2348 0.2643 0.0093  -0.0047 0.0173  177 MET A CE  
1376 C CE  B MET A 189 ? 0.1603 0.1771 0.2167 0.0028  -0.0061 0.0208  177 MET A CE  
1377 N N   . ASN A 190 ? 0.2553 0.2124 0.3173 0.0074  -0.0101 0.0154  178 ASN A N   
1378 C CA  A ASN A 190 ? 0.3011 0.2504 0.3704 0.0072  -0.0081 0.0243  178 ASN A CA  
1379 C CA  B ASN A 190 ? 0.3006 0.2499 0.3696 0.0076  -0.0080 0.0242  178 ASN A CA  
1380 C C   . ASN A 190 ? 0.3038 0.2659 0.3726 0.0062  -0.0049 0.0354  178 ASN A C   
1381 O O   . ASN A 190 ? 0.3032 0.2639 0.3787 0.0029  -0.0037 0.0447  178 ASN A O   
1382 C CB  A ASN A 190 ? 0.2810 0.2174 0.3618 0.0000  -0.0108 0.0247  178 ASN A CB  
1383 C CB  B ASN A 190 ? 0.2855 0.2199 0.3654 0.0014  -0.0106 0.0240  178 ASN A CB  
1384 C CG  A ASN A 190 ? 0.4323 0.3558 0.5207 0.0019  -0.0085 0.0333  178 ASN A CG  
1385 C CG  B ASN A 190 ? 0.2943 0.2126 0.3714 0.0031  -0.0141 0.0107  178 ASN A CG  
1386 O OD1 A ASN A 190 ? 0.3891 0.3096 0.4739 0.0102  -0.0060 0.0353  178 ASN A OD1 
1387 O OD1 B ASN A 190 ? 0.3104 0.2214 0.3810 0.0119  -0.0119 0.0064  178 ASN A OD1 
1388 N ND2 A ASN A 190 ? 0.3979 0.3151 0.4985 -0.0056 -0.0091 0.0400  178 ASN A ND2 
1389 N ND2 B ASN A 190 ? 0.3568 0.2708 0.4384 -0.0051 -0.0194 0.0040  178 ASN A ND2 
1390 N N   . LEU A 191 ? 0.2544 0.2284 0.3146 0.0088  -0.0035 0.0345  179 LEU A N   
1391 C CA  . LEU A 191 ? 0.2524 0.2370 0.3090 0.0078  -0.0010 0.0423  179 LEU A CA  
1392 C C   . LEU A 191 ? 0.2773 0.2654 0.3287 0.0130  -0.0005 0.0444  179 LEU A C   
1393 O O   . LEU A 191 ? 0.3152 0.3019 0.3648 0.0177  -0.0008 0.0391  179 LEU A O   
1394 C CB  . LEU A 191 ? 0.2575 0.2520 0.3088 0.0059  0.0002  0.0391  179 LEU A CB  
1395 C CG  . LEU A 191 ? 0.2219 0.2185 0.2796 0.0012  -0.0003 0.0379  179 LEU A CG  
1396 C CD1 . LEU A 191 ? 0.2411 0.2475 0.2935 0.0021  0.0019  0.0358  179 LEU A CD1 
1397 C CD2 . LEU A 191 ? 0.2751 0.2723 0.3408 -0.0037 0.0014  0.0468  179 LEU A CD2 
1398 N N   . GLY A 192 ? 0.2647 0.2592 0.3137 0.0119  0.0003  0.0525  180 GLY A N   
1399 C CA  . GLY A 192 ? 0.2738 0.2747 0.3197 0.0152  -0.0006 0.0561  180 GLY A CA  
1400 C C   . GLY A 192 ? 0.2454 0.2556 0.2819 0.0126  -0.0006 0.0536  180 GLY A C   
1401 O O   . GLY A 192 ? 0.2692 0.2802 0.3011 0.0094  0.0012  0.0507  180 GLY A O   
1402 N N   . TRP A 193 ? 0.2461 0.2631 0.2811 0.0141  -0.0024 0.0549  181 TRP A N   
1403 C CA  . TRP A 193 ? 0.2430 0.2659 0.2704 0.0108  -0.0028 0.0514  181 TRP A CA  
1404 C C   . TRP A 193 ? 0.2570 0.2816 0.2749 0.0063  -0.0023 0.0524  181 TRP A C   
1405 O O   . TRP A 193 ? 0.2728 0.3008 0.2885 0.0053  -0.0035 0.0592  181 TRP A O   
1406 C CB  . TRP A 193 ? 0.2519 0.2840 0.2816 0.0112  -0.0061 0.0554  181 TRP A CB  
1407 C CG  . TRP A 193 ? 0.2292 0.2658 0.2521 0.0060  -0.0076 0.0516  181 TRP A CG  
1408 C CD1 . TRP A 193 ? 0.2522 0.2933 0.2661 0.0004  -0.0108 0.0524  181 TRP A CD1 
1409 C CD2 . TRP A 193 ? 0.2368 0.2723 0.2610 0.0058  -0.0060 0.0465  181 TRP A CD2 
1410 N NE1 . TRP A 193 ? 0.2435 0.2838 0.2535 -0.0039 -0.0114 0.0467  181 TRP A NE1 
1411 C CE2 . TRP A 193 ? 0.2133 0.2507 0.2307 -0.0007 -0.0083 0.0442  181 TRP A CE2 
1412 C CE3 . TRP A 193 ? 0.2361 0.2692 0.2655 0.0104  -0.0028 0.0437  181 TRP A CE3 
1413 C CZ2 . TRP A 193 ? 0.2489 0.2843 0.2670 -0.0030 -0.0071 0.0404  181 TRP A CZ2 
1414 C CZ3 . TRP A 193 ? 0.2459 0.2796 0.2751 0.0088  -0.0013 0.0410  181 TRP A CZ3 
1415 C CH2 . TRP A 193 ? 0.2497 0.2837 0.2743 0.0019  -0.0033 0.0398  181 TRP A CH2 
1416 N N   . GLY A 194 ? 0.2541 0.2763 0.2657 0.0044  0.0003  0.0461  182 GLY A N   
1417 C CA  . GLY A 194 ? 0.2687 0.2912 0.2698 0.0016  0.0025  0.0456  182 GLY A CA  
1418 C C   . GLY A 194 ? 0.2597 0.2795 0.2634 0.0026  0.0072  0.0452  182 GLY A C   
1419 O O   . GLY A 194 ? 0.2927 0.3124 0.2888 0.0021  0.0112  0.0429  182 GLY A O   
1420 N N   . GLN A 195 ? 0.2464 0.2639 0.2612 0.0040  0.0069  0.0474  183 GLN A N   
1421 C CA  . GLN A 195 ? 0.2211 0.2385 0.2408 0.0034  0.0103  0.0482  183 GLN A CA  
1422 C C   . GLN A 195 ? 0.2394 0.2566 0.2601 0.0049  0.0121  0.0417  183 GLN A C   
1423 O O   . GLN A 195 ? 0.2382 0.2580 0.2558 0.0053  0.0164  0.0411  183 GLN A O   
1424 C CB  . GLN A 195 ? 0.2322 0.2459 0.2640 0.0028  0.0083  0.0520  183 GLN A CB  
1425 C CG  . GLN A 195 ? 0.2874 0.3017 0.3196 0.0020  0.0078  0.0614  183 GLN A CG  
1426 C CD  . GLN A 195 ? 0.2829 0.2905 0.3283 0.0008  0.0069  0.0661  183 GLN A CD  
1427 O OE1 . GLN A 195 ? 0.2769 0.2767 0.3282 0.0028  0.0041  0.0630  183 GLN A OE1 
1428 N NE2 . GLN A 195 ? 0.3002 0.3104 0.3507 -0.0025 0.0099  0.0732  183 GLN A NE2 
1429 N N   . LEU A 196 ? 0.2243 0.2389 0.2485 0.0067  0.0094  0.0374  184 LEU A N   
1430 C CA  . LEU A 196 ? 0.2282 0.2436 0.2516 0.0089  0.0108  0.0326  184 LEU A CA  
1431 C C   . LEU A 196 ? 0.2350 0.2488 0.2495 0.0091  0.0122  0.0308  184 LEU A C   
1432 O O   . LEU A 196 ? 0.2479 0.2610 0.2618 0.0094  0.0099  0.0298  184 LEU A O   
1433 C CB  . LEU A 196 ? 0.2455 0.2597 0.2736 0.0112  0.0076  0.0294  184 LEU A CB  
1434 C CG  . LEU A 196 ? 0.2545 0.2715 0.2820 0.0140  0.0087  0.0263  184 LEU A CG  
1435 C CD1 . LEU A 196 ? 0.2599 0.2820 0.2926 0.0135  0.0098  0.0272  184 LEU A CD1 
1436 C CD2 . LEU A 196 ? 0.2879 0.3046 0.3161 0.0170  0.0058  0.0231  184 LEU A CD2 
1437 N N   . ASP A 197 ? 0.2317 0.2450 0.2395 0.0085  0.0161  0.0304  185 ASP A N   
1438 C CA  . ASP A 197 ? 0.2365 0.2459 0.2336 0.0067  0.0166  0.0278  185 ASP A CA  
1439 C C   . ASP A 197 ? 0.2302 0.2344 0.2261 0.0087  0.0195  0.0237  185 ASP A C   
1440 O O   . ASP A 197 ? 0.2523 0.2530 0.2438 0.0108  0.0248  0.0217  185 ASP A O   
1441 C CB  . ASP A 197 ? 0.2625 0.2724 0.2502 0.0059  0.0201  0.0286  185 ASP A CB  
1442 C CG  . ASP A 197 ? 0.2989 0.3038 0.2726 0.0031  0.0195  0.0241  185 ASP A CG  
1443 O OD1 . ASP A 197 ? 0.2967 0.3010 0.2713 -0.0001 0.0142  0.0231  185 ASP A OD1 
1444 O OD2 . ASP A 197 ? 0.3268 0.3291 0.2892 0.0039  0.0241  0.0216  185 ASP A OD2 
1445 N N   . MET A 198 ? 0.2288 0.2329 0.2297 0.0090  0.0170  0.0234  186 MET A N   
1446 C CA  . MET A 198 ? 0.2438 0.2439 0.2462 0.0116  0.0199  0.0220  186 MET A CA  
1447 C C   . MET A 198 ? 0.2346 0.2336 0.2387 0.0090  0.0173  0.0224  186 MET A C   
1448 O O   . MET A 198 ? 0.2425 0.2473 0.2503 0.0078  0.0133  0.0246  186 MET A O   
1449 C CB  . MET A 198 ? 0.2629 0.2691 0.2734 0.0163  0.0203  0.0242  186 MET A CB  
1450 C CG  . MET A 198 ? 0.2644 0.2743 0.2772 0.0182  0.0227  0.0251  186 MET A CG  
1451 S SD  . MET A 198 ? 0.2658 0.2854 0.2884 0.0216  0.0203  0.0270  186 MET A SD  
1452 C CE  . MET A 198 ? 0.2246 0.2433 0.2475 0.0271  0.0247  0.0286  186 MET A CE  
1453 N N   . ILE A 199 ? 0.2335 0.2249 0.2361 0.0083  0.0200  0.0209  187 ILE A N   
1454 C CA  . ILE A 199 ? 0.2600 0.2516 0.2680 0.0064  0.0187  0.0233  187 ILE A CA  
1455 C C   . ILE A 199 ? 0.2326 0.2251 0.2459 0.0124  0.0228  0.0268  187 ILE A C   
1456 O O   . ILE A 199 ? 0.2635 0.2496 0.2753 0.0157  0.0272  0.0261  187 ILE A O   
1457 C CB  . ILE A 199 ? 0.3058 0.2879 0.3099 -0.0007 0.0178  0.0202  187 ILE A CB  
1458 C CG1 . ILE A 199 ? 0.3257 0.3100 0.3392 -0.0035 0.0168  0.0247  187 ILE A CG1 
1459 C CG2 . ILE A 199 ? 0.3490 0.3172 0.3462 0.0005  0.0228  0.0156  187 ILE A CG2 
1460 C CD1 . ILE A 199 ? 0.4952 0.4762 0.5080 -0.0137 0.0119  0.0225  187 ILE A CD1 
1461 N N   . LEU A 200 ? 0.2190 0.2201 0.2379 0.0149  0.0217  0.0308  188 LEU A N   
1462 C CA  . LEU A 200 ? 0.2355 0.2403 0.2576 0.0211  0.0248  0.0348  188 LEU A CA  
1463 C C   . LEU A 200 ? 0.2326 0.2301 0.2579 0.0201  0.0286  0.0387  188 LEU A C   
1464 O O   . LEU A 200 ? 0.2402 0.2368 0.2692 0.0148  0.0276  0.0406  188 LEU A O   
1465 C CB  . LEU A 200 ? 0.2510 0.2672 0.2753 0.0248  0.0230  0.0373  188 LEU A CB  
1466 C CG  . LEU A 200 ? 0.2117 0.2320 0.2338 0.0256  0.0192  0.0332  188 LEU A CG  
1467 C CD1 . LEU A 200 ? 0.2424 0.2708 0.2650 0.0299  0.0183  0.0342  188 LEU A CD1 
1468 C CD2 . LEU A 200 ? 0.2444 0.2650 0.2650 0.0280  0.0190  0.0311  188 LEU A CD2 
1469 N N   . PRO A 201 ? 0.2249 0.2175 0.2508 0.0248  0.0331  0.0410  189 PRO A N   
1470 C CA  . PRO A 201 ? 0.2280 0.2111 0.2583 0.0241  0.0374  0.0459  189 PRO A CA  
1471 C C   . PRO A 201 ? 0.2298 0.2226 0.2663 0.0249  0.0378  0.0540  189 PRO A C   
1472 O O   . PRO A 201 ? 0.2268 0.2337 0.2624 0.0297  0.0364  0.0562  189 PRO A O   
1473 C CB  . PRO A 201 ? 0.2411 0.2210 0.2717 0.0320  0.0423  0.0488  189 PRO A CB  
1474 C CG  . PRO A 201 ? 0.2410 0.2229 0.2665 0.0332  0.0409  0.0423  189 PRO A CG  
1475 C CD  . PRO A 201 ? 0.2311 0.2254 0.2550 0.0305  0.0347  0.0399  189 PRO A CD  
1476 N N   . LEU A 202 ? 0.2408 0.2256 0.2836 0.0199  0.0401  0.0582  190 LEU A N   
1477 C CA  . LEU A 202 ? 0.2351 0.2294 0.2856 0.0216  0.0426  0.0687  190 LEU A CA  
1478 C C   . LEU A 202 ? 0.2483 0.2503 0.2975 0.0321  0.0466  0.0760  190 LEU A C   
1479 O O   . LEU A 202 ? 0.2390 0.2324 0.2875 0.0363  0.0497  0.0771  190 LEU A O   
1480 C CB  . LEU A 202 ? 0.2659 0.2482 0.3257 0.0137  0.0450  0.0733  190 LEU A CB  
1481 C CG  . LEU A 202 ? 0.2820 0.2603 0.3434 0.0021  0.0393  0.0665  190 LEU A CG  
1482 C CD1 . LEU A 202 ? 0.3133 0.2727 0.3816 -0.0071 0.0406  0.0672  190 LEU A CD1 
1483 C CD2 . LEU A 202 ? 0.2572 0.2553 0.3251 0.0002  0.0364  0.0712  190 LEU A CD2 
1484 N N   . THR A 203 ? 0.2172 0.2361 0.2657 0.0370  0.0468  0.0814  191 THR A N   
1485 C CA  . THR A 203 ? 0.2199 0.2506 0.2640 0.0470  0.0488  0.0876  191 THR A CA  
1486 C C   . THR A 203 ? 0.1982 0.2321 0.2345 0.0515  0.0449  0.0804  191 THR A C   
1487 O O   . THR A 203 ? 0.2192 0.2624 0.2525 0.0591  0.0454  0.0855  191 THR A O   
1488 C CB  . THR A 203 ? 0.2184 0.2470 0.2684 0.0512  0.0551  0.1007  191 THR A CB  
1489 O OG1 . THR A 203 ? 0.2424 0.2541 0.2957 0.0508  0.0573  0.0999  191 THR A OG1 
1490 C CG2 . THR A 203 ? 0.2568 0.2853 0.3166 0.0462  0.0590  0.1096  191 THR A CG2 
1491 N N   . SER A 204 ? 0.2204 0.2490 0.2541 0.0468  0.0406  0.0699  192 SER A N   
1492 C CA  . SER A 204 ? 0.2125 0.2458 0.2414 0.0502  0.0371  0.0646  192 SER A CA  
1493 C C   . SER A 204 ? 0.2081 0.2562 0.2304 0.0542  0.0330  0.0627  192 SER A C   
1494 O O   . SER A 204 ? 0.2196 0.2721 0.2397 0.0538  0.0328  0.0620  192 SER A O   
1495 C CB  . SER A 204 ? 0.2353 0.2602 0.2633 0.0444  0.0342  0.0554  192 SER A CB  
1496 O OG  . SER A 204 ? 0.2234 0.2492 0.2497 0.0396  0.0309  0.0505  192 SER A OG  
1497 N N   . VAL A 205 ? 0.1949 0.3128 0.2404 0.0203  0.0112  0.0416  193 VAL A N   
1498 C CA  . VAL A 205 ? 0.1870 0.3150 0.2216 0.0281  0.0166  0.0427  193 VAL A CA  
1499 C C   . VAL A 205 ? 0.1808 0.3019 0.2026 0.0343  0.0085  0.0355  193 VAL A C   
1500 O O   . VAL A 205 ? 0.1994 0.3074 0.2109 0.0345  0.0056  0.0347  193 VAL A O   
1501 C CB  . VAL A 205 ? 0.2136 0.3355 0.2310 0.0291  0.0222  0.0522  193 VAL A CB  
1502 C CG1 . VAL A 205 ? 0.2496 0.3768 0.2469 0.0349  0.0225  0.0487  193 VAL A CG1 
1503 C CG2 . VAL A 205 ? 0.2152 0.3378 0.2390 0.0218  0.0324  0.0644  193 VAL A CG2 
1504 N N   . SER A 206 ? 0.2080 0.3363 0.2332 0.0399  0.0078  0.0309  194 SER A N   
1505 C CA  . SER A 206 ? 0.2061 0.3234 0.2190 0.0445  0.0023  0.0269  194 SER A CA  
1506 C C   . SER A 206 ? 0.2144 0.3330 0.2205 0.0488  0.0087  0.0221  194 SER A C   
1507 O O   . SER A 206 ? 0.2989 0.4288 0.3108 0.0513  0.0184  0.0201  194 SER A O   
1508 C CB  . SER A 206 ? 0.2018 0.3174 0.2237 0.0480  -0.0078 0.0262  194 SER A CB  
1509 O OG  . SER A 206 ? 0.1931 0.3066 0.2145 0.0420  -0.0169 0.0276  194 SER A OG  
1510 N N   . VAL A 207 ? 0.2204 0.3270 0.2128 0.0478  0.0053  0.0190  195 VAL A N   
1511 C CA  . VAL A 207 ? 0.2284 0.3308 0.2069 0.0485  0.0081  0.0106  195 VAL A CA  
1512 C C   . VAL A 207 ? 0.2401 0.3241 0.2199 0.0518  0.0052  0.0028  195 VAL A C   
1513 O O   . VAL A 207 ? 0.2350 0.3078 0.2178 0.0483  -0.0009 0.0076  195 VAL A O   
1514 C CB  . VAL A 207 ? 0.2637 0.3677 0.2284 0.0414  0.0019  0.0129  195 VAL A CB  
1515 C CG1 . VAL A 207 ? 0.2532 0.3490 0.1951 0.0393  -0.0003 0.0007  195 VAL A CG1 
1516 C CG2 . VAL A 207 ? 0.2727 0.3884 0.2368 0.0404  0.0040  0.0245  195 VAL A CG2 
1517 N N   . LEU A 208 ? 0.2292 0.3071 0.2068 0.0592  0.0126  -0.0086 196 LEU A N   
1518 C CA  . LEU A 208 ? 0.2464 0.2980 0.2230 0.0624  0.0106  -0.0183 196 LEU A CA  
1519 C C   . LEU A 208 ? 0.2852 0.3241 0.2348 0.0558  0.0113  -0.0342 196 LEU A C   
1520 O O   . LEU A 208 ? 0.2834 0.3328 0.2126 0.0559  0.0189  -0.0403 196 LEU A O   
1521 C CB  . LEU A 208 ? 0.2762 0.3247 0.2733 0.0787  0.0189  -0.0234 196 LEU A CB  
1522 C CG  . LEU A 208 ? 0.2314 0.2977 0.2594 0.0868  0.0141  -0.0097 196 LEU A CG  
1523 C CD1 . LEU A 208 ? 0.2629 0.3315 0.3234 0.1058  0.0215  -0.0155 196 LEU A CD1 
1524 C CD2 . LEU A 208 ? 0.2677 0.3202 0.2918 0.0814  -0.0017 0.0043  196 LEU A CD2 
1525 N N   . ALA A 209 ? 0.2710 0.2849 0.2174 0.0482  0.0027  -0.0407 197 ALA A N   
1526 C CA  . ALA A 209 ? 0.3005 0.2955 0.2210 0.0399  -0.0010 -0.0604 197 ALA A CA  
1527 C C   . ALA A 209 ? 0.3488 0.3076 0.2702 0.0496  0.0073  -0.0776 197 ALA A C   
1528 O O   . ALA A 209 ? 0.3498 0.2904 0.2953 0.0541  0.0055  -0.0692 197 ALA A O   
1529 C CB  . ALA A 209 ? 0.3258 0.3187 0.2518 0.0210  -0.0180 -0.0567 197 ALA A CB  
1530 N N   . VAL A 210 ? 0.3622 0.3079 0.2554 0.0545  0.0178  -0.1006 198 VAL A N   
1531 C CA  . VAL A 210 ? 0.4268 0.3392 0.3254 0.0702  0.0324  -0.1193 198 VAL A CA  
1532 C C   . VAL A 210 ? 0.4812 0.3546 0.3400 0.0596  0.0295  -0.1498 198 VAL A C   
1533 O O   . VAL A 210 ? 0.5387 0.4200 0.3531 0.0497  0.0275  -0.1620 198 VAL A O   
1534 C CB  . VAL A 210 ? 0.4422 0.3764 0.3495 0.0910  0.0571  -0.1222 198 VAL A CB  
1535 C CG1 . VAL A 210 ? 0.4946 0.3955 0.4141 0.1105  0.0745  -0.1434 198 VAL A CG1 
1536 C CG2 . VAL A 210 ? 0.4305 0.4025 0.3805 0.0979  0.0544  -0.0935 198 VAL A CG2 
1537 N N   . LYS A 211 ? 0.5081 0.3349 0.3788 0.0614  0.0282  -0.1626 199 LYS A N   
1538 C CA  . LYS A 211 ? 0.6116 0.3908 0.4450 0.0533  0.0281  -0.1982 199 LYS A CA  
1539 C C   . LYS A 211 ? 0.6428 0.3709 0.5021 0.0710  0.0405  -0.2104 199 LYS A C   
1540 O O   . LYS A 211 ? 0.6351 0.3481 0.5326 0.0704  0.0309  -0.1897 199 LYS A O   
1541 C CB  . LYS A 211 ? 0.6562 0.4261 0.4776 0.0215  -0.0008 -0.2003 199 LYS A CB  
1542 C CG  . LYS A 211 ? 0.7776 0.4977 0.5547 0.0071  -0.0077 -0.2403 199 LYS A CG  
1543 C CD  . LYS A 211 ? 0.8233 0.5379 0.6088 -0.0265 -0.0395 -0.2391 199 LYS A CD  
1544 C CE  . LYS A 211 ? 0.8186 0.4894 0.5725 -0.0452 -0.0484 -0.2767 199 LYS A CE  
1545 N NZ  . LYS A 211 ? 0.8987 0.5948 0.6027 -0.0420 -0.0437 -0.2963 199 LYS A NZ  
1546 N N   . ASP A 212 ? 0.7718 0.4749 0.6122 0.0869  0.0641  -0.2404 200 ASP A N   
1547 C CA  . ASP A 212 ? 0.8064 0.4666 0.6738 0.1095  0.0700  -0.2455 200 ASP A CA  
1548 C C   . ASP A 212 ? 0.7176 0.3970 0.6433 0.1326  0.0770  -0.2133 200 ASP A C   
1549 O O   . ASP A 212 ? 0.7244 0.4581 0.6668 0.1440  0.0872  -0.1993 200 ASP A O   
1550 C CB  . ASP A 212 ? 0.8878 0.4862 0.7429 0.0881  0.0513  -0.2575 200 ASP A CB  
1551 C CG  . ASP A 212 ? 1.0455 0.6383 0.8550 0.0679  0.0402  -0.2928 200 ASP A CG  
1552 O OD1 . ASP A 212 ? 1.0862 0.6977 0.8669 0.0808  0.0550  -0.3119 200 ASP A OD1 
1553 O OD2 . ASP A 212 ? 1.0670 0.6412 0.8739 0.0366  0.0186  -0.3005 200 ASP A OD2 
1554 N N   . GLU A 213 ? 0.8362 0.4778 0.7954 0.1380  0.0677  -0.1979 201 GLU A N   
1555 C CA  . GLU A 213 ? 0.8078 0.4710 0.8195 0.1591  0.0646  -0.1639 201 GLU A CA  
1556 C C   . GLU A 213 ? 0.8006 0.4959 0.8252 0.1427  0.0444  -0.1329 201 GLU A C   
1557 O O   . GLU A 213 ? 0.7974 0.5057 0.8554 0.1556  0.0353  -0.1023 201 GLU A O   
1558 C CB  . GLU A 213 ? 0.9147 0.5232 0.9446 0.1729  0.0592  -0.1548 201 GLU A CB  
1559 C CG  . GLU A 213 ? 1.0298 0.5884 1.0539 0.1474  0.0422  -0.1438 201 GLU A CG  
1560 C CD  . GLU A 213 ? 1.1067 0.6302 1.0897 0.1184  0.0406  -0.1767 201 GLU A CD  
1561 O OE1 . GLU A 213 ? 1.1823 0.6820 1.1369 0.1266  0.0503  -0.2080 201 GLU A OE1 
1562 O OE2 . GLU A 213 ? 1.0902 0.6142 1.0702 0.0877  0.0254  -0.1714 201 GLU A OE2 
1563 N N   . ARG A 214 ? 0.6245 0.3376 0.6150 0.1130  0.0347  -0.1349 202 ARG A N   
1564 C CA  . ARG A 214 ? 0.5074 0.2496 0.5014 0.0945  0.0176  -0.1030 202 ARG A CA  
1565 C C   . ARG A 214 ? 0.4851 0.2921 0.4747 0.0947  0.0193  -0.0927 202 ARG A C   
1566 O O   . ARG A 214 ? 0.5300 0.3577 0.4952 0.0909  0.0273  -0.1112 202 ARG A O   
1567 C CB  . ARG A 214 ? 0.6595 0.3805 0.6343 0.0620  0.0052  -0.1083 202 ARG A CB  
1568 C CG  . ARG A 214 ? 0.7469 0.4861 0.7327 0.0442  -0.0062 -0.0756 202 ARG A CG  
1569 C CD  . ARG A 214 ? 0.6795 0.3786 0.6686 0.0169  -0.0141 -0.0752 202 ARG A CD  
1570 N NE  . ARG A 214 ? 0.6410 0.3742 0.6375 -0.0042 -0.0192 -0.0513 202 ARG A NE  
1571 C CZ  . ARG A 214 ? 0.8570 0.6002 0.8603 0.0000  -0.0162 -0.0197 202 ARG A CZ  
1572 N NH1 . ARG A 214 ? 0.9502 0.6707 0.9553 0.0222  -0.0146 -0.0044 202 ARG A NH1 
1573 N NH2 . ARG A 214 ? 0.6538 0.4313 0.6613 -0.0173 -0.0153 -0.0033 202 ARG A NH2 
1574 N N   . MET A 215 ? 0.4628 0.2970 0.4717 0.0986  0.0116  -0.0632 203 MET A N   
1575 C CA  . MET A 215 ? 0.3830 0.2715 0.3904 0.0960  0.0112  -0.0520 203 MET A CA  
1576 C C   . MET A 215 ? 0.4200 0.3156 0.4223 0.0788  -0.0016 -0.0287 203 MET A C   
1577 O O   . MET A 215 ? 0.4363 0.3156 0.4480 0.0830  -0.0089 -0.0088 203 MET A O   
1578 C CB  . MET A 215 ? 0.5008 0.4164 0.5398 0.1185  0.0146  -0.0416 203 MET A CB  
1579 C CG  . MET A 215 ? 0.5670 0.4888 0.6230 0.1386  0.0338  -0.0615 203 MET A CG  
1580 S SD  . MET A 215 ? 0.4994 0.4803 0.5987 0.1530  0.0363  -0.0461 203 MET A SD  
1581 C CE  . MET A 215 ? 0.5164 0.4986 0.6414 0.1773  0.0674  -0.0723 203 MET A CE  
1582 N N   . VAL A 216 ? 0.3006 0.2191 0.2872 0.0608  -0.0035 -0.0305 204 VAL A N   
1583 C CA  . VAL A 216 ? 0.3263 0.2556 0.3115 0.0448  -0.0095 -0.0123 204 VAL A CA  
1584 C C   . VAL A 216 ? 0.2727 0.2426 0.2575 0.0479  -0.0087 -0.0027 204 VAL A C   
1585 O O   . VAL A 216 ? 0.2845 0.2782 0.2649 0.0496  -0.0054 -0.0119 204 VAL A O   
1586 C CB  . VAL A 216 ? 0.3161 0.2432 0.2965 0.0234  -0.0134 -0.0219 204 VAL A CB  
1587 C CG1 . VAL A 216 ? 0.3319 0.2837 0.3202 0.0098  -0.0141 -0.0053 204 VAL A CG1 
1588 C CG2 . VAL A 216 ? 0.3952 0.2757 0.3790 0.0151  -0.0156 -0.0298 204 VAL A CG2 
1589 N N   . VAL A 217 ? 0.2642 0.2371 0.2488 0.0474  -0.0113 0.0155  205 VAL A N   
1590 C CA  . VAL A 217 ? 0.2445 0.2475 0.2263 0.0470  -0.0109 0.0221  205 VAL A CA  
1591 C C   . VAL A 217 ? 0.2268 0.2443 0.2071 0.0329  -0.0070 0.0214  205 VAL A C   
1592 O O   . VAL A 217 ? 0.2708 0.2800 0.2509 0.0225  -0.0036 0.0293  205 VAL A O   
1593 C CB  . VAL A 217 ? 0.2422 0.2387 0.2151 0.0503  -0.0164 0.0380  205 VAL A CB  
1594 C CG1 . VAL A 217 ? 0.2702 0.2919 0.2378 0.0480  -0.0158 0.0393  205 VAL A CG1 
1595 C CG2 . VAL A 217 ? 0.3005 0.2877 0.2854 0.0663  -0.0254 0.0409  205 VAL A CG2 
1596 N N   . ARG A 218 ? 0.2173 0.2577 0.1998 0.0330  -0.0067 0.0143  206 ARG A N   
1597 C CA  A ARG A 218 ? 0.2375 0.2953 0.2266 0.0235  -0.0072 0.0152  206 ARG A CA  
1598 C CA  B ARG A 218 ? 0.2458 0.3025 0.2354 0.0230  -0.0068 0.0160  206 ARG A CA  
1599 C C   . ARG A 218 ? 0.2170 0.2907 0.2098 0.0255  -0.0020 0.0240  206 ARG A C   
1600 O O   . ARG A 218 ? 0.2400 0.3219 0.2450 0.0197  0.0028  0.0288  206 ARG A O   
1601 C CB  A ARG A 218 ? 0.2567 0.3247 0.2391 0.0234  -0.0129 0.0052  206 ARG A CB  
1602 C CB  B ARG A 218 ? 0.2249 0.2913 0.2115 0.0198  -0.0140 0.0059  206 ARG A CB  
1603 C CG  A ARG A 218 ? 0.2857 0.3762 0.2759 0.0182  -0.0193 0.0095  206 ARG A CG  
1604 C CG  B ARG A 218 ? 0.1822 0.2695 0.1852 0.0110  -0.0203 0.0103  206 ARG A CG  
1605 C CD  A ARG A 218 ? 0.2189 0.3131 0.2245 0.0050  -0.0297 0.0064  206 ARG A CD  
1606 C CD  B ARG A 218 ? 0.2050 0.2961 0.1970 0.0049  -0.0349 0.0000  206 ARG A CD  
1607 N NE  A ARG A 218 ? 0.3107 0.3855 0.2999 -0.0018 -0.0381 -0.0092 206 ARG A NE  
1608 N NE  B ARG A 218 ? 0.2499 0.3185 0.2395 -0.0055 -0.0402 -0.0128 206 ARG A NE  
1609 C CZ  A ARG A 218 ? 0.2832 0.3346 0.2793 -0.0107 -0.0379 -0.0154 206 ARG A CZ  
1610 C CZ  B ARG A 218 ? 0.2466 0.3032 0.2136 -0.0113 -0.0513 -0.0293 206 ARG A CZ  
1611 N NH1 A ARG A 218 ? 0.3096 0.3542 0.3246 -0.0139 -0.0282 -0.0041 206 ARG A NH1 
1612 N NH1 B ARG A 218 ? 0.2545 0.3203 0.1922 -0.0073 -0.0574 -0.0335 206 ARG A NH1 
1613 N NH2 A ARG A 218 ? 0.3264 0.3561 0.3054 -0.0175 -0.0468 -0.0336 206 ARG A NH2 
1614 N NH2 B ARG A 218 ? 0.2666 0.2967 0.2355 -0.0226 -0.0559 -0.0423 206 ARG A NH2 
1615 N N   . SER A 219 ? 0.2338 0.3119 0.2206 0.0333  -0.0015 0.0246  207 SER A N   
1616 C CA  . SER A 219 ? 0.2067 0.2919 0.1945 0.0341  0.0029  0.0292  207 SER A CA  
1617 C C   . SER A 219 ? 0.2293 0.3113 0.2105 0.0385  0.0000  0.0292  207 SER A C   
1618 O O   . SER A 219 ? 0.2220 0.3067 0.2078 0.0430  -0.0039 0.0268  207 SER A O   
1619 C CB  . SER A 219 ? 0.2226 0.3234 0.2211 0.0349  0.0029  0.0308  207 SER A CB  
1620 O OG  . SER A 219 ? 0.2481 0.3544 0.2412 0.0373  -0.0005 0.0295  207 SER A OG  
1621 N N   . ILE A 220 ? 0.2209 0.2977 0.1937 0.0370  0.0018  0.0302  208 ILE A N   
1622 C CA  . ILE A 220 ? 0.1975 0.2707 0.1637 0.0376  -0.0070 0.0294  208 ILE A CA  
1623 C C   . ILE A 220 ? 0.2219 0.2940 0.1875 0.0340  -0.0053 0.0253  208 ILE A C   
1624 O O   . ILE A 220 ? 0.2294 0.2901 0.1824 0.0325  0.0035  0.0224  208 ILE A O   
1625 C CB  . ILE A 220 ? 0.2212 0.2765 0.1620 0.0364  -0.0125 0.0332  208 ILE A CB  
1626 C CG1 . ILE A 220 ? 0.2466 0.2935 0.1884 0.0391  -0.0134 0.0392  208 ILE A CG1 
1627 C CG2 . ILE A 220 ? 0.2488 0.3051 0.1864 0.0367  -0.0296 0.0329  208 ILE A CG2 
1628 C CD1 . ILE A 220 ? 0.2977 0.3211 0.2096 0.0370  -0.0167 0.0489  208 ILE A CD1 
1629 N N   . GLY A 221 ? 0.2121 0.2936 0.1932 0.0320  -0.0120 0.0241  209 GLY A N   
1630 C CA  . GLY A 221 ? 0.2012 0.2734 0.1789 0.0250  -0.0156 0.0184  209 GLY A CA  
1631 C C   . GLY A 221 ? 0.1819 0.2460 0.1668 0.0237  -0.0043 0.0173  209 GLY A C   
1632 O O   . GLY A 221 ? 0.2308 0.2765 0.2068 0.0182  -0.0053 0.0091  209 GLY A O   
1633 N N   . ASP A 222 ? 0.1878 0.2614 0.1860 0.0285  0.0038  0.0251  210 ASP A N   
1634 C CA  . ASP A 222 ? 0.1803 0.2433 0.1863 0.0307  0.0119  0.0284  210 ASP A CA  
1635 C C   . ASP A 222 ? 0.2061 0.2646 0.2267 0.0235  0.0114  0.0330  210 ASP A C   
1636 O O   . ASP A 222 ? 0.1861 0.2601 0.2160 0.0215  0.0125  0.0425  210 ASP A O   
1637 C CB  . ASP A 222 ? 0.1776 0.2534 0.1904 0.0382  0.0149  0.0376  210 ASP A CB  
1638 C CG  . ASP A 222 ? 0.1916 0.2591 0.2183 0.0443  0.0193  0.0450  210 ASP A CG  
1639 O OD1 . ASP A 222 ? 0.2171 0.2748 0.2495 0.0418  0.0194  0.0525  210 ASP A OD1 
1640 O OD2 . ASP A 222 ? 0.2151 0.2857 0.2520 0.0518  0.0234  0.0450  210 ASP A OD2 
1641 N N   . ALA A 223 ? 0.2139 0.2474 0.2348 0.0192  0.0128  0.0259  211 ALA A N   
1642 C CA  . ALA A 223 ? 0.2242 0.2455 0.2621 0.0097  0.0136  0.0312  211 ALA A CA  
1643 C C   . ALA A 223 ? 0.2474 0.2400 0.2906 0.0168  0.0221  0.0355  211 ALA A C   
1644 O O   . ALA A 223 ? 0.2742 0.2371 0.3250 0.0093  0.0236  0.0313  211 ALA A O   
1645 C CB  . ALA A 223 ? 0.2515 0.2657 0.2928 -0.0059 0.0031  0.0180  211 ALA A CB  
1646 N N   . THR A 224 ? 0.2372 0.2376 0.2810 0.0316  0.0264  0.0435  212 THR A N   
1647 C CA  . THR A 224 ? 0.2272 0.2048 0.2847 0.0437  0.0333  0.0480  212 THR A CA  
1648 C C   . THR A 224 ? 0.2485 0.2091 0.3197 0.0420  0.0326  0.0683  212 THR A C   
1649 O O   . THR A 224 ? 0.2817 0.2128 0.3682 0.0516  0.0373  0.0723  212 THR A O   
1650 C CB  . THR A 224 ? 0.2416 0.2404 0.3078 0.0592  0.0350  0.0526  212 THR A CB  
1651 O OG1 . THR A 224 ? 0.2461 0.2734 0.3101 0.0588  0.0252  0.0685  212 THR A OG1 
1652 C CG2 . THR A 224 ? 0.2513 0.2568 0.3057 0.0607  0.0424  0.0340  212 THR A CG2 
1653 N N   . HIS A 225 ? 0.2507 0.2263 0.3170 0.0308  0.0295  0.0824  213 HIS A N   
1654 C CA  . HIS A 225 ? 0.2686 0.2225 0.3425 0.0248  0.0325  0.1039  213 HIS A CA  
1655 C C   . HIS A 225 ? 0.3010 0.2168 0.3891 0.0118  0.0366  0.0943  213 HIS A C   
1656 O O   . HIS A 225 ? 0.3430 0.2294 0.4412 0.0076  0.0405  0.1123  213 HIS A O   
1657 C CB  . HIS A 225 ? 0.2647 0.2443 0.3271 0.0131  0.0351  0.1187  213 HIS A CB  
1658 C CG  . HIS A 225 ? 0.2442 0.2485 0.3108 0.0006  0.0361  0.1012  213 HIS A CG  
1659 N ND1 . HIS A 225 ? 0.2404 0.2718 0.2970 0.0073  0.0309  0.0870  213 HIS A ND1 
1660 C CD2 . HIS A 225 ? 0.2540 0.2598 0.3398 -0.0176 0.0394  0.0966  213 HIS A CD2 
1661 C CE1 . HIS A 225 ? 0.2309 0.2791 0.2990 -0.0036 0.0302  0.0763  213 HIS A CE1 
1662 N NE2 . HIS A 225 ? 0.2220 0.2587 0.3107 -0.0190 0.0341  0.0807  213 HIS A NE2 
1663 N N   . LEU A 226 ? 0.2931 0.2050 0.3786 0.0041  0.0341  0.0668  214 LEU A N   
1664 C CA  . LEU A 226 ? 0.3335 0.2052 0.4276 -0.0101 0.0340  0.0517  214 LEU A CA  
1665 C C   . LEU A 226 ? 0.3687 0.1974 0.4600 0.0046  0.0404  0.0365  214 LEU A C   
1666 O O   . LEU A 226 ? 0.4140 0.1990 0.5075 -0.0056 0.0414  0.0198  214 LEU A O   
1667 C CB  . LEU A 226 ? 0.3231 0.2122 0.4104 -0.0271 0.0232  0.0291  214 LEU A CB  
1668 C CG  . LEU A 226 ? 0.2977 0.2324 0.3992 -0.0394 0.0189  0.0406  214 LEU A CG  
1669 C CD1 . LEU A 226 ? 0.3528 0.3020 0.4541 -0.0530 0.0026  0.0185  214 LEU A CD1 
1670 C CD2 . LEU A 226 ? 0.3307 0.2615 0.4584 -0.0541 0.0277  0.0632  214 LEU A CD2 
1671 N N   . ALA A 227 ? 0.3529 0.1936 0.4421 0.0281  0.0459  0.0390  215 ALA A N   
1672 C CA  . ALA A 227 ? 0.3996 0.2066 0.4904 0.0444  0.0576  0.0200  215 ALA A CA  
1673 C C   . ALA A 227 ? 0.5176 0.2708 0.6311 0.0497  0.0639  0.0263  215 ALA A C   
1674 O O   . ALA A 227 ? 0.5982 0.3056 0.7076 0.0519  0.0737  0.0005  215 ALA A O   
1675 C CB  . ALA A 227 ? 0.4036 0.2431 0.5022 0.0675  0.0635  0.0254  215 ALA A CB  
1676 N N   . ALA A 228 ? 0.5069 0.2591 0.6395 0.0517  0.0592  0.0599  216 ALA A N   
1677 C CA  . ALA A 228 ? 0.6558 0.3511 0.8116 0.0581  0.0642  0.0719  216 ALA A CA  
1678 C C   . ALA A 228 ? 0.5687 0.2239 0.7239 0.0286  0.0627  0.0689  216 ALA A C   
1679 O O   . ALA A 228 ? 0.6994 0.3116 0.8627 0.0286  0.0635  0.0734  216 ALA A O   
1680 C CB  . ALA A 228 ? 0.6923 0.4086 0.8582 0.0731  0.0552  0.1100  216 ALA A CB  
1681 N N   . ALA A 229 ? 0.6207 0.3046 0.7610 0.0024  0.0556  0.0569  217 ALA A N   
1682 C CA  . ALA A 229 ? 0.5741 0.2390 0.7253 -0.0296 0.0520  0.0598  217 ALA A CA  
1683 C C   . ALA A 229 ? 0.7569 0.3602 0.9096 -0.0430 0.0518  0.0263  217 ALA A C   
1684 O O   . ALA A 229 ? 0.7177 0.2999 0.8516 -0.0290 0.0555  -0.0049 217 ALA A O   
1685 C CB  . ALA A 229 ? 0.5491 0.2730 0.6937 -0.0491 0.0430  0.0551  217 ALA A CB  
1686 N N   . PRO A 230 ? 0.7040 0.2815 0.8721 -0.0713 0.0477  0.0305  218 PRO A N   
1687 C CA  . PRO A 230 ? 0.7790 0.3053 0.9371 -0.0879 0.0410  -0.0046 218 PRO A CA  
1688 C C   . PRO A 230 ? 0.9204 0.4620 1.0612 -0.1045 0.0278  -0.0436 218 PRO A C   
1689 O O   . PRO A 230 ? 0.8920 0.4957 1.0279 -0.1055 0.0203  -0.0397 218 PRO A O   
1690 C CB  . PRO A 230 ? 0.8668 0.3808 1.0460 -0.1173 0.0375  0.0151  218 PRO A CB  
1691 C CG  . PRO A 230 ? 0.7897 0.3271 0.9790 -0.1041 0.0482  0.0615  218 PRO A CG  
1692 C CD  . PRO A 230 ? 0.7484 0.3416 0.9327 -0.0857 0.0500  0.0689  218 PRO A CD  
1693 N N   . SER A 231 ? 1.0487 0.5425 1.1633 -0.1142 0.0199  -0.0798 219 SER A N   
1694 C CA  . SER A 231 ? 1.1200 0.6219 1.2009 -0.1289 0.0026  -0.1188 219 SER A CA  
1695 C C   . SER A 231 ? 1.0079 0.5555 1.1140 -0.1647 -0.0211 -0.1151 219 SER A C   
1696 O O   . SER A 231 ? 1.0243 0.6108 1.1123 -0.1707 -0.0391 -0.1316 219 SER A O   
1697 C CB  . SER A 231 ? 1.0813 0.5187 1.1208 -0.1302 -0.0030 -0.1559 219 SER A CB  
1698 O OG  . SER A 231 ? 1.1115 0.5120 1.1660 -0.1586 -0.0151 -0.1548 219 SER A OG  
1699 N N   . ASP A 232 ? 1.0030 0.5530 1.1483 -0.1862 -0.0215 -0.0909 220 ASP A N   
1700 C CA  . ASP A 232 ? 0.9765 0.5816 1.1575 -0.2173 -0.0383 -0.0830 220 ASP A CA  
1701 C C   . ASP A 232 ? 0.8935 0.5707 1.1098 -0.2085 -0.0310 -0.0500 220 ASP A C   
1702 O O   . ASP A 232 ? 0.9352 0.6644 1.1896 -0.2285 -0.0368 -0.0361 220 ASP A O   
1703 C CB  . ASP A 232 ? 0.9443 0.5232 1.1506 -0.2463 -0.0374 -0.0745 220 ASP A CB  
1704 C CG  . ASP A 232 ? 0.9932 0.5481 1.2167 -0.2348 -0.0121 -0.0371 220 ASP A CG  
1705 O OD1 . ASP A 232 ? 1.0929 0.6557 1.3097 -0.2041 0.0035  -0.0163 220 ASP A OD1 
1706 O OD2 . ASP A 232 ? 0.9644 0.4927 1.2056 -0.2575 -0.0092 -0.0277 220 ASP A OD2 
1707 N N   . VAL A 233 ? 0.7206 0.4078 0.9164 -0.1755 -0.0158 -0.0369 221 VAL A N   
1708 C CA  . VAL A 233 ? 0.6060 0.3610 0.8120 -0.1617 -0.0073 -0.0071 221 VAL A CA  
1709 C C   . VAL A 233 ? 0.7047 0.4961 0.8718 -0.1374 -0.0139 -0.0192 221 VAL A C   
1710 O O   . VAL A 233 ? 0.6403 0.4911 0.8176 -0.1360 -0.0192 -0.0098 221 VAL A O   
1711 C CB  . VAL A 233 ? 0.6246 0.3679 0.8376 -0.1463 0.0173  0.0306  221 VAL A CB  
1712 C CG1 . VAL A 233 ? 0.4910 0.2984 0.6999 -0.1306 0.0255  0.0549  221 VAL A CG1 
1713 C CG2 . VAL A 233 ? 0.6249 0.3433 0.8721 -0.1729 0.0248  0.0488  221 VAL A CG2 
1714 N N   . ILE A 234 ? 0.8363 0.5917 0.9611 -0.1180 -0.0112 -0.0397 222 ILE A N   
1715 C CA  . ILE A 234 ? 0.8017 0.5877 0.8893 -0.0958 -0.0128 -0.0475 222 ILE A CA  
1716 C C   . ILE A 234 ? 0.8324 0.6530 0.9088 -0.1100 -0.0380 -0.0636 222 ILE A C   
1717 O O   . ILE A 234 ? 0.8749 0.6774 0.9520 -0.1340 -0.0580 -0.0846 222 ILE A O   
1718 C CB  . ILE A 234 ? 0.9144 0.6552 0.9635 -0.0744 0.0003  -0.0672 222 ILE A CB  
1719 C CG1 . ILE A 234 ? 0.8310 0.5372 0.9021 -0.0586 0.0206  -0.0491 222 ILE A CG1 
1720 C CG2 . ILE A 234 ? 0.7743 0.5502 0.7924 -0.0527 0.0043  -0.0679 222 ILE A CG2 
1721 C CD1 . ILE A 234 ? 0.9136 0.5699 0.9631 -0.0380 0.0363  -0.0712 222 ILE A CD1 
1722 O OXT . ILE A 234 ? 0.7694 0.6350 0.8365 -0.0978 -0.0416 -0.0556 222 ILE A OXT 
1731 N N   . SER B 14  ? 0.4308 1.0938 1.1566 -0.0101 -0.0574 0.1118  2   SER B N   
1732 C CA  . SER B 14  ? 0.2730 0.9387 1.0219 -0.0306 -0.0217 0.0907  2   SER B CA  
1733 C C   . SER B 14  ? 0.3129 0.8989 1.0183 -0.0266 0.0194  0.0797  2   SER B C   
1734 O O   . SER B 14  ? 0.2567 0.8088 0.9683 0.0042  0.0512  0.0862  2   SER B O   
1735 C CB  . SER B 14  ? 0.3111 1.0052 1.0506 -0.0814 -0.0404 0.0712  2   SER B CB  
1736 O OG  . SER B 14  ? 0.3323 1.0600 1.1175 -0.0992 -0.0131 0.0565  2   SER B OG  
1737 N N   . ASP B 15  ? 0.2934 0.8412 0.9503 -0.0599 0.0191  0.0624  3   ASP B N   
1738 C CA  . ASP B 15  ? 0.2290 0.6948 0.8404 -0.0617 0.0531  0.0509  3   ASP B CA  
1739 C C   . ASP B 15  ? 0.3640 0.7737 0.9011 -0.0487 0.0332  0.0518  3   ASP B C   
1740 O O   . ASP B 15  ? 0.4048 0.8066 0.8989 -0.0699 0.0049  0.0419  3   ASP B O   
1741 C CB  . ASP B 15  ? 0.2495 0.6865 0.8311 -0.1056 0.0645  0.0267  3   ASP B CB  
1742 C CG  . ASP B 15  ? 0.2597 0.5975 0.7725 -0.1081 0.0968  0.0140  3   ASP B CG  
1743 O OD1 . ASP B 15  ? 0.2624 0.5430 0.7190 -0.0892 0.0922  0.0166  3   ASP B OD1 
1744 O OD2 . ASP B 15  ? 0.3319 0.6489 0.8437 -0.1329 0.1251  0.0019  3   ASP B OD2 
1745 N N   . GLY B 16  ? 0.2801 0.6477 0.7982 -0.0164 0.0515  0.0613  4   GLY B N   
1746 C CA  . GLY B 16  ? 0.2185 0.5392 0.6700 -0.0046 0.0350  0.0618  4   GLY B CA  
1747 C C   . GLY B 16  ? 0.2195 0.4624 0.5956 -0.0190 0.0433  0.0428  4   GLY B C   
1748 O O   . GLY B 16  ? 0.2167 0.4222 0.5451 -0.0070 0.0365  0.0430  4   GLY B O   
1749 N N   . ARG B 17  ? 0.2401 0.4571 0.6048 -0.0443 0.0570  0.0278  5   ARG B N   
1750 C CA  . ARG B 17  ? 0.2550 0.3959 0.5539 -0.0528 0.0630  0.0162  5   ARG B CA  
1751 C C   . ARG B 17  ? 0.2404 0.3675 0.5032 -0.0589 0.0361  0.0056  5   ARG B C   
1752 O O   . ARG B 17  ? 0.2885 0.3695 0.5093 -0.0499 0.0350  0.0030  5   ARG B O   
1753 C CB  . ARG B 17  ? 0.2878 0.3947 0.5767 -0.0789 0.0835  0.0064  5   ARG B CB  
1754 C CG  . ARG B 17  ? 0.3839 0.4946 0.6690 -0.1092 0.0702  -0.0084 5   ARG B CG  
1755 C CD  . ARG B 17  ? 0.3952 0.4589 0.6590 -0.1359 0.0927  -0.0161 5   ARG B CD  
1756 N NE  . ARG B 17  ? 0.3981 0.5065 0.7142 -0.1460 0.1174  -0.0147 5   ARG B NE  
1757 C CZ  . ARG B 17  ? 0.3844 0.4607 0.6887 -0.1717 0.1452  -0.0216 5   ARG B CZ  
1758 N NH1 . ARG B 17  ? 0.4813 0.4755 0.7147 -0.1887 0.1457  -0.0264 5   ARG B NH1 
1759 N NH2 . ARG B 17  ? 0.3772 0.5033 0.7343 -0.1763 0.1675  -0.0218 5   ARG B NH2 
1760 N N   . GLU B 18  ? 0.2800 0.4464 0.5583 -0.0769 0.0163  -0.0015 6   GLU B N   
1761 C CA  . GLU B 18  ? 0.2657 0.4112 0.5054 -0.0861 -0.0015 -0.0155 6   GLU B CA  
1762 C C   . GLU B 18  ? 0.2437 0.3935 0.4661 -0.0649 -0.0126 -0.0088 6   GLU B C   
1763 O O   . GLU B 18  ? 0.2720 0.3821 0.4572 -0.0612 -0.0127 -0.0194 6   GLU B O   
1764 C CB  . GLU B 18  ? 0.3493 0.5305 0.5987 -0.1182 -0.0173 -0.0259 6   GLU B CB  
1765 C CG  . GLU B 18  ? 0.5399 0.6993 0.7884 -0.1461 -0.0044 -0.0385 6   GLU B CG  
1766 C CD  . GLU B 18  ? 0.8371 0.9169 1.0352 -0.1519 0.0039  -0.0553 6   GLU B CD  
1767 O OE1 . GLU B 18  ? 0.7473 0.7947 0.9210 -0.1315 0.0019  -0.0570 6   GLU B OE1 
1768 O OE2 . GLU B 18  ? 0.9017 0.9514 1.0876 -0.1769 0.0130  -0.0661 6   GLU B OE2 
1769 N N   . SER B 19  ? 0.2394 0.4361 0.4904 -0.0510 -0.0211 0.0093  7   SER B N   
1770 C CA  . SER B 19  ? 0.2308 0.4236 0.4580 -0.0321 -0.0300 0.0180  7   SER B CA  
1771 C C   . SER B 19  ? 0.2407 0.3807 0.4375 -0.0132 -0.0096 0.0176  7   SER B C   
1772 O O   . SER B 19  ? 0.2765 0.3887 0.4343 -0.0109 -0.0121 0.0090  7   SER B O   
1773 C CB  . SER B 19  ? 0.2907 0.5378 0.5619 -0.0160 -0.0403 0.0433  7   SER B CB  
1774 O OG  . SER B 19  ? 0.3460 0.5812 0.5893 0.0028  -0.0474 0.0549  7   SER B OG  
1775 N N   . PHE B 20  ? 0.2291 0.3542 0.4415 -0.0046 0.0127  0.0250  8   PHE B N   
1776 C CA  . PHE B 20  ? 0.2296 0.3030 0.4070 0.0046  0.0308  0.0254  8   PHE B CA  
1777 C C   . PHE B 20  ? 0.2469 0.2834 0.3922 -0.0065 0.0252  0.0099  8   PHE B C   
1778 O O   . PHE B 20  ? 0.2875 0.3007 0.4033 0.0006  0.0252  0.0081  8   PHE B O   
1779 C CB  . PHE B 20  ? 0.2582 0.3156 0.4496 0.0047  0.0576  0.0327  8   PHE B CB  
1780 C CG  . PHE B 20  ? 0.2982 0.2986 0.4431 0.0054  0.0747  0.0344  8   PHE B CG  
1781 C CD1 . PHE B 20  ? 0.3878 0.3727 0.5126 0.0206  0.0885  0.0442  8   PHE B CD1 
1782 C CD2 . PHE B 20  ? 0.3805 0.3411 0.4987 -0.0117 0.0750  0.0281  8   PHE B CD2 
1783 C CE1 . PHE B 20  ? 0.4401 0.3741 0.5164 0.0139  0.1033  0.0457  8   PHE B CE1 
1784 C CE2 . PHE B 20  ? 0.5148 0.4285 0.5887 -0.0161 0.0846  0.0331  8   PHE B CE2 
1785 C CZ  . PHE B 20  ? 0.4625 0.3647 0.5142 -0.0058 0.0992  0.0407  8   PHE B CZ  
1786 N N   . LEU B 21  ? 0.2800 0.3106 0.4336 -0.0234 0.0214  -0.0008 9   LEU B N   
1787 C CA  . LEU B 21  ? 0.3150 0.3055 0.4462 -0.0284 0.0180  -0.0120 9   LEU B CA  
1788 C C   . LEU B 21  ? 0.2731 0.2699 0.3950 -0.0272 0.0072  -0.0261 9   LEU B C   
1789 O O   . LEU B 21  ? 0.3310 0.3022 0.4407 -0.0205 0.0077  -0.0321 9   LEU B O   
1790 C CB  . LEU B 21  ? 0.3319 0.3029 0.4687 -0.0468 0.0198  -0.0186 9   LEU B CB  
1791 C CG  . LEU B 21  ? 0.3955 0.3477 0.5319 -0.0549 0.0349  -0.0082 9   LEU B CG  
1792 C CD1 . LEU B 21  ? 0.3944 0.3301 0.5327 -0.0783 0.0363  -0.0173 9   LEU B CD1 
1793 C CD2 . LEU B 21  ? 0.4451 0.3512 0.5503 -0.0498 0.0392  0.0019  9   LEU B CD2 
1794 N N   . GLU B 22  ? 0.2872 0.3184 0.4148 -0.0357 -0.0022 -0.0312 10  GLU B N   
1795 C CA  . GLU B 22  ? 0.3175 0.3482 0.4248 -0.0407 -0.0081 -0.0469 10  GLU B CA  
1796 C C   . GLU B 22  ? 0.2997 0.3268 0.3885 -0.0245 -0.0051 -0.0419 10  GLU B C   
1797 O O   . GLU B 22  ? 0.3231 0.3323 0.3986 -0.0232 0.0001  -0.0561 10  GLU B O   
1798 C CB  . GLU B 22  ? 0.3517 0.4188 0.4580 -0.0599 -0.0226 -0.0492 10  GLU B CB  
1799 C CG  . GLU B 22  ? 0.5422 0.5992 0.6153 -0.0763 -0.0253 -0.0696 10  GLU B CG  
1800 C CD  . GLU B 22  ? 0.8258 0.9044 0.8898 -0.1093 -0.0390 -0.0773 10  GLU B CD  
1801 O OE1 . GLU B 22  ? 0.8186 0.9340 0.9106 -0.1160 -0.0509 -0.0628 10  GLU B OE1 
1802 O OE2 . GLU B 22  ? 0.9669 1.0261 0.9955 -0.1319 -0.0359 -0.0989 10  GLU B OE2 
1803 N N   . VAL B 23  ? 0.2959 0.3377 0.3852 -0.0122 -0.0048 -0.0225 11  VAL B N   
1804 C CA  . VAL B 23  ? 0.3238 0.3541 0.3870 -0.0004 0.0010  -0.0178 11  VAL B CA  
1805 C C   . VAL B 23  ? 0.3004 0.3011 0.3580 0.0050  0.0118  -0.0196 11  VAL B C   
1806 O O   . VAL B 23  ? 0.3043 0.2967 0.3460 0.0057  0.0148  -0.0288 11  VAL B O   
1807 C CB  . VAL B 23  ? 0.2595 0.3026 0.3232 0.0124  0.0023  0.0042  11  VAL B CB  
1808 C CG1 . VAL B 23  ? 0.3210 0.3390 0.3479 0.0216  0.0134  0.0088  11  VAL B CG1 
1809 C CG2 . VAL B 23  ? 0.3263 0.4017 0.3940 0.0074  -0.0158 0.0095  11  VAL B CG2 
1810 N N   . MET B 24  ? 0.3146 0.3008 0.3851 0.0052  0.0166  -0.0109 12  MET B N   
1811 C CA  . MET B 24  ? 0.3386 0.2968 0.4000 0.0057  0.0201  -0.0076 12  MET B CA  
1812 C C   . MET B 24  ? 0.3428 0.2968 0.4165 0.0058  0.0132  -0.0226 12  MET B C   
1813 O O   . MET B 24  ? 0.3327 0.2823 0.4029 0.0093  0.0126  -0.0223 12  MET B O   
1814 C CB  . MET B 24  ? 0.4120 0.3489 0.4776 -0.0010 0.0244  0.0030  12  MET B CB  
1815 C CG  . MET B 24  ? 0.4865 0.3915 0.5331 -0.0057 0.0228  0.0123  12  MET B CG  
1816 S SD  . MET B 24  ? 0.7502 0.6184 0.7869 -0.0214 0.0270  0.0236  12  MET B SD  
1817 C CE  . MET B 24  ? 0.7022 0.5679 0.7676 -0.0223 0.0142  0.0114  12  MET B CE  
1818 N N   . ARG B 25  ? 0.3195 0.2749 0.4101 0.0009  0.0100  -0.0362 13  ARG B N   
1819 C CA  . ARG B 25  ? 0.3164 0.2615 0.4233 0.0037  0.0104  -0.0527 13  ARG B CA  
1820 C C   . ARG B 25  ? 0.3426 0.3046 0.4422 0.0049  0.0169  -0.0678 13  ARG B C   
1821 O O   . ARG B 25  ? 0.3518 0.3127 0.4693 0.0124  0.0214  -0.0758 13  ARG B O   
1822 C CB  . ARG B 25  ? 0.3417 0.2747 0.4571 -0.0066 0.0114  -0.0659 13  ARG B CB  
1823 C CG  . ARG B 25  ? 0.4632 0.3739 0.5964 -0.0028 0.0189  -0.0849 13  ARG B CG  
1824 C CD  . ARG B 25  ? 0.6384 0.5241 0.7688 -0.0180 0.0230  -0.0969 13  ARG B CD  
1825 N NE  . ARG B 25  ? 0.8290 0.7359 0.9424 -0.0376 0.0170  -0.0930 13  ARG B NE  
1826 C CZ  . ARG B 25  ? 0.7710 0.6715 0.8857 -0.0461 0.0128  -0.0812 13  ARG B CZ  
1827 N NH1 . ARG B 25  ? 0.8020 0.6665 0.9216 -0.0395 0.0126  -0.0706 13  ARG B NH1 
1828 N NH2 . ARG B 25  ? 0.4986 0.4307 0.6103 -0.0637 0.0082  -0.0791 13  ARG B NH2 
1829 N N   . SER B 26  ? 0.3262 0.3050 0.4012 -0.0033 0.0172  -0.0706 14  SER B N   
1830 C CA  . SER B 26  ? 0.3187 0.3059 0.3737 -0.0082 0.0246  -0.0852 14  SER B CA  
1831 C C   . SER B 26  ? 0.3562 0.3464 0.4038 -0.0004 0.0290  -0.0772 14  SER B C   
1832 O O   . SER B 26  ? 0.3374 0.3329 0.3886 -0.0022 0.0390  -0.0928 14  SER B O   
1833 C CB  . SER B 26  ? 0.3978 0.3973 0.4206 -0.0202 0.0178  -0.0826 14  SER B CB  
1834 O OG  . SER B 26  ? 0.4566 0.4566 0.4808 -0.0361 0.0135  -0.0947 14  SER B OG  
1835 N N   . VAL B 27  ? 0.3105 0.2965 0.3475 0.0049  0.0248  -0.0548 15  VAL B N   
1836 C CA  . VAL B 27  ? 0.2978 0.2812 0.3190 0.0055  0.0295  -0.0466 15  VAL B CA  
1837 C C   . VAL B 27  ? 0.3248 0.3118 0.3801 0.0090  0.0257  -0.0486 15  VAL B C   
1838 O O   . VAL B 27  ? 0.3280 0.3300 0.3900 0.0065  0.0305  -0.0573 15  VAL B O   
1839 C CB  . VAL B 27  ? 0.3150 0.2824 0.3115 0.0067  0.0313  -0.0239 15  VAL B CB  
1840 C CG1 . VAL B 27  ? 0.3443 0.3004 0.3157 -0.0001 0.0369  -0.0151 15  VAL B CG1 
1841 C CG2 . VAL B 27  ? 0.3347 0.3027 0.3068 0.0092  0.0347  -0.0183 15  VAL B CG2 
1842 N N   . TYR B 28  ? 0.3151 0.2900 0.3955 0.0141  0.0161  -0.0397 16  TYR B N   
1843 C CA  . TYR B 28  ? 0.3373 0.3136 0.4548 0.0206  0.0067  -0.0356 16  TYR B CA  
1844 C C   . TYR B 28  ? 0.3576 0.3539 0.5139 0.0280  0.0154  -0.0584 16  TYR B C   
1845 O O   . TYR B 28  ? 0.3028 0.3203 0.4894 0.0323  0.0128  -0.0574 16  TYR B O   
1846 C CB  . TYR B 28  ? 0.3956 0.3457 0.5278 0.0242  -0.0037 -0.0250 16  TYR B CB  
1847 C CG  . TYR B 28  ? 0.4185 0.3459 0.5251 0.0151  -0.0144 0.0007  16  TYR B CG  
1848 C CD1 . TYR B 28  ? 0.4902 0.4214 0.5817 0.0070  -0.0227 0.0163  16  TYR B CD1 
1849 C CD2 . TYR B 28  ? 0.5188 0.4186 0.6120 0.0090  -0.0144 0.0080  16  TYR B CD2 
1850 C CE1 . TYR B 28  ? 0.4265 0.3282 0.4822 -0.0089 -0.0302 0.0383  16  TYR B CE1 
1851 C CE2 . TYR B 28  ? 0.4419 0.3137 0.5046 -0.0046 -0.0190 0.0284  16  TYR B CE2 
1852 C CZ  . TYR B 28  ? 0.4461 0.3157 0.4864 -0.0143 -0.0266 0.0435  16  TYR B CZ  
1853 O OH  . TYR B 28  ? 0.5138 0.3472 0.5128 -0.0346 -0.0292 0.0623  16  TYR B OH  
1854 N N   . GLU B 29  ? 0.2979 0.2888 0.4547 0.0268  0.0277  -0.0802 17  GLU B N   
1855 C CA  . GLU B 29  ? 0.3203 0.3210 0.5107 0.0309  0.0444  -0.1063 17  GLU B CA  
1856 C C   . GLU B 29  ? 0.2831 0.3106 0.4633 0.0227  0.0569  -0.1181 17  GLU B C   
1857 O O   . GLU B 29  ? 0.2881 0.3358 0.5134 0.0289  0.0693  -0.1329 17  GLU B O   
1858 C CB  . GLU B 29  ? 0.3908 0.3708 0.5673 0.0221  0.0571  -0.1283 17  GLU B CB  
1859 C CG  . GLU B 29  ? 0.5828 0.5337 0.7760 0.0282  0.0499  -0.1218 17  GLU B CG  
1860 C CD  . GLU B 29  ? 0.7654 0.6946 0.9376 0.0121  0.0629  -0.1445 17  GLU B CD  
1861 O OE1 . GLU B 29  ? 0.8448 0.7815 0.9872 -0.0050 0.0753  -0.1640 17  GLU B OE1 
1862 O OE2 . GLU B 29  ? 0.6852 0.5861 0.8638 0.0119  0.0603  -0.1424 17  GLU B OE2 
1863 N N   . ARG B 30  ? 0.3081 0.3356 0.4332 0.0094  0.0553  -0.1110 18  ARG B N   
1864 C CA  . ARG B 30  ? 0.3116 0.3560 0.4151 -0.0027 0.0681  -0.1215 18  ARG B CA  
1865 C C   . ARG B 30  ? 0.2756 0.3473 0.4146 0.0009  0.0627  -0.1116 18  ARG B C   
1866 O O   . ARG B 30  ? 0.3145 0.4116 0.4658 -0.0074 0.0772  -0.1275 18  ARG B O   
1867 C CB  . ARG B 30  ? 0.3639 0.3920 0.3986 -0.0143 0.0651  -0.1091 18  ARG B CB  
1868 C CG  . ARG B 30  ? 0.4164 0.4479 0.4099 -0.0310 0.0796  -0.1197 18  ARG B CG  
1869 C CD  . ARG B 30  ? 0.5613 0.5657 0.4871 -0.0372 0.0757  -0.1047 18  ARG B CD  
1870 N NE  . ARG B 30  ? 0.5528 0.5468 0.4604 -0.0411 0.0723  -0.1119 18  ARG B NE  
1871 C CZ  . ARG B 30  ? 0.5618 0.5387 0.4238 -0.0435 0.0636  -0.0971 18  ARG B CZ  
1872 N NH1 . ARG B 30  ? 0.4694 0.4304 0.3016 -0.0373 0.0622  -0.0748 18  ARG B NH1 
1873 N NH2 . ARG B 30  ? 0.6024 0.5759 0.4471 -0.0535 0.0566  -0.1040 18  ARG B NH2 
1874 N N   . TYR B 31  ? 0.2518 0.3189 0.4019 0.0081  0.0415  -0.0846 19  TYR B N   
1875 C CA  . TYR B 31  ? 0.2145 0.3073 0.3916 0.0061  0.0280  -0.0685 19  TYR B CA  
1876 C C   . TYR B 31  ? 0.2162 0.3239 0.4706 0.0264  0.0138  -0.0617 19  TYR B C   
1877 O O   . TYR B 31  ? 0.2189 0.3438 0.4971 0.0260  -0.0085 -0.0387 19  TYR B O   
1878 C CB  . TYR B 31  ? 0.2177 0.2877 0.3395 -0.0074 0.0149  -0.0419 19  TYR B CB  
1879 C CG  . TYR B 31  ? 0.2498 0.3018 0.3018 -0.0226 0.0324  -0.0482 19  TYR B CG  
1880 C CD1 . TYR B 31  ? 0.2548 0.3218 0.2818 -0.0411 0.0422  -0.0540 19  TYR B CD1 
1881 C CD2 . TYR B 31  ? 0.2956 0.3176 0.3122 -0.0179 0.0388  -0.0484 19  TYR B CD2 
1882 C CE1 . TYR B 31  ? 0.3195 0.3601 0.2776 -0.0539 0.0594  -0.0587 19  TYR B CE1 
1883 C CE2 . TYR B 31  ? 0.3383 0.3415 0.2972 -0.0268 0.0521  -0.0500 19  TYR B CE2 
1884 C CZ  . TYR B 31  ? 0.3459 0.3527 0.2714 -0.0442 0.0630  -0.0548 19  TYR B CZ  
1885 O OH  . TYR B 31  ? 0.3885 0.3672 0.2503 -0.0529 0.0772  -0.0553 19  TYR B OH  
1886 N N   . LEU B 32  ? 0.2175 0.3546 0.4064 0.0420  -0.0788 -0.1128 20  LEU B N   
1887 C CA  . LEU B 32  ? 0.2762 0.3976 0.4724 0.0184  -0.0672 -0.0987 20  LEU B CA  
1888 C C   . LEU B 32  ? 0.2311 0.3894 0.4751 -0.0101 -0.0489 -0.0906 20  LEU B C   
1889 O O   . LEU B 32  ? 0.2585 0.3956 0.4932 -0.0276 -0.0347 -0.0728 20  LEU B O   
1890 C CB  . LEU B 32  ? 0.2310 0.3086 0.3763 0.0214  -0.0549 -0.0812 20  LEU B CB  
1891 C CG  . LEU B 32  ? 0.2851 0.3221 0.3819 0.0417  -0.0697 -0.0901 20  LEU B CG  
1892 C CD1 . LEU B 32  ? 0.3019 0.3087 0.3583 0.0411  -0.0530 -0.0761 20  LEU B CD1 
1893 C CD2 . LEU B 32  ? 0.2797 0.3038 0.3862 0.0433  -0.0915 -0.1054 20  LEU B CD2 
1894 N N   . VAL B 33  ? 0.2283 0.4397 0.5193 -0.0142 -0.0486 -0.1045 21  VAL B N   
1895 C CA  . VAL B 33  ? 0.2775 0.5268 0.6123 -0.0456 -0.0270 -0.0985 21  VAL B CA  
1896 C C   . VAL B 33  ? 0.2675 0.5358 0.6513 -0.0666 -0.0397 -0.1138 21  VAL B C   
1897 O O   . VAL B 33  ? 0.2742 0.5575 0.6742 -0.0501 -0.0626 -0.1358 21  VAL B O   
1898 C CB  . VAL B 33  ? 0.2440 0.5483 0.6032 -0.0394 -0.0128 -0.1058 21  VAL B CB  
1899 C CG1 . VAL B 33  ? 0.3126 0.6434 0.6975 -0.0729 0.0135  -0.0953 21  VAL B CG1 
1900 C CG2 . VAL B 33  ? 0.2476 0.5257 0.5542 -0.0196 -0.0031 -0.0902 21  VAL B CG2 
1901 N N   . GLY B 34  ? 0.3372 0.5900 0.7284 -0.1008 -0.0265 -0.0995 22  GLY B N   
1902 C CA  . GLY B 34  ? 0.3968 0.6492 0.8120 -0.1210 -0.0381 -0.1070 22  GLY B CA  
1903 C C   . GLY B 34  ? 0.3300 0.5407 0.7319 -0.1071 -0.0696 -0.1181 22  GLY B C   
1904 O O   . GLY B 34  ? 0.4623 0.6801 0.8845 -0.1085 -0.0881 -0.1335 22  GLY B O   
1905 N N   . VAL B 35  ? 0.3581 0.5188 0.7101 -0.0892 -0.0734 -0.1070 23  VAL B N   
1906 C CA  . VAL B 35  ? 0.4383 0.5530 0.7578 -0.0685 -0.0992 -0.1151 23  VAL B CA  
1907 C C   . VAL B 35  ? 0.3521 0.4125 0.6367 -0.0793 -0.0944 -0.0968 23  VAL B C   
1908 O O   . VAL B 35  ? 0.3847 0.4319 0.6420 -0.0788 -0.0748 -0.0782 23  VAL B O   
1909 C CB  . VAL B 35  ? 0.3954 0.4971 0.6712 -0.0312 -0.1049 -0.1191 23  VAL B CB  
1910 C CG1 . VAL B 35  ? 0.4677 0.5171 0.7002 -0.0130 -0.1239 -0.1245 23  VAL B CG1 
1911 C CG2 . VAL B 35  ? 0.4011 0.5450 0.7031 -0.0142 -0.1187 -0.1409 23  VAL B CG2 
1912 N N   . PRO B 36  ? 0.3968 0.4232 0.6808 -0.0875 -0.1144 -0.1033 24  PRO B N   
1913 C CA  . PRO B 36  ? 0.4060 0.3769 0.6531 -0.0923 -0.1142 -0.0890 24  PRO B CA  
1914 C C   . PRO B 36  ? 0.4155 0.3598 0.6145 -0.0587 -0.1145 -0.0880 24  PRO B C   
1915 O O   . PRO B 36  ? 0.3946 0.3485 0.5806 -0.0343 -0.1198 -0.0993 24  PRO B O   
1916 C CB  . PRO B 36  ? 0.3866 0.3283 0.6448 -0.1049 -0.1410 -0.1014 24  PRO B CB  
1917 C CG  . PRO B 36  ? 0.4232 0.3949 0.7014 -0.0874 -0.1581 -0.1233 24  PRO B CG  
1918 C CD  . PRO B 36  ? 0.3910 0.4246 0.7046 -0.0890 -0.1418 -0.1259 24  PRO B CD  
1919 N N   . GLY B 37  ? 0.3762 0.2854 0.5465 -0.0585 -0.1084 -0.0752 25  GLY B N   
1920 C CA  . GLY B 37  ? 0.3825 0.2720 0.5150 -0.0300 -0.1077 -0.0778 25  GLY B CA  
1921 C C   . GLY B 37  ? 0.3861 0.3025 0.5073 -0.0173 -0.0860 -0.0708 25  GLY B C   
1922 O O   . GLY B 37  ? 0.4237 0.3346 0.5183 0.0042  -0.0838 -0.0777 25  GLY B O   
1923 N N   . VAL B 38  ? 0.3246 0.2682 0.4627 -0.0314 -0.0691 -0.0579 26  VAL B N   
1924 C CA  . VAL B 38  ? 0.2682 0.2328 0.3939 -0.0205 -0.0509 -0.0509 26  VAL B CA  
1925 C C   . VAL B 38  ? 0.3109 0.2589 0.4214 -0.0224 -0.0403 -0.0373 26  VAL B C   
1926 O O   . VAL B 38  ? 0.3984 0.3304 0.5137 -0.0396 -0.0403 -0.0271 26  VAL B O   
1927 C CB  . VAL B 38  ? 0.2629 0.2668 0.4138 -0.0299 -0.0415 -0.0482 26  VAL B CB  
1928 C CG1 . VAL B 38  ? 0.2504 0.2666 0.3829 -0.0197 -0.0246 -0.0390 26  VAL B CG1 
1929 C CG2 . VAL B 38  ? 0.2621 0.2837 0.4279 -0.0215 -0.0571 -0.0664 26  VAL B CG2 
1930 N N   . SER B 39  ? 0.2557 0.2024 0.3452 -0.0052 -0.0335 -0.0388 27  SER B N   
1931 C CA  A SER B 39  ? 0.2519 0.1905 0.3314 -0.0029 -0.0256 -0.0298 27  SER B CA  
1932 C CA  B SER B 39  ? 0.2547 0.1931 0.3346 -0.0034 -0.0256 -0.0294 27  SER B CA  
1933 C C   . SER B 39  ? 0.2229 0.1863 0.3007 -0.0036 -0.0087 -0.0201 27  SER B C   
1934 O O   . SER B 39  ? 0.2296 0.2133 0.3087 -0.0019 -0.0039 -0.0224 27  SER B O   
1935 C CB  A SER B 39  ? 0.2977 0.2262 0.3634 0.0157  -0.0293 -0.0421 27  SER B CB  
1936 C CB  B SER B 39  ? 0.2852 0.2101 0.3515 0.0146  -0.0311 -0.0416 27  SER B CB  
1937 O OG  A SER B 39  ? 0.3570 0.2597 0.4203 0.0202  -0.0470 -0.0528 27  SER B OG  
1938 O OG  B SER B 39  ? 0.2492 0.1922 0.3051 0.0261  -0.0213 -0.0510 27  SER B OG  
1939 N N   . GLU B 40  ? 0.2075 0.1650 0.2787 -0.0039 -0.0028 -0.0106 28  GLU B N   
1940 C CA  . GLU B 40  ? 0.2085 0.1843 0.2748 -0.0037 0.0108  -0.0018 28  GLU B CA  
1941 C C   . GLU B 40  ? 0.1952 0.1705 0.2519 0.0074  0.0137  -0.0045 28  GLU B C   
1942 O O   . GLU B 40  ? 0.2341 0.1939 0.2906 0.0138  0.0050  -0.0094 28  GLU B O   
1943 C CB  . GLU B 40  ? 0.2219 0.1948 0.2892 -0.0171 0.0169  0.0129  28  GLU B CB  
1944 C CG  . GLU B 40  ? 0.2368 0.2256 0.3231 -0.0320 0.0194  0.0134  28  GLU B CG  
1945 C CD  . GLU B 40  ? 0.2973 0.2827 0.3826 -0.0499 0.0300  0.0270  28  GLU B CD  
1946 O OE1 . GLU B 40  ? 0.2836 0.2491 0.3462 -0.0493 0.0348  0.0384  28  GLU B OE1 
1947 O OE2 . GLU B 40  ? 0.2993 0.3015 0.4060 -0.0668 0.0340  0.0255  28  GLU B OE2 
1948 N N   . VAL B 41  ? 0.2070 0.1988 0.2561 0.0101  0.0240  -0.0035 29  VAL B N   
1949 C CA  . VAL B 41  ? 0.1964 0.1937 0.2410 0.0155  0.0288  -0.0060 29  VAL B CA  
1950 C C   . VAL B 41  ? 0.1970 0.1951 0.2337 0.0123  0.0335  0.0072  29  VAL B C   
1951 O O   . VAL B 41  ? 0.2091 0.2143 0.2374 0.0099  0.0391  0.0122  29  VAL B O   
1952 C CB  . VAL B 41  ? 0.2195 0.2276 0.2541 0.0170  0.0376  -0.0160 29  VAL B CB  
1953 C CG1 . VAL B 41  ? 0.2173 0.2371 0.2543 0.0170  0.0445  -0.0199 29  VAL B CG1 
1954 C CG2 . VAL B 41  ? 0.2381 0.2440 0.2750 0.0218  0.0345  -0.0299 29  VAL B CG2 
1955 N N   . TRP B 42  ? 0.2078 0.1955 0.2439 0.0150  0.0287  0.0114  30  TRP B N   
1956 C CA  . TRP B 42  ? 0.2084 0.1921 0.2313 0.0144  0.0319  0.0229  30  TRP B CA  
1957 C C   . TRP B 42  ? 0.1962 0.1900 0.2191 0.0189  0.0328  0.0162  30  TRP B C   
1958 O O   . TRP B 42  ? 0.2074 0.2007 0.2406 0.0252  0.0246  0.0077  30  TRP B O   
1959 C CB  . TRP B 42  ? 0.2435 0.2000 0.2556 0.0140  0.0245  0.0324  30  TRP B CB  
1960 C CG  . TRP B 42  ? 0.2457 0.1943 0.2558 0.0013  0.0293  0.0413  30  TRP B CG  
1961 C CD1 . TRP B 42  ? 0.2546 0.2160 0.2812 -0.0051 0.0308  0.0357  30  TRP B CD1 
1962 C CD2 . TRP B 42  ? 0.2617 0.1896 0.2527 -0.0084 0.0341  0.0554  30  TRP B CD2 
1963 N NE1 . TRP B 42  ? 0.2645 0.2191 0.2907 -0.0204 0.0360  0.0446  30  TRP B NE1 
1964 C CE2 . TRP B 42  ? 0.2619 0.1964 0.2648 -0.0241 0.0406  0.0573  30  TRP B CE2 
1965 C CE3 . TRP B 42  ? 0.3003 0.2022 0.2620 -0.0064 0.0339  0.0661  30  TRP B CE3 
1966 C CZ2 . TRP B 42  ? 0.2973 0.2176 0.2867 -0.0415 0.0507  0.0695  30  TRP B CZ2 
1967 C CZ3 . TRP B 42  ? 0.3341 0.2164 0.2742 -0.0213 0.0441  0.0795  30  TRP B CZ3 
1968 C CH2 . TRP B 42  ? 0.3349 0.2271 0.2898 -0.0408 0.0539  0.0813  30  TRP B CH2 
1969 N N   . LEU B 43  ? 0.1991 0.2012 0.2107 0.0155  0.0410  0.0178  31  LEU B N   
1970 C CA  . LEU B 43  ? 0.1869 0.1948 0.1939 0.0133  0.0439  0.0127  31  LEU B CA  
1971 C C   . LEU B 43  ? 0.2185 0.2158 0.2153 0.0175  0.0378  0.0208  31  LEU B C   
1972 O O   . LEU B 43  ? 0.2379 0.2257 0.2165 0.0197  0.0391  0.0318  31  LEU B O   
1973 C CB  . LEU B 43  ? 0.2101 0.2149 0.1945 0.0081  0.0515  0.0139  31  LEU B CB  
1974 C CG  . LEU B 43  ? 0.2216 0.2287 0.2042 0.0051  0.0565  0.0058  31  LEU B CG  
1975 C CD1 . LEU B 43  ? 0.2659 0.2559 0.2126 0.0037  0.0584  0.0083  31  LEU B CD1 
1976 C CD2 . LEU B 43  ? 0.2216 0.2421 0.2187 -0.0001 0.0630  -0.0078 31  LEU B CD2 
1977 N N   . ILE B 44  ? 0.1969 0.1974 0.2061 0.0202  0.0302  0.0132  32  ILE B N   
1978 C CA  . ILE B 44  ? 0.2068 0.1910 0.2029 0.0271  0.0200  0.0195  32  ILE B CA  
1979 C C   . ILE B 44  ? 0.2090 0.2020 0.2090 0.0217  0.0186  0.0116  32  ILE B C   
1980 O O   . ILE B 44  ? 0.1958 0.2118 0.2235 0.0161  0.0196  -0.0040 32  ILE B O   
1981 C CB  . ILE B 44  ? 0.2291 0.2022 0.2352 0.0380  0.0048  0.0146  32  ILE B CB  
1982 C CG1 . ILE B 44  ? 0.2696 0.2248 0.2651 0.0382  0.0063  0.0243  32  ILE B CG1 
1983 C CG2 . ILE B 44  ? 0.2679 0.2187 0.2555 0.0473  -0.0090 0.0187  32  ILE B CG2 
1984 C CD1 . ILE B 44  ? 0.2861 0.2189 0.2830 0.0489  -0.0116 0.0185  32  ILE B CD1 
1985 N N   . ARG B 45  ? 0.2310 0.2068 0.2042 0.0228  0.0160  0.0207  33  ARG B N   
1986 C CA  . ARG B 45  ? 0.2185 0.1969 0.1952 0.0161  0.0104  0.0127  33  ARG B CA  
1987 C C   . ARG B 45  ? 0.2522 0.2285 0.2445 0.0278  -0.0085 0.0049  33  ARG B C   
1988 O O   . ARG B 45  ? 0.2583 0.2104 0.2306 0.0422  -0.0182 0.0138  33  ARG B O   
1989 C CB  . ARG B 45  ? 0.2670 0.2207 0.2045 0.0152  0.0096  0.0231  33  ARG B CB  
1990 C CG  . ARG B 45  ? 0.2575 0.2087 0.1970 0.0041  0.0027  0.0149  33  ARG B CG  
1991 C CD  . ARG B 45  ? 0.2859 0.2035 0.1794 0.0046  -0.0019 0.0244  33  ARG B CD  
1992 N NE  . ARG B 45  ? 0.3078 0.2199 0.2042 -0.0111 -0.0093 0.0159  33  ARG B NE  
1993 C CZ  . ARG B 45  ? 0.3548 0.2343 0.2173 -0.0090 -0.0226 0.0199  33  ARG B CZ  
1994 N NH1 . ARG B 45  ? 0.3964 0.2475 0.2171 0.0101  -0.0283 0.0312  33  ARG B NH1 
1995 N NH2 . ARG B 45  ? 0.3409 0.2186 0.2138 -0.0270 -0.0303 0.0102  33  ARG B NH2 
1996 N N   . HIS B 46  ? 0.2474 0.2016 0.2640 0.0419  -0.0045 0.0562  34  HIS B N   
1997 C CA  . HIS B 46  ? 0.2453 0.2194 0.2482 0.0536  0.0067  0.0426  34  HIS B CA  
1998 C C   . HIS B 46  ? 0.2418 0.2352 0.2602 0.0634  0.0158  0.0314  34  HIS B C   
1999 O O   . HIS B 46  ? 0.2315 0.2209 0.2759 0.0634  0.0191  0.0308  34  HIS B O   
2000 C CB  . HIS B 46  ? 0.2439 0.2211 0.2369 0.0502  0.0080  0.0329  34  HIS B CB  
2001 C CG  . HIS B 46  ? 0.2412 0.2177 0.2562 0.0423  0.0063  0.0249  34  HIS B CG  
2002 N ND1 . HIS B 46  ? 0.2406 0.2305 0.2708 0.0455  0.0092  0.0085  34  HIS B ND1 
2003 C CD2 . HIS B 46  ? 0.2598 0.2163 0.2812 0.0307  0.0020  0.0326  34  HIS B CD2 
2004 C CE1 . HIS B 46  ? 0.2909 0.2670 0.3413 0.0363  0.0079  0.0050  34  HIS B CE1 
2005 N NE2 . HIS B 46  ? 0.3053 0.2638 0.3532 0.0278  0.0036  0.0220  34  HIS B NE2 
2006 N N   . ALA B 47  ? 0.2476 0.2594 0.2457 0.0729  0.0208  0.0231  35  ALA B N   
2007 C CA  . ALA B 47  ? 0.2692 0.2932 0.2603 0.0812  0.0297  0.0092  35  ALA B CA  
2008 C C   . ALA B 47  ? 0.2513 0.2775 0.2416 0.0743  0.0243  -0.0142 35  ALA B C   
2009 O O   . ALA B 47  ? 0.2538 0.2798 0.2554 0.0639  0.0150  -0.0158 35  ALA B O   
2010 C CB  . ALA B 47  ? 0.2809 0.3219 0.2421 0.0924  0.0328  0.0143  35  ALA B CB  
2011 N N   . ASP B 48  ? 0.2701 0.2967 0.2419 0.0788  0.0311  -0.0326 36  ASP B N   
2012 C CA  . ASP B 48  ? 0.2961 0.3128 0.2672 0.0684  0.0259  -0.0585 36  ASP B CA  
2013 C C   . ASP B 48  ? 0.3243 0.3644 0.2904 0.0571  0.0051  -0.0648 36  ASP B C   
2014 O O   . ASP B 48  ? 0.3088 0.3756 0.2538 0.0625  -0.0040 -0.0587 36  ASP B O   
2015 C CB  . ASP B 48  ? 0.3496 0.3543 0.2855 0.0750  0.0380  -0.0809 36  ASP B CB  
2016 C CG  . ASP B 48  ? 0.3796 0.3632 0.3101 0.0610  0.0313  -0.1116 36  ASP B CG  
2017 O OD1 . ASP B 48  ? 0.4247 0.3790 0.3870 0.0589  0.0420  -0.1166 36  ASP B OD1 
2018 O OD2 . ASP B 48  ? 0.4370 0.4327 0.3345 0.0506  0.0127  -0.1290 36  ASP B OD2 
2019 N N   . SER B 49  ? 0.3094 0.3409 0.3014 0.0412  -0.0022 -0.0748 37  SER B N   
2020 C CA  . SER B 49  ? 0.3407 0.3948 0.3388 0.0257  -0.0216 -0.0860 37  SER B CA  
2021 C C   . SER B 49  ? 0.4182 0.4470 0.4131 0.0092  -0.0270 -0.1164 37  SER B C   
2022 O O   . SER B 49  ? 0.4845 0.5256 0.4573 -0.0020 -0.0458 -0.1357 37  SER B O   
2023 C CB  . SER B 49  ? 0.3079 0.3748 0.3461 0.0174  -0.0232 -0.0681 37  SER B CB  
2024 O OG  . SER B 49  ? 0.3232 0.4135 0.3603 0.0301  -0.0206 -0.0460 37  SER B OG  
2025 N N   . TYR B 50  ? 0.3843 0.3740 0.3994 0.0067  -0.0128 -0.1209 38  TYR B N   
2026 C CA  . TYR B 50  ? 0.4254 0.3843 0.4493 -0.0125 -0.0176 -0.1473 38  TYR B CA  
2027 C C   . TYR B 50  ? 0.5521 0.4729 0.5320 -0.0075 -0.0076 -0.1797 38  TYR B C   
2028 O O   . TYR B 50  ? 0.5582 0.4553 0.5226 -0.0270 -0.0191 -0.2106 38  TYR B O   
2029 C CB  . TYR B 50  ? 0.4200 0.3500 0.4893 -0.0171 -0.0062 -0.1334 38  TYR B CB  
2030 C CG  . TYR B 50  ? 0.3343 0.2920 0.4382 -0.0293 -0.0143 -0.1090 38  TYR B CG  
2031 C CD1 . TYR B 50  ? 0.3467 0.3250 0.4712 -0.0523 -0.0304 -0.1173 38  TYR B CD1 
2032 C CD2 . TYR B 50  ? 0.3416 0.3017 0.4572 -0.0199 -0.0049 -0.0784 38  TYR B CD2 
2033 C CE1 . TYR B 50  ? 0.3487 0.3533 0.5089 -0.0611 -0.0298 -0.0932 38  TYR B CE1 
2034 C CE2 . TYR B 50  ? 0.3537 0.3323 0.4892 -0.0292 -0.0055 -0.0579 38  TYR B CE2 
2035 C CZ  . TYR B 50  ? 0.3019 0.3037 0.4628 -0.0484 -0.0144 -0.0648 38  TYR B CZ  
2036 O OH  . TYR B 50  ? 0.3233 0.3453 0.5095 -0.0560 -0.0076 -0.0428 38  TYR B OH  
2037 N N   . THR B 51  ? 0.5210 0.4316 0.4802 0.0167  0.0157  -0.1742 39  THR B N   
2038 C CA  . THR B 51  ? 0.6047 0.4726 0.5205 0.0249  0.0354  -0.2053 39  THR B CA  
2039 C C   . THR B 51  ? 0.5724 0.4527 0.4140 0.0248  0.0261  -0.2239 39  THR B C   
2040 O O   . THR B 51  ? 0.7537 0.5919 0.5413 0.0271  0.0397  -0.2505 39  THR B O   
2041 C CB  . THR B 51  ? 0.7178 0.5652 0.6552 0.0516  0.0717  -0.1911 39  THR B CB  
2042 O OG1 . THR B 51  ? 0.6282 0.5109 0.5522 0.0691  0.0796  -0.1671 39  THR B OG1 
2043 C CG2 . THR B 51  ? 0.6824 0.5215 0.6918 0.0514  0.0740  -0.1656 39  THR B CG2 
2044 N N   . GLY B 52  ? 0.5704 0.5023 0.4049 0.0232  0.0034  -0.2036 40  GLY B N   
2045 C CA  . GLY B 52  ? 0.6870 0.6331 0.4503 0.0255  -0.0072 -0.2130 40  GLY B CA  
2046 C C   . GLY B 52  ? 0.8091 0.7811 0.5507 0.0007  -0.0508 -0.2259 40  GLY B C   
2047 O O   . GLY B 52  ? 1.0010 0.9585 0.6745 -0.0063 -0.0599 -0.2364 40  GLY B O   
2048 N N   . LEU B 53  ? 0.8213 0.8277 0.6251 -0.0156 -0.0752 -0.2116 41  LEU B N   
2049 C CA  . LEU B 53  ? 1.0626 1.1108 0.8625 -0.0368 -0.1186 -0.2135 41  LEU B CA  
2050 C C   . LEU B 53  ? 1.0302 1.0532 0.8421 -0.0715 -0.1407 -0.2417 41  LEU B C   
2051 O O   . LEU B 53  ? 1.0406 1.0360 0.8986 -0.0809 -0.1277 -0.2521 41  LEU B O   
2052 C CB  . LEU B 53  ? 0.9895 1.1013 0.8519 -0.0303 -0.1307 -0.1729 41  LEU B CB  
2053 C CG  . LEU B 53  ? 0.8836 1.0436 0.7151 -0.0241 -0.1586 -0.1563 41  LEU B CG  
2054 C CD1 . LEU B 53  ? 0.6415 0.7727 0.3929 -0.0035 -0.1390 -0.1545 41  LEU B CD1 
2055 C CD2 . LEU B 53  ? 0.8374 1.0514 0.7347 -0.0099 -0.1596 -0.1148 41  LEU B CD2 
2056 N N   . GLU B 54  ? 1.0532 1.0800 0.8241 -0.0917 -0.1744 -0.2463 42  GLU B N   
2057 C CA  . GLU B 54  ? 1.2116 1.2006 0.9777 -0.1268 -0.1977 -0.2704 42  GLU B CA  
2058 C C   . GLU B 54  ? 1.2228 1.2572 1.0867 -0.1500 -0.2183 -0.2550 42  GLU B C   
2059 O O   . GLU B 54  ? 1.2977 1.2982 1.2002 -0.1652 -0.2066 -0.2664 42  GLU B O   
2060 C CB  . GLU B 54  ? 1.2702 1.2445 0.9562 -0.1418 -0.2341 -0.2786 42  GLU B CB  
2061 C CG  . GLU B 54  ? 1.3470 1.2580 0.9242 -0.1229 -0.2098 -0.2976 42  GLU B CG  
2062 C CD  . GLU B 54  ? 1.3728 1.1980 0.9141 -0.1231 -0.1929 -0.3370 42  GLU B CD  
2063 O OE1 . GLU B 54  ? 1.3474 1.1438 0.9269 -0.1152 -0.1583 -0.3443 42  GLU B OE1 
2064 O OE2 . GLU B 54  ? 1.2914 1.0955 0.7856 -0.1182 -0.2189 -0.3682 42  GLU B OE2 
2065 N N   . ASP B 55  ? 1.1477 1.2566 1.0563 -0.1514 -0.2454 -0.2239 43  ASP B N   
2066 C CA  . ASP B 55  ? 0.9637 1.1224 0.9713 -0.1706 -0.2585 -0.2022 43  ASP B CA  
2067 C C   . ASP B 55  ? 0.9504 1.1665 1.0217 -0.1420 -0.2369 -0.1696 43  ASP B C   
2068 O O   . ASP B 55  ? 0.9361 1.1632 0.9747 -0.1105 -0.2222 -0.1600 43  ASP B O   
2069 C CB  . ASP B 55  ? 0.8857 1.0820 0.9110 -0.1991 -0.3080 -0.1885 43  ASP B CB  
2070 C CG  . ASP B 55  ? 0.9419 1.1816 1.0584 -0.2308 -0.3061 -0.1757 43  ASP B CG  
2071 O OD1 . ASP B 55  ? 0.8072 1.0314 0.9702 -0.2278 -0.2764 -0.1750 43  ASP B OD1 
2072 O OD2 . ASP B 55  ? 0.9327 1.2511 1.0988 -0.2417 -0.3225 -0.1951 43  ASP B OD2 
2073 N N   . TYR B 56  ? 0.7995 1.0484 0.9593 -0.1543 -0.2320 -0.1503 44  TYR B N   
2074 C CA  . TYR B 56  ? 0.7864 1.0726 1.0046 -0.1299 -0.2034 -0.1200 44  TYR B CA  
2075 C C   . TYR B 56  ? 0.5983 0.9610 0.8902 -0.1332 -0.2192 -0.0839 44  TYR B C   
2076 O O   . TYR B 56  ? 0.6258 1.0163 0.9596 -0.1628 -0.2321 -0.0840 44  TYR B O   
2077 C CB  . TYR B 56  ? 0.7644 1.0060 1.0124 -0.1362 -0.1697 -0.1200 44  TYR B CB  
2078 C CG  . TYR B 56  ? 0.9576 1.1221 1.1398 -0.1282 -0.1507 -0.1465 44  TYR B CG  
2079 C CD1 . TYR B 56  ? 1.0526 1.1673 1.2068 -0.1527 -0.1643 -0.1844 44  TYR B CD1 
2080 C CD2 . TYR B 56  ? 0.7668 0.9077 0.9174 -0.0961 -0.1195 -0.1338 44  TYR B CD2 
2081 C CE1 . TYR B 56  ? 0.9894 1.0345 1.0912 -0.1404 -0.1412 -0.2067 44  TYR B CE1 
2082 C CE2 . TYR B 56  ? 0.9045 0.9842 1.0099 -0.0869 -0.1015 -0.1530 44  TYR B CE2 
2083 C CZ  . TYR B 56  ? 0.9970 1.0299 1.0805 -0.1066 -0.1097 -0.1886 44  TYR B CZ  
2084 O OH  . TYR B 56  ? 1.0589 1.0312 1.1056 -0.0930 -0.0859 -0.2059 44  TYR B OH  
2085 N N   . ASP B 57  ? 0.4894 0.8904 0.7922 -0.0999 -0.2080 -0.0564 45  ASP B N   
2086 C CA  . ASP B 57  ? 0.4680 0.9279 0.8334 -0.0875 -0.2161 -0.0302 45  ASP B CA  
2087 C C   . ASP B 57  ? 0.3403 0.8247 0.7714 -0.0727 -0.1741 -0.0009 45  ASP B C   
2088 O O   . ASP B 57  ? 0.3063 0.8358 0.7921 -0.0646 -0.1722 0.0197  45  ASP B O   
2089 C CB  . ASP B 57  ? 0.5216 0.9900 0.8423 -0.0611 -0.2323 -0.0165 45  ASP B CB  
2090 C CG  . ASP B 57  ? 0.6491 1.1048 0.9165 -0.0789 -0.2791 -0.0389 45  ASP B CG  
2091 O OD1 . ASP B 57  ? 0.6692 1.1178 0.9468 -0.1100 -0.3005 -0.0673 45  ASP B OD1 
2092 O OD2 . ASP B 57  ? 0.6937 1.1436 0.9047 -0.0614 -0.2912 -0.0301 45  ASP B OD2 
2093 N N   . GLY B 58  ? 0.4142 0.8642 0.8393 -0.0705 -0.1405 0.0016  46  GLY B N   
2094 C CA  . GLY B 58  ? 0.3547 0.8087 0.8232 -0.0577 -0.0969 0.0260  46  GLY B CA  
2095 C C   . GLY B 58  ? 0.4192 0.8344 0.8988 -0.0814 -0.0783 0.0187  46  GLY B C   
2096 O O   . GLY B 58  ? 0.3101 0.7144 0.7988 -0.1130 -0.0987 0.0004  46  GLY B O   
2097 N N   . ASP B 59  ? 0.2623 0.6440 0.7256 -0.0644 -0.0368 0.0317  47  ASP B N   
2098 C CA  . ASP B 59  ? 0.1939 0.5290 0.6538 -0.0821 -0.0155 0.0292  47  ASP B CA  
2099 C C   . ASP B 59  ? 0.2081 0.4815 0.6032 -0.0900 -0.0321 -0.0004 47  ASP B C   
2100 O O   . ASP B 59  ? 0.2107 0.4557 0.5441 -0.0681 -0.0304 -0.0078 47  ASP B O   
2101 C CB  . ASP B 59  ? 0.2120 0.5220 0.6462 -0.0579 0.0297  0.0501  47  ASP B CB  
2102 C CG  . ASP B 59  ? 0.3992 0.6618 0.8226 -0.0728 0.0544  0.0562  47  ASP B CG  
2103 O OD1 . ASP B 59  ? 0.3170 0.5505 0.7396 -0.0962 0.0374  0.0413  47  ASP B OD1 
2104 O OD2 . ASP B 59  ? 0.3178 0.5667 0.7273 -0.0598 0.0925  0.0764  47  ASP B OD2 
2105 N N   . PRO B 60  ? 0.2362 0.4892 0.6488 -0.1205 -0.0483 -0.0180 48  PRO B N   
2106 C CA  . PRO B 60  ? 0.2578 0.4482 0.6131 -0.1233 -0.0572 -0.0461 48  PRO B CA  
2107 C C   . PRO B 60  ? 0.2442 0.3825 0.5560 -0.1038 -0.0291 -0.0365 48  PRO B C   
2108 O O   . PRO B 60  ? 0.2685 0.3674 0.5317 -0.0922 -0.0316 -0.0522 48  PRO B O   
2109 C CB  . PRO B 60  ? 0.2983 0.4705 0.6934 -0.1607 -0.0708 -0.0610 48  PRO B CB  
2110 C CG  . PRO B 60  ? 0.3687 0.5800 0.8261 -0.1724 -0.0562 -0.0315 48  PRO B CG  
2111 C CD  . PRO B 60  ? 0.2602 0.5395 0.7406 -0.1523 -0.0558 -0.0126 48  PRO B CD  
2112 N N   . ARG B 61  ? 0.2321 0.3704 0.5591 -0.0997 -0.0020 -0.0092 49  ARG B N   
2113 C CA  . ARG B 61  ? 0.2285 0.3194 0.5093 -0.0846 0.0181  0.0027  49  ARG B CA  
2114 C C   . ARG B 61  ? 0.2667 0.3635 0.5032 -0.0565 0.0251  0.0093  49  ARG B C   
2115 O O   . ARG B 61  ? 0.2766 0.3348 0.4701 -0.0458 0.0337  0.0164  49  ARG B O   
2116 C CB  . ARG B 61  ? 0.2783 0.3566 0.5782 -0.0952 0.0437  0.0289  49  ARG B CB  
2117 C CG  . ARG B 61  ? 0.3564 0.4152 0.6985 -0.1240 0.0397  0.0268  49  ARG B CG  
2118 C CD  . ARG B 61  ? 0.4340 0.4661 0.7771 -0.1313 0.0673  0.0574  49  ARG B CD  
2119 N NE  . ARG B 61  ? 0.5044 0.5783 0.8753 -0.1333 0.0880  0.0762  49  ARG B NE  
2120 C CZ  . ARG B 61  ? 0.4097 0.4807 0.7498 -0.1197 0.1186  0.0993  49  ARG B CZ  
2121 N NH1 . ARG B 61  ? 0.4868 0.5167 0.7603 -0.1049 0.1281  0.1074  49  ARG B NH1 
2122 N NH2 . ARG B 61  ? 0.5257 0.6324 0.8971 -0.1209 0.1388  0.1132  49  ARG B NH2 
2123 N N   . ASP B 62  ? 0.2033 0.3459 0.4515 -0.0456 0.0189  0.0085  50  ASP B N   
2124 C CA  . ASP B 62  ? 0.2086 0.3526 0.4193 -0.0191 0.0277  0.0161  50  ASP B CA  
2125 C C   . ASP B 62  ? 0.1730 0.3552 0.3873 -0.0096 0.0055  0.0063  50  ASP B C   
2126 O O   . ASP B 62  ? 0.1877 0.4110 0.4264 0.0027  0.0082  0.0189  50  ASP B O   
2127 C CB  . ASP B 62  ? 0.1997 0.3539 0.4219 -0.0104 0.0580  0.0385  50  ASP B CB  
2128 C CG  . ASP B 62  ? 0.2053 0.3415 0.3807 0.0152  0.0727  0.0451  50  ASP B CG  
2129 O OD1 . ASP B 62  ? 0.2266 0.3411 0.3613 0.0247  0.0599  0.0366  50  ASP B OD1 
2130 O OD2 . ASP B 62  ? 0.2502 0.3920 0.4343 0.0237  0.1017  0.0601  50  ASP B OD2 
2131 N N   . PRO B 63  ? 0.1915 0.3578 0.3779 -0.0125 -0.0143 -0.0140 51  PRO B N   
2132 C CA  . PRO B 63  ? 0.2145 0.4136 0.3929 -0.0068 -0.0374 -0.0231 51  PRO B CA  
2133 C C   . PRO B 63  ? 0.1825 0.3788 0.3221 0.0200  -0.0312 -0.0131 51  PRO B C   
2134 O O   . PRO B 63  ? 0.2113 0.3715 0.3224 0.0310  -0.0133 -0.0066 51  PRO B O   
2135 C CB  . PRO B 63  ? 0.2456 0.4149 0.3981 -0.0212 -0.0528 -0.0513 51  PRO B CB  
2136 C CG  . PRO B 63  ? 0.3058 0.4237 0.4418 -0.0184 -0.0326 -0.0502 51  PRO B CG  
2137 C CD  . PRO B 63  ? 0.2413 0.3599 0.4075 -0.0227 -0.0153 -0.0289 51  PRO B CD  
2138 N N   . ALA B 64  ? 0.2159 0.4497 0.3543 0.0280  -0.0496 -0.0106 52  ALA B N   
2139 C CA  . ALA B 64  ? 0.2572 0.4831 0.3551 0.0512  -0.0456 -0.0016 52  ALA B CA  
2140 C C   . ALA B 64  ? 0.3028 0.4937 0.3507 0.0492  -0.0481 -0.0202 52  ALA B C   
2141 O O   . ALA B 64  ? 0.2764 0.4492 0.3196 0.0324  -0.0539 -0.0419 52  ALA B O   
2142 C CB  . ALA B 64  ? 0.2424 0.5188 0.3530 0.0623  -0.0652 0.0126  52  ALA B CB  
2143 N N   . LEU B 65  ? 0.2703 0.4487 0.2837 0.0673  -0.0400 -0.0106 53  LEU B N   
2144 C CA  . LEU B 65  ? 0.3080 0.4596 0.2794 0.0683  -0.0366 -0.0245 53  LEU B CA  
2145 C C   . LEU B 65  ? 0.3048 0.4720 0.2477 0.0599  -0.0578 -0.0434 53  LEU B C   
2146 O O   . LEU B 65  ? 0.3086 0.5144 0.2562 0.0587  -0.0803 -0.0368 53  LEU B O   
2147 C CB  . LEU B 65  ? 0.3146 0.4550 0.2602 0.0874  -0.0231 -0.0062 53  LEU B CB  
2148 C CG  . LEU B 65  ? 0.2652 0.3786 0.2248 0.0915  -0.0058 0.0081  53  LEU B CG  
2149 C CD1 . LEU B 65  ? 0.2859 0.3886 0.2224 0.1060  0.0040  0.0251  53  LEU B CD1 
2150 C CD2 . LEU B 65  ? 0.2808 0.3660 0.2492 0.0796  0.0008  -0.0038 53  LEU B CD2 
2151 N N   . SER B 66  ? 0.3478 0.4826 0.2607 0.0535  -0.0511 -0.0673 54  SER B N   
2152 C CA  . SER B 66  ? 0.3507 0.4831 0.2125 0.0467  -0.0655 -0.0900 54  SER B CA  
2153 C C   . SER B 66  ? 0.3987 0.5354 0.2079 0.0658  -0.0588 -0.0763 54  SER B C   
2154 O O   . SER B 66  ? 0.3764 0.5131 0.1965 0.0827  -0.0407 -0.0510 54  SER B O   
2155 C CB  . SER B 66  ? 0.4409 0.5256 0.2850 0.0382  -0.0503 -0.1210 54  SER B CB  
2156 O OG  . SER B 66  ? 0.4218 0.4808 0.2611 0.0565  -0.0179 -0.1118 54  SER B OG  
2157 N N   . GLU B 67  ? 0.3411 0.4320 0.2968 0.0055  -0.0900 -0.0200 55  GLU B N   
2158 C CA  . GLU B 67  ? 0.3627 0.4544 0.2963 0.0106  -0.0919 -0.0120 55  GLU B CA  
2159 C C   . GLU B 67  ? 0.3536 0.4287 0.2756 0.0137  -0.0784 -0.0104 55  GLU B C   
2160 O O   . GLU B 67  ? 0.3710 0.4438 0.2866 0.0195  -0.0752 0.0009  55  GLU B O   
2161 C CB  . GLU B 67  ? 0.3962 0.4965 0.3086 0.0055  -0.1013 -0.0197 55  GLU B CB  
2162 C CG  . GLU B 67  ? 0.4955 0.5974 0.3825 0.0100  -0.1035 -0.0106 55  GLU B CG  
2163 C CD  . GLU B 67  ? 0.6561 0.7691 0.5204 0.0046  -0.1145 -0.0174 55  GLU B CD  
2164 O OE1 . GLU B 67  ? 0.5616 0.6810 0.4311 -0.0033 -0.1204 -0.0307 55  GLU B OE1 
2165 O OE2 . GLU B 67  ? 0.7658 0.8810 0.6061 0.0074  -0.1172 -0.0094 55  GLU B OE2 
2166 N N   . LYS B 68  ? 0.3356 0.3990 0.2565 0.0098  -0.0702 -0.0213 56  LYS B N   
2167 C CA  . LYS B 68  ? 0.3239 0.3742 0.2385 0.0134  -0.0578 -0.0202 56  LYS B CA  
2168 C C   . LYS B 68  ? 0.3177 0.3649 0.2487 0.0183  -0.0527 -0.0094 56  LYS B C   
2169 O O   . LYS B 68  ? 0.3301 0.3739 0.2554 0.0226  -0.0466 -0.0020 56  LYS B O   
2170 C CB  . LYS B 68  ? 0.3318 0.3699 0.2473 0.0096  -0.0510 -0.0333 56  LYS B CB  
2171 C CG  . LYS B 68  ? 0.3532 0.3793 0.2675 0.0142  -0.0386 -0.0327 56  LYS B CG  
2172 C CD  . LYS B 68  ? 0.3953 0.4084 0.3104 0.0114  -0.0331 -0.0458 56  LYS B CD  
2173 C CE  . LYS B 68  ? 0.5258 0.5281 0.4456 0.0172  -0.0219 -0.0445 56  LYS B CE  
2174 N NZ  . LYS B 68  ? 0.6038 0.5912 0.5270 0.0156  -0.0172 -0.0559 56  LYS B NZ  
2175 N N   . GLY B 69  ? 0.2985 0.3469 0.2498 0.0169  -0.0544 -0.0093 57  GLY B N   
2176 C CA  . GLY B 69  ? 0.2902 0.3360 0.2560 0.0207  -0.0495 -0.0006 57  GLY B CA  
2177 C C   . GLY B 69  ? 0.2832 0.3349 0.2482 0.0258  -0.0525 0.0111  57  GLY B C   
2178 O O   . GLY B 69  ? 0.2718 0.3178 0.2387 0.0291  -0.0460 0.0180  57  GLY B O   
2179 N N   . ARG B 70  ? 0.2928 0.3556 0.2558 0.0264  -0.0627 0.0138  58  ARG B N   
2180 C CA  . ARG B 70  ? 0.2971 0.3628 0.2585 0.0322  -0.0655 0.0262  58  ARG B CA  
2181 C C   . ARG B 70  ? 0.3147 0.3727 0.2558 0.0339  -0.0593 0.0314  58  ARG B C   
2182 O O   . ARG B 70  ? 0.3120 0.3645 0.2547 0.0375  -0.0548 0.0409  58  ARG B O   
2183 C CB  . ARG B 70  ? 0.3442 0.4243 0.3064 0.0336  -0.0788 0.0292  58  ARG B CB  
2184 C CG  . ARG B 70  ? 0.3098 0.4006 0.2972 0.0324  -0.0840 0.0254  58  ARG B CG  
2185 C CD  . ARG B 70  ? 0.3644 0.4724 0.3577 0.0362  -0.0981 0.0311  58  ARG B CD  
2186 N NE  . ARG B 70  ? 0.3811 0.4981 0.3560 0.0320  -0.1079 0.0261  58  ARG B NE  
2187 C CZ  . ARG B 70  ? 0.3946 0.5210 0.3734 0.0244  -0.1134 0.0138  58  ARG B CZ  
2188 N NH1 . ARG B 70  ? 0.3865 0.5137 0.3867 0.0196  -0.1092 0.0057  58  ARG B NH1 
2189 N NH2 . ARG B 70  ? 0.4135 0.5476 0.3724 0.0204  -0.1225 0.0092  58  ARG B NH2 
2190 N N   . ALA B 71  ? 0.3198 0.3768 0.2421 0.0307  -0.0581 0.0243  59  ALA B N   
2191 C CA  . ALA B 71  ? 0.3061 0.3576 0.2094 0.0315  -0.0509 0.0281  59  ALA B CA  
2192 C C   . ALA B 71  ? 0.3175 0.3602 0.2296 0.0322  -0.0390 0.0283  59  ALA B C   
2193 O O   . ALA B 71  ? 0.3245 0.3637 0.2323 0.0339  -0.0331 0.0365  59  ALA B O   
2194 C CB  . ALA B 71  ? 0.3195 0.3725 0.2019 0.0276  -0.0510 0.0181  59  ALA B CB  
2195 N N   . GLN B 72  ? 0.2998 0.3391 0.2247 0.0307  -0.0357 0.0198  60  GLN B N   
2196 C CA  . GLN B 72  ? 0.2748 0.3079 0.2091 0.0318  -0.0262 0.0205  60  GLN B CA  
2197 C C   . GLN B 72  ? 0.2795 0.3116 0.2262 0.0336  -0.0255 0.0299  60  GLN B C   
2198 O O   . GLN B 72  ? 0.2802 0.3092 0.2279 0.0342  -0.0186 0.0343  60  GLN B O   
2199 C CB  . GLN B 72  ? 0.2705 0.2993 0.2160 0.0302  -0.0243 0.0117  60  GLN B CB  
2200 C CG  . GLN B 72  ? 0.2862 0.3123 0.2216 0.0285  -0.0232 0.0008  60  GLN B CG  
2201 C CD  . GLN B 72  ? 0.2883 0.3073 0.2357 0.0270  -0.0218 -0.0061 60  GLN B CD  
2202 O OE1 . GLN B 72  ? 0.2718 0.2908 0.2324 0.0254  -0.0249 -0.0041 60  GLN B OE1 
2203 N NE2 . GLN B 72  ? 0.3411 0.3531 0.2835 0.0276  -0.0166 -0.0144 60  GLN B NE2 
2204 N N   . ALA B 73  ? 0.2923 0.3275 0.2504 0.0342  -0.0321 0.0320  61  ALA B N   
2205 C CA  . ALA B 73  ? 0.2796 0.3126 0.2500 0.0363  -0.0306 0.0395  61  ALA B CA  
2206 C C   . ALA B 73  ? 0.2592 0.2897 0.2205 0.0387  -0.0298 0.0497  61  ALA B C   
2207 O O   . ALA B 73  ? 0.2821 0.3066 0.2490 0.0389  -0.0239 0.0545  61  ALA B O   
2208 C CB  . ALA B 73  ? 0.2628 0.3011 0.2483 0.0370  -0.0370 0.0388  61  ALA B CB  
2209 N N   . ARG B 74  ? 0.2785 0.3124 0.2242 0.0396  -0.0350 0.0530  62  ARG B N   
2210 C CA  . ARG B 74  ? 0.3020 0.3315 0.2363 0.0414  -0.0334 0.0642  62  ARG B CA  
2211 C C   . ARG B 74  ? 0.3283 0.3524 0.2558 0.0384  -0.0222 0.0643  62  ARG B C   
2212 O O   . ARG B 74  ? 0.3237 0.3410 0.2527 0.0382  -0.0170 0.0721  62  ARG B O   
2213 C CB  . ARG B 74  ? 0.3191 0.3542 0.2343 0.0424  -0.0415 0.0677  62  ARG B CB  
2214 C CG  . ARG B 74  ? 0.3993 0.4420 0.3232 0.0462  -0.0539 0.0706  62  ARG B CG  
2215 C CD  . ARG B 74  ? 0.4343 0.4835 0.3372 0.0474  -0.0636 0.0764  62  ARG B CD  
2216 N NE  . ARG B 74  ? 0.5384 0.6001 0.4526 0.0499  -0.0767 0.0749  62  ARG B NE  
2217 C CZ  . ARG B 74  ? 0.5862 0.6588 0.4972 0.0459  -0.0837 0.0643  62  ARG B CZ  
2218 N NH1 . ARG B 74  ? 0.4207 0.4917 0.3148 0.0401  -0.0792 0.0542  62  ARG B NH1 
2219 N NH2 . ARG B 74  ? 0.5506 0.6365 0.4766 0.0477  -0.0953 0.0631  62  ARG B NH2 
2220 N N   . LEU B 75  ? 0.2883 0.3154 0.2094 0.0359  -0.0181 0.0553  63  LEU B N   
2221 C CA  . LEU B 75  ? 0.2906 0.3160 0.2080 0.0335  -0.0074 0.0547  63  LEU B CA  
2222 C C   . LEU B 75  ? 0.2597 0.2824 0.1958 0.0326  -0.0024 0.0542  63  LEU B C   
2223 O O   . LEU B 75  ? 0.2906 0.3114 0.2279 0.0304  0.0048  0.0583  63  LEU B O   
2224 C CB  . LEU B 75  ? 0.3314 0.3611 0.2406 0.0325  -0.0040 0.0442  63  LEU B CB  
2225 C CG  . LEU B 75  ? 0.3677 0.4004 0.2541 0.0319  -0.0070 0.0431  63  LEU B CG  
2226 C CD1 . LEU B 75  ? 0.3847 0.4196 0.2663 0.0312  -0.0050 0.0295  63  LEU B CD1 
2227 C CD2 . LEU B 75  ? 0.4015 0.4333 0.2713 0.0301  -0.0003 0.0517  63  LEU B CD2 
2228 N N   . LEU B 76  ? 0.2527 0.2756 0.2026 0.0335  -0.0061 0.0491  64  LEU B N   
2229 C CA  . LEU B 76  ? 0.2322 0.2529 0.1973 0.0322  -0.0024 0.0487  64  LEU B CA  
2230 C C   . LEU B 76  ? 0.2653 0.2801 0.2347 0.0319  -0.0014 0.0567  64  LEU B C   
2231 O O   . LEU B 76  ? 0.2657 0.2780 0.2404 0.0289  0.0046  0.0582  64  LEU B O   
2232 C CB  . LEU B 76  ? 0.2357 0.2571 0.2118 0.0328  -0.0064 0.0426  64  LEU B CB  
2233 C CG  . LEU B 76  ? 0.2338 0.2530 0.2229 0.0311  -0.0037 0.0422  64  LEU B CG  
2234 C CD1 . LEU B 76  ? 0.2695 0.2910 0.2604 0.0294  0.0017  0.0397  64  LEU B CD1 
2235 C CD2 . LEU B 76  ? 0.2972 0.3165 0.2949 0.0312  -0.0077 0.0380  64  LEU B CD2 
2236 N N   . ALA B 77  ? 0.2625 0.2752 0.2312 0.0349  -0.0075 0.0616  65  ALA B N   
2237 C CA  . ALA B 77  ? 0.2581 0.2629 0.2328 0.0361  -0.0065 0.0691  65  ALA B CA  
2238 C C   . ALA B 77  ? 0.2744 0.2730 0.2386 0.0337  -0.0006 0.0768  65  ALA B C   
2239 O O   . ALA B 77  ? 0.2967 0.2869 0.2673 0.0314  0.0048  0.0802  65  ALA B O   
2240 C CB  . ALA B 77  ? 0.2989 0.3048 0.2767 0.0414  -0.0152 0.0731  65  ALA B CB  
2241 N N   . ALA B 78  ? 0.2679 0.2698 0.2153 0.0333  -0.0006 0.0792  66  ALA B N   
2242 C CA  . ALA B 78  ? 0.3027 0.2995 0.2390 0.0297  0.0068  0.0865  66  ALA B CA  
2243 C C   . ALA B 78  ? 0.2827 0.2820 0.2269 0.0240  0.0161  0.0813  66  ALA B C   
2244 O O   . ALA B 78  ? 0.3248 0.3177 0.2702 0.0196  0.0230  0.0865  66  ALA B O   
2245 C CB  . ALA B 78  ? 0.3062 0.3075 0.2211 0.0300  0.0056  0.0891  66  ALA B CB  
2246 N N   . ARG B 79  ? 0.3050 0.3139 0.2546 0.0239  0.0163  0.0713  67  ARG B N   
2247 C CA  . ARG B 79  ? 0.2802 0.2947 0.2394 0.0196  0.0234  0.0664  67  ARG B CA  
2248 C C   . ARG B 79  ? 0.2667 0.2757 0.2397 0.0165  0.0246  0.0669  67  ARG B C   
2249 O O   . ARG B 79  ? 0.3161 0.3251 0.2937 0.0108  0.0312  0.0679  67  ARG B O   
2250 C CB  . ARG B 79  ? 0.2755 0.2993 0.2393 0.0221  0.0215  0.0568  67  ARG B CB  
2251 C CG  . ARG B 79  ? 0.2729 0.3037 0.2501 0.0192  0.0260  0.0524  67  ARG B CG  
2252 C CD  . ARG B 79  ? 0.2700 0.3069 0.2530 0.0231  0.0230  0.0447  67  ARG B CD  
2253 N NE  . ARG B 79  ? 0.2508 0.2952 0.2471 0.0212  0.0251  0.0419  67  ARG B NE  
2254 C CZ  . ARG B 79  ? 0.2788 0.3293 0.2816 0.0247  0.0237  0.0368  67  ARG B CZ  
2255 N NH1 . ARG B 79  ? 0.2391 0.2866 0.2368 0.0296  0.0210  0.0331  67  ARG B NH1 
2256 N NH2 . ARG B 79  ? 0.2374 0.2966 0.2523 0.0232  0.0245  0.0356  67  ARG B NH2 
2257 N N   . LEU B 80  ? 0.2800 0.2842 0.2598 0.0196  0.0188  0.0657  68  LEU B N   
2258 C CA  . LEU B 80  ? 0.2544 0.2532 0.2463 0.0166  0.0204  0.0641  68  LEU B CA  
2259 C C   . LEU B 80  ? 0.2980 0.2830 0.2897 0.0159  0.0227  0.0716  68  LEU B C   
2260 O O   . LEU B 80  ? 0.3137 0.2922 0.3146 0.0125  0.0257  0.0693  68  LEU B O   
2261 C CB  . LEU B 80  ? 0.2714 0.2721 0.2713 0.0197  0.0151  0.0582  68  LEU B CB  
2262 C CG  . LEU B 80  ? 0.2796 0.2907 0.2808 0.0200  0.0134  0.0514  68  LEU B CG  
2263 C CD1 . LEU B 80  ? 0.3199 0.3308 0.3278 0.0216  0.0093  0.0469  68  LEU B CD1 
2264 C CD2 . LEU B 80  ? 0.2937 0.3114 0.2988 0.0154  0.0179  0.0488  68  LEU B CD2 
2265 N N   . ALA B 81  ? 0.3026 0.2820 0.2832 0.0187  0.0218  0.0804  69  ALA B N   
2266 C CA  . ALA B 81  ? 0.2967 0.2604 0.2773 0.0195  0.0234  0.0892  69  ALA B CA  
2267 C C   . ALA B 81  ? 0.3522 0.3076 0.3366 0.0112  0.0326  0.0899  69  ALA B C   
2268 O O   . ALA B 81  ? 0.3915 0.3326 0.3830 0.0105  0.0351  0.0920  69  ALA B O   
2269 C CB  . ALA B 81  ? 0.3390 0.2994 0.3041 0.0236  0.0203  0.0998  69  ALA B CB  
2270 N N   . GLY B 82  ? 0.3469 0.3112 0.3279 0.0046  0.0381  0.0877  70  GLY B N   
2271 C CA  . GLY B 82  ? 0.4022 0.3616 0.3878 -0.0051 0.0470  0.0879  70  GLY B CA  
2272 C C   . GLY B 82  ? 0.3752 0.3425 0.3749 -0.0109 0.0483  0.0770  70  GLY B C   
2273 O O   . GLY B 82  ? 0.4390 0.4058 0.4441 -0.0203 0.0550  0.0752  70  GLY B O   
2274 N N   . VAL B 83  ? 0.3038 0.2788 0.3091 -0.0064 0.0420  0.0697  71  VAL B N   
2275 C CA  . VAL B 83  ? 0.2959 0.2786 0.3117 -0.0113 0.0418  0.0601  71  VAL B CA  
2276 C C   . VAL B 83  ? 0.3038 0.2724 0.3253 -0.0119 0.0421  0.0574  71  VAL B C   
2277 O O   . VAL B 83  ? 0.2999 0.2624 0.3209 -0.0042 0.0380  0.0589  71  VAL B O   
2278 C CB  . VAL B 83  ? 0.3152 0.3125 0.3316 -0.0059 0.0354  0.0549  71  VAL B CB  
2279 C CG1 . VAL B 83  ? 0.3068 0.3107 0.3313 -0.0098 0.0338  0.0468  71  VAL B CG1 
2280 C CG2 . VAL B 83  ? 0.3112 0.3217 0.3234 -0.0047 0.0364  0.0559  71  VAL B CG2 
2281 N N   . PRO B 84  ? 0.2830 0.2474 0.3108 -0.0209 0.0468  0.0522  72  PRO B N   
2282 C CA  . PRO B 84  ? 0.2886 0.2396 0.3214 -0.0213 0.0479  0.0473  72  PRO B CA  
2283 C C   . PRO B 84  ? 0.2866 0.2470 0.3209 -0.0166 0.0422  0.0408  72  PRO B C   
2284 O O   . PRO B 84  ? 0.2954 0.2710 0.3301 -0.0197 0.0393  0.0355  72  PRO B O   
2285 C CB  . PRO B 84  ? 0.3103 0.2595 0.3480 -0.0339 0.0535  0.0406  72  PRO B CB  
2286 C CG  . PRO B 84  ? 0.3706 0.3244 0.4064 -0.0391 0.0574  0.0467  72  PRO B CG  
2287 C CD  . PRO B 84  ? 0.3101 0.2807 0.3411 -0.0316 0.0521  0.0504  72  PRO B CD  
2288 N N   . LEU B 85  ? 0.2723 0.2244 0.3082 -0.0088 0.0405  0.0420  73  LEU B N   
2289 C CA  . LEU B 85  ? 0.2747 0.2342 0.3126 -0.0049 0.0365  0.0364  73  LEU B CA  
2290 C C   . LEU B 85  ? 0.2644 0.2110 0.3086 -0.0041 0.0406  0.0315  73  LEU B C   
2291 O O   . LEU B 85  ? 0.2817 0.2139 0.3297 0.0000  0.0435  0.0362  73  LEU B O   
2292 C CB  . LEU B 85  ? 0.3070 0.2728 0.3432 0.0045  0.0304  0.0411  73  LEU B CB  
2293 C CG  . LEU B 85  ? 0.3839 0.3626 0.4136 0.0057  0.0260  0.0440  73  LEU B CG  
2294 C CD1 . LEU B 85  ? 0.3131 0.2950 0.3417 0.0140  0.0203  0.0468  73  LEU B CD1 
2295 C CD2 . LEU B 85  ? 0.3214 0.3121 0.3507 0.0009  0.0249  0.0378  73  LEU B CD2 
2296 N N   . HIS B 86  ? 0.2385 0.1901 0.2835 -0.0072 0.0411  0.0227  74  HIS B N   
2297 C CA  . HIS B 86  ? 0.2417 0.1819 0.2921 -0.0084 0.0471  0.0153  74  HIS B CA  
2298 C C   . HIS B 86  ? 0.2675 0.2125 0.3220 -0.0025 0.0463  0.0120  74  HIS B C   
2299 O O   . HIS B 86  ? 0.2629 0.1989 0.3237 -0.0015 0.0522  0.0060  74  HIS B O   
2300 C CB  . HIS B 86  ? 0.2617 0.2012 0.3084 -0.0203 0.0512  0.0058  74  HIS B CB  
2301 C CG  . HIS B 86  ? 0.2555 0.1922 0.3009 -0.0269 0.0524  0.0090  74  HIS B CG  
2302 N ND1 . HIS B 86  ? 0.2457 0.1984 0.2871 -0.0313 0.0478  0.0109  74  HIS B ND1 
2303 C CD2 . HIS B 86  ? 0.2901 0.2103 0.3388 -0.0287 0.0577  0.0124  74  HIS B CD2 
2304 C CE1 . HIS B 86  ? 0.2568 0.2047 0.2995 -0.0365 0.0509  0.0142  74  HIS B CE1 
2305 N NE2 . HIS B 86  ? 0.2724 0.1995 0.3185 -0.0356 0.0570  0.0156  74  HIS B NE2 
2306 N N   . GLY B 87  ? 0.2365 0.1947 0.2884 0.0013  0.0400  0.0154  75  GLY B N   
2307 C CA  . GLY B 87  ? 0.2343 0.1979 0.2915 0.0065  0.0391  0.0136  75  GLY B CA  
2308 C C   . GLY B 87  ? 0.2290 0.2041 0.2831 0.0104  0.0315  0.0193  75  GLY B C   
2309 O O   . GLY B 87  ? 0.2228 0.2030 0.2692 0.0080  0.0278  0.0224  75  GLY B O   
2310 N N   . VAL B 88  ? 0.2233 0.2031 0.2847 0.0160  0.0297  0.0197  76  VAL B N   
2311 C CA  . VAL B 88  ? 0.2130 0.2029 0.2723 0.0186  0.0230  0.0231  76  VAL B CA  
2312 C C   . VAL B 88  ? 0.2079 0.2039 0.2730 0.0180  0.0247  0.0181  76  VAL B C   
2313 O O   . VAL B 88  ? 0.2110 0.2069 0.2883 0.0216  0.0279  0.0158  76  VAL B O   
2314 C CB  . VAL B 88  ? 0.2186 0.2091 0.2812 0.0259  0.0175  0.0305  76  VAL B CB  
2315 C CG1 . VAL B 88  ? 0.2633 0.2638 0.3234 0.0272  0.0111  0.0315  76  VAL B CG1 
2316 C CG2 . VAL B 88  ? 0.2552 0.2391 0.3104 0.0257  0.0170  0.0364  76  VAL B CG2 
2317 N N   . TRP B 89  ? 0.2012 0.2025 0.2584 0.0136  0.0231  0.0167  77  TRP B N   
2318 C CA  . TRP B 89  ? 0.2079 0.2146 0.2679 0.0115  0.0249  0.0132  77  TRP B CA  
2319 C C   . TRP B 89  ? 0.2054 0.2175 0.2637 0.0128  0.0185  0.0165  77  TRP B C   
2320 O O   . TRP B 89  ? 0.2190 0.2305 0.2701 0.0141  0.0135  0.0202  77  TRP B O   
2321 C CB  . TRP B 89  ? 0.2188 0.2241 0.2690 0.0042  0.0296  0.0090  77  TRP B CB  
2322 C CG  . TRP B 89  ? 0.2532 0.2533 0.3057 0.0019  0.0372  0.0029  77  TRP B CG  
2323 C CD1 . TRP B 89  ? 0.2670 0.2602 0.3170 0.0005  0.0390  0.0016  77  TRP B CD1 
2324 C CD2 . TRP B 89  ? 0.2771 0.2780 0.3358 0.0001  0.0453  -0.0037 77  TRP B CD2 
2325 N NE1 . TRP B 89  ? 0.3459 0.3340 0.3996 -0.0017 0.0474  -0.0060 77  TRP B NE1 
2326 C CE2 . TRP B 89  ? 0.2902 0.2834 0.3492 -0.0016 0.0517  -0.0095 77  TRP B CE2 
2327 C CE3 . TRP B 89  ? 0.3130 0.3205 0.3778 -0.0007 0.0485  -0.0058 77  TRP B CE3 
2328 C CZ2 . TRP B 89  ? 0.3754 0.3671 0.4401 -0.0032 0.0616  -0.0180 77  TRP B CZ2 
2329 C CZ3 . TRP B 89  ? 0.3310 0.3389 0.4023 -0.0025 0.0585  -0.0135 77  TRP B CZ3 
2330 C CH2 . TRP B 89  ? 0.3570 0.3569 0.4280 -0.0032 0.0651  -0.0198 77  TRP B CH2 
2331 N N   . ALA B 90  ? 0.1941 0.2115 0.2600 0.0120  0.0193  0.0142  78  ALA B N   
2332 C CA  . ALA B 90  ? 0.2015 0.2228 0.2668 0.0120  0.0139  0.0158  78  ALA B CA  
2333 C C   . ALA B 90  ? 0.1966 0.2212 0.2660 0.0068  0.0178  0.0125  78  ALA B C   
2334 O O   . ALA B 90  ? 0.2056 0.2333 0.2831 0.0050  0.0243  0.0087  78  ALA B O   
2335 C CB  . ALA B 90  ? 0.2304 0.2576 0.3053 0.0177  0.0079  0.0176  78  ALA B CB  
2336 N N   . SER B 91  ? 0.2070 0.2302 0.2706 0.0041  0.0146  0.0136  79  SER B N   
2337 C CA  . SER B 91  ? 0.1933 0.2193 0.2625 -0.0012 0.0173  0.0112  79  SER B CA  
2338 C C   . SER B 91  ? 0.2357 0.2733 0.3237 0.0008  0.0161  0.0081  79  SER B C   
2339 O O   . SER B 91  ? 0.2176 0.2594 0.3109 0.0070  0.0105  0.0094  79  SER B O   
2340 C CB  . SER B 91  ? 0.2370 0.2569 0.2976 -0.0028 0.0126  0.0132  79  SER B CB  
2341 O OG  . SER B 91  ? 0.2657 0.2889 0.3344 -0.0066 0.0118  0.0105  79  SER B OG  
2342 N N   . GLY B 92  ? 0.1940 0.2378 0.2923 -0.0046 0.0213  0.0046  80  GLY B N   
2343 C CA  . GLY B 92  ? 0.1999 0.2583 0.3193 -0.0028 0.0191  0.0014  80  GLY B CA  
2344 C C   . GLY B 92  ? 0.1857 0.2488 0.3079 -0.0028 0.0097  0.0014  80  GLY B C   
2345 O O   . GLY B 92  ? 0.2031 0.2804 0.3424 -0.0005 0.0052  -0.0007 80  GLY B O   
2346 N N   . ALA B 93  ? 0.1984 0.2508 0.3053 -0.0056 0.0067  0.0028  81  ALA B N   
2347 C CA  . ALA B 93  ? 0.1819 0.2375 0.2903 -0.0071 -0.0012 0.0007  81  ALA B CA  
2348 C C   . ALA B 93  ? 0.1951 0.2596 0.3072 0.0009  -0.0101 0.0021  81  ALA B C   
2349 O O   . ALA B 93  ? 0.1926 0.2522 0.2966 0.0073  -0.0108 0.0064  81  ALA B O   
2350 C CB  . ALA B 93  ? 0.2188 0.2586 0.3087 -0.0089 -0.0022 0.0021  81  ALA B CB  
2351 N N   . HIS B 94  ? 0.1917 0.2689 0.3146 -0.0004 -0.0172 -0.0013 82  HIS B N   
2352 C CA  . HIS B 94  ? 0.2140 0.3012 0.3401 0.0073  -0.0265 0.0013  82  HIS B CA  
2353 C C   . HIS B 94  ? 0.2105 0.2863 0.3153 0.0115  -0.0302 0.0051  82  HIS B C   
2354 O O   . HIS B 94  ? 0.2134 0.2897 0.3150 0.0189  -0.0331 0.0106  82  HIS B O   
2355 C CB  . HIS B 94  ? 0.2013 0.3054 0.3404 0.0040  -0.0352 -0.0034 82  HIS B CB  
2356 C CG  . HIS B 94  ? 0.2069 0.3264 0.3709 0.0000  -0.0316 -0.0074 82  HIS B CG  
2357 N ND1 . HIS B 94  ? 0.2079 0.3373 0.3895 0.0063  -0.0282 -0.0051 82  HIS B ND1 
2358 C CD2 . HIS B 94  ? 0.2068 0.3341 0.3824 -0.0100 -0.0303 -0.0141 82  HIS B CD2 
2359 C CE1 . HIS B 94  ? 0.2160 0.3605 0.4197 0.0007  -0.0246 -0.0105 82  HIS B CE1 
2360 N NE2 . HIS B 94  ? 0.2120 0.3558 0.4125 -0.0098 -0.0259 -0.0157 82  HIS B NE2 
2361 N N   . ARG B 95  ? 0.2078 0.2724 0.2982 0.0070  -0.0293 0.0025  83  ARG B N   
2362 C CA  . ARG B 95  ? 0.2377 0.2937 0.3097 0.0110  -0.0318 0.0050  83  ARG B CA  
2363 C C   . ARG B 95  ? 0.2214 0.2685 0.2865 0.0155  -0.0259 0.0109  83  ARG B C   
2364 O O   . ARG B 95  ? 0.2569 0.3019 0.3121 0.0204  -0.0280 0.0149  83  ARG B O   
2365 C CB  . ARG B 95  ? 0.2577 0.3040 0.3186 0.0060  -0.0316 -0.0002 83  ARG B CB  
2366 C CG  . ARG B 95  ? 0.2523 0.2862 0.3120 0.0016  -0.0237 -0.0010 83  ARG B CG  
2367 C CD  . ARG B 95  ? 0.3034 0.3285 0.3567 -0.0036 -0.0248 -0.0075 83  ARG B CD  
2368 N NE  . ARG B 95  ? 0.3326 0.3426 0.3822 -0.0065 -0.0179 -0.0065 83  ARG B NE  
2369 C CZ  . ARG B 95  ? 0.3562 0.3640 0.4138 -0.0125 -0.0130 -0.0060 83  ARG B CZ  
2370 N NH1 . ARG B 95  ? 0.3796 0.4006 0.4519 -0.0168 -0.0133 -0.0078 83  ARG B NH1 
2371 N NH2 . ARG B 95  ? 0.5531 0.5455 0.6040 -0.0142 -0.0075 -0.0032 83  ARG B NH2 
2372 N N   . ALA B 96  ? 0.2069 0.2495 0.2765 0.0132  -0.0185 0.0112  84  ALA B N   
2373 C CA  . ALA B 96  ? 0.2128 0.2488 0.2770 0.0162  -0.0135 0.0155  84  ALA B CA  
2374 C C   . ALA B 96  ? 0.2074 0.2491 0.2806 0.0213  -0.0140 0.0186  84  ALA B C   
2375 O O   . ALA B 96  ? 0.2123 0.2493 0.2789 0.0252  -0.0135 0.0229  84  ALA B O   
2376 C CB  . ALA B 96  ? 0.2051 0.2351 0.2689 0.0115  -0.0062 0.0146  84  ALA B CB  
2377 N N   . GLN B 97  ? 0.1982 0.2501 0.2880 0.0216  -0.0147 0.0167  85  GLN B N   
2378 C CA  . GLN B 97  ? 0.1796 0.2364 0.2805 0.0281  -0.0155 0.0199  85  GLN B CA  
2379 C C   . GLN B 97  ? 0.2329 0.2902 0.3264 0.0340  -0.0234 0.0256  85  GLN B C   
2380 O O   . GLN B 97  ? 0.2133 0.2648 0.3050 0.0391  -0.0222 0.0309  85  GLN B O   
2381 C CB  . GLN B 97  ? 0.2110 0.2823 0.3335 0.0281  -0.0165 0.0164  85  GLN B CB  
2382 C CG  . GLN B 97  ? 0.2292 0.3006 0.3600 0.0225  -0.0065 0.0113  85  GLN B CG  
2383 C CD  . GLN B 97  ? 0.2293 0.2949 0.3637 0.0257  0.0018  0.0117  85  GLN B CD  
2384 O OE1 . GLN B 97  ? 0.2601 0.3297 0.4072 0.0333  0.0007  0.0137  85  GLN B OE1 
2385 N NE2 . GLN B 97  ? 0.2285 0.2846 0.3526 0.0203  0.0099  0.0095  85  GLN B NE2 
2386 N N   . GLN B 98  ? 0.2194 0.2828 0.3078 0.0327  -0.0313 0.0244  86  GLN B N   
2387 C CA  . GLN B 98  ? 0.2394 0.3049 0.3183 0.0375  -0.0393 0.0298  86  GLN B CA  
2388 C C   . GLN B 98  ? 0.2147 0.2673 0.2746 0.0382  -0.0357 0.0338  86  GLN B C   
2389 O O   . GLN B 98  ? 0.2627 0.3124 0.3163 0.0431  -0.0378 0.0410  86  GLN B O   
2390 C CB  . GLN B 98  ? 0.2795 0.3540 0.3545 0.0339  -0.0474 0.0251  86  GLN B CB  
2391 C CG  . GLN B 98  ? 0.3981 0.4846 0.4748 0.0386  -0.0585 0.0292  86  GLN B CG  
2392 C CD  . GLN B 98  ? 0.3571 0.4542 0.4308 0.0332  -0.0669 0.0224  86  GLN B CD  
2393 O OE1 . GLN B 98  ? 0.2913 0.3912 0.3732 0.0261  -0.0647 0.0141  86  GLN B OE1 
2394 N NE2 . GLN B 98  ? 0.3553 0.4571 0.4151 0.0356  -0.0760 0.0257  86  GLN B NE2 
2395 N N   . THR B 99  ? 0.2173 0.2627 0.2687 0.0333  -0.0305 0.0296  87  THR B N   
2396 C CA  . THR B 99  ? 0.2310 0.2672 0.2680 0.0336  -0.0264 0.0325  87  THR B CA  
2397 C C   . THR B 99  ? 0.2258 0.2559 0.2669 0.0356  -0.0208 0.0370  87  THR B C   
2398 O O   . THR B 99  ? 0.2290 0.2542 0.2621 0.0377  -0.0198 0.0426  87  THR B O   
2399 C CB  . THR B 99  ? 0.2158 0.2471 0.2467 0.0293  -0.0225 0.0274  87  THR B CB  
2400 O OG1 . THR B 99  ? 0.2308 0.2655 0.2586 0.0270  -0.0271 0.0222  87  THR B OG1 
2401 C CG2 . THR B 99  ? 0.2213 0.2471 0.2399 0.0303  -0.0190 0.0300  87  THR B CG2 
2402 N N   . ALA B 100 ? 0.2192 0.2487 0.2717 0.0338  -0.0160 0.0341  88  ALA B N   
2403 C CA  . ALA B 100 ? 0.2266 0.2494 0.2832 0.0347  -0.0100 0.0362  88  ALA B CA  
2404 C C   . ALA B 100 ? 0.2247 0.2462 0.2867 0.0409  -0.0124 0.0423  88  ALA B C   
2405 O O   . ALA B 100 ? 0.2380 0.2504 0.2965 0.0417  -0.0085 0.0462  88  ALA B O   
2406 C CB  . ALA B 100 ? 0.2452 0.2684 0.3117 0.0314  -0.0043 0.0308  88  ALA B CB  
2407 N N   . SER B 101 ? 0.2268 0.2574 0.2980 0.0452  -0.0189 0.0435  89  SER B N   
2408 C CA  A SER B 101 ? 0.2222 0.2520 0.3001 0.0527  -0.0224 0.0508  89  SER B CA  
2409 C CA  B SER B 101 ? 0.2227 0.2521 0.3006 0.0526  -0.0222 0.0508  89  SER B CA  
2410 C C   . SER B 101 ? 0.2607 0.2838 0.3216 0.0544  -0.0253 0.0590  89  SER B C   
2411 O O   . SER B 101 ? 0.2588 0.2720 0.3193 0.0583  -0.0232 0.0661  89  SER B O   
2412 C CB  A SER B 101 ? 0.2733 0.3183 0.3641 0.0566  -0.0310 0.0504  89  SER B CB  
2413 C CB  B SER B 101 ? 0.2742 0.3183 0.3673 0.0571  -0.0299 0.0504  89  SER B CB  
2414 O OG  A SER B 101 ? 0.3141 0.3595 0.4136 0.0654  -0.0354 0.0584  89  SER B OG  
2415 O OG  B SER B 101 ? 0.2082 0.2576 0.3198 0.0561  -0.0247 0.0437  89  SER B OG  
2416 N N   . ALA B 102 ? 0.2629 0.2900 0.3091 0.0511  -0.0290 0.0578  90  ALA B N   
2417 C CA  . ALA B 102 ? 0.2980 0.3197 0.3261 0.0516  -0.0301 0.0648  90  ALA B CA  
2418 C C   . ALA B 102 ? 0.2714 0.2808 0.2943 0.0485  -0.0208 0.0666  90  ALA B C   
2419 O O   . ALA B 102 ? 0.2886 0.2895 0.3049 0.0503  -0.0193 0.0750  90  ALA B O   
2420 C CB  . ALA B 102 ? 0.2845 0.3126 0.2985 0.0479  -0.0335 0.0603  90  ALA B CB  
2421 N N   . VAL B 103 ? 0.2657 0.2742 0.2917 0.0433  -0.0147 0.0593  91  VAL B N   
2422 C CA  . VAL B 103 ? 0.2702 0.2700 0.2930 0.0392  -0.0067 0.0596  91  VAL B CA  
2423 C C   . VAL B 103 ? 0.2568 0.2465 0.2889 0.0410  -0.0027 0.0628  91  VAL B C   
2424 O O   . VAL B 103 ? 0.2868 0.2667 0.3138 0.0401  0.0011  0.0686  91  VAL B O   
2425 C CB  . VAL B 103 ? 0.2472 0.2503 0.2722 0.0340  -0.0031 0.0513  91  VAL B CB  
2426 C CG1 . VAL B 103 ? 0.2616 0.2586 0.2862 0.0293  0.0039  0.0507  91  VAL B CG1 
2427 C CG2 . VAL B 103 ? 0.2863 0.2960 0.3018 0.0327  -0.0055 0.0484  91  VAL B CG2 
2428 N N   . ALA B 104 ? 0.2541 0.2455 0.3006 0.0436  -0.0029 0.0591  92  ALA B N   
2429 C CA  . ALA B 104 ? 0.2433 0.2241 0.3004 0.0453  0.0028  0.0593  92  ALA B CA  
2430 C C   . ALA B 104 ? 0.2611 0.2330 0.3187 0.0520  0.0005  0.0697  92  ALA B C   
2431 O O   . ALA B 104 ? 0.2842 0.2418 0.3450 0.0520  0.0066  0.0721  92  ALA B O   
2432 C CB  . ALA B 104 ? 0.2550 0.2422 0.3280 0.0475  0.0033  0.0527  92  ALA B CB  
2433 N N   . ALA B 105 ? 0.2790 0.2585 0.3327 0.0575  -0.0084 0.0763  93  ALA B N   
2434 C CA  . ALA B 105 ? 0.3171 0.2894 0.3711 0.0652  -0.0124 0.0879  93  ALA B CA  
2435 C C   . ALA B 105 ? 0.3618 0.3190 0.4011 0.0622  -0.0077 0.0961  93  ALA B C   
2436 O O   . ALA B 105 ? 0.3986 0.3427 0.4395 0.0676  -0.0075 0.1059  93  ALA B O   
2437 C CB  . ALA B 105 ? 0.3435 0.3295 0.3937 0.0707  -0.0244 0.0929  93  ALA B CB  
2438 N N   . GLU B 106 ? 0.3269 0.2851 0.3534 0.0537  -0.0034 0.0927  94  GLU B N   
2439 C CA  . GLU B 106 ? 0.3511 0.2967 0.3654 0.0493  0.0025  0.0998  94  GLU B CA  
2440 C C   . GLU B 106 ? 0.3848 0.3162 0.4075 0.0441  0.0124  0.0960  94  GLU B C   
2441 O O   . GLU B 106 ? 0.4081 0.3288 0.4230 0.0384  0.0187  0.1006  94  GLU B O   
2442 C CB  . GLU B 106 ? 0.3687 0.3238 0.3682 0.0424  0.0039  0.0967  94  GLU B CB  
2443 C CG  . GLU B 106 ? 0.3762 0.3442 0.3643 0.0456  -0.0045 0.0982  94  GLU B CG  
2444 C CD  . GLU B 106 ? 0.4960 0.4591 0.4721 0.0509  -0.0099 0.1114  94  GLU B CD  
2445 O OE1 . GLU B 106 ? 0.5106 0.4599 0.4794 0.0494  -0.0047 0.1208  94  GLU B OE1 
2446 O OE2 . GLU B 106 ? 0.5126 0.4859 0.4858 0.0560  -0.0197 0.1126  94  GLU B OE2 
2447 N N   . HIS B 107 ? 0.3113 0.2855 0.3391 0.0559  0.0497  0.0975  95  HIS B N   
2448 C CA  . HIS B 107 ? 0.3298 0.2856 0.3681 0.0458  0.0620  0.0887  95  HIS B CA  
2449 C C   . HIS B 107 ? 0.3244 0.2625 0.3734 0.0509  0.0737  0.0914  95  HIS B C   
2450 O O   . HIS B 107 ? 0.3666 0.2781 0.4131 0.0402  0.0867  0.0816  95  HIS B O   
2451 C CB  . HIS B 107 ? 0.2969 0.2590 0.3340 0.0315  0.0534  0.0722  95  HIS B CB  
2452 C CG  . HIS B 107 ? 0.2817 0.2608 0.3188 0.0288  0.0475  0.0727  95  HIS B CG  
2453 N ND1 . HIS B 107 ? 0.3428 0.3205 0.3919 0.0196  0.0538  0.0762  95  HIS B ND1 
2454 C CD2 . HIS B 107 ? 0.3132 0.3079 0.3424 0.0343  0.0397  0.0717  95  HIS B CD2 
2455 C CE1 . HIS B 107 ? 0.3217 0.3149 0.3752 0.0225  0.0531  0.0793  95  HIS B CE1 
2456 N NE2 . HIS B 107 ? 0.3224 0.3222 0.3594 0.0312  0.0459  0.0751  95  HIS B NE2 
2457 N N   . GLY B 108 ? 0.3048 0.2545 0.3656 0.0654  0.0701  0.1055  96  GLY B N   
2458 C CA  . GLY B 108 ? 0.3367 0.2694 0.4181 0.0734  0.0876  0.1121  96  GLY B CA  
2459 C C   . GLY B 108 ? 0.3572 0.2788 0.4357 0.0657  0.0927  0.0943  96  GLY B C   
2460 O O   . GLY B 108 ? 0.3838 0.2739 0.4673 0.0672  0.1171  0.0924  96  GLY B O   
2461 N N   . LEU B 109 ? 0.2925 0.2344 0.3601 0.0581  0.0736  0.0821  97  LEU B N   
2462 C CA  . LEU B 109 ? 0.3030 0.2344 0.3625 0.0498  0.0768  0.0663  97  LEU B CA  
2463 C C   . LEU B 109 ? 0.3206 0.2748 0.4025 0.0607  0.0704  0.0739  97  LEU B C   
2464 O O   . LEU B 109 ? 0.2958 0.2818 0.3883 0.0664  0.0503  0.0842  97  LEU B O   
2465 C CB  . LEU B 109 ? 0.3012 0.2405 0.3389 0.0333  0.0603  0.0504  97  LEU B CB  
2466 C CG  . LEU B 109 ? 0.3103 0.2302 0.3332 0.0177  0.0638  0.0444  97  LEU B CG  
2467 C CD1 . LEU B 109 ? 0.3228 0.2668 0.3432 0.0071  0.0440  0.0399  97  LEU B CD1 
2468 C CD2 . LEU B 109 ? 0.4019 0.2786 0.4018 0.0026  0.0794  0.0318  97  LEU B CD2 
2469 N N   . ARG B 110 ? 0.3340 0.2681 0.4179 0.0602  0.0875  0.0673  98  ARG B N   
2470 C CA  . ARG B 110 ? 0.2934 0.2484 0.4033 0.0684  0.0840  0.0740  98  ARG B CA  
2471 C C   . ARG B 110 ? 0.3272 0.2939 0.4164 0.0566  0.0665  0.0574  98  ARG B C   
2472 O O   . ARG B 110 ? 0.3824 0.3246 0.4393 0.0430  0.0715  0.0405  98  ARG B O   
2473 C CB  . ARG B 110 ? 0.3602 0.2818 0.4823 0.0751  0.1188  0.0760  98  ARG B CB  
2474 C CG  . ARG B 110 ? 0.5494 0.4765 0.7181 0.0929  0.1361  0.1023  98  ARG B CG  
2475 C CD  . ARG B 110 ? 0.7176 0.6178 0.8932 0.0929  0.1719  0.1016  98  ARG B CD  
2476 N NE  . ARG B 110 ? 0.8311 0.7284 0.9995 0.0887  0.1735  0.0909  98  ARG B NE  
2477 C CZ  . ARG B 110 ? 0.9476 0.7990 1.0668 0.0775  0.1902  0.0672  98  ARG B CZ  
2478 N NH1 . ARG B 110 ? 0.9084 0.7115 0.9778 0.0652  0.2032  0.0500  98  ARG B NH1 
2479 N NH2 . ARG B 110 ? 0.9667 0.8190 1.0819 0.0747  0.1916  0.0608  98  ARG B NH2 
2480 N N   . VAL B 111 ? 0.2752 0.2767 0.3819 0.0600  0.0457  0.0638  99  VAL B N   
2481 C CA  . VAL B 111 ? 0.2519 0.2625 0.3450 0.0512  0.0332  0.0506  99  VAL B CA  
2482 C C   . VAL B 111 ? 0.2690 0.2613 0.3659 0.0512  0.0523  0.0457  99  VAL B C   
2483 O O   . VAL B 111 ? 0.2903 0.2847 0.4216 0.0623  0.0669  0.0592  99  VAL B O   
2484 C CB  . VAL B 111 ? 0.2636 0.3076 0.3706 0.0525  0.0091  0.0578  99  VAL B CB  
2485 C CG1 . VAL B 111 ? 0.2867 0.3362 0.3856 0.0453  0.0016  0.0457  99  VAL B CG1 
2486 C CG2 . VAL B 111 ? 0.2754 0.3269 0.3638 0.0507  -0.0057 0.0604  99  VAL B CG2 
2487 N N   . ARG B 112 ? 0.2486 0.2224 0.3121 0.0389  0.0536  0.0296  100 ARG B N   
2488 C CA  . ARG B 112 ? 0.2734 0.2258 0.3287 0.0368  0.0709  0.0238  100 ARG B CA  
2489 C C   . ARG B 112 ? 0.2443 0.2185 0.2996 0.0323  0.0534  0.0194  100 ARG B C   
2490 O O   . ARG B 112 ? 0.2423 0.2331 0.2866 0.0258  0.0322  0.0150  100 ARG B O   
2491 C CB  . ARG B 112 ? 0.3397 0.2432 0.3472 0.0234  0.0886  0.0106  100 ARG B CB  
2492 C CG  . ARG B 112 ? 0.4320 0.3040 0.4438 0.0303  0.1165  0.0157  100 ARG B CG  
2493 C CD  . ARG B 112 ? 0.5841 0.3920 0.5412 0.0153  0.1428  0.0009  100 ARG B CD  
2494 N NE  . ARG B 112 ? 0.7403 0.5181 0.6829 0.0165  0.1685  -0.0030 100 ARG B NE  
2495 C CZ  . ARG B 112 ? 0.8656 0.5790 0.7465 0.0008  0.1933  -0.0177 100 ARG B CZ  
2496 N NH1 . ARG B 112 ? 0.8560 0.5279 0.6840 -0.0202 0.1930  -0.0304 100 ARG B NH1 
2497 N NH2 . ARG B 112 ? 0.8579 0.5463 0.7268 0.0036  0.2186  -0.0189 100 ARG B NH2 
2498 N N   . THR B 113 ? 0.2340 0.2043 0.3025 0.0360  0.0665  0.0215  101 THR B N   
2499 C CA  . THR B 113 ? 0.2107 0.2018 0.2872 0.0335  0.0527  0.0198  101 THR B CA  
2500 C C   . THR B 113 ? 0.2571 0.2179 0.2950 0.0238  0.0639  0.0097  101 THR B C   
2501 O O   . THR B 113 ? 0.2910 0.2153 0.3103 0.0232  0.0908  0.0074  101 THR B O   
2502 C CB  . THR B 113 ? 0.2485 0.2610 0.3759 0.0436  0.0581  0.0336  101 THR B CB  
2503 O OG1 . THR B 113 ? 0.2570 0.3007 0.4153 0.0482  0.0392  0.0457  101 THR B OG1 
2504 C CG2 . THR B 113 ? 0.2646 0.2902 0.3967 0.0385  0.0486  0.0302  101 THR B CG2 
2505 N N   . ASP B 114 ? 0.2460 0.2193 0.2708 0.0162  0.0450  0.0052  102 ASP B N   
2506 C CA  . ASP B 114 ? 0.2656 0.2161 0.2573 0.0070  0.0510  0.0003  102 ASP B CA  
2507 C C   . ASP B 114 ? 0.2716 0.2480 0.2858 0.0096  0.0391  0.0033  102 ASP B C   
2508 O O   . ASP B 114 ? 0.2443 0.2421 0.2636 0.0077  0.0190  0.0035  102 ASP B O   
2509 C CB  . ASP B 114 ? 0.3042 0.2381 0.2509 -0.0090 0.0381  -0.0046 102 ASP B CB  
2510 C CG  . ASP B 114 ? 0.3390 0.2423 0.2404 -0.0222 0.0428  -0.0071 102 ASP B CG  
2511 O OD1 . ASP B 114 ? 0.3376 0.2384 0.2446 -0.0174 0.0534  -0.0051 102 ASP B OD1 
2512 O OD2 . ASP B 114 ? 0.4185 0.2950 0.2728 -0.0401 0.0363  -0.0104 102 ASP B OD2 
2513 N N   . ALA B 115 ? 0.2694 0.2397 0.2970 0.0136  0.0552  0.0061  103 ALA B N   
2514 C CA  . ALA B 115 ? 0.2503 0.2415 0.3010 0.0148  0.0462  0.0087  103 ALA B CA  
2515 C C   . ALA B 115 ? 0.2582 0.2431 0.2788 0.0067  0.0359  0.0071  103 ALA B C   
2516 O O   . ALA B 115 ? 0.2522 0.2535 0.2907 0.0078  0.0271  0.0090  103 ALA B O   
2517 C CB  . ALA B 115 ? 0.3266 0.3131 0.4041 0.0201  0.0679  0.0146  103 ALA B CB  
2518 N N   . ARG B 116 ? 0.2599 0.2214 0.2362 -0.0030 0.0349  0.0054  104 ARG B N   
2519 C CA  . ARG B 116 ? 0.2676 0.2307 0.2233 -0.0115 0.0191  0.0104  104 ARG B CA  
2520 C C   . ARG B 116 ? 0.2432 0.2361 0.2225 -0.0092 -0.0012 0.0142  104 ARG B C   
2521 O O   . ARG B 116 ? 0.2297 0.2313 0.2091 -0.0124 -0.0128 0.0234  104 ARG B O   
2522 C CB  . ARG B 116 ? 0.3152 0.2447 0.2140 -0.0278 0.0182  0.0105  104 ARG B CB  
2523 C CG  . ARG B 116 ? 0.3814 0.2684 0.2438 -0.0308 0.0456  0.0062  104 ARG B CG  
2524 C CD  . ARG B 116 ? 0.4594 0.3004 0.2501 -0.0512 0.0468  0.0023  104 ARG B CD  
2525 N NE  . ARG B 116 ? 0.4536 0.2833 0.2377 -0.0541 0.0501  -0.0061 104 ARG B NE  
2526 C CZ  . ARG B 116 ? 0.5267 0.3055 0.2478 -0.0717 0.0601  -0.0144 104 ARG B CZ  
2527 N NH1 . ARG B 116 ? 0.5994 0.3297 0.2502 -0.0896 0.0675  -0.0164 104 ARG B NH1 
2528 N NH2 . ARG B 116 ? 0.5264 0.2979 0.2496 -0.0730 0.0634  -0.0210 104 ARG B NH2 
2529 N N   . LEU B 117 ? 0.2274 0.2349 0.2285 -0.0027 -0.0033 0.0101  105 LEU B N   
2530 C CA  . LEU B 117 ? 0.1969 0.2259 0.2176 0.0011  -0.0151 0.0128  105 LEU B CA  
2531 C C   . LEU B 117 ? 0.2007 0.2407 0.2458 0.0084  -0.0131 0.0106  105 LEU B C   
2532 O O   . LEU B 117 ? 0.1944 0.2428 0.2490 0.0118  -0.0168 0.0103  105 LEU B O   
2533 C CB  . LEU B 117 ? 0.1977 0.2296 0.2192 0.0023  -0.0169 0.0096  105 LEU B CB  
2534 C CG  . LEU B 117 ? 0.2052 0.2234 0.2020 -0.0080 -0.0198 0.0106  105 LEU B CG  
2535 C CD1 . LEU B 117 ? 0.2186 0.2357 0.2195 -0.0045 -0.0160 0.0071  105 LEU B CD1 
2536 C CD2 . LEU B 117 ? 0.2271 0.2574 0.2262 -0.0154 -0.0349 0.0212  105 LEU B CD2 
2537 N N   . ARG B 118 ? 0.1919 0.2275 0.2448 0.0093  -0.0053 0.0085  106 ARG B N   
2538 C CA  . ARG B 118 ? 0.1829 0.2249 0.2558 0.0110  -0.0057 0.0054  106 ARG B CA  
2539 C C   . ARG B 118 ? 0.1651 0.2052 0.2387 0.0122  -0.0057 0.0082  106 ARG B C   
2540 O O   . ARG B 118 ? 0.1800 0.2190 0.2478 0.0125  -0.0062 0.0173  106 ARG B O   
2541 C CB  . ARG B 118 ? 0.2003 0.2390 0.2876 0.0099  0.0034  0.0061  106 ARG B CB  
2542 C CG  . ARG B 118 ? 0.2149 0.2402 0.2893 0.0089  0.0126  0.0114  106 ARG B CG  
2543 C CD  . ARG B 118 ? 0.2421 0.2608 0.3314 0.0089  0.0280  0.0134  106 ARG B CD  
2544 N NE  . ARG B 118 ? 0.3020 0.3024 0.3696 0.0073  0.0382  0.0190  106 ARG B NE  
2545 C CZ  . ARG B 118 ? 0.3561 0.3347 0.3874 0.0042  0.0466  0.0214  106 ARG B CZ  
2546 N NH1 . ARG B 118 ? 0.3559 0.3261 0.3691 0.0027  0.0480  0.0173  106 ARG B NH1 
2547 N NH2 . ARG B 118 ? 0.4040 0.3637 0.4108 0.0007  0.0542  0.0283  106 ARG B NH2 
2548 N N   . GLU B 119 ? 0.1922 0.2292 0.2722 0.0117  -0.0052 0.0020  107 GLU B N   
2549 C CA  . GLU B 119 ? 0.1913 0.2188 0.2740 0.0148  0.0028  0.0049  107 GLU B CA  
2550 C C   . GLU B 119 ? 0.1950 0.2183 0.2862 0.0151  0.0092  0.0119  107 GLU B C   
2551 O O   . GLU B 119 ? 0.1889 0.2124 0.2827 0.0115  0.0100  0.0106  107 GLU B O   
2552 C CB  . GLU B 119 ? 0.2327 0.2448 0.3080 0.0105  0.0061  -0.0065 107 GLU B CB  
2553 C CG  . GLU B 119 ? 0.2162 0.2062 0.2904 0.0146  0.0231  -0.0059 107 GLU B CG  
2554 C CD  . GLU B 119 ? 0.2382 0.2328 0.3221 0.0260  0.0321  0.0071  107 GLU B CD  
2555 O OE1 . GLU B 119 ? 0.2295 0.2442 0.3293 0.0301  0.0256  0.0222  107 GLU B OE1 
2556 O OE2 . GLU B 119 ? 0.2590 0.2346 0.3348 0.0298  0.0470  0.0043  107 GLU B OE2 
2557 N N   . VAL B 120 ? 0.1946 0.2136 0.2933 0.0206  0.0164  0.0223  108 VAL B N   
2558 C CA  A VAL B 120 ? 0.2093 0.2210 0.3167 0.0218  0.0244  0.0310  108 VAL B CA  
2559 C CA  B VAL B 120 ? 0.2067 0.2185 0.3139 0.0217  0.0243  0.0309  108 VAL B CA  
2560 C C   . VAL B 120 ? 0.2134 0.2119 0.3244 0.0156  0.0310  0.0183  108 VAL B C   
2561 O O   . VAL B 120 ? 0.2301 0.2189 0.3374 0.0105  0.0315  0.0050  108 VAL B O   
2562 C CB  A VAL B 120 ? 0.2116 0.2200 0.3361 0.0308  0.0342  0.0465  108 VAL B CB  
2563 C CB  B VAL B 120 ? 0.2096 0.2175 0.3339 0.0306  0.0344  0.0463  108 VAL B CB  
2564 C CG1 A VAL B 120 ? 0.2335 0.2210 0.3605 0.0338  0.0505  0.0355  108 VAL B CG1 
2565 C CG1 B VAL B 120 ? 0.2260 0.2296 0.3586 0.0324  0.0397  0.0611  108 VAL B CG1 
2566 C CG2 A VAL B 120 ? 0.2280 0.2317 0.3622 0.0332  0.0403  0.0617  108 VAL B CG2 
2567 C CG2 B VAL B 120 ? 0.1939 0.2201 0.3258 0.0347  0.0255  0.0613  108 VAL B CG2 
2568 N N   . ARG B 121 ? 0.2048 0.2011 0.3205 0.0137  0.0354  0.0232  109 ARG B N   
2569 C CA  A ARG B 121 ? 0.2298 0.2156 0.3580 0.0064  0.0422  0.0149  109 ARG B CA  
2570 C CA  B ARG B 121 ? 0.2288 0.2145 0.3570 0.0065  0.0422  0.0149  109 ARG B CA  
2571 C C   . ARG B 121 ? 0.2461 0.2101 0.3785 0.0069  0.0545  0.0128  109 ARG B C   
2572 O O   . ARG B 121 ? 0.2488 0.2070 0.3858 0.0165  0.0644  0.0264  109 ARG B O   
2573 C CB  A ARG B 121 ? 0.2410 0.2260 0.3755 0.0060  0.0500  0.0233  109 ARG B CB  
2574 C CB  B ARG B 121 ? 0.2411 0.2259 0.3756 0.0061  0.0502  0.0234  109 ARG B CB  
2575 C CG  A ARG B 121 ? 0.2770 0.2586 0.4345 -0.0034 0.0551  0.0168  109 ARG B CG  
2576 C CG  B ARG B 121 ? 0.2676 0.2438 0.4241 -0.0021 0.0584  0.0185  109 ARG B CG  
2577 C CD  A ARG B 121 ? 0.3047 0.2839 0.4708 -0.0021 0.0685  0.0266  109 ARG B CD  
2578 C CD  B ARG B 121 ? 0.3051 0.2821 0.4704 -0.0018 0.0694  0.0272  109 ARG B CD  
2579 N NE  A ARG B 121 ? 0.3900 0.3521 0.5537 0.0014  0.0822  0.0367  109 ARG B NE  
2580 N NE  B ARG B 121 ? 0.3396 0.3061 0.4827 0.0058  0.0776  0.0412  109 ARG B NE  
2581 C CZ  A ARG B 121 ? 0.3814 0.3370 0.5216 0.0084  0.0863  0.0508  109 ARG B CZ  
2582 C CZ  B ARG B 121 ? 0.3495 0.3016 0.4960 0.0079  0.0900  0.0513  109 ARG B CZ  
2583 N NH1 A ARG B 121 ? 0.4216 0.3825 0.5341 0.0101  0.0775  0.0539  109 ARG B NH1 
2584 N NH1 B ARG B 121 ? 0.2798 0.2227 0.4517 0.0030  0.0991  0.0469  109 ARG B NH1 
2585 N NH2 A ARG B 121 ? 0.3838 0.3249 0.5260 0.0114  0.0982  0.0632  109 ARG B NH2 
2586 N NH2 B ARG B 121 ? 0.3628 0.3076 0.4846 0.0130  0.0918  0.0677  109 ARG B NH2 
2587 N N   . THR B 122 ? 0.2443 0.1936 0.3737 -0.0047 0.0539  -0.0028 110 THR B N   
2588 C CA  . THR B 122 ? 0.2704 0.1860 0.3923 -0.0076 0.0697  -0.0098 110 THR B CA  
2589 C C   . THR B 122 ? 0.2914 0.1885 0.4244 -0.0195 0.0774  -0.0145 110 THR B C   
2590 O O   . THR B 122 ? 0.2807 0.1938 0.4307 -0.0283 0.0679  -0.0138 110 THR B O   
2591 C CB  . THR B 122 ? 0.2986 0.1965 0.3922 -0.0182 0.0643  -0.0273 110 THR B CB  
2592 O OG1 . THR B 122 ? 0.3170 0.2249 0.4097 -0.0371 0.0432  -0.0369 110 THR B OG1 
2593 C CG2 . THR B 122 ? 0.2838 0.1971 0.3679 -0.0071 0.0594  -0.0230 110 THR B CG2 
2594 N N   . ASN B 123 ? 0.3087 0.1684 0.4347 -0.0200 0.0983  -0.0184 111 ASN B N   
2595 C CA  . ASN B 123 ? 0.3464 0.1784 0.4758 -0.0367 0.1061  -0.0277 111 ASN B CA  
2596 C C   . ASN B 123 ? 0.3679 0.2047 0.4893 -0.0626 0.0819  -0.0434 111 ASN B C   
2597 O O   . ASN B 123 ? 0.3594 0.2058 0.5058 -0.0755 0.0750  -0.0416 111 ASN B O   
2598 C CB  . ASN B 123 ? 0.3929 0.1723 0.5041 -0.0366 0.1344  -0.0351 111 ASN B CB  
2599 C CG  . ASN B 123 ? 0.4300 0.2045 0.5666 -0.0143 0.1599  -0.0133 111 ASN B CG  
2600 O OD1 . ASN B 123 ? 0.4172 0.2242 0.5784 -0.0029 0.1537  0.0060  111 ASN B OD1 
2601 N ND2 . ASN B 123 ? 0.5662 0.3070 0.6916 -0.0100 0.1859  -0.0153 111 ASN B ND2 
2602 N N   . TRP B 124 ? 0.3869 0.2168 0.4758 -0.0714 0.0687  -0.0560 112 TRP B N   
2603 C CA  . TRP B 124 ? 0.4174 0.2546 0.4979 -0.0980 0.0399  -0.0660 112 TRP B CA  
2604 C C   . TRP B 124 ? 0.3656 0.2570 0.4912 -0.0954 0.0198  -0.0512 112 TRP B C   
2605 O O   . TRP B 124 ? 0.3878 0.2915 0.5384 -0.1155 0.0034  -0.0496 112 TRP B O   
2606 C CB  . TRP B 124 ? 0.4319 0.2532 0.4645 -0.1052 0.0293  -0.0781 112 TRP B CB  
2607 C CG  . TRP B 124 ? 0.4628 0.2798 0.4756 -0.1387 -0.0020 -0.0878 112 TRP B CG  
2608 C CD1 . TRP B 124 ? 0.5511 0.3639 0.5793 -0.1654 -0.0161 -0.0901 112 TRP B CD1 
2609 C CD2 . TRP B 124 ? 0.4802 0.3017 0.4589 -0.1502 -0.0266 -0.0919 112 TRP B CD2 
2610 N NE1 . TRP B 124 ? 0.6326 0.4470 0.6377 -0.1956 -0.0512 -0.0946 112 TRP B NE1 
2611 C CE2 . TRP B 124 ? 0.5088 0.3285 0.4815 -0.1862 -0.0584 -0.0953 112 TRP B CE2 
2612 C CE3 . TRP B 124 ? 0.5089 0.3359 0.4627 -0.1350 -0.0258 -0.0910 112 TRP B CE3 
2613 C CZ2 . TRP B 124 ? 0.6622 0.4915 0.6060 -0.2003 -0.0885 -0.0944 112 TRP B CZ2 
2614 C CZ3 . TRP B 124 ? 0.5640 0.3909 0.4825 -0.1542 -0.0541 -0.0941 112 TRP B CZ3 
2615 C CH2 . TRP B 124 ? 0.5578 0.3846 0.4690 -0.1878 -0.0865 -0.0954 112 TRP B CH2 
2616 N N   . ASP B 125 ? 0.3325 0.2533 0.4717 -0.0719 0.0235  -0.0387 113 ASP B N   
2617 C CA  . ASP B 125 ? 0.3407 0.3017 0.5186 -0.0672 0.0146  -0.0250 113 ASP B CA  
2618 C C   . ASP B 125 ? 0.3143 0.2772 0.5285 -0.0700 0.0268  -0.0164 113 ASP B C   
2619 O O   . ASP B 125 ? 0.3553 0.3444 0.6084 -0.0757 0.0194  -0.0068 113 ASP B O   
2620 C CB  . ASP B 125 ? 0.2628 0.2406 0.4375 -0.0442 0.0224  -0.0153 113 ASP B CB  
2621 C CG  . ASP B 125 ? 0.3135 0.2983 0.4636 -0.0398 0.0104  -0.0196 113 ASP B CG  
2622 O OD1 . ASP B 125 ? 0.3243 0.3129 0.4673 -0.0531 -0.0080 -0.0258 113 ASP B OD1 
2623 O OD2 . ASP B 125 ? 0.2584 0.2445 0.3957 -0.0245 0.0181  -0.0150 113 ASP B OD2 
2624 N N   . ASP B 126 ? 0.3113 0.2469 0.5184 -0.0650 0.0479  -0.0168 114 ASP B N   
2625 C CA  . ASP B 126 ? 0.3493 0.2800 0.5868 -0.0680 0.0628  -0.0087 114 ASP B CA  
2626 C C   . ASP B 126 ? 0.3543 0.2663 0.6024 -0.0951 0.0563  -0.0186 114 ASP B C   
2627 O O   . ASP B 126 ? 0.4177 0.3221 0.6932 -0.1002 0.0697  -0.0126 114 ASP B O   
2628 C CB  . ASP B 126 ? 0.3905 0.2989 0.6161 -0.0507 0.0880  -0.0009 114 ASP B CB  
2629 C CG  . ASP B 126 ? 0.4306 0.3564 0.6458 -0.0292 0.0919  0.0131  114 ASP B CG  
2630 O OD1 . ASP B 126 ? 0.4368 0.3865 0.6569 -0.0268 0.0832  0.0165  114 ASP B OD1 
2631 O OD2 . ASP B 126 ? 0.5810 0.4939 0.7831 -0.0162 0.1040  0.0226  114 ASP B OD2 
2632 N N   . GLY B 127 ? 0.3926 0.2930 0.6148 -0.1147 0.0360  -0.0334 115 GLY B N   
2633 C CA  . GLY B 127 ? 0.4531 0.3314 0.6748 -0.1475 0.0237  -0.0441 115 GLY B CA  
2634 C C   . GLY B 127 ? 0.4785 0.2986 0.6610 -0.1539 0.0451  -0.0591 115 GLY B C   
2635 O O   . GLY B 127 ? 0.5500 0.3504 0.7265 -0.1756 0.0390  -0.0635 115 GLY B O   
2636 N N   . ARG B 128 ? 0.2597 0.4299 0.7164 -0.0377 -0.0320 -0.1619 116 ARG B N   
2637 C CA  . ARG B 128 ? 0.2340 0.3687 0.6782 -0.0603 -0.0239 -0.1488 116 ARG B CA  
2638 C C   . ARG B 128 ? 0.3013 0.3891 0.6799 -0.0386 -0.0546 -0.1450 116 ARG B C   
2639 O O   . ARG B 128 ? 0.2935 0.3630 0.6171 -0.0113 -0.0697 -0.1402 116 ARG B O   
2640 C CB  . ARG B 128 ? 0.2451 0.3503 0.6486 -0.0786 0.0165  -0.1138 116 ARG B CB  
2641 C CG  . ARG B 128 ? 0.2950 0.4289 0.7377 -0.0984 0.0564  -0.1094 116 ARG B CG  
2642 C CD  . ARG B 128 ? 0.5410 0.6266 0.9211 -0.1086 0.0883  -0.0748 116 ARG B CD  
2643 N NE  . ARG B 128 ? 0.6730 0.7687 1.0437 -0.1075 0.1191  -0.0635 116 ARG B NE  
2644 C CZ  . ARG B 128 ? 0.6445 0.7255 1.0035 -0.1217 0.1507  -0.0519 116 ARG B CZ  
2645 N NH1 . ARG B 128 ? 0.5946 0.6490 0.9492 -0.1401 0.1579  -0.0478 116 ARG B NH1 
2646 N NH2 . ARG B 128 ? 0.7103 0.7999 1.0580 -0.1159 0.1753  -0.0445 116 ARG B NH2 
2647 N N   . PRO B 129 ? 0.2979 0.3583 0.6734 -0.0511 -0.0600 -0.1445 117 PRO B N   
2648 C CA  . PRO B 129 ? 0.3228 0.3364 0.6307 -0.0303 -0.0821 -0.1385 117 PRO B CA  
2649 C C   . PRO B 129 ? 0.3007 0.2843 0.5386 -0.0240 -0.0621 -0.1067 117 PRO B C   
2650 O O   . PRO B 129 ? 0.2719 0.2572 0.5073 -0.0401 -0.0325 -0.0866 117 PRO B O   
2651 C CB  . PRO B 129 ? 0.3225 0.3147 0.6469 -0.0492 -0.0850 -0.1428 117 PRO B CB  
2652 C CG  . PRO B 129 ? 0.4094 0.4425 0.8129 -0.0726 -0.0754 -0.1590 117 PRO B CG  
2653 C CD  . PRO B 129 ? 0.3002 0.3668 0.7259 -0.0820 -0.0447 -0.1491 117 PRO B CD  
2654 N N   . SER B 130 ? 0.3200 0.2737 0.4999 0.0004  -0.0788 -0.1043 118 SER B N   
2655 C CA  . SER B 130 ? 0.3316 0.2606 0.4535 0.0051  -0.0613 -0.0789 118 SER B CA  
2656 C C   . SER B 130 ? 0.3575 0.2610 0.4587 -0.0011 -0.0550 -0.0690 118 SER B C   
2657 O O   . SER B 130 ? 0.3673 0.2590 0.4792 -0.0013 -0.0706 -0.0821 118 SER B O   
2658 C CB  . SER B 130 ? 0.3529 0.2584 0.4213 0.0321  -0.0763 -0.0814 118 SER B CB  
2659 O OG  . SER B 130 ? 0.3478 0.2707 0.4271 0.0416  -0.0842 -0.0907 118 SER B OG  
2660 N N   . GLU B 131 ? 0.3328 0.2281 0.4065 -0.0048 -0.0343 -0.0482 119 GLU B N   
2661 C CA  . GLU B 131 ? 0.3457 0.2201 0.3978 -0.0056 -0.0285 -0.0399 119 GLU B CA  
2662 C C   . GLU B 131 ? 0.3278 0.1956 0.3404 0.0056  -0.0179 -0.0274 119 GLU B C   
2663 O O   . GLU B 131 ? 0.3239 0.2040 0.3352 0.0018  -0.0056 -0.0177 119 GLU B O   
2664 C CB  . GLU B 131 ? 0.3849 0.2592 0.4557 -0.0249 -0.0120 -0.0304 119 GLU B CB  
2665 C CG  . GLU B 131 ? 0.4403 0.2875 0.4856 -0.0218 -0.0110 -0.0251 119 GLU B CG  
2666 C CD  . GLU B 131 ? 0.4649 0.2958 0.5140 -0.0376 0.0034  -0.0162 119 GLU B CD  
2667 O OE1 . GLU B 131 ? 0.4047 0.2487 0.4710 -0.0497 0.0185  -0.0102 119 GLU B OE1 
2668 O OE2 . GLU B 131 ? 0.5708 0.3702 0.5972 -0.0347 0.0000  -0.0151 119 GLU B OE2 
2669 N N   . LEU B 132 ? 0.3470 0.1962 0.3304 0.0189  -0.0215 -0.0292 120 LEU B N   
2670 C CA  . LEU B 132 ? 0.3725 0.2233 0.3315 0.0257  -0.0056 -0.0195 120 LEU B CA  
2671 C C   . LEU B 132 ? 0.3442 0.2036 0.3170 0.0186  0.0029  -0.0130 120 LEU B C   
2672 O O   . LEU B 132 ? 0.3730 0.2171 0.3415 0.0225  -0.0043 -0.0171 120 LEU B O   
2673 C CB  . LEU B 132 ? 0.4101 0.2391 0.3329 0.0453  -0.0097 -0.0258 120 LEU B CB  
2674 C CG  . LEU B 132 ? 0.4254 0.2619 0.3297 0.0520  0.0121  -0.0190 120 LEU B CG  
2675 C CD1 . LEU B 132 ? 0.4492 0.2907 0.3447 0.0456  0.0289  -0.0108 120 LEU B CD1 
2676 C CD2 . LEU B 132 ? 0.4892 0.3017 0.3541 0.0739  0.0108  -0.0259 120 LEU B CD2 
2677 N N   . LYS B 133 ? 0.3185 0.1947 0.3025 0.0107  0.0139  -0.0047 121 LYS B N   
2678 C CA  . LYS B 133 ? 0.3245 0.2037 0.3141 0.0094  0.0176  -0.0007 121 LYS B CA  
2679 C C   . LYS B 133 ? 0.3163 0.2075 0.3009 0.0221  0.0218  -0.0042 121 LYS B C   
2680 O O   . LYS B 133 ? 0.3373 0.2420 0.3200 0.0245  0.0314  -0.0052 121 LYS B O   
2681 C CB  . LYS B 133 ? 0.2881 0.1796 0.2890 0.0002  0.0241  0.0065  121 LYS B CB  
2682 C CG  . LYS B 133 ? 0.3155 0.2004 0.3260 -0.0110 0.0246  0.0093  121 LYS B CG  
2683 C CD  . LYS B 133 ? 0.3321 0.1931 0.3399 -0.0156 0.0241  0.0094  121 LYS B CD  
2684 C CE  . LYS B 133 ? 0.3467 0.2031 0.3643 -0.0289 0.0352  0.0149  121 LYS B CE  
2685 N NZ  . LYS B 133 ? 0.3757 0.1996 0.3869 -0.0381 0.0404  0.0160  121 LYS B NZ  
2686 N N   . PRO B 134 ? 0.3194 0.2040 0.3003 0.0311  0.0160  -0.0073 122 PRO B N   
2687 C CA  . PRO B 134 ? 0.3327 0.2403 0.3208 0.0455  0.0183  -0.0152 122 PRO B CA  
2688 C C   . PRO B 134 ? 0.2852 0.2254 0.2996 0.0365  0.0278  -0.0142 122 PRO B C   
2689 O O   . PRO B 134 ? 0.2990 0.2350 0.3169 0.0252  0.0266  -0.0073 122 PRO B O   
2690 C CB  . PRO B 134 ? 0.3797 0.2649 0.3531 0.0586  0.0042  -0.0191 122 PRO B CB  
2691 C CG  . PRO B 134 ? 0.3843 0.2252 0.3351 0.0494  -0.0010 -0.0123 122 PRO B CG  
2692 C CD  . PRO B 134 ? 0.3463 0.1988 0.3144 0.0291  0.0081  -0.0046 122 PRO B CD  
2693 N N   . HIS B 135 ? 0.3116 0.2845 0.3463 0.0417  0.0380  -0.0229 123 HIS B N   
2694 C CA  . HIS B 135 ? 0.2703 0.2757 0.3386 0.0305  0.0461  -0.0258 123 HIS B CA  
2695 C C   . HIS B 135 ? 0.2804 0.2843 0.3566 0.0357  0.0272  -0.0297 123 HIS B C   
2696 O O   . HIS B 135 ? 0.3165 0.3096 0.3816 0.0549  0.0114  -0.0372 123 HIS B O   
2697 C CB  . HIS B 135 ? 0.3141 0.3610 0.4139 0.0348  0.0620  -0.0388 123 HIS B CB  
2698 C CG  . HIS B 135 ? 0.2539 0.3380 0.4003 0.0209  0.0680  -0.0465 123 HIS B CG  
2699 N ND1 . HIS B 135 ? 0.2800 0.4016 0.4683 0.0325  0.0547  -0.0661 123 HIS B ND1 
2700 C CD2 . HIS B 135 ? 0.2423 0.3255 0.3977 -0.0026 0.0799  -0.0390 123 HIS B CD2 
2701 C CE1 . HIS B 135 ? 0.2893 0.4381 0.5192 0.0143  0.0596  -0.0721 123 HIS B CE1 
2702 N NE2 . HIS B 135 ? 0.2405 0.3629 0.4480 -0.0082 0.0756  -0.0543 123 HIS B NE2 
2703 N N   . GLY B 136 ? 0.2668 0.2729 0.3527 0.0219  0.0272  -0.0250 124 GLY B N   
2704 C CA  . GLY B 136 ? 0.2726 0.2698 0.3563 0.0299  0.0087  -0.0288 124 GLY B CA  
2705 C C   . GLY B 136 ? 0.2824 0.2356 0.3261 0.0297  0.0041  -0.0149 124 GLY B C   
2706 O O   . GLY B 136 ? 0.3653 0.3024 0.3962 0.0359  -0.0070 -0.0150 124 GLY B O   
2707 N N   . VAL B 137 ? 0.2672 0.2012 0.2926 0.0227  0.0132  -0.0047 125 VAL B N   
2708 C CA  . VAL B 137 ? 0.2897 0.1895 0.2889 0.0185  0.0144  0.0062  125 VAL B CA  
2709 C C   . VAL B 137 ? 0.2763 0.1836 0.2833 0.0032  0.0234  0.0135  125 VAL B C   
2710 O O   . VAL B 137 ? 0.2713 0.1877 0.2852 -0.0035 0.0291  0.0137  125 VAL B O   
2711 C CB  . VAL B 137 ? 0.2920 0.1668 0.2742 0.0199  0.0152  0.0081  125 VAL B CB  
2712 C CG1 . VAL B 137 ? 0.3296 0.1750 0.2964 0.0092  0.0227  0.0180  125 VAL B CG1 
2713 C CG2 . VAL B 137 ? 0.3541 0.2121 0.3182 0.0395  0.0034  0.0003  125 VAL B CG2 
2714 N N   . TYR B 138 ? 0.2936 0.1917 0.2920 0.0020  0.0229  0.0181  126 TYR B N   
2715 C CA  . TYR B 138 ? 0.2653 0.1694 0.2680 -0.0078 0.0285  0.0226  126 TYR B CA  
2716 C C   . TYR B 138 ? 0.2806 0.1803 0.2848 -0.0140 0.0354  0.0254  126 TYR B C   
2717 O O   . TYR B 138 ? 0.3107 0.1947 0.3088 -0.0151 0.0403  0.0281  126 TYR B O   
2718 C CB  . TYR B 138 ? 0.3274 0.2184 0.3150 -0.0027 0.0254  0.0255  126 TYR B CB  
2719 C CG  . TYR B 138 ? 0.2682 0.1625 0.2552 -0.0076 0.0275  0.0281  126 TYR B CG  
2720 C CD1 . TYR B 138 ? 0.2727 0.1761 0.2677 -0.0130 0.0230  0.0250  126 TYR B CD1 
2721 C CD2 . TYR B 138 ? 0.2968 0.1824 0.2737 -0.0063 0.0355  0.0328  126 TYR B CD2 
2722 C CE1 . TYR B 138 ? 0.2969 0.1926 0.2809 -0.0144 0.0220  0.0269  126 TYR B CE1 
2723 C CE2 . TYR B 138 ? 0.3036 0.1917 0.2768 -0.0053 0.0347  0.0327  126 TYR B CE2 
2724 C CZ  . TYR B 138 ? 0.2808 0.1703 0.2535 -0.0079 0.0258  0.0300  126 TYR B CZ  
2725 O OH  . TYR B 138 ? 0.2857 0.1681 0.2457 -0.0044 0.0223  0.0294  126 TYR B OH  
2726 N N   . PRO B 139 ? 0.2534 0.1632 0.2649 -0.0178 0.0352  0.0230  127 PRO B N   
2727 C CA  . PRO B 139 ? 0.2631 0.1735 0.2838 -0.0204 0.0347  0.0190  127 PRO B CA  
2728 C C   . PRO B 139 ? 0.2801 0.1983 0.3112 -0.0222 0.0365  0.0170  127 PRO B C   
2729 O O   . PRO B 139 ? 0.2696 0.1956 0.3195 -0.0242 0.0335  0.0089  127 PRO B O   
2730 C CB  . PRO B 139 ? 0.2794 0.1898 0.2927 -0.0162 0.0295  0.0142  127 PRO B CB  
2731 C CG  . PRO B 139 ? 0.3341 0.2449 0.3358 -0.0170 0.0335  0.0183  127 PRO B CG  
2732 C CD  . PRO B 139 ? 0.2578 0.1737 0.2666 -0.0187 0.0349  0.0215  127 PRO B CD  
2733 N N   . PHE B 140 ? 0.2705 0.1882 0.2929 -0.0199 0.0399  0.0216  128 PHE B N   
2734 C CA  . PHE B 140 ? 0.2560 0.1845 0.2866 -0.0165 0.0403  0.0171  128 PHE B CA  
2735 C C   . PHE B 140 ? 0.2555 0.1840 0.2887 -0.0179 0.0551  0.0214  128 PHE B C   
2736 O O   . PHE B 140 ? 0.3092 0.2188 0.3200 -0.0160 0.0602  0.0298  128 PHE B O   
2737 C CB  . PHE B 140 ? 0.2449 0.1651 0.2530 -0.0090 0.0316  0.0176  128 PHE B CB  
2738 C CG  . PHE B 140 ? 0.2583 0.1668 0.2512 -0.0097 0.0252  0.0175  128 PHE B CG  
2739 C CD1 . PHE B 140 ? 0.2655 0.1713 0.2559 -0.0047 0.0181  0.0101  128 PHE B CD1 
2740 C CD2 . PHE B 140 ? 0.2613 0.1598 0.2419 -0.0149 0.0274  0.0232  128 PHE B CD2 
2741 C CE1 . PHE B 140 ? 0.3197 0.2058 0.2843 -0.0038 0.0180  0.0119  128 PHE B CE1 
2742 C CE2 . PHE B 140 ? 0.2980 0.1861 0.2661 -0.0187 0.0299  0.0237  128 PHE B CE2 
2743 C CZ  . PHE B 140 ? 0.3143 0.1924 0.2686 -0.0126 0.0276  0.0198  128 PHE B CZ  
2744 N N   . PRO B 141 ? 0.2502 0.1988 0.3088 -0.0187 0.0627  0.0140  129 PRO B N   
2745 C CA  . PRO B 141 ? 0.2814 0.2280 0.3383 -0.0200 0.0843  0.0191  129 PRO B CA  
2746 C C   . PRO B 141 ? 0.2790 0.2131 0.3021 -0.0050 0.0825  0.0240  129 PRO B C   
2747 O O   . PRO B 141 ? 0.3211 0.2358 0.3199 -0.0013 0.0982  0.0322  129 PRO B O   
2748 C CB  . PRO B 141 ? 0.2591 0.2422 0.3663 -0.0260 0.0934  0.0050  129 PRO B CB  
2749 C CG  . PRO B 141 ? 0.3180 0.3186 0.4394 -0.0167 0.0662  -0.0095 129 PRO B CG  
2750 C CD  . PRO B 141 ? 0.2631 0.2373 0.3560 -0.0181 0.0529  -0.0018 129 PRO B CD  
2751 N N   . GLU B 142 ? 0.2692 0.2052 0.2822 0.0051  0.0633  0.0192  130 GLU B N   
2752 C CA  . GLU B 142 ? 0.2675 0.1854 0.2462 0.0190  0.0588  0.0226  130 GLU B CA  
2753 C C   . GLU B 142 ? 0.2768 0.1657 0.2265 0.0181  0.0516  0.0312  130 GLU B C   
2754 O O   . GLU B 142 ? 0.3112 0.1986 0.2657 0.0106  0.0403  0.0309  130 GLU B O   
2755 C CB  . GLU B 142 ? 0.3113 0.2288 0.2810 0.0290  0.0396  0.0147  130 GLU B CB  
2756 C CG  . GLU B 142 ? 0.3243 0.2186 0.2570 0.0440  0.0322  0.0161  130 GLU B CG  
2757 C CD  . GLU B 142 ? 0.3132 0.1942 0.2262 0.0546  0.0129  0.0088  130 GLU B CD  
2758 O OE1 . GLU B 142 ? 0.3162 0.2023 0.2380 0.0530  0.0050  0.0029  130 GLU B OE1 
2759 O OE2 . GLU B 142 ? 0.3612 0.2197 0.2422 0.0677  0.0053  0.0087  130 GLU B OE2 
2760 N N   . PRO B 143 ? 0.3145 0.1805 0.2340 0.0282  0.0567  0.0364  131 PRO B N   
2761 C CA  . PRO B 143 ? 0.3804 0.2203 0.2760 0.0318  0.0442  0.0393  131 PRO B CA  
2762 C C   . PRO B 143 ? 0.3534 0.1923 0.2516 0.0293  0.0215  0.0339  131 PRO B C   
2763 O O   . PRO B 143 ? 0.3473 0.1820 0.2370 0.0330  0.0132  0.0308  131 PRO B O   
2764 C CB  . PRO B 143 ? 0.4589 0.2677 0.3109 0.0503  0.0502  0.0431  131 PRO B CB  
2765 C CG  . PRO B 143 ? 0.4042 0.2253 0.2642 0.0487  0.0805  0.0465  131 PRO B CG  
2766 C CD  . PRO B 143 ? 0.3675 0.2296 0.2725 0.0391  0.0765  0.0383  131 PRO B CD  
2767 N N   . GLU B 144 ? 0.3800 0.1624 0.2734 0.0439  -0.0116 0.0187  132 GLU B N   
2768 C CA  . GLU B 144 ? 0.3613 0.1709 0.2650 0.0553  -0.0129 0.0099  132 GLU B CA  
2769 C C   . GLU B 144 ? 0.3676 0.2072 0.2743 0.0542  -0.0133 0.0142  132 GLU B C   
2770 O O   . GLU B 144 ? 0.3230 0.1884 0.2405 0.0516  -0.0125 0.0072  132 GLU B O   
2771 C CB  . GLU B 144 ? 0.4101 0.2060 0.3106 0.0758  -0.0152 0.0114  132 GLU B CB  
2772 C CG  . GLU B 144 ? 0.4205 0.2492 0.3347 0.0894  -0.0164 0.0065  132 GLU B CG  
2773 C CD  . GLU B 144 ? 0.4672 0.2866 0.3839 0.1136  -0.0153 0.0137  132 GLU B CD  
2774 O OE1 . GLU B 144 ? 0.5386 0.3218 0.4454 0.1199  -0.0132 0.0200  132 GLU B OE1 
2775 O OE2 . GLU B 144 ? 0.6824 0.5326 0.6133 0.1266  -0.0159 0.0152  132 GLU B OE2 
2776 N N   . LYS B 145 ? 0.3643 0.1982 0.2578 0.0548  -0.0153 0.0257  133 LYS B N   
2777 C CA  . LYS B 145 ? 0.3688 0.2233 0.2547 0.0506  -0.0165 0.0279  133 LYS B CA  
2778 C C   . LYS B 145 ? 0.4101 0.2675 0.2934 0.0381  -0.0052 0.0240  133 LYS B C   
2779 O O   . LYS B 145 ? 0.3759 0.2456 0.2526 0.0346  -0.0035 0.0206  133 LYS B O   
2780 C CB  . LYS B 145 ? 0.3957 0.2449 0.2634 0.0517  -0.0239 0.0422  133 LYS B CB  
2781 C CG  . LYS B 145 ? 0.4180 0.2760 0.2973 0.0676  -0.0346 0.0514  133 LYS B CG  
2782 C CD  . LYS B 145 ? 0.4716 0.3367 0.3378 0.0655  -0.0458 0.0708  133 LYS B CD  
2783 C CE  . LYS B 145 ? 0.4601 0.3425 0.3479 0.0840  -0.0545 0.0854  133 LYS B CE  
2784 N NZ  . LYS B 145 ? 0.5318 0.4281 0.4110 0.0786  -0.0687 0.1105  133 LYS B NZ  
2785 N N   . GLU B 146 ? 0.3373 0.1832 0.2261 0.0311  0.0031  0.0263  134 GLU B N   
2786 C CA  . GLU B 146 ? 0.3444 0.2006 0.2412 0.0228  0.0165  0.0262  134 GLU B CA  
2787 C C   . GLU B 146 ? 0.3076 0.1869 0.2284 0.0226  0.0158  0.0173  134 GLU B C   
2788 O O   . GLU B 146 ? 0.3111 0.2037 0.2376 0.0209  0.0244  0.0156  134 GLU B O   
2789 C CB  . GLU B 146 ? 0.3730 0.2198 0.2764 0.0140  0.0242  0.0370  134 GLU B CB  
2790 C CG  . GLU B 146 ? 0.4165 0.2444 0.2967 0.0121  0.0281  0.0483  134 GLU B CG  
2791 C CD  . GLU B 146 ? 0.4689 0.2919 0.3579 0.0020  0.0354  0.0628  134 GLU B CD  
2792 O OE1 . GLU B 146 ? 0.4424 0.2808 0.3567 -0.0050 0.0391  0.0661  134 GLU B OE1 
2793 O OE2 . GLU B 146 ? 0.4973 0.3041 0.3691 -0.0007 0.0356  0.0735  134 GLU B OE2 
2794 N N   . VAL B 147 ? 0.3100 0.1915 0.2428 0.0239  0.0069  0.0118  135 VAL B N   
2795 C CA  . VAL B 147 ? 0.2832 0.1891 0.2355 0.0229  0.0043  0.0035  135 VAL B CA  
2796 C C   . VAL B 147 ? 0.2541 0.1764 0.2032 0.0306  0.0004  -0.0016 135 VAL B C   
2797 O O   . VAL B 147 ? 0.2560 0.1979 0.2175 0.0272  0.0034  -0.0041 135 VAL B O   
2798 C CB  . VAL B 147 ? 0.2617 0.1606 0.2163 0.0234  -0.0035 -0.0035 135 VAL B CB  
2799 C CG1 . VAL B 147 ? 0.2721 0.1996 0.2447 0.0208  -0.0065 -0.0114 135 VAL B CG1 
2800 C CG2 . VAL B 147 ? 0.3084 0.1860 0.2605 0.0099  -0.0027 0.0027  135 VAL B CG2 
2801 N N   . ALA B 148 ? 0.2860 0.2019 0.2202 0.0396  -0.0075 -0.0005 136 ALA B N   
2802 C CA  . ALA B 148 ? 0.2870 0.2214 0.2179 0.0432  -0.0152 -0.0011 136 ALA B CA  
2803 C C   . ALA B 148 ? 0.2958 0.2260 0.2116 0.0343  -0.0091 -0.0003 136 ALA B C   
2804 O O   . ALA B 148 ? 0.3014 0.2469 0.2214 0.0313  -0.0115 -0.0042 136 ALA B O   
2805 C CB  . ALA B 148 ? 0.3178 0.2490 0.2383 0.0527  -0.0251 0.0071  136 ALA B CB  
2806 N N   . GLU B 149 ? 0.3028 0.2093 0.1987 0.0300  0.0003  0.0045  137 GLU B N   
2807 C CA  . GLU B 149 ? 0.3315 0.2244 0.2037 0.0231  0.0109  0.0038  137 GLU B CA  
2808 C C   . GLU B 149 ? 0.3371 0.2391 0.2303 0.0220  0.0246  -0.0003 137 GLU B C   
2809 O O   . GLU B 149 ? 0.3373 0.2365 0.2204 0.0192  0.0278  -0.0049 137 GLU B O   
2810 C CB  . GLU B 149 ? 0.3923 0.2593 0.2394 0.0200  0.0214  0.0108  137 GLU B CB  
2811 C CG  . GLU B 149 ? 0.5050 0.3506 0.3227 0.0148  0.0395  0.0087  137 GLU B CG  
2812 C CD  . GLU B 149 ? 0.8997 0.7199 0.6835 0.0106  0.0483  0.0160  137 GLU B CD  
2813 O OE1 . GLU B 149 ? 0.8391 0.6579 0.6151 0.0091  0.0340  0.0232  137 GLU B OE1 
2814 O OE2 . GLU B 149 ? 0.9531 0.7551 0.7191 0.0099  0.0711  0.0160  137 GLU B OE2 
2815 N N   . ARG B 150 ? 0.2864 0.1971 0.2075 0.0224  0.0328  0.0039  138 ARG B N   
2816 C CA  . ARG B 150 ? 0.2841 0.2087 0.2311 0.0211  0.0461  0.0061  138 ARG B CA  
2817 C C   . ARG B 150 ? 0.2516 0.2009 0.2187 0.0207  0.0347  -0.0006 138 ARG B C   
2818 O O   . ARG B 150 ? 0.2487 0.2027 0.2243 0.0205  0.0429  -0.0008 138 ARG B O   
2819 C CB  . ARG B 150 ? 0.2780 0.2121 0.2523 0.0175  0.0544  0.0179  138 ARG B CB  
2820 C CG  . ARG B 150 ? 0.2539 0.2021 0.2473 0.0120  0.0385  0.0172  138 ARG B CG  
2821 C CD  . ARG B 150 ? 0.2550 0.2131 0.2735 0.0022  0.0455  0.0327  138 ARG B CD  
2822 N NE  . ARG B 150 ? 0.2356 0.1925 0.2570 -0.0072 0.0300  0.0311  138 ARG B NE  
2823 C CZ  . ARG B 150 ? 0.2129 0.1866 0.2482 -0.0135 0.0194  0.0256  138 ARG B CZ  
2824 N NH1 . ARG B 150 ? 0.2145 0.2121 0.2658 -0.0106 0.0195  0.0214  138 ARG B NH1 
2825 N NH2 . ARG B 150 ? 0.2381 0.2004 0.2664 -0.0242 0.0081  0.0236  138 ARG B NH2 
2826 N N   . MET B 151 ? 0.2418 0.2049 0.2149 0.0217  0.0174  -0.0052 139 MET B N   
2827 C CA  . MET B 151 ? 0.2232 0.2131 0.2145 0.0212  0.0067  -0.0102 139 MET B CA  
2828 C C   . MET B 151 ? 0.2745 0.2612 0.2463 0.0209  0.0011  -0.0133 139 MET B C   
2829 O O   . MET B 151 ? 0.2341 0.2349 0.2188 0.0176  0.0002  -0.0146 139 MET B O   
2830 C CB  . MET B 151 ? 0.2076 0.2101 0.2046 0.0251  -0.0068 -0.0142 139 MET B CB  
2831 C CG  . MET B 151 ? 0.2183 0.2227 0.2308 0.0200  -0.0048 -0.0135 139 MET B CG  
2832 S SD  . MET B 151 ? 0.1951 0.2325 0.2422 0.0088  -0.0039 -0.0104 139 MET B SD  
2833 C CE  . MET B 151 ? 0.2326 0.2963 0.2834 0.0138  -0.0167 -0.0185 139 MET B CE  
2834 N N   A ARG B 152 ? 0.2544 0.2216 0.1936 0.0214  -0.0040 -0.0125 140 ARG B N   
2835 N N   B ARG B 152 ? 0.2558 0.2249 0.1964 0.0217  -0.0051 -0.0126 140 ARG B N   
2836 C CA  A ARG B 152 ? 0.2840 0.2463 0.1993 0.0152  -0.0131 -0.0133 140 ARG B CA  
2837 C CA  B ARG B 152 ? 0.2838 0.2461 0.1992 0.0155  -0.0131 -0.0132 140 ARG B CA  
2838 C C   A ARG B 152 ? 0.3270 0.2602 0.2213 0.0098  0.0031  -0.0166 140 ARG B C   
2839 C C   B ARG B 152 ? 0.2919 0.2292 0.1927 0.0106  0.0036  -0.0165 140 ARG B C   
2840 O O   A ARG B 152 ? 0.2886 0.2170 0.1714 0.0030  -0.0014 -0.0193 140 ARG B O   
2841 O O   B ARG B 152 ? 0.2884 0.2286 0.1897 0.0056  0.0002  -0.0191 140 ARG B O   
2842 C CB  A ARG B 152 ? 0.3178 0.2715 0.2048 0.0137  -0.0260 -0.0073 140 ARG B CB  
2843 C CB  B ARG B 152 ? 0.3236 0.2710 0.2059 0.0131  -0.0232 -0.0076 140 ARG B CB  
2844 C CG  A ARG B 152 ? 0.3765 0.3363 0.2439 0.0032  -0.0434 -0.0034 140 ARG B CG  
2845 C CG  B ARG B 152 ? 0.3920 0.3483 0.2562 0.0035  -0.0425 -0.0029 140 ARG B CG  
2846 C CD  A ARG B 152 ? 0.4687 0.4145 0.3013 -0.0039 -0.0546 0.0066  140 ARG B CD  
2847 C CD  B ARG B 152 ? 0.4825 0.4185 0.3071 -0.0047 -0.0510 0.0058  140 ARG B CD  
2848 N NE  A ARG B 152 ? 0.4661 0.4327 0.2912 -0.0142 -0.0778 0.0178  140 ARG B NE  
2849 N NE  B ARG B 152 ? 0.5650 0.5248 0.3855 -0.0119 -0.0752 0.0194  140 ARG B NE  
2850 C CZ  A ARG B 152 ? 0.4641 0.4200 0.2690 -0.0301 -0.0819 0.0161  140 ARG B CZ  
2851 C CZ  B ARG B 152 ? 0.4351 0.4170 0.2698 -0.0040 -0.0864 0.0340  140 ARG B CZ  
2852 N NH1 A ARG B 152 ? 0.4729 0.3878 0.2449 -0.0381 -0.0692 0.0033  140 ARG B NH1 
2853 N NH1 B ARG B 152 ? 0.5564 0.5360 0.4090 0.0116  -0.0764 0.0336  140 ARG B NH1 
2854 N NH2 A ARG B 152 ? 0.3854 0.3682 0.2070 -0.0349 -0.0936 0.0266  140 ARG B NH2 
2855 N NH2 B ARG B 152 ? 0.5319 0.5409 0.3777 -0.0082 -0.0981 0.0466  140 ARG B NH2 
2856 N N   . THR B 153 ? 0.3107 0.2218 0.1981 0.0130  0.0232  -0.0153 141 THR B N   
2857 C CA  . THR B 153 ? 0.3423 0.2247 0.2138 0.0129  0.0458  -0.0174 141 THR B CA  
2858 C C   . THR B 153 ? 0.3351 0.2391 0.2474 0.0162  0.0521  -0.0158 141 THR B C   
2859 O O   . THR B 153 ? 0.3263 0.2109 0.2261 0.0148  0.0606  -0.0192 141 THR B O   
2860 C CB  . THR B 153 ? 0.3539 0.2184 0.2188 0.0183  0.0677  -0.0119 141 THR B CB  
2861 O OG1 . THR B 153 ? 0.4409 0.2814 0.2620 0.0131  0.0619  -0.0127 141 THR B OG1 
2862 C CG2 . THR B 153 ? 0.4530 0.2916 0.3096 0.0237  0.0975  -0.0113 141 THR B CG2 
2863 N N   . ALA B 154 ? 0.2837 0.2242 0.2419 0.0188  0.0481  -0.0099 142 ALA B N   
2864 C CA  . ALA B 154 ? 0.2580 0.2253 0.2583 0.0191  0.0515  -0.0047 142 ALA B CA  
2865 C C   . ALA B 154 ? 0.2356 0.2155 0.2363 0.0139  0.0341  -0.0103 142 ALA B C   
2866 O O   . ALA B 154 ? 0.2484 0.2260 0.2602 0.0136  0.0414  -0.0082 142 ALA B O   
2867 C CB  . ALA B 154 ? 0.2493 0.2522 0.2902 0.0171  0.0457  0.0031  142 ALA B CB  
2868 N N   . VAL B 155 ? 0.2310 0.2244 0.2213 0.0104  0.0122  -0.0149 143 VAL B N   
2869 C CA  . VAL B 155 ? 0.2430 0.2538 0.2350 0.0043  -0.0056 -0.0166 143 VAL B CA  
2870 C C   . VAL B 155 ? 0.2581 0.2305 0.2102 -0.0025 -0.0033 -0.0201 143 VAL B C   
2871 O O   . VAL B 155 ? 0.2590 0.2335 0.2181 -0.0077 -0.0066 -0.0196 143 VAL B O   
2872 C CB  . VAL B 155 ? 0.2358 0.2724 0.2275 0.0047  -0.0266 -0.0165 143 VAL B CB  
2873 C CG1 . VAL B 155 ? 0.2738 0.3304 0.2644 -0.0028 -0.0457 -0.0140 143 VAL B CG1 
2874 C CG2 . VAL B 155 ? 0.2437 0.3101 0.2695 0.0098  -0.0266 -0.0158 143 VAL B CG2 
2875 N N   . THR B 156 ? 0.2909 0.2244 0.1973 -0.0045 0.0022  -0.0235 144 THR B N   
2876 C CA  . THR B 156 ? 0.3464 0.2325 0.2026 -0.0141 0.0061  -0.0286 144 THR B CA  
2877 C C   . THR B 156 ? 0.3490 0.2095 0.2118 -0.0080 0.0316  -0.0306 144 THR B C   
2878 O O   . THR B 156 ? 0.3780 0.2144 0.2215 -0.0157 0.0298  -0.0339 144 THR B O   
2879 C CB  . THR B 156 ? 0.4254 0.2737 0.2297 -0.0180 0.0109  -0.0311 144 THR B CB  
2880 O OG1 . THR B 156 ? 0.4177 0.2932 0.2211 -0.0229 -0.0142 -0.0248 144 THR B OG1 
2881 C CG2 . THR B 156 ? 0.4846 0.2725 0.2236 -0.0312 0.0173  -0.0386 144 THR B CG2 
2882 N N   . ALA B 157 ? 0.3318 0.1996 0.2256 0.0055  0.0546  -0.0258 145 ALA B N   
2883 C CA  . ALA B 157 ? 0.3583 0.2069 0.2665 0.0151  0.0825  -0.0221 145 ALA B CA  
2884 C C   . ALA B 157 ? 0.3107 0.1928 0.2650 0.0136  0.0729  -0.0159 145 ALA B C   
2885 O O   . ALA B 157 ? 0.3256 0.1807 0.2763 0.0162  0.0867  -0.0154 145 ALA B O   
2886 C CB  . ALA B 157 ? 0.3432 0.2048 0.2827 0.0284  0.1063  -0.0116 145 ALA B CB  
2887 N N   . ALA B 158 ? 0.2699 0.2065 0.2643 0.0095  0.0509  -0.0111 146 ALA B N   
2888 C CA  . ALA B 158 ? 0.2284 0.2024 0.2666 0.0058  0.0399  -0.0038 146 ALA B CA  
2889 C C   . ALA B 158 ? 0.2626 0.2203 0.2732 -0.0055 0.0228  -0.0097 146 ALA B C   
2890 O O   . ALA B 158 ? 0.2783 0.2323 0.3049 -0.0069 0.0259  -0.0050 146 ALA B O   
2891 C CB  . ALA B 158 ? 0.2052 0.2364 0.2810 0.0021  0.0203  0.0004  146 ALA B CB  
2892 N N   . VAL B 159 ? 0.2750 0.2207 0.2433 -0.0150 0.0043  -0.0173 147 VAL B N   
2893 C CA  . VAL B 159 ? 0.3019 0.2294 0.2385 -0.0303 -0.0140 -0.0197 147 VAL B CA  
2894 C C   . VAL B 159 ? 0.3569 0.2148 0.2510 -0.0313 0.0070  -0.0261 147 VAL B C   
2895 O O   . VAL B 159 ? 0.3677 0.2082 0.2564 -0.0394 0.0022  -0.0252 147 VAL B O   
2896 C CB  . VAL B 159 ? 0.3235 0.2542 0.2243 -0.0411 -0.0370 -0.0211 147 VAL B CB  
2897 C CG1 . VAL B 159 ? 0.3845 0.2894 0.2425 -0.0621 -0.0573 -0.0206 147 VAL B CG1 
2898 C CG2 . VAL B 159 ? 0.3051 0.3029 0.2492 -0.0371 -0.0557 -0.0139 147 VAL B CG2 
2899 N N   . ALA B 160 ? 0.3731 0.1860 0.2329 -0.0229 0.0321  -0.0327 148 ALA B N   
2900 C CA  . ALA B 160 ? 0.4601 0.1983 0.2705 -0.0215 0.0575  -0.0407 148 ALA B CA  
2901 C C   . ALA B 160 ? 0.4349 0.1711 0.2883 -0.0063 0.0817  -0.0332 148 ALA B C   
2902 O O   . ALA B 160 ? 0.4894 0.1682 0.3102 -0.0075 0.0954  -0.0382 148 ALA B O   
2903 C CB  . ALA B 160 ? 0.4956 0.1909 0.2612 -0.0143 0.0820  -0.0480 148 ALA B CB  
2904 N N   . ALA B 161 ? 0.3377 0.2112 0.2578 -0.0122 0.1059  -0.0258 149 ALA B N   
2905 C CA  . ALA B 161 ? 0.3221 0.2366 0.3064 -0.0064 0.1119  -0.0390 149 ALA B CA  
2906 C C   . ALA B 161 ? 0.2737 0.2092 0.2917 0.0104  0.0850  -0.0270 149 ALA B C   
2907 O O   . ALA B 161 ? 0.2876 0.2446 0.3496 0.0193  0.0799  -0.0367 149 ALA B O   
2908 C CB  . ALA B 161 ? 0.3903 0.3258 0.4030 -0.0146 0.1297  -0.0512 149 ALA B CB  
2909 N N   . THR B 162 ? 0.2826 0.2070 0.2802 0.0140  0.0680  -0.0106 150 THR B N   
2910 C CA  . THR B 162 ? 0.2927 0.2284 0.3115 0.0224  0.0509  0.0002  150 THR B CA  
2911 C C   . THR B 162 ? 0.2856 0.2094 0.3048 0.0251  0.0436  -0.0006 150 THR B C   
2912 O O   . THR B 162 ? 0.2819 0.1905 0.2805 0.0225  0.0408  -0.0015 150 THR B O   
2913 C CB  . THR B 162 ? 0.2902 0.2270 0.2971 0.0206  0.0428  0.0118  150 THR B CB  
2914 O OG1 . THR B 162 ? 0.3229 0.2684 0.3280 0.0187  0.0477  0.0127  150 THR B OG1 
2915 C CG2 . THR B 162 ? 0.3051 0.2475 0.3250 0.0222  0.0348  0.0206  150 THR B CG2 
2916 N N   . PRO B 163 ? 0.2669 0.1908 0.3064 0.0314  0.0365  -0.0021 151 PRO B N   
2917 C CA  . PRO B 163 ? 0.2558 0.1642 0.2946 0.0324  0.0287  -0.0016 151 PRO B CA  
2918 C C   . PRO B 163 ? 0.2856 0.1889 0.3160 0.0251  0.0250  0.0089  151 PRO B C   
2919 O O   . PRO B 163 ? 0.2972 0.2065 0.3254 0.0211  0.0262  0.0175  151 PRO B O   
2920 C CB  . PRO B 163 ? 0.3185 0.2182 0.3722 0.0411  0.0163  -0.0024 151 PRO B CB  
2921 C CG  . PRO B 163 ? 0.3166 0.2351 0.3923 0.0481  0.0188  -0.0155 151 PRO B CG  
2922 C CD  . PRO B 163 ? 0.3130 0.2450 0.3758 0.0399  0.0303  -0.0073 151 PRO B CD  
2923 N N   . PRO B 164 ? 0.2923 0.1865 0.3226 0.0226  0.0214  0.0041  152 PRO B N   
2924 C CA  . PRO B 164 ? 0.2869 0.1836 0.3260 0.0141  0.0199  0.0047  152 PRO B CA  
2925 C C   . PRO B 164 ? 0.3090 0.1969 0.3498 0.0040  0.0259  0.0139  152 PRO B C   
2926 O O   . PRO B 164 ? 0.3255 0.1914 0.3564 0.0054  0.0226  0.0198  152 PRO B O   
2927 C CB  . PRO B 164 ? 0.3696 0.2560 0.4148 0.0158  0.0115  -0.0072 152 PRO B CB  
2928 C CG  . PRO B 164 ? 0.3560 0.2304 0.3922 0.0230  0.0110  -0.0093 152 PRO B CG  
2929 C CD  . PRO B 164 ? 0.2896 0.1725 0.3159 0.0271  0.0191  -0.0071 152 PRO B CD  
2930 N N   . ALA B 165 ? 0.2803 0.1787 0.3300 -0.0075 0.0343  0.0123  153 ALA B N   
2931 C CA  . ALA B 165 ? 0.3000 0.1801 0.3379 -0.0238 0.0475  0.0195  153 ALA B CA  
2932 C C   . ALA B 165 ? 0.3644 0.2199 0.4055 -0.0347 0.0505  0.0161  153 ALA B C   
2933 O O   . ALA B 165 ? 0.3447 0.2136 0.4160 -0.0337 0.0459  0.0013  153 ALA B O   
2934 C CB  . ALA B 165 ? 0.2991 0.2026 0.3565 -0.0372 0.0618  0.0093  153 ALA B CB  
2935 N N   . PRO B 166 ? 0.3835 0.1953 0.3888 -0.0470 0.0573  0.0284  154 PRO B N   
2936 C CA  . PRO B 166 ? 0.4286 0.2076 0.4305 -0.0620 0.0627  0.0260  154 PRO B CA  
2937 C C   . PRO B 166 ? 0.4062 0.2014 0.4414 -0.0879 0.0878  0.0084  154 PRO B C   
2938 O O   . PRO B 166 ? 0.4729 0.2598 0.5295 -0.0985 0.0914  -0.0025 154 PRO B O   
2939 C CB  . PRO B 166 ? 0.5112 0.2237 0.4478 -0.0684 0.0603  0.0453  154 PRO B CB  
2940 C CG  . PRO B 166 ? 0.5333 0.2499 0.4443 -0.0636 0.0615  0.0543  154 PRO B CG  
2941 C CD  . PRO B 166 ? 0.4601 0.2405 0.4186 -0.0438 0.0534  0.0449  154 PRO B CD  
2942 N N   . ASP B 167 ? 0.4685 0.2906 0.5169 -0.0984 0.1053  0.0004  155 ASP B N   
2943 C CA  . ASP B 167 ? 0.4321 0.2851 0.5302 -0.1191 0.1269  -0.0270 155 ASP B CA  
2944 C C   . ASP B 167 ? 0.4080 0.3039 0.5346 -0.1163 0.1323  -0.0397 155 ASP B C   
2945 O O   . ASP B 167 ? 0.4574 0.3450 0.5453 -0.1089 0.1303  -0.0218 155 ASP B O   
2946 C CB  . ASP B 167 ? 0.5957 0.4187 0.6572 -0.1436 0.1509  -0.0258 155 ASP B CB  
2947 C CG  . ASP B 167 ? 0.9085 0.7047 0.9075 -0.1505 0.1629  -0.0104 155 ASP B CG  
2948 O OD1 . ASP B 167 ? 0.9930 0.7596 0.9444 -0.1352 0.1437  0.0139  155 ASP B OD1 
2949 O OD2 . ASP B 167 ? 1.0828 0.8865 1.0821 -0.1695 0.1902  -0.0266 155 ASP B OD2 
2950 N N   . GLY B 168 ? 0.4121 0.3544 0.6064 -0.1169 0.1325  -0.0730 156 GLY B N   
2951 C CA  . GLY B 168 ? 0.3161 0.2983 0.5405 -0.1103 0.1310  -0.0889 156 GLY B CA  
2952 C C   . GLY B 168 ? 0.3138 0.3063 0.5297 -0.0788 0.0959  -0.0779 156 GLY B C   
2953 O O   . GLY B 168 ? 0.3752 0.3530 0.5738 -0.0599 0.0716  -0.0665 156 GLY B O   
2954 N N   . THR B 169 ? 0.2686 0.2810 0.4843 -0.0735 0.0956  -0.0794 157 THR B N   
2955 C CA  . THR B 169 ? 0.2313 0.2524 0.4385 -0.0460 0.0641  -0.0744 157 THR B CA  
2956 C C   . THR B 169 ? 0.2239 0.2177 0.3687 -0.0364 0.0606  -0.0391 157 THR B C   
2957 O O   . THR B 169 ? 0.2685 0.2483 0.3813 -0.0463 0.0780  -0.0226 157 THR B O   
2958 C CB  . THR B 169 ? 0.2349 0.2883 0.4737 -0.0465 0.0662  -0.0946 157 THR B CB  
2959 O OG1 . THR B 169 ? 0.2787 0.3641 0.5918 -0.0555 0.0697  -0.1369 157 THR B OG1 
2960 C CG2 . THR B 169 ? 0.2408 0.2937 0.4639 -0.0206 0.0332  -0.0898 157 THR B CG2 
2961 N N   . THR B 170 ? 0.2116 0.1947 0.3388 -0.0176 0.0380  -0.0316 158 THR B N   
2962 C CA  . THR B 170 ? 0.2201 0.1879 0.3056 -0.0083 0.0354  -0.0085 158 THR B CA  
2963 C C   . THR B 170 ? 0.2211 0.2027 0.3015 -0.0025 0.0315  -0.0072 158 THR B C   
2964 O O   . THR B 170 ? 0.2228 0.2137 0.3178 0.0049  0.0161  -0.0220 158 THR B O   
2965 C CB  . THR B 170 ? 0.2302 0.1816 0.2994 0.0043  0.0203  -0.0074 158 THR B CB  
2966 O OG1 . THR B 170 ? 0.2559 0.1958 0.3336 0.0003  0.0215  -0.0108 158 THR B OG1 
2967 C CG2 . THR B 170 ? 0.2972 0.2393 0.3378 0.0101  0.0236  0.0078  158 THR B CG2 
2968 N N   . ARG B 171 ? 0.1965 0.1745 0.2551 -0.0036 0.0402  0.0084  159 ARG B N   
2969 C CA  A ARG B 171 ? 0.2110 0.2024 0.2667 0.0008  0.0376  0.0094  159 ARG B CA  
2970 C CA  B ARG B 171 ? 0.2102 0.2018 0.2662 0.0003  0.0381  0.0093  159 ARG B CA  
2971 C C   . ARG B 171 ? 0.2345 0.2163 0.2670 0.0086  0.0352  0.0239  159 ARG B C   
2972 O O   . ARG B 171 ? 0.2506 0.2183 0.2707 0.0087  0.0384  0.0331  159 ARG B O   
2973 C CB  A ARG B 171 ? 0.2338 0.2339 0.2931 -0.0110 0.0533  0.0071  159 ARG B CB  
2974 C CB  B ARG B 171 ? 0.2336 0.2334 0.2949 -0.0132 0.0554  0.0057  159 ARG B CB  
2975 C CG  A ARG B 171 ? 0.1642 0.1828 0.2601 -0.0225 0.0623  -0.0156 159 ARG B CG  
2976 C CG  B ARG B 171 ? 0.2263 0.2430 0.2896 -0.0109 0.0554  0.0023  159 ARG B CG  
2977 C CD  A ARG B 171 ? 0.2164 0.2419 0.3096 -0.0379 0.0850  -0.0208 159 ARG B CD  
2978 C CD  B ARG B 171 ? 0.2414 0.2631 0.3079 -0.0290 0.0791  -0.0072 159 ARG B CD  
2979 N NE  A ARG B 171 ? 0.2045 0.2541 0.3445 -0.0543 0.1021  -0.0508 159 ARG B NE  
2980 N NE  B ARG B 171 ? 0.2452 0.2908 0.3599 -0.0400 0.0881  -0.0353 159 ARG B NE  
2981 C CZ  A ARG B 171 ? 0.3231 0.3593 0.4639 -0.0769 0.1276  -0.0565 159 ARG B CZ  
2982 C CZ  B ARG B 171 ? 0.2371 0.2753 0.3610 -0.0600 0.1101  -0.0443 159 ARG B CZ  
2983 N NH1 A ARG B 171 ? 0.2764 0.2673 0.3622 -0.0846 0.1359  -0.0309 159 ARG B NH1 
2984 N NH1 B ARG B 171 ? 0.2918 0.2889 0.3678 -0.0715 0.1237  -0.0235 159 ARG B NH1 
2985 N NH2 A ARG B 171 ? 0.2201 0.2804 0.4108 -0.0877 0.1374  -0.0900 159 ARG B NH2 
2986 N NH2 B ARG B 171 ? 0.2204 0.2896 0.4052 -0.0681 0.1158  -0.0780 159 ARG B NH2 
2987 N N   . VAL B 172 ? 0.2217 0.2073 0.2495 0.0152  0.0275  0.0227  160 VAL B N   
2988 C CA  . VAL B 172 ? 0.2419 0.2247 0.2598 0.0196  0.0289  0.0295  160 VAL B CA  
2989 C C   . VAL B 172 ? 0.2142 0.2090 0.2332 0.0214  0.0260  0.0300  160 VAL B C   
2990 O O   . VAL B 172 ? 0.2217 0.2196 0.2416 0.0221  0.0184  0.0235  160 VAL B O   
2991 C CB  . VAL B 172 ? 0.2715 0.2395 0.2762 0.0199  0.0300  0.0259  160 VAL B CB  
2992 C CG1 . VAL B 172 ? 0.3168 0.2680 0.3003 0.0197  0.0202  0.0209  160 VAL B CG1 
2993 C CG2 . VAL B 172 ? 0.2809 0.2522 0.2901 0.0200  0.0390  0.0244  160 VAL B CG2 
2994 N N   . ALA B 173 ? 0.2145 0.2127 0.2339 0.0245  0.0272  0.0351  161 ALA B N   
2995 C CA  . ALA B 173 ? 0.2205 0.2291 0.2414 0.0278  0.0232  0.0349  161 ALA B CA  
2996 C C   . ALA B 173 ? 0.2148 0.2231 0.2400 0.0289  0.0236  0.0317  161 ALA B C   
2997 O O   . ALA B 173 ? 0.2092 0.2150 0.2436 0.0292  0.0288  0.0279  161 ALA B O   
2998 C CB  . ALA B 173 ? 0.2421 0.2459 0.2546 0.0314  0.0208  0.0397  161 ALA B CB  
2999 N N   . VAL B 174 ? 0.2053 0.2143 0.2255 0.0278  0.0195  0.0298  162 VAL B N   
3000 C CA  . VAL B 174 ? 0.2060 0.2056 0.2215 0.0227  0.0247  0.0262  162 VAL B CA  
3001 C C   . VAL B 174 ? 0.1993 0.2101 0.2239 0.0264  0.0177  0.0252  162 VAL B C   
3002 O O   . VAL B 174 ? 0.2101 0.2201 0.2262 0.0292  0.0066  0.0257  162 VAL B O   
3003 C CB  . VAL B 174 ? 0.2316 0.1997 0.2129 0.0157  0.0238  0.0257  162 VAL B CB  
3004 C CG1 . VAL B 174 ? 0.2823 0.2272 0.2435 0.0043  0.0340  0.0228  162 VAL B CG1 
3005 C CG2 . VAL B 174 ? 0.2724 0.2278 0.2437 0.0129  0.0304  0.0249  162 VAL B CG2 
3006 N N   . VAL B 175 ? 0.1871 0.2100 0.2352 0.0282  0.0211  0.0196  163 VAL B N   
3007 C CA  . VAL B 175 ? 0.1962 0.2307 0.2571 0.0337  0.0120  0.0168  163 VAL B CA  
3008 C C   . VAL B 175 ? 0.1723 0.1961 0.2333 0.0217  0.0216  0.0102  163 VAL B C   
3009 O O   . VAL B 175 ? 0.1860 0.2099 0.2650 0.0116  0.0385  -0.0011 163 VAL B O   
3010 C CB  . VAL B 175 ? 0.1925 0.2404 0.2784 0.0458  0.0026  0.0110  163 VAL B CB  
3011 C CG1 . VAL B 175 ? 0.2234 0.2797 0.3176 0.0530  -0.0100 0.0075  163 VAL B CG1 
3012 C CG2 . VAL B 175 ? 0.2235 0.2630 0.2909 0.0531  -0.0043 0.0193  163 VAL B CG2 
3013 N N   . GLY B 176 ? 0.1878 0.1991 0.2278 0.0209  0.0119  0.0143  164 GLY B N   
3014 C CA  . GLY B 176 ? 0.2045 0.1907 0.2289 0.0073  0.0188  0.0108  164 GLY B CA  
3015 C C   . GLY B 176 ? 0.1978 0.1888 0.2272 0.0142  0.0020  0.0101  164 GLY B C   
3016 O O   . GLY B 176 ? 0.1956 0.2168 0.2531 0.0279  -0.0092 0.0076  164 GLY B O   
3017 N N   . HIS B 177 ? 0.2371 0.1879 0.2300 0.0034  -0.0005 0.0117  165 HIS B N   
3018 C CA  . HIS B 177 ? 0.2145 0.1581 0.2083 0.0045  -0.0133 0.0088  165 HIS B CA  
3019 C C   . HIS B 177 ? 0.2643 0.1739 0.2179 0.0123  -0.0407 0.0128  165 HIS B C   
3020 O O   . HIS B 177 ? 0.3093 0.1762 0.2177 0.0081  -0.0460 0.0169  165 HIS B O   
3021 C CB  . HIS B 177 ? 0.2523 0.1679 0.2388 -0.0203 0.0114  0.0023  165 HIS B CB  
3022 C CG  . HIS B 177 ? 0.2456 0.2021 0.2906 -0.0254 0.0347  -0.0122 165 HIS B CG  
3023 N ND1 . HIS B 177 ? 0.2103 0.2064 0.3126 -0.0157 0.0276  -0.0250 165 HIS B ND1 
3024 C CD2 . HIS B 177 ? 0.2518 0.2177 0.3117 -0.0340 0.0577  -0.0194 165 HIS B CD2 
3025 C CE1 . HIS B 177 ? 0.2185 0.2439 0.3716 -0.0184 0.0439  -0.0425 165 HIS B CE1 
3026 N NE2 . HIS B 177 ? 0.2261 0.2359 0.3567 -0.0302 0.0639  -0.0399 165 HIS B NE2 
3027 N N   . ASP B 178 ? 0.2082 0.2134 0.2322 -0.0031 0.0058  0.0086  166 ASP B N   
3028 C CA  . ASP B 178 ? 0.2084 0.2039 0.2231 -0.0017 0.0034  0.0052  166 ASP B CA  
3029 C C   . ASP B 178 ? 0.2081 0.1986 0.2197 -0.0033 0.0050  0.0070  166 ASP B C   
3030 O O   . ASP B 178 ? 0.2140 0.2021 0.2204 -0.0006 0.0070  0.0057  166 ASP B O   
3031 C CB  . ASP B 178 ? 0.2364 0.2260 0.2486 -0.0035 -0.0033 0.0028  166 ASP B CB  
3032 C CG  . ASP B 178 ? 0.2411 0.2195 0.2455 -0.0012 -0.0058 -0.0008 166 ASP B CG  
3033 O OD1 . ASP B 178 ? 0.2696 0.2481 0.2700 0.0036  -0.0037 -0.0030 166 ASP B OD1 
3034 O OD2 . ASP B 178 ? 0.2658 0.2355 0.2696 -0.0045 -0.0103 -0.0006 166 ASP B OD2 
3035 N N   . SER B 179 ? 0.2039 0.1931 0.2185 -0.0082 0.0035  0.0107  167 SER B N   
3036 C CA  . SER B 179 ? 0.2082 0.1914 0.2185 -0.0102 0.0034  0.0134  167 SER B CA  
3037 C C   . SER B 179 ? 0.2098 0.1989 0.2177 -0.0094 0.0100  0.0152  167 SER B C   
3038 O O   . SER B 179 ? 0.2089 0.1936 0.2096 -0.0084 0.0101  0.0151  167 SER B O   
3039 C CB  . SER B 179 ? 0.2181 0.1984 0.2326 -0.0167 -0.0003 0.0184  167 SER B CB  
3040 O OG  . SER B 179 ? 0.2693 0.2402 0.2834 -0.0174 -0.0077 0.0149  167 SER B OG  
3041 N N   . ALA B 180 ? 0.2244 0.2236 0.2381 -0.0095 0.0154  0.0163  168 ALA B N   
3042 C CA  . ALA B 180 ? 0.2013 0.2049 0.2110 -0.0080 0.0222  0.0161  168 ALA B CA  
3043 C C   . ALA B 180 ? 0.2065 0.2059 0.2096 -0.0035 0.0225  0.0109  168 ALA B C   
3044 O O   . ALA B 180 ? 0.2164 0.2142 0.2115 -0.0034 0.0246  0.0100  168 ALA B O   
3045 C CB  . ALA B 180 ? 0.2110 0.2257 0.2297 -0.0073 0.0282  0.0173  168 ALA B CB  
3046 N N   . LEU B 181 ? 0.1959 0.1944 0.2022 -0.0006 0.0199  0.0080  169 LEU B N   
3047 C CA  . LEU B 181 ? 0.2063 0.2021 0.2083 0.0027  0.0197  0.0044  169 LEU B CA  
3048 C C   . LEU B 181 ? 0.2188 0.2087 0.2139 0.0027  0.0157  0.0042  169 LEU B C   
3049 O O   . LEU B 181 ? 0.2092 0.1977 0.1990 0.0034  0.0161  0.0031  169 LEU B O   
3050 C CB  . LEU B 181 ? 0.1920 0.1903 0.1996 0.0052  0.0181  0.0031  169 LEU B CB  
3051 C CG  . LEU B 181 ? 0.2085 0.2127 0.2242 0.0065  0.0216  0.0037  169 LEU B CG  
3052 C CD1 . LEU B 181 ? 0.2118 0.2189 0.2323 0.0080  0.0185  0.0043  169 LEU B CD1 
3053 C CD2 . LEU B 181 ? 0.2335 0.2361 0.2473 0.0085  0.0260  0.0012  169 LEU B CD2 
3054 N N   . VAL B 182 ? 0.2130 0.1987 0.2085 0.0020  0.0114  0.0054  170 VAL B N   
3055 C CA  . VAL B 182 ? 0.2164 0.1962 0.2073 0.0032  0.0076  0.0057  170 VAL B CA  
3056 C C   . VAL B 182 ? 0.2130 0.1912 0.1987 0.0002  0.0081  0.0094  170 VAL B C   
3057 O O   . VAL B 182 ? 0.2319 0.2083 0.2130 0.0012  0.0063  0.0100  170 VAL B O   
3058 C CB  . VAL B 182 ? 0.2458 0.2192 0.2384 0.0037  0.0028  0.0051  170 VAL B CB  
3059 C CG1 . VAL B 182 ? 0.2560 0.2219 0.2456 0.0053  -0.0011 0.0064  170 VAL B CG1 
3060 C CG2 . VAL B 182 ? 0.2511 0.2270 0.2457 0.0071  0.0021  0.0009  170 VAL B CG2 
3061 N N   . ILE B 183 ? 0.2146 0.1948 0.2009 -0.0038 0.0106  0.0126  171 ILE B N   
3062 C CA  . ILE B 183 ? 0.2392 0.2201 0.2190 -0.0071 0.0121  0.0167  171 ILE B CA  
3063 C C   . ILE B 183 ? 0.2256 0.2099 0.1984 -0.0060 0.0156  0.0136  171 ILE B C   
3064 O O   . ILE B 183 ? 0.2369 0.2196 0.2018 -0.0071 0.0137  0.0152  171 ILE B O   
3065 C CB  . ILE B 183 ? 0.2184 0.2039 0.2012 -0.0117 0.0153  0.0213  171 ILE B CB  
3066 C CG1 . ILE B 183 ? 0.2237 0.2025 0.2115 -0.0147 0.0093  0.0257  171 ILE B CG1 
3067 C CG2 . ILE B 183 ? 0.2463 0.2358 0.2206 -0.0147 0.0189  0.0250  171 ILE B CG2 
3068 C CD1 . ILE B 183 ? 0.2487 0.2332 0.2433 -0.0200 0.0113  0.0307  171 ILE B CD1 
3069 N N   . LEU B 184 ? 0.2255 0.2138 0.2012 -0.0040 0.0201  0.0092  172 LEU B N   
3070 C CA  . LEU B 184 ? 0.2175 0.2061 0.1865 -0.0030 0.0225  0.0051  172 LEU B CA  
3071 C C   . LEU B 184 ? 0.2127 0.1977 0.1790 -0.0019 0.0172  0.0041  172 LEU B C   
3072 O O   . LEU B 184 ? 0.2340 0.2180 0.1916 -0.0037 0.0159  0.0038  172 LEU B O   
3073 C CB  . LEU B 184 ? 0.2382 0.2295 0.2133 -0.0001 0.0271  0.0008  172 LEU B CB  
3074 C CG  . LEU B 184 ? 0.2190 0.2074 0.1884 0.0011  0.0285  -0.0046 172 LEU B CG  
3075 C CD1 . LEU B 184 ? 0.2470 0.2355 0.2048 -0.0009 0.0320  -0.0061 172 LEU B CD1 
3076 C CD2 . LEU B 184 ? 0.2416 0.2310 0.2202 0.0046  0.0321  -0.0076 172 LEU B CD2 
3077 N N   . MET B 185 ? 0.2111 0.1957 0.1849 0.0008  0.0143  0.0036  173 MET B N   
3078 C CA  . MET B 185 ? 0.2312 0.2155 0.2047 0.0022  0.0103  0.0031  173 MET B CA  
3079 C C   . MET B 185 ? 0.2352 0.2176 0.2046 0.0013  0.0058  0.0071  173 MET B C   
3080 O O   . MET B 185 ? 0.2502 0.2337 0.2161 0.0004  0.0028  0.0077  173 MET B O   
3081 C CB  . MET B 185 ? 0.2246 0.2110 0.2060 0.0056  0.0093  0.0021  173 MET B CB  
3082 C CG  . MET B 185 ? 0.2416 0.2303 0.2267 0.0061  0.0123  -0.0006 173 MET B CG  
3083 S SD  . MET B 185 ? 0.2393 0.2326 0.2323 0.0092  0.0112  -0.0004 173 MET B SD  
3084 C CE  . MET B 185 ? 0.2577 0.2508 0.2534 0.0100  0.0118  -0.0002 173 MET B CE  
3085 N N   . GLY B 186 ? 0.2412 0.2206 0.2120 0.0012  0.0043  0.0104  174 GLY B N   
3086 C CA  . GLY B 186 ? 0.2549 0.2314 0.2226 0.0004  -0.0003 0.0154  174 GLY B CA  
3087 C C   . GLY B 186 ? 0.2543 0.2325 0.2119 -0.0042 0.0001  0.0179  174 GLY B C   
3088 O O   . GLY B 186 ? 0.2725 0.2516 0.2264 -0.0048 -0.0042 0.0204  174 GLY B O   
3089 N N   . SER B 187 ? 0.2616 0.2415 0.2144 -0.0071 0.0053  0.0169  175 SER B N   
3090 C CA  A SER B 187 ? 0.2712 0.2533 0.2118 -0.0112 0.0067  0.0182  175 SER B CA  
3091 C CA  B SER B 187 ? 0.2716 0.2538 0.2120 -0.0112 0.0069  0.0181  175 SER B CA  
3092 C C   . SER B 187 ? 0.2762 0.2591 0.2106 -0.0115 0.0052  0.0136  175 SER B C   
3093 O O   . SER B 187 ? 0.2879 0.2716 0.2118 -0.0148 0.0021  0.0158  175 SER B O   
3094 C CB  A SER B 187 ? 0.2856 0.2713 0.2233 -0.0129 0.0143  0.0168  175 SER B CB  
3095 C CB  B SER B 187 ? 0.2858 0.2716 0.2237 -0.0128 0.0146  0.0165  175 SER B CB  
3096 O OG  A SER B 187 ? 0.3451 0.3318 0.2830 -0.0106 0.0188  0.0092  175 SER B OG  
3097 O OG  B SER B 187 ? 0.2555 0.2443 0.1797 -0.0156 0.0181  0.0149  175 SER B OG  
3098 N N   . LEU B 188 ? 0.2516 0.2342 0.1922 -0.0087 0.0065  0.0079  176 LEU B N   
3099 C CA  . LEU B 188 ? 0.2831 0.2652 0.2194 -0.0099 0.0042  0.0040  176 LEU B CA  
3100 C C   . LEU B 188 ? 0.2755 0.2595 0.2143 -0.0103 -0.0034 0.0083  176 LEU B C   
3101 O O   . LEU B 188 ? 0.3140 0.2987 0.2481 -0.0131 -0.0072 0.0068  176 LEU B O   
3102 C CB  . LEU B 188 ? 0.2563 0.2374 0.2006 -0.0072 0.0070  -0.0013 176 LEU B CB  
3103 C CG  . LEU B 188 ? 0.2694 0.2489 0.2118 -0.0064 0.0142  -0.0061 176 LEU B CG  
3104 C CD1 . LEU B 188 ? 0.2671 0.2455 0.2201 -0.0033 0.0158  -0.0093 176 LEU B CD1 
3105 C CD2 . LEU B 188 ? 0.3005 0.2774 0.2286 -0.0091 0.0163  -0.0107 176 LEU B CD2 
3106 N N   . MET B 189 ? 0.2746 0.2596 0.2214 -0.0074 -0.0060 0.0135  177 MET B N   
3107 C CA  A MET B 189 ? 0.2908 0.2789 0.2418 -0.0064 -0.0128 0.0185  177 MET B CA  
3108 C CA  B MET B 189 ? 0.2935 0.2816 0.2440 -0.0066 -0.0129 0.0185  177 MET B CA  
3109 C C   . MET B 189 ? 0.2953 0.2821 0.2415 -0.0080 -0.0166 0.0256  177 MET B C   
3110 O O   . MET B 189 ? 0.3014 0.2899 0.2539 -0.0056 -0.0221 0.0310  177 MET B O   
3111 C CB  A MET B 189 ? 0.2979 0.2884 0.2626 -0.0004 -0.0131 0.0184  177 MET B CB  
3112 C CB  B MET B 189 ? 0.2999 0.2907 0.2641 -0.0008 -0.0133 0.0184  177 MET B CB  
3113 C CG  A MET B 189 ? 0.3157 0.3104 0.2857 0.0001  -0.0116 0.0143  177 MET B CG  
3114 C CG  B MET B 189 ? 0.2742 0.2671 0.2426 -0.0002 -0.0098 0.0131  177 MET B CG  
3115 S SD  A MET B 189 ? 0.4140 0.4145 0.3980 0.0071  -0.0103 0.0142  177 MET B SD  
3116 S SD  B MET B 189 ? 0.2539 0.2546 0.2359 0.0053  -0.0115 0.0148  177 MET B SD  
3117 C CE  A MET B 189 ? 0.2708 0.2643 0.2537 0.0092  -0.0054 0.0109  177 MET B CE  
3118 C CE  B MET B 189 ? 0.2070 0.2037 0.1922 0.0107  -0.0118 0.0169  177 MET B CE  
3119 N N   . ASN B 190 ? 0.2757 0.2603 0.2116 -0.0119 -0.0137 0.0266  178 ASN B N   
3120 C CA  . ASN B 190 ? 0.3220 0.3056 0.2530 -0.0145 -0.0173 0.0350  178 ASN B CA  
3121 C C   . ASN B 190 ? 0.2855 0.2643 0.2282 -0.0102 -0.0198 0.0400  178 ASN B C   
3122 O O   . ASN B 190 ? 0.3298 0.3073 0.2740 -0.0102 -0.0259 0.0478  178 ASN B O   
3123 C CB  . ASN B 190 ? 0.3142 0.3017 0.2380 -0.0178 -0.0245 0.0396  178 ASN B CB  
3124 C CG  . ASN B 190 ? 0.4142 0.4018 0.3290 -0.0220 -0.0274 0.0485  178 ASN B CG  
3125 O OD1 . ASN B 190 ? 0.4913 0.4774 0.4003 -0.0245 -0.0224 0.0497  178 ASN B OD1 
3126 N ND2 . ASN B 190 ? 0.4356 0.4257 0.3507 -0.0229 -0.0358 0.0562  178 ASN B ND2 
3127 N N   . LEU B 191 ? 0.2694 0.2450 0.2204 -0.0066 -0.0160 0.0355  179 LEU B N   
3128 C CA  . LEU B 191 ? 0.2853 0.2542 0.2459 -0.0027 -0.0182 0.0378  179 LEU B CA  
3129 C C   . LEU B 191 ? 0.2984 0.2630 0.2579 -0.0061 -0.0148 0.0388  179 LEU B C   
3130 O O   . LEU B 191 ? 0.3304 0.2990 0.2863 -0.0085 -0.0088 0.0348  179 LEU B O   
3131 C CB  . LEU B 191 ? 0.2635 0.2326 0.2337 0.0038  -0.0171 0.0315  179 LEU B CB  
3132 C CG  . LEU B 191 ? 0.2694 0.2454 0.2433 0.0071  -0.0198 0.0311  179 LEU B CG  
3133 C CD1 . LEU B 191 ? 0.2915 0.2695 0.2741 0.0132  -0.0174 0.0254  179 LEU B CD1 
3134 C CD2 . LEU B 191 ? 0.3064 0.2820 0.2840 0.0093  -0.0265 0.0384  179 LEU B CD2 
3135 N N   . GLY B 192 ? 0.2968 0.2535 0.2609 -0.0060 -0.0187 0.0443  180 GLY B N   
3136 C CA  . GLY B 192 ? 0.2989 0.2516 0.2642 -0.0102 -0.0168 0.0466  180 GLY B CA  
3137 C C   . GLY B 192 ? 0.2735 0.2192 0.2479 -0.0062 -0.0173 0.0408  180 GLY B C   
3138 O O   . GLY B 192 ? 0.2875 0.2303 0.2666 0.0004  -0.0193 0.0360  180 GLY B O   
3139 N N   . TRP B 193 ? 0.2831 0.2263 0.2599 -0.0106 -0.0159 0.0420  181 TRP B N   
3140 C CA  . TRP B 193 ? 0.2858 0.2229 0.2692 -0.0082 -0.0168 0.0360  181 TRP B CA  
3141 C C   . TRP B 193 ? 0.2693 0.1936 0.2571 -0.0027 -0.0233 0.0347  181 TRP B C   
3142 O O   . TRP B 193 ? 0.3057 0.2209 0.2951 -0.0041 -0.0285 0.0416  181 TRP B O   
3143 C CB  . TRP B 193 ? 0.2838 0.2197 0.2703 -0.0152 -0.0165 0.0399  181 TRP B CB  
3144 C CG  . TRP B 193 ? 0.2633 0.1930 0.2556 -0.0141 -0.0187 0.0338  181 TRP B CG  
3145 C CD1 . TRP B 193 ? 0.2731 0.1877 0.2694 -0.0145 -0.0257 0.0337  181 TRP B CD1 
3146 C CD2 . TRP B 193 ? 0.2604 0.1974 0.2545 -0.0129 -0.0149 0.0271  181 TRP B CD2 
3147 N NE1 . TRP B 193 ? 0.2761 0.1891 0.2748 -0.0137 -0.0262 0.0264  181 TRP B NE1 
3148 C CE2 . TRP B 193 ? 0.2666 0.1940 0.2645 -0.0132 -0.0199 0.0233  181 TRP B CE2 
3149 C CE3 . TRP B 193 ? 0.2458 0.1958 0.2386 -0.0118 -0.0082 0.0242  181 TRP B CE3 
3150 C CZ2 . TRP B 193 ? 0.2706 0.2027 0.2704 -0.0126 -0.0187 0.0173  181 TRP B CZ2 
3151 C CZ3 . TRP B 193 ? 0.2996 0.2537 0.2960 -0.0108 -0.0069 0.0190  181 TRP B CZ3 
3152 C CH2 . TRP B 193 ? 0.2867 0.2329 0.2863 -0.0115 -0.0122 0.0161  181 TRP B CH2 
3153 N N   . GLY B 194 ? 0.2739 0.1972 0.2640 0.0038  -0.0227 0.0261  182 GLY B N   
3154 C CA  . GLY B 194 ? 0.2938 0.2061 0.2877 0.0109  -0.0272 0.0225  182 GLY B CA  
3155 C C   . GLY B 194 ? 0.2912 0.2097 0.2862 0.0186  -0.0265 0.0211  182 GLY B C   
3156 O O   . GLY B 194 ? 0.3080 0.2218 0.3064 0.0265  -0.0278 0.0156  182 GLY B O   
3157 N N   . GLN B 195 ? 0.2727 0.2020 0.2648 0.0163  -0.0247 0.0258  183 GLN B N   
3158 C CA  . GLN B 195 ? 0.2734 0.2103 0.2681 0.0224  -0.0249 0.0254  183 GLN B CA  
3159 C C   . GLN B 195 ? 0.2507 0.1973 0.2460 0.0260  -0.0199 0.0178  183 GLN B C   
3160 O O   . GLN B 195 ? 0.2619 0.2100 0.2619 0.0336  -0.0197 0.0137  183 GLN B O   
3161 C CB  . GLN B 195 ? 0.2647 0.2089 0.2553 0.0178  -0.0261 0.0330  183 GLN B CB  
3162 C CG  . GLN B 195 ? 0.2813 0.2168 0.2721 0.0152  -0.0319 0.0421  183 GLN B CG  
3163 C CD  . GLN B 195 ? 0.3203 0.2636 0.3060 0.0113  -0.0343 0.0498  183 GLN B CD  
3164 O OE1 . GLN B 195 ? 0.3076 0.2575 0.2842 0.0046  -0.0311 0.0506  183 GLN B OE1 
3165 N NE2 . GLN B 195 ? 0.3508 0.2934 0.3421 0.0156  -0.0400 0.0556  183 GLN B NE2 
3166 N N   . LEU B 196 ? 0.2527 0.2059 0.2436 0.0208  -0.0157 0.0160  184 LEU B N   
3167 C CA  . LEU B 196 ? 0.2483 0.2091 0.2401 0.0232  -0.0115 0.0099  184 LEU B CA  
3168 C C   . LEU B 196 ? 0.2483 0.2018 0.2404 0.0241  -0.0115 0.0049  184 LEU B C   
3169 O O   . LEU B 196 ? 0.2573 0.2096 0.2475 0.0190  -0.0102 0.0045  184 LEU B O   
3170 C CB  . LEU B 196 ? 0.2494 0.2177 0.2375 0.0177  -0.0078 0.0102  184 LEU B CB  
3171 C CG  . LEU B 196 ? 0.2628 0.2395 0.2529 0.0195  -0.0042 0.0059  184 LEU B CG  
3172 C CD1 . LEU B 196 ? 0.2852 0.2701 0.2792 0.0236  -0.0046 0.0062  184 LEU B CD1 
3173 C CD2 . LEU B 196 ? 0.2880 0.2680 0.2748 0.0140  -0.0008 0.0059  184 LEU B CD2 
3174 N N   . ASP B 197 ? 0.2515 0.2001 0.2460 0.0309  -0.0131 0.0009  185 ASP B N   
3175 C CA  . ASP B 197 ? 0.2719 0.2088 0.2652 0.0315  -0.0154 -0.0039 185 ASP B CA  
3176 C C   . ASP B 197 ? 0.2730 0.2165 0.2638 0.0335  -0.0122 -0.0107 185 ASP B C   
3177 O O   . ASP B 197 ? 0.2786 0.2224 0.2688 0.0407  -0.0115 -0.0165 185 ASP B O   
3178 C CB  . ASP B 197 ? 0.2850 0.2106 0.2811 0.0385  -0.0193 -0.0053 185 ASP B CB  
3179 C CG  . ASP B 197 ? 0.3135 0.2234 0.3075 0.0390  -0.0230 -0.0114 185 ASP B CG  
3180 O OD1 . ASP B 197 ? 0.3088 0.2150 0.3005 0.0313  -0.0244 -0.0109 185 ASP B OD1 
3181 O OD2 . ASP B 197 ? 0.3317 0.2330 0.3268 0.0473  -0.0247 -0.0169 185 ASP B OD2 
3182 N N   . MET B 198 ? 0.2699 0.2194 0.2595 0.0273  -0.0101 -0.0095 186 MET B N   
3183 C CA  . MET B 198 ? 0.2536 0.2115 0.2414 0.0283  -0.0073 -0.0137 186 MET B CA  
3184 C C   . MET B 198 ? 0.2275 0.1849 0.2149 0.0216  -0.0080 -0.0131 186 MET B C   
3185 O O   . MET B 198 ? 0.2630 0.2196 0.2526 0.0160  -0.0080 -0.0083 186 MET B O   
3186 C CB  . MET B 198 ? 0.2808 0.2525 0.2707 0.0285  -0.0030 -0.0106 186 MET B CB  
3187 C CG  . MET B 198 ? 0.2525 0.2290 0.2449 0.0345  -0.0023 -0.0099 186 MET B CG  
3188 S SD  . MET B 198 ? 0.2877 0.2785 0.2833 0.0322  0.0009  -0.0056 186 MET B SD  
3189 C CE  . MET B 198 ? 0.2696 0.2701 0.2645 0.0334  0.0041  -0.0082 186 MET B CE  
3190 N N   . ILE B 199 ? 0.2365 0.1955 0.2210 0.0223  -0.0087 -0.0178 187 ILE B N   
3191 C CA  A ILE B 199 ? 0.2527 0.2159 0.2386 0.0165  -0.0091 -0.0163 187 ILE B CA  
3192 C CA  B ILE B 199 ? 0.2527 0.2159 0.2385 0.0166  -0.0092 -0.0165 187 ILE B CA  
3193 C C   . ILE B 199 ? 0.2501 0.2268 0.2368 0.0179  -0.0052 -0.0153 187 ILE B C   
3194 O O   . ILE B 199 ? 0.2827 0.2641 0.2656 0.0224  -0.0042 -0.0186 187 ILE B O   
3195 C CB  A ILE B 199 ? 0.2795 0.2346 0.2618 0.0144  -0.0145 -0.0209 187 ILE B CB  
3196 C CB  B ILE B 199 ? 0.2600 0.2172 0.2411 0.0157  -0.0140 -0.0220 187 ILE B CB  
3197 C CG1 A ILE B 199 ? 0.3018 0.2641 0.2876 0.0082  -0.0156 -0.0180 187 ILE B CG1 
3198 C CG1 B ILE B 199 ? 0.2461 0.1868 0.2256 0.0144  -0.0195 -0.0246 187 ILE B CG1 
3199 C CG2 A ILE B 199 ? 0.3045 0.2577 0.2790 0.0209  -0.0151 -0.0288 187 ILE B CG2 
3200 C CG2 B ILE B 199 ? 0.2839 0.2487 0.2683 0.0094  -0.0150 -0.0190 187 ILE B CG2 
3201 C CD1 A ILE B 199 ? 0.4014 0.3539 0.3849 0.0037  -0.0225 -0.0210 187 ILE B CD1 
3202 C CD1 B ILE B 199 ? 0.2801 0.2139 0.2529 0.0140  -0.0246 -0.0321 187 ILE B CD1 
3203 N N   . LEU B 200 ? 0.2290 0.2119 0.2209 0.0140  -0.0029 -0.0105 188 LEU B N   
3204 C CA  . LEU B 200 ? 0.2227 0.2164 0.2169 0.0150  0.0003  -0.0085 188 LEU B CA  
3205 C C   . LEU B 200 ? 0.2065 0.2050 0.1994 0.0140  -0.0020 -0.0095 188 LEU B C   
3206 O O   . LEU B 200 ? 0.2279 0.2245 0.2229 0.0100  -0.0049 -0.0088 188 LEU B O   
3207 C CB  . LEU B 200 ? 0.2452 0.2420 0.2454 0.0122  0.0033  -0.0041 188 LEU B CB  
3208 C CG  . LEU B 200 ? 0.2245 0.2174 0.2237 0.0123  0.0051  -0.0032 188 LEU B CG  
3209 C CD1 . LEU B 200 ? 0.2479 0.2435 0.2509 0.0099  0.0085  -0.0006 188 LEU B CD1 
3210 C CD2 . LEU B 200 ? 0.2758 0.2713 0.2730 0.0160  0.0058  -0.0039 188 LEU B CD2 
3211 N N   . PRO B 201 ? 0.2146 0.2201 0.2039 0.0171  -0.0012 -0.0105 189 PRO B N   
3212 C CA  . PRO B 201 ? 0.2218 0.2332 0.2086 0.0155  -0.0038 -0.0105 189 PRO B CA  
3213 C C   . PRO B 201 ? 0.2234 0.2406 0.2190 0.0116  -0.0040 -0.0043 189 PRO B C   
3214 O O   . PRO B 201 ? 0.2161 0.2350 0.2190 0.0115  -0.0007 -0.0004 189 PRO B O   
3215 C CB  . PRO B 201 ? 0.2616 0.2820 0.2436 0.0196  -0.0014 -0.0107 189 PRO B CB  
3216 C CG  . PRO B 201 ? 0.2611 0.2778 0.2418 0.0243  0.0014  -0.0136 189 PRO B CG  
3217 C CD  . PRO B 201 ? 0.2305 0.2402 0.2178 0.0219  0.0018  -0.0112 189 PRO B CD  
3218 N N   . LEU B 202 ? 0.2298 0.2500 0.2250 0.0085  -0.0084 -0.0038 190 LEU B N   
3219 C CA  . LEU B 202 ? 0.2174 0.2456 0.2222 0.0058  -0.0090 0.0029  190 LEU B CA  
3220 C C   . LEU B 202 ? 0.2165 0.2526 0.2243 0.0083  -0.0058 0.0076  190 LEU B C   
3221 O O   . LEU B 202 ? 0.2432 0.2839 0.2436 0.0102  -0.0058 0.0069  190 LEU B O   
3222 C CB  . LEU B 202 ? 0.2331 0.2648 0.2349 0.0021  -0.0155 0.0028  190 LEU B CB  
3223 C CG  . LEU B 202 ? 0.2415 0.2646 0.2424 -0.0020 -0.0199 -0.0009 190 LEU B CG  
3224 C CD1 . LEU B 202 ? 0.2829 0.3073 0.2759 -0.0055 -0.0275 -0.0035 190 LEU B CD1 
3225 C CD2 . LEU B 202 ? 0.2466 0.2721 0.2618 -0.0051 -0.0186 0.0049  190 LEU B CD2 
3226 N N   . THR B 203 ? 0.2004 0.2387 0.2196 0.0082  -0.0034 0.0128  191 THR B N   
3227 C CA  . THR B 203 ? 0.1927 0.2352 0.2172 0.0100  -0.0008 0.0177  191 THR B CA  
3228 C C   . THR B 203 ? 0.1914 0.2306 0.2113 0.0121  0.0025  0.0155  191 THR B C   
3229 O O   . THR B 203 ? 0.2166 0.2594 0.2395 0.0126  0.0036  0.0196  191 THR B O   
3230 C CB  . THR B 203 ? 0.1905 0.2428 0.2161 0.0092  -0.0040 0.0239  191 THR B CB  
3231 O OG1 . THR B 203 ? 0.2165 0.2733 0.2298 0.0094  -0.0055 0.0218  191 THR B OG1 
3232 C CG2 . THR B 203 ? 0.1997 0.2567 0.2326 0.0068  -0.0081 0.0277  191 THR B CG2 
3233 N N   . SER B 204 ? 0.2046 0.2370 0.2188 0.0129  0.0037  0.0098  192 SER B N   
3234 C CA  . SER B 204 ? 0.1846 0.2157 0.1965 0.0148  0.0063  0.0088  192 SER B CA  
3235 C C   . SER B 204 ? 0.1844 0.2116 0.2031 0.0141  0.0087  0.0109  192 SER B C   
3236 O O   . SER B 204 ? 0.1994 0.2228 0.2228 0.0133  0.0097  0.0107  192 SER B O   
3237 C CB  . SER B 204 ? 0.2178 0.2429 0.2228 0.0164  0.0063  0.0032  192 SER B CB  
3238 O OG  . SER B 204 ? 0.2150 0.2324 0.2217 0.0147  0.0063  0.0016  192 SER B OG  
3239 N N   . VAL B 205 ? 0.1878 0.2164 0.2068 0.0144  0.0097  0.0123  193 VAL B N   
3240 C CA  . VAL B 205 ? 0.2039 0.2273 0.2273 0.0133  0.0110  0.0131  193 VAL B CA  
3241 C C   . VAL B 205 ? 0.1880 0.2078 0.2063 0.0133  0.0113  0.0098  193 VAL B C   
3242 O O   . VAL B 205 ? 0.1913 0.2164 0.2070 0.0145  0.0108  0.0101  193 VAL B O   
3243 C CB  . VAL B 205 ? 0.1976 0.2255 0.2264 0.0121  0.0101  0.0189  193 VAL B CB  
3244 C CG1 . VAL B 205 ? 0.2507 0.2711 0.2830 0.0103  0.0103  0.0188  193 VAL B CG1 
3245 C CG2 . VAL B 205 ? 0.2054 0.2371 0.2401 0.0121  0.0090  0.0237  193 VAL B CG2 
3246 N N   . SER B 206 ? 0.1797 0.1919 0.1971 0.0124  0.0124  0.0070  194 SER B N   
3247 C CA  . SER B 206 ? 0.1982 0.2070 0.2110 0.0115  0.0119  0.0050  194 SER B CA  
3248 C C   . SER B 206 ? 0.2146 0.2175 0.2287 0.0092  0.0122  0.0044  194 SER B C   
3249 O O   . SER B 206 ? 0.2581 0.2570 0.2753 0.0095  0.0140  0.0035  194 SER B O   
3250 C CB  . SER B 206 ? 0.2096 0.2139 0.2171 0.0118  0.0124  0.0020  194 SER B CB  
3251 O OG  . SER B 206 ? 0.2016 0.2083 0.2079 0.0136  0.0115  0.0017  194 SER B OG  
3252 N N   . VAL B 207 ? 0.2163 0.2184 0.2288 0.0071  0.0101  0.0046  195 VAL B N   
3253 C CA  . VAL B 207 ? 0.2004 0.1954 0.2134 0.0041  0.0091  0.0033  195 VAL B CA  
3254 C C   . VAL B 207 ? 0.2192 0.2089 0.2236 0.0021  0.0081  -0.0005 195 VAL B C   
3255 O O   . VAL B 207 ? 0.2205 0.2146 0.2224 0.0013  0.0056  0.0010  195 VAL B O   
3256 C CB  . VAL B 207 ? 0.2239 0.2229 0.2433 0.0013  0.0059  0.0081  195 VAL B CB  
3257 C CG1 . VAL B 207 ? 0.2180 0.2065 0.2370 -0.0026 0.0034  0.0058  195 VAL B CG1 
3258 C CG2 . VAL B 207 ? 0.2214 0.2263 0.2485 0.0028  0.0067  0.0131  195 VAL B CG2 
3259 N N   . LEU B 208 ? 0.2138 0.1945 0.2136 0.0015  0.0100  -0.0054 196 LEU B N   
3260 C CA  . LEU B 208 ? 0.2075 0.1824 0.1973 -0.0015 0.0085  -0.0094 196 LEU B CA  
3261 C C   . LEU B 208 ? 0.2178 0.1847 0.2077 -0.0050 0.0054  -0.0118 196 LEU B C   
3262 O O   . LEU B 208 ? 0.2288 0.1898 0.2246 -0.0037 0.0068  -0.0129 196 LEU B O   
3263 C CB  . LEU B 208 ? 0.2241 0.1944 0.2060 0.0002  0.0134  -0.0143 196 LEU B CB  
3264 C CG  . LEU B 208 ? 0.2116 0.1882 0.1952 0.0030  0.0167  -0.0118 196 LEU B CG  
3265 C CD1 . LEU B 208 ? 0.2643 0.2384 0.2413 0.0038  0.0220  -0.0156 196 LEU B CD1 
3266 C CD2 . LEU B 208 ? 0.2324 0.2139 0.2134 0.0019  0.0133  -0.0082 196 LEU B CD2 
3267 N N   . ALA B 209 ? 0.2249 0.1905 0.2087 -0.0096 0.0005  -0.0124 197 ALA B N   
3268 C CA  . ALA B 209 ? 0.2390 0.1945 0.2201 -0.0143 -0.0037 -0.0160 197 ALA B CA  
3269 C C   . ALA B 209 ? 0.2634 0.2099 0.2290 -0.0151 -0.0023 -0.0243 197 ALA B C   
3270 O O   . ALA B 209 ? 0.2652 0.2166 0.2220 -0.0154 -0.0019 -0.0240 197 ALA B O   
3271 C CB  . ALA B 209 ? 0.2698 0.2316 0.2546 -0.0200 -0.0112 -0.0106 197 ALA B CB  
3272 N N   . VAL B 210 ? 0.2693 0.2025 0.2311 -0.0151 -0.0011 -0.0318 198 VAL B N   
3273 C CA  . VAL B 210 ? 0.2866 0.2119 0.2329 -0.0139 0.0028  -0.0410 198 VAL B CA  
3274 C C   . VAL B 210 ? 0.3075 0.2181 0.2451 -0.0189 -0.0026 -0.0487 198 VAL B C   
3275 O O   . VAL B 210 ? 0.3345 0.2353 0.2807 -0.0197 -0.0053 -0.0497 198 VAL B O   
3276 C CB  . VAL B 210 ? 0.3176 0.2412 0.2673 -0.0063 0.0120  -0.0445 198 VAL B CB  
3277 C CG1 . VAL B 210 ? 0.3748 0.2923 0.3078 -0.0045 0.0175  -0.0543 198 VAL B CG1 
3278 C CG2 . VAL B 210 ? 0.3230 0.2600 0.2818 -0.0026 0.0160  -0.0370 198 VAL B CG2 
3279 N N   . LYS B 211 ? 0.3226 0.2304 0.2425 -0.0226 -0.0047 -0.0540 199 LYS B N   
3280 C CA  . LYS B 211 ? 0.3712 0.2633 0.2792 -0.0277 -0.0101 -0.0635 199 LYS B CA  
3281 C C   . LYS B 211 ? 0.4204 0.3109 0.3056 -0.0281 -0.0074 -0.0714 199 LYS B C   
3282 O O   . LYS B 211 ? 0.4275 0.3295 0.3057 -0.0312 -0.0096 -0.0660 199 LYS B O   
3283 C CB  . LYS B 211 ? 0.4067 0.2995 0.3189 -0.0370 -0.0221 -0.0581 199 LYS B CB  
3284 C CG  . LYS B 211 ? 0.4965 0.3721 0.3955 -0.0442 -0.0298 -0.0679 199 LYS B CG  
3285 C CD  . LYS B 211 ? 0.5168 0.3961 0.4233 -0.0542 -0.0422 -0.0604 199 LYS B CD  
3286 C CE  . LYS B 211 ? 0.5667 0.4284 0.4587 -0.0630 -0.0516 -0.0703 199 LYS B CE  
3287 N NZ  . LYS B 211 ? 0.6443 0.4838 0.5351 -0.0597 -0.0488 -0.0813 199 LYS B NZ  
3288 N N   . ASP B 212 ? 0.4242 0.3008 0.2980 -0.0248 -0.0025 -0.0839 200 ASP B N   
3289 C CA  . ASP B 212 ? 0.4884 0.3630 0.3378 -0.0252 0.0009  -0.0929 200 ASP B CA  
3290 C C   . ASP B 212 ? 0.5315 0.4242 0.3781 -0.0226 0.0073  -0.0853 200 ASP B C   
3291 O O   . ASP B 212 ? 0.5675 0.4674 0.4002 -0.0279 0.0035  -0.0824 200 ASP B O   
3292 C CB  . ASP B 212 ? 0.5578 0.4258 0.3910 -0.0354 -0.0106 -0.0965 200 ASP B CB  
3293 C CG  . ASP B 212 ? 0.6610 0.5097 0.4974 -0.0395 -0.0185 -0.1035 200 ASP B CG  
3294 O OD1 . ASP B 212 ? 0.6766 0.5117 0.5174 -0.0332 -0.0128 -0.1116 200 ASP B OD1 
3295 O OD2 . ASP B 212 ? 0.7047 0.5522 0.5410 -0.0493 -0.0306 -0.1000 200 ASP B OD2 
3296 N N   . GLU B 213 ? 0.4638 0.3639 0.3248 -0.0151 0.0160  -0.0811 201 GLU B N   
3297 C CA  . GLU B 213 ? 0.5703 0.4860 0.4299 -0.0127 0.0226  -0.0743 201 GLU B CA  
3298 C C   . GLU B 213 ? 0.5007 0.4287 0.3686 -0.0167 0.0165  -0.0612 201 GLU B C   
3299 O O   . GLU B 213 ? 0.4810 0.4203 0.3520 -0.0146 0.0210  -0.0543 201 GLU B O   
3300 C CB  . GLU B 213 ? 0.6915 0.6087 0.5270 -0.0135 0.0274  -0.0807 201 GLU B CB  
3301 C CG  . GLU B 213 ? 0.7890 0.6955 0.6137 -0.0079 0.0356  -0.0950 201 GLU B CG  
3302 C CD  . GLU B 213 ? 0.8965 0.8108 0.7327 0.0014  0.0484  -0.0945 201 GLU B CD  
3303 O OE1 . GLU B 213 ? 0.8370 0.7661 0.6842 0.0019  0.0509  -0.0832 201 GLU B OE1 
3304 O OE2 . GLU B 213 ? 0.9573 0.8629 0.7921 0.0082  0.0556  -0.1053 201 GLU B OE2 
3305 N N   . ARG B 214 ? 0.4052 0.3314 0.2771 -0.0223 0.0063  -0.0576 202 ARG B N   
3306 C CA  . ARG B 214 ? 0.4123 0.3502 0.2942 -0.0244 0.0011  -0.0459 202 ARG B CA  
3307 C C   . ARG B 214 ? 0.3601 0.3014 0.2634 -0.0199 0.0030  -0.0405 202 ARG B C   
3308 O O   . ARG B 214 ? 0.3590 0.2929 0.2707 -0.0187 0.0030  -0.0438 202 ARG B O   
3309 C CB  . ARG B 214 ? 0.4609 0.3977 0.3401 -0.0318 -0.0103 -0.0438 202 ARG B CB  
3310 C CG  . ARG B 214 ? 0.5705 0.5195 0.4616 -0.0329 -0.0156 -0.0322 202 ARG B CG  
3311 C CD  . ARG B 214 ? 0.7788 0.7311 0.6597 -0.0400 -0.0252 -0.0291 202 ARG B CD  
3312 N NE  . ARG B 214 ? 0.7943 0.7586 0.6897 -0.0398 -0.0302 -0.0180 202 ARG B NE  
3313 C CZ  . ARG B 214 ? 0.7129 0.6812 0.6208 -0.0426 -0.0371 -0.0138 202 ARG B CZ  
3314 N NH1 . ARG B 214 ? 0.6118 0.5723 0.5197 -0.0474 -0.0412 -0.0189 202 ARG B NH1 
3315 N NH2 . ARG B 214 ? 0.7069 0.6875 0.6284 -0.0406 -0.0399 -0.0041 202 ARG B NH2 
3316 N N   A MET B 215 ? 0.3210 0.2727 0.2324 -0.0176 0.0046  -0.0324 203 MET B N   
3317 N N   B MET B 215 ? 0.3206 0.2726 0.2324 -0.0179 0.0037  -0.0319 203 MET B N   
3318 C CA  A MET B 215 ? 0.3011 0.2573 0.2301 -0.0136 0.0061  -0.0274 203 MET B CA  
3319 C CA  B MET B 215 ? 0.3039 0.2604 0.2331 -0.0133 0.0065  -0.0273 203 MET B CA  
3320 C C   A MET B 215 ? 0.2926 0.2574 0.2282 -0.0152 0.0001  -0.0191 203 MET B C   
3321 C C   B MET B 215 ? 0.2967 0.2622 0.2346 -0.0139 0.0016  -0.0186 203 MET B C   
3322 O O   A MET B 215 ? 0.3134 0.2828 0.2431 -0.0162 -0.0014 -0.0152 203 MET B O   
3323 O O   B MET B 215 ? 0.2470 0.2179 0.1830 -0.0130 0.0022  -0.0143 203 MET B O   
3324 C CB  A MET B 215 ? 0.3238 0.2841 0.2571 -0.0085 0.0141  -0.0264 203 MET B CB  
3325 C CB  B MET B 215 ? 0.3238 0.2831 0.2544 -0.0085 0.0151  -0.0278 203 MET B CB  
3326 C CG  A MET B 215 ? 0.3535 0.3081 0.2842 -0.0051 0.0213  -0.0337 203 MET B CG  
3327 C CG  B MET B 215 ? 0.3726 0.3270 0.2914 -0.0072 0.0215  -0.0355 203 MET B CG  
3328 S SD  A MET B 215 ? 0.3641 0.3282 0.3023 -0.0006 0.0291  -0.0293 203 MET B SD  
3329 S SD  B MET B 215 ? 0.4345 0.3955 0.3634 -0.0011 0.0311  -0.0337 203 MET B SD  
3330 C CE  A MET B 215 ? 0.4665 0.4255 0.4014 0.0041  0.0380  -0.0383 203 MET B CE  
3331 C CE  B MET B 215 ? 0.2579 0.2145 0.2037 0.0022  0.0298  -0.0342 203 MET B CE  
3332 N N   . VAL B 216 ? 0.2548 0.2222 0.2031 -0.0149 -0.0029 -0.0159 204 VAL B N   
3333 C CA  . VAL B 216 ? 0.2501 0.2269 0.2069 -0.0149 -0.0075 -0.0085 204 VAL B CA  
3334 C C   . VAL B 216 ? 0.2404 0.2223 0.2094 -0.0098 -0.0037 -0.0055 204 VAL B C   
3335 O O   . VAL B 216 ? 0.2407 0.2202 0.2160 -0.0086 -0.0013 -0.0070 204 VAL B O   
3336 C CB  . VAL B 216 ? 0.2919 0.2698 0.2527 -0.0199 -0.0145 -0.0069 204 VAL B CB  
3337 C CG1 . VAL B 216 ? 0.3273 0.3179 0.3005 -0.0185 -0.0176 0.0010  204 VAL B CG1 
3338 C CG2 . VAL B 216 ? 0.3322 0.3062 0.2798 -0.0258 -0.0200 -0.0094 204 VAL B CG2 
3339 N N   . VAL B 217 ? 0.2294 0.2177 0.2018 -0.0067 -0.0037 -0.0012 205 VAL B N   
3340 C CA  . VAL B 217 ? 0.2227 0.2155 0.2046 -0.0021 -0.0008 0.0007  205 VAL B CA  
3341 C C   . VAL B 217 ? 0.2300 0.2307 0.2214 -0.0021 -0.0037 0.0045  205 VAL B C   
3342 O O   . VAL B 217 ? 0.2487 0.2562 0.2429 -0.0019 -0.0073 0.0082  205 VAL B O   
3343 C CB  . VAL B 217 ? 0.2191 0.2136 0.2005 0.0013  -0.0001 0.0028  205 VAL B CB  
3344 C CG1 . VAL B 217 ? 0.2470 0.2452 0.2360 0.0056  0.0022  0.0033  205 VAL B CG1 
3345 C CG2 . VAL B 217 ? 0.2502 0.2387 0.2232 0.0001  0.0028  0.0007  205 VAL B CG2 
3346 N N   . ARG B 218 ? 0.2185 0.2201 0.2162 -0.0019 -0.0019 0.0046  206 ARG B N   
3347 C CA  . ARG B 218 ? 0.2198 0.2308 0.2269 -0.0027 -0.0041 0.0095  206 ARG B CA  
3348 C C   . ARG B 218 ? 0.2124 0.2326 0.2254 0.0024  -0.0011 0.0121  206 ARG B C   
3349 O O   . ARG B 218 ? 0.2179 0.2492 0.2371 0.0038  -0.0021 0.0163  206 ARG B O   
3350 C CB  . ARG B 218 ? 0.2742 0.2809 0.2849 -0.0070 -0.0054 0.0097  206 ARG B CB  
3351 C CG  . ARG B 218 ? 0.3064 0.3247 0.3275 -0.0097 -0.0085 0.0167  206 ARG B CG  
3352 C CD  . ARG B 218 ? 0.2866 0.2990 0.3111 -0.0161 -0.0124 0.0178  206 ARG B CD  
3353 N NE  . ARG B 218 ? 0.2819 0.2857 0.2990 -0.0210 -0.0171 0.0139  206 ARG B NE  
3354 C CZ  . ARG B 218 ? 0.3466 0.3381 0.3613 -0.0266 -0.0208 0.0106  206 ARG B CZ  
3355 N NH1 . ARG B 218 ? 0.3831 0.3682 0.4039 -0.0278 -0.0203 0.0114  206 ARG B NH1 
3356 N NH2 . ARG B 218 ? 0.3545 0.3391 0.3598 -0.0310 -0.0254 0.0062  206 ARG B NH2 
3357 N N   . SER B 219 ? 0.2040 0.2207 0.2151 0.0054  0.0025  0.0097  207 SER B N   
3358 C CA  . SER B 219 ? 0.2067 0.2311 0.2208 0.0099  0.0047  0.0110  207 SER B CA  
3359 C C   . SER B 219 ? 0.1967 0.2148 0.2061 0.0123  0.0069  0.0072  207 SER B C   
3360 O O   . SER B 219 ? 0.2093 0.2194 0.2158 0.0104  0.0077  0.0049  207 SER B O   
3361 C CB  . SER B 219 ? 0.1914 0.2237 0.2119 0.0091  0.0055  0.0152  207 SER B CB  
3362 O OG  . SER B 219 ? 0.2269 0.2519 0.2480 0.0068  0.0061  0.0146  207 SER B OG  
3363 N N   . ILE B 220 ? 0.1978 0.2196 0.2065 0.0165  0.0077  0.0064  208 ILE B N   
3364 C CA  . ILE B 220 ? 0.1981 0.2133 0.2025 0.0180  0.0083  0.0031  208 ILE B CA  
3365 C C   . ILE B 220 ? 0.2039 0.2235 0.2080 0.0209  0.0091  0.0021  208 ILE B C   
3366 O O   . ILE B 220 ? 0.2106 0.2365 0.2146 0.0247  0.0095  0.0017  208 ILE B O   
3367 C CB  . ILE B 220 ? 0.2159 0.2263 0.2172 0.0198  0.0066  0.0018  208 ILE B CB  
3368 C CG1 . ILE B 220 ? 0.2125 0.2197 0.2121 0.0166  0.0050  0.0033  208 ILE B CG1 
3369 C CG2 . ILE B 220 ? 0.2113 0.2137 0.2091 0.0197  0.0064  -0.0007 208 ILE B CG2 
3370 C CD1 . ILE B 220 ? 0.2436 0.2476 0.2413 0.0183  0.0024  0.0041  208 ILE B CD1 
3371 N N   . GLY B 221 ? 0.1935 0.2105 0.1972 0.0193  0.0095  0.0014  209 GLY B N   
3372 C CA  . GLY B 221 ? 0.2100 0.2283 0.2106 0.0214  0.0088  -0.0009 209 GLY B CA  
3373 C C   . GLY B 221 ? 0.1952 0.2235 0.1956 0.0228  0.0095  0.0007  209 GLY B C   
3374 O O   . GLY B 221 ? 0.2228 0.2524 0.2178 0.0251  0.0088  -0.0025 209 GLY B O   
3375 N N   . ASP B 222 ? 0.2056 0.2408 0.2109 0.0211  0.0105  0.0058  210 ASP B N   
3376 C CA  . ASP B 222 ? 0.2040 0.2509 0.2091 0.0219  0.0114  0.0092  210 ASP B CA  
3377 C C   . ASP B 222 ? 0.2035 0.2521 0.2077 0.0201  0.0099  0.0108  210 ASP B C   
3378 O O   . ASP B 222 ? 0.2051 0.2514 0.2155 0.0172  0.0091  0.0146  210 ASP B O   
3379 C CB  . ASP B 222 ? 0.1992 0.2523 0.2114 0.0196  0.0121  0.0154  210 ASP B CB  
3380 C CG  . ASP B 222 ? 0.2396 0.3069 0.2524 0.0198  0.0133  0.0209  210 ASP B CG  
3381 O OD1 . ASP B 222 ? 0.2157 0.2862 0.2275 0.0185  0.0125  0.0238  210 ASP B OD1 
3382 O OD2 . ASP B 222 ? 0.2148 0.2915 0.2297 0.0211  0.0151  0.0232  210 ASP B OD2 
3383 N N   . ALA B 223 ? 0.2103 0.2635 0.2071 0.0221  0.0093  0.0083  211 ALA B N   
3384 C CA  . ALA B 223 ? 0.2312 0.2891 0.2262 0.0199  0.0071  0.0111  211 ALA B CA  
3385 C C   . ALA B 223 ? 0.2336 0.3051 0.2228 0.0213  0.0084  0.0139  211 ALA B C   
3386 O O   . ALA B 223 ? 0.2639 0.3399 0.2449 0.0213  0.0065  0.0124  211 ALA B O   
3387 C CB  . ALA B 223 ? 0.2584 0.3089 0.2483 0.0193  0.0037  0.0054  211 ALA B CB  
3388 N N   . THR B 224 ? 0.2281 0.3078 0.2217 0.0219  0.0114  0.0185  212 THR B N   
3389 C CA  . THR B 224 ? 0.2354 0.3309 0.2242 0.0232  0.0139  0.0224  212 THR B CA  
3390 C C   . THR B 224 ? 0.2428 0.3469 0.2322 0.0192  0.0117  0.0311  212 THR B C   
3391 O O   . THR B 224 ? 0.2549 0.3731 0.2370 0.0199  0.0134  0.0342  212 THR B O   
3392 C CB  . THR B 224 ? 0.2635 0.3667 0.2596 0.0239  0.0173  0.0269  212 THR B CB  
3393 O OG1 . THR B 224 ? 0.2240 0.3224 0.2317 0.0189  0.0153  0.0337  212 THR B OG1 
3394 C CG2 . THR B 224 ? 0.2970 0.3949 0.2918 0.0290  0.0194  0.0188  212 THR B CG2 
3395 N N   . HIS B 225 ? 0.2226 0.3191 0.2198 0.0156  0.0081  0.0350  213 HIS B N   
3396 C CA  . HIS B 225 ? 0.2440 0.3479 0.2422 0.0123  0.0049  0.0435  213 HIS B CA  
3397 C C   . HIS B 225 ? 0.2421 0.3498 0.2276 0.0127  0.0022  0.0392  213 HIS B C   
3398 O O   . HIS B 225 ? 0.2828 0.3995 0.2666 0.0100  -0.0008 0.0466  213 HIS B O   
3399 C CB  . HIS B 225 ? 0.2510 0.3456 0.2624 0.0096  0.0018  0.0484  213 HIS B CB  
3400 C CG  . HIS B 225 ? 0.2300 0.3117 0.2428 0.0108  0.0010  0.0402  213 HIS B CG  
3401 N ND1 . HIS B 225 ? 0.2278 0.2997 0.2427 0.0124  0.0037  0.0342  213 HIS B ND1 
3402 C CD2 . HIS B 225 ? 0.2425 0.3210 0.2544 0.0103  -0.0022 0.0376  213 HIS B CD2 
3403 C CE1 . HIS B 225 ? 0.2235 0.2867 0.2386 0.0127  0.0026  0.0287  213 HIS B CE1 
3404 N NE2 . HIS B 225 ? 0.2601 0.3273 0.2742 0.0114  -0.0009 0.0306  213 HIS B NE2 
3405 N N   . LEU B 226 ? 0.2414 0.3412 0.2181 0.0156  0.0023  0.0278  214 LEU B N   
3406 C CA  . LEU B 226 ? 0.2838 0.3856 0.2467 0.0155  -0.0010 0.0223  214 LEU B CA  
3407 C C   . LEU B 226 ? 0.2807 0.3925 0.2285 0.0194  0.0026  0.0177  214 LEU B C   
3408 O O   . LEU B 226 ? 0.3079 0.4225 0.2417 0.0191  -0.0002 0.0130  214 LEU B O   
3409 C CB  . LEU B 226 ? 0.2734 0.3601 0.2347 0.0158  -0.0039 0.0126  214 LEU B CB  
3410 C CG  . LEU B 226 ? 0.2716 0.3498 0.2475 0.0127  -0.0063 0.0164  214 LEU B CG  
3411 C CD1 . LEU B 226 ? 0.3032 0.3677 0.2777 0.0126  -0.0084 0.0075  214 LEU B CD1 
3412 C CD2 . LEU B 226 ? 0.3050 0.3904 0.2865 0.0086  -0.0111 0.0252  214 LEU B CD2 
3413 N N   . ALA B 227 ? 0.2616 0.3801 0.2121 0.0228  0.0088  0.0191  215 ALA B N   
3414 C CA  . ALA B 227 ? 0.3098 0.4381 0.2466 0.0282  0.0136  0.0130  215 ALA B CA  
3415 C C   . ALA B 227 ? 0.2985 0.4432 0.2226 0.0265  0.0133  0.0175  215 ALA B C   
3416 O O   . ALA B 227 ? 0.3432 0.4925 0.2503 0.0307  0.0154  0.0088  215 ALA B O   
3417 C CB  . ALA B 227 ? 0.3211 0.4574 0.2665 0.0317  0.0202  0.0163  215 ALA B CB  
3418 N N   . ALA B 228 ? 0.2924 0.4461 0.2235 0.0207  0.0108  0.0309  216 ALA B N   
3419 C CA  . ALA B 228 ? 0.3413 0.5124 0.2609 0.0182  0.0102  0.0379  216 ALA B CA  
3420 C C   . ALA B 228 ? 0.3248 0.4919 0.2367 0.0138  0.0018  0.0375  216 ALA B C   
3421 O O   . ALA B 228 ? 0.3699 0.5513 0.2709 0.0109  -0.0002 0.0437  216 ALA B O   
3422 C CB  . ALA B 228 ? 0.3296 0.5138 0.2619 0.0137  0.0112  0.0552  216 ALA B CB  
3423 N N   . ALA B 229 ? 0.3131 0.4626 0.2309 0.0129  -0.0032 0.0311  217 ALA B N   
3424 C CA  . ALA B 229 ? 0.3373 0.4835 0.2522 0.0079  -0.0119 0.0321  217 ALA B CA  
3425 C C   . ALA B 229 ? 0.3398 0.4865 0.2315 0.0087  -0.0146 0.0205  217 ALA B C   
3426 O O   . ALA B 229 ? 0.3486 0.4921 0.2289 0.0144  -0.0095 0.0087  217 ALA B O   
3427 C CB  . ALA B 229 ? 0.3419 0.4706 0.2708 0.0071  -0.0151 0.0282  217 ALA B CB  
3428 N N   . PRO B 230 ? 0.3629 0.5125 0.2479 0.0032  -0.0232 0.0229  218 PRO B N   
3429 C CA  . PRO B 230 ? 0.3798 0.5254 0.2425 0.0029  -0.0276 0.0098  218 PRO B CA  
3430 C C   . PRO B 230 ? 0.3454 0.4701 0.2090 0.0058  -0.0278 -0.0048 218 PRO B C   
3431 O O   . PRO B 230 ? 0.3893 0.5030 0.2713 0.0054  -0.0278 -0.0030 218 PRO B O   
3432 C CB  . PRO B 230 ? 0.3995 0.5499 0.2625 -0.0051 -0.0386 0.0176  218 PRO B CB  
3433 C CG  . PRO B 230 ? 0.3762 0.5408 0.2540 -0.0075 -0.0379 0.0362  218 PRO B CG  
3434 C CD  . PRO B 230 ? 0.3800 0.5375 0.2769 -0.0030 -0.0297 0.0381  218 PRO B CD  
3435 N N   . SER B 231 ? 0.4195 0.5382 0.2619 0.0089  -0.0280 -0.0195 219 SER B N   
3436 C CA  . SER B 231 ? 0.4274 0.5256 0.2700 0.0128  -0.0274 -0.0333 219 SER B CA  
3437 C C   . SER B 231 ? 0.4446 0.5280 0.2984 0.0062  -0.0365 -0.0336 219 SER B C   
3438 O O   . SER B 231 ? 0.5175 0.5848 0.3794 0.0083  -0.0355 -0.0397 219 SER B O   
3439 C CB  . SER B 231 ? 0.4899 0.5834 0.3072 0.0180  -0.0261 -0.0497 219 SER B CB  
3440 O OG  . SER B 231 ? 0.5082 0.6029 0.3078 0.0118  -0.0354 -0.0533 219 SER B OG  
3441 N N   . ASP B 232 ? 0.4177 0.5077 0.2732 -0.0018 -0.0452 -0.0259 220 ASP B N   
3442 C CA  . ASP B 232 ? 0.4245 0.5043 0.2928 -0.0085 -0.0537 -0.0244 220 ASP B CA  
3443 C C   . ASP B 232 ? 0.4412 0.5232 0.3362 -0.0092 -0.0508 -0.0120 220 ASP B C   
3444 O O   . ASP B 232 ? 0.4144 0.4914 0.3226 -0.0143 -0.0565 -0.0088 220 ASP B O   
3445 C CB  . ASP B 232 ? 0.4469 0.5333 0.3061 -0.0169 -0.0654 -0.0220 220 ASP B CB  
3446 C CG  . ASP B 232 ? 0.4404 0.5478 0.3051 -0.0197 -0.0666 -0.0061 220 ASP B CG  
3447 O OD1 . ASP B 232 ? 0.4066 0.5231 0.2795 -0.0152 -0.0583 0.0022  220 ASP B OD1 
3448 O OD2 . ASP B 232 ? 0.5040 0.6191 0.3655 -0.0270 -0.0768 -0.0010 220 ASP B OD2 
3449 N N   . VAL B 233 ? 0.3663 0.4556 0.2694 -0.0043 -0.0421 -0.0053 221 VAL B N   
3450 C CA  . VAL B 233 ? 0.3263 0.4158 0.2526 -0.0042 -0.0390 0.0047  221 VAL B CA  
3451 C C   . VAL B 233 ? 0.3683 0.4457 0.2997 0.0011  -0.0318 -0.0017 221 VAL B C   
3452 O O   . VAL B 233 ? 0.3518 0.4232 0.2993 0.0007  -0.0302 0.0017  221 VAL B O   
3453 C CB  . VAL B 233 ? 0.3371 0.4420 0.2700 -0.0038 -0.0361 0.0178  221 VAL B CB  
3454 C CG1 . VAL B 233 ? 0.3599 0.4618 0.3148 -0.0022 -0.0315 0.0253  221 VAL B CG1 
3455 C CG2 . VAL B 233 ? 0.3755 0.4923 0.3073 -0.0095 -0.0444 0.0266  221 VAL B CG2 
3456 N N   . ILE B 234 ? 0.3811 0.4557 0.2987 0.0063  -0.0273 -0.0108 222 ILE B N   
3457 C CA  . ILE B 234 ? 0.4241 0.4898 0.3466 0.0120  -0.0205 -0.0155 222 ILE B CA  
3458 C C   . ILE B 234 ? 0.4398 0.4882 0.3676 0.0103  -0.0238 -0.0215 222 ILE B C   
3459 O O   . ILE B 234 ? 0.4748 0.5148 0.3942 0.0073  -0.0302 -0.0285 222 ILE B O   
3460 C CB  . ILE B 234 ? 0.4336 0.5030 0.3415 0.0189  -0.0147 -0.0230 222 ILE B CB  
3461 C CG1 . ILE B 234 ? 0.5196 0.6089 0.4231 0.0189  -0.0118 -0.0145 222 ILE B CG1 
3462 C CG2 . ILE B 234 ? 0.4898 0.5528 0.4058 0.0247  -0.0082 -0.0254 222 ILE B CG2 
3463 C CD1 . ILE B 234 ? 0.4832 0.5818 0.3716 0.0255  -0.0053 -0.0204 222 ILE B CD1 
3464 O OXT . ILE B 234 ? 0.4986 0.5413 0.4392 0.0112  -0.0206 -0.0189 222 ILE B OXT 
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